data_4CQZ # _entry.id 4CQZ # _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 4CQZ PDBE EBI-59807 WWPDB D_1290059807 # 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 4CQU unspecified ;H5 (VN1194) ASN186LYS MUTANT HAEMAGGLUTININ IN COMPLEX WITH HUMAN RECEPTOR ANALOGUE 6'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 4CR0 unspecified 'CRYSTAL STRUCTURE OF H5 (VN1194) ASN186LYS/GLY143ARG MUTANT HAEMAGGLUTININ' # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 4CQZ _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 'Liu, J.' 1 'Xiong, X.' 2 'Xiao, H.' 3 'Martin, S.R.' 4 'Coombs, P.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 4CQZ _cell.length_a 101.149 _cell.length_b 101.149 _cell.length_c 447.887 _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 4CQZ _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' 36979.828 1 ? YES 'HA1 OF TRYPSIN RELEASED ECTODOMAIN, RESIDUES 17-340' ? 2 polymer nat 'HAEMAGGLUTININ HA2' 19097.990 1 ? ? 'HA2 OF TRYPSIN RELEASED ECTODOMAIN, RESIDUES 347-512' ? 3 non-polymer man 'O-SIALIC ACID' 309.270 1 ? ? ? ? 4 non-polymer man BETA-D-GALACTOSE 180.156 1 ? ? ? ? 5 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 6 ? ? ? ? 6 non-polymer syn '3[N-MORPHOLINO]PROPANE SULFONIC ACID' 209.263 1 ? ? ? ? 7 water nat water 18.015 87 ? ? ? ? # 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 KRSYNNTNQEDLLVLWGIHHPNDAAEQTKLYRNPTTYISVGTSTLNQRLVPRIATRSKVNGQSGRMEFFWTILKPNDAIN FESNGNFIAPEYAYKIVKKGDSTIMKSELEYGNCNTKCQTPMGAINSSMPFHNIHPLTIGECPKYVKSNRLVLATGLRNS PQRETR ; ;DQICIGYHANNSTEQVDTIMEKNVTVTHAQDILEKTHNGKLCDLDGVKPLILRDCSVAGWLLGNPMCDEFINVPEWSYIV EKANPVNDLCYPGDFNDYEELKHLLSRINHFEKIQIIPKSSWSSHEASLGVSSACPYQGKSSFFRNVVWLIKKNSTYPTI KRSYNNTNQEDLLVLWGIHHPNDAAEQTKLYRNPTTYISVGTSTLNQRLVPRIATRSKVNGQSGRMEFFWTILKPNDAIN 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 ASN 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 ARG 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 ? ? ? ? ? ? ? 'GLN196ARG MUTANT' ? ? ? ? ? ? ? ? ? 2 1 sample ? ? ? 'INFLUENZA A VIRUS (A/VIETNAM/1194/2004(H5N1))' 644788 ? ? ? ? ? ? ? 'GLN196ARG 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 4CQZ A 1 ? 324 ? Q6DQ34 17 ? 340 ? 1 324 2 2 4CQZ 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 4CQZ THR A 325 ? UNP Q6DQ34 ? ? 'expression tag' 325 1 1 4CQZ ARG A 326 ? UNP Q6DQ34 ? ? 'expression tag' 326 2 1 4CQZ ARG A 192 ? UNP Q6DQ34 GLN 208 'engineered mutation' 192 3 # loop_ _chem_comp.id _chem_comp.type _chem_comp.mon_nstd_flag _chem_comp.name _chem_comp.pdbx_synonyms _chem_comp.formula _chem_comp.formula_weight ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 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 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 4CQZ _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_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 1.54 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source 'ROTATING ANODE' _diffrn_source.type ? _diffrn_source.pdbx_synchrotron_site ? _diffrn_source.pdbx_synchrotron_beamline ? _diffrn_source.pdbx_wavelength 1.54 _diffrn_source.pdbx_wavelength_list ? # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 4CQZ _reflns.observed_criterion_sigma_I 1.9 _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 74.65 _reflns.d_resolution_high 2.70 _reflns.number_obs 24883 _reflns.number_all ? _reflns.percent_possible_obs 99.9 _reflns.pdbx_Rmerge_I_obs 0.08 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 11.70 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 5.2 # _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_ordinal 1 _reflns_shell.d_res_high 2.70 _reflns_shell.d_res_low 2.85 _reflns_shell.percent_possible_all 99.4 _reflns_shell.Rmerge_I_obs 0.43 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs 1.90 _reflns_shell.pdbx_redundancy 3.3 # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 4CQZ _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 23515 _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 149.30 _refine.ls_d_res_high 2.70 _refine.ls_percent_reflns_obs 99.44 _refine.ls_R_factor_obs 0.21899 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.21721 _refine.ls_R_factor_R_free 0.25225 _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 1261 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.940 _refine.correlation_coeff_Fo_to_Fc_free 0.926 _refine.B_iso_mean 74.888 _refine.aniso_B[1][1] 1.33 _refine.aniso_B[2][2] 1.33 _refine.aniso_B[3][3] -4.31 _refine.aniso_B[1][2] 0.66 _refine.aniso_B[1][3] 0.00 _refine.aniso_B[2][3] 0.00 _refine.solvent_model_details MASK _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.20 _refine.pdbx_solvent_ion_probe_radii 0.80 _refine.pdbx_solvent_shrinkage_radii 0.80 _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details 'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.' _refine.pdbx_starting_model '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 0.450 _refine.pdbx_overall_ESU_R_Free 0.289 _refine.overall_SU_ML 0.255 _refine.pdbx_overall_phase_error ? _refine.overall_SU_B 26.609 _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 3861 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 129 _refine_hist.number_atoms_solvent 87 _refine_hist.number_atoms_total 4077 _refine_hist.d_res_high 2.70 _refine_hist.d_res_low 149.30 # 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 ? 4096 'X-RAY DIFFRACTION' ? r_bond_other_d 0.001 0.020 ? 3760 'X-RAY DIFFRACTION' ? r_angle_refined_deg 0.982 1.974 ? 5563 'X-RAY DIFFRACTION' ? r_angle_other_deg 0.657 3.003 ? 8644 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 5.296 5.000 ? 483 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg 36.895 25.075 ? 201 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg 14.626 15.000 ? 679 'X-RAY DIFFRACTION' ? r_dihedral_angle_4_deg 11.425 15.000 ? 18 'X-RAY DIFFRACTION' ? r_chiral_restr 0.054 0.200 ? 610 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.003 0.020 ? 4609 'X-RAY DIFFRACTION' ? r_gen_planes_other 0.001 0.020 ? 947 '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 1.454 4.748 ? 1932 'X-RAY DIFFRACTION' ? r_mcbond_other 1.439 4.746 ? 1931 'X-RAY DIFFRACTION' ? r_mcangle_it 2.496 7.117 ? 2412 'X-RAY DIFFRACTION' ? r_mcangle_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scbond_it 1.822 5.273 ? 2164 '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 2.700 _refine_ls_shell.d_res_low 2.770 _refine_ls_shell.number_reflns_R_work 1723 _refine_ls_shell.R_factor_R_work 0.343 _refine_ls_shell.percent_reflns_obs 98.57 _refine_ls_shell.R_factor_R_free 0.359 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 68 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? # _struct.entry_id 4CQZ _struct.title 'Crystal Structure of H5 (VN1194) Gln196Arg Mutant Haemagglutinin' _struct.pdbx_descriptor 'HAEMAGGLUTININ HA1, HAEMAGGLUTININ HA2' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 4CQZ _struct_keywords.pdbx_keywords 'VIRAL PROTEIN' _struct_keywords.text ;VIRAL PROTEIN, HAEMAGGLUTININ MUTANT, 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 4 ? E N N 5 ? F N N 5 ? G N N 5 ? H N N 5 ? I N N 6 ? J N N 5 ? K N N 5 ? L N N 7 ? M N N 7 ? # _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 ? ARG A 192 ? ASP A 183 ARG 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 ? ? ? ? ? ? ? 2.063 ? disulf2 disulf ? ? A CYS 42 SG ? ? ? 1_555 A CYS 274 SG ? ? A CYS 42 A CYS 274 1_555 ? ? ? ? ? ? ? 2.044 ? disulf3 disulf ? ? A CYS 55 SG ? ? ? 1_555 A CYS 67 SG ? ? A CYS 55 A CYS 67 1_555 ? ? ? ? ? ? ? 2.048 ? disulf4 disulf ? ? A CYS 90 SG ? ? ? 1_555 A CYS 135 SG ? ? A CYS 90 A CYS 135 1_555 ? ? ? ? ? ? ? 2.051 ? disulf5 disulf ? ? A CYS 278 SG ? ? ? 1_555 A CYS 302 SG ? ? A CYS 278 A CYS 302 1_555 ? ? ? ? ? ? ? 2.051 ? disulf6 disulf ? ? B CYS 144 SG ? ? ? 1_555 B CYS 148 SG ? ? B CYS 144 B CYS 148 1_555 ? ? ? ? ? ? ? 2.039 ? covale1 covale ? ? A ASN 23 ND2 ? ? ? 1_555 H NAG . C1 ? ? A ASN 23 A NAG 1327 1_555 ? ? ? ? ? ? ? 1.452 ? covale2 covale ? ? A ASN 165 ND2 ? ? ? 1_555 F NAG . C1 ? ? A ASN 165 A NAG 1325 1_555 ? ? ? ? ? ? ? 1.436 ? covale3 covale ? ? C SIA . C2 ? ? ? 1_555 D GAL . O3 ? ? A SIA 1322 A GAL 1323 1_555 ? ? ? ? ? ? ? 1.439 ? covale4 covale ? ? D GAL . C1 ? ? ? 1_555 E NAG . O3 ? ? A GAL 1323 A NAG 1324 1_555 ? ? ? ? ? ? ? 1.432 ? covale5 covale ? ? F NAG . O3 ? ? ? 1_555 G NAG . C1 ? ? A NAG 1325 A NAG 1326 1_555 ? ? ? ? ? ? ? 1.448 ? covale6 covale ? ? B ASN 154 ND2 ? ? ? 1_555 J NAG . C1 ? ? B ASN 154 B NAG 1164 1_555 ? ? ? ? ? ? ? 1.441 ? covale7 covale ? ? J NAG . O4 ? ? ? 1_555 K NAG . C1 ? ? B NAG 1164 B NAG 1165 1_555 ? ? ? ? ? ? ? 1.444 ? # 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 ? ? ? ? 2 'Binding site for Mono-Saccharide NAG A1327 bound to ASN A 23' AC3 Software ? ? ? ? 2 'Binding site for Poly-Saccharide residues NAG A1325 through NAG A1326 bound to ASN A 165' AC4 Software ? ? ? ? 3 'Binding site for Poly-Saccharide residues NAG B1164 through NAG B1165 bound to ASN B 154' AC5 Software ? ? ? ? 10 'Binding site for Poly-Saccharide residues SIA A1322 through NAG A1324' # 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 2 ASN A 23 ? ASN A 23 . ? 1_555 ? 6 AC2 2 HOH L . ? HOH A 2055 . ? 1_555 ? 7 AC3 2 ASN A 165 ? ASN A 165 . ? 1_555 ? 8 AC3 2 ASN A 236 ? ASN A 236 . ? 1_555 ? 9 AC4 3 GLU B 147 ? GLU B 147 . ? 1_555 ? 10 AC4 3 GLU B 150 ? GLU B 150 . ? 1_555 ? 11 AC4 3 ASN B 154 ? ASN B 154 . ? 1_555 ? 12 AC5 10 TYR A 91 ? TYR A 91 . ? 1_555 ? 13 AC5 10 LEU A 129 ? LEU A 129 . ? 1_555 ? 14 AC5 10 VAL A 131 ? VAL A 131 . ? 1_555 ? 15 AC5 10 SER A 132 ? SER A 132 . ? 1_555 ? 16 AC5 10 SER A 133 ? SER A 133 . ? 1_555 ? 17 AC5 10 HIS A 179 ? HIS A 179 . ? 1_555 ? 18 AC5 10 GLU A 186 ? GLU A 186 . ? 1_555 ? 19 AC5 10 LEU A 190 ? LEU A 190 . ? 1_555 ? 20 AC5 10 GLN A 222 ? GLN A 222 . ? 1_555 ? 21 AC5 10 HOH L . ? HOH A 2041 . ? 1_555 ? # _database_PDB_matrix.entry_id 4CQZ _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 4CQZ _atom_sites.fract_transf_matrix[1][1] 0.009886 _atom_sites.fract_transf_matrix[1][2] 0.005708 _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] 0.011416 _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] 0.002233 _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 ? -31.520 33.853 -8.480 1.00 66.20 ? 1 ASP A N 1 ATOM 2 C CA . ASP A 1 1 ? -31.653 34.873 -7.409 1.00 65.97 ? 1 ASP A CA 1 ATOM 3 C C . ASP A 1 1 ? -32.701 34.443 -6.396 1.00 64.63 ? 1 ASP A C 1 ATOM 4 O O . ASP A 1 1 ? -33.776 33.984 -6.779 1.00 62.89 ? 1 ASP A O 1 ATOM 5 C CB . ASP A 1 1 ? -32.036 36.234 -8.002 1.00 67.07 ? 1 ASP A CB 1 ATOM 6 C CG . ASP A 1 1 ? -30.966 36.795 -8.920 1.00 69.57 ? 1 ASP A CG 1 ATOM 7 O OD1 . ASP A 1 1 ? -30.062 36.034 -9.319 1.00 70.85 ? 1 ASP A OD1 1 ATOM 8 O OD2 . ASP A 1 1 ? -31.028 38.001 -9.244 1.00 72.90 ? 1 ASP A OD2 1 ATOM 9 N N . GLN A 1 2 ? -32.392 34.592 -5.107 1.00 65.07 ? 2 GLN A N 1 ATOM 10 C CA . GLN A 1 2 ? -33.356 34.256 -4.062 1.00 64.00 ? 2 GLN A CA 1 ATOM 11 C C . GLN A 1 2 ? -33.242 35.087 -2.795 1.00 62.43 ? 2 GLN A C 1 ATOM 12 O O . GLN A 1 2 ? -32.185 35.621 -2.479 1.00 63.77 ? 2 GLN A O 1 ATOM 13 C CB . GLN A 1 2 ? -33.261 32.774 -3.707 1.00 65.02 ? 2 GLN A CB 1 ATOM 14 C CG . GLN A 1 2 ? -31.966 32.342 -3.046 1.00 66.62 ? 2 GLN A CG 1 ATOM 15 C CD . GLN A 1 2 ? -32.060 30.934 -2.493 1.00 66.53 ? 2 GLN A CD 1 ATOM 16 O OE1 . GLN A 1 2 ? -31.656 30.675 -1.364 1.00 66.91 ? 2 GLN A OE1 1 ATOM 17 N NE2 . GLN A 1 2 ? -32.609 30.018 -3.285 1.00 66.40 ? 2 GLN A NE2 1 ATOM 18 N N . ILE A 1 3 ? -34.359 35.191 -2.083 1.00 60.46 ? 3 ILE A N 1 ATOM 19 C CA . ILE A 1 3 ? -34.397 35.830 -0.774 1.00 59.86 ? 3 ILE A CA 1 ATOM 20 C C . ILE A 1 3 ? -35.000 34.842 0.224 1.00 57.87 ? 3 ILE A C 1 ATOM 21 O O . ILE A 1 3 ? -35.982 34.165 -0.082 1.00 58.52 ? 3 ILE A O 1 ATOM 22 C CB . ILE A 1 3 ? -35.181 37.162 -0.802 1.00 59.71 ? 3 ILE A CB 1 ATOM 23 C CG1 . ILE A 1 3 ? -34.907 37.972 0.467 1.00 60.47 ? 3 ILE A CG1 1 ATOM 24 C CG2 . ILE A 1 3 ? -36.676 36.932 -0.969 1.00 58.48 ? 3 ILE A CG2 1 ATOM 25 C CD1 . ILE A 1 3 ? -35.552 39.342 0.462 1.00 60.43 ? 3 ILE A CD1 1 ATOM 26 N N . CYS A 1 4 ? -34.392 34.751 1.401 1.00 56.92 ? 4 CYS A N 1 ATOM 27 C CA . CYS A 1 4 ? -34.795 33.790 2.420 1.00 56.08 ? 4 CYS A CA 1 ATOM 28 C C . CYS A 1 4 ? -35.194 34.493 3.694 1.00 54.34 ? 4 CYS A C 1 ATOM 29 O O . CYS A 1 4 ? -34.652 35.540 4.022 1.00 55.66 ? 4 CYS A O 1 ATOM 30 C CB . CYS A 1 4 ? -33.638 32.850 2.740 1.00 57.56 ? 4 CYS A CB 1 ATOM 31 S SG . CYS A 1 4 ? -32.974 31.979 1.305 1.00 60.44 ? 4 CYS A SG 1 ATOM 32 N N . ILE A 1 5 ? -36.132 33.904 4.424 1.00 52.96 ? 5 ILE A N 1 ATOM 33 C CA . ILE A 1 5 ? -36.429 34.345 5.780 1.00 52.00 ? 5 ILE A CA 1 ATOM 34 C C . ILE A 1 5 ? -35.793 33.375 6.756 1.00 51.08 ? 5 ILE A C 1 ATOM 35 O O . ILE A 1 5 ? -35.870 32.167 6.567 1.00 51.08 ? 5 ILE A O 1 ATOM 36 C CB . ILE A 1 5 ? -37.935 34.394 6.029 1.00 51.98 ? 5 ILE A CB 1 ATOM 37 C CG1 . ILE A 1 5 ? -38.625 35.201 4.922 1.00 52.91 ? 5 ILE A CG1 1 ATOM 38 C CG2 . ILE A 1 5 ? -38.229 34.976 7.406 1.00 51.98 ? 5 ILE A CG2 1 ATOM 39 C CD1 . ILE A 1 5 ? -38.185 36.643 4.837 1.00 53.40 ? 5 ILE A CD1 1 ATOM 40 N N . GLY A 1 6 ? -35.155 33.911 7.790 1.00 50.87 ? 6 GLY A N 1 ATOM 41 C CA . GLY A 1 6 ? -34.474 33.092 8.795 1.00 50.62 ? 6 GLY A CA 1 ATOM 42 C C . GLY A 1 6 ? -34.319 33.801 10.130 1.00 49.92 ? 6 GLY A C 1 ATOM 43 O O . GLY A 1 6 ? -34.840 34.900 10.336 1.00 50.00 ? 6 GLY A O 1 ATOM 44 N N . TYR A 1 7 ? -33.596 33.166 11.041 1.00 49.12 ? 7 TYR A N 1 ATOM 45 C CA . TYR A 1 7 ? -33.513 33.653 12.400 1.00 48.94 ? 7 TYR A CA 1 ATOM 46 C C . TYR A 1 7 ? -32.105 33.516 12.971 1.00 49.53 ? 7 TYR A C 1 ATOM 47 O O . TYR A 1 7 ? -31.264 32.808 12.430 1.00 48.37 ? 7 TYR A O 1 ATOM 48 C CB . TYR A 1 7 ? -34.539 32.928 13.276 1.00 48.84 ? 7 TYR A CB 1 ATOM 49 C CG . TYR A 1 7 ? -34.423 31.414 13.266 1.00 49.01 ? 7 TYR A CG 1 ATOM 50 C CD1 . TYR A 1 7 ? -35.121 30.648 12.343 1.00 47.64 ? 7 TYR A CD1 1 ATOM 51 C CD2 . TYR A 1 7 ? -33.617 30.750 14.196 1.00 50.07 ? 7 TYR A CD2 1 ATOM 52 C CE1 . TYR A 1 7 ? -35.005 29.265 12.330 1.00 48.48 ? 7 TYR A CE1 1 ATOM 53 C CE2 . TYR A 1 7 ? -33.501 29.366 14.191 1.00 50.11 ? 7 TYR A CE2 1 ATOM 54 C CZ . TYR A 1 7 ? -34.195 28.628 13.256 1.00 49.23 ? 7 TYR A CZ 1 ATOM 55 O OH . TYR A 1 7 ? -34.071 27.254 13.258 1.00 48.50 ? 7 TYR A OH 1 ATOM 56 N N . HIS A 1 8 ? -31.878 34.215 14.075 1.00 50.88 ? 8 HIS A N 1 ATOM 57 C CA . HIS A 1 8 ? -30.563 34.338 14.711 1.00 52.82 ? 8 HIS A CA 1 ATOM 58 C C . HIS A 1 8 ? -30.065 33.020 15.293 1.00 53.04 ? 8 HIS A C 1 ATOM 59 O O . HIS A 1 8 ? -30.840 32.191 15.752 1.00 51.28 ? 8 HIS A O 1 ATOM 60 C CB . HIS A 1 8 ? -30.652 35.396 15.819 1.00 53.27 ? 8 HIS A CB 1 ATOM 61 C CG . HIS A 1 8 ? -29.350 35.711 16.492 1.00 55.49 ? 8 HIS A CG 1 ATOM 62 N ND1 . HIS A 1 8 ? -28.319 36.369 15.855 1.00 57.10 ? 8 HIS A ND1 1 ATOM 63 C CD2 . HIS A 1 8 ? -28.935 35.507 17.765 1.00 55.66 ? 8 HIS A CD2 1 ATOM 64 C CE1 . HIS A 1 8 ? -27.316 36.534 16.699 1.00 57.69 ? 8 HIS A CE1 1 ATOM 65 N NE2 . HIS A 1 8 ? -27.666 36.025 17.866 1.00 57.47 ? 8 HIS A NE2 1 ATOM 66 N N . ALA A 1 9 ? -28.757 32.829 15.244 1.00 55.55 ? 9 ALA A N 1 ATOM 67 C CA . ALA A 1 9 ? -28.107 31.743 15.963 1.00 56.33 ? 9 ALA A CA 1 ATOM 68 C C . ALA A 1 9 ? -26.784 32.281 16.477 1.00 57.85 ? 9 ALA A C 1 ATOM 69 O O . ALA A 1 9 ? -26.241 33.238 15.925 1.00 59.80 ? 9 ALA A O 1 ATOM 70 C CB . ALA A 1 9 ? -27.893 30.549 15.053 1.00 56.35 ? 9 ALA A CB 1 ATOM 71 N N . ASN A 1 10 ? -26.276 31.686 17.545 1.00 58.34 ? 10 ASN A N 1 ATOM 72 C CA . ASN A 1 10 ? -25.004 32.110 18.105 1.00 60.80 ? 10 ASN A CA 1 ATOM 73 C C . ASN A 1 10 ? -24.293 30.951 18.797 1.00 62.49 ? 10 ASN A C 1 ATOM 74 O O . ASN A 1 10 ? -24.710 29.806 18.657 1.00 60.59 ? 10 ASN A O 1 ATOM 75 C CB . ASN A 1 10 ? -25.216 33.301 19.044 1.00 60.75 ? 10 ASN A CB 1 ATOM 76 C CG . ASN A 1 10 ? -26.080 32.962 20.233 1.00 60.15 ? 10 ASN A CG 1 ATOM 77 O OD1 . ASN A 1 10 ? -26.415 31.801 20.469 1.00 60.08 ? 10 ASN A OD1 1 ATOM 78 N ND2 . ASN A 1 10 ? -26.457 33.982 20.989 1.00 60.10 ? 10 ASN A ND2 1 ATOM 79 N N . ASN A 1 11 ? -23.213 31.247 19.515 1.00 66.18 ? 11 ASN A N 1 ATOM 80 C CA . ASN A 1 11 ? -22.403 30.213 20.150 1.00 69.53 ? 11 ASN A CA 1 ATOM 81 C C . ASN A 1 11 ? -22.862 29.913 21.582 1.00 68.74 ? 11 ASN A C 1 ATOM 82 O O . ASN A 1 11 ? -22.105 29.351 22.375 1.00 70.56 ? 11 ASN A O 1 ATOM 83 C CB . ASN A 1 11 ? -20.911 30.605 20.109 1.00 74.40 ? 11 ASN A CB 1 ATOM 84 C CG . ASN A 1 11 ? -20.598 31.869 20.910 1.00 76.91 ? 11 ASN A CG 1 ATOM 85 O OD1 . ASN A 1 11 ? -21.475 32.439 21.564 1.00 77.20 ? 11 ASN A OD1 1 ATOM 86 N ND2 . ASN A 1 11 ? -19.339 32.317 20.851 1.00 78.78 ? 11 ASN A ND2 1 ATOM 87 N N . SER A 1 12 ? -24.110 30.268 21.894 1.00 66.51 ? 12 SER A N 1 ATOM 88 C CA . SER A 1 12 ? -24.634 30.187 23.254 1.00 65.13 ? 12 SER A CA 1 ATOM 89 C C . SER A 1 12 ? -24.928 28.742 23.647 1.00 65.21 ? 12 SER A C 1 ATOM 90 O O . SER A 1 12 ? -25.431 27.958 22.839 1.00 63.81 ? 12 SER A O 1 ATOM 91 C CB . SER A 1 12 ? -25.901 31.043 23.394 1.00 63.29 ? 12 SER A CB 1 ATOM 92 O OG . SER A 1 12 ? -26.299 31.190 24.748 1.00 62.25 ? 12 SER A OG 1 ATOM 93 N N . THR A 1 13 ? -24.583 28.409 24.891 1.00 65.47 ? 13 THR A N 1 ATOM 94 C CA . THR A 1 13 ? -24.830 27.093 25.468 1.00 64.90 ? 13 THR A CA 1 ATOM 95 C C . THR A 1 13 ? -25.821 27.179 26.634 1.00 64.07 ? 13 THR A C 1 ATOM 96 O O . THR A 1 13 ? -26.074 26.184 27.306 1.00 62.40 ? 13 THR A O 1 ATOM 97 C CB . THR A 1 13 ? -23.512 26.464 25.966 1.00 66.84 ? 13 THR A CB 1 ATOM 98 O OG1 . THR A 1 13 ? -22.850 27.371 26.858 1.00 66.85 ? 13 THR A OG1 1 ATOM 99 C CG2 . THR A 1 13 ? -22.588 26.151 24.797 1.00 67.70 ? 13 THR A CG2 1 ATOM 100 N N . GLU A 1 14 ? -26.382 28.367 26.862 1.00 63.98 ? 14 GLU A N 1 ATOM 101 C CA . GLU A 1 14 ? -27.383 28.574 27.900 1.00 63.87 ? 14 GLU A CA 1 ATOM 102 C C . GLU A 1 14 ? -28.626 27.736 27.616 1.00 62.58 ? 14 GLU A C 1 ATOM 103 O O . GLU A 1 14 ? -29.179 27.790 26.519 1.00 62.49 ? 14 GLU A O 1 ATOM 104 C CB . GLU A 1 14 ? -27.784 30.048 27.971 1.00 66.07 ? 14 GLU A CB 1 ATOM 105 C CG . GLU A 1 14 ? -26.678 30.993 28.418 1.00 69.23 ? 14 GLU A CG 1 ATOM 106 C CD . GLU A 1 14 ? -26.384 30.896 29.903 1.00 73.52 ? 14 GLU A CD 1 ATOM 107 O OE1 . GLU A 1 14 ? -27.341 31.011 30.706 1.00 75.28 ? 14 GLU A OE1 1 ATOM 108 O OE2 . GLU A 1 14 ? -25.198 30.697 30.267 1.00 76.59 ? 14 GLU A OE2 1 ATOM 109 N N . GLN A 1 15 ? -29.064 26.971 28.614 1.00 62.07 ? 15 GLN A N 1 ATOM 110 C CA . GLN A 1 15 ? -30.227 26.098 28.485 1.00 59.34 ? 15 GLN A CA 1 ATOM 111 C C . GLN A 1 15 ? -31.361 26.556 29.383 1.00 55.61 ? 15 GLN A C 1 ATOM 112 O O . GLN A 1 15 ? -31.122 27.088 30.453 1.00 54.56 ? 15 GLN A O 1 ATOM 113 C CB . GLN A 1 15 ? -29.856 24.686 28.894 1.00 62.09 ? 15 GLN A CB 1 ATOM 114 C CG . GLN A 1 15 ? -28.859 23.996 27.993 1.00 65.04 ? 15 GLN A CG 1 ATOM 115 C CD . GLN A 1 15 ? -28.586 22.583 28.455 1.00 67.90 ? 15 GLN A CD 1 ATOM 116 O OE1 . GLN A 1 15 ? -28.867 22.231 29.602 1.00 70.89 ? 15 GLN A OE1 1 ATOM 117 N NE2 . GLN A 1 15 ? -28.044 21.762 27.567 1.00 70.13 ? 15 GLN A NE2 1 ATOM 118 N N . VAL A 1 16 ? -32.594 26.331 28.951 1.00 53.30 ? 16 VAL A N 1 ATOM 119 C CA . VAL A 1 16 ? -33.763 26.601 29.780 1.00 51.42 ? 16 VAL A CA 1 ATOM 120 C C . VAL A 1 16 ? -34.705 25.429 29.667 1.00 51.45 ? 16 VAL A C 1 ATOM 121 O O . VAL A 1 16 ? -34.656 24.697 28.680 1.00 51.74 ? 16 VAL A O 1 ATOM 122 C CB . VAL A 1 16 ? -34.504 27.888 29.367 1.00 50.47 ? 16 VAL A CB 1 ATOM 123 C CG1 . VAL A 1 16 ? -33.556 29.079 29.410 1.00 51.02 ? 16 VAL A CG1 1 ATOM 124 C CG2 . VAL A 1 16 ? -35.137 27.744 27.992 1.00 50.25 ? 16 VAL A CG2 1 ATOM 125 N N . ASP A 1 17 ? -35.548 25.252 30.681 1.00 51.13 ? 17 ASP A N 1 ATOM 126 C CA . ASP A 1 17 ? -36.526 24.173 30.700 1.00 51.62 ? 17 ASP A CA 1 ATOM 127 C C . ASP A 1 17 ? -37.906 24.662 30.259 1.00 51.06 ? 17 ASP A C 1 ATOM 128 O O . ASP A 1 17 ? -38.263 25.830 30.455 1.00 50.61 ? 17 ASP A O 1 ATOM 129 C CB . ASP A 1 17 ? -36.629 23.585 32.109 1.00 53.53 ? 17 ASP A CB 1 ATOM 130 C CG . ASP A 1 17 ? -35.411 22.755 32.504 1.00 56.17 ? 17 ASP A CG 1 ATOM 131 O OD1 . ASP A 1 17 ? -34.726 22.208 31.611 1.00 57.36 ? 17 ASP A OD1 1 ATOM 132 O OD2 . ASP A 1 17 ? -35.153 22.632 33.727 1.00 57.59 ? 17 ASP A OD2 1 ATOM 133 N N . THR A 1 18 ? -38.678 23.761 29.657 1.00 50.91 ? 18 THR A N 1 ATOM 134 C CA . THR A 1 18 ? -40.101 23.997 29.393 1.00 50.59 ? 18 THR A CA 1 ATOM 135 C C . THR A 1 18 ? -40.903 22.811 29.917 1.00 52.62 ? 18 THR A C 1 ATOM 136 O O . THR A 1 18 ? -40.336 21.833 30.397 1.00 56.30 ? 18 THR A O 1 ATOM 137 C CB . THR A 1 18 ? -40.391 24.196 27.885 1.00 48.99 ? 18 THR A CB 1 ATOM 138 O OG1 . THR A 1 18 ? -40.192 22.968 27.183 1.00 49.03 ? 18 THR A OG1 1 ATOM 139 C CG2 . THR A 1 18 ? -39.484 25.256 27.295 1.00 47.94 ? 18 THR A CG2 1 ATOM 140 N N . ILE A 1 19 ? -42.221 22.894 29.826 1.00 54.79 ? 19 ILE A N 1 ATOM 141 C CA . ILE A 1 19 ? -43.089 21.802 30.272 1.00 56.84 ? 19 ILE A CA 1 ATOM 142 C C . ILE A 1 19 ? -42.828 20.516 29.479 1.00 56.89 ? 19 ILE A C 1 ATOM 143 O O . ILE A 1 19 ? -42.710 19.432 30.058 1.00 56.06 ? 19 ILE A O 1 ATOM 144 C CB . ILE A 1 19 ? -44.577 22.200 30.137 1.00 58.69 ? 19 ILE A CB 1 ATOM 145 C CG1 . ILE A 1 19 ? -44.930 23.308 31.135 1.00 59.45 ? 19 ILE A CG1 1 ATOM 146 C CG2 . ILE A 1 19 ? -45.493 21.004 30.345 1.00 59.77 ? 19 ILE A CG2 1 ATOM 147 C CD1 . ILE A 1 19 ? -45.026 22.839 32.576 1.00 60.36 ? 19 ILE A CD1 1 ATOM 148 N N . MET A 1 20 ? -42.731 20.652 28.158 1.00 56.00 ? 20 MET A N 1 ATOM 149 C CA . MET A 1 20 ? -42.549 19.507 27.270 1.00 56.88 ? 20 MET A CA 1 ATOM 150 C C . MET A 1 20 ? -41.099 19.111 27.006 1.00 57.05 ? 20 MET A C 1 ATOM 151 O O . MET A 1 20 ? -40.845 18.015 26.514 1.00 57.18 ? 20 MET A O 1 ATOM 152 C CB . MET A 1 20 ? -43.202 19.788 25.930 1.00 58.06 ? 20 MET A CB 1 ATOM 153 C CG . MET A 1 20 ? -44.710 19.838 25.987 1.00 58.96 ? 20 MET A CG 1 ATOM 154 S SD . MET A 1 20 ? -45.369 20.010 24.330 1.00 61.39 ? 20 MET A SD 1 ATOM 155 C CE . MET A 1 20 ? -46.852 19.036 24.499 1.00 63.48 ? 20 MET A CE 1 ATOM 156 N N . GLU A 1 21 ? -40.151 19.991 27.303 1.00 57.66 ? 21 GLU A N 1 ATOM 157 C CA . GLU A 1 21 ? -38.761 19.728 26.954 1.00 58.59 ? 21 GLU A CA 1 ATOM 158 C C . GLU A 1 21 ? -37.808 20.379 27.934 1.00 59.65 ? 21 GLU A C 1 ATOM 159 O O . GLU A 1 21 ? -37.875 21.589 28.169 1.00 58.51 ? 21 GLU A O 1 ATOM 160 C CB . GLU A 1 21 ? -38.461 20.222 25.542 1.00 58.07 ? 21 GLU A CB 1 ATOM 161 C CG . GLU A 1 21 ? -37.273 19.520 24.908 1.00 60.19 ? 21 GLU A CG 1 ATOM 162 C CD . GLU A 1 21 ? -36.945 20.036 23.515 1.00 61.76 ? 21 GLU A CD 1 ATOM 163 O OE1 . GLU A 1 21 ? -37.817 20.682 22.881 1.00 61.41 ? 21 GLU A OE1 1 ATOM 164 O OE2 . GLU A 1 21 ? -35.806 19.789 23.053 1.00 60.69 ? 21 GLU A OE2 1 ATOM 165 N N . LYS A 1 22 ? -36.925 19.555 28.498 1.00 61.00 ? 22 LYS A N 1 ATOM 166 C CA . LYS A 1 22 ? -35.891 20.012 29.415 1.00 60.77 ? 22 LYS A CA 1 ATOM 167 C C . LYS A 1 22 ? -34.631 20.308 28.618 1.00 59.55 ? 22 LYS A C 1 ATOM 168 O O . LYS A 1 22 ? -34.436 19.755 27.544 1.00 58.93 ? 22 LYS A O 1 ATOM 169 C CB . LYS A 1 22 ? -35.612 18.948 30.484 1.00 62.86 ? 22 LYS A CB 1 ATOM 170 C CG . LYS A 1 22 ? -36.339 19.158 31.804 1.00 64.78 ? 22 LYS A CG 1 ATOM 171 C CD . LYS A 1 22 ? -37.849 18.991 31.698 1.00 66.94 ? 22 LYS A CD 1 ATOM 172 C CE . LYS A 1 22 ? -38.568 19.915 32.681 1.00 68.75 ? 22 LYS A CE 1 ATOM 173 N NZ . LYS A 1 22 ? -40.053 19.828 32.595 1.00 68.72 ? 22 LYS A NZ 1 ATOM 174 N N . ASN A 1 23 ? -33.789 21.190 29.143 1.00 60.32 ? 23 ASN A N 1 ATOM 175 C CA . ASN A 1 23 ? -32.479 21.463 28.557 1.00 62.84 ? 23 ASN A CA 1 ATOM 176 C C . ASN A 1 23 ? -32.561 21.872 27.082 1.00 59.25 ? 23 ASN A C 1 ATOM 177 O O . ASN A 1 23 ? -32.014 21.211 26.206 1.00 58.29 ? 23 ASN A O 1 ATOM 178 C CB . ASN A 1 23 ? -31.543 20.252 28.755 1.00 68.22 ? 23 ASN A CB 1 ATOM 179 C CG . ASN A 1 23 ? -31.216 19.992 30.220 1.00 74.17 ? 23 ASN A CG 1 ATOM 180 O OD1 . ASN A 1 23 ? -31.397 20.868 31.070 1.00 74.25 ? 23 ASN A OD1 1 ATOM 181 N ND2 . ASN A 1 23 ? -30.726 18.782 30.523 1.00 82.29 ? 23 ASN A ND2 1 ATOM 182 N N . VAL A 1 24 ? -33.272 22.965 26.828 1.00 56.48 ? 24 VAL A N 1 ATOM 183 C CA . VAL A 1 24 ? -33.366 23.562 25.500 1.00 54.15 ? 24 VAL A CA 1 ATOM 184 C C . VAL A 1 24 ? -32.358 24.700 25.400 1.00 54.73 ? 24 VAL A C 1 ATOM 185 O O . VAL A 1 24 ? -32.479 25.697 26.112 1.00 55.23 ? 24 VAL A O 1 ATOM 186 C CB . VAL A 1 24 ? -34.765 24.146 25.243 1.00 52.21 ? 24 VAL A CB 1 ATOM 187 C CG1 . VAL A 1 24 ? -34.808 24.880 23.906 1.00 52.28 ? 24 VAL A CG1 1 ATOM 188 C CG2 . VAL A 1 24 ? -35.808 23.043 25.285 1.00 52.09 ? 24 VAL A CG2 1 ATOM 189 N N . THR A 1 25 ? -31.373 24.551 24.519 1.00 54.35 ? 25 THR A N 1 ATOM 190 C CA . THR A 1 25 ? -30.374 25.585 24.314 1.00 54.72 ? 25 THR A CA 1 ATOM 191 C C . THR A 1 25 ? -31.025 26.792 23.659 1.00 53.71 ? 25 THR A C 1 ATOM 192 O O . THR A 1 25 ? -31.805 26.636 22.723 1.00 53.98 ? 25 THR A O 1 ATOM 193 C CB . THR A 1 25 ? -29.241 25.105 23.393 1.00 56.73 ? 25 THR A CB 1 ATOM 194 O OG1 . THR A 1 25 ? -28.853 23.775 23.758 1.00 59.16 ? 25 THR A OG1 1 ATOM 195 C CG2 . THR A 1 25 ? -28.038 26.041 23.496 1.00 57.69 ? 25 THR A CG2 1 ATOM 196 N N . VAL A 1 26 ? -30.701 27.987 24.146 1.00 52.13 ? 26 VAL A N 1 ATOM 197 C CA . VAL A 1 26 ? -31.248 29.214 23.582 1.00 51.11 ? 26 VAL A CA 1 ATOM 198 C C . VAL A 1 26 ? -30.164 30.246 23.348 1.00 52.37 ? 26 VAL A C 1 ATOM 199 O O . VAL A 1 26 ? -29.112 30.205 23.980 1.00 55.79 ? 26 VAL A O 1 ATOM 200 C CB . VAL A 1 26 ? -32.330 29.834 24.481 1.00 49.50 ? 26 VAL A CB 1 ATOM 201 C CG1 . VAL A 1 26 ? -33.538 28.917 24.555 1.00 48.43 ? 26 VAL A CG1 1 ATOM 202 C CG2 . VAL A 1 26 ? -31.782 30.145 25.868 1.00 50.01 ? 26 VAL A CG2 1 ATOM 203 N N . THR A 1 27 ? -30.442 31.187 22.452 1.00 52.02 ? 27 THR A N 1 ATOM 204 C CA . THR A 1 27 ? -29.474 32.221 22.096 1.00 52.19 ? 27 THR A CA 1 ATOM 205 C C . THR A 1 27 ? -29.269 33.198 23.250 1.00 52.31 ? 27 THR A C 1 ATOM 206 O O . THR A 1 27 ? -28.163 33.676 23.473 1.00 54.16 ? 27 THR A O 1 ATOM 207 C CB . THR A 1 27 ? -29.911 33.001 20.844 1.00 51.81 ? 27 THR A CB 1 ATOM 208 O OG1 . THR A 1 27 ? -31.118 33.725 21.113 1.00 51.01 ? 27 THR A OG1 1 ATOM 209 C CG2 . THR A 1 27 ? -30.145 32.052 19.675 1.00 51.78 ? 27 THR A CG2 1 ATOM 210 N N . HIS A 1 28 ? -30.339 33.490 23.984 1.00 51.02 ? 28 HIS A N 1 ATOM 211 C CA . HIS A 1 28 ? -30.270 34.412 25.113 1.00 50.64 ? 28 HIS A CA 1 ATOM 212 C C . HIS A 1 28 ? -31.159 33.969 26.266 1.00 49.84 ? 28 HIS A C 1 ATOM 213 O O . HIS A 1 28 ? -32.236 33.416 26.061 1.00 47.96 ? 28 HIS A O 1 ATOM 214 C CB . HIS A 1 28 ? -30.675 35.807 24.664 1.00 50.59 ? 28 HIS A CB 1 ATOM 215 C CG . HIS A 1 28 ? -29.878 36.319 23.508 1.00 51.78 ? 28 HIS A CG 1 ATOM 216 N ND1 . HIS A 1 28 ? -30.220 36.058 22.198 1.00 51.21 ? 28 HIS A ND1 1 ATOM 217 C CD2 . HIS A 1 28 ? -28.750 37.067 23.463 1.00 52.42 ? 28 HIS A CD2 1 ATOM 218 C CE1 . HIS A 1 28 ? -29.340 36.629 21.396 1.00 51.76 ? 28 HIS A CE1 1 ATOM 219 N NE2 . HIS A 1 28 ? -28.438 37.245 22.139 1.00 52.76 ? 28 HIS A NE2 1 ATOM 220 N N . ALA A 1 29 ? -30.702 34.231 27.483 1.00 51.62 ? 29 ALA A N 1 ATOM 221 C CA . ALA A 1 29 ? -31.433 33.831 28.682 1.00 52.15 ? 29 ALA A CA 1 ATOM 222 C C . ALA A 1 29 ? -31.188 34.835 29.781 1.00 54.36 ? 29 ALA A C 1 ATOM 223 O O . ALA A 1 29 ? -30.282 35.661 29.690 1.00 55.57 ? 29 ALA A O 1 ATOM 224 C CB . ALA A 1 29 ? -31.001 32.446 29.136 1.00 51.51 ? 29 ALA A CB 1 ATOM 225 N N . GLN A 1 30 ? -32.002 34.766 30.822 1.00 56.92 ? 30 GLN A N 1 ATOM 226 C CA . GLN A 1 30 ? -31.805 35.619 31.980 1.00 59.55 ? 30 GLN A CA 1 ATOM 227 C C . GLN A 1 30 ? -31.974 34.825 33.264 1.00 58.24 ? 30 GLN A C 1 ATOM 228 O O . GLN A 1 30 ? -33.077 34.409 33.613 1.00 57.32 ? 30 GLN A O 1 ATOM 229 C CB . GLN A 1 30 ? -32.772 36.800 31.949 1.00 61.31 ? 30 GLN A CB 1 ATOM 230 C CG . GLN A 1 30 ? -32.539 37.789 33.080 1.00 63.66 ? 30 GLN A CG 1 ATOM 231 C CD . GLN A 1 30 ? -33.268 39.098 32.873 1.00 66.18 ? 30 GLN A CD 1 ATOM 232 O OE1 . GLN A 1 30 ? -33.582 39.484 31.744 1.00 68.02 ? 30 GLN A OE1 1 ATOM 233 N NE2 . GLN A 1 30 ? -33.535 39.799 33.968 1.00 67.88 ? 30 GLN A NE2 1 ATOM 234 N N . ASP A 1 31 ? -30.863 34.603 33.953 1.00 59.32 ? 31 ASP A N 1 ATOM 235 C CA . ASP A 1 31 ? -30.894 33.989 35.266 1.00 58.48 ? 31 ASP A CA 1 ATOM 236 C C . ASP A 1 31 ? -31.531 34.993 36.234 1.00 58.04 ? 31 ASP A C 1 ATOM 237 O O . ASP A 1 31 ? -31.179 36.181 36.234 1.00 58.05 ? 31 ASP A O 1 ATOM 238 C CB . ASP A 1 31 ? -29.478 33.629 35.705 1.00 59.24 ? 31 ASP A CB 1 ATOM 239 C CG . ASP A 1 31 ? -29.450 32.782 36.956 1.00 60.71 ? 31 ASP A CG 1 ATOM 240 O OD1 . ASP A 1 31 ? -30.516 32.564 37.576 1.00 61.02 ? 31 ASP A OD1 1 ATOM 241 O OD2 . ASP A 1 31 ? -28.349 32.326 37.319 1.00 62.33 ? 31 ASP A OD2 1 ATOM 242 N N . ILE A 1 32 ? -32.476 34.515 37.038 1.00 55.56 ? 32 ILE A N 1 ATOM 243 C CA . ILE A 1 32 ? -33.179 35.370 37.991 1.00 55.25 ? 32 ILE A CA 1 ATOM 244 C C . ILE A 1 32 ? -33.030 34.897 39.442 1.00 55.87 ? 32 ILE A C 1 ATOM 245 O O . ILE A 1 32 ? -33.693 35.412 40.340 1.00 55.65 ? 32 ILE A O 1 ATOM 246 C CB . ILE A 1 32 ? -34.667 35.492 37.621 1.00 54.09 ? 32 ILE A CB 1 ATOM 247 C CG1 . ILE A 1 32 ? -35.313 34.117 37.468 1.00 52.75 ? 32 ILE A CG1 1 ATOM 248 C CG2 . ILE A 1 32 ? -34.813 36.275 36.330 1.00 55.33 ? 32 ILE A CG2 1 ATOM 249 C CD1 . ILE A 1 32 ? -36.823 34.165 37.458 1.00 52.27 ? 32 ILE A CD1 1 ATOM 250 N N . LEU A 1 33 ? -32.139 33.937 39.667 1.00 56.77 ? 33 LEU A N 1 ATOM 251 C CA . LEU A 1 33 ? -31.923 33.369 40.989 1.00 57.37 ? 33 LEU A CA 1 ATOM 252 C C . LEU A 1 33 ? -30.501 33.623 41.473 1.00 59.67 ? 33 LEU A C 1 ATOM 253 O O . LEU A 1 33 ? -29.544 33.143 40.864 1.00 61.57 ? 33 LEU A O 1 ATOM 254 C CB . LEU A 1 33 ? -32.168 31.866 40.938 1.00 56.78 ? 33 LEU A CB 1 ATOM 255 C CG . LEU A 1 33 ? -32.102 31.125 42.267 1.00 56.41 ? 33 LEU A CG 1 ATOM 256 C CD1 . LEU A 1 33 ? -33.217 31.608 43.180 1.00 56.51 ? 33 LEU A CD1 1 ATOM 257 C CD2 . LEU A 1 33 ? -32.196 29.626 42.033 1.00 56.33 ? 33 LEU A CD2 1 ATOM 258 N N . GLU A 1 34 ? -30.364 34.366 42.568 1.00 60.93 ? 34 GLU A N 1 ATOM 259 C CA . GLU A 1 34 ? -29.061 34.545 43.213 1.00 63.14 ? 34 GLU A CA 1 ATOM 260 C C . GLU A 1 34 ? -28.700 33.297 43.999 1.00 61.69 ? 34 GLU A C 1 ATOM 261 O O . GLU A 1 34 ? -29.455 32.875 44.870 1.00 60.37 ? 34 GLU A O 1 ATOM 262 C CB . GLU A 1 34 ? -29.075 35.740 44.166 1.00 64.57 ? 34 GLU A CB 1 ATOM 263 C CG . GLU A 1 34 ? -27.739 35.998 44.849 1.00 66.17 ? 34 GLU A CG 1 ATOM 264 C CD . GLU A 1 34 ? -26.606 36.158 43.857 1.00 68.32 ? 34 GLU A CD 1 ATOM 265 O OE1 . GLU A 1 34 ? -26.731 37.007 42.952 1.00 69.72 ? 34 GLU A OE1 1 ATOM 266 O OE2 . GLU A 1 34 ? -25.602 35.425 43.968 1.00 70.80 ? 34 GLU A OE2 1 ATOM 267 N N . LYS A 1 35 ? -27.544 32.718 43.698 1.00 61.78 ? 35 LYS A N 1 ATOM 268 C CA . LYS A 1 35 ? -27.116 31.495 44.365 1.00 62.93 ? 35 LYS A CA 1 ATOM 269 C C . LYS A 1 35 ? -25.957 31.701 45.340 1.00 63.62 ? 35 LYS A C 1 ATOM 270 O O . LYS A 1 35 ? -25.681 30.816 46.149 1.00 63.47 ? 35 LYS A O 1 ATOM 271 C CB . LYS A 1 35 ? -26.738 30.433 43.332 1.00 63.49 ? 35 LYS A CB 1 ATOM 272 C CG . LYS A 1 35 ? -27.928 29.811 42.622 1.00 63.21 ? 35 LYS A CG 1 ATOM 273 C CD . LYS A 1 35 ? -27.480 28.828 41.544 1.00 64.78 ? 35 LYS A CD 1 ATOM 274 C CE . LYS A 1 35 ? -28.197 29.067 40.224 1.00 64.69 ? 35 LYS A CE 1 ATOM 275 N NZ . LYS A 1 35 ? -27.824 30.377 39.611 1.00 65.57 ? 35 LYS A NZ 1 ATOM 276 N N . THR A 1 36 ? -25.292 32.852 45.275 1.00 64.14 ? 36 THR A N 1 ATOM 277 C CA . THR A 1 36 ? -24.095 33.076 46.072 1.00 67.80 ? 36 THR A CA 1 ATOM 278 C C . THR A 1 36 ? -24.318 34.053 47.216 1.00 69.07 ? 36 THR A C 1 ATOM 279 O O . THR A 1 36 ? -25.290 34.811 47.230 1.00 66.41 ? 36 THR A O 1 ATOM 280 C CB . THR A 1 36 ? -22.931 33.613 45.220 1.00 70.11 ? 36 THR A CB 1 ATOM 281 O OG1 . THR A 1 36 ? -23.245 34.929 44.755 1.00 71.12 ? 36 THR A OG1 1 ATOM 282 C CG2 . THR A 1 36 ? -22.664 32.703 44.033 1.00 70.71 ? 36 THR A CG2 1 ATOM 283 N N . HIS A 1 37 ? -23.384 34.015 48.164 1.00 71.31 ? 37 HIS A N 1 ATOM 284 C CA . HIS A 1 37 ? -23.351 34.929 49.298 1.00 72.16 ? 37 HIS A CA 1 ATOM 285 C C . HIS A 1 37 ? -21.908 35.014 49.803 1.00 75.44 ? 37 HIS A C 1 ATOM 286 O O . HIS A 1 37 ? -21.117 34.097 49.581 1.00 76.88 ? 37 HIS A O 1 ATOM 287 C CB . HIS A 1 37 ? -24.282 34.430 50.403 1.00 71.25 ? 37 HIS A CB 1 ATOM 288 C CG . HIS A 1 37 ? -23.912 33.082 50.941 1.00 71.83 ? 37 HIS A CG 1 ATOM 289 N ND1 . HIS A 1 37 ? -23.198 32.919 52.107 1.00 71.52 ? 37 HIS A ND1 1 ATOM 290 C CD2 . HIS A 1 37 ? -24.142 31.836 50.466 1.00 72.36 ? 37 HIS A CD2 1 ATOM 291 C CE1 . HIS A 1 37 ? -23.010 31.632 52.334 1.00 72.38 ? 37 HIS A CE1 1 ATOM 292 N NE2 . HIS A 1 37 ? -23.575 30.952 51.354 1.00 73.01 ? 37 HIS A NE2 1 ATOM 293 N N . ASN A 1 38 ? -21.564 36.107 50.479 1.00 77.65 ? 38 ASN A N 1 ATOM 294 C CA . ASN A 1 38 ? -20.185 36.308 50.954 1.00 80.62 ? 38 ASN A CA 1 ATOM 295 C C . ASN A 1 38 ? -19.799 35.485 52.198 1.00 81.95 ? 38 ASN A C 1 ATOM 296 O O . ASN A 1 38 ? -18.630 35.460 52.586 1.00 85.08 ? 38 ASN A O 1 ATOM 297 C CB . ASN A 1 38 ? -19.899 37.799 51.201 1.00 80.31 ? 38 ASN A CB 1 ATOM 298 C CG . ASN A 1 38 ? -20.644 38.357 52.402 1.00 78.02 ? 38 ASN A CG 1 ATOM 299 O OD1 . ASN A 1 38 ? -21.225 37.616 53.196 1.00 76.25 ? 38 ASN A OD1 1 ATOM 300 N ND2 . ASN A 1 38 ? -20.628 39.673 52.537 1.00 77.40 ? 38 ASN A ND2 1 ATOM 301 N N . GLY A 1 39 ? -20.780 34.852 52.837 1.00 79.64 ? 39 GLY A N 1 ATOM 302 C CA . GLY A 1 39 ? -20.514 33.896 53.921 1.00 79.12 ? 39 GLY A CA 1 ATOM 303 C C . GLY A 1 39 ? -20.199 34.531 55.261 1.00 77.83 ? 39 GLY A C 1 ATOM 304 O O . GLY A 1 39 ? -19.659 33.872 56.151 1.00 74.79 ? 39 GLY A O 1 ATOM 305 N N . LYS A 1 40 ? -20.562 35.805 55.401 1.00 79.21 ? 40 LYS A N 1 ATOM 306 C CA . LYS A 1 40 ? -20.175 36.628 56.541 1.00 80.40 ? 40 LYS A CA 1 ATOM 307 C C . LYS A 1 40 ? -21.373 37.350 57.145 1.00 80.20 ? 40 LYS A C 1 ATOM 308 O O . LYS A 1 40 ? -22.362 37.614 56.463 1.00 78.37 ? 40 LYS A O 1 ATOM 309 C CB . LYS A 1 40 ? -19.155 37.675 56.092 1.00 83.11 ? 40 LYS A CB 1 ATOM 310 C CG . LYS A 1 40 ? -17.802 37.106 55.695 1.00 86.69 ? 40 LYS A CG 1 ATOM 311 C CD . LYS A 1 40 ? -17.019 38.050 54.794 1.00 88.55 ? 40 LYS A CD 1 ATOM 312 C CE . LYS A 1 40 ? -15.694 37.423 54.385 1.00 91.53 ? 40 LYS A CE 1 ATOM 313 N NZ . LYS A 1 40 ? -14.932 38.258 53.416 1.00 94.29 ? 40 LYS A NZ 1 ATOM 314 N N . LEU A 1 41 ? -21.274 37.678 58.428 1.00 81.61 ? 41 LEU A N 1 ATOM 315 C CA . LEU A 1 41 ? -22.229 38.583 59.057 1.00 81.81 ? 41 LEU A CA 1 ATOM 316 C C . LEU A 1 41 ? -21.702 40.011 58.907 1.00 80.73 ? 41 LEU A C 1 ATOM 317 O O . LEU A 1 41 ? -20.558 40.291 59.267 1.00 82.60 ? 41 LEU A O 1 ATOM 318 C CB . LEU A 1 41 ? -22.424 38.215 60.524 1.00 83.43 ? 41 LEU A CB 1 ATOM 319 C CG . LEU A 1 41 ? -22.850 36.760 60.763 1.00 84.20 ? 41 LEU A CG 1 ATOM 320 C CD1 . LEU A 1 41 ? -22.848 36.449 62.253 1.00 84.10 ? 41 LEU A CD1 1 ATOM 321 C CD2 . LEU A 1 41 ? -24.214 36.468 60.143 1.00 82.71 ? 41 LEU A CD2 1 ATOM 322 N N . CYS A 1 42 ? -22.535 40.898 58.362 1.00 77.87 ? 42 CYS A N 1 ATOM 323 C CA . CYS A 1 42 ? -22.121 42.258 58.000 1.00 77.94 ? 42 CYS A CA 1 ATOM 324 C C . CYS A 1 42 ? -23.019 43.295 58.635 1.00 75.32 ? 42 CYS A C 1 ATOM 325 O O . CYS A 1 42 ? -24.076 42.973 59.157 1.00 73.31 ? 42 CYS A O 1 ATOM 326 C CB . CYS A 1 42 ? -22.193 42.458 56.480 1.00 78.68 ? 42 CYS A CB 1 ATOM 327 S SG . CYS A 1 42 ? -21.321 41.234 55.479 1.00 78.62 ? 42 CYS A SG 1 ATOM 328 N N . ASP A 1 43 ? -22.597 44.552 58.554 1.00 77.22 ? 43 ASP A N 1 ATOM 329 C CA . ASP A 1 43 ? -23.429 45.675 58.973 1.00 77.91 ? 43 ASP A CA 1 ATOM 330 C C . ASP A 1 43 ? -24.577 45.823 57.980 1.00 77.09 ? 43 ASP A C 1 ATOM 331 O O . ASP A 1 43 ? -24.430 45.475 56.807 1.00 76.56 ? 43 ASP A O 1 ATOM 332 C CB . ASP A 1 43 ? -22.614 46.977 59.020 1.00 80.55 ? 43 ASP A CB 1 ATOM 333 C CG . ASP A 1 43 ? -21.409 46.897 59.958 1.00 82.46 ? 43 ASP A CG 1 ATOM 334 O OD1 . ASP A 1 43 ? -21.347 45.978 60.795 1.00 83.45 ? 43 ASP A OD1 1 ATOM 335 O OD2 . ASP A 1 43 ? -20.515 47.760 59.861 1.00 84.13 ? 43 ASP A OD2 1 ATOM 336 N N . LEU A 1 44 ? -25.709 46.341 58.450 1.00 77.00 ? 44 LEU A N 1 ATOM 337 C CA . LEU A 1 44 ? -26.882 46.538 57.602 1.00 78.31 ? 44 LEU A CA 1 ATOM 338 C C . LEU A 1 44 ? -27.112 48.023 57.320 1.00 80.63 ? 44 LEU A C 1 ATOM 339 O O . LEU A 1 44 ? -27.633 48.749 58.169 1.00 79.18 ? 44 LEU A O 1 ATOM 340 C CB . LEU A 1 44 ? -28.122 45.923 58.259 1.00 77.74 ? 44 LEU A CB 1 ATOM 341 C CG . LEU A 1 44 ? -29.409 45.883 57.419 1.00 78.32 ? 44 LEU A CG 1 ATOM 342 C CD1 . LEU A 1 44 ? -29.283 44.901 56.261 1.00 77.55 ? 44 LEU A CD1 1 ATOM 343 C CD2 . LEU A 1 44 ? -30.612 45.538 58.287 1.00 77.03 ? 44 LEU A CD2 1 ATOM 344 N N . ASP A 1 45 ? -26.744 48.450 56.110 1.00 84.55 ? 45 ASP A N 1 ATOM 345 C CA . ASP A 1 45 ? -26.787 49.864 55.708 1.00 87.97 ? 45 ASP A CA 1 ATOM 346 C C . ASP A 1 45 ? -26.027 50.718 56.722 1.00 87.24 ? 45 ASP A C 1 ATOM 347 O O . ASP A 1 45 ? -26.545 51.711 57.239 1.00 85.17 ? 45 ASP A O 1 ATOM 348 C CB . ASP A 1 45 ? -28.235 50.352 55.515 1.00 91.01 ? 45 ASP A CB 1 ATOM 349 C CG . ASP A 1 45 ? -28.825 49.926 54.168 1.00 95.24 ? 45 ASP A CG 1 ATOM 350 O OD1 . ASP A 1 45 ? -28.533 50.600 53.155 1.00 99.00 ? 45 ASP A OD1 1 ATOM 351 O OD2 . ASP A 1 45 ? -29.570 48.918 54.115 1.00 95.48 ? 45 ASP A OD2 1 ATOM 352 N N . GLY A 1 46 ? -24.798 50.292 57.012 1.00 87.07 ? 46 GLY A N 1 ATOM 353 C CA . GLY A 1 46 ? -23.911 50.993 57.939 1.00 88.16 ? 46 GLY A CA 1 ATOM 354 C C . GLY A 1 46 ? -24.026 50.550 59.388 1.00 87.02 ? 46 GLY A C 1 ATOM 355 O O . GLY A 1 46 ? -23.040 50.595 60.122 1.00 86.68 ? 46 GLY A O 1 ATOM 356 N N . VAL A 1 47 ? -25.217 50.104 59.792 1.00 84.47 ? 47 VAL A N 1 ATOM 357 C CA . VAL A 1 47 ? -25.533 49.864 61.205 1.00 83.00 ? 47 VAL A CA 1 ATOM 358 C C . VAL A 1 47 ? -25.141 48.450 61.652 1.00 82.11 ? 47 VAL A C 1 ATOM 359 O O . VAL A 1 47 ? -25.770 47.468 61.257 1.00 81.59 ? 47 VAL A O 1 ATOM 360 C CB . VAL A 1 47 ? -27.035 50.102 61.479 1.00 81.07 ? 47 VAL A CB 1 ATOM 361 C CG1 . VAL A 1 47 ? -27.352 49.919 62.958 1.00 80.99 ? 47 VAL A CG1 1 ATOM 362 C CG2 . VAL A 1 47 ? -27.449 51.492 61.014 1.00 81.81 ? 47 VAL A CG2 1 ATOM 363 N N . LYS A 1 48 ? -24.110 48.364 62.489 1.00 82.85 ? 48 LYS A N 1 ATOM 364 C CA . LYS A 1 48 ? -23.567 47.088 62.964 1.00 83.44 ? 48 LYS A CA 1 ATOM 365 C C . LYS A 1 48 ? -24.601 46.288 63.754 1.00 79.90 ? 48 LYS A C 1 ATOM 366 O O . LYS A 1 48 ? -25.393 46.863 64.500 1.00 78.14 ? 48 LYS A O 1 ATOM 367 C CB . LYS A 1 48 ? -22.334 47.348 63.845 1.00 88.72 ? 48 LYS A CB 1 ATOM 368 C CG . LYS A 1 48 ? -21.550 46.118 64.298 1.00 91.31 ? 48 LYS A CG 1 ATOM 369 C CD . LYS A 1 48 ? -20.770 46.408 65.576 1.00 95.51 ? 48 LYS A CD 1 ATOM 370 C CE . LYS A 1 48 ? -19.985 45.198 66.063 1.00 97.54 ? 48 LYS A CE 1 ATOM 371 N NZ . LYS A 1 48 ? -18.689 45.040 65.347 1.00 100.54 ? 48 LYS A NZ 1 ATOM 372 N N . PRO A 1 49 ? -24.602 44.953 63.587 1.00 78.54 ? 49 PRO A N 1 ATOM 373 C CA . PRO A 1 49 ? -25.476 44.141 64.421 1.00 76.38 ? 49 PRO A CA 1 ATOM 374 C C . PRO A 1 49 ? -24.923 43.979 65.822 1.00 76.55 ? 49 PRO A C 1 ATOM 375 O O . PRO A 1 49 ? -23.731 44.186 66.049 1.00 78.07 ? 49 PRO A O 1 ATOM 376 C CB . PRO A 1 49 ? -25.462 42.784 63.720 1.00 74.64 ? 49 PRO A CB 1 ATOM 377 C CG . PRO A 1 49 ? -24.122 42.721 63.082 1.00 76.25 ? 49 PRO A CG 1 ATOM 378 C CD . PRO A 1 49 ? -23.865 44.127 62.611 1.00 78.11 ? 49 PRO A CD 1 ATOM 379 N N . LEU A 1 50 ? -25.798 43.600 66.744 1.00 74.45 ? 50 LEU A N 1 ATOM 380 C CA . LEU A 1 50 ? -25.392 43.208 68.078 1.00 74.23 ? 50 LEU A CA 1 ATOM 381 C C . LEU A 1 50 ? -25.057 41.725 68.033 1.00 73.15 ? 50 LEU A C 1 ATOM 382 O O . LEU A 1 50 ? -25.953 40.891 67.935 1.00 74.00 ? 50 LEU A O 1 ATOM 383 C CB . LEU A 1 50 ? -26.528 43.485 69.070 1.00 73.40 ? 50 LEU A CB 1 ATOM 384 C CG . LEU A 1 50 ? -26.374 43.017 70.517 1.00 73.05 ? 50 LEU A CG 1 ATOM 385 C CD1 . LEU A 1 50 ? -24.967 43.251 71.045 1.00 74.38 ? 50 LEU A CD1 1 ATOM 386 C CD2 . LEU A 1 50 ? -27.408 43.715 71.391 1.00 73.43 ? 50 LEU A CD2 1 ATOM 387 N N . ILE A 1 51 ? -23.771 41.395 68.071 1.00 74.01 ? 51 ILE A N 1 ATOM 388 C CA . ILE A 1 51 ? -23.348 39.992 68.050 1.00 74.08 ? 51 ILE A CA 1 ATOM 389 C C . ILE A 1 51 ? -23.053 39.520 69.472 1.00 73.95 ? 51 ILE A C 1 ATOM 390 O O . ILE A 1 51 ? -21.987 39.796 70.019 1.00 75.87 ? 51 ILE A O 1 ATOM 391 C CB . ILE A 1 51 ? -22.136 39.781 67.117 1.00 74.94 ? 51 ILE A CB 1 ATOM 392 C CG1 . ILE A 1 51 ? -22.527 40.199 65.695 1.00 76.06 ? 51 ILE A CG1 1 ATOM 393 C CG2 . ILE A 1 51 ? -21.660 38.330 67.149 1.00 74.54 ? 51 ILE A CG2 1 ATOM 394 C CD1 . ILE A 1 51 ? -21.601 39.711 64.602 1.00 78.27 ? 51 ILE A CD1 1 ATOM 395 N N . LEU A 1 52 ? -24.001 38.787 70.052 1.00 72.32 ? 52 LEU A N 1 ATOM 396 C CA . LEU A 1 52 ? -23.918 38.360 71.451 1.00 71.73 ? 52 LEU A CA 1 ATOM 397 C C . LEU A 1 52 ? -22.804 37.350 71.705 1.00 73.88 ? 52 LEU A C 1 ATOM 398 O O . LEU A 1 52 ? -22.456 37.096 72.854 1.00 76.16 ? 52 LEU A O 1 ATOM 399 C CB . LEU A 1 52 ? -25.256 37.778 71.910 1.00 68.53 ? 52 LEU A CB 1 ATOM 400 C CG . LEU A 1 52 ? -26.449 38.737 71.798 1.00 67.79 ? 52 LEU A CG 1 ATOM 401 C CD1 . LEU A 1 52 ? -27.757 38.043 72.133 1.00 66.03 ? 52 LEU A CD1 1 ATOM 402 C CD2 . LEU A 1 52 ? -26.256 39.956 72.687 1.00 70.00 ? 52 LEU A CD2 1 ATOM 403 N N . ARG A 1 53 ? -22.258 36.776 70.637 1.00 76.05 ? 53 ARG A N 1 ATOM 404 C CA . ARG A 1 53 ? -21.139 35.853 70.736 1.00 79.39 ? 53 ARG A CA 1 ATOM 405 C C . ARG A 1 53 ? -21.565 34.607 71.526 1.00 80.74 ? 53 ARG A C 1 ATOM 406 O O . ARG A 1 53 ? -22.446 33.874 71.068 1.00 83.57 ? 53 ARG A O 1 ATOM 407 C CB . ARG A 1 53 ? -19.931 36.565 71.338 1.00 83.04 ? 53 ARG A CB 1 ATOM 408 C CG . ARG A 1 53 ? -18.605 35.887 71.048 1.00 87.09 ? 53 ARG A CG 1 ATOM 409 C CD . ARG A 1 53 ? -17.482 36.490 71.880 1.00 90.61 ? 53 ARG A CD 1 ATOM 410 N NE . ARG A 1 53 ? -16.415 37.028 71.039 1.00 93.77 ? 53 ARG A NE 1 ATOM 411 C CZ . ARG A 1 53 ? -16.439 38.223 70.447 1.00 95.43 ? 53 ARG A CZ 1 ATOM 412 N NH1 . ARG A 1 53 ? -17.480 39.043 70.585 1.00 95.35 ? 53 ARG A NH1 1 ATOM 413 N NH2 . ARG A 1 53 ? -15.409 38.607 69.706 1.00 97.50 ? 53 ARG A NH2 1 ATOM 414 N N . ASP A 1 54 ? -20.978 34.367 72.698 1.00 81.11 ? 54 ASP A N 1 ATOM 415 C CA . ASP A 1 54 ? -21.368 33.230 73.532 1.00 80.52 ? 54 ASP A CA 1 ATOM 416 C C . ASP A 1 54 ? -22.458 33.553 74.549 1.00 79.46 ? 54 ASP A C 1 ATOM 417 O O . ASP A 1 54 ? -22.957 32.647 75.213 1.00 79.27 ? 54 ASP A O 1 ATOM 418 C CB . ASP A 1 54 ? -20.151 32.672 74.261 1.00 82.92 ? 54 ASP A CB 1 ATOM 419 C CG . ASP A 1 54 ? -19.194 31.969 73.330 1.00 84.09 ? 54 ASP A CG 1 ATOM 420 O OD1 . ASP A 1 54 ? -19.656 31.130 72.526 1.00 81.24 ? 54 ASP A OD1 1 ATOM 421 O OD2 . ASP A 1 54 ? -17.980 32.250 73.411 1.00 85.84 ? 54 ASP A OD2 1 ATOM 422 N N . CYS A 1 55 ? -22.824 34.826 74.682 1.00 79.78 ? 55 CYS A N 1 ATOM 423 C CA . CYS A 1 55 ? -23.906 35.213 75.592 1.00 80.87 ? 55 CYS A CA 1 ATOM 424 C C . CYS A 1 55 ? -25.276 35.014 74.944 1.00 77.20 ? 55 CYS A C 1 ATOM 425 O O . CYS A 1 55 ? -25.417 35.108 73.728 1.00 79.07 ? 55 CYS A O 1 ATOM 426 C CB . CYS A 1 55 ? -23.748 36.667 76.061 1.00 82.45 ? 55 CYS A CB 1 ATOM 427 S SG . CYS A 1 55 ? -22.352 36.917 77.187 1.00 91.15 ? 55 CYS A SG 1 ATOM 428 N N . SER A 1 56 ? -26.274 34.721 75.771 1.00 73.84 ? 56 SER A N 1 ATOM 429 C CA . SER A 1 56 ? -27.661 34.687 75.338 1.00 71.87 ? 56 SER A CA 1 ATOM 430 C C . SER A 1 56 ? -28.333 36.013 75.668 1.00 71.78 ? 56 SER A C 1 ATOM 431 O O . SER A 1 56 ? -27.787 36.833 76.409 1.00 71.42 ? 56 SER A O 1 ATOM 432 C CB . SER A 1 56 ? -28.411 33.576 76.056 1.00 71.65 ? 56 SER A CB 1 ATOM 433 O OG . SER A 1 56 ? -28.798 34.008 77.347 1.00 72.27 ? 56 SER A OG 1 ATOM 434 N N . VAL A 1 57 ? -29.536 36.205 75.137 1.00 70.84 ? 57 VAL A N 1 ATOM 435 C CA . VAL A 1 57 ? -30.310 37.413 75.409 1.00 70.99 ? 57 VAL A CA 1 ATOM 436 C C . VAL A 1 57 ? -30.521 37.559 76.919 1.00 71.37 ? 57 VAL A C 1 ATOM 437 O O . VAL A 1 57 ? -30.385 38.658 77.463 1.00 71.50 ? 57 VAL A O 1 ATOM 438 C CB . VAL A 1 57 ? -31.667 37.398 74.669 1.00 70.37 ? 57 VAL A CB 1 ATOM 439 C CG1 . VAL A 1 57 ? -32.543 38.563 75.103 1.00 70.44 ? 57 VAL A CG1 1 ATOM 440 C CG2 . VAL A 1 57 ? -31.452 37.444 73.165 1.00 71.95 ? 57 VAL A CG2 1 ATOM 441 N N . ALA A 1 58 ? -30.840 36.446 77.583 1.00 70.58 ? 58 ALA A N 1 ATOM 442 C CA . ALA A 1 58 ? -30.985 36.408 79.044 1.00 69.34 ? 58 ALA A CA 1 ATOM 443 C C . ALA A 1 58 ? -29.692 36.816 79.757 1.00 70.10 ? 58 ALA A C 1 ATOM 444 O O . ALA A 1 58 ? -29.702 37.707 80.613 1.00 70.95 ? 58 ALA A O 1 ATOM 445 C CB . ALA A 1 58 ? -31.409 35.020 79.491 1.00 68.07 ? 58 ALA A CB 1 ATOM 446 N N . GLY A 1 59 ? -28.588 36.163 79.394 1.00 69.61 ? 59 GLY A N 1 ATOM 447 C CA . GLY A 1 59 ? -27.271 36.492 79.933 1.00 70.04 ? 59 GLY A CA 1 ATOM 448 C C . GLY A 1 59 ? -26.907 37.950 79.718 1.00 72.14 ? 59 GLY A C 1 ATOM 449 O O . GLY A 1 59 ? -26.242 38.556 80.550 1.00 76.16 ? 59 GLY A O 1 ATOM 450 N N . TRP A 1 60 ? -27.344 38.513 78.595 1.00 72.48 ? 60 TRP A N 1 ATOM 451 C CA . TRP A 1 60 ? -27.090 39.913 78.281 1.00 73.35 ? 60 TRP A CA 1 ATOM 452 C C . TRP A 1 60 ? -27.938 40.829 79.154 1.00 74.02 ? 60 TRP A C 1 ATOM 453 O O . TRP A 1 60 ? -27.407 41.713 79.821 1.00 76.40 ? 60 TRP A O 1 ATOM 454 C CB . TRP A 1 60 ? -27.351 40.179 76.786 1.00 74.61 ? 60 TRP A CB 1 ATOM 455 C CG . TRP A 1 60 ? -27.586 41.630 76.419 1.00 75.54 ? 60 TRP A CG 1 ATOM 456 C CD1 . TRP A 1 60 ? -26.930 42.722 76.912 1.00 77.39 ? 60 TRP A CD1 1 ATOM 457 C CD2 . TRP A 1 60 ? -28.529 42.130 75.459 1.00 74.59 ? 60 TRP A CD2 1 ATOM 458 N NE1 . TRP A 1 60 ? -27.418 43.871 76.333 1.00 77.76 ? 60 TRP A NE1 1 ATOM 459 C CE2 . TRP A 1 60 ? -28.400 43.536 75.439 1.00 75.36 ? 60 TRP A CE2 1 ATOM 460 C CE3 . TRP A 1 60 ? -29.472 41.527 74.617 1.00 72.92 ? 60 TRP A CE3 1 ATOM 461 C CZ2 . TRP A 1 60 ? -29.178 44.348 74.613 1.00 75.55 ? 60 TRP A CZ2 1 ATOM 462 C CZ3 . TRP A 1 60 ? -30.248 42.339 73.793 1.00 71.87 ? 60 TRP A CZ3 1 ATOM 463 C CH2 . TRP A 1 60 ? -30.093 43.732 73.797 1.00 73.53 ? 60 TRP A CH2 1 ATOM 464 N N . LEU A 1 61 ? -29.249 40.611 79.154 1.00 74.02 ? 61 LEU A N 1 ATOM 465 C CA . LEU A 1 61 ? -30.182 41.526 79.822 1.00 75.04 ? 61 LEU A CA 1 ATOM 466 C C . LEU A 1 61 ? -30.051 41.510 81.345 1.00 74.62 ? 61 LEU A C 1 ATOM 467 O O . LEU A 1 61 ? -29.950 42.561 81.974 1.00 73.30 ? 61 LEU A O 1 ATOM 468 C CB . LEU A 1 61 ? -31.628 41.224 79.412 1.00 74.71 ? 61 LEU A CB 1 ATOM 469 C CG . LEU A 1 61 ? -31.967 41.580 77.960 1.00 75.87 ? 61 LEU A CG 1 ATOM 470 C CD1 . LEU A 1 61 ? -33.369 41.103 77.612 1.00 76.78 ? 61 LEU A CD1 1 ATOM 471 C CD2 . LEU A 1 61 ? -31.834 43.074 77.700 1.00 76.47 ? 61 LEU A CD2 1 ATOM 472 N N . LEU A 1 62 ? -30.049 40.319 81.933 1.00 73.10 ? 62 LEU A N 1 ATOM 473 C CA . LEU A 1 62 ? -29.851 40.185 83.374 1.00 71.70 ? 62 LEU A CA 1 ATOM 474 C C . LEU A 1 62 ? -28.459 40.658 83.792 1.00 74.50 ? 62 LEU A C 1 ATOM 475 O O . LEU A 1 62 ? -28.256 41.080 84.929 1.00 73.56 ? 62 LEU A O 1 ATOM 476 C CB . LEU A 1 62 ? -30.061 38.740 83.809 1.00 69.22 ? 62 LEU A CB 1 ATOM 477 C CG . LEU A 1 62 ? -31.502 38.264 83.668 1.00 67.79 ? 62 LEU A CG 1 ATOM 478 C CD1 . LEU A 1 62 ? -31.564 36.751 83.744 1.00 67.95 ? 62 LEU A CD1 1 ATOM 479 C CD2 . LEU A 1 62 ? -32.397 38.894 84.725 1.00 67.78 ? 62 LEU A CD2 1 ATOM 480 N N . GLY A 1 63 ? -27.504 40.586 82.868 1.00 76.11 ? 63 GLY A N 1 ATOM 481 C CA . GLY A 1 63 ? -26.157 41.076 83.118 1.00 78.83 ? 63 GLY A CA 1 ATOM 482 C C . GLY A 1 63 ? -25.253 40.028 83.741 1.00 78.71 ? 63 GLY A C 1 ATOM 483 O O . GLY A 1 63 ? -24.574 40.300 84.728 1.00 80.10 ? 63 GLY A O 1 ATOM 484 N N . ASN A 1 64 ? -25.250 38.829 83.163 1.00 76.88 ? 64 ASN A N 1 ATOM 485 C CA . ASN A 1 64 ? -24.248 37.819 83.478 1.00 77.03 ? 64 ASN A CA 1 ATOM 486 C C . ASN A 1 64 ? -22.857 38.466 83.433 1.00 80.98 ? 64 ASN A C 1 ATOM 487 O O . ASN A 1 64 ? -22.545 39.190 82.485 1.00 82.27 ? 64 ASN A O 1 ATOM 488 C CB . ASN A 1 64 ? -24.354 36.668 82.471 1.00 75.55 ? 64 ASN A CB 1 ATOM 489 C CG . ASN A 1 64 ? -23.381 35.530 82.747 1.00 75.66 ? 64 ASN A CG 1 ATOM 490 O OD1 . ASN A 1 64 ? -22.219 35.748 83.083 1.00 75.62 ? 64 ASN A OD1 1 ATOM 491 N ND2 . ASN A 1 64 ? -23.852 34.300 82.567 1.00 75.33 ? 64 ASN A ND2 1 ATOM 492 N N . PRO A 1 65 ? -22.021 38.228 84.464 1.00 84.61 ? 65 PRO A N 1 ATOM 493 C CA . PRO A 1 65 ? -20.683 38.836 84.523 1.00 87.52 ? 65 PRO A CA 1 ATOM 494 C C . PRO A 1 65 ? -19.732 38.391 83.406 1.00 89.67 ? 65 PRO A C 1 ATOM 495 O O . PRO A 1 65 ? -18.727 39.059 83.160 1.00 92.61 ? 65 PRO A O 1 ATOM 496 C CB . PRO A 1 65 ? -20.151 38.381 85.885 1.00 87.65 ? 65 PRO A CB 1 ATOM 497 C CG . PRO A 1 65 ? -20.917 37.145 86.201 1.00 85.52 ? 65 PRO A CG 1 ATOM 498 C CD . PRO A 1 65 ? -22.285 37.393 85.648 1.00 83.53 ? 65 PRO A CD 1 ATOM 499 N N . MET A 1 66 ? -20.041 37.273 82.750 1.00 89.78 ? 66 MET A N 1 ATOM 500 C CA . MET A 1 66 ? -19.324 36.859 81.543 1.00 91.26 ? 66 MET A CA 1 ATOM 501 C C . MET A 1 66 ? -19.744 37.692 80.324 1.00 89.79 ? 66 MET A C 1 ATOM 502 O O . MET A 1 66 ? -19.116 37.607 79.270 1.00 88.55 ? 66 MET A O 1 ATOM 503 C CB . MET A 1 66 ? -19.569 35.370 81.260 1.00 91.98 ? 66 MET A CB 1 ATOM 504 C CG . MET A 1 66 ? -19.001 34.419 82.307 1.00 93.83 ? 66 MET A CG 1 ATOM 505 S SD . MET A 1 66 ? -17.205 34.259 82.197 1.00 99.04 ? 66 MET A SD 1 ATOM 506 C CE . MET A 1 66 ? -16.864 33.035 83.462 1.00 99.75 ? 66 MET A CE 1 ATOM 507 N N . CYS A 1 67 ? -20.798 38.496 80.479 1.00 88.00 ? 67 CYS A N 1 ATOM 508 C CA . CYS A 1 67 ? -21.364 39.295 79.394 1.00 86.40 ? 67 CYS A CA 1 ATOM 509 C C . CYS A 1 67 ? -21.124 40.788 79.598 1.00 85.95 ? 67 CYS A C 1 ATOM 510 O O . CYS A 1 67 ? -21.972 41.617 79.260 1.00 84.30 ? 67 CYS A O 1 ATOM 511 C CB . CYS A 1 67 ? -22.860 39.007 79.291 1.00 85.11 ? 67 CYS A CB 1 ATOM 512 S SG . CYS A 1 67 ? -23.195 37.255 79.023 1.00 86.34 ? 67 CYS A SG 1 ATOM 513 N N . ASP A 1 68 ? -19.955 41.126 80.134 1.00 86.89 ? 68 ASP A N 1 ATOM 514 C CA . ASP A 1 68 ? -19.581 42.521 80.347 1.00 88.35 ? 68 ASP A CA 1 ATOM 515 C C . ASP A 1 68 ? -19.401 43.275 79.031 1.00 89.20 ? 68 ASP A C 1 ATOM 516 O O . ASP A 1 68 ? -19.629 44.482 78.976 1.00 90.54 ? 68 ASP A O 1 ATOM 517 C CB . ASP A 1 68 ? -18.300 42.614 81.178 1.00 90.31 ? 68 ASP A CB 1 ATOM 518 C CG . ASP A 1 68 ? -18.512 42.217 82.626 1.00 89.97 ? 68 ASP A CG 1 ATOM 519 O OD1 . ASP A 1 68 ? -19.649 41.851 82.989 1.00 88.89 ? 68 ASP A OD1 1 ATOM 520 O OD2 . ASP A 1 68 ? -17.537 42.273 83.407 1.00 91.16 ? 68 ASP A OD2 1 ATOM 521 N N . GLU A 1 69 ? -18.997 42.565 77.977 1.00 88.23 ? 69 GLU A N 1 ATOM 522 C CA . GLU A 1 69 ? -18.893 43.145 76.631 1.00 87.80 ? 69 GLU A CA 1 ATOM 523 C C . GLU A 1 69 ? -20.178 43.862 76.227 1.00 85.70 ? 69 GLU A C 1 ATOM 524 O O . GLU A 1 69 ? -20.134 44.900 75.566 1.00 83.62 ? 69 GLU A O 1 ATOM 525 C CB . GLU A 1 69 ? -18.567 42.056 75.594 1.00 87.57 ? 69 GLU A CB 1 ATOM 526 C CG . GLU A 1 69 ? -18.355 42.574 74.172 1.00 88.06 ? 69 GLU A CG 1 ATOM 527 C CD . GLU A 1 69 ? -18.066 41.475 73.160 1.00 87.21 ? 69 GLU A CD 1 ATOM 528 O OE1 . GLU A 1 69 ? -17.966 40.292 73.557 1.00 87.58 ? 69 GLU A OE1 1 ATOM 529 O OE2 . GLU A 1 69 ? -17.943 41.799 71.959 1.00 85.87 ? 69 GLU A OE2 1 ATOM 530 N N . PHE A 1 70 ? -21.314 43.309 76.644 1.00 85.78 ? 70 PHE A N 1 ATOM 531 C CA . PHE A 1 70 ? -22.626 43.792 76.218 1.00 86.34 ? 70 PHE A CA 1 ATOM 532 C C . PHE A 1 70 ? -23.331 44.628 77.283 1.00 89.02 ? 70 PHE A C 1 ATOM 533 O O . PHE A 1 70 ? -24.560 44.696 77.319 1.00 88.04 ? 70 PHE A O 1 ATOM 534 C CB . PHE A 1 70 ? -23.476 42.599 75.791 1.00 82.82 ? 70 PHE A CB 1 ATOM 535 C CG . PHE A 1 70 ? -22.734 41.656 74.897 1.00 82.19 ? 70 PHE A CG 1 ATOM 536 C CD1 . PHE A 1 70 ? -22.420 42.031 73.599 1.00 80.53 ? 70 PHE A CD1 1 ATOM 537 C CD2 . PHE A 1 70 ? -22.284 40.431 75.369 1.00 82.07 ? 70 PHE A CD2 1 ATOM 538 C CE1 . PHE A 1 70 ? -21.711 41.184 72.772 1.00 80.59 ? 70 PHE A CE1 1 ATOM 539 C CE2 . PHE A 1 70 ? -21.571 39.577 74.543 1.00 82.38 ? 70 PHE A CE2 1 ATOM 540 C CZ . PHE A 1 70 ? -21.286 39.955 73.242 1.00 81.13 ? 70 PHE A CZ 1 ATOM 541 N N . ILE A 1 71 ? -22.536 45.262 78.141 1.00 93.75 ? 71 ILE A N 1 ATOM 542 C CA . ILE A 1 71 ? -23.029 46.262 79.073 1.00 96.92 ? 71 ILE A CA 1 ATOM 543 C C . ILE A 1 71 ? -23.060 47.584 78.301 1.00 100.09 ? 71 ILE A C 1 ATOM 544 O O . ILE A 1 71 ? -22.056 47.979 77.700 1.00 103.73 ? 71 ILE A O 1 ATOM 545 C CB . ILE A 1 71 ? -22.128 46.324 80.337 1.00 101.24 ? 71 ILE A CB 1 ATOM 546 C CG1 . ILE A 1 71 ? -22.873 46.948 81.517 1.00 102.12 ? 71 ILE A CG1 1 ATOM 547 C CG2 . ILE A 1 71 ? -20.813 47.061 80.081 1.00 103.09 ? 71 ILE A CG2 1 ATOM 548 C CD1 . ILE A 1 71 ? -22.112 46.851 82.822 1.00 101.94 ? 71 ILE A CD1 1 ATOM 549 N N . ASN A 1 72 ? -24.219 48.240 78.272 1.00 99.75 ? 72 ASN A N 1 ATOM 550 C CA . ASN A 1 72 ? -24.409 49.462 77.469 1.00 99.54 ? 72 ASN A CA 1 ATOM 551 C C . ASN A 1 72 ? -23.977 49.319 76.003 1.00 96.61 ? 72 ASN A C 1 ATOM 552 O O . ASN A 1 72 ? -22.946 49.854 75.593 1.00 98.24 ? 72 ASN A O 1 ATOM 553 C CB . ASN A 1 72 ? -23.678 50.643 78.115 1.00 101.99 ? 72 ASN A CB 1 ATOM 554 C CG . ASN A 1 72 ? -24.076 50.849 79.561 1.00 104.90 ? 72 ASN A CG 1 ATOM 555 O OD1 . ASN A 1 72 ? -25.128 50.382 80.002 1.00 103.67 ? 72 ASN A OD1 1 ATOM 556 N ND2 . ASN A 1 72 ? -23.232 51.545 80.311 1.00 109.13 ? 72 ASN A ND2 1 ATOM 557 N N . VAL A 1 73 ? -24.770 48.592 75.221 1.00 92.55 ? 73 VAL A N 1 ATOM 558 C CA . VAL A 1 73 ? -24.485 48.398 73.793 1.00 91.21 ? 73 VAL A CA 1 ATOM 559 C C . VAL A 1 73 ? -25.127 49.492 72.940 1.00 90.77 ? 73 VAL A C 1 ATOM 560 O O . VAL A 1 73 ? -26.222 49.964 73.257 1.00 90.42 ? 73 VAL A O 1 ATOM 561 C CB . VAL A 1 73 ? -24.977 47.026 73.279 1.00 88.21 ? 73 VAL A CB 1 ATOM 562 C CG1 . VAL A 1 73 ? -24.348 45.901 74.083 1.00 87.40 ? 73 VAL A CG1 1 ATOM 563 C CG2 . VAL A 1 73 ? -26.501 46.933 73.306 1.00 86.67 ? 73 VAL A CG2 1 ATOM 564 N N . PRO A 1 74 ? -24.459 49.888 71.840 1.00 90.79 ? 74 PRO A N 1 ATOM 565 C CA . PRO A 1 74 ? -25.034 50.911 70.970 1.00 90.45 ? 74 PRO A CA 1 ATOM 566 C C . PRO A 1 74 ? -26.185 50.364 70.127 1.00 88.13 ? 74 PRO A C 1 ATOM 567 O O . PRO A 1 74 ? -26.447 49.156 70.135 1.00 84.60 ? 74 PRO A O 1 ATOM 568 C CB . PRO A 1 74 ? -23.856 51.317 70.078 1.00 91.67 ? 74 PRO A CB 1 ATOM 569 C CG . PRO A 1 74 ? -23.005 50.097 70.005 1.00 91.30 ? 74 PRO A CG 1 ATOM 570 C CD . PRO A 1 74 ? -23.185 49.364 71.309 1.00 91.15 ? 74 PRO A CD 1 ATOM 571 N N . GLU A 1 75 ? -26.861 51.261 69.412 1.00 87.97 ? 75 GLU A N 1 ATOM 572 C CA . GLU A 1 75 ? -27.935 50.894 68.492 1.00 85.43 ? 75 GLU A CA 1 ATOM 573 C C . GLU A 1 75 ? -27.480 49.781 67.544 1.00 83.71 ? 75 GLU A C 1 ATOM 574 O O . GLU A 1 75 ? -26.353 49.798 67.052 1.00 81.66 ? 75 GLU A O 1 ATOM 575 C CB . GLU A 1 75 ? -28.374 52.123 67.688 1.00 86.89 ? 75 GLU A CB 1 ATOM 576 C CG . GLU A 1 75 ? -29.575 51.896 66.780 1.00 85.98 ? 75 GLU A CG 1 ATOM 577 C CD . GLU A 1 75 ? -29.928 53.110 65.939 1.00 86.35 ? 75 GLU A CD 1 ATOM 578 O OE1 . GLU A 1 75 ? -29.399 54.213 66.204 1.00 87.82 ? 75 GLU A OE1 1 ATOM 579 O OE2 . GLU A 1 75 ? -30.743 52.955 65.004 1.00 85.03 ? 75 GLU A OE2 1 ATOM 580 N N . TRP A 1 76 ? -28.360 48.810 67.310 1.00 83.16 ? 76 TRP A N 1 ATOM 581 C CA . TRP A 1 76 ? -28.063 47.693 66.412 1.00 83.31 ? 76 TRP A CA 1 ATOM 582 C C . TRP A 1 76 ? -29.059 47.638 65.253 1.00 82.15 ? 76 TRP A C 1 ATOM 583 O O . TRP A 1 76 ? -30.122 48.272 65.290 1.00 82.48 ? 76 TRP A O 1 ATOM 584 C CB . TRP A 1 76 ? -28.054 46.363 67.172 1.00 81.29 ? 76 TRP A CB 1 ATOM 585 C CG . TRP A 1 76 ? -29.370 46.015 67.776 1.00 82.20 ? 76 TRP A CG 1 ATOM 586 C CD1 . TRP A 1 76 ? -30.404 45.359 67.171 1.00 83.13 ? 76 TRP A CD1 1 ATOM 587 C CD2 . TRP A 1 76 ? -29.802 46.301 69.108 1.00 82.89 ? 76 TRP A CD2 1 ATOM 588 N NE1 . TRP A 1 76 ? -31.457 45.222 68.047 1.00 82.34 ? 76 TRP A NE1 1 ATOM 589 C CE2 . TRP A 1 76 ? -31.111 45.792 69.243 1.00 82.18 ? 76 TRP A CE2 1 ATOM 590 C CE3 . TRP A 1 76 ? -29.210 46.937 70.202 1.00 84.00 ? 76 TRP A CE3 1 ATOM 591 C CZ2 . TRP A 1 76 ? -31.835 45.902 70.426 1.00 81.85 ? 76 TRP A CZ2 1 ATOM 592 C CZ3 . TRP A 1 76 ? -29.931 47.047 71.375 1.00 84.08 ? 76 TRP A CZ3 1 ATOM 593 C CH2 . TRP A 1 76 ? -31.230 46.533 71.478 1.00 83.25 ? 76 TRP A CH2 1 ATOM 594 N N . SER A 1 77 ? -28.687 46.887 64.220 1.00 79.90 ? 77 SER A N 1 ATOM 595 C CA . SER A 1 77 ? -29.534 46.676 63.046 1.00 78.49 ? 77 SER A CA 1 ATOM 596 C C . SER A 1 77 ? -30.321 45.386 63.222 1.00 76.90 ? 77 SER A C 1 ATOM 597 O O . SER A 1 77 ? -31.533 45.336 63.003 1.00 76.73 ? 77 SER A O 1 ATOM 598 C CB . SER A 1 77 ? -28.670 46.573 61.795 1.00 77.47 ? 77 SER A CB 1 ATOM 599 O OG . SER A 1 77 ? -27.554 45.721 62.011 1.00 75.58 ? 77 SER A OG 1 ATOM 600 N N . TYR A 1 78 ? -29.596 44.342 63.602 1.00 74.63 ? 78 TYR A N 1 ATOM 601 C CA . TYR A 1 78 ? -30.185 43.071 63.970 1.00 71.67 ? 78 TYR A CA 1 ATOM 602 C C . TYR A 1 78 ? -29.342 42.468 65.092 1.00 72.63 ? 78 TYR A C 1 ATOM 603 O O . TYR A 1 78 ? -28.249 42.953 65.391 1.00 73.33 ? 78 TYR A O 1 ATOM 604 C CB . TYR A 1 78 ? -30.274 42.132 62.748 1.00 69.00 ? 78 TYR A CB 1 ATOM 605 C CG . TYR A 1 78 ? -28.952 41.833 62.059 1.00 66.89 ? 78 TYR A CG 1 ATOM 606 C CD1 . TYR A 1 78 ? -28.406 42.716 61.126 1.00 66.58 ? 78 TYR A CD1 1 ATOM 607 C CD2 . TYR A 1 78 ? -28.252 40.665 62.338 1.00 65.69 ? 78 TYR A CD2 1 ATOM 608 C CE1 . TYR A 1 78 ? -27.191 42.446 60.502 1.00 66.20 ? 78 TYR A CE1 1 ATOM 609 C CE2 . TYR A 1 78 ? -27.043 40.384 61.719 1.00 65.88 ? 78 TYR A CE2 1 ATOM 610 C CZ . TYR A 1 78 ? -26.511 41.277 60.801 1.00 65.99 ? 78 TYR A CZ 1 ATOM 611 O OH . TYR A 1 78 ? -25.306 40.978 60.193 1.00 64.27 ? 78 TYR A OH 1 ATOM 612 N N . ILE A 1 79 ? -29.868 41.427 65.723 1.00 71.94 ? 79 ILE A N 1 ATOM 613 C CA . ILE A 1 79 ? -29.165 40.732 66.785 1.00 70.57 ? 79 ILE A CA 1 ATOM 614 C C . ILE A 1 79 ? -28.775 39.354 66.273 1.00 69.69 ? 79 ILE A C 1 ATOM 615 O O . ILE A 1 79 ? -29.528 38.732 65.527 1.00 67.67 ? 79 ILE A O 1 ATOM 616 C CB . ILE A 1 79 ? -30.061 40.586 68.029 1.00 71.19 ? 79 ILE A CB 1 ATOM 617 C CG1 . ILE A 1 79 ? -30.411 41.966 68.598 1.00 73.38 ? 79 ILE A CG1 1 ATOM 618 C CG2 . ILE A 1 79 ? -29.381 39.729 69.088 1.00 71.55 ? 79 ILE A CG2 1 ATOM 619 C CD1 . ILE A 1 79 ? -31.476 41.937 69.676 1.00 73.52 ? 79 ILE A CD1 1 ATOM 620 N N . VAL A 1 80 ? -27.598 38.882 66.673 1.00 70.49 ? 80 VAL A N 1 ATOM 621 C CA . VAL A 1 80 ? -27.161 37.523 66.365 1.00 69.83 ? 80 VAL A CA 1 ATOM 622 C C . VAL A 1 80 ? -26.942 36.751 67.666 1.00 69.30 ? 80 VAL A C 1 ATOM 623 O O . VAL A 1 80 ? -26.431 37.296 68.635 1.00 69.26 ? 80 VAL A O 1 ATOM 624 C CB . VAL A 1 80 ? -25.867 37.522 65.534 1.00 70.27 ? 80 VAL A CB 1 ATOM 625 C CG1 . VAL A 1 80 ? -25.496 36.106 65.110 1.00 69.86 ? 80 VAL A CG1 1 ATOM 626 C CG2 . VAL A 1 80 ? -26.030 38.423 64.323 1.00 71.00 ? 80 VAL A CG2 1 ATOM 627 N N . GLU A 1 81 ? -27.333 35.483 67.668 1.00 68.39 ? 81 GLU A N 1 ATOM 628 C CA . GLU A 1 81 ? -27.264 34.642 68.849 1.00 69.45 ? 81 GLU A CA 1 ATOM 629 C C . GLU A 1 81 ? -26.935 33.229 68.403 1.00 70.34 ? 81 GLU A C 1 ATOM 630 O O . GLU A 1 81 ? -27.472 32.754 67.407 1.00 71.57 ? 81 GLU A O 1 ATOM 631 C CB . GLU A 1 81 ? -28.611 34.655 69.582 1.00 69.56 ? 81 GLU A CB 1 ATOM 632 C CG . GLU A 1 81 ? -28.648 33.834 70.864 1.00 70.98 ? 81 GLU A CG 1 ATOM 633 C CD . GLU A 1 81 ? -29.979 33.919 71.598 1.00 71.42 ? 81 GLU A CD 1 ATOM 634 O OE1 . GLU A 1 81 ? -31.039 33.761 70.952 1.00 70.96 ? 81 GLU A OE1 1 ATOM 635 O OE2 . GLU A 1 81 ? -29.964 34.144 72.831 1.00 70.92 ? 81 GLU A OE2 1 ATOM 636 N N . LYS A 1 82 ? -26.057 32.552 69.131 1.00 71.71 ? 82 LYS A N 1 ATOM 637 C CA . LYS A 1 82 ? -25.744 31.166 68.813 1.00 73.08 ? 82 LYS A CA 1 ATOM 638 C C . LYS A 1 82 ? -26.927 30.254 69.141 1.00 73.01 ? 82 LYS A C 1 ATOM 639 O O . LYS A 1 82 ? -27.858 30.643 69.858 1.00 69.68 ? 82 LYS A O 1 ATOM 640 C CB . LYS A 1 82 ? -24.483 30.710 69.547 1.00 74.56 ? 82 LYS A CB 1 ATOM 641 C CG . LYS A 1 82 ? -23.211 31.300 68.961 1.00 76.43 ? 82 LYS A CG 1 ATOM 642 C CD . LYS A 1 82 ? -21.967 30.710 69.603 1.00 78.16 ? 82 LYS A CD 1 ATOM 643 C CE . LYS A 1 82 ? -20.733 30.923 68.739 1.00 80.95 ? 82 LYS A CE 1 ATOM 644 N NZ . LYS A 1 82 ? -20.447 32.364 68.501 1.00 82.84 ? 82 LYS A NZ 1 ATOM 645 N N . ALA A 1 83 ? -26.892 29.044 68.589 1.00 74.35 ? 83 ALA A N 1 ATOM 646 C CA . ALA A 1 83 ? -27.930 28.048 68.844 1.00 75.07 ? 83 ALA A CA 1 ATOM 647 C C . ALA A 1 83 ? -27.963 27.631 70.321 1.00 75.95 ? 83 ALA A C 1 ATOM 648 O O . ALA A 1 83 ? -29.038 27.505 70.912 1.00 74.40 ? 83 ALA A O 1 ATOM 649 C CB . ALA A 1 83 ? -27.722 26.832 67.951 1.00 74.94 ? 83 ALA A CB 1 ATOM 650 N N . ASN A 1 84 ? -26.780 27.426 70.903 1.00 76.99 ? 84 ASN A N 1 ATOM 651 C CA . ASN A 1 84 ? -26.648 27.024 72.305 1.00 77.75 ? 84 ASN A CA 1 ATOM 652 C C . ASN A 1 84 ? -25.567 27.838 73.014 1.00 76.43 ? 84 ASN A C 1 ATOM 653 O O . ASN A 1 84 ? -24.468 27.334 73.258 1.00 76.58 ? 84 ASN A O 1 ATOM 654 C CB . ASN A 1 84 ? -26.336 25.527 72.395 1.00 81.12 ? 84 ASN A CB 1 ATOM 655 C CG . ASN A 1 84 ? -27.455 24.668 71.830 1.00 83.39 ? 84 ASN A CG 1 ATOM 656 O OD1 . ASN A 1 84 ? -28.564 24.643 72.368 1.00 84.28 ? 84 ASN A OD1 1 ATOM 657 N ND2 . ASN A 1 84 ? -27.173 23.965 70.733 1.00 83.31 ? 84 ASN A ND2 1 ATOM 658 N N . PRO A 1 85 ? -25.875 29.104 73.350 1.00 74.38 ? 85 PRO A N 1 ATOM 659 C CA . PRO A 1 85 ? -24.873 29.968 73.970 1.00 75.43 ? 85 PRO A CA 1 ATOM 660 C C . PRO A 1 85 ? -24.515 29.492 75.374 1.00 75.34 ? 85 PRO A C 1 ATOM 661 O O . PRO A 1 85 ? -25.413 29.224 76.173 1.00 74.83 ? 85 PRO A O 1 ATOM 662 C CB . PRO A 1 85 ? -25.563 31.345 74.019 1.00 74.81 ? 85 PRO A CB 1 ATOM 663 C CG . PRO A 1 85 ? -26.795 31.224 73.186 1.00 72.04 ? 85 PRO A CG 1 ATOM 664 C CD . PRO A 1 85 ? -27.176 29.782 73.234 1.00 71.95 ? 85 PRO A CD 1 ATOM 665 N N . VAL A 1 86 ? -23.219 29.389 75.664 1.00 76.95 ? 86 VAL A N 1 ATOM 666 C CA . VAL A 1 86 ? -22.758 28.858 76.957 1.00 78.23 ? 86 VAL A CA 1 ATOM 667 C C . VAL A 1 86 ? -23.065 29.787 78.136 1.00 77.34 ? 86 VAL A C 1 ATOM 668 O O . VAL A 1 86 ? -23.359 29.313 79.234 1.00 77.34 ? 86 VAL A O 1 ATOM 669 C CB . VAL A 1 86 ? -21.243 28.530 76.957 1.00 79.54 ? 86 VAL A CB 1 ATOM 670 C CG1 . VAL A 1 86 ? -20.896 27.590 75.806 1.00 79.79 ? 86 VAL A CG1 1 ATOM 671 C CG2 . VAL A 1 86 ? -20.400 29.799 76.905 1.00 80.66 ? 86 VAL A CG2 1 ATOM 672 N N . ASN A 1 87 ? -22.996 31.098 77.902 1.00 76.61 ? 87 ASN A N 1 ATOM 673 C CA . ASN A 1 87 ? -23.219 32.096 78.947 1.00 77.28 ? 87 ASN A CA 1 ATOM 674 C C . ASN A 1 87 ? -24.673 32.545 78.996 1.00 76.11 ? 87 ASN A C 1 ATOM 675 O O . ASN A 1 87 ? -25.007 33.678 78.644 1.00 77.26 ? 87 ASN A O 1 ATOM 676 C CB . ASN A 1 87 ? -22.292 33.303 78.752 1.00 78.91 ? 87 ASN A CB 1 ATOM 677 C CG . ASN A 1 87 ? -20.840 32.982 79.060 1.00 81.57 ? 87 ASN A CG 1 ATOM 678 O OD1 . ASN A 1 87 ? -20.538 32.246 80.001 1.00 82.66 ? 87 ASN A OD1 1 ATOM 679 N ND2 . ASN A 1 87 ? -19.931 33.543 78.274 1.00 83.62 ? 87 ASN A ND2 1 ATOM 680 N N . ASP A 1 88 ? -25.534 31.640 79.445 1.00 75.14 ? 88 ASP A N 1 ATOM 681 C CA . ASP A 1 88 ? -26.953 31.918 79.590 1.00 73.38 ? 88 ASP A CA 1 ATOM 682 C C . ASP A 1 88 ? -27.183 32.353 81.049 1.00 73.62 ? 88 ASP A C 1 ATOM 683 O O . ASP A 1 88 ? -26.571 33.325 81.498 1.00 72.16 ? 88 ASP A O 1 ATOM 684 C CB . ASP A 1 88 ? -27.767 30.677 79.174 1.00 72.33 ? 88 ASP A CB 1 ATOM 685 C CG . ASP A 1 88 ? -29.238 30.982 78.925 1.00 71.74 ? 88 ASP A CG 1 ATOM 686 O OD1 . ASP A 1 88 ? -29.632 32.162 78.978 1.00 70.90 ? 88 ASP A OD1 1 ATOM 687 O OD2 . ASP A 1 88 ? -30.009 30.032 78.674 1.00 74.13 ? 88 ASP A OD2 1 ATOM 688 N N . LEU A 1 89 ? -28.048 31.648 81.779 1.00 73.31 ? 89 LEU A N 1 ATOM 689 C CA . LEU A 1 89 ? -28.238 31.885 83.202 1.00 73.72 ? 89 LEU A CA 1 ATOM 690 C C . LEU A 1 89 ? -27.160 31.136 83.981 1.00 75.58 ? 89 LEU A C 1 ATOM 691 O O . LEU A 1 89 ? -27.272 29.928 84.203 1.00 74.10 ? 89 LEU A O 1 ATOM 692 C CB . LEU A 1 89 ? -29.626 31.407 83.644 1.00 72.66 ? 89 LEU A CB 1 ATOM 693 C CG . LEU A 1 89 ? -30.839 31.991 82.911 1.00 71.49 ? 89 LEU A CG 1 ATOM 694 C CD1 . LEU A 1 89 ? -32.128 31.415 83.481 1.00 71.27 ? 89 LEU A CD1 1 ATOM 695 C CD2 . LEU A 1 89 ? -30.853 33.509 82.985 1.00 71.02 ? 89 LEU A CD2 1 ATOM 696 N N . CYS A 1 90 ? -26.115 31.864 84.374 1.00 78.93 ? 90 CYS A N 1 ATOM 697 C CA . CYS A 1 90 ? -25.012 31.318 85.170 1.00 82.49 ? 90 CYS A CA 1 ATOM 698 C C . CYS A 1 90 ? -25.537 30.613 86.419 1.00 78.33 ? 90 CYS A C 1 ATOM 699 O O . CYS A 1 90 ? -25.213 29.452 86.662 1.00 77.71 ? 90 CYS A O 1 ATOM 700 C CB . CYS A 1 90 ? -24.031 32.431 85.564 1.00 88.65 ? 90 CYS A CB 1 ATOM 701 S SG . CYS A 1 90 ? -24.849 33.952 86.111 1.00 95.22 ? 90 CYS A SG 1 ATOM 702 N N . TYR A 1 91 ? -26.346 31.317 87.203 1.00 76.02 ? 91 TYR A N 1 ATOM 703 C CA . TYR A 1 91 ? -27.052 30.702 88.319 1.00 76.58 ? 91 TYR A CA 1 ATOM 704 C C . TYR A 1 91 ? -28.287 30.022 87.753 1.00 74.18 ? 91 TYR A C 1 ATOM 705 O O . TYR A 1 91 ? -29.125 30.692 87.161 1.00 74.10 ? 91 TYR A O 1 ATOM 706 C CB . TYR A 1 91 ? -27.460 31.748 89.361 1.00 77.96 ? 91 TYR A CB 1 ATOM 707 C CG . TYR A 1 91 ? -27.897 31.155 90.691 1.00 78.93 ? 91 TYR A CG 1 ATOM 708 C CD1 . TYR A 1 91 ? -29.142 30.546 90.831 1.00 78.16 ? 91 TYR A CD1 1 ATOM 709 C CD2 . TYR A 1 91 ? -27.060 31.198 91.808 1.00 79.00 ? 91 TYR A CD2 1 ATOM 710 C CE1 . TYR A 1 91 ? -29.542 30.004 92.042 1.00 79.34 ? 91 TYR A CE1 1 ATOM 711 C CE2 . TYR A 1 91 ? -27.453 30.658 93.023 1.00 78.50 ? 91 TYR A CE2 1 ATOM 712 C CZ . TYR A 1 91 ? -28.695 30.063 93.135 1.00 78.84 ? 91 TYR A CZ 1 ATOM 713 O OH . TYR A 1 91 ? -29.095 29.524 94.336 1.00 78.42 ? 91 TYR A OH 1 ATOM 714 N N . PRO A 1 92 ? -28.423 28.699 87.952 1.00 74.62 ? 92 PRO A N 1 ATOM 715 C CA . PRO A 1 92 ? -29.480 27.948 87.268 1.00 74.22 ? 92 PRO A CA 1 ATOM 716 C C . PRO A 1 92 ? -30.885 28.477 87.564 1.00 75.31 ? 92 PRO A C 1 ATOM 717 O O . PRO A 1 92 ? -31.129 29.015 88.643 1.00 78.28 ? 92 PRO A O 1 ATOM 718 C CB . PRO A 1 92 ? -29.310 26.532 87.824 1.00 74.15 ? 92 PRO A CB 1 ATOM 719 C CG . PRO A 1 92 ? -28.720 26.734 89.175 1.00 74.84 ? 92 PRO A CG 1 ATOM 720 C CD . PRO A 1 92 ? -27.775 27.886 88.998 1.00 75.93 ? 92 PRO A CD 1 ATOM 721 N N . GLY A 1 93 ? -31.802 28.334 86.613 1.00 76.32 ? 93 GLY A N 1 ATOM 722 C CA . GLY A 1 93 ? -33.162 28.802 86.831 1.00 76.47 ? 93 GLY A CA 1 ATOM 723 C C . GLY A 1 93 ? -34.059 28.841 85.612 1.00 75.11 ? 93 GLY A C 1 ATOM 724 O O . GLY A 1 93 ? -33.989 27.973 84.744 1.00 74.60 ? 93 GLY A O 1 ATOM 725 N N . ASP A 1 94 ? -34.926 29.850 85.577 1.00 74.51 ? 94 ASP A N 1 ATOM 726 C CA . ASP A 1 94 ? -35.854 30.061 84.473 1.00 72.94 ? 94 ASP A CA 1 ATOM 727 C C . ASP A 1 94 ? -36.015 31.547 84.219 1.00 71.75 ? 94 ASP A C 1 ATOM 728 O O . ASP A 1 94 ? -35.874 32.368 85.133 1.00 72.61 ? 94 ASP A O 1 ATOM 729 C CB . ASP A 1 94 ? -37.227 29.476 84.795 1.00 73.78 ? 94 ASP A CB 1 ATOM 730 C CG . ASP A 1 94 ? -37.210 27.970 84.896 1.00 75.67 ? 94 ASP A CG 1 ATOM 731 O OD1 . ASP A 1 94 ? -36.983 27.308 83.860 1.00 74.69 ? 94 ASP A OD1 1 ATOM 732 O OD2 . ASP A 1 94 ? -37.429 27.450 86.013 1.00 78.55 ? 94 ASP A OD2 1 ATOM 733 N N . PHE A 1 95 ? -36.311 31.881 82.968 1.00 68.07 ? 95 PHE A N 1 ATOM 734 C CA . PHE A 1 95 ? -36.669 33.231 82.589 1.00 64.38 ? 95 PHE A CA 1 ATOM 735 C C . PHE A 1 95 ? -38.127 33.183 82.152 1.00 62.74 ? 95 PHE A C 1 ATOM 736 O O . PHE A 1 95 ? -38.456 32.580 81.139 1.00 62.49 ? 95 PHE A O 1 ATOM 737 C CB . PHE A 1 95 ? -35.765 33.701 81.463 1.00 64.14 ? 95 PHE A CB 1 ATOM 738 C CG . PHE A 1 95 ? -35.650 35.191 81.352 1.00 64.60 ? 95 PHE A CG 1 ATOM 739 C CD1 . PHE A 1 95 ? -36.766 35.976 81.107 1.00 64.54 ? 95 PHE A CD1 1 ATOM 740 C CD2 . PHE A 1 95 ? -34.416 35.811 81.480 1.00 65.08 ? 95 PHE A CD2 1 ATOM 741 C CE1 . PHE A 1 95 ? -36.653 37.351 80.997 1.00 65.71 ? 95 PHE A CE1 1 ATOM 742 C CE2 . PHE A 1 95 ? -34.299 37.184 81.372 1.00 65.93 ? 95 PHE A CE2 1 ATOM 743 C CZ . PHE A 1 95 ? -35.419 37.956 81.133 1.00 66.04 ? 95 PHE A CZ 1 ATOM 744 N N . ASN A 1 96 ? -38.998 33.799 82.940 1.00 62.45 ? 96 ASN A N 1 ATOM 745 C CA . ASN A 1 96 ? -40.434 33.773 82.693 1.00 61.84 ? 96 ASN A CA 1 ATOM 746 C C . ASN A 1 96 ? -40.816 34.567 81.446 1.00 61.41 ? 96 ASN A C 1 ATOM 747 O O . ASN A 1 96 ? -40.308 35.669 81.237 1.00 59.73 ? 96 ASN A O 1 ATOM 748 C CB . ASN A 1 96 ? -41.161 34.348 83.906 1.00 63.85 ? 96 ASN A CB 1 ATOM 749 C CG . ASN A 1 96 ? -42.652 34.115 83.856 1.00 64.74 ? 96 ASN A CG 1 ATOM 750 O OD1 . ASN A 1 96 ? -43.115 32.971 83.905 1.00 64.30 ? 96 ASN A OD1 1 ATOM 751 N ND2 . ASN A 1 96 ? -43.417 35.202 83.768 1.00 65.64 ? 96 ASN A ND2 1 ATOM 752 N N . ASP A 1 97 ? -41.718 34.000 80.638 1.00 62.33 ? 97 ASP A N 1 ATOM 753 C CA . ASP A 1 97 ? -42.163 34.591 79.356 1.00 62.72 ? 97 ASP A CA 1 ATOM 754 C C . ASP A 1 97 ? -40.997 35.089 78.488 1.00 61.04 ? 97 ASP A C 1 ATOM 755 O O . ASP A 1 97 ? -41.048 36.182 77.919 1.00 62.31 ? 97 ASP A O 1 ATOM 756 C CB . ASP A 1 97 ? -43.187 35.716 79.596 1.00 65.11 ? 97 ASP A CB 1 ATOM 757 C CG . ASP A 1 97 ? -44.570 35.189 79.966 1.00 66.64 ? 97 ASP A CG 1 ATOM 758 O OD1 . ASP A 1 97 ? -44.966 34.122 79.456 1.00 67.83 ? 97 ASP A OD1 1 ATOM 759 O OD2 . ASP A 1 97 ? -45.275 35.856 80.755 1.00 68.84 ? 97 ASP A OD2 1 ATOM 760 N N . TYR A 1 98 ? -39.960 34.261 78.391 1.00 58.60 ? 98 TYR A N 1 ATOM 761 C CA . TYR A 1 98 ? -38.698 34.618 77.737 1.00 57.76 ? 98 TYR A CA 1 ATOM 762 C C . TYR A 1 98 ? -38.855 34.826 76.239 1.00 58.51 ? 98 TYR A C 1 ATOM 763 O O . TYR A 1 98 ? -38.249 35.728 75.658 1.00 58.05 ? 98 TYR A O 1 ATOM 764 C CB . TYR A 1 98 ? -37.688 33.499 77.985 1.00 56.60 ? 98 TYR A CB 1 ATOM 765 C CG . TYR A 1 98 ? -36.283 33.745 77.497 1.00 55.80 ? 98 TYR A CG 1 ATOM 766 C CD1 . TYR A 1 98 ? -35.624 34.934 77.780 1.00 56.32 ? 98 TYR A CD1 1 ATOM 767 C CD2 . TYR A 1 98 ? -35.589 32.757 76.791 1.00 55.27 ? 98 TYR A CD2 1 ATOM 768 C CE1 . TYR A 1 98 ? -34.325 35.149 77.348 1.00 57.16 ? 98 TYR A CE1 1 ATOM 769 C CE2 . TYR A 1 98 ? -34.291 32.959 76.358 1.00 55.05 ? 98 TYR A CE2 1 ATOM 770 C CZ . TYR A 1 98 ? -33.664 34.153 76.642 1.00 56.74 ? 98 TYR A CZ 1 ATOM 771 O OH . TYR A 1 98 ? -32.378 34.369 76.226 1.00 58.11 ? 98 TYR A OH 1 ATOM 772 N N . GLU A 1 99 ? -39.669 33.982 75.618 1.00 59.89 ? 99 GLU A N 1 ATOM 773 C CA . GLU A 1 99 ? -39.881 34.052 74.178 1.00 61.47 ? 99 GLU A CA 1 ATOM 774 C C . GLU A 1 99 ? -40.699 35.293 73.827 1.00 61.76 ? 99 GLU A C 1 ATOM 775 O O . GLU A 1 99 ? -40.400 35.984 72.854 1.00 61.96 ? 99 GLU A O 1 ATOM 776 C CB . GLU A 1 99 ? -40.560 32.782 73.663 1.00 61.77 ? 99 GLU A CB 1 ATOM 777 C CG . GLU A 1 99 ? -39.649 31.553 73.638 1.00 63.11 ? 99 GLU A CG 1 ATOM 778 C CD . GLU A 1 99 ? -39.319 30.999 75.017 1.00 64.16 ? 99 GLU A CD 1 ATOM 779 O OE1 . GLU A 1 99 ? -40.167 31.086 75.933 1.00 66.07 ? 99 GLU A OE1 1 ATOM 780 O OE2 . GLU A 1 99 ? -38.202 30.471 75.184 1.00 64.20 ? 99 GLU A OE2 1 ATOM 781 N N . GLU A 1 100 ? -41.715 35.582 74.637 1.00 61.65 ? 100 GLU A N 1 ATOM 782 C CA . GLU A 1 100 ? -42.517 36.788 74.457 1.00 61.38 ? 100 GLU A CA 1 ATOM 783 C C . GLU A 1 100 ? -41.655 38.037 74.579 1.00 61.53 ? 100 GLU A C 1 ATOM 784 O O . GLU A 1 100 ? -41.932 39.051 73.938 1.00 63.34 ? 100 GLU A O 1 ATOM 785 C CB . GLU A 1 100 ? -43.669 36.836 75.460 1.00 61.23 ? 100 GLU A CB 1 ATOM 786 C CG . GLU A 1 100 ? -44.828 35.913 75.108 1.00 61.80 ? 100 GLU A CG 1 ATOM 787 C CD . GLU A 1 100 ? -45.651 36.407 73.929 1.00 61.78 ? 100 GLU A CD 1 ATOM 788 O OE1 . GLU A 1 100 ? -46.025 37.594 73.927 1.00 63.17 ? 100 GLU A OE1 1 ATOM 789 O OE2 . GLU A 1 100 ? -45.938 35.613 73.006 1.00 60.53 ? 100 GLU A OE2 1 ATOM 790 N N . LEU A 1 101 ? -40.610 37.964 75.393 1.00 59.95 ? 101 LEU A N 1 ATOM 791 C CA . LEU A 1 101 ? -39.680 39.076 75.508 1.00 60.98 ? 101 LEU A CA 1 ATOM 792 C C . LEU A 1 101 ? -38.820 39.162 74.253 1.00 60.62 ? 101 LEU A C 1 ATOM 793 O O . LEU A 1 101 ? -38.704 40.224 73.641 1.00 59.76 ? 101 LEU A O 1 ATOM 794 C CB . LEU A 1 101 ? -38.805 38.926 76.754 1.00 60.74 ? 101 LEU A CB 1 ATOM 795 C CG . LEU A 1 101 ? -37.815 40.058 77.026 1.00 61.45 ? 101 LEU A CG 1 ATOM 796 C CD1 . LEU A 1 101 ? -38.488 41.426 76.980 1.00 61.01 ? 101 LEU A CD1 1 ATOM 797 C CD2 . LEU A 1 101 ? -37.153 39.819 78.376 1.00 63.37 ? 101 LEU A CD2 1 ATOM 798 N N . LYS A 1 102 ? -38.221 38.037 73.872 1.00 60.43 ? 102 LYS A N 1 ATOM 799 C CA . LYS A 1 102 ? -37.459 37.956 72.627 1.00 60.63 ? 102 LYS A CA 1 ATOM 800 C C . LYS A 1 102 ? -38.241 38.520 71.439 1.00 60.41 ? 102 LYS A C 1 ATOM 801 O O . LYS A 1 102 ? -37.677 39.169 70.561 1.00 61.64 ? 102 LYS A O 1 ATOM 802 C CB . LYS A 1 102 ? -37.066 36.511 72.340 1.00 61.73 ? 102 LYS A CB 1 ATOM 803 C CG . LYS A 1 102 ? -35.829 36.043 73.085 1.00 63.72 ? 102 LYS A CG 1 ATOM 804 C CD . LYS A 1 102 ? -35.497 34.604 72.722 1.00 65.06 ? 102 LYS A CD 1 ATOM 805 C CE . LYS A 1 102 ? -34.021 34.304 72.919 1.00 67.66 ? 102 LYS A CE 1 ATOM 806 N NZ . LYS A 1 102 ? -33.646 32.970 72.374 1.00 68.71 ? 102 LYS A NZ 1 ATOM 807 N N . HIS A 1 103 ? -39.542 38.268 71.416 1.00 60.05 ? 103 HIS A N 1 ATOM 808 C CA . HIS A 1 103 ? -40.393 38.807 70.376 1.00 60.15 ? 103 HIS A CA 1 ATOM 809 C C . HIS A 1 103 ? -40.434 40.330 70.412 1.00 62.30 ? 103 HIS A C 1 ATOM 810 O O . HIS A 1 103 ? -40.460 40.971 69.364 1.00 64.50 ? 103 HIS A O 1 ATOM 811 C CB . HIS A 1 103 ? -41.806 38.256 70.506 1.00 59.77 ? 103 HIS A CB 1 ATOM 812 C CG . HIS A 1 103 ? -42.720 38.694 69.409 1.00 58.97 ? 103 HIS A CG 1 ATOM 813 N ND1 . HIS A 1 103 ? -42.799 38.036 68.201 1.00 58.51 ? 103 HIS A ND1 1 ATOM 814 C CD2 . HIS A 1 103 ? -43.582 39.734 69.332 1.00 59.11 ? 103 HIS A CD2 1 ATOM 815 C CE1 . HIS A 1 103 ? -43.680 38.647 67.430 1.00 59.22 ? 103 HIS A CE1 1 ATOM 816 N NE2 . HIS A 1 103 ? -44.171 39.679 68.094 1.00 59.73 ? 103 HIS A NE2 1 ATOM 817 N N . LEU A 1 104 ? -40.462 40.903 71.612 1.00 63.59 ? 104 LEU A N 1 ATOM 818 C CA . LEU A 1 104 ? -40.421 42.358 71.760 1.00 66.39 ? 104 LEU A CA 1 ATOM 819 C C . LEU A 1 104 ? -39.135 42.950 71.193 1.00 67.66 ? 104 LEU A C 1 ATOM 820 O O . LEU A 1 104 ? -39.161 44.025 70.601 1.00 67.82 ? 104 LEU A O 1 ATOM 821 C CB . LEU A 1 104 ? -40.584 42.779 73.227 1.00 68.15 ? 104 LEU A CB 1 ATOM 822 C CG . LEU A 1 104 ? -41.967 43.271 73.653 1.00 69.06 ? 104 LEU A CG 1 ATOM 823 C CD1 . LEU A 1 104 ? -43.056 42.256 73.347 1.00 69.73 ? 104 LEU A CD1 1 ATOM 824 C CD2 . LEU A 1 104 ? -41.940 43.582 75.138 1.00 70.53 ? 104 LEU A CD2 1 ATOM 825 N N . LEU A 1 105 ? -38.021 42.241 71.376 1.00 69.73 ? 105 LEU A N 1 ATOM 826 C CA . LEU A 1 105 ? -36.713 42.674 70.866 1.00 70.91 ? 105 LEU A CA 1 ATOM 827 C C . LEU A 1 105 ? -36.624 42.740 69.355 1.00 72.26 ? 105 LEU A C 1 ATOM 828 O O . LEU A 1 105 ? -35.813 43.498 68.815 1.00 74.81 ? 105 LEU A O 1 ATOM 829 C CB . LEU A 1 105 ? -35.612 41.728 71.329 1.00 70.04 ? 105 LEU A CB 1 ATOM 830 C CG . LEU A 1 105 ? -35.160 41.841 72.766 1.00 70.73 ? 105 LEU A CG 1 ATOM 831 C CD1 . LEU A 1 105 ? -34.002 40.884 72.991 1.00 71.39 ? 105 LEU A CD1 1 ATOM 832 C CD2 . LEU A 1 105 ? -34.748 43.271 73.074 1.00 72.43 ? 105 LEU A CD2 1 ATOM 833 N N . SER A 1 106 ? -37.426 41.929 68.676 1.00 75.68 ? 106 SER A N 1 ATOM 834 C CA A SER A 1 106 ? -37.460 41.923 67.216 0.50 78.46 ? 106 SER A CA 1 ATOM 835 C CA B SER A 1 106 ? -37.431 41.929 67.224 0.50 78.03 ? 106 SER A CA 1 ATOM 836 C C . SER A 1 106 ? -37.982 43.253 66.683 1.00 80.61 ? 106 SER A C 1 ATOM 837 O O . SER A 1 106 ? -37.834 43.554 65.501 1.00 83.47 ? 106 SER A O 1 ATOM 838 C CB A SER A 1 106 ? -38.330 40.773 66.689 0.50 78.72 ? 106 SER A CB 1 ATOM 839 C CB B SER A 1 106 ? -38.233 40.736 66.713 0.50 77.79 ? 106 SER A CB 1 ATOM 840 O OG A SER A 1 106 ? -39.718 41.066 66.782 0.50 79.21 ? 106 SER A OG 1 ATOM 841 O OG B SER A 1 106 ? -37.776 39.543 67.334 0.50 76.05 ? 106 SER A OG 1 ATOM 842 N N . ARG A 1 107 ? -38.603 44.041 67.562 1.00 83.52 ? 107 ARG A N 1 ATOM 843 C CA . ARG A 1 107 ? -39.122 45.365 67.221 1.00 87.95 ? 107 ARG A CA 1 ATOM 844 C C . ARG A 1 107 ? -38.302 46.496 67.866 1.00 84.30 ? 107 ARG A C 1 ATOM 845 O O . ARG A 1 107 ? -38.713 47.657 67.829 1.00 83.36 ? 107 ARG A O 1 ATOM 846 C CB . ARG A 1 107 ? -40.580 45.473 67.673 1.00 95.22 ? 107 ARG A CB 1 ATOM 847 C CG . ARG A 1 107 ? -41.535 44.486 67.003 1.00 101.99 ? 107 ARG A CG 1 ATOM 848 C CD . ARG A 1 107 ? -42.675 44.069 67.933 1.00 109.32 ? 107 ARG A CD 1 ATOM 849 N NE . ARG A 1 107 ? -43.274 45.199 68.655 1.00 115.70 ? 107 ARG A NE 1 ATOM 850 C CZ . ARG A 1 107 ? -44.205 45.088 69.606 1.00 118.37 ? 107 ARG A CZ 1 ATOM 851 N NH1 . ARG A 1 107 ? -44.680 43.894 69.965 1.00 117.28 ? 107 ARG A NH1 1 ATOM 852 N NH2 . ARG A 1 107 ? -44.674 46.184 70.198 1.00 118.80 ? 107 ARG A NH2 1 ATOM 853 N N . ILE A 1 108 ? -37.150 46.159 68.447 1.00 80.12 ? 108 ILE A N 1 ATOM 854 C CA . ILE A 1 108 ? -36.321 47.132 69.163 1.00 79.84 ? 108 ILE A CA 1 ATOM 855 C C . ILE A 1 108 ? -34.903 47.195 68.589 1.00 78.87 ? 108 ILE A C 1 ATOM 856 O O . ILE A 1 108 ? -34.263 46.164 68.362 1.00 76.15 ? 108 ILE A O 1 ATOM 857 C CB . ILE A 1 108 ? -36.245 46.815 70.679 1.00 79.12 ? 108 ILE A CB 1 ATOM 858 C CG1 . ILE A 1 108 ? -37.629 46.959 71.327 1.00 79.22 ? 108 ILE A CG1 1 ATOM 859 C CG2 . ILE A 1 108 ? -35.260 47.747 71.383 1.00 78.53 ? 108 ILE A CG2 1 ATOM 860 C CD1 . ILE A 1 108 ? -37.726 46.384 72.726 1.00 77.38 ? 108 ILE A CD1 1 ATOM 861 N N . ASN A 1 109 ? -34.422 48.418 68.381 1.00 79.21 ? 109 ASN A N 1 ATOM 862 C CA . ASN A 1 109 ? -33.082 48.662 67.861 1.00 81.27 ? 109 ASN A CA 1 ATOM 863 C C . ASN A 1 109 ? -32.108 49.233 68.891 1.00 82.03 ? 109 ASN A C 1 ATOM 864 O O . ASN A 1 109 ? -30.896 49.179 68.674 1.00 81.17 ? 109 ASN A O 1 ATOM 865 C CB . ASN A 1 109 ? -33.156 49.603 66.656 1.00 83.97 ? 109 ASN A CB 1 ATOM 866 C CG . ASN A 1 109 ? -33.659 48.907 65.411 1.00 85.25 ? 109 ASN A CG 1 ATOM 867 O OD1 . ASN A 1 109 ? -34.809 49.083 65.008 1.00 88.15 ? 109 ASN A OD1 1 ATOM 868 N ND2 . ASN A 1 109 ? -32.803 48.094 64.804 1.00 85.31 ? 109 ASN A ND2 1 ATOM 869 N N . HIS A 1 110 ? -32.615 49.789 69.993 1.00 81.96 ? 110 HIS A N 1 ATOM 870 C CA . HIS A 1 110 ? -31.729 50.367 71.006 1.00 83.45 ? 110 HIS A CA 1 ATOM 871 C C . HIS A 1 110 ? -32.316 50.445 72.419 1.00 82.11 ? 110 HIS A C 1 ATOM 872 O O . HIS A 1 110 ? -33.446 50.904 72.631 1.00 79.60 ? 110 HIS A O 1 ATOM 873 C CB . HIS A 1 110 ? -31.260 51.759 70.563 1.00 86.55 ? 110 HIS A CB 1 ATOM 874 C CG . HIS A 1 110 ? -30.061 52.262 71.310 1.00 88.82 ? 110 HIS A CG 1 ATOM 875 N ND1 . HIS A 1 110 ? -29.815 53.606 71.504 1.00 90.60 ? 110 HIS A ND1 1 ATOM 876 C CD2 . HIS A 1 110 ? -29.043 51.602 71.913 1.00 88.23 ? 110 HIS A CD2 1 ATOM 877 C CE1 . HIS A 1 110 ? -28.695 53.750 72.190 1.00 91.53 ? 110 HIS A CE1 1 ATOM 878 N NE2 . HIS A 1 110 ? -28.208 52.550 72.452 1.00 89.60 ? 110 HIS A NE2 1 ATOM 879 N N . PHE A 1 111 ? -31.518 49.980 73.377 1.00 81.75 ? 111 PHE A N 1 ATOM 880 C CA . PHE A 1 111 ? -31.782 50.178 74.793 1.00 82.03 ? 111 PHE A CA 1 ATOM 881 C C . PHE A 1 111 ? -30.824 51.221 75.345 1.00 83.75 ? 111 PHE A C 1 ATOM 882 O O . PHE A 1 111 ? -29.666 51.269 74.931 1.00 84.31 ? 111 PHE A O 1 ATOM 883 C CB . PHE A 1 111 ? -31.544 48.892 75.575 1.00 80.21 ? 111 PHE A CB 1 ATOM 884 C CG . PHE A 1 111 ? -32.616 47.853 75.409 1.00 78.18 ? 111 PHE A CG 1 ATOM 885 C CD1 . PHE A 1 111 ? -33.958 48.166 75.594 1.00 77.58 ? 111 PHE A CD1 1 ATOM 886 C CD2 . PHE A 1 111 ? -32.274 46.542 75.131 1.00 75.86 ? 111 PHE A CD2 1 ATOM 887 C CE1 . PHE A 1 111 ? -34.933 47.195 75.469 1.00 74.43 ? 111 PHE A CE1 1 ATOM 888 C CE2 . PHE A 1 111 ? -33.244 45.572 75.009 1.00 73.49 ? 111 PHE A CE2 1 ATOM 889 C CZ . PHE A 1 111 ? -34.575 45.898 75.177 1.00 73.34 ? 111 PHE A CZ 1 ATOM 890 N N . GLU A 1 112 ? -31.303 52.044 76.277 1.00 85.38 ? 112 GLU A N 1 ATOM 891 C CA . GLU A 1 112 ? -30.416 52.842 77.134 1.00 86.78 ? 112 GLU A CA 1 ATOM 892 C C . GLU A 1 112 ? -30.617 52.378 78.574 1.00 82.44 ? 112 GLU A C 1 ATOM 893 O O . GLU A 1 112 ? -31.716 52.476 79.111 1.00 78.37 ? 112 GLU A O 1 ATOM 894 C CB . GLU A 1 112 ? -30.690 54.347 77.009 1.00 90.92 ? 112 GLU A CB 1 ATOM 895 C CG . GLU A 1 112 ? -29.569 55.214 77.584 1.00 95.13 ? 112 GLU A CG 1 ATOM 896 C CD . GLU A 1 112 ? -30.029 56.603 78.006 1.00 98.73 ? 112 GLU A CD 1 ATOM 897 O OE1 . GLU A 1 112 ? -30.539 57.350 77.144 1.00 102.03 ? 112 GLU A OE1 1 ATOM 898 O OE2 . GLU A 1 112 ? -29.871 56.952 79.199 1.00 98.13 ? 112 GLU A OE2 1 ATOM 899 N N . LYS A 1 113 ? -29.556 51.860 79.183 1.00 81.84 ? 113 LYS A N 1 ATOM 900 C CA . LYS A 1 113 ? -29.622 51.335 80.550 1.00 82.44 ? 113 LYS A CA 1 ATOM 901 C C . LYS A 1 113 ? -29.621 52.466 81.571 1.00 83.70 ? 113 LYS A C 1 ATOM 902 O O . LYS A 1 113 ? -28.840 53.403 81.442 1.00 86.79 ? 113 LYS A O 1 ATOM 903 C CB . LYS A 1 113 ? -28.434 50.408 80.795 1.00 82.34 ? 113 LYS A CB 1 ATOM 904 C CG . LYS A 1 113 ? -28.379 49.797 82.183 1.00 83.41 ? 113 LYS A CG 1 ATOM 905 C CD . LYS A 1 113 ? -27.997 48.322 82.147 1.00 84.00 ? 113 LYS A CD 1 ATOM 906 C CE . LYS A 1 113 ? -26.655 48.056 81.478 1.00 85.56 ? 113 LYS A CE 1 ATOM 907 N NZ . LYS A 1 113 ? -26.362 46.596 81.401 1.00 85.77 ? 113 LYS A NZ 1 ATOM 908 N N . ILE A 1 114 ? -30.503 52.392 82.570 1.00 83.81 ? 114 ILE A N 1 ATOM 909 C CA . ILE A 1 114 ? -30.487 53.362 83.674 1.00 86.93 ? 114 ILE A CA 1 ATOM 910 C C . ILE A 1 114 ? -30.776 52.723 85.027 1.00 86.08 ? 114 ILE A C 1 ATOM 911 O O . ILE A 1 114 ? -31.488 51.724 85.117 1.00 87.37 ? 114 ILE A O 1 ATOM 912 C CB . ILE A 1 114 ? -31.481 54.530 83.469 1.00 89.62 ? 114 ILE A CB 1 ATOM 913 C CG1 . ILE A 1 114 ? -32.928 54.030 83.384 1.00 90.26 ? 114 ILE A CG1 1 ATOM 914 C CG2 . ILE A 1 114 ? -31.117 55.343 82.231 1.00 91.33 ? 