data_4CQS # _entry.id 4CQS # _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 4CQS PDBE EBI-59783 WWPDB D_1290059783 # 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 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 4CQZ unspecified 'CRYSTAL STRUCTURE OF H5 (VN1194) GLN196ARG MUTANT HAEMAGGLUTININ' PDB 4CR0 unspecified 'CRYSTAL STRUCTURE OF H5 (VN1194) ASN186LYS/GLY143ARG MUTANT HAEMAGGLUTININ' # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 4CQS _pdbx_database_status.deposit_site PDBE _pdbx_database_status.process_site PDBE _pdbx_database_status.SG_entry . _pdbx_database_status.recvd_initial_deposition_date 2014-02-21 _pdbx_database_status.pdb_format_compatible Y _pdbx_database_status.status_code_sf ? _pdbx_database_status.status_code_mr ? _pdbx_database_status.status_code_cs ? _pdbx_database_status.methods_development_category ? # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Xiong, X.' 1 'Xiao, H.' 2 'Martin, S.R.' 3 'Coombs, P.J.' 4 'Liu, J.' 5 'Collins, P.J.' 6 'Vachieri, S.G.' 7 'Walker, P.A.' 8 'Lin, Y.P.' 9 'McCauley, J.W.' 10 'Gamblin, S.J.' 11 'Skehel, J.J.' 12 # _citation.id primary _citation.title 'Enhanced Human Receptor Binding by H5 Haemagglutinins.' _citation.journal_abbrev Virology _citation.journal_volume 456 _citation.page_first 179 _citation.page_last ? _citation.year 2014 _citation.journal_id_ASTM VIRLAX _citation.country US _citation.journal_id_ISSN 0042-6822 _citation.journal_id_CSD 0922 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 24889237 _citation.pdbx_database_id_DOI 10.1016/J.VIROL.2014.03.008 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Xiong, X.' 1 primary 'Xiao, H.' 2 primary 'Martin, S.R.' 3 primary 'Coombs, P.J.' 4 primary 'Liu, J.' 5 primary 'Collins, P.J.' 6 primary 'Vachieri, S.G.' 7 primary 'Walker, P.A.' 8 primary 'Lin, Y.P.' 9 primary 'Mccauley, J.W.' 10 primary 'Gamblin, S.J.' 11 primary 'Skehel, J.J.' 12 # _cell.entry_id 4CQS _cell.length_a 101.201 _cell.length_b 101.201 _cell.length_c 451.666 _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 4CQS _symmetry.space_group_name_H-M 'H 3 2' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 155 # loop_ _entity.id _entity.type _entity.src_method _entity.pdbx_description _entity.formula_weight _entity.pdbx_number_of_molecules _entity.pdbx_ec _entity.pdbx_mutation _entity.pdbx_fragment _entity.details 1 polymer nat 'HAEMAGGLUTININ HA1' 36965.844 1 ? YES 'HA1 OF TRYPSIN RELEASED ECTODOMAIN, RESIDUES 17-342' ? 2 polymer nat 'HAEMAGGLUTININ HA2' 19097.990 1 ? ? 'HA2 OF TRYPSIN RELEASED ECTODOMAIN, RESIDUES 347-512' ? 3 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 8 ? ? ? ? 4 non-polymer man ALPHA-D-MANNOSE 180.156 2 ? ? ? ? 5 non-polymer man BETA-D-MANNOSE 180.156 2 ? ? ? ? 6 non-polymer syn '3[N-MORPHOLINO]PROPANE SULFONIC ACID' 209.263 2 ? ? ? ? 7 water nat water 18.015 164 ? ? ? ? # loop_ _entity_poly.entity_id _entity_poly.type _entity_poly.nstd_linkage _entity_poly.nstd_monomer _entity_poly.pdbx_seq_one_letter_code _entity_poly.pdbx_seq_one_letter_code_can _entity_poly.pdbx_strand_id _entity_poly.pdbx_target_identifier 1 'polypeptide(L)' no no ;DQICIGYHANNSTEQVDTIMEKNVTVTHAQDILEKTHNGKLCDLDGVKPLILRDCSVAGWLLGNPMCDEFINVPEWSYIV EKANPVNDLCYPGDFNDYEELKHLLSRINHFEKIQIIPKSSWSSHEASLGVSSACPYQGKSSFFRNVVWLIKKNSTYPTI KRSYNNTNQEDLLVLWGIHHPKDAAEQTKLYQNPTTYISVGTSTLNQRLVPRIATRSKVNGQSGRMEFFWTILKPNDAIN FESNGNFIAPEYAYKIVKKGDSTIMKSELEYGNCNTKCQTPMGAINSSMPFHNIHPLTIGECPKYVKSNRLVLATGLRNS PQRETR ; ;DQICIGYHANNSTEQVDTIMEKNVTVTHAQDILEKTHNGKLCDLDGVKPLILRDCSVAGWLLGNPMCDEFINVPEWSYIV EKANPVNDLCYPGDFNDYEELKHLLSRINHFEKIQIIPKSSWSSHEASLGVSSACPYQGKSSFFRNVVWLIKKNSTYPTI KRSYNNTNQEDLLVLWGIHHPKDAAEQTKLYQNPTTYISVGTSTLNQRLVPRIATRSKVNGQSGRMEFFWTILKPNDAIN FESNGNFIAPEYAYKIVKKGDSTIMKSELEYGNCNTKCQTPMGAINSSMPFHNIHPLTIGECPKYVKSNRLVLATGLRNS PQRETR ; A ? 2 'polypeptide(L)' no no ;GLFGAIAGFIEGGWQGMVDGWYGYHHSNEQGSGYAADKESTQKAIDGVTNKVNSIIDKMNTQFEAVGREFNNLERRIENL NKKMEDGFLDVWTYNAELLVLMENERTLDFHDSNVKNLYDKVRLQLRDNAKELGNGCFEFYHKCDNECMESVRNGTYDYP QYSEEA ; ;GLFGAIAGFIEGGWQGMVDGWYGYHHSNEQGSGYAADKESTQKAIDGVTNKVNSIIDKMNTQFEAVGREFNNLERRIENL NKKMEDGFLDVWTYNAELLVLMENERTLDFHDSNVKNLYDKVRLQLRDNAKELGNGCFEFYHKCDNECMESVRNGTYDYP QYSEEA ; B ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 ASP n 1 2 GLN n 1 3 ILE n 1 4 CYS n 1 5 ILE n 1 6 GLY n 1 7 TYR n 1 8 HIS n 1 9 ALA n 1 10 ASN n 1 11 ASN n 1 12 SER n 1 13 THR n 1 14 GLU n 1 15 GLN n 1 16 VAL n 1 17 ASP n 1 18 THR n 1 19 ILE n 1 20 MET n 1 21 GLU n 1 22 LYS n 1 23 ASN n 1 24 VAL n 1 25 THR n 1 26 VAL n 1 27 THR n 1 28 HIS n 1 29 ALA n 1 30 GLN n 1 31 ASP n 1 32 ILE n 1 33 LEU n 1 34 GLU n 1 35 LYS n 1 36 THR n 1 37 HIS n 1 38 ASN n 1 39 GLY n 1 40 LYS n 1 41 LEU n 1 42 CYS n 1 43 ASP n 1 44 LEU n 1 45 ASP n 1 46 GLY n 1 47 VAL n 1 48 LYS n 1 49 PRO n 1 50 LEU n 1 51 ILE n 1 52 LEU n 1 53 ARG n 1 54 ASP n 1 55 CYS n 1 56 SER n 1 57 VAL n 1 58 ALA n 1 59 GLY n 1 60 TRP n 1 61 LEU n 1 62 LEU n 1 63 GLY n 1 64 ASN n 1 65 PRO n 1 66 MET n 1 67 CYS n 1 68 ASP n 1 69 GLU n 1 70 PHE n 1 71 ILE n 1 72 ASN n 1 73 VAL n 1 74 PRO n 1 75 GLU n 1 76 TRP n 1 77 SER n 1 78 TYR n 1 79 ILE n 1 80 VAL n 1 81 GLU n 1 82 LYS n 1 83 ALA n 1 84 ASN n 1 85 PRO n 1 86 VAL n 1 87 ASN n 1 88 ASP n 1 89 LEU n 1 90 CYS n 1 91 TYR n 1 92 PRO n 1 93 GLY n 1 94 ASP n 1 95 PHE n 1 96 ASN n 1 97 ASP n 1 98 TYR n 1 99 GLU n 1 100 GLU n 1 101 LEU n 1 102 LYS n 1 103 HIS n 1 104 LEU n 1 105 LEU n 1 106 SER n 1 107 ARG n 1 108 ILE n 1 109 ASN n 1 110 HIS n 1 111 PHE n 1 112 GLU n 1 113 LYS n 1 114 ILE n 1 115 GLN n 1 116 ILE n 1 117 ILE n 1 118 PRO n 1 119 LYS n 1 120 SER n 1 121 SER n 1 122 TRP n 1 123 SER n 1 124 SER n 1 125 HIS n 1 126 GLU n 1 127 ALA n 1 128 SER n 1 129 LEU n 1 130 GLY n 1 131 VAL n 1 132 SER n 1 133 SER n 1 134 ALA n 1 135 CYS n 1 136 PRO n 1 137 TYR n 1 138 GLN n 1 139 GLY n 1 140 LYS n 1 141 SER n 1 142 SER n 1 143 PHE n 1 144 PHE n 1 145 ARG n 1 146 ASN n 1 147 VAL n 1 148 VAL n 1 149 TRP n 1 150 LEU n 1 151 ILE n 1 152 LYS n 1 153 LYS n 1 154 ASN n 1 155 SER n 1 156 THR n 1 157 TYR n 1 158 PRO n 1 159 THR n 1 160 ILE n 1 161 LYS n 1 162 ARG n 1 163 SER n 1 164 TYR n 1 165 ASN n 1 166 ASN n 1 167 THR n 1 168 ASN n 1 169 GLN n 1 170 GLU n 1 171 ASP n 1 172 LEU n 1 173 LEU n 1 174 VAL n 1 175 LEU n 1 176 TRP n 1 177 GLY n 1 178 ILE n 1 179 HIS n 1 180 HIS n 1 181 PRO n 1 182 LYS n 1 183 ASP n 1 184 ALA n 1 185 ALA n 1 186 GLU n 1 187 GLN n 1 188 THR n 1 189 LYS n 1 190 LEU n 1 191 TYR n 1 192 GLN n 1 193 ASN n 1 194 PRO n 1 195 THR n 1 196 THR n 1 197 TYR n 1 198 ILE n 1 199 SER n 1 200 VAL n 1 201 GLY n 1 202 THR n 1 203 SER n 1 204 THR n 1 205 LEU n 1 206 ASN n 1 207 GLN n 1 208 ARG n 1 209 LEU n 1 210 VAL n 1 211 PRO n 1 212 ARG n 1 213 ILE n 1 214 ALA n 1 215 THR n 1 216 ARG n 1 217 SER n 1 218 LYS n 1 219 VAL n 1 220 ASN n 1 221 GLY n 1 222 GLN n 1 223 SER n 1 224 GLY n 1 225 ARG n 1 226 MET n 1 227 GLU n 1 228 PHE n 1 229 PHE n 1 230 TRP n 1 231 THR n 1 232 ILE n 1 233 LEU n 1 234 LYS n 1 235 PRO n 1 236 ASN n 1 237 ASP n 1 238 ALA n 1 239 ILE n 1 240 ASN n 1 241 PHE n 1 242 GLU n 1 243 SER n 1 244 ASN n 1 245 GLY n 1 246 ASN n 1 247 PHE n 1 248 ILE n 1 249 ALA n 1 250 PRO n 1 251 GLU n 1 252 TYR n 1 253 ALA n 1 254 TYR n 1 255 LYS n 1 256 ILE n 1 257 VAL n 1 258 LYS n 1 259 LYS n 1 260 GLY n 1 261 ASP n 1 262 SER n 1 263 THR n 1 264 ILE n 1 265 MET n 1 266 LYS n 1 267 SER n 1 268 GLU n 1 269 LEU n 1 270 GLU n 1 271 TYR n 1 272 GLY n 1 273 ASN n 1 274 CYS n 1 275 ASN n 1 276 THR n 1 277 LYS n 1 278 CYS n 1 279 GLN n 1 280 THR n 1 281 PRO n 1 282 MET n 1 283 GLY n 1 284 ALA n 1 285 ILE n 1 286 ASN n 1 287 SER n 1 288 SER n 1 289 MET n 1 290 PRO n 1 291 PHE n 1 292 HIS n 1 293 ASN n 1 294 ILE n 1 295 HIS n 1 296 PRO n 1 297 LEU n 1 298 THR n 1 299 ILE n 1 300 GLY n 1 301 GLU n 1 302 CYS n 1 303 PRO n 1 304 LYS n 1 305 TYR n 1 306 VAL n 1 307 LYS n 1 308 SER n 1 309 ASN n 1 310 ARG n 1 311 LEU n 1 312 VAL n 1 313 LEU n 1 314 ALA n 1 315 THR n 1 316 GLY n 1 317 LEU n 1 318 ARG n 1 319 ASN n 1 320 SER n 1 321 PRO n 1 322 GLN n 1 323 ARG n 1 324 GLU n 1 325 THR n 1 326 ARG n 2 1 GLY n 2 2 LEU n 2 3 PHE n 2 4 GLY n 2 5 ALA n 2 6 ILE n 2 7 ALA n 2 8 GLY n 2 9 PHE n 2 10 ILE n 2 11 GLU n 2 12 GLY n 2 13 GLY n 2 14 TRP n 2 15 GLN n 2 16 GLY n 2 17 MET n 2 18 VAL n 2 19 ASP n 2 20 GLY n 2 21 TRP n 2 22 TYR n 2 23 GLY n 2 24 TYR n 2 25 HIS n 2 26 HIS n 2 27 SER n 2 28 ASN n 2 29 GLU n 2 30 GLN n 2 31 GLY n 2 32 SER n 2 33 GLY n 2 34 TYR n 2 35 ALA n 2 36 ALA n 2 37 ASP n 2 38 LYS n 2 39 GLU n 2 40 SER n 2 41 THR n 2 42 GLN n 2 43 LYS n 2 44 ALA n 2 45 ILE n 2 46 ASP n 2 47 GLY n 2 48 VAL n 2 49 THR n 2 50 ASN n 2 51 LYS n 2 52 VAL n 2 53 ASN n 2 54 SER n 2 55 ILE n 2 56 ILE n 2 57 ASP n 2 58 LYS n 2 59 MET n 2 60 ASN n 2 61 THR n 2 62 GLN n 2 63 PHE n 2 64 GLU n 2 65 ALA n 2 66 VAL n 2 67 GLY n 2 68 ARG n 2 69 GLU n 2 70 PHE n 2 71 ASN n 2 72 ASN n 2 73 LEU n 2 74 GLU n 2 75 ARG n 2 76 ARG n 2 77 ILE n 2 78 GLU n 2 79 ASN n 2 80 LEU n 2 81 ASN n 2 82 LYS n 2 83 LYS n 2 84 MET n 2 85 GLU n 2 86 ASP n 2 87 GLY n 2 88 PHE n 2 89 LEU n 2 90 ASP n 2 91 VAL n 2 92 TRP n 2 93 THR n 2 94 TYR n 2 95 ASN n 2 96 ALA n 2 97 GLU n 2 98 LEU n 2 99 LEU n 2 100 VAL n 2 101 LEU n 2 102 MET n 2 103 GLU n 2 104 ASN n 2 105 GLU n 2 106 ARG n 2 107 THR n 2 108 LEU n 2 109 ASP n 2 110 PHE n 2 111 HIS n 2 112 ASP n 2 113 SER n 2 114 ASN n 2 115 VAL n 2 116 LYS n 2 117 ASN n 2 118 LEU n 2 119 TYR n 2 120 ASP n 2 121 LYS n 2 122 VAL n 2 123 ARG n 2 124 LEU n 2 125 GLN n 2 126 LEU n 2 127 ARG n 2 128 ASP n 2 129 ASN n 2 130 ALA n 2 131 LYS n 2 132 GLU n 2 133 LEU n 2 134 GLY n 2 135 ASN n 2 136 GLY n 2 137 CYS n 2 138 PHE n 2 139 GLU n 2 140 PHE n 2 141 TYR n 2 142 HIS n 2 143 LYS n 2 144 CYS n 2 145 ASP n 2 146 ASN n 2 147 GLU n 2 148 CYS n 2 149 MET n 2 150 GLU n 2 151 SER n 2 152 VAL n 2 153 ARG n 2 154 ASN n 2 155 GLY n 2 156 THR n 2 157 TYR n 2 158 ASP n 2 159 TYR n 2 160 PRO n 2 161 GLN n 2 162 TYR n 2 163 SER n 2 164 GLU n 2 165 GLU n 2 166 ALA n # loop_ _entity_src_nat.entity_id _entity_src_nat.pdbx_src_id _entity_src_nat.pdbx_alt_source_flag _entity_src_nat.pdbx_beg_seq_num _entity_src_nat.pdbx_end_seq_num _entity_src_nat.common_name _entity_src_nat.pdbx_organism_scientific _entity_src_nat.pdbx_ncbi_taxonomy_id _entity_src_nat.genus _entity_src_nat.species _entity_src_nat.strain _entity_src_nat.tissue _entity_src_nat.tissue_fraction _entity_src_nat.pdbx_secretion _entity_src_nat.pdbx_fragment _entity_src_nat.pdbx_variant _entity_src_nat.pdbx_cell_line _entity_src_nat.pdbx_atcc _entity_src_nat.pdbx_cellular_location _entity_src_nat.pdbx_organ _entity_src_nat.pdbx_organelle _entity_src_nat.pdbx_cell _entity_src_nat.pdbx_plasmid_name _entity_src_nat.pdbx_plasmid_details _entity_src_nat.details 1 1 sample ? ? ? 'INFLUENZA A VIRUS (A/VIETNAM/1194/2004(H5N1))' 644788 ? ? 'A/VIETNAM/1194/2004 (H5N1)' ? ? ? ? 'ASN186LYS MUTANT' ? ? ? ? ? ? ? ? ? 2 1 sample ? ? ? 'INFLUENZA A VIRUS (A/VIETNAM/1194/2004(H5N1))' 644788 ? ? 'A/VIETNAM/1194/2004 (H5N1)' ? ? ? ? 'ASN186LYS MUTANT' ? ? ? ? ? ? ? ? ? # loop_ _struct_ref.id _struct_ref.db_name _struct_ref.db_code _struct_ref.entity_id _struct_ref.pdbx_seq_one_letter_code _struct_ref.pdbx_align_begin _struct_ref.pdbx_db_accession _struct_ref.pdbx_db_isoform 1 UNP Q6DQ34_9INFA 1 ? ? Q6DQ34 ? 2 UNP Q6DQ34_9INFA 2 ? ? Q6DQ34 ? # loop_ _struct_ref_seq.align_id _struct_ref_seq.ref_id _struct_ref_seq.pdbx_PDB_id_code _struct_ref_seq.pdbx_strand_id _struct_ref_seq.seq_align_beg _struct_ref_seq.pdbx_seq_align_beg_ins_code _struct_ref_seq.seq_align_end _struct_ref_seq.pdbx_seq_align_end_ins_code _struct_ref_seq.pdbx_db_accession _struct_ref_seq.db_align_beg _struct_ref_seq.pdbx_db_align_beg_ins_code _struct_ref_seq.db_align_end _struct_ref_seq.pdbx_db_align_end_ins_code _struct_ref_seq.pdbx_auth_seq_align_beg _struct_ref_seq.pdbx_auth_seq_align_end 1 1 4CQS A 1 ? 326 ? Q6DQ34 17 ? 342 ? 1 326 2 2 4CQS 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 4CQS LYS A 182 ? UNP Q6DQ34 ASN 198 'engineered mutation' 182 1 1 4CQS THR A 325 ? UNP Q6DQ34 ARG 341 conflict 325 2 # loop_ _chem_comp.id _chem_comp.type _chem_comp.mon_nstd_flag _chem_comp.name _chem_comp.pdbx_synonyms _chem_comp.formula _chem_comp.formula_weight ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 BMA D-saccharide . BETA-D-MANNOSE ? 'C6 H12 O6' 180.156 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MAN D-saccharide . ALPHA-D-MANNOSE ? 'C6 H12 O6' 180.156 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 MPO non-polymer . '3[N-MORPHOLINO]PROPANE SULFONIC ACID' ? 'C7 H15 N O4 S' 209.263 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 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 4CQS _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 3.74 _exptl_crystal.density_percent_sol 67 _exptl_crystal.description NONE # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method ? _exptl_crystal_grow.temp ? _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH ? _exptl_crystal_grow.pdbx_pH_range ? _exptl_crystal_grow.pdbx_details '0.1 M HEPES/MOPS PH 7.0, 0.05 M MGCL2, 28-30% PEG 550 MME, SEEDED WITH CRUSHED WILD-TYPE VN1194 HA CRYSTALS.' # _diffrn.id 1 _diffrn.ambient_temp 100 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector CCD _diffrn_detector.type MARRESEARCH _diffrn_detector.pdbx_collection_date ? _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator ? _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 0.92 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'DIAMOND BEAMLINE I04-1' _diffrn_source.pdbx_synchrotron_site Diamond _diffrn_source.pdbx_synchrotron_beamline I04-1 _diffrn_source.pdbx_wavelength 0.92 _diffrn_source.pdbx_wavelength_list ? # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 4CQS _reflns.observed_criterion_sigma_I 3.2 _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 39.43 _reflns.d_resolution_high 2.55 _reflns.number_obs 29712 _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 16.66 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 9.1 # _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_ordinal 1 _reflns_shell.d_res_high 2.55 _reflns_shell.d_res_low 2.69 _reflns_shell.percent_possible_all 100.0 _reflns_shell.Rmerge_I_obs 0.63 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs 3.20 _reflns_shell.pdbx_redundancy 8.5 # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 4CQS _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 28206 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F . _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 150.56 _refine.ls_d_res_high 2.55 _refine.ls_percent_reflns_obs 99.88 _refine.ls_R_factor_obs 0.19661 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.19474 _refine.ls_R_factor_R_free 0.23227 _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 1506 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.956 _refine.correlation_coeff_Fo_to_Fc_free 0.943 _refine.B_iso_mean 78.980 _refine.aniso_B[1][1] 2.50 _refine.aniso_B[2][2] 2.50 _refine.aniso_B[3][3] -8.10 _refine.aniso_B[1][2] 1.25 _refine.aniso_B[1][3] 0.00 _refine.aniso_B[2][3] 0.00 _refine.solvent_model_details MASK _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.20 _refine.pdbx_solvent_ion_probe_radii 0.80 _refine.pdbx_solvent_shrinkage_radii 0.80 _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details 'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. WITH TLS ADDED' _refine.pdbx_starting_model 'PDB ENTRY 4BGW' _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values 'MAXIMUM LIKELIHOOD' _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_overall_ESU_R 0.308 _refine.pdbx_overall_ESU_R_Free 0.233 _refine.overall_SU_ML 0.202 _refine.pdbx_overall_phase_error ? _refine.overall_SU_B 19.263 _refine.overall_SU_R_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 3860 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 182 _refine_hist.number_atoms_solvent 164 _refine_hist.number_atoms_total 4206 _refine_hist.d_res_high 2.55 _refine_hist.d_res_low 150.56 # 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 ? 4153 'X-RAY DIFFRACTION' ? r_bond_other_d 0.001 0.020 ? 3806 'X-RAY DIFFRACTION' ? r_angle_refined_deg 1.038 1.990 ? 5643 'X-RAY DIFFRACTION' ? r_angle_other_deg 0.662 3.003 ? 8740 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 5.578 5.000 ? 483 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg 37.695 25.150 ? 200 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg 15.691 15.000 ? 681 'X-RAY DIFFRACTION' ? r_dihedral_angle_4_deg 13.043 15.000 ? 17 'X-RAY DIFFRACTION' ? r_chiral_restr 0.056 0.200 ? 629 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.003 0.020 ? 4611 'X-RAY DIFFRACTION' ? r_gen_planes_other 0.001 0.020 ? 944 'X-RAY DIFFRACTION' ? r_nbd_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbd_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbtor_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbtor_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_metal_ion_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_metal_ion_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_vdw_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_vdw_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_hbond_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_hbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_metal_ion_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_metal_ion_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcbond_it 1.357 4.311 ? 1932 'X-RAY DIFFRACTION' ? r_mcbond_other 1.353 4.311 ? 1931 'X-RAY DIFFRACTION' ? r_mcangle_it 2.310 6.465 ? 2412 'X-RAY DIFFRACTION' ? r_mcangle_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scbond_it 2.457 5.206 ? 2221 '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 2.550 _refine_ls_shell.d_res_low 2.616 _refine_ls_shell.number_reflns_R_work 2077 _refine_ls_shell.R_factor_R_work 0.316 _refine_ls_shell.percent_reflns_obs 99.95 _refine_ls_shell.R_factor_R_free 0.350 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 98 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? # _struct.entry_id 4CQS _struct.title ;H5 (VN1194) Asn186Lys Mutant Haemagglutinin in Complex with Avian Receptor Analogue 3'SLN ; _struct.pdbx_descriptor 'HAEMAGGLUTININ HA1, HAEMAGGLUTININ HA2' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 4CQS _struct_keywords.pdbx_keywords 'VIRAL PROTEIN' _struct_keywords.text ;VIRAL PROTEIN, SIALIC ACID, GLYCOPROTEIN, VIRUS RECEPTOR, AVIAN FLU, SIALYLLACTOSAMINE, 3SLN, 3'SLN, 6SLN, 6'SLN, LSTA ; # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 3 ? D N N 3 ? E N N 3 ? F N N 3 ? G N N 3 ? H N N 4 ? I N N 5 ? J N N 4 ? K N N 3 ? L N N 6 ? M N N 3 ? N N N 3 ? O N N 5 ? P N N 6 ? Q N N 7 ? R 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 CYS A 67 ? ILE A 71 ? CYS A 67 ILE A 71 5 ? 5 HELX_P HELX_P3 3 ASP A 97 ? SER A 106 ? ASP A 97 SER A 106 1 ? 10 HELX_P HELX_P4 4 PRO A 118 ? TRP A 122 ? PRO A 118 TRP A 122 5 ? 5 HELX_P HELX_P5 5 ASP A 183 ? GLN A 192 ? ASP A 183 GLN A 192 1 ? 10 HELX_P HELX_P6 6 ASP B 37 ? MET B 59 ? ASP B 37 MET B 59 1 ? 23 HELX_P HELX_P7 7 GLU B 74 ? ARG B 127 ? GLU B 74 ARG B 127 1 ? 54 HELX_P HELX_P8 8 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 ? ? ? ? ? ? ? 2.085 ? disulf2 disulf ? ? A CYS 42 SG ? ? ? 1_555 A CYS 274 SG ? ? A CYS 42 A CYS 274 1_555 ? ? ? ? ? ? ? 2.036 ? 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 ? ? ? ? ? ? ? 2.060 ? disulf5 disulf ? ? A CYS 278 SG ? ? ? 1_555 A CYS 302 SG ? ? A CYS 278 A CYS 302 1_555 ? ? ? ? ? ? ? 2.049 ? disulf6 disulf ? ? B CYS 144 SG ? ? ? 1_555 B CYS 148 SG ? ? B CYS 144 B CYS 148 1_555 ? ? ? ? ? ? ? 2.045 ? covale1 covale ? ? A ASN 11 ND2 ? ? ? 1_555 C NAG . C1 ? ? A ASN 11 A NAG 1322 1_555 ? ? ? ? ? ? ? 1.455 ? covale2 covale ? ? A ASN 23 ND2 ? ? ? 1_555 D NAG . C1 ? ? A ASN 23 A NAG 1323 1_555 ? ? ? ? ? ? ? 1.449 ? covale3 covale ? ? A ASN 165 ND2 ? ? ? 1_555 F NAG . C1 ? ? A ASN 165 A NAG 1325 1_555 ? ? ? ? ? ? ? 1.441 ? covale4 covale ? ? A ASN 286 ND2 ? ? ? 1_555 K NAG . C1 ? ? A ASN 286 A NAG 1330 1_555 ? ? ? ? ? ? ? 1.456 ? covale5 covale ? ? D NAG . O4 ? ? ? 1_555 E NAG . C1 ? ? A NAG 1323 A NAG 1324 1_555 ? ? ? ? ? ? ? 1.444 ? covale6 covale ? ? F NAG . O4 ? ? ? 1_555 G NAG . C1 ? ? A NAG 1325 A NAG 1326 1_555 ? ? ? ? ? ? ? 1.433 ? covale7 covale ? ? G NAG . O4 ? ? ? 1_555 H MAN . C1 ? ? A NAG 1326 A MAN 1327 1_555 ? ? ? ? ? ? ? 1.446 ? covale8 covale ? ? H MAN . O3 ? ? ? 1_555 I BMA . C1 ? ? A MAN 1327 A BMA 1328 1_555 ? ? ? ? ? ? ? 1.440 ? covale9 covale ? ? H MAN . O6 ? ? ? 1_555 J MAN . C1 ? ? A MAN 1327 A MAN 1329 1_555 ? ? ? ? ? ? ? 1.451 ? covale10 covale ? ? B ASN 154 ND2 ? ? ? 1_555 M NAG . C1 ? ? B ASN 154 B NAG 1163 1_555 ? ? ? ? ? ? ? 1.443 ? covale11 covale ? ? M NAG . O4 ? ? ? 1_555 N NAG . C1 ? ? B NAG 1163 B NAG 1164 1_555 ? ? ? ? ? ? ? 1.447 ? covale12 covale ? ? N NAG . O4 ? ? ? 1_555 O BMA . C1 ? ? B NAG 1164 B BMA 1165 1_555 ? ? ? ? ? ? ? 1.451 ? # 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 ? ? ? ? 5 'BINDING SITE FOR RESIDUE MPO A 1331' AC2 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE MPO B 1166' AC3 Software ? ? ? ? 1 'Binding site for Mono-Saccharide NAG A1322 bound to ASN A 11' AC4 Software ? ? ? ? 2 'Binding site for Poly-Saccharide residues NAG A1323 through NAG A1324 bound to ASN A 23' AC5 Software ? ? ? ? 8 'Binding site for Poly-Saccharide residues NAG A1325 through MAN A1329 bound to ASN A 165' AC6 Software ? ? ? ? 1 'Binding site for Mono-Saccharide NAG A1330 bound to ASN A 286' AC7 Software ? ? ? ? 3 'Binding site for Poly-Saccharide residues NAG B1163 through BMA B1165 bound to ASN B 154' # 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 5 LEU A 129 ? LEU A 129 . ? 1_555 ? 2 AC1 5 VAL A 131 ? VAL A 131 . ? 1_555 ? 3 AC1 5 SER A 132 ? SER A 132 . ? 1_555 ? 4 AC1 5 SER A 133 ? SER A 133 . ? 1_555 ? 5 AC1 5 GLN A 222 ? GLN A 222 . ? 1_555 ? 6 AC2 6 CYS A 4 ? CYS A 4 . ? 1_555 ? 7 AC2 6 TRP B 14 ? TRP B 14 . ? 1_555 ? 8 AC2 6 HIS B 25 ? HIS B 25 . ? 1_555 ? 9 AC2 6 ASN B 135 ? ASN B 135 . ? 1_555 ? 10 AC2 6 CYS B 137 ? CYS B 137 . ? 1_555 ? 11 AC2 6 HOH R . ? HOH B 2058 . ? 1_555 ? 12 AC3 1 ASN A 11 ? ASN A 11 . ? 1_555 ? 13 AC4 2 ASN A 23 ? ASN A 23 . ? 1_555 ? 14 AC4 2 HOH Q . ? HOH A 2021 . ? 1_555 ? 15 AC5 8 ASN A 165 ? ASN A 165 . ? 1_555 ? 16 AC5 8 ASN A 236 ? ASN A 236 . ? 1_555 ? 17 AC5 8 ALA A 238 ? ALA A 238 . ? 1_555 ? 18 AC5 8 HIS A 295 ? HIS A 295 . ? 4_545 ? 19 AC5 8 HOH Q . ? HOH A 2089 . ? 4_545 ? 20 AC5 8 HOH Q . ? HOH A 2104 . ? 1_555 ? 21 AC5 8 ARG B 75 ? ARG B 75 . ? 4_545 ? 22 AC5 8 GLU B 78 ? GLU B 78 . ? 4_545 ? 23 AC6 1 ASN A 286 ? ASN A 286 . ? 1_555 ? 24 AC7 3 GLU B 147 ? GLU B 147 . ? 1_555 ? 25 AC7 3 GLU B 150 ? GLU B 150 . ? 1_555 ? 26 AC7 3 ASN B 154 ? ASN B 154 . ? 1_555 ? # _database_PDB_matrix.entry_id 4CQS _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 4CQS _atom_sites.fract_transf_matrix[1][1] 0.009881 _atom_sites.fract_transf_matrix[1][2] 0.005705 _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] 0.011410 _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] 0.002214 _atom_sites.fract_transf_vector[1] 0.00000 _atom_sites.fract_transf_vector[2] 0.00000 _atom_sites.fract_transf_vector[3] 0.00000 # loop_ _atom_type.symbol C N O S # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 N N . ASP A 1 1 ? 37.083 -15.418 -83.694 1.00 65.04 ? 1 ASP A N 1 ATOM 2 C CA . ASP A 1 1 ? 36.199 -15.917 -82.606 1.00 65.20 ? 1 ASP A CA 1 ATOM 3 C C . ASP A 1 1 ? 37.018 -16.671 -81.578 1.00 62.72 ? 1 ASP A C 1 ATOM 4 O O . ASP A 1 1 ? 37.898 -17.446 -81.946 1.00 60.27 ? 1 ASP A O 1 ATOM 5 C CB . ASP A 1 1 ? 35.130 -16.854 -83.169 1.00 66.14 ? 1 ASP A CB 1 ATOM 6 C CG . ASP A 1 1 ? 34.208 -16.167 -84.138 1.00 68.94 ? 1 ASP A CG 1 ATOM 7 O OD1 . ASP A 1 1 ? 34.396 -14.960 -84.407 1.00 69.96 ? 1 ASP A OD1 1 ATOM 8 O OD2 . ASP A 1 1 ? 33.281 -16.842 -84.629 1.00 73.01 ? 1 ASP A OD2 1 ATOM 9 N N . GLN A 1 2 ? 36.723 -16.453 -80.296 1.00 62.95 ? 2 GLN A N 1 ATOM 10 C CA . GLN A 1 2 ? 37.475 -17.113 -79.236 1.00 60.92 ? 2 GLN A CA 1 ATOM 11 C C . GLN A 1 2 ? 36.694 -17.428 -77.977 1.00 58.12 ? 2 GLN A C 1 ATOM 12 O O . GLN A 1 2 ? 35.648 -16.842 -77.710 1.00 57.99 ? 2 GLN A O 1 ATOM 13 C CB . GLN A 1 2 ? 38.712 -16.292 -78.867 1.00 63.04 ? 2 GLN A CB 1 ATOM 14 C CG . GLN A 1 2 ? 38.450 -14.892 -78.356 1.00 66.83 ? 2 GLN A CG 1 ATOM 15 C CD . GLN A 1 2 ? 39.731 -14.215 -77.901 1.00 68.42 ? 2 GLN A CD 1 ATOM 16 O OE1 . GLN A 1 2 ? 39.826 -13.746 -76.770 1.00 69.05 ? 2 GLN A OE1 1 ATOM 17 N NE2 . GLN A 1 2 ? 40.729 -14.172 -78.781 1.00 69.48 ? 2 GLN A NE2 1 ATOM 18 N N . ILE A 1 3 ? 37.234 -18.375 -77.215 1.00 55.31 ? 3 ILE A N 1 ATOM 19 C CA . ILE A 1 3 ? 36.720 -18.718 -75.898 1.00 54.74 ? 3 ILE A CA 1 ATOM 20 C C . ILE A 1 3 ? 37.874 -18.700 -74.901 1.00 53.02 ? 3 ILE A C 1 ATOM 21 O O . ILE A 1 3 ? 38.950 -19.224 -75.182 1.00 51.15 ? 3 ILE A O 1 ATOM 22 C CB . ILE A 1 3 ? 35.995 -20.081 -75.893 1.00 54.43 ? 3 ILE A CB 1 ATOM 23 C CG1 . ILE A 1 3 ? 35.219 -20.266 -74.587 1.00 54.74 ? 3 ILE A CG1 1 ATOM 24 C CG2 . ILE A 1 3 ? 36.963 -21.235 -76.092 1.00 52.50 ? 3 ILE A CG2 1 ATOM 25 C CD1 . ILE A 1 3 ? 34.191 -21.371 -74.653 1.00 55.67 ? 3 ILE A CD1 1 ATOM 26 N N . CYS A 1 4 ? 37.641 -18.076 -73.750 1.00 53.59 ? 4 CYS A N 1 ATOM 27 C CA . CYS A 1 4 ? 38.671 -17.872 -72.743 1.00 53.04 ? 4 CYS A CA 1 ATOM 28 C C . CYS A 1 4 ? 38.270 -18.541 -71.462 1.00 51.54 ? 4 CYS A C 1 ATOM 29 O O . CYS A 1 4 ? 37.085 -18.642 -71.169 1.00 54.37 ? 4 CYS A O 1 ATOM 30 C CB . CYS A 1 4 ? 38.845 -16.383 -72.456 1.00 55.31 ? 4 CYS A CB 1 ATOM 31 S SG . CYS A 1 4 ? 39.301 -15.408 -73.901 1.00 60.25 ? 4 CYS A SG 1 ATOM 32 N N . ILE A 1 5 ? 39.260 -18.963 -70.685 1.00 48.50 ? 5 ILE A N 1 ATOM 33 C CA . ILE A 1 5 ? 39.031 -19.477 -69.343 1.00 47.23 ? 5 ILE A CA 1 ATOM 34 C C . ILE A 1 5 ? 39.513 -18.453 -68.325 1.00 46.75 ? 5 ILE A C 1 ATOM 35 O O . ILE A 1 5 ? 40.578 -17.867 -68.490 1.00 44.83 ? 5 ILE A O 1 ATOM 36 C CB . ILE A 1 5 ? 39.782 -20.790 -69.122 1.00 46.03 ? 5 ILE A CB 1 ATOM 37 C CG1 . ILE A 1 5 ? 39.341 -21.819 -70.163 1.00 47.86 ? 5 ILE A CG1 1 ATOM 38 C CG2 . ILE A 1 5 ? 39.559 -21.312 -67.707 1.00 45.24 ? 5 ILE A CG2 1 ATOM 39 C CD1 . ILE A 1 5 ? 37.919 -22.300 -69.976 1.00 50.42 ? 5 ILE A CD1 1 ATOM 40 N N . GLY A 1 6 ? 38.724 -18.251 -67.273 1.00 46.80 ? 6 GLY A N 1 ATOM 41 C CA . GLY A 1 6 ? 39.050 -17.264 -66.254 1.00 46.88 ? 6 GLY A CA 1 ATOM 42 C C . GLY A 1 6 ? 38.345 -17.502 -64.935 1.00 47.01 ? 6 GLY A C 1 ATOM 43 O O . GLY A 1 6 ? 37.637 -18.492 -64.762 1.00 49.91 ? 6 GLY A O 1 ATOM 44 N N . TYR A 1 7 ? 38.542 -16.578 -64.008 1.00 46.06 ? 7 TYR A N 1 ATOM 45 C CA . TYR A 1 7 ? 38.071 -16.734 -62.655 1.00 46.80 ? 7 TYR A CA 1 ATOM 46 C C . TYR A 1 7 ? 37.533 -15.421 -62.123 1.00 47.79 ? 7 TYR A C 1 ATOM 47 O O . TYR A 1 7 ? 37.779 -14.364 -62.690 1.00 47.23 ? 7 TYR A O 1 ATOM 48 C CB . TYR A 1 7 ? 39.206 -17.244 -61.757 1.00 46.93 ? 7 TYR A CB 1 ATOM 49 C CG . TYR A 1 7 ? 40.476 -16.415 -61.821 1.00 46.66 ? 7 TYR A CG 1 ATOM 50 C CD1 . TYR A 1 7 ? 41.414 -16.619 -62.817 1.00 45.81 ? 7 TYR A CD1 1 ATOM 51 C CD2 . TYR A 1 7 ? 40.733 -15.430 -60.876 1.00 48.11 ? 7 TYR A CD2 1 ATOM 52 C CE1 . TYR A 1 7 ? 42.567 -15.853 -62.883 1.00 47.04 ? 7 TYR A CE1 1 ATOM 53 C CE2 . TYR A 1 7 ? 41.886 -14.663 -60.930 1.00 47.68 ? 7 TYR A CE2 1 ATOM 54 C CZ . TYR A 1 7 ? 42.801 -14.877 -61.934 1.00 47.50 ? 7 TYR A CZ 1 ATOM 55 O OH . TYR A 1 7 ? 43.950 -14.112 -61.992 1.00 47.92 ? 7 TYR A OH 1 ATOM 56 N N . HIS A 1 8 ? 36.810 -15.525 -61.016 1.00 48.94 ? 8 HIS A N 1 ATOM 57 C CA . HIS A 1 8 ? 36.072 -14.428 -60.401 1.00 51.76 ? 8 HIS A CA 1 ATOM 58 C C . HIS A 1 8 ? 36.994 -13.362 -59.816 1.00 52.96 ? 8 HIS A C 1 ATOM 59 O O . HIS A 1 8 ? 38.091 -13.660 -59.339 1.00 51.83 ? 8 HIS A O 1 ATOM 60 C CB . HIS A 1 8 ? 35.198 -15.027 -59.296 1.00 52.55 ? 8 HIS A CB 1 ATOM 61 C CG . HIS A 1 8 ? 34.346 -14.044 -58.556 1.00 55.82 ? 8 HIS A CG 1 ATOM 62 N ND1 . HIS A 1 8 ? 33.227 -13.460 -59.110 1.00 58.86 ? 8 HIS A ND1 1 ATOM 63 C CD2 . HIS A 1 8 ? 34.402 -13.604 -57.274 1.00 56.23 ? 8 HIS A CD2 1 ATOM 64 C CE1 . HIS A 1 8 ? 32.650 -12.677 -58.212 1.00 60.01 ? 8 HIS A CE1 1 ATOM 65 N NE2 . HIS A 1 8 ? 33.342 -12.748 -57.089 1.00 57.56 ? 8 HIS A NE2 1 ATOM 66 N N . ALA A 1 9 ? 36.537 -12.115 -59.868 1.00 55.26 ? 9 ALA A N 1 ATOM 67 C CA . ALA A 1 9 ? 37.152 -11.018 -59.120 1.00 55.20 ? 9 ALA A CA 1 ATOM 68 C C . ALA A 1 9 ? 36.051 -10.106 -58.592 1.00 57.87 ? 9 ALA A C 1 ATOM 69 O O . ALA A 1 9 ? 34.925 -10.144 -59.080 1.00 60.47 ? 9 ALA A O 1 ATOM 70 C CB . ALA A 1 9 ? 38.108 -10.244 -59.998 1.00 54.53 ? 9 ALA A CB 1 ATOM 71 N N . ASN A 1 10 ? 36.365 -9.299 -57.587 1.00 58.21 ? 10 ASN A N 1 ATOM 72 C CA . ASN A 1 10 ? 35.390 -8.367 -57.040 1.00 61.28 ? 10 ASN A CA 1 ATOM 73 C C . ASN A 1 10 ? 36.062 -7.187 -56.339 1.00 64.59 ? 10 ASN A C 1 ATOM 74 O O . ASN A 1 10 ? 37.269 -7.014 -56.458 1.00 62.62 ? 10 ASN A O 1 ATOM 75 C CB . ASN A 1 10 ? 34.410 -9.108 -56.120 1.00 60.48 ? 10 ASN A CB 1 ATOM 76 C CG . ASN A 1 10 ? 35.071 -9.688 -54.889 1.00 58.36 ? 10 ASN A CG 1 ATOM 77 O OD1 . ASN A 1 10 ? 36.226 -9.390 -54.579 1.00 56.53 ? 10 ASN A OD1 1 ATOM 78 N ND2 . ASN A 1 10 ? 34.330 -10.527 -54.171 1.00 57.55 ? 10 ASN A ND2 1 ATOM 79 N N . ASN A 1 11 ? 35.279 -6.376 -55.629 1.00 71.76 ? 11 ASN A N 1 ATOM 80 C CA . ASN A 1 11 ? 35.795 -5.182 -54.948 1.00 77.30 ? 11 ASN A CA 1 ATOM 81 C C . ASN A 1 11 ? 36.278 -5.442 -53.506 1.00 72.93 ? 11 ASN A C 1 ATOM 82 O O . ASN A 1 11 ? 36.513 -4.500 -52.748 1.00 73.06 ? 11 ASN A O 1 ATOM 83 C CB . ASN A 1 11 ? 34.747 -4.046 -54.987 1.00 87.38 ? 11 ASN A CB 1 ATOM 84 C CG . ASN A 1 11 ? 33.441 -4.401 -54.274 1.00 98.45 ? 11 ASN A CG 1 ATOM 85 O OD1 . ASN A 1 11 ? 33.368 -5.387 -53.537 1.00 96.77 ? 11 ASN A OD1 1 ATOM 86 N ND2 . ASN A 1 11 ? 32.397 -3.585 -54.499 1.00 116.58 ? 11 ASN A ND2 1 ATOM 87 N N . SER A 1 12 ? 36.434 -6.716 -53.145 1.00 68.10 ? 12 SER A N 1 ATOM 88 C CA . SER A 1 12 ? 36.844 -7.109 -51.800 1.00 64.52 ? 12 SER A CA 1 ATOM 89 C C . SER A 1 12 ? 38.250 -6.615 -51.484 1.00 63.76 ? 12 SER A C 1 ATOM 90 O O . SER A 1 12 ? 39.145 -6.669 -52.334 1.00 61.03 ? 12 SER A O 1 ATOM 91 C CB . SER A 1 12 ? 36.793 -8.640 -51.642 1.00 62.39 ? 12 SER A CB 1 ATOM 92 O OG . SER A 1 12 ? 37.069 -9.057 -50.312 1.00 58.50 ? 12 SER A OG 1 ATOM 93 N N . THR A 1 13 ? 38.413 -6.118 -50.257 1.00 64.80 ? 13 THR A N 1 ATOM 94 C CA . THR A 1 13 ? 39.705 -5.716 -49.712 1.00 63.56 ? 13 THR A CA 1 ATOM 95 C C . THR A 1 13 ? 40.124 -6.627 -48.563 1.00 61.94 ? 13 THR A C 1 ATOM 96 O O . THR A 1 13 ? 41.156 -6.389 -47.943 1.00 60.12 ? 13 THR A O 1 ATOM 97 C CB . THR A 1 13 ? 39.649 -4.275 -49.179 1.00 66.10 ? 13 THR A CB 1 ATOM 98 O OG1 . THR A 1 13 ? 38.637 -4.177 -48.164 1.00 67.41 ? 13 THR A OG1 1 ATOM 99 C CG2 . THR A 1 13 ? 39.338 -3.300 -50.306 1.00 67.08 ? 13 THR A CG2 1 ATOM 100 N N . GLU A 1 14 ? 39.330 -7.662 -48.282 1.00 61.85 ? 14 GLU A N 1 ATOM 101 C CA . GLU A 1 14 ? 39.660 -8.634 -47.236 1.00 61.57 ? 14 GLU A CA 1 ATOM 102 C C . GLU A 1 14 ? 41.018 -9.261 -47.510 1.00 57.89 ? 14 GLU A C 1 ATOM 103 O O . GLU A 1 14 ? 41.313 -9.641 -48.642 1.00 56.56 ? 14 GLU A O 1 ATOM 104 C CB . GLU A 1 14 ? 38.621 -9.753 -47.166 1.00 64.78 ? 14 GLU A CB 1 ATOM 105 C CG . GLU A 1 14 ? 37.205 -9.315 -46.831 1.00 69.97 ? 14 GLU A CG 1 ATOM 106 C CD . GLU A 1 14 ? 37.043 -8.912 -45.381 1.00 74.19 ? 14 GLU A CD 1 ATOM 107 O OE1 . GLU A 1 14 ? 37.328 -9.757 -44.502 1.00 75.43 ? 14 GLU A OE1 1 ATOM 108 O OE2 . GLU A 1 14 ? 36.630 -7.753 -45.128 1.00 78.60 ? 14 GLU A OE2 1 ATOM 109 N N . GLN A 1 15 ? 41.832 -9.374 -46.465 1.00 56.51 ? 15 GLN A N 1 ATOM 110 C CA . GLN A 1 15 ? 43.178 -9.921 -46.570 1.00 54.15 ? 15 GLN A CA 1 ATOM 111 C C . GLN A 1 15 ? 43.318 -11.166 -45.710 1.00 50.39 ? 15 GLN A C 1 ATOM 112 O O . GLN A 1 15 ? 42.659 -11.283 -44.694 1.00 49.58 ? 15 GLN A O 1 ATOM 113 C CB . GLN A 1 15 ? 44.191 -8.882 -46.111 1.00 56.29 ? 15 GLN A CB 1 ATOM 114 C CG . GLN A 1 15 ? 44.212 -7.627 -46.962 1.00 59.01 ? 15 GLN A CG 1 ATOM 115 C CD . GLN A 1 15 ? 45.297 -6.651 -46.553 1.00 61.31 ? 15 GLN A CD 1 ATOM 116 O OE1 . GLN A 1 15 ? 45.817 -5.909 -47.383 1.00 65.88 ? 15 GLN A OE1 1 ATOM 117 N NE2 . GLN A 1 15 ? 45.639 -6.640 -45.273 1.00 62.02 ? 15 GLN A NE2 1 ATOM 118 N N . VAL A 1 16 ? 44.167 -12.097 -46.131 1.00 48.47 ? 16 VAL A N 1 ATOM 119 C CA . VAL A 1 16 ? 44.494 -13.282 -45.338 1.00 45.51 ? 16 VAL A CA 1 ATOM 120 C C . VAL A 1 16 ? 45.986 -13.467 -45.372 1.00 45.30 ? 16 VAL A C 1 ATOM 121 O O . VAL A 1 16 ? 46.642 -13.007 -46.313 1.00 44.52 ? 16 VAL A O 1 ATOM 122 C CB . VAL A 1 16 ? 43.833 -14.569 -45.877 1.00 44.70 ? 16 VAL A CB 1 ATOM 123 C CG1 . VAL A 1 16 ? 42.329 -14.414 -45.908 1.00 46.35 ? 16 VAL A CG1 1 ATOM 124 C CG2 . VAL A 1 16 ? 44.350 -14.935 -47.262 1.00 45.22 ? 16 VAL A CG2 1 ATOM 125 N N . ASP A 1 17 ? 46.516 -14.143 -44.357 1.00 45.50 ? 17 ASP A N 1 ATOM 126 C CA . ASP A 1 17 ? 47.938 -14.456 -44.308 1.00 46.72 ? 17 ASP A CA 1 ATOM 127 C C . ASP A 1 17 ? 48.178 -15.909 -44.694 1.00 45.96 ? 17 ASP A C 1 ATOM 128 O O . ASP A 1 17 ? 47.325 -16.774 -44.462 1.00 44.27 ? 17 ASP A O 1 ATOM 129 C CB . ASP A 1 17 ? 48.499 -14.208 -42.907 1.00 49.64 ? 17 ASP A CB 1 ATOM 130 C CG . ASP A 1 17 ? 48.584 -12.720 -42.545 1.00 52.90 ? 17 ASP A CG 1 ATOM 131 O OD1 . ASP A 1 17 ? 48.897 -11.881 -43.425 1.00 53.13 ? 17 ASP A OD1 1 ATOM 132 O OD2 . ASP A 1 17 ? 48.361 -12.400 -41.352 1.00 55.38 ? 17 ASP A OD2 1 ATOM 133 N N . THR A 1 18 ? 49.346 -16.156 -45.288 1.00 46.13 ? 18 THR A N 1 ATOM 134 C CA . THR A 1 18 ? 49.856 -17.504 -45.547 1.00 45.89 ? 18 THR A CA 1 ATOM 135 C C . THR A 1 18 ? 51.308 -17.596 -45.058 1.00 48.63 ? 18 THR A C 1 ATOM 136 O O . THR A 1 18 ? 51.890 -16.606 -44.625 1.00 49.69 ? 18 THR A O 1 ATOM 137 C CB . THR A 1 18 ? 49.811 -17.859 -47.054 1.00 44.72 ? 18 THR A CB 1 ATOM 138 O OG1 . THR A 1 18 ? 50.680 -16.993 -47.787 1.00 45.13 ? 18 THR A OG1 1 ATOM 139 C CG2 . THR A 1 18 ? 48.428 -17.718 -47.599 1.00 44.05 ? 18 THR A CG2 1 ATOM 140 N N . ILE A 1 19 ? 51.897 -18.781 -45.147 1.00 52.31 ? 19 ILE A N 1 ATOM 141 C CA . ILE A 1 19 ? 53.280 -18.998 -44.711 1.00 53.48 ? 19 ILE A CA 1 ATOM 142 C C . ILE A 1 19 ? 54.277 -18.147 -45.508 1.00 54.19 ? 19 ILE A C 1 ATOM 143 O O . ILE A 1 19 ? 55.184 -17.540 -44.938 1.00 53.50 ? 19 ILE A O 1 ATOM 144 C CB . ILE A 1 19 ? 53.663 -20.482 -44.875 1.00 56.01 ? 19 ILE A CB 1 ATOM 145 C CG1 . ILE A 1 19 ? 52.785 -21.377 -43.995 1.00 58.15 ? 19 ILE A CG1 1 ATOM 146 C CG2 . ILE A 1 19 ? 55.128 -20.712 -44.543 1.00 58.39 ? 19 ILE A CG2 1 ATOM 147 C CD1 . ILE A 1 19 ? 53.117 -21.330 -42.518 1.00 58.19 ? 19 ILE A CD1 1 ATOM 148 N N . MET A 1 20 ? 54.108 -18.119 -46.829 1.00 55.12 ? 20 MET A N 1 ATOM 149 C CA . MET A 1 20 ? 55.052 -17.436 -47.720 1.00 56.98 ? 20 MET A CA 1 ATOM 150 C C . MET A 1 20 ? 54.696 -15.982 -47.992 1.00 57.52 ? 20 MET A C 1 ATOM 151 O O . MET A 1 20 ? 55.513 -15.241 -48.546 1.00 58.07 ? 20 MET A O 1 ATOM 152 C CB . MET A 1 20 ? 55.138 -18.155 -49.067 1.00 57.77 ? 20 MET A CB 1 ATOM 153 C CG . MET A 1 20 ? 55.908 -19.459 -49.030 1.00 60.39 ? 20 MET A CG 1 ATOM 154 S SD . MET A 1 20 ? 56.246 -20.102 -50.681 1.00 63.42 ? 20 MET A SD 1 ATOM 155 C CE . MET A 1 20 ? 56.404 -21.852 -50.284 1.00 67.93 ? 20 MET A CE 1 ATOM 156 N N . GLU A 1 21 ? 53.480 -15.574 -47.642 1.00 55.20 ? 21 GLU A N 1 ATOM 157 C CA . GLU A 1 21 ? 53.023 -14.245 -47.993 1.00 55.29 ? 21 GLU A CA 1 ATOM 158 C C . GLU A 1 21 ? 51.976 -13.758 -47.020 1.00 55.03 ? 21 GLU A C 1 ATOM 159 O O . GLU A 1 21 ? 51.110 -14.513 -46.592 1.00 54.88 ? 21 GLU A O 1 ATOM 160 C CB . GLU A 1 21 ? 52.455 -14.242 -49.409 1.00 56.61 ? 21 GLU A CB 1 ATOM 161 C CG . GLU A 1 21 ? 52.366 -12.856 -50.035 1.00 59.32 ? 21 GLU A CG 1 ATOM 162 C CD . GLU A 1 21 ? 51.875 -12.881 -51.480 1.00 62.09 ? 21 GLU A CD 1 ATOM 163 O OE1 . GLU A 1 21 ? 51.787 -13.990 -52.079 1.00 57.77 ? 21 GLU A OE1 1 ATOM 164 O OE2 . GLU A 1 21 ? 51.581 -11.779 -52.015 1.00 62.81 ? 21 GLU A OE2 1 ATOM 165 N N . LYS A 1 22 ? 52.059 -12.478 -46.690 1.00 56.50 ? 22 LYS A N 1 ATOM 166 C CA . LYS A 1 22 ? 51.137 -11.864 -45.763 1.00 58.06 ? 22 LYS A CA 1 ATOM 167 C C . LYS A 1 22 ? 50.270 -10.854 -46.487 1.00 55.61 ? 22 LYS A C 1 ATOM 168 O O . LYS A 1 22 ? 50.652 -10.332 -47.531 1.00 55.28 ? 22 LYS A O 1 ATOM 169 C CB . LYS A 1 22 ? 51.921 -11.210 -44.636 1.00 62.82 ? 22 LYS A CB 1 ATOM 170 C CG . LYS A 1 22 ? 52.627 -12.216 -43.743 1.00 66.83 ? 22 LYS A CG 1 ATOM 171 C CD . LYS A 1 22 ? 53.434 -11.511 -42.666 1.00 74.39 ? 22 LYS A CD 1 ATOM 172 C CE . LYS A 1 22 ? 53.284 -12.192 -41.310 1.00 78.49 ? 22 LYS A CE 1 ATOM 173 N NZ . LYS A 1 22 ? 53.692 -11.322 -40.167 1.00 79.86 ? 22 LYS A NZ 1 ATOM 174 N N . ASN A 1 23 ? 49.088 -10.608 -45.944 1.00 55.32 ? 23 ASN A N 1 ATOM 175 C CA . ASN A 1 23 ? 48.191 -9.587 -46.474 1.00 58.38 ? 23 ASN A CA 1 ATOM 176 C C . ASN A 1 23 ? 47.838 -9.805 -47.941 1.00 55.55 ? 23 ASN A C 1 ATOM 177 O O . ASN A 1 23 ? 47.928 -8.891 -48.755 1.00 55.22 ? 23 ASN A O 1 ATOM 178 C CB . ASN A 1 23 ? 48.791 -8.194 -46.257 1.00 62.53 ? 23 ASN A CB 1 ATOM 179 C CG . ASN A 1 23 ? 48.875 -7.816 -44.791 1.00 69.94 ? 23 ASN A CG 1 ATOM 180 O OD1 . ASN A 1 23 ? 48.275 -8.464 -43.924 1.00 67.40 ? 23 ASN A OD1 1 ATOM 181 N ND2 . ASN A 1 23 ? 49.620 -6.746 -44.503 1.00 80.76 ? 23 ASN A ND2 1 ATOM 182 N N . VAL A 1 24 ? 47.428 -11.031 -48.258 1.00 52.52 ? 24 VAL A N 1 ATOM 183 C CA . VAL A 1 24 ? 46.969 -11.381 -49.597 1.00 49.83 ? 24 VAL A CA 1 ATOM 184 C C . VAL A 1 24 ? 45.495 -11.015 -49.725 1.00 49.95 ? 24 VAL A C 1 ATOM 185 O O . VAL A 1 24 ? 44.675 -11.444 -48.921 1.00 50.12 ? 24 VAL A O 1 ATOM 186 C CB . VAL A 1 24 ? 47.130 -12.884 -49.859 1.00 48.13 ? 24 VAL A CB 1 ATOM 187 C CG1 . VAL A 1 24 ? 46.729 -13.216 -51.285 1.00 48.98 ? 24 VAL A CG1 1 ATOM 188 C CG2 . VAL A 1 24 ? 48.565 -13.315 -49.598 1.00 47.74 ? 24 VAL A CG2 1 ATOM 189 N N . THR A 1 25 ? 45.155 -10.206 -50.720 1.00 49.51 ? 25 THR A N 1 ATOM 190 C CA . THR A 1 25 ? 43.776 -9.777 -50.891 1.00 49.75 ? 25 THR A CA 1 ATOM 191 C C . THR A 1 25 ? 43.003 -10.896 -51.557 1.00 48.74 ? 25 THR A C 1 ATOM 192 O O . THR A 1 25 ? 43.449 -11.434 -52.571 1.00 49.64 ? 25 THR A O 1 ATOM 193 C CB . THR A 1 25 ? 43.687 -8.516 -51.757 1.00 51.84 ? 25 THR A CB 1 ATOM 194 O OG1 . THR A 1 25 ? 44.553 -7.517 -51.215 1.00 53.76 ? 25 THR A OG1 1 ATOM 195 C CG2 . THR A 1 25 ? 42.272 -7.980 -51.785 1.00 53.63 ? 25 THR A CG2 1 ATOM 196 N N . VAL A 1 26 ? 41.855 -11.246 -50.988 1.00 47.61 ? 26 VAL A N 1 ATOM 197 C CA . VAL A 1 26 ? 41.033 -12.331 -51.516 1.00 46.75 ? 26 VAL A CA 1 ATOM 198 C C . VAL A 1 26 ? 39.593 -11.898 -51.740 1.00 48.47 ? 26 VAL A C 1 ATOM 199 O O . VAL A 1 26 ? 39.108 -10.964 -51.107 1.00 50.99 ? 26 VAL A O 1 ATOM 200 C CB . VAL A 1 26 ? 41.038 -13.562 -50.587 1.00 45.13 ? 26 VAL A CB 1 ATOM 201 C CG1 . VAL A 1 26 ? 42.442 -14.129 -50.474 1.00 43.92 ? 26 VAL A CG1 1 ATOM 202 C CG2 . VAL A 1 26 ? 40.470 -13.233 -49.211 1.00 45.27 ? 26 VAL A CG2 1 ATOM 203 N N . THR A 1 27 ? 38.910 -12.607 -52.631 1.00 48.93 ? 27 THR A N 1 ATOM 204 C CA . THR A 1 27 ? 37.522 -12.297 -52.968 1.00 50.57 ? 27 THR A CA 1 ATOM 205 C C . THR A 1 27 ? 36.566 -12.565 -51.819 1.00 51.13 ? 27 THR A C 1 ATOM 206 O O . THR A 1 27 ? 35.599 -11.839 -51.643 1.00 53.74 ? 27 THR A O 1 ATOM 207 C CB . THR A 1 27 ? 37.046 -13.107 -54.179 1.00 50.96 ? 27 THR A CB 1 ATOM 208 O OG1 . THR A 1 27 ? 37.124 -14.509 -53.884 1.00 50.23 ? 27 THR A OG1 1 ATOM 209 C CG2 . THR A 1 27 ? 37.907 -12.795 -55.381 1.00 51.35 ? 27 THR A CG2 1 ATOM 210 N N . HIS A 1 28 ? 36.823 -13.624 -51.057 1.00 50.94 ? 28 HIS A N 1 ATOM 211 C CA . HIS A 1 28 ? 35.998 -13.962 -49.895 1.00 51.25 ? 28 HIS A CA 1 ATOM 212 C C . HIS A 1 28 ? 36.831 -14.527 -48.758 1.00 51.65 ? 28 HIS A C 1 ATOM 213 O O . HIS A 1 28 ? 37.804 -15.253 -48.984 1.00 50.18 ? 28 HIS A O 1 ATOM 214 C CB . HIS A 1 28 ? 34.926 -14.972 -50.276 1.00 50.46 ? 28 HIS A CB 1 ATOM 215 C CG . HIS A 1 28 ? 34.117 -14.557 -51.458 1.00 51.72 ? 28 HIS A CG 1 ATOM 216 N ND1 . HIS A 1 28 ? 34.584 -14.667 -52.749 1.00 50.75 ? 28 HIS A ND1 1 ATOM 217 C CD2 . HIS A 1 28 ? 32.882 -14.011 -51.547 1.00 53.27 ? 28 HIS A CD2 1 ATOM 218 C CE1 . HIS A 1 28 ? 33.666 -14.218 -53.584 1.00 52.46 ? 28 HIS A CE1 1 ATOM 219 N NE2 . HIS A 1 28 ? 32.625 -13.812 -52.880 1.00 53.96 ? 28 HIS A NE2 1 ATOM 220 N N . ALA A 1 29 ? 36.427 -14.189 -47.536 1.00 53.70 ? 29 ALA A N 1 ATOM 221 C CA . ALA A 1 29 ? 37.089 -14.664 -46.329 1.00 54.06 ? 29 ALA A CA 1 ATOM 222 C C . ALA A 1 29 ? 36.061 -14.946 -45.245 1.00 55.25 ? 29 ALA A C 1 ATOM 223 O O . ALA A 1 29 ? 34.879 -14.625 -45.392 1.00 56.62 ? 29 ALA A O 1 ATOM 224 C CB . ALA A 1 29 ? 38.097 -13.644 -45.841 1.00 53.83 ? 29 ALA A CB 1 ATOM 225 N N . GLN A 1 30 ? 36.522 -15.565 -44.166 1.00 54.27 ? 30 GLN A N 1 ATOM 226 C CA . GLN A 1 30 ? 35.663 -15.898 -43.041 1.00 55.37 ? 30 GLN A CA 1 ATOM 227 C C . GLN A 1 30 ? 36.429 -15.710 -41.734 1.00 53.48 ? 30 GLN A C 1 ATOM 228 O O . GLN A 1 30 ? 37.344 -16.470 -41.417 1.00 50.64 ? 30 GLN A O 1 ATOM 229 C CB . GLN A 1 30 ? 35.142 -17.337 -43.157 1.00 55.94 ? 30 GLN A CB 1 ATOM 230 C CG . GLN A 1 30 ? 34.293 -17.769 -41.963 1.00 58.48 ? 30 GLN A CG 1 ATOM 231 C CD . GLN A 1 30 ? 33.407 -18.968 -42.239 1.00 60.02 ? 30 GLN A CD 1 ATOM 232 O OE1 . GLN A 1 30 ? 33.205 -19.366 -43.382 1.00 63.40 ? 30 GLN A OE1 1 ATOM 233 N NE2 . GLN A 1 30 ? 32.860 -19.542 -41.184 1.00 61.75 ? 30 GLN A NE2 1 ATOM 234 N N . ASP A 1 31 ? 36.052 -14.679 -40.991 1.00 54.69 ? 31 ASP A N 1 ATOM 235 C CA . ASP A 1 31 ? 36.594 -14.447 -39.660 1.00 55.33 ? 31 ASP A CA 1 ATOM 236 C C . ASP A 1 31 ? 36.073 -15.540 -38.713 1.00 54.67 ? 31 ASP A C 1 ATOM 237 O O . ASP A 1 31 ? 34.904 -15.909 -38.765 1.00 55.01 ? 31 ASP A O 1 ATOM 238 C CB . ASP A 1 31 ? 36.184 -13.060 -39.179 1.00 56.13 ? 31 ASP A CB 1 ATOM 239 C CG . ASP A 1 31 ? 36.894 -12.639 -37.917 1.00 57.43 ? 31 ASP A CG 1 ATOM 240 O OD1 . ASP A 1 31 ? 37.689 -13.430 -37.370 1.00 56.41 ? 31 ASP A OD1 1 ATOM 241 O OD2 . ASP A 1 31 ? 36.649 -11.499 -37.468 1.00 60.99 ? 31 ASP A OD2 1 ATOM 242 N N . ILE A 1 32 ? 36.952 -16.068 -37.869 1.00 53.93 ? 32 ILE A N 1 ATOM 243 C CA . ILE A 1 32 ? 36.581 -17.137 -36.938 1.00 54.09 ? 32 ILE A CA 1 ATOM 244 C C . ILE A 1 32 ? 36.930 -16.816 -35.477 1.00 54.03 ? 32 ILE A C 1 ATOM 245 O O . ILE A 1 32 ? 36.859 -17.696 -34.616 1.00 52.78 ? 32 ILE A O 1 ATOM 246 C CB . ILE A 1 32 ? 37.242 -18.473 -37.347 1.00 52.44 ? 32 ILE A CB 1 ATOM 247 C CG1 . ILE A 1 32 ? 38.763 -18.344 -37.387 1.00 51.28 ? 32 ILE A CG1 1 ATOM 248 C CG2 . ILE A 1 32 ? 36.739 -18.913 -38.707 1.00 53.03 ? 32 ILE A CG2 1 ATOM 249 C CD1 . ILE A 1 32 ? 39.474 -19.672 -37.514 1.00 51.36 ? 32 ILE A CD1 1 ATOM 250 N N . LEU A 1 33 ? 37.290 -15.561 -35.207 1.00 54.16 ? 33 LEU A N 1 ATOM 251 C CA . LEU A 1 33 ? 37.708 -15.129 -33.874 1.00 55.45 ? 33 LEU A CA 1 ATOM 252 C C . LEU A 1 33 ? 36.817 -14.002 -33.370 1.00 57.80 ? 33 LEU A C 1 ATOM 253 O O . LEU A 1 33 ? 36.791 -12.913 -33.955 1.00 59.48 ? 33 LEU A O 1 ATOM 254 C CB . LEU A 1 33 ? 39.156 -14.643 -33.908 1.00 54.57 ? 33 LEU A CB 1 ATOM 255 C CG . LEU A 1 33 ? 39.757 -14.136 -32.595 1.00 53.84 ? 33 LEU A CG 1 ATOM 256 C CD1 . LEU A 1 33 ? 39.928 -15.278 -31.612 1.00 53.43 ? 33 LEU A CD1 1 ATOM 257 C CD2 . LEU A 1 33 ? 41.091 -13.453 -32.848 1.00 53.91 ? 33 LEU A CD2 1 ATOM 258 N N . GLU A 1 34 ? 36.096 -14.262 -32.283 1.00 59.08 ? 34 GLU A N 1 ATOM 259 C CA . GLU A 1 34 ? 35.261 -13.241 -31.659 1.00 60.06 ? 34 GLU A CA 1 ATOM 260 C C . GLU A 1 34 ? 36.131 -12.320 -30.821 1.00 58.07 ? 34 GLU A C 1 ATOM 261 O O . GLU A 1 34 ? 36.822 -12.778 -29.916 1.00 54.87 ? 34 GLU A O 1 ATOM 262 C CB . GLU A 1 34 ? 34.188 -13.879 -30.776 1.00 62.35 ? 34 GLU A CB 1 ATOM 263 C CG . GLU A 1 34 ? 33.223 -12.877 -30.166 1.00 64.44 ? 34 GLU A CG 1 ATOM 264 C CD . GLU A 1 34 ? 32.590 -11.982 -31.211 1.00 67.34 ? 34 GLU A CD 1 ATOM 265 O OE1 . GLU A 1 34 ? 31.862 -12.505 -32.086 1.00 69.97 ? 34 GLU A OE1 1 ATOM 266 O OE2 . GLU A 1 34 ? 32.842 -10.762 -31.171 1.00 68.38 ? 34 GLU A OE2 1 ATOM 267 N N . LYS A 1 35 ? 36.090 -11.025 -31.130 1.00 59.08 ? 35 LYS A N 1 ATOM 268 C CA . LYS A 1 35 ? 36.914 -10.028 -30.445 1.00 58.80 ? 35 LYS A CA 1 ATOM 269 C C . LYS A 1 35 ? 36.115 -9.113 -29.518 1.00 58.61 ? 35 LYS A C 1 ATOM 270 O O . LYS A 1 35 ? 36.711 -8.413 -28.698 1.00 57.80 ? 35 LYS A O 1 ATOM 271 C CB . LYS A 1 35 ? 37.659 -9.166 -31.462 1.00 59.46 ? 35 LYS A CB 1 ATOM 272 C CG . LYS A 1 35 ? 38.718 -9.895 -32.263 1.00 59.70 ? 35 LYS A CG 1 ATOM 273 C CD . LYS A 1 35 ? 39.268 -8.996 -33.369 1.00 62.08 ? 35 LYS A CD 1 ATOM 274 C CE . LYS A 1 35 ? 39.232 -9.669 -34.737 1.00 62.79 ? 35 LYS A CE 1 ATOM 275 N NZ . LYS A 1 35 ? 37.867 -10.153 -35.117 1.00 62.52 ? 35 LYS A NZ 1 ATOM 276 N N . THR A 1 36 ? 34.788 -9.115 -29.641 1.00 58.78 ? 36 THR A N 1 ATOM 277 C CA . THR A 1 36 ? 33.944 -8.217 -28.854 1.00 62.32 ? 36 THR A CA 1 ATOM 278 C C . THR A 1 36 ? 33.149 -8.924 -27.754 1.00 63.44 ? 36 THR A C 1 ATOM 279 O O . THR A 1 36 ? 32.828 -10.109 -27.865 1.00 61.48 ? 36 THR A O 1 ATOM 280 C CB . THR A 1 36 ? 32.937 -7.470 -29.740 1.00 64.25 ? 36 THR A CB 1 ATOM 281 O OG1 . THR A 1 36 ? 31.972 -8.395 -30.241 1.00 66.56 ? 36 THR A OG1 1 ATOM 282 C CG2 . THR A 1 36 ? 33.636 -6.793 -30.903 1.00 64.92 ? 36 THR A CG2 1 ATOM 283 N N . HIS A 1 37 ? 32.836 -8.157 -26.706 1.00 64.76 ? 37 HIS A N 1 ATOM 284 C CA . HIS A 1 37 ? 31.991 -8.587 -25.590 1.00 65.49 ? 37 HIS A CA 1 ATOM 285 C C . HIS A 1 37 ? 31.113 -7.404 -25.154 1.00 67.82 ? 37 HIS A C 1 ATOM 286 O O . HIS A 1 37 ? 31.325 -6.282 -25.605 1.00 69.14 ? 37 HIS A O 1 ATOM 287 C CB . HIS A 1 37 ? 32.858 -9.080 -24.421 1.00 64.70 ? 37 HIS A CB 1 ATOM 288 C CG . HIS A 1 37 ? 33.809 -8.052 -23.888 1.00 64.63 ? 37 HIS A CG 1 ATOM 289 N ND1 . HIS A 1 37 ? 33.481 -7.200 -22.857 1.00 66.43 ? 37 HIS A ND1 1 ATOM 290 C CD2 . HIS A 1 37 ? 35.077 -7.737 -24.242 1.00 64.39 ? 37 HIS A CD2 1 ATOM 291 C CE1 . HIS A 1 37 ? 34.501 -6.404 -22.595 1.00 65.65 ? 37 HIS A CE1 1 ATOM 292 N NE2 . HIS A 1 37 ? 35.485 -6.712 -23.420 1.00 65.70 ? 37 HIS A NE2 1 ATOM 293 N N . ASN A 1 38 ? 30.136 -7.646 -24.280 1.00 69.29 ? 38 ASN A N 1 ATOM 294 C CA . ASN A 1 38 ? 29.183 -6.594 -23.874 1.00 70.45 ? 38 ASN A CA 1 ATOM 295 C C . ASN A 1 38 ? 29.596 -5.818 -22.617 1.00 70.84 ? 38 ASN A C 1 ATOM 296 O O . ASN A 1 38 ? 28.912 -4.881 -22.210 1.00 73.31 ? 38 ASN A O 1 ATOM 297 C CB . ASN A 1 38 ? 27.771 -7.175 -23.690 1.00 70.81 ? 38 ASN A CB 1 ATOM 298 C CG . ASN A 1 38 ? 27.621 -7.985 -22.412 1.00 69.88 ? 38 ASN A CG 1 ATOM 299 O OD1 . ASN A 1 38 ? 28.604 -8.362 -21.776 1.00 69.89 ? 38 ASN A OD1 1 ATOM 300 N ND2 . ASN A 1 38 ? 26.386 -8.263 -22.037 1.00 70.21 ? 38 ASN A ND2 1 ATOM 301 N N . GLY A 1 39 ? 30.675 -6.251 -21.977 1.00 69.27 ? 39 GLY A N 1 ATOM 302 C CA . GLY A 1 39 ? 31.295 -5.500 -20.883 1.00 69.08 ? 39 GLY A CA 1 ATOM 303 C C . GLY A 1 39 ? 30.566 -5.610 -19.558 1.00 70.44 ? 39 GLY A C 1 ATOM 304 O O . GLY A 1 39 ? 30.817 -4.820 -18.647 1.00 68.93 ? 39 GLY A O 1 ATOM 305 N N . LYS A 1 40 ? 29.678 -6.600 -19.447 1.00 72.14 ? 40 LYS A N 1 ATOM 306 C CA . LYS A 1 40 ? 28.763 -6.717 -18.316 1.00 72.65 ? 40 LYS A CA 1 ATOM 307 C C . LYS A 1 40 ? 28.771 -8.099 -17.682 1.00 73.16 ? 40 LYS A C 1 ATOM 308 O O . LYS A 1 40 ? 29.108 -9.090 -18.326 1.00 72.32 ? 40 LYS A O 1 ATOM 309 C CB . LYS A 1 40 ? 27.353 -6.411 -18.787 1.00 74.40 ? 40 LYS A CB 1 ATOM 310 C CG . LYS A 1 40 ? 27.151 -4.964 -19.173 1.00 77.26 ? 40 LYS A CG 1 ATOM 311 C CD . LYS A 1 40 ? 25.827 -4.752 -19.882 1.00 79.98 ? 40 LYS A CD 1 ATOM 312 C CE . LYS A 1 40 ? 25.625 -3.278 -20.192 1.00 83.61 ? 40 LYS A CE 1 ATOM 313 N NZ . LYS A 1 40 ? 24.556 -3.061 -21.206 1.00 87.67 ? 40 LYS A NZ 1 ATOM 314 N N . LEU A 1 41 ? 28.385 -8.156 -16.411 1.00 75.79 ? 41 LEU A N 1 ATOM 315 C CA . LEU A 1 41 ? 28.115 -9.428 -15.746 1.00 76.42 ? 41 LEU A CA 1 ATOM 316 C C . LEU A 1 41 ? 26.619 -9.708 -15.844 1.00 76.02 ? 41 LEU A C 1 ATOM 317 O O . LEU A 1 41 ? 25.800 -8.846 -15.523 1.00 75.99 ? 41 LEU A O 1 ATOM 318 C CB . LEU A 1 41 ? 28.567 -9.383 -14.289 1.00 76.95 ? 41 LEU A CB 1 ATOM 319 C CG . LEU A 1 41 ? 30.046 -9.053 -14.106 1.00 77.73 ? 41 LEU A CG 1 ATOM 320 C CD1 . LEU A 1 41 ? 30.365 -8.964 -12.623 1.00 78.83 ? 41 LEU A CD1 1 ATOM 321 C CD2 . LEU A 1 41 ? 30.943 -10.074 -14.798 1.00 76.48 ? 41 LEU A CD2 1 ATOM 322 N N . CYS A 1 42 ? 26.274 -10.912 -16.291 1.00 74.67 ? 42 CYS A N 1 ATOM 323 C CA . CYS A 1 42 ? 24.906 -11.227 -16.688 1.00 76.40 ? 42 CYS A CA 1 ATOM 324 C C . CYS A 1 42 ? 24.437 -12.535 -16.109 1.00 73.95 ? 42 CYS A C 1 ATOM 325 O O . CYS A 1 42 ? 25.241 -13.363 -15.685 1.00 69.89 ? 42 CYS A O 1 ATOM 326 C CB . CYS A 1 42 ? 24.825 -11.345 -18.209 1.00 79.41 ? 42 CYS A CB 1 ATOM 327 S SG . CYS A 1 42 ? 25.489 -9.922 -19.091 1.00 81.10 ? 42 CYS A SG 1 ATOM 328 N N . ASP A 1 43 ? 23.122 -12.723 -16.126 1.00 75.59 ? 43 ASP A N 1 ATOM 329 C CA . ASP A 1 43 ? 22.536 -14.022 -15.839 1.00 76.02 ? 43 ASP A CA 1 ATOM 330 C C . ASP A 1 43 ? 23.126 -15.010 -16.822 1.00 74.50 ? 43 ASP A C 1 ATOM 331 O O . ASP A 1 43 ? 23.305 -14.692 -17.997 1.00 72.70 ? 43 ASP A O 1 ATOM 332 C CB . ASP A 1 43 ? 21.010 -14.007 -16.006 1.00 78.59 ? 43 ASP A CB 1 ATOM 333 C CG . ASP A 1 43 ? 20.314 -13.072 -15.033 1.00 80.10 ? 43 ASP A CG 1 ATOM 334 O OD1 . ASP A 1 43 ? 20.988 -12.457 -14.188 1.00 79.03 ? 43 ASP A OD1 1 ATOM 335 O OD2 . ASP A 1 43 ? 19.080 -12.941 -15.122 1.00 83.46 ? 43 ASP A OD2 1 ATOM 336 N N . LEU A 1 44 ? 23.456 -16.195 -16.333 1.00 76.15 ? 44 LEU A N 1 ATOM 337 C CA . LEU A 1 44 ? 23.876 -17.276 -17.197 1.00 79.09 ? 44 LEU A CA 1 ATOM 338 C C . LEU A 1 44 ? 22.642 -18.120 -17.481 1.00 85.16 ? 44 LEU A C 1 ATOM 339 O O . LEU A 1 44 ? 22.173 -18.869 -16.622 1.00 85.73 ? 44 LEU A O 1 ATOM 340 C CB . LEU A 1 44 ? 24.977 -18.114 -16.540 1.00 78.39 ? 44 LEU A CB 1 ATOM 341 C CG . LEU A 1 44 ? 25.647 -19.165 -17.434 1.00 79.18 ? 44 LEU A CG 1 ATOM 342 C CD1 . LEU A 1 44 ? 26.379 -18.508 -18.599 1.00 78.54 ? 44 LEU A CD1 1 ATOM 343 C CD2 . LEU A 1 44 ? 26.604 -20.036 -16.631 1.00 77.84 ? 44 LEU A CD2 1 ATOM 344 N N . ASP A 1 45 ? 22.090 -17.957 -18.680 1.00 89.36 ? 45 ASP A N 1 ATOM 345 C CA . ASP A 1 45 ? 20.982 -18.783 -19.130 1.00 92.35 ? 45 ASP A CA 1 ATOM 346 C C . ASP A 1 45 ? 19.784 -18.653 -18.184 1.00 91.14 ? 45 ASP A C 1 ATOM 347 O O . ASP A 1 45 ? 19.174 -19.648 -17.795 1.00 90.52 ? 45 ASP A O 1 ATOM 348 C CB . ASP A 1 45 ? 21.457 -20.236 -19.237 1.00 96.30 ? 45 ASP A CB 1 ATOM 349 C CG . ASP A 1 45 ? 20.937 -20.919 -20.468 1.00 103.82 ? 45 ASP A CG 1 ATOM 350 O OD1 . ASP A 1 45 ? 19.712 -21.183 -20.521 1.00 110.08 ? 45 ASP A OD1 1 ATOM 351 O OD2 . ASP A 1 45 ? 21.757 -21.170 -21.386 1.00 103.79 ? 45 ASP A OD2 1 ATOM 352 N N . GLY A 1 46 ? 19.474 -17.413 -17.809 1.00 88.77 ? 46 GLY A N 1 ATOM 353 C CA . GLY A 1 46 ? 18.355 -17.111 -16.922 1.00 89.64 ? 46 GLY A CA 1 ATOM 354 C C . GLY A 1 46 ? 18.680 -17.078 -15.435 1.00 88.90 ? 46 GLY A C 1 ATOM 355 O O . GLY A 1 46 ? 17.930 -16.478 -14.662 1.00 91.72 ? 46 GLY A O 1 ATOM 356 N N . VAL A 1 47 ? 19.787 -17.710 -15.032 1.00 83.95 ? 47 VAL A N 1 ATOM 357 C CA . VAL A 1 47 ? 20.139 -17.867 -13.613 1.00 81.63 ? 47 VAL A CA 1 ATOM 358 C C . VAL A 1 47 ? 21.183 -16.841 -13.155 1.00 79.30 ? 47 VAL A C 1 ATOM 359 O O . VAL A 1 47 ? 22.369 -16.971 -13.463 1.00 76.65 ? 47 VAL A O 1 ATOM 360 C CB . VAL A 1 47 ? 20.682 -19.284 -13.336 1.00 80.51 ? 47 VAL A CB 1 ATOM 361 C CG1 . VAL A 1 47 ? 21.005 -19.462 -11.856 1.00 80.85 ? 47 VAL A CG1 1 ATOM 362 C CG2 . VAL A 1 47 ? 19.685 -20.331 -13.802 1.00 82.11 ? 47 VAL A CG2 1 ATOM 363 N N . LYS A 1 48 ? 20.736 -15.844 -12.397 1.00 79.84 ? 48 LYS A N 1 ATOM 364 C CA . LYS A 1 48 ? 21.593 -14.745 -11.933 1.00 79.22 ? 48 LYS A CA 1 ATOM 365 C C . LYS A 1 48 ? 22.795 -15.214 -11.095 1.00 77.41 ? 48 LYS A C 1 ATOM 366 O O . LYS A 1 48 ? 22.676 -16.167 -10.322 1.00 78.43 ? 48 LYS A O 1 ATOM 367 C CB . LYS A 1 48 ? 20.757 -13.753 -11.110 1.00 81.36 ? 48 LYS A CB 1 ATOM 368 C CG . LYS A 1 48 ? 21.480 -12.461 -10.776 1.00 82.39 ? 48 LYS A CG 1 ATOM 369 C CD . LYS A 1 48 ? 20.723 -11.565 -9.813 1.00 85.17 ? 48 LYS A CD 1 ATOM 370 C CE . LYS A 1 48 ? 21.636 -10.448 -9.325 1.00 86.01 ? 48 LYS A CE 1 ATOM 371 N NZ . LYS A 1 48 ? 20.892 -9.324 -8.697 1.00 91.12 ? 48 LYS A NZ 1 ATOM 372 N N . PRO A 1 49 ? 23.959 -14.542 -11.243 1.00 74.68 ? 49 PRO A N 1 ATOM 373 C CA . PRO A 1 49 ? 25.096 -14.884 -10.385 1.00 72.17 ? 49 PRO A CA 1 ATOM 374 C C . PRO A 1 49 ? 24.951 -14.339 -8.974 1.00 71.68 ? 49 PRO A C 1 ATOM 375 O O . PRO A 1 49 ? 24.190 -13.402 -8.748 1.00 72.29 ? 49 PRO A O 1 ATOM 376 C CB . PRO A 1 49 ? 26.276 -14.188 -11.070 1.00 69.21 ? 49 PRO A CB 1 ATOM 377 C CG . PRO A 1 49 ? 25.665 -13.013 -11.745 1.00 70.85 ? 49 PRO A CG 1 ATOM 378 C CD . PRO A 1 49 ? 24.322 -13.501 -12.228 1.00 73.57 ? 49 PRO A CD 1 ATOM 379 N N . LEU A 1 50 ? 25.692 -14.928 -8.042 1.00 70.83 ? 50 LEU A N 1 ATOM 380 C CA . LEU A 1 50 ? 25.868 -14.360 -6.711 1.00 70.77 ? 50 LEU A CA 1 ATOM 381 C C . LEU A 1 50 ? 26.975 -13.324 -6.793 1.00 69.00 ? 50 LEU A C 1 ATOM 382 O O . LEU A 1 50 ? 28.131 -13.672 -7.020 1.00 69.03 ? 50 LEU A O 1 ATOM 383 C CB . LEU A 1 50 ? 26.248 -15.449 -5.700 1.00 71.24 ? 50 LEU A CB 1 ATOM 384 C CG . LEU A 1 50 ? 26.613 -15.009 -4.276 1.00 71.30 ? 50 LEU A CG 1 ATOM 385 C CD1 . LEU A 1 50 ? 25.515 -14.146 -3.679 1.00 72.66 ? 50 LEU A CD1 1 ATOM 386 C CD2 . LEU A 1 50 ? 26.884 -16.216 -3.386 1.00 71.90 ? 50 LEU A CD2 1 ATOM 387 N N . ILE A 1 51 ? 26.622 -12.056 -6.624 1.00 69.79 ? 51 ILE A N 1 ATOM 388 C CA . ILE A 1 51 ? 27.600 -10.973 -6.687 1.00 69.04 ? 51 ILE A CA 1 ATOM 389 C C . ILE A 1 51 ? 27.891 -10.455 -5.279 1.00 68.52 ? 51 ILE A C 1 ATOM 390 O O . ILE A 1 51 ? 27.145 -9.649 -4.732 1.00 69.37 ? 51 ILE A O 1 ATOM 391 C CB . ILE A 1 51 ? 27.115 -9.854 -7.626 1.00 70.38 ? 51 ILE A CB 1 ATOM 392 C CG1 . ILE A 1 51 ? 26.995 -10.426 -9.042 1.00 71.91 ? 51 ILE A CG1 1 ATOM 393 C CG2 . ILE A 1 51 ? 28.069 -8.662 -7.601 1.00 69.78 ? 51 ILE A CG2 1 ATOM 394 C CD1 . ILE A 1 51 ? 26.521 -9.438 -10.082 1.00 74.33 ? 51 ILE A CD1 1 ATOM 395 N N . LEU A 1 52 ? 28.996 -10.924 -4.706 1.00 67.62 ? 52 LEU A N 1 ATOM 396 C CA . LEU A 1 52 ? 29.343 -10.625 -3.315 1.00 67.61 ? 52 LEU A CA 1 ATOM 397 C C . LEU A 1 52 ? 29.673 -9.156 -3.076 1.00 68.45 ? 52 LEU A C 1 ATOM 398 O O . LEU A 1 52 ? 29.713 -8.715 -1.932 1.00 67.61 ? 52 LEU A O 1 ATOM 399 C CB . LEU A 1 52 ? 30.515 -11.496 -2.859 1.00 65.97 ? 52 LEU A CB 1 ATOM 400 C CG . LEU A 1 52 ? 30.255 -13.007 -2.858 1.00 66.74 ? 52 LEU A CG 1 ATOM 401 C CD1 . LEU A 1 52 ? 31.548 -13.776 -2.645 1.00 65.92 ? 52 LEU A CD1 1 ATOM 402 C CD2 . LEU A 1 52 ? 29.223 -13.393 -1.808 1.00 68.29 ? 52 LEU A CD2 1 ATOM 403 N N . ARG A 1 53 ? 29.922 -8.412 -4.151 1.00 70.81 ? 53 ARG A N 1 ATOM 404 C CA . ARG A 1 53 ? 30.186 -6.980 -4.075 1.00 75.21 ? 53 ARG A CA 1 ATOM 405 C C . ARG A 1 53 ? 31.404 -6.693 -3.172 1.00 75.07 ? 53 ARG A C 1 ATOM 406 O O . ARG A 1 53 ? 32.533 -7.077 -3.519 1.00 76.36 ? 53 ARG A O 1 ATOM 407 C CB . ARG A 1 53 ? 28.914 -6.253 -3.634 1.00 81.12 ? 53 ARG A CB 1 ATOM 408 C CG . ARG A 1 53 ? 28.950 -4.738 -3.776 1.00 87.88 ? 53 ARG A CG 1 ATOM 409 C CD . ARG A 1 53 ? 27.802 -4.104 -3.006 1.00 93.75 ? 53 ARG A CD 1 ATOM 410 N NE . ARG A 1 53 ? 26.527 -4.730 -3.358 1.00 99.11 ? 53 ARG A NE 1 ATOM 411 C CZ . ARG A 1 53 ? 25.722 -4.338 -4.344 1.00 101.85 ? 53 ARG A CZ 1 ATOM 412 N NH1 . ARG A 1 53 ? 26.025 -3.288 -5.105 1.00 104.50 ? 53 ARG A NH1 1 ATOM 413 N NH2 . ARG A 1 53 ? 24.594 -5.003 -4.567 1.00 103.21 ? 53 ARG A NH2 1 ATOM 414 N N . ASP A 1 54 ? 31.185 -6.063 -2.019 1.00 74.72 ? 54 ASP A N 1 ATOM 415 C CA . ASP A 1 54 ? 32.266 -5.729 -1.099 1.00 74.32 ? 54 ASP A CA 1 ATOM 416 C C . ASP A 1 54 ? 32.540 -6.820 -0.069 1.00 73.29 ? 54 ASP A C 1 ATOM 417 O O . ASP A 1 54 ? 33.457 -6.679 0.733 1.00 74.89 ? 54 ASP A O 1 ATOM 418 C CB . ASP A 1 54 ? 31.959 -4.420 -0.362 1.00 76.92 ? 54 ASP A CB 1 ATOM 419 C CG . ASP A 1 54 ? 32.000 -3.204 -1.272 1.00 78.72 ? 54 ASP A CG 1 ATOM 420 O OD1 . ASP A 1 54 ? 32.878 -3.144 -2.166 1.00 77.00 ? 54 ASP A OD1 1 ATOM 421 O OD2 . ASP A 1 54 ? 31.156 -2.298 -1.076 1.00 80.57 ? 54 ASP A OD2 1 ATOM 422 N N . CYS A 1 55 ? 31.760 -7.896 -0.070 1.00 73.66 ? 55 CYS A N 1 ATOM 423 C CA . CYS A 1 55 ? 32.026 -9.008 0.844 1.00 75.04 ? 55 CYS A CA 1 ATOM 424 C C . CYS A 1 55 ? 32.918 -10.047 0.185 1.00 72.08 ? 55 CYS A C 1 ATOM 425 O O . CYS A 1 55 ? 32.985 -10.137 -1.035 1.00 73.66 ? 55 CYS A O 1 ATOM 426 C CB . CYS A 1 55 ? 30.728 -9.656 1.333 1.00 76.29 ? 55 CYS A CB 1 ATOM 427 S SG . CYS A 1 55 ? 29.735 -8.535 2.336 1.00 83.20 ? 55 CYS A SG 1 ATOM 428 N N . SER A 1 56 ? 33.613 -10.815 1.017 1.00 71.11 ? 56 SER A N 1 ATOM 429 C CA . SER A 1 56 ? 34.380 -11.968 0.574 1.00 68.92 ? 56 SER A CA 1 ATOM 430 C C . SER A 1 56 ? 33.618 -13.245 0.918 1.00 68.90 ? 56 SER A C 1 ATOM 431 O O . SER A 1 56 ? 32.594 -13.209 1.600 1.00 68.03 ? 56 SER A O 1 ATOM 432 C CB . SER A 1 56 ? 35.740 -11.989 1.264 1.00 68.19 ? 56 SER A CB 1 ATOM 433 O OG . SER A 1 56 ? 35.630 -12.521 2.573 1.00 68.12 ? 56 SER A OG 1 ATOM 434 N N . VAL A 1 57 ? 34.136 -14.380 0.470 1.00 68.56 ? 57 VAL A N 1 ATOM 435 C CA . VAL A 1 57 ? 33.473 -15.655 0.722 1.00 70.48 ? 57 VAL A CA 1 ATOM 436 C C . VAL A 1 57 ? 33.430 -15.956 2.226 1.00 70.23 ? 57 VAL A C 1 ATOM 437 O O . VAL A 1 57 ? 32.459 -16.529 2.716 1.00 70.59 ? 57 VAL A O 1 ATOM 438 C CB . VAL A 1 57 ? 34.144 -16.804 -0.065 1.00 71.38 ? 57 VAL A CB 1 ATOM 439 C CG1 . VAL A 1 57 ? 33.508 -18.143 0.279 1.00 72.81 ? 57 VAL A CG1 1 ATOM 440 C CG2 . VAL A 1 57 ? 34.038 -16.543 -1.564 1.00 71.48 ? 57 VAL A CG2 1 ATOM 441 N N . ALA A 1 58 ? 34.476 -15.553 2.948 1.00 69.31 ? 58 ALA A N 1 ATOM 442 C CA . ALA A 1 58 ? 34.521 -15.697 4.404 1.00 69.03 ? 58 ALA A CA 1 ATOM 443 C C . ALA A 1 58 ? 33.495 -14.785 5.085 1.00 70.02 ? 58 ALA A C 1 ATOM 444 O O . ALA A 1 58 ? 32.656 -15.250 5.864 1.00 71.28 ? 58 ALA A O 1 ATOM 445 C CB . ALA A 1 58 ? 35.914 -15.399 4.922 1.00 67.72 ? 58 ALA A CB 1 ATOM 446 N N . GLY A 1 59 ? 33.555 -13.493 4.779 1.00 68.48 ? 59 GLY A N 1 ATOM 447 C CA . GLY A 1 59 ? 32.567 -12.543 5.271 1.00 69.30 ? 59 GLY A CA 1 ATOM 448 C C . GLY A 1 59 ? 31.141 -13.023 5.051 1.00 71.62 ? 59 GLY A C 1 ATOM 449 O O . GLY A 1 59 ? 30.293 -12.879 5.927 1.00 77.10 ? 59 GLY A O 1 ATOM 450 N N . TRP A 1 60 ? 30.878 -13.602 3.883 1.00 71.08 ? 60 TRP A N 1 ATOM 451 C CA . TRP A 1 60 ? 29.545 -14.085 3.547 1.00 71.13 ? 60 TRP A CA 1 ATOM 452 C C . TRP A 1 60 ? 29.157 -15.279 4.411 1.00 73.35 ? 60 TRP A C 1 ATOM 453 O O . TRP A 1 60 ? 28.104 -15.269 5.056 1.00 75.56 ? 60 TRP A O 1 ATOM 454 C CB . TRP A 1 60 ? 29.462 -14.447 2.057 1.00 70.16 ? 60 TRP A CB 1 ATOM 455 C CG . TRP A 1 60 ? 28.302 -15.336 1.688 1.00 70.01 ? 60 TRP A CG 1 ATOM 456 C CD1 . TRP A 1 60 ? 27.022 -15.252 2.153 1.00 70.91 ? 60 TRP A CD1 1 ATOM 457 C CD2 . TRP A 1 60 ? 28.319 -16.427 0.759 1.00 68.45 ? 60 TRP A CD2 1 ATOM 458 N NE1 . TRP A 1 60 ? 26.247 -16.232 1.583 1.00 72.13 ? 60 TRP A NE1 1 ATOM 459 C CE2 . TRP A 1 60 ? 27.018 -16.965 0.721 1.00 69.96 ? 60 TRP A CE2 1 ATOM 460 C CE3 . TRP A 1 60 ? 29.311 -17.002 -0.044 1.00 66.86 ? 60 TRP A CE3 1 ATOM 461 C CZ2 . TRP A 1 60 ? 26.681 -18.054 -0.083 1.00 70.64 ? 60 TRP A CZ2 1 ATOM 462 C CZ3 . TRP A 1 60 ? 28.977 -18.084 -0.844 1.00 66.59 ? 60 TRP A CZ3 1 ATOM 463 C CH2 . TRP A 1 60 ? 27.674 -18.597 -0.858 1.00 69.46 ? 60 TRP A CH2 1 ATOM 464 N N . LEU A 1 61 ? 30.009 -16.299 4.428 1.00 73.24 ? 61 LEU A N 1 ATOM 465 C CA . LEU A 1 61 ? 29.666 -17.570 5.074 1.00 74.46 ? 61 LEU A CA 1 ATOM 466 C C . LEU A 1 61 ? 29.633 -17.481 6.598 1.00 74.60 ? 61 LEU A C 1 ATOM 467 O O . LEU A 1 61 ? 28.701 -17.976 7.228 1.00 75.76 ? 61 LEU A O 1 ATOM 468 C CB . LEU A 1 61 ? 30.617 -18.681 4.624 1.00 73.65 ? 61 LEU A CB 1 ATOM 469 C CG . LEU A 1 61 ? 30.453 -19.089 3.157 1.00 73.63 ? 61 LEU A CG 1 ATOM 470 C CD1 . LEU A 1 61 ? 31.544 -20.067 2.752 1.00 74.45 ? 61 LEU A CD1 1 ATOM 471 C CD2 . LEU A 1 61 ? 29.081 -19.688 2.893 1.00 75.08 ? 61 LEU A CD2 1 ATOM 472 N N . LEU A 1 62 ? 30.640 -16.845 7.186 1.00 73.58 ? 62 LEU A N 1 ATOM 473 C CA . LEU A 1 62 ? 30.646 -16.597 8.630 1.00 73.34 ? 62 LEU A CA 1 ATOM 474 C C . LEU A 1 62 ? 29.550 -15.617 9.059 1.00 76.07 ? 62 LEU A C 1 ATOM 475 O O . LEU A 1 62 ? 29.149 -15.600 10.223 1.00 77.72 ? 62 LEU A O 1 ATOM 476 C CB . LEU A 1 62 ? 32.007 -16.072 9.076 1.00 71.22 ? 62 LEU A CB 1 ATOM 477 C CG . LEU A 1 62 ? 33.147 -17.084 8.999 1.00 69.65 ? 62 LEU A CG 1 ATOM 478 C CD1 . LEU A 1 62 ? 34.473 -16.368 9.128 1.00 68.25 ? 62 LEU A CD1 1 ATOM 479 C CD2 . LEU A 1 62 ? 33.005 -18.156 10.070 1.00 71.05 ? 62 LEU A CD2 1 ATOM 480 N N . GLY A 1 63 ? 29.064 -14.805 8.121 1.00 77.53 ? 63 GLY A N 1 ATOM 481 C CA . GLY A 1 63 ? 27.980 -13.865 8.402 1.00 78.71 ? 63 GLY A CA 1 ATOM 482 C C . GLY A 1 63 ? 28.472 -12.579 9.043 1.00 77.50 ? 63 GLY A C 1 ATOM 483 O O . GLY A 1 63 ? 27.910 -12.122 10.038 1.00 75.35 ? 63 GLY A O 1 ATOM 484 N N . ASN A 1 64 ? 29.531 -12.006 8.471 1.00 75.44 ? 64 ASN A N 1 ATOM 485 C CA . ASN A 1 64 ? 30.000 -10.674 8.838 1.00 74.89 ? 64 ASN A CA 1 ATOM 486 C C . ASN A 1 64 ? 28.816 -9.709 8.768 1.00 76.88 ? 64 ASN A C 1 ATOM 487 O O . ASN A 1 64 ? 28.165 -9.629 7.734 1.00 77.98 ? 64 ASN A O 1 ATOM 488 C CB . ASN A 1 64 ? 31.117 -10.246 7.873 1.00 72.75 ? 64 ASN A CB 1 ATOM 489 C CG . ASN A 1 64 ? 31.638 -8.840 8.138 1.00 70.79 ? 64 ASN A CG 1 ATOM 490 O OD1 . ASN A 1 64 ? 30.889 -7.944 8.507 1.00 70.65 ? 64 ASN A OD1 1 ATOM 491 N ND2 . ASN A 1 64 ? 32.930 -8.639 7.913 1.00 69.38 ? 64 ASN A ND2 1 ATOM 492 N N . PRO A 1 65 ? 28.527 -8.981 9.866 1.00 79.90 ? 65 PRO A N 1 ATOM 493 C CA . PRO A 1 65 ? 27.311 -8.150 9.939 1.00 81.62 ? 65 PRO A CA 1 ATOM 494 C C . PRO A 1 65 ? 27.191 -7.054 8.872 1.00 82.98 ? 65 PRO A C 1 ATOM 495 O O . PRO A 1 65 ? 26.101 -6.521 8.669 1.00 85.36 ? 65 PRO A O 1 ATOM 496 C CB . PRO A 1 65 ? 27.379 -7.534 11.339 1.00 83.36 ? 65 PRO A CB 1 ATOM 497 C CG . PRO A 1 65 ? 28.798 -7.672 11.773 1.00 82.32 ? 65 PRO A CG 1 ATOM 498 C CD . PRO A 1 65 ? 29.325 -8.899 11.103 1.00 80.74 ? 65 PRO A CD 1 ATOM 499 N N . MET A 1 66 ? 28.296 -6.732 8.201 1.00 83.67 ? 66 MET A N 1 ATOM 500 C CA . MET A 1 66 ? 28.277 -5.877 7.006 1.00 85.23 ? 66 MET A CA 1 ATOM 501 C C . MET A 1 66 ? 27.813 -6.624 5.744 1.00 83.07 ? 66 MET A C 1 ATOM 502 O O . MET A 1 66 ? 27.730 -6.027 4.676 1.00 81.57 ? 66 MET A O 1 ATOM 503 C CB . MET A 1 66 ? 29.680 -5.309 6.745 1.00 86.54 ? 66 MET A CB 1 ATOM 504 C CG . MET A 1 66 ? 30.182 -4.333 7.796 1.00 88.25 ? 66 MET A CG 1 ATOM 505 S SD . MET A 1 66 ? 29.604 -2.655 7.495 1.00 92.64 ? 66 MET A SD 1 ATOM 506 C CE . MET A 1 66 ? 30.572 -1.737 8.697 1.00 94.55 ? 66 MET A CE 1 ATOM 507 N N . CYS A 1 67 ? 27.522 -7.918 5.868 1.00 82.96 ? 67 CYS A N 1 ATOM 508 C CA . CYS A 1 67 ? 27.200 -8.771 4.724 1.00 83.52 ? 67 CYS A CA 1 ATOM 509 C C . CYS A 1 67 ? 25.807 -9.393 4.858 1.00 85.46 ? 67 CYS A C 1 ATOM 510 O O . CYS A 1 67 ? 25.596 -10.563 4.523 1.00 85.39 ? 67 CYS A O 1 ATOM 511 C CB . CYS A 1 67 ? 28.262 -9.864 4.590 1.00 82.34 ? 67 CYS A CB 1 ATOM 512 S SG . CYS A 1 67 ? 29.916 -9.211 4.261 1.00 82.51 ? 67 CYS A SG 1 ATOM 513 N N . ASP A 1 68 ? 24.857 -8.594 5.338 1.00 86.19 ? 68 ASP A N 1 ATOM 514 C CA . ASP A 1 68 ? 23.483 -9.052 5.528 1.00 87.02 ? 68 ASP A CA 1 ATOM 515 C C . ASP A 1 68 ? 22.736 -9.202 4.213 1.00 88.00 ? 68 ASP A C 1 ATOM 516 O O . ASP A 1 68 ? 21.765 -9.950 4.145 1.00 90.32 ? 68 ASP A O 1 ATOM 517 C CB . ASP A 1 68 ? 22.716 -8.108 6.460 1.00 88.51 ? 68 ASP A CB 1 ATOM 518 C CG . ASP A 1 68 ? 23.187 -8.200 7.900 1.00 88.40 ? 68 ASP A CG 1 ATOM 519 O OD1 . ASP A 1 68 ? 24.235 -8.833 8.151 1.00 88.07 ? 68 ASP A OD1 1 ATOM 520 O OD2 . ASP A 1 68 ? 22.512 -7.641 8.786 1.00 88.91 ? 68 ASP A OD2 1 ATOM 521 N N . GLU A 1 69 ? 23.183 -8.506 3.168 1.00 87.44 ? 69 GLU A N 1 ATOM 522 C CA . GLU A 1 69 ? 22.602 -8.675 1.830 1.00 87.73 ? 69 GLU A CA 1 ATOM 523 C C . GLU A 1 69 ? 22.571 -10.153 1.437 1.00 86.14 ? 69 GLU A C 1 ATOM 524 O O . GLU A 1 69 ? 21.657 -10.602 0.740 1.00 87.86 ? 69 GLU A O 1 ATOM 525 C CB . GLU A 1 69 ? 23.389 -7.880 0.776 1.00 87.44 ? 69 GLU A CB 1 ATOM 526 C CG . GLU A 1 69 ? 22.752 -7.890 -0.615 1.00 88.07 ? 69 GLU A CG 1 ATOM 527 C CD . GLU A 1 69 ? 23.612 -7.244 -1.689 1.00 86.88 ? 69 GLU A CD 1 ATOM 528 O OE1 . GLU A 1 69 ? 24.587 -6.538 -1.361 1.00 85.03 ? 69 GLU A OE1 1 ATOM 529 O OE2 . GLU A 1 69 ? 23.302 -7.439 -2.881 1.00 88.97 ? 69 GLU A OE2 1 ATOM 530 N N . PHE A 1 70 ? 23.568 -10.898 1.904 1.00 83.25 ? 70 PHE A N 1 ATOM 531 C CA . PHE A 1 70 ? 23.721 -12.306 1.564 1.00 82.36 ? 70 PHE A CA 1 ATOM 532 C C . PHE A 1 70 ? 23.324 -13.225 2.724 1.00 83.55 ? 70 PHE A C 1 ATOM 533 O O . PHE A 1 70 ? 23.797 -14.361 2.823 1.00 79.43 ? 70 PHE A O 1 ATOM 534 C CB . PHE A 1 70 ? 25.165 -12.550 1.121 1.00 79.28 ? 70 PHE A CB 1 ATOM 535 C CG . PHE A 1 70 ? 25.696 -11.469 0.219 1.00 77.94 ? 70 PHE A CG 1 ATOM 536 C CD1 . PHE A 1 70 ? 25.264 -11.374 -1.096 1.00 77.18 ? 70 PHE A CD1 1 ATOM 537 C CD2 . PHE A 1 70 ? 26.584 -10.515 0.699 1.00 76.57 ? 70 PHE A CD2 1 ATOM 538 C CE1 . PHE A 1 70 ? 25.733 -10.371 -1.926 1.00 76.02 ? 70 PHE A CE1 1 ATOM 539 C CE2 . PHE A 1 70 ? 27.054 -9.509 -0.127 1.00 75.48 ? 70 PHE A CE2 1 ATOM 540 C CZ . PHE A 1 70 ? 26.629 -9.437 -1.441 1.00 74.37 ? 70 PHE A CZ 1 ATOM 541 N N . ILE A 1 71 ? 22.430 -12.732 3.583 1.00 88.02 ? 71 ILE A N 1 ATOM 542 C CA . ILE A 1 71 ? 21.940 -13.503 4.729 1.00 91.38 ? 71 ILE A CA 1 ATOM 543 C C . ILE A 1 71 ? 21.239 -14.780 4.250 1.00 93.71 ? 71 ILE A C 1 ATOM 544 O O . ILE A 1 71 ? 21.392 -15.834 4.860 1.00 92.95 ? 71 ILE A O 1 ATOM 545 C CB . ILE A 1 71 ? 21.015 -12.652 5.649 1.00 94.06 ? 71 ILE A CB 1 ATOM 546 C CG1 . ILE A 1 71 ? 20.827 -13.318 7.022 1.00 95.09 ? 71 ILE A CG1 1 ATOM 547 C CG2 . ILE A 1 71 ? 19.668 -12.355 4.991 1.00 96.28 ? 71 ILE A CG2 1 ATOM 548 C CD1 . ILE A 1 71 ? 21.871 -12.923 8.049 1.00 92.57 ? 71 ILE A CD1 1 ATOM 549 N N . ASN A 1 72 ? 20.491 -14.684 3.151 1.00 95.17 ? 72 ASN A N 1 ATOM 550 C CA . ASN A 1 72 ? 19.892 -15.854 2.520 1.00 97.50 ? 72 ASN A CA 1 ATOM 551 C C . ASN A 1 72 ? 19.799 -15.656 1.014 1.00 96.24 ? 72 ASN A C 1 ATOM 552 O O . ASN A 1 72 ? 18.851 -15.057 0.509 1.00 101.19 ? 72 ASN A O 1 ATOM 553 C CB . ASN A 1 72 ? 18.516 -16.149 3.124 1.00 102.52 ? 72 ASN A CB 1 ATOM 554 C CG . ASN A 1 72 ? 18.607 -16.945 4.416 1.00 105.80 ? 72 ASN A CG 1 ATOM 555 O OD1 . ASN A 1 72 ? 19.249 -17.997 4.462 1.00 105.91 ? 72 ASN A OD1 1 ATOM 556 N ND2 . ASN A 1 72 ? 17.973 -16.443 5.476 1.00 108.84 ? 72 ASN A ND2 1 ATOM 557 N N . VAL A 1 73 ? 20.803 -16.156 0.304 1.00 91.37 ? 73 VAL A N 1 ATOM 558 C CA . VAL A 1 73 ? 20.880 -15.980 -1.141 1.00 88.58 ? 73 VAL A CA 1 ATOM 559 C C . VAL A 1 73 ? 20.318 -17.199 -1.857 1.00 87.04 ? 73 VAL A C 1 ATOM 560 O O . VAL A 1 73 ? 20.573 -18.332 -1.451 1.00 85.90 ? 73 VAL A O 1 ATOM 561 C CB . VAL A 1 73 ? 22.330 -15.726 -1.628 1.00 86.44 ? 73 VAL A CB 1 ATOM 562 C CG1 . VAL A 1 73 ? 22.925 -14.518 -0.919 1.00 84.63 ? 73 VAL A CG1 1 ATOM 563 C CG2 . VAL A 1 73 ? 23.215 -16.959 -1.451 1.00 85.00 ? 73 VAL A CG2 1 ATOM 564 N N . PRO A 1 74 ? 19.563 -16.969 -2.940 1.00 86.60 ? 74 PRO A N 1 ATOM 565 C CA . PRO A 1 74 ? 19.009 -18.065 -3.721 1.00 88.08 ? 74 PRO A CA 1 ATOM 566 C C . PRO A 1 74 ? 20.068 -18.767 -4.576 1.00 85.43 ? 74 PRO A C 1 ATOM 567 O O . PRO A 1 74 ? 21.245 -18.413 -4.522 1.00 82.12 ? 74 PRO A O 1 ATOM 568 C CB . PRO A 1 74 ? 17.985 -17.360 -4.613 1.00 90.01 ? 74 PRO A CB 1 ATOM 569 C CG . PRO A 1 74 ? 18.570 -16.010 -4.828 1.00 88.35 ? 74 PRO A CG 1 ATOM 570 C CD . PRO A 1 74 ? 19.235 -15.657 -3.529 1.00 86.81 ? 74 PRO A CD 1 ATOM 571 N N . GLU A 1 75 ? 19.635 -19.758 -5.351 1.00 86.52 ? 75 GLU A N 1 ATOM 572 C CA . GLU A 1 75 ? 20.510 -20.499 -6.254 1.00 85.90 ? 75 GLU A CA 1 ATOM 573 C C . GLU A 1 75 ? 21.230 -19.560 -7.221 1.00 84.27 ? 75 GLU A C 1 ATOM 574 O O . GLU A 1 75 ? 20.632 -18.610 -7.719 1.00 84.41 ? 75 GLU A O 1 ATOM 575 C CB . GLU A 1 75 ? 19.689 -21.524 -7.042 1.00 88.58 ? 75 GLU A CB 1 ATOM 576 C CG . GLU A 1 75 ? 20.487 -22.337 -8.054 1.00 88.00 ? 75 GLU A CG 1 ATOM 577 C CD . GLU A 1 75 ? 19.641 -23.340 -8.816 1.00 90.07 ? 75 GLU A CD 1 ATOM 578 O OE1 . GLU A 1 75 ? 18.449 -23.518 -8.479 1.00 93.76 ? 75 GLU A OE1 1 ATOM 579 O OE2 . GLU A 1 75 ? 20.178 -23.955 -9.761 1.00 89.31 ? 75 GLU A OE2 1 ATOM 580 N N . TRP A 1 76 ? 22.509 -19.833 -7.480 1.00 82.29 ? 76 TRP A N 1 ATOM 581 C CA . TRP A 1 76 ? 23.309 -19.016 -8.398 1.00 81.57 ? 76 TRP A CA 1 ATOM 582 C C . TRP A 1 76 ? 23.917 -19.852 -9.528 1.00 81.29 ? 76 TRP A C 1 ATOM 583 O O . TRP A 1 76 ? 23.997 -21.080 -9.443 1.00 84.74 ? 76 TRP A O 1 ATOM 584 C CB . TRP A 1 76 ? 24.419 -18.283 -7.638 1.00 78.91 ? 76 TRP A CB 1 ATOM 585 C CG . TRP A 1 76 ? 25.429 -19.203 -7.025 1.00 77.86 ? 76 TRP A CG 1 ATOM 586 C CD1 . TRP A 1 76 ? 26.547 -19.708 -7.621 1.00 76.62 ? 76 TRP A CD1 1 ATOM 587 C CD2 . TRP A 1 76 ? 25.407 -19.739 -5.696 1.00 77.35 ? 76 TRP A CD2 1 ATOM 588 N NE1 . TRP A 1 76 ? 27.223 -20.525 -6.745 1.00 75.95 ? 76 TRP A NE1 1 ATOM 589 C CE2 . TRP A 1 76 ? 26.544 -20.559 -5.557 1.00 75.47 ? 76 TRP A CE2 1 ATOM 590 C CE3 . TRP A 1 76 ? 24.537 -19.602 -4.610 1.00 77.64 ? 76 TRP A CE3 1 ATOM 591 C CZ2 . TRP A 1 76 ? 26.830 -21.240 -4.378 1.00 75.55 ? 76 TRP A CZ2 1 ATOM 592 C CZ3 . TRP A 1 76 ? 24.826 -20.275 -3.440 1.00 77.01 ? 76 TRP A CZ3 1 ATOM 593 C CH2 . TRP A 1 76 ? 25.959 -21.086 -3.333 1.00 76.16 ? 76 TRP A CH2 1 ATOM 594 N N . SER A 1 77 ? 24.344 -19.167 -10.582 1.00 79.07 ? 77 SER A N 1 ATOM 595 C CA . SER A 1 77 ? 25.015 -19.798 -11.717 1.00 77.79 ? 77 SER A CA 1 ATOM 596 C C . SER A 1 77 ? 26.526 -19.765 -11.500 1.00 74.65 ? 77 SER A C 1 ATOM 597 O O . SER A 1 77 ? 27.199 -20.791 -11.571 1.00 75.31 ? 77 SER A O 1 ATOM 598 C CB . SER A 1 77 ? 24.667 -19.050 -12.998 1.00 78.11 ? 77 SER A CB 1 ATOM 599 O OG . SER A 1 77 ? 24.791 -17.649 -12.801 1.00 78.38 ? 77 SER A OG 1 ATOM 600 N N . TYR A 1 78 ? 27.047 -18.572 -11.238 1.00 70.80 ? 78 TYR A N 1 ATOM 601 C CA . TYR A 1 78 ? 28.439 -18.396 -10.838 1.00 66.86 ? 78 TYR A CA 1 ATOM 602 C C . TYR A 1 78 ? 28.513 -17.366 -9.714 1.00 66.47 ? 78 TYR A C 1 ATOM 603 O O . TYR A 1 78 ? 27.520 -16.711 -9.395 1.00 67.24 ? 78 TYR A O 1 ATOM 604 C CB . TYR A 1 78 ? 29.309 -17.980 -12.040 1.00 63.85 ? 78 TYR A CB 1 ATOM 605 C CG . TYR A 1 78 ? 28.885 -16.698 -12.735 1.00 62.00 ? 78 TYR A CG 1 ATOM 606 C CD1 . TYR A 1 78 ? 27.833 -16.686 -13.647 1.00 62.87 ? 78 TYR A CD1 1 ATOM 607 C CD2 . TYR A 1 78 ? 29.539 -15.500 -12.482 1.00 60.52 ? 78 TYR A CD2 1 ATOM 608 C CE1 . TYR A 1 78 ? 27.444 -15.512 -14.280 1.00 62.65 ? 78 TYR A CE1 1 ATOM 609 C CE2 . TYR A 1 78 ? 29.160 -14.327 -13.112 1.00 60.21 ? 78 TYR A CE2 1 ATOM 610 C CZ . TYR A 1 78 ? 28.114 -14.336 -14.006 1.00 61.12 ? 78 TYR A CZ 1 ATOM 611 O OH . TYR A 1 78 ? 27.747 -13.158 -14.618 1.00 61.39 ? 78 TYR A OH 1 ATOM 612 N N . ILE A 1 79 ? 29.688 -17.240 -9.108 1.00 65.69 ? 79 ILE A N 1 ATOM 613 C CA . ILE A 1 79 ? 29.907 -16.299 -8.014 1.00 66.36 ? 79 ILE A CA 1 ATOM 614 C C . ILE A 1 79 ? 30.928 -15.257 -8.455 1.00 65.60 ? 79 ILE A C 1 ATOM 615 O O . ILE A 1 79 ? 31.874 -15.581 -9.173 1.00 63.37 ? 79 ILE A O 1 ATOM 616 C CB . ILE A 1 79 ? 30.431 -17.024 -6.760 1.00 67.83 ? 79 ILE A CB 1 ATOM 617 C CG1 . ILE A 1 79 ? 29.393 -18.022 -6.248 1.00 70.29 ? 79 ILE A CG1 1 ATOM 618 C CG2 . ILE A 1 79 ? 30.770 -16.035 -5.651 1.00 68.75 ? 79 ILE A CG2 1 ATOM 619 C CD1 . ILE A 1 79 ? 29.941 -18.976 -5.208 1.00 71.46 ? 79 ILE A CD1 1 ATOM 620 N N . VAL A 1 80 ? 30.744 -14.012 -8.022 1.00 67.08 ? 80 VAL A N 1 ATOM 621 C CA . VAL A 1 80 ? 31.687 -12.938 -8.347 1.00 67.27 ? 80 VAL A CA 1 ATOM 622 C C . VAL A 1 80 ? 32.195 -12.251 -7.082 1.00 67.25 ? 80 VAL A C 1 ATOM 623 O O . VAL A 1 80 ? 31.407 -11.742 -6.288 1.00 68.15 ? 80 VAL A O 1 ATOM 624 C CB . VAL A 1 80 ? 31.053 -11.883 -9.269 1.00 68.17 ? 80 VAL A CB 1 ATOM 625 C CG1 . VAL A 1 80 ? 32.051 -10.767 -9.567 1.00 67.11 ? 80 VAL A CG1 1 ATOM 626 C CG2 . VAL A 1 80 ? 30.560 -12.538 -10.551 1.00 68.37 ? 80 VAL A CG2 1 ATOM 627 N N . GLU A 1 81 ? 33.515 -12.231 -6.927 1.00 65.76 ? 81 GLU A N 1 ATOM 628 C CA . GLU A 1 81 ? 34.174 -11.681 -5.753 1.00 67.28 ? 81 GLU A CA 1 ATOM 629 C C . GLU A 1 81 ? 35.216 -10.687 -6.225 1.00 66.57 ? 81 GLU A C 1 ATOM 630 O O . GLU A 1 81 ? 35.917 -10.940 -7.197 1.00 67.17 ? 81 GLU A O 1 ATOM 631 C CB . GLU A 1 81 ? 34.853 -12.809 -4.970 1.00 69.03 ? 81 GLU A CB 1 ATOM 632 C CG . GLU A 1 81 ? 35.454 -12.404 -3.627 1.00 71.50 ? 81 GLU A CG 1 ATOM 633 C CD . GLU A 1 81 ? 36.342 -13.485 -3.017 1.00 72.70 ? 81 GLU A CD 1 ATOM 634 O OE1 . GLU A 1 81 ? 37.125 -14.118 -3.760 1.00 70.65 ? 81 GLU A OE1 1 ATOM 635 O OE2 . GLU A 1 81 ? 36.262 -13.704 -1.785 1.00 76.36 ? 81 GLU A OE2 1 ATOM 636 N N . LYS A 1 82 ? 35.335 -9.559 -5.541 1.00 68.62 ? 82 LYS A N 1 ATOM 637 C CA . LYS A 1 82 ? 36.361 -8.581 -5.899 1.00 68.91 ? 82 LYS A CA 1 ATOM 638 C C . LYS A 1 82 ? 37.764 -9.105 -5.561 1.00 68.31 ? 82 LYS A C 1 ATOM 639 O O . LYS A 1 82 ? 37.913 -10.107 -4.857 1.00 67.32 ? 82 LYS A O 1 ATOM 640 C CB . LYS A 1 82 ? 36.089 -7.240 -5.213 1.00 69.81 ? 82 LYS A CB 1 ATOM 641 C CG . LYS A 1 82 ? 34.907 -6.481 -5.801 1.00 71.11 ? 82 LYS A CG 1 ATOM 642 C CD . LYS A 1 82 ? 34.728 -5.126 -5.130 1.00 72.94 ? 82 LYS A CD 1 ATOM 643 C CE . LYS A 1 82 ? 33.999 -4.134 -6.021 1.00 75.27 ? 82 LYS A CE 1 ATOM 644 N NZ . LYS A 1 82 ? 32.628 -4.591 -6.371 1.00 77.94 ? 82 LYS A NZ 1 ATOM 645 N N . ALA A 1 83 ? 38.788 -8.436 -6.082 1.00 69.20 ? 83 ALA A N 1 ATOM 646 C CA . ALA A 1 83 ? 40.176 -8.834 -5.826 1.00 70.04 ? 83 ALA A CA 1 ATOM 647 C C . ALA A 1 83 ? 40.558 -8.661 -4.351 1.00 71.77 ? 83 ALA A C 1 ATOM 648 O O . ALA A 1 83 ? 41.182 -9.545 -3.760 1.00 73.83 ? 83 ALA A O 1 ATOM 649 C CB . ALA A 1 83 ? 41.129 -8.054 -6.724 1.00 68.85 ? 83 ALA A CB 1 ATOM 650 N N . ASN A 1 84 ? 40.177 -7.529 -3.761 1.00 72.04 ? 84 ASN A N 1 ATOM 651 C CA . ASN A 1 84 ? 40.419 -7.274 -2.342 1.00 73.98 ? 84 ASN A CA 1 ATOM 652 C C . ASN A 1 84 ? 39.175 -6.746 -1.646 1.00 73.28 ? 84 ASN A C 1 ATOM 653 O O . ASN A 1 84 ? 39.079 -5.548 -1.374 1.00 74.73 ? 84 ASN A O 1 ATOM 654 C CB . ASN A 1 84 ? 41.576 -6.292 -2.167 1.00 77.10 ? 84 ASN A CB 1 ATOM 655 C CG . ASN A 1 84 ? 42.889 -6.856 -2.670 1.00 79.28 ? 84 ASN A CG 1 ATOM 656 O OD1 . ASN A 1 84 ? 43.536 -7.657 -1.993 1.00 81.37 ? 84 ASN A OD1 1 ATOM 657 N ND2 . ASN A 1 84 ? 43.282 -6.453 -3.870 1.00 80.40 ? 84 ASN A ND2 1 ATOM 658 N N . PRO A 1 85 ? 38.215 -7.644 -1.349 1.00 71.90 ? 85 PRO A N 1 ATOM 659 C CA . PRO A 1 85 ? 36.974 -7.230 -0.696 1.00 72.58 ? 85 PRO A CA 1 ATOM 660 C C . PRO A 1 85 ? 37.259 -6.601 0.659 1.00 72.98 ? 85 PRO A C 1 ATOM 661 O O . PRO A 1 85 ? 38.055 -7.148 1.421 1.00 72.81 ? 85 PRO A O 1 ATOM 662 C CB . PRO A 1 85 ? 36.198 -8.547 -0.533 1.00 72.57 ? 85 PRO A CB 1 ATOM 663 C CG . PRO A 1 85 ? 36.828 -9.506 -1.484 1.00 70.22 ? 85 PRO A CG 1 ATOM 664 C CD . PRO A 1 85 ? 38.264 -9.102 -1.555 1.00 70.23 ? 85 PRO A CD 1 ATOM 665 N N . VAL A 1 86 ? 36.631 -5.463 0.950 1.00 74.13 ? 86 VAL A N 1 ATOM 666 C CA . VAL A 1 86 ? 36.906 -4.743 2.199 1.00 75.76 ? 86 VAL A CA 1 ATOM 667 C C . VAL A 1 86 ? 36.302 -5.436 3.416 1.00 74.23 ? 86 VAL A C 1 ATOM 668 O O . VAL A 1 86 ? 36.856 -5.349 4.507 1.00 75.90 ? 86 VAL A O 1 ATOM 669 C CB . VAL A 1 86 ? 36.414 -3.279 2.163 1.00 78.85 ? 86 VAL A CB 1 ATOM 670 C CG1 . VAL A 1 86 ? 36.944 -2.569 0.921 1.00 79.60 ? 86 VAL A CG1 1 ATOM 671 C CG2 . VAL A 1 86 ? 34.892 -3.206 2.237 1.00 81.04 ? 86 VAL A CG2 1 ATOM 672 N N . ASN A 1 87 ? 35.177 -6.119 3.222 1.00 72.84 ? 87 ASN A N 1 ATOM 673 C CA . ASN A 1 87 ? 34.478 -6.794 4.307 1.00 73.27 ? 87 ASN A CA 1 ATOM 674 C C . ASN A 1 87 ? 34.752 -8.293 4.320 1.00 72.37 ? 87 ASN A C 1 ATOM 675 O O . ASN A 1 87 ? 33.988 -9.088 3.775 1.00 72.58 ? 87 ASN A O 1 ATOM 676 C CB . ASN A 1 87 ? 32.981 -6.521 4.209 1.00 75.33 ? 87 ASN A CB 1 ATOM 677 C CG . ASN A 1 87 ? 32.644 -5.067 4.470 1.00 78.12 ? 87 ASN A CG 1 ATOM 678 O OD1 . ASN A 1 87 ? 33.101 -4.475 5.454 1.00 79.32 ? 87 ASN A OD1 1 ATOM 679 N ND2 . ASN A 1 87 ? 31.842 -4.480 3.592 1.00 79.49 ? 87 ASN A ND2 1 ATOM 680 N N . ASP A 1 88 ? 35.861 -8.660 4.954 1.00 72.89 ? 88 ASP A N 1 ATOM 681 C CA . ASP A 1 88 ? 36.304 -10.044 5.062 1.00 72.18 ? 88 ASP A CA 1 ATOM 682 C C . ASP A 1 88 ? 36.075 -10.469 6.523 1.00 73.01 ? 88 ASP A C 1 ATOM 683 O O . ASP A 1 88 ? 34.921 -10.630 6.938 1.00 70.66 ? 88 ASP A O 1 ATOM 684 C CB . ASP A 1 88 ? 37.777 -10.143 4.598 1.00 71.80 ? 88 ASP A CB 1 ATOM 685 C CG . ASP A 1 88 ? 38.289 -11.583 4.489 1.00 72.19 ? 88 ASP A CG 1 ATOM 686 O OD1 . ASP A 1 88 ? 37.479 -12.519 4.349 1.00 72.40 ? 88 ASP A OD1 1 ATOM 687 O OD2 . ASP A 1 88 ? 39.524 -11.776 4.530 1.00 73.80 ? 88 ASP A OD2 1 ATOM 688 N N . LEU A 1 89 ? 37.148 -10.613 7.304 1.00 73.39 ? 89 LEU A N 1 ATOM 689 C CA . LEU A 1 89 ? 37.050 -10.949 8.721 1.00 74.15 ? 89 LEU A CA 1 ATOM 690 C C . LEU A 1 89 ? 37.114 -9.674 9.551 1.00 74.08 ? 89 LEU A C 1 ATOM 691 O O . LEU A 1 89 ? 38.198 -9.125 9.772 1.00 71.70 ? 89 LEU A O 1 ATOM 692 C CB . LEU A 1 89 ? 38.189 -11.883 9.137 1.00 74.63 ? 89 LEU A CB 1 ATOM 693 C CG . LEU A 1 89 ? 38.346 -13.187 8.352 1.00 75.04 ? 89 LEU A CG 1 ATOM 694 C CD1 . LEU A 1 89 ? 39.463 -14.022 8.963 1.00 75.79 ? 89 LEU A CD1 1 ATOM 695 C CD2 . LEU A 1 89 ? 37.041 -13.971 8.307 1.00 75.36 ? 89 LEU A CD2 1 ATOM 696 N N . CYS A 1 90 ? 35.953 -9.219 10.022 1.00 75.19 ? 90 CYS A N 1 ATOM 697 C CA . CYS A 1 90 ? 35.873 -7.976 10.780 1.00 75.88 ? 90 CYS A CA 1 ATOM 698 C C . CYS A 1 90 ? 36.732 -8.037 12.054 1.00 73.94 ? 90 CYS A C 1 ATOM 699 O O . CYS A 1 90 ? 37.475 -7.100 12.343 1.00 74.21 ? 90 CYS A O 1 ATOM 700 C CB . CYS A 1 90 ? 34.412 -7.601 11.072 1.00 78.51 ? 90 CYS A CB 1 ATOM 701 S SG . CYS A 1 90 ? 33.380 -8.874 11.839 1.00 82.35 ? 90 CYS A SG 1 ATOM 702 N N . TYR A 1 91 ? 36.651 -9.143 12.789 1.00 71.37 ? 91 TYR A N 1 ATOM 703 C CA . TYR A 1 91 ? 37.605 -9.422 13.856 1.00 72.11 ? 91 TYR A CA 1 ATOM 704 C C . TYR A 1 91 ? 38.761 -10.171 13.216 1.00 71.02 ? 91 TYR A C 1 ATOM 705 O O . TYR A 1 91 ? 38.542 -11.208 12.601 1.00 71.52 ? 91 TYR A O 1 ATOM 706 C CB . TYR A 1 91 ? 36.961 -10.278 14.945 1.00 74.83 ? 91 TYR A CB 1 ATOM 707 C CG . TYR A 1 91 ? 37.676 -10.256 16.287 1.00 76.54 ? 91 TYR A CG 1 ATOM 708 C CD1 . TYR A 1 91 ? 38.898 -10.901 16.462 1.00 76.41 ? 91 TYR A CD1 1 ATOM 709 C CD2 . TYR A 1 91 ? 37.120 -9.601 17.387 1.00 77.51 ? 91 TYR A CD2 1 ATOM 710 C CE1 . TYR A 1 91 ? 39.546 -10.886 17.687 1.00 77.05 ? 91 TYR A CE1 1 ATOM 711 C CE2 . TYR A 1 91 ? 37.764 -9.585 18.615 1.00 77.69 ? 91 TYR A CE2 1 ATOM 712 C CZ . TYR A 1 91 ? 38.978 -10.227 18.758 1.00 76.71 ? 91 TYR A CZ 1 ATOM 713 O OH . TYR A 1 91 ? 39.622 -10.214 19.974 1.00 77.88 ? 91 TYR A OH 1 ATOM 714 N N . PRO A 1 92 ? 39.998 -9.666 13.360 1.00 71.61 ? 92 PRO A N 1 ATOM 715 C CA . PRO A 1 92 ? 41.122 -10.268 12.635 1.00 72.09 ? 92 PRO A CA 1 ATOM 716 C C . PRO A 1 92 ? 41.385 -11.726 13.005 1.00 74.25 ? 92 PRO A C 1 ATOM 717 O O . PRO A 1 92 ? 40.971 -12.186 14.075 1.00 75.18 ? 92 PRO A O 1 ATOM 718 C CB . PRO A 1 92 ? 42.314 -9.396 13.045 1.00 72.73 ? 92 PRO A CB 1 ATOM 719 C CG . PRO A 1 92 ? 41.937 -8.860 14.382 1.00 73.99 ? 92 PRO A CG 1 ATOM 720 C CD . PRO A 1 92 ? 40.453 -8.620 14.293 1.00 73.64 ? 92 PRO A CD 1 ATOM 721 N N . GLY A 1 93 ? 42.076 -12.436 12.116 1.00 75.93 ? 93 GLY A N 1 ATOM 722 C CA . GLY A 1 93 ? 42.362 -13.854 12.313 1.00 77.58 ? 93 GLY A CA 1 ATOM 723 C C . GLY A 1 93 ? 42.643 -14.604 11.022 1.00 77.02 ? 93 GLY A C 1 ATOM 724 O O . GLY A 1 93 ? 43.080 -14.013 10.039 1.00 74.38 ? 93 GLY A O 1 ATOM 725 N N . ASP A 1 94 ? 42.398 -15.914 11.045 1.00 78.70 ? 94 ASP A N 1 ATOM 726 C CA . ASP A 1 94 ? 42.607 -16.789 9.891 1.00 79.98 ? 94 ASP A CA 1 ATOM 727 C C . ASP A 1 94 ? 41.358 -17.610 9.611 1.00 77.93 ? 94 ASP A C 1 ATOM 728 O O . ASP A 1 94 ? 40.485 -17.760 10.474 1.00 78.77 ? 94 ASP A O 1 ATOM 729 C CB . ASP A 1 94 ? 43.774 -17.750 10.141 1.00 84.42 ? 94 ASP A CB 1 ATOM 730 C CG . ASP A 1 94 ? 45.111 -17.035 10.257 1.00 89.42 ? 94 ASP A CG 1 ATOM 731 O OD1 . ASP A 1 94 ? 45.607 -16.536 9.224 1.00 91.73 ? 94 ASP A OD1 1 ATOM 732 O OD2 . ASP A 1 94 ? 45.672 -16.984 11.379 1.00 94.96 ? 94 ASP A OD2 1 ATOM 733 N N . PHE A 1 95 ? 41.282 -18.130 8.391 1.00 74.25 ? 95 PHE A N 1 ATOM 734 C CA . PHE A 1 95 ? 40.250 -19.078 8.005 1.00 71.23 ? 95 PHE A CA 1 ATOM 735 C C . PHE A 1 95 ? 40.972 -20.322 7.506 1.00 70.51 ? 95 PHE A C 1 ATOM 736 O O . PHE A 1 95 ? 41.581 -20.313 6.441 1.00 69.35 ? 95 PHE A O 1 ATOM 737 C CB . PHE A 1 95 ? 39.365 -18.473 6.923 1.00 69.53 ? 95 PHE A CB 1 ATOM 738 C CG . PHE A 1 95 ? 38.048 -19.173 6.745 1.00 69.90 ? 95 PHE A CG 1 ATOM 739 C CD1 . PHE A 1 95 ? 37.993 -20.486 6.309 1.00 71.47 ? 95 PHE A CD1 1 ATOM 740 C CD2 . PHE A 1 95 ? 36.860 -18.509 6.992 1.00 69.78 ? 95 PHE A CD2 1 ATOM 741 C CE1 . PHE A 1 95 ? 36.776 -21.124 6.133 1.00 72.64 ? 95 PHE A CE1 1 ATOM 742 C CE2 . PHE A 1 95 ? 35.642 -19.141 6.820 1.00 70.76 ? 95 PHE A CE2 1 ATOM 743 C CZ . PHE A 1 95 ? 35.599 -20.452 6.393 1.00 71.81 ? 95 PHE A CZ 1 ATOM 744 N N . ASN A 1 96 ? 40.918 -21.384 8.295 1.00 71.51 ? 96 ASN A N 1 ATOM 745 C CA . ASN A 1 96 ? 41.661 -22.601 8.001 1.00 72.01 ? 96 ASN A CA 1 ATOM 746 C C . ASN A 1 96 ? 41.141 -23.304 6.745 1.00 71.10 ? 96 ASN A C 1 ATOM 747 O O . ASN A 1 96 ? 39.928 -23.436 6.556 1.00 68.80 ? 96 ASN A O 1 ATOM 748 C CB . ASN A 1 96 ? 41.594 -23.548 9.202 1.00 74.67 ? 96 ASN A CB 1 ATOM 749 C CG . ASN A 1 96 ? 42.689 -24.586 9.183 1.00 77.75 ? 96 ASN A CG 1 ATOM 750 O OD1 . ASN A 1 96 ? 43.874 -24.257 9.280 1.00 78.65 ? 96 ASN A OD1 1 ATOM 751 N ND2 . ASN A 1 96 ? 42.302 -25.851 9.061 1.00 80.17 ? 96 ASN A ND2 1 ATOM 752 N N . ASP A 1 97 ? 42.071 -23.753 5.898 1.00 72.11 ? 97 ASP A N 1 ATOM 753 C CA . ASP A 1 97 ? 41.762 -24.405 4.613 1.00 71.04 ? 97 ASP A CA 1 ATOM 754 C C . ASP A 1 97 ? 40.764 -23.597 3.779 1.00 67.99 ? 97 ASP A C 1 ATOM 755 O O . ASP A 1 97 ? 39.823 -24.148 3.201 1.00 67.22 ? 97 ASP A O 1 ATOM 756 C CB . ASP A 1 97 ? 41.251 -25.839 4.838 1.00 75.03 ? 97 ASP A CB 1 ATOM 757 C CG . ASP A 1 97 ? 42.374 -26.831 5.120 1.00 78.75 ? 97 ASP A CG 1 ATOM 758 O OD1 . ASP A 1 97 ? 43.490 -26.645 4.589 1.00 81.14 ? 97 ASP A OD1 1 ATOM 759 O OD2 . ASP A 1 97 ? 42.132 -27.811 5.859 1.00 81.92 ? 97 ASP A OD2 1 ATOM 760 N N . TYR A 1 98 ? 40.984 -22.289 3.719 1.00 65.62 ? 98 TYR A N 1 ATOM 761 C CA . TYR A 1 98 ? 40.054 -21.370 3.060 1.00 65.44 ? 98 TYR A CA 1 ATOM 762 C C . TYR A 1 98 ? 39.930 -21.679 1.566 1.00 65.80 ? 98 TYR A C 1 ATOM 763 O O . TYR A 1 98 ? 38.831 -21.673 1.004 1.00 64.01 ? 98 TYR A O 1 ATOM 764 C CB . TYR A 1 98 ? 40.522 -19.925 3.285 1.00 63.46 ? 98 TYR A CB 1 ATOM 765 C CG . TYR A 1 98 ? 39.590 -18.836 2.788 1.00 62.65 ? 98 TYR A CG 1 ATOM 766 C CD1 . TYR A 1 98 ? 38.224 -18.882 3.041 1.00 62.67 ? 98 TYR A CD1 1 ATOM 767 C CD2 . TYR A 1 98 ? 40.092 -17.731 2.089 1.00 62.15 ? 98 TYR A CD2 1 ATOM 768 C CE1 . TYR A 1 98 ? 37.379 -17.875 2.591 1.00 63.02 ? 98 TYR A CE1 1 ATOM 769 C CE2 . TYR A 1 98 ? 39.261 -16.722 1.638 1.00 60.71 ? 98 TYR A CE2 1 ATOM 770 C CZ . TYR A 1 98 ? 37.907 -16.793 1.892 1.00 62.97 ? 98 TYR A CZ 1 ATOM 771 O OH . TYR A 1 98 ? 37.076 -15.785 1.445 1.00 65.51 ? 98 TYR A OH 1 ATOM 772 N N . GLU A 1 99 ? 41.063 -21.980 0.939 1.00 67.41 ? 99 GLU A N 1 ATOM 773 C CA . GLU A 1 99 ? 41.107 -22.210 -0.503 1.00 67.45 ? 99 GLU A CA 1 ATOM 774 C C . GLU A 1 99 ? 40.485 -23.549 -0.885 1.00 66.93 ? 99 GLU A C 1 ATOM 775 O O . GLU A 1 99 ? 39.800 -23.646 -1.901 1.00 65.42 ? 99 GLU A O 1 ATOM 776 C CB . GLU A 1 99 ? 42.539 -22.115 -1.020 1.00 69.27 ? 99 GLU A CB 1 ATOM 777 C CG . GLU A 1 99 ? 43.146 -20.713 -0.915 1.00 71.35 ? 99 GLU A CG 1 ATOM 778 C CD . GLU A 1 99 ? 43.655 -20.353 0.478 1.00 74.37 ? 99 GLU A CD 1 ATOM 779 O OE1 . GLU A 1 99 ? 43.743 -21.244 1.361 1.00 76.68 ? 99 GLU A OE1 1 ATOM 780 O OE2 . GLU A 1 99 ? 43.968 -19.164 0.688 1.00 74.86 ? 99 GLU A OE2 1 ATOM 781 N N . GLU A 1 100 ? 40.707 -24.575 -0.066 1.00 66.81 ? 100 GLU A N 1 ATOM 782 C CA . GLU A 1 100 ? 40.059 -25.863 -0.291 1.00 66.97 ? 100 GLU A CA 1 ATOM 783 C C . GLU A 1 100 ? 38.545 -25.718 -0.197 1.00 67.15 ? 100 GLU A C 1 ATOM 784 O O . GLU A 1 100 ? 37.811 -26.422 -0.889 1.00 68.64 ? 100 GLU A O 1 ATOM 785 C CB . GLU A 1 100 ? 40.564 -26.929 0.687 1.00 67.79 ? 100 GLU A CB 1 ATOM 786 C CG . GLU A 1 100 ? 41.917 -27.524 0.317 1.00 68.48 ? 100 GLU A CG 1 ATOM 787 C CD . GLU A 1 100 ? 41.883 -28.356 -0.958 1.00 68.56 ? 100 GLU A CD 1 ATOM 788 O OE1 . GLU A 1 100 ? 41.069 -29.300 -1.049 1.00 70.18 ? 100 GLU A OE1 1 ATOM 789 O OE2 . GLU A 1 100 ? 42.681 -28.072 -1.874 1.00 66.57 ? 100 GLU A OE2 1 ATOM 790 N N . LEU A 1 101 ? 38.077 -24.799 0.642 1.00 66.75 ? 101 LEU A N 1 ATOM 791 C CA . LEU A 1 101 ? 36.644 -24.562 0.769 1.00 67.45 ? 101 LEU A CA 1 ATOM 792 C C . LEU A 1 101 ? 36.122 -23.796 -0.439 1.00 65.84 ? 101 LEU A C 1 ATOM 793 O O . LEU A 1 101 ? 35.095 -24.163 -1.012 1.00 64.75 ? 101 LEU A O 1 ATOM 794 C CB . LEU A 1 101 ? 36.314 -23.803 2.056 1.00 67.38 ? 101 LEU A CB 1 ATOM 795 C CG . LEU A 1 101 ? 34.833 -23.460 2.242 1.00 67.46 ? 101 LEU A CG 1 ATOM 796 C CD1 . LEU A 1 101 ? 33.955 -24.706 2.228 1.00 68.12 ? 101 LEU A CD1 1 ATOM 797 C CD2 . LEU A 1 101 ? 34.665 -22.683 3.534 1.00 69.50 ? 101 LEU A CD2 1 ATOM 798 N N . LYS A 1 102 ? 36.819 -22.729 -0.814 1.00 65.31 ? 102 LYS A N 1 ATOM 799 C CA . LYS A 1 102 ? 36.485 -22.002 -2.041 1.00 65.59 ? 102 LYS A CA 1 ATOM 800 C C . LYS A 1 102 ? 36.385 -22.941 -3.244 1.00 65.09 ? 102 LYS A C 1 ATOM 801 O O . LYS A 1 102 ? 35.494 -22.801 -4.079 1.00 64.49 ? 102 LYS A O 1 ATOM 802 C CB . LYS A 1 102 ? 37.518 -20.920 -2.329 1.00 65.57 ? 102 LYS A CB 1 ATOM 803 C CG . LYS A 1 102 ? 37.256 -19.603 -1.626 1.00 68.43 ? 102 LYS A CG 1 ATOM 804 C CD . LYS A 1 102 ? 38.390 -18.618 -1.886 1.00 69.83 ? 102 LYS A CD 1 ATOM 805 C CE . LYS A 1 102 ? 37.888 -17.187 -1.994 1.00 72.06 ? 102 LYS A CE 1 ATOM 806 N NZ . LYS A 1 102 ? 38.938 -16.268 -2.516 1.00 73.46 ? 102 LYS A NZ 1 ATOM 807 N N . HIS A 1 103 ? 37.298 -23.902 -3.324 1.00 65.37 ? 103 HIS A N 1 ATOM 808 C CA . HIS A 1 103 ? 37.286 -24.859 -4.414 1.00 66.00 ? 103 HIS A CA 1 ATOM 809 C C . HIS A 1 103 ? 36.027 -25.716 -4.371 1.00 69.36 ? 103 HIS A C 1 ATOM 810 O O . HIS A 1 103 ? 35.499 -26.120 -5.406 1.00 70.05 ? 103 HIS A O 1 ATOM 811 C CB . HIS A 1 103 ? 38.519 -25.750 -4.361 1.00 66.19 ? 103 HIS A CB 1 ATOM 812 C CG . HIS A 1 103 ? 38.587 -26.733 -5.483 1.00 65.94 ? 103 HIS A CG 1 ATOM 813 N ND1 . HIS A 1 103 ? 39.073 -26.405 -6.729 1.00 64.90 ? 103 HIS A ND1 1 ATOM 814 C CD2 . HIS A 1 103 ? 38.194 -28.025 -5.558 1.00 67.03 ? 103 HIS A CD2 1 ATOM 815 C CE1 . HIS A 1 103 ? 38.994 -27.458 -7.521 1.00 65.32 ? 103 HIS A CE1 1 ATOM 816 N NE2 . HIS A 1 103 ? 38.464 -28.454 -6.834 1.00 67.24 ? 103 HIS A NE2 1 ATOM 817 N N . LEU A 1 104 ? 35.557 -25.990 -3.164 1.00 72.33 ? 104 LEU A N 1 ATOM 818 C CA . LEU A 1 104 ? 34.328 -26.748 -2.959 1.00 76.34 ? 104 LEU A CA 1 ATOM 819 C C . LEU A 1 104 ? 33.103 -26.009 -3.518 1.00 77.08 ? 104 LEU A C 1 ATOM 820 O O . LEU A 1 104 ? 32.169 -26.640 -4.012 1.00 78.80 ? 104 LEU A O 1 ATOM 821 C CB . LEU A 1 104 ? 34.138 -27.013 -1.461 1.00 78.33 ? 104 LEU A CB 1 ATOM 822 C CG . LEU A 1 104 ? 33.519 -28.339 -1.046 1.00 80.28 ? 104 LEU A CG 1 ATOM 823 C CD1 . LEU A 1 104 ? 34.378 -29.513 -1.495 1.00 80.91 ? 104 LEU A CD1 1 ATOM 824 C CD2 . LEU A 1 104 ? 33.353 -28.332 0.464 1.00 80.78 ? 104 LEU A CD2 1 ATOM 825 N N . LEU A 1 105 ? 33.123 -24.677 -3.432 1.00 77.14 ? 105 LEU A N 1 ATOM 826 C CA . LEU A 1 105 ? 32.027 -23.820 -3.918 1.00 76.50 ? 105 LEU A CA 1 ATOM 827 C C . LEU A 1 105 ? 31.884 -23.794 -5.426 1.00 77.33 ? 105 LEU A C 1 ATOM 828 O O . LEU A 1 105 ? 30.831 -23.417 -5.944 1.00 79.60 ? 105 LEU A O 1 ATOM 829 C CB . LEU A 1 105 ? 32.225 -22.374 -3.468 1.00 74.65 ? 105 LEU A CB 1 ATOM 830 C CG . LEU A 1 105 ? 31.857 -22.012 -2.043 1.00 74.31 ? 105 LEU A CG 1 ATOM 831 C CD1 . LEU A 1 105 ? 32.050 -20.518 -1.856 1.00 73.23 ? 105 LEU A CD1 1 ATOM 832 C CD2 . LEU A 1 105 ? 30.424 -22.413 -1.749 1.00 76.41 ? 105 LEU A CD2 1 ATOM 833 N N . SER A 1 106 ? 32.950 -24.153 -6.129 1.00 83.00 ? 106 SER A N 1 ATOM 834 C CA A SER A 1 106 ? 32.913 -24.229 -7.587 0.50 84.80 ? 106 SER A CA 1 ATOM 835 C CA B SER A 1 106 ? 32.917 -24.227 -7.580 0.50 84.42 ? 106 SER A CA 1 ATOM 836 C C . SER A 1 106 ? 32.075 -25.423 -8.034 1.00 86.62 ? 106 SER A C 1 ATOM 837 O O . SER A 1 106 ? 31.702 -25.520 -9.203 1.00 90.01 ? 106 SER A O 1 ATOM 838 C CB A SER A 1 106 ? 34.329 -24.312 -8.176 0.50 84.77 ? 106 SER A CB 1 ATOM 839 C CB B SER A 1 106 ? 34.344 -24.318 -8.119 0.50 84.00 ? 106 SER A CB 1 ATOM 840 O OG A SER A 1 106 ? 34.909 -25.594 -7.995 0.50 84.91 ? 106 SER A OG 1 ATOM 841 O OG B SER A 1 106 ? 35.177 -23.373 -7.459 0.50 81.29 ? 106 SER A OG 1 ATOM 842 N N . ARG A 1 107 ? 31.786 -26.329 -7.100 1.00 88.70 ? 107 ARG A N 1 ATOM 843 C CA . ARG A 1 107 ? 30.900 -27.465 -7.348 1.00 93.22 ? 107 ARG A CA 1 ATOM 844 C C . ARG A 1 107 ? 29.519 -27.253 -6.709 1.00 89.81 ? 107 ARG A C 1 ATOM 845 O O . ARG A 1 107 ? 28.713 -28.182 -6.677 1.00 90.32 ? 107 ARG A O 1 ATOM 846 C CB . ARG A 1 107 ? 31.517 -28.765 -6.804 1.00 99.28 ? 107 ARG A CB 1 ATOM 847 C CG . ARG A 1 107 ? 32.545 -29.433 -7.708 1.00 105.16 ? 107 ARG A CG 1 ATOM 848 C CD . ARG A 1 107 ? 33.893 -28.720 -7.686 1.00 110.17 ? 107 ARG A CD 1 ATOM 849 N NE . ARG A 1 107 ? 34.995 -29.577 -8.149 1.00 116.64 ? 107 ARG A NE 1 ATOM 850 C CZ . ARG A 1 107 ? 35.695 -30.422 -7.382 1.00 118.78 ? 107 ARG A CZ 1 ATOM 851 N NH1 . ARG A 1 107 ? 35.433 -30.557 -6.077 1.00 119.32 ? 107 ARG A NH1 1 ATOM 852 N NH2 . ARG A 1 107 ? 36.674 -31.144 -7.925 1.00 116.71 ? 107 ARG A NH2 1 ATOM 853 N N . ILE A 1 108 ? 29.243 -26.048 -6.206 1.00 84.96 ? 108 ILE A N 1 ATOM 854 C CA . ILE A 1 108 ? 27.979 -25.772 -5.505 1.00 84.19 ? 108 ILE A CA 1 ATOM 855 C C . ILE A 1 108 ? 27.205 -24.609 -6.132 1.00 81.62 ? 108 ILE A C 1 ATOM 856 O O . ILE A 1 108 ? 27.768 -23.544 -6.385 1.00 80.23 ? 108 ILE A O 1 ATOM 857 C CB . ILE A 1 108 ? 28.213 -25.471 -4.003 1.00 83.74 ? 108 ILE A CB 1 ATOM 858 C CG1 . ILE A 1 108 ? 28.822 -26.690 -3.302 1.00 84.24 ? 108 ILE A CG1 1 ATOM 859 C CG2 . ILE A 1 108 ? 26.903 -25.101 -3.314 1.00 84.25 ? 108 ILE A CG2 1 ATOM 860 C CD1 . ILE A 1 108 ? 29.343 -26.408 -1.908 1.00 82.86 ? 108 ILE A CD1 1 ATOM 861 N N . ASN A 1 109 ? 25.908 -24.822 -6.356 1.00 80.78 ? 109 ASN A N 1 ATOM 862 C CA . ASN A 1 109 ? 25.019 -23.794 -6.896 1.00 81.32 ? 109 ASN A CA 1 ATOM 863 C C . ASN A 1 109 ? 24.019 -23.231 -5.887 1.00 81.87 ? 109 ASN A C 1 ATOM 864 O O . ASN A 1 109 ? 23.461 -22.155 -6.127 1.00 80.92 ? 109 ASN A O 1 ATOM 865 C CB . ASN A 1 109 ? 24.242 -24.342 -8.093 1.00 83.98 ? 109 ASN A CB 1 ATOM 866 C CG . ASN A 1 109 ? 25.126 -24.583 -9.297 1.00 84.51 ? 109 ASN A CG 1 ATOM 867 O OD1 . ASN A 1 109 ? 25.761 -23.660 -9.807 1.00 83.96 ? 109 ASN A OD1 1 ATOM 868 N ND2 . ASN A 1 109 ? 25.171 -25.826 -9.763 1.00 86.59 ? 109 ASN A ND2 1 ATOM 869 N N . HIS A 1 110 ? 23.773 -23.943 -4.782 1.00 82.01 ? 110 HIS A N 1 ATOM 870 C CA . HIS A 1 110 ? 22.771 -23.499 -3.805 1.00 82.90 ? 110 HIS A CA 1 ATOM 871 C C . HIS A 1 110 ? 22.985 -24.005 -2.378 1.00 82.92 ? 110 HIS A C 1 ATOM 872 O O . HIS A 1 110 ? 23.199 -25.200 -2.150 1.00 82.51 ? 110 HIS A O 1 ATOM 873 C CB . HIS A 1 110 ? 21.368 -23.894 -4.276 1.00 85.65 ? 110 HIS A CB 1 ATOM 874 C CG . HIS A 1 110 ? 20.265 -23.188 -3.549 1.00 87.11 ? 110 HIS A CG 1 ATOM 875 N ND1 . HIS A 1 110 ? 18.993 -23.708 -3.437 1.00 89.73 ? 110 HIS A ND1 1 ATOM 876 C CD2 . HIS A 1 110 ? 20.246 -22.003 -2.893 1.00 86.26 ? 110 HIS A CD2 1 ATOM 877 C CE1 . HIS A 1 110 ? 18.238 -22.872 -2.749 1.00 90.35 ? 110 HIS A CE1 1 ATOM 878 N NE2 . HIS A 1 110 ? 18.975 -21.830 -2.405 1.00 87.89 ? 110 HIS A NE2 1 ATOM 879 N N . PHE A 1 111 ? 22.912 -23.069 -1.430 1.00 83.12 ? 111 PHE A N 1 ATOM 880 C CA . PHE A 1 111 ? 22.942 -23.371 -0.001 1.00 84.27 ? 111 PHE A CA 1 ATOM 881 C C . PHE A 1 111 ? 21.584 -23.105 0.621 1.00 86.46 ? 111 PHE A C 1 ATOM 882 O O . PHE A 1 111 ? 20.822 -22.280 0.125 1.00 88.07 ? 111 PHE A O 1 ATOM 883 C CB . PHE A 1 111 ? 23.945 -22.479 0.738 1.00 82.13 ? 111 PHE A CB 1 ATOM 884 C CG . PHE A 1 111 ? 25.382 -22.921 0.633 1.00 80.30 ? 111 PHE A CG 1 ATOM 885 C CD1 . PHE A 1 111 ? 25.754 -24.248 0.828 1.00 80.59 ? 111 PHE A CD1 1 ATOM 886 C CD2 . PHE A 1 111 ? 26.378 -21.985 0.398 1.00 77.72 ? 111 PHE A CD2 1 ATOM 887 C CE1 . PHE A 1 111 ? 27.082 -24.629 0.753 1.00 78.25 ? 111 PHE A CE1 1 ATOM 888 C CE2 . PHE A 1 111 ? 27.703 -22.364 0.325 1.00 76.06 ? 111 PHE A CE2 1 ATOM 889 C CZ . PHE A 1 111 ? 28.057 -23.688 0.505 1.00 76.01 ? 111 PHE A CZ 1 ATOM 890 N N . GLU A 1 112 ? 21.305 -23.790 1.725 1.00 89.01 ? 112 GLU A N 1 ATOM 891 C CA . GLU A 1 112 ? 20.144 -23.492 2.569 1.00 91.75 ? 112 GLU A CA 1 ATOM 892 C C . GLU A 1 112 ? 20.607 -23.362 4.010 1.00 87.31 ? 112 GLU A C 1 ATOM 893 O O . GLU A 1 112 ? 20.993 -24.353 4.631 1.00 84.20 ? 112 GLU A O 1 ATOM 894 C CB . GLU A 1 112 ? 19.093 -24.596 2.462 1.00 97.48 ? 112 GLU A CB 1 ATOM 895 C CG . GLU A 1 112 ? 18.168 -24.459 1.262 1.00 103.53 ? 112 GLU A CG 1 ATOM 896 C CD . GLU A 1 112 ? 16.951 -23.588 1.526 1.00 108.73 ? 112 GLU A CD 1 ATOM 897 O OE1 . GLU A 1 112 ? 16.512 -23.504 2.698 1.00 110.73 ? 112 GLU A OE1 1 ATOM 898 O OE2 . GLU A 1 112 ? 16.425 -23.005 0.547 1.00 111.62 ? 112 GLU A OE2 1 ATOM 899 N N . LYS A 1 113 ? 20.573 -22.142 4.536 1.00 85.34 ? 113 LYS A N 1 ATOM 900 C CA . LYS A 1 113 ? 20.995 -21.894 5.912 1.00 86.49 ? 113 LYS A CA 1 ATOM 901 C C . LYS A 1 113 ? 20.000 -22.483 6.905 1.00 88.97 ? 113 LYS A C 1 ATOM 902 O O . LYS A 1 113 ? 18.811 -22.178 6.837 1.00 91.23 ? 113 LYS A O 1 ATOM 903 C CB . LYS A 1 113 ? 21.138 -20.394 6.158 1.00 86.00 ? 113 LYS A CB 1 ATOM 904 C CG . LYS A 1 113 ? 21.623 -20.046 7.554 1.00 86.75 ? 113 LYS A CG 1 ATOM 905 C CD . LYS A 1 113 ? 22.694 -18.965 7.527 1.00 86.59 ? 113 LYS A CD 1 ATOM 906 C CE . LYS A 1 113 ? 22.139 -17.611 7.125 1.00 87.10 ? 113 LYS A CE 1 ATOM 907 N NZ . LYS A 1 113 ? 23.221 -16.675 6.704 1.00 84.85 ? 113 LYS A NZ 1 ATOM 908 N N . ILE A 1 114 ? 20.480 -23.328 7.818 1.00 88.88 ? 114 ILE A N 1 ATOM 909 C CA . ILE A 1 114 ? 19.633 -23.842 8.897 1.00 91.67 ? 114 ILE A CA 1 ATOM 910 C C . ILE A 1 114 ? 20.298 -23.708 10.257 1.00 92.06 ? 114 ILE A C 1 ATOM 911 O O . ILE A 1 114 ? 21.525 -23.699 10.367 1.00 90.56 ? 114 ILE A O 1 ATOM 912 C CB . ILE A 1 114 ? 19.226 -25.315 8.691 1.00 93.47 ? 114 ILE A CB 1 ATOM 913 C CG1 . ILE A 1 114 ? 20.453 -26.230 8.644 1.00 92.66 ? 114 ILE A CG1 1 ATOM 914 C CG2 . ILE A 1 114 ? 18.389 -25.463 7.428 1.00 94.13 ? 114 ILE A CG2 1 ATOM 915 C CD1 . ILE A 1 114 ? 20.137 -27.659 9.027 1.00 94.92 ? 114 ILE A CD1 1 ATOM 916 N N . GLN A 1 115 ? 19.463 -23.618 11.288 1.00 94.52 ? 115 GLN A N 1 ATOM 917 C CA . GLN A 1 115 ? 19.929 -23.469 12.655 1.00 93.98 ? 115 GLN A CA 1 ATOM 918 C C . GLN A 1 115 ? 20.152 -24.839 13.269 1.00 94.45 ? 115 GLN A C 1 ATOM 919 O O . GLN A 1 115 ? 19.207 -25.609 13.415 1.00 95.92 ? 115 GLN A O 1 ATOM 920 C CB . GLN A 1 115 ? 18.894 -22.706 13.476 1.00 96.15 ? 115 GLN A CB 1 ATOM 921 C CG . GLN A 1 115 ? 19.364 -22.343 14.872 1.00 96.68 ? 115 GLN A CG 1 ATOM 922 C CD . GLN A 1 115 ? 18.260 -21.744 15.706 1.00 99.17 ? 115 GLN A CD 1 ATOM 923 O OE1 . GLN A 1 115 ? 18.258 -20.548 15.979 1.00 99.07 ? 115 GLN A OE1 1 ATOM 924 N NE2 . GLN A 1 115 ? 17.307 -22.574 16.107 1.00 102.30 ? 115 GLN A NE2 1 ATOM 925 N N . ILE A 1 116 ? 21.394 -25.139 13.637 1.00 92.87 ? 116 ILE A N 1 ATOM 926 C CA . ILE A 1 116 ? 21.703 -26.432 14.251 1.00 94.97 ? 116 ILE A CA 1 ATOM 927 C C . ILE A 1 116 ? 21.771 -26.351 15.778 1.00 98.39 ? 116 ILE A C 1 ATOM 928 O O . ILE A 1 116 ? 21.280 -27.251 16.460 1.00 103.10 ? 116 ILE A O 1 ATOM 929 C CB . ILE A 1 116 ? 22.980 -27.081 13.669 1.00 91.43 ? 116 ILE A CB 1 ATOM 930 C CG1 . ILE A 1 116 ? 24.166 -26.119 13.696 1.00 88.66 ? 116 ILE A CG1 1 ATOM 931 C CG2 . ILE A 1 116 ? 22.729 -27.544 12.244 1.00 90.35 ? 116 ILE A CG2 1 ATOM 932 C CD1 . ILE A 1 116 ? 25.485 -26.798 13.417 1.00 87.52 ? 116 ILE A CD1 1 ATOM 933 N N . ILE A 1 117 ? 22.351 -25.273 16.310 1.00 98.89 ? 117 ILE A N 1 ATOM 934 C CA . ILE A 1 117 ? 22.426 -25.055 17.763 1.00 101.01 ? 117 ILE A CA 1 ATOM 935 C C . ILE A 1 117 ? 21.862 -23.673 18.116 1.00 101.36 ? 117 ILE A C 1 ATOM 936 O O . ILE A 1 117 ? 22.540 -22.663 17.913 1.00 99.65 ? 117 ILE A O 1 ATOM 937 C CB . ILE A 1 117 ? 23.875 -25.171 18.282 1.00 100.78 ? 117 ILE A CB 1 ATOM 938 C CG1 . ILE A 1 117 ? 24.486 -26.505 17.840 1.00 100.75 ? 117 ILE A CG1 1 ATOM 939 C CG2 . ILE A 1 117 ? 23.913 -25.045 19.803 1.00 103.62 ? 117 ILE A CG2 1 ATOM 940 C CD1 . ILE A 1 117 ? 25.920 -26.710 18.280 1.00 100.22 ? 117 ILE A CD1 1 ATOM 941 N N . PRO A 1 118 ? 20.626 -23.622 18.658 1.00 104.65 ? 118 PRO A N 1 ATOM 942 C CA . PRO A 1 118 ? 20.005 -22.320 18.912 1.00 105.72 ? 118 PRO A CA 1 ATOM 943 C C . PRO A 1 118 ? 20.771 -21.477 19.928 1.00 106.41 ? 118 PRO A C 1 ATOM 944 O O . PRO A 1 118 ? 21.400 -22.015 20.839 1.00 107.09 ? 118 PRO A O 1 ATOM 945 C CB . PRO A 1 118 ? 18.613 -22.681 19.457 1.00 108.96 ? 118 PRO A CB 1 ATOM 946 C CG . PRO A 1 118 ? 18.407 -24.121 19.139 1.00 109.31 ? 118 PRO A CG 1 ATOM 947 C CD . PRO A 1 118 ? 19.771 -24.730 19.120 1.00 107.60 ? 118 PRO A CD 1 ATOM 948 N N . LYS A 1 119 ? 20.709 -20.163 19.758 1.00 107.04 ? 119 LYS A N 1 ATOM 949 C CA . LYS A 1 119 ? 21.400 -19.230 20.640 1.00 108.39 ? 119 LYS A CA 1 ATOM 950 C C . LYS A 1 119 ? 20.792 -19.251 22.043 1.00 113.16 ? 119 LYS A C 1 ATOM 951 O O . LYS A 1 119 ? 21.497 -19.102 23.047 1.00 114.97 ? 119 LYS A O 1 ATOM 952 C CB . LYS A 1 119 ? 21.319 -17.823 20.054 1.00 108.15 ? 119 LYS A CB 1 ATOM 953 C CG . LYS A 1 119 ? 22.307 -16.842 20.645 1.00 108.83 ? 119 LYS A CG 1 ATOM 954 C CD . LYS A 1 119 ? 22.318 -15.557 19.839 1.00 109.29 ? 119 LYS A CD 1 ATOM 955 C CE . LYS A 1 119 ? 23.317 -14.566 20.404 1.00 110.53 ? 119 LYS A CE 1 ATOM 956 N NZ . LYS A 1 119 ? 23.501 -13.396 19.503 1.00 110.61 ? 119 LYS A NZ 1 ATOM 957 N N . SER A 1 120 ? 19.477 -19.452 22.097 1.00 115.55 ? 120 SER A N 1 ATOM 958 C CA . SER A 1 120 ? 18.737 -19.508 23.352 1.00 116.98 ? 120 SER A CA 1 ATOM 959 C C . SER A 1 120 ? 18.981 -20.792 24.147 1.00 117.28 ? 120 SER A C 1 ATOM 960 O O . SER A 1 120 ? 18.573 -20.881 25.301 1.00 122.28 ? 120 SER A O 1 ATOM 961 C CB . SER A 1 120 ? 17.239 -19.372 23.073 1.00 119.42 ? 120 SER A CB 1 ATOM 962 O OG . SER A 1 120 ? 16.769 -20.458 22.289 1.00 119.56 ? 120 SER A OG 1 ATOM 963 N N . SER A 1 121 ? 19.633 -21.782 23.542 1.00 113.85 ? 121 SER A N 1 ATOM 964 C CA . SER A 1 121 ? 19.857 -23.066 24.205 1.00 114.14 ? 121 SER A CA 1 ATOM 965 C C . SER A 1 121 ? 21.120 -23.108 25.079 1.00 113.02 ? 121 SER A C 1 ATOM 966 O O . SER A 1 121 ? 21.414 -24.143 25.678 1.00 113.35 ? 121 SER A O 1 ATOM 967 C CB . SER A 1 121 ? 19.920 -24.184 23.165 1.00 112.47 ? 121 SER A CB 1 ATOM 968 O OG . SER A 1 121 ? 21.070 -24.048 22.356 1.00 108.61 ? 121 SER A OG 1 ATOM 969 N N . TRP A 1 122 ? 21.867 -22.005 25.148 1.00 110.40 ? 122 TRP A N 1 ATOM 970 C CA . TRP A 1 122 ? 23.078 -21.950 25.972 1.00 108.80 ? 122 TRP A CA 1 ATOM 971 C C . TRP A 1 122 ? 22.740 -21.458 27.376 1.00 111.65 ? 122 TRP A C 1 ATOM 972 O O . TRP A 1 122 ? 22.946 -20.290 27.704 1.00 112.03 ? 122 TRP A O 1 ATOM 973 C CB . TRP A 1 122 ? 24.130 -21.050 25.328 1.00 104.76 ? 122 TRP A CB 1 ATOM 974 C CG . TRP A 1 122 ? 24.670 -21.589 24.044 1.00 102.00 ? 122 TRP A CG 1 ATOM 975 C CD1 . TRP A 1 122 ? 24.386 -21.145 22.787 1.00 99.58 ? 122 TRP A CD1 1 ATOM 976 C CD2 . TRP A 1 122 ? 25.594 -22.674 23.886 1.00 100.69 ? 122 TRP A CD2 1 ATOM 977 N NE1 . TRP A 1 122 ? 25.075 -21.882 21.856 1.00 97.71 ? 122 TRP A NE1 1 ATOM 978 C CE2 . TRP A 1 122 ? 25.825 -22.827 22.503 1.00 97.78 ? 122 TRP A CE2 1 ATOM 979 C CE3 . TRP A 1 122 ? 26.249 -23.529 24.779 1.00 101.94 ? 122 TRP A CE3 1 ATOM 980 C CZ2 . TRP A 1 122 ? 26.684 -23.803 21.988 1.00 96.12 ? 122 TRP A CZ2 1 ATOM 981 C CZ3 . TRP A 1 122 ? 27.104 -24.501 24.266 1.00 100.76 ? 122 TRP A CZ3 1 ATOM 982 C CH2 . TRP A 1 122 ? 27.313 -24.628 22.883 1.00 97.67 ? 122 TRP A CH2 1 ATOM 983 N N . SER A 1 123 ? 22.235 -22.370 28.200 1.00 113.84 ? 123 SER A N 1 ATOM 984 C CA . SER A 1 123 ? 21.670 -22.025 29.504 1.00 117.08 ? 123 SER A CA 1 ATOM 985 C C . SER A 1 123 ? 22.697 -21.902 30.634 1.00 118.36 ? 123 SER A C 1 ATOM 986 O O . SER A 1 123 ? 22.374 -21.374 31.694 1.00 121.02 ? 123 SER A O 1 ATOM 987 C CB . SER A 1 123 ? 20.615 -23.062 29.891 1.00 119.90 ? 123 SER A CB 1 ATOM 988 O OG . SER A 1 123 ? 21.137 -24.372 29.774 1.00 118.89 ? 123 SER A OG 1 ATOM 989 N N . SER A 1 124 ? 23.917 -22.391 30.414 1.00 117.08 ? 124 SER A N 1 ATOM 990 C CA . SER A 1 124 ? 24.982 -22.336 31.428 1.00 117.15 ? 124 SER A CA 1 ATOM 991 C C . SER A 1 124 ? 26.127 -21.374 31.072 1.00 115.15 ? 124 SER A C 1 ATOM 992 O O . SER A 1 124 ? 27.070 -21.216 31.846 1.00 115.56 ? 124 SER A O 1 ATOM 993 C CB . SER A 1 124 ? 25.557 -23.735 31.648 1.00 117.08 ? 124 SER A CB 1 ATOM 994 O OG . SER A 1 124 ? 24.525 -24.674 31.879 1.00 118.69 ? 124 SER A OG 1 ATOM 995 N N . HIS A 1 125 ? 26.050 -20.750 29.900 1.00 113.63 ? 125 HIS A N 1 ATOM 996 C CA . HIS A 1 125 ? 27.059 -19.790 29.459 1.00 111.62 ? 125 HIS A CA 1 ATOM 997 C C . HIS A 1 125 ? 26.366 -18.557 28.893 1.00 112.31 ? 125 HIS A C 1 ATOM 998 O O . HIS A 1 125 ? 25.218 -18.627 28.447 1.00 113.63 ? 125 HIS A O 1 ATOM 999 C CB . HIS A 1 125 ? 27.963 -20.400 28.380 1.00 107.32 ? 125 HIS A CB 1 ATOM 1000 C CG . HIS A 1 125 ? 28.645 -21.669 28.792 1.00 107.16 ? 125 HIS A CG 1 ATOM 1001 N ND1 . HIS A 1 125 ? 27.995 -22.884 28.836 1.00 108.60 ? 125 HIS A ND1 1 ATOM 1002 C CD2 . HIS A 1 125 ? 29.927 -21.916 29.152 1.00 106.42 ? 125 HIS A CD2 1 ATOM 1003 C CE1 . HIS A 1 125 ? 28.843 -23.822 29.218 1.00 109.10 ? 125 HIS A CE1 1 ATOM 1004 N NE2 . HIS A 1 125 ? 30.022 -23.261 29.416 1.00 108.02 ? 125 HIS A NE2 1 ATOM 1005 N N . GLU A 1 126 ? 27.073 -17.433 28.903 1.00 111.80 ? 126 GLU A N 1 ATOM 1006 C CA . GLU A 1 126 ? 26.543 -16.196 28.345 1.00 111.25 ? 126 GLU A CA 1 ATOM 1007 C C . GLU A 1 126 ? 26.753 -16.178 26.829 1.00 107.93 ? 126 GLU A C 1 ATOM 1008 O O . GLU A 1 126 ? 27.878 -16.344 26.347 1.00 106.36 ? 126 GLU A O 1 ATOM 1009 C CB . GLU A 1 126 ? 27.218 -14.995 29.005 1.00 112.23 ? 126 GLU A CB 1 ATOM 1010 C CG . GLU A 1 126 ? 26.593 -13.652 28.664 1.00 112.95 ? 126 GLU A CG 1 ATOM 1011 C CD . GLU A 1 126 ? 25.106 -13.590 28.975 1.00 116.60 ? 126 GLU A CD 1 ATOM 1012 O OE1 . GLU A 1 126 ? 24.735 -13.666 30.174 1.00 115.61 ? 126 GLU A OE1 1 ATOM 1013 O OE2 . GLU A 1 126 ? 24.316 -13.463 28.009 1.00 116.55 ? 126 GLU A OE2 1 ATOM 1014 N N . ALA A 1 127 ? 25.665 -15.976 26.086 1.00 106.63 ? 127 ALA A N 1 ATOM 1015 C CA . ALA A 1 127 ? 25.680 -16.091 24.625 1.00 102.49 ? 127 ALA A CA 1 ATOM 1016 C C . ALA A 1 127 ? 25.359 -14.794 23.873 1.00 101.20 ? 127 ALA A C 1 ATOM 1017 O O . ALA A 1 127 ? 25.586 -14.716 22.664 1.00 99.72 ? 127 ALA A O 1 ATOM 1018 C CB . ALA A 1 127 ? 24.720 -17.190 24.190 1.00 102.68 ? 127 ALA A CB 1 ATOM 1019 N N . SER A 1 128 ? 24.856 -13.779 24.576 1.00 102.18 ? 128 SER A N 1 ATOM 1020 C CA . SER A 1 128 ? 24.424 -12.533 23.936 1.00 101.30 ? 128 SER A CA 1 ATOM 1021 C C . SER A 1 128 ? 25.361 -11.345 24.174 1.00 99.54 ? 128 SER A C 1 ATOM 1022 O O . SER A 1 128 ? 25.019 -10.213 23.829 1.00 99.29 ? 128 SER A O 1 ATOM 1023 C CB . SER A 1 128 ? 23.010 -12.186 24.398 1.00 105.54 ? 128 SER A CB 1 ATOM 1024 O OG . SER A 1 128 ? 22.078 -13.081 23.822 1.00 107.83 ? 128 SER A OG 1 ATOM 1025 N N . LEU A 1 129 ? 26.537 -11.600 24.746 1.00 97.68 ? 129 LEU A N 1 ATOM 1026 C CA . LEU A 1 129 ? 27.523 -10.548 24.996 1.00 97.00 ? 129 LEU A CA 1 ATOM 1027 C C . LEU A 1 129 ? 28.812 -10.765 24.206 1.00 94.46 ? 129 LEU A C 1 ATOM 1028 O O . LEU A 1 129 ? 29.824 -10.123 24.482 1.00 94.72 ? 129 LEU A O 1 ATOM 1029 C CB . LEU A 1 129 ? 27.851 -10.471 26.489 1.00 100.23 ? 129 LEU A CB 1 ATOM 1030 C CG . LEU A 1 129 ? 26.681 -10.369 27.475 1.00 103.10 ? 129 LEU A CG 1 ATOM 1031 C CD1 . LEU A 1 129 ? 27.219 -10.210 28.890 1.00 104.61 ? 129 LEU A CD1 1 ATOM 1032 C CD2 . LEU A 1 129 ? 25.739 -9.225 27.123 1.00 104.14 ? 129 LEU A CD2 1 ATOM 1033 N N . GLY A 1 130 ? 28.774 -11.664 23.224 1.00 92.33 ? 130 GLY A N 1 ATOM 1034 C CA . GLY A 1 130 ? 29.926 -11.929 22.373 1.00 88.73 ? 130 GLY A CA 1 ATOM 1035 C C . GLY A 1 130 ? 29.987 -10.985 21.184 1.00 86.74 ? 130 GLY A C 1 ATOM 1036 O O . GLY A 1 130 ? 29.759 -11.400 20.042 1.00 84.72 ? 130 GLY A O 1 ATOM 1037 N N . VAL A 1 131 ? 30.311 -9.718 21.453 1.00 85.59 ? 131 VAL A N 1 ATOM 1038 C CA . VAL A 1 131 ? 30.338 -8.676 20.421 1.00 83.27 ? 131 VAL A CA 1 ATOM 1039 C C . VAL A 1 131 ? 31.576 -7.795 20.531 1.00 81.84 ? 131 VAL A C 1 ATOM 1040 O O . VAL A 1 131 ? 32.147 -7.648 21.605 1.00 83.92 ? 131 VAL A O 1 ATOM 1041 C CB . VAL A 1 131 ? 29.077 -7.785 20.480 1.00 85.45 ? 131 VAL A CB 1 ATOM 1042 C CG1 . VAL A 1 131 ? 27.849 -8.576 20.050 1.00 85.46 ? 131 VAL A CG1 1 ATOM 1043 C CG2 . VAL A 1 131 ? 28.874 -7.204 21.875 1.00 87.74 ? 131 VAL A CG2 1 ATOM 1044 N N . SER A 1 132 ? 31.969 -7.203 19.406 1.00 80.33 ? 132 SER A N 1 ATOM 1045 C CA . SER A 1 132 ? 33.191 -6.401 19.311 1.00 79.10 ? 132 SER A CA 1 ATOM 1046 C C . SER A 1 132 ? 32.960 -5.133 18.496 1.00 79.21 ? 132 SER A C 1 ATOM 1047 O O . SER A 1 132 ? 32.145 -5.123 17.563 1.00 79.43 ? 132 SER A O 1 ATOM 1048 C CB . SER A 1 132 ? 34.305 -7.226 18.652 1.00 76.50 ? 132 SER A CB 1 ATOM 1049 O OG . SER A 1 132 ? 35.438 -6.429 18.342 1.00 75.07 ? 132 SER A OG 1 ATOM 1050 N N . SER A 1 133 ? 33.693 -4.072 18.838 1.00 78.81 ? 133 SER A N 1 ATOM 1051 C CA . SER A 1 133 ? 33.687 -2.848 18.039 1.00 79.47 ? 133 SER A CA 1 ATOM 1052 C C . SER A 1 133 ? 34.366 -3.055 16.677 1.00 78.73 ? 133 SER A C 1 ATOM 1053 O O . SER A 1 133 ? 34.199 -2.239 15.773 1.00 78.19 ? 133 SER A O 1 ATOM 1054 C CB . SER A 1 133 ? 34.374 -1.720 18.788 1.00 80.41 ? 133 SER A CB 1 ATOM 1055 O OG . SER A 1 133 ? 35.693 -2.096 19.111 1.00 80.28 ? 133 SER A OG 1 ATOM 1056 N N . ALA A 1 134 ? 35.131 -4.140 16.541 1.00 79.20 ? 134 ALA A N 1 ATOM 1057 C CA . ALA A 1 134 ? 35.731 -4.530 15.263 1.00 78.90 ? 134 ALA A CA 1 ATOM 1058 C C . ALA A 1 134 ? 34.684 -4.960 14.231 1.00 80.12 ? 134 ALA A C 1 ATOM 1059 O O . ALA A 1 134 ? 34.928 -4.870 13.024 1.00 77.65 ? 134 ALA A O 1 ATOM 1060 C CB . ALA A 1 134 ? 36.732 -5.654 15.478 1.00 78.20 ? 134 ALA A CB 1 ATOM 1061 N N . CYS A 1 135 ? 33.530 -5.425 14.715 1.00 82.74 ? 135 CYS A N 1 ATOM 1062 C CA . CYS A 1 135 ? 32.425 -5.873 13.864 1.00 82.27 ? 135 CYS A CA 1 ATOM 1063 C C . CYS A 1 135 ? 31.168 -5.035 14.104 1.00 81.68 ? 135 CYS A C 1 ATOM 1064 O O . CYS A 1 135 ? 30.174 -5.534 14.634 1.00 80.47 ? 135 CYS A O 1 ATOM 1065 C CB . CYS A 1 135 ? 32.123 -7.341 14.155 1.00 84.34 ? 135 CYS A CB 1 ATOM 1066 S SG . CYS A 1 135 ? 33.516 -8.444 13.849 1.00 87.13 ? 135 CYS A SG 1 ATOM 1067 N N . PRO A 1 136 ? 31.202 -3.754 13.701 1.00 80.74 ? 136 PRO A N 1 ATOM 1068 C CA . PRO A 1 136 ? 30.081 -2.883 14.001 1.00 81.74 ? 136 PRO A CA 1 ATOM 1069 C C . PRO A 1 136 ? 28.873 -3.158 13.110 1.00 81.55 ? 136 PRO A C 1 ATOM 1070 O O . PRO A 1 136 ? 29.032 -3.538 11.952 1.00 78.39 ? 136 PRO A O 1 ATOM 1071 C CB . PRO A 1 136 ? 30.644 -1.493 13.711 1.00 82.73 ? 136 PRO A CB 1 ATOM 1072 C CG . PRO A 1 136 ? 31.609 -1.724 12.602 1.00 80.28 ? 136 PRO A CG 1 ATOM 1073 C CD . PRO A 1 136 ? 32.219 -3.072 12.877 1.00 79.12 ? 136 PRO A CD 1 ATOM 1074 N N . TYR A 1 137 ? 27.680 -2.976 13.670 1.00 84.17 ? 137 TYR A N 1 ATOM 1075 C CA . TYR A 1 137 ? 26.435 -3.019 12.911 1.00 84.44 ? 137 TYR A CA 1 ATOM 1076 C C . TYR A 1 137 ? 25.523 -1.896 13.370 1.00 85.89 ? 137 TYR A C 1 ATOM 1077 O O . TYR A 1 137 ? 25.065 -1.892 14.513 1.00 87.32 ? 137 TYR A O 1 ATOM 1078 C CB . TYR A 1 137 ? 25.726 -4.355 13.107 1.00 85.20 ? 137 TYR A CB 1 ATOM 1079 C CG . TYR A 1 137 ? 24.366 -4.422 12.442 1.00 87.07 ? 137 TYR A CG 1 ATOM 1080 C CD1 . TYR A 1 137 ? 24.248 -4.395 11.051 1.00 86.69 ? 137 TYR A CD1 1 ATOM 1081 C CD2 . TYR A 1 137 ? 23.199 -4.522 13.200 1.00 88.90 ? 137 TYR A CD2 1 ATOM 1082 C CE1 . TYR A 1 137 ? 23.007 -4.462 10.437 1.00 87.79 ? 137 TYR A CE1 1 ATOM 1083 C CE2 . TYR A 1 137 ? 21.956 -4.589 12.593 1.00 90.50 ? 137 TYR A CE2 1 ATOM 1084 C CZ . TYR A 1 137 ? 21.866 -4.561 11.214 1.00 90.18 ? 137 TYR A CZ 1 ATOM 1085 O OH . TYR A 1 137 ? 20.634 -4.629 10.607 1.00 92.39 ? 137 TYR A OH 1 ATOM 1086 N N . GLN A 1 138 ? 25.271 -0.942 12.478 1.00 86.00 ? 138 GLN A N 1 ATOM 1087 C CA . GLN A 1 138 ? 24.320 0.127 12.745 1.00 89.03 ? 138 GLN A CA 1 ATOM 1088 C C . GLN A 1 138 ? 24.779 0.978 13.941 1.00 90.08 ? 138 GLN A C 1 ATOM 1089 O O . GLN A 1 138 ? 23.978 1.376 14.786 1.00 92.42 ? 138 GLN A O 1 ATOM 1090 C CB . GLN A 1 138 ? 22.934 -0.493 12.979 1.00 91.68 ? 138 GLN A CB 1 ATOM 1091 C CG . GLN A 1 138 ? 21.770 0.243 12.334 1.00 94.60 ? 138 GLN A CG 1 ATOM 1092 C CD . GLN A 1 138 ? 20.728 -0.716 11.781 1.00 95.29 ? 138 GLN A CD 1 ATOM 1093 O OE1 . GLN A 1 138 ? 19.610 -0.797 12.286 1.00 97.89 ? 138 GLN A OE1 1 ATOM 1094 N NE2 . GLN A 1 138 ? 21.102 -1.463 10.746 1.00 93.31 ? 138 GLN A NE2 1 ATOM 1095 N N . GLY A 1 139 ? 26.083 1.241 14.004 1.00 88.54 ? 139 GLY A N 1 ATOM 1096 C CA . GLY A 1 139 ? 26.671 2.060 15.064 1.00 89.56 ? 139 GLY A CA 1 ATOM 1097 C C . GLY A 1 139 ? 27.061 1.304 16.322 1.00 89.07 ? 139 GLY A C 1 ATOM 1098 O O . GLY A 1 139 ? 27.789 1.830 17.161 1.00 89.04 ? 139 GLY A O 1 ATOM 1099 N N . LYS A 1 140 ? 26.584 0.071 16.457 1.00 88.43 ? 140 LYS A N 1 ATOM 1100 C CA . LYS A 1 140 ? 26.786 -0.708 17.675 1.00 89.50 ? 140 LYS A CA 1 ATOM 1101 C C . LYS A 1 140 ? 27.785 -1.816 17.420 1.00 86.31 ? 140 LYS A C 1 ATOM 1102 O O . LYS A 1 140 ? 28.034 -2.172 16.272 1.00 83.93 ? 140 LYS A O 1 ATOM 1103 C CB . LYS A 1 140 ? 25.466 -1.332 18.128 1.00 92.16 ? 140 LYS A CB 1 ATOM 1104 C CG . LYS A 1 140 ? 24.435 -0.341 18.635 1.00 96.46 ? 140 LYS A CG 1 ATOM 1105 C CD . LYS A 1 140 ? 23.039 -0.952 18.631 1.00 99.42 ? 140 LYS A CD 1 ATOM 1106 C CE . LYS A 1 140 ? 22.213 -0.496 19.828 1.00 104.47 ? 140 LYS A CE 1 ATOM 1107 N NZ . LYS A 1 140 ? 22.032 0.983 19.896 1.00 107.09 ? 140 LYS A NZ 1 ATOM 1108 N N . SER A 1 141 ? 28.342 -2.363 18.499 1.00 86.11 ? 141 SER A N 1 ATOM 1109 C CA . SER A 1 141 ? 29.215 -3.535 18.417 1.00 83.18 ? 141 SER A CA 1 ATOM 1110 C C . SER A 1 141 ? 28.387 -4.782 18.111 1.00 82.77 ? 141 SER A C 1 ATOM 1111 O O . SER A 1 141 ? 27.323 -4.986 18.697 1.00 84.83 ? 141 SER A O 1 ATOM 1112 C CB . SER A 1 141 ? 29.975 -3.721 19.728 1.00 83.14 ? 141 SER A CB 1 ATOM 1113 O OG . SER A 1 141 ? 30.844 -2.627 19.956 1.00 83.83 ? 141 SER A OG 1 ATOM 1114 N N . SER A 1 142 ? 28.870 -5.607 17.187 1.00 80.09 ? 142 SER A N 1 ATOM 1115 C CA . SER A 1 142 ? 28.166 -6.826 16.802 1.00 79.68 ? 142 SER A CA 1 ATOM 1116 C C . SER A 1 142 ? 29.176 -7.942 16.551 1.00 77.15 ? 142 SER A C 1 ATOM 1117 O O . SER A 1 142 ? 30.290 -7.883 17.069 1.00 76.66 ? 142 SER A O 1 ATOM 1118 C CB . SER A 1 142 ? 27.300 -6.564 15.566 1.00 80.53 ? 142 SER A CB 1 ATOM 1119 O OG . SER A 1 142 ? 26.422 -7.646 15.317 1.00 81.51 ? 142 SER A OG 1 ATOM 1120 N N . PHE A 1 143 ? 28.791 -8.959 15.777 1.00 75.60 ? 143 PHE A N 1 ATOM 1121 C CA . PHE A 1 143 ? 29.666 -10.105 15.523 1.00 74.63 ? 143 PHE A CA 1 ATOM 1122 C C . PHE A 1 143 ? 29.164 -10.981 14.366 1.00 74.55 ? 143 PHE A C 1 ATOM 1123 O O . PHE A 1 143 ? 28.021 -10.853 13.927 1.00 76.26 ? 143 PHE A O 1 ATOM 1124 C CB . PHE A 1 143 ? 29.798 -10.948 16.799 1.00 75.72 ? 143 PHE A CB 1 ATOM 1125 C CG . PHE A 1 143 ? 31.014 -11.831 16.824 1.00 74.93 ? 143 PHE A CG 1 ATOM 1126 C CD1 . PHE A 1 143 ? 32.289 -11.279 16.820 1.00 74.53 ? 143 PHE A CD1 1 ATOM 1127 C CD2 . PHE A 1 143 ? 30.887 -13.213 16.857 1.00 74.59 ? 143 PHE A CD2 1 ATOM 1128 C CE1 . PHE A 1 143 ? 33.414 -12.088 16.841 1.00 73.63 ? 143 PHE A CE1 1 ATOM 1129 C CE2 . PHE A 1 143 ? 32.008 -14.025 16.882 1.00 74.01 ? 143 PHE A CE2 1 ATOM 1130 C CZ . PHE A 1 143 ? 33.274 -13.462 16.875 1.00 73.39 ? 143 PHE A CZ 1 ATOM 1131 N N . PHE A 1 144 ? 30.033 -11.859 13.867 1.00 73.35 ? 144 PHE A N 1 ATOM 1132 C CA . PHE A 1 144 ? 29.656 -12.836 12.847 1.00 72.55 ? 144 PHE A CA 1 ATOM 1133 C C . PHE A 1 144 ? 28.326 -13.495 13.228 1.00 74.38 ? 144 PHE A C 1 ATOM 1134 O O . PHE A 1 144 ? 28.229 -14.167 14.248 1.00 77.42 ? 144 PHE A O 1 ATOM 1135 C CB . PHE A 1 144 ? 30.731 -13.922 12.701 1.00 71.49 ? 144 PHE A CB 1 ATOM 1136 C CG . PHE A 1 144 ? 32.082 -13.407 12.268 1.00 71.30 ? 144 PHE A CG 1 ATOM 1137 C CD1 . PHE A 1 144 ? 32.283 -12.930 10.978 1.00 70.03 ? 144 PHE A CD1 1 ATOM 1138 C CD2 . PHE A 1 144 ? 33.164 -13.412 13.154 1.00 71.25 ? 144 PHE A CD2 1 ATOM 1139 C CE1 . PHE A 1 144 ? 33.530 -12.468 10.582 1.00 68.98 ? 144 PHE A CE1 1 ATOM 1140 C CE2 . PHE A 1 144 ? 34.408 -12.949 12.761 1.00 69.53 ? 144 PHE A CE2 1 ATOM 1141 C CZ . PHE A 1 144 ? 34.592 -12.478 11.473 1.00 68.90 ? 144 PHE A CZ 1 ATOM 1142 N N . ARG A 1 145 ? 27.309 -13.305 12.397 1.00 74.32 ? 145 ARG A N 1 ATOM 1143 C CA . ARG A 1 145 ? 25.948 -13.712 12.728 1.00 75.42 ? 145 ARG A CA 1 ATOM 1144 C C . ARG A 1 145 ? 25.703 -15.218 12.812 1.00 76.92 ? 145 ARG A C 1 ATOM 1145 O O . ARG A 1 145 ? 24.696 -15.645 13.382 1.00 80.56 ? 145 ARG A O 1 ATOM 1146 C CB . ARG A 1 145 ? 24.978 -13.132 11.707 1.00 74.77 ? 145 ARG A CB 1 ATOM 1147 C CG . ARG A 1 145 ? 25.003 -11.622 11.626 1.00 74.85 ? 145 ARG A CG 1 ATOM 1148 C CD . ARG A 1 145 ? 23.706 -11.124 11.027 1.00 77.06 ? 145 ARG A CD 1 ATOM 1149 N NE . ARG A 1 145 ? 23.713 -9.681 10.848 1.00 78.31 ? 145 ARG A NE 1 ATOM 1150 C CZ . ARG A 1 145 ? 23.553 -8.799 11.830 1.00 80.61 ? 145 ARG A CZ 1 ATOM 1151 N NH1 . ARG A 1 145 ? 23.399 -9.188 13.096 1.00 80.67 ? 145 ARG A NH1 1 ATOM 1152 N NH2 . ARG A 1 145 ? 23.568 -7.506 11.542 1.00 82.66 ? 145 ARG A NH2 1 ATOM 1153 N N . ASN A 1 146 ? 26.596 -16.018 12.238 1.00 76.80 ? 146 ASN A N 1 ATOM 1154 C CA . ASN A 1 146 ? 26.374 -17.462 12.139 1.00 77.44 ? 146 ASN A CA 1 ATOM 1155 C C . ASN A 1 146 ? 27.073 -18.258 13.232 1.00 78.62 ? 146 ASN A C 1 ATOM 1156 O O . ASN A 1 146 ? 26.836 -19.460 13.375 1.00 80.07 ? 146 ASN A O 1 ATOM 1157 C CB . ASN A 1 146 ? 26.791 -17.971 10.754 1.00 74.90 ? 146 ASN A CB 1 ATOM 1158 C CG . ASN A 1 146 ? 25.906 -17.427 9.649 1.00 75.21 ? 146 ASN A CG 1 ATOM 1159 O OD1 . ASN A 1 146 ? 24.706 -17.229 9.844 1.00 77.55 ? 146 ASN A OD1 1 ATOM 1160 N ND2 . ASN A 1 146 ? 26.491 -17.181 8.484 1.00 74.49 ? 146 ASN A ND2 1 ATOM 1161 N N . VAL A 1 147 ? 27.920 -17.588 14.007 1.00 78.54 ? 147 VAL A N 1 ATOM 1162 C CA . VAL A 1 147 ? 28.612 -18.234 15.116 1.00 79.48 ? 147 VAL A CA 1 ATOM 1163 C C . VAL A 1 147 ? 28.428 -17.433 16.395 1.00 79.92 ? 147 VAL A C 1 ATOM 1164 O O . VAL A 1 147 ? 28.131 -16.240 16.358 1.00 80.17 ? 147 VAL A O 1 ATOM 1165 C CB . VAL A 1 147 ? 30.108 -18.454 14.809 1.00 78.91 ? 147 VAL A CB 1 ATOM 1166 C CG1 . VAL A 1 147 ? 30.268 -19.477 13.694 1.00 78.07 ? 147 VAL A CG1 1 ATOM 1167 C CG2 . VAL A 1 147 ? 30.799 -17.150 14.428 1.00 77.97 ? 147 VAL A CG2 1 ATOM 1168 N N . VAL A 1 148 ? 28.597 -18.106 17.524 1.00 81.88 ? 148 VAL A N 1 ATOM 1169 C CA . VAL A 1 148 ? 28.299 -17.528 18.834 1.00 83.35 ? 148 VAL A CA 1 ATOM 1170 C C . VAL A 1 148 ? 29.580 -17.467 19.649 1.00 82.67 ? 148 VAL A C 1 ATOM 1171 O O . VAL A 1 148 ? 30.187 -18.500 19.928 1.00 83.63 ? 148 VAL A O 1 ATOM 1172 C CB . VAL A 1 148 ? 27.248 -18.378 19.585 1.00 86.00 ? 148 VAL A CB 1 ATOM 1173 C CG1 . VAL A 1 148 ? 26.961 -17.805 20.965 1.00 88.79 ? 148 VAL A CG1 1 ATOM 1174 C CG2 . VAL A 1 148 ? 25.963 -18.478 18.770 1.00 86.67 ? 148 VAL A CG2 1 ATOM 1175 N N . TRP A 1 149 ? 29.996 -16.257 20.010 1.00 81.94 ? 149 TRP A N 1 ATOM 1176 C CA . TRP A 1 149 ? 31.152 -16.065 20.876 1.00 82.73 ? 149 TRP A CA 1 ATOM 1177 C C . TRP A 1 149 ? 30.695 -16.211 22.332 1.00 86.04 ? 149 TRP A C 1 ATOM 1178 O O . TRP A 1 149 ? 30.213 -15.257 22.950 1.00 87.41 ? 149 TRP A O 1 ATOM 1179 C CB . TRP A 1 149 ? 31.777 -14.693 20.622 1.00 81.72 ? 149 TRP A CB 1 ATOM 1180 C CG . TRP A 1 149 ? 33.046 -14.419 21.371 1.00 82.08 ? 149 TRP A CG 1 ATOM 1181 C CD1 . TRP A 1 149 ? 33.678 -15.235 22.273 1.00 82.83 ? 149 TRP A CD1 1 ATOM 1182 C CD2 . TRP A 1 149 ? 33.822 -13.221 21.307 1.00 81.53 ? 149 TRP A CD2 1 ATOM 1183 N NE1 . TRP A 1 149 ? 34.808 -14.620 22.755 1.00 82.84 ? 149 TRP A NE1 1 ATOM 1184 C CE2 . TRP A 1 149 ? 34.918 -13.382 22.180 1.00 81.64 ? 149 TRP A CE2 1 ATOM 1185 C CE3 . TRP A 1 149 ? 33.700 -12.026 20.588 1.00 81.21 ? 149 TRP A CE3 1 ATOM 1186 C CZ2 . TRP A 1 149 ? 35.886 -12.395 22.353 1.00 81.70 ? 149 TRP A CZ2 1 ATOM 1187 C CZ3 . TRP A 1 149 ? 34.666 -11.043 20.763 1.00 81.35 ? 149 TRP A CZ3 1 ATOM 1188 C CH2 . TRP A 1 149 ? 35.744 -11.236 21.639 1.00 81.27 ? 149 TRP A CH2 1 ATOM 1189 N N . LEU A 1 150 ? 30.840 -17.422 22.864 1.00 87.40 ? 150 LEU A N 1 ATOM 1190 C CA . LEU A 1 150 ? 30.386 -17.742 24.211 1.00 90.50 ? 150 LEU A CA 1 ATOM 1191 C C . LEU A 1 150 ? 31.414 -17.294 25.239 1.00 91.51 ? 150 LEU A C 1 ATOM 1192 O O . LEU A 1 150 ? 32.603 -17.592 25.087 1.00 90.03 ? 150 LEU A O 1 ATOM 1193 C CB . LEU A 1 150 ? 30.162 -19.249 24.350 1.00 91.90 ? 150 LEU A CB 1 ATOM 1194 C CG . LEU A 1 150 ? 29.049 -19.851 23.491 1.00 91.68 ? 150 LEU A CG 1 ATOM 1195 C CD1 . LEU A 1 150 ? 29.178 -21.365 23.425 1.00 92.66 ? 150 LEU A CD1 1 ATOM 1196 C CD2 . LEU A 1 150 ? 27.682 -19.454 24.024 1.00 93.75 ? 150 LEU A CD2 1 ATOM 1197 N N . ILE A 1 151 ? 30.943 -16.591 26.274 1.00 93.48 ? 151 ILE A N 1 ATOM 1198 C CA . ILE A 1 151 ? 31.777 -16.182 27.414 1.00 95.25 ? 151 ILE A CA 1 ATOM 1199 C C . ILE A 1 151 ? 31.190 -16.669 28.746 1.00 98.31 ? 151 ILE A C 1 ATOM 1200 O O . ILE A 1 151 ? 30.047 -17.127 28.807 1.00 98.54 ? 151 ILE A O 1 ATOM 1201 C CB . ILE A 1 151 ? 31.963 -14.647 27.466 1.00 95.36 ? 151 ILE A CB 1 ATOM 1202 C CG1 . ILE A 1 151 ? 30.638 -13.937 27.765 1.00 97.68 ? 151 ILE A CG1 1 ATOM 1203 C CG2 . ILE A 1 151 ? 32.544 -14.134 26.156 1.00 91.90 ? 151 ILE A CG2 1 ATOM 1204 C CD1 . ILE A 1 151 ? 30.791 -12.456 28.040 1.00 98.44 ? 151 ILE A CD1 1 ATOM 1205 N N . LYS A 1 152 ? 31.977 -16.545 29.811 1.00 101.58 ? 152 LYS A N 1 ATOM 1206 C CA . LYS A 1 152 ? 31.581 -17.009 31.154 1.00 106.04 ? 152 LYS A CA 1 ATOM 1207 C C . LYS A 1 152 ? 30.294 -16.366 31.676 1.00 108.76 ? 152 LYS A C 1 ATOM 1208 O O . LYS A 1 152 ? 29.997 -15.208 31.372 1.00 108.32 ? 152 LYS A O 1 ATOM 1209 C CB . LYS A 1 152 ? 32.700 -16.737 32.165 1.00 107.02 ? 152 LYS A CB 1 ATOM 1210 C CG . LYS A 1 152 ? 32.869 -15.267 32.531 1.00 107.34 ? 152 LYS A CG 1 ATOM 1211 C CD . LYS A 1 152 ? 34.053 -15.065 33.457 1.00 108.77 ? 152 LYS A CD 1 ATOM 1212 C CE . LYS A 1 152 ? 34.050 -13.689 34.091 1.00 109.62 ? 152 LYS A CE 1 ATOM 1213 N NZ . LYS A 1 152 ? 35.317 -13.454 34.832 1.00 111.24 ? 152 LYS A NZ 1 ATOM 1214 N N . LYS A 1 153 ? 29.554 -17.120 32.486 1.00 112.36 ? 153 LYS A N 1 ATOM 1215 C CA . LYS A 1 153 ? 28.318 -16.635 33.092 1.00 115.71 ? 153 LYS A CA 1 ATOM 1216 C C . LYS A 1 153 ? 28.417 -16.713 34.612 1.00 118.87 ? 153 LYS A C 1 ATOM 1217 O O . LYS A 1 153 ? 28.597 -17.794 35.172 1.00 119.68 ? 153 LYS A O 1 ATOM 1218 C CB . LYS A 1 153 ? 27.128 -17.452 32.594 1.00 116.76 ? 153 LYS A CB 1 ATOM 1219 C CG . LYS A 1 153 ? 25.783 -16.790 32.850 1.00 119.51 ? 153 LYS A CG 1 ATOM 1220 C CD . LYS A 1 153 ? 24.645 -17.594 32.244 1.00 120.81 ? 153 LYS A CD 1 ATOM 1221 C CE . LYS A 1 153 ? 24.248 -18.769 33.125 1.00 123.28 ? 153 LYS A CE 1 ATOM 1222 N NZ . LYS A 1 153 ? 23.273 -18.371 34.174 1.00 127.12 ? 153 LYS A NZ 1 ATOM 1223 N N . ASN A 1 154 ? 28.297 -15.559 35.266 1.00 120.71 ? 154 ASN A N 1 ATOM 1224 C CA . ASN A 1 154 ? 28.462 -15.442 36.720 1.00 125.54 ? 154 ASN A CA 1 ATOM 1225 C C . ASN A 1 154 ? 29.775 -16.076 37.205 1.00 125.23 ? 154 ASN A C 1 ATOM 1226 O O . ASN A 1 154 ? 29.802 -16.798 38.205 1.00 126.73 ? 154 ASN A O 1 ATOM 1227 C CB . ASN A 1 154 ? 27.246 -16.028 37.463 1.00 129.29 ? 154 ASN A CB 1 ATOM 1228 C CG . ASN A 1 154 ? 27.153 -15.556 38.908 1.00 134.23 ? 154 ASN A CG 1 ATOM 1229 O OD1 . ASN A 1 154 ? 27.771 -14.563 39.289 1.00 135.61 ? 154 ASN A OD1 1 ATOM 1230 N ND2 . ASN A 1 154 ? 26.377 -16.270 39.721 1.00 138.26 ? 154 ASN A ND2 1 ATOM 1231 N N . SER A 1 155 ? 30.857 -15.796 36.475 1.00 121.77 ? 155 SER A N 1 ATOM 1232 C CA . SER A 1 155 ? 32.201 -16.273 36.817 1.00 121.60 ? 155 SER A CA 1 ATOM 1233 C C . SER A 1 155 ? 32.319 -17.804 36.870 1.00 122.26 ? 155 SER A C 1 ATOM 1234 O O . SER A 1 155 ? 32.894 -18.347 37.812 1.00 125.62 ? 155 SER A O 1 ATOM 1235 C CB . SER A 1 155 ? 32.672 -15.664 38.152 1.00 124.35 ? 155 SER A CB 1 ATOM 1236 O OG . SER A 1 155 ? 32.590 -14.250 38.140 1.00 123.46 ? 155 SER A OG 1 ATOM 1237 N N . THR A 1 156 ? 31.762 -18.490 35.872 1.00 119.87 ? 156 THR A N 1 ATOM 1238 C CA . THR A 1 156 ? 32.003 -19.926 35.662 1.00 119.56 ? 156 THR A CA 1 ATOM 1239 C C . THR A 1 156 ? 31.817 -20.262 34.189 1.00 116.82 ? 156 THR A C 1 ATOM 1240 O O . THR A 1 156 ? 30.787 -19.925 33.607 1.00 118.62 ? 156 THR A O 1 ATOM 1241 C CB . THR A 1 156 ? 31.023 -20.840 36.431 1.00 122.25 ? 156 THR A CB 1 ATOM 1242 O OG1 . THR A 1 156 ? 29.687 -20.606 35.971 1.00 122.47 ? 156 THR A OG1 1 ATOM 1243 C CG2 . THR A 1 156 ? 31.092 -20.629 37.934 1.00 126.10 ? 156 THR A CG2 1 ATOM 1244 N N . TYR A 1 157 ? 32.808 -20.919 33.593 1.00 114.22 ? 157 TYR A N 1 ATOM 1245 C CA . TYR A 1 157 ? 32.677 -21.476 32.250 1.00 109.93 ? 157 TYR A CA 1 ATOM 1246 C C . TYR A 1 157 ? 32.817 -22.991 32.397 1.00 110.63 ? 157 TYR A C 1 ATOM 1247 O O . TYR A 1 157 ? 33.930 -23.522 32.353 1.00 109.41 ? 157 TYR A O 1 ATOM 1248 C CB . TYR A 1 157 ? 33.746 -20.900 31.313 1.00 107.29 ? 157 TYR A CB 1 ATOM 1249 C CG . TYR A 1 157 ? 33.463 -21.057 29.819 1.00 104.45 ? 157 TYR A CG 1 ATOM 1250 C CD1 . TYR A 1 157 ? 33.423 -22.314 29.215 1.00 104.05 ? 157 TYR A CD1 1 ATOM 1251 C CD2 . TYR A 1 157 ? 33.253 -19.942 29.011 1.00 101.99 ? 157 TYR A CD2 1 ATOM 1252 C CE1 . TYR A 1 157 ? 33.180 -22.454 27.854 1.00 102.00 ? 157 TYR A CE1 1 ATOM 1253 C CE2 . TYR A 1 157 ? 33.009 -20.073 27.653 1.00 99.82 ? 157 TYR A CE2 1 ATOM 1254 C CZ . TYR A 1 157 ? 32.969 -21.332 27.076 1.00 99.80 ? 157 TYR A CZ 1 ATOM 1255 O OH . TYR A 1 157 ? 32.729 -21.462 25.721 1.00 96.27 ? 157 TYR A OH 1 ATOM 1256 N N . PRO A 1 158 ? 31.690 -23.691 32.616 1.00 111.99 ? 158 PRO A N 1 ATOM 1257 C CA . PRO A 1 158 ? 31.759 -25.142 32.759 1.00 112.92 ? 158 PRO A CA 1 ATOM 1258 C C . PRO A 1 158 ? 31.988 -25.822 31.418 1.00 109.36 ? 158 PRO A C 1 ATOM 1259 O O . PRO A 1 158 ? 31.768 -25.212 30.370 1.00 106.18 ? 158 PRO A O 1 ATOM 1260 C CB . PRO A 1 158 ? 30.387 -25.508 33.339 1.00 115.81 ? 158 PRO A CB 1 ATOM 1261 C CG . PRO A 1 158 ? 29.477 -24.424 32.884 1.00 114.66 ? 158 PRO A CG 1 ATOM 1262 C CD . PRO A 1 158 ? 30.317 -23.180 32.796 1.00 113.23 ? 158 PRO A CD 1 ATOM 1263 N N . THR A 1 159 ? 32.432 -27.073 31.457 1.00 110.27 ? 159 THR A N 1 ATOM 1264 C CA . THR A 1 159 ? 32.730 -27.810 30.238 1.00 108.11 ? 159 THR A CA 1 ATOM 1265 C C . THR A 1 159 ? 31.475 -27.937 29.380 1.00 107.54 ? 159 THR A C 1 ATOM 1266 O O . THR A 1 159 ? 30.412 -28.312 29.872 1.00 108.20 ? 159 THR A O 1 ATOM 1267 C CB . THR A 1 159 ? 33.288 -29.218 30.534 1.00 109.92 ? 159 THR A CB 1 ATOM 1268 O OG1 . THR A 1 159 ? 34.351 -29.129 31.488 1.00 111.43 ? 159 THR A OG1 1 ATOM 1269 C CG2 . THR A 1 159 ? 33.818 -29.868 29.262 1.00 107.85 ? 159 THR A CG2 1 ATOM 1270 N N . ILE A 1 160 ? 31.615 -27.592 28.102 1.00 105.80 ? 160 ILE A N 1 ATOM 1271 C CA . ILE A 1 160 ? 30.553 -27.760 27.114 1.00 105.62 ? 160 ILE A CA 1 ATOM 1272 C C . ILE A 1 160 ? 30.691 -29.150 26.512 1.00 107.13 ? 160 ILE A C 1 ATOM 1273 O O . ILE A 1 160 ? 31.797 -29.580 26.204 1.00 106.43 ? 160 ILE A O 1 ATOM 1274 C CB . ILE A 1 160 ? 30.656 -26.692 25.998 1.00 101.86 ? 160 ILE A CB 1 ATOM 1275 C CG1 . ILE A 1 160 ? 30.361 -25.302 26.574 1.00 102.08 ? 160 ILE A CG1 1 ATOM 1276 C CG2 . ILE A 1 160 ? 29.704 -27.005 24.848 1.00 100.67 ? 160 ILE A CG2 1 ATOM 1277 C CD1 . ILE A 1 160 ? 30.811 -24.154 25.698 1.00 99.21 ? 160 ILE A CD1 1 ATOM 1278 N N . LYS A 1 161 ? 29.575 -29.858 26.372 1.00 110.28 ? 161 LYS A N 1 ATOM 1279 C CA . LYS A 1 161 ? 29.554 -31.149 25.684 1.00 112.60 ? 161 LYS A CA 1 ATOM 1280 C C . LYS A 1 161 ? 28.293 -31.220 24.841 1.00 113.37 ? 161 LYS A C 1 ATOM 1281 O O . LYS A 1 161 ? 27.248 -31.669 25.307 1.00 116.61 ? 161 LYS A O 1 ATOM 1282 C CB . LYS A 1 161 ? 29.603 -32.314 26.680 1.00 118.09 ? 161 LYS A CB 1 ATOM 1283 C CG . LYS A 1 161 ? 30.993 -32.628 27.217 1.00 120.07 ? 161 LYS A CG 1 ATOM 1284 C CD . LYS A 1 161 ? 30.947 -33.535 28.442 1.00 124.47 ? 161 LYS A CD 1 ATOM 1285 C CE . LYS A 1 161 ? 32.326 -33.708 29.071 1.00 125.66 ? 161 LYS A CE 1 ATOM 1286 N NZ . LYS A 1 161 ? 32.270 -34.331 30.426 1.00 130.00 ? 161 LYS A NZ 1 ATOM 1287 N N . ARG A 1 162 ? 28.396 -30.754 23.601 1.00 111.48 ? 162 ARG A N 1 ATOM 1288 C CA . ARG A 1 162 ? 27.254 -30.693 22.705 1.00 111.69 ? 162 ARG A CA 1 ATOM 1289 C C . ARG A 1 162 ? 27.450 -31.605 21.519 1.00 110.87 ? 162 ARG A C 1 ATOM 1290 O O . ARG A 1 162 ? 28.580 -31.909 21.135 1.00 110.99 ? 162 ARG A O 1 ATOM 1291 C CB . ARG A 1 162 ? 27.051 -29.265 22.210 1.00 110.33 ? 162 ARG A CB 1 ATOM 1292 C CG . ARG A 1 162 ? 26.310 -28.371 23.185 1.00 113.28 ? 162 ARG A CG 1 ATOM 1293 C CD . ARG A 1 162 ? 24.860 -28.804 23.361 1.00 116.60 ? 162 ARG A CD 1 ATOM 1294 N NE . ARG A 1 162 ? 23.936 -27.715 23.060 1.00 117.15 ? 162 ARG A NE 1 ATOM 1295 C CZ . ARG A 1 162 ? 23.780 -26.619 23.800 1.00 119.31 ? 162 ARG A CZ 1 ATOM 1296 N NH1 . ARG A 1 162 ? 24.487 -26.436 24.913 1.00 121.69 ? 162 ARG A NH1 1 ATOM 1297 N NH2 . ARG A 1 162 ? 22.910 -25.690 23.422 1.00 119.96 ? 162 ARG A NH2 1 ATOM 1298 N N . SER A 1 163 ? 26.337 -32.030 20.932 1.00 110.50 ? 163 SER A N 1 ATOM 1299 C CA . SER A 1 163 ? 26.373 -32.863 19.741 1.00 107.29 ? 163 SER A CA 1 ATOM 1300 C C . SER A 1 163 ? 25.241 -32.480 18.790 1.00 105.59 ? 163 SER A C 1 ATOM 1301 O O . SER A 1 163 ? 24.135 -32.180 19.227 1.00 104.85 ? 163 SER A O 1 ATOM 1302 C CB . SER A 1 163 ? 26.269 -34.337 20.132 1.00 109.48 ? 163 SER A CB 1 ATOM 1303 O OG . SER A 1 163 ? 26.796 -35.170 19.114 1.00 109.63 ? 163 SER A OG 1 ATOM 1304 N N . TYR A 1 164 ? 25.530 -32.458 17.492 1.00 103.80 ? 164 TYR A N 1 ATOM 1305 C CA . TYR A 1 164 ? 24.483 -32.304 16.489 1.00 103.58 ? 164 TYR A CA 1 ATOM 1306 C C . TYR A 1 164 ? 24.513 -33.483 15.533 1.00 105.58 ? 164 TYR A C 1 ATOM 1307 O O . TYR A 1 164 ? 25.585 -33.941 15.139 1.00 105.60 ? 164 TYR A O 1 ATOM 1308 C CB . TYR A 1 164 ? 24.628 -31.000 15.709 1.00 99.38 ? 164 TYR A CB 1 ATOM 1309 C CG . TYR A 1 164 ? 23.656 -30.923 14.558 1.00 99.27 ? 164 TYR A CG 1 ATOM 1310 C CD1 . TYR A 1 164 ? 22.323 -30.589 14.767 1.00 100.56 ? 164 TYR A CD1 1 ATOM 1311 C CD2 . TYR A 1 164 ? 24.061 -31.225 13.261 1.00 98.93 ? 164 TYR A CD2 1 ATOM 1312 C CE1 . TYR A 1 164 ? 21.424 -30.536 13.715 1.00 101.28 ? 164 TYR A CE1 1 ATOM 1313 C CE2 . TYR A 1 164 ? 23.170 -31.177 12.200 1.00 98.91 ? 164 TYR A CE2 1 ATOM 1314 C CZ . TYR A 1 164 ? 21.855 -30.834 12.432 1.00 100.75 ? 164 TYR A CZ 1 ATOM 1315 O OH . TYR A 1 164 ? 20.978 -30.785 11.377 1.00 102.04 ? 164 TYR A OH 1 ATOM 1316 N N . ASN A 1 165 ? 23.325 -33.958 15.166 1.00 109.15 ? 165 ASN A N 1 ATOM 1317 C CA . ASN A 1 165 ? 23.172 -35.068 14.236 1.00 111.68 ? 165 ASN A CA 1 ATOM 1318 C C . ASN A 1 165 ? 22.570 -34.576 12.930 1.00 108.18 ? 165 ASN A C 1 ATOM 1319 O O . ASN A 1 165 ? 21.471 -34.023 12.924 1.00 108.62 ? 165 ASN A O 1 ATOM 1320 C CB . ASN A 1 165 ? 22.265 -36.130 14.850 1.00 119.02 ? 165 ASN A CB 1 ATOM 1321 C CG . ASN A 1 165 ? 22.239 -37.417 14.050 1.00 124.77 ? 165 ASN A CG 1 ATOM 1322 O OD1 . ASN A 1 165 ? 22.663 -37.472 12.900 1.00 125.40 ? 165 ASN A OD1 1 ATOM 1323 N ND2 . ASN A 1 165 ? 21.736 -38.469 14.672 1.00 135.72 ? 165 ASN A ND2 1 ATOM 1324 N N . ASN A 1 166 ? 23.286 -34.779 11.826 1.00 104.34 ? 166 ASN A N 1 ATOM 1325 C CA . ASN A 1 166 ? 22.761 -34.409 10.519 1.00 101.94 ? 166 ASN A CA 1 ATOM 1326 C C . ASN A 1 166 ? 21.672 -35.376 10.095 1.00 103.93 ? 166 ASN A C 1 ATOM 1327 O O . ASN A 1 166 ? 21.950 -36.446 9.550 1.00 103.55 ? 166 ASN A O 1 ATOM 1328 C CB . ASN A 1 166 ? 23.851 -34.365 9.455 1.00 98.79 ? 166 ASN A CB 1 ATOM 1329 C CG . ASN A 1 166 ? 23.335 -33.843 8.131 1.00 97.71 ? 166 ASN A CG 1 ATOM 1330 O OD1 . ASN A 1 166 ? 22.245 -33.266 8.062 1.00 96.62 ? 166 ASN A OD1 1 ATOM 1331 N ND2 . ASN A 1 166 ? 24.112 -34.041 7.072 1.00 96.59 ? 166 ASN A ND2 1 ATOM 1332 N N . THR A 1 167 ? 20.431 -34.982 10.365 1.00 105.41 ? 167 THR A N 1 ATOM 1333 C CA . THR A 1 167 ? 19.262 -35.781 10.027 1.00 108.00 ? 167 THR A CA 1 ATOM 1334 C C . THR A 1 167 ? 18.793 -35.502 8.597 1.00 108.31 ? 167 THR A C 1 ATOM 1335 O O . THR A 1 167 ? 17.975 -36.244 8.053 1.00 112.09 ? 167 THR A O 1 ATOM 1336 C CB . THR A 1 167 ? 18.111 -35.492 11.003 1.00 109.22 ? 167 THR A CB 1 ATOM 1337 O OG1 . THR A 1 167 ? 17.722 -34.116 10.900 1.00 106.96 ? 167 THR A OG1 1 ATOM 1338 C CG2 . THR A 1 167 ? 18.550 -35.783 12.422 1.00 109.38 ? 167 THR A CG2 1 ATOM 1339 N N . ASN A 1 168 ? 19.325 -34.442 7.991 1.00 104.93 ? 168 ASN A N 1 ATOM 1340 C CA . ASN A 1 168 ? 18.946 -34.056 6.637 1.00 103.46 ? 168 ASN A CA 1 ATOM 1341 C C . ASN A 1 168 ? 19.499 -35.027 5.613 1.00 103.95 ? 168 ASN A C 1 ATOM 1342 O O . ASN A 1 168 ? 20.435 -35.770 5.901 1.00 104.64 ? 168 ASN A O 1 ATOM 1343 C CB . ASN A 1 168 ? 19.473 -32.663 6.316 1.00 100.32 ? 168 ASN A CB 1 ATOM 1344 C CG . ASN A 1 168 ? 19.066 -31.637 7.346 1.00 99.52 ? 168 ASN A CG 1 ATOM 1345 O OD1 . ASN A 1 168 ? 17.930 -31.165 7.343 1.00 100.98 ? 168 ASN A OD1 1 ATOM 1346 N ND2 . ASN A 1 168 ? 19.994 -31.278 8.231 1.00 97.14 ? 168 ASN A ND2 1 ATOM 1347 N N . GLN A 1 169 ? 18.927 -35.005 4.413 1.00 104.21 ? 169 GLN A N 1 ATOM 1348 C CA . GLN A 1 169 ? 19.446 -35.808 3.307 1.00 105.13 ? 169 GLN A CA 1 ATOM 1349 C C . GLN A 1 169 ? 20.744 -35.218 2.763 1.00 101.57 ? 169 GLN A C 1 ATOM 1350 O O . GLN A 1 169 ? 21.598 -35.951 2.273 1.00 101.14 ? 169 GLN A O 1 ATOM 1351 C CB . GLN A 1 169 ? 18.424 -35.907 2.166 1.00 108.30 ? 169 GLN A CB 1 ATOM 1352 C CG . GLN A 1 169 ? 17.040 -36.352 2.593 1.00 112.68 ? 169 GLN A CG 1 ATOM 1353 C CD . GLN A 1 169 ? 17.091 -37.497 3.583 1.00 116.49 ? 169 GLN A CD 1 ATOM 1354 O OE1 . GLN A 1 169 ? 17.502 -38.605 3.238 1.00 118.72 ? 169 GLN A OE1 1 ATOM 1355 N NE2 . GLN A 1 169 ? 16.689 -37.234 4.825 1.00 118.42 ? 169 GLN A NE2 1 ATOM 1356 N N . GLU A 1 170 ? 20.891 -33.898 2.882 1.00 98.91 ? 170 GLU A N 1 ATOM 1357 C CA . GLU A 1 170 ? 21.937 -33.141 2.196 1.00 95.45 ? 170 GLU A CA 1 ATOM 1358 C C . GLU A 1 170 ? 23.179 -32.939 3.050 1.00 93.64 ? 170 GLU A C 1 ATOM 1359 O O . GLU A 1 170 ? 23.070 -32.707 4.252 1.00 96.09 ? 170 GLU A O 1 ATOM 1360 C CB . GLU A 1 170 ? 21.404 -31.764 1.804 1.00 94.12 ? 170 GLU A CB 1 ATOM 1361 C CG . GLU A 1 170 ? 20.119 -31.791 0.989 1.00 96.44 ? 170 GLU A CG 1 ATOM 1362 C CD . GLU A 1 170 ? 18.866 -31.792 1.843 1.00 98.14 ? 170 GLU A CD 1 ATOM 1363 O OE1 . GLU A 1 170 ? 18.932 -32.260 2.997 1.00 100.51 ? 170 GLU A OE1 1 ATOM 1364 O OE2 . GLU A 1 170 ? 17.814 -31.322 1.363 1.00 98.16 ? 170 GLU A OE2 1 ATOM 1365 N N . ASP A 1 171 ? 24.355 -33.025 2.424 1.00 92.84 ? 171 ASP A N 1 ATOM 1366 C CA . ASP A 1 171 ? 25.623 -32.694 3.083 1.00 89.73 ? 171 ASP A CA 1 ATOM 1367 C C . ASP A 1 171 ? 25.481 -31.355 3.788 1.00 88.14 ? 171 ASP A C 1 ATOM 1368 O O . ASP A 1 171 ? 24.782 -30.462 3.302 1.00 86.47 ? 171 ASP A O 1 ATOM 1369 C CB . ASP A 1 171 ? 26.773 -32.587 2.068 1.00 89.14 ? 171 ASP A CB 1 ATOM 1370 C CG . ASP A 1 171 ? 27.284 -33.939 1.582 1.00 91.25 ? 171 ASP A CG 1 ATOM 1371 O OD1 . ASP A 1 171 ? 26.997 -34.977 2.216 1.00 92.69 ? 171 ASP A OD1 1 ATOM 1372 O OD2 . ASP A 1 171 ? 28.002 -33.953 0.556 1.00 90.72 ? 171 ASP A OD2 1 ATOM 1373 N N . LEU A 1 172 ? 26.156 -31.218 4.925 1.00 88.57 ? 172 LEU A N 1 ATOM 1374 C CA . LEU A 1 172 ? 26.048 -30.022 5.744 1.00 88.04 ? 172 LEU A CA 1 ATOM 1375 C C . LEU A 1 172 ? 27.421 -29.403 5.990 1.00 86.21 ? 172 LEU A C 1 ATOM 1376 O O . LEU A 1 172 ? 28.298 -30.043 6.571 1.00 87.12 ? 172 LEU A O 1 ATOM 1377 C CB . LEU A 1 172 ? 25.384 -30.371 7.075 1.00 90.66 ? 172 LEU A CB 1 ATOM 1378 C CG . LEU A 1 172 ? 24.798 -29.194 7.861 1.00 91.79 ? 172 LEU A CG 1 ATOM 1379 C CD1 . LEU A 1 172 ? 23.498 -28.705 7.234 1.00 92.23 ? 172 LEU A CD1 1 ATOM 1380 C CD2 . LEU A 1 172 ? 24.569 -29.582 9.315 1.00 93.88 ? 172 LEU A CD2 1 ATOM 1381 N N . LEU A 1 173 ? 27.601 -28.165 5.530 1.00 83.54 ? 173 LEU A N 1 ATOM 1382 C CA . LEU A 1 173 ? 28.801 -27.389 5.838 1.00 80.40 ? 173 LEU A CA 1 ATOM 1383 C C . LEU A 1 173 ? 28.652 -26.778 7.219 1.00 80.10 ? 173 LEU A C 1 ATOM 1384 O O . LEU A 1 173 ? 27.735 -25.994 7.443 1.00 81.51 ? 173 LEU A O 1 ATOM 1385 C CB . LEU A 1 173 ? 29.008 -26.263 4.825 1.00 78.58 ? 173 LEU A CB 1 ATOM 1386 C CG . LEU A 1 173 ? 30.091 -25.239 5.190 1.00 76.39 ? 173 LEU A CG 1 ATOM 1387 C CD1 . LEU A 1 173 ? 31.448 -25.913 5.271 1.00 75.95 ? 173 LEU A CD1 1 ATOM 1388 C CD2 . LEU A 1 173 ? 30.127 -24.086 4.201 1.00 75.14 ? 173 LEU A CD2 1 ATOM 1389 N N . VAL A 1 174 ? 29.563 -27.122 8.128 1.00 79.17 ? 174 VAL A N 1 ATOM 1390 C CA . VAL A 1 174 ? 29.556 -26.593 9.491 1.00 78.34 ? 174 VAL A CA 1 ATOM 1391 C C . VAL A 1 174 ? 30.798 -25.739 9.720 1.00 75.75 ? 174 VAL A C 1 ATOM 1392 O O . VAL A 1 174 ? 31.888 -26.106 9.287 1.00 75.55 ? 174 VAL A O 1 ATOM 1393 C CB . VAL A 1 174 ? 29.544 -27.726 10.538 1.00 80.42 ? 174 VAL A CB 1 ATOM 1394 C CG1 . VAL A 1 174 ? 29.287 -27.163 11.929 1.00 81.60 ? 174 VAL A CG1 1 ATOM 1395 C CG2 . VAL A 1 174 ? 28.496 -28.770 10.186 1.00 82.67 ? 174 VAL A CG2 1 ATOM 1396 N N . LEU A 1 175 ? 30.625 -24.619 10.421 1.00 74.77 ? 175 LEU A N 1 ATOM 1397 C CA . LEU A 1 175 ? 31.711 -23.686 10.723 1.00 73.02 ? 175 LEU A CA 1 ATOM 1398 C C . LEU A 1 175 ? 31.782 -23.407 12.213 1.00 74.05 ? 175 LEU A C 1 ATOM 1399 O O . LEU A 1 175 ? 30.752 -23.216 12.851 1.00 75.56 ? 175 LEU A O 1 ATOM 1400 C CB . LEU A 1 175 ? 31.463 -22.363 10.014 1.00 71.54 ? 175 LEU A CB 1 ATOM 1401 C CG . LEU A 1 175 ? 31.387 -22.430 8.490 1.00 71.09 ? 175 LEU A CG 1 ATOM 1402 C CD1 . LEU A 1 175 ? 30.330 -21.461 7.982 1.00 71.52 ? 175 LEU A CD1 1 ATOM 1403 C CD2 . LEU A 1 175 ? 32.750 -22.149 7.872 1.00 69.08 ? 175 LEU A CD2 1 ATOM 1404 N N . TRP A 1 176 ? 32.992 -23.366 12.763 1.00 73.58 ? 176 TRP A N 1 ATOM 1405 C CA . TRP A 1 176 ? 33.194 -22.952 14.152 1.00 75.16 ? 176 TRP A CA 1 ATOM 1406 C C . TRP A 1 176 ? 34.499 -22.164 14.286 1.00 74.29 ? 176 TRP A C 1 ATOM 1407 O O . TRP A 1 176 ? 35.131 -21.843 13.285 1.00 73.22 ? 176 TRP A O 1 ATOM 1408 C CB . TRP A 1 176 ? 33.160 -24.169 15.085 1.00 77.76 ? 176 TRP A CB 1 ATOM 1409 C CG . TRP A 1 176 ? 34.248 -25.161 14.844 1.00 78.07 ? 176 TRP A CG 1 ATOM 1410 C CD1 . TRP A 1 176 ? 35.415 -25.280 15.538 1.00 79.04 ? 176 TRP A CD1 1 ATOM 1411 C CD2 . TRP A 1 176 ? 34.271 -26.181 13.843 1.00 77.76 ? 176 TRP A CD2 1 ATOM 1412 N NE1 . TRP A 1 176 ? 36.167 -26.310 15.031 1.00 78.76 ? 176 TRP A NE1 1 ATOM 1413 C CE2 . TRP A 1 176 ? 35.485 -26.882 13.990 1.00 78.74 ? 176 TRP A CE2 1 ATOM 1414 C CE3 . TRP A 1 176 ? 33.381 -26.572 12.837 1.00 77.79 ? 176 TRP A CE3 1 ATOM 1415 C CZ2 . TRP A 1 176 ? 35.837 -27.952 13.163 1.00 79.65 ? 176 TRP A CZ2 1 ATOM 1416 C CZ3 . TRP A 1 176 ? 33.728 -27.637 12.018 1.00 78.34 ? 176 TRP A CZ3 1 ATOM 1417 C CH2 . TRP A 1 176 ? 34.947 -28.312 12.183 1.00 79.05 ? 176 TRP A CH2 1 ATOM 1418 N N . GLY A 1 177 ? 34.893 -21.830 15.513 1.00 76.36 ? 177 GLY A N 1 ATOM 1419 C CA . GLY A 1 177 ? 36.116 -21.051 15.722 1.00 76.25 ? 177 GLY A CA 1 ATOM 1420 C C . GLY A 1 177 ? 36.734 -21.135 17.106 1.00 78.18 ? 177 GLY A C 1 ATOM 1421 O O . GLY A 1 177 ? 36.144 -21.670 18.045 1.00 79.76 ? 177 GLY A O 1 ATOM 1422 N N . ILE A 1 178 ? 37.939 -20.589 17.212 1.00 78.26 ? 178 ILE A N 1 ATOM 1423 C CA . ILE A 1 178 ? 38.687 -20.530 18.462 1.00 80.69 ? 178 ILE A CA 1 ATOM 1424 C C . ILE A 1 178 ? 39.138 -19.078 18.639 1.00 80.97 ? 178 ILE A C 1 ATOM 1425 O O . ILE A 1 178 ? 39.539 -18.427 17.671 1.00 79.51 ? 178 ILE A O 1 ATOM 1426 C CB . ILE A 1 178 ? 39.894 -21.512 18.450 1.00 81.91 ? 178 ILE A CB 1 ATOM 1427 C CG1 . ILE A 1 178 ? 40.764 -21.380 19.707 1.00 84.47 ? 178 ILE A CG1 1 ATOM 1428 C CG2 . ILE A 1 178 ? 40.775 -21.309 17.229 1.00 80.71 ? 178 ILE A CG2 1 ATOM 1429 C CD1 . ILE A 1 178 ? 40.459 -22.388 20.789 1.00 87.51 ? 178 ILE A CD1 1 ATOM 1430 N N . HIS A 1 179 ? 39.052 -18.568 19.865 1.00 82.12 ? 179 HIS A N 1 ATOM 1431 C CA . HIS A 1 179 ? 39.531 -17.223 20.169 1.00 82.73 ? 179 HIS A CA 1 ATOM 1432 C C . HIS A 1 179 ? 40.931 -17.268 20.784 1.00 83.56 ? 179 HIS A C 1 ATOM 1433 O O . HIS A 1 179 ? 41.177 -18.010 21.738 1.00 85.95 ? 179 HIS A O 1 ATOM 1434 C CB . HIS A 1 179 ? 38.565 -16.501 21.108 1.00 84.34 ? 179 HIS A CB 1 ATOM 1435 C CG . HIS A 1 179 ? 39.029 -15.137 21.508 1.00 84.99 ? 179 HIS A CG 1 ATOM 1436 N ND1 . HIS A 1 179 ? 39.046 -14.710 22.818 1.00 87.51 ? 179 HIS A ND1 1 ATOM 1437 C CD2 . HIS A 1 179 ? 39.516 -14.111 20.772 1.00 84.32 ? 179 HIS A CD2 1 ATOM 1438 C CE1 . HIS A 1 179 ? 39.507 -13.473 22.870 1.00 88.14 ? 179 HIS A CE1 1 ATOM 1439 N NE2 . HIS A 1 179 ? 39.801 -13.086 21.642 1.00 86.46 ? 179 HIS A NE2 1 ATOM 1440 N N . HIS A 1 180 ? 41.834 -16.466 20.224 1.00 81.97 ? 180 HIS A N 1 ATOM 1441 C CA . HIS A 1 180 ? 43.213 -16.366 20.687 1.00 83.11 ? 180 HIS A CA 1 ATOM 1442 C C . HIS A 1 180 ? 43.391 -15.011 21.361 1.00 84.14 ? 180 HIS A C 1 ATOM 1443 O O . HIS A 1 180 ? 43.698 -14.029 20.695 1.00 83.62 ? 180 HIS A O 1 ATOM 1444 C CB . HIS A 1 180 ? 44.177 -16.473 19.503 1.00 82.10 ? 180 HIS A CB 1 ATOM 1445 C CG . HIS A 1 180 ? 44.124 -17.790 18.796 1.00 80.69 ? 180 HIS A CG 1 ATOM 1446 N ND1 . HIS A 1 180 ? 44.291 -18.986 19.453 1.00 82.35 ? 180 HIS A ND1 1 ATOM 1447 C CD2 . HIS A 1 180 ? 43.930 -18.100 17.494 1.00 78.54 ? 180 HIS A CD2 1 ATOM 1448 C CE1 . HIS A 1 180 ? 44.199 -19.980 18.590 1.00 80.32 ? 180 HIS A CE1 1 ATOM 1449 N NE2 . HIS A 1 180 ? 43.977 -19.470 17.394 1.00 78.85 ? 180 HIS A NE2 1 ATOM 1450 N N . PRO A 1 181 ? 43.198 -14.945 22.684 1.00 86.49 ? 181 PRO A N 1 ATOM 1451 C CA . PRO A 1 181 ? 43.199 -13.631 23.326 1.00 87.85 ? 181 PRO A CA 1 ATOM 1452 C C . PRO A 1 181 ? 44.582 -12.996 23.431 1.00 88.37 ? 181 PRO A C 1 ATOM 1453 O O . PRO A 1 181 ? 45.600 -13.668 23.254 1.00 87.52 ? 181 PRO A O 1 ATOM 1454 C CB . PRO A 1 181 ? 42.629 -13.907 24.728 1.00 90.64 ? 181 PRO A CB 1 ATOM 1455 C CG . PRO A 1 181 ? 42.400 -15.384 24.818 1.00 90.97 ? 181 PRO A CG 1 ATOM 1456 C CD . PRO A 1 181 ? 43.098 -16.034 23.665 1.00 89.16 ? 181 PRO A CD 1 ATOM 1457 N N . LYS A 1 182 ? 44.593 -11.703 23.729 1.00 89.09 ? 182 LYS A N 1 ATOM 1458 C CA . LYS A 1 182 ? 45.829 -10.924 23.803 1.00 91.46 ? 182 LYS A CA 1 ATOM 1459 C C . LYS A 1 182 ? 46.723 -11.228 25.020 1.00 93.44 ? 182 LYS A C 1 ATOM 1460 O O . LYS A 1 182 ? 47.948 -11.116 24.925 1.00 94.32 ? 182 LYS A O 1 ATOM 1461 C CB . LYS A 1 182 ? 45.503 -9.427 23.760 1.00 93.22 ? 182 LYS A CB 1 ATOM 1462 C CG . LYS A 1 182 ? 44.658 -8.922 24.922 1.00 96.28 ? 182 LYS A CG 1 ATOM 1463 C CD . LYS A 1 182 ? 44.283 -7.465 24.731 1.00 97.90 ? 182 LYS A CD 1 ATOM 1464 C CE . LYS A 1 182 ? 43.513 -6.930 25.925 1.00 100.54 ? 182 LYS A CE 1 ATOM 1465 N NZ . LYS A 1 182 ? 43.340 -5.453 25.840 1.00 101.70 ? 182 LYS A NZ 1 ATOM 1466 N N . ASP A 1 183 ? 46.127 -11.592 26.156 1.00 94.01 ? 183 ASP A N 1 ATOM 1467 C CA . ASP A 1 183 ? 46.912 -11.838 27.379 1.00 97.10 ? 183 ASP A CA 1 ATOM 1468 C C . ASP A 1 183 ? 46.236 -12.769 28.396 1.00 97.53 ? 183 ASP A C 1 ATOM 1469 O O . ASP A 1 183 ? 45.068 -13.129 28.252 1.00 96.12 ? 183 ASP A O 1 ATOM 1470 C CB . ASP A 1 183 ? 47.321 -10.501 28.043 1.00 98.39 ? 183 ASP A CB 1 ATOM 1471 C CG . ASP A 1 183 ? 46.127 -9.658 28.499 1.00 98.30 ? 183 ASP A CG 1 ATOM 1472 O OD1 . ASP A 1 183 ? 45.147 -10.214 29.039 1.00 98.79 ? 183 ASP A OD1 1 ATOM 1473 O OD2 . ASP A 1 183 ? 46.180 -8.420 28.335 1.00 97.66 ? 183 ASP A OD2 1 ATOM 1474 N N . ALA A 1 184 ? 46.999 -13.153 29.419 1.00 99.96 ? 184 ALA A N 1 ATOM 1475 C CA . ALA A 1 184 ? 46.510 -14.017 30.500 1.00 101.58 ? 184 ALA A CA 1 ATOM 1476 C C . ALA A 1 184 ? 45.283 -13.445 31.225 1.00 102.08 ? 184 ALA A C 1 ATOM 1477 O O . ALA A 1 184 ? 44.410 -14.202 31.663 1.00 102.20 ? 184 ALA A O 1 ATOM 1478 C CB . ALA A 1 184 ? 47.630 -14.288 31.497 1.00 103.71 ? 184 ALA A CB 1 ATOM 1479 N N . ALA A 1 185 ? 45.224 -12.118 31.349 1.00 102.19 ? 185 ALA A N 1 ATOM 1480 C CA . ALA A 1 185 ? 44.111 -11.443 32.025 1.00 102.81 ? 185 ALA A CA 1 ATOM 1481 C C . ALA A 1 185 ? 42.804 -11.615 31.259 1.00 100.88 ? 185 ALA A C 1 ATOM 1482 O O . ALA A 1 185 ? 41.774 -11.950 31.845 1.00 101.36 ? 185 ALA A O 1 ATOM 1483 C CB . ALA A 1 185 ? 44.415 -9.963 32.214 1.00 103.31 ? 185 ALA A CB 1 ATOM 1484 N N . GLU A 1 186 ? 42.851 -11.386 29.950 1.00 98.78 ? 186 GLU A N 1 ATOM 1485 C CA . GLU A 1 186 ? 41.659 -11.514 29.110 1.00 98.07 ? 186 GLU A CA 1 ATOM 1486 C C . GLU A 1 186 ? 41.122 -12.950 29.119 1.00 96.88 ? 186 GLU A C 1 ATOM 1487 O O . GLU A 1 186 ? 39.908 -13.162 29.154 1.00 95.41 ? 186 GLU A O 1 ATOM 1488 C CB . GLU A 1 186 ? 41.953 -11.058 27.674 1.00 96.89 ? 186 GLU A CB 1 ATOM 1489 C CG . GLU A 1 186 ? 40.728 -10.612 26.883 1.00 96.07 ? 186 GLU A CG 1 ATOM 1490 C CD . GLU A 1 186 ? 40.112 -9.311 27.385 1.00 98.54 ? 186 GLU A CD 1 ATOM 1491 O OE1 . GLU A 1 186 ? 40.698 -8.640 28.267 1.00 101.45 ? 186 GLU A OE1 1 ATOM 1492 O OE2 . GLU A 1 186 ? 39.022 -8.955 26.890 1.00 99.96 ? 186 GLU A OE2 1 ATOM 1493 N N . GLN A 1 187 ? 42.033 -13.923 29.105 1.00 96.99 ? 187 GLN A N 1 ATOM 1494 C CA . GLN A 1 187 ? 41.669 -15.342 29.178 1.00 97.14 ? 187 GLN A CA 1 ATOM 1495 C C . GLN A 1 187 ? 40.781 -15.622 30.387 1.00 99.22 ? 187 GLN A C 1 ATOM 1496 O O . GLN A 1 187 ? 39.688 -16.177 30.240 1.00 98.24 ? 187 GLN A O 1 ATOM 1497 C CB . GLN A 1 187 ? 42.928 -16.222 29.226 1.00 98.05 ? 187 GLN A CB 1 ATOM 1498 C CG . GLN A 1 187 ? 42.680 -17.717 29.430 1.00 98.64 ? 187 GLN A CG 1 ATOM 1499 C CD . GLN A 1 187 ? 41.899 -18.362 28.295 1.00 96.06 ? 187 GLN A CD 1 ATOM 1500 O OE1 . GLN A 1 187 ? 42.235 -18.204 27.120 1.00 92.81 ? 187 GLN A OE1 1 ATOM 1501 N NE2 . GLN A 1 187 ? 40.858 -19.109 28.646 1.00 96.48 ? 187 GLN A NE2 1 ATOM 1502 N N . THR A 1 188 ? 41.247 -15.238 31.575 1.00 101.28 ? 188 THR A N 1 ATOM 1503 C CA . THR A 1 188 ? 40.454 -15.436 32.788 1.00 103.59 ? 188 THR A CA 1 ATOM 1504 C C . THR A 1 188 ? 39.241 -14.497 32.783 1.00 103.25 ? 188 THR A C 1 ATOM 1505 O O . THR A 1 188 ? 38.141 -14.905 33.153 1.00 104.00 ? 188 THR A O 1 ATOM 1506 C CB . THR A 1 188 ? 41.281 -15.278 34.092 1.00 106.71 ? 188 THR A CB 1 ATOM 1507 O OG1 . THR A 1 188 ? 41.697 -13.918 34.259 1.00 107.37 ? 188 THR A OG1 1 ATOM 1508 C CG2 . THR A 1 188 ? 42.505 -16.193 34.077 1.00 107.09 ? 188 THR A CG2 1 ATOM 1509 N N . LYS A 1 189 ? 39.431 -13.260 32.329 1.00 102.08 ? 189 LYS A N 1 ATOM 1510 C CA . LYS A 1 189 ? 38.339 -12.285 32.276 1.00 102.53 ? 189 LYS A CA 1 ATOM 1511 C C . LYS A 1 189 ? 37.142 -12.785 31.465 1.00 100.80 ? 189 LYS A C 1 ATOM 1512 O O . LYS A 1 189 ? 35.998 -12.589 31.869 1.00 100.68 ? 189 LYS A O 1 ATOM 1513 C CB . LYS A 1 189 ? 38.834 -10.961 31.694 1.00 102.88 ? 189 LYS A CB 1 ATOM 1514 C CG . LYS A 1 189 ? 37.763 -9.888 31.568 1.00 104.71 ? 189 LYS A CG 1 ATOM 1515 C CD . LYS A 1 189 ? 38.340 -8.601 31.004 1.00 105.43 ? 189 LYS A CD 1 ATOM 1516 C CE . LYS A 1 189 ? 37.245 -7.606 30.661 1.00 106.31 ? 189 LYS A CE 1 ATOM 1517 N NZ . LYS A 1 189 ? 37.788 -6.425 29.937 1.00 106.15 ? 189 LYS A NZ 1 ATOM 1518 N N . LEU A 1 190 ? 37.413 -13.420 30.327 1.00 98.49 ? 190 LEU A N 1 ATOM 1519 C CA . LEU A 1 190 ? 36.357 -13.910 29.435 1.00 97.84 ? 190 LEU A CA 1 ATOM 1520 C C . LEU A 1 190 ? 35.911 -15.335 29.757 1.00 99.89 ? 190 LEU A C 1 ATOM 1521 O O . LEU A 1 190 ? 34.720 -15.647 29.671 1.00 99.82 ? 190 LEU A O 1 ATOM 1522 C CB . LEU A 1 190 ? 36.818 -13.859 27.973 1.00 93.90 ? 190 LEU A CB 1 ATOM 1523 C CG . LEU A 1 190 ? 37.120 -12.478 27.391 1.00 92.53 ? 190 LEU A CG 1 ATOM 1524 C CD1 . LEU A 1 190 ? 37.647 -12.625 25.974 1.00 89.60 ? 190 LEU A CD1 1 ATOM 1525 C CD2 . LEU A 1 190 ? 35.893 -11.578 27.421 1.00 92.80 ? 190 LEU A CD2 1 ATOM 1526 N N . TYR A 1 191 ? 36.864 -16.196 30.112 1.00 101.78 ? 191 TYR A N 1 ATOM 1527 C CA . TYR A 1 191 ? 36.603 -17.637 30.217 1.00 103.05 ? 191 TYR A CA 1 ATOM 1528 C C . TYR A 1 191 ? 36.947 -18.292 31.567 1.00 107.39 ? 191 TYR A C 1 ATOM 1529 O O . TYR A 1 191 ? 36.735 -19.496 31.726 1.00 110.29 ? 191 TYR A O 1 ATOM 1530 C CB . TYR A 1 191 ? 37.361 -18.367 29.104 1.00 100.63 ? 191 TYR A CB 1 ATOM 1531 C CG . TYR A 1 191 ? 37.254 -17.695 27.753 1.00 97.17 ? 191 TYR A CG 1 ATOM 1532 C CD1 . TYR A 1 191 ? 36.045 -17.668 27.062 1.00 96.19 ? 191 TYR A CD1 1 ATOM 1533 C CD2 . TYR A 1 191 ? 38.354 -17.071 27.174 1.00 95.04 ? 191 TYR A CD2 1 ATOM 1534 C CE1 . TYR A 1 191 ? 35.939 -17.050 25.825 1.00 92.93 ? 191 TYR A CE1 1 ATOM 1535 C CE2 . TYR A 1 191 ? 38.255 -16.448 25.943 1.00 92.20 ? 191 TYR A CE2 1 ATOM 1536 C CZ . TYR A 1 191 ? 37.044 -16.442 25.274 1.00 90.58 ? 191 TYR A CZ 1 ATOM 1537 O OH . TYR A 1 191 ? 36.933 -15.824 24.055 1.00 87.26 ? 191 TYR A OH 1 ATOM 1538 N N . GLN A 1 192 ? 37.468 -17.524 32.525 1.00 108.23 ? 192 GLN A N 1 ATOM 1539 C CA . GLN A 1 192 ? 37.904 -18.057 33.831 1.00 111.28 ? 192 GLN A CA 1 ATOM 1540 C C . GLN A 1 192 ? 39.110 -18.996 33.755 1.00 110.95 ? 192 GLN A C 1 ATOM 1541 O O . GLN A 1 192 ? 40.203 -18.660 34.229 1.00 111.03 ? 192 GLN A O 1 ATOM 1542 C CB . GLN A 1 192 ? 36.757 -18.775 34.560 1.00 113.76 ? 192 GLN A CB 1 ATOM 1543 C CG . GLN A 1 192 ? 35.667 -17.852 35.069 1.00 114.55 ? 192 GLN A CG 1 ATOM 1544 C CD . GLN A 1 192 ? 35.928 -17.368 36.476 1.00 116.38 ? 192 GLN A CD 1 ATOM 1545 O OE1 . GLN A 1 192 ? 36.649 -16.398 36.688 1.00 116.05 ? 192 GLN A OE1 1 ATOM 1546 N NE2 . GLN A 1 192 ? 35.342 -18.045 37.446 1.00 119.88 ? 192 GLN A NE2 1 ATOM 1547 N N . ASN A 1 193 ? 38.894 -20.175 33.176 1.00 109.56 ? 193 ASN A N 1 ATOM 1548 C CA . ASN A 1 193 ? 39.903 -21.229 33.144 1.00 110.15 ? 193 ASN A CA 1 ATOM 1549 C C . ASN A 1 193 ? 41.155 -20.767 32.408 1.00 108.33 ? 193 ASN A C 1 ATOM 1550 O O . ASN A 1 193 ? 41.060 -20.265 31.292 1.00 104.47 ? 193 ASN A O 1 ATOM 1551 C CB . ASN A 1 193 ? 39.332 -22.482 32.483 1.00 109.39 ? 193 ASN A CB 1 ATOM 1552 C CG . ASN A 1 193 ? 38.062 -22.968 33.162 1.00 111.74 ? 193 ASN A CG 1 ATOM 1553 O OD1 . ASN A 1 193 ? 38.100 -23.459 34.290 1.00 115.17 ? 193 ASN A OD1 1 ATOM 1554 N ND2 . ASN A 1 193 ? 36.928 -22.817 32.482 1.00 109.80 ? 193 ASN A ND2 1 ATOM 1555 N N . PRO A 1 194 ? 42.332 -20.912 33.041 1.00 111.26 ? 194 PRO A N 1 ATOM 1556 C CA . PRO A 1 194 ? 43.562 -20.428 32.422 1.00 110.23 ? 194 PRO A CA 1 ATOM 1557 C C . PRO A 1 194 ? 43.983 -21.290 31.235 1.00 108.30 ? 194 PRO A C 1 ATOM 1558 O O . PRO A 1 194 ? 44.470 -20.762 30.237 1.00 105.48 ? 194 PRO A O 1 ATOM 1559 C CB . PRO A 1 194 ? 44.585 -20.523 33.556 1.00 113.77 ? 194 PRO A CB 1 ATOM 1560 C CG . PRO A 1 194 ? 44.090 -21.636 34.412 1.00 116.18 ? 194 PRO A CG 1 ATOM 1561 C CD . PRO A 1 194 ? 42.591 -21.605 34.317 1.00 114.99 ? 194 PRO A CD 1 ATOM 1562 N N . THR A 1 195 ? 43.785 -22.602 31.352 1.00 109.52 ? 195 THR A N 1 ATOM 1563 C CA . THR A 1 195 ? 44.109 -23.546 30.293 1.00 107.95 ? 195 THR A CA 1 ATOM 1564 C C . THR A 1 195 ? 42.818 -24.114 29.725 1.00 106.22 ? 195 THR A C 1 ATOM 1565 O O . THR A 1 195 ? 42.003 -24.662 30.463 1.00 108.54 ? 195 THR A O 1 ATOM 1566 C CB . THR A 1 195 ? 44.968 -24.701 30.835 1.00 110.38 ? 195 THR A CB 1 ATOM 1567 O OG1 . THR A 1 195 ? 46.158 -24.169 31.423 1.00 111.06 ? 195 THR A OG1 1 ATOM 1568 C CG2 . THR A 1 195 ? 45.346 -25.674 29.722 1.00 110.06 ? 195 THR A CG2 1 ATOM 1569 N N . THR A 1 196 ? 42.630 -23.979 28.417 1.00 103.00 ? 196 THR A N 1 ATOM 1570 C CA . THR A 1 196 ? 41.394 -24.418 27.778 1.00 101.19 ? 196 THR A CA 1 ATOM 1571 C C . THR A 1 196 ? 41.672 -25.129 26.465 1.00 98.50 ? 196 THR A C 1 ATOM 1572 O O . THR A 1 196 ? 42.818 -25.227 26.025 1.00 96.91 ? 196 THR A O 1 ATOM 1573 C CB . THR A 1 196 ? 40.465 -23.223 27.505 1.00 99.90 ? 196 THR A CB 1 ATOM 1574 O OG1 . THR A 1 196 ? 41.130 -22.299 26.636 1.00 98.15 ? 196 THR A OG1 1 ATOM 1575 C CG2 . THR A 1 196 ? 40.097 -22.519 28.800 1.00 102.11 ? 196 THR A CG2 1 ATOM 1576 N N . TYR A 1 197 ? 40.607 -25.626 25.847 1.00 97.65 ? 197 TYR A N 1 ATOM 1577 C CA . TYR A 1 197 ? 40.702 -26.337 24.584 1.00 95.18 ? 197 TYR A CA 1 ATOM 1578 C C . TYR A 1 197 ? 39.344 -26.425 23.920 1.00 95.13 ? 197 TYR A C 1 ATOM 1579 O O . TYR A 1 197 ? 38.323 -26.162 24.549 1.00 95.57 ? 197 TYR A O 1 ATOM 1580 C CB . TYR A 1 197 ? 41.216 -27.755 24.820 1.00 96.76 ? 197 TYR A CB 1 ATOM 1581 C CG . TYR A 1 197 ? 40.294 -28.607 25.671 1.00 98.36 ? 197 TYR A CG 1 ATOM 1582 C CD1 . TYR A 1 197 ? 40.216 -28.419 27.054 1.00 101.29 ? 197 TYR A CD1 1 ATOM 1583 C CD2 . TYR A 1 197 ? 39.500 -29.598 25.098 1.00 97.24 ? 197 TYR A CD2 1 ATOM 1584 C CE1 . TYR A 1 197 ? 39.378 -29.194 27.838 1.00 102.94 ? 197 TYR A CE1 1 ATOM 1585 C CE2 . TYR A 1 197 ? 38.660 -30.381 25.872 1.00 99.75 ? 197 TYR A CE2 1 ATOM 1586 C CZ . TYR A 1 197 ? 38.603 -30.174 27.244 1.00 103.19 ? 197 TYR A CZ 1 ATOM 1587 O OH . TYR A 1 197 ? 37.769 -30.944 28.024 1.00 104.68 ? 197 TYR A OH 1 ATOM 1588 N N . ILE A 1 198 ? 39.347 -26.782 22.640 1.00 94.58 ? 198 ILE A N 1 ATOM 1589 C CA . ILE A 1 198 ? 38.135 -27.185 21.940 1.00 94.99 ? 198 ILE A CA 1 ATOM 1590 C C . ILE A 1 198 ? 38.438 -28.497 21.228 1.00 95.44 ? 198 ILE A C 1 ATOM 1591 O O . ILE A 1 198 ? 39.362 -28.559 20.417 1.00 94.60 ? 198 ILE A O 1 ATOM 1592 C CB . ILE A 1 198 ? 37.692 -26.160 20.881 1.00 93.81 ? 198 ILE A CB 1 ATOM 1593 C CG1 . ILE A 1 198 ? 37.560 -24.761 21.481 1.00 93.12 ? 198 ILE A CG1 1 ATOM 1594 C CG2 . ILE A 1 198 ? 36.363 -26.584 20.266 1.00 94.56 ? 198 ILE A CG2 1 ATOM 1595 C CD1 . ILE A 1 198 ? 37.511 -23.675 20.427 1.00 90.75 ? 198 ILE A CD1 1 ATOM 1596 N N . SER A 1 199 ? 37.674 -29.541 21.536 1.00 96.22 ? 199 SER A N 1 ATOM 1597 C CA . SER A 1 199 ? 37.845 -30.826 20.871 1.00 96.01 ? 199 SER A CA 1 ATOM 1598 C C . SER A 1 199 ? 36.640 -31.088 19.982 1.00 93.47 ? 199 SER A C 1 ATOM 1599 O O . SER A 1 199 ? 35.498 -30.997 20.425 1.00 92.59 ? 199 SER A O 1 ATOM 1600 C CB . SER A 1 199 ? 38.040 -31.952 21.891 1.00 99.43 ? 199 SER A CB 1 ATOM 1601 O OG . SER A 1 199 ? 36.829 -32.284 22.534 1.00 101.58 ? 199 SER A OG 1 ATOM 1602 N N . VAL A 1 200 ? 36.910 -31.396 18.719 1.00 92.63 ? 200 VAL A N 1 ATOM 1603 C CA . VAL A 1 200 ? 35.865 -31.603 17.725 1.00 91.41 ? 200 VAL A CA 1 ATOM 1604 C C . VAL A 1 200 ? 36.083 -32.951 17.064 1.00 92.22 ? 200 VAL A C 1 ATOM 1605 O O . VAL A 1 200 ? 37.212 -33.299 16.712 1.00 92.04 ? 200 VAL A O 1 ATOM 1606 C CB . VAL A 1 200 ? 35.888 -30.510 16.635 1.00 88.97 ? 200 VAL A CB 1 ATOM 1607 C CG1 . VAL A 1 200 ? 34.548 -30.449 15.918 1.00 88.91 ? 200 VAL A CG1 1 ATOM 1608 C CG2 . VAL A 1 200 ? 36.229 -29.151 17.231 1.00 88.10 ? 200 VAL A CG2 1 ATOM 1609 N N . GLY A 1 201 ? 35.005 -33.709 16.895 1.00 93.87 ? 201 GLY A N 1 ATOM 1610 C CA . GLY A 1 201 ? 35.091 -35.013 16.250 1.00 95.76 ? 201 GLY A CA 1 ATOM 1611 C C . GLY A 1 201 ? 33.869 -35.362 15.422 1.00 95.49 ? 201 GLY A C 1 ATOM 1612 O O . GLY A 1 201 ? 32.743 -35.024 15.785 1.00 95.84 ? 201 GLY A O 1 ATOM 1613 N N . THR A 1 202 ? 34.109 -36.023 14.294 1.00 95.36 ? 202 THR A N 1 ATOM 1614 C CA . THR A 1 202 ? 33.054 -36.643 13.495 1.00 95.95 ? 202 THR A CA 1 ATOM 1615 C C . THR A 1 202 ? 33.512 -38.063 13.213 1.00 99.18 ? 202 THR A C 1 ATOM 1616 O O . THR A 1 202 ? 34.355 -38.605 13.938 1.00 100.69 ? 202 THR A O 1 ATOM 1617 C CB . THR A 1 202 ? 32.798 -35.897 12.164 1.00 92.28 ? 202 THR A CB 1 ATOM 1618 O OG1 . THR A 1 202 ? 33.923 -36.054 11.289 1.00 90.20 ? 202 THR A OG1 1 ATOM 1619 C CG2 . THR A 1 202 ? 32.545 -34.431 12.409 1.00 90.07 ? 202 THR A CG2 1 ATOM 1620 N N . SER A 1 203 ? 32.961 -38.670 12.170 1.00 100.71 ? 203 SER A N 1 ATOM 1621 C CA . SER A 1 203 ? 33.408 -39.984 11.748 1.00 104.50 ? 203 SER A CA 1 ATOM 1622 C C . SER A 1 203 ? 34.842 -39.920 11.231 1.00 103.82 ? 203 SER A C 1 ATOM 1623 O O . SER A 1 203 ? 35.638 -40.821 11.489 1.00 106.46 ? 203 SER A O 1 ATOM 1624 C CB . SER A 1 203 ? 32.489 -40.538 10.666 1.00 105.67 ? 203 SER A CB 1 ATOM 1625 O OG . SER A 1 203 ? 32.694 -41.927 10.526 1.00 109.70 ? 203 SER A OG 1 ATOM 1626 N N . THR A 1 204 ? 35.164 -38.850 10.508 1.00 101.22 ? 204 THR A N 1 ATOM 1627 C CA . THR A 1 204 ? 36.494 -38.673 9.922 1.00 99.99 ? 204 THR A CA 1 ATOM 1628 C C . THR A 1 204 ? 37.385 -37.712 10.712 1.00 99.34 ? 204 THR A C 1 ATOM 1629 O O . THR A 1 204 ? 38.610 -37.807 10.635 1.00 100.52 ? 204 THR A O 1 ATOM 1630 C CB . THR A 1 204 ? 36.398 -38.137 8.482 1.00 96.94 ? 204 THR A CB 1 ATOM 1631 O OG1 . THR A 1 204 ? 35.856 -36.808 8.499 1.00 93.31 ? 204 THR A OG1 1 ATOM 1632 C CG2 . THR A 1 204 ? 35.518 -39.042 7.625 1.00 97.97 ? 204 THR A CG2 1 ATOM 1633 N N . LEU A 1 205 ? 36.775 -36.790 11.457 1.00 97.77 ? 205 LEU A N 1 ATOM 1634 C CA . LEU A 1 205 ? 37.517 -35.710 12.112 1.00 96.93 ? 205 LEU A CA 1 ATOM 1635 C C . LEU A 1 205 ? 37.942 -36.048 13.553 1.00 97.26 ? 205 LEU A C 1 ATOM 1636 O O . LEU A 1 205 ? 37.176 -36.640 14.322 1.00 97.05 ? 205 LEU A O 1 ATOM 1637 C CB . LEU A 1 205 ? 36.682 -34.423 12.091 1.00 96.36 ? 205 LEU A CB 1 ATOM 1638 C CG . LEU A 1 205 ? 37.381 -33.120 12.493 1.00 96.16 ? 205 LEU A CG 1 ATOM 1639 C CD1 . LEU A 1 205 ? 38.621 -32.861 11.648 1.00 94.79 ? 205 LEU A CD1 1 ATOM 1640 C CD2 . LEU A 1 205 ? 36.408 -31.958 12.373 1.00 94.80 ? 205 LEU A CD2 1 ATOM 1641 N N . ASN A 1 206 ? 39.174 -35.664 13.896 1.00 95.07 ? 206 ASN A N 1 ATOM 1642 C CA . ASN A 1 206 ? 39.750 -35.908 15.218 1.00 95.93 ? 206 ASN A CA 1 ATOM 1643 C C . ASN A 1 206 ? 40.558 -34.684 15.662 1.00 94.17 ? 206 ASN A C 1 ATOM 1644 O O . ASN A 1 206 ? 41.781 -34.736 15.789 1.00 94.90 ? 206 ASN A O 1 ATOM 1645 C CB . ASN A 1 206 ? 40.623 -37.171 15.188 1.00 97.75 ? 206 ASN A CB 1 ATOM 1646 C CG . ASN A 1 206 ? 41.101 -37.605 16.570 1.00 99.61 ? 206 ASN A CG 1 ATOM 1647 O OD1 . ASN A 1 206 ? 40.769 -37.000 17.592 1.00 99.50 ? 206 ASN A OD1 1 ATOM 1648 N ND2 . ASN A 1 206 ? 41.893 -38.665 16.599 1.00 101.51 ? 206 ASN A ND2 1 ATOM 1649 N N . GLN A 1 207 ? 39.852 -33.589 15.913 1.00 91.81 ? 207 GLN A N 1 ATOM 1650 C CA . GLN A 1 207 ? 40.480 -32.302 16.165 1.00 90.32 ? 207 GLN A CA 1 ATOM 1651 C C . GLN A 1 207 ? 40.546 -31.980 17.658 1.00 92.16 ? 207 GLN A C 1 ATOM 1652 O O . GLN A 1 207 ? 39.721 -32.435 18.448 1.00 92.27 ? 207 GLN A O 1 ATOM 1653 C CB . GLN A 1 207 ? 39.702 -31.219 15.420 1.00 88.01 ? 207 GLN A CB 1 ATOM 1654 C CG . GLN A 1 207 ? 40.267 -29.818 15.544 1.00 86.95 ? 207 GLN A CG 1 ATOM 1655 C CD . GLN A 1 207 ? 39.418 -28.796 14.823 1.00 85.38 ? 207 GLN A CD 1 ATOM 1656 O OE1 . GLN A 1 207 ? 38.668 -28.043 15.447 1.00 87.13 ? 207 GLN A OE1 1 ATOM 1657 N NE2 . GLN A 1 207 ? 39.525 -28.765 13.504 1.00 84.37 ? 207 GLN A NE2 1 ATOM 1658 N N . ARG A 1 208 ? 41.548 -31.193 18.031 1.00 92.73 ? 208 ARG A N 1 ATOM 1659 C CA . ARG A 1 208 ? 41.664 -30.667 19.381 1.00 94.59 ? 208 ARG A CA 1 ATOM 1660 C C . ARG A 1 208 ? 42.500 -29.394 19.350 1.00 93.97 ? 208 ARG A C 1 ATOM 1661 O O . ARG A 1 208 ? 43.721 -29.451 19.226 1.00 94.52 ? 208 ARG A O 1 ATOM 1662 C CB . ARG A 1 208 ? 42.308 -31.694 20.305 1.00 98.86 ? 208 ARG A CB 1 ATOM 1663 C CG . ARG A 1 208 ? 42.403 -31.249 21.758 1.00 101.41 ? 208 ARG A CG 1 ATOM 1664 C CD . ARG A 1 208 ? 43.476 -32.023 22.508 1.00 105.12 ? 208 ARG A CD 1 ATOM 1665 N NE . ARG A 1 208 ? 43.773 -31.414 23.803 1.00 106.60 ? 208 ARG A NE 1 ATOM 1666 C CZ . ARG A 1 208 ? 43.016 -31.530 24.891 1.00 108.33 ? 208 ARG A CZ 1 ATOM 1667 N NH1 . ARG A 1 208 ? 41.888 -32.241 24.871 1.00 108.25 ? 208 ARG A NH1 1 ATOM 1668 N NH2 . ARG A 1 208 ? 43.389 -30.925 26.014 1.00 110.11 ? 208 ARG A NH2 1 ATOM 1669 N N . LEU A 1 209 ? 41.834 -28.250 19.469 1.00 93.65 ? 209 LEU A N 1 ATOM 1670 C CA . LEU A 1 209 ? 42.491 -26.948 19.375 1.00 92.17 ? 209 LEU A CA 1 ATOM 1671 C C . LEU A 1 209 ? 42.812 -26.425 20.767 1.00 92.87 ? 209 LEU A C 1 ATOM 1672 O O . LEU A 1 209 ? 42.104 -26.732 21.719 1.00 93.54 ? 209 LEU A O 1 ATOM 1673 C CB . LEU A 1 209 ? 41.580 -25.947 18.658 1.00 90.32 ? 209 LEU A CB 1 ATOM 1674 C CG . LEU A 1 209 ? 40.880 -26.415 17.375 1.00 88.84 ? 209 LEU A CG 1 ATOM 1675 C CD1 . LEU A 1 209 ? 39.839 -25.396 16.936 1.00 87.02 ? 209 LEU A CD1 1 ATOM 1676 C CD2 . LEU A 1 209 ? 41.895 -26.668 16.271 1.00 88.64 ? 209 LEU A CD2 1 ATOM 1677 N N . VAL A 1 210 ? 43.884 -25.643 20.872 1.00 93.37 ? 210 VAL A N 1 ATOM 1678 C CA . VAL A 1 210 ? 44.225 -24.920 22.100 1.00 95.35 ? 210 VAL A CA 1 ATOM 1679 C C . VAL A 1 210 ? 44.539 -23.462 21.751 1.00 94.10 ? 210 VAL A C 1 ATOM 1680 O O . VAL A 1 210 ? 45.247 -23.201 20.771 1.00 93.60 ? 210 VAL A O 1 ATOM 1681 C CB . VAL A 1 210 ? 45.424 -25.544 22.860 1.00 98.29 ? 210 VAL A CB 1 ATOM 1682 C CG1 . VAL A 1 210 ? 45.031 -26.878 23.476 1.00 100.64 ? 210 VAL A CG1 1 ATOM 1683 C CG2 . VAL A 1 210 ? 46.645 -25.706 21.962 1.00 98.17 ? 210 VAL A CG2 1 ATOM 1684 N N . PRO A 1 211 ? 44.009 -22.505 22.539 1.00 93.19 ? 211 PRO A N 1 ATOM 1685 C CA . PRO A 1 211 ? 44.315 -21.111 22.225 1.00 91.33 ? 211 PRO A CA 1 ATOM 1686 C C . PRO A 1 211 ? 45.783 -20.779 22.465 1.00 92.37 ? 211 PRO A C 1 ATOM 1687 O O . PRO A 1 211 ? 46.352 -21.197 23.471 1.00 93.97 ? 211 PRO A O 1 ATOM 1688 C CB . PRO A 1 211 ? 43.430 -20.310 23.194 1.00 91.60 ? 211 PRO A CB 1 ATOM 1689 C CG . PRO A 1 211 ? 42.487 -21.281 23.805 1.00 92.16 ? 211 PRO A CG 1 ATOM 1690 C CD . PRO A 1 211 ? 43.118 -22.631 23.705 1.00 93.65 ? 211 PRO A CD 1 ATOM 1691 N N . ARG A 1 212 ? 46.392 -20.070 21.523 1.00 91.34 ? 212 ARG A N 1 ATOM 1692 C CA . ARG A 1 212 ? 47.709 -19.498 21.723 1.00 94.10 ? 212 ARG A CA 1 ATOM 1693 C C . ARG A 1 212 ? 47.564 -18.053 22.180 1.00 94.74 ? 212 ARG A C 1 ATOM 1694 O O . ARG A 1 212 ? 47.073 -17.210 21.426 1.00 92.61 ? 212 ARG A O 1 ATOM 1695 C CB . ARG A 1 212 ? 48.529 -19.580 20.435 1.00 93.44 ? 212 ARG A CB 1 ATOM 1696 C CG . ARG A 1 212 ? 48.892 -21.006 20.038 1.00 94.10 ? 212 ARG A CG 1 ATOM 1697 C CD . ARG A 1 212 ? 48.023 -21.519 18.911 1.00 92.21 ? 212 ARG A CD 1 ATOM 1698 N NE . ARG A 1 212 ? 48.374 -20.865 17.654 1.00 90.83 ? 212 ARG A NE 1 ATOM 1699 C CZ . ARG A 1 212 ? 47.659 -20.938 16.536 1.00 89.61 ? 212 ARG A CZ 1 ATOM 1700 N NH1 . ARG A 1 212 ? 46.533 -21.642 16.487 1.00 87.85 ? 212 ARG A NH1 1 ATOM 1701 N NH2 . ARG A 1 212 ? 48.077 -20.300 15.450 1.00 91.59 ? 212 ARG A NH2 1 ATOM 1702 N N . ILE A 1 213 ? 47.980 -17.786 23.419 1.00 98.09 ? 213 ILE A N 1 ATOM 1703 C CA . ILE A 1 213 ? 47.927 -16.445 24.001 1.00 99.92 ? 213 ILE A CA 1 ATOM 1704 C C . ILE A 1 213 ? 49.205 -15.690 23.656 1.00 100.63 ? 213 ILE A C 1 ATOM 1705 O O . ILE A 1 213 ? 50.306 -16.185 23.878 1.00 103.11 ? 213 ILE A O 1 ATOM 1706 C CB . ILE A 1 213 ? 47.772 -16.477 25.543 1.00 103.60 ? 213 ILE A CB 1 ATOM 1707 C CG1 . ILE A 1 213 ? 46.458 -17.165 25.953 1.00 104.61 ? 213 ILE A CG1 1 ATOM 1708 C CG2 . ILE A 1 213 ? 47.840 -15.066 26.123 1.00 104.18 ? 213 ILE A CG2 1 ATOM 1709 C CD1 . ILE A 1 213 ? 46.591 -18.645 26.257 1.00 106.23 ? 213 ILE A CD1 1 ATOM 1710 N N . ALA A 1 214 ? 49.042 -14.486 23.119 1.00 99.79 ? 214 ALA A N 1 ATOM 1711 C CA . ALA A 1 214 ? 50.167 -13.634 22.754 1.00 100.24 ? 