114 ILE A CG2 1 ATOM 915 C CD1 . ILE A 1 114 ? -33.940 55.087 83.775 1.00 91.88 ? 114 ILE A CD1 1 ATOM 916 N N . GLN A 1 115 ? -30.230 53.326 86.075 1.00 86.25 ? 115 GLN A N 1 ATOM 917 C CA . GLN A 1 115 ? -30.406 52.841 87.439 1.00 84.03 ? 115 GLN A CA 1 ATOM 918 C C . GLN A 1 115 ? -31.739 53.319 87.985 1.00 81.63 ? 115 GLN A C 1 ATOM 919 O O . GLN A 1 115 ? -32.015 54.514 87.973 1.00 80.22 ? 115 GLN A O 1 ATOM 920 C CB . GLN A 1 115 ? -29.270 53.361 88.317 1.00 86.33 ? 115 GLN A CB 1 ATOM 921 C CG . GLN A 1 115 ? -29.438 53.099 89.803 1.00 87.64 ? 115 GLN A CG 1 ATOM 922 C CD . GLN A 1 115 ? -28.223 53.529 90.600 1.00 88.85 ? 115 GLN A CD 1 ATOM 923 O OE1 . GLN A 1 115 ? -28.228 54.581 91.237 1.00 90.31 ? 115 GLN A OE1 1 ATOM 924 N NE2 . GLN A 1 115 ? -27.171 52.719 90.561 1.00 88.80 ? 115 GLN A NE2 1 ATOM 925 N N . ILE A 1 116 ? -32.561 52.391 88.464 1.00 80.22 ? 116 ILE A N 1 ATOM 926 C CA . ILE A 1 116 ? -33.841 52.758 89.078 1.00 81.97 ? 116 ILE A CA 1 ATOM 927 C C . ILE A 1 116 ? -33.820 52.595 90.602 1.00 84.48 ? 116 ILE A C 1 ATOM 928 O O . ILE A 1 116 ? -34.414 53.405 91.317 1.00 86.10 ? 116 ILE A O 1 ATOM 929 C CB . ILE A 1 116 ? -35.046 52.005 88.458 1.00 78.95 ? 116 ILE A CB 1 ATOM 930 C CG1 . ILE A 1 116 ? -34.804 50.496 88.402 1.00 76.95 ? 116 ILE A CG1 1 ATOM 931 C CG2 . ILE A 1 116 ? -35.333 52.532 87.061 1.00 79.36 ? 116 ILE A CG2 1 ATOM 932 C CD1 . ILE A 1 116 ? -36.059 49.702 88.124 1.00 75.40 ? 116 ILE A CD1 1 ATOM 933 N N . ILE A 1 117 ? -33.134 51.565 91.095 1.00 86.21 ? 117 ILE A N 1 ATOM 934 C CA . ILE A 1 117 ? -32.966 51.363 92.538 1.00 89.31 ? 117 ILE A CA 1 ATOM 935 C C . ILE A 1 117 ? -31.477 51.197 92.865 1.00 89.93 ? 117 ILE A C 1 ATOM 936 O O . ILE A 1 117 ? -30.917 50.119 92.656 1.00 90.10 ? 117 ILE A O 1 ATOM 937 C CB . ILE A 1 117 ? -33.760 50.139 93.038 1.00 88.36 ? 117 ILE A CB 1 ATOM 938 C CG1 . ILE A 1 117 ? -35.244 50.293 92.682 1.00 88.20 ? 117 ILE A CG1 1 ATOM 939 C CG2 . ILE A 1 117 ? -33.582 49.967 94.541 1.00 88.41 ? 117 ILE A CG2 1 ATOM 940 C CD1 . ILE A 1 117 ? -36.112 49.117 93.083 1.00 87.56 ? 117 ILE A CD1 1 ATOM 941 N N . PRO A 1 118 ? -30.833 52.262 93.383 1.00 91.05 ? 118 PRO A N 1 ATOM 942 C CA . PRO A 1 118 ? -29.394 52.181 93.650 1.00 92.15 ? 118 PRO A CA 1 ATOM 943 C C . PRO A 1 118 ? -29.036 51.079 94.645 1.00 92.43 ? 118 PRO A C 1 ATOM 944 O O . PRO A 1 118 ? -29.821 50.764 95.539 1.00 91.45 ? 118 PRO A O 1 ATOM 945 C CB . PRO A 1 118 ? -29.049 53.564 94.228 1.00 94.18 ? 118 PRO A CB 1 ATOM 946 C CG . PRO A 1 118 ? -30.194 54.453 93.881 1.00 93.40 ? 118 PRO A CG 1 ATOM 947 C CD . PRO A 1 118 ? -31.397 53.568 93.774 1.00 92.16 ? 118 PRO A CD 1 ATOM 948 N N . LYS A 1 119 ? -27.853 50.501 94.474 1.00 93.71 ? 119 LYS A N 1 ATOM 949 C CA . LYS A 1 119 ? -27.399 49.411 95.328 1.00 95.04 ? 119 LYS A CA 1 ATOM 950 C C . LYS A 1 119 ? -27.163 49.925 96.750 1.00 97.14 ? 119 LYS A C 1 ATOM 951 O O . LYS A 1 119 ? -27.539 49.272 97.726 1.00 98.31 ? 119 LYS A O 1 ATOM 952 C CB . LYS A 1 119 ? -26.124 48.786 94.751 1.00 96.53 ? 119 LYS A CB 1 ATOM 953 C CG . LYS A 1 119 ? -25.920 47.330 95.125 1.00 97.00 ? 119 LYS A CG 1 ATOM 954 C CD . LYS A 1 119 ? -24.638 46.780 94.521 1.00 98.51 ? 119 LYS A CD 1 ATOM 955 C CE . LYS A 1 119 ? -24.268 45.439 95.134 1.00 99.44 ? 119 LYS A CE 1 ATOM 956 N NZ . LYS A 1 119 ? -22.873 45.040 94.804 1.00 101.07 ? 119 LYS A NZ 1 ATOM 957 N N . SER A 1 120 ? -26.552 51.106 96.850 1.00 98.06 ? 120 SER A N 1 ATOM 958 C CA . SER A 1 120 ? -26.333 51.786 98.129 1.00 97.45 ? 120 SER A CA 1 ATOM 959 C C . SER A 1 120 ? -27.635 52.007 98.898 1.00 97.14 ? 120 SER A C 1 ATOM 960 O O . SER A 1 120 ? -27.655 51.936 100.123 1.00 98.30 ? 120 SER A O 1 ATOM 961 C CB . SER A 1 120 ? -25.659 53.137 97.891 1.00 97.89 ? 120 SER A CB 1 ATOM 962 O OG . SER A 1 120 ? -26.487 53.985 97.114 1.00 96.40 ? 120 SER A OG 1 ATOM 963 N N . SER A 1 121 ? -28.716 52.260 98.164 1.00 95.88 ? 121 SER A N 1 ATOM 964 C CA . SER A 1 121 ? -30.032 52.571 98.739 1.00 95.89 ? 121 SER A CA 1 ATOM 965 C C . SER A 1 121 ? -30.549 51.590 99.806 1.00 93.98 ? 121 SER A C 1 ATOM 966 O O . SER A 1 121 ? -31.374 51.968 100.632 1.00 92.15 ? 121 SER A O 1 ATOM 967 C CB . SER A 1 121 ? -31.066 52.667 97.608 1.00 95.36 ? 121 SER A CB 1 ATOM 968 O OG . SER A 1 121 ? -32.334 53.066 98.090 1.00 96.76 ? 121 SER A OG 1 ATOM 969 N N . TRP A 1 122 ? -30.087 50.342 99.778 1.00 94.23 ? 122 TRP A N 1 ATOM 970 C CA . TRP A 1 122 ? -30.591 49.311 100.692 1.00 95.52 ? 122 TRP A CA 1 ATOM 971 C C . TRP A 1 122 ? -29.959 49.403 102.080 1.00 98.99 ? 122 TRP A C 1 ATOM 972 O O . TRP A 1 122 ? -28.976 48.723 102.372 1.00 100.13 ? 122 TRP A O 1 ATOM 973 C CB . TRP A 1 122 ? -30.354 47.921 100.100 1.00 94.19 ? 122 TRP A CB 1 ATOM 974 C CG . TRP A 1 122 ? -31.093 47.701 98.822 1.00 92.83 ? 122 TRP A CG 1 ATOM 975 C CD1 . TRP A 1 122 ? -30.567 47.675 97.564 1.00 92.10 ? 122 TRP A CD1 1 ATOM 976 C CD2 . TRP A 1 122 ? -32.501 47.492 98.674 1.00 91.57 ? 122 TRP A CD2 1 ATOM 977 N NE1 . TRP A 1 122 ? -31.560 47.451 96.641 1.00 92.05 ? 122 TRP A NE1 1 ATOM 978 C CE2 . TRP A 1 122 ? -32.758 47.337 97.295 1.00 90.93 ? 122 TRP A CE2 1 ATOM 979 C CE3 . TRP A 1 122 ? -33.570 47.417 99.574 1.00 91.22 ? 122 TRP A CE3 1 ATOM 980 C CZ2 . TRP A 1 122 ? -34.043 47.111 96.791 1.00 88.90 ? 122 TRP A CZ2 1 ATOM 981 C CZ3 . TRP A 1 122 ? -34.846 47.192 99.076 1.00 90.96 ? 122 TRP A CZ3 1 ATOM 982 C CH2 . TRP A 1 122 ? -35.071 47.039 97.694 1.00 89.70 ? 122 TRP A CH2 1 ATOM 983 N N . SER A 1 123 ? -30.537 50.240 102.935 1.00 101.32 ? 123 SER A N 1 ATOM 984 C CA . SER A 1 123 ? -30.001 50.468 104.282 1.00 103.78 ? 123 SER A CA 1 ATOM 985 C C . SER A 1 123 ? -30.436 49.382 105.275 1.00 102.79 ? 123 SER A C 1 ATOM 986 O O . SER A 1 123 ? -29.634 48.910 106.077 1.00 102.58 ? 123 SER A O 1 ATOM 987 C CB . SER A 1 123 ? -30.416 51.854 104.787 1.00 105.87 ? 123 SER A CB 1 ATOM 988 O OG . SER A 1 123 ? -31.758 52.146 104.437 1.00 104.54 ? 123 SER A OG 1 ATOM 989 N N . SER A 1 124 ? -31.705 48.990 105.204 1.00 102.02 ? 124 SER A N 1 ATOM 990 C CA . SER A 1 124 ? -32.266 47.944 106.066 1.00 100.76 ? 124 SER A CA 1 ATOM 991 C C . SER A 1 124 ? -31.734 46.525 105.777 1.00 98.34 ? 124 SER A C 1 ATOM 992 O O . SER A 1 124 ? -31.780 45.662 106.652 1.00 94.91 ? 124 SER A O 1 ATOM 993 C CB . SER A 1 124 ? -33.799 47.950 105.948 1.00 101.86 ? 124 SER A CB 1 ATOM 994 O OG . SER A 1 124 ? -34.222 47.953 104.585 1.00 101.74 ? 124 SER A OG 1 ATOM 995 N N . HIS A 1 125 ? -31.243 46.289 104.555 1.00 97.59 ? 125 HIS A N 1 ATOM 996 C CA . HIS A 1 125 ? -30.831 44.944 104.108 1.00 94.97 ? 125 HIS A CA 1 ATOM 997 C C . HIS A 1 125 ? -29.415 44.923 103.526 1.00 95.69 ? 125 HIS A C 1 ATOM 998 O O . HIS A 1 125 ? -28.877 45.963 103.142 1.00 96.28 ? 125 HIS A O 1 ATOM 999 C CB . HIS A 1 125 ? -31.804 44.420 103.048 1.00 90.35 ? 125 HIS A CB 1 ATOM 1000 C CG . HIS A 1 125 ? -33.234 44.403 103.490 1.00 87.82 ? 125 HIS A CG 1 ATOM 1001 N ND1 . HIS A 1 125 ? -34.024 45.533 103.497 1.00 87.22 ? 125 HIS A ND1 1 ATOM 1002 C CD2 . HIS A 1 125 ? -34.020 43.391 103.929 1.00 86.34 ? 125 HIS A CD2 1 ATOM 1003 C CE1 . HIS A 1 125 ? -35.231 45.219 103.933 1.00 87.16 ? 125 HIS A CE1 1 ATOM 1004 N NE2 . HIS A 1 125 ? -35.256 43.925 104.199 1.00 86.34 ? 125 HIS A NE2 1 ATOM 1005 N N . GLU A 1 126 ? -28.827 43.730 103.448 1.00 96.04 ? 126 GLU A N 1 ATOM 1006 C CA . GLU A 1 126 ? -27.471 43.559 102.915 1.00 97.79 ? 126 GLU A CA 1 ATOM 1007 C C . GLU A 1 126 ? -27.509 43.302 101.411 1.00 97.20 ? 126 GLU A C 1 ATOM 1008 O O . GLU A 1 126 ? -28.259 42.440 100.945 1.00 96.83 ? 126 GLU A O 1 ATOM 1009 C CB . GLU A 1 126 ? -26.764 42.403 103.624 1.00 99.82 ? 126 GLU A CB 1 ATOM 1010 C CG . GLU A 1 126 ? -25.313 42.185 103.206 1.00 101.50 ? 126 GLU A CG 1 ATOM 1011 C CD . GLU A 1 126 ? -24.425 43.399 103.448 1.00 103.80 ? 126 GLU A CD 1 ATOM 1012 O OE1 . GLU A 1 126 ? -24.275 43.816 104.624 1.00 101.49 ? 126 GLU A OE1 1 ATOM 1013 O OE2 . GLU A 1 126 ? -23.873 43.928 102.455 1.00 103.49 ? 126 GLU A OE2 1 ATOM 1014 N N . ALA A 1 127 ? -26.685 44.037 100.662 1.00 96.84 ? 127 ALA A N 1 ATOM 1015 C CA . ALA A 1 127 ? -26.738 44.021 99.195 1.00 92.85 ? 127 ALA A CA 1 ATOM 1016 C C . ALA A 1 127 ? -25.447 43.580 98.495 1.00 93.01 ? 127 ALA A C 1 ATOM 1017 O O . ALA A 1 127 ? -25.465 43.329 97.288 1.00 92.23 ? 127 ALA A O 1 ATOM 1018 C CB . ALA A 1 127 ? -27.157 45.392 98.688 1.00 92.25 ? 127 ALA A CB 1 ATOM 1019 N N . SER A 1 128 ? -24.341 43.478 99.233 1.00 94.24 ? 128 SER A N 1 ATOM 1020 C CA . SER A 1 128 ? -23.039 43.135 98.636 1.00 94.12 ? 128 SER A CA 1 ATOM 1021 C C . SER A 1 128 ? -22.585 41.696 98.908 1.00 92.29 ? 128 SER A C 1 ATOM 1022 O O . SER A 1 128 ? -21.439 41.342 98.625 1.00 90.36 ? 128 SER A O 1 ATOM 1023 C CB . SER A 1 128 ? -21.970 44.126 99.102 1.00 97.27 ? 128 SER A CB 1 ATOM 1024 O OG . SER A 1 128 ? -22.002 45.288 98.293 1.00 99.09 ? 128 SER A OG 1 ATOM 1025 N N . LEU A 1 129 ? -23.488 40.872 99.438 1.00 90.71 ? 129 LEU A N 1 ATOM 1026 C CA . LEU A 1 129 ? -23.197 39.468 99.728 1.00 91.11 ? 129 LEU A CA 1 ATOM 1027 C C . LEU A 1 129 ? -24.054 38.516 98.887 1.00 90.78 ? 129 LEU A C 1 ATOM 1028 O O . LEU A 1 129 ? -24.071 37.310 99.136 1.00 91.78 ? 129 LEU A O 1 ATOM 1029 C CB . LEU A 1 129 ? -23.411 39.195 101.219 1.00 93.26 ? 129 LEU A CB 1 ATOM 1030 C CG . LEU A 1 129 ? -22.230 39.453 102.164 1.00 95.27 ? 129 LEU A CG 1 ATOM 1031 C CD1 . LEU A 1 129 ? -21.503 40.761 101.871 1.00 95.81 ? 129 LEU A CD1 1 ATOM 1032 C CD2 . LEU A 1 129 ? -22.723 39.425 103.605 1.00 96.32 ? 129 LEU A CD2 1 ATOM 1033 N N . GLY A 1 130 ? -24.742 39.058 97.881 1.00 89.69 ? 130 GLY A N 1 ATOM 1034 C CA . GLY A 1 130 ? -25.630 38.274 97.027 1.00 86.62 ? 130 GLY A CA 1 ATOM 1035 C C . GLY A 1 130 ? -24.938 37.700 95.802 1.00 86.84 ? 130 GLY A C 1 ATOM 1036 O O . GLY A 1 130 ? -25.251 38.078 94.664 1.00 83.11 ? 130 GLY A O 1 ATOM 1037 N N . VAL A 1 131 ? -24.016 36.764 96.041 1.00 87.37 ? 131 VAL A N 1 ATOM 1038 C CA . VAL A 1 131 ? -23.160 36.200 94.989 1.00 86.00 ? 131 VAL A CA 1 ATOM 1039 C C . VAL A 1 131 ? -23.139 34.665 95.011 1.00 84.11 ? 131 VAL A C 1 ATOM 1040 O O . VAL A 1 131 ? -23.662 34.044 95.937 1.00 83.99 ? 131 VAL A O 1 ATOM 1041 C CB . VAL A 1 131 ? -21.714 36.739 95.106 1.00 89.02 ? 131 VAL A CB 1 ATOM 1042 C CG1 . VAL A 1 131 ? -21.696 38.255 94.954 1.00 89.48 ? 131 VAL A CG1 1 ATOM 1043 C CG2 . VAL A 1 131 ? -21.070 36.330 96.427 1.00 90.81 ? 131 VAL A CG2 1 ATOM 1044 N N . SER A 1 132 ? -22.532 34.068 93.985 1.00 82.99 ? 132 SER A N 1 ATOM 1045 C CA . SER A 1 132 ? -22.466 32.607 93.845 1.00 82.21 ? 132 SER A CA 1 ATOM 1046 C C . SER A 1 132 ? -21.258 32.132 93.032 1.00 83.42 ? 132 SER A C 1 ATOM 1047 O O . SER A 1 132 ? -20.707 32.877 92.215 1.00 81.37 ? 132 SER A O 1 ATOM 1048 C CB . SER A 1 132 ? -23.747 32.076 93.190 1.00 79.37 ? 132 SER A CB 1 ATOM 1049 O OG . SER A 1 132 ? -23.600 30.720 92.789 1.00 77.37 ? 132 SER A OG 1 ATOM 1050 N N . SER A 1 133 ? -20.870 30.879 93.266 1.00 85.40 ? 133 SER A N 1 ATOM 1051 C CA . SER A 1 133 ? -19.791 30.229 92.525 1.00 88.01 ? 133 SER A CA 1 ATOM 1052 C C . SER A 1 133 ? -20.211 29.889 91.100 1.00 88.80 ? 133 SER A C 1 ATOM 1053 O O . SER A 1 133 ? -19.372 29.849 90.197 1.00 88.54 ? 133 SER A O 1 ATOM 1054 C CB . SER A 1 133 ? -19.371 28.944 93.224 1.00 88.89 ? 133 SER A CB 1 ATOM 1055 O OG . SER A 1 133 ? -19.031 29.202 94.569 1.00 94.50 ? 133 SER A OG 1 ATOM 1056 N N . ALA A 1 134 ? -21.506 29.633 90.909 1.00 88.97 ? 134 ALA A N 1 ATOM 1057 C CA . ALA A 1 134 ? -22.058 29.328 89.588 1.00 88.69 ? 134 ALA A CA 1 ATOM 1058 C C . ALA A 1 134 ? -21.909 30.502 88.629 1.00 89.35 ? 134 ALA A C 1 ATOM 1059 O O . ALA A 1 134 ? -21.860 30.316 87.409 1.00 86.89 ? 134 ALA A O 1 ATOM 1060 C CB . ALA A 1 134 ? -23.525 28.942 89.702 1.00 87.39 ? 134 ALA A CB 1 ATOM 1061 N N . CYS A 1 135 ? -21.819 31.705 89.190 1.00 91.00 ? 135 CYS A N 1 ATOM 1062 C CA . CYS A 1 135 ? -21.815 32.927 88.410 1.00 92.47 ? 135 CYS A CA 1 ATOM 1063 C C . CYS A 1 135 ? -20.567 33.791 88.716 1.00 89.36 ? 135 CYS A C 1 ATOM 1064 O O . CYS A 1 135 ? -20.677 34.883 89.274 1.00 86.74 ? 135 CYS A O 1 ATOM 1065 C CB . CYS A 1 135 ? -23.139 33.655 88.681 1.00 95.62 ? 135 CYS A CB 1 ATOM 1066 S SG . CYS A 1 135 ? -23.577 34.874 87.429 1.00 107.87 ? 135 CYS A SG 1 ATOM 1067 N N . PRO A 1 136 ? -19.370 33.298 88.322 1.00 86.99 ? 136 PRO A N 1 ATOM 1068 C CA . PRO A 1 136 ? -18.089 33.888 88.706 1.00 87.84 ? 136 PRO A CA 1 ATOM 1069 C C . PRO A 1 136 ? -17.595 35.032 87.826 1.00 88.50 ? 136 PRO A C 1 ATOM 1070 O O . PRO A 1 136 ? -17.963 35.113 86.655 1.00 86.41 ? 136 PRO A O 1 ATOM 1071 C CB . PRO A 1 136 ? -17.130 32.712 88.545 1.00 89.24 ? 136 PRO A CB 1 ATOM 1072 C CG . PRO A 1 136 ? -17.674 31.985 87.366 1.00 86.47 ? 136 PRO A CG 1 ATOM 1073 C CD . PRO A 1 136 ? -19.168 32.083 87.506 1.00 85.61 ? 136 PRO A CD 1 ATOM 1074 N N . TYR A 1 137 ? -16.742 35.886 88.396 1.00 91.31 ? 137 TYR A N 1 ATOM 1075 C CA . TYR A 1 137 ? -16.047 36.939 87.647 1.00 93.11 ? 137 TYR A CA 1 ATOM 1076 C C . TYR A 1 137 ? -14.619 37.122 88.157 1.00 94.79 ? 137 TYR A C 1 ATOM 1077 O O . TYR A 1 137 ? -14.407 37.347 89.349 1.00 97.77 ? 137 TYR A O 1 ATOM 1078 C CB . TYR A 1 137 ? -16.790 38.271 87.755 1.00 94.15 ? 137 TYR A CB 1 ATOM 1079 C CG . TYR A 1 137 ? -16.096 39.406 87.025 1.00 96.52 ? 137 TYR A CG 1 ATOM 1080 C CD1 . TYR A 1 137 ? -16.021 39.425 85.628 1.00 96.62 ? 137 TYR A CD1 1 ATOM 1081 C CD2 . TYR A 1 137 ? -15.507 40.458 87.728 1.00 97.27 ? 137 TYR A CD2 1 ATOM 1082 C CE1 . TYR A 1 137 ? -15.383 40.459 84.957 1.00 97.17 ? 137 TYR A CE1 1 ATOM 1083 C CE2 . TYR A 1 137 ? -14.872 41.495 87.065 1.00 98.42 ? 137 TYR A CE2 1 ATOM 1084 C CZ . TYR A 1 137 ? -14.811 41.491 85.684 1.00 98.47 ? 137 TYR A CZ 1 ATOM 1085 O OH . TYR A 1 137 ? -14.180 42.520 85.034 1.00 99.51 ? 137 TYR A OH 1 ATOM 1086 N N . GLN A 1 138 ? -13.651 37.042 87.246 1.00 94.07 ? 138 GLN A N 1 ATOM 1087 C CA . GLN A 1 138 ? -12.236 37.141 87.591 1.00 95.69 ? 138 GLN A CA 1 ATOM 1088 C C . GLN A 1 138 ? -11.878 36.222 88.764 1.00 96.63 ? 138 GLN A C 1 ATOM 1089 O O . GLN A 1 138 ? -11.162 36.615 89.688 1.00 98.96 ? 138 GLN A O 1 ATOM 1090 C CB . GLN A 1 138 ? -11.864 38.593 87.895 1.00 98.45 ? 138 GLN A CB 1 ATOM 1091 C CG . GLN A 1 138 ? -11.902 39.508 86.678 1.00 98.92 ? 138 GLN A CG 1 ATOM 1092 C CD . GLN A 1 138 ? -11.530 40.950 86.999 1.00 101.18 ? 138 GLN A CD 1 ATOM 1093 O OE1 . GLN A 1 138 ? -11.407 41.780 86.097 1.00 100.00 ? 138 GLN A OE1 1 ATOM 1094 N NE2 . GLN A 1 138 ? -11.354 41.257 88.286 1.00 102.27 ? 138 GLN A NE2 1 ATOM 1095 N N . GLY A 1 139 ? -12.401 35.000 88.725 1.00 94.68 ? 139 GLY A N 1 ATOM 1096 C CA . GLY A 1 139 ? -12.067 33.978 89.714 1.00 94.66 ? 139 GLY A CA 1 ATOM 1097 C C . GLY A 1 139 ? -12.812 34.039 91.034 1.00 92.90 ? 139 GLY A C 1 ATOM 1098 O O . GLY A 1 139 ? -12.591 33.187 91.892 1.00 93.73 ? 139 GLY A O 1 ATOM 1099 N N . LYS A 1 140 ? -13.694 35.025 91.199 1.00 91.45 ? 140 LYS A N 1 ATOM 1100 C CA . LYS A 1 140 ? -14.433 35.216 92.455 1.00 92.47 ? 140 LYS A CA 1 ATOM 1101 C C . LYS A 1 140 ? -15.936 35.092 92.225 1.00 89.77 ? 140 LYS A C 1 ATOM 1102 O O . LYS A 1 140 ? -16.414 35.272 91.108 1.00 89.15 ? 140 LYS A O 1 ATOM 1103 C CB . LYS A 1 140 ? -14.115 36.585 93.070 1.00 94.10 ? 140 LYS A CB 1 ATOM 1104 C CG . LYS A 1 140 ? -12.661 36.999 92.913 1.00 97.07 ? 140 LYS A CG 1 ATOM 1105 C CD . LYS A 1 140 ? -12.238 38.053 93.922 1.00 99.26 ? 140 LYS A CD 1 ATOM 1106 C CE . LYS A 1 140 ? -10.775 38.429 93.724 1.00 101.30 ? 140 LYS A CE 1 ATOM 1107 N NZ . LYS A 1 140 ? -10.192 39.078 94.929 1.00 103.02 ? 140 LYS A NZ 1 ATOM 1108 N N . SER A 1 141 ? -16.674 34.792 93.289 1.00 88.99 ? 141 SER A N 1 ATOM 1109 C CA . SER A 1 141 ? -18.126 34.650 93.210 1.00 86.48 ? 141 SER A CA 1 ATOM 1110 C C . SER A 1 141 ? -18.800 36.001 92.969 1.00 86.28 ? 141 SER A C 1 ATOM 1111 O O . SER A 1 141 ? -18.675 36.914 93.782 1.00 88.48 ? 141 SER A O 1 ATOM 1112 C CB . SER A 1 141 ? -18.669 34.025 94.497 1.00 85.97 ? 141 SER A CB 1 ATOM 1113 O OG . SER A 1 141 ? -18.165 32.713 94.677 1.00 85.65 ? 141 SER A OG 1 ATOM 1114 N N . SER A 1 142 ? -19.519 36.118 91.855 1.00 84.38 ? 142 SER A N 1 ATOM 1115 C CA . SER A 1 142 ? -20.199 37.357 91.486 1.00 83.46 ? 142 SER A CA 1 ATOM 1116 C C . SER A 1 142 ? -21.670 37.065 91.179 1.00 81.95 ? 142 SER A C 1 ATOM 1117 O O . SER A 1 142 ? -22.187 36.020 91.581 1.00 83.25 ? 142 SER A O 1 ATOM 1118 C CB . SER A 1 142 ? -19.500 37.988 90.283 1.00 84.13 ? 142 SER A CB 1 ATOM 1119 O OG . SER A 1 142 ? -20.065 39.246 89.967 1.00 85.29 ? 142 SER A OG 1 ATOM 1120 N N . PHE A 1 143 ? -22.345 37.976 90.475 1.00 80.47 ? 143 PHE A N 1 ATOM 1121 C CA . PHE A 1 143 ? -23.772 37.807 90.168 1.00 77.50 ? 143 PHE A CA 1 ATOM 1122 C C . PHE A 1 143 ? -24.241 38.720 89.038 1.00 75.97 ? 143 PHE A C 1 ATOM 1123 O O . PHE A 1 143 ? -23.557 39.678 88.673 1.00 76.50 ? 143 PHE A O 1 ATOM 1124 C CB . PHE A 1 143 ? -24.613 38.088 91.418 1.00 76.74 ? 143 PHE A CB 1 ATOM 1125 C CG . PHE A 1 143 ? -25.992 37.489 91.381 1.00 74.72 ? 143 PHE A CG 1 ATOM 1126 C CD1 . PHE A 1 143 ? -26.165 36.110 91.337 1.00 74.13 ? 143 PHE A CD1 1 ATOM 1127 C CD2 . PHE A 1 143 ? -27.120 38.301 91.417 1.00 73.66 ? 143 PHE A CD2 1 ATOM 1128 C CE1 . PHE A 1 143 ? -27.435 35.552 91.316 1.00 72.68 ? 143 PHE A CE1 1 ATOM 1129 C CE2 . PHE A 1 143 ? -28.392 37.749 91.399 1.00 72.69 ? 143 PHE A CE2 1 ATOM 1130 C CZ . PHE A 1 143 ? -28.551 36.373 91.352 1.00 72.27 ? 143 PHE A CZ 1 ATOM 1131 N N . PHE A 1 144 ? -25.412 38.393 88.493 1.00 73.14 ? 144 PHE A N 1 ATOM 1132 C CA . PHE A 1 144 ? -26.112 39.224 87.519 1.00 71.95 ? 144 PHE A CA 1 ATOM 1133 C C . PHE A 1 144 ? -26.021 40.708 87.894 1.00 72.20 ? 144 PHE A C 1 ATOM 1134 O O . PHE A 1 144 ? -26.590 41.138 88.891 1.00 74.80 ? 144 PHE A O 1 ATOM 1135 C CB . PHE A 1 144 ? -27.591 38.811 87.437 1.00 71.29 ? 144 PHE A CB 1 ATOM 1136 C CG . PHE A 1 144 ? -27.816 37.400 86.940 1.00 70.93 ? 144 PHE A CG 1 ATOM 1137 C CD1 . PHE A 1 144 ? -27.485 37.042 85.638 1.00 70.72 ? 144 PHE A CD1 1 ATOM 1138 C CD2 . PHE A 1 144 ? -28.370 36.429 87.776 1.00 70.04 ? 144 PHE A CD2 1 ATOM 1139 C CE1 . PHE A 1 144 ? -27.698 35.745 85.182 1.00 69.66 ? 144 PHE A CE1 1 ATOM 1140 C CE2 . PHE A 1 144 ? -28.582 35.135 87.325 1.00 69.07 ? 144 PHE A CE2 1 ATOM 1141 C CZ . PHE A 1 144 ? -28.245 34.792 86.024 1.00 68.69 ? 144 PHE A CZ 1 ATOM 1142 N N . ARG A 1 145 ? -25.323 41.490 87.081 1.00 71.47 ? 145 ARG A N 1 ATOM 1143 C CA . ARG A 1 145 ? -25.011 42.876 87.421 1.00 72.56 ? 145 ARG A CA 1 ATOM 1144 C C . ARG A 1 145 ? -26.207 43.834 87.513 1.00 72.33 ? 145 ARG A C 1 ATOM 1145 O O . ARG A 1 145 ? -26.089 44.910 88.100 1.00 74.61 ? 145 ARG A O 1 ATOM 1146 C CB . ARG A 1 145 ? -24.002 43.439 86.423 1.00 73.46 ? 145 ARG A CB 1 ATOM 1147 C CG . ARG A 1 145 ? -22.699 42.664 86.366 1.00 75.47 ? 145 ARG A CG 1 ATOM 1148 C CD . ARG A 1 145 ? -21.590 43.528 85.799 1.00 79.22 ? 145 ARG A CD 1 ATOM 1149 N NE . ARG A 1 145 ? -20.357 42.776 85.583 1.00 82.62 ? 145 ARG A NE 1 ATOM 1150 C CZ . ARG A 1 145 ? -19.513 42.405 86.545 1.00 86.13 ? 145 ARG A CZ 1 ATOM 1151 N NH1 . ARG A 1 145 ? -19.757 42.686 87.823 1.00 87.65 ? 145 ARG A NH1 1 ATOM 1152 N NH2 . ARG A 1 145 ? -18.415 41.730 86.228 1.00 88.10 ? 145 ARG A NH2 1 ATOM 1153 N N . ASN A 1 146 ? -27.344 43.461 86.937 1.00 71.22 ? 146 ASN A N 1 ATOM 1154 C CA . ASN A 1 146 ? -28.486 44.375 86.845 1.00 70.63 ? 146 ASN A CA 1 ATOM 1155 C C . ASN A 1 146 ? -29.518 44.173 87.939 1.00 69.14 ? 146 ASN A C 1 ATOM 1156 O O . ASN A 1 146 ? -30.428 44.987 88.102 1.00 67.79 ? 146 ASN A O 1 ATOM 1157 C CB . ASN A 1 146 ? -29.130 44.270 85.462 1.00 69.53 ? 146 ASN A CB 1 ATOM 1158 C CG . ASN A 1 146 ? -28.186 44.701 84.362 1.00 71.87 ? 146 ASN A CG 1 ATOM 1159 O OD1 . ASN A 1 146 ? -27.389 45.624 84.547 1.00 74.01 ? 146 ASN A OD1 1 ATOM 1160 N ND2 . ASN A 1 146 ? -28.258 44.034 83.214 1.00 73.25 ? 146 ASN A ND2 1 ATOM 1161 N N . VAL A 1 147 ? -29.362 43.100 88.702 1.00 69.50 ? 147 VAL A N 1 ATOM 1162 C CA . VAL A 1 147 ? -30.226 42.849 89.846 1.00 70.81 ? 147 VAL A CA 1 ATOM 1163 C C . VAL A 1 147 ? -29.411 42.611 91.117 1.00 71.88 ? 147 VAL A C 1 ATOM 1164 O O . VAL A 1 147 ? -28.253 42.193 91.065 1.00 72.47 ? 147 VAL A O 1 ATOM 1165 C CB . VAL A 1 147 ? -31.171 41.668 89.574 1.00 70.11 ? 147 VAL A CB 1 ATOM 1166 C CG1 . VAL A 1 147 ? -32.162 42.043 88.484 1.00 69.47 ? 147 VAL A CG1 1 ATOM 1167 C CG2 . VAL A 1 147 ? -30.394 40.417 89.177 1.00 70.30 ? 147 VAL A CG2 1 ATOM 1168 N N . VAL A 1 148 ? -30.025 42.895 92.258 1.00 74.43 ? 148 VAL A N 1 ATOM 1169 C CA . VAL A 1 148 ? -29.353 42.794 93.557 1.00 75.42 ? 148 VAL A CA 1 ATOM 1170 C C . VAL A 1 148 ? -29.962 41.647 94.348 1.00 74.80 ? 148 VAL A C 1 ATOM 1171 O O . VAL A 1 148 ? -31.155 41.668 94.647 1.00 74.75 ? 148 VAL A O 1 ATOM 1172 C CB . VAL A 1 148 ? -29.503 44.098 94.363 1.00 76.40 ? 148 VAL A CB 1 ATOM 1173 C CG1 . VAL A 1 148 ? -28.875 43.956 95.743 1.00 79.80 ? 148 VAL A CG1 1 ATOM 1174 C CG2 . VAL A 1 148 ? -28.883 45.263 93.603 1.00 76.93 ? 148 VAL A CG2 1 ATOM 1175 N N . TRP A 1 149 ? -29.147 40.649 94.675 1.00 75.70 ? 149 TRP A N 1 ATOM 1176 C CA . TRP A 1 149 ? -29.596 39.542 95.516 1.00 77.74 ? 149 TRP A CA 1 ATOM 1177 C C . TRP A 1 149 ? -29.515 39.965 96.995 1.00 79.69 ? 149 TRP A C 1 ATOM 1178 O O . TRP A 1 149 ? -28.480 39.829 97.641 1.00 80.00 ? 149 TRP A O 1 ATOM 1179 C CB . TRP A 1 149 ? -28.778 38.278 95.213 1.00 77.65 ? 149 TRP A CB 1 ATOM 1180 C CG . TRP A 1 149 ? -29.237 37.021 95.920 1.00 78.02 ? 149 TRP A CG 1 ATOM 1181 C CD1 . TRP A 1 149 ? -30.310 36.884 96.759 1.00 78.81 ? 149 TRP A CD1 1 ATOM 1182 C CD2 . TRP A 1 149 ? -28.657 35.717 95.803 1.00 77.37 ? 149 TRP A CD2 1 ATOM 1183 N NE1 . TRP A 1 149 ? -30.415 35.582 97.188 1.00 79.03 ? 149 TRP A NE1 1 ATOM 1184 C CE2 . TRP A 1 149 ? -29.416 34.844 96.612 1.00 78.03 ? 149 TRP A CE2 1 ATOM 1185 C CE3 . TRP A 1 149 ? -27.564 35.204 95.101 1.00 77.42 ? 149 TRP A CE3 1 ATOM 1186 C CZ2 . TRP A 1 149 ? -29.117 33.488 96.737 1.00 78.11 ? 149 TRP A CZ2 1 ATOM 1187 C CZ3 . TRP A 1 149 ? -27.267 33.853 95.226 1.00 78.58 ? 149 TRP A CZ3 1 ATOM 1188 C CH2 . TRP A 1 149 ? -28.043 33.012 96.037 1.00 78.54 ? 149 TRP A CH2 1 ATOM 1189 N N . LEU A 1 150 ? -30.624 40.491 97.510 1.00 81.98 ? 150 LEU A N 1 ATOM 1190 C CA . LEU A 1 150 ? -30.692 40.981 98.884 1.00 86.81 ? 150 LEU A CA 1 ATOM 1191 C C . LEU A 1 150 ? -30.778 39.828 99.874 1.00 88.30 ? 150 LEU A C 1 ATOM 1192 O O . LEU A 1 150 ? -31.470 38.836 99.616 1.00 87.21 ? 150 LEU A O 1 ATOM 1193 C CB . LEU A 1 150 ? -31.908 41.897 99.076 1.00 87.79 ? 150 LEU A CB 1 ATOM 1194 C CG . LEU A 1 150 ? -31.980 43.160 98.206 1.00 88.90 ? 150 LEU A CG 1 ATOM 1195 C CD1 . LEU A 1 150 ? -33.364 43.784 98.289 1.00 89.42 ? 150 LEU A CD1 1 ATOM 1196 C CD2 . LEU A 1 150 ? -30.920 44.181 98.592 1.00 90.21 ? 150 LEU A CD2 1 ATOM 1197 N N . ILE A 1 151 ? -30.067 39.972 100.997 1.00 90.29 ? 151 ILE A N 1 ATOM 1198 C CA . ILE A 1 151 ? -30.143 39.037 102.127 1.00 91.21 ? 151 ILE A CA 1 ATOM 1199 C C . ILE A 1 151 ? -30.251 39.789 103.458 1.00 92.56 ? 151 ILE A C 1 ATOM 1200 O O . ILE A 1 151 ? -30.042 41.005 103.520 1.00 91.94 ? 151 ILE A O 1 ATOM 1201 C CB . ILE A 1 151 ? -28.922 38.094 102.179 1.00 92.27 ? 151 ILE A CB 1 ATOM 1202 C CG1 . ILE A 1 151 ? -27.639 38.874 102.491 1.00 94.17 ? 151 ILE A CG1 1 ATOM 1203 C CG2 . ILE A 1 151 ? -28.778 37.341 100.865 1.00 91.02 ? 151 ILE A CG2 1 ATOM 1204 C CD1 . ILE A 1 151 ? -26.412 37.997 102.621 1.00 95.51 ? 151 ILE A CD1 1 ATOM 1205 N N . LYS A 1 152 ? -30.560 39.045 104.518 1.00 94.68 ? 152 LYS A N 1 ATOM 1206 C CA . LYS A 1 152 ? -30.743 39.617 105.861 1.00 97.10 ? 152 LYS A CA 1 ATOM 1207 C C . LYS A 1 152 ? -29.532 40.410 106.366 1.00 99.50 ? 152 LYS A C 1 ATOM 1208 O O . LYS A 1 152 ? -28.379 40.058 106.095 1.00 96.80 ? 152 LYS A O 1 ATOM 1209 C CB . LYS A 1 152 ? -31.081 38.521 106.882 1.00 97.06 ? 152 LYS A CB 1 ATOM 1210 C CG . LYS A 1 152 ? -30.058 37.398 106.966 1.00 97.37 ? 152 LYS A CG 1 ATOM 1211 C CD . LYS A 1 152 ? -30.074 36.727 108.325 1.00 100.01 ? 152 LYS A CD 1 ATOM 1212 C CE . LYS A 1 152 ? -29.548 35.306 108.259 1.00 99.67 ? 152 LYS A CE 1 ATOM 1213 N NZ . LYS A 1 152 ? -29.543 34.647 109.593 1.00 101.99 ? 152 LYS A NZ 1 ATOM 1214 N N . LYS A 1 153 ? -29.819 41.481 107.105 1.00 102.51 ? 153 LYS A N 1 ATOM 1215 C CA . LYS A 1 153 ? -28.793 42.310 107.725 1.00 105.41 ? 153 LYS A CA 1 ATOM 1216 C C . LYS A 1 153 ? -28.916 42.188 109.238 1.00 107.12 ? 153 LYS A C 1 ATOM 1217 O O . LYS A 1 153 ? -29.927 42.593 109.816 1.00 106.41 ? 153 LYS A O 1 ATOM 1218 C CB . LYS A 1 153 ? -28.938 43.771 107.292 1.00 105.78 ? 153 LYS A CB 1 ATOM 1219 C CG . LYS A 1 153 ? -27.731 44.625 107.642 1.00 108.10 ? 153 LYS A CG 1 ATOM 1220 C CD . LYS A 1 153 ? -27.832 46.019 107.050 1.00 108.26 ? 153 LYS A CD 1 ATOM 1221 C CE . LYS A 1 153 ? -26.626 46.859 107.435 1.00 110.76 ? 153 LYS A CE 1 ATOM 1222 N NZ . LYS A 1 153 ? -26.729 48.244 106.902 1.00 111.49 ? 153 LYS A NZ 1 ATOM 1223 N N . ASN A 1 154 ? -27.885 41.619 109.861 1.00 108.53 ? 154 ASN A N 1 ATOM 1224 C CA . ASN A 1 154 ? -27.860 41.377 111.305 1.00 110.92 ? 154 ASN A CA 1 ATOM 1225 C C . ASN A 1 154 ? -29.059 40.537 111.776 1.00 109.41 ? 154 ASN A C 1 ATOM 1226 O O . ASN A 1 154 ? -29.764 40.903 112.718 1.00 107.62 ? 154 ASN A O 1 ATOM 1227 C CB . ASN A 1 154 ? -27.764 42.707 112.075 1.00 111.96 ? 154 ASN A CB 1 ATOM 1228 C CG . ASN A 1 154 ? -27.114 42.550 113.442 1.00 114.99 ? 154 ASN A CG 1 ATOM 1229 O OD1 . ASN A 1 154 ? -26.292 41.657 113.656 1.00 116.34 ? 154 ASN A OD1 1 ATOM 1230 N ND2 . ASN A 1 154 ? -27.472 43.430 114.372 1.00 115.38 ? 154 ASN A ND2 1 ATOM 1231 N N . SER A 1 155 ? -29.278 39.418 111.083 1.00 107.57 ? 155 SER A N 1 ATOM 1232 C CA . SER A 1 155 ? -30.272 38.403 111.462 1.00 106.16 ? 155 SER A CA 1 ATOM 1233 C C . SER A 1 155 ? -31.729 38.863 111.367 1.00 104.22 ? 155 SER A C 1 ATOM 1234 O O . SER A 1 155 ? -32.592 38.319 112.051 1.00 105.68 ? 155 SER A O 1 ATOM 1235 C CB . SER A 1 155 ? -29.975 37.868 112.867 1.00 107.28 ? 155 SER A CB 1 ATOM 1236 O OG . SER A 1 155 ? -28.600 37.554 112.992 1.00 107.38 ? 155 SER A OG 1 ATOM 1237 N N . THR A 1 156 ? -31.997 39.845 110.509 1.00 101.74 ? 156 THR A N 1 ATOM 1238 C CA . THR A 1 156 ? -33.350 40.378 110.328 1.00 100.18 ? 156 THR A CA 1 ATOM 1239 C C . THR A 1 156 ? -33.614 40.711 108.858 1.00 96.77 ? 156 THR A C 1 ATOM 1240 O O . THR A 1 156 ? -32.729 41.214 108.167 1.00 96.18 ? 156 THR A O 1 ATOM 1241 C CB . THR A 1 156 ? -33.556 41.669 111.143 1.00 101.20 ? 156 THR A CB 1 ATOM 1242 O OG1 . THR A 1 156 ? -32.705 42.698 110.626 1.00 102.68 ? 156 THR A OG1 1 ATOM 1243 C CG2 . THR A 1 156 ? -33.244 41.448 112.620 1.00 103.44 ? 156 THR A CG2 1 ATOM 1244 N N . TYR A 1 157 ? -34.827 40.431 108.390 1.00 94.28 ? 157 TYR A N 1 ATOM 1245 C CA . TYR A 1 157 ? -35.251 40.821 107.042 1.00 92.49 ? 157 TYR A CA 1 ATOM 1246 C C . TYR A 1 157 ? -36.604 41.519 107.150 1.00 90.35 ? 157 TYR A C 1 ATOM 1247 O O . TYR A 1 157 ? -37.653 40.874 107.042 1.00 87.77 ? 157 TYR A O 1 ATOM 1248 C CB . TYR A 1 157 ? -35.328 39.603 106.109 1.00 92.06 ? 157 TYR A CB 1 ATOM 1249 C CG . TYR A 1 157 ? -35.240 39.924 104.618 1.00 91.50 ? 157 TYR A CG 1 ATOM 1250 C CD1 . TYR A 1 157 ? -36.221 40.683 103.976 1.00 91.83 ? 157 TYR A CD1 1 ATOM 1251 C CD2 . TYR A 1 157 ? -34.180 39.451 103.847 1.00 91.66 ? 157 TYR A CD2 1 ATOM 1252 C CE1 . TYR A 1 157 ? -36.146 40.959 102.615 1.00 90.62 ? 157 TYR A CE1 1 ATOM 1253 C CE2 . TYR A 1 157 ? -34.097 39.725 102.490 1.00 89.57 ? 157 TYR A CE2 1 ATOM 1254 C CZ . TYR A 1 157 ? -35.079 40.483 101.878 1.00 89.24 ? 157 TYR A CZ 1 ATOM 1255 O OH . TYR A 1 157 ? -34.997 40.750 100.529 1.00 87.32 ? 157 TYR A OH 1 ATOM 1256 N N . PRO A 1 158 ? -36.583 42.844 107.389 1.00 90.33 ? 158 PRO A N 1 ATOM 1257 C CA . PRO A 1 158 ? -37.832 43.595 107.491 1.00 89.48 ? 158 PRO A CA 1 ATOM 1258 C C . PRO A 1 158 ? -38.514 43.735 106.136 1.00 87.05 ? 158 PRO A C 1 ATOM 1259 O O . PRO A 1 158 ? -37.849 43.691 105.096 1.00 84.92 ? 158 PRO A O 1 ATOM 1260 C CB . PRO A 1 158 ? -37.384 44.961 108.028 1.00 90.90 ? 158 PRO A CB 1 ATOM 1261 C CG . PRO A 1 158 ? -35.961 45.095 107.617 1.00 90.85 ? 158 PRO A CG 1 ATOM 1262 C CD . PRO A 1 158 ? -35.398 43.703 107.596 1.00 91.05 ? 158 PRO A CD 1 ATOM 1263 N N . THR A 1 159 ? -39.834 43.893 106.155 1.00 86.57 ? 159 THR A N 1 ATOM 1264 C CA . THR A 1 159 ? -40.604 43.997 104.925 1.00 84.68 ? 159 THR A CA 1 ATOM 1265 C C . THR A 1 159 ? -40.086 45.157 104.080 1.00 85.14 ? 159 THR A C 1 ATOM 1266 O O . THR A 1 159 ? -39.992 46.291 104.555 1.00 84.34 ? 159 THR A O 1 ATOM 1267 C CB . THR A 1 159 ? -42.112 44.176 105.204 1.00 84.52 ? 159 THR A CB 1 ATOM 1268 O OG1 . THR A 1 159 ? -42.571 43.116 106.051 1.00 84.14 ? 159 THR A OG1 1 ATOM 1269 C CG2 . THR A 1 159 ? -42.917 44.150 103.905 1.00 83.32 ? 159 THR A CG2 1 ATOM 1270 N N . ILE A 1 160 ? -39.727 44.843 102.838 1.00 85.60 ? 160 ILE A N 1 ATOM 1271 C CA . ILE A 1 160 ? -39.297 45.835 101.853 1.00 86.33 ? 160 ILE A CA 1 ATOM 1272 C C . ILE A 1 160 ? -40.528 46.486 101.229 1.00 85.81 ? 160 ILE A C 1 ATOM 1273 O O . ILE A 1 160 ? -41.538 45.826 101.016 1.00 85.64 ? 160 ILE A O 1 ATOM 1274 C CB . ILE A 1 160 ? -38.436 45.176 100.751 1.00 85.99 ? 160 ILE A CB 1 ATOM 1275 C CG1 . ILE A 1 160 ? -37.094 44.736 101.338 1.00 87.00 ? 160 ILE A CG1 1 ATOM 1276 C CG2 . ILE A 1 160 ? -38.211 46.127 99.580 1.00 85.70 ? 160 ILE A CG2 1 ATOM 1277 C CD1 . ILE A 1 160 ? -36.308 43.791 100.457 1.00 86.32 ? 160 ILE A CD1 1 ATOM 1278 N N . LYS A 1 161 ? -40.441 47.785 100.961 1.00 86.66 ? 161 LYS A N 1 ATOM 1279 C CA . LYS A 1 161 ? -41.513 48.522 100.290 1.00 87.02 ? 161 LYS A CA 1 ATOM 1280 C C . LYS A 1 161 ? -40.887 49.612 99.422 1.00 87.92 ? 161 LYS A C 1 ATOM 1281 O O . LYS A 1 161 ? -40.588 50.700 99.909 1.00 89.32 ? 161 LYS A O 1 ATOM 1282 C CB . LYS A 1 161 ? -42.483 49.142 101.308 1.00 88.84 ? 161 LYS A CB 1 ATOM 1283 C CG . LYS A 1 161 ? -43.296 48.131 102.107 1.00 89.85 ? 161 LYS A CG 1 ATOM 1284 C CD . LYS A 1 161 ? -44.272 48.781 103.082 1.00 91.10 ? 161 LYS A CD 1 ATOM 1285 C CE . LYS A 1 161 ? -44.994 47.715 103.901 1.00 92.46 ? 161 LYS A CE 1 ATOM 1286 N NZ . LYS A 1 161 ? -45.793 48.251 105.038 1.00 94.71 ? 161 LYS A NZ 1 ATOM 1287 N N . ARG A 1 162 ? -40.680 49.309 98.141 1.00 87.14 ? 162 ARG A N 1 ATOM 1288 C CA . ARG A 1 162 ? -40.023 50.236 97.224 1.00 86.19 ? 162 ARG A CA 1 ATOM 1289 C C . ARG A 1 162 ? -40.880 50.530 96.009 1.00 85.32 ? 162 ARG A C 1 ATOM 1290 O O . ARG A 1 162 ? -41.620 49.667 95.536 1.00 86.52 ? 162 ARG A O 1 ATOM 1291 C CB . ARG A 1 162 ? -38.689 49.662 96.756 1.00 86.14 ? 162 ARG A CB 1 ATOM 1292 C CG . ARG A 1 162 ? -37.672 49.450 97.862 1.00 88.74 ? 162 ARG A CG 1 ATOM 1293 C CD . ARG A 1 162 ? -37.387 50.726 98.642 1.00 91.63 ? 162 ARG A CD 1 ATOM 1294 N NE . ARG A 1 162 ? -36.048 50.700 99.228 1.00 93.42 ? 162 ARG A NE 1 ATOM 1295 C CZ . ARG A 1 162 ? -34.931 51.066 98.599 1.00 93.50 ? 162 ARG A CZ 1 ATOM 1296 N NH1 . ARG A 1 162 ? -34.956 51.510 97.348 1.00 92.80 ? 162 ARG A NH1 1 ATOM 1297 N NH2 . ARG A 1 162 ? -33.771 50.986 99.231 1.00 96.45 ? 162 ARG A NH2 1 ATOM 1298 N N . SER A 1 163 ? -40.753 51.752 95.498 1.00 85.28 ? 163 SER A N 1 ATOM 1299 C CA . SER A 1 163 ? -41.456 52.175 94.292 1.00 83.43 ? 163 SER A CA 1 ATOM 1300 C C . SER A 1 163 ? -40.524 52.882 93.322 1.00 83.93 ? 163 SER A C 1 ATOM 1301 O O . SER A 1 163 ? -39.598 53.581 93.737 1.00 82.99 ? 163 SER A O 1 ATOM 1302 C CB . SER A 1 163 ? -42.601 53.115 94.648 1.00 83.53 ? 163 SER A CB 1 ATOM 1303 O OG . SER A 1 163 ? -43.646 52.403 95.271 1.00 83.23 ? 163 SER A OG 1 ATOM 1304 N N . TYR A 1 164 ? -40.769 52.688 92.027 1.00 83.88 ? 164 TYR A N 1 ATOM 1305 C CA . TYR A 1 164 ? -40.128 53.504 91.008 1.00 84.31 ? 164 TYR A CA 1 ATOM 1306 C C . TYR A 1 164 ? -41.167 54.092 90.065 1.00 85.02 ? 164 TYR A C 1 ATOM 1307 O O . TYR A 1 164 ? -42.059 53.391 89.597 1.00 84.95 ? 164 TYR A O 1 ATOM 1308 C CB . TYR A 1 164 ? -39.087 52.724 90.216 1.00 82.57 ? 164 TYR A CB 1 ATOM 1309 C CG . TYR A 1 164 ? -38.539 53.551 89.084 1.00 85.21 ? 164 TYR A CG 1 ATOM 1310 C CD1 . TYR A 1 164 ? -37.610 54.560 89.319 1.00 87.19 ? 164 TYR A CD1 1 ATOM 1311 C CD2 . TYR A 1 164 ? -38.990 53.366 87.784 1.00 86.36 ? 164 TYR A CD2 1 ATOM 1312 C CE1 . TYR A 1 164 ? -37.121 55.340 88.285 1.00 88.24 ? 164 TYR A CE1 1 ATOM 1313 C CE2 . TYR A 1 164 ? -38.509 54.140 86.742 1.00 88.14 ? 164 TYR A CE2 1 ATOM 1314 C CZ . TYR A 1 164 ? -37.575 55.122 86.995 1.00 89.41 ? 164 TYR A CZ 1 ATOM 1315 O OH . TYR A 1 164 ? -37.107 55.881 85.946 1.00 93.05 ? 164 TYR A OH 1 ATOM 1316 N N . ASN A 1 165 ? -41.024 55.384 89.791 1.00 87.65 ? 165 ASN A N 1 ATOM 1317 C CA . ASN A 1 165 ? -41.910 56.111 88.904 1.00 90.68 ? 165 ASN A CA 1 ATOM 1318 C C . ASN A 1 165 ? -41.221 56.302 87.565 1.00 90.70 ? 165 ASN A C 1 ATOM 1319 O O . ASN A 1 165 ? -40.100 56.800 87.513 1.00 92.91 ? 165 ASN A O 1 ATOM 1320 C CB . ASN A 1 165 ? -42.225 57.470 89.517 1.00 95.21 ? 165 ASN A CB 1 ATOM 1321 C CG . ASN A 1 165 ? -43.338 58.203 88.795 1.00 100.00 ? 165 ASN A CG 1 ATOM 1322 O OD1 . ASN A 1 165 ? -43.283 58.417 87.586 1.00 98.80 ? 165 ASN A OD1 1 ATOM 1323 N ND2 . ASN A 1 165 ? -44.351 58.605 89.546 1.00 107.00 ? 165 ASN A ND2 1 ATOM 1324 N N . ASN A 1 166 ? -41.884 55.902 86.485 1.00 90.01 ? 166 ASN A N 1 ATOM 1325 C CA . ASN A 1 166 ? -41.340 56.105 85.151 1.00 90.36 ? 166 ASN A CA 1 ATOM 1326 C C . ASN A 1 166 ? -41.592 57.536 84.704 1.00 91.78 ? 166 ASN A C 1 ATOM 1327 O O . ASN A 1 166 ? -42.598 57.828 84.051 1.00 91.02 ? 166 ASN A O 1 ATOM 1328 C CB . ASN A 1 166 ? -41.949 55.118 84.151 1.00 90.26 ? 166 ASN A CB 1 ATOM 1329 C CG . ASN A 1 166 ? -41.202 55.095 82.828 1.00 91.69 ? 166 ASN A CG 1 ATOM 1330 O OD1 . ASN A 1 166 ? -40.030 55.463 82.760 1.00 93.53 ? 166 ASN A OD1 1 ATOM 1331 N ND2 . ASN A 1 166 ? -41.873 54.646 81.772 1.00 90.21 ? 166 ASN A ND2 1 ATOM 1332 N N . THR A 1 167 ? -40.679 58.427 85.082 1.00 92.25 ? 167 THR A N 1 ATOM 1333 C CA . THR A 1 167 ? -40.792 59.844 84.742 1.00 93.88 ? 167 THR A CA 1 ATOM 1334 C C . THR A 1 167 ? -40.365 60.103 83.301 1.00 94.44 ? 167 THR A C 1 ATOM 1335 O O . THR A 1 167 ? -41.037 60.843 82.578 1.00 97.22 ? 167 THR A O 1 ATOM 1336 C CB . THR A 1 167 ? -39.940 60.722 85.675 1.00 94.00 ? 167 THR A CB 1 ATOM 1337 O OG1 . THR A 1 167 ? -38.576 60.282 85.637 1.00 93.60 ? 167 THR A OG1 1 ATOM 1338 C CG2 . THR A 1 167 ? -40.461 60.639 87.091 1.00 93.33 ? 167 THR A CG2 1 ATOM 1339 N N . ASN A 1 168 ? -39.239 59.515 82.899 1.00 91.84 ? 168 ASN A N 1 ATOM 1340 C CA . ASN A 1 168 ? -38.765 59.603 81.506 1.00 91.00 ? 168 ASN A CA 1 ATOM 1341 C C . ASN A 1 168 ? -39.792 59.145 80.454 1.00 88.20 ? 168 ASN A C 1 ATOM 1342 O O . ASN A 1 168 ? -40.605 58.261 80.714 1.00 85.32 ? 168 ASN A O 1 ATOM 1343 C CB . ASN A 1 168 ? -37.413 58.887 81.312 1.00 89.36 ? 168 ASN A CB 1 ATOM 1344 C CG . ASN A 1 168 ? -37.298 57.593 82.098 1.00 86.50 ? 168 ASN A CG 1 ATOM 1345 O OD1 . ASN A 1 168 ? -36.195 57.180 82.453 1.00 85.87 ? 168 ASN A OD1 1 ATOM 1346 N ND2 . ASN A 1 168 ? -38.424 56.948 82.371 1.00 84.34 ? 168 ASN A ND2 1 ATOM 1347 N N . GLN A 1 169 ? -39.734 59.762 79.274 1.00 88.68 ? 169 GLN A N 1 ATOM 1348 C CA . GLN A 1 169 ? -40.752 59.583 78.223 1.00 89.59 ? 169 GLN A CA 1 ATOM 1349 C C . GLN A 1 169 ? -40.873 58.160 77.651 1.00 86.79 ? 169 GLN A C 1 ATOM 1350 O O . GLN A 1 169 ? -41.946 57.774 77.186 1.00 84.81 ? 169 GLN A O 1 ATOM 1351 C CB . GLN A 1 169 ? -40.500 60.558 77.055 1.00 92.20 ? 169 GLN A CB 1 ATOM 1352 C CG . GLN A 1 169 ? -41.553 61.644 76.871 1.00 94.13 ? 169 GLN A CG 1 ATOM 1353 C CD . GLN A 1 169 ? -41.667 62.102 75.416 1.00 95.79 ? 169 GLN A CD 1 ATOM 1354 O OE1 . GLN A 1 169 ? -40.868 62.912 74.937 1.00 96.62 ? 169 GLN A OE1 1 ATOM 1355 N NE2 . GLN A 1 169 ? -42.666 61.579 74.707 1.00 93.99 ? 169 GLN A NE2 1 ATOM 1356 N N . GLU A 1 170 ? -39.782 57.394 77.694 1.00 84.70 ? 170 GLU A N 1 ATOM 1357 C CA . GLU A 1 170 ? -39.683 56.106 76.998 1.00 81.18 ? 170 GLU A CA 1 ATOM 1358 C C . GLU A 1 170 ? -40.149 54.930 77.855 1.00 79.48 ? 170 GLU A C 1 ATOM 1359 O O . GLU A 1 170 ? -39.843 54.874 79.045 1.00 80.26 ? 170 GLU A O 1 ATOM 1360 C CB . GLU A 1 170 ? -38.236 55.854 76.581 1.00 80.04 ? 170 GLU A CB 1 ATOM 1361 C CG . GLU A 1 170 ? -37.624 56.953 75.723 1.00 82.77 ? 170 GLU A CG 1 ATOM 1362 C CD . GLU A 1 170 ? -36.934 58.036 76.527 1.00 84.63 ? 170 GLU A CD 1 ATOM 1363 O OE1 . GLU A 1 170 ? -37.344 58.292 77.679 1.00 88.15 ? 170 GLU A OE1 1 ATOM 1364 O OE2 . GLU A 1 170 ? -35.981 58.641 76.004 1.00 86.10 ? 170 GLU A OE2 1 ATOM 1365 N N . ASP A 1 171 ? -40.892 54.001 77.246 1.00 78.56 ? 171 ASP A N 1 ATOM 1366 C CA . ASP A 1 171 ? -41.257 52.731 77.883 1.00 76.40 ? 171 ASP A CA 1 ATOM 1367 C C . ASP A 1 171 ? -40.023 52.156 78.557 1.00 75.51 ? 171 ASP A C 1 ATOM 1368 O O . ASP A 1 171 ? -38.919 52.260 78.018 1.00 75.68 ? 171 ASP A O 1 ATOM 1369 C CB . ASP A 1 171 ? -41.756 51.706 76.846 1.00 77.52 ? 171 ASP A CB 1 ATOM 1370 C CG . ASP A 1 171 ? -43.227 51.887 76.461 1.00 78.68 ? 171 ASP A CG 1 ATOM 1371 O OD1 . ASP A 1 171 ? -44.017 52.458 77.237 1.00 80.41 ? 171 ASP A OD1 1 ATOM 1372 O OD2 . ASP A 1 171 ? -43.601 51.415 75.369 1.00 79.10 ? 171 ASP A OD2 1 ATOM 1373 N N . LEU A 1 172 ? -40.209 51.544 79.724 1.00 74.97 ? 172 LEU A N 1 ATOM 1374 C CA . LEU A 1 172 ? -39.096 50.995 80.487 1.00 74.17 ? 172 LEU A CA 1 ATOM 1375 C C . LEU A 1 172 ? -39.255 49.489 80.697 1.00 72.35 ? 172 LEU A C 1 ATOM 1376 O O . LEU A 1 172 ? -40.322 49.021 81.091 1.00 72.25 ? 172 LEU A O 1 ATOM 1377 C CB . LEU A 1 172 ? -38.992 51.702 81.835 1.00 75.32 ? 172 LEU A CB 1 ATOM 1378 C CG . LEU A 1 172 ? -37.685 51.477 82.609 1.00 76.42 ? 172 LEU A CG 1 ATOM 1379 C CD1 . LEU A 1 172 ? -36.565 52.375 82.095 1.00 76.94 ? 172 LEU A CD1 1 ATOM 1380 C CD2 . LEU A 1 172 ? -37.903 51.706 84.098 1.00 77.05 ? 172 LEU A CD2 1 ATOM 1381 N N . LEU A 1 173 ? -38.187 48.742 80.420 1.00 71.00 ? 173 LEU A N 1 ATOM 1382 C CA . LEU A 1 173 ? -38.145 47.312 80.683 1.00 69.88 ? 173 LEU A CA 1 ATOM 1383 C C . LEU A 1 173 ? -37.558 47.077 82.064 1.00 71.83 ? 173 LEU A C 1 ATOM 1384 O O . LEU A 1 173 ? -36.367 47.305 82.280 1.00 72.70 ? 173 LEU A O 1 ATOM 1385 C CB . LEU A 1 173 ? -37.291 46.584 79.646 1.00 68.92 ? 173 LEU A CB 1 ATOM 1386 C CG . LEU A 1 173 ? -37.017 45.097 79.917 1.00 68.09 ? 173 LEU A CG 1 ATOM 1387 C CD1 . LEU A 1 173 ? -38.309 44.306 80.021 1.00 67.96 ? 173 LEU A CD1 1 ATOM 1388 C CD2 . LEU A 1 173 ? -36.134 44.491 78.840 1.00 68.00 ? 173 LEU A CD2 1 ATOM 1389 N N . VAL A 1 174 ? -38.396 46.600 82.983 1.00 72.44 ? 174 VAL A N 1 ATOM 1390 C CA . VAL A 1 174 ? -37.981 46.305 84.349 1.00 72.14 ? 174 VAL A CA 1 ATOM 1391 C C . VAL A 1 174 ? -37.816 44.798 84.533 1.00 70.74 ? 174 VAL A C 1 ATOM 1392 O O . VAL A 1 174 ? -38.681 44.022 84.125 1.00 70.39 ? 174 VAL A O 1 ATOM 1393 C CB . VAL A 1 174 ? -39.013 46.828 85.363 1.00 72.67 ? 174 VAL A CB 1 ATOM 1394 C CG1 . VAL A 1 174 ? -38.511 46.619 86.785 1.00 73.66 ? 174 VAL A CG1 1 ATOM 1395 C CG2 . VAL A 1 174 ? -39.307 48.297 85.100 1.00 73.47 ? 174 VAL A CG2 1 ATOM 1396 N N . LEU A 1 175 ? -36.702 44.405 85.151 1.00 70.16 ? 175 LEU A N 1 ATOM 1397 C CA . LEU A 1 175 ? -36.375 43.006 85.394 1.00 69.85 ? 175 LEU A CA 1 ATOM 1398 C C . LEU A 1 175 ? -36.185 42.772 86.882 1.00 71.65 ? 175 LEU A C 1 ATOM 1399 O O . LEU A 1 175 ? -35.490 43.536 87.550 1.00 71.29 ? 175 LEU A O 1 ATOM 1400 C CB . LEU A 1 175 ? -35.070 42.634 84.695 1.00 70.33 ? 175 LEU A CB 1 ATOM 1401 C CG . LEU A 1 175 ? -35.027 42.721 83.169 1.00 71.71 ? 175 LEU A CG 1 ATOM 1402 C CD1 . LEU A 1 175 ? -33.590 42.612 82.676 1.00 72.96 ? 175 LEU A CD1 1 ATOM 1403 C CD2 . LEU A 1 175 ? -35.895 41.646 82.537 1.00 70.21 ? 175 LEU A CD2 1 ATOM 1404 N N . TRP A 1 176 ? -36.797 41.709 87.393 1.00 70.34 ? 176 TRP A N 1 ATOM 1405 C CA . TRP A 1 176 ? -36.560 41.267 88.757 1.00 70.44 ? 176 TRP A CA 1 ATOM 1406 C C . TRP A 1 176 ? -36.628 39.750 88.825 1.00 70.98 ? 176 TRP A C 1 ATOM 1407 O O . TRP A 1 176 ? -36.892 39.093 87.822 1.00 72.06 ? 176 TRP A O 1 ATOM 1408 C CB . TRP A 1 176 ? -37.573 41.901 89.709 1.00 70.31 ? 176 TRP A CB 1 ATOM 1409 C CG . TRP A 1 176 ? -38.974 41.439 89.513 1.00 68.29 ? 176 TRP A CG 1 ATOM 1410 C CD1 . TRP A 1 176 ? -39.622 40.474 90.218 1.00 67.56 ? 176 TRP A CD1 1 ATOM 1411 C CD2 . TRP A 1 176 ? -39.910 41.935 88.556 1.00 67.15 ? 176 TRP A CD2 1 ATOM 1412 N NE1 . TRP A 1 176 ? -40.907 40.334 89.762 1.00 66.20 ? 176 TRP A NE1 1 ATOM 1413 C CE2 . TRP A 1 176 ? -41.111 41.221 88.740 1.00 66.27 ? 176 TRP A CE2 1 ATOM 1414 C CE3 . TRP A 1 176 ? -39.850 42.913 87.557 1.00 67.19 ? 176 TRP A CE3 1 ATOM 1415 C CZ2 . TRP A 1 176 ? -42.244 41.451 87.963 1.00 66.61 ? 176 TRP A CZ2 1 ATOM 1416 C CZ3 . TRP A 1 176 ? -40.976 43.145 86.786 1.00 66.63 ? 176 TRP A CZ3 1 ATOM 1417 C CH2 . TRP A 1 176 ? -42.159 42.417 86.992 1.00 66.57 ? 176 TRP A CH2 1 ATOM 1418 N N . GLY A 1 177 ? -36.377 39.196 90.006 1.00 73.40 ? 177 GLY A N 1 ATOM 1419 C CA . GLY A 1 177 ? -36.401 37.747 90.189 1.00 73.49 ? 177 GLY A CA 1 ATOM 1420 C C . GLY A 1 177 ? -36.817 37.307 91.579 1.00 73.50 ? 177 GLY A C 1 ATOM 1421 O O . GLY A 1 177 ? -37.130 38.128 92.441 1.00 72.29 ? 177 GLY A O 1 ATOM 1422 N N . ILE A 1 178 ? -36.833 35.993 91.774 1.00 73.19 ? 178 ILE A N 1 ATOM 1423 C CA . ILE A 1 178 ? -37.100 35.393 93.073 1.00 73.65 ? 178 ILE A CA 1 ATOM 1424 C C . ILE A 1 178 ? -36.158 34.213 93.242 1.00 73.79 ? 178 ILE A C 1 ATOM 1425 O O . ILE A 1 178 ? -35.867 33.509 92.283 1.00 74.39 ? 178 ILE A O 1 ATOM 1426 C CB . ILE A 1 178 ? -38.573 34.934 93.213 1.00 74.55 ? 178 ILE A CB 1 ATOM 1427 C CG1 . ILE A 1 178 ? -38.819 34.323 94.598 1.00 76.33 ? 178 ILE A CG1 1 ATOM 1428 C CG2 . ILE A 1 178 ? -38.955 33.934 92.127 1.00 73.73 ? 178 ILE A CG2 1 ATOM 1429 C CD1 . ILE A 1 178 ? -40.270 34.001 94.884 1.00 77.15 ? 178 ILE A CD1 1 ATOM 1430 N N . HIS A 1 179 ? -35.673 34.007 94.459 1.00 76.13 ? 179 HIS A N 1 ATOM 1431 C CA . HIS A 1 179 ? -34.797 32.877 94.749 1.00 75.85 ? 179 HIS A CA 1 ATOM 1432 C C . HIS A 1 179 ? -35.579 31.724 95.376 1.00 76.11 ? 179 HIS A C 1 ATOM 1433 O O . HIS A 1 179 ? -36.351 31.912 96.320 1.00 76.76 ? 179 HIS A O 1 ATOM 1434 C CB . HIS A 1 179 ? -33.650 33.299 95.668 1.00 76.19 ? 179 HIS A CB 1 ATOM 1435 C CG . HIS A 1 179 ? -32.818 32.154 96.148 1.00 76.59 ? 179 HIS A CG 1 ATOM 1436 N ND1 . HIS A 1 179 ? -32.674 31.844 97.483 1.00 78.42 ? 179 HIS A ND1 1 ATOM 1437 C CD2 . HIS A 1 179 ? -32.108 31.225 95.467 1.00 76.54 ? 179 HIS A CD2 1 ATOM 1438 C CE1 . HIS A 1 179 ? -31.896 30.785 97.605 1.00 79.74 ? 179 HIS A CE1 1 ATOM 1439 N NE2 . HIS A 1 179 ? -31.541 30.389 96.396 1.00 79.18 ? 179 HIS A NE2 1 ATOM 1440 N N . HIS A 1 180 ? -35.374 30.532 94.830 1.00 76.22 ? 180 HIS A N 1 ATOM 1441 C CA . HIS A 1 180 ? -35.941 29.315 95.378 1.00 77.42 ? 180 HIS A CA 1 ATOM 1442 C C . HIS A 1 180 ? -34.802 28.563 96.060 1.00 79.58 ? 180 HIS A C 1 ATOM 1443 O O . HIS A 1 180 ? -33.849 28.156 95.394 1.00 79.53 ? 180 HIS A O 1 ATOM 1444 C CB . HIS A 1 180 ? -36.552 28.470 94.264 1.00 77.60 ? 180 HIS A CB 1 ATOM 1445 C CG . HIS A 1 180 ? -37.592 29.190 93.461 1.00 76.28 ? 180 HIS A CG 1 ATOM 1446 N ND1 . HIS A 1 180 ? -38.696 29.776 94.036 1.00 77.48 ? 180 HIS A ND1 1 ATOM 1447 C CD2 . HIS A 1 180 ? -37.699 29.415 92.131 1.00 75.07 ? 180 HIS A CD2 1 ATOM 1448 C CE1 . HIS A 1 180 ? -39.440 30.333 93.099 1.00 75.75 ? 180 HIS A CE1 1 ATOM 1449 N NE2 . HIS A 1 180 ? -38.857 30.128 91.933 1.00 75.76 ? 180 HIS A NE2 1 ATOM 1450 N N . PRO A 1 181 ? -34.876 28.402 97.392 1.00 80.43 ? 181 PRO A N 1 ATOM 1451 C CA . PRO A 1 181 ? -33.822 27.715 98.127 1.00 81.37 ? 181 PRO A CA 1 ATOM 1452 C C . PRO A 1 181 ? -34.027 26.206 98.146 1.00 81.06 ? 181 PRO A C 1 ATOM 1453 O O . PRO A 1 181 ? -35.068 25.723 97.704 1.00 79.19 ? 181 PRO A O 1 ATOM 1454 C CB . PRO A 1 181 ? -33.964 28.288 99.533 1.00 83.35 ? 181 PRO A CB 1 ATOM 1455 C CG . PRO A 1 181 ? -35.423 28.567 99.666 1.00 83.02 ? 181 PRO A CG 1 ATOM 1456 C CD . PRO A 1 181 ? -35.945 28.875 98.290 1.00 81.38 ? 181 PRO A CD 1 ATOM 1457 N N . ASN A 1 182 ? -33.042 25.479 98.667 1.00 82.30 ? 182 ASN A N 1 ATOM 1458 C CA . ASN A 1 182 ? -33.072 24.016 98.675 1.00 84.46 ? 182 ASN A CA 1 ATOM 1459 C C . ASN A 1 182 ? -33.932 23.417 99.783 1.00 87.74 ? 182 ASN A C 1 ATOM 1460 O O . ASN A 1 182 ? -34.648 22.437 99.547 1.00 88.53 ? 182 ASN A O 1 ATOM 1461 C CB . ASN A 1 182 ? -31.652 23.466 98.774 1.00 85.24 ? 182 ASN A CB 1 ATOM 1462 C CG . ASN A 1 182 ? -30.852 23.734 97.526 1.00 84.40 ? 182 ASN A CG 1 ATOM 1463 O OD1 . ASN A 1 182 ? -31.249 23.326 96.442 1.00 85.49 ? 182 ASN A OD1 1 ATOM 1464 N ND2 . ASN A 1 182 ? -29.736 24.439 97.661 1.00 84.88 ? 182 ASN A ND2 1 ATOM 1465 N N . ASP A 1 183 ? -33.850 24.000 100.981 1.00 89.92 ? 183 ASP A N 1 ATOM 1466 C CA . ASP A 1 183 ? -34.591 23.507 102.151 1.00 91.81 ? 183 ASP A CA 1 ATOM 1467 C C . ASP A 1 183 ? -35.004 24.641 103.100 1.00 91.01 ? 183 ASP A C 1 ATOM 1468 O O . ASP A 1 183 ? -34.736 25.817 102.832 1.00 87.92 ? 183 ASP A O 1 ATOM 1469 C CB . ASP A 1 183 ? -33.764 22.441 102.892 1.00 94.69 ? 183 ASP A CB 1 ATOM 1470 C CG . ASP A 1 183 ? -32.360 22.916 103.241 1.00 96.16 ? 183 ASP A CG 1 ATOM 1471 O OD1 . ASP A 1 183 ? -32.214 24.014 103.820 1.00 96.95 ? 183 ASP A OD1 1 ATOM 1472 O OD2 . ASP A 1 183 ? -31.399 22.176 102.945 1.00 96.68 ? 183 ASP A OD2 1 ATOM 1473 N N . ALA A 1 184 ? -35.666 24.276 104.200 1.00 92.55 ? 184 ALA A N 1 ATOM 1474 C CA . ALA A 1 184 ? -36.132 25.245 105.202 1.00 91.70 ? 184 ALA A CA 1 ATOM 1475 C C . ALA A 1 184 ? -34.975 25.901 105.960 1.00 92.43 ? 184 ALA A C 1 ATOM 1476 O O . ALA A 1 184 ? -35.079 27.057 106.384 1.00 90.40 ? 184 ALA A O 1 ATOM 1477 C CB . ALA A 1 184 ? -37.092 24.576 106.176 1.00 91.18 ? 184 ALA A CB 1 ATOM 1478 N N . ALA A 1 185 ? -33.878 25.161 106.122 1.00 94.17 ? 185 ALA A N 1 ATOM 1479 C CA . ALA A 1 185 ? -32.690 25.669 106.809 1.00 96.60 ? 185 ALA A CA 1 ATOM 1480 C C . ALA A 1 185 ? -31.951 26.729 105.985 1.00 95.65 ? 185 ALA A C 1 ATOM 1481 O O . ALA A 1 185 ? -31.332 27.634 106.549 1.00 97.72 ? 185 ALA A O 1 ATOM 1482 C CB . ALA A 1 185 ? -31.753 24.524 107.158 1.00 98.58 ? 185 ALA A CB 1 ATOM 1483 N N . GLU A 1 186 ? -32.014 26.614 104.659 1.00 92.53 ? 186 GLU A N 1 ATOM 1484 C CA . GLU A 1 186 ? -31.432 27.623 103.770 1.00 89.97 ? 186 GLU A CA 1 ATOM 1485 C C . GLU A 1 186 ? -32.274 28.902 103.778 1.00 87.18 ? 186 GLU A C 1 ATOM 1486 O O . GLU A 1 186 ? -31.731 30.010 103.797 1.00 85.26 ? 186 GLU A O 1 ATOM 1487 C CB . GLU A 1 186 ? -31.300 27.072 102.346 1.00 89.31 ? 186 GLU A CB 1 ATOM 1488 C CG . GLU A 1 186 ? -30.560 27.982 101.370 1.00 87.53 ? 186 GLU A CG 1 ATOM 1489 C CD . GLU A 1 186 ? -29.996 27.224 100.178 1.00 86.44 ? 186 GLU A CD 1 ATOM 1490 O OE1 . GLU A 1 186 ? -30.718 27.084 99.167 1.00 86.72 ? 186 GLU A OE1 1 ATOM 1491 O OE2 . GLU A 1 186 ? -28.838 26.756 100.256 1.00 85.50 ? 186 GLU A OE2 1 ATOM 1492 N N . GLN A 1 187 ? -33.597 28.738 103.776 1.00 85.43 ? 187 GLN A N 1 ATOM 1493 C CA . GLN A 1 187 ? -34.530 29.866 103.836 1.00 84.67 ? 187 GLN A CA 1 ATOM 1494 C C . GLN A 1 187 ? -34.222 30.803 105.012 1.00 87.53 ? 187 GLN A C 1 ATOM 1495 O O . GLN A 1 187 ? -34.054 32.011 104.815 1.00 85.50 ? 187 GLN A O 1 ATOM 1496 C CB . GLN A 1 187 ? -35.977 29.353 103.924 1.00 83.97 ? 187 GLN A CB 1 ATOM 1497 C CG . GLN A 1 187 ? -37.051 30.436 104.000 1.00 82.73 ? 187 GLN A CG 1 ATOM 1498 C CD . GLN A 1 187 ? -37.101 31.323 102.764 1.00 80.06 ? 187 GLN A CD 1 ATOM 1499 O OE1 . GLN A 1 187 ? -36.982 30.845 101.636 1.00 78.63 ? 187 GLN A OE1 1 ATOM 1500 N NE2 . GLN A 1 187 ? -37.290 32.621 102.973 1.00 78.85 ? 187 GLN A NE2 1 ATOM 1501 N N . THR A 1 188 ? -34.143 30.244 106.223 1.00 90.56 ? 188 THR A N 1 ATOM 1502 C CA . THR A 1 188 ? -33.856 31.043 107.419 1.00 92.15 ? 188 THR A CA 1 ATOM 1503 C C . THR A 1 188 ? -32.416 31.569 107.398 1.00 92.09 ? 188 THR A C 1 ATOM 1504 O O . THR A 1 188 ? -32.165 32.712 107.782 1.00 92.51 ? 188 THR A O 1 ATOM 1505 C CB . THR A 1 188 ? -34.110 30.268 108.736 1.00 95.87 ? 188 THR A CB 1 ATOM 1506 O OG1 . THR A 1 188 ? -33.195 29.172 108.853 1.00 98.89 ? 188 THR A OG1 1 ATOM 1507 C CG2 . THR A 1 188 ? -35.546 29.750 108.801 1.00 95.75 ? 188 THR A CG2 1 ATOM 1508 N N . LYS A 1 189 ? -31.480 30.748 106.927 1.00 91.04 ? 189 LYS A N 1 ATOM 1509 C CA . LYS A 1 189 ? -30.074 31.146 106.857 1.00 92.24 ? 189 LYS A CA 1 ATOM 1510 C C . LYS A 1 189 ? -29.834 32.412 106.022 1.00 91.33 ? 189 LYS A C 1 ATOM 1511 O O . LYS A 1 189 ? -28.928 33.185 106.329 1.00 90.34 ? 189 LYS A O 1 ATOM 1512 C CB . LYS A 1 189 ? -29.218 29.991 106.319 1.00 93.78 ? 189 LYS A CB 1 ATOM 1513 C CG . LYS A 1 189 ? -27.729 30.304 106.222 1.00 96.37 ? 189 LYS A CG 1 ATOM 1514 C CD . LYS A 1 189 ? -26.939 29.153 105.616 1.00 97.99 ? 189 LYS A CD 1 ATOM 1515 C CE . LYS A 1 189 ? -25.691 29.660 104.905 1.00 98.35 ? 189 LYS A CE 1 ATOM 1516 N NZ . LYS A 1 189 ? -24.987 28.581 104.160 1.00 98.25 ? 189 LYS A NZ 1 ATOM 1517 N N . LEU A 1 190 ? -30.628 32.617 104.971 1.00 90.65 ? 190 LEU A N 1 ATOM 1518 C CA . LEU A 1 190 ? -30.461 33.783 104.095 1.00 90.82 ? 190 LEU A CA 1 ATOM 1519 C C . LEU A 1 190 ? -31.437 34.918 104.394 1.00 91.17 ? 190 LEU A C 1 ATOM 1520 O O . LEU A 1 190 ? -31.086 36.089 104.247 1.00 89.65 ? 190 LEU A O 1 ATOM 1521 C CB . LEU A 1 190 ? -30.616 33.385 102.623 1.00 89.76 ? 190 LEU A CB 1 ATOM 1522 C CG . LEU A 1 190 ? -29.732 32.261 102.081 1.00 90.63 ? 190 LEU A CG 1 ATOM 1523 C CD1 . LEU A 1 190 ? -29.818 32.231 100.563 1.00 88.45 ? 190 LEU A CD1 1 ATOM 1524 C CD2 . LEU A 1 190 ? -28.287 32.402 102.538 1.00 92.29 ? 190 LEU A CD2 1 ATOM 1525 N N . TYR A 1 191 ? -32.662 34.572 104.786 1.00 92.89 ? 191 TYR A N 1 ATOM 1526 C CA . TYR A 1 191 ? -33.748 35.551 104.895 1.00 93.82 ? 191 TYR A CA 1 ATOM 1527 C C . TYR A 1 191 ? -34.466 35.584 106.257 1.00 97.53 ? 191 TYR A C 1 ATOM 1528 O O . TYR A 1 191 ? -35.357 36.412 106.463 1.00 96.42 ? 191 TYR A O 1 ATOM 1529 C CB . TYR A 1 191 ? -34.776 35.280 103.790 1.00 92.32 ? 191 TYR A CB 1 ATOM 1530 C CG . TYR A 1 191 ? -34.165 34.969 102.438 1.00 90.26 ? 191 TYR A CG 1 ATOM 1531 C CD1 . TYR A 1 191 ? -33.476 35.945 101.724 1.00 90.67 ? 191 TYR A CD1 1 ATOM 1532 C CD2 . TYR A 1 191 ? -34.266 33.696 101.879 1.00 89.54 ? 191 TYR A CD2 1 ATOM 1533 C CE1 . TYR A 1 191 ? -32.917 35.672 100.484 1.00 90.17 ? 191 TYR A CE1 1 ATOM 1534 C CE2 . TYR A 1 191 ? -33.708 33.410 100.643 1.00 89.49 ? 191 TYR A CE2 1 ATOM 1535 C CZ . TYR A 1 191 ? -33.033 34.405 99.949 1.00 89.33 ? 191 TYR A CZ 1 ATOM 1536 O OH . TYR A 1 191 ? -32.471 34.137 98.724 1.00 85.12 ? 191 TYR A OH 1 ATOM 1537 N N . ARG A 1 192 ? -34.080 34.693 107.172 1.00 100.26 ? 192 ARG A N 1 ATOM 1538 C CA . ARG A 1 192 ? -34.730 34.523 108.482 1.00 103.14 ? 192 ARG A CA 1 ATOM 1539 C C . ARG A 1 192 ? -36.207 34.097 108.410 1.00 102.14 ? 192 ARG A C 1 ATOM 1540 O O . ARG A 1 192 ? -36.573 33.045 108.947 1.00 102.67 ? 192 ARG A O 1 ATOM 1541 C CB . ARG A 1 192 ? -34.582 35.776 109.364 1.00 106.35 ? 192 ARG A CB 1 ATOM 1542 C CG . ARG A 1 192 ? -34.193 35.451 110.808 1.00 111.91 ? 192 ARG A CG 1 ATOM 1543 C CD . ARG A 1 192 ? -34.847 36.367 111.833 1.00 115.14 ? 192 ARG A CD 1 ATOM 1544 N NE . ARG A 1 192 ? -36.136 35.851 112.309 1.00 117.00 ? 192 ARG A NE 1 ATOM 1545 C CZ . ARG A 1 192 ? -36.321 35.108 113.405 1.00 120.23 ? 192 ARG A CZ 1 ATOM 1546 N NH1 . ARG A 1 192 ? -35.305 34.757 114.192 1.00 121.21 ? 192 ARG A NH1 1 ATOM 1547 N NH2 . ARG A 1 192 ? -37.549 34.707 113.721 1.00 121.00 ? 192 ARG A NH2 1 ATOM 1548 N N . ASN A 1 193 ? -37.045 34.909 107.762 1.00 99.52 ? 193 ASN A N 1 ATOM 1549 C CA . ASN A 1 193 ? -38.483 34.636 107.677 1.00 98.20 ? 193 ASN A CA 1 ATOM 1550 C C . ASN A 1 193 ? -38.725 33.302 106.968 1.00 96.83 ? 193 ASN A C 1 ATOM 1551 O O . ASN A 1 193 ? -38.161 33.066 105.904 1.00 95.49 ? 193 ASN A O 1 ATOM 1552 C CB . ASN A 1 193 ? -39.222 35.756 106.931 1.00 97.60 ? 193 ASN A CB 1 ATOM 1553 C CG . ASN A 1 193 ? -38.863 37.149 107.434 1.00 99.53 ? 193 ASN A CG 1 ATOM 1554 O OD1 . ASN A 1 193 ? -37.705 37.433 107.727 1.00 103.04 ? 193 ASN A OD1 1 ATOM 1555 N ND2 . ASN A 1 193 ? -39.854 38.033 107.508 1.00 99.01 ? 193 ASN A ND2 1 ATOM 1556 N N . PRO A 1 194 ? -39.550 32.417 107.558 1.00 98.14 ? 194 PRO A N 1 ATOM 1557 C CA . PRO A 1 194 ? -39.762 31.104 106.945 1.00 96.51 ? 194 PRO A CA 1 ATOM 1558 C C . PRO A 1 194 ? -40.699 31.160 105.740 1.00 93.70 ? 194 PRO A C 1 ATOM 1559 O O . PRO A 1 194 ? -40.442 30.495 104.738 1.00 91.28 ? 194 PRO A O 1 ATOM 1560 C CB . PRO A 1 194 ? -40.390 30.288 108.075 1.00 98.26 ? 194 PRO A CB 1 ATOM 1561 C CG . PRO A 1 194 ? -41.111 31.294 108.905 1.00 100.09 ? 194 PRO A CG 1 ATOM 1562 C CD . PRO A 1 194 ? -40.360 32.593 108.779 1.00 99.80 ? 194 PRO A CD 1 ATOM 1563 N N . THR A 1 195 ? -41.771 31.944 105.845 1.00 92.27 ? 195 THR A N 1 ATOM 1564 C CA . THR A 1 195 ? -42.742 32.088 104.769 1.00 90.44 ? 195 THR A CA 1 ATOM 1565 C C . THR A 1 195 ? -42.635 33.497 104.201 1.00 87.81 ? 195 THR A C 1 ATOM 1566 O O . THR A 1 195 ? -42.997 34.465 104.867 1.00 88.21 ? 195 THR A O 1 ATOM 1567 C CB . THR A 1 195 ? -44.182 31.857 105.275 1.00 91.21 ? 195 THR A CB 1 ATOM 1568 O OG1 . THR A 1 195 ? -44.237 30.649 106.038 1.00 92.08 ? 195 THR A OG1 1 ATOM 1569 C CG2 . THR A 1 195 ? -45.156 31.757 104.109 1.00 90.35 ? 195 THR A CG2 1 ATOM 1570 N N . THR A 1 196 ? -42.137 33.608 102.975 1.00 85.35 ? 196 THR A N 1 ATOM 1571 C CA . THR A 1 196 ? -41.951 34.909 102.344 1.00 83.80 ? 196 THR A CA 1 ATOM 1572 C C . THR A 1 196 ? -42.771 35.039 101.073 1.00 81.60 ? 196 THR A C 1 ATOM 1573 O O . THR A 1 196 ? -43.401 34.083 100.619 1.00 79.45 ? 196 THR A O 1 ATOM 1574 C CB . THR A 1 196 ? -40.469 35.164 102.018 1.00 84.17 ? 196 THR A CB 1 ATOM 1575 O OG1 . THR A 1 196 ? -39.979 34.120 101.168 1.00 83.46 ? 196 THR A OG1 1 ATOM 1576 C CG2 . THR A 1 196 ? -39.646 35.209 103.298 1.00 85.89 ? 196 THR A CG2 1 ATOM 1577 N N . TYR A 1 197 ? -42.764 36.245 100.519 1.00 81.12 ? 197 TYR A N 1 ATOM 1578 C CA . TYR A 1 197 ? -43.473 36.547 99.291 1.00 79.50 ? 197 TYR A CA 1 ATOM 1579 C C . TYR A 1 197 ? -42.840 37.761 98.616 1.00 79.40 ? 197 TYR A C 1 ATOM 1580 O O . TYR A 1 197 ? -42.070 38.486 99.236 1.00 78.74 ? 197 TYR A O 1 ATOM 1581 C CB . TYR A 1 197 ? -44.940 36.841 99.599 1.00 80.40 ? 197 TYR A CB 1 ATOM 1582 C CG . TYR A 1 197 ? -45.154 38.131 100.365 1.00 82.41 ? 197 TYR A CG 1 ATOM 1583 C CD1 . TYR A 1 197 ? -45.059 38.163 101.755 1.00 84.77 ? 197 TYR A CD1 1 ATOM 1584 C CD2 . TYR A 1 197 ? -45.445 39.321 99.701 1.00 82.19 ? 197 TYR A CD2 1 ATOM 1585 C CE1 . TYR A 1 197 ? -45.254 39.341 102.459 1.00 85.18 ? 197 TYR A CE1 1 ATOM 1586 C CE2 . TYR A 1 197 ? -45.639 40.503 100.397 1.00 83.64 ? 197 TYR A CE2 1 ATOM 1587 C CZ . TYR A 1 197 ? -45.541 40.508 101.780 1.00 85.12 ? 197 TYR A CZ 1 ATOM 1588 O OH . TYR A 1 197 ? -45.730 41.678 102.483 1.00 85.14 ? 197 TYR A OH 1 ATOM 1589 N N . ILE A 1 198 ? -43.160 37.965 97.340 1.00 79.09 ? 198 ILE A N 1 ATOM 1590 C CA . ILE A 1 198 ? -42.795 39.190 96.629 1.00 78.34 ? 198 ILE A CA 1 ATOM 1591 C C . ILE A 1 198 ? -44.016 39.664 95.861 1.00 77.63 ? 198 ILE A C 1 ATOM 1592 O O . ILE A 1 198 ? -44.454 38.996 94.925 1.00 80.30 ? 198 ILE A O 1 ATOM 1593 C CB . ILE A 1 198 ? -41.652 38.971 95.616 1.00 78.18 ? 198 ILE A CB 1 ATOM 1594 C CG1 . ILE A 1 198 ? -40.383 38.461 96.303 1.00 79.23 ? 198 ILE A CG1 1 ATOM 1595 C CG2 . ILE A 1 198 ? -41.344 40.270 94.880 1.00 78.54 ? 198 ILE A CG2 1 ATOM 1596 C CD1 . ILE A 1 198 ? -39.481 37.661 95.388 1.00 78.77 ? 198 ILE A CD1 1 ATOM 1597 N N . SER A 1 199 ? -44.569 40.807 96.248 1.00 76.54 ? 199 SER A N 1 ATOM 1598 C CA . SER A 1 199 ? -45.712 41.363 95.539 1.00 76.30 ? 199 SER A CA 1 ATOM 1599 C C . SER A 1 199 ? -45.252 42.487 94.622 1.00 74.39 ? 199 SER A C 1 ATOM 1600 O O . SER A 1 199 ? -44.486 43.348 95.031 1.00 74.28 ? 199 SER A O 1 ATOM 1601 C CB . SER A 1 199 ? -46.771 41.862 96.520 1.00 78.32 ? 199 SER A CB 1 ATOM 1602 O OG . SER A 1 199 ? -46.252 42.878 97.354 1.00 81.74 ? 199 SER A OG 1 ATOM 1603 N N . VAL A 1 200 ? -45.716 42.456 93.375 1.00 75.03 ? 200 VAL A N 1 ATOM 1604 C CA . VAL A 1 200 ? -45.364 43.461 92.377 1.00 74.28 ? 200 VAL A CA 1 ATOM 1605 C C . VAL A 1 200 ? -46.644 44.019 91.779 1.00 75.18 ? 200 VAL A C 1 ATOM 1606 O O . VAL A 1 200 ? -47.507 43.260 91.331 1.00 76.47 ? 200 VAL A O 1 ATOM 1607 C CB . VAL A 1 200 ? -44.510 42.866 91.240 1.00 73.86 ? 200 VAL A CB 1 ATOM 1608 C CG1 . VAL A 1 200 ? -43.841 43.976 90.445 1.00 74.43 ? 200 VAL A CG1 1 ATOM 1609 C CG2 . VAL A 1 200 ? -43.463 41.911 91.793 1.00 74.67 ? 200 VAL A CG2 1 ATOM 1610 N N . GLY A 1 201 ? -46.762 45.343 91.768 1.00 76.80 ? 201 GLY A N 1 ATOM 1611 C CA . GLY A 1 201 ? -47.945 46.007 91.229 1.00 78.55 ? 201 GLY A CA 1 ATOM 1612 C C . GLY A 1 201 ? -47.607 47.144 90.284 1.00 79.20 ? 201 GLY A C 1 ATOM 1613 O O . GLY A 1 201 ? -46.632 47.863 90.493 1.00 80.05 ? 201 GLY A O 1 ATOM 1614 N N . THR A 1 202 ? -48.405 47.284 89.229 1.00 79.43 ? 202 THR A N 1 ATOM 1615 C CA . THR A 1 202 ? -48.391 48.474 88.375 1.00 81.01 ? 202 THR A CA 1 ATOM 1616 C C . THR A 1 202 ? -49.839 48.809 88.024 1.00 82.59 ? 202 THR A C 1 ATOM 1617 O O . THR A 1 202 ? -50.771 48.304 88.660 1.00 83.25 ? 202 THR A O 1 ATOM 1618 C CB . THR A 1 202 ? -47.576 48.267 87.070 1.00 80.88 ? 202 THR A CB 1 ATOM 1619 O OG1 . THR A 1 202 ? -48.283 47.402 86.167 1.00 80.52 ? 202 THR A OG1 1 ATOM 1620 C CG2 . THR A 1 202 ? -46.207 47.688 87.360 1.00 80.41 ? 202 THR A CG2 1 ATOM 1621 N N . SER A 1 203 ? -50.022 49.666 87.020 1.00 84.04 ? 203 SER A N 1 ATOM 1622 C CA . SER A 1 203 ? -51.335 49.905 86.419 1.00 84.42 ? 203 SER A CA 1 ATOM 1623 C C . SER A 1 203 ? -52.010 48.599 86.071 1.00 80.95 ? 203 SER A C 1 ATOM 1624 O O . SER A 1 203 ? -53.194 48.411 86.336 1.00 79.89 ? 203 SER A O 1 ATOM 1625 C CB . SER A 1 203 ? -51.192 50.711 85.128 1.00 86.15 ? 203 SER A CB 1 ATOM 1626 O OG . SER A 1 203 ? -50.440 51.883 85.350 1.00 90.57 ? 203 SER A OG 1 ATOM 1627 N N . THR A 1 204 ? -51.239 47.704 85.464 1.00 78.82 ? 204 THR A N 1 ATOM 1628 C CA . THR A 1 204 ? -51.765 46.450 84.949 1.00 77.93 ? 204 THR A CA 1 ATOM 1629 C C . THR A 1 204 ? -51.362 45.267 85.819 1.00 77.89 ? 204 THR A C 1 ATOM 1630 O O . THR A 1 204 ? -52.189 44.407 86.121 1.00 81.12 ? 204 THR A O 1 ATOM 1631 C CB . THR A 1 204 ? -51.285 46.211 83.505 1.00 75.90 ? 204 THR A CB 1 ATOM 1632 O OG1 . THR A 1 204 ? -49.876 45.941 83.497 1.00 74.62 ? 204 THR A OG1 1 ATOM 1633 C CG2 . THR A 1 204 ? -51.577 47.432 82.637 1.00 75.32 ? 204 THR A CG2 1 ATOM 1634 N N . LEU A 1 205 ? -50.099 45.229 86.231 1.00 76.83 ? 205 LEU A N 1 ATOM 1635 C CA . LEU A 1 205 ? -49.557 44.059 86.918 1.00 76.30 ? 205 LEU A CA 1 ATOM 1636 C C . LEU A 1 205 ? -50.138 43.855 88.327 1.00 76.72 ? 205 LEU A C 1 ATOM 1637 O O . LEU A 1 205 ? -50.283 44.808 89.099 1.00 76.03 ? 205 LEU A O 1 ATOM 1638 C CB . LEU A 1 205 ? -48.027 44.149 86.979 1.00 76.17 ? 205 LEU A CB 1 ATOM 1639 C CG . LEU A 1 205 ? -47.274 42.899 87.448 1.00 76.70 ? 205 LEU A CG 1 ATOM 1640 C CD1 . LEU A 1 205 ? -47.638 41.675 86.618 1.00 76.42 ? 205 LEU A CD1 1 ATOM 1641 C CD2 . LEU A 1 205 ? -45.776 43.147 87.399 1.00 76.44 ? 205 LEU A CD2 1 ATOM 1642 N N . ASN A 1 206 ? -50.479 42.604 88.638 1.00 75.69 ? 206 ASN A N 1 ATOM 1643 C CA . ASN A 1 206 ? -50.916 42.213 89.978 1.00 75.47 ? 206 ASN A CA 1 ATOM 1644 C C . ASN A 1 206 ? -50.291 40.871 90.374 1.00 73.70 ? 206 ASN A C 1 ATOM 1645 O O . ASN A 1 206 ? -50.957 39.839 90.392 1.00 72.77 ? 206 ASN A O 1 ATOM 1646 C CB . ASN A 1 206 ? -52.446 42.144 90.042 1.00 76.70 ? 206 ASN A CB 1 ATOM 1647 C CG . ASN A 1 206 ? -52.961 41.770 91.421 1.00 78.81 ? 206 ASN A CG 1 ATOM 1648 O OD1 . ASN A 1 206 ? -52.309 42.032 92.432 1.00 81.30 ? 206 ASN A OD1 1 ATOM 1649 N ND2 . ASN A 1 206 ? -54.135 41.146 91.468 1.00 79.34 ? 206 ASN A ND2 1 ATOM 1650 N N . GLN A 1 207 ? -49.006 40.904 90.710 1.00 72.92 ? 207 GLN A N 1 ATOM 1651 C CA . GLN A 1 207 ? -48.233 39.691 90.963 1.00 74.46 ? 207 GLN A CA 1 ATOM 1652 C C . GLN A 1 207 ? -47.977 39.451 92.454 1.00 75.21 ? 207 GLN A C 1 ATOM 1653 O O . GLN A 1 207 ? -47.912 40.389 93.238 1.00 73.82 ? 207 GLN A O 1 ATOM 1654 C CB . GLN A 1 207 ? -46.906 39.794 90.215 1.00 75.31 ? 207 GLN A CB 1 ATOM 1655 C CG . GLN A 1 207 ? -45.963 38.616 90.378 1.00 75.95 ? 207 GLN A CG 1 ATOM 1656 C CD . GLN A 1 207 ? -44.702 38.786 89.557 1.00 76.49 ? 207 GLN A CD 1 ATOM 1657 O OE1 . GLN A 1 207 ? -43.654 39.175 90.079 1.00 77.35 ? 207 GLN A OE1 1 ATOM 1658 N NE2 . GLN A 1 207 ? -44.802 38.521 88.260 1.00 76.47 ? 207 GLN A NE2 1 ATOM 1659 N N . ARG A 1 208 ? -47.826 38.184 92.826 1.00 76.80 ? 208 ARG A N 1 ATOM 1660 C CA . ARG A 1 208 ? -47.517 37.794 94.202 1.00 80.03 ? 208 ARG A CA 1 ATOM 1661 C C . ARG A 1 208 ? -46.743 36.476 94.189 1.00 79.88 ? 208 ARG A C 1 ATOM 1662 O O . ARG A 1 208 ? -47.330 35.396 94.284 1.00 80.14 ? 208 ARG A O 1 ATOM 1663 C CB . ARG A 1 208 ? -48.810 37.644 95.012 1.00 83.46 ? 208 ARG A CB 1 ATOM 1664 C CG . ARG A 1 208 ? -48.633 37.221 96.467 1.00 85.38 ? 208 ARG A CG 1 ATOM 1665 C CD . ARG A 1 208 ? -48.753 38.391 97.427 1.00 87.33 ? 208 ARG A CD 1 ATOM 1666 N NE . ARG A 1 208 ? -48.746 37.951 98.822 1.00 90.43 ? 208 ARG A NE 1 ATOM 1667 C CZ . ARG A 1 208 ? -48.819 38.766 99.875 1.00 93.66 ? 208 ARG A CZ 1 ATOM 1668 N NH1 . ARG A 1 208 ? -48.912 40.083 99.710 1.00 93.99 ? 208 ARG A NH1 1 ATOM 1669 N NH2 . ARG A 1 208 ? -48.797 38.262 101.106 1.00 95.38 ? 208 ARG A NH2 1 ATOM 1670 N N . LEU A 1 209 ? -45.424 36.575 94.069 1.00 79.63 ? 209 LEU A N 1 ATOM 1671 C CA . LEU A 1 209 ? -44.567 35.399 93.958 1.00 79.26 ? 209 LEU A CA 1 ATOM 1672 C C . LEU A 1 209 ? -44.261 34.831 95.336 1.00 80.33 ? 209 LEU A C 1 ATOM 1673 O O . LEU A 1 209 ? -44.101 35.583 96.296 1.00 79.70 ? 209 LEU A O 1 ATOM 1674 C CB . LEU A 1 209 ? -43.258 35.763 93.260 1.00 79.77 ? 209 LEU A CB 1 ATOM 1675 C CG . LEU A 1 209 ? -43.362 36.466 91.904 1.00 80.52 ? 209 LEU A CG 1 ATOM 1676 C CD1 . LEU A 1 209 ? -41.972 36.810 91.388 1.00 80.85 ? 209 LEU A CD1 1 ATOM 1677 C CD2 . LEU A 1 209 ? -44.123 35.612 90.895 1.00 80.33 ? 209 LEU A CD2 1 ATOM 1678 N N . VAL A 1 210 ? -44.181 33.507 95.426 1.00 81.25 ? 210 VAL A N 1 ATOM 1679 C CA . VAL A 1 210 ? -43.791 32.829 96.664 1.00 83.53 ? 210 VAL A CA 1 ATOM 1680 C C . VAL A 1 210 ? -42.768 31.739 96.350 1.00 83.40 ? 210 VAL A C 1 ATOM 1681 O O . VAL A 1 210 ? -42.904 31.041 95.339 1.00 81.97 ? 210 VAL A O 1 ATOM 1682 C CB . VAL A 1 210 ? -45.002 32.224 97.416 1.00 85.51 ? 210 VAL A CB 1 ATOM 1683 C CG1 . VAL A 1 210 ? -45.912 33.329 97.933 1.00 85.97 ? 210 VAL A CG1 1 ATOM 1684 C CG2 . VAL A 1 210 ? -45.787 31.255 96.539 1.00 86.08 ? 210 VAL A CG2 1 ATOM 1685 N N . PRO A 1 211 ? -41.734 31.593 97.204 1.00 84.06 ? 211 PRO A N 1 ATOM 1686 C CA . PRO A 1 211 ? -40.690 30.613 96.905 1.00 84.56 ? 211 PRO A CA 1 ATOM 1687 C C . PRO A 1 211 ? -41.165 29.170 97.015 1.00 84.84 ? 211 PRO A C 1 ATOM 1688 O O . PRO A 1 211 ? -41.764 28.785 98.017 1.00 85.87 ? 211 PRO A O 1 ATOM 1689 C CB . PRO A 1 211 ? -39.610 30.895 97.960 1.00 85.12 ? 211 PRO A CB 1 ATOM 1690 C CG . PRO A 1 211 ? -39.920 32.243 98.494 1.00 85.36 ? 211 PRO A CG 1 ATOM 1691 C CD . PRO A 1 211 ? -41.406 32.381 98.402 1.00 85.09 ? 211 PRO A CD 1 ATOM 1692 N N . ARG A 1 212 ? -40.905 28.395 95.969 1.00 84.17 ? 212 ARG A N 1 ATOM 1693 C CA . ARG A 1 212 ? -41.192 26.973 95.954 1.00 85.98 ? 212 ARG A CA 1 ATOM 1694 C C . ARG A 1 212 ? -39.934 26.207 96.319 1.00 85.96 ? 212 ARG A C 1 ATOM 1695 O O . ARG A 1 212 ? -38.933 26.274 95.607 1.00 85.50 ? 212 ARG A O 1 ATOM 1696 C CB . ARG A 1 212 ? -41.690 26.557 94.571 1.00 85.88 ? 212 ARG A CB 1 ATOM 1697 C CG . ARG A 1 212 ? -43.108 27.033 94.280 1.00 86.77 ? 212 ARG A CG 1 ATOM 1698 C CD . ARG A 1 212 ? -43.217 27.726 92.938 1.00 86.53 ? 212 ARG A CD 1 ATOM 1699 N NE . ARG A 1 212 ? -42.591 26.952 91.871 1.00 87.36 ? 212 ARG A NE 1 ATOM 1700 C CZ . ARG A 1 212 ? -42.137 27.469 90.730 1.00 90.17 ? 212 ARG A CZ 1 ATOM 1701 N NH1 . ARG A 1 212 ? -42.231 28.774 90.480 1.00 89.70 ? 212 ARG A NH1 1 ATOM 1702 N NH2 . ARG A 1 212 ? -41.578 26.676 89.826 1.00 92.76 ? 212 ARG A NH2 1 ATOM 1703 N N . ILE A 1 213 ? -39.988 25.490 97.437 1.00 87.08 ? 213 ILE A N 1 ATOM 1704 C CA . ILE A 1 213 ? -38.866 24.674 97.887 1.00 87.15 ? 213 ILE A CA 1 ATOM 1705 C C . ILE A 1 213 ? -38.960 23.268 97.287 1.00 87.09 ? 213 ILE A C 1 ATOM 1706 O O . ILE A 1 213 ? -40.036 22.667 97.249 1.00 87.01 ? 213 ILE A O 1 ATOM 1707 C CB . ILE A 1 213 ? -38.808 24.604 99.428 1.00 88.18 ? 213 ILE A CB 1 ATOM 1708 C CG1 . ILE A 1 213 ? -38.515 25.998 99.995 1.00 88.72 ? 213 ILE A CG1 1 ATOM 1709 C CG2 . ILE A 1 213 ? -37.742 23.618 99.889 1.00 88.89 ? 213 ILE A CG2 1 ATOM 1710 C CD1 . ILE A 1 213 ? -38.782 26.136 101.479 1.00 90.56 ? 213 ILE A CD1 1 ATOM 1711 N N . ALA A 1 214 ? -37.824 22.769 96.807 1.00 86.30 ? 214 ALA A N 1 ATOM 1712 C CA . ALA A 1 214 ? -37.707 21.404 96.299 1.00 86.56 ? 214 ALA A CA 1 ATOM 1713 C C . ALA A 1 214 ? -36.232 21.036 96.182 1.00 86.92 ? 214 ALA A C 1 ATOM 1714 O O . ALA A 1 214 ? -35.385 21.904 95.962 1.00 84.79 ? 214 ALA A O 1 ATOM 1715 C CB . ALA A 1 214 ? -38.389 21.272 94.948 1.00 85.54 ? 214 ALA A CB 1 ATOM 1716 N N . THR A 1 215 ? -35.922 19.753 96.333 1.00 88.80 ? 215 THR A N 1 ATOM 1717 C CA . THR A 1 215 ? -34.537 19.305 96.233 1.00 89.55 ? 215 THR A CA 1 ATOM 1718 C C . THR A 1 215 ? -34.249 18.993 94.775 1.00 86.71 ? 215 THR A C 1 ATOM 1719 O O . THR A 1 215 ? -34.935 18.181 94.158 1.00 86.63 ? 215 THR A O 1 ATOM 1720 C CB . THR A 1 215 ? -34.249 18.080 97.120 1.00 92.80 ? 215 THR A CB 1 ATOM 1721 O OG1 . THR A 1 215 ? -34.844 16.912 96.545 1.00 94.53 ? 215 THR A OG1 1 ATOM 1722 C CG2 . THR A 1 215 ? -34.789 18.302 98.542 1.00 94.00 ? 215 THR A CG2 1 ATOM 1723 N N . ARG A 1 216 ? -33.233 19.654 94.232 1.00 84.44 ? 216 ARG A N 1 ATOM 1724 C CA . ARG A 1 216 ? -32.978 19.643 92.803 1.00 82.45 ? 216 ARG A CA 1 ATOM 1725 C C . ARG A 1 216 ? -31.547 19.251 92.499 1.00 82.43 ? 216 ARG A C 1 ATOM 1726 O O . ARG A 1 216 ? -30.644 19.479 93.301 1.00 80.10 ? 216 ARG A O 1 ATOM 1727 C CB . ARG A 1 216 ? -33.237 21.035 92.230 1.00 80.35 ? 216 ARG A CB 1 ATOM 1728 C CG . ARG A 1 216 ? -34.644 21.552 92.467 1.00 80.00 ? 216 ARG A CG 1 ATOM 1729 C CD . ARG A 1 216 ? -34.729 23.042 92.203 1.00 78.68 ? 216 ARG A CD 1 ATOM 1730 N NE . ARG A 1 216 ? -34.343 23.838 93.369 1.00 79.31 ? 216 ARG A NE 1 ATOM 1731 C CZ . ARG A 1 216 ? -35.187 24.443 94.208 1.00 78.75 ? 216 ARG A CZ 1 ATOM 1732 N NH1 . ARG A 1 216 ? -36.502 24.358 94.051 1.00 78.55 ? 216 ARG A NH1 1 ATOM 1733 N NH2 . ARG A 1 216 ? -34.708 25.143 95.227 1.00 79.49 ? 216 ARG A NH2 1 ATOM 1734 N N . SER A 1 217 ? -31.348 18.680 91.316 1.00 83.44 ? 217 SER A N 1 ATOM 1735 C CA . SER A 1 217 ? -30.016 18.352 90.834 1.00 84.98 ? 217 SER A CA 1 ATOM 1736 C C . SER A 1 217 ? -29.176 19.619 90.754 1.00 84.50 ? 217 SER A C 1 ATOM 1737 O O . SER A 1 217 ? -29.688 20.691 90.426 1.00 83.78 ? 217 SER A O 1 ATOM 1738 C CB . SER A 1 217 ? -30.096 17.694 89.455 1.00 84.86 ? 217 SER A CB 1 ATOM 1739 O OG . SER A 1 217 ? -31.001 16.602 89.464 1.00 86.35 ? 217 SER A OG 1 ATOM 1740 N N . LYS A 1 218 ? -27.892 19.502 91.076 1.00 85.96 ? 218 LYS A N 1 ATOM 1741 C CA . LYS A 1 218 ? -26.980 20.623 90.924 1.00 85.87 ? 218 LYS A CA 1 ATOM 1742 C C . LYS A 1 218 ? -26.858 20.945 89.444 1.00 84.40 ? 218 LYS A C 1 ATOM 1743 O O . LYS A 1 218 ? -26.765 20.049 88.609 1.00 83.80 ? 218 LYS A O 1 ATOM 1744 C CB . LYS A 1 218 ? -25.597 20.316 91.507 1.00 88.81 ? 218 LYS A CB 1 ATOM 1745 C CG . LYS A 1 218 ? -25.521 20.419 93.021 1.00 91.76 ? 218 LYS A CG 1 ATOM 1746 C CD . LYS A 1 218 ? -24.126 20.078 93.529 1.00 94.44 ? 218 LYS A CD 1 ATOM 1747 C CE . LYS A 1 218 ? -24.031 20.188 95.042 1.00 96.97 ? 218 LYS A CE 1 ATOM 1748 N NZ . LYS A 1 218 ? -24.925 19.225 95.743 1.00 98.37 ? 218 LYS A NZ 1 ATOM 1749 N N . VAL A 1 219 ? -26.902 22.232 89.131 1.00 82.85 ? 219 VAL A N 1 ATOM 1750 C CA . VAL A 1 219 ? -26.653 22.720 87.792 1.00 81.68 ? 219 VAL A CA 1 ATOM 1751 C C . VAL A 1 219 ? -25.701 23.895 87.957 1.00 81.58 ? 219 VAL A C 1 ATOM 1752 O O . VAL A 1 219 ? -26.037 24.874 88.617 1.00 80.21 ? 219 VAL A O 1 ATOM 1753 C CB . VAL A 1 219 ? -27.960 23.158 87.102 1.00 80.89 ? 219 VAL A CB 1 ATOM 1754 C CG1 . VAL A 1 219 ? -27.669 23.828 85.765 1.00 79.83 ? 219 VAL A CG1 1 ATOM 1755 C CG2 . VAL A 1 219 ? -28.879 21.960 86.913 1.00 81.09 ? 219 VAL A CG2 1 ATOM 1756 N N . ASN A 1 220 ? -24.514 23.782 87.365 1.00 82.97 ? 220 ASN A N 1 ATOM 1757 C CA . ASN A 1 220 ? -23.416 24.709 87.626 1.00 84.74 ? 220 ASN A CA 1 ATOM 1758 C C . ASN A 1 220 ? -23.085 24.764 89.121 1.00 85.28 ? 220 ASN A C 1 ATOM 1759 O O . ASN A 1 220 ? -22.847 25.835 89.681 1.00 86.08 ? 220 ASN A O 1 ATOM 1760 C CB . ASN A 1 220 ? -23.720 26.113 87.080 1.00 85.07 ? 220 ASN A CB 1 ATOM 1761 C CG . ASN A 1 220 ? -23.885 26.136 85.571 1.00 85.58 ? 220 ASN A CG 1 ATOM 1762 O OD1 . ASN A 1 220 ? -23.937 25.092 84.914 1.00 87.09 ? 220 ASN A OD1 1 ATOM 1763 N ND2 . ASN A 1 220 ? -23.968 27.338 85.011 1.00 84.82 ? 220 ASN A ND2 1 ATOM 1764 N N . GLY A 1 221 ? -23.086 23.596 89.760 1.00 84.79 ? 221 GLY A N 1 ATOM 1765 C CA . GLY A 1 221 ? -22.693 23.471 91.160 1.00 85.10 ? 221 GLY A CA 1 ATOM 1766 C C . GLY A 1 221 ? -23.689 23.993 92.181 1.00 83.52 ? 221 GLY A C 1 ATOM 1767 O O . GLY A 1 221 ? -23.345 24.135 93.353 1.00 83.31 ? 221 GLY A O 1 ATOM 1768 N N . GLN A 1 222 ? -24.921 24.265 91.754 1.00 80.45 ? 222 GLN A N 1 ATOM 1769 C CA . GLN A 1 222 ? -25.941 24.808 92.648 1.00 80.13 ? 222 GLN A CA 1 ATOM 1770 C C . GLN A 1 222 ? -27.303 24.150 92.446 1.00 80.34 ? 222 GLN A C 1 ATOM 1771 O O . GLN A 1 222 ? -27.731 23.922 91.316 1.00 80.20 ? 222 GLN A O 1 ATOM 1772 C CB . GLN A 1 222 ? -26.059 26.320 92.455 1.00 78.92 ? 222 GLN A CB 1 ATOM 1773 C CG . GLN A 1 222 ? -24.843 27.100 92.933 1.00 80.18 ? 222 GLN A CG 1 ATOM 1774 C CD . GLN A 1 222 ? -24.512 26.837 94.395 1.00 81.49 ? 222 GLN A CD 1 ATOM 1775 O OE1 . GLN A 1 222 ? -25.402 26.742 95.240 1.00 80.41 ? 222 GLN A OE1 1 ATOM 1776 N NE2 . GLN A 1 222 ? -23.227 26.717 94.695 1.00 83.28 ? 222 GLN A NE2 1 ATOM 1777 N N . SER A 1 223 ? -27.974 23.853 93.557 1.00 82.16 ? 223 SER A N 1 ATOM 1778 C CA . SER A 1 223 ? -29.280 23.200 93.536 1.00 82.68 ? 223 SER A CA 1 ATOM 1779 C C . SER A 1 223 ? -30.422 24.205 93.690 1.00 82.38 ? 223 SER A C 1 ATOM 1780 O O . SER A 1 223 ? -31.562 23.918 93.316 1.00 82.14 ? 223 SER A O 1 ATOM 1781 C CB . SER A 1 223 ? -29.353 22.137 94.629 1.00 84.18 ? 223 SER A CB 1 ATOM 1782 O OG . SER A 1 223 ? -28.448 21.086 94.361 1.00 86.10 ? 223 SER A OG 1 ATOM 1783 N N . GLY A 1 224 ? -30.118 25.380 94.237 1.00 82.02 ? 224 GLY A N 1 ATOM 1784 C CA . GLY A 1 224 ? -31.079 26.476 94.281 1.00 80.76 ? 224 GLY A CA 1 ATOM 1785 C C . GLY A 1 224 ? -31.454 26.921 92.882 1.00 78.61 ? 224 GLY A C 1 ATOM 1786 O O . GLY A 1 224 ? -30.815 26.520 91.909 1.00 79.00 ? 224 GLY A O 1 ATOM 1787 N N . ARG A 1 225 ? -32.502 27.737 92.773 1.00 77.79 ? 225 ARG A N 1 ATOM 1788 C CA . ARG A 1 225 ? -32.958 28.244 91.474 1.00 76.95 ? 225 ARG A CA 1 ATOM 1789 C C . ARG A 1 225 ? -33.347 29.716 91.538 1.00 75.96 ? 225 ARG A C 1 ATOM 1790 O O . ARG A 1 225 ? -33.716 30.228 92.588 1.00 76.96 ? 225 ARG A O 1 ATOM 1791 C CB . ARG A 1 225 ? -34.155 27.436 90.965 1.00 76.33 ? 225 ARG A CB 1 ATOM 1792 C CG . ARG A 1 225 ? -33.868 25.970 90.672 1.00 76.66 ? 225 ARG A CG 1 ATOM 1793 C CD . ARG A 1 225 ? -33.149 25.774 89.350 1.00 75.49 ? 225 ARG A CD 1 ATOM 1794 N NE . ARG A 1 225 ? -32.873 24.357 89.099 1.00 75.76 ? 225 ARG A NE 1 ATOM 1795 C CZ . ARG A 1 225 ? -31.776 23.705 89.485 1.00 75.96 ? 225 ARG A CZ 1 ATOM 1796 N NH1 . ARG A 1 225 ? -30.808 24.324 90.159 1.00 76.55 ? 225 ARG A NH1 1 ATOM 1797 N NH2 . ARG A 1 225 ? -31.645 22.414 89.194 1.00 76.09 ? 225 ARG A NH2 1 ATOM 1798 N N . MET A 1 226 ? -33.258 30.389 90.399 1.00 75.62 ? 226 MET A N 1 ATOM 1799 C CA . MET A 1 226 ? -33.747 31.751 90.269 1.00 76.58 ? 226 MET A CA 1 ATOM 1800 C C . MET A 1 226 ? -34.800 31.764 89.178 1.00 75.58 ? 226 MET A C 1 ATOM 1801 O O . MET A 1 226 ? -34.665 31.067 88.175 1.00 77.87 ? 226 MET A O 1 ATOM 1802 C CB . MET A 1 226 ? -32.611 32.699 89.903 1.00 78.88 ? 226 MET A CB 1 ATOM 1803 C CG . MET A 1 226 ? -31.556 32.848 90.987 1.00 82.25 ? 226 MET A CG 1 ATOM 1804 S SD . MET A 1 226 ? -32.048 33.931 92.341 1.00 83.88 ? 226 MET A SD 1 ATOM 1805 C CE . MET A 1 226 ? -30.491 34.023 93.217 1.00 86.28 ? 226 MET A CE 1 ATOM 1806 N N . GLU A 1 227 ? -35.856 32.542 89.379 1.00 72.85 ? 227 GLU A N 1 ATOM 1807 C CA . GLU A 1 227 ? -36.916 32.650 88.394 1.00 70.66 ? 227 GLU A CA 1 ATOM 1808 C C . GLU A 1 227 ? -37.109 34.120 88.096 1.00 70.11 ? 227 GLU A C 1 ATOM 1809 O O . GLU A 1 227 ? -37.555 34.880 88.953 1.00 70.89 ? 227 GLU A O 1 ATOM 1810 C CB . GLU A 1 227 ? -38.202 32.016 88.915 1.00 70.97 ? 227 GLU A CB 1 ATOM 1811 C CG . GLU A 1 227 ? -39.248 31.766 87.839 1.00 70.79 ? 227 GLU A CG 1 ATOM 1812 C CD . GLU A 1 227 ? -40.412 30.934 88.343 1.00 71.90 ? 227 GLU A CD 1 ATOM 1813 O OE1 . GLU A 1 227 ? -40.583 30.820 89.578 1.00 71.62 ? 227 GLU A OE1 1 ATOM 1814 O OE2 . GLU A 1 227 ? -41.155 30.385 87.502 1.00 71.50 ? 227 GLU A OE2 1 ATOM 1815 N N . PHE A 1 228 ? -36.758 34.520 86.881 1.00 68.57 ? 228 PHE A N 1 ATOM 1816 C CA . PHE A 1 228 ? -36.751 35.927 86.529 1.00 68.75 ? 228 PHE A CA 1 ATOM 1817 C C . PHE A 1 228 ? -38.021 36.340 85.803 1.00 67.08 ? 228 PHE A C 1 ATOM 1818 O O . PHE A 1 228 ? -38.467 35.662 84.882 1.00 65.09 ? 228 PHE A O 1 ATOM 1819 C CB . PHE A 1 228 ? -35.507 36.246 85.706 1.00 70.28 ? 228 PHE A CB 1 ATOM 1820 C CG . PHE A 1 228 ? -34.233 36.098 86.489 1.00 71.02 ? 228 PHE A CG 1 ATOM 1821 C CD1 . PHE A 1 228 ? -33.758 37.146 87.266 1.00 70.96 ? 228 PHE A CD1 1 ATOM 1822 C CD2 . PHE A 1 228 ? -33.534 34.898 86.486 1.00 70.87 ? 228 PHE A CD2 1 ATOM 1823 C CE1 . PHE A 1 228 ? -32.598 37.007 88.005 1.00 71.17 ? 228 PHE A CE1 1 ATOM 1824 C CE2 . PHE A 1 228 ? -32.372 34.755 87.221 1.00 71.00 ? 228 PHE A CE2 1 ATOM 1825 C CZ . PHE A 1 228 ? -31.904 35.810 87.982 1.00 71.39 ? 228 PHE A CZ 1 ATOM 1826 N N . PHE A 1 229 ? -38.594 37.454 86.254 1.00 66.12 ? 229 PHE A N 1 ATOM 1827 C CA . PHE A 1 229 ? -39.812 38.013 85.686 1.00 65.18 ? 229 PHE A CA 1 ATOM 1828 C C . PHE A 1 229 ? -39.529 39.390 85.131 1.00 64.96 ? 229 PHE A C 1 ATOM 1829 O O . PHE A 1 229 ? -38.493 39.989 85.430 1.00 65.38 ? 229 PHE A O 1 ATOM 1830 C CB . PHE A 1 229 ? -40.898 38.095 86.750 1.00 64.91 ? 229 PHE A CB 1 ATOM 1831 C CG . PHE A 1 229 ? -41.352 36.754 87.230 1.00 66.07 ? 229 PHE A CG 1 ATOM 1832 C CD1 . PHE A 1 229 ? -40.600 36.049 88.153 1.00 67.16 ? 229 PHE A CD1 1 ATOM 1833 C CD2 . PHE A 1 229 ? -42.512 36.181 86.734 1.00 67.20 ? 229 PHE A CD2 1 ATOM 1834 C CE1 . PHE A 1 229 ? -41.006 34.800 88.591 1.00 68.56 ? 229 PHE A CE1 1 ATOM 1835 C CE2 . PHE A 1 229 ? -42.924 34.932 87.167 1.00 68.70 ? 229 PHE A CE2 1 ATOM 1836 C CZ . PHE A 1 229 ? -42.169 34.239 88.099 1.00 68.57 ? 229 PHE A CZ 1 ATOM 1837 N N . TRP A 1 230 ? -40.448 39.887 84.311 1.00 63.69 ? 230 TRP A N 1 ATOM 1838 C CA . TRP A 1 230 ? -40.272 41.188 83.692 1.00 62.92 ? 230 TRP A CA 1 ATOM 1839 C C . TRP A 1 230 ? -41.592 41.864 83.389 1.00 62.91 ? 230 TRP A C 1 ATOM 1840 O O . TRP A 1 230 ? -42.642 41.226 83.374 1.00 62.81 ? 230 TRP A O 1 ATOM 1841 C CB . TRP A 1 230 ? -39.470 41.046 82.404 1.00 63.19 ? 230 TRP A CB 1 ATOM 1842 C CG . TRP A 1 230 ? -40.122 40.178 81.358 1.00 62.43 ? 230 TRP A CG 1 ATOM 1843 C CD1 . TRP A 1 230 ? -39.942 38.836 81.181 1.00 61.96 ? 230 TRP A CD1 1 ATOM 1844 C CD2 . TRP A 1 230 ? -41.036 40.596 80.344 1.00 61.19 ? 230 TRP A CD2 1 ATOM 1845 N NE1 . TRP A 1 230 ? -40.689 38.392 80.124 1.00 61.78 ? 230 TRP A NE1 1 ATOM 1846 C CE2 . TRP A 1 230 ? -41.373 39.453 79.591 1.00 63.02 ? 230 TRP A CE2 1 ATOM 1847 C CE3 . TRP A 1 230 ? -41.608 41.824 79.999 1.00 61.09 ? 230 TRP A CE3 1 ATOM 1848 C CZ2 . TRP A 1 230 ? -42.260 39.503 78.508 1.00 63.75 ? 230 TRP A CZ2 1 ATOM 1849 C CZ3 . TRP A 1 230 ? -42.491 41.872 78.928 1.00 61.93 ? 230 TRP A CZ3 1 ATOM 1850 C CH2 . TRP A 1 230 ? -42.809 40.721 78.197 1.00 62.78 ? 230 TRP A CH2 1 ATOM 1851 N N . THR A 1 231 ? -41.520 43.166 83.146 1.00 62.74 ? 231 THR A N 1 ATOM 1852 C CA . THR A 1 231 ? -42.669 43.923 82.688 1.00 63.18 ? 231 THR A CA 1 ATOM 1853 C C . THR A 1 231 ? -42.203 45.109 81.852 1.00 64.66 ? 231 THR A C 1 ATOM 1854 O O . THR A 1 231 ? -41.019 45.445 81.843 1.00 65.03 ? 231 THR A O 1 ATOM 1855 C CB . THR A 1 231 ? -43.520 44.418 83.871 1.00 63.59 ? 231 THR A CB 1 ATOM 1856 O OG1 . THR A 1 231 ? -44.740 44.988 83.385 1.00 64.03 ? 231 THR A OG1 1 ATOM 1857 C CG2 . THR A 1 231 ? -42.771 45.463 84.688 1.00 64.21 ? 231 THR A CG2 1 ATOM 1858 N N . ILE A 1 232 ? -43.138 45.712 81.128 1.00 66.18 ? 232 ILE A N 1 ATOM 1859 C CA . ILE A 1 232 ? -42.901 46.975 80.454 1.00 68.50 ? 232 ILE A CA 1 ATOM 1860 C C . ILE A 1 232 ? -43.696 48.002 81.237 1.00 70.44 ? 232 ILE A C 1 ATOM 1861 O O . ILE A 1 232 ? -44.921 47.919 81.319 1.00 71.44 ? 232 ILE A O 1 ATOM 1862 C CB . ILE A 1 232 ? -43.326 46.943 78.967 1.00 68.89 ? 232 ILE A CB 1 ATOM 1863 C CG1 . ILE A 1 232 ? -42.153 46.523 78.083 1.00 68.93 ? 232 ILE A CG1 1 ATOM 1864 C CG2 . ILE A 1 232 ? -43.769 48.319 78.483 1.00 70.38 ? 232 ILE A CG2 1 ATOM 1865 C CD1 . ILE A 1 232 ? -41.492 45.237 78.508 1.00 69.14 ? 232 ILE A CD1 1 ATOM 1866 N N . LEU A 1 233 ? -42.984 48.959 81.820 1.00 71.82 ? 233 LEU A N 1 ATOM 1867 C CA . LEU A 1 233 ? -43.587 49.981 82.649 1.00 72.32 ? 233 LEU A CA 1 ATOM 1868 C C . LEU A 1 233 ? -43.836 51.198 81.778 1.00 75.50 ? 233 LEU A C 1 ATOM 1869 O O . LEU A 1 233 ? -42.890 51.836 81.313 1.00 76.53 ? 233 LEU A O 1 ATOM 1870 C CB . LEU A 1 233 ? -42.636 50.318 83.799 1.00 72.61 ? 233 LEU A CB 1 ATOM 1871 C CG . LEU A 1 233 ? -43.118 51.230 84.926 1.00 72.14 ? 233 LEU A CG 1 ATOM 1872 C CD1 . LEU A 1 233 ? -44.275 50.600 85.685 1.00 70.89 ? 233 LEU A CD1 1 ATOM 1873 C CD2 . LEU A 1 233 ? -41.952 51.526 85.853 1.00 71.89 ? 233 LEU A CD2 1 ATOM 1874 N N . LYS A 1 234 ? -45.108 51.511 81.549 1.00 79.24 ? 234 LYS A N 1 ATOM 1875 C CA . LYS A 1 234 ? -45.496 52.596 80.637 1.00 83.60 ? 234 LYS A CA 1 ATOM 1876 C C . LYS A 1 234 ? -45.066 53.969 81.169 1.00 86.65 ? 234 LYS A C 1 ATOM 1877 O O . LYS A 1 234 ? -44.661 54.084 82.331 1.00 86.71 ? 234 LYS A O 1 ATOM 1878 C CB . LYS A 1 234 ? -47.012 52.551 80.388 1.00 85.89 ? 234 LYS A CB 1 ATOM 1879 C CG . LYS A 1 234 ? -47.435 51.495 79.374 1.00 86.28 ? 234 LYS A CG 1 ATOM 1880 C CD . LYS A 1 234 ? -48.951 51.379 79.284 1.00 89.08 ? 234 LYS A CD 1 ATOM 1881 C CE . LYS A 1 234 ? -49.391 50.033 78.718 1.00 89.41 ? 234 LYS A CE 1 ATOM 1882 N NZ . LYS A 1 234 ? -48.995 49.844 77.296 1.00 90.08 ? 234 LYS A NZ 1 ATOM 1883 N N . PRO A 1 235 ? -45.129 55.016 80.318 1.00 89.67 ? 235 PRO A N 1 ATOM 1884 C CA . PRO A 1 235 ? -44.725 56.338 80.819 1.00 90.60 ? 235 PRO A CA 1 ATOM 1885 C C . PRO A 1 235 ? -45.641 56.833 81.924 1.00 91.72 ? 235 PRO A C 1 ATOM 1886 O O . PRO A 1 235 ? -46.850 56.602 81.871 1.00 90.66 ? 235 PRO A O 1 ATOM 1887 C CB . PRO A 1 235 ? -44.836 57.252 79.590 1.00 92.78 ? 235 PRO A CB 1 ATOM 1888 C CG . PRO A 1 235 ? -45.661 56.508 78.594 1.00 91.95 ? 235 PRO A CG 1 ATOM 1889 C CD . PRO A 1 235 ? -45.523 55.048 78.895 1.00 89.09 ? 235 PRO A CD 1 ATOM 1890 N N . ASN A 1 236 ? -45.059 57.488 82.926 1.00 93.96 ? 236 ASN A N 1 ATOM 1891 C CA . ASN A 1 236 ? -45.827 58.137 83.980 1.00 94.69 ? 236 ASN A CA 1 ATOM 1892 C C . ASN A 1 236 ? -46.533 57.123 84.890 1.00 91.99 ? 236 ASN A C 1 ATOM 1893 O O . ASN A 1 236 ? -47.496 57.460 85.579 1.00 92.71 ? 236 ASN A O 1 ATOM 1894 C CB . ASN A 1 236 ? -46.843 59.105 83.349 1.00 98.04 ? 236 ASN A CB 1 ATOM 1895 C CG . ASN A 1 236 ? -47.148 60.302 84.225 1.00 102.20 ? 236 ASN A CG 1 ATOM 1896 O OD1 . ASN A 1 236 ? -46.474 60.557 85.220 1.00 103.22 ? 236 ASN A OD1 1 ATOM 1897 N ND2 . ASN A 1 236 ? -48.170 61.055 83.846 1.00 106.45 ? 236 ASN A ND2 1 ATOM 1898 N N . ASP A 1 237 ? -46.040 55.887 84.893 1.00 88.55 ? 237 ASP A N 1 ATOM 1899 C CA . ASP A 1 237 ? -46.606 54.814 85.704 1.00 85.85 ? 237 ASP A CA 1 ATOM 1900 C C . ASP A 1 237 ? -45.545 54.331 86.680 1.00 83.82 ? 237 ASP A C 1 ATOM 1901 O O . ASP A 1 237 ? -44.347 54.411 86.398 1.00 82.41 ? 237 ASP A O 1 ATOM 1902 C CB . ASP A 1 237 ? -47.065 53.659 84.808 1.00 85.43 ? 237 ASP A CB 1 ATOM 1903 C CG . ASP A 1 237 ? -47.709 52.512 85.587 1.00 84.70 ? 237 ASP A CG 1 ATOM 1904 O OD1 . ASP A 1 237 ? -48.298 52.759 86.663 1.00 84.80 ? 237 ASP A OD1 1 ATOM 1905 O OD2 . ASP A 1 237 ? -47.644 51.357 85.107 1.00 83.16 ? 237 ASP A OD2 1 ATOM 1906 N N . ALA A 1 238 ? -45.994 53.826 87.825 1.00 82.99 ? 238 ALA A N 1 ATOM 1907 C CA . ALA A 1 238 ? -45.096 53.388 88.883 1.00 81.40 ? 238 ALA A CA 1 ATOM 1908 C C . ALA A 1 238 ? -45.200 51.887 89.100 1.00 79.52 ? 238 ALA A C 1 ATOM 1909 O O . ALA A 1 238 ? -46.273 51.303 88.936 1.00 78.90 ? 238 ALA A O 1 ATOM 1910 C CB . ALA A 1 238 ? -45.414 54.130 90.173 1.00 81.94 ? 238 ALA A CB 1 ATOM 1911 N N . ILE A 1 239 ? -44.075 51.273 89.463 1.00 79.02 ? 239 ILE A N 1 ATOM 1912 C CA . ILE A 1 239 ? -44.041 49.866 89.876 1.00 77.96 ? 239 ILE A CA 1 ATOM 1913 C C . ILE A 1 239 ? -43.750 49.774 91.379 1.00 79.82 ? 239 ILE A C 1 ATOM 1914 O O . ILE A 1 239 ? -42.861 50.462 91.879 1.00 79.81 ? 239 ILE A O 1 ATOM 1915 C CB . ILE A 1 239 ? -43.008 49.047 89.066 1.00 75.53 ? 239 ILE A CB 1 ATOM 1916 C CG1 . ILE A 1 239 ? -43.175 47.550 89.353 1.00 74.42 ? 239 ILE A CG1 1 ATOM 1917 C CG2 . ILE A 1 239 ? -41.578 49.490 89.363 1.00 75.53 ? 