214 ALA A CA 1 ATOM 1712 C C . ALA A 1 214 ? 49.659 -12.241 22.397 1.00 99.80 ? 214 ALA A C 1 ATOM 1713 O O . ALA A 1 214 ? 48.558 -12.083 21.867 1.00 98.25 ? 214 ALA A O 1 ATOM 1714 C CB . ALA A 1 214 ? 50.939 -14.234 21.583 1.00 99.16 ? 214 ALA A CB 1 ATOM 1715 N N . THR A 1 215 ? 50.463 -11.231 22.702 1.00 102.76 ? 215 THR A N 1 ATOM 1716 C CA . THR A 1 215 ? 50.165 -9.864 22.293 1.00 102.23 ? 215 THR A CA 1 ATOM 1717 C C . THR A 1 215 ? 50.627 -9.689 20.844 1.00 99.83 ? 215 THR A C 1 ATOM 1718 O O . THR A 1 215 ? 51.764 -10.017 20.497 1.00 101.18 ? 215 THR A O 1 ATOM 1719 C CB . THR A 1 215 ? 50.853 -8.838 23.219 1.00 105.35 ? 215 THR A CB 1 ATOM 1720 O OG1 . THR A 1 215 ? 52.261 -9.105 23.270 1.00 107.47 ? 215 THR A OG1 1 ATOM 1721 C CG2 . THR A 1 215 ? 50.272 -8.910 24.638 1.00 105.67 ? 215 THR A CG2 1 ATOM 1722 N N . ARG A 1 216 ? 49.731 -9.189 20.001 1.00 97.17 ? 216 ARG A N 1 ATOM 1723 C CA . ARG A 1 216 ? 49.987 -9.067 18.572 1.00 95.23 ? 216 ARG A CA 1 ATOM 1724 C C . ARG A 1 216 ? 49.684 -7.656 18.087 1.00 94.56 ? 216 ARG A C 1 ATOM 1725 O O . ARG A 1 216 ? 49.075 -6.863 18.802 1.00 94.22 ? 216 ARG A O 1 ATOM 1726 C CB . ARG A 1 216 ? 49.113 -10.065 17.811 1.00 93.08 ? 216 ARG A CB 1 ATOM 1727 C CG . ARG A 1 216 ? 49.472 -11.524 18.051 1.00 93.32 ? 216 ARG A CG 1 ATOM 1728 C CD . ARG A 1 216 ? 48.352 -12.448 17.601 1.00 91.14 ? 216 ARG A CD 1 ATOM 1729 N NE . ARG A 1 216 ? 47.380 -12.680 18.669 1.00 91.68 ? 216 ARG A NE 1 ATOM 1730 C CZ . ARG A 1 216 ? 47.356 -13.742 19.479 1.00 92.05 ? 216 ARG A CZ 1 ATOM 1731 N NH1 . ARG A 1 216 ? 48.249 -14.722 19.367 1.00 93.52 ? 216 ARG A NH1 1 ATOM 1732 N NH2 . ARG A 1 216 ? 46.418 -13.828 20.414 1.00 91.61 ? 216 ARG A NH2 1 ATOM 1733 N N . SER A 1 217 ? 50.106 -7.349 16.865 1.00 94.82 ? 217 SER A N 1 ATOM 1734 C CA . SER A 1 217 ? 49.772 -6.078 16.231 1.00 95.50 ? 217 SER A CA 1 ATOM 1735 C C . SER A 1 217 ? 48.258 -5.896 16.194 1.00 94.14 ? 217 SER A C 1 ATOM 1736 O O . SER A 1 217 ? 47.519 -6.861 15.999 1.00 95.33 ? 217 SER A O 1 ATOM 1737 C CB . SER A 1 217 ? 50.334 -6.037 14.812 1.00 96.11 ? 217 SER A CB 1 ATOM 1738 O OG . SER A 1 217 ? 51.723 -6.316 14.817 1.00 100.32 ? 217 SER A OG 1 ATOM 1739 N N . LYS A 1 218 ? 47.794 -4.666 16.388 1.00 93.89 ? 218 LYS A N 1 ATOM 1740 C CA . LYS A 1 218 ? 46.356 -4.398 16.437 1.00 92.64 ? 218 LYS A CA 1 ATOM 1741 C C . LYS A 1 218 ? 45.761 -4.177 15.051 1.00 90.75 ? 218 LYS A C 1 ATOM 1742 O O . LYS A 1 218 ? 46.214 -3.318 14.302 1.00 91.97 ? 218 LYS A O 1 ATOM 1743 C CB . LYS A 1 218 ? 46.043 -3.213 17.356 1.00 94.28 ? 218 LYS A CB 1 ATOM 1744 C CG . LYS A 1 218 ? 45.753 -3.647 18.781 1.00 95.67 ? 218 LYS A CG 1 ATOM 1745 C CD . LYS A 1 218 ? 45.815 -2.493 19.763 1.00 98.72 ? 218 LYS A CD 1 ATOM 1746 C CE . LYS A 1 218 ? 45.686 -2.998 21.193 1.00 101.30 ? 218 LYS A CE 1 ATOM 1747 N NZ . LYS A 1 218 ? 46.385 -2.117 22.169 1.00 104.29 ? 218 LYS A NZ 1 ATOM 1748 N N . VAL A 1 219 ? 44.745 -4.968 14.724 1.00 88.56 ? 219 VAL A N 1 ATOM 1749 C CA . VAL A 1 219 ? 44.025 -4.849 13.463 1.00 86.20 ? 219 VAL A CA 1 ATOM 1750 C C . VAL A 1 219 ? 42.543 -4.660 13.775 1.00 84.57 ? 219 VAL A C 1 ATOM 1751 O O . VAL A 1 219 ? 41.947 -5.478 14.470 1.00 84.16 ? 219 VAL A O 1 ATOM 1752 C CB . VAL A 1 219 ? 44.218 -6.111 12.610 1.00 85.53 ? 219 VAL A CB 1 ATOM 1753 C CG1 . VAL A 1 219 ? 43.618 -5.912 11.225 1.00 84.32 ? 219 VAL A CG1 1 ATOM 1754 C CG2 . VAL A 1 219 ? 45.700 -6.470 12.536 1.00 86.27 ? 219 VAL A CG2 1 ATOM 1755 N N . ASN A 1 220 ? 41.958 -3.579 13.266 1.00 83.99 ? 220 ASN A N 1 ATOM 1756 C CA . ASN A 1 220 ? 40.616 -3.143 13.673 1.00 84.50 ? 220 ASN A CA 1 ATOM 1757 C C . ASN A 1 220 ? 40.496 -3.010 15.187 1.00 83.86 ? 220 ASN A C 1 ATOM 1758 O O . ASN A 1 220 ? 39.464 -3.343 15.774 1.00 83.71 ? 220 ASN A O 1 ATOM 1759 C CB . ASN A 1 220 ? 39.531 -4.089 13.144 1.00 84.93 ? 220 ASN A CB 1 ATOM 1760 C CG . ASN A 1 220 ? 39.485 -4.148 11.631 1.00 85.19 ? 220 ASN A CG 1 ATOM 1761 O OD1 . ASN A 1 220 ? 38.822 -5.012 11.064 1.00 86.77 ? 220 ASN A OD1 1 ATOM 1762 N ND2 . ASN A 1 220 ? 40.181 -3.232 10.970 1.00 86.58 ? 220 ASN A ND2 1 ATOM 1763 N N . GLY A 1 221 ? 41.564 -2.523 15.812 1.00 83.65 ? 221 GLY A N 1 ATOM 1764 C CA . GLY A 1 221 ? 41.603 -2.330 17.252 1.00 84.01 ? 221 GLY A CA 1 ATOM 1765 C C . GLY A 1 221 ? 41.755 -3.599 18.071 1.00 83.10 ? 221 GLY A C 1 ATOM 1766 O O . GLY A 1 221 ? 41.643 -3.545 19.293 1.00 85.63 ? 221 GLY A O 1 ATOM 1767 N N . GLN A 1 222 ? 42.032 -4.733 17.424 1.00 80.38 ? 222 GLN A N 1 ATOM 1768 C CA . GLN A 1 222 ? 42.123 -6.015 18.130 1.00 80.47 ? 222 GLN A CA 1 ATOM 1769 C C . GLN A 1 222 ? 43.523 -6.615 18.140 1.00 81.14 ? 222 GLN A C 1 ATOM 1770 O O . GLN A 1 222 ? 44.172 -6.736 17.101 1.00 81.19 ? 222 GLN A O 1 ATOM 1771 C CB . GLN A 1 222 ? 41.152 -7.035 17.531 1.00 78.79 ? 222 GLN A CB 1 ATOM 1772 C CG . GLN A 1 222 ? 39.701 -6.582 17.508 1.00 78.74 ? 222 GLN A CG 1 ATOM 1773 C CD . GLN A 1 222 ? 39.269 -5.901 18.794 1.00 80.05 ? 222 GLN A CD 1 ATOM 1774 O OE1 . GLN A 1 222 ? 39.451 -6.435 19.895 1.00 79.50 ? 222 GLN A OE1 1 ATOM 1775 N NE2 . GLN A 1 222 ? 38.696 -4.710 18.661 1.00 80.94 ? 222 GLN A NE2 1 ATOM 1776 N N . SER A 1 223 ? 43.963 -7.002 19.333 1.00 83.19 ? 223 SER A N 1 ATOM 1777 C CA . SER A 1 223 ? 45.232 -7.687 19.534 1.00 84.34 ? 223 SER A CA 1 ATOM 1778 C C . SER A 1 223 ? 45.024 -9.204 19.578 1.00 83.27 ? 223 SER A C 1 ATOM 1779 O O . SER A 1 223 ? 45.962 -9.972 19.370 1.00 85.23 ? 223 SER A O 1 ATOM 1780 C CB . SER A 1 223 ? 45.878 -7.199 20.833 1.00 87.28 ? 223 SER A CB 1 ATOM 1781 O OG . SER A 1 223 ? 47.042 -7.944 21.138 1.00 89.78 ? 223 SER A OG 1 ATOM 1782 N N . GLY A 1 224 ? 43.797 -9.629 19.865 1.00 81.92 ? 224 GLY A N 1 ATOM 1783 C CA . GLY A 1 224 ? 43.442 -11.040 19.830 1.00 80.07 ? 224 GLY A CA 1 ATOM 1784 C C . GLY A 1 224 ? 43.108 -11.463 18.418 1.00 77.40 ? 224 GLY A C 1 ATOM 1785 O O . GLY A 1 224 ? 43.023 -10.623 17.523 1.00 75.49 ? 224 GLY A O 1 ATOM 1786 N N . ARG A 1 225 ? 42.910 -12.766 18.223 1.00 77.04 ? 225 ARG A N 1 ATOM 1787 C CA . ARG A 1 225 ? 42.639 -13.327 16.898 1.00 76.66 ? 225 ARG A CA 1 ATOM 1788 C C . ARG A 1 225 ? 41.539 -14.381 16.936 1.00 76.08 ? 225 ARG A C 1 ATOM 1789 O O . ARG A 1 225 ? 41.262 -14.959 17.976 1.00 77.53 ? 225 ARG A O 1 ATOM 1790 C CB . ARG A 1 225 ? 43.910 -13.956 16.312 1.00 76.88 ? 225 ARG A CB 1 ATOM 1791 C CG . ARG A 1 225 ? 45.052 -12.985 16.057 1.00 78.06 ? 225 ARG A CG 1 ATOM 1792 C CD . ARG A 1 225 ? 44.788 -12.090 14.857 1.00 77.07 ? 225 ARG A CD 1 ATOM 1793 N NE . ARG A 1 225 ? 45.941 -11.234 14.569 1.00 78.31 ? 225 ARG A NE 1 ATOM 1794 C CZ . ARG A 1 225 ? 46.101 -9.978 14.991 1.00 79.37 ? 225 ARG A CZ 1 ATOM 1795 N NH1 . ARG A 1 225 ? 45.182 -9.368 15.736 1.00 79.46 ? 225 ARG A NH1 1 ATOM 1796 N NH2 . ARG A 1 225 ? 47.205 -9.321 14.658 1.00 81.00 ? 225 ARG A NH2 1 ATOM 1797 N N . MET A 1 226 ? 40.927 -14.622 15.781 1.00 75.58 ? 226 MET A N 1 ATOM 1798 C CA . MET A 1 226 ? 39.930 -15.670 15.622 1.00 76.83 ? 226 MET A CA 1 ATOM 1799 C C . MET A 1 226 ? 40.347 -16.593 14.476 1.00 77.73 ? 226 MET A C 1 ATOM 1800 O O . MET A 1 226 ? 40.488 -16.151 13.336 1.00 78.80 ? 226 MET A O 1 ATOM 1801 C CB . MET A 1 226 ? 38.568 -15.057 15.307 1.00 76.92 ? 226 MET A CB 1 ATOM 1802 C CG . MET A 1 226 ? 38.003 -14.168 16.404 1.00 79.29 ? 226 MET A CG 1 ATOM 1803 S SD . MET A 1 226 ? 37.127 -15.063 17.701 1.00 81.30 ? 226 MET A SD 1 ATOM 1804 C CE . MET A 1 226 ? 36.482 -13.682 18.641 1.00 83.60 ? 226 MET A CE 1 ATOM 1805 N N . GLU A 1 227 ? 40.544 -17.871 14.787 1.00 78.41 ? 227 GLU A N 1 ATOM 1806 C CA . GLU A 1 227 ? 40.926 -18.871 13.800 1.00 76.85 ? 227 GLU A CA 1 ATOM 1807 C C . GLU A 1 227 ? 39.707 -19.732 13.524 1.00 76.13 ? 227 GLU A C 1 ATOM 1808 O O . GLU A 1 227 ? 39.189 -20.384 14.426 1.00 77.37 ? 227 GLU A O 1 ATOM 1809 C CB . GLU A 1 227 ? 42.082 -19.723 14.330 1.00 79.08 ? 227 GLU A CB 1 ATOM 1810 C CG . GLU A 1 227 ? 42.743 -20.609 13.285 1.00 81.05 ? 227 GLU A CG 1 ATOM 1811 C CD . GLU A 1 227 ? 44.082 -21.163 13.741 1.00 83.74 ? 227 GLU A CD 1 ATOM 1812 O OE1 . GLU A 1 227 ? 44.356 -21.160 14.961 1.00 84.34 ? 227 GLU A OE1 1 ATOM 1813 O OE2 . GLU A 1 227 ? 44.869 -21.602 12.875 1.00 84.85 ? 227 GLU A OE2 1 ATOM 1814 N N . PHE A 1 228 ? 39.238 -19.723 12.281 1.00 74.45 ? 228 PHE A N 1 ATOM 1815 C CA . PHE A 1 228 ? 37.996 -20.404 11.942 1.00 73.35 ? 228 PHE A CA 1 ATOM 1816 C C . PHE A 1 228 ? 38.265 -21.709 11.217 1.00 72.86 ? 228 PHE A C 1 ATOM 1817 O O . PHE A 1 228 ? 39.192 -21.802 10.412 1.00 72.17 ? 228 PHE A O 1 ATOM 1818 C CB . PHE A 1 228 ? 37.109 -19.488 11.107 1.00 72.72 ? 228 PHE A CB 1 ATOM 1819 C CG . PHE A 1 228 ? 36.546 -18.336 11.887 1.00 74.02 ? 228 PHE A CG 1 ATOM 1820 C CD1 . PHE A 1 228 ? 35.400 -18.496 12.657 1.00 74.46 ? 228 PHE A CD1 1 ATOM 1821 C CD2 . PHE A 1 228 ? 37.173 -17.096 11.876 1.00 74.41 ? 228 PHE A CD2 1 ATOM 1822 C CE1 . PHE A 1 228 ? 34.884 -17.440 13.386 1.00 74.60 ? 228 PHE A CE1 1 ATOM 1823 C CE2 . PHE A 1 228 ? 36.659 -16.035 12.605 1.00 74.11 ? 228 PHE A CE2 1 ATOM 1824 C CZ . PHE A 1 228 ? 35.514 -16.208 13.362 1.00 74.16 ? 228 PHE A CZ 1 ATOM 1825 N N . PHE A 1 229 ? 37.449 -22.714 11.525 1.00 72.11 ? 229 PHE A N 1 ATOM 1826 C CA . PHE A 1 229 ? 37.571 -24.035 10.930 1.00 72.44 ? 229 PHE A CA 1 ATOM 1827 C C . PHE A 1 229 ? 36.242 -24.467 10.352 1.00 73.00 ? 229 PHE A C 1 ATOM 1828 O O . PHE A 1 229 ? 35.205 -23.874 10.641 1.00 72.88 ? 229 PHE A O 1 ATOM 1829 C CB . PHE A 1 229 ? 38.017 -25.054 11.970 1.00 73.89 ? 229 PHE A CB 1 ATOM 1830 C CG . PHE A 1 229 ? 39.397 -24.819 12.484 1.00 75.23 ? 229 PHE A CG 1 ATOM 1831 C CD1 . PHE A 1 229 ? 39.616 -23.943 13.537 1.00 76.31 ? 229 PHE A CD1 1 ATOM 1832 C CD2 . PHE A 1 229 ? 40.479 -25.468 11.916 1.00 76.82 ? 229 PHE A CD2 1 ATOM 1833 C CE1 . PHE A 1 229 ? 40.892 -23.718 14.018 1.00 77.24 ? 229 PHE A CE1 1 ATOM 1834 C CE2 . PHE A 1 229 ? 41.760 -25.248 12.389 1.00 78.42 ? 229 PHE A CE2 1 ATOM 1835 C CZ . PHE A 1 229 ? 41.967 -24.372 13.443 1.00 78.55 ? 229 PHE A CZ 1 ATOM 1836 N N . TRP A 1 230 ? 36.282 -25.513 9.536 1.00 74.13 ? 230 TRP A N 1 ATOM 1837 C CA . TRP A 1 230 ? 35.078 -26.036 8.918 1.00 73.67 ? 230 TRP A CA 1 ATOM 1838 C C . TRP A 1 230 ? 35.186 -27.521 8.663 1.00 74.72 ? 230 TRP A C 1 ATOM 1839 O O . TRP A 1 230 ? 36.266 -28.095 8.719 1.00 75.31 ? 230 TRP A O 1 ATOM 1840 C CB . TRP A 1 230 ? 34.816 -25.323 7.596 1.00 71.92 ? 230 TRP A CB 1 ATOM 1841 C CG . TRP A 1 230 ? 35.936 -25.461 6.603 1.00 71.12 ? 230 TRP A CG 1 ATOM 1842 C CD1 . TRP A 1 230 ? 37.052 -24.685 6.518 1.00 70.20 ? 230 TRP A CD1 1 ATOM 1843 C CD2 . TRP A 1 230 ? 36.041 -26.430 5.558 1.00 70.77 ? 230 TRP A CD2 1 ATOM 1844 N NE1 . TRP A 1 230 ? 37.843 -25.105 5.485 1.00 69.31 ? 230 TRP A NE1 1 ATOM 1845 C CE2 . TRP A 1 230 ? 37.247 -26.178 4.879 1.00 70.37 ? 230 TRP A CE2 1 ATOM 1846 C CE3 . TRP A 1 230 ? 35.229 -27.487 5.128 1.00 71.58 ? 230 TRP A CE3 1 ATOM 1847 C CZ2 . TRP A 1 230 ? 37.663 -26.941 3.788 1.00 71.87 ? 230 TRP A CZ2 1 ATOM 1848 C CZ3 . TRP A 1 230 ? 35.642 -28.247 4.047 1.00 72.08 ? 230 TRP A CZ3 1 ATOM 1849 C CH2 . TRP A 1 230 ? 36.849 -27.973 3.389 1.00 72.27 ? 230 TRP A CH2 1 ATOM 1850 N N . THR A 1 231 ? 34.042 -28.130 8.387 1.00 76.04 ? 231 THR A N 1 ATOM 1851 C CA . THR A 1 231 ? 33.992 -29.498 7.904 1.00 76.91 ? 231 THR A CA 1 ATOM 1852 C C . THR A 1 231 ? 32.697 -29.720 7.126 1.00 76.91 ? 231 THR A C 1 ATOM 1853 O O . THR A 1 231 ? 31.784 -28.896 7.176 1.00 76.03 ? 231 THR A O 1 ATOM 1854 C CB . THR A 1 231 ? 34.097 -30.506 9.062 1.00 78.51 ? 231 THR A CB 1 ATOM 1855 O OG1 . THR A 1 231 ? 34.294 -31.820 8.534 1.00 80.68 ? 231 THR A OG1 1 ATOM 1856 C CG2 . THR A 1 231 ? 32.837 -30.493 9.928 1.00 79.11 ? 231 THR A CG2 1 ATOM 1857 N N . ILE A 1 232 ? 32.641 -30.821 6.388 1.00 79.09 ? 232 ILE A N 1 ATOM 1858 C CA . ILE A 1 232 ? 31.416 -31.259 5.727 1.00 80.64 ? 232 ILE A CA 1 ATOM 1859 C C . ILE A 1 232 ? 30.894 -32.427 6.543 1.00 82.35 ? 232 ILE A C 1 ATOM 1860 O O . ILE A 1 232 ? 31.506 -33.490 6.580 1.00 84.58 ? 232 ILE A O 1 ATOM 1861 C CB . ILE A 1 232 ? 31.668 -31.653 4.242 1.00 80.74 ? 232 ILE A CB 1 ATOM 1862 C CG1 . ILE A 1 232 ? 31.415 -30.463 3.317 1.00 78.48 ? 232 ILE A CG1 1 ATOM 1863 C CG2 . ILE A 1 232 ? 30.750 -32.783 3.782 1.00 83.21 ? 232 ILE A CG2 1 ATOM 1864 C CD1 . ILE A 1 232 ? 32.090 -29.191 3.758 1.00 77.75 ? 232 ILE A CD1 1 ATOM 1865 N N . LEU A 1 233 ? 29.776 -32.214 7.221 1.00 83.74 ? 233 LEU A N 1 ATOM 1866 C CA . LEU A 1 233 ? 29.146 -33.267 8.004 1.00 85.92 ? 233 LEU A CA 1 ATOM 1867 C C . LEU A 1 233 ? 28.249 -34.076 7.079 1.00 87.76 ? 233 LEU A C 1 ATOM 1868 O O . LEU A 1 233 ? 27.264 -33.559 6.548 1.00 87.17 ? 233 LEU A O 1 ATOM 1869 C CB . LEU A 1 233 ? 28.335 -32.658 9.147 1.00 86.78 ? 233 LEU A CB 1 ATOM 1870 C CG . LEU A 1 233 ? 27.766 -33.598 10.211 1.00 89.80 ? 233 LEU A CG 1 ATOM 1871 C CD1 . LEU A 1 233 ? 28.859 -34.381 10.930 1.00 90.63 ? 233 LEU A CD1 1 ATOM 1872 C CD2 . LEU A 1 233 ? 26.947 -32.785 11.201 1.00 90.12 ? 233 LEU A CD2 1 ATOM 1873 N N . LYS A 1 234 ? 28.600 -35.341 6.882 1.00 90.35 ? 234 LYS A N 1 ATOM 1874 C CA . LYS A 1 234 ? 27.865 -36.218 5.969 1.00 93.88 ? 234 LYS A CA 1 ATOM 1875 C C . LYS A 1 234 ? 26.454 -36.526 6.490 1.00 96.25 ? 234 LYS A C 1 ATOM 1876 O O . LYS A 1 234 ? 26.147 -36.241 7.653 1.00 96.48 ? 234 LYS A O 1 ATOM 1877 C CB . LYS A 1 234 ? 28.672 -37.501 5.737 1.00 97.26 ? 234 LYS A CB 1 ATOM 1878 C CG . LYS A 1 234 ? 29.768 -37.331 4.694 1.00 97.66 ? 234 LYS A CG 1 ATOM 1879 C CD . LYS A 1 234 ? 30.845 -38.396 4.821 1.00 100.95 ? 234 LYS A CD 1 ATOM 1880 C CE . LYS A 1 234 ? 31.981 -38.162 3.833 1.00 101.26 ? 234 LYS A CE 1 ATOM 1881 N NZ . LYS A 1 234 ? 31.589 -38.460 2.428 1.00 102.94 ? 234 LYS A NZ 1 ATOM 1882 N N . PRO A 1 235 ? 25.581 -37.094 5.629 1.00 98.03 ? 235 PRO A N 1 ATOM 1883 C CA . PRO A 1 235 ? 24.245 -37.387 6.151 1.00 99.76 ? 235 PRO A CA 1 ATOM 1884 C C . PRO A 1 235 ? 24.325 -38.437 7.235 1.00 102.31 ? 235 PRO A C 1 ATOM 1885 O O . PRO A 1 235 ? 25.137 -39.357 7.136 1.00 102.46 ? 235 PRO A O 1 ATOM 1886 C CB . PRO A 1 235 ? 23.470 -37.928 4.941 1.00 100.61 ? 235 PRO A CB 1 ATOM 1887 C CG . PRO A 1 235 ? 24.461 -38.159 3.858 1.00 99.29 ? 235 PRO A CG 1 ATOM 1888 C CD . PRO A 1 235 ? 25.787 -37.597 4.257 1.00 97.03 ? 235 PRO A CD 1 ATOM 1889 N N . ASN A 1 236 ? 23.518 -38.276 8.278 1.00 105.39 ? 236 ASN A N 1 ATOM 1890 C CA . ASN A 1 236 ? 23.369 -39.302 9.300 1.00 108.67 ? 236 ASN A CA 1 ATOM 1891 C C . ASN A 1 236 ? 24.615 -39.480 10.177 1.00 108.60 ? 236 ASN A C 1 ATOM 1892 O O . ASN A 1 236 ? 24.721 -40.461 10.913 1.00 110.51 ? 236 ASN A O 1 ATOM 1893 C CB . ASN A 1 236 ? 23.000 -40.631 8.627 1.00 111.68 ? 236 ASN A CB 1 ATOM 1894 C CG . ASN A 1 236 ? 22.067 -41.469 9.460 1.00 117.12 ? 236 ASN A CG 1 ATOM 1895 O OD1 . ASN A 1 236 ? 21.469 -40.989 10.423 1.00 119.19 ? 236 ASN A OD1 1 ATOM 1896 N ND2 . ASN A 1 236 ? 21.923 -42.731 9.083 1.00 121.46 ? 236 ASN A ND2 1 ATOM 1897 N N . ASP A 1 237 ? 25.555 -38.539 10.084 1.00 106.84 ? 237 ASP A N 1 ATOM 1898 C CA . ASP A 1 237 ? 26.744 -38.517 10.931 1.00 106.09 ? 237 ASP A CA 1 ATOM 1899 C C . ASP A 1 237 ? 26.552 -37.396 11.939 1.00 104.52 ? 237 ASP A C 1 ATOM 1900 O O . ASP A 1 237 ? 25.699 -36.524 11.752 1.00 102.26 ? 237 ASP A O 1 ATOM 1901 C CB . ASP A 1 237 ? 28.008 -38.276 10.091 1.00 104.48 ? 237 ASP A CB 1 ATOM 1902 C CG . ASP A 1 237 ? 29.302 -38.552 10.863 1.00 104.59 ? 237 ASP A CG 1 ATOM 1903 O OD1 . ASP A 1 237 ? 29.282 -39.358 11.818 1.00 105.58 ? 237 ASP A OD1 1 ATOM 1904 O OD2 . ASP A 1 237 ? 30.347 -37.966 10.502 1.00 102.92 ? 237 ASP A OD2 1 ATOM 1905 N N . ALA A 1 238 ? 27.341 -37.425 13.007 1.00 105.53 ? 238 ALA A N 1 ATOM 1906 C CA . ALA A 1 238 ? 27.190 -36.484 14.107 1.00 105.06 ? 238 ALA A CA 1 ATOM 1907 C C . ALA A 1 238 ? 28.514 -35.823 14.445 1.00 102.34 ? 238 ALA A C 1 ATOM 1908 O O . ALA A 1 238 ? 29.565 -36.463 14.400 1.00 103.25 ? 238 ALA A O 1 ATOM 1909 C CB . ALA A 1 238 ? 26.640 -37.203 15.328 1.00 108.14 ? 238 ALA A CB 1 ATOM 1910 N N . ILE A 1 239 ? 28.451 -34.544 14.798 1.00 100.12 ? 239 ILE A N 1 ATOM 1911 C CA . ILE A 1 239 ? 29.637 -33.790 15.199 1.00 98.40 ? 239 ILE A CA 1 ATOM 1912 C C . ILE A 1 239 ? 29.636 -33.535 16.719 1.00 100.85 ? 239 ILE A C 1 ATOM 1913 O O . ILE A 1 239 ? 28.643 -33.066 17.277 1.00 100.67 ? 239 ILE A O 1 ATOM 1914 C CB . ILE A 1 239 ? 29.768 -32.475 14.391 1.00 94.18 ? 239 ILE A CB 1 ATOM 1915 C CG1 . ILE A 1 239 ? 31.131 -31.830 14.644 1.00 93.29 ? 239 ILE A CG1 1 ATOM 1916 C CG2 . ILE A 1 239 ? 28.640 -31.495 14.704 1.00 93.44 ? 239 ILE A CG2 1 ATOM 1917 C CD1 . ILE A 1 239 ? 31.449 -30.692 13.700 1.00 90.58 ? 239 ILE A CD1 1 ATOM 1918 N N . ASN A 1 240 ? 30.750 -33.868 17.374 1.00 102.32 ? 240 ASN A N 1 ATOM 1919 C CA . ASN A 1 240 ? 30.899 -33.729 18.827 1.00 104.41 ? 240 ASN A CA 1 ATOM 1920 C C . ASN A 1 240 ? 31.730 -32.508 19.184 1.00 101.94 ? 240 ASN A C 1 ATOM 1921 O O . ASN A 1 240 ? 32.799 -32.300 18.613 1.00 102.55 ? 240 ASN A O 1 ATOM 1922 C CB . ASN A 1 240 ? 31.596 -34.956 19.407 1.00 108.11 ? 240 ASN A CB 1 ATOM 1923 C CG . ASN A 1 240 ? 30.871 -36.243 19.088 1.00 112.04 ? 240 ASN A CG 1 ATOM 1924 O OD1 . ASN A 1 240 ? 29.926 -36.614 19.779 1.00 113.77 ? 240 ASN A OD1 1 ATOM 1925 N ND2 . ASN A 1 240 ? 31.314 -36.937 18.037 1.00 112.40 ? 240 ASN A ND2 1 ATOM 1926 N N . PHE A 1 241 ? 31.249 -31.715 20.134 1.00 100.84 ? 241 PHE A N 1 ATOM 1927 C CA . PHE A 1 241 ? 32.012 -30.584 20.653 1.00 98.86 ? 241 PHE A CA 1 ATOM 1928 C C . PHE A 1 241 ? 32.320 -30.767 22.137 1.00 100.47 ? 241 PHE A C 1 ATOM 1929 O O . PHE A 1 241 ? 31.564 -31.407 22.865 1.00 101.82 ? 241 PHE A O 1 ATOM 1930 C CB . PHE A 1 241 ? 31.251 -29.281 20.435 1.00 97.16 ? 241 PHE A CB 1 ATOM 1931 C CG . PHE A 1 241 ? 31.216 -28.839 19.005 1.00 95.09 ? 241 PHE A CG 1 ATOM 1932 C CD1 . PHE A 1 241 ? 32.365 -28.360 18.389 1.00 93.47 ? 241 PHE A CD1 1 ATOM 1933 C CD2 . PHE A 1 241 ? 30.043 -28.905 18.270 1.00 95.72 ? 241 PHE A CD2 1 ATOM 1934 C CE1 . PHE A 1 241 ? 32.344 -27.948 17.069 1.00 91.85 ? 241 PHE A CE1 1 ATOM 1935 C CE2 . PHE A 1 241 ? 30.015 -28.496 16.947 1.00 94.03 ? 241 PHE A CE2 1 ATOM 1936 C CZ . PHE A 1 241 ? 31.167 -28.017 16.345 1.00 91.99 ? 241 PHE A CZ 1 ATOM 1937 N N . GLU A 1 242 ? 33.448 -30.210 22.564 1.00 99.75 ? 242 GLU A N 1 ATOM 1938 C CA . GLU A 1 242 ? 33.853 -30.224 23.962 1.00 102.29 ? 242 GLU A CA 1 ATOM 1939 C C . GLU A 1 242 ? 34.812 -29.052 24.179 1.00 101.42 ? 242 GLU A C 1 ATOM 1940 O O . GLU A 1 242 ? 35.765 -28.898 23.411 1.00 99.97 ? 242 GLU A O 1 ATOM 1941 C CB . GLU A 1 242 ? 34.544 -31.548 24.319 1.00 104.77 ? 242 GLU A CB 1 ATOM 1942 C CG . GLU A 1 242 ? 34.058 -32.194 25.614 1.00 108.98 ? 242 GLU A CG 1 ATOM 1943 C CD . GLU A 1 242 ? 35.178 -32.799 26.453 1.00 111.13 ? 242 GLU A CD 1 ATOM 1944 O OE1 . GLU A 1 242 ? 36.054 -32.039 26.919 1.00 109.22 ? 242 GLU A OE1 1 ATOM 1945 O OE2 . GLU A 1 242 ? 35.180 -34.032 26.659 1.00 113.28 ? 242 GLU A OE2 1 ATOM 1946 N N . SER A 1 243 ? 34.571 -28.230 25.204 1.00 102.51 ? 243 SER A N 1 ATOM 1947 C CA . SER A 1 243 ? 35.434 -27.069 25.449 1.00 101.37 ? 243 SER A CA 1 ATOM 1948 C C . SER A 1 243 ? 35.413 -26.509 26.875 1.00 103.88 ? 243 SER A C 1 ATOM 1949 O O . SER A 1 243 ? 34.385 -26.535 27.546 1.00 105.57 ? 243 SER A O 1 ATOM 1950 C CB . SER A 1 243 ? 35.079 -25.947 24.473 1.00 98.42 ? 243 SER A CB 1 ATOM 1951 O OG . SER A 1 243 ? 36.004 -24.881 24.570 1.00 97.23 ? 243 SER A OG 1 ATOM 1952 N N . ASN A 1 244 ? 36.571 -25.996 27.304 1.00 105.69 ? 244 ASN A N 1 ATOM 1953 C CA . ASN A 1 244 ? 36.730 -25.240 28.558 1.00 107.87 ? 244 ASN A CA 1 ATOM 1954 C C . ASN A 1 244 ? 36.517 -23.745 28.395 1.00 106.04 ? 244 ASN A C 1 ATOM 1955 O O . ASN A 1 244 ? 36.256 -23.043 29.368 1.00 105.77 ? 244 ASN A O 1 ATOM 1956 C CB . ASN A 1 244 ? 38.146 -25.410 29.099 1.00 110.36 ? 244 ASN A CB 1 ATOM 1957 C CG . ASN A 1 244 ? 38.307 -26.651 29.931 1.00 115.22 ? 244 ASN A CG 1 ATOM 1958 O OD1 . ASN A 1 244 ? 37.389 -27.462 30.044 1.00 119.21 ? 244 ASN A OD1 1 ATOM 1959 N ND2 . ASN A 1 244 ? 39.482 -26.808 30.530 1.00 117.10 ? 244 ASN A ND2 1 ATOM 1960 N N . GLY A 1 245 ? 36.681 -23.261 27.169 1.00 103.61 ? 245 GLY A N 1 ATOM 1961 C CA . GLY A 1 245 ? 36.589 -21.841 26.873 1.00 102.00 ? 245 GLY A CA 1 ATOM 1962 C C . GLY A 1 245 ? 37.166 -21.537 25.509 1.00 99.72 ? 245 GLY A C 1 ATOM 1963 O O . GLY A 1 245 ? 37.756 -22.407 24.865 1.00 100.25 ? 245 GLY A O 1 ATOM 1964 N N . ASN A 1 246 ? 36.997 -20.289 25.080 1.00 98.60 ? 246 ASN A N 1 ATOM 1965 C CA . ASN A 1 246 ? 37.486 -19.802 23.785 1.00 95.62 ? 246 ASN A CA 1 ATOM 1966 C C . ASN A 1 246 ? 36.712 -20.370 22.593 1.00 92.50 ? 246 ASN A C 1 ATOM 1967 O O . ASN A 1 246 ? 37.112 -20.184 21.450 1.00 92.24 ? 246 ASN A O 1 ATOM 1968 C CB . ASN A 1 246 ? 38.998 -20.055 23.614 1.00 96.00 ? 246 ASN A CB 1 ATOM 1969 C CG . ASN A 1 246 ? 39.833 -19.409 24.712 1.00 98.43 ? 246 ASN A CG 1 ATOM 1970 O OD1 . ASN A 1 246 ? 40.295 -18.278 24.565 1.00 98.75 ? 246 ASN A OD1 1 ATOM 1971 N ND2 . ASN A 1 246 ? 40.042 -20.127 25.810 1.00 99.76 ? 246 ASN A ND2 1 ATOM 1972 N N . PHE A 1 247 ? 35.585 -21.023 22.861 1.00 92.15 ? 247 PHE A N 1 ATOM 1973 C CA . PHE A 1 247 ? 34.821 -21.709 21.827 1.00 88.59 ? 247 PHE A CA 1 ATOM 1974 C C . PHE A 1 247 ? 33.930 -20.723 21.097 1.00 86.28 ? 247 PHE A C 1 ATOM 1975 O O . PHE A 1 247 ? 33.157 -20.000 21.718 1.00 87.57 ? 247 PHE A O 1 ATOM 1976 C CB . PHE A 1 247 ? 33.981 -22.825 22.460 1.00 91.19 ? 247 PHE A CB 1 ATOM 1977 C CG . PHE A 1 247 ? 33.205 -23.663 21.474 1.00 90.00 ? 247 PHE A CG 1 ATOM 1978 C CD1 . PHE A 1 247 ? 33.796 -24.147 20.321 1.00 87.77 ? 247 PHE A CD1 1 ATOM 1979 C CD2 . PHE A 1 247 ? 31.886 -24.008 21.733 1.00 91.57 ? 247 PHE A CD2 1 ATOM 1980 C CE1 . PHE A 1 247 ? 33.081 -24.927 19.430 1.00 87.77 ? 247 PHE A CE1 1 ATOM 1981 C CE2 . PHE A 1 247 ? 31.169 -24.795 20.849 1.00 90.43 ? 247 PHE A CE2 1 ATOM 1982 C CZ . PHE A 1 247 ? 31.766 -25.252 19.694 1.00 89.01 ? 247 PHE A CZ 1 ATOM 1983 N N . ILE A 1 248 ? 34.064 -20.681 19.776 1.00 84.22 ? 248 ILE A N 1 ATOM 1984 C CA . ILE A 1 248 ? 33.163 -19.913 18.936 1.00 82.30 ? 248 ILE A CA 1 ATOM 1985 C C . ILE A 1 248 ? 32.233 -20.939 18.313 1.00 82.58 ? 248 ILE A C 1 ATOM 1986 O O . ILE A 1 248 ? 32.592 -21.624 17.357 1.00 82.26 ? 248 ILE A O 1 ATOM 1987 C CB . ILE A 1 248 ? 33.921 -19.112 17.864 1.00 80.91 ? 248 ILE A CB 1 ATOM 1988 C CG1 . ILE A 1 248 ? 35.119 -18.374 18.476 1.00 81.85 ? 248 ILE A CG1 1 ATOM 1989 C CG2 . ILE A 1 248 ? 32.990 -18.125 17.183 1.00 80.20 ? 248 ILE A CG2 1 ATOM 1990 C CD1 . ILE A 1 248 ? 34.765 -17.424 19.602 1.00 83.88 ? 248 ILE A CD1 1 ATOM 1991 N N . ALA A 1 249 ? 31.045 -21.066 18.889 1.00 84.76 ? 249 ALA A N 1 ATOM 1992 C CA . ALA A 1 249 ? 30.142 -22.164 18.566 1.00 85.74 ? 249 ALA A CA 1 ATOM 1993 C C . ALA A 1 249 ? 29.285 -21.863 17.341 1.00 84.74 ? 249 ALA A C 1 ATOM 1994 O O . ALA A 1 249 ? 28.931 -20.711 17.099 1.00 83.57 ? 249 ALA A O 1 ATOM 1995 C CB . ALA A 1 249 ? 29.248 -22.465 19.756 1.00 88.94 ? 249 ALA A CB 1 ATOM 1996 N N . PRO A 1 250 ? 28.943 -22.903 16.563 1.00 85.06 ? 250 PRO A N 1 ATOM 1997 C CA . PRO A 1 250 ? 28.031 -22.685 15.450 1.00 84.65 ? 250 PRO A CA 1 ATOM 1998 C C . PRO A 1 250 ? 26.619 -22.405 15.934 1.00 86.96 ? 250 PRO A C 1 ATOM 1999 O O . PRO A 1 250 ? 26.195 -22.986 16.926 1.00 91.27 ? 250 PRO A O 1 ATOM 2000 C CB . PRO A 1 250 ? 28.073 -24.012 14.685 1.00 84.06 ? 250 PRO A CB 1 ATOM 2001 C CG . PRO A 1 250 ? 28.589 -25.017 15.643 1.00 85.05 ? 250 PRO A CG 1 ATOM 2002 C CD . PRO A 1 250 ? 29.471 -24.278 16.594 1.00 85.53 ? 250 PRO A CD 1 ATOM 2003 N N . GLU A 1 251 ? 25.922 -21.495 15.260 1.00 87.28 ? 251 GLU A N 1 ATOM 2004 C CA . GLU A 1 251 ? 24.476 -21.352 15.419 1.00 90.41 ? 251 GLU A CA 1 ATOM 2005 C C . GLU A 1 251 ? 23.790 -21.823 14.138 1.00 90.21 ? 251 GLU A C 1 ATOM 2006 O O . GLU A 1 251 ? 22.881 -22.658 14.180 1.00 90.33 ? 251 GLU A O 1 ATOM 2007 C CB . GLU A 1 251 ? 24.081 -19.906 15.730 1.00 91.87 ? 251 GLU A CB 1 ATOM 2008 C CG . GLU A 1 251 ? 22.650 -19.778 16.244 1.00 96.12 ? 251 GLU A CG 1 ATOM 2009 C CD . GLU A 1 251 ? 22.178 -18.341 16.390 1.00 98.31 ? 251 GLU A CD 1 ATOM 2010 O OE1 . GLU A 1 251 ? 23.004 -17.405 16.274 1.00 98.66 ? 251 GLU A OE1 1 ATOM 2011 O OE2 . GLU A 1 251 ? 20.965 -18.150 16.624 1.00 100.35 ? 251 GLU A OE2 1 ATOM 2012 N N . TYR A 1 252 ? 24.237 -21.278 13.006 1.00 87.13 ? 252 TYR A N 1 ATOM 2013 C CA . TYR A 1 252 ? 23.727 -21.662 11.698 1.00 86.48 ? 252 TYR A CA 1 ATOM 2014 C C . TYR A 1 252 ? 24.778 -22.439 10.903 1.00 85.55 ? 252 TYR A C 1 ATOM 2015 O O . TYR A 1 252 ? 25.987 -22.230 11.056 1.00 83.16 ? 252 TYR A O 1 ATOM 2016 C CB . TYR A 1 252 ? 23.290 -20.424 10.910 1.00 85.70 ? 252 TYR A CB 1 ATOM 2017 C CG . TYR A 1 252 ? 22.176 -19.643 11.569 1.00 88.21 ? 252 TYR A CG 1 ATOM 2018 C CD1 . TYR A 1 252 ? 20.842 -20.002 11.390 1.00 89.99 ? 252 TYR A CD1 1 ATOM 2019 C CD2 . TYR A 1 252 ? 22.455 -18.547 12.383 1.00 88.03 ? 252 TYR A CD2 1 ATOM 2020 C CE1 . TYR A 1 252 ? 19.822 -19.289 12.001 1.00 91.08 ? 252 TYR A CE1 1 ATOM 2021 C CE2 . TYR A 1 252 ? 21.441 -17.830 12.995 1.00 89.08 ? 252 TYR A CE2 1 ATOM 2022 C CZ . TYR A 1 252 ? 20.128 -18.206 12.803 1.00 90.74 ? 252 TYR A CZ 1 ATOM 2023 O OH . TYR A 1 252 ? 19.127 -17.493 13.417 1.00 93.06 ? 252 TYR A OH 1 ATOM 2024 N N . ALA A 1 253 ? 24.296 -23.346 10.061 1.00 85.91 ? 253 ALA A N 1 ATOM 2025 C CA . ALA A 1 253 ? 25.135 -24.065 9.110 1.00 84.30 ? 253 ALA A CA 1 ATOM 2026 C C . ALA A 1 253 ? 24.380 -24.167 7.783 1.00 83.80 ? 253 ALA A C 1 ATOM 2027 O O . ALA A 1 253 ? 23.162 -23.978 7.744 1.00 85.03 ? 253 ALA A O 1 ATOM 2028 C CB . ALA A 1 253 ? 25.477 -25.445 9.653 1.00 85.42 ? 253 ALA A CB 1 ATOM 2029 N N . TYR A 1 254 ? 25.102 -24.460 6.705 1.00 81.77 ? 254 TYR A N 1 ATOM 2030 C CA . TYR A 1 254 ? 24.516 -24.471 5.368 1.00 81.74 ? 254 TYR A CA 1 ATOM 2031 C C . TYR A 1 254 ? 24.312 -25.883 4.835 1.00 82.65 ? 254 TYR A C 1 ATOM 2032 O O . TYR A 1 254 ? 25.235 -26.695 4.836 1.00 82.43 ? 254 TYR A O 1 ATOM 2033 C CB . TYR A 1 254 ? 25.408 -23.713 4.394 1.00 80.51 ? 254 TYR A CB 1 ATOM 2034 C CG . TYR A 1 254 ? 25.592 -22.245 4.705 1.00 79.21 ? 254 TYR A CG 1 ATOM 2035 C CD1 . TYR A 1 254 ? 26.633 -21.814 5.519 1.00 78.24 ? 254 TYR A CD1 1 ATOM 2036 C CD2 . TYR A 1 254 ? 24.746 -21.285 4.156 1.00 79.35 ? 254 TYR A CD2 1 ATOM 2037 C CE1 . TYR A 1 254 ? 26.818 -20.468 5.791 1.00 78.04 ? 254 TYR A CE1 1 ATOM 2038 C CE2 . TYR A 1 254 ? 24.922 -19.938 4.419 1.00 79.17 ? 254 TYR A CE2 1 ATOM 2039 C CZ . TYR A 1 254 ? 25.960 -19.534 5.236 1.00 79.06 ? 254 TYR A CZ 1 ATOM 2040 O OH . TYR A 1 254 ? 26.139 -18.197 5.504 1.00 81.46 ? 254 TYR A OH 1 ATOM 2041 N N . LYS A 1 255 ? 23.093 -26.160 4.379 1.00 84.35 ? 255 LYS A N 1 ATOM 2042 C CA . LYS A 1 255 ? 22.790 -27.390 3.653 1.00 85.59 ? 255 LYS A CA 1 ATOM 2043 C C . LYS A 1 255 ? 23.222 -27.234 2.198 1.00 83.68 ? 255 LYS A C 1 ATOM 2044 O O . LYS A 1 255 ? 22.967 -26.202 1.580 1.00 80.79 ? 255 LYS A O 1 ATOM 2045 C CB . LYS A 1 255 ? 21.287 -27.687 3.694 1.00 88.63 ? 255 LYS A CB 1 ATOM 2046 C CG . LYS A 1 255 ? 20.770 -28.214 5.020 1.00 90.78 ? 255 LYS A CG 1 ATOM 2047 C CD . LYS A 1 255 ? 19.275 -27.968 5.188 1.00 93.43 ? 255 LYS A CD 1 ATOM 2048 C CE . LYS A 1 255 ? 18.453 -28.617 4.089 1.00 95.63 ? 255 LYS A CE 1 ATOM 2049 N NZ . LYS A 1 255 ? 17.006 -28.651 4.433 1.00 98.99 ? 255 LYS A NZ 1 ATOM 2050 N N . ILE A 1 256 ? 23.863 -28.268 1.661 1.00 84.24 ? 256 ILE A N 1 ATOM 2051 C CA . ILE A 1 256 ? 24.256 -28.302 0.255 1.00 84.24 ? 256 ILE A CA 1 ATOM 2052 C C . ILE A 1 256 ? 23.160 -28.992 -0.549 1.00 86.90 ? 256 ILE A C 1 ATOM 2053 O O . ILE A 1 256 ? 23.162 -30.217 -0.703 1.00 88.48 ? 256 ILE A O 1 ATOM 2054 C CB . ILE A 1 256 ? 25.593 -29.043 0.069 1.00 83.14 ? 256 ILE A CB 1 ATOM 2055 C CG1 . ILE A 1 256 ? 26.710 -28.297 0.807 1.00 80.81 ? 256 ILE A CG1 1 ATOM 2056 C CG2 . ILE A 1 256 ? 25.934 -29.170 -1.411 1.00 83.12 ? 256 ILE A CG2 1 ATOM 2057 C CD1 . ILE A 1 256 ? 27.970 -29.109 1.020 1.00 80.39 ? 256 ILE A CD1 1 ATOM 2058 N N . VAL A 1 257 ? 22.226 -28.195 -1.061 1.00 88.72 ? 257 VAL A N 1 ATOM 2059 C CA . VAL A 1 257 ? 21.029 -28.731 -1.722 1.00 92.27 ? 257 VAL A CA 1 ATOM 2060 C C . VAL A 1 257 ? 21.211 -29.005 -3.218 1.00 92.76 ? 257 VAL A C 1 ATOM 2061 O O . VAL A 1 257 ? 20.526 -29.865 -3.783 1.00 94.28 ? 257 VAL A O 1 ATOM 2062 C CB . VAL A 1 257 ? 19.795 -27.822 -1.510 1.00 93.87 ? 257 VAL A CB 1 ATOM 2063 C CG1 . VAL A 1 257 ? 19.514 -27.662 -0.028 1.00 94.80 ? 257 VAL A CG1 1 ATOM 2064 C CG2 . VAL A 1 257 ? 19.970 -26.458 -2.166 1.00 92.83 ? 257 VAL A CG2 1 ATOM 2065 N N . LYS A 1 258 ? 22.120 -28.272 -3.854 1.00 91.31 ? 258 LYS A N 1 ATOM 2066 C CA . LYS A 1 258 ? 22.378 -28.450 -5.277 1.00 92.48 ? 258 LYS A CA 1 ATOM 2067 C C . LYS A 1 258 ? 23.861 -28.337 -5.593 1.00 90.81 ? 258 LYS A C 1 ATOM 2068 O O . LYS A 1 258 ? 24.500 -27.348 -5.242 1.00 89.54 ? 258 LYS A O 1 ATOM 2069 C CB . LYS A 1 258 ? 21.598 -27.419 -6.086 1.00 93.07 ? 258 LYS A CB 1 ATOM 2070 C CG . LYS A 1 258 ? 21.747 -27.597 -7.583 1.00 94.88 ? 258 LYS A CG 1 ATOM 2071 C CD . LYS A 1 258 ? 20.645 -26.878 -8.336 1.00 98.03 ? 258 LYS A CD 1 ATOM 2072 C CE . LYS A 1 258 ? 20.794 -27.066 -9.836 1.00 99.73 ? 258 LYS A CE 1 ATOM 2073 N NZ . LYS A 1 258 ? 19.541 -26.715 -10.557 1.00 102.77 ? 258 LYS A NZ 1 ATOM 2074 N N . LYS A 1 259 ? 24.396 -29.358 -6.256 1.00 92.80 ? 259 LYS A N 1 ATOM 2075 C CA . LYS A 1 259 ? 25.767 -29.337 -6.756 1.00 92.86 ? 259 LYS A CA 1 ATOM 2076 C C . LYS A 1 259 ? 25.760 -29.126 -8.266 1.00 93.22 ? 259 LYS A C 1 ATOM 2077 O O . LYS A 1 259 ? 24.696 -29.076 -8.880 1.00 94.71 ? 259 LYS A O 1 ATOM 2078 C CB . LYS A 1 259 ? 26.489 -30.635 -6.388 1.00 95.05 ? 259 LYS A CB 1 ATOM 2079 C CG . LYS A 1 259 ? 27.045 -30.632 -4.972 1.00 96.56 ? 259 LYS A CG 1 ATOM 2080 C CD . LYS A 1 259 ? 27.425 -32.027 -4.504 1.00 99.27 ? 259 LYS A CD 1 ATOM 2081 C CE . LYS A 1 259 ? 27.912 -32.013 -3.066 1.00 100.32 ? 259 LYS A CE 1 ATOM 2082 N NZ . LYS A 1 259 ? 27.718 -33.328 -2.395 1.00 102.93 ? 259 LYS A NZ 1 ATOM 2083 N N . GLY A 1 260 ? 26.946 -28.982 -8.856 1.00 93.39 ? 260 GLY A N 1 ATOM 2084 C CA . GLY A 1 260 ? 27.074 -28.836 -10.308 1.00 93.79 ? 260 GLY A CA 1 ATOM 2085 C C . GLY A 1 260 ? 28.012 -27.728 -10.742 1.00 91.73 ? 260 GLY A C 1 ATOM 2086 O O . GLY A 1 260 ? 28.851 -27.270 -9.969 1.00 90.78 ? 260 GLY A O 1 ATOM 2087 N N . ASP A 1 261 ? 27.851 -27.293 -11.988 1.00 92.92 ? 261 ASP A N 1 ATOM 2088 C CA . ASP A 1 261 ? 28.787 -26.367 -12.619 1.00 92.26 ? 261 ASP A CA 1 ATOM 2089 C C . ASP A 1 261 ? 28.670 -24.968 -12.055 1.00 88.36 ? 261 ASP A C 1 ATOM 2090 O O . ASP A 1 261 ? 27.625 -24.334 -12.160 1.00 88.86 ? 261 ASP A O 1 ATOM 2091 C CB . ASP A 1 261 ? 28.572 -26.315 -14.140 1.00 96.35 ? 261 ASP A CB 1 ATOM 2092 C CG . ASP A 1 261 ? 29.294 -27.431 -14.873 1.00 101.15 ? 261 ASP A CG 1 ATOM 2093 O OD1 . ASP A 1 261 ? 30.087 -28.153 -14.226 1.00 103.70 ? 261 ASP A OD1 1 ATOM 2094 O OD2 . ASP A 1 261 ? 29.076 -27.582 -16.099 1.00 104.41 ? 261 ASP A OD2 1 ATOM 2095 N N . SER A 1 262 ? 29.762 -24.496 -11.466 1.00 84.61 ? 262 SER A N 1 ATOM 2096 C CA . SER A 1 262 ? 29.843 -23.142 -10.937 1.00 83.04 ? 262 SER A CA 1 ATOM 2097 C C . SER A 1 262 ? 31.302 -22.708 -10.950 1.00 81.10 ? 262 SER A C 1 ATOM 2098 O O . SER A 1 262 ? 32.182 -23.492 -11.311 1.00 84.53 ? 262 SER A O 1 ATOM 2099 C CB . SER A 1 262 ? 29.280 -23.082 -9.516 1.00 82.06 ? 262 SER A CB 1 ATOM 2100 O OG . SER A 1 262 ? 29.196 -21.746 -9.050 1.00 81.99 ? 262 SER A OG 1 ATOM 2101 N N . THR A 1 263 ? 31.555 -21.458 -10.572 1.00 82.96 ? 263 THR A N 1 ATOM 2102 C CA . THR A 1 263 ? 32.912 -20.929 -10.529 1.00 77.70 ? 263 THR A CA 1 ATOM 2103 C C . THR A 1 263 ? 32.931 -19.648 -9.727 1.00 73.69 ? 263 THR A C 1 ATOM 2104 O O . THR A 1 263 ? 31.943 -18.916 -9.708 1.00 72.87 ? 263 THR A O 1 ATOM 2105 C CB . THR A 1 263 ? 33.471 -20.644 -11.947 1.00 75.26 ? 263 THR A CB 1 ATOM 2106 O OG1 . THR A 1 263 ? 34.876 -20.402 -11.868 1.00 74.05 ? 263 THR A OG1 1 ATOM 2107 C CG2 . THR A 1 263 ? 32.806 -19.430 -12.594 1.00 72.64 ? 263 THR A CG2 1 ATOM 2108 N N . ILE A 1 264 ? 34.051 -19.387 -9.058 1.00 71.93 ? 264 ILE A N 1 ATOM 2109 C CA . ILE A 1 264 ? 34.278 -18.099 -8.412 1.00 68.50 ? 264 ILE A CA 1 ATOM 2110 C C . ILE A 1 264 ? 35.081 -17.251 -9.386 1.00 66.15 ? 264 ILE A C 1 ATOM 2111 O O . ILE A 1 264 ? 36.190 -17.608 -9.766 1.00 67.25 ? 264 ILE A O 1 ATOM 2112 C CB . ILE A 1 264 ? 35.027 -18.237 -7.077 1.00 68.41 ? 264 ILE A CB 1 ATOM 2113 C CG1 . ILE A 1 264 ? 34.255 -19.172 -6.145 1.00 70.85 ? 264 ILE A CG1 1 ATOM 2114 C CG2 . ILE A 1 264 ? 35.209 -16.869 -6.434 1.00 66.38 ? 264 ILE A CG2 1 ATOM 2115 C CD1 . ILE A 1 264 ? 34.976 -19.493 -4.856 1.00 73.04 ? 264 ILE A CD1 1 ATOM 2116 N N . MET A 1 265 ? 34.503 -16.132 -9.789 1.00 64.55 ? 265 MET A N 1 ATOM 2117 C CA . MET A 1 265 ? 35.063 -15.284 -10.824 1.00 63.57 ? 265 MET A CA 1 ATOM 2118 C C . MET A 1 265 ? 35.545 -14.003 -10.161 1.00 64.68 ? 265 MET A C 1 ATOM 2119 O O . MET A 1 265 ? 34.808 -13.390 -9.401 1.00 67.88 ? 265 MET A O 1 ATOM 2120 C CB . MET A 1 265 ? 33.958 -14.984 -11.821 1.00 63.13 ? 265 MET A CB 1 ATOM 2121 C CG . MET A 1 265 ? 34.372 -14.299 -13.095 1.00 62.74 ? 265 MET A CG 1 ATOM 2122 S SD . MET A 1 265 ? 32.961 -14.168 -14.215 1.00 64.15 ? 265 MET A SD 1 ATOM 2123 C CE . MET A 1 265 ? 32.757 -15.880 -14.706 1.00 64.57 ? 265 MET A CE 1 ATOM 2124 N N . LYS A 1 266 ? 36.786 -13.613 -10.415 1.00 65.79 ? 266 LYS A N 1 ATOM 2125 C CA . LYS A 1 266 ? 37.343 -12.423 -9.790 1.00 67.29 ? 266 LYS A CA 1 ATOM 2126 C C . LYS A 1 266 ? 37.161 -11.252 -10.746 1.00 66.36 ? 266 LYS A C 1 ATOM 2127 O O . LYS A 1 266 ? 37.692 -11.271 -11.859 1.00 66.28 ? 266 LYS A O 1 ATOM 2128 C CB . LYS A 1 266 ? 38.820 -12.624 -9.432 1.00 70.47 ? 266 LYS A CB 1 ATOM 2129 C CG . LYS A 1 266 ? 39.116 -13.907 -8.652 1.00 74.49 ? 266 LYS A CG 1 ATOM 2130 C CD . LYS A 1 266 ? 38.658 -13.847 -7.198 1.00 77.07 ? 266 LYS A CD 1 ATOM 2131 C CE . LYS A 1 266 ? 39.691 -13.166 -6.310 1.00 81.41 ? 266 LYS A CE 1 ATOM 2132 N NZ . LYS A 1 266 ? 39.142 -12.692 -4.996 1.00 83.76 ? 266 LYS A NZ 1 ATOM 2133 N N . SER A 1 267 ? 36.398 -10.248 -10.309 1.00 65.98 ? 267 SER A N 1 ATOM 2134 C CA . SER A 1 267 ? 36.026 -9.112 -11.151 1.00 65.48 ? 267 SER A CA 1 ATOM 2135 C C . SER A 1 267 ? 35.556 -7.939 -10.299 1.00 67.29 ? 267 SER A C 1 ATOM 2136 O O . SER A 1 267 ? 34.932 -8.137 -9.258 1.00 69.46 ? 267 SER A O 1 ATOM 2137 C CB . SER A 1 267 ? 34.905 -9.529 -12.105 1.00 65.60 ? 267 SER A CB 1 ATOM 2138 O OG . SER A 1 267 ? 34.411 -8.434 -12.862 1.00 66.45 ? 267 SER A OG 1 ATOM 2139 N N . GLU A 1 268 ? 35.850 -6.723 -10.749 1.00 68.34 ? 268 GLU A N 1 ATOM 2140 C CA . GLU A 1 268 ? 35.410 -5.510 -10.058 1.00 69.32 ? 268 GLU A CA 1 ATOM 2141 C C . GLU A 1 268 ? 34.050 -5.013 -10.566 1.00 69.88 ? 268 GLU A C 1 ATOM 2142 O O . GLU A 1 268 ? 33.455 -4.105 -9.981 1.00 72.55 ? 268 GLU A O 1 ATOM 2143 C CB . GLU A 1 268 ? 36.458 -4.407 -10.214 1.00 71.13 ? 268 GLU A CB 1 ATOM 2144 C CG . GLU A 1 268 ? 37.869 -4.820 -9.818 1.00 72.17 ? 268 GLU A CG 1 ATOM 2145 C CD . GLU A 1 268 ? 37.965 -5.321 -8.386 1.00 73.95 ? 268 GLU A CD 1 ATOM 2146 O OE1 . GLU A 1 268 ? 37.558 -4.580 -7.458 1.00 73.23 ? 268 GLU A OE1 1 ATOM 2147 O OE2 . GLU A 1 268 ? 38.453 -6.459 -8.191 1.00 74.89 ? 268 GLU A OE2 1 ATOM 2148 N N . LEU A 1 269 ? 33.552 -5.623 -11.637 1.00 68.74 ? 269 LEU A N 1 ATOM 2149 C CA . LEU A 1 269 ? 32.279 -5.225 -12.241 1.00 71.08 ? 269 LEU A CA 1 ATOM 2150 C C . LEU A 1 269 ? 31.085 -5.631 -11.373 1.00 72.34 ? 269 LEU A C 1 ATOM 2151 O O . LEU A 1 269 ? 31.157 -6.616 -10.639 1.00 70.54 ? 269 LEU A O 1 ATOM 2152 C CB . LEU A 1 269 ? 32.129 -5.857 -13.633 1.00 69.32 ? 269 LEU A CB 1 ATOM 2153 C CG . LEU A 1 269 ? 33.194 -5.523 -14.684 1.00 68.24 ? 269 LEU A CG 1 ATOM 2154 C CD1 . LEU A 1 269 ? 33.075 -6.450 -15.882 1.00 67.05 ? 269 LEU A CD1 1 ATOM 2155 C CD2 . LEU A 1 269 ? 33.093 -4.071 -15.128 1.00 70.64 ? 269 LEU A CD2 1 ATOM 2156 N N . GLU A 1 270 ? 29.997 -4.865 -11.475 1.00 76.14 ? 270 GLU A N 1 ATOM 2157 C CA . GLU A 1 270 ? 28.729 -5.176 -10.798 1.00 79.07 ? 270 GLU A CA 1 ATOM 2158 C C . GLU A 1 270 ? 27.708 -5.793 -11.782 1.00 75.94 ? 270 GLU A C 1 ATOM 2159 O O . GLU A 1 270 ? 28.047 -6.102 -12.921 1.00 75.35 ? 270 GLU A O 1 ATOM 2160 C CB . GLU A 1 270 ? 28.160 -3.912 -10.128 1.00 85.06 ? 270 GLU A CB 1 ATOM 2161 C CG . GLU A 1 270 ? 29.139 -3.148 -9.230 1.00 89.27 ? 270 GLU A CG 1 ATOM 2162 C CD . GLU A 1 270 ? 29.382 -3.789 -7.858 1.00 91.17 ? 270 GLU A CD 1 ATOM 2163 O OE1 . GLU A 1 270 ? 29.355 -5.039 -7.739 1.00 92.17 ? 270 GLU A OE1 1 ATOM 2164 O OE2 . GLU A 1 270 ? 29.613 -3.032 -6.886 1.00 90.47 ? 270 GLU A OE2 1 ATOM 2165 N N . TYR A 1 271 ? 26.468 -5.983 -11.336 1.00 76.10 ? 271 TYR A N 1 ATOM 2166 C CA . TYR A 1 271 ? 25.429 -6.640 -12.145 1.00 75.27 ? 271 TYR A CA 1 ATOM 2167 C C . TYR A 1 271 ? 24.967 -5.799 -13.334 1.00 77.01 ? 271 TYR A C 1 ATOM 2168 O O . TYR A 1 271 ? 24.728 -4.600 -13.206 1.00 77.67 ? 271 TYR A O 1 ATOM 2169 C CB . TYR A 1 271 ? 24.220 -6.975 -11.275 1.00 76.46 ? 271 TYR A CB 1 ATOM 2170 C CG . TYR A 1 271 ? 23.164 -7.815 -11.960 1.00 76.89 ? 271 TYR A CG 1 ATOM 2171 C CD1 . TYR A 1 271 ? 23.487 -9.029 -12.558 1.00 74.38 ? 271 TYR A CD1 1 ATOM 2172 C CD2 . TYR A 1 271 ? 21.832 -7.406 -11.982 1.00 79.92 ? 271 TYR A CD2 1 ATOM 2173 C CE1 . TYR A 1 271 ? 22.521 -9.802 -13.176 1.00 75.91 ? 271 TYR A CE1 1 ATOM 2174 C CE2 . TYR A 1 271 ? 20.855 -8.174 -12.590 1.00 81.18 ? 271 TYR A CE2 1 ATOM 2175 C CZ . TYR A 1 271 ? 21.200 -9.371 -13.187 1.00 79.59 ? 271 TYR A CZ 1 ATOM 2176 O OH . TYR A 1 271 ? 20.223 -10.127 -13.792 1.00 79.62 ? 271 TYR A OH 1 ATOM 2177 N N . GLY A 1 272 ? 24.816 -6.452 -14.483 1.00 78.10 ? 272 GLY A N 1 ATOM 2178 C CA . GLY A 1 272 ? 24.519 -5.763 -15.734 1.00 80.63 ? 272 GLY A CA 1 ATOM 2179 C C . GLY A 1 272 ? 23.068 -5.763 -16.174 1.00 85.44 ? 272 GLY A C 1 ATOM 2180 O O . GLY A 1 272 ? 22.755 -5.188 -17.214 1.00 86.41 ? 272 GLY A O 1 ATOM 2181 N N . ASN A 1 273 ? 22.183 -6.391 -15.394 1.00 89.62 ? 273 ASN A N 1 ATOM 2182 C CA . ASN A 1 273 ? 20.758 -6.511 -15.750 1.00 95.72 ? 273 ASN A CA 1 ATOM 2183 C C . ASN A 1 273 ? 20.624 -7.051 -17.170 1.00 94.70 ? 273 ASN A C 1 ATOM 2184 O O . ASN A 1 273 ? 20.211 -6.344 -18.089 1.00 97.29 ? 273 ASN A O 1 ATOM 2185 C CB . ASN A 1 273 ? 20.040 -5.164 -15.598 1.00 100.84 ? 273 ASN A CB 1 ATOM 2186 C CG . ASN A 1 273 ? 19.859 -4.759 -14.146 1.00 104.20 ? 273 ASN A CG 1 ATOM 2187 O OD1 . ASN A 1 273 ? 20.637 -3.973 -13.602 1.00 104.58 ? 273 ASN A OD1 1 ATOM 2188 N ND2 . ASN A 1 273 ? 18.829 -5.301 -13.509 1.00 107.89 ? 273 ASN A ND2 1 ATOM 2189 N N . CYS A 1 274 ? 20.965 -8.324 -17.327 1.00 91.75 ? 274 CYS A N 1 ATOM 2190 C CA . CYS A 1 274 ? 21.465 -8.819 -18.597 1.00 89.72 ? 274 CYS A CA 1 ATOM 2191 C C . CYS A 1 274 ? 21.429 -10.348 -18.653 1.00 84.88 ? 274 CYS A C 1 ATOM 2192 O O . CYS A 1 274 ? 21.440 -11.002 -17.614 1.00 85.32 ? 274 CYS A O 1 ATOM 2193 C CB . CYS A 1 274 ? 22.906 -8.319 -18.722 1.00 91.06 ? 274 CYS A CB 1 ATOM 2194 S SG . CYS A 1 274 ? 23.870 -9.102 -20.013 1.00 98.53 ? 274 CYS A SG 1 ATOM 2195 N N . ASN A 1 275 ? 21.406 -10.917 -19.857 1.00 81.67 ? 275 ASN A N 1 ATOM 2196 C CA . ASN A 1 275 ? 21.408 -12.379 -20.027 1.00 81.13 ? 275 ASN A CA 1 ATOM 2197 C C . ASN A 1 275 ? 22.372 -12.861 -21.119 1.00 79.30 ? 275 ASN A C 1 ATOM 2198 O O . ASN A 1 275 ? 22.598 -12.166 -22.111 1.00 80.66 ? 275 ASN A O 1 ATOM 2199 C CB . ASN A 1 275 ? 19.993 -12.866 -20.332 1.00 84.88 ? 275 ASN A CB 1 ATOM 2200 C CG . ASN A 1 275 ? 19.861 -14.378 -20.268 1.00 85.36 ? 275 ASN A CG 1 ATOM 2201 O OD1 . ASN A 1 275 ? 20.384 -15.028 -19.371 1.00 83.92 ? 275 ASN A OD1 1 ATOM 2202 N ND2 . ASN A 1 275 ? 19.143 -14.942 -21.220 1.00 89.14 ? 275 ASN A ND2 1 ATOM 2203 N N . THR A 1 276 ? 22.937 -14.053 -20.936 1.00 77.50 ? 276 THR A N 1 ATOM 2204 C CA . THR A 1 276 ? 23.934 -14.586 -21.864 1.00 74.21 ? 276 THR A CA 1 ATOM 2205 C C . THR A 1 276 ? 24.107 -16.088 -21.697 1.00 75.85 ? 276 THR A C 1 ATOM 2206 O O . THR A 1 276 ? 23.675 -16.657 -20.703 1.00 79.18 ? 276 THR A O 1 ATOM 2207 C CB . THR A 1 276 ? 25.308 -13.921 -21.641 1.00 71.05 ? 276 THR A CB 1 ATOM 2208 O OG1 . THR A 1 276 ? 26.231 -14.357 -22.644 1.00 69.42 ? 276 THR A OG1 1 ATOM 2209 C CG2 . THR A 1 276 ? 25.879 -14.272 -20.264 1.00 71.06 ? 276 THR A CG2 1 ATOM 2210 N N . LYS A 1 277 ? 24.757 -16.717 -22.672 1.00 77.13 ? 277 LYS A N 1 ATOM 2211 C CA . LYS A 1 277 ? 25.105 -18.140 -22.600 1.00 79.50 ? 277 LYS A CA 1 ATOM 2212 C C . LYS A 1 277 ? 26.603 -18.352 -22.376 1.00 74.56 ? 277 LYS A C 1 ATOM 2213 O O . LYS A 1 277 ? 27.063 -19.487 -22.261 1.00 74.08 ? 277 LYS A O 1 ATOM 2214 C CB . LYS A 1 277 ? 24.671 -18.865 -23.881 1.00 84.69 ? 277 LYS A CB 1 ATOM 2215 C CG . LYS A 1 277 ? 23.213 -18.627 -24.268 1.00 91.04 ? 277 LYS A CG 1 ATOM 2216 C CD . LYS A 1 277 ? 22.667 -19.739 -25.155 1.00 95.64 ? 277 LYS A CD 1 ATOM 2217 C CE . LYS A 1 277 ? 22.165 -20.913 -24.325 1.00 100.51 ? 277 LYS A CE 1 ATOM 2218 N NZ . LYS A 1 277 ? 21.779 -22.089 -25.152 1.00 104.39 ? 277 LYS A NZ 1 ATOM 2219 N N . CYS A 1 278 ? 27.360 -17.263 -22.320 1.00 71.01 ? 278 CYS A N 1 ATOM 2220 C CA . CYS A 1 278 ? 28.799 -17.342 -22.115 1.00 69.36 ? 278 CYS A CA 1 ATOM 2221 C C . CYS A 1 278 ? 29.279 -16.094 -21.394 1.00 65.08 ? 278 CYS A C 1 ATOM 2222 O O . CYS A 1 278 ? 29.096 -14.977 -21.885 1.00 62.81 ? 278 CYS A O 1 ATOM 2223 C CB . CYS A 1 278 ? 29.522 -17.486 -23.454 1.00 69.89 ? 278 CYS A CB 1 ATOM 2224 S SG . CYS A 1 278 ? 31.332 -17.513 -23.329 1.00 71.79 ? 278 CYS A SG 1 ATOM 2225 N N . GLN A 1 279 ? 29.892 -16.287 -20.229 1.00 62.91 ? 279 GLN A N 1 ATOM 2226 C CA . GLN A 1 279 ? 30.298 -15.165 -19.391 1.00 61.59 ? 279 GLN A CA 1 ATOM 2227 C C . GLN A 1 279 ? 31.785 -15.204 -19.100 1.00 59.37 ? 279 GLN A C 1 ATOM 2228 O O . GLN A 1 279 ? 32.340 -16.275 -18.868 1.00 59.24 ? 279 GLN A O 1 ATOM 2229 C CB . GLN A 1 279 ? 29.521 -15.185 -18.074 1.00 62.35 ? 279 GLN A CB 1 ATOM 2230 C CG . GLN A 1 279 ? 29.767 -13.975 -17.187 1.00 61.38 ? 279 GLN A CG 1 ATOM 2231 C CD . GLN A 1 279 ? 29.140 -12.711 -17.734 1.00 61.48 ? 279 GLN A CD 1 ATOM 2232 O OE1 . GLN A 1 279 ? 27.926 -12.644 -17.925 1.00 63.39 ? 279 GLN A OE1 1 ATOM 2233 N NE2 . GLN A 1 279 ? 29.963 -11.695 -17.984 1.00 60.18 ? 279 GLN A NE2 1 ATOM 2234 N N . THR A 1 280 ? 32.408 -14.027 -19.108 1.00 58.15 ? 280 THR A N 1 ATOM 2235 C CA . THR A 1 280 ? 33.810 -13.859 -18.716 1.00 59.01 ? 280 THR A CA 1 ATOM 2236 C C . THR A 1 280 ? 33.937 -12.712 -17.709 1.00 60.24 ? 280 THR A C 1 ATOM 2237 O O . THR A 1 280 ? 33.057 -11.852 -17.641 1.00 62.48 ? 280 THR A O 1 ATOM 2238 C CB . THR A 1 280 ? 34.706 -13.509 -19.920 1.00 57.68 ? 280 THR A CB 1 ATOM 2239 O OG1 . THR A 1 280 ? 34.667 -12.096 -20.150 1.00 56.70 ? 280 THR A OG1 1 ATOM 2240 C CG2 . THR A 1 280 ? 34.253 -14.238 -21.168 1.00 57.56 ? 280 THR A CG2 1 ATOM 2241 N N . PRO A 1 281 ? 35.043 -12.670 -16.945 1.00 60.76 ? 281 PRO A N 1 ATOM 2242 C CA . PRO A 1 281 ? 35.222 -11.629 -15.928 1.00 61.73 ? 281 PRO A CA 1 ATOM 2243 C C . PRO A 1 281 ? 35.180 -10.193 -16.449 1.00 63.73 ? 281 PRO A C 1 ATOM 2244 O O . PRO A 1 281 ? 35.030 -9.267 -15.646 1.00 64.92 ? 281 PRO A O 1 ATOM 2245 C CB . PRO A 1 281 ? 36.606 -11.926 -15.354 1.00 62.08 ? 281 PRO A CB 1 ATOM 2246 C CG . PRO A 1 281 ? 36.838 -13.364 -15.616 1.00 61.97 ? 281 PRO A CG 1 ATOM 2247 C CD . PRO A 1 281 ? 36.079 -13.713 -16.856 1.00 60.83 ? 281 PRO A CD 1 ATOM 2248 N N . MET A 1 282 ? 35.328 -10.009 -17.761 1.00 65.06 ? 282 MET A N 1 ATOM 2249 C CA . MET A 1 282 ? 35.285 -8.681 -18.374 1.00 67.17 ? 282 MET A CA 1 ATOM 2250 C C . MET A 1 282 ? 33.972 -8.384 -19.074 1.00 64.76 ? 282 MET A C 1 ATOM 2251 O O . MET A 1 282 ? 33.700 -7.232 -19.409 1.00 66.00 ? 282 MET A O 1 ATOM 2252 C CB . MET A 1 282 ? 36.385 -8.553 -19.412 1.00 72.13 ? 282 MET A CB 1 ATOM 2253 C CG . MET A 1 282 ? 37.786 -8.560 -18.845 1.00 78.20 ? 282 MET A CG 1 ATOM 2254 S SD . MET A 1 282 ? 38.930 -8.963 -20.170 1.00 91.28 ? 282 MET A SD 1 ATOM 2255 C CE . MET A 1 282 ? 38.506 -7.728 -21.400 1.00 89.08 ? 282 MET A CE 1 ATOM 2256 N N . GLY A 1 283 ? 33.176 -9.415 -19.323 1.00 61.91 ? 283 GLY A N 1 ATOM 2257 C CA . GLY A 1 283 ? 31.933 -9.248 -20.060 1.00 62.78 ? 283 GLY A CA 1 ATOM 2258 C C . GLY A 1 283 ? 31.446 -10.553 -20.649 1.00 62.15 ? 283 GLY A C 1 ATOM 2259 O O . GLY A 1 283 ? 32.149 -11.561 -20.603 1.00 61.02 ? 283 GLY A O 1 ATOM 2260 N N . ALA A 1 284 ? 30.243 -10.527 -21.209 1.00 63.44 ? 284 ALA A N 1 ATOM 2261 C CA . ALA A 1 284 ? 29.628 -11.724 -21.771 1.00 65.39 ? 284 ALA A CA 1 ATOM 2262 C C . ALA A 1 284 ? 29.800 -11.775 -23.285 1.00 66.48 ? 284 ALA A C 1 ATOM 2263 O O . ALA A 1 284 ? 30.029 -10.751 -23.933 1.00 65.98 ? 284 ALA A O 1 ATOM 2264 C CB . ALA A 1 284 ? 28.159 -11.778 -21.408 1.00 67.39 ? 284 ALA A CB 1 ATOM 2265 N N . ILE A 1 285 ? 29.669 -12.981 -23.833 1.00 68.24 ? 285 ILE A N 1 ATOM 2266 C CA . ILE A 1 285 ? 29.922 -13.244 -25.247 1.00 69.30 ? 285 ILE A CA 1 ATOM 2267 C C . ILE A 1 285 ? 28.676 -13.819 -25.914 1.00 73.24 ? 285 ILE A C 1 ATOM 2268 O O . ILE A 1 285 ? 28.070 -14.765 -25.412 1.00 76.12 ? 285 ILE A O 1 ATOM 2269 C CB . ILE A 1 285 ? 31.104 -14.227 -25.427 1.00 66.60 ? 285 ILE A CB 1 ATOM 2270 C CG1 . ILE A 1 285 ? 32.416 -13.546 -25.035 1.00 65.02 ? 285 ILE A CG1 1 ATOM 2271 C CG2 . ILE A 1 285 ? 31.195 -14.721 -26.863 1.00 65.55 ? 285 ILE A CG2 1 ATOM 2272 C CD1 . ILE A 1 285 ? 33.597 -14.490 -24.927 1.00 64.03 ? 285 ILE A CD1 1 ATOM 2273 N N . ASN A 1 286 ? 28.314 -13.236 -27.052 1.00 76.87 ? 286 ASN A N 1 ATOM 2274 C CA . ASN A 1 286 ? 27.206 -13.709 -27.869 1.00 82.45 ? 286 ASN A CA 1 ATOM 2275 C C . ASN A 1 286 ? 27.677 -13.848 -29.312 1.00 78.79 ? 286 ASN A C 1 ATOM 2276 O O . ASN A 1 286 ? 27.598 -12.906 -30.096 1.00 75.92 ? 286 ASN A O 1 ATOM 2277 C CB . ASN A 1 286 ? 26.043 -12.721 -27.768 1.00 90.38 ? 286 ASN A CB 1 ATOM 2278 C CG . ASN A 1 286 ? 24.852 -13.115 -28.620 1.00 102.21 ? 286 ASN A CG 1 ATOM 2279 O OD1 . ASN A 1 286 ? 24.534 -14.299 -28.768 1.00 98.85 ? 286 ASN A OD1 1 ATOM 2280 N ND2 . ASN A 1 286 ? 24.173 -12.101 -29.183 1.00 118.42 ? 286 ASN A ND2 1 ATOM 2281 N N . SER A 1 287 ? 28.197 -15.020 -29.654 1.00 76.76 ? 287 SER A N 1 ATOM 2282 C CA . SER A 1 287 ? 28.648 -15.261 -31.017 1.00 76.79 ? 287 SER A CA 1 ATOM 2283 C C . SER A 1 287 ? 28.691 -16.735 -31.384 1.00 76.89 ? 287 SER A C 1 ATOM 2284 O O . SER A 1 287 ? 28.688 -17.609 -30.520 1.00 76.63 ? 287 SER A O 1 ATOM 2285 C CB . SER A 1 287 ? 30.026 -14.636 -31.245 1.00 74.97 ? 287 SER A CB 1 ATOM 2286 O OG . SER A 1 287 ? 31.056 -15.460 -30.747 1.00 73.33 ? 287 SER A OG 1 ATOM 2287 N N . SER A 1 288 ? 28.741 -16.986 -32.689 1.00 77.57 ? 288 SER A N 1 ATOM 2288 C CA . SER A 1 288 ? 28.798 -18.338 -33.232 1.00 78.43 ? 288 SER A CA 1 ATOM 2289 C C . SER A 1 288 ? 30.210 -18.690 -33.708 1.00 73.45 ? 288 SER A C 1 ATOM 2290 O O . SER A 1 288 ? 30.410 -19.716 -34.356 1.00 73.65 ? 288 SER A O 1 ATOM 2291 C CB . SER A 1 288 ? 27.798 -18.465 -34.384 1.00 82.21 ? 288 SER A CB 1 ATOM 2292 O OG . SER A 1 288 ? 27.940 -17.385 -35.293 1.00 83.63 ? 288 SER A OG 1 ATOM 2293 N N . MET A 1 289 ? 31.186 -17.853 -33.365 1.00 68.11 ? 289 MET A N 1 ATOM 2294 C CA . MET A 1 289 ? 32.571 -18.080 -33.767 1.00 65.95 ? 289 MET A CA 1 ATOM 2295 C C . MET A 1 289 ? 33.152 -19.248 -32.980 1.00 65.36 ? 289 MET A C 1 ATOM 2296 O O . MET A 1 289 ? 32.776 -19.468 -31.838 1.00 67.07 ? 289 MET A O 1 ATOM 2297 C CB . MET A 1 289 ? 33.433 -16.854 -33.483 1.00 66.41 ? 289 MET A CB 1 ATOM 2298 C CG . MET A 1 289 ? 32.953 -15.555 -34.091 1.00 67.26 ? 289 MET A CG 1 ATOM 2299 S SD . MET A 1 289 ? 33.295 -15.466 -35.845 1.00 69.11 ? 289 MET A SD 1 ATOM 2300 C CE . MET A 1 289 ? 33.603 -13.700 -35.984 1.00 68.58 ? 289 MET A CE 1 ATOM 2301 N N . PRO A 1 290 ? 34.077 -20.001 -33.586 1.00 64.52 ? 290 PRO A N 1 ATOM 2302 C CA . PRO A 1 290 ? 34.726 -21.085 -32.855 1.00 64.54 ? 290 PRO A CA 1 ATOM 2303 C C . PRO A 1 290 ? 35.813 -20.620 -31.882 1.00 62.80 ? 290 PRO A C 1 ATOM 2304 O O . PRO A 1 290 ? 36.284 -21.425 -31.081 1.00 65.14 ? 290 PRO A O 1 ATOM 2305 C CB . PRO A 1 290 ? 35.352 -21.920 -33.974 1.00 64.53 ? 290 PRO A CB 1 ATOM 2306 C CG . PRO A 1 290 ? 35.658 -20.917 -35.028 1.00 63.15 ? 290 PRO A CG 1 ATOM 2307 C CD . PRO A 1 290 ? 34.480 -19.987 -35.005 1.00 63.08 ? 290 PRO A CD 1 ATOM 2308 N N . PHE A 1 291 ? 36.221 -19.355 -31.961 1.00 58.89 ? 291 PHE A N 1 ATOM 2309 C CA . PHE A 1 291 ? 37.285 -18.843 -31.105 1.00 58.51 ? 291 PHE A CA 1 ATOM 2310 C C . PHE A 1 291 ? 36.956 -17.469 -30.583 1.00 56.31 ? 291 PHE A C 1 ATOM 2311 O O . PHE A 1 291 ? 36.175 -16.743 -31.196 1.00 55.96 ? 291 PHE A O 1 ATOM 2312 C CB . PHE A 1 291 ? 38.588 -18.684 -31.881 1.00 59.87 ? 291 PHE A CB 1 ATOM 2313 C CG . PHE A 1 291 ? 39.214 -19.968 -32.313 1.00 62.09 ? 291 PHE A CG 1 ATOM 2314 C CD1 . PHE A 1 291 ? 39.871 -20.773 -31.400 1.00 65.14 ? 291 PHE A CD1 1 ATOM 2315 C CD2 . PHE A 1 291 ? 39.190 -20.349 -33.647 1.00 63.21 ? 291 PHE A CD2 1 ATOM 2316 C CE1 . PHE A 1 291 ? 40.472 -21.952 -31.803 1.00 67.52 ? 291 PHE A CE1 1 ATOM 2317 C CE2 . PHE A 1 291 ? 39.788 -21.526 -34.059 1.00 65.10 ? 291 PHE A CE2 1 ATOM 2318 C CZ . PHE A 1 291 ? 40.427 -22.326 -33.135 1.00 67.36 ? 291 PHE A CZ 1 ATOM 2319 N N . HIS A 1 292 ? 37.601 -17.100 -29.477 1.00 53.99 ? 292 HIS A N 1 ATOM 2320 C CA . HIS A 1 292 ? 37.591 -15.719 -28.999 1.00 51.79 ? 292 HIS A CA 1 ATOM 2321 C C . HIS A 1 292 ? 38.907 -15.405 -28.298 1.00 50.70 ? 292 HIS A C 1 ATOM 2322 O O . HIS A 1 292 ? 39.678 -16.316 -27.986 1.00 50.67 ? 292 HIS A O 1 ATOM 2323 C CB . HIS A 1 292 ? 36.414 -15.487 -28.052 1.00 53.21 ? 292 HIS A CB 1 ATOM 2324 C CG . HIS A 1 292 ? 36.567 -16.165 -26.728 1.00 55.26 ? 292 HIS A CG 1 ATOM 2325 N ND1 . HIS A 1 292 ? 37.021 -15.512 -25.605 1.00 56.24 ? 292 HIS A ND1 1 ATOM 2326 C CD2 . HIS A 1 292 ? 36.359 -17.448 -26.356 1.00 57.22 ? 292 HIS A CD2 1 ATOM 2327 C CE1 . HIS A 1 292 ? 37.072 -16.360 -24.595 1.00 57.90 ? 292 HIS A CE1 1 ATOM 2328 N NE2 . HIS A 1 292 ? 36.677 -17.543 -25.025 1.00 58.33 ? 292 HIS A NE2 1 ATOM 2329 N N . ASN A 1 293 ? 39.160 -14.119 -28.055 1.00 49.69 ? 293 ASN A N 1 ATOM 2330 C CA . ASN A 1 293 ? 40.378 -13.675 -27.359 1.00 50.78 ? 293 ASN A CA 1 ATOM 2331 C C . ASN A 1 293 ? 40.080 -12.687 -26.218 1.00 52.44 ? 293 ASN A C 1 ATOM 2332 O O . ASN A 1 293 ? 40.905 -11.832 -25.881 1.00 52.54 ? 293 ASN A O 1 ATOM 2333 C CB . ASN A 1 293 ? 41.346 -13.046 -28.360 1.00 50.96 ? 293 ASN A CB 1 ATOM 2334 C CG . ASN A 1 293 ? 40.824 -11.744 -28.941 1.00 51.31 ? 293 ASN A CG 1 ATOM 2335 O OD1 . ASN A 1 293 ? 39.692 -11.337 -28.677 1.00 51.82 ? 293 ASN A OD1 1 ATOM 2336 N ND2 . ASN A 1 293 ? 41.650 -11.084 -29.737 1.00 52.25 ? 293 ASN A ND2 1 ATOM 2337 N N . ILE A 1 294 ? 38.893 -12.815 -25.629 1.00 53.06 ? 294 ILE A N 1 ATOM 2338 C CA . ILE A 1 294 ? 38.457 -11.934 -24.541 1.00 54.81 ? 294 ILE A CA 1 ATOM 2339 C C . ILE A 1 294 ? 39.191 -12.228 -23.231 1.00 54.73 ? 294 ILE A C 1 ATOM 2340 O O . ILE A 1 294 ? 39.815 -11.344 -22.659 1.00 55.45 ? 294 ILE A O 1 ATOM 2341 C CB . ILE A 1 294 ? 36.930 -12.041 -24.279 1.00 55.43 ? 294 ILE A CB 1 ATOM 2342 C CG1 . ILE A 1 294 ? 36.115 -11.873 -25.571 1.00 55.89 ? 294 ILE A CG1 1 ATOM 2343 C CG2 . ILE A 1 294 ? 36.500 -11.001 -23.259 1.00 55.98 ? 294 ILE A CG2 1 ATOM 2344 C CD1 . ILE A 1 294 ? 36.499 -10.659 -26.391 1.00 57.18 ? 294 ILE A CD1 1 ATOM 2345 N N . HIS A 1 295 ? 39.098 -13.468 -22.759 1.00 55.39 ? 295 HIS A N 1 ATOM 2346 C CA . HIS A 1 295 ? 39.631 -13.854 -21.456 1.00 56.75 ? 295 HIS A CA 1 ATOM 2347 C C . HIS A 1 295 ? 39.597 -15.393 -21.315 1.00 57.99 ? 295 HIS A C 1 ATOM 2348 O O . HIS A 1 295 ? 38.645 -16.024 -21.764 1.00 57.32 ? 295 HIS A O 1 ATOM 2349 C CB . HIS A 1 295 ? 38.772 -13.204 -20.375 1.00 57.59 ? 295 HIS A CB 1 ATOM 2350 C CG . HIS A 1 295 ? 39.384 -13.225 -19.017 1.00 60.09 ? 295 HIS A CG 1 ATOM 2351 N ND1 . HIS A 1 295 ? 39.483 -14.376 -18.271 1.00 61.93 ? 295 HIS A ND1 1 ATOM 2352 C CD2 . HIS A 1 295 ? 39.909 -12.237 -18.257 1.00 62.14 ? 295 HIS A CD2 1 ATOM 2353 C CE1 . HIS A 1 295 ? 40.058 -14.102 -17.115 1.00 63.55 ? 295 HIS A CE1 1 ATOM 2354 N NE2 . HIS A 1 295 ? 40.325 -12.811 -17.080 1.00 63.24 ? 295 HIS A NE2 1 ATOM 2355 N N . PRO A 1 296 ? 40.625 -16.002 -20.691 1.00 59.68 ? 296 PRO A N 1 ATOM 2356 C CA . PRO A 1 296 ? 40.650 -17.473 -20.600 1.00 61.55 ? 296 PRO A CA 1 ATOM 2357 C C . PRO A 1 296 ? 39.610 -18.118 -19.664 1.00 63.16 ? 296 PRO A C 1 ATOM 2358 O O . PRO A 1 296 ? 39.103 -19.194 -19.966 1.00 62.81 ? 296 PRO A O 1 ATOM 2359 C CB . PRO A 1 296 ? 42.072 -17.770 -20.102 1.00 63.23 ? 296 PRO A CB 1 ATOM 2360 C CG . PRO A 1 296 ? 42.521 -16.522 -19.437 1.00 63.00 ? 296 PRO A CG 1 ATOM 2361 C CD . PRO A 1 296 ? 41.877 -15.404 -20.200 1.00 60.96 ? 296 PRO A CD 1 ATOM 2362 N N . LEU A 1 297 ? 39.330 -17.493 -18.525 1.00 65.52 ? 297 LEU A N 1 ATOM 2363 C CA . LEU A 1 297 ? 38.362 -18.031 -17.554 1.00 67.81 ? 297 LEU A CA 1 ATOM 2364 C C . LEU A 1 297 ? 36.918 -17.699 -17.922 1.00 65.04 ? 297 LEU A C 1 ATOM 2365 O O . LEU A 1 297 ? 36.410 -16.652 -17.557 1.00 67.21 ? 297 LEU A O 1 ATOM 2366 C CB . LEU A 1 297 ? 38.673 -17.510 -16.141 1.00 68.98 ? 297 LEU A CB 1 ATOM 2367 C CG . LEU A 1 297 ? 40.101 -17.755 -15.628 1.00 73.49 ? 297 LEU A CG 1 ATOM 2368 C CD1 . LEU A 1 297 ? 40.364 -16.961 -14.349 1.00 74.87 ? 297 LEU A CD1 1 ATOM 2369 C CD2 . LEU A 1 297 ? 40.380 -19.241 -15.407 1.00 76.65 ? 297 LEU A CD2 1 ATOM 2370 N N . THR A 1 298 ? 36.255 -18.595 -18.640 1.00 63.94 ? 298 THR A N 1 ATOM 2371 C CA . THR A 1 298 ? 34.850 -18.397 -18.985 1.00 61.71 ? 298 THR A CA 1 ATOM 2372 C C . THR A 1 298 ? 33.983 -19.474 -18.353 1.00 63.52 ? 298 THR A C 1 ATOM 2373 O O . THR A 1 298 ? 34.488 -20.494 -17.887 1.00 63.30 ? 298 THR A O 1 ATOM 2374 C CB . THR A 1 298 ? 34.627 -18.416 -20.509 1.00 60.03 ? 298 THR A CB 1 ATOM 2375 O OG1 . THR A 1 298 ? 34.782 -19.745 -21.014 1.00 60.82 ? 298 THR A OG1 1 ATOM 2376 C CG2 . THR A 1 298 ? 35.614 -17.511 -21.199 1.00 59.37 ? 298 THR A CG2 1 ATOM 2377 N N . ILE A 1 299 ? 32.676 -19.227 -18.340 1.00 64.37 ? 299 ILE A N 1 ATOM 2378 C CA . ILE A 1 299 ? 31.696 -20.229 -17.928 1.00 68.22 ? 299 ILE A CA 1 ATOM 2379 C C . ILE A 1 299 ? 30.531 -20.214 -18.906 1.00 68.85 ? 299 ILE A C 1 ATOM 2380 O O . ILE A 1 299 ? 30.132 -19.147 -19.379 1.00 66.77 ? 299 ILE A O 1 ATOM 2381 C CB . ILE A 1 299 ? 31.198 -20.000 -16.478 1.00 70.78 ? 299 ILE A CB 1 ATOM 2382 C CG1 . ILE A 1 299 ? 30.202 -21.088 -16.072 1.00 73.92 ? 299 ILE A CG1 1 ATOM 2383 C CG2 . ILE A 1 299 ? 30.563 -18.623 -16.308 1.00 69.88 ? 299 ILE A CG2 1 ATOM 2384 C CD1 . ILE A 1 299 ? 29.906 -21.111 -14.591 1.00 76.24 ? 299 ILE A CD1 1 ATOM 2385 N N . GLY A 1 300 ? 30.003 -21.399 -19.205 1.00 72.80 ? 300 GLY A N 1 ATOM 2386 C CA . GLY A 1 300 ? 28.912 -21.555 -20.161 1.00 77.25 ? 300 GLY A CA 1 ATOM 2387 C C . GLY A 1 300 ? 29.366 -22.177 -21.473 1.00 80.97 ? 300 GLY A C 1 ATOM 2388 O O . GLY A 1 300 ? 30.518 -22.610 -21.603 1.00 81.83 ? 300 GLY A O 1 ATOM 2389 N N . GLU A 1 301 ? 28.455 -22.222 -22.446 1.00 85.10 ? 301 GLU A N 1 ATOM 2390 C CA . GLU A 1 301 ? 28.764 -22.746 -23.781 1.00 87.35 ? 301 GLU A CA 1 ATOM 2391 C C . GLU A 1 301 ? 29.506 -21.635 -24.517 1.00 81.45 ? 301 GLU A C 1 ATOM 2392 O O . GLU A 1 301 ? 28.892 -20.673 -24.984 1.00 78.70 ? 301 GLU A O 1 ATOM 2393 C CB . GLU A 1 301 ? 27.488 -23.161 -24.538 1.00 92.94 ? 301 GLU A CB 1 ATOM 2394 C CG . GLU A 1 301 ? 27.485 -24.602 -25.054 1.00 99.42 ? 301 GLU A CG 1 ATOM 2395 C CD . GLU A 1 301 ? 26.973 -25.613 -24.022 1.00 106.11 ? 301 GLU A CD 1 ATOM 2396 O OE1 . GLU A 1 301 ? 27.370 -25.526 -22.839 1.00 108.81 ? 301 GLU A OE1 1 ATOM 2397 O OE2 . GLU A 1 301 ? 26.171 -26.504 -24.391 1.00 110.41 ? 301 GLU A OE2 1 ATOM 2398 N N . CYS A 1 302 ? 30.830 -21.767 -24.587 1.00 78.80 ? 302 CYS A N 1 ATOM 2399 C CA . CYS A 1 302 ? 31.692 -20.695 -25.074 1.00 75.12 ? 302 CYS A CA 1 ATOM 2400 C C . CYS A 1 302 ? 32.560 -21.099 -26.260 1.00 72.15 ? 302 CYS A C 1 ATOM 2401 O O . CYS A 1 302 ? 32.848 -22.281 -26.463 1.00 71.76 ? 302 CYS A O 1 ATOM 2402 C CB . CYS A 1 302 ? 32.615 -20.214 -23.953 1.00 75.64 ? 302 CYS A CB 1 ATOM 2403 S SG . CYS A 1 302 ? 31.771 -19.374 -22.593 1.00 78.60 ? 302 CYS A SG 1 ATOM 2404 N N . PRO A 1 303 ? 32.998 -20.104 -27.043 1.00 68.70 ? 303 PRO A N 1 ATOM 2405 C CA . PRO A 1 303 ? 34.061 -20.355 -28.005 1.00 67.51 ? 303 PRO A CA 1 ATOM 2406 C C . PRO A 1 303 ? 35.378 -20.659 -27.288 1.00 67.09 ? 303 PRO A C 1 ATOM 2407 O O . PRO A 1 303 ? 35.507 -20.395 -26.093 1.00 66.73 ? 303 PRO A O 1 ATOM 2408 C CB . PRO A 1 303 ? 34.159 -19.039 -28.795 1.00 66.12 ? 303 PRO A CB 1 ATOM 2409 C CG . PRO A 1 303 ? 32.953 -18.239 -28.433 1.00 65.71 ? 303 PRO A CG 1 ATOM 2410 C CD . PRO A 1 303 ? 32.532 -18.707 -27.077 1.00 67.27 ? 303 PRO A CD 1 ATOM 2411 N N . LYS A 1 304 ? 36.349 -21.200 -28.013 1.00 66.78 ? 304 LYS A N 1 ATOM 2412 C CA . LYS A 1 304 ? 37.618 -21.584 -27.412 1.00 67.54 ? 304 LYS A CA 1 ATOM 2413 C C . LYS A 1 304 ? 38.556 -20.384 -27.381 1.00 63.65 ? 304 LYS A C 1 ATOM 2414 O O . LYS A 1 304 ? 38.677 -19.645 -28.356 1.00 63.48 ? 304 LYS A O 1 ATOM 2415 C CB . LYS A 1 304 ? 38.239 -22.758 -28.168 1.00 71.81 ? 304 LYS A CB 1 ATOM 2416 C CG . LYS A 1 304 ? 37.292 -23.952 -28.339 1.00 78.24 ? 304 LYS A CG 1 ATOM 2417 C CD . LYS A 1 304 ? 37.016 -24.681 -27.022 1.00 83.86 ? 304 LYS A CD 1 ATOM 2418 C CE . LYS A 1 304 ? 35.601 -25.245 -26.951 1.00 86.75 ? 304 LYS A CE 1 ATOM 2419 N NZ . LYS A 1 304 ? 35.466 -26.229 -25.837 1.00 91.53 ? 304 LYS A NZ 1 ATOM 2420 N N . TYR A 1 305 ? 39.203 -20.181 -26.244 1.00 61.31 ? 305 TYR A N 1 ATOM 2421 C CA . TYR A 1 305 ? 40.039 -19.020 -26.055 1.00 58.62 ? 305 TYR A CA 1 ATOM 2422 C C . TYR A 1 305 ? 41.400 -19.243 -26.683 1.00 59.44 ? 305 TYR A C 1 ATOM 2423 O O . TYR A 1 305 ? 42.038 -20.261 -26.431 1.00 62.13 ? 305 TYR A O 1 ATOM 2424 C CB . TYR A 1 305 ? 40.214 -18.709 -24.567 1.00 58.76 ? 305 TYR A CB 1 ATOM 2425 C CG . TYR A 1 305 ? 41.164 -17.563 -24.322 1.00 57.07 ? 305 TYR A CG 1 ATOM 2426 C CD1 . TYR A 1 305 ? 40.731 -16.244 -24.421 1.00 54.79 ? 305 TYR A CD1 1 ATOM 2427 C CD2 . TYR A 1 305 ? 42.499 -17.796 -24.032 1.00 58.01 ? 305 TYR A CD2 1 ATOM 2428 C CE1 . TYR A 1 305 ? 41.601 -15.191 -24.217 1.00 54.84 ? 305 TYR A CE1 1 ATOM 2429 C CE2 . TYR A 1 305 ? 43.376 -16.747 -23.823 1.00 58.92 ? 305 TYR A CE2 1 ATOM 2430 C CZ . TYR A 1 305 ? 42.921 -15.447 -23.915 1.00 57.05 ? 305 TYR A CZ 1 ATOM 2431 O OH . TYR A 1 305 ? 43.788 -14.400 -23.709 1.00 57.84 ? 305 TYR A OH 1 ATOM 2432 N N . VAL A 1 306 ? 41.836 -18.278 -27.491 1.00 58.22 ? 306 VAL A N 1 ATOM 2433 C CA . VAL A 1 306 ? 43.209 -18.230 -28.001 1.00 58.56 ? 306 VAL A CA 1 ATOM 2434 C C . VAL A 1 306 ? 43.779 -16.852 -27.712 1.00 58.38 ? 306 VAL A C 1 ATOM 2435 O O . VAL A 1 306 ? 43.034 -15.922 -27.442 1.00 57.97 ? 306 VAL A O 1 ATOM 2436 C CB . VAL A 1 306 ? 43.284 -18.520 -29.514 1.00 57.05 ? 306 VAL A CB 1 ATOM 2437 C CG1 . VAL A 1 306 ? 42.844 -19.942 -29.798 1.00 58.47 ? 306 VAL A CG1 1 ATOM 2438 C CG2 . VAL A 1 306 ? 42.426 -17.552 -30.310 1.00 55.32 ? 306 VAL A CG2 1 ATOM 2439 N N . LYS A 1 307 ? 45.095 -16.725 -27.782 1.00 61.22 ? 307 LYS A N 1 ATOM 2440 C CA . LYS A 1 307 ? 45.758 -15.438 -27.584 1.00 64.30 ? 307 LYS A CA 1 ATOM 2441 C C . LYS A 1 307 ? 45.907 -14.601 -28.869 1.00 63.87 ? 307 LYS A C 1 ATOM 2442 O O . LYS A 1 307 ? 46.583 -13.579 -28.848 1.00 68.23 ? 307 LYS A O 1 ATOM 2443 C CB . LYS A 1 307 ? 47.151 -15.643 -26.967 1.00 67.76 ? 307 LYS A CB 1 ATOM 2444 C CG . LYS A 1 307 ? 47.184 -15.662 -25.455 1.00 69.83 ? 307 LYS A CG 1 ATOM 2445 C CD . LYS A 1 307 ? 48.628 -15.704 -24.987 1.00 75.83 ? 307 LYS A CD 1 ATOM 2446 C CE . LYS A 1 307 ? 48.784 -16.334 -23.612 1.00 79.57 ? 307 LYS A CE 1 ATOM 2447 N NZ . LYS A 1 307 ? 50.213 -16.667 -23.342 1.00 84.68 ? 307 LYS A NZ 1 ATOM 2448 N N . SER A 1 308 ? 45.290 -15.011 -29.974 1.00 61.49 ? 308 SER A N 1 ATOM 2449 C CA . SER A 1 308 ? 45.472 -14.309 -31.250 1.00 60.73 ? 308 SER A CA 1 ATOM 2450 C C . SER A 1 308 ? 44.842 -12.929 -31.245 1.00 60.63 ? 308 SER A C 1 ATOM 2451 O O . SER A 1 308 ? 43.880 -12.677 -30.525 1.00 59.69 ? 308 SER A O 1 ATOM 2452 C CB . SER A 1 308 ? 44.854 -15.099 -32.408 1.00 57.96 ? 308 SER A CB 1 ATOM 2453 O OG . SER A 1 308 ? 45.219 -16.457 -32.347 1.00 59.04 ? 308 SER A OG 1 ATOM 2454 N N . ASN A 1 309 ? 45.382 -12.048 -32.077 1.00 63.97 ? 309 ASN A N 1 ATOM 2455 C CA . ASN A 1 309 ? 44.713 -10.796 -32.411 1.00 66.52 ? 309 ASN A CA 1 ATOM 2456 C C . ASN A 1 309 ? 43.829 -10.910 -33.656 1.00 63.53 ? 309 ASN A C 1 ATOM 2457 O O . ASN A 1 309 ? 42.990 -10.041 -33.894 1.00 64.84 ? 309 ASN A O 1 ATOM 2458 C CB . ASN A 1 309 ? 45.745 -9.683 -32.596 1.00 72.21 ? 309 ASN A CB 1 ATOM 2459 C CG . ASN A 1 309 ? 46.338 -9.220 -31.272 1.00 78.42 ? 309 ASN A CG 1 ATOM 2460 O OD1 . ASN A 1 309 ? 45.608 -8.959 -30.303 1.00 78.42 ? 309 ASN A OD1 1 ATOM 2461 N ND2 . ASN A 1 309 ? 47.667 -9.115 -31.219 1.00 83.29 ? 309 ASN A ND2 1 ATOM 2462 N N . ARG A 1 310 ? 43.999 -11.992 -34.421 1.00 60.44 ? 310 ARG A N 1 ATOM 2463 C CA . ARG A 1 310 ? 43.388 -12.125 -35.742 1.00 58.66 ? 310 ARG A CA 1 ATOM 2464 C C . ARG A 1 310 ? 43.402 -13.580 -36.250 1.00 56.11 ? 310 ARG A C 1 ATOM 2465 O O . ARG A 1 310 ? 44.452 -14.216 -36.306 1.00 56.57 ? 310 ARG A O 1 ATOM 2466 C CB . ARG A 1 310 ? 44.156 -11.227 -36.718 1.00 62.03 ? 310 ARG A CB 1 ATOM 2467 C CG . ARG A 1 310 ? 43.553 -11.096 -38.102 1.00 64.59 ? 310 ARG A CG 1 ATOM 2468 C CD . ARG A 1 310 ? 44.366 -10.151 -38.976 1.00 68.72 ? 310 ARG A CD 1 ATOM 2469 N NE . ARG A 1 310 ? 44.164 -10.436 -40.401 1.00 72.21 ? 310 ARG A NE 1 ATOM 2470 C CZ . ARG A 1 310 ? 43.124 -10.023 -41.128 1.00 73.15 ? 310 ARG A CZ 1 ATOM 2471 N NH1 . ARG A 1 310 ? 42.156 -9.283 -40.595 1.00 73.77 ? 310 ARG A NH1 1 ATOM 2472 N NH2 . ARG A 1 310 ? 43.056 -10.349 -42.409 1.00 74.34 ? 310 ARG A NH2 1 ATOM 2473 N N . LEU A 1 311 ? 42.236 -14.111 -36.605 1.00 53.25 ? 311 LEU A N 1 ATOM 2474 C CA . LEU A 1 311 ? 42.155 -15.411 -37.284 1.00 53.43 ? 311 LEU A CA 1 ATOM 2475 C C . LEU A 1 311 ? 41.137 -15.321 -38.410 1.00 51.73 ? 311 LEU A C 1 ATOM 2476 O O . LEU A 1 311 ? 39.926 -15.246 -38.164 1.00 51.47 ? 311 LEU A O 1 ATOM 2477 C CB . LEU A 1 311 ? 41.763 -16.541 -36.325 1.00 53.08 ? 311 LEU A CB 1 ATOM 2478 C CG . LEU A 1 311 ? 42.744 -16.901 -35.209 1.00 55.05 ? 311 LEU A CG 1 ATOM 2479 C CD1 . LEU A 1 311 ? 42.108 -17.881 -34.240 1.00 56.10 ? 311 LEU A CD1 1 ATOM 2480 C CD2 . LEU A 1 311 ? 44.028 -17.492 -35.757 1.00 57.49 ? 311 LEU A CD2 1 ATOM 2481 N N . VAL A 1 312 ? 41.632 -15.322 -39.644 1.00 50.46 ? 312 VAL A N 1 ATOM 2482 C CA . VAL A 1 312 ? 40.775 -15.175 -40.817 1.00 49.62 ? 312 VAL A CA 1 ATOM 2483 C C . VAL A 1 312 ? 41.144 -16.221 -41.849 1.00 48.79 ? 312 VAL A C 1 ATOM 2484 O O . VAL A 1 312 ? 42.287 -16.265 -42.292 1.00 48.12 ? 312 VAL A O 1 ATOM 2485 C CB . VAL A 1 312 ? 40.937 -13.782 -41.436 1.00 49.83 ? 312 VAL A CB 1 ATOM 2486 C CG1 . VAL A 1 312 ? 40.084 -13.653 -42.686 1.00 50.30 ? 312 VAL A CG1 1 ATOM 2487 C CG2 . VAL A 1 312 ? 40.581 -12.714 -40.409 1.00 49.89 ? 312 VAL A CG2 1 ATOM 2488 N N . LEU A 1 313 ? 40.178 -17.071 -42.197 1.00 48.95 ? 313 LEU A N 1 ATOM 2489 C CA . LEU A 1 313 ? 40.363 -18.116 -43.214 1.00 49.85 ? 313 LEU A CA 1 ATOM 2490 C C . LEU A 1 313 ? 39.996 -17.579 -44.585 1.00 50.47 ? 313 LEU A C 1 ATOM 2491 O O . LEU A 1 313 ? 39.020 -16.829 -44.723 1.00 52.20 ? 313 LEU A O 1 ATOM 2492 C CB . LEU A 1 313 ? 39.470 -19.330 -42.943 1.00 49.57 ? 313 LEU A CB 1 ATOM 2493 C CG . LEU A 1 313 ? 39.905 -20.321 -41.868 1.00 51.90 ? 313 LEU A CG 1 ATOM 2494 C CD1 . LEU A 1 313 ? 38.769 -21.280 -41.547 1.00 52.51 ? 313 LEU A CD1 1 ATOM 2495 C CD2 . LEU A 1 313 ? 41.142 -21.100 -42.300 1.00 53.43 ? 313 LEU A CD2 1 ATOM 2496 N N . ALA A 1 314 ? 40.767 -17.969 -45.596 1.00 49.44 ? 314 ALA A N 1 ATOM 2497 C CA . ALA A 1 314 ? 40.409 -17.689 -46.980 1.00 48.30 ? 314 ALA A CA 1 ATOM 2498 C C . ALA A 1 314 ? 39.360 -18.692 -47.406 1.00 47.80 ? 314 ALA A C 1 ATOM 2499 O O . ALA A 1 314 ? 39.489 -19.883 -47.117 1.00 46.74 ? 314 ALA A O 1 ATOM 2500 C CB . ALA A 1 314 ? 41.625 -17.790 -47.890 1.00 49.35 ? 314 ALA A CB 1 ATOM 2501 N N . THR A 1 315 ? 38.316 -18.198 -48.067 1.00 47.92 ? 315 THR A N 1 ATOM 2502 C CA . THR A 1 315 ? 37.326 -19.053 -48.726 1.00 49.41 ? 315 THR A CA 1 ATOM 2503 C C . THR A 1 315 ? 37.424 -18.867 -50.229 1.00 49.23 ? 315 THR A C 1 ATOM 2504 O O . THR A 1 315 ? 37.511 -19.832 -50.980 1.00 50.61 ? 315 THR A O 1 ATOM 2505 C CB . THR A 1 315 ? 35.895 -18.717 -48.277 1.00 50.45 ? 315 THR A CB 1 ATOM 2506 O OG1 . THR A 1 315 ? 35.765 -17.297 -48.123 1.00 51.01 ? 315 THR A OG1 1 ATOM 2507 C CG2 . THR A 1 315 ? 35.578 -19.394 -46.950 1.00 51.21 ? 315 THR A CG2 1 ATOM 2508 N N . GLY A 1 316 ? 37.426 -17.615 -50.660 1.00 48.55 ? 316 GLY A N 1 ATOM 2509 C CA . GLY A 1 316 ? 37.578 -17.294 -52.064 1.00 48.40 ? 316 GLY A CA 1 ATOM 2510 C C . GLY A 1 316 ? 39.016 -17.375 -52.521 1.00 48.62 ? 316 GLY A C 1 ATOM 2511 O O . GLY A 1 316 ? 39.875 -17.971 -51.855 1.00 47.47 ? 316 GLY A O 1 ATOM 2512 N N . LEU A 1 317 ? 39.281 -16.742 -53.654 1.00 48.81 ? 317 LEU A N 1 ATOM 2513 C CA . LEU A 1 317 ? 40.576 -16.851 -54.296 1.00 50.07 ? 317 LEU A CA 1 ATOM 2514 C C . LEU A 1 317 ? 41.255 -15.490 -54.342 1.00 49.68 ? 317 LEU A C 1 ATOM 2515 O O . LEU A 1 317 ? 40.667 -14.483 -53.958 1.00 48.84 ? 317 LEU A O 1 ATOM 2516 C CB . LEU A 1 317 ? 40.436 -17.484 -55.690 1.00 51.75 ? 317 LEU A CB 1 ATOM 2517 C CG . LEU A 1 317 ? 39.386 -16.927 -56.652 1.00 52.83 ? 317 LEU A CG 1 ATOM 2518 C CD1 . LEU A 1 317 ? 39.841 -15.584 -57.195 1.00 54.86 ? 317 LEU A CD1 1 ATOM 2519 C CD2 . LEU A 1 317 ? 39.127 -17.896 -57.791 1.00 53.00 ? 317 LEU A CD2 1 ATOM 2520 N N . ARG A 1 318 ? 42.506 -15.486 -54.784 1.00 49.71 ? 318 ARG A N 1 ATOM 2521 C CA . ARG A 1 318 ? 43.322 -14.283 -54.813 1.00 51.94 ? 318 ARG A CA 1 ATOM 2522 C C . ARG A 1 318 ? 42.697 -13.234 -55.714 1.00 52.87 ? 318 ARG A C 1 ATOM 2523 O O . ARG A 1 318 ? 42.522 -13.456 -56.910 1.00 51.86 ? 318 ARG A O 1 ATOM 2524 C CB . ARG A 1 318 ? 44.733 -14.625 -55.299 1.00 54.04 ? 318 ARG A CB 1 ATOM 2525 C CG . ARG A 1 318 ? 45.710 -13.465 -55.274 1.00 57.74 ? 318 ARG A CG 1 ATOM 2526 C CD . ARG A 1 318 ? 47.041 -13.857 -55.886 1.00 61.02 ? 318 ARG A CD 1 ATOM 2527 N NE . ARG A 1 318 ? 47.842 -14.660 -54.964 1.00 62.71 ? 318 ARG A NE 1 ATOM 2528 C CZ . ARG A 1 318 ? 48.751 -14.173 -54.122 1.00 65.37 ? 318 ARG A CZ 1 ATOM 2529 N NH1 . ARG A 1 318 ? 49.000 -12.867 -54.057 1.00 66.32 ? 318 ARG A NH1 1 ATOM 2530 N NH2 . ARG A 1 318 ? 49.420 -15.007 -53.333 1.00 67.93 ? 318 ARG A NH2 1 ATOM 2531 N N . ASN A 1 319 ? 42.382 -12.086 -55.127 1.00 56.38 ? 319 ASN A N 1 ATOM 2532 C CA . ASN A 1 319 ? 41.659 -11.029 -55.814 1.00 60.12 ? 319 ASN A CA 1 ATOM 2533 C C . ASN A 1 319 ? 42.589 -10.092 -56.563 1.00 67.76 ? 319 ASN A C 1 ATOM 2534 O O . ASN A 1 319 ? 43.604 -9.648 -56.034 1.00 71.83 ? 319 ASN A O 1 ATOM 2535 C CB . ASN A 1 319 ? 40.828 -10.228 -54.822 1.00 59.22 ? 319 ASN A CB 1 ATOM 2536 C CG . ASN A 1 319 ? 39.739 -9.428 -55.493 1.00 59.43 ? 319 ASN A CG 1 ATOM 2537 O OD1 . ASN A 1 319 ? 39.452 -9.622 -56.668 1.00 58.63 ? 319 ASN A OD1 1 ATOM 2538 N ND2 . ASN A 1 319 ? 39.116 -8.528 -54.744 1.00 60.56 ? 319 ASN A ND2 1 ATOM 2539 N N . SER A 1 320 ? 42.210 -9.783 -57.796 1.00 77.35 ? 320 SER A N 1 ATOM 2540 C CA . SER A 1 320 ? 43.057 -9.043 -58.724 1.00 85.32 ? 320 SER A CA 1 ATOM 2541 C C . SER A 1 320 ? 43.033 -7.544 -58.425 1.00 90.32 ? 320 SER A C 1 ATOM 2542 O O . SER A 1 320 ? 41.984 -7.006 -58.067 1.00 88.15 ? 320 SER A O 1 ATOM 2543 C CB . SER A 1 320 ? 42.586 -9.290 -60.166 1.00 85.15 ? 320 SER A CB 1 ATOM 2544 O OG . SER A 1 320 ? 42.363 -10.672 -60.390 1.00 81.96 ? 320 SER A OG 1 ATOM 2545 N N . PRO A 1 321 ? 44.192 -6.871 -58.566 1.00 99.42 ? 321 PRO A N 1 ATOM 2546 C CA . PRO A 1 321 ? 44.258 -5.413 -58.468 1.00 105.56 ? 321 PRO A CA 1 ATOM 2547 C C . PRO A 1 321 ? 43.931 -4.738 -59.800 1.00 106.02 ? 321 PRO A C 1 ATOM 2548 O O . PRO A 1 321 ? 42.802 -4.290 -60.002 1.00 105.14 ? 321 PRO A O 1 ATOM 2549 C CB . PRO A 1 321 ? 45.715 -5.158 -58.069 1.00 108.03 ? 321 PRO A CB 1 ATOM 2550 C CG . PRO A 1 321 ? 46.472 -6.289 -58.679 1.00 106.79 ? 321 PRO A CG 1 ATOM 2551 C CD . PRO A 1 321 ? 45.535 -7.470 -58.723 1.00 102.77 ? 321 PRO A CD 1 ATOM 2552 N N . GLY B 2 1 ? 50.974 -18.657 -57.992 1.00 48.43 ? 1 GLY B N 1 ATOM 2553 C CA . GLY B 2 1 ? 50.442 -19.895 -57.353 1.00 46.31 ? 1 GLY B CA 1 ATOM 2554 C C . GLY B 2 1 ? 51.157 -21.129 -57.860 1.00 46.49 ? 1 GLY B C 1 ATOM 2555 O O . GLY B 2 1 ? 51.830 -21.094 -58.889 1.00 48.38 ? 1 GLY B O 1 ATOM 2556 N N . LEU B 2 2 ? 51.003 -22.234 -57.147 1.00 45.04 ? 2 LEU B N 1 ATOM 2557 C CA . LEU B 2 2 ? 51.714 -23.448 -57.506 1.00 44.85 ? 2 LEU B CA 1 ATOM 2558 C C . LEU B 2 2 ? 51.344 -23.966 -58.903 1.00 45.17 ? 2 LEU B C 1 ATOM 2559 O O . LEU B 2 2 ? 52.171 -24.586 -59.564 1.00 46.67 ? 2 LEU B O 1 ATOM 2560 C CB . LEU B 2 2 ? 51.450 -24.537 -56.476 1.00 43.58 ? 2 LEU B CB 1 ATOM 2561 C CG . LEU B 2 2 ? 52.105 -24.402 -55.111 1.00 43.47 ? 2 LEU B CG 1 ATOM 2562 C CD1 . LEU B 2 2 ? 51.708 -25.586 -54.242 1.00 42.49 ? 2 LEU B CD1 1 ATOM 2563 C CD2 . LEU B 2 2 ? 53.617 -24.308 -55.226 1.00 45.46 ? 2 LEU B CD2 1 ATOM 2564 N N . PHE B 2 3 ? 50.119 -23.704 -59.353 1.00 43.87 ? 3 PHE B N 1 ATOM 2565 C CA . PHE B 2 3 ? 49.602 -24.331 -60.577 1.00 44.53 ? 3 PHE B CA 1 ATOM 2566 C C . PHE B 2 3 ? 49.655 -23.436 -61.796 1.00 46.13 ? 3 PHE B C 1 ATOM 2567 O O . PHE B 2 3 ? 49.300 -23.859 -62.894 1.00 46.86 ? 3 PHE B O 1 ATOM 2568 C CB . PHE B 2 3 ? 48.198 -24.888 -60.324 1.00 43.08 ? 3 PHE B CB 1 ATOM 2569 C CG . PHE B 2 3 ? 48.209 -26.000 -59.325 1.00 42.86 ? 3 PHE B CG 1 ATOM 2570 C CD1 . PHE B 2 3 ? 48.164 -25.720 -57.960 1.00 42.56 ? 3 PHE B CD1 1 ATOM 2571 C CD2 . PHE B 2 3 ? 48.374 -27.312 -59.734 1.00 42.64 ? 3 PHE B CD2 1 ATOM 2572 C CE1 . PHE B 2 3 ? 48.250 -26.737 -57.022 1.00 42.18 ? 3 PHE B CE1 1 ATOM 2573 C CE2 . PHE B 2 3 ? 48.449 -28.331 -58.804 1.00 43.71 ? 3 PHE B CE2 1 ATOM 2574 C CZ . PHE B 2 3 ? 48.389 -28.045 -57.444 1.00 42.71 ? 3 PHE B CZ 1 ATOM 2575 N N . GLY B 2 4 ? 50.120 -22.206 -61.593 1.00 47.17 ? 4 GLY B N 1 ATOM 2576 C CA . GLY B 2 4 ? 50.469 -21.317 -62.677 1.00 47.92 ? 4 GLY B CA 1 ATOM 2577 C C . GLY B 2 4 ? 49.340 -20.569 -63.347 1.00 47.58 ? 4 GLY B C 1 ATOM 2578 O O . GLY B 2 4 ? 49.605 -19.698 -64.166 1.00 51.58 ? 4 GLY B O 1 ATOM 2579 N N . ALA B 2 5 ? 48.087 -20.883 -63.037 1.00 45.40 ? 5 ALA B N 1 ATOM 2580 C CA . ALA B 2 5 ? 46.975 -20.265 -63.762 1.00 44.64 ? 5 ALA B CA 1 ATOM 2581 C C . ALA B 2 5 ? 46.615 -18.909 -63.194 1.00 44.57 ? 5 ALA B C 1 ATOM 2582 O O . ALA B 2 5 ? 46.763 -17.897 -63.869 1.00 45.12 ? 5 ALA B O 1 ATOM 2583 C CB . ALA B 2 5 ? 45.757 -21.175 -63.770 1.00 43.90 ? 5 ALA B CB 1 ATOM 2584 N N . ILE B 2 6 ? 46.145 -18.894 -61.950 1.00 44.71 ? 6 ILE B N 1 ATOM 2585 C CA . ILE B 2 6 ? 45.689 -17.655 -61.310 1.00 45.79 ? 6 ILE B CA 1 ATOM 2586 C C . ILE B 2 6 ? 46.849 -16.674 -61.129 1.00 47.31 ? 6 ILE B C 1 ATOM 2587 O O . ILE B 2 6 ? 47.898 -17.021 -60.578 1.00 46.43 ? 6 ILE B O 1 ATOM 2588 C CB . ILE B 2 6 ? 45.006 -17.938 -59.955 1.00 45.58 ? 6 ILE B CB 1 ATOM 2589 C CG1 . ILE B 2 6 ? 43.634 -18.560 -60.197 1.00 45.40 ? 6 ILE B CG1 1 ATOM 2590 C CG2 . ILE B 2 6 ? 44.858 -16.659 -59.139 1.00 46.60 ? 6 ILE B CG2 1 ATOM 2591 C CD1 . ILE B 2 6 ? 42.963 -19.094 -58.953 1.00 45.34 ? 6 ILE B CD1 1 ATOM 2592 N N . ALA B 2 7 ? 46.651 -15.452 -61.613 1.00 48.66 ? 7 ALA B N 1 ATOM 2593 C CA . ALA B 2 7 ? 47.702 -14.437 -61.607 1.00 51.05 ? 7 ALA B CA 1 ATOM 2594 C C . ALA B 2 7 ? 48.997 -14.990 -62.184 1.00 52.34 ? 7 ALA B C 1 ATOM 2595 O O . ALA B 2 7 ? 50.073 -14.707 -61.681 1.00 54.63 ? 7 ALA B O 1 ATOM 2596 C CB . ALA B 2 7 ? 47.924 -13.914 -60.195 1.00 51.08 ? 7 ALA B CB 1 ATOM 2597 N N . GLY B 2 8 ? 48.878 -15.787 -63.240 1.00 52.91 ? 8 GLY B N 1 ATOM 2598 C CA . GLY B 2 8 ? 50.024 -16.408 -63.899 1.00 54.33 ? 8 GLY B CA 1 ATOM 2599 C C . GLY B 2 8 ? 49.866 -16.252 -65.394 1.00 55.72 ? 8 GLY B C 1 ATOM 2600 O O . GLY B 2 8 ? 50.077 -15.165 -65.913 1.00 58.56 ? 8 GLY B O 1 ATOM 2601 N N . PHE B 2 9 ? 49.487 -17.317 -66.097 1.00 54.48 ? 9 PHE B N 1 ATOM 2602 C CA . PHE B 2 9 ? 49.250 -17.191 -67.525 1.00 56.16 ? 9 PHE B CA 1 ATOM 2603 C C . PHE B 2 9 ? 47.865 -16.578 -67.754 1.00 56.81 ? 9 PHE B C 1 ATOM 2604 O O . PHE B 2 9 ? 47.607 -15.991 -68.808 1.00 59.04 ? 9 PHE B O 1 ATOM 2605 C CB . PHE B 2 9 ? 49.488 -18.507 -68.290 1.00 56.41 ? 9 PHE B CB 1 ATOM 2606 C CG . PHE B 2 9 ? 48.455 -19.573 -68.052 1.00 54.39 ? 9 PHE B CG 1 ATOM 2607 C CD1 . PHE B 2 9 ? 47.264 -19.575 -68.762 1.00 54.05 ? 9 PHE B CD1 1 ATOM 2608 C CD2 . PHE B 2 9 ? 48.697 -20.602 -67.159 1.00 53.31 ? 9 PHE B CD2 1 ATOM 2609 C CE1 . PHE B 2 9 ? 46.310 -20.562 -68.553 1.00 52.88 ? 9 PHE B CE1 1 ATOM 2610 C CE2 . PHE B 2 9 ? 47.755 -21.595 -66.951 1.00 52.44 ? 9 PHE B CE2 1 ATOM 2611 C CZ . PHE B 2 9 ? 46.555 -21.571 -67.642 1.00 51.86 ? 9 PHE B CZ 1 ATOM 2612 N N . ILE B 2 10 ? 46.987 -16.696 -66.759 1.00 55.70 ? 10 ILE B N 1 ATOM 2613 C CA . ILE B 2 10 ? 45.766 -15.896 -66.716 1.00 56.38 ? 10 ILE B CA 1 ATOM 2614 C C . ILE B 2 10 ? 46.053 -14.727 -65.782 1.00 59.61 ? 10 ILE B C 1 ATOM 2615 O O . ILE B 2 10 ? 46.181 -14.899 -64.571 1.00 61.11 ? 10 ILE B O 1 ATOM 2616 C CB . ILE B 2 10 ? 44.548 -16.708 -66.250 1.00 53.83 ? 10 ILE B CB 1 ATOM 2617 C CG1 . ILE B 2 10 ? 44.430 -17.983 -67.083 1.00 53.20 ? 10 ILE B CG1 1 ATOM 2618 C CG2 . ILE B 2 10 ? 43.277 -15.878 -66.384 1.00 53.33 ? 10 ILE B CG2 1 ATOM 2619 C CD1 . ILE B 2 10 ? 43.296 -18.888 -66.668 1.00 52.47 ? 10 ILE B CD1 1 ATOM 2620 N N . GLU B 2 11 ? 46.164 -13.538 -66.359 1.00 63.92 ? 11 GLU B N 1 ATOM 2621 C CA . GLU B 2 11 ? 46.754 -12.395 -65.667 1.00 67.31 ? 11 GLU B CA 1 ATOM 2622 C C . GLU B 2 11 ? 45.897 -11.824 -64.553 1.00 64.71 ? 11 GLU B C 1 ATOM 2623 O O . GLU B 2 11 ? 46.420 -11.281 -63.585 1.00 65.40 ? 11 GLU B O 1 ATOM 2624 C CB . GLU B 2 11 ? 47.066 -11.279 -66.661 1.00 73.83 ? 11 GLU B CB 1 ATOM 2625 C CG . GLU B 2 11 ? 48.351 -11.482 -67.443 1.00 79.37 ? 11 GLU B CG 1 ATOM 2626 C CD . GLU B 2 11 ? 48.969 -10.162 -67.863 1.00 87.11 ? 11 GLU B CD 1 ATOM 2627 O OE1 . GLU B 2 11 ? 48.226 -9.298 -68.395 1.00 89.70 ? 11 GLU B OE1 1 ATOM 2628 O OE2 . GLU B 2 11 ? 50.193 -9.988 -67.646 1.00 92.12 ? 11 GLU B OE2 1 ATOM 2629 N N . GLY B 2 12 ? 44.585 -11.918 -64.703 1.00 62.51 ? 12 GLY B N 1 ATOM 2630 C CA . GLY B 2 12 ? 43.671 -11.395 -63.695 1.00 61.66 ? 12 GLY B CA 1 ATOM 2631 C C . GLY B 2 12 ? 42.297 -12.020 -63.778 1.00 59.22 ? 12 GLY B C 1 ATOM 2632 O O . GLY B 2 12 ? 41.959 -12.685 -64.757 1.00 59.16 ? 12 GLY B O 1 ATOM 2633 N N . GLY B 2 13 ? 41.511 -11.809 -62.732 1.00 58.01 ? 13 GLY B N 1 ATOM 2634 C CA . GLY B 2 13 ? 40.137 -12.278 -62.686 1.00 56.81 ? 13 GLY B CA 1 ATOM 2635 C C . GLY B 2 13 ? 39.177 -11.347 -63.410 1.00 57.66 ? 13 GLY B C 1 ATOM 2636 O O . GLY B 2 13 ? 39.575 -10.306 -63.935 1.00 58.35 ? 13 GLY B O 1 ATOM 2637 N N . TRP B 2 14 ? 37.904 -11.735 -63.412 1.00 56.85 ? 14 TRP B N 1 ATOM 2638 C CA . TRP B 2 14 ? 36.858 -11.047 -64.140 1.00 56.84 ? 14 TRP B CA 1 ATOM 2639 C C . TRP B 2 14 ? 35.800 -10.474 -63.208 1.00 59.74 ? 14 TRP B C 1 ATOM 2640 O O . TRP B 2 14 ? 35.059 -11.214 -62.563 1.00 57.57 ? 14 TRP B O 1 ATOM 2641 C CB . TRP B 2 14 ? 36.190 -12.020 -65.103 1.00 54.74 ? 14 TRP B CB 1 ATOM 2642 C CG . TRP B 2 14 ? 37.058 -12.455 -66.238 1.00 53.54 ? 14 TRP B CG 1 ATOM 2643 C CD1 . TRP B 2 14 ? 38.071 -11.748 -66.819 1.00 53.92 ? 14 TRP B CD1 1 ATOM 2644 C CD2 . TRP B 2 14 ? 36.959 -13.685 -66.969 1.00 51.49 ? 14 TRP B CD2 1 ATOM 2645 N NE1 . TRP B 2 14 ? 38.613 -12.465 -67.859 1.00 53.18 ? 14 TRP B NE1 1 ATOM 2646 C CE2 . TRP B 2 14 ? 37.947 -13.656 -67.972 1.00 51.89 ? 14 TRP B CE2 1 ATOM 2647 C CE3 . TRP B 2 14 ? 36.128 -14.801 -66.877 1.00 50.11 ? 14 TRP B CE3 1 ATOM 2648 C CZ2 . TRP B 2 14 ? 38.136 -14.710 -68.866 1.00 50.99 ? 14 TRP B CZ2 1 ATOM 2649 C CZ3 . TRP B 2 14 ? 36.310 -15.837 -67.766 1.00 49.67 ? 14 TRP B CZ3 1 ATOM 2650 C CH2 . TRP B 2 14 ? 37.309 -15.788 -68.749 1.00 49.86 ? 14 TRP B CH2 1 ATOM 2651 N N . GLN B 2 15 ? 35.720 -9.146 -63.161 1.00 64.85 ? 15 GLN B N 1 ATOM 2652 C CA . GLN B 2 15 ? 34.638 -8.461 -62.453 1.00 68.48 ? 15 GLN B CA 1 ATOM 2653 C C . GLN B 2 15 ? 33.290 -8.874 -63.042 1.00 68.17 ? 15 GLN B C 1 ATOM 2654 O O . GLN B 2 15 ? 32.305 -9.002 -62.320 1.00 69.29 ? 15 GLN B O 1 ATOM 2655 C CB . GLN B 2 15 ? 34.795 -6.931 -62.542 1.00 71.86 ? 15 GLN B CB 1 ATOM 2656 C CG . GLN B 2 15 ? 36.012 -6.347 -61.824 1.00 73.51 ? 15 GLN B CG 1 ATOM 2657 C CD . GLN B 2 15 ? 35.847 -6.244 -60.313 1.00 75.38 ? 15 GLN B CD 1 ATOM 2658 O OE1 . GLN B 2 15 ? 36.719 -6.672 -59.557 1.00 76.35 ? 15 GLN B OE1 1 ATOM 2659 N NE2 . GLN B 2 15 ? 34.732 -5.673 -59.866 1.00 78.04 ? 15 GLN B NE2 1 ATOM 2660 N N . GLY B 2 16 ? 33.259 -9.084 -64.355 1.00 67.66 ? 16 GLY B N 1 ATOM 2661 C CA . GLY B 2 16 ? 32.025 -9.414 -65.064 1.00 68.77 ? 16 GLY B CA 1 ATOM 2662 C C . GLY B 2 16 ? 31.425 -10.789 -64.800 1.00 68.11 ? 16 GLY B C 1 ATOM 2663 O O . GLY B 2 16 ? 30.243 -10.999 -65.067 1.00 70.61 ? 16 GLY B O 1 ATOM 2664 N N . MET B 2 17 ? 32.214 -11.733 -64.290 1.00 65.82 ? 17 MET B N 1 ATOM 2665 C CA . MET B 2 17 ? 31.685 -13.064 -63.979 1.00 65.81 ? 17 MET B CA 1 ATOM 2666 C C . MET B 2 17 ? 31.251 -13.161 -62.517 1.00 66.39 ? 17 MET B C 1 ATOM 2667 O O . MET B 2 17 ? 32.069 -13.362 -61.623 1.00 65.32 ? 17 MET B O 1 ATOM 2668 C CB . MET B 2 17 ? 32.704 -14.155 -64.288 1.00 64.46 ? 17 MET B CB 1 ATOM 2669 C CG . MET B 2 17 ? 32.108 -15.542 -64.145 1.00 64.40 ? 17 MET B CG 1 ATOM 2670 S SD . MET B 2 17 ? 33.209 -16.806 -64.756 1.00 62.97 ? 17 MET B SD 1 ATOM 2671 C CE . MET B 2 17 ? 34.617 -16.498 -63.693 1.00 63.22 ? 17 MET B CE 1 ATOM 2672 N N . VAL B 2 18 ? 29.947 -13.053 -62.296 1.00 69.40 ? 18 VAL B N 1 ATOM 2673 C CA . VAL B 2 18 ? 29.388 -12.851 -60.962 1.00 70.75 ? 18 VAL B CA 1 ATOM 2674 C C . VAL B 2 18 ? 28.819 -14.126 -60.347 1.00 70.22 ? 18 VAL B C 1 ATOM 2675 O O . VAL B 2 18 ? 28.801 -14.272 -59.129 1.00 71.30 ? 18 VAL B O 1 ATOM 2676 C CB . VAL B 2 18 ? 28.284 -11.781 -61.016 1.00 74.38 ? 18 VAL B CB 1 ATOM 2677 C CG1 . VAL B 2 18 ? 27.704 -11.528 -59.634 1.00 78.20 ? 18 VAL B CG1 1 ATOM 2678 C CG2 . VAL B 2 18 ? 28.842 -10.493 -61.604 1.00 75.35 ? 18 VAL B CG2 1 ATOM 2679 N N . ASP B 2 19 ? 28.378 -15.057 -61.184 1.00 69.79 ? 19 ASP B N 1 ATOM 2680 C CA . ASP B 2 19 ? 27.620 -16.214 -60.709 1.00 70.12 ? 19 ASP B CA 1 ATOM 2681 C C . ASP B 2 19 ? 28.458 -17.496 -60.614 1.00 65.67 ? 19 ASP B C 1 ATOM 2682 O O . ASP B 2 19 ? 27.933 -18.601 -60.701 1.00 66.65 ? 19 ASP B O 1 ATOM 2683 C CB . ASP B 2 19 ? 26.374 -16.421 -61.590 1.00 73.27 ? 19 ASP B CB 1 ATOM 2684 C CG . ASP B 2 19 ? 26.702 -16.518 -63.074 1.00 73.77 ? 19 ASP B CG 1 ATOM 2685 O OD1 . ASP B 2 19 ? 27.898 -16.474 -63.458 1.00 71.74 ? 19 ASP B OD1 1 ATOM 2686 O OD2 . ASP B 2 19 ? 25.745 -16.635 -63.862 1.00 77.77 ? 19 ASP B OD2 1 ATOM 2687 N N . GLY B 2 20 ? 29.758 -17.353 -60.411 1.00 61.51 ? 20 GLY B N 1 ATOM 2688 C CA . GLY B 2 20 ? 30.608 -18.518 -60.217 1.00 59.51 ? 20 GLY B CA 1 ATOM 2689 C C . GLY B 2 20 ? 32.039 -18.127 -59.930 1.00 57.99 ? 20 GLY B C 1 ATOM 2690 O O . GLY B 2 20 ? 32.417 -16.967 -60.094 1.00 59.07 ? 20 GLY B O 1 ATOM 2691 N N . TRP B 2 21 ? 32.839 -19.097 -59.499 1.00 56.17 ? 21 TRP B N 1 ATOM 2692 C CA . TRP B 2 21 ? 34.242 -18.838 -59.186 1.00 54.52 ? 21 TRP B CA 1 ATOM 2693 C C . TRP B 2 21 ? 35.127 -19.008 -60.409 1.00 50.75 ? 21 TRP B C 1 ATOM 2694 O O . TRP B 2 21 ? 36.120 -18.309 -60.554 1.00 48.89 ? 21 TRP B O 1 ATOM 2695 C CB . TRP B 2 21 ? 