239 ILE A CG2 1 ATOM 1918 C CD1 . ILE A 1 239 ? -42.410 46.656 88.404 1.00 72.73 ? 239 ILE A CD1 1 ATOM 1919 N N . ASN A 1 240 ? -44.502 48.928 92.084 1.00 80.85 ? 240 ASN A N 1 ATOM 1920 C CA . ASN A 1 240 ? -44.442 48.842 93.547 1.00 83.14 ? 240 ASN A CA 1 ATOM 1921 C C . ASN A 1 240 ? -44.037 47.460 94.034 1.00 82.65 ? 240 ASN A C 1 ATOM 1922 O O . ASN A 1 240 ? -44.778 46.497 93.846 1.00 83.04 ? 240 ASN A O 1 ATOM 1923 C CB . ASN A 1 240 ? -45.808 49.157 94.146 1.00 85.40 ? 240 ASN A CB 1 ATOM 1924 C CG . ASN A 1 240 ? -46.321 50.523 93.753 1.00 88.98 ? 240 ASN A CG 1 ATOM 1925 O OD1 . ASN A 1 240 ? -45.635 51.526 93.936 1.00 90.61 ? 240 ASN A OD1 1 ATOM 1926 N ND2 . ASN A 1 240 ? -47.542 50.572 93.219 1.00 90.73 ? 240 ASN A ND2 1 ATOM 1927 N N . PHE A 1 241 ? -42.878 47.367 94.679 1.00 82.40 ? 241 PHE A N 1 ATOM 1928 C CA . PHE A 1 241 ? -42.412 46.105 95.240 1.00 82.64 ? 241 PHE A CA 1 ATOM 1929 C C . PHE A 1 241 ? -42.705 46.014 96.734 1.00 85.54 ? 241 PHE A C 1 ATOM 1930 O O . PHE A 1 241 ? -42.810 47.030 97.420 1.00 87.84 ? 241 PHE A O 1 ATOM 1931 C CB . PHE A 1 241 ? -40.915 45.937 94.994 1.00 82.29 ? 241 PHE A CB 1 ATOM 1932 C CG . PHE A 1 241 ? -40.564 45.732 93.550 1.00 81.83 ? 241 PHE A CG 1 ATOM 1933 C CD1 . PHE A 1 241 ? -40.713 44.485 92.958 1.00 80.57 ? 241 PHE A CD1 1 ATOM 1934 C CD2 . PHE A 1 241 ? -40.092 46.782 92.779 1.00 82.35 ? 241 PHE A CD2 1 ATOM 1935 C CE1 . PHE A 1 241 ? -40.392 44.288 91.628 1.00 80.26 ? 241 PHE A CE1 1 ATOM 1936 C CE2 . PHE A 1 241 ? -39.768 46.592 91.447 1.00 80.86 ? 241 PHE A CE2 1 ATOM 1937 C CZ . PHE A 1 241 ? -39.918 45.343 90.871 1.00 80.06 ? 241 PHE A CZ 1 ATOM 1938 N N . GLU A 1 242 ? -42.850 44.787 97.223 1.00 87.09 ? 242 GLU A N 1 ATOM 1939 C CA . GLU A 1 242 ? -42.955 44.521 98.657 1.00 89.58 ? 242 GLU A CA 1 ATOM 1940 C C . GLU A 1 242 ? -42.607 43.052 98.903 1.00 88.44 ? 242 GLU A C 1 ATOM 1941 O O . GLU A 1 242 ? -43.132 42.176 98.212 1.00 88.83 ? 242 GLU A O 1 ATOM 1942 C CB . GLU A 1 242 ? -44.364 44.856 99.175 1.00 91.63 ? 242 GLU A CB 1 ATOM 1943 C CG . GLU A 1 242 ? -44.599 44.551 100.655 1.00 93.99 ? 242 GLU A CG 1 ATOM 1944 C CD . GLU A 1 242 ? -46.034 44.805 101.101 1.00 95.02 ? 242 GLU A CD 1 ATOM 1945 O OE1 . GLU A 1 242 ? -46.613 45.847 100.720 1.00 95.54 ? 242 GLU A OE1 1 ATOM 1946 O OE2 . GLU A 1 242 ? -46.584 43.960 101.838 1.00 93.75 ? 242 GLU A OE2 1 ATOM 1947 N N . SER A 1 243 ? -41.722 42.783 99.866 1.00 87.51 ? 243 SER A N 1 ATOM 1948 C CA . SER A 1 243 ? -41.247 41.414 100.092 1.00 88.15 ? 243 SER A CA 1 ATOM 1949 C C . SER A 1 243 ? -40.627 41.139 101.476 1.00 91.87 ? 243 SER A C 1 ATOM 1950 O O . SER A 1 243 ? -39.982 42.012 102.060 1.00 93.87 ? 243 SER A O 1 ATOM 1951 C CB . SER A 1 243 ? -40.229 41.051 99.009 1.00 85.59 ? 243 SER A CB 1 ATOM 1952 O OG . SER A 1 243 ? -39.872 39.684 99.087 1.00 85.16 ? 243 SER A OG 1 ATOM 1953 N N . ASN A 1 244 ? -40.821 39.909 101.967 1.00 94.10 ? 244 ASN A N 1 ATOM 1954 C CA . ASN A 1 244 ? -40.188 39.410 103.205 1.00 96.86 ? 244 ASN A CA 1 ATOM 1955 C C . ASN A 1 244 ? -38.837 38.744 102.994 1.00 96.20 ? 244 ASN A C 1 ATOM 1956 O O . ASN A 1 244 ? -38.131 38.462 103.958 1.00 95.40 ? 244 ASN A O 1 ATOM 1957 C CB . ASN A 1 244 ? -41.066 38.353 103.864 1.00 100.09 ? 244 ASN A CB 1 ATOM 1958 C CG . ASN A 1 244 ? -42.419 38.877 104.250 1.00 105.02 ? 244 ASN A CG 1 ATOM 1959 O OD1 . ASN A 1 244 ? -42.681 40.077 104.174 1.00 113.15 ? 244 ASN A OD1 1 ATOM 1960 N ND2 . ASN A 1 244 ? -43.297 37.975 104.674 1.00 107.08 ? 244 ASN A ND2 1 ATOM 1961 N N . GLY A 1 245 ? -38.503 38.445 101.743 1.00 95.20 ? 245 GLY A N 1 ATOM 1962 C CA . GLY A 1 245 ? -37.289 37.705 101.434 1.00 93.86 ? 245 GLY A CA 1 ATOM 1963 C C . GLY A 1 245 ? -37.363 36.982 100.107 1.00 90.88 ? 245 GLY A C 1 ATOM 1964 O O . GLY A 1 245 ? -38.424 36.906 99.479 1.00 89.27 ? 245 GLY A O 1 ATOM 1965 N N . ASN A 1 246 ? -36.217 36.441 99.700 1.00 89.53 ? 246 ASN A N 1 ATOM 1966 C CA . ASN A 1 246 ? -36.050 35.756 98.418 1.00 87.62 ? 246 ASN A CA 1 ATOM 1967 C C . ASN A 1 246 ? -36.142 36.711 97.228 1.00 85.40 ? 246 ASN A C 1 ATOM 1968 O O . ASN A 1 246 ? -36.211 36.270 96.083 1.00 85.15 ? 246 ASN A O 1 ATOM 1969 C CB . ASN A 1 246 ? -37.057 34.606 98.256 1.00 87.16 ? 246 ASN A CB 1 ATOM 1970 C CG . ASN A 1 246 ? -37.074 33.664 99.452 1.00 87.43 ? 246 ASN A CG 1 ATOM 1971 O OD1 . ASN A 1 246 ? -37.470 34.048 100.552 1.00 85.31 ? 246 ASN A OD1 1 ATOM 1972 N ND2 . ASN A 1 246 ? -36.665 32.420 99.235 1.00 87.90 ? 246 ASN A ND2 1 ATOM 1973 N N . PHE A 1 247 ? -36.099 38.013 97.503 1.00 84.68 ? 247 PHE A N 1 ATOM 1974 C CA . PHE A 1 247 ? -36.318 39.030 96.481 1.00 82.48 ? 247 PHE A CA 1 ATOM 1975 C C . PHE A 1 247 ? -35.014 39.384 95.774 1.00 81.77 ? 247 PHE A C 1 ATOM 1976 O O . PHE A 1 247 ? -34.038 39.788 96.412 1.00 83.32 ? 247 PHE A O 1 ATOM 1977 C CB . PHE A 1 247 ? -36.947 40.280 97.113 1.00 83.30 ? 247 PHE A CB 1 ATOM 1978 C CG . PHE A 1 247 ? -37.212 41.405 96.140 1.00 82.36 ? 247 PHE A CG 1 ATOM 1979 C CD1 . PHE A 1 247 ? -37.796 41.161 94.903 1.00 79.42 ? 247 PHE A CD1 1 ATOM 1980 C CD2 . PHE A 1 247 ? -36.903 42.716 96.481 1.00 82.78 ? 247 PHE A CD2 1 ATOM 1981 C CE1 . PHE A 1 247 ? -38.045 42.196 94.023 1.00 79.34 ? 247 PHE A CE1 1 ATOM 1982 C CE2 . PHE A 1 247 ? -37.159 43.756 95.605 1.00 81.68 ? 247 PHE A CE2 1 ATOM 1983 C CZ . PHE A 1 247 ? -37.727 43.495 94.373 1.00 80.87 ? 247 PHE A CZ 1 ATOM 1984 N N . ILE A 1 248 ? -35.009 39.216 94.454 1.00 79.51 ? 248 ILE A N 1 ATOM 1985 C CA . ILE A 1 248 ? -33.904 39.656 93.617 1.00 78.11 ? 248 ILE A CA 1 ATOM 1986 C C . ILE A 1 248 ? -34.356 40.973 93.005 1.00 77.36 ? 248 ILE A C 1 ATOM 1987 O O . ILE A 1 248 ? -35.100 40.992 92.023 1.00 77.54 ? 248 ILE A O 1 ATOM 1988 C CB . ILE A 1 248 ? -33.558 38.628 92.518 1.00 76.52 ? 248 ILE A CB 1 ATOM 1989 C CG1 . ILE A 1 248 ? -33.564 37.198 93.071 1.00 77.49 ? 248 ILE A CG1 1 ATOM 1990 C CG2 . ILE A 1 248 ? -32.203 38.945 91.911 1.00 76.79 ? 248 ILE A CG2 1 ATOM 1991 C CD1 . ILE A 1 248 ? -32.660 36.977 94.267 1.00 79.86 ? 248 ILE A CD1 1 ATOM 1992 N N . ALA A 1 249 ? -33.926 42.074 93.610 1.00 77.11 ? 249 ALA A N 1 ATOM 1993 C CA . ALA A 1 249 ? -34.434 43.397 93.259 1.00 76.54 ? 249 ALA A CA 1 ATOM 1994 C C . ALA A 1 249 ? -33.723 43.979 92.043 1.00 75.80 ? 249 ALA A C 1 ATOM 1995 O O . ALA A 1 249 ? -32.549 43.688 91.813 1.00 74.41 ? 249 ALA A O 1 ATOM 1996 C CB . ALA A 1 249 ? -34.292 44.343 94.439 1.00 78.44 ? 249 ALA A CB 1 ATOM 1997 N N . PRO A 1 250 ? -34.432 44.814 91.264 1.00 74.95 ? 250 PRO A N 1 ATOM 1998 C CA . PRO A 1 250 ? -33.769 45.521 90.179 1.00 75.38 ? 250 PRO A CA 1 ATOM 1999 C C . PRO A 1 250 ? -32.770 46.543 90.691 1.00 78.96 ? 250 PRO A C 1 ATOM 2000 O O . PRO A 1 250 ? -33.000 47.162 91.729 1.00 82.52 ? 250 PRO A O 1 ATOM 2001 C CB . PRO A 1 250 ? -34.918 46.243 89.463 1.00 74.10 ? 250 PRO A CB 1 ATOM 2002 C CG . PRO A 1 250 ? -36.030 46.301 90.438 1.00 73.69 ? 250 PRO A CG 1 ATOM 2003 C CD . PRO A 1 250 ? -35.878 45.095 91.309 1.00 74.44 ? 250 PRO A CD 1 ATOM 2004 N N . GLU A 1 251 ? -31.660 46.696 89.978 1.00 80.32 ? 251 GLU A N 1 ATOM 2005 C CA . GLU A 1 251 ? -30.818 47.872 90.128 1.00 84.04 ? 251 GLU A CA 1 ATOM 2006 C C . GLU A 1 251 ? -30.946 48.699 88.854 1.00 84.91 ? 251 GLU A C 1 ATOM 2007 O O . GLU A 1 251 ? -31.359 49.863 88.893 1.00 86.05 ? 251 GLU A O 1 ATOM 2008 C CB . GLU A 1 251 ? -29.361 47.485 90.382 1.00 86.53 ? 251 GLU A CB 1 ATOM 2009 C CG . GLU A 1 251 ? -28.483 48.662 90.789 1.00 89.85 ? 251 GLU A CG 1 ATOM 2010 C CD . GLU A 1 251 ? -27.036 48.277 91.033 1.00 92.01 ? 251 GLU A CD 1 ATOM 2011 O OE1 . GLU A 1 251 ? -26.705 47.071 90.938 1.00 92.05 ? 251 GLU A OE1 1 ATOM 2012 O OE2 . GLU A 1 251 ? -26.232 49.192 91.319 1.00 92.04 ? 251 GLU A OE2 1 ATOM 2013 N N . TYR A 1 252 ? -30.605 48.078 87.726 1.00 83.42 ? 252 TYR A N 1 ATOM 2014 C CA . TYR A 1 252 ? -30.696 48.723 86.424 1.00 83.06 ? 252 TYR A CA 1 ATOM 2015 C C . TYR A 1 252 ? -31.873 48.164 85.627 1.00 80.89 ? 252 TYR A C 1 ATOM 2016 O O . TYR A 1 252 ? -32.209 46.981 85.727 1.00 76.98 ? 252 TYR A O 1 ATOM 2017 C CB . TYR A 1 252 ? -29.398 48.533 85.634 1.00 84.33 ? 252 TYR A CB 1 ATOM 2018 C CG . TYR A 1 252 ? -28.172 49.075 86.331 1.00 87.62 ? 252 TYR A CG 1 ATOM 2019 C CD1 . TYR A 1 252 ? -27.905 50.443 86.351 1.00 90.13 ? 252 TYR A CD1 1 ATOM 2020 C CD2 . TYR A 1 252 ? -27.282 48.222 86.981 1.00 88.08 ? 252 TYR A CD2 1 ATOM 2021 C CE1 . TYR A 1 252 ? -26.783 50.944 86.995 1.00 91.34 ? 252 TYR A CE1 1 ATOM 2022 C CE2 . TYR A 1 252 ? -26.159 48.713 87.626 1.00 90.17 ? 252 TYR A CE2 1 ATOM 2023 C CZ . TYR A 1 252 ? -25.913 50.076 87.631 1.00 91.57 ? 252 TYR A CZ 1 ATOM 2024 O OH . TYR A 1 252 ? -24.796 50.565 88.270 1.00 91.38 ? 252 TYR A OH 1 ATOM 2025 N N . ALA A 1 253 ? -32.494 49.041 84.846 1.00 80.44 ? 253 ALA A N 1 ATOM 2026 C CA . ALA A 1 253 ? -33.573 48.679 83.940 1.00 78.44 ? 253 ALA A CA 1 ATOM 2027 C C . ALA A 1 253 ? -33.295 49.346 82.593 1.00 79.00 ? 253 ALA A C 1 ATOM 2028 O O . ALA A 1 253 ? -32.728 50.445 82.543 1.00 80.33 ? 253 ALA A O 1 ATOM 2029 C CB . ALA A 1 253 ? -34.908 49.135 84.509 1.00 77.84 ? 253 ALA A CB 1 ATOM 2030 N N . TYR A 1 254 ? -33.685 48.673 81.512 1.00 76.90 ? 254 TYR A N 1 ATOM 2031 C CA . TYR A 1 254 ? -33.399 49.143 80.159 1.00 76.48 ? 254 TYR A CA 1 ATOM 2032 C C . TYR A 1 254 ? -34.501 50.045 79.624 1.00 76.69 ? 254 TYR A C 1 ATOM 2033 O O . TYR A 1 254 ? -35.680 49.727 79.709 1.00 77.05 ? 254 TYR A O 1 ATOM 2034 C CB . TYR A 1 254 ? -33.214 47.966 79.211 1.00 75.06 ? 254 TYR A CB 1 ATOM 2035 C CG . TYR A 1 254 ? -31.987 47.138 79.495 1.00 74.24 ? 254 TYR A CG 1 ATOM 2036 C CD1 . TYR A 1 254 ? -30.767 47.442 78.901 1.00 74.90 ? 254 TYR A CD1 1 ATOM 2037 C CD2 . TYR A 1 254 ? -32.048 46.044 80.345 1.00 73.21 ? 254 TYR A CD2 1 ATOM 2038 C CE1 . TYR A 1 254 ? -29.637 46.680 79.146 1.00 75.10 ? 254 TYR A CE1 1 ATOM 2039 C CE2 . TYR A 1 254 ? -30.928 45.273 80.598 1.00 73.97 ? 254 TYR A CE2 1 ATOM 2040 C CZ . TYR A 1 254 ? -29.720 45.594 79.995 1.00 75.43 ? 254 TYR A CZ 1 ATOM 2041 O OH . TYR A 1 254 ? -28.593 44.834 80.246 1.00 76.46 ? 254 TYR A OH 1 ATOM 2042 N N . LYS A 1 255 ? -34.093 51.168 79.053 1.00 79.17 ? 255 LYS A N 1 ATOM 2043 C CA . LYS A 1 255 ? -35.012 52.140 78.484 1.00 81.56 ? 255 LYS A CA 1 ATOM 2044 C C . LYS A 1 255 ? -35.120 51.892 76.973 1.00 79.34 ? 255 LYS A C 1 ATOM 2045 O O . LYS A 1 255 ? -34.114 51.652 76.307 1.00 76.56 ? 255 LYS A O 1 ATOM 2046 C CB . LYS A 1 255 ? -34.489 53.551 78.786 1.00 85.54 ? 255 LYS A CB 1 ATOM 2047 C CG . LYS A 1 255 ? -35.543 54.641 78.838 1.00 87.99 ? 255 LYS A CG 1 ATOM 2048 C CD . LYS A 1 255 ? -35.095 55.823 79.694 1.00 89.77 ? 255 LYS A CD 1 ATOM 2049 C CE . LYS A 1 255 ? -33.888 56.539 79.106 1.00 91.50 ? 255 LYS A CE 1 ATOM 2050 N NZ . LYS A 1 255 ? -33.626 57.833 79.797 1.00 94.00 ? 255 LYS A NZ 1 ATOM 2051 N N . ILE A 1 256 ? -36.341 51.936 76.447 1.00 78.34 ? 256 ILE A N 1 ATOM 2052 C CA . ILE A 1 256 ? -36.595 51.636 75.039 1.00 78.64 ? 256 ILE A CA 1 ATOM 2053 C C . ILE A 1 256 ? -36.637 52.933 74.230 1.00 81.80 ? 256 ILE A C 1 ATOM 2054 O O . ILE A 1 256 ? -37.698 53.537 74.036 1.00 80.23 ? 256 ILE A O 1 ATOM 2055 C CB . ILE A 1 256 ? -37.904 50.838 74.873 1.00 77.27 ? 256 ILE A CB 1 ATOM 2056 C CG1 . ILE A 1 256 ? -37.790 49.493 75.597 1.00 75.75 ? 256 ILE A CG1 1 ATOM 2057 C CG2 . ILE A 1 256 ? -38.211 50.598 73.398 1.00 78.12 ? 256 ILE A CG2 1 ATOM 2058 C CD1 . ILE A 1 256 ? -39.118 48.881 75.986 1.00 74.87 ? 256 ILE A CD1 1 ATOM 2059 N N . VAL A 1 257 ? -35.467 53.359 73.762 1.00 85.57 ? 257 VAL A N 1 ATOM 2060 C CA . VAL A 1 257 ? -35.345 54.640 73.063 1.00 91.02 ? 257 VAL A CA 1 ATOM 2061 C C . VAL A 1 257 ? -35.778 54.544 71.600 1.00 93.00 ? 257 VAL A C 1 ATOM 2062 O O . VAL A 1 257 ? -36.457 55.447 71.094 1.00 94.32 ? 257 VAL A O 1 ATOM 2063 C CB . VAL A 1 257 ? -33.918 55.244 73.167 1.00 92.87 ? 257 VAL A CB 1 ATOM 2064 C CG1 . VAL A 1 257 ? -33.538 55.456 74.624 1.00 93.21 ? 257 VAL A CG1 1 ATOM 2065 C CG2 . VAL A 1 257 ? -32.875 54.383 72.463 1.00 93.24 ? 257 VAL A CG2 1 ATOM 2066 N N . LYS A 1 258 ? -35.401 53.454 70.931 1.00 92.44 ? 258 LYS A N 1 ATOM 2067 C CA . LYS A 1 258 ? -35.707 53.293 69.510 1.00 94.70 ? 258 LYS A CA 1 ATOM 2068 C C . LYS A 1 258 ? -36.361 51.956 69.184 1.00 91.45 ? 258 LYS A C 1 ATOM 2069 O O . LYS A 1 258 ? -35.829 50.895 69.516 1.00 89.38 ? 258 LYS A O 1 ATOM 2070 C CB . LYS A 1 258 ? -34.443 53.466 68.671 1.00 96.39 ? 258 LYS A CB 1 ATOM 2071 C CG . LYS A 1 258 ? -34.723 53.572 67.185 1.00 98.31 ? 258 LYS A CG 1 ATOM 2072 C CD . LYS A 1 258 ? -33.519 54.105 66.435 1.00 102.15 ? 258 LYS A CD 1 ATOM 2073 C CE . LYS A 1 258 ? -33.784 54.153 64.939 1.00 103.51 ? 258 LYS A CE 1 ATOM 2074 N NZ . LYS A 1 258 ? -32.701 54.872 64.215 1.00 106.37 ? 258 LYS A NZ 1 ATOM 2075 N N . LYS A 1 259 ? -37.517 52.031 68.526 1.00 90.99 ? 259 LYS A N 1 ATOM 2076 C CA . LYS A 1 259 ? -38.216 50.865 68.005 1.00 90.83 ? 259 LYS A CA 1 ATOM 2077 C C . LYS A 1 259 ? -38.144 50.884 66.486 1.00 90.93 ? 259 LYS A C 1 ATOM 2078 O O . LYS A 1 259 ? -38.326 51.930 65.869 1.00 92.73 ? 259 LYS A O 1 ATOM 2079 C CB . LYS A 1 259 ? -39.680 50.890 68.431 1.00 92.12 ? 259 LYS A CB 1 ATOM 2080 C CG . LYS A 1 259 ? -39.899 50.840 69.931 1.00 94.14 ? 259 LYS A CG 1 ATOM 2081 C CD . LYS A 1 259 ? -41.378 50.922 70.271 1.00 95.54 ? 259 LYS A CD 1 ATOM 2082 C CE . LYS A 1 259 ? -41.592 50.979 71.771 1.00 96.65 ? 259 LYS A CE 1 ATOM 2083 N NZ . LYS A 1 259 ? -42.998 51.320 72.117 1.00 98.14 ? 259 LYS A NZ 1 ATOM 2084 N N . GLY A 1 260 ? -37.889 49.730 65.882 1.00 90.57 ? 260 GLY A N 1 ATOM 2085 C CA . GLY A 1 260 ? -37.851 49.634 64.425 1.00 91.57 ? 260 GLY A CA 1 ATOM 2086 C C . GLY A 1 260 ? -37.766 48.210 63.922 1.00 90.28 ? 260 GLY A C 1 ATOM 2087 O O . GLY A 1 260 ? -38.066 47.263 64.652 1.00 91.66 ? 260 GLY A O 1 ATOM 2088 N N . ASP A 1 261 ? -37.366 48.061 62.664 1.00 89.99 ? 261 ASP A N 1 ATOM 2089 C CA . ASP A 1 261 ? -37.187 46.742 62.071 1.00 89.35 ? 261 ASP A CA 1 ATOM 2090 C C . ASP A 1 261 ? -35.918 46.104 62.600 1.00 85.17 ? 261 ASP A C 1 ATOM 2091 O O . ASP A 1 261 ? -34.840 46.691 62.533 1.00 85.88 ? 261 ASP A O 1 ATOM 2092 C CB . ASP A 1 261 ? -37.128 46.812 60.536 1.00 94.29 ? 261 ASP A CB 1 ATOM 2093 C CG . ASP A 1 261 ? -38.446 46.435 59.878 1.00 97.97 ? 261 ASP A CG 1 ATOM 2094 O OD1 . ASP A 1 261 ? -39.404 46.091 60.607 1.00 100.29 ? 261 ASP A OD1 1 ATOM 2095 O OD2 . ASP A 1 261 ? -38.519 46.476 58.627 1.00 101.53 ? 261 ASP A OD2 1 ATOM 2096 N N . SER A 1 262 ? -36.059 44.894 63.122 1.00 80.46 ? 262 SER A N 1 ATOM 2097 C CA . SER A 1 262 ? -34.927 44.140 63.630 1.00 79.61 ? 262 SER A CA 1 ATOM 2098 C C . SER A 1 262 ? -35.296 42.662 63.661 1.00 77.39 ? 262 SER A C 1 ATOM 2099 O O . SER A 1 262 ? -36.409 42.289 63.288 1.00 79.03 ? 262 SER A O 1 ATOM 2100 C CB . SER A 1 262 ? -34.544 44.634 65.028 1.00 79.44 ? 262 SER A CB 1 ATOM 2101 O OG . SER A 1 262 ? -33.434 43.917 65.540 1.00 80.33 ? 262 SER A OG 1 ATOM 2102 N N . THR A 1 263 ? -34.361 41.825 64.095 1.00 71.40 ? 263 THR A N 1 ATOM 2103 C CA . THR A 1 263 ? -34.596 40.391 64.174 1.00 67.63 ? 263 THR A CA 1 ATOM 2104 C C . THR A 1 263 ? -33.501 39.731 64.997 1.00 67.02 ? 263 THR A C 1 ATOM 2105 O O . THR A 1 263 ? -32.395 40.272 65.123 1.00 65.96 ? 263 THR A O 1 ATOM 2106 C CB . THR A 1 263 ? -34.642 39.743 62.773 1.00 66.26 ? 263 THR A CB 1 ATOM 2107 O OG1 . THR A 1 263 ? -35.160 38.417 62.875 1.00 65.17 ? 263 THR A OG1 1 ATOM 2108 C CG2 . THR A 1 263 ? -33.256 39.687 62.128 1.00 65.48 ? 263 THR A CG2 1 ATOM 2109 N N . ILE A 1 264 ? -33.820 38.568 65.561 1.00 66.62 ? 264 ILE A N 1 ATOM 2110 C CA . ILE A 1 264 ? -32.840 37.762 66.280 1.00 65.33 ? 264 ILE A CA 1 ATOM 2111 C C . ILE A 1 264 ? -32.457 36.597 65.374 1.00 65.10 ? 264 ILE A C 1 ATOM 2112 O O . ILE A 1 264 ? -33.214 35.645 65.191 1.00 64.06 ? 264 ILE A O 1 ATOM 2113 C CB . ILE A 1 264 ? -33.369 37.274 67.645 1.00 64.45 ? 264 ILE A CB 1 ATOM 2114 C CG1 . ILE A 1 264 ? -33.760 38.477 68.506 1.00 65.33 ? 264 ILE A CG1 1 ATOM 2115 C CG2 . ILE A 1 264 ? -32.312 36.451 68.367 1.00 62.77 ? 264 ILE A CG2 1 ATOM 2116 C CD1 . ILE A 1 264 ? -34.487 38.119 69.782 1.00 66.28 ? 264 ILE A CD1 1 ATOM 2117 N N . MET A 1 265 ? -31.268 36.710 64.800 1.00 66.14 ? 265 MET A N 1 ATOM 2118 C CA . MET A 1 265 ? -30.740 35.743 63.860 1.00 65.69 ? 265 MET A CA 1 ATOM 2119 C C . MET A 1 265 ? -30.019 34.652 64.642 1.00 66.60 ? 265 MET A C 1 ATOM 2120 O O . MET A 1 265 ? -29.270 34.946 65.573 1.00 66.56 ? 265 MET A O 1 ATOM 2121 C CB . MET A 1 265 ? -29.762 36.462 62.935 1.00 66.31 ? 265 MET A CB 1 ATOM 2122 C CG . MET A 1 265 ? -29.551 35.822 61.584 1.00 67.51 ? 265 MET A CG 1 ATOM 2123 S SD . MET A 1 265 ? -28.674 36.958 60.492 1.00 69.50 ? 265 MET A SD 1 ATOM 2124 C CE . MET A 1 265 ? -30.001 38.069 60.025 1.00 69.43 ? 265 MET A CE 1 ATOM 2125 N N . LYS A 1 266 ? -30.262 33.397 64.280 1.00 68.31 ? 266 LYS A N 1 ATOM 2126 C CA . LYS A 1 266 ? -29.552 32.276 64.880 1.00 69.87 ? 266 LYS A CA 1 ATOM 2127 C C . LYS A 1 266 ? -28.432 31.876 63.938 1.00 70.57 ? 266 LYS A C 1 ATOM 2128 O O . LYS A 1 266 ? -28.682 31.487 62.800 1.00 72.12 ? 266 LYS A O 1 ATOM 2129 C CB . LYS A 1 266 ? -30.494 31.101 65.143 1.00 72.32 ? 266 LYS A CB 1 ATOM 2130 C CG . LYS A 1 266 ? -31.723 31.456 65.984 1.00 76.73 ? 266 LYS A CG 1 ATOM 2131 C CD . LYS A 1 266 ? -31.394 31.849 67.425 1.00 77.75 ? 266 LYS A CD 1 ATOM 2132 C CE . LYS A 1 266 ? -31.165 30.629 68.305 1.00 81.91 ? 266 LYS A CE 1 ATOM 2133 N NZ . LYS A 1 266 ? -30.529 30.959 69.619 1.00 85.22 ? 266 LYS A NZ 1 ATOM 2134 N N . SER A 1 267 ? -27.196 31.996 64.414 1.00 73.06 ? 267 SER A N 1 ATOM 2135 C CA . SER A 1 267 ? -26.010 31.755 63.594 1.00 73.58 ? 267 SER A CA 1 ATOM 2136 C C . SER A 1 267 ? -24.777 31.549 64.467 1.00 74.42 ? 267 SER A C 1 ATOM 2137 O O . SER A 1 267 ? -24.605 32.222 65.482 1.00 75.53 ? 267 SER A O 1 ATOM 2138 C CB . SER A 1 267 ? -25.777 32.943 62.658 1.00 74.04 ? 267 SER A CB 1 ATOM 2139 O OG . SER A 1 267 ? -24.582 32.788 61.910 1.00 75.94 ? 267 SER A OG 1 ATOM 2140 N N . GLU A 1 268 ? -23.918 30.622 64.062 1.00 74.07 ? 268 GLU A N 1 ATOM 2141 C CA . GLU A 1 268 ? -22.673 30.373 64.770 1.00 75.06 ? 268 GLU A CA 1 ATOM 2142 C C . GLU A 1 268 ? -21.550 31.273 64.267 1.00 75.32 ? 268 GLU A C 1 ATOM 2143 O O . GLU A 1 268 ? -20.486 31.326 64.872 1.00 80.33 ? 268 GLU A O 1 ATOM 2144 C CB . GLU A 1 268 ? -22.272 28.904 64.632 1.00 77.86 ? 268 GLU A CB 1 ATOM 2145 C CG . GLU A 1 268 ? -23.331 27.925 65.118 1.00 79.16 ? 268 GLU A CG 1 ATOM 2146 C CD . GLU A 1 268 ? -23.748 28.181 66.555 1.00 81.25 ? 268 GLU A CD 1 ATOM 2147 O OE1 . GLU A 1 268 ? -22.858 28.228 67.434 1.00 81.30 ? 268 GLU A OE1 1 ATOM 2148 O OE2 . GLU A 1 268 ? -24.964 28.341 66.804 1.00 82.17 ? 268 GLU A OE2 1 ATOM 2149 N N . LEU A 1 269 ? -21.789 31.990 63.173 1.00 74.15 ? 269 LEU A N 1 ATOM 2150 C CA . LEU A 1 269 ? -20.781 32.875 62.588 1.00 74.94 ? 269 LEU A CA 1 ATOM 2151 C C . LEU A 1 269 ? -20.509 34.076 63.474 1.00 76.83 ? 269 LEU A C 1 ATOM 2152 O O . LEU A 1 269 ? -21.345 34.459 64.294 1.00 73.76 ? 269 LEU A O 1 ATOM 2153 C CB . LEU A 1 269 ? -21.225 33.384 61.213 1.00 73.08 ? 269 LEU A CB 1 ATOM 2154 C CG . LEU A 1 269 ? -21.445 32.364 60.095 1.00 71.95 ? 269 LEU A CG 1 ATOM 2155 C CD1 . LEU A 1 269 ? -21.903 33.076 58.831 1.00 71.13 ? 269 LEU A CD1 1 ATOM 2156 C CD2 . LEU A 1 269 ? -20.181 31.564 59.832 1.00 73.51 ? 269 LEU A CD2 1 ATOM 2157 N N . GLU A 1 270 ? -19.329 34.662 63.283 1.00 82.30 ? 270 GLU A N 1 ATOM 2158 C CA . GLU A 1 270 ? -18.913 35.869 63.988 1.00 86.55 ? 270 GLU A CA 1 ATOM 2159 C C . GLU A 1 270 ? -18.918 37.050 63.014 1.00 85.94 ? 270 GLU A C 1 ATOM 2160 O O . GLU A 1 270 ? -19.262 36.890 61.848 1.00 86.97 ? 270 GLU A O 1 ATOM 2161 C CB . GLU A 1 270 ? -17.517 35.671 64.605 1.00 91.67 ? 270 GLU A CB 1 ATOM 2162 C CG . GLU A 1 270 ? -17.415 34.527 65.618 1.00 94.30 ? 270 GLU A CG 1 ATOM 2163 C CD . GLU A 1 270 ? -17.940 34.880 67.012 1.00 95.74 ? 270 GLU A CD 1 ATOM 2164 O OE1 . GLU A 1 270 ? -19.069 35.414 67.135 1.00 92.22 ? 270 GLU A OE1 1 ATOM 2165 O OE2 . GLU A 1 270 ? -17.214 34.618 68.001 1.00 98.73 ? 270 GLU A OE2 1 ATOM 2166 N N . TYR A 1 271 ? -18.551 38.231 63.503 1.00 86.82 ? 271 TYR A N 1 ATOM 2167 C CA . TYR A 1 271 ? -18.510 39.446 62.686 1.00 87.47 ? 271 TYR A CA 1 ATOM 2168 C C . TYR A 1 271 ? -17.513 39.320 61.524 1.00 90.02 ? 271 TYR A C 1 ATOM 2169 O O . TYR A 1 271 ? -16.450 38.710 61.673 1.00 90.17 ? 271 TYR A O 1 ATOM 2170 C CB . TYR A 1 271 ? -18.142 40.644 63.568 1.00 88.60 ? 271 TYR A CB 1 ATOM 2171 C CG . TYR A 1 271 ? -18.296 41.984 62.895 1.00 89.09 ? 271 TYR A CG 1 ATOM 2172 C CD1 . TYR A 1 271 ? -19.535 42.410 62.439 1.00 87.09 ? 271 TYR A CD1 1 ATOM 2173 C CD2 . TYR A 1 271 ? -17.205 42.834 62.727 1.00 91.02 ? 271 TYR A CD2 1 ATOM 2174 C CE1 . TYR A 1 271 ? -19.688 43.638 61.825 1.00 88.03 ? 271 TYR A CE1 1 ATOM 2175 C CE2 . TYR A 1 271 ? -17.348 44.066 62.115 1.00 92.76 ? 271 TYR A CE2 1 ATOM 2176 C CZ . TYR A 1 271 ? -18.592 44.465 61.663 1.00 91.48 ? 271 TYR A CZ 1 ATOM 2177 O OH . TYR A 1 271 ? -18.733 45.692 61.052 1.00 92.39 ? 271 TYR A OH 1 ATOM 2178 N N . GLY A 1 272 ? -17.862 39.904 60.377 1.00 90.79 ? 272 GLY A N 1 ATOM 2179 C CA . GLY A 1 272 ? -17.062 39.764 59.150 1.00 93.08 ? 272 GLY A CA 1 ATOM 2180 C C . GLY A 1 272 ? -16.372 41.020 58.631 1.00 94.95 ? 272 GLY A C 1 ATOM 2181 O O . GLY A 1 272 ? -15.607 40.945 57.665 1.00 94.62 ? 272 GLY A O 1 ATOM 2182 N N . ASN A 1 273 ? -16.644 42.164 59.263 1.00 94.40 ? 273 ASN A N 1 ATOM 2183 C CA . ASN A 1 273 ? -16.107 43.467 58.841 1.00 95.86 ? 273 ASN A CA 1 ATOM 2184 C C . ASN A 1 273 ? -16.539 43.858 57.429 1.00 93.81 ? 273 ASN A C 1 ATOM 2185 O O . ASN A 1 273 ? -15.724 44.285 56.617 1.00 95.54 ? 273 ASN A O 1 ATOM 2186 C CB . ASN A 1 273 ? -14.578 43.499 58.956 1.00 100.01 ? 273 ASN A CB 1 ATOM 2187 C CG . ASN A 1 273 ? -14.095 43.176 60.352 1.00 102.81 ? 273 ASN A CG 1 ATOM 2188 O OD1 . ASN A 1 273 ? -13.738 42.036 60.644 1.00 105.05 ? 273 ASN A OD1 1 ATOM 2189 N ND2 . ASN A 1 273 ? -14.097 44.174 61.231 1.00 103.50 ? 273 ASN A ND2 1 ATOM 2190 N N . CYS A 1 274 ? -17.831 43.717 57.154 1.00 89.71 ? 274 CYS A N 1 ATOM 2191 C CA . CYS A 1 274 ? -18.391 44.058 55.848 1.00 88.67 ? 274 CYS A CA 1 ATOM 2192 C C . CYS A 1 274 ? -19.652 44.903 56.002 1.00 86.24 ? 274 CYS A C 1 ATOM 2193 O O . CYS A 1 274 ? -20.124 45.134 57.120 1.00 84.51 ? 274 CYS A O 1 ATOM 2194 C CB . CYS A 1 274 ? -18.694 42.782 55.045 1.00 87.29 ? 274 CYS A CB 1 ATOM 2195 S SG . CYS A 1 274 ? -19.356 41.401 56.017 1.00 86.33 ? 274 CYS A SG 1 ATOM 2196 N N . ASN A 1 275 ? -20.177 45.371 54.871 1.00 85.20 ? 275 ASN A N 1 ATOM 2197 C CA . ASN A 1 275 ? -21.448 46.089 54.822 1.00 84.45 ? 275 ASN A CA 1 ATOM 2198 C C . ASN A 1 275 ? -22.341 45.487 53.737 1.00 83.69 ? 275 ASN A C 1 ATOM 2199 O O . ASN A 1 275 ? -21.839 44.965 52.740 1.00 84.68 ? 275 ASN A O 1 ATOM 2200 C CB . ASN A 1 275 ? -21.210 47.576 54.552 1.00 85.65 ? 275 ASN A CB 1 ATOM 2201 C CG . ASN A 1 275 ? -22.456 48.414 54.771 1.00 84.96 ? 275 ASN A CG 1 ATOM 2202 O OD1 . ASN A 1 275 ? -22.950 48.522 55.887 1.00 85.20 ? 275 ASN A OD1 1 ATOM 2203 N ND2 . ASN A 1 275 ? -22.968 49.010 53.707 1.00 85.89 ? 275 ASN A ND2 1 ATOM 2204 N N . THR A 1 276 ? -23.657 45.552 53.934 1.00 82.50 ? 276 THR A N 1 ATOM 2205 C CA . THR A 1 276 ? -24.606 44.970 52.982 1.00 80.40 ? 276 THR A CA 1 ATOM 2206 C C . THR A 1 276 ? -25.994 45.592 53.110 1.00 81.00 ? 276 THR A C 1 ATOM 2207 O O . THR A 1 276 ? -26.293 46.268 54.092 1.00 83.67 ? 276 THR A O 1 ATOM 2208 C CB . THR A 1 276 ? -24.710 43.437 53.157 1.00 77.92 ? 276 THR A CB 1 ATOM 2209 O OG1 . THR A 1 276 ? -25.526 42.880 52.120 1.00 78.59 ? 276 THR A OG1 1 ATOM 2210 C CG2 . THR A 1 276 ? -25.310 43.072 54.503 1.00 77.58 ? 276 THR A CG2 1 ATOM 2211 N N . LYS A 1 277 ? -26.826 45.358 52.099 1.00 81.30 ? 277 LYS A N 1 ATOM 2212 C CA . LYS A 1 277 ? -28.216 45.811 52.083 1.00 82.84 ? 277 LYS A CA 1 ATOM 2213 C C . LYS A 1 277 ? -29.171 44.698 52.504 1.00 78.45 ? 277 LYS A C 1 ATOM 2214 O O . LYS A 1 277 ? -30.369 44.931 52.682 1.00 76.30 ? 277 LYS A O 1 ATOM 2215 C CB . LYS A 1 277 ? -28.598 46.252 50.671 1.00 87.41 ? 277 LYS A CB 1 ATOM 2216 C CG . LYS A 1 277 ? -27.750 47.379 50.105 1.00 93.76 ? 277 LYS A CG 1 ATOM 2217 C CD . LYS A 1 277 ? -28.017 48.693 50.822 1.00 98.77 ? 277 LYS A CD 1 ATOM 2218 C CE . LYS A 1 277 ? -27.860 49.882 49.888 1.00 104.10 ? 277 LYS A CE 1 ATOM 2219 N NZ . LYS A 1 277 ? -28.432 51.120 50.485 1.00 107.82 ? 277 LYS A NZ 1 ATOM 2220 N N . CYS A 1 278 ? -28.635 43.490 52.644 1.00 75.05 ? 278 CYS A N 1 ATOM 2221 C CA . CYS A 1 278 ? -29.441 42.293 52.812 1.00 72.73 ? 278 CYS A CA 1 ATOM 2222 C C . CYS A 1 278 ? -28.600 41.236 53.502 1.00 70.19 ? 278 CYS A C 1 ATOM 2223 O O . CYS A 1 278 ? -27.552 40.838 52.983 1.00 71.13 ? 278 CYS A O 1 ATOM 2224 C CB . CYS A 1 278 ? -29.901 41.785 51.444 1.00 72.72 ? 278 CYS A CB 1 ATOM 2225 S SG . CYS A 1 278 ? -30.740 40.181 51.462 1.00 72.87 ? 278 CYS A SG 1 ATOM 2226 N N . GLN A 1 279 ? -29.055 40.783 54.668 1.00 66.81 ? 279 GLN A N 1 ATOM 2227 C CA . GLN A 1 279 ? -28.273 39.865 55.487 1.00 64.40 ? 279 GLN A CA 1 ATOM 2228 C C . GLN A 1 279 ? -29.046 38.599 55.784 1.00 61.11 ? 279 GLN A C 1 ATOM 2229 O O . GLN A 1 279 ? -30.239 38.651 56.068 1.00 60.09 ? 279 GLN A O 1 ATOM 2230 C CB . GLN A 1 279 ? -27.884 40.531 56.804 1.00 65.10 ? 279 GLN A CB 1 ATOM 2231 C CG . GLN A 1 279 ? -26.961 39.687 57.667 1.00 65.14 ? 279 GLN A CG 1 ATOM 2232 C CD . GLN A 1 279 ? -25.557 39.603 57.103 1.00 66.87 ? 279 GLN A CD 1 ATOM 2233 O OE1 . GLN A 1 279 ? -24.906 40.624 56.893 1.00 68.19 ? 279 GLN A OE1 1 ATOM 2234 N NE2 . GLN A 1 279 ? -25.080 38.387 56.860 1.00 66.92 ? 279 GLN A NE2 1 ATOM 2235 N N . THR A 1 280 ? -28.345 37.470 55.725 1.00 59.85 ? 280 THR A N 1 ATOM 2236 C CA . THR A 1 280 ? -28.894 36.176 56.118 1.00 59.66 ? 280 THR A CA 1 ATOM 2237 C C . THR A 1 280 ? -27.974 35.521 57.149 1.00 59.65 ? 280 THR A C 1 ATOM 2238 O O . THR A 1 280 ? -26.807 35.908 57.267 1.00 59.50 ? 280 THR A O 1 ATOM 2239 C CB . THR A 1 280 ? -29.049 35.223 54.907 1.00 58.87 ? 280 THR A CB 1 ATOM 2240 O OG1 . THR A 1 280 ? -27.843 34.473 54.699 1.00 57.70 ? 280 THR A OG1 1 ATOM 2241 C CG2 . THR A 1 280 ? -29.393 36.002 53.651 1.00 58.95 ? 280 THR A CG2 1 ATOM 2242 N N . PRO A 1 281 ? -28.488 34.518 57.883 1.00 60.03 ? 281 PRO A N 1 ATOM 2243 C CA . PRO A 1 281 ? -27.692 33.781 58.875 1.00 62.61 ? 281 PRO A CA 1 ATOM 2244 C C . PRO A 1 281 ? -26.444 33.092 58.315 1.00 65.16 ? 281 PRO A C 1 ATOM 2245 O O . PRO A 1 281 ? -25.494 32.852 59.064 1.00 64.35 ? 281 PRO A O 1 ATOM 2246 C CB . PRO A 1 281 ? -28.666 32.727 59.404 1.00 62.39 ? 281 PRO A CB 1 ATOM 2247 C CG . PRO A 1 281 ? -30.023 33.255 59.118 1.00 61.52 ? 281 PRO A CG 1 ATOM 2248 C CD . PRO A 1 281 ? -29.912 34.142 57.921 1.00 60.61 ? 281 PRO A CD 1 ATOM 2249 N N . MET A 1 282 ? -26.458 32.771 57.022 1.00 68.22 ? 282 MET A N 1 ATOM 2250 C CA . MET A 1 282 ? -25.327 32.110 56.368 1.00 70.74 ? 282 MET A CA 1 ATOM 2251 C C . MET A 1 282 ? -24.354 33.087 55.722 1.00 68.69 ? 282 MET A C 1 ATOM 2252 O O . MET A 1 282 ? -23.234 32.709 55.388 1.00 68.33 ? 282 MET A O 1 ATOM 2253 C CB . MET A 1 282 ? -25.830 31.143 55.301 1.00 74.64 ? 282 MET A CB 1 ATOM 2254 C CG . MET A 1 282 ? -26.567 29.940 55.857 1.00 77.80 ? 282 MET A CG 1 ATOM 2255 S SD . MET A 1 282 ? -27.259 28.956 54.517 1.00 88.42 ? 282 MET A SD 1 ATOM 2256 C CE . MET A 1 282 ? -25.796 28.575 53.555 1.00 86.07 ? 282 MET A CE 1 ATOM 2257 N N . GLY A 1 283 ? -24.786 34.332 55.540 1.00 67.27 ? 283 GLY A N 1 ATOM 2258 C CA . GLY A 1 283 ? -23.976 35.346 54.865 1.00 68.35 ? 283 GLY A CA 1 ATOM 2259 C C . GLY A 1 283 ? -24.838 36.436 54.261 1.00 67.77 ? 283 GLY A C 1 ATOM 2260 O O . GLY A 1 283 ? -26.063 36.386 54.362 1.00 67.77 ? 283 GLY A O 1 ATOM 2261 N N . ALA A 1 284 ? -24.200 37.414 53.624 1.00 68.65 ? 284 ALA A N 1 ATOM 2262 C CA . ALA A 1 284 ? -24.903 38.575 53.068 1.00 69.88 ? 284 ALA A CA 1 ATOM 2263 C C . ALA A 1 284 ? -25.079 38.473 51.552 1.00 71.65 ? 284 ALA A C 1 ATOM 2264 O O . ALA A 1 284 ? -24.302 37.795 50.868 1.00 73.20 ? 284 ALA A O 1 ATOM 2265 C CB . ALA A 1 284 ? -24.157 39.851 53.416 1.00 71.68 ? 284 ALA A CB 1 ATOM 2266 N N . ILE A 1 285 ? -26.091 39.175 51.039 1.00 71.18 ? 285 ILE A N 1 ATOM 2267 C CA . ILE A 1 285 ? -26.465 39.110 49.624 1.00 71.04 ? 285 ILE A CA 1 ATOM 2268 C C . ILE A 1 285 ? -26.340 40.468 48.936 1.00 73.49 ? 285 ILE A C 1 ATOM 2269 O O . ILE A 1 285 ? -26.898 41.462 49.399 1.00 75.07 ? 285 ILE A O 1 ATOM 2270 C CB . ILE A 1 285 ? -27.908 38.591 49.467 1.00 69.29 ? 285 ILE A CB 1 ATOM 2271 C CG1 . ILE A 1 285 ? -27.947 37.085 49.715 1.00 68.06 ? 285 ILE A CG1 1 ATOM 2272 C CG2 . ILE A 1 285 ? -28.464 38.900 48.084 1.00 69.82 ? 285 ILE A CG2 1 ATOM 2273 C CD1 . ILE A 1 285 ? -29.325 36.553 50.038 1.00 67.51 ? 285 ILE A CD1 1 ATOM 2274 N N . ASN A 1 286 ? -25.615 40.483 47.820 1.00 75.80 ? 286 ASN A N 1 ATOM 2275 C CA . ASN A 1 286 ? -25.456 41.667 46.982 1.00 77.94 ? 286 ASN A CA 1 ATOM 2276 C C . ASN A 1 286 ? -25.813 41.309 45.545 1.00 77.32 ? 286 ASN A C 1 ATOM 2277 O O . ASN A 1 286 ? -24.962 40.851 44.786 1.00 77.75 ? 286 ASN A O 1 ATOM 2278 C CB . ASN A 1 286 ? -24.010 42.172 47.062 1.00 81.54 ? 286 ASN A CB 1 ATOM 2279 C CG . ASN A 1 286 ? -23.746 43.366 46.159 1.00 84.94 ? 286 ASN A CG 1 ATOM 2280 O OD1 . ASN A 1 286 ? -24.576 44.270 46.046 1.00 86.40 ? 286 ASN A OD1 1 ATOM 2281 N ND2 . ASN A 1 286 ? -22.579 43.380 45.518 1.00 87.03 ? 286 ASN A ND2 1 ATOM 2282 N N . SER A 1 287 ? -27.079 41.493 45.179 1.00 76.98 ? 287 SER A N 1 ATOM 2283 C CA . SER A 1 287 ? -27.513 41.235 43.808 1.00 77.87 ? 287 SER A CA 1 ATOM 2284 C C . SER A 1 287 ? -28.823 41.926 43.451 1.00 77.01 ? 287 SER A C 1 ATOM 2285 O O . SER A 1 287 ? -29.603 42.304 44.320 1.00 74.79 ? 287 SER A O 1 ATOM 2286 C CB . SER A 1 287 ? -27.648 39.732 43.557 1.00 77.32 ? 287 SER A CB 1 ATOM 2287 O OG . SER A 1 287 ? -28.839 39.225 44.120 1.00 76.17 ? 287 SER A OG 1 ATOM 2288 N N . SER A 1 288 ? -29.047 42.063 42.148 1.00 78.97 ? 288 SER A N 1 ATOM 2289 C CA . SER A 1 288 ? -30.245 42.696 41.602 1.00 79.66 ? 288 SER A CA 1 ATOM 2290 C C . SER A 1 288 ? -31.284 41.663 41.144 1.00 77.32 ? 288 SER A C 1 ATOM 2291 O O . SER A 1 288 ? -32.282 42.013 40.509 1.00 75.50 ? 288 SER A O 1 ATOM 2292 C CB . SER A 1 288 ? -29.841 43.578 40.428 1.00 82.40 ? 288 SER A CB 1 ATOM 2293 O OG . SER A 1 288 ? -29.084 42.825 39.495 1.00 83.30 ? 288 SER A OG 1 ATOM 2294 N N . MET A 1 289 ? -31.050 40.395 41.478 1.00 75.38 ? 289 MET A N 1 ATOM 2295 C CA . MET A 1 289 ? -31.967 39.313 41.134 1.00 73.21 ? 289 MET A CA 1 ATOM 2296 C C . MET A 1 289 ? -33.279 39.471 41.889 1.00 71.71 ? 289 MET A C 1 ATOM 2297 O O . MET A 1 289 ? -33.290 39.972 43.008 1.00 73.90 ? 289 MET A O 1 ATOM 2298 C CB . MET A 1 289 ? -31.375 37.961 41.531 1.00 73.92 ? 289 MET A CB 1 ATOM 2299 C CG . MET A 1 289 ? -30.048 37.609 40.893 1.00 75.35 ? 289 MET A CG 1 ATOM 2300 S SD . MET A 1 289 ? -30.223 37.297 39.138 1.00 75.65 ? 289 MET A SD 1 ATOM 2301 C CE . MET A 1 289 ? -28.945 36.057 38.938 1.00 74.97 ? 289 MET A CE 1 ATOM 2302 N N . PRO A 1 290 ? -34.392 39.028 41.290 1.00 69.20 ? 290 PRO A N 1 ATOM 2303 C CA . PRO A 1 290 ? -35.652 39.006 42.021 1.00 68.05 ? 290 PRO A CA 1 ATOM 2304 C C . PRO A 1 290 ? -35.750 37.864 43.033 1.00 66.06 ? 290 PRO A C 1 ATOM 2305 O O . PRO A 1 290 ? -36.605 37.915 43.917 1.00 66.51 ? 290 PRO A O 1 ATOM 2306 C CB . PRO A 1 290 ? -36.684 38.808 40.912 1.00 67.77 ? 290 PRO A CB 1 ATOM 2307 C CG . PRO A 1 290 ? -35.951 38.031 39.886 1.00 67.31 ? 290 PRO A CG 1 ATOM 2308 C CD . PRO A 1 290 ? -34.570 38.608 39.890 1.00 67.98 ? 290 PRO A CD 1 ATOM 2309 N N . PHE A 1 291 ? -34.903 36.843 42.897 1.00 64.29 ? 291 PHE A N 1 ATOM 2310 C CA . PHE A 1 291 ? -34.939 35.682 43.787 1.00 63.61 ? 291 PHE A CA 1 ATOM 2311 C C . PHE A 1 291 ? -33.570 35.278 44.285 1.00 60.97 ? 291 PHE A C 1 ATOM 2312 O O . PHE A 1 291 ? -32.559 35.571 43.654 1.00 60.91 ? 291 PHE A O 1 ATOM 2313 C CB . PHE A 1 291 ? -35.481 34.459 43.064 1.00 66.15 ? 291 PHE A CB 1 ATOM 2314 C CG . PHE A 1 291 ? -36.899 34.580 42.619 1.00 68.18 ? 291 PHE A CG 1 ATOM 2315 C CD1 . PHE A 1 291 ? -37.934 34.399 43.523 1.00 69.55 ? 291 PHE A CD1 1 ATOM 2316 C CD2 . PHE A 1 291 ? -37.202 34.826 41.288 1.00 68.67 ? 291 PHE A CD2 1 ATOM 2317 C CE1 . PHE A 1 291 ? -39.249 34.484 43.112 1.00 70.13 ? 291 PHE A CE1 1 ATOM 2318 C CE2 . PHE A 1 291 ? -38.517 34.915 40.871 1.00 70.52 ? 291 PHE A CE2 1 ATOM 2319 C CZ . PHE A 1 291 ? -39.540 34.740 41.784 1.00 70.34 ? 291 PHE A CZ 1 ATOM 2320 N N . HIS A 1 292 ? -33.562 34.557 45.401 1.00 59.56 ? 292 HIS A N 1 ATOM 2321 C CA . HIS A 1 292 ? -32.365 33.875 45.895 1.00 58.15 ? 292 HIS A CA 1 ATOM 2322 C C . HIS A 1 292 ? -32.761 32.557 46.561 1.00 56.48 ? 292 HIS A C 1 ATOM 2323 O O . HIS A 1 292 ? -33.945 32.300 46.787 1.00 56.83 ? 292 HIS A O 1 ATOM 2324 C CB . HIS A 1 292 ? -31.611 34.763 46.880 1.00 59.14 ? 292 HIS A CB 1 ATOM 2325 C CG . HIS A 1 292 ? -32.300 34.921 48.198 1.00 59.22 ? 292 HIS A CG 1 ATOM 2326 N ND1 . HIS A 1 292 ? -31.834 34.335 49.353 1.00 58.95 ? 292 HIS A ND1 1 ATOM 2327 C CD2 . HIS A 1 292 ? -33.429 35.581 48.540 1.00 60.44 ? 292 HIS A CD2 1 ATOM 2328 C CE1 . HIS A 1 292 ? -32.641 34.637 50.353 1.00 60.07 ? 292 HIS A CE1 1 ATOM 2329 N NE2 . HIS A 1 292 ? -33.620 35.390 49.887 1.00 60.64 ? 292 HIS A NE2 1 ATOM 2330 N N . ASN A 1 293 ? -31.773 31.726 46.871 1.00 55.05 ? 293 ASN A N 1 ATOM 2331 C CA . ASN A 1 293 ? -32.034 30.435 47.501 1.00 54.69 ? 293 ASN A CA 1 ATOM 2332 C C . ASN A 1 293 ? -31.094 30.148 48.675 1.00 55.41 ? 293 ASN A C 1 ATOM 2333 O O . ASN A 1 293 ? -30.794 28.994 48.977 1.00 56.01 ? 293 ASN A O 1 ATOM 2334 C CB . ASN A 1 293 ? -31.955 29.322 46.449 1.00 53.98 ? 293 ASN A CB 1 ATOM 2335 C CG . ASN A 1 293 ? -30.534 29.033 45.990 1.00 53.74 ? 293 ASN A CG 1 ATOM 2336 O OD1 . ASN A 1 293 ? -29.589 29.774 46.281 1.00 53.11 ? 293 ASN A OD1 1 ATOM 2337 N ND2 . ASN A 1 293 ? -30.379 27.943 45.263 1.00 54.20 ? 293 ASN A ND2 1 ATOM 2338 N N . ILE A 1 294 ? -30.648 31.207 49.339 1.00 55.57 ? 294 ILE A N 1 ATOM 2339 C CA . ILE A 1 294 ? -29.660 31.092 50.411 1.00 58.08 ? 294 ILE A CA 1 ATOM 2340 C C . ILE A 1 294 ? -30.294 30.608 51.717 1.00 58.49 ? 294 ILE A C 1 ATOM 2341 O O . ILE A 1 294 ? -29.925 29.554 52.234 1.00 58.58 ? 294 ILE A O 1 ATOM 2342 C CB . ILE A 1 294 ? -28.938 32.440 50.654 1.00 58.97 ? 294 ILE A CB 1 ATOM 2343 C CG1 . ILE A 1 294 ? -28.291 32.956 49.355 1.00 59.51 ? 294 ILE A CG1 1 ATOM 2344 C CG2 . ILE A 1 294 ? -27.900 32.305 51.753 1.00 59.90 ? 294 ILE A CG2 1 ATOM 2345 C CD1 . ILE A 1 294 ? -27.456 31.930 48.618 1.00 59.99 ? 294 ILE A CD1 1 ATOM 2346 N N . HIS A 1 295 ? -31.248 31.376 52.235 1.00 59.27 ? 295 HIS A N 1 ATOM 2347 C CA . HIS A 1 295 ? -31.869 31.092 53.526 1.00 61.53 ? 295 HIS A CA 1 ATOM 2348 C C . HIS A 1 295 ? -33.179 31.877 53.636 1.00 61.12 ? 295 HIS A C 1 ATOM 2349 O O . HIS A 1 295 ? -33.251 33.008 53.163 1.00 59.43 ? 295 HIS A O 1 ATOM 2350 C CB . HIS A 1 295 ? -30.905 31.516 54.636 1.00 64.61 ? 295 HIS A CB 1 ATOM 2351 C CG . HIS A 1 295 ? -31.220 30.942 55.980 1.00 67.29 ? 295 HIS A CG 1 ATOM 2352 N ND1 . HIS A 1 295 ? -32.197 31.463 56.799 1.00 68.96 ? 295 HIS A ND1 1 ATOM 2353 C CD2 . HIS A 1 295 ? -30.662 29.917 56.667 1.00 70.34 ? 295 HIS A CD2 1 ATOM 2354 C CE1 . HIS A 1 295 ? -32.245 30.771 57.924 1.00 69.79 ? 295 HIS A CE1 1 ATOM 2355 N NE2 . HIS A 1 295 ? -31.321 29.829 57.871 1.00 70.60 ? 295 HIS A NE2 1 ATOM 2356 N N . PRO A 1 296 ? -34.222 31.290 54.254 1.00 62.65 ? 296 PRO A N 1 ATOM 2357 C CA . PRO A 1 296 ? -35.504 32.010 54.313 1.00 62.36 ? 296 PRO A CA 1 ATOM 2358 C C . PRO A 1 296 ? -35.489 33.271 55.184 1.00 63.17 ? 296 PRO A C 1 ATOM 2359 O O . PRO A 1 296 ? -35.996 34.306 54.765 1.00 63.66 ? 296 PRO A O 1 ATOM 2360 C CB . PRO A 1 296 ? -36.482 30.967 54.876 1.00 62.21 ? 296 PRO A CB 1 ATOM 2361 C CG . PRO A 1 296 ? -35.641 29.926 55.517 1.00 62.81 ? 296 PRO A CG 1 ATOM 2362 C CD . PRO A 1 296 ? -34.333 29.917 54.781 1.00 63.24 ? 296 PRO A CD 1 ATOM 2363 N N . LEU A 1 297 ? -34.931 33.175 56.386 1.00 65.07 ? 297 LEU A N 1 ATOM 2364 C CA . LEU A 1 297 ? -34.893 34.308 57.322 1.00 67.12 ? 297 LEU A CA 1 ATOM 2365 C C . LEU A 1 297 ? -33.857 35.347 56.905 1.00 65.07 ? 297 LEU A C 1 ATOM 2366 O O . LEU A 1 297 ? -32.661 35.130 57.069 1.00 66.44 ? 297 LEU A O 1 ATOM 2367 C CB . LEU A 1 297 ? -34.586 33.828 58.747 1.00 69.44 ? 297 LEU A CB 1 ATOM 2368 C CG . LEU A 1 297 ? -35.469 32.715 59.334 1.00 73.08 ? 297 LEU A CG 1 ATOM 2369 C CD1 . LEU A 1 297 ? -34.880 32.208 60.649 1.00 74.61 ? 297 LEU A CD1 1 ATOM 2370 C CD2 . LEU A 1 297 ? -36.907 33.189 59.530 1.00 74.68 ? 297 LEU A CD2 1 ATOM 2371 N N . THR A 1 298 ? -34.311 36.469 56.357 1.00 63.00 ? 298 THR A N 1 ATOM 2372 C CA . THR A 1 298 ? -33.403 37.552 55.987 1.00 61.67 ? 298 THR A CA 1 ATOM 2373 C C . THR A 1 298 ? -33.871 38.868 56.586 1.00 62.10 ? 298 THR A C 1 ATOM 2374 O O . THR A 1 298 ? -34.974 38.959 57.126 1.00 60.75 ? 298 THR A O 1 ATOM 2375 C CB . THR A 1 298 ? -33.264 37.715 54.455 1.00 60.53 ? 298 THR A CB 1 ATOM 2376 O OG1 . THR A 1 298 ? -34.360 38.476 53.931 1.00 58.98 ? 298 THR A OG1 1 ATOM 2377 C CG2 . THR A 1 298 ? -33.207 36.366 53.771 1.00 60.59 ? 298 THR A CG2 1 ATOM 2378 N N . ILE A 1 299 ? -33.017 39.881 56.487 1.00 61.90 ? 299 ILE A N 1 ATOM 2379 C CA . ILE A 1 299 ? -33.369 41.224 56.908 1.00 63.94 ? 299 ILE A CA 1 ATOM 2380 C C . ILE A 1 299 ? -32.764 42.230 55.937 1.00 66.28 ? 299 ILE A C 1 ATOM 2381 O O . ILE A 1 299 ? -31.650 42.029 55.441 1.00 65.25 ? 299 ILE A O 1 ATOM 2382 C CB . ILE A 1 299 ? -32.921 41.499 58.362 1.00 65.27 ? 299 ILE A CB 1 ATOM 2383 C CG1 . ILE A 1 299 ? -33.319 42.912 58.791 1.00 66.80 ? 299 ILE A CG1 1 ATOM 2384 C CG2 . ILE A 1 299 ? -31.422 41.289 58.534 1.00 65.40 ? 299 ILE A CG2 1 ATOM 2385 C CD1 . ILE A 1 299 ? -33.439 43.079 60.284 1.00 67.98 ? 299 ILE A CD1 1 ATOM 2386 N N . GLY A 1 300 ? -33.515 43.297 55.664 1.00 69.39 ? 300 GLY A N 1 ATOM 2387 C CA . GLY A 1 300 ? -33.102 44.333 54.721 1.00 74.02 ? 300 GLY A CA 1 ATOM 2388 C C . GLY A 1 300 ? -33.826 44.225 53.390 1.00 77.78 ? 300 GLY A C 1 ATOM 2389 O O . GLY A 1 300 ? -34.782 43.452 53.252 1.00 78.92 ? 300 GLY A O 1 ATOM 2390 N N . GLU A 1 301 ? -33.363 44.999 52.408 1.00 81.63 ? 301 GLU A N 1 ATOM 2391 C CA . GLU A 1 301 ? -33.943 44.980 51.062 1.00 84.13 ? 301 GLU A CA 1 ATOM 2392 C C . GLU A 1 301 ? -33.380 43.768 50.336 1.00 79.63 ? 301 GLU A C 1 ATOM 2393 O O . GLU A 1 301 ? -32.259 43.809 49.828 1.00 78.32 ? 301 GLU A O 1 ATOM 2394 C CB . GLU A 1 301 ? -33.623 46.276 50.294 1.00 90.59 ? 301 GLU A CB 1 ATOM 2395 C CG . GLU A 1 301 ? -34.842 46.954 49.670 1.00 96.28 ? 301 GLU A CG 1 ATOM 2396 C CD . GLU A 1 301 ? -35.744 47.641 50.697 1.00 101.24 ? 301 GLU A CD 1 ATOM 2397 O OE1 . GLU A 1 301 ? -35.235 48.142 51.726 1.00 100.73 ? 301 GLU A OE1 1 ATOM 2398 O OE2 . GLU A 1 301 ? -36.974 47.684 50.476 1.00 107.29 ? 301 GLU A OE2 1 ATOM 2399 N N . CYS A 1 302 ? -34.159 42.685 50.314 1.00 76.79 ? 302 CYS A N 1 ATOM 2400 C CA . CYS A 1 302 ? -33.690 41.395 49.815 1.00 74.13 ? 302 CYS A CA 1 ATOM 2401 C C . CYS A 1 302 ? -34.505 40.889 48.626 1.00 70.90 ? 302 CYS A C 1 ATOM 2402 O O . CYS A 1 302 ? -35.652 41.292 48.429 1.00 70.14 ? 302 CYS A O 1 ATOM 2403 C CB . CYS A 1 302 ? -33.759 40.345 50.929 1.00 74.93 ? 302 CYS A CB 1 ATOM 2404 S SG . CYS A 1 302 ? -32.578 40.565 52.286 1.00 77.97 ? 302 CYS A SG 1 ATOM 2405 N N . PRO A 1 303 ? -33.914 39.983 47.833 1.00 67.45 ? 303 PRO A N 1 ATOM 2406 C CA . PRO A 1 303 ? -34.723 39.235 46.878 1.00 67.18 ? 303 PRO A CA 1 ATOM 2407 C C . PRO A 1 303 ? -35.630 38.251 47.614 1.00 66.55 ? 303 PRO A C 1 ATOM 2408 O O . PRO A 1 303 ? -35.446 38.023 48.813 1.00 67.80 ? 303 PRO A O 1 ATOM 2409 C CB . PRO A 1 303 ? -33.685 38.473 46.034 1.00 66.63 ? 303 PRO A CB 1 ATOM 2410 C CG . PRO A 1 303 ? -32.346 39.003 46.431 1.00 66.94 ? 303 PRO A CG 1 ATOM 2411 C CD . PRO A 1 303 ? -32.501 39.573 47.804 1.00 66.84 ? 303 PRO A CD 1 ATOM 2412 N N . LYS A 1 304 ? -36.582 37.659 46.905 1.00 65.20 ? 304 LYS A N 1 ATOM 2413 C CA . LYS A 1 304 ? -37.489 36.701 47.520 1.00 65.24 ? 304 LYS A CA 1 ATOM 2414 C C . LYS A 1 304 ? -36.822 35.338 47.588 1.00 62.48 ? 304 LYS A C 1 ATOM 2415 O O . LYS A 1 304 ? -36.108 34.940 46.671 1.00 62.64 ? 304 LYS A O 1 ATOM 2416 C CB . LYS A 1 304 ? -38.799 36.605 46.740 1.00 69.00 ? 304 LYS A CB 1 ATOM 2417 C CG . LYS A 1 304 ? -39.451 37.950 46.446 1.00 74.05 ? 304 LYS A CG 1 ATOM 2418 C CD . LYS A 1 304 ? -39.944 38.643 47.708 1.00 78.40 ? 304 LYS A CD 1 ATOM 2419 C CE . LYS A 1 304 ? -39.698 40.144 47.659 1.00 82.16 ? 304 LYS A CE 1 ATOM 2420 N NZ . LYS A 1 304 ? -40.163 40.801 48.912 1.00 84.60 ? 304 LYS A NZ 1 ATOM 2421 N N . TYR A 1 305 ? -37.050 34.625 48.684 1.00 60.12 ? 305 TYR A N 1 ATOM 2422 C CA . TYR A 1 305 ? -36.464 33.311 48.863 1.00 57.81 ? 305 TYR A CA 1 ATOM 2423 C C . TYR A 1 305 ? -37.327 32.254 48.204 1.00 57.66 ? 305 TYR A C 1 ATOM 2424 O O . TYR A 1 305 ? -38.542 32.252 48.373 1.00 58.63 ? 305 TYR A O 1 ATOM 2425 C CB . TYR A 1 305 ? -36.317 32.980 50.345 1.00 57.77 ? 305 TYR A CB 1 ATOM 2426 C CG . TYR A 1 305 ? -35.807 31.579 50.582 1.00 56.98 ? 305 TYR A CG 1 ATOM 2427 C CD1 . TYR A 1 305 ? -34.452 31.290 50.508 1.00 57.15 ? 305 TYR A CD1 1 ATOM 2428 C CD2 . TYR A 1 305 ? -36.680 30.542 50.856 1.00 56.85 ? 305 TYR A CD2 1 ATOM 2429 C CE1 . TYR A 1 305 ? -33.983 30.006 50.716 1.00 57.62 ? 305 TYR A CE1 1 ATOM 2430 C CE2 . TYR A 1 305 ? -36.221 29.255 51.063 1.00 57.63 ? 305 TYR A CE2 1 ATOM 2431 C CZ . TYR A 1 305 ? -34.872 28.994 50.994 1.00 57.32 ? 305 TYR A CZ 1 ATOM 2432 O OH . TYR A 1 305 ? -34.407 27.721 51.194 1.00 57.40 ? 305 TYR A OH 1 ATOM 2433 N N . VAL A 1 306 ? -36.690 31.355 47.458 1.00 57.01 ? 306 VAL A N 1 ATOM 2434 C CA . VAL A 1 306 ? -37.343 30.143 46.968 1.00 56.85 ? 306 VAL A CA 1 ATOM 2435 C C . VAL A 1 306 ? -36.449 28.936 47.223 1.00 57.63 ? 306 VAL A C 1 ATOM 2436 O O . VAL A 1 306 ? -35.257 29.080 47.491 1.00 57.08 ? 306 VAL A O 1 ATOM 2437 C CB . VAL A 1 306 ? -37.688 30.230 45.467 1.00 56.98 ? 306 VAL A CB 1 ATOM 2438 C CG1 . VAL A 1 306 ? -38.787 31.249 45.237 1.00 57.28 ? 306 VAL A CG1 1 ATOM 2439 C CG2 . VAL A 1 306 ? -36.460 30.568 44.632 1.00 56.46 ? 306 VAL A CG2 1 ATOM 2440 N N . LYS A 1 307 ? -37.028 27.747 47.131 1.00 60.17 ? 307 LYS A N 1 ATOM 2441 C CA . LYS A 1 307 ? -36.273 26.512 47.332 1.00 63.14 ? 307 LYS A CA 1 ATOM 2442 C C . LYS A 1 307 ? -35.603 25.980 46.054 1.00 62.89 ? 307 LYS A C 1 ATOM 2443 O O . LYS A 1 307 ? -35.067 24.873 46.059 1.00 65.69 ? 307 LYS A O 1 ATOM 2444 C CB . LYS A 1 307 ? -37.181 25.427 47.932 1.00 65.72 ? 307 LYS A CB 1 ATOM 2445 C CG . LYS A 1 307 ? -37.315 25.518 49.438 1.00 67.75 ? 307 LYS A CG 1 ATOM 2446 C CD . LYS A 1 307 ? -38.117 24.354 49.989 1.00 71.72 ? 307 LYS A CD 1 ATOM 2447 C CE . LYS A 1 307 ? -38.408 24.544 51.466 1.00 75.25 ? 307 LYS A CE 1 ATOM 2448 N NZ . LYS A 1 307 ? -39.348 23.511 51.984 1.00 80.09 ? 307 LYS A NZ 1 ATOM 2449 N N . SER A 1 308 ? -35.613 26.755 44.973 1.00 61.04 ? 308 SER A N 1 ATOM 2450 C CA . SER A 1 308 ? -35.111 26.266 43.688 1.00 60.76 ? 308 SER A CA 1 ATOM 2451 C C . SER A 1 308 ? -33.591 26.250 43.634 1.00 60.51 ? 308 SER A C 1 ATOM 2452 O O . SER A 1 308 ? -32.926 27.044 44.293 1.00 60.04 ? 308 SER A O 1 ATOM 2453 C CB . SER A 1 308 ? -35.643 27.124 42.538 1.00 59.18 ? 308 SER A CB 1 ATOM 2454 O OG . SER A 1 308 ? -37.036 27.312 42.652 1.00 58.42 ? 308 SER A OG 1 ATOM 2455 N N . ASN A 1 309 ? -33.057 25.331 42.839 1.00 62.61 ? 309 ASN A N 1 ATOM 2456 C CA . ASN A 1 309 ? -31.636 25.310 42.504 1.00 63.89 ? 309 ASN A CA 1 ATOM 2457 C C . ASN A 1 309 ? -31.342 26.110 41.245 1.00 62.74 ? 309 ASN A C 1 ATOM 2458 O O . ASN A 1 309 ? -30.198 26.498 41.006 1.00 62.61 ? 309 ASN A O 1 ATOM 2459 C CB . ASN A 1 309 ? -31.177 23.869 42.296 1.00 66.58 ? 309 ASN A CB 1 ATOM 2460 C CG . ASN A 1 309 ? -31.234 23.059 43.575 1.00 69.35 ? 309 ASN A CG 1 ATOM 2461 O OD1 . ASN A 1 309 ? -30.737 23.496 44.619 1.00 69.44 ? 309 ASN A OD1 1 ATOM 2462 N ND2 . ASN A 1 309 ? -31.842 21.877 43.508 1.00 71.44 ? 309 ASN A ND2 1 ATOM 2463 N N . ARG A 1 310 ? -32.384 26.356 40.451 1.00 62.10 ? 310 ARG A N 1 ATOM 2464 C CA . ARG A 1 310 ? -32.234 26.931 39.121 1.00 62.35 ? 310 ARG A CA 1 ATOM 2465 C C . ARG A 1 310 ? -33.524 27.626 38.650 1.00 58.38 ? 310 ARG A C 1 ATOM 2466 O O . ARG A 1 310 ? -34.597 27.021 38.631 1.00 56.03 ? 310 ARG A O 1 ATOM 2467 C CB . ARG A 1 310 ? -31.847 25.818 38.139 1.00 67.35 ? 310 ARG A CB 1 ATOM 2468 C CG . ARG A 1 310 ? -31.253 26.315 36.830 1.00 72.90 ? 310 ARG A CG 1 ATOM 2469 C CD . ARG A 1 310 ? -31.168 25.216 35.776 1.00 77.63 ? 310 ARG A CD 1 ATOM 2470 N NE . ARG A 1 310 ? -31.084 25.779 34.425 1.00 80.05 ? 310 ARG A NE 1 ATOM 2471 C CZ . ARG A 1 310 ? -29.979 26.292 33.878 1.00 83.18 ? 310 ARG A CZ 1 ATOM 2472 N NH1 . ARG A 1 310 ? -28.824 26.321 34.547 1.00 84.51 ? 310 ARG A NH1 1 ATOM 2473 N NH2 . ARG A 1 310 ? -30.026 26.777 32.644 1.00 83.15 ? 310 ARG A NH2 1 ATOM 2474 N N . LEU A 1 311 ? -33.411 28.904 38.292 1.00 55.27 ? 311 LEU A N 1 ATOM 2475 C CA . LEU A 1 311 ? -34.499 29.631 37.631 1.00 54.08 ? 311 LEU A CA 1 ATOM 2476 C C . LEU A 1 311 ? -33.939 30.515 36.528 1.00 52.72 ? 311 LEU A C 1 ATOM 2477 O O . LEU A 1 311 ? -33.354 31.566 36.797 1.00 54.69 ? 311 LEU A O 1 ATOM 2478 C CB . LEU A 1 311 ? -35.279 30.496 38.617 1.00 53.32 ? 311 LEU A CB 1 ATOM 2479 C CG . LEU A 1 311 ? -36.199 29.788 39.607 1.00 53.88 ? 311 LEU A CG 1 ATOM 2480 C CD1 . LEU A 1 311 ? -36.808 30.817 40.540 1.00 54.33 ? 311 LEU A CD1 1 ATOM 2481 C CD2 . LEU A 1 311 ? -37.294 29.011 38.903 1.00 54.49 ? 311 LEU A CD2 1 ATOM 2482 N N . VAL A 1 312 ? -34.128 30.079 35.290 1.00 50.95 ? 312 VAL A N 1 ATOM 2483 C CA . VAL A 1 312 ? -33.612 30.783 34.127 1.00 50.11 ? 312 VAL A CA 1 ATOM 2484 C C . VAL A 1 312 ? -34.728 30.993 33.116 1.00 49.28 ? 312 VAL A C 1 ATOM 2485 O O . VAL A 1 312 ? -35.417 30.049 32.737 1.00 48.16 ? 312 VAL A O 1 ATOM 2486 C CB . VAL A 1 312 ? -32.479 29.984 33.464 1.00 50.54 ? 312 VAL A CB 1 ATOM 2487 C CG1 . VAL A 1 312 ? -31.946 30.721 32.242 1.00 50.74 ? 312 VAL A CG1 1 ATOM 2488 C CG2 . VAL A 1 312 ? -31.367 29.718 34.472 1.00 50.28 ? 312 VAL A CG2 1 ATOM 2489 N N . LEU A 1 313 ? -34.900 32.240 32.694 1.00 49.39 ? 313 LEU A N 1 ATOM 2490 C CA . LEU A 1 313 ? -35.920 32.593 31.713 1.00 50.02 ? 313 LEU A CA 1 ATOM 2491 C C . LEU A 1 313 ? -35.315 32.626 30.331 1.00 50.20 ? 313 LEU A C 1 ATOM 2492 O O . LEU A 1 313 ? -34.201 33.111 30.148 1.00 51.86 ? 313 LEU A O 1 ATOM 2493 C CB . LEU A 1 313 ? -36.507 33.971 32.007 1.00 50.26 ? 313 LEU A CB 1 ATOM 2494 C CG . LEU A 1 313 ? -37.548 34.020 33.117 1.00 51.17 ? 313 LEU A CG 1 ATOM 2495 C CD1 . LEU A 1 313 ? -37.739 35.452 33.592 1.00 51.82 ? 313 LEU A CD1 1 ATOM 2496 C CD2 . LEU A 1 313 ? -38.867 33.418 32.646 1.00 51.96 ? 313 LEU A CD2 1 ATOM 2497 N N . ALA A 1 314 ? -36.055 32.115 29.359 1.00 49.87 ? 314 ALA A N 1 ATOM 2498 C CA . ALA A 1 314 ? -35.696 32.296 27.969 1.00 49.82 ? 314 ALA A CA 1 ATOM 2499 C C . ALA A 1 314 ? -36.000 33.738 27.628 1.00 50.40 ? 314 ALA A C 1 ATOM 2500 O O . ALA A 1 314 ? -37.085 34.233 27.944 1.00 50.90 ? 314 ALA A O 1 ATOM 2501 C CB . ALA A 1 314 ? -36.501 31.362 27.074 1.00 49.67 ? 314 ALA A CB 1 ATOM 2502 N N . THR A 1 315 ? -35.029 34.417 27.025 1.00 50.81 ? 315 THR A N 1 ATOM 2503 C CA . THR A 1 315 ? -35.276 35.693 26.350 1.00 51.00 ? 315 THR A CA 1 ATOM 2504 C C . THR A 1 315 ? -35.155 35.520 24.853 1.00 50.36 ? 315 THR A C 1 ATOM 2505 O O . THR A 1 315 ? -35.943 36.077 24.103 1.00 51.32 ? 315 THR A O 1 ATOM 2506 C CB . THR A 1 315 ? -34.289 36.783 26.788 1.00 51.59 ? 315 THR A CB 1 ATOM 2507 O OG1 . THR A 1 315 ? -32.955 36.266 26.738 1.00 52.03 ? 315 THR A OG1 1 ATOM 2508 C CG2 . THR A 1 315 ? -34.614 37.261 28.202 1.00 51.26 ? 315 THR A CG2 1 ATOM 2509 N N . GLY A 1 316 ? -34.162 34.748 24.427 1.00 50.19 ? 316 GLY A N 1 ATOM 2510 C CA . GLY A 1 316 ? -33.915 34.510 23.012 1.00 51.02 ? 316 GLY A CA 1 ATOM 2511 C C . GLY A 1 316 ? -34.699 33.335 22.480 1.00 50.91 ? 316 GLY A C 1 ATOM 2512 O O . GLY A 1 316 ? -35.701 32.932 23.066 1.00 50.16 ? 316 GLY A O 1 ATOM 2513 N N . LEU A 1 317 ? -34.231 32.773 21.372 1.00 52.53 ? 317 LEU A N 1 ATOM 2514 C CA . LEU A 1 317 ? -34.947 31.683 20.710 1.00 54.00 ? 317 LEU A CA 1 ATOM 2515 C C . LEU A 1 317 ? -34.108 30.416 20.672 1.00 54.76 ? 317 LEU A C 1 ATOM 2516 O O . LEU A 1 317 ? -32.920 30.443 20.976 1.00 54.07 ? 317 LEU A O 1 ATOM 2517 C CB . LEU A 1 317 ? -35.414 32.092 19.302 1.00 54.65 ? 317 LEU A CB 1 ATOM 2518 C CG . LEU A 1 317 ? -34.481 32.914 18.414 1.00 55.71 ? 317 LEU A CG 1 ATOM 2519 C CD1 . LEU A 1 317 ? -33.370 32.033 17.884 1.00 57.25 ? 317 LEU A CD1 1 ATOM 2520 C CD2 . LEU A 1 317 ? -35.241 33.549 17.262 1.00 56.33 ? 317 LEU A CD2 1 ATOM 2521 N N . ARG A 1 318 ? -34.751 29.308 20.322 1.00 56.62 ? 318 ARG A N 1 ATOM 2522 C CA . ARG A 1 318 ? -34.085 28.021 20.236 1.00 59.15 ? 318 ARG A CA 1 ATOM 2523 C C . ARG A 1 318 ? -32.863 28.148 19.344 1.00 61.22 ? 318 ARG A C 1 ATOM 2524 O O . ARG A 1 318 ? -32.975 28.478 18.162 1.00 60.57 ? 318 ARG A O 1 ATOM 2525 C CB . ARG A 1 318 ? -35.033 26.958 19.685 1.00 61.24 ? 318 ARG A CB 1 ATOM 2526 C CG . ARG A 1 318 ? -34.449 25.553 19.649 1.00 64.50 ? 318 ARG A CG 1 ATOM 2527 C CD . ARG A 1 318 ? -35.443 24.565 19.063 1.00 66.87 ? 318 ARG A CD 1 ATOM 2528 N NE . ARG A 1 318 ? -36.544 24.300 19.989 1.00 68.46 ? 318 ARG A NE 1 ATOM 2529 C CZ . ARG A 1 318 ? -36.577 23.307 20.877 1.00 70.91 ? 318 ARG A CZ 1 ATOM 2530 N NH1 . ARG A 1 318 ? -35.566 22.446 20.984 1.00 72.78 ? 318 ARG A NH1 1 ATOM 2531 N NH2 . ARG A 1 318 ? -37.635 23.171 21.671 1.00 71.35 ? 318 ARG A NH2 1 ATOM 2532 N N . ASN A 1 319 ? -31.698 27.895 19.929 1.00 64.11 ? 319 ASN A N 1 ATOM 2533 C CA . ASN A 1 319 ? -30.434 28.034 19.235 1.00 66.96 ? 319 ASN A CA 1 ATOM 2534 C C . ASN A 1 319 ? -30.110 26.782 18.433 1.00 74.13 ? 319 ASN A C 1 ATOM 2535 O O . ASN A 1 319 ? -30.269 25.667 18.923 1.00 75.61 ? 319 ASN A O 1 ATOM 2536 C CB . ASN A 1 319 ? -29.332 28.300 20.245 1.00 65.57 ? 319 ASN A CB 1 ATOM 2537 C CG . ASN A 1 319 ? -28.065 28.808 19.606 1.00 65.33 ? 319 ASN A CG 1 ATOM 2538 O OD1 . ASN A 1 319 ? -28.025 29.082 18.408 1.00 65.08 ? 319 ASN A OD1 1 ATOM 2539 N ND2 . ASN A 1 319 ? -27.015 28.942 20.408 1.00 65.29 ? 319 ASN A ND2 1 ATOM 2540 N N . SER A 1 320 ? -29.646 26.977 17.201 1.00 84.49 ? 320 SER A N 1 ATOM 2541 C CA . SER A 1 320 ? -29.335 25.868 16.294 1.00 91.59 ? 320 SER A CA 1 ATOM 2542 C C . SER A 1 320 ? -28.021 25.178 16.671 1.00 99.31 ? 320 SER A C 1 ATOM 2543 O O . SER A 1 320 ? -27.089 25.840 17.142 1.00 98.75 ? 320 SER A O 1 ATOM 2544 C CB . SER A 1 320 ? -29.244 26.374 14.856 1.00 91.63 ? 320 SER A CB 1 ATOM 2545 O OG . SER A 1 320 ? -30.398 27.124 14.531 1.00 92.59 ? 320 SER A OG 1 ATOM 2546 N N . PRO A 1 321 ? -27.934 23.847 16.447 1.00 107.10 ? 321 PRO A N 1 ATOM 2547 C CA . PRO A 1 321 ? -26.727 23.098 16.827 1.00 111.90 ? 321 PRO A CA 1 ATOM 2548 C C . PRO A 1 321 ? -25.503 23.455 15.982 1.00 112.58 ? 321 PRO A C 1 ATOM 2549 O O . PRO A 1 321 ? -25.623 23.635 14.771 1.00 110.91 ? 321 PRO A O 1 ATOM 2550 C CB . PRO A 1 321 ? -27.124 21.626 16.597 1.00 113.74 ? 321 PRO A CB 1 ATOM 2551 C CG . PRO A 1 321 ? -28.592 21.620 16.321 1.00 110.96 ? 321 PRO A CG 1 ATOM 2552 C CD . PRO A 1 321 ? -28.929 22.978 15.792 1.00 108.39 ? 321 PRO A CD 1 ATOM 2553 N N . GLY B 2 1 ? -41.696 23.347 17.131 1.00 49.86 ? 1 GLY B N 1 ATOM 2554 C CA . GLY B 2 1 ? -42.450 24.490 17.713 1.00 48.49 ? 1 GLY B CA 1 ATOM 2555 C C . GLY B 2 1 ? -43.830 24.638 17.116 1.00 48.16 ? 1 GLY B C 1 ATOM 2556 O O . GLY B 2 1 ? -44.096 24.173 16.012 1.00 52.00 ? 1 GLY B O 1 ATOM 2557 N N . LEU B 2 2 ? -44.703 25.320 17.839 1.00 47.05 ? 2 LEU B N 1 ATOM 2558 C CA . LEU B 2 2 ? -46.108 25.402 17.462 1.00 46.94 ? 2 LEU B CA 1 ATOM 2559 C C . LEU B 2 2 ? -46.369 25.993 16.077 1.00 47.21 ? 2 LEU B C 1 ATOM 2560 O O . LEU B 2 2 ? -47.323 25.602 15.418 1.00 49.23 ? 2 LEU B O 1 ATOM 2561 C CB . LEU B 2 2 ? -46.884 26.208 18.503 1.00 45.60 ? 2 LEU B CB 1 ATOM 2562 C CG . LEU B 2 2 ? -47.241 25.472 19.790 1.00 44.73 ? 2 LEU B CG 1 ATOM 2563 C CD1 . LEU B 2 2 ? -47.925 26.413 20.769 1.00 43.49 ? 2 LEU B CD1 1 ATOM 2564 C CD2 . LEU B 2 2 ? -48.118 24.274 19.489 1.00 45.12 ? 2 LEU B CD2 1 ATOM 2565 N N . PHE B 2 3 ? -45.532 26.924 15.639 1.00 46.60 ? 3 PHE B N 1 ATOM 2566 C CA . PHE B 2 3 ? -45.824 27.680 14.427 1.00 48.19 ? 3 PHE B CA 1 ATOM 2567 C C . PHE B 2 3 ? -45.055 27.187 13.207 1.00 50.15 ? 3 PHE B C 1 ATOM 2568 O O . PHE B 2 3 ? -45.237 27.706 12.107 1.00 51.79 ? 3 PHE B O 1 ATOM 2569 C CB . PHE B 2 3 ? -45.650 29.178 14.702 1.00 47.56 ? 3 PHE B CB 1 ATOM 2570 C CG . PHE B 2 3 ? -46.642 29.688 15.708 1.00 47.65 ? 3 PHE B CG 1 ATOM 2571 C CD1 . PHE B 2 3 ? -47.909 30.097 15.308 1.00 47.45 ? 3 PHE B CD1 1 ATOM 2572 C CD2 . PHE B 2 3 ? -46.349 29.659 17.066 1.00 47.40 ? 3 PHE B CD2 1 ATOM 2573 C CE1 . PHE B 2 3 ? -48.846 30.511 16.240 1.00 48.46 ? 3 PHE B CE1 1 ATOM 2574 C CE2 . PHE B 2 3 ? -47.290 30.067 18.004 1.00 47.82 ? 3 PHE B CE2 1 ATOM 2575 C CZ . PHE B 2 3 ? -48.539 30.496 17.591 1.00 47.42 ? 3 PHE B CZ 1 ATOM 2576 N N . GLY B 2 4 ? -44.217 26.170 13.411 1.00 51.56 ? 4 GLY B N 1 ATOM 2577 C CA . GLY B 2 4 ? -43.629 25.409 12.321 1.00 51.21 ? 4 GLY B CA 1 ATOM 2578 C C . GLY B 2 4 ? -42.387 25.983 11.675 1.00 51.28 ? 4 GLY B C 1 ATOM 2579 O O . GLY B 2 4 ? -41.734 25.288 10.905 1.00 53.86 ? 4 GLY B O 1 ATOM 2580 N N . ALA B 2 5 ? -42.037 27.233 11.965 1.00 49.74 ? 5 ALA B N 1 ATOM 2581 C CA . ALA B 2 5 ? -40.922 27.866 11.259 1.00 49.37 ? 5 ALA B CA 1 ATOM 2582 C C . ALA B 2 5 ? -39.580 27.472 11.850 1.00 49.59 ? 5 ALA B C 1 ATOM 2583 O O . ALA B 2 5 ? -38.786 26.783 11.201 1.00 49.36 ? 5 ALA B O 1 ATOM 2584 C CB . ALA B 2 5 ? -41.078 29.380 11.245 1.00 48.85 ? 5 ALA B CB 1 ATOM 2585 N N . ILE B 2 6 ? -39.337 27.912 13.083 1.00 49.04 ? 6 ILE B N 1 ATOM 2586 C CA . ILE B 2 6 ? -38.060 27.686 13.756 1.00 49.23 ? 6 ILE B CA 1 ATOM 2587 C C . ILE B 2 6 ? -37.851 26.194 13.974 1.00 50.88 ? 6 ILE B C 1 ATOM 2588 O O . ILE B 2 6 ? -38.701 25.530 14.562 1.00 52.17 ? 6 ILE B O 1 ATOM 2589 C CB . ILE B 2 6 ? -38.006 28.420 15.110 1.00 48.47 ? 6 ILE B CB 1 ATOM 2590 C CG1 . ILE B 2 6 ? -37.981 29.933 14.884 1.00 48.54 ? 6 ILE B CG1 1 ATOM 2591 C CG2 . ILE B 2 6 ? -36.783 27.991 15.907 1.00 49.36 ? 6 ILE B CG2 1 ATOM 2592 C CD1 . ILE B 2 6 ? -38.096 30.747 16.156 1.00 48.65 ? 6 ILE B CD1 1 ATOM 2593 N N . ALA B 2 7 ? -36.728 25.673 13.487 1.00 53.24 ? 7 ALA B N 1 ATOM 2594 C CA . ALA B 2 7 ? -36.437 24.238 13.546 1.00 55.56 ? 7 ALA B CA 1 ATOM 2595 C C . ALA B 2 7 ? -37.591 23.409 12.988 1.00 57.61 ? 7 ALA B C 1 ATOM 2596 O O . ALA B 2 7 ? -37.918 22.347 13.519 1.00 60.38 ? 7 ALA B O 1 ATOM 2597 C CB . ALA B 2 7 ? -36.132 23.822 14.975 1.00 56.07 ? 7 ALA B CB 1 ATOM 2598 N N . GLY B 2 8 ? -38.213 23.914 11.928 1.00 57.86 ? 8 GLY B N 1 ATOM 2599 C CA . GLY B 2 8 ? -39.328 23.243 11.271 1.00 58.62 ? 8 GLY B CA 1 ATOM 2600 C C . GLY B 2 8 ? -39.074 23.271 9.778 1.00 59.54 ? 8 GLY B C 1 ATOM 2601 O O . GLY B 2 8 ? -38.217 22.541 9.301 1.00 60.45 ? 8 GLY B O 1 ATOM 2602 N N . PHE B 2 9 ? -39.791 24.118 9.039 1.00 58.17 ? 9 PHE B N 1 ATOM 2603 C CA . PHE B 2 9 ? -39.518 24.257 7.616 1.00 59.62 ? 9 PHE B CA 1 ATOM 2604 C C . PHE B 2 9 ? -38.269 25.098 7.381 1.00 60.34 ? 9 PHE B C 1 ATOM 2605 O O . PHE B 2 9 ? -37.682 25.034 6.303 1.00 63.90 ? 9 PHE B O 1 ATOM 2606 C CB . PHE B 2 9 ? -40.745 24.738 6.813 1.00 59.90 ? 9 PHE B CB 1 ATOM 2607 C CG . PHE B 2 9 ? -41.117 26.177 7.019 1.00 57.96 ? 9 PHE B CG 1 ATOM 2608 C CD1 . PHE B 2 9 ? -40.560 27.168 6.232 1.00 59.18 ? 9 PHE B CD1 1 ATOM 2609 C CD2 . PHE B 2 9 ? -42.068 26.532 7.955 1.00 57.47 ? 9 PHE B CD2 1 ATOM 2610 C CE1 . PHE B 2 9 ? -40.912 28.495 6.406 1.00 58.30 ? 9 PHE B CE1 1 ATOM 2611 C CE2 . PHE B 2 9 ? -42.432 27.855 8.133 1.00 56.59 ? 9 PHE B CE2 1 ATOM 2612 C CZ . PHE B 2 9 ? -41.849 28.838 7.359 1.00 57.04 ? 9 PHE B CZ 1 ATOM 2613 N N . ILE B 2 10 ? -37.856 25.866 8.392 1.00 59.29 ? 10 ILE B N 1 ATOM 2614 C CA . ILE B 2 10 ? -36.548 26.535 8.397 1.00 58.47 ? 10 ILE B CA 1 ATOM 2615 C C . ILE B 2 10 ? -35.614 25.752 9.323 1.00 61.34 ? 10 ILE B C 1 ATOM 2616 O O . ILE B 2 10 ? -35.641 25.925 10.541 1.00 61.72 ? 10 ILE B O 1 ATOM 2617 C CB . ILE B 2 10 ? -36.660 27.998 8.860 1.00 55.95 ? 10 ILE B CB 1 ATOM 2618 C CG1 . ILE B 2 10 ? -37.624 28.765 7.954 1.00 55.27 ? 10 ILE B CG1 1 ATOM 2619 C CG2 . ILE B 2 10 ? -35.295 28.672 8.853 1.00 56.00 ? 10 ILE B CG2 1 ATOM 2620 C CD1 . ILE B 2 10 ? -37.974 30.147 8.460 1.00 54.63 ? 10 ILE B CD1 1 ATOM 2621 N N . GLU B 2 11 ? -34.793 24.889 8.730 1.00 65.05 ? 11 GLU B N 1 ATOM 2622 C CA . GLU B 2 11 ? -33.968 23.925 9.466 1.00 68.81 ? 11 GLU B CA 1 ATOM 2623 C C . GLU B 2 11 ? -33.207 24.489 10.657 1.00 67.20 ? 11 GLU B C 1 ATOM 2624 O O . GLU B 2 11 ? -33.178 23.872 11.722 1.00 68.24 ? 11 GLU B O 1 ATOM 2625 C CB . GLU B 2 11 ? -32.940 23.294 8.533 1.00 75.89 ? 11 GLU B CB 1 ATOM 2626 C CG . GLU B 2 11 ? -33.501 22.316 7.520 1.00 81.02 ? 11 GLU B CG 1 ATOM 2627 C CD . GLU B 2 11 ? -32.396 21.659 6.718 1.00 88.41 ? 11 GLU B CD 1 ATOM 2628 O OE1 . GLU B 2 11 ? -31.628 22.388 6.041 1.00 88.40 ? 11 GLU B OE1 1 ATOM 2629 O OE2 . GLU B 2 11 ? -32.289 20.414 6.778 1.00 95.61 ? 11 GLU B OE2 1 ATOM 2630 N N . GLY B 2 12 ? -32.570 25.640 10.461 1.00 65.28 ? 12 GLY B N 1 ATOM 2631 C CA . GLY B 2 12 ? -31.704 26.232 11.483 1.00 64.10 ? 12 GLY B CA 1 ATOM 2632 C C . GLY B 2 12 ? -31.530 27.738 11.372 1.00 62.18 ? 12 GLY B C 1 ATOM 2633 O O . GLY B 2 12 ? -31.908 28.357 10.376 1.00 62.16 ? 12 GLY B O 1 ATOM 2634 N N . GLY B 2 13 ? -30.952 28.325 12.413 1.00 60.77 ? 13 GLY B N 1 ATOM 2635 C CA . GLY B 2 13 ? -30.684 29.755 12.461 1.00 59.35 ? 13 GLY B CA 1 ATOM 2636 C C . GLY B 2 13 ? -29.432 30.162 11.700 1.00 60.02 ? 13 GLY B C 1 ATOM 2637 O O . GLY B 2 13 ? -28.774 29.335 11.068 1.00 60.99 ? 13 GLY B O 1 ATOM 2638 N N . TRP B 2 14 ? -29.102 31.449 11.786 1.00 58.35 ? 14 TRP B N 1 ATOM 2639 C CA . TRP B 2 14 ? -28.000 32.034 11.046 1.00 57.32 ? 14 TRP B CA 1 ATOM 2640 C C . TRP B 2 14 ? -26.996 32.711 11.964 1.00 59.29 ? 14 TRP B C 1 ATOM 2641 O O . TRP B 2 14 ? -27.256 33.788 12.494 1.00 57.26 ? 14 TRP B O 1 ATOM 2642 C CB . TRP B 2 14 ? -28.532 33.075 10.071 1.00 55.52 ? 14 TRP B CB 1 ATOM 2643 C CG . TRP B 2 14 ? -29.319 32.522 8.933 1.00 53.54 ? 14 TRP B CG 1 ATOM 2644 C CD1 . TRP B 2 14 ? -29.191 31.294 8.366 1.00 53.71 ? 14 TRP B CD1 1 ATOM 2645 C CD2 . TRP B 2 14 ? -30.327 33.208 8.180 1.00 51.90 ? 14 TRP B CD2 1 ATOM 2646 N NE1 . TRP B 2 14 ? -30.076 31.161 7.323 1.00 53.20 ? 14 TRP B NE1 1 ATOM 2647 C CE2 . TRP B 2 14 ? -30.780 32.327 7.187 1.00 51.41 ? 14 TRP B CE2 1 ATOM 2648 C CE3 . TRP B 2 14 ? -30.898 34.481 8.261 1.00 51.44 ? 14 TRP B CE3 1 ATOM 2649 C CZ2 . TRP B 2 14 ? -31.778 32.672 6.285 1.00 50.56 ? 14 TRP B CZ2 1 ATOM 2650 C CZ3 . TRP B 2 14 ? -31.887 34.821 7.364 1.00 50.34 ? 14 TRP B CZ3 1 ATOM 2651 C CH2 . TRP B 2 14 ? -32.315 33.922 6.388 1.00 49.82 ? 14 TRP B CH2 1 ATOM 2652 N N . GLN B 2 15 ? -25.834 32.084 12.119 1.00 63.38 ? 15 GLN B N 1 ATOM 2653 C CA . GLN B 2 15 ? -24.700 32.699 12.814 1.00 66.31 ? 15 GLN B CA 1 ATOM 2654 C C . GLN B 2 15 ? -24.355 34.068 12.213 1.00 66.19 ? 15 GLN B C 1 ATOM 2655 O O . GLN B 2 15 ? -23.929 34.974 12.927 1.00 67.35 ? 15 GLN B O 1 ATOM 2656 C CB . GLN B 2 15 ? -23.470 31.787 12.730 1.00 70.27 ? 15 GLN B CB 1 ATOM 2657 C CG . GLN B 2 15 ? -23.583 30.465 13.484 1.00 71.99 ? 15 GLN B CG 1 ATOM 2658 C CD . GLN B 2 15 ? -23.182 30.577 14.949 1.00 75.22 ? 15 GLN B CD 1 ATOM 2659 O OE1 . GLN B 2 15 ? -22.134 31.142 15.284 1.00 78.39 ? 15 GLN B OE1 1 ATOM 2660 N NE2 . GLN B 2 15 ? -24.010 30.024 15.832 1.00 74.08 ? 15 GLN B NE2 1 ATOM 2661 N N . GLY B 2 16 ? -24.540 34.204 10.900 1.00 65.30 ? 16 GLY B N 1 ATOM 2662 C CA . GLY B 2 16 ? -24.191 35.428 10.172 1.00 66.16 ? 16 GLY B CA 1 ATOM 2663 C C . GLY B 2 16 ? -25.155 36.604 10.273 1.00 65.07 ? 16 GLY B C 1 ATOM 2664 O O . GLY B 2 16 ? -24.854 37.688 9.772 1.00 66.07 ? 16 GLY B O 1 ATOM 2665 N N . MET B 2 17 ? -26.315 36.405 10.896 1.00 63.31 ? 17 MET B N 1 ATOM 2666 C CA . MET B 2 17 ? -27.223 37.515 11.180 1.00 62.45 ? 17 MET B CA 1 ATOM 2667 C C . MET B 2 17 ? -27.105 37.951 12.646 1.00 62.24 ? 17 MET B C 1 ATOM 2668 O O . MET B 2 17 ? -27.754 37.402 13.534 1.00 59.24 ? 17 MET B O 1 ATOM 2669 C CB . MET B 2 17 ? -28.659 37.143 10.847 1.00 61.14 ? 17 MET B CB 1 ATOM 2670 C CG . MET B 2 17 ? -29.589 38.338 10.896 1.00 61.38 ? 17 MET B CG 1 ATOM 2671 S SD . MET B 2 17 ? -31.206 37.877 10.299 1.00 62.17 ? 17 MET B SD 1 ATOM 2672 C CE . MET B 2 17 ? -31.681 36.683 11.549 1.00 62.12 ? 17 MET B CE 1 ATOM 2673 N N . VAL B 2 18 ? -26.284 38.968 12.869 1.00 64.39 ? 18 VAL B N 1 ATOM 2674 C CA . VAL B 2 18 ? -25.861 39.369 14.198 1.00 66.45 ? 18 VAL B CA 1 ATOM 2675 C C . VAL B 2 18 ? -26.663 40.543 14.755 1.00 66.97 ? 18 VAL B C 1 ATOM 2676 O O . VAL B 2 18 ? -26.759 40.707 15.971 1.00 68.80 ? 18 VAL B O 1 ATOM 2677 C CB . VAL B 2 18 ? -24.372 39.761 14.183 1.00 69.78 ? 18 VAL B CB 1 ATOM 2678 C CG1 . VAL B 2 18 ? -23.893 40.084 15.591 1.00 74.18 ? 18 VAL B CG1 1 ATOM 2679 C CG2 . VAL B 2 18 ? -23.540 38.639 13.576 1.00 70.04 ? 18 VAL B CG2 1 ATOM 2680 N N . ASP B 2 19 ? -27.245 41.350 13.876 1.00 66.60 ? 19 ASP B N 1 ATOM 2681 C CA . ASP B 2 19 ? -27.888 42.597 14.290 1.00 67.36 ? 19 ASP B CA 1 ATOM 2682 C C . ASP B 2 19 ? -29.406 42.466 14.506 1.00 64.13 ? 19 ASP B C 1 ATOM 2683 O O . ASP B 2 19 ? -30.113 43.466 14.571 1.00 64.37 ? 19 ASP B O 1 ATOM 2684 C CB . ASP B 2 19 ? -27.556 43.723 13.286 1.00 70.29 ? 19 ASP B CB 1 ATOM 2685 C CG . ASP B 2 19 ? -27.979 43.398 11.851 1.00 69.73 ? 19 ASP B CG 1 ATOM 2686 O OD1 . ASP B 2 19 ? -28.205 42.209 11.523 1.00 67.44 ? 19 ASP B OD1 1 ATOM 2687 O OD2 . ASP B 2 19 ? -28.073 44.345 11.042 1.00 72.21 ? 19 ASP B OD2 1 ATOM 2688 N N . GLY B 2 20 ? -29.909 41.242 14.636 1.00 61.09 ? 20 GLY B N 1 ATOM 2689 C CA . GLY B 2 20 ? -31.328 41.045 14.898 1.00 59.47 ? 20 GLY B CA 1 ATOM 2690 C C . GLY B 2 20 ? -31.702 39.604 15.156 1.00 58.29 ? 20 GLY B C 1 ATOM 2691 O O . GLY B 2 20 ? -30.885 38.708 14.967 1.00 60.08 ? 20 GLY B O 1 ATOM 2692 N N . TRP B 2 21 ? -32.941 39.385 15.589 1.00 56.74 ? 21 TRP B N 1 ATOM 2693 C CA . TRP B 2 21 ? -33.438 38.035 15.854 1.00 55.41 ? 21 TRP B CA 1 ATOM 2694 C C . TRP B 2 21 ? -34.009 37.376 14.603 1.00 52.70 ? 21 TRP B C 1 ATOM 2695 O O . TRP B 2 21 ? -33.840 36.176 14.393 1.00 51.58 ? 21 TRP B O 1 ATOM 2696 C CB . TRP B 2 21 ? -34.507 38.049 16.955 1.00 56.15 ? 21 TRP B CB 1 ATOM 2697 C CG . TRP B 2 21 ? -33.979 37.869 18.355 1.00 57.88 ? 21 TRP B CG 1 ATOM 2698 C CD1 . TRP B 2 21 ? -32.911 37.111 18.750 1.00 58.91 ? 21 TRP B CD1 1 ATOM 2699 C CD2 . TRP B 2 21 ? -34.533 38.422 19.544 1.00 59.20 ? 21 TRP B CD2 1 ATOM 2700 N NE1 . TRP B 2 21 ? -32.756 37.179 20.107 1.00 59.25 ? 21 TRP B NE1 1 ATOM 2701 C CE2 . TRP B 2 21 ? -33.740 37.978 20.621 1.00 59.86 ? 21 TRP B CE2 1 ATOM 2702 C CE3 . TRP B 2 21 ? -35.625 39.256 19.805 1.00 60.43 ? 21 TRP B CE3 1 ATOM 2703 C CZ2 . TRP B 2 21 ? -34.001 38.342 21.938 1.00 61.27 ? 21 TRP B CZ2 1 ATOM 2704 C CZ3 . TRP B 2 21 ? -35.888 39.615 21.114 1.00 61.66 ? 21 TRP B CZ3 1 ATOM 2705 C CH2 . TRP B 2 21 ? -35.078 39.160 22.166 1.00 61.92 ? 21 TRP B CH2 1 ATOM 2706 N N . TYR B 2 22 ? -34.710 38.163 13.793 1.00 51.62 ? 22 TYR B N 1 ATOM 2707 C CA . TYR B 2 22 ? -35.299 37.679 12.549 1.00 49.50 ? 22 TYR B CA 1 ATOM 2708 C C . TYR B 2 22 ? -34.885 38.594 11.419 1.00 50.36 ? 22 TYR B C 1 ATOM 2709 O O . TYR B 2 22 ? -34.646 39.787 11.626 1.00 50.53 ? 22 TYR B O 1 ATOM 2710 C CB . TYR B 2 22 ? -36.821 37.674 12.631 1.00 47.91 ? 22 TYR B CB 1 ATOM 2711 C CG . TYR B 2 22 ? -37.377 37.503 14.021 1.00 47.04 ? 22 TYR B CG 1 ATOM 2712 C CD1 . TYR B 2 22 ? -37.288 36.287 14.681 1.00 45.95 ? 22 TYR B CD1 1 ATOM 2713 C CD2 . TYR B 2 22 ? -37.999 38.559 14.673 1.00 47.28 ? 22 TYR B CD2 1 ATOM 2714 C CE1 . TYR B 2 22 ? -37.806 36.129 15.954 1.00 45.15 ? 22 TYR B CE1 1 ATOM 2715 C CE2 . TYR B 2 22 ? -38.513 38.409 15.941 1.00 46.43 ? 22 TYR B CE2 1 ATOM 2716 C CZ . TYR B 2 22 ? -38.413 37.195 16.576 1.00 44.91 ? 22 TYR B CZ 1 ATOM 2717 O OH . TYR B 2 22 ? -38.925 37.041 17.836 1.00 43.69 ? 22 TYR B OH 1 ATOM 2718 N N . GLY B 2 23 ? -34.823 38.040 10.217 1.00 50.91 ? 23 GLY B N 1 ATOM 2719 C CA . GLY B 2 23 ? -34.429 38.827 9.066 1.00 52.44 ? 23 GLY B CA 1 ATOM 2720 C C . GLY B 2 23 ? -34.319 38.048 7.779 1.00 52.57 ? 23 GLY B C 1 ATOM 2721 O O . GLY B 2 23 ? -34.861 36.947 7.654 1.00 50.45 ? 23 GLY B O 1 ATOM 2722 N N . TYR B 2 24 ? -33.592 38.641 6.833 1.00 55.39 ? 24 TYR B N 1 ATOM 2723 C CA . TYR B 2 24 ? -33.544 38.197 5.446 1.00 55.29 ? 24 TYR B CA 1 ATOM 2724 C C . TYR B 2 24 ? -32.133 37.856 5.049 1.00 55.41 ? 24 TYR B C 1 ATOM 2725 O O . TYR B 2 24 ? -31.199 38.530 5.461 1.00 56.18 ? 24 TYR B O 1 ATOM 2726 C CB . TYR B 2 24 ? -34.011 39.326 4.527 1.00 56.93 ? 24 TYR B CB 1 ATOM 2727 C CG . TYR B 2 24 ? -35.304 39.963 4.952 1.00 58.65 ? 24 TYR B CG 1 ATOM 2728 C CD1 . TYR B 2 24 ? -36.521 39.465 4.511 1.00 58.79 ? 24 TYR B CD1 1 ATOM 2729 C CD2 . TYR B 2 24 ? -35.313 41.067 5.801 1.00 59.83 ? 24 TYR B CD2 1 ATOM 2730 C CE1 . TYR B 2 24 ? -37.713 40.045 4.905 1.00 60.18 ? 24 TYR B CE1 1 ATOM 2731 C CE2 . TYR B 2 24 ? -36.501 41.654 6.199 1.00 60.79 ? 24 TYR B CE2 1 ATOM 2732 C CZ . TYR B 2 24 ? -37.699 41.135 5.750 1.00 60.83 ? 24 TYR B CZ 1 ATOM 2733 O OH . TYR B 2 24 ? -38.890 41.705 6.137 1.00 63.90 ? 24 TYR B OH 1 ATOM 2734 N N . HIS B 2 25 ? -31.982 36.823 4.227 1.00 55.93 ? 25 HIS B N 1 ATOM 2735 C CA . HIS B 2 25 ? -30.731 36.593 3.503 1.00 57.19 ? 25 HIS B CA 1 ATOM 2736 C C . HIS B 2 25 ? -31.007 36.581 2.012 1.00 57.83 ? 25 HIS B C 1 ATOM 2737 O O . HIS B 2 25 ? -31.921 35.904 1.566 1.00 56.44 ? 25 HIS B O 1 ATOM 2738 C CB . HIS B 2 25 ? -30.095 35.270 3.902 1.00 57.12 ? 25 HIS B CB 1 ATOM 2739 C CG . HIS B 2 25 ? -28.801 34.996 3.205 1.00 58.46 ? 25 HIS B CG 1 ATOM 2740 N ND1 . HIS B 2 25 ? -28.717 34.203 2.082 1.00 58.77 ? 25 HIS B ND1 1 ATOM 2741 C CD2 . HIS B 2 25 ? -27.541 35.423 3.460 1.00 60.75 ? 25 HIS B CD2 1 ATOM 2742 C CE1 . HIS B 2 25 ? -27.460 34.143 1.682 1.00 60.67 ? 25 HIS B CE1 1 ATOM 2743 N NE2 . HIS B 2 25 ? -26.726 34.877 2.498 1.00 61.79 ? 25 HIS B NE2 1 ATOM 2744 N N . HIS B 2 26 ? -30.212 37.324 1.244 1.00 61.43 ? 26 HIS B N 1 ATOM 2745 C CA . HIS B 2 26 ? -30.415 37.427 -0.203 1.00 62.99 ? 26 HIS B CA 1 ATOM 2746 C C . HIS B 2 26 ? -29.223 36.890 -0.988 1.00 64.32 ? 26 HIS B C 1 ATOM 2747 O O . HIS B 2 26 ? -28.112 36.823 -0.472 1.00 65.78 ? 26 HIS B O 1 ATOM 2748 C CB . HIS B 2 26 ? -30.714 38.878 -0.601 1.00 64.40 ? 26 HIS B CB 1 ATOM 2749 C CG . HIS B 2 26 ? -29.522 39.781 -0.566 1.00 66.71 ? 26 HIS B CG 1 ATOM 2750 N ND1 . HIS B 2 26 ? -29.060 40.358 0.596 1.00 68.45 ? 26 HIS B ND1 1 ATOM 2751 C CD2 . HIS B 2 26 ? -28.701 40.214 -1.553 1.00 68.05 ? 26 HIS B CD2 1 ATOM 2752 C CE1 . HIS B 2 26 ? -28.003 41.105 0.325 1.00 69.57 ? 26 HIS B CE1 1 ATOM 2753 N NE2 . HIS B 2 26 ? -27.767 41.035 -0.973 1.00 69.63 ? 26 HIS B NE2 1 ATOM 2754 N N . SER B 2 27 ? -29.481 36.507 -2.235 1.00 64.78 ? 27 SER B N 1 ATOM 2755 C CA . SER B 2 27 ? -28.462 36.007 -3.157 1.00 65.98 ? 27 SER B CA 1 ATOM 2756 C C . SER B 2 27 ? -28.807 36.432 -4.573 1.00 66.77 ? 27 SER B C 1 ATOM 2757 O O . SER B 2 27 ? -29.823 36.005 -5.110 1.00 66.01 ? 27 SER B O 1 ATOM 2758 C CB . SER B 2 27 ? -28.399 34.480 -3.116 1.00 66.18 ? 27 SER B CB 1 ATOM 2759 O OG . SER B 2 27 ? -27.258 34.044 -2.414 1.00 68.25 ? 27 SER B OG 1 ATOM 2760 N N . ASN B 2 28 ? -27.966 37.272 -5.168 1.00 67.65 ? 28 ASN B N 1 ATOM 2761 C CA . ASN B 2 28 ? -28.160 37.716 -6.541 1.00 69.00 ? 28 ASN B CA 1 ATOM 2762 C C . ASN B 2 28 ? -26.812 37.929 -7.235 1.00 72.34 ? 28 ASN B C 1 ATOM 2763 O O . ASN B 2 28 ? -25.761 37.682 -6.642 1.00 71.99 ? 28 ASN B O 1 ATOM 2764 C CB . ASN B 2 28 ? -29.030 38.985 -6.571 1.00 67.88 ? 28 ASN B CB 1 ATOM 2765 C CG . ASN B 2 28 ? -28.363 40.186 -5.917 1.00 67.52 ? 28 ASN B CG 1 ATOM 2766 O OD1 . ASN B 2 28 ? -27.198 40.141 -5.527 1.00 67.66 ? 28 ASN B OD1 1 ATOM 2767 N ND2 . ASN B 2 28 ? -29.112 41.276 -5.798 1.00 67.45 ? 28 ASN B ND2 1 ATOM 2768 N N . GLU B 2 29 ? -26.834 38.381 -8.484 1.00 75.64 ? 29 GLU B N 1 ATOM 2769 C CA . GLU B 2 29 ? -25.588 38.582 -9.217 1.00 79.97 ? 29 GLU B CA 1 ATOM 2770 C C . GLU B 2 29 ? -24.604 39.417 -8.409 1.00 80.41 ? 29 GLU B C 1 ATOM 2771 O O . GLU B 2 29 ? -23.437 39.067 -8.305 1.00 81.39 ? 29 GLU B O 1 ATOM 2772 C CB . GLU B 2 29 ? -25.839 39.253 -10.566 1.00 84.69 ? 29 GLU B CB 1 ATOM 2773 C CG . GLU B 2 29 ? -26.644 38.399 -11.539 1.00 86.53 ? 29 GLU B CG 1 ATOM 2774 C CD . GLU B 2 29 ? -26.360 38.719 -12.998 1.00 89.51 ? 29 GLU B CD 1 ATOM 2775 O OE1 . GLU B 2 29 ? -25.876 39.832 -13.307 1.00 92.08 ? 29 GLU B OE1 1 ATOM 2776 O OE2 . GLU B 2 29 ? -26.619 37.839 -13.843 1.00 91.40 ? 29 GLU B OE2 1 ATOM 2777 N N . GLN B 2 30 ? -25.093 40.499 -7.815 1.00 80.68 ? 30 GLN B N 1 ATOM 2778 C CA . GLN B 2 30 ? -24.234 41.458 -7.119 1.00 81.85 ? 30 GLN B CA 1 ATOM 2779 C C . GLN B 2 30 ? -23.631 40.949 -5.804 1.00 79.30 ? 30 GLN B C 1 ATOM 2780 O O . GLN B 2 30 ? -22.655 41.521 -5.311 1.00 79.88 ? 30 GLN B O 1 ATOM 2781 C CB . GLN B 2 30 ? -25.000 42.753 -6.855 1.00 85.07 ? 30 GLN B CB 1 ATOM 2782 C CG . GLN B 2 30 ? -25.401 43.509 -8.113 1.00 89.55 ? 30 GLN B CG 1 ATOM 2783 C CD . GLN B 2 30 ? -26.760 44.166 -7.973 1.00 92.79 ? 30 GLN B CD 1 ATOM 2784 O OE1 . GLN B 2 30 ? -27.779 43.483 -7.826 1.00 92.36 ? 30 GLN B OE1 1 ATOM 2785 N NE2 . GLN B 2 30 ? -26.785 45.497 -8.007 1.00 95.28 ? 30 GLN B NE2 1 ATOM 2786 N N . GLY B 2 31 ? -24.200 39.895 -5.226 1.00 75.39 ? 31 GLY B N 1 ATOM 2787 C CA . GLY B 2 31 ? -23.633 39.319 -4.005 1.00 74.05 ? 31 GLY B CA 1 ATOM 2788 C C . GLY B 2 31 ? -24.637 38.663 -3.090 1.00 69.41 ? 31 GLY B C 1 ATOM 2789 O O . GLY B 2 31 ? -25.657 38.158 -3.539 1.00 68.69 ? 31 GLY B O 1 ATOM 2790 N N . SER B 2 32 ? -24.335 38.658 -1.798 1.00 68.05 ? 32 SER B N 1 ATOM 2791 C CA . SER B 2 32 ? -25.225 38.052 -0.813 1.00 66.17 ? 32 SER B CA 1 ATOM 2792 C C . SER B 2 32 ? -24.999 38.618 0.576 1.00 66.13 ? 32 SER B C 1 ATOM 2793 O O . SER B 2 32 ? -23.967 39.228 0.846 1.00 68.49 ? 32 SER B O 1 ATOM 2794 C CB . SER B 2 32 ? -25.022 36.538 -0.779 1.00 65.58 ? 32 SER B CB 1 ATOM 2795 O OG . SER B 2 32 ? -23.722 36.213 -0.342 1.00 66.69 ? 32 SER B OG 1 ATOM 2796 N N . GLY B 2 33 ? -25.963 38.406 1.462 1.00 64.78 ? 33 GLY B N 1 ATOM 2797 C CA . GLY B 2 33 ? -25.820 38.870 2.832 1.00 65.30 ? 33 GLY B CA 1 ATOM 2798 C C . GLY B 2 33 ? -27.074 38.810 3.672 1.00 62.88 ? 33 GLY B C 1 ATOM 2799 O O . GLY B 2 33 ? -28.150 38.474 3.184 1.00 61.09 ? 33 GLY B O 1 ATOM 2800 N N . TYR B 2 34 ? -26.916 39.156 4.946 1.00 62.53 ? 34 TYR B N 1 ATOM 2801 C CA . TYR B 2 34 ? -28.005 39.129 5.908 1.00 60.35 ? 34 TYR B CA 1 ATOM 2802 C C . TYR B 2 34 ? -28.465 40.536 6.208 1.00 60.27 ? 34 TYR B C 1 ATOM 2803 O O . TYR B 2 34 ? -27.664 41.456 6.238 1.00 62.30 ? 34 TYR B O 1 ATOM 2804 C CB . TYR B 2 34 ? -27.549 38.456 7.194 1.00 59.98 ? 34 TYR B CB 1 ATOM 2805 C CG . TYR B 2 34 ? -27.005 37.066 6.970 1.00 60.63 ? 34 TYR B CG 1 ATOM 2806 C CD1 . TYR B 2 34 ? -25.667 36.871 6.643 1.00 62.95 ? 34 TYR B CD1 1 ATOM 2807 C CD2 . TYR B 2 34 ? -27.824 35.945 7.071 1.00 58.68 ? 34 TYR B CD2 1 ATOM 2808 C CE1 . TYR B 2 34 ? -25.156 35.604 6.430 1.00 62.68 ? 34 TYR B CE1 1 ATOM 2809 C CE2 . TYR B 2 34 ? -27.318 34.673 6.861 1.00 59.27 ? 34 TYR B CE2 1 ATOM 2810 C CZ . TYR B 2 34 ? -25.982 34.513 6.542 1.00 61.29 ? 34 TYR B CZ 1 ATOM 2811 O OH . TYR B 2 34 ? -25.462 33.261 6.332 1.00 62.82 ? 34 TYR B OH 1 ATOM 2812 N N . ALA B 2 35 ? -29.764 40.695 6.412 1.00 59.10 ? 35 ALA B N 1 ATOM 2813 C CA . ALA B 2 35 ? -30.328 41.949 6.881 1.00 59.93 ? 35 ALA B CA 1 ATOM 2814 C C . ALA B 2 35 ? -31.398 41.622 7.913 1.00 59.56 ? 35 ALA B C 1 ATOM 2815 O O . ALA B 2 35 ? -32.367 40.932 7.616 1.00 58.64 ? 35 ALA B O 1 ATOM 2816 C CB . ALA B 2 35 ? -30.924 42.727 5.730 1.00 60.03 ? 35 ALA B CB 1 ATOM 2817 N N . ALA B 2 36 ? -31.202 42.095 9.134 1.00 61.20 ? 36 ALA B N 1 ATOM 2818 C CA . ALA B 2 36 ? -32.197 41.935 10.176 1.00 60.50 ? 36 ALA B CA 1 ATOM 2819 C C . ALA B 2 36 ? -33.452 42.734 9.826 1.00 61.82 ? 36 ALA B C 1 ATOM 2820 O O . ALA B 2 36 ? -33.360 43.783 9.195 1.00 64.66 ? 36 ALA B O 1 ATOM 2821 C CB . ALA B 2 36 ? -31.628 42.400 11.507 1.00 61.42 ? 36 ALA B CB 1 ATOM 2822 N N . ASP B 2 37 ? -34.618 42.220 10.212 1.00 61.85 ? 37 ASP B N 1 ATOM 2823 C CA . ASP B 2 37 ? -35.865 42.974 10.149 1.00 63.36 ? 37 ASP B CA 1 ATOM 2824 C C . ASP B 2 37 ? -36.036 43.726 11.471 1.00 66.65 ? 37 ASP B C 1 ATOM 2825 O O . ASP B 2 37 ? -36.332 43.121 12.500 1.00 64.85 ? 37 ASP B O 1 ATOM 2826 C CB . ASP B 2 37 ? -37.045 42.035 9.921 1.00 62.43 ? 37 ASP B CB 1 ATOM 2827 C CG . ASP B 2 37 ? -38.338 42.776 9.689 1.00 64.23 ? 37 ASP B CG 1 ATOM 2828 O OD1 . ASP B 2 37 ? -38.570 43.208 8.538 1.00 66.40 ? 37 ASP B OD1 1 ATOM 2829 O OD2 . ASP B 2 37 ? -39.121 42.925 10.651 1.00 64.06 ? 37 ASP B OD2 1 ATOM 2830 N N . LYS B 2 38 ? -35.842 45.042 11.430 1.00 72.32 ? 38 LYS B N 1 ATOM 2831 C CA . LYS B 2 38 ? -35.838 45.885 12.626 1.00 76.97 ? 38 LYS B CA 1 ATOM 2832 C C . LYS B 2 38 ? -37.184 45.880 13.351 1.00 77.73 ? 38 LYS B C 1 ATOM 2833 O O . LYS B 2 38 ? -37.228 45.726 14.571 1.00 77.85 ? 38 LYS B O 1 ATOM 2834 C CB . LYS B 2 38 ? -35.468 47.326 12.250 1.00 83.84 ? 38 LYS B CB 1 ATOM 2835 C CG . LYS B 2 38 ? -35.120 48.232 13.431 1.00 89.91 ? 38 LYS B CG 1 ATOM 2836 C CD . LYS B 2 38 ? -35.755 49.620 13.320 1.00 94.77 ? 38 LYS B CD 1 ATOM 2837 C CE . LYS B 2 38 ? -35.231 50.438 12.139 1.00 98.11 ? 38 LYS B CE 1 ATOM 2838 N NZ . LYS B 2 38 ? -33.991 51.205 12.454 1.00 100.79 ? 38 LYS B NZ 1 ATOM 2839 N N . GLU B 2 39 ? -38.269 46.047 12.596 1.00 79.79 ? 39 GLU B N 1 ATOM 2840 C CA . GLU B 2 39 ? -39.620 46.167 13.162 1.00 81.51 ? 39 GLU B CA 1 ATOM 2841 C C . GLU B 2 39 ? -40.043 44.948 13.974 1.00 75.22 ? 39 GLU B C 1 ATOM 2842 O O . GLU B 2 39 ? -40.466 45.081 15.120 1.00 74.82 ? 39 GLU B O 1 ATOM 2843 C CB . GLU B 2 39 ? -40.651 46.411 12.048 1.00 88.15 ? 39 GLU B CB 1 ATOM 2844 C CG . GLU B 2 39 ? -42.111 46.343 12.503 1.00 92.74 ? 39 GLU B CG 1 ATOM 2845 C CD . GLU B 2 39 ? -43.089 46.834 11.444 1.00 98.45 ? 39 GLU B CD 1 ATOM 2846 O OE1 . GLU B 2 39 ? -43.041 46.328 10.300 1.00 100.46 ? 39 GLU B OE1 1 ATOM 2847 O OE2 . GLU B 2 39 ? -43.907 47.730 11.754 1.00 104.13 ? 39 GLU B OE2 1 ATOM 2848 N N . SER B 2 40 ? -39.953 43.769 13.371 1.00 69.85 ? 40 SER B N 1 ATOM 2849 C CA . SER B 2 40 ? -40.377 42.543 14.042 1.00 66.25 ? 40 SER B CA 1 ATOM 2850 C C . SER B 2 40 ? -39.450 42.194 15.202 1.00 63.18 ? 40 SER B C 1 ATOM 2851 O O . SER B 2 40 ? -39.901 41.660 16.214 1.00 61.47 ? 40 SER B O 1 ATOM 2852 C CB . SER B 2 40 ? -40.440 41.380 13.057 1.00 64.44 ? 40 SER B CB 1 ATOM 2853 O OG . SER B 2 40 ? -39.149 41.046 12.588 1.00 65.56 ? 40 SER B OG 1 ATOM 2854 N N . THR B 2 41 ? -38.163 42.498 15.050 1.00 61.61 ? 41 THR B N 1 ATOM 2855 C CA . THR B 2 41 ? -37.178 42.256 16.103 1.00 60.29 ? 41 THR B CA 1 ATOM 2856 C C . THR B 2 41 ? -37.458 43.118 17.333 1.00 61.00 ? 41 THR B C 1 ATOM 2857 O O . THR B 2 41 ? -37.543 42.608 18.442 1.00 60.27 ? 41 THR B O 1 ATOM 2858 C CB . THR B 2 41 ? -35.740 42.519 15.602 1.00 60.55 ? 41 THR B CB 1 ATOM 2859 O OG1 . THR B 2 41 ? -35.403 41.570 14.582 1.00 58.90 ? 41 THR B OG1 1 ATOM 2860 C CG2 . THR B 2 41 ? -34.731 42.400 16.731 1.00 60.88 ? 41 THR B CG2 1 ATOM 2861 N N . GLN B 2 42 ? -37.605 44.422 17.131 1.00 63.94 ? 42 GLN B N 1 ATOM 2862 C CA . GLN B 2 42 ? -37.855 45.350 18.237 1.00 65.89 ? 42 GLN B CA 1 ATOM 2863 C C . GLN B 2 42 ? -39.171 45.042 18.942 1.00 64.84 ? 42 GLN B C 1 ATOM 2864 O O . GLN B 2 42 ? -39.287 45.199 20.158 1.00 65.15 ? 42 GLN B O 1 ATOM 2865 C CB . GLN B 2 42 ? -37.874 46.795 17.731 1.00 68.79 ? 42 GLN B CB 1 ATOM 2866 C CG . GLN B 2 42 ? -37.991 47.841 18.828 1.00 72.25 ? 42 GLN B CG 1 ATOM 2867 C CD . GLN B 2 42 ? -36.867 47.758 19.848 1.00 73.96 ? 42 GLN B CD 1 ATOM 2868 O OE1 . GLN B 2 42 ? -37.111 47.687 21.053 1.00 74.78 ? 42 GLN B OE1 1 ATOM 2869 N NE2 . GLN B 2 42 ? -35.627 47.764 19.367 1.00 74.79 ? 42 GLN B NE2 1 ATOM 2870 N N . LYS B 2 43 ? -40.158 44.616 18.165 1.00 63.48 ? 43 LYS B N 1 ATOM 2871 C CA . LYS B 2 43 ? -41.445 44.210 18.700 1.00 64.81 ? 43 LYS B CA 1 ATOM 2872 C C . LYS B 2 43 ? -41.284 43.005 19.626 1.00 61.05 ? 43 LYS B C 1 ATOM 2873 O O . LYS B 2 43 ? -41.920 42.926 20.681 1.00 61.32 ? 43 LYS B O 1 ATOM 2874 C CB . LYS B 2 43 ? -42.398 43.868 17.553 1.00 68.56 ? 43 LYS B CB 1 ATOM 2875 C CG . LYS B 2 43 ? -43.868 43.992 17.904 1.00 74.12 ? 43 LYS B CG 1 ATOM 2876 C CD . LYS B 2 43 ? -44.693 44.414 16.692 1.00 79.34 ? 43 LYS B CD 1 ATOM 2877 C CE . LYS B 2 43 ? -46.100 44.815 17.109 1.00 83.16 ? 43 LYS B CE 1 ATOM 2878 N NZ . LYS B 2 43 ? -47.015 44.882 15.939 1.00 86.36 ? 43 LYS B NZ 1 ATOM 2879 N N . ALA B 2 44 ? -40.423 42.075 19.223 1.00 56.81 ? 44 ALA B N 1 ATOM 2880 C CA . ALA B 2 44 ? -40.124 40.905 20.026 1.00 53.68 ? 44 ALA B CA 1 ATOM 2881 C C . ALA B 2 44 ? -39.346 41.275 21.279 1.00 54.41 ? 44 ALA B C 1 ATOM 2882 O O . ALA B 2 44 ? -39.543 40.676 22.330 1.00 54.46 ? 44 ALA B O 1 ATOM 2883 C CB . ALA B 2 44 ? -39.344 39.897 19.206 1.00 52.49 ? 44 ALA B CB 1 ATOM 2884 N N . ILE B 2 45 ? -38.460 42.257 21.171 1.00 56.01 ? 45 ILE B N 1 ATOM 2885 C CA . ILE B 2 45 ? -37.678 42.703 22.321 1.00 57.92 ? 45 ILE B CA 1 ATOM 2886 C C . ILE B 2 45 ? -38.573 43.335 23.383 1.00 59.08 ? 45 ILE B C 1 ATOM 2887 O O . ILE B 2 45 ? -38.374 43.113 24.575 1.00 59.08 ? 45 ILE B O 1 ATOM 2888 C CB . ILE B 2 45 ? -36.558 43.676 21.896 1.00 60.32 ? 45 ILE B CB 1 ATOM 2889 C CG1 . ILE B 2 45 ? -35.419 42.889 21.247 1.00 59.55 ? 45 ILE B CG1 1 ATOM 2890 C CG2 . ILE B 2 45 ? -36.028 44.467 23.087 1.00 62.47 ? 45 ILE B CG2 1 ATOM 2891 C CD1 . ILE B 2 45 ? -34.370 43.752 20.580 1.00 62.45 ? 45 ILE B CD1 1 ATOM 2892 N N . ASP B 2 46 ? -39.555 44.116 22.946 1.00 60.95 ? 46 ASP B N 1 ATOM 2893 C CA . ASP B 2 46 ? -40.493 44.752 23.868 1.00 62.75 ? 46 ASP B CA 1 ATOM 2894 C C . ASP B 2 46 ? -41.328 43.699 24.581 1.00 59.66 ? 46 ASP B C 1 ATOM 2895 O O . ASP B 2 46 ? -41.481 43.749 25.799 1.00 61.64 ? 46 ASP B O 1 ATOM 2896 C CB . ASP B 2 46 ? -41.410 45.732 23.130 1.00 65.64 ? 46 ASP B CB 1 ATOM 2897 C CG . ASP B 2 46 ? -40.648 46.879 22.479 1.00 69.63 ? 46 ASP B CG 1 ATOM 2898 O OD1 . ASP B 2 46 ? -39.478 47.116 22.851 1.00 71.77 ? 46 ASP B OD1 1 ATOM 2899 O OD2 . ASP B 2 46 ? -41.221 47.547 21.591 1.00 72.37 ? 46 ASP B OD2 1 ATOM 2900 N N . GLY B 2 47 ? -41.852 42.743 23.823 1.00 56.12 ? 47 GLY B N 1 ATOM 2901 C CA . GLY B 2 47 ? -42.673 41.678 24.389 1.00 54.53 ? 47 GLY B CA 1 ATOM 2902 C C . GLY B 2 47 ? -41.969 40.928 25.507 1.00 54.47 ? 47 GLY B C 1 ATOM 2903 O O . GLY B 2 47 ? -42.517 40.751 26.599 1.00 55.29 ? 47 GLY B O 1 ATOM 2904 N N . VAL B 2 48 ? -40.738 40.510 25.237 1.00 53.09 ? 48 VAL B N 1 ATOM 2905 C CA . VAL B 2 48 ? -39.950 39.739 26.190 1.00 51.69 ? 48 VAL B CA 1 ATOM 2906 C C . VAL B 2 48 ? -39.527 40.591 27.393 1.00 52.88 ? 48 VAL B C 1 ATOM 2907 O O . VAL B 2 48 ? -39.599 40.143 28.535 1.00 52.17 ? 48 VAL B O 1 ATOM 2908 C CB . VAL B 2 48 ? -38.726 39.119 25.487 1.00 51.83 ? 48 VAL B CB 1 ATOM 2909 C CG1 . VAL B 2 48 ? -37.754 38.514 26.490 1.00 52.29 ? 48 VAL B CG1 1 ATOM 2910 C CG2 . VAL B 2 48 ? -39.186 38.068 24.479 1.00 49.68 ? 48 VAL B CG2 1 ATOM 2911 N N . THR B 2 49 ? -39.099 41.821 27.136 1.00 54.09 ? 49 THR B N 1 ATOM 2912 C CA . THR B 2 49 ? -38.743 42.745 28.209 1.00 56.36 ? 49 THR B CA 1 ATOM 2913 C C . THR B 2 49 ? -39.904 42.963 29.175 1.00 57.40 ? 49 THR B C 1 ATOM 2914 O O . THR B 2 49 ? -39.713 42.961 30.387 1.00 58.03 ? 49 THR B O 1 ATOM 2915 C CB . THR B 2 49 ? -38.311 44.100 27.640 1.00 58.51 ? 49 THR B CB 1 ATOM 2916 O OG1 . THR B 2 49 ? -37.161 43.916 26.812 1.00 57.97 ? 49 THR B OG1 1 ATOM 2917 C CG2 . THR B 2 49 ? -37.976 45.084 28.750 1.00 61.49 ? 49 THR B CG2 1 ATOM 2918 N N . ASN B 2 50 ? -41.103 43.156 28.637 1.00 58.65 ? 50 ASN B N 1 ATOM 2919 C CA . ASN B 2 50 ? -42.292 43.331 29.473 1.00 60.27 ? 50 ASN B CA 1 ATOM 2920 C C . ASN B 2 50 ? -42.623 42.061 30.238 1.00 58.83 ? 50 ASN B C 1 ATOM 2921 O O . ASN B 2 50 ? -43.018 42.116 31.400 1.00 59.80 ? 50 ASN B O 1 ATOM 2922 C CB . ASN B 2 50 ? -43.498 43.740 28.632 1.00 60.94 ? 50 ASN B CB 1 ATOM 2923 C CG . ASN B 2 50 ? -43.366 45.136 28.050 1.00 64.69 ? 50 ASN B CG 1 ATOM 2924 O OD1 . ASN B 2 50 ? -42.589 45.959 28.532 1.00 68.09 ? 50 ASN B OD1 1 ATOM 2925 N ND2 . ASN B 2 50 ? -44.135 45.411 27.004 1.00 65.61 ? 50 ASN B ND2 1 ATOM 2926 N N . LYS B 2 51 ? -42.459 40.919 29.577 1.00 57.28 ? 51 LYS B N 1 ATOM 2927 C CA . LYS B 2 51 ? -42.702 39.623 30.200 1.00 55.24 ? 51 LYS B CA 1 ATOM 2928 C C . LYS B 2 51 ? -41.862 39.476 31.453 1.00 56.14 ? 51 LYS B C 1 ATOM 2929 O O . LYS B 2 51 ? -42.372 39.130 32.514 1.00 57.75 ? 51 LYS B O 1 ATOM 2930 C CB . LYS B 2 51 ? -42.360 38.497 29.227 1.00 52.91 ? 51 LYS B CB 1 ATOM 2931 C CG . LYS B 2 51 ? -42.539 37.094 29.783 1.00 51.81 ? 51 LYS B CG 1 ATOM 2932 C CD . LYS B 2 51 ? -42.055 36.048 28.793 1.00 51.07 ? 51 LYS B CD 1 ATOM 2933 C CE . LYS B 2 51 ? -43.022 35.865 27.637 1.00 49.91 ? 51 LYS B CE 1 ATOM 2934 N NZ . LYS B 2 51 ? -43.742 34.574 27.740 1.00 49.82 ? 51 LYS B NZ 1 ATOM 2935 N N . VAL B 2 52 ? -40.573 39.753 31.319 1.00 56.71 ? 52 VAL B N 1 ATOM 2936 C CA . VAL B 2 52 ? -39.641 39.579 32.418 1.00 57.32 ? 52 VAL B CA 1 ATOM 2937 C C . VAL B 2 52 ? -40.001 40.510 33.571 1.00 59.51 ? 