34.732 -19.749 -58.055 1.00 55.80 ? 21 TRP B CB 1 ATOM 2696 C CG . TRP B 2 21 ? 34.682 -19.125 -56.688 1.00 58.22 ? 21 TRP B CG 1 ATOM 2697 C CD1 . TRP B 2 21 ? 34.925 -17.818 -56.355 1.00 59.69 ? 21 TRP B CD1 1 ATOM 2698 C CD2 . TRP B 2 21 ? 34.421 -19.800 -55.471 1.00 60.78 ? 21 TRP B CD2 1 ATOM 2699 N NE1 . TRP B 2 21 ? 34.813 -17.641 -54.999 1.00 60.17 ? 21 TRP B NE1 1 ATOM 2700 C CE2 . TRP B 2 21 ? 34.501 -18.846 -54.433 1.00 61.42 ? 21 TRP B CE2 1 ATOM 2701 C CE3 . TRP B 2 21 ? 34.135 -21.125 -55.150 1.00 63.93 ? 21 TRP B CE3 1 ATOM 2702 C CZ2 . TRP B 2 21 ? 34.292 -19.175 -53.105 1.00 65.07 ? 21 TRP B CZ2 1 ATOM 2703 C CZ3 . TRP B 2 21 ? 33.931 -21.456 -53.825 1.00 67.45 ? 21 TRP B CZ3 1 ATOM 2704 C CH2 . TRP B 2 21 ? 34.008 -20.484 -52.816 1.00 67.34 ? 21 TRP B CH2 1 ATOM 2705 N N . TYR B 2 22 ? 34.763 -19.953 -61.270 1.00 48.94 ? 22 TYR B N 1 ATOM 2706 C CA . TYR B 2 22 ? 35.483 -20.209 -62.505 1.00 47.26 ? 22 TYR B CA 1 ATOM 2707 C C . TYR B 2 22 ? 34.489 -20.327 -63.637 1.00 47.63 ? 22 TYR B C 1 ATOM 2708 O O . TYR B 2 22 ? 33.347 -20.742 -63.427 1.00 47.67 ? 22 TYR B O 1 ATOM 2709 C CB . TYR B 2 22 ? 36.259 -21.526 -62.417 1.00 46.54 ? 22 TYR B CB 1 ATOM 2710 C CG . TYR B 2 22 ? 36.711 -21.903 -61.028 1.00 45.72 ? 22 TYR B CG 1 ATOM 2711 C CD1 . TYR B 2 22 ? 37.692 -21.173 -60.380 1.00 44.93 ? 22 TYR B CD1 1 ATOM 2712 C CD2 . TYR B 2 22 ? 36.163 -23.001 -60.367 1.00 46.19 ? 22 TYR B CD2 1 ATOM 2713 C CE1 . TYR B 2 22 ? 38.113 -21.517 -59.111 1.00 44.48 ? 22 TYR B CE1 1 ATOM 2714 C CE2 . TYR B 2 22 ? 36.581 -23.352 -59.098 1.00 45.46 ? 22 TYR B CE2 1 ATOM 2715 C CZ . TYR B 2 22 ? 37.557 -22.604 -58.480 1.00 44.52 ? 22 TYR B CZ 1 ATOM 2716 O OH . TYR B 2 22 ? 37.993 -22.932 -57.230 1.00 44.22 ? 22 TYR B OH 1 ATOM 2717 N N . GLY B 2 23 ? 34.927 -19.983 -64.843 1.00 47.45 ? 23 GLY B N 1 ATOM 2718 C CA . GLY B 2 23 ? 34.068 -20.109 -66.008 1.00 48.54 ? 23 GLY B CA 1 ATOM 2719 C C . GLY B 2 23 ? 34.721 -19.675 -67.297 1.00 48.93 ? 23 GLY B C 1 ATOM 2720 O O . GLY B 2 23 ? 35.954 -19.627 -67.399 1.00 47.97 ? 23 GLY B O 1 ATOM 2721 N N . TYR B 2 24 ? 33.876 -19.346 -68.271 1.00 50.89 ? 24 TYR B N 1 ATOM 2722 C CA . TYR B 2 24 ? 34.301 -19.062 -69.639 1.00 51.84 ? 24 TYR B CA 1 ATOM 2723 C C . TYR B 2 24 ? 33.890 -17.668 -70.071 1.00 52.02 ? 24 TYR B C 1 ATOM 2724 O O . TYR B 2 24 ? 32.892 -17.138 -69.593 1.00 53.06 ? 24 TYR B O 1 ATOM 2725 C CB . TYR B 2 24 ? 33.646 -20.048 -70.607 1.00 54.03 ? 24 TYR B CB 1 ATOM 2726 C CG . TYR B 2 24 ? 33.706 -21.490 -70.174 1.00 55.14 ? 24 TYR B CG 1 ATOM 2727 C CD1 . TYR B 2 24 ? 32.760 -22.009 -69.299 1.00 56.24 ? 24 TYR B CD1 1 ATOM 2728 C CD2 . TYR B 2 24 ? 34.695 -22.338 -70.650 1.00 55.97 ? 24 TYR B CD2 1 ATOM 2729 C CE1 . TYR B 2 24 ? 32.800 -23.328 -68.898 1.00 57.07 ? 24 TYR B CE1 1 ATOM 2730 C CE2 . TYR B 2 24 ? 34.746 -23.662 -70.250 1.00 57.41 ? 24 TYR B CE2 1 ATOM 2731 C CZ . TYR B 2 24 ? 33.798 -24.149 -69.372 1.00 58.19 ? 24 TYR B CZ 1 ATOM 2732 O OH . TYR B 2 24 ? 33.839 -25.464 -68.971 1.00 61.79 ? 24 TYR B OH 1 ATOM 2733 N N . HIS B 2 25 ? 34.650 -17.087 -70.994 1.00 52.00 ? 25 HIS B N 1 ATOM 2734 C CA . HIS B 2 25 ? 34.215 -15.885 -71.711 1.00 53.09 ? 25 HIS B CA 1 ATOM 2735 C C . HIS B 2 25 ? 34.344 -16.112 -73.201 1.00 53.82 ? 25 HIS B C 1 ATOM 2736 O O . HIS B 2 25 ? 35.403 -16.506 -73.662 1.00 53.99 ? 25 HIS B O 1 ATOM 2737 C CB . HIS B 2 25 ? 35.054 -14.671 -71.336 1.00 52.70 ? 25 HIS B CB 1 ATOM 2738 C CG . HIS B 2 25 ? 34.645 -13.424 -72.052 1.00 54.30 ? 25 HIS B CG 1 ATOM 2739 N ND1 . HIS B 2 25 ? 35.258 -12.995 -73.210 1.00 54.87 ? 25 HIS B ND1 1 ATOM 2740 C CD2 . HIS B 2 25 ? 33.663 -12.528 -71.791 1.00 55.23 ? 25 HIS B CD2 1 ATOM 2741 C CE1 . HIS B 2 25 ? 34.685 -11.879 -73.621 1.00 55.60 ? 25 HIS B CE1 1 ATOM 2742 N NE2 . HIS B 2 25 ? 33.715 -11.575 -72.776 1.00 56.50 ? 25 HIS B NE2 1 ATOM 2743 N N . HIS B 2 26 ? 33.278 -15.847 -73.955 1.00 56.29 ? 26 HIS B N 1 ATOM 2744 C CA . HIS B 2 26 ? 33.300 -16.051 -75.410 1.00 57.53 ? 26 HIS B CA 1 ATOM 2745 C C . HIS B 2 26 ? 33.150 -14.744 -76.185 1.00 58.12 ? 26 HIS B C 1 ATOM 2746 O O . HIS B 2 26 ? 32.630 -13.773 -75.662 1.00 57.23 ? 26 HIS B O 1 ATOM 2747 C CB . HIS B 2 26 ? 32.214 -17.044 -75.824 1.00 58.51 ? 26 HIS B CB 1 ATOM 2748 C CG . HIS B 2 26 ? 30.842 -16.459 -75.863 1.00 60.50 ? 26 HIS B CG 1 ATOM 2749 N ND1 . HIS B 2 26 ? 30.010 -16.440 -74.766 1.00 62.27 ? 26 HIS B ND1 1 ATOM 2750 C CD2 . HIS B 2 26 ? 30.152 -15.873 -76.868 1.00 62.45 ? 26 HIS B CD2 1 ATOM 2751 C CE1 . HIS B 2 26 ? 28.866 -15.866 -75.091 1.00 63.37 ? 26 HIS B CE1 1 ATOM 2752 N NE2 . HIS B 2 26 ? 28.926 -15.515 -76.363 1.00 64.37 ? 26 HIS B NE2 1 ATOM 2753 N N . SER B 2 27 ? 33.634 -14.752 -77.426 1.00 59.69 ? 27 SER B N 1 ATOM 2754 C CA . SER B 2 27 ? 33.557 -13.621 -78.364 1.00 61.35 ? 27 SER B CA 1 ATOM 2755 C C . SER B 2 27 ? 33.399 -14.155 -79.775 1.00 61.86 ? 27 SER B C 1 ATOM 2756 O O . SER B 2 27 ? 34.274 -14.869 -80.265 1.00 61.11 ? 27 SER B O 1 ATOM 2757 C CB . SER B 2 27 ? 34.848 -12.809 -78.341 1.00 62.26 ? 27 SER B CB 1 ATOM 2758 O OG . SER B 2 27 ? 34.770 -11.758 -77.416 1.00 64.74 ? 27 SER B OG 1 ATOM 2759 N N . ASN B 2 28 ? 32.305 -13.797 -80.433 1.00 63.23 ? 28 ASN B N 1 ATOM 2760 C CA . ASN B 2 28 ? 32.082 -14.183 -81.826 1.00 63.68 ? 28 ASN B CA 1 ATOM 2761 C C . ASN B 2 28 ? 31.267 -13.095 -82.538 1.00 66.38 ? 28 ASN B C 1 ATOM 2762 O O . ASN B 2 28 ? 31.159 -11.984 -82.026 1.00 66.54 ? 28 ASN B O 1 ATOM 2763 C CB . ASN B 2 28 ? 31.423 -15.569 -81.883 1.00 61.88 ? 28 ASN B CB 1 ATOM 2764 C CG . ASN B 2 28 ? 30.073 -15.602 -81.206 1.00 61.03 ? 28 ASN B CG 1 ATOM 2765 O OD1 . ASN B 2 28 ? 29.424 -14.576 -81.060 1.00 62.09 ? 28 ASN B OD1 1 ATOM 2766 N ND2 . ASN B 2 28 ? 29.639 -16.784 -80.796 1.00 59.80 ? 28 ASN B ND2 1 ATOM 2767 N N . GLU B 2 29 ? 30.712 -13.387 -83.709 1.00 70.02 ? 29 GLU B N 1 ATOM 2768 C CA . GLU B 2 29 ? 29.963 -12.370 -84.453 1.00 74.60 ? 29 GLU B CA 1 ATOM 2769 C C . GLU B 2 29 ? 28.666 -11.952 -83.756 1.00 75.50 ? 29 GLU B C 1 ATOM 2770 O O . GLU B 2 29 ? 28.248 -10.801 -83.852 1.00 75.80 ? 29 GLU B O 1 ATOM 2771 C CB . GLU B 2 29 ? 29.647 -12.853 -85.869 1.00 78.95 ? 29 GLU B CB 1 ATOM 2772 C CG . GLU B 2 29 ? 30.870 -12.978 -86.772 1.00 81.34 ? 29 GLU B CG 1 ATOM 2773 C CD . GLU B 2 29 ? 30.508 -12.938 -88.251 1.00 85.52 ? 29 GLU B CD 1 ATOM 2774 O OE1 . GLU B 2 29 ? 29.990 -11.897 -88.736 1.00 87.68 ? 29 GLU B OE1 1 ATOM 2775 O OE2 . GLU B 2 29 ? 30.733 -13.960 -88.928 1.00 87.88 ? 29 GLU B OE2 1 ATOM 2776 N N . GLN B 2 30 ? 28.040 -12.893 -83.056 1.00 76.15 ? 30 GLN B N 1 ATOM 2777 C CA . GLN B 2 30 ? 26.775 -12.641 -82.361 1.00 77.16 ? 30 GLN B CA 1 ATOM 2778 C C . GLN B 2 30 ? 26.928 -11.832 -81.066 1.00 74.63 ? 30 GLN B C 1 ATOM 2779 O O . GLN B 2 30 ? 25.953 -11.265 -80.576 1.00 74.61 ? 30 GLN B O 1 ATOM 2780 C CB . GLN B 2 30 ? 26.083 -13.968 -82.046 1.00 79.50 ? 30 GLN B CB 1 ATOM 2781 C CG . GLN B 2 30 ? 25.667 -14.764 -83.275 1.00 82.77 ? 30 GLN B CG 1 ATOM 2782 C CD . GLN B 2 30 ? 25.463 -16.242 -82.967 1.00 85.11 ? 30 GLN B CD 1 ATOM 2783 O OE1 . GLN B 2 30 ? 26.373 -16.925 -82.478 1.00 83.39 ? 30 GLN B OE1 1 ATOM 2784 N NE2 . GLN B 2 30 ? 24.265 -16.745 -83.253 1.00 88.15 ? 30 GLN B NE2 1 ATOM 2785 N N . GLY B 2 31 ? 28.135 -11.791 -80.505 1.00 71.54 ? 31 GLY B N 1 ATOM 2786 C CA . GLY B 2 31 ? 28.378 -11.024 -79.280 1.00 70.67 ? 31 GLY B CA 1 ATOM 2787 C C . GLY B 2 31 ? 29.445 -11.600 -78.374 1.00 67.26 ? 31 GLY B C 1 ATOM 2788 O O . GLY B 2 31 ? 30.401 -12.212 -78.840 1.00 66.48 ? 31 GLY B O 1 ATOM 2789 N N . SER B 2 32 ? 29.278 -11.398 -77.071 1.00 65.83 ? 32 SER B N 1 ATOM 2790 C CA . SER B 2 32 ? 30.257 -11.864 -76.091 1.00 63.29 ? 32 SER B CA 1 ATOM 2791 C C . SER B 2 32 ? 29.653 -11.945 -74.704 1.00 62.54 ? 32 SER B C 1 ATOM 2792 O O . SER B 2 32 ? 28.620 -11.345 -74.447 1.00 64.91 ? 32 SER B O 1 ATOM 2793 C CB . SER B 2 32 ? 31.448 -10.908 -76.046 1.00 63.09 ? 32 SER B CB 1 ATOM 2794 O OG . SER B 2 32 ? 31.030 -9.636 -75.602 1.00 64.94 ? 32 SER B OG 1 ATOM 2795 N N . GLY B 2 33 ? 30.303 -12.678 -73.808 1.00 60.85 ? 33 GLY B N 1 ATOM 2796 C CA . GLY B 2 33 ? 29.852 -12.740 -72.426 1.00 61.30 ? 33 GLY B CA 1 ATOM 2797 C C . GLY B 2 33 ? 30.466 -13.825 -71.563 1.00 59.82 ? 33 GLY B C 1 ATOM 2798 O O . GLY B 2 33 ? 31.245 -14.655 -72.030 1.00 58.53 ? 33 GLY B O 1 ATOM 2799 N N . TYR B 2 34 ? 30.085 -13.812 -70.288 1.00 60.29 ? 34 TYR B N 1 ATOM 2800 C CA . TYR B 2 34 ? 30.624 -14.729 -69.300 1.00 58.58 ? 34 TYR B CA 1 ATOM 2801 C C . TYR B 2 34 ? 29.632 -15.836 -69.001 1.00 58.63 ? 34 TYR B C 1 ATOM 2802 O O . TYR B 2 34 ? 28.436 -15.619 -69.022 1.00 60.18 ? 34 TYR B O 1 ATOM 2803 C CB . TYR B 2 34 ? 30.950 -13.980 -68.010 1.00 58.37 ? 34 TYR B CB 1 ATOM 2804 C CG . TYR B 2 34 ? 31.895 -12.810 -68.196 1.00 58.37 ? 34 TYR B CG 1 ATOM 2805 C CD1 . TYR B 2 34 ? 33.278 -12.982 -68.159 1.00 56.66 ? 34 TYR B CD1 1 ATOM 2806 C CD2 . TYR B 2 34 ? 31.404 -11.529 -68.403 1.00 60.42 ? 34 TYR B CD2 1 ATOM 2807 C CE1 . TYR B 2 34 ? 34.136 -11.901 -68.327 1.00 57.30 ? 34 TYR B CE1 1 ATOM 2808 C CE2 . TYR B 2 34 ? 32.253 -10.451 -68.571 1.00 60.71 ? 34 TYR B CE2 1 ATOM 2809 C CZ . TYR B 2 34 ? 33.610 -10.641 -68.531 1.00 59.44 ? 34 TYR B CZ 1 ATOM 2810 O OH . TYR B 2 34 ? 34.429 -9.556 -68.698 1.00 61.42 ? 34 TYR B OH 1 ATOM 2811 N N . ALA B 2 35 ? 30.147 -17.025 -68.727 1.00 58.13 ? 35 ALA B N 1 ATOM 2812 C CA . ALA B 2 35 ? 29.337 -18.136 -68.247 1.00 58.82 ? 35 ALA B CA 1 ATOM 2813 C C . ALA B 2 35 ? 30.136 -18.933 -67.205 1.00 58.17 ? 35 ALA B C 1 ATOM 2814 O O . ALA B 2 35 ? 31.254 -19.391 -67.470 1.00 55.90 ? 35 ALA B O 1 ATOM 2815 C CB . ALA B 2 35 ? 28.925 -19.028 -69.399 1.00 58.91 ? 35 ALA B CB 1 ATOM 2816 N N . ALA B 2 36 ? 29.555 -19.082 -66.021 1.00 59.17 ? 36 ALA B N 1 ATOM 2817 C CA . ALA B 2 36 ? 30.180 -19.827 -64.943 1.00 59.58 ? 36 ALA B CA 1 ATOM 2818 C C . ALA B 2 36 ? 30.153 -21.316 -65.252 1.00 60.97 ? 36 ALA B C 1 ATOM 2819 O O . ALA B 2 36 ? 29.190 -21.805 -65.827 1.00 64.25 ? 36 ALA B O 1 ATOM 2820 C CB . ALA B 2 36 ? 29.456 -19.553 -63.637 1.00 60.58 ? 36 ALA B CB 1 ATOM 2821 N N . ASP B 2 37 ? 31.217 -22.024 -64.887 1.00 61.04 ? 37 ASP B N 1 ATOM 2822 C CA . ASP B 2 37 ? 31.243 -23.477 -64.956 1.00 62.82 ? 37 ASP B CA 1 ATOM 2823 C C . ASP B 2 37 ? 30.720 -24.013 -63.622 1.00 67.17 ? 37 ASP B C 1 ATOM 2824 O O . ASP B 2 37 ? 31.378 -23.879 -62.587 1.00 66.44 ? 37 ASP B O 1 ATOM 2825 C CB . ASP B 2 37 ? 32.661 -23.975 -65.217 1.00 61.25 ? 37 ASP B CB 1 ATOM 2826 C CG . ASP B 2 37 ? 32.722 -25.467 -65.433 1.00 62.29 ? 37 ASP B CG 1 ATOM 2827 O OD1 . ASP B 2 37 ? 32.524 -25.918 -66.583 1.00 62.59 ? 37 ASP B OD1 1 ATOM 2828 O OD2 . ASP B 2 37 ? 32.977 -26.192 -64.449 1.00 62.88 ? 37 ASP B OD2 1 ATOM 2829 N N . LYS B 2 38 ? 29.531 -24.611 -63.658 1.00 73.52 ? 38 LYS B N 1 ATOM 2830 C CA . LYS B 2 38 ? 28.816 -25.052 -62.457 1.00 78.22 ? 38 LYS B CA 1 ATOM 2831 C C . LYS B 2 38 ? 29.542 -26.167 -61.705 1.00 76.77 ? 38 LYS B C 1 ATOM 2832 O O . LYS B 2 38 ? 29.673 -26.116 -60.484 1.00 74.34 ? 38 LYS B O 1 ATOM 2833 C CB . LYS B 2 38 ? 27.419 -25.538 -62.850 1.00 85.75 ? 38 LYS B CB 1 ATOM 2834 C CG . LYS B 2 38 ? 26.508 -25.928 -61.690 1.00 92.49 ? 38 LYS B CG 1 ATOM 2835 C CD . LYS B 2 38 ? 25.754 -27.235 -61.953 1.00 98.39 ? 38 LYS B CD 1 ATOM 2836 C CE . LYS B 2 38 ? 24.811 -27.162 -63.155 1.00 102.20 ? 38 LYS B CE 1 ATOM 2837 N NZ . LYS B 2 38 ? 23.612 -26.306 -62.919 1.00 105.39 ? 38 LYS B NZ 1 ATOM 2838 N N . GLU B 2 39 ? 30.009 -27.171 -62.439 1.00 78.10 ? 39 GLU B N 1 ATOM 2839 C CA . GLU B 2 39 ? 30.566 -28.366 -61.820 1.00 79.73 ? 39 GLU B CA 1 ATOM 2840 C C . GLU B 2 39 ? 31.804 -28.055 -60.988 1.00 73.51 ? 39 GLU B C 1 ATOM 2841 O O . GLU B 2 39 ? 31.880 -28.452 -59.825 1.00 74.76 ? 39 GLU B O 1 ATOM 2842 C CB . GLU B 2 39 ? 30.906 -29.433 -62.867 1.00 86.59 ? 39 GLU B CB 1 ATOM 2843 C CG . GLU B 2 39 ? 30.781 -30.861 -62.336 1.00 94.67 ? 39 GLU B CG 1 ATOM 2844 C CD . GLU B 2 39 ? 31.916 -31.779 -62.769 1.00 98.85 ? 39 GLU B CD 1 ATOM 2845 O OE1 . GLU B 2 39 ? 32.336 -31.717 -63.948 1.00 98.68 ? 39 GLU B OE1 1 ATOM 2846 O OE2 . GLU B 2 39 ? 32.393 -32.565 -61.917 1.00 103.69 ? 39 GLU B OE2 1 ATOM 2847 N N . SER B 2 40 ? 32.767 -27.346 -61.572 1.00 66.29 ? 40 SER B N 1 ATOM 2848 C CA . SER B 2 40 ? 34.010 -27.045 -60.859 1.00 61.59 ? 40 SER B CA 1 ATOM 2849 C C . SER B 2 40 ? 33.789 -26.038 -59.738 1.00 59.18 ? 40 SER B C 1 ATOM 2850 O O . SER B 2 40 ? 34.460 -26.108 -58.708 1.00 57.78 ? 40 SER B O 1 ATOM 2851 C CB . SER B 2 40 ? 35.113 -26.568 -61.809 1.00 59.18 ? 40 SER B CB 1 ATOM 2852 O OG . SER B 2 40 ? 34.732 -25.403 -62.505 1.00 60.85 ? 40 SER B OG 1 ATOM 2853 N N . THR B 2 41 ? 32.843 -25.120 -59.930 1.00 57.71 ? 41 THR B N 1 ATOM 2854 C CA . THR B 2 41 ? 32.489 -24.154 -58.893 1.00 56.55 ? 41 THR B CA 1 ATOM 2855 C C . THR B 2 41 ? 31.896 -24.848 -57.665 1.00 56.69 ? 41 THR B C 1 ATOM 2856 O O . THR B 2 41 ? 32.286 -24.564 -56.539 1.00 54.67 ? 41 THR B O 1 ATOM 2857 C CB . THR B 2 41 ? 31.500 -23.083 -59.419 1.00 57.45 ? 41 THR B CB 1 ATOM 2858 O OG1 . THR B 2 41 ? 32.125 -22.314 -60.457 1.00 55.88 ? 41 THR B OG1 1 ATOM 2859 C CG2 . THR B 2 41 ? 31.063 -22.139 -58.300 1.00 57.52 ? 41 THR B CG2 1 ATOM 2860 N N . GLN B 2 42 ? 30.958 -25.762 -57.882 1.00 60.05 ? 42 GLN B N 1 ATOM 2861 C CA . GLN B 2 42 ? 30.302 -26.464 -56.769 1.00 62.58 ? 42 GLN B CA 1 ATOM 2862 C C . GLN B 2 42 ? 31.270 -27.391 -56.045 1.00 61.66 ? 42 GLN B C 1 ATOM 2863 O O . GLN B 2 42 ? 31.163 -27.592 -54.838 1.00 61.85 ? 42 GLN B O 1 ATOM 2864 C CB . GLN B 2 42 ? 29.096 -27.265 -57.262 1.00 65.43 ? 42 GLN B CB 1 ATOM 2865 C CG . GLN B 2 42 ? 28.241 -27.844 -56.143 1.00 68.68 ? 42 GLN B CG 1 ATOM 2866 C CD . GLN B 2 42 ? 27.650 -26.780 -55.234 1.00 70.02 ? 42 GLN B CD 1 ATOM 2867 O OE1 . GLN B 2 42 ? 27.794 -26.839 -54.013 1.00 69.95 ? 42 GLN B OE1 1 ATOM 2868 N NE2 . GLN B 2 42 ? 26.985 -25.796 -55.827 1.00 71.32 ? 42 GLN B NE2 1 ATOM 2869 N N . LYS B 2 43 ? 32.189 -27.971 -56.808 1.00 61.44 ? 43 LYS B N 1 ATOM 2870 C CA . LYS B 2 43 ? 33.321 -28.720 -56.273 1.00 61.72 ? 43 LYS B CA 1 ATOM 2871 C C . LYS B 2 43 ? 34.124 -27.831 -55.316 1.00 58.06 ? 43 LYS B C 1 ATOM 2872 O O . LYS B 2 43 ? 34.465 -28.241 -54.204 1.00 59.20 ? 43 LYS B O 1 ATOM 2873 C CB . LYS B 2 43 ? 34.219 -29.165 -57.438 1.00 65.52 ? 43 LYS B CB 1 ATOM 2874 C CG . LYS B 2 43 ? 34.537 -30.648 -57.514 1.00 70.80 ? 43 LYS B CG 1 ATOM 2875 C CD . LYS B 2 43 ? 34.383 -31.168 -58.947 1.00 76.26 ? 43 LYS B CD 1 ATOM 2876 C CE . LYS B 2 43 ? 35.109 -32.493 -59.169 1.00 79.94 ? 43 LYS B CE 1 ATOM 2877 N NZ . LYS B 2 43 ? 34.838 -33.501 -58.101 1.00 81.66 ? 43 LYS B NZ 1 ATOM 2878 N N . ALA B 2 44 ? 34.419 -26.611 -55.747 1.00 53.15 ? 44 ALA B N 1 ATOM 2879 C CA . ALA B 2 44 ? 35.168 -25.689 -54.917 1.00 51.77 ? 44 ALA B CA 1 ATOM 2880 C C . ALA B 2 44 ? 34.404 -25.323 -53.648 1.00 52.49 ? 44 ALA B C 1 ATOM 2881 O O . ALA B 2 44 ? 34.973 -25.297 -52.565 1.00 53.02 ? 44 ALA B O 1 ATOM 2882 C CB . ALA B 2 44 ? 35.530 -24.435 -55.703 1.00 51.13 ? 44 ALA B CB 1 ATOM 2883 N N . ILE B 2 45 ? 33.115 -25.047 -53.777 1.00 54.05 ? 45 ILE B N 1 ATOM 2884 C CA . ILE B 2 45 ? 32.301 -24.718 -52.615 1.00 56.57 ? 45 ILE B CA 1 ATOM 2885 C C . ILE B 2 45 ? 32.256 -25.865 -51.608 1.00 57.82 ? 45 ILE B C 1 ATOM 2886 O O . ILE B 2 45 ? 32.389 -25.643 -50.404 1.00 59.69 ? 45 ILE B O 1 ATOM 2887 C CB . ILE B 2 45 ? 30.863 -24.339 -53.020 1.00 59.54 ? 45 ILE B CB 1 ATOM 2888 C CG1 . ILE B 2 45 ? 30.863 -22.996 -53.763 1.00 59.26 ? 45 ILE B CG1 1 ATOM 2889 C CG2 . ILE B 2 45 ? 29.952 -24.274 -51.798 1.00 60.23 ? 45 ILE B CG2 1 ATOM 2890 C CD1 . ILE B 2 45 ? 29.584 -22.740 -54.535 1.00 62.08 ? 45 ILE B CD1 1 ATOM 2891 N N . ASP B 2 46 ? 32.061 -27.085 -52.091 1.00 58.36 ? 46 ASP B N 1 ATOM 2892 C CA . ASP B 2 46 ? 32.005 -28.241 -51.197 1.00 59.97 ? 46 ASP B CA 1 ATOM 2893 C C . ASP B 2 46 ? 33.333 -28.440 -50.452 1.00 57.35 ? 46 ASP B C 1 ATOM 2894 O O . ASP B 2 46 ? 33.342 -28.729 -49.259 1.00 58.20 ? 46 ASP B O 1 ATOM 2895 C CB . ASP B 2 46 ? 31.621 -29.510 -51.967 1.00 61.75 ? 46 ASP B CB 1 ATOM 2896 C CG . ASP B 2 46 ? 30.223 -29.433 -52.571 1.00 65.18 ? 46 ASP B CG 1 ATOM 2897 O OD1 . ASP B 2 46 ? 29.484 -28.478 -52.251 1.00 66.36 ? 46 ASP B OD1 1 ATOM 2898 O OD2 . ASP B 2 46 ? 29.864 -30.324 -53.376 1.00 67.59 ? 46 ASP B OD2 1 ATOM 2899 N N . GLY B 2 47 ? 34.447 -28.263 -51.151 1.00 54.22 ? 47 GLY B N 1 ATOM 2900 C CA . GLY B 2 47 ? 35.759 -28.491 -50.557 1.00 53.03 ? 47 GLY B CA 1 ATOM 2901 C C . GLY B 2 47 ? 36.077 -27.495 -49.464 1.00 52.87 ? 47 GLY B C 1 ATOM 2902 O O . GLY B 2 47 ? 36.434 -27.876 -48.343 1.00 52.93 ? 47 GLY B O 1 ATOM 2903 N N . VAL B 2 48 ? 35.936 -26.214 -49.793 1.00 52.07 ? 48 VAL B N 1 ATOM 2904 C CA . VAL B 2 48 ? 36.181 -25.139 -48.842 1.00 51.51 ? 48 VAL B CA 1 ATOM 2905 C C . VAL B 2 48 ? 35.215 -25.200 -47.643 1.00 52.65 ? 48 VAL B C 1 ATOM 2906 O O . VAL B 2 48 ? 35.623 -24.961 -46.510 1.00 51.99 ? 48 VAL B O 1 ATOM 2907 C CB . VAL B 2 48 ? 36.126 -23.767 -49.556 1.00 52.02 ? 48 VAL B CB 1 ATOM 2908 C CG1 . VAL B 2 48 ? 36.050 -22.613 -48.565 1.00 52.73 ? 48 VAL B CG1 1 ATOM 2909 C CG2 . VAL B 2 48 ? 37.341 -23.608 -50.465 1.00 50.90 ? 48 VAL B CG2 1 ATOM 2910 N N . THR B 2 49 ? 33.952 -25.537 -47.884 1.00 53.84 ? 49 THR B N 1 ATOM 2911 C CA . THR B 2 49 ? 32.985 -25.666 -46.793 1.00 56.85 ? 49 THR B CA 1 ATOM 2912 C C . THR B 2 49 ? 33.364 -26.797 -45.840 1.00 58.50 ? 49 THR B C 1 ATOM 2913 O O . THR B 2 49 ? 33.326 -26.635 -44.621 1.00 59.42 ? 49 THR B O 1 ATOM 2914 C CB . THR B 2 49 ? 31.564 -25.912 -47.328 1.00 58.72 ? 49 THR B CB 1 ATOM 2915 O OG1 . THR B 2 49 ? 31.208 -24.851 -48.220 1.00 57.63 ? 49 THR B OG1 1 ATOM 2916 C CG2 . THR B 2 49 ? 30.555 -25.980 -46.192 1.00 60.41 ? 49 THR B CG2 1 ATOM 2917 N N . ASN B 2 50 ? 33.741 -27.941 -46.393 1.00 60.33 ? 50 ASN B N 1 ATOM 2918 C CA . ASN B 2 50 ? 34.169 -29.070 -45.561 1.00 62.57 ? 50 ASN B CA 1 ATOM 2919 C C . ASN B 2 50 ? 35.433 -28.754 -44.777 1.00 60.09 ? 50 ASN B C 1 ATOM 2920 O O . ASN B 2 50 ? 35.595 -29.205 -43.648 1.00 61.19 ? 50 ASN B O 1 ATOM 2921 C CB . ASN B 2 50 ? 34.378 -30.324 -46.409 1.00 63.59 ? 50 ASN B CB 1 ATOM 2922 C CG . ASN B 2 50 ? 33.079 -30.862 -46.980 1.00 67.65 ? 50 ASN B CG 1 ATOM 2923 O OD1 . ASN B 2 50 ? 31.998 -30.575 -46.471 1.00 72.78 ? 50 ASN B OD1 1 ATOM 2924 N ND2 . ASN B 2 50 ? 33.179 -31.644 -48.043 1.00 68.87 ? 50 ASN B ND2 1 ATOM 2925 N N . LYS B 2 51 ? 36.319 -27.970 -45.377 1.00 57.37 ? 51 LYS B N 1 ATOM 2926 C CA . LYS B 2 51 ? 37.570 -27.592 -44.724 1.00 55.71 ? 51 LYS B CA 1 ATOM 2927 C C . LYS B 2 51 ? 37.287 -26.745 -43.484 1.00 55.51 ? 51 LYS B C 1 ATOM 2928 O O . LYS B 2 51 ? 37.791 -27.022 -42.398 1.00 55.06 ? 51 LYS B O 1 ATOM 2929 C CB . LYS B 2 51 ? 38.467 -26.823 -45.704 1.00 54.06 ? 51 LYS B CB 1 ATOM 2930 C CG . LYS B 2 51 ? 39.644 -26.113 -45.054 1.00 54.00 ? 51 LYS B CG 1 ATOM 2931 C CD . LYS B 2 51 ? 40.506 -25.389 -46.073 1.00 53.58 ? 51 LYS B CD 1 ATOM 2932 C CE . LYS B 2 51 ? 41.203 -26.357 -47.008 1.00 52.90 ? 51 LYS B CE 1 ATOM 2933 N NZ . LYS B 2 51 ? 42.362 -25.702 -47.666 1.00 53.21 ? 51 LYS B NZ 1 ATOM 2934 N N . VAL B 2 52 ? 36.474 -25.714 -43.662 1.00 54.71 ? 52 VAL B N 1 ATOM 2935 C CA . VAL B 2 52 ? 36.162 -24.805 -42.587 1.00 55.62 ? 52 VAL B CA 1 ATOM 2936 C C . VAL B 2 52 ? 35.570 -25.598 -41.421 1.00 57.32 ? 52 VAL B C 1 ATOM 2937 O O . VAL B 2 52 ? 36.030 -25.481 -40.282 1.00 57.61 ? 52 VAL B O 1 ATOM 2938 C CB . VAL B 2 52 ? 35.200 -23.694 -43.062 1.00 57.39 ? 52 VAL B CB 1 ATOM 2939 C CG1 . VAL B 2 52 ? 34.701 -22.857 -41.888 1.00 59.62 ? 52 VAL B CG1 1 ATOM 2940 C CG2 . VAL B 2 52 ? 35.888 -22.802 -44.084 1.00 55.91 ? 52 VAL B CG2 1 ATOM 2941 N N . ASN B 2 53 ? 34.579 -26.432 -41.711 1.00 58.27 ? 53 ASN B N 1 ATOM 2942 C CA . ASN B 2 53 ? 33.942 -27.223 -40.665 1.00 61.39 ? 53 ASN B CA 1 ATOM 2943 C C . ASN B 2 53 ? 34.929 -28.213 -40.041 1.00 61.46 ? 53 ASN B C 1 ATOM 2944 O O . ASN B 2 53 ? 34.921 -28.412 -38.830 1.00 62.64 ? 53 ASN B O 1 ATOM 2945 C CB . ASN B 2 53 ? 32.696 -27.945 -41.196 1.00 63.47 ? 53 ASN B CB 1 ATOM 2946 C CG . ASN B 2 53 ? 31.671 -26.991 -41.792 1.00 64.85 ? 53 ASN B CG 1 ATOM 2947 O OD1 . ASN B 2 53 ? 31.660 -25.799 -41.493 1.00 65.66 ? 53 ASN B OD1 1 ATOM 2948 N ND2 . ASN B 2 53 ? 30.813 -27.514 -42.653 1.00 66.72 ? 53 ASN B ND2 1 ATOM 2949 N N . SER B 2 54 ? 35.788 -28.816 -40.862 1.00 61.43 ? 54 SER B N 1 ATOM 2950 C CA . SER B 2 54 ? 36.867 -29.675 -40.352 1.00 62.64 ? 54 SER B CA 1 ATOM 2951 C C . SER B 2 54 ? 37.764 -28.910 -39.372 1.00 63.85 ? 54 SER B C 1 ATOM 2952 O O . SER B 2 54 ? 38.114 -29.434 -38.314 1.00 64.09 ? 54 SER B O 1 ATOM 2953 C CB . SER B 2 54 ? 37.725 -30.248 -41.493 1.00 60.34 ? 54 SER B CB 1 ATOM 2954 O OG . SER B 2 54 ? 37.110 -31.377 -42.081 1.00 60.70 ? 54 SER B OG 1 ATOM 2955 N N . ILE B 2 55 ? 38.126 -27.680 -39.737 1.00 64.91 ? 55 ILE B N 1 ATOM 2956 C CA . ILE B 2 55 ? 38.932 -26.809 -38.877 1.00 67.47 ? 55 ILE B CA 1 ATOM 2957 C C . ILE B 2 55 ? 38.193 -26.489 -37.575 1.00 70.69 ? 55 ILE B C 1 ATOM 2958 O O . ILE B 2 55 ? 38.709 -26.739 -36.482 1.00 71.04 ? 55 ILE B O 1 ATOM 2959 C CB . ILE B 2 55 ? 39.329 -25.503 -39.614 1.00 68.31 ? 55 ILE B CB 1 ATOM 2960 C CG1 . ILE B 2 55 ? 40.447 -25.806 -40.614 1.00 67.87 ? 55 ILE B CG1 1 ATOM 2961 C CG2 . ILE B 2 55 ? 39.779 -24.416 -38.640 1.00 69.72 ? 55 ILE B CG2 1 ATOM 2962 C CD1 . ILE B 2 55 ? 40.861 -24.628 -41.462 1.00 68.07 ? 55 ILE B CD1 1 ATOM 2963 N N . ILE B 2 56 ? 36.985 -25.947 -37.702 1.00 71.87 ? 56 ILE B N 1 ATOM 2964 C CA . ILE B 2 56 ? 36.153 -25.623 -36.546 1.00 74.36 ? 56 ILE B CA 1 ATOM 2965 C C . ILE B 2 56 ? 35.986 -26.830 -35.612 1.00 78.68 ? 56 ILE B C 1 ATOM 2966 O O . ILE B 2 56 ? 36.020 -26.686 -34.386 1.00 80.18 ? 56 ILE B O 1 ATOM 2967 C CB . ILE B 2 56 ? 34.762 -25.122 -36.994 1.00 75.30 ? 56 ILE B CB 1 ATOM 2968 C CG1 . ILE B 2 56 ? 34.894 -23.749 -37.659 1.00 73.75 ? 56 ILE B CG1 1 ATOM 2969 C CG2 . ILE B 2 56 ? 33.788 -25.064 -35.816 1.00 78.14 ? 56 ILE B CG2 1 ATOM 2970 C CD1 . ILE B 2 56 ? 33.627 -23.253 -38.317 1.00 75.27 ? 56 ILE B CD1 1 ATOM 2971 N N . ASP B 2 57 ? 35.812 -28.013 -36.198 1.00 81.46 ? 57 ASP B N 1 ATOM 2972 C CA . ASP B 2 57 ? 35.493 -29.216 -35.429 1.00 86.49 ? 57 ASP B CA 1 ATOM 2973 C C . ASP B 2 57 ? 36.694 -29.780 -34.666 1.00 84.24 ? 57 ASP B C 1 ATOM 2974 O O . ASP B 2 57 ? 36.550 -30.237 -33.538 1.00 85.91 ? 57 ASP B O 1 ATOM 2975 C CB . ASP B 2 57 ? 34.905 -30.289 -36.352 1.00 89.81 ? 57 ASP B CB 1 ATOM 2976 C CG . ASP B 2 57 ? 34.429 -31.513 -35.597 1.00 96.07 ? 57 ASP B CG 1 ATOM 2977 O OD1 . ASP B 2 57 ? 33.693 -31.351 -34.593 1.00 102.63 ? 57 ASP B OD1 1 ATOM 2978 O OD2 . ASP B 2 57 ? 34.789 -32.636 -36.009 1.00 97.03 ? 57 ASP B OD2 1 ATOM 2979 N N . LYS B 2 58 ? 37.869 -29.756 -35.284 1.00 82.62 ? 58 LYS B N 1 ATOM 2980 C CA . LYS B 2 58 ? 39.093 -30.229 -34.632 1.00 82.41 ? 58 LYS B CA 1 ATOM 2981 C C . LYS B 2 58 ? 39.467 -29.385 -33.420 1.00 85.76 ? 58 LYS B C 1 ATOM 2982 O O . LYS B 2 58 ? 39.972 -29.907 -32.428 1.00 84.98 ? 58 LYS B O 1 ATOM 2983 C CB . LYS B 2 58 ? 40.261 -30.269 -35.632 1.00 79.75 ? 58 LYS B CB 1 ATOM 2984 C CG . LYS B 2 58 ? 40.677 -31.660 -36.095 1.00 78.92 ? 58 LYS B CG 1 ATOM 2985 C CD . LYS B 2 58 ? 39.543 -32.671 -36.042 1.00 81.50 ? 58 LYS B CD 1 ATOM 2986 C CE . LYS B 2 58 ? 39.956 -33.997 -36.642 1.00 82.37 ? 58 LYS B CE 1 ATOM 2987 N NZ . LYS B 2 58 ? 39.231 -35.134 -36.010 1.00 85.07 ? 58 LYS B NZ 1 ATOM 2988 N N . MET B 2 59 ? 39.197 -28.087 -33.501 1.00 89.92 ? 59 MET B N 1 ATOM 2989 C CA . MET B 2 59 ? 39.527 -27.154 -32.426 1.00 94.44 ? 59 MET B CA 1 ATOM 2990 C C . MET B 2 59 ? 38.476 -27.156 -31.307 1.00 100.07 ? 59 MET B C 1 ATOM 2991 O O . MET B 2 59 ? 38.708 -26.584 -30.242 1.00 102.58 ? 59 MET B O 1 ATOM 2992 C CB . MET B 2 59 ? 39.680 -25.738 -32.993 1.00 94.37 ? 59 MET B CB 1 ATOM 2993 C CG . MET B 2 59 ? 40.699 -25.610 -34.123 1.00 91.77 ? 59 MET B CG 1 ATOM 2994 S SD . MET B 2 59 ? 42.436 -25.851 -33.687 1.00 91.88 ? 59 MET B SD 1 ATOM 2995 C CE . MET B 2 59 ? 42.689 -24.837 -32.231 1.00 93.10 ? 59 MET B CE 1 ATOM 2996 N N . ASN B 2 60 ? 37.331 -27.795 -31.552 1.00 104.36 ? 60 ASN B N 1 ATOM 2997 C CA . ASN B 2 60 ? 36.237 -27.875 -30.568 1.00 109.18 ? 60 ASN B CA 1 ATOM 2998 C C . ASN B 2 60 ? 36.637 -28.535 -29.232 1.00 110.95 ? 60 ASN B C 1 ATOM 2999 O O . ASN B 2 60 ? 36.215 -28.084 -28.166 1.00 111.06 ? 60 ASN B O 1 ATOM 3000 C CB . ASN B 2 60 ? 34.990 -28.540 -31.200 1.00 110.46 ? 60 ASN B CB 1 ATOM 3001 C CG . ASN B 2 60 ? 34.378 -29.621 -30.325 1.00 113.06 ? 60 ASN B CG 1 ATOM 3002 O OD1 . ASN B 2 60 ? 34.811 -30.775 -30.346 1.00 111.25 ? 60 ASN B OD1 1 ATOM 3003 N ND2 . ASN B 2 60 ? 33.350 -29.258 -29.570 1.00 116.01 ? 60 ASN B ND2 1 ATOM 3004 N N . THR B 2 61 ? 37.442 -29.595 -29.293 1.00 118.21 ? 61 THR B N 1 ATOM 3005 C CA . THR B 2 61 ? 38.027 -30.185 -28.089 1.00 115.97 ? 61 THR B CA 1 ATOM 3006 C C . THR B 2 61 ? 39.341 -29.468 -27.824 1.00 112.27 ? 61 THR B C 1 ATOM 3007 O O . THR B 2 61 ? 40.297 -29.611 -28.583 1.00 114.56 ? 61 THR B O 1 ATOM 3008 C CB . THR B 2 61 ? 38.293 -31.698 -28.232 1.00 120.07 ? 61 THR B CB 1 ATOM 3009 O OG1 . THR B 2 61 ? 37.059 -32.393 -28.452 1.00 122.97 ? 61 THR B OG1 1 ATOM 3010 C CG2 . THR B 2 61 ? 38.962 -32.251 -26.970 1.00 119.07 ? 61 THR B CG2 1 ATOM 3011 N N . GLN B 2 62 ? 39.380 -28.697 -26.745 1.00 108.22 ? 62 GLN B N 1 ATOM 3012 C CA . GLN B 2 62 ? 40.532 -27.856 -26.443 1.00 105.16 ? 62 GLN B CA 1 ATOM 3013 C C . GLN B 2 62 ? 40.501 -27.409 -24.976 1.00 103.33 ? 62 GLN B C 1 ATOM 3014 O O . GLN B 2 62 ? 39.426 -27.299 -24.369 1.00 105.03 ? 62 GLN B O 1 ATOM 3015 C CB . GLN B 2 62 ? 40.561 -26.655 -27.404 1.00 104.89 ? 62 GLN B CB 1 ATOM 3016 C CG . GLN B 2 62 ? 41.381 -25.453 -26.948 1.00 102.08 ? 62 GLN B CG 1 ATOM 3017 C CD . GLN B 2 62 ? 41.424 -24.338 -27.979 1.00 104.53 ? 62 GLN B CD 1 ATOM 3018 O OE1 . GLN B 2 62 ? 41.237 -24.568 -29.174 1.00 107.57 ? 62 GLN B OE1 1 ATOM 3019 N NE2 . GLN B 2 62 ? 41.667 -23.118 -27.516 1.00 104.18 ? 62 GLN B NE2 1 ATOM 3020 N N . PHE B 2 63 ? 41.692 -27.156 -24.430 1.00 97.31 ? 63 PHE B N 1 ATOM 3021 C CA . PHE B 2 63 ? 41.885 -26.826 -23.014 1.00 93.73 ? 63 PHE B CA 1 ATOM 3022 C C . PHE B 2 63 ? 40.982 -25.694 -22.510 1.00 95.45 ? 63 PHE B C 1 ATOM 3023 O O . PHE B 2 63 ? 40.755 -24.709 -23.215 1.00 99.18 ? 63 PHE B O 1 ATOM 3024 C CB . PHE B 2 63 ? 43.349 -26.449 -22.768 1.00 88.07 ? 63 PHE B CB 1 ATOM 3025 C CG . PHE B 2 63 ? 43.699 -26.308 -21.320 1.00 83.78 ? 63 PHE B CG 1 ATOM 3026 C CD1 . PHE B 2 63 ? 43.859 -27.434 -20.521 1.00 81.53 ? 63 PHE B CD1 1 ATOM 3027 C CD2 . PHE B 2 63 ? 43.864 -25.049 -20.749 1.00 83.21 ? 63 PHE B CD2 1 ATOM 3028 C CE1 . PHE B 2 63 ? 44.178 -27.310 -19.181 1.00 79.57 ? 63 PHE B CE1 1 ATOM 3029 C CE2 . PHE B 2 63 ? 44.184 -24.917 -19.406 1.00 79.46 ? 63 PHE B CE2 1 ATOM 3030 C CZ . PHE B 2 63 ? 44.342 -26.050 -18.623 1.00 79.02 ? 63 PHE B CZ 1 ATOM 3031 N N . GLU B 2 64 ? 40.471 -25.857 -21.290 1.00 95.39 ? 64 GLU B N 1 ATOM 3032 C CA . GLU B 2 64 ? 39.684 -24.826 -20.611 1.00 96.74 ? 64 GLU B CA 1 ATOM 3033 C C . GLU B 2 64 ? 40.288 -24.546 -19.239 1.00 95.23 ? 64 GLU B C 1 ATOM 3034 O O . GLU B 2 64 ? 40.625 -25.474 -18.499 1.00 95.56 ? 64 GLU B O 1 ATOM 3035 C CB . GLU B 2 64 ? 38.235 -25.278 -20.442 1.00 100.71 ? 64 GLU B CB 1 ATOM 3036 C CG . GLU B 2 64 ? 37.496 -25.536 -21.745 1.00 104.50 ? 64 GLU B CG 1 ATOM 3037 C CD . GLU B 2 64 ? 36.137 -26.173 -21.525 1.00 108.51 ? 64 GLU B CD 1 ATOM 3038 O OE1 . GLU B 2 64 ? 35.561 -25.989 -20.429 1.00 107.38 ? 64 GLU B OE1 1 ATOM 3039 O OE2 . GLU B 2 64 ? 35.649 -26.862 -22.449 1.00 111.31 ? 64 GLU B OE2 1 ATOM 3040 N N . ALA B 2 65 ? 40.417 -23.267 -18.901 1.00 95.34 ? 65 ALA B N 1 ATOM 3041 C CA . ALA B 2 65 ? 41.003 -22.866 -17.625 1.00 94.09 ? 65 ALA B CA 1 ATOM 3042 C C . ALA B 2 65 ? 39.952 -22.816 -16.512 1.00 95.48 ? 65 ALA B C 1 ATOM 3043 O O . ALA B 2 65 ? 38.794 -22.476 -16.755 1.00 93.82 ? 65 ALA B O 1 ATOM 3044 C CB . ALA B 2 65 ? 41.694 -21.518 -17.767 1.00 93.90 ? 65 ALA B CB 1 ATOM 3045 N N . VAL B 2 66 ? 40.375 -23.164 -15.297 1.00 96.49 ? 66 VAL B N 1 ATOM 3046 C CA . VAL B 2 66 ? 39.516 -23.140 -14.112 1.00 98.27 ? 66 VAL B CA 1 ATOM 3047 C C . VAL B 2 66 ? 40.124 -22.201 -13.071 1.00 96.96 ? 66 VAL B C 1 ATOM 3048 O O . VAL B 2 66 ? 41.337 -21.967 -13.069 1.00 97.16 ? 66 VAL B O 1 ATOM 3049 C CB . VAL B 2 66 ? 39.363 -24.553 -13.501 1.00 100.34 ? 66 VAL B CB 1 ATOM 3050 C CG1 . VAL B 2 66 ? 38.275 -24.573 -12.427 1.00 104.82 ? 66 VAL B CG1 1 ATOM 3051 C CG2 . VAL B 2 66 ? 39.057 -25.571 -14.594 1.00 102.43 ? 66 VAL B CG2 1 ATOM 3052 N N . GLY B 2 67 ? 39.277 -21.661 -12.197 1.00 96.52 ? 67 GLY B N 1 ATOM 3053 C CA . GLY B 2 67 ? 39.729 -20.834 -11.082 1.00 92.55 ? 67 GLY B CA 1 ATOM 3054 C C . GLY B 2 67 ? 40.336 -21.681 -9.977 1.00 88.08 ? 67 GLY B C 1 ATOM 3055 O O . GLY B 2 67 ? 39.708 -22.619 -9.486 1.00 90.14 ? 67 GLY B O 1 ATOM 3056 N N . ARG B 2 68 ? 41.566 -21.353 -9.597 1.00 81.11 ? 68 ARG B N 1 ATOM 3057 C CA . ARG B 2 68 ? 42.276 -22.052 -8.531 1.00 77.52 ? 68 ARG B CA 1 ATOM 3058 C C . ARG B 2 68 ? 43.080 -21.032 -7.724 1.00 76.44 ? 68 ARG B C 1 ATOM 3059 O O . ARG B 2 68 ? 43.915 -20.311 -8.277 1.00 76.57 ? 68 ARG B O 1 ATOM 3060 C CB . ARG B 2 68 ? 43.205 -23.117 -9.120 1.00 74.34 ? 68 ARG B CB 1 ATOM 3061 C CG . ARG B 2 68 ? 42.644 -24.530 -9.101 1.00 75.50 ? 68 ARG B CG 1 ATOM 3062 C CD . ARG B 2 68 ? 43.595 -25.544 -9.736 1.00 73.14 ? 68 ARG B CD 1 ATOM 3063 N NE . ARG B 2 68 ? 42.992 -26.207 -10.893 1.00 73.65 ? 68 ARG B NE 1 ATOM 3064 C CZ . ARG B 2 68 ? 43.131 -25.828 -12.163 1.00 72.37 ? 68 ARG B CZ 1 ATOM 3065 N NH1 . ARG B 2 68 ? 43.897 -24.798 -12.502 1.00 68.81 ? 68 ARG B NH1 1 ATOM 3066 N NH2 . ARG B 2 68 ? 42.498 -26.506 -13.117 1.00 75.46 ? 68 ARG B NH2 1 ATOM 3067 N N . GLU B 2 69 ? 42.827 -20.976 -6.421 1.00 76.37 ? 69 GLU B N 1 ATOM 3068 C CA . GLU B 2 69 ? 43.464 -19.993 -5.552 1.00 73.82 ? 69 GLU B CA 1 ATOM 3069 C C . GLU B 2 69 ? 44.379 -20.671 -4.552 1.00 69.51 ? 69 GLU B C 1 ATOM 3070 O O . GLU B 2 69 ? 44.144 -21.811 -4.162 1.00 68.78 ? 69 GLU B O 1 ATOM 3071 C CB . GLU B 2 69 ? 42.405 -19.162 -4.834 1.00 79.67 ? 69 GLU B CB 1 ATOM 3072 C CG . GLU B 2 69 ? 41.458 -18.476 -5.806 1.00 83.05 ? 69 GLU B CG 1 ATOM 3073 C CD . GLU B 2 69 ? 40.489 -17.529 -5.135 1.00 89.21 ? 69 GLU B CD 1 ATOM 3074 O OE1 . GLU B 2 69 ? 40.920 -16.755 -4.253 1.00 92.42 ? 69 GLU B OE1 1 ATOM 3075 O OE2 . GLU B 2 69 ? 39.294 -17.553 -5.505 1.00 92.65 ? 69 GLU B OE2 1 ATOM 3076 N N . PHE B 2 70 ? 45.429 -19.957 -4.159 1.00 66.56 ? 70 PHE B N 1 ATOM 3077 C CA . PHE B 2 70 ? 46.454 -20.484 -3.267 1.00 65.38 ? 70 PHE B CA 1 ATOM 3078 C C . PHE B 2 70 ? 46.895 -19.405 -2.281 1.00 66.30 ? 70 PHE B C 1 ATOM 3079 O O . PHE B 2 70 ? 46.846 -18.216 -2.587 1.00 65.54 ? 70 PHE B O 1 ATOM 3080 C CB . PHE B 2 70 ? 47.657 -20.964 -4.079 1.00 62.59 ? 70 PHE B CB 1 ATOM 3081 C CG . PHE B 2 70 ? 47.300 -21.898 -5.200 1.00 61.47 ? 70 PHE B CG 1 ATOM 3082 C CD1 . PHE B 2 70 ? 46.999 -21.404 -6.467 1.00 61.65 ? 70 PHE B CD1 1 ATOM 3083 C CD2 . PHE B 2 70 ? 47.267 -23.271 -4.995 1.00 62.04 ? 70 PHE B CD2 1 ATOM 3084 C CE1 . PHE B 2 70 ? 46.662 -22.261 -7.504 1.00 60.57 ? 70 PHE B CE1 1 ATOM 3085 C CE2 . PHE B 2 70 ? 46.938 -24.134 -6.027 1.00 61.38 ? 70 PHE B CE2 1 ATOM 3086 C CZ . PHE B 2 70 ? 46.634 -23.628 -7.284 1.00 61.04 ? 70 PHE B CZ 1 ATOM 3087 N N . ASN B 2 71 ? 47.327 -19.820 -1.097 1.00 67.89 ? 71 ASN B N 1 ATOM 3088 C CA . ASN B 2 71 ? 47.689 -18.862 -0.052 1.00 70.28 ? 71 ASN B CA 1 ATOM 3089 C C . ASN B 2 71 ? 49.142 -18.424 -0.200 1.00 69.25 ? 71 ASN B C 1 ATOM 3090 O O . ASN B 2 71 ? 49.805 -18.791 -1.173 1.00 67.33 ? 71 ASN B O 1 ATOM 3091 C CB . ASN B 2 71 ? 47.373 -19.414 1.356 1.00 72.89 ? 71 ASN B CB 1 ATOM 3092 C CG . ASN B 2 71 ? 48.336 -20.495 1.807 1.00 71.25 ? 71 ASN B CG 1 ATOM 3093 O OD1 . ASN B 2 71 ? 49.544 -20.385 1.621 1.00 69.61 ? 71 ASN B OD1 1 ATOM 3094 N ND2 . ASN B 2 71 ? 47.801 -21.544 2.422 1.00 74.53 ? 71 ASN B ND2 1 ATOM 3095 N N . ASN B 2 72 ? 49.629 -17.651 0.768 1.00 72.84 ? 72 ASN B N 1 ATOM 3096 C CA . ASN B 2 72 ? 50.943 -17.016 0.673 1.00 72.86 ? 72 ASN B CA 1 ATOM 3097 C C . ASN B 2 72 ? 52.139 -17.968 0.785 1.00 71.13 ? 72 ASN B C 1 ATOM 3098 O O . ASN B 2 72 ? 53.247 -17.612 0.375 1.00 71.36 ? 72 ASN B O 1 ATOM 3099 C CB . ASN B 2 72 ? 51.072 -15.917 1.727 1.00 77.61 ? 72 ASN B CB 1 ATOM 3100 C CG . ASN B 2 72 ? 52.158 -14.922 1.387 1.00 79.48 ? 72 ASN B CG 1 ATOM 3101 O OD1 . ASN B 2 72 ? 52.145 -14.338 0.311 1.00 82.31 ? 72 ASN B OD1 1 ATOM 3102 N ND2 . ASN B 2 72 ? 53.105 -14.725 2.295 1.00 83.14 ? 72 ASN B ND2 1 ATOM 3103 N N . LEU B 2 73 ? 51.923 -19.151 1.360 1.00 70.28 ? 73 LEU B N 1 ATOM 3104 C CA . LEU B 2 73 ? 52.955 -20.188 1.433 1.00 69.37 ? 73 LEU B CA 1 ATOM 3105 C C . LEU B 2 73 ? 52.570 -21.400 0.577 1.00 68.57 ? 73 LEU B C 1 ATOM 3106 O O . LEU B 2 73 ? 52.825 -22.553 0.945 1.00 68.63 ? 73 LEU B O 1 ATOM 3107 C CB . LEU B 2 73 ? 53.188 -20.599 2.887 1.00 73.21 ? 73 LEU B CB 1 ATOM 3108 C CG . LEU B 2 73 ? 53.832 -19.535 3.787 1.00 75.89 ? 73 LEU B CG 1 ATOM 3109 C CD1 . LEU B 2 73 ? 53.745 -19.950 5.247 1.00 78.53 ? 73 LEU B CD1 1 ATOM 3110 C CD2 . LEU B 2 73 ? 55.279 -19.276 3.381 1.00 74.83 ? 73 LEU B CD2 1 ATOM 3111 N N . GLU B 2 74 ? 51.937 -21.125 -0.561 1.00 65.19 ? 74 GLU B N 1 ATOM 3112 C CA . GLU B 2 74 ? 51.699 -22.128 -1.588 1.00 62.72 ? 74 GLU B CA 1 ATOM 3113 C C . GLU B 2 74 ? 52.101 -21.538 -2.935 1.00 61.73 ? 74 GLU B C 1 ATOM 3114 O O . GLU B 2 74 ? 51.433 -21.761 -3.945 1.00 59.29 ? 74 GLU B O 1 ATOM 3115 C CB . GLU B 2 74 ? 50.230 -22.542 -1.599 1.00 62.89 ? 74 GLU B CB 1 ATOM 3116 C CG . GLU B 2 74 ? 49.813 -23.379 -0.404 1.00 64.73 ? 74 GLU B CG 1 ATOM 3117 C CD . GLU B 2 74 ? 48.328 -23.684 -0.400 1.00 66.15 ? 74 GLU B CD 1 ATOM 3118 O OE1 . GLU B 2 74 ? 47.541 -22.802 -0.792 1.00 66.06 ? 74 GLU B OE1 1 ATOM 3119 O OE2 . GLU B 2 74 ? 47.941 -24.803 -0.006 1.00 67.53 ? 74 GLU B OE2 1 ATOM 3120 N N . ARG B 2 75 ? 53.195 -20.773 -2.934 1.00 63.48 ? 75 ARG B N 1 ATOM 3121 C CA . ARG B 2 75 ? 53.638 -20.057 -4.125 1.00 62.20 ? 75 ARG B CA 1 ATOM 3122 C C . ARG B 2 75 ? 54.132 -21.007 -5.197 1.00 59.69 ? 75 ARG B C 1 ATOM 3123 O O . ARG B 2 75 ? 53.914 -20.774 -6.377 1.00 58.93 ? 75 ARG B O 1 ATOM 3124 C CB . ARG B 2 75 ? 54.747 -19.044 -3.790 1.00 66.61 ? 75 ARG B CB 1 ATOM 3125 C CG . ARG B 2 75 ? 54.301 -17.813 -3.015 1.00 71.08 ? 75 ARG B CG 1 ATOM 3126 C CD . ARG B 2 75 ? 53.057 -17.186 -3.627 1.00 76.58 ? 75 ARG B CD 1 ATOM 3127 N NE . ARG B 2 75 ? 52.651 -15.946 -2.969 1.00 85.05 ? 75 ARG B NE 1 ATOM 3128 C CZ . ARG B 2 75 ? 51.466 -15.355 -3.132 1.00 89.36 ? 75 ARG B CZ 1 ATOM 3129 N NH1 . ARG B 2 75 ? 50.543 -15.884 -3.936 1.00 88.92 ? 75 ARG B NH1 1 ATOM 3130 N NH2 . ARG B 2 75 ? 51.199 -14.226 -2.482 1.00 92.52 ? 75 ARG B NH2 1 ATOM 3131 N N . ARG B 2 76 ? 54.801 -22.080 -4.792 1.00 60.03 ? 76 ARG B N 1 ATOM 3132 C CA . ARG B 2 76 ? 55.336 -23.023 -5.763 1.00 58.32 ? 76 ARG B CA 1 ATOM 3133 C C . ARG B 2 76 ? 54.229 -23.628 -6.629 1.00 56.69 ? 76 ARG B C 1 ATOM 3134 O O . ARG B 2 76 ? 54.322 -23.596 -7.854 1.00 53.76 ? 76 ARG B O 1 ATOM 3135 C CB . ARG B 2 76 ? 56.127 -24.120 -5.064 1.00 58.72 ? 76 ARG B CB 1 ATOM 3136 C CG . ARG B 2 76 ? 57.454 -23.657 -4.497 1.00 59.38 ? 76 ARG B CG 1 ATOM 3137 C CD . ARG B 2 76 ? 58.062 -24.761 -3.649 1.00 61.82 ? 76 ARG B CD 1 ATOM 3138 N NE . ARG B 2 76 ? 57.160 -25.121 -2.556 1.00 60.99 ? 76 ARG B NE 1 ATOM 3139 C CZ . ARG B 2 76 ? 57.159 -26.281 -1.907 1.00 62.12 ? 76 ARG B CZ 1 ATOM 3140 N NH1 . ARG B 2 76 ? 58.020 -27.245 -2.223 1.00 64.38 ? 76 ARG B NH1 1 ATOM 3141 N NH2 . ARG B 2 76 ? 56.276 -26.480 -0.936 1.00 61.72 ? 76 ARG B NH2 1 ATOM 3142 N N . ILE B 2 77 ? 53.186 -24.166 -5.997 1.00 57.19 ? 77 ILE B N 1 ATOM 3143 C CA . ILE B 2 77 ? 52.098 -24.793 -6.750 1.00 58.71 ? 77 ILE B CA 1 ATOM 3144 C C . ILE B 2 77 ? 51.184 -23.771 -7.431 1.00 58.58 ? 77 ILE B C 1 ATOM 3145 O O . ILE B 2 77 ? 50.530 -24.085 -8.421 1.00 61.51 ? 77 ILE B O 1 ATOM 3146 C CB . ILE B 2 77 ? 51.265 -25.786 -5.911 1.00 59.81 ? 77 ILE B CB 1 ATOM 3147 C CG1 . ILE B 2 77 ? 50.481 -25.076 -4.814 1.00 62.49 ? 77 ILE B CG1 1 ATOM 3148 C CG2 . ILE B 2 77 ? 52.161 -26.870 -5.329 1.00 62.23 ? 77 ILE B CG2 1 ATOM 3149 C CD1 . ILE B 2 77 ? 49.678 -26.029 -3.954 1.00 66.72 ? 77 ILE B CD1 1 ATOM 3150 N N . GLU B 2 78 ? 51.134 -22.556 -6.909 1.00 58.14 ? 78 GLU B N 1 ATOM 3151 C CA . GLU B 2 78 ? 50.460 -21.486 -7.618 1.00 59.89 ? 78 GLU B CA 1 ATOM 3152 C C . GLU B 2 78 ? 51.181 -21.228 -8.937 1.00 57.64 ? 78 GLU B C 1 ATOM 3153 O O . GLU B 2 78 ? 50.549 -21.081 -9.981 1.00 56.86 ? 78 GLU B O 1 ATOM 3154 C CB . GLU B 2 78 ? 50.429 -20.212 -6.778 1.00 65.36 ? 78 GLU B CB 1 ATOM 3155 C CG . GLU B 2 78 ? 50.065 -18.952 -7.549 1.00 70.15 ? 78 GLU B CG 1 ATOM 3156 C CD . GLU B 2 78 ? 49.552 -17.861 -6.636 1.00 79.85 ? 78 GLU B CD 1 ATOM 3157 O OE1 . GLU B 2 78 ? 48.379 -17.953 -6.208 1.00 87.89 ? 78 GLU B OE1 1 ATOM 3158 O OE2 . GLU B 2 78 ? 50.327 -16.932 -6.319 1.00 84.97 ? 78 GLU B OE2 1 ATOM 3159 N N . ASN B 2 79 ? 52.505 -21.171 -8.873 1.00 55.71 ? 79 ASN B N 1 ATOM 3160 C CA . ASN B 2 79 ? 53.322 -20.892 -10.039 1.00 58.00 ? 79 ASN B CA 1 ATOM 3161 C C . ASN B 2 79 ? 53.204 -22.020 -11.052 1.00 56.99 ? 79 ASN B C 1 ATOM 3162 O O . ASN B 2 79 ? 53.074 -21.782 -12.250 1.00 56.53 ? 79 ASN B O 1 ATOM 3163 C CB . ASN B 2 79 ? 54.779 -20.719 -9.625 1.00 61.53 ? 79 ASN B CB 1 ATOM 3164 C CG . ASN B 2 79 ? 55.676 -20.366 -10.788 1.00 64.81 ? 79 ASN B CG 1 ATOM 3165 O OD1 . ASN B 2 79 ? 55.356 -19.489 -11.580 1.00 68.58 ? 79 ASN B OD1 1 ATOM 3166 N ND2 . ASN B 2 79 ? 56.813 -21.034 -10.887 1.00 69.23 ? 79 ASN B ND2 1 ATOM 3167 N N . LEU B 2 80 ? 53.243 -23.245 -10.544 1.00 56.63 ? 80 LEU B N 1 ATOM 3168 C CA . LEU B 2 80 ? 53.038 -24.438 -11.346 1.00 56.21 ? 80 LEU B CA 1 ATOM 3169 C C . LEU B 2 80 ? 51.711 -24.334 -12.079 1.00 54.66 ? 80 LEU B C 1 ATOM 3170 O O . LEU B 2 80 ? 51.636 -24.546 -13.285 1.00 54.27 ? 80 LEU B O 1 ATOM 3171 C CB . LEU B 2 80 ? 53.045 -25.666 -10.436 1.00 58.13 ? 80 LEU B CB 1 ATOM 3172 C CG . LEU B 2 80 ? 53.324 -27.016 -11.074 1.00 61.03 ? 80 LEU B CG 1 ATOM 3173 C CD1 . LEU B 2 80 ? 53.530 -28.069 -9.998 1.00 63.50 ? 80 LEU B CD1 1 ATOM 3174 C CD2 . LEU B 2 80 ? 52.192 -27.411 -11.999 1.00 63.14 ? 80 LEU B CD2 1 ATOM 3175 N N . ASN B 2 81 ? 50.665 -23.983 -11.340 1.00 55.04 ? 81 ASN B N 1 ATOM 3176 C CA . ASN B 2 81 ? 49.327 -23.857 -11.906 1.00 55.04 ? 81 ASN B CA 1 ATOM 3177 C C . ASN B 2 81 ? 49.269 -22.783 -12.985 1.00 56.65 ? 81 ASN B C 1 ATOM 3178 O O . ASN B 2 81 ? 48.579 -22.943 -13.986 1.00 56.18 ? 81 ASN B O 1 ATOM 3179 C CB . ASN B 2 81 ? 48.319 -23.539 -10.807 1.00 55.21 ? 81 ASN B CB 1 ATOM 3180 C CG . ASN B 2 81 ? 46.911 -23.381 -11.336 1.00 55.57 ? 81 ASN B CG 1 ATOM 3181 O OD1 . ASN B 2 81 ? 46.333 -24.321 -11.869 1.00 58.78 ? 81 ASN B OD1 1 ATOM 3182 N ND2 . ASN B 2 81 ? 46.352 -22.195 -11.187 1.00 55.38 ? 81 ASN B ND2 1 ATOM 3183 N N . LYS B 2 82 ? 49.996 -21.692 -12.777 1.00 58.27 ? 82 LYS B N 1 ATOM 3184 C CA . LYS B 2 82 ? 50.017 -20.614 -13.741 1.00 63.26 ? 82 LYS B CA 1 ATOM 3185 C C . LYS B 2 82 ? 50.752 -21.060 -14.995 1.00 64.46 ? 82 LYS B C 1 ATOM 3186 O O . LYS B 2 82 ? 50.239 -20.891 -16.091 1.00 63.68 ? 82 LYS B O 1 ATOM 3187 C CB . LYS B 2 82 ? 50.680 -19.363 -13.167 1.00 68.83 ? 82 LYS B CB 1 ATOM 3188 C CG . LYS B 2 82 ? 50.325 -18.108 -13.949 1.00 77.76 ? 82 LYS B CG 1 ATOM 3189 C CD . LYS B 2 82 ? 51.449 -17.082 -13.969 1.00 86.86 ? 82 LYS B CD 1 ATOM 3190 C CE . LYS B 2 82 ? 51.105 -15.937 -14.914 1.00 95.13 ? 82 LYS B CE 1 ATOM 3191 N NZ . LYS B 2 82 ? 52.246 -15.004 -15.118 1.00 102.30 ? 82 LYS B NZ 1 ATOM 3192 N N . LYS B 2 83 ? 51.948 -21.627 -14.822 1.00 66.44 ? 83 LYS B N 1 ATOM 3193 C CA . LYS B 2 83 ? 52.743 -22.150 -15.947 1.00 68.91 ? 83 LYS B CA 1 ATOM 3194 C C . LYS B 2 83 ? 52.002 -23.219 -16.744 1.00 65.69 ? 83 LYS B C 1 ATOM 3195 O O . LYS B 2 83 ? 52.165 -23.319 -17.956 1.00 65.32 ? 83 LYS B O 1 ATOM 3196 C CB . LYS B 2 83 ? 54.095 -22.709 -15.471 1.00 73.45 ? 83 LYS B CB 1 ATOM 3197 C CG . LYS B 2 83 ? 55.310 -21.868 -15.846 1.00 80.59 ? 83 LYS B CG 1 ATOM 3198 C CD . LYS B 2 83 ? 55.267 -20.464 -15.243 1.00 84.74 ? 83 LYS B CD 1 ATOM 3199 C CE . LYS B 2 83 ? 54.793 -19.394 -16.229 1.00 88.52 ? 83 LYS B CE 1 ATOM 3200 N NZ . LYS B 2 83 ? 55.797 -19.077 -17.287 1.00 92.52 ? 83 LYS B NZ 1 ATOM 3201 N N . MET B 2 84 ? 51.196 -24.018 -16.055 1.00 63.69 ? 84 MET B N 1 ATOM 3202 C CA . MET B 2 84 ? 50.413 -25.050 -16.710 1.00 62.82 ? 84 MET B CA 1 ATOM 3203 C C . MET B 2 84 ? 49.289 -24.454 -17.553 1.00 59.46 ? 84 MET B C 1 ATOM 3204 O O . MET B 2 84 ? 49.119 -24.837 -18.711 1.00 61.64 ? 84 MET B O 1 ATOM 3205 C CB . MET B 2 84 ? 49.817 -26.013 -15.688 1.00 64.03 ? 84 MET B CB 1 ATOM 3206 C CG . MET B 2 84 ? 49.370 -27.318 -16.315 1.00 67.63 ? 84 MET B CG 1 ATOM 3207 S SD . MET B 2 84 ? 47.812 -27.925 -15.682 1.00 71.93 ? 84 MET B SD 1 ATOM 3208 C CE . MET B 2 84 ? 46.722 -26.555 -16.030 1.00 73.65 ? 84 MET B CE 1 ATOM 3209 N N . GLU B 2 85 ? 48.527 -23.525 -16.984 1.00 71.72 ? 85 GLU B N 1 ATOM 3210 C CA . GLU B 2 85 ? 47.408 -22.940 -17.713 1.00 70.85 ? 85 GLU B CA 1 ATOM 3211 C C . GLU B 2 85 ? 47.922 -22.164 -18.919 1.00 68.33 ? 85 GLU B C 1 ATOM 3212 O O . GLU B 2 85 ? 47.428 -22.345 -20.031 1.00 67.03 ? 85 GLU B O 1 ATOM 3213 C CB . GLU B 2 85 ? 46.522 -22.079 -16.806 1.00 74.61 ? 85 GLU B CB 1 ATOM 3214 C CG . GLU B 2 85 ? 45.921 -22.869 -15.641 1.00 78.75 ? 85 GLU B CG 1 ATOM 3215 C CD . GLU B 2 85 ? 44.417 -22.705 -15.475 1.00 84.16 ? 85 GLU B CD 1 ATOM 3216 O OE1 . GLU B 2 85 ? 43.971 -21.614 -15.050 1.00 89.22 ? 85 GLU B OE1 1 ATOM 3217 O OE2 . GLU B 2 85 ? 43.679 -23.685 -15.739 1.00 85.81 ? 85 GLU B OE2 1 ATOM 3218 N N . ASP B 2 86 ? 48.943 -21.342 -18.703 1.00 67.48 ? 86 ASP B N 1 ATOM 3219 C CA . ASP B 2 86 ? 49.568 -20.578 -19.784 1.00 66.79 ? 86 ASP B CA 1 ATOM 3220 C C . ASP B 2 86 ? 50.181 -21.457 -20.859 1.00 63.15 ? 86 ASP B C 1 ATOM 3221 O O . ASP B 2 86 ? 50.078 -21.155 -22.042 1.00 62.46 ? 86 ASP B O 1 ATOM 3222 C CB . ASP B 2 86 ? 50.652 -19.644 -19.241 1.00 70.35 ? 86 ASP B CB 1 ATOM 3223 C CG . ASP B 2 86 ? 50.132 -18.261 -18.961 1.00 75.73 ? 86 ASP B CG 1 ATOM 3224 O OD1 . ASP B 2 86 ? 49.554 -17.649 -19.894 1.00 80.38 ? 86 ASP B OD1 1 ATOM 3225 O OD2 . ASP B 2 86 ? 50.306 -17.782 -17.817 1.00 79.20 ? 86 ASP B OD2 1 ATOM 3226 N N . GLY B 2 87 ? 50.839 -22.529 -20.439 1.00 61.40 ? 87 GLY B N 1 ATOM 3227 C CA . GLY B 2 87 ? 51.478 -23.444 -21.367 1.00 60.59 ? 87 GLY B CA 1 ATOM 3228 C C . GLY B 2 87 ? 50.514 -23.971 -22.410 1.00 59.24 ? 87 GLY B C 1 ATOM 3229 O O . GLY B 2 87 ? 50.825 -23.992 -23.602 1.00 58.67 ? 87 GLY B O 1 ATOM 3230 N N . PHE B 2 88 ? 49.334 -24.383 -21.967 1.00 58.71 ? 88 PHE B N 1 ATOM 3231 C CA . PHE B 2 88 ? 48.332 -24.911 -22.881 1.00 57.54 ? 88 PHE B CA 1 ATOM 3232 C C . PHE B 2 88 ? 47.756 -23.830 -23.807 1.00 57.58 ? 88 PHE B C 1 ATOM 3233 O O . PHE B 2 88 ? 47.491 -24.107 -24.977 1.00 57.21 ? 88 PHE B O 1 ATOM 3234 C CB . PHE B 2 88 ? 47.225 -25.632 -22.109 1.00 58.20 ? 88 PHE B CB 1 ATOM 3235 C CG . PHE B 2 88 ? 47.637 -26.978 -21.569 1.00 58.76 ? 88 PHE B CG 1 ATOM 3236 C CD1 . PHE B 2 88 ? 48.052 -27.985 -22.424 1.00 59.52 ? 88 PHE B CD1 1 ATOM 3237 C CD2 . PHE B 2 88 ? 47.596 -27.244 -20.212 1.00 60.89 ? 88 PHE B CD2 1 ATOM 3238 C CE1 . PHE B 2 88 ? 48.425 -29.229 -21.940 1.00 61.24 ? 88 PHE B CE1 1 ATOM 3239 C CE2 . PHE B 2 88 ? 47.964 -28.486 -19.717 1.00 62.68 ? 88 PHE B CE2 1 ATOM 3240 C CZ . PHE B 2 88 ? 48.382 -29.480 -20.583 1.00 63.27 ? 88 PHE B CZ 1 ATOM 3241 N N . LEU B 2 89 ? 47.583 -22.607 -23.307 1.00 58.35 ? 89 LEU B N 1 ATOM 3242 C CA . LEU B 2 89 ? 47.119 -21.508 -24.161 1.00 60.12 ? 89 LEU B CA 1 ATOM 3243 C C . LEU B 2 89 ? 48.089 -21.234 -25.308 1.00 57.24 ? 89 LEU B C 1 ATOM 3244 O O . LEU B 2 89 ? 47.677 -21.030 -26.437 1.00 55.28 ? 89 LEU B O 1 ATOM 3245 C CB . LEU B 2 89 ? 46.928 -20.220 -23.369 1.00 64.53 ? 89 LEU B CB 1 ATOM 3246 C CG . LEU B 2 89 ? 45.888 -20.251 -22.250 1.00 70.21 ? 89 LEU B CG 1 ATOM 3247 C CD1 . LEU B 2 89 ? 45.856 -18.889 -21.559 1.00 73.97 ? 89 LEU B CD1 1 ATOM 3248 C CD2 . LEU B 2 89 ? 44.504 -20.655 -22.761 1.00 71.40 ? 89 LEU B CD2 1 ATOM 3249 N N . ASP B 2 90 ? 49.378 -21.221 -25.008 1.00 56.87 ? 90 ASP B N 1 ATOM 3250 C CA . ASP B 2 90 ? 50.391 -21.053 -26.044 1.00 57.38 ? 90 ASP B CA 1 ATOM 3251 C C . ASP B 2 90 ? 50.343 -22.184 -27.081 1.00 54.43 ? 90 ASP B C 1 ATOM 3252 O O . ASP B 2 90 ? 50.515 -21.947 -28.272 1.00 53.46 ? 90 ASP B O 1 ATOM 3253 C CB . ASP B 2 90 ? 51.788 -20.965 -25.422 1.00 58.84 ? 90 ASP B CB 1 ATOM 3254 C CG . ASP B 2 90 ? 52.005 -19.674 -24.664 1.00 63.36 ? 90 ASP B CG 1 ATOM 3255 O OD1 . ASP B 2 90 ? 51.214 -18.724 -24.863 1.00 64.55 ? 90 ASP B OD1 1 ATOM 3256 O OD2 . ASP B 2 90 ? 52.970 -19.607 -23.868 1.00 67.78 ? 90 ASP B OD2 1 ATOM 3257 N N . VAL B 2 91 ? 50.109 -23.405 -26.614 1.00 52.80 ? 91 VAL B N 1 ATOM 3258 C CA . VAL B 2 91 ? 50.034 -24.559 -27.492 1.00 51.54 ? 91 VAL B CA 1 ATOM 3259 C C . VAL B 2 91 ? 48.842 -24.450 -28.437 1.00 50.64 ? 91 VAL B C 1 ATOM 3260 O O . VAL B 2 91 ? 48.987 -24.662 -29.642 1.00 51.16 ? 91 VAL B O 1 ATOM 3261 C CB . VAL B 2 91 ? 49.957 -25.882 -26.703 1.00 51.10 ? 91 VAL B CB 1 ATOM 3262 C CG1 . VAL B 2 91 ? 49.679 -27.052 -27.639 1.00 50.40 ? 91 VAL B CG1 1 ATOM 3263 C CG2 . VAL B 2 91 ? 51.258 -26.116 -25.953 1.00 52.22 ? 91 VAL B CG2 1 ATOM 3264 N N . TRP B 2 92 ? 47.676 -24.120 -27.896 1.00 50.08 ? 92 TRP B N 1 ATOM 3265 C CA . TRP B 2 92 ? 46.476 -23.997 -28.717 1.00 50.09 ? 92 TRP B CA 1 ATOM 3266 C C . TRP B 2 92 ? 46.471 -22.746 -29.587 1.00 50.43 ? 92 TRP B C 1 ATOM 3267 O O . TRP B 2 92 ? 45.886 -22.743 -30.663 1.00 50.83 ? 92 TRP B O 1 ATOM 3268 C CB . TRP B 2 92 ? 45.229 -24.058 -27.840 1.00 51.19 ? 92 TRP B CB 1 ATOM 3269 C CG . TRP B 2 92 ? 45.013 -25.438 -27.326 1.00 52.14 ? 92 TRP B CG 1 ATOM 3270 C CD1 . TRP B 2 92 ? 45.135 -25.861 -26.041 1.00 53.11 ? 92 TRP B CD1 1 ATOM 3271 C CD2 . TRP B 2 92 ? 44.686 -26.595 -28.103 1.00 52.16 ? 92 TRP B CD2 1 ATOM 3272 N NE1 . TRP B 2 92 ? 44.885 -27.208 -25.960 1.00 54.63 ? 92 TRP B NE1 1 ATOM 3273 C CE2 . TRP B 2 92 ? 44.605 -27.684 -27.213 1.00 53.78 ? 92 TRP B CE2 1 ATOM 3274 C CE3 . TRP B 2 92 ? 44.443 -26.814 -29.465 1.00 52.03 ? 92 TRP B CE3 1 ATOM 3275 C CZ2 . TRP B 2 92 ? 44.281 -28.976 -27.635 1.00 55.19 ? 92 TRP B CZ2 1 ATOM 3276 C CZ3 . TRP B 2 92 ? 44.119 -28.093 -29.888 1.00 52.86 ? 92 TRP B CZ3 1 ATOM 3277 C CH2 . TRP B 2 92 ? 44.039 -29.161 -28.972 1.00 54.92 ? 92 TRP B CH2 1 ATOM 3278 N N . THR B 2 93 ? 47.129 -21.691 -29.125 1.00 51.70 ? 93 THR B N 1 ATOM 3279 C CA . THR B 2 93 ? 47.238 -20.475 -29.900 1.00 52.49 ? 93 THR B CA 1 ATOM 3280 C C . THR B 2 93 ? 48.100 -20.757 -31.125 1.00 52.18 ? 93 THR B C 1 ATOM 3281 O O . THR B 2 93 ? 47.742 -20.369 -32.243 1.00 53.09 ? 93 THR B O 1 ATOM 3282 C CB . THR B 2 93 ? 47.832 -19.336 -29.060 1.00 54.36 ? 93 THR B CB 1 ATOM 3283 O OG1 . THR B 2 93 ? 46.922 -19.018 -28.002 1.00 56.57 ? 93 THR B OG1 1 ATOM 3284 C CG2 . THR B 2 93 ? 48.046 -18.101 -29.895 1.00 56.10 ? 93 THR B CG2 1 ATOM 3285 N N . TYR B 2 94 ? 49.216 -21.450 -30.905 1.00 50.96 ? 94 TYR B N 1 ATOM 3286 C CA . TYR B 2 94 ? 50.121 -21.863 -31.979 1.00 50.21 ? 94 TYR B CA 1 ATOM 3287 C C . TYR B 2 94 ? 49.385 -22.767 -32.957 1.00 49.52 ? 94 TYR B C 1 ATOM 3288 O O . TYR B 2 94 ? 49.353 -22.497 -34.153 1.00 49.48 ? 94 TYR B O 1 ATOM 3289 C CB . TYR B 2 94 ? 51.347 -22.575 -31.398 1.00 50.63 ? 94 TYR B CB 1 ATOM 3290 C CG . TYR B 2 94 ? 52.208 -23.292 -32.410 1.00 51.61 ? 94 TYR B CG 1 ATOM 3291 C CD1 . TYR B 2 94 ? 51.925 -24.609 -32.789 1.00 51.27 ? 94 TYR B CD1 1 ATOM 3292 C CD2 . TYR B 2 94 ? 53.317 -22.672 -32.980 1.00 52.97 ? 94 TYR B CD2 1 ATOM 3293 C CE1 . TYR B 2 94 ? 52.711 -25.278 -33.713 1.00 51.48 ? 94 TYR B CE1 1 ATOM 3294 C CE2 . TYR B 2 94 ? 54.108 -23.334 -33.911 1.00 53.94 ? 94 TYR B CE2 1 ATOM 3295 C CZ . TYR B 2 94 ? 53.798 -24.640 -34.271 1.00 53.19 ? 94 TYR B CZ 1 ATOM 3296 O OH . TYR B 2 94 ? 54.571 -25.313 -35.189 1.00 54.56 ? 94 TYR B OH 1 ATOM 3297 N N . ASN B 2 95 ? 48.771 -23.825 -32.441 1.00 50.11 ? 95 ASN B N 1 ATOM 3298 C CA . ASN B 2 95 ? 47.967 -24.722 -33.271 1.00 49.58 ? 95 ASN B CA 1 ATOM 3299 C C . ASN B 2 95 ? 46.986 -23.970 -34.164 1.00 49.46 ? 95 ASN B C 1 ATOM 3300 O O . ASN B 2 95 ? 46.938 -24.208 -35.363 1.00 48.77 ? 95 ASN B O 1 ATOM 3301 C CB . ASN B 2 95 ? 47.194 -25.724 -32.415 1.00 50.11 ? 95 ASN B CB 1 ATOM 3302 C CG . ASN B 2 95 ? 48.076 -26.812 -31.839 1.00 51.91 ? 95 ASN B CG 1 ATOM 3303 O OD1 . ASN B 2 95 ? 49.266 -26.886 -32.121 1.00 53.06 ? 95 ASN B OD1 1 ATOM 3304 N ND2 . ASN B 2 95 ? 47.485 -27.670 -31.023 1.00 54.39 ? 95 ASN B ND2 1 ATOM 3305 N N . ALA B 2 96 ? 46.209 -23.065 -33.580 1.00 50.25 ? 96 ALA B N 1 ATOM 3306 C CA . ALA B 2 96 ? 45.188 -22.349 -34.343 1.00 51.43 ? 96 ALA B CA 1 ATOM 3307 C C . ALA B 2 96 ? 45.807 -21.454 -35.418 1.00 51.18 ? 96 ALA B C 1 ATOM 3308 O O . ALA B 2 96 ? 45.366 -21.458 -36.562 1.00 50.11 ? 96 ALA B O 1 ATOM 3309 C CB . ALA B 2 96 ? 44.313 -21.519 -33.417 1.00 53.06 ? 96 ALA B CB 1 ATOM 3310 N N . GLU B 2 97 ? 46.826 -20.688 -35.045 1.00 51.75 ? 97 GLU B N 1 ATOM 3311 C CA . GLU B 2 97 ? 47.422 -19.728 -35.971 1.00 52.84 ? 97 GLU B CA 1 ATOM 3312 C C . GLU B 2 97 ? 48.125 -20.430 -37.125 1.00 51.95 ? 97 GLU B C 1 ATOM 3313 O O . GLU B 2 97 ? 48.075 -19.963 -38.258 1.00 52.04 ? 97 GLU B O 1 ATOM 3314 C CB . GLU B 2 97 ? 48.367 -18.770 -35.235 1.00 54.35 ? 97 GLU B CB 1 ATOM 3315 C CG . GLU B 2 97 ? 47.617 -17.606 -34.596 1.00 57.15 ? 97 GLU B CG 1 ATOM 3316 C CD . GLU B 2 97 ? 48.447 -16.778 -33.637 1.00 60.50 ? 97 GLU B CD 1 ATOM 3317 O OE1 . GLU B 2 97 ? 49.641 -17.083 -33.434 1.00 62.96 ? 97 GLU B OE1 1 ATOM 3318 O OE2 . GLU B 2 97 ? 47.897 -15.809 -33.074 1.00 64.11 ? 97 GLU B OE2 1 ATOM 3319 N N . LEU B 2 98 ? 48.752 -21.567 -36.834 1.00 51.71 ? 98 LEU B N 1 ATOM 3320 C CA . LEU B 2 98 ? 49.492 -22.315 -37.840 1.00 50.55 ? 98 LEU B CA 1 ATOM 3321 C C . LEU B 2 98 ? 48.552 -23.015 -38.803 1.00 48.89 ? 98 LEU B C 1 ATOM 3322 O O . LEU B 2 98 ? 48.802 -23.051 -39.997 1.00 49.42 ? 98 LEU B O 1 ATOM 3323 C CB . LEU B 2 98 ? 50.385 -23.348 -37.179 1.00 51.66 ? 98 LEU B CB 1 ATOM 3324 C CG . LEU B 2 98 ? 51.328 -24.086 -38.130 1.00 53.29 ? 98 LEU B CG 1 ATOM 3325 C CD1 . LEU B 2 98 ? 52.391 -23.136 -38.664 1.00 54.72 ? 98 LEU B CD1 1 ATOM 3326 C CD2 . LEU B 2 98 ? 51.961 -25.273 -37.416 1.00 53.77 ? 98 LEU B CD2 1 ATOM 3327 N N . LEU B 2 99 ? 47.476 -23.580 -38.281 1.00 47.90 ? 99 LEU B N 1 ATOM 3328 C CA . LEU B 2 99 ? 46.500 -24.257 -39.113 1.00 48.09 ? 99 LEU B CA 1 ATOM 3329 C C . LEU B 2 99 ? 45.893 -23.274 -40.117 1.00 47.73 ? 99 LEU B C 1 ATOM 3330 O O . LEU B 2 99 ? 45.762 -23.579 -41.309 1.00 47.61 ? 99 LEU B O 1 ATOM 3331 C CB . LEU B 2 99 ? 45.402 -24.881 -38.245 1.00 49.97 ? 99 LEU B CB 1 ATOM 3332 C CG . LEU B 2 99 ? 44.348 -25.719 -38.980 1.00 52.07 ? 99 LEU B CG 1 ATOM 3333 C CD1 . LEU B 2 99 ? 44.997 -26.903 -39.684 1.00 53.17 ? 99 LEU B CD1 1 ATOM 3334 C CD2 . LEU B 2 99 ? 43.269 -26.187 -38.015 1.00 54.22 ? 99 LEU B CD2 1 ATOM 3335 N N . VAL B 2 100 ? 45.525 -22.092 -39.634 1.00 46.76 ? 100 VAL B N 1 ATOM 3336 C CA . VAL B 2 100 ? 44.986 -21.060 -40.507 1.00 45.47 ? 100 VAL B CA 1 ATOM 3337 C C . VAL B 2 100 ? 45.974 -20.685 -41.613 1.00 43.96 ? 100 VAL B C 1 ATOM 3338 O O . VAL B 2 100 ? 45.579 -20.614 -42.776 1.00 42.15 ? 100 VAL B O 1 ATOM 3339 C CB . VAL B 2 100 ? 44.545 -19.819 -39.710 1.00 46.45 ? 100 VAL B CB 1 ATOM 3340 C CG1 . VAL B 2 100 ? 44.323 -18.622 -40.628 1.00 46.80 ? 100 VAL B CG1 1 ATOM 3341 C CG2 . VAL B 2 100 ? 43.271 -20.153 -38.947 1.00 47.47 ? 100 VAL B CG2 1 ATOM 3342 N N . LEU B 2 101 ? 47.238 -20.451 -41.256 1.00 43.21 ? 101 LEU B N 1 ATOM 3343 C CA . LEU B 2 101 ? 48.268 -20.118 -42.253 1.00 43.78 ? 101 LEU B CA 1 ATOM 3344 C C . LEU B 2 101 ? 48.412 -21.220 -43.305 1.00 43.87 ? 101 LEU B C 1 ATOM 3345 O O . LEU B 2 101 ? 48.348 -20.968 -44.505 1.00 44.90 ? 101 LEU B O 1 ATOM 3346 C CB . LEU B 2 101 ? 49.631 -19.890 -41.589 1.00 44.33 ? 101 LEU B CB 1 ATOM 3347 C CG . LEU B 2 101 ? 49.819 -18.588 -40.820 1.00 46.84 ? 101 LEU B CG 1 ATOM 3348 C CD1 . LEU B 2 101 ? 51.250 -18.492 -40.317 1.00 49.13 ? 101 LEU B CD1 1 ATOM 3349 C CD2 . LEU B 2 101 ? 49.488 -17.371 -41.669 1.00 48.32 ? 101 LEU B CD2 1 ATOM 3350 N N . MET B 2 102 ? 48.611 -22.443 -42.842 1.00 44.05 ? 102 MET B N 1 ATOM 3351 C CA . MET B 2 102 ? 48.840 -23.561 -43.724 1.00 44.83 ? 102 MET B CA 1 ATOM 3352 C C . MET B 2 102 ? 47.659 -23.806 -44.650 1.00 44.54 ? 102 MET B C 1 ATOM 3353 O O . MET B 2 102 ? 47.842 -24.034 -45.852 1.00 45.21 ? 102 MET B O 1 ATOM 3354 C CB . MET B 2 102 ? 49.105 -24.816 -42.909 1.00 46.86 ? 102 MET B CB 1 ATOM 3355 C CG . MET B 2 102 ? 50.451 -24.833 -42.217 1.00 49.52 ? 102 MET B CG 1 ATOM 3356 S SD . MET B 2 102 ? 50.659 -26.400 -41.349 1.00 53.78 ? 102 MET B SD 1 ATOM 3357 C CE . MET B 2 102 ? 52.442 -26.549 -41.430 1.00 56.30 ? 102 MET B CE 1 ATOM 3358 N N . GLU B 2 103 ? 46.453 -23.764 -44.098 1.00 43.80 ? 103 GLU B N 1 ATOM 3359 C CA . GLU B 2 103 ? 45.270 -24.083 -44.881 1.00 45.37 ? 103 GLU B CA 1 ATOM 3360 C C . GLU B 2 103 ? 44.856 -22.939 -45.803 1.00 45.14 ? 103 GLU B C 1 ATOM 3361 O O . GLU B 2 103 ? 44.270 -23.169 -46.861 1.00 44.82 ? 103 GLU B O 1 ATOM 3362 C CB . GLU B 2 103 ? 44.122 -24.519 -43.969 1.00 47.85 ? 103 GLU B CB 1 ATOM 3363 C CG . GLU B 2 103 ? 44.367 -25.880 -43.312 1.00 50.65 ? 103 GLU B CG 1 ATOM 3364 C CD . GLU B 2 103 ? 44.472 -27.027 -44.313 1.00 53.43 ? 103 GLU B CD 1 ATOM 3365 O OE1 . GLU B 2 103 ? 43.851 -26.939 -45.394 1.00 53.93 ? 103 GLU B OE1 1 ATOM 3366 O OE2 . GLU B 2 103 ? 45.178 -28.029 -44.025 1.00 58.78 ? 103 GLU B OE2 1 ATOM 3367 N N . ASN B 2 104 ? 45.161 -21.709 -45.413 1.00 45.92 ? 104 ASN B N 1 ATOM 3368 C CA . ASN B 2 104 ? 44.973 -20.584 -46.312 1.00 46.65 ? 104 ASN B CA 1 ATOM 3369 C C . ASN B 2 104 ? 45.817 -20.762 -47.561 1.00 46.92 ? 104 ASN B C 1 ATOM 3370 O O . ASN B 2 104 ? 45.344 -20.569 -48.674 1.00 45.57 ? 104 ASN B O 1 ATOM 3371 C CB . ASN B 2 104 ? 45.336 -19.270 -45.626 1.00 47.77 ? 104 ASN B CB 1 ATOM 3372 C CG . ASN B 2 104 ? 44.239 -18.776 -44.711 1.00 48.70 ? 104 ASN B CG 1 ATOM 3373 O OD1 . ASN B 2 104 ? 43.117 -19.282 -44.745 1.00 47.64 ? 104 ASN B OD1 1 ATOM 3374 N ND2 . ASN B 2 104 ? 44.554 -17.777 -43.889 1.00 50.09 ? 104 ASN B ND2 1 ATOM 3375 N N . GLU B 2 105 ? 47.070 -21.144 -47.372 1.00 48.34 ? 105 GLU B N 1 ATOM 3376 C CA . GLU B 2 105 ? 47.924 -21.424 -48.501 1.00 49.67 ? 105 GLU B CA 1 ATOM 3377 C C . GLU B 2 105 ? 47.330 -22.524 -49.370 1.00 46.45 ? 105 GLU B C 1 ATOM 3378 O O . GLU B 2 105 ? 47.276 -22.391 -50.586 1.00 44.69 ? 105 GLU B O 1 ATOM 3379 C CB . GLU B 2 105 ? 49.305 -21.828 -48.029 1.00 55.05 ? 105 GLU B CB 1 ATOM 3380 C CG . GLU B 2 105 ? 50.370 -21.662 -49.087 1.00 62.60 ? 105 GLU B CG 1 ATOM 3381 C CD . GLU B 2 105 ? 51.717 -21.435 -48.459 1.00 72.39 ? 105 GLU B CD 1 ATOM 3382 O OE1 . GLU B 2 105 ? 52.164 -22.340 -47.721 1.00 82.92 ? 105 GLU B OE1 1 ATOM 3383 O OE2 . GLU B 2 105 ? 52.307 -20.349 -48.671 1.00 78.00 ? 105 GLU B OE2 1 ATOM 3384 N N . ARG B 2 106 ? 46.873 -23.605 -48.752 1.00 45.67 ? 106 ARG B N 1 ATOM 3385 C CA . ARG B 2 106 ? 46.294 -24.700 -49.522 1.00 47.75 ? 106 ARG B CA 1 ATOM 3386 C C . ARG B 2 106 ? 45.009 -24.283 -50.247 1.00 45.15 ? 106 ARG B C 1 ATOM 3387 O O . ARG B 2 106 ? 44.777 -24.691 -51.378 1.00 45.35 ? 106 ARG B O 1 ATOM 3388 C CB . ARG B 2 106 ? 46.061 -25.930 -48.644 1.00 51.93 ? 106 ARG B CB 1 ATOM 3389 C CG . ARG B 2 106 ? 47.356 -26.550 -48.125 1.00 57.81 ? 106 ARG B CG 1 ATOM 3390 C CD . ARG B 2 106 ? 47.202 -28.020 -47.738 1.00 65.81 ? 106 ARG B CD 1 ATOM 3391 N NE . ARG B 2 106 ? 47.774 -28.949 -48.738 1.00 72.71 ? 106 ARG B NE 1 ATOM 3392 C CZ . ARG B 2 106 ? 47.095 -29.858 -49.450 1.00 77.82 ? 106 ARG B CZ 1 ATOM 3393 N NH1 . ARG B 2 106 ? 45.779 -30.014 -49.313 1.00 79.28 ? 106 ARG B NH1 1 ATOM 3394 N NH2 . ARG B 2 106 ? 47.744 -30.641 -50.312 1.00 84.73 ? 106 ARG B NH2 1 ATOM 3395 N N . THR B 2 107 ? 44.190 -23.453 -49.609 1.00 43.46 ? 107 THR B N 1 ATOM 3396 C CA . THR B 2 107 ? 42.953 -22.978 -50.222 1.00 41.69 ? 107 THR B CA 1 ATOM 3397 C C . THR B 2 107 ? 43.236 -22.150 -51.486 1.00 41.49 ? 107 THR B C 1 ATOM 3398 O O . THR B 2 107 ? 42.606 -22.358 -52.522 1.00 40.95 ? 107 THR B O 1 ATOM 3399 C CB . THR B 2 107 ? 42.093 -22.188 -49.212 1.00 41.79 ? 107 THR B CB 1 ATOM 3400 O OG1 . THR B 2 107 ? 41.625 -23.077 -48.185 1.00 41.55 ? 107 THR B OG1 1 ATOM 3401 C CG2 . THR B 2 107 ? 40.887 -21.556 -49.892 1.00 42.31 ? 107 THR B CG2 1 ATOM 3402 N N . LEU B 2 108 ? 44.192 -21.234 -51.418 1.00 40.82 ? 108 LEU B N 1 ATOM 3403 C CA . LEU B 2 108 ? 44.532 -20.443 -52.587 1.00 41.91 ? 108 LEU B CA 1 ATOM 3404 C C . LEU B 2 108 ? 45.058 -21.308 -53.741 1.00 41.95 ? 108 LEU B C 1 ATOM 3405 O O . LEU B 2 108 ? 44.659 -21.121 -54.896 1.00 40.71 ? 108 LEU B O 1 ATOM 3406 C CB . LEU B 2 108 ? 45.535 -19.348 -52.229 1.00 42.94 ? 108 LEU B CB 1 ATOM 3407 C CG . LEU B 2 108 ? 45.019 -18.282 -51.256 1.00 44.60 ? 108 LEU B CG 1 ATOM 3408 C CD1 . LEU B 2 108 ? 46.073 -17.205 -51.062 1.00 46.98 ? 108 LEU B CD1 1 ATOM 3409 C CD2 . LEU B 2 108 ? 43.711 -17.656 -51.716 1.00 45.32 ? 108 LEU B CD2 1 ATOM 3410 N N . ASP B 2 109 ? 45.944 -22.248 -53.424 1.00 42.69 ? 109 ASP B N 1 ATOM 3411 C CA . ASP B 2 109 ? 46.474 -23.182 -54.421 1.00 43.08 ? 109 ASP B CA 1 ATOM 3412 C C . ASP B 2 109 ? 45.390 -24.092 -55.020 1.00 42.55 ? 109 ASP B C 1 ATOM 3413 O O . ASP B 2 109 ? 45.497 -24.518 -56.164 1.00 44.68 ? 109 ASP B O 1 ATOM 3414 C CB . ASP B 2 109 ? 47.547 -24.064 -53.799 1.00 45.04 ? 109 ASP B CB 1 ATOM 3415 C CG . ASP B 2 109 ? 48.837 -23.302 -53.465 1.00 48.69 ? 109 ASP B CG 1 ATOM 3416 O OD1 . ASP B 2 109 ? 49.191 -22.356 -54.210 1.00 47.86 ? 109 ASP B OD1 1 ATOM 3417 O OD2 . ASP B 2 109 ? 49.509 -23.698 -52.461 1.00 51.07 ? 109 ASP B OD2 1 ATOM 3418 N N . PHE B 2 110 ? 44.367 -24.405 -54.233 1.00 40.68 ? 110 PHE B N 1 ATOM 3419 C CA . PHE B 2 110 ? 43.279 -25.280 -54.657 1.00 39.71 ? 110 PHE B CA 1 ATOM 3420 C C . PHE B 2 110 ? 42.476 -24.601 -55.759 1.00 40.02 ? 110 PHE B C 1 ATOM 3421 O O . PHE B 2 110 ? 42.148 -25.222 -56.772 1.00 40.14 ? 110 PHE B O 1 ATOM 3422 C CB . PHE B 2 110 ? 42.422 -25.613 -53.431 1.00 39.75 ? 110 PHE B CB 1 ATOM 3423 C CG . PHE B 2 110 ? 41.137 -26.321 -53.730 1.00 40.35 ? 110 PHE B CG 1 ATOM 3424 C CD1 . PHE B 2 110 ? 41.128 -27.552 -54.369 1.00 41.78 ? 110 PHE B CD1 1 ATOM 3425 C CD2 . PHE B 2 110 ? 39.931 -25.785 -53.307 1.00 40.81 ? 110 PHE B CD2 1 ATOM 3426 C CE1 . PHE B 2 110 ? 39.930 -28.207 -54.631 1.00 43.51 ? 110 PHE B CE1 1 ATOM 3427 C CE2 . PHE B 2 110 ? 38.726 -26.437 -53.565 1.00 43.01 ? 110 PHE B CE2 1 ATOM 3428 C CZ . PHE B 2 110 ? 38.726 -27.649 -54.231 1.00 43.84 ? 110 PHE B CZ 1 ATOM 3429 N N . HIS B 2 111 ? 42.188 -23.315 -55.567 1.00 40.46 ? 111 HIS B N 1 ATOM 3430 C CA . HIS B 2 111 ? 41.546 -22.492 -56.592 1.00 40.84 ? 111 HIS B CA 1 ATOM 3431 C C . HIS B 2 111 ? 42.421 -22.379 -57.860 1.00 41.53 ? 111 HIS B C 1 ATOM 3432 O O . HIS B 2 111 ? 41.925 -22.485 -58.988 1.00 42.36 ? 111 HIS B O 1 ATOM 3433 C CB . HIS B 2 111 ? 41.268 -21.085 -56.057 1.00 41.46 ? 111 HIS B CB 1 ATOM 3434 C CG . HIS B 2 111 ? 40.150 -21.011 -55.061 1.00 41.96 ? 111 HIS B CG 1 ATOM 3435 N ND1 . HIS B 2 111 ? 38.854 -21.357 -55.372 1.00 42.42 ? 111 HIS B ND1 1 ATOM 3436 C CD2 . HIS B 2 111 ? 40.128 -20.577 -53.778 1.00 41.95 ? 111 HIS B CD2 1 ATOM 3437 C CE1 . HIS B 2 111 ? 38.086 -21.164 -54.316 1.00 44.03 ? 111 HIS B CE1 1 ATOM 3438 N NE2 . HIS B 2 111 ? 38.833 -20.686 -53.336 1.00 43.27 ? 111 HIS B NE2 1 ATOM 3439 N N . ASP B 2 112 ? 43.717 -22.157 -57.673 1.00 40.61 ? 112 ASP B N 1 ATOM 3440 C CA . ASP B 2 112 ? 44.656 -22.150 -58.787 1.00 40.65 ? 112 ASP B CA 1 ATOM 3441 C C . ASP B 2 112 ? 44.531 -23.471 -59.553 1.00 41.44 ? 112 ASP B C 1 ATOM 3442 O O . ASP B 2 112 ? 44.448 -23.486 -60.779 1.00 43.59 ? 112 ASP B O 1 ATOM 3443 C CB . ASP B 2 112 ? 46.090 -21.956 -58.267 1.00 41.54 ? 112 ASP B CB 1 ATOM 3444 C CG . ASP B 2 112 ? 47.060 -21.509 -59.351 1.00 44.01 ? 112 ASP B CG 1 ATOM 3445 O OD1 . ASP B 2 112 ? 46.615 -21.200 -60.484 1.00 45.47 ? 112 ASP B OD1 1 ATOM 3446 O OD2 . ASP B 2 112 ? 48.279 -21.473 -59.073 1.00 44.98 ? 112 ASP B OD2 1 ATOM 3447 N N . SER B 2 113 ? 44.487 -24.579 -58.817 1.00 40.83 ? 113 SER B N 1 ATOM 3448 C CA . SER B 2 113 ? 44.421 -25.910 -59.412 1.00 40.91 ? 113 SER B CA 1 ATOM 3449 C C . SER B 2 113 ? 43.137 -26.138 -60.210 1.00 41.53 ? 113 SER B C 1 ATOM 3450 O O . SER B 2 113 ? 43.168 -26.691 -61.312 1.00 41.82 ? 113 SER B O 1 ATOM 3451 C CB . SER B 2 113 ? 44.542 -26.978 -58.320 1.00 40.85 ? 113 SER B CB 1 ATOM 3452 O OG . SER B 2 113 ? 44.222 -28.257 -58.821 1.00 41.95 ? 113 SER B OG 1 ATOM 3453 N N . ASN B 2 114 ? 42.008 -25.731 -59.641 1.00 41.18 ? 114 ASN B N 1 ATOM 3454 C CA . ASN B 2 114 ? 40.725 -25.880 -60.320 1.00 41.65 ? 114 ASN B CA 1 ATOM 3455 C C . ASN B 2 114 ? 40.682 -25.093 -61.639 1.00 41.42 ? 114 ASN B C 1 ATOM 3456 O O . ASN B 2 114 ? 40.078 -25.551 -62.611 1.00 41.98 ? 114 ASN B O 1 ATOM 3457 C CB . ASN B 2 114 ? 39.577 -25.437 -59.409 1.00 42.04 ? 114 ASN B CB 1 ATOM 3458 C CG . ASN B 2 114 ? 39.397 -26.337 -58.200 1.00 42.87 ? 114 ASN B CG 1 ATOM 3459 O OD1 . ASN B 2 114 ? 39.639 -27.545 -58.251 1.00 44.47 ? 114 ASN B OD1 1 ATOM 3460 N ND2 . ASN B 2 114 ? 38.948 -25.751 -57.109 1.00 42.42 ? 114 ASN B ND2 1 ATOM 3461 N N . VAL B 2 115 ? 41.327 -23.922 -61.677 1.00 40.21 ? 115 VAL B N 1 ATOM 3462 C CA . VAL B 2 115 ? 41.349 -23.105 -62.890 1.00 40.26 ? 115 VAL B CA 1 ATOM 3463 C C . VAL B 2 115 ? 42.228 -23.766 -63.950 1.00 41.26 ? 115 VAL B C 1 ATOM 3464 O O . VAL B 2 115 ? 41.841 -23.888 -65.108 1.00 40.79 ? 115 VAL B O 1 ATOM 3465 C CB . VAL B 2 115 ? 41.875 -21.685 -62.618 1.00 40.40 ? 115 VAL B CB 1 ATOM 3466 C CG1 . VAL B 2 115 ? 42.052 -20.917 -63.920 1.00 41.69 ? 115 VAL B CG1 1 ATOM 3467 C CG2 . VAL B 2 115 ? 40.929 -20.922 -61.713 1.00 41.51 ? 115 VAL B CG2 1 ATOM 3468 N N . LYS B 2 116 ? 43.428 -24.162 -63.544 1.00 42.11 ? 116 LYS B N 1 ATOM 3469 C CA . LYS B 2 116 ? 44.339 -24.885 -64.413 1.00 44.60 ? 116 LYS B CA 1 ATOM 3470 C C . LYS B 2 116 ? 43.680 -26.120 -65.019 1.00 45.63 ? 116 LYS B C 1 ATOM 3471 O O . LYS B 2 116 ? 43.836 -26.392 -66.208 1.00 46.83 ? 116 LYS B O 1 ATOM 3472 C CB . LYS B 2 116 ? 45.567 -25.298 -63.616 1.00 46.89 ? 116 LYS B CB 1 ATOM 3473 C CG . LYS B 2 116 ? 46.519 -26.230 -64.328 1.00 50.34 ? 116 LYS B CG 1 ATOM 3474 C CD . LYS B 2 116 ? 47.273 -25.517 -65.430 1.00 53.96 ? 116 LYS B CD 1 ATOM 3475 C CE . LYS B 2 116 ? 48.681 -26.093 -65.584 1.00 59.08 ? 116 LYS B CE 1 ATOM 3476 N NZ . LYS B 2 116 ? 49.662 -24.977 -65.681 1.00 61.58 ? 116 LYS B NZ 1 ATOM 3477 N N . ASN B 2 117 ? 42.946 -26.867 -64.202 1.00 45.87 ? 117 ASN B N 1 ATOM 3478 C CA . ASN B 2 117 ? 42.295 -28.087 -64.675 1.00 48.44 ? 117 ASN B CA 1 ATOM 3479 C C . ASN B 2 117 ? 41.166 -27.786 -65.648 1.00 48.88 ? 117 ASN B C 1 ATOM 3480 O O . ASN B 2 117 ? 40.961 -28.509 -66.619 1.00 50.31 ? 117 ASN B O 1 ATOM 3481 C CB . ASN B 2 117 ? 41.792 -28.929 -63.498 1.00 48.83 ? 117 ASN B CB 1 ATOM 3482 C CG . ASN B 2 117 ? 42.926 -29.549 -62.701 1.00 49.57 ? 117 ASN B CG 1 ATOM 3483 O OD1 . ASN B 2 117 ? 44.022 -29.761 -63.214 1.00 49.95 ? 117 ASN B OD1 1 ATOM 3484 N ND2 . ASN B 2 117 ? 42.666 -29.840 -61.439 1.00 50.17 ? 117 ASN B ND2 1 ATOM 3485 N N . LEU B 2 118 ? 40.439 -26.711 -65.390 1.00 48.01 ? 118 LEU B N 1 ATOM 3486 C CA . LEU B 2 118 ? 39.373 -26.310 -66.288 1.00 49.68 ? 118 LEU B CA 1 ATOM 3487 C C . LEU B 2 118 ? 39.964 -25.920 -67.630 1.00 49.95 ? 118 LEU B C 1 ATOM 3488 O O . LEU B 2 118 ? 39.469 -26.332 -68.676 1.00 52.78 ? 118 LEU B O 1 ATOM 3489 C CB . LEU B 2 118 ? 38.587 -25.157 -65.685 1.00 49.77 ? 118 LEU B CB 1 ATOM 3490 C CG . LEU B 2 118 ? 37.386 -24.651 -66.460 1.00 52.17 ? 118 LEU B CG 1 ATOM 3491 C CD1 . LEU B 2 118 ? 36.476 -25.793 -66.891 1.00 55.53 ? 118 LEU B CD1 1 ATOM 3492 C CD2 . LEU B 2 118 ? 36.641 -23.654 -65.592 1.00 52.72 ? 118 LEU B CD2 1 ATOM 3493 N N . TYR B 2 119 ? 41.044 -25.146 -67.591 1.00 48.57 ? 119 TYR B N 1 ATOM 3494 C CA . TYR B 2 119 ? 41.751 -24.748 -68.795 1.00 47.84 ? 119 TYR B CA 1 ATOM 3495 C C . TYR B 2 119 ? 42.229 -25.966 -69.598 1.00 50.40 ? 119 TYR B C 1 ATOM 3496 O O . TYR B 2 119 ? 42.082 -26.006 -70.815 1.00 53.07 ? 119 TYR B O 1 ATOM 3497 C CB . TYR B 2 119 ? 42.933 -23.834 -68.442 1.00 46.63 ? 119 TYR B CB 1 ATOM 3498 C CG . TYR B 2 119 ? 43.765 -23.426 -69.643 1.00 47.34 ? 119 TYR B CG 1 ATOM 3499 C CD1 . TYR B 2 119 ? 43.366 -22.378 -70.465 1.00 47.46 ? 119 TYR B CD1 1 ATOM 3500 C CD2 . TYR B 2 119 ? 44.944 -24.097 -69.963 1.00 47.83 ? 119 TYR B CD2 1 ATOM 3501 C CE1 . TYR B 2 119 ? 44.113 -22.007 -71.571 1.00 48.53 ? 119 TYR B CE1 1 ATOM 3502 C CE2 . TYR B 2 119 ? 45.698 -23.729 -71.063 1.00 49.08 ? 119 TYR B CE2 1 ATOM 3503 C CZ . TYR B 2 119 ? 45.274 -22.686 -71.862 1.00 49.65 ? 119 TYR B CZ 1 ATOM 3504 O OH . TYR B 2 119 ? 46.003 -22.311 -72.954 1.00 50.84 ? 119 TYR B OH 1 ATOM 3505 N N . ASP B 2 120 ? 42.801 -26.956 -68.929 1.00 51.84 ? 120 ASP B N 1 ATOM 3506 C CA . ASP B 2 120 ? 43.302 -28.133 -69.634 1.00 54.64 ? 120 ASP B CA 1 ATOM 3507 C C . ASP B 2 120 ? 42.146 -28.942 -70.230 1.00 55.28 ? 120 ASP B C 1 ATOM 3508 O O . ASP B 2 120 ? 42.245 -29.463 -71.334 1.00 55.51 ? 120 ASP B O 1 ATOM 3509 C CB . ASP B 2 120 ? 44.179 -28.991 -68.711 1.00 56.80 ? 120 ASP B CB 1 ATOM 3510 C CG . ASP B 2 120 ? 45.550 -28.350 -68.436 1.00 58.79 ? 120 ASP B CG 1 ATOM 3511 O OD1 . ASP B 2 120 ? 46.085 -27.659 -69.333 1.00 59.05 ? 120 ASP B OD1 1 ATOM 3512 O OD2 . ASP B 2 120 ? 46.110 -28.546 -67.325 1.00 61.59 ? 120 ASP B OD2 1 ATOM 3513 N N . LYS B 2 121 ? 41.045 -29.019 -69.503 1.00 55.99 ? 121 LYS B N 1 ATOM 3514 C CA . LYS B 2 121 ? 39.836 -29.680 -69.985 1.00 60.47 ? 121 LYS B CA 1 ATOM 3515 C C . LYS B 2 121 ? 39.435 -29.153 -71.365 1.00 61.33 ? 121 LYS B C 1 ATOM 3516 O O . LYS B 2 121 ? 39.211 -29.929 -72.289 1.00 65.21 ? 121 LYS B O 1 ATOM 3517 C CB . LYS B 2 121 ? 38.710 -29.445 -68.980 1.00 62.08 ? 121 LYS B CB 1 ATOM 3518 C CG . LYS B 2 121 ? 37.460 -30.284 -69.145 1.00 66.70 ? 121 LYS B CG 1 ATOM 3519 C CD . LYS B 2 121 ? 36.529 -29.992 -67.967 1.00 68.76 ? 121 LYS B CD 1 ATOM 3520 C CE . LYS B 2 121 ? 35.216 -30.757 -68.035 1.00 74.25 ? 121 LYS B CE 1 ATOM 3521 N NZ . LYS B 2 121 ? 34.396 -30.348 -69.212 1.00 77.12 ? 121 LYS B NZ 1 ATOM 3522 N N . VAL B 2 122 ? 39.376 -27.831 -71.508 1.00 58.40 ? 122 VAL B N 1 ATOM 3523 C CA . VAL B 2 122 ? 39.050 -27.208 -72.785 1.00 57.60 ? 122 VAL B CA 1 ATOM 3524 C C . VAL B 2 122 ? 40.149 -27.428 -73.822 1.00 58.83 ? 122 VAL B C 1 ATOM 3525 O O . VAL B 2 122 ? 39.862 -27.782 -74.968 1.00 60.19 ? 122 VAL B O 1 ATOM 3526 C CB . VAL B 2 122 ? 38.784 -25.703 -72.615 1.00 56.14 ? 122 VAL B CB 1 ATOM 3527 C CG1 . VAL B 2 122 ? 38.647 -25.005 -73.965 1.00 55.93 ? 122 VAL B CG1 1 ATOM 3528 C CG2 . VAL B 2 122 ? 37.535 -25.500 -71.766 1.00 56.53 ? 122 VAL B CG2 1 ATOM 3529 N N . ARG B 2 123 ? 41.401 -27.223 -73.431 1.00 57.91 ? 123 ARG B N 1 ATOM 3530 C CA . ARG B 2 123 ? 42.522 -27.447 -74.342 1.00 59.65 ? 123 ARG B CA 1 ATOM 3531 C C . ARG B 2 123 ? 42.455 -28.841 -74.972 1.00 63.01 ? 123 ARG B C 1 ATOM 3532 O O . ARG B 2 123 ? 42.607 -28.979 -76.188 1.00 64.33 ? 123 ARG B O 1 ATOM 3533 C CB . ARG B 2 123 ? 43.845 -27.273 -73.606 1.00 60.68 ? 123 ARG B CB 1 ATOM 3534 C CG . ARG B 2 123 ? 45.061 -27.305 -74.513 1.00 63.95 ? 123 ARG B CG 1 ATOM 3535 C CD . ARG B 2 123 ? 46.357 -27.089 -73.740 1.00 65.77 ? 123 ARG B CD 1 ATOM 3536 N NE . ARG B 2 123 ? 46.474 -27.952 -72.560 1.00 67.54 ? 123 ARG B NE 1 ATOM 3537 C CZ . ARG B 2 123 ? 46.798 -29.247 -72.578 1.00 70.52 ? 123 ARG B CZ 1 ATOM 3538 N NH1 . ARG B 2 123 ? 47.046 -29.889 -73.719 1.00 73.75 ? 123 ARG B NH1 1 ATOM 3539 N NH2 . ARG B 2 123 ? 46.869 -29.909 -71.436 1.00 71.69 ? 123 ARG B NH2 1 ATOM 3540 N N . LEU B 2 124 ? 42.202 -29.857 -74.144 1.00 64.94 ? 124 LEU B N 1 ATOM 3541 C CA . LEU B 2 124 ? 42.139 -31.260 -74.595 1.00 69.57 ? 124 LEU B CA 1 ATOM 3542 C C . LEU B 2 124 ? 40.977 -31.574 -75.548 1.00 72.08 ? 124 LEU B C 1 ATOM 3543 O O . LEU B 2 124 ? 41.010 -32.588 -76.241 1.00 75.20 ? 124 LEU B O 1 ATOM 3544 C CB . LEU B 2 124 ? 42.065 -32.210 -73.394 1.00 70.79 ? 124 LEU B CB 1 ATOM 3545 C CG . LEU B 2 124 ? 43.308 -32.247 -72.496 1.00 71.45 ? 124 LEU B CG 1 ATOM 3546 C CD1 . LEU B 2 124 ? 42.999 -32.826 -71.111 1.00 71.69 ? 124 LEU B CD1 1 ATOM 3547 C CD2 . LEU B 2 124 ? 44.439 -33.008 -73.173 1.00 74.52 ? 124 LEU B CD2 1 ATOM 3548 N N . GLN B 2 125 ? 39.948 -30.730 -75.562 1.00 71.44 ? 125 GLN B N 1 ATOM 3549 C CA . GLN B 2 125 ? 38.849 -30.867 -76.515 1.00 73.04 ? 125 GLN B CA 1 ATOM 3550 C C . GLN B 2 125 ? 39.201 -30.223 -77.838 1.00 72.69 ? 125 GLN B C 1 ATOM 3551 O O . GLN B 2 125 ? 39.126 -30.856 -78.890 1.00 75.81 ? 125 GLN B O 1 ATOM 3552 C CB . GLN B 2 125 ? 37.589 -30.200 -75.985 1.00 72.41 ? 125 GLN B CB 1 ATOM 3553 C CG . GLN B 2 125 ? 37.015 -30.861 -74.755 1.00 74.67 ? 125 GLN B CG 1 ATOM 3554 C CD . GLN B 2 125 ? 35.637 -30.334 -74.438 1.00 75.71 ? 125 GLN B CD 1 ATOM 3555 O OE1 . GLN B 2 125 ? 34.663 -30.686 -75.105 1.00 79.20 ? 125 GLN B OE1 1 ATOM 3556 N NE2 . GLN B 2 125 ? 35.544 -29.479 -73.425 1.00 74.18 ? 125 GLN B NE2 1 ATOM 3557 N N . LEU B 2 126 ? 39.581 -28.954 -77.772 1.00 70.74 ? 126 LEU B N 1 ATOM 3558 C CA . LEU B 2 126 ? 39.869 -28.174 -78.967 1.00 72.27 ? 126 LEU B CA 1 ATOM 3559 C C . LEU B 2 126 ? 41.070 -28.719 -79.722 1.00 77.08 ? 126 LEU B C 1 ATOM 3560 O O . LEU B 2 126 ? 41.085 -28.690 -80.945 1.00 80.74 ? 126 LEU B O 1 ATOM 3561 C CB . LEU B 2 126 ? 40.092 -26.700 -78.619 1.00 68.10 ? 126 LEU B CB 1 ATOM 3562 C CG . LEU B 2 126 ? 38.961 -26.020 -77.847 1.00 65.31 ? 126 LEU B CG 1 ATOM 3563 C CD1 . LEU B 2 126 ? 39.217 -24.529 -77.770 1.00 63.57 ? 126 LEU B CD1 1 ATOM 3564 C CD2 . LEU B 2 126 ? 37.611 -26.301 -78.480 1.00 67.16 ? 126 LEU B CD2 1 ATOM 3565 N N . ARG B 2 127 ? 42.068 -29.218 -79.000 1.00 83.48 ? 127 ARG B N 1 ATOM 3566 C CA . ARG B 2 127 ? 43.246 -29.828 -79.629 1.00 90.38 ? 127 ARG B CA 1 ATOM 3567 C C . ARG B 2 127 ? 43.830 -28.865 -80.689 1.00 91.83 ? 127 ARG B C 1 ATOM 3568 O O . ARG B 2 127 ? 44.184 -27.736 -80.347 1.00 91.72 ? 127 ARG B O 1 ATOM 3569 C CB . ARG B 2 127 ? 42.894 -31.222 -80.191 1.00 94.62 ? 127 ARG B CB 1 ATOM 3570 C CG . ARG B 2 127 ? 42.532 -32.248 -79.117 1.00 95.96 ? 127 ARG B CG 1 ATOM 3571 C CD . ARG B 2 127 ? 41.578 -33.330 -79.614 1.00 99.73 ? 127 ARG B CD 1 ATOM 3572 N NE . ARG B 2 127 ? 42.168 -34.184 -80.646 1.00 107.02 ? 127 ARG B NE 1 ATOM 3573 C CZ . ARG B 2 127 ? 41.554 -35.221 -81.224 1.00 113.94 ? 127 ARG B CZ 1 ATOM 3574 N NH1 . ARG B 2 127 ? 40.313 -35.549 -80.876 1.00 116.46 ? 127 ARG B NH1 1 ATOM 3575 N NH2 . ARG B 2 127 ? 42.182 -35.944 -82.154 1.00 117.30 ? 127 ARG B NH2 1 ATOM 3576 N N . ASP B 2 128 ? 43.897 -29.270 -81.957 1.00 95.19 ? 128 ASP B N 1 ATOM 3577 C CA . ASP B 2 128 ? 44.471 -28.408 -83.001 1.00 95.87 ? 128 ASP B CA 1 ATOM 3578 C C . ASP B 2 128 ? 43.420 -27.668 -83.860 1.00 92.29 ? 128 ASP B C 1 ATOM 3579 O O . ASP B 2 128 ? 43.737 -27.169 -84.938 1.00 94.25 ? 128 ASP B O 1 ATOM 3580 C CB . ASP B 2 128 ? 45.441 -29.206 -83.884 1.00 102.27 ? 128 ASP B CB 1 ATOM 3581 C CG . ASP B 2 128 ? 44.772 -30.376 -84.597 1.00 108.48 ? 128 ASP B CG 1 ATOM 3582 O OD1 . ASP B 2 128 ? 43.542 -30.552 -84.455 1.00 107.84 ? 128 ASP B OD1 1 ATOM 3583 O OD2 . ASP B 2 128 ? 45.488 -31.125 -85.300 1.00 115.96 ? 128 ASP B OD2 1 ATOM 3584 N N . ASN B 2 129 ? 42.181 -27.588 -83.376 1.00 88.40 ? 129 ASN B N 1 ATOM 3585 C CA . ASN B 2 129 ? 41.145 -26.782 -84.029 1.00 85.39 ? 129 ASN B CA 1 ATOM 3586 C C . ASN B 2 129 ? 41.121 -25.320 -83.552 1.00 81.27 ? 129 ASN B C 1 ATOM 3587 O O . ASN B 2 129 ? 40.200 -24.572 -83.903 1.00 81.30 ? 129 ASN B O 1 ATOM 3588 C CB . ASN B 2 129 ? 39.758 -27.416 -83.827 1.00 87.63 ? 129 ASN B CB 1 ATOM 3589 C CG . ASN B 2 129 ? 39.585 -28.719 -84.593 1.00 92.50 ? 129 ASN B CG 1 ATOM 3590 O OD1 . ASN B 2 129 ? 40.548 -29.285 -85.106 1.00 97.62 ? 129 ASN B OD1 1 ATOM 3591 N ND2 . ASN B 2 129 ? 38.348 -29.201 -84.670 1.00 92.87 ? 129 ASN B ND2 1 ATOM 3592 N N . ALA B 2 130 ? 42.128 -24.909 -82.773 1.00 77.46 ? 130 ALA B N 1 ATOM 3593 C CA . ALA B 2 130 ? 42.214 -23.532 -82.272 1.00 74.21 ? 130 ALA B CA 1 ATOM 3594 C C . ALA B 2 130 ? 43.639 -23.152 -81.879 1.00 73.84 ? 130 ALA B C 1 ATOM 3595 O O . ALA B 2 130 ? 44.402 -24.012 -81.449 1.00 75.89 ? 130 ALA B O 1 ATOM 3596 C CB . ALA B 2 130 ? 41.295 -23.365 -81.074 1.00 72.80 ? 130 ALA B CB 1 ATOM 3597 N N . LYS B 2 131 ? 43.992 -21.872 -82.018 1.00 72.65 ? 131 LYS B N 1 ATOM 3598 C CA . LYS B 2 131 ? 45.288 -21.373 -81.540 1.00 74.25 ? 131 LYS B CA 1 ATOM 3599 C C . LYS B 2 131 ? 45.266 -21.170 -80.030 1.00 70.21 ? 131 LYS B C 1 ATOM 3600 O O . LYS B 2 131 ? 44.439 -20.420 -79.508 1.00 67.13 ? 131 LYS B O 1 ATOM 3601 C CB . LYS B 2 131 ? 45.657 -20.037 -82.189 1.00 79.96 ? 131 LYS B CB 1 ATOM 3602 C CG . LYS B 2 131 ? 45.917 -20.080 -83.687 1.00 87.56 ? 131 LYS B CG 1 ATOM 3603 C CD . LYS B 2 131 ? 45.945 -18.669 -84.279 1.00 93.26 ? 131 LYS B CD 1 ATOM 3604 C CE . LYS B 2 131 ? 46.612 -18.605 -85.653 1.00 98.51 ? 131 LYS B CE 1 ATOM 3605 N NZ . LYS B 2 131 ? 48.100 -18.769 -85.598 1.00 101.97 ? 131 LYS B NZ 1 ATOM 3606 N N . GLU B 2 132 ? 46.181 -21.827 -79.328 1.00 67.94 ? 132 GLU B N 1 ATOM 3607 C CA . GLU B 2 132 ? 46.379 -21.546 -77.922 1.00 65.24 ? 132 GLU B CA 1 ATOM 3608 C C . GLU B 2 132 ? 47.136 -20.222 -77.821 1.00 65.90 ? 132 GLU B C 1 ATOM 3609 O O . GLU B 2 132 ? 48.305 -20.147 -78.193 1.00 68.68 ? 132 GLU B O 1 ATOM 3610 C CB . GLU B 2 132 ? 47.152 -22.674 -77.263 1.00 66.20 ? 132 GLU B CB 1 ATOM 3611 C CG . GLU B 2 132 ? 47.042 -22.678 -75.752 1.00 64.53 ? 132 GLU B CG 1 ATOM 3612 C CD . GLU B 2 132 ? 47.770 -23.842 -75.099 1.00 66.12 ? 132 GLU B CD 1 ATOM 3613 O OE1 . GLU B 2 132 ? 48.416 -24.642 -75.820 1.00 69.85 ? 132 GLU B OE1 1 ATOM 3614 O OE2 . GLU B 2 132 ? 47.693 -23.952 -73.854 1.00 65.13 ? 132 GLU B OE2 1 ATOM 3615 N N . LEU B 2 133 ? 46.466 -19.178 -77.336 1.00 63.50 ? 133 LEU B N 1 ATOM 3616 C CA . LEU B 2 133 ? 47.032 -17.819 -77.362 1.00 64.54 ? 133 LEU B CA 1 ATOM 3617 C C . LEU B 2 133 ? 48.061 -17.527 -76.269 1.00 66.09 ? 133 LEU B C 1 ATOM 3618 O O . LEU B 2 133 ? 48.840 -16.588 -76.399 1.00 67.75 ? 133 LEU B O 1 ATOM 3619 C CB . LEU B 2 133 ? 45.918 -16.767 -77.297 1.00 63.37 ? 133 LEU B CB 1 ATOM 3620 C CG . LEU B 2 133 ? 45.014 -16.621 -78.526 1.00 63.29 ? 133 LEU B CG 1 ATOM 3621 C CD1 . LEU B 2 133 ? 44.095 -15.426 -78.353 1.00 64.04 ? 133 LEU B CD1 1 ATOM 3622 C CD2 . LEU B 2 133 ? 45.820 -16.467 -79.804 1.00 65.68 ? 133 LEU B CD2 1 ATOM 3623 N N . GLY B 2 134 ? 48.048 -18.310 -75.192 1.00 65.05 ? 134 GLY B N 1 ATOM 3624 C CA . GLY B 2 134 ? 49.010 -18.146 -74.098 1.00 66.16 ? 134 GLY B CA 1 ATOM 3625 C C . GLY B 2 134 ? 48.527 -17.306 -72.923 1.00 64.77 ? 134 GLY B C 1 ATOM 3626 O O . GLY B 2 134 ? 49.304 -17.028 -72.003 1.00 65.55 ? 134 GLY B O 1 ATOM 3627 N N . ASN B 2 135 ? 47.252 -16.916 -72.942 1.00 61.77 ? 135 ASN B N 1 ATOM 3628 C CA . ASN B 2 135 ? 46.692 -16.041 -71.906 1.00 61.41 ? 135 ASN B CA 1 ATOM 3629 C C . ASN B 2 135 ? 45.359 -16.544 -71.342 1.00 58.44 ? 135 ASN B C 1 ATOM 3630 O O . ASN B 2 135 ? 44.604 -15.780 -70.727 1.00 56.83 ? 135 ASN B O 1 ATOM 3631 C CB . ASN B 2 135 ? 46.500 -14.639 -72.476 1.00 64.08 ? 135 ASN B CB 1 ATOM 3632 C CG . ASN B 2 135 ? 45.449 -14.597 -73.563 1.00 63.76 ? 135 ASN B CG 1 ATOM 3633 O OD1 . ASN B 2 135 ? 45.222 -15.582 -74.264 1.00 62.60 ? 135 ASN B OD1 1 ATOM 3634 N ND2 . ASN B 2 135 ? 44.794 -13.459 -73.703 1.00 66.88 ? 135 ASN B ND2 1 ATOM 3635 N N . GLY B 2 136 ? 45.078 -17.827 -71.555 1.00 56.39 ? 136 GLY B N 1 ATOM 3636 C CA . GLY B 2 136 ? 43.815 -18.419 -71.153 1.00 54.17 ? 136 GLY B CA 1 ATOM 3637 C C . GLY B 2 136 ? 42.793 -18.516 -72.271 1.00 53.80 ? 136 GLY B C 1 ATOM 3638 O O . GLY B 2 136 ? 41.733 -19.108 -72.081 1.00 52.52 ? 136 GLY B O 1 ATOM 3639 N N . CYS B 2 137 ? 43.101 -17.952 -73.436 1.00 56.15 ? 137 CYS B N 1 ATOM 3640 C CA . CYS B 2 137 ? 42.131 -17.897 -74.530 1.00 57.31 ? 137 CYS B CA 1 ATOM 3641 C C . CYS B 2 137 ? 42.502 -18.825 -75.673 1.00 56.92 ? 137 CYS B C 1 ATOM 3642 O O . CYS B 2 137 ? 43.670 -19.140 -75.885 1.00 57.09 ? 137 CYS B O 1 ATOM 3643 C CB . CYS B 2 137 ? 41.978 -16.474 -75.058 1.00 59.16 ? 137 CYS B CB 1 ATOM 3644 S SG . CYS B 2 137 ? 41.381 -15.282 -73.840 1.00 62.45 ? 137 CYS B SG 1 ATOM 3645 N N . PHE B 2 138 ? 41.476 -19.254 -76.399 1.00 56.63 ? 138 PHE B N 1 ATOM 3646 C CA . PHE B 2 138 ? 41.632 -20.074 -77.583 1.00 57.62 ? 138 PHE B CA 1 ATOM 3647 C C . PHE B 2 138 ? 40.958 -19.389 -78.764 1.00 59.58 ? 138 PHE B C 1 ATOM 3648 O O . PHE B 2 138 ? 39.777 -19.098 -78.717 1.00 58.16 ? 138 PHE B O 1 ATOM 3649 C CB . PHE B 2 138 ? 40.995 -21.445 -77.369 1.00 56.24 ? 138 PHE B CB 1 ATOM 3650 C CG . PHE B 2 138 ? 41.647 -22.255 -76.291 1.00 55.94 ? 138 PHE B CG 1 ATOM 3651 C CD1 . PHE B 2 138 ? 42.767 -23.032 -76.567 1.00 56.06 ? 138 PHE B CD1 1 ATOM 3652 C CD2 . PHE B 2 138 ? 41.137 -22.253 -74.998 1.00 55.01 ? 138 PHE B CD2 1 ATOM 3653 C CE1 . PHE B 2 138 ? 43.365 -23.792 -75.574 1.00 55.93 ? 138 PHE B CE1 1 ATOM 3654 C CE2 . PHE B 2 138 ? 41.736 -23.010 -74.000 1.00 54.79 ? 138 PHE B CE2 1 ATOM 3655 C CZ . PHE B 2 138 ? 42.854 -23.776 -74.289 1.00 55.13 ? 138 PHE B CZ 1 ATOM 3656 N N . GLU B 2 139 ? 41.713 -19.163 -79.829 1.00 63.75 ? 139 GLU B N 1 ATOM 3657 C CA . GLU B 2 139 ? 41.191 -18.568 -81.042 1.00 67.39 ? 139 GLU B CA 1 ATOM 3658 C C . GLU B 2 139 ? 40.875 -19.676 -82.043 1.00 67.44 ? 139 GLU B C 1 ATOM 3659 O O . GLU B 2 139 ? 41.766 -20.421 -82.446 1.00 70.28 ? 139 GLU B O 1 ATOM 3660 C CB . GLU B 2 139 ? 42.239 -17.624 -81.605 1.00 72.68 ? 139 GLU B CB 1 ATOM 3661 C CG . GLU B 2 139 ? 41.717 -16.586 -82.572 1.00 77.28 ? 139 GLU B CG 1 ATOM 3662 C CD . GLU B 2 139 ? 42.820 -15.636 -82.981 1.00 83.51 ? 139 GLU B CD 1 ATOM 3663 O OE1 . GLU B 2 139 ? 43.828 -16.113 -83.552 1.00 86.20 ? 139 GLU B OE1 1 ATOM 3664 O OE2 . GLU B 2 139 ? 42.700 -14.425 -82.696 1.00 89.21 ? 139 GLU B OE2 1 ATOM 3665 N N . PHE B 2 140 ? 39.612 -19.788 -82.440 1.00 67.10 ? 140 PHE B N 1 ATOM 3666 C CA . PHE B 2 140 ? 39.168 -20.872 -83.323 1.00 68.09 ? 140 PHE B CA 1 ATOM 3667 C C . PHE B 2 140 ? 39.590 -20.652 -84.777 1.00 71.46 ? 140 PHE B C 1 ATOM 3668 O O . PHE B 2 140 ? 39.700 -19.511 -85.230 1.00 70.85 ? 140 PHE B O 1 ATOM 3669 C CB . PHE B 2 140 ? 37.649 -21.006 -83.266 1.00 66.16 ? 140 PHE B CB 1 ATOM 3670 C CG . PHE B 2 140 ? 37.131 -21.439 -81.932 1.00 64.83 ? 140 PHE B CG 1 ATOM 3671 C CD1 . PHE B 2 140 ? 36.824 -20.507 -80.955 1.00 64.13 ? 140 PHE B CD1 1 ATOM 3672 C CD2 . PHE B 2 140 ? 36.942 -22.786 -81.654 1.00 65.35 ? 140 PHE B CD2 1 ATOM 3673 C CE1 . PHE B 2 140 ? 36.338 -20.908 -79.725 1.00 63.77 ? 140 PHE B CE1 1 ATOM 3674 C CE2 . PHE B 2 140 ? 36.458 -23.197 -80.424 1.00 64.91 ? 140 PHE B CE2 1 ATOM 3675 C CZ . PHE B 2 140 ? 36.159 -22.256 -79.457 1.00 64.51 ? 140 PHE B CZ 1 ATOM 3676 N N . TYR B 2 141 ? 39.821 -21.743 -85.508 1.00 75.02 ? 141 TYR B N 1 ATOM 3677 C CA . TYR B 2 141 ? 40.095 -21.649 -86.951 1.00 79.51 ? 141 TYR B CA 1 ATOM 3678 C C . TYR B 2 141 ? 38.797 -21.519 -87.724 1.00 80.20 ? 141 TYR B C 1 ATOM 3679 O O . TYR B 2 141 ? 38.704 -20.734 -88.665 1.00 84.98 ? 141 TYR B O 1 ATOM 3680 C CB . TYR B 2 141 ? 40.903 -22.845 -87.454 1.00 81.07 ? 141 TYR B CB 1 ATOM 3681 C CG . TYR B 2 141 ? 42.287 -22.862 -86.875 1.00 82.84 ? 141 TYR B CG 1 ATOM 3682 C CD1 . TYR B 2 141 ? 