52 VAL B C 1 ATOM 2938 O O . VAL B 2 52 ? -40.076 40.073 34.719 1.00 59.78 ? 52 VAL B O 1 ATOM 2939 C CB . VAL B 2 52 ? -38.193 39.814 31.961 1.00 58.28 ? 52 VAL B CB 1 ATOM 2940 C CG1 . VAL B 2 52 ? -37.242 39.813 33.152 1.00 60.73 ? 52 VAL B CG1 1 ATOM 2941 C CG2 . VAL B 2 52 ? -37.787 38.746 30.958 1.00 56.51 ? 52 VAL B CG2 1 ATOM 2942 N N . ASN B 2 53 ? -40.241 41.781 33.263 1.00 61.42 ? 53 ASN B N 1 ATOM 2943 C CA . ASN B 2 53 ? -40.647 42.749 34.286 1.00 64.92 ? 53 ASN B CA 1 ATOM 2944 C C . ASN B 2 53 ? -41.991 42.388 34.923 1.00 65.23 ? 53 ASN B C 1 ATOM 2945 O O . ASN B 2 53 ? -42.219 42.678 36.098 1.00 67.43 ? 53 ASN B O 1 ATOM 2946 C CB . ASN B 2 53 ? -40.725 44.167 33.714 1.00 66.94 ? 53 ASN B CB 1 ATOM 2947 C CG . ASN B 2 53 ? -39.429 44.612 33.069 1.00 68.35 ? 53 ASN B CG 1 ATOM 2948 O OD1 . ASN B 2 53 ? -38.371 44.035 33.310 1.00 68.42 ? 53 ASN B OD1 1 ATOM 2949 N ND2 . ASN B 2 53 ? -39.511 45.635 32.225 1.00 70.53 ? 53 ASN B ND2 1 ATOM 2950 N N . SER B 2 54 ? -42.875 41.764 34.149 1.00 63.92 ? 54 SER B N 1 ATOM 2951 C CA . SER B 2 54 ? -44.177 41.351 34.662 1.00 64.93 ? 54 SER B CA 1 ATOM 2952 C C . SER B 2 54 ? -44.017 40.189 35.628 1.00 65.21 ? 54 SER B C 1 ATOM 2953 O O . SER B 2 54 ? -44.674 40.146 36.668 1.00 67.24 ? 54 SER B O 1 ATOM 2954 C CB . SER B 2 54 ? -45.113 40.955 33.520 1.00 63.58 ? 54 SER B CB 1 ATOM 2955 O OG . SER B 2 54 ? -45.387 42.067 32.691 1.00 65.21 ? 54 SER B OG 1 ATOM 2956 N N . ILE B 2 55 ? -43.139 39.255 35.270 1.00 64.34 ? 55 ILE B N 1 ATOM 2957 C CA . ILE B 2 55 ? -42.797 38.130 36.130 1.00 64.69 ? 55 ILE B CA 1 ATOM 2958 C C . ILE B 2 55 ? -42.151 38.619 37.425 1.00 67.04 ? 55 ILE B C 1 ATOM 2959 O O . ILE B 2 55 ? -42.602 38.276 38.511 1.00 66.95 ? 55 ILE B O 1 ATOM 2960 C CB . ILE B 2 55 ? -41.861 37.140 35.404 1.00 65.24 ? 55 ILE B CB 1 ATOM 2961 C CG1 . ILE B 2 55 ? -42.673 36.317 34.401 1.00 64.40 ? 55 ILE B CG1 1 ATOM 2962 C CG2 . ILE B 2 55 ? -41.154 36.214 36.390 1.00 66.58 ? 55 ILE B CG2 1 ATOM 2963 C CD1 . ILE B 2 55 ? -41.842 35.457 33.475 1.00 63.35 ? 55 ILE B CD1 1 ATOM 2964 N N . ILE B 2 56 ? -41.103 39.424 37.303 1.00 69.35 ? 56 ILE B N 1 ATOM 2965 C CA . ILE B 2 56 ? -40.432 39.988 38.470 1.00 73.22 ? 56 ILE B CA 1 ATOM 2966 C C . ILE B 2 56 ? -41.428 40.717 39.382 1.00 77.15 ? 56 ILE B C 1 ATOM 2967 O O . ILE B 2 56 ? -41.397 40.552 40.604 1.00 77.05 ? 56 ILE B O 1 ATOM 2968 C CB . ILE B 2 56 ? -39.300 40.948 38.047 1.00 74.91 ? 56 ILE B CB 1 ATOM 2969 C CG1 . ILE B 2 56 ? -38.149 40.156 37.418 1.00 74.12 ? 56 ILE B CG1 1 ATOM 2970 C CG2 . ILE B 2 56 ? -38.787 41.751 39.238 1.00 77.91 ? 56 ILE B CG2 1 ATOM 2971 C CD1 . ILE B 2 56 ? -37.174 41.002 36.630 1.00 75.82 ? 56 ILE B CD1 1 ATOM 2972 N N . ASP B 2 57 ? -42.316 41.506 38.782 1.00 80.60 ? 57 ASP B N 1 ATOM 2973 C CA . ASP B 2 57 ? -43.269 42.310 39.546 1.00 84.63 ? 57 ASP B CA 1 ATOM 2974 C C . ASP B 2 57 ? -44.321 41.465 40.272 1.00 81.81 ? 57 ASP B C 1 ATOM 2975 O O . ASP B 2 57 ? -44.616 41.719 41.431 1.00 80.44 ? 57 ASP B O 1 ATOM 2976 C CB . ASP B 2 57 ? -43.964 43.326 38.636 1.00 88.58 ? 57 ASP B CB 1 ATOM 2977 C CG . ASP B 2 57 ? -44.825 44.304 39.410 1.00 94.36 ? 57 ASP B CG 1 ATOM 2978 O OD1 . ASP B 2 57 ? -44.266 45.062 40.233 1.00 100.40 ? 57 ASP B OD1 1 ATOM 2979 O OD2 . ASP B 2 57 ? -46.059 44.313 39.199 1.00 95.68 ? 57 ASP B OD2 1 ATOM 2980 N N . LYS B 2 58 ? -44.891 40.473 39.593 1.00 79.65 ? 58 LYS B N 1 ATOM 2981 C CA . LYS B 2 58 ? -45.895 39.609 40.216 1.00 78.56 ? 58 LYS B CA 1 ATOM 2982 C C . LYS B 2 58 ? -45.340 38.888 41.436 1.00 81.79 ? 58 LYS B C 1 ATOM 2983 O O . LYS B 2 58 ? -46.061 38.666 42.407 1.00 84.09 ? 58 LYS B O 1 ATOM 2984 C CB . LYS B 2 58 ? -46.428 38.573 39.225 1.00 75.63 ? 58 LYS B CB 1 ATOM 2985 C CG . LYS B 2 58 ? -47.413 39.101 38.193 1.00 75.34 ? 58 LYS B CG 1 ATOM 2986 C CD . LYS B 2 58 ? -48.650 39.749 38.811 1.00 75.44 ? 58 LYS B CD 1 ATOM 2987 C CE . LYS B 2 58 ? -48.579 41.272 38.789 1.00 76.43 ? 58 LYS B CE 1 ATOM 2988 N NZ . LYS B 2 58 ? -49.914 41.905 38.960 1.00 76.70 ? 58 LYS B NZ 1 ATOM 2989 N N . MET B 2 59 ? -44.058 38.533 41.382 1.00 84.17 ? 59 MET B N 1 ATOM 2990 C CA . MET B 2 59 ? -43.392 37.809 42.467 1.00 86.45 ? 59 MET B CA 1 ATOM 2991 C C . MET B 2 59 ? -42.842 38.748 43.550 1.00 92.32 ? 59 MET B C 1 ATOM 2992 O O . MET B 2 59 ? -42.269 38.289 44.537 1.00 93.07 ? 59 MET B O 1 ATOM 2993 C CB . MET B 2 59 ? -42.252 36.967 41.898 1.00 85.00 ? 59 MET B CB 1 ATOM 2994 C CG . MET B 2 59 ? -42.671 35.983 40.812 1.00 82.17 ? 59 MET B CG 1 ATOM 2995 S SD . MET B 2 59 ? -43.684 34.587 41.338 1.00 81.38 ? 59 MET B SD 1 ATOM 2996 C CE . MET B 2 59 ? -43.027 34.166 42.948 1.00 84.30 ? 59 MET B CE 1 ATOM 2997 N N . ASN B 2 60 ? -43.016 40.054 43.351 1.00 97.79 ? 60 ASN B N 1 ATOM 2998 C CA . ASN B 2 60 ? -42.604 41.092 44.305 1.00 100.75 ? 60 ASN B CA 1 ATOM 2999 C C . ASN B 2 60 ? -43.264 40.942 45.677 1.00 100.33 ? 60 ASN B C 1 ATOM 3000 O O . ASN B 2 60 ? -42.616 41.116 46.708 1.00 100.69 ? 60 ASN B O 1 ATOM 3001 C CB . ASN B 2 60 ? -42.931 42.472 43.718 1.00 102.82 ? 60 ASN B CB 1 ATOM 3002 C CG . ASN B 2 60 ? -42.461 43.613 44.590 1.00 107.19 ? 60 ASN B CG 1 ATOM 3003 O OD1 . ASN B 2 60 ? -43.183 44.063 45.476 1.00 108.21 ? 60 ASN B OD1 1 ATOM 3004 N ND2 . ASN B 2 60 ? -41.259 44.109 44.322 1.00 110.15 ? 60 ASN B ND2 1 ATOM 3005 N N . THR B 2 61 ? -44.559 40.643 45.679 1.00 96.29 ? 61 THR B N 1 ATOM 3006 C CA . THR B 2 61 ? -45.290 40.374 46.911 1.00 95.92 ? 61 THR B CA 1 ATOM 3007 C C . THR B 2 61 ? -45.293 38.868 47.122 1.00 92.29 ? 61 THR B C 1 ATOM 3008 O O . THR B 2 61 ? -45.880 38.131 46.334 1.00 95.19 ? 61 THR B O 1 ATOM 3009 C CB . THR B 2 61 ? -46.744 40.882 46.845 1.00 98.73 ? 61 THR B CB 1 ATOM 3010 O OG1 . THR B 2 61 ? -46.800 42.106 46.100 1.00 101.53 ? 61 THR B OG1 1 ATOM 3011 C CG2 . THR B 2 61 ? -47.289 41.115 48.248 1.00 100.56 ? 61 THR B CG2 1 ATOM 3012 N N . GLN B 2 62 ? -44.627 38.420 48.179 1.00 89.62 ? 62 GLN B N 1 ATOM 3013 C CA . GLN B 2 62 ? -44.428 36.995 48.427 1.00 87.60 ? 62 GLN B CA 1 ATOM 3014 C C . GLN B 2 62 ? -44.027 36.757 49.885 1.00 85.50 ? 62 GLN B C 1 ATOM 3015 O O . GLN B 2 62 ? -43.379 37.608 50.502 1.00 89.01 ? 62 GLN B O 1 ATOM 3016 C CB . GLN B 2 62 ? -43.366 36.448 47.465 1.00 88.14 ? 62 GLN B CB 1 ATOM 3017 C CG . GLN B 2 62 ? -42.624 35.209 47.949 1.00 88.56 ? 62 GLN B CG 1 ATOM 3018 C CD . GLN B 2 62 ? -41.731 34.605 46.886 1.00 91.25 ? 62 GLN B CD 1 ATOM 3019 O OE1 . GLN B 2 62 ? -41.764 35.010 45.723 1.00 94.19 ? 62 GLN B OE1 1 ATOM 3020 N NE2 . GLN B 2 62 ? -40.924 33.627 47.281 1.00 93.00 ? 62 GLN B NE2 1 ATOM 3021 N N . PHE B 2 63 ? -44.403 35.594 50.417 1.00 79.38 ? 63 PHE B N 1 ATOM 3022 C CA . PHE B 2 63 ? -44.214 35.290 51.833 1.00 77.09 ? 63 PHE B CA 1 ATOM 3023 C C . PHE B 2 63 ? -42.763 35.441 52.299 1.00 79.96 ? 63 PHE B C 1 ATOM 3024 O O . PHE B 2 63 ? -41.826 34.936 51.668 1.00 81.32 ? 63 PHE B O 1 ATOM 3025 C CB . PHE B 2 63 ? -44.706 33.880 52.160 1.00 72.69 ? 63 PHE B CB 1 ATOM 3026 C CG . PHE B 2 63 ? -44.665 33.556 53.624 1.00 69.98 ? 63 PHE B CG 1 ATOM 3027 C CD1 . PHE B 2 63 ? -45.696 33.953 54.468 1.00 68.30 ? 63 PHE B CD1 1 ATOM 3028 C CD2 . PHE B 2 63 ? -43.587 32.865 54.166 1.00 69.28 ? 63 PHE B CD2 1 ATOM 3029 C CE1 . PHE B 2 63 ? -45.653 33.660 55.820 1.00 66.35 ? 63 PHE B CE1 1 ATOM 3030 C CE2 . PHE B 2 63 ? -43.541 32.571 55.517 1.00 66.96 ? 63 PHE B CE2 1 ATOM 3031 C CZ . PHE B 2 63 ? -44.573 32.969 56.343 1.00 65.19 ? 63 PHE B CZ 1 ATOM 3032 N N . GLU B 2 64 ? -42.603 36.153 53.412 1.00 80.73 ? 64 GLU B N 1 ATOM 3033 C CA . GLU B 2 64 ? -41.318 36.324 54.060 1.00 83.16 ? 64 GLU B CA 1 ATOM 3034 C C . GLU B 2 64 ? -41.377 35.695 55.446 1.00 81.53 ? 64 GLU B C 1 ATOM 3035 O O . GLU B 2 64 ? -42.277 35.988 56.237 1.00 80.76 ? 64 GLU B O 1 ATOM 3036 C CB . GLU B 2 64 ? -40.983 37.804 54.174 1.00 87.92 ? 64 GLU B CB 1 ATOM 3037 C CG . GLU B 2 64 ? -40.801 38.487 52.830 1.00 91.39 ? 64 GLU B CG 1 ATOM 3038 C CD . GLU B 2 64 ? -40.545 39.974 52.961 1.00 96.41 ? 64 GLU B CD 1 ATOM 3039 O OE1 . GLU B 2 64 ? -40.238 40.438 54.080 1.00 99.28 ? 64 GLU B OE1 1 ATOM 3040 O OE2 . GLU B 2 64 ? -40.652 40.680 51.939 1.00 100.28 ? 64 GLU B OE2 1 ATOM 3041 N N . ALA B 2 65 ? -40.415 34.824 55.730 1.00 80.40 ? 65 ALA B N 1 ATOM 3042 C CA . ALA B 2 65 ? -40.352 34.148 57.011 1.00 77.72 ? 65 ALA B CA 1 ATOM 3043 C C . ALA B 2 65 ? -39.886 35.117 58.094 1.00 78.56 ? 65 ALA B C 1 ATOM 3044 O O . ALA B 2 65 ? -39.080 36.012 57.836 1.00 77.99 ? 65 ALA B O 1 ATOM 3045 C CB . ALA B 2 65 ? -39.421 32.946 56.930 1.00 78.52 ? 65 ALA B CB 1 ATOM 3046 N N . VAL B 2 66 ? -40.420 34.933 59.297 1.00 77.68 ? 66 VAL B N 1 ATOM 3047 C CA . VAL B 2 66 ? -40.028 35.707 60.465 1.00 79.55 ? 66 VAL B CA 1 ATOM 3048 C C . VAL B 2 66 ? -39.613 34.722 61.547 1.00 79.13 ? 66 VAL B C 1 ATOM 3049 O O . VAL B 2 66 ? -40.245 33.673 61.715 1.00 77.72 ? 66 VAL B O 1 ATOM 3050 C CB . VAL B 2 66 ? -41.190 36.582 60.974 1.00 80.31 ? 66 VAL B CB 1 ATOM 3051 C CG1 . VAL B 2 66 ? -40.757 37.420 62.171 1.00 83.41 ? 66 VAL B CG1 1 ATOM 3052 C CG2 . VAL B 2 66 ? -41.708 37.473 59.851 1.00 81.72 ? 66 VAL B CG2 1 ATOM 3053 N N . GLY B 2 67 ? -38.547 35.057 62.269 1.00 80.87 ? 67 GLY B N 1 ATOM 3054 C CA . GLY B 2 67 ? -38.060 34.222 63.361 1.00 80.87 ? 67 GLY B CA 1 ATOM 3055 C C . GLY B 2 67 ? -39.001 34.240 64.555 1.00 78.88 ? 67 GLY B C 1 ATOM 3056 O O . GLY B 2 67 ? -39.382 35.305 65.042 1.00 81.81 ? 67 GLY B O 1 ATOM 3057 N N . ARG B 2 68 ? -39.393 33.057 65.014 1.00 74.85 ? 68 ARG B N 1 ATOM 3058 C CA . ARG B 2 68 ? -40.208 32.920 66.216 1.00 71.61 ? 68 ARG B CA 1 ATOM 3059 C C . ARG B 2 68 ? -39.682 31.759 67.032 1.00 69.09 ? 68 ARG B C 1 ATOM 3060 O O . ARG B 2 68 ? -39.374 30.702 66.484 1.00 67.72 ? 68 ARG B O 1 ATOM 3061 C CB . ARG B 2 68 ? -41.675 32.667 65.863 1.00 70.30 ? 68 ARG B CB 1 ATOM 3062 C CG . ARG B 2 68 ? -42.384 33.854 65.239 1.00 70.65 ? 68 ARG B CG 1 ATOM 3063 C CD . ARG B 2 68 ? -43.871 33.588 65.065 1.00 68.86 ? 68 ARG B CD 1 ATOM 3064 N NE . ARG B 2 68 ? -44.419 34.392 63.980 1.00 69.83 ? 68 ARG B NE 1 ATOM 3065 C CZ . ARG B 2 68 ? -44.279 34.106 62.686 1.00 70.47 ? 68 ARG B CZ 1 ATOM 3066 N NH1 . ARG B 2 68 ? -43.623 33.017 62.292 1.00 68.94 ? 68 ARG B NH1 1 ATOM 3067 N NH2 . ARG B 2 68 ? -44.799 34.918 61.773 1.00 73.68 ? 68 ARG B NH2 1 ATOM 3068 N N . GLU B 2 69 ? -39.586 31.959 68.342 1.00 69.83 ? 69 GLU B N 1 ATOM 3069 C CA . GLU B 2 69 ? -39.072 30.939 69.243 1.00 68.54 ? 69 GLU B CA 1 ATOM 3070 C C . GLU B 2 69 ? -40.158 30.486 70.194 1.00 64.18 ? 69 GLU B C 1 ATOM 3071 O O . GLU B 2 69 ? -41.102 31.222 70.462 1.00 63.68 ? 69 GLU B O 1 ATOM 3072 C CB . GLU B 2 69 ? -37.866 31.471 70.005 1.00 73.14 ? 69 GLU B CB 1 ATOM 3073 C CG . GLU B 2 69 ? -36.716 31.835 69.078 1.00 76.70 ? 69 GLU B CG 1 ATOM 3074 C CD . GLU B 2 69 ? -35.382 31.944 69.789 1.00 82.28 ? 69 GLU B CD 1 ATOM 3075 O OE1 . GLU B 2 69 ? -35.118 31.127 70.698 1.00 82.33 ? 69 GLU B OE1 1 ATOM 3076 O OE2 . GLU B 2 69 ? -34.588 32.839 69.426 1.00 87.52 ? 69 GLU B OE2 1 ATOM 3077 N N . PHE B 2 70 ? -40.022 29.256 70.677 1.00 62.40 ? 70 PHE B N 1 ATOM 3078 C CA . PHE B 2 70 ? -41.015 28.639 71.544 1.00 59.51 ? 70 PHE B CA 1 ATOM 3079 C C . PHE B 2 70 ? -40.315 27.775 72.584 1.00 60.55 ? 70 PHE B C 1 ATOM 3080 O O . PHE B 2 70 ? -39.296 27.161 72.286 1.00 61.61 ? 70 PHE B O 1 ATOM 3081 C CB . PHE B 2 70 ? -41.969 27.783 70.711 1.00 57.24 ? 70 PHE B CB 1 ATOM 3082 C CG . PHE B 2 70 ? -42.597 28.517 69.558 1.00 56.36 ? 70 PHE B CG 1 ATOM 3083 C CD1 . PHE B 2 70 ? -41.946 28.598 68.326 1.00 57.10 ? 70 PHE B CD1 1 ATOM 3084 C CD2 . PHE B 2 70 ? -43.837 29.128 69.699 1.00 55.17 ? 70 PHE B CD2 1 ATOM 3085 C CE1 . PHE B 2 70 ? -42.521 29.276 67.260 1.00 55.74 ? 70 PHE B CE1 1 ATOM 3086 C CE2 . PHE B 2 70 ? -44.420 29.806 68.638 1.00 54.96 ? 70 PHE B CE2 1 ATOM 3087 C CZ . PHE B 2 70 ? -43.760 29.880 67.415 1.00 55.38 ? 70 PHE B CZ 1 ATOM 3088 N N . ASN B 2 71 ? -40.850 27.726 73.802 1.00 60.97 ? 71 ASN B N 1 ATOM 3089 C CA . ASN B 2 71 ? -40.220 26.942 74.868 1.00 62.56 ? 71 ASN B CA 1 ATOM 3090 C C . ASN B 2 71 ? -40.516 25.453 74.703 1.00 62.22 ? 71 ASN B C 1 ATOM 3091 O O . ASN B 2 71 ? -41.222 25.050 73.772 1.00 58.56 ? 71 ASN B O 1 ATOM 3092 C CB . ASN B 2 71 ? -40.606 27.460 76.270 1.00 62.86 ? 71 ASN B CB 1 ATOM 3093 C CG . ASN B 2 71 ? -42.009 27.051 76.704 1.00 60.37 ? 71 ASN B CG 1 ATOM 3094 O OD1 . ASN B 2 71 ? -42.374 25.876 76.670 1.00 58.73 ? 71 ASN B OD1 1 ATOM 3095 N ND2 . ASN B 2 71 ? -42.793 28.025 77.148 1.00 60.84 ? 71 ASN B ND2 1 ATOM 3096 N N . ASN B 2 72 ? -39.988 24.650 75.625 1.00 64.09 ? 72 ASN B N 1 ATOM 3097 C CA . ASN B 2 72 ? -40.057 23.195 75.525 1.00 64.62 ? 72 ASN B CA 1 ATOM 3098 C C . ASN B 2 72 ? -41.468 22.586 75.629 1.00 61.47 ? 72 ASN B C 1 ATOM 3099 O O . ASN B 2 72 ? -41.673 21.440 75.220 1.00 61.43 ? 72 ASN B O 1 ATOM 3100 C CB . ASN B 2 72 ? -39.147 22.576 76.587 1.00 69.11 ? 72 ASN B CB 1 ATOM 3101 C CG . ASN B 2 72 ? -38.854 21.116 76.325 1.00 72.08 ? 72 ASN B CG 1 ATOM 3102 O OD1 . ASN B 2 72 ? -38.399 20.748 75.241 1.00 74.71 ? 72 ASN B OD1 1 ATOM 3103 N ND2 . ASN B 2 72 ? -39.104 20.274 77.323 1.00 73.30 ? 72 ASN B ND2 1 ATOM 3104 N N . LEU B 2 73 ? -42.425 23.334 76.183 1.00 58.87 ? 73 LEU B N 1 ATOM 3105 C CA . LEU B 2 73 ? -43.824 22.886 76.257 1.00 57.66 ? 73 LEU B CA 1 ATOM 3106 C C . LEU B 2 73 ? -44.744 23.700 75.337 1.00 55.60 ? 73 LEU B C 1 ATOM 3107 O O . LEU B 2 73 ? -45.929 23.893 75.623 1.00 54.17 ? 73 LEU B O 1 ATOM 3108 C CB . LEU B 2 73 ? -44.324 22.937 77.704 1.00 59.41 ? 73 LEU B CB 1 ATOM 3109 C CG . LEU B 2 73 ? -43.649 21.967 78.689 1.00 61.35 ? 73 LEU B CG 1 ATOM 3110 C CD1 . LEU B 2 73 ? -44.073 22.283 80.114 1.00 61.14 ? 73 LEU B CD1 1 ATOM 3111 C CD2 . LEU B 2 73 ? -43.951 20.511 78.344 1.00 61.84 ? 73 LEU B CD2 1 ATOM 3112 N N . GLU B 2 74 ? -44.185 24.162 74.222 1.00 54.52 ? 74 GLU B N 1 ATOM 3113 C CA . GLU B 2 74 ? -44.955 24.812 73.174 1.00 53.40 ? 74 GLU B CA 1 ATOM 3114 C C . GLU B 2 74 ? -44.661 24.139 71.848 1.00 54.30 ? 74 GLU B C 1 ATOM 3115 O O . GLU B 2 74 ? -44.563 24.800 70.817 1.00 52.76 ? 74 GLU B O 1 ATOM 3116 C CB . GLU B 2 74 ? -44.589 26.284 73.102 1.00 52.56 ? 74 GLU B CB 1 ATOM 3117 C CG . GLU B 2 74 ? -45.080 27.074 74.290 1.00 52.89 ? 74 GLU B CG 1 ATOM 3118 C CD . GLU B 2 74 ? -44.578 28.492 74.266 1.00 54.37 ? 74 GLU B CD 1 ATOM 3119 O OE1 . GLU B 2 74 ? -43.419 28.696 73.862 1.00 55.81 ? 74 GLU B OE1 1 ATOM 3120 O OE2 . GLU B 2 74 ? -45.336 29.402 74.654 1.00 55.27 ? 74 GLU B OE2 1 ATOM 3121 N N . ARG B 2 75 ? -44.510 22.817 71.884 1.00 57.18 ? 75 ARG B N 1 ATOM 3122 C CA . ARG B 2 75 ? -44.057 22.063 70.720 1.00 59.48 ? 75 ARG B CA 1 ATOM 3123 C C . ARG B 2 75 ? -45.081 22.059 69.591 1.00 56.62 ? 75 ARG B C 1 ATOM 3124 O O . ARG B 2 75 ? -44.717 22.036 68.423 1.00 56.07 ? 75 ARG B O 1 ATOM 3125 C CB . ARG B 2 75 ? -43.693 20.627 71.113 1.00 65.04 ? 75 ARG B CB 1 ATOM 3126 C CG . ARG B 2 75 ? -42.443 20.513 71.971 1.00 69.89 ? 75 ARG B CG 1 ATOM 3127 C CD . ARG B 2 75 ? -41.181 20.748 71.157 1.00 75.57 ? 75 ARG B CD 1 ATOM 3128 N NE . ARG B 2 75 ? -40.005 20.980 71.997 1.00 83.44 ? 75 ARG B NE 1 ATOM 3129 C CZ . ARG B 2 75 ? -38.777 21.238 71.537 1.00 89.23 ? 75 ARG B CZ 1 ATOM 3130 N NH1 . ARG B 2 75 ? -38.535 21.299 70.224 1.00 89.83 ? 75 ARG B NH1 1 ATOM 3131 N NH2 . ARG B 2 75 ? -37.780 21.436 72.398 1.00 91.67 ? 75 ARG B NH2 1 ATOM 3132 N N . ARG B 2 76 ? -46.359 22.088 69.939 1.00 55.82 ? 76 ARG B N 1 ATOM 3133 C CA . ARG B 2 76 ? -47.414 22.087 68.931 1.00 55.41 ? 76 ARG B CA 1 ATOM 3134 C C . ARG B 2 76 ? -47.407 23.373 68.099 1.00 55.13 ? 76 ARG B C 1 ATOM 3135 O O . ARG B 2 76 ? -47.395 23.309 66.868 1.00 55.21 ? 76 ARG B O 1 ATOM 3136 C CB . ARG B 2 76 ? -48.775 21.899 69.589 1.00 54.88 ? 76 ARG B CB 1 ATOM 3137 C CG . ARG B 2 76 ? -48.971 20.529 70.207 1.00 56.16 ? 76 ARG B CG 1 ATOM 3138 C CD . ARG B 2 76 ? -50.232 20.512 71.044 1.00 56.86 ? 76 ARG B CD 1 ATOM 3139 N NE . ARG B 2 76 ? -50.144 21.513 72.101 1.00 55.33 ? 76 ARG B NE 1 ATOM 3140 C CZ . ARG B 2 76 ? -51.180 22.060 72.730 1.00 54.99 ? 76 ARG B CZ 1 ATOM 3141 N NH1 . ARG B 2 76 ? -52.429 21.715 72.433 1.00 57.19 ? 76 ARG B NH1 1 ATOM 3142 N NH2 . ARG B 2 76 ? -50.960 22.972 73.665 1.00 53.08 ? 76 ARG B NH2 1 ATOM 3143 N N . ILE B 2 77 ? -47.408 24.529 68.765 1.00 54.29 ? 77 ILE B N 1 ATOM 3144 C CA . ILE B 2 77 ? -47.388 25.807 68.054 1.00 55.31 ? 77 ILE B CA 1 ATOM 3145 C C . ILE B 2 77 ? -46.043 26.062 67.361 1.00 56.01 ? 77 ILE B C 1 ATOM 3146 O O . ILE B 2 77 ? -45.991 26.772 66.356 1.00 56.00 ? 77 ILE B O 1 ATOM 3147 C CB . ILE B 2 77 ? -47.793 27.012 68.939 1.00 56.31 ? 77 ILE B CB 1 ATOM 3148 C CG1 . ILE B 2 77 ? -46.795 27.245 70.072 1.00 58.17 ? 77 ILE B CG1 1 ATOM 3149 C CG2 . ILE B 2 77 ? -49.195 26.817 69.501 1.00 58.16 ? 77 ILE B CG2 1 ATOM 3150 C CD1 . ILE B 2 77 ? -47.074 28.501 70.871 1.00 59.50 ? 77 ILE B CD1 1 ATOM 3151 N N . GLU B 2 78 ? -44.964 25.487 67.885 1.00 56.25 ? 78 GLU B N 1 ATOM 3152 C CA . GLU B 2 78 ? -43.680 25.542 67.194 1.00 58.27 ? 78 GLU B CA 1 ATOM 3153 C C . GLU B 2 78 ? -43.798 24.807 65.862 1.00 56.75 ? 78 GLU B C 1 ATOM 3154 O O . GLU B 2 78 ? -43.402 25.327 64.824 1.00 56.24 ? 78 GLU B O 1 ATOM 3155 C CB . GLU B 2 78 ? -42.570 24.913 68.036 1.00 62.62 ? 78 GLU B CB 1 ATOM 3156 C CG . GLU B 2 78 ? -41.191 24.935 67.388 1.00 67.38 ? 78 GLU B CG 1 ATOM 3157 C CD . GLU B 2 78 ? -40.101 24.423 68.315 1.00 75.12 ? 78 GLU B CD 1 ATOM 3158 O OE1 . GLU B 2 78 ? -40.329 23.403 69.007 1.00 79.67 ? 78 GLU B OE1 1 ATOM 3159 O OE2 . GLU B 2 78 ? -39.010 25.038 68.353 1.00 79.83 ? 78 GLU B OE2 1 ATOM 3160 N N . ASN B 2 79 ? -44.342 23.597 65.913 1.00 55.42 ? 79 ASN B N 1 ATOM 3161 C CA . ASN B 2 79 ? -44.538 22.774 64.734 1.00 55.88 ? 79 ASN B CA 1 ATOM 3162 C C . ASN B 2 79 ? -45.550 23.407 63.786 1.00 55.78 ? 79 ASN B C 1 ATOM 3163 O O . ASN B 2 79 ? -45.390 23.342 62.570 1.00 57.35 ? 79 ASN B O 1 ATOM 3164 C CB . ASN B 2 79 ? -45.013 21.389 65.151 1.00 58.01 ? 79 ASN B CB 1 ATOM 3165 C CG . ASN B 2 79 ? -45.089 20.420 63.993 1.00 60.41 ? 79 ASN B CG 1 ATOM 3166 O OD1 . ASN B 2 79 ? -44.080 20.095 63.375 1.00 63.21 ? 79 ASN B OD1 1 ATOM 3167 N ND2 . ASN B 2 79 ? -46.282 19.923 63.715 1.00 61.95 ? 79 ASN B ND2 1 ATOM 3168 N N . LEU B 2 80 ? -46.583 24.032 64.344 1.00 54.45 ? 80 LEU B N 1 ATOM 3169 C CA . LEU B 2 80 ? -47.573 24.737 63.534 1.00 53.43 ? 80 LEU B CA 1 ATOM 3170 C C . LEU B 2 80 ? -46.866 25.810 62.735 1.00 51.88 ? 80 LEU B C 1 ATOM 3171 O O . LEU B 2 80 ? -47.028 25.903 61.527 1.00 53.48 ? 80 LEU B O 1 ATOM 3172 C CB . LEU B 2 80 ? -48.646 25.370 64.423 1.00 53.96 ? 80 LEU B CB 1 ATOM 3173 C CG . LEU B 2 80 ? -49.934 25.856 63.749 1.00 55.92 ? 80 LEU B CG 1 ATOM 3174 C CD1 . LEU B 2 80 ? -51.014 26.122 64.785 1.00 56.90 ? 80 LEU B CD1 1 ATOM 3175 C CD2 . LEU B 2 80 ? -49.706 27.095 62.899 1.00 56.20 ? 80 LEU B CD2 1 ATOM 3176 N N . ASN B 2 81 ? -46.065 26.607 63.432 1.00 51.25 ? 81 ASN B N 1 ATOM 3177 C CA . ASN B 2 81 ? -45.290 27.685 62.834 1.00 49.80 ? 81 ASN B CA 1 ATOM 3178 C C . ASN B 2 81 ? -44.314 27.180 61.779 1.00 50.85 ? 81 ASN B C 1 ATOM 3179 O O . ASN B 2 81 ? -44.122 27.816 60.754 1.00 49.06 ? 81 ASN B O 1 ATOM 3180 C CB . ASN B 2 81 ? -44.531 28.425 63.930 1.00 49.50 ? 81 ASN B CB 1 ATOM 3181 C CG . ASN B 2 81 ? -43.726 29.590 63.405 1.00 50.31 ? 81 ASN B CG 1 ATOM 3182 O OD1 . ASN B 2 81 ? -44.279 30.543 62.850 1.00 51.30 ? 81 ASN B OD1 1 ATOM 3183 N ND2 . ASN B 2 81 ? -42.414 29.537 63.598 1.00 51.14 ? 81 ASN B ND2 1 ATOM 3184 N N . LYS B 2 82 ? -43.702 26.032 62.043 1.00 54.06 ? 82 LYS B N 1 ATOM 3185 C CA . LYS B 2 82 ? -42.752 25.436 61.118 1.00 58.09 ? 82 LYS B CA 1 ATOM 3186 C C . LYS B 2 82 ? -43.477 25.041 59.838 1.00 59.46 ? 82 LYS B C 1 ATOM 3187 O O . LYS B 2 82 ? -43.070 25.429 58.745 1.00 58.69 ? 82 LYS B O 1 ATOM 3188 C CB . LYS B 2 82 ? -42.089 24.213 61.757 1.00 62.33 ? 82 LYS B CB 1 ATOM 3189 C CG . LYS B 2 82 ? -40.951 23.581 60.961 1.00 68.43 ? 82 LYS B CG 1 ATOM 3190 C CD . LYS B 2 82 ? -40.528 22.265 61.609 1.00 74.71 ? 82 LYS B CD 1 ATOM 3191 C CE . LYS B 2 82 ? -39.361 21.603 60.887 1.00 81.31 ? 82 LYS B CE 1 ATOM 3192 N NZ . LYS B 2 82 ? -39.674 21.290 59.461 1.00 83.06 ? 82 LYS B NZ 1 ATOM 3193 N N . LYS B 2 83 ? -44.563 24.285 59.983 1.00 60.66 ? 83 LYS B N 1 ATOM 3194 C CA . LYS B 2 83 ? -45.337 23.822 58.833 1.00 62.13 ? 83 LYS B CA 1 ATOM 3195 C C . LYS B 2 83 ? -46.006 24.964 58.071 1.00 60.04 ? 83 LYS B C 1 ATOM 3196 O O . LYS B 2 83 ? -46.211 24.868 56.862 1.00 60.49 ? 83 LYS B O 1 ATOM 3197 C CB . LYS B 2 83 ? -46.373 22.776 59.256 1.00 65.03 ? 83 LYS B CB 1 ATOM 3198 C CG . LYS B 2 83 ? -45.914 21.336 59.064 1.00 70.31 ? 83 LYS B CG 1 ATOM 3199 C CD . LYS B 2 83 ? -44.525 21.072 59.640 1.00 71.82 ? 83 LYS B CD 1 ATOM 3200 C CE . LYS B 2 83 ? -44.104 19.618 59.450 1.00 76.95 ? 83 LYS B CE 1 ATOM 3201 N NZ . LYS B 2 83 ? -44.023 19.236 58.008 1.00 79.10 ? 83 LYS B NZ 1 ATOM 3202 N N . MET B 2 84 ? -46.327 26.046 58.770 1.00 57.74 ? 84 MET B N 1 ATOM 3203 C CA . MET B 2 84 ? -46.912 27.208 58.120 1.00 57.17 ? 84 MET B CA 1 ATOM 3204 C C . MET B 2 84 ? -45.886 27.907 57.225 1.00 55.87 ? 84 MET B C 1 ATOM 3205 O O . MET B 2 84 ? -46.171 28.184 56.064 1.00 57.37 ? 84 MET B O 1 ATOM 3206 C CB . MET B 2 84 ? -47.455 28.192 59.152 1.00 56.92 ? 84 MET B CB 1 ATOM 3207 C CG . MET B 2 84 ? -48.383 29.240 58.562 1.00 58.35 ? 84 MET B CG 1 ATOM 3208 S SD . MET B 2 84 ? -48.013 30.905 59.132 1.00 60.44 ? 84 MET B SD 1 ATOM 3209 C CE . MET B 2 84 ? -46.470 31.200 58.301 1.00 59.96 ? 84 MET B CE 1 ATOM 3210 N N . GLU B 2 85 ? -44.698 28.182 57.761 1.00 65.48 ? 85 GLU B N 1 ATOM 3211 C CA . GLU B 2 85 ? -43.674 28.909 57.011 1.00 65.14 ? 85 GLU B CA 1 ATOM 3212 C C . GLU B 2 85 ? -43.149 28.087 55.834 1.00 64.33 ? 85 GLU B C 1 ATOM 3213 O O . GLU B 2 85 ? -42.920 28.622 54.750 1.00 64.58 ? 85 GLU B O 1 ATOM 3214 C CB . GLU B 2 85 ? -42.531 29.369 57.928 1.00 67.14 ? 85 GLU B CB 1 ATOM 3215 C CG . GLU B 2 85 ? -42.982 30.362 59.005 1.00 68.90 ? 85 GLU B CG 1 ATOM 3216 C CD . GLU B 2 85 ? -41.976 31.466 59.303 1.00 71.25 ? 85 GLU B CD 1 ATOM 3217 O OE1 . GLU B 2 85 ? -40.829 31.154 59.695 1.00 73.83 ? 85 GLU B OE1 1 ATOM 3218 O OE2 . GLU B 2 85 ? -42.348 32.654 59.164 1.00 70.99 ? 85 GLU B OE2 1 ATOM 3219 N N . ASP B 2 86 ? -42.982 26.788 56.045 1.00 63.28 ? 86 ASP B N 1 ATOM 3220 C CA . ASP B 2 86 ? -42.619 25.872 54.965 1.00 62.07 ? 86 ASP B CA 1 ATOM 3221 C C . ASP B 2 86 ? -43.683 25.765 53.894 1.00 59.43 ? 86 ASP B C 1 ATOM 3222 O O . ASP B 2 86 ? -43.361 25.652 52.714 1.00 59.31 ? 86 ASP B O 1 ATOM 3223 C CB . ASP B 2 86 ? -42.376 24.467 55.505 1.00 64.05 ? 86 ASP B CB 1 ATOM 3224 C CG . ASP B 2 86 ? -40.942 24.204 55.768 1.00 67.08 ? 86 ASP B CG 1 ATOM 3225 O OD1 . ASP B 2 86 ? -40.148 24.349 54.805 1.00 69.90 ? 86 ASP B OD1 1 ATOM 3226 O OD2 . ASP B 2 86 ? -40.611 23.851 56.925 1.00 69.30 ? 86 ASP B OD2 1 ATOM 3227 N N . GLY B 2 87 ? -44.942 25.743 54.314 1.00 57.53 ? 87 GLY B N 1 ATOM 3228 C CA . GLY B 2 87 ? -46.054 25.620 53.388 1.00 56.78 ? 87 GLY B CA 1 ATOM 3229 C C . GLY B 2 87 ? -46.036 26.729 52.354 1.00 56.19 ? 87 GLY B C 1 ATOM 3230 O O . GLY B 2 87 ? -46.159 26.477 51.155 1.00 56.04 ? 87 GLY B O 1 ATOM 3231 N N . PHE B 2 88 ? -45.860 27.962 52.820 1.00 55.37 ? 88 PHE B N 1 ATOM 3232 C CA . PHE B 2 88 ? -45.786 29.102 51.928 1.00 54.21 ? 88 PHE B CA 1 ATOM 3233 C C . PHE B 2 88 ? -44.555 29.048 51.021 1.00 54.64 ? 88 PHE B C 1 ATOM 3234 O O . PHE B 2 88 ? -44.664 29.309 49.828 1.00 54.61 ? 88 PHE B O 1 ATOM 3235 C CB . PHE B 2 88 ? -45.822 30.402 52.725 1.00 54.20 ? 88 PHE B CB 1 ATOM 3236 C CG . PHE B 2 88 ? -47.182 30.741 53.255 1.00 53.69 ? 88 PHE B CG 1 ATOM 3237 C CD1 . PHE B 2 88 ? -48.225 31.006 52.390 1.00 53.26 ? 88 PHE B CD1 1 ATOM 3238 C CD2 . PHE B 2 88 ? -47.418 30.796 54.615 1.00 54.73 ? 88 PHE B CD2 1 ATOM 3239 C CE1 . PHE B 2 88 ? -49.483 31.316 52.868 1.00 54.37 ? 88 PHE B CE1 1 ATOM 3240 C CE2 . PHE B 2 88 ? -48.674 31.110 55.108 1.00 55.25 ? 88 PHE B CE2 1 ATOM 3241 C CZ . PHE B 2 88 ? -49.710 31.373 54.232 1.00 55.54 ? 88 PHE B CZ 1 ATOM 3242 N N . LEU B 2 89 ? -43.396 28.696 51.568 1.00 56.40 ? 89 LEU B N 1 ATOM 3243 C CA . LEU B 2 89 ? -42.183 28.593 50.755 1.00 57.83 ? 89 LEU B CA 1 ATOM 3244 C C . LEU B 2 89 ? -42.346 27.581 49.611 1.00 56.67 ? 89 LEU B C 1 ATOM 3245 O O . LEU B 2 89 ? -41.865 27.807 48.502 1.00 54.51 ? 89 LEU B O 1 ATOM 3246 C CB . LEU B 2 89 ? -40.977 28.229 51.618 1.00 61.03 ? 89 LEU B CB 1 ATOM 3247 C CG . LEU B 2 89 ? -40.551 29.288 52.650 1.00 65.02 ? 89 LEU B CG 1 ATOM 3248 C CD1 . LEU B 2 89 ? -39.485 28.704 53.569 1.00 67.71 ? 89 LEU B CD1 1 ATOM 3249 C CD2 . LEU B 2 89 ? -40.061 30.595 52.022 1.00 65.44 ? 89 LEU B CD2 1 ATOM 3250 N N . ASP B 2 90 ? -43.038 26.479 49.888 1.00 56.06 ? 90 ASP B N 1 ATOM 3251 C CA . ASP B 2 90 ? -43.315 25.459 48.877 1.00 55.45 ? 90 ASP B CA 1 ATOM 3252 C C . ASP B 2 90 ? -44.313 25.945 47.834 1.00 53.75 ? 90 ASP B C 1 ATOM 3253 O O . ASP B 2 90 ? -44.203 25.606 46.660 1.00 52.69 ? 90 ASP B O 1 ATOM 3254 C CB . ASP B 2 90 ? -43.833 24.173 49.534 1.00 56.06 ? 90 ASP B CB 1 ATOM 3255 C CG . ASP B 2 90 ? -42.742 23.415 50.269 1.00 58.21 ? 90 ASP B CG 1 ATOM 3256 O OD1 . ASP B 2 90 ? -41.557 23.779 50.137 1.00 59.19 ? 90 ASP B OD1 1 ATOM 3257 O OD2 . ASP B 2 90 ? -43.060 22.445 50.980 1.00 60.00 ? 90 ASP B OD2 1 ATOM 3258 N N . VAL B 2 91 ? -45.294 26.721 48.275 1.00 53.18 ? 91 VAL B N 1 ATOM 3259 C CA . VAL B 2 91 ? -46.279 27.297 47.371 1.00 52.13 ? 91 VAL B CA 1 ATOM 3260 C C . VAL B 2 91 ? -45.637 28.322 46.450 1.00 51.24 ? 91 VAL B C 1 ATOM 3261 O O . VAL B 2 91 ? -45.955 28.375 45.264 1.00 51.81 ? 91 VAL B O 1 ATOM 3262 C CB . VAL B 2 91 ? -47.431 27.968 48.140 1.00 52.26 ? 91 VAL B CB 1 ATOM 3263 C CG1 . VAL B 2 91 ? -48.281 28.826 47.208 1.00 52.94 ? 91 VAL B CG1 1 ATOM 3264 C CG2 . VAL B 2 91 ? -48.294 26.910 48.806 1.00 52.90 ? 91 VAL B CG2 1 ATOM 3265 N N . TRP B 2 92 ? -44.745 29.134 47.000 1.00 50.54 ? 92 TRP B N 1 ATOM 3266 C CA . TRP B 2 92 ? -44.098 30.182 46.224 1.00 50.58 ? 92 TRP B CA 1 ATOM 3267 C C . TRP B 2 92 ? -42.983 29.643 45.338 1.00 50.97 ? 92 TRP B C 1 ATOM 3268 O O . TRP B 2 92 ? -42.716 30.187 44.278 1.00 52.04 ? 92 TRP B O 1 ATOM 3269 C CB . TRP B 2 92 ? -43.582 31.288 47.144 1.00 50.97 ? 92 TRP B CB 1 ATOM 3270 C CG . TRP B 2 92 ? -44.684 32.178 47.581 1.00 51.54 ? 92 TRP B CG 1 ATOM 3271 C CD1 . TRP B 2 92 ? -45.200 32.288 48.831 1.00 52.24 ? 92 TRP B CD1 1 ATOM 3272 C CD2 . TRP B 2 92 ? -45.450 33.058 46.750 1.00 51.91 ? 92 TRP B CD2 1 ATOM 3273 N NE1 . TRP B 2 92 ? -46.231 33.193 48.838 1.00 53.06 ? 92 TRP B NE1 1 ATOM 3274 C CE2 . TRP B 2 92 ? -46.400 33.685 47.573 1.00 52.65 ? 92 TRP B CE2 1 ATOM 3275 C CE3 . TRP B 2 92 ? -45.414 33.383 45.389 1.00 51.94 ? 92 TRP B CE3 1 ATOM 3276 C CZ2 . TRP B 2 92 ? -47.307 34.623 47.087 1.00 54.39 ? 92 TRP B CZ2 1 ATOM 3277 C CZ3 . TRP B 2 92 ? -46.313 34.317 44.904 1.00 52.99 ? 92 TRP B CZ3 1 ATOM 3278 C CH2 . TRP B 2 92 ? -47.248 34.929 45.752 1.00 54.17 ? 92 TRP B CH2 1 ATOM 3279 N N . THR B 2 93 ? -42.324 28.585 45.783 1.00 52.25 ? 93 THR B N 1 ATOM 3280 C CA . THR B 2 93 ? -41.348 27.896 44.965 1.00 52.26 ? 93 THR B CA 1 ATOM 3281 C C . THR B 2 93 ? -42.044 27.307 43.738 1.00 52.44 ? 93 THR B C 1 ATOM 3282 O O . THR B 2 93 ? -41.582 27.490 42.599 1.00 52.72 ? 93 THR B O 1 ATOM 3283 C CB . THR B 2 93 ? -40.649 26.790 45.769 1.00 53.02 ? 93 THR B CB 1 ATOM 3284 O OG1 . THR B 2 93 ? -39.832 27.396 46.774 1.00 54.31 ? 93 THR B OG1 1 ATOM 3285 C CG2 . THR B 2 93 ? -39.778 25.928 44.878 1.00 54.21 ? 93 THR B CG2 1 ATOM 3286 N N . TYR B 2 94 ? -43.149 26.606 43.982 1.00 51.83 ? 94 TYR B N 1 ATOM 3287 C CA . TYR B 2 94 ? -43.967 26.035 42.915 1.00 51.43 ? 94 TYR B CA 1 ATOM 3288 C C . TYR B 2 94 ? -44.388 27.136 41.944 1.00 51.49 ? 94 TYR B C 1 ATOM 3289 O O . TYR B 2 94 ? -44.168 27.025 40.739 1.00 50.81 ? 94 TYR B O 1 ATOM 3290 C CB . TYR B 2 94 ? -45.189 25.325 43.510 1.00 50.97 ? 94 TYR B CB 1 ATOM 3291 C CG . TYR B 2 94 ? -46.245 24.917 42.517 1.00 50.83 ? 94 TYR B CG 1 ATOM 3292 C CD1 . TYR B 2 94 ? -47.285 25.779 42.196 1.00 50.66 ? 94 TYR B CD1 1 ATOM 3293 C CD2 . TYR B 2 94 ? -46.223 23.662 41.912 1.00 51.68 ? 94 TYR B CD2 1 ATOM 3294 C CE1 . TYR B 2 94 ? -48.267 25.418 41.289 1.00 51.05 ? 94 TYR B CE1 1 ATOM 3295 C CE2 . TYR B 2 94 ? -47.202 23.291 40.997 1.00 52.22 ? 94 TYR B CE2 1 ATOM 3296 C CZ . TYR B 2 94 ? -48.223 24.179 40.688 1.00 51.87 ? 94 TYR B CZ 1 ATOM 3297 O OH . TYR B 2 94 ? -49.213 23.847 39.788 1.00 52.85 ? 94 TYR B OH 1 ATOM 3298 N N . ASN B 2 95 ? -44.973 28.204 42.478 1.00 51.83 ? 95 ASN B N 1 ATOM 3299 C CA . ASN B 2 95 ? -45.408 29.327 41.654 1.00 51.82 ? 95 ASN B CA 1 ATOM 3300 C C . ASN B 2 95 ? -44.300 29.850 40.750 1.00 52.00 ? 95 ASN B C 1 ATOM 3301 O O . ASN B 2 95 ? -44.537 30.127 39.574 1.00 54.13 ? 95 ASN B O 1 ATOM 3302 C CB . ASN B 2 95 ? -45.954 30.465 42.520 1.00 51.84 ? 95 ASN B CB 1 ATOM 3303 C CG . ASN B 2 95 ? -47.351 30.181 43.045 1.00 52.99 ? 95 ASN B CG 1 ATOM 3304 O OD1 . ASN B 2 95 ? -47.924 29.127 42.782 1.00 52.53 ? 95 ASN B OD1 1 ATOM 3305 N ND2 . ASN B 2 95 ? -47.903 31.124 43.799 1.00 54.42 ? 95 ASN B ND2 1 ATOM 3306 N N . ALA B 2 96 ? -43.097 29.966 41.293 1.00 51.09 ? 96 ALA B N 1 ATOM 3307 C CA . ALA B 2 96 ? -41.966 30.500 40.545 1.00 51.18 ? 96 ALA B CA 1 ATOM 3308 C C . ALA B 2 96 ? -41.467 29.552 39.451 1.00 50.84 ? 96 ALA B C 1 ATOM 3309 O O . ALA B 2 96 ? -41.204 29.980 38.333 1.00 51.61 ? 96 ALA B O 1 ATOM 3310 C CB . ALA B 2 96 ? -40.831 30.833 41.496 1.00 52.17 ? 96 ALA B CB 1 ATOM 3311 N N . GLU B 2 97 ? -41.320 28.275 39.783 1.00 51.21 ? 97 GLU B N 1 ATOM 3312 C CA . GLU B 2 97 ? -40.778 27.291 38.847 1.00 51.76 ? 97 GLU B CA 1 ATOM 3313 C C . GLU B 2 97 ? -41.744 26.999 37.707 1.00 51.30 ? 97 GLU B C 1 ATOM 3314 O O . GLU B 2 97 ? -41.319 26.783 36.567 1.00 52.20 ? 97 GLU B O 1 ATOM 3315 C CB . GLU B 2 97 ? -40.412 25.994 39.570 1.00 53.24 ? 97 GLU B CB 1 ATOM 3316 C CG . GLU B 2 97 ? -39.214 26.148 40.491 1.00 55.20 ? 97 GLU B CG 1 ATOM 3317 C CD . GLU B 2 97 ? -38.894 24.900 41.290 1.00 58.09 ? 97 GLU B CD 1 ATOM 3318 O OE1 . GLU B 2 97 ? -39.796 24.057 41.489 1.00 59.43 ? 97 GLU B OE1 1 ATOM 3319 O OE2 . GLU B 2 97 ? -37.733 24.766 41.735 1.00 61.05 ? 97 GLU B OE2 1 ATOM 3320 N N . LEU B 2 98 ? -43.035 26.997 38.014 1.00 50.54 ? 98 LEU B N 1 ATOM 3321 C CA . LEU B 2 98 ? -44.050 26.739 37.013 1.00 50.71 ? 98 LEU B CA 1 ATOM 3322 C C . LEU B 2 98 ? -44.178 27.923 36.075 1.00 50.67 ? 98 LEU B C 1 ATOM 3323 O O . LEU B 2 98 ? -44.168 27.762 34.859 1.00 51.45 ? 98 LEU B O 1 ATOM 3324 C CB . LEU B 2 98 ? -45.392 26.468 37.669 1.00 51.54 ? 98 LEU B CB 1 ATOM 3325 C CG . LEU B 2 98 ? -46.465 25.937 36.724 1.00 52.84 ? 98 LEU B CG 1 ATOM 3326 C CD1 . LEU B 2 98 ? -46.119 24.521 36.286 1.00 54.01 ? 98 LEU B CD1 1 ATOM 3327 C CD2 . LEU B 2 98 ? -47.823 25.972 37.407 1.00 54.21 ? 98 LEU B CD2 1 ATOM 3328 N N . LEU B 2 99 ? -44.289 29.117 36.639 1.00 50.83 ? 99 LEU B N 1 ATOM 3329 C CA . LEU B 2 99 ? -44.392 30.320 35.826 1.00 51.37 ? 99 LEU B CA 1 ATOM 3330 C C . LEU B 2 99 ? -43.248 30.377 34.816 1.00 50.45 ? 99 LEU B C 1 ATOM 3331 O O . LEU B 2 99 ? -43.460 30.706 33.644 1.00 50.11 ? 99 LEU B O 1 ATOM 3332 C CB . LEU B 2 99 ? -44.393 31.574 36.706 1.00 52.72 ? 99 LEU B CB 1 ATOM 3333 C CG . LEU B 2 99 ? -44.549 32.928 36.004 1.00 54.40 ? 99 LEU B CG 1 ATOM 3334 C CD1 . LEU B 2 99 ? -45.698 32.917 35.014 1.00 56.03 ? 99 LEU B CD1 1 ATOM 3335 C CD2 . LEU B 2 99 ? -44.751 34.037 37.022 1.00 55.88 ? 99 LEU B CD2 1 ATOM 3336 N N . VAL B 2 100 ? -42.044 30.036 35.266 1.00 49.27 ? 100 VAL B N 1 ATOM 3337 C CA . VAL B 2 100 ? -40.883 30.024 34.379 1.00 49.14 ? 100 VAL B CA 1 ATOM 3338 C C . VAL B 2 100 ? -41.038 28.980 33.265 1.00 48.13 ? 100 VAL B C 1 ATOM 3339 O O . VAL B 2 100 ? -40.845 29.294 32.082 1.00 47.05 ? 100 VAL B O 1 ATOM 3340 C CB . VAL B 2 100 ? -39.575 29.811 35.169 1.00 49.66 ? 100 VAL B CB 1 ATOM 3341 C CG1 . VAL B 2 100 ? -38.416 29.475 34.239 1.00 50.19 ? 100 VAL B CG1 1 ATOM 3342 C CG2 . VAL B 2 100 ? -39.259 31.063 35.967 1.00 50.23 ? 100 VAL B CG2 1 ATOM 3343 N N . LEU B 2 101 ? -41.386 27.755 33.658 1.00 47.36 ? 101 LEU B N 1 ATOM 3344 C CA . LEU B 2 101 ? -41.655 26.664 32.721 1.00 47.28 ? 101 LEU B CA 1 ATOM 3345 C C . LEU B 2 101 ? -42.689 27.049 31.659 1.00 47.75 ? 101 LEU B C 1 ATOM 3346 O O . LEU B 2 101 ? -42.482 26.837 30.462 1.00 48.50 ? 101 LEU B O 1 ATOM 3347 C CB . LEU B 2 101 ? -42.163 25.440 33.482 1.00 48.12 ? 101 LEU B CB 1 ATOM 3348 C CG . LEU B 2 101 ? -41.211 24.275 33.733 1.00 49.75 ? 101 LEU B CG 1 ATOM 3349 C CD1 . LEU B 2 101 ? -39.837 24.721 34.197 1.00 50.78 ? 101 LEU B CD1 1 ATOM 3350 C CD2 . LEU B 2 101 ? -41.837 23.345 34.752 1.00 50.61 ? 101 LEU B CD2 1 ATOM 3351 N N . MET B 2 102 ? -43.804 27.614 32.105 1.00 47.48 ? 102 MET B N 1 ATOM 3352 C CA . MET B 2 102 ? -44.898 27.926 31.208 1.00 47.62 ? 102 MET B CA 1 ATOM 3353 C C . MET B 2 102 ? -44.549 29.065 30.277 1.00 47.45 ? 102 MET B C 1 ATOM 3354 O O . MET B 2 102 ? -44.844 29.000 29.079 1.00 47.76 ? 102 MET B O 1 ATOM 3355 C CB . MET B 2 102 ? -46.153 28.265 31.993 1.00 48.51 ? 102 MET B CB 1 ATOM 3356 C CG . MET B 2 102 ? -46.745 27.070 32.700 1.00 50.39 ? 102 MET B CG 1 ATOM 3357 S SD . MET B 2 102 ? -48.400 27.416 33.308 1.00 54.44 ? 102 MET B SD 1 ATOM 3358 C CE . MET B 2 102 ? -48.083 28.800 34.400 1.00 54.53 ? 102 MET B CE 1 ATOM 3359 N N . GLU B 2 103 ? -43.923 30.106 30.817 1.00 47.32 ? 103 GLU B N 1 ATOM 3360 C CA . GLU B 2 103 ? -43.595 31.269 30.005 1.00 47.77 ? 103 GLU B CA 1 ATOM 3361 C C . GLU B 2 103 ? -42.380 31.028 29.119 1.00 47.75 ? 103 GLU B C 1 ATOM 3362 O O . GLU B 2 103 ? -42.250 31.649 28.075 1.00 47.92 ? 103 GLU B O 1 ATOM 3363 C CB . GLU B 2 103 ? -43.415 32.510 30.869 1.00 48.12 ? 103 GLU B CB 1 ATOM 3364 C CG . GLU B 2 103 ? -44.704 32.961 31.545 1.00 49.86 ? 103 GLU B CG 1 ATOM 3365 C CD . GLU B 2 103 ? -45.781 33.447 30.584 1.00 50.73 ? 103 GLU B CD 1 ATOM 3366 O OE1 . GLU B 2 103 ? -45.453 33.831 29.452 1.00 50.89 ? 103 GLU B OE1 1 ATOM 3367 O OE2 . GLU B 2 103 ? -46.971 33.459 30.965 1.00 53.61 ? 103 GLU B OE2 1 ATOM 3368 N N . ASN B 2 104 ? -41.497 30.127 29.521 1.00 48.69 ? 104 ASN B N 1 ATOM 3369 C CA . ASN B 2 104 ? -40.401 29.739 28.651 1.00 49.40 ? 104 ASN B CA 1 ATOM 3370 C C . ASN B 2 104 ? -40.938 29.098 27.386 1.00 50.27 ? 104 ASN B C 1 ATOM 3371 O O . ASN B 2 104 ? -40.515 29.431 26.285 1.00 50.16 ? 104 ASN B O 1 ATOM 3372 C CB . ASN B 2 104 ? -39.446 28.777 29.360 1.00 50.23 ? 104 ASN B CB 1 ATOM 3373 C CG . ASN B 2 104 ? -38.460 29.492 30.259 1.00 50.10 ? 104 ASN B CG 1 ATOM 3374 O OD1 . ASN B 2 104 ? -38.370 30.715 30.249 1.00 49.51 ? 104 ASN B OD1 1 ATOM 3375 N ND2 . ASN B 2 104 ? -37.707 28.726 31.037 1.00 51.25 ? 104 ASN B ND2 1 ATOM 3376 N N . GLU B 2 105 ? -41.880 28.182 27.544 1.00 51.90 ? 105 GLU B N 1 ATOM 3377 C CA . GLU B 2 105 ? -42.485 27.543 26.395 1.00 54.31 ? 105 GLU B CA 1 ATOM 3378 C C . GLU B 2 105 ? -43.182 28.571 25.517 1.00 54.11 ? 105 GLU B C 1 ATOM 3379 O O . GLU B 2 105 ? -43.113 28.499 24.290 1.00 54.54 ? 105 GLU B O 1 ATOM 3380 C CB . GLU B 2 105 ? -43.484 26.488 26.836 1.00 57.91 ? 105 GLU B CB 1 ATOM 3381 C CG . GLU B 2 105 ? -43.945 25.593 25.707 1.00 61.73 ? 105 GLU B CG 1 ATOM 3382 C CD . GLU B 2 105 ? -44.581 24.327 26.218 1.00 66.94 ? 105 GLU B CD 1 ATOM 3383 O OE1 . GLU B 2 105 ? -45.769 24.388 26.607 1.00 71.61 ? 105 GLU B OE1 1 ATOM 3384 O OE2 . GLU B 2 105 ? -43.894 23.277 26.229 1.00 70.69 ? 105 GLU B OE2 1 ATOM 3385 N N . ARG B 2 106 ? -43.852 29.531 26.146 1.00 54.09 ? 106 ARG B N 1 ATOM 3386 C CA . ARG B 2 106 ? -44.560 30.555 25.391 1.00 54.92 ? 106 ARG B CA 1 ATOM 3387 C C . ARG B 2 106 ? -43.593 31.486 24.671 1.00 52.49 ? 106 ARG B C 1 ATOM 3388 O O . ARG B 2 106 ? -43.874 31.923 23.557 1.00 53.26 ? 106 ARG B O 1 ATOM 3389 C CB . ARG B 2 106 ? -45.515 31.345 26.286 1.00 57.42 ? 106 ARG B CB 1 ATOM 3390 C CG . ARG B 2 106 ? -46.691 30.516 26.791 1.00 61.11 ? 106 ARG B CG 1 ATOM 3391 C CD . ARG B 2 106 ? -47.938 31.359 26.996 1.00 65.85 ? 106 ARG B CD 1 ATOM 3392 N NE . ARG B 2 106 ? -48.655 31.614 25.739 1.00 69.77 ? 106 ARG B NE 1 ATOM 3393 C CZ . ARG B 2 106 ? -49.590 32.551 25.576 1.00 74.04 ? 106 ARG B CZ 1 ATOM 3394 N NH1 . ARG B 2 106 ? -49.940 33.343 26.587 1.00 77.42 ? 106 ARG B NH1 1 ATOM 3395 N NH2 . ARG B 2 106 ? -50.187 32.701 24.397 1.00 76.27 ? 106 ARG B NH2 1 ATOM 3396 N N . THR B 2 107 ? -42.452 31.766 25.296 1.00 49.71 ? 107 THR B N 1 ATOM 3397 C CA . THR B 2 107 ? -41.454 32.658 24.715 1.00 47.93 ? 107 THR B CA 1 ATOM 3398 C C . THR B 2 107 ? -40.821 32.045 23.461 1.00 46.77 ? 107 THR B C 1 ATOM 3399 O O . THR B 2 107 ? -40.572 32.739 22.486 1.00 45.54 ? 107 THR B O 1 ATOM 3400 C CB . THR B 2 107 ? -40.360 33.037 25.740 1.00 47.21 ? 107 THR B CB 1 ATOM 3401 O OG1 . THR B 2 107 ? -40.958 33.708 26.850 1.00 47.29 ? 107 THR B OG1 1 ATOM 3402 C CG2 . THR B 2 107 ? -39.338 33.976 25.127 1.00 47.86 ? 107 THR B CG2 1 ATOM 3403 N N . LEU B 2 108 ? -40.570 30.744 23.483 1.00 46.11 ? 108 LEU B N 1 ATOM 3404 C CA . LEU B 2 108 ? -40.005 30.075 22.320 1.00 46.00 ? 108 LEU B CA 1 ATOM 3405 C C . LEU B 2 108 ? -41.017 30.015 21.179 1.00 46.78 ? 108 LEU B C 1 ATOM 3406 O O . LEU B 2 108 ? -40.677 30.242 20.009 1.00 46.40 ? 108 LEU B O 1 ATOM 3407 C CB . LEU B 2 108 ? -39.547 28.671 22.689 1.00 46.07 ? 108 LEU B CB 1 ATOM 3408 C CG . LEU B 2 108 ? -38.501 28.602 23.798 1.00 46.11 ? 108 LEU B CG 1 ATOM 3409 C CD1 . LEU B 2 108 ? -38.101 27.155 24.021 1.00 47.28 ? 108 LEU B CD1 1 ATOM 3410 C CD2 . LEU B 2 108 ? -37.290 29.456 23.469 1.00 46.45 ? 108 LEU B CD2 1 ATOM 3411 N N . ASP B 2 109 ? -42.262 29.706 21.527 1.00 47.19 ? 109 ASP B N 1 ATOM 3412 C CA . ASP B 2 109 ? -43.346 29.724 20.560 1.00 48.00 ? 109 ASP B CA 1 ATOM 3413 C C . ASP B 2 109 ? -43.554 31.128 19.990 1.00 47.26 ? 109 ASP B C 1 ATOM 3414 O O . ASP B 2 109 ? -43.837 31.279 18.810 1.00 49.26 ? 109 ASP B O 1 ATOM 3415 C CB . ASP B 2 109 ? -44.637 29.213 21.200 1.00 49.92 ? 109 ASP B CB 1 ATOM 3416 C CG . ASP B 2 109 ? -44.601 27.707 21.488 1.00 52.54 ? 109 ASP B CG 1 ATOM 3417 O OD1 . ASP B 2 109 ? -43.841 26.978 20.803 1.00 52.49 ? 109 ASP B OD1 1 ATOM 3418 O OD2 . ASP B 2 109 ? -45.352 27.256 22.396 1.00 54.64 ? 109 ASP B OD2 1 ATOM 3419 N N . PHE B 2 110 ? -43.415 32.147 20.832 1.00 45.37 ? 110 PHE B N 1 ATOM 3420 C CA . PHE B 2 110 ? -43.561 33.535 20.412 1.00 44.44 ? 110 PHE B CA 1 ATOM 3421 C C . PHE B 2 110 ? -42.569 33.877 19.293 1.00 44.56 ? 110 PHE B C 1 ATOM 3422 O O . PHE B 2 110 ? -42.943 34.451 18.271 1.00 45.53 ? 110 PHE B O 1 ATOM 3423 C CB . PHE B 2 110 ? -43.354 34.435 21.626 1.00 44.04 ? 110 PHE B CB 1 ATOM 3424 C CG . PHE B 2 110 ? -43.366 35.898 21.321 1.00 44.85 ? 110 PHE B CG 1 ATOM 3425 C CD1 . PHE B 2 110 ? -44.470 36.488 20.733 1.00 46.40 ? 110 PHE B CD1 1 ATOM 3426 C CD2 . PHE B 2 110 ? -42.280 36.698 21.655 1.00 44.67 ? 110 PHE B CD2 1 ATOM 3427 C CE1 . PHE B 2 110 ? -44.479 37.846 20.450 1.00 47.74 ? 110 PHE B CE1 1 ATOM 3428 C CE2 . PHE B 2 110 ? -42.290 38.059 21.385 1.00 46.16 ? 110 PHE B CE2 1 ATOM 3429 C CZ . PHE B 2 110 ? -43.388 38.634 20.778 1.00 47.37 ? 110 PHE B CZ 1 ATOM 3430 N N . HIS B 2 111 ? -41.309 33.507 19.484 1.00 43.71 ? 111 HIS B N 1 ATOM 3431 C CA . HIS B 2 111 ? -40.287 33.696 18.461 1.00 43.70 ? 111 HIS B CA 1 ATOM 3432 C C . HIS B 2 111 ? -40.625 32.962 17.162 1.00 43.95 ? 111 HIS B C 1 ATOM 3433 O O . HIS B 2 111 ? -40.448 33.506 16.076 1.00 44.74 ? 111 HIS B O 1 ATOM 3434 C CB . HIS B 2 111 ? -38.934 33.217 18.973 1.00 43.37 ? 111 HIS B CB 1 ATOM 3435 C CG . HIS B 2 111 ? -38.303 34.141 19.962 1.00 43.63 ? 111 HIS B CG 1 ATOM 3436 N ND1 . HIS B 2 111 ? -37.925 35.424 19.640 1.00 44.29 ? 111 HIS B ND1 1 ATOM 3437 C CD2 . HIS B 2 111 ? -37.951 33.957 21.256 1.00 43.82 ? 111 HIS B CD2 1 ATOM 3438 C CE1 . HIS B 2 111 ? -37.384 36.000 20.697 1.00 45.31 ? 111 HIS B CE1 1 ATOM 3439 N NE2 . HIS B 2 111 ? -37.386 35.129 21.692 1.00 44.69 ? 111 HIS B NE2 1 ATOM 3440 N N . ASP B 2 112 ? -41.097 31.725 17.288 1.00 43.60 ? 112 ASP B N 1 ATOM 3441 C CA . ASP B 2 112 ? -41.519 30.922 16.151 1.00 43.88 ? 112 ASP B CA 1 ATOM 3442 C C . ASP B 2 112 ? -42.606 31.663 15.378 1.00 45.09 ? 112 ASP B C 1 ATOM 3443 O O . ASP B 2 112 ? -42.563 31.760 14.149 1.00 45.96 ? 112 ASP B O 1 ATOM 3444 C CB . ASP B 2 112 ? -42.052 29.572 16.649 1.00 44.99 ? 112 ASP B CB 1 ATOM 3445 C CG . ASP B 2 112 ? -42.058 28.496 15.575 1.00 46.35 ? 112 ASP B CG 1 ATOM 3446 O OD1 . ASP B 2 112 ? -41.601 28.763 14.434 1.00 46.22 ? 112 ASP B OD1 1 ATOM 3447 O OD2 . ASP B 2 112 ? -42.523 27.371 15.888 1.00 47.08 ? 112 ASP B OD2 1 ATOM 3448 N N . SER B 2 113 ? -43.571 32.201 16.117 1.00 45.54 ? 113 SER B N 1 ATOM 3449 C CA . SER B 2 113 ? -44.685 32.936 15.541 1.00 46.34 ? 113 SER B CA 1 ATOM 3450 C C . SER B 2 113 ? -44.203 34.142 14.759 1.00 46.64 ? 113 SER B C 1 ATOM 3451 O O . SER B 2 113 ? -44.654 34.377 13.640 1.00 47.80 ? 113 SER B O 1 ATOM 3452 C CB . SER B 2 113 ? -45.638 33.400 16.642 1.00 47.10 ? 113 SER B CB 1 ATOM 3453 O OG . SER B 2 113 ? -46.584 34.329 16.144 1.00 48.72 ? 113 SER B OG 1 ATOM 3454 N N . ASN B 2 114 ? -43.300 34.911 15.360 1.00 45.92 ? 114 ASN B N 1 ATOM 3455 C CA . ASN B 2 114 ? -42.733 36.077 14.700 1.00 46.47 ? 114 ASN B CA 1 ATOM 3456 C C . ASN B 2 114 ? -42.039 35.718 13.382 1.00 46.58 ? 114 ASN B C 1 ATOM 3457 O O . ASN B 2 114 ? -42.136 36.465 12.406 1.00 47.41 ? 114 ASN B O 1 ATOM 3458 C CB . ASN B 2 114 ? -41.752 36.799 15.621 1.00 46.24 ? 114 ASN B CB 1 ATOM 3459 C CG . ASN B 2 114 ? -42.433 37.449 16.808 1.00 47.17 ? 114 ASN B CG 1 ATOM 3460 O OD1 . ASN B 2 114 ? -43.558 37.931 16.709 1.00 48.26 ? 114 ASN B OD1 1 ATOM 3461 N ND2 . ASN B 2 114 ? -41.743 37.475 17.942 1.00 46.78 ? 114 ASN B ND2 1 ATOM 3462 N N . VAL B 2 115 ? -41.357 34.577 13.348 1.00 45.88 ? 115 VAL B N 1 ATOM 3463 C CA . VAL B 2 115 ? -40.667 34.150 12.133 1.00 46.43 ? 115 VAL B CA 1 ATOM 3464 C C . VAL B 2 115 ? -41.681 33.747 11.066 1.00 47.45 ? 115 VAL B C 1 ATOM 3465 O O . VAL B 2 115 ? -41.568 34.148 9.913 1.00 47.49 ? 115 VAL B O 1 ATOM 3466 C CB . VAL B 2 115 ? -39.690 32.988 12.402 1.00 45.58 ? 115 VAL B CB 1 ATOM 3467 C CG1 . VAL B 2 115 ? -39.102 32.465 11.099 1.00 45.70 ? 115 VAL B CG1 1 ATOM 3468 C CG2 . VAL B 2 115 ? -38.566 33.440 13.323 1.00 45.48 ? 115 VAL B CG2 1 ATOM 3469 N N . LYS B 2 116 ? -42.668 32.956 11.465 1.00 48.78 ? 116 LYS B N 1 ATOM 3470 C CA . LYS B 2 116 ? -43.726 32.515 10.566 1.00 51.08 ? 116 LYS B CA 1 ATOM 3471 C C . LYS B 2 116 ? -44.461 33.704 9.967 1.00 52.31 ? 116 LYS B C 1 ATOM 3472 O O . LYS B 2 116 ? -44.713 33.740 8.769 1.00 53.37 ? 116 LYS B O 1 ATOM 3473 C CB . LYS B 2 116 ? -44.708 31.618 11.325 1.00 53.22 ? 116 LYS B CB 1 ATOM 3474 C CG . LYS B 2 116 ? -45.837 31.018 10.505 1.00 56.85 ? 116 LYS B CG 1 ATOM 3475 C CD . LYS B 2 116 ? -45.307 30.250 9.295 1.00 58.98 ? 116 LYS B CD 1 ATOM 3476 C CE . LYS B 2 116 ? -46.138 29.009 8.993 1.00 61.67 ? 116 LYS B CE 1 ATOM 3477 N NZ . LYS B 2 116 ? -47.579 29.346 8.862 1.00 64.60 ? 116 LYS B NZ 1 ATOM 3478 N N . ASN B 2 117 ? -44.793 34.685 10.800 1.00 52.99 ? 117 ASN B N 1 ATOM 3479 C CA . ASN B 2 117 ? -45.539 35.853 10.333 1.00 54.60 ? 117 ASN B CA 1 ATOM 3480 C C . ASN B 2 117 ? -44.738 36.673 9.327 1.00 54.65 ? 117 ASN B C 1 ATOM 3481 O O . ASN B 2 117 ? -45.279 37.153 8.325 1.00 55.67 ? 117 ASN B O 1 ATOM 3482 C CB . ASN B 2 117 ? -45.987 36.715 11.515 1.00 54.72 ? 117 ASN B CB 1 ATOM 3483 C CG . ASN B 2 117 ? -47.085 36.055 12.327 1.00 55.86 ? 117 ASN B CG 1 ATOM 3484 O OD1 . ASN B 2 117 ? -47.811 35.200 11.823 1.00 56.81 ? 117 ASN B OD1 1 ATOM 3485 N ND2 . ASN B 2 117 ? -47.217 36.453 13.590 1.00 56.07 ? 117 ASN B ND2 1 ATOM 3486 N N . LEU B 2 118 ? -43.445 36.804 9.600 1.00 53.98 ? 118 LEU B N 1 ATOM 3487 C CA . LEU B 2 118 ? -42.517 37.478 8.710 1.00 54.71 ? 118 LEU B CA 1 ATOM 3488 C C . LEU B 2 118 ? -42.383 36.716 7.392 1.00 55.24 ? 118 LEU B C 1 ATOM 3489 O O . LEU B 2 118 ? -42.337 37.314 6.320 1.00 55.97 ? 118 LEU B O 1 ATOM 3490 C CB . LEU B 2 118 ? -41.161 37.607 9.395 1.00 54.06 ? 118 LEU B CB 1 ATOM 3491 C CG . LEU B 2 118 ? -40.050 38.324 8.643 1.00 55.47 ? 118 LEU B CG 1 ATOM 3492 C CD1 . LEU B 2 118 ? -40.524 39.685 8.163 1.00 58.71 ? 118 LEU B CD1 1 ATOM 3493 C CD2 . LEU B 2 118 ? -38.826 38.468 9.529 1.00 55.19 ? 118 LEU B CD2 1 ATOM 3494 N N . TYR B 2 119 ? -42.332 35.393 7.477 1.00 55.11 ? 119 TYR B N 1 ATOM 3495 C CA . TYR B 2 119 ? -42.288 34.561 6.288 1.00 55.45 ? 119 TYR B CA 1 ATOM 3496 C C . TYR B 2 119 ? -43.538 34.763 5.461 1.00 58.52 ? 119 TYR B C 1 ATOM 3497 O O . TYR B 2 119 ? -43.466 34.907 4.248 1.00 60.41 ? 119 TYR B O 1 ATOM 3498 C CB . TYR B 2 119 ? -42.170 33.085 6.663 1.00 55.00 ? 119 TYR B CB 1 ATOM 3499 C CG . TYR B 2 119 ? -42.164 32.151 5.471 1.00 55.93 ? 119 TYR B CG 1 ATOM 3500 C CD1 . TYR B 2 119 ? -41.023 31.998 4.695 1.00 55.65 ? 119 TYR B CD1 1 ATOM 3501 C CD2 . TYR B 2 119 ? -43.294 31.420 5.122 1.00 56.89 ? 119 TYR B CD2 1 ATOM 3502 C CE1 . TYR B 2 119 ? -41.007 31.148 3.607 1.00 56.58 ? 119 TYR B CE1 1 ATOM 3503 C CE2 . TYR B 2 119 ? -43.284 30.565 4.034 1.00 57.83 ? 119 TYR B CE2 1 ATOM 3504 C CZ . TYR B 2 119 ? -42.138 30.437 3.283 1.00 57.69 ? 119 TYR B CZ 1 ATOM 3505 O OH . TYR B 2 119 ? -42.106 29.599 2.200 1.00 59.48 ? 119 TYR B OH 1 ATOM 3506 N N . ASP B 2 120 ? -44.689 34.761 6.119 1.00 61.33 ? 120 ASP B N 1 ATOM 3507 C CA . ASP B 2 120 ? -45.953 34.884 5.412 1.00 64.42 ? 120 ASP B CA 1 ATOM 3508 C C . ASP B 2 120 ? -46.110 36.272 4.802 1.00 66.08 ? 120 ASP B C 1 ATOM 3509 O O . ASP B 2 120 ? -46.710 36.408 3.746 1.00 68.59 ? 120 ASP B O 1 ATOM 3510 C CB . ASP B 2 120 ? -47.133 34.545 6.331 1.00 66.31 ? 120 ASP B CB 1 ATOM 3511 C CG . ASP B 2 120 ? -47.263 33.048 6.588 1.00 66.90 ? 120 ASP B CG 1 ATOM 3512 O OD1 . ASP B 2 120 ? -46.972 32.247 5.676 1.00 68.84 ? 120 ASP B OD1 1 ATOM 3513 O OD2 . ASP B 2 120 ? -47.671 32.664 7.701 1.00 68.43 ? 120 ASP B OD2 1 ATOM 3514 N N . LYS B 2 121 ? -45.556 37.292 5.447 1.00 66.46 ? 121 LYS B N 1 ATOM 3515 C CA . LYS B 2 121 ? -45.649 38.652 4.926 1.00 69.95 ? 121 LYS B CA 1 ATOM 3516 C C . LYS B 2 121 ? -44.930 38.765 3.589 1.00 69.61 ? 121 LYS B C 1 ATOM 3517 O O . LYS B 2 121 ? -45.427 39.397 2.658 1.00 72.90 ? 121 LYS B O 1 ATOM 3518 C CB . LYS B 2 121 ? -45.064 39.657 5.914 1.00 72.62 ? 121 LYS B CB 1 ATOM 3519 C CG . LYS B 2 121 ? -45.366 41.103 5.554 1.00 78.19 ? 121 LYS B CG 1 ATOM 3520 C CD . LYS B 2 121 ? -45.014 42.056 6.686 1.00 82.50 ? 121 LYS B CD 1 ATOM 3521 C CE . LYS B 2 121 ? -43.510 42.258 6.805 1.00 82.94 ? 121 LYS B CE 1 ATOM 3522 N NZ . LYS B 2 121 ? -43.172 43.238 7.877 1.00 86.00 ? 121 LYS B NZ 1 ATOM 3523 N N . VAL B 2 122 ? -43.758 38.149 3.505 1.00 66.53 ? 122 VAL B N 1 ATOM 3524 C CA . VAL B 2 122 ? -42.999 38.090 2.263 1.00 65.41 ? 122 VAL B CA 1 ATOM 3525 C C . VAL B 2 122 ? -43.708 37.214 1.232 1.00 66.92 ? 122 VAL B C 1 ATOM 3526 O O . VAL B 2 122 ? -43.771 37.564 0.058 1.00 67.83 ? 122 VAL B O 1 ATOM 3527 C CB . VAL B 2 122 ? -41.565 37.581 2.524 1.00 62.15 ? 122 VAL B CB 1 ATOM 3528 C CG1 . VAL B 2 122 ? -40.833 37.262 1.222 1.00 61.42 ? 122 VAL B CG1 1 ATOM 3529 C CG2 . VAL B 2 122 ? -40.806 38.612 3.344 1.00 61.97 ? 122 VAL B CG2 1 ATOM 3530 N N . ARG B 2 123 ? -44.246 36.084 1.673 1.00 68.05 ? 123 ARG B N 1 ATOM 3531 C CA . ARG B 2 123 ? -44.965 35.181 0.780 1.00 71.76 ? 123 ARG B CA 1 ATOM 3532 C C . ARG B 2 123 ? -46.127 35.890 0.081 1.00 76.26 ? 123 ARG B C 1 ATOM 3533 O O . ARG B 2 123 ? -46.329 35.722 -1.123 1.00 78.14 ? 123 ARG B O 1 ATOM 3534 C CB . ARG B 2 123 ? -45.485 33.978 1.563 1.00 72.97 ? 123 ARG B CB 1 ATOM 3535 C CG . ARG B 2 123 ? -46.051 32.863 0.703 1.00 76.03 ? 123 ARG B CG 1 ATOM 3536 C CD . ARG B 2 123 ? -46.627 31.738 1.555 1.00 78.49 ? 123 ARG B CD 1 ATOM 3537 N NE . ARG B 2 123 ? -47.610 32.207 2.538 1.00 80.41 ? 123 ARG B NE 1 ATOM 3538 C CZ . ARG B 2 123 ? -48.865 32.564 2.257 1.00 84.23 ? 123 ARG B CZ 1 ATOM 3539 N NH1 . ARG B 2 123 ? -49.331 32.526 1.009 1.00 86.20 ? 123 ARG B NH1 1 ATOM 3540 N NH2 . ARG B 2 123 ? -49.664 32.976 3.234 1.00 85.40 ? 123 ARG B NH2 1 ATOM 3541 N N . LEU B 2 124 ? -46.879 36.688 0.840 1.00 79.58 ? 124 LEU B N 1 ATOM 3542 C CA . LEU B 2 124 ? -48.035 37.422 0.305 1.00 85.30 ? 124 LEU B CA 1 ATOM 3543 C C . LEU B 2 124 ? -47.650 38.528 -0.684 1.00 86.41 ? 124 LEU B C 1 ATOM 3544 O O . LEU B 2 124 ? -48.490 38.978 -1.456 1.00 91.03 ? 124 LEU B O 1 ATOM 3545 C CB . LEU B 2 124 ? -48.858 38.038 1.443 1.00 88.06 ? 124 LEU B CB 1 ATOM 3546 C CG . LEU B 2 124 ? -49.555 37.055 2.393 1.00 90.44 ? 124 LEU B CG 1 ATOM 3547 C CD1 . LEU B 2 124 ? -49.891 37.707 3.736 1.00 91.42 ? 124 LEU B CD1 1 ATOM 3548 C CD2 . LEU B 2 124 ? -50.796 36.459 1.741 1.00 93.48 ? 124 LEU B CD2 1 ATOM 3549 N N . GLN B 2 125 ? -46.398 38.978 -0.637 1.00 83.72 ? 125 GLN B N 1 ATOM 3550 C CA . GLN B 2 125 ? -45.904 40.001 -1.554 1.00 83.89 ? 125 GLN B CA 1 ATOM 3551 C C . GLN B 2 125 ? -45.435 39.393 -2.859 1.00 82.25 ? 125 GLN B C 1 ATOM 3552 O O . GLN B 2 125 ? -45.800 39.860 -3.929 1.00 85.85 ? 125 GLN B O 1 ATOM 3553 C CB . GLN B 2 125 ? -44.752 40.783 -0.928 1.00 83.48 ? 125 GLN B CB 1 ATOM 3554 C CG . GLN B 2 125 ? -45.185 41.757 0.151 1.00 86.43 ? 125 GLN B CG 1 ATOM 3555 C CD . GLN B 2 125 ? -44.125 42.795 0.432 1.00 87.72 ? 125 GLN B CD 1 ATOM 3556 O OE1 . GLN B 2 125 ? -44.268 43.953 0.051 1.00 92.32 ? 125 GLN B OE1 1 ATOM 3557 N NE2 . GLN B 2 125 ? -43.039 42.379 1.072 1.00 86.07 ? 125 GLN B NE2 1 ATOM 3558 N N . LEU B 2 126 ? -44.618 38.355 -2.767 1.00 79.85 ? 126 LEU B N 1 ATOM 3559 C CA . LEU B 2 126 ? -44.051 37.734 -3.953 1.00 80.53 ? 126 LEU B CA 1 ATOM 3560 C C . LEU B 2 126 ? -45.121 37.025 -4.762 1.00 86.37 ? 126 LEU B C 1 ATOM 3561 O O . LEU B 2 126 ? -45.131 37.111 -5.988 1.00 88.47 ? 126 LEU B O 1 ATOM 3562 C CB . LEU B 2 126 ? -42.943 36.755 -3.573 1.00 76.20 ? 126 LEU B CB 1 ATOM 3563 C CG . LEU B 2 126 ? -41.765 37.369 -2.814 1.00 73.78 ? 126 LEU B CG 1 ATOM 3564 C CD1 . LEU B 2 126 ? -40.685 36.323 -2.601 1.00 72.11 ? 126 LEU B CD1 1 ATOM 3565 C CD2 . LEU B 2 126 ? -41.195 38.578 -3.539 1.00 74.28 ? 126 LEU B CD2 1 ATOM 3566 N N . ARG B 2 127 ? -46.022 36.335 -4.069 1.00 93.11 ? 127 ARG B N 1 ATOM 3567 C CA . ARG B 2 127 ? -47.139 35.631 -4.707 1.00 100.73 ? 127 ARG B CA 1 ATOM 3568 C C . ARG B 2 127 ? -46.656 34.653 -5.798 1.00 99.79 ? 127 ARG B C 1 ATOM 3569 O O . ARG B 2 127 ? -46.095 33.606 -5.481 1.00 98.07 ? 127 ARG B O 1 ATOM 3570 C CB . ARG B 2 127 ? -48.188 36.641 -5.224 1.00 107.83 ? 127 ARG B CB 1 ATOM 3571 C CG . ARG B 2 127 ? -49.052 37.242 -4.115 1.00 112.17 ? 127 ARG B CG 1 ATOM 3572 C CD . ARG B 2 127 ? -49.465 38.688 -4.376 1.00 115.80 ? 127 ARG B CD 1 ATOM 3573 N NE . ARG B 2 127 ? -50.145 38.869 -5.658 1.00 121.30 ? 127 ARG B NE 1 ATOM 3574 C CZ . ARG B 2 127 ? -50.590 40.038 -6.119 1.00 126.59 ? 127 ARG B CZ 1 ATOM 3575 N NH1 . ARG B 2 127 ? -50.446 41.153 -5.407 1.00 127.91 ? 127 ARG B NH1 1 ATOM 3576 N NH2 . ARG B 2 127 ? -51.189 40.096 -7.302 1.00 129.87 ? 127 ARG B NH2 1 ATOM 3577 N N . ASP B 2 128 ? -46.843 35.004 -7.066 1.00 101.10 ? 128 ASP B N 1 ATOM 3578 C CA . ASP B 2 128 ? -46.497 34.115 -8.175 1.00 101.11 ? 128 ASP B CA 1 ATOM 3579 C C . ASP B 2 128 ? -45.192 34.525 -8.872 1.00 98.47 ? 128 ASP B C 1 ATOM 3580 O O . ASP B 2 128 ? -44.711 33.813 -9.751 1.00 99.33 ? 128 ASP B O 1 ATOM 3581 C CB . ASP B 2 128 ? -47.653 34.045 -9.185 1.00 107.39 ? 128 ASP B CB 1 ATOM 3582 C CG . ASP B 2 128 ? -48.250 35.412 -9.498 1.00 111.55 ? 128 ASP B CG 1 ATOM 3583 O OD1 . ASP B 2 128 ? -48.448 36.206 -8.554 1.00 112.70 ? 128 ASP B OD1 1 ATOM 3584 O OD2 . ASP B 2 128 ? -48.518 35.693 -10.685 1.00 115.99 ? 128 ASP B OD2 1 ATOM 3585 N N . ASN B 2 129 ? -44.610 35.655 -8.470 1.00 95.88 ? 129 ASN B N 1 ATOM 3586 C CA . ASN B 2 129 ? -43.351 36.132 -9.059 1.00 93.00 ? 129 ASN B CA 1 ATOM 3587 C C . ASN B 2 129 ? -42.100 35.403 -8.544 1.00 88.84 ? 129 ASN B C 1 ATOM 3588 O O . ASN B 2 129 ? -40.978 35.722 -8.959 1.00 86.81 ? 129 ASN B O 1 ATOM 3589 C CB . ASN B 2 129 ? -43.193 37.641 -8.829 1.00 94.77 ? 129 ASN B CB 1 ATOM 3590 C CG . ASN B 2 129 ? -44.182 38.463 -9.638 1.00 99.73 ? 129 ASN B CG 1 ATOM 3591 O OD1 . ASN B 2 129 ? -45.339 38.633 -9.249 1.00 103.34 ? 129 ASN B OD1 1 ATOM 3592 N ND2 . ASN B 2 129 ? -43.728 38.981 -10.769 1.00 101.26 ? 129 ASN B ND2 1 ATOM 3593 N N . ALA B 2 130 ? -42.291 34.435 -7.646 1.00 86.16 ? 130 ALA B N 1 ATOM 3594 C CA . ALA B 2 130 ? -41.186 33.653 -7.095 1.00 82.26 ? 130 ALA B CA 1 ATOM 3595 C C . ALA B 2 130 ? -41.624 32.231 -6.752 1.00 81.07 ? 130 ALA B C 1 ATOM 3596 O O . ALA B 2 130 ? -42.788 31.988 -6.451 1.00 81.68 ? 130 ALA B O 1 ATOM 3597 C CB . ALA B 2 130 ? -40.632 34.342 -5.859 1.00 81.19 ? 130 ALA B CB 1 ATOM 3598 N N . LYS B 2 131 ? -40.673 31.304 -6.795 1.00 79.42 ? 131 LYS B N 1 ATOM 3599 C CA . LYS B 2 131 ? -40.911 29.894 -6.489 1.00 80.69 ? 131 LYS B CA 1 ATOM 3600 C C . LYS B 2 131 ? -40.647 29.624 -5.002 1.00 78.08 ? 131 LYS B C 1 ATOM 3601 O O . LYS B 2 131 ? -39.525 29.806 -4.524 1.00 75.31 ? 131 LYS B O 1 ATOM 3602 C CB . LYS B 2 131 ? -39.985 29.042 -7.355 1.00 84.16 ? 131 LYS B CB 1 ATOM 3603 C CG . LYS B 2 131 ? -40.144 27.534 -7.238 1.00 88.39 ? 131 LYS B CG 1 ATOM 3604 C CD . LYS B 2 131 ? -39.476 26.853 -8.432 1.00 94.15 ? 131 LYS B CD 1 ATOM 3605 C CE . LYS B 2 131 ? -40.403 26.795 -9.648 1.00 98.93 ? 131 LYS B CE 1 ATOM 3606 N NZ . LYS B 2 131 ? -39.863 26.009 -10.797 1.00 101.17 ? 131 LYS B NZ 1 ATOM 3607 N N . GLU B 2 132 ? -41.681 29.202 -4.275 1.00 76.18 ? 132 GLU B N 1 ATOM 3608 C CA . GLU B 2 132 ? -41.564 28.925 -2.844 1.00 72.76 ? 132 GLU B CA 1 ATOM 3609 C C . GLU B 2 132 ? -40.844 27.594 -2.622 1.00 72.27 ? 132 GLU B C 1 ATOM 3610 O O . GLU B 2 132 ? -41.434 26.529 -2.799 1.00 74.75 ? 132 GLU B O 1 ATOM 3611 C CB . GLU B 2 132 ? -42.951 28.898 -2.203 1.00 73.44 ? 132 GLU B CB 1 ATOM 3612 C CG . GLU B 2 132 ? -42.943 28.764 -0.689 1.00 72.19 ? 132 GLU B CG 1 ATOM 3613 C CD . GLU B 2 132 ? -44.333 28.833 -0.075 1.00 73.03 ? 132 GLU B CD 1 ATOM 3614 O OE1 . GLU B 2 132 ? -45.328 28.681 -0.814 1.00 75.76 ? 132 GLU B OE1 1 ATOM 3615 O OE2 . GLU B 2 132 ? -44.435 29.039 1.152 1.00 72.01 ? 132 GLU B OE2 1 ATOM 3616 N N . LEU B 2 133 ? -39.572 27.657 -2.231 1.00 69.57 ? 133 LEU B N 1 ATOM 3617 C CA . LEU B 2 133 ? -38.721 26.460 -2.188 1.00 70.16 ? 133 LEU B CA 1 ATOM 3618 C C . LEU B 2 133 ? -39.089 25.447 -1.118 1.00 70.47 ? 133 LEU B C 1 ATOM 3619 O O . LEU B 2 133 ? -38.784 24.267 -1.273 1.00 70.95 ? 133 LEU B O 1 ATOM 3620 C CB . LEU B 2 133 ? -37.242 26.830 -2.041 1.00 70.38 ? 133 LEU B CB 1 ATOM 3621 C CG . LEU B 2 133 ? -36.445 26.890 -3.347 1.00 71.62 ? 133 LEU B CG 1 ATOM 3622 C CD1 . LEU B 2 133 ? -37.059 27.886 -4.316 1.00 71.58 ? 133 LEU B CD1 1 ATOM 3623 C CD2 . LEU B 2 133 ? -34.989 27.236 -3.063 1.00 71.13 ? 133 LEU B CD2 1 ATOM 3624 N N . GLY B 2 134 ? -39.719 25.909 -0.038 1.00 69.74 ? 134 GLY B N 1 ATOM 3625 C CA . GLY B 2 134 ? -40.143 25.036 1.060 1.00 70.31 ? 134 GLY B CA 1 ATOM 3626 C C . GLY B 2 134 ? -39.176 24.983 2.235 1.00 69.47 ? 134 GLY B C 1 ATOM 3627 O O . GLY B 2 134 ? -39.335 24.148 3.133 1.00 70.79 ? 134 GLY B O 1 ATOM 3628 N N . ASN B 2 135 ? -38.184 25.875 2.243 1.00 66.70 ? 135 ASN B N 1 ATOM 3629 C CA . ASN B 2 135 ? -37.154 25.879 3.287 1.00 65.88 ? 135 ASN B CA 1 ATOM 3630 C C . ASN B 2 135 ? -36.934 27.253 3.921 1.00 63.00 ? 135 ASN B C 1 ATOM 3631 O O . ASN B 2 135 ? -35.956 27.455 4.638 1.00 61.32 ? 135 ASN B O 1 ATOM 3632 C CB . ASN B 2 135 ? -35.833 25.371 2.710 1.00 67.35 ? 135 ASN B CB 1 ATOM 3633 C CG . ASN B 2 135 ? -35.334 26.222 1.557 1.00 67.61 ? 135 ASN B CG 1 ATOM 3634 O OD1 . ASN B 2 135 ? -35.880 27.289 1.270 1.00 66.59 ? 135 ASN B OD1 1 ATOM 3635 N ND2 . ASN B 2 135 ? -34.302 25.746 0.881 1.00 70.22 ? 135 ASN B ND2 1 ATOM 3636 N N . GLY B 2 136 ? -37.849 28.184 3.655 1.00 61.92 ? 136 GLY B N 1 ATOM 3637 C CA . GLY B 2 136 ? -37.688 29.579 4.045 1.00 60.11 ? 136 GLY B CA 1 ATOM 3638 C C . GLY B 2 136 ? -37.311 30.492 2.890 1.00 59.61 ? 136 GLY B C 1 ATOM 3639 O O . GLY B 2 136 ? -37.354 31.714 3.029 1.00 56.87 ? 136 GLY B O 1 ATOM 3640 N N . CYS B 2 137 ? -36.952 29.907 1.747 1.00 62.00 ? 137 CYS B N 1 ATOM 3641 C CA . CYS B 2 137 ? -36.428 30.687 0.621 1.00 63.10 ? 137 CYS B CA 1 ATOM 3642 C C . CYS B 2 137 ? -37.399 30.806 -0.544 1.00 63.85 ? 137 CYS B C 1 ATOM 3643 O O . CYS B 2 137 ? -38.161 29.884 -0.841 1.00 63.26 ? 137 CYS B O 1 ATOM 3644 C CB . CYS B 2 137 ? -35.101 30.110 0.129 1.00 63.93 ? 137 CYS B CB 1 ATOM 3645 S SG . CYS B 2 137 ? -33.805 30.093 1.390 1.00 66.40 ? 137 CYS B SG 1 ATOM 3646 N N . PHE B 2 138 ? -37.354 31.964 -1.193 1.00 64.60 ? 138 PHE B N 1 ATOM 3647 C CA . PHE B 2 138 ? -38.134 32.230 -2.384 1.00 66.75 ? 138 PHE B CA 1 ATOM 3648 C C . PHE B 2 138 ? -37.172 32.492 -3.538 1.00 68.41 ? 138 PHE B C 1 ATOM 3649 O O . PHE B 2 138 ? -36.375 33.424 -3.476 1.00 67.95 ? 138 PHE B O 1 ATOM 3650 C CB . PHE B 2 138 ? -39.017 33.457 -2.172 1.00 66.60 ? 138 PHE B CB 1 ATOM 3651 C CG . PHE B 2 138 ? -40.057 33.284 -1.105 1.00 67.33 ? 138 PHE B CG 1 ATOM 3652 C CD1 . PHE B 2 138 ? -41.312 32.778 -1.414 1.00 68.37 ? 138 PHE B CD1 1 ATOM 3653 C CD2 . PHE B 2 138 ? -39.789 33.646 0.207 1.00 68.13 ? 138 PHE B CD2 1 ATOM 3654 C CE1 . PHE B 2 138 ? -42.278 32.625 -0.437 1.00 68.95 ? 138 PHE B CE1 1 ATOM 3655 C CE2 . PHE B 2 138 ? -40.751 33.494 1.194 1.00 68.50 ? 138 PHE B CE2 1 ATOM 3656 C CZ . PHE B 2 138 ? -41.997 32.981 0.870 1.00 69.42 ? 138 PHE B CZ 1 ATOM 3657 N N . GLU B 2 139 ? -37.255 31.666 -4.578 1.00 70.93 ? 139 GLU B N 1 ATOM 3658 C CA . GLU B 2 139 ? -36.430 31.807 -5.776 1.00 72.49 ? 139 GLU B CA 1 ATOM 3659 C C . GLU B 2 139 ? -37.189 32.591 -6.842 1.00 72.35 ? 139 GLU B C 1 ATOM 3660 O O . GLU B 2 139 ? -38.259 32.174 -7.282 1.00 73.37 ? 139 GLU B O 1 ATOM 3661 C CB . GLU B 2 139 ? -36.063 30.423 -6.303 1.00 76.11 ? 139 GLU B CB 1 ATOM 3662 C CG . GLU B 2 139 ? -35.246 30.406 -7.582 1.00 79.89 ? 139 GLU B CG 1 ATOM 3663 C CD . GLU B 2 139 ? -34.863 28.993 -7.989 1.00 85.71 ? 139 GLU B CD 1 ATOM 3664 O OE1 . GLU B 2 139 ? -34.332 28.241 -7.140 1.00 88.21 ? 139 GLU B OE1 1 ATOM 3665 O OE2 . GLU B 2 139 ? -35.095 28.627 -9.160 1.00 90.49 ? 139 GLU B OE2 1 ATOM 3666 N N . PHE B 2 140 ? -36.621 33.716 -7.266 1.00 71.94 ? 140 PHE B N 1 ATOM 3667 C CA . PHE B 2 140 ? -37.301 34.631 -8.185 1.00 72.76 ? 140 PHE B CA 1 ATOM 3668 C C . PHE B 2 140 ? -37.272 34.135 -9.627 1.00 75.45 ? 140 PHE B C 1 ATOM 3669 O O . PHE B 2 140 ? -36.305 33.500 -10.055 1.00 73.94 ? 140 PHE B O 1 ATOM 3670 C CB . PHE B 2 140 ? -36.665 36.016 -8.128 1.00 70.72 ? 140 PHE B CB 1 ATOM 3671 C CG . PHE B 2 140 ? -36.860 36.715 -6.824 1.00 69.80 ? 140 PHE B CG 1 ATOM 3672 C CD1 . PHE B 2 140 ? -36.015 36.464 -5.756 1.00 68.82 ? 140 PHE B CD1 1 ATOM 3673 C CD2 . PHE B 2 140 ? -37.885 37.635 -6.665 1.00 71.16 ? 140 PHE B CD2 1 ATOM 3674 C CE1 . PHE B 2 140 ? -36.193 37.113 -4.548 1.00 68.81 ? 140 PHE B CE1 1 ATOM 3675 C CE2 . PHE B 2 140 ? -38.071 38.289 -5.460 1.00 71.21 ? 140 PHE B CE2 1 ATOM 3676 C CZ . PHE B 2 140 ? -37.224 38.026 -4.398 1.00 70.27 ? 140 PHE B CZ 1 ATOM 3677 N N . TYR B 2 141 ? -38.338 34.440 -10.367 1.00 78.82 ? 141 TYR B N 1 ATOM 3678 C CA . TYR B 2 141 ? -38.407 34.127 -11.798 1.00 82.89 ? 141 TYR B CA 1 ATOM 3679 C C . TYR B 2 141 ? -37.733 35.230 -12.605 1.00 84.95 ? 141 TYR B C 1 ATOM 3680 O O . TYR B 2 141 ? -36.943 34.958 -13.512 1.00 86.18 ? 141 TYR B O 1 ATOM 3681 C CB . TYR B 2 141 ? -39.858 33.941 -12.248 1.00 83.09 ? 141 TYR B CB 1 ATOM 3682 C CG . TYR B 2 141 ? -40.528 32.760 -11.587 1.00 83.06 ? 141 TYR B CG 1 ATOM 3683 C CD1 . TYR B 2 141 ? -39.983 31.482 -11.692 1.00 82.68 ? 141 TYR B CD1 1 ATOM 3684 C CD2 . TYR B 2 141 ? -41.689 32.921 -10.836 1.00 83.19 ? 141 TYR B CD2 1 ATOM 3685 C CE1 . TYR B 2 141 ? -40.581 30.395 -11.081 1.00 83.39 ? 141 TYR B CE1 1 ATOM 3686 C CE2 . TYR B 2 141 ? -42.296 31.840 -10.225 1.00 83.71 ? 141 TYR B CE2 1 ATOM 3687 C CZ . TYR B 2 141 ? -41.740 30.580 -10.350 1.00 84.70 ? 141 TYR B CZ 1 ATOM 3688 O OH . TYR B 2 141 ? -42.355 29.510 -9.738 1.00 87.32 ? 141 TYR B OH 1 ATOM 3689 N N . HIS B 2 142 ? -38.061 36.473 -12.272 1.00 101.76 ? 142 HIS B N 1 ATOM 3690 C CA . HIS B 2 142 ? -37.324 37.622 -12.782 1.00 104.12 ? 142 HIS B CA 1 ATOM 3691 C C . HIS B 2 142 ? -36.005 37.749 -12.024 1.00 101.40 ? 142 HIS B C 1 ATOM 3692 O O . HIS B 2 142 ? -35.845 37.201 -10.935 1.00 96.96 ? 142 HIS B O 1 ATOM 3693 C CB . HIS B 2 142 ? -38.152 38.911 -12.659 1.00 104.42 ? 142 HIS B CB 1 ATOM 3694 C CG . HIS B 2 142 ? -38.527 39.266 -11.253 1.00 100.02 ? 142 HIS B CG 1 ATOM 3695 N ND1 . HIS B 2 142 ? -37.864 40.234 -10.528 1.00 98.25 ? 142 HIS B ND1 1 ATOM 3696 C CD2 . HIS B 2 142 ? -39.497 38.785 -10.440 1.00 98.19 ? 142 HIS B CD2 1 ATOM 3697 C CE1 . HIS B 2 142 ? -38.411 40.332 -9.330 1.00 95.59 ? 142 HIS B CE1 1 ATOM 3698 N NE2 . HIS B 2 142 ? -39.402 39.463 -9.250 1.00 95.66 ? 142 HIS B NE2 1 ATOM 3699 N N . LYS B 2 143 ? -35.055 38.461 -12.615 1.00 103.83 ? 143 LYS B N 1 ATOM 3700 C CA . LYS B 2 143 ? -33.784 38.730 -11.959 1.00 102.25 ? 143 LYS B CA 1 ATOM 3701 C C . LYS B 2 143 ? -34.041 39.826 -10.922 1.00 96.38 ? 143 LYS B C 1 ATOM 3702 O O . LYS B 2 143 ? -34.861 40.714 -11.148 1.00 95.59 ? 143 LYS B O 1 ATOM 3703 C CB . LYS B 2 143 ? -32.733 39.146 -12.998 1.00 108.88 ? 143 LYS B CB 1 ATOM 3704 C CG . LYS B 2 143 ? -31.317 38.661 -12.712 1.00 111.06 ? 143 LYS B CG 1 ATOM 3705 C CD . LYS B 2 143 ? -30.461 39.742 -12.072 1.00 110.65 ? 143 LYS B CD 1 ATOM 3706 C CE . LYS B 2 143 ? -29.929 40.718 -13.111 1.00 114.59 ? 143 LYS B CE 1 ATOM 3707 N NZ . LYS B 2 143 ? -29.169 41.828 -12.473 1.00 113.17 ? 143 LYS B NZ 1 ATOM 3708 N N . CYS B 2 144 ? -33.367 39.747 -9.779 1.00 92.14 ? 144 CYS B N 1 ATOM 3709 C CA . CYS B 2 144 ? -33.674 40.619 -8.644 1.00 86.95 ? 144 CYS B CA 1 ATOM 3710 C C . CYS B 2 144 ? -32.405 41.232 -8.057 1.00 84.94 ? 144 CYS B C 1 ATOM 3711 O O . CYS B 2 144 ? -31.676 40.574 -7.321 1.00 84.06 ? 144 CYS B O 1 ATOM 3712 C CB . CYS B 2 144 ? -34.436 39.819 -7.579 1.00 83.53 ? 144 CYS B CB 1 ATOM 3713 S SG . CYS B 2 144 ? -35.086 40.783 -6.191 1.00 81.69 ? 144 CYS B SG 1 ATOM 3714 N N . ASP B 2 145 ? -32.145 42.495 -8.389 1.00 86.11 ? 145 ASP B N 1 ATOM 3715 C CA . ASP B 2 145 ? -30.955 43.204 -7.895 1.00 85.26 ? 145 ASP B CA 1 ATOM 3716 C C . ASP B 2 145 ? -31.163 43.697 -6.451 1.00 81.49 ? 145 ASP B C 1 ATOM 3717 O O . ASP B 2 145 ? -32.153 43.342 -5.819 1.00 79.08 ? 145 ASP B O 1 ATOM 3718 C CB . ASP B 2 145 ? -30.558 44.344 -8.856 1.00 87.80 ? 145 ASP B CB 1 ATOM 3719 C CG . ASP B 2 145 ? -31.611 45.440 -8.966 1.00 88.64 ? 145 ASP B CG 1 ATOM 3720 O OD1 . ASP B 2 145 ? -32.542 45.496 -8.137 1.00 85.40 ? 145 ASP B OD1 1 ATOM 3721 O OD2 . ASP B 2 145 ? -31.493 46.262 -9.899 1.00 93.83 ? 145 ASP B OD2 1 ATOM 3722 N N . ASN B 2 146 ? -30.236 44.501 -5.934 1.00 81.83 ? 146 ASN B N 1 ATOM 3723 C CA . ASN B 2 146 ? -30.300 44.957 -4.537 1.00 80.67 ? 146 ASN B CA 1 ATOM 3724 C C . ASN B 2 146 ? -31.473 45.888 -4.219 1.00 82.51 ? 146 ASN B C 1 ATOM 3725 O O . ASN B 2 146 ? -32.017 45.836 -3.115 1.00 82.66 ? 146 ASN B O 1 ATOM 3726 C CB . ASN B 2 146 ? -28.986 45.620 -4.121 1.00 79.97 ? 146 ASN B CB 1 ATOM 3727 C CG . ASN B 2 146 ? -27.809 44.660 -4.150 1.00 79.41 ? 146 ASN B CG 1 ATOM 3728 O OD1 . ASN B 2 146 ? -27.970 43.441 -4.252 1.00 78.89 ? 146 ASN B OD1 1 ATOM 3729 N ND2 . ASN B 2 146 ? -26.612 45.211 -4.063 1.00 80.43 ? 146 ASN B ND2 1 ATOM 3730 N N . GLU B 2 147 ? -31.859 46.734 -5.172 1.00 87.46 ? 147 GLU B N 1 ATOM 3731 C CA . GLU B 2 147 ? -33.088 47.529 -5.035 1.00 90.43 ? 147 GLU B CA 1 ATOM 3732 C C . GLU B 2 147 ? -34.305 46.609 -4.972 1.00 86.38 ? 147 GLU B C 1 ATOM 3733 O O . GLU B 2 147 ? -35.205 46.808 -4.157 1.00 85.75 ? 147 GLU B O 1 ATOM 3734 C CB . GLU B 2 147 ? -33.263 48.516 -6.201 1.00 97.80 ? 147 GLU B CB 1 ATOM 3735 C CG . GLU B 2 147 ? -32.456 49.798 -6.077 1.00 102.33 ? 147 GLU B CG 1 ATOM 3736 C CD . GLU B 2 147 ? -31.005 49.610 -6.468 1.00 105.67 ? 147 GLU B CD 1 ATOM 3737 O OE1 . GLU B 2 147 ? -30.731 49.441 -7.677 1.00 110.23 ? 147 GLU B OE1 1 ATOM 3738 O OE2 . GLU B 2 147 ? -30.140 49.632 -5.567 1.00 107.81 ? 147 GLU B OE2 1 ATOM 3739 N N . CYS B 2 148 ? -34.321 45.607 -5.847 1.00 84.27 ? 148 CYS B N 1 ATOM 3740 C CA . CYS B 2 148 ? -35.402 44.630 -5.896 1.00 82.21 ? 148 CYS B CA 1 ATOM 3741 C C . CYS B 2 148 ? -35.490 43.846 -4.590 1.00 78.26 ? 148 CYS B C 1 ATOM 3742 O O . CYS B 2 148 ? -36.585 43.568 -4.096 1.00 78.57 ? 148 CYS B O 1 ATOM 3743 C CB . CYS B 2 148 ? -35.199 43.679 -7.077 1.00 84.20 ? 148 CYS B CB 1 ATOM 3744 S SG . CYS B 2 148 ? -36.252 42.216 -7.054 1.00 84.93 ? 148 CYS B SG 1 ATOM 3745 N N . MET B 2 149 ? -34.333 43.496 -4.036 1.00 74.91 ? 149 MET B N 1 ATOM 3746 C CA . MET B 2 149 ? -34.276 42.857 -2.730 1.00 70.89 ? 149 MET B CA 1 ATOM 3747 C C . MET B 2 149 ? -34.778 43.822 -1.673 1.00 71.56 ? 149 MET B C 1 ATOM 3748 O O . MET B 2 149 ? -35.683 43.499 -0.909 1.00 70.99 ? 149 MET B O 1 ATOM 3749 C CB . MET B 2 149 ? -32.849 42.436 -2.402 1.00 69.32 ? 149 MET B CB 1 ATOM 3750 C CG . MET B 2 149 ? -32.299 41.347 -3.306 1.00 69.72 ? 149 MET B CG 1 ATOM 3751 S SD . MET B 2 149 ? -33.294 39.849 -3.277 1.00 68.84 ? 149 MET B SD 1 ATOM 3752 C CE . MET B 2 149 ? -32.265 38.730 -4.224 1.00 68.90 ? 149 MET B CE 1 ATOM 3753 N N . GLU B 2 150 ? -34.197 45.015 -1.645 1.00 74.05 ? 150 GLU B N 1 ATOM 3754 C CA . GLU B 2 150 ? -34.583 46.030 -0.670 1.00 76.73 ? 150 GLU B CA 1 ATOM 3755 C C . GLU B 2 150 ? -36.087 46.292 -0.686 1.00 77.52 ? 150 GLU B C 1 ATOM 3756 O O . GLU B 2 150 ? -36.682 46.494 0.367 1.00 77.47 ? 150 GLU B O 1 ATOM 3757 C CB . GLU B 2 150 ? -33.805 47.330 -0.912 1.00 80.44 ? 150 GLU B CB 1 ATOM 3758 C CG . GLU B 2 150 ? -34.117 48.469 0.056 1.00 83.75 ? 150 GLU B CG 1 ATOM 3759 C CD . GLU B 2 150 ? -33.805 48.146 1.509 1.00 84.15 ? 150 GLU B CD 1 ATOM 3760 O OE1 . GLU B 2 150 ? -32.923 47.299 1.775 1.00 83.06 ? 150 GLU B OE1 1 ATOM 3761 O OE2 . GLU B 2 150 ? -34.441 48.753 2.395 1.00 86.43 ? 150 GLU B OE2 1 ATOM 3762 N N . SER B 2 151 ? -36.696 46.272 -1.872 1.00 78.79 ? 151 SER B N 1 ATOM 3763 C CA . SER B 2 151 ? -38.134 46.522 -1.999 1.00 80.80 ? 151 SER B CA 1 ATOM 3764 C C . SER B 2 151 ? -38.968 45.428 -1.322 1.00 79.55 ? 151 SER B C 1 ATOM 3765 O O . SER B 2 151 ? -40.051 45.705 -0.801 1.00 80.65 ? 151 SER B O 1 ATOM 3766 C CB . SER B 2 151 ? -38.542 46.678 -3.471 1.00 82.31 ? 151 SER B CB 1 ATOM 3767 O OG . SER B 2 151 ? -38.557 45.435 -4.148 1.00 81.59 ? 151 SER B OG 1 ATOM 3768 N N . VAL B 2 152 ? -38.466 44.193 -1.333 1.00 77.43 ? 152 VAL B N 1 ATOM 3769 C CA . VAL B 2 152 ? -39.114 43.104 -0.599 1.00 76.48 ? 152 VAL B CA 1 ATOM 3770 C C . VAL B 2 152 ? -38.996 43.352 0.901 1.00 77.97 ? 152 VAL B C 1 ATOM 3771 O O . VAL B 2 152 ? -39.967 43.177 1.632 1.00 79.74 ? 152 VAL B O 1 ATOM 3772 C CB . VAL B 2 152 ? -38.509 41.725 -0.923 1.00 74.77 ? 152 VAL B CB 1 ATOM 3773 C CG1 . VAL B 2 152 ? -39.174 40.640 -0.084 1.00 73.37 ? 152 VAL B CG1 1 ATOM 3774 C CG2 . VAL B 2 152 ? -38.652 41.409 -2.405 1.00 75.33 ? 152 VAL B CG2 1 ATOM 3775 N N . ARG B 2 153 ? -37.812 43.763 1.353 1.00 79.29 ? 153 ARG B N 1 ATOM 3776 C CA . ARG B 2 153 ? -37.607 44.096 2.769 1.00 82.93 ? 153 ARG B CA 1 ATOM 3777 C C . ARG B 2 153 ? -38.401 45.335 3.188 1.00 87.80 ? 153 ARG B C 1 ATOM 3778 O O . ARG B 2 153 ? -38.845 45.427 4.326 1.00 88.64 ? 153 ARG B O 1 ATOM 3779 C CB . ARG B 2 153 ? -36.128 44.323 3.071 1.00 81.78 ? 153 ARG B CB 1 ATOM 3780 C CG . ARG B 2 153 ? -35.244 43.133 2.759 1.00 79.57 ? 153 ARG B CG 1 ATOM 3781 C CD . ARG B 2 153 ? -33.835 43.337 3.287 1.00 79.23 ? 153 ARG B CD 1 ATOM 3782 N NE . ARG B 2 153 ? -32.861 42.760 2.367 1.00 78.52 ? 153 ARG B NE 1 ATOM 3783 C CZ . ARG B 2 153 ? -32.161 43.438 1.460 1.00 79.42 ? 153 ARG B CZ 1 ATOM 3784 N NH1 . ARG B 2 153 ? -32.277 44.758 1.335 1.00 79.95 ? 153 ARG B NH1 1 ATOM 3785 N NH2 . ARG B 2 153 ? -31.317 42.783 0.673 1.00 80.94 ? 153 ARG B NH2 1 ATOM 3786 N N . ASN B 2 154 ? -38.548 46.285 2.264 1.00 93.99 ? 154 ASN B N 1 ATOM 3787 C CA . ASN B 2 154 ? -39.384 47.476 2.458 1.00 98.99 ? 154 ASN B CA 1 ATOM 3788 C C . ASN B 2 154 ? -40.831 47.152 2.776 1.00 98.34 ? 154 ASN B C 1 ATOM 3789 O O . ASN B 2 154 ? -41.431 47.757 3.661 1.00 100.50 ? 154 ASN B O 1 ATOM 3790 C CB . ASN B 2 154 ? -39.399 48.327 1.183 1.00 104.71 ? 154 ASN B CB 1 ATOM 3791 C CG . ASN B 2 154 ? -38.215 49.255 1.076 1.00 113.75 ? 154 ASN B CG 1 ATOM 3792 O OD1 . ASN B 2 154 ? -37.284 49.195 1.878 1.00 115.42 ? 154 ASN B OD1 1 ATOM 3793 N ND2 . ASN B 2 154 ? -38.246 50.129 0.073 1.00 124.24 ? 154 ASN B ND2 1 ATOM 3794 N N . GLY B 2 155 ? -41.381 46.195 2.035 1.00 95.33 ? 155 GLY B N 1 ATOM 3795 C CA . GLY B 2 155 ? -42.821 46.010 1.940 1.00 94.87 ? 155 GLY B CA 1 ATOM 3796 C C . GLY B 2 155 ? -43.357 46.713 0.703 1.00 95.74 ? 155 GLY B C 1 ATOM 3797 O O . GLY B 2 155 ? -44.566 46.814 0.524 1.00 97.14 ? 155 GLY B O 1 ATOM 3798 N N . THR B 2 156 ? -42.453 47.179 -0.159 1.00 96.40 ? 156 THR B N 1 ATOM 3799 C CA . THR B 2 156 ? -42.807 47.987 -1.322 1.00 99.94 ? 156 THR B CA 1 ATOM 3800 C C . THR B 2 156 ? -42.518 47.239 -2.617 1.00 99.76 ? 156 THR B C 1 ATOM 3801 O O . THR B 2 156 ? -42.203 47.848 -3.637 1.00 103.19 ? 156 THR B O 1 ATOM 3802 C CB . THR B 2 156 ? -42.003 49.306 -1.338 1.00 103.91 ? 156 THR B CB 1 ATOM 3803 O OG1 . THR B 2 156 ? -41.958 49.861 -0.019 1.00 105.44 ? 156 THR B OG1 1 ATOM 3804 C CG2 . THR B 2 156 ? -42.625 50.333 -2.305 1.00 109.30 ? 156 THR B CG2 1 ATOM 3805 N N . TYR B 2 157 ? -42.622 45.918 -2.582 1.00 98.02 ? 157 TYR B N 1 ATOM 3806 C CA . TYR B 2 157 ? -42.368 45.122 -3.772 1.00 98.30 ? 157 TYR B CA 1 ATOM 3807 C C . TYR B 2 157 ? -43.618 45.111 -4.640 1.00 105.26 ? 157 TYR B C 1 ATOM 3808 O O . TYR B 2 157 ? -44.631 44.514 -4.272 1.00 103.82 ? 157 TYR B O 1 ATOM 3809 C CB . TYR B 2 157 ? -41.971 43.701 -3.389 1.00 93.55 ? 157 TYR B CB 1 ATOM 3810 C CG . TYR B 2 157 ? -41.828 42.775 -4.569 1.00 89.63 ? 157 TYR B CG 1 ATOM 3811 C CD1 . TYR B 2 157 ? -40.641 42.710 -5.289 1.00 87.16 ? 157 TYR B CD1 1 ATOM 3812 C CD2 . TYR B 2 157 ? -42.884 41.962 -4.964 1.00 88.25 ? 157 TYR B CD2 1 ATOM 3813 C CE1 . TYR B 2 157 ? -40.511 41.856 -6.370 1.00 86.79 ? 157 TYR B CE1 1 ATOM 3814 C CE2 . TYR B 2 157 ? -42.763 41.108 -6.042 1.00 87.47 ? 157 TYR B CE2 1 ATOM 3815 C CZ . TYR B 2 157 ? -41.577 41.058 -6.741 1.00 86.60 ? 157 TYR B CZ 1 ATOM 3816 O OH . TYR B 2 157 ? -41.471 40.204 -7.810 1.00 87.10 ? 157 TYR B OH 1 ATOM 3817 N N . ASP B 2 158 ? -43.540 45.775 -5.788 1.00 116.14 ? 158 ASP B N 1 ATOM 3818 C CA . ASP B 2 158 ? -44.680 45.874 -6.702 1.00 128.48 ? 158 ASP B CA 1 ATOM 3819 C C . ASP B 2 158 ? -44.829 44.620 -7.556 1.00 135.82 ? 158 ASP B C 1 ATOM 3820 O O . ASP B 2 158 ? -43.939 44.282 -8.336 1.00 137.80 ? 158 ASP B O 1 ATOM 3821 C CB . ASP B 2 158 ? -44.551 47.100 -7.621 1.00 131.62 ? 158 ASP B CB 1 ATOM 3822 C CG . ASP B 2 158 ? -45.104 48.366 -6.994 1.00 133.52 ? 158 ASP B CG 1 ATOM 3823 O OD1 . ASP B 2 158 ? -46.234 48.326 -6.457 1.00 134.37 ? 158 ASP B OD1 1 ATOM 3824 O OD2 . ASP B 2 158 ? -44.411 49.404 -7.043 1.00 132.56 ? 158 ASP B OD2 1 ATOM 3825 N N . TYR B 2 159 ? -45.961 43.939 -7.401 1.00 143.86 ? 159 TYR B N 1 ATOM 3826 C CA . TYR B 2 159 ? -46.338 42.846 -8.296 1.00 151.97 ? 159 TYR B CA 1 ATOM 3827 C C . TYR B 2 159 ? -46.473 43.320 -9.757 1.00 161.04 ? 159 TYR B C 1 ATOM 3828 O O . TYR B 2 159 ? -45.938 42.669 -10.658 1.00 161.31 ? 159 TYR B O 1 ATOM 3829 C CB . TYR B 2 159 ? -47.634 42.172 -7.806 1.00 153.89 ? 159 TYR B CB 1 ATOM 3830 C CG . TYR B 2 159 ? -48.347 41.328 -8.844 1.00 159.45 ? 159 TYR B CG 1 ATOM 3831 C CD1 . TYR B 2 159 ? -49.265 41.900 -9.728 1.00 164.78 ? 159 TYR B CD1 1 ATOM 3832 C CD2 . TYR B 2 159 ? -48.117 39.959 -8.935 1.00 159.11 ? 159 TYR B CD2 1 ATOM 3833 C CE1 . TYR B 2 159 ? -49.920 41.134 -10.680 1.00 168.52 ? 159 TYR B CE1 1 ATOM 3834 C CE2 . TYR B 2 159 ? -48.770 39.184 -9.881 1.00 163.27 ? 159 TYR B CE2 1 ATOM 3835 C CZ . TYR B 2 159 ? -49.671 39.775 -10.751 1.00 168.72 ? 159 TYR B CZ 1 ATOM 3836 O OH . TYR B 2 159 ? -50.324 39.012 -11.694 1.00 170.63 ? 159 TYR B OH 1 ATOM 3837 N N . PRO B 2 160 ? -47.180 44.452 -9.996 1.00 169.35 ? 160 PRO B N 1 ATOM 3838 C CA . PRO B 2 160 ? -47.392 44.935 -11.376 1.00 173.51 ? 160 PRO B CA 1 ATOM 3839 C C . PRO B 2 160 ? -46.115 45.303 -12.141 1.00 171.21 ? 160 PRO B C 1 ATOM 3840 O O . PRO B 2 160 ? -46.092 45.206 -13.370 1.00 171.94 ? 160 PRO B O 1 ATOM 3841 C CB . PRO B 2 160 ? -48.267 46.186 -11.189 1.00 177.89 ? 160 PRO B CB 1 ATOM 3842 C CG . PRO B 2 160 ? -48.881 46.039 -9.842 1.00 175.84 ? 160 PRO B CG 1 ATOM 3843 C CD . PRO B 2 160 ? -47.855 45.325 -9.016 1.00 171.00 ? 160 PRO B CD 1 ATOM 3844 N N . GLN B 2 161 ? -45.079 45.734 -11.422 1.00 165.08 ? 161 GLN B N 1 ATOM 3845 C CA . GLN B 2 161 ? -43.791 46.081 -12.036 1.00 162.28 ? 161 GLN B CA 1 ATOM 3846 C C . GLN B 2 161 ? -43.066 44.845 -12.577 1.00 159.08 ? 161 GLN B C 1 ATOM 3847 O O . GLN B 2 161 ? -42.306 44.942 -13.542 1.00 162.08 ? 161 GLN B O 1 ATOM 3848 C CB . GLN B 2 161 ? -42.896 46.813 -11.029 1.00 156.92 ? 161 GLN B CB 1 ATOM 3849 C CG . GLN B 2 161 ? -41.609 47.376 -11.622 1.00 154.93 ? 161 GLN B CG 1 ATOM 3850 C CD . GLN B 2 161 ? -40.773 48.135 -10.608 1.00 150.38 ? 161 GLN B CD 1 ATOM 3851 O OE1 . GLN B 2 161 ? -41.253 48.503 -9.537 1.00 147.88 ? 161 GLN B OE1 1 ATOM 3852 N NE2 . GLN B 2 161 ? -39.510 48.373 -10.944 1.00 148.85 ? 161 GLN B NE2 1 ATOM 3853 N N . TYR B 2 162 ? -43.297 43.695 -11.946 1.00 151.75 ? 162 TYR B N 1 ATOM 3854 C CA . TYR B 2 162 ? -42.736 42.426 -12.401 1.00 148.19 ? 162 TYR B CA 1 ATOM 3855 C C . TYR B 2 162 ? -43.872 41.469 -12.763 1.00 143.12 ? 162 TYR B C 1 ATOM 3856 O O . TYR B 2 162 ? -43.702 40.546 -13.561 1.00 137.40 ? 162 TYR B O 1 ATOM 3857 C CB . TYR B 2 162 ? -41.850 41.813 -11.312 1.00 145.70 ? 162 TYR B CB 1 ATOM 3858 C CG . TYR B 2 162 ? -40.811 42.757 -10.730 1.00 146.06 ? 162 TYR B CG 1 ATOM 3859 C CD1 . TYR B 2 162 ? -39.596 42.982 -11.378 1.00 147.78 ? 162 TYR B CD1 1 ATOM 3860 C CD2 . TYR B 2 162 ? -41.038 43.413 -9.521 1.00 143.20 ? 162 TYR B CD2 1 ATOM 3861 C CE1 . TYR B 2 162 ? -38.646 43.840 -10.842 1.00 145.90 ? 162 TYR B CE1 1 ATOM 3862 C CE2 . TYR B 2 162 ? -40.095 44.272 -8.978 1.00 141.71 ? 162 TYR B CE2 1 ATOM 3863 C CZ . TYR B 2 162 ? -38.902 44.482 -9.640 1.00 143.27 ? 162 TYR B CZ 1 ATOM 3864 O OH . TYR B 2 162 ? -37.969 45.335 -9.097 1.00 141.51 ? 162 TYR B OH 1 HETATM 3865 C C1 . SIA C 3 . ? -22.906 29.585 96.093 1.00 90.29 ? 1322 SIA A C1 1 HETATM 3866 C C2 . SIA C 3 . ? -23.142 29.141 97.522 1.00 86.71 ? 1322 SIA A C2 1 HETATM 3867 C C3 . SIA C 3 . ? -22.303 30.041 98.437 1.00 83.32 ? 1322 SIA A C3 1 HETATM 3868 C C4 . SIA C 3 . ? -22.838 31.471 98.398 1.00 81.16 ? 1322 SIA A C4 1 HETATM 3869 C C5 . SIA C 3 . ? -24.304 31.473 98.802 1.00 79.16 ? 1322 SIA A C5 1 HETATM 3870 C C6 . SIA C 3 . ? -25.118 30.541 97.907 1.00 78.46 ? 1322 SIA A C6 1 HETATM 3871 C C7 . SIA C 3 . ? -26.578 30.404 98.333 1.00 76.58 ? 1322 SIA A C7 1 HETATM 3872 C C8 . SIA C 3 . ? -27.295 29.243 97.650 1.00 75.16 ? 1322 SIA A C8 1 HETATM 3873 C C9 . SIA C 3 . ? -28.802 29.438 97.745 1.00 73.74 ? 1322 SIA A C9 1 HETATM 3874 C C10 . SIA C 3 . ? -25.752 33.402 99.217 1.00 82.72 ? 1322 SIA A C10 1 HETATM 3875 C C11 . SIA C 3 . ? -26.059 34.824 98.842 1.00 83.77 ? 1322 SIA A C11 1 HETATM 3876 N N5 . SIA C 3 . ? -24.741 32.840 98.561 1.00 80.24 ? 1322 SIA A N5 1 HETATM 3877 O O1A . SIA C 3 . ? -21.722 29.767 95.720 1.00 91.10 ? 1322 SIA A O1A 1 HETATM 3878 O O1B . SIA C 3 . ? -23.884 29.751 95.328 1.00 93.12 ? 1322 SIA A O1B 1 HETATM 3879 O O4 . SIA C 3 . ? -22.107 32.332 99.278 1.00 81.45 ? 1322 SIA A O4 1 HETATM 3880 O O6 . SIA C 3 . ? -24.527 29.236 97.894 1.00 81.52 ? 1322 SIA A O6 1 HETATM 3881 O O7 . SIA C 3 . ? -26.659 30.213 99.746 1.00 80.21 ? 1322 SIA A O7 1 HETATM 3882 O O8 . SIA C 3 . ? -26.923 29.155 96.271 1.00 75.17 ? 1322 SIA A O8 1 HETATM 3883 O O9 . SIA C 3 . ? -29.490 28.314 97.181 1.00 73.42 ? 1322 SIA A O9 1 HETATM 3884 O O10 . SIA C 3 . ? -26.400 32.802 100.060 1.00 81.77 ? 1322 SIA A O10 1 HETATM 3885 C C1 . GAL D 4 . ? -22.045 25.095 100.105 1.00 96.80 ? 1323 GAL A C1 1 HETATM 3886 C C2 . GAL D 4 . ? -21.823 26.015 98.906 1.00 95.78 ? 1323 GAL A C2 1 HETATM 3887 C C3 . GAL D 4 . ? -22.955 27.027 98.773 1.00 93.35 ? 1323 GAL A C3 1 HETATM 3888 C C4 . GAL D 4 . ? -24.315 26.328 98.792 1.00 91.24 ? 1323 GAL A C4 1 HETATM 3889 C C5 . GAL D 4 . ? -24.397 25.383 99.998 1.00 92.20 ? 1323 GAL A C5 1 HETATM 3890 C C6 . GAL D 4 . ? -25.758 24.684 100.097 1.00 91.65 ? 1323 GAL A C6 1 HETATM 3891 O O2 . GAL D 4 . ? -20.584 26.720 99.038 1.00 95.24 ? 1323 GAL A O2 1 HETATM 3892 O O3 . GAL D 4 . ? -22.737 27.761 97.562 1.00 89.27 ? 1323 GAL A O3 1 HETATM 3893 O O4 . GAL D 4 . ? -24.513 25.625 97.562 1.00 88.17 ? 1323 GAL A O4 1 HETATM 3894 O O5 . GAL D 4 . ? -23.311 24.445 99.947 1.00 95.35 ? 1323 GAL A O5 1 HETATM 3895 O O6 . GAL D 4 . ? -25.624 23.256 100.114 1.00 86.60 ? 1323 GAL A O6 1 HETATM 3896 C C1 . NAG E 5 . ? -19.315 23.228 103.476 1.00 102.46 ? 1324 NAG A C1 1 HETATM 3897 C C2 . NAG E 5 . ? -19.633 24.053 102.227 1.00 100.98 ? 1324 NAG A C2 1 HETATM 3898 C C3 . NAG E 5 . ? -20.827 23.487 101.453 1.00 101.70 ? 1324 NAG A C3 1 HETATM 3899 C C4 . NAG E 5 . ? -20.625 21.995 101.198 1.00 101.54 ? 1324 NAG A C4 1 HETATM 3900 C C5 . NAG E 5 . ? -20.189 21.243 102.458 1.00 102.77 ? 1324 NAG A C5 1 HETATM 3901 C C6 . NAG E 5 . ? -19.810 19.807 102.113 1.00 103.72 ? 1324 NAG A C6 1 HETATM 3902 C C7 . NAG E 5 . ? -19.234 26.454 102.570 1.00 99.83 ? 1324 NAG A C7 1 HETATM 3903 C C8 . NAG E 5 . ? -19.800 27.740 103.105 1.00 97.66 ? 1324 NAG A C8 1 HETATM 3904 N N2 . NAG E 5 . ? -20.022 25.382 102.694 1.00 99.85 ? 1324 NAG A N2 1 HETATM 3905 O O1 . NAG E 5 . ? -18.169 23.756 104.152 1.00 98.35 ? 1324 NAG A O1 1 HETATM 3906 O O3 . NAG E 5 . ? -20.983 24.137 100.183 1.00 100.68 ? 1324 NAG A O3 1 HETATM 3907 O O4 . NAG E 5 . ? -21.844 21.436 100.691 1.00 95.81 ? 1324 NAG A O4 1 HETATM 3908 O O5 . NAG E 5 . ? -19.067 21.875 103.085 1.00 103.47 ? 1324 NAG A O5 1 HETATM 3909 O O6 . NAG E 5 . ? -20.965 19.100 101.648 1.00 104.11 ? 1324 NAG A O6 1 HETATM 3910 O O7 . NAG E 5 . ? -18.125 26.409 102.056 1.00 98.06 ? 1324 NAG A O7 1 HETATM 3911 C C1 . NAG F 5 . ? -45.471 59.314 88.993 1.00 85.93 ? 1325 NAG A C1 1 HETATM 3912 C C2 . NAG F 5 . ? -45.700 60.699 88.382 1.00 94.24 ? 1325 NAG A C2 1 HETATM 3913 C C3 . NAG F 5 . ? -47.156 61.147 88.541 1.00 97.49 ? 1325 NAG A C3 1 HETATM 3914 C C4 . NAG F 5 . ? -48.130 60.005 88.254 1.00 96.74 ? 1325 NAG A C4 1 HETATM 3915 C C5 . NAG F 5 . ? -47.745 58.809 89.114 1.00 93.82 ? 1325 NAG A C5 1 HETATM 3916 C C6 . NAG F 5 . ? -48.732 57.649 89.034 1.00 93.68 ? 1325 NAG A C6 1 HETATM 3917 C C7 . NAG F 5 . ? -44.278 62.768 88.551 1.00 108.86 ? 1325 NAG A C7 1 HETATM 3918 C C8 . NAG F 5 . ? -44.486 63.162 87.112 1.00 112.19 ? 1325 NAG A C8 1 HETATM 3919 N N2 . NAG F 5 . ? -44.840 61.658 89.067 1.00 101.03 ? 1325 NAG A N2 1 HETATM 3920 O O3 . NAG F 5 . ? -47.439 62.219 87.667 1.00 107.29 ? 1325 NAG A O3 1 HETATM 3921 O O4 . NAG F 5 . ? -49.460 60.409 88.497 1.00 97.95 ? 1325 NAG A O4 1 HETATM 3922 O O5 . NAG F 5 . ? -46.484 58.400 88.633 1.00 90.10 ? 1325 NAG A O5 1 HETATM 3923 O O6 . NAG F 5 . ? -48.312 56.645 89.928 1.00 93.06 ? 1325 NAG A O6 1 HETATM 3924 O O7 . NAG F 5 . ? -43.566 63.504 89.244 1.00 105.17 ? 1325 NAG A O7 1 HETATM 3925 C C1 . NAG G 5 . ? -48.218 63.277 88.275 1.00 120.17 ? 1326 NAG A C1 1 HETATM 3926 C C2 . NAG G 5 . ? -48.787 64.120 87.138 1.00 123.76 ? 1326 NAG A C2 1 HETATM 3927 C C3 . NAG G 5 . ? -49.659 65.253 87.666 1.00 127.13 ? 1326 NAG A C3 1 HETATM 3928 C C4 . NAG G 5 . ? -50.689 64.742 88.668 1.00 129.64 ? 1326 NAG A C4 1 HETATM 3929 C C5 . NAG G 5 . ? -50.031 63.860 89.728 1.00 128.58 ? 1326 NAG A C5 1 HETATM 3930 C C6 . NAG G 5 . ? -51.090 63.237 90.637 1.00 126.83 ? 1326 NAG A C6 1 HETATM 3931 C C7 . NAG G 5 . ? -47.562 64.399 85.024 1.00 126.44 ? 1326 NAG A C7 1 HETATM 3932 C C8 . NAG G 5 . ? -46.392 65.031 84.322 1.00 125.38 ? 1326 NAG A C8 1 HETATM 3933 N N2 . NAG G 5 . ? -47.706 64.661 86.327 1.00 125.75 ? 1326 NAG A N2 1 HETATM 3934 O O3 . NAG G 5 . ? -50.325 65.867 86.588 1.00 127.98 ? 1326 NAG A O3 1 HETATM 3935 O O4 . NAG G 5 . ? -51.340 65.843 89.269 1.00 132.11 ? 1326 NAG A O4 1 HETATM 3936 O O5 . NAG G 5 . ? -49.277 62.831 89.107 1.00 126.50 ? 1326 NAG A O5 1 HETATM 3937 O O6 . NAG G 5 . ? -50.469 62.503 91.666 1.00 123.93 ? 1326 NAG A O6 1 HETATM 3938 O O7 . NAG G 5 . ? -48.328 63.678 84.385 1.00 125.43 ? 1326 NAG A O7 1 HETATM 3939 C C1 . NAG H 5 . ? -30.358 18.398 31.874 1.00 76.55 ? 1327 NAG A C1 1 HETATM 3940 C C2 . NAG H 5 . ? -30.551 16.912 32.199 1.00 84.54 ? 1327 NAG A C2 1 HETATM 3941 C C3 . NAG H 5 . ? -29.955 16.537 33.556 1.00 86.21 ? 1327 NAG A C3 1 HETATM 3942 C C4 . NAG H 5 . ? -28.532 17.056 33.688 1.00 86.95 ? 1327 NAG A C4 1 HETATM 3943 C C5 . NAG H 5 . ? -28.597 18.570 33.485 1.00 83.53 ? 1327 NAG A C5 1 HETATM 3944 C C6 . NAG H 5 . ? -27.276 19.288 33.767 1.00 82.51 ? 1327 NAG A C6 1 HETATM 3945 C C7 . NAG H 5 . ? -32.611 15.979 31.220 1.00 85.22 ? 1327 NAG A C7 1 HETATM 3946 C C8 . NAG H 5 . ? -34.070 15.682 31.426 1.00 84.32 ? 1327 NAG A C8 1 HETATM 3947 N N2 . NAG H 5 . ? -31.965 16.563 32.233 1.00 86.89 ? 1327 NAG A N2 1 HETATM 3948 O O3 . NAG H 5 . ? -29.985 15.141 33.749 1.00 85.24 ? 1327 NAG A O3 1 HETATM 3949 O O4 . NAG H 5 . ? -28.026 16.679 34.953 1.00 90.85 ? 1327 NAG A O4 1 HETATM 3950 O O5 . NAG H 5 . ? -29.022 18.798 32.152 1.00 79.71 ? 