43.152 -21.791 -87.076 1.00 84.55 ? 141 TYR B CD1 1 ATOM 3683 C CD2 . TYR B 2 141 ? 42.724 -23.923 -86.088 1.00 84.20 ? 141 TYR B CD2 1 ATOM 3684 C CE1 . TYR B 2 141 ? 44.419 -21.784 -86.526 1.00 86.75 ? 141 TYR B CE1 1 ATOM 3685 C CE2 . TYR B 2 141 ? 43.993 -23.929 -85.535 1.00 85.17 ? 141 TYR B CE2 1 ATOM 3686 C CZ . TYR B 2 141 ? 44.838 -22.856 -85.758 1.00 86.97 ? 141 TYR B CZ 1 ATOM 3687 O OH . TYR B 2 141 ? 46.101 -22.852 -85.211 1.00 88.62 ? 141 TYR B OH 1 ATOM 3688 N N . HIS B 2 142 ? 37.799 -22.293 -87.317 1.00 95.79 ? 142 HIS B N 1 ATOM 3689 C CA . HIS B 2 142 ? 36.448 -22.150 -87.846 1.00 96.95 ? 142 HIS B CA 1 ATOM 3690 C C . HIS B 2 142 ? 35.713 -21.046 -87.102 1.00 92.72 ? 142 HIS B C 1 ATOM 3691 O O . HIS B 2 142 ? 36.135 -20.624 -86.025 1.00 88.12 ? 142 HIS B O 1 ATOM 3692 C CB . HIS B 2 142 ? 35.676 -23.470 -87.727 1.00 99.66 ? 142 HIS B CB 1 ATOM 3693 C CG . HIS B 2 142 ? 35.627 -24.031 -86.338 1.00 95.78 ? 142 HIS B CG 1 ATOM 3694 N ND1 . HIS B 2 142 ? 34.535 -23.878 -85.510 1.00 93.81 ? 142 HIS B ND1 1 ATOM 3695 C CD2 . HIS B 2 142 ? 36.534 -24.752 -85.635 1.00 94.30 ? 142 HIS B CD2 1 ATOM 3696 C CE1 . HIS B 2 142 ? 34.771 -24.482 -84.359 1.00 91.57 ? 142 HIS B CE1 1 ATOM 3697 N NE2 . HIS B 2 142 ? 35.977 -25.019 -84.408 1.00 91.81 ? 142 HIS B NE2 1 ATOM 3698 N N . LYS B 2 143 ? 34.620 -20.566 -87.679 1.00 94.34 ? 143 LYS B N 1 ATOM 3699 C CA . LYS B 2 143 ? 33.711 -19.722 -86.922 1.00 93.08 ? 143 LYS B CA 1 ATOM 3700 C C . LYS B 2 143 ? 33.027 -20.599 -85.887 1.00 90.38 ? 143 LYS B C 1 ATOM 3701 O O . LYS B 2 143 ? 32.804 -21.792 -86.124 1.00 91.71 ? 143 LYS B O 1 ATOM 3702 C CB . LYS B 2 143 ? 32.667 -19.060 -87.806 1.00 97.94 ? 143 LYS B CB 1 ATOM 3703 C CG . LYS B 2 143 ? 33.209 -17.935 -88.668 1.00 102.05 ? 143 LYS B CG 1 ATOM 3704 C CD . LYS B 2 143 ? 32.190 -16.811 -88.837 1.00 105.64 ? 143 LYS B CD 1 ATOM 3705 C CE . LYS B 2 143 ? 30.819 -17.298 -89.302 1.00 110.07 ? 143 LYS B CE 1 ATOM 3706 N NZ . LYS B 2 143 ? 29.776 -17.129 -88.237 1.00 109.15 ? 143 LYS B NZ 1 ATOM 3707 N N . CYS B 2 144 ? 32.708 -20.002 -84.742 1.00 84.94 ? 144 CYS B N 1 ATOM 3708 C CA . CYS B 2 144 ? 32.140 -20.730 -83.622 1.00 81.95 ? 144 CYS B CA 1 ATOM 3709 C C . CYS B 2 144 ? 31.008 -19.904 -83.018 1.00 80.45 ? 144 CYS B C 1 ATOM 3710 O O . CYS B 2 144 ? 31.246 -19.017 -82.199 1.00 77.68 ? 144 CYS B O 1 ATOM 3711 C CB . CYS B 2 144 ? 33.239 -21.020 -82.595 1.00 78.88 ? 144 CYS B CB 1 ATOM 3712 S SG . CYS B 2 144 ? 32.762 -22.078 -81.208 1.00 79.94 ? 144 CYS B SG 1 ATOM 3713 N N . ASP B 2 145 ? 29.779 -20.189 -83.449 1.00 83.31 ? 145 ASP B N 1 ATOM 3714 C CA . ASP B 2 145 ? 28.585 -19.484 -82.952 1.00 83.63 ? 145 ASP B CA 1 ATOM 3715 C C . ASP B 2 145 ? 28.197 -19.988 -81.548 1.00 80.70 ? 145 ASP B C 1 ATOM 3716 O O . ASP B 2 145 ? 28.886 -20.834 -80.983 1.00 79.14 ? 145 ASP B O 1 ATOM 3717 C CB . ASP B 2 145 ? 27.422 -19.603 -83.956 1.00 89.19 ? 145 ASP B CB 1 ATOM 3718 C CG . ASP B 2 145 ? 26.922 -21.032 -84.135 1.00 93.19 ? 145 ASP B CG 1 ATOM 3719 O OD1 . ASP B 2 145 ? 27.489 -21.966 -83.536 1.00 91.87 ? 145 ASP B OD1 1 ATOM 3720 O OD2 . ASP B 2 145 ? 25.948 -21.221 -84.890 1.00 100.09 ? 145 ASP B OD2 1 ATOM 3721 N N . ASN B 2 146 ? 27.103 -19.480 -80.988 1.00 80.79 ? 146 ASN B N 1 ATOM 3722 C CA . ASN B 2 146 ? 26.757 -19.789 -79.595 1.00 79.02 ? 146 ASN B CA 1 ATOM 3723 C C . ASN B 2 146 ? 26.513 -21.271 -79.311 1.00 82.63 ? 146 ASN B C 1 ATOM 3724 O O . ASN B 2 146 ? 26.814 -21.740 -78.217 1.00 81.47 ? 146 ASN B O 1 ATOM 3725 C CB . ASN B 2 146 ? 25.559 -18.956 -79.132 1.00 79.88 ? 146 ASN B CB 1 ATOM 3726 C CG . ASN B 2 146 ? 25.804 -17.461 -79.247 1.00 77.07 ? 146 ASN B CG 1 ATOM 3727 O OD1 . ASN B 2 146 ? 26.940 -16.999 -79.328 1.00 73.01 ? 146 ASN B OD1 1 ATOM 3728 N ND2 . ASN B 2 146 ? 24.732 -16.700 -79.264 1.00 80.05 ? 146 ASN B ND2 1 ATOM 3729 N N . GLU B 2 147 ? 25.986 -22.008 -80.287 1.00 90.49 ? 147 GLU B N 1 ATOM 3730 C CA . GLU B 2 147 ? 25.849 -23.473 -80.159 1.00 96.12 ? 147 GLU B CA 1 ATOM 3731 C C . GLU B 2 147 ? 27.218 -24.143 -80.094 1.00 91.46 ? 147 GLU B C 1 ATOM 3732 O O . GLU B 2 147 ? 27.440 -25.051 -79.290 1.00 91.81 ? 147 GLU B O 1 ATOM 3733 C CB . GLU B 2 147 ? 25.051 -24.078 -81.326 1.00 105.59 ? 147 GLU B CB 1 ATOM 3734 C CG . GLU B 2 147 ? 23.544 -24.065 -81.128 1.00 113.87 ? 147 GLU B CG 1 ATOM 3735 C CD . GLU B 2 147 ? 23.003 -22.663 -80.940 1.00 114.68 ? 147 GLU B CD 1 ATOM 3736 O OE1 . GLU B 2 147 ? 23.372 -21.776 -81.745 1.00 114.26 ? 147 GLU B OE1 1 ATOM 3737 O OE2 . GLU B 2 147 ? 22.230 -22.444 -79.980 1.00 117.11 ? 147 GLU B OE2 1 ATOM 3738 N N . CYS B 2 148 ? 28.121 -23.698 -80.960 1.00 88.05 ? 148 CYS B N 1 ATOM 3739 C CA . CYS B 2 148 ? 29.500 -24.169 -80.954 1.00 85.69 ? 148 CYS B CA 1 ATOM 3740 C C . CYS B 2 148 ? 30.170 -23.850 -79.606 1.00 79.06 ? 148 CYS B C 1 ATOM 3741 O O . CYS B 2 148 ? 30.771 -24.725 -78.977 1.00 78.37 ? 148 CYS B O 1 ATOM 3742 C CB . CYS B 2 148 ? 30.265 -23.539 -82.121 1.00 86.48 ? 148 CYS B CB 1 ATOM 3743 S SG . CYS B 2 148 ? 32.052 -23.782 -82.089 1.00 87.81 ? 148 CYS B SG 1 ATOM 3744 N N . MET B 2 149 ? 30.036 -22.603 -79.159 1.00 73.68 ? 149 MET B N 1 ATOM 3745 C CA . MET B 2 149 ? 30.553 -22.188 -77.857 1.00 68.91 ? 149 MET B CA 1 ATOM 3746 C C . MET B 2 149 ? 29.963 -23.038 -76.743 1.00 70.49 ? 149 MET B C 1 ATOM 3747 O O . MET B 2 149 ? 30.687 -23.536 -75.883 1.00 68.65 ? 149 MET B O 1 ATOM 3748 C CB . MET B 2 149 ? 30.243 -20.713 -77.591 1.00 66.53 ? 149 MET B CB 1 ATOM 3749 C CG . MET B 2 149 ? 30.970 -19.739 -78.507 1.00 65.00 ? 149 MET B CG 1 ATOM 3750 S SD . MET B 2 149 ? 32.768 -19.824 -78.377 1.00 61.82 ? 149 MET B SD 1 ATOM 3751 C CE . MET B 2 149 ? 33.252 -18.552 -79.545 1.00 61.56 ? 149 MET B CE 1 ATOM 3752 N N . GLU B 2 150 ? 28.647 -23.208 -76.762 1.00 75.37 ? 150 GLU B N 1 ATOM 3753 C CA . GLU B 2 150 ? 27.980 -24.017 -75.749 1.00 78.66 ? 150 GLU B CA 1 ATOM 3754 C C . GLU B 2 150 ? 28.527 -25.437 -75.739 1.00 79.92 ? 150 GLU B C 1 ATOM 3755 O O . GLU B 2 150 ? 28.689 -26.020 -74.673 1.00 79.61 ? 150 GLU B O 1 ATOM 3756 C CB . GLU B 2 150 ? 26.458 -24.006 -75.961 1.00 84.68 ? 150 GLU B CB 1 ATOM 3757 C CG . GLU B 2 150 ? 25.642 -24.915 -75.040 1.00 90.07 ? 150 GLU B CG 1 ATOM 3758 C CD . GLU B 2 150 ? 25.759 -24.581 -73.557 1.00 88.77 ? 150 GLU B CD 1 ATOM 3759 O OE1 . GLU B 2 150 ? 26.403 -23.578 -73.187 1.00 85.29 ? 150 GLU B OE1 1 ATOM 3760 O OE2 . GLU B 2 150 ? 25.188 -25.336 -72.745 1.00 93.33 ? 150 GLU B OE2 1 ATOM 3761 N N . SER B 2 151 ? 28.829 -25.978 -76.919 1.00 82.00 ? 151 SER B N 1 ATOM 3762 C CA . SER B 2 151 ? 29.310 -27.357 -77.030 1.00 85.91 ? 151 SER B CA 1 ATOM 3763 C C . SER B 2 151 ? 30.682 -27.532 -76.392 1.00 82.61 ? 151 SER B C 1 ATOM 3764 O O . SER B 2 151 ? 31.026 -28.633 -75.957 1.00 85.95 ? 151 SER B O 1 ATOM 3765 C CB . SER B 2 151 ? 29.357 -27.813 -78.493 1.00 89.43 ? 151 SER B CB 1 ATOM 3766 O OG . SER B 2 151 ? 30.515 -27.332 -79.151 1.00 86.15 ? 151 SER B OG 1 ATOM 3767 N N . VAL B 2 152 ? 31.464 -26.453 -76.350 1.00 77.89 ? 152 VAL B N 1 ATOM 3768 C CA . VAL B 2 152 ? 32.754 -26.457 -75.658 1.00 74.50 ? 152 VAL B CA 1 ATOM 3769 C C . VAL B 2 152 ? 32.551 -26.463 -74.144 1.00 74.68 ? 152 VAL B C 1 ATOM 3770 O O . VAL B 2 152 ? 33.223 -27.205 -73.431 1.00 73.75 ? 152 VAL B O 1 ATOM 3771 C CB . VAL B 2 152 ? 33.618 -25.249 -76.056 1.00 70.67 ? 152 VAL B CB 1 ATOM 3772 C CG1 . VAL B 2 152 ? 34.911 -25.218 -75.248 1.00 69.19 ? 152 VAL B CG1 1 ATOM 3773 C CG2 . VAL B 2 152 ? 33.924 -25.298 -77.544 1.00 71.86 ? 152 VAL B CG2 1 ATOM 3774 N N . ARG B 2 153 ? 31.624 -25.639 -73.661 1.00 75.54 ? 153 ARG B N 1 ATOM 3775 C CA . ARG B 2 153 ? 31.280 -25.630 -72.241 1.00 78.18 ? 153 ARG B CA 1 ATOM 3776 C C . ARG B 2 153 ? 30.641 -26.947 -71.823 1.00 85.37 ? 153 ARG B C 1 ATOM 3777 O O . ARG B 2 153 ? 30.843 -27.393 -70.700 1.00 88.12 ? 153 ARG B O 1 ATOM 3778 C CB . ARG B 2 153 ? 30.321 -24.491 -71.909 1.00 78.55 ? 153 ARG B CB 1 ATOM 3779 C CG . ARG B 2 153 ? 30.827 -23.107 -72.268 1.00 75.05 ? 153 ARG B CG 1 ATOM 3780 C CD . ARG B 2 153 ? 29.871 -22.034 -71.775 1.00 75.50 ? 153 ARG B CD 1 ATOM 3781 N NE . ARG B 2 153 ? 29.897 -20.879 -72.667 1.00 74.98 ? 153 ARG B NE 1 ATOM 3782 C CZ . ARG B 2 153 ? 28.973 -20.582 -73.578 1.00 77.22 ? 153 ARG B CZ 1 ATOM 3783 N NH1 . ARG B 2 153 ? 27.888 -21.334 -73.739 1.00 80.45 ? 153 ARG B NH1 1 ATOM 3784 N NH2 . ARG B 2 153 ? 29.132 -19.502 -74.335 1.00 77.63 ? 153 ARG B NH2 1 ATOM 3785 N N . ASN B 2 154 ? 29.854 -27.542 -72.723 1.00 93.01 ? 154 ASN B N 1 ATOM 3786 C CA . ASN B 2 154 ? 29.271 -28.876 -72.525 1.00 101.04 ? 154 ASN B CA 1 ATOM 3787 C C . ASN B 2 154 ? 30.312 -29.918 -72.160 1.00 99.97 ? 154 ASN B C 1 ATOM 3788 O O . ASN B 2 154 ? 30.189 -30.612 -71.154 1.00 102.98 ? 154 ASN B O 1 ATOM 3789 C CB . ASN B 2 154 ? 28.596 -29.366 -73.812 1.00 110.37 ? 154 ASN B CB 1 ATOM 3790 C CG . ASN B 2 154 ? 27.182 -28.864 -73.977 1.00 121.56 ? 154 ASN B CG 1 ATOM 3791 O OD1 . ASN B 2 154 ? 26.767 -27.903 -73.333 1.00 121.38 ? 154 ASN B OD1 1 ATOM 3792 N ND2 . ASN B 2 154 ? 26.428 -29.524 -74.858 1.00 138.20 ? 154 ASN B ND2 1 ATOM 3793 N N . GLY B 2 155 ? 31.347 -29.999 -72.992 1.00 95.60 ? 155 GLY B N 1 ATOM 3794 C CA . GLY B 2 155 ? 32.230 -31.158 -73.052 1.00 95.77 ? 155 GLY B CA 1 ATOM 3795 C C . GLY B 2 155 ? 32.011 -31.910 -74.354 1.00 98.08 ? 155 GLY B C 1 ATOM 3796 O O . GLY B 2 155 ? 32.726 -32.863 -74.653 1.00 100.20 ? 155 GLY B O 1 ATOM 3797 N N . THR B 2 156 ? 31.039 -31.451 -75.142 1.00 97.80 ? 156 THR B N 1 ATOM 3798 C CA . THR B 2 156 ? 30.573 -32.154 -76.331 1.00 102.34 ? 156 THR B CA 1 ATOM 3799 C C . THR B 2 156 ? 31.188 -31.616 -77.619 1.00 99.40 ? 156 THR B C 1 ATOM 3800 O O . THR B 2 156 ? 30.788 -32.026 -78.704 1.00 103.51 ? 156 THR B O 1 ATOM 3801 C CB . THR B 2 156 ? 29.038 -32.024 -76.447 1.00 106.83 ? 156 THR B CB 1 ATOM 3802 O OG1 . THR B 2 156 ? 28.439 -32.317 -75.181 1.00 108.70 ? 156 THR B OG1 1 ATOM 3803 C CG2 . THR B 2 156 ? 28.463 -32.976 -77.506 1.00 115.69 ? 156 THR B CG2 1 ATOM 3804 N N . TYR B 2 157 ? 32.153 -30.706 -77.517 1.00 94.45 ? 157 TYR B N 1 ATOM 3805 C CA . TYR B 2 157 ? 32.718 -30.082 -78.716 1.00 92.71 ? 157 TYR B CA 1 ATOM 3806 C C . TYR B 2 157 ? 33.133 -31.144 -79.720 1.00 99.28 ? 157 TYR B C 1 ATOM 3807 O O . TYR B 2 157 ? 34.126 -31.846 -79.523 1.00 99.05 ? 157 TYR B O 1 ATOM 3808 C CB . TYR B 2 157 ? 33.918 -29.193 -78.393 1.00 85.51 ? 157 TYR B CB 1 ATOM 3809 C CG . TYR B 2 157 ? 34.586 -28.638 -79.638 1.00 82.91 ? 157 TYR B CG 1 ATOM 3810 C CD1 . TYR B 2 157 ? 33.983 -27.625 -80.386 1.00 81.26 ? 157 TYR B CD1 1 ATOM 3811 C CD2 . TYR B 2 157 ? 35.809 -29.133 -80.074 1.00 82.63 ? 157 TYR B CD2 1 ATOM 3812 C CE1 . TYR B 2 157 ? 34.591 -27.118 -81.525 1.00 80.29 ? 157 TYR B CE1 1 ATOM 3813 C CE2 . TYR B 2 157 ? 36.423 -28.631 -81.211 1.00 81.88 ? 157 TYR B CE2 1 ATOM 3814 C CZ . TYR B 2 157 ? 35.812 -27.627 -81.933 1.00 80.30 ? 157 TYR B CZ 1 ATOM 3815 O OH . TYR B 2 157 ? 36.427 -27.134 -83.058 1.00 79.25 ? 157 TYR B OH 1 ATOM 3816 N N . ASP B 2 158 ? 32.362 -31.249 -80.795 1.00 106.60 ? 158 ASP B N 1 ATOM 3817 C CA . ASP B 2 158 ? 32.572 -32.288 -81.791 1.00 116.19 ? 158 ASP B CA 1 ATOM 3818 C C . ASP B 2 158 ? 33.795 -31.937 -82.634 1.00 116.63 ? 158 ASP B C 1 ATOM 3819 O O . ASP B 2 158 ? 33.699 -31.226 -83.640 1.00 116.66 ? 158 ASP B O 1 ATOM 3820 C CB . ASP B 2 158 ? 31.320 -32.471 -82.659 1.00 121.87 ? 158 ASP B CB 1 ATOM 3821 C CG . ASP B 2 158 ? 31.075 -33.910 -83.011 1.00 129.89 ? 158 ASP B CG 1 ATOM 3822 O OD1 . ASP B 2 158 ? 30.826 -34.706 -82.084 1.00 132.30 ? 158 ASP B OD1 1 ATOM 3823 O OD2 . ASP B 2 158 ? 31.147 -34.252 -84.205 1.00 135.49 ? 158 ASP B OD2 1 ATOM 3824 N N . TYR B 2 159 ? 34.948 -32.430 -82.194 1.00 119.28 ? 159 TYR B N 1 ATOM 3825 C CA . TYR B 2 159 ? 36.224 -32.099 -82.818 1.00 119.76 ? 159 TYR B CA 1 ATOM 3826 C C . TYR B 2 159 ? 36.251 -32.446 -84.311 1.00 126.84 ? 159 TYR B C 1 ATOM 3827 O O . TYR B 2 159 ? 36.588 -31.586 -85.128 1.00 126.55 ? 159 TYR B O 1 ATOM 3828 C CB . TYR B 2 159 ? 37.385 -32.769 -82.065 1.00 120.09 ? 159 TYR B CB 1 ATOM 3829 C CG . TYR B 2 159 ? 38.685 -32.798 -82.833 1.00 121.23 ? 159 TYR B CG 1 ATOM 3830 C CD1 . TYR B 2 159 ? 39.599 -31.757 -82.723 1.00 116.25 ? 159 TYR B CD1 1 ATOM 3831 C CD2 . TYR B 2 159 ? 39.001 -33.868 -83.672 1.00 127.69 ? 159 TYR B CD2 1 ATOM 3832 C CE1 . TYR B 2 159 ? 40.791 -31.778 -83.424 1.00 118.16 ? 159 TYR B CE1 1 ATOM 3833 C CE2 . TYR B 2 159 ? 40.190 -33.896 -84.380 1.00 128.63 ? 159 TYR B CE2 1 ATOM 3834 C CZ . TYR B 2 159 ? 41.082 -32.847 -84.251 1.00 123.82 ? 159 TYR B CZ 1 ATOM 3835 O OH . TYR B 2 159 ? 42.265 -32.867 -84.948 1.00 125.28 ? 159 TYR B OH 1 ATOM 3836 N N . PRO B 2 160 ? 35.889 -33.696 -84.673 1.00 135.96 ? 160 PRO B N 1 ATOM 3837 C CA . PRO B 2 160 ? 35.936 -34.087 -86.094 1.00 143.03 ? 160 PRO B CA 1 ATOM 3838 C C . PRO B 2 160 ? 35.027 -33.248 -87.004 1.00 142.81 ? 160 PRO B C 1 ATOM 3839 O O . PRO B 2 160 ? 35.369 -33.016 -88.167 1.00 145.20 ? 160 PRO B O 1 ATOM 3840 C CB . PRO B 2 160 ? 35.477 -35.556 -86.077 1.00 151.78 ? 160 PRO B CB 1 ATOM 3841 C CG . PRO B 2 160 ? 35.677 -36.015 -84.672 1.00 149.64 ? 160 PRO B CG 1 ATOM 3842 C CD . PRO B 2 160 ? 35.418 -34.806 -83.824 1.00 140.44 ? 160 PRO B CD 1 ATOM 3843 N N . GLN B 2 161 ? 33.889 -32.801 -86.470 1.00 140.39 ? 161 GLN B N 1 ATOM 3844 C CA . GLN B 2 161 ? 32.943 -31.957 -87.211 1.00 139.74 ? 161 GLN B CA 1 ATOM 3845 C C . GLN B 2 161 ? 33.617 -30.686 -87.732 1.00 131.90 ? 161 GLN B C 1 ATOM 3846 O O . GLN B 2 161 ? 33.266 -30.181 -88.799 1.00 133.61 ? 161 GLN B O 1 ATOM 3847 C CB . GLN B 2 161 ? 31.748 -31.583 -86.324 1.00 138.82 ? 161 GLN B CB 1 ATOM 3848 C CG . GLN B 2 161 ? 30.490 -31.198 -87.089 1.00 143.41 ? 161 GLN B CG 1 ATOM 3849 C CD . GLN B 2 161 ? 29.418 -30.619 -86.186 1.00 140.91 ? 161 GLN B CD 1 ATOM 3850 O OE1 . GLN B 2 161 ? 28.367 -31.223 -85.980 1.00 148.00 ? 161 GLN B OE1 1 ATOM 3851 N NE2 . GLN B 2 161 ? 29.683 -29.443 -85.640 1.00 132.23 ? 161 GLN B NE2 1 ATOM 3852 N N . TYR B 2 162 ? 34.577 -30.176 -86.962 1.00 122.45 ? 162 TYR B N 1 ATOM 3853 C CA . TYR B 2 162 ? 35.396 -29.047 -87.372 1.00 116.12 ? 162 TYR B CA 1 ATOM 3854 C C . TYR B 2 162 ? 36.835 -29.521 -87.568 1.00 114.08 ? 162 TYR B C 1 ATOM 3855 O O . TYR B 2 162 ? 37.463 -29.254 -88.589 1.00 112.27 ? 162 TYR B O 1 ATOM 3856 C CB . TYR B 2 162 ? 35.351 -27.946 -86.310 1.00 109.59 ? 162 TYR B CB 1 ATOM 3857 C CG . TYR B 2 162 ? 33.957 -27.532 -85.854 1.00 109.19 ? 162 TYR B CG 1 ATOM 3858 C CD1 . TYR B 2 162 ? 33.192 -26.634 -86.600 1.00 109.86 ? 162 TYR B CD1 1 ATOM 3859 C CD2 . TYR B 2 162 ? 33.417 -28.016 -84.659 1.00 107.89 ? 162 TYR B CD2 1 ATOM 3860 C CE1 . TYR B 2 162 ? 31.925 -26.243 -86.180 1.00 108.89 ? 162 TYR B CE1 1 ATOM 3861 C CE2 . TYR B 2 162 ? 32.152 -27.631 -84.231 1.00 107.11 ? 162 TYR B CE2 1 ATOM 3862 C CZ . TYR B 2 162 ? 31.411 -26.743 -84.993 1.00 107.75 ? 162 TYR B CZ 1 ATOM 3863 O OH . TYR B 2 162 ? 30.156 -26.357 -84.574 1.00 106.83 ? 162 TYR B OH 1 HETATM 3864 C C1 . NAG C 3 . ? 31.070 -3.748 -53.926 1.00 110.27 ? 1322 NAG A C1 1 HETATM 3865 C C2 . NAG C 3 . ? 30.429 -2.517 -53.274 1.00 122.49 ? 1322 NAG A C2 1 HETATM 3866 C C3 . NAG C 3 . ? 28.982 -2.758 -52.822 1.00 128.27 ? 1322 NAG A C3 1 HETATM 3867 C C4 . NAG C 3 . ? 28.152 -3.541 -53.835 1.00 129.52 ? 1322 NAG A C4 1 HETATM 3868 C C5 . NAG C 3 . ? 28.952 -4.728 -54.370 1.00 126.33 ? 1322 NAG A C5 1 HETATM 3869 C C6 . NAG C 3 . ? 28.186 -5.492 -55.449 1.00 124.29 ? 1322 NAG A C6 1 HETATM 3870 C C7 . NAG C 3 . ? 32.142 -1.116 -52.207 1.00 124.17 ? 1322 NAG A C7 1 HETATM 3871 C C8 . NAG C 3 . ? 32.880 -0.774 -50.944 1.00 121.95 ? 1322 NAG A C8 1 HETATM 3872 N N2 . NAG C 3 . ? 31.220 -2.081 -52.131 1.00 123.19 ? 1322 NAG A N2 1 HETATM 3873 O O3 . NAG C 3 . ? 28.342 -1.523 -52.588 1.00 134.04 ? 1322 NAG A O3 1 HETATM 3874 O O4 . NAG C 3 . ? 26.949 -3.970 -53.222 1.00 125.68 ? 1322 NAG A O4 1 HETATM 3875 O O5 . NAG C 3 . ? 30.180 -4.258 -54.903 1.00 118.62 ? 1322 NAG A O5 1 HETATM 3876 O O6 . NAG C 3 . ? 27.993 -6.825 -55.028 1.00 119.77 ? 1322 NAG A O6 1 HETATM 3877 O O7 . NAG C 3 . ? 32.407 -0.509 -53.245 1.00 126.96 ? 1322 NAG A O7 1 HETATM 3878 C C1 . NAG D 3 . ? 49.758 -6.277 -43.139 1.00 79.84 ? 1323 NAG A C1 1 HETATM 3879 C C2 . NAG D 3 . ? 51.087 -5.687 -42.666 1.00 90.84 ? 1323 NAG A C2 1 HETATM 3880 C C3 . NAG D 3 . ? 51.017 -5.076 -41.264 1.00 97.14 ? 1323 NAG A C3 1 HETATM 3881 C C4 . NAG D 3 . ? 49.734 -4.292 -41.028 1.00 99.58 ? 1323 NAG A C4 1 HETATM 3882 C C5 . NAG D 3 . ? 48.553 -5.188 -41.391 1.00 94.67 ? 1323 NAG A C5 1 HETATM 3883 C C6 . NAG D 3 . ? 47.174 -4.603 -41.055 1.00 92.03 ? 1323 NAG A C6 1 HETATM 3884 C C7 . NAG D 3 . ? 53.026 -6.818 -43.690 1.00 94.29 ? 1323 NAG A C7 1 HETATM 3885 C C8 . NAG D 3 . ? 54.036 -7.929 -43.583 1.00 92.49 ? 1323 NAG A C8 1 HETATM 3886 N N2 . NAG D 3 . ? 52.125 -6.713 -42.704 1.00 93.29 ? 1323 NAG A N2 1 HETATM 3887 O O3 . NAG D 3 . ? 52.125 -4.232 -41.040 1.00 98.83 ? 1323 NAG A O3 1 HETATM 3888 O O4 . NAG D 3 . ? 49.725 -3.921 -39.664 1.00 116.34 ? 1323 NAG A O4 1 HETATM 3889 O O5 . NAG D 3 . ? 48.649 -5.474 -42.772 1.00 84.07 ? 1323 NAG A O5 1 HETATM 3890 O O6 . NAG D 3 . ? 46.769 -3.667 -42.028 1.00 91.10 ? 1323 NAG A O6 1 HETATM 3891 O O7 . NAG D 3 . ? 53.065 -6.064 -44.664 1.00 96.64 ? 1323 NAG A O7 1 HETATM 3892 C C1 . NAG E 3 . ? 49.442 -2.517 -39.478 1.00 131.44 ? 1324 NAG A C1 1 HETATM 3893 C C2 . NAG E 3 . ? 49.236 -2.257 -37.980 1.00 133.44 ? 1324 NAG A C2 1 HETATM 3894 C C3 . NAG E 3 . ? 49.243 -0.766 -37.609 1.00 137.95 ? 1324 NAG A C3 1 HETATM 3895 C C4 . NAG E 3 . ? 50.261 0.042 -38.414 1.00 138.56 ? 1324 NAG A C4 1 HETATM 3896 C C5 . NAG E 3 . ? 50.134 -0.315 -39.891 1.00 137.21 ? 1324 NAG A C5 1 HETATM 3897 C C6 . NAG E 3 . ? 51.051 0.509 -40.788 1.00 134.68 ? 1324 NAG A C6 1 HETATM 3898 C C7 . NAG E 3 . ? 47.926 -4.137 -37.073 1.00 123.73 ? 1324 NAG A C7 1 HETATM 3899 C C8 . NAG E 3 . ? 46.577 -4.643 -36.651 1.00 122.59 ? 1324 NAG A C8 1 HETATM 3900 N N2 . NAG E 3 . ? 47.992 -2.881 -37.534 1.00 130.00 ? 1324 NAG A N2 1 HETATM 3901 O O3 . NAG E 3 . ? 49.522 -0.623 -36.232 1.00 138.04 ? 1324 NAG A O3 1 HETATM 3902 O O4 . NAG E 3 . ? 50.040 1.423 -38.224 1.00 139.75 ? 1324 NAG A O4 1 HETATM 3903 O O5 . NAG E 3 . ? 50.460 -1.684 -40.002 1.00 136.14 ? 1324 NAG A O5 1 HETATM 3904 O O6 . NAG E 3 . ? 52.382 0.374 -40.347 1.00 136.60 ? 1324 NAG A O6 1 HETATM 3905 O O7 . NAG E 3 . ? 48.899 -4.884 -36.981 1.00 120.20 ? 1324 NAG A O7 1 HETATM 3906 C C1 . NAG F 3 . ? 21.646 -39.755 14.029 1.00 84.58 ? 1325 NAG A C1 1 HETATM 3907 C C2 . NAG F 3 . ? 22.656 -40.858 14.334 1.00 89.00 ? 1325 NAG A C2 1 HETATM 3908 C C3 . NAG F 3 . ? 22.342 -42.078 13.496 1.00 92.20 ? 1325 NAG A C3 1 HETATM 3909 C C4 . NAG F 3 . ? 20.923 -42.518 13.803 1.00 99.28 ? 1325 NAG A C4 1 HETATM 3910 C C5 . NAG F 3 . ? 19.929 -41.396 13.498 1.00 97.90 ? 1325 NAG A C5 1 HETATM 3911 C C6 . NAG F 3 . ? 18.507 -41.733 13.961 1.00 101.89 ? 1325 NAG A C6 1 HETATM 3912 C C7 . NAG F 3 . ? 25.074 -40.999 14.677 1.00 97.24 ? 1325 NAG A C7 1 HETATM 3913 C C8 . NAG F 3 . ? 26.446 -40.475 14.361 1.00 96.71 ? 1325 NAG A C8 1 HETATM 3914 N N2 . NAG F 3 . ? 24.018 -40.414 14.092 1.00 92.42 ? 1325 NAG A N2 1 HETATM 3915 O O3 . NAG F 3 . ? 23.230 -43.137 13.772 1.00 91.57 ? 1325 NAG A O3 1 HETATM 3916 O O4 . NAG F 3 . ? 20.692 -43.637 12.988 1.00 112.06 ? 1325 NAG A O4 1 HETATM 3917 O O5 . NAG F 3 . ? 20.315 -40.213 14.164 1.00 90.84 ? 1325 NAG A O5 1 HETATM 3918 O O6 . NAG F 3 . ? 17.720 -40.583 14.216 1.00 101.55 ? 1325 NAG A O6 1 HETATM 3919 O O7 . NAG F 3 . ? 24.975 -41.944 15.455 1.00 100.24 ? 1325 NAG A O7 1 HETATM 3920 C C1 . NAG G 3 . ? 19.931 -44.649 13.660 1.00 125.23 ? 1326 NAG A C1 1 HETATM 3921 C C2 . NAG G 3 . ? 19.391 -45.551 12.574 1.00 129.54 ? 1326 NAG A C2 1 HETATM 3922 C C3 . NAG G 3 . ? 18.501 -46.616 13.181 1.00 139.36 ? 1326 NAG A C3 1 HETATM 3923 C C4 . NAG G 3 . ? 19.158 -47.317 14.382 1.00 146.18 ? 1326 NAG A C4 1 HETATM 3924 C C5 . NAG G 3 . ? 19.839 -46.309 15.314 1.00 139.70 ? 1326 NAG A C5 1 HETATM 3925 C C6 . NAG G 3 . ? 20.662 -47.011 16.392 1.00 138.29 ? 1326 NAG A C6 1 HETATM 3926 C C7 . NAG G 3 . ? 19.131 -44.429 10.400 1.00 126.31 ? 1326 NAG A C7 1 HETATM 3927 C C8 . NAG G 3 . ? 18.227 -43.633 9.503 1.00 123.35 ? 1326 NAG A C8 1 HETATM 3928 N N2 . NAG G 3 . ? 18.639 -44.781 11.593 1.00 129.34 ? 1326 NAG A N2 1 HETATM 3929 O O3 . NAG G 3 . ? 18.253 -47.499 12.117 1.00 143.39 ? 1326 NAG A O3 1 HETATM 3930 O O4 . NAG G 3 . ? 18.218 -48.037 15.168 1.00 157.42 ? 1326 NAG A O4 1 HETATM 3931 O O5 . NAG G 3 . ? 20.668 -45.429 14.577 1.00 131.78 ? 1326 NAG A O5 1 HETATM 3932 O O6 . NAG G 3 . ? 21.324 -46.042 17.173 1.00 133.59 ? 1326 NAG A O6 1 HETATM 3933 O O7 . NAG G 3 . ? 20.263 -44.718 10.011 1.00 121.55 ? 1326 NAG A O7 1 HETATM 3934 C C1 . MAN H 4 . ? 17.600 -49.173 14.521 1.00 166.49 ? 1327 MAN A C1 1 HETATM 3935 C C2 . MAN H 4 . ? 17.861 -50.427 15.348 1.00 166.21 ? 1327 MAN A C2 1 HETATM 3936 C C3 . MAN H 4 . ? 17.803 -51.668 14.456 1.00 169.50 ? 1327 MAN A C3 1 HETATM 3937 C C4 . MAN H 4 . ? 16.784 -51.480 13.330 1.00 175.28 ? 1327 MAN A C4 1 HETATM 3938 C C5 . MAN H 4 . ? 17.234 -50.333 12.429 1.00 177.37 ? 1327 MAN A C5 1 HETATM 3939 C C6 . MAN H 4 . ? 16.046 -49.604 11.791 1.00 177.74 ? 1327 MAN A C6 1 HETATM 3940 O O2 . MAN H 4 . ? 16.898 -50.507 16.407 1.00 161.02 ? 1327 MAN A O2 1 HETATM 3941 O O3 . MAN H 4 . ? 17.475 -52.824 15.237 1.00 164.89 ? 1327 MAN A O3 1 HETATM 3942 O O4 . MAN H 4 . ? 16.635 -52.666 12.541 1.00 175.07 ? 1327 MAN A O4 1 HETATM 3943 O O5 . MAN H 4 . ? 18.035 -49.414 13.179 1.00 175.00 ? 1327 MAN A O5 1 HETATM 3944 O O6 . MAN H 4 . ? 15.369 -50.408 10.808 1.00 179.80 ? 1327 MAN A O6 1 HETATM 3945 C C1 . BMA I 5 . ? 18.205 -53.973 14.768 1.00 155.44 ? 1328 BMA A C1 1 HETATM 3946 C C2 . BMA I 5 . ? 19.550 -54.055 15.486 1.00 151.36 ? 1328 BMA A C2 1 HETATM 3947 C C3 . BMA I 5 . ? 20.324 -55.263 14.973 1.00 145.49 ? 1328 BMA A C3 1 HETATM 3948 C C4 . BMA I 5 . ? 19.445 -56.508 15.040 1.00 146.89 ? 1328 BMA A C4 1 HETATM 3949 C C5 . BMA I 5 . ? 18.080 -56.293 14.374 1.00 147.31 ? 1328 BMA A C5 1 HETATM 3950 C C6 . BMA I 5 . ? 17.154 -57.506 14.512 1.00 143.97 ? 1328 BMA A C6 1 HETATM 3951 O O2 . BMA I 5 . ? 19.354 -54.139 16.882 1.00 148.95 ? 1328 BMA A O2 1 HETATM 3952 O O3 . BMA I 5 . ? 21.485 -55.462 15.746 1.00 140.39 ? 1328 BMA A O3 1 HETATM 3953 O O4 . BMA I 5 . ? 20.134 -57.606 14.473 1.00 139.24 ? 1328 BMA A O4 1 HETATM 3954 O O5 . BMA I 5 . ? 17.465 -55.160 14.958 1.00 151.31 ? 1328 BMA A O5 1 HETATM 3955 O O6 . BMA I 5 . ? 16.165 -57.289 15.496 1.00 137.58 ? 1328 BMA A O6 1 HETATM 3956 C C1 . MAN J 4 . ? 16.153 -50.854 9.671 1.00 176.42 ? 1329 MAN A C1 1 HETATM 3957 C C2 . MAN J 4 . ? 16.970 -49.751 8.996 1.00 172.70 ? 1329 MAN A C2 1 HETATM 3958 C C3 . MAN J 4 . ? 16.034 -48.686 8.436 1.00 168.24 ? 1329 MAN A C3 1 HETATM 3959 C C4 . MAN J 4 . ? 14.994 -49.317 7.516 1.00 168.82 ? 1329 MAN A C4 1 HETATM 3960 C C5 . MAN J 4 . ? 14.329 -50.523 8.185 1.00 170.35 ? 1329 MAN A C5 1 HETATM 3961 C C6 . MAN J 4 . ? 13.448 -51.316 7.227 1.00 165.34 ? 1329 MAN A C6 1 HETATM 3962 O O2 . MAN J 4 . ? 17.713 -50.318 7.939 1.00 166.57 ? 1329 MAN A O2 1 HETATM 3963 O O3 . MAN J 4 . ? 16.770 -47.714 7.729 1.00 164.10 ? 1329 MAN A O3 1 HETATM 3964 O O4 . MAN J 4 . ? 14.023 -48.344 7.204 1.00 163.98 ? 1329 MAN A O4 1 HETATM 3965 O O5 . MAN J 4 . ? 15.309 -51.414 8.688 1.00 178.76 ? 1329 MAN A O5 1 HETATM 3966 O O6 . MAN J 4 . ? 12.941 -50.494 6.201 1.00 159.12 ? 1329 MAN A O6 1 HETATM 3967 C C1 . NAG K 3 . ? 23.004 -12.231 -30.041 1.00 113.12 ? 1330 NAG A C1 1 HETATM 3968 C C2 . NAG K 3 . ? 21.649 -11.870 -29.405 1.00 123.89 ? 1330 NAG A C2 1 HETATM 3969 C C3 . NAG K 3 . ? 20.509 -11.734 -30.417 1.00 127.91 ? 1330 NAG A C3 1 HETATM 3970 C C4 . NAG K 3 . ? 20.958 -10.933 -31.638 1.00 131.15 ? 1330 NAG A C4 1 HETATM 3971 C C5 . NAG K 3 . ? 22.210 -11.588 -32.222 1.00 129.30 ? 1330 NAG A C5 1 HETATM 3972 C C6 . NAG K 3 . ? 22.688 -10.912 -33.507 1.00 127.53 ? 1330 NAG A C6 1 HETATM 3973 C C7 . NAG K 3 . ? 21.178 -12.511 -27.071 1.00 119.74 ? 1330 NAG A C7 1 HETATM 3974 C C8 . NAG K 3 . ? 20.787 -13.604 -26.118 1.00 115.50 ? 1330 NAG A C8 1 HETATM 3975 N N2 . NAG K 3 . ? 21.276 -12.831 -28.367 1.00 122.28 ? 1330 NAG A N2 1 HETATM 3976 O O3 . NAG K 3 . ? 19.413 -11.106 -29.788 1.00 126.20 ? 1330 NAG A O3 1 HETATM 3977 O O4 . NAG K 3 . ? 19.923 -10.871 -32.600 1.00 135.37 ? 1330 NAG A O4 1 HETATM 3978 O O5 . NAG K 3 . ? 23.238 -11.524 -31.254 1.00 121.63 ? 1330 NAG A O5 1 HETATM 3979 O O6 . NAG K 3 . ? 23.831 -11.580 -33.997 1.00 124.70 ? 1330 NAG A O6 1 HETATM 3980 O O7 . NAG K 3 . ? 21.396 -11.383 -26.630 1.00 120.22 ? 1330 NAG A O7 1 HETATM 3981 S S1 . MPO L 6 . ? 36.165 -4.816 21.840 1.00 117.84 ? 1331 MPO A S1 1 HETATM 3982 O O1 . MPO L 6 . ? 36.379 -5.760 20.779 1.00 120.61 ? 1331 MPO A O1 1 HETATM 3983 O O2 . MPO L 6 . ? 34.763 -4.733 22.144 1.00 117.38 ? 1331 MPO A O2 1 HETATM 3984 O O4 . MPO L 6 . ? 32.500 -9.441 25.480 1.00 114.29 ? 1331 MPO A O4 1 HETATM 3985 N N1 . MPO L 6 . ? 34.285 -7.489 24.442 1.00 113.79 ? 1331 MPO A N1 1 HETATM 3986 C C1 . MPO L 6 . ? 37.009 -5.331 23.178 1.00 117.91 ? 1331 MPO A C1 1 HETATM 3987 O O3 . MPO L 6 . ? 36.700 -3.338 21.384 1.00 108.27 ? 1331 MPO A O3 1 HETATM 3988 C C2 . MPO L 6 . ? 36.481 -6.680 23.662 1.00 115.35 ? 1331 MPO A C2 1 HETATM 3989 C C3 . MPO L 6 . ? 35.370 -6.526 24.697 1.00 113.16 ? 1331 MPO A C3 1 HETATM 3990 C C4 . MPO L 6 . ? 33.120 -7.109 25.261 1.00 115.19 ? 1331 MPO A C4 1 HETATM 3991 C C5 . MPO L 6 . ? 32.004 -8.143 25.147 1.00 114.36 ? 1331 MPO A C5 1 HETATM 3992 C C6 . MPO L 6 . ? 33.562 -9.836 24.615 1.00 113.66 ? 1331 MPO A C6 1 HETATM 3993 C C7 . MPO L 6 . ? 34.722 -8.859 24.772 1.00 113.89 ? 1331 MPO A C7 1 HETATM 3994 C C1 . NAG M 3 . ? 25.052 -29.206 -75.156 1.00 96.16 ? 1163 NAG B C1 1 HETATM 3995 C C2 . NAG M 3 . ? 24.046 -30.364 -75.313 1.00 106.06 ? 1163 NAG B C2 1 HETATM 3996 C C3 . NAG M 3 . ? 23.562 -30.643 -76.742 1.00 112.94 ? 1163 NAG B C3 1 HETATM 3997 C C4 . NAG M 3 . ? 23.566 -29.402 -77.619 1.00 118.15 ? 1163 NAG B C4 1 HETATM 3998 C C5 . NAG M 3 . ? 24.928 -28.734 -77.486 1.00 111.32 ? 1163 NAG B C5 1 HETATM 3999 C C6 . NAG M 3 . ? 25.157 -27.616 -78.502 1.00 109.93 ? 1163 NAG B C6 1 HETATM 4000 C C7 . NAG M 3 . ? 24.734 -31.798 -73.441 1.00 107.18 ? 1163 NAG B C7 1 HETATM 4001 C C8 . NAG M 3 . ? 25.296 -33.124 -73.008 1.00 104.67 ? 1163 NAG B C8 1 HETATM 4002 N N2 . NAG M 3 . ? 24.581 -31.602 -74.754 1.00 106.05 ? 1163 NAG B N2 1 HETATM 4003 O O3 . NAG M 3 . ? 22.259 -31.186 -76.707 1.00 113.87 ? 1163 NAG B O3 1 HETATM 4004 O O4 . NAG M 3 . ? 23.234 -29.751 -78.955 1.00 127.76 ? 1163 NAG B O4 1 HETATM 4005 O O5 . NAG M 3 . ? 24.972 -28.220 -76.172 1.00 102.65 ? 1163 NAG B O5 1 HETATM 4006 O O6 . NAG M 3 . ? 24.209 -26.587 -78.323 1.00 107.75 ? 1163 NAG B O6 1 HETATM 4007 O O7 . NAG M 3 . ? 24.443 -30.952 -72.595 1.00 105.80 ? 1163 NAG B O7 1 HETATM 4008 C C1 . NAG N 3 . ? 22.025 -29.080 -79.380 1.00 133.90 ? 1164 NAG B C1 1 HETATM 4009 C C2 . NAG N 3 . ? 21.718 -29.481 -80.825 1.00 135.86 ? 1164 NAG B C2 1 HETATM 4010 C C3 . NAG N 3 . ? 20.306 -29.078 -81.277 1.00 141.32 ? 1164 NAG B C3 1 HETATM 4011 C C4 . NAG N 3 . ? 19.240 -29.277 -80.194 1.00 145.19 ? 1164 NAG B C4 1 HETATM 4012 C C5 . NAG N 3 . ? 19.748 -28.671 -78.886 1.00 139.26 ? 1164 NAG B C5 1 HETATM 4013 C C6 . NAG N 3 . ? 18.743 -28.756 -77.739 1.00 133.90 ? 1164 NAG B C6 1 HETATM 4014 C C7 . NAG N 3 . ? 23.921 -29.438 -81.920 1.00 129.21 ? 1164 NAG B C7 1 HETATM 4015 C C8 . NAG N 3 . ? 24.831 -28.740 -82.891 1.00 126.75 ? 1164 NAG B C8 1 HETATM 4016 N N2 . NAG N 3 . ? 22.707 -28.910 -81.733 1.00 133.62 ? 1164 NAG B N2 1 HETATM 4017 O O3 . NAG N 3 . ? 19.968 -29.804 -82.439 1.00 138.72 ? 1164 NAG B O3 1 HETATM 4018 O O4 . NAG N 3 . ? 18.000 -28.698 -80.584 1.00 155.75 ? 1164 NAG B O4 1 HETATM 4019 O O5 . NAG N 3 . ? 20.925 -29.369 -78.535 1.00 136.56 ? 1164 NAG B O5 1 HETATM 4020 O O6 . NAG N 3 . ? 18.548 -30.102 -77.372 1.00 127.74 ? 1164 NAG B O6 1 HETATM 4021 O O7 . NAG N 3 . ? 24.314 -30.448 -81.338 1.00 127.78 ? 1164 NAG B O7 1 HETATM 4022 C C1 . BMA O 5 . ? 17.119 -29.618 -81.279 1.00 162.12 ? 1165 BMA B C1 1 HETATM 4023 C C2 . BMA O 5 . ? 15.704 -29.506 -80.719 1.00 162.21 ? 1165 BMA B C2 1 HETATM 4024 C C3 . BMA O 5 . ? 14.774 -30.513 -81.393 1.00 160.67 ? 1165 BMA B C3 1 HETATM 4025 C C4 . BMA O 5 . ? 14.890 -30.463 -82.916 1.00 158.59 ? 1165 BMA B C4 1 HETATM 4026 C C5 . BMA O 5 . ? 16.340 -30.412 -83.396 1.00 158.55 ? 1165 BMA B C5 1 HETATM 4027 C C6 . BMA O 5 . ? 16.391 -30.153 -84.900 1.00 156.96 ? 1165 BMA B C6 1 HETATM 4028 O O2 . BMA O 5 . ? 15.205 -28.178 -80.922 1.00 159.96 ? 1165 BMA B O2 1 HETATM 4029 O O3 . BMA O 5 . ? 13.417 -30.252 -81.012 1.00 158.64 ? 1165 BMA B O3 1 HETATM 4030 O O4 . BMA O 5 . ? 14.260 -31.625 -83.465 1.00 155.01 ? 1165 BMA B O4 1 HETATM 4031 O O5 . BMA O 5 . ? 17.064 -29.395 -82.692 1.00 163.16 ? 1165 BMA B O5 1 HETATM 4032 O O6 . BMA O 5 . ? 17.746 -29.987 -85.340 1.00 154.16 ? 1165 BMA B O6 1 HETATM 4033 S S1 . MPO P 6 . ? 38.526 -11.035 -71.297 1.00 116.17 ? 1166 MPO B S1 1 HETATM 4034 O O1 . MPO P 6 . ? 39.487 -10.451 -70.396 1.00 122.33 ? 1166 MPO B O1 1 HETATM 4035 O O2 . MPO P 6 . ? 37.996 -9.990 -72.133 1.00 119.66 ? 1166 MPO B O2 1 HETATM 4036 O O4 . MPO P 6 . ? 44.300 -10.519 -72.983 1.00 103.93 ? 1166 MPO B O4 1 HETATM 4037 N N1 . MPO P 6 . ? 41.988 -10.895 -71.613 1.00 104.58 ? 1166 MPO B N1 1 HETATM 4038 C C1 . MPO P 6 . ? 39.243 -12.219 -72.219 1.00 102.89 ? 1166 MPO B C1 1 HETATM 4039 O O3 . MPO P 6 . ? 37.290 -11.695 -70.455 1.00 115.31 ? 1166 MPO B O3 1 HETATM 4040 C C2 . MPO P 6 . ? 40.467 -12.812 -71.525 1.00 98.94 ? 1166 MPO B C2 1 HETATM 4041 C C3 . MPO P 6 . ? 41.773 -12.275 -72.099 1.00 99.69 ? 1166 MPO B C3 1 HETATM 4042 C C4 . MPO P 6 . ? 41.941 -9.912 -72.724 1.00 109.08 ? 1166 MPO B C4 1 HETATM 4043 C C5 . MPO P 6 . ? 43.155 -9.993 -73.654 1.00 107.72 ? 1166 MPO B C5 1 HETATM 4044 C C6 . MPO P 6 . ? 44.373 -10.136 -71.611 1.00 103.97 ? 1166 MPO B C6 1 HETATM 4045 C C7 . MPO P 6 . ? 43.227 -10.756 -70.811 1.00 104.72 ? 1166 MPO B C7 1 HETATM 4046 O O . HOH Q 7 . ? 38.834 -13.895 -82.220 1.00 65.40 ? 2001 HOH A O 1 HETATM 4047 O O . HOH Q 7 . ? 37.687 -17.737 -85.219 1.00 66.03 ? 2002 HOH A O 1 HETATM 4048 O O . HOH Q 7 . ? 34.565 -12.076 -83.470 1.00 74.51 ? 2003 HOH A O 1 HETATM 4049 O O . HOH Q 7 . ? 36.112 -13.927 -75.617 1.00 60.39 ? 2004 HOH A O 1 HETATM 4050 O O . HOH Q 7 . ? 42.772 -13.118 -76.332 1.00 66.78 ? 2005 HOH A O 1 HETATM 4051 O O . HOH Q 7 . ? 30.777 -17.748 -56.125 1.00 51.72 ? 2006 HOH A O 1 HETATM 4052 O O . HOH Q 7 . ? 41.441 -15.621 -69.965 1.00 53.87 ? 2007 HOH A O 1 HETATM 4053 O O . HOH Q 7 . ? 39.960 -14.328 -65.435 1.00 44.58 ? 2008 HOH A O 1 HETATM 4054 O O . HOH Q 7 . ? 44.036 -12.858 -59.348 1.00 62.21 ? 2009 HOH A O 1 HETATM 4055 O O . HOH Q 7 . ? 40.343 -12.498 -58.752 1.00 46.43 ? 2010 HOH A O 1 HETATM 4056 O O . HOH Q 7 . ? 31.019 -15.357 -56.446 1.00 74.85 ? 2011 HOH A O 1 HETATM 4057 O O . HOH Q 7 . ? 31.266 -11.518 -54.698 1.00 62.15 ? 2012 HOH A O 1 HETATM 4058 O O . HOH Q 7 . ? 32.247 -9.560 -59.520 1.00 65.75 ? 2013 HOH A O 1 HETATM 4059 O O . HOH Q 7 . ? 32.296 -6.596 -56.049 1.00 55.32 ? 2014 HOH A O 1 HETATM 4060 O O . HOH Q 7 . ? 32.837 -2.277 -57.315 1.00 68.14 ? 2015 HOH A O 1 HETATM 4061 O O . HOH Q 7 . ? 35.467 -6.725 -33.623 1.00 65.62 ? 2016 HOH A O 1 HETATM 4062 O O . HOH Q 7 . ? 34.191 -10.493 -49.605 1.00 65.09 ? 2017 HOH A O 1 HETATM 4063 O O . HOH Q 7 . ? 36.135 -6.081 -48.590 1.00 64.98 ? 2018 HOH A O 1 HETATM 4064 O O . HOH Q 7 . ? 42.896 -5.393 -49.386 1.00 79.45 ? 2019 HOH A O 1 HETATM 4065 O O . HOH Q 7 . ? 40.982 -7.823 -43.953 1.00 72.77 ? 2020 HOH A O 1 HETATM 4066 O O . HOH Q 7 . ? 47.448 -4.301 -45.195 1.00 71.31 ? 2021 HOH A O 1 HETATM 4067 O O . HOH Q 7 . ? 46.265 -10.422 -43.753 1.00 67.38 ? 2022 HOH A O 1 HETATM 4068 O O . HOH Q 7 . ? 44.819 -14.864 -42.272 1.00 44.94 ? 2023 HOH A O 1 HETATM 4069 O O . HOH Q 7 . ? 49.618 -9.627 -41.169 1.00 55.38 ? 2024 HOH A O 1 HETATM 4070 O O . HOH Q 7 . ? 46.492 -12.692 -39.442 1.00 55.78 ? 2025 HOH A O 1 HETATM 4071 O O . HOH Q 7 . ? 51.274 -18.562 -50.378 1.00 58.12 ? 2026 HOH A O 1 HETATM 4072 O O . HOH Q 7 . ? 52.494 -16.669 -51.936 1.00 55.79 ? 2027 HOH A O 1 HETATM 4073 O O . HOH Q 7 . ? 54.128 -11.047 -47.143 1.00 75.03 ? 2028 HOH A O 1 HETATM 4074 O O . HOH Q 7 . ? 49.564 -4.973 -47.173 1.00 74.30 ? 2029 HOH A O 1 HETATM 4075 O O . HOH Q 7 . ? 18.337 -18.307 8.917 1.00 64.62 ? 2030 HOH A O 1 HETATM 4076 O O . HOH Q 7 . ? 18.201 -15.836 9.174 1.00 64.76 ? 2031 HOH A O 1 HETATM 4077 O O . HOH Q 7 . ? 45.072 -5.796 -54.329 1.00 76.52 ? 2032 HOH A O 1 HETATM 4078 O O . HOH Q 7 . ? 31.655 -17.509 -50.699 1.00 61.35 ? 2033 HOH A O 1 HETATM 4079 O O . HOH Q 7 . ? 34.291 -11.957 -47.283 1.00 49.30 ? 2034 HOH A O 1 HETATM 4080 O O . HOH Q 7 . ? 33.002 -17.404 -46.009 1.00 68.15 ? 2035 HOH A O 1 HETATM 4081 O O . HOH Q 7 . ? 32.186 -14.621 -44.124 1.00 75.87 ? 2036 HOH A O 1 HETATM 4082 O O . HOH Q 7 . ? 33.799 -13.123 -41.760 1.00 57.57 ? 2037 HOH A O 1 HETATM 4083 O O . HOH Q 7 . ? 40.035 -12.238 -36.670 1.00 46.32 ? 2038 HOH A O 1 HETATM 4084 O O . HOH Q 7 . ? 34.708 -10.007 -33.571 1.00 69.25 ? 2039 HOH A O 1 HETATM 4085 O O . HOH Q 7 . ? 47.853 -28.429 -1.120 1.00 61.90 ? 2040 HOH A O 1 HETATM 4086 O O . HOH Q 7 . ? 39.572 -8.791 -28.050 1.00 69.51 ? 2041 HOH A O 1 HETATM 4087 O O . HOH Q 7 . ? 40.045 -9.595 -37.932 1.00 66.30 ? 2042 HOH A O 1 HETATM 4088 O O . HOH Q 7 . ? 30.399 -11.415 -28.130 1.00 54.47 ? 2043 HOH A O 1 HETATM 4089 O O . HOH Q 7 . ? 32.452 -3.392 -24.302 1.00 70.65 ? 2044 HOH A O 1 HETATM 4090 O O . HOH Q 7 . ? 24.474 -6.605 -24.527 1.00 65.76 ? 2045 HOH A O 1 HETATM 4091 O O . HOH Q 7 . ? 29.351 -3.657 -16.454 1.00 66.11 ? 2046 HOH A O 1 HETATM 4092 O O . HOH Q 7 . ? 33.130 -3.272 -18.739 1.00 63.33 ? 2047 HOH A O 1 HETATM 4093 O O . HOH Q 7 . ? 17.270 -11.775 -12.989 1.00 73.23 ? 2048 HOH A O 1 HETATM 4094 O O . HOH Q 7 . ? 22.655 -21.152 -16.012 1.00 73.82 ? 2049 HOH A O 1 HETATM 4095 O O . HOH Q 7 . ? 21.369 -15.921 -7.883 1.00 70.52 ? 2050 HOH A O 1 HETATM 4096 O O . HOH Q 7 . ? 19.315 -9.268 9.910 1.00 56.90 ? 2051 HOH A O 1 HETATM 4097 O O . HOH Q 7 . ? 17.675 -11.522 8.807 1.00 71.46 ? 2052 HOH A O 1 HETATM 4098 O O . HOH Q 7 . ? 24.945 -8.146 -5.064 1.00 72.94 ? 2053 HOH A O 1 HETATM 4099 O O . HOH Q 7 . ? 28.811 -5.928 -0.240 1.00 73.44 ? 2054 HOH A O 1 HETATM 4100 O O . HOH Q 7 . ? 31.419 -8.779 -6.526 1.00 64.39 ? 2055 HOH A O 1 HETATM 4101 O O . HOH Q 7 . ? 35.296 -4.394 -1.590 1.00 69.03 ? 2056 HOH A O 1 HETATM 4102 O O . HOH Q 7 . ? 25.394 -13.754 5.764 1.00 60.64 ? 2057 HOH A O 1 HETATM 4103 O O . HOH Q 7 . ? 33.847 -6.033 7.992 1.00 74.24 ? 2058 HOH A O 1 HETATM 4104 O O . HOH Q 7 . ? 25.340 -6.779 3.075 1.00 67.54 ? 2059 HOH A O 1 HETATM 4105 O O . HOH Q 7 . ? 20.717 -5.782 7.784 1.00 65.76 ? 2060 HOH A O 1 HETATM 4106 O O . HOH Q 7 . ? 26.020 -5.595 0.601 1.00 62.79 ? 2061 HOH A O 1 HETATM 4107 O O . HOH Q 7 . ? 16.905 -16.335 -0.974 1.00 78.33 ? 2062 HOH A O 1 HETATM 4108 O O . HOH Q 7 . ? 16.210 -17.444 7.534 1.00 81.16 ? 2063 HOH A O 1 HETATM 4109 O O . HOH Q 7 . ? 17.909 -19.713 -0.222 1.00 68.92 ? 2064 HOH A O 1 HETATM 4110 O O . HOH Q 7 . ? 22.227 -15.798 -5.078 1.00 74.84 ? 2065 HOH A O 1 HETATM 4111 O O . HOH Q 7 . ? 32.582 -6.869 -8.235 1.00 61.23 ? 2066 HOH A O 1 HETATM 4112 O O . HOH Q 7 . ? 39.139 -5.515 -5.164 1.00 65.92 ? 2067 HOH A O 1 HETATM 4113 O O . HOH Q 7 . ? 41.095 -15.031 5.272 1.00 67.31 ? 2068 HOH A O 1 HETATM 4114 O O . HOH Q 7 . ? 41.664 -8.174 21.128 1.00 74.37 ? 2069 HOH A O 1 HETATM 4115 O O . HOH Q 7 . ? 44.851 -27.063 11.709 1.00 74.24 ? 2070 HOH A O 1 HETATM 4116 O O . HOH Q 7 . ? 43.049 -24.652 1.668 1.00 60.01 ? 2071 HOH A O 1 HETATM 4117 O O . HOH Q 7 . ? 45.261 -29.244 -2.852 1.00 60.84 ? 2072 HOH A O 1 HETATM 4118 O O . HOH Q 7 . ? 18.088 -27.154 16.304 1.00 73.77 ? 2073 HOH A O 1 HETATM 4119 O O . HOH Q 7 . ? 15.732 -21.722 11.105 1.00 59.21 ? 2074 HOH A O 1 HETATM 4120 O O . HOH Q 7 . ? 27.936 -13.888 24.911 1.00 71.74 ? 2075 HOH A O 1 HETATM 4121 O O . HOH Q 7 . ? 28.832 -14.095 19.688 1.00 71.50 ? 2076 HOH A O 1 HETATM 4122 O O . HOH Q 7 . ? 28.032 0.794 11.851 1.00 73.42 ? 2077 HOH A O 1 HETATM 4123 O O . HOH Q 7 . ? 27.537 -0.980 21.033 1.00 76.60 ? 2078 HOH A O 1 HETATM 4124 O O . HOH Q 7 . ? 19.944 -9.690 12.160 1.00 63.89 ? 2079 HOH A O 1 HETATM 4125 O O . HOH Q 7 . ? 25.841 -25.755 27.558 1.00 72.00 ? 2080 HOH A O 1 HETATM 4126 O O . HOH Q 7 . ? 23.950 -35.209 4.052 1.00 68.98 ? 2081 HOH A O 1 HETATM 4127 O O . HOH Q 7 . ? 15.491 -29.914 6.221 1.00 77.49 ? 2082 HOH A O 1 HETATM 4128 O O . HOH Q 7 . ? 41.502 -10.594 23.113 1.00 54.05 ? 2083 HOH A O 1 HETATM 4129 O O . HOH Q 7 . ? 47.776 -10.252 31.406 1.00 73.07 ? 2084 HOH A O 1 HETATM 4130 O O . HOH Q 7 . ? 46.404 -11.374 34.326 1.00 70.19 ? 2085 HOH A O 1 HETATM 4131 O O . HOH Q 7 . ? 41.990 -35.430 12.199 1.00 76.00 ? 2086 HOH A O 1 HETATM 4132 O O . HOH Q 7 . ? 43.760 -1.638 14.754 1.00 74.35 ? 2087 HOH A O 1 HETATM 4133 O O . HOH Q 7 . ? 48.217 -12.710 13.518 1.00 84.27 ? 2088 HOH A O 1 HETATM 4134 O O . HOH Q 7 . ? 39.499 -13.087 -13.372 1.00 66.28 ? 2089 HOH A O 1 HETATM 4135 O O . HOH Q 7 . ? 25.855 -5.884 -8.164 1.00 83.76 ? 2090 HOH A O 1 HETATM 4136 O O . HOH Q 7 . ? 25.753 -12.198 -24.238 1.00 66.16 ? 2091 HOH A O 1 HETATM 4137 O O . HOH Q 7 . ? 30.511 -18.877 -36.936 1.00 79.31 ? 2092 HOH A O 1 HETATM 4138 O O . HOH Q 7 . ? 42.114 -8.849 -26.056 1.00 66.52 ? 2093 HOH A O 1 HETATM 4139 O O . HOH Q 7 . ? 41.597 -8.333 -30.968 1.00 63.39 ? 2094 HOH A O 1 HETATM 4140 O O . HOH Q 7 . ? 45.452 -11.333 -27.326 1.00 68.21 ? 2095 HOH A O 1 HETATM 4141 O O . HOH Q 7 . ? 47.847 -12.535 -33.706 1.00 64.36 ? 2096 HOH A O 1 HETATM 4142 O O . HOH Q 7 . ? 45.155 -15.300 -39.502 1.00 45.39 ? 2097 HOH A O 1 HETATM 4143 O O . HOH Q 7 . ? 40.097 -7.242 -40.974 1.00 74.45 ? 2098 HOH A O 1 HETATM 4144 O O . HOH Q 7 . ? 41.562 -21.514 -45.935 1.00 43.03 ? 2099 HOH A O 1 HETATM 4145 O O . HOH Q 7 . ? 32.415 -19.737 -49.863 1.00 62.62 ? 2100 HOH A O 1 HETATM 4146 O O . HOH Q 7 . ? 43.917 -18.035 -55.513 1.00 43.44 ? 2101 HOH A O 1 HETATM 4147 O O . HOH Q 7 . ? 46.759 -17.908 -56.067 1.00 52.61 ? 2102 HOH A O 1 HETATM 4148 O O . HOH Q 7 . ? 50.905 -15.369 -56.829 1.00 69.06 ? 2103 HOH A O 1 HETATM 4149 O O . HOH Q 7 . ? 23.200 -43.558 17.215 1.00 73.71 ? 2104 HOH A O 1 HETATM 4150 O O . HOH Q 7 . ? 17.396 -52.598 19.344 1.00 77.41 ? 2105 HOH A O 1 HETATM 4151 O O . HOH R 7 . ? 48.320 -16.969 -57.821 1.00 52.85 ? 2001 HOH B O 1 HETATM 4152 O O . HOH R 7 . ? 49.333 -19.355 -60.378 1.00 44.32 ? 2002 HOH B O 1 HETATM 4153 O O . HOH R 7 . ? 52.690 -25.741 -61.971 1.00 57.47 ? 2003 HOH B O 1 HETATM 4154 O O . HOH R 7 . ? 50.240 -12.841 -64.579 1.00 62.58 ? 2004 HOH B O 1 HETATM 4155 O O . HOH R 7 . ? 45.510 -13.230 -69.302 1.00 66.91 ? 2005 HOH B O 1 HETATM 4156 O O . HOH R 7 . ? 49.748 -13.896 -69.865 1.00 77.30 ? 2006 HOH B O 1 HETATM 4157 O O . HOH R 7 . ? 43.411 -12.295 -67.766 1.00 64.08 ? 2007 HOH B O 1 HETATM 4158 O O . HOH R 7 . ? 49.177 -11.315 -63.001 1.00 65.30 ? 2008 HOH B O 1 HETATM 4159 O O . HOH R 7 . ? 41.487 -9.256 -65.559 1.00 65.06 ? 2009 HOH B O 1 HETATM 4160 O O . HOH R 7 . ? 37.776 -7.714 -64.219 1.00 69.14 ? 2010 HOH B O 1 HETATM 4161 O O . HOH R 7 . ? 35.351 -8.820 -66.281 1.00 50.56 ? 2011 HOH B O 1 HETATM 4162 O O . HOH R 7 . ? 29.954 -30.365 -40.309 1.00 69.46 ? 2012 HOH B O 1 HETATM 4163 O O . HOH R 7 . ? 37.422 -35.148 -40.332 1.00 62.57 ? 2013 HOH B O 1 HETATM 4164 O O . HOH R 7 . ? 28.570 -15.205 -65.627 1.00 69.00 ? 2014 HOH B O 1 HETATM 4165 O O . HOH R 7 . ? 26.835 -17.863 -65.907 1.00 63.79 ? 2015 HOH B O 1 HETATM 4166 O O . HOH R 7 . ? 28.284 -19.539 -56.450 1.00 64.40 ? 2016 HOH B O 1 HETATM 4167 O O . HOH R 7 . ? 30.869 -17.699 -72.181 1.00 63.94 ? 2017 HOH B O 1 HETATM 4168 O O . HOH R 7 . ? 27.856 -14.420 -78.641 1.00 64.89 ? 2018 HOH B O 1 HETATM 4169 O O . HOH R 7 . ? 25.314 -14.584 -75.279 0.50 55.44 ? 2019 HOH B O 1 HETATM 4170 O O . HOH R 7 . ? 34.901 -8.668 -76.583 1.00 73.60 ? 2020 HOH B O 1 HETATM 4171 O O . HOH R 7 . ? 23.599 -19.434 -85.583 1.00 66.71 ? 2021 HOH B O 1 HETATM 4172 O O . HOH R 7 . ? 29.268 -22.872 -68.686 1.00 70.64 ? 2022 HOH B O 1 HETATM 4173 O O . HOH R 7 . ? 37.432 -28.970 -64.522 1.00 66.89 ? 2023 HOH B O 1 HETATM 4174 O O . HOH R 7 . ? 29.213 -27.334 -65.313 1.00 78.36 ? 2024 HOH B O 1 HETATM 4175 O O . HOH R 7 . ? 27.956 -24.108 -59.244 1.00 69.10 ? 2025 HOH B O 1 HETATM 4176 O O . HOH R 7 . ? 29.994 -29.757 -48.259 1.00 74.99 ? 2026 HOH B O 1 HETATM 4177 O O . HOH R 7 . ? 32.432 -21.301 -47.870 1.00 60.80 ? 2027 HOH B O 1 HETATM 4178 O O . HOH R 7 . ? 34.097 -31.349 -42.286 1.00 64.66 ? 2028 HOH B O 1 HETATM 4179 O O . HOH R 7 . ? 31.743 -30.357 -43.374 1.00 67.29 ? 2029 HOH B O 1 HETATM 4180 O O . HOH R 7 . ? 32.364 -27.873 -37.216 1.00 74.51 ? 2030 HOH B O 1 HETATM 4181 O O . HOH R 7 . ? 37.049 -33.978 -42.620 1.00 52.79 ? 2031 HOH B O 1 HETATM 4182 O O . HOH R 7 . ? 54.041 -24.875 0.203 1.00 68.89 ? 2032 HOH B O 1 HETATM 4183 O O . HOH R 7 . ? 51.280 -23.837 3.447 1.00 75.71 ? 2033 HOH B O 1 HETATM 4184 O O . HOH R 7 . ? 47.584 -19.956 -10.368 1.00 59.05 ? 2034 HOH B O 1 HETATM 4185 O O . HOH R 7 . ? 52.271 -12.358 -16.566 1.00 74.90 ? 2035 HOH B O 1 HETATM 4186 O O . HOH R 7 . ? 53.548 -24.012 -23.857 1.00 60.53 ? 2036 HOH B O 1 HETATM 4187 O O . HOH R 7 . ? 50.510 -17.841 -27.654 1.00 75.60 ? 2037 HOH B O 1 HETATM 4188 O O . HOH R 7 . ? 47.511 -26.832 -35.916 1.00 50.10 ? 2038 HOH B O 1 HETATM 4189 O O . HOH R 7 . ? 47.222 -17.268 -38.688 1.00 44.01 ? 2039 HOH B O 1 HETATM 4190 O O . HOH R 7 . ? 52.073 -18.855 -32.154 1.00 61.28 ? 2040 HOH B O 1 HETATM 4191 O O . HOH R 7 . ? 45.953 -27.068 -52.304 1.00 44.45 ? 2041 HOH B O 1 HETATM 4192 O O . HOH R 7 . ? 49.956 -27.783 -46.227 1.00 72.40 ? 2042 HOH B O 1 HETATM 4193 O O . HOH R 7 . ? 44.555 -29.279 -51.488 1.00 52.56 ? 2043 HOH B O 1 HETATM 4194 O O . HOH R 7 . ? 49.681 -31.854 -52.454 1.00 47.50 ? 2044 HOH B O 1 HETATM 4195 O O . HOH R 7 . ? 51.651 -22.350 -52.387 1.00 41.59 ? 2045 HOH B O 1 HETATM 4196 O O . HOH R 7 . ? 41.875 -28.927 -57.661 1.00 47.44 ? 2046 HOH B O 1 HETATM 4197 O O . HOH R 7 . ? 38.431 -27.560 -62.260 1.00 50.14 ? 2047 HOH B O 1 HETATM 4198 O O . HOH R 7 . ? 37.348 -29.112 -57.218 1.00 68.02 ? 2048 HOH B O 1 HETATM 4199 O O . HOH R 7 . ? 39.716 -29.373 -60.645 1.00 57.25 ? 2049 HOH B O 1 HETATM 4200 O O . HOH R 7 . ? 42.005 -31.269 -66.636 1.00 57.53 ? 2050 HOH B O 1 HETATM 4201 O O . HOH R 7 . ? 44.889 -30.434 -65.549 1.00 55.77 ? 2051 HOH B O 1 HETATM 4202 O O . HOH R 7 . ? 45.839 -19.710 -73.754 1.00 52.27 ? 2052 HOH B O 1 HETATM 4203 O O . HOH R 7 . ? 38.338 -32.408 -72.062 1.00 67.35 ? 2053 HOH B O 1 HETATM 4204 O O . HOH R 7 . ? 37.591 -33.382 -78.819 1.00 68.76 ? 2054 HOH B O 1 HETATM 4205 O O . HOH R 7 . ? 48.087 -23.949 -80.795 1.00 66.45 ? 2055 HOH B O 1 HETATM 4206 O O . HOH R 7 . ? 49.398 -27.610 -75.444 1.00 66.45 ? 2056 HOH B O 1 HETATM 4207 O O . HOH R 7 . ? 51.657 -16.924 -70.267 1.00 73.87 ? 2057 HOH B O 1 HETATM 4208 O O . HOH R 7 . ? 47.022 -11.307 -73.142 1.00 58.91 ? 2058 HOH B O 1 HETATM 4209 O O . HOH R 7 . ? 47.424 -3.736 -24.670 1.00 82.31 ? 2059 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 ? 0.8700 0.9043 0.6968 0.2517 -0.0740 -0.0158 1 ASP A N 2 C CA . ASP A 1 ? 0.8444 0.9347 0.6983 0.2478 -0.0749 -0.0261 1 ASP A CA 3 C C . ASP A 1 ? 0.8108 0.8822 0.6898 0.2148 -0.0669 -0.0246 1 ASP A C 4 O O . ASP A 1 ? 0.7829 0.8342 0.6728 0.1887 -0.0609 -0.0213 1 ASP A O 5 C CB . ASP A 1 ? 0.8228 0.9921 0.6982 0.2411 -0.0776 -0.0391 1 ASP A CB 6 C CG . ASP A 1 ? 0.8548 1.0570 0.7078 0.2764 -0.0865 -0.0423 1 ASP A CG 7 O OD1 . ASP A 1 ? 0.8953 1.0514 0.7115 0.3082 -0.0903 -0.0336 1 ASP A OD1 8 O OD2 . ASP A 1 ? 0.8771 1.1511 0.7458 0.2722 -0.0891 -0.0541 1 ASP A OD2 9 N N . GLN A 2 ? 0.8089 0.8878 0.6953 0.2181 -0.0667 -0.0271 2 GLN A N 10 C CA . GLN A 2 ? 0.7820 0.8431 0.6896 0.1901 -0.0594 -0.0254 2 GLN A CA 11 C C . GLN A 2 ? 0.7265 0.8283 0.6534 0.1866 -0.0594 -0.0338 2 GLN A C 12 O O . GLN A 2 ? 0.7149 0.8523 0.6361 0.2105 -0.0654 -0.0399 2 GLN A O 13 C CB . GLN A 2 ? 0.8384 0.8296 0.7272 0.1907 -0.0560 -0.0136 2 GLN A CB 14 C CG . GLN A 2 ? 0.9052 0.8693 0.7647 0.2196 -0.0600 -0.0104 2 GLN A CG 15 C CD . GLN A 2 ? 0.9539 0.8507 0.7950 0.2110 -0.0545 -0.0005 2 GLN A CD 16 O OE1 . GLN A 2 ? 0.9679 0.8495 0.8061 0.2130 -0.0531 0.0001 2 GLN A OE1 17 N NE2 . GLN A 2 ? 0.9840 0.8435 0.8125 0.1995 -0.0510 0.0062 2 GLN A NE2 18 N N . ILE A 3 ? 0.6859 0.7819 0.6337 0.1577 -0.0522 -0.0342 3 ILE A N 19 C CA . ILE A 3 ? 0.6641 0.7872 0.6286 0.1496 -0.0504 -0.0406 3 ILE A CA 20 C C . ILE A 3 ? 0.6577 0.7317 0.6251 0.1373 -0.0447 -0.0322 3 ILE A C 21 O O . ILE A 3 ? 0.6446 0.6854 0.6136 0.1203 -0.0393 -0.0259 3 ILE A O 22 C CB . ILE A 3 ? 0.6365 0.8109 0.6207 0.1239 -0.0465 -0.0523 3 ILE A CB 23 C CG1 . ILE A 3 ? 0.6241 0.8345 0.6213 0.1190 -0.0456 -0.0607 3 ILE A CG1 24 C CG2 . ILE A 3 ? 0.6207 0.7636 0.6105 0.0941 -0.0377 -0.0486 3 ILE A CG2 25 C CD1 . ILE A 3 ? 0.6116 0.8828 0.6210 0.0963 -0.0425 -0.0752 3 ILE A CD1 26 N N . CYS A 4 ? 0.6652 0.7383 0.6324 0.1475 -0.0461 -0.0326 4 CYS A N 27 C CA . CYS A 4 ? 0.6722 0.7029 0.6401 0.1390 -0.0416 -0.0252 4 CYS A CA 28 C C . CYS A 4 ? 0.6381 0.6948 0.6255 0.1255 -0.0384 -0.0312 4 CYS A C 29 O O . CYS A 4 ? 0.6558 0.7599 0.6503 0.1308 -0.0414 -0.0408 4 CYS A O 30 C CB . CYS A 4 ? 0.7207 0.7167 0.6640 0.1630 -0.0452 -0.0196 4 CYS A CB 31 S SG . CYS A 4 ? 0.8086 0.7629 0.7179 0.1803 -0.0481 -0.0121 4 CYS A SG 32 N N . ILE A 5 ? 0.6069 0.6348 0.6013 0.1088 -0.0324 -0.0259 5 ILE A N 33 C CA . ILE A 5 ? 0.5813 0.6235 0.5896 0.0973 -0.0289 -0.0298 5 ILE A CA 34 C C . ILE A 5 ? 0.5863 0.6016 0.5885 0.1081 -0.0299 -0.0245 5 ILE A C 35 O O . ILE A 5 ? 0.5793 0.5540 0.5700 0.1099 -0.0288 -0.0162 5 ILE A O 36 C CB . ILE A 5 ? 0.5678 0.5966 0.5846 0.0723 -0.0209 -0.0279 5 ILE A CB 37 C CG1 . ILE A 5 ? 0.5844 0.6325 0.6015 0.0595 -0.0186 -0.0334 5 ILE A CG1 38 C CG2 . ILE A 5 ? 0.5513 0.5899 0.5779 0.0611 -0.0168 -0.0313 5 ILE A CG2 39 C CD1 . ILE A 5 ? 0.5976 0.6969 0.6211 0.0524 -0.0191 -0.0461 5 ILE A CD1 40 N N . GLY A 6 ? 0.5766 0.6163 0.5853 0.1132 -0.0314 -0.0303 6 GLY A N 41 C CA . GLY A 6 ? 0.5881 0.6041 0.5893 0.1236 -0.0322 -0.0266 6 GLY A CA 42 C C . GLY A 6 ? 0.5754 0.6206 0.5902 0.1203 -0.0315 -0.0331 6 GLY A C 43 O O . GLY A 6 ? 0.5946 0.6777 0.6240 0.1070 -0.0295 -0.0407 6 GLY A O 44 N N . TYR A 7 ? 0.5724 0.5982 0.5794 0.1308 -0.0324 -0.0306 7 TYR A N 45 C CA . TYR A 7 ? 0.5707 0.6177 0.5898 0.1269 -0.0312 -0.0355 7 TYR A CA 46 C C . TYR A 7 ? 0.5897 0.6329 0.5932 0.1522 -0.0359 -0.0372 7 TYR A C 47 O O . TYR A 7 ? 0.6019 0.6121 0.5804 0.1705 -0.0386 -0.0327 7 TYR A O 48 C CB . TYR A 7 ? 0.5784 0.5989 0.6058 0.1071 -0.0248 -0.0296 7 TYR A CB 49 C CG . TYR A 7 ? 0.5961 0.5684 0.6083 0.1091 -0.0235 -0.0204 7 TYR A CG 50 C CD1 . TYR A 7 ? 0.5950 0.5442 0.6015 0.1021 -0.0216 -0.0144 7 TYR A CD1 51 C CD2 . TYR A 7 ? 0.6248 0.5765 0.6267 0.1160 -0.0236 -0.0187 7 TYR A CD2 52 C CE1 . TYR A 7 ? 0.6285 0.5393 0.6196 0.1004 -0.0196 -0.0076 7 TYR A CE1 53 C CE2 . TYR A 7 ? 0.6392 0.5488 0.6237 0.1132 -0.0212 -0.0120 7 TYR A CE2 54 C CZ . TYR A 7 ? 0.6448 0.5359 0.6242 0.1044 -0.0191 -0.0067 7 TYR A CZ 55 O OH . TYR A 7 ? 0.6685 0.5228 0.6294 0.0980 -0.0159 -0.0015 7 TYR A OH 56 N N . HIS A 8 ? 0.5902 0.6642 0.6050 0.1526 -0.0360 -0.0439 8 HIS A N 57 C CA . HIS A 8 ? 0.6280 0.7090 0.6295 0.1782 -0.0405 -0.0478 8 HIS A CA 58 C C . HIS A 8 ? 0.6698 0.6927 0.6498 0.1845 -0.0387 -0.0399 8 HIS A C 59 O O . HIS A 8 ? 0.6629 0.6575 0.6491 0.1637 -0.0335 -0.0339 8 HIS A O 60 C CB . HIS A 8 ? 0.6141 0.7454 0.6372 0.1700 -0.0396 -0.0572 8 HIS A CB 61 C CG . HIS A 8 ? 0.6533 0.8016 0.6660 0.1962 -0.0439 -0.0628 8 HIS A CG 62 N ND1 . HIS A 8 ? 0.6836 0.8682 0.6847 0.2257 -0.0505 -0.0701 8 HIS A ND1 63 C CD2 . HIS A 8 ? 0.6618 0.8006 0.6739 0.1983 -0.0425 -0.0631 8 HIS A CD2 64 C CE1 . HIS A 8 ? 0.6979 0.8921 0.6900 0.2468 -0.0530 -0.0743 8 HIS A CE1 65 N NE2 . HIS A 8 ? 0.6741 0.8397 0.6730 0.2294 -0.0480 -0.0703 8 HIS A NE2 66 N N . ALA A 9 ? 0.7144 0.7199 0.6654 0.2139 -0.0427 -0.0405 9 ALA A N 67 C CA . ALA A 9 ? 0.7401 0.6927 0.6647 0.2204 -0.0403 -0.0358 9 ALA A CA 68 C C . ALA A 9 ? 0.7761 0.7411 0.6815 0.2528 -0.0448 -0.0421 9 ALA A C 69 O O . ALA A 9 ? 0.7939 0.8034 0.7004 0.2746 -0.0504 -0.0489 9 ALA A O 70 C CB . ALA A 9 ? 0.7639 0.6536 0.6546 0.2219 -0.0382 -0.0273 9 ALA A CB 71 N N . ASN A 10 ? 0.7986 0.7277 0.6855 0.2565 -0.0421 -0.0405 10 ASN A N 72 C CA . ASN A 10 ? 0.8438 0.7775 0.7070 0.2898 -0.0457 -0.0462 10 ASN A CA 73 C C . ASN A 10 ? 0.9225 0.7855 0.7460 0.2942 -0.0412 -0.0415 10 ASN A C 74 O O . ASN A 10 ? 0.9186 0.7305 0.7301 0.2718 -0.0355 -0.0343 10 ASN A O 75 C CB . ASN A 10 ? 0.7968 0.8040 0.6973 0.2876 -0.0480 -0.0560 10 ASN A CB 76 C CG . ASN A 10 ? 0.7613 0.7680 0.6881 0.2562 -0.0425 -0.0548 10 ASN A CG 77 O OD1 . ASN A 10 ? 0.7593 0.7133 0.6752 0.2398 -0.0374 -0.0474 10 ASN A OD1 78 N ND2 . ASN A 10 ? 0.7196 0.7876 0.6795 0.2469 -0.0431 -0.0628 10 ASN A ND2 79 N N . ASN A 11 ? 1.0212 0.8830 0.8222 0.3225 -0.0432 -0.0465 11 ASN A N 80 C CA . ASN A 11 ? 1.1304 0.9207 0.8858 0.3288 -0.0383 -0.0433 11 ASN A CA 81 C C . ASN A 11 ? 1.0652 0.8612 0.8447 0.3027 -0.0336 -0.0445 11 ASN A C 82 O O . ASN A 11 ? 1.0943 0.8422 0.8395 0.3083 -0.0297 -0.0442 11 ASN A O 83 C CB . ASN A 11 ? 1.2798 1.0535 0.9869 0.3779 -0.0422 -0.0473 11 ASN A CB 84 C CG . ASN A 11 ? 1.3838 1.2369 1.1200 0.3988 -0.0483 -0.0579 11 ASN A CG 85 O OD1 . ASN A 11 ? 1.3265 1.2363 1.1142 0.3730 -0.0481 -0.0620 11 ASN A OD1 86 N ND2 . ASN A 11 ? 1.6242 1.4816 1.3238 0.4468 -0.0535 -0.0626 11 ASN A ND2 87 N N . SER A 12 ? 0.9675 0.8183 0.8016 0.2744 -0.0335 -0.0460 12 SER A N 88 C CA . SER A 12 ? 0.9096 0.7727 0.7692 0.2507 -0.0297 -0.0471 12 SER A CA 89 C C . SER A 12 ? 0.9272 0.7289 0.7666 0.2268 -0.0224 -0.0403 12 SER A C 90 O O . SER A 12 ? 0.9051 0.6778 0.7360 0.2119 -0.0197 -0.0344 12 SER A O 91 C CB . SER A 12 ? 0.8438 0.7690 0.7578 0.2255 -0.0302 -0.0490 12 SER A CB 92 O OG . SER A 12 ? 0.7820 0.7218 0.7187 0.2062 -0.0268 -0.0503 12 SER A OG 93 N N . THR A 13 ? 0.9484 0.7344 0.7793 0.2229 -0.0190 -0.0423 13 THR A N 94 C CA . THR A 13 ? 0.9527 0.6933 0.7688 0.1962 -0.0116 -0.0381 13 THR A CA 95 C C . THR A 13 ? 0.9041 0.6853 0.7640 0.1706 -0.0097 -0.0391 13 THR A C 96 O O . THR A 13 ? 0.8912 0.6484 0.7448 0.1482 -0.0040 -0.0370 13 THR A O 97 C CB . THR A 13 ? 1.0236 0.7032 0.7847 0.2108 -0.0078 -0.0398 13 THR A CB 98 O OG1 . THR A 13 ? 1.0274 0.7368 0.7972 0.2304 -0.0109 -0.0463 13 THR A OG1 99 C CG2 . THR A 13 ? 1.0722 0.6981 0.7784 0.2373 -0.0083 -0.0379 13 THR A CG2 100 N N . GLU A 14 ? 0.8690 0.7113 0.7698 0.1732 -0.0140 -0.0427 14 GLU A N 101 C CA . GLU A 14 ? 0.8406 0.7192 0.7796 0.1507 -0.0120 -0.0432 14 GLU A CA 102 C C . GLU A 14 ? 0.7927 0.6628 0.7442 0.1231 -0.0079 -0.0366 14 GLU A C 103 O O . GLU A 14 ? 0.7761 0.6437 0.7294 0.1203 -0.0086 -0.0330 14 GLU A O 104 C CB . GLU A 14 ? 0.8489 0.7889 0.8235 0.1539 -0.0160 -0.0480 14 GLU A CB 105 C CG . GLU A 14 ? 0.9071 0.8747 0.8766 0.1803 -0.0204 -0.0564 14 GLU A CG 106 C CD . GLU A 14 ? 0.9602 0.9297 0.9290 0.1807 -0.0186 -0.0602 14 GLU A CD 107 O OE1 . GLU A 14 ? 0.9586 0.9523 0.9553 0.1592 -0.0160 -0.0602 14 GLU A OE1 108 O OE2 . GLU A 14 ? 1.0351 0.9792 0.9722 0.2038 -0.0195 -0.0632 14 GLU A OE2 109 N N . GLN A 15 ? 0.7726 0.6421 0.7324 0.1044 -0.0037 -0.0354 15 GLN A N 110 C CA . GLN A 15 ? 0.7397 0.6079 0.7101 0.0807 0.0003 -0.0301 15 GLN A CA 111 C C . GLN A 15 ? 0.6666 0.5756 0.6723 0.0690 0.0009 -0.0296 15 GLN A C 112 O O . GLN A 15 ? 0.6468 0.5746 0.6626 0.0728 0.0002 -0.0334 15 GLN A O 113 C CB . GLN A 15 ? 0.7884 0.6194 0.7310 0.0675 0.0057 -0.0297 15 GLN A CB 114 C CG . GLN A 15 ? 0.8556 0.6334 0.7530 0.0753 0.0072 -0.0297 15 GLN A CG 115 C CD . GLN A 15 ? 0.9088 0.6471 0.7737 0.0553 0.0145 -0.0303 15 GLN A CD 116 O OE1 . GLN A 15 ? 0.9927 0.6885 0.8221 0.0493 0.0182 -0.0290 15 GLN A OE1 117 N NE2 . GLN A 15 ? 0.9100 0.6620 0.7843 0.0431 0.0173 -0.0328 15 GLN A NE2 118 N N . VAL A 16 ? 0.6335 0.5541 0.6541 0.0563 0.0026 -0.0248 16 VAL A N 119 C CA . VAL A 16 ? 0.5782 0.5279 0.6232 0.0465 0.0043 -0.0231 16 VAL A CA 120 C C . VAL A 16 ? 0.5763 0.5239 0.6209 0.0325 0.0079 -0.0184 16 VAL A C 121 O O . VAL A 16 ? 0.5768 0.5068 0.6080 0.0288 0.0088 -0.0165 16 VAL A O 122 C CB . VAL A 16 ? 0.5548 0.5266 0.6169 0.0490 0.0029 -0.0226 16 VAL A CB 123 C CG1 . VAL A 16 ? 0.5707 0.5559 0.6344 0.0613 -0.0007 -0.0290 16 VAL A CG1 124 C CG2 . VAL A 16 ? 0.5654 0.5283 0.6246 0.0477 0.0028 -0.0184 16 VAL A CG2 125 N N . ASP A 17 ? 0.5678 0.5356 0.6255 0.0255 0.0102 -0.0171 17 ASP A N 126 C CA . ASP A 17 ? 0.5795 0.5569 0.6387 0.0153 0.0133 -0.0134 17 ASP A CA 127 C C . ASP A 17 ? 0.5605 0.5537 0.6322 0.0186 0.0137 -0.0087 17 ASP A C 128 O O . ASP A 17 ? 0.5347 0.5332 0.6143 0.0240 0.0131 -0.0087 17 ASP A O 129 C CB . ASP A 17 ? 0.6113 0.6024 0.6725 0.0078 0.0156 -0.0149 17 ASP A CB 130 C CG . ASP A 17 ? 0.6659 0.6364 0.7078 0.0003 0.0171 -0.0197 17 ASP A CG 131 O OD1 . ASP A 17 ? 0.6834 0.6296 0.7056 -0.0046 0.0182 -0.0205 17 ASP A OD1 132 O OD2 . ASP A 17 ? 0.6955 0.6707 0.7381 -0.0014 0.0179 -0.0227 17 ASP A OD2 133 N N . THR A 18 ? 0.5612 0.5606 0.6308 0.0147 0.0154 -0.0053 18 THR A N 134 C CA . THR A 18 ? 0.5520 0.5643 0.6275 0.0199 0.0168 -0.0005 18 THR A CA 135 C C . THR A 18 ? 0.5786 0.6152 0.6539 0.0165 0.0192 0.0012 18 THR A C 136 O O . THR A 18 ? 0.5907 0.6349 0.6622 0.0061 0.0202 -0.0021 18 THR A O 137 C CB . THR A 18 ? 0.5420 0.5429 0.6142 0.0231 0.0159 0.0017 18 THR A CB 138 O OG1 . THR A 18 ? 0.5505 0.5493 0.6150 0.0159 0.0163 0.0013 18 THR A OG1 139 C CG2 . THR A 18 ? 0.5389 0.5238 0.6110 0.0267 0.0132 -0.0009 18 THR A CG2 140 N N . ILE A 19 ? 0.6207 0.6699 0.6968 0.0255 0.0207 0.0056 19 ILE A N 141 C CA . ILE A 19 ? 0.6252 0.7060 0.7007 0.0272 0.0226 0.0069 19 ILE A CA 142 C C . ILE A 19 ? 0.6305 0.7255 0.7031 0.0160 0.0233 0.0043 19 ILE A C 143 O O . ILE A 19 ? 0.6127 0.7353 0.6849 0.0063 0.0248 0.0008 19 ILE A O 144 C CB . ILE A 19 ? 0.6576 0.7426 0.7277 0.0444 0.0242 0.0127 19 ILE A CB 145 C CG1 . ILE A 19 ? 0.6919 0.7598 0.7577 0.0523 0.0254 0.0149 19 ILE A CG1 146 C CG2 . ILE A 19 ? 0.6752 0.7999 0.7434 0.0512 0.0256 0.0135 19 ILE A CG2 147 C CD1 . ILE A 19 ? 0.6853 0.7732 0.7524 0.0543 0.0262 0.0145 19 ILE A CD1 148 N N . MET A 20 ? 0.6494 0.7266 0.7184 0.0155 0.0225 0.0053 20 MET A N 149 C CA . MET A 20 ? 0.6712 0.7594 0.7344 0.0041 0.0239 0.0030 20 MET A CA 150 C C . MET A 20 ? 0.6902 0.7530 0.7424 -0.0131 0.0243 -0.0016 20 MET A C 151 O O . MET A 20 ? 0.6986 0.7673 0.7403 -0.0281 0.0268 -0.0047 20 MET A O 152 C CB . MET A 20 ? 0.6843 0.7647 0.7459 0.0126 0.0234 0.0067 20 MET A CB 153 C CG . MET A 20 ? 0.7086 0.8143 0.7718 0.0294 0.0245 0.0108 20 MET A CG 154 S SD . MET A 20 ? 0.7507 0.8501 0.8089 0.0367 0.0247 0.0138 20 MET A SD 155 C CE . MET A 20 ? 0.8091 0.9111 0.8608 0.0632 0.0263 0.0198 20 MET A CE 156 N N . GLU A 21 ? 0.6712 0.7046 0.7217 -0.0107 0.0223 -0.0025 21 GLU A N 157 C CA . GLU A 21 ? 0.6890 0.6895 0.7221 -0.0209 0.0226 -0.0061 21 GLU A CA 158 C C . GLU A 21 ? 0.6918 0.6754 0.7236 -0.0172 0.0212 -0.0085 21 GLU A C 159 O O . GLU A 21 ? 0.6843 0.6715 0.7296 -0.0046 0.0185 -0.0068 21 GLU A O 160 C CB . GLU A 21 ? 0.7168 0.6909 0.7433 -0.0149 0.0205 -0.0040 21 GLU A CB 161 C CG . GLU A 21 ? 0.7721 0.7101 0.7717 -0.0252 0.0222 -0.0070 21 GLU A CG 162 C CD . GLU A 21 ? 0.8176 0.7321 0.8095 -0.0176 0.0199 -0.0045 21 GLU A CD 163 O OE1 . GLU A 21 ? 0.7520 0.6823 0.7608 -0.0079 0.0177 -0.0009 21 GLU A OE1 164 O OE2 . GLU A 21 ? 0.8481 0.7252 0.8131 -0.0210 0.0208 -0.0062 21 GLU A OE2 165 N N . LYS A 22 ? 0.7239 0.6873 0.7356 -0.0295 0.0237 -0.0130 22 LYS A N 166 C CA . LYS A 22 ? 0.7514 0.6970 0.7575 -0.0255 0.0228 -0.0161 22 LYS A CA 167 C C . LYS A 22 ? 0.7440 0.6440 0.7249 -0.0200 0.0219 -0.0177 22 LYS A C 168 O O . LYS A 22 ? 0.7540 0.6315 0.7149 -0.0262 0.0237 -0.0173 22 LYS A O 169 C CB . LYS A 22 ? 0.8108 0.7672 0.8089 -0.0423 0.0272 -0.0205 22 LYS A CB 170 C CG . LYS A 22 ? 0.8375 0.8420 0.8597 -0.0421 0.0272 -0.0190 22 LYS A CG 171 C CD . LYS A 22 ? 0.9306 0.9512 0.9445 -0.0602 0.0315 -0.0244 22 LYS A CD 172 C CE . LYS A 22 ? 0.9664 1.0161 0.9997 -0.0521 0.0300 -0.0237 22 LYS A CE 173 N NZ . LYS A 22 ? 0.9849 1.0414 1.0079 -0.0685 0.0337 -0.0299 22 LYS A NZ 174 N N . ASN A 23 ? 0.7446 0.6324 0.7248 -0.0064 0.0191 -0.0195 23 ASN A N 175 C CA . ASN A 23 ? 0.8068 0.6525 0.7589 0.0046 0.0180 -0.0216 23 ASN A CA 176 C C . ASN A 23 ? 0.7760 0.6102 0.7244 0.0149 0.0151 -0.0185 23 ASN A C 177 O O . ASN A 23 ? 0.7955 0.5910 0.7117 0.0143 0.0168 -0.0187 23 ASN A O 178 C CB . ASN A 23 ? 0.8858 0.6919 0.7981 -0.0103 0.0240 -0.0252 23 ASN A CB 179 C CG . ASN A 23 ? 0.9781 0.7900 0.8894 -0.0179 0.0266 -0.0293 23 ASN A CG 180 O OD1 . ASN A 23 ? 0.9273 0.7681 0.8655 -0.0078 0.0232 -0.0295 23 ASN A OD1 181 N ND2 . ASN A 23 ? 1.1362 0.9190 1.0135 -0.0377 0.0335 -0.0332 23 ASN A ND2 182 N N . VAL A 24 ? 0.7173 0.5826 0.6955 0.0235 0.0112 -0.0159 24 VAL A N 183 C CA . VAL A 24 ? 0.6847 0.5453 0.6632 0.0336 0.0080 -0.0137 24 VAL A CA 184 C C . VAL A 24 ? 0.6911 0.5439 0.6629 0.0545 0.0035 -0.0168 24 VAL A C 185 O O . VAL A 24 ? 0.6797 0.5562 0.6686 0.0617 0.0013 -0.0197 24 VAL A O 186 C CB . VAL A 24 ? 0.6418 0.5366 0.6502 0.0325 0.0069 -0.0105 24 VAL A CB 187 C CG1 . VAL A 24 ? 0.6548 0.5444 0.6619 0.0404 0.0043 -0.0086 24 VAL A CG1 188 C CG2 . VAL A 24 ? 0.6293 0.5398 0.6447 0.0172 0.0109 -0.0078 24 VAL A CG2 189 N N . THR A 25 ? 0.7050 0.5264 0.6496 0.0651 0.0022 -0.0168 25 THR A N 190 C CA . THR A 25 ? 0.7126 0.5304 0.6471 0.0894 -0.0025 -0.0204 25 THR A CA 191 C C . THR A 25 ? 0.6781 0.5338 0.6399 0.0972 -0.0071 -0.0208 25 THR A C 192 O O . THR A 25 ? 0.6873 0.5445 0.6544 0.0912 -0.0070 -0.0172 25 THR A O 193 C CB . THR A 25 ? 0.7711 0.5382 0.6604 0.1014 -0.0021 -0.0198 25 THR A CB 194 O OG1 . THR A 25 ? 0.8196 0.5455 0.6775 0.0874 0.0042 -0.0198 25 THR A OG1 195 C CG2 . THR A 25 ? 0.7991 0.5649 0.6737 0.1317 -0.0071 -0.0240 25 THR A CG2 196 N N . VAL A 26 ? 0.6481 0.5356 0.6255 0.1086 -0.0104 -0.0258 26 VAL A N 197 C CA . VAL A 26 ? 0.6160 0.5431 0.6171 0.1117 -0.0136 -0.0282 26 VAL A CA 198 C C . VAL A 26 ? 0.6338 0.5800 0.6279 0.1356 -0.0188 -0.0350 26 VAL A C 199 O O . VAL A 26 ? 0.6745 0.6111 0.6519 0.1510 -0.0201 -0.0384 26 VAL A O 200 C CB . VAL A 26 ? 0.5745 0.5350 0.6051 0.0961 -0.0112 -0.0294 26 VAL A CB 201 C CG1 . VAL A 26 ? 0.5611 0.5096 0.5980 0.0773 -0.0066 -0.0228 26 VAL A CG1 202 C CG2 . VAL A 26 ? 0.5709 0.5443 0.6050 0.0998 -0.0112 -0.0342 26 VAL A CG2 203 N N . THR A 27 ? 0.6257 0.6019 0.6317 0.1392 -0.0217 -0.0376 27 THR A N 204 C CA . THR A 27 ? 0.6376 0.6447 0.6392 0.1625 -0.0272 -0.0452 27 THR A CA 205 C C . THR A 27 ? 0.6248 0.6751 0.6428 0.1642 -0.0279 -0.0534 27 THR A C 206 O O . THR A 27 ? 0.6561 0.7231 0.6627 0.1883 -0.0319 -0.0597 27 THR A O 207 C CB . THR A 27 ? 0.6290 0.6657 0.6416 0.1611 -0.0294 -0.0472 27 THR A CB 208 O OG1 . THR A 27 ? 0.6013 0.6661 0.6412 0.1357 -0.0257 -0.0486 27 THR A OG1 209 C CG2 . THR A 27 ? 0.6533 0.6494 0.6485 0.1615 -0.0291 -0.0396 27 THR A CG2 210 N N . HIS A 28 ? 0.6083 0.6769 0.6504 0.1400 -0.0237 -0.0536 28 HIS A N 211 C CA . HIS A 28 ? 0.5942 0.7018 0.6512 0.1368 -0.0232 -0.0613 28 HIS A CA 212 C C . HIS A 28 ? 0.5999 0.6942 0.6683 0.1147 -0.0176 -0.0571 28 HIS A C 213 O O . HIS A 28 ? 0.5861 0.6612 0.6594 0.0974 -0.0138 -0.0503 28 HIS A O 214 C CB . HIS A 28 ? 0.5602 0.7231 0.6340 0.1294 -0.0238 -0.0700 28 HIS A CB 215 C CG . HIS A 28 ? 0.5717 0.7568 0.6367 0.1503 -0.0294 -0.0747 28 HIS A CG 216 N ND1 . HIS A 28 ? 0.5686 0.7332 0.6265 0.1506 -0.0303 -0.0694 28 HIS A ND1 217 C CD2 . HIS A 28 ? 0.5783 0.8067 0.6390 0.1740 -0.0347 -0.0845 28 HIS A CD2 218 C CE1 . HIS A 28 ? 0.5836 0.7764 0.6331 0.1730 -0.0359 -0.0753 28 HIS A CE1 219 N NE2 . HIS A 28 ? 0.5888 0.8221 0.6395 0.1887 -0.0388 -0.0846 28 HIS A NE2 220 N N . ALA A 29 ? 0.6210 0.7276 0.6919 0.1179 -0.0174 -0.0614 29 ALA A N 221 C CA . ALA A 29 ? 0.6250 0.7237 0.7056 0.0997 -0.0125 -0.0583 29 ALA A CA 222 C C . ALA A 29 ? 0.6227 0.7619 0.7148 0.0976 -0.0121 -0.0672 29 ALA A C 223 O O . ALA A 29 ? 0.6281 0.8031 0.7202 0.1121 -0.0158 -0.0761 29 ALA A O 224 C CB . ALA A 29 ? 0.6412 0.6974 0.7068 0.1037 -0.0117 -0.0524 29 ALA A CB 225 N N . GLN A 30 ? 0.6083 0.7446 0.7091 0.0802 -0.0074 -0.0650 30 GLN A N 226 C CA . GLN A 30 ? 0.6075 0.7786 0.7178 0.0743 -0.0059 -0.0728 30 GLN A CA 227 C C . GLN A 30 ? 0.5903 0.7406 0.7009 0.0679 -0.0029 -0.0683 30 GLN A C 228 O O . GLN A 30 ? 0.5599 0.6916 0.6728 0.0521 0.0015 -0.0615 30 GLN A O 229 C CB . GLN A 30 ? 0.6026 0.8011 0.7219 0.0523 -0.0014 -0.0769 30 GLN A CB 230 C CG . GLN A 30 ? 0.6208 0.8540 0.7471 0.0411 0.0017 -0.0854 30 GLN A CG 231 C CD . GLN A 30 ? 0.6279 0.8958 0.7567 0.0198 0.0062 -0.0937 30 GLN A CD 232 O OE1 . GLN A 30 ? 0.6693 0.9437 0.7959 0.0167 0.0059 -0.0951 30 GLN A OE1 233 N NE2 . GLN A 30 ? 0.6419 0.9316 0.7726 0.0031 0.0111 -0.0999 30 GLN A NE2 234 N N . ASP A 31 ? 0.6061 0.7599 0.7119 0.0821 -0.0053 -0.0724 31 ASP A N 235 C CA . ASP A 31 ? 0.6183 0.7595 0.7246 0.0761 -0.0026 -0.0703 31 ASP A CA 236 C C . ASP A 31 ? 0.5951 0.7671 0.7150 0.0586 0.0014 -0.0745 31 ASP A C 237 O O . ASP A 31 ? 0.5841 0.7957 0.7102 0.0576 0.0009 -0.0835 31 ASP A O 238 C CB . ASP A 31 ? 0.6345 0.7701 0.7279 0.0969 -0.0058 -0.0748 31 ASP A CB 239 C CG . ASP A 31 ? 0.6586 0.7745 0.7489 0.0906 -0.0030 -0.0722 31 ASP A CG 240 O OD1 . ASP A 31 ? 0.6440 0.7556 0.7439 0.0717 0.0009 -0.0669 31 ASP A OD1 241 O OD2 . ASP A 31 ? 0.7128 0.8166 0.7879 0.1060 -0.0045 -0.0757 31 ASP A OD2 242 N N . ILE A 32 ? 0.5908 0.7457 0.7126 0.0444 0.0057 -0.0683 32 ILE A N 243 C CA . ILE A 32 ? 0.5846 0.7582 0.7122 0.0270 0.0106 -0.0709 32 ILE A CA 244 C C . ILE A 32 ? 0.5848 0.7544 0.7135 0.0250 0.0123 -0.0700 32 ILE A C 245 O O . ILE A 32 ? 0.5665 0.7426 0.6962 0.0105 0.0170 -0.0701 32 ILE A O 246 C CB . ILE A 32 ? 0.5714 0.7267 0.6946 0.0108 0.0157 -0.0639 32 ILE A CB 247 C CG1 . ILE A 32 ? 0.5699 0.6902 0.6884 0.0134 0.0161 -0.0529 32 ILE A CG1 248 C CG2 . ILE A 32 ? 0.5766 0.7398 0.6983 0.0093 0.0150 -0.0665 32 ILE A CG2 249 C CD1 . ILE A 32 ? 0.5798 0.6815 0.6900 0.0020 0.0216 -0.0458 32 ILE A CD1 250 N N . LEU A 33 ? 0.5924 0.7483 0.7171 0.0387 0.0090 -0.0694 33 LEU A N 251 C CA . LEU A 33 ? 0.6107 0.7612 0.7350 0.0367 0.0105 -0.0688 33 LEU A CA 252 C C . LEU A 33 ? 0.6369 0.8012 0.7581 0.0519 0.0075 -0.0774 33 LEU A C 253 O O . LEU A 33 ? 0.6679 0.8155 0.7767 0.0685 0.0041 -0.0784 33 LEU A O 254 C CB . LEU A 33 ? 0.6132 0.7303 0.7300 0.0358 0.0111 -0.0604 33 LEU A CB 255 C CG . LEU A 33 ? 0.6065 0.7180 0.7213 0.0321 0.0128 -0.0597 33 LEU A CG 256 C CD1 . LEU A 33 ? 0.5942 0.7190 0.7169 0.0192 0.0167 -0.0572 33 LEU A CD1 257 C CD2 . LEU A 33 ? 0.6199 0.7040 0.7244 0.0302 0.0133 -0.0541 33 LEU A CD2 258 N N . GLU A 34 ? 0.6415 0.8334 0.7699 0.0471 0.0091 -0.0835 34 GLU A N 259 C CA . GLU A 34 ? 0.6499 0.8575 0.7746 0.0629 0.0066 -0.0922 34 GLU A CA 260 C C . GLU A 34 ? 0.6386 0.8150 0.7529 0.0654 0.0074 -0.0886 34 GLU A C 261 O O . GLU A 34 ? 0.5978 0.7695 0.7173 0.0504 0.0108 -0.0844 34 GLU A O 262 C CB . GLU A 34 ? 0.6601 0.9126 0.7965 0.0544 0.0085 -0.1009 34 GLU A CB 263 C CG . GLU A 34 ? 0.6795 0.9562 0.8127 0.0734 0.0057 -0.1110 34 GLU A CG 264 C CD . GLU A 34 ? 0.7183 0.9995 0.8407 0.1003 0.0003 -0.1158 34 GLU A CD 265 O OE1 . GLU A 34 ? 0.7388 1.0520 0.8678 0.1011 -0.0013 -0.1204 34 GLU A OE1 266 O OE2 . GLU A 34 ? 0.7481 0.9983 0.8517 0.1204 -0.0019 -0.1150 34 GLU A OE2 267 N N . LYS A 35 ? 0.6653 0.8186 0.7609 0.0843 0.0049 -0.0907 35 LYS A N 268 C CA . LYS A 35 ? 0.6793 0.7969 0.7578 0.0845 0.0068 -0.0886 35 LYS A CA 269 C C . LYS A 35 ? 0.6785 0.8021 0.7461 0.0998 0.0062 -0.0971 35 LYS A C 270 O O . LYS A 35 ? 0.6811 0.7796 0.7355 0.0960 0.0088 -0.0966 35 LYS A O 271 C CB . LYS A 35 ? 0.7109 0.7829 0.7655 0.0910 0.0064 -0.0841 35 LYS A CB 272 C CG . LYS A 35 ? 0.7149 0.7763 0.7773 0.0751 0.0076 -0.0754 35 LYS A CG 273 C CD . LYS A 35 ? 0.7677 0.7868 0.8041 0.0819 0.0074 -0.0725 35 LYS A CD 274 C CE . LYS A 35 ? 0.7722 0.7969 0.8167 0.0833 0.0050 -0.0686 35 LYS A CE 275 N NZ . LYS A 35 ? 0.7525 0.8134 0.8094 0.0971 0.0012 -0.0742 35 LYS A NZ 276 N N . THR A 36 ? 0.6673 0.8268 0.7393 0.1167 0.0030 -0.1055 36 THR A N 277 C CA . THR A 36 ? 0.7132 0.8819 0.7726 0.1364 0.0020 -0.1144 36 THR A CA 278 C C . THR A 36 ? 0.7022 0.9236 0.7847 0.1277 0.0030 -0.1213 36 THR A C 279 O O . THR A 36 ? 0.6574 0.9157 0.7627 0.1114 0.0037 -0.1218 36 THR A O 280 C CB . THR A 36 ? 0.7418 0.9166 0.7828 0.1693 -0.0026 -0.1208 36 THR A CB 281 O OG1 . THR A 36 ? 0.7436 0.9770 0.8083 0.1692 -0.0054 -0.1261 36 THR A OG1 282 C CG2 . THR A 36 ? 0.7776 0.8977 0.7914 0.1783 -0.0031 -0.1141 36 THR A CG2 283 N N . HIS A 37 ? 0.7225 0.9433 0.7947 0.1378 0.0037 -0.1270 37 HIS A N 284 C CA . HIS A 37 ? 0.7096 0.9797 0.7990 0.1331 0.0046 -0.1352 37 HIS A CA 285 C C . HIS A 37 ? 0.7437 1.0199 0.8131 0.1640 0.0024 -0.1451 37 HIS A C 286 O O . HIS A 37 ? 0.7860 1.0171 0.8241 0.1863 0.0013 -0.1439 37 HIS A O 287 C CB . HIS A 37 ? 0.6996 0.9592 0.7995 0.1066 0.0092 -0.1299 37 HIS A CB 288 C CG . HIS A 37 ? 0.7228 0.9320 0.8009 0.1083 0.0113 -0.1260 37 HIS A CG 289 N ND1 . HIS A 37 ? 0.7511 0.9569 0.8161 0.1188 0.0123 -0.1325 37 HIS A ND1 290 C CD2 . HIS A 37 ? 0.7399 0.9017 0.8049 0.0988 0.0131 -0.1175 37 HIS A CD2 291 C CE1 . HIS A 37 ? 0.7651 0.9208 0.8083 0.1141 0.0151 -0.1281 37 HIS A CE1 292 N NE2 . HIS A 37 ? 0.7741 0.9049 0.8175 0.1011 0.0157 -0.1194 37 HIS A NE2 293 N N . ASN A 38 ? 0.7403 1.0692 0.8233 0.1658 0.0025 -0.1549 38 ASN A N 294 C CA . ASN A 38 ? 0.7562 1.1000 0.8205 0.1990 0.0001 -0.1655 38 ASN A CA 295 C C . ASN A 38 ? 0.7774 1.0885 0.8256 0.1997 0.0034 -0.1659 38 ASN A C 296 O O . ASN A 38 ? 0.8149 1.1286 0.8421 0.2284 0.0022 -0.1741 38 ASN A O 297 C CB . ASN A 38 ? 0.7254 1.1538 0.8112 0.2041 -0.0020 -0.1785 38 ASN A CB 298 C CG . ASN A 38 ? 0.6936 1.1584 0.8031 0.1757 0.0022 -0.1819 38 ASN A CG 299 O OD1 . ASN A 38 ? 0.7034 1.1342 0.8180 0.1500 0.0063 -0.1732 38 ASN A OD1 300 N ND2 . ASN A 38 ? 0.6694 1.2062 0.7920 0.1804 0.0014 -0.1951 38 ASN A ND2 301 N N . GLY A 39 ? 0.7631 1.0480 0.8208 0.1692 0.0076 -0.1577 39 GLY A N 302 C CA . GLY A 39 ? 0.7789 1.0263 0.8196 0.1656 0.0112 -0.1568 39 GLY A CA 303 C C . GLY A 39 ? 0.7778 1.0679 0.8307 0.1646 0.0124 -0.1655 39 GLY A C 304 O O . GLY A 39 ? 0.7736 1.0371 0.8084 0.1685 0.0150 -0.1675 39 GLY A O 305 N N . LYS A 40 ? 0.7680 1.1235 0.8495 0.1568 0.0113 -0.1713 40 LYS A N 306 C CA . LYS A 40 ? 0.7538 1.1602 0.8465 0.1577 0.0122 -0.1818 40 LYS A CA 307 C C . LYS A 40 ? 0.7376 1.1819 0.8601 0.1224 0.0157 -0.1805 40 LYS A C 308 O O . LYS A 40 ? 0.7222 1.1680 0.8577 0.1024 0.0165 -0.1741 40 LYS A O 309 C CB . LYS A 40 ? 0.7588 1.2187 0.8495 0.1879 0.0080 -0.1945 40 LYS A CB 310 C CG . LYS A 40 ? 0.8197 1.2430 0.8729 0.2298 0.0051 -0.1976 40 LYS A CG 311 C CD . LYS A 40 ? 0.8364 1.3159 0.8868 0.2635 -0.0001 -0.2091 40 LYS A CD 312 C CE . LYS A 40 ? 0.9124 1.3476 0.9168 0.3101 -0.0024 -0.2117 40 LYS A CE 313 N NZ . LYS A 40 ? 0.9515 1.4313 0.9483 0.3469 -0.0083 -0.2199 40 LYS A NZ 314 N N . LEU A 41 ? 0.7598 1.2309 0.8888 0.1155 0.0182 -0.1867 41 LEU A N 315 C CA . LEU A 41 ? 0.7470 1.2587 0.8981 0.0846 0.0222 -0.1881 41 LEU A CA 316 C C . LEU A 41 ? 0.7134 1.2999 0.8752 0.0910 0.0212 -0.2030 41 LEU A C 317 O O . LEU A 41 ? 0.7058 1.3207 0.8608 0.1174 0.0186 -0.2139 41 LEU A O 318 C CB . LEU A 41 ? 0.7573 1.2578 0.9086 0.0708 0.0260 -0.1865 41 LEU A CB 319 C CG . LEU A 41 ? 0.7922 1.2285 0.9327 0.0637 0.0272 -0.1738 41 LEU A CG 320 C CD1 . LEU A 41 ? 0.8068 1.2409 0.9476 0.0521 0.0306 -0.1741 41 LEU A CD1 321 C CD2 . LEU A 41 ? 0.7812 1.1957 0.9288 0.0427 0.0285 -0.1617 41 LEU A CD2 322 N N . CYS A 42 ? 0.6810 1.2997 0.8565 0.0667 0.0236 -0.2040 42 CYS A N 323 C CA . CYS A 42 ? 0.6749 1.3685 0.8597 0.0696 0.0228 -0.2188 42 CYS A CA 324 C C . CYS A 42 ? 0.6265 1.3607 0.8226 0.0306 0.0298 -0.2239 42 CYS A C 325 O O . CYS A 42 ? 0.5884 1.2843 0.7829 0.0022 0.0350 -0.2135 42 CYS A O 326 C CB . CYS A 42 ? 0.7131 1.4070 0.8971 0.0789 0.0192 -0.2171 42 CYS A CB 327 S SG . CYS A 42 ? 0.7617 1.3947 0.9249 0.1207 0.0123 -0.2092 42 CYS A SG 328 N N . ASP A 43 ? 0.6185 1.4312 0.8225 0.0298 0.0302 -0.2404 43 ASP A N 329 C CA . ASP A 43 ? 0.6079 1.4632 0.8175 -0.0113 0.0380 -0.2476 43 ASP A CA 330 C C . ASP A 43 ? 0.6023 1.4208 0.8075 -0.0345 0.0410 -0.2375 43 ASP A C 331 O O . ASP A 43 ? 0.5838 1.3896 0.7888 -0.0160 0.0358 -0.2340 43 ASP A O 332 C CB . ASP A 43 ? 0.6044 1.5586 0.8229 -0.0076 0.0374 -0.2688 43 ASP A CB 333 C CG . ASP A 43 ? 0.6075 1.6068 0.8293 0.0175 0.0347 -0.2806 43 ASP A CG 334 O OD1 . ASP A 43 ? 0.6118 1.5629 0.8281 0.0292 0.0338 -0.2725 43 ASP A OD1 335 O OD2 . ASP A 43 ? 0.6186 1.7050 0.8476 0.0262 0.0334 -0.2987 43 ASP A OD2 336 N N . LEU A 44 ? 0.6331 1.4294 0.8308 -0.0736 0.0497 -0.2325 44 LEU A N 337 C CA . LEU A 44 ? 0.6842 1.4487 0.8723 -0.0984 0.0543 -0.2249 44 LEU A CA 338 C C . LEU A 44 ? 0.7388 1.5713 0.9257 -0.1275 0.0605 -0.2415 44 LEU A C 339 O O . LEU A 44 ? 0.7419 1.5952 0.9204 -0.1598 0.0693 -0.2485 44 LEU A O 340 C CB . LEU A 44 ? 0.7037 1.3985 0.8762 -0.1219 0.0610 -0.2096 44 LEU A CB 341 C CG . LEU A 44 ? 0.7353 1.3810 0.8923 -0.1409 0.0654 -0.1987 44 LEU A CG 342 C CD1 . LEU A 44 ? 0.7352 1.3496 0.8994 -0.1123 0.0571 -0.1892 44 LEU A CD1 343 C CD2 . LEU A 44 ? 0.7458 1.3295 0.8821 -0.1611 0.0727 -0.1853 44 LEU A CD2 344 N N . ASP A 45 ? 0.7771 1.6473 0.9708 -0.1163 0.0563 -0.2487 45 ASP A N 345 C CA . ASP A 45 ? 0.7935 1.7304 0.9851 -0.1463 0.0624 -0.2650 45 ASP A CA 346 C C . ASP A 45 ? 0.7477 1.7688 0.9464 -0.1554 0.0653 -0.2845 45 ASP A C 347 O O . ASP A 45 ? 0.7332 1.7852 0.9208 -0.1986 0.0758 -0.2947 45 ASP A O 348 C CB . ASP A 45 ? 0.8686 1.7538 1.0365 -0.1919 0.0739 -0.2575 45 ASP A CB 349 C CG . ASP A 45 ? 0.9566 1.8693 1.1188 -0.2112 0.0770 -0.2651 45 ASP A CG 350 O OD1 . ASP A 45 ? 1.0072 2.0032 1.1721 -0.2311 0.0810 -0.2851 45 ASP A OD1 351 O OD2 . ASP A 45 ? 0.9778 1.8326 1.1330 -0.2065 0.0756 -0.2519 45 ASP A OD2 352 N N . GLY A 46 ? 0.7017 1.7562 0.9151 -0.1146 0.0565 -0.2895 46 GLY A N 353 C CA . GLY A 46 ? 0.6817 1.8205 0.9036 -0.1145 0.0576 -0.3083 46 GLY A CA 354 C C . GLY A 46 ? 0.6826 1.7946 0.9006 -0.1242 0.0618 -0.3043 46 GLY A C 355 O O . GLY A 46 ? 0.6956 1.8671 0.9223 -0.1105 0.0601 -0.3172 46 GLY A O 356 N N . VAL A 47 ? 0.6534 1.6788 0.8573 -0.1457 0.0672 -0.2868 47 VAL A N 357 C CA . VAL A 47 ? 0.6357 1.6331 0.8327 -0.1603 0.0724 -0.2824 47 VAL A CA 358 C C . VAL A 47 ? 0.6251 1.5615 0.8262 -0.1243 0.0649 -0.2675 47 VAL A C 359 O O . VAL A 47 ? 0.6198 1.4793 0.8133 -0.1214 0.0638 -0.2498 47 VAL A O 360 C CB . VAL A 47 ? 0.6484 1.5899 0.8208 -0.2071 0.0843 -0.2731 47 VAL A CB 361 C CG1 . VAL A 47 ? 0.6647 1.5798 0.8276 -0.2210 0.0897 -0.2688 47 VAL A CG1 362 C CG2 . VAL A 47 ? 0.6552 1.6485 0.8162 -0.2484 0.0937 -0.2882 47 VAL A CG2 363 N N . LYS A 48 ? 0.6168 1.5893 0.8277 -0.0986 0.0603 -0.2758 48 LYS A N 364 C CA . LYS A 48 ? 0.6260 1.5466 0.8375 -0.0649 0.0539 -0.2649 48 LYS A CA 365 C C . LYS A 48 ? 0.6312 1.4775 0.8324 -0.0843 0.0585 -0.2484 48 LYS A C 366 O O . LYS A 48 ? 0.6457 1.4950 0.8392 -0.1188 0.0669 -0.2495 48 LYS A O 367 C CB . LYS A 48 ? 0.6322 1.6086 0.8508 -0.0395 0.0505 -0.2790 48 LYS A CB 368 C CG . LYS A 48 ? 0.6634 1.5896 0.8774 -0.0015 0.0439 -0.2708 48 LYS A CG 369 C CD . LYS A 48 ? 0.6827 1.6549 0.8986 0.0215 0.0420 -0.2839 48 LYS A CD 370 C CE . LYS A 48 ? 0.7195 1.6246 0.9239 0.0489 0.0383 -0.2737 48 LYS A CE 371 N NZ . LYS A 48 ? 0.7738 1.7148 0.9735 0.0835 0.0350 -0.2864 48 LYS A NZ 372 N N . PRO A 49 ? 0.6197 1.4000 0.8179 -0.0622 0.0534 -0.2337 49 PRO A N 373 C CA . PRO A 49 ? 0.6108 1.3311 0.8004 -0.0765 0.0569 -0.2194 49 PRO A CA 374 C C . PRO A 49 ? 0.5997 1.3331 0.7908 -0.0725 0.0578 -0.2241 49 PRO A C 375 O O . PRO A 49 ? 0.5913 1.3663 0.7891 -0.0495 0.0539 -0.2361 49 PRO A O 376 C CB . PRO A 49 ? 0.5942 1.2540 0.7813 -0.0531 0.0509 -0.2056 49 PRO A CB 377 C CG . PRO A 49 ? 0.6047 1.2905 0.7966 -0.0186 0.0437 -0.2145 49 PRO A CG 378 C CD . PRO A 49 ? 0.6130 1.3700 0.8122 -0.0259 0.0450 -0.2295 49 PRO A CD 379 N N . LEU A 50 ? 0.6037 1.3009 0.7864 -0.0929 0.0629 -0.2146 50 LEU A N 380 C CA . LEU A 50 ? 0.6036 1.2990 0.7865 -0.0880 0.0632 -0.2156 50 LEU A CA 381 C C . LEU A 50 ? 0.5982 1.2435 0.7798 -0.0627 0.0572 -0.2054 50 LEU A C 382 O O . LEU A 50 ? 0.6177 1.2122 0.7928 -0.0685 0.0575 -0.1911 50 LEU A O 383 C CB . LEU A 50 ? 0.6200 1.2958 0.7909 -0.1197 0.0712 -0.2091 50 LEU A CB 384 C CG . LEU A 50 ? 0.6239 1.2915 0.7936 -0.1180 0.0720 -0.2076 50 LEU A CG 385 C CD1 . LEU A 50 ? 0.6184 1.3435 0.7988 -0.1049 0.0702 -0.2244 50 LEU A CD1 386 C CD2 . LEU A 50 ? 0.6432 1.2923 0.7965 -0.1492 0.0805 -0.2014 50 LEU A CD2 387 N N . ILE A 51 ? 0.6028 1.2619 0.7868 -0.0349 0.0524 -0.2134 51 ILE A N 388 C CA . ILE A 51 ? 0.6125 1.2217 0.7888 -0.0135 0.0482 -0.2058 51 ILE A CA 389 C C . ILE A 51 ? 0.6097 1.2115 0.7821 -0.0142 0.0500 -0.2069 51 ILE A C 390 O O . ILE A 51 ? 0.6119 1.2409 0.7830 0.0023 0.0489 -0.2184 51 ILE A O 391 C CB . ILE A 51 ? 0.6297 1.2432 0.8013 0.0202 0.0424 -0.2127 51 ILE A CB 392 C CG1 . ILE A 51 ? 0.6468 1.2633 0.8223 0.0189 0.0406 -0.2098 51 ILE A CG1 393 C CG2 . ILE A 51 ? 0.6465 1.2030 0.8019 0.0392 0.0399 -0.2065 51 ILE A CG2 394 C CD1 . ILE A 51 ? 0.6785 1.2987 0.8470 0.0528 0.0348 -0.2155 51 ILE A CD1 395 N N . LEU A 52 ? 0.6114 1.1775 0.7804 -0.0318 0.0526 -0.1951 52 LEU A N 396 C CA . LEU A 52 ? 0.6139 1.1753 0.7798 -0.0373 0.0549 -0.1952 52 LEU A CA 397 C C . LEU A 52 ? 0.6356 1.1735 0.7915 -0.0148 0.0520 -0.1984 52 LEU A C 398 O O . LEU A 52 ? 0.6251 1.1660 0.7775 -0.0159 0.0538 -0.2021 52 LEU A O 399 C CB . LEU A 52 ? 0.6046 1.1351 0.7670 -0.0584 0.0580 -0.1813 52 LEU A CB 400 C CG . LEU A 52 ? 0.6108 1.1524 0.7724 -0.0824 0.0630 -0.1774 52 LEU A CG 401 C CD1 . LEU A 52 ? 0.6168 1.1192 0.7688 -0.0942 0.0650 -0.1620 52 LEU A CD1 402 C CD2 . LEU A 52 ? 0.6163 1.1992 0.7791 -0.0963 0.0677 -0.1877 52 LEU A CD2 403 N N . ARG A 53 ? 0.6775 1.1879 0.8249 0.0041 0.0483 -0.1970 53 ARG A N 404 C CA . ARG A 53 ? 0.7505 1.2286 0.8788 0.0254 0.0468 -0.2005 53 ARG A CA 405 C C . ARG A 53 ? 0.7630 1.2065 0.8830 0.0113 0.0494 -0.1938 53 ARG A C 406 O O . ARG A 53 ? 0.7882 1.2046 0.9086 -0.0022 0.0496 -0.1827 53 ARG A O 407 C CB . ARG A 53 ? 0.8155 1.3278 0.9389 0.0475 0.0461 -0.2155 53 ARG A CB 408 C CG . ARG A 53 ? 0.9236 1.3974 1.0182 0.0763 0.0450 -0.2206 53 ARG A CG 409 C CD . ARG A 53 ? 0.9883 1.4972 1.0765 0.0974 0.0452 -0.2350 53 ARG A CD 410 N NE . ARG A 53 ? 1.0274 1.6038 1.1345 0.1044 0.0430 -0.2439 53 ARG A NE 411 C CZ . ARG A 53 ? 1.0585 1.6527 1.1587 0.1331 0.0392 -0.2505 53 ARG A CZ 412 N NH1 . ARG A 53 ? 1.1192 1.6613 1.1902 0.1604 0.0371 -0.2487 53 ARG A NH1 413 N NH2 . ARG A 53 ? 1.0453 1.7109 1.1652 0.1337 0.0379 -0.2598 53 ARG A NH2 414 N N . ASP A 54 ? 0.7591 1.2082 0.8719 0.0142 0.0515 -0.2010 54 ASP A N 415 C CA . ASP A 54 ? 0.7657 1.1882 0.8698 0.0004 0.0542 -0.1966 54 ASP A CA 416 C C . ASP A 54 ? 0.7384 1.1871 0.8591 -0.0232 0.0566 -0.1916 54 ASP A C 417 O O . ASP A 54 ? 0.7650 1.1997 0.8809 -0.0353 0.0586 -0.1877 54 ASP A O 418 C CB . ASP A 54 ? 0.8106 1.2188 0.8931 0.0152 0.0559 -0.2071 54 ASP A CB 419 C CG . ASP A 54 ? 0.8585 1.2210 0.9115 0.0377 0.0551 -0.2102 54 ASP A CG 420 O OD1 . ASP A 54 ? 0.8509 1.1784 0.8963 0.0323 0.0546 -0.2023 54 ASP A OD1 421 O OD2 . ASP A 54 ? 0.8890 1.2491 0.9231 0.0617 0.0554 -0.2209 54 ASP A OD2 422 N N . CYS A 55 ? 0.7256 1.2113 0.8620 -0.0306 0.0570 -0.1922 55 CYS A N 423 C CA . CYS A 55 ? 0.7350 1.2366 0.8795 -0.0528 0.0603 -0.1864 55 CYS A CA 424 C C . CYS A 55 ? 0.7031 1.1861 0.8495 -0.0650 0.0603 -0.1728 55 CYS A C 425 O O . CYS A 55 ? 0.7270 1.1974 0.8742 -0.0587 0.0579 -0.1695 55 CYS A O 426 C CB . CYS A 55 ? 0.7326 1.2801 0.8859 -0.0590 0.0627 -0.1951 55 CYS A CB 427 S SG . CYS A 55 ? 0.8114 1.3876 0.9622 -0.0442 0.0631 -0.2113 55 CYS A SG 428 N N . SER A 56 ? 0.6922 1.1729 0.8369 -0.0804 0.0629 -0.1648 56 SER A N 429 C CA . SER A 56 ? 0.6706 1.1357 0.8124 -0.0899 0.0638 -0.1518 56 SER A CA 430 C C . SER A 56 ? 0.6658 1.1473 0.8048 -0.1043 0.0684 -0.1514 56 SER A C 431 O O . SER A 56 ? 0.6446 1.1541 0.7863 -0.1093 0.0708 -0.1612 56 SER A O 432 C CB . SER A 56 ? 0.6683 1.1189 0.8038 -0.0944 0.0639 -0.1429 56 SER A CB 433 O OG . SER A 56 ? 0.6639 1.1289 0.7954 -0.1046 0.0674 -0.1426 56 SER A OG 434 N N . VAL A 57 ? 0.6711 1.1333 0.8007 -0.1118 0.0703 -0.1403 57 VAL A N 435 C CA . VAL A 57 ? 0.6980 1.1643 0.8155 -0.1285 0.0764 -0.1394 57 VAL A CA 436 C C . VAL A 57 ? 0.6952 1.1700 0.8033 -0.1391 0.0806 -0.1397 57 VAL A C 437 O O . VAL A 57 ? 0.6964 1.1880 0.7977 -0.1542 0.0860 -0.1460 57 VAL A O 438 C CB . VAL A 57 ? 0.7258 1.1591 0.8271 -0.1321 0.0783 -0.1265 57 VAL A CB 439 C CG1 . VAL A 57 ? 0.7537 1.1804 0.8322 -0.1521 0.0866 -0.1253 57 VAL A CG1 440 C CG2 . VAL A 57 ? 0.7255 1.1539 0.8366 -0.1235 0.0745 -0.1273 57 VAL A CG2 441 N N . ALA A 58 ? 0.6869 1.1528 0.7939 -0.1327 0.0785 -0.1338 58 ALA A N 442 C CA . ALA A 58 ? 0.6829 1.1581 0.7820 -0.1403 0.0817 -0.1342 58 ALA A CA 443 C C . ALA A 58 ? 0.6796 1.1883 0.7924 -0.1415 0.0817 -0.1492 58 ALA A C 444 O O . ALA A 58 ? 0.6916 1.2182 0.7986 -0.1546 0.0867 -0.1548 58 ALA A O 445 C CB . ALA A 58 ? 0.6708 1.1352 0.7670 -0.1322 0.0789 -0.1256 58 ALA A CB 446 N N . GLY A 59 ? 0.6533 1.1684 0.7804 -0.1275 0.0768 -0.1559 59 GLY A N 447 C CA . GLY A 59 ? 0.6511 1.1945 0.7876 -0.1228 0.0764 -0.1705 59 GLY A CA 448 C C . GLY A 59 ? 0.6691 1.2431 0.8090 -0.1298 0.0794 -0.1803 59 GLY A C 449 O O . GLY A 59 ? 0.7275 1.3322 0.8697 -0.1350 0.0821 -0.1904 59 GLY A O 450 N N . TRP A 60 ? 0.6639 1.2330 0.8039 -0.1313 0.0793 -0.1780 60 TRP A N 451 C CA . TRP A 60 ? 0.6522 1.2556 0.7949 -0.1407 0.0825 -0.1884 60 TRP A CA 452 C C . TRP A 60 ? 0.6829 1.2935 0.8106 -0.1670 0.0905 -0.1877 60 TRP A C 453 O O . TRP A 60 ? 0.6967 1.3473 0.8270 -0.1767 0.0940 -0.2001 60 TRP A O 454 C CB . TRP A 60 ? 0.6426 1.2365 0.7867 -0.1378 0.0807 -0.1856 60 TRP A CB 455 C CG . TRP A 60 ? 0.6316 1.2559 0.7724 -0.1560 0.0859 -0.1937 60 TRP A CG 456 C CD1 . TRP A 60 ? 0.6236 1.3005 0.7701 -0.1638 0.0888 -0.2093 60 TRP A CD1 457 C CD2 . TRP A 60 ? 0.6218 1.2281 0.7509 -0.1704 0.0894 -0.1879 60 TRP A CD2 458 N NE1 . TRP A 60 ? 0.6353 1.3309 0.7745 -0.1850 0.0943 -0.2141 60 TRP A NE1 459 C CE2 . TRP A 60 ? 0.6272 1.2768 0.7543 -0.1898 0.0949 -0.2010 60 TRP A CE2 460 C CE3 . TRP A 60 ? 0.6209 1.1802 0.7394 -0.1692 0.0887 -0.1735 60 TRP A CE3 461 C CZ2 . TRP A 60 ? 0.6427 1.2858 0.7553 -0.2105 0.1005 -0.2002 60 TRP A CZ2 462 C CZ3 . TRP A 60 ? 0.6253 1.1754 0.7296 -0.1864 0.0938 -0.1719 60 TRP A CZ3 463 C CH2 . TRP A 60 ? 0.6498 1.2395 0.7501 -0.2080 0.0999 -0.1853 60 TRP A CH2 464 N N . LEU A 61 ? 0.7011 1.2719 0.8095 -0.1777 0.0938 -0.1735 61 LEU A N 465 C CA . LEU A 61 ? 0.7272 1.2910 0.8108 -0.2034 0.1029 -0.1713 61 LEU A CA 466 C C . LEU A 61 ? 0.7274 1.3020 0.8051 -0.2106 0.1060 -0.1735 61 LEU A C 467 O O . LEU A 61 ? 0.7377 1.3351 0.8056 -0.2312 0.1129 -0.1819 61 LEU A O 468 C CB . LEU A 61 ? 0.7435 1.2543 0.8007 -0.2078 0.1059 -0.1548 61 LEU A CB 469 C CG . LEU A 61 ? 0.7474 1.2467 0.8037 -0.2084 0.1055 -0.1536 61 LEU A CG 470 C CD1 . LEU A 61 ? 0.7853 1.2290 0.8144 -0.2069 0.1076 -0.1365 61 LEU A CD1 471 C CD2 . LEU A 61 ? 0.7587 1.2860 0.8080 -0.2326 0.1126 -0.1661 61 LEU A CD2 472 N N . LEU A 62 ? 0.7173 1.2782 0.8003 -0.1954 0.1013 -0.1667 62 LEU A N 473 C CA . LEU A 62 ? 0.7107 1.2848 0.7912 -0.1996 0.1032 -0.1694 62 LEU A CA 474 C C . LEU A 62 ? 0.7221 1.3451 0.8229 -0.1971 0.1020 -0.1869 62 LEU A C 475 O O . LEU A 62 ? 0.7375 1.3804 0.8350 -0.2065 0.1056 -0.1926 62 LEU A O 476 C CB . LEU A 62 ? 0.6902 1.2434 0.7723 -0.1844 0.0982 -0.1594 62 LEU A CB 477 C CG . LEU A 62 ? 0.6920 1.2043 0.7502 -0.1841 0.0998 -0.1423 62 LEU A CG 478 C CD1 . LEU A 62 ? 0.6740 1.1788 0.7405 -0.1671 0.0934 -0.1353 62 LEU A CD1 479 C CD2 . LEU A 62 ? 0.7238 1.2238 0.7521 -0.2002 0.1076 -0.1376 62 LEU A CD2 480 N N . GLY A 63 ? 0.7279 1.3702 0.8476 -0.1823 0.0971 -0.1955 63 GLY A N 481 C CA . GLY A 63 ? 0.7219 1.4113 0.8574 -0.1739 0.0956 -0.2126 63 GLY A CA 482 C C . GLY A 63 ? 0.7053 1.3912 0.8484 -0.1547 0.0910 -0.2150 63 GLY A C 483 O O . GLY A 63 ? 0.6676 1.3819 0.8136 -0.1550 0.0925 -0.2249 63 GLY A O 484 N N . ASN A 64 ? 0.6907 1.3410 0.8346 -0.1399 0.0860 -0.2065 64 ASN A N 485 C CA . ASN A 64 ? 0.6861 1.3270 0.8323 -0.1228 0.0822 -0.2100 64 ASN A CA 486 C C . ASN A 64 ? 0.6985 1.3716 0.8510 -0.1061 0.0809 -0.2265 64 ASN A C 487 O O . ASN A 64 ? 0.7068 1.3921 0.8641 -0.0957 0.0788 -0.2314 64 ASN A O 488 C CB . ASN A 64 ? 0.6731 1.2742 0.8170 -0.1119 0.0779 -0.2007 64 ASN A CB 489 C CG . ASN A 64 ? 0.6556 1.2394 0.7948 -0.0981 0.0755 -0.2050 64 ASN A CG 490 O OD1 . ASN A 64 ? 0.6495 1.2476 0.7873 -0.0864 0.0755 -0.2172 64 ASN A OD1 491 N ND2 . ASN A 64 ? 0.6502 1.2024 0.7836 -0.0995 0.0739 -0.1956 64 ASN A ND2 492 N N . PRO A 65 ? 0.7322 1.4207 0.8830 -0.1017 0.0820 -0.2354 65 PRO A N 493 C CA . PRO A 65 ? 0.7409 1.4657 0.8946 -0.0835 0.0813 -0.2520 65 PRO A CA 494 C C . PRO A 65 ? 0.7657 1.4731 0.9140 -0.0541 0.0766 -0.2566 65 PRO A C 495 O O . PRO A 65 ? 0.7845 1.5251 0.9335 -0.0347 0.0755 -0.2698 65 PRO A O 496 C CB . PRO A 65 ? 0.7631 1.4927 0.9115 -0.0840 0.0834 -0.2576 65 PRO A CB 497 C CG . PRO A 65 ? 0.7658 1.4542 0.9076 -0.0966 0.0838 -0.2442 65 PRO A CG 498 C CD . PRO A 65 ? 0.7493 1.4245 0.8941 -0.1120 0.0840 -0.2308 65 PRO A CD 499 N N . MET A 66 ? 0.7937 1.4511 0.9342 -0.0504 0.0742 -0.2461 66 MET A N 500 C CA . MET A 66 ? 0.8249 1.4573 0.9561 -0.0260 0.0704 -0.2479 66 MET A CA 501 C C . MET A 66 ? 0.7886 1.4371 0.9306 -0.0251 0.0682 -0.2456 66 MET A C 502 O O . MET A 66 ? 0.7778 1.4089 0.9126 -0.0046 0.0649 -0.2468 66 MET A O 503 C CB . MET A 66 ? 0.8658 1.4396 0.9827 -0.0275 0.0697 -0.2380 66 MET A CB 504 C CG . MET A 66 ? 0.9005 1.4518 1.0007 -0.0269 0.0722 -0.2419 66 MET A CG 505 S SD . MET A 66 ? 0.9755 1.4986 1.0457 0.0071 0.0720 -0.2549 66 MET A SD 506 C CE . MET A 66 ? 1.0200 1.5053 1.0672 -0.0041 0.0765 -0.2562 66 MET A CE 507 N N . CYS A 67 ? 0.7731 1.4509 0.9283 -0.0480 0.0708 -0.2426 67 CYS A N 508 C CA . CYS A 67 ? 0.7738 1.4630 0.9367 -0.0535 0.0699 -0.2395 67 CYS A CA 509 C C . CYS A 67 ? 0.7740 1.5265 0.9465 -0.0616 0.0727 -0.2519 67 CYS A C 510 O O . CYS A 67 ? 0.7675 1.5333 0.9437 -0.0839 0.0758 -0.2488 67 CYS A O 511 C CB . CYS A 67 ? 0.7700 1.4268 0.9319 -0.0769 0.0719 -0.2234 67 CYS A CB 512 S SG . CYS A 67 ? 0.7958 1.3906 0.9484 -0.0695 0.0687 -0.2102 67 CYS A SG 513 N N . ASP A 68 ? 0.7699 1.5616 0.9433 -0.0437 0.0720 -0.2669 68 ASP A N 514 C CA . ASP A 68 ? 0.7534 1.6166 0.9363 -0.0504 0.0746 -0.2815 68 ASP A CA 515 C C . ASP A 68 ? 0.7533 1.6480 0.9422 -0.0397 0.0718 -0.2876 68 ASP A C 516 O O . ASP A 68 ? 0.7607 1.7134 0.9576 -0.0562 0.0751 -0.2974 68 ASP A O 517 C CB . ASP A 68 ? 0.7606 1.6606 0.9419 -0.0308 0.0744 -0.2963 68 ASP A CB 518 C CG . ASP A 68 ? 0.7646 1.6515 0.9426 -0.0485 0.0785 -0.2932 68 ASP A CG 519 O OD1 . ASP A 68 ? 0.7761 1.6194 0.9509 -0.0705 0.0806 -0.2786 68 ASP A OD1 520 O OD2 . ASP A 68 ? 0.7596 1.6815 0.9371 -0.0388 0.0796 -0.3055 68 ASP A OD2 521 N N . GLU A 69 ? 0.7603 1.6183 0.9436 -0.0143 0.0664 -0.2825 69 GLU A N 522 C CA . GLU A 69 ? 0.7542 1.6368 0.9424 -0.0037 0.0633 -0.2863 69 GLU A CA 523 C C . GLU A 69 ? 0.7274 1.6223 0.9233 -0.0406 0.0678 -0.2814 69 GLU A C 524 O O . GLU A 69 ? 0.7299 1.6757 0.9328 -0.0445 0.0682 -0.2907 69 GLU A O 525 C CB . GLU A 69 ? 0.7738 1.5976 0.9510 0.0222 0.0578 -0.2771 69 GLU A CB 526 C CG . GLU A 69 ? 0.7721 1.6216 0.9525 0.0390 0.0538 -0.2818 69 GLU A CG 527 C CD . GLU A 69 ? 0.7826 1.5683 0.9500 0.0594 0.0493 -0.2711 69 GLU A CD 528 O OE1 . GLU A 69 ? 0.7843 1.5094 0.9371 0.0657 0.0491 -0.2630 69 GLU A OE1 529 O OE2 . GLU A 69 ? 0.8040 1.6019 0.9744 0.0676 0.0464 -0.2717 69 GLU A OE2 530 N N . PHE A 70 ? 0.7080 1.5562 0.8990 -0.0670 0.0716 -0.2672 70 PHE A N 531 C CA . PHE A 70 ? 0.6999 1.5408 0.8885 -0.1006 0.0769 -0.2600 70 PHE A CA 532 C C . PHE A 70 ? 0.7088 1.5735 0.8923 -0.1338 0.0852 -0.2637 70 PHE A C 533 O O . PHE A 70 ? 0.6708 1.5052 0.8419 -0.1623 0.0910 -0.2537 70 PHE A O 534 C CB . PHE A 70 ? 0.6879 1.4556 0.8687 -0.1026 0.0754 -0.2406 70 PHE A CB 535 C CG . PHE A 70 ? 0.6808 1.4180 0.8627 -0.0710 0.0680 -0.2368 70 PHE A CG 536 C CD1 . PHE A 70 ? 0.6658 1.4153 0.8516 -0.0580 0.0645 -0.2400 70 PHE A CD1 537 C CD2 . PHE A 70 ? 0.6787 1.3757 0.8547 -0.0556 0.0652 -0.2312 70 PHE A CD2 538 C CE1 . PHE A 70 ? 0.6632 1.3802 0.8451 -0.0293 0.0584 -0.2365 70 PHE A CE1 539 C CE2 . PHE A 70 ? 0.6777 1.3418 0.8482 -0.0299 0.0599 -0.2285 70 PHE A CE2 540 C CZ . PHE A 70 ? 0.6605 1.3324 0.8330 -0.0160 0.0565 -0.2308 70 PHE A CZ 541 N N . ILE A 71 ? 0.7458 1.6634 0.9352 -0.1290 0.0861 -0.2784 71 ILE A N 542 C CA . ILE A 71 ? 0.7809 1.7266 0.9644 -0.1605 0.0943 -0.2841 71 ILE A CA 543 C C . ILE A 71 ? 0.8033 1.7776 0.9796 -0.1956 0.1019 -0.2892 71 ILE A C 544 O O . ILE A 71 ? 0.8060 1.7610 0.9647 -0.2298 0.1104 -0.2843 71 ILE A O 545 C CB . ILE A 71 ? 0.7919 1.7976 0.9845 -0.1461 0.0936 -0.3012 71 ILE A CB 546 C CG1 . ILE A 71 ? 0.8034 1.8218 0.9878 -0.1774 0.1017 -0.3035 71 ILE A CG1 547 C CG2 . ILE A 71 ? 0.7896 1.8750 0.9938 -0.1333 0.0917 -0.3204 71 ILE A CG2 548 C CD1 . ILE A 71 ? 0.7909 1.7571 0.9692 -0.1717 0.1008 -0.2918 71 ILE A CD1 549 N N . ASN A 72 ? 0.8046 1.8213 0.9902 -0.1873 0.0993 -0.2991 72 ASN A N 550 C CA . ASN A 72 ? 0.8292 1.8696 1.0059 -0.2215 0.1065 -0.3042 72 ASN A CA 551 C C . ASN A 72 ? 0.8083 1.8546 0.9937 -0.2036 0.1007 -0.3045 72 ASN A C 552 O O . ASN A 72 ? 0.8436 1.9572 1.0437 -0.1843 0.0964 -0.3199 72 ASN A O 553 C CB . ASN A 72 ? 0.8633 1.9900 1.0418 -0.2447 0.1133 -0.3255 72 ASN A CB 554 C CG . ASN A 72 ? 0.9171 2.0269 1.0761 -0.2812 0.1235 -0.3233 72 ASN A CG 555 O OD1 . ASN A 72 ? 0.9472 1.9960 1.0811 -0.3100 0.1306 -0.3102 72 ASN A OD1 556 N ND2 . ASN A 72 ? 0.9357 2.0966 1.1028 -0.2781 0.1243 -0.3359 72 ASN A ND2 557 N N . VAL A 73 ? 0.7732 1.7501 0.9484 -0.2078 0.1003 -0.2873 73 VAL A N 558 C CA . VAL A 73 ? 0.7372 1.7093 0.9193 -0.1907 0.0947 -0.2852 73 VAL A CA 559 C C . VAL A 73 ? 0.7152 1.7063 0.8855 -0.2268 0.1025 -0.2902 73 VAL A C 560 O O . VAL A 73 ? 0.7199 1.6768 0.8669 -0.2635 0.1122 -0.2841 73 VAL A O 561 C CB . VAL A 73 ? 0.7394 1.6273 0.9177 -0.1721 0.0892 -0.2643 73 VAL A CB 562 C CG1 . VAL A 73 ? 0.7214 1.5875 0.9067 -0.1413 0.0828 -0.2602 73 VAL A CG1 563 C CG2 . VAL A 73 ? 0.7498 1.5744 0.9055 -0.2024 0.0965 -0.2487 73 VAL A CG2 564 N N . PRO A 74 ? 0.6884 1.7312 0.8707 -0.2161 0.0988 -0.3014 74 PRO A N 565 C CA . PRO A 74 ? 0.7038 1.7681 0.8746 -0.2509 0.1062 -0.3077 74 PRO A CA 566 C C . PRO A 74 ? 0.7031 1.6851 0.8579 -0.2589 0.1074 -0.2889 74 PRO A C 567 O O . PRO A 74 ? 0.6842 1.5975 0.8384 -0.2378 0.1023 -0.2714 74 PRO A O 568 C CB . PRO A 74 ? 0.6935 1.8409 0.8857 -0.2266 0.0994 -0.3248 74 PRO A CB 569 C CG . PRO A 74 ? 0.6763 1.7974 0.8832 -0.1735 0.0870 -0.3169 74 PRO A CG 570 C CD . PRO A 74 ? 0.6722 1.7510 0.8752 -0.1691 0.0876 -0.3083 74 PRO A CD 571 N N . GLU A 75 ? 0.7182 1.7105 0.8586 -0.2903 0.1146 -0.2938 75 GLU A N 572 C CA . GLU A 75 ? 0.7406 1.6602 0.8629 -0.2988 0.1166 -0.2781 75 GLU A CA 573 C C . GLU A 75 ? 0.7216 1.6159 0.8644 -0.2546 0.1039 -0.2678 75 GLU A C 574 O O . GLU A 75 ? 0.6972 1.6468 0.8633 -0.2259 0.0955 -0.2782 75 GLU A O 575 C CB . GLU A 75 ? 0.7698 1.7205 0.8754 -0.3372 0.1258 -0.2897 75 GLU A CB 576 C CG . GLU A 75 ? 0.7938 1.6721 0.8777 -0.3469 0.1287 -0.2751 75 GLU A CG 577 C CD . GLU A 75 ? 0.8167 1.7249 0.8805 -0.3879 0.1389 -0.2879 75 GLU A CD 578 O OE1 . GLU A 75 ? 0.8376 1.8232 0.9015 -0.4148 0.1452 -0.3085 75 GLU A OE1 579 O OE2 . GLU A 75 ? 0.8303 1.6861 0.8769 -0.3944 0.1410 -0.2781 75 GLU A OE2 580 N N . TRP A 76 ? 0.7283 1.5393 0.8591 -0.2486 0.1028 -0.2477 76 TRP A N 581 C CA . TRP A 76 ? 0.7246 1.5044 0.8704 -0.2115 0.0921 -0.2370 76 TRP A CA 582 C C . TRP A 76 ? 0.7426 1.4729 0.8732 -0.2222 0.0944 -0.2260 76 TRP A C 583 O O . TRP A 76 ? 0.8056 1.5057 0.9085 -0.2559 0.1047 -0.2225 76 TRP A O 584 C CB . TRP A 76 ? 0.7058 1.4369 0.8556 -0.1875 0.0868 -0.2235 76 TRP A CB 585 C CG . TRP A 76 ? 0.7227 1.3874 0.8483 -0.2065 0.0933 -0.2080 76 TRP A CG 586 C CD1 . TRP A 76 ? 0.7327 1.3335 0.8449 -0.2046 0.0932 -0.1915 76 TRP A CD1 587 C CD2 . TRP A 76 ? 0.7242 1.3813 0.8335 -0.2279 0.1008 -0.2076 76 TRP A CD2 588 N NE1 . TRP A 76 ? 0.7481 1.3026 0.8351 -0.2207 0.1000 -0.1809 76 TRP A NE1 589 C CE2 . TRP A 76 ? 0.7326 1.3183 0.8167 -0.2357 0.1049 -0.1901 76 TRP A CE2 590 C CE3 . TRP A 76 ? 0.7110 1.4157 0.8231 -0.2400 0.1046 -0.2206 76 TRP A CE3 591 C CZ2 . TRP A 76 ? 0.7512 1.3088 0.8107 -0.2537 0.1125 -0.1847 76 TRP A CZ2 592 C CZ3 . TRP A 76 ? 0.7200 1.3965 0.8096 -0.2609 0.1123 -0.2152 76 TRP A CZ3 593 C CH2 . TRP A 76 ? 0.7430 1.3451 0.8055 -0.2671 0.1162 -0.1972 76 TRP A CH2 594 N N . SER A 77 ? 0.7136 1.4322 0.8585 -0.1930 0.0855 -0.2207 77 SER A N 595 C CA . SER A 77 ? 0.7169 1.3882 0.8505 -0.1972 0.0861 -0.2096 77 SER A CA 596 C C . SER A 77 ? 0.7050 1.3008 0.8306 -0.1841 0.0838 -0.1895 77 SER A C 597 O O . SER A 77 ? 0.7386 1.2828 0.8402 -0.2013 0.0901 -0.1784 77 SER A O 598 C CB . SER A 77 ? 0.7045 1.4063 0.8571 -0.1720 0.0776 -0.2149 77 SER A CB 599 O OG . SER A 77 ? 0.6980 1.4110 0.8693 -0.1344 0.0679 -0.2157 77 SER A OG 600 N N . TYR A 78 ? 0.6521 1.2429 0.7949 -0.1533 0.0753 -0.1858 78 TYR A N 601 C CA . TYR A 78 ? 0.6233 1.1562 0.7609 -0.1420 0.0731 -0.1696 78 TYR A CA 602 C C . TYR A 78 ? 0.6104 1.1563 0.7590 -0.1265 0.0694 -0.1726 78 TYR A C 603 O O . TYR A 78 ? 0.5995 1.1952 0.7599 -0.1195 0.0676 -0.1863 78 TYR A O 604 C CB . TYR A 78 ? 0.5946 1.0941 0.7373 -0.1213 0.0666 -0.1598 78 TYR A CB 605 C CG . TYR A 78 ? 0.5560 1.0829 0.7169 -0.0937 0.0581 -0.1674 78 TYR A CG 606 C CD1 . TYR A 78 ? 0.5507 1.1200 0.7183 -0.0919 0.0568 -0.1787 78 TYR A CD1 607 C CD2 . TYR A 78 ? 0.5414 1.0499 0.7083 -0.0693 0.0521 -0.1637 78 TYR A CD2 608 C CE1 . TYR A 78 ? 0.5369 1.1280 0.7157 -0.0621 0.0491 -0.1851 78 TYR A CE1 609 C CE2 . TYR A 78 ? 0.5301 1.0531 0.7043 -0.0425 0.0455 -0.1702 78 TYR A CE2 610 C CZ . TYR A 78 ? 0.5265 1.0898 0.7061 -0.0369 0.0437 -0.1804 78 TYR A CZ 611 O OH . TYR A 78 ? 0.5255 1.0998 0.7072 -0.0059 0.0371 -0.1862 78 TYR A OH 612 N N . ILE A 79 ? 0.6164 1.1201 0.7596 -0.1210 0.0686 -0.1602 79 ILE A N 613 C CA . ILE A 79 ? 0.6205 1.1299 0.7709 -0.1088 0.0658 -0.1621 79 ILE A CA 614 C C . ILE A 79 ? 0.6191 1.0983 0.7752 -0.0850 0.0589 -0.1547 79 ILE A C 615 O O . ILE A 79 ? 0.6043 1.0481 0.7552 -0.0836 0.0579 -0.1435 79 ILE A O 616 C CB . ILE A 79 ? 0.6505 1.1402 0.7866 -0.1257 0.0717 -0.1551 79 ILE A CB 617 C CG1 . ILE A 79 ? 0.6770 1.1922 0.8014 -0.1528 0.0801 -0.1632 79 ILE A CG1 618 C CG2 . ILE A 79 ? 0.6583 1.1522 0.8018 -0.1137 0.0688 -0.1565 79 ILE A CG2 619 C CD1 . ILE A 79 ? 0.7103 1.1939 0.8111 -0.1706 0.0872 -0.1543 79 ILE A CD1 620 N N . VAL A 80 ? 0.6313 1.1230 0.7945 -0.0673 0.0549 -0.1616 80 VAL A N 621 C CA . VAL A 80 ? 0.6449 1.1041 0.8068 -0.0485 0.0500 -0.1562 80 VAL A CA 622 C C . VAL A 80 ? 0.6483 1.0996 0.8072 -0.0467 0.0504 -0.1563 80 VAL A C 623 O O . VAL A 80 ? 0.6500 1.1281 0.8112 -0.0424 0.0509 -0.1665 80 VAL A O 624 C CB . VAL A 80 ? 0.6526 1.1210 0.8164 -0.0249 0.0450 -0.1644 80 VAL A CB 625 C CG1 . VAL A 80 ? 0.6564 1.0826 0.8108 -0.0095 0.0417 -0.1592 80 VAL A CG1 626 C CG2 . VAL A 80 ? 0.6501 1.1301 0.8177 -0.0266 0.0442 -0.1648 80 VAL A CG2 627 N N . GLU A 81 ? 0.6424 1.0604 0.7959 -0.0499 0.0503 -0.1455 81 GLU A N 628 C CA . GLU A 81 ? 0.6654 1.0760 0.8150 -0.0518 0.0512 -0.1447 81 GLU A CA 629 C C . GLU A 81 ? 0.6693 1.0482 0.8117 -0.0428 0.0485 -0.1410 81 GLU A C 630 O O . GLU A 81 ? 0.6838 1.0432 0.8249 -0.0425 0.0471 -0.1334 81 GLU A O 631 C CB . GLU A 81 ? 0.6897 1.0970 0.8360 -0.0684 0.0548 -0.1354 81 GLU A CB 632 C CG . GLU A 81 ? 0.7218 1.1299 0.8649 -0.0722 0.0561 -0.1350 81 GLU A CG 633 C CD . GLU A 81 ? 0.7421 1.1425 0.8778 -0.0831 0.0588 -0.1238 81 GLU A CD 634 O OE1 . GLU A 81 ? 0.7237 1.1060 0.8546 -0.0825 0.0583 -0.1139 81 GLU A OE1 635 O OE2 . GLU A 81 ? 0.7856 1.1978 0.9180 -0.0904 0.0616 -0.1248 81 GLU A OE2 636 N N . LYS A 82 ? 0.6999 1.0723 0.8349 -0.0371 0.0485 -0.1470 82 LYS A N 637 C CA . LYS A 82 ? 0.7191 1.0582 0.8411 -0.0340 0.0477 -0.1448 82 LYS A CA 638 C C . LYS A 82 ? 0.7131 1.0463 0.8359 -0.0489 0.0489 -0.1348 82 LYS A C 639 O O . LYS A 82 ? 0.6922 1.0433 0.8222 -0.0582 0.0504 -0.1297 82 LYS A O 640 C CB . LYS A 82 ? 0.7391 1.0675 0.8460 -0.0259 0.0489 -0.1547 82 LYS A CB 641 C CG . LYS A 82 ? 0.7591 1.0854 0.8574 -0.0038 0.0471 -0.1642 82 LYS A CG 642 C CD . LYS A 82 ? 0.7967 1.1027 0.8719 0.0068 0.0491 -0.1735 82 LYS A CD 643 C CE . LYS A 82 ? 0.8411 1.1242 0.8945 0.0333 0.0475 -0.1803 82 LYS A CE 644 N NZ . LYS A 82 ? 0.8559 1.1811 0.9243 0.0498 0.0443 -0.1862 82 LYS A NZ 645 N N . ALA A 83 ? 0.7360 1.0448 0.8483 -0.0507 0.0487 -0.1322 83 ALA A N 646 C CA . ALA A 83 ? 0.7458 1.0572 0.8583 -0.0631 0.0495 -0.1242 83 ALA A CA 647 C C . ALA A 83 ? 0.7628 1.0903 0.8736 -0.0727 0.0519 -0.1267 83 ALA A C 648 O O . ALA A 83 ? 0.7806 1.1272 0.8974 -0.0790 0.0522 -0.1199 83 ALA A O 649 C CB . ALA A 83 ? 0.7431 1.0297 0.8432 -0.0658 0.0495 -0.1234 83 ALA A CB 650 N N . ASN A 84 ? 0.7731 1.0914 0.8728 -0.0721 0.0537 -0.1365 84 ASN A N 651 C CA . ASN A 84 ? 0.7935 1.1267 0.8907 -0.0813 0.0562 -0.1404 84 ASN A CA 652 C C . ASN A 84 ? 0.7847 1.1204 0.8791 -0.0732 0.0572 -0.1502 84 ASN A C 653 O O . ASN A 84 ? 0.8160 1.1313 0.8922 -0.0715 0.0594 -0.1588 84 ASN A O 654 C CB . ASN A 84 ? 0.8434 1.1626 0.9236 -0.0939 0.0588 -0.1434 84 ASN A CB 655 C CG . ASN A 84 ? 0.8659 1.1960 0.9505 -0.1028 0.0579 -0.1348 84 ASN A CG 656 O OD1 . ASN A 84 ? 0.8791 1.2391 0.9733 -0.1079 0.0574 -0.1291 84 ASN A OD1 657 N ND2 . ASN A 84 ? 0.8907 1.1975 0.9665 -0.1028 0.0576 -0.1339 84 ASN A ND2 658 N N . PRO A 85 ? 0.7543 1.1143 0.8634 -0.0689 0.0563 -0.1496 85 PRO A N 659 C CA . PRO A 85 ? 0.7588 1.1311 0.8677 -0.0608 0.0572 -0.1599 85 PRO A CA 660 C C . PRO A 85 ? 0.7652 1.1414 0.8661 -0.0683 0.0601 -0.1653 85 PRO A C 661 O O . PRO A 85 ? 0.7571 1.1468 0.8627 -0.0816 0.0611 -0.1596 85 PRO A O 662 C CB . PRO A 85 ? 0.7432 1.1456 0.8684 -0.0637 0.0571 -0.1569 85 PRO A CB 663 C CG . PRO A 85 ? 0.7145 1.1091 0.8444 -0.0676 0.0557 -0.1457 85 PRO A CG 664 C CD . PRO A 85 ? 0.7231 1.0998 0.8456 -0.0730 0.0555 -0.1400 85 PRO A CD 665 N N . VAL A 86 ? 0.7890 1.1526 0.8752 -0.0584 0.0614 -0.1761 86 VAL A N 666 C CA . VAL A 86 ? 0.8139 1.1760 0.8885 -0.0659 0.0648 -0.1824 86 VAL A CA 667 C C . VAL A 86 ? 0.7769 1.1769 0.8667 -0.0705 0.0655 -0.1841 86 VAL A C 668 O O . VAL A 86 ? 0.7960 1.2042 0.8836 -0.0827 0.0678 -0.1845 86 VAL A O 669 C CB . VAL A 86 ? 0.8734 1.2025 0.9200 -0.0520 0.0670 -0.1938 86 VAL A CB 670 C CG1 . VAL A 86 ? 0.9050 1.1894 0.9298 -0.0476 0.0672 -0.1923 86 VAL A CG1 671 C CG2 . VAL A 86 ? 0.8935 1.2417 0.9440 -0.0308 0.0656 -0.2021 86 VAL A CG2 672 N N . ASN A 87 ? 0.7464 1.1712 0.8501 -0.0626 0.0641 -0.1856 87 ASN A N 673 C CA . ASN A 87 ? 0.7361 1.1966 0.8512 -0.0689 0.0657 -0.1884 87 ASN A CA 674 C C . ASN A 87 ? 0.7152 1.1916 0.8428 -0.0825 0.0659 -0.1775 87 ASN A C 675 O O . ASN A 87 ? 0.7106 1.2012 0.8460 -0.0819 0.0657 -0.1769 87 ASN A O 676 C CB . ASN A 87 ? 0.7540 1.2364 0.8717 -0.0536 0.0653 -0.1998 87 ASN A CB 677 C CG . ASN A 87 ? 0.8014 1.2667 0.9002 -0.0368 0.0660 -0.2111 87 ASN A CG 678 O OD1 . ASN A 87 ? 0.8235 1.2788 0.9116 -0.0429 0.0686 -0.2140 87 ASN A OD1 679 N ND2 . ASN A 87 ? 0.8231 1.2832 0.9140 -0.0145 0.0640 -0.2178 87 ASN A ND2 680 N N . ASP A 88 ? 0.7238 1.1968 0.8491 -0.0944 0.0669 -0.1694 88 ASP A N 681 C CA . ASP A 88 ? 0.7115 1.1912 0.8399 -0.1039 0.0676 -0.1579 88 ASP A CA 682 C C . ASP A 88 ? 0.7155 1.2161 0.8425 -0.1135 0.0708 -0.1592 88 ASP A C 683 O O . ASP A 88 ? 0.6784 1.1976 0.8086 -0.1151 0.0729 -0.1666 88 ASP A O 684 C CB . ASP A 88 ? 0.7135 1.1768 0.8377 -0.1056 0.0658 -0.1477 88 ASP A CB 685 C CG . ASP A 88 ? 0.7192 1.1828 0.8409 -0.1091 0.0663 -0.1347 88 ASP A CG 686 O OD1 . ASP A 88 ? 0.7216 1.1869 0.8424 -0.1113 0.0683 -0.1329 88 ASP A OD1 687 O OD2 . ASP A 88 ? 0.7417 1.2035 0.8589 -0.1096 0.0653 -0.1268 88 ASP A OD2 688 N N . LEU A 89 ? 0.7219 1.2233 0.8435 -0.1195 0.0712 -0.1529 89 LEU A N 689 C CA . LEU A 89 ? 0.7266 1.2461 0.8446 -0.1277 0.0740 -0.1536 89 LEU A CA 690 C C . LEU A 89 ? 0.7236 1.2499 0.8412 -0.1284 0.0744 -0.1640 89 LEU A C 691 O O . LEU A 89 ? 0.6962 1.2188 0.8092 -0.1312 0.0736 -0.1626 89 LEU A O 692 C CB . LEU A 89 ? 0.7359 1.2547 0.8449 -0.1309 0.0742 -0.1407 89 LEU A CB 693 C CG . LEU A 89 ? 0.7489 1.2523 0.8500 -0.1285 0.0746 -0.1288 89 LEU A CG 694 C CD1 . LEU A 89 ? 0.7632 1.2669 0.8497 -0.1266 0.0750 -0.1169 89 LEU A CD1 695 C CD2 . LEU A 89 ? 0.7546 1.2568 0.8520 -0.1349 0.0786 -0.1314 89 LEU A CD2 696 N N . CYS A 90 ? 0.7327 1.2711 0.8530 -0.1266 0.0761 -0.1751 90 CYS A N 697 C CA . CYS A 90 ? 0.7425 1.2824 0.8581 -0.1252 0.0771 -0.1861 90 CYS A CA 698 C C . CYS A 90 ? 0.7157 1.2669 0.8266 -0.1365 0.0787 -0.1834 90 CYS A C 699 O O . CYS A 90 ? 0.7244 1.2675 0.8276 -0.1397 0.0790 -0.1872 90 CYS A O 700 C CB . CYS A 90 ? 0.7694 1.3256 0.8880 -0.1181 0.0785 -0.1986 90 CYS A CB 701 S SG . CYS A 90 ? 0.8042 1.3948 0.9302 -0.1283 0.0816 -0.1986 90 CYS A SG 702 N N . TYR A 91 ? 0.6771 1.2453 0.7892 -0.1434 0.0802 -0.1769 91 TYR A N 703 C CA . TYR A 91 ? 0.6846 1.2644 0.7909 -0.1514 0.0809 -0.1714 91 TYR A CA 704 C C . TYR A 91 ? 0.6744 1.2467 0.7773 -0.1493 0.0786 -0.1580 91 TYR A C 705 O O . TYR A 91 ? 0.6844 1.2477 0.7854 -0.1461 0.0785 -0.1497 91 TYR A O 706 C CB . TYR A 91 ? 0.7143 1.3114 0.8176 -0.1578 0.0841 -0.1703 91 TYR A CB 707 C CG . TYR A 91 ? 0.7328 1.3460 0.8294 -0.1643 0.0852 -0.1688 91 TYR A CG 708 C CD1 . TYR A 91 ? 0.7329 1.3488 0.8215 -0.1636 0.0837 -0.1570 91 TYR A CD1 709 C CD2 . TYR A 91 ? 0.7396 1.3683 0.8370 -0.1696 0.0875 -0.1794 91 TYR A CD2 710 C CE1 . TYR A 91 ? 0.7365 1.3723 0.8187 -0.1680 0.0844 -0.1560 91 TYR A CE1 711 C CE2 . TYR A 91 ? 0.7384 1.3836 0.8297 -0.1761 0.0885 -0.1783 91 TYR A CE2 712 C CZ . TYR A 91 ? 0.7270 1.3767 0.8110 -0.1754 0.0868 -0.1666 91 TYR A CZ 713 O OH . TYR A 91 ? 0.7368 1.4079 0.8144 -0.1803 0.0874 -0.1658 91 TYR A OH 714 N N . PRO A 92 ? 0.6811 1.2589 0.7810 -0.1519 0.0771 -0.1566 92 PRO A N 715 C CA . PRO A 92 ? 0.6885 1.2647 0.7858 -0.1475 0.0744 -0.1454 92 PRO A CA 716 C C . PRO A 92 ? 0.7172 1.2987 0.8053 -0.1421 0.0747 -0.1323 92 PRO A C 717 O O . PRO A 92 ? 0.7283 1.3184 0.8097 -0.1450 0.0772 -0.1318 92 PRO A O 718 C CB . PRO A 92 ? 0.6919 1.2850 0.7865 -0.1550 0.0739 -0.1495 92 PRO A CB 719 C CG . PRO A 92 ? 0.7039 1.3111 0.7963 -0.1632 0.0766 -0.1582 92 PRO A CG 720 C CD . PRO A 92 ? 0.7037 1.2941 0.8001 -0.1604 0.0784 -0.1655 92 PRO A CD 721 N N . GLY A 93 ? 0.7428 1.3158 0.8265 -0.1334 0.0726 -0.1219 93 GLY A N 722 C CA . GLY A 93 ? 0.7712 1.3388 0.8377 -0.1244 0.0734 -0.1086 93 GLY A CA 723 C C . GLY A 93 ? 0.7731 1.3189 0.8343 -0.1142 0.0720 -0.0991 93 GLY A C 724 O O . GLY A 93 ? 0.7362 1.2813 0.8085 -0.1129 0.0692 -0.1012 93 GLY A O 725 N N . ASP A 94 ? 0.8086 1.3330 0.8486 -0.1079 0.0748 -0.0888 94 ASP A N 726 C CA . ASP A 94 ? 0.8376 1.3354 0.8660 -0.0979 0.0747 -0.0791 94 ASP A CA 727 C C . ASP A 94 ? 0.8265 1.2923 0.8421 -0.1054 0.0799 -0.0783 94 ASP A C 728 O O . ASP A 94 ? 0.8392 1.3049 0.8487 -0.1165 0.0841 -0.0828 94 ASP A O 729 C CB . ASP A 94 ? 0.9023 1.4001 0.9053 -0.0799 0.0739 -0.0657 94 ASP A CB 730 C CG . ASP A 94 ? 0.9480 1.4861 0.9634 -0.0728 0.0687 -0.0669 94 ASP A CG 731 O OD1 . ASP A 94 ? 0.9703 1.5147 1.0004 -0.0716 0.0655 -0.0687 94 ASP A OD1 732 O OD2 . ASP A 94 ? 1.0112 1.5768 1.0202 -0.0698 0.0682 -0.0665 94 ASP A OD2 733 N N . PHE A 95 ? 0.7898 1.2309 0.8005 -0.1011 0.0801 -0.0735 95 PHE A N 734 C CA . PHE A 95 ? 0.7683 1.1776 0.7606 -0.1096 0.0859 -0.0719 95 PHE A CA 735 C C . PHE A 95 ? 0.7818 1.1567 0.7405 -0.0958 0.0879 -0.0573 95 PHE A C 736 O O . PHE A 95 ? 0.7670 1.1365 0.7314 -0.0851 0.0844 -0.0531 95 PHE A O 737 C CB . PHE A 95 ? 0.7379 1.1495 0.7545 -0.1179 0.0846 -0.0815 95 PHE A CB 738 C CG . PHE A 95 ? 0.7520 1.1475 0.7563 -0.1334 0.0911 -0.0855 95 PHE A CG 739 C CD1 . PHE A 95 ? 0.7958 1.1531 0.7666 -0.1354 0.0967 -0.0763 95 PHE A CD1 740 C CD2 . PHE A 95 ? 0.7361 1.1558 0.7595 -0.1464 0.0921 -0.0994 95 PHE A CD2 741 C CE1 . PHE A 95 ? 0.8195 1.1640 0.7763 -0.1548 0.1039 -0.0816 95 PHE A CE1 742 C CE2 . PHE A 95 ? 0.7536 1.1684 0.7667 -0.1631 0.0983 -0.1049 95 PHE A CE2 743 C CZ . PHE A 95 ? 0.7904 1.1680 0.7700 -0.1697 0.1046 -0.0964 95 PHE A CZ 744 N N . ASN A 96 ? 0.8159 1.1651 0.7359 -0.0950 0.0939 -0.0495 96 ASN A N 745 C CA . ASN A 96 ? 0.8492 1.1597 0.7271 -0.0774 0.0966 -0.0348 96 ASN A CA 746 C C . ASN A 96 ? 0.8559 1.1266 0.7191 -0.0827 0.1006 -0.0325 96 ASN A C 747 O O . ASN A 96 ? 0.8305 1.0898 0.6937 -0.1051 0.1060 -0.0401 96 ASN A O 748 C CB . ASN A 96 ? 0.9070 1.1909 0.7392 -0.0762 0.1035 -0.0277 96 ASN A CB 749 C CG . ASN A 96 ? 0.9717 1.2240 0.7583 -0.0482 0.1045 -0.0119 96 ASN A CG 750 O OD1 . ASN A 96 ? 0.9694 1.2530 0.7661 -0.0255 0.0975 -0.0075 96 ASN A OD1 751 N ND2 . ASN A 96 ? 1.0412 1.2314 0.7736 -0.0496 0.1137 -0.0038 96 ASN A ND2 752 N N . ASP A 97 ? 0.8785 1.1325 0.7288 -0.0622 0.0982 -0.0227 97 ASP A N 753 C CA . ASP A 97 ? 0.8824 1.0986 0.7182 -0.0644 0.1014 -0.0196 97 ASP A CA 754 C C . ASP A 97 ? 0.8237 1.0597 0.7001 -0.0849 0.0996 -0.0326 97 ASP A C 755 O O . ASP A 97 ? 0.8273 1.0367 0.6900 -0.1013 0.1056 -0.0356 97 ASP A O 756 C CB . ASP A 97 ? 0.9743 1.1278 0.7490 -0.0709 0.1127 -0.0123 97 ASP A CB 757 C CG . ASP A 97 ? 1.0503 1.1679 0.7738 -0.0412 0.1146 0.0036 97 ASP A CG 758 O OD1 . ASP A 97 ? 1.0710 1.2063 0.8055 -0.0155 0.1075 0.0094 97 ASP A OD1 759 O OD2 . ASP A 97 ? 1.1241 1.1952 0.7932 -0.0430 0.1235 0.0099 97 ASP A OD2 760 N N . TYR A 98 ? 0.7627 1.0452 0.6853 -0.0835 0.0916 -0.0408 98 TYR A N 761 C CA . TYR A 98 ? 0.7412 1.0449 0.7003 -0.0982 0.0893 -0.0536 98 TYR A CA 762 C C . TYR A 98 ? 0.7524 1.0355 0.7121 -0.0969 0.0890 -0.0518 98 TYR A C 763 O O . TYR A 98 ? 0.7280 1.0093 0.6949 -0.1121 0.0916 -0.0597 98 TYR A O 764 C CB . TYR A 98 ? 0.6891 1.0354 0.6867 -0.0936 0.0817 -0.0609 98 TYR A CB 765 C CG . TYR A 98 ? 0.6613 1.0279 0.6914 -0.1039 0.0791 -0.0744 98 TYR A CG 766 C CD1 . TYR A 98 ? 0.6593 1.0306 0.6913 -0.1196 0.0833 -0.0837 98 TYR A CD1 767 C CD2 . TYR A 98 ? 0.6412 1.0234 0.6968 -0.0971 0.0729 -0.0784 98 TYR A CD2 768 C CE1 . TYR A 98 ? 0.6474 1.0406 0.7063 -0.1236 0.0806 -0.0963 98 TYR A CE1 769 C CE2 . TYR A 98 ? 0.6113 1.0060 0.6894 -0.1021 0.0708 -0.0901 98 TYR A CE2 770 C CZ . TYR A 98 ? 0.6369 1.0385 0.7171 -0.1130 0.0743 -0.0988 98 TYR A CZ 771 O OH . TYR A 98 ? 0.6574 1.0745 0.7573 -0.1129 0.0718 -0.1107 98 TYR A OH 772 N N . GLU A 99 ? 0.7796 1.0508 0.7307 -0.0782 0.0859 -0.0417 99 GLU A N 773 C CA . GLU A 99 ? 0.7854 1.0388 0.7385 -0.0748 0.0849 -0.0394 99 GLU A CA 774 C C . GLU A 99 ? 0.8081 1.0138 0.7210 -0.0831 0.0936 -0.0346 99 GLU A C 775 O O . GLU A 99 ? 0.7902 0.9866 0.7087 -0.0935 0.0950 -0.0390 99 GLU A O 776 C CB . GLU A 99 ? 0.8056 1.0652 0.7610 -0.0524 0.0793 -0.0310 99 GLU A CB 777 C CG . GLU A 99 ? 0.8043 1.1090 0.7979 -0.0497 0.0717 -0.0376 99 GLU A CG 778 C CD . GLU A 99 ? 0.8332 1.1652 0.8274 -0.0471 0.0706 -0.0383 99 GLU A CD 779 O OE1 . GLU A 99 ? 0.8774 1.1947 0.8413 -0.0419 0.0748 -0.0315 99 GLU A OE1 780 O OE2 . GLU A 99 ? 0.8190 1.1848 0.8407 -0.0508 0.0661 -0.0460 99 GLU A OE2 781 N N . GLU A 100 ? 0.8321 1.0056 0.7009 -0.0795 0.1000 -0.0261 100 GLU A N 782 C CA . GLU A 100 ? 0.8680 0.9877 0.6887 -0.0919 0.1106 -0.0224 100 GLU A CA 783 C C . GLU A 100 ? 0.8634 0.9938 0.6941 -0.1238 0.1158 -0.0358 100 GLU A C 784 O O . GLU A 100 ? 0.8991 1.0009 0.7079 -0.1408 0.1228 -0.0381 100 GLU A O 785 C CB . GLU A 100 ? 0.9113 0.9890 0.6756 -0.0813 0.1173 -0.0108 100 GLU A CB 786 C CG . GLU A 100 ? 0.9376 0.9904 0.6738 -0.0481 0.1151 0.0036 100 GLU A CG 787 C CD . GLU A 100 ? 0.9639 0.9693 0.6718 -0.0463 0.1196 0.0086 100 GLU A CD 788 O OE1 . GLU A 100 ? 1.0166 0.9699 0.6801 -0.0655 0.1306 0.0086 100 GLU A OE1 789 O OE2 . GLU A 100 ? 0.9273 0.9471 0.6551 -0.0275 0.1127 0.0120 100 GLU A OE2 790 N N . LEU A 101 ? 0.8330 1.0075 0.6957 -0.1322 0.1126 -0.0456 101 LEU A N 791 C CA . LEU A 101 ? 0.8301 1.0266 0.7060 -0.1595 0.1167 -0.0598 101 LEU A CA 792 C C . LEU A 101 ? 0.7869 1.0128 0.7021 -0.1619 0.1111 -0.0692 101 LEU A C 793 O O . LEU A 101 ? 0.7751 1.0003 0.6848 -0.1817 0.1163 -0.0771 101 LEU A O 794 C CB . LEU A 101 ? 0.8098 1.0447 0.7059 -0.1646 0.1149 -0.0675 101 LEU A CB 795 C CG . LEU A 101 ? 0.7941 1.0623 0.7068 -0.1898 0.1184 -0.0837 101 LEU A CG 796 C CD1 . LEU A 101 ? 0.8278 1.0637 0.6966 -0.2172 0.1309 -0.0855 101 LEU A CD1 797 C CD2 . LEU A 101 ? 0.8018 1.1059 0.7332 -0.1904 0.1161 -0.0902 101 LEU A CD2 798 N N . LYS A 102 ? 0.7591 1.0113 0.7110 -0.1427 0.1011 -0.0691 102 LYS A N 799 C CA . LYS A 102 ? 0.7456 1.0176 0.7291 -0.1404 0.0956 -0.0760 102 LYS A CA 800 C C . LYS A 102 ? 0.7575 0.9959 0.7196 -0.1447 0.0996 -0.0714 102 LYS A C 801 O O . LYS A 102 ? 0.7410 0.9933 0.7159 -0.1553 0.0999 -0.0802 102 LYS A O 802 C CB . LYS A 102 ? 0.7300 1.0190 0.7423 -0.1194 0.0861 -0.0734 102 LYS A CB 803 C CG . LYS A 102 ? 0.7433 1.0709 0.7856 -0.1184 0.0813 -0.0836 102 LYS A CG 804 C CD . LYS A 102 ? 0.7518 1.0884 0.8129 -0.1020 0.0739 -0.0808 102 LYS A CD 805 C CE . LYS A 102 ? 0.7620 1.1249 0.8511 -0.1007 0.0693 -0.0929 102 LYS A CE 806 N NZ . LYS A 102 ? 0.7757 1.1389 0.8766 -0.0893 0.0637 -0.0909 102 LYS A NZ 807 N N . HIS A 103 ? 0.7871 0.9824 0.7143 -0.1350 0.1028 -0.0579 103 HIS A N 808 C CA . HIS A 103 ? 0.8171 0.9732 0.7174 -0.1380 0.1075 -0.0527 103 HIS A CA 809 C C . HIS A 103 ? 0.8749 1.0142 0.7464 -0.1680 0.1184 -0.0599 103 HIS A C 810 O O . HIS A 103 ? 0.8894 1.0179 0.7543 -0.1797 0.1216 -0.0634 103 HIS A O 811 C CB . HIS A 103 ? 0.8476 0.9583 0.7091 -0.1182 0.1094 -0.0367 103 HIS A CB 812 C CG . HIS A 103 ? 0.8702 0.9354 0.6998 -0.1187 0.1146 -0.0308 103 HIS A CG 813 N ND1 . HIS A 103 ? 0.8480 0.9189 0.6990 -0.1058 0.1083 -0.0289 103 HIS A ND1 814 C CD2 . HIS A 103 ? 0.9206 0.9308 0.6954 -0.1325 0.1262 -0.0272 103 HIS A CD2 815 C CE1 . HIS A 103 ? 0.8817 0.9055 0.6948 -0.1101 0.1153 -0.0240 103 HIS A CE1 816 N NE2 . HIS A 103 ? 0.9354 0.9195 0.7000 -0.1267 0.1265 -0.0230 103 HIS A NE2 817 N N . LEU A 104 ? 0.9187 1.0577 0.7718 -0.1822 0.1245 -0.0629 104 LEU A N 818 C CA . LEU A 104 ? 0.9825 1.1114 0.8066 -0.2157 0.1360 -0.0717 104 LEU A CA 819 C C . LEU A 104 ? 0.9593 1.1453 0.8239 -0.2324 0.1334 -0.0891 104 LEU A C 820 O O . LEU A 104 ? 0.9886 1.1709 0.8346 -0.2588 0.1415 -0.0971 104 LEU A O 821 C CB . LEU A 104 ? 1.0171 1.1410 0.8180 -0.2259 0.1420 -0.0719 104 LEU A CB 822 C CG . LEU A 104 ? 1.0796 1.1535 0.8173 -0.2552 0.1576 -0.0718 104 LEU A CG 823 C CD1 . LEU A 104 ? 1.1332 1.1287 0.8125 -0.2440 0.1639 -0.0561 104 LEU A CD1 824 C CD2 . LEU A 104 ? 1.0883 1.1679 0.8130 -0.2625 0.1613 -0.0729 104 LEU A CD2 825 N N . LEU A 105 ? 0.9257 1.1638 0.8414 -0.2165 0.1225 -0.0951 105 LEU A N 826 C CA . LEU A 105 ? 0.8857 1.1812 0.8398 -0.2235 0.1185 -0.1113 105 LEU A CA 827 C C . LEU A 105 ? 0.8920 1.1890 0.8573 -0.2203 0.1155 -0.1130 105 LEU A C 828 O O . LEU A 105 ? 0.8996 1.2398 0.8851 -0.2300 0.1147 -0.1266 105 LEU A O 829 C CB . LEU A 105 ? 0.8338 1.1716 0.8310 -0.2025 0.1080 -0.1156 105 LEU A CB 830 C CG . LEU A 105 ? 0.8197 1.1827 0.8209 -0.2086 0.1095 -0.1216 105 LEU A CG 831 C CD1 . LEU A 105 ? 0.7808 1.1798 0.8217 -0.1867 0.0993 -0.1266 105 LEU A CD1 832 C CD2 . LEU A 105 ? 0.8387 1.2324 0.8321 -0.2372 0.1175 -0.1362 105 LEU A CD2 833 N N . SER A 106 ? 1.0060 1.3963 0.7512 -0.2029 0.1289 -0.1000 106 SER A N 834 C CA A SER A 106 ? 1.0378 1.4209 0.7631 -0.2080 0.1279 -0.1001 106 SER A CA 835 C CA B SER A 106 ? 1.0330 1.4161 0.7584 -0.2079 0.1279 -0.1001 106 SER A CA 836 C C . SER A 106 ? 1.0817 1.4388 0.7706 -0.2267 0.1301 -0.1093 106 SER A C 837 O O . SER A 106 ? 1.1327 1.4848 0.8023 -0.2360 0.1259 -0.1116 106 SER A O 838 C CB A SER A 106 ? 1.0466 1.4139 0.7605 -0.1918 0.1384 -0.0945 106 SER A CB 839 C CB B SER A 106 ? 1.0365 1.4039 0.7511 -0.1915 0.1385 -0.0945 106 SER A CB 840 O OG A SER A 106 ? 1.0711 1.4010 0.7540 -0.1870 0.1515 -0.0986 106 SER A OG 841 O OG B SER A 106 ? 0.9833 1.3726 0.7325 -0.1764 0.1369 -0.0866 106 SER A OG 842 N N . ARG A 107 ? 1.1185 1.4566 0.7952 -0.2334 0.1362 -0.1141 107 ARG A N 843 C CA . ARG A 107 ? 1.1953 1.5078 0.8391 -0.2551 0.1377 -0.1229 107 ARG A CA 844 C C . ARG A 107 ? 1.1343 1.4770 0.8011 -0.2743 0.1299 -0.1274 107 ARG A C 845 O O . ARG A 107 ? 1.1536 1.4795 0.7987 -0.2957 0.1316 -0.1344 107 ARG A O 846 C CB . ARG A 107 ? 1.3008 1.5633 0.9081 -0.2517 0.1510 -0.1249 107 ARG A CB 847 C CG . ARG A 107 ? 1.3999 1.6237 0.9719 -0.2391 0.1603 -0.1257 107 ARG A CG 848 C CD . ARG A 107 ? 1.4513 1.6891 1.0455 -0.2118 0.1648 -0.1174 107 ARG A CD 849 N NE . ARG A 107 ? 1.5568 1.7555 1.1196 -0.1958 0.1778 -0.1189 107 ARG A NE 850 C CZ . ARG A 107 ? 1.5996 1.7659 1.1477 -0.1825 0.1859 -0.1188 107 ARG A CZ 851 N NH1 . ARG A 107 ? 1.6039 1.7688 1.1611 -0.1848 0.1826 -0.1164 107 ARG A NH1 852 N NH2 . ARG A 107 ? 1.5926 1.7266 1.1150 -0.1654 0.1976 -0.1212 107 ARG A NH2 853 N N . ILE A 108 ? 1.0435 1.4303 0.7541 -0.2673 0.1221 -0.1240 108 ILE A N 854 C CA . ILE A 108 ? 1.0133 1.4342 0.7512 -0.2819 0.1170 -0.1291 108 ILE A CA 855 C C . ILE A 108 ? 0.9535 1.4205 0.7272 -0.2822 0.1009 -0.1294 108 ILE A C 856 O O . ILE A 108 ? 0.9245 1.4061 0.7177 -0.2645 0.0944 -0.1227 108 ILE A O 857 C CB . ILE A 108 ? 0.9985 1.4280 0.7551 -0.2724 0.1238 -0.1272 108 ILE A CB 858 C CG1 . ILE A 108 ? 1.0333 1.4155 0.7520 -0.2737 0.1374 -0.1266 108 ILE A CG1 859 C CG2 . ILE A 108 ? 0.9816 1.4510 0.7684 -0.2859 0.1211 -0.1335 108 ILE A CG2 860 C CD1 . ILE A 108 ? 1.0125 1.3949 0.7410 -0.2607 0.1426 -0.1228 108 ILE A CD1 861 N N . ASN A 109 ? 0.9322 1.4218 0.7150 -0.3026 0.0938 -0.1367 109 ASN A N 862 C CA . ASN A 109 ? 0.9118 1.4473 0.7307 -0.3027 0.0763 -0.1378 109 ASN A CA 863 C C . ASN A 109 ? 0.8884 1.4704 0.7519 -0.3051 0.0748 -0.1432 109 ASN A C 864 O O . ASN A 109 ? 0.8512 1.4724 0.7512 -0.2967 0.0606 -0.1432 109 ASN A O 865 C CB . ASN A 109 ? 0.9519 1.4862 0.7530 -0.3228 0.0651 -0.1428 109 ASN A CB 866 C CG . ASN A 109 ? 0.9849 1.4809 0.7453 -0.3176 0.0637 -0.1380 109 ASN A CG 867 O OD1 . ASN A 109 ? 0.9745 1.4744 0.7413 -0.2998 0.0577 -0.1300 109 ASN A OD1 868 N ND2 . ASN A 109 ? 1.0389 1.4958 0.7552 -0.3336 0.0700 -0.1432 109 ASN A ND2 869 N N . HIS A 110 ? 0.8935 1.4701 0.7526 -0.3159 0.0896 -0.1478 110 HIS A N 870 C CA . HIS A 110 ? 0.8765 1.4982 0.7752 -0.3201 0.0920 -0.1543 110 HIS A CA 871 C C . HIS A 110 ? 0.8855 1.4920 0.7733 -0.3229 0.1112 -0.1555 110 HIS A C 872 O O . HIS A 110 ? 0.9059 1.4737 0.7554 -0.3381 0.1228 -0.1554 110 HIS A O 873 C CB . HIS A 110 ? 0.8946 1.5500 0.8098 -0.3451 0.0849 -0.1630 110 HIS A CB 874 C CG . HIS A 110 ? 0.8760 1.5909 0.8430 -0.3452 0.0842 -0.1703 110 HIS A CG 875 N ND1 . HIS A 110 ? 0.8908 1.6411 0.8775 -0.3706 0.0860 -0.1795 110 HIS A ND1 876 C CD2 . HIS A 110 ? 0.8427 1.5883 0.8464 -0.3228 0.0827 -0.1708 110 HIS A CD2 877 C CE1 . HIS A 110 ? 0.8644 1.6683 0.9002 -0.3623 0.0868 -0.1854 110 HIS A CE1 878 N NE2 . HIS A 110 ? 0.8317 1.6311 0.8765 -0.3326 0.0847 -0.1807 110 HIS A NE2 879 N N . PHE A 111 ? 0.8684 1.5028 0.7871 -0.3078 0.1135 -0.1568 111 PHE A N 880 C CA . PHE A 111 ? 0.8877 1.5151 0.7989 -0.3104 0.1305 -0.1589 111 PHE A CA 881 C C . PHE A 111 ? 0.8860 1.5653 0.8338 -0.3222 0.1357 -0.1690 111 PHE A C 882 O O . PHE A 111 ? 0.8771 1.6027 0.8663 -0.3172 0.1236 -0.1738 111 PHE A O 883 C CB . PHE A 111 ? 0.8622 1.4804 0.7778 -0.2836 0.1304 -0.1540 111 PHE A CB 884 C CG . PHE A 111 ? 0.8684 1.4354 0.7471 -0.2728 0.1319 -0.1444 111 PHE A CG 885 C CD1 . PHE A 111 ? 0.9013 1.4241 0.7366 -0.2854 0.1429 -0.1420 111 PHE A CD1 886 C CD2 . PHE A 111 ? 0.8337 1.3970 0.7225 -0.2495 0.1224 -0.1380 111 PHE A CD2 887 C CE1 . PHE A 111 ? 0.8958 1.3754 0.7019 -0.2720 0.1438 -0.1340 111 PHE A CE1 888 C CE2 . PHE A 111 ? 0.8349 1.3586 0.6965 -0.2389 0.1244 -0.1298 111 PHE A CE2 889 C CZ . PHE A 111 ? 0.8611 1.3445 0.6826 -0.2487 0.1350 -0.1281 111 PHE A CZ 890 N N . GLU A 112 ? 0.9262 1.5975 0.8582 -0.3368 0.1541 -0.1720 112 GLU A N 891 C CA . GLU A 112 ? 0.9332 1.6542 0.8987 -0.3459 0.1646 -0.1819 112 GLU A CA 892 C C . GLU A 112 ? 0.8883 1.5923 0.8368 -0.3369 0.1804 -0.1813 112 GLU A C 893 O O . GLU A 112 ? 0.8777 1.5390 0.7823 -0.3501 0.1935 -0.1769 112 GLU A O 894 C CB . GLU A 112 ? 1.0034 1.7360 0.9643 -0.3818 0.1741 -0.1870 112 GLU A CB 895 C CG . GLU A 112 ? 1.0544 1.8292 1.0502 -0.3923 0.1579 -0.1922 112 GLU A CG 896 C CD . GLU A 112 ? 1.0742 1.9249 1.1322 -0.3896 0.1569 -0.2030 112 GLU A CD 897 O OE1 . GLU A 112 ? 1.0883 1.9610 1.1580 -0.3930 0.1759 -0.2087 112 GLU A OE1 898 O OE2 . GLU A 112 ? 1.0863 1.9743 1.1804 -0.3837 0.1372 -0.2058 112 GLU A OE2 899 N N . LYS A 113 ? 0.8430 1.5767 0.8230 -0.3142 0.1778 -0.1858 113 LYS A N 900 C CA . LYS A 113 ? 0.8682 1.5869 0.8313 -0.3043 0.1908 -0.1867 113 LYS A CA 901 C C . LYS A 113 ? 0.8940 1.6325 0.8538 -0.3273 0.2137 -0.1943 113 LYS A C 902 O O . LYS A 113 ? 0.8900 1.6846 0.8917 -0.3353 0.2180 -0.2045 113 LYS A O 903 C CB . LYS A 113 ? 0.8419 1.5864 0.8392 -0.2748 0.1813 -0.1914 113 LYS A CB 904 C CG . LYS A 113 ? 0.8640 1.5906 0.8414 -0.2633 0.1921 -0.1934 113 LYS A CG 905 C CD . LYS A 113 ? 0.8668 1.5756 0.8475 -0.2345 0.1759 -0.1893 113 LYS A CD 906 C CE . LYS A 113 ? 0.8426 1.5940 0.8730 -0.2156 0.1637 -0.1973 113 LYS A CE 907 N NZ . LYS A 113 ? 0.8207 1.5498 0.8533 -0.1927 0.1444 -0.1902 113 LYS A NZ 908 N N . ILE A 114 ? 0.9245 1.6178 0.8348 -0.3380 0.2282 -0.1890 114 ILE A N 909 C CA . ILE A 114 ? 0.9589 1.6654 0.8587 -0.3601 0.2524 -0.1948 114 ILE A CA 910 C C . ILE A 114 ? 0.9876 1.6606 0.8498 -0.3494 0.2631 -0.1926 114 ILE A C 911 O O . ILE A 114 ? 0.9950 1.6201 0.8257 -0.3325 0.2525 -0.1834 114 ILE A O 912 C CB . ILE A 114 ? 1.0005 1.6825 0.8683 -0.3962 0.2631 -0.1904 114 ILE A CB 913 C CG1 . ILE A 114 ? 1.0364 1.6407 0.8436 -0.3954 0.2583 -0.1769 114 ILE A CG1 914 C CG2 . ILE A 114 ? 0.9834 1.7040 0.8891 -0.4111 0.2530 -0.1948 114 ILE A CG2 915 C CD1 . ILE A 114 ? 1.0936 1.6592 0.8537 -0.4293 0.2745 -0.1723 114 ILE A CD1 916 N N . GLN A 115 ? 1.0081 1.7090 0.8741 -0.3599 0.2843 -0.2013 115 GLN A N 917 C CA . GLN A 115 ? 1.0235 1.6960 0.8511 -0.3520 0.2962 -0.2009 115 GLN A CA 918 C C . GLN A 115 ? 1.0689 1.6866 0.8330 -0.3778 0.3103 -0.1906 115 GLN A C 919 O O . GLN A 115 ? 1.0842 1.7161 0.8441 -0.4087 0.3289 -0.1927 115 GLN A O 920 C CB . GLN A 115 ? 1.0221 1.7501 0.8810 -0.3506 0.3146 -0.2162 115 GLN A CB 921 C CG . GLN A 115 ? 1.0507 1.7520 0.8707 -0.3388 0.3252 -0.2182 115 GLN A CG 922 C CD . GLN A 115 ? 1.0560 1.8107 0.9015 -0.3404 0.3485 -0.2346 115 GLN A CD 923 O OE1 . GLN A 115 ? 1.0378 1.8165 0.9098 -0.3137 0.3439 -0.2455 115 GLN A OE1 924 N NE2 . GLN A 115 ? 1.0920 1.8653 0.9296 -0.3723 0.3743 -0.2368 115 GLN A NE2 925 N N . ILE A 116 ? 1.0861 1.6413 0.8011 -0.3654 0.3009 -0.1793 116 ILE A N 926 C CA . ILE A 116 ? 1.1550 1.6495 0.8041 -0.3862 0.3115 -0.1681 116 ILE A CA 927 C C . ILE A 116 ? 1.2189 1.6934 0.8259 -0.3864 0.3270 -0.1684 116 ILE A C 928 O O . ILE A 116 ? 1.2994 1.7523 0.8657 -0.4137 0.3470 -0.1649 116 ILE A O 929 C CB . ILE A 116 ? 1.1418 1.5747 0.7575 -0.3753 0.2921 -0.1542 116 ILE A CB 930 C CG1 . ILE A 116 ? 1.1063 1.5311 0.7313 -0.3390 0.2716 -0.1521 116 ILE A CG1 931 C CG2 . ILE A 116 ? 1.1169 1.5592 0.7568 -0.3856 0.2835 -0.1534 116 ILE A CG2 932 C CD1 . ILE A 116 ? 1.1243 1.4886 0.7123 -0.3272 0.2561 -0.1385 116 ILE A CD1 933 N N . ILE A 117 ? 1.2210 1.7011 0.8353 -0.3577 0.3178 -0.1729 117 ILE A N 934 C CA . ILE A 117 ? 1.2674 1.7298 0.8409 -0.3554 0.3308 -0.1752 117 ILE A CA 935 C C . ILE A 117 ? 1.2379 1.7572 0.8560 -0.3383 0.3359 -0.1924 117 ILE A C 936 O O . ILE A 117 ? 1.2070 1.7313 0.8480 -0.3095 0.3161 -0.1956 117 ILE A O 937 C CB . ILE A 117 ? 1.3024 1.7008 0.8260 -0.3360 0.3121 -0.1632 117 ILE A CB 938 C CG1 . ILE A 117 ? 1.3345 1.6757 0.8178 -0.3475 0.3050 -0.1469 117 ILE A CG1 939 C CG2 . ILE A 117 ? 1.3631 1.7381 0.8360 -0.3366 0.3248 -0.1650 117 ILE A CG2 940 C CD1 . ILE A 117 ? 1.3626 1.6439 0.8014 -0.3271 0.2851 -0.1346 117 ILE A CD1 941 N N . PRO A 118 ? 1.2614 1.8231 0.8917 -0.3559 0.3631 -0.2040 118 PRO A N 942 C CA . PRO A 118 ? 1.2402 1.8591 0.9176 -0.3376 0.3689 -0.2222 118 PRO A CA 943 C C . PRO A 118 ? 1.2685 1.8598 0.9150 -0.3126 0.3626 -0.2263 118 PRO A C 944 O O . PRO A 118 ? 1.3170 1.8538 0.8982 -0.3178 0.3652 -0.2176 118 PRO A O 945 C CB . PRO A 118 ? 1.2641 1.9265 0.9492 -0.3649 0.4034 -0.2320 118 PRO A CB 946 C CG . PRO A 118 ? 1.2866 1.9232 0.9433 -0.4000 0.4116 -0.2188 118 PRO A CG 947 C CD . PRO A 118 ? 1.3102 1.8680 0.9103 -0.3930 0.3907 -0.2011 118 PRO A CD 948 N N . LYS A 119 ? 1.2495 1.8760 0.9414 -0.2857 0.3527 -0.2396 119 LYS A N 949 C CA . LYS A 119 ? 1.2827 1.8854 0.9504 -0.2614 0.3443 -0.2459 119 LYS A CA 950 C C . LYS A 119 ? 1.3566 1.9590 0.9839 -0.2707 0.3735 -0.2563 119 LYS A C 951 O O . LYS A 119 ? 1.4127 1.9702 0.9854 -0.2630 0.3703 -0.2552 119 LYS A O 952 C CB . LYS A 119 ? 1.2467 1.8879 0.9747 -0.2327 0.3285 -0.2586 119 LYS A CB 953 C CG . LYS A 119 ? 1.2735 1.8813 0.9804 -0.2067 0.3098 -0.2621 119 LYS A CG 954 C CD . LYS A 119 ? 1.2496 1.8873 1.0155 -0.1810 0.2904 -0.2709 119 LYS A CD 955 C CE . LYS A 119 ? 1.2842 1.8863 1.0293 -0.1578 0.2706 -0.2745 119 LYS A CE 956 N NZ . LYS A 119 ? 1.2617 1.8819 1.0590 -0.1351 0.2480 -0.2788 119 LYS A NZ 957 N N . SER A 120 ? 1.3607 2.0149 1.0149 -0.2883 0.4022 -0.2665 120 SER A N 958 C CA . SER A 120 ? 1.3865 2.0502 1.0079 -0.3003 0.4357 -0.2775 120 SER A CA 959 C C . SER A 120 ? 1.4348 2.0437 0.9778 -0.3295 0.4503 -0.2623 120 SER A C 960 O O . SER A 120 ? 1.5147 2.1171 1.0142 -0.3399 0.4767 -0.2686 120 SER A O 961 C CB . SER A 120 ? 1.3705 2.1138 1.0529 -0.3115 0.4623 -0.2925 120 SER A CB 962 O OG . SER A 120 ? 1.3620 2.1196 1.0610 -0.3414 0.4672 -0.2813 120 SER A OG 963 N N . SER A 121 ? 1.4122 1.9795 0.9342 -0.3423 0.4340 -0.2425 121 SER A N 964 C CA . SER A 121 ? 1.4600 1.9699 0.9069 -0.3699 0.4456 -0.2265 121 SER A CA 965 C C . SER A 121 ? 1.4947 1.9307 0.8688 -0.3559 0.4280 -0.2162 121 SER A C 966 O O . SER A 121 ? 1.5403 1.9206 0.8458 -0.3751 0.4338 -0.2015 121 SER A O 967 C CB . SER A 121 ? 1.4410 1.9366 0.8959 -0.3903 0.4372 -0.2108 121 SER A CB 968 O OG . SER A 121 ? 1.3984 1.8648 0.8634 -0.3678 0.4020 -0.2013 121 SER A OG 969 N N . TRP A 122 ? 1.4578 1.8913 0.8455 -0.3233 0.4051 -0.2234 122 TRP A N 970 C CA . TRP A 122 ? 1.4802 1.8493 0.8046 -0.3091 0.3851 -0.2151 122 TRP A CA 971 C C . TRP A 122 ? 1.5343 1.8965 0.8115 -0.3084 0.4051 -0.2278 122 TRP A C 972 O O . TRP A 122 ? 1.5306 1.9048 0.8211 -0.2842 0.3965 -0.2425 122 TRP A O 973 C CB . TRP A 122 ? 1.4174 1.7846 0.7783 -0.2774 0.3486 -0.2155 122 TRP A CB 974 C CG . TRP A 122 ? 1.3729 1.7360 0.7668 -0.2768 0.3279 -0.2014 122 TRP A CG 975 C CD1 . TRP A 122 ? 1.3027 1.7123 0.7687 -0.2695 0.3201 -0.2059 122 TRP A CD1 976 C CD2 . TRP A 122 ? 1.3884 1.6958 0.7415 -0.2825 0.3124 -0.1810 122 TRP A CD2 977 N NE1 . TRP A 122 ? 1.2850 1.6717 0.7559 -0.2714 0.3023 -0.1901 122 TRP A NE1 978 C CE2 . TRP A 122 ? 1.3286 1.6535 0.7329 -0.2783 0.2976 -0.1752 122 TRP A CE2 979 C CE3 . TRP A 122 ? 1.4512 1.6941 0.7279 -0.2894 0.3089 -0.1670 122 TRP A CE3 980 C CZ2 . TRP A 122 ? 1.3292 1.6107 0.7124 -0.2799 0.2815 -0.1575 122 TRP A CZ2 981 C CZ3 . TRP A 122 ? 1.4571 1.6565 0.7148 -0.2899 0.2910 -0.1486 122 TRP A CZ3 982 C CH2 . TRP A 122 ? 1.3932 1.6130 0.7049 -0.2847 0.2784 -0.1447 122 TRP A CH2 983 N N . SER A 123 ? 1.5896 1.9282 0.8075 -0.3359 0.4321 -0.2219 123 SER A N 984 C CA . SER A 123 ? 1.6460 1.9845 0.8179 -0.3412 0.4599 -0.2348 123 SER A CA 985 C C . SER A 123 ? 1.7122 1.9823 0.8025 -0.3295 0.4433 -0.2296 123 SER A C 986 O O . SER A 123 ? 1.7591 2.0274 0.8117 -0.3272 0.4611 -0.2432 123 SER A O 987 C CB . SER A 123 ? 1.6891 2.0345 0.8320 -0.3797 0.4992 -0.2303 123 SER A CB 988 O OG . SER A 123 ? 1.7126 1.9989 0.8060 -0.3999 0.4901 -0.2060 123 SER A OG 989 N N . SER A 124 ? 1.7233 1.9389 0.7864 -0.3217 0.4093 -0.2107 124 SER A N 990 C CA . SER A 124 ? 1.7710 1.9212 0.7589 -0.3101 0.3876 -0.2037 124 SER A CA 991 C C . SER A 124 ? 1.7365 1.8827 0.7559 -0.2770 0.3468 -0.2070 124 SER A C 992 O O . SER A 124 ? 1.7757 1.8735 0.7417 -0.2654 0.3241 -0.2026 124 SER A O 993 C CB . SER A 124 ? 1.8147 1.8981 0.7358 -0.3271 0.3794 -0.1780 124 SER A CB 994 O OG . SER A 124 ? 1.8442 1.9282 0.7374 -0.3610 0.4160 -0.1730 124 SER A OG 995 N N . HIS A 125 ? 1.6721 1.8683 0.7769 -0.2635 0.3368 -0.2139 125 HIS A N 996 C CA . HIS A 125 ? 1.6339 1.8317 0.7754 -0.2351 0.3007 -0.2171 125 HIS A CA 997 C C . HIS A 125 ? 1.5976 1.8574 0.8125 -0.2212 0.3078 -0.2384 125 HIS A C 998 O O . HIS A 125 ? 1.5849 1.8928 0.8398 -0.2321 0.3348 -0.2464 125 HIS A O 999 C CB . HIS A 125 ? 1.5739 1.7594 0.7444 -0.2308 0.2733 -0.1981 125 HIS A CB 1000 C CG . HIS A 125 ? 1.6140 1.7386 0.7189 -0.2415 0.2645 -0.1765 125 HIS A CG 1001 N ND1 . HIS A 125 ? 1.6482 1.7571 0.7211 -0.2675 0.2882 -0.1658 125 HIS A ND1 1002 C CD2 . HIS A 125 ? 1.6340 1.7090 0.7007 -0.2292 0.2332 -0.1632 125 HIS A CD2 1003 C CE1 . HIS A 125 ? 1.6945 1.7421 0.7087 -0.2695 0.2719 -0.1466 125 HIS A CE1 1004 N NE2 . HIS A 125 ? 1.6884 1.7166 0.6994 -0.2454 0.2381 -0.1448 125 HIS A NE2 1005 N N . GLU A 126 ? 1.5857 1.8434 0.8187 -0.1971 0.2822 -0.2473 126 GLU A N 1006 C CA . GLU A 126 ? 1.5398 1.8476 0.8397 -0.1806 0.2838 -0.2664 126 GLU A CA 1007 C C . GLU A 126 ? 1.4631 1.8013 0.8363 -0.1752 0.2672 -0.2576 126 GLU A C 1008 O O . GLU A 126 ? 1.4500 1.7640 0.8273 -0.1686 0.2379 -0.2432 126 GLU A O 1009 C CB . GLU A 126 ? 1.5649 1.8510 0.8482 -0.1592 0.2627 -0.2794 126 GLU A CB 1010 C CG . GLU A 126 ? 1.5414 1.8696 0.8807 -0.1409 0.2668 -0.3016 126 GLU A CG 1011 C CD . GLU A 126 ? 1.5702 1.9406 0.9195 -0.1474 0.3077 -0.3189 126 GLU A CD 1012 O OE1 . GLU A 126 ? 1.5831 1.9357 0.8737 -0.1534 0.3292 -0.3287 126 GLU A OE1 1013 O OE2 . GLU A 126 ? 1.5297 1.9525 0.9462 -0.1464 0.3179 -0.3226 126 GLU A OE2 1014 N N . ALA A 127 ? 1.4093 1.8021 0.8399 -0.1779 0.2860 -0.2667 127 ALA A N 1015 C CA . ALA A 127 ? 1.3255 1.7482 0.8203 -0.1766 0.2743 -0.2582 127 ALA A CA 1016 C C . ALA A 127 ? 1.2727 1.7375 0.8351 -0.1561 0.2653 -0.2723 127 ALA A C 1017 O O . ALA A 127 ? 1.2319 1.7142 0.8427 -0.1517 0.2495 -0.2645 127 ALA A O 1018 C CB . ALA A 127 ? 1.3163 1.7641 0.8211 -0.2012 0.2996 -0.2522 127 ALA A CB 1019 N N . SER A 128 ? 1.2809 1.7582 0.8432 -0.1427 0.2748 -0.2927 128 SER A N 1020 C CA . SER A 128 ? 1.2371 1.7516 0.8604 -0.1219 0.2680 -0.3073 128 SER A CA 1021 C C . SER A 128 ? 1.2268 1.7107 0.8443 -0.0997 0.2401 -0.3135 128 SER A C 1022 O O . SER A 128 ? 1.2031 1.7083 0.8613 -0.0809 0.2344 -0.3273 128 SER A O 1023 C CB . SER A 128 ? 1.2706 1.8294 0.9102 -0.1205 0.3005 -0.3284 128 SER A CB 1024 O OG . SER A 128 ? 1.2762 1.8766 0.9445 -0.1399 0.3215 -0.3233 128 SER A OG 1025 N N . LEU A 129 ? 1.2366 1.6703 0.8046 -0.1021 0.2214 -0.3031 129 LEU A N 1026 C CA . LEU A 129 ? 1.2409 1.6435 0.8013 -0.0852 0.1926 -0.3076 129 LEU A CA 1027 C C . LEU A 129 ? 1.2102 1.5939 0.7849 -0.0857 0.1611 -0.2873 129 LEU A C 1028 O O . LEU A 129 ? 1.2276 1.5815 0.7897 -0.0770 0.1353 -0.2869 129 LEU A O 1029 C CB . LEU A 129 ? 1.3198 1.6803 0.8084 -0.0856 0.1948 -0.3161 129 LEU A CB 1030 C CG . LEU A 129 ? 1.3615 1.7344 0.8215 -0.0869 0.2294 -0.3361 129 LEU A CG 1031 C CD1 . LEU A 129 ? 1.4229 1.7457 0.8061 -0.0863 0.2254 -0.3433 129 LEU A CD1 1032 C CD2 . LEU A 129 ? 1.3443 1.7566 0.8560 -0.0685 0.2396 -0.3577 129 LEU A CD2 1033 N N . GLY A 130 ? 1.1684 1.5702 0.7696 -0.0964 0.1636 -0.2712 130 GLY A N 1034 C CA . GLY A 130 ? 1.1210 1.5105 0.7399 -0.0964 0.1378 -0.2525 130 GLY A CA 1035 C C . GLY A 130 ? 1.0670 1.4814 0.7473 -0.0848 0.1231 -0.2534 130 GLY A C 1036 O O . GLY A 130 ? 1.0208 1.4599 0.7383 -0.0895 0.1252 -0.2439 130 GLY A O 1037 N N . VAL A 131 ? 1.0538 1.4576 0.7406 -0.0705 0.1073 -0.2644 131 VAL A N 1038 C CA . VAL A 131 ? 1.0012 1.4221 0.7406 -0.0590 0.0926 -0.2660 131 VAL A CA 1039 C C . VAL A 131 ? 0.9940 1.3849 0.7307 -0.0519 0.0628 -0.2636 131 VAL A C 1040 O O . VAL A 131 ? 1.0447 1.4043 0.7396 -0.0515 0.0545 -0.2686 131 VAL A O 1041 C CB . VAL A 131 ? 1.0126 1.4589 0.7750 -0.0467 0.1072 -0.2863 131 VAL A CB 1042 C CG1 . VAL A 131 ? 0.9922 1.4797 0.7751 -0.0549 0.1337 -0.2870 131 VAL A CG1 1043 C CG2 . VAL A 131 ? 1.0632 1.4869 0.7836 -0.0391 0.1139 -0.3057 131 VAL A CG2 1044 N N . SER A 132 ? 0.9571 1.3576 0.7373 -0.0477 0.0465 -0.2559 132 SER A N 1045 C CA . SER A 132 ? 0.9479 1.3244 0.7333 -0.0448 0.0180 -0.2508 132 SER A CA 1046 C C . SER A 132 ? 0.9338 1.3168 0.7591 -0.0346 0.0074 -0.2556 132 SER A C 1047 O O . SER A 132 ? 0.9159 1.3269 0.7749 -0.0315 0.0171 -0.2543 132 SER A O 1048 C CB . SER A 132 ? 0.9118 1.2887 0.7063 -0.0548 0.0064 -0.2289 132 SER A CB 1049 O OG . SER A 132 ? 0.8925 1.2561 0.7037 -0.0539 -0.0195 -0.2227 132 SER A OG 1050 N N . SER A 133 ? 0.9399 1.2947 0.7597 -0.0302 -0.0144 -0.2606 133 SER A N 1051 C CA . SER A 133 ? 0.9382 1.2897 0.7916 -0.0224 -0.0286 -0.2620 133 SER A CA 1052 C C . SER A 133 ? 0.9119 1.2780 0.8017 -0.0309 -0.0388 -0.2404 133 SER A C 1053 O O . SER A 133 ? 0.8943 1.2628 0.8137 -0.0261 -0.0467 -0.2378 133 SER A O 1054 C CB . SER A 133 ? 0.9696 1.2822 0.8034 -0.0190 -0.0501 -0.2722 133 SER A CB 1055 O OG . SER A 133 ? 0.9778 1.2757 0.7969 -0.0315 -0.0670 -0.2607 133 SER A OG 1056 N N . ALA A 134 ? 0.9170 1.2904 0.8017 -0.0425 -0.0383 -0.2250 134 ALA A N 1057 C CA . ALA A 134 ? 0.8972 1.2876 0.8132 -0.0502 -0.0428 -0.2053 134 ALA A CA 1058 C C . ALA A 134 ? 0.8951 1.3147 0.8345 -0.0486 -0.0259 -0.2020 134 ALA A C 1059 O O . ALA A 134 ? 0.8508 1.2816 0.8178 -0.0519 -0.0307 -0.1893 134 ALA A O 1060 C CB . ALA A 134 ? 0.8928 1.2833 0.7952 -0.0597 -0.0446 -0.1924 134 ALA A CB 1061 N N . CYS A 135 ? 0.9280 1.3605 0.8552 -0.0447 -0.0064 -0.2136 135 CYS A N 1062 C CA . CYS A 135 ? 0.9043 1.3679 0.8536 -0.0443 0.0094 -0.2128 135 CYS A CA 1063 C C . CYS A 135 ? 0.8898 1.3638 0.8498 -0.0306 0.0163 -0.2308 135 CYS A C 1064 O O . CYS A 135 ? 0.8711 1.3633 0.8232 -0.0296 0.0360 -0.2417 135 CYS A O 1065 C CB . CYS A 135 ? 0.9331 1.4088 0.8625 -0.0546 0.0287 -0.2094 135 CYS A CB 1066 S SG . CYS A 135 ? 0.9764 1.4403 0.8938 -0.0666 0.0220 -0.1891 135 CYS A SG 1067 N N . PRO A 136 ? 0.8753 1.3381 0.8544 -0.0198 0.0004 -0.2341 136 PRO A N 1068 C CA . PRO A 136 ? 0.8827 1.3515 0.8715 -0.0028 0.0051 -0.2526 136 PRO A CA 1069 C C . PRO A 136 ? 0.8562 1.3649 0.8776 0.0015 0.0164 -0.2528 136 PRO A C 1070 O O . PRO A 136 ? 0.8055 1.3271 0.8460 -0.0063 0.0117 -0.2370 136 PRO A O 1071 C CB . PRO A 136 ? 0.9028 1.3406 0.8999 0.0059 -0.0186 -0.2524 136 PRO A CB 1072 C CG . PRO A 136 ? 0.8678 1.3037 0.8788 -0.0073 -0.0314 -0.2298 136 PRO A CG 1073 C CD . PRO A 136 ? 0.8560 1.3008 0.8496 -0.0228 -0.0214 -0.2202 136 PRO A CD 1074 N N . TYR A 137 ? 0.8807 1.4098 0.9077 0.0135 0.0315 -0.2712 137 TYR A N 1075 C CA . TYR A 137 ? 0.8581 1.4285 0.9218 0.0208 0.0394 -0.2747 137 TYR A CA 1076 C C . TYR A 137 ? 0.8704 1.4449 0.9482 0.0452 0.0403 -0.2958 137 TYR A C 1077 O O . TYR A 137 ? 0.8933 1.4705 0.9540 0.0511 0.0568 -0.3136 137 TYR A O 1078 C CB . TYR A 137 ? 0.8561 1.4630 0.9181 0.0069 0.0639 -0.2755 137 TYR A CB 1079 C CG . TYR A 137 ? 0.8501 1.5055 0.9526 0.0130 0.0724 -0.2815 137 TYR A CG 1080 C CD1 . TYR A 137 ? 0.8307 1.5004 0.9626 0.0119 0.0585 -0.2683 137 TYR A CD1 1081 C CD2 . TYR A 137 ? 0.8592 1.5481 0.9705 0.0194 0.0944 -0.3003 137 TYR A CD2 1082 C CE1 . TYR A 137 ? 0.8167 1.5324 0.9865 0.0173 0.0632 -0.2736 137 TYR A CE1 1083 C CE2 . TYR A 137 ? 0.8485 1.5877 1.0025 0.0247 0.1010 -0.3060 137 TYR A CE2 1084 C CZ . TYR A 137 ? 0.8302 1.5826 1.0137 0.0238 0.0839 -0.2925 137 TYR A CZ 1085 O OH . TYR A 137 ? 0.8266 1.6305 1.0533 0.0289 0.0875 -0.2981 137 TYR A OH 1086 N N . GLN A 138 ? 0.8629 1.4353 0.9694 0.0601 0.0227 -0.2937 138 GLN A N 1087 C CA . GLN A 138 ? 0.8929 1.4710 1.0186 0.0869 0.0219 -0.3132 138 GLN A CA 1088 C C . GLN A 138 ? 0.9318 1.4661 1.0247 0.0979 0.0193 -0.3291 138 GLN A C 1089 O O . GLN A 138 ? 0.9589 1.5020 1.0508 0.1153 0.0329 -0.3515 138 GLN A O 1090 C CB . GLN A 138 ? 0.8991 1.5348 1.0494 0.0914 0.0467 -0.3267 138 GLN A CB 1091 C CG . GLN A 138 ? 0.9103 1.5775 1.1066 0.1156 0.0410 -0.3356 138 GLN A CG 1092 C CD . GLN A 138 ? 0.8862 1.6170 1.1175 0.1070 0.0556 -0.3338 138 GLN A CD 1093 O OE1 . GLN A 138 ? 0.8970 1.6714 1.1510 0.1173 0.0748 -0.3517 138 GLN A OE1 1094 N NE2 . GLN A 138 ? 0.8578 1.5947 1.0930 0.0869 0.0471 -0.3127 138 GLN A NE2 1095 N N . GLY A 139 ? 0.9367 1.4249 1.0027 0.0868 0.0019 -0.3180 139 GLY A N 1096 C CA . GLY A 139 ? 0.9767 1.4178 1.0085 0.0935 -0.0056 -0.3313 139 GLY A CA 1097 C C . GLY A 139 ? 0.9861 1.4207 0.9773 0.0808 0.0099 -0.3382 139 GLY A C 1098 O O . GLY A 139 ? 1.0112 1.4034 0.9684 0.0807 0.0003 -0.3455 139 GLY A O 1099 N N . LYS A 140 ? 0.9649 1.4383 0.9568 0.0691 0.0325 -0.3356 140 LYS A N 1100 C CA . LYS A 140 ? 0.9942 1.4621 0.9444 0.0578 0.0495 -0.3421 140 LYS A CA 1101 C C . LYS A 140 ? 0.9600 1.4238 0.8955 0.0334 0.0455 -0.3200 140 LYS A C 1102 O O . LYS A 140 ? 0.9162 1.3943 0.8783 0.0252 0.0374 -0.3018 140 LYS A O 1103 C CB . LYS A 140 ? 1.0106 1.5231 0.9681 0.0611 0.0808 -0.3560 140 LYS A CB 1104 C CG . LYS A 140 ? 1.0587 1.5793 1.0272 0.0873 0.0904 -0.3819 140 LYS A CG 1105 C CD . LYS A 140 ? 1.0664 1.6474 1.0637 0.0899 0.1195 -0.3915 140 LYS A CD 1106 C CE . LYS A 140 ? 1.1335 1.7206 1.1151 0.1070 0.1424 -0.4197 140 LYS A CE 1107 N NZ . LYS A 140 ? 1.1717 1.7342 1.1631 0.1374 0.1285 -0.4372 140 LYS A NZ 1108 N N . SER A 141 ? 0.9791 1.4223 0.8702 0.0231 0.0511 -0.3220 141 SER A N 1109 C CA . SER A 141 ? 0.9490 1.3888 0.8228 0.0025 0.0496 -0.3027 141 SER A CA 1110 C C . SER A 141 ? 0.9274 1.4066 0.8108 -0.0081 0.0737 -0.2974 141 SER A C 1111 O O . SER A 141 ? 0.9480 1.4487 0.8264 -0.0049 0.0970 -0.3118 141 SER A O 1112 C CB . SER A 141 ? 0.9780 1.3823 0.7987 -0.0034 0.0468 -0.3073 141 SER A CB 1113 O OG . SER A 141 ? 1.0020 1.3689 0.8141 0.0027 0.0215 -0.3109 141 SER A OG 1114 N N . SER A 142 ? 0.8858 1.3745 0.7829 -0.0214 0.0690 -0.2773 142 SER A N 1115 C CA . SER A 142 ? 0.8674 1.3882 0.7720 -0.0340 0.0892 -0.2710 142 SER A CA 1116 C C . SER A 142 ? 0.8466 1.3523 0.7323 -0.0504 0.0841 -0.2512 142 SER A C 1117 O O . SER A 142 ? 0.8599 1.3334 0.7195 -0.0518 0.0701 -0.2459 142 SER A O 1118 C CB . SER A 142 ? 0.8493 1.4068 0.8036 -0.0287 0.0895 -0.2698 142 SER A CB 1119 O OG . SER A 142 ? 0.8478 1.4393 0.8101 -0.0411 0.1102 -0.2681 142 SER A OG 1120 N N . PHE A 143 ? 0.8150 1.3436 0.7139 -0.0623 0.0947 -0.2410 143 PHE A N 1121 C CA . PHE A 143 ? 0.8142 1.3275 0.6940 -0.0760 0.0922 -0.2235 143 PHE A CA 1122 C C . PHE A 143 ? 0.7973 1.3359 0.6994 -0.0868 0.1006 -0.2139 143 PHE A C 1123 O O . PHE A 143 ? 0.7992 1.3704 0.7280 -0.0865 0.1108 -0.2213 143 PHE A O 1124 C CB . PHE A 143 ? 0.8518 1.3435 0.6815 -0.0845 0.1045 -0.2254 143 PHE A CB 1125 C CG . PHE A 143 ? 0.8598 1.3234 0.6640 -0.0919 0.0944 -0.2089 143 PHE A CG 1126 C CD1 . PHE A 143 ? 0.8615 1.3039 0.6665 -0.0849 0.0707 -0.2023 143 PHE A CD1 1127 C CD2 . PHE A 143 ? 0.8650 1.3235 0.6454 -0.1058 0.1080 -0.2000 143 PHE A CD2 1128 C CE1 . PHE A 143 ? 0.8631 1.2847 0.6498 -0.0893 0.0610 -0.1877 143 PHE A CE1 1129 C CE2 . PHE A 143 ? 0.8745 1.3057 0.6320 -0.1091 0.0979 -0.1854 143 PHE A CE2 1130 C CZ . PHE A 143 ? 0.8702 1.2855 0.6329 -0.0997 0.0744 -0.1794 143 PHE A CZ 1131 N N . PHE A 144 ? 0.7905 1.3142 0.6822 -0.0956 0.0953 -0.1979 144 PHE A N 1132 C CA . PHE A 144 ? 0.7715 1.3108 0.6742 -0.1074 0.1034 -0.1891 144 PHE A CA 1133 C C . PHE A 144 ? 0.7893 1.3505 0.6864 -0.1186 0.1265 -0.1982 144 PHE A C 1134 O O . PHE A 144 ? 0.8448 1.3911 0.7058 -0.1267 0.1396 -0.2006 144 PHE A O 1135 C CB . PHE A 144 ? 0.7755 1.2880 0.6529 -0.1150 0.1001 -0.1739 144 PHE A CB 1136 C CG . PHE A 144 ? 0.7748 1.2722 0.6619 -0.1062 0.0795 -0.1639 144 PHE A CG 1137 C CD1 . PHE A 144 ? 0.7431 1.2543 0.6634 -0.1033 0.0701 -0.1574 144 PHE A CD1 1138 C CD2 . PHE A 144 ? 0.7914 1.2618 0.6540 -0.1019 0.0694 -0.1606 144 PHE A CD2 1139 C CE1 . PHE A 144 ? 0.7302 1.2302 0.6604 -0.0977 0.0536 -0.1479 144 PHE A CE1 1140 C CE2 . PHE A 144 ? 0.7676 1.2299 0.6443 -0.0956 0.0510 -0.1516 144 PHE A CE2 1141 C CZ . PHE A 144 ? 0.7429 1.2208 0.6541 -0.0942 0.0444 -0.1452 144 PHE A CZ 1142 N N . ARG A 145 ? 0.7648 1.3616 0.6974 -0.1200 0.1308 -0.2028 145 ARG A N 1143 C CA . ARG A 145 ? 0.7663 1.3942 0.7050 -0.1299 0.1519 -0.2137 145 ARG A CA 1144 C C . ARG A 145 ? 0.7967 1.4179 0.7080 -0.1528 0.1683 -0.2072 145 ARG A C 1145 O O . ARG A 145 ? 0.8376 1.4788 0.7445 -0.1646 0.1887 -0.2158 145 ARG A O 1146 C CB . ARG A 145 ? 0.7274 1.3979 0.7157 -0.1249 0.1481 -0.2191 145 ARG A CB 1147 C CG . ARG A 145 ? 0.7172 1.3940 0.7328 -0.1019 0.1330 -0.2268 145 ARG A CG 1148 C CD . ARG A 145 ? 0.7143 1.4383 0.7755 -0.0958 0.1348 -0.2367 145 ARG A CD 1149 N NE . ARG A 145 ? 0.7214 1.4465 0.8077 -0.0722 0.1185 -0.2430 145 ARG A NE 1150 C CZ . ARG A 145 ? 0.7530 1.4736 0.8364 -0.0563 0.1216 -0.2575 145 ARG A CZ 1151 N NH1 . ARG A 145 ? 0.7650 1.4806 0.8195 -0.0615 0.1411 -0.2670 145 ARG A NH1 1152 N NH2 . ARG A 145 ? 0.7730 1.4895 0.8783 -0.0351 0.1047 -0.2623 145 ARG A NH2 1153 N N . ASN A 146 ? 0.8106 1.4038 0.7038 -0.1594 0.1605 -0.1924 146 ASN A N 1154 C CA . ASN A 146 ? 0.8313 1.4126 0.6983 -0.1808 0.1738 -0.1856 146 ASN A CA 1155 C C . ASN A 146 ? 0.8787 1.4163 0.6922 -0.1862 0.1799 -0.1797 146 ASN A C 1156 O O . ASN A 146 ? 0.9125 1.4335 0.6964 -0.2045 0.1926 -0.1746 146 ASN A O 1157 C CB . ASN A 146 ? 0.7974 1.3735 0.6751 -0.1848 0.1633 -0.1743 146 ASN A CB 1158 C CG . ASN A 146 ? 0.7720 1.3902 0.6957 -0.1844 0.1587 -0.1793 146 ASN A CG 1159 O OD1 . ASN A 146 ? 0.7822 1.4368 0.7275 -0.1898 0.1692 -0.1903 146 ASN A OD1 1160 N ND2 . ASN A 146 ? 0.7589 1.3735 0.6977 -0.1776 0.1429 -0.1710 146 ASN A ND2 1161 N N . VAL A 147 ? 0.8894 1.4063 0.6884 -0.1709 0.1694 -0.1802 147 VAL A N 1162 C CA . VAL A 147 ? 0.9327 1.4077 0.6795 -0.1736 0.1715 -0.1747 147 VAL A CA 1163 C C . VAL A 147 ? 0.9439 1.4177 0.6749 -0.1659 0.1754 -0.1865 147 VAL A C 1164 O O . VAL A 147 ? 0.9285 1.4270 0.6907 -0.1531 0.1706 -0.1976 147 VAL A O 1165 C CB . VAL A 147 ? 0.9401 1.3822 0.6758 -0.1633 0.1514 -0.1610 147 VAL A CB 1166 C CG1 . VAL A 147 ? 0.9308 1.3662 0.6695 -0.1721 0.1521 -0.1502 147 VAL A CG1 1167 C CG2 . VAL A 147 ? 0.9127 1.3667 0.6830 -0.1448 0.1313 -0.1627 147 VAL A CG2 1168 N N . VAL A 148 ? 0.9969 1.4384 0.6756 -0.1736 0.1840 -0.1842 148 VAL A N 1169 C CA . VAL A 148 ? 1.0259 1.4626 0.6784 -0.1699 0.1921 -0.1962 148 VAL A CA 1170 C C . VAL A 148 ? 1.0455 1.4378 0.6577 -0.1598 0.1736 -0.1895 148 VAL A C 1171 O O . VAL A 148 ? 1.0831 1.4391 0.6554 -0.1666 0.1709 -0.1766 148 VAL A O 1172 C CB . VAL A 148 ? 1.0704 1.5080 0.6893 -0.1908 0.2212 -0.2000 148 VAL A CB 1173 C CG1 . VAL A 148 ? 1.1189 1.5496 0.7049 -0.1870 0.2319 -0.2129 148 VAL A CG1 1174 C CG2 . VAL A 148 ? 1.0475 1.5346 0.7111 -0.2026 0.2384 -0.2068 148 VAL A CG2 1175 N N . TRP A 149 ? 1.0323 1.4261 0.6551 -0.1434 0.1591 -0.1983 149 TRP A N 1176 C CA . TRP A 149 ? 1.0673 1.4227 0.6535 -0.1345 0.1397 -0.1944 149 TRP A CA 1177 C C . TRP A 149 ? 1.1352 1.4692 0.6646 -0.1406 0.1547 -0.2030 149 TRP A C 1178 O O . TRP A 149 ? 1.1496 1.4934 0.6781 -0.1338 0.1602 -0.2195 149 TRP A O 1179 C CB . TRP A 149 ? 1.0402 1.4043 0.6606 -0.1172 0.1172 -0.2007 149 TRP A CB 1180 C CG . TRP A 149 ? 1.0657 1.3955 0.6576 -0.1090 0.0929 -0.1966 149 TRP A CG 1181 C CD1 . TRP A 149 ? 1.1054 1.3978 0.6438 -0.1128 0.0876 -0.1881 149 TRP A CD1 1182 C CD2 . TRP A 149 ? 1.0513 1.3804 0.6661 -0.0963 0.0690 -0.2009 149 TRP A CD2 1183 N NE1 . TRP A 149 ? 1.1149 1.3877 0.6449 -0.1026 0.0606 -0.1873 149 TRP A NE1 1184 C CE2 . TRP A 149 ? 1.0769 1.3717 0.6535 -0.0937 0.0493 -0.1953 149 TRP A CE2 1185 C CE3 . TRP A 149 ? 1.0236 1.3758 0.6863 -0.0876 0.0610 -0.2084 149 TRP A CE3 1186 C CZ2 . TRP A 149 ? 1.0766 1.3630 0.6645 -0.0847 0.0225 -0.1976 149 TRP A CZ2 1187 C CZ3 . TRP A 149 ? 1.0272 1.3662 0.6976 -0.0790 0.0355 -0.2101 149 TRP A CZ3 1188 C CH2 . TRP A 149 ? 1.0484 1.3565 0.6829 -0.0786 0.0167 -0.2051 149 TRP A CH2 1189 N N . LEU A 150 ? 1.1801 1.4818 0.6590 -0.1532 0.1620 -0.1918 150 LEU A N 1190 C CA . LEU A 150 ? 1.2483 1.5253 0.6652 -0.1626 0.1787 -0.1970 150 LEU A CA 1191 C C . LEU A 150 ? 1.2880 1.5266 0.6623 -0.1510 0.1562 -0.1972 150 LEU A C 1192 O O . LEU A 150 ? 1.2794 1.4934 0.6480 -0.1439 0.1305 -0.1837 150 LEU A O 1193 C CB . LEU A 150 ? 1.2886 1.5397 0.6635 -0.1822 0.1937 -0.1828 150 LEU A CB 1194 C CG . LEU A 150 ? 1.2641 1.5487 0.6707 -0.1992 0.2180 -0.1829 150 LEU A CG 1195 C CD1 . LEU A 150 ? 1.3018 1.5502 0.6686 -0.2166 0.2238 -0.1656 150 LEU A CD1 1196 C CD2 . LEU A 150 ? 1.2784 1.5962 0.6875 -0.2093 0.2482 -0.2000 150 LEU A CD2 1197 N N . ILE A 151 ? 1.3239 1.5588 0.6691 -0.1491 0.1659 -0.2132 151 ILE A N 1198 C CA . ILE A 151 ? 1.3768 1.5716 0.6707 -0.1409 0.1464 -0.2157 151 ILE A CA 1199 C C . ILE A 151 ? 1.4505 1.6161 0.6686 -0.1533 0.1684 -0.2201 151 ILE A C 1200 O O . ILE A 151 ? 1.4494 1.6327 0.6619 -0.1679 0.2015 -0.2243 151 ILE A O 1201 C CB . ILE A 151 ? 1.3636 1.5727 0.6872 -0.1241 0.1316 -0.2331 151 ILE A CB 1202 C CG1 . ILE A 151 ? 1.3806 1.6182 0.7127 -0.1239 0.1607 -0.2551 151 ILE A CG1 1203 C CG2 . ILE A 151 ? 1.2872 1.5227 0.6819 -0.1140 0.1108 -0.2276 151 ILE A CG2 1204 C CD1 . ILE A 151 ? 1.3851 1.6243 0.7310 -0.1068 0.1471 -0.2739 151 ILE A CD1 1205 N N . LYS A 152 ? 1.5260 1.6478 0.6858 -0.1485 0.1497 -0.2192 152 LYS A N 1206 C CA . LYS A 152 ? 1.6225 1.7075 0.6988 -0.1601 0.1671 -0.2215 152 LYS A CA 1207 C C . LYS A 152 ? 1.6505 1.7606 0.7211 -0.1642 0.2018 -0.2442 152 LYS A C 1208 O O . LYS A 152 ? 1.6186 1.7611 0.7358 -0.1510 0.2016 -0.2622 152 LYS A O 1209 C CB . LYS A 152 ? 1.6703 1.7066 0.6896 -0.1510 0.1355 -0.2195 152 LYS A CB 1210 C CG . LYS A 152 ? 1.6680 1.7114 0.6989 -0.1362 0.1223 -0.2407 152 LYS A CG 1211 C CD . LYS A 152 ? 1.7202 1.7158 0.6970 -0.1292 0.0867 -0.2373 152 LYS A CD 1212 C CE . LYS A 152 ? 1.7356 1.7270 0.7026 -0.1188 0.0786 -0.2610 152 LYS A CE 1213 N NZ . LYS A 152 ? 1.7842 1.7334 0.7091 -0.1126 0.0378 -0.2569 152 LYS A NZ 1214 N N . LYS A 153 ? 1.7215 1.8149 0.7329 -0.1822 0.2316 -0.2432 153 LYS A N 1215 C CA . LYS A 153 ? 1.7595 1.8773 0.7596 -0.1876 0.2688 -0.2645 153 LYS A CA 1216 C C . LYS A 153 ? 1.8485 1.9161 0.7518 -0.1931 0.2750 -0.2688 153 LYS A C 1217 O O . LYS A 153 ? 1.8945 1.9204 0.7326 -0.2093 0.2787 -0.2518 153 LYS A O 1218 C CB . LYS A 153 ? 1.7522 1.9071 0.7769 -0.2083 0.3063 -0.2612 153 LYS A CB 1219 C CG . LYS A 153 ? 1.7638 1.9667 0.8102 -0.2096 0.3442 -0.2854 153 LYS A CG 1220 C CD . LYS A 153 ? 1.7540 2.0007 0.8356 -0.2314 0.3778 -0.2814 153 LYS A CD 1221 C CE . LYS A 153 ? 1.8217 2.0357 0.8266 -0.2602 0.4050 -0.2703 153 LYS A CE 1222 N NZ . LYS A 153 ? 1.8769 2.1059 0.8473 -0.2664 0.4431 -0.2903 153 LYS A NZ 1223 N N . ASN A 154 ? 1.8758 1.9440 0.7667 -0.1792 0.2756 -0.2916 154 ASN A N 1224 C CA . ASN A 154 ? 1.9850 2.0033 0.7815 -0.1816 0.2780 -0.2989 154 ASN A CA 1225 C C . ASN A 154 ? 2.0225 1.9780 0.7576 -0.1828 0.2401 -0.2775 154 ASN A C 1226 O O . ASN A 154 ? 2.0861 1.9950 0.7342 -0.1964 0.2479 -0.2690 154 ASN A O 1227 C CB . ASN A 154 ? 2.0472 2.0704 0.7948 -0.2025 0.3274 -0.3044 154 ASN A CB 1228 C CG . ASN A 154 ? 2.1519 2.1363 0.8117 -0.2014 0.3379 -0.3207 154 ASN A CG 1229 O OD1 . ASN A 154 ? 2.1800 2.1447 0.8279 -0.1827 0.3124 -0.3345 154 ASN A OD1 1230 N ND2 . ASN A 154 ? 2.2287 2.2004 0.8240 -0.2230 0.3759 -0.3193 154 ASN A ND2 1231 N N . SER A 155 ? 1.9630 1.9189 0.7449 -0.1683 0.1992 -0.2687 155 SER A N 1232 C CA . SER A 155 ? 1.9916 1.8972 0.7314 -0.1649 0.1581 -0.2496 155 SER A CA 1233 C C . SER A 155 ? 2.0243 1.8990 0.7221 -0.1810 0.1626 -0.2233 155 SER A C 1234 O O . SER A 155 ? 2.1122 1.9313 0.7295 -0.1848 0.1474 -0.2120 155 SER A O 1235 C CB . SER A 155 ? 2.0683 1.9269 0.7294 -0.1596 0.1414 -0.2612 155 SER A CB 1236 O OG . SER A 155 ? 2.0391 1.9185 0.7332 -0.1448 0.1359 -0.2862 155 SER A OG 1237 N N . THR A 156 ? 1.9660 1.8735 0.7150 -0.1903 0.1824 -0.2138 156 THR A N 1238 C CA . THR A 156 ? 1.9806 1.8586 0.7034 -0.2031 0.1812 -0.1879 156 THR A CA 1239 C C . THR A 156 ? 1.9025 1.8249 0.7113 -0.2034 0.1855 -0.1808 156 THR A C 1240 O O . THR A 156 ? 1.8914 1.8639 0.7516 -0.2093 0.2143 -0.1935 156 THR A O 1241 C CB . THR A 156 ? 2.0471 1.9001 0.6978 -0.2287 0.2200 -0.1832 156 THR A CB 1242 O OG1 . THR A 156 ? 2.0155 1.9242 0.7135 -0.2403 0.2618 -0.1980 156 THR A OG1 1243 C CG2 . THR A 156 ? 2.1443 1.9489 0.6979 -0.2317 0.2212 -0.1893 156 THR A CG2 1244 N N . TYR A 157 ? 1.8705 1.7751 0.6942 -0.1962 0.1567 -0.1612 157 TYR A N 1245 C CA . TYR A 157 ? 1.7841 1.7192 0.6737 -0.1987 0.1614 -0.1518 157 TYR A CA 1246 C C . TYR A 157 ? 1.8273 1.7136 0.6625 -0.2124 0.1642 -0.1290 157 TYR A C 1247 O O . TYR A 157 ? 1.8285 1.6799 0.6486 -0.2007 0.1330 -0.1127 157 TYR A O 1248 C CB . TYR A 157 ? 1.7200 1.6779 0.6788 -0.1768 0.1265 -0.1498 157 TYR A CB 1249 C CG . TYR A 157 ? 1.6423 1.6452 0.6811 -0.1771 0.1343 -0.1473 157 TYR A CG 1250 C CD1 . TYR A 157 ? 1.6432 1.6315 0.6788 -0.1870 0.1410 -0.1304 157 TYR A CD1 1251 C CD2 . TYR A 157 ? 1.5687 1.6242 0.6821 -0.1674 0.1336 -0.1618 157 TYR A CD2 1252 C CE1 . TYR A 157 ? 1.5818 1.6083 0.6855 -0.1876 0.1471 -0.1290 157 TYR A CE1 1253 C CE2 . TYR A 157 ? 1.5059 1.5997 0.6870 -0.1678 0.1391 -0.1590 157 TYR A CE2 1254 C CZ . TYR A 157 ? 1.5121 1.5921 0.6878 -0.1782 0.1461 -0.1431 157 TYR A CZ 1255 O OH . TYR A 157 ? 1.4345 1.5503 0.6732 -0.1791 0.1509 -0.1412 157 TYR A OH 1256 N N . PRO A 158 ? 1.8563 1.7386 0.6603 -0.2372 0.2014 -0.1280 158 PRO A N 1257 C CA . PRO A 158 ? 1.9042 1.7342 0.6521 -0.2527 0.2054 -0.1061 158 PRO A CA 1258 C C . PRO A 158 ? 1.8358 1.6792 0.6402 -0.2508 0.1986 -0.0949 158 PRO A C 1259 O O . PRO A 158 ? 1.7495 1.6495 0.6354 -0.2441 0.2007 -0.1053 158 PRO A O 1260 C CB . PRO A 158 ? 1.9539 1.7854 0.6609 -0.2826 0.2504 -0.1114 158 PRO A CB 1261 C CG . PRO A 158 ? 1.8911 1.7963 0.6690 -0.2817 0.2725 -0.1352 158 PRO A CG 1262 C CD . PRO A 158 ? 1.8537 1.7780 0.6705 -0.2524 0.2413 -0.1469 158 PRO A CD 1263 N N . THR A 159 ? 1.8813 1.6693 0.6390 -0.2559 0.1900 -0.0739 159 THR A N 1264 C CA . THR A 159 ? 1.8384 1.6295 0.6399 -0.2528 0.1826 -0.0632 159 THR A CA 1265 C C . THR A 159 ? 1.8002 1.6373 0.6486 -0.2750 0.2169 -0.0717 159 THR A C 1266 O O . THR A 159 ? 1.8220 1.6545 0.6346 -0.3020 0.2489 -0.0737 159 THR A O 1267 C CB . THR A 159 ? 1.9095 1.6249 0.6422 -0.2560 0.1711 -0.0398 159 THR A CB 1268 O OG1 . THR A 159 ? 1.9605 1.6316 0.6416 -0.2372 0.1396 -0.0316 159 THR A OG1 1269 C CG2 . THR A 159 ? 1.8671 1.5838 0.6471 -0.2455 0.1581 -0.0306 159 THR A CG2 1270 N N . ILE A 160 ? 1.7359 1.6192 0.6648 -0.2638 0.2095 -0.0768 160 ILE A N 1271 C CA . ILE A 160 ? 1.7023 1.6293 0.6814 -0.2823 0.2352 -0.0835 160 ILE A CA 1272 C C . ILE A 160 ? 1.7424 1.6273 0.7007 -0.2933 0.2350 -0.0667 160 ILE A C 1273 O O . ILE A 160 ? 1.7465 1.5980 0.6995 -0.2740 0.2083 -0.0548 160 ILE A O 1274 C CB . ILE A 160 ? 1.6020 1.5948 0.6733 -0.2645 0.2254 -0.0966 160 ILE A CB 1275 C CG1 . ILE A 160 ? 1.5849 1.6175 0.6763 -0.2554 0.2286 -0.1150 160 ILE A CG1 1276 C CG2 . ILE A 160 ? 1.5571 1.5893 0.6786 -0.2816 0.2456 -0.1007 160 ILE A CG2 1277 C CD1 . ILE A 160 ? 1.5069 1.5876 0.6749 -0.2327 0.2098 -0.1249 160 ILE A CD1 1278 N N . LYS A 161 ? 1.7863 1.6719 0.7319 -0.3243 0.2647 -0.0663 161 LYS A N 1279 C CA . LYS A 161 ? 1.8337 1.6813 0.7635 -0.3382 0.2668 -0.0528 161 LYS A CA 1280 C C . LYS A 161 ? 1.8106 1.7087 0.7882 -0.3642 0.2939 -0.0629 161 LYS A C 1281 O O . LYS A 161 ? 1.8623 1.7581 0.8104 -0.3960 0.3225 -0.0636 161 LYS A O 1282 C CB . LYS A 161 ? 1.9622 1.7291 0.7955 -0.3554 0.2722 -0.0356 161 LYS A CB 1283 C CG . LYS A 161 ? 2.0239 1.7287 0.8095 -0.3282 0.2388 -0.0208 161 LYS A CG 1284 C CD . LYS A 161 ? 2.1396 1.7667 0.8229 -0.3447 0.2445 -0.0051 161 LYS A CD 1285 C CE . LYS A 161 ? 2.1885 1.7595 0.8265 -0.3147 0.2079 0.0085 161 LYS A CE 1286 N NZ . LYS A 161 ? 2.3017 1.8010 0.8365 -0.3287 0.2115 0.0223 161 LYS A NZ 1287 N N . ARG A 162 ? 1.7462 1.6915 0.7981 -0.3512 0.2843 -0.0705 162 ARG A N 1288 C CA . ARG A 162 ? 1.7129 1.7126 0.8182 -0.3722 0.3046 -0.0812 162 ARG A CA 1289 C C . ARG A 162 ? 1.7052 1.6847 0.8226 -0.3768 0.2971 -0.0735 162 ARG A C 1290 O O . ARG A 162 ? 1.7212 1.6647 0.8313 -0.3540 0.2732 -0.0643 162 ARG A O 1291 C CB . ARG A 162 ? 1.6443 1.7205 0.8273 -0.3542 0.3008 -0.0985 162 ARG A CB 1292 C CG . ARG A 162 ? 1.6694 1.7820 0.8527 -0.3586 0.3192 -0.1119 162 ARG A CG 1293 C CD . ARG A 162 ? 1.7036 1.8422 0.8846 -0.3946 0.3541 -0.1177 162 ARG A CD 1294 N NE . ARG A 162 ? 1.6608 1.8798 0.9105 -0.3925 0.3671 -0.1372 162 ARG A NE 1295 C CZ . ARG A 162 ? 1.6752 1.9238 0.9342 -0.3781 0.3722 -0.1506 162 ARG A CZ 1296 N NH1 . ARG A 162 ? 1.7388 1.9440 0.9409 -0.3661 0.3651 -0.1470 162 ARG A NH1 1297 N NH2 . ARG A 162 ? 1.6377 1.9582 0.9621 -0.3746 0.3833 -0.1682 162 ARG A NH2 1298 N N . SER A 163 ? 1.6855 1.6902 0.8228 -0.4064 0.3177 -0.0784 163 SER A N 1299 C CA . SER A 163 ? 1.6461 1.6346 0.7958 -0.4141 0.3122 -0.0739 163 SER A CA 1300 C C . SER A 163 ? 1.5789 1.6382 0.7948 -0.4319 0.3255 -0.0878 163 SER A C 1301 O O . SER A 163 ? 1.5509 1.6526 0.7803 -0.4539 0.3480 -0.0967 163 SER A O 1302 C CB . SER A 163 ? 1.7246 1.6362 0.7989 -0.4400 0.3212 -0.0594 163 SER A CB 1303 O OG . SER A 163 ? 1.7404 1.6138 0.8114 -0.4352 0.3074 -0.0527 163 SER A OG 1304 N N . TYR A 164 ? 1.5372 1.6115 0.7952 -0.4210 0.3110 -0.0900 164 TYR A N 1305 C CA . TYR A 164 ? 1.4970 1.6284 0.8100 -0.4399 0.3200 -0.1010 164 TYR A CA 1306 C C . TYR A 164 ? 1.5425 1.6325 0.8367 -0.4558 0.3163 -0.0947 164 TYR A C 1307 O O . TYR A 164 ? 1.5670 1.6072 0.8381 -0.4359 0.2989 -0.0862 164 TYR A O 1308 C CB . TYR A 164 ? 1.3977 1.5945 0.7839 -0.4134 0.3063 -0.1121 164 TYR A CB 1309 C CG . TYR A 164 ? 1.3612 1.6102 0.8004 -0.4303 0.3104 -0.1217 164 TYR A CG 1310 C CD1 . TYR A 164 ? 1.3472 1.6548 0.8188 -0.4532 0.3297 -0.1327 164 TYR A CD1 1311 C CD2 . TYR A 164 ? 1.3545 1.5944 0.8100 -0.4239 0.2949 -0.1199 164 TYR A CD2 1312 C CE1 . TYR A 164 ? 1.3230 1.6803 0.8447 -0.4686 0.3307 -0.1413 164 TYR A CE1 1313 C CE2 . TYR A 164 ? 1.3245 1.6095 0.8242 -0.4402 0.2963 -0.1283 164 TYR A CE2 1314 C CZ . TYR A 164 ? 1.3169 1.6609 0.8504 -0.4625 0.3128 -0.1387 164 TYR A CZ 1315 O OH . TYR A 164 ? 1.3024 1.6932 0.8815 -0.4780 0.3111 -0.1469 164 TYR A OH 1316 N N . ASN A 165 ? 1.5765 1.6889 0.8820 -0.4917 0.3327 -0.1000 165 ASN A N 1317 C CA . ASN A 165 ? 1.6266 1.7021 0.9146 -0.5123 0.3305 -0.0964 165 ASN A CA 1318 C C . ASN A 165 ? 1.5386 1.6778 0.8939 -0.5154 0.3246 -0.1086 165 ASN A C 1319 O O . ASN A 165 ? 1.5063 1.7135 0.9074 -0.5323 0.3366 -0.1192 165 ASN A O 1320 C CB . ASN A 165 ? 1.7459 1.7896 0.9867 -0.5569 0.3527 -0.0917 165 ASN A CB 1321 C CG . ASN A 165 ? 1.8496 1.8352 1.0558 -0.5789 0.3492 -0.0864 165 ASN A CG 1322 O OD1 . ASN A 165 ? 1.8517 1.8344 1.0784 -0.5646 0.3327 -0.0894 165 ASN A OD1 1323 N ND2 . ASN A 165 ? 2.0240 1.9594 1.1733 -0.6149 0.3655 -0.0784 165 ASN A ND2 1324 N N . ASN A 166 ? 1.4955 1.6130 0.8561 -0.4983 0.3063 -0.1072 166 ASN A N 1325 C CA . ASN A 166 ? 1.4298 1.5985 0.8450 -0.5021 0.2988 -0.1175 166 ASN A CA 1326 C C . ASN A 166 ? 1.4603 1.6238 0.8649 -0.5460 0.3097 -0.1205 166 ASN A C 1327 O O . ASN A 166 ? 1.4895 1.5922 0.8527 -0.5571 0.3052 -0.1158 166 ASN A O 1328 C CB . ASN A 166 ? 1.3965 1.5416 0.8155 -0.4725 0.2781 -0.1153 166 ASN A CB 1329 C CG . ASN A 166 ? 1.3466 1.5461 0.8199 -0.4743 0.2690 -0.1254 166 ASN A CG 1330 O OD1 . ASN A 166 ? 1.2960 1.5605 0.8146 -0.4901 0.2749 -0.1344 166 ASN A OD1 1331 N ND2 . ASN A 166 ? 1.3426 1.5163 0.8111 -0.4573 0.2546 -0.1240 166 ASN A ND2 1332 N N . THR A 167 ? 1.4446 1.6729 0.8877 -0.5706 0.3240 -0.1292 167 THR A N 1333 C CA . THR A 167 ? 1.4739 1.7121 0.9175 -0.6161 0.3351 -0.1334 167 THR A CA 1334 C C . THR A 167 ? 1.4452 1.7299 0.9403 -0.6190 0.3202 -0.1435 167 THR A C 1335 O O . THR A 167 ? 1.4931 1.7788 0.9869 -0.6552 0.3230 -0.1472 167 THR A O 1336 C CB . THR A 167 ? 1.4635 1.7570 0.9292 -0.6422 0.3591 -0.1386 167 THR A CB 1337 O OG1 . THR A 167 ? 1.3817 1.7626 0.9199 -0.6208 0.3563 -0.1500 167 THR A OG1 1338 C CG2 . THR A 167 ? 1.5016 1.7454 0.9091 -0.6411 0.3741 -0.1283 167 THR A CG2 1339 N N . ASN A 168 ? 1.3764 1.6967 0.9137 -0.5823 0.3034 -0.1474 168 ASN A N 1340 C CA . ASN A 168 ? 1.3277 1.6917 0.9116 -0.5811 0.2872 -0.1559 168 ASN A CA 1341 C C . ASN A 168 ? 1.3692 1.6688 0.9116 -0.5858 0.2750 -0.1525 168 ASN A C 1342 O O . ASN A 168 ? 1.4225 1.6460 0.9072 -0.5771 0.2757 -0.1434 168 ASN A O 1343 C CB . ASN A 168 ? 1.2570 1.6661 0.8886 -0.5397 0.2729 -0.1589 168 ASN A CB 1344 C CG . ASN A 168 ? 1.2160 1.6810 0.8841 -0.5291 0.2838 -0.1632 168 ASN A CG 1345 O OD1 . ASN A 168 ? 1.1952 1.7289 0.9127 -0.5433 0.2897 -0.1729 168 ASN A OD1 1346 N ND2 . ASN A 168 ? 1.2033 1.6397 0.8478 -0.5032 0.2859 -0.1569 168 ASN A ND2 1347 N N . GLN A 169 ? 1.3529 1.6826 0.9241 -0.5979 0.2628 -0.1604 169 GLN A N 1348 C CA . GLN A 169 ? 1.3961 1.6685 0.9298 -0.5995 0.2501 -0.1596 169 GLN A CA 1349 C C . GLN A 169 ? 1.3576 1.6118 0.8899 -0.5548 0.2361 -0.1558 169 GLN A C 1350 O O . GLN A 169 ? 1.3897 1.5776 0.8757 -0.5459 0.2312 -0.1520 169 GLN A O 1351 C CB . GLN A 169 ? 1.4130 1.7251 0.9768 -0.6264 0.2395 -0.1699 169 GLN A CB 1352 C CG . GLN A 169 ? 1.4510 1.7988 1.0314 -0.6723 0.2519 -0.1752 169 GLN A CG 1353 C CD . GLN A 169 ? 1.5416 1.8230 1.0615 -0.6980 0.2709 -0.1676 169 GLN A CD 1354 O OE1 . GLN A 169 ? 1.6159 1.8185 1.0764 -0.7104 0.2687 -0.1641 169 GLN A OE1 1355 N NE2 . GLN A 169 ? 1.5530 1.8623 1.0843 -0.7052 0.2900 -0.1651 169 GLN A NE2 1356 N N . GLU A 170 ? 1.2876 1.6002 0.8703 -0.5270 0.2308 -0.1571 170 GLU A N 1357 C CA . GLU A 170 ? 1.2397 1.5523 0.8346 -0.4889 0.2163 -0.1547 170 GLU A CA 1358 C C . GLU A 170 ? 1.2357 1.5134 0.8087 -0.4578 0.2197 -0.1455 170 GLU A C 1359 O O . GLU A 170 ? 1.2634 1.5500 0.8376 -0.4573 0.2301 -0.1430 170 GLU A O 1360 C CB . GLU A 170 ? 1.1739 1.5668 0.8355 -0.4764 0.2064 -0.1607 170 GLU A CB 1361 C CG . GLU A 170 ? 1.1770 1.6169 0.8704 -0.5041 0.1997 -0.1700 170 GLU A CG 1362 C CD . GLU A 170 ? 1.1730 1.6610 0.8947 -0.5312 0.2131 -0.1757 170 GLU A CD 1363 O OE1 . GLU A 170 ? 1.2204 1.6831 0.9154 -0.5400 0.2307 -0.1717 170 GLU A OE1 1364 O OE2 . GLU A 170 ? 1.1356 1.6877 0.9064 -0.5434 0.2060 -0.1839 170 GLU A OE2 1365 N N . ASP A 171 ? 1.2447 1.4847 0.7982 -0.4321 0.2108 -0.1410 171 ASP A N 1366 C CA . ASP A 171 ? 1.2166 1.4332 0.7595 -0.3992 0.2099 -0.1328 171 ASP A CA 1367 C C . ASP A 171 ? 1.1612 1.4365 0.7512 -0.3843 0.2089 -0.1337 171 ASP A C 1368 O O . ASP A 171 ? 1.1048 1.4387 0.7419 -0.3860 0.2033 -0.1401 171 ASP A O 1369 C CB . ASP A 171 ? 1.2175 1.4135 0.7560 -0.3719 0.1993 -0.1303 171 ASP A CB 1370 C CG . ASP A 171 ? 1.2869 1.4106 0.7697 -0.3762 0.2016 -0.1287 171 ASP A CG 1371 O OD1 . ASP A 171 ? 1.3342 1.4121 0.7753 -0.3956 0.2103 -0.1268 171 ASP A OD1 1372 O OD2 . ASP A 171 ? 1.2859 1.3963 0.7648 -0.3594 0.1952 -0.1295 171 ASP A OD2 1373 N N . LEU A 172 ? 1.1777 1.4345 0.7528 -0.3687 0.2129 -0.1274 172 LEU A N 1374 C CA . LEU A 172 ? 1.1436 1.4470 0.7546 -0.3554 0.2129 -0.1291 172 LEU A CA 1375 C C . LEU A 172 ? 1.1239 1.4148 0.7368 -0.3208 0.2029 -0.1226 172 LEU A C 1376 O O . LEU A 172 ? 1.1650 1.4063 0.7390 -0.3113 0.2036 -0.1149 172 LEU A O 1377 C CB . LEU A 172 ? 1.1853 1.4837 0.7757 -0.3743 0.2284 -0.1293 172 LEU A CB 1378 C CG . LEU A 172 ? 1.1672 1.5230 0.7973 -0.3693 0.2327 -0.1357 172 LEU A CG 1379 C CD1 . LEU A 172 ? 1.1352 1.5547 0.8144 -0.3857 0.2343 -0.1464 172 LEU A CD1 1380 C CD2 . LEU A 172 ? 1.2122 1.5473 0.8075 -0.3810 0.2485 -0.1333 172 LEU A CD2 1381 N N . LEU A 173 ? 1.0599 1.3956 0.7186 -0.3026 0.1926 -0.1252 173 LEU A N 1382 C CA . LEU A 173 ? 1.0174 1.3514 0.6861 -0.2730 0.1830 -0.1199 173 LEU A CA 1383 C C . LEU A 173 ? 1.0080 1.3555 0.6801 -0.2689 0.1867 -0.1214 173 LEU A C 1384 O O . LEU A 173 ? 1.0006 1.3926 0.7038 -0.2749 0.1898 -0.1292 173 LEU A O 1385 C CB . LEU A 173 ? 0.9663 1.3397 0.6797 -0.2580 0.1708 -0.1217 173 LEU A CB 1386 C CG . LEU A 173 ? 0.9296 1.3112 0.6619 -0.2313 0.1606 -0.1174 173 LEU A CG 1387 C CD1 . LEU A 173 ? 0.9482 1.2858 0.6519 -0.2163 0.1580 -0.1086 173 LEU A CD1 1388 C CD2 . LEU A 173 ? 0.8870 1.3066 0.6616 -0.2210 0.1496 -0.1187 173 LEU A CD2 1389 N N . VAL A 174 ? 1.0198 1.3287 0.6596 -0.2574 0.1858 -0.1144 174 VAL A N 1390 C CA . VAL A 174 ? 1.0097 1.3233 0.6434 -0.2526 0.1881 -0.1154 174 VAL A CA 1391 C C . VAL A 174 ? 0.9718 1.2866 0.6199 -0.2244 0.1727 -0.1113 174 VAL A C 1392 O O . VAL A 174 ? 0.9805 1.2699 0.6202 -0.2101 0.1639 -0.1038 174 VAL A O 1393 C CB . VAL A 174 ? 1.0718 1.3354 0.6485 -0.2651 0.1983 -0.1098 174 VAL A CB 1394 C CG1 . VAL A 174 ? 1.0869 1.3592 0.6543 -0.2648 0.2036 -0.1127 174 VAL A CG1 1395 C CG2 . VAL A 174 ? 1.1106 1.3628 0.6677 -0.2955 0.2126 -0.1118 174 VAL A CG2 1396 N N . LEU A 175 ? 0.9424 1.2866 0.6120 -0.2169 0.1699 -0.1169 175 LEU A N 1397 C CA . LEU A 175 ? 0.9137 1.2618 0.5989 -0.1935 0.1544 -0.1143 175 LEU A CA 1398 C C . LEU A 175 ? 0.9387 1.2752 0.5997 -0.1905 0.1551 -0.1162 175 LEU A C 1399 O O . LEU A 175 ? 0.9542 1.3059 0.6110 -0.2029 0.1676 -0.1243 175 LEU A O 1400 C CB . LEU A 175 ? 0.8623 1.2567 0.5991 -0.1857 0.1469 -0.1206 175 LEU A CB 1401 C CG . LEU A 175 ? 0.8435 1.2527 0.6050 -0.1877 0.1442 -0.1190 175 LEU A CG 1402 C CD1 . LEU A 175 ? 0.8204 1.2753 0.6217 -0.1918 0.1442 -0.1279 175 LEU A CD1 1403 C CD2 . LEU A 175 ? 0.8168 1.2179 0.5900 -0.1695 0.1308 -0.1108 175 LEU A CD2 1404 N N . TRP A 176 ? 0.9461 1.2577 0.5918 -0.1741 0.1416 -0.1093 176 TRP A N 1405 C CA . TRP A 176 ? 0.9779 1.2777 0.6000 -0.1690 0.1379 -0.1113 176 TRP A CA 1406 C C . TRP A 176 ? 0.9607 1.2617 0.6003 -0.1473 0.1161 -0.1077 176 TRP A C 1407 O O . TRP A 176 ? 0.9303 1.2471 0.6047 -0.1377 0.1067 -0.1043 176 TRP A O 1408 C CB . TRP A 176 ? 1.0467 1.2992 0.6086 -0.1789 0.1459 -0.1048 176 TRP A CB 1409 C CG . TRP A 176 ? 1.0719 1.2839 0.6105 -0.1690 0.1359 -0.0922 176 TRP A CG 1410 C CD1 . TRP A 176 ? 1.1007 1.2846 0.6180 -0.1522 0.1192 -0.0844 176 TRP A CD1 1411 C CD2 . TRP A 176 ? 1.0752 1.2700 0.6093 -0.1741 0.1411 -0.0868 176 TRP A CD2 1412 N NE1 . TRP A 176 ? 1.1125 1.2647 0.6153 -0.1443 0.1143 -0.0744 176 TRP A NE1 1413 C CE2 . TRP A 176 ? 1.1083 1.2643 0.6190 -0.1575 0.1283 -0.0761 176 TRP A CE2 1414 C CE3 . TRP A 176 ? 1.0668 1.2749 0.6139 -0.1906 0.1543 -0.0907 176 TRP A CE3 1415 C CZ2 . TRP A 176 ? 1.1333 1.2611 0.6320 -0.1555 0.1301 -0.0700 176 TRP A CZ2 1416 C CZ3 . TRP A 176 ? 1.0888 1.2670 0.6209 -0.1910 0.1553 -0.0846 176 TRP A CZ3 1417 C CH2 . TRP A 176 ? 1.1194 1.2569 0.6270 -0.1728 0.1442 -0.0747 176 TRP A CH2 1418 N N . GLY A 177 ? 1.0002 1.2856 0.6154 -0.1411 0.1081 -0.1086 177 GLY A N 1419 C CA . GLY A 177 ? 0.9922 1.2802 0.6246 -0.1231 0.0857 -0.1059 177 GLY A CA 1420 C C . GLY A 177 ? 1.0408 1.2978 0.6318 -0.1169 0.0741 -0.1035 177 GLY A C 1421 O O . GLY A 177 ? 1.0849 1.3168 0.6290 -0.1268 0.0847 -0.1048 177 GLY A O 1422 N N . ILE A 178 ? 1.0354 1.2947 0.6436 -0.1017 0.0516 -0.0998 178 ILE A N 1423 C CA . ILE A 178 ? 1.0861 1.3194 0.6605 -0.0940 0.0344 -0.0974 178 ILE A CA 1424 C C . ILE A 178 ? 1.0705 1.3282 0.6776 -0.0868 0.0175 -0.1052 178 ILE A C 1425 O O . ILE A 178 ? 1.0253 1.3127 0.6830 -0.0821 0.0112 -0.1049 178 ILE A O 1426 C CB . ILE A 178 ? 1.1146 1.3222 0.6756 -0.0815 0.0194 -0.0833 178 ILE A CB 1427 C CG1 . ILE A 178 ? 1.1652 1.3490 0.6953 -0.0719 -0.0037 -0.0802 178 ILE A CG1 1428 C CG2 . ILE A 178 ? 1.0714 1.3075 0.6877 -0.0705 0.0107 -0.0783 178 ILE A CG2 1429 C CD1 . ILE A 178 ? 1.2436 1.3785 0.7030 -0.0769 0.0006 -0.0751 178 ILE A CD1 1430 N N . HIS A 179 ? 1.1008 1.3433 0.6759 -0.0872 0.0107 -0.1123 179 HIS A N 1431 C CA . HIS A 179 ? 1.0961 1.3532 0.6942 -0.0812 -0.0077 -0.1204 179 HIS A CA 1432 C C . HIS A 179 ? 1.1149 1.3562 0.7037 -0.0706 -0.0366 -0.1126 179 HIS A C 1433 O O . HIS A 179 ? 1.1731 1.3807 0.7118 -0.0691 -0.0426 -0.1076 179 HIS A O 1434 C CB . HIS A 179 ? 1.1276 1.3790 0.6980 -0.0873 0.0020 -0.1358 179 HIS A CB 1435 C CG . HIS A 179 ? 1.1286 1.3864 0.7145 -0.0814 -0.0175 -0.1455 179 HIS A CG 1436 N ND1 . HIS A 179 ? 1.1833 1.4164 0.7252 -0.0809 -0.0259 -0.1546 179 HIS A ND1 1437 C CD2 . HIS A 179 ? 1.0948 1.3771 0.7318 -0.0770 -0.0309 -0.1473 179 HIS A CD2 1438 C CE1 . HIS A 179 ? 1.1804 1.4220 0.7466 -0.0764 -0.0441 -0.1626 179 HIS A CE1 1439 N NE2 . HIS A 179 ? 1.1298 1.4009 0.7542 -0.0744 -0.0474 -0.1579 179 HIS A NE2 1440 N N . HIS A 180 ? 1.0704 1.3364 0.7078 -0.0643 -0.0549 -0.1112 180 HIS A N 1441 C CA . HIS A 180 ? 1.0846 1.3464 0.7269 -0.0550 -0.0844 -0.1046 180 HIS A CA 1442 C C . HIS A 180 ? 1.0958 1.3599 0.7412 -0.0572 -0.1017 -0.1162 180 HIS A C 1443 O O . HIS A 180 ? 1.0646 1.3550 0.7576 -0.0584 -0.1087 -0.1191 180 HIS A O 1444 C CB . HIS A 180 ? 1.0428 1.3347 0.7420 -0.0482 -0.0914 -0.0943 180 HIS A CB 1445 C CG . HIS A 180 ? 1.0277 1.3145 0.7236 -0.0441 -0.0762 -0.0839 180 HIS A CG 1446 N ND1 . HIS A 180 ? 1.0752 1.3282 0.7253 -0.0384 -0.0780 -0.0764 180 HIS A ND1 1447 C CD2 . HIS A 180 ? 0.9827 1.2898 0.7116 -0.0449 -0.0597 -0.0801 180 HIS A CD2 1448 C CE1 . HIS A 180 ? 1.0484 1.2995 0.7040 -0.0356 -0.0631 -0.0690 180 HIS A CE1 1449 N NE2 . HIS A 180 ? 1.0029 1.2874 0.7057 -0.0397 -0.0516 -0.0716 180 HIS A NE2 1450 N N . PRO A 181 ? 1.1540 1.3871 0.7452 -0.0585 -0.1086 -0.1230 181 PRO A N 1451 C CA . PRO A 181 ? 1.1732 1.4035 0.7613 -0.0613 -0.1222 -0.1370 181 PRO A CA 1452 C C . PRO A 181 ? 1.1668 1.4069 0.7840 -0.0577 -0.1564 -0.1336 181 PRO A C 1453 O O . PRO A 181 ? 1.1485 1.3958 0.7810 -0.0511 -0.1716 -0.1203 181 PRO A O 1454 C CB . PRO A 181 ? 1.2461 1.4373 0.7605 -0.0638 -0.1184 -0.1446 181 PRO A CB 1455 C CG . PRO A 181 ? 1.2681 1.4407 0.7476 -0.0635 -0.1045 -0.1324 181 PRO A CG 1456 C CD . PRO A 181 ? 1.2215 1.4170 0.7491 -0.0574 -0.1073 -0.1177 181 PRO A CD 1457 N N . LYS A 182 ? 1.1733 1.4136 0.7982 -0.0620 -0.1682 -0.1462 182 LYS A N 1458 C CA . LYS A 182 ? 1.1893 1.4405 0.8452 -0.0628 -0.2006 -0.1449 182 LYS A CA 1459 C C . LYS A 182 ? 1.2351 1.4630 0.8521 -0.0596 -0.2304 -0.1426 182 LYS A C 1460 O O . LYS A 182 ? 1.2292 1.4748 0.8795 -0.0581 -0.2574 -0.1348 182 LYS A O 1461 C CB . LYS A 182 ? 1.2065 1.4578 0.8775 -0.0698 -0.2044 -0.1599 182 LYS A CB 1462 C CG . LYS A 182 ? 1.2769 1.4924 0.8888 -0.0710 -0.2004 -0.1780 182 LYS A CG 1463 C CD . LYS A 182 ? 1.2917 1.5059 0.9220 -0.0751 -0.2021 -0.1932 182 LYS A CD 1464 C CE . LYS A 182 ? 1.3572 1.5349 0.9279 -0.0742 -0.1985 -0.2132 182 LYS A CE 1465 N NZ . LYS A 182 ? 1.3696 1.5392 0.9554 -0.0764 -0.2064 -0.2286 182 LYS A NZ 1466 N N . ASP A 183 ? 1.2782 1.4681 0.8256 -0.0591 -0.2261 -0.1491 183 ASP A N 1467 C CA . ASP A 183 ? 