1327 NAG A O5 1 HETATM 3951 O O6 . NAG H 5 . ? -26.634 19.651 32.567 1.00 83.93 ? 1327 NAG A O6 1 HETATM 3952 O O7 . NAG H 5 . ? -32.077 15.688 30.151 1.00 83.90 ? 1327 NAG A O7 1 HETATM 3953 S S1 . MPO I 6 . ? -28.510 30.738 3.984 1.00 132.15 ? 1163 MPO B S1 1 HETATM 3954 O O1 . MPO I 6 . ? -29.414 31.699 3.416 1.00 132.89 ? 1163 MPO B O1 1 HETATM 3955 O O2 . MPO I 6 . ? -28.056 31.219 5.257 1.00 137.28 ? 1163 MPO B O2 1 HETATM 3956 O O4 . MPO I 6 . ? -30.233 24.248 2.667 1.00 122.51 ? 1163 MPO B O4 1 HETATM 3957 N N1 . MPO I 6 . ? -30.733 26.958 3.303 1.00 120.04 ? 1163 MPO B N1 1 HETATM 3958 C C1 . MPO I 6 . ? -29.290 29.287 4.191 1.00 123.92 ? 1163 MPO B C1 1 HETATM 3959 O O3 . MPO I 6 . ? -27.212 30.527 3.006 1.00 129.87 ? 1163 MPO B O3 1 HETATM 3960 C C2 . MPO I 6 . ? -30.744 29.362 3.735 1.00 114.86 ? 1163 MPO B C2 1 HETATM 3961 C C3 . MPO I 6 . ? -31.441 28.039 4.011 1.00 115.58 ? 1163 MPO B C3 1 HETATM 3962 C C4 . MPO I 6 . ? -31.667 26.196 2.459 1.00 120.46 ? 1163 MPO B C4 1 HETATM 3963 C C5 . MPO I 6 . ? -30.928 25.075 1.732 1.00 120.54 ? 1163 MPO B C5 1 HETATM 3964 C C6 . MPO I 6 . ? -29.309 24.977 3.477 1.00 122.05 ? 1163 MPO B C6 1 HETATM 3965 C C7 . MPO I 6 . ? -30.066 26.049 4.254 1.00 122.99 ? 1163 MPO B C7 1 HETATM 3966 C C1 . NAG J 5 . ? -37.193 51.089 -0.143 1.00 104.83 ? 1164 NAG B C1 1 HETATM 3967 C C2 . NAG J 5 . ? -37.806 52.489 -0.306 1.00 112.72 ? 1164 NAG B C2 1 HETATM 3968 C C3 . NAG J 5 . ? -38.003 52.935 -1.758 1.00 116.38 ? 1164 NAG B C3 1 HETATM 3969 C C4 . NAG J 5 . ? -36.858 52.460 -2.643 1.00 119.05 ? 1164 NAG B C4 1 HETATM 3970 C C5 . NAG J 5 . ? -36.713 50.950 -2.492 1.00 113.28 ? 1164 NAG B C5 1 HETATM 3971 C C6 . NAG J 5 . ? -35.687 50.335 -3.445 1.00 110.31 ? 1164 NAG B C6 1 HETATM 3972 C C7 . NAG J 5 . ? -39.202 52.650 1.749 1.00 112.09 ? 1164 NAG B C7 1 HETATM 3973 C C8 . NAG J 5 . ? -37.994 52.621 2.647 1.00 113.12 ? 1164 NAG B C8 1 HETATM 3974 N N2 . NAG J 5 . ? -39.073 52.590 0.417 1.00 111.04 ? 1164 NAG B N2 1 HETATM 3975 O O3 . NAG J 5 . ? -38.107 54.343 -1.816 1.00 113.42 ? 1164 NAG B O3 1 HETATM 3976 O O4 . NAG J 5 . ? -37.085 52.857 -3.986 1.00 124.76 ? 1164 NAG B O4 1 HETATM 3977 O O5 . NAG J 5 . ? -36.296 50.703 -1.169 1.00 110.27 ? 1164 NAG B O5 1 HETATM 3978 O O6 . NAG J 5 . ? -34.378 50.493 -2.941 1.00 103.31 ? 1164 NAG B O6 1 HETATM 3979 O O7 . NAG J 5 . ? -40.312 52.731 2.270 1.00 110.16 ? 1164 NAG B O7 1 HETATM 3980 C C1 . NAG K 5 . ? -35.981 53.642 -4.485 1.00 127.56 ? 1165 NAG B C1 1 HETATM 3981 C C2 . NAG K 5 . ? -36.190 53.888 -5.982 1.00 127.75 ? 1165 NAG B C2 1 HETATM 3982 C C3 . NAG K 5 . ? -35.301 55.010 -6.547 1.00 132.23 ? 1165 NAG B C3 1 HETATM 3983 C C4 . NAG K 5 . ? -35.122 56.180 -5.577 1.00 132.76 ? 1165 NAG B C4 1 HETATM 3984 C C5 . NAG K 5 . ? -34.742 55.630 -4.207 1.00 133.30 ? 1165 NAG B C5 1 HETATM 3985 C C6 . NAG K 5 . ? -34.429 56.718 -3.182 1.00 131.63 ? 1165 NAG B C6 1 HETATM 3986 C C7 . NAG K 5 . ? -36.878 51.686 -6.859 1.00 119.45 ? 1165 NAG B C7 1 HETATM 3987 C C8 . NAG K 5 . ? -36.471 50.464 -7.632 1.00 118.27 ? 1165 NAG B C8 1 HETATM 3988 N N2 . NAG K 5 . ? -35.953 52.643 -6.707 1.00 123.75 ? 1165 NAG B N2 1 HETATM 3989 O O3 . NAG K 5 . ? -35.833 55.483 -7.767 1.00 132.39 ? 1165 NAG B O3 1 HETATM 3990 O O4 . NAG K 5 . ? -34.135 57.070 -6.056 1.00 130.62 ? 1165 NAG B O4 1 HETATM 3991 O O5 . NAG K 5 . ? -35.837 54.855 -3.768 1.00 130.33 ? 1165 NAG B O5 1 HETATM 3992 O O6 . NAG K 5 . ? -35.582 57.487 -2.934 1.00 130.66 ? 1165 NAG B O6 1 HETATM 3993 O O7 . NAG K 5 . ? -38.019 51.753 -6.403 1.00 114.51 ? 1165 NAG B O7 1 HETATM 3994 O O . HOH L 7 . ? -34.396 30.341 5.056 1.00 63.50 ? 2001 HOH A O 1 HETATM 3995 O O . HOH L 7 . ? -32.336 30.987 9.898 1.00 51.26 ? 2002 HOH A O 1 HETATM 3996 O O . HOH L 7 . ? -31.140 29.814 16.339 1.00 45.10 ? 2003 HOH A O 1 HETATM 3997 O O . HOH L 7 . ? -25.420 37.395 20.718 1.00 58.93 ? 2004 HOH A O 1 HETATM 3998 O O . HOH L 7 . ? -34.665 41.180 27.459 1.00 46.33 ? 2005 HOH A O 1 HETATM 3999 O O . HOH L 7 . ? -21.913 34.018 19.054 1.00 45.16 ? 2006 HOH A O 1 HETATM 4000 O O . HOH L 7 . ? -18.425 31.260 17.868 1.00 60.95 ? 2007 HOH A O 1 HETATM 4001 O O . HOH L 7 . ? -32.135 23.715 31.448 1.00 60.02 ? 2008 HOH A O 1 HETATM 4002 O O . HOH L 7 . ? -35.352 27.264 32.467 1.00 43.54 ? 2009 HOH A O 1 HETATM 4003 O O . HOH L 7 . ? -33.157 20.435 33.503 1.00 57.91 ? 2010 HOH A O 1 HETATM 4004 O O . HOH L 7 . ? -48.374 21.554 25.390 1.00 49.81 ? 2011 HOH A O 1 HETATM 4005 O O . HOH L 7 . ? -40.682 21.263 22.898 1.00 59.67 ? 2012 HOH A O 1 HETATM 4006 O O . HOH L 7 . ? -36.469 16.887 27.983 1.00 64.72 ? 2013 HOH A O 1 HETATM 4007 O O . HOH L 7 . ? -22.620 50.172 84.077 1.00 64.55 ? 2014 HOH A O 1 HETATM 4008 O O . HOH L 7 . ? -31.694 24.086 21.321 1.00 63.98 ? 2015 HOH A O 1 HETATM 4009 O O . HOH L 7 . ? -31.244 41.005 23.932 1.00 62.11 ? 2016 HOH A O 1 HETATM 4010 O O . HOH L 7 . ? -34.945 42.090 30.729 1.00 69.97 ? 2017 HOH A O 1 HETATM 4011 O O . HOH L 7 . ? -28.333 35.468 33.237 1.00 62.13 ? 2018 HOH A O 1 HETATM 4012 O O . HOH L 7 . ? -30.731 29.787 38.072 1.00 55.54 ? 2019 HOH A O 1 HETATM 4013 O O . HOH L 7 . ? -48.753 31.361 73.563 1.00 59.18 ? 2020 HOH A O 1 HETATM 4014 O O . HOH L 7 . ? -25.213 37.535 46.846 1.00 62.05 ? 2021 HOH A O 1 HETATM 4015 O O . HOH L 7 . ? -19.150 31.911 50.020 1.00 61.18 ? 2022 HOH A O 1 HETATM 4016 O O . HOH L 7 . ? -18.379 36.527 59.296 1.00 63.43 ? 2023 HOH A O 1 HETATM 4017 O O . HOH L 7 . ? -25.540 43.642 80.804 1.00 63.56 ? 2024 HOH A O 1 HETATM 4018 O O . HOH L 7 . ? -18.684 40.210 77.924 1.00 64.60 ? 2025 HOH A O 1 HETATM 4019 O O . HOH L 7 . ? -24.629 51.644 83.664 1.00 50.30 ? 2026 HOH A O 1 HETATM 4020 O O . HOH L 7 . ? -31.651 32.859 74.451 1.00 48.97 ? 2027 HOH A O 1 HETATM 4021 O O . HOH L 7 . ? -24.304 27.075 69.629 1.00 65.76 ? 2028 HOH A O 1 HETATM 4022 O O . HOH L 7 . ? -33.430 29.823 79.551 1.00 59.68 ? 2029 HOH A O 1 HETATM 4023 O O . HOH L 7 . ? -42.933 33.485 76.441 1.00 53.81 ? 2030 HOH A O 1 HETATM 4024 O O . HOH L 7 . ? -44.335 38.343 81.789 1.00 67.51 ? 2031 HOH A O 1 HETATM 4025 O O . HOH L 7 . ? -47.964 33.780 71.988 1.00 45.46 ? 2032 HOH A O 1 HETATM 4026 O O . HOH L 7 . ? -31.235 25.034 59.474 1.00 77.04 ? 2033 HOH A O 1 HETATM 4027 O O . HOH L 7 . ? -31.208 23.828 52.226 1.00 75.31 ? 2034 HOH A O 1 HETATM 4028 O O . HOH L 7 . ? -34.191 48.973 102.786 1.00 40.21 ? 2035 HOH A O 1 HETATM 4029 O O . HOH L 7 . ? -26.303 40.895 99.676 1.00 62.56 ? 2036 HOH A O 1 HETATM 4030 O O . HOH L 7 . ? -22.166 42.231 89.839 1.00 61.07 ? 2037 HOH A O 1 HETATM 4031 O O . HOH L 7 . ? -18.086 45.837 86.506 1.00 57.34 ? 2038 HOH A O 1 HETATM 4032 O O . HOH L 7 . ? -27.884 45.837 116.149 1.00 74.28 ? 2039 HOH A O 1 HETATM 4033 O O . HOH L 7 . ? -42.549 55.465 78.905 1.00 62.06 ? 2040 HOH A O 1 HETATM 4034 O O . HOH L 7 . ? -28.033 26.369 96.021 1.00 75.54 ? 2041 HOH A O 1 HETATM 4035 O O . HOH L 7 . ? -51.579 40.330 87.362 1.00 77.50 ? 2042 HOH A O 1 HETATM 4036 O O . HOH L 7 . ? -48.929 36.174 90.676 1.00 71.98 ? 2043 HOH A O 1 HETATM 4037 O O . HOH L 7 . ? -23.534 21.002 88.670 1.00 61.07 ? 2044 HOH A O 1 HETATM 4038 O O . HOH L 7 . ? -44.499 40.984 81.218 1.00 68.13 ? 2045 HOH A O 1 HETATM 4039 O O . HOH L 7 . ? -17.023 46.625 58.473 1.00 72.10 ? 2046 HOH A O 1 HETATM 4040 O O . HOH L 7 . ? -29.387 26.016 48.560 1.00 66.37 ? 2047 HOH A O 1 HETATM 4041 O O . HOH L 7 . ? -27.827 27.886 50.890 1.00 51.42 ? 2048 HOH A O 1 HETATM 4042 O O . HOH L 7 . ? -30.387 27.880 59.887 1.00 71.47 ? 2049 HOH A O 1 HETATM 4043 O O . HOH L 7 . ? -33.102 24.107 54.403 1.00 75.04 ? 2050 HOH A O 1 HETATM 4044 O O . HOH L 7 . ? -39.405 33.287 29.142 1.00 46.01 ? 2051 HOH A O 1 HETATM 4045 O O . HOH L 7 . ? -37.960 29.278 19.625 1.00 44.14 ? 2052 HOH A O 1 HETATM 4046 O O . HOH L 7 . ? -38.901 26.758 18.838 1.00 65.41 ? 2053 HOH A O 1 HETATM 4047 O O . HOH L 7 . ? -22.527 24.263 15.282 1.00 69.89 ? 2054 HOH A O 1 HETATM 4048 O O . HOH L 7 . ? -27.507 17.443 37.214 1.00 72.14 ? 2055 HOH A O 1 HETATM 4049 O O . HOH M 7 . ? -48.780 25.541 12.877 1.00 52.12 ? 2001 HOH B O 1 HETATM 4050 O O . HOH M 7 . ? -42.725 22.684 10.333 1.00 57.84 ? 2002 HOH B O 1 HETATM 4051 O O . HOH M 7 . ? -36.292 21.462 10.844 1.00 56.60 ? 2003 HOH B O 1 HETATM 4052 O O . HOH M 7 . ? -30.997 40.727 19.051 1.00 48.01 ? 2004 HOH B O 1 HETATM 4053 O O . HOH M 7 . ? -33.745 25.275 5.808 1.00 64.42 ? 2005 HOH B O 1 HETATM 4054 O O . HOH M 7 . ? -34.378 21.042 12.740 1.00 59.64 ? 2006 HOH B O 1 HETATM 4055 O O . HOH M 7 . ? -32.425 29.187 7.022 1.00 70.62 ? 2007 HOH B O 1 HETATM 4056 O O . HOH M 7 . ? -25.231 32.200 9.163 1.00 55.24 ? 2008 HOH B O 1 HETATM 4057 O O . HOH M 7 . ? -29.069 39.554 18.468 1.00 48.62 ? 2009 HOH B O 1 HETATM 4058 O O . HOH M 7 . ? -30.827 43.793 18.428 1.00 63.49 ? 2010 HOH B O 1 HETATM 4059 O O . HOH M 7 . ? -30.425 40.538 2.997 1.00 66.11 ? 2011 HOH B O 1 HETATM 4060 O O . HOH M 7 . ? -40.229 47.375 26.616 1.00 67.12 ? 2012 HOH B O 1 HETATM 4061 O O . HOH M 7 . ? -40.766 44.580 37.837 1.00 61.66 ? 2013 HOH B O 1 HETATM 4062 O O . HOH M 7 . ? -52.382 42.156 37.113 1.00 61.32 ? 2014 HOH B O 1 HETATM 4063 O O . HOH M 7 . ? -44.035 40.174 52.540 1.00 70.88 ? 2015 HOH B O 1 HETATM 4064 O O . HOH M 7 . ? -36.500 35.068 68.093 1.00 71.11 ? 2016 HOH B O 1 HETATM 4065 O O . HOH M 7 . ? -46.587 26.549 78.078 1.00 54.02 ? 2017 HOH B O 1 HETATM 4066 O O . HOH M 7 . ? -38.019 25.293 78.024 1.00 68.76 ? 2018 HOH B O 1 HETATM 4067 O O . HOH M 7 . ? -42.103 21.039 67.675 1.00 58.25 ? 2019 HOH B O 1 HETATM 4068 O O . HOH M 7 . ? -40.911 27.097 64.449 1.00 53.05 ? 2020 HOH B O 1 HETATM 4069 O O . HOH M 7 . ? -41.590 17.676 61.922 1.00 63.99 ? 2021 HOH B O 1 HETATM 4070 O O . HOH M 7 . ? -47.400 24.013 50.972 1.00 46.37 ? 2022 HOH B O 1 HETATM 4071 O O . HOH M 7 . ? -45.636 22.214 51.576 1.00 52.40 ? 2023 HOH B O 1 HETATM 4072 O O . HOH M 7 . ? -42.219 22.946 42.748 1.00 61.89 ? 2024 HOH B O 1 HETATM 4073 O O . HOH M 7 . ? -52.328 31.562 22.734 1.00 51.66 ? 2025 HOH B O 1 HETATM 4074 O O . HOH M 7 . ? -46.232 36.857 17.491 1.00 40.36 ? 2026 HOH B O 1 HETATM 4075 O O . HOH M 7 . ? -49.208 35.127 9.179 1.00 57.38 ? 2027 HOH B O 1 HETATM 4076 O O . HOH M 7 . ? -39.775 28.457 1.257 1.00 50.85 ? 2028 HOH B O 1 HETATM 4077 O O . HOH M 7 . ? -46.482 28.876 3.237 1.00 56.27 ? 2029 HOH B O 1 HETATM 4078 O O . HOH M 7 . ? -47.932 29.029 0.204 1.00 63.91 ? 2030 HOH B O 1 HETATM 4079 O O . HOH M 7 . ? -37.096 21.572 2.353 1.00 68.92 ? 2031 HOH B O 1 HETATM 4080 O O . HOH M 7 . ? -18.674 48.290 83.729 1.00 64.06 ? 2032 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 ? 0.7876 1.0664 0.6612 -0.1079 0.0378 0.0768 1 ASP A N 2 C CA . ASP A 1 ? 0.7906 1.0551 0.6606 -0.1211 0.0318 0.0783 1 ASP A CA 3 C C . ASP A 1 ? 0.7810 1.0192 0.6552 -0.1090 0.0301 0.0733 1 ASP A C 4 O O . ASP A 1 ? 0.7670 0.9823 0.6400 -0.0990 0.0304 0.0693 1 ASP A O 5 C CB . ASP A 1 ? 0.8187 1.0575 0.6719 -0.1390 0.0263 0.0812 1 ASP A CB 6 C CG . ASP A 1 ? 0.8444 1.1082 0.6904 -0.1556 0.0273 0.0867 1 ASP A CG 7 O OD1 . ASP A 1 ? 0.8442 1.1473 0.7002 -0.1501 0.0331 0.0877 1 ASP A OD1 8 O OD2 . ASP A 1 ? 0.8993 1.1431 0.7272 -0.1740 0.0224 0.0901 1 ASP A OD2 9 N N . GLN A 2 ? 0.7833 1.0267 0.6621 -0.1111 0.0282 0.0736 2 GLN A N 10 C CA . GLN A 2 ? 0.7764 0.9965 0.6587 -0.1014 0.0263 0.0691 2 GLN A CA 11 C C . GLN A 2 ? 0.7593 0.9728 0.6398 -0.1110 0.0214 0.0704 2 GLN A C 12 O O . GLN A 2 ? 0.7696 1.0042 0.6492 -0.1234 0.0206 0.0747 2 GLN A O 13 C CB . GLN A 2 ? 0.7820 1.0143 0.6739 -0.0830 0.0317 0.0655 2 GLN A CB 14 C CG . GLN A 2 ? 0.7881 1.0557 0.6875 -0.0799 0.0346 0.0678 2 GLN A CG 15 C CD . GLN A 2 ? 0.7855 1.0536 0.6886 -0.0599 0.0387 0.0637 2 GLN A CD 16 O OE1 . GLN A 2 ? 0.7854 1.0633 0.6934 -0.0557 0.0386 0.0634 2 GLN A OE1 17 N NE2 . GLN A 2 ? 0.7900 1.0448 0.6878 -0.0480 0.0421 0.0604 2 GLN A NE2 18 N N . ILE A 3 ? 0.7444 0.9295 0.6233 -0.1057 0.0182 0.0666 3 ILE A N 19 C CA . ILE A 3 ? 0.7406 0.9161 0.6176 -0.1113 0.0137 0.0669 3 ILE A CA 20 C C . ILE A 3 ? 0.7129 0.8850 0.6006 -0.0965 0.0155 0.0620 3 ILE A C 21 O O . ILE A 3 ? 0.7249 0.8842 0.6141 -0.0857 0.0170 0.0578 3 ILE A O 22 C CB . ILE A 3 ? 0.7562 0.8970 0.6154 -0.1202 0.0069 0.0673 3 ILE A CB 23 C CG1 . ILE A 3 ? 0.7708 0.9031 0.6235 -0.1293 0.0022 0.0688 3 ILE A CG1 24 C CG2 . ILE A 3 ? 0.7491 0.8655 0.6071 -0.1073 0.0057 0.0622 3 ILE A CG2 25 C CD1 . ILE A 3 ? 0.7909 0.8854 0.6197 -0.1373 -0.0048 0.0696 3 ILE A CD1 26 N N . CYS A 4 ? 0.6949 0.8793 0.5885 -0.0975 0.0152 0.0627 4 CYS A N 27 C CA . CYS A 4 ? 0.6819 0.8646 0.5841 -0.0847 0.0170 0.0586 4 CYS A CA 28 C C . CYS A 4 ? 0.6658 0.8329 0.5659 -0.0892 0.0120 0.0578 4 CYS A C 29 O O . CYS A 4 ? 0.6847 0.8518 0.5783 -0.1023 0.0082 0.0614 4 CYS A O 30 C CB . CYS A 4 ? 0.6874 0.9012 0.5984 -0.0778 0.0217 0.0598 4 CYS A CB 31 S SG . CYS A 4 ? 0.7164 0.9523 0.6277 -0.0698 0.0279 0.0609 4 CYS A SG 32 N N . ILE A 5 ? 0.6516 0.8052 0.5553 -0.0792 0.0121 0.0531 5 ILE A N 33 C CA . ILE A 5 ? 0.6429 0.7861 0.5465 -0.0808 0.0083 0.0519 5 ILE A CA 34 C C . ILE A 5 ? 0.6222 0.7826 0.5357 -0.0741 0.0115 0.0512 5 ILE A C 35 O O . ILE A 5 ? 0.6192 0.7848 0.5365 -0.0632 0.0160 0.0488 5 ILE A O 36 C CB . ILE A 5 ? 0.6517 0.7713 0.5520 -0.0744 0.0058 0.0470 5 ILE A CB 37 C CG1 . ILE A 5 ? 0.6723 0.7763 0.5617 -0.0771 0.0031 0.0472 5 ILE A CG1 38 C CG2 . ILE A 5 ? 0.6558 0.7647 0.5543 -0.0759 0.0016 0.0459 5 ILE A CG2 39 C CD1 . ILE A 5 ? 0.6871 0.7792 0.5623 -0.0889 -0.0020 0.0513 5 ILE A CD1 40 N N . GLY A 6 ? 0.6169 0.7840 0.5316 -0.0808 0.0089 0.0534 6 GLY A N 41 C CA . GLY A 6 ? 0.6050 0.7898 0.5282 -0.0744 0.0114 0.0532 6 GLY A CA 42 C C . GLY A 6 ? 0.5976 0.7786 0.5204 -0.0815 0.0071 0.0540 6 GLY A C 43 O O . GLY A 6 ? 0.6082 0.7689 0.5224 -0.0903 0.0021 0.0542 6 GLY A O 44 N N . TYR A 7 ? 0.5789 0.7783 0.5090 -0.0766 0.0089 0.0544 7 TYR A N 45 C CA . TYR A 7 ? 0.5778 0.7733 0.5083 -0.0817 0.0053 0.0545 7 TYR A CA 46 C C . TYR A 7 ? 0.5721 0.8011 0.5085 -0.0847 0.0064 0.0583 7 TYR A C 47 O O . TYR A 7 ? 0.5466 0.8032 0.4878 -0.0782 0.0105 0.0599 7 TYR A O 48 C CB . TYR A 7 ? 0.5820 0.7589 0.5148 -0.0704 0.0058 0.0493 7 TYR A CB 49 C CG . TYR A 7 ? 0.5801 0.7652 0.5169 -0.0554 0.0111 0.0469 7 TYR A CG 50 C CD1 . TYR A 7 ? 0.5675 0.7417 0.5006 -0.0477 0.0143 0.0441 7 TYR A CD1 51 C CD2 . TYR A 7 ? 0.5868 0.7882 0.5275 -0.0488 0.0127 0.0475 7 TYR A CD2 52 C CE1 . TYR A 7 ? 0.5789 0.7540 0.5092 -0.0345 0.0188 0.0420 7 TYR A CE1 53 C CE2 . TYR A 7 ? 0.5876 0.7905 0.5258 -0.0335 0.0172 0.0454 7 TYR A CE2 54 C CZ . TYR A 7 ? 0.5838 0.7714 0.5153 -0.0268 0.0202 0.0426 7 TYR A CZ 55 O OH . TYR A 7 ? 0.5789 0.7618 0.5018 -0.0121 0.0243 0.0404 7 TYR A OH 56 N N . HIS A 8 ? 0.5903 0.8175 0.5251 -0.0940 0.0024 0.0595 8 HIS A N 57 C CA . HIS A 8 ? 0.6025 0.8628 0.5415 -0.1009 0.0021 0.0635 8 HIS A CA 58 C C . HIS A 8 ? 0.5944 0.8772 0.5434 -0.0834 0.0063 0.0621 8 HIS A C 59 O O . HIS A 8 ? 0.5781 0.8417 0.5283 -0.0695 0.0079 0.0577 8 HIS A O 60 C CB . HIS A 8 ? 0.6157 0.8606 0.5475 -0.1149 -0.0036 0.0645 8 HIS A CB 61 C CG . HIS A 8 ? 0.6321 0.9103 0.5660 -0.1266 -0.0048 0.0689 8 HIS A CG 62 N ND1 . HIS A 8 ? 0.6452 0.9499 0.5743 -0.1438 -0.0055 0.0742 8 HIS A ND1 63 C CD2 . HIS A 8 ? 0.6285 0.9187 0.5676 -0.1251 -0.0058 0.0689 8 HIS A CD2 64 C CE1 . HIS A 8 ? 0.6418 0.9765 0.5736 -0.1528 -0.0068 0.0773 8 HIS A CE1 65 N NE2 . HIS A 8 ? 0.6399 0.9657 0.5780 -0.1410 -0.0070 0.0742 8 HIS A NE2 66 N N . ALA A 9 ? 0.6107 0.9352 0.5647 -0.0841 0.0082 0.0658 9 ALA A N 67 C CA . ALA A 9 ? 0.6104 0.9589 0.5708 -0.0672 0.0112 0.0651 9 ALA A CA 68 C C . ALA A 9 ? 0.6140 1.0056 0.5785 -0.0789 0.0095 0.0700 9 ALA A C 69 O O . ALA A 9 ? 0.6339 1.0423 0.5958 -0.0982 0.0076 0.0741 9 ALA A O 70 C CB . ALA A 9 ? 0.6068 0.9670 0.5670 -0.0474 0.0168 0.0637 9 ALA A CB 71 N N . ASN A 10 ? 0.6127 1.0220 0.5819 -0.0685 0.0099 0.0696 10 ASN A N 72 C CA . ASN A 10 ? 0.6269 1.0824 0.6005 -0.0786 0.0084 0.0741 10 ASN A CA 73 C C . ASN A 10 ? 0.6368 1.1220 0.6155 -0.0557 0.0113 0.0733 10 ASN A C 74 O O . ASN A 10 ? 0.6193 1.0878 0.5950 -0.0321 0.0149 0.0695 10 ASN A O 75 C CB . ASN A 10 ? 0.6335 1.0717 0.6031 -0.1016 0.0025 0.0755 10 ASN A CB 76 C CG . ASN A 10 ? 0.6376 1.0407 0.6070 -0.0922 0.0010 0.0713 10 ASN A CG 77 O OD1 . ASN A 10 ? 0.6385 1.0335 0.6107 -0.0698 0.0043 0.0676 10 ASN A OD1 78 N ND2 . ASN A 10 ? 0.6466 1.0266 0.6101 -0.1096 -0.0040 0.0717 10 ASN A ND2 79 N N . ASN A 11 ? 0.6673 1.1959 0.6510 -0.0627 0.0097 0.0768 11 ASN A N 80 C CA . ASN A 11 ? 0.6971 1.2604 0.6843 -0.0398 0.0121 0.0765 11 ASN A CA 81 C C . ASN A 11 ? 0.6961 1.2334 0.6824 -0.0331 0.0099 0.0737 11 ASN A C 82 O O . ASN A 11 ? 0.7082 1.2758 0.6968 -0.0198 0.0104 0.0743 11 ASN A O 83 C CB . ASN A 11 ? 0.7331 1.3670 0.7267 -0.0490 0.0118 0.0819 11 ASN A CB 84 C CG . ASN A 11 ? 0.7612 1.4051 0.7560 -0.0803 0.0063 0.0856 11 ASN A CG 85 O OD1 . ASN A 11 ? 0.7819 1.3787 0.7723 -0.0923 0.0027 0.0838 11 ASN A OD1 86 N ND2 . ASN A 11 ? 0.7626 1.4691 0.7615 -0.0940 0.0056 0.0906 11 ASN A ND2 87 N N . SER A 12 ? 0.6873 1.1701 0.6697 -0.0412 0.0077 0.0706 12 SER A N 88 C CA . SER A 12 ? 0.6788 1.1354 0.6603 -0.0396 0.0051 0.0681 12 SER A CA 89 C C . SER A 12 ? 0.6869 1.1275 0.6631 -0.0111 0.0085 0.0640 12 SER A C 90 O O . SER A 12 ? 0.6783 1.0984 0.6477 0.0031 0.0120 0.0613 12 SER A O 91 C CB . SER A 12 ? 0.6736 1.0800 0.6511 -0.0560 0.0017 0.0659 12 SER A CB 92 O OG . SER A 12 ? 0.6670 1.0541 0.6440 -0.0584 -0.0013 0.0642 12 SER A OG 93 N N . THR A 13 ? 0.6874 1.1361 0.6641 -0.0039 0.0072 0.0637 13 THR A N 94 C CA . THR A 13 ? 0.6898 1.1189 0.6570 0.0214 0.0095 0.0600 13 THR A CA 95 C C . THR A 13 ? 0.6940 1.0816 0.6587 0.0158 0.0068 0.0568 13 THR A C 96 O O . THR A 13 ? 0.6827 1.0505 0.6377 0.0330 0.0080 0.0539 13 THR A O 97 C CB . THR A 13 ? 0.6986 1.1750 0.6657 0.0394 0.0105 0.0623 13 THR A CB 98 O OG1 . THR A 13 ? 0.6845 1.1929 0.6623 0.0221 0.0065 0.0657 13 THR A OG1 99 C CG2 . THR A 13 ? 0.6956 1.2137 0.6627 0.0507 0.0139 0.0647 13 THR A CG2 100 N N . GLU A 14 ? 0.6956 1.0688 0.6664 -0.0075 0.0031 0.0573 14 GLU A N 101 C CA . GLU A 14 ? 0.7074 1.0431 0.6761 -0.0135 0.0005 0.0541 14 GLU A CA 102 C C . GLU A 14 ? 0.7088 1.0010 0.6680 -0.0030 0.0030 0.0491 14 GLU A C 103 O O . GLU A 14 ? 0.7127 0.9916 0.6699 -0.0051 0.0046 0.0481 14 GLU A O 104 C CB . GLU A 14 ? 0.7373 1.0631 0.7099 -0.0386 -0.0038 0.0555 14 GLU A CB 105 C CG . GLU A 14 ? 0.7637 1.1254 0.7412 -0.0548 -0.0073 0.0604 14 GLU A CG 106 C CD . GLU A 14 ? 0.8157 1.1829 0.7946 -0.0535 -0.0096 0.0603 14 GLU A CD 107 O OE1 . GLU A 14 ? 0.8511 1.1824 0.8267 -0.0551 -0.0114 0.0570 14 GLU A OE1 108 O OE2 . GLU A 14 ? 0.8389 1.2488 0.8221 -0.0503 -0.0096 0.0635 14 GLU A OE2 109 N N . GLN A 15 ? 0.7119 0.9825 0.6640 0.0068 0.0032 0.0460 15 GLN A N 110 C CA . GLN A 15 ? 0.6949 0.9251 0.6347 0.0144 0.0055 0.0413 15 GLN A CA 111 C C . GLN A 15 ? 0.6567 0.8588 0.5975 0.0029 0.0028 0.0382 15 GLN A C 112 O O . GLN A 15 ? 0.6390 0.8483 0.5855 -0.0032 -0.0002 0.0391 15 GLN A O 113 C CB . GLN A 15 ? 0.7370 0.9608 0.6613 0.0359 0.0082 0.0399 15 GLN A CB 114 C CG . GLN A 15 ? 0.7689 1.0155 0.6866 0.0531 0.0114 0.0419 15 GLN A CG 115 C CD . GLN A 15 ? 0.8174 1.0489 0.7132 0.0767 0.0135 0.0400 15 GLN A CD 116 O OE1 . GLN A 15 ? 0.8639 1.0770 0.7524 0.0788 0.0121 0.0383 15 GLN A OE1 117 N NE2 . GLN A 15 ? 0.8486 1.0853 0.7307 0.0952 0.0168 0.0403 15 GLN A NE2 118 N N . VAL A 16 ? 0.6394 0.8117 0.5741 0.0004 0.0039 0.0345 16 VAL A N 119 C CA . VAL A 16 ? 0.6239 0.7720 0.5578 -0.0078 0.0018 0.0309 16 VAL A CA 120 C C . VAL A 16 ? 0.6388 0.7584 0.5574 -0.0014 0.0048 0.0267 16 VAL A C 121 O O . VAL A 16 ? 0.6474 0.7617 0.5566 0.0058 0.0079 0.0264 16 VAL A O 122 C CB . VAL A 16 ? 0.6104 0.7546 0.5526 -0.0223 -0.0009 0.0306 16 VAL A CB 123 C CG1 . VAL A 16 ? 0.6066 0.7738 0.5580 -0.0316 -0.0041 0.0351 16 VAL A CG1 124 C CG2 . VAL A 16 ? 0.6116 0.7471 0.5505 -0.0223 0.0013 0.0294 16 VAL A CG2 125 N N . ASP A 17 ? 0.6424 0.7437 0.5564 -0.0052 0.0037 0.0235 17 ASP A N 126 C CA . ASP A 17 ? 0.6636 0.7372 0.5603 -0.0035 0.0061 0.0195 17 ASP A CA 127 C C . ASP A 17 ? 0.6586 0.7231 0.5584 -0.0152 0.0056 0.0163 17 ASP A C 128 O O . ASP A 17 ? 0.6452 0.7190 0.5587 -0.0232 0.0026 0.0163 17 ASP A O 129 C CB . ASP A 17 ? 0.6952 0.7559 0.5825 -0.0014 0.0054 0.0178 17 ASP A CB 130 C CG . ASP A 17 ? 0.7312 0.7952 0.6079 0.0139 0.0065 0.0201 17 ASP A CG 131 O OD1 . ASP A 17 ? 0.7475 0.8155 0.6164 0.0250 0.0088 0.0218 17 ASP A OD1 132 O OD2 . ASP A 17 ? 0.7500 0.8130 0.6250 0.0160 0.0049 0.0201 17 ASP A OD2 133 N N . THR A 18 ? 0.6679 0.7139 0.5525 -0.0157 0.0083 0.0135 18 THR A N 134 C CA . THR A 18 ? 0.6660 0.7054 0.5506 -0.0266 0.0080 0.0098 18 THR A CA 135 C C . THR A 18 ? 0.7064 0.7229 0.5697 -0.0302 0.0099 0.0062 18 THR A C 136 O O . THR A 18 ? 0.7640 0.7649 0.6103 -0.0234 0.0112 0.0067 18 THR A O 137 C CB . THR A 18 ? 0.6439 0.6869 0.5304 -0.0283 0.0094 0.0100 18 THR A CB 138 O OG1 . THR A 18 ? 0.6562 0.6832 0.5233 -0.0229 0.0129 0.0098 18 THR A OG1 139 C CG2 . THR A 18 ? 0.6184 0.6815 0.5214 -0.0257 0.0078 0.0140 18 THR A CG2 140 N N . ILE A 19 ? 0.7351 0.7498 0.5968 -0.0412 0.0097 0.0027 19 ILE A N 141 C CA . ILE A 19 ? 0.7751 0.7698 0.6144 -0.0491 0.0114 -0.0007 19 ILE A CA 142 C C . ILE A 19 ? 0.7931 0.7626 0.6055 -0.0462 0.0146 -0.0005 19 ILE A C 143 O O . ILE A 19 ? 0.7996 0.7435 0.5866 -0.0454 0.0158 -0.0013 19 ILE A O 144 C CB . ILE A 19 ? 0.7933 0.7991 0.6372 -0.0622 0.0107 -0.0044 19 ILE A CB 145 C CG1 . ILE A 19 ? 0.7903 0.8151 0.6534 -0.0635 0.0074 -0.0054 19 ILE A CG1 146 C CG2 . ILE A 19 ? 0.8219 0.8091 0.6396 -0.0743 0.0127 -0.0078 19 ILE A CG2 147 C CD1 . ILE A 19 ? 0.8075 0.8236 0.6622 -0.0666 0.0070 -0.0068 19 ILE A CD1 148 N N . MET A 20 ? 0.7793 0.7536 0.5948 -0.0440 0.0159 0.0004 20 MET A N 149 C CA . MET A 20 ? 0.8076 0.7573 0.5963 -0.0409 0.0189 0.0004 20 MET A CA 150 C C . MET A 20 ? 0.8138 0.7576 0.5959 -0.0226 0.0201 0.0038 20 MET A C 151 O O . MET A 20 ? 0.8340 0.7512 0.5872 -0.0166 0.0225 0.0036 20 MET A O 152 C CB . MET A 20 ? 0.8181 0.7760 0.6116 -0.0475 0.0198 -0.0003 20 MET A CB 153 C CG . MET A 20 ? 0.8287 0.7910 0.6202 -0.0649 0.0193 -0.0042 20 MET A CG 154 S SD . MET A 20 ? 0.8561 0.8269 0.6495 -0.0708 0.0205 -0.0049 20 MET A SD 155 C CE . MET A 20 ? 0.8959 0.8533 0.6624 -0.0918 0.0216 -0.0094 20 MET A CE 156 N N . GLU A 21 ? 0.8052 0.7741 0.6114 -0.0138 0.0184 0.0069 21 GLU A N 157 C CA . GLU A 21 ? 0.8163 0.7901 0.6197 0.0034 0.0196 0.0103 21 GLU A CA 158 C C . GLU A 21 ? 0.8162 0.8124 0.6377 0.0101 0.0173 0.0130 21 GLU A C 159 O O . GLU A 21 ? 0.7852 0.8052 0.6327 0.0027 0.0148 0.0141 21 GLU A O 160 C CB . GLU A 21 ? 0.8001 0.7906 0.6154 0.0056 0.0207 0.0122 21 GLU A CB 161 C CG . GLU A 21 ? 0.8323 0.8210 0.6337 0.0237 0.0231 0.0146 21 GLU A CG 162 C CD . GLU A 21 ? 0.8417 0.8493 0.6556 0.0252 0.0243 0.0166 21 GLU A CD 163 O OE1 . GLU A 21 ? 0.8318 0.8439 0.6575 0.0121 0.0237 0.0155 21 GLU A OE1 164 O OE2 . GLU A 21 ? 0.8251 0.8447 0.6361 0.0405 0.0258 0.0192 21 GLU A OE2 165 N N . LYS A 22 ? 0.8421 0.8288 0.6468 0.0246 0.0180 0.0141 22 LYS A N 166 C CA . LYS A 22 ? 0.8268 0.8365 0.6456 0.0327 0.0160 0.0169 22 LYS A CA 167 C C . LYS A 22 ? 0.7981 0.8370 0.6275 0.0450 0.0168 0.0208 22 LYS A C 168 O O . LYS A 22 ? 0.7966 0.8290 0.6133 0.0532 0.0194 0.0210 22 LYS A O 169 C CB . LYS A 22 ? 0.8695 0.8555 0.6630 0.0431 0.0161 0.0160 22 LYS A CB 170 C CG . LYS A 22 ? 0.8956 0.8732 0.6923 0.0312 0.0139 0.0139 22 LYS A CG 171 C CD . LYS A 22 ? 0.9332 0.8887 0.7213 0.0136 0.0144 0.0100 22 LYS A CD 172 C CE . LYS A 22 ? 0.9448 0.9136 0.7537 -0.0003 0.0116 0.0086 22 LYS A CE 173 N NZ . LYS A 22 ? 0.9505 0.9069 0.7534 -0.0171 0.0120 0.0047 22 LYS A NZ 174 N N . ASN A 23 ? 0.7895 0.8614 0.6409 0.0453 0.0145 0.0240 23 ASN A N 175 C CA . ASN A 23 ? 0.8066 0.9131 0.6677 0.0559 0.0151 0.0280 23 ASN A CA 176 C C . ASN A 23 ? 0.7555 0.8718 0.6240 0.0515 0.0167 0.0289 23 ASN A C 177 O O . ASN A 23 ? 0.7465 0.8650 0.6031 0.0651 0.0195 0.0297 23 ASN A O 178 C CB . ASN A 23 ? 0.8837 0.9863 0.7217 0.0797 0.0170 0.0285 23 ASN A CB 179 C CG . ASN A 23 ? 0.9614 1.0620 0.7947 0.0854 0.0150 0.0285 23 ASN A CG 180 O OD1 . ASN A 23 ? 0.9519 1.0648 0.8043 0.0718 0.0120 0.0291 23 ASN A OD1 181 N ND2 . ASN A 23 ? 1.0794 1.1626 0.8846 0.1065 0.0163 0.0279 23 ASN A ND2 182 N N . VAL A 24 ? 0.7131 0.8336 0.5992 0.0336 0.0147 0.0288 24 VAL A N 183 C CA . VAL A 24 ? 0.6769 0.8082 0.5720 0.0274 0.0155 0.0300 24 VAL A CA 184 C C . VAL A 24 ? 0.6650 0.8343 0.5799 0.0218 0.0134 0.0345 24 VAL A C 185 O O . VAL A 24 ? 0.6650 0.8412 0.5923 0.0093 0.0099 0.0353 24 VAL A O 186 C CB . VAL A 24 ? 0.6570 0.7699 0.5566 0.0118 0.0142 0.0271 24 VAL A CB 187 C CG1 . VAL A 24 ? 0.6509 0.7755 0.5598 0.0055 0.0145 0.0287 24 VAL A CG1 188 C CG2 . VAL A 24 ? 0.6736 0.7525 0.5527 0.0133 0.0163 0.0227 24 VAL A CG2 189 N N . THR A 25 ? 0.6519 0.8456 0.5675 0.0302 0.0155 0.0374 25 THR A N 190 C CA . THR A 25 ? 0.6381 0.8709 0.5698 0.0224 0.0137 0.0420 25 THR A CA 191 C C . THR A 25 ? 0.6236 0.8518 0.5650 0.0033 0.0115 0.0425 25 THR A C 192 O O . THR A 25 ? 0.6349 0.8443 0.5717 0.0024 0.0131 0.0405 25 THR A O 193 C CB . THR A 25 ? 0.6544 0.9173 0.5835 0.0359 0.0168 0.0447 25 THR A CB 194 O OG1 . THR A 25 ? 0.6930 0.9493 0.6053 0.0587 0.0194 0.0432 25 THR A OG1 195 C CG2 . THR A 25 ? 0.6457 0.9562 0.5899 0.0275 0.0148 0.0497 25 THR A CG2 196 N N . VAL A 26 ? 0.5950 0.8384 0.5470 -0.0116 0.0076 0.0452 26 VAL A N 197 C CA . VAL A 26 ? 0.5834 0.8187 0.5395 -0.0287 0.0048 0.0460 26 VAL A CA 198 C C . VAL A 26 ? 0.5868 0.8536 0.5491 -0.0419 0.0025 0.0512 26 VAL A C 199 O O . VAL A 26 ? 0.6192 0.9151 0.5853 -0.0411 0.0020 0.0540 26 VAL A O 200 C CB . VAL A 26 ? 0.5725 0.7802 0.5280 -0.0375 0.0012 0.0431 26 VAL A CB 201 C CG1 . VAL A 26 ? 0.5708 0.7496 0.5195 -0.0288 0.0034 0.0380 26 VAL A CG1 202 C CG2 . VAL A 26 ? 0.5746 0.7921 0.5333 -0.0411 -0.0016 0.0444 26 VAL A CG2 203 N N . THR A 27 ? 0.5848 0.8456 0.5460 -0.0549 0.0009 0.0526 27 THR A N 204 C CA . THR A 27 ? 0.5779 0.8647 0.5403 -0.0712 -0.0013 0.0577 27 THR A CA 205 C C . THR A 27 ? 0.5807 0.8655 0.5412 -0.0863 -0.0064 0.0594 27 THR A C 206 O O . THR A 27 ? 0.5934 0.9092 0.5553 -0.0974 -0.0080 0.0638 27 THR A O 207 C CB . THR A 27 ? 0.5793 0.8528 0.5364 -0.0819 -0.0022 0.0586 27 THR A CB 208 O OG1 . THR A 27 ? 0.5845 0.8191 0.5345 -0.0880 -0.0058 0.0558 27 THR A OG1 209 C CG2 . THR A 27 ? 0.5783 0.8524 0.5364 -0.0679 0.0027 0.0569 27 THR A CG2 210 N N . HIS A 28 ? 0.5773 0.8273 0.5336 -0.0870 -0.0090 0.0559 28 HIS A N 211 C CA . HIS A 28 ? 0.5769 0.8187 0.5285 -0.0998 -0.0140 0.0569 28 HIS A CA 212 C C . HIS A 28 ? 0.5742 0.7927 0.5267 -0.0901 -0.0145 0.0523 28 HIS A C 213 O O . HIS A 28 ? 0.5577 0.7543 0.5100 -0.0795 -0.0125 0.0479 28 HIS A O 214 C CB . HIS A 28 ? 0.5888 0.8064 0.5267 -0.1170 -0.0185 0.0582 28 HIS A CB 215 C CG . HIS A 28 ? 0.5988 0.8354 0.5328 -0.1294 -0.0184 0.0627 28 HIS A CG 216 N ND1 . HIS A 28 ? 0.5925 0.8261 0.5271 -0.1240 -0.0156 0.0621 28 HIS A ND1 217 C CD2 . HIS A 28 ? 0.6009 0.8613 0.5294 -0.1484 -0.0208 0.0681 28 HIS A CD2 218 C CE1 . HIS A 28 ? 0.5941 0.8482 0.5241 -0.1384 -0.0161 0.0669 28 HIS A CE1 219 N NE2 . HIS A 28 ? 0.6024 0.8739 0.5283 -0.1541 -0.0192 0.0706 28 HIS A NE2 220 N N . ALA A 29 ? 0.5945 0.8195 0.5472 -0.0952 -0.0171 0.0533 29 ALA A N 221 C CA . ALA A 29 ? 0.6073 0.8134 0.5608 -0.0871 -0.0177 0.0493 29 ALA A CA 222 C C . ALA A 29 ? 0.6391 0.8398 0.5866 -0.1006 -0.0228 0.0508 29 ALA A C 223 O O . ALA A 29 ? 0.6509 0.8668 0.5937 -0.1162 -0.0256 0.0553 29 ALA A O 224 C CB . ALA A 29 ? 0.5906 0.8146 0.5518 -0.0709 -0.0137 0.0483 29 ALA A CB 225 N N . GLN A 30 ? 0.6793 0.8581 0.6251 -0.0959 -0.0242 0.0471 30 GLN A N 226 C CA . GLN A 30 ? 0.7174 0.8887 0.6563 -0.1068 -0.0289 0.0480 30 GLN A CA 227 C C . GLN A 30 ? 0.6985 0.8706 0.6438 -0.0967 -0.0280 0.0453 30 GLN A C 228 O O . GLN A 30 ? 0.6939 0.8448 0.6392 -0.0871 -0.0269 0.0406 30 GLN A O 229 C CB . GLN A 30 ? 0.7570 0.8919 0.6803 -0.1140 -0.0333 0.0462 30 GLN A CB 230 C CG . GLN A 30 ? 0.7952 0.9173 0.7061 -0.1263 -0.0386 0.0473 30 GLN A CG 231 C CD . GLN A 30 ? 0.8471 0.9316 0.7355 -0.1337 -0.0435 0.0465 30 GLN A CD 232 O OE1 . GLN A 30 ? 0.8766 0.9503 0.7575 -0.1348 -0.0436 0.0468 30 GLN A OE1 233 N NE2 . GLN A 30 ? 0.8804 0.9430 0.7556 -0.1378 -0.0478 0.0453 30 GLN A NE2 234 N N . ASP A 31 ? 0.7015 0.9005 0.6517 -0.0992 -0.0283 0.0484 31 ASP A N 235 C CA . ASP A 31 ? 0.6894 0.8889 0.6434 -0.0914 -0.0282 0.0465 31 ASP A CA 236 C C . ASP A 31 ? 0.6961 0.8683 0.6405 -0.1009 -0.0330 0.0448 31 ASP A C 237 O O . ASP A 31 ? 0.7013 0.8687 0.6354 -0.1171 -0.0373 0.0476 31 ASP A O 238 C CB . ASP A 31 ? 0.6839 0.9223 0.6443 -0.0918 -0.0280 0.0506 31 ASP A CB 239 C CG . ASP A 31 ? 0.7009 0.9411 0.6647 -0.0803 -0.0272 0.0487 31 ASP A CG 240 O OD1 . ASP A 31 ? 0.7157 0.9263 0.6765 -0.0750 -0.0272 0.0443 31 ASP A OD1 241 O OD2 . ASP A 31 ? 0.7088 0.9820 0.6774 -0.0762 -0.0267 0.0515 31 ASP A OD2 242 N N . ILE A 32 ? 0.6710 0.8241 0.6160 -0.0912 -0.0323 0.0402 32 ILE A N 243 C CA . ILE A 32 ? 0.6787 0.8063 0.6142 -0.0967 -0.0364 0.0379 32 ILE A CA 244 C C . ILE A 32 ? 0.6841 0.8153 0.6231 -0.0930 -0.0368 0.0367 32 ILE A C 245 O O . ILE A 32 ? 0.6906 0.8012 0.6226 -0.0947 -0.0396 0.0341 32 ILE A O 246 C CB . ILE A 32 ? 0.6748 0.7749 0.6053 -0.0897 -0.0359 0.0329 32 ILE A CB 247 C CG1 . ILE A 32 ? 0.6537 0.7571 0.5934 -0.0757 -0.0307 0.0293 32 ILE A CG1 248 C CG2 . ILE A 32 ? 0.6958 0.7877 0.6187 -0.0952 -0.0370 0.0343 32 ILE A CG2 249 C CD1 . ILE A 32 ? 0.6559 0.7384 0.5914 -0.0700 -0.0305 0.0240 32 ILE A CD1 250 N N . LEU A 33 ? 0.6838 0.8411 0.6319 -0.0869 -0.0343 0.0387 33 LEU A N 251 C CA . LEU A 33 ? 0.6890 0.8510 0.6397 -0.0818 -0.0345 0.0379 33 LEU A CA 252 C C . LEU A 33 ? 0.7071 0.8994 0.6603 -0.0896 -0.0367 0.0429 33 LEU A C 253 O O . LEU A 33 ? 0.7191 0.9417 0.6783 -0.0862 -0.0346 0.0461 33 LEU A O 254 C CB . LEU A 33 ? 0.6795 0.8433 0.6344 -0.0648 -0.0296 0.0354 33 LEU A CB 255 C CG . LEU A 33 ? 0.6754 0.8380 0.6297 -0.0575 -0.0294 0.0340 33 LEU A CG 256 C CD1 . LEU A 33 ? 0.6870 0.8233 0.6368 -0.0618 -0.0316 0.0300 33 LEU A CD1 257 C CD2 . LEU A 33 ? 0.6757 0.8367 0.6277 -0.0412 -0.0248 0.0322 33 LEU A CD2 258 N N . GLU A 34 ? 0.7269 0.9133 0.6748 -0.0999 -0.0409 0.0434 34 GLU A N 259 C CA . GLU A 34 ? 0.7438 0.9612 0.6938 -0.1081 -0.0432 0.0479 34 GLU A CA 260 C C . GLU A 34 ? 0.7172 0.9515 0.6751 -0.0920 -0.0407 0.0471 34 GLU A C 261 O O . GLU A 34 ? 0.7083 0.9208 0.6645 -0.0844 -0.0403 0.0433 34 GLU A O 262 C CB . GLU A 34 ? 0.7710 0.9725 0.7096 -0.1250 -0.0488 0.0485 34 GLU A CB 263 C CG . GLU A 34 ? 0.7798 1.0149 0.7192 -0.1368 -0.0516 0.0533 34 GLU A CG 264 C CD . GLU A 34 ? 0.7932 1.0666 0.7360 -0.1461 -0.0512 0.0585 34 GLU A CD 265 O OE1 . GLU A 34 ? 0.8181 1.0795 0.7515 -0.1592 -0.0527 0.0598 34 GLU A OE1 266 O OE2 . GLU A 34 ? 0.8068 1.1228 0.7603 -0.1393 -0.0495 0.0611 34 GLU A OE2 267 N N . LYS A 35 ? 0.7032 0.9764 0.6677 -0.0864 -0.0391 0.0507 35 LYS A N 268 C CA . LYS A 35 ? 0.7115 1.0001 0.6794 -0.0680 -0.0368 0.0501 35 LYS A CA 269 C C . LYS A 35 ? 0.7079 1.0309 0.6784 -0.0734 -0.0399 0.0538 35 LYS A C 270 O O . LYS A 35 ? 0.7033 1.0341 0.6741 -0.0587 -0.0391 0.0531 35 LYS A O 271 C CB . LYS A 35 ? 0.7119 1.0180 0.6823 -0.0503 -0.0322 0.0506 35 LYS A CB 272 C CG . LYS A 35 ? 0.7218 0.9922 0.6876 -0.0404 -0.0286 0.0462 35 LYS A CG 273 C CD . LYS A 35 ? 0.7368 1.0227 0.7018 -0.0239 -0.0243 0.0470 35 LYS A CD 274 C CE . LYS A 35 ? 0.7412 1.0105 0.7060 -0.0280 -0.0223 0.0457 35 LYS A CE 275 N NZ . LYS A 35 ? 0.7453 1.0303 0.7155 -0.0476 -0.0250 0.0491 35 LYS A NZ 276 N N . THR A 36 ? 0.7083 1.0505 0.6782 -0.0950 -0.0437 0.0577 36 THR A N 277 C CA . THR A 36 ? 0.7404 1.1227 0.7128 -0.1027 -0.0467 0.0618 36 THR A CA 278 C C . THR A 36 ? 0.7658 1.1281 0.7304 -0.1212 -0.0517 0.0616 36 THR A C 279 O O . THR A 36 ? 0.7492 1.0691 0.7047 -0.1310 -0.0535 0.0591 36 THR A O 280 C CB . THR A 36 ? 0.7531 1.1822 0.7284 -0.1167 -0.0475 0.0672 36 THR A CB 281 O OG1 . THR A 36 ? 0.7763 1.1838 0.7419 -0.1421 -0.0507 0.0684 36 THR A OG1 282 C CG2 . THR A 36 ? 0.7512 1.2020 0.7333 -0.0981 -0.0426 0.0675 36 THR A CG2 283 N N . HIS A 37 ? 0.7826 1.1773 0.7494 -0.1245 -0.0541 0.0644 37 HIS A N 284 C CA . HIS A 37 ? 0.8001 1.1832 0.7584 -0.1433 -0.0592 0.0650 37 HIS A CA 285 C C . HIS A 37 ? 0.8216 1.2610 0.7838 -0.1523 -0.0617 0.0701 37 HIS A C 286 O O . HIS A 37 ? 0.8216 1.3048 0.7943 -0.1357 -0.0591 0.0718 37 HIS A O 287 C CB . HIS A 37 ? 0.8012 1.1478 0.7579 -0.1299 -0.0588 0.0602 37 HIS A CB 288 C CG . HIS A 37 ? 0.7987 1.1666 0.7636 -0.1059 -0.0560 0.0594 37 HIS A CG 289 N ND1 . HIS A 37 ? 0.7866 1.1779 0.7526 -0.1054 -0.0585 0.0611 37 HIS A ND1 290 C CD2 . HIS A 37 ? 0.8047 1.1712 0.7734 -0.0814 -0.0512 0.0573 37 HIS A CD2 291 C CE1 . HIS A 37 ? 0.7925 1.1952 0.7622 -0.0802 -0.0554 0.0599 37 HIS A CE1 292 N NE2 . HIS A 37 ? 0.8061 1.1921 0.7760 -0.0656 -0.0510 0.0576 37 HIS A NE2 293 N N . ASN A 38 ? 0.8531 1.2922 0.8049 -0.1781 -0.0670 0.0726 38 ASN A N 294 C CA . ASN A 38 ? 0.8708 1.3672 0.8250 -0.1913 -0.0699 0.0778 38 ASN A CA 295 C C . ASN A 38 ? 0.8779 1.3957 0.8398 -0.1749 -0.0701 0.0772 38 ASN A C 296 O O . ASN A 38 ? 0.8979 1.4705 0.8640 -0.1808 -0.0720 0.0813 38 ASN A O 297 C CB . ASN A 38 ? 0.8761 1.3633 0.8117 -0.2283 -0.0759 0.0810 38 ASN A CB 298 C CG . ASN A 38 ? 0.8683 1.3059 0.7901 -0.2354 -0.0796 0.0781 38 ASN A CG 299 O OD1 . ASN A 38 ? 0.8495 1.2693 0.7784 -0.2144 -0.0779 0.0742 38 ASN A OD1 300 N ND2 . ASN A 38 ? 0.8760 1.2893 0.7753 -0.2654 -0.0848 0.0800 38 ASN A ND2 301 N N . GLY A 39 ? 0.8626 1.3385 0.8248 -0.1556 -0.0683 0.0722 39 GLY A N 302 C CA . GLY A 39 ? 0.8493 1.3397 0.8171 -0.1358 -0.0678 0.0711 39 GLY A CA 303 C C . GLY A 39 ? 0.8342 1.3271 0.7959 -0.1524 -0.0729 0.0724 39 GLY A C 304 O O . GLY A 39 ? 0.7855 1.3042 0.7519 -0.1398 -0.0734 0.0729 39 GLY A O 305 N N . LYS A 40 ? 0.8661 1.3289 0.8147 -0.1796 -0.0768 0.0727 40 LYS A N 306 C CA . LYS A 40 ? 0.8840 1.3483 0.8224 -0.2013 -0.0823 0.0745 40 LYS A CA 307 C C . LYS A 40 ? 0.9088 1.3066 0.8317 -0.2092 -0.0845 0.0704 40 LYS A C 308 O O . LYS A 40 ? 0.9015 1.2572 0.8187 -0.2069 -0.0829 0.0673 40 LYS A O 309 C CB . LYS A 40 ? 0.9094 1.4088 0.8393 -0.2330 -0.0863 0.0803 40 LYS A CB 310 C CG . LYS A 40 ? 0.9242 1.5012 0.8684 -0.2288 -0.0851 0.0850 40 LYS A CG 311 C CD . LYS A 40 ? 0.9399 1.5480 0.8763 -0.2590 -0.0873 0.0902 40 LYS A CD 312 C CE . LYS A 40 ? 0.9444 1.6367 0.8966 -0.2523 -0.0857 0.0946 40 LYS A CE 313 N NZ . LYS A 40 ? 0.9698 1.6975 0.9153 -0.2817 -0.0873 0.0996 40 LYS A NZ 314 N N . LEU A 41 ? 0.9315 1.3221 0.8470 -0.2176 -0.0883 0.0703 41 LEU A N 315 C CA . LEU A 41 ? 0.9599 1.2921 0.8564 -0.2290 -0.0915 0.0670 41 LEU A CA 316 C C . LEU A 41 ? 0.9552 1.2828 0.8291 -0.2637 -0.0972 0.0710 41 LEU A C 317 O O . LEU A 41 ? 0.9656 1.3351 0.8375 -0.2819 -0.1004 0.0758 41 LEU A O 318 C CB . LEU A 41 ? 0.9830 1.3063 0.8805 -0.2206 -0.0927 0.0647 41 LEU A CB 319 C CG . LEU A 41 ? 0.9855 1.3127 0.9007 -0.1885 -0.0875 0.0612 41 LEU A CG 320 C CD1 . LEU A 41 ? 0.9857 1.3096 0.9001 -0.1834 -0.0893 0.0599 41 LEU A CD1 321 C CD2 . LEU A 41 ? 0.9817 1.2640 0.8969 -0.1735 -0.0834 0.0560 41 LEU A CD2 322 N N . CYS A 42 ? 0.9425 1.2192 0.7969 -0.2728 -0.0985 0.0690 42 CYS A N 323 C CA . CYS A 42 ? 0.9574 1.2201 0.7838 -0.3054 -0.1038 0.0727 42 CYS A CA 324 C C . CYS A 42 ? 0.9567 1.1524 0.7524 -0.3145 -0.1081 0.0694 42 CYS A C 325 O O . CYS A 42 ? 0.9416 1.1033 0.7404 -0.2939 -0.1062 0.0640 42 CYS A O 326 C CB . CYS A 42 ? 0.9673 1.2293 0.7925 -0.3084 -0.1017 0.0739 42 CYS A CB 327 S SG . CYS A 42 ? 0.9314 1.2655 0.7902 -0.2931 -0.0959 0.0769 42 CYS A SG 328 N N . ASP A 43 ? 0.9982 1.1744 0.7613 -0.3456 -0.1139 0.0728 43 ASP A N 329 C CA . ASP A 43 ? 1.0430 1.1487 0.7685 -0.3544 -0.1185 0.0699 43 ASP A CA 330 C C . ASP A 43 ? 1.0489 1.1117 0.7684 -0.3381 -0.1160 0.0658 43 ASP A C 331 O O . ASP A 43 ? 1.0301 1.1150 0.7638 -0.3343 -0.1126 0.0673 43 ASP A O 332 C CB . ASP A 43 ? 1.0939 1.1865 0.7799 -0.3940 -0.1256 0.0750 43 ASP A CB 333 C CG . ASP A 43 ? 1.1006 1.2412 0.7911 -0.4138 -0.1286 0.0795 43 ASP A CG 334 O OD1 . ASP A 43 ? 1.0937 1.2646 0.8122 -0.3953 -0.1259 0.0779 43 ASP A OD1 335 O OD2 . ASP A 43 ? 1.1279 1.2764 0.7921 -0.4491 -0.1336 0.0848 43 ASP A OD2 336 N N . LEU A 44 ? 1.0745 1.0783 0.7726 -0.3279 -0.1177 0.0607 44 LEU A N 337 C CA . LEU A 44 ? 1.1074 1.0703 0.7975 -0.3108 -0.1158 0.0564 44 LEU A CA 338 C C . LEU A 44 ? 1.1738 1.0766 0.8130 -0.3294 -0.1222 0.0570 44 LEU A C 339 O O . LEU A 44 ? 1.1815 1.0367 0.7903 -0.3300 -0.1264 0.0542 44 LEU A O 340 C CB . LEU A 44 ? 1.1016 1.0461 0.8060 -0.2804 -0.1124 0.0495 44 LEU A CB 341 C CG . LEU A 44 ? 1.1190 1.0336 0.8230 -0.2583 -0.1094 0.0445 44 LEU A CG 342 C CD1 . LEU A 44 ? 1.0850 1.0393 0.8219 -0.2477 -0.1034 0.0456 44 LEU A CD1 343 C CD2 . LEU A 44 ? 1.1079 1.0016 0.8171 -0.2342 -0.1075 0.0379 44 LEU A CD2 344 N N . ASP A 45 ? 1.2273 1.1301 0.8549 -0.3434 -0.1229 0.0605 45 ASP A N 345 C CA . ASP A 45 ? 1.3075 1.1531 0.8816 -0.3649 -0.1293 0.0621 45 ASP A CA 346 C C . ASP A 45 ? 1.3154 1.1443 0.8547 -0.3947 -0.1361 0.0654 45 ASP A C 347 O O . ASP A 45 ? 1.3256 1.0907 0.8196 -0.3989 -0.1415 0.0632 45 ASP A O 348 C CB . ASP A 45 ? 1.3749 1.1572 0.9256 -0.3413 -0.1299 0.0559 45 ASP A CB 349 C CG . ASP A 45 ? 1.4200 1.2094 0.9891 -0.3233 -0.1251 0.0543 45 ASP A CG 350 O OD1 . ASP A 45 ? 1.4815 1.2539 1.0261 -0.3393 -0.1275 0.0575 45 ASP A OD1 351 O OD2 . ASP A 45 ? 1.4033 1.2148 1.0096 -0.2946 -0.1192 0.0500 45 ASP A OD2 352 N N . GLY A 46 ? 1.2865 1.1749 0.8466 -0.4141 -0.1358 0.0706 46 GLY A N 353 C CA . GLY A 46 ? 1.3107 1.1964 0.8423 -0.4460 -0.1420 0.0745 46 GLY A CA 354 C C . GLY A 46 ? 1.2886 1.1829 0.8346 -0.4348 -0.1420 0.0718 46 GLY A C 355 O O . GLY A 46 ? 1.2739 1.2002 0.8194 -0.4569 -0.1447 0.0758 46 GLY A O 356 N N . VAL A 47 ? 1.2603 1.1295 0.8196 -0.4010 -0.1388 0.0651 47 VAL A N 357 C CA . VAL A 47 ? 1.2424 1.1046 0.8064 -0.3899 -0.1394 0.0617 47 VAL A CA 358 C C . VAL A 47 ? 1.1901 1.1210 0.8084 -0.3738 -0.1336 0.0618 47 VAL A C 359 O O . VAL A 47 ? 1.1662 1.1150 0.8187 -0.3454 -0.1274 0.0584 47 VAL A O 360 C CB . VAL A 47 ? 1.2426 1.0458 0.7918 -0.3618 -0.1389 0.0543 47 VAL A CB 361 C CG1 . VAL A 47 ? 1.2436 1.0386 0.7948 -0.3521 -0.1397 0.0509 47 VAL A CG1 362 C CG2 . VAL A 47 ? 1.2952 1.0266 0.7864 -0.3734 -0.1448 0.0539 47 VAL A CG2 363 N N . LYS A 48 ? 1.1863 1.1530 0.8086 -0.3924 -0.1361 0.0657 48 LYS A N 364 C CA . LYS A 48 ? 1.1566 1.1889 0.8245 -0.3789 -0.1317 0.0666 48 LYS A CA 365 C C . LYS A 48 ? 1.1094 1.1285 0.7979 -0.3462 -0.1277 0.0602 48 LYS A C 366 O O . LYS A 48 ? 1.1120 1.0803 0.7767 -0.3423 -0.1304 0.0562 48 LYS A O 367 C CB . LYS A 48 ? 1.2147 1.2810 0.8753 -0.4064 -0.1363 0.0717 48 LYS A CB 368 C CG . LYS A 48 ? 1.2089 1.3484 0.9118 -0.3951 -0.1327 0.0736 48 LYS A CG 369 C CD . LYS A 48 ? 1.2602 1.4162 0.9525 -0.4148 -0.1376 0.0763 48 LYS A CD 370 C CE . LYS A 48 ? 1.2487 1.4769 0.9803 -0.4013 -0.1344 0.0781 48 LYS A CE 371 N NZ . LYS A 48 ? 1.2596 1.5569 1.0033 -0.4180 -0.1345 0.0845 48 LYS A NZ 372 N N . PRO A 49 ? 1.0633 1.1270 0.7935 -0.3227 -0.1215 0.0592 49 PRO A N 373 C CA . PRO A 49 ? 1.0332 1.0879 0.7811 -0.2957 -0.1181 0.0538 49 PRO A CA 374 C C . PRO A 49 ? 1.0292 1.1005 0.7788 -0.3015 -0.1206 0.0548 49 PRO A C 375 O O . PRO A 49 ? 1.0375 1.1439 0.7847 -0.3228 -0.1238 0.0601 49 PRO A O 376 C CB . PRO A 49 ? 0.9845 1.0812 0.7703 -0.2731 -0.1113 0.0534 49 PRO A CB 377 C CG . PRO A 49 ? 0.9851 1.1331 0.7789 -0.2896 -0.1120 0.0599 49 PRO A CG 378 C CD . PRO A 49 ? 1.0293 1.1496 0.7886 -0.3189 -0.1174 0.0628 49 PRO A CD 379 N N . LEU A 50 ? 1.0087 1.0575 0.7625 -0.2829 -0.1191 0.0497 50 LEU A N 380 C CA . LEU A 50 ? 0.9976 1.0642 0.7584 -0.2827 -0.1204 0.0499 50 LEU A CA 381 C C . LEU A 50 ? 0.9550 1.0715 0.7528 -0.2624 -0.1150 0.0505 50 LEU A C 382 O O . LEU A 50 ? 0.9637 1.0709 0.7769 -0.2382 -0.1100 0.0461 50 LEU A O 383 C CB . LEU A 50 ? 1.0081 1.0263 0.7544 -0.2717 -0.1211 0.0440 50 LEU A CB 384 C CG . LEU A 50 ? 0.9977 1.0265 0.7512 -0.2674 -0.1218 0.0431 50 LEU A CG 385 C CD1 . LEU A 50 ? 1.0037 1.0685 0.7539 -0.2907 -0.1263 0.0491 50 LEU A CD1 386 C CD2 . LEU A 50 ? 1.0288 1.0037 0.7575 -0.2636 -0.1241 0.0378 50 LEU A CD2 387 N N . ILE A 51 ? 0.9444 1.1136 0.7539 -0.2720 -0.1161 0.0558 51 ILE A N 388 C CA . ILE A 51 ? 0.9197 1.1356 0.7594 -0.2508 -0.1115 0.0566 51 ILE A CA 389 C C . ILE A 51 ? 0.9121 1.1412 0.7564 -0.2459 -0.1129 0.0563 51 ILE A C 390 O O . ILE A 51 ? 0.9264 1.1886 0.7676 -0.2622 -0.1169 0.0607 51 ILE A O 391 C CB . ILE A 51 ? 0.9080 1.1800 0.7594 -0.2585 -0.1112 0.0623 51 ILE A CB 392 C CG1 . ILE A 51 ? 0.9292 1.1845 0.7761 -0.2620 -0.1094 0.0622 51 ILE A CG1 393 C CG2 . ILE A 51 ? 0.8788 1.1969 0.7565 -0.2334 -0.1069 0.0630 51 ILE A CG2 394 C CD1 . ILE A 51 ? 0.9340 1.2426 0.7971 -0.2610 -0.1070 0.0665 51 ILE A CD1 395 N N . LEU A 52 ? 0.8971 1.1021 0.7484 -0.2239 -0.1096 0.0513 52 LEU A N 396 C CA . LEU A 52 ? 0.8881 1.0962 0.7410 -0.2182 -0.1109 0.0502 52 LEU A CA 397 C C . LEU A 52 ? 0.8908 1.1547 0.7614 -0.2086 -0.1101 0.0540 52 LEU A C 398 O O . LEU A 52 ? 0.9161 1.1908 0.7868 -0.2073 -0.1122 0.0544 52 LEU A O 399 C CB . LEU A 52 ? 0.8597 1.0292 0.7147 -0.1977 -0.1071 0.0439 52 LEU A CB 400 C CG . LEU A 52 ? 0.8741 0.9906 0.7109 -0.2026 -0.1078 0.0394 52 LEU A CG 401 C CD1 . LEU A 52 ? 0.8591 0.9484 0.7010 -0.1818 -0.1034 0.0332 52 LEU A CD1 402 C CD2 . LEU A 52 ? 0.9174 1.0121 0.7301 -0.2236 -0.1140 0.0401 52 LEU A CD2 403 N N . ARG A 53 ? 0.9021 1.2010 0.7862 -0.2004 -0.1073 0.0566 53 ARG A N 404 C CA . ARG A 53 ? 0.9209 1.2762 0.8193 -0.1887 -0.1068 0.0603 53 ARG A CA 405 C C . ARG A 53 ? 0.9390 1.2850 0.8436 -0.1616 -0.1038 0.0571 53 ARG A C 406 O O . ARG A 53 ? 0.9827 1.3019 0.8906 -0.1430 -0.0990 0.0533 53 ARG A O 407 C CB . ARG A 53 ? 0.9555 1.3508 0.8486 -0.2121 -0.1125 0.0655 53 ARG A CB 408 C CG . ARG A 53 ? 0.9785 1.4446 0.8857 -0.2044 -0.1124 0.0704 53 ARG A CG 409 C CD . ARG A 53 ? 1.0108 1.5190 0.9129 -0.2267 -0.1183 0.0750 53 ARG A CD 410 N NE . ARG A 53 ? 1.0329 1.5933 0.9364 -0.2468 -0.1202 0.0805 53 ARG A NE 411 C CZ . ARG A 53 ? 1.0642 1.6086 0.9530 -0.2773 -0.1228 0.0822 53 ARG A CZ 412 N NH1 . ARG A 53 ? 1.0920 1.5680 0.9625 -0.2892 -0.1239 0.0787 53 ARG A NH1 413 N NH2 . ARG A 53 ? 1.0724 1.6697 0.9625 -0.2958 -0.1244 0.0875 53 ARG A NH2 414 N N . ASP A 54 ? 0.9373 1.3030 0.8413 -0.1605 -0.1066 0.0585 54 ASP A N 415 C CA . ASP A 54 ? 0.9336 1.2864 0.8393 -0.1365 -0.1043 0.0555 54 ASP A CA 416 C C . ASP A 54 ? 0.9406 1.2424 0.8361 -0.1408 -0.1049 0.0509 54 ASP A C 417 O O . ASP A 54 ? 0.9443 1.2285 0.8389 -0.1231 -0.1027 0.0479 54 ASP A O 418 C CB . ASP A 54 ? 0.9459 1.3488 0.8558 -0.1287 -0.1068 0.0594 54 ASP A CB 419 C CG . ASP A 54 ? 0.9404 1.3942 0.8601 -0.1137 -0.1051 0.0630 54 ASP A CG 420 O OD1 . ASP A 54 ? 0.9085 1.3479 0.8304 -0.0931 -0.1003 0.0609 54 ASP A OD1 421 O OD2 . ASP A 54 ? 0.9426 1.4521 0.8666 -0.1224 -0.1085 0.0678 54 ASP A OD2 422 N N . CYS A 55 ? 0.9563 1.2335 0.8414 -0.1637 -0.1080 0.0501 55 CYS A N 423 C CA . CYS A 55 ? 0.9898 1.2189 0.8637 -0.1666 -0.1085 0.0454 55 CYS A CA 424 C C . CYS A 55 ? 0.9571 1.1454 0.8305 -0.1557 -0.1038 0.0401 55 CYS A C 425 O O . CYS A 55 ? 0.9792 1.1683 0.8565 -0.1552 -0.1016 0.0404 55 CYS A O 426 C CB . CYS A 55 ? 1.0200 1.2351 0.8775 -0.1937 -0.1141 0.0465 55 CYS A CB 427 S SG . CYS A 55 ? 1.1171 1.3741 0.9719 -0.2090 -0.1201 0.0516 55 CYS A SG 428 N N . SER A 56 ? 0.9270 1.0827 0.7956 -0.1475 -0.1022 0.0353 56 SER A N 429 C CA . SER A 56 ? 0.9153 1.0340 0.7814 -0.1403 -0.0984 0.0300 56 SER A CA 430 C C . SER A 56 ? 0.9303 1.0160 0.7809 -0.1546 -0.1014 0.0273 56 SER A C 431 O O . SER A 56 ? 0.9292 1.0150 0.7692 -0.1695 -0.1064 0.0293 56 SER A O 432 C CB . SER A 56 ? 0.9169 1.0210 0.7843 -0.1237 -0.0948 0.0261 56 SER A CB 433 O OG . SER A 56 ? 0.9342 1.0195 0.7922 -0.1294 -0.0973 0.0238 56 SER A OG 434 N N . VAL A 57 ? 0.9292 0.9859 0.7762 -0.1491 -0.0986 0.0228 57 VAL A N 435 C CA . VAL A 57 ? 0.9486 0.9706 0.7777 -0.1574 -0.1012 0.0195 57 VAL A CA 436 C C . VAL A 57 ? 0.9611 0.9695 0.7810 -0.1589 -0.1034 0.0173 57 VAL A C 437 O O . VAL A 57 ? 0.9747 0.9654 0.7764 -0.1720 -0.1082 0.0175 57 VAL A O 438 C CB . VAL A 57 ? 0.9489 0.9475 0.7773 -0.1464 -0.0971 0.0143 57 VAL A CB 439 C CG1 . VAL A 57 ? 0.9688 0.9315 0.7761 -0.1499 -0.0998 0.0102 57 VAL A CG1 440 C CG2 . VAL A 57 ? 0.9634 0.9720 0.7981 -0.1470 -0.0956 0.0165 57 VAL A CG2 441 N N . ALA A 58 ? 0.9458 0.9603 0.7754 -0.1462 -0.1002 0.0153 58 ALA A N 442 C CA . ALA A 58 ? 0.9353 0.9408 0.7582 -0.1466 -0.1019 0.0135 58 ALA A CA 443 C C . ALA A 58 ? 0.9404 0.9639 0.7592 -0.1602 -0.1073 0.0184 58 ALA A C 444 O O . ALA A 58 ? 0.9620 0.9682 0.7652 -0.1709 -0.1114 0.0177 58 ALA A O 445 C CB . ALA A 58 ? 0.9141 0.9250 0.7469 -0.1318 -0.0975 0.0114 58 ALA A CB 446 N N . GLY A 59 ? 0.9181 0.9773 0.7494 -0.1592 -0.1073 0.0234 59 GLY A N 447 C CA . GLY A 59 ? 0.9150 1.0014 0.7445 -0.1724 -0.1123 0.0286 59 GLY A CA 448 C C . GLY A 59 ? 0.9504 1.0271 0.7634 -0.1949 -0.1174 0.0306 59 GLY A C 449 O O . GLY A 59 ? 1.0034 1.0847 0.8055 -0.2101 -0.1224 0.0330 59 GLY A O 450 N N . TRP A 60 ? 0.9615 1.0224 0.7698 -0.1979 -0.1164 0.0298 60 TRP A N 451 C CA . TRP A 60 ? 0.9857 1.0288 0.7724 -0.2193 -0.1213 0.0315 60 TRP A CA 452 C C . TRP A 60 ? 1.0179 1.0143 0.7800 -0.2233 -0.1240 0.0271 60 TRP A C 453 O O . TRP A 60 ? 1.0582 1.0448 0.7999 -0.2418 -0.1296 0.0291 60 TRP A O 454 C CB . TRP A 60 ? 1.0031 1.0410 0.7906 -0.2189 -0.1192 0.0317 60 TRP A CB 455 C CG . TRP A 60 ? 1.0369 1.0377 0.7954 -0.2357 -0.1234 0.0314 60 TRP A CG 456 C CD1 . TRP A 60 ? 1.0728 1.0617 0.8056 -0.2595 -0.1299 0.0342 60 TRP A CD1 457 C CD2 . TRP A 60 ? 1.0391 1.0075 0.7873 -0.2299 -0.1218 0.0281 60 TRP A CD2 458 N NE1 . TRP A 60 ? 1.1013 1.0476 0.8055 -0.2684 -0.1324 0.0329 60 TRP A NE1 459 C CE2 . TRP A 60 ? 1.0716 1.0059 0.7856 -0.2494 -0.1276 0.0291 60 TRP A CE2 460 C CE3 . TRP A 60 ? 1.0145 0.9789 0.7771 -0.2105 -0.1162 0.0245 60 TRP A CE3 461 C CZ2 . TRP A 60 ? 1.0939 0.9893 0.7871 -0.2475 -0.1280 0.0265 60 TRP A CZ2 462 C CZ3 . TRP A 60 ? 1.0182 0.9489 0.7634 -0.2094 -0.1165 0.0220 60 TRP A CZ3 463 C CH2 . TRP A 60 ? 1.0622 0.9585 0.7729 -0.2266 -0.1224 0.0229 60 TRP A CH2 464 N N . LEU A 61 ? 1.0270 0.9961 0.7894 -0.2062 -0.1202 0.0211 61 LEU A N 465 C CA . LEU A 61 ? 1.0630 0.9876 0.8004 -0.2062 -0.1223 0.0163 61 LEU A CA 466 C C . LEU A 61 ? 1.0612 0.9817 0.7921 -0.2090 -0.1248 0.0154 61 LEU A C 467 O O . LEU A 61 ? 1.0625 0.9559 0.7664 -0.2219 -0.1299 0.0152 61 LEU A O 468 C CB . LEU A 61 ? 1.0637 0.9693 0.8054 -0.1859 -0.1172 0.0101 61 LEU A CB 469 C CG . LEU A 61 ? 1.0817 0.9794 0.8215 -0.1838 -0.1158 0.0099 61 LEU A CG 470 C CD1 . LEU A 61 ? 1.0937 0.9820 0.8415 -0.1633 -0.1104 0.0039 61 LEU A CD1 471 C CD2 . LEU A 61 ? 1.1121 0.9751 0.8182 -0.1983 -0.1215 0.0107 61 LEU A CD2 472 N N . LEU A 62 ? 1.0268 0.9713 0.7793 -0.1971 -0.1214 0.0149 62 LEU A N 473 C CA . LEU A 62 ? 1.0105 0.9549 0.7589 -0.1992 -0.1235 0.0145 62 LEU A CA 474 C C . LEU A 62 ? 1.0418 1.0056 0.7830 -0.2199 -0.1294 0.0205 62 LEU A C 475 O O . LEU A 62 ? 1.0380 0.9915 0.7653 -0.2285 -0.1332 0.0203 62 LEU A O 476 C CB . LEU A 62 ? 0.9645 0.9303 0.7353 -0.1826 -0.1187 0.0133 62 LEU A CB 477 C CG . LEU A 62 ? 0.9512 0.8984 0.7259 -0.1655 -0.1133 0.0071 62 LEU A CG 478 C CD1 . LEU A 62 ? 0.9396 0.9081 0.7339 -0.1519 -0.1085 0.0071 62 LEU A CD1 479 C CD2 . LEU A 62 ? 0.9672 0.8837 0.7241 -0.1642 -0.1145 0.0020 62 LEU A CD2 480 N N . GLY A 63 ? 1.0490 1.0433 0.7994 -0.2285 -0.1301 0.0257 63 GLY A N 481 C CA . GLY A 63 ? 1.0773 1.0969 0.8209 -0.2506 -0.1356 0.0317 63 GLY A CA 482 C C . GLY A 63 ? 1.0533 1.1195 0.8176 -0.2452 -0.1353 0.0351 63 GLY A C 483 O O . GLY A 63 ? 1.0701 1.1468 0.8264 -0.2576 -0.1397 0.0373 63 GLY A O 484 N N . ASN A 64 ? 1.0133 1.1059 0.8016 -0.2258 -0.1302 0.0353 64 ASN A N 485 C CA . ASN A 64 ? 0.9936 1.1337 0.7992 -0.2183 -0.1301 0.0392 64 ASN A CA 486 C C . ASN A 64 ? 1.0324 1.2108 0.8337 -0.2410 -0.1356 0.0456 64 ASN A C 487 O O . ASN A 64 ? 1.0493 1.2317 0.8447 -0.2561 -0.1370 0.0480 64 ASN A O 488 C CB . ASN A 64 ? 0.9621 1.1210 0.7873 -0.1971 -0.1244 0.0392 64 ASN A CB 489 C CG . ASN A 64 ? 0.9436 1.1480 0.7831 -0.1838 -0.1240 0.0428 64 ASN A CG 490 O OD1 . ASN A 64 ? 0.9302 1.1728 0.7703 -0.1946 -0.1282 0.0475 64 ASN A OD1 491 N ND2 . ASN A 64 ? 0.9376 1.1382 0.7861 -0.1598 -0.1190 0.0405 64 ASN A ND2 492 N N . PRO A 65 ? 1.0681 1.2756 0.8709 -0.2448 -0.1389 0.0484 65 PRO A N 493 C CA . PRO A 65 ? 1.0925 1.3421 0.8907 -0.2684 -0.1445 0.0545 65 PRO A CA 494 C C . PRO A 65 ? 1.0960 1.4004 0.9107 -0.2661 -0.1433 0.0592 65 PRO A C 495 O O . PRO A 65 ? 1.1236 1.4623 0.9328 -0.2895 -0.1475 0.0642 65 PRO A O 496 C CB . PRO A 65 ? 1.0862 1.3574 0.8865 -0.2652 -0.1471 0.0556 65 PRO A CB 497 C CG . PRO A 65 ? 1.0597 1.3167 0.8728 -0.2342 -0.1419 0.0515 65 PRO A CG 498 C CD . PRO A 65 ? 1.0542 1.2578 0.8617 -0.2284 -0.1379 0.0460 65 PRO A CD 499 N N . MET A 66 ? 1.0885 1.4013 0.9213 -0.2389 -0.1376 0.0577 66 MET A N 500 C CA . MET A 66 ? 1.0876 1.4449 0.9347 -0.2334 -0.1357 0.0614 66 MET A CA 501 C C . MET A 66 ? 1.0790 1.4132 0.9193 -0.2473 -0.1348 0.0610 66 MET A C 502 O O . MET A 66 ? 1.0485 1.4184 0.8976 -0.2491 -0.1338 0.0643 66 MET A O 503 C CB . MET A 66 ? 1.0884 1.4544 0.9517 -0.1988 -0.1301 0.0596 66 MET A CB 504 C CG . MET A 66 ? 1.1010 1.4947 0.9693 -0.1817 -0.1310 0.0607 66 MET A CG 505 S SD . MET A 66 ? 1.1350 1.6151 1.0127 -0.1850 -0.1348 0.0680 66 MET A SD 506 C CE . MET A 66 ? 1.1379 1.6345 1.0174 -0.1579 -0.1353 0.0677 66 MET A CE 507 N N . CYS A 67 ? 1.0816 1.3569 0.9050 -0.2560 -0.1352 0.0568 67 CYS A N 508 C CA . CYS A 67 ? 1.0751 1.3193 0.8881 -0.2660 -0.1344 0.0556 67 CYS A CA 509 C C . CYS A 67 ? 1.0863 1.3082 0.8709 -0.2989 -0.1406 0.0574 67 CYS A C 510 O O . CYS A 67 ? 1.0888 1.2599 0.8541 -0.3053 -0.1410 0.0543 67 CYS A O 511 C CB . CYS A 67 ? 1.0761 1.2685 0.8889 -0.2464 -0.1297 0.0490 67 CYS A CB 512 S SG . CYS A 67 ? 1.0771 1.2875 0.9160 -0.2113 -0.1227 0.0469 67 CYS A SG 513 N N . ASP A 68 ? 1.0872 1.3474 0.8668 -0.3197 -0.1456 0.0624 68 ASP A N 514 C CA . ASP A 68 ? 1.1225 1.3635 0.8707 -0.3548 -0.1521 0.0649 68 ASP A CA 515 C C . ASP A 68 ? 1.1386 1.3754 0.8748 -0.3730 -0.1528 0.0673 68 ASP A C 516 O O . ASP A 68 ? 1.1818 1.3738 0.8845 -0.3964 -0.1570 0.0672 68 ASP A O 517 C CB . ASP A 68 ? 1.1308 1.4224 0.8779 -0.3743 -0.1571 0.0701 68 ASP A CB 518 C CG . ASP A 68 ? 1.1289 1.4117 0.8775 -0.3636 -0.1581 0.0677 68 ASP A CG 519 O OD1 . ASP A 68 ? 1.1292 1.3680 0.8800 -0.3416 -0.1546 0.0619 68 ASP A OD1 520 O OD2 . ASP A 68 ? 1.1312 1.4535 0.8787 -0.3780 -0.1623 0.0715 68 ASP A OD2 521 N N . GLU A 69 ? 1.1038 1.3842 0.8642 -0.3616 -0.1489 0.0696 69 GLU A N 522 C CA . GLU A 69 ? 1.1019 1.3798 0.8543 -0.3754 -0.1487 0.0717 69 GLU A CA 523 C C . GLU A 69 ? 1.1077 1.3105 0.8379 -0.3730 -0.1479 0.0667 69 GLU A C 524 O O . GLU A 69 ? 1.0987 1.2760 0.8025 -0.3958 -0.1510 0.0683 69 GLU A O 525 C CB . GLU A 69 ? 1.0715 1.3993 0.8564 -0.3537 -0.1431 0.0731 69 GLU A CB 526 C CG . GLU A 69 ? 1.0778 1.4109 0.8571 -0.3677 -0.1427 0.0757 69 GLU A CG 527 C CD . GLU A 69 ? 1.0409 1.4213 0.8512 -0.3444 -0.1370 0.0767 69 GLU A CD 528 O OE1 . GLU A 69 ? 1.0280 1.4375 0.8618 -0.3172 -0.1336 0.0757 69 GLU A OE1 529 O OE2 . GLU A 69 ? 1.0227 1.4086 0.8310 -0.3530 -0.1360 0.0786 69 GLU A OE2 530 N N . PHE A 70 ? 1.1173 1.2857 0.8560 -0.3456 -0.1440 0.0607 70 PHE A N 531 C CA . PHE A 70 ? 1.1506 1.2561 0.8735 -0.3363 -0.1423 0.0553 70 PHE A CA 532 C C . PHE A 70 ? 1.2136 1.2624 0.9062 -0.3419 -0.1461 0.0515 70 PHE A C 533 O O . PHE A 70 ? 1.2183 1.2220 0.9045 -0.3243 -0.1437 0.0457 70 PHE A O 534 C CB . PHE A 70 ? 1.0950 1.2043 0.8474 -0.3022 -0.1350 0.0511 70 PHE A CB 535 C CG . PHE A 70 ? 1.0588 1.2241 0.8397 -0.2935 -0.1314 0.0547 70 PHE A CG 536 C CD1 . PHE A 70 ? 1.0352 1.2105 0.8141 -0.3037 -0.1311 0.0575 70 PHE A CD1 537 C CD2 . PHE A 70 ? 1.0346 1.2425 0.8410 -0.2756 -0.1287 0.0555 70 PHE A CD2 538 C CE1 . PHE A 70 ? 1.0100 1.2382 0.8138 -0.2949 -0.1278 0.0607 70 PHE A CE1 539 C CE2 . PHE A 70 ? 1.0143 1.2725 0.8431 -0.2654 -0.1256 0.0587 70 PHE A CE2 540 C CZ . PHE A 70 ? 0.9948 1.2645 0.8231 -0.2749 -0.1250 0.0612 70 PHE A CZ 541 N N . ILE A 71 ? 1.2785 1.3321 0.9514 -0.3666 -0.1520 0.0547 71 ILE A N 542 C CA . ILE A 71 ? 1.3498 1.3468 0.9856 -0.3776 -0.1568 0.0519 71 ILE A CA 543 C C . ILE A 71 ? 1.4183 1.3713 1.0132 -0.4009 -0.1612 0.0532 71 ILE A C 544 O O . ILE A 71 ? 1.4582 1.4377 1.0453 -0.4269 -0.1642 0.0590 71 ILE A O 545 C CB . ILE A 71 ? 1.3980 1.4195 1.0291 -0.3948 -0.1614 0.0551 71 ILE A CB 546 C CG1 . ILE A 71 ? 1.4375 1.4025 1.0398 -0.3942 -0.1644 0.0505 71 ILE A CG1 547 C CG2 . ILE A 71 ? 1.4182 1.4678 1.0309 -0.4325 -0.1672 0.0621 71 ILE A CG2 548 C CD1 . ILE A 71 ? 1.4274 1.4167 1.0292 -0.4066 -0.1682 0.0529 71 ILE A CD1 549 N N . ASN A 72 ? 1.4449 1.3323 1.0126 -0.3906 -0.1615 0.0479 72 ASN A N 550 C CA . ASN A 72 ? 1.4736 1.3101 0.9983 -0.4073 -0.1655 0.0483 72 ASN A CA 551 C C . ASN A 72 ? 1.4224 1.2875 0.9605 -0.4133 -0.1633 0.0521 72 ASN A C 552 O O . ASN A 72 ? 1.4427 1.3250 0.9650 -0.4442 -0.1674 0.0580 72 ASN A O 553 C CB . ASN A 72 ? 1.5300 1.3382 1.0068 -0.4434 -0.1739 0.0518 72 ASN A CB 554 C CG . ASN A 72 ? 1.5826 1.3601 1.0430 -0.4386 -0.1763 0.0482 72 ASN A CG 555 O OD1 . ASN A 72 ? 1.5680 1.3286 1.0422 -0.4080 -0.1723 0.0421 72 ASN A OD1 556 N ND2 . ASN A 72 ? 1.6482 1.4199 1.0782 -0.4699 -0.1830 0.0520 72 ASN A ND2 557 N N . VAL A 73 ? 1.3596 1.2308 0.9259 -0.3848 -0.1569 0.0486 73 VAL A N 558 C CA . VAL A 73 ? 1.3298 1.2256 0.9101 -0.3867 -0.1543 0.0515 73 VAL A CA 559 C C . VAL A 73 ? 1.3579 1.1927 0.8982 -0.3920 -0.1568 0.0499 73 VAL A C 560 O O . VAL A 73 ? 1.3798 1.1587 0.8967 -0.3766 -0.1574 0.0443 73 VAL A O 561 C CB . VAL A 73 ? 1.2630 1.1962 0.8921 -0.3543 -0.1462 0.0489 73 VAL A CB 562 C CG1 . VAL A 73 ? 1.2223 1.2115 0.8868 -0.3465 -0.1438 0.0505 73 VAL A CG1 563 C CG2 . VAL A 73 ? 1.2591 1.1475 0.8862 -0.3256 -0.1427 0.0415 73 VAL A CG2 564 N N . PRO A 74 ? 1.3573 1.2037 0.8884 -0.4124 -0.1583 0.0547 74 PRO A N 565 C CA . PRO A 74 ? 1.3863 1.1733 0.8770 -0.4173 -0.1608 0.0535 74 PRO A CA 566 C C . PRO A 74 ? 1.3524 1.1305 0.8653 -0.3833 -0.1547 0.0484 74 PRO A C 567 O O . PRO A 74 ? 1.2780 1.0986 0.8378 -0.3593 -0.1483 0.0464 74 PRO A O 568 C CB . PRO A 74 ? 1.3961 1.2103 0.8767 -0.4507 -0.1637 0.0608 74 PRO A CB 569 C CG . PRO A 74 ? 1.3449 1.2445 0.8794 -0.4469 -0.1590 0.0642 74 PRO A CG 570 C CD . PRO A 74 ? 1.3296 1.2461 0.8875 -0.4295 -0.1573 0.0613 74 PRO A CD 571 N N . GLU A 75 ? 1.3817 1.1031 0.8577 -0.3819 -0.1569 0.0463 75 GLU A N 572 C CA . GLU A 75 ? 1.3475 1.0591 0.8391 -0.3527 -0.1517 0.0419 75 GLU A CA 573 C C . GLU A 75 ? 1.2874 1.0640 0.8290 -0.3471 -0.1456 0.0447 75 GLU A C 574 O O . GLU A 75 ? 1.2484 1.0600 0.7944 -0.3710 -0.1468 0.0508 75 GLU A O 575 C CB . GLU A 75 ? 1.4046 1.0519 0.8448 -0.3593 -0.1562 0.0413 75 GLU A CB 576 C CG . GLU A 75 ? 1.3950 1.0266 0.8450 -0.3284 -0.1517 0.0362 75 GLU A CG 577 C CD . GLU A 75 ? 1.4384 1.0070 0.8352 -0.3345 -0.1565 0.0360 75 GLU A CD 578 O OE1 . GLU A 75 ? 1.4891 1.0136 0.8338 -0.3609 -0.1637 0.0389 75 GLU A OE1 579 O OE2 . GLU A 75 ? 1.4213 0.9830 0.8262 -0.3130 -0.1531 0.0330 75 GLU A OE2 580 N N . TRP A 76 ? 1.2630 1.0562 0.8403 -0.3157 -0.1390 0.0401 76 TRP A N 581 C CA . TRP A 76 ? 1.2317 1.0800 0.8535 -0.3064 -0.1329 0.0420 76 TRP A CA 582 C C . TRP A 76 ? 1.2225 1.0517 0.8471 -0.2870 -0.1293 0.0385 76 TRP A C 583 O O . TRP A 76 ? 1.2519 1.0312 0.8507 -0.2744 -0.1306 0.0337 76 TRP A O 584 C CB . TRP A 76 ? 1.1772 1.0701 0.8412 -0.2885 -0.1279 0.0405 76 TRP A CB 585 C CG . TRP A 76 ? 1.1952 1.0635 0.8644 -0.2618 -0.1249 0.0335 76 TRP A CG 586 C CD1 . TRP A 76 ? 1.2005 1.0690 0.8890 -0.2370 -0.1194 0.0290 76 TRP A CD1 587 C CD2 . TRP A 76 ? 1.2175 1.0600 0.8716 -0.2582 -0.1273 0.0301 76 TRP A CD2 588 N NE1 . TRP A 76 ? 1.1981 1.0455 0.8849 -0.2189 -0.1182 0.0231 76 TRP A NE1 589 C CE2 . TRP A 76 ? 1.2085 1.0393 0.8746 -0.2306 -0.1229 0.0235 76 TRP A CE2 590 C CE3 . TRP A 76 ? 1.2437 1.0732 0.8746 -0.2764 -0.1328 0.0319 76 TRP A CE3 591 C CZ2 . TRP A 76 ? 1.2150 1.0232 0.8714 -0.2200 -0.1236 0.0188 76 TRP A CZ2 592 C CZ3 . TRP A 76 ? 1.2567 1.0602 0.8775 -0.2651 -0.1336 0.0271 76 TRP A CZ3 593 C CH2 . TRP A 76 ? 1.2451 1.0389 0.8790 -0.2367 -0.1290 0.0206 76 TRP A CH2 594 N N . SER A 77 ? 1.1702 1.0408 0.8248 -0.2840 -0.1249 0.0410 77 SER A N 595 C CA . SER A 77 ? 1.1526 1.0142 0.8154 -0.2662 -0.1209 0.0383 77 SER A CA 596 C C . SER A 77 ? 1.1117 0.9975 0.8125 -0.2377 -0.1141 0.0337 77 SER A C 597 O O . SER A 77 ? 1.1177 0.9800 0.8174 -0.2175 -0.1118 0.0283 77 SER A O 598 C CB . SER A 77 ? 1.1261 1.0186 0.7985 -0.2800 -0.1199 0.0436 77 SER A CB 599 O OG . SER A 77 ? 1.0726 1.0241 0.7748 -0.2872 -0.1180 0.0480 77 SER A OG 600 N N . TYR A 78 ? 1.0565 0.9904 0.7885 -0.2368 -0.1112 0.0361 78 TYR A N 601 C CA . TYR A 78 ? 1.0017 0.9567 0.7648 -0.2135 -0.1055 0.0324 78 TYR A CA 602 C C . TYR A 78 ? 0.9988 0.9852 0.7756 -0.2179 -0.1060 0.0347 78 TYR A C 603 O O . TYR A 78 ? 1.0061 1.0065 0.7733 -0.2388 -0.1102 0.0396 78 TYR A O 604 C CB . TYR A 78 ? 0.9499 0.9325 0.7393 -0.2011 -0.0997 0.0327 78 TYR A CB 605 C CG . TYR A 78 ? 0.9047 0.9299 0.7069 -0.2137 -0.0995 0.0390 78 TYR A CG 606 C CD1 . TYR A 78 ? 0.9076 0.9286 0.6933 -0.2321 -0.1024 0.0429 78 TYR A CD1 607 C CD2 . TYR A 78 ? 0.8657 0.9356 0.6944 -0.2064 -0.0964 0.0410 78 TYR A CD2 608 C CE1 . TYR A 78 ? 0.8839 0.9494 0.6817 -0.2440 -0.1021 0.0486 78 TYR A CE1 609 C CE2 . TYR A 78 ? 0.8498 0.9634 0.6898 -0.2153 -0.0961 0.0465 78 TYR A CE2 610 C CZ . TYR A 78 ? 0.8558 0.9697 0.6817 -0.2346 -0.0988 0.0504 78 TYR A CZ 611 O OH . TYR A 78 ? 0.8136 0.9766 0.6516 -0.2434 -0.0983 0.0558 78 TYR A OH 612 N N . ILE A 79 ? 0.9797 0.9766 0.7767 -0.1992 -0.1019 0.0313 79 ILE A N 613 C CA . ILE A 79 ? 0.9486 0.9739 0.7588 -0.1994 -0.1020 0.0330 79 ILE A CA 614 C C . ILE A 79 ? 0.9142 0.9801 0.7534 -0.1857 -0.0968 0.0345 79 ILE A C 615 O O . ILE A 79 ? 0.8865 0.9484 0.7363 -0.1705 -0.0921 0.0316 79 ILE A O 616 C CB . ILE A 79 ? 0.9656 0.9675 0.7718 -0.1885 -0.1018 0.0279 79 ILE A CB 617 C CG1 . ILE A 79 ? 1.0184 0.9777 0.7918 -0.2002 -0.1073 0.0263 79 ILE A CG1 618 C CG2 . ILE A 79 ? 0.9556 0.9866 0.7763 -0.1863 -0.1014 0.0295 79 ILE A CG2 619 C CD1 . ILE A 79 ? 1.0309 0.9644 0.7980 -0.1872 -0.1067 0.0204 79 ILE A CD1 620 N N . VAL A 80 ? 0.9080 1.0126 0.7575 -0.1906 -0.0977 0.0389 80 VAL A N 621 C CA . VAL A 80 ? 0.8797 1.0211 0.7522 -0.1745 -0.0933 0.0402 80 VAL A CA 622 C C . VAL A 80 ? 0.8671 1.0199 0.7457 -0.1657 -0.0933 0.0396 80 VAL A C 623 O O . VAL A 80 ? 0.8686 1.0244 0.7385 -0.1783 -0.0976 0.0412 80 VAL A O 624 C CB . VAL A 80 ? 0.8683 1.0533 0.7480 -0.1837 -0.0940 0.0461 80 VAL A CB 625 C CG1 . VAL A 80 ? 0.8454 1.0639 0.7449 -0.1628 -0.0892 0.0469 80 VAL A CG1 626 C CG2 . VAL A 80 ? 0.8856 1.0565 0.7555 -0.1960 -0.0948 0.0471 80 VAL A CG2 627 N N . GLU A 81 ? 0.8503 1.0071 0.7410 -0.1449 -0.0885 0.0373 81 GLU A N 628 C CA . GLU A 81 ? 0.8613 1.0227 0.7549 -0.1343 -0.0881 0.0362 81 GLU A CA 629 C C . GLU A 81 ? 0.8614 1.0449 0.7663 -0.1145 -0.0839 0.0370 81 GLU A C 630 O O . GLU A 81 ? 0.8785 1.0537 0.7869 -0.1051 -0.0799 0.0354 81 GLU A O 631 C CB . GLU A 81 ? 0.8784 0.9997 0.7647 -0.1292 -0.0869 0.0303 81 GLU A CB 632 C CG . GLU A 81 ? 0.8963 1.0173 0.7831 -0.1200 -0.0865 0.0289 81 GLU A CG 633 C CD . GLU A 81 ? 0.9165 1.0016 0.7955 -0.1170 -0.0853 0.0231 81 GLU A CD 634 O OE1 . GLU A 81 ? 0.9168 0.9834 0.7960 -0.1108 -0.0818 0.0193 81 GLU A OE1 635 O OE2 . GLU A 81 ? 0.9145 0.9928 0.7873 -0.1210 -0.0879 0.0223 81 GLU A OE2 636 N N . LYS A 82 ? 0.8689 1.0790 0.7767 -0.1072 -0.0849 0.0396 82 LYS A N 637 C CA . LYS A 82 ? 0.8796 1.1051 0.7919 -0.0853 -0.0813 0.0401 82 LYS A CA 638 C C . LYS A 82 ? 0.8934 1.0812 0.7995 -0.0716 -0.0774 0.0350 82 LYS A C 639 O O . LYS A 82 ? 0.8628 1.0209 0.7635 -0.0781 -0.0779 0.0313 82 LYS A O 640 C CB . LYS A 82 ? 0.8849 1.1491 0.7990 -0.0792 -0.0839 0.0441 82 LYS A CB 641 C CG . LYS A 82 ? 0.8900 1.2026 0.8113 -0.0897 -0.0866 0.0496 82 LYS A CG 642 C CD . LYS A 82 ? 0.8959 1.2540 0.8196 -0.0796 -0.0887 0.0534 82 LYS A CD 643 C CE . LYS A 82 ? 0.9098 1.3238 0.8419 -0.0833 -0.0898 0.0586 82 LYS A CE 644 N NZ . LYS A 82 ? 0.9303 1.3546 0.8625 -0.1146 -0.0935 0.0612 82 LYS A NZ 645 N N . ALA A 83 ? 0.9105 1.0995 0.8149 -0.0530 -0.0737 0.0347 83 ALA A N 646 C CA . ALA A 83 ? 0.9346 1.0886 0.8290 -0.0415 -0.0700 0.0304 83 ALA A CA 647 C C . ALA A 83 ? 0.9520 1.0957 0.8378 -0.0381 -0.0717 0.0293 83 ALA A C 648 O O . ALA A 83 ? 0.9452 1.0575 0.8239 -0.0409 -0.0704 0.0251 83 ALA A O 649 C CB . ALA A 83 ? 0.9343 1.0899 0.8232 -0.0227 -0.0663 0.0309 83 ALA A CB 650 N N . ASN A 84 ? 0.9554 1.1283 0.8416 -0.0321 -0.0746 0.0331 84 ASN A N 651 C CA . ASN A 84 ? 0.9698 1.1367 0.8475 -0.0279 -0.0767 0.0327 84 ASN A CA 652 C C . ASN A 84 ? 0.9388 1.1409 0.8240 -0.0378 -0.0818 0.0366 84 ASN A C 653 O O . ASN A 84 ? 0.9304 1.1643 0.8150 -0.0263 -0.0835 0.0402 84 ASN A O 654 C CB . ASN A 84 ? 1.0191 1.1808 0.8822 -0.0042 -0.0747 0.0331 84 ASN A CB 655 C CG . ASN A 84 ? 1.0655 1.1872 0.9158 0.0025 -0.0699 0.0291 84 ASN A CG 656 O OD1 . ASN A 84 ? 1.0897 1.1789 0.9334 -0.0052 -0.0686 0.0251 84 ASN A OD1 657 N ND2 . ASN A 84 ? 1.0647 1.1901 0.9103 0.0163 -0.0673 0.0302 84 ASN A ND2 658 N N . PRO A 85 ? 0.9132 1.1097 0.8030 -0.0590 -0.0845 0.0360 85 PRO A N 659 C CA . PRO A 85 ? 0.9148 1.1424 0.8086 -0.0727 -0.0897 0.0398 85 PRO A CA 660 C C . PRO A 85 ? 0.9146 1.1458 0.8023 -0.0664 -0.0920 0.0401 85 PRO A C 661 O O . PRO A 85 ? 0.9222 1.1189 0.8020 -0.0644 -0.0910 0.0363 85 PRO A O 662 C CB . PRO A 85 ? 0.9151 1.1198 0.8075 -0.0950 -0.0916 0.0378 85 PRO A CB 663 C CG . PRO A 85 ? 0.8914 1.0629 0.7828 -0.0911 -0.0872 0.0336 85 PRO A CG 664 C CD . PRO A 85 ? 0.8952 1.0553 0.7832 -0.0705 -0.0831 0.0315 85 PRO A CD 665 N N . VAL A 86 ? 0.9192 1.1942 0.8103 -0.0634 -0.0952 0.0448 86 VAL A N 666 C CA . VAL A 86 ? 0.9347 1.2179 0.8196 -0.0548 -0.0976 0.0455 86 VAL A CA 667 C C . VAL A 86 ? 0.9296 1.1973 0.8114 -0.0743 -0.1013 0.0443 86 VAL A C 668 O O . VAL A 86 ? 0.9382 1.1880 0.8122 -0.0678 -0.1017 0.0424 86 VAL A O 669 C CB . VAL A 86 ? 0.9304 1.2716 0.8199 -0.0452 -0.1004 0.0509 86 VAL A CB 670 C CG1 . VAL A 86 ? 0.9281 1.2851 0.8182 -0.0230 -0.0969 0.0520 86 VAL A CG1 671 C CG2 . VAL A 86 ? 0.9285 1.3091 0.8269 -0.0703 -0.1049 0.0549 86 VAL A CG2 672 N N . ASN A 87 ? 0.9178 1.1899 0.8028 -0.0981 -0.1040 0.0454 87 ASN A N 673 C CA . ASN A 87 ? 0.9340 1.1899 0.8122 -0.1176 -0.1079 0.0444 87 ASN A CA 674 C C . ASN A 87 ? 0.9389 1.1424 0.8103 -0.1227 -0.1057 0.0388 87 ASN A C 675 O O . ASN A 87 ? 0.9600 1.1483 0.8270 -0.1398 -0.1073 0.0381 87 ASN A O 676 C CB . ASN A 87 ? 0.9445 1.2304 0.8231 -0.1419 -0.1128 0.0488 87 ASN A CB 677 C CG . ASN A 87 ? 0.9570 1.3008 0.8414 -0.1400 -0.1160 0.0542 87 ASN A CG 678 O OD1 . ASN A 87 ? 0.9677 1.3217 0.8513 -0.1266 -0.1168 0.0544 87 ASN A OD1 679 N ND2 . ASN A 87 ? 0.9680 1.3518 0.8572 -0.1535 -0.1180 0.0587 87 ASN A ND2 680 N N . ASP A 88 ? 0.9369 1.1133 0.8048 -0.1074 -0.1023 0.0349 88 ASP A N 681 C CA . ASP A 88 ? 0.9311 1.0640 0.7929 -0.1099 -0.0999 0.0292 88 ASP A CA 682 C C . ASP A 88 ? 0.9421 1.0597 0.7952 -0.1177 -0.1029 0.0275 88 ASP A C 683 O O . ASP A 88 ? 0.9215 1.0491 0.7710 -0.1335 -0.1077 0.0298 88 ASP A O 684 C CB . ASP A 88 ? 0.9239 1.0389 0.7852 -0.0918 -0.0942 0.0261 88 ASP A CB 685 C CG . ASP A 88 ? 0.9294 1.0091 0.7871 -0.0949 -0.0911 0.0206 88 ASP A CG 686 O OD1 . ASP A 88 ? 0.9236 0.9915 0.7788 -0.1079 -0.0931 0.0191 88 ASP A OD1 687 O OD2 . ASP A 88 ? 0.9660 1.0295 0.8210 -0.0840 -0.0866 0.0177 88 ASP A OD2 688 N N . LEU A 89 ? 0.9481 1.0413 0.7958 -0.1083 -0.1003 0.0235 89 LEU A N 689 C CA . LEU A 89 ? 0.9603 1.0408 0.7999 -0.1132 -0.1028 0.0218 89 LEU A CA 690 C C . LEU A 89 ? 0.9753 1.0811 0.8151 -0.1059 -0.1052 0.0256 89 LEU A C 691 O O . LEU A 89 ? 0.9591 1.0604 0.7957 -0.0900 -0.1026 0.0250 89 LEU A O 692 C CB . LEU A 89 ? 0.9601 1.0072 0.7933 -0.1068 -0.0988 0.0160 89 LEU A CB 693 C CG . LEU A 89 ? 0.9530 0.9777 0.7855 -0.1102 -0.0960 0.0116 89 LEU A CG 694 C CD1 . LEU A 89 ? 0.9603 0.9608 0.7865 -0.1045 -0.0922 0.0061 89 LEU A CD1 695 C CD2 . LEU A 89 ? 0.9514 0.9683 0.7785 -0.1247 -0.0999 0.0112 89 LEU A CD2 696 N N . CYS A 90 ? 1.0087 1.1403 0.8497 -0.1177 -0.1103 0.0296 90 CYS A N 697 C CA . CYS A 90 ? 1.0437 1.2055 0.8849 -0.1119 -0.1134 0.0335 90 CYS A CA 698 C C . CYS A 90 ? 1.0015 1.1406 0.8338 -0.1030 -0.1127 0.0306 90 CYS A C 699 O O . CYS A 90 ? 0.9923 1.1384 0.8217 -0.0855 -0.1115 0.0316 90 CYS A O 700 C CB . CYS A 90 ? 1.1128 1.3013 0.9539 -0.1320 -0.1194 0.0374 90 CYS A CB 701 S SG . CYS A 90 ? 1.2130 1.3631 1.0416 -0.1555 -0.1221 0.0340 90 CYS A SG 702 N N . TYR A 91 ? 0.9842 1.0947 0.8096 -0.1144 -0.1135 0.0269 91 TYR A N 703 C CA . TYR A 91 ? 1.0026 1.0880 0.8190 -0.1076 -0.1121 0.0235 91 TYR A CA 704 C C . TYR A 91 ? 0.9825 1.0392 0.7966 -0.0983 -0.1062 0.0190 91 TYR A C 705 O O . TYR A 91 ? 0.9862 1.0271 0.8020 -0.1052 -0.1043 0.0159 91 TYR A O 706 C CB . TYR A 91 ? 1.0284 1.0961 0.8375 -0.1228 -0.1151 0.0211 91 TYR A CB 707 C CG . TYR A 91 ? 1.0494 1.0999 0.8495 -0.1174 -0.1148 0.0186 91 TYR A CG 708 C CD1 . TYR A 91 ? 1.0512 1.0724 0.8459 -0.1103 -0.1100 0.0136 91 TYR A CD1 709 C CD2 . TYR A 91 ? 1.0465 1.1119 0.8429 -0.1205 -0.1193 0.0213 91 TYR A CD2 710 C CE1 . TYR A 91 ? 1.0745 1.0803 0.8595 -0.1071 -0.1097 0.0114 91 TYR A CE1 711 C CE2 . TYR A 91 ? 1.0488 1.0976 0.8362 -0.1158 -0.1191 0.0191 91 TYR A CE2 712 C CZ . TYR A 91 ? 1.0652 1.0835 0.8466 -0.1093 -0.1142 0.0142 91 TYR A CZ 713 O OH . TYR A 91 ? 1.0689 1.0708 0.8399 -0.1062 -0.1139 0.0120 91 TYR A OH 714 N N . PRO A 92 ? 0.9929 1.0417 0.8003 -0.0830 -0.1035 0.0185 92 PRO A N 715 C CA . PRO A 92 ? 0.9974 1.0221 0.8004 -0.0759 -0.0979 0.0149 92 PRO A CA 716 C C . PRO A 92 ? 1.0211 1.0191 0.8212 -0.0855 -0.0955 0.0092 92 PRO A C 717 O O . PRO A 92 ? 1.0626 1.0530 0.8587 -0.0929 -0.0976 0.0075 92 PRO A O 718 C CB . PRO A 92 ? 1.0046 1.0196 0.7931 -0.0611 -0.0968 0.0155 92 PRO A CB 719 C CG . PRO A 92 ? 1.0119 1.0347 0.7968 -0.0635 -0.1012 0.0170 92 PRO A CG 720 C CD . PRO A 92 ? 1.0104 1.0652 0.8091 -0.0735 -0.1056 0.0205 92 PRO A CD 721 N N . GLY A 93 ? 1.0373 1.0233 0.8389 -0.0846 -0.0912 0.0063 93 GLY A N 722 C CA . GLY A 93 ? 1.0466 1.0131 0.8455 -0.0916 -0.0887 0.0007 93 GLY A CA 723 C C . GLY A 93 ? 1.0298 0.9908 0.8330 -0.0913 -0.0846 -0.0020 93 GLY A C 724 O O . GLY A 93 ? 1.0234 0.9849 0.8261 -0.0843 -0.0818 -0.0008 93 GLY A O 725 N N . ASP A 94 ? 1.0238 0.9784 0.8288 -0.0979 -0.0843 -0.0058 94 ASP A N 726 C CA . ASP A 94 ? 1.0037 0.9551 0.8126 -0.0975 -0.0808 -0.0088 94 ASP A CA 727 C C . ASP A 94 ? 0.9880 0.9387 0.7994 -0.1028 -0.0834 -0.0101 94 ASP A C 728 O O . ASP A 94 ? 1.0025 0.9480 0.8082 -0.1077 -0.0870 -0.0106 94 ASP A O 729 C CB . ASP A 94 ? 1.0204 0.9606 0.8222 -0.0975 -0.0763 -0.0142 94 ASP A CB 730 C CG . ASP A 94 ? 1.0494 0.9830 0.8424 -0.0939 -0.0734 -0.0132 94 ASP A CG 731 O OD1 . ASP A 94 ? 1.0364 0.9711 0.8303 -0.0895 -0.0714 -0.0113 94 ASP A OD1 732 O OD2 . ASP A 94 ? 1.0925 1.0172 0.8749 -0.0956 -0.0733 -0.0145 94 ASP A OD2 733 N N . PHE A 95 ? 0.9388 0.8917 0.7556 -0.1017 -0.0819 -0.0105 95 PHE A N 734 C CA . PHE A 95 ? 0.8951 0.8414 0.7093 -0.1049 -0.0839 -0.0123 95 PHE A CA 735 C C . PHE A 95 ? 0.8765 0.8177 0.6895 -0.1000 -0.0796 -0.0180 95 PHE A C 736 O O . PHE A 95 ? 0.8693 0.8164 0.6886 -0.0967 -0.0760 -0.0182 95 PHE A O 737 C CB . PHE A 95 ? 0.8874 0.8421 0.7073 -0.1078 -0.0860 -0.0079 95 PHE A CB 738 C CG . PHE A 95 ? 0.9000 0.8437 0.7107 -0.1146 -0.0903 -0.0079 95 PHE A CG 739 C CD1 . PHE A 95 ? 0.9075 0.8352 0.7095 -0.1112 -0.0896 -0.0128 95 PHE A CD1 740 C CD2 . PHE A 95 ? 0.9053 0.8543 0.7130 -0.1245 -0.0953 -0.0030 95 PHE A CD2 741 C CE1 . PHE A 95 ? 0.9330 0.8437 0.7201 -0.1163 -0.0940 -0.0129 95 PHE A CE1 742 C CE2 . PHE A 95 ? 0.9261 0.8594 0.7194 -0.1331 -0.0997 -0.0028 95 PHE A CE2 743 C CZ . PHE A 95 ? 0.9390 0.8497 0.7203 -0.1284 -0.0991 -0.0078 95 PHE A CZ 744 N N . ASN A 96 ? 0.8787 0.8110 0.6828 -0.0992 -0.0799 -0.0227 96 ASN A N 745 C CA . ASN A 96 ? 0.8711 0.8049 0.6736 -0.0938 -0.0760 -0.0285 96 ASN A CA 746 C C . ASN A 96 ? 0.8658 0.7986 0.6688 -0.0897 -0.0759 -0.0296 96 ASN A C 747 O O . ASN A 96 ? 0.8505 0.7722 0.6468 -0.0908 -0.0802 -0.0280 96 ASN A O 748 C CB . ASN A 96 ? 0.9025 0.8296 0.6939 -0.0921 -0.0769 -0.0331 96 ASN A CB 749 C CG . ASN A 96 ? 0.9109 0.8477 0.7010 -0.0868 -0.0724 -0.0392 96 ASN A CG 750 O OD1 . ASN A 96 ? 0.9004 0.8478 0.6947 -0.0896 -0.0682 -0.0402 96 ASN A OD1 751 N ND2 . ASN A 96 ? 0.9262 0.8596 0.7079 -0.0791 -0.0734 -0.0435 96 ASN A ND2 752 N N . ASP A 97 ? 0.8720 0.8152 0.6807 -0.0859 -0.0713 -0.0323 97 ASP A N 753 C CA . ASP A 97 ? 0.8759 0.8207 0.6862 -0.0809 -0.0707 -0.0334 97 ASP A CA 754 C C . ASP A 97 ? 0.8559 0.7944 0.6689 -0.0842 -0.0740 -0.0281 97 ASP A C 755 O O . ASP A 97 ? 0.8778 0.8063 0.6833 -0.0818 -0.0766 -0.0285 97 ASP A O 756 C CB . ASP A 97 ? 0.9121 0.8514 0.7104 -0.0726 -0.0718 -0.0389 97 ASP A CB 757 C CG . ASP A 97 ? 0.9257 0.8818 0.7243 -0.0681 -0.0673 -0.0448 97 ASP A CG 758 O OD1 . ASP A 97 ? 0.9326 0.9039 0.7404 -0.0715 -0.0628 -0.0450 97 ASP A OD1 759 O OD2 . ASP A 97 ? 0.9576 0.9122 0.7455 -0.0616 -0.0682 -0.0493 97 ASP A OD2 760 N N . TYR A 98 ? 0.8200 0.7648 0.6414 -0.0892 -0.0739 -0.0231 98 TYR A N 761 C CA . TYR A 98 ? 0.8080 0.7536 0.6329 -0.0939 -0.0771 -0.0174 98 TYR A CA 762 C C . TYR A 98 ? 0.8148 0.7635 0.6446 -0.0915 -0.0756 -0.0169 98 TYR A C 763 O O . TYR A 98 ? 0.8120 0.7554 0.6380 -0.0954 -0.0790 -0.0142 98 TYR A O 764 C CB . TYR A 98 ? 0.7869 0.7438 0.6196 -0.0959 -0.0765 -0.0129 98 TYR A CB 765 C CG . TYR A 98 ? 0.7723 0.7383 0.6094 -0.1007 -0.0798 -0.0069 98 TYR A CG 766 C CD1 . TYR A 98 ? 0.7831 0.7440 0.6128 -0.1089 -0.0851 -0.0047 98 TYR A CD1 767 C CD2 . TYR A 98 ? 0.7577 0.7383 0.6039 -0.0974 -0.0778 -0.0032 98 TYR A CD2 768 C CE1 . TYR A 98 ? 0.7880 0.7625 0.6214 -0.1158 -0.0881 0.0009 98 TYR A CE1 769 C CE2 . TYR A 98 ? 0.7483 0.7438 0.5992 -0.1012 -0.0806 0.0022 98 TYR A CE2 770 C CZ . TYR A 98 ? 0.7718 0.7667 0.6174 -0.1114 -0.0857 0.0044 98 TYR A CZ 771 O OH . TYR A 98 ? 0.7813 0.7957 0.6309 -0.1176 -0.0886 0.0100 98 TYR A OH 772 N N . GLU A 99 ? 0.8276 0.7840 0.6637 -0.0867 -0.0707 -0.0193 99 GLU A N 773 C CA . GLU A 99 ? 0.8444 0.8051 0.6859 -0.0841 -0.0689 -0.0190 99 GLU A CA 774 C C . GLU A 99 ? 0.8543 0.8053 0.6867 -0.0798 -0.0705 -0.0226 99 GLU A C 775 O O . GLU A 99 ? 0.8590 0.8053 0.6897 -0.0801 -0.0723 -0.0208 99 GLU A O 776 C CB . GLU A 99 ? 0.8429 0.8132 0.6907 -0.0815 -0.0634 -0.0207 99 GLU A CB 777 C CG . GLU A 99 ? 0.8569 0.8316 0.7091 -0.0830 -0.0620 -0.0165 99 GLU A CG 778 C CD . GLU A 99 ? 0.8731 0.8444 0.7202 -0.0848 -0.0629 -0.0160 99 GLU A CD 779 O OE1 . GLU A 99 ? 0.9004 0.8680 0.7416 -0.0858 -0.0623 -0.0201 99 GLU A OE1 780 O OE2 . GLU A 99 ? 0.8723 0.8463 0.7207 -0.0845 -0.0642 -0.0116 99 GLU A OE2 781 N N . GLU A 100 ? 0.8567 0.8046 0.6811 -0.0750 -0.0701 -0.0278 100 GLU A N 782 C CA . GLU A 100 ? 0.8611 0.7984 0.6724 -0.0672 -0.0720 -0.0318 100 GLU A CA 783 C C . GLU A 100 ? 0.8756 0.7902 0.6719 -0.0710 -0.0781 -0.0289 100 GLU A C 784 O O . GLU A 100 ? 0.9079 0.8077 0.6908 -0.0662 -0.0804 -0.0301 100 GLU A O 785 C CB . GLU A 100 ? 0.8601 0.8014 0.6646 -0.0603 -0.0706 -0.0378 100 GLU A CB 786 C CG . GLU A 100 ? 0.8565 0.8211 0.6703 -0.0569 -0.0649 -0.0417 100 GLU A CG 787 C CD . GLU A 100 ? 0.8547 0.8256 0.6671 -0.0478 -0.0638 -0.0445 100 GLU A CD 788 O OE1 . GLU A 100 ? 0.8811 0.8401 0.6789 -0.0377 -0.0669 -0.0471 100 GLU A OE1 789 O OE2 . GLU A 100 ? 0.8300 0.8162 0.6537 -0.0499 -0.0600 -0.0441 100 GLU A OE2 790 N N . LEU A 101 ? 0.8571 0.7678 0.6529 -0.0804 -0.0808 -0.0251 101 LEU A N 791 C CA . LEU A 101 ? 0.8820 0.7728 0.6622 -0.0884 -0.0867 -0.0217 101 LEU A CA 792 C C . LEU A 101 ? 0.8741 0.7691 0.6601 -0.0953 -0.0876 -0.0166 101 LEU A C 793 O O . LEU A 101 ? 0.8748 0.7511 0.6446 -0.0975 -0.0910 -0.0159 101 LEU A O 794 C CB . LEU A 101 ? 0.8792 0.7700 0.6583 -0.0975 -0.0894 -0.0190 101 LEU A CB 795 C CG . LEU A 101 ? 0.9010 0.7723 0.6613 -0.1094 -0.0959 -0.0153 101 LEU A CG 796 C CD1 . LEU A 101 ? 0.9159 0.7545 0.6476 -0.1046 -0.0994 -0.0189 101 LEU A CD1 797 C CD2 . LEU A 101 ? 0.9242 0.7989 0.6844 -0.1168 -0.0981 -0.0136 101 LEU A CD2 798 N N . LYS A 102 ? 0.8572 0.7752 0.6634 -0.0983 -0.0845 -0.0132 102 LYS A N 799 C CA . LYS A 102 ? 0.8539 0.7815 0.6681 -0.1030 -0.0844 -0.0087 102 LYS A CA 800 C C . LYS A 102 ? 0.8560 0.7743 0.6649 -0.0969 -0.0834 -0.0111 102 LYS A C 801 O O . LYS A 102 ? 0.8755 0.7878 0.6785 -0.1029 -0.0858 -0.0079 102 LYS A O 802 C CB . LYS A 102 ? 0.8528 0.8049 0.6874 -0.1010 -0.0801 -0.0064 102 LYS A CB 803 C CG . LYS A 102 ? 0.8720 0.8373 0.7115 -0.1075 -0.0820 -0.0018 102 LYS A CG 804 C CD . LYS A 102 ? 0.8776 0.8624 0.7319 -0.1017 -0.0779 0.0000 102 LYS A CD 805 C CE . LYS A 102 ? 0.9024 0.9065 0.7619 -0.1064 -0.0802 0.0059 102 LYS A CE 806 N NZ . LYS A 102 ? 0.9068 0.9272 0.7764 -0.0978 -0.0765 0.0078 102 LYS A NZ 807 N N . HIS A 103 ? 0.8509 0.7696 0.6609 -0.0854 -0.0800 -0.0166 103 HIS A N 808 C CA . HIS A 103 ? 0.8564 0.7684 0.6604 -0.0773 -0.0792 -0.0195 103 HIS A CA 809 C C . HIS A 103 ? 0.9027 0.7847 0.6797 -0.0768 -0.0847 -0.0202 103 HIS A C 810 O O . HIS A 103 ? 0.9372 0.8082 0.7053 -0.0757 -0.0861 -0.0194 103 HIS A O 811 C CB . HIS A 103 ? 0.8461 0.7697 0.6553 -0.0656 -0.0747 -0.0255 103 HIS A CB 812 C CG . HIS A 103 ? 0.8375 0.7604 0.6425 -0.0559 -0.0735 -0.0286 103 HIS A CG 813 N ND1 . HIS A 103 ? 0.8220 0.7597 0.6411 -0.0559 -0.0700 -0.0273 103 HIS A ND1 814 C CD2 . HIS A 103 ? 0.8502 0.7589 0.6367 -0.0446 -0.0756 -0.0328 103 HIS A CD2 815 C CE1 . HIS A 103 ? 0.8347 0.7694 0.6460 -0.0460 -0.0699 -0.0306 103 HIS A CE1 816 N NE2 . HIS A 103 ? 0.8537 0.7711 0.6447 -0.0380 -0.0734 -0.0340 103 HIS A NE2 817 N N . LEU A 104 ? 0.9297 0.7955 0.6908 -0.0773 -0.0879 -0.0219 104 LEU A N 818 C CA . LEU A 104 ? 0.9878 0.8180 0.7165 -0.0776 -0.0938 -0.0225 104 LEU A CA 819 C C . LEU A 104 ? 1.0113 0.8291 0.7304 -0.0945 -0.0981 -0.0161 104 LEU A C 820 O O . LEU A 104 ? 1.0313 0.8206 0.7248 -0.0951 -0.1019 -0.0158 104 LEU A O 821 C CB . LEU A 104 ? 1.0206 0.8354 0.7332 -0.0763 -0.0965 -0.0251 104 LEU A CB 822 C CG . LEU A 104 ? 1.0414 0.8449 0.7375 -0.0571 -0.0961 -0.0323 104 LEU A CG 823 C CD1 . LEU A 104 ? 1.0307 0.8676 0.7508 -0.0451 -0.0895 -0.0364 104 LEU A CD1 824 C CD2 . LEU A 104 ? 1.0692 0.8594 0.7512 -0.0579 -0.0987 -0.0341 104 LEU A CD2 825 N N . LEU A 105 ? 1.0239 0.8638 0.7617 -0.1079 -0.0976 -0.0110 105 LEU A N 826 C CA . LEU A 105 ? 1.0410 0.8797 0.7732 -0.1259 -0.1013 -0.0045 105 LEU A CA 827 C C . LEU A 105 ? 1.0553 0.8984 0.7919 -0.1265 -0.1001 -0.0024 105 LEU A C 828 O O . LEU A 105 ? 1.0965 0.9280 0.8177 -0.1408 -0.1040 0.0018 105 LEU A O 829 C CB . LEU A 105 ? 1.0117 0.8827 0.7667 -0.1359 -0.1002 0.0001 105 LEU A CB 830 C CG . LEU A 105 ? 1.0240 0.8916 0.7719 -0.1430 -0.1033 0.0006 105 LEU A CG 831 C CD1 . LEU A 105 ? 1.0129 0.9163 0.7833 -0.1509 -0.1022 0.0057 105 LEU A CD1 832 C CD2 . LEU A 105 ? 1.0682 0.9020 0.7815 -0.1567 -0.1101 0.0020 105 LEU A CD2 833 N N . SER A 106 ? 1.2184 0.9543 0.7029 -0.1692 -0.1116 -0.0059 106 SER A N 834 C CA A SER A 106 ? 1.2637 0.9888 0.7286 -0.1697 -0.1130 -0.0051 106 SER A CA 835 C CA B SER A 106 ? 1.2582 0.9833 0.7230 -0.1700 -0.1128 -0.0050 106 SER A CA 836 C C . SER A 106 ? 1.3119 1.0057 0.7451 -0.1648 -0.1199 -0.0009 106 SER A C 837 O O . SER A 106 ? 1.3612 1.0400 0.7703 -0.1660 -0.1201 0.0019 106 SER A O 838 C CB A SER A 106 ? 1.2558 0.9986 0.7363 -0.1615 -0.1168 -0.0111 106 SER A CB 839 C CB B SER A 106 ? 1.2436 0.9872 0.7248 -0.1623 -0.1160 -0.0110 106 SER A CB 840 O OG A SER A 106 ? 1.2631 1.0026 0.7438 -0.1486 -0.1273 -0.0136 106 SER A OG 841 O OG B SER A 106 ? 1.2037 0.9721 0.7138 -0.1658 -0.1084 -0.0139 106 SER A OG 842 N N . ARG A 107 ? 1.3526 1.0360 0.7847 -0.1582 -0.1251 -0.0003 107 ARG A N 843 C CA . ARG A 107 ? 1.4294 1.0804 0.8317 -0.1518 -0.1311 0.0040 107 ARG A CA 844 C C . ARG A 107 ? 1.3953 1.0236 0.7839 -0.1618 -0.1257 0.0076 107 ARG A C 845 O O . ARG A 107 ? 1.4012 0.9994 0.7665 -0.1565 -0.1294 0.0111 107 ARG A O 846 C CB . ARG A 107 ? 1.5177 1.1721 0.9280 -0.1347 -0.1415 0.0008 107 ARG A CB 847 C CG . ARG A 107 ? 1.5917 1.2677 1.0154 -0.1248 -0.1482 -0.0044 107 ARG A CG 848 C CD . ARG A 107 ? 1.6689 1.3651 1.1196 -0.1137 -0.1535 -0.0101 107 ARG A CD 849 N NE . ARG A 107 ? 1.7589 1.4373 1.1996 -0.1043 -0.1583 -0.0080 107 ARG A NE 850 C CZ . ARG A 107 ? 1.7815 1.4737 1.2423 -0.0945 -0.1617 -0.0119 107 ARG A CZ 851 N NH1 . ARG A 107 ? 1.7465 1.4700 1.2395 -0.0933 -0.1604 -0.0178 107 ARG A NH1 852 N NH2 . ARG A 107 ? 1.7974 1.4707 1.2458 -0.0857 -0.1655 -0.0101 107 ARG A NH2 853 N N . ILE A 108 ? 1.3328 0.9755 0.7359 -0.1760 -0.1169 0.0063 108 ILE A N 854 C CA . ILE A 108 ? 1.3370 0.9643 0.7322 -0.1874 -0.1119 0.0070 108 ILE A CA 855 C C . ILE A 108 ? 1.3276 0.9532 0.7156 -0.2057 -0.1014 0.0094 108 ILE A C 856 O O . ILE A 108 ? 1.2787 0.9310 0.6837 -0.2111 -0.0962 0.0078 108 ILE A O 857 C CB . ILE A 108 ? 1.3116 0.9615 0.7329 -0.1872 -0.1119 0.0016 108 ILE A CB 858 C CG1 . ILE A 108 ? 1.3118 0.9601 0.7380 -0.1700 -0.1208 -0.0003 108 ILE A CG1 859 C CG2 . ILE A 108 ? 1.3102 0.9485 0.7249 -0.2011 -0.1068 0.0002 108 ILE A CG2 860 C CD1 . ILE A 108 ? 1.2706 0.9455 0.7237 -0.1667 -0.1204 -0.0050 108 ILE A CD1 861 N N . ASN A 109 ? 1.3508 0.9445 0.7143 -0.2150 -0.0974 0.0128 109 ASN A N 862 C CA . ASN A 109 ? 1.3808 0.9702 0.7365 -0.2340 -0.0862 0.0150 109 ASN A CA 863 C C . ASN A 109 ? 1.3863 0.9788 0.7515 -0.2496 -0.0806 0.0103 109 ASN A C 864 O O . ASN A 109 ? 1.3708 0.9730 0.7402 -0.2664 -0.0711 0.0097 109 ASN A O 865 C CB . ASN A 109 ? 1.4410 0.9901 0.7594 -0.2354 -0.0832 0.0232 109 ASN A CB 866 C CG . ASN A 109 ? 1.4591 1.0122 0.7677 -0.2251 -0.0860 0.0271 109 ASN A CG 867 O OD1 . ASN A 109 ? 1.5051 1.0443 0.7995 -0.2084 -0.0952 0.0295 109 ASN A OD1 868 N ND2 . ASN A 109 ? 1.4501 1.0243 0.7670 -0.2343 -0.0783 0.0267 109 ASN A ND2 869 N N . HIS A 110 ? 1.3867 0.9722 0.7552 -0.2444 -0.0864 0.0061 110 HIS A N 870 C CA . HIS A 110 ? 1.4015 0.9907 0.7782 -0.2591 -0.0823 -0.0002 110 HIS A CA 871 C C . HIS A 110 ? 1.3768 0.9758 0.7671 -0.2497 -0.0899 -0.0069 110 HIS A C 872 O O . HIS A 110 ? 1.3554 0.9340 0.7347 -0.2352 -0.0970 -0.0060 110 HIS A O 873 C CB . HIS A 110 ? 1.4644 1.0111 0.8130 -0.2730 -0.0757 0.0021 110 HIS A CB 874 C CG . HIS A 110 ? 1.4873 1.0414 0.8458 -0.2938 -0.0690 -0.0055 110 HIS A CG 875 N ND1 . HIS A 110 ? 1.5286 1.0456 0.8680 -0.3056 -0.0650 -0.0077 110 HIS A ND1 876 C CD2 . HIS A 110 ? 1.4570 1.0523 0.8429 -0.3047 -0.0659 -0.0123 110 HIS A CD2 877 C CE1 . HIS A 110 ? 1.5283 1.0650 0.8842 -0.3244 -0.0599 -0.0167 110 HIS A CE1 878 N NE2 . HIS A 110 ? 1.4782 1.0638 0.8624 -0.3234 -0.0609 -0.0194 110 HIS A NE2 879 N N . PHE A 111 ? 1.3533 0.9856 0.7673 -0.2573 -0.0881 -0.0136 111 PHE A N 880 C CA . PHE A 111 ? 1.3499 0.9922 0.7746 -0.2521 -0.0934 -0.0209 111 PHE A CA 881 C C . PHE A 111 ? 1.3771 1.0087 0.7961 -0.2705 -0.0894 -0.0284 111 PHE A C 882 O O . PHE A 111 ? 1.3805 1.0200 0.8026 -0.2884 -0.0819 -0.0295 111 PHE A O 883 C CB . PHE A 111 ? 1.3011 0.9906 0.7558 -0.2463 -0.0945 -0.0236 111 PHE A CB 884 C CG . PHE A 111 ? 1.2679 0.9698 0.7326 -0.2276 -0.0987 -0.0188 111 PHE A CG 885 C CD1 . PHE A 111 ? 1.2691 0.9529 0.7255 -0.2120 -0.1054 -0.0177 111 PHE A CD1 886 C CD2 . PHE A 111 ? 1.2215 0.9547 0.7059 -0.2256 -0.0953 -0.0164 111 PHE A CD2 887 C CE1 . PHE A 111 ? 1.2203 0.9185 0.6892 -0.1966 -0.1087 -0.0148 111 PHE A CE1 888 C CE2 . PHE A 111 ? 1.1844 0.9283 0.6796 -0.2103 -0.0982 -0.0134 111 PHE A CE2 889 C CZ . PHE A 111 ? 1.1902 0.9176 0.6785 -0.1966 -0.1049 -0.0129 111 PHE A CZ 890 N N . GLU A 112 ? 1.4058 1.0207 0.8174 -0.2666 -0.0941 -0.0344 112 GLU A N 891 C CA . GLU A 112 ? 1.4231 1.0379 0.8361 -0.2829 -0.0920 -0.0452 112 GLU A CA 892 C C . GLU A 112 ? 1.3512 0.9984 0.7826 -0.2728 -0.0986 -0.0528 112 GLU A C 893 O O . GLU A 112 ? 1.3044 0.9420 0.7311 -0.2558 -0.1047 -0.0527 112 GLU A O 894 C CB . GLU A 112 ? 1.5024 1.0649 0.8873 -0.2890 -0.0905 -0.0472 112 GLU A CB 895 C CG . GLU A 112 ? 1.5567 1.1155 0.9421 -0.3120 -0.0857 -0.0590 112 GLU A CG 896 C CD . GLU A 112 ? 1.6256 1.1376 0.9878 -0.3134 -0.0864 -0.0649 112 GLU A CD 897 O OE1 . GLU A 112 ? 1.6919 1.1567 1.0280 -0.3112 -0.0830 -0.0570 112 GLU A OE1 898 O OE2 . GLU A 112 ? 1.6126 1.1343 0.9814 -0.3161 -0.0903 -0.0776 112 GLU A OE2 899 N N . LYS A 113 ? 1.3235 1.0102 0.7755 -0.2823 -0.0972 -0.0592 113 LYS A N 900 C CA . LYS A 113 ? 1.3140 1.0353 0.7828 -0.2722 -0.1029 -0.0657 113 LYS A CA 901 C C . LYS A 113 ? 1.3387 1.0442 0.7970 -0.2772 -0.1065 -0.0779 113 LYS A C 902 O O . LYS A 113 ? 1.3860 1.0752 0.8364 -0.2969 -0.1030 -0.0854 113 LYS A O 903 C CB . LYS A 113 ? 1.2887 1.0583 0.7815 -0.2794 -0.1004 -0.0680 113 LYS A CB 904 C CG . LYS A 113 ? 1.2842 1.0921 0.7929 -0.2682 -0.1058 -0.0733 113 LYS A CG 905 C CD . LYS A 113 ? 1.2702 1.1201 0.8011 -0.2595 -0.1037 -0.0666 113 LYS A CD 906 C CE . LYS A 113 ? 1.2789 1.1503 0.8215 -0.2761 -0.0977 -0.0675 113 LYS A CE 907 N NZ . LYS A 113 ? 1.2625 1.1710 0.8252 -0.2652 -0.0952 -0.0603 113 LYS A NZ 908 N N . ILE A 114 ? 1.3390 1.0482 0.7969 -0.2599 -0.1127 -0.0803 114 ILE A N 909 C CA . ILE A 114 ? 1.3849 1.0841 0.8339 -0.2629 -0.1165 -0.0935 114 ILE A CA 910 C C . ILE A 114 ? 1.3583 1.0927 0.8194 -0.2471 -0.1221 -0.0977 114 ILE A C 911 O O . ILE A 114 ? 