1.3419 1.5042 0.8434 -0.0562 -0.2561 -0.1474 183 ASP A CA 1468 C C . ASP A 183 ? 1.3880 1.5082 0.8094 -0.0544 -0.2440 -0.1472 183 ASP A C 1469 O O . ASP A 183 ? 1.3798 1.4925 0.7797 -0.0574 -0.2105 -0.1508 183 ASP A O 1470 C CB . ASP A 183 ? 1.3629 1.5157 0.8597 -0.0629 -0.2825 -0.1619 183 ASP A CB 1471 C CG . ASP A 183 ? 1.3820 1.5112 0.8419 -0.0683 -0.2631 -0.1822 183 ASP A CG 1472 O OD1 . ASP A 183 ? 1.4142 1.5192 0.8201 -0.0672 -0.2391 -0.1866 183 ASP A OD1 1473 O OD2 . ASP A 183 ? 1.3640 1.4979 0.8486 -0.0737 -0.2718 -0.1942 183 ASP A OD2 1474 N N . ALA A 184 ? 1.4421 1.5359 0.8202 -0.0504 -0.2724 -0.1422 184 ALA A N 1475 C CA . ALA A 184 ? 1.5060 1.5535 0.7999 -0.0496 -0.2659 -0.1401 184 ALA A CA 1476 C C . ALA A 184 ? 1.5397 1.5604 0.7785 -0.0586 -0.2423 -0.1587 184 ALA A C 1477 O O . ALA A 184 ? 1.5682 1.5628 0.7523 -0.0616 -0.2171 -0.1575 184 ALA A O 1478 C CB . ALA A 184 ? 1.5529 1.5766 0.8110 -0.0436 -0.3070 -0.1329 184 ALA A CB 1479 N N . ALA A 185 ? 1.5343 1.5609 0.7876 -0.0631 -0.2499 -0.1761 185 ALA A N 1480 C CA . ALA A 185 ? 1.5655 1.5691 0.7715 -0.0688 -0.2284 -0.1966 185 ALA A CA 1481 C C . ALA A 185 ? 1.5275 1.5512 0.7543 -0.0710 -0.1842 -0.2005 185 ALA A C 1482 O O . ALA A 185 ? 1.5578 1.5613 0.7321 -0.0748 -0.1567 -0.2075 185 ALA A O 1483 C CB . ALA A 185 ? 1.5663 1.5703 0.7887 -0.0714 -0.2486 -0.2143 185 ALA A CB 1484 N N . GLU A 186 ? 1.4618 1.5266 0.7649 -0.0695 -0.1778 -0.1958 186 GLU A N 1485 C CA . GLU A 186 ? 1.4360 1.5242 0.7660 -0.0715 -0.1398 -0.1989 186 GLU A CA 1486 C C . GLU A 186 ? 1.4341 1.5137 0.7333 -0.0741 -0.1161 -0.1863 186 GLU A C 1487 O O . GLU A 186 ? 1.4211 1.5017 0.7023 -0.0793 -0.0830 -0.1934 186 GLU A O 1488 C CB . GLU A 186 ? 1.3790 1.5096 0.7929 -0.0696 -0.1416 -0.1937 186 GLU A CB 1489 C CG . GLU A 186 ? 1.3502 1.5046 0.7954 -0.0709 -0.1105 -0.2035 186 GLU A CG 1490 C CD . GLU A 186 ? 1.3886 1.5332 0.8222 -0.0698 -0.1078 -0.2260 186 GLU A CD 1491 O OE1 . GLU A 186 ? 1.4440 1.5627 0.8481 -0.0695 -0.1316 -0.2347 186 GLU A OE1 1492 O OE2 . GLU A 186 ? 1.3940 1.5563 0.8478 -0.0686 -0.0823 -0.2355 186 GLU A OE2 1493 N N . GLN A 187 ? 1.4403 1.5110 0.7337 -0.0705 -0.1338 -0.1678 187 GLN A N 1494 C CA . GLN A 187 ? 1.4603 1.5129 0.7176 -0.0728 -0.1160 -0.1542 187 GLN A CA 1495 C C . GLN A 187 ? 1.5267 1.5411 0.7023 -0.0809 -0.0976 -0.1619 187 GLN A C 1496 O O . GLN A 187 ? 1.5188 1.5341 0.6796 -0.0894 -0.0636 -0.1628 187 GLN A O 1497 C CB . GLN A 187 ? 1.4771 1.5171 0.7313 -0.0641 -0.1447 -0.1349 187 GLN A CB 1498 C CG . GLN A 187 ? 1.5106 1.5199 0.7175 -0.0652 -0.1316 -0.1198 187 GLN A CG 1499 C CD . GLN A 187 ? 1.4595 1.4902 0.7002 -0.0701 -0.0996 -0.1150 187 GLN A CD 1500 O OE1 . GLN A 187 ? 1.3835 1.4509 0.6921 -0.0652 -0.1007 -0.1118 187 GLN A OE1 1501 N NE2 . GLN A 187 ? 1.4891 1.4961 0.6804 -0.0814 -0.0709 -0.1144 187 GLN A NE2 1502 N N . THR A 188 ? 1.5815 1.5632 0.7036 -0.0796 -0.1198 -0.1677 188 THR A N 1503 C CA . THR A 188 ? 1.6516 1.5945 0.6898 -0.0876 -0.1022 -0.1758 188 THR A CA 1504 C C . THR A 188 ? 1.6383 1.5996 0.6849 -0.0926 -0.0716 -0.1984 188 THR A C 1505 O O . THR A 188 ? 1.6633 1.6165 0.6716 -0.1016 -0.0375 -0.2033 188 THR A O 1506 C CB . THR A 188 ? 1.7280 1.6272 0.6995 -0.0848 -0.1356 -0.1765 188 THR A CB 1507 O OG1 . THR A 188 ? 1.7257 1.6345 0.7193 -0.0811 -0.1572 -0.1931 188 THR A OG1 1508 C CG2 . THR A 188 ? 1.7383 1.6232 0.7074 -0.0767 -0.1685 -0.1541 188 THR A CG2 1509 N N . LYS A 189 ? 1.5975 1.5846 0.6965 -0.0868 -0.0829 -0.2117 189 LYS A N 1510 C CA . LYS A 189 ? 1.5931 1.5974 0.7052 -0.0875 -0.0572 -0.2338 189 LYS A CA 1511 C C . LYS A 189 ? 1.5499 1.5864 0.6936 -0.0927 -0.0174 -0.2328 189 LYS A C 1512 O O . LYS A 189 ? 1.5550 1.5945 0.6760 -0.0967 0.0134 -0.2476 189 LYS A O 1513 C CB . LYS A 189 ? 1.5707 1.5962 0.7420 -0.0800 -0.0786 -0.2441 189 LYS A CB 1514 C CG . LYS A 189 ? 1.5827 1.6239 0.7719 -0.0770 -0.0556 -0.2669 189 LYS A CG 1515 C CD . LYS A 189 ? 1.5700 1.6235 0.8122 -0.0705 -0.0800 -0.2750 189 LYS A CD 1516 C CE . LYS A 189 ? 1.5662 1.6377 0.8356 -0.0645 -0.0570 -0.2952 189 LYS A CE 1517 N NZ . LYS A 189 ? 1.5424 1.6240 0.8667 -0.0594 -0.0800 -0.2996 189 LYS A NZ 1518 N N . LEU A 190 ? 1.4945 1.5565 0.6910 -0.0928 -0.0184 -0.2163 190 LEU A N 1519 C CA . LEU A 190 ? 1.4640 1.5582 0.6954 -0.0988 0.0150 -0.2145 190 LEU A CA 1520 C C . LEU A 190 ? 1.5123 1.5868 0.6963 -0.1106 0.0357 -0.2015 190 LEU A C 1521 O O . LEU A 190 ? 1.5076 1.5969 0.6883 -0.1204 0.0698 -0.2071 190 LEU A O 1522 C CB . LEU A 190 ? 1.3762 1.5059 0.6858 -0.0940 0.0049 -0.2042 190 LEU A CB 1523 C CG . LEU A 190 ? 1.3325 1.4858 0.6976 -0.0851 -0.0111 -0.2148 190 LEU A CG 1524 C CD1 . LEU A 190 ? 1.2625 1.4465 0.6952 -0.0826 -0.0196 -0.2012 190 LEU A CD1 1525 C CD2 . LEU A 190 ? 1.3263 1.4973 0.7022 -0.0837 0.0125 -0.2357 190 LEU A CD2 1526 N N . TYR A 191 ? 1.5590 1.6002 0.7079 -0.1098 0.0145 -0.1842 191 TYR A N 1527 C CA . TYR A 191 ? 1.5962 1.6141 0.7053 -0.1202 0.0297 -0.1681 191 TYR A CA 1528 C C . TYR A 191 ? 1.7002 1.6616 0.7186 -0.1240 0.0208 -0.1606 191 TYR A C 1529 O O . TYR A 191 ? 1.7594 1.6938 0.7372 -0.1334 0.0327 -0.1463 191 TYR A O 1530 C CB . TYR A 191 ? 1.5465 1.5753 0.7017 -0.1146 0.0157 -0.1498 191 TYR A CB 1531 C CG . TYR A 191 ? 1.4571 1.5370 0.6980 -0.1096 0.0182 -0.1548 191 TYR A CG 1532 C CD1 . TYR A 191 ? 1.4239 1.5355 0.6953 -0.1187 0.0496 -0.1623 191 TYR A CD1 1533 C CD2 . TYR A 191 ? 1.4079 1.5048 0.6985 -0.0969 -0.0112 -0.1519 191 TYR A CD2 1534 C CE1 . TYR A 191 ? 1.3437 1.4987 0.6887 -0.1138 0.0500 -0.1660 191 TYR A CE1 1535 C CE2 . TYR A 191 ? 1.3335 1.4731 0.6966 -0.0937 -0.0084 -0.1554 191 TYR A CE2 1536 C CZ . TYR A 191 ? 1.2958 1.4622 0.6835 -0.1016 0.0215 -0.1621 191 TYR A CZ 1537 O OH . TYR A 191 ? 1.2184 1.4239 0.6733 -0.0981 0.0226 -0.1647 191 TYR A OH 1538 N N . GLN A 192 ? 1.7295 1.6697 0.7129 -0.1177 -0.0009 -0.1698 192 GLN A N 1539 C CA . GLN A 192 ? 1.8168 1.7008 0.7107 -0.1199 -0.0151 -0.1626 192 GLN A CA 1540 C C . GLN A 192 ? 1.8246 1.6823 0.7088 -0.1116 -0.0476 -0.1395 192 GLN A C 1541 O O . GLN A 192 ? 1.8343 1.6763 0.7078 -0.1007 -0.0855 -0.1370 192 GLN A O 1542 C CB . GLN A 192 ? 1.8800 1.7380 0.7042 -0.1374 0.0224 -0.1631 192 GLN A CB 1543 C CG . GLN A 192 ? 1.8889 1.7627 0.7006 -0.1436 0.0517 -0.1875 192 GLN A CG 1544 C CD . GLN A 192 ? 1.9530 1.7839 0.6851 -0.1424 0.0391 -0.1973 192 GLN A CD 1545 O OE1 . GLN A 192 ? 1.9453 1.7754 0.6886 -0.1304 0.0096 -0.2074 192 GLN A OE1 1546 N NE2 . GLN A 192 ? 2.0378 1.8308 0.6863 -0.1564 0.0614 -0.1944 192 GLN A NE2 1547 N N . ASN A 193 ? 1.8077 1.6601 0.6950 -0.1166 -0.0330 -0.1233 193 ASN A N 1548 C CA . ASN A 193 ? 1.8312 1.6525 0.7013 -0.1076 -0.0591 -0.1011 193 ASN A CA 1549 C C . ASN A 193 ? 1.7740 1.6262 0.7156 -0.0889 -0.0946 -0.0976 193 ASN A C 1550 O O . ASN A 193 ? 1.6833 1.5838 0.7023 -0.0864 -0.0870 -0.1034 193 ASN A O 1551 C CB . ASN A 193 ? 1.8247 1.6378 0.6937 -0.1168 -0.0334 -0.0874 193 ASN A CB 1552 C CG . ASN A 193 ? 1.8854 1.6722 0.6882 -0.1389 0.0041 -0.0901 193 ASN A CG 1553 O OD1 . ASN A 193 ? 1.9748 1.7087 0.6926 -0.1446 0.0005 -0.0831 193 ASN A OD1 1554 N ND2 . ASN A 193 ? 1.8352 1.6601 0.6766 -0.1522 0.0401 -0.1001 193 ASN A ND2 1555 N N . PRO A 194 ? 1.8286 1.6545 0.7444 -0.0764 -0.1338 -0.0882 194 PRO A N 1556 C CA . PRO A 194 ? 1.7810 1.6407 0.7665 -0.0600 -0.1679 -0.0856 194 PRO A CA 1557 C C . PRO A 194 ? 1.7320 1.6111 0.7718 -0.0506 -0.1663 -0.0707 194 PRO A C 1558 O O . PRO A 194 ? 1.6542 1.5805 0.7733 -0.0434 -0.1731 -0.0732 194 PRO A O 1559 C CB . PRO A 194 ? 1.8560 1.6781 0.7887 -0.0507 -0.2088 -0.0787 194 PRO A CB 1560 C CG . PRO A 194 ? 1.9374 1.6995 0.7775 -0.0574 -0.1970 -0.0674 194 PRO A CG 1561 C CD . PRO A 194 ? 1.9278 1.6920 0.7495 -0.0769 -0.1488 -0.0779 194 PRO A CD 1562 N N . THR A 195 ? 1.7760 1.6157 0.7695 -0.0514 -0.1566 -0.0556 195 THR A N 1563 C CA . THR A 195 ? 1.7403 1.5883 0.7731 -0.0423 -0.1528 -0.0422 195 THR A CA 1564 C C . THR A 195 ? 1.7219 1.5671 0.7470 -0.0596 -0.1099 -0.0435 195 THR A C 1565 O O . THR A 195 ? 1.7885 1.5926 0.7431 -0.0743 -0.0910 -0.0415 195 THR A O 1566 C CB . THR A 195 ? 1.8036 1.6023 0.7882 -0.0276 -0.1786 -0.0228 195 THR A CB 1567 O OG1 . THR A 195 ? 1.8079 1.6120 0.7999 -0.0121 -0.2209 -0.0218 195 THR A OG1 1568 C CG2 . THR A 195 ? 1.7838 1.5889 0.8091 -0.0153 -0.1747 -0.0105 195 THR A CG2 1569 N N . THR A 196 ? 1.6425 1.5318 0.7392 -0.0592 -0.0947 -0.0469 196 THR A N 1570 C CA . THR A 196 ? 1.6172 1.5117 0.7158 -0.0767 -0.0561 -0.0498 196 THR A CA 1571 C C . THR A 196 ? 1.5620 1.4715 0.7091 -0.0693 -0.0513 -0.0415 196 THR A C 1572 O O . THR A 196 ? 1.5262 1.4464 0.7096 -0.0496 -0.0756 -0.0343 196 THR A O 1573 C CB . THR A 196 ? 1.5734 1.5133 0.7093 -0.0889 -0.0352 -0.0690 196 THR A CB 1574 O OG1 . THR A 196 ? 1.5089 1.4977 0.7227 -0.0769 -0.0504 -0.0746 196 THR A OG1 1575 C CG2 . THR A 196 ? 1.6241 1.5472 0.7085 -0.0960 -0.0359 -0.0799 196 THR A CG2 1576 N N . TYR A 197 ? 1.5504 1.4619 0.6979 -0.0857 -0.0194 -0.0432 197 TYR A N 1577 C CA . TYR A 197 ? 1.5031 1.4244 0.6889 -0.0818 -0.0111 -0.0371 197 TYR A CA 1578 C C . TYR A 197 ? 1.4926 1.4320 0.6900 -0.1041 0.0238 -0.0450 197 TYR A C 1579 O O . TYR A 197 ? 1.5086 1.4462 0.6764 -0.1225 0.0431 -0.0529 197 TYR A O 1580 C CB . TYR A 197 ? 1.5592 1.4224 0.6947 -0.0738 -0.0199 -0.0200 197 TYR A CB 1581 C CG . TYR A 197 ? 1.6249 1.4333 0.6788 -0.0944 -0.0011 -0.0146 197 TYR A CG 1582 C CD1 . TYR A 197 ? 1.6937 1.4705 0.6846 -0.0995 -0.0083 -0.0137 197 TYR A CD1 1583 C CD2 . TYR A 197 ? 1.6236 1.4102 0.6607 -0.1106 0.0240 -0.0104 197 TYR A CD2 1584 C CE1 . TYR A 197 ? 1.7572 1.4833 0.6707 -0.1204 0.0109 -0.0079 197 TYR A CE1 1585 C CE2 . TYR A 197 ? 1.6970 1.4334 0.6596 -0.1326 0.0423 -0.0046 197 TYR A CE2 1586 C CZ . TYR A 197 ? 1.7711 1.4779 0.6719 -0.1375 0.0366 -0.0030 197 TYR A CZ 1587 O OH . TYR A 197 ? 1.8324 1.4888 0.6563 -0.1614 0.0567 0.0036 197 TYR A OH 1588 N N . ILE A 198 ? 1.4642 1.4232 0.7060 -0.1021 0.0317 -0.0435 198 ILE A N 1589 C CA . ILE A 198 ? 1.4650 1.4325 0.7117 -0.1233 0.0618 -0.0479 198 ILE A CA 1590 C C . ILE A 198 ? 1.4862 1.4197 0.7205 -0.1199 0.0634 -0.0363 198 ILE A C 1591 O O . ILE A 198 ? 1.4585 1.4043 0.7317 -0.1006 0.0494 -0.0327 198 ILE A O 1592 C CB . ILE A 198 ? 1.4050 1.4356 0.7239 -0.1258 0.0708 -0.0607 198 ILE A CB 1593 C CG1 . ILE A 198 ? 1.3790 1.4424 0.7166 -0.1241 0.0654 -0.0729 198 ILE A CG1 1594 C CG2 . ILE A 198 ? 1.4104 1.4508 0.7315 -0.1491 0.1001 -0.0657 198 ILE A CG2 1595 C CD1 . ILE A 198 ? 1.3060 1.4255 0.7165 -0.1194 0.0648 -0.0824 198 ILE A CD1 1596 N N . SER A 199 ? 1.5292 1.4186 0.7082 -0.1390 0.0810 -0.0308 199 SER A N 1597 C CA . SER A 199 ? 1.5459 1.3955 0.7066 -0.1381 0.0841 -0.0210 199 SER A CA 1598 C C . SER A 199 ? 1.5023 1.3697 0.6793 -0.1634 0.1116 -0.0281 199 SER A C 1599 O O . SER A 199 ? 1.4959 1.3688 0.6534 -0.1890 0.1322 -0.0336 199 SER A O 1600 C CB . SER A 199 ? 1.6418 1.4156 0.7203 -0.1399 0.0788 -0.0067 199 SER A CB 1601 O OG . SER A 199 ? 1.6928 1.4448 0.7218 -0.1709 0.1028 -0.0076 199 SER A OG 1602 N N . VAL A 200 ? 1.4756 1.3544 0.6896 -0.1559 0.1115 -0.0287 200 VAL A N 1603 C CA . VAL A 200 ? 1.4463 1.3455 0.6814 -0.1780 0.1333 -0.0360 200 VAL A CA 1604 C C . VAL A 200 ? 1.4830 1.3313 0.6898 -0.1779 0.1353 -0.0281 200 VAL A C 1605 O O . VAL A 200 ? 1.4851 1.3149 0.6972 -0.1517 0.1189 -0.0220 200 VAL A O 1606 C CB . VAL A 200 ? 1.3671 1.3346 0.6786 -0.1702 0.1319 -0.0468 200 VAL A CB 1607 C CG1 . VAL A 200 ? 1.3497 1.3472 0.6813 -0.1969 0.1538 -0.0563 200 VAL A CG1 1608 C CG2 . VAL A 200 ? 1.3323 1.3408 0.6743 -0.1581 0.1200 -0.0525 200 VAL A CG2 1609 N N . GLY A 201 ? 1.5210 1.3470 0.6986 -0.2073 0.1555 -0.0290 201 GLY A N 1610 C CA . GLY A 201 ? 1.5735 1.3456 0.7194 -0.2109 0.1586 -0.0230 201 GLY A CA 1611 C C . GLY A 201 ? 1.5635 1.3476 0.7172 -0.2427 0.1797 -0.0308 201 GLY A C 1612 O O . GLY A 201 ? 1.5581 1.3693 0.7139 -0.2702 0.1960 -0.0366 201 GLY A O 1613 N N . THR A 202 ? 1.5659 1.3319 0.7254 -0.2382 0.1789 -0.0317 202 THR A N 1614 C CA . THR A 202 ? 1.5773 1.3373 0.7310 -0.2690 0.1955 -0.0375 202 THR A CA 1615 C C . THR A 202 ? 1.6633 1.3422 0.7628 -0.2655 0.1926 -0.0296 202 THR A C 1616 O O . THR A 202 ? 1.7145 1.3394 0.7719 -0.2462 0.1812 -0.0184 202 THR A O 1617 C CB . THR A 202 ? 1.4874 1.3117 0.7071 -0.2678 0.1970 -0.0497 202 THR A CB 1618 O OG1 . THR A 202 ? 1.4596 1.2733 0.6943 -0.2376 0.1846 -0.0488 202 THR A OG1 1619 C CG2 . THR A 202 ? 1.4162 1.3155 0.6905 -0.2638 0.1960 -0.0569 202 THR A CG2 1620 N N . SER A 203 ? 1.6867 1.3546 0.7853 -0.2832 0.2015 -0.0357 203 SER A N 1621 C CA . SER A 203 ? 1.7772 1.3669 0.8265 -0.2780 0.1986 -0.0307 203 SER A CA 1622 C C . SER A 203 ? 1.7637 1.3484 0.8326 -0.2328 0.1822 -0.0293 203 SER A C 1623 O O . SER A 203 ? 1.8341 1.3518 0.8591 -0.2130 0.1735 -0.0208 203 SER A O 1624 C CB . SER A 203 ? 1.7943 1.3786 0.8421 -0.3077 0.2107 -0.0398 203 SER A CB 1625 O OG . SER A 203 ? 1.8961 1.3914 0.8807 -0.3110 0.2104 -0.0344 203 SER A OG 1626 N N . THR A 204 ? 1.6849 1.3410 0.8201 -0.2167 0.1784 -0.0375 204 THR A N 1627 C CA . THR A 204 ? 1.6571 1.3214 0.8205 -0.1762 0.1656 -0.0374 204 THR A CA 1628 C C . THR A 204 ? 1.6254 1.3282 0.8210 -0.1493 0.1511 -0.0323 204 THR A C 1629 O O . THR A 204 ? 1.6400 1.3343 0.8451 -0.1149 0.1382 -0.0283 204 THR A O 1630 C CB . THR A 204 ? 1.5847 1.2998 0.7988 -0.1753 0.1705 -0.0491 204 THR A CB 1631 O OG1 . THR A 204 ? 1.4953 1.2875 0.7625 -0.1858 0.1722 -0.0544 204 THR A OG1 1632 C CG2 . THR A 204 ? 1.6197 1.2993 0.8033 -0.2027 0.1827 -0.0557 204 THR A CG2 1633 N N . LEU A 205 ? 1.5852 1.3310 0.7984 -0.1648 0.1531 -0.0333 205 LEU A N 1634 C CA . LEU A 205 ? 1.5484 1.3375 0.7969 -0.1430 0.1392 -0.0310 205 LEU A CA 1635 C C . LEU A 205 ? 1.5830 1.3282 0.7843 -0.1349 0.1280 -0.0196 205 LEU A C 1636 O O . LEU A 205 ? 1.6117 1.3155 0.7602 -0.1585 0.1365 -0.0151 205 LEU A O 1637 C CB . LEU A 205 ? 1.5024 1.3621 0.7970 -0.1606 0.1460 -0.0399 205 LEU A CB 1638 C CG . LEU A 205 ? 1.4669 1.3790 0.8076 -0.1404 0.1322 -0.0408 205 LEU A CG 1639 C CD1 . LEU A 205 ? 1.4291 1.3618 0.8109 -0.1101 0.1204 -0.0403 205 LEU A CD1 1640 C CD2 . LEU A 205 ? 1.4159 1.3892 0.7968 -0.1589 0.1408 -0.0507 205 LEU A CD2 1641 N N . ASN A 206 ? 1.5453 1.3010 0.7661 -0.1024 0.1086 -0.0147 206 ASN A N 1642 C CA . ASN A 206 ? 1.5827 1.2999 0.7622 -0.0897 0.0927 -0.0036 206 ASN A CA 1643 C C . ASN A 206 ? 1.5266 1.2984 0.7531 -0.0694 0.0750 -0.0047 206 ASN A C 1644 O O . ASN A 206 ? 1.5326 1.3015 0.7716 -0.0386 0.0553 0.0010 206 ASN A O 1645 C CB . ASN A 206 ? 1.6418 1.2909 0.7812 -0.0660 0.0820 0.0061 206 ASN A CB 1646 C CG . ASN A 206 ? 1.7012 1.2981 0.7855 -0.0553 0.0647 0.0194 206 ASN A CG 1647 O OD1 . ASN A 206 ? 1.7003 1.3090 0.7712 -0.0672 0.0618 0.0213 206 ASN A OD1 1648 N ND2 . ASN A 206 ? 1.7568 1.2935 0.8068 -0.0312 0.0526 0.0285 206 ASN A ND2 1649 N N . GLN A 207 ? 1.4715 1.2928 0.7240 -0.0872 0.0817 -0.0123 207 GLN A N 1650 C CA . GLN A 207 ? 1.4177 1.2944 0.7195 -0.0726 0.0670 -0.0159 207 GLN A CA 1651 C C . GLN A 207 ? 1.4582 1.3191 0.7242 -0.0735 0.0550 -0.0114 207 GLN A C 1652 O O . GLN A 207 ? 1.4904 1.3142 0.7012 -0.0941 0.0655 -0.0088 207 GLN A O 1653 C CB . GLN A 207 ? 1.3499 1.2898 0.7045 -0.0886 0.0804 -0.0283 207 GLN A CB 1654 C CG . GLN A 207 ? 1.3001 1.2962 0.7074 -0.0764 0.0666 -0.0330 207 GLN A CG 1655 C CD . GLN A 207 ? 1.2469 1.2973 0.7000 -0.0920 0.0795 -0.0444 207 GLN A CD 1656 O OE1 . GLN A 207 ? 1.2629 1.3323 0.7153 -0.1058 0.0842 -0.0507 207 GLN A OE1 1657 N NE2 . GLN A 207 ? 1.2135 1.2878 0.7045 -0.0889 0.0851 -0.0473 207 GLN A NE2 1658 N N . ARG A 208 ? 1.4459 1.3348 0.7424 -0.0522 0.0330 -0.0106 208 ARG A N 1659 C CA . ARG A 208 ? 1.4811 1.3630 0.7499 -0.0525 0.0191 -0.0087 208 ARG A CA 1660 C C . ARG A 208 ? 1.4349 1.3727 0.7627 -0.0367 0.0003 -0.0139 208 ARG A C 1661 O O . ARG A 208 ? 1.4316 1.3759 0.7838 -0.0118 -0.0209 -0.0084 208 ARG A O 1662 C CB . ARG A 208 ? 1.5776 1.3942 0.7843 -0.0388 0.0022 0.0053 208 ARG A CB 1663 C CG . ARG A 208 ? 1.6286 1.4297 0.7948 -0.0404 -0.0129 0.0080 208 ARG A CG 1664 C CD . ARG A 208 ? 1.7060 1.4569 0.8311 -0.0164 -0.0406 0.0223 208 ARG A CD 1665 N NE . ARG A 208 ? 1.7363 1.4816 0.8326 -0.0143 -0.0607 0.0239 208 ARG A NE 1666 C CZ . ARG A 208 ? 1.7939 1.5007 0.8214 -0.0340 -0.0531 0.0259 208 ARG A CZ 1667 N NH1 . ARG A 208 ? 1.8195 1.4917 0.8019 -0.0593 -0.0249 0.0272 208 ARG A NH1 1668 N NH2 . ARG A 208 ? 1.8261 1.5290 0.8285 -0.0298 -0.0736 0.0262 208 ARG A NH2 1669 N N . LEU A 209 ? 1.4096 1.3875 0.7610 -0.0516 0.0079 -0.0248 209 LEU A N 1670 C CA . LEU A 209 ? 1.3551 1.3847 0.7623 -0.0413 -0.0080 -0.0310 209 LEU A CA 1671 C C . LEU A 209 ? 1.3785 1.3953 0.7549 -0.0385 -0.0275 -0.0308 209 LEU A C 1672 O O . LEU A 209 ? 1.4185 1.3996 0.7359 -0.0518 -0.0199 -0.0304 209 LEU A O 1673 C CB . LEU A 209 ? 1.3016 1.3787 0.7515 -0.0574 0.0099 -0.0436 209 LEU A CB 1674 C CG . LEU A 209 ? 1.2729 1.3602 0.7423 -0.0675 0.0324 -0.0459 209 LEU A CG 1675 C CD1 . LEU A 209 ? 1.2249 1.3545 0.7268 -0.0840 0.0475 -0.0581 209 LEU A CD1 1676 C CD2 . LEU A 209 ? 1.2515 1.3540 0.7624 -0.0490 0.0252 -0.0411 209 LEU A CD2 1677 N N . VAL A 210 ? 1.3623 1.4081 0.7774 -0.0226 -0.0522 -0.0311 210 VAL A N 1678 C CA . VAL A 210 ? 1.3961 1.4371 0.7898 -0.0209 -0.0734 -0.0336 210 VAL A CA 1679 C C . VAL A 210 ? 1.3414 1.4369 0.7969 -0.0207 -0.0823 -0.0438 210 VAL A C 1680 O O . VAL A 210 ? 1.3029 1.4351 0.8184 -0.0109 -0.0876 -0.0424 210 VAL A O 1681 C CB . VAL A 210 ? 1.4521 1.4626 0.8196 -0.0004 -0.1039 -0.0214 210 VAL A CB 1682 C CG1 . VAL A 210 ? 1.5291 1.4744 0.8205 -0.0026 -0.0974 -0.0110 210 VAL A CG1 1683 C CG2 . VAL A 210 ? 1.4205 1.4612 0.8483 0.0218 -0.1188 -0.0156 210 VAL A CG2 1684 N N . PRO A 211 ? 1.3343 1.4330 0.7735 -0.0320 -0.0830 -0.0543 211 PRO A N 1685 C CA . PRO A 211 ? 1.2776 1.4210 0.7717 -0.0321 -0.0929 -0.0639 211 PRO A CA 1686 C C . PRO A 211 ? 1.2771 1.4340 0.7987 -0.0166 -0.1270 -0.0586 211 PRO A C 1687 O O . PRO A 211 ? 1.3208 1.4477 0.8020 -0.0087 -0.1481 -0.0526 211 PRO A O 1688 C CB . PRO A 211 ? 1.2966 1.4292 0.7544 -0.0454 -0.0869 -0.0767 211 PRO A CB 1689 C CG . PRO A 211 ? 1.3395 1.4309 0.7314 -0.0553 -0.0667 -0.0744 211 PRO A CG 1690 C CD . PRO A 211 ? 1.3755 1.4369 0.7459 -0.0450 -0.0736 -0.0584 211 PRO A CD 1691 N N . ARG A 212 ? 1.2261 1.4284 0.8161 -0.0129 -0.1326 -0.0598 212 ARG A N 1692 C CA . ARG A 212 ? 1.2412 1.4667 0.8674 -0.0028 -0.1639 -0.0572 212 ARG A CA 1693 C C . ARG A 212 ? 1.2415 1.4808 0.8775 -0.0140 -0.1740 -0.0697 212 ARG A C 1694 O O . ARG A 212 ? 1.1939 1.4592 0.8657 -0.0233 -0.1601 -0.0772 212 ARG A O 1695 C CB . ARG A 212 ? 1.1961 1.4634 0.8908 0.0064 -0.1630 -0.0508 212 ARG A CB 1696 C CG . ARG A 212 ? 1.2125 1.4643 0.8985 0.0218 -0.1575 -0.0393 212 ARG A CG 1697 C CD . ARG A 212 ? 1.1867 1.4389 0.8779 0.0158 -0.1247 -0.0399 212 ARG A CD 1698 N NE . ARG A 212 ? 1.1307 1.4315 0.8890 0.0147 -0.1176 -0.0415 212 ARG A NE 1699 C CZ . ARG A 212 ? 1.1066 1.4181 0.8801 0.0068 -0.0918 -0.0439 212 ARG A CZ 1700 N NH1 . ARG A 212 ? 1.1087 1.3894 0.8400 -0.0014 -0.0705 -0.0457 212 ARG A NH1 1701 N NH2 . ARG A 212 ? 1.0986 1.4521 0.9292 0.0059 -0.0877 -0.0442 212 ARG A NH2 1702 N N . ILE A 213 ? 1.3029 1.5207 0.9033 -0.0126 -0.1992 -0.0719 213 ILE A N 1703 C CA . ILE A 213 ? 1.3242 1.5468 0.9254 -0.0224 -0.2125 -0.0848 213 ILE A CA 1704 C C . ILE A 213 ? 1.2997 1.5607 0.9629 -0.0193 -0.2400 -0.0827 213 ILE A C 1705 O O . ILE A 213 ? 1.3251 1.5927 1.0000 -0.0078 -0.2640 -0.0730 213 ILE A O 1706 C CB . ILE A 213 ? 1.4102 1.5884 0.9377 -0.0240 -0.2276 -0.0896 213 ILE A CB 1707 C CG1 . ILE A 213 ? 1.4565 1.5977 0.9205 -0.0304 -0.1979 -0.0922 213 ILE A CG1 1708 C CG2 . ILE A 213 ? 1.4160 1.5973 0.9450 -0.0329 -0.2441 -0.1042 213 ILE A CG2 1709 C CD1 . ILE A 213 ? 1.5027 1.6106 0.9230 -0.0220 -0.1968 -0.0777 213 ILE A CD1 1710 N N . ALA A 214 ? 1.2675 1.5536 0.9706 -0.0300 -0.2366 -0.0916 214 ALA A N 1711 C CA . ALA A 214 ? 1.2411 1.5638 1.0038 -0.0323 -0.2601 -0.0903 214 ALA A CA 1712 C C . ALA A 214 ? 1.2252 1.5574 1.0095 -0.0467 -0.2540 -0.1023 214 ALA A C 1713 O O . ALA A 214 ? 1.2087 1.5366 0.9877 -0.0512 -0.2265 -0.1078 214 ALA A O 1714 C CB . ALA A 214 ? 1.1946 1.5565 1.0165 -0.0236 -0.2548 -0.0772 214 ALA A CB 1715 N N . THR A 215 ? 1.2509 1.5945 1.0591 -0.0540 -0.2812 -0.1065 215 THR A N 1716 C CA . THR A 215 ? 1.2333 1.5842 1.0666 -0.0675 -0.2792 -0.1164 215 THR A CA 1717 C C . THR A 215 ? 1.1650 1.5597 1.0684 -0.0708 -0.2692 -0.1066 215 THR A C 1718 O O . THR A 215 ? 1.1573 1.5840 1.1030 -0.0677 -0.2824 -0.0957 215 THR A O 1719 C CB . THR A 215 ? 1.2786 1.6189 1.1053 -0.0766 -0.3136 -0.1252 215 THR A CB 1720 O OG1 . THR A 215 ? 1.2834 1.6526 1.1472 -0.0746 -0.3413 -0.1146 215 THR A OG1 1721 C CG2 . THR A 215 ? 1.3244 1.6168 1.0740 -0.0743 -0.3206 -0.1370 215 THR A CG2 1722 N N . ARG A 216 ? 1.1270 1.5235 1.0416 -0.0764 -0.2453 -0.1105 216 ARG A N 1723 C CA . ARG A 216 ? 1.0716 1.5039 1.0427 -0.0800 -0.2314 -0.1011 216 ARG A CA 1724 C C . ARG A 216 ? 1.0563 1.4885 1.0483 -0.0938 -0.2315 -0.1077 216 ARG A C 1725 O O . ARG A 216 ? 1.0726 1.4747 1.0328 -0.0979 -0.2375 -0.1211 216 ARG A O 1726 C CB . ARG A 216 ? 1.0474 1.4802 1.0089 -0.0718 -0.1998 -0.0965 216 ARG A CB 1727 C CG . ARG A 216 ? 1.0562 1.4878 1.0015 -0.0581 -0.1977 -0.0877 216 ARG A CG 1728 C CD . ARG A 216 ? 1.0423 1.4601 0.9606 -0.0532 -0.1676 -0.0870 216 ARG A CD 1729 N NE . ARG A 216 ? 1.0820 1.4618 0.9396 -0.0528 -0.1630 -0.0963 216 ARG A NE 1730 C CZ . ARG A 216 ? 1.1099 1.4646 0.9230 -0.0449 -0.1645 -0.0933 216 ARG A CZ 1731 N NH1 . ARG A 216 ? 1.1234 1.4846 0.9454 -0.0339 -0.1722 -0.0814 216 ARG A NH1 1732 N NH2 . ARG A 216 ? 1.1338 1.4554 0.8915 -0.0476 -0.1575 -0.1021 216 ARG A NH2 1733 N N . SER A 217 ? 1.0323 1.4954 1.0750 -0.1004 -0.2242 -0.0984 217 SER A N 1734 C CA . SER A 217 ? 1.0357 1.4957 1.0971 -0.1132 -0.2220 -0.1020 217 SER A CA 1735 C C . SER A 217 ? 1.0394 1.4716 1.0657 -0.1086 -0.2022 -0.1123 217 SER A C 1736 O O . SER A 217 ? 1.0609 1.4925 1.0688 -0.0988 -0.1813 -0.1111 217 SER A O 1737 C CB . SER A 217 ? 1.0138 1.5103 1.1278 -0.1197 -0.2110 -0.0881 217 SER A CB 1738 O OG . SER A 217 ? 1.0435 1.5732 1.1951 -0.1222 -0.2260 -0.0787 217 SER A OG 1739 N N . LYS A 218 ? 1.0467 1.4561 1.0647 -0.1155 -0.2092 -0.1228 218 LYS A N 1740 C CA . LYS A 218 ? 1.0487 1.4344 1.0368 -0.1091 -0.1922 -0.1345 218 LYS A CA 1741 C C . LYS A 218 ? 1.0112 1.4108 1.0261 -0.1104 -0.1733 -0.1278 218 LYS A C 1742 O O . LYS A 218 ? 1.0143 1.4200 1.0601 -0.1206 -0.1803 -0.1217 218 LYS A O 1743 C CB . LYS A 218 ? 1.0900 1.4404 1.0517 -0.1119 -0.2079 -0.1512 218 LYS A CB 1744 C CG . LYS A 218 ? 1.1328 1.4590 1.0433 -0.1044 -0.2124 -0.1637 218 LYS A CG 1745 C CD . LYS A 218 ? 1.1917 1.4830 1.0762 -0.1087 -0.2334 -0.1798 218 LYS A CD 1746 C CE . LYS A 218 ? 1.2506 1.5180 1.0804 -0.1026 -0.2392 -0.1906 218 LYS A CE 1747 N NZ . LYS A 218 ? 1.3040 1.5442 1.1142 -0.1105 -0.2697 -0.2011 218 LYS A NZ 1748 N N . VAL A 219 ? 0.9868 1.3902 0.9877 -0.1013 -0.1501 -0.1286 219 VAL A N 1749 C CA . VAL A 219 ? 0.9468 1.3616 0.9667 -0.1012 -0.1327 -0.1235 219 VAL A CA 1750 C C . VAL A 219 ? 0.9404 1.3388 0.9339 -0.0927 -0.1199 -0.1376 219 VAL A C 1751 O O . VAL A 219 ? 0.9464 1.3406 0.9108 -0.0860 -0.1090 -0.1442 219 VAL A O 1752 C CB . VAL A 219 ? 0.9252 1.3662 0.9584 -0.0991 -0.1161 -0.1104 219 VAL A CB 1753 C CG1 . VAL A 219 ? 0.8995 1.3520 0.9523 -0.1012 -0.1015 -0.1041 219 VAL A CG1 1754 C CG2 . VAL A 219 ? 0.9199 1.3803 0.9776 -0.1035 -0.1276 -0.0987 219 VAL A CG2 1755 N N . ASN A 220 ? 0.9327 1.3219 0.9366 -0.0928 -0.1212 -0.1419 220 ASN A N 1756 C CA . ASN A 220 ? 0.9510 1.3251 0.9345 -0.0828 -0.1128 -0.1579 220 ASN A CA 1757 C C . ASN A 220 ? 0.9630 1.3136 0.9099 -0.0781 -0.1192 -0.1742 220 ASN A C 1758 O O . ASN A 220 ? 0.9705 1.3176 0.8927 -0.0695 -0.1046 -0.1863 220 ASN A O 1759 C CB . ASN A 220 ? 0.9504 1.3443 0.9323 -0.0767 -0.0889 -0.1571 220 ASN A CB 1760 C CG . ASN A 220 ? 0.9372 1.3504 0.9493 -0.0805 -0.0827 -0.1432 220 ASN A CG 1761 O OD1 . ASN A 220 ? 0.9510 1.3818 0.9641 -0.0787 -0.0659 -0.1400 220 ASN A OD1 1762 N ND2 . ASN A 220 ? 0.9491 1.3573 0.9831 -0.0873 -0.0963 -0.1349 220 ASN A ND2 1763 N N . GLY A 221 ? 0.9667 1.3020 0.9095 -0.0850 -0.1410 -0.1744 221 GLY A N 1764 C CA . GLY A 221 ? 0.9930 1.3020 0.8970 -0.0822 -0.1510 -0.1895 221 GLY A CA 1765 C C . GLY A 221 ? 0.9898 1.3031 0.8647 -0.0801 -0.1448 -0.1882 221 GLY A C 1766 O O . GLY A 221 ? 1.0429 1.3329 0.8779 -0.0773 -0.1502 -0.2008 221 GLY A O 1767 N N . GLN A 222 ? 0.9415 1.2805 0.8321 -0.0815 -0.1344 -0.1730 222 GLN A N 1768 C CA . GLN A 222 ? 0.9528 1.2915 0.8133 -0.0787 -0.1279 -0.1702 222 GLN A CA 1769 C C . GLN A 222 ? 0.9533 1.3026 0.8271 -0.0825 -0.1444 -0.1561 222 GLN A C 1770 O O . GLN A 222 ? 0.9324 1.3060 0.8465 -0.0861 -0.1453 -0.1427 222 GLN A O 1771 C CB . GLN A 222 ? 0.9267 1.2812 0.7858 -0.0751 -0.1003 -0.1663 222 GLN A CB 1772 C CG . GLN A 222 ? 0.9294 1.2818 0.7805 -0.0704 -0.0824 -0.1801 222 GLN A CG 1773 C CD . GLN A 222 ? 0.9674 1.2928 0.7812 -0.0662 -0.0866 -0.1988 222 GLN A CD 1774 O OE1 . GLN A 222 ? 0.9797 1.2880 0.7531 -0.0663 -0.0885 -0.2025 222 GLN A OE1 1775 N NE2 . GLN A 222 ? 0.9774 1.2961 0.8017 -0.0616 -0.0883 -0.2108 222 GLN A NE2 1776 N N . SER A 223 ? 0.9971 1.3284 0.8353 -0.0808 -0.1571 -0.1594 223 SER A N 1777 C CA . SER A 223 ? 1.0058 1.3466 0.8520 -0.0811 -0.1744 -0.1472 223 SER A CA 1778 C C . SER A 223 ? 0.9989 1.3411 0.8237 -0.0740 -0.1587 -0.1387 223 SER A C 1779 O O . SER A 223 ? 1.0140 1.3700 0.8544 -0.0707 -0.1667 -0.1259 223 SER A O 1780 C CB . SER A 223 ? 1.0608 1.3778 0.8778 -0.0832 -0.2019 -0.1553 223 SER A CB 1781 O OG . SER A 223 ? 1.0874 1.4141 0.9096 -0.0812 -0.2202 -0.1439 223 SER A OG 1782 N N . GLY A 224 ? 0.9986 1.3261 0.7879 -0.0716 -0.1365 -0.1461 224 GLY A N 1783 C CA . GLY A 224 ? 0.9837 1.3083 0.7503 -0.0678 -0.1189 -0.1383 224 GLY A CA 1784 C C . GLY A 224 ? 0.9290 1.2793 0.7325 -0.0684 -0.0995 -0.1299 224 GLY A C 1785 O O . GLY A 224 ? 0.8859 1.2548 0.7278 -0.0716 -0.0982 -0.1307 224 GLY A O 1786 N N . ARG A 225 ? 0.9308 1.2780 0.7183 -0.0659 -0.0850 -0.1218 225 ARG A N 1787 C CA . ARG A 225 ? 0.9098 1.2773 0.7258 -0.0666 -0.0671 -0.1139 225 ARG A CA 1788 C C . ARG A 225 ? 0.9178 1.2726 0.7005 -0.0692 -0.0431 -0.1150 225 ARG A C 1789 O O . ARG A 225 ? 0.9600 1.2892 0.6966 -0.0694 -0.0410 -0.1174 225 ARG A O 1790 C CB . ARG A 225 ? 0.8991 1.2801 0.7417 -0.0606 -0.0767 -0.0998 225 ARG A CB 1791 C CG . ARG A 225 ? 0.8928 1.2949 0.7781 -0.0610 -0.0980 -0.0968 225 ARG A CG 1792 C CD . ARG A 225 ? 0.8589 1.2841 0.7852 -0.0676 -0.0902 -0.0970 225 ARG A CD 1793 N NE . ARG A 225 ? 0.8544 1.2994 0.8214 -0.0709 -0.1090 -0.0923 225 ARG A NE 1794 C CZ . ARG A 225 ? 0.8667 1.3077 0.8414 -0.0775 -0.1253 -0.0991 225 ARG A CZ 1795 N NH1 . ARG A 225 ? 0.8858 1.3033 0.8300 -0.0791 -0.1252 -0.1124 225 ARG A NH1 1796 N NH2 . ARG A 225 ? 0.8678 1.3285 0.8814 -0.0831 -0.1414 -0.0931 225 ARG A NH2 1797 N N . MET A 226 ? 0.8983 1.2702 0.7032 -0.0727 -0.0257 -0.1127 226 MET A N 1798 C CA . MET A 226 ? 0.9252 1.2887 0.7051 -0.0779 -0.0033 -0.1127 226 MET A CA 1799 C C . MET A 226 ? 0.9286 1.2994 0.7256 -0.0762 0.0032 -0.1013 226 MET A C 1800 O O . MET A 226 ? 0.9214 1.3157 0.7569 -0.0765 0.0044 -0.0987 226 MET A O 1801 C CB . MET A 226 ? 0.9185 1.2967 0.7073 -0.0848 0.0124 -0.1238 226 MET A CB 1802 C CG . MET A 226 ? 0.9571 1.3279 0.7274 -0.0849 0.0102 -0.1377 226 MET A CG 1803 S SD . MET A 226 ? 1.0114 1.3564 0.7213 -0.0913 0.0269 -0.1437 226 MET A SD 1804 C CE . MET A 226 ? 1.0428 1.3884 0.7453 -0.0886 0.0255 -0.1626 226 MET A CE 1805 N N . GLU A 227 ? 0.9558 1.3030 0.7206 -0.0742 0.0076 -0.0946 227 GLU A N 1806 C CA . GLU A 227 ? 0.9333 1.2802 0.7064 -0.0710 0.0148 -0.0852 227 GLU A CA 1807 C C . GLU A 227 ? 0.9369 1.2715 0.6842 -0.0823 0.0368 -0.0877 227 GLU A C 1808 O O . GLU A 227 ? 0.9760 1.2836 0.6799 -0.0877 0.0432 -0.0891 227 GLU A O 1809 C CB . GLU A 227 ? 0.9745 1.3000 0.7300 -0.0586 0.0018 -0.0758 227 GLU A CB 1810 C CG . GLU A 227 ? 0.9935 1.3213 0.7647 -0.0503 0.0064 -0.0670 227 GLU A CG 1811 C CD . GLU A 227 ? 1.0318 1.3491 0.8010 -0.0334 -0.0109 -0.0584 227 GLU A CD 1812 O OE1 . GLU A 227 ? 1.0546 1.3529 0.7968 -0.0298 -0.0257 -0.0579 227 GLU A OE1 1813 O OE2 . GLU A 227 ? 1.0334 1.3625 0.8281 -0.0230 -0.0099 -0.0523 227 GLU A OE2 1814 N N . PHE A 228 ? 0.9009 1.2546 0.6732 -0.0876 0.0481 -0.0882 228 PHE A N 1815 C CA . PHE A 228 ? 0.8949 1.2429 0.6489 -0.1011 0.0675 -0.0920 228 PHE A CA 1816 C C . PHE A 228 ? 0.9004 1.2286 0.6395 -0.1008 0.0753 -0.0845 228 PHE A C 1817 O O . PHE A 228 ? 0.8823 1.2170 0.6429 -0.0906 0.0700 -0.0784 228 PHE A O 1818 C CB . PHE A 228 ? 0.8646 1.2458 0.6525 -0.1083 0.0733 -0.0991 228 PHE A CB 1819 C CG . PHE A 228 ? 0.8742 1.2690 0.6692 -0.1092 0.0696 -0.1091 228 PHE A CG 1820 C CD1 . PHE A 228 ? 0.8888 1.2801 0.6601 -0.1189 0.0824 -0.1177 228 PHE A CD1 1821 C CD2 . PHE A 228 ? 0.8643 1.2743 0.6886 -0.1006 0.0542 -0.1103 228 PHE A CD2 1822 C CE1 . PHE A 228 ? 0.8848 1.2879 0.6616 -0.1174 0.0806 -0.1285 228 PHE A CE1 1823 C CE2 . PHE A 228 ? 0.8571 1.2743 0.6845 -0.1000 0.0505 -0.1207 228 PHE A CE2 1824 C CZ . PHE A 228 ? 0.8667 1.2807 0.6703 -0.1070 0.0640 -0.1305 228 PHE A CZ 1825 N N . PHE A 229 ? 0.9120 1.2148 0.6130 -0.1126 0.0888 -0.0854 229 PHE A N 1826 C CA . PHE A 229 ? 0.9331 1.2079 0.6113 -0.1142 0.0969 -0.0796 229 PHE A CA 1827 C C . PHE A 229 ? 0.9419 1.2195 0.6122 -0.1345 0.1141 -0.0852 229 PHE A C 1828 O O . PHE A 229 ? 0.9306 1.2298 0.6086 -0.1467 0.1205 -0.0930 229 PHE A O 1829 C CB . PHE A 229 ? 0.9829 1.2118 0.6128 -0.1097 0.0938 -0.0731 229 PHE A CB 1830 C CG . PHE A 229 ? 0.9988 1.2238 0.6359 -0.0886 0.0744 -0.0667 229 PHE A CG 1831 C CD1 . PHE A 229 ? 1.0090 1.2428 0.6475 -0.0851 0.0619 -0.0690 229 PHE A CD1 1832 C CD2 . PHE A 229 ? 1.0205 1.2344 0.6640 -0.0721 0.0684 -0.0593 229 PHE A CD2 1833 C CE1 . PHE A 229 ? 1.0184 1.2510 0.6655 -0.0672 0.0416 -0.0633 229 PHE A CE1 1834 C CE2 . PHE A 229 ? 1.0356 1.2523 0.6918 -0.0525 0.0495 -0.0536 229 PHE A CE2 1835 C CZ . PHE A 229 ? 1.0331 1.2598 0.6916 -0.0510 0.0350 -0.0553 229 PHE A CZ 1836 N N . TRP A 230 ? 0.9684 1.2244 0.6237 -0.1376 0.1212 -0.0818 230 TRP A N 1837 C CA . TRP A 230 ? 0.9655 1.2217 0.6120 -0.1587 0.1357 -0.0869 230 TRP A CA 1838 C C . TRP A 230 ? 1.0086 1.2170 0.6134 -0.1635 0.1427 -0.0823 230 TRP A C 1839 O O . TRP A 230 ? 1.0309 1.2101 0.6205 -0.1465 0.1363 -0.0754 230 TRP A O 1840 C CB . TRP A 230 ? 0.9167 1.2112 0.6047 -0.1599 0.1352 -0.0910 230 TRP A CB 1841 C CG . TRP A 230 ? 0.9036 1.1944 0.6042 -0.1440 0.1297 -0.0855 230 TRP A CG 1842 C CD1 . TRP A 230 ? 0.8765 1.1849 0.6059 -0.1254 0.1185 -0.0814 230 TRP A CD1 1843 C CD2 . TRP A 230 ? 0.9118 1.1808 0.5965 -0.1462 0.1366 -0.0844 230 TRP A CD2 1844 N NE1 . TRP A 230 ? 0.8654 1.1681 0.6000 -0.1156 0.1197 -0.0775 230 TRP A NE1 1845 C CE2 . TRP A 230 ? 0.8972 1.1739 0.6028 -0.1269 0.1308 -0.0798 230 TRP A CE2 1846 C CE3 . TRP A 230 ? 0.9409 1.1839 0.5948 -0.1637 0.1473 -0.0875 230 TRP A CE3 1847 C CZ2 . TRP A 230 ? 0.9254 1.1847 0.6205 -0.1224 0.1369 -0.0789 230 TRP A CZ2 1848 C CZ3 . TRP A 230 ? 0.9586 1.1802 0.5999 -0.1599 0.1512 -0.0868 230 TRP A CZ3 1849 C CH2 . TRP A 230 ? 0.9518 1.1813 0.6127 -0.1384 0.1467 -0.0829 230 TRP A CH2 1850 N N . THR A 231 ? 1.0335 1.2346 0.6211 -0.1868 0.1555 -0.0868 231 THR A N 1851 C CA . THR A 231 ? 1.0725 1.2279 0.6220 -0.1952 0.1626 -0.0842 231 THR A CA 1852 C C . THR A 231 ? 1.0661 1.2364 0.6199 -0.2217 0.1733 -0.0918 231 THR A C 1853 O O . THR A 231 ? 1.0302 1.2449 0.6136 -0.2333 0.1758 -0.0983 231 THR A O 1854 C CB . THR A 231 ? 1.1290 1.2302 0.6240 -0.1991 0.1655 -0.0778 231 THR A CB 1855 O OG1 . THR A 231 ? 1.1863 1.2358 0.6435 -0.2017 0.1696 -0.0746 231 THR A OG1 1856 C CG2 . THR A 231 ? 1.1398 1.2471 0.6189 -0.2255 0.1772 -0.0816 231 THR A CG2 1857 N N . ILE A 232 ? 1.1154 1.2489 0.6408 -0.2301 0.1782 -0.0915 232 ILE A N 1858 C CA . ILE A 232 ? 1.1348 1.2735 0.6556 -0.2587 0.1870 -0.0983 232 ILE A CA 1859 C C . ILE A 232 ? 1.1900 1.2796 0.6592 -0.2799 0.1970 -0.0957 232 ILE A C 1860 O O . ILE A 232 ? 1.2525 1.2831 0.6783 -0.2747 0.1972 -0.0902 232 ILE A O 1861 C CB . ILE A 232 ? 1.1391 1.2682 0.6604 -0.2562 0.1851 -0.1011 232 ILE A CB 1862 C CG1 . ILE A 232 ? 1.0738 1.2619 0.6461 -0.2526 0.1790 -0.1061 232 ILE A CG1 1863 C CG2 . ILE A 232 ? 1.1926 1.2896 0.6794 -0.2852 0.1934 -0.1055 232 ILE A CG2 1864 C CD1 . ILE A 232 ? 1.0394 1.2647 0.6499 -0.2301 0.1707 -0.1030 232 ILE A CD1 1865 N N . LEU A 233 ? 1.1983 1.3117 0.6718 -0.3033 0.2059 -0.0994 233 LEU A N 1866 C CA . LEU A 233 ? 1.2563 1.3271 0.6813 -0.3290 0.2178 -0.0966 233 LEU A CA 1867 C C . LEU A 233 ? 1.2864 1.3471 0.7010 -0.3582 0.2242 -0.1021 233 LEU A C 1868 O O . LEU A 233 ? 1.2489 1.3619 0.7013 -0.3750 0.2266 -0.1106 233 LEU A O 1869 C CB . LEU A 233 ? 1.2521 1.3573 0.6876 -0.3423 0.2270 -0.0989 233 LEU A CB 1870 C CG . LEU A 233 ? 1.3219 1.3852 0.7050 -0.3682 0.2413 -0.0942 233 LEU A CG 1871 C CD1 . LEU A 233 ? 1.3753 1.3664 0.7018 -0.3520 0.2356 -0.0819 233 LEU A CD1 1872 C CD2 . LEU A 233 ? 1.3036 1.4141 0.7065 -0.3787 0.2521 -0.0991 233 LEU A CD2 1873 N N . LYS A 234 ? 1.3592 1.3513 0.7222 -0.3633 0.2256 -0.0976 234 LYS A N 1874 C CA . LYS A 234 ? 1.4169 1.3881 0.7621 -0.3911 0.2298 -0.1031 234 LYS A CA 1875 C C . LYS A 234 ? 1.4439 1.4293 0.7836 -0.4328 0.2432 -0.1063 234 LYS A C 1876 O O . LYS A 234 ? 1.4430 1.4416 0.7811 -0.4388 0.2515 -0.1030 234 LYS A O 1877 C CB . LYS A 234 ? 1.5077 1.3938 0.7939 -0.3834 0.2279 -0.0976 234 LYS A CB 1878 C CG . LYS A 234 ? 1.5101 1.3917 0.8090 -0.3505 0.2175 -0.0993 234 LYS A CG 1879 C CD . LYS A 234 ? 1.5957 1.3979 0.8420 -0.3301 0.2150 -0.0925 234 LYS A CD 1880 C CE . LYS A 234 ? 1.5926 1.3982 0.8567 -0.2954 0.2073 -0.0948 234 LYS A CE 1881 N NZ . LYS A 234 ? 1.6147 1.4187 0.8778 -0.3076 0.2087 -0.1049 234 LYS A NZ 1882 N N . PRO A 235 ? 1.4674 1.4525 0.8048 -0.4627 0.2456 -0.1134 235 PRO A N 1883 C CA . PRO A 235 ? 1.4831 1.4874 0.8201 -0.5041 0.2591 -0.1164 235 PRO A CA 1884 C C . PRO A 235 ? 1.5602 1.4945 0.8328 -0.5199 0.2703 -0.1066 235 PRO A C 1885 O O . PRO A 235 ? 1.6051 1.4626 0.8252 -0.5099 0.2659 -0.1000 235 PRO A O 1886 C CB . PRO A 235 ? 1.4917 1.4986 0.8323 -0.5321 0.2559 -0.1253 235 PRO A CB 1887 C CG . PRO A 235 ? 1.4924 1.4622 0.8180 -0.5064 0.2428 -0.1260 235 PRO A CG 1888 C CD . PRO A 235 ? 1.4658 1.4270 0.7940 -0.4621 0.2372 -0.1186 235 PRO A CD 1889 N N . ASN A 236 ? 1.5896 1.5494 0.8653 -0.5425 0.2849 -0.1054 236 ASN A N 1890 C CA . ASN A 236 ? 1.6741 1.5691 0.8856 -0.5661 0.2979 -0.0956 236 ASN A CA 1891 C C . ASN A 236 ? 1.7086 1.5435 0.8741 -0.5341 0.2925 -0.0830 236 ASN A C 1892 O O . ASN A 236 ? 1.7782 1.5416 0.8792 -0.5480 0.2990 -0.0726 236 ASN A O 1893 C CB . ASN A 236 ? 1.7475 1.5811 0.9147 -0.5979 0.2991 -0.0958 236 ASN A CB 1894 C CG . ASN A 236 ? 1.8393 1.6445 0.9662 -0.6440 0.3177 -0.0909 236 ASN A CG 1895 O OD1 . ASN A 236 ? 1.8464 1.6936 0.9885 -0.6570 0.3323 -0.0899 236 ASN A OD1 1896 N ND2 . ASN A 236 ? 1.9364 1.6686 1.0099 -0.6704 0.3182 -0.0883 236 ASN A ND2 1897 N N . ASP A 237 ? 1.6660 1.5292 0.8643 -0.4922 0.2795 -0.0833 237 ASP A N 1898 C CA . ASP A 237 ? 1.6810 1.5023 0.8477 -0.4595 0.2716 -0.0725 237 ASP A CA 1899 C C . ASP A 237 ? 1.6327 1.5098 0.8287 -0.4522 0.2765 -0.0736 237 ASP A C 1900 O O . ASP A 237 ? 1.5614 1.5128 0.8111 -0.4628 0.2830 -0.0839 237 ASP A O 1901 C CB . ASP A 237 ? 1.6575 1.4709 0.8411 -0.4181 0.2531 -0.0726 237 ASP A CB 1902 C CG . ASP A 237 ? 1.6901 1.4486 0.8350 -0.3857 0.2426 -0.0606 237 ASP A CG 1903 O OD1 . ASP A 237 ? 1.7425 1.4410 0.8282 -0.3972 0.2476 -0.0506 237 ASP A OD1 1904 O OD2 . ASP A 237 ? 1.6537 1.4292 0.8274 -0.3490 0.2288 -0.0607 237 ASP A OD2 1905 N N . ALA A 238 ? 1.6702 1.5099 0.8296 -0.4333 0.2723 -0.0634 238 ALA A N 1906 C CA . ALA A 238 ? 1.6466 1.5258 0.8194 -0.4279 0.2774 -0.0642 238 ALA A CA 1907 C C . ALA A 238 ? 1.6109 1.4868 0.7907 -0.3850 0.2583 -0.0597 238 ALA A C 1908 O O . ALA A 238 ? 1.6530 1.4713 0.7989 -0.3641 0.2449 -0.0503 238 ALA A O 1909 C CB . ALA A 238 ? 1.7207 1.5562 0.8317 -0.4563 0.2940 -0.0559 238 ALA A CB 1910 N N . ILE A 239 ? 1.5474 1.4850 0.7717 -0.3721 0.2569 -0.0668 239 ILE A N 1911 C CA . ILE A 239 ? 1.5208 1.4621 0.7557 -0.3350 0.2386 -0.0636 239 ILE A CA 1912 C C . ILE A 239 ? 1.5688 1.4965 0.7667 -0.3359 0.2426 -0.0594 239 ILE A C 1913 O O . ILE A 239 ? 1.5519 1.5153 0.7577 -0.3557 0.2595 -0.0666 239 ILE A O 1914 C CB . ILE A 239 ? 1.4183 1.4318 0.7281 -0.3160 0.2297 -0.0743 239 ILE A CB 1915 C CG1 . ILE A 239 ? 1.4041 1.4156 0.7248 -0.2792 0.2087 -0.0700 239 ILE A CG1 1916 C CG2 . ILE A 239 ? 1.3749 1.4531 0.7222 -0.3309 0.2431 -0.0861 239 ILE A CG2 1917 C CD1 . ILE A 239 ? 1.3279 1.3976 0.7160 -0.2603 0.1983 -0.0778 239 ILE A CD1 1918 N N . ASN A 240 ? 1.6184 1.4943 0.7751 -0.3140 0.2269 -0.0480 240 ASN A N 1919 C CA . ASN A 240 ? 1.6681 1.5198 0.7789 -0.3129 0.2269 -0.0423 240 ASN A CA 1920 C C . ASN A 240 ? 1.6141 1.5010 0.7582 -0.2821 0.2087 -0.0463 240 ASN A C 1921 O O . ASN A 240 ? 1.6120 1.5014 0.7831 -0.2541 0.1881 -0.0440 240 ASN A O 1922 C CB . ASN A 240 ? 1.7691 1.5335 0.8051 -0.3090 0.2181 -0.0256 240 ASN A CB 1923 C CG . ASN A 240 ? 1.8485 1.5654 0.8433 -0.3399 0.2341 -0.0204 240 ASN A CG 1924 O OD1 . ASN A 240 ? 1.8879 1.5904 0.8444 -0.3720 0.2544 -0.0186 240 ASN A OD1 1925 N ND2 . ASN A 240 ? 1.8594 1.5507 0.8605 -0.3312 0.2258 -0.0182 240 ASN A ND2 1926 N N . PHE A 241 ? 1.5926 1.5055 0.7333 -0.2882 0.2168 -0.0527 241 PHE A N 1927 C CA . PHE A 241 ? 1.5526 1.4897 0.7140 -0.2620 0.1991 -0.0566 241 PHE A CA 1928 C C . PHE A 241 ? 1.6111 1.5018 0.7044 -0.2612 0.1950 -0.0490 241 PHE A C 1929 O O . PHE A 241 ? 1.6563 1.5163 0.6959 -0.2862 0.2141 -0.0452 241 PHE A O 1930 C CB . PHE A 241 ? 1.4869 1.4974 0.7073 -0.2648 0.2089 -0.0735 241 PHE A CB 1931 C CG . PHE A 241 ? 1.4218 1.4794 0.7118 -0.2577 0.2048 -0.0802 241 PHE A CG 1932 C CD1 . PHE A 241 ? 1.3866 1.4535 0.7114 -0.2299 0.1815 -0.0781 241 PHE A CD1 1933 C CD2 . PHE A 241 ? 1.4079 1.5011 0.7278 -0.2797 0.2239 -0.0884 241 PHE A CD2 1934 C CE1 . PHE A 241 ? 1.3331 1.4403 0.7165 -0.2244 0.1786 -0.0833 241 PHE A CE1 1935 C CE2 . PHE A 241 ? 1.3535 1.4869 0.7323 -0.2731 0.2183 -0.0939 241 PHE A CE2 1936 C CZ . PHE A 241 ? 1.3163 1.4546 0.7243 -0.2456 0.1963 -0.0910 241 PHE A CZ 1937 N N . GLU A 242 ? 1.6031 1.4887 0.6982 -0.2334 0.1695 -0.0463 242 GLU A N 1938 C CA . GLU A 242 ? 1.6695 1.5145 0.7027 -0.2291 0.1603 -0.0400 242 GLU A CA 1939 C C . GLU A 242 ? 1.6372 1.5114 0.7048 -0.2014 0.1346 -0.0456 242 GLU A C 1940 O O . GLU A 242 ? 1.6001 1.4877 0.7108 -0.1792 0.1139 -0.0431 242 GLU A O 1941 C CB . GLU A 242 ? 1.7486 1.5161 0.7162 -0.2248 0.1479 -0.0211 242 GLU A CB 1942 C CG . GLU A 242 ? 1.8499 1.5610 0.7298 -0.2452 0.1598 -0.0125 242 GLU A CG 1943 C CD . GLU A 242 ? 1.9207 1.5640 0.7377 -0.2259 0.1323 0.0041 242 GLU A CD 1944 O OE1 . GLU A 242 ? 1.8890 1.5444 0.7165 -0.2021 0.1075 0.0023 242 GLU A OE1 1945 O OE2 . GLU A 242 ? 1.9905 1.5669 0.7466 -0.2349 0.1343 0.0190 242 GLU A OE2 1946 N N . SER A 243 ? 1.6541 1.5380 0.7027 -0.2034 0.1363 -0.0538 243 SER A N 1947 C CA . SER A 243 ? 1.6210 1.5306 0.7001 -0.1801 0.1114 -0.0604 243 SER A CA 1948 C C . SER A 243 ? 1.6757 1.5675 0.7037 -0.1811 0.1077 -0.0651 243 SER A C 1949 O O . SER A 243 ? 1.7111 1.5981 0.7019 -0.2015 0.1332 -0.0710 243 SER A O 1950 C CB . SER A 243 ? 1.5335 1.5119 0.6943 -0.1766 0.1168 -0.0756 243 SER A CB 1951 O OG . SER A 243 ? 1.5005 1.5003 0.6936 -0.1552 0.0911 -0.0805 243 SER A OG 1952 N N . ASN A 244 ? 1.7012 1.5854 0.7291 -0.1591 0.0756 -0.0629 244 ASN A N 1953 C CA . ASN A 244 ? 1.7462 1.6185 0.7340 -0.1561 0.0654 -0.0699 244 ASN A CA 1954 C C . ASN A 244 ? 1.6870 1.6133 0.7288 -0.1508 0.0655 -0.0895 244 ASN A C 1955 O O . ASN A 244 ? 1.6957 1.6175 0.7054 -0.1534 0.0675 -0.1003 244 ASN A O 1956 C CB . ASN A 244 ? 1.7976 1.6352 0.7603 -0.1350 0.0262 -0.0580 244 ASN A CB 1957 C CG . ASN A 244 ? 1.9108 1.6787 0.7884 -0.1397 0.0225 -0.0408 244 ASN A CG 1958 O OD1 . ASN A 244 ? 1.9834 1.7260 0.8202 -0.1606 0.0503 -0.0363 244 ASN A OD1 1959 N ND2 . ASN A 244 ? 1.9546 1.6903 0.8044 -0.1209 -0.0130 -0.0304 244 ASN A ND2 1960 N N . GLY A 245 ? 1.6144 1.5876 0.7347 -0.1425 0.0622 -0.0937 245 GLY A N 1961 C CA . GLY A 245 ? 1.5598 1.5806 0.7352 -0.1356 0.0587 -0.1103 245 GLY A CA 1962 C C . GLY A 245 ? 1.4925 1.5514 0.7451 -0.1239 0.0466 -0.1080 245 GLY A C 1963 O O . GLY A 245 ? 1.4996 1.5477 0.7616 -0.1187 0.0391 -0.0944 245 GLY A O 1964 N N . ASN A 246 ? 1.4468 1.5477 0.7517 -0.1194 0.0453 -0.1217 246 ASN A N 1965 C CA . ASN A 246 ? 1.3720 1.5112 0.7500 -0.1100 0.0352 -0.1207 246 ASN A CA 1966 C C . ASN A 246 ? 1.3142 1.4758 0.7245 -0.1191 0.0578 -0.1185 246 ASN A C 1967 O O . ASN A 246 ? 1.2845 1.4725 0.7477 -0.1125 0.0514 -0.1154 246 ASN A O 1968 C CB . ASN A 246 ? 1.3764 1.5048 0.7663 -0.0943 0.0043 -0.1077 246 ASN A CB 1969 C CG . ASN A 246 ? 1.4212 1.5325 0.7862 -0.0857 -0.0228 -0.1104 246 ASN A CG 1970 O OD1 . ASN A 246 ? 1.4044 1.5399 0.8076 -0.0795 -0.0386 -0.1180 246 ASN A OD1 1971 N ND2 . ASN A 246 ? 1.4750 1.5417 0.7735 -0.0863 -0.0295 -0.1037 246 ASN A ND2 1972 N N . PHE A 247 ? 1.3236 1.4758 0.7018 -0.1357 0.0844 -0.1206 247 PHE A N 1973 C CA . PHE A 247 ? 1.2657 1.4339 0.6665 -0.1476 0.1048 -0.1180 247 PHE A CA 1974 C C . PHE A 247 ? 1.2009 1.4204 0.6568 -0.1503 0.1170 -0.1320 247 PHE A C 1975 O O . PHE A 247 ? 1.2138 1.4481 0.6653 -0.1541 0.1284 -0.1454 247 PHE A O 1976 C CB . PHE A 247 ? 1.3283 1.4651 0.6715 -0.1673 0.1276 -0.1140 247 PHE A CB 1977 C CG . PHE A 247 ? 1.3044 1.4514 0.6638 -0.1828 0.1473 -0.1108 247 PHE A CG 1978 C CD1 . PHE A 247 ? 1.2658 1.4140 0.6550 -0.1759 0.1377 -0.1021 247 PHE A CD1 1979 C CD2 . PHE A 247 ? 1.3275 1.4820 0.6696 -0.2055 0.1758 -0.1169 247 PHE A CD2 1980 C CE1 . PHE A 247 ? 1.2608 1.4142 0.6599 -0.1912 0.1543 -0.1002 247 PHE A CE1 1981 C CE2 . PHE A 247 ? 1.3055 1.4687 0.6616 -0.2223 0.1919 -0.1143 247 PHE A CE2 1982 C CZ . PHE A 247 ? 1.2795 1.4402 0.6623 -0.2151 0.1803 -0.1061 247 PHE A CZ 1983 N N . ILE A 248 ? 1.1493 1.3948 0.6559 -0.1469 0.1139 -0.1289 248 ILE A N 1984 C CA . ILE A 248 ? 1.0928 1.3843 0.6501 -0.1501 0.1247 -0.1398 248 ILE A CA 1985 C C . ILE A 248 ? 1.0957 1.3916 0.6505 -0.1680 0.1459 -0.1370 248 ILE A C 1986 O O . ILE A 248 ? 1.0893 1.3801 0.6560 -0.1687 0.1425 -0.1277 248 ILE A O 1987 C CB . ILE A 248 ? 1.0489 1.3647 0.6608 -0.1359 0.1061 -0.1380 248 ILE A CB 1988 C CG1 . ILE A 248 ? 1.0658 1.3689 0.6751 -0.1207 0.0814 -0.1367 248 ILE A CG1 1989 C CG2 . ILE A 248 ? 1.0099 1.3687 0.6687 -0.1367 0.1137 -0.1498 248 ILE A CG2 1990 C CD1 . ILE A 248 ? 1.0979 1.3995 0.6896 -0.1186 0.0809 -0.1502 248 ILE A CD1 1991 N N . ALA A 249 ? 1.1261 1.4308 0.6636 -0.1835 0.1684 -0.1456 249 ALA A N 1992 C CA . ALA A 249 ? 1.1436 1.4463 0.6679 -0.2054 0.1895 -0.1425 249 ALA A CA 1993 C C . ALA A 249 ? 1.0962 1.4467 0.6767 -0.2111 0.1969 -0.1492 249 ALA A C 1994 O O . ALA A 249 ? 1.0542 1.4438 0.6771 -0.2015 0.1941 -0.1602 249 ALA A O 1995 C CB . ALA A 249 ? 1.2017 1.4952 0.6826 -0.2221 0.2119 -0.1482 249 ALA A CB 1996 N N . PRO A 250 ? 1.1029 1.4475 0.6814 -0.2267 0.2049 -0.1426 250 PRO A N 1997 C CA . PRO A 250 ? 1.0666 1.4562 0.6938 -0.2347 0.2113 -0.1492 250 PRO A CA 1998 C C . PRO A 250 ? 1.0793 1.5067 0.7181 -0.2497 0.2331 -0.1623 250 PRO A C 1999 O O . PRO A 250 ? 1.1535 1.5630 0.7512 -0.2649 0.2502 -0.1626 250 PRO A O 2000 C CB . PRO A 250 ? 1.0738 1.4372 0.6829 -0.2500 0.2145 -0.1391 250 PRO A CB 2001 C CG . PRO A 250 ? 1.1263 1.4332 0.6721 -0.2558 0.2178 -0.1292 250 PRO A CG 2002 C CD . PRO A 250 ? 1.1414 1.4349 0.6734 -0.2352 0.2047 -0.1288 250 PRO A CD 2003 N N . GLU A 251 ? 1.0475 1.5269 0.7416 -0.2443 0.2324 -0.1729 251 GLU A N 2004 C CA . GLU A 251 ? 1.0640 1.5894 0.7817 -0.2591 0.2532 -0.1855 251 GLU A CA 2005 C C . GLU A 251 ? 1.0407 1.5942 0.7928 -0.2736 0.2538 -0.1846 251 GLU A C 2006 O O . GLU A 251 ? 1.0411 1.6048 0.7861 -0.2993 0.2718 -0.1859 251 GLU A O 2007 C CB . GLU A 251 ? 1.0566 1.6222 0.8119 -0.2399 0.2517 -0.2004 251 GLU A CB 2008 C CG . GLU A 251 ? 1.0894 1.7007 0.8621 -0.2526 0.2769 -0.2148 251 GLU A CG 2009 C CD . GLU A 251 ? 1.0886 1.7421 0.9045 -0.2306 0.2750 -0.2311 251 GLU A CD 2010 O OE1 . GLU A 251 ? 1.0949 1.7347 0.9189 -0.2066 0.2543 -0.2310 251 GLU A OE1 2011 O OE2 . GLU A 251 ? 1.0898 1.7905 0.9325 -0.2374 0.2945 -0.2442 251 GLU A OE2 2012 N N . TYR A 252 ? 0.9861 1.5510 0.7733 -0.2584 0.2339 -0.1821 252 TYR A N 2013 C CA . TYR A 252 ? 0.9610 1.5477 0.7770 -0.2697 0.2300 -0.1807 252 TYR A CA 2014 C C . TYR A 252 ? 0.9722 1.5145 0.7637 -0.2691 0.2171 -0.1670 252 TYR A C 2015 O O . TYR A 252 ? 0.9583 1.4685 0.7331 -0.2512 0.2047 -0.1596 252 TYR A O 2016 C CB . TYR A 252 ? 0.9152 1.5512 0.7898 -0.2535 0.2178 -0.1889 252 TYR A CB 2017 C CG . TYR A 252 ? 0.9205 1.6051 0.8259 -0.2511 0.2304 -0.2042 252 TYR A CG 2018 C CD1 . TYR A 252 ? 0.9195 1.6488 0.8508 -0.2707 0.2449 -0.2123 252 TYR A CD1 2019 C CD2 . TYR A 252 ? 0.9164 1.6029 0.8255 -0.2291 0.2279 -0.2115 252 TYR A CD2 2020 C CE1 . TYR A 252 ? 0.9063 1.6848 0.8697 -0.2665 0.2582 -0.2274 252 TYR A CE1 2021 C CE2 . TYR A 252 ? 0.9064 1.6359 0.8424 -0.2243 0.2409 -0.2272 252 TYR A CE2 2022 C CZ . TYR A 252 ? 0.9019 1.6792 0.8666 -0.2421 0.2568 -0.2351 252 TYR A CZ 2023 O OH . TYR A 252 ? 0.9054 1.7298 0.9006 -0.2354 0.2713 -0.2516 252 TYR A OH 2024 N N . ALA A 253 ? 0.9774 1.5193 0.7677 -0.2890 0.2206 -0.1645 253 ALA A N 2025 C CA . ALA A 253 ? 0.9754 1.4805 0.7471 -0.2882 0.2096 -0.1541 253 ALA A CA 2026 C C . ALA A 253 ? 0.9488 1.4840 0.7514 -0.2999 0.2050 -0.1575 253 ALA A C 2027 O O . ALA A 253 ? 0.9398 1.5196 0.7715 -0.3137 0.2123 -0.1667 253 ALA A O 2028 C CB . ALA A 253 ? 1.0272 1.4769 0.7415 -0.3036 0.2196 -0.1460 253 ALA A CB 2029 N N . TYR A 254 ? 0.9326 1.4453 0.7289 -0.2941 0.1929 -0.1507 254 TYR A N 2030 C CA . TYR A 254 ? 0.9157 1.4529 0.7370 -0.3026 0.1851 -0.1534 254 TYR A CA 2031 C C . TYR A 254 ? 0.9498 1.4539 0.7366 -0.3269 0.1908 -0.1508 254 TYR A C 2032 O O . TYR A 254 ? 0.9783 1.4297 0.7240 -0.3241 0.1915 -0.1431 254 TYR A O 2033 C CB . TYR A 254 ? 0.8948 1.4315 0.7326 -0.2799 0.1676 -0.1484 254 TYR A CB 2034 C CG . TYR A 254 ? 0.8565 1.4234 0.7297 -0.2571 0.1587 -0.1507 254 TYR A CG 2035 C CD1 . TYR A 254 ? 0.8552 1.4006 0.7169 -0.2388 0.1567 -0.1463 254 TYR A CD1 2036 C CD2 . TYR A 254 ? 0.8276 1.4422 0.7450 -0.2535 0.1504 -0.1573 254 TYR A CD2 2037 C CE1 . TYR A 254 ? 0.8354 1.4034 0.7265 -0.2196 0.1476 -0.1491 254 TYR A CE1 2038 C CE2 . TYR A 254 ? 0.8087 1.4443 0.7552 -0.2320 0.1414 -0.1596 254 TYR A CE2 2039 C CZ . TYR A 254 ? 0.8202 1.4311 0.7525 -0.2161 0.1405 -0.1557 254 TYR A CZ 2040 O OH . TYR A 254 ? 0.8367 1.4637 0.7949 -0.1964 0.1308 -0.1587 254 TYR A OH 2041 N N . LYS A 255 ? 0.9548 1.4905 0.7597 -0.3504 0.1939 -0.1579 255 LYS A N 2042 C CA . LYS A 255 ? 0.9891 1.4971 0.7659 -0.3755 0.1958 -0.1572 255 LYS A CA 2043 C C . LYS A 255 ? 0.9646 1.4680 0.7470 -0.3659 0.1792 -0.1553 255 LYS A C 2044 O O . LYS A 255 ? 0.9001 1.4462 0.7233 -0.3538 0.1668 -0.1582 255 LYS A O 2045 C CB . LYS A 255 ? 1.0064 1.5560 0.8051 -0.4064 0.2038 -0.1662 255 LYS A CB 2046 C CG . LYS A 255 ? 1.0411 1.5862 0.8220 -0.4256 0.2248 -0.1675 255 LYS A CG 2047 C CD . LYS A 255 ? 1.0377 1.6493 0.8628 -0.4474 0.2331 -0.1783 255 LYS A CD 2048 C CE . LYS A 255 ? 1.0575 1.6835 0.8926 -0.4750 0.2261 -0.1824 255 LYS A CE 2049 N NZ . LYS A 255 ? 1.0671 1.7539 0.9402 -0.5024 0.2378 -0.1921 255 LYS A NZ 2050 N N . ILE A 256 ? 1.0044 1.4535 0.7429 -0.3711 0.1793 -0.1506 256 ILE A N 2051 C CA . ILE A 256 ? 1.0094 1.4477 0.7437 -0.3652 0.1666 -0.1496 256 ILE A CA 2052 C C . ILE A 256 ? 1.0411 1.4880 0.7725 -0.3958 0.1640 -0.1566 256 ILE A C 2053 O O . ILE A 256 ? 1.0910 1.4914 0.7795 -0.4149 0.1700 -0.1569 256 ILE A O 2054 C CB . ILE A 256 ? 1.0320 1.4067 0.7202 -0.3515 0.1688 -0.1424 256 ILE A CB 2055 C CG1 . ILE A 256 ? 1.0004 1.3727 0.6972 -0.3214 0.1684 -0.1355 256 ILE A CG1 2056 C CG2 . ILE A 256 ? 1.0391 1.4013 0.7179 -0.3479 0.1591 -0.1427 256 ILE A CG2 2057 C CD1 . ILE A 256 ? 1.0288 1.3423 0.6834 -0.3078 0.1727 -0.1284 256 ILE A CD1 2058 N N . VAL A 257 ? 1.0297 1.5348 0.8066 -0.4000 0.1536 -0.1624 257 VAL A N 2059 C CA . VAL A 257 ? 1.0653 1.5913 0.8492 -0.4308 0.1488 -0.1701 257 VAL A CA 2060 C C . VAL A 257 ? 1.0843 1.5907 0.8494 -0.4334 0.1338 -0.1707 257 VAL A C 2061 O O . VAL A 257 ? 1.1124 1.6092 0.8605 -0.4617 0.1310 -0.1762 257 VAL A O 2062 C CB . VAL A 257 ? 1.0394 1.6428 0.8846 -0.4357 0.1440 -0.1774 257 VAL A CB 2063 C CG1 . VAL A 257 ? 1.0406 1.6620 0.8992 -0.4367 0.1620 -0.1788 257 VAL A CG1 2064 C CG2 . VAL A 257 ? 1.0013 1.6411 0.8848 -0.4077 0.1263 -0.1760 257 VAL A CG2 2065 N N . LYS A 258 ? 1.0676 1.5677 0.8340 -0.4057 0.1245 -0.1652 258 LYS A N 2066 C CA . LYS A 258 ? 1.0965 1.5766 0.8409 -0.4058 0.1118 -0.1652 258 LYS A CA 2067 C C . LYS A 258 ? 1.0985 1.5366 0.8152 -0.3788 0.1147 -0.1573 258 LYS A C 2068 O O . LYS A 258 ? 1.0688 1.5239 0.8093 -0.3538 0.1139 -0.1512 258 LYS A O 2069 C CB . LYS A 258 ? 1.0711 1.6071 0.8581 -0.4035 0.0921 -0.1676 258 LYS A CB 2070 C CG . LYS A 258 ? 1.1095 1.6255 0.8699 -0.4066 0.0778 -0.1678 258 LYS A CG 2071 C CD . LYS A 258 ? 1.1189 1.6890 0.9169 -0.4137 0.0561 -0.1717 258 LYS A CD 2072 C CE . LYS A 258 ? 1.1595 1.7058 0.9240 -0.4177 0.0407 -0.1715 258 LYS A CE 2073 N NZ . LYS A 258 ? 1.1724 1.7663 0.9661 -0.4326 0.0177 -0.1770 258 LYS A NZ 2074 N N . LYS A 259 ? 1.1584 1.5423 0.8253 -0.3845 0.1184 -0.1580 259 LYS A N 2075 C CA . LYS A 259 ? 1.1800 1.5272 0.8209 -0.3600 0.1219 -0.1521 259 LYS A CA 2076 C C . LYS A 259 ? 1.1888 1.5355 0.8175 -0.3605 0.1097 -0.1536 259 LYS A C 2077 O O . LYS A 259 ? 1.1967 1.5675 0.8342 -0.3801 0.0968 -0.1593 259 LYS A O 2078 C CB . LYS A 259 ? 1.2459 1.5286 0.8369 -0.3610 0.1365 -0.1523 259 LYS A CB 2079 C CG . LYS A 259 ? 1.2654 1.5406 0.8628 -0.3480 0.1476 -0.1465 259 LYS A CG 2080 C CD . LYS A 259 ? 1.3379 1.5491 0.8849 -0.3547 0.1596 -0.1471 259 LYS A CD 2081 C CE . LYS A 259 ? 1.3527 1.5560 0.9032 -0.3428 0.1683 -0.1406 259 LYS A CE 2082 N NZ . LYS A 259 ? 1.4184 1.5683 0.9242 -0.3603 0.1780 -0.1414 259 LYS A NZ 2083 N N . GLY A 260 ? 1.2059 1.5273 0.8150 -0.3390 0.1136 -0.1485 260 GLY A N 2084 C CA . GLY A 260 ? 1.2207 1.5342 0.8087 -0.3387 0.1050 -0.1494 260 GLY A CA 2085 C C . GLY A 260 ? 1.1840 1.5132 0.7882 -0.3131 0.1035 -0.1400 260 GLY A C 2086 O O . GLY A 260 ? 1.1633 1.4982 0.7875 -0.2934 0.1117 -0.1332 260 GLY A O 2087 N N . ASP A 261 ? 1.2004 1.5358 0.7945 -0.3153 0.0922 -0.1393 261 ASP A N 2088 C CA . ASP A 261 ? 1.1887 1.5300 0.7867 -0.2950 0.0925 -0.1299 261 ASP A CA 2089 C C . ASP A 261 ? 1.1061 1.4942 0.7570 -0.2831 0.0830 -0.1215 261 ASP A C 2090 O O . ASP A 261 ? 1.0924 1.5147 0.7692 -0.2914 0.0660 -0.1223 261 ASP A O 2091 C CB . ASP A 261 ? 1.2551 1.5857 0.8201 -0.3030 0.0823 -0.1310 261 ASP A CB 2092 C CG . ASP A 261 ? 1.3530 1.6301 0.8602 -0.3034 0.0970 -0.1369 261 ASP A CG 2093 O OD1 . ASP A 261 ? 1.3979 1.6478 0.8946 -0.2934 0.1149 -0.1386 261 ASP A OD1 2094 O OD2 . ASP A 261 ? 1.4119 1.6729 0.8824 -0.3126 0.0900 -0.1401 261 ASP A OD2 2095 N N . SER A 262 ? 1.0532 1.4417 0.7199 -0.2630 0.0935 -0.1140 262 SER A N 2096 C CA . SER A 262 ? 1.0061 1.4311 0.7180 -0.2501 0.0855 -0.1060 262 SER A CA 2097 C C . SER A 262 ? 0.9844 1.3998 0.6974 -0.2308 0.0965 -0.0968 262 SER A C 2098 O O . SER A 262 ? 1.0481 1.4332 0.7306 -0.2262 0.1110 -0.0975 262 SER A O 2099 C CB . SER A 262 ? 0.9757 1.4219 0.7203 -0.2514 0.0857 -0.1098 262 SER A CB 2100 O OG . SER A 262 ? 0.9495 1.4297 0.7359 -0.2398 0.0760 -0.1043 262 SER A OG 2101 N N . THR A 263 ? 1.2599 1.0764 0.8156 -0.2028 0.0617 -0.0481 263 THR A N 2102 C CA . THR A 263 ? 1.1720 1.0106 0.7698 -0.1397 0.0492 -0.0463 263 THR A CA 2103 C C . THR A 263 ? 1.0530 1.0032 0.7438 -0.1321 0.0455 -0.0628 263 THR A C 2104 O O . THR A 263 ? 1.0006 1.0200 0.7482 -0.1629 0.0498 -0.0768 263 THR A O 2105 C CB . THR A 263 ? 1.1258 0.9673 0.7665 -0.1135 0.0428 -0.0468 263 THR A CB 2106 O OG1 . THR A 263 ? 1.1007 0.9554 0.7575 -0.0570 0.0325 -0.0452 263 THR A OG1 2107 C CG2 . THR A 263 ? 1.0271 0.9621 0.7708 -0.1300 0.0431 -0.0635 263 THR A CG2 2108 N N . ILE A 264 ? 1.0208 0.9911 0.7211 -0.0896 0.0381 -0.0629 264 ILE A N 2109 C CA . ILE A 264 ? 0.9149 0.9860 0.7017 -0.0809 0.0356 -0.0809 264 ILE A CA 2110 C C . ILE A 264 ? 0.8504 0.9595 0.7034 -0.0550 0.0307 -0.0900 264 ILE A C 2111 O O . ILE A 264 ? 0.8777 0.9670 0.7106 -0.0198 0.0245 -0.0844 264 ILE A O 2112 C CB . ILE A 264 ? 0.9175 1.0038 0.6780 -0.0563 0.0321 -0.0801 264 ILE A CB 2113 C CG1 . ILE A 264 ? 0.9942 1.0253 0.6725 -0.0836 0.0385 -0.0685 264 ILE A CG1 2114 C CG2 . ILE A 264 ? 0.8288 1.0173 0.6759 -0.0553 0.0318 -0.1019 264 ILE A CG2 2115 C CD1 . ILE A 264 ? 1.0371 1.0676 0.6704 -0.0545 0.0350 -0.0637 264 ILE A CD1 2116 N N . MET A 265 ? 0.7887 0.9512 0.7128 -0.0712 0.0344 -0.1047 265 MET A N 2117 C CA . MET A 265 ? 0.7519 0.9355 0.7282 -0.0561 0.0334 -0.1130 265 MET A CA 2118 C C . MET A 265 ? 0.7259 0.9754 0.7562 -0.0511 0.0362 -0.1329 265 MET A C 2119 O O . MET A 265 ? 0.7481 1.0316 0.7996 -0.0668 0.0408 -0.1432 265 MET A O 2120 C CB . MET A 265 ? 0.7401 0.9198 0.7386 -0.0761 0.0375 -0.1143 265 MET A CB 2121 C CG . MET A 265 ? 0.7232 0.9025 0.7583 -0.0624 0.0375 -0.1182 265 MET A CG 2122 S SD . MET A 265 ? 0.7373 0.9154 0.7846 -0.0799 0.0409 -0.1177 265 MET A SD 2123 C CE . MET A 265 ? 0.7882 0.8994 0.7658 -0.0958 0.0386 -0.0988 265 MET A CE 2124 N N . LYS A 266 ? 0.7274 0.9978 0.7747 -0.0320 0.0346 -0.1404 266 LYS A N 2125 C CA . LYS A 266 ? 0.7135 1.0422 0.8011 -0.0358 0.0402 -0.1623 266 LYS A CA 2126 C C . LYS A 266 ? 0.6915 1.0145 0.8153 -0.0463 0.0488 -0.1739 266 LYS A C 2127 O O . LYS A 266 ? 0.6964 1.0001 0.8220 -0.0397 0.0483 -0.1708 266 LYS A O 2128 C CB . LYS A 266 ? 0.7424 1.1128 0.8224 -0.0152 0.0359 -0.1690 266 LYS A CB 2129 C CG . LYS A 266 ? 0.8147 1.1753 0.8403 0.0098 0.0263 -0.1540 266 LYS A CG 2130 C CD . LYS A 266 ? 0.8409 1.2272 0.8602 0.0003 0.0278 -0.1577 266 LYS A CD 2131 C CE . LYS A 266 ? 0.8588 1.3311 0.9033 0.0069 0.0290 -0.1797 266 LYS A CE 2132 N NZ . LYS A 266 ? 0.8732 1.3791 0.9301 -0.0111 0.0334 -0.1896 266 LYS A NZ 2133 N N . SER A 267 ? 0.6761 1.0104 0.8206 -0.0595 0.0569 -0.1868 267 SER A N 2134 C CA . SER A 267 ? 0.6722 0.9829 0.8328 -0.0629 0.0663 -0.1962 267 SER A CA 2135 C C . SER A 267 ? 0.6870 1.0124 0.8571 -0.0703 0.0764 -0.2153 267 SER A C 2136 O O . SER A 267 ? 0.7045 1.0592 0.8755 -0.0730 0.0738 -0.2167 267 SER A O 2137 C CB . SER A 267 ? 0.6858 0.9658 0.8409 -0.0571 0.0626 -0.1815 267 SER A CB 2138 O OG . SER A 267 ? 0.7020 0.9587 0.8642 -0.0509 0.0709 -0.1893 267 SER A OG 2139 N N . GLU A 268 ? 0.7102 1.0077 0.8786 -0.0744 0.0890 -0.2302 268 GLU A N 2140 C CA . GLU A 268 ? 0.7273 1.0171 0.8895 -0.0778 0.1011 -0.2495 268 GLU A CA 2141 C C . GLU A 268 ? 0.7482 1.0068 0.9002 -0.0554 0.1028 -0.2464 268 GLU A C 2142 O O . GLU A 268 ? 0.7885 1.0399 0.9283 -0.0472 0.1108 -0.2607 268 GLU A O 2143 C CB . GLU A 268 ? 0.7652 1.0264 0.9111 -0.0978 0.1178 -0.2700 268 GLU A CB 2144 C CG . GLU A 268 ? 0.7569 1.0714 0.9138 -0.1190 0.1168 -0.2781 268 GLU A CG 2145 C CD . GLU A 268 ? 0.7519 1.1346 0.9233 -0.1209 0.1095 -0.2825 268 GLU A CD 2146 O OE1 . GLU A 268 ? 0.7427 1.1297 0.9102 -0.1287 0.1176 -0.2979 268 GLU A OE1 2147 O OE2 . GLU A 268 ? 0.7463 1.1732 0.9261 -0.1112 0.0959 -0.2703 268 GLU A OE2 2148 N N . LEU A 269 ? 0.7371 0.9835 0.8912 -0.0423 0.0951 -0.2293 269 LEU A N 2149 C CA . LEU A 269 ? 0.7737 1.0085 0.9184 -0.0161 0.0952 -0.2273 269 LEU A CA 2150 C C . LEU A 269 ? 0.7647 1.0630 0.9208 -0.0112 0.0881 -0.2289 269 LEU A C 2151 O O . LEU A 269 ? 0.7242 1.0634 0.8927 -0.0314 0.0805 -0.2227 269 LEU A O 2152 C CB . LEU A 269 ? 0.7569 0.9743 0.9027 -0.0081 0.0887 -0.2102 269 LEU A CB 2153 C CG . LEU A 269 ? 0.7663 0.9260 0.9003 -0.0122 0.0951 -0.2075 269 LEU A CG 2154 C CD1 . LEU A 269 ? 0.7500 0.9068 0.8909 -0.0077 0.0857 -0.1893 269 LEU A CD1 2155 C CD2 . LEU A 269 ? 0.8305 0.9247 0.9289 0.0044 0.1104 -0.2191 269 LEU A CD2 2156 N N . GLU A 270 ? 0.8142 1.1202 0.9587 0.0176 0.0913 -0.2379 270 GLU A N 2157 C CA . GLU A 270 ? 0.8220 1.2053 0.9769 0.0240 0.0851 -0.2429 270 GLU A CA 2158 C C . GLU A 270 ? 0.7677 1.1910 0.9267 0.0346 0.0774 -0.2343 270 GLU A C 2159 O O . GLU A 270 ? 0.7733 1.1601 0.9295 0.0352 0.0757 -0.2220 270 GLU A O 2160 C CB . GLU A 270 ? 0.9034 1.2885 1.0400 0.0543 0.0932 -0.2631 270 GLU A CB 2161 C CG . GLU A 270 ? 0.9758 1.3155 1.1004 0.0408 0.1040 -0.2758 270 GLU A CG 2162 C CD . GLU A 270 ? 0.9721 1.3702 1.1217 0.0091 0.0996 -0.2788 270 GLU A CD 2163 O OE1 . GLU A 270 ? 0.9635 1.4048 1.1336 -0.0141 0.0893 -0.2646 270 GLU A OE1 2164 O OE2 . GLU A 270 ? 0.9681 1.3609 1.1085 0.0074 0.1077 -0.2955 270 GLU A OE2 2165 N N . TYR A 271 ? 0.7395 1.2472 0.9049 0.0397 0.0734 -0.2431 271 TYR A N 2166 C CA . TYR A 271 ? 0.7065 1.2772 0.8762 0.0403 0.0672 -0.2401 271 TYR A CA 2167 C C . TYR A 271 ? 0.7379 1.2954 0.8928 0.0908 0.0684 -0.2432 271 TYR A C 2168 O O . TYR A 271 ? 0.7595 1.2984 0.8934 0.1368 0.0736 -0.2552 271 TYR A O 2169 C CB . TYR A 271 ? 0.6817 1.3636 0.8597 0.0285 0.0645 -0.2541 271 TYR A CB 2170 C CG . TYR A 271 ? 0.6584 1.4239 0.8392 0.0116 0.0601 -0.2553 271 TYR A CG 2171 C CD1 . TYR A 271 ? 0.6375 1.3757 0.8128 -0.0323 0.0584 -0.2393 271 TYR A CD1 2172 C CD2 . TYR A 271 ? 0.6582 1.5363 0.8419 0.0390 0.0585 -0.2752 271 TYR A CD2 2173 C CE1 . TYR A 271 ? 0.6333 1.4466 0.8045 -0.0568 0.0571 -0.2435 271 TYR A CE1 2174 C CE2 . TYR A 271 ? 0.6417 1.6150 0.8278 0.0166 0.0559 -0.2811 271 TYR A CE2 2175 C CZ . TYR A 271 ? 0.6357 1.5735 0.8150 -0.0358 0.0561 -0.2655 271 TYR A CZ 2176 O OH . TYR A 271 ? 0.6062 1.6374 0.7815 -0.0660 0.0561 -0.2743 271 TYR A OH 2177 N N . GLY A 272 ? 0.7490 1.3118 0.9067 0.0842 0.0640 -0.2323 272 GLY A N 2178 C CA . GLY A 272 ? 0.7938 1.3357 0.9342 0.1317 0.0647 -0.2316 272 GLY A CA 2179 C C . GLY A 272 ? 0.8170 1.4715 0.9579 0.1612 0.0594 -0.2441 272 GLY A C 2180 O O . GLY A 272 ? 0.8389 1.4834 0.9608 0.2085 0.0591 -0.2438 272 GLY A O 2181 N N . ASN A 273 ? 0.8266 1.5936 0.9851 0.1337 0.0560 -0.2565 273 ASN A N 2182 C CA . ASN A 273 ? 0.8561 1.7624 1.0185 0.1522 0.0513 -0.2735 273 ASN A CA 2183 C C . ASN A 273 ? 0.8404 1.7548 1.0029 0.1482 0.0481 -0.2649 273 ASN A C 2184 O O . ASN A 273 ? 0.8736 1.8017 1.0212 0.2075 0.0462 -0.2684 273 ASN A O 2185 C CB . ASN A 273 ? 0.9156 1.8595 1.0565 0.2330 0.0514 -0.2914 273 ASN A CB 2186 C CG . ASN A 273 ? 0.9476 1.9210 1.0905 0.2335 0.0538 -0.3058 273 ASN A CG 2187 O OD1 . ASN A 273 ? 0.9930 1.8626 1.1181 0.2509 0.0598 -0.3025 273 ASN A OD1 2188 N ND2 . ASN A 273 ? 0.9393 2.0585 1.1014 0.2094 0.0505 -0.3238 273 ASN A ND2 2189 N N . CYS A 274 ? 0.8043 1.7058 0.9761 0.0800 0.0482 -0.2537 274 CYS A N 2190 C CA . CYS A 274 ? 0.7994 1.6424 0.9673 0.0701 0.0470 -0.2376 274 CYS A CA 2191 C C . CYS A 274 ? 0.7338 1.5919 0.8994 -0.0072 0.0482 -0.2323 274 CYS A C 2192 O O . CYS A 274 ? 0.7388 1.6040 0.8991 -0.0552 0.0512 -0.2340 274 CYS A O 2193 C CB . CYS A 274 ? 0.8684 1.5625 1.0290 0.0852 0.0496 -0.2186 274 CYS A CB 2194 S SG . CYS A 274 ? 0.9939 1.5988 1.1511 0.0610 0.0486 -0.1964 274 CYS A SG 2195 N N . ASN A 275 ? 0.6969 1.5489 0.8573 -0.0193 0.0471 -0.2257 275 ASN A N 2196 C CA . ASN A 275 ? 0.6992 1.5424 0.8411 -0.0928 0.0506 -0.2207 275 ASN A CA 2197 C C . ASN A 275 ? 0.7154 1.4509 0.8465 -0.0970 0.0495 -0.1998 275 ASN A C 2198 O O . ASN A 275 ? 0.7357 1.4511 0.8781 -0.0491 0.0458 -0.1948 275 ASN A O 2199 C CB . ASN A 275 ? 0.6985 1.6891 0.8374 -0.1235 0.0529 -0.2438 275 ASN A CB 2200 C CG . ASN A 275 ? 0.7213 1.6984 0.8236 -0.2124 0.0612 -0.2432 275 ASN A CG 2201 O OD1 . ASN A 275 ? 0.7373 1.6383 0.8128 -0.2540 0.0661 -0.2334 275 ASN A OD1 2202 N ND2 . ASN A 275 ? 0.7490 1.7967 0.8411 -0.2417 0.0642 -0.2548 275 ASN A ND2 2203 N N . THR A 276 ? 0.7271 1.3890 0.8285 -0.1517 0.0531 -0.1878 276 THR A N 2204 C CA . THR A 276 ? 0.7255 1.2823 0.8117 -0.1537 0.0517 -0.1684 276 THR A CA 2205 C C . THR A 276 ? 0.7833 1.2814 0.8173 -0.2180 0.0577 -0.1612 276 THR A C 2206 O O . THR A 276 ? 0.8289 1.3442 0.8352 -0.2613 0.0637 -0.1677 276 THR A O 2207 C CB . THR A 276 ? 0.7138 1.1729 0.8130 -0.1140 0.0481 -0.1527 276 THR A CB 2208 O OG1 . THR A 276 ? 0.7243 1.1010 0.8124 -0.1105 0.0461 -0.1369 276 THR A OG1 2209 C CG2 . THR A 276 ? 0.7332 1.1499 0.8168 -0.1350 0.0499 -0.1482 276 THR A CG2 2210 N N . LYS A 277 ? 0.8328 1.2526 0.8451 -0.2227 0.0570 -0.1478 277 LYS A N 2211 C CA . LYS A 277 ? 0.9152 1.2452 0.8604 -0.2733 0.0633 -0.1380 277 LYS A CA 2212 C C . LYS A 277 ? 0.8990 1.1075 0.8264 -0.2461 0.0587 -0.1167 277 LYS A C 2213 O O . LYS A 277 ? 0.9458 1.0618 0.8072 -0.2724 0.0628 -0.1060 277 LYS A O 2214 C CB . LYS A 277 ? 0.9886 1.3206 0.9085 -0.3022 0.0673 -0.1414 277 LYS A CB 2215 C CG . LYS A 277 ? 1.0140 1.4897 0.9553 -0.3249 0.0711 -0.1659 277 LYS A CG 2216 C CD . LYS A 277 ? 1.0892 1.5639 0.9807 -0.3843 0.0805 -0.1738 277 LYS A CD 2217 C CE . LYS A 277 ? 1.1862 1.6329 0.9997 -0.4672 0.0959 -0.1819 277 LYS A CE 2218 N NZ . LYS A 277 ? 1.2696 1.6824 1.0143 -0.5337 0.1087 -0.1892 277 LYS A NZ 2219 N N . CYS A 278 ? 0.8370 1.0463 0.8150 -0.1932 0.0512 -0.1124 278 CYS A N 2220 C CA . CYS A 278 ? 0.8476 0.9709 0.8167 -0.1661 0.0467 -0.0972 278 CYS A CA 2221 C C . CYS A 278 ? 0.7681 0.9196 0.7852 -0.1301 0.0436 -0.1012 278 CYS A C 2222 O O . CYS A 278 ? 0.7114 0.9034 0.7715 -0.1018 0.0425 -0.1079 278 CYS A O 2223 C CB . CYS A 278 ? 0.8697 0.9460 0.8397 -0.1452 0.0428 -0.0877 278 CYS A CB 2224 S SG . CYS A 278 ? 0.9214 0.9210 0.8854 -0.1077 0.0367 -0.0741 278 CYS A SG 2225 N N . GLN A 279 ? 0.7551 0.8791 0.7560 -0.1311 0.0433 -0.0977 279 GLN A N 2226 C CA . GLN A 279 ? 0.7157 0.8689 0.7556 -0.1063 0.0424 -0.1047 279 GLN A CA 2227 C C . GLN A 279 ? 0.7056 0.8102 0.7400 -0.0853 0.0389 -0.0971 279 GLN A C 2228 O O . GLN A 279 ? 0.7362 0.7901 0.7245 -0.0906 0.0367 -0.0865 279 GLN A O 2229 C CB . GLN A 279 ? 0.7126 0.9100 0.7465 -0.1281 0.0457 -0.1134 279 GLN A CB 2230 C CG . GLN A 279 ? 0.6761 0.9081 0.7481 -0.1049 0.0461 -0.1237 279 GLN A CG 2231 C CD . GLN A 279 ? 0.6492 0.9280 0.7589 -0.0796 0.0478 -0.1356 279 GLN A CD 2232 O OE1 . GLN A 279 ? 0.6518 0.9908 0.7659 -0.0856 0.0489 -0.1446 279 GLN A OE1 2233 N NE2 . GLN A 279 ? 0.6353 0.8871 0.7643 -0.0506 0.0491 -0.1374 279 GLN A NE2 2234 N N . THR A 280 ? 0.6718 0.7925 0.7451 -0.0612 0.0396 -0.1042 280 THR A N 2235 C CA . THR A 280 ? 0.6876 0.7914 0.7632 -0.0455 0.0378 -0.1039 280 THR A CA 2236 C C . THR A 280 ? 0.6817 0.8220 0.7852 -0.0419 0.0426 -0.1183 280 THR A C 2237 O O . THR A 280 ? 0.6954 0.8609 0.8177 -0.0415 0.0473 -0.1274 280 THR A O 2238 C CB . THR A 280 ? 0.6733 0.7567 0.7616 -0.0288 0.0374 -0.1021 280 THR A CB 2239 O OG1 . THR A 280 ? 0.6453 0.7444 0.7645 -0.0221 0.0446 -0.1137 280 THR A OG1 2240 C CG2 . THR A 280 ? 0.6864 0.7420 0.7587 -0.0316 0.0347 -0.0917 280 THR A CG2 2241 N N . PRO A 281 ? 0.6866 0.8330 0.7889 -0.0363 0.0418 -0.1222 281 PRO A N 2242 C CA . PRO A 281 ? 0.6806 0.8606 0.8041 -0.0385 0.0478 -0.1380 281 PRO A CA 2243 C C . PRO A 281 ? 0.7003 0.8761 0.8451 -0.0352 0.0575 -0.1508 281 PRO A C 2244 O O . PRO A 281 ? 0.7075 0.8988 0.8604 -0.0384 0.0647 -0.1649 281 PRO A O 2245 C CB . PRO A 281 ? 0.6825 0.8773 0.7989 -0.0319 0.0449 -0.1409 281 PRO A CB 2246 C CG . PRO A 281 ? 0.7035 0.8689 0.7821 -0.0216 0.0356 -0.1236 281 PRO A CG 2247 C CD . PRO A 281 ? 0.7038 0.8313 0.7760 -0.0258 0.0350 -0.1129 281 PRO A CD 2248 N N . MET A 282 ? 0.7269 0.8732 0.8718 -0.0284 0.0590 -0.1461 282 MET A N 2249 C CA . MET A 282 ? 0.7615 0.8824 0.9083 -0.0233 0.0701 -0.1558 282 MET A CA 2250 C C . MET A 282 ? 0.7356 0.8462 0.8788 -0.0074 0.0704 -0.1515 282 MET A C 2251 O O . MET A 282 ? 0.7647 0.8469 0.8962 0.0060 0.0800 -0.1592 282 MET A O 2252 C CB . MET A 282 ? 0.8339 0.9298 0.9770 -0.0258 0.0734 -0.1549 282 MET A CB 2253 C CG . MET A 282 ? 0.9007 1.0240 1.0467 -0.0397 0.0757 -0.1658 282 MET A CG 2254 S SD . MET A 282 ? 1.0691 1.1867 1.2126 -0.0391 0.0739 -0.1613 282 MET A SD 2255 C CE . MET A 282 ? 1.0671 1.1214 1.1963 -0.0421 0.0881 -0.1630 282 MET A CE 2256 N N . GLY A 283 ? 0.6919 0.8237 0.8366 -0.0083 0.0611 -0.1406 283 GLY A N 2257 C CA . GLY A 283 ? 0.6989 0.8441 0.8423 0.0062 0.0603 -0.1390 283 GLY A CA 2258 C C . GLY A 283 ? 0.6873 0.8475 0.8265 -0.0068 0.0521 -0.1275 283 GLY A C 2259 O O . GLY A 283 ? 0.6831 0.8231 0.8122 -0.0221 0.0476 -0.1184 283 GLY A O 2260 N N . ALA A 284 ? 0.6915 0.8874 0.8315 0.0008 0.0510 -0.1295 284 ALA A N 2261 C CA . ALA A 284 ? 0.7127 0.9290 0.8430 -0.0203 0.0461 -0.1230 284 ALA A CA 2262 C C . ALA A 284 ? 0.7353 0.9264 0.8643 -0.0079 0.0447 -0.1153 284 ALA A C 2263 O O . ALA A 284 ? 0.7338 0.9046 0.8684 0.0211 0.0480 -0.1163 284 ALA A O 2264 C CB . ALA A 284 ? 0.7109 1.0065 0.8431 -0.0279 0.0462 -0.1343 284 ALA A CB 2265 N N . ILE A 285 ? 0.7651 0.9500 0.8779 -0.0320 0.0413 -0.1078 285 ILE A N 2266 C CA . ILE A 285 ? 0.7884 0.9471 0.8977 -0.0251 0.0395 -0.0999 285 ILE A CA 2267 C C . ILE A 285 ? 0.8227 1.0352 0.9249 -0.0413 0.0389 -0.1046 285 ILE A C 2268 O O . ILE A 285 ? 0.8589 1.0936 0.9399 -0.0787 0.0402 -0.1083 285 ILE A O 2269 C CB . ILE A 285 ? 0.7829 0.8764 0.8710 -0.0370 0.0366 -0.0878 285 ILE A CB 2270 C CG1 . ILE A 285 ? 0.7695 0.8316 0.8695 -0.0187 0.0373 -0.0869 285 ILE A CG1 2271 C CG2 . ILE A 285 ? 0.7796 0.8515 0.8594 -0.0357 0.0345 -0.0807 285 ILE A CG2 2272 C CD1 . ILE A 285 ? 0.7789 0.7978 0.8561 -0.0218 0.0331 -0.0785 285 ILE A CD1 2273 N N . ASN A 286 ? 0.8577 1.0915 0.9717 -0.0155 0.0384 -0.1057 286 ASN A N 2274 C CA . ASN A 286 ? 0.9083 1.2064 1.0183 -0.0274 0.0376 -0.1125 286 ASN A CA 2275 C C . ASN A 286 ? 0.8748 1.1359 0.9828 -0.0153 0.0357 -0.1029 286 ASN A C 2276 O O . ASN A 286 ? 0.8322 1.1012 0.9513 0.0245 0.0353 -0.1023 286 ASN A O 2277 C CB . ASN A 286 ? 0.9728 1.3626 1.0985 0.0041 0.0379 -0.1272 286 ASN A CB 2278 C CG . ASN A 286 ? 1.0915 1.5756 1.2163 -0.0041 0.0368 -0.1386 286 ASN A CG 2279 O OD1 . ASN A 286 ? 1.0485 1.5504 1.1571 -0.0558 0.0387 -0.1420 286 ASN A OD1 2280 N ND2 . ASN A 286 ? 1.2736 1.8181 1.4076 0.0481 0.0349 -0.1461 286 ASN A ND2 2281 N N . SER A 287 ? 0.8731 1.0848 0.9586 -0.0469 0.0351 -0.0950 287 SER A N 2282 C CA . SER A 287 ? 0.8856 1.0644 0.9678 -0.0381 0.0331 -0.0868 287 SER A CA 2283 C C . SER A 287 ? 0.9109 1.0553 0.9555 -0.0798 0.0340 -0.0840 287 SER A C 2284 O O . SER A 287 ? 0.9283 1.0441 0.9391 -0.1136 0.0369 -0.0844 287 SER A O 2285 C CB . SER A 287 ? 0.8823 0.9918 0.9744 -0.0086 0.0319 -0.0755 287 SER A CB 2286 O OG . SER A 287 ? 0.8885 0.9372 0.9606 -0.0244 0.0304 -0.0682 287 SER A OG 2287 N N . SER A 288 ? 0.9225 1.0604 0.9645 -0.0759 0.0327 -0.0809 288 SER A N 2288 C CA . SER A 288 ? 0.9626 1.0568 0.9607 -0.1127 0.0349 -0.0791 288 SER A CA 2289 C C . SER A 288 ? 0.9349 0.9374 0.9185 -0.0933 0.0311 -0.0645 288 SER A C 2290 O O . SER A 288 ? 0.9671 0.9206 0.9105 -0.1117 0.0322 -0.0616 288 SER A O 2291 C CB . SER A 288 ? 0.9859 1.1492 0.9885 -0.1253 0.0365 -0.0893 288 SER A CB 2292 O OG . SER A 288 ? 0.9807 1.1734 1.0233 -0.0770 0.0317 -0.0854 288 SER A OG 2293 N N . MET A 289 ? 0.8646 0.8474 0.8757 -0.0580 0.0275 -0.0577 289 MET A N 2294 C CA . MET A 289 ? 0.8610 0.7812 0.8634 -0.0374 0.0237 -0.0477 289 MET A CA 2295 C C . MET A 289 ? 0.8933 0.7478 0.8424 -0.0497 0.0231 -0.0433 289 MET A C 2296 O O . MET A 289 ? 0.9210 0.7750 0.8524 -0.0668 0.0257 -0.0459 289 MET A O 2297 C CB . MET A 289 ? 0.8519 0.7796 0.8919 -0.0065 0.0228 -0.0464 289 MET A CB 2298 C CG . MET A 289 ? 0.8378 0.8057 0.9123 0.0127 0.0256 -0.0493 289 MET A CG 2299 S SD . MET A 289 ? 0.8639 0.8199 0.9423 0.0278 0.0245 -0.0433 289 MET A SD 2300 C CE . MET A 289 ? 0.8503 0.8060 0.9493 0.0573 0.0310 -0.0437 289 MET A CE 2301 N N . PRO A 290 ? 0.9128 0.7093 0.8295 -0.0368 0.0198 -0.0364 290 PRO A N 2302 C CA . PRO A 290 ? 0.9588 0.6825 0.8109 -0.0343 0.0188 -0.0311 290 PRO A CA 2303 C C . PRO A 290 ? 0.9292 0.6599 0.7969 -0.0031 0.0140 -0.0295 290 PRO A C 2304 O O . PRO A 290 ? 0.9944 0.6737 0.8068 0.0056 0.0127 -0.0254 290 PRO A O 2305 C CB . PRO A 290 ? 0.9902 0.6585 0.8033 -0.0206 0.0161 -0.0261 290 PRO A CB 2306 C CG . PRO A 290 ? 0.9317 0.6565 0.8114 -0.0019 0.0128 -0.0274 290 PRO A CG 2307 C CD . PRO A 290 ? 0.8923 0.6846 0.8199 -0.0220 0.0171 -0.0336 290 PRO A CD 2308 N N . PHE A 291 ? 0.8384 0.6280 0.7711 0.0130 0.0128 -0.0337 291 PHE A N 2309 C CA . PHE A 291 ? 0.8214 0.6311 0.7709 0.0354 0.0102 -0.0366 291 PHE A CA 2310 C C . PHE A 291 ? 0.7575 0.6213 0.7609 0.0283 0.0149 -0.0442 291 PHE A C 2311 O O . PHE A 291 ? 0.7361 0.6223 0.7678 0.0200 0.0189 -0.0461 291 PHE A O 2312 C CB . PHE A 291 ? 0.8313 0.6513 0.7924 0.0630 0.0060 -0.0378 291 PHE A CB 2313 C CG . PHE A 291 ? 0.8957 0.6643 0.7991 0.0845 0.0001 -0.0319 291 PHE A CG 2314 C CD1 . PHE A 291 ? 0.9614 0.7007 0.8130 0.1085 -0.0045 -0.0299 291 PHE A CD1 2315 C CD2 . PHE A 291 ? 0.9200 0.6672 0.8147 0.0867 -0.0010 -0.0286 291 PHE A CD2 2316 C CE1 . PHE A 291 ? 1.0337 0.7142 0.8175 0.1383 -0.0098 -0.0245 291 PHE A CE1 2317 C CE2 . PHE A 291 ? 0.9827 0.6748 0.8160 0.1109 -0.0060 -0.0242 291 PHE A CE2 2318 C CZ . PHE A 291 ? 1.0435 0.6983 0.8176 0.1389 -0.0103 -0.0220 291 PHE A CZ 2319 N N . HIS A 292 ? 0.7191 0.6022 0.7301 0.0359 0.0148 -0.0493 292 HIS A N 2320 C CA . HIS A 292 ? 0.6631 0.5875 0.7171 0.0315 0.0209 -0.0587 292 HIS A CA 2321 C C . HIS A 292 ? 0.6383 0.5892 0.6988 0.0429 0.0206 -0.0671 292 HIS A C 2322 O O . HIS A 292 ? 0.6495 0.5947 0.6811 0.0600 0.0137 -0.0649 292 HIS A O 2323 C CB . HIS A 292 ? 0.6757 0.6126 0.7335 0.0153 0.0241 -0.0610 292 HIS A CB 2324 C CG . HIS A 292 ? 0.7124 0.6432 0.7439 0.0124 0.0213 -0.0606 292 HIS A CG 2325 N ND1 . HIS A 292 ? 0.7096 0.6697 0.7577 0.0149 0.0233 -0.0689 292 HIS A ND1 2326 C CD2 . HIS A 292 ? 0.7677 0.6584 0.7480 0.0070 0.0180 -0.0529 292 HIS A CD2 2327 C CE1 . HIS A 292 ? 0.7467 0.6928 0.7605 0.0149 0.0199 -0.0654 292 HIS A CE1 2328 N NE2 . HIS A 292 ? 0.7840 0.6811 0.7513 0.0104 0.0172 -0.0550 292 HIS A NE2 2329 N N . ASN A 293 ? 0.6061 0.5854 0.6966 0.0344 0.0289 -0.0781 293 ASN A N 2330 C CA . ASN A 293 ? 0.6034 0.6236 0.7023 0.0351 0.0314 -0.0915 293 ASN A CA 2331 C C . ASN A 293 ? 0.6137 0.6515 0.7273 0.0193 0.0397 -0.1024 293 ASN A C 2332 O O . ASN A 293 ? 0.6012 0.6697 0.7252 0.0073 0.0481 -0.1177 293 ASN A O 2333 C CB . ASN A 293 ? 0.5963 0.6337 0.7063 0.0309 0.0374 -0.0997 293 ASN A CB 2334 C CG . ASN A 293 ? 0.6061 0.6173 0.7261 0.0126 0.0507 -0.1027 293 ASN A CG 2335 O OD1 . ASN A 293 ? 0.6210 0.6065 0.7416 0.0110 0.0536 -0.0984 293 ASN A OD1 2336 N ND2 . ASN A 293 ? 0.6161 0.6329 0.7362 0.0007 0.0596 -0.1109 293 ASN A ND2 2337 N N . ILE A 294 ? 0.6278 0.6497 0.7387 0.0161 0.0385 -0.0965 294 ILE A N 2338 C CA . ILE A 294 ? 0.6413 0.6777 0.7634 0.0050 0.0456 -0.1063 294 ILE A CA 2339 C C . ILE A 294 ? 0.6294 0.7016 0.7484 0.0051 0.0428 -0.1141 294 ILE A C 2340 O O . ILE A 294 ? 0.6254 0.7257 0.7557 -0.0061 0.0509 -0.1296 294 ILE A O 2341 C CB . ILE A 294 ? 0.6531 0.6793 0.7735 0.0031 0.0444 -0.1001 294 ILE A CB 2342 C CG1 . ILE A 294 ? 0.6654 0.6714 0.7867 0.0086 0.0454 -0.0932 294 ILE A CG1 2343 C CG2 . ILE A 294 ? 0.6516 0.6931 0.7822 -0.0028 0.0522 -0.1119 294 ILE A CG2 2344 C CD1 . ILE A 294 ? 0.6871 0.6731 0.8122 0.0130 0.0553 -0.0985 294 ILE A CD1 2345 N N . HIS A 295 ? 0.6475 0.7140 0.7431 0.0167 0.0326 -0.1039 295 HIS A N 2346 C CA . HIS A 295 ? 0.6592 0.7546 0.7424 0.0236 0.0287 -0.1083 295 HIS A CA 2347 C C . HIS A 295 ? 0.7037 0.7625 0.7373 0.0430 0.0183 -0.0926 295 HIS A C 2348 O O . HIS A 295 ? 0.7186 0.7291 0.7302 0.0349 0.0173 -0.0804 295 HIS A O 2349 C CB . HIS A 295 ? 0.6616 0.7682 0.7584 0.0068 0.0343 -0.1144 295 HIS A CB 2350 C CG . HIS A 295 ? 0.6808 0.8280 0.7742 0.0099 0.0331 -0.1235 295 HIS A CG 2351 N ND1 . HIS A 295 ? 0.7194 0.8582 0.7755 0.0258 0.0245 -0.1137 295 HIS A ND1 2352 C CD2 . HIS A 295 ? 0.6842 0.8772 0.7998 -0.0014 0.0405 -0.1420 295 HIS A CD2 2353 C CE1 . HIS A 295 ? 0.7223 0.9092 0.7833 0.0288 0.0249 -0.1250 295 HIS A CE1 2354 N NE2 . HIS A 295 ? 0.6925 0.9176 0.7926 0.0098 0.0346 -0.1434 295 HIS A NE2 2355 N N . PRO A 296 ? 0.7270 0.8066 0.7340 0.0690 0.0118 -0.0942 296 PRO A N 2356 C CA . PRO A 296 ? 0.7929 0.8146 0.7313 0.0945 0.0035 -0.0782 296 PRO A CA 2357 C C . PRO A 296 ? 0.8441 0.8153 0.7402 0.0798 0.0050 -0.0675 296 PRO A C 2358 O O . PRO A 296 ? 0.8856 0.7801 0.7209 0.0790 0.0042 -0.0532 296 PRO A O 2359 C CB . PRO A 296 ? 0.8039 0.8751 0.7236 0.1351 -0.0038 -0.0857 296 PRO A CB 2360 C CG . PRO A 296 ? 0.7522 0.9119 0.7298 0.1175 0.0020 -0.1065 296 PRO A CG 2361 C CD . PRO A 296 ? 0.7101 0.8668 0.7393 0.0790 0.0123 -0.1122 296 PRO A CD 2362 N N . LEU A 297 ? 0.8524 0.8640 0.7730 0.0651 0.0085 -0.0758 297 LEU A N 2363 C CA . LEU A 297 ? 0.9062 0.8815 0.7885 0.0467 0.0110 -0.0680 297 LEU A CA 2364 C C . LEU A 297 ? 0.8667 0.8330 0.7717 0.0062 0.0181 -0.0680 297 LEU A C 2365 O O . LEU A 297 ? 0.8597 0.8771 0.8169 -0.0106 0.0227 -0.0795 297 LEU A O 2366 C CB . LEU A 297 ? 0.8968 0.9279 0.7963 0.0497 0.0113 -0.0781 297 LEU A CB 2367 C CG . LEU A 297 ? 0.9479 1.0160 0.8286 0.0921 0.0039 -0.0827 297 LEU A CG 2368 C CD1 . LEU A 297 ? 0.9290 1.0718 0.8440 0.0867 0.0061 -0.0980 297 LEU A CD1 2369 C CD2 . LEU A 297 ? 1.0456 1.0376 0.8290 0.1274 -0.0025 -0.0647 297 LEU A CD2 2370 N N . THR A 298 ? 0.8881 0.7929 0.7486 -0.0080 0.0195 -0.0570 298 THR A N 2371 C CA . THR A 298 ? 0.8514 0.7652 0.7282 -0.0467 0.0261 -0.0598 298 THR A CA 2372 C C . THR A 298 ? 0.9150 0.7783 0.7201 -0.0786 0.0316 -0.0528 298 THR A C 2373 O O . THR A 298 ? 0.9612 0.7540 0.6897 -0.0674 0.0307 -0.0418 298 THR A O 2374 C CB . THR A 298 ? 0.8300 0.7310 0.7199 -0.0494 0.0262 -0.0578 298 THR A CB 2375 O OG1 . THR A 298 ? 0.8922 0.7115 0.7071 -0.0498 0.0257 -0.0455 298 THR A OG1 2376 C CG2 . THR A 298 ? 0.7933 0.7269 0.7357 -0.0207 0.0225 -0.0630 298 THR A CG2 2377 N N . ILE A 299 ? 0.9074 0.8079 0.7305 -0.1176 0.0381 -0.0606 299 ILE A N 2378 C CA . ILE A 299 ? 0.9926 0.8539 0.7457 -0.1634 0.0469 -0.0581 299 ILE A CA 2379 C C . ILE A 299 ? 0.9838 0.8800 0.7523 -0.1998 0.0525 -0.0666 299 ILE A C 2380 O O . ILE A 299 ? 0.9047 0.8831 0.7491 -0.1897 0.0500 -0.0775 299 ILE A O 2381 C CB . ILE A 299 ? 1.0122 0.9118 0.7653 -0.1822 0.0506 -0.0643 299 ILE A CB 2382 C CG1 . ILE A 299 ? 1.0949 0.9495 0.7642 -0.2389 0.0625 -0.0630 299 ILE A CG1 2383 C CG2 . ILE A 299 ? 0.9332 0.9441 0.7777 -0.1812 0.0497 -0.0813 299 ILE A CG2 2384 C CD1 . ILE A 299 ? 1.1263 0.9963 0.7742 -0.2563 0.0667 -0.0654 299 ILE A CD1 2385 N N . GLY A 300 ? 1.0826 0.9132 0.7702 -0.2409 0.0613 -0.0626 300 GLY A N 2386 C CA . GLY A 300 ? 1.1251 0.9934 0.8167 -0.2820 0.0680 -0.0731 300 GLY A CA 2387 C C . GLY A 300 ? 1.2056 1.0052 0.8656 -0.2737 0.0670 -0.0649 300 GLY A C 2388 O O . GLY A 300 ? 1.2569 0.9714 0.8810 -0.2363 0.0616 -0.0506 300 GLY A O 2389 N N . GLU A 301 ? 1.2384 1.0841 0.9109 -0.3061 0.0720 -0.0758 301 GLU A N 2390 C CA . GLU A 301 ? 1.2923 1.0852 0.9414 -0.3017 0.0715 -0.0705 301 GLU A CA 2391 C C . GLU A 301 ? 1.1715 1.0128 0.9106 -0.2413 0.0582 -0.0675 301 GLU A C 2392 O O . GLU A 301 ? 1.0800 1.0193 0.8908 -0.2345 0.0557 -0.0783 301 GLU A O 2393 C CB . GLU A 301 ? 1.3536 1.1928 0.9848 -0.3619 0.0824 -0.0862 301 GLU A CB 2394 C CG . GLU A 301 ? 1.5137 1.2321 1.0317 -0.4057 0.0946 -0.0820 301 GLU A CG 2395 C CD . GLU A 301 ? 1.6589 1.3039 1.0687 -0.4685 0.1115 -0.0842 301 GLU A CD 2396 O OE1 . GLU A 301 ? 1.7074 1.3238 1.1032 -0.4510 0.1094 -0.0757 301 GLU A OE1 2397 O OE2 . GLU A 301 ? 1.7498 1.3634 1.0820 -0.5396 0.1283 -0.0953 301 GLU A OE2 2398 N N . CYS A 302 ? 1.1648 0.9374 0.8916 -0.1967 0.0508 -0.0539 302 CYS A N 2399 C CA . CYS A 302 ? 1.0792 0.8930 0.8822 -0.1456 0.0406 -0.0523 302 CYS A CA 2400 C C . CYS A 302 ? 1.0641 0.8252 0.8520 -0.1199 0.0359 -0.0439 302 CYS A C 2401 O O . CYS A 302 ? 1.1155 0.7871 0.8238 -0.1260 0.0383 -0.0361 302 CYS A O 2402 C CB . CYS A 302 ? 1.0792 0.8958 0.8989 -0.1134 0.0354 -0.0493 302 CYS A CB 2403 S SG . CYS A 302 ? 1.0778 0.9722 0.9366 -0.1314 0.0389 -0.0608 302 CYS A SG 2404 N N . PRO A 303 ? 0.9814 0.7911 0.8378 -0.0900 0.0303 -0.0459 303 PRO A N 2405 C CA . PRO A 303 ? 0.9818 0.7522 0.8310 -0.0595 0.0248 -0.0388 303 PRO A CA 2406 C C . PRO A 303 ? 0.9979 0.7314 0.8197 -0.0246 0.0191 -0.0329 303 PRO A C 2407 O O . PRO A 303 ? 0.9862 0.7371 0.8120 -0.0216 0.0191 -0.0349 303 PRO A O 2408 C CB . PRO A 303 ? 0.9165 0.7528 0.8431 -0.0414 0.0226 -0.0440 303 PRO A CB 2409 C CG . PRO A 303 ? 0.8773 0.7785 0.8407 -0.0598 0.0270 -0.0532 303 PRO A CG 2410 C CD . PRO A 303 ? 0.9095 0.8046 0.8419 -0.0821 0.0300 -0.0552 303 PRO A CD 2411 N N . LYS A 304 ? 1.0168 0.7095 0.8110 0.0046 0.0141 -0.0273 304 LYS A N 2412 C CA . LYS A 304 ? 1.0449 0.7154 0.8059 0.0460 0.0076 -0.0238 304 LYS A CA 2413 C C . LYS A 304 ? 0.9425 0.6972 0.7789 0.0696 0.0033 -0.0328 304 LYS A C 2414 O O . LYS A 304 ? 0.9107 0.7030 0.7982 0.0681 0.0038 -0.0372 304 LYS A O 2415 C CB . LYS A 304 ? 1.1501 0.7416 0.8368 0.0723 0.0042 -0.0158 304 LYS A CB 2416 C CG . LYS A 304 ? 1.2946 0.7862 0.8921 0.0388 0.0125 -0.0091 304 LYS A CG 2417 C CD . LYS A 304 ? 1.4147 0.8400 0.9316 0.0292 0.0176 -0.0036 304 LYS A CD 2418 C CE . LYS A 304 ? 1.4835 0.8609 0.9515 -0.0365 0.0313 -0.0047 304 LYS A CE 2419 N NZ . LYS A 304 ? 1.6149 0.8918 0.9712 -0.0463 0.0389 0.0029 304 LYS A NZ 2420 N N . TYR A 305 ? 0.9032 0.6861 0.7404 0.0873 0.0007 -0.0367 305 TYR A N 2421 C CA . TYR A 305 ? 0.8202 0.6857 0.7215 0.0975 0.0000 -0.0493 305 TYR A CA 2422 C C . TYR A 305 ? 0.8249 0.7137 0.7198 0.1345 -0.0065 -0.0532 305 TYR A C 2423 O O . TYR A 305 ? 0.8894 0.7478 0.7236 0.1711 -0.0135 -0.0483 305 TYR A O 2424 C CB . TYR A 305 ? 0.8091 0.7087 0.7147 0.0990 0.0004 -0.0553 305 TYR A CB 2425 C CG . TYR A 305 ? 0.7409 0.7253 0.7022 0.1034 0.0020 -0.0719 305 TYR A CG 2426 C CD1 . TYR A 305 ? 0.6821 0.7001 0.6997 0.0736 0.0110 -0.0815 305 TYR A CD1 2427 C CD2 . TYR A 305 ? 0.7415 0.7722 0.6905 0.1372 -0.0042 -0.0798 305 TYR A CD2 2428 C CE1 . TYR A 305 ? 0.6494 0.7308 0.7037 0.0680 0.0163 -0.0987 305 TYR A CE1 2429 C CE2 . TYR A 305 ? 0.7081 0.8262 0.7044 0.1304 -0.0001 -0.0994 305 TYR A CE2 2430 C CZ . TYR A 305 ? 0.6619 0.7978 0.7078 0.0910 0.0115 -0.1087 305 TYR A CZ 2431 O OH . TYR A 305 ? 0.6368 0.8452 0.7156 0.0751 0.0193 -0.1300 305 TYR A OH 2432 N N . VAL A 306 ? 0.7734 0.7152 0.7236 0.1266 -0.0034 -0.0629 306 VAL A N 2433 C CA . VAL A 306 ? 0.7577 0.7527 0.7146 0.1539 -0.0077 -0.0728 306 VAL A CA 2434 C C . VAL A 306 ? 0.7089 0.7863 0.7229 0.1319 0.0003 -0.0914 306 VAL A C 2435 O O . VAL A 306 ? 0.6950 0.7679 0.7397 0.0993 0.0093 -0.0936 306 VAL A O 2436 C CB . VAL A 306 ? 0.7477 0.7182 0.7017 0.1587 -0.0092 -0.0678 306 VAL A CB 2437 C CG1 . VAL A 306 ? 0.8184 0.7004 0.7026 0.1786 -0.0152 -0.0523 306 VAL A CG1 2438 C CG2 . VAL A 306 ? 0.7129 0.6768 0.7122 0.1209 0.0000 -0.0668 306 VAL A CG2 2439 N N . LYS A 307 ? 0.7174 0.8702 0.7383 0.1493 -0.0019 -0.1066 307 LYS A N 2440 C CA . LYS A 307 ? 0.7157 0.9476 0.7800 0.1188 0.0090 -0.1285 307 LYS A CA 2441 C C . LYS A 307 ? 0.7008 0.9355 0.7906 0.0900 0.0192 -0.1340 307 LYS A C 2442 O O . LYS A 307 ? 0.7298 1.0216 0.8411 0.0596 0.0311 -0.1539 307 LYS A O 2443 C CB . LYS A 307 ? 0.7269 1.0623 0.7855 0.1444 0.0037 -0.1480 307 LYS A CB 2444 C CG . LYS A 307 ? 0.7449 1.1113 0.7971 0.1515 0.0018 -0.1537 307 LYS A CG 2445 C CD . LYS A 307 ? 0.7785 1.2720 0.8307 0.1750 -0.0023 -0.1780 307 LYS A CD 2446 C CE . LYS A 307 ? 0.8280 1.3451 0.8500 0.2127 -0.0117 -0.1772 307 LYS A CE 2447 N NZ . LYS A 307 ? 0.8534 1.5006 0.8636 0.2555 -0.0201 -0.1990 307 LYS A NZ 2448 N N . SER A 308 ? 0.6944 0.8661 0.7758 0.0956 0.0164 -0.1178 308 SER A N 2449 C CA . SER A 308 ? 