1.3656 1.1175 0.8363 -0.2291 -0.1231 -0.0885 114 ILE A O 912 C CB . ILE A 114 ? 1.4454 1.0912 0.8686 -0.2579 -0.1174 -0.0939 114 ILE A CB 913 C CG1 . ILE A 114 ? 1.4561 1.0958 0.8772 -0.2329 -0.1208 -0.0839 114 ILE A CG1 914 C CG2 . ILE A 114 ? 1.4858 1.0918 0.8924 -0.2743 -0.1109 -0.0902 114 ILE A CG2 915 C CD1 . ILE A 114 ? 1.4966 1.0975 0.8970 -0.2225 -0.1238 -0.0880 114 ILE A CD1 916 N N . GLN A 115 ? 1.3579 1.1016 0.8175 -0.2544 -0.1253 -0.1120 115 GLN A N 917 C CA . GLN A 115 ? 1.3161 1.0929 0.7835 -0.2401 -0.1306 -0.1171 115 GLN A CA 918 C C . GLN A 115 ? 1.2997 1.0498 0.7518 -0.2225 -0.1335 -0.1175 115 GLN A C 919 O O . GLN A 115 ? 1.3010 1.0124 0.7345 -0.2282 -0.1339 -0.1251 115 GLN A O 920 C CB . GLN A 115 ? 1.3370 1.1353 0.8075 -0.2552 -0.1337 -0.1341 115 GLN A CB 921 C CG . GLN A 115 ? 1.3430 1.1711 0.8157 -0.2407 -0.1399 -0.1417 115 GLN A CG 922 C CD . GLN A 115 ? 1.3475 1.2032 0.8250 -0.2562 -0.1441 -0.1595 115 GLN A CD 923 O OE1 . GLN A 115 ? 1.3764 1.2143 0.8404 -0.2630 -0.1474 -0.1748 115 GLN A OE1 924 N NE2 . GLN A 115 ? 1.3255 1.2255 0.8228 -0.2616 -0.1441 -0.1584 115 GLN A NE2 925 N N . ILE A 116 ? 1.2725 1.0426 0.7327 -0.2012 -0.1344 -0.1094 116 ILE A N 926 C CA . ILE A 116 ? 1.3049 1.0560 0.7534 -0.1832 -0.1366 -0.1099 116 ILE A CA 927 C C . ILE A 116 ? 1.3268 1.1064 0.7766 -0.1728 -0.1400 -0.1184 116 ILE A C 928 O O . ILE A 116 ? 1.3585 1.1194 0.7935 -0.1660 -0.1424 -0.1270 116 ILE A O 929 C CB . ILE A 116 ? 1.2665 1.0123 0.7206 -0.1659 -0.1343 -0.0951 116 ILE A CB 930 C CG1 . ILE A 116 ? 1.2204 1.0064 0.6968 -0.1599 -0.1314 -0.0848 116 ILE A CG1 931 C CG2 . ILE A 116 ? 1.2877 0.9957 0.7319 -0.1728 -0.1326 -0.0893 116 ILE A CG2 932 C CD1 . ILE A 116 ? 1.1980 0.9843 0.6823 -0.1420 -0.1291 -0.0732 116 ILE A CD1 933 N N . ILE A 117 ? 1.3285 1.1526 0.7945 -0.1704 -0.1399 -0.1158 117 ILE A N 934 C CA . ILE A 117 ? 1.3576 1.2124 0.8234 -0.1604 -0.1433 -0.1233 117 ILE A CA 935 C C . ILE A 117 ? 1.3506 1.2407 0.8256 -0.1743 -0.1463 -0.1318 117 ILE A C 936 O O . ILE A 117 ? 1.3365 1.2586 0.8282 -0.1724 -0.1442 -0.1229 117 ILE A O 937 C CB . ILE A 117 ? 1.3342 1.2129 0.8099 -0.1375 -0.1399 -0.1102 117 ILE A CB 938 C CG1 . ILE A 117 ? 1.3443 1.1923 0.8143 -0.1245 -0.1370 -0.1029 117 ILE A CG1 939 C CG2 . ILE A 117 ? 1.3262 1.2351 0.7979 -0.1259 -0.1428 -0.1170 117 ILE A CG2 940 C CD1 . ILE A 117 ? 1.3256 1.1939 0.8071 -0.1041 -0.1320 -0.0901 117 ILE A CD1 941 N N . PRO A 118 ? 1.3698 1.2548 0.8347 -0.1882 -0.1512 -0.1499 118 PRO A N 942 C CA . PRO A 118 ? 1.3682 1.2892 0.8438 -0.2032 -0.1547 -0.1600 118 PRO A CA 943 C C . PRO A 118 ? 1.3509 1.3240 0.8370 -0.1871 -0.1574 -0.1567 118 PRO A C 944 O O . PRO A 118 ? 1.3388 1.3180 0.8176 -0.1667 -0.1580 -0.1535 118 PRO A O 945 C CB . PRO A 118 ? 1.4047 1.3082 0.8654 -0.2178 -0.1596 -0.1818 118 PRO A CB 946 C CG . PRO A 118 ? 1.4192 1.2681 0.8611 -0.2144 -0.1570 -0.1809 118 PRO A CG 947 C CD . PRO A 118 ? 1.4034 1.2508 0.8473 -0.1903 -0.1535 -0.1627 118 PRO A CD 948 N N . LYS A 119 ? 1.3491 1.3593 0.8519 -0.1956 -0.1583 -0.1570 119 LYS A N 949 C CA . LYS A 119 ? 1.3460 1.4064 0.8587 -0.1796 -0.1606 -0.1524 119 LYS A CA 950 C C . LYS A 119 ? 1.3692 1.4510 0.8704 -0.1745 -0.1690 -0.1689 119 LYS A C 951 O O . LYS A 119 ? 1.3782 1.4822 0.8747 -0.1525 -0.1700 -0.1635 119 LYS A O 952 C CB . LYS A 119 ? 1.3466 1.4413 0.8799 -0.1905 -0.1599 -0.1504 119 LYS A CB 953 C CG . LYS A 119 ? 1.3349 1.4701 0.8805 -0.1699 -0.1579 -0.1362 119 LYS A CG 954 C CD . LYS A 119 ? 1.3361 1.5045 0.9021 -0.1804 -0.1572 -0.1352 119 LYS A CD 955 C CE . LYS A 119 ? 1.3297 1.5427 0.9058 -0.1585 -0.1567 -0.1241 119 LYS A CE 956 N NZ . LYS A 119 ? 1.3303 1.5839 0.9258 -0.1675 -0.1582 -0.1274 119 LYS A NZ 957 N N . SER A 120 ? 1.3856 1.4590 0.8812 -0.1954 -0.1744 -0.1894 120 SER A N 958 C CA . SER A 120 ? 1.3771 1.4657 0.8598 -0.1940 -0.1831 -0.2090 120 SER A CA 959 C C . SER A 120 ? 1.3881 1.4527 0.8501 -0.1739 -0.1823 -0.2071 120 SER A C 960 O O . SER A 120 ? 1.3976 1.4873 0.8497 -0.1600 -0.1878 -0.2145 120 SER A O 961 C CB . SER A 120 ? 1.3901 1.4597 0.8696 -0.2228 -0.1865 -0.2312 120 SER A CB 962 O OG . SER A 120 ? 1.3951 1.4050 0.8624 -0.2311 -0.1806 -0.2293 120 SER A OG 963 N N . SER A 121 ? 1.3899 1.4077 0.8454 -0.1717 -0.1755 -0.1970 121 SER A N 964 C CA . SER A 121 ? 1.4050 1.3959 0.8424 -0.1540 -0.1737 -0.1952 121 SER A CA 965 C C . SER A 121 ? 1.3713 1.3932 0.8059 -0.1264 -0.1728 -0.1854 121 SER A C 966 O O . SER A 121 ? 1.3576 1.3681 0.7755 -0.1127 -0.1730 -0.1899 121 SER A O 967 C CB . SER A 121 ? 1.4136 1.3589 0.8505 -0.1532 -0.1660 -0.1813 121 SER A CB 968 O OG . SER A 121 ? 1.4456 1.3643 0.8666 -0.1372 -0.1642 -0.1809 121 SER A OG 969 N N . TRP A 122 ? 1.3571 1.4159 0.8070 -0.1176 -0.1708 -0.1716 122 TRP A N 970 C CA . TRP A 122 ? 1.3657 1.4505 0.8130 -0.0911 -0.1675 -0.1588 122 TRP A CA 971 C C . TRP A 122 ? 1.4007 1.5237 0.8366 -0.0827 -0.1757 -0.1721 122 TRP A C 972 O O . TRP A 122 ? 1.3981 1.5633 0.8430 -0.0802 -0.1794 -0.1707 122 TRP A O 973 C CB . TRP A 122 ? 1.3353 1.4409 0.8022 -0.0841 -0.1610 -0.1382 122 TRP A CB 974 C CG . TRP A 122 ? 1.3263 1.3976 0.8032 -0.0889 -0.1529 -0.1248 122 TRP A CG 975 C CD1 . TRP A 122 ? 1.3156 1.3772 0.8063 -0.1065 -0.1516 -0.1221 122 TRP A CD1 976 C CD2 . TRP A 122 ? 1.3205 1.3645 0.7941 -0.0757 -0.1453 -0.1132 122 TRP A CD2 977 N NE1 . TRP A 122 ? 1.3241 1.3541 0.8189 -0.1043 -0.1445 -0.1096 122 TRP A NE1 978 C CE2 . TRP A 122 ? 1.3165 1.3361 0.8022 -0.0860 -0.1408 -0.1043 122 TRP A CE2 979 C CE3 . TRP A 122 ? 1.3214 1.3611 0.7834 -0.0562 -0.1416 -0.1098 122 TRP A CE3 980 C CZ2 . TRP A 122 ? 1.2990 1.2921 0.7867 -0.0774 -0.1339 -0.0932 122 TRP A CZ2 981 C CZ3 . TRP A 122 ? 1.3256 1.3390 0.7912 -0.0484 -0.1337 -0.0983 122 TRP A CZ3 982 C CH2 . TRP A 122 ? 1.3125 1.3039 0.7915 -0.0590 -0.1305 -0.0906 122 TRP A CH2 983 N N . SER A 123 ? 1.4418 1.5506 0.8571 -0.0771 -0.1787 -0.1851 123 SER A N 984 C CA . SER A 123 ? 1.4666 1.6091 0.8674 -0.0694 -0.1874 -0.2005 123 SER A CA 985 C C . SER A 123 ? 1.4468 1.6183 0.8403 -0.0397 -0.1830 -0.1853 123 SER A C 986 O O . SER A 123 ? 1.4304 1.6458 0.8213 -0.0308 -0.1890 -0.1880 123 SER A O 987 C CB . SER A 123 ? 1.5096 1.6231 0.8896 -0.0760 -0.1920 -0.2224 123 SER A CB 988 O OG . SER A 123 ? 1.5100 1.5790 0.8829 -0.0690 -0.1836 -0.2141 123 SER A OG 989 N N . SER A 124 ? 1.4463 1.5934 0.8364 -0.0245 -0.1723 -0.1691 124 SER A N 990 C CA . SER A 124 ? 1.4256 1.5935 0.8091 0.0029 -0.1647 -0.1522 124 SER A CA 991 C C . SER A 124 ? 1.3797 1.5765 0.7803 0.0113 -0.1596 -0.1317 124 SER A C 992 O O . SER A 124 ? 1.3299 1.5532 0.7230 0.0332 -0.1556 -0.1203 124 SER A O 993 C CB . SER A 124 ? 1.4527 1.5853 0.8320 0.0139 -0.1534 -0.1413 124 SER A CB 994 O OG . SER A 124 ? 1.4560 1.5567 0.8530 0.0006 -0.1483 -0.1331 124 SER A OG 995 N N . HIS A 125 ? 1.3652 1.5553 0.7872 -0.0052 -0.1589 -0.1268 125 HIS A N 996 C CA . HIS A 125 ? 1.3193 1.5300 0.7589 0.0018 -0.1525 -0.1069 125 HIS A CA 997 C C . HIS A 125 ? 1.3151 1.5503 0.7701 -0.0147 -0.1606 -0.1142 125 HIS A C 998 O O . HIS A 125 ? 1.3248 1.5522 0.7811 -0.0365 -0.1690 -0.1327 125 HIS A O 999 C CB . HIS A 125 ? 1.2672 1.4445 0.7210 0.0006 -0.1404 -0.0897 125 HIS A CB 1000 C CG . HIS A 125 ? 1.2462 1.4007 0.6899 0.0154 -0.1314 -0.0823 125 HIS A CG 1001 N ND1 . HIS A 125 ? 1.2524 1.3763 0.6851 0.0095 -0.1336 -0.0945 125 HIS A ND1 1002 C CD2 . HIS A 125 ? 1.2262 1.3841 0.6700 0.0358 -0.1192 -0.0638 125 HIS A CD2 1003 C CE1 . HIS A 125 ? 1.2572 1.3697 0.6846 0.0261 -0.1237 -0.0844 125 HIS A CE1 1004 N NE2 . HIS A 125 ? 1.2378 1.3704 0.6722 0.0413 -0.1145 -0.0658 125 HIS A NE2 1005 N N . GLU A 126 ? 1.3061 1.5698 0.7730 -0.0042 -0.1569 -0.0993 126 GLU A N 1006 C CA . GLU A 126 ? 1.3132 1.6054 0.7967 -0.0170 -0.1633 -0.1043 126 GLU A CA 1007 C C . GLU A 126 ? 1.3072 1.5746 0.8113 -0.0329 -0.1565 -0.0957 126 GLU A C 1008 O O . GLU A 126 ? 1.3063 1.5559 0.8168 -0.0233 -0.1451 -0.0769 126 GLU A O 1009 C CB . GLU A 126 ? 1.3235 1.6608 0.8083 0.0047 -0.1631 -0.0929 126 GLU A CB 1010 C CG . GLU A 126 ? 1.3266 1.7008 0.8290 -0.0052 -0.1704 -0.0987 126 GLU A CG 1011 C CD . GLU A 126 ? 1.3499 1.7428 0.8510 -0.0251 -0.1851 -0.1261 126 GLU A CD 1012 O OE1 . GLU A 126 ? 1.3188 1.7346 0.8028 -0.0161 -0.1941 -0.1385 126 GLU A OE1 1013 O OE2 . GLU A 126 ? 1.3434 1.7281 0.8605 -0.0503 -0.1872 -0.1355 126 GLU A OE2 1014 N N . ALA A 127 ? 1.2993 1.5665 0.8136 -0.0574 -0.1630 -0.1099 127 ALA A N 1015 C CA . ALA A 127 ? 1.2527 1.4923 0.7826 -0.0748 -0.1572 -0.1043 127 ALA A CA 1016 C C . ALA A 127 ? 1.2385 1.5067 0.7885 -0.0856 -0.1586 -0.1045 127 ALA A C 1017 O O . ALA A 127 ? 1.2306 1.4800 0.7935 -0.0963 -0.1523 -0.0970 127 ALA A O 1018 C CB . ALA A 127 ? 1.2609 1.4609 0.7832 -0.0958 -0.1602 -0.1187 127 ALA A CB 1019 N N . SER A 128 ? 1.2376 1.5525 0.7903 -0.0823 -0.1670 -0.1133 128 SER A N 1020 C CA . SER A 128 ? 1.2184 1.5659 0.7916 -0.0926 -0.1690 -0.1157 128 SER A CA 1021 C C . SER A 128 ? 1.1803 1.5637 0.7624 -0.0692 -0.1650 -0.0989 128 SER A C 1022 O O . SER A 128 ? 1.1386 1.5573 0.7371 -0.0732 -0.1677 -0.1014 128 SER A O 1023 C CB . SER A 128 ? 1.2478 1.6253 0.8224 -0.1095 -0.1818 -0.1403 128 SER A CB 1024 O OG . SER A 128 ? 1.2817 1.6256 0.8576 -0.1380 -0.1821 -0.1536 128 SER A OG 1025 N N . LEU A 129 ? 1.1672 1.5404 0.7388 -0.0450 -0.1577 -0.0818 129 LEU A N 1026 C CA . LEU A 129 ? 1.1618 1.5612 0.7387 -0.0206 -0.1516 -0.0635 129 LEU A CA 1027 C C . LEU A 129 ? 1.1668 1.5319 0.7505 -0.0143 -0.1366 -0.0427 129 LEU A C 1028 O O . LEU A 129 ? 1.1751 1.5511 0.7608 0.0070 -0.1285 -0.0253 129 LEU A O 1029 C CB . LEU A 129 ? 1.1881 1.6096 0.7454 0.0050 -0.1548 -0.0603 129 LEU A CB 1030 C CG . LEU A 129 ? 1.1966 1.6722 0.7508 0.0102 -0.1688 -0.0746 129 LEU A CG 1031 C CD1 . LEU A 129 ? 1.1982 1.6826 0.7594 -0.0188 -0.1810 -0.1009 129 LEU A CD1 1032 C CD2 . LEU A 129 ? 1.2147 1.7012 0.7437 0.0335 -0.1717 -0.0732 129 LEU A CD2 1033 N N . GLY A 130 ? 1.1655 1.4894 0.7527 -0.0329 -0.1327 -0.0448 130 GLY A N 1034 C CA . GLY A 130 ? 1.1355 1.4262 0.7295 -0.0296 -0.1197 -0.0282 130 GLY A CA 1035 C C . GLY A 130 ? 1.1307 1.4243 0.7443 -0.0393 -0.1151 -0.0237 130 GLY A C 1036 O O . GLY A 130 ? 1.0913 1.3556 0.7109 -0.0571 -0.1125 -0.0260 130 GLY A O 1037 N N . VAL A 131 ? 1.1227 1.4518 0.7451 -0.0258 -0.1136 -0.0167 131 VAL A N 1038 C CA . VAL A 131 ? 1.0955 1.4352 0.7368 -0.0331 -0.1097 -0.0138 131 VAL A CA 1039 C C . VAL A 131 ? 1.0671 1.4138 0.7148 -0.0103 -0.0984 0.0055 131 VAL A C 1040 O O . VAL A 131 ? 1.0687 1.4162 0.7060 0.0115 -0.0939 0.0169 131 VAL A O 1041 C CB . VAL A 131 ? 1.1165 1.4992 0.7663 -0.0436 -0.1206 -0.0290 131 VAL A CB 1042 C CG1 . VAL A 131 ? 1.1280 1.4988 0.7727 -0.0692 -0.1298 -0.0487 131 VAL A CG1 1043 C CG2 . VAL A 131 ? 1.1260 1.5540 0.7704 -0.0214 -0.1269 -0.0283 131 VAL A CG2 1044 N N . SER A 132 ? 1.0463 1.3964 0.7104 -0.0155 -0.0928 0.0093 132 SER A N 1045 C CA . SER A 132 ? 1.0333 1.3856 0.7046 0.0044 -0.0808 0.0269 132 SER A CA 1046 C C . SER A 132 ? 1.0345 1.4113 0.7237 0.0007 -0.0793 0.0258 132 SER A C 1047 O O . SER A 132 ? 1.0044 1.3848 0.7023 -0.0216 -0.0842 0.0132 132 SER A O 1048 C CB . SER A 132 ? 1.0129 1.3186 0.6840 0.0040 -0.0684 0.0378 132 SER A CB 1049 O OG . SER A 132 ? 0.9851 1.2885 0.6659 0.0179 -0.0560 0.0522 132 SER A OG 1050 N N . SER A 133 ? 1.0529 1.4449 0.7467 0.0234 -0.0714 0.0397 133 SER A N 1051 C CA . SER A 133 ? 1.0730 1.4872 0.7838 0.0247 -0.0677 0.0410 133 SER A CA 1052 C C . SER A 133 ? 1.0918 1.4701 0.8119 0.0110 -0.0572 0.0438 133 SER A C 1053 O O . SER A 133 ? 1.0795 1.4709 0.8134 0.0008 -0.0563 0.0385 133 SER A O 1054 C CB . SER A 133 ? 1.0772 1.5126 0.7876 0.0561 -0.0610 0.0567 133 SER A CB 1055 O OG . SER A 133 ? 1.1408 1.6098 0.8399 0.0714 -0.0707 0.0551 133 SER A OG 1056 N N . ALA A 134 ? 1.1106 1.4459 0.8236 0.0112 -0.0493 0.0515 134 ALA A N 1057 C CA . ALA A 134 ? 1.1166 1.4164 0.8367 -0.0014 -0.0403 0.0531 134 ALA A CA 1058 C C . ALA A 134 ? 1.1267 1.4188 0.8491 -0.0296 -0.0476 0.0382 134 ALA A C 1059 O O . ALA A 134 ? 1.0982 1.3746 0.8283 -0.0411 -0.0422 0.0369 134 ALA A O 1060 C CB . ALA A 134 ? 1.1160 1.3756 0.8287 0.0036 -0.0320 0.0622 134 ALA A CB 1061 N N . CYS A 135 ? 1.1468 1.4492 0.8614 -0.0403 -0.0595 0.0269 135 CYS A N 1062 C CA . CYS A 135 ? 1.1705 1.4594 0.8836 -0.0667 -0.0658 0.0135 135 CYS A CA 1063 C C . CYS A 135 ? 1.1166 1.4441 0.8344 -0.0779 -0.0762 -0.0001 135 CYS A C 1064 O O . CYS A 135 ? 1.0862 1.4144 0.7949 -0.0879 -0.0856 -0.0108 135 CYS A O 1065 C CB . CYS A 135 ? 1.2269 1.4808 0.9254 -0.0718 -0.0688 0.0120 135 CYS A CB 1066 S SG . CYS A 135 ? 1.3953 1.6142 1.0890 -0.1003 -0.0719 0.0013 135 CYS A SG 1067 N N . PRO A 136 ? 1.0708 1.4306 0.8037 -0.0768 -0.0739 -0.0009 136 PRO A N 1068 C CA . PRO A 136 ? 1.0634 1.4689 0.8051 -0.0841 -0.0828 -0.0134 136 PRO A CA 1069 C C . PRO A 136 ? 1.0714 1.4734 0.8178 -0.1144 -0.0859 -0.0279 136 PRO A C 1070 O O . PRO A 136 ? 1.0558 1.4257 0.8017 -0.1276 -0.0790 -0.0261 136 PRO A O 1071 C CB . PRO A 136 ? 1.0648 1.5036 0.8221 -0.0676 -0.0766 -0.0059 136 PRO A CB 1072 C CG . PRO A 136 ? 1.0411 1.4438 0.8006 -0.0687 -0.0641 0.0036 136 PRO A CG 1073 C CD . PRO A 136 ? 1.0509 1.4074 0.7945 -0.0673 -0.0622 0.0096 136 PRO A CD 1074 N N . TYR A 137 ? 1.0941 1.5301 0.8451 -0.1250 -0.0958 -0.0423 137 TYR A N 1075 C CA . TYR A 137 ? 1.1133 1.5529 0.8716 -0.1543 -0.0975 -0.0568 137 TYR A CA 1076 C C . TYR A 137 ? 1.1088 1.6081 0.8847 -0.1575 -0.1044 -0.0690 137 TYR A C 1077 O O . TYR A 137 ? 1.1377 1.6657 0.9111 -0.1488 -0.1146 -0.0756 137 TYR A O 1078 C CB . TYR A 137 ? 1.1437 1.5479 0.8856 -0.1731 -0.1031 -0.0664 137 TYR A CB 1079 C CG . TYR A 137 ? 1.1721 1.5755 0.9197 -0.2040 -0.1035 -0.0808 137 TYR A CG 1080 C CD1 . TYR A 137 ? 1.1801 1.5602 0.9308 -0.2189 -0.0937 -0.0773 137 TYR A CD1 1081 C CD2 . TYR A 137 ? 1.1736 1.5990 0.9229 -0.2188 -0.1130 -0.0981 137 TYR A CD2 1082 C CE1 . TYR A 137 ? 1.1866 1.5641 0.9412 -0.2472 -0.0922 -0.0892 137 TYR A CE1 1083 C CE2 . TYR A 137 ? 1.1874 1.6097 0.9424 -0.2485 -0.1116 -0.1112 137 TYR A CE2 1084 C CZ . TYR A 137 ? 1.1953 1.5931 0.9527 -0.2624 -0.1007 -0.1059 137 TYR A CZ 1085 O OH . TYR A 137 ? 1.2087 1.6017 0.9704 -0.2919 -0.0976 -0.1177 137 TYR A OH 1086 N N . GLN A 138 ? 1.0870 1.6064 0.8806 -0.1701 -0.0988 -0.0728 138 GLN A N 1087 C CA . GLN A 138 ? 1.0802 1.6606 0.8949 -0.1738 -0.1040 -0.0848 138 GLN A CA 1088 C C . GLN A 138 ? 1.0760 1.7005 0.8948 -0.1427 -0.1103 -0.0794 138 GLN A C 1089 O O . GLN A 138 ? 1.0882 1.7581 0.9138 -0.1419 -0.1215 -0.0917 138 GLN A O 1090 C CB . GLN A 138 ? 1.1122 1.7007 0.9276 -0.2012 -0.1128 -0.1050 138 GLN A CB 1091 C CG . GLN A 138 ? 1.1304 1.6834 0.9447 -0.2328 -0.1052 -0.1108 138 GLN A CG 1092 C CD . GLN A 138 ? 1.1575 1.7145 0.9721 -0.2607 -0.1123 -0.1310 138 GLN A CD 1093 O OE1 . GLN A 138 ? 1.1509 1.6830 0.9653 -0.2877 -0.1059 -0.1369 138 GLN A OE1 1094 N NE2 . GLN A 138 ? 1.1615 1.7487 0.9755 -0.2542 -0.1251 -0.1417 138 GLN A NE2 1095 N N . GLY A 139 ? 1.0581 1.6678 0.8715 -0.1169 -0.1028 -0.0610 139 GLY A N 1096 C CA . GLY A 139 ? 1.0448 1.6913 0.8604 -0.0845 -0.1058 -0.0522 139 GLY A CA 1097 C C . GLY A 139 ? 1.0309 1.6719 0.8269 -0.0673 -0.1140 -0.0489 139 GLY A C 1098 O O . GLY A 139 ? 1.0327 1.7014 0.8270 -0.0387 -0.1159 -0.0400 139 GLY A O 1099 N N . LYS A 140 ? 1.0298 1.6348 0.8098 -0.0832 -0.1181 -0.0554 140 LYS A N 1100 C CA . LYS A 140 ? 1.0514 1.6503 0.8117 -0.0690 -0.1257 -0.0541 140 LYS A CA 1101 C C . LYS A 140 ? 1.0436 1.5814 0.7856 -0.0664 -0.1178 -0.0419 140 LYS A C 1102 O O . LYS A 140 ? 1.0483 1.5474 0.7914 -0.0828 -0.1102 -0.0400 140 LYS A O 1103 C CB . LYS A 140 ? 1.0671 1.6834 0.8246 -0.0888 -0.1392 -0.0757 140 LYS A CB 1104 C CG . LYS A 140 ? 1.0793 1.7491 0.8596 -0.1037 -0.1456 -0.0925 140 LYS A CG 1105 C CD . LYS A 140 ? 1.0976 1.7985 0.8754 -0.1139 -0.1607 -0.1134 140 LYS A CD 1106 C CE . LYS A 140 ? 1.0957 1.8529 0.9000 -0.1304 -0.1664 -0.1311 140 LYS A CE 1107 N NZ . LYS A 140 ? 1.1017 1.9060 0.9063 -0.1308 -0.1826 -0.1503 140 LYS A NZ 1108 N N . SER A 141 ? 1.0416 1.5726 0.7668 -0.0455 -0.1197 -0.0338 141 SER A N 1109 C CA . SER A 141 ? 1.0328 1.5108 0.7421 -0.0414 -0.1124 -0.0227 141 SER A CA 1110 C C . SER A 141 ? 1.0446 1.4894 0.7441 -0.0664 -0.1173 -0.0356 141 SER A C 1111 O O . SER A 141 ? 1.0706 1.5290 0.7619 -0.0721 -0.1280 -0.0489 141 SER A O 1112 C CB . SER A 141 ? 1.0296 1.5130 0.7236 -0.0127 -0.1124 -0.0113 141 SER A CB 1113 O OG . SER A 141 ? 1.0159 1.5220 0.7162 0.0123 -0.1058 0.0033 141 SER A OG 1114 N N . SER A 142 ? 1.0352 1.4361 0.7346 -0.0801 -0.1095 -0.0318 142 SER A N 1115 C CA . SER A 142 ? 1.0390 1.4036 0.7282 -0.1022 -0.1128 -0.0420 142 SER A CA 1116 C C . SER A 142 ? 1.0396 1.3560 0.7178 -0.0961 -0.1052 -0.0301 142 SER A C 1117 O O . SER A 142 ? 1.0575 1.3716 0.7341 -0.0744 -0.0987 -0.0159 142 SER A O 1118 C CB . SER A 142 ? 1.0449 1.4062 0.7452 -0.1288 -0.1118 -0.0516 142 SER A CB 1119 O OG . SER A 142 ? 1.0751 1.4015 0.7639 -0.1496 -0.1150 -0.0615 142 SER A OG 1120 N N . PHE A 143 ? 1.0361 1.3143 0.7071 -0.1146 -0.1055 -0.0358 143 PHE A N 1121 C CA . PHE A 143 ? 1.0159 1.2510 0.6777 -0.1097 -0.0996 -0.0266 143 PHE A CA 1122 C C . PHE A 143 ? 1.0108 1.2079 0.6678 -0.1313 -0.0994 -0.0323 143 PHE A C 1123 O O . PHE A 143 ? 1.0167 1.2161 0.6736 -0.1509 -0.1041 -0.0442 143 PHE A O 1124 C CB . PHE A 143 ? 1.0128 1.2428 0.6599 -0.0966 -0.1036 -0.0266 143 PHE A CB 1125 C CG . PHE A 143 ? 0.9992 1.1983 0.6415 -0.0840 -0.0957 -0.0140 143 PHE A CG 1126 C CD1 . PHE A 143 ? 0.9874 1.1908 0.6381 -0.0671 -0.0857 0.0010 143 PHE A CD1 1127 C CD2 . PHE A 143 ? 1.0007 1.1670 0.6308 -0.0888 -0.0977 -0.0176 143 PHE A CD2 1128 C CE1 . PHE A 143 ? 0.9789 1.1550 0.6274 -0.0573 -0.0775 0.0114 143 PHE A CE1 1129 C CE2 . PHE A 143 ? 0.9971 1.1391 0.6255 -0.0777 -0.0903 -0.0071 143 PHE A CE2 1130 C CZ . PHE A 143 ? 0.9867 1.1342 0.6251 -0.0628 -0.0801 0.0071 143 PHE A CZ 1131 N N . PHE A 144 ? 0.9877 1.1504 0.6408 -0.1270 -0.0935 -0.0235 144 PHE A N 1132 C CA . PHE A 144 ? 0.9884 1.1120 0.6333 -0.1425 -0.0938 -0.0271 144 PHE A CA 1133 C C . PHE A 144 ? 0.9990 1.1132 0.6310 -0.1567 -0.1025 -0.0409 144 PHE A C 1134 O O . PHE A 144 ? 1.0363 1.1473 0.6582 -0.1491 -0.1071 -0.0441 144 PHE A O 1135 C CB . PHE A 144 ? 0.9914 1.0857 0.6316 -0.1311 -0.0895 -0.0180 144 PHE A CB 1136 C CG . PHE A 144 ? 0.9821 1.0781 0.6347 -0.1198 -0.0799 -0.0057 144 PHE A CG 1137 C CD1 . PHE A 144 ? 0.9794 1.0680 0.6393 -0.1292 -0.0752 -0.0040 144 PHE A CD1 1138 C CD2 . PHE A 144 ? 0.9672 1.0705 0.6232 -0.1000 -0.0746 0.0039 144 PHE A CD2 1139 C CE1 . PHE A 144 ? 0.9624 1.0508 0.6333 -0.1192 -0.0661 0.0057 144 PHE A CE1 1140 C CE2 . PHE A 144 ? 0.9517 1.0533 0.6191 -0.0907 -0.0646 0.0146 144 PHE A CE2 1141 C CZ . PHE A 144 ? 0.9469 1.0409 0.6220 -0.1004 -0.0606 0.0148 144 PHE A CZ 1142 N N . ARG A 145 ? 0.9918 1.0998 0.6238 -0.1776 -0.1036 -0.0490 145 ARG A N 1143 C CA . ARG A 145 ? 1.0114 1.1124 0.6331 -0.1935 -0.1106 -0.0633 145 ARG A CA 1144 C C . ARG A 145 ? 1.0286 1.0880 0.6316 -0.1945 -0.1135 -0.0660 145 ARG A C 1145 O O . ARG A 145 ? 1.0629 1.1162 0.6557 -0.2031 -0.1194 -0.0781 145 ARG A O 1146 C CB . ARG A 145 ? 1.0211 1.1220 0.6477 -0.2167 -0.1085 -0.0699 145 ARG A CB 1147 C CG . ARG A 145 ? 1.0252 1.1709 0.6712 -0.2173 -0.1062 -0.0700 145 ARG A CG 1148 C CD . ARG A 145 ? 1.0688 1.2214 0.7196 -0.2426 -0.1059 -0.0815 145 ARG A CD 1149 N NE . ARG A 145 ? 1.0906 1.2867 0.7619 -0.2435 -0.1026 -0.0813 145 ARG A NE 1150 C CZ . ARG A 145 ? 1.1149 1.3588 0.7989 -0.2359 -0.1077 -0.0867 145 ARG A CZ 1151 N NH1 . ARG A 145 ? 1.1325 1.3878 0.8098 -0.2265 -0.1163 -0.0928 145 ARG A NH1 1152 N NH2 . ARG A 145 ? 1.1206 1.4028 0.8238 -0.2362 -0.1041 -0.0860 145 ARG A NH2 1153 N N . ASN A 146 ? 1.0252 1.0566 0.6242 -0.1859 -0.1095 -0.0559 146 ASN A N 1154 C CA . ASN A 146 ? 1.0365 1.0281 0.6188 -0.1865 -0.1120 -0.0579 146 ASN A CA 1155 C C . ASN A 146 ? 1.0194 1.0108 0.5968 -0.1674 -0.1139 -0.0555 146 ASN A C 1156 O O . ASN A 146 ? 1.0163 0.9795 0.5799 -0.1659 -0.1166 -0.0589 146 ASN A O 1157 C CB . ASN A 146 ? 1.0337 0.9946 0.6134 -0.1901 -0.1075 -0.0502 146 ASN A CB 1158 C CG . ASN A 146 ? 1.0655 1.0203 0.6450 -0.2102 -0.1050 -0.0532 146 ASN A CG 1159 O OD1 . ASN A 146 ? 1.0936 1.0496 0.6686 -0.2254 -0.1075 -0.0635 146 ASN A OD1 1160 N ND2 . ASN A 146 ? 1.0832 1.0320 0.6678 -0.2108 -0.0995 -0.0449 146 ASN A ND2 1161 N N . VAL A 147 ? 1.0101 1.0326 0.5979 -0.1522 -0.1116 -0.0493 147 VAL A N 1162 C CA . VAL A 147 ? 1.0270 1.0534 0.6101 -0.1338 -0.1120 -0.0464 147 VAL A CA 1163 C C . VAL A 147 ? 1.0275 1.0917 0.6117 -0.1258 -0.1153 -0.0504 147 VAL A C 1164 O O . VAL A 147 ? 1.0219 1.1152 0.6162 -0.1298 -0.1157 -0.0513 147 VAL A O 1165 C CB . VAL A 147 ? 1.0166 1.0383 0.6089 -0.1189 -0.1040 -0.0321 147 VAL A CB 1166 C CG1 . VAL A 147 ? 1.0218 1.0073 0.6105 -0.1245 -0.1029 -0.0304 147 VAL A CG1 1167 C CG2 . VAL A 147 ? 1.0057 1.0512 0.6141 -0.1160 -0.0979 -0.0235 147 VAL A CG2 1168 N N . VAL A 148 ? 1.0632 1.1282 0.6364 -0.1138 -0.1179 -0.0531 148 VAL A N 1169 C CA . VAL A 148 ? 1.0653 1.1652 0.6351 -0.1046 -0.1224 -0.0581 148 VAL A CA 1170 C C . VAL A 148 ? 1.0523 1.1658 0.6239 -0.0807 -0.1158 -0.0443 148 VAL A C 1171 O O . VAL A 148 ? 1.0606 1.1542 0.6254 -0.0708 -0.1121 -0.0398 148 VAL A O 1172 C CB . VAL A 148 ? 1.0864 1.1773 0.6389 -0.1094 -0.1306 -0.0738 148 VAL A CB 1173 C CG1 . VAL A 148 ? 1.1185 1.2475 0.6658 -0.0982 -0.1359 -0.0796 148 VAL A CG1 1174 C CG2 . VAL A 148 ? 1.0996 1.1736 0.6497 -0.1343 -0.1356 -0.0875 148 VAL A CG2 1175 N N . TRP A 149 ? 1.0496 1.1965 0.6302 -0.0710 -0.1134 -0.0373 149 TRP A N 1176 C CA . TRP A 149 ? 1.0710 1.2313 0.6512 -0.0475 -0.1061 -0.0233 149 TRP A CA 1177 C C . TRP A 149 ? 1.0944 1.2749 0.6583 -0.0355 -0.1122 -0.0300 149 TRP A C 1178 O O . TRP A 149 ? 1.0869 1.3026 0.6498 -0.0308 -0.1178 -0.0341 149 TRP A O 1179 C CB . TRP A 149 ? 1.0570 1.2413 0.6521 -0.0402 -0.1002 -0.0119 149 TRP A CB 1180 C CG . TRP A 149 ? 1.0589 1.2512 0.6541 -0.0163 -0.0898 0.0049 149 TRP A CG 1181 C CD1 . TRP A 149 ? 1.0760 1.2575 0.6608 -0.0018 -0.0845 0.0112 149 TRP A CD1 1182 C CD2 . TRP A 149 ? 1.0410 1.2511 0.6473 -0.0044 -0.0820 0.0181 149 TRP A CD2 1183 N NE1 . TRP A 149 ? 1.0745 1.2654 0.6628 0.0175 -0.0733 0.0280 149 TRP A NE1 1184 C CE2 . TRP A 149 ? 1.0521 1.2593 0.6531 0.0167 -0.0717 0.0326 149 TRP A CE2 1185 C CE3 . TRP A 149 ? 1.0313 1.2591 0.6512 -0.0090 -0.0818 0.0192 149 TRP A CE3 1186 C CZ2 . TRP A 149 ? 1.0473 1.2655 0.6550 0.0334 -0.0611 0.0485 149 TRP A CZ2 1187 C CZ3 . TRP A 149 ? 1.0392 1.2798 0.6664 0.0084 -0.0720 0.0344 149 TRP A CZ3 1188 C CH2 . TRP A 149 ? 1.0431 1.2773 0.6635 0.0294 -0.0617 0.0490 149 TRP A CH2 1189 N N . LEU A 150 ? 1.1348 1.2940 0.6859 -0.0302 -0.1113 -0.0319 150 LEU A N 1190 C CA . LEU A 150 ? 1.1971 1.3710 0.7301 -0.0189 -0.1166 -0.0394 150 LEU A CA 1191 C C . LEU A 150 ? 1.2094 1.4067 0.7388 0.0060 -0.1092 -0.0245 150 LEU A C 1192 O O . LEU A 150 ? 1.1967 1.3827 0.7341 0.0160 -0.0970 -0.0079 150 LEU A O 1193 C CB . LEU A 150 ? 1.2244 1.3663 0.7447 -0.0201 -0.1167 -0.0457 150 LEU A CB 1194 C CG . LEU A 150 ? 1.2487 1.3612 0.7676 -0.0422 -0.1233 -0.0599 150 LEU A CG 1195 C CD1 . LEU A 150 ? 1.2696 1.3490 0.7787 -0.0383 -0.1205 -0.0612 150 LEU A CD1 1196 C CD2 . LEU A 150 ? 1.2633 1.3903 0.7738 -0.0554 -0.1353 -0.0793 150 LEU A CD2 1197 N N . ILE A 151 ? 1.2281 1.4577 0.7449 0.0159 -0.1165 -0.0310 151 ILE A N 1198 C CA . ILE A 151 ? 1.2354 1.4876 0.7423 0.0420 -0.1104 -0.0178 151 ILE A CA 1199 C C . ILE A 151 ? 1.2560 1.5216 0.7393 0.0516 -0.1180 -0.0293 151 ILE A C 1200 O O . ILE A 151 ? 1.2515 1.5137 0.7277 0.0369 -0.1292 -0.0493 151 ILE A O 1201 C CB . ILE A 151 ? 1.2341 1.5223 0.7494 0.0507 -0.1113 -0.0102 151 ILE A CB 1202 C CG1 . ILE A 151 ? 1.2477 1.5699 0.7605 0.0412 -0.1275 -0.0295 151 ILE A CG1 1203 C CG2 . ILE A 151 ? 1.2151 1.4901 0.7529 0.0417 -0.1035 0.0000 151 ILE A CG2 1204 C CD1 . ILE A 151 ? 1.2481 1.6113 0.7693 0.0518 -0.1296 -0.0234 151 ILE A CD1 1205 N N . LYS A 152 ? 1.2825 1.5623 0.7525 0.0763 -0.1109 -0.0165 152 LYS A N 1206 C CA . LYS A 152 ? 1.3170 1.6105 0.7618 0.0892 -0.1163 -0.0253 152 LYS A CA 1207 C C . LYS A 152 ? 1.3389 1.6661 0.7755 0.0827 -0.1341 -0.0464 152 LYS A C 1208 O O . LYS A 152 ? 1.2914 1.6471 0.7393 0.0795 -0.1403 -0.0476 152 LYS A O 1209 C CB . LYS A 152 ? 1.3162 1.6237 0.7477 0.1186 -0.1048 -0.0054 152 LYS A CB 1210 C CG . LYS A 152 ? 1.3079 1.6465 0.7450 0.1319 -0.1034 0.0077 152 LYS A CG 1211 C CD . LYS A 152 ? 1.3414 1.7032 0.7553 0.1620 -0.0983 0.0202 152 LYS A CD 1212 C CE . LYS A 152 ? 1.3301 1.7062 0.7508 0.1794 -0.0886 0.0424 152 LYS A CE 1213 N NZ . LYS A 152 ? 1.3608 1.7581 0.7560 0.2105 -0.0830 0.0563 152 LYS A NZ 1214 N N . LYS A 153 ? 1.3842 1.7085 0.8020 0.0807 -0.1420 -0.0639 153 LYS A N 1215 C CA . LYS A 153 ? 1.4137 1.7693 0.8217 0.0744 -0.1588 -0.0866 153 LYS A CA 1216 C C . LYS A 153 ? 1.4363 1.8169 0.8169 0.0995 -0.1607 -0.0868 153 LYS A C 1217 O O . LYS A 153 ? 1.4399 1.7999 0.8030 0.1072 -0.1558 -0.0881 153 LYS A O 1218 C CB . LYS A 153 ? 1.4273 1.7567 0.8349 0.0488 -0.1672 -0.1102 153 LYS A CB 1219 C CG . LYS A 153 ? 1.4474 1.8074 0.8524 0.0351 -0.1843 -0.1356 153 LYS A CG 1220 C CD . LYS A 153 ? 1.4595 1.7875 0.8664 0.0074 -0.1902 -0.1573 153 LYS A CD 1221 C CE . LYS A 153 ? 1.4812 1.8401 0.8870 -0.0079 -0.2062 -0.1840 153 LYS A CE 1222 N NZ . LYS A 153 ? 1.5022 1.8258 0.9079 -0.0352 -0.2104 -0.2052 153 LYS A NZ 1223 N N . ASN A 154 ? 1.4403 1.8665 0.8168 0.1133 -0.1675 -0.0852 154 ASN A N 1224 C CA . ASN A 154 ? 1.4700 1.9256 0.8187 0.1401 -0.1699 -0.0836 154 ASN A CA 1225 C C . ASN A 154 ? 1.4624 1.8967 0.7978 0.1639 -0.1512 -0.0587 154 ASN A C 1226 O O . ASN A 154 ? 1.4495 1.8788 0.7606 0.1764 -0.1490 -0.0619 154 ASN A O 1227 C CB . ASN A 154 ? 1.4871 1.9503 0.8165 0.1323 -0.1842 -0.1124 154 ASN A CB 1228 C CG . ASN A 154 ? 1.5176 2.0289 0.8225 0.1549 -0.1942 -0.1182 154 ASN A CG 1229 O OD1 . ASN A 154 ? 1.5213 2.0698 0.8290 0.1701 -0.1965 -0.1072 154 ASN A OD1 1230 N ND2 . ASN A 154 ? 1.5309 2.0423 0.8106 0.1582 -0.2007 -0.1361 154 ASN A ND2 1231 N N . SER A 155 ? 1.4377 1.8591 0.7902 0.1690 -0.1371 -0.0346 155 SER A N 1232 C CA . SER A 155 ? 1.4283 1.8326 0.7724 0.1912 -0.1173 -0.0085 155 SER A CA 1233 C C . SER A 155 ? 1.4186 1.7815 0.7598 0.1861 -0.1063 -0.0078 155 SER A C 1234 O O . SER A 155 ? 1.4445 1.7990 0.7717 0.2055 -0.0919 0.0079 155 SER A O 1235 C CB . SER A 155 ? 1.4409 1.8789 0.7562 0.2220 -0.1171 0.0000 155 SER A CB 1236 O OG . SER A 155 ? 1.4272 1.9077 0.7450 0.2275 -0.1297 -0.0032 155 SER A OG 1237 N N . THR A 156 ? 1.3910 1.7287 0.7458 0.1606 -0.1123 -0.0242 156 THR A N 1238 C CA . THR A 156 ? 1.3842 1.6839 0.7382 0.1551 -0.1037 -0.0255 156 THR A CA 1239 C C . THR A 156 ? 1.3427 1.6107 0.7231 0.1299 -0.1035 -0.0290 156 THR A C 1240 O O . THR A 156 ? 1.3298 1.6030 0.7215 0.1109 -0.1156 -0.0423 156 THR A O 1241 C CB . THR A 156 ? 1.4047 1.7045 0.7356 0.1536 -0.1141 -0.0485 156 THR A CB 1242 O OG1 . THR A 156 ? 1.4202 1.7231 0.7578 0.1303 -0.1313 -0.0722 156 THR A OG1 1243 C CG2 . THR A 156 ? 1.4317 1.7651 0.7332 0.1785 -0.1164 -0.0479 156 THR A CG2 1244 N N . TYR A 157 ? 1.3183 1.5552 0.7085 0.1299 -0.0895 -0.0173 157 TYR A N 1245 C CA . TYR A 157 ? 1.2989 1.5044 0.7109 0.1081 -0.0894 -0.0211 157 TYR A CA 1246 C C . TYR A 157 ? 1.2833 1.4600 0.6896 0.1084 -0.0840 -0.0257 157 TYR A C 1247 O O . TYR A 157 ? 1.2526 1.4149 0.6672 0.1164 -0.0691 -0.0107 157 TYR A O 1248 C CB . TYR A 157 ? 1.2878 1.4862 0.7236 0.1069 -0.0778 -0.0013 157 TYR A CB 1249 C CG . TYR A 157 ? 1.2807 1.4572 0.7386 0.0832 -0.0819 -0.0067 157 TYR A CG 1250 C CD1 . TYR A 157 ? 1.2937 1.4383 0.7569 0.0716 -0.0814 -0.0136 157 TYR A CD1 1251 C CD2 . TYR A 157 ? 1.2737 1.4623 0.7465 0.0737 -0.0860 -0.0045 157 TYR A CD2 1252 C CE1 . TYR A 157 ? 1.2794 1.4039 0.7599 0.0517 -0.0850 -0.0175 157 TYR A CE1 1253 C CE2 . TYR A 157 ? 1.2479 1.4166 0.7387 0.0529 -0.0888 -0.0088 157 TYR A CE2 1254 C CZ . TYR A 157 ? 1.2536 1.3900 0.7472 0.0421 -0.0885 -0.0151 157 TYR A CZ 1255 O OH . TYR A 157 ? 1.2307 1.3474 0.7395 0.0230 -0.0913 -0.0185 157 TYR A OH 1256 N N . PRO A 158 ? 1.2902 1.4590 0.6829 0.0998 -0.0956 -0.0472 158 PRO A N 1257 C CA . PRO A 158 ? 1.2905 1.4320 0.6770 0.1011 -0.0913 -0.0530 158 PRO A CA 1258 C C . PRO A 158 ? 1.2630 1.3726 0.6716 0.0861 -0.0880 -0.0502 158 PRO A C 1259 O O . PRO A 158 ? 1.2324 1.3376 0.6564 0.0695 -0.0936 -0.0512 158 PRO A O 1260 C CB . PRO A 158 ? 1.3153 1.4569 0.6813 0.0944 -0.1060 -0.0781 158 PRO A CB 1261 C CG . PRO A 158 ? 1.3070 1.4658 0.6789 0.0790 -0.1189 -0.0873 158 PRO A CG 1262 C CD . PRO A 158 ? 1.2971 1.4824 0.6800 0.0887 -0.1128 -0.0678 158 PRO A CD 1263 N N . THR A 159 ? 1.2632 1.3527 0.6733 0.0926 -0.0789 -0.0468 159 THR A N 1264 C CA . THR A 159 ? 1.2418 1.3036 0.6720 0.0813 -0.0757 -0.0438 159 THR A CA 1265 C C . THR A 159 ? 1.2545 1.2965 0.6839 0.0610 -0.0898 -0.0609 159 THR A C 1266 O O . THR A 159 ? 1.2532 1.2871 0.6643 0.0589 -0.0982 -0.0780 159 THR A O 1267 C CB . THR A 159 ? 1.2447 1.2915 0.6750 0.0925 -0.0654 -0.0410 159 THR A CB 1268 O OG1 . THR A 159 ? 1.2340 1.2988 0.6640 0.1106 -0.0506 -0.0251 159 THR A OG1 1269 C CG2 . THR A 159 ? 1.2298 1.2530 0.6830 0.0824 -0.0625 -0.0370 159 THR A CG2 1270 N N . ILE A 160 ? 1.2567 1.2904 0.7050 0.0463 -0.0915 -0.0560 160 ILE A N 1271 C CA . ILE A 160 ? 1.2732 1.2846 0.7225 0.0264 -0.1022 -0.0688 160 ILE A CA 1272 C C . ILE A 160 ? 1.2765 1.2554 0.7285 0.0255 -0.1001 -0.0709 160 ILE A C 1273 O O . ILE A 160 ? 1.2708 1.2471 0.7358 0.0344 -0.0903 -0.0588 160 ILE A O 1274 C CB . ILE A 160 ? 1.2609 1.2776 0.7286 0.0124 -0.1036 -0.0617 160 ILE A CB 1275 C CG1 . ILE A 160 ? 1.2640 1.3136 0.7281 0.0124 -0.1080 -0.0628 160 ILE A CG1 1276 C CG2 . ILE A 160 ? 1.2658 1.2547 0.7355 -0.0075 -0.1115 -0.0716 160 ILE A CG2 1277 C CD1 . ILE A 160 ? 1.2450 1.3064 0.7281 0.0046 -0.1062 -0.0523 160 ILE A CD1 1278 N N . LYS A 161 ? 1.2995 1.2540 0.7393 0.0152 -0.1091 -0.0865 161 LYS A N 1279 C CA . LYS A 161 ? 1.3148 1.2365 0.7551 0.0148 -0.1086 -0.0891 161 LYS A CA 1280 C C . LYS A 161 ? 1.3375 1.2320 0.7709 -0.0042 -0.1185 -0.1012 161 LYS A C 1281 O O . LYS A 161 ? 1.3658 1.2475 0.7805 -0.0082 -0.1248 -0.1169 161 LYS A O 1282 C CB . LYS A 161 ? 1.3450 1.2604 0.7699 0.0310 -0.1058 -0.0960 161 LYS A CB 1283 C CG . LYS A 161 ? 1.3480 1.2861 0.7798 0.0501 -0.0936 -0.0832 161 LYS A CG 1284 C CD . LYS A 161 ? 1.3709 1.3030 0.7873 0.0663 -0.0900 -0.0905 161 LYS A CD 1285 C CE . LYS A 161 ? 1.3777 1.3342 0.8009 0.0843 -0.0760 -0.0766 161 LYS A CE 1286 N NZ . LYS A 161 ? 1.4117 1.3688 0.8177 0.1013 -0.0713 -0.0834 161 LYS A NZ 1287 N N . ARG A 162 ? 1.3260 1.2110 0.7739 -0.0163 -0.1190 -0.0939 162 ARG A N 1288 C CA . ARG A 162 ? 1.3246 1.1838 0.7664 -0.0353 -0.1264 -0.1028 162 ARG A CA 1289 C C . ARG A 162 ? 1.3220 1.1507 0.7689 -0.0370 -0.1255 -0.0975 162 ARG A C 1290 O O . ARG A 162 ? 1.3295 1.1651 0.7926 -0.0294 -0.1200 -0.0850 162 ARG A O 1291 C CB . ARG A 162 ? 1.3141 1.1927 0.7661 -0.0504 -0.1286 -0.1002 162 ARG A CB 1292 C CG . ARG A 162 ? 1.3379 1.2490 0.7848 -0.0500 -0.1316 -0.1068 162 ARG A CG 1293 C CD . ARG A 162 ? 1.3854 1.2850 0.8109 -0.0543 -0.1386 -0.1263 162 ARG A CD 1294 N NE . ARG A 162 ? 1.3992 1.3277 0.8226 -0.0632 -0.1446 -0.1359 162 ARG A NE 1295 C CZ . ARG A 162 ? 1.3989 1.3269 0.8265 -0.0842 -0.1497 -0.1433 162 ARG A CZ 1296 N NH1 . ARG A 162 ? 1.3991 1.2962 0.8307 -0.0988 -0.1490 -0.1416 162 ARG A NH1 1297 N NH2 . ARG A 162 ? 1.4256 1.3858 0.8533 -0.0903 -0.1554 -0.1526 162 ARG A NH2 1298 N N . SER A 163 ? 1.3378 1.1324 0.7701 -0.0472 -0.1310 -0.1075 163 SER A N 1299 C CA . SER A 163 ? 1.3247 1.0876 0.7574 -0.0488 -0.1314 -0.1031 163 SER A CA 1300 C C . SER A 163 ? 1.3418 1.0802 0.7667 -0.0695 -0.1358 -0.1076 163 SER A C 1301 O O . SER A 163 ? 1.3356 1.0690 0.7486 -0.0817 -0.1392 -0.1196 163 SER A O 1302 C CB . SER A 163 ? 1.3394 1.0763 0.7580 -0.0348 -0.1318 -0.1092 163 SER A CB 1303 O OG . SER A 163 ? 1.3249 1.0828 0.7544 -0.0157 -0.1261 -0.1026 163 SER A OG 1304 N N . TYR A 164 ? 1.3436 1.0678 0.7753 -0.0737 -0.1353 -0.0983 164 TYR A N 1305 C CA . TYR A 164 ? 1.3632 1.0563 0.7838 -0.0909 -0.1379 -0.1013 164 TYR A CA 1306 C C . TYR A 164 ? 1.3868 1.0445 0.7989 -0.0834 -0.1387 -0.0966 164 TYR A C 1307 O O . TYR A 164 ? 1.3786 1.0456 0.8035 -0.0716 -0.1374 -0.0867 164 TYR A O 1308 C CB . TYR A 164 ? 1.3307 1.0417 0.7649 -0.1064 -0.1367 -0.0947 164 TYR A CB 1309 C CG . TYR A 164 ? 1.3793 1.0567 0.8015 -0.1234 -0.1378 -0.0961 164 TYR A CG 1310 C CD1 . TYR A 164 ? 1.4147 1.0750 0.8228 -0.1398 -0.1392 -0.1083 164 TYR A CD1 1311 C CD2 . TYR A 164 ? 1.3987 1.0599 0.8225 -0.1228 -0.1369 -0.0856 164 TYR A CD2 1312 C CE1 . TYR A 164 ? 1.4432 1.0699 0.8394 -0.1559 -0.1382 -0.1087 164 TYR A CE1 1313 C CE2 . TYR A 164 ? 1.4367 1.0652 0.8467 -0.1372 -0.1368 -0.0856 164 TYR A CE2 1314 C CZ . TYR A 164 ? 1.4636 1.0739 0.8597 -0.1539 -0.1367 -0.0964 164 TYR A CZ 1315 O OH . TYR A 164 ? 1.5258 1.1016 0.9079 -0.1687 -0.1346 -0.0953 164 TYR A OH 1316 N N . ASN A 165 ? 1.4409 1.0581 0.8313 -0.0903 -0.1408 -0.1042 165 ASN A N 1317 C CA . ASN A 165 ? 1.4963 1.0753 0.8737 -0.0825 -0.1419 -0.1001 165 ASN A CA 1318 C C . ASN A 165 ? 1.5053 1.0634 0.8772 -0.0990 -0.1416 -0.0944 165 ASN A C 1319 O O . ASN A 165 ? 1.5397 1.0868 0.9035 -0.1183 -0.1406 -0.1007 165 ASN A O 1320 C CB . ASN A 165 ? 1.5736 1.1164 0.9274 -0.0776 -0.1431 -0.1118 165 ASN A CB 1321 C CG . ASN A 165 ? 1.6512 1.1568 0.9912 -0.0631 -0.1443 -0.1073 165 ASN A CG 1322 O OD1 . ASN A 165 ? 1.6461 1.1285 0.9794 -0.0682 -0.1447 -0.0996 165 ASN A OD1 1323 N ND2 . ASN A 165 ? 1.7435 1.2436 1.0781 -0.0437 -0.1447 -0.1120 165 ASN A ND2 1324 N N . ASN A 166 ? 1.4964 1.0505 0.8730 -0.0917 -0.1423 -0.0831 166 ASN A N 1325 C CA . ASN A 166 ? 1.5109 1.0432 0.8791 -0.1049 -0.1416 -0.0766 166 ASN A CA 1326 C C . ASN A 166 ? 1.5564 1.0350 0.8957 -0.1041 -0.1420 -0.0790 166 ASN A C 1327 O O . ASN A 166 ? 1.5565 1.0148 0.8869 -0.0888 -0.1444 -0.0726 166 ASN A O 1328 C CB . ASN A 166 ? 1.4991 1.0484 0.8818 -0.0968 -0.1426 -0.0646 166 ASN A CB 1329 C CG . ASN A 166 ? 1.5239 1.0596 0.9001 -0.1119 -0.1411 -0.0579 166 ASN A CG 1330 O OD1 . ASN A 166 ? 1.5524 1.0794 0.9217 -0.1312 -0.1379 -0.0615 166 ASN A OD1 1331 N ND2 . ASN A 166 ? 1.5041 1.0400 0.8831 -0.1034 -0.1432 -0.0488 166 ASN A ND2 1332 N N . THR A 167 ? 1.5746 1.0308 0.8994 -0.1204 -0.1396 -0.0886 167 THR A N 1333 C CA . THR A 167 ? 1.6236 1.0238 0.9193 -0.1219 -0.1382 -0.0917 167 THR A CA 1334 C C . THR A 167 ? 1.6444 1.0165 0.9274 -0.1331 -0.1352 -0.0817 167 THR A C 1335 O O . THR A 167 ? 1.7000 1.0318 0.9618 -0.1226 -0.1353 -0.0755 167 THR A O 1336 C CB . THR A 167 ? 1.6338 1.0187 0.9191 -0.1375 -0.1358 -0.1073 167 THR A CB 1337 O OG1 . THR A 167 ? 1.6166 1.0255 0.9143 -0.1617 -0.1332 -0.1105 167 THR A OG1 1338 C CG2 . THR A 167 ? 1.6161 1.0222 0.9076 -0.1238 -0.1387 -0.1177 167 THR A CG2 1339 N N . ASN A 168 ? 1.6006 0.9937 0.8952 -0.1535 -0.1320 -0.0799 168 ASN A N 1340 C CA . ASN A 168 ? 1.6002 0.9727 0.8846 -0.1648 -0.1280 -0.0697 168 ASN A CA 1341 C C . ASN A 168 ? 1.5660 0.9369 0.8483 -0.1461 -0.1316 -0.0559 168 ASN A C 1342 O O . ASN A 168 ? 1.5122 0.9164 0.8129 -0.1297 -0.1367 -0.0536 168 ASN A O 1343 C CB . ASN A 168 ? 1.5632 0.9672 0.8648 -0.1880 -0.1239 -0.0705 168 ASN A CB 1344 C CG . ASN A 168 ? 1.4974 0.9595 0.8294 -0.1841 -0.1272 -0.0729 168 ASN A CG 1345 O OD1 . ASN A 168 ? 1.4754 0.9654 0.8217 -0.2006 -0.1249 -0.0783 168 ASN A OD1 1346 N ND2 . ASN A 168 ? 1.4605 0.9413 0.8027 -0.1621 -0.1320 -0.0688 168 ASN A ND2 1347 N N . GLN A 169 ? 1.5926 0.9246 0.8519 -0.1491 -0.1287 -0.0473 169 GLN A N 1348 C CA . GLN A 169 ? 1.6102 0.9331 0.8606 -0.1299 -0.1330 -0.0353 169 GLN A CA 1349 C C . GLN A 169 ? 1.5515 0.9203 0.8258 -0.1269 -0.1362 -0.0288 169 GLN A C 1350 O O . GLN A 169 ? 1.5227 0.8999 0.7997 -0.1074 -0.1424 -0.0231 169 GLN A O 1351 C CB . GLN A 169 ? 1.6718 0.9421 0.8892 -0.1352 -0.1280 -0.0266 169 GLN A CB 1352 C CG . GLN A 169 ? 1.7211 0.9447 0.9104 -0.1140 -0.1306 -0.0230 169 GLN A CG 1353 C CD . GLN A 169 ? 1.7643 0.9505 0.9248 -0.1098 -0.1285 -0.0090 169 GLN A CD 1354 O OE1 . GLN A 169 ? 1.7962 0.9414 0.9334 -0.1259 -0.1194 -0.0059 169 GLN A OE1 1355 N NE2 . GLN A 169 ? 1.7360 0.9371 0.8978 -0.0883 -0.1366 -0.0007 169 GLN A NE2 1356 N N . GLU A 170 ? 1.5090 0.9077 0.8012 -0.1460 -0.1320 -0.0306 170 GLU A N 1357 C CA . GLU A 170 ? 1.4458 0.8813 0.7572 -0.1467 -0.1329 -0.0244 170 GLU A CA 1358 C C . GLU A 170 ? 1.3977 0.8816 0.7405 -0.1371 -0.1367 -0.0281 170 GLU A C 1359 O O . GLU A 170 ? 1.3981 0.8986 0.7528 -0.1406 -0.1358 -0.0362 170 GLU A O 1360 C CB . GLU A 170 ? 1.4277 0.8709 0.7425 -0.1712 -0.1253 -0.0240 170 GLU A CB 1361 C CG . GLU A 170 ? 1.4878 0.8842 0.7728 -0.1844 -0.1188 -0.0199 170 GLU A CG 1362 C CD . GLU A 170 ? 1.5231 0.8942 0.7981 -0.1992 -0.1138 -0.0292 170 GLU A CD 1363 O OE1 . GLU A 170 ? 1.5644 0.9395 0.8451 -0.1918 -0.1177 -0.0380 170 GLU A OE1 1364 O OE2 . GLU A 170 ? 1.5543 0.9012 0.8157 -0.2188 -0.1055 -0.0282 170 GLU A OE2 1365 N N . ASP A 171 ? 1.3745 0.8803 0.7300 -0.1251 -0.1406 -0.0225 171 ASP A N 1366 C CA . ASP A 171 ? 1.3215 0.8730 0.7082 -0.1185 -0.1420 -0.0245 171 ASP A CA 1367 C C . ASP A 171 ? 1.2962 0.8737 0.6988 -0.1352 -0.1364 -0.0285 171 ASP A C 1368 O O . ASP A 171 ? 1.3025 0.8740 0.6989 -0.1523 -0.1318 -0.0274 171 ASP A O 1369 C CB . ASP A 171 ? 1.3253 0.8962 0.7235 -0.1123 -0.1444 -0.0185 171 ASP A CB 1370 C CG . ASP A 171 ? 1.3436 0.9077 0.7379 -0.0912 -0.1519 -0.0165 171 ASP A CG 1371 O OD1 . ASP A 171 ? 1.3686 0.9254 0.7609 -0.0782 -0.1548 -0.0201 171 ASP A OD1 1372 O OD2 . ASP A 171 ? 1.3473 0.9162 0.7417 -0.0870 -0.1551 -0.0122 171 ASP A OD2 1373 N N . LEU A 172 ? 1.2728 0.8801 0.6955 -0.1295 -0.1364 -0.0329 172 LEU A N 1374 C CA . LEU A 172 ? 1.2486 0.8834 0.6860 -0.1419 -0.1320 -0.0368 172 LEU A CA 1375 C C . LEU A 172 ? 1.2027 0.8784 0.6677 -0.1361 -0.1302 -0.0334 172 LEU A C 1376 O O . LEU A 172 ? 1.1936 0.8814 0.6699 -0.1209 -0.1319 -0.0324 172 LEU A O 1377 C CB . LEU A 172 ? 1.2658 0.8975 0.6985 -0.1410 -0.1327 -0.0456 172 LEU A CB 1378 C CG . LEU A 172 ? 1.2690 0.9239 0.7106 -0.1556 -0.1295 -0.0515 172 LEU A CG 1379 C CD1 . LEU A 172 ? 1.2884 0.9201 0.7146 -0.1761 -0.1270 -0.0551 172 LEU A CD1 1380 C CD2 . LEU A 172 ? 1.2726 0.9387 0.7162 -0.1478 -0.1312 -0.0596 172 LEU A CD2 1381 N N . LEU A 173 ? 1.1752 0.8712 0.6511 -0.1484 -0.1258 -0.0317 173 LEU A N 1382 C CA . LEU A 173 ? 1.1405 0.8730 0.6415 -0.1442 -0.1225 -0.0285 173 LEU A CA 1383 C C . LEU A 173 ? 1.1540 0.9105 0.6647 -0.1445 -0.1204 -0.0327 173 LEU A C 1384 O O . LEU A 173 ? 1.1635 0.9265 0.6722 -0.1574 -0.1188 -0.0363 173 LEU A O 1385 C CB . LEU A 173 ? 1.1230 0.8653 0.6301 -0.1553 -0.1185 -0.0244 173 LEU A CB 1386 C CG . LEU A 173 ? 1.0924 0.8702 0.6245 -0.1524 -0.1135 -0.0213 173 LEU A CG 1387 C CD1 . LEU A 173 ? 1.0831 0.8699 0.6292 -0.1372 -0.1140 -0.0186 173 LEU A CD1 1388 C CD2 . LEU A 173 ? 1.0878 0.8723 0.6235 -0.1633 -0.1093 -0.0182 173 LEU A CD2 1389 N N . VAL A 174 ? 1.1529 0.9246 0.6747 -0.1300 -0.1202 -0.0323 174 VAL A N 1390 C CA . VAL A 174 ? 1.1387 0.9344 0.6680 -0.1267 -0.1183 -0.0352 174 VAL A CA 1391 C C . VAL A 174 ? 1.1027 0.9306 0.6544 -0.1219 -0.1123 -0.0287 174 VAL A C 1392 O O . VAL A 174 ? 1.0930 0.9246 0.6568 -0.1138 -0.1099 -0.0234 174 VAL A O 1393 C CB . VAL A 174 ? 1.1492 0.9388 0.6731 -0.1127 -0.1205 -0.0388 174 VAL A CB 1394 C CG1 . VAL A 174 ? 1.1525 0.9661 0.6800 -0.1093 -0.1188 -0.0423 174 VAL A CG1 1395 C CG2 . VAL A 174 ? 1.1789 0.9323 0.6800 -0.1152 -0.1257 -0.0447 174 VAL A CG2 1396 N N . LEU A 175 ? 1.0857 0.9367 0.6430 -0.1268 -0.1099 -0.0295 175 LEU A N 1397 C CA . LEU A 175 ? 1.0658 0.9460 0.6421 -0.1216 -0.1035 -0.0228 175 LEU A CA 1398 C C . LEU A 175 ? 1.0803 0.9830 0.6590 -0.1121 -0.1021 -0.0236 175 LEU A C 1399 O O . LEU A 175 ? 1.0780 0.9842 0.6462 -0.1170 -0.1063 -0.0310 175 LEU A O 1400 C CB . LEU A 175 ? 1.0667 0.9579 0.6476 -0.1344 -0.1015 -0.0220 175 LEU A CB 1401 C CG . LEU A 175 ? 1.0912 0.9641 0.6691 -0.1445 -0.1015 -0.0205 175 LEU A CG 1402 C CD1 . LEU A 175 ? 1.1024 0.9873 0.6823 -0.1583 -0.0993 -0.0216 175 LEU A CD1 1403 C CD2 . LEU A 175 ? 1.0674 0.9418 0.6585 -0.1362 -0.0975 -0.0140 175 LEU A CD2 1404 N N . TRP A 176 ? 1.0543 0.9720 0.6462 -0.0988 -0.0958 -0.0163 176 TRP A N 1405 C CA . TRP A 176 ? 1.0471 0.9882 0.6409 -0.0880 -0.0927 -0.0144 176 TRP A CA 1406 C C . TRP A 176 ? 1.0420 1.0012 0.6535 -0.0791 -0.0830 -0.0035 176 TRP A C 1407 O O . TRP A 176 ? 1.0541 1.0069 0.6769 -0.0823 -0.0791 0.0008 176 TRP A O 1408 C CB . TRP A 176 ? 1.0511 0.9845 0.6356 -0.0772 -0.0942 -0.0177 176 TRP A CB 1409 C CG . TRP A 176 ? 1.0251 0.9501 0.6194 -0.0675 -0.0891 -0.0122 176 TRP A CG 1410 C CD1 . TRP A 176 ? 1.0073 0.9464 0.6131 -0.0544 -0.0802 -0.0045 176 TRP A CD1 1411 C CD2 . TRP A 176 ? 1.0185 0.9205 0.6123 -0.0701 -0.0924 -0.0144 176 TRP A CD2 1412 N NE1 . TRP A 176 ? 0.9908 0.9187 0.6058 -0.0502 -0.0776 -0.0028 176 TRP A NE1 1413 C CE2 . TRP A 176 ? 1.0011 0.9076 0.6090 -0.0589 -0.0858 -0.0091 176 TRP A CE2 1414 C CE3 . TRP A 176 ? 1.0308 0.9088 0.6132 -0.0804 -0.0999 -0.0200 176 TRP A CE3 1415 C CZ2 . TRP A 176 ? 1.0088 0.9005 0.6213 -0.0573 -0.0879 -0.0104 176 TRP A CZ2 1416 C CZ3 . TRP A 176 ? 1.0288 0.8897 0.6129 -0.0772 -0.1019 -0.0200 176 TRP A CZ3 1417 C CH2 . TRP A 176 ? 1.0199 0.8895 0.6197 -0.0657 -0.0966 -0.0158 176 TRP A CH2 1418 N N . GLY A 177 ? 1.0650 1.0457 0.6778 -0.0675 -0.0787 0.0007 177 GLY A N 1419 C CA . GLY A 177 ? 1.0564 1.0519 0.6840 -0.0577 -0.0678 0.0122 177 GLY A CA 1420 C C . GLY A 177 ? 1.0528 1.0617 0.6782 -0.0409 -0.0615 0.0183 177 GLY A C 1421 O O . GLY A 177 ? 1.0420 1.0504 0.6542 -0.0362 -0.0660 0.0128 177 GLY A O 1422 N N . ILE A 178 ? 1.0414 1.0605 0.6788 -0.0315 -0.0502 0.0298 178 ILE A N 1423 C CA . ILE A 178 ? 1.0437 1.0761 0.6783 -0.0144 -0.0418 0.0384 178 ILE A CA 1424 C C . ILE A 178 ? 1.0376 1.0875 0.6784 -0.0072 -0.0344 0.0486 178 ILE A C 1425 O O . ILE A 178 ? 1.0424 1.0880 0.6961 -0.0132 -0.0304 0.0518 178 ILE A O 1426 C CB . ILE A 178 ? 1.0562 1.0761 0.7002 -0.0075 -0.0314 0.0442 178 ILE A CB 1427 C CG1 . ILE A 178 ? 1.0761 1.1089 0.7151 0.0103 -0.0208 0.0543 178 ILE A CG1 1428 C CG2 . ILE A 178 ? 1.0424 1.0520 0.7067 -0.0131 -0.0230 0.0494 178 ILE A CG2 1429 C CD1 . ILE A 178 ? 1.0869 1.1097 0.7346 0.0166 -0.0098 0.0591 178 ILE A CD1 1430 N N . HIS A 179 ? 1.0642 1.1339 0.6945 0.0067 -0.0327 0.0535 179 HIS A N 1431 C CA . HIS A 179 ? 1.0535 1.1407 0.6875 0.0175 -0.0254 0.0646 179 HIS A CA 1432 C C . HIS A 179 ? 1.0570 1.1394 0.6954 0.0334 -0.0084 0.0799 179 HIS A C 1433 O O . HIS A 179 ? 1.0684 1.1499 0.6981 0.0431 -0.0044 0.0827 179 HIS A O 1434 C CB . HIS A 179 ? 1.0533 1.1687 0.6726 0.0244 -0.0345 0.0608 179 HIS A CB 1435 C CG . HIS A 179 ? 1.0512 1.1870 0.6716 0.0401 -0.0271 0.0734 179 HIS A CG 1436 N ND1 . HIS A 179 ? 1.0731 1.2269 0.6795 0.0600 -0.0239 0.0812 179 HIS A ND1 1437 C CD2 . HIS A 179 ? 1.0451 1.1851 0.6779 0.0404 -0.0218 0.0799 179 HIS A CD2 1438 C CE1 . HIS A 179 ? 1.0837 1.2520 0.6937 0.0725 -0.0172 0.0927 179 HIS A CE1 1439 N NE2 . HIS A 179 ? 1.0740 1.2340 0.7005 0.0609 -0.0157 0.0919 179 HIS A NE2 1440 N N . HIS A 180 ? 1.0552 1.1334 0.7072 0.0355 0.0023 0.0897 180 HIS A N 1441 C CA . HIS A 180 ? 1.0709 1.1429 0.7276 0.0500 0.0204 0.1054 180 HIS A CA 1442 C C . HIS A 180 ? 1.0942 1.1863 0.7428 0.0665 0.0241 0.1162 180 HIS A C 1443 O O . HIS A 180 ? 1.0892 1.1880 0.7446 0.0636 0.0221 0.1161 180 HIS A O 1444 C CB . HIS A 180 ? 1.0734 1.1236 0.7513 0.0407 0.0310 0.1081 180 HIS A CB 1445 C CG . HIS A 180 ? 1.0592 1.0930 0.7460 0.0250 0.0255 0.0968 180 HIS A CG 1446 N ND1 . HIS A 180 ? 1.0772 1.1059 0.7605 0.0268 0.0261 0.0944 180 HIS A ND1 1447 C CD2 . HIS A 180 ? 1.0440 1.0661 0.7420 0.0086 0.0195 0.0874 180 HIS A CD2 1448 C CE1 . HIS A 180 ? 1.0567 1.0721 0.7494 0.0129 0.0200 0.0841 180 HIS A CE1 1449 N NE2 . HIS A 180 ? 1.0556 1.0665 0.7565 0.0017 0.0158 0.0799 180 HIS A NE2 1450 N N . PRO A 181 ? 1.1064 1.2098 0.7395 0.0851 0.0292 0.1253 181 PRO A N 1451 C CA . PRO A 181 ? 1.1147 1.2392 0.7374 0.1039 0.0320 0.1363 181 PRO A CA 1452 C C . PRO A 181 ? 1.1131 1.2232 0.7435 0.1166 0.0528 0.1549 181 PRO A C 1453 O O . PRO A 181 ? 1.0934 1.1779 0.7372 0.1100 0.0656 0.1586 181 PRO A O 1454 C CB . PRO A 181 ? 1.1420 1.2825 0.7423 0.1181 0.0283 0.1371 181 PRO A CB 1455 C CG . PRO A 181 ? 1.1444 1.2630 0.7471 0.1133 0.0359 0.1365 181 PRO A CG 1456 C CD . PRO A 181 ? 1.1235 1.2217 0.7466 0.0906 0.0326 0.1258 181 PRO A CD 1457 N N . ASN A 182 ? 1.1261 1.2528 0.7480 0.1349 0.0562 0.1661 182 ASN A N 1458 C CA . ASN A 182 ? 1.1568 1.2681 0.7842 0.1486 0.0764 0.1846 182 ASN A CA 1459 C C . ASN A 182 ? 1.2062 1.3054 0.8219 0.1658 0.0943 0.2013 182 ASN A C 1460 O O . ASN A 182 ? 1.2216 1.2936 0.8483 0.1663 0.1139 0.2123 182 ASN A O 1461 C CB . ASN A 182 ? 1.1608 1.2946 0.7831 0.1636 0.0733 0.1908 182 ASN A CB 1462 C CG . ASN A 182 ? 1.1427 1.2833 0.7807 0.1467 0.0618 0.1774 182 ASN A CG 1463 O OD1 . ASN A 182 ? 1.1585 1.2754 0.8142 0.1327 0.0687 0.1750 182 ASN A OD1 1464 N ND2 . ASN A 182 ? 1.1398 1.3136 0.7716 0.1470 0.0445 0.1677 182 ASN A ND2 1465 N N . ASP A 183 ? 1.2346 1.3538 0.8279 0.1794 0.0881 0.2026 183 ASP A N 1466 C CA . ASP A 183 ? 1.2664 1.3774 0.8444 0.1978 0.1049 0.2190 183 ASP A CA 1467 C C . ASP A 183 ? 1.2573 1.3838 0.8166 0.2001 0.0945 0.2107 183 ASP A C 1468 O O . ASP A 183 ? 1.2133 1.3547 0.7724 0.1867 0.0744 0.1916 183 ASP A O 1469 C CB . ASP A 183 ? 1.3052 1.4247 0.8676 0.2254 0.1153 0.2392 183 ASP A CB 1470 C CG . ASP A 183 ? 1.3157 1.4740 0.8640 0.2361 0.0955 0.2330 183 ASP A CG 1471 O OD1 . ASP A 183 ? 1.3222 1.5043 0.8570 0.2349 0.0788 0.2205 183 ASP A OD1 1472 O OD2 . ASP A 183 ? 1.3187 1.4844 0.8702 0.2460 0.0968 0.2400 183 ASP A OD2 1473 N N . ALA A 184 ? 1.2839 1.4051 0.8272 0.2172 0.1094 0.2250 184 ALA A N 1474 C CA . ALA A 184 ? 1.2754 1.4099 0.7987 0.2223 0.1026 0.2186 184 ALA A CA 1475 C C . ALA A 184 ? 1.2804 1.4513 0.7800 0.2352 0.0832 0.2118 184 ALA A C 1476 O O . ALA A 184 ? 1.2537 1.4389 0.7419 0.2306 0.0686 0.1965 184 ALA A O 1477 C CB . ALA A 184 ? 1.2776 1.3974 0.7893 0.2384 0.1259 0.2373 184 ALA A CB 1478 N N . ALA A 185 ? 1.2996 1.4857 0.7924 0.2515 0.0832 0.2223 185 ALA A N 1479 C CA . ALA A 185 ? 1.3239 1.5493 0.7968 0.2646 0.0645 0.2157 185 ALA A CA 1480 C C . ALA A 185 ? 1.3016 1.5449 0.7877 0.2424 0.0406 0.1911 185 ALA A C 1481 O O . ALA A 185 ? 1.3225 1.5958 0.7943 0.2443 0.0224 0.1774 185 ALA A O 1482 C CB . ALA A 185 ? 1.3481 1.5854 0.8120 0.2895 0.0719 0.2345 185 ALA A CB 1483 N N . GLU A 186 ? 1.2594 1.4842 0.7721 0.2213 0.0412 0.1854 186 GLU A N 1484 C CA . GLU A 186 ? 1.2189 1.4548 0.7448 0.1980 0.0212 0.1632 186 GLU A CA 1485 C C . GLU A 186 ? 1.1873 1.4140 0.7109 0.1809 0.0123 0.1462 186 GLU A C 1486 O O . GLU A 186 ? 1.1584 1.4037 0.6773 0.1706 -0.0062 0.1278 186 GLU A O 1487 C CB . GLU A 186 ? 1.2079 1.4250 0.7604 0.1821 0.0261 0.1634 186 GLU A CB 1488 C CG . GLU A 186 ? 1.1770 1.4060 0.7425 0.1595 0.0075 0.1430 186 GLU A CG 1489 C CD . GLU A 186 ? 1.1586 1.3805 0.7449 0.1520 0.0120 0.1461 186 GLU A CD 1490 O OE1 . GLU A 186 ? 1.1664 1.3590 0.7693 0.1358 0.0188 0.1444 186 GLU A OE1 1491 O OE2 . GLU A 186 ? 1.1386 1.3853 0.7246 0.1633 0.0088 0.1498 186 GLU A OE2 1492 N N . GLN A 187 ? 1.1735 1.3715 0.7010 0.1782 0.0264 0.1523 187 GLN A N 1493 C CA . GLN A 187 ? 1.1683 1.3555 0.6933 0.1653 0.0203 0.1383 187 GLN A CA 1494 C C . GLN A 187 ? 1.2049 1.4168 0.7039 0.1751 0.0076 0.1286 187 GLN A C 1495 O O . GLN A 187 ? 1.1780 1.3953 0.6752 0.1604 -0.0089 0.1088 187 GLN A O 1496 C CB . GLN A 187 ? 1.1666 1.3259 0.6980 0.1672 0.0401 0.1496 187 GLN A CB 1497 C CG . GLN A 187 ? 1.1550 1.3032 0.6852 0.1566 0.0358 0.1366 187 GLN A CG 1498 C CD . GLN A 187 ? 1.1191 1.2565 0.6660 0.1316 0.0220 0.1185 187 GLN A CD 1499 O OE1 . GLN A 187 ? 1.0982 1.2236 0.6655 0.1195 0.0241 0.1195 187 GLN A OE1 1500 N NE2 . GLN A 187 ? 1.1063 1.2463 0.6431 0.1244 0.0084 0.1019 187 GLN A NE2 1501 N N . THR A 188 ? 1.2457 1.4714 0.7236 0.2000 0.0156 0.1424 188 THR A N 1502 C CA . THR A 188 ? 1.2666 1.5175 0.7171 0.2118 0.0041 0.1335 188 THR A CA 1503 C C . THR A 188 ? 1.2558 1.5404 0.7025 0.2089 -0.0169 0.1192 188 THR A C 1504 O O . THR A 188 ? 1.2598 1.5596 0.6952 0.2024 -0.0331 0.1000 188 THR A O 1505 C CB . THR A 188 ? 1.3194 1.5776 0.7454 0.2411 0.0186 0.1531 188 THR A CB 1506 O OG1 . THR A 188 ? 1.3537 1.6260 0.7774 0.2583 0.0236 0.1693 188 THR A OG1 1507 C CG2 . THR A 188 ? 1.3268 1.5531 0.7581 0.2429 0.0412 0.1670 188 THR A CG2 1508 N N . LYS A 189 ? 1.2350 1.5313 0.6926 0.2129 -0.0163 0.1275 189 LYS A N 1509 C CA . LYS A 189 ? 1.2382 1.5702 0.6961 0.2102 -0.0352 0.1145 189 LYS A CA 1510 C C . LYS A 189 ? 1.2227 1.5534 0.6940 0.1808 -0.0520 0.0894 189 LYS A C 1511 O O . LYS A 189 ? 1.2022 1.5630 0.6672 0.1767 -0.0695 0.0727 189 LYS A O 1512 C CB . LYS A 189 ? 1.2503 1.5909 0.7218 0.2185 -0.0293 0.1284 189 LYS A CB 1513 C CG . LYS A 189 ? 1.2683 1.6499 0.7434 0.2168 -0.0477 0.1157 189 LYS A CG 1514 C CD . LYS A 189 ? 1.2816 1.6698 0.7716 0.2253 -0.0407 0.1295 189 LYS A CD 1515 C CE . LYS A 189 ? 1.2708 1.6884 0.7774 0.2097 -0.0576 0.1122 189 LYS A CE 1516 N NZ . LYS A 189 ? 1.2628 1.6836 0.7865 0.2158 -0.0500 0.1242 189 LYS A NZ 1517 N N . LEU A 190 ? 1.2196 1.5159 0.7088 0.1606 -0.0466 0.0868 190 LEU A N 1518 C CA . LEU A 190 ? 1.2202 1.5097 0.7207 0.1332 -0.0605 0.0654 190 LEU A CA 1519 C C . LEU A 190 ? 1.2343 1.5051 0.7243 0.1244 -0.0643 0.0526 190 LEU A C 1520 O O . LEU A 190 ? 1.2145 1.4895 0.7020 0.1085 -0.0790 0.0325 190 LEU A O 1521 C CB . LEU A 190 ? 1.2065 1.4712 0.7326 0.1159 -0.0542 0.0688 190 LEU A CB 1522 C CG . LEU A 190 ? 1.2090 1.4856 0.7489 0.1218 -0.0489 0.0805 190 LEU A CG 1523 C CD1 . LEU A 190 ? 1.1812 1.4349 0.7442 0.0999 -0.0471 0.0771 190 LEU A CD1 1524 C CD2 . LEU A 190 ? 1.2174 1.5371 0.7521 0.1282 -0.0623 0.0734 190 LEU A CD2 1525 N N . TYR A 191 ? 1.2651 1.5144 0.7497 0.1344 -0.0502 0.0640 191 TYR A N 1526 C CA . TYR A 191 ? 1.2862 1.5134 0.7648 0.1262 -0.0513 0.0535 191 TYR A CA 1527 C C . TYR A 191 ? 1.3396 1.5710 0.7949 0.1464 -0.0446 0.0586 191 TYR A C 1528 O O . TYR A 191 ? 1.3330 1.5487 0.7817 0.1421 -0.0453 0.0494 191 TYR A O 1529 C CB . TYR A 191 ? 1.2717 1.4645 0.7715 0.1137 -0.0406 0.0593 191 TYR A CB 1530 C CG . TYR A 191 ? 1.2401 1.4271 0.7621 0.0973 -0.0432 0.0587 191 TYR A CG 1531 C CD1 . TYR A 191 ? 1.2433 1.4321 0.7696 0.0775 -0.0586 0.0411 191 TYR A CD1 1532 C CD2 . TYR A 191 ? 1.2284 1.4072 0.7664 0.1014 -0.0294 0.0754 191 TYR A CD2 1533 C CE1 . TYR A 191 ? 1.2323 1.4162 0.7775 0.0628 -0.0600 0.0408 191 TYR A CE1 1534 C CE2 . TYR A 191 ? 1.2232 1.3969 0.7800 0.0871 -0.0315 0.0741 191 TYR A CE2 1535 C CZ . TYR A 191 ? 1.2189 1.3961 0.7789 0.0681 -0.0469 0.0570 191 TYR A CZ 1536 O OH . TYR A 191 ? 1.1613 1.3341 0.7387 0.0543 -0.0482 0.0559 191 TYR A OH 1537 N N . ARG A 192 ? 1.3717 1.6240 0.8136 0.1693 -0.0377 0.0733 192 ARG A N 1538 C CA . ARG A 192 ? 1.4146 1.6713 0.8326 0.1914 -0.0282 0.0821 192 ARG A CA 1539 C C . ARG A 192 ? 1.4097 1.6361 0.8349 0.1936 -0.0084 0.0948 192 ARG A C 1540 O O . ARG A 192 ? 1.4188 1.6432 0.8390 0.2115 0.0092 0.1154 192 ARG A O 1541 C CB . ARG A 192 ? 1.4579 1.7303 0.8524 0.1924 -0.0434 0.0619 192 ARG A CB 1542 C CG . ARG A 192 ? 1.5285 1.8301 0.8934 0.2193 -0.0428 0.0686 192 ARG A CG 1543 C CD . ARG A 192 ? 1.5775 1.8799 0.9173 0.2263 -0.0455 0.0569 192 ARG A CD 1544 N NE . ARG A 192 ? 1.6097 1.8920 0.9434 0.2397 -0.0245 0.0736 192 ARG A NE 1545 C CZ . ARG A 192 ? 1.6544 1.9478 0.9659 0.2657 -0.0117 0.0910 192 ARG A CZ 1546 N NH1 . ARG A 192 ? 1.6629 1.9886 0.9537 0.2841 -0.0185 0.0948 192 ARG A NH1 1547 N NH2 . ARG A 192 ? 1.6715 1.9444 0.9812 0.2740 0.0086 0.1049 192 ARG A NH2 1548 N N . ASN A 193 ? 1.3802 1.5838 0.8171 0.1760 -0.0108 0.0827 193 ASN A N 1549 C CA . ASN A 193 ? 1.3687 1.5475 0.8149 0.1767 0.0061 0.0915 193 ASN A CA 1550 C C . ASN A 193 ? 1.3483 1.5134 0.8171 0.1761 0.0230 0.1106 193 ASN A C 1551 O O . ASN A 193 ? 1.3266 1.4875 0.8138 0.1625 0.0177 0.1087 193 ASN A O 1552 C CB . ASN A 193 ? 1.3642 1.5226 0.8215 0.1574 -0.0018 0.0741 193 ASN A CB 1553 C CG . ASN A 193 ? 1.3923 1.5596 0.8295 0.1541 -0.0196 0.0526 193 ASN A CG 1554 O OD1 . ASN A 193 ? 1.4337 1.6222 0.8592 0.1545 -0.0330 0.0445 193 ASN A OD1 1555 N ND2 . ASN A 193 ? 1.3921 1.5432 0.8264 0.1504 -0.0200 0.0423 193 ASN A ND2 1556 N N . PRO A 194 ? 1.3681 1.5256 0.8351 0.1904 0.0441 0.1287 194 PRO A N 1557 C CA . PRO A 194 ? 1.3454 1.4882 0.8332 0.1898 0.0615 0.1465 194 PRO A CA 1558 C C . PRO A 194 ? 1.3079 1.4265 0.8257 0.1692 0.0654 0.1411 194 PRO A C 1559 O O . PRO A 194 ? 1.2736 1.3824 0.8120 0.1590 0.0680 0.1450 194 PRO A O 1560 C CB . PRO A 194 ? 1.3726 1.5143 0.8462 0.2112 0.0833 0.1661 194 PRO A CB 1561 C CG . PRO A 194 ? 1.4000 1.5464 0.8565 0.2157 0.0802 0.1560 194 PRO A CG 1562 C CD . PRO A 194 ? 1.3950 1.5553 0.8415 0.2067 0.0541 0.1331 194 PRO A CD 1563 N N . THR A 195 ? 1.2919 1.4022 0.8114 0.1642 0.0655 0.1319 195 THR A N 1564 C CA . THR A 195 ? 1.2662 1.3570 0.8128 0.1467 0.0678 0.1256 195 THR A CA 1565 C C . THR A 195 ? 1.2340 1.3231 0.7791 0.1325 0.0464 0.1039 195 THR A C 1566 O O . THR A 195 ? 1.2432 1.3359 0.7724 0.1371 0.0404 0.0940 195 THR A O 1567 C CB . THR A 195 ? 1.2766 1.3591 0.8295 0.1525 0.0864 0.1324 195 THR A CB 1568 O OG1 . THR A 195 ? 1.2889 1.3727 0.8368 0.1680 0.1075 0.1533 195 THR A OG1 1569 C CG2 . THR A 195 ? 1.2606 1.3264 0.8456 0.1353 0.0903 0.1277 195 THR A CG2 1570 N N . THR A 196 ? 1.2001 1.2820 0.7605 0.1158 0.0359 0.0966 196 THR A N 1571 C CA . THR A 196 ? 1.1828 1.2598 0.7412 0.1016 0.0166 0.0774 196 THR A CA 1572 C C . THR A 196 ? 1.1535 1.2111 0.7358 0.0858 0.0162 0.0722 196 THR A C 1573 O O . THR A 196 ? 1.1220 1.1721 0.7247 0.0841 0.0298 0.0820 196 THR A O 1574 C CB . THR A 196 ? 1.1862 1.2744 0.7372 0.0950 0.0014 0.0710 196 THR A CB 1575 O OG1 . THR A 196 ? 1.1721 1.2580 0.7408 0.0896 0.0069 0.0804 196 THR A OG1 1576 C CG2 . THR A 196 ? 1.2086 1.3201 0.7347 0.1108 -0.0015 0.0728 196 THR A CG2 1577 N N . TYR A 197 ? 1.1513 1.2005 0.7301 0.0745 0.0007 0.0563 197 TYR A N 1578 C CA . TYR A 197 ? 1.1305 1.1622 0.7278 0.0607 -0.0027 0.0498 197 TYR A CA 1579 C C . TYR A 197 ? 1.1352 1.1585 0.7232 0.0478 -0.0215 0.0345 197 TYR A C 1580 O O . TYR A 197 ? 1.1310 1.1615 0.6990 0.0496 -0.0309 0.0270 197 TYR A O 1581 C CB . TYR A 197 ? 1.1421 1.1675 0.7452 0.0665 0.0046 0.0483 197 TYR A CB 1582 C CG . TYR A 197 ? 1.1750 1.1998 0.7564 0.0726 -0.0040 0.0366 197 TYR A CG 1583 C CD1 . TYR A 197 ? 1.2071 1.2450 0.7687 0.0880 0.0010 0.0397 197 TYR A CD1 1584 C CD2 . TYR A 197 ? 1.1781 1.1876 0.7571 0.0639 -0.0172 0.0225 197 TYR A CD2 1585 C CE1 . TYR A 197 ? 1.2195 1.2561 0.7606 0.0936 -0.0066 0.0275 197 TYR A CE1 1586 C CE2 . TYR A 197 ? 1.2045 1.2103 0.7630 0.0698 -0.0244 0.0111 197 TYR A CE2 1587 C CZ . TYR A 197 ? 1.2248 1.2445 0.7648 0.0842 -0.0192 0.0130 197 TYR A CZ 1588 O OH . TYR A 197 ? 1.2335 1.2489 0.7524 0.0901 -0.0262 0.0003 197 TYR A OH 1589 N N . ILE A 198 ? 1.1316 1.1395 0.7338 0.0347 -0.0264 0.0297 198 ILE A N 1590 C CA . ILE A 198 ? 1.1296 1.1239 0.7228 0.0226 -0.0421 0.0160 198 ILE A CA 1591 C C . ILE A 198 ? 1.1230 1.0999 0.7264 0.0191 -0.0434 0.0113 198 ILE A C 1592 O O . ILE A 198 ? 1.1518 1.1244 0.7748 0.0136 -0.0392 0.0156 198 ILE A O 1593 C CB . ILE A 198 ? 1.1263 1.1199 0.7242 0.0087 -0.0486 0.0154 198 ILE A CB 1594 C CG1 . ILE A 198 ? 1.1352 1.1497 0.7253 0.0127 -0.0481 0.0199 198 ILE A CG1 1595 C CG2 . ILE A 198 ? 1.1400 1.1166 0.7276 -0.0042 -0.0629 0.0021 198 ILE A CG2 1596 C CD1 . ILE A 198 ? 1.1239 1.1426 0.7263 0.0038 -0.0474 0.0250 198 ILE A CD1 1597 N N . SER A 199 ? 1.1168 1.0842 0.7069 0.0232 -0.0494 0.0017 199 SER A N 1598 C CA . SER A 199 ? 1.1163 1.0682 0.7144 0.0221 -0.0520 -0.0033 199 SER A CA 1599 C C . SER A 199 ? 1.1029 1.0340 0.6894 0.0104 -0.0664 -0.0136 199 SER A C 1600 O O . SER A 199 ? 1.1101 1.0357 0.6764 0.0076 -0.0742 -0.0214 199 SER A O 1601 C CB . SER A 199 ? 1.1434 1.0968 0.7356 0.0363 -0.0475 -0.0062 199 SER A CB 1602 O OG . SER A 199 ? 1.1964 1.1462 0.7631 0.0399 -0.0547 -0.0152 199 SER A OG 1603 N N . VAL A 200 ? 1.1108 1.0302 0.7096 0.0034 -0.0694 -0.0138 200 VAL A N 1604 C CA . VAL A 200 ? 1.1126 1.0096 0.7000 -0.0070 -0.0815 -0.0215 200 VAL A CA 1605 C C . VAL A 200 ? 1.1272 1.0102 0.7190 -0.0017 -0.0846 -0.0251 200 VAL A C 1606 O O . VAL A 200 ? 1.1336 1.0254 0.7465 0.0011 -0.0793 -0.0205 200 VAL A O 1607 C CB . VAL A 200 ? 1.1048 1.0011 0.7002 -0.0209 -0.0835 -0.0178 200 VAL A CB 1608 C CG1 . VAL A 200 ? 1.1253 0.9990 0.7034 -0.0325 -0.0946 -0.0253 200 VAL A CG1 1609 C CG2 . VAL A 200 ? 1.1070 1.0239 0.7063 -0.0226 -0.0774 -0.0113 200 VAL A CG2 1610 N N . GLY A 201 ? 1.1613 1.0229 0.7337 -0.0003 -0.0931 -0.0338 201 GLY A N 1611 C CA . GLY A 201 ? 1.1879 1.0352 0.7614 0.0070 -0.0971 -0.0375 201 GLY A CA 1612 C C . GLY A 201 ? 1.2125 1.0293 0.7672 -0.0002 -0.1080 -0.0431 201 GLY A C 1613 O O . GLY A 201 ? 1.2346 1.0371 0.7696 -0.0081 -0.1123 -0.0480 201 GLY A O 1614 N N . THR A 202 ? 1.2164 1.0239 0.7774 0.0022 -0.1122 -0.0425 202 THR A N 1615 C CA . THR A 202 ? 1.2539 1.0292 0.7948 0.0003 -0.1218 -0.0469 202 THR A CA 1616 C C . THR A 202 ? 1.2728 1.0452 0.8200 0.0156 -0.1245 -0.0482 202 THR A C 1617 O O . THR A 202 ? 1.2679 1.0624 0.8329 0.0268 -0.1187 -0.0477 202 THR A O 1618 C CB . THR A 202 ? 1.2564 1.0217 0.7949 -0.0147 -0.1259 -0.0433 202 THR A CB 1619 O OG1 . THR A 202 ? 1.2402 1.0196 0.7994 -0.0128 -0.1256 -0.0388 202 THR A OG1 1620 C CG2 . THR A 202 ? 1.2465 1.0230 0.7856 -0.0289 -0.1222 -0.0413 202 THR A CG2 1621 N N . SER A 203 ? 1.3050 1.0508 0.8374 0.0164 -0.1329 -0.0496 203 SER A N 1622 C CA . SER A 203 ? 1.3075 1.0529 0.8469 0.0309 -0.1374 -0.0501 203 SER A CA 1623 C C . SER A 203 ? 1.2414 1.0209 0.8133 0.0317 -0.1336 -0.0465 203 SER A C 1624 O O . SER A 203 ? 1.2162 1.0137 0.8054 0.0448 -0.1318 -0.0482 203 SER A O 1625 C CB . SER A 203 ? 1.3464 1.0610 0.8658 0.0287 -0.1467 -0.0493 203 SER A CB 1626 O OG . SER A 203 ? 1.4241 1.1036 0.9135 0.0244 -0.1488 -0.0524 203 SER A OG 1627 N N . THR A 204 ? 1.2087 0.9968 0.7892 0.0170 -0.1320 -0.0421 204 THR A N 1628 C CA . THR A 204 ? 1.1783 0.9942 0.7882 0.0150 -0.1287 -0.0396 204 THR A CA 1629 C C . THR A 204 ? 1.1635 1.0038 0.7922 0.0089 -0.1168 -0.0358 204 THR A C 1630 O O . THR A 204 ? 1.1873 1.0525 0.8420 0.0135 -0.1098 -0.0351 204 THR A O 1631 C CB . THR A 204 ? 1.1567 0.9641 0.7630 0.0043 -0.1350 -0.0376 204 THR A CB 1632 O OG1 . THR A 204 ? 1.1460 0.9464 0.7427 -0.0110 -0.1319 -0.0342 204 THR A OG1 1633 C CG2 . THR A 204 ? 1.1667 0.9459 0.7492 0.0111 -0.1462 -0.0395 204 THR A CG2 1634 N N . LEU A 205 ? 1.1566 0.9902 0.7724 -0.0011 -0.1142 -0.0334 205 LEU A N 1635 C CA . LEU A 205 ? 1.1376 0.9927 0.7685 -0.0066 -0.1035 -0.0284 205 LEU A CA 1636 C C . LEU A 205 ? 1.1349 1.0064 0.7737 0.0045 -0.0943 -0.0278 205 LEU A C 1637 O O . LEU A 205 ? 1.1348 0.9966 0.7571 0.0127 -0.0963 -0.0319 205 LEU A O 1638 C CB . LEU A 205 ? 1.1445 0.9905 0.7588 -0.0189 -0.1043 -0.0267 205 LEU A CB 1639 C CG . LEU A 205 ? 1.1399 1.0066 0.7678 -0.0248 -0.0946 -0.0204 205 LEU A CG 1640 C CD1 . LEU A 205 ? 1.1238 1.0037 0.7761 -0.0289 -0.0899 -0.0166 205 LEU A CD1 1641 C CD2 . LEU A 205 ? 1.1446 1.0037 0.7560 -0.0363 -0.0975 -0.0203 205 LEU A CD2 1642 N N . ASN A 206 ? 1.1058 1.0006 0.7692 0.0047 -0.0833 -0.0227 206 ASN A N 1643 C CA . ASN A 206 ? 1.0950 1.0065 0.7660 0.0142 -0.0718 -0.0198 206 ASN A CA 1644 C C . ASN A 206 ? 1.0630 0.9902 0.7469 0.0086 -0.0598 -0.0112 206 ASN A C 1645 O O . ASN A 206 ? 1.0377 0.9807 0.7463 0.0093 -0.0494 -0.0072 206 ASN A O 1646 C CB . ASN A 206 ? 1.0994 1.0238 0.7908 0.0247 -0.0680 -0.0224 206 ASN A CB 1647 C CG . ASN A 206 ? 1.1181 1.0594 0.8169 0.0349 -0.0545 -0.0190 206 ASN A CG 1648 O OD1 . ASN A 206 ? 1.1566 1.0952 0.8370 0.0384 -0.0516 -0.0172 206 ASN A OD1 1649 N ND2 . ASN A 206 ? 1.1095 1.0697 0.8354 0.0395 -0.0458 -0.0186 206 ASN A ND2 1650 N N . GLN A 207 ? 1.0602 0.9829 0.7273 0.0033 -0.0610 -0.0087 207 GLN A N 1651 C CA . GLN A 207 ? 1.0727 1.0078 0.7485 -0.0012 -0.0513 -0.0001 207 GLN A CA 1652 C C . GLN A 207 ? 1.0808 1.0279 0.7489 0.0083 -0.0420 0.0051 207 GLN A C 1653 O O . GLN A 207 ? 1.0708 1.0140 0.7198 0.0149 -0.0463 0.0004 207 GLN A O 1654 C CB . GLN A 207 ? 1.0904 1.0162 0.7547 -0.0134 -0.0592 -0.0006 207 GLN A CB 1655 C CG . GLN A 207 ? 1.0922 1.0298 0.7635 -0.0174 -0.0507 0.0077 207 GLN A CG 1656 C CD . GLN A 207 ? 1.1047 1.0350 0.7663 -0.0294 -0.0586 0.0060 207 GLN A CD 1657 O OE1 . GLN A 207 ? 1.1203 1.0525 0.7660 -0.0309 -0.0620 0.0053 207 GLN A OE1 1658 N NE2 . GLN A 207 ? 1.1037 1.0268 0.7747 -0.0382 -0.0617 0.0045 207 GLN A NE2 1659 N N . ARG A 208 ? 1.0919 1.0523 0.7737 0.0094 -0.0288 0.0148 208 ARG A N 1660 C CA . ARG A 208 ? 1.1317 1.1041 0.8050 0.0196 -0.0187 0.0221 208 ARG A CA 1661 C C . ARG A 208 ? 1.1242 1.1045 0.8063 0.0168 -0.0089 0.0330 208 ARG A C 1662 O O . ARG A 208 ? 1.1191 1.1053 0.8204 0.0190 0.0053 0.0410 208 ARG A O 1663 C CB . ARG A 208 ? 1.1689 1.1498 0.8521 0.0310 -0.0072 0.0244 208 ARG A CB 1664 C CG . ARG A 208 ? 1.1926 1.1857 0.8656 0.0435 0.0049 0.0331 208 ARG A CG 1665 C CD . ARG A 208 ? 1.2253 1.2180 0.8748 0.0536 -0.0008 0.0259 208 ARG A CD 1666 N NE . ARG A 208 ? 1.2635 1.2693 0.9030 0.0671 0.0118 0.0343 208 ARG A NE 1667 C CZ . ARG A 208 ? 1.3107 1.3194 0.9284 0.0782 0.0097 0.0295 208 ARG A CZ 1668 N NH1 . ARG A 208 ? 1.3231 1.3206 0.9273 0.0771 -0.0040 0.0159 208 ARG A NH1 1669 N NH2 . ARG A 208 ? 1.3315 1.3530 0.9392 0.0911 0.0221 0.0383 208 ARG A NH2 1670 N N . LEU A 209 ? 1.1256 1.1058 0.7941 0.0121 -0.0160 0.0330 209 LEU A N 1671 C CA . LEU A 209 ? 1.1164 1.1033 0.7917 0.0102 -0.0083 0.0426 209 LEU A CA 1672 C C . LEU A 209 ? 1.1284 1.1289 0.7946 0.0241 0.0026 0.0529 209 LEU A C 1673 O O . LEU A 209 ? 1.1250 1.1311 0.7718 0.0322 -0.0017 0.0498 209 LEU A O 1674 C CB . LEU A 209 ? 1.1271 1.1114 0.7924 0.0001 -0.0204 0.0380 209 LEU A CB 1675 C CG . LEU A 209 ? 1.1407 1.1101 0.8086 -0.0132 -0.0323 0.0283 209 LEU A CG 1676 C CD1 . LEU A 209 ? 1.1488 1.1175 0.8054 -0.0228 -0.0418 0.0248 209 LEU A CD1 1677 C CD2 . LEU A 209 ? 1.1321 1.0966 0.8233 -0.0186 -0.0261 0.0303 209 LEU A CD2 1678 N N . VAL A 210 ? 1.1345 1.1390 0.8134 0.0274 0.0170 0.0650 210 VAL A N 1679 C CA . VAL A 210 ? 1.1630 1.1790 0.8317 0.0420 0.0286 0.0773 210 VAL A CA 1680 C C . VAL A 210 ? 1.1590 1.1776 0.8322 0.0415 0.0341 0.0867 210 VAL A C 1681 O O . VAL A 210 ? 1.1376 1.1470 0.8299 0.0321 0.0384 0.0876 210 VAL A O 1682 C CB . VAL A 210 ? 1.1848 1.2012 0.8630 0.0515 0.0468 0.0860 210 VAL A CB 1683 C CG1 . VAL A 210 ? 1.1928 1.2102 0.8633 0.0555 0.0418 0.0772 210 VAL A CG1 1684 C CG2 . VAL A 210 ? 1.1854 1.1925 0.8926 0.0426 0.0584 0.0892 210 VAL A CG2 1685 N N . PRO A 211 ? 1.1688 1.2009 0.8242 0.0524 0.0335 0.0929 211 PRO A N 1686 C CA . PRO A 211 ? 1.1726 1.2087 0.8315 0.0539 0.0377 0.1014 211 PRO A CA 1687 C C . PRO A 211 ? 1.1740 1.2021 0.8472 0.0604 0.0590 0.1166 211 PRO A C 1688 O O . PRO A 211 ? 1.1882 1.2175 0.8568 0.0729 0.0724 0.1266 211 PRO A O 1689 C CB . PRO A 211 ? 1.1809 1.2371 0.8162 0.0667 0.0314 0.1038 211 PRO A CB 1690 C CG . PRO A 211 ? 1.1877 1.2478 0.8077 0.0661 0.0194 0.0917 211 PRO A CG 1691 C CD . PRO A 211 ? 1.1854 1.2311 0.8163 0.0637 0.0270 0.0904 211 PRO A CD 1692 N N . ARG A 212 ? 1.1630 1.1818 0.8531 0.0514 0.0627 0.1179 212 ARG A N 1693 C CA . ARG A 212 ? 1.1849 1.1930 0.8889 0.0560 0.0830 0.1313 212 ARG A CA 1694 C C . ARG A 212 ? 1.1856 1.2014 0.8791 0.0684 0.0871 0.1428 212 ARG A C 1695 O O . ARG A 212 ? 1.1780 1.1988 0.8716 0.0628 0.0769 0.1377 212 ARG A O 1696 C CB . ARG A 212 ? 1.1806 1.1731 0.9092 0.0391 0.0848 0.1243 212 ARG A CB 1697 C CG . ARG A 212 ? 1.1893 1.1753 0.9321 0.0297 0.0849 0.1155 212 ARG A CG 1698 C CD . ARG A 212 ? 1.1847 1.1663 0.9365 0.0129 0.0690 0.0998 212 ARG A CD 1699 N NE . ARG A 212 ? 1.1942 1.1682 0.9567 0.0047 0.0703 0.0992 212 ARG A NE 1700 C CZ . ARG A 212 ? 1.2303 1.2024 0.9932 -0.0072 0.0559 0.0881 212 ARG A CZ 1701 N NH1 . ARG A 212 ? 1.2265 1.2018 0.9795 -0.0128 0.0391 0.0772 212 ARG A NH1 1702 N NH2 . ARG A 212 ? 1.2622 1.2278 1.0342 -0.0133 0.0591 0.0882 212 ARG A NH2 1703 N N . ILE A 213 ? 1.2024 1.2198 0.8862 0.0861 0.1024 0.1586 213 ILE A N 1704 C CA . ILE A 213 ? 1.2046 1.2293 0.8772 0.1017 0.1079 0.1718 213 ILE A CA 1705 C C . ILE A 213 ? 1.2049 1.2089 0.8950 0.1008 0.1265 0.1820 213 ILE A C 1706 O O . ILE A 213 ? 1.2054 1.1909 0.9097 0.0969 0.1431 0.1868 213 ILE A O 1707 C CB . ILE A 213 ? 1.2215 1.2580 0.8706 0.1240 0.1150 0.1848 213 ILE A CB 1708 C CG1 . ILE A 213 ? 1.2275 1.2858 0.8577 0.1249 0.0950 0.1725 213 ILE A CG1 1709 C CG2 . ILE A 213 ? 1.2323 1.2748 0.8702 0.1429 0.1229 0.2007 213 ILE A CG2 1710 C CD1 . ILE A 213 ? 1.2549 1.3238 0.8622 0.1442 0.1010 0.1816 213 ILE A CD1 1711 N N . ALA A 214 ? 1.1938 1.2015 0.8836 0.1038 0.1236 0.1843 214 ALA A N 1712 C CA . ALA A 214 ? 1.1993 1.1873 0.9023 0.1057 0.1410 0.1944 214 ALA A CA 1713 C C . ALA A 214 ? 1.2023 1.2034 0.8967 0.1167 0.1357 0.1988 214 ALA A C 1714 O O . ALA A 214 ? 1.1702 1.1935 0.8579 0.1131 0.1161 0.1881 214 ALA A O 1715 C CB . ALA A 214 ? 1.1841 1.1536 0.9124 0.0833 0.1417 0.1820 214 ALA A CB 1716 N N . THR A 215 ? 1.2304 1.2179 0.9256 0.1302 0.1537 0.2144 215 THR A N 1717 C CA . THR A 215 ? 1.2379 1.2384 0.9260 0.1432 0.1501 0.2196 215 THR A CA 1718 C C . THR A 215 ? 1.1991 1.1883 0.9070 0.1267 0.1480 0.2088 215 THR A C 1719 O O . THR A 215 ? 1.2021 1.1631 0.9262 0.1183 0.1630 0.2101 215 THR A O 1720 C CB . THR A 215 ? 1.2862 1.2771 0.9626 0.1690 0.1704 0.2426 215 THR A CB 1721 O OG1 . THR A 215 ? 1.3144 1.2698 1.0073 0.1640 0.1921 0.2492 215 THR A OG1 1722 C CG2 . THR A 215 ? 1.3061 1.3026 0.9626 0.1843 0.1763 0.2543 215 THR A CG2 1723 N N . ARG A 216 ? 1.1632 1.1753 0.8697 0.1216 0.1295 0.1976 216 ARG A N 1724 C CA . ARG A 216 ? 1.1348 1.1401 0.8578 0.1035 0.1240 0.1845 216 ARG A CA 1725 C C . ARG A 216 ? 1.1297 1.1515 0.8505 0.1135 0.1205 0.1865 216 ARG A C 1726 O O . ARG A 216 ? 1.0959 1.1448 0.8025 0.1296 0.1134 0.1919 216 ARG A O 1727 C CB . ARG A 216 ? 1.1038 1.1199 0.8290 0.0827 0.1040 0.1657 216 ARG A CB 1728 C CG . ARG A 216 ? 1.1027 1.1058 0.8309 0.0729 0.1052 0.1617 216 ARG A CG 1729 C CD . ARG A 216 ? 1.0828 1.0999 0.8065 0.0584 0.0844 0.1457 216 ARG A CD 1730 N NE . ARG A 216 ? 1.0895 1.1297 0.7941 0.0696 0.0749 0.1475 216 ARG A NE 1731 C CZ . ARG A 216 ? 1.0851 1.1256 0.7814 0.0720 0.0740 0.1476 216 ARG A CZ 1732 N NH1 . ARG A 216 ? 1.0856 1.1063 0.7923 0.0643 0.0823 0.1466 216 ARG A NH1 1733 N NH2 . ARG A 216 ? 1.0932 1.1558 0.7709 0.0823 0.0646 0.1478 216 ARG A NH2 1734 N N . SER A 217 ? 1.1426 1.1498 0.8779 0.1038 0.1250 0.1810 217 SER A N 1735 C CA . SER A 217 ? 1.1564 1.1796 0.8926 0.1108 0.1215 0.1804 217 SER A CA 1736 C C . SER A 217 ? 1.1406 1.1990 0.8711 0.1034 0.0990 0.1681 217 SER A C 1737 O O . SER A 217 ? 1.1305 1.1905 0.8620 0.0848 0.0866 0.1551 217 SER A O 1738 C CB . SER A 217 ? 1.1571 1.1573 0.9099 0.0976 0.1288 0.1730 217 SER A CB 1739 O OG . SER A 217 ? 1.1851 1.1504 0.9455 0.1000 0.1494 0.1814 217 SER A OG 1740 N N . LYS A 218 ? 1.1515 1.2383 0.8763 0.1184 0.0942 0.1720 218 LYS A N 1741 C CA . LYS A 218 ? 1.1394 1.2610 0.8619 0.1100 0.0743 0.1591 218 LYS A CA 1742 C C . LYS A 218 ? 1.1190 1.2330 0.8547 0.0870 0.0693 0.1444 218 LYS A C 1743 O O . LYS A 218 ? 1.1138 1.2104 0.8595 0.0867 0.0802 0.1459 218 LYS A O 1744 C CB . LYS A 218 ? 1.1668 1.3235 0.8839 0.1311 0.0712 0.1657 218 LYS A CB 1745 C CG . LYS A 218 ? 1.2036 1.3796 0.9033 0.1523 0.0690 0.1763 218 LYS A CG 1746 C CD . LYS A 218 ? 1.2263 1.4403 0.9217 0.1744 0.0648 0.1820 218 LYS A CD 1747 C CE . LYS A 218 ? 1.2576 1.4932 0.9334 0.1968 0.0615 0.1920 218 LYS A CE 1748 N NZ . LYS A 218 ? 1.2895 1.4931 0.9549 0.2144 0.0807 0.2115 218 LYS A NZ 1749 N N . VAL A 219 ? 1.0962 1.2210 0.8304 0.0681 0.0534 0.1302 219 VAL A N 1750 C CA . VAL A 219 ? 1.0795 1.2015 0.8223 0.0470 0.0468 0.1163 219 VAL A CA 1751 C C . VAL A 219 ? 1.0685 1.2246 0.8064 0.0399 0.0298 0.1063 219 VAL A C 1752 O O . VAL A 219 ? 1.0518 1.2149 0.7806 0.0352 0.0196 0.1018 219 VAL A O 1753 C CB . VAL A 219 ? 1.0787 1.1702 0.8244 0.0278 0.0461 0.1085 219 VAL A CB 1754 C CG1 . VAL A 219 ? 1.0642 1.1545 0.8144 0.0067 0.0375 0.0944 219 VAL A CG1 1755 C CG2 . VAL A 219 ? 1.0892 1.1490 0.8427 0.0330 0.0634 0.1166 219 VAL A CG2 1756 N N . ASN A 220 ? 1.0766 1.2541 0.8214 0.0389 0.0276 0.1022 220 ASN A N 1757 C CA . ASN A 220 ? 1.0869 1.3026 0.8300 0.0346 0.0137 0.0936 220 ASN A CA 1758 C C . ASN A 220 ? 1.0879 1.3307 0.8214 0.0540 0.0091 0.1004 220 ASN A C 1759 O O . ASN A 220 ? 1.0932 1.3570 0.8202 0.0473 -0.0041 0.0918 220 ASN A O 1760 C CB . ASN A 220 ? 1.0940 1.3042 0.8340 0.0087 0.0013 0.0789 220 ASN A CB 1761 C CG . ASN A 220 ? 1.1053 1.2937 0.8523 -0.0094 0.0043 0.0718 220 ASN A CG 1762 O OD1 . ASN A 220 ? 1.1268 1.3008 0.8813 -0.0041 0.0159 0.0768 220 ASN A OD1 1763 N ND2 . ASN A 220 ? 1.0982 1.2830 0.8415 -0.0307 -0.0056 0.0599 220 ASN A ND2 1764 N N . GLY A 221 ? 1.0831 1.3238 0.8147 0.0783 0.0208 0.1157 221 GLY A N 1765 C CA . GLY A 221 ? 1.0817 1.3492 0.8022 0.1010 0.0179 0.1243 221 GLY A CA 1766 C C . GLY A 221 ? 1.0700 1.3271 0.7760 0.1032 0.0150 0.1268 221 GLY A C 1767 O O . GLY A 221 ? 1.0628 1.3455 0.7571 0.1194 0.0096 0.1309 221 GLY A O 1768 N N . GLN A 222 ? 1.0430 1.2644 0.7492 0.0880 0.0187 0.1241 222 GLN A N 1769 C CA . GLN A 222 ? 1.0468 1.2573 0.7403 0.0888 0.0166 0.1254 222 GLN A CA 1770 C C . GLN A 222 ? 1.0622 1.2317 0.7586 0.0880 0.0316 0.1338 222 GLN A C 1771 O O . GLN A 222 ? 1.0644 1.2098 0.7727 0.0735 0.0366 0.1295 222 GLN A O 1772 C CB . GLN A 222 ? 1.0304 1.2471 0.7208 0.0669 0.0003 0.1080 222 GLN A CB 1773 C CG . GLN A 222 ? 1.0337 1.2924 0.7201 0.0670 -0.0148 0.0984 222 GLN A CG 1774 C CD . GLN A 222 ? 1.0462 1.3311 0.7189 0.0917 -0.0162 0.1071 222 GLN A CD 1775 O OE1 . GLN A 222 ? 1.0411 1.3123 0.7015 0.1020 -0.0113 0.1149 222 GLN A OE1 1776 N NE2 . GLN A 222 ? 1.0549 1.3796 0.7296 0.1019 -0.0228 0.1057 222 GLN A NE2 1777 N N . SER A 223 ? 1.0911 1.2542 0.7762 0.1035 0.0389 0.1451 223 SER A N 1778 C CA . SER A 223 ? 1.1086 1.2358 0.7971 0.1037 0.0546 0.1537 223 SER A CA 1779 C C . SER A 223 ? 1.1098 1.2251 0.7949 0.0896 0.0485 0.1450 223 SER A C 1780 O O . SER A 223 ? 1.1134 1.2005 0.8068 0.0818 0.0581 0.1461 223 SER A O 1781 C CB . SER A 223 ? 1.1318 1.2562 0.8105 0.1301 0.0700 0.1735 223 SER A CB 1782 O OG . SER A 223 ? 1.1532 1.2814 0.8365 0.1437 0.0783 0.1825 223 SER A OG 1783 N N . GLY A 224 ? 1.1017 1.2392 0.7752 0.0864 0.0326 0.1354 224 GLY A N 1784 C CA . GLY A 224 ? 1.0905 1.2175 0.7603 0.0724 0.0248 0.1250 224 GLY A CA 1785 C C . GLY A 224 ? 1.0651 1.1735 0.7482 0.0490 0.0203 0.1127 224 GLY A C 1786 O O . GLY A 224 ? 1.0666 1.1746 0.7602 0.0425 0.0209 0.1106 224 GLY A O 1787 N N . ARG A 225 ? 1.0601 1.1533 0.7421 0.0375 0.0159 0.1050 225 ARG A N 1788 C CA . ARG A 225 ? 1.0522 1.1273 0.7441 0.0168 0.0106 0.0936 225 ARG A CA 1789 C C . ARG A 225 ? 1.0432 1.1172 0.7255 0.0053 -0.0034 0.0808 225 ARG A C 1790 O O . ARG A 225 ? 1.0578 1.1377 0.7285 0.0130 -0.0059 0.0811 225 ARG A O 1791 C CB . ARG A 225 ? 1.0487 1.0974 0.7542 0.0144 0.0240 0.0983 225 ARG A CB 1792 C CG . ARG A 225 ? 1.0513 1.0933 0.7679 0.0224 0.0393 0.1092 225 ARG A CG 1793 C CD . ARG A 225 ? 1.0341 1.0741 0.7598 0.0109 0.0362 0.1024 225 ARG A CD 1794 N NE . ARG A 225 ? 1.0370 1.0688 0.7726 0.0196 0.0516 0.1122 225 ARG A NE 1795 C CZ . ARG A 225 ? 1.0356 1.0826 0.7679 0.0341 0.0559 0.1207 225 ARG A CZ 1796 N NH1 . ARG A 225 ? 1.0375 1.1127 0.7582 0.0411 0.0452 0.1201 225 ARG A NH1 1797 N NH2 . ARG A 225 ? 1.0385 1.0726 0.7796 0.0420 0.0710 0.1294 225 ARG A NH2 1798 N N . MET A 226 ? 1.0407 1.1059 0.7267 -0.0124 -0.0121 0.0697 226 MET A N 1799 C CA . MET A 226 ? 1.0585 1.1153 0.7358 -0.0240 -0.0239 0.0581 226 MET A CA 1800 C C . MET A 226 ? 1.0510 1.0827 0.7377 -0.0348 -0.0221 0.0546 226 MET A C 1801 O O . MET A 226 ? 1.0786 1.1032 0.7766 -0.0403 -0.0173 0.0557 226 MET A O 1802 C CB . MET A 226 ? 1.0858 1.1549 0.7562 -0.0357 -0.0367 0.0476 226 MET A CB 1803 C CG . MET A 226 ? 1.1216 1.2200 0.7832 -0.0265 -0.0412 0.0479 226 MET A CG 1804 S SD . MET A 226 ? 1.1468 1.2496 0.7904 -0.0207 -0.0490 0.0421 226 MET A SD 1805 C CE . MET A 226 ? 1.1664 1.3086 0.8032 -0.0138 -0.0563 0.0394 226 MET A CE 1806 N N . GLU A 227 ? 1.0222 1.0417 0.7041 -0.0368 -0.0261 0.0498 227 GLU A N 1807 C CA . GLU A 227 ? 0.9985 0.9974 0.6888 -0.0456 -0.0262 0.0454 227 GLU A CA 1808 C C . GLU A 227 ? 0.9988 0.9885 0.6764 -0.0552 -0.0397 0.0345 227 GLU A C 1809 O O . GLU A 227 ? 1.0120 1.0018 0.6796 -0.0501 -0.0436 0.0319 227 GLU A O 1810 C CB . GLU A 227 ? 1.0012 0.9938 0.7014 -0.0366 -0.0155 0.0515 227 GLU A CB 1811 C CG . GLU A 227 ? 0.9995 0.9759 0.7140 -0.0448 -0.0135 0.0476 227 GLU A CG 1812 C CD . GLU A 227 ? 1.0098 0.9833 0.7387 -0.0372 -0.0003 0.0537 227 GLU A CD 1813 O OE1 . GLU A 227 ? 1.0053 0.9864 0.7295 -0.0254 0.0061 0.0607 227 GLU A OE1 1814 O OE2 . GLU A 227 ? 1.0024 0.9666 0.7475 -0.0434 0.0040 0.0512 227 GLU A OE2 1815 N N . PHE A 228 ? 0.9828 0.9630 0.6595 -0.0684 -0.0461 0.0282 228 PHE A N 1816 C CA . PHE A 228 ? 0.9936 0.9623 0.6559 -0.0780 -0.0580 0.0188 228 PHE A CA 1817 C C . PHE A 228 ? 0.9789 0.9271 0.6425 -0.0808 -0.0610 0.0149 228 PHE A C 1818 O O . PHE A 228 ? 0.9519 0.8940 0.6272 -0.0836 -0.0573 0.0160 228 PHE A O 1819 C CB . PHE A 228 ? 1.0140 0.9849 0.6714 -0.0905 -0.0629 0.0147 228 PHE A CB 1820 C CG . PHE A 228 ? 1.0160 1.0107 0.6714 -0.0880 -0.0626 0.0161 228 PHE A CG 1821 C CD1 . PHE A 228 ? 1.0176 1.0188 0.6597 -0.0900 -0.0705 0.0096 228 PHE A CD1 1822 C CD2 . PHE A 228 ? 1.0048 1.0160 0.6716 -0.0824 -0.0545 0.0233 228 PHE A CD2 1823 C CE1 . PHE A 228 ? 1.0119 1.0391 0.6531 -0.0873 -0.0714 0.0094 228 PHE A CE1 1824 C CE2 . PHE A 228 ? 0.9986 1.0350 0.6640 -0.0780 -0.0551 0.0245 228 PHE A CE2 1825 C CZ . PHE A 228 ? 1.0044 1.0505 0.6574 -0.0806 -0.0640 0.0172 228 PHE A CZ 1826 N N . PHE A 229 ? 0.9739 0.9129 0.6254 -0.0792 -0.0679 0.0097 229 PHE A N 1827 C CA . PHE A 229 ? 0.9681 0.8894 0.6188 -0.0793 -0.0722 0.0056 229 PHE A CA 1828 C C . PHE A 229 ? 0.9776 0.8810 0.6094 -0.0883 -0.0831 -0.0018 229 PHE A C 1829 O O . PHE A 229 ? 0.9862 0.8918 0.6062 -0.0943 -0.0867 -0.0047 229 PHE A O 1830 C CB . PHE A 229 ? 0.9628 0.8871 0.6162 -0.0669 -0.0691 0.0067 229 PHE A CB 1831 C CG . PHE A 229 ? 0.9668 0.9045 0.6390 -0.0586 -0.0565 0.0147 229 PHE A CG 1832 C CD1 . PHE A 229 ? 0.9749 0.9286 0.6480 -0.0525 -0.0491 0.0216 229 PHE A CD1 1833 C CD2 . PHE A 229 ? 0.9766 0.9110 0.6657 -0.0571 -0.0518 0.0152 229 PHE A CD2 1834 C CE1 . PHE A 229 ? 0.9846 0.9469 0.6734 -0.0445 -0.0358 0.0303 229 PHE A CE1 1835 C CE2 . PHE A 229 ? 0.9862 0.9306 0.6934 -0.0512 -0.0385 0.0223 229 PHE A CE2 1836 C CZ . PHE A 229 ? 0.9809 0.9373 0.6871 -0.0447 -0.0298 0.0307 229 PHE A CZ 1837 N N . TRP A 230 ? 0.9683 0.8542 0.5974 -0.0891 -0.0880 -0.0049 230 TRP A N 1838 C CA . TRP A 230 ? 0.9723 0.8364 0.5817 -0.0965 -0.0971 -0.0106 230 TRP A CA 1839 C C . TRP A 230 ? 0.9793 0.8267 0.5841 -0.0896 -0.1024 -0.0135 230 TRP A C 1840 O O . TRP A 230 ? 0.9704 0.8254 0.5907 -0.0815 -0.0995 -0.0120 230 TRP A O 1841 C CB . TRP A 230 ? 0.9788 0.8367 0.5853 -0.1088 -0.0981 -0.0102 230 TRP A CB 1842 C CG . TRP A 230 ? 0.9647 0.8230 0.5841 -0.1080 -0.0961 -0.0082 230 TRP A CG 1843 C CD1 . TRP A 230 ? 0.9472 0.8217 0.5851 -0.1078 -0.0883 -0.0044 230 TRP A CD1 1844 C CD2 . TRP A 230 ? 0.9562 0.7983 0.5704 -0.1070 -0.1021 -0.0107 230 TRP A CD2 1845 N NE1 . TRP A 230 ? 0.9441 0.8136 0.5894 -0.1082 -0.0892 -0.0057 230 TRP A NE1 1846 C CE2 . TRP A 230 ? 0.9706 0.8221 0.6016 -0.1073 -0.0982 -0.0096 230 TRP A CE2 1847 C CE3 . TRP A 230 ? 0.9683 0.7884 0.5645 -0.1050 -0.1105 -0.0139 230 TRP A CE3 1848 C CZ2 . TRP A 230 ? 0.9827 0.8257 0.6136 -0.1059 -0.1035 -0.0125 230 TRP A CZ2 1849 C CZ3 . TRP A 230 ? 0.9823 0.7933 0.5775 -0.1020 -0.1156 -0.0153 230 TRP A CZ3 1850 C CH2 . TRP A 230 ? 0.9827 0.8068 0.5955 -0.1026 -0.1126 -0.0151 230 TRP A CH2 1851 N N . THR A 231 ? 0.9916 0.8165 0.5756 -0.0928 -0.1098 -0.0180 231 THR A N 1852 C CA . THR A 231 ? 1.0060 0.8122 0.5822 -0.0856 -0.1159 -0.0206 231 THR A CA 1853 C C . THR A 231 ? 1.0425 0.8198 0.5944 -0.0938 -0.1224 -0.0230 231 THR A C 1854 O O . THR A 231 ? 1.0522 0.8247 0.5940 -0.1058 -0.1217 -0.0239 231 THR A O 1855 C CB . THR A 231 ? 1.0112 0.8184 0.5863 -0.0728 -0.1161 -0.0233 231 THR A CB 1856 O OG1 . THR A 231 ? 1.0225 0.8161 0.5943 -0.0634 -0.1215 -0.0254 231 THR A OG1 1857 C CG2 . THR A 231 ? 1.0294 0.8252 0.5850 -0.0763 -0.1184 -0.0280 231 THR A CG2 1858 N N . ILE A 232 ? 1.0709 0.8297 0.6139 -0.0873 -0.1283 -0.0237 232 ILE A N 1859 C CA . ILE A 232 ? 1.1201 0.8461 0.6366 -0.0916 -0.1338 -0.0250 232 ILE A CA 1860 C C . ILE A 232 ? 1.1535 0.8640 0.6588 -0.0799 -0.1374 -0.0290 232 ILE A C 1861 O O . ILE A 232 ? 1.1618 0.8773 0.6751 -0.0656 -0.1398 -0.0294 232 ILE A O 1862 C CB . ILE A 232 ? 1.1309 0.8451 0.6414 -0.0910 -0.1382 -0.0221 232 ILE A CB 1863 C CG1 . ILE A 232 ? 1.1322 0.8470 0.6397 -0.1065 -0.1349 -0.0192 232 ILE A CG1 1864 C CG2 . ILE A 232 ? 1.1706 0.8495 0.6541 -0.0856 -0.1446 -0.0226 232 ILE A CG2 1865 C CD1 . ILE A 232 ? 1.1168 0.8626 0.6474 -0.1124 -0.1279 -0.0183 232 ILE A CD1 1866 N N . LEU A 233 ? 1.1826 0.8755 0.6704 -0.0862 -0.1373 -0.0329 233 LEU A N 1867 C CA . LEU A 233 ? 1.1988 0.8748 0.6739 -0.0761 -0.1398 -0.0381 233 LEU A CA 1868 C C . LEU A 233 ? 1.2612 0.8970 0.7103 -0.0748 -0.1447 -0.0379 233 LEU A C 1869 O O . LEU A 233 ? 1.2876 0.9007 0.7192 -0.0887 -0.1440 -0.0380 233 LEU A O 1870 C CB . LEU A 233 ? 1.2030 0.8824 0.6732 -0.0844 -0.1369 -0.0440 233 LEU A CB 1871 C CG . LEU A 233 ? 1.2048 0.8724 0.6637 -0.0747 -0.1383 -0.0513 233 LEU A CG 1872 C CD1 . LEU A 233 ? 1.1754 0.8666 0.6515 -0.0569 -0.1366 -0.0504 233 LEU A CD1 1873 C CD2 . LEU A 233 ? 1.2020 0.8742 0.6550 -0.0866 -0.1364 -0.0583 233 LEU A CD2 1874 N N . LYS A 234 ? 1.3120 0.9397 0.7590 -0.0578 -0.1492 -0.0372 234 LYS A N 1875 C CA . LYS A 234 ? 1.3883 0.9780 0.8100 -0.0523 -0.1543 -0.0352 234 LYS A CA 1876 C C . LYS A 234 ? 1.4479 1.0006 0.8435 -0.0556 -0.1535 -0.0401 234 LYS A C 1877 O O . LYS A 234 ? 1.4451 1.0053 0.8440 -0.0595 -0.1504 -0.0467 234 LYS A O 1878 C CB . LYS A 234 ? 1.4131 1.0088 0.8416 -0.0309 -0.1598 -0.0342 234 LYS A CB 1879 C CG . LYS A 234 ? 1.4041 1.0238 0.8501 -0.0293 -0.1624 -0.0297 234 LYS A CG 1880 C CD . LYS A 234 ? 1.4309 1.0645 0.8891 -0.0087 -0.1679 -0.0309 234 LYS A CD 1881 C CE . LYS A 234 ? 1.4137 1.0834 0.8999 -0.0092 -0.1685 -0.0300 234 LYS A CE 1882 N NZ . LYS A 234 ? 1.4284 1.0898 0.9044 -0.0164 -0.1722 -0.0259 234 LYS A NZ 1883 N N . PRO A 235 ? 1.5090 1.0206 0.8774 -0.0542 -0.1559 -0.0372 235 PRO A N 1884 C CA . PRO A 235 ? 1.5421 1.0145 0.8855 -0.0583 -0.1539 -0.0426 235 PRO A CA 1885 C C . PRO A 235 ? 1.5570 1.0274 0.9003 -0.0409 -0.1555 -0.0495 235 PRO A C 1886 O O . PRO A 235 ? 1.5366 1.0191 0.8888 -0.0211 -0.1596 -0.0475 235 PRO A O 1887 C CB . PRO A 235 ? 1.5941 1.0224 0.9086 -0.0560 -0.1555 -0.0358 235 PRO A CB 1888 C CG . PRO A 235 ? 1.5742 1.0211 0.8983 -0.0435 -0.1609 -0.0281 235 PRO A CG 1889 C CD . PRO A 235 ? 1.5097 1.0076 0.8675 -0.0489 -0.1599 -0.0292 235 PRO A CD 1890 N N . ASN A 236 ? 1.5926 1.0502 0.9270 -0.0486 -0.1523 -0.0584 236 ASN A N 1891 C CA . ASN A 236 ? 1.6066 1.0556 0.9354 -0.0329 -0.1530 -0.0663 236 ASN A CA 1892 C C . ASN A 236 ? 1.5475 1.0434 0.9042 -0.0207 -0.1530 -0.0680 236 ASN A C 1893 O O . ASN A 236 ? 1.5567 1.0525 0.9132 -0.0026 -0.1539 -0.0721 236 ASN A O 1894 C CB . ASN A 236 ? 1.6687 1.0798 0.9764 -0.0140 -0.1566 -0.0628 236 ASN A CB 1895 C CG . ASN A 236 ? 1.7390 1.1172 1.0268 -0.0049 -0.1554 -0.0721 236 ASN A CG 1896 O OD1 . ASN A 236 ? 1.7526 1.1306 1.0385 -0.0158 -0.1520 -0.0821 236 ASN A OD1 1897 N ND2 . ASN A 236 ? 1.8072 1.1576 1.0795 0.0159 -0.1585 -0.0694 236 ASN A ND2 1898 N N . ASP A 237 ? 1.4831 1.0179 0.8632 -0.0305 -0.1511 -0.0645 237 ASP A N 1899 C CA . ASP A 237 ? 1.4256 1.0040 0.8323 -0.0212 -0.1491 -0.0645 237 ASP A CA 1900 C C . ASP A 237 ? 1.3898 0.9907 0.8041 -0.0346 -0.1448 -0.0691 237 ASP A C 1901 O O . ASP A 237 ? 1.3761 0.9708 0.7842 -0.0532 -0.1440 -0.0699 237 ASP A O 1902 C CB . ASP A 237 ? 1.4039 1.0091 0.8328 -0.0188 -0.1500 -0.0558 237 ASP A CB 1903 C CG . ASP A 237 ? 1.3710 1.0187 0.8285 -0.0099 -0.1461 -0.0550 237 ASP A CG 1904 O OD1 . ASP A 237 ? 1.3697 1.0236 0.8285 0.0020 -0.1441 -0.0599 237 ASP A OD1 1905 O OD2 . ASP A 237 ? 1.3358 1.0098 0.8141 -0.0148 -0.1443 -0.0494 237 ASP A OD2 1906 N N . ALA A 238 ? 1.3656 0.9943 0.7932 -0.0245 -0.1418 -0.0718 238 ALA A N 1907 C CA . ALA A 238 ? 1.3359 0.9880 0.7687 -0.0330 -0.1383 -0.0762 238 ALA A CA 1908 C C . ALA A 238 ? 1.2888 0.9835 0.7488 -0.0306 -0.1337 -0.0686 238 ALA A C 1909 O O . ALA A 238 ? 1.2712 0.9797 0.7469 -0.0179 -0.1320 -0.0634 238 ALA A O 1910 C CB . ALA A 238 ? 1.3488 0.9950 0.7694 -0.0230 -0.1376 -0.0862 238 ALA A CB 1911 N N . ILE A 239 ? 1.2738 0.9889 0.7397 -0.0429 -0.1313 -0.0684 239 ILE A N 1912 C CA . ILE A 239 ? 1.2399 0.9934 0.7287 -0.0400 -0.1255 -0.0614 239 ILE A CA 1913 C C . ILE A 239 ? 1.2579 1.0308 0.7439 -0.0346 -0.1224 -0.0662 239 ILE A C 1914 O O . ILE A 239 ? 1.2653 1.0312 0.7360 -0.0429 -0.1255 -0.0748 239 ILE A O 1915 C CB . ILE A 239 ? 1.2016 0.9671 0.7009 -0.0552 -0.1245 -0.0554 239 ILE A CB 1916 C CG1 . ILE A 239 ? 1.1681 0.9681 0.6914 -0.0498 -0.1175 -0.0469 239 ILE A CG1 1917 C CG2 . ILE A 239 ? 1.2060 0.9701 0.6936 -0.0704 -0.1265 -0.0617 239 ILE A CG2 1918 C CD1 . ILE A 239 ? 1.1392 0.9494 0.6747 -0.0616 -0.1159 -0.0404 239 ILE A CD1 1919 N N . ASN A 240 ? 1.2579 1.0553 0.7585 -0.0211 -0.1160 -0.0611 240 ASN A N 1920 C CA . ASN A 240 ? 1.2824 1.0980 0.7782 -0.0120 -0.1122 -0.0645 240 ASN A CA 1921 C C . ASN A 240 ? 1.2595 1.1091 0.7716 -0.0105 -0.1048 -0.0554 240 ASN A C 1922 O O . ASN A 240 ? 1.2534 1.1167 0.7848 -0.0037 -0.0978 -0.0461 240 ASN A O 1923 C CB . ASN A 240 ? 1.3122 1.1251 0.8075 0.0059 -0.1089 -0.0662 240 ASN A CB 1924 C CG . ASN A 240 ? 1.3748 1.1529 0.8529 0.0084 -0.1154 -0.0748 240 ASN A CG 1925 O OD1 . ASN A 240 ? 1.4093 1.1666 0.8666 0.0010 -0.1208 -0.0845 240 ASN A OD1 1926 N ND2 . ASN A 240 ? 1.3962 1.1680 0.8832 0.0191 -0.1148 -0.0717 240 ASN A ND2 1927 N N . PHE A 241 ? 1.2541 1.1177 0.7588 -0.0164 -0.1061 -0.0583 241 PHE A N 1928 C CA . PHE A 241 ? 1.2426 1.1378 0.7593 -0.0127 -0.0992 -0.0492 241 PHE A CA 1929 C C . PHE A 241 ? 1.2765 1.1886 0.7847 0.0024 -0.0944 -0.0503 241 PHE A C 1930 O O . PHE A 241 ? 1.3150 1.2174 0.8048 0.0061 -0.0988 -0.0614 241 PHE A O 1931 C CB . PHE A 241 ? 1.2354 1.1406 0.7506 -0.0268 -0.1036 -0.0507 241 PHE A CB 1932 C CG . PHE A 241 ? 1.2298 1.1239 0.7552 -0.0407 -0.1055 -0.0470 241 PHE A CG 1933 C CD1 . PHE A 241 ? 1.2030 1.1095 0.7485 -0.0397 -0.0988 -0.0351 241 PHE A CD1 1934 C CD2 . PHE A 241 ? 1.2483 1.1181 0.7624 -0.0549 -0.1133 -0.0553 241 PHE A CD2 1935 C CE1 . PHE A 241 ? 1.1997 1.0966 0.7532 -0.0518 -0.1006 -0.0325 241 PHE A CE1 1936 C CE2 . PHE A 241 ? 1.2302 1.0900 0.7517 -0.0669 -0.1143 -0.0513 241 PHE A CE2 1937 C CZ . PHE A 241 ? 1.2089 1.0832 0.7498 -0.0651 -0.1084 -0.0403 241 PHE A CZ 1938 N N . GLU A 242 ? 1.2840 1.2201 0.8048 0.0116 -0.0846 -0.0385 242 GLU A N 1939 C CA . GLU A 242 ? 1.3121 1.2678 0.8236 0.0265 -0.0786 -0.0370 242 GLU A CA 1940 C C . GLU A 242 ? 1.2850 1.2652 0.8099 0.0316 -0.0687 -0.0222 242 GLU A C 1941 O O . GLU A 242 ? 1.2835 1.2630 0.8287 0.0308 -0.0609 -0.0119 242 GLU A O 1942 C CB . GLU A 242 ? 1.3410 1.2895 0.8509 0.0405 -0.0726 -0.0380 242 GLU A CB 1943 C CG . GLU A 242 ? 1.3678 1.3360 0.8673 0.0573 -0.0645 -0.0352 242 GLU A CG 1944 C CD . GLU A 242 ? 1.3820 1.3451 0.8830 0.0710 -0.0567 -0.0354 242 GLU A CD 1945 O OE1 . GLU A 242 ? 1.3973 1.3393 0.8933 0.0698 -0.0630 -0.0456 242 GLU A OE1 1946 O OE2 . GLU A 242 ? 1.3582 1.3384 0.8653 0.0835 -0.0436 -0.0251 242 GLU A OE2 1947 N N . SER A 243 ? 1.2701 1.2714 0.7832 0.0372 -0.0689 -0.0215 243 SER A N 1948 C CA . SER A 243 ? 1.2678 1.2907 0.7908 0.0431 -0.0598 -0.0068 243 SER A CA 1949 C C . SER A 243 ? 1.3122 1.3601 0.8182 0.0569 -0.0581 -0.0046 243 SER A C 1950 O O . SER A 243 ? 1.3418 1.3955 0.8291 0.0557 -0.0686 -0.0175 243 SER A O 1951 C CB . SER A 243 ? 1.2312 1.2549 0.7659 0.0282 -0.0650 -0.0054 243 SER A CB 1952 O OG . SER A 243 ? 1.2163 1.2567 0.7624 0.0344 -0.0551 0.0093 243 SER A OG 1953 N N . ASN A 244 ? 1.3337 1.3956 0.8459 0.0699 -0.0446 0.0115 244 ASN A N 1954 C CA . ASN A 244 ? 1.3655 1.4526 0.8618 0.0854 -0.0414 0.0175 244 ASN A CA 1955 C C . ASN A 244 ? 1.3501 1.4556 0.8494 0.0827 -0.0453 0.0224 244 ASN A C 1956 O O . ASN A 244 ? 1.3371 1.4661 0.8216 0.0951 -0.0462 0.0252 244 ASN A O 1957 C CB . ASN A 244 ? 1.4039 1.4950 0.9039 0.1022 -0.0226 0.0349 244 ASN A CB 1958 C CG . ASN A 244 ? 1.4713 1.5502 0.9688 0.1081 -0.0162 0.0317 244 ASN A CG 1959 O OD1 . ASN A 244 ? 1.5806 1.6486 1.0699 0.1024 -0.0266 0.0162 244 ASN A OD1 1960 N ND2 . ASN A 244 ? 1.4943 1.5745 0.9994 0.1197 0.0017 0.0465 244 ASN A ND2 1961 N N . GLY A 245 ? 1.3341 1.4305 0.8525 0.0681 -0.0472 0.0238 245 GLY A N 1962 C CA . GLY A 245 ? 1.3092 1.4228 0.8340 0.0661 -0.0490 0.0295 245 GLY A CA 1963 C C . GLY A 245 ? 1.2682 1.3681 0.8166 0.0550 -0.0435 0.0368 245 GLY A C 1964 O O . GLY A 245 ? 1.2507 1.3296 0.8116 0.0503 -0.0372 0.0391 245 GLY A O 1965 N N . ASN A 246 ? 1.2444 1.3583 0.7990 0.0516 -0.0462 0.0398 246 ASN A N 1966 C CA . ASN A 246 ? 1.2167 1.3204 0.7920 0.0407 -0.0423 0.0451 246 ASN A CA 1967 C C . ASN A 246 ? 1.1929 1.2773 0.7743 0.0199 -0.0522 0.0320 246 ASN A C 1968 O O . ASN A 246 ? 1.1886 1.2609 0.7857 0.0102 -0.0492 0.0349 246 ASN A O 1969 C CB . ASN A 246 ? 1.2105 1.3011 0.7998 0.0484 -0.0250 0.0603 246 ASN A CB 1970 C CG . ASN A 246 ? 1.2120 1.3167 0.7931 0.0697 -0.0126 0.0752 246 ASN A CG 1971 O OD1 . ASN A 246 ? 1.1884 1.2994 0.7534 0.0813 -0.0118 0.0749 246 ASN A OD1 1972 N ND2 . ASN A 246 ? 1.2136 1.3215 0.8047 0.0759 -0.0021 0.0888 246 ASN A ND2 1973 N N . PHE A 247 ? 1.1897 1.2706 0.7571 0.0135 -0.0637 0.0176 247 PHE A N 1974 C CA . PHE A 247 ? 1.1689 1.2269 0.7379 -0.0041 -0.0721 0.0059 247 PHE A CA 1975 C C . PHE A 247 ? 1.1568 1.2221 0.7276 -0.0196 -0.0813 -0.0017 247 PHE A C 1976 O O . PHE A 247 ? 1.1729 1.2584 0.7342 -0.0202 -0.0888 -0.0092 247 PHE A O 1977 C CB . PHE A 247 ? 1.1886 1.2351 0.7409 -0.0031 -0.0785 -0.0057 247 PHE A CB 1978 C CG . PHE A 247 ? 1.1864 1.2060 0.7369 -0.0191 -0.0866 -0.0170 247 PHE A CG 1979 C CD1 . PHE A 247 ? 1.1510 1.1512 0.7153 -0.0266 -0.0836 -0.0127 247 PHE A CD1 1980 C CD2 . PHE A 247 ? 1.1996 1.2122 0.7333 -0.0260 -0.0969 -0.0321 247 PHE A CD2 1981 C CE1 . PHE A 247 ? 1.1599 1.1347 0.7198 -0.0392 -0.0909 -0.0217 247 PHE A CE1 1982 C CE2 . PHE A 247 ? 1.1965 1.1806 0.7263 -0.0394 -0.1031 -0.0411 247 PHE A CE2 1983 C CZ . PHE A 247 ? 1.1883 1.1537 0.7305 -0.0453 -0.1001 -0.0351 247 PHE A CZ 1984 N N . ILE A 248 ? 1.1290 1.1793 0.7125 -0.0322 -0.0805 -0.0004 248 ILE A N 1985 C CA . ILE A 248 ? 1.1099 1.1624 0.6954 -0.0490 -0.0879 -0.0080 248 ILE A CA 1986 C C . ILE A 248 ? 1.1128 1.1369 0.6895 -0.0627 -0.0952 -0.0193 248 ILE A C 1987 O O . ILE A 248 ? 1.1209 1.1218 0.7031 -0.0677 -0.0930 -0.0168 248 ILE A O 1988 C CB . ILE A 248 ? 1.0837 1.1371 0.6864 -0.0535 -0.0815 0.0008 248 ILE A CB 1989 C CG1 . ILE A 248 ? 1.0872 1.1581 0.6989 -0.0366 -0.0707 0.0150 248 ILE A CG1 1990 C CG2 . ILE A 248 ? 1.0825 1.1476 0.6874 -0.0680 -0.0877 -0.0060 248 ILE A CG2 1991 C CD1 . ILE A 248 ? 1.1092 1.2114 0.7134 -0.0248 -0.0725 0.0160 248 ILE A CD1 1992 N N . ALA A 249 ? 1.1140 1.1395 0.6762 -0.0679 -0.1038 -0.0320 249 ALA A N 1993 C CA . ALA A 249 ? 1.1208 1.1162 0.6709 -0.0779 -0.1098 -0.0427 249 ALA A CA 1994 C C . ALA A 249 ? 1.1159 1.0968 0.6672 -0.0984 -0.1139 -0.0483 249 ALA A C 1995 O O . ALA A 249 ? 1.0893 1.0902 0.6477 -0.1069 -0.1149 -0.0494 249 ALA A O 1996 C CB . ALA A 249 ? 1.1491 1.1491 0.6821 -0.0753 -0.1164 -0.0551 249 ALA A CB 1997 N N . PRO A 250 ? 1.1189 1.0656 0.6630 -0.1055 -0.1158 -0.0515 250 PRO A N 1998 C CA . PRO A 250 ? 1.1313 1.0605 0.6721 -0.1248 -0.1190 -0.0570 250 PRO A CA 1999 C C . PRO A 250 ? 1.1788 1.1119 0.7092 -0.1377 -0.1253 -0.0712 250 PRO A C 2000 O O . PRO A 250 ? 1.2277 1.1607 0.7467 -0.1322 -0.1290 -0.0796 250 PRO A O 2001 C CB . PRO A 250 ? 1.1310 1.0217 0.6625 -0.1247 -0.1197 -0.0567 250 PRO A CB 2002 C CG . PRO A 250 ? 1.1281 1.0170 0.6549 -0.1075 -0.1192 -0.0565 250 PRO A CG 2003 C CD . PRO A 250 ? 1.1220 1.0454 0.6609 -0.0949 -0.1143 -0.0494 250 PRO A CD 2004 N N . GLU A 251 ? 1.1928 1.1308 0.7278 -0.1550 -0.1259 -0.0746 251 GLU A N 2005 C CA . GLU A 251 ? 1.2452 1.1770 0.7706 -0.1726 -0.1309 -0.0893 251 GLU A CA 2006 C C . GLU A 251 ? 1.2724 1.1645 0.7893 -0.1880 -0.1294 -0.0898 251 GLU A C 2007 O O . GLU A 251 ? 1.3032 1.1625 0.8034 -0.1930 -0.1319 -0.0976 251 GLU A O 2008 C CB . GLU A 251 ? 1.2594 1.2309 0.7973 -0.1816 -0.1323 -0.0942 251 GLU A CB 2009 C CG . GLU A 251 ? 1.3038 1.2757 0.8341 -0.1996 -0.1379 -0.1122 251 GLU A CG 2010 C CD . GLU A 251 ? 1.3114 1.3277 0.8568 -0.2085 -0.1399 -0.1182 251 GLU A CD 2011 O OE1 . GLU A 251 ? 1.2967 1.3433 0.8572 -0.1986 -0.1369 -0.1075 251 GLU A OE1 2012 O OE2 . GLU A 251 ? 1.3112 1.3320 0.8539 -0.2255 -0.1443 -0.1342 251 GLU A OE2 2013 N N . TYR A 252 ? 1.2494 1.1435 0.7764 -0.1941 -0.1248 -0.0810 252 TYR A N 2014 C CA . TYR A 252 ? 1.2597 1.1182 0.7778 -0.2072 -0.1224 -0.0791 252 TYR A CA 2015 C C . TYR A 252 ? 1.2383 1.0787 0.7564 -0.1945 -0.1199 -0.0667 252 TYR A C 2016 O O . TYR A 252 ? 1.1768 1.0390 0.7090 -0.1815 -0.1174 -0.0582 252 TYR A O 2017 C CB . TYR A 252 ? 1.2676 1.1409 0.7954 -0.2252 -0.1188 -0.0796 252 TYR A CB 2018 C CG . TYR A 252 ? 1.3008 1.1962 0.8320 -0.2398 -0.1214 -0.0932 252 TYR A CG 2019 C CD1 . TYR A 252 ? 1.3463 1.2147 0.8632 -0.2566 -0.1229 -0.1052 252 TYR A CD1 2020 C CD2 . TYR A 252 ? 1.2848 1.2282 0.8336 -0.2366 -0.1224 -0.0947 252 TYR A CD2 2021 C CE1 . TYR A 252 ? 1.3526 1.2431 0.8746 -0.2717 -0.1255 -0.1197 252 TYR A CE1 2022 C CE2 . TYR A 252 ? 1.3013 1.2696 0.8549 -0.2498 -0.1260 -0.1086 252 TYR A CE2 2023 C CZ . TYR A 252 ? 1.3319 1.2744 0.8729 -0.2683 -0.1277 -0.1219 252 TYR A CZ 2024 O OH . TYR A 252 ? 1.3184 1.2874 0.8660 -0.2830 -0.1314 -0.1376 252 TYR A OH 2025 N N . ALA A 253 ? 1.2514 1.0516 0.7533 -0.1983 -0.1203 -0.0663 253 ALA A N 2026 C CA . ALA A 253 ? 1.2328 1.0145 0.7331 -0.1881 -0.1192 -0.0563 253 ALA A CA 2027 C C . ALA A 253 ? 1.2545 1.0054 0.7415 -0.2020 -0.1172 -0.0543 253 ALA A C 2028 O O . ALA A 253 ? 1.2830 1.0128 0.7561 -0.2162 -0.1171 -0.0613 253 ALA A O 2029 C CB . ALA A 253 ? 1.2344 0.9977 0.7253 -0.1723 -0.1228 -0.0572 253 ALA A CB 2030 N N . TYR A 254 ? 1.2276 0.9757 0.7183 -0.1982 -0.1150 -0.0451 254 TYR A N 2031 C CA . TYR A 254 ? 1.2354 0.9575 0.7129 -0.2097 -0.1123 -0.0415 254 TYR A CA 2032 C C . TYR A 254 ? 1.2590 0.9399 0.7149 -0.2022 -0.1157 -0.0391 254 TYR A C 2033 O O . TYR A 254 ? 1.2632 0.9429 0.7214 -0.1853 -0.1193 -0.0359 254 TYR A O 2034 C CB . TYR A 254 ? 1.2070 0.9474 0.6974 -0.2090 -0.1085 -0.0338 254 TYR A CB 2035 C CG . TYR A 254 ? 1.1779 0.9554 0.6873 -0.2172 -0.1041 -0.0352 254 TYR A CG 2036 C CD1 . TYR A 254 ? 1.1866 0.9653 0.6939 -0.2356 -0.0993 -0.0371 254 TYR A CD1 2037 C CD2 . TYR A 254 ? 1.1469 0.9584 0.6763 -0.2059 -0.1040 -0.0341 254 TYR A CD2 2038 C CE1 . TYR A 254 ? 1.1705 0.9862 0.6965 -0.2417 -0.0955 -0.0387 254 TYR A CE1 2039 C CE2 . TYR A 254 ? 1.1395 0.9852 0.6855 -0.2109 -0.1002 -0.0346 254 TYR A CE2 2040 C CZ . TYR A 254 ? 1.1572 1.0064 0.7022 -0.2285 -0.0964 -0.0374 254 TYR A CZ 2041 O OH . TYR A 254 ? 1.1521 1.0382 0.7147 -0.2323 -0.0928 -0.0383 254 TYR A OH 2042 N N . LYS A 255 ? 1.3086 0.9558 0.7437 -0.2149 -0.1137 -0.0406 255 LYS A N 2043 C CA . LYS A 255 ? 1.3613 0.9652 0.7722 -0.2078 -0.1162 -0.0376 255 LYS A CA 2044 C C . LYS A 255 ? 1.3407 0.9315 0.7424 -0.2086 -0.1140 -0.0280 255 LYS A C 2045 O O . LYS A 255 ? 1.3025 0.9001 0.7061 -0.2235 -0.1081 -0.0261 255 LYS A O 2046 C CB . LYS A 255 ? 1.4294 1.0000 0.8205 -0.2211 -0.1141 -0.0446 255 LYS A CB 2047 C CG . LYS A 255 ? 1.4823 1.0105 0.8501 -0.2092 -0.1177 -0.0447 255 LYS A CG 2048 C CD . LYS A 255 ? 1.5166 1.0219 0.8722 -0.2197 -0.1163 -0.0557 255 LYS A CD 2049 C CE . LYS A 255 ? 1.5493 1.0333 0.8937 -0.2445 -0.1085 -0.0576 255 LYS A CE 2050 N NZ . LYS A 255 ? 1.5968 1.0488 0.9257 -0.2544 -0.1068 -0.0687 255 LYS A NZ 2051 N N . ILE A 256 ? 1.3365 0.9112 0.7288 -0.1919 -0.1189 -0.0226 256 ILE A N 2052 C CA . ILE A 256 ? 1.3465 0.9118 0.7294 -0.1892 -0.1186 -0.0142 256 ILE A CA 2053 C C . ILE A 256 ? 1.4139 0.9304 0.7634 -0.1926 -0.1170 -0.0100 256 ILE A C 2054 O O . ILE A 256 ? 1.4080 0.8989 0.7411 -0.1772 -0.1224 -0.0072 256 ILE A O 2055 C CB . ILE A 256 ? 1.3203 0.9011 0.7143 -0.1689 -0.1254 -0.0115 256 ILE A CB 2056 C CG1 . ILE A 256 ? 1.2753 0.9012 0.7015 -0.1670 -0.1245 -0.0144 256 ILE A CG1 2057 C CG2 . ILE A 256 ? 1.3383 0.9093 0.7203 -0.1654 -0.1265 -0.0044 256 ILE A CG2 2058 C CD1 . ILE A 256 ? 1.2540 0.8957 0.6950 -0.1481 -0.1301 -0.0147 256 ILE A CD1 2059 N N . VAL A 257 ? 1.4693 0.9730 0.8089 -0.2123 -0.1089 -0.0092 257 VAL A N 2060 C CA . VAL A 257 ? 1.5658 1.0198 0.8726 -0.2184 -0.1046 -0.0047 257 VAL A CA 2061 C C . VAL A 257 ? 1.6032 1.0399 0.8903 -0.2106 -0.1048 0.0062 257 VAL A C 2062 O O . VAL A 257 ? 1.6427 1.0394 0.9017 -0.2005 -0.1067 0.0119 257 VAL A O 2063 C CB . VAL A 257 ? 1.5935 1.0381 0.8969 -0.2446 -0.0943 -0.0088 257 VAL A CB 2064 C CG1 . VAL A 257 ? 1.5871 1.0474 0.9070 -0.2513 -0.0956 -0.0210 257 VAL A CG1 2065 C CG2 . VAL A 257 ? 1.5844 1.0572 0.9009 -0.2588 -0.0874 -0.0061 257 VAL A CG2 2066 N N . LYS A 258 ? 1.5816 1.0483 0.8822 -0.2139 -0.1030 0.0088 258 LYS A N 2067 C CA . LYS A 258 ? 1.6208 1.0748 0.9025 -0.2076 -0.1030 0.0181 258 LYS A CA 2068 C C . LYS A 258 ? 1.5606 1.0515 0.8623 -0.1945 -0.1098 0.0178 258 LYS A C 2069 O O . LYS A 258 ? 1.5127 1.0414 0.8417 -0.2009 -0.1075 0.0134 258 LYS A O 2070 C CB . LYS A 258 ? 1.6492 1.0937 0.9193 -0.2281 -0.0910 0.0223 258 LYS A CB 2071 C CG . LYS A 258 ? 1.6903 1.1125 0.9323 -0.2218 -0.0898 0.0327 258 LYS A CG 2072 C CD . LYS A 258 ? 1.7521 1.1532 0.9758 -0.2424 -0.0758 0.0380 258 LYS A CD 2073 C CE . LYS A 258 ? 1.7863 1.1667 0.9798 -0.2349 -0.0740 0.0490 258 LYS A CE 2074 N NZ . LYS A 258 ? 1.8398 1.1915 1.0102 -0.2543 -0.0588 0.0558 258 LYS A NZ 2075 N N . LYS A 259 ? 1.5635 1.0425 0.8510 -0.1758 -0.1180 0.0220 259 LYS A N 2076 C CA . LYS A 259 ? 1.5465 1.0556 0.8490 -0.1638 -0.1246 0.0212 259 LYS A CA 2077 C C . LYS A 259 ? 1.5611 1.0554 0.8382 -0.1626 -0.1234 0.0285 259 LYS A C 2078 O O . LYS A 259 ? 1.6079 1.0636 0.8517 -0.1584 -0.1232 0.0357 259 LYS A O 2079 C CB . LYS A 259 ? 1.5595 1.0725 0.8680 -0.1422 -0.1361 0.0186 259 LYS A CB 2080 C CG . LYS A 259 ? 1.5721 1.1006 0.9041 -0.1406 -0.1374 0.0117 259 LYS A CG 2081 C CD . LYS A 259 ? 1.5871 1.1188 0.9239 -0.1189 -0.1477 0.0095 259 LYS A CD 2082 C CE . LYS A 259 ? 1.5906 1.1345 0.9470 -0.1167 -0.1478 0.0031 259 LYS A CE 2083 N NZ . LYS A 259 ? 1.6102 1.1513 0.9671 -0.0956 -0.1565 0.0014 259 LYS A NZ 2084 N N . GLY A 260 ? 1.5423 1.0656 0.8334 -0.1655 -0.1222 0.0268 260 GLY A N 2085 C CA . GLY A 260 ? 1.5662 1.0795 0.8335 -0.1633 -0.1215 0.0325 260 GLY A CA 2086 C C . GLY A 260 ? 1.5306 1.0807 0.8188 -0.1639 -0.1219 0.0276 260 GLY A C 2087 O O . GLY A 260 ? 1.5265 1.1086 0.8475 -0.1614 -0.1249 0.0201 260 GLY A O 2088 N N . ASP A 261 ? 1.5358 1.0795 0.8036 -0.1668 -0.1180 0.0318 261 ASP A N 2089 C CA . ASP A 261 ? 1.5119 1.0869 0.7960 -0.1683 -0.1170 0.0265 261 ASP A CA 2090 C C . ASP A 261 ? 1.4439 1.0402 0.7519 -0.1860 -0.1053 0.0235 261 ASP A C 2091 O O . ASP A 261 ? 1.4614 1.0437 0.7580 -0.2006 -0.0948 0.0282 261 ASP A O 2092 C CB . ASP A 261 ? 1.5897 1.1510 0.8416 -0.1652 -0.1163 0.0316 261 ASP A CB 2093 C CG . ASP A 261 ? 1.6353 1.2050 0.8821 -0.1458 -0.1303 0.0278 261 ASP A CG 2094 O OD1 . ASP A 261 ? 1.6509 1.2379 0.9215 -0.1358 -0.1399 0.0211 261 ASP A OD1 2095 O OD2 . ASP A 261 ? 1.6927 1.2531 0.9117 -0.1406 -0.1317 0.0312 261 ASP A OD2 2096 N N . SER A 262 ? 1.3616 0.9922 0.7033 -0.1844 -0.1068 0.0157 262 SER A N 2097 C CA . SER A 262 ? 1.3346 0.9894 0.7008 -0.1977 -0.0966 0.0127 262 SER A CA 2098 C C . SER A 262 ? 1.2863 0.9733 0.6807 -0.1918 -0.0986 0.0052 262 SER A C 2099 O O . SER A 262 ? 1.3057 0.9961 0.7010 -0.1794 -0.1077 0.0015 262 SER A O 2100 C CB . SER A 262 ? 1.3269 0.9833 0.7081 -0.2040 -0.0945 0.0122 262 SER A CB 2101 O OG . SER A 262 ? 1.3217 1.0041 0.7263 -0.2152 -0.0856 0.0094 262 SER A OG 2102 N N . THR A 263 ? 1.0321 0.9583 0.7222 -0.0367 -0.1095 0.0022 263 THR A N 2103 C CA . THR A 263 ? 0.9531 0.9298 0.6866 -0.0487 -0.1002 0.0012 263 THR A CA 2104 C C . THR A 263 ? 0.9439 0.9113 0.6911 -0.0718 -0.1016 0.0090 263 THR A C 2105 O O . THR A 263 ? 0.9452 0.8805 0.6804 -0.0826 -0.1084 0.0164 263 THR A O 2106 C CB . THR A 263 ? 0.9182 0.9213 0.6780 -0.0522 -0.0954 0.0019 263 THR A CB 2107 O OG1 . THR A 263 ? 0.8813 0.9260 0.6689 -0.0616 -0.0877 -0.0009 263 THR A OG1 2108 C CG2 . THR A 263 ? 0.9121 0.8954 0.6804 -0.0695 -0.0988 0.0118 263 THR A CG2 2109 N N . ILE A 264 ? 0.9227 0.9184 0.6902 -0.0805 -0.0960 0.0071 264 ILE A N 2110 C CA . ILE A 264 ? 0.9056 0.8927 0.6836 -0.0983 -0.0981 0.0133 264 ILE A CA 2111 C C . ILE A 264 ? 0.8891 0.8935 0.6907 -0.1065 -0.0953 0.0156 264 ILE A C 2112 O O . ILE A 264 ? 0.8666 0.8919 0.6754 -0.1098 -0.0899 0.0116 264 ILE A O 2113 C CB . ILE A 264 ? 0.8951 0.8872 0.6664 -0.1029 -0.0961 0.0099 264 ILE A CB 2114 C CG1 . ILE A 264 ? 0.9212 0.8955 0.6655 -0.0901 -0.0993 0.0066 264 ILE A CG1 2115 C CG2 . ILE A 264 ? 0.8773 0.8540 0.6536 -0.1180 -0.1002 0.0161 264 ILE A CG2 2116 C CD1 . ILE A 264 ? 0.9312 0.9191 0.6678 -0.0920 -0.0960 0.0017 264 ILE A CD1 2117 N N . MET A 265 ? 0.9025 0.8987 0.7116 -0.1107 -0.0996 0.0219 265 MET A N 2118 C CA . MET A 265 ? 0.8858 0.8968 0.7132 -0.1130 -0.0983 0.0238 265 MET A CA 2119 C C . MET A 265 ? 0.8987 0.9044 0.7272 -0.1187 -0.1019 0.0258 265 MET A C 2120 O O . MET A 265 ? 0.9038 0.8985 0.7264 -0.1227 -0.1074 0.0291 265 MET A O 2121 C CB . MET A 265 ? 0.8917 0.9040 0.7237 -0.1142 -0.1015 0.0289 265 MET A CB 2122 C CG . MET A 265 ? 0.8946 0.9270 0.7435 -0.1109 -0.0985 0.0289 265 MET A CG 2123 S SD . MET A 265 ? 0.9190 0.9549 0.7666 -0.1162 -0.1011 0.0344 265 MET A SD 2124 C CE . MET A 265 ? 0.9319 0.9472 0.7589 -0.1072 -0.0989 0.0302 265 MET A CE 2125 N N . LYS A 266 ? 0.9190 0.9277 0.7487 -0.1186 -0.1001 0.0236 266 LYS A N 2126 C CA . LYS A 266 ? 0.9469 0.9407 0.7671 -0.1191 -0.1058 0.0248 266 LYS A CA 2127 C C . LYS A 266 ? 0.9484 0.9538 0.7790 -0.1087 -0.1096 0.0268 266 LYS A C 2128 O O . LYS A 266 ? 0.9636 0.9772 0.7992 -0.1041 -0.1064 0.0251 266 LYS A O 2129 C CB . LYS A 266 ? 0.9900 0.9678 0.7900 -0.1270 -0.1038 0.0210 266 LYS A CB 2130 C CG . LYS A 266 ? 1.0472 1.0293 0.8386 -0.1387 -0.0984 0.0178 266 LYS A CG 2131 C CD . LYS A 266 ? 1.0680 1.0358 0.8504 -0.1417 -0.1022 0.0195 266 LYS A CD 2132 C CE . LYS A 266 ? 1.1399 1.0765 0.8956 -0.1504 -0.1076 0.0201 266 LYS A CE 2133 N NZ . LYS A 266 ? 1.1897 1.1102 0.9380 -0.1504 -0.1132 0.0225 266 LYS A NZ 2134 N N . SER A 267 ? 0.9768 0.9886 0.8103 -0.1045 -0.1164 0.0298 267 SER A N 2135 C CA . SER A 267 ? 0.9704 1.0091 0.8160 -0.0930 -0.1202 0.0310 267 SER A CA 2136 C C . SER A 267 ? 0.9789 1.0273 0.8213 -0.0868 -0.1292 0.0324 267 SER A C 2137 O O . SER A 267 ? 0.9950 1.0390 0.8356 -0.0973 -0.1316 0.0351 267 SER A O 2138 C CB . SER A 267 ? 0.9607 1.0272 0.8250 -0.1000 -0.1162 0.0342 267 SER A CB 2139 O OG . SER A 267 ? 0.9681 1.0720 0.8452 -0.0923 -0.1192 0.0353 267 SER A OG 2140 N N . GLU A 268 ? 0.9705 1.0335 0.8099 -0.0671 -0.1350 0.0299 268 GLU A N 2141 C CA . GLU A 268 ? 0.9769 1.0610 0.8139 -0.0552 -0.1446 0.0297 268 GLU A CA 2142 C C . GLU A 268 ? 0.9501 1.0976 0.8138 -0.0604 -0.1450 0.0329 268 GLU A C 2143 O O . GLU A 268 ? 1.0017 1.1819 0.8684 -0.0560 -0.1524 0.0333 268 GLU A O 2144 C CB . GLU A 268 ? 1.0260 1.0943 0.8378 -0.0255 -0.1528 0.0238 268 GLU A CB 2145 C CG . GLU A 268 ? 1.0785 1.0770 0.8520 -0.0265 -0.1541 0.0213 268 GLU A CG 2146 C CD . GLU A 268 ? 1.1191 1.0875 0.8804 -0.0434 -0.1554 0.0236 268 GLU A CD 2147 O OE1 . GLU A 268 ? 1.1172 1.0958 0.8758 -0.0354 -0.1635 0.0240 268 GLU A OE1 2148 O OE2 . GLU A 268 ? 1.1425 1.0825 0.8971 -0.0640 -0.1483 0.0245 268 GLU A OE2 2149 N N . LEU A 269 ? 0.9236 1.0902 0.8035 -0.0720 -0.1375 0.0352 269 LEU A N 2150 C CA . LEU A 269 ? 0.9078 1.1328 0.8067 -0.0843 -0.1375 0.0390 269 LEU A CA 2151 C C . LEU A 269 ? 0.9326 1.1575 0.8287 -0.1121 -0.1398 0.0452 269 LEU A C 2152 O O . LEU A 269 ? 0.9148 1.0905 0.7970 -0.1217 -0.1389 0.0466 269 LEU A O 2153 C CB . LEU A 269 ? 0.8786 1.1108 0.7870 -0.0929 -0.1293 0.0405 269 LEU A CB 2154 C CG . LEU A 269 ? 0.8620 1.0985 0.7731 -0.0692 -0.1263 0.0351 269 LEU A CG 2155 C CD1 . LEU A 269 ? 0.8466 1.0889 0.7669 -0.0821 -0.1184 0.0375 269 LEU A CD1 2156 C CD2 . LEU A 269 ? 0.8618 1.1524 0.7786 -0.0446 -0.1325 0.0309 269 LEU A CD2 2157 N N . GLU A 270 ? 0.9792 1.2622 0.8854 -0.1259 -0.1432 0.0486 270 GLU A N 2158 C CA . GLU A 270 ? 1.0355 1.3204 0.9324 -0.1582 -0.1469 0.0554 270 GLU A CA 2159 C C . GLU A 270 ? 1.0280 1.3180 0.9192 -0.1875 -0.1429 0.0613 270 GLU A C 2160 O O . GLU A 270 ? 1.0367 1.3319 0.9357 -0.1803 -0.1368 0.0597 270 GLU A O 2161 C CB . GLU A 270 ? 1.0759 1.4255 0.9814 -0.1585 -0.1555 0.0554 270 GLU A CB 2162 C CG . GLU A 270 ? 1.1136 1.4528 1.0164 -0.1275 -0.1619 0.0494 270 GLU A CG 2163 C CD . GLU A 270 ? 1.1573 1.4386 1.0414 -0.1391 -0.1651 0.0520 270 GLU A CD 2164 O OE1 . GLU A 270 ? 1.1376 1.3577 1.0086 -0.1509 -0.1597 0.0543 270 GLU A OE1 2165 O OE2 . GLU A 270 ? 1.1897 1.4903 1.0711 -0.1340 -0.1736 0.0512 270 GLU A OE2 2166 N N . TYR A 271 ? 1.0488 1.3301 0.9198 -0.2216 -0.1473 0.0682 271 TYR A N 2167 C CA . TYR A 271 ? 1.0672 1.3389 0.9173 -0.2544 -0.1462 0.0748 271 TYR A CA 2168 C C . TYR A 271 ? 1.0665 1.4181 0.9355 -0.2636 -0.1442 0.0756 271 TYR A C 2169 O O . TYR A 271 ? 1.0351 1.4636 0.9271 -0.2569 -0.1471 0.0732 271 TYR A O 2170 C CB . TYR A 271 ? 1.1028 1.3462 0.9172 -0.2915 -0.1543 0.0822 271 TYR A CB 2171 C CG . TYR A 271 ? 1.1367 1.3387 0.9094 -0.3263 -0.1558 0.0893 271 TYR A CG 2172 C CD1 . TYR A 271 ? 1.1434 1.2726 0.8929 -0.3147 -0.1524 0.0877 271 TYR A CD1 2173 C CD2 . TYR A 271 ? 1.1579 1.3925 0.9081 -0.3718 -0.1618 0.0972 271 TYR A CD2 2174 C CE1 . TYR A 271 ? 1.1878 1.2679 0.8887 -0.3425 -0.1559 0.0935 271 TYR A CE1 2175 C CE2 . TYR A 271 ? 1.2142 1.3971 0.9131 -0.4067 -0.1651 0.1042 271 TYR A CE2 2176 C CZ . TYR A 271 ? 1.2344 1.3350 0.9064 -0.3896 -0.1626 0.1022 271 TYR A CZ 2177 O OH . TYR A 271 ? 1.2866 1.3259 0.8978 -0.4206 -0.1679 0.1086 271 TYR A OH 2178 N N . GLY A 272 ? 1.0854 1.4215 0.9427 -0.2769 -0.1396 0.0783 272 GLY A N 2179 C CA . GLY A 272 ? 1.0840 1.4939 0.9585 -0.2846 -0.1360 0.0786 272 GLY A CA 2180 C C . GLY A 272 ? 1.1124 1.5381 0.9571 -0.3364 -0.1388 0.0877 272 GLY A C 2181 O O . GLY A 272 ? 1.0796 1.5776 0.9379 -0.3481 -0.1357 0.0883 272 GLY A O 2182 N N . ASN A 273 ? 1.1442 1.5000 0.9425 -0.3682 -0.1452 0.0946 273 ASN A N 2183 C CA . ASN A 273 ? 1.1822 1.5268 0.9330 -0.4235 -0.1503 0.1045 273 ASN A CA 2184 C C . ASN A 273 ? 1.1698 1.4908 0.9037 -0.4303 -0.1454 0.1060 273 ASN A C 2185 O O . ASN A 273 ? 1.1790 1.5491 0.9020 -0.4669 -0.1452 0.1113 273 ASN A O 2186 C CB . ASN A 273 ? 1.1955 1.6456 0.9586 -0.4586 -0.1539 0.1082 273 ASN A CB 2187 C CG . ASN A 273 ? 1.2183 1.6932 0.9946 -0.4533 -0.1601 0.1068 273 ASN A CG 2188 O OD1 . ASN A 273 ? 1.2083 1.7505 1.0325 -0.4160 -0.1579 0.0991 273 ASN A OD1 2189 N ND2 . ASN A 273 ? 1.2639 1.6770 0.9914 -0.4887 -0.1691 0.1141 273 ASN A ND2 2190 N N . CYS A 274 ? 1.1429 1.3922 0.8731 -0.3964 -0.1415 0.1013 274 CYS A N 2191 C CA . CYS A 274 ? 1.1457 1.3645 0.8588 -0.3966 -0.1374 0.1018 274 CYS A CA 2192 C C . CYS A 274 ? 1.1710 1.2740 0.8318 -0.3883 -0.1419 0.1019 274 CYS A C 2193 O O . CYS A 274 ? 1.1721 1.2238 0.8149 -0.3790 -0.1470 0.1008 274 CYS A O 2194 C CB . CYS A 274 ? 1.0919 1.3625 0.8622 -0.3539 -0.1268 0.0933 274 CYS A CB 2195 S SG . CYS A 274 ? 1.0635 1.3367 0.8798 -0.3001 -0.1235 0.0833 274 CYS A SG 2196 N N . ASN A 275 ? 1.1793 1.2442 0.8136 -0.3896 -0.1405 0.1026 275 ASN A N 2197 C CA . ASN A 275 ? 1.2201 1.1829 0.8057 -0.3714 -0.1448 0.1003 275 ASN A CA 2198 C C . ASN A 275 ? 1.1985 1.1679 0.8132 -0.3356 -0.1361 0.0933 275 ASN A C 2199 O O . ASN A 275 ? 1.1799 1.2106 0.8270 -0.3403 -0.1292 0.0937 275 ASN A O 2200 C CB . ASN A 275 ? 1.2905 1.1758 0.7878 -0.4142 -0.1566 0.1092 275 ASN A CB 2201 C CG . ASN A 275 ? 1.3408 1.1124 0.7747 -0.3902 -0.1648 0.1058 275 ASN A CG 2202 O OD1 . ASN A 275 ? 1.3602 1.0940 0.7830 -0.3714 -0.1691 0.1023 275 ASN A OD1 2203 N ND2 . ASN A 275 ? 1.3849 1.1037 0.7748 -0.3880 -0.1676 0.1059 275 ASN A ND2 2204 N N . THR A 276 ? 1.2065 1.1184 0.8094 -0.2996 -0.1365 0.0865 276 THR A N 2205 C CA . THR A 276 ? 1.1683 1.0881 0.7981 -0.2658 -0.1288 0.0793 276 THR A CA 2206 C C . THR A 276 ? 1.2148 1.0588 0.8037 -0.2365 -0.1335 0.0733 276 THR A C 2207 O O . THR A 276 ? 1.2802 1.0703 0.8286 -0.2342 -0.1415 0.0730 276 THR A O 2208 C CB . THR A 276 ? 1.0883 1.0797 0.7926 -0.2381 -0.1183 0.0727 276 THR A CB 2209 O OG1 . THR A 276 ? 1.0863 1.0872 0.8123 -0.2126 -0.1114 0.0668 276 THR A OG1 2210 C CG2 . THR A 276 ? 1.0851 1.0626 0.7999 -0.2174 -0.1191 0.0678 276 THR A CG2 2211 N N . LYS A 277 ? 1.2155 1.0595 0.8139 -0.2123 -0.1289 0.0678 277 LYS A N 2212 C CA . LYS A 277 ? 1.2630 1.0540 0.8302 -0.1774 -0.1325 0.0597 277 LYS A CA 2213 C C . LYS A 277 ? 1.1736 1.0103 0.7968 -0.1427 -0.1235 0.0501 277 LYS A C 2214 O O . LYS A 277 ? 1.1596 0.9726 0.7665 -0.1118 -0.1253 0.0418 277 LYS A O 2215 C CB . LYS A 277 ? 1.3381 1.1045 0.8784 -0.1724 -0.1337 0.0591 277 LYS A CB 2216 C CG . LYS A 277 ? 1.4583 1.1717 0.9323 -0.2105 -0.1432 0.0689 277 LYS A CG 2217 C CD . LYS A 277 ? 1.5841 1.1987 0.9697 -0.2119 -0.1586 0.0701 277 LYS A CD 2218 C CE . LYS A 277 ? 1.7078 1.2409 1.0063 -0.2321 -0.1704 0.0757 277 LYS A CE 2219 N NZ . LYS A 277 ? 1.8248 1.2461 1.0256 -0.2182 -0.1874 0.0736 277 LYS A NZ 2220 N N . CYS A 278 ? 1.0883 0.9910 0.7720 -0.1480 -0.1148 0.0507 278 CYS A N 2221 C CA . CYS A 278 ? 1.0291 0.9735 0.7608 -0.1230 -0.1064 0.0428 278 CYS A CA 2222 C C . CYS A 278 ? 0.9676 0.9582 0.7412 -0.1328 -0.1023 0.0451 278 CYS A C 2223 O O . CYS A 278 ? 0.9613 0.9868 0.7545 -0.1480 -0.1002 0.0497 278 CYS A O 2224 C CB . CYS A 278 ? 1.0142 0.9824 0.7662 -0.1116 -0.1003 0.0396 278 CYS A CB 2225 S SG . CYS A 278 ? 0.9817 1.0007 0.7863 -0.0911 -0.0906 0.0315 278 CYS A SG 2226 N N . GLN A 279 ? 0.9206 0.9131 0.7047 -0.1224 -0.1017 0.0411 279 GLN A N 2227 C CA . GLN A 279 ? 0.8699 0.8941 0.6828 -0.1295 -0.1003 0.0429 279 GLN A CA 2228 C C . GLN A 279 ? 0.8118 0.8574 0.6526 -0.1123 -0.0945 0.0363 279 GLN A C 2229 O O . GLN A 279 ? 0.8051 0.8391 0.6389 -0.0991 -0.0928 0.0305 279 GLN A O 2230 C CB . GLN A 279 ? 0.8950 0.8933 0.6849 -0.1407 -0.1070 0.0462 279 GLN A CB 2231 C CG . GLN A 279 ? 0.8764 0.9067 0.6917 -0.1479 -0.1073 0.0483 279 GLN A CG 2232 C CD . GLN A 279 ? 0.8815 0.9502 0.7089 -0.1658 -0.1085 0.0542 279 GLN A CD 2233 O OE1 . GLN A 279 ? 0.9103 0.9684 0.7122 -0.1891 -0.1133 0.0604 279 GLN A OE1 2234 N NE2 . GLN A 279 ? 0.8560 0.9696 0.7167 -0.1556 -0.1050 0.0519 279 GLN A NE2 2235 N N . THR A 280 ? 0.7766 0.8536 0.6435 -0.1129 -0.0924 0.0370 280 THR A N 2236 C CA . THR A 280 ? 0.7664 0.8524 0.6479 -0.1020 -0.0893 0.0319 280 THR A CA 2237 C C . THR A 280 ? 0.7619 0.8554 0.6488 -0.1049 -0.0932 0.0338 280 THR A C 2238 O O . THR A 280 ? 0.7548 0.8627 0.6433 -0.1136 -0.0971 0.0385 280 THR A O 2239 C CB . THR A 280 ? 0.7454 0.8499 0.6413 -0.0936 -0.0849 0.0293 280 THR A CB 2240 O OG1 . THR A 280 ? 0.7195 0.8463 0.6265 -0.0916 -0.0869 0.0312 280 THR A OG1 2241 C CG2 . THR A 280 ? 0.7477 0.8521 0.6401 -0.0931 -0.0825 0.0296 280 THR A CG2 2242 N N . PRO A 281 ? 0.7698 0.8550 0.6559 -0.0992 -0.0928 0.0300 281 PRO A N 2243 C CA . PRO A 281 ? 0.8029 0.8881 0.6878 -0.0981 -0.0978 0.0309 281 PRO A CA 2244 C C . PRO A 281 ? 0.8233 0.9349 0.7176 -0.0893 -0.1010 0.0317 281 PRO A C 2245 O O . PRO A 281 ? 0.8098 0.9315 0.7036 -0.0869 -0.1068 0.0330 281 PRO A O 2246 C CB . PRO A 281 ? 0.8105 0.8755 0.6843 -0.0953 -0.0964 0.0262 281 PRO A CB 2247 C CG . PRO A 281 ? 0.8010 0.8634 0.6728 -0.0987 -0.0905 0.0232 281 PRO A CG 2248 C CD . PRO A 281 ? 0.7824 0.8575 0.6630 -0.0962 -0.0883 0.0247 281 PRO A CD 2249 N N . MET A 282 ? 0.8547 0.9807 0.7564 -0.0821 -0.0978 0.0303 282 MET A N 2250 C CA . MET A 282 ? 0.8737 1.0310 0.7828 -0.0688 -0.1005 0.0296 282 MET A CA 2251 C C . MET A 282 ? 0.8291 1.0283 0.7523 -0.0787 -0.0998 0.0340 282 MET A C 2252 O O . MET A 282 ? 0.8078 1.0489 0.7394 -0.0694 -0.1025 0.0334 282 MET A O 2253 C CB . MET A 282 ? 0.9276 1.0764 0.8320 -0.0551 -0.0978 0.0253 282 MET A CB 2254 C CG . MET A 282 ? 0.9896 1.0966 0.8698 -0.0486 -0.1006 0.0212 282 MET A CG 2255 S SD . MET A 282 ? 1.1338 1.2244 1.0010 -0.0398 -0.0981 0.0171 282 MET A SD 2256 C CE . MET A 282 ? 1.0894 1.2172 0.9635 -0.0149 -0.1016 0.0156 282 MET A CE 2257 N N . GLY A 283 ? 0.8158 1.0038 0.7361 -0.0974 -0.0970 0.0380 283 GLY A N 2258 C CA . GLY A 283 ? 0.8191 1.0360 0.7417 -0.1146 -0.0969 0.0432 283 GLY A CA 2259 C C . GLY A 283 ? 0.8274 1.0121 0.7352 -0.1268 -0.0940 0.0454 283 GLY A C 2260 O O . GLY A 283 ? 0.8412 0.9916 0.7421 -0.1181 -0.0917 0.0419 283 GLY A O 2261 N N . ALA A 284 ? 0.8375 1.0349 0.7360 -0.1469 -0.0949 0.0508 284 ALA A N 2262 C CA . ALA A 284 ? 0.8757 1.0321 0.7474 -0.1581 -0.0949 0.0532 284 ALA A CA 2263 C C . ALA A 284 ? 0.8920 1.0610 0.7692 -0.1539 -0.0899 0.0522 284 ALA A C 2264 O O . ALA A 284 ? 0.8885 1.1057 0.7870 -0.1509 -0.0870 0.0518 284 ALA A O 2265 C CB . ALA A 284 ? 0.9130 1.0561 0.7543 -0.1890 -0.1012 0.0608 284 ALA A CB 2266 N N . ILE A 285 ? 0.9077 1.0342 0.7626 -0.1512 -0.0897 0.0512 285 ILE A N 2267 C CA . ILE A 285 ? 0.9038 1.0344 0.7610 -0.1449 -0.0854 0.0497 285 ILE A CA 2268 C C . ILE A 285 ? 0.9588 1.0569 0.7763 -0.1652 -0.0894 0.0551 285 ILE A C 2269 O O . ILE A 285 ? 1.0096 1.0538 0.7886 -0.1678 -0.0955 0.0559 285 ILE A O 2270 C CB . ILE A 285 ? 0.8856 0.9977 0.7493 -0.1200 -0.0821 0.0422 285 ILE A CB 2271 C CG1 . ILE A 285 ? 0.8497 0.9912 0.7448 -0.1051 -0.0781 0.0376 285 ILE A CG1 2272 C CG2 . ILE A 285 ? 0.8982 1.0014 0.7532 -0.1150 -0.0798 0.0409 285 ILE A CG2 2273 C CD1 . ILE A 285 ? 0.8475 0.9731 0.7444 -0.0899 -0.0761 0.0310 285 ILE A CD1 2274 N N . ASN A 286 ? 0.9769 1.1049 0.7982 -0.1782 -0.0868 0.0584 286 ASN A N 2275 C CA . ASN A 286 ? 1.0289 1.1248 0.8076 -0.2011 -0.0905 0.0640 286 ASN A CA 2276 C C . ASN A 286 ? 1.0129 1.1219 0.8027 -0.1897 -0.0848 0.0614 286 ASN A C 2277 O O . ASN A 286 ? 0.9938 1.1555 0.8048 -0.1986 -0.0800 0.0631 286 ASN A O 2278 C CB . ASN A 286 ? 1.0682 1.1953 0.8346 -0.2399 -0.0932 0.0724 286 ASN A CB 2279 C CG . ASN A 286 ? 1.1407 1.2321 0.8545 -0.2718 -0.0977 0.0794 286 ASN A CG 2280 O OD1 . ASN A 286 ? 1.2016 1.2154 0.8656 -0.2691 -0.1043 0.0796 286 ASN A OD1 2281 N ND2 . ASN A 286 ? 1.1462 1.2946 0.8657 -0.3017 -0.0950 0.0847 286 ASN A ND2 2282 N N . SER A 287 ? 1.0273 1.0940 0.8033 -0.1679 -0.0855 0.0563 287 SER A N 2283 C CA . SER A 287 ? 1.0343 1.1077 0.8165 -0.1571 -0.0811 0.0537 287 SER A CA 2284 C C . SER A 287 ? 1.0536 1.0706 0.8018 -0.1387 -0.0856 0.0494 287 SER A C 2285 O O . SER A 287 ? 1.0425 1.0258 0.7733 -0.1245 -0.0905 0.0457 287 SER A O 2286 C CB . SER A 287 ? 0.9930 1.1178 0.8269 -0.1355 -0.0730 0.0479 287 SER A CB 2287 O OG . SER A 287 ? 0.9796 1.0902 0.8242 -0.1115 -0.0725 0.0409 287 SER A OG 2288 N N . SER A 288 ? 1.0833 1.0951 0.8220 -0.1365 -0.0841 0.0491 288 SER A N 2289 C CA . SER A 288 ? 1.1191 1.0835 0.8241 -0.1156 -0.0891 0.0441 288 SER A CA 2290 C C . SER A 288 ? 1.0649 1.0629 0.8099 -0.0865 -0.0826 0.0354 288 SER A C 2291 O O . SER A 288 ? 1.0557 1.0315 0.7813 -0.0670 -0.0855 0.0302 288 SER A O 2292 C CB . SER A 288 ? 1.1798 1.1104 0.8404 -0.1341 -0.0930 0.0497 288 SER A CB 2293 O OG . SER A 288 ? 1.1612 1.1462 0.8575 -0.1468 -0.0842 0.0524 288 SER A OG 2294 N N . MET A 289 ? 1.0067 1.0557 0.8015 -0.0842 -0.0751 0.0336 289 MET A N 2295 C CA . MET A 289 ? 0.9592 1.0367 0.7858 -0.0639 -0.0697 0.0263 289 MET A CA 2296 C C . MET A 289 ? 0.9461 1.0125 0.7657 -0.0442 -0.0728 0.0189 289 MET A C 2297 O O . MET A 289 ? 0.9845 1.0331 0.7900 -0.0447 -0.0769 0.0191 289 MET A O 2298 C CB . MET A 289 ? 0.9413 1.0602 0.8072 -0.0668 -0.0638 0.0263 289 MET A CB 2299 C CG . MET A 289 ? 0.9461 1.0927 0.8241 -0.0797 -0.0604 0.0314 289 MET A CG 2300 S SD . MET A 289 ? 0.9452 1.1028 0.8263 -0.0739 -0.0562 0.0300 289 MET A SD 2301 C CE . MET A 289 ? 0.9103 1.1179 0.8201 -0.0738 -0.0511 0.0307 289 MET A CE 2302 N N . PRO A 290 ? 0.9057 0.9883 0.7349 -0.0272 -0.0707 0.0118 290 PRO A N 2303 C CA . PRO A 290 ? 0.8879 0.9806 0.7167 -0.0096 -0.0723 0.0036 290 PRO A CA 2304 C C . PRO A 290 ? 0.8422 0.9661 0.7013 -0.0162 -0.0676 0.0019 290 PRO A C 2305 O O . PRO A 290 ? 0.8450 0.9799 0.7022 -0.0074 -0.0687 -0.0037 290 PRO A O 2306 C CB . PRO A 290 ? 0.8777 0.9884 0.7087 0.0054 -0.0714 -0.0028 290 PRO A CB 2307 C CG . PRO A 290 ? 0.8619 0.9833 0.7122 -0.0079 -0.0661 0.0018 290 PRO A CG 2308 C CD . PRO A 290 ? 0.8830 0.9789 0.7207 -0.0242 -0.0674 0.0107 290 PRO A CD 2309 N N . PHE A 291 ? 0.8079 0.9451 0.6895 -0.0300 -0.0631 0.0062 291 PHE A N 2310 C CA . PHE A 291 ? 0.7874 0.9421 0.6871 -0.0365 -0.0604 0.0049 291 PHE A CA 2311 C C . PHE A 291 ? 0.7527 0.9033 0.6603 -0.0472 -0.0603 0.0110 291 PHE A C 2312 O O . PHE A 291 ? 0.7526 0.9016 0.6598 -0.0517 -0.0602 0.0160 291 PHE A O 2313 C CB . PHE A 291 ? 0.8093 0.9833 0.7207 -0.0377 -0.0568 0.0014 291 PHE A CB 2314 C CG . PHE A 291 ? 0.8297 1.0228 0.7379 -0.0299 -0.0565 -0.0055 291 PHE A CG 2315 C CD1 . PHE A 291 ? 0.8398 1.0546 0.7478 -0.0305 -0.0565 -0.0112 291 PHE A CD1 2316 C CD2 . PHE A 291 ? 0.8359 1.0320 0.7412 -0.0224 -0.0563 -0.0069 291 PHE A CD2 2317 C CE1 . PHE A 291 ? 0.8369 1.0842 0.7435 -0.0231 -0.0563 -0.0188 291 PHE A CE1 2318 C CE2 . PHE A 291 ? 0.8516 1.0732 0.7546 -0.0135 -0.0567 -0.0143 291 PHE A CE2 2319 C CZ . PHE A 291 ? 0.8389 1.0903 0.7434 -0.0136 -0.0567 -0.0205 291 PHE A CZ 2320 N N . HIS A 292 ? 0.7321 0.8856 0.6453 -0.0512 -0.0604 0.0102 292 HIS A N 2321 C CA . HIS A 292 ? 0.7116 0.8659 0.6317 -0.0563 -0.0612 0.0141 292 HIS A CA 2322 C C . HIS A 292 ? 0.6916 0.8436 0.6106 -0.0579 -0.0613 0.0108 292 HIS A C 2323 O O . HIS A 292 ? 0.6968 0.8511 0.6111 -0.0609 -0.0603 0.0064 292 HIS A O 2324 C CB . HIS A 292 ? 0.7284 0.8747 0.6438 -0.0625 -0.0644 0.0184 292 HIS A CB 2325 C CG . HIS A 292 ? 0.7346 0.8713 0.6439 -0.0633 -0.0662 0.0160 292 HIS A CG 2326 N ND1 . HIS A 292 ? 0.7311 0.8658 0.6430 -0.0677 -0.0679 0.0170 292 HIS A ND1 2327 C CD2 . HIS A 292 ? 0.7552 0.8867 0.6541 -0.0579 -0.0667 0.0118 292 HIS A CD2 2328 C CE1 . HIS A 292 ? 0.7499 0.8778 0.6544 -0.0681 -0.0686 0.0142 292 HIS A CE1 2329 N NE2 . HIS A 292 ? 0.7592 0.8883 0.6564 -0.0610 -0.0678 0.0106 292 HIS A NE2 2330 N N . ASN A 293 ? 0.6750 0.8231 0.5932 -0.0562 -0.0635 0.0126 293 ASN A N 2331 C CA . ASN A 293 ? 0.6808 0.8121 0.5850 -0.0581 -0.0660 0.0100 293 ASN A CA 2332 C C . ASN A 293 ? 0.6942 0.8170 0.5940 -0.0562 -0.0704 0.0120 293 ASN A C 2333 O O . ASN A 293 ? 0.7147 0.8173 0.5959 -0.0514 -0.0748 0.0105 293 ASN A O 2334 C CB . ASN A 293 ? 0.6789 0.8007 0.5711 -0.0514 -0.0667 0.0079 293 ASN A CB 2335 C CG . ASN A 293 ? 0.6727 0.8021 0.5671 -0.0357 -0.0689 0.0094 293 ASN A CG 2336 O OD1 . ASN A 293 ? 0.6524 0.8035 0.5618 -0.0335 -0.0689 0.0126 293 ASN A OD1 2337 N ND2 . ASN A 293 ? 0.6898 0.8037 0.5656 -0.0249 -0.0713 0.0067 293 ASN A ND2 2338 N N . ILE A 294 ? 0.6891 0.8222 0.5999 -0.0595 -0.0707 0.0152 294 ILE A N 2339 C CA . ILE A 294 ? 0.7217 0.8537 0.6312 -0.0581 -0.0751 0.0175 294 ILE A CA 2340 C C . ILE A 294 ? 0.7392 0.8484 0.6347 -0.0648 -0.0775 0.0157 294 ILE A C 2341 O O . ILE A 294 ? 0.7520 0.8428 0.6309 -0.0601 -0.0822 0.0145 294 ILE A O 2342 C CB . ILE A 294 ? 0.7237 0.8723 0.6444 -0.0648 -0.0754 0.0223 294 ILE A CB 2343 C CG1 . ILE A 294 ? 0.7197 0.8918 0.6493 -0.0642 -0.0730 0.0247 294 ILE A CG1 2344 C CG2 . ILE A 294 ? 0.7337 0.8880 0.6542 -0.0647 -0.0804 0.0244 294 ILE A CG2 2345 C CD1 . ILE A 294 ? 0.7179 0.9101 0.6511 -0.0502 -0.0736 0.0228 294 ILE A CD1 2346 N N . HIS A 295 ? 0.7485 0.8577 0.6457 -0.0741 -0.0748 0.0150 295 HIS A N 2347 C CA . HIS A 295 ? 0.7855 0.8813 0.6709 -0.0827 -0.0760 0.0134 295 HIS A CA 2348 C C . HIS A 295 ? 0.7753 0.8841 0.6628 -0.0875 -0.0717 0.0100 295 HIS A C 2349 O O . HIS A 295 ? 0.7482 0.8663 0.6432 -0.0814 -0.0705 0.0105 295 HIS A O 2350 C CB . HIS A 295 ? 0.8256 0.9168 0.7125 -0.0823 -0.0802 0.0169 295 HIS A CB 2351 C CG . HIS A 295 ? 0.8710 0.9435 0.7422 -0.0896 -0.0828 0.0157 295 HIS A CG 2352 N ND1 . HIS A 295 ? 0.8925 0.9670 0.7606 -0.0982 -0.0802 0.0137 295 HIS A ND1 2353 C CD2 . HIS A 295 ? 0.9227 0.9733 0.7766 -0.0882 -0.0884 0.0159 295 HIS A CD2 2354 C CE1 . HIS A 295 ? 0.9144 0.9710 0.7662 -0.1058 -0.0831 0.0134 295 HIS A CE1 2355 N NE2 . HIS A 295 ? 0.9347 0.9721 0.7756 -0.1001 -0.0886 0.0149 295 HIS A NE2 2356 N N . PRO A 296 ? 0.7980 0.9083 0.6740 -0.0982 -0.0702 0.0062 296 PRO A N 2357 C CA . PRO A 296 ? 0.7844 0.9217 0.6633 -0.0984 -0.0662 0.0012 296 PRO A CA 2358 C C . PRO A 296 ? 0.7941 0.9324 0.6737 -0.0899 -0.0673 0.0010 296 PRO A C 2359 O O . PRO A 296 ? 0.7962 0.9462 0.6763 -0.0772 -0.0666 -0.0018 296 PRO A O 2360 C CB . PRO A 296 ? 0.7847 0.9302 0.6485 -0.1173 -0.0646 -0.0023 296 PRO A CB 2361 C CG . PRO A 296 ? 0.8108 0.9184 0.6571 -0.1261 -0.0694 0.0015 296 PRO A CG 2362 C CD . PRO A 296 ? 0.8198 0.9091 0.6739 -0.1109 -0.0728 0.0057 296 PRO A CD 2363 N N . LEU A 297 ? 0.8258 0.9470 0.6995 -0.0952 -0.0701 0.0037 297 LEU A N 2364 C CA . LEU A 297 ? 0.8556 0.9709 0.7238 -0.0886 -0.0722 0.0037 297 LEU A CA 2365 C C . LEU A 297 ? 0.8361 0.9321 0.7041 -0.0813 -0.0762 0.0089 297 LEU A C 2366 O O . LEU A 297 ? 0.8562 0.9398 0.7281 -0.0871 -0.0794 0.0146 297 LEU A O 2367 C CB . LEU A 297 ? 0.8920 0.9938 0.7524 -0.0988 -0.0743 0.0053 297 LEU A CB 2368 C CG . LEU A 297 ? 0.9374 1.0504 0.7885 -0.1141 -0.0714 0.0015 297 LEU A CG 2369 C CD1 . LEU A 297 ? 0.9693 1.0571 0.8081 -0.1239 -0.0752 0.0046 297 LEU A CD1 2370 C CD2 . LEU A 297 ? 0.9455 1.0972 0.7948 -0.1121 -0.0665 -0.0060 297 LEU A CD2 2371 N N . THR A 298 ? 0.8136 0.9077 0.6723 -0.0693 -0.0769 0.0067 298 THR A N 2372 C CA . THR A 298 ? 0.8097 0.8773 0.6561 -0.0683 -0.0820 0.0122 298 THR A CA 2373 C C . THR A 298 ? 0.8337 0.8763 0.6495 -0.0568 -0.0868 0.0096 298 THR A C 2374 O O . THR A 298 ? 0.8144 0.8702 0.6234 -0.0439 -0.0854 0.0021 298 THR A O 2375 C CB . THR A 298 ? 0.7928 0.8639 0.6429 -0.0654 -0.0808 0.0134 298 THR A CB 2376 O OG1 . THR A 298 ? 0.7792 0.8488 0.6129 -0.0485 -0.0813 0.0073 298 THR A OG1 2377 C CG2 . THR A 298 ? 0.7773 0.8732 0.6515 -0.0700 -0.0759 0.0130 298 THR A CG2 2378 N N . ILE A 299 ? 0.8509 0.8577 0.6431 -0.0622 -0.0933 0.0155 299 ILE A N 2379 C CA . ILE A 299 ? 0.9051 0.8709 0.6534 -0.0502 -0.1006 0.0135 299 ILE A CA 2380 C C . ILE A 299 ? 0.9583 0.8851 0.6748 -0.0560 -0.1070 0.0189 299 ILE A C 2381 O O . ILE A 299 ? 0.9396 0.8712 0.6683 -0.0783 -0.1066 0.0269 299 ILE A O 2382 C CB . ILE A 299 ? 0.9337 0.8782 0.6680 -0.0580 -0.1049 0.0161 299 ILE A CB 2383 C CG1 . ILE A 299 ? 0.9892 0.8812 0.6676 -0.0426 -0.1142 0.0134 299 ILE A CG1 2384 C CG2 . ILE A 299 ? 0.9330 0.8738 0.6780 -0.0852 -0.1071 0.0262 299 ILE A CG2 2385 C CD1 . ILE A 299 ? 1.0125 0.8924 0.6776 -0.0398 -0.1168 0.0116 299 ILE A CD1 2386 N N . GLY A 300 ? 1.0250 0.9146 0.6966 -0.0351 -0.1134 0.0140 300 GLY A N 2387 C CA . GLY A 300 ? 1.1153 0.9549 0.7422 -0.0400 -0.1212 0.0185 300 GLY A CA 2388 C C . GLY A 300 ? 1.1557 1.0111 0.7884 -0.0228 -0.1183 0.0134 300 GLY A C 2389 O O . GLY A 300 ? 1.1420 1.0472 0.8093 -0.0048 -0.1111 0.0054 300 GLY A O 2390 N N . GLU A 301 ? 1.2309 1.0439 0.8264 -0.0317 -0.1244 0.0185 301 GLU A N 2391 C CA . GLU A 301 ? 1.2596 1.0811 0.8556 -0.0171 -0.1228 0.0146 301 GLU A CA 2392 C C . GLU A 301 ? 1.1623 1.0429 0.8202 -0.0368 -0.1116 0.0189 301 GLU A C 2393 O O . GLU A 301 ? 1.1472 1.0229 0.8058 -0.0644 -0.1114 0.0279 301 GLU A O 2394 C CB . GLU A 301 ? 1.3908 1.1361 0.9151 -0.0215 -0.1346 0.0190 301 GLU A CB 2395 C CG . GLU A 301 ? 1.4871 1.2028 0.9682 0.0188 -0.1417 0.0087 301 GLU A CG 2396 C CD . GLU A 301 ? 1.5746 1.2598 1.0121 0.0549 -0.1504 -0.0009 301 GLU A CD 2397 O OE1 . GLU A 301 ? 1.5926 1.2360 0.9985 0.0435 -0.1566 0.0030 301 GLU A OE1 2398 O OE2 . GLU A 301 ? 1.6451 1.3523 1.0788 0.0962 -0.1514 -0.0133 301 GLU A OE2 2399 N N . CYS A 302 ? 1.0918 1.0288 0.7967 -0.0232 -0.1029 0.0121 302 CYS A N 2400 C CA . CYS A 302 ? 1.0241 1.0107 0.7815 -0.0382 -0.0934 0.0150 302 CYS A CA 2401 C C . CYS A 302 ? 0.9681 0.9829 0.7427 -0.0247 -0.0887 0.0095 302 CYS A C 2402 O O . CYS A 302 ? 0.9638 0.9788 0.7222 -0.0008 -0.0910 0.0013 302 CYS A O 2403 C CB . CYS A 302 ? 1.0112 1.0324 0.8031 -0.0420 -0.0882 0.0132 302 CYS A CB 2404 S SG . CYS A 302 ? 1.0585 1.0602 0.8438 -0.0620 -0.0921 0.0206 302 CYS A SG 2405 N N . PRO A 303 ? 0.9049 0.9468 0.7110 -0.0380 -0.0826 0.0132 303 PRO A N 2406 C CA . PRO A 303 ? 0.8841 0.9573 0.7109 -0.0278 -0.0775 0.0078 303 PRO A CA 2407 C C . PRO A 303 ? 0.8564 0.9657 0.7064 -0.0231 -0.0730 0.0013 303 PRO A C 2408 O O . PRO A 303 ? 0.8707 0.9806 0.7247 -0.0293 -0.0731 0.0020 303 PRO A O 2409 C CB . PRO A 303 ? 0.8647 0.9526 0.7141 -0.0435 -0.0730 0.0138 303 PRO A CB 2410 C CG . PRO A 303 ? 0.8779 0.9484 0.7169 -0.0614 -0.0761 0.0221 303 PRO A CG 2411 C CD . PRO A 303 ? 0.8893 0.9388 0.7112 -0.0605 -0.0808 0.0216 303 PRO A CD 2412 N N . LYS A 304 ? 0.8252 0.9646 0.6873 -0.0159 -0.0695 -0.0046 304 LYS A N 2413 C CA . LYS A 304 ? 0.8080 0.9845 0.6862 -0.0189 -0.0655 -0.0104 304 LYS A CA 2414 C C . LYS A 304 ? 0.7657 0.9459 0.6622 -0.0385 -0.0618 -0.0059 304 LYS A C 2415 O O . LYS A 304 ? 0.7682 0.9405 0.6711 -0.0427 -0.0607 -0.0018 304 LYS A O 2416 C CB . LYS A 304 ? 0.8433 1.0555 0.7229 -0.0071 -0.0640 -0.0187 304 LYS A CB 2417 C CG . LYS A 304 ? 0.9180 1.1232 0.7723 0.0204 -0.0697 -0.0246 304 LYS A CG 2418 C CD . LYS A 304 ? 0.9781 1.1852 0.8154 0.0349 -0.0732 -0.0298 304 LYS A CD 2419 C CE . LYS A 304 ? 1.0573 1.2120 0.8524 0.0572 -0.0824 -0.0298 304 LYS A CE 2420 N NZ . LYS A 304 ? 1.0964 1.2482 0.8696 0.0746 -0.0866 -0.0356 304 LYS A NZ 2421 N N . TYR A 305 ? 0.7317 0.9211 0.6314 -0.0487 -0.0606 -0.0071 305 TYR A N 2422 C CA . TYR A 305 ? 0.7034 0.8848 0.6080 -0.0642 -0.0595 -0.0037 305 TYR A CA 2423 C C . TYR A 305 ? 0.6960 0.8954 0.5993 -0.0736 -0.0570 -0.0075 305 TYR A C 2424 O O . TYR A 305 ? 0.6984 0.9292 0.5999 -0.0770 -0.0552 -0.0135 305 TYR A O 2425 C CB . TYR A 305 ? 0.7071 0.8811 0.6068 -0.0734 -0.0607 -0.0029 305 TYR A CB 2426 C CG . TYR A 305 ? 0.7049 0.8616 0.5981 -0.0864 -0.0618 -0.0004 305 TYR A CG 2427 C CD1 . TYR A 305 ? 0.7142 0.8488 0.6084 -0.0823 -0.0648 0.0046 305 TYR A CD1 2428 C CD2 . TYR A 305 ? 0.7060 0.8680 0.5857 -0.1028 -0.0610 -0.0036 305 TYR A CD2 2429 C CE1 . TYR A 305 ? 0.7325 0.8450 0.6116 -0.0870 -0.0680 0.0055 305 TYR A CE1 2430 C CE2 . TYR A 305 ? 0.7331 0.8639 0.5926 -0.1138 -0.0644 -0.0015 305 TYR A CE2 2431 C CZ . TYR A 305 ? 0.7389 0.8420 0.5969 -0.1023 -0.0684 0.0026 305 TYR A CZ 2432 O OH . TYR A 305 ? 0.7617 0.8279 0.5912 -0.1061 -0.0738 0.0034 305 TYR A OH 2433 N N . VAL A 306 ? 0.6943 0.8763 0.5954 -0.0779 -0.0574 -0.0045 306 VAL A N 2434 C CA . VAL A 306 ? 0.6958 0.8796 0.5846 -0.0918 -0.0570 -0.0069 306 VAL A CA 2435 C C . VAL A 306 ? 0.7248 0.8697 0.5949 -0.0980 -0.0608 -0.0034 306 VAL A C 2436 O O . VAL A 306 ? 0.7222 0.8500 0.5964 -0.0870 -0.0630 0.0002 306 VAL A O 2437 C CB . VAL A 306 ? 0.6916 0.8876 0.5854 -0.0856 -0.0553 -0.0086 306 VAL A CB 2438 C CG1 . VAL A 306 ? 0.6793 0.9140 0.5828 -0.0773 -0.0533 -0.0140 306 VAL A CG1 2439 C CG2 . VAL A 306 ? 0.6886 0.8663 0.5902 -0.0709 -0.0558 -0.0040 306 VAL A CG2 2440 N N . LYS A 307 ? 0.7707 0.9009 0.6145 -0.1156 -0.0627 -0.0050 307 LYS A N 2441 C CA . LYS A 307 ? 0.8358 0.9162 0.6470 -0.1183 -0.0689 -0.0028 307 LYS A CA 2442 C C . LYS A 307 ? 0.8427 0.9018 0.6447 -0.1037 -0.0712 -0.0022 307 LYS A C 2443 O O . LYS A 307 ? 0.9056 0.9189 0.6712 -0.1011 -0.0778 -0.0019 307 LYS A O 2444 C CB . LYS A 307 ? 0.8886 0.9483 0.6600 -0.1482 -0.0721 -0.0043 307 LYS A CB 2445 C CG . LYS A 307 ? 0.9162 0.9755 0.6824 -0.1600 -0.0727 -0.0038 307 LYS A CG 2446 C CD . LYS A 307 ? 0.9915 1.0240 0.7092 -0.1948 -0.0767 -0.0044 307 LYS A CD 2447 C CE . LYS A 307 ? 1.0337 1.0760 0.7491 -0.2092 -0.0758 -0.0043 307 LYS A CE 2448 N NZ . LYS A 307 ? 1.1169 1.1427 0.7834 -0.2509 -0.0787 -0.0048 307 LYS A NZ 2449 N N . SER A 308 ? 0.8006 0.8888 0.6298 -0.0922 -0.0666 -0.0025 308 SER A N 2450 C CA . SER A 308 ? 0.8047 0.8785 0.6254 -0.0797 -0.0678 -0.0026 308 SER A CA 2451 C C . SER A 308 ? 0.8032 0.8678 0.6281 -0.0561 -0.0702 -0.0005 308 SER A C 2452 O O . SER A 308 ? 0.7836 0.8666 0.6307 -0.0497 -0.0689 0.0017 308 SER A O 2453 C CB . SER A 308 ? 0.7646 0.8731 0.6108 -0.0763 -0.0622 -0.0036 308 SER A CB 2454 O OG . SER A 308 ? 0.7462 0.8793 0.5939 -0.0936 -0.0600 -0.0068 308 SER A OG 2455 N N . ASN A 309 ? 0.8466 0.8854 0.6469 -0.0431 -0.0742 -0.0018 309 ASN A N 2456 C CA . ASN A 309 ? 0.8584 0.9046 0.6644 -0.0164 -0.0758 -0.0016 309 ASN A CA 2457 C C . ASN A 309 ? 0.8215 0.9052 0.6570 -0.0082 -0.0695 -0.0007 309 ASN A C 2458 O O . ASN A 309 ? 0.8050 0.9166 0.6570 0.0075 -0.0683 0.0003 309 ASN A O 2459 C CB . ASN A 309 ? 0.9256 0.9224 0.6815 -0.0001 -0.0849 -0.0050 309 ASN A CB 2460 C CG . ASN A 309 ? 0.9891 0.9396 0.7062 -0.0057 -0.0933 -0.0056 309 ASN A CG 2461 O OD1 . ASN A 309 ? 0.9796 0.9453 0.7132 -0.0033 -0.0935 -0.0040 309 ASN A OD1 2462 N ND2 . ASN A 309 ? 1.0549 0.9444 0.7148 -0.0156 -0.1009 -0.0075 309 ASN A ND2 2463 N N . ARG A 310 ? 0.8104 0.8985 0.6505 -0.0206 -0.0657 -0.0012 310 ARG A N 2464 C CA . ARG A 310 ? 0.7996 0.9120 0.6574 -0.0136 -0.0608 -0.0008 310 ARG A CA 2465 C C . ARG A 310 ? 0.7406 0.8665 0.6107 -0.0286 -0.0568 -0.0012 310 ARG A C 2466 O O . ARG A 310 ? 0.7213 0.8334 0.5742 -0.0418 -0.0584 -0.0038 310 ARG A O 2467 C CB . ARG A 310 ? 0.8798 0.9692 0.7098 0.0016 -0.0642 -0.0037 310 ARG A CB 2468 C CG . ARG A 310 ? 0.9344 1.0532 0.7820 0.0141 -0.0594 -0.0032 310 ARG A CG 2469 C CD . ARG A 310 ? 1.0136 1.1059 0.8298 0.0286 -0.0627 -0.0070 310 ARG A CD 2470 N NE . ARG A 310 ? 1.0296 1.1487 0.8631 0.0323 -0.0569 -0.0064 310 ARG A NE 2471 C CZ . ARG A 310 ? 1.0501 1.2080 0.9022 0.0459 -0.0529 -0.0054 310 ARG A CZ 2472 N NH1 . ARG A 310 ? 1.0565 1.2388 0.9154 0.0585 -0.0541 -0.0054 310 ARG A NH1 2473 N NH2 . ARG A 310 ? 1.0399 1.2166 0.9026 0.0453 -0.0479 -0.0047 310 ARG A NH2 2474 N N . LEU A 311 ? 0.6841 0.8369 0.5788 -0.0272 -0.0526 0.0009 311 LEU A N 2475 C CA . LEU A 311 ? 0.6625 0.8280 0.5643 -0.0326 -0.0501 -0.0005 311 LEU A CA 2476 C C . LEU A 311 ? 0.6379 0.8154 0.5495 -0.0250 -0.0472 0.0019 311 LEU A C 2477 O O . LEU A 311 ? 0.6577 0.8427 0.5774 -0.0254 -0.0465 0.0054 311 LEU A O 2478 C CB . LEU A 311 ? 0.6466 0.8230 0.5560 -0.0392 -0.0503 -0.0014 311 LEU A CB 2479 C CG . LEU A 311 ? 0.6575 0.8325 0.5572 -0.0518 -0.0521 -0.0046 311 LEU A CG 2480 C CD1 . LEU A 311 ? 0.6541 0.8470 0.5629 -0.0523 -0.0518 -0.0060 311 LEU A CD1 2481 C CD2 . LEU A 311 ? 0.6679 0.8475 0.5550 -0.0618 -0.0525 -0.0086 311 LEU A CD2 2482 N N . VAL A 312 ? 0.6180 0.7939 0.5239 -0.0209 -0.0461 0.0003 312 VAL A N 2483 C CA . VAL A 312 ? 0.6024 0.7881 0.5132 -0.0156 -0.0433 0.0025 312 VAL A CA 2484 C C . VAL A 312 ? 0.5933 0.7790 0.5000 -0.0158 -0.0430 -0.0003 312 VAL A C 2485 O O . VAL A 312 ? 0.5842 0.7639 0.4818 -0.0176 -0.0442 -0.0038 312 VAL A O 2486 C CB . VAL A 312 ? 0.6081 0.7972 0.5150 -0.0056 -0.0420 0.0030 312 VAL A CB 2487 C CG1 . VAL A 312 ? 0.6037 0.8088 0.5151 -0.0039 -0.0383 0.0055 312 VAL A CG1 2488 C CG2 . VAL A 312 ? 0.6012 0.7979 0.5112 -0.0013 -0.0434 0.0046 312 VAL A CG2 2489 N N . LEU A 313 ? 0.5933 0.7822 0.5010 -0.0146 -0.0428 0.0010 313 LEU A N 2490 C CA . LEU A 313 ? 0.6028 0.7930 0.5044 -0.0105 -0.0437 -0.0022 313 LEU A CA 2491 C C . LEU A 313 ? 0.6074 0.7948 0.5048 -0.0075 -0.0412 0.0000 313 LEU A C 2492 O O . LEU A 313 ? 0.6285 0.8162 0.5256 -0.0099 -0.0391 0.0047 313 LEU A O 2493 C CB . LEU A 313 ? 0.6099 0.7960 0.5037 -0.0056 -0.0471 -0.0030 313 LEU A CB 2494 C CG . LEU A 313 ? 0.6165 0.8150 0.5126 -0.0037 -0.0499 -0.0080 313 LEU A CG 2495 C CD1 . LEU A 313 ? 0.6342 0.8193 0.5150 0.0059 -0.0544 -0.0083 313 LEU A CD1 2496 C CD2 . LEU A 313 ? 0.6180 0.8406 0.5156 -0.0022 -0.0507 -0.0149 313 LEU A CD2 2497 N N . ALA A 314 ? 0.6043 0.7931 0.4973 -0.0044 -0.0414 -0.0035 314 ALA A N 2498 C CA . ALA A 314 ? 0.6068 0.7923 0.4936 -0.0006 -0.0393 -0.0021 314 ALA A CA 2499 C C . ALA A 314 ? 0.6206 0.7975 0.4967 0.0018 -0.0418 -0.0009 314 ALA A C 2500 O O . ALA A 314 ? 0.6285 0.8059 0.4996 0.0077 -0.0461 -0.0051 314 ALA A O 2501 C CB . ALA A 314 ? 0.6066 0.7924 0.4880 0.0011 -0.0400 -0.0065 314 ALA A CB 2502 N N . THR A 315 ? 0.6315 0.8005 0.4986 -0.0024 -0.0399 0.0042 315 THR A N 2503 C CA . THR A 315 ? 0.6494 0.7961 0.4921 -0.0014 -0.0436 0.0057 315 THR A CA 2504 C C . THR A 315 ? 0.6438 0.7898 0.4795 -0.0003 -0.0411 0.0061 315 THR A C 2505 O O . THR A 315 ? 0.6673 0.7975 0.4852 0.0075 -0.0453 0.0036 315 THR A O 2506 C CB . THR A 315 ? 0.6686 0.7981 0.4936 -0.0149 -0.0447 0.0125 315 THR A CB 2507 O OG1 . THR A 315 ? 0.6609 0.8154 0.5004 -0.0272 -0.0382 0.0171 315 THR A OG1 2508 C CG2 . THR A 315 ? 0.6687 0.7879 0.4909 -0.0133 -0.0493 0.0117 315 THR A CG2 2509 N N . GLY A 316 ? 0.6316 0.7962 0.4792 -0.0054 -0.0349 0.0085 316 GLY A N 2510 C CA . GLY A 316 ? 0.6432 0.8107 0.4844 -0.0041 -0.0316 0.0088 316 GLY A CA 2511 C C . GLY A 316 ? 0.6377 0.8099 0.4867 0.0070 -0.0316 0.0030 316 GLY A C 2512 O O . GLY A 316 ? 0.6268 0.7980 0.4811 0.0109 -0.0352 -0.0013 316 GLY A O 2513 N N . LEU A 317 ? 0.6571 0.8355 0.5032 0.0099 -0.0277 0.0030 317 LEU A N 2514 C CA . LEU A 317 ? 0.6777 0.8520 0.5220 0.0182 -0.0287 -0.0019 317 LEU A CA 2515 C C . LEU A 317 ? 0.6846 0.8661 0.5298 0.0254 -0.0256 -0.0032 317 LEU A C 2516 O O . LEU A 317 ? 0.6678 0.8675 0.5188 0.0268 -0.0218 -0.0008 317 LEU A O 2517 C CB . LEU A 317 ? 0.6935 0.8587 0.5242 0.0205 -0.0293 -0.0025 317 LEU A CB 2518 C CG . LEU A 317 ? 0.7102 0.8764 0.5301 0.0153 -0.0252 0.0023 317 LEU A CG 2519 C CD1 . LEU A 317 ? 0.7214 0.9084 0.5454 0.0193 -0.0187 0.0026 317 LEU A CD1 2520 C CD2 . LEU A 317 ? 0.7306 0.8778 0.5317 0.0174 -0.0285 0.0015 317 LEU A CD2 2521 N N . ARG A 318 ? 0.7167 0.8832 0.5511 0.0303 -0.0285 -0.0076 318 ARG A N 2522 C CA . ARG A 318 ? 0.7560 0.9142 0.5771 0.0419 -0.0284 -0.0101 318 ARG A CA 2523 C C . ARG A 318 ? 0.7755 0.9545 0.5960 0.0529 -0.0225 -0.0089 318 ARG A C 2524 O O . ARG A 318 ? 0.7684 0.9489 0.5839 0.0527 -0.0202 -0.0085 318 ARG A O 2525 C CB . ARG A 318 ? 0.8003 0.9289 0.5975 0.0414 -0.0336 -0.0143 318 ARG A CB 2526 C CG . ARG A 318 ? 0.8603 0.9623 0.6280 0.0554 -0.0367 -0.0176 318 ARG A CG 2527 C CD . ARG A 318 ? 0.9141 0.9779 0.6484 0.0486 -0.0433 -0.0209 318 ARG A CD 2528 N NE . ARG A 318 ? 0.9400 0.9919 0.6690 0.0270 -0.0489 -0.0213 318 ARG A NE 2529 C CZ . ARG A 318 ? 0.9918 1.0103 0.6922 0.0221 -0.0550 -0.0226 318 ARG A CZ 2530 N NH1 . ARG A 318 ? 1.0356 1.0233 0.7064 0.0427 -0.0578 -0.0244 318 ARG A NH1 2531 N NH2 . ARG A 318 ? 0.9991 1.0158 0.6961 -0.0026 -0.0591 -0.0227 318 ARG A NH2 2532 N N . ASN A 319 ? 0.8033 1.0036 0.6286 0.0624 -0.0203 -0.0088 319 ASN A N 2533 C CA . ASN A 319 ? 0.8262 1.0640 0.6539 0.0722 -0.0141 -0.0084 319 ASN A CA 2534 C C . ASN A 319 ? 0.9287 1.1561 0.7318 0.0973 -0.0154 -0.0145 319 ASN A C 2535 O O . ASN A 319 ? 0.9651 1.1607 0.7468 0.1117 -0.0218 -0.0190 319 ASN A O 2536 C CB . ASN A 319 ? 0.7909 1.0665 0.6340 0.0729 -0.0118 -0.0068 319 ASN A CB 2537 C CG . ASN A 319 ? 0.7665 1.0985 0.6173 0.0728 -0.0044 -0.0051 319 ASN A CG 2538 O OD1 . ASN A 319 ? 0.7627 1.1028 0.6073 0.0698 -0.0004 -0.0044 319 ASN A OD1 2539 N ND2 . ASN A 319 ? 0.7469 1.1232 0.6104 0.0739 -0.0025 -0.0045 319 ASN A ND2 2540 N N . SER A 320 ? 1.0536 1.3031 0.8535 0.1024 -0.0101 -0.0148 320 SER A N 2541 C CA . SER A 320 ? 1.1562 1.3952 0.9286 0.1290 -0.0113 -0.0211 320 SER A CA 2542 C C . SER A 320 ? 1.2446 1.5185 1.0102 0.1587 -0.0109 -0.0264 320 SER A C 2543 O O . SER A 320 ? 1.2100 1.5416 1.0001 0.1540 -0.0055 -0.0241 320 SER A O 2544 C CB . SER A 320 ? 1.1508 1.4077 0.9229 0.1249 -0.0052 -0.0198 320 SER A CB 2545 O OG . SER A 320 ? 1.1704 1.3997 0.9477 0.1009 -0.0064 -0.0154 320 SER A OG 2546 N N . PRO A 321 ? 1.3681 1.6063 1.0947 0.1901 -0.0177 -0.0340 321 PRO A N 2547 C CA . PRO A 321 ? 1.4245 1.6912 1.1359 0.2274 -0.0198 -0.0412 321 PRO A CA 2548 C C . PRO A 321 ? 1.4009 1.7497 1.1266 0.2432 -0.0105 -0.0439 321 PRO A C 2549 O O . PRO A 321 ? 1.3790 1.7340 1.1010 0.2404 -0.0057 -0.0436 321 PRO A O 2550 C CB . PRO A 321 ? 1.4937 1.6828 1.1451 0.2563 -0.0315 -0.0486 321 PRO A CB 2551 C CG . PRO A 321 ? 1.4834 1.6081 1.1244 0.2256 -0.0353 -0.0441 321 PRO A CG 2552 C CD . PRO A 321 ? 1.4209 1.5888 1.1086 0.1935 -0.0250 -0.0368 321 PRO A CD 2553 N N . GLY B 1 ? 0.6659 0.5855 0.6428 0.0067 0.1462 0.0358 1 GLY B N 2554 C CA . GLY B 1 ? 0.6321 0.5863 0.6239 0.0029 0.1213 0.0352 1 GLY B CA 2555 C C . GLY B 1 ? 0.6287 0.5899 0.6112 -0.0202 0.1158 0.0231 1 GLY B C 2556 O O . GLY B 1 ? 0.6864 0.6354 0.6539 -0.0383 0.1257 0.0135 1 GLY B O 2557 N N . LEU B 2 ? 0.6034 0.5900 0.5942 -0.0195 0.1001 0.0236 2 LEU B N 2558 C CA . LEU B 2 ? 0.5983 0.6040 0.5812 -0.0382 0.0952 0.0149 2 LEU B CA 2559 C C . LEU B 2 ? 0.5970 0.6200 0.5765 -0.0512 0.0883 0.0091 2 LEU B C 2560 O O . LEU B 2 ? 0.6222 0.6587 0.5893 -0.0727 0.0926 0.0007 2 LEU B O 2561 C CB . LEU B 2 ? 0.5676 0.6031 0.5618 -0.0280 0.0787 0.0185 2 LEU B CB 2562 C CG . LEU B 2 ? 0.5587 0.5890 0.5516 -0.0246 0.0857 0.0214 2 LEU B CG 2563 C CD1 . LEU B 2 ? 0.5282 0.5912 0.5327 -0.0124 0.0686 0.0241 2 LEU B CD1 2564 C CD2 . LEU B 2 ? 0.5740 0.5937 0.5466 -0.0494 0.1022 0.0136 2 LEU B CD2 2565 N N . PHE B 3 ? 0.5850 0.6114 0.5741 -0.0406 0.0781 0.0140 3 PHE B N 2566 C CA . PHE B 3 ? 0.5993 0.6456 0.5860 -0.0495 0.0689 0.0120 3 PHE B CA 2567 C C . PHE B 3 ? 0.6319 0.6632 0.6103 -0.0615 0.0804 0.0074 3 PHE B C 2568 O O . PHE B 3 ? 0.6478 0.6969 0.6230 -0.0711 0.0745 0.0060 3 PHE B O 2569 C CB . PHE B 3 ? 0.5840 0.6422 0.5807 -0.0325 0.0497 0.0205 3 PHE B CB 2570 C CG . PHE B 3 ? 0.5781 0.6537 0.5785 -0.0214 0.0400 0.0228 3 PHE B CG 2571 C CD1 . PHE B 3 ? 0.5662 0.6744 0.5623 -0.0235 0.0331 0.0228 3 PHE B CD1 2572 C CD2 . PHE B 3 ? 0.5758 0.6418 0.5833 -0.0086 0.0391 0.0254 3 PHE B CD2 2573 C CE1 . PHE B 3 ? 0.5712 0.6997 0.5701 -0.0107 0.0259 0.0252 3 PHE B CE1 2574 C CE2 . PHE B 3 ? 0.5745 0.6579 0.5842 0.0013 0.0316 0.0263 3 PHE B CE2 2575 C CZ . PHE B 3 ? 0.5609 0.6746 0.5663 0.0013 0.0252 0.0259 3 PHE B CZ 2576 N N . GLY B 4 ? 0.6618 0.6615 0.6354 -0.0591 0.0981 0.0059 4 GLY B N 2577 C CA . GLY B 4 ? 0.6685 0.6484 0.6288 -0.0706 0.1152 -0.0010 4 GLY B CA 2578 C C . GLY B 4 ? 0.6656 0.6487 0.6339 -0.0617 0.1113 0.0042 4 GLY B C 2579 O O . GLY B 4 ? 0.7076 0.6732 0.6656 -0.0662 0.1275 -0.0007 4 GLY B O 2580 N N . ALA B 5 ? 0.6344 0.6377 0.6178 -0.0507 0.0917 0.0135 5 ALA B N 2581 C CA . ALA B 5 ? 0.6255 0.6363 0.6137 -0.0486 0.0871 0.0182 5 ALA B CA 2582 C C . ALA B 5 ? 0.6281 0.6324 0.6235 -0.0321 0.0960 0.0252 5 ALA B C 2583 O O . ALA B 5 ? 0.6295 0.6262 0.6196 -0.0308 0.1113 0.0236 5 ALA B O 2584 C CB . ALA B 5 ? 0.6111 0.6395 0.6052 -0.0475 0.0652 0.0250 5 ALA B CB 2585 N N . ILE B 6 ? 0.6150 0.6267 0.6214 -0.0187 0.0872 0.0333 6 ILE B N 2586 C CA . ILE B 6 ? 0.6114 0.6325 0.6266 -0.0024 0.0929 0.0429 6 ILE B CA 2587 C C . ILE B 6 ? 0.6417 0.6410 0.6502 0.0103 0.1171 0.0438 6 ILE B C 2588 O O . ILE B 6 ? 0.6671 0.6457 0.6693 0.0113 0.1242 0.0410 6 ILE B O 2589 C CB . ILE B 6 ? 0.5931 0.6297 0.6186 0.0055 0.0790 0.0498 6 ILE B CB 2590 C CG1 . ILE B 6 ? 0.5905 0.6380 0.6157 -0.0061 0.0592 0.0494 6 ILE B CG1 2591 C CG2 . ILE B 6 ? 0.5947 0.6513 0.6292 0.0225 0.0867 0.0611 6 ILE B CG2 2592 C CD1 . ILE B 6 ? 0.5885 0.6430 0.6171 -0.0025 0.0468 0.0521 6 ILE B CD1 2593 N N . ALA B 7 ? 0.6710 0.6733 0.6783 0.0208 0.1312 0.0483 7 ALA B N 2594 C CA . ALA B 7 ? 0.7147 0.6867 0.7094 0.0372 0.1590 0.0501 7 ALA B CA 2595 C C . ALA B 7 ? 0.7630 0.6904 0.7353 0.0201 0.1729 0.0352 7 ALA B C 2596 O O . ALA B 7 ? 0.8151 0.7062 0.7729 0.0277 0.1920 0.0354 7 ALA B O 2597 C CB . ALA B 7 ? 0.7170 0.6940 0.7191 0.0612 0.1637 0.0644 7 ALA B CB 2598 N N . GLY B 8 ? 0.7661 0.6986 0.7334 -0.0049 0.1637 0.0228 8 GLY B N 2599 C CA . GLY B 8 ? 0.7927 0.6967 0.7379 -0.0284 0.1749 0.0071 8 GLY B CA 2600 C C . GLY B 8 ? 0.8067 0.7136 0.7417 -0.0443 0.1801 -0.0030 8 GLY B C 2601 O O . GLY B 8 ? 0.8288 0.7152 0.7527 -0.0346 0.2008 -0.0043 8 GLY B O 2602 N N . PHE B 9 ? 0.7791 0.7138 0.7172 -0.0662 0.1621 -0.0089 9 PHE B N 2603 C CA . PHE B 9 ? 0.7965 0.7421 0.7268 -0.0818 0.1646 -0.0167 9 PHE B CA 2604 C C . PHE B 9 ? 0.7909 0.7632 0.7385 -0.0679 0.1537 -0.0052 9 PHE B C 2605 O O . PHE B 9 ? 0.8358 0.8146 0.7773 -0.0744 0.1605 -0.0095 9 PHE B O 2606 C CB . PHE B 9 ? 0.7939 0.7640 0.7180 -0.1101 0.1524 -0.0254 9 PHE B CB 2607 C CG . PHE B 9 ? 0.7504 0.7580 0.6935 -0.1066 0.1238 -0.0138 9 PHE B CG 2608 C CD1 . PHE B 9 ? 0.7554 0.7872 0.7059 -0.1077 0.1105 -0.0072 9 PHE B CD1 2609 C CD2 . PHE B 9 ? 0.7394 0.7551 0.6889 -0.1029 0.1119 -0.0098 9 PHE B CD2 2610 C CE1 . PHE B 9 ? 0.7333 0.7876 0.6943 -0.1036 0.0877 0.0039 9 PHE B CE1 2611 C CE2 . PHE B 9 ? 0.7154 0.7575 0.6771 -0.0964 0.0889 0.0005 9 PHE B CE2 2612 C CZ . PHE B 9 ? 0.7148 0.7720 0.6805 -0.0964 0.0777 0.0076 9 PHE B CZ 2613 N N . ILE B 10 ? 0.7656 0.7547 0.7323 -0.0515 0.1380 0.0084 10 ILE B N 2614 C CA . ILE B 10 ? 0.7419 0.7573 0.7223 -0.0401 0.1306 0.0196 10 ILE B CA 2615 C C . ILE B 10 ? 0.7783 0.7885 0.7635 -0.0134 0.1458 0.0285 10 ILE B C 2616 O O . ILE B 10 ? 0.7781 0.7934 0.7735 -0.0012 0.1389 0.0370 10 ILE B O 2617 C CB . ILE B 10 ? 0.6979 0.7369 0.6910 -0.0441 0.1040 0.0282 10 ILE B CB 2618 C CG1 . ILE B 10 ? 0.6899 0.7336 0.6763 -0.0640 0.0910 0.0234 10 ILE B CG1 2619 C CG2 . ILE B 10 ? 0.6860 0.7533 0.6884 -0.0398 0.0976 0.0382 10 ILE B CG2 2620 C CD1 . ILE B 10 ? 0.6774 0.7292 0.6688 -0.0647 0.0689 0.0315 10 ILE B CD1 2621 N N . GLU B 11 ? 0.8309 0.8332 0.8072 -0.0028 0.1674 0.0273 11 GLU B N 2622 C CA . GLU B 11 ? 0.8818 0.8750 0.8574 0.0280 0.1882 0.0373 11 GLU B CA 2623 C C . GLU B 11 ? 0.8407 0.8745 0.8377 0.0463 0.1754 0.0550 11 GLU B C 2624 O O . GLU B 11 ? 0.8568 0.8807 0.8550 0.0675 0.1847 0.0640 11 GLU B O 2625 C CB . GLU B 11 ? 0.9740 0.9690 0.9403 0.0402 0.2094 0.0367 11 GLU B CB 2626 C CG . GLU B 11 ? 1.0654 1.0098 1.0029 0.0284 0.2330 0.0186 11 GLU B CG 2627 C CD . GLU B 11 ? 1.1628 1.1069 1.0895 0.0465 0.2569 0.0187 11 GLU B CD 2628 O OE1 . GLU B 11 ? 1.1423 1.1343 1.0819 0.0420 0.2454 0.0220 11 GLU B OE1 2629 O OE2 . GLU B 11 ? 1.2787 1.1724 1.1815 0.0658 0.2886 0.0159 11 GLU B OE2 2630 N N . GLY B 12 ? 0.7964 0.8765 0.8074 0.0361 0.1555 0.0602 12 GLY B N 2631 C CA . GLY B 12 ? 0.7601 0.8873 0.7881 0.0468 0.1440 0.0752 12 GLY B CA 2632 C C . GLY B 12 ? 0.7228 0.8816 0.7579 0.0216 0.1180 0.0752 12 GLY B C 2633 O O . GLY B 12 ? 0.7282 0.8769 0.7565 -0.0002 0.1093 0.0667 12 GLY B O 2634 N N . GLY B 13 ? 0.6890 0.8850 0.7347 0.0239 0.1071 0.0853 13 GLY B N 2635 C CA . GLY B 13 ? 0.6629 0.8829 0.7091 -0.0018 0.0855 0.0851 13 GLY B CA 2636 C C . GLY B 13 ? 0.6555 0.9222 0.7027 -0.0120 0.0847 0.0903 13 GLY B C 2637 O O . GLY B 13 ? 0.6611 0.9452 0.7107 0.0036 0.1008 0.0939 13 GLY B O 2638 N N . TRP B 14 ? 0.6297 0.9149 0.6722 -0.0390 0.0673 0.0904 14 TRP B N 2639 C CA . TRP B 14 ? 0.6030 0.9318 0.6428 -0.0576 0.0638 0.0943 14 TRP B CA 2640 C C . TRP B 14 ? 0.6081 0.9943 0.6501 -0.0712 0.0553 0.1022 14 TRP B C 2641 O O . TRP B 14 ? 0.5915 0.9623 0.6217 -0.0960 0.0412 0.0978 14 TRP B O 2642 C CB . TRP B 14 ? 0.5976 0.8904 0.6213 -0.0865 0.0518 0.0865 14 TRP B CB 2643 C CG . TRP B 14 ? 0.5861 0.8417 0.6064 -0.0804 0.0592 0.0794 14 TRP B CG 2644 C CD1 . TRP B 14 ? 0.5851 0.8442 0.6112 -0.0599 0.0772 0.0779 14 TRP B CD1 2645 C CD2 . TRP B 14 ? 0.5841 0.7965 0.5910 -0.0965 0.0500 0.0730 14 TRP B CD2 2646 N NE1 . TRP B 14 ? 0.5940 0.8163 0.6110 -0.0669 0.0792 0.0687 14 TRP B NE1 2647 C CE2 . TRP B 14 ? 0.5824 0.7815 0.5895 -0.0882 0.0618 0.0670 14 TRP B CE2 2648 C CE3 . TRP B 14 ? 0.5931 0.7760 0.5852 -0.1157 0.0347 0.0726 14 TRP B CE3 2649 C CZ2 . TRP B 14 ? 0.5850 0.7545 0.5816 -0.0997 0.0567 0.0616 14 TRP B CZ2 2650 C CZ3 . TRP B 14 ? 0.5939 0.7431 0.5755 -0.1214 0.0307 0.0695 14 TRP B CZ3 2651 C CH2 . TRP B 14 ? 0.5863 0.7349 0.5717 -0.1142 0.0407 0.0646 14 TRP B CH2 2652 N N . GLN B 15 ? 0.6330 1.0874 0.6875 -0.0553 0.0654 0.1139 15 GLN B N 2653 C CA . GLN B 15 ? 0.6444 1.1742 0.7008 -0.0726 0.0582 0.1225 15 GLN B CA 2654 C C . GLN B 15 ? 0.6484 1.1805 0.6859 -0.1195 0.0439 0.1163 15 GLN B C 2655 O O . GLN B 15 ? 0.6576 1.2165 0.6848 -0.1490 0.0333 0.1157 15 GLN B O 2656 C CB . GLN B 15 ? 0.6620 1.2735 0.7343 -0.0454 0.0731 0.1382 15 GLN B CB 2657 C CG . GLN B 15 ? 0.6776 1.2934 0.7642 0.0027 0.0899 0.1491 15 GLN B CG 2658 C CD . GLN B 15 ? 0.6969 1.3692 0.7919 0.0064 0.0848 0.1601 15 GLN B CD 2659 O OE1 . GLN B 15 ? 0.7081 1.4648 0.8054 -0.0122 0.0779 0.1681 15 GLN B OE1 2660 N NE2 . GLN B 15 ? 0.6950 1.3262 0.7934 0.0284 0.0886 0.1607 15 GLN B NE2 2661 N N . GLY B 16 ? 0.6496 1.1520 0.6795 -0.1280 0.0449 0.1115 16 GLY B N 2662 C CA . GLY B 16 ? 0.6679 1.1683 0.6774 -0.1707 0.0338 0.1080 16 GLY B CA 2663 C C . GLY B 16 ? 0.6880 1.1115 0.6727 -0.1973 0.0211 0.0983 16 GLY B C 2664 O O . GLY B 16 ? 0.7116 1.1250 0.6735 -0.2336 0.0135 0.0967 16 GLY B O 2665 N N . MET B 17 ? 0.6837 1.0516 0.6702 -0.1785 0.0202 0.0928 17 MET B N 2666 C CA . MET B 17 ? 0.7038 1.0028 0.6661 -0.1972 0.0100 0.0852 17 MET B CA 2667 C C . MET B 17 ? 0.7004 1.0078 0.6566 -0.2065 0.0053 0.0824 17 MET B C 2668 O O . MET B 17 ? 0.6620 0.9582 0.6304 -0.1823 0.0071 0.0807 17 MET B O 2669 C CB . MET B 17 ? 0.7071 0.9433 0.6725 -0.1731 0.0113 0.0807 17 MET B CB 2670 C CG . MET B 17 ? 0.7420 0.9094 0.6804 -0.1876 0.0025 0.0758 17 MET B CG 2671 S SD . MET B 17 ? 0.7675 0.8835 0.7112 -0.1602 0.0040 0.0733 17 MET B SD 2672 C CE . MET B 17 ? 0.7540 0.8839 0.7224 -0.1297 0.0099 0.0702 17 MET B CE 2673 N N . VAL B 18 ? 0.7287 1.0551 0.6625 -0.2454 0.0000 0.0811 18 VAL B N 2674 C CA . VAL B 18 ? 0.7481 1.1026 0.6740 -0.2626 -0.0032 0.0778 18 VAL B CA 2675 C C . VAL B 18 ? 0.7928 1.0673 0.6842 -0.2831 -0.0086 0.0662 18 VAL B C 2676 O O . VAL B 18 ? 0.8161 1.0950 0.7028 -0.2868 -0.0100 0.0605 18 VAL B O 2677 C CB . VAL B 18 ? 0.7661 1.2008 0.6843 -0.2991 -0.0042 0.0821 18 VAL B CB 2678 C CG1 . VAL B 18 ? 0.8099 1.2877 0.7207 -0.3190 -0.0070 0.0786 18 VAL B CG1 2679 C CG2 . VAL B 18 ? 0.7316 1.2477 0.6819 -0.2747 0.0029 0.0950 18 VAL B CG2 2680 N N . ASP B 19 ? 0.8211 1.0227 0.6867 -0.2941 -0.0103 0.0634 19 ASP B N 2681 C CA . ASP B 19 ? 0.8718 0.9910 0.6963 -0.3139 -0.0123 0.0539 19 ASP B CA 2682 C C . ASP B 19 ? 0.8520 0.9046 0.6800 -0.2773 -0.0121 0.0512 19 ASP B C 2683 O O . ASP B 19 ? 0.8921 0.8676 0.6859 -0.2835 -0.0117 0.0462 19 ASP B O 2684 C CB . ASP B 19 ? 0.9366 1.0120 0.7222 -0.3496 -0.0122 0.0550 19 ASP B CB 2685 C CG . ASP B 19 ? 0.9307 0.9905 0.7282 -0.3299 -0.0120 0.0645 19 ASP B CG 2686 O OD1 . ASP B 19 ? 0.8752 0.9750 0.7120 -0.2963 -0.0109 0.0692 19 ASP B OD1 2687 O OD2 . ASP B 19 ? 0.9913 0.9970 0.7553 -0.3499 -0.0117 0.0672 19 ASP B OD2 2688 N N . GLY B 20 ? 0.7909 0.8729 0.6573 -0.2392 -0.0109 0.0548 20 GLY B N 2689 C CA . GLY B 20 ? 0.7852 0.8177 0.6565 -0.2074 -0.0109 0.0522 20 GLY B CA 2690 C C . GLY B 20 ? 0.7439 0.8158 0.6548 -0.1727 -0.0078 0.0555 20 GLY B C 2691 O O . GLY B 20 ? 0.7393 0.8698 0.6735 -0.1681 -0.0040 0.0613 20 GLY B O 2692 N N . TRP B 21 ? 0.7341 0.7721 0.6495 -0.1480 -0.0079 0.0523 21 TRP B N 2693 C CA . TRP B 21 ? 0.6981 0.7621 0.6449 -0.1181 -0.0035 0.0546 21 TRP B CA 2694 C C . TRP B 21 ? 0.6630 0.7187 0.6205 -0.1039 0.0001 0.0580 21 TRP B C 2695 O O . TRP B 21 ? 0.6316 0.7172 0.6110 -0.0893 0.0075 0.0608 21 TRP B O 2696 C CB . TRP B 21 ? 0.7158 0.7553 0.6622 -0.1015 -0.0050 0.0492 21 TRP B CB 2697 C CG . TRP B 21 ? 0.7242 0.7978 0.6769 -0.1039 -0.0050 0.0472 21 TRP B CG 2698 C CD1 . TRP B 21 ? 0.7103 0.8457 0.6819 -0.1042 -0.0014 0.0536 21 TRP B CD1 2699 C CD2 . TRP B 21 ? 0.7519 0.8049 0.6922 -0.1037 -0.0080 0.0396 21 TRP B CD2 2700 N NE1 . TRP B 21 ? 0.7069 0.8651 0.6789 -0.1061 -0.0030 0.0513 21 TRP B NE1 2701 C CE2 . TRP B 21 ? 0.7383 0.8451 0.6909 -0.1074 -0.0070 0.0413 21 TRP B CE2 2702 C CE3 . TRP B 21 ? 0.7935 0.7901 0.7122 -0.0985 -0.0104 0.0322 21 TRP B CE3 2703 C CZ2 . TRP B 21 ? 0.7592 0.8651 0.7033 -0.1102 -0.0091 0.0341 21 TRP B CZ2 2704 C CZ3 . TRP B 21 ? 0.8140 0.8052 0.7233 -0.0991 -0.0113 0.0243 21 TRP B CZ3 2705 C CH2 . TRP B 21 ? 0.7950 0.8405 0.7170 -0.1069 -0.0111 0.0244 21 TRP B CH2 2706 N N . TYR B 22 ? 0.6694 0.6832 0.6085 -0.1077 -0.0036 0.0579 22 TYR B N 2707 C CA . TYR B 22 ? 0.6414 0.6519 0.5872 -0.0988 -0.0011 0.0608 22 TYR B CA 2708 C C . TYR B 22 ? 0.6641 0.6595 0.5898 -0.1181 -0.0042 0.0656 22 TYR B C 2709 O O . TYR B 22 ? 0.6851 0.6497 0.5848 -0.1341 -0.0083 0.0663 22 TYR B O 2710 C CB . TYR B 22 ? 0.6310 0.6142 0.5751 -0.0798 -0.0026 0.0593 22 TYR B CB 2711 C CG . TYR B 22 ? 0.6196 0.5986 0.5689 -0.0662 -0.0032 0.0546 22 TYR B CG 2712 C CD1 . TYR B 22 ? 0.5886 0.5969 0.5603 -0.0554 0.0025 0.0526 22 TYR B CD1 2713 C CD2 . TYR B 22 ? 0.6416 0.5843 0.5706 -0.0629 -0.0079 0.0527 22 TYR B CD2 2714 C CE1 . TYR B 22 ? 0.5773 0.5844 0.5535 -0.0439 0.0018 0.0493 22 TYR B CE1 2715 C CE2 . TYR B 22 ? 0.6295 0.5716 0.5630 -0.0508 -0.0082 0.0477 22 TYR B CE2 2716 C CZ . TYR B 22 ? 0.5903 0.5675 0.5486 -0.0425 -0.0042 0.0462 22 TYR B CZ 2717 O OH . TYR B 22 ? 0.5726 0.5519 0.5352 -0.0315 -0.0047 0.0422 22 TYR B OH 2718 N N . GLY B 23 ? 0.6621 0.6754 0.5966 -0.1181 -0.0008 0.0684 23 GLY B N 2719 C CA . GLY B 23 ? 0.6905 0.6946 0.6073 -0.1363 -0.0035 0.0744 23 GLY B CA 2720 C C . GLY B 23 ? 0.6786 0.7109 0.6077 -0.1361 0.0013 0.0758 23 GLY B C 2721 O O . GLY B 23 ? 0.6410 0.6882 0.5876 -0.1208 0.0075 0.0712 23 GLY B O 2722 N N . TYR B 24 ? 0.7168 0.7544 0.6332 -0.1561 -0.0003 0.0813 24 TYR B N 2723 C CA . TYR B 24 ? 0.7067 0.7661 0.6277 -0.1597 0.0032 0.0834 24 TYR B CA 2724 C C . TYR B 24 ? 0.6918 0.7936 0.6200 -0.1745 0.0078 0.0834 24 TYR B C 2725 O O . TYR B 24 ? 0.7024 0.8110 0.6209 -0.1923 0.0044 0.0863 24 TYR B O 2726 C CB . TYR B 24 ? 0.7454 0.7755 0.6419 -0.1695 -0.0030 0.0933 24 TYR B CB 2727 C CG . TYR B 24 ? 0.7857 0.7736 0.6690 -0.1530 -0.0075 0.0972 24 TYR B CG 2728 C CD1 . TYR B 24 ? 0.7819 0.7779 0.6737 -0.1352 -0.0068 0.0977 24 TYR B CD1 2729 C CD2 . TYR B 24 ? 0.8235 0.7659 0.6835 -0.1557 -0.0111 0.1001 24 TYR B CD2 2730 C CE1 . TYR B 24 ? 0.8127 0.7802 0.6935 -0.1167 -0.0105 0.1031 24 TYR B CE1 2731 C CE2 . TYR B 24 ? 0.8533 0.7567 0.6996 -0.1357 -0.0132 0.1043 24 TYR B CE2 2732 C CZ . TYR B 24 ? 0.8443 0.7642 0.7028 -0.1143 -0.0133 0.1069 24 TYR B CZ 2733 O OH . TYR B 24 ? 0.8967 0.7883 0.7428 -0.0912 -0.0149 0.1129 24 TYR B OH 2734 N N . HIS B 25 ? 0.6834 0.8155 0.6261 -0.1684 0.0166 0.0797 25 HIS B N 2735 C CA . HIS B 25 ? 0.6840 0.8586 0.6303 -0.1811 0.0217 0.0814 25 HIS B CA 2736 C C . HIS B 25 ? 0.6925 0.8720 0.6324 -0.1895 0.0231 0.0824 25 HIS B C 2737 O O . HIS B 25 ? 0.6759 0.8480 0.6204 -0.1783 0.0281 0.0766 25 HIS B O 2738 C CB . HIS B 25 ? 0.6643 0.8744 0.6316 -0.1628 0.0351 0.0760 25 HIS B CB 2739 C CG . HIS B 25 ? 0.6631 0.9233 0.6348 -0.1705 0.0421 0.0786 25 HIS B CG 2740 N ND1 . HIS B 25 ? 0.6608 0.9365 0.6357 -0.1658 0.0534 0.0739 25 HIS B ND1 2741 C CD2 . HIS B 25 ? 0.6779 0.9808 0.6496 -0.1840 0.0397 0.0851 25 HIS B CD2 2742 C CE1 . HIS B 25 ? 0.6672 0.9923 0.6454 -0.1722 0.0581 0.0780 25 HIS B CE1 2743 N NE2 . HIS B 25 ? 0.6748 1.0210 0.6520 -0.1838 0.0494 0.0855 25 HIS B NE2 2744 N N . HIS B 26 ? 0.7368 0.9324 0.6646 -0.2122 0.0191 0.0895 26 HIS B N 2745 C CA . HIS B 26 ? 0.7563 0.9607 0.6763 -0.2226 0.0194 0.0923 26 HIS B CA 2746 C C . HIS B 26 ? 0.7534 1.0096 0.6808 -0.2317 0.0278 0.0903 26 HIS B C 2747 O O . HIS B 26 ? 0.7595 1.0466 0.6930 -0.2354 0.0302 0.0913 26 HIS B O 2748 C CB . HIS B 26 ? 0.7940 0.9654 0.6876 -0.2406 0.0079 0.1054 26 HIS B CB 2749 C CG . HIS B 26 ? 0.8257 1.0050 0.7036 -0.2676 0.0038 0.1126 26 HIS B CG 2750 N ND1 . HIS B 26 ? 0.8561 1.0190 0.7255 -0.2761 0.0003 0.1127 26 HIS B ND1 2751 C CD2 . HIS B 26 ? 0.8380 1.0427 0.7048 -0.2920 0.0032 0.1193 26 HIS B CD2 2752 C CE1 . HIS B 26 ? 0.8710 1.0489 0.7232 -0.3069 -0.0019 0.1186 26 HIS B CE1 2753 N NE2 . HIS B 26 ? 0.8638 1.0669 0.7146 -0.3164 -0.0005 0.1233 26 HIS B NE2 2754 N N . SER B 27 ? 0.7547 1.0255 0.6808 -0.2350 0.0327 0.0876 27 SER B N 2755 C CA . SER B 27 ? 0.7523 1.0715 0.6829 -0.2428 0.0418 0.0849 27 SER B CA 2756 C C . SER B 27 ? 0.7646 1.0902 0.6819 -0.2603 0.0383 0.0891 27 SER B C 2757 O O . SER B 27 ? 0.7590 1.0738 0.6753 -0.2543 0.0412 0.0835 27 SER B O 2758 C CB . SER B 27 ? 0.7449 1.0787 0.6907 -0.2196 0.0603 0.0706 27 SER B CB 2759 O OG . SER B 27 ? 0.7567 1.1221 0.7144 -0.2082 0.0680 0.0714 27 SER B OG 2760 N N . ASN B 28 ? 0.7722 1.1198 0.6782 -0.2839 0.0324 0.0996 28 ASN B N 2761 C CA . ASN B 28 ? 0.7898 1.1493 0.6824 -0.3016 0.0291 0.1063 28 ASN B CA 2762 C C . ASN B 28 ? 0.8167 1.2258 0.7061 -0.3231 0.0312 0.1105 28 ASN B C 2763 O O . ASN B 28 ? 0.7992 1.2381 0.6980 -0.3224 0.0355 0.1080 28 ASN B O 2764 C CB . ASN B 28 ? 0.7984 1.1113 0.6693 -0.3098 0.0155 0.1221 28 ASN B CB 2765 C CG . ASN B 28 ? 0.8084 1.0959 0.6611 -0.3278 0.0071 0.1341 28 ASN B CG 2766 O OD1 . ASN B 28 ? 0.7992 1.1155 0.6561 -0.3398 0.0093 0.1315 28 ASN B OD1 2767 N ND2 . ASN B 28 ? 0.8332 1.0672 0.6624 -0.3302 -0.0012 0.1476 28 ASN B ND2 2768 N N . GLU B 29 ? 0.8575 1.2824 0.7339 -0.3419 0.0281 0.1179 29 GLU B N 2769 C CA . GLU B 29 ? 0.8962 1.3731 0.7689 -0.3642 0.0301 0.1221 29 GLU B CA 2770 C C . GLU B 29 ? 0.9037 1.3834 0.7681 -0.3826 0.0234 0.1312 29 GLU B C 2771 O O . GLU B 29 ? 0.8946 1.4288 0.7688 -0.3874 0.0293 0.1281 29 GLU B O 2772 C CB . GLU B 29 ? 0.9596 1.4439 0.8140 -0.3859 0.0245 0.1337 29 GLU B CB 2773 C CG . GLU B 29 ? 0.9754 1.4757 0.8363 -0.3753 0.0321 0.1234 29 GLU B CG 2774 C CD . GLU B 29 ? 1.0037 1.5442 0.8528 -0.3982 0.0312 0.1309 29 GLU B CD 2775 O OE1 . GLU B 29 ? 1.0427 1.5824 0.8735 -0.4222 0.0218 0.1492 29 GLU B OE1 2776 O OE2 . GLU B 29 ? 1.0153 1.5868 0.8706 -0.3943 0.0412 0.1177 29 GLU B OE2 2777 N N . GLN B 30 ? 0.9328 1.3553 0.7771 -0.3925 0.0127 0.1420 30 GLN B N 2778 C CA . GLN B 30 ? 0.9557 1.3719 0.7824 -0.4192 0.0067 0.1499 30 GLN B CA 2779 C C . GLN B 30 ? 0.9103 1.3480 0.7547 -0.4083 0.0102 0.1405 30 GLN B C 2780 O O . GLN B 30 ? 0.9136 1.3738 0.7474 -0.4342 0.0074 0.1444 30 GLN B O 2781 C CB . GLN B 30 ? 1.0341 1.3703 0.8277 -0.4308 -0.0021 0.1628 30 GLN B CB 2782 C CG . GLN B 30 ? 1.1055 1.4224 0.8745 -0.4456 -0.0058 0.1785 30 GLN B CG 2783 C CD . GLN B 30 ? 1.1780 1.4192 0.9281 -0.4285 -0.0101 0.1890 30 GLN B CD 2784 O OE1 . GLN B 30 ? 1.1681 1.4036 0.9375 -0.3969 -0.0090 0.1824 30 GLN B OE1 2785 N NE2 . GLN B 30 ? 1.2427 1.4251 0.9523 -0.4490 -0.0136 0.2059 30 GLN B NE2 2786 N N . GLY B 31 ? 0.8540 1.2873 0.7229 -0.3725 0.0166 0.1291 31 GLY B N 2787 C CA . GLY B 31 ? 0.8226 1.2814 0.7096 -0.3578 0.0210 0.1226 31 GLY B CA 2788 C C . GLY B 31 ? 0.7729 1.1902 0.6739 -0.3245 0.0236 0.1144 31 GLY B C 2789 O O . GLY B 31 ? 0.7716 1.1609 0.6773 -0.3063 0.0268 0.1092 31 GLY B O 2790 N N . SER B 32 ? 0.7531 1.1723 0.6601 -0.3191 0.0226 0.1131 32 SER B N 2791 C CA . SER B 32 ? 0.7371 1.1200 0.6570 -0.2889 0.0250 0.1061 32 SER B CA 2792 C C . SER B 32 ? 0.7420 1.1138 0.6567 -0.2959 0.0186 0.1077 32 SER B C 2793 O O . SER B 32 ? 0.7634 1.1703 0.6686 -0.3224 0.0151 0.1124 32 SER B O 2794 C CB . SER B 32 ? 0.7090 1.1277 0.6549 -0.2557 0.0404 0.0979 32 SER B CB 2795 O OG . SER B 32 ? 0.6973 1.1818 0.6546 -0.2538 0.0462 0.1014 32 SER B OG 2796 N N . GLY B 33 ? 0.7382 1.0652 0.6577 -0.2747 0.0176 0.1030 33 GLY B N 2797 C CA . GLY B 33 ? 0.7499 1.0663 0.6646 -0.2798 0.0125 0.1027 33 GLY B CA 2798 C C . GLY B 33 ? 0.7383 0.9967 0.6540 -0.2584 0.0102 0.0980 33 GLY B C 2799 O O . GLY B 33 ? 0.7258 0.9508 0.6445 -0.2409 0.0115 0.0956 33 GLY B O 2800 N N . TYR B 34 ? 0.7370 0.9900 0.6489 -0.2624 0.0067 0.0964 34 TYR B N 2801 C CA . TYR B 34 ? 0.7251 0.9299 0.6379 -0.2429 0.0045 0.0917 34 TYR B CA 2802 C C . TYR B 34 ? 0.7561 0.8987 0.6349 -0.2639 -0.0034 0.0928 34 TYR B C 2803 O O . TYR B 34 ? 0.7893 0.9333 0.6443 -0.2972 -0.0064 0.0950 34 TYR B O 2804 C CB . TYR B 34 ? 0.7016 0.9439 0.6333 -0.2292 0.0080 0.0891 34 TYR B CB 2805 C CG . TYR B 34 ? 0.6815 0.9802 0.6420 -0.2042 0.0195 0.0903 34 TYR B CG 2806 C CD1 . TYR B 34 ? 0.6855 1.0534 0.6525 -0.2139 0.0238 0.0958 34 TYR B CD1 2807 C CD2 . TYR B 34 ? 0.6568 0.9382 0.6343 -0.1709 0.0280 0.0863 34 TYR B CD2 2808 C CE1 . TYR B 34 ? 0.6589 1.0740 0.6486 -0.1857 0.0374 0.0982 34 TYR B CE1 2809 C CE2 . TYR B 34 ? 0.6450 0.9653 0.6416 -0.1468 0.0423 0.0873 34 TYR B CE2 2810 C CZ . TYR B 34 ? 0.6470 1.0323 0.6495 -0.1517 0.0475 0.0938 34 TYR B CZ 2811 O OH . TYR B 34 ? 0.6493 1.0698 0.6676 -0.1226 0.0645 0.0962 34 TYR B OH 2812 N N . ALA B 35 ? 0.7617 0.8487 0.6351 -0.2444 -0.0054 0.0913 35 ALA B N 2813 C CA . ALA B 35 ? 0.8057 0.8257 0.6454 -0.2546 -0.0098 0.0921 35 ALA B CA 2814 C C . ALA B 35 ? 0.8064 0.8006 0.6560 -0.2260 -0.0099 0.0864 35 ALA B C 2815 O O . ALA B 35 ? 0.7893 0.7820 0.6565 -0.1991 -0.0088 0.0864 35 ALA B O 2816 C CB . ALA B 35 ? 0.8299 0.8053 0.6457 -0.2582 -0.0114 0.1015 35 ALA B CB 2817 N N . ALA B 36 ? 0.8362 0.8153 0.6736 -0.2348 -0.0110 0.0806 36 ALA B N 2818 C CA . ALA B 36 ? 0.8344 0.7870 0.6770 -0.2103 -0.0112 0.0750 36 ALA B CA 2819 C C . ALA B 36 ? 0.8816 0.7667 0.7003 -0.1958 -0.0122 0.0794 36 ALA B C 2820 O O . ALA B 36 ? 0.9429 0.7854 0.7285 -0.2119 -0.0120 0.0857 36 ALA B O 2821 C CB . ALA B 36 ? 0.8508 0.8027 0.6801 -0.2279 -0.0117 0.0672 36 ALA B CB 2822 N N . ASP B 37 ? 0.8790 0.7576 0.7133 -0.1645 -0.0122 0.0776 37 ASP B N 2823 C CA . ASP B 37 ? 0.9236 0.7472 0.7363 -0.1449 -0.0124 0.0825 37 ASP B CA 2824 C C . ASP B 37 ? 0.9876 0.7674 0.7771 -0.1453 -0.0110 0.0750 37 ASP B C 2825 O O . ASP B 37 ? 0.9519 0.7514 0.7606 -0.1322 -0.0114 0.0670 37 ASP B O 2826 C CB . ASP B 37 ? 0.8943 0.7430 0.7346 -0.1140 -0.0130 0.0839 37 ASP B CB 2827 C CG . ASP B 37 ? 0.9371 0.7456 0.7576 -0.0907 -0.0132 0.0925 37 ASP B CG 2828 O OD1 . ASP B 37 ? 0.9716 0.7715 0.7795 -0.0898 -0.0135 0.1044 37 ASP B OD1 2829 O OD2 . ASP B 37 ? 0.9423 0.7320 0.7596 -0.0715 -0.0126 0.0887 37 ASP B OD2 2830 N N . LYS B 38 ? 1.0954 0.8124 0.8401 -0.1615 -0.0078 0.0772 38 LYS B N 2831 C CA . LYS B 38 ? 1.1818 0.8481 0.8945 -0.1696 -0.0037 0.0675 38 LYS B CA 2832 C C . LYS B 38 ? 1.1990 0.8407 0.9135 -0.1318 -0.0021 0.0657 38 LYS B C 2833 O O . LYS B 38 ? 1.1975 0.8441 0.9161 -0.1304 -0.0016 0.0540 38 LYS B O 2834 C CB . LYS B 38 ? 1.3135 0.9027 0.9693 -0.1941 0.0029 0.0711 38 LYS B CB 2835 C CG . LYS B 38 ? 1.4223 0.9573 1.0363 -0.2172 0.0097 0.0571 38 LYS B CG 2836 C CD . LYS B 38 ? 1.5404 0.9666 1.0939 -0.2098 0.0212 0.0617 38 LYS B CD 2837 C CE . LYS B 38 ? 1.6096 0.9918 1.1260 -0.2336 0.0258 0.0742 38 LYS B CE 2838 N NZ . LYS B 38 ? 1.6681 1.0198 1.1413 -0.2907 0.0317 0.0630 38 LYS B NZ 2839 N N . GLU B 39 ? 1.2324 0.8552 0.9440 -0.1014 -0.0013 0.0782 39 GLU B N 2840 C CA . GLU B 39 ? 1.2615 0.8643 0.9710 -0.0631 0.0008 0.0795 39 GLU B CA 2841 C C . GLU B 39 ? 1.1468 0.8108 0.9000 -0.0487 -0.0039 0.0705 39 GLU B C 2842 O O . GLU B 39 ? 1.1484 0.7980 0.8964 -0.0375 -0.0018 0.0617 39 GLU B O 2843 C CB . GLU B 39 ? 1.3496 0.9450 1.0544 -0.0333 0.0015 0.0979 39 GLU B CB 2844 C CG . GLU B 39 ? 1.4044 1.0039 1.1152 0.0093 0.0028 0.1017 39 GLU B CG 2845 C CD . GLU B 39 ? 1.4840 1.0750 1.1815 0.0397 0.0050 0.1230 39 GLU B CD 2846 O OE1 . GLU B 39 ? 1.4879 1.1241 1.2048 0.0342 0.0000 0.1325 39 GLU B OE1 2847 O OE2 . GLU B 39 ? 1.5829 1.1244 1.2490 0.0705 0.0127 0.1310 39 GLU B OE2 2848 N N . SER B 40 ? 1.0444 0.7725 0.8370 -0.0491 -0.0088 0.0728 40 SER B N 2849 C CA . SER B 40 ? 0.9689 0.7490 0.7989 -0.0364 -0.0112 0.0659 40 SER B CA 2850 C C . SER B 40 ? 0.9217 0.7181 0.7606 -0.0542 -0.0112 0.0540 40 SER B C 2851 O O . SER B 40 ? 0.8889 0.7033 0.7433 -0.0415 -0.0114 0.0477 40 SER B O 2852 C CB . SER B 40 ? 0.9176 0.7512 0.7793 -0.0359 -0.0129 0.0700 40 SER B CB 2853 O OG . SER B 40 ? 0.9226 0.7764 0.7918 -0.0614 -0.0127 0.0687 40 SER B OG 2854 N N . THR B 41 ? 0.9053 0.7015 0.7341 -0.0841 -0.0110 0.0522 41 THR B N 2855 C CA . THR B 41 ? 0.8777 0.7001 0.7127 -0.1034 -0.0111 0.0431 41 THR B CA 2856 C C . THR B 41 ? 0.9098 0.6908 0.7171 -0.1048 -0.0089 0.0334 41 THR B C 2857 O O . THR B 41 ? 0.8863 0.6941 0.7093 -0.0989 -0.0095 0.0266 41 THR B O 2858 C CB . THR B 41 ? 0.8786 0.7170 0.7048 -0.1380 -0.0112 0.0442 41 THR B CB 2859 O OG1 . THR B 41 ? 0.8330 0.7172 0.6878 -0.1349 -0.0118 0.0515 41 THR B OG1 2860 C CG2 . THR B 41 ? 0.8700 0.7439 0.6991 -0.1593 -0.0113 0.0362 41 THR B CG2 2861 N N . GLN B 42 ? 0.9845 0.6969 0.7478 -0.1123 -0.0048 0.0330 42 GLN B N 2862 C CA . GLN B 42 ? 1.0385 0.6985 0.7662 -0.1153 0.0005 0.0217 42 GLN B CA 2863 C C . GLN B 42 ? 1.0211 0.6807 0.7617 -0.0773 0.0009 0.0201 42 GLN B C 2864 O O . GLN B 42 ? 1.0297 0.6832 0.7622 -0.0777 0.0031 0.0085 42 GLN B O 2865 C CB . GLN B 42 ? 1.1231 0.6956 0.7949 -0.1258 0.0086 0.0236 42 GLN B CB 2866 C CG . GLN B 42 ? 1.2050 0.7104 0.8296 -0.1344 0.0180 0.0094 42 GLN B CG 2867 C CD . GLN B 42 ? 1.2167 0.7546 0.8387 -0.1752 0.0171 -0.0063 42 GLN B CD 2868 O OE1 . GLN B 42 ? 1.2249 0.7695 0.8468 -0.1716 0.0185 -0.0186 42 GLN B OE1 2869 N NE2 . GLN B 42 ? 1.2186 0.7844 0.8386 -0.2147 0.0146 -0.0054 42 GLN B NE2 2870 N N . LYS B 43 ? 0.9938 0.6650 0.7531 -0.0467 -0.0011 0.0315 43 LYS B N 2871 C CA . LYS B 43 ? 1.0006 0.6859 0.7758 -0.0118 -0.0015 0.0318 43 LYS B CA 2872 C C . LYS B 43 ? 0.9193 0.6672 0.7328 -0.0138 -0.0058 0.0248 43 LYS B C 2873 O O . LYS B 43 ? 0.9209 0.6723 0.7366 0.0009 -0.0049 0.0181 43 LYS B O 2874 C CB . LYS B 43 ? 1.0372 0.7403 0.8274 0.0135 -0.0036 0.0462 43 LYS B CB 2875 C CG . LYS B 43 ? 1.1086 0.8099 0.8974 0.0513 -0.0017 0.0497 43 LYS B CG 2876 C CD . LYS B 43 ? 1.1809 0.8737 0.9597 0.0744 -0.0005 0.0666 43 LYS B CD 2877 C CE . LYS B 43 ? 1.2344 0.9221 1.0033 0.1149 0.0032 0.0718 43 LYS B CE 2878 N NZ . LYS B 43 ? 1.2662 0.9777 1.0373 0.1396 0.0025 0.0907 43 LYS B NZ 2879 N N . ALA B 44 ? 0.8403 0.6362 0.6818 -0.0303 -0.0092 0.0273 44 ALA B N 2880 C CA . ALA B 44 ? 0.7712 0.6226 0.6457 -0.0312 -0.0109 0.0241 44 ALA B CA 2881 C C . ALA B 44 ? 0.7834 0.6373 0.6463 -0.0498 -0.0102 0.0141 44 ALA B C 2882 O O . ALA B 44 ? 0.7684 0.6527 0.6479 -0.0420 -0.0107 0.0104 44 ALA B O 2883 C CB . ALA B 44 ? 0.7328 0.6275 0.6339 -0.0406 -0.0114 0.0307 44 ALA B CB 2884 N N . ILE B 45 ? 0.8237 0.6481 0.6560 -0.0774 -0.0087 0.0097 45 ILE B N 2885 C CA . ILE B 45 ? 0.8517 0.6815 0.6672 -0.1024 -0.0075 -0.0014 45 ILE B CA 2886 C C . ILE B 45 ? 0.8871 0.6775 0.6800 -0.0896 -0.0040 -0.0124 45 ILE B C 2887 O O . ILE B 45 ? 0.8755 0.6953 0.6737 -0.0958 -0.0043 -0.0204 45 ILE B O 2888 C CB . ILE B 45 ? 0.9021 0.7063 0.6832 -0.1412 -0.0053 -0.0051 45 ILE B CB 2889 C CG1 . ILE B 45 ? 0.8615 0.7304 0.6705 -0.1569 -0.0090 0.0039 45 ILE B CG1 2890 C CG2 . ILE B 45 ? 0.9448 0.7354 0.6933 -0.1705 -0.0018 -0.0206 45 ILE B CG2 2891 C CD1 . ILE B 45 ? 0.9142 0.7659 0.6927 -0.1952 -0.0076 0.0030 45 ILE B CD1 2892 N N . ASP B 46 ? 0.9403 0.6678 0.7076 -0.0697 0.0002 -0.0116 46 ASP B N 2893 C CA . ASP B 46 ? 0.9847 0.6712 0.7280 -0.0512 0.0057 -0.0211 46 ASP B CA 2894 C C . ASP B 46 ? 0.9148 0.6553 0.6966 -0.0242 0.0014 -0.0195 46 ASP B C 2895 O O . ASP B 46 ? 0.9388 0.6870 0.7163 -0.0242 0.0029 -0.0301 46 ASP B O 2896 C CB . ASP B 46 ? 1.0569 0.6705 0.7664 -0.0273 0.0126 -0.0156 46 ASP B CB 2897 C CG . ASP B 46 ? 1.1457 0.6915 0.8081 -0.0544 0.0195 -0.0167 46 ASP B CG 2898 O OD1 . ASP B 46 ? 1.1768 0.7255 0.8246 -0.0956 0.0201 -0.0268 46 ASP B OD1 2899 O OD2 . ASP B 46 ? 1.2061 0.6987 0.8447 -0.0352 0.0249 -0.0064 46 ASP B OD2 2900 N N . GLY B 47 ? 0.8458 0.6237 0.6627 -0.0045 -0.0032 -0.0069 47 GLY B N 2901 C CA . GLY B 47 ? 0.7980 0.6249 0.6487 0.0172 -0.0061 -0.0046 47 GLY B CA 2902 C C . GLY B 47 ? 0.7744 0.6499 0.6452 0.0029 -0.0081 -0.0093 47 GLY B C 2903 O O . GLY B 47 ? 0.7783 0.6689 0.6533 0.0135 -0.0077 -0.0149 47 GLY B O 2904 N N . VAL B 48 ? 0.7435 0.6476 0.6258 -0.0198 -0.0098 -0.0057 48 VAL B N 2905 C CA . VAL B 48 ? 0.7004 0.6602 0.6032 -0.0306 -0.0110 -0.0054 48 VAL B CA 2906 C C . VAL B 48 ? 0.7265 0.6792 0.6034 -0.0499 -0.0099 -0.0190 48 VAL B C 2907 O O . VAL B 48 ? 0.7013 0.6908 0.5900 -0.0466 -0.0105 -0.0214 48 VAL B O 2908 C CB . VAL B 48 ? 0.6841 0.6807 0.6043 -0.0459 -0.0116 0.0040 48 VAL B CB 2909 C CG1 . VAL B 48 ? 0.6643 0.7221 0.6002 -0.0566 -0.0117 0.0068 48 VAL B CG1 2910 C CG2 . VAL B 48 ? 0.6446 0.6520 0.5908 -0.0269 -0.0104 0.0152 48 VAL B CG2 2911 N N . THR B 49 ? 0.7712 0.6745 0.6094 -0.0720 -0.0071 -0.0282 49 THR B N 2912 C CA . THR B 49 ? 0.8175 0.7024 0.6213 -0.0956 -0.0035 -0.0447 49 THR B CA 2913 C C . THR B 49 ? 0.8407 0.7045 0.6356 -0.0726 -0.0004 -0.0539 49 THR B C 2914 O O . THR B 49 ? 0.8408 0.7317 0.6323 -0.0833 0.0000 -0.0635 49 THR B O 2915 C CB . THR B 49 ? 0.8850 0.6989 0.6392 -0.1218 0.0023 -0.0538 49 THR B CB 2916 O OG1 . THR B 49 ? 0.8661 0.7082 0.6281 -0.1470 -0.0007 -0.0458 49 THR B OG1 2917 C CG2 . THR B 49 ? 0.9465 0.7322 0.6573 -0.1509 0.0089 -0.0741 49 THR B CG2 2918 N N . ASN B 50 ? 0.8716 0.6938 0.6628 -0.0408 0.0016 -0.0504 50 ASN B N 2919 C CA . ASN B 50 ? 0.8989 0.7076 0.6835 -0.0141 0.0049 -0.0573 50 ASN B CA 2920 C C . ASN B 50 ? 0.8420 0.7238 0.6694 -0.0010 -0.0008 -0.0514 50 ASN B C 2921 O O . ASN B 50 ? 0.8515 0.7459 0.6747 0.0036 0.0007 -0.0605 50 ASN B O 2922 C CB . ASN B 50 ? 0.9259 0.6890 0.7004 0.0200 0.0084 -0.0508 50 ASN B CB 2923 C CG . ASN B 50 ? 1.0193 0.6962 0.7423 0.0139 0.0176 -0.0560 50 ASN B CG 2924 O OD1 . ASN B 50 ? 1.0875 0.7260 0.7733 -0.0159 0.0237 -0.0700 50 ASN B OD1 2925 N ND2 . ASN B 50 ? 1.0429 0.6892 0.7607 0.0411 0.0196 -0.0440 50 ASN B ND2 2926 N N . LYS B 51 ? 0.7950 0.7210 0.6603 0.0043 -0.0059 -0.0361 51 LYS B N 2927 C CA . LYS B 51 ? 0.7362 0.7238 0.6385 0.0153 -0.0090 -0.0280 51 LYS B CA 2928 C C . LYS B 51 ? 0.7332 0.7620 0.6375 -0.0035 -0.0097 -0.0329 51 LYS B C 2929 O O . LYS B 51 ? 0.7418 0.7980 0.6544 0.0058 -0.0098 -0.0353 51 LYS B O 2930 C CB . LYS B 51 ? 0.6869 0.7034 0.6200 0.0176 -0.0108 -0.0124 51 LYS B CB 2931 C CG . LYS B 51 ? 0.6446 0.7135 0.6103 0.0282 -0.0106 -0.0024 51 LYS B CG 2932 C CD . LYS B 51 ? 0.6224 0.7078 0.6100 0.0286 -0.0086 0.0110 51 LYS B CD 2933 C CE . LYS B 51 ? 0.6150 0.6763 0.6048 0.0408 -0.0077 0.0135 51 LYS B CE 2934 N NZ . LYS B 51 ? 0.5989 0.6844 0.6092 0.0526 -0.0039 0.0208 51 LYS B NZ 2935 N N . VAL B 52 ? 0.7396 0.7790 0.6358 -0.0313 -0.0102 -0.0337 52 VAL B N 2936 C CA . VAL B 52 ? 0.7283 0.8218 0.6278 -0.0519 -0.0112 -0.0357 52 VAL B CA 2937 C C . VAL B 52 ? 0.7732 0.8464 0.6415 -0.0615 -0.0085 -0.0551 52 VAL B C 2938 O O . VAL B 52 ? 0.7572 0.8772 0.6369 -0.0597 -0.0095 -0.0557 52 VAL B O 2939 C CB . VAL B 52 ? 0.7355 0.8499 0.6287 -0.0827 -0.0121 -0.0332 52 VAL B CB 2940 C CG1 . VAL B 52 ? 0.7461 0.9241 0.6373 -0.1075 -0.0131 -0.0365 52 VAL B CG1 2941 C CG2 . VAL B 52 ? 0.6925 0.8360 0.6187 -0.0699 -0.0132 -0.0136 52 VAL B CG2 2942 N N . ASN B 53 ? 0.8355 0.8360 0.6620 -0.0705 -0.0034 -0.0705 53 ASN B N 2943 C CA . ASN B 53 ? 0.9039 0.8697 0.6928 -0.0779 0.0028 -0.0914 53 ASN B CA 2944 C C . ASN B 53 ? 0.9019 0.8725 0.7039 -0.0425 0.0033 -0.0917 53 ASN B C 2945 O O . ASN B 53 ? 0.9316 0.9113 0.7192 -0.0467 0.0063 -0.1051 53 ASN B O 2946 C CB . ASN B 53 ? 0.9787 0.8500 0.7145 -0.0890 0.0119 -0.1059 53 ASN B CB 2947 C CG . ASN B 53 ? 1.0054 0.8685 0.7229 -0.1286 0.0122 -0.1068 53 ASN B CG 2948 O OD1 . ASN B 53 ? 0.9755 0.9100 0.7141 -0.1528 0.0063 -0.1010 53 ASN B OD1 2949 N ND2 . ASN B 53 ? 1.0745 0.8533 0.7518 -0.1339 0.0196 -0.1122 53 ASN B ND2 2950 N N . SER B 54 ? 0.8774 0.8461 0.7049 -0.0103 0.0006 -0.0776 54 SER B N 2951 C CA . SER B 54 ? 0.8808 0.8635 0.7226 0.0214 0.0007 -0.0760 54 SER B CA 2952 C C . SER B 54 ? 0.8472 0.9069 0.7234 0.0200 -0.0042 -0.0680 54 SER B C 2953 O O . SER B 54 ? 0.8668 0.9455 0.7423 0.0298 -0.0031 -0.0745 54 SER B O 2954 C CB . SER B 54 ? 0.8623 0.8324 0.7211 0.0500 -0.0007 -0.0627 54 SER B CB 2955 O OG . SER B 54 ? 0.9173 0.8178 0.7426 0.0572 0.0047 -0.0674 54 SER B OG 2956 N N . ILE B 55 ? 0.8125 0.9151 0.7169 0.0099 -0.0084 -0.0527 55 ILE B N 2957 C CA . ILE B 55 ? 0.7837 0.9566 0.7177 0.0094 -0.0111 -0.0410 55 ILE B CA 2958 C C . ILE B 55 ? 0.8084 1.0121 0.7264 -0.0129 -0.0108 -0.0527 55 ILE B C 2959 O O . ILE B 55 ? 0.7930 1.0321 0.7185 -0.0059 -0.0111 -0.0536 55 ILE B O 2960 C CB . ILE B 55 ? 0.7709 0.9759 0.7317 0.0058 -0.0124 -0.0215 55 ILE B CB 2961 C CG1 . ILE B 55 ? 0.7593 0.9477 0.7396 0.0284 -0.0114 -0.0096 55 ILE B CG1 2962 C CG2 . ILE B 55 ? 0.7568 1.0337 0.7392 0.0025 -0.0128 -0.0085 55 ILE B CG2 2963 C CD1 . ILE B 55 ? 0.7350 0.9375 0.7346 0.0268 -0.0098 0.0064 55 ILE B CD1 2964 N N . ILE B 56 ? 0.8491 1.0422 0.7433 -0.0428 -0.0099 -0.0621 56 ILE B N 2965 C CA . ILE B 56 ? 0.8951 1.1187 0.7682 -0.0718 -0.0088 -0.0761 56 ILE B CA 2966 C C . ILE B 56 ? 0.9646 1.1558 0.8109 -0.0654 -0.0041 -0.0967 56 ILE B C 2967 O O . ILE B 56 ? 0.9465 1.1864 0.7944 -0.0724 -0.0045 -0.1013 56 ILE B O 2968 C CB . ILE B 56 ? 0.9343 1.1364 0.7754 -0.1102 -0.0068 -0.0875 56 ILE B CB 2969 C CG1 . ILE B 56 ? 0.8956 1.1548 0.7657 -0.1184 -0.0115 -0.0665 56 ILE B CG1 2970 C CG2 . ILE B 56 ? 0.9775 1.1976 0.7850 -0.1459 -0.0034 -0.1085 56 ILE B CG2 2971 C CD1 . ILE B 56 ? 0.9349 1.1678 0.7778 -0.1520 -0.0100 -0.0741 56 ILE B CD1 2972 N N . ASP B 57 ? 1.0429 1.1552 0.8643 -0.0495 0.0012 -0.1075 57 ASP B N 2973 C CA . ASP B 57 ? 1.1175 1.1901 0.9078 -0.0388 0.0085 -0.1274 57 ASP B CA 2974 C C . ASP B 57 ? 1.0565 1.1752 0.8765 -0.0089 0.0054 -0.1195 57 ASP B C 2975 O O . ASP B 57 ? 1.0377 1.1736 0.8447 -0.0119 0.0085 -0.1329 57 ASP B O 2976 C CB . ASP B 57 ? 1.2103 1.1885 0.9665 -0.0220 0.0167 -0.1359 57 ASP B CB 2977 C CG . ASP B 57 ? 1.3139 1.2420 1.0291 -0.0099 0.0281 -0.1577 57 ASP B CG 2978 O OD1 . ASP B 57 ? 1.4086 1.3201 1.0860 -0.0403 0.0353 -0.1790 57 ASP B OD1 2979 O OD2 . ASP B 57 ? 1.3360 1.2442 1.0551 0.0295 0.0308 -0.1537 57 ASP B OD2 2980 N N . LYS B 58 ? 1.0102 1.1488 0.8672 0.0167 0.0002 -0.0990 58 LYS B N 2981 C CA . LYS B 58 ? 0.9728 1.1558 0.8563 0.0408 -0.0021 -0.0904 58 LYS B CA 2982 C C . LYS B 58 ? 0.9832 1.2397 0.8846 0.0266 -0.0055 -0.0851 58 LYS B C 2983 O O . LYS B 58 ? 1.0008 1.2876 0.9065 0.0371 -0.0050 -0.0881 58 LYS B O 2984 C CB . LYS B 58 ? 0.9211 1.1144 0.8378 0.0614 -0.0059 -0.0694 58 LYS B CB 2985 C CG . LYS B 58 ? 0.9386 1.0799 0.8438 0.0842 -0.0032 -0.0714 58 LYS B CG 2986 C CD . LYS B 58 ? 0.9503 1.0790 0.8368 0.1073 0.0015 -0.0839 58 LYS B CD 2987 C CE . LYS B 58 ? 1.0024 1.0600 0.8415 0.1071 0.0104 -0.1037 58 LYS B CE 2988 N NZ . LYS B 58 ? 1.0196 1.0546 0.8399 0.1412 0.0175 -0.1110 58 LYS B NZ 2989 N N . MET B 59 ? 0.9988 1.2889 0.9102 0.0040 -0.0085 -0.0758 59 MET B N 2990 C CA . MET B 59 ? 0.9955 1.3642 0.9250 -0.0075 -0.0114 -0.0657 59 MET B CA 2991 C C . MET B 59 ? 1.0748 1.4594 0.9733 -0.0368 -0.0093 -0.0872 59 MET B C 2992 O O . MET B 59 ? 1.0565 1.5134 0.9662 -0.0491 -0.0117 -0.0804 59 MET B O 2993 C CB . MET B 59 ? 0.9562 1.3626 0.9106 -0.0140 -0.0142 -0.0430 59 MET B CB 2994 C CG . MET B 59 ? 0.9175 1.3060 0.8984 0.0103 -0.0140 -0.0232 59 MET B CG 2995 S SD . MET B 59 ? 0.8868 1.3085 0.8967 0.0370 -0.0127 -0.0042 59 MET B SD 2996 C CE . MET B 59 ? 0.8934 1.3982 0.9111 0.0277 -0.0136 0.0045 59 MET B CE 2997 N N . ASN B 60 ? 1.1810 1.4966 1.0376 -0.0483 -0.0033 -0.1127 60 ASN B N 2998 C CA . ASN B 60 ? 1.2335 1.5449 1.0493 -0.0798 0.0022 -0.1390 60 ASN B CA 2999 C C . ASN B 60 ? 1.2141 1.5675 1.0304 -0.0731 0.0033 -0.1468 60 ASN B C 3000 O O . ASN B 60 ? 1.2056 1.6098 1.0102 -0.1018 0.0036 -0.1561 60 ASN B O 3001 C CB . ASN B 60 ? 1.3111 1.5186 1.0769 -0.0844 0.0123 -0.1635 60 ASN B CB 3002 C CG . ASN B 60 ? 1.3912 1.5768 1.1047 -0.1221 0.0217 -0.1939 60 ASN B CG 3003 O OD1 . ASN B 60 ? 1.4166 1.5874 1.1074 -0.1154 0.0288 -0.2122 60 ASN B OD1 3004 N ND2 . ASN B 60 ? 1.4372 1.6195 1.1282 -0.1641 0.0229 -0.2008 60 ASN B ND2 3005 N N . THR B 61 ? 1.2811 1.2522 1.1251 -0.1148 -0.0277 0.2009 61 THR B N 3006 C CA . THR B 61 ? 1.2757 1.2406 1.1282 -0.0939 -0.0286 0.1904 61 THR B CA 3007 C C . THR B 61 ? 1.1885 1.2249 1.0931 -0.0954 -0.0307 0.1771 61 THR B C 3008 O O . THR B 61 ? 1.2065 1.2841 1.1260 -0.0875 -0.0325 0.1785 61 THR B O 3009 C CB . THR B 61 ? 1.3232 1.2727 1.1553 -0.0492 -0.0252 0.2022 61 THR B CB 3010 O OG1 . THR B 61 ? 1.3984 1.2848 1.1741 -0.0395 -0.0203 0.2191 61 THR B OG1 3011 C CG2 . THR B 61 ? 1.3636 1.2779 1.1792 -0.0254 -0.0206 0.1971 61 THR B CG2 3012 N N . GLN B 62 ? 1.1479 1.1898 1.0675 -0.1082 -0.0311 0.1653 62 GLN B N 3013 C CA . GLN B 62 ? 1.0949 1.1861 1.0471 -0.1076 -0.0297 0.1536 62 GLN B CA 3014 C C . GLN B 62 ? 1.0665 1.1535 1.0285 -0.1118 -0.0308 0.1430 62 GLN B C 3015 O O . GLN B 62 ? 1.1264 1.1841 1.0714 -0.1298 -0.0343 0.1459 62 GLN B O 3016 C CB . GLN B 62 ? 1.0890 1.2135 1.0463 -0.1185 -0.0233 0.1585 62 GLN B CB 3017 C CG . GLN B 62 ? 1.0784 1.2360 1.0502 -0.1134 -0.0158 0.1510 62 GLN B CG 3018 C CD . GLN B 62 ? 1.1058 1.2925 1.0687 -0.1071 -0.0025 0.1602 62 GLN B CD 3019 O OE1 . GLN B 62 ? 1.1492 1.3319 1.0974 -0.1105 -0.0007 0.1694 62 GLN B OE1 3020 N NE2 . GLN B 62 ? 1.1179 1.3326 1.0831 -0.0914 0.0095 0.1602 62 GLN B NE2 3021 N N . PHE B 63 ? 0.9755 1.0853 0.9549 -0.1007 -0.0292 0.1318 63 PHE B N 3022 C CA . PHE B 63 ? 0.9453 1.0511 0.9327 -0.0997 -0.0301 0.1218 63 PHE B CA 3023 C C . PHE B 63 ? 0.9742 1.0970 0.9666 -0.1192 -0.0310 0.1255 63 PHE B C 3024 O O . PHE B 63 ? 0.9731 1.1394 0.9770 -0.1220 -0.0250 0.1337 63 PHE B O 3025 C CB . PHE B 63 ? 0.8806 1.0045 0.8768 -0.0887 -0.0268 0.1112 63 PHE B CB 3026 C CG . PHE B 63 ? 0.8461 0.9641 0.8486 -0.0844 -0.0270 0.1016 63 PHE B CG 3027 C CD1 . PHE B 63 ? 0.8312 0.9318 0.8319 -0.0742 -0.0292 0.0994 63 PHE B CD1 3028 C CD2 . PHE B 63 ? 0.8295 0.9652 0.8373 -0.0847 -0.0230 0.0986 63 PHE B CD2 3029 C CE1 . PHE B 63 ? 0.8094 0.9007 0.8109 -0.0696 -0.0285 0.0907 63 PHE B CE1 3030 C CE2 . PHE B 63 ? 0.8007 0.9315 0.8117 -0.0806 -0.0242 0.0908 63 PHE B CE2 3031 C CZ . PHE B 63 ? 0.7888 0.8926 0.7955 -0.0757 -0.0276 0.0849 63 PHE B CZ 3032 N N . GLU B 64 ? 0.9991 1.0910 0.9770 -0.1320 -0.0382 0.1231 64 GLU B N 3033 C CA . GLU B 64 ? 1.0202 1.1388 1.0006 -0.1606 -0.0450 0.1300 64 GLU B CA 3034 C C . GLU B 64 ? 0.9964 1.1178 0.9835 -0.1515 -0.0470 0.1185 64 GLU B C 3035 O O . GLU B 64 ? 1.0126 1.0784 0.9774 -0.1405 -0.0482 0.1070 64 GLU B O 3036 C CB . GLU B 64 ? 1.1151 1.1767 1.0487 -0.1985 -0.0562 0.1382 64 GLU B CB 3037 C CG . GLU B 64 ? 1.1651 1.2210 1.0862 -0.2119 -0.0542 0.1522 64 GLU B CG 3038 C CD . GLU B 64 ? 1.2802 1.2515 1.1314 -0.2532 -0.0646 0.1600 64 GLU B CD 3039 O OE1 . GLU B 64 ? 1.3455 1.2710 1.1556 -0.2818 -0.0757 0.1564 64 GLU B OE1 3040 O OE2 . GLU B 64 ? 1.3488 1.2877 1.1736 -0.2591 -0.0617 0.1698 64 GLU B OE2 3041 N N . ALA B 65 ? 0.9503 1.1395 0.9647 -0.1499 -0.0447 0.1249 65 ALA B N 3042 C CA . ALA B 65 ? 0.9117 1.1095 0.9315 -0.1394 -0.0460 0.1167 65 ALA B CA 3043 C C . ALA B 65 ? 0.9386 1.1135 0.9326 -0.1772 -0.0635 0.1190 65 ALA B C 3044 O O . ALA B 65 ? 0.9322 1.1189 0.9119 -0.2193 -0.0754 0.1344 65 ALA B O 3045 C CB . ALA B 65 ? 0.8874 1.1627 0.9331 -0.1172 -0.0350 0.1280 65 ALA B CB 3046 N N . VAL B 66 ? 0.9460 1.0812 0.9241 -0.1668 -0.0656 0.1044 66 VAL B N 3047 C CA . VAL B 66 ? 0.9956 1.0938 0.9330 -0.2015 -0.0823 0.1036 66 VAL B CA 3048 C C . VAL B 66 ? 0.9659 1.1148 0.9256 -0.1889 -0.0835 0.1023 66 VAL B C 3049 O O . VAL B 66 ? 0.9394 1.0931 0.9203 -0.1469 -0.0689 0.0917 66 VAL B O 3050 C CB . VAL B 66 ? 1.0652 1.0448 0.9412 -0.1924 -0.0802 0.0877 66 VAL B CB 3051 C CG1 . VAL B 66 ? 1.1500 1.0625 0.9564 -0.2311 -0.0969 0.0852 66 VAL B CG1 3052 C CG2 . VAL B 66 ? 1.1083 1.0374 0.9590 -0.1908 -0.0747 0.0918 66 VAL B CG2 3053 N N . GLY B 67 ? 0.9788 1.1660 0.9275 -0.2298 -0.1023 0.1158 67 GLY B N 3054 C CA . GLY B 67 ? 0.9551 1.1969 0.9206 -0.2191 -0.1059 0.1190 67 GLY B CA 3055 C C . GLY B 67 ? 0.9739 1.1243 0.8986 -0.2046 -0.1051 0.0952 67 GLY B C 3056 O O . GLY B 67 ? 1.0643 1.1192 0.9246 -0.2315 -0.1150 0.0853 67 GLY B O 3057 N N . ARG B 68 ? 0.9080 1.0773 0.8583 -0.1596 -0.0906 0.0872 68 ARG B N 3058 C CA . ARG B 68 ? 0.9001 1.0022 0.8184 -0.1435 -0.0878 0.0688 68 ARG B CA 3059 C C . ARG B 68 ? 0.8407 1.0031 0.7811 -0.1220 -0.0856 0.0742 68 ARG B C 3060 O O . ARG B 68 ? 0.7918 1.0131 0.7677 -0.0908 -0.0718 0.0832 68 ARG B O 3061 C CB . ARG B 68 ? 0.9018 0.9481 0.8210 -0.1061 -0.0675 0.0533 68 ARG B CB 3062 C CG . ARG B 68 ? 0.9390 0.9185 0.8268 -0.1135 -0.0663 0.0502 68 ARG B CG 3063 C CD . ARG B 68 ? 0.9235 0.8757 0.8169 -0.0746 -0.0474 0.0429 68 ARG B CD 3064 N NE . ARG B 68 ? 0.9461 0.8750 0.8321 -0.0713 -0.0430 0.0482 68 ARG B NE 3065 C CZ . ARG B 68 ? 0.9266 0.9012 0.8494 -0.0745 -0.0416 0.0552 68 ARG B CZ 3066 N NH1 . ARG B 68 ? 0.8735 0.9107 0.8351 -0.0765 -0.0412 0.0576 68 ARG B NH1 3067 N NH2 . ARG B 68 ? 0.9796 0.9297 0.8900 -0.0703 -0.0383 0.0613 68 ARG B NH2 3068 N N . GLU B 69 ? 0.8706 1.0061 0.7765 -0.1354 -0.0975 0.0692 69 GLU B N 3069 C CA . GLU B 69 ? 0.8319 1.0213 0.7511 -0.1146 -0.0970 0.0761 69 GLU B CA 3070 C C . GLU B 69 ? 0.8098 0.9256 0.7029 -0.0858 -0.0843 0.0554 69 GLU B C 3071 O O . GLU B 69 ? 0.8439 0.8752 0.7002 -0.0902 -0.0818 0.0398 69 GLU B O 3072 C CB . GLU B 69 ? 0.8766 1.1221 0.7803 -0.1608 -0.1255 0.0946 69 GLU B CB 3073 C CG . GLU B 69 ? 0.8763 1.2242 0.8137 -0.1931 -0.1380 0.1238 69 GLU B CG 3074 C CD . GLU B 69 ? 0.9083 1.3671 0.8507 -0.2331 -0.1650 0.1547 69 GLU B CD 3075 O OE1 . GLU B 69 ? 0.8918 1.3946 0.8414 -0.2049 -0.1639 0.1615 69 GLU B OE1 3076 O OE2 . GLU B 69 ? 0.9598 1.4684 0.8971 -0.2959 -0.1885 0.1759 69 GLU B OE2 3077 N N . PHE B 70 ? 0.7720 0.9203 0.6787 -0.0515 -0.0732 0.0588 70 PHE B N 3078 C CA . PHE B 70 ? 0.7623 0.8517 0.6471 -0.0252 -0.0591 0.0430 70 PHE B CA 3079 C C . PHE B 70 ? 0.7656 0.8920 0.6430 -0.0078 -0.0612 0.0521 70 PHE B C 3080 O O . PHE B 70 ? 0.7463 0.9492 0.6453 0.0073 -0.0609 0.0724 70 PHE B O 3081 C CB . PHE B 70 ? 0.7360 0.8035 0.6350 0.0020 -0.0358 0.0365 70 PHE B CB 3082 C CG . PHE B 70 ? 0.7260 0.7769 0.6383 -0.0107 -0.0340 0.0329 70 PHE B CG 3083 C CD1 . PHE B 70 ? 0.7132 0.8061 0.6500 -0.0168 -0.0357 0.0433 70 PHE B CD1 3084 C CD2 . PHE B 70 ? 0.7325 0.7326 0.6311 -0.0109 -0.0283 0.0232 70 PHE B CD2 3085 C CE1 . PHE B 70 ? 0.6984 0.7751 0.6444 -0.0278 -0.0345 0.0411 70 PHE B CE1 3086 C CE2 . PHE B 70 ? 0.7288 0.7211 0.6380 -0.0164 -0.0258 0.0243 70 PHE B CE2 3087 C CZ . PHE B 70 ? 0.7149 0.7418 0.6474 -0.0274 -0.0303 0.0318 70 PHE B CZ 3088 N N . ASN B 71 ? 0.7988 0.8750 0.6426 -0.0037 -0.0609 0.0406 71 ASN B N 3089 C CA . ASN B 71 ? 0.8127 0.9200 0.6440 0.0136 -0.0636 0.0498 71 ASN B CA 3090 C C . ASN B 71 ? 0.8106 0.9103 0.6428 0.0601 -0.0375 0.0518 71 ASN B C 3091 O O . ASN B 71 ? 0.7727 0.8410 0.6113 0.0698 -0.0203 0.0450 71 ASN B O 3092 C CB . ASN B 71 ? 0.8517 0.9011 0.6353 -0.0007 -0.0735 0.0375 71 ASN B CB 3093 C CG . ASN B 71 ? 0.8520 0.8256 0.6159 0.0243 -0.0500 0.0202 71 ASN B CG 3094 O OD1 . ASN B 71 ? 0.8289 0.8021 0.6004 0.0536 -0.0308 0.0214 71 ASN B OD1 3095 N ND2 . ASN B 71 ? 0.8926 0.7985 0.6203 0.0128 -0.0502 0.0072 71 ASN B ND2 3096 N N . ASN B 72 ? 0.8342 0.9534 0.6475 0.0855 -0.0354 0.0619 72 ASN B N 3097 C CA . ASN B 72 ? 0.8561 0.9528 0.6463 0.1324 -0.0099 0.0675 72 ASN B CA 3098 C C . ASN B 72 ? 0.8588 0.8592 0.6176 0.1343 0.0098 0.0478 72 ASN B C 3099 O O . ASN B 72 ? 0.8844 0.8407 0.6086 0.1593 0.0309 0.0499 72 ASN B O 3100 C CB . ASN B 72 ? 0.9051 1.0452 0.6756 0.1623 -0.0127 0.0863 72 ASN B CB 3101 C CG . ASN B 72 ? 0.9622 1.0820 0.6945 0.2216 0.0157 0.1003 72 ASN B CG 3102 O OD1 . ASN B 72 ? 0.9880 1.1280 0.7225 0.2468 0.0292 0.1131 72 ASN B OD1 3103 N ND2 . ASN B 72 ? 1.0111 1.0789 0.6951 0.2474 0.0272 0.0989 72 ASN B ND2 3104 N N . LEU B 73 ? 0.8366 0.8029 0.5970 0.1079 0.0042 0.0322 73 LEU B N 3105 C CA . LEU B 73 ? 0.8476 0.7531 0.5898 0.1035 0.0214 0.0212 73 LEU B CA 3106 C C . LEU B 73 ? 0.8116 0.7171 0.5836 0.0794 0.0211 0.0148 73 LEU B C 3107 O O . LEU B 73 ? 0.8009 0.6865 0.5708 0.0713 0.0293 0.0109 73 LEU B O 3108 C CB . LEU B 73 ? 0.8880 0.7651 0.6040 0.1059 0.0230 0.0159 73 LEU B CB 3109 C CG . LEU B 73 ? 0.9278 0.7964 0.6065 0.1324 0.0266 0.0233 73 LEU B CG 3110 C CD1 . LEU B 73 ? 0.9415 0.7859 0.5956 0.1310 0.0245 0.0173 73 LEU B CD1 3111 C CD2 . LEU B 73 ? 0.9640 0.7830 0.6025 0.1497 0.0490 0.0276 73 LEU B CD2 3112 N N . GLU B 74 ? 0.7781 0.7154 0.5777 0.0720 0.0131 0.0182 74 GLU B N 3113 C CA . GLU B 74 ? 0.7548 0.6946 0.5796 0.0540 0.0136 0.0153 74 GLU B CA 3114 C C . GLU B 74 ? 0.7630 0.7091 0.5911 0.0551 0.0193 0.0202 74 GLU B C 3115 O O . GLU B 74 ? 0.7272 0.6957 0.5815 0.0437 0.0133 0.0217 74 GLU B O 3116 C CB . GLU B 74 ? 0.7335 0.6889 0.5745 0.0399 -0.0025 0.0138 74 GLU B CB 3117 C CG . GLU B 74 ? 0.7585 0.6787 0.5722 0.0399 -0.0046 0.0073 74 GLU B CG 3118 C CD . GLU B 74 ? 0.7878 0.6923 0.5855 0.0208 -0.0215 0.0052 74 GLU B CD 3119 O OE1 . GLU B 74 ? 0.7904 0.7307 0.5994 0.0020 -0.0383 0.0115 74 GLU B OE1 3120 O OE2 . GLU B 74 ? 0.8272 0.6807 0.5920 0.0252 -0.0164 0.0002 74 GLU B OE2 3121 N N . ARG B 75 ? 0.8241 0.7367 0.6117 0.0711 0.0326 0.0231 75 ARG B N 3122 C CA . ARG B 75 ? 0.8672 0.7625 0.6300 0.0819 0.0421 0.0283 75 ARG B CA 3123 C C . ARG B 75 ? 0.8389 0.7122 0.6000 0.0516 0.0436 0.0241 75 ARG B C 3124 O O . ARG B 75 ? 0.8324 0.7070 0.5906 0.0528 0.0450 0.0269 75 ARG B O 3125 C CB . ARG B 75 ? 0.9820 0.8167 0.6724 0.1122 0.0600 0.0329 75 ARG B CB 3126 C CG . ARG B 75 ? 1.0295 0.9049 0.7208 0.1525 0.0598 0.0452 75 ARG B CG 3127 C CD . ARG B 75 ? 1.0718 1.0135 0.7859 0.1791 0.0594 0.0621 75 ARG B CD 3128 N NE . ARG B 75 ? 1.1353 1.1608 0.8741 0.2041 0.0506 0.0808 75 ARG B NE 3129 C CZ . ARG B 75 ? 1.1673 1.2867 0.9363 0.2259 0.0478 0.1050 75 ARG B CZ 3130 N NH1 . ARG B 75 ? 1.1685 1.3003 0.9441 0.2322 0.0563 0.1112 75 ARG B NH1 3131 N NH2 . ARG B 75 ? 1.1599 1.3711 0.9519 0.2395 0.0357 0.1268 75 ARG B NH2 3132 N N . ARG B 76 ? 0.8313 0.6949 0.5944 0.0246 0.0432 0.0211 76 ARG B N 3133 C CA . ARG B 76 ? 0.8251 0.6898 0.5903 -0.0097 0.0413 0.0235 76 ARG B CA 3134 C C . ARG B 76 ? 0.7833 0.7042 0.6072 -0.0132 0.0305 0.0253 76 ARG B C 3135 O O . ARG B 76 ? 0.7866 0.7052 0.6057 -0.0253 0.0285 0.0270 76 ARG B O 3136 C CB . ARG B 76 ? 0.8157 0.6894 0.5800 -0.0365 0.0433 0.0291 76 ARG B CB 3137 C CG . ARG B 76 ? 0.8790 0.6838 0.5707 -0.0475 0.0536 0.0293 76 ARG B CG 3138 C CD . ARG B 76 ? 0.8728 0.7107 0.5769 -0.0726 0.0556 0.0395 76 ARG B CD 3139 N NE . ARG B 76 ? 0.8210 0.7056 0.5755 -0.0396 0.0566 0.0383 76 ARG B NE 3140 C CZ . ARG B 76 ? 0.7876 0.7273 0.5744 -0.0422 0.0608 0.0502 76 ARG B CZ 3141 N NH1 . ARG B 76 ? 0.7994 0.7830 0.5903 -0.0799 0.0627 0.0692 76 ARG B NH1 3142 N NH2 . ARG B 76 ? 0.7519 0.7050 0.5599 -0.0072 0.0636 0.0462 76 ARG B NH2 3143 N N . ILE B 77 ? 0.7471 0.7039 0.6116 -0.0026 0.0246 0.0248 77 ILE B N 3144 C CA . ILE B 77 ? 0.7368 0.7261 0.6387 -0.0043 0.0162 0.0270 77 ILE B CA 3145 C C . ILE B 77 ? 0.7409 0.7378 0.6493 0.0016 0.0096 0.0261 77 ILE B C 3146 O O . ILE B 77 ? 0.7282 0.7430 0.6566 -0.0063 0.0043 0.0292 77 ILE B O 3147 C CB . ILE B 77 ? 0.7430 0.7391 0.6572 0.0070 0.0148 0.0273 77 ILE B CB 3148 C CG1 . ILE B 77 ? 0.7794 0.7545 0.6761 0.0176 0.0092 0.0200 77 ILE B CG1 3149 C CG2 . ILE B 77 ? 0.7614 0.7726 0.6758 0.0085 0.0257 0.0361 77 ILE B CG2 3150 C CD1 . ILE B 77 ? 0.8097 0.7608 0.6902 0.0260 0.0074 0.0179 77 ILE B CD1 3151 N N . GLU B 78 ? 0.7506 0.7438 0.6427 0.0177 0.0110 0.0262 78 GLU B N 3152 C CA . GLU B 78 ? 0.7634 0.7869 0.6636 0.0274 0.0084 0.0340 78 GLU B CA 3153 C C . GLU B 78 ? 0.7582 0.7610 0.6368 0.0296 0.0189 0.0361 78 GLU B C 3154 O O . GLU B 78 ? 0.7368 0.7655 0.6343 0.0252 0.0157 0.0413 78 GLU B O 3155 C CB . GLU B 78 ? 0.8178 0.8586 0.7028 0.0530 0.0112 0.0416 78 GLU B CB 3156 C CG . GLU B 78 ? 0.8533 0.9544 0.7522 0.0695 0.0111 0.0594 78 GLU B CG 3157 C CD . GLU B 78 ? 0.9390 1.0847 0.8303 0.0984 0.0124 0.0752 78 GLU B CD 3158 O OE1 . GLU B 78 ? 1.0256 1.1256 0.8757 0.1241 0.0255 0.0720 78 GLU B OE1 3159 O OE2 . GLU B 78 ? 0.9592 1.1910 0.8830 0.0928 -0.0004 0.0941 78 GLU B OE2 3160 N N . ASN B 79 ? 0.7777 0.7232 0.6046 0.0325 0.0312 0.0322 79 ASN B N 3161 C CA . ASN B 79 ? 0.8171 0.7129 0.5931 0.0283 0.0409 0.0323 79 ASN B CA 3162 C C . ASN B 79 ? 0.8023 0.7135 0.6035 -0.0080 0.0303 0.0308 79 ASN B C 3163 O O . ASN B 79 ? 0.8314 0.7317 0.6158 -0.0121 0.0319 0.0329 79 ASN B O 3164 C CB . ASN B 79 ? 0.9001 0.7098 0.5940 0.0268 0.0536 0.0283 79 ASN B CB 3165 C CG . ASN B 79 ? 0.9880 0.7131 0.5941 0.0213 0.0649 0.0275 79 ASN B CG 3166 O OD1 . ASN B 79 ? 1.0420 0.7468 0.6125 0.0599 0.0790 0.0331 79 ASN B OD1 3167 N ND2 . ASN B 79 ? 1.0394 0.7140 0.6005 -0.0276 0.0594 0.0234 79 ASN B ND2 3168 N N . LEU B 80 ? 0.7630 0.7042 0.6014 -0.0287 0.0214 0.0305 80 LEU B N 3169 C CA . LEU B 80 ? 0.7284 0.7045 0.5970 -0.0540 0.0124 0.0361 80 LEU B CA 3170 C C . LEU B 80 ? 0.6862 0.6938 0.5910 -0.0435 0.0069 0.0382 80 LEU B C 3171 O O . LEU B 80 ? 0.7064 0.7176 0.6079 -0.0559 0.0041 0.0418 80 LEU B O 3172 C CB . LEU B 80 ? 0.7101 0.7261 0.6137 -0.0586 0.0097 0.0419 80 LEU B CB 3173 C CG . LEU B 80 ? 0.7091 0.7771 0.6382 -0.0792 0.0041 0.0567 80 LEU B CG 3174 C CD1 . LEU B 80 ? 0.7004 0.8111 0.6503 -0.0745 0.0089 0.0687 80 LEU B CD1 3175 C CD2 . LEU B 80 ? 0.6928 0.7875 0.6549 -0.0665 -0.0009 0.0605 80 LEU B CD2 3176 N N . ASN B 81 ? 0.6631 0.6897 0.5943 -0.0264 0.0040 0.0370 81 ASN B N 3177 C CA . ASN B 81 ? 0.6273 0.6801 0.5847 -0.0255 -0.0030 0.0413 81 ASN B CA 3178 C C . ASN B 81 ? 0.6428 0.7012 0.5881 -0.0183 0.0022 0.0462 81 ASN B C 3179 O O . ASN B 81 ? 0.6096 0.6854 0.5691 -0.0257 -0.0012 0.0516 81 ASN B O 3180 C CB . ASN B 81 ? 0.6169 0.6794 0.5842 -0.0211 -0.0100 0.0406 81 ASN B CB 3181 C CG . ASN B 81 ? 0.6156 0.6985 0.5973 -0.0341 -0.0204 0.0474 81 ASN B CG 3182 O OD1 . ASN B 81 ? 0.6315 0.7016 0.6158 -0.0430 -0.0238 0.0486 81 ASN B OD1 3183 N ND2 . ASN B 81 ? 0.6121 0.7314 0.5993 -0.0359 -0.0253 0.0558 81 ASN B ND2 3184 N N . LYS B 82 ? 0.7011 0.7404 0.6123 0.0020 0.0138 0.0467 82 LYS B N 3185 C CA . LYS B 82 ? 0.7611 0.8001 0.6457 0.0241 0.0262 0.0553 82 LYS B CA 3186 C C . LYS B 82 ? 0.8063 0.7995 0.6534 0.0096 0.0300 0.0513 82 LYS B C 3187 O O . LYS B 82 ? 0.7880 0.7997 0.6419 0.0109 0.0312 0.0580 82 LYS B O 3188 C CB . LYS B 82 ? 0.8403 0.8516 0.6764 0.0608 0.0431 0.0591 82 LYS B CB 3189 C CG . LYS B 82 ? 0.9280 0.9443 0.7275 0.1033 0.0633 0.0749 82 LYS B CG 3190 C CD . LYS B 82 ? 1.0486 1.0126 0.7771 0.1490 0.0848 0.0794 82 LYS B CD 3191 C CE . LYS B 82 ? 1.1467 1.1158 0.8267 0.2095 0.1123 0.1011 82 LYS B CE 3192 N NZ . LYS B 82 ? 1.2137 1.1100 0.8320 0.2075 0.1240 0.0958 82 LYS B NZ 3193 N N . LYS B 83 ? 0.8544 0.7913 0.6588 -0.0103 0.0300 0.0425 83 LYS B N 3194 C CA . LYS B 83 ? 0.9047 0.7954 0.6602 -0.0374 0.0285 0.0404 83 LYS B CA 3195 C C . LYS B 83 ? 0.8411 0.7876 0.6525 -0.0628 0.0128 0.0451 83 LYS B C 3196 O O . LYS B 83 ? 0.8620 0.7911 0.6451 -0.0775 0.0109 0.0472 83 LYS B O 3197 C CB . LYS B 83 ? 0.9834 0.8106 0.6766 -0.0678 0.0276 0.0347 83 LYS B CB 3198 C CG . LYS B 83 ? 1.1277 0.8409 0.7028 -0.0533 0.0461 0.0302 83 LYS B CG 3199 C CD . LYS B 83 ? 1.1498 0.8609 0.7180 0.0098 0.0664 0.0341 83 LYS B CD 3200 C CE . LYS B 83 ? 1.3039 0.8850 0.7346 0.0386 0.0913 0.0329 83 LYS B CE 3201 N NZ . LYS B 83 ? 1.3840 0.8908 0.7304 0.0368 0.1002 0.0324 83 LYS B NZ 3202 N N . MET B 84 ? 0.7707 0.7740 0.6489 -0.0638 0.0034 0.0478 84 MET B N 3203 C CA . MET B 84 ? 0.7346 0.7821 0.6554 -0.0755 -0.0072 0.0554 84 MET B CA 3204 C C . MET B 84 ? 0.7090 0.7700 0.6437 -0.0642 -0.0060 0.0593 84 MET B C 3205 O O . MET B 84 ? 0.7274 0.7939 0.6584 -0.0751 -0.0098 0.0646 84 MET B O 3206 C CB . MET B 84 ? 0.7063 0.7864 0.6698 -0.0686 -0.0116 0.0584 84 MET B CB 3207 C CG . MET B 84 ? 0.7036 0.8200 0.6933 -0.0717 -0.0179 0.0708 84 MET B CG 3208 S SD . MET B 84 ? 0.7255 0.8367 0.7340 -0.0486 -0.0177 0.0731 84 MET B SD 3209 C CE . MET B 84 ? 0.7248 0.8235 0.7299 -0.0560 -0.0206 0.0698 84 MET B CE 3210 N N . GLU B 85 ? 0.7753 1.0588 0.6535 -0.1102 0.0243 0.0533 85 GLU B N 3211 C CA . GLU B 85 ? 0.7701 1.0594 0.6453 -0.1167 0.0182 0.0594 85 GLU B CA 3212 C C . GLU B 85 ? 0.7550 1.0465 0.6428 -0.1000 0.0227 0.0728 85 GLU B C 3213 O O . GLU B 85 ? 0.7621 1.0411 0.6502 -0.1003 0.0192 0.0699 85 GLU B O 3214 C CB . GLU B 85 ? 0.7854 1.1147 0.6507 -0.1373 0.0127 0.0708 85 GLU B CB 3215 C CG . GLU B 85 ? 0.8211 1.1349 0.6619 -0.1588 0.0095 0.0553 85 GLU B CG 3216 C CD . GLU B 85 ? 0.8566 1.1824 0.6679 -0.1931 0.0031 0.0566 85 GLU B CD 3217 O OE1 . GLU B 85 ? 0.8663 1.2547 0.6840 -0.2064 0.0000 0.0757 85 GLU B OE1 3218 O OE2 . GLU B 85 ? 0.8834 1.1559 0.6580 -0.2073 0.0028 0.0392 85 GLU B OE2 3219 N N . ASP B 86 ? 0.7382 1.0372 0.6289 -0.0842 0.0324 0.0874 86 ASP B N 3220 C CA . ASP B 86 ? 0.7277 1.0126 0.6180 -0.0643 0.0416 0.0994 86 ASP B CA 3221 C C . ASP B 86 ? 0.7090 0.9506 0.5983 -0.0641 0.0446 0.0826 86 ASP B C 3222 O O . ASP B 86 ? 0.7113 0.9404 0.6018 -0.0561 0.0466 0.0861 86 ASP B O 3223 C CB . ASP B 86 ? 0.7594 1.0396 0.6343 -0.0447 0.0565 0.1176 86 ASP B CB 3224 C CG . ASP B 86 ? 0.7813 1.1114 0.6560 -0.0269 0.0587 0.1455 86 ASP B CG 3225 O OD1 . ASP B 86 ? 0.8098 1.1561 0.6898 -0.0171 0.0579 0.1555 86 ASP B OD1 3226 O OD2 . ASP B 86 ? 0.8012 1.1615 0.6702 -0.0219 0.0614 0.1585 86 ASP B OD2 3227 N N . GLY B 87 ? 0.6907 0.9177 0.5772 -0.0732 0.0455 0.0658 87 GLY B N 3228 C CA . GLY B 87 ? 0.6891 0.8940 0.5742 -0.0765 0.0482 0.0506 87 GLY B CA 3229 C C . GLY B 87 ? 0.6781 0.8832 0.5737 -0.0748 0.0387 0.0427 87 GLY B C 3230 O O . GLY B 87 ? 0.6808 0.8715 0.5767 -0.0713 0.0415 0.0415 87 GLY B O 3231 N N . PHE B 88 ? 0.6644 0.8785 0.5606 -0.0786 0.0291 0.0374 88 PHE B N 3232 C CA . PHE B 88 ? 0.6552 0.8563 0.5482 -0.0769 0.0223 0.0307 88 PHE B CA 3233 C C . PHE B 88 ? 0.6592 0.8608 0.5560 -0.0765 0.0206 0.0438 88 PHE B C 3234 O O . PHE B 88 ? 0.6631 0.8502 0.5615 -0.0714 0.0194 0.0404 88 PHE B O 3235 C CB . PHE B 88 ? 0.6646 0.8564 0.5383 -0.0838 0.0167 0.0222 88 PHE B CB 3236 C CG . PHE B 88 ? 0.6616 0.8504 0.5277 -0.0750 0.0191 0.0077 88 PHE B CG 3237 C CD1 . PHE B 88 ? 0.6567 0.8434 0.5233 -0.0587 0.0207 -0.0013 88 PHE B CD1 3238 C CD2 . PHE B 88 ? 0.6747 0.8719 0.5330 -0.0812 0.0202 0.0047 88 PHE B CD2 3239 C CE1 . PHE B 88 ? 0.6684 0.8689 0.5282 -0.0456 0.0239 -0.0118 88 PHE B CE1 3240 C CE2 . PHE B 88 ? 0.6823 0.8839 0.5329 -0.0697 0.0235 -0.0073 88 PHE B CE2 3241 C CZ . PHE B 88 ? 0.6839 0.8909 0.5354 -0.0503 0.0255 -0.0150 88 PHE B CZ 3242 N N . LEU B 89 ? 0.6727 0.8991 0.5709 -0.0803 0.0208 0.0603 89 LEU B N 3243 C CA . LEU B 89 ? 0.6839 0.9268 0.5863 -0.0772 0.0201 0.0757 89 LEU B CA 3244 C C . LEU B 89 ? 0.6740 0.8976 0.5815 -0.0595 0.0294 0.0801 89 LEU B C 3245 O O . LEU B 89 ? 0.6467 0.8672 0.5570 -0.0565 0.0277 0.0833 89 LEU B O 3246 C CB . LEU B 89 ? 0.7078 0.9999 0.6112 -0.0786 0.0207 0.0965 89 LEU B CB 3247 C CG . LEU B 89 ? 0.7535 1.0712 0.6453 -0.1057 0.0113 0.0938 89 LEU B CG 3248 C CD1 . LEU B 89 ? 0.7645 1.1472 0.6606 -0.1045 0.0130 0.1168 89 LEU B CD1 3249 C CD2 . LEU B 89 ? 0.7673 1.0769 0.6421 -0.1298 0.0026 0.0869 89 LEU B CD2 3250 N N . ASP B 90 ? 0.6743 0.8797 0.5759 -0.0517 0.0403 0.0795 90 ASP B N 3251 C CA . ASP B 90 ? 0.6810 0.8537 0.5720 -0.0420 0.0524 0.0811 90 ASP B CA 3252 C C . ASP B 90 ? 0.6633 0.8196 0.5592 -0.0507 0.0479 0.0628 90 ASP B C 3253 O O . ASP B 90 ? 0.6574 0.7955 0.5490 -0.0466 0.0527 0.0643 90 ASP B O 3254 C CB . ASP B 90 ? 0.7052 0.8519 0.5729 -0.0397 0.0675 0.0837 90 ASP B CB 3255 C CG . ASP B 90 ? 0.7342 0.8896 0.5879 -0.0195 0.0773 0.1076 90 ASP B CG 3256 O OD1 . ASP B 90 ? 0.7302 0.9229 0.5957 -0.0068 0.0728 0.1237 90 ASP B OD1 3257 O OD2 . ASP B 90 ? 0.7743 0.9035 0.6018 -0.0159 0.0904 0.1118 90 ASP B OD2 3258 N N . VAL B 91 ? 0.6508 0.8168 0.5529 -0.0597 0.0402 0.0471 91 VAL B N 3259 C CA . VAL B 91 ? 0.6365 0.8013 0.5426 -0.0615 0.0360 0.0326 91 VAL B CA 3260 C C . VAL B 91 ? 0.6256 0.7851 0.5361 -0.0559 0.0276 0.0339 91 VAL B C 3261 O O . VAL B 91 ? 0.6344 0.7872 0.5467 -0.0532 0.0277 0.0299 91 VAL B O 3262 C CB . VAL B 91 ? 0.6319 0.8149 0.5387 -0.0629 0.0316 0.0189 91 VAL B CB 3263 C CG1 . VAL B 91 ? 0.6372 0.8284 0.5457 -0.0542 0.0269 0.0085 91 VAL B CG1 3264 C CG2 . VAL B 91 ? 0.6384 0.8319 0.5394 -0.0740 0.0400 0.0150 91 VAL B CG2 3265 N N . TRP B 92 ? 0.6166 0.7796 0.5241 -0.0586 0.0210 0.0393 92 TRP B N 3266 C CA . TRP B 92 ? 0.6227 0.7750 0.5238 -0.0608 0.0139 0.0398 92 TRP B CA 3267 C C . TRP B 92 ? 0.6225 0.7826 0.5313 -0.0592 0.0158 0.0540 92 TRP B C 3268 O O . TRP B 92 ? 0.6403 0.7897 0.5469 -0.0594 0.0122 0.0530 92 TRP B O 3269 C CB . TRP B 92 ? 0.6354 0.7840 0.5170 -0.0741 0.0077 0.0385 92 TRP B CB 3270 C CG . TRP B 92 ? 0.6575 0.7814 0.5193 -0.0685 0.0073 0.0234 92 TRP B CG 3271 C CD1 . TRP B 92 ? 0.6682 0.7949 0.5216 -0.0699 0.0089 0.0179 92 TRP B CD1 3272 C CD2 . TRP B 92 ? 0.6779 0.7723 0.5222 -0.0542 0.0072 0.0135 92 TRP B CD2 3273 N NE1 . TRP B 92 ? 0.6950 0.7957 0.5251 -0.0552 0.0107 0.0055 92 TRP B NE1 3274 C CE2 . TRP B 92 ? 0.6988 0.7798 0.5216 -0.0432 0.0101 0.0035 92 TRP B CE2 3275 C CE3 . TRP B 92 ? 0.6840 0.7632 0.5261 -0.0466 0.0059 0.0135 92 TRP B CE3 3276 C CZ2 . TRP B 92 ? 0.7389 0.7929 0.5347 -0.0192 0.0133 -0.0043 92 TRP B CZ2 3277 C CZ3 . TRP B 92 ? 0.7145 0.7667 0.5319 -0.0262 0.0077 0.0051 92 TRP B CZ3 3278 C CH2 . TRP B 92 ? 0.7416 0.7819 0.5346 -0.0099 0.0121 -0.0028 92 TRP B CH2 3279 N N . THR B 93 ? 0.6310 0.8093 0.5448 -0.0539 0.0230 0.0685 93 THR B N 3280 C CA . THR B 93 ? 0.6277 0.8140 0.5439 -0.0429 0.0291 0.0844 93 THR B CA 3281 C C . THR B 93 ? 0.6418 0.7951 0.5553 -0.0362 0.0362 0.0774 93 THR B C 3282 O O . THR B 93 ? 0.6459 0.7954 0.5615 -0.0331 0.0352 0.0804 93 THR B O 3283 C CB . THR B 93 ? 0.6322 0.8384 0.5438 -0.0285 0.0398 0.1035 93 THR B CB 3284 O OG1 . THR B 93 ? 0.6316 0.8846 0.5473 -0.0381 0.0318 0.1125 93 THR B OG1 3285 C CG2 . THR B 93 ? 0.6494 0.8558 0.5543 -0.0066 0.0513 0.1213 93 THR B CG2 3286 N N . TYR B 94 ? 0.6435 0.7766 0.5491 -0.0384 0.0437 0.0678 94 TYR B N 3287 C CA . TYR B 94 ? 0.6500 0.7575 0.5466 -0.0421 0.0508 0.0589 94 TYR B CA 3288 C C . TYR B 94 ? 0.6441 0.7589 0.5532 -0.0454 0.0393 0.0481 94 TYR B C 3289 O O . TYR B 94 ? 0.6397 0.7432 0.5474 -0.0435 0.0412 0.0494 94 TYR B O 3290 C CB . TYR B 94 ? 0.6516 0.7505 0.5346 -0.0546 0.0582 0.0483 94 TYR B CB 3291 C CG . TYR B 94 ? 0.6568 0.7459 0.5284 -0.0696 0.0632 0.0360 94 TYR B CG 3292 C CD1 . TYR B 94 ? 0.6382 0.7609 0.5257 -0.0754 0.0526 0.0225 94 TYR B CD1 3293 C CD2 . TYR B 94 ? 0.6932 0.7399 0.5304 -0.0779 0.0804 0.0387 94 TYR B CD2 3294 C CE1 . TYR B 94 ? 0.6428 0.7756 0.5211 -0.0916 0.0563 0.0129 94 TYR B CE1 3295 C CE2 . TYR B 94 ? 0.7068 0.7493 0.5278 -0.1008 0.0851 0.0265 94 TYR B CE2 3296 C CZ . TYR B 94 ? 0.6766 0.7716 0.5226 -0.1090 0.0717 0.0139 94 TYR B CZ 3297 O OH . TYR B 94 ? 0.6883 0.7991 0.5206 -0.1336 0.0752 0.0033 94 TYR B OH 3298 N N . ASN B 95 ? 0.6417 0.7706 0.5570 -0.0473 0.0291 0.0384 95 ASN B N 3299 C CA . ASN B 95 ? 0.6414 0.7696 0.5579 -0.0432 0.0208 0.0301 95 ASN B CA 3300 C C . ASN B 95 ? 0.6477 0.7642 0.5635 -0.0420 0.0164 0.0378 95 ASN B C 3301 O O . ASN B 95 ? 0.6770 0.7865 0.5929 -0.0387 0.0148 0.0345 95 ASN B O 3302 C CB . ASN B 95 ? 0.6437 0.7739 0.5520 -0.0385 0.0144 0.0221 95 ASN B CB 3303 C CG . ASN B 95 ? 0.6496 0.8036 0.5599 -0.0354 0.0176 0.0126 95 ASN B CG 3304 O OD1 . ASN B 95 ? 0.6367 0.8066 0.5524 -0.0442 0.0239 0.0108 95 ASN B OD1 3305 N ND2 . ASN B 95 ? 0.6712 0.8263 0.5701 -0.0249 0.0148 0.0065 95 ASN B ND2 3306 N N . ALA B 96 ? 0.6346 0.7571 0.5492 -0.0466 0.0146 0.0488 96 ALA B N 3307 C CA . ALA B 96 ? 0.6361 0.7600 0.5482 -0.0509 0.0101 0.0571 96 ALA B CA 3308 C C . ALA B 96 ? 0.6285 0.7544 0.5486 -0.0426 0.0174 0.0664 96 ALA B C 3309 O O . ALA B 96 ? 0.6409 0.7594 0.5605 -0.0433 0.0142 0.0661 96 ALA B O 3310 C CB . ALA B 96 ? 0.6422 0.7909 0.5491 -0.0630 0.0064 0.0677 96 ALA B CB 3311 N N . GLU B 97 ? 0.6322 0.7608 0.5524 -0.0333 0.0291 0.0751 97 GLU B N 3312 C CA . GLU B 97 ? 0.6448 0.7628 0.5591 -0.0210 0.0408 0.0856 97 GLU B CA 3313 C C . GLU B 97 ? 0.6511 0.7387 0.5593 -0.0253 0.0448 0.0730 97 GLU B C 3314 O O . GLU B 97 ? 0.6673 0.7443 0.5716 -0.0207 0.0489 0.0772 97 GLU B O 3315 C CB . GLU B 97 ? 0.6705 0.7827 0.5696 -0.0055 0.0567 0.0993 97 GLU B CB 3316 C CG . GLU B 97 ? 0.6773 0.8367 0.5831 0.0036 0.0543 0.1178 97 GLU B CG 3317 C CD . GLU B 97 ? 0.7224 0.8762 0.6084 0.0262 0.0715 0.1338 97 GLU B CD 3318 O OE1 . GLU B 97 ? 0.7632 0.8678 0.6269 0.0259 0.0833 0.1259 97 GLU B OE1 3319 O OE2 . GLU B 97 ? 0.7434 0.9448 0.6312 0.0439 0.0739 0.1556 97 GLU B OE2 3320 N N . LEU B 98 ? 0.6440 0.7257 0.5504 -0.0354 0.0438 0.0584 98 LEU B N 3321 C CA . LEU B 98 ? 0.6519 0.7228 0.5519 -0.0449 0.0468 0.0468 98 LEU B CA 3322 C C . LEU B 98 ? 0.6430 0.7261 0.5561 -0.0431 0.0341 0.0415 98 LEU B C 3323 O O . LEU B 98 ? 0.6566 0.7312 0.5666 -0.0450 0.0364 0.0408 98 LEU B O 3324 C CB . LEU B 98 ? 0.6603 0.7423 0.5555 -0.0576 0.0484 0.0346 98 LEU B CB 3325 C CG . LEU B 98 ? 0.6805 0.7646 0.5626 -0.0755 0.0541 0.0239 98 LEU B CG 3326 C CD1 . LEU B 98 ? 0.7236 0.7591 0.5694 -0.0863 0.0734 0.0281 98 LEU B CD1 3327 C CD2 . LEU B 98 ? 0.6852 0.8060 0.5684 -0.0887 0.0519 0.0126 98 LEU B CD2 3328 N N . LEU B 99 ? 0.6386 0.7338 0.5585 -0.0391 0.0227 0.0382 99 LEU B N 3329 C CA . LEU B 99 ? 0.6469 0.7391 0.5656 -0.0340 0.0133 0.0344 99 LEU B CA 3330 C C . LEU B 99 ? 0.6387 0.7200 0.5578 -0.0353 0.0126 0.0432 99 LEU B C 3331 O O . LEU B 99 ? 0.6365 0.7126 0.5545 -0.0335 0.0103 0.0404 99 LEU B O 3332 C CB . LEU B 99 ? 0.6703 0.7549 0.5776 -0.0298 0.0057 0.0317 99 LEU B CB 3333 C CG . LEU B 99 ? 0.7059 0.7676 0.5934 -0.0213 -0.0002 0.0281 99 LEU B CG 3334 C CD1 . LEU B 99 ? 0.7199 0.7975 0.6114 -0.0077 0.0005 0.0227 99 LEU B CD1 3335 C CD2 . LEU B 99 ? 0.7420 0.7795 0.6013 -0.0164 -0.0022 0.0238 99 LEU B CD2 3336 N N . VAL B 100 ? 0.6216 0.7078 0.5423 -0.0372 0.0150 0.0551 100 VAL B N 3337 C CA . VAL B 100 ? 0.6185 0.7083 0.5403 -0.0370 0.0154 0.0658 100 VAL B CA 3338 C C . VAL B 100 ? 0.6104 0.6872 0.5310 -0.0311 0.0261 0.0669 100 VAL B C 3339 O O . VAL B 100 ? 0.5985 0.6698 0.5193 -0.0320 0.0236 0.0665 100 VAL B O 3340 C CB . VAL B 100 ? 0.6149 0.7331 0.5386 -0.0368 0.0168 0.0816 100 VAL B CB 3341 C CG1 . VAL B 100 ? 0.6151 0.7509 0.5409 -0.0306 0.0210 0.0958 100 VAL B CG1 3342 C CG2 . VAL B 100 ? 0.6219 0.7493 0.5371 -0.0535 0.0054 0.0794 100 VAL B CG2 3343 N N . LEU B 101 ? 0.6078 0.6724 0.5193 -0.0277 0.0393 0.0678 101 LEU B N 3344 C CA . LEU B 101 ? 0.6223 0.6582 0.5157 -0.0281 0.0537 0.0666 101 LEU B CA 3345 C C . LEU B 101 ? 0.6278 0.6632 0.5232 -0.0412 0.0482 0.0526 101 LEU B C 3346 O O . LEU B 101 ? 0.6438 0.6665 0.5323 -0.0426 0.0522 0.0533 101 LEU B O 3347 C CB . LEU B 101 ? 0.6499 0.6598 0.5185 -0.0306 0.0695 0.0656 101 LEU B CB 3348 C CG . LEU B 101 ? 0.6901 0.6701 0.5298 -0.0113 0.0892 0.0820 101 LEU B CG 3349 C CD1 . LEU B 101 ? 0.6838 0.7030 0.5423 0.0104 0.0839 0.1007 101 LEU B CD1 3350 C CD2 . LEU B 101 ? 0.7201 0.6710 0.5316 -0.0167 0.1022 0.0794 101 LEU B CD2 3351 N N . MET B 102 ? 0.6149 0.6705 0.5186 -0.0481 0.0397 0.0414 102 MET B N 3352 C CA . MET B 102 ? 0.6107 0.6831 0.5156 -0.0565 0.0354 0.0308 102 MET B CA 3353 C C . MET B 102 ? 0.6037 0.6806 0.5183 -0.0469 0.0242 0.0327 102 MET B C 3354 O O . MET B 102 ? 0.6074 0.6876 0.5195 -0.0518 0.0248 0.0299 102 MET B O 3355 C CB . MET B 102 ? 0.6092 0.7148 0.5190 -0.0590 0.0305 0.0218 102 MET B CB 3356 C CG . MET B 102 ? 0.6388 0.7426 0.5330 -0.0772 0.0423 0.0174 102 MET B CG 3357 S SD . MET B 102 ? 0.6678 0.8321 0.5685 -0.0839 0.0367 0.0066 102 MET B SD 3358 C CE . MET B 102 ? 0.6621 0.8300 0.5797 -0.0540 0.0246 0.0103 102 MET B CE 3359 N N . GLU B 103 ? 0.6017 0.6751 0.5208 -0.0368 0.0151 0.0370 103 GLU B N 3360 C CA . GLU B 103 ? 0.6115 0.6765 0.5270 -0.0309 0.0061 0.0382 103 GLU B CA 3361 C C . GLU B 103 ? 0.6144 0.6686 0.5309 -0.0353 0.0081 0.0469 103 GLU B C 3362 O O . GLU B 103 ? 0.6202 0.6677 0.5328 -0.0346 0.0033 0.0469 103 GLU B O 3363 C CB . GLU B 103 ? 0.6245 0.6763 0.5273 -0.0255 -0.0014 0.0381 103 GLU B CB 3364 C CG . GLU B 103 ? 0.6456 0.7069 0.5418 -0.0127 -0.0025 0.0303 103 GLU B CG 3365 C CD . GLU B 103 ? 0.6536 0.7294 0.5444 0.0030 -0.0041 0.0265 103 GLU B CD 3366 O OE1 . GLU B 103 ? 0.6619 0.7249 0.5468 0.0046 -0.0065 0.0291 103 GLU B OE1 3367 O OE2 . GLU B 103 ? 0.6790 0.7868 0.5708 0.0152 -0.0028 0.0221 103 GLU B OE2 3368 N N . ASN B 104 ? 0.6252 0.6803 0.5443 -0.0364 0.0162 0.0557 104 ASN B N 3369 C CA . ASN B 104 ? 0.6350 0.6885 0.5535 -0.0345 0.0211 0.0659 104 ASN B CA 3370 C C . ASN B 104 ? 0.6529 0.6918 0.5652 -0.0368 0.0284 0.0607 104 ASN B C 3371 O O . ASN B 104 ? 0.6520 0.6889 0.5646 -0.0375 0.0257 0.0628 104 ASN B O 3372 C CB . ASN B 104 ? 0.6436 0.7051 0.5597 -0.0251 0.0323 0.0795 104 ASN B CB 3373 C CG . ASN B 104 ? 0.6293 0.7221 0.5519 -0.0273 0.0240 0.0893 104 ASN B CG 3374 O OD1 . ASN B 104 ? 0.6211 0.7175 0.5423 -0.0405 0.0112 0.0850 104 ASN B OD1 3375 N ND2 . ASN B 104 ? 0.6370 0.7509 0.5590 -0.0153 0.0329 0.1032 104 ASN B ND2 3376 N N . GLU B 105 ? 0.6802 0.7092 0.5823 -0.0428 0.0380 0.0532 105 GLU B N 3377 C CA . GLU B 105 ? 0.7197 0.7359 0.6077 -0.0542 0.0459 0.0465 105 GLU B CA 3378 C C . GLU B 105 ? 0.7054 0.7451 0.6053 -0.0575 0.0325 0.0396 105 GLU B C 3379 O O . GLU B 105 ? 0.7140 0.7491 0.6091 -0.0625 0.0340 0.0389 105 GLU B O 3380 C CB . GLU B 105 ? 0.7762 0.7813 0.6425 -0.0705 0.0580 0.0380 105 GLU B CB 3381 C CG . GLU B 105 ? 0.8423 0.8244 0.6787 -0.0912 0.0711 0.0314 105 GLU B CG 3382 C CD . GLU B 105 ? 0.9324 0.8827 0.7281 -0.1131 0.0891 0.0250 105 GLU B CD 3383 O OE1 . GLU B 105 ? 0.9793 0.9645 0.7772 -0.1338 0.0843 0.0147 105 GLU B OE1 3384 O OE2 . GLU B 105 ? 1.0136 0.9031 0.7690 -0.1087 0.1096 0.0313 105 GLU B OE2 3385 N N . ARG B 106 ? 0.6940 0.7565 0.6044 -0.0511 0.0210 0.0356 106 ARG B N 3386 C CA . ARG B 106 ? 0.6968 0.7794 0.6102 -0.0444 0.0109 0.0320 106 ARG B CA 3387 C C . ARG B 106 ? 0.6736 0.7356 0.5851 -0.0369 0.0039 0.0384 106 ARG B C 3388 O O . ARG B 106 ? 0.6826 0.7498 0.5912 -0.0345 0.0002 0.0376 106 ARG B O 3389 C CB . ARG B 106 ? 0.7206 0.8258 0.6350 -0.0312 0.0043 0.0282 106 ARG B CB 3390 C CG . ARG B 106 ? 0.7543 0.8968 0.6706 -0.0423 0.0099 0.0212 106 ARG B CG 3391 C CD . ARG B 106 ? 0.7984 0.9878 0.7157 -0.0241 0.0037 0.0189 106 ARG B CD 3392 N NE . ARG B 106 ? 0.8349 1.0642 0.7515 -0.0207 0.0011 0.0191 106 ARG B NE 3393 C CZ . ARG B 106 ? 0.8759 1.1481 0.7888 0.0069 -0.0037 0.0221 106 ARG B CZ 3394 N NH1 . ARG B 106 ? 0.9217 1.1930 0.8268 0.0346 -0.0052 0.0240 106 ARG B NH1 3395 N NH2 . ARG B 106 ? 0.8893 1.2063 0.8021 0.0102 -0.0056 0.0245 106 ARG B NH2 3396 N N . THR B 107 ? 0.6446 0.6888 0.5552 -0.0363 0.0023 0.0452 107 THR B N 3397 C CA . THR B 107 ? 0.6300 0.6584 0.5326 -0.0376 -0.0040 0.0512 107 THR B CA 3398 C C . THR B 107 ? 0.6135 0.6427 0.5207 -0.0428 0.0008 0.0555 107 THR B C 3399 O O . THR B 107 ? 0.6028 0.6241 0.5034 -0.0442 -0.0045 0.0567 107 THR B O 3400 C CB . THR B 107 ? 0.6237 0.6487 0.5214 -0.0441 -0.0065 0.0580 107 THR B CB 3401 O OG1 . THR B 107 ? 0.6318 0.6469 0.5180 -0.0406 -0.0102 0.0529 107 THR B OG1 3402 C CG2 . THR B 107 ? 0.6409 0.6545 0.5230 -0.0553 -0.0127 0.0635 107 THR B CG2 3403 N N . LEU B 108 ? 0.6030 0.6345 0.5143 -0.0441 0.0129 0.0582 108 LEU B N 3404 C CA . LEU B 108 ? 0.6054 0.6295 0.5126 -0.0456 0.0212 0.0623 108 LEU B CA 3405 C C . LEU B 108 ? 0.6173 0.6401 0.5200 -0.0533 0.0210 0.0530 108 LEU B C 3406 O O . LEU B 108 ? 0.6141 0.6339 0.5150 -0.0555 0.0195 0.0547 108 LEU B O 3407 C CB . LEU B 108 ? 0.6143 0.6253 0.5107 -0.0399 0.0390 0.0683 108 LEU B CB 3408 C CG . LEU B 108 ? 0.6079 0.6345 0.5092 -0.0280 0.0408 0.0812 108 LEU B CG 3409 C CD1 . LEU B 108 ? 0.6371 0.6422 0.5170 -0.0131 0.0624 0.0896 108 LEU B CD1 3410 C CD2 . LEU B 108 ? 0.5998 0.6545 0.5105 -0.0279 0.0316 0.0918 108 LEU B CD2 3411 N N . ASP B 109 ? 0.6196 0.6533 0.5200 -0.0594 0.0225 0.0439 109 ASP B N 3412 C CA . ASP B 109 ? 0.6243 0.6781 0.5213 -0.0692 0.0208 0.0362 109 ASP B CA 3413 C C . ASP B 109 ? 0.6079 0.6764 0.5113 -0.0559 0.0064 0.0379 109 ASP B C 3414 O O . ASP B 109 ? 0.6304 0.7099 0.5312 -0.0594 0.0046 0.0370 109 ASP B O 3415 C CB . ASP B 109 ? 0.6410 0.7215 0.5340 -0.0804 0.0241 0.0277 109 ASP B CB 3416 C CG . ASP B 109 ? 0.6919 0.7435 0.5609 -0.1006 0.0422 0.0241 109 ASP B CG 3417 O OD1 . ASP B 109 ? 0.7107 0.7231 0.5603 -0.1053 0.0544 0.0270 109 ASP B OD1 3418 O OD2 . ASP B 109 ? 0.7166 0.7801 0.5792 -0.1108 0.0460 0.0187 109 ASP B OD2 3419 N N . PHE B 110 ? 0.5860 0.6478 0.4898 -0.0409 -0.0017 0.0408 110 PHE B N 3420 C CA . PHE B 110 ? 0.5809 0.6346 0.4728 -0.0252 -0.0113 0.0433 110 PHE B CA 3421 C C . PHE B 110 ? 0.5919 0.6232 0.4777 -0.0312 -0.0136 0.0483 110 PHE B C 3422 O O . PHE B 110 ? 0.6063 0.6401 0.4834 -0.0244 -0.0174 0.0491 110 PHE B O 3423 C CB . PHE B 110 ? 0.5885 0.6179 0.4667 -0.0145 -0.0153 0.0448 110 PHE B CB 3424 C CG . PHE B 110 ? 0.6212 0.6160 0.4670 0.0009 -0.0207 0.0477 110 PHE B CG 3425 C CD1 . PHE B 110 ? 0.6406 0.6489 0.4731 0.0251 -0.0217 0.0484 110 PHE B CD1 3426 C CD2 . PHE B 110 ? 0.6429 0.5913 0.4629 -0.0092 -0.0230 0.0509 110 PHE B CD2 3427 C CE1 . PHE B 110 ? 0.6881 0.6489 0.4767 0.0453 -0.0230 0.0527 110 PHE B CE1 3428 C CE2 . PHE B 110 ? 0.6948 0.5918 0.4673 0.0010 -0.0246 0.0527 110 PHE B CE2 3429 C CZ . PHE B 110 ? 0.7168 0.6122 0.4706 0.0316 -0.0235 0.0539 110 PHE B CZ 3430 N N . HIS B 111 ? 0.5845 0.6015 0.4744 -0.0422 -0.0107 0.0530 111 HIS B N 3431 C CA . HIS B 111 ? 0.5890 0.5959 0.4752 -0.0500 -0.0117 0.0586 111 HIS B CA 3432 C C . HIS B 111 ? 0.5866 0.6044 0.4786 -0.0542 -0.0064 0.0562 111 HIS B C 3433 O O . HIS B 111 ? 0.6007 0.6131 0.4860 -0.0554 -0.0107 0.0579 111 HIS B O 3434 C CB . HIS B 111 ? 0.5814 0.5927 0.4737 -0.0574 -0.0073 0.0666 111 HIS B CB 3435 C CG . HIS B 111 ? 0.5909 0.5957 0.4711 -0.0636 -0.0141 0.0703 111 HIS B CG 3436 N ND1 . HIS B 111 ? 0.6162 0.5970 0.4696 -0.0739 -0.0221 0.0712 111 HIS B ND1 3437 C CD2 . HIS B 111 ? 0.5885 0.6042 0.4721 -0.0655 -0.0128 0.0732 111 HIS B CD2 3438 C CE1 . HIS B 111 ? 0.6365 0.6113 0.4735 -0.0862 -0.0251 0.0732 111 HIS B CE1 3439 N NE2 . HIS B 111 ? 0.6125 0.6139 0.4716 -0.0804 -0.0204 0.0748 111 HIS B NE2 3440 N N . ASP B 112 ? 0.5773 0.6047 0.4744 -0.0597 0.0040 0.0518 112 ASP B N 3441 C CA . ASP B 112 ? 0.5812 0.6131 0.4728 -0.0713 0.0118 0.0473 112 ASP B CA 3442 C C . ASP B 112 ? 0.5875 0.6465 0.4789 -0.0698 0.0025 0.0435 112 ASP B C 3443 O O . ASP B 112 ? 0.5987 0.6611 0.4864 -0.0750 0.0015 0.0440 112 ASP B O 3444 C CB . ASP B 112 ? 0.6003 0.6275 0.4813 -0.0836 0.0262 0.0413 112 ASP B CB 3445 C CG . ASP B 112 ? 0.6316 0.6396 0.4899 -0.1014 0.0408 0.0374 112 ASP B CG 3446 O OD1 . ASP B 112 ? 0.6311 0.6359 0.4889 -0.1017 0.0390 0.0400 112 ASP B OD1 3447 O OD2 . ASP B 112 ? 0.6551 0.6448 0.4888 -0.1175 0.0557 0.0312 112 ASP B OD2 3448 N N . SER B 113 ? 0.5846 0.6669 0.4785 -0.0588 -0.0035 0.0415 113 SER B N 3449 C CA . SER B 113 ? 0.5830 0.7033 0.4742 -0.0469 -0.0108 0.0416 113 SER B CA 3450 C C . SER B 113 ? 0.5987 0.6951 0.4782 -0.0308 -0.0186 0.0485 113 SER B C 3451 O O . SER B 113 ? 0.6071 0.7263 0.4827 -0.0282 -0.0211 0.0503 113 SER B O 3452 C CB . SER B 113 ? 0.5838 0.7303 0.4754 -0.0285 -0.0140 0.0411 113 SER B CB 3453 O OG . SER B 113 ? 0.5952 0.7776 0.4782 -0.0036 -0.0199 0.0460 113 SER B OG 3454 N N . ASN B 114 ? 0.6086 0.6593 0.4767 -0.0233 -0.0218 0.0525 114 ASN B N 3455 C CA . ASN B 114 ? 0.6360 0.6495 0.4799 -0.0153 -0.0272 0.0583 114 ASN B CA 3456 C C . ASN B 114 ? 0.6355 0.6488 0.4855 -0.0317 -0.0266 0.0597 114 ASN B C 3457 O O . ASN B 114 ? 0.6547 0.6587 0.4879 -0.0241 -0.0306 0.0635 114 ASN B O 3458 C CB . ASN B 114 ? 0.6559 0.6211 0.4796 -0.0192 -0.0290 0.0607 114 ASN B CB 3459 C CG . ASN B 114 ? 0.6793 0.6294 0.4835 0.0000 -0.0290 0.0596 114 ASN B CG 3460 O OD1 . ASN B 114 ? 0.6938 0.6551 0.4845 0.0269 -0.0289 0.0608 114 ASN B OD1 3461 N ND2 . ASN B 114 ? 0.6825 0.6121 0.4828 -0.0119 -0.0284 0.0587 114 ASN B ND2 3462 N N . VAL B 115 ? 0.6181 0.6382 0.4867 -0.0505 -0.0198 0.0577 115 VAL B N 3463 C CA . VAL B 115 ? 0.6248 0.6432 0.4960 -0.0634 -0.0166 0.0594 115 VAL B CA 3464 C C . VAL B 115 ? 0.6273 0.6752 0.5002 -0.0673 -0.0151 0.0551 115 VAL B C 3465 O O . VAL B 115 ? 0.6300 0.6778 0.4965 -0.0686 -0.0184 0.0576 115 VAL B O 3466 C CB . VAL B 115 ? 0.6124 0.6262 0.4930 -0.0739 -0.0056 0.0606 115 VAL B CB 3467 C CG1 . VAL B 115 ? 0.6157 0.6268 0.4937 -0.0828 0.0006 0.0622 115 VAL B CG1 3468 C CG2 . VAL B 115 ? 0.6146 0.6184 0.4949 -0.0725 -0.0083 0.0677 115 VAL B CG2 3469 N N . LYS B 116 ? 0.6325 0.7098 0.5111 -0.0731 -0.0099 0.0488 116 LYS B N 3470 C CA . LYS B 116 ? 0.6480 0.7681 0.5246 -0.0853 -0.0081 0.0443 116 LYS B CA 3471 C C . LYS B 116 ? 0.6545 0.8055 0.5272 -0.0636 -0.0192 0.0504 116 LYS B C 3472 O O . LYS B 116 ? 0.6615 0.8353 0.5308 -0.0698 -0.0206 0.0516 116 LYS B O 3473 C CB . LYS B 116 ? 0.6641 0.8164 0.5414 -0.0996 -0.0015 0.0368 116 LYS B CB 3474 C CG . LYS B 116 ? 0.6940 0.9024 0.5635 -0.1245 0.0016 0.0310 116 LYS B CG 3475 C CD . LYS B 116 ? 0.7350 0.9173 0.5883 -0.1514 0.0110 0.0269 116 LYS B CD 3476 C CE . LYS B 116 ? 0.7703 0.9748 0.5981 -0.1952 0.0237 0.0159 116 LYS B CE 3477 N NZ . LYS B 116 ? 0.7730 1.0734 0.6078 -0.2026 0.0149 0.0158 116 LYS B NZ 3478 N N . ASN B 117 ? 0.6663 0.8135 0.5334 -0.0352 -0.0252 0.0554 117 ASN B N 3479 C CA . ASN B 117 ? 0.6854 0.8527 0.5362 -0.0035 -0.0318 0.0640 117 ASN B CA 3480 C C . ASN B 117 ? 0.7076 0.8293 0.5393 0.0018 -0.0354 0.0701 117 ASN B C 3481 O O . ASN B 117 ? 0.7153 0.8633 0.5365 0.0159 -0.0383 0.0764 117 ASN B O 3482 C CB . ASN B 117 ? 0.6964 0.8508 0.5318 0.0293 -0.0332 0.0682 117 ASN B CB 3483 C CG . ASN B 117 ? 0.6830 0.9032 0.5360 0.0292 -0.0307 0.0643 117 ASN B CG 3484 O OD1 . ASN B 117 ? 0.6671 0.9556 0.5358 0.0084 -0.0291 0.0606 117 ASN B OD1 3485 N ND2 . ASN B 117 ? 0.6948 0.8953 0.5403 0.0479 -0.0299 0.0646 117 ASN B ND2 3486 N N . LEU B 118 ? 0.7213 0.7823 0.5474 -0.0110 -0.0349 0.0690 118 LEU B N 3487 C CA . LEU B 118 ? 0.7514 0.7693 0.5580 -0.0157 -0.0378 0.0737 118 LEU B CA 3488 C C . LEU B 118 ? 0.7426 0.7899 0.5661 -0.0356 -0.0362 0.0716 118 LEU B C 3489 O O . LEU B 118 ? 0.7590 0.7999 0.5674 -0.0307 -0.0396 0.0767 118 LEU B O 3490 C CB . LEU B 118 ? 0.7612 0.7308 0.5618 -0.0326 -0.0372 0.0731 118 LEU B CB 3491 C CG . LEU B 118 ? 0.8008 0.7294 0.5773 -0.0458 -0.0400 0.0776 118 LEU B CG 3492 C CD1 . LEU B 118 ? 0.8715 0.7590 0.6002 -0.0243 -0.0429 0.0837 118 LEU B CD1 3493 C CD2 . LEU B 118 ? 0.8085 0.7105 0.5779 -0.0656 -0.0397 0.0781 118 LEU B CD2 3494 N N . TYR B 119 ? 0.7250 0.7966 0.5721 -0.0580 -0.0292 0.0643 119 TYR B N 3495 C CA . TYR B 119 ? 0.7208 0.8119 0.5739 -0.0794 -0.0242 0.0607 119 TYR B CA 3496 C C . TYR B 119 ? 0.7423 0.8883 0.5926 -0.0744 -0.0282 0.0621 119 TYR B C 3497 O O . TYR B 119 ? 0.7652 0.9196 0.6102 -0.0802 -0.0299 0.0644 119 TYR B O 3498 C CB . TYR B 119 ? 0.7122 0.8043 0.5729 -0.1023 -0.0114 0.0522 119 TYR B CB 3499 C CG . TYR B 119 ? 0.7249 0.8227 0.5774 -0.1275 -0.0022 0.0470 119 TYR B CG 3500 C CD1 . TYR B 119 ? 0.7339 0.7991 0.5813 -0.1324 0.0024 0.0495 119 TYR B CD1 3501 C CD2 . TYR B 119 ? 0.7262 0.8644 0.5709 -0.1494 0.0028 0.0395 119 TYR B CD2 3502 C CE1 . TYR B 119 ? 0.7518 0.8134 0.5845 -0.1542 0.0130 0.0444 119 TYR B CE1 3503 C CE2 . TYR B 119 ? 0.7455 0.8799 0.5718 -0.1784 0.0131 0.0334 119 TYR B CE2 3504 C CZ . TYR B 119 ? 0.7606 0.8511 0.5800 -0.1784 0.0188 0.0357 119 TYR B CZ 3505 O OH . TYR B 119 ? 0.7956 0.8738 0.5903 -0.2056 0.0311 0.0294 119 TYR B OH 3506 N N . ASP B 120 ? 0.7611 0.9538 0.6153 -0.0636 -0.0295 0.0618 120 ASP B N 3507 C CA . ASP B 120 ? 0.7748 1.0445 0.6281 -0.0584 -0.0328 0.0654 120 ASP B CA 3508 C C . ASP B 120 ? 0.8029 1.0693 0.6382 -0.0199 -0.0406 0.0789 120 ASP B C 3509 O O . ASP B 120 ? 0.8184 1.1372 0.6505 -0.0174 -0.0433 0.0844 120 ASP B O 3510 C CB . ASP B 120 ? 0.7748 1.1085 0.6361 -0.0555 -0.0318 0.0634 120 ASP B CB 3511 C CG . ASP B 120 ? 0.7765 1.1228 0.6424 -0.1022 -0.0218 0.0498 120 ASP B CG 3512 O OD1 . ASP B 120 ? 0.8066 1.1443 0.6644 -0.1367 -0.0152 0.0432 120 ASP B OD1 3513 O OD2 . ASP B 120 ? 0.7905 1.1485 0.6608 -0.1050 -0.0188 0.0456 120 ASP B OD2 3514 N N . LYS B 121 ? 0.8365 1.0367 0.6520 0.0078 -0.0427 0.0845 121 LYS B N 3515 C CA . LYS B 121 ? 0.9020 1.0738 0.6819 0.0453 -0.0462 0.0975 121 LYS B CA 3516 C C . LYS B 121 ? 0.9075 1.0563 0.6808 0.0288 -0.0482 0.0990 121 LYS B C 3517 O O . LYS B 121 ? 0.9484 1.1182 0.7031 0.0509 -0.0506 0.1093 121 LYS B O 3518 C CB . LYS B 121 ? 0.9766 1.0611 0.7214 0.0664 -0.0448 0.1005 121 LYS B CB 3519 C CG . LYS B 121 ? 1.0811 1.1206 0.7690 0.1113 -0.0436 0.1145 121 LYS B CG 3520 C CD . LYS B 121 ? 1.1821 1.1311 0.8211 0.1302 -0.0387 0.1160 121 LYS B CD 3521 C CE . LYS B 121 ? 1.2215 1.0865 0.8434 0.0911 -0.0395 0.1091 121 LYS B CE 3522 N NZ . LYS B 121 ? 1.3104 1.0839 0.8731 0.1010 -0.0338 0.1097 121 LYS B NZ 3523 N N . VAL B 122 ? 0.8769 0.9868 0.6639 -0.0067 -0.0465 0.0902 122 VAL B N 3524 C CA . VAL B 122 ? 0.8689 0.9626 0.6537 -0.0264 -0.0474 0.0904 122 VAL B CA 3525 C C . VAL B 122 ? 0.8578 1.0228 0.6621 -0.0443 -0.0461 0.0872 122 VAL B C 3526 O O . VAL B 122 ? 0.8686 1.0455 0.6630 -0.0427 -0.0490 0.0926 122 VAL B O 3527 C CB . VAL B 122 ? 0.8397 0.8873 0.6342 -0.0552 -0.0439 0.0838 122 VAL B CB 3528 C CG1 . VAL B 122 ? 0.8304 0.8754 0.6278 -0.0770 -0.0428 0.0831 122 VAL B CG1 3529 C CG2 . VAL B 122 ? 0.8682 0.8514 0.6348 -0.0461 -0.0464 0.0879 122 VAL B CG2 3530 N N . ARG B 123 ? 0.8504 1.0594 0.6755 -0.0652 -0.0408 0.0781 123 ARG B N 3531 C CA . ARG B 123 ? 0.8733 1.1474 0.7057 -0.0932 -0.0375 0.0730 123 ARG B CA 3532 C C . ARG B 123 ? 0.9070 1.2572 0.7332 -0.0700 -0.0447 0.0844 123 ARG B C 3533 O O . ARG B 123 ? 0.9194 1.3065 0.7430 -0.0857 -0.0457 0.0857 123 ARG B O 3534 C CB . ARG B 123 ? 0.8763 1.1782 0.7177 -0.1205 -0.0292 0.0617 123 ARG B CB 3535 C CG . ARG B 123 ? 0.9017 1.2509 0.7360 -0.1651 -0.0217 0.0525 123 ARG B CG 3536 C CD . ARG B 123 ? 0.9288 1.2955 0.7579 -0.1959 -0.0117 0.0412 123 ARG B CD 3537 N NE . ARG B 123 ? 0.9289 1.3556 0.7704 -0.1729 -0.0187 0.0465 123 ARG B NE 3538 C CZ . ARG B 123 ? 0.9412 1.4726 0.7865 -0.1663 -0.0256 0.0538 123 ARG B CZ 3539 N NH1 . ARG B 123 ? 0.9478 1.5405 0.7866 -0.1840 -0.0279 0.0565 123 ARG B NH1 3540 N NH2 . ARG B 123 ? 0.9357 1.5182 0.7906 -0.1396 -0.0300 0.0597 123 ARG B NH2 3541 N N . LEU B 124 ? 0.9425 1.3180 0.7630 -0.0294 -0.0487 0.0943 124 LEU B N 3542 C CA . LEU B 124 ? 0.9912 1.4482 0.8016 0.0062 -0.0535 0.1098 124 LEU B CA 3543 C C . LEU B 124 ? 1.0275 1.4448 0.8106 0.0363 -0.0571 0.1229 124 LEU B C 3544 O O . LEU B 124 ? 1.0655 1.5540 0.8391 0.0614 -0.0599 0.1367 124 LEU B O 3545 C CB . LEU B 124 ? 1.0196 1.5033 0.8228 0.0515 -0.0536 0.1189 124 LEU B CB 3546 C CG . LEU B 124 ? 1.0204 1.5680 0.8478 0.0268 -0.0508 0.1091 124 LEU B CG 3547 C CD1 . LEU B 124 ? 1.0413 1.5722 0.8598 0.0704 -0.0496 0.1150 124 LEU B CD1 3548 C CD2 . LEU B 124 ? 1.0085 1.6954 0.8478 0.0068 -0.0521 0.1119 124 LEU B CD2 3549 N N . GLN B 125 ? 1.0348 1.3441 0.8019 0.0335 -0.0566 0.1199 125 GLN B N 3550 C CA . GLN B 125 ? 1.0659 1.3224 0.7990 0.0535 -0.0587 0.1306 125 GLN B CA 3551 C C . GLN B 125 ? 1.0346 1.3077 0.7827 0.0151 -0.0602 0.1250 125 GLN B C 3552 O O . GLN B 125 ? 1.0749 1.3783 0.8086 0.0295 -0.0631 0.1357 125 GLN B O 3553 C CB . GLN B 125 ? 1.1108 1.2485 0.8123 0.0584 -0.0570 0.1293 125 GLN B CB 3554 C CG . GLN B 125 ? 1.1748 1.2712 0.8379 0.1040 -0.0536 0.1379 125 GLN B CG 3555 C CD . GLN B 125 ? 1.2505 1.2232 0.8593 0.1060 -0.0508 0.1394 125 GLN B CD 3556 O OE1 . GLN B 125 ? 1.3478 1.2643 0.8953 0.1410 -0.0470 0.1523 125 GLN B OE1 3557 N NE2 . GLN B 125 ? 1.2386 1.1688 0.8628 0.0667 -0.0512 0.1270 125 GLN B NE2 3558 N N . LEU B 126 ? 1.0034 1.2544 0.7758 -0.0302 -0.0568 0.1095 126 LEU B N 3559 C CA . LEU B 126 ? 1.0089 1.2618 0.7891 -0.0658 -0.0552 0.1034 126 LEU B CA 3560 C C . LEU B 126 ? 1.0467 1.3965 0.8383 -0.0848 -0.0549 0.1021 126 LEU B C 3561 O O . LEU B 126 ? 1.0681 1.4398 0.8535 -0.0938 -0.0569 0.1056 126 LEU B O 3562 C CB . LEU B 126 ? 0.9652 1.1698 0.7601 -0.1009 -0.0477 0.0895 126 LEU B CB 3563 C CG . LEU B 126 ? 0.9640 1.0898 0.7495 -0.0914 -0.0484 0.0910 126 LEU B CG 3564 C CD1 . LEU B 126 ? 0.9466 1.0457 0.7473 -0.1204 -0.0396 0.0811 126 LEU B CD1 3565 C CD2 . LEU B 126 ? 0.9949 1.0763 0.7510 -0.0781 -0.0542 0.1009 126 LEU B CD2 3566 N N . ARG B 127 ? 1.1074 1.5182 0.9122 -0.0949 -0.0522 0.0969 127 ARG B N 3567 C CA . ARG B 127 ? 1.1670 1.6834 0.9769 -0.1222 -0.0514 0.0951 127 ARG B CA 3568 C C . ARG B 127 ? 1.1606 1.6653 0.9654 -0.1751 -0.0445 0.0826 127 ARG B C 3569 O O . ARG B 127 ? 1.1568 1.6112 0.9582 -0.2110 -0.0333 0.0673 127 ARG B O 3570 C CB . ARG B 127 ? 1.2301 1.8334 1.0331 -0.0794 -0.0601 0.1153 127 ARG B CB 3571 C CG . ARG B 127 ? 1.2712 1.9162 1.0744 -0.0328 -0.0623 0.1265 127 ARG B CG 3572 C CD . ARG B 127 ? 1.3222 1.9772 1.1002 0.0367 -0.0668 0.1505 127 ARG B CD 3573 N NE . ARG B 127 ? 1.3619 2.1113 1.1353 0.0423 -0.0707 0.1636 127 ARG B NE 3574 C CZ . ARG B 127 ? 1.4316 2.2013 1.1767 0.1046 -0.0726 0.1874 127 ARG B CZ 3575 N NH1 . ARG B 127 ? 1.4863 2.1766 1.1968 0.1660 -0.0691 0.1996 127 ARG B NH1 3576 N NH2 . ARG B 127 ? 1.4415 2.3074 1.1853 0.1061 -0.0762 0.1996 127 ARG B NH2 3577 N N . ASP B 128 ? 1.1667 1.7102 0.9645 -0.1764 -0.0491 0.0900 128 ASP B N 3578 C CA . ASP B 128 ? 1.1723 1.7097 0.9596 -0.2267 -0.0417 0.0786 128 ASP B CA 3579 C C . ASP B 128 ? 1.1694 1.6202 0.9516 -0.2185 -0.0417 0.0797 128 ASP B C 3580 O O . ASP B 128 ? 1.1914 1.6204 0.9624 -0.2549 -0.0337 0.0702 128 ASP B O 3581 C CB . ASP B 128 ? 1.2140 1.8701 0.9960 -0.2457 -0.0462 0.0845 128 ASP B CB 3582 C CG . ASP B 128 ? 1.2445 1.9625 1.0311 -0.1874 -0.0594 0.1083 128 ASP B CG 3583 O OD1 . ASP B 128 ? 1.2607 1.9696 1.0515 -0.1371 -0.0637 0.1191 128 ASP B OD1 3584 O OD2 . ASP B 128 ? 1.2856 2.0560 1.0655 -0.1896 -0.0639 0.1169 128 ASP B OD2 3585 N N . ASN B 129 ? 1.1533 1.5523 0.9371 -0.1741 -0.0490 0.0907 129 ASN B N 3586 C CA . ASN B 129 ? 1.1449 1.4680 0.9207 -0.1700 -0.0497 0.0926 129 ASN B CA 3587 C C . ASN B 129 ? 1.1158 1.3637 0.8957 -0.1897 -0.0396 0.0807 129 ASN B C 3588 O O . ASN B 129 ? 1.1091 1.3050 0.8840 -0.1893 -0.0394 0.0824 129 ASN B O 3589 C CB . ASN B 129 ? 1.1839 1.4724 0.9446 -0.1225 -0.0592 0.1085 129 ASN B CB 3590 C CG . ASN B 129 ? 1.2311 1.5811 0.9770 -0.0937 -0.0665 0.1247 129 ASN B CG 3591 O OD1 . ASN B 129 ? 1.2527 1.6732 1.0005 -0.0697 -0.0689 0.1329 129 ASN B OD1 3592 N ND2 . ASN B 129 ? 1.2628 1.5922 0.9925 -0.0932 -0.0694 0.1310 129 ASN B ND2 3593 N N . ALA B 130 ? 1.0801 1.3273 0.8661 -0.2052 -0.0304 0.0703 130 ALA B N 3594 C CA . ALA B 130 ? 1.0522 1.2354 0.8378 -0.2166 -0.0181 0.0618 130 ALA B CA 3595 C C . ALA B 130 ? 1.0401 1.2260 0.8142 -0.2480 -0.0022 0.0482 130 ALA B C 3596 O O . ALA B 130 ? 1.0306 1.2691 0.8037 -0.2591 -0.0036 0.0452 130 ALA B O 3597 C CB . ALA B 130 ? 1.0472 1.1946 0.8430 -0.1878 -0.0235 0.0676 130 ALA B CB 3598 N N . LYS B 131 ? 1.0437 1.1714 0.8022 -0.2611 0.0144 0.0411 131 LYS B N 3599 C CA . LYS B 131 ? 1.0789 1.1794 0.8075 -0.2899 0.0352 0.0282 131 LYS B CA 3600 C C . LYS B 131 ? 1.0536 1.1239 0.7891 -0.2719 0.0401 0.0282 131 LYS B C 3601 O O . LYS B 131 ? 1.0276 1.0603 0.7736 -0.2465 0.0420 0.0346 131 LYS B O 3602 C CB . LYS B 131 ? 1.1530 1.1954 0.8490 -0.3044 0.0549 0.0230 131 LYS B CB 3603 C CG . LYS B 131 ? 1.2429 1.2308 0.8847 -0.3350 0.0826 0.0096 131 LYS B CG 3604 C CD . LYS B 131 ? 1.3466 1.2838 0.9465 -0.3504 0.1018 0.0049 131 LYS B CD 3605 C CE . LYS B 131 ? 1.4000 1.3785 0.9802 -0.3945 0.0987 -0.0029 131 LYS B CE 3606 N NZ . LYS B 131 ? 1.4652 1.3855 0.9930 -0.4162 0.1208 -0.0101 131 LYS B NZ 3607 N N . GLU B 132 ? 1.0233 1.1186 0.7525 -0.2871 0.0419 0.0219 132 GLU B N 3608 C CA . GLU B 132 ? 0.9864 1.0571 0.7209 -0.2723 0.0464 0.0215 132 GLU B CA 3609 C C . GLU B 132 ? 1.0204 1.0123 0.7130 -0.2827 0.0734 0.0145 132 GLU B C 3610 O O . GLU B 132 ? 1.0749 1.0438 0.7212 -0.3192 0.0911 0.0026 132 GLU B O 3611 C CB . GLU B 132 ? 0.9743 1.1032 0.7126 -0.2869 0.0401 0.0173 132 GLU B CB 3612 C CG . GLU B 132 ? 0.9610 1.0726 0.7089 -0.2701 0.0417 0.0175 132 GLU B CG 3613 C CD . GLU B 132 ? 0.9463 1.1274 0.7008 -0.2823 0.0342 0.0147 132 GLU B CD 3614 O OE1 . GLU B 132 ? 0.9640 1.2075 0.7069 -0.3126 0.0323 0.0108 132 GLU B OE1 3615 O OE2 . GLU B 132 ? 0.9279 1.1091 0.6987 -0.2623 0.0304 0.0170 132 GLU B OE2 3616 N N . LEU B 133 ? 0.9971 0.9478 0.6984 -0.2507 0.0783 0.0228 133 LEU B N 3617 C CA . LEU B 133 ? 1.0445 0.9204 0.7007 -0.2470 0.1067 0.0211 133 LEU B CA 3618 C C . LEU B 133 ? 1.0746 0.9070 0.6957 -0.2537 0.1250 0.0148 133 LEU B C 3619 O O . LEU B 133 ? 1.1262 0.8840 0.6856 -0.2610 0.1540 0.0100 133 LEU B O 3620 C CB . LEU B 133 ? 1.0437 0.9093 0.7209 -0.2073 0.1067 0.0353 133 LEU B CB 3621 C CG . LEU B 133 ? 1.0651 0.9229 0.7331 -0.2054 0.1117 0.0390 133 LEU B CG 3622 C CD1 . LEU B 133 ? 1.0390 0.9476 0.7329 -0.2245 0.0891 0.0370 133 LEU B CD1 3623 C CD2 . LEU B 133 ? 1.0493 0.9150 0.7384 -0.1685 0.1116 0.0546 133 LEU B CD2 3624 N N . GLY B 134 ? 1.0419 0.9131 0.6947 -0.2494 0.1101 0.0153 134 GLY B N 3625 C CA . GLY B 134 ? 1.0708 0.9070 0.6934 -0.2574 0.1249 0.0094 134 GLY B CA 3626 C C . GLY B 134 ? 1.0646 0.8745 0.7005 -0.2161 0.1297 0.0205 134 GLY B C 3627 O O . GLY B 134 ? 1.1064 0.8737 0.7095 -0.2172 0.1461 0.0175 134 GLY B O 3628 N N . ASN B 135 ? 1.0053 0.8438 0.6850 -0.1831 0.1157 0.0337 135 ASN B N 3629 C CA . ASN B 135 ? 0.9927 0.8238 0.6864 -0.1462 0.1192 0.0465 135 ASN B CA 3630 C C . ASN B 135 ? 0.9168 0.8078 0.6689 -0.1313 0.0913 0.0546 135 ASN B C 3631 O O . ASN B 135 ? 0.8870 0.7880 0.6547 -0.1060 0.0906 0.0665 135 ASN B O 3632 C CB . ASN B 135 ? 1.0293 0.8298 0.6996 -0.1207 0.1382 0.0572 135 ASN B CB 3633 C CG . ASN B 135 ? 1.0116 0.8491 0.7079 -0.1225 0.1240 0.0613 135 ASN B CG 3634 O OD1 . ASN B 135 ? 0.9721 0.8539 0.7039 -0.1381 0.0993 0.0580 135 ASN B OD1 3635 N ND2 . ASN B 135 ? 1.0593 0.8762 0.7324 -0.1037 0.1413 0.0696 135 ASN B ND2 3636 N N . GLY B 136 ? 0.8822 0.8119 0.6585 -0.1469 0.0702 0.0492 136 GLY B N 3637 C CA . GLY B 136 ? 0.8342 0.8017 0.6478 -0.1346 0.0467 0.0561 136 GLY B CA 3638 C C . GLY B 136 ? 0.8197 0.8031 0.6421 -0.1370 0.0347 0.0602 136 GLY B C 3639 O O . GLY B 136 ? 0.7738 0.7752 0.6119 -0.1315 0.0169 0.0645 136 GLY B O 3640 N N . CYS B 137 ? 0.8608 0.8296 0.6653 -0.1454 0.0462 0.0589 137 CYS B N 3641 C CA . CYS B 137 ? 0.8681 0.8501 0.6790 -0.1478 0.0366 0.0637 137 CYS B CA 3642 C C . CYS B 137 ? 0.8764 0.8704 0.6792 -0.1671 0.0321 0.0564 137 CYS B C 3643 O O . CYS B 137 ? 0.8785 0.8647 0.6601 -0.1854 0.0440 0.0469 137 CYS B O 3644 C CB . CYS B 137 ? 0.8870 0.8552 0.6867 -0.1387 0.0515 0.0709 137 CYS B CB 3645 S SG . CYS B 137 ? 0.9096 0.8913 0.7217 -0.1134 0.0553 0.0847 137 CYS B SG 3646 N N . PHE B 138 ? 0.8760 0.8889 0.6895 -0.1652 0.0156 0.0615 138 PHE B N 3647 C CA . PHE B 138 ? 0.8984 0.9318 0.7057 -0.1784 0.0098 0.0584 138 PHE B CA 3648 C C . PHE B 138 ? 0.9240 0.9484 0.7266 -0.1819 0.0100 0.0631 138 PHE B C 3649 O O . PHE B 138 ? 0.9173 0.9381 0.7264 -0.1725 0.0003 0.0715 138 PHE B O 3650 C CB . PHE B 138 ? 0.8846 0.9453 0.7006 -0.1658 -0.0084 0.0629 138 PHE B CB 3651 C CG . PHE B 138 ? 0.8850 0.9665 0.7067 -0.1604 -0.0094 0.0593 138 PHE B CG 3652 C CD1 . PHE B 138 ? 0.8851 1.0099 0.7026 -0.1753 -0.0075 0.0533 138 PHE B CD1 3653 C CD2 . PHE B 138 ? 0.8979 0.9630 0.7276 -0.1437 -0.0126 0.0622 138 PHE B CD2 3654 C CE1 . PHE B 138 ? 0.8808 1.0352 0.7035 -0.1721 -0.0086 0.0506 138 PHE B CE1 3655 C CE2 . PHE B 138 ? 0.8939 0.9800 0.7288 -0.1380 -0.0133 0.0590 138 PHE B CE2 3656 C CZ . PHE B 138 ? 0.8909 1.0233 0.7232 -0.1514 -0.0114 0.0534 138 PHE B CZ 3657 N N . GLU B 139 ? 0.9636 0.9825 0.7489 -0.1993 0.0221 0.0571 139 GLU B N 3658 C CA . GLU B 139 ? 0.9874 1.0005 0.7664 -0.2040 0.0239 0.0607 139 GLU B CA 3659 C C . GLU B 139 ? 0.9760 1.0173 0.7554 -0.2139 0.0100 0.0611 139 GLU B C 3660 O O . GLU B 139 ? 0.9846 1.0481 0.7548 -0.2308 0.0119 0.0542 139 GLU B O 3661 C CB . GLU B 139 ? 1.0535 1.0346 0.8036 -0.2146 0.0485 0.0541 139 GLU B CB 3662 C CG . GLU B 139 ? 1.1070 1.0818 0.8465 -0.2187 0.0539 0.0570 139 GLU B CG 3663 C CD . GLU B 139 ? 1.2099 1.1383 0.9081 -0.2229 0.0831 0.0512 139 GLU B CD 3664 O OE1 . GLU B 139 ? 1.2564 1.1547 0.9404 -0.2038 0.1001 0.0538 139 GLU B OE1 3665 O OE2 . GLU B 139 ? 1.2826 1.1998 0.9557 -0.2437 0.0908 0.0447 139 GLU B OE2 3666 N N . PHE B 140 ? 0.9684 1.0114 0.7533 -0.2055 -0.0030 0.0701 140 PHE B N 3667 C CA . PHE B 140 ? 0.9731 1.0377 0.7535 -0.2063 -0.0165 0.0741 140 PHE B CA 3668 C C . PHE B 140 ? 1.0077 1.0817 0.7774 -0.2265 -0.0102 0.0703 140 PHE B C 3669 O O . PHE B 140 ? 0.9977 1.0502 0.7612 -0.2347 0.0018 0.0682 140 PHE B O 3670 C CB . PHE B 140 ? 0.9558 1.0008 0.7304 -0.1933 -0.0296 0.0847 140 PHE B CB 3671 C CG . PHE B 140 ? 0.9494 0.9796 0.7230 -0.1754 -0.0364 0.0884 140 PHE B CG 3672 C CD1 . PHE B 140 ? 0.9396 0.9538 0.7212 -0.1752 -0.0320 0.0880 140 PHE B CD1 3673 C CD2 . PHE B 140 ? 0.9696 1.0038 0.7303 -0.1558 -0.0460 0.0938 140 PHE B CD2 3674 C CE1 . PHE B 140 ? 0.9464 0.9445 0.7233 -0.1623 -0.0377 0.0906 140 PHE B CE1 3675 C CE2 . PHE B 140 ? 0.9807 0.9923 0.7325 -0.1376 -0.0499 0.0970 140 PHE B CE2 3676 C CZ . PHE B 140 ? 0.9728 0.9641 0.7328 -0.1441 -0.0462 0.0943 140 PHE B CZ 3677 N N . TYR B 141 ? 1.0394 1.1505 0.8047 -0.2320 -0.0178 0.0710 141 TYR B N 3678 C CA . TYR B 141 ? 1.0899 1.2161 0.8432 -0.2534 -0.0142 0.0682 141 TYR B CA 3679 C C . TYR B 141 ? 1.1207 1.2360 0.8709 -0.2438 -0.0251 0.0785 141 TYR B C 3680 O O . TYR B 141 ? 1.1433 1.2445 0.8866 -0.2576 -0.0190 0.0769 141 TYR B O 3681 C CB . TYR B 141 ? 1.0738 1.2605 0.8227 -0.2672 -0.0176 0.0658 141 TYR B CB 3682 C CG . TYR B 141 ? 1.0725 1.2691 0.8141 -0.2892 -0.0049 0.0537 141 TYR B CG 3683 C CD1 . TYR B 141 ? 1.0913 1.2407 0.8095 -0.3148 0.0161 0.0413 141 TYR B CD1 3684 C CD2 . TYR B 141 ? 1.0541 1.3021 0.8045 -0.2830 -0.0119 0.0554 141 TYR B CD2 3685 C CE1 . TYR B 141 ? 1.1095 1.2519 0.8069 -0.3385 0.0305 0.0298 141 TYR B CE1 3686 C CE2 . TYR B 141 ? 1.0619 1.3182 0.8004 -0.3094 0.0000 0.0437 141 TYR B CE2 3687 C CZ . TYR B 141 ? 1.1037 1.3016 0.8127 -0.3394 0.0214 0.0304 141 TYR B CZ 3688 O OH . TYR B 141 ? 1.1473 1.3394 0.8309 -0.3690 0.0357 0.0184 141 TYR B OH 3689 N N . HIS B 142 ? 1.4910 1.5582 0.8172 -0.4082 0.0715 0.0526 142 HIS B N 3690 C CA . HIS B 142 ? 1.5277 1.6190 0.8093 -0.4384 0.0727 0.0808 142 HIS B CA 3691 C C . HIS B 142 ? 1.4787 1.5695 0.8044 -0.4126 0.1038 0.0632 142 HIS B C 3692 O O . HIS B 142 ? 1.4092 1.4743 0.8004 -0.3695 0.1126 0.0470 142 HIS B O 3693 C CB . HIS B 142 ? 1.5400 1.6091 0.8183 -0.4433 0.0263 0.1522 142 HIS B CB 3694 C CG . HIS B 142 ? 1.4741 1.4997 0.8264 -0.3919 0.0131 0.1713 142 HIS B CG 3695 N ND1 . HIS B 142 ? 1.4436 1.4593 0.8300 -0.3741 0.0131 0.1910 142 HIS B ND1 3696 C CD2 . HIS B 142 ? 1.4453 1.4425 0.8429 -0.3581 0.0010 0.1705 142 HIS B CD2 3697 C CE1 . HIS B 142 ? 1.4002 1.3868 0.8448 -0.3329 0.0031 0.1962 142 HIS B CE1 3698 N NE2 . HIS B 142 ? 1.4020 1.3792 0.8532 -0.3233 -0.0029 0.1861 142 HIS B NE2 3699 N N . LYS B 143 ? 1.5102 1.6339 0.8010 -0.4429 0.1182 0.0706 143 LYS B N 3700 C CA . LYS B 143 ? 1.4756 1.5996 0.8095 -0.4223 0.1435 0.0602 143 LYS B CA 3701 C C . LYS B 143 ? 1.4020 1.4863 0.7737 -0.3927 0.1118 0.1123 143 LYS B C 3702 O O . LYS B 143 ? 1.4012 1.4750 0.7555 -0.4065 0.0751 0.1605 143 LYS B O 3703 C CB . LYS B 143 ? 1.5574 1.7363 0.8432 -0.4688 0.1701 0.0521 143 LYS B CB 3704 C CG . LYS B 143 ? 1.5629 1.7603 0.8965 -0.4550 0.2159 0.0026 143 LYS B CG 3705 C CD . LYS B 143 ? 1.5513 1.7368 0.9160 -0.4420 0.2110 0.0399 143 LYS B CD 3706 C CE . LYS B 143 ? 1.6043 1.8384 0.9111 -0.4950 0.2147 0.0709 143 LYS B CE 3707 N NZ . LYS B 143 ? 1.5779 1.7958 0.9259 -0.4815 0.2036 0.1112 143 LYS B NZ 3708 N N . CYS B 144 ? 1.3348 1.3998 0.7661 -0.3537 0.1236 0.1002 144 CYS B N 3709 C CA . CYS B 144 ? 1.2662 1.2987 0.7387 -0.3225 0.0972 0.1335 144 CYS B CA 3710 C C . CYS B 144 ? 1.2289 1.2635 0.7347 -0.3111 0.1092 0.1336 144 CYS B C 3711 O O . CYS B 144 ? 1.2054 1.2384 0.7499 -0.2872 0.1293 0.1059 144 CYS B O 3712 C CB . CYS B 144 ? 1.2179 1.2265 0.7293 -0.2847 0.0914 0.1215 144 CYS B CB 3713 S SG . CYS B 144 ? 1.1883 1.1715 0.7439 -0.2511 0.0631 0.1494 144 CYS B SG 3714 N N . ASP B 145 ? 1.2445 1.2832 0.7439 -0.3301 0.0925 0.1689 145 ASP B N 3715 C CA . ASP B 145 ? 1.2212 1.2616 0.7564 -0.3221 0.0995 0.1727 145 ASP B CA 3716 C C . ASP B 145 ? 1.1650 1.1753 0.7557 -0.2816 0.0797 0.1758 145 ASP B C 3717 O O . ASP B 145 ? 1.1369 1.1312 0.7365 -0.2600 0.0680 0.1708 145 ASP B O 3718 C CB . ASP B 145 ? 1.2530 1.3144 0.7683 -0.3626 0.0874 0.2125 145 ASP B CB 3719 C CG . ASP B 145 ? 1.2656 1.3081 0.7941 -0.3712 0.0398 0.2619 145 ASP B CG 3720 O OD1 . ASP B 145 ? 1.2232 1.2353 0.7861 -0.3401 0.0193 0.2593 145 ASP B OD1 3721 O OD2 . ASP B 145 ? 1.3299 1.3930 0.8422 -0.4121 0.0219 0.3055 145 ASP B OD2 3722 N N . ASN B 146 ? 1.1577 1.1660 0.7853 -0.2740 0.0770 0.1813 146 ASN B N 3723 C CA . ASN B 146 ? 1.1329 1.1228 0.8093 -0.2396 0.0615 0.1740 146 ASN B CA 3724 C C . ASN B 146 ? 1.1532 1.1263 0.8554 -0.2319 0.0275 0.1909 146 ASN B C 3725 O O . ASN B 146 ? 1.1488 1.1161 0.8758 -0.2047 0.0214 0.1726 146 ASN B O 3726 C CB . ASN B 146 ? 1.1106 1.1039 0.8239 -0.2362 0.0645 0.1727 146 ASN B CB 3727 C CG . ASN B 146 ? 1.0984 1.1075 0.8110 -0.2363 0.0974 0.1500 146 ASN B CG 3728 O OD1 . ASN B 146 ? 1.0949 1.1103 0.7923 -0.2329 0.1166 0.1297 146 ASN B OD1 3729 N ND2 . ASN B 146 ? 1.0989 1.1145 0.8423 -0.2402 0.1021 0.1527 146 ASN B ND2 3730 N N . GLU B 147 ? 1.2161 1.1871 0.9196 -0.2586 0.0047 0.2259 147 GLU B N 3731 C CA . GLU B 147 ? 1.2453 1.1999 0.9905 -0.2540 -0.0305 0.2432 147 GLU B CA 3732 C C . GLU B 147 ? 1.2042 1.1555 0.9223 -0.2448 -0.0273 0.2321 147 GLU B C 3733 O O . GLU B 147 ? 1.1853 1.1282 0.9442 -0.2215 -0.0392 0.2190 147 GLU B O 3734 C CB . GLU B 147 ? 1.3340 1.2895 1.0925 -0.2918 -0.0625 0.2953 147 GLU B CB 3735 C CG . GLU B 147 ? 1.3704 1.3227 1.1949 -0.2971 -0.0829 0.3152 147 GLU B CG 3736 C CD . GLU B 147 ? 1.4176 1.3911 1.2064 -0.3143 -0.0555 0.3168 147 GLU B CD 3737 O OE1 . GLU B 147 ? 1.4846 1.4833 1.2201 -0.3554 -0.0489 0.3474 147 GLU B OE1 3738 O OE2 . GLU B 147 ? 1.4369 1.4070 1.2521 -0.2894 -0.0403 0.2863 147 GLU B OE2 3739 N N . CYS B 148 ? 1.1950 1.1574 0.8492 -0.2647 -0.0098 0.2337 148 CYS B N 3740 C CA . CYS B 148 ? 1.1782 1.1377 0.8077 -0.2588 -0.0071 0.2239 148 CYS B CA 3741 C C . CYS B 148 ? 1.1225 1.0814 0.7695 -0.2223 0.0108 0.1901 148 CYS B C 3742 O O . CYS B 148 ? 1.1229 1.0776 0.7848 -0.2073 0.0029 0.1862 148 CYS B O 3743 C CB . CYS B 148 ? 1.2198 1.1963 0.7830 -0.2887 0.0110 0.2211 148 CYS B CB 3744 S SG . CYS B 148 ? 1.2373 1.2107 0.7787 -0.2783 0.0197 0.1985 148 CYS B SG 3745 N N . MET B 149 ? 1.0766 1.0441 0.7254 -0.2116 0.0329 0.1702 149 MET B N 3746 C CA . MET B 149 ? 1.0171 0.9913 0.6849 -0.1837 0.0436 0.1485 149 MET B CA 3747 C C . MET B 149 ? 1.0119 0.9873 0.7197 -0.1653 0.0271 0.1435 149 MET B C 3748 O O . MET B 149 ? 0.9981 0.9831 0.7158 -0.1508 0.0259 0.1345 149 MET B O 3749 C CB . MET B 149 ? 0.9923 0.9758 0.6655 -0.1804 0.0632 0.1349 149 MET B CB 3750 C CG . MET B 149 ? 1.0021 0.9914 0.6552 -0.1954 0.0856 0.1251 149 MET B CG 3751 S SD . MET B 149 ? 0.9919 0.9820 0.6415 -0.1888 0.0901 0.1158 149 MET B SD 3752 C CE . MET B 149 ? 0.9871 0.9887 0.6419 -0.2046 0.1193 0.0876 149 MET B CE 3753 N N . GLU B 150 ? 1.0352 1.0056 0.7724 -0.1678 0.0152 0.1462 150 GLU B N 3754 C CA . GLU B 150 ? 1.0503 1.0251 0.8401 -0.1513 0.0001 0.1295 150 GLU B CA 3755 C C . GLU B 150 ? 1.0518 1.0239 0.8697 -0.1469 -0.0147 0.1303 150 GLU B C 3756 O O . GLU B 150 ? 1.0344 1.0249 0.8840 -0.1294 -0.0132 0.1025 150 GLU B O 3757 C CB . GLU B 150 ? 1.0864 1.0506 0.9193 -0.1586 -0.0167 0.1366 150 GLU B CB 3758 C CG . GLU B 150 ? 1.1024 1.0717 1.0080 -0.1419 -0.0336 0.1089 150 GLU B CG 3759 C CD . GLU B 150 ? 1.1001 1.0983 0.9987 -0.1228 -0.0176 0.0684 150 GLU B CD 3760 O OE1 . GLU B 150 ? 1.0984 1.1061 0.9514 -0.1237 -0.0007 0.0706 150 GLU B OE1 3761 O OE2 . GLU B 150 ? 1.1077 1.1240 1.0522 -0.1097 -0.0231 0.0332 150 GLU B OE2 3762 N N . SER B 151 ? 1.0770 1.0322 0.8842 -0.1657 -0.0285 0.1606 151 SER B N 3763 C CA . SER B 151 ? 1.0919 1.0416 0.9363 -0.1638 -0.0474 0.1671 151 SER B CA 3764 C C . SER B 151 ? 1.0776 1.0440 0.9007 -0.1485 -0.0291 0.1492 151 SER B C 3765 O O . SER B 151 ? 1.0728 1.0482 0.9431 -0.1366 -0.0355 0.1362 151 SER B O 3766 C CB . SER B 151 ? 1.1216 1.0533 0.9522 -0.1939 -0.0714 0.2110 151 SER B CB 3767 O OG . SER B 151 ? 1.1367 1.0714 0.8917 -0.2073 -0.0552 0.2183 151 SER B OG 3768 N N . VAL B 152 ? 1.0680 1.0414 0.8323 -0.1500 -0.0073 0.1488 152 VAL B N 3769 C CA . VAL B 152 ? 1.0535 1.0465 0.8056 -0.1377 0.0074 0.1387 152 VAL B CA 3770 C C . VAL B 152 ? 1.0538 1.0803 0.8284 -0.1201 0.0183 0.1112 152 VAL B C 3771 O O . VAL B 152 ? 1.0615 1.1135 0.8544 -0.1114 0.0229 0.0999 152 VAL B O 3772 C CB . VAL B 152 ? 1.0471 1.0399 0.7539 -0.1440 0.0237 0.1447 152 VAL B CB 3773 C CG1 . VAL B 152 ? 1.0209 1.0362 0.7306 -0.1332 0.0328 0.1429 152 VAL B CG1 3774 C CG2 . VAL B 152 ? 1.0713 1.0425 0.7485 -0.1657 0.0172 0.1608 152 VAL B CG2 3775 N N . ARG B 153 ? 1.0693 1.1016 0.8415 -0.1182 0.0228 0.0996 153 ARG B N 3776 C CA . ARG B 153 ? 1.0977 1.1684 0.8846 -0.1071 0.0304 0.0701 153 ARG B CA 3777 C C . ARG B 153 ? 1.1354 1.2176 0.9828 -0.0988 0.0218 0.0396 153 ARG B C 3778 O O . ARG B 153 ? 1.1268 1.2539 0.9869 -0.0919 0.0329 0.0078 153 ARG B O 3779 C CB . ARG B 153 ? 1.0865 1.1575 0.8632 -0.1088 0.0320 0.0653 153 ARG B CB 3780 C CG . ARG B 153 ? 1.0731 1.1368 0.8133 -0.1157 0.0411 0.0881 153 ARG B CG 3781 C CD . ARG B 153 ? 1.0657 1.1368 0.8078 -0.1162 0.0416 0.0821 153 ARG B CD 3782 N NE . ARG B 153 ? 1.0676 1.1144 0.8013 -0.1245 0.0479 0.0992 153 ARG B NE 3783 C CZ . ARG B 153 ? 1.0845 1.1076 0.8253 -0.1323 0.0467 0.1025 153 ARG B CZ 3784 N NH1 . ARG B 153 ? 1.0865 1.1003 0.8508 -0.1323 0.0332 0.0967 153 ARG B NH1 3785 N NH2 . ARG B 153 ? 1.1096 1.1226 0.8429 -0.1420 0.0592 0.1109 153 ARG B NH2 3786 N N . ASN B 154 ? 1.2109 1.2579 1.1022 -0.1025 0.0013 0.0488 154 ASN B N 3787 C CA . ASN B 154 ? 1.2443 1.2943 1.2226 -0.0948 -0.0134 0.0230 154 ASN B CA 3788 C C . ASN B 154 ? 1.2201 1.2922 1.2240 -0.0882 -0.0067 0.0108 154 ASN B C 3789 O O . ASN B 154 ? 1.2159 1.3226 1.2799 -0.0774 0.0001 -0.0348 154 ASN B O 3790 C CB . ASN B 154 ? 1.3164 1.3216 1.3406 -0.1069 -0.0452 0.0567 154 ASN B CB 3791 C CG . ASN B 154 ? 1.4266 1.4180 1.4770 -0.1111 -0.0579 0.0567 154 ASN B CG 3792 O OD1 . ASN B 154 ? 1.4494 1.4595 1.4763 -0.1042 -0.0426 0.0314 154 ASN B OD1 3793 N ND2 . ASN B 154 ? 1.5518 1.5127 1.6558 -0.1254 -0.0900 0.0905 154 ASN B ND2 3794 N N . GLY B 155 ? 1.2011 1.2567 1.1640 -0.0960 -0.0076 0.0475 155 GLY B N 3795 C CA . GLY B 155 ? 1.1805 1.2425 1.1815 -0.0930 -0.0108 0.0490 155 GLY B CA 3796 C C . GLY B 155 ? 1.1881 1.2067 1.2427 -0.1032 -0.0459 0.0799 155 GLY B C 3797 O O . GLY B 155 ? 1.1876 1.2055 1.2977 -0.1014 -0.0572 0.0830 155 GLY B O 3798 N N . THR B 156 ? 1.2121 1.1986 1.2520 -0.1174 -0.0649 0.1076 156 THR B N 3799 C CA . THR B 156 ? 1.2508 1.2034 1.3428 -0.1351 -0.1048 0.1466 156 THR B CA 3800 C C . THR B 156 ? 1.2846 1.2159 1.2900 -0.1623 -0.1133 0.1957 156 THR B C 3801 O O . THR B 156 ? 1.3324 1.2444 1.3437 -0.1871 -0.1420 0.2349 156 THR B O 3802 C CB . THR B 156 ? 1.2830 1.2246 1.4402 -0.1375 -0.1251 0.1440 156 THR B CB 3803 O OG1 . THR B 156 ? 1.2726 1.2421 1.4914 -0.1128 -0.1085 0.0833 156 THR B OG1 3804 C CG2 . THR B 156 ? 1.3288 1.2431 1.5807 -0.1554 -0.1750 0.1858 156 THR B CG2 3805 N N . TYR B 157 ? 1.2849 1.2252 1.2142 -0.1609 -0.0891 0.1927 157 TYR B N 3806 C CA . TYR B 157 ? 1.3187 1.2461 1.1701 -0.1867 -0.0923 0.2243 157 TYR B CA 3807 C C . TYR B 157 ? 1.4046 1.3184 1.2761 -0.2035 -0.1234 0.2558 157 TYR B C 3808 O O . TYR B 157 ? 1.3790 1.2983 1.2673 -0.1910 -0.1191 0.2466 157 TYR B O 3809 C CB . TYR B 157 ? 1.2761 1.2173 1.0607 -0.1781 -0.0581 0.2050 157 TYR B CB 3810 C CG . TYR B 157 ? 1.2516 1.1848 0.9690 -0.2028 -0.0577 0.2220 157 TYR B CG 3811 C CD1 . TYR B 157 ? 1.2366 1.1707 0.9041 -0.2226 -0.0481 0.2250 157 TYR B CD1 3812 C CD2 . TYR B 157 ? 1.2383 1.1680 0.9465 -0.2078 -0.0652 0.2298 157 TYR B CD2 3813 C CE1 . TYR B 157 ? 1.2507 1.1877 0.8592 -0.2480 -0.0429 0.2282 157 TYR B CE1 3814 C CE2 . TYR B 157 ? 1.2488 1.1760 0.8985 -0.2322 -0.0645 0.2353 157 TYR B CE2 3815 C CZ . TYR B 157 ? 1.2526 1.1860 0.8518 -0.2527 -0.0518 0.2309 157 TYR B CZ 3816 O OH . TYR B 157 ? 1.2750 1.2155 0.8187 -0.2794 -0.0467 0.2247 157 TYR B OH 3817 N N . ASP B 158 ? 1.5468 1.4470 1.4187 -0.2353 -0.1571 0.2975 158 ASP B N 3818 C CA . ASP B 158 ? 1.6999 1.5885 1.5933 -0.2586 -0.1962 0.3370 158 ASP B CA 3819 C C . ASP B 158 ? 1.8233 1.7161 1.6210 -0.2805 -0.1885 0.3446 158 ASP B C 3820 O O . ASP B 158 ? 1.8722 1.7743 1.5893 -0.3069 -0.1787 0.3508 158 ASP B O 3821 C CB . ASP B 158 ? 1.7289 1.6081 1.6639 -0.2921 -0.2433 0.3893 158 ASP B CB 3822 C CG . ASP B 158 ? 1.7090 1.5772 1.7868 -0.2735 -0.2716 0.3892 158 ASP B CG 3823 O OD1 . ASP B 158 ? 1.6962 1.5618 1.8472 -0.2521 -0.2762 0.3717 158 ASP B OD1 3824 O OD2 . ASP B 158 ? 1.6817 1.5462 1.8086 -0.2809 -0.2890 0.4040 158 ASP B OD2 3825 N N . TYR B 159 ? 1.9207 1.8103 1.7347 -0.2704 -0.1918 0.3394 159 TYR B N 3826 C CA . TYR B 159 ? 2.0465 1.9376 1.7899 -0.2936 -0.1950 0.3475 159 TYR B CA 3827 C C . TYR B 159 ? 2.1728 2.0636 1.8823 -0.3447 -0.2380 0.3971 159 TYR B C 3828 O O . TYR B 159 ? 2.2018 2.1079 1.8192 -0.3757 -0.2291 0.3949 159 TYR B O 3829 C CB . TYR B 159 ? 2.0578 1.9446 1.8447 -0.2730 -0.1969 0.3386 159 TYR B CB 3830 C CG . TYR B 159 ? 2.1443 2.0274 1.8864 -0.3008 -0.2177 0.3556 159 TYR B CG 3831 C CD1 . TYR B 159 ? 2.2059 2.0791 1.9758 -0.3304 -0.2686 0.4009 159 TYR B CD1 3832 C CD2 . TYR B 159 ? 2.1574 2.0479 1.8402 -0.2991 -0.1907 0.3263 159 TYR B CD2 3833 C CE1 . TYR B 159 ? 2.2683 2.1414 1.9930 -0.3593 -0.2907 0.4149 159 TYR B CE1 3834 C CE2 . TYR B 159 ? 2.2225 2.1114 1.8693 -0.3252 -0.2105 0.3338 159 TYR B CE2 3835 C CZ . TYR B 159 ? 2.2895 2.1709 1.9503 -0.3560 -0.2598 0.3772 159 TYR B CZ 3836 O OH . TYR B 159 ? 2.3264 2.2095 1.9472 -0.3852 -0.2824 0.3834 159 TYR B OH 3837 N N . PRO B 160 ? 2.2552 2.1343 2.0449 -0.3568 -0.2857 0.4413 160 PRO B N 3838 C CA . PRO B 160 ? 2.3150 2.1995 2.0780 -0.4125 -0.3362 0.5024 160 PRO B CA 3839 C C . PRO B 160 ? 2.3038 2.2113 1.9899 -0.4506 -0.3318 0.5214 160 PRO B C 3840 O O . PRO B 160 ? 2.3301 2.2601 1.9426 -0.5046 -0.3563 0.5583 160 PRO B O 3841 C CB . PRO B 160 ? 2.3309 2.1963 2.2317 -0.4090 -0.3877 0.5439 160 PRO B CB 3842 C CG . PRO B 160 ? 2.2800 2.1337 2.2675 -0.3530 -0.3606 0.4945 160 PRO B CG 3843 C CD . PRO B 160 ? 2.2375 2.1032 2.1564 -0.3229 -0.2978 0.4365 160 PRO B CD 3844 N N . GLN B 161 ? 2.2204 2.1281 1.9236 -0.4262 -0.3016 0.4969 161 GLN B N 3845 C CA . GLN B 161 ? 2.1979 2.1300 1.8377 -0.4586 -0.2915 0.5114 161 GLN B CA 3846 C C . GLN B 161 ? 2.1891 2.1498 1.7052 -0.4755 -0.2468 0.4725 161 GLN B C 3847 O O . GLN B 161 ? 2.2403 2.2353 1.6826 -0.5219 -0.2445 0.4908 161 GLN B O 3848 C CB . GLN B 161 ? 2.1130 2.0354 1.8137 -0.4237 -0.2707 0.4898 161 GLN B CB 3849 C CG . GLN B 161 ? 2.0936 2.0397 1.7531 -0.4569 -0.2666 0.5136 161 GLN B CG 3850 C CD . GLN B 161 ? 2.0168 1.9505 1.7463 -0.4221 -0.2516 0.4924 161 GLN B CD 3851 O OE1 . GLN B 161 ? 1.9627 1.8726 1.7835 -0.3795 -0.2545 0.4674 161 GLN B OE1 3852 N NE2 . GLN B 161 ? 2.0043 1.9593 1.6921 -0.4423 -0.2343 0.4989 161 GLN B NE2 3853 N N . TYR B 162 ? 2.1034 2.0549 1.6072 -0.4397 -0.2113 0.4180 162 TYR B N 3854 C CA . TYR B 162 ? 2.0800 2.0550 1.4954 -0.4510 -0.1716 0.3728 162 TYR B CA 3855 C C . TYR B 162 ? 2.0229 1.9933 1.4214 -0.4562 -0.1842 0.3635 162 TYR B C 3856 O O . TYR B 162 ? 1.9665 1.9615 1.2925 -0.4833 -0.1690 0.3361 162 TYR B O 3857 C CB . TYR B 162 ? 2.0451 2.0143 1.4762 -0.4052 -0.1209 0.3177 162 TYR B CB 3858 C CG . TYR B 162 ? 2.0396 2.0077 1.5024 -0.3918 -0.1105 0.3231 162 TYR B CG 3859 C CD1 . TYR B 162 ? 2.0683 2.0646 1.4819 -0.4215 -0.0927 0.3235 162 TYR B CD1 3860 C CD2 . TYR B 162 ? 1.9840 1.9283 1.5286 -0.3511 -0.1167 0.3231 162 TYR B CD2 3861 C CE1 . TYR B 162 ? 2.0334 2.0274 1.4827 -0.4092 -0.0855 0.3298 162 TYR B CE1 3862 C CE2 . TYR B 162 ? 1.9543 1.8979 1.5318 -0.3394 -0.1096 0.3233 162 TYR B CE2 3863 C CZ . TYR B 162 ? 1.9821 1.9472 1.5139 -0.3675 -0.0960 0.3294 162 TYR B CZ 3864 O OH . TYR B 162 ? 1.9475 1.9105 1.5185 -0.3558 -0.0915 0.3311 162 TYR B OH # _database_PDB_caveat.id 1 _database_PDB_caveat.text 'NAG A1325 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 ASN 182 182 182 ASN ASN 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 ARG 192 192 192 ARG ARG 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 SIA 1 1322 1322 SIA SIA A . D 4 GAL 2 1323 1323 GAL GAL A . E 5 NAG 3 1324 1324 NAG NAG A . F 5 NAG 1 1325 1325 NAG NAG A . G 5 NAG 2 1326 1326 NAG NAG A . H 5 NAG 1 1327 1327 NAG NAG A . I 6 MPO 1 1163 1163 MPO MPO B . J 5 NAG 1 1164 1164 NAG NAG B . K 5 NAG 2 1165 1165 NAG NAG B . L 7 HOH 1 2001 2001 HOH HOH A . L 7 HOH 2 2002 2002 HOH HOH A . L 7 HOH 3 2003 2003 HOH HOH A . L 7 HOH 4 2004 2004 HOH HOH A . L 7 HOH 5 2005 2005 HOH HOH A . L 7 HOH 6 2006 2006 HOH HOH A . L 7 HOH 7 2007 2007 HOH HOH A . L 7 HOH 8 2008 2008 HOH HOH A . L 7 HOH 9 2009 2009 HOH HOH A . L 7 HOH 10 2010 2010 HOH HOH A . L 7 HOH 11 2011 2011 HOH HOH A . L 7 HOH 12 2012 2012 HOH HOH A . L 7 HOH 13 2013 2013 HOH HOH A . L 7 HOH 14 2014 2014 HOH HOH A . L 7 HOH 15 2015 2015 HOH HOH A . L 7 HOH 16 2016 2016 HOH HOH A . L 7 HOH 17 2017 2017 HOH HOH A . L 7 HOH 18 2018 2018 HOH HOH A . L 7 HOH 19 2019 2019 HOH HOH A . L 7 HOH 20 2020 2020 HOH HOH A . L 7 HOH 21 2021 2021 HOH HOH A . L 7 HOH 22 2022 2022 HOH HOH A . L 7 HOH 23 2023 2023 HOH HOH A . L 7 HOH 24 2024 2024 HOH HOH A . L 7 HOH 25 2025 2025 HOH HOH A . L 7 HOH 26 2026 2026 HOH HOH A . L 7 HOH 27 2027 2027 HOH HOH A . L 7 HOH 28 2028 2028 HOH HOH A . L 7 HOH 29 2029 2029 HOH HOH A . L 7 HOH 30 2030 2030 HOH HOH A . L 7 HOH 31 2031 2031 HOH HOH A . L 7 HOH 32 2032 2032 HOH HOH A . L 7 HOH 33 2033 2033 HOH HOH A . L 7 HOH 34 2034 2034 HOH HOH A . L 7 HOH 35 2035 2035 HOH HOH A . L 7 HOH 36 2036 2036 HOH HOH A . L 7 HOH 37 2037 2037 HOH HOH A . L 7 HOH 38 2038 2038 HOH HOH A . L 7 HOH 39 2039 2039 HOH HOH A . L 7 HOH 40 2040 2040 HOH HOH A . L 7 HOH 41 2041 2041 HOH HOH A . L 7 HOH 42 2042 2042 HOH HOH A . L 7 HOH 43 2043 2043 HOH HOH A . L 7 HOH 44 2044 2044 HOH HOH A . L 7 HOH 45 2045 2045 HOH HOH A . L 7 HOH 46 2046 2046 HOH HOH A . L 7 HOH 47 2047 2047 HOH HOH A . L 7 HOH 48 2048 2048 HOH HOH A . L 7 HOH 49 2049 2049 HOH HOH A . L 7 HOH 50 2050 2050 HOH HOH A . L 7 HOH 51 2051 2051 HOH HOH A . L 7 HOH 52 2052 2052 HOH HOH A . L 7 HOH 53 2053 2053 HOH HOH A . L 7 HOH 54 2054 2054 HOH HOH A . L 7 HOH 55 2055 2055 HOH HOH A . M 7 HOH 1 2001 2001 HOH HOH B . M 7 HOH 2 2002 2002 HOH HOH B . M 7 HOH 3 2003 2003 HOH HOH B . M 7 HOH 4 2004 2004 HOH HOH B . M 7 HOH 5 2005 2005 HOH HOH B . M 7 HOH 6 2006 2006 HOH HOH B . M 7 HOH 7 2007 2007 HOH HOH B . M 7 HOH 8 2008 2008 HOH HOH B . M 7 HOH 9 2009 2009 HOH HOH B . M 7 HOH 10 2010 2010 HOH HOH B . M 7 HOH 11 2011 2011 HOH HOH B . M 7 HOH 12 2012 2012 HOH HOH B . M 7 HOH 13 2013 2013 HOH HOH B . M 7 HOH 14 2014 2014 HOH HOH B . M 7 HOH 15 2015 2015 HOH HOH B . M 7 HOH 16 2016 2016 HOH HOH B . M 7 HOH 17 2017 2017 HOH HOH B . M 7 HOH 18 2018 2018 HOH HOH B . M 7 HOH 19 2019 2019 HOH HOH B . M 7 HOH 20 2020 2020 HOH HOH B . M 7 HOH 21 2021 2021 HOH HOH B . M 7 HOH 22 2022 2022 HOH HOH B . M 7 HOH 23 2023 2023 HOH HOH B . M 7 HOH 24 2024 2024 HOH HOH B . M 7 HOH 25 2025 2025 HOH HOH B . M 7 HOH 26 2026 2026 HOH HOH B . M 7 HOH 27 2027 2027 HOH HOH B . M 7 HOH 28 2028 2028 HOH HOH B . M 7 HOH 29 2029 2029 HOH HOH B . M 7 HOH 30 2030 2030 HOH HOH B . M 7 HOH 31 2031 2031 HOH HOH B . M 7 HOH 32 2032 2032 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 23 A ASN 23 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 165 A ASN 165 ? ASN 'GLYCOSYLATION SITE' 3 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 # 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)' 35160 ? 1 MORE -63.6 ? 1 'SSA (A^2)' 60190 ? # 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_565 -y,x-y+1,z -0.5000000000 -0.8660254038 0.0000000000 -50.5745000000 0.8660254038 -0.5000000000 0.0000000000 87.5976035674 0.0000000000 0.0000000000 1.0000000000 0.0000000000 3 'crystal symmetry operation' 3_455 -x+y-1,-x,z -0.5000000000 0.8660254038 0.0000000000 -101.1490000000 -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 -29.3125 35.6782 56.0648 0.2160 0.3668 0.1328 -0.1279 -0.0673 0.0384 0.1019 0.1625 3.5818 0.0457 0.2112 0.0119 -0.0516 0.0455 0.0443 0.0687 -0.0855 -0.0906 -0.3220 0.7415 0.1371 'X-RAY DIFFRACTION' 2 ? refined -34.7946 41.3370 91.3109 0.4493 0.4412 0.0316 -0.0784 -0.0960 -0.0203 1.5747 1.2813 2.0177 -0.5444 -0.6408 0.4453 -0.2861 -0.4971 0.0421 0.1399 0.2186 -0.0070 -0.3493 0.3922 0.0675 'X-RAY DIFFRACTION' 3 ? refined -30.4676 35.0077 47.9598 0.2041 0.3498 0.1196 -0.0706 -0.0679 0.0233 0.2450 0.6483 7.6511 0.1115 1.2229 0.5192 0.0177 0.1216 -0.0040 0.0597 -0.1115 -0.1110 -0.2483 0.2574 0.0938 'X-RAY DIFFRACTION' 4 ? refined -36.1814 37.5394 16.3212 0.2146 0.2211 0.1686 -0.0741 -0.0038 0.0493 2.6444 0.2467 6.4143 0.6226 -1.8338 -0.6624 -0.1311 -0.1076 0.1606 -0.0437 0.0206 -0.0372 -0.7318 0.6216 0.1105 'X-RAY DIFFRACTION' 5 ? refined -43.5899 28.1035 64.4692 0.1794 0.2554 0.1431 -0.0135 -0.0108 0.0430 1.2158 3.5563 14.9885 -0.0174 -1.0979 -4.6373 -0.2228 0.0442 0.1881 0.1524 -0.0614 -0.1225 0.1779 0.7120 0.2842 'X-RAY DIFFRACTION' 6 ? refined -42.8656 31.7615 18.2408 0.2704 0.3274 0.1698 -0.0555 0.0015 0.0428 1.0274 0.3805 10.4564 0.5834 -2.1845 -1.1707 -0.2476 0.1409 0.0004 -0.0689 -0.0106 0.0059 -0.0184 -0.6453 0.2582 'X-RAY DIFFRACTION' 7 ? refined -38.1248 44.0166 -5.7018 0.5337 0.4756 0.1830 -0.2437 -0.0368 0.2310 11.9564 5.4460 0.6578 3.9748 2.4034 0.0273 -0.8614 0.9200 1.0878 -0.8855 0.6571 0.4540 -0.1568 0.1946 0.2044 # 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 MOSFLM 'data reduction' . ? 2 SCALA 'data scaling' . ? 3 PHASER phasing . ? 4 # _pdbx_entry_details.entry_id 4CQZ _pdbx_entry_details.compound_details ? _pdbx_entry_details.source_details ? _pdbx_entry_details.nonpolymer_details ? _pdbx_entry_details.sequence_details 'MULTIBASIC SITE REMOVED' # _pdbx_validate_close_contact.id 1 _pdbx_validate_close_contact.PDB_model_num 1 _pdbx_validate_close_contact.auth_atom_id_1 OG _pdbx_validate_close_contact.auth_asym_id_1 A _pdbx_validate_close_contact.auth_comp_id_1 SER _pdbx_validate_close_contact.auth_seq_id_1 124 _pdbx_validate_close_contact.PDB_ins_code_1 ? _pdbx_validate_close_contact.label_alt_id_1 ? _pdbx_validate_close_contact.auth_atom_id_2 O _pdbx_validate_close_contact.auth_asym_id_2 A _pdbx_validate_close_contact.auth_comp_id_2 HOH _pdbx_validate_close_contact.auth_seq_id_2 2035 _pdbx_validate_close_contact.PDB_ins_code_2 ? _pdbx_validate_close_contact.label_alt_id_2 ? _pdbx_validate_close_contact.dist 2.07 # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 ARG A 53 ? ? 63.32 -115.23 2 1 ASN A 72 ? ? 51.05 73.18 3 1 ASP A 88 ? ? -94.75 -122.13 4 1 SER A 142 ? ? -128.05 -161.55 5 1 ARG A 192 ? ? 61.79 -59.23 6 1 ARG A 208 ? ? -151.70 87.33 7 1 ARG B 127 ? ? 54.59 -105.70 # loop_ _pdbx_validate_chiral.id _pdbx_validate_chiral.PDB_model_num _pdbx_validate_chiral.auth_atom_id _pdbx_validate_chiral.label_alt_id _pdbx_validate_chiral.auth_asym_id _pdbx_validate_chiral.auth_comp_id _pdbx_validate_chiral.auth_seq_id _pdbx_validate_chiral.PDB_ins_code _pdbx_validate_chiral.details _pdbx_validate_chiral.omega 1 1 C1 ? A NAG 1325 ? PLANAR . 2 1 C1 ? B NAG 1164 ? 'WRONG HAND' . # _pdbx_distant_solvent_atoms.id 1 _pdbx_distant_solvent_atoms.PDB_model_num 1 _pdbx_distant_solvent_atoms.auth_atom_id O _pdbx_distant_solvent_atoms.label_alt_id ? _pdbx_distant_solvent_atoms.auth_asym_id B _pdbx_distant_solvent_atoms.auth_comp_id HOH _pdbx_distant_solvent_atoms.auth_seq_id 2032 _pdbx_distant_solvent_atoms.PDB_ins_code ? _pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 6.06 _pdbx_distant_solvent_atoms.neighbor_ligand_distance . # 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 'O-SIALIC ACID' SIA 4 BETA-D-GALACTOSE GAL 5 N-ACETYL-D-GLUCOSAMINE NAG 6 '3[N-MORPHOLINO]PROPANE SULFONIC ACID' MPO 7 water HOH #