0.6793 0.8506 0.7775 0.0738 0.0252 -0.1213 308 SER A CA 2450 C C . SER A 308 ? 0.6822 0.8240 0.7976 0.0330 0.0417 -0.1247 308 SER A C 2451 O O . SER A 308 ? 0.6824 0.7866 0.7988 0.0270 0.0436 -0.1183 308 SER A O 2452 C CB . SER A 308 ? 0.6697 0.7796 0.7529 0.0910 0.0180 -0.1028 308 SER A CB 2453 O OG . SER A 308 ? 0.6962 0.8017 0.7454 0.1319 0.0039 -0.0967 308 SER A OG 2454 N N . ASN A 309 ? 0.7189 0.8727 0.8391 0.0067 0.0543 -0.1350 309 ASN A N 2455 C CA . ASN A 309 ? 0.7724 0.8672 0.8879 -0.0237 0.0710 -0.1339 309 ASN A CA 2456 C C . ASN A 309 ? 0.7580 0.7886 0.8673 -0.0119 0.0689 -0.1147 309 ASN A C 2457 O O . ASN A 309 ? 0.7978 0.7702 0.8957 -0.0208 0.0791 -0.1090 309 ASN A O 2458 C CB . ASN A 309 ? 0.8372 0.9628 0.9436 -0.0660 0.0904 -0.1563 309 ASN A CB 2459 C CG . ASN A 309 ? 0.8967 1.0770 1.0058 -0.0888 0.0978 -0.1780 309 ASN A CG 2460 O OD1 . ASN A 309 ? 0.9069 1.0568 1.0159 -0.0875 0.0986 -0.1749 309 ASN A OD1 2461 N ND2 . ASN A 309 ? 0.9268 1.1991 1.0387 -0.1107 0.1034 -0.2024 309 ASN A ND2 2462 N N . ARG A 310 ? 0.7144 0.7560 0.8258 0.0125 0.0557 -0.1057 310 ARG A N 2463 C CA . ARG A 310 ? 0.7083 0.7055 0.8149 0.0204 0.0543 -0.0913 310 ARG A CA 2464 C C . ARG A 310 ? 0.6760 0.6775 0.7785 0.0501 0.0376 -0.0813 310 ARG A C 2465 O O . ARG A 310 ? 0.6680 0.7147 0.7668 0.0641 0.0310 -0.0890 310 ARG A O 2466 C CB . ARG A 310 ? 0.7521 0.7535 0.8514 -0.0036 0.0683 -0.1002 310 ARG A CB 2467 C CG . ARG A 310 ? 0.8037 0.7566 0.8940 0.0024 0.0701 -0.0861 310 ARG A CG 2468 C CD . ARG A 310 ? 0.8631 0.8123 0.9357 -0.0264 0.0867 -0.0954 310 ARG A CD 2469 N NE . ARG A 310 ? 0.9157 0.8440 0.9840 -0.0142 0.0834 -0.0833 310 ARG A NE 2470 C CZ . ARG A 310 ? 0.9535 0.8195 1.0063 -0.0033 0.0866 -0.0682 310 ARG A CZ 2471 N NH1 . ARG A 310 ? 0.9831 0.7996 1.0200 0.0012 0.0931 -0.0630 310 ARG A NH1 2472 N NH2 . ARG A 310 ? 0.9716 0.8306 1.0224 0.0073 0.0829 -0.0591 310 ARG A NH2 2473 N N . LEU A 311 ? 0.6568 0.6132 0.7533 0.0603 0.0317 -0.0662 311 LEU A N 2474 C CA . LEU A 311 ? 0.6697 0.6106 0.7497 0.0808 0.0199 -0.0573 311 LEU A CA 2475 C C . LEU A 311 ? 0.6589 0.5664 0.7402 0.0768 0.0215 -0.0466 311 LEU A C 2476 O O . LEU A 311 ? 0.6620 0.5502 0.7435 0.0712 0.0223 -0.0408 311 LEU A O 2477 C CB . LEU A 311 ? 0.6805 0.6006 0.7354 0.0938 0.0107 -0.0524 311 LEU A CB 2478 C CG . LEU A 311 ? 0.6990 0.6509 0.7419 0.1097 0.0061 -0.0611 311 LEU A CG 2479 C CD1 . LEU A 311 ? 0.7381 0.6483 0.7450 0.1184 0.0001 -0.0533 311 LEU A CD1 2480 C CD2 . LEU A 311 ? 0.7236 0.7088 0.7520 0.1372 -0.0007 -0.0676 311 LEU A CD2 2481 N N . VAL A 312 ? 0.6412 0.5528 0.7232 0.0806 0.0219 -0.0459 312 VAL A N 2482 C CA . VAL A 312 ? 0.6379 0.5266 0.7209 0.0794 0.0236 -0.0367 312 VAL A CA 2483 C C . VAL A 312 ? 0.6328 0.5178 0.7030 0.0922 0.0155 -0.0337 312 VAL A C 2484 O O . VAL A 312 ? 0.6161 0.5255 0.6869 0.0987 0.0149 -0.0398 312 VAL A O 2485 C CB . VAL A 312 ? 0.6394 0.5248 0.7290 0.0688 0.0365 -0.0381 312 VAL A CB 2486 C CG1 . VAL A 312 ? 0.6533 0.5190 0.7390 0.0759 0.0371 -0.0281 312 VAL A CG1 2487 C CG2 . VAL A 312 ? 0.6436 0.5185 0.7335 0.0584 0.0461 -0.0422 312 VAL A CG2 2488 N N . LEU A 313 ? 0.6484 0.5079 0.7037 0.0934 0.0103 -0.0267 313 LEU A N 2489 C CA . LEU A 313 ? 0.6724 0.5155 0.7064 0.1032 0.0040 -0.0242 313 LEU A CA 2490 C C . LEU A 313 ? 0.6721 0.5238 0.7217 0.0998 0.0077 -0.0201 313 LEU A C 2491 O O . LEU A 313 ? 0.6878 0.5449 0.7506 0.0922 0.0128 -0.0166 313 LEU A O 2492 C CB . LEU A 313 ? 0.6942 0.4973 0.6918 0.0966 0.0000 -0.0212 313 LEU A CB 2493 C CG . LEU A 313 ? 0.7496 0.5177 0.7046 0.1067 -0.0047 -0.0226 313 LEU A CG 2494 C CD1 . LEU A 313 ? 0.7884 0.5074 0.6995 0.0851 -0.0030 -0.0202 313 LEU A CD1 2495 C CD2 . LEU A 313 ? 0.7835 0.5386 0.7078 0.1379 -0.0114 -0.0250 313 LEU A CD2 2496 N N . ALA A 314 ? 0.6597 0.5154 0.7035 0.1102 0.0047 -0.0210 314 ALA A N 2497 C CA . ALA A 314 ? 0.6412 0.5012 0.6928 0.1088 0.0069 -0.0164 314 ALA A CA 2498 C C . ALA A 314 ? 0.6481 0.4882 0.6800 0.1037 0.0026 -0.0138 314 ALA A C 2499 O O . ALA A 314 ? 0.6560 0.4653 0.6544 0.1056 -0.0026 -0.0162 314 ALA A O 2500 C CB . ALA A 314 ? 0.6487 0.5261 0.7003 0.1192 0.0056 -0.0202 314 ALA A CB 2501 N N . THR A 315 ? 0.6402 0.4963 0.6843 0.0972 0.0059 -0.0101 315 THR A N 2502 C CA . THR A 315 ? 0.6643 0.5208 0.6922 0.0860 0.0037 -0.0113 315 THR A CA 2503 C C . THR A 315 ? 0.6541 0.5267 0.6898 0.0945 0.0037 -0.0085 315 THR A C 2504 O O . THR A 315 ? 0.6826 0.5421 0.6982 0.0909 0.0004 -0.0112 315 THR A O 2505 C CB . THR A 315 ? 0.6648 0.5519 0.7003 0.0731 0.0067 -0.0133 315 THR A CB 2506 O OG1 . THR A 315 ? 0.6563 0.5652 0.7165 0.0891 0.0112 -0.0088 315 THR A OG1 2507 C CG2 . THR A 315 ? 0.6879 0.5550 0.7028 0.0546 0.0066 -0.0181 315 THR A CG2 2508 N N . GLY A 316 ? 0.6319 0.5243 0.6885 0.1061 0.0086 -0.0029 316 GLY A N 2509 C CA . GLY A 316 ? 0.6250 0.5290 0.6849 0.1159 0.0098 0.0014 316 GLY A CA 2510 C C . GLY A 316 ? 0.6322 0.5240 0.6910 0.1203 0.0095 0.0007 316 GLY A C 2511 O O . GLY A 316 ? 0.6236 0.5043 0.6759 0.1199 0.0059 -0.0050 316 GLY A O 2512 N N . LEU A 317 ? 0.6312 0.5308 0.6925 0.1269 0.0137 0.0056 317 LEU A N 2513 C CA . LEU A 317 ? 0.6461 0.5499 0.7066 0.1278 0.0139 0.0026 317 LEU A CA 2514 C C . LEU A 317 ? 0.6434 0.5418 0.7023 0.1213 0.0261 0.0050 317 LEU A C 2515 O O . LEU A 317 ? 0.6424 0.5196 0.6936 0.1210 0.0343 0.0108 317 LEU A O 2516 C CB . LEU A 317 ? 0.6650 0.5801 0.7213 0.1336 0.0095 0.0036 317 LEU A CB 2517 C CG . LEU A 317 ? 0.6752 0.6008 0.7314 0.1394 0.0127 0.0119 317 LEU A CG 2518 C CD1 . LEU A 317 ? 0.7071 0.6215 0.7558 0.1434 0.0236 0.0200 317 LEU A CD1 2519 C CD2 . LEU A 317 ? 0.6731 0.6153 0.7254 0.1408 0.0063 0.0090 317 LEU A CD2 2520 N N . ARG A 318 ? 0.6380 0.5543 0.6965 0.1150 0.0284 -0.0014 318 ARG A N 2521 C CA . ARG A 318 ? 0.6712 0.5834 0.7188 0.0960 0.0431 -0.0037 318 ARG A CA 2522 C C . ARG A 318 ? 0.7040 0.5776 0.7271 0.0964 0.0545 0.0091 318 ARG A C 2523 O O . ARG A 318 ? 0.6902 0.5701 0.7102 0.1056 0.0520 0.0148 318 ARG A O 2524 C CB . ARG A 318 ? 0.6807 0.6399 0.7325 0.0874 0.0427 -0.0163 318 ARG A CB 2525 C CG . ARG A 318 ? 0.7303 0.6974 0.7662 0.0547 0.0606 -0.0244 318 ARG A CG 2526 C CD . ARG A 318 ? 0.7468 0.7826 0.7892 0.0462 0.0596 -0.0399 318 ARG A CD 2527 N NE . ARG A 318 ? 0.7418 0.8390 0.8021 0.0579 0.0490 -0.0564 318 ARG A NE 2528 C CZ . ARG A 318 ? 0.7599 0.9033 0.8207 0.0347 0.0572 -0.0733 318 ARG A CZ 2529 N NH1 . ARG A 318 ? 0.7847 0.9103 0.8248 -0.0100 0.0785 -0.0771 318 ARG A NH1 2530 N NH2 . ARG A 318 ? 0.7673 0.9724 0.8413 0.0569 0.0449 -0.0876 318 ARG A NH2 2531 N N . ASN A 319 ? 0.7715 0.6006 0.7701 0.0896 0.0674 0.0135 319 ASN A N 2532 C CA . ASN A 319 ? 0.8504 0.6254 0.8085 0.1013 0.0788 0.0273 319 ASN A CA 2533 C C . ASN A 319 ? 0.9733 0.7127 0.8888 0.0759 0.0974 0.0275 319 ASN A C 2534 O O . ASN A 319 ? 1.0294 0.7663 0.9335 0.0407 0.1094 0.0156 319 ASN A O 2535 C CB . ASN A 319 ? 0.8608 0.5917 0.7975 0.1124 0.0848 0.0317 319 ASN A CB 2536 C CG . ASN A 319 ? 0.8926 0.5785 0.7868 0.1461 0.0902 0.0466 319 ASN A CG 2537 O OD1 . ASN A 319 ? 0.8803 0.5780 0.7695 0.1628 0.0866 0.0542 319 ASN A OD1 2538 N ND2 . ASN A 319 ? 0.9351 0.5714 0.7944 0.1613 0.0985 0.0504 319 ASN A ND2 2539 N N . SER A 320 ? 1.1123 0.8269 0.9998 0.0914 0.1010 0.0397 320 SER A N 2540 C CA . SER A 320 ? 1.2399 0.9204 1.0816 0.0655 0.1186 0.0409 320 SER A CA 2541 C C . SER A 320 ? 1.3644 0.9413 1.1259 0.0512 0.1436 0.0468 320 SER A C 2542 O O . SER A 320 ? 1.3652 0.8878 1.0964 0.0849 0.1448 0.0581 320 SER A O 2543 C CB . SER A 320 ? 1.2377 0.9245 1.0729 0.0913 0.1130 0.0532 320 SER A CB 2544 O OG . SER A 320 ? 1.1498 0.9163 1.0481 0.1077 0.0909 0.0481 320 SER A OG 2545 N N . PRO A 321 ? 1.5027 1.0523 1.2226 0.0000 0.1648 0.0371 321 PRO A N 2546 C CA . PRO A 321 ? 1.6540 1.0822 1.2744 -0.0226 0.1939 0.0421 321 PRO A CA 2547 C C . PRO A 321 ? 1.7129 1.0590 1.2565 -0.0063 0.2067 0.0607 321 PRO A C 2548 O O . PRO A 321 ? 1.7385 1.0177 1.2387 0.0466 0.2055 0.0793 321 PRO A O 2549 C CB . PRO A 321 ? 1.6789 1.1343 1.2916 -0.0952 0.2114 0.0185 321 PRO A CB 2550 C CG . PRO A 321 ? 1.5976 1.1765 1.2835 -0.1027 0.1948 0.0072 321 PRO A CG 2551 C CD . PRO A 321 ? 1.5032 1.1395 1.2621 -0.0421 0.1637 0.0173 321 PRO A CD 2552 N N . GLY B 1 ? 0.4938 0.5781 0.7683 -0.0359 -0.0828 0.1178 1 GLY B N 2553 C CA . GLY B 1 ? 0.4750 0.5438 0.7408 -0.0153 -0.0728 0.0945 1 GLY B CA 2554 C C . GLY B 1 ? 0.4583 0.5738 0.7344 0.0039 -0.0603 0.0957 1 GLY B C 2555 O O . GLY B 1 ? 0.4611 0.6259 0.7512 0.0076 -0.0549 0.1113 1 GLY B O 2556 N N . LEU B 2 ? 0.4497 0.5477 0.7139 0.0185 -0.0559 0.0794 2 LEU B N 2557 C CA . LEU B 2 ? 0.4370 0.5672 0.7000 0.0417 -0.0471 0.0787 2 LEU B CA 2558 C C . LEU B 2 ? 0.4380 0.5847 0.6935 0.0606 -0.0351 0.0747 2 LEU B C 2559 O O . LEU B 2 ? 0.4428 0.6311 0.6992 0.0812 -0.0288 0.0818 2 LEU B O 2560 C CB . LEU B 2 ? 0.4411 0.5328 0.6821 0.0528 -0.0467 0.0605 2 LEU B CB 2561 C CG . LEU B 2 ? 0.4416 0.5244 0.6855 0.0437 -0.0573 0.0640 2 LEU B CG 2562 C CD1 . LEU B 2 ? 0.4530 0.4929 0.6687 0.0567 -0.0549 0.0456 2 LEU B CD1 2563 C CD2 . LEU B 2 ? 0.4392 0.5828 0.7053 0.0467 -0.0615 0.0845 2 LEU B CD2 2564 N N . PHE B 3 ? 0.4346 0.5515 0.6807 0.0563 -0.0328 0.0636 3 PHE B N 2565 C CA . PHE B 3 ? 0.4460 0.5675 0.6785 0.0742 -0.0239 0.0555 3 PHE B CA 2566 C C . PHE B 3 ? 0.4512 0.6051 0.6965 0.0713 -0.0211 0.0698 3 PHE B C 2567 O O . PHE B 3 ? 0.4620 0.6230 0.6956 0.0871 -0.0145 0.0647 3 PHE B O 2568 C CB . PHE B 3 ? 0.4509 0.5236 0.6623 0.0728 -0.0236 0.0332 3 PHE B CB 2569 C CG . PHE B 3 ? 0.4654 0.5063 0.6569 0.0777 -0.0251 0.0208 3 PHE B CG 2570 C CD1 . PHE B 3 ? 0.4674 0.4870 0.6626 0.0635 -0.0305 0.0195 3 PHE B CD1 2571 C CD2 . PHE B 3 ? 0.4760 0.5046 0.6396 0.0985 -0.0227 0.0117 3 PHE B CD2 2572 C CE1 . PHE B 3 ? 0.4794 0.4692 0.6540 0.0680 -0.0319 0.0101 3 PHE B CE1 2573 C CE2 . PHE B 3 ? 0.5098 0.5020 0.6488 0.1028 -0.0259 0.0018 3 PHE B CE2 2574 C CZ . PHE B 3 ? 0.5006 0.4754 0.6468 0.0867 -0.0298 0.0017 3 PHE B CZ 2575 N N . GLY B 4 ? 0.4528 0.6218 0.7176 0.0500 -0.0281 0.0883 4 GLY B N 2576 C CA . GLY B 4 ? 0.4468 0.6509 0.7231 0.0435 -0.0268 0.1084 4 GLY B CA 2577 C C . GLY B 4 ? 0.4548 0.6317 0.7215 0.0384 -0.0280 0.1031 4 GLY B C 2578 O O . GLY B 4 ? 0.4966 0.6942 0.7689 0.0299 -0.0290 0.1212 4 GLY B O 2579 N N . ALA B 5 ? 0.4461 0.5809 0.6978 0.0434 -0.0283 0.0803 5 ALA B N 2580 C CA . ALA B 5 ? 0.4453 0.5631 0.6878 0.0441 -0.0290 0.0743 5 ALA B CA 2581 C C . ALA B 5 ? 0.4558 0.5427 0.6951 0.0268 -0.0410 0.0798 5 ALA B C 2582 O O . ALA B 5 ? 0.4627 0.5519 0.6997 0.0191 -0.0458 0.0951 5 ALA B O 2583 C CB . ALA B 5 ? 0.4475 0.5442 0.6764 0.0560 -0.0250 0.0498 5 ALA B CB 2584 N N . ILE B 6 ? 0.4705 0.5243 0.7039 0.0222 -0.0468 0.0677 6 ILE B N 2585 C CA . ILE B 6 ? 0.5019 0.5163 0.7218 0.0125 -0.0598 0.0690 6 ILE B CA 2586 C C . ILE B 6 ? 0.5218 0.5324 0.7435 -0.0087 -0.0728 0.0927 6 ILE B C 2587 O O . ILE B 6 ? 0.5000 0.5287 0.7355 -0.0188 -0.0747 0.1020 6 ILE B O 2588 C CB . ILE B 6 ? 0.5121 0.4967 0.7229 0.0155 -0.0620 0.0514 6 ILE B CB 2589 C CG1 . ILE B 6 ? 0.5100 0.4985 0.7164 0.0304 -0.0528 0.0319 6 ILE B CG1 2590 C CG2 . ILE B 6 ? 0.5467 0.4869 0.7370 0.0086 -0.0780 0.0545 6 ILE B CG2 2591 C CD1 . ILE B 6 ? 0.5162 0.4897 0.7168 0.0325 -0.0509 0.0168 6 ILE B CD1 2592 N N . ALA B 7 ? 0.5522 0.5389 0.7576 -0.0163 -0.0835 0.1033 7 ALA B N 2593 C CA . ALA B 7 ? 0.5861 0.5652 0.7883 -0.0428 -0.0989 0.1294 7 ALA B CA 2594 C C . ALA B 7 ? 0.5705 0.6152 0.8031 -0.0528 -0.0904 0.1501 7 ALA B C 2595 O O . ALA B 7 ? 0.5917 0.6492 0.8347 -0.0755 -0.1006 0.1685 7 ALA B O 2596 C CB . ALA B 7 ? 0.6071 0.5396 0.7939 -0.0564 -0.1169 0.1279 7 ALA B CB 2597 N N . GLY B 8 ? 0.5591 0.6474 0.8039 -0.0340 -0.0726 0.1470 8 GLY B N 2598 C CA . GLY B 8 ? 0.5462 0.7029 0.8151 -0.0332 -0.0616 0.1647 8 GLY B CA 2599 C C . GLY B 8 ? 0.5557 0.7395 0.8217 -0.0238 -0.0520 0.1739 8 GLY B C 2600 O O . GLY B 8 ? 0.5958 0.7744 0.8547 -0.0430 -0.0604 0.1950 8 GLY B O 2601 N N . PHE B 9 ? 0.5324 0.7391 0.7985 0.0048 -0.0362 0.1588 9 PHE B N 2602 C CA . PHE B 9 ? 0.5492 0.7771 0.8078 0.0169 -0.0277 0.1651 9 PHE B CA 2603 C C . PHE B 9 ? 0.5824 0.7575 0.8188 0.0206 -0.0340 0.1493 9 PHE B C 2604 O O . PHE B 9 ? 0.6137 0.7910 0.8387 0.0230 -0.0332 0.1584 9 PHE B O 2605 C CB . PHE B 9 ? 0.5374 0.8083 0.7976 0.0475 -0.0113 0.1570 9 PHE B CB 2606 C CG . PHE B 9 ? 0.5278 0.7651 0.7736 0.0686 -0.0084 0.1244 9 PHE B CG 2607 C CD1 . PHE B 9 ? 0.5374 0.7500 0.7662 0.0796 -0.0081 0.1086 9 PHE B CD1 2608 C CD2 . PHE B 9 ? 0.5151 0.7478 0.7627 0.0762 -0.0070 0.1112 9 PHE B CD2 2609 C CE1 . PHE B 9 ? 0.5355 0.7216 0.7519 0.0928 -0.0076 0.0815 9 PHE B CE1 2610 C CE2 . PHE B 9 ? 0.5208 0.7199 0.7517 0.0900 -0.0062 0.0843 9 PHE B CE2 2611 C CZ . PHE B 9 ? 0.5254 0.7029 0.7419 0.0960 -0.0069 0.0701 9 PHE B CZ 2612 N N . ILE B 10 ? 0.5851 0.7167 0.8143 0.0226 -0.0402 0.1270 10 ILE B N 2613 C CA . ILE B 10 ? 0.6162 0.7013 0.8246 0.0253 -0.0490 0.1153 10 ILE B CA 2614 C C . ILE B 10 ? 0.6748 0.7182 0.8718 0.0034 -0.0663 0.1265 10 ILE B C 2615 O O . ILE B 10 ? 0.6987 0.7244 0.8988 -0.0029 -0.0716 0.1193 10 ILE B O 2616 C CB . ILE B 10 ? 0.5898 0.6605 0.7950 0.0423 -0.0450 0.0858 10 ILE B CB 2617 C CG1 . ILE B 10 ? 0.5690 0.6727 0.7799 0.0594 -0.0320 0.0756 10 ILE B CG1 2618 C CG2 . ILE B 10 ? 0.6007 0.6397 0.7860 0.0509 -0.0524 0.0754 10 ILE B CG2 2619 C CD1 . ILE B 10 ? 0.5646 0.6569 0.7721 0.0689 -0.0300 0.0499 10 ILE B CD1 2620 N N . GLU B 11 ? 0.7425 0.7649 0.9211 -0.0082 -0.0769 0.1445 11 GLU B N 2621 C CA . GLU B 11 ? 0.8047 0.7857 0.9669 -0.0353 -0.0970 0.1623 11 GLU B CA 2622 C C . GLU B 11 ? 0.8036 0.7181 0.9371 -0.0290 -0.1117 0.1441 11 GLU B C 2623 O O . GLU B 11 ? 0.8278 0.7073 0.9499 -0.0481 -0.1279 0.1513 11 GLU B O 2624 C CB . GLU B 11 ? 0.8985 0.8666 1.0402 -0.0512 -0.1063 0.1880 11 GLU B CB 2625 C CG . GLU B 11 ? 0.9380 0.9717 1.1058 -0.0704 -0.0977 0.2179 11 GLU B CG 2626 C CD . GLU B 11 ? 1.0517 1.0610 1.1971 -0.1040 -0.1152 0.2512 11 GLU B CD 2627 O OE1 . GLU B 11 ? 1.1144 1.0713 1.2224 -0.0988 -0.1246 0.2505 11 GLU B OE1 2628 O OE2 . GLU B 11 ? 1.0980 1.1405 1.2615 -0.1365 -0.1208 0.2787 11 GLU B OE2 2629 N N . GLY B 12 ? 0.7854 0.6848 0.9051 -0.0013 -0.1072 0.1214 12 GLY B N 2630 C CA . GLY B 12 ? 0.8022 0.6480 0.8927 0.0124 -0.1187 0.1035 12 GLY B CA 2631 C C . GLY B 12 ? 0.7636 0.6282 0.8582 0.0431 -0.1063 0.0776 12 GLY B C 2632 O O . GLY B 12 ? 0.7428 0.6497 0.8554 0.0528 -0.0927 0.0735 12 GLY B O 2633 N N . GLY B 13 ? 0.7642 0.5995 0.8405 0.0581 -0.1120 0.0610 13 GLY B N 2634 C CA . GLY B 13 ? 0.7402 0.5988 0.8195 0.0853 -0.1021 0.0389 13 GLY B CA 2635 C C . GLY B 13 ? 0.7677 0.6072 0.8159 0.1091 -0.1095 0.0352 13 GLY B C 2636 O O . GLY B 13 ? 0.8003 0.5979 0.8189 0.1045 -0.1233 0.0496 13 GLY B O 2637 N N . TRP B 14 ? 0.7448 0.6166 0.7987 0.1338 -0.1012 0.0170 14 TRP B N 2638 C CA . TRP B 14 ? 0.7532 0.6231 0.7833 0.1617 -0.1060 0.0109 14 TRP B CA 2639 C C . TRP B 14 ? 0.8050 0.6590 0.8059 0.1930 -0.1123 -0.0040 14 TRP B C 2640 O O . TRP B 14 ? 0.7553 0.6544 0.7778 0.2017 -0.1012 -0.0173 14 TRP B O 2641 C CB . TRP B 14 ? 0.6937 0.6292 0.7570 0.1661 -0.0916 0.0030 14 TRP B CB 2642 C CG . TRP B 14 ? 0.6677 0.6178 0.7486 0.1468 -0.0861 0.0161 14 TRP B CG 2643 C CD1 . TRP B 14 ? 0.6887 0.6061 0.7539 0.1331 -0.0934 0.0359 14 TRP B CD1 2644 C CD2 . TRP B 14 ? 0.6139 0.6158 0.7266 0.1407 -0.0730 0.0111 14 TRP B CD2 2645 N NE1 . TRP B 14 ? 0.6597 0.6132 0.7477 0.1224 -0.0830 0.0437 14 TRP B NE1 2646 C CE2 . TRP B 14 ? 0.6192 0.6192 0.7330 0.1288 -0.0714 0.0273 14 TRP B CE2 2647 C CE3 . TRP B 14 ? 0.5735 0.6207 0.7097 0.1431 -0.0642 -0.0045 14 TRP B CE3 2648 C CZ2 . TRP B 14 ? 0.5885 0.6267 0.7223 0.1253 -0.0610 0.0260 14 TRP B CZ2 2649 C CZ3 . TRP B 14 ? 0.5522 0.6292 0.7059 0.1350 -0.0568 -0.0056 14 TRP B CZ3 2650 C CH2 . TRP B 14 ? 0.5578 0.6283 0.7082 0.1292 -0.0551 0.0084 14 TRP B CH2 2651 N N . GLN B 15 ? 0.9091 0.6982 0.8566 0.2112 -0.1308 -0.0006 15 GLN B N 2652 C CA . GLN B 15 ? 0.9739 0.7456 0.8825 0.2521 -0.1383 -0.0152 15 GLN B CA 2653 C C . GLN B 15 ? 0.9389 0.7837 0.8677 0.2803 -0.1264 -0.0283 15 GLN B C 2654 O O . GLN B 15 ? 0.9412 0.8217 0.8698 0.3073 -0.1211 -0.0418 15 GLN B O 2655 C CB . GLN B 15 ? 1.0720 0.7498 0.9084 0.2695 -0.1638 -0.0089 15 GLN B CB 2656 C CG . GLN B 15 ? 1.1300 0.7271 0.9358 0.2419 -0.1819 0.0042 15 GLN B CG 2657 C CD . GLN B 15 ? 1.1706 0.7404 0.9531 0.2570 -0.1873 -0.0076 15 GLN B CD 2658 O OE1 . GLN B 15 ? 1.1790 0.7418 0.9802 0.2272 -0.1868 -0.0022 15 GLN B OE1 2659 N NE2 . GLN B 15 ? 1.2230 0.7796 0.9625 0.3062 -0.1925 -0.0236 15 GLN B NE2 2660 N N . GLY B 16 ? 0.9177 0.7890 0.8641 0.2733 -0.1226 -0.0231 16 GLY B N 2661 C CA . GLY B 16 ? 0.9034 0.8423 0.8672 0.2972 -0.1150 -0.0339 16 GLY B CA 2662 C C . GLY B 16 ? 0.8478 0.8733 0.8666 0.2853 -0.0972 -0.0432 16 GLY B C 2663 O O . GLY B 16 ? 0.8549 0.9419 0.8861 0.3063 -0.0931 -0.0529 16 GLY B O 2664 N N . MET B 17 ? 0.8065 0.8378 0.8563 0.2508 -0.0881 -0.0395 17 MET B N 2665 C CA . MET B 17 ? 0.7686 0.8696 0.8625 0.2355 -0.0739 -0.0470 17 MET B CA 2666 C C . MET B 17 ? 0.7722 0.8857 0.8646 0.2439 -0.0695 -0.0536 17 MET B C 2667 O O . MET B 17 ? 0.7702 0.8502 0.8614 0.2270 -0.0684 -0.0502 17 MET B O 2668 C CB . MET B 17 ? 0.7417 0.8425 0.8648 0.1976 -0.0667 -0.0404 17 MET B CB 2669 C CG . MET B 17 ? 0.7089 0.8701 0.8678 0.1803 -0.0560 -0.0477 17 MET B CG 2670 S SD . MET B 17 ? 0.6864 0.8400 0.8661 0.1460 -0.0506 -0.0423 17 MET B SD 2671 C CE . MET B 17 ? 0.7119 0.8091 0.8812 0.1344 -0.0512 -0.0330 17 MET B CE 2672 N N . VAL B 18 ? 0.7915 0.9604 0.8851 0.2709 -0.0667 -0.0623 18 VAL B N 2673 C CA . VAL B 18 ? 0.8077 0.9911 0.8894 0.2914 -0.0632 -0.0680 18 VAL B CA 2674 C C . VAL B 18 ? 0.7620 1.0202 0.8858 0.2693 -0.0483 -0.0698 18 VAL B C 2675 O O . VAL B 18 ? 0.7766 1.0362 0.8962 0.2707 -0.0426 -0.0708 18 VAL B O 2676 C CB . VAL B 18 ? 0.8589 1.0599 0.9075 0.3433 -0.0698 -0.0750 18 VAL B CB 2677 C CG1 . VAL B 18 ? 0.9073 1.1259 0.9379 0.3714 -0.0655 -0.0808 18 VAL B CG1 2678 C CG2 . VAL B 18 ? 0.9174 1.0312 0.9144 0.3638 -0.0875 -0.0722 18 VAL B CG2 2679 N N . ASP B 19 ? 0.7255 1.0404 0.8856 0.2470 -0.0435 -0.0693 19 ASP B N 2680 C CA . ASP B 19 ? 0.6928 1.0831 0.8885 0.2246 -0.0327 -0.0694 19 ASP B CA 2681 C C . ASP B 19 ? 0.6365 1.0057 0.8529 0.1776 -0.0283 -0.0652 19 ASP B C 2682 O O . ASP B 19 ? 0.6235 1.0425 0.8665 0.1497 -0.0242 -0.0641 19 ASP B O 2683 C CB . ASP B 19 ? 0.6975 1.1710 0.9154 0.2306 -0.0337 -0.0716 19 ASP B CB 2684 C CG . ASP B 19 ? 0.7096 1.1628 0.9306 0.2207 -0.0421 -0.0718 19 ASP B CG 2685 O OD1 . ASP B 19 ? 0.7122 1.0933 0.9204 0.2083 -0.0454 -0.0689 19 ASP B OD1 2686 O OD2 . ASP B 19 ? 0.7346 1.2496 0.9707 0.2261 -0.0455 -0.0740 19 ASP B OD2 2687 N N . GLY B 20 ? 0.6138 0.9086 0.8147 0.1690 -0.0309 -0.0623 20 GLY B N 2688 C CA . GLY B 20 ? 0.5915 0.8638 0.8060 0.1321 -0.0271 -0.0589 20 GLY B CA 2689 C C . GLY B 20 ? 0.6026 0.8014 0.7994 0.1296 -0.0308 -0.0545 20 GLY B C 2690 O O . GLY B 20 ? 0.6364 0.7971 0.8106 0.1502 -0.0384 -0.0526 20 GLY B O 2691 N N . TRP B 21 ? 0.5837 0.7622 0.7883 0.1034 -0.0271 -0.0518 21 TRP B N 2692 C CA . TRP B 21 ? 0.5863 0.7063 0.7790 0.0983 -0.0307 -0.0461 21 TRP B CA 2693 C C . TRP B 21 ? 0.5430 0.6454 0.7397 0.0896 -0.0340 -0.0407 21 TRP B C 2694 O O . TRP B 21 ? 0.5353 0.6009 0.7216 0.0920 -0.0395 -0.0330 21 TRP B O 2695 C CB . TRP B 21 ? 0.6057 0.7132 0.8014 0.0796 -0.0255 -0.0455 21 TRP B CB 2696 C CG . TRP B 21 ? 0.6474 0.7379 0.8267 0.0922 -0.0257 -0.0464 21 TRP B CG 2697 C CD1 . TRP B 21 ? 0.6859 0.7411 0.8408 0.1139 -0.0344 -0.0456 21 TRP B CD1 2698 C CD2 . TRP B 21 ? 0.6764 0.7770 0.8559 0.0838 -0.0186 -0.0480 21 TRP B CD2 2699 N NE1 . TRP B 21 ? 0.7015 0.7443 0.8404 0.1223 -0.0334 -0.0481 21 TRP B NE1 2700 C CE2 . TRP B 21 ? 0.7013 0.7755 0.8570 0.1043 -0.0223 -0.0492 21 TRP B CE2 2701 C CE3 . TRP B 21 ? 0.7044 0.8283 0.8965 0.0600 -0.0109 -0.0479 21 TRP B CE3 2702 C CZ2 . TRP B 21 ? 0.7493 0.8266 0.8967 0.1044 -0.0164 -0.0504 21 TRP B CZ2 2703 C CZ3 . TRP B 21 ? 0.7505 0.8770 0.9352 0.0567 -0.0049 -0.0476 21 TRP B CZ3 2704 C CH2 . TRP B 21 ? 0.7627 0.8693 0.9268 0.0799 -0.0066 -0.0489 21 TRP B CH2 2705 N N . TYR B 22 ? 0.5068 0.6365 0.7163 0.0786 -0.0314 -0.0438 22 TYR B N 2706 C CA . TYR B 22 ? 0.4890 0.6080 0.6988 0.0750 -0.0335 -0.0399 22 TYR B CA 2707 C C . TYR B 22 ? 0.4808 0.6341 0.6949 0.0803 -0.0357 -0.0452 22 TYR B C 2708 O O . TYR B 22 ? 0.4661 0.6566 0.6888 0.0760 -0.0352 -0.0518 22 TYR B O 2709 C CB . TYR B 22 ? 0.4838 0.5890 0.6953 0.0569 -0.0305 -0.0398 22 TYR B CB 2710 C CG . TYR B 22 ? 0.4803 0.5665 0.6902 0.0472 -0.0276 -0.0391 22 TYR B CG 2711 C CD1 . TYR B 22 ? 0.4811 0.5396 0.6866 0.0514 -0.0292 -0.0318 22 TYR B CD1 2712 C CD2 . TYR B 22 ? 0.4835 0.5775 0.6938 0.0314 -0.0248 -0.0447 22 TYR B CD2 2713 C CE1 . TYR B 22 ? 0.4824 0.5229 0.6846 0.0439 -0.0277 -0.0317 22 TYR B CE1 2714 C CE2 . TYR B 22 ? 0.4824 0.5568 0.6880 0.0236 -0.0221 -0.0436 22 TYR B CE2 2715 C CZ . TYR B 22 ? 0.4804 0.5287 0.6824 0.0318 -0.0233 -0.0379 22 TYR B CZ 2716 O OH . TYR B 22 ? 0.4854 0.5135 0.6811 0.0255 -0.0218 -0.0372 22 TYR B OH 2717 N N . GLY B 23 ? 0.4831 0.6282 0.6915 0.0883 -0.0387 -0.0410 23 GLY B N 2718 C CA . GLY B 23 ? 0.4868 0.6610 0.6965 0.0943 -0.0424 -0.0463 23 GLY B CA 2719 C C . GLY B 23 ? 0.5000 0.6599 0.6992 0.1047 -0.0446 -0.0397 23 GLY B C 2720 O O . GLY B 23 ? 0.4981 0.6319 0.6925 0.1019 -0.0419 -0.0301 23 GLY B O 2721 N N . TYR B 24 ? 0.5182 0.7010 0.7143 0.1170 -0.0494 -0.0436 24 TYR B N 2722 C CA . TYR B 24 ? 0.5369 0.7119 0.7209 0.1274 -0.0515 -0.0382 24 TYR B CA 2723 C C . TYR B 24 ? 0.5440 0.7166 0.7157 0.1486 -0.0564 -0.0338 24 TYR B C 2724 O O . TYR B 24 ? 0.5512 0.7413 0.7237 0.1600 -0.0599 -0.0400 24 TYR B O 2725 C CB . TYR B 24 ? 0.5571 0.7551 0.7405 0.1239 -0.0559 -0.0479 24 TYR B CB 2726 C CG . TYR B 24 ? 0.5710 0.7662 0.7577 0.1027 -0.0558 -0.0549 24 TYR B CG 2727 C CD1 . TYR B 24 ? 0.5729 0.7914 0.7726 0.0868 -0.0580 -0.0622 24 TYR B CD1 2728 C CD2 . TYR B 24 ? 0.5950 0.7640 0.7674 0.0997 -0.0543 -0.0535 24 TYR B CD2 2729 C CE1 . TYR B 24 ? 0.5883 0.7958 0.7845 0.0641 -0.0602 -0.0670 24 TYR B CE1 2730 C CE2 . TYR B 24 ? 0.6205 0.7750 0.7858 0.0827 -0.0570 -0.0606 24 TYR B CE2 2731 C CZ . TYR B 24 ? 0.6217 0.7914 0.7978 0.0627 -0.0607 -0.0670 24 TYR B CZ 2732 O OH . TYR B 24 ? 0.6791 0.8264 0.8420 0.0425 -0.0655 -0.0725 24 TYR B OH 2733 N N . HIS B 25 ? 0.5557 0.7076 0.7125 0.1556 -0.0569 -0.0223 25 HIS B N 2734 C CA . HIS B 25 ? 0.5786 0.7230 0.7157 0.1761 -0.0637 -0.0180 25 HIS B CA 2735 C C . HIS B 25 ? 0.5880 0.7409 0.7159 0.1826 -0.0640 -0.0152 25 HIS B C 2736 O O . HIS B 25 ? 0.5936 0.7376 0.7200 0.1743 -0.0581 -0.0054 25 HIS B O 2737 C CB . HIS B 25 ? 0.5949 0.6944 0.7129 0.1768 -0.0668 -0.0024 25 HIS B CB 2738 C CG . HIS B 25 ? 0.6321 0.7109 0.7203 0.1976 -0.0761 0.0030 25 HIS B CG 2739 N ND1 . HIS B 25 ? 0.6498 0.7139 0.7210 0.1985 -0.0769 0.0175 25 HIS B ND1 2740 C CD2 . HIS B 25 ? 0.6535 0.7235 0.7215 0.2211 -0.0852 -0.0039 25 HIS B CD2 2741 C CE1 . HIS B 25 ? 0.6773 0.7178 0.7175 0.2190 -0.0873 0.0195 25 HIS B CE1 2742 N NE2 . HIS B 25 ? 0.6892 0.7318 0.7257 0.2351 -0.0929 0.0058 25 HIS B NE2 2743 N N . HIS B 26 ? 0.6151 0.7885 0.7352 0.2000 -0.0709 -0.0232 26 HIS B N 2744 C CA . HIS B 26 ? 0.6326 0.8133 0.7400 0.2088 -0.0726 -0.0218 26 HIS B CA 2745 C C . HIS B 26 ? 0.6553 0.8175 0.7354 0.2300 -0.0786 -0.0126 26 HIS B C 2746 O O . HIS B 26 ? 0.6519 0.8015 0.7212 0.2427 -0.0847 -0.0129 26 HIS B O 2747 C CB . HIS B 26 ? 0.6284 0.8482 0.7464 0.2083 -0.0783 -0.0391 26 HIS B CB 2748 C CG . HIS B 26 ? 0.6431 0.8936 0.7622 0.2254 -0.0875 -0.0481 26 HIS B CG 2749 N ND1 . HIS B 26 ? 0.6501 0.9285 0.7874 0.2235 -0.0886 -0.0557 26 HIS B ND1 2750 C CD2 . HIS B 26 ? 0.6690 0.9318 0.7721 0.2477 -0.0958 -0.0502 26 HIS B CD2 2751 C CE1 . HIS B 26 ? 0.6540 0.9657 0.7880 0.2454 -0.0969 -0.0619 26 HIS B CE1 2752 N NE2 . HIS B 26 ? 0.6773 0.9781 0.7903 0.2603 -0.1021 -0.0593 26 HIS B NE2 2753 N N . SER B 27 ? 0.6822 0.8395 0.7462 0.2354 -0.0771 -0.0041 27 SER B N 2754 C CA . SER B 27 ? 0.7204 0.8575 0.7532 0.2542 -0.0828 0.0067 27 SER B CA 2755 C C . SER B 27 ? 0.7239 0.8802 0.7463 0.2649 -0.0832 0.0036 27 SER B C 2756 O O . SER B 27 ? 0.7130 0.8725 0.7362 0.2569 -0.0747 0.0099 27 SER B O 2757 C CB . SER B 27 ? 0.7502 0.8485 0.7669 0.2430 -0.0785 0.0316 27 SER B CB 2758 O OG . SER B 27 ? 0.7979 0.8601 0.8018 0.2428 -0.0860 0.0364 27 SER B OG 2759 N N . ASN B 28 ? 0.7414 0.9106 0.7505 0.2863 -0.0935 -0.0059 28 ASN B N 2760 C CA . ASN B 28 ? 0.7479 0.9309 0.7409 0.2993 -0.0967 -0.0092 28 ASN B CA 2761 C C . ASN B 28 ? 0.7936 0.9701 0.7586 0.3266 -0.1077 -0.0086 28 ASN B C 2762 O O . ASN B 28 ? 0.8092 0.9591 0.7600 0.3350 -0.1116 -0.0015 28 ASN B O 2763 C CB . ASN B 28 ? 0.7063 0.9255 0.7194 0.2914 -0.1010 -0.0296 28 ASN B CB 2764 C CG . ASN B 28 ? 0.6771 0.9311 0.7108 0.2928 -0.1112 -0.0457 28 ASN B CG 2765 O OD1 . ASN B 28 ? 0.6920 0.9489 0.7181 0.3115 -0.1169 -0.0451 28 ASN B OD1 2766 N ND2 . ASN B 28 ? 0.6448 0.9261 0.7013 0.2737 -0.1143 -0.0591 28 ASN B ND2 2767 N N . GLU B 29 ? 0.8380 1.0330 0.7893 0.3422 -0.1146 -0.0161 29 GLU B N 2768 C CA . GLU B 29 ? 0.9084 1.0966 0.8295 0.3711 -0.1257 -0.0153 29 GLU B CA 2769 C C . GLU B 29 ? 0.9076 1.1220 0.8392 0.3868 -0.1371 -0.0300 29 GLU B C 2770 O O . GLU B 29 ? 0.9280 1.1213 0.8309 0.4121 -0.1449 -0.0260 29 GLU B O 2771 C CB . GLU B 29 ? 0.9638 1.1686 0.8674 0.3851 -0.1315 -0.0211 29 GLU B CB 2772 C CG . GLU B 29 ? 1.0101 1.1898 0.8906 0.3817 -0.1203 -0.0036 29 GLU B CG 2773 C CD . GLU B 29 ? 1.0730 1.2559 0.9203 0.4056 -0.1277 -0.0053 29 GLU B CD 2774 O OE1 . GLU B 29 ? 1.1144 1.2830 0.9339 0.4279 -0.1362 -0.0007 29 GLU B OE1 2775 O OE2 . GLU B 29 ? 1.0998 1.2955 0.9439 0.4044 -0.1262 -0.0120 29 GLU B OE2 2776 N N . GLN B 30 ? 0.8877 1.1485 0.8572 0.3727 -0.1382 -0.0458 30 GLN B N 2777 C CA . GLN B 30 ? 0.8805 1.1849 0.8665 0.3867 -0.1470 -0.0587 30 GLN B CA 2778 C C . GLN B 30 ? 0.8565 1.1374 0.8417 0.3907 -0.1426 -0.0536 30 GLN B C 2779 O O . GLN B 30 ? 0.8477 1.1550 0.8319 0.4147 -0.1496 -0.0613 30 GLN B O 2780 C CB . GLN B 30 ? 0.8763 1.2415 0.9027 0.3640 -0.1501 -0.0737 30 GLN B CB 2781 C CG . GLN B 30 ? 0.9109 1.3005 0.9334 0.3619 -0.1608 -0.0822 30 GLN B CG 2782 C CD . GLN B 30 ? 0.9205 1.3409 0.9724 0.3272 -0.1639 -0.0926 30 GLN B CD 2783 O OE1 . GLN B 30 ? 0.9066 1.2973 0.9646 0.3032 -0.1539 -0.0892 30 GLN B OE1 2784 N NE2 . GLN B 30 ? 0.9343 1.4133 1.0017 0.3237 -0.1797 -0.1045 30 GLN B NE2 2785 N N . GLY B 31 ? 0.8334 1.0675 0.8171 0.3693 -0.1318 -0.0411 31 GLY B N 2786 C CA . GLY B 31 ? 0.8355 1.0373 0.8125 0.3711 -0.1300 -0.0360 31 GLY B CA 2787 C C . GLY B 31 ? 0.7911 0.9744 0.7901 0.3375 -0.1181 -0.0293 31 GLY B C 2788 O O . GLY B 31 ? 0.7827 0.9553 0.7878 0.3163 -0.1103 -0.0210 31 GLY B O 2789 N N . SER B 32 ? 0.7704 0.9518 0.7788 0.3361 -0.1170 -0.0330 32 SER B N 2790 C CA . SER B 32 ? 0.7385 0.9006 0.7655 0.3065 -0.1072 -0.0270 32 SER B CA 2791 C C . SER B 32 ? 0.7163 0.8996 0.7604 0.3084 -0.1063 -0.0371 32 SER B C 2792 O O . SER B 32 ? 0.7435 0.9460 0.7767 0.3371 -0.1133 -0.0454 32 SER B O 2793 C CB . SER B 32 ? 0.7695 0.8622 0.7654 0.3000 -0.1081 -0.0072 32 SER B CB 2794 O OG . SER B 32 ? 0.8188 0.8714 0.7774 0.3247 -0.1196 -0.0062 32 SER B OG 2795 N N . GLY B 33 ? 0.6874 0.8692 0.7557 0.2809 -0.0974 -0.0359 33 GLY B N 2796 C CA . GLY B 33 ? 0.6834 0.8809 0.7648 0.2815 -0.0952 -0.0433 33 GLY B CA 2797 C C . GLY B 33 ? 0.6523 0.8569 0.7637 0.2490 -0.0851 -0.0436 33 GLY B C 2798 O O . GLY B 33 ? 0.6336 0.8334 0.7569 0.2264 -0.0799 -0.0395 33 GLY B O 2799 N N . TYR B 34 ? 0.6518 0.8679 0.7712 0.2506 -0.0827 -0.0489 34 TYR B N 2800 C CA . TYR B 34 ? 0.6220 0.8393 0.7644 0.2227 -0.0741 -0.0490 34 TYR B CA 2801 C C . TYR B 34 ? 0.5904 0.8735 0.7638 0.2107 -0.0704 -0.0593 34 TYR B C 2802 O O . TYR B 34 ? 0.5917 0.9248 0.7701 0.2285 -0.0736 -0.0660 34 TYR B O 2803 C CB . TYR B 34 ? 0.6372 0.8174 0.7633 0.2300 -0.0746 -0.0463 34 TYR B CB 2804 C CG . TYR B 34 ? 0.6728 0.7820 0.7631 0.2368 -0.0826 -0.0342 34 TYR B CG 2805 C CD1 . TYR B 34 ? 0.6633 0.7340 0.7555 0.2107 -0.0803 -0.0216 34 TYR B CD1 2806 C CD2 . TYR B 34 ? 0.7211 0.8020 0.7726 0.2688 -0.0940 -0.0341 34 TYR B CD2 2807 C CE1 . TYR B 34 ? 0.7022 0.7125 0.7623 0.2104 -0.0896 -0.0072 34 TYR B CE1 2808 C CE2 . TYR B 34 ? 0.7622 0.7700 0.7745 0.2700 -0.1046 -0.0211 34 TYR B CE2 2809 C CZ . TYR B 34 ? 0.7549 0.7299 0.7736 0.2377 -0.1025 -0.0067 34 TYR B CZ 2810 O OH . TYR B 34 ? 0.8155 0.7224 0.7958 0.2332 -0.1149 0.0092 34 TYR B OH 2811 N N . ALA B 35 ? 0.5779 0.8611 0.7697 0.1799 -0.0647 -0.0592 35 ALA B N 2812 C CA . ALA B 35 ? 0.5614 0.8954 0.7781 0.1598 -0.0626 -0.0659 35 ALA B CA 2813 C C . ALA B 35 ? 0.5597 0.8675 0.7831 0.1344 -0.0553 -0.0634 35 ALA B C 2814 O O . ALA B 35 ? 0.5469 0.8130 0.7640 0.1215 -0.0536 -0.0594 35 ALA B O 2815 C CB . ALA B 35 ? 0.5516 0.9111 0.7755 0.1462 -0.0690 -0.0704 35 ALA B CB 2816 N N . ALA B 36 ? 0.5594 0.8951 0.7938 0.1301 -0.0508 -0.0652 36 ALA B N 2817 C CA . ALA B 36 ? 0.5706 0.8840 0.8093 0.1075 -0.0444 -0.0630 36 ALA B CA 2818 C C . ALA B 36 ? 0.5830 0.9032 0.8303 0.0747 -0.0464 -0.0651 36 ALA B C 2819 O O . ALA B 36 ? 0.6067 0.9706 0.8638 0.0652 -0.0523 -0.0686 36 ALA B O 2820 C CB . ALA B 36 ? 0.5704 0.9164 0.8151 0.1143 -0.0389 -0.0636 36 ALA B CB 2821 N N . ASP B 37 ? 0.6018 0.8758 0.8416 0.0584 -0.0437 -0.0628 37 ASP B N 2822 C CA . ASP B 37 ? 0.6281 0.8936 0.8650 0.0289 -0.0473 -0.0653 37 ASP B CA 2823 C C . ASP B 37 ? 0.6738 0.9591 0.9194 0.0090 -0.0429 -0.0636 37 ASP B C 2824 O O . ASP B 37 ? 0.6744 0.9334 0.9164 0.0107 -0.0358 -0.0605 37 ASP B O 2825 C CB . ASP B 37 ? 0.6337 0.8407 0.8528 0.0275 -0.0467 -0.0636 37 ASP B CB 2826 C CG . ASP B 37 ? 0.6596 0.8441 0.8629 0.0035 -0.0537 -0.0678 37 ASP B CG 2827 O OD1 . ASP B 37 ? 0.6685 0.8498 0.8596 0.0024 -0.0627 -0.0724 37 ASP B OD1 2828 O OD2 . ASP B 37 ? 0.6759 0.8398 0.8733 -0.0134 -0.0517 -0.0668 37 ASP B OD2 2829 N N . LYS B 38 ? 0.7339 1.0687 0.9908 -0.0113 -0.0477 -0.0643 38 LYS B N 2830 C CA . LYS B 38 ? 0.7776 1.1487 1.0457 -0.0318 -0.0428 -0.0596 38 LYS B CA 2831 C C . LYS B 38 ? 0.7822 1.1012 1.0333 -0.0585 -0.0423 -0.0573 38 LYS B C 2832 O O . LYS B 38 ? 0.7515 1.0691 1.0038 -0.0603 -0.0334 -0.0532 38 LYS B O 2833 C CB . LYS B 38 ? 0.8442 1.2852 1.1289 -0.0541 -0.0506 -0.0579 38 LYS B CB 2834 C CG . LYS B 38 ? 0.9048 1.4039 1.2055 -0.0768 -0.0448 -0.0494 38 LYS B CG 2835 C CD . LYS B 38 ? 0.9716 1.4933 1.2733 -0.1262 -0.0578 -0.0442 38 LYS B CD 2836 C CE . LYS B 38 ? 0.9971 1.5732 1.3127 -0.1298 -0.0710 -0.0464 38 LYS B CE 2837 N NZ . LYS B 38 ? 0.9908 1.6737 1.3398 -0.1118 -0.0641 -0.0414 38 LYS B NZ 2838 N N . GLU B 39 ? 0.8214 1.0943 1.0515 -0.0759 -0.0529 -0.0606 39 GLU B N 2839 C CA . GLU B 39 ? 0.8678 1.0879 1.0737 -0.1012 -0.0560 -0.0592 39 GLU B CA 2840 C C . GLU B 39 ? 0.8068 0.9817 1.0045 -0.0828 -0.0458 -0.0582 39 GLU B C 2841 O O . GLU B 39 ? 0.8276 0.9922 1.0206 -0.0962 -0.0409 -0.0539 39 GLU B O 2842 C CB . GLU B 39 ? 0.9825 1.1511 1.1566 -0.1144 -0.0717 -0.0649 39 GLU B CB 2843 C CG . GLU B 39 ? 1.1081 1.2363 1.2526 -0.1526 -0.0822 -0.0626 39 GLU B CG 2844 C CD . GLU B 39 ? 1.2058 1.2465 1.3035 -0.1468 -0.0915 -0.0691 39 GLU B CD 2845 O OE1 . GLU B 39 ? 1.2151 1.2356 1.2987 -0.1265 -0.0977 -0.0762 39 GLU B OE1 2846 O OE2 . GLU B 39 ? 1.2918 1.2845 1.3636 -0.1596 -0.0925 -0.0669 39 GLU B OE2 2847 N N . SER B 40 ? 0.7239 0.8750 0.9198 -0.0541 -0.0432 -0.0606 40 SER B N 2848 C CA . SER B 40 ? 0.6793 0.7919 0.8690 -0.0393 -0.0361 -0.0581 40 SER B CA 2849 C C . SER B 40 ? 0.6350 0.7722 0.8413 -0.0288 -0.0269 -0.0542 40 SER B C 2850 O O . SER B 40 ? 0.6284 0.7389 0.8279 -0.0287 -0.0226 -0.0517 40 SER B O 2851 C CB . SER B 40 ? 0.6585 0.7472 0.8430 -0.0158 -0.0366 -0.0582 40 SER B CB 2852 O OG . SER B 40 ? 0.6638 0.7842 0.8641 0.0019 -0.0356 -0.0574 40 SER B OG 2853 N N . THR B 41 ? 0.5945 0.7803 0.8179 -0.0170 -0.0250 -0.0545 41 THR B N 2854 C CA . THR B 41 ? 0.5699 0.7780 0.8007 -0.0014 -0.0179 -0.0523 41 THR B CA 2855 C C . THR B 41 ? 0.5649 0.7926 0.7965 -0.0211 -0.0123 -0.0491 41 THR B C 2856 O O . THR B 41 ? 0.5472 0.7579 0.7720 -0.0140 -0.0067 -0.0472 41 THR B O 2857 C CB . THR B 41 ? 0.5608 0.8185 0.8034 0.0208 -0.0183 -0.0541 41 THR B CB 2858 O OG1 . THR B 41 ? 0.5510 0.7837 0.7882 0.0399 -0.0232 -0.0551 41 THR B OG1 2859 C CG2 . THR B 41 ? 0.5556 0.8334 0.7966 0.0425 -0.0120 -0.0532 41 THR B CG2 2860 N N . GLN B 42 ? 0.5937 0.8565 0.8314 -0.0480 -0.0150 -0.0474 42 GLN B N 2861 C CA . GLN B 42 ? 0.6169 0.9056 0.8554 -0.0723 -0.0099 -0.0408 42 GLN B CA 2862 C C . GLN B 42 ? 0.6348 0.8584 0.8497 -0.0894 -0.0105 -0.0392 42 GLN B C 2863 O O . GLN B 42 ? 0.6377 0.8645 0.8477 -0.0969 -0.0033 -0.0339 42 GLN B O 2864 C CB . GLN B 42 ? 0.6318 0.9733 0.8812 -0.1044 -0.0160 -0.0364 42 GLN B CB 2865 C CG . GLN B 42 ? 0.6559 1.0430 0.9107 -0.1317 -0.0097 -0.0255 42 GLN B CG 2866 C CD . GLN B 42 ? 0.6469 1.0958 0.9176 -0.1025 0.0046 -0.0223 42 GLN B CD 2867 O OE1 . GLN B 42 ? 0.6506 1.0943 0.9128 -0.1022 0.0141 -0.0173 42 GLN B OE1 2868 N NE2 . GLN B 42 ? 0.6388 1.1434 0.9276 -0.0741 0.0055 -0.0257 42 GLN B NE2 2869 N N . LYS B 43 ? 0.6566 0.8234 0.8543 -0.0927 -0.0191 -0.0436 43 LYS B N 2870 C CA . LYS B 43 ? 0.6912 0.7912 0.8629 -0.0978 -0.0208 -0.0438 43 LYS B CA 2871 C C . LYS B 43 ? 0.6485 0.7344 0.8231 -0.0733 -0.0125 -0.0431 43 LYS B C 2872 O O . LYS B 43 ? 0.6755 0.7372 0.8366 -0.0802 -0.0093 -0.0401 43 LYS B O 2873 C CB . LYS B 43 ? 0.7604 0.8139 0.9149 -0.0909 -0.0302 -0.0496 43 LYS B CB 2874 C CG . LYS B 43 ? 0.8582 0.8559 0.9759 -0.1126 -0.0406 -0.0510 43 LYS B CG 2875 C CD . LYS B 43 ? 0.9368 0.9209 1.0396 -0.1160 -0.0533 -0.0568 43 LYS B CD 2876 C CE . LYS B 43 ? 1.0252 0.9335 1.0786 -0.1221 -0.0657 -0.0610 43 LYS B CE 2877 N NZ . LYS B 43 ? 1.0670 0.9419 1.0936 -0.1524 -0.0701 -0.0562 43 LYS B NZ 2878 N N . ALA B 44 ? 0.5782 0.6749 0.7664 -0.0462 -0.0111 -0.0452 44 ALA B N 2879 C CA . ALA B 44 ? 0.5675 0.6453 0.7541 -0.0256 -0.0077 -0.0442 44 ALA B CA 2880 C C . ALA B 44 ? 0.5675 0.6723 0.7545 -0.0228 -0.0002 -0.0420 44 ALA B C 2881 O O . ALA B 44 ? 0.5876 0.6647 0.7622 -0.0196 0.0018 -0.0405 44 ALA B O 2882 C CB . ALA B 44 ? 0.5559 0.6356 0.7511 -0.0015 -0.0108 -0.0451 44 ALA B CB 2883 N N . ILE B 45 ? 0.5636 0.7264 0.7638 -0.0219 0.0038 -0.0414 45 ILE B N 2884 C CA . ILE B 45 ? 0.5830 0.7835 0.7827 -0.0151 0.0127 -0.0383 45 ILE B CA 2885 C C . ILE B 45 ? 0.6053 0.7974 0.7943 -0.0426 0.0173 -0.0322 45 ILE B C 2886 O O . ILE B 45 ? 0.6357 0.8197 0.8125 -0.0335 0.0233 -0.0302 45 ILE B O 2887 C CB . ILE B 45 ? 0.5882 0.8675 0.8066 -0.0091 0.0166 -0.0370 45 ILE B CB 2888 C CG1 . ILE B 45 ? 0.5830 0.8652 0.8032 0.0263 0.0122 -0.0432 45 ILE B CG1 2889 C CG2 . ILE B 45 ? 0.5797 0.9111 0.7978 -0.0052 0.0279 -0.0312 45 ILE B CG2 2890 C CD1 . ILE B 45 ? 0.5880 0.9438 0.8270 0.0326 0.0128 -0.0432 45 ILE B CD1 2891 N N . ASP B 46 ? 0.6137 0.8021 0.8015 -0.0760 0.0130 -0.0290 46 ASP B N 2892 C CA . ASP B 46 ? 0.6456 0.8169 0.8162 -0.1059 0.0149 -0.0217 46 ASP B CA 2893 C C . ASP B 46 ? 0.6444 0.7437 0.7909 -0.0977 0.0133 -0.0241 46 ASP B C 2894 O O . ASP B 46 ? 0.6629 0.7536 0.7949 -0.1033 0.0191 -0.0190 46 ASP B O 2895 C CB . ASP B 46 ? 0.6728 0.8369 0.8366 -0.1443 0.0053 -0.0184 46 ASP B CB 2896 C CG . ASP B 46 ? 0.6813 0.9250 0.8701 -0.1593 0.0053 -0.0135 46 ASP B CG 2897 O OD1 . ASP B 46 ? 0.6665 0.9776 0.8774 -0.1385 0.0153 -0.0116 46 ASP B OD1 2898 O OD2 . ASP B 46 ? 0.7154 0.9539 0.8987 -0.1901 -0.0063 -0.0118 46 ASP B OD2 2899 N N . GLY B 47 ? 0.6213 0.6749 0.7638 -0.0834 0.0057 -0.0309 47 GLY B N 2900 C CA . GLY B 47 ? 0.6329 0.6266 0.7556 -0.0754 0.0026 -0.0324 47 GLY B CA 2901 C C . GLY B 47 ? 0.6313 0.6240 0.7535 -0.0532 0.0073 -0.0324 47 GLY B C 2902 O O . GLY B 47 ? 0.6471 0.6135 0.7506 -0.0563 0.0092 -0.0299 47 GLY B O 2903 N N . VAL B 48 ? 0.6086 0.6241 0.7457 -0.0300 0.0073 -0.0354 48 VAL B N 2904 C CA . VAL B 48 ? 0.6072 0.6138 0.7361 -0.0065 0.0079 -0.0366 48 VAL B CA 2905 C C . VAL B 48 ? 0.6147 0.6517 0.7342 -0.0058 0.0181 -0.0335 48 VAL B C 2906 O O . VAL B 48 ? 0.6212 0.6326 0.7217 0.0047 0.0185 -0.0335 48 VAL B O 2907 C CB . VAL B 48 ? 0.6072 0.6242 0.7453 0.0174 0.0028 -0.0402 48 VAL B CB 2908 C CG1 . VAL B 48 ? 0.6255 0.6324 0.7457 0.0435 0.0012 -0.0424 48 VAL B CG1 2909 C CG2 . VAL B 48 ? 0.6026 0.5855 0.7461 0.0173 -0.0070 -0.0400 48 VAL B CG2 2910 N N . THR B 49 ? 0.6060 0.7013 0.7384 -0.0174 0.0262 -0.0296 49 THR B N 2911 C CA . THR B 49 ? 0.6317 0.7705 0.7579 -0.0185 0.0380 -0.0233 49 THR B CA 2912 C C . THR B 49 ? 0.6702 0.7761 0.7764 -0.0429 0.0405 -0.0168 49 THR B C 2913 O O . THR B 49 ? 0.6886 0.7921 0.7769 -0.0325 0.0469 -0.0142 49 THR B O 2914 C CB . THR B 49 ? 0.6209 0.8405 0.7696 -0.0322 0.0451 -0.0171 49 THR B CB 2915 O OG1 . THR B 49 ? 0.5926 0.8407 0.7564 -0.0059 0.0421 -0.0236 49 THR B OG1 2916 C CG2 . THR B 49 ? 0.6238 0.9028 0.7687 -0.0315 0.0592 -0.0077 49 THR B CG2 2917 N N . ASN B 50 ? 0.7048 0.7798 0.8079 -0.0729 0.0343 -0.0147 50 ASN B N 2918 C CA . ASN B 50 ? 0.7566 0.7880 0.8329 -0.0951 0.0339 -0.0089 50 ASN B CA 2919 C C . ASN B 50 ? 0.7515 0.7238 0.8079 -0.0737 0.0294 -0.0144 50 ASN B C 2920 O O . ASN B 50 ? 0.7806 0.7308 0.8134 -0.0784 0.0328 -0.0098 50 ASN B O 2921 C CB . ASN B 50 ? 0.7840 0.7812 0.8509 -0.1262 0.0242 -0.0076 50 ASN B CB 2922 C CG . ASN B 50 ? 0.8133 0.8641 0.8931 -0.1576 0.0257 0.0006 50 ASN B CG 2923 O OD1 . ASN B 50 ? 0.8512 0.9694 0.9449 -0.1626 0.0365 0.0091 50 ASN B OD1 2924 N ND2 . ASN B 50 ? 0.8397 0.8636 0.9133 -0.1780 0.0138 -0.0015 50 ASN B ND2 2925 N N . LYS B 51 ? 0.7216 0.6710 0.7872 -0.0519 0.0210 -0.0227 51 LYS B N 2926 C CA . LYS B 51 ? 0.7221 0.6218 0.7728 -0.0341 0.0137 -0.0265 51 LYS B CA 2927 C C . LYS B 51 ? 0.7214 0.6286 0.7590 -0.0140 0.0184 -0.0268 51 LYS B C 2928 O O . LYS B 51 ? 0.7344 0.6089 0.7485 -0.0119 0.0175 -0.0256 51 LYS B O 2929 C CB . LYS B 51 ? 0.7003 0.5864 0.7672 -0.0193 0.0034 -0.0318 51 LYS B CB 2930 C CG . LYS B 51 ? 0.7154 0.5641 0.7724 -0.0020 -0.0062 -0.0338 51 LYS B CG 2931 C CD . LYS B 51 ? 0.7062 0.5490 0.7806 0.0061 -0.0165 -0.0348 51 LYS B CD 2932 C CE . LYS B 51 ? 0.6980 0.5326 0.7794 -0.0043 -0.0189 -0.0335 51 LYS B CE 2933 N NZ . LYS B 51 ? 0.6993 0.5283 0.7943 0.0043 -0.0288 -0.0310 51 LYS B NZ 2934 N N . VAL B 52 ? 0.6942 0.6422 0.7424 0.0041 0.0224 -0.0289 52 VAL B N 2935 C CA . VAL B 52 ? 0.7107 0.6630 0.7395 0.0308 0.0252 -0.0310 52 VAL B CA 2936 C C . VAL B 52 ? 0.7326 0.7017 0.7437 0.0204 0.0379 -0.0233 52 VAL B C 2937 O O . VAL B 52 ? 0.7564 0.6923 0.7402 0.0323 0.0363 -0.0242 52 VAL B O 2938 C CB . VAL B 52 ? 0.7147 0.7132 0.7527 0.0551 0.0282 -0.0344 52 VAL B CB 2939 C CG1 . VAL B 52 ? 0.7501 0.7561 0.7591 0.0878 0.0324 -0.0368 52 VAL B CG1 2940 C CG2 . VAL B 52 ? 0.7023 0.6726 0.7493 0.0660 0.0139 -0.0406 52 VAL B CG2 2941 N N . ASN B 53 ? 0.7233 0.7426 0.7483 -0.0045 0.0490 -0.0145 53 ASN B N 2942 C CA . ASN B 53 ? 0.7606 0.8026 0.7695 -0.0205 0.0615 -0.0033 53 ASN B CA 2943 C C . ASN B 53 ? 0.7927 0.7669 0.7757 -0.0385 0.0556 -0.0010 53 ASN B C 2944 O O . ASN B 53 ? 0.8198 0.7835 0.7766 -0.0349 0.0615 0.0038 53 ASN B O 2945 C CB . ASN B 53 ? 0.7565 0.8682 0.7869 -0.0515 0.0714 0.0086 53 ASN B CB 2946 C CG . ASN B 53 ? 0.7400 0.9276 0.7963 -0.0306 0.0774 0.0068 53 ASN B CG 2947 O OD1 . ASN B 53 ? 0.7510 0.9438 0.7999 0.0106 0.0778 -0.0014 53 ASN B OD1 2948 N ND2 . ASN B 53 ? 0.7368 0.9792 0.8192 -0.0581 0.0798 0.0141 53 ASN B ND2 2949 N N . SER B 54 ? 0.8061 0.7347 0.7932 -0.0537 0.0438 -0.0048 54 SER B N 2950 C CA . SER B 54 ? 0.8534 0.7137 0.8129 -0.0623 0.0357 -0.0048 54 SER B CA 2951 C C . SER B 54 ? 0.8866 0.7110 0.8284 -0.0329 0.0301 -0.0112 54 SER B C 2952 O O . SER B 54 ? 0.9106 0.7019 0.8226 -0.0347 0.0304 -0.0078 54 SER B O 2953 C CB . SER B 54 ? 0.8349 0.6572 0.8006 -0.0717 0.0232 -0.0098 54 SER B CB 2954 O OG . SER B 54 ? 0.8398 0.6655 0.8009 -0.1042 0.0238 -0.0031 54 SER B OG 2955 N N . ILE B 55 ? 0.8942 0.7214 0.8507 -0.0078 0.0229 -0.0198 55 ILE B N 2956 C CA . ILE B 55 ? 0.9449 0.7362 0.8826 0.0179 0.0133 -0.0258 55 ILE B CA 2957 C C . ILE B 55 ? 0.9898 0.7954 0.9008 0.0333 0.0232 -0.0236 55 ILE B C 2958 O O . ILE B 55 ? 1.0162 0.7853 0.8978 0.0383 0.0204 -0.0230 55 ILE B O 2959 C CB . ILE B 55 ? 0.9506 0.7400 0.9049 0.0369 0.0014 -0.0333 55 ILE B CB 2960 C CG1 . ILE B 55 ? 0.9460 0.7131 0.9197 0.0255 -0.0103 -0.0341 55 ILE B CG1 2961 C CG2 . ILE B 55 ? 0.9884 0.7447 0.9159 0.0631 -0.0097 -0.0388 55 ILE B CG2 2962 C CD1 . ILE B 55 ? 0.9425 0.7101 0.9337 0.0369 -0.0218 -0.0376 55 ILE B CD1 2963 N N . ILE B 56 ? 0.9830 0.8452 0.9027 0.0435 0.0350 -0.0220 56 ILE B N 2964 C CA . ILE B 56 ? 1.0136 0.9037 0.9080 0.0631 0.0473 -0.0187 56 ILE B CA 2965 C C . ILE B 56 ? 1.0755 0.9638 0.9502 0.0408 0.0582 -0.0071 56 ILE B C 2966 O O . ILE B 56 ? 1.1105 0.9841 0.9518 0.0579 0.0615 -0.0062 56 ILE B O 2967 C CB . ILE B 56 ? 0.9929 0.9626 0.9057 0.0739 0.0611 -0.0157 56 ILE B CB 2968 C CG1 . ILE B 56 ? 0.9749 0.9354 0.8919 0.1052 0.0490 -0.0279 56 ILE B CG1 2969 C CG2 . ILE B 56 ? 1.0211 1.0377 0.9102 0.0910 0.0784 -0.0082 56 ILE B CG2 2970 C CD1 . ILE B 56 ? 0.9623 0.9985 0.8992 0.1184 0.0598 -0.0265 56 ILE B CD1 2971 N N . ASP B 57 ? 1.1027 0.9999 0.9926 0.0027 0.0621 0.0019 57 ASP B N 2972 C CA . ASP B 57 ? 1.1742 1.0699 1.0422 -0.0248 0.0718 0.0159 57 ASP B CA 2973 C C . ASP B 57 ? 1.1833 0.9998 1.0176 -0.0250 0.0609 0.0133 57 ASP B C 2974 O O . ASP B 57 ? 1.2184 1.0249 1.0208 -0.0276 0.0682 0.0216 57 ASP B O 2975 C CB . ASP B 57 ? 1.2018 1.1218 1.0889 -0.0678 0.0748 0.0264 57 ASP B CB 2976 C CG . ASP B 57 ? 1.2901 1.2093 1.1508 -0.1023 0.0834 0.0441 57 ASP B CG 2977 O OD1 . ASP B 57 ? 1.3628 1.3259 1.2109 -0.0963 0.0985 0.0546 57 ASP B OD1 2978 O OD2 . ASP B 57 ? 1.3220 1.1945 1.1702 -0.1343 0.0743 0.0482 57 ASP B OD2 2979 N N . LYS B 58 ? 1.1776 0.9430 1.0185 -0.0213 0.0439 0.0030 58 LYS B N 2980 C CA . LYS B 58 ? 1.2076 0.9043 1.0194 -0.0170 0.0316 -0.0002 58 LYS B CA 2981 C C . LYS B 58 ? 1.2647 0.9423 1.0514 0.0137 0.0280 -0.0056 58 LYS B C 2982 O O . LYS B 58 ? 1.2799 0.9166 1.0324 0.0153 0.0251 -0.0033 58 LYS B O 2983 C CB . LYS B 58 ? 1.1792 0.8421 1.0088 -0.0157 0.0148 -0.0089 58 LYS B CB 2984 C CG . LYS B 58 ? 1.1851 0.8116 1.0017 -0.0387 0.0102 -0.0049 58 LYS B CG 2985 C CD . LYS B 58 ? 1.2175 0.8590 1.0200 -0.0709 0.0223 0.0078 58 LYS B CD 2986 C CE . LYS B 58 ? 1.2521 0.8443 1.0333 -0.0925 0.0130 0.0100 58 LYS B CE 2987 N NZ . LYS B 58 ? 1.3051 0.8790 1.0483 -0.1241 0.0190 0.0245 58 LYS B NZ 2988 N N . MET B 59 ? 1.3057 1.0075 1.1034 0.0391 0.0266 -0.0131 59 MET B N 2989 C CA . MET B 59 ? 1.3817 1.0577 1.1491 0.0710 0.0191 -0.0202 59 MET B CA 2990 C C . MET B 59 ? 1.4524 1.1597 1.1903 0.0830 0.0372 -0.0130 59 MET B C 2991 O O . MET B 59 ? 1.5052 1.1853 1.2070 0.1102 0.0321 -0.0181 59 MET B O 2992 C CB . MET B 59 ? 1.3759 1.0531 1.1567 0.0943 0.0066 -0.0311 59 MET B CB 2993 C CG . MET B 59 ? 1.3398 0.9959 1.1513 0.0826 -0.0103 -0.0356 59 MET B CG 2994 S SD . MET B 59 ? 1.3664 0.9591 1.1655 0.0805 -0.0334 -0.0386 59 MET B SD 2995 C CE . MET B 59 ? 1.4114 0.9628 1.1633 0.1102 -0.0469 -0.0456 59 MET B CE 2996 N N . ASN B 60 ? 1.4821 1.2489 1.2342 0.0625 0.0574 -0.0004 60 ASN B N 2997 C CA . ASN B 60 ? 1.5344 1.3497 1.2640 0.0705 0.0779 0.0108 60 ASN B CA 2998 C C . ASN B 60 ? 1.5860 1.3593 1.2704 0.0696 0.0797 0.0171 60 ASN B C 2999 O O . ASN B 60 ? 1.5934 1.3809 1.2456 0.0969 0.0885 0.0187 60 ASN B O 3000 C CB . ASN B 60 ? 1.5144 1.4085 1.2739 0.0390 0.0969 0.0267 60 ASN B CB 3001 C CG . ASN B 60 ? 1.5476 1.4638 1.2845 0.0125 0.1135 0.0470 60 ASN B CG 3002 O OD1 . ASN B 60 ? 1.5426 1.4155 1.2689 -0.0227 0.1088 0.0547 60 ASN B OD1 3003 N ND2 . ASN B 60 ? 1.5658 1.5502 1.2919 0.0300 0.1327 0.0568 60 ASN B ND2 3004 N N . THR B 61 ? 1.3966 1.6753 1.4196 0.0568 -0.3494 -0.2352 61 THR B N 3005 C CA . THR B 61 ? 1.3763 1.6139 1.4161 0.0464 -0.3197 -0.2350 61 THR B CA 3006 C C . THR B 61 ? 1.3451 1.5741 1.3465 0.0698 -0.2843 -0.2180 61 THR B C 3007 O O . THR B 61 ? 1.3952 1.6218 1.3359 0.0874 -0.2823 -0.2334 61 THR B O 3008 C CB . THR B 61 ? 1.4577 1.6349 1.4694 0.0354 -0.3399 -0.2711 61 THR B CB 3009 O OG1 . THR B 61 ? 1.4822 1.6629 1.5272 0.0014 -0.3765 -0.2844 61 THR B OG1 3010 C CG2 . THR B 61 ? 1.4616 1.5826 1.4798 0.0278 -0.3170 -0.2653 61 THR B CG2 3011 N N . GLN B 62 ? 1.2799 1.5146 1.3174 0.0679 -0.2564 -0.1896 62 GLN B N 3012 C CA . GLN B 62 ? 1.2533 1.4832 1.2592 0.0825 -0.2264 -0.1690 62 GLN B CA 3013 C C . GLN B 62 ? 1.2184 1.4390 1.2688 0.0757 -0.1988 -0.1482 62 GLN B C 3014 O O . GLN B 62 ? 1.2148 1.4549 1.3210 0.0648 -0.2015 -0.1445 62 GLN B O 3015 C CB . GLN B 62 ? 1.2549 1.5084 1.2219 0.0925 -0.2378 -0.1479 62 GLN B CB 3016 C CG . GLN B 62 ? 1.2298 1.4743 1.1745 0.0947 -0.2144 -0.1148 62 GLN B CG 3017 C CD . GLN B 62 ? 1.2788 1.5262 1.1665 0.0943 -0.2352 -0.0880 62 GLN B CD 3018 O OE1 . GLN B 62 ? 1.3253 1.5908 1.1711 0.0932 -0.2591 -0.0967 62 GLN B OE1 3019 N NE2 . GLN B 62 ? 1.2871 1.5072 1.1640 0.0925 -0.2312 -0.0543 62 GLN B NE2 3020 N N . PHE B 63 ? 1.1563 1.3594 1.1816 0.0817 -0.1721 -0.1384 63 PHE B N 3021 C CA . PHE B 63 ? 1.1068 1.2948 1.1598 0.0755 -0.1458 -0.1221 63 PHE B CA 3022 C C . PHE B 63 ? 1.1093 1.3169 1.2007 0.0777 -0.1436 -0.1046 63 PHE B C 3023 O O . PHE B 63 ? 1.1583 1.3743 1.2356 0.0911 -0.1596 -0.0932 63 PHE B O 3024 C CB . PHE B 63 ? 1.0506 1.2297 1.0659 0.0832 -0.1240 -0.1129 63 PHE B CB 3025 C CG . PHE B 63 ? 0.9971 1.1547 1.0313 0.0767 -0.1009 -0.1008 63 PHE B CG 3026 C CD1 . PHE B 63 ? 0.9760 1.1031 1.0186 0.0694 -0.0988 -0.1119 63 PHE B CD1 3027 C CD2 . PHE B 63 ? 0.9900 1.1469 1.0247 0.0766 -0.0870 -0.0779 63 PHE B CD2 3028 C CE1 . PHE B 63 ? 0.9553 1.0622 1.0057 0.0607 -0.0799 -0.0985 63 PHE B CE1 3029 C CE2 . PHE B 63 ? 0.9449 1.0834 0.9910 0.0705 -0.0669 -0.0702 63 PHE B CE2 3030 C CZ . PHE B 63 ? 0.9433 1.0622 0.9970 0.0618 -0.0617 -0.0795 63 PHE B CZ 3031 N N . GLU B 64 ? 1.0921 1.3056 1.2266 0.0658 -0.1271 -0.1045 64 GLU B N 3032 C CA . GLU B 64 ? 1.0860 1.3286 1.2611 0.0761 -0.1207 -0.0991 64 GLU B CA 3033 C C . GLU B 64 ? 1.0747 1.2973 1.2462 0.0710 -0.0896 -0.0902 64 GLU B C 3034 O O . GLU B 64 ? 1.0855 1.2926 1.2527 0.0480 -0.0742 -0.0907 64 GLU B O 3035 C CB . GLU B 64 ? 1.0941 1.3987 1.3337 0.0635 -0.1286 -0.1156 64 GLU B CB 3036 C CG . GLU B 64 ? 1.1298 1.4614 1.3795 0.0675 -0.1646 -0.1268 64 GLU B CG 3037 C CD . GLU B 64 ? 1.1331 1.5381 1.4515 0.0430 -0.1718 -0.1441 64 GLU B CD 3038 O OE1 . GLU B 64 ? 1.0850 1.5430 1.4521 0.0334 -0.1485 -0.1482 64 GLU B OE1 3039 O OE2 . GLU B 64 ? 1.1633 1.5808 1.4853 0.0296 -0.2006 -0.1553 64 GLU B OE2 3040 N N . ALA B 65 ? 1.0812 1.2938 1.2473 0.0921 -0.0867 -0.0821 65 ALA B N 3041 C CA . ALA B 65 ? 1.0758 1.2671 1.2323 0.0891 -0.0609 -0.0764 65 ALA B CA 3042 C C . ALA B 65 ? 1.0593 1.3020 1.2665 0.0879 -0.0436 -0.0929 65 ALA B C 3043 O O . ALA B 65 ? 1.0043 1.3019 1.2587 0.1052 -0.0555 -0.1099 65 ALA B O 3044 C CB . ALA B 65 ? 1.1014 1.2471 1.2192 0.1071 -0.0703 -0.0618 65 ALA B CB 3045 N N . VAL B 66 ? 1.0785 1.3130 1.2747 0.0675 -0.0163 -0.0896 66 VAL B N 3046 C CA . VAL B 66 ? 1.0694 1.3633 1.3011 0.0582 0.0078 -0.1048 66 VAL B CA 3047 C C . VAL B 66 ? 1.0719 1.3363 1.2756 0.0734 0.0236 -0.1060 66 VAL B C 3048 O O . VAL B 66 ? 1.1135 1.3094 1.2690 0.0734 0.0200 -0.0886 66 VAL B O 3049 C CB . VAL B 66 ? 1.0917 1.3993 1.3216 0.0066 0.0234 -0.0965 66 VAL B CB 3050 C CG1 . VAL B 66 ? 1.1051 1.5036 1.3740 -0.0149 0.0506 -0.1115 66 VAL B CG1 3051 C CG2 . VAL B 66 ? 1.1163 1.4200 1.3557 -0.0114 -0.0007 -0.0941 66 VAL B CG2 3052 N N . GLY B 67 ? 1.0353 1.3613 1.2709 0.0864 0.0404 -0.1309 67 GLY B N 3053 C CA . GLY B 67 ? 1.0024 1.3052 1.2091 0.1003 0.0556 -0.1401 67 GLY B CA 3054 C C . GLY B 67 ? 0.9618 1.2537 1.1310 0.0553 0.0831 -0.1235 67 GLY B C 3055 O O . GLY B 67 ? 0.9634 1.3136 1.1481 0.0170 0.1027 -0.1223 67 GLY B O 3056 N N . ARG B 68 ? 0.9167 1.1324 1.0328 0.0552 0.0801 -0.1081 68 ARG B N 3057 C CA . ARG B 68 ? 0.8935 1.0859 0.9659 0.0194 0.0970 -0.0913 68 ARG B CA 3058 C C . ARG B 68 ? 0.9081 1.0565 0.9398 0.0354 0.0983 -0.0972 68 ARG B C 3059 O O . ARG B 68 ? 0.9350 1.0257 0.9487 0.0531 0.0770 -0.0898 68 ARG B O 3060 C CB . ARG B 68 ? 0.8791 1.0176 0.9280 -0.0018 0.0804 -0.0625 68 ARG B CB 3061 C CG . ARG B 68 ? 0.8861 1.0412 0.9414 -0.0405 0.0820 -0.0515 68 ARG B CG 3062 C CD . ARG B 68 ? 0.8867 0.9759 0.9163 -0.0465 0.0565 -0.0334 68 ARG B CD 3063 N NE . ARG B 68 ? 0.8797 0.9800 0.9385 -0.0487 0.0397 -0.0378 68 ARG B NE 3064 C CZ . ARG B 68 ? 0.8565 0.9600 0.9334 -0.0192 0.0244 -0.0465 68 ARG B CZ 3065 N NH1 . ARG B 68 ? 0.8181 0.9112 0.8851 0.0096 0.0228 -0.0472 68 ARG B NH1 3066 N NH2 . ARG B 68 ? 0.8845 0.9997 0.9830 -0.0251 0.0080 -0.0527 68 ARG B NH2 3067 N N . GLU B 69 ? 0.9038 1.0822 0.9157 0.0231 0.1223 -0.1099 69 GLU B N 3068 C CA . GLU B 69 ? 0.8984 1.0378 0.8686 0.0382 0.1223 -0.1226 69 GLU B CA 3069 C C . GLU B 69 ? 0.8729 0.9810 0.7872 0.0012 0.1295 -0.0993 69 GLU B C 3070 O O . GLU B 69 ? 0.8593 0.9904 0.7636 -0.0360 0.1417 -0.0812 69 GLU B O 3071 C CB . GLU B 69 ? 0.9453 1.1490 0.9329 0.0668 0.1404 -0.1686 69 GLU B CB 3072 C CG . GLU B 69 ? 0.9585 1.1926 1.0044 0.1132 0.1242 -0.1954 69 GLU B CG 3073 C CD . GLU B 69 ? 1.0082 1.3055 1.0759 0.1591 0.1339 -0.2522 69 GLU B CD 3074 O OE1 . GLU B 69 ? 1.0770 1.3347 1.0997 0.1753 0.1334 -0.2738 69 GLU B OE1 3075 O OE2 . GLU B 69 ? 0.9991 1.3905 1.1308 0.1823 0.1391 -0.2800 69 GLU B OE2 3076 N N . PHE B 70 ? 0.8685 0.9176 0.7428 0.0088 0.1156 -0.0978 70 PHE B N 3077 C CA . PHE B 70 ? 0.8828 0.8974 0.7040 -0.0197 0.1127 -0.0763 70 PHE B CA 3078 C C . PHE B 70 ? 0.9178 0.9059 0.6955 -0.0103 0.1111 -0.0972 70 PHE B C 3079 O O . PHE B 70 ? 0.9140 0.8771 0.6990 0.0189 0.0989 -0.1199 70 PHE B O 3080 C CB . PHE B 70 ? 0.8615 0.8323 0.6843 -0.0239 0.0861 -0.0478 70 PHE B CB 3081 C CG . PHE B 70 ? 0.8292 0.8154 0.6910 -0.0246 0.0812 -0.0354 70 PHE B CG 3082 C CD1 . PHE B 70 ? 0.8153 0.8104 0.7168 -0.0027 0.0733 -0.0422 70 PHE B CD1 3083 C CD2 . PHE B 70 ? 0.8423 0.8228 0.6921 -0.0486 0.0785 -0.0165 70 PHE B CD2 3084 C CE1 . PHE B 70 ? 0.7864 0.7963 0.7186 -0.0032 0.0670 -0.0347 70 PHE B CE1 3085 C CE2 . PHE B 70 ? 0.8228 0.8064 0.7029 -0.0487 0.0685 -0.0100 70 PHE B CE2 3086 C CZ . PHE B 70 ? 0.7973 0.8015 0.7204 -0.0251 0.0649 -0.0213 70 PHE B CZ 3087 N N . ASN B 71 ? 0.9575 0.9400 0.6821 -0.0362 0.1176 -0.0889 71 ASN B N 3088 C CA . ASN B 71 ? 1.0117 0.9718 0.6869 -0.0300 0.1159 -0.1129 71 ASN B CA 3089 C C . ASN B 71 ? 1.0275 0.9217 0.6820 -0.0336 0.0820 -0.0970 71 ASN B C 3090 O O . ASN B 71 ? 0.9974 0.8787 0.6821 -0.0364 0.0644 -0.0717 71 ASN B O 3091 C CB . ASN B 71 ? 1.0519 1.0471 0.6706 -0.0593 0.1399 -0.1147 71 ASN B CB 3092 C CG . ASN B 71 ? 1.0584 1.0165 0.6324 -0.0957 0.1224 -0.0712 71 ASN B CG 3093 O OD1 . ASN B 71 ? 1.0569 0.9643 0.6235 -0.0920 0.0913 -0.0561 71 ASN B OD1 3094 N ND2 . ASN B 71 ? 1.1016 1.0870 0.6434 -0.1328 0.1388 -0.0508 71 ASN B ND2 3095 N N . ASN B 72 ? 1.1002 0.9639 0.7036 -0.0355 0.0734 -0.1149 72 ASN B N 3096 C CA . ASN B 72 ? 1.1242 0.9341 0.7101 -0.0442 0.0394 -0.1053 72 ASN B CA 3097 C C . ASN B 72 ? 1.1035 0.9171 0.6818 -0.0694 0.0221 -0.0694 72 ASN B C 3098 O O . ASN B 72 ? 1.1084 0.9068 0.6959 -0.0787 -0.0043 -0.0580 72 ASN B O 3099 C CB . ASN B 72 ? 1.2164 0.9873 0.7452 -0.0403 0.0302 -0.1393 72 ASN B CB 3100 C CG . ASN B 72 ? 1.2648 0.9724 0.7829 -0.0512 -0.0087 -0.1354 72 ASN B CG 3101 O OD1 . ASN B 72 ? 1.2994 0.9794 0.8488 -0.0446 -0.0234 -0.1302 72 ASN B OD1 3102 N ND2 . ASN B 72 ? 1.3348 1.0199 0.8044 -0.0744 -0.0281 -0.1352 72 ASN B ND2 3103 N N . LEU B 73 ? 1.0921 0.9269 0.6512 -0.0818 0.0330 -0.0527 73 LEU B N 3104 C CA . LEU B 73 ? 1.0844 0.9142 0.6371 -0.0939 0.0081 -0.0217 73 LEU B CA 3105 C C . LEU B 73 ? 1.0567 0.9004 0.6483 -0.0889 0.0113 -0.0014 73 LEU B C 3106 O O . LEU B 73 ? 1.0710 0.8983 0.6381 -0.0982 -0.0044 0.0212 73 LEU B O 3107 C CB . LEU B 73 ? 1.1635 0.9770 0.6413 -0.1147 0.0012 -0.0143 73 LEU B CB 3108 C CG . LEU B 73 ? 1.2194 1.0135 0.6508 -0.1212 -0.0126 -0.0344 73 LEU B CG 3109 C CD1 . LEU B 73 ? 1.2846 1.0686 0.6307 -0.1432 -0.0121 -0.0298 73 LEU B CD1 3110 C CD2 . LEU B 73 ? 1.1983 0.9892 0.6559 -0.1217 -0.0506 -0.0253 73 LEU B CD2 3111 N N . GLU B 74 ? 0.9895 0.8526 0.6349 -0.0737 0.0254 -0.0101 74 GLU B N 3112 C CA . GLU B 74 ? 0.9407 0.8150 0.6273 -0.0661 0.0229 0.0036 74 GLU B CA 3113 C C . GLU B 74 ? 0.9051 0.7972 0.6433 -0.0485 0.0164 -0.0022 74 GLU B C 3114 O O . GLU B 74 ? 0.8564 0.7642 0.6319 -0.0384 0.0249 -0.0038 74 GLU B O 3115 C CB . GLU B 74 ? 0.9345 0.8269 0.6280 -0.0745 0.0503 0.0003 74 GLU B CB 3116 C CG . GLU B 74 ? 0.9800 0.8626 0.6167 -0.1063 0.0571 0.0154 74 GLU B CG 3117 C CD . GLU B 74 ? 0.9795 0.9055 0.6282 -0.1251 0.0887 0.0103 74 GLU B CD 3118 O OE1 . GLU B 74 ? 0.9493 0.9219 0.6387 -0.1061 0.1114 -0.0183 74 GLU B OE1 3119 O OE2 . GLU B 74 ? 1.0117 0.9258 0.6284 -0.1607 0.0870 0.0351 74 GLU B OE2 3120 N N . ARG B 75 ? 0.9280 0.8210 0.6628 -0.0516 -0.0001 -0.0035 75 ARG B N 3121 C CA . ARG B 75 ? 0.8940 0.8063 0.6630 -0.0496 -0.0061 -0.0039 75 ARG B CA 3122 C C . ARG B 75 ? 0.8351 0.7896 0.6435 -0.0374 -0.0137 0.0032 75 ARG B C 3123 O O . ARG B 75 ? 0.8093 0.7843 0.6454 -0.0332 -0.0087 0.0029 75 ARG B O 3124 C CB . ARG B 75 ? 0.9571 0.8659 0.7079 -0.0701 -0.0242 -0.0037 75 ARG B CB 3125 C CG . ARG B 75 ? 1.0454 0.9000 0.7554 -0.0785 -0.0238 -0.0182 75 ARG B CG 3126 C CD . ARG B 75 ? 1.1206 0.9485 0.8406 -0.0612 -0.0115 -0.0303 75 ARG B CD 3127 N NE . ARG B 75 ? 1.2601 1.0298 0.9418 -0.0575 -0.0190 -0.0532 75 ARG B NE 3128 C CZ . ARG B 75 ? 1.3219 1.0666 1.0068 -0.0299 -0.0127 -0.0758 75 ARG B CZ 3129 N NH1 . ARG B 75 ? 1.2907 1.0699 1.0178 -0.0099 0.0030 -0.0745 75 ARG B NH1 3130 N NH2 . ARG B 75 ? 1.3942 1.0803 1.0406 -0.0184 -0.0264 -0.1045 75 ARG B NH2 3131 N N . ARG B 76 ? 0.8370 0.8011 0.6428 -0.0282 -0.0300 0.0067 76 ARG B N 3132 C CA . ARG B 76 ? 0.7900 0.7941 0.6318 -0.0057 -0.0426 0.0028 76 ARG B CA 3133 C C . ARG B 76 ? 0.7682 0.7591 0.6267 0.0058 -0.0305 0.0005 76 ARG B C 3134 O O . ARG B 76 ? 0.7075 0.7382 0.5968 0.0157 -0.0275 -0.0066 76 ARG B O 3135 C CB . ARG B 76 ? 0.8016 0.7979 0.6315 0.0123 -0.0725 0.0029 76 ARG B CB 3136 C CG . ARG B 76 ? 0.7959 0.8338 0.6266 0.0075 -0.0918 0.0002 76 ARG B CG 3137 C CD . ARG B 76 ? 0.8421 0.8547 0.6520 0.0306 -0.1292 0.0015 76 ARG B CD 3138 N NE . ARG B 76 ? 0.8819 0.8057 0.6296 0.0135 -0.1283 0.0201 76 ARG B NE 3139 C CZ . ARG B 76 ? 0.9300 0.7920 0.6385 0.0247 -0.1602 0.0319 76 ARG B CZ 3140 N NH1 . ARG B 76 ? 0.9500 0.8179 0.6783 0.0660 -0.2024 0.0216 76 ARG B NH1 3141 N NH2 . ARG B 76 ? 0.9688 0.7628 0.6135 -0.0058 -0.1523 0.0531 76 ARG B NH2 3142 N N . ILE B 77 ? 0.7984 0.7411 0.6336 -0.0010 -0.0238 0.0068 77 ILE B N 3143 C CA . ILE B 77 ? 0.8146 0.7489 0.6673 0.0028 -0.0158 0.0049 77 ILE B CA 3144 C C . ILE B 77 ? 0.7983 0.7541 0.6735 -0.0013 0.0073 -0.0011 77 ILE B C 3145 O O . ILE B 77 ? 0.8230 0.7907 0.7235 0.0063 0.0096 -0.0058 77 ILE B O 3146 C CB . ILE B 77 ? 0.8554 0.7413 0.6759 -0.0150 -0.0182 0.0169 77 ILE B CB 3147 C CG1 . ILE B 77 ? 0.8984 0.7841 0.6919 -0.0412 0.0077 0.0208 77 ILE B CG1 3148 C CG2 . ILE B 77 ? 0.9115 0.7529 0.7000 -0.0069 -0.0544 0.0259 77 ILE B CG2 3149 C CD1 . ILE B 77 ? 0.9752 0.8302 0.7295 -0.0730 0.0096 0.0372 77 ILE B CD1 3150 N N . GLU B 78 ? 0.7978 0.7510 0.6604 -0.0101 0.0180 -0.0029 78 GLU B N 3151 C CA . GLU B 78 ? 0.8125 0.7717 0.6916 -0.0055 0.0266 -0.0097 78 GLU B CA 3152 C C . GLU B 78 ? 0.7701 0.7537 0.6662 -0.0024 0.0154 -0.0048 78 GLU B C 3153 O O . GLU B 78 ? 0.7512 0.7441 0.6651 0.0050 0.0159 -0.0061 78 GLU B O 3154 C CB . GLU B 78 ? 0.8991 0.8324 0.7520 -0.0108 0.0294 -0.0170 78 GLU B CB 3155 C CG . GLU B 78 ? 0.9642 0.8790 0.8222 -0.0031 0.0219 -0.0219 78 GLU B CG 3156 C CD . GLU B 78 ? 1.1079 0.9851 0.9409 0.0050 0.0220 -0.0413 78 GLU B CD 3157 O OE1 . GLU B 78 ? 1.1998 1.0945 1.0453 0.0227 0.0380 -0.0617 78 GLU B OE1 3158 O OE2 . GLU B 78 ? 1.1971 1.0333 0.9979 -0.0072 0.0052 -0.0396 78 GLU B OE2 3159 N N . ASN B 79 ? 0.7411 0.7455 0.6302 -0.0107 0.0050 0.0002 79 ASN B N 3160 C CA . ASN B 79 ? 0.7504 0.8018 0.6517 -0.0171 -0.0011 0.0043 79 ASN B CA 3161 C C . ASN B 79 ? 0.7168 0.8053 0.6432 0.0045 -0.0016 -0.0054 79 ASN B C 3162 O O . ASN B 79 ? 0.6996 0.8159 0.6325 0.0028 0.0000 -0.0044 79 ASN B O 3163 C CB . ASN B 79 ? 0.7829 0.8742 0.6807 -0.0322 -0.0106 0.0067 79 ASN B CB 3164 C CG . ASN B 79 ? 0.7957 0.9612 0.7057 -0.0497 -0.0118 0.0109 79 ASN B CG 3165 O OD1 . ASN B 79 ? 0.8523 1.0060 0.7474 -0.0714 -0.0103 0.0244 79 ASN B OD1 3166 N ND2 . ASN B 79 ? 0.8165 1.0633 0.7507 -0.0408 -0.0169 -0.0014 79 ASN B ND2 3167 N N . LEU B 80 ? 0.7139 0.7925 0.6453 0.0236 -0.0086 -0.0148 80 LEU B N 3168 C CA . LEU B 80 ? 0.6997 0.7888 0.6470 0.0478 -0.0172 -0.0293 80 LEU B CA 3169 C C . LEU B 80 ? 0.6838 0.7550 0.6380 0.0447 -0.0084 -0.0280 80 LEU B C 3170 O O . LEU B 80 ? 0.6650 0.7671 0.6300 0.0546 -0.0109 -0.0375 80 LEU B O 3171 C CB . LEU B 80 ? 0.7442 0.7851 0.6793 0.0611 -0.0351 -0.0324 80 LEU B CB 3172 C CG . LEU B 80 ? 0.7793 0.8170 0.7225 0.0939 -0.0598 -0.0534 80 LEU B CG 3173 C CD1 . LEU B 80 ? 0.8428 0.8111 0.7588 0.1029 -0.0891 -0.0494 80 LEU B CD1 3174 C CD2 . LEU B 80 ? 0.8096 0.8297 0.7597 0.0929 -0.0566 -0.0590 80 LEU B CD2 3175 N N . ASN B 81 ? 0.7035 0.7358 0.6520 0.0320 0.0015 -0.0196 81 ASN B N 3176 C CA . ASN B 81 ? 0.6994 0.7282 0.6636 0.0315 0.0076 -0.0219 81 ASN B CA 3177 C C . ASN B 81 ? 0.7122 0.7608 0.6793 0.0328 0.0065 -0.0186 81 ASN B C 3178 O O . ASN B 81 ? 0.6979 0.7587 0.6779 0.0398 0.0014 -0.0231 81 ASN B O 3179 C CB . ASN B 81 ? 0.7084 0.7182 0.6710 0.0201 0.0214 -0.0201 81 ASN B CB 3180 C CG . ASN B 81 ? 0.6975 0.7255 0.6883 0.0232 0.0263 -0.0279 81 ASN B CG 3181 O OD1 . ASN B 81 ? 0.7300 0.7662 0.7370 0.0202 0.0204 -0.0317 81 ASN B OD1 3182 N ND2 . ASN B 81 ? 0.6916 0.7239 0.6886 0.0317 0.0318 -0.0335 81 ASN B ND2 3183 N N . LYS B 82 ? 0.7403 0.7851 0.6886 0.0214 0.0064 -0.0082 82 LYS B N 3184 C CA . LYS B 82 ? 0.8082 0.8527 0.7426 0.0126 -0.0020 0.0032 82 LYS B CA 3185 C C . LYS B 82 ? 0.8059 0.9050 0.7382 0.0089 -0.0048 0.0037 82 LYS B C 3186 O O . LYS B 82 ? 0.7955 0.9016 0.7225 0.0102 -0.0119 0.0070 82 LYS B O 3187 C CB . LYS B 82 ? 0.8989 0.9125 0.8039 -0.0088 -0.0077 0.0168 82 LYS B CB 3188 C CG . LYS B 82 ? 1.0344 1.0076 0.9124 -0.0193 -0.0265 0.0326 82 LYS B CG 3189 C CD . LYS B 82 ? 1.1688 1.1251 1.0065 -0.0593 -0.0389 0.0548 82 LYS B CD 3190 C CE . LYS B 82 ? 1.3062 1.2057 1.1024 -0.0762 -0.0667 0.0781 82 LYS B CE 3191 N NZ . LYS B 82 ? 1.4180 1.3032 1.1659 -0.1323 -0.0816 0.1076 82 LYS B NZ 3192 N N . LYS B 83 ? 0.8143 0.9599 0.7502 0.0075 -0.0009 -0.0033 83 LYS B N 3193 C CA . LYS B 83 ? 0.8191 1.0415 0.7578 0.0111 -0.0001 -0.0145 83 LYS B CA 3194 C C . LYS B 83 ? 0.7731 0.9986 0.7242 0.0389 -0.0050 -0.0354 83 LYS B C 3195 O O . LYS B 83 ? 0.7548 1.0303 0.6967 0.0397 -0.0054 -0.0429 83 LYS B O 3196 C CB . LYS B 83 ? 0.8516 1.1343 0.8048 0.0188 0.0012 -0.0298 83 LYS B CB 3197 C CG . LYS B 83 ? 0.9185 1.2811 0.8623 -0.0160 0.0074 -0.0188 83 LYS B CG 3198 C CD . LYS B 83 ? 0.9993 1.3055 0.9148 -0.0591 0.0043 0.0139 83 LYS B CD 3199 C CE . LYS B 83 ? 1.0690 1.3486 0.9458 -0.0934 -0.0006 0.0414 83 LYS B CE 3200 N NZ . LYS B 83 ? 1.0922 1.4716 0.9515 -0.1334 0.0060 0.0518 83 LYS B NZ 3201 N N . MET B 84 ? 0.7602 0.9334 0.7264 0.0558 -0.0100 -0.0442 84 MET B N 3202 C CA . MET B 84 ? 0.7496 0.9119 0.7252 0.0742 -0.0203 -0.0627 84 MET B CA 3203 C C . MET B 84 ? 0.7099 0.8655 0.6839 0.0657 -0.0225 -0.0536 84 MET B C 3204 O O . MET B 84 ? 0.7309 0.9124 0.6989 0.0741 -0.0308 -0.0665 84 MET B O 3205 C CB . MET B 84 ? 0.7815 0.8853 0.7660 0.0788 -0.0279 -0.0667 84 MET B CB 3206 C CG . MET B 84 ? 0.8329 0.9170 0.8197 0.0947 -0.0478 -0.0891 84 MET B CG 3207 S SD . MET B 84 ? 0.9041 0.9289 0.9001 0.0711 -0.0536 -0.0798 84 MET B SD 3208 C CE . MET B 84 ? 0.9064 0.9679 0.9239 0.0572 -0.0355 -0.0659 84 MET B CE 3209 N N . GLU B 85 ? 0.8681 1.0297 0.8272 0.1305 -0.0519 -0.0454 85 GLU B N 3210 C CA . GLU B 85 ? 0.8550 1.0239 0.8132 0.1394 -0.0512 -0.0523 85 GLU B CA 3211 C C . GLU B 85 ? 0.8363 0.9633 0.7966 0.1289 -0.0636 -0.0570 85 GLU B C 3212 O O . GLU B 85 ? 0.8121 0.9452 0.7895 0.1213 -0.0566 -0.0536 85 GLU B O 3213 C CB . GLU B 85 ? 0.9078 1.0929 0.8341 0.1750 -0.0575 -0.0661 85 GLU B CB 3214 C CG . GLU B 85 ? 0.9404 1.1849 0.8667 0.1818 -0.0438 -0.0585 85 GLU B CG 3215 C CD . GLU B 85 ? 0.9866 1.3058 0.9054 0.2060 -0.0354 -0.0605 85 GLU B CD 3216 O OE1 . GLU B 85 ? 1.0621 1.3824 0.9456 0.2514 -0.0469 -0.0777 85 GLU B OE1 3217 O OE2 . GLU B 85 ? 0.9806 1.3600 0.9197 0.1802 -0.0189 -0.0441 85 GLU B OE2 3218 N N . ASP B 86 ? 0.8458 0.9327 0.7854 0.1221 -0.0829 -0.0627 86 ASP B N 3219 C CA . ASP B 86 ? 0.8523 0.8999 0.7855 0.1008 -0.0977 -0.0634 86 ASP B CA 3220 C C . ASP B 86 ? 0.7826 0.8582 0.7586 0.0780 -0.0858 -0.0487 86 ASP B C 3221 O O . ASP B 86 ? 0.7761 0.8379 0.7592 0.0674 -0.0877 -0.0476 86 ASP B O 3222 C CB . ASP B 86 ? 0.9235 0.9309 0.8185 0.0824 -0.1233 -0.0672 86 ASP B CB 3223 C CG . ASP B 86 ? 1.0418 0.9708 0.8648 0.0989 -0.1473 -0.0842 86 ASP B CG 3224 O OD1 . ASP B 86 ? 1.1215 1.0100 0.9227 0.1057 -0.1532 -0.0895 86 ASP B OD1 3225 O OD2 . ASP B 86 ? 1.1102 1.0102 0.8889 0.1091 -0.1619 -0.0929 86 ASP B OD2 3226 N N . GLY B 87 ? 0.7424 0.8527 0.7378 0.0761 -0.0751 -0.0382 87 GLY B N 3227 C CA . GLY B 87 ? 0.7166 0.8489 0.7365 0.0680 -0.0653 -0.0257 87 GLY B CA 3228 C C . GLY B 87 ? 0.6987 0.8218 0.7304 0.0687 -0.0521 -0.0234 87 GLY B C 3229 O O . GLY B 87 ? 0.6870 0.8100 0.7321 0.0594 -0.0520 -0.0190 87 GLY B O 3230 N N . PHE B 88 ? 0.6938 0.8182 0.7189 0.0765 -0.0420 -0.0250 88 PHE B N 3231 C CA . PHE B 88 ? 0.6761 0.8019 0.7081 0.0692 -0.0311 -0.0211 88 PHE B CA 3232 C C . PHE B 88 ? 0.6753 0.7971 0.7152 0.0701 -0.0376 -0.0302 88 PHE B C 3233 O O . PHE B 88 ? 0.6675 0.7865 0.7196 0.0604 -0.0327 -0.0263 88 PHE B O 3234 C CB . PHE B 88 ? 0.6816 0.8294 0.7005 0.0669 -0.0202 -0.0164 88 PHE B CB 3235 C CG . PHE B 88 ? 0.7030 0.8312 0.6982 0.0595 -0.0135 -0.0036 88 PHE B CG 3236 C CD1 . PHE B 88 ? 0.7315 0.8204 0.7097 0.0514 -0.0105 0.0059 88 PHE B CD1 3237 C CD2 . PHE B 88 ? 0.7324 0.8715 0.7098 0.0652 -0.0120 -0.0015 88 PHE B CD2 3238 C CE1 . PHE B 88 ? 0.7822 0.8297 0.7149 0.0522 -0.0080 0.0167 88 PHE B CE1 3239 C CE2 . PHE B 88 ? 0.7781 0.8842 0.7192 0.0605 -0.0079 0.0108 88 PHE B CE2 3240 C CZ . PHE B 88 ? 0.8126 0.8660 0.7255 0.0555 -0.0070 0.0196 88 PHE B CZ 3241 N N . LEU B 89 ? 0.6949 0.8054 0.7168 0.0849 -0.0507 -0.0427 89 LEU B N 3242 C CA . LEU B 89 ? 0.7298 0.8157 0.7389 0.0925 -0.0610 -0.0522 89 LEU B CA 3243 C C . LEU B 89 ? 0.6996 0.7575 0.7180 0.0692 -0.0689 -0.0469 89 LEU B C 3244 O O . LEU B 89 ? 0.6748 0.7256 0.6998 0.0667 -0.0677 -0.0471 89 LEU B O 3245 C CB . LEU B 89 ? 0.8140 0.8632 0.7746 0.1175 -0.0796 -0.0674 89 LEU B CB 3246 C CG . LEU B 89 ? 0.8786 0.9663 0.8226 0.1517 -0.0738 -0.0748 89 LEU B CG 3247 C CD1 . LEU B 89 ? 0.9684 0.9967 0.8454 0.1845 -0.0972 -0.0923 89 LEU B CD1 3248 C CD2 . LEU B 89 ? 0.8659 1.0196 0.8275 0.1655 -0.0581 -0.0729 89 LEU B CD2 3249 N N . ASP B 90 ? 0.6959 0.7503 0.7146 0.0517 -0.0771 -0.0410 90 ASP B N 3250 C CA . ASP B 90 ? 0.6979 0.7539 0.7282 0.0263 -0.0836 -0.0319 90 ASP B CA 3251 C C . ASP B 90 ? 0.6396 0.7249 0.7035 0.0273 -0.0657 -0.0225 90 ASP B C 3252 O O . ASP B 90 ? 0.6251 0.7082 0.6980 0.0158 -0.0676 -0.0187 90 ASP B O 3253 C CB . ASP B 90 ? 0.7099 0.7893 0.7365 0.0074 -0.0943 -0.0245 90 ASP B CB 3254 C CG . ASP B 90 ? 0.7991 0.8310 0.7773 -0.0069 -0.1191 -0.0323 90 ASP B CG 3255 O OD1 . ASP B 90 ? 0.8491 0.8163 0.7873 0.0003 -0.1310 -0.0436 90 ASP B OD1 3256 O OD2 . ASP B 90 ? 0.8501 0.9048 0.8204 -0.0230 -0.1288 -0.0276 90 ASP B OD2 3257 N N . VAL B 91 ? 0.6111 0.7132 0.6820 0.0401 -0.0507 -0.0184 91 VAL B N 3258 C CA . VAL B 91 ? 0.5914 0.6964 0.6704 0.0425 -0.0379 -0.0102 91 VAL B CA 3259 C C . VAL B 91 ? 0.5821 0.6751 0.6670 0.0374 -0.0329 -0.0137 91 VAL B C 3260 O O . VAL B 91 ? 0.5869 0.6763 0.6806 0.0327 -0.0307 -0.0098 91 VAL B O 3261 C CB . VAL B 91 ? 0.5948 0.6929 0.6540 0.0533 -0.0278 -0.0045 91 VAL B CB 3262 C CG1 . VAL B 91 ? 0.6008 0.6714 0.6429 0.0534 -0.0193 0.0026 91 VAL B CG1 3263 C CG2 . VAL B 91 ? 0.6049 0.7227 0.6567 0.0664 -0.0319 -0.0002 91 VAL B CG2 3264 N N . TRP B 92 ? 0.5752 0.6734 0.6544 0.0414 -0.0313 -0.0208 92 TRP B N 3265 C CA . TRP B 92 ? 0.5700 0.6784 0.6546 0.0395 -0.0266 -0.0236 92 TRP B CA 3266 C C . TRP B 92 ? 0.5796 0.6714 0.6650 0.0450 -0.0375 -0.0315 92 TRP B C 3267 O O . TRP B 92 ? 0.5804 0.6767 0.6743 0.0424 -0.0341 -0.0314 92 TRP B O 3268 C CB . TRP B 92 ? 0.5742 0.7205 0.6503 0.0465 -0.0212 -0.0267 92 TRP B CB 3269 C CG . TRP B 92 ? 0.5867 0.7417 0.6526 0.0272 -0.0109 -0.0145 92 TRP B CG 3270 C CD1 . TRP B 92 ? 0.6020 0.7632 0.6529 0.0282 -0.0090 -0.0111 92 TRP B CD1 3271 C CD2 . TRP B 92 ? 0.5953 0.7365 0.6501 0.0010 -0.0044 -0.0032 92 TRP B CD2 3272 N NE1 . TRP B 92 ? 0.6339 0.7814 0.6604 0.0025 -0.0021 0.0027 92 TRP B NE1 3273 C CE2 . TRP B 92 ? 0.6305 0.7594 0.6536 -0.0158 -0.0005 0.0076 92 TRP B CE2 3274 C CE3 . TRP B 92 ? 0.5963 0.7252 0.6555 -0.0113 -0.0034 -0.0011 92 TRP B CE3 3275 C CZ2 . TRP B 92 ? 0.6745 0.7650 0.6576 -0.0479 0.0014 0.0208 92 TRP B CZ2 3276 C CZ3 . TRP B 92 ? 0.6275 0.7266 0.6543 -0.0407 -0.0004 0.0108 92 TRP B CZ3 3277 C CH2 . TRP B 92 ? 0.6769 0.7499 0.6598 -0.0605 0.0006 0.0219 92 TRP B CH2 3278 N N . THR B 93 ? 0.6110 0.6755 0.6780 0.0493 -0.0527 -0.0373 93 THR B N 3279 C CA . THR B 93 ? 0.6410 0.6659 0.6874 0.0481 -0.0680 -0.0427 93 THR B CA 3280 C C . THR B 93 ? 0.6285 0.6568 0.6975 0.0243 -0.0666 -0.0316 93 THR B C 3281 O O . THR B 93 ? 0.6446 0.6593 0.7132 0.0227 -0.0684 -0.0324 93 THR B O 3282 C CB . THR B 93 ? 0.6959 0.6723 0.6971 0.0472 -0.0897 -0.0492 93 THR B CB 3283 O OG1 . THR B 93 ? 0.7346 0.7075 0.7073 0.0804 -0.0913 -0.0617 93 THR B OG1 3284 C CG2 . THR B 93 ? 0.7535 0.6656 0.7126 0.0363 -0.1102 -0.0518 93 THR B CG2 3285 N N . TYR B 94 ? 0.5989 0.6529 0.6844 0.0118 -0.0633 -0.0213 94 TYR B N 3286 C CA . TYR B 94 ? 0.5747 0.6532 0.6798 -0.0012 -0.0604 -0.0097 94 TYR B CA 3287 C C . TYR B 94 ? 0.5599 0.6413 0.6802 0.0086 -0.0457 -0.0088 94 TYR B C 3288 O O . TYR B 94 ? 0.5580 0.6367 0.6854 0.0022 -0.0468 -0.0066 94 TYR B O 3289 C CB . TYR B 94 ? 0.5636 0.6844 0.6759 -0.0004 -0.0582 -0.0002 94 TYR B CB 3290 C CG . TYR B 94 ? 0.5570 0.7199 0.6840 0.0041 -0.0520 0.0111 94 TYR B CG 3291 C CD1 . TYR B 94 ? 0.5566 0.7116 0.6797 0.0291 -0.0379 0.0122 94 TYR B CD1 3292 C CD2 . TYR B 94 ? 0.5563 0.7666 0.6899 -0.0171 -0.0621 0.0219 94 TYR B CD2 3293 C CE1 . TYR B 94 ? 0.5492 0.7355 0.6715 0.0455 -0.0338 0.0205 94 TYR B CE1 3294 C CE2 . TYR B 94 ? 0.5457 0.8128 0.6909 -0.0043 -0.0555 0.0325 94 TYR B CE2 3295 C CZ . TYR B 94 ? 0.5438 0.7954 0.6818 0.0336 -0.0412 0.0302 94 TYR B CZ 3296 O OH . TYR B 94 ? 0.5459 0.8456 0.6815 0.0583 -0.0363 0.0387 94 TYR B OH 3297 N N . ASN B 95 ? 0.5682 0.6501 0.6857 0.0190 -0.0341 -0.0094 95 ASN B N 3298 C CA . ASN B 95 ? 0.5644 0.6383 0.6812 0.0183 -0.0239 -0.0075 95 ASN B CA 3299 C C . ASN B 95 ? 0.5597 0.6340 0.6856 0.0145 -0.0254 -0.0136 95 ASN B C 3300 O O . ASN B 95 ? 0.5502 0.6205 0.6824 0.0105 -0.0228 -0.0107 95 ASN B O 3301 C CB . ASN B 95 ? 0.5793 0.6472 0.6772 0.0158 -0.0162 -0.0059 95 ASN B CB 3302 C CG . ASN B 95 ? 0.6174 0.6652 0.6897 0.0244 -0.0141 0.0014 95 ASN B CG 3303 O OD1 . ASN B 95 ? 0.6300 0.6834 0.7026 0.0390 -0.0168 0.0048 95 ASN B OD1 3304 N ND2 . ASN B 95 ? 0.6645 0.6943 0.7079 0.0167 -0.0100 0.0049 95 ASN B ND2 3305 N N . ALA B 96 ? 0.5699 0.6494 0.6899 0.0224 -0.0303 -0.0226 96 ALA B N 3306 C CA . ALA B 96 ? 0.5836 0.6683 0.7022 0.0307 -0.0323 -0.0297 96 ALA B CA 3307 C C . ALA B 96 ? 0.5919 0.6453 0.7073 0.0272 -0.0426 -0.0296 96 ALA B C 3308 O O . ALA B 96 ? 0.5747 0.6313 0.6981 0.0263 -0.0398 -0.0292 96 ALA B O 3309 C CB . ALA B 96 ? 0.6072 0.7040 0.7050 0.0548 -0.0376 -0.0407 96 ALA B CB 3310 N N . GLU B 97 ? 0.6139 0.6391 0.7133 0.0197 -0.0559 -0.0282 97 GLU B N 3311 C CA . GLU B 97 ? 0.6439 0.6364 0.7275 0.0052 -0.0695 -0.0249 97 GLU B CA 3312 C C . GLU B 97 ? 0.6124 0.6349 0.7267 -0.0102 -0.0613 -0.0128 97 GLU B C 3313 O O . GLU B 97 ? 0.6185 0.6287 0.7300 -0.0168 -0.0652 -0.0104 97 GLU B O 3314 C CB . GLU B 97 ? 0.6871 0.6434 0.7346 -0.0129 -0.0894 -0.0229 97 GLU B CB 3315 C CG . GLU B 97 ? 0.7647 0.6547 0.7521 0.0079 -0.1063 -0.0373 97 GLU B CG 3316 C CD . GLU B 97 ? 0.8405 0.6804 0.7778 -0.0117 -0.1284 -0.0369 97 GLU B CD 3317 O OE1 . GLU B 97 ? 0.8535 0.7276 0.8112 -0.0465 -0.1300 -0.0238 97 GLU B OE1 3318 O OE2 . GLU B 97 ? 0.9330 0.7002 0.8025 0.0106 -0.1459 -0.0499 97 GLU B OE2 3319 N N . LEU B 98 ? 0.5904 0.6488 0.7257 -0.0096 -0.0506 -0.0057 98 LEU B N 3320 C CA . LEU B 98 ? 0.5602 0.6483 0.7122 -0.0110 -0.0437 0.0045 98 LEU B CA 3321 C C . LEU B 98 ? 0.5407 0.6186 0.6984 -0.0013 -0.0333 0.0012 98 LEU B C 3322 O O . LEU B 98 ? 0.5425 0.6283 0.7070 -0.0028 -0.0322 0.0059 98 LEU B O 3323 C CB . LEU B 98 ? 0.5638 0.6822 0.7169 0.0007 -0.0377 0.0108 98 LEU B CB 3324 C CG . LEU B 98 ? 0.5704 0.7270 0.7274 0.0135 -0.0328 0.0209 98 LEU B CG 3325 C CD1 . LEU B 98 ? 0.5673 0.7763 0.7356 -0.0086 -0.0429 0.0323 98 LEU B CD1 3326 C CD2 . LEU B 98 ? 0.5782 0.7478 0.7172 0.0416 -0.0269 0.0236 98 LEU B CD2 3327 N N . LEU B 99 ? 0.5337 0.6006 0.6858 0.0044 -0.0266 -0.0054 99 LEU B N 3328 C CA . LEU B 99 ? 0.5382 0.5999 0.6889 0.0028 -0.0193 -0.0069 99 LEU B CA 3329 C C . LEU B 99 ? 0.5300 0.5938 0.6897 0.0026 -0.0234 -0.0115 99 LEU B C 3330 O O . LEU B 99 ? 0.5275 0.5901 0.6914 0.0004 -0.0205 -0.0093 99 LEU B O 3331 C CB . LEU B 99 ? 0.5642 0.6310 0.7035 -0.0031 -0.0141 -0.0098 99 LEU B CB 3332 C CG . LEU B 99 ? 0.5940 0.6619 0.7225 -0.0189 -0.0091 -0.0080 99 LEU B CG 3333 C CD1 . LEU B 99 ? 0.6324 0.6551 0.7329 -0.0212 -0.0084 -0.0014 99 LEU B CD1 3334 C CD2 . LEU B 99 ? 0.6166 0.7110 0.7326 -0.0357 -0.0059 -0.0067 99 LEU B CD2 3335 N N . VAL B 100 ? 0.5222 0.5804 0.6741 0.0094 -0.0317 -0.0186 100 VAL B N 3336 C CA . VAL B 100 ? 0.5135 0.5581 0.6562 0.0172 -0.0388 -0.0237 100 VAL B CA 3337 C C . VAL B 100 ? 0.4991 0.5273 0.6440 0.0035 -0.0444 -0.0152 100 VAL B C 3338 O O . VAL B 100 ? 0.4745 0.5033 0.6240 0.0053 -0.0426 -0.0151 100 VAL B O 3339 C CB . VAL B 100 ? 0.5462 0.5642 0.6546 0.0363 -0.0515 -0.0339 100 VAL B CB 3340 C CG1 . VAL B 100 ? 0.5761 0.5505 0.6517 0.0469 -0.0645 -0.0380 100 VAL B CG1 3341 C CG2 . VAL B 100 ? 0.5440 0.6065 0.6533 0.0569 -0.0437 -0.0421 100 VAL B CG2 3342 N N . LEU B 101 ? 0.4915 0.5171 0.6330 -0.0122 -0.0514 -0.0065 101 LEU B N 3343 C CA . LEU B 101 ? 0.4949 0.5299 0.6388 -0.0316 -0.0569 0.0059 101 LEU B CA 3344 C C . LEU B 101 ? 0.4758 0.5458 0.6452 -0.0233 -0.0434 0.0110 101 LEU B C 3345 O O . LEU B 101 ? 0.4879 0.5583 0.6598 -0.0264 -0.0439 0.0143 101 LEU B O 3346 C CB . LEU B 101 ? 0.4955 0.5539 0.6351 -0.0538 -0.0654 0.0174 101 LEU B CB 3347 C CG . LEU B 101 ? 0.5581 0.5669 0.6545 -0.0755 -0.0862 0.0166 101 LEU B CG 3348 C CD1 . LEU B 101 ? 0.5723 0.6259 0.6685 -0.1077 -0.0947 0.0317 101 LEU B CD1 3349 C CD2 . LEU B 101 ? 0.6124 0.5579 0.6655 -0.0893 -0.1024 0.0168 101 LEU B CD2 3350 N N . MET B 102 ? 0.4694 0.5580 0.6463 -0.0102 -0.0332 0.0114 102 MET B N 3351 C CA . MET B 102 ? 0.4747 0.5758 0.6528 0.0044 -0.0244 0.0150 102 MET B CA 3352 C C . MET B 102 ? 0.4797 0.5565 0.6562 0.0058 -0.0202 0.0081 102 MET B C 3353 O O . MET B 102 ? 0.4860 0.5687 0.6633 0.0110 -0.0183 0.0115 102 MET B O 3354 C CB . MET B 102 ? 0.5085 0.6030 0.6691 0.0215 -0.0185 0.0146 102 MET B CB 3355 C CG . MET B 102 ? 0.5279 0.6647 0.6889 0.0295 -0.0210 0.0229 102 MET B CG 3356 S SD . MET B 102 ? 0.6041 0.7132 0.7261 0.0604 -0.0155 0.0211 102 MET B SD 3357 C CE . MET B 102 ? 0.6090 0.8002 0.7298 0.0891 -0.0168 0.0332 102 MET B CE 3358 N N . GLU B 103 ? 0.4764 0.5379 0.6500 0.0016 -0.0191 -0.0007 103 GLU B N 3359 C CA . GLU B 103 ? 0.4982 0.5558 0.6697 -0.0015 -0.0156 -0.0058 103 GLU B CA 3360 C C . GLU B 103 ? 0.4903 0.5535 0.6715 0.0010 -0.0202 -0.0087 103 GLU B C 3361 O O . GLU B 103 ? 0.4845 0.5514 0.6673 0.0007 -0.0177 -0.0101 103 GLU B O 3362 C CB . GLU B 103 ? 0.5295 0.5954 0.6931 -0.0101 -0.0127 -0.0108 103 GLU B CB 3363 C CG . GLU B 103 ? 0.5824 0.6231 0.7189 -0.0185 -0.0098 -0.0061 103 GLU B CG 3364 C CD . GLU B 103 ? 0.6417 0.6429 0.7456 -0.0222 -0.0098 -0.0026 103 GLU B CD 3365 O OE1 . GLU B 103 ? 0.6444 0.6520 0.7526 -0.0293 -0.0102 -0.0044 103 GLU B OE1 3366 O OE2 . GLU B 103 ? 0.7373 0.6943 0.8018 -0.0136 -0.0111 0.0012 103 GLU B OE2 3367 N N . ASN B 104 ? 0.5050 0.5581 0.6814 0.0029 -0.0292 -0.0094 104 ASN B N 3368 C CA . ASN B 104 ? 0.5238 0.5591 0.6894 0.0057 -0.0375 -0.0103 104 ASN B CA 3369 C C . ASN B 104 ? 0.5213 0.5646 0.6968 -0.0040 -0.0362 0.0003 104 ASN B C 3370 O O . ASN B 104 ? 0.5049 0.5461 0.6805 0.0002 -0.0358 -0.0008 104 ASN B O 3371 C CB . ASN B 104 ? 0.5622 0.5574 0.6956 0.0036 -0.0529 -0.0110 104 ASN B CB 3372 C CG . ASN B 104 ? 0.5859 0.5690 0.6957 0.0287 -0.0568 -0.0246 104 ASN B CG 3373 O OD1 . ASN B 104 ? 0.5548 0.5772 0.6781 0.0450 -0.0474 -0.0319 104 ASN B OD1 3374 N ND2 . ASN B 104 ? 0.6341 0.5674 0.7016 0.0312 -0.0722 -0.0274 104 ASN B ND2 3375 N N . GLU B 105 ? 0.5302 0.5938 0.7128 -0.0132 -0.0354 0.0109 105 GLU B N 3376 C CA . GLU B 105 ? 0.5343 0.6274 0.7255 -0.0154 -0.0329 0.0219 105 GLU B CA 3377 C C . GLU B 105 ? 0.4925 0.5851 0.6872 0.0020 -0.0230 0.0166 105 GLU B C 3378 O O . GLU B 105 ? 0.4675 0.5658 0.6646 0.0038 -0.0225 0.0193 105 GLU B O 3379 C CB . GLU B 105 ? 0.5857 0.7244 0.7818 -0.0176 -0.0323 0.0336 105 GLU B CB 3380 C CG . GLU B 105 ? 0.6608 0.8549 0.8628 -0.0241 -0.0334 0.0493 105 GLU B CG 3381 C CD . GLU B 105 ? 0.7626 1.0210 0.9670 -0.0401 -0.0387 0.0643 105 GLU B CD 3382 O OE1 . GLU B 105 ? 0.8865 1.1717 1.0923 -0.0161 -0.0325 0.0626 105 GLU B OE1 3383 O OE2 . GLU B 105 ? 0.8290 1.1084 1.0261 -0.0794 -0.0509 0.0786 105 GLU B OE2 3384 N N . ARG B 106 ? 0.4904 0.5686 0.6764 0.0106 -0.0172 0.0100 106 ARG B N 3385 C CA . ARG B 106 ? 0.5287 0.5872 0.6983 0.0180 -0.0127 0.0058 106 ARG B CA 3386 C C . ARG B 106 ? 0.4942 0.5505 0.6708 0.0089 -0.0132 -0.0010 106 ARG B C 3387 O O . ARG B 106 ? 0.5012 0.5515 0.6703 0.0119 -0.0122 -0.0015 106 ARG B O 3388 C CB . ARG B 106 ? 0.6024 0.6289 0.7417 0.0188 -0.0109 0.0027 106 ARG B CB 3389 C CG . ARG B 106 ? 0.6834 0.7098 0.8034 0.0409 -0.0105 0.0086 106 ARG B CG 3390 C CD . ARG B 106 ? 0.8250 0.7893 0.8861 0.0501 -0.0119 0.0060 106 ARG B CD 3391 N NE . ARG B 106 ? 0.9400 0.8707 0.9520 0.0817 -0.0142 0.0067 106 ARG B NE 3392 C CZ . ARG B 106 ? 1.0460 0.9074 1.0034 0.0773 -0.0196 0.0023 106 ARG B CZ 3393 N NH1 . ARG B 106 ? 1.0766 0.9091 1.0266 0.0347 -0.0225 -0.0008 106 ARG B NH1 3394 N NH2 . ARG B 106 ? 1.1645 0.9887 1.0661 0.1165 -0.0236 0.0017 106 ARG B NH2 3395 N N . THR B 107 ? 0.4666 0.5320 0.6525 0.0036 -0.0156 -0.0067 107 THR B N 3396 C CA . THR B 107 ? 0.4380 0.5186 0.6273 0.0048 -0.0165 -0.0134 107 THR B CA 3397 C C . THR B 107 ? 0.4361 0.5115 0.6287 0.0125 -0.0200 -0.0107 107 THR B C 3398 O O . THR B 107 ? 0.4258 0.5106 0.6194 0.0140 -0.0184 -0.0131 107 THR B O 3399 C CB . THR B 107 ? 0.4337 0.5326 0.6215 0.0127 -0.0194 -0.0208 107 THR B CB 3400 O OG1 . THR B 107 ? 0.4252 0.5427 0.6107 0.0002 -0.0150 -0.0217 107 THR B OG1 3401 C CG2 . THR B 107 ? 0.4312 0.5595 0.6168 0.0273 -0.0212 -0.0280 107 THR B CG2 3402 N N . LEU B 108 ? 0.4337 0.4943 0.6229 0.0115 -0.0263 -0.0039 108 LEU B N 3403 C CA . LEU B 108 ? 0.4523 0.5042 0.6359 0.0105 -0.0315 0.0024 108 LEU B CA 3404 C C . LEU B 108 ? 0.4419 0.5149 0.6371 0.0111 -0.0246 0.0088 108 LEU B C 3405 O O . LEU B 108 ? 0.4262 0.5000 0.6208 0.0158 -0.0246 0.0082 108 LEU B O 3406 C CB . LEU B 108 ? 0.4790 0.5087 0.6439 -0.0055 -0.0431 0.0127 108 LEU B CB 3407 C CG . LEU B 108 ? 0.5270 0.5101 0.6574 -0.0005 -0.0553 0.0051 108 LEU B CG 3408 C CD1 . LEU B 108 ? 0.5828 0.5258 0.6765 -0.0287 -0.0720 0.0180 108 LEU B CD1 3409 C CD2 . LEU B 108 ? 0.5517 0.5121 0.6581 0.0271 -0.0592 -0.0071 108 LEU B CD2 3410 N N . ASP B 109 ? 0.4453 0.5335 0.6434 0.0132 -0.0198 0.0140 109 ASP B N 3411 C CA . ASP B 109 ? 0.4471 0.5493 0.6402 0.0272 -0.0147 0.0180 109 ASP B CA 3412 C C . ASP B 109 ? 0.4544 0.5297 0.6327 0.0324 -0.0122 0.0073 109 ASP B C 3413 O O . ASP B 109 ? 0.4851 0.5596 0.6531 0.0434 -0.0111 0.0082 109 ASP B O 3414 C CB . ASP B 109 ? 0.4705 0.5880 0.6529 0.0416 -0.0119 0.0230 109 ASP B CB 3415 C CG . ASP B 109 ? 0.4943 0.6651 0.6907 0.0327 -0.0149 0.0378 109 ASP B CG 3416 O OD1 . ASP B 109 ? 0.4718 0.6694 0.6774 0.0161 -0.0191 0.0484 109 ASP B OD1 3417 O OD2 . ASP B 109 ? 0.5200 0.7077 0.7126 0.0391 -0.0142 0.0404 109 ASP B OD2 3418 N N . PHE B 110 ? 0.4380 0.4969 0.6108 0.0209 -0.0124 -0.0012 110 PHE B N 3419 C CA . PHE B 110 ? 0.4384 0.4799 0.5904 0.0105 -0.0130 -0.0082 110 PHE B CA 3420 C C . PHE B 110 ? 0.4297 0.4942 0.5966 0.0100 -0.0139 -0.0113 110 PHE B C 3421 O O . PHE B 110 ? 0.4408 0.4938 0.5906 0.0080 -0.0151 -0.0133 110 PHE B O 3422 C CB . PHE B 110 ? 0.4405 0.4837 0.5863 -0.0095 -0.0136 -0.0121 110 PHE B CB 3423 C CG . PHE B 110 ? 0.4536 0.5007 0.5787 -0.0360 -0.0165 -0.0157 110 PHE B CG 3424 C CD1 . PHE B 110 ? 0.5061 0.5000 0.5814 -0.0487 -0.0219 -0.0151 110 PHE B CD1 3425 C CD2 . PHE B 110 ? 0.4330 0.5395 0.5780 -0.0488 -0.0159 -0.0190 110 PHE B CD2 3426 C CE1 . PHE B 110 ? 0.5364 0.5335 0.5833 -0.0871 -0.0282 -0.0157 110 PHE B CE1 3427 C CE2 . PHE B 110 ? 0.4571 0.5930 0.5842 -0.0818 -0.0194 -0.0190 110 PHE B CE2 3428 C CZ . PHE B 110 ? 0.5027 0.5821 0.5810 -0.1080 -0.0263 -0.0163 110 PHE B CZ 3429 N N . HIS B 111 ? 0.4206 0.5081 0.6087 0.0154 -0.0152 -0.0123 111 HIS B N 3430 C CA . HIS B 111 ? 0.4184 0.5214 0.6121 0.0243 -0.0173 -0.0149 111 HIS B CA 3431 C C . HIS B 111 ? 0.4306 0.5232 0.6239 0.0312 -0.0172 -0.0073 111 HIS B C 3432 O O . HIS B 111 ? 0.4396 0.5392 0.6308 0.0351 -0.0171 -0.0097 111 HIS B O 3433 C CB . HIS B 111 ? 0.4271 0.5295 0.6184 0.0377 -0.0228 -0.0173 111 HIS B CB 3434 C CG . HIS B 111 ? 0.4237 0.5572 0.6132 0.0435 -0.0230 -0.0263 111 HIS B CG 3435 N ND1 . HIS B 111 ? 0.4105 0.5980 0.6033 0.0439 -0.0209 -0.0327 111 HIS B ND1 3436 C CD2 . HIS B 111 ? 0.4269 0.5574 0.6095 0.0502 -0.0254 -0.0291 111 HIS B CD2 3437 C CE1 . HIS B 111 ? 0.4179 0.6464 0.6086 0.0517 -0.0211 -0.0379 111 HIS B CE1 3438 N NE2 . HIS B 111 ? 0.4241 0.6127 0.6073 0.0587 -0.0237 -0.0368 111 HIS B NE2 3439 N N . ASP B 112 ? 0.4198 0.5081 0.6151 0.0313 -0.0174 0.0031 112 ASP B N 3440 C CA . ASP B 112 ? 0.4158 0.5175 0.6111 0.0371 -0.0164 0.0134 112 ASP B CA 3441 C C . ASP B 112 ? 0.4330 0.5284 0.6133 0.0499 -0.0125 0.0084 112 ASP B C 3442 O O . ASP B 112 ? 0.4594 0.5605 0.6361 0.0581 -0.0122 0.0092 112 ASP B O 3443 C CB . ASP B 112 ? 0.4182 0.5433 0.6170 0.0321 -0.0169 0.0272 112 ASP B CB 3444 C CG . ASP B 112 ? 0.4358 0.5996 0.6366 0.0301 -0.0176 0.0430 112 ASP B CG 3445 O OD1 . ASP B 112 ? 0.4568 0.6158 0.6552 0.0329 -0.0182 0.0427 112 ASP B OD1 3446 O OD2 . ASP B 112 ? 0.4315 0.6419 0.6358 0.0246 -0.0177 0.0571 112 ASP B OD2 3447 N N . SER B 113 ? 0.4402 0.5113 0.6000 0.0512 -0.0118 0.0030 113 SER B N 3448 C CA . SER B 113 ? 0.4675 0.5016 0.5852 0.0627 -0.0135 -0.0021 113 SER B CA 3449 C C . SER B 113 ? 0.4838 0.5032 0.5907 0.0468 -0.0172 -0.0104 113 SER B C 3450 O O . SER B 113 ? 0.5036 0.5026 0.5827 0.0582 -0.0199 -0.0124 113 SER B O 3451 C CB . SER B 113 ? 0.4943 0.4838 0.5739 0.0617 -0.0161 -0.0053 113 SER B CB 3452 O OG . SER B 113 ? 0.5521 0.4750 0.5666 0.0649 -0.0233 -0.0115 113 SER B OG 3453 N N . ASN B 114 ? 0.4672 0.5053 0.5922 0.0227 -0.0180 -0.0150 114 ASN B N 3454 C CA . ASN B 114 ? 0.4707 0.5223 0.5897 0.0045 -0.0217 -0.0211 114 ASN B CA 3455 C C . ASN B 114 ? 0.4528 0.5295 0.5913 0.0215 -0.0203 -0.0206 114 ASN B C 3456 O O . ASN B 114 ? 0.4669 0.5404 0.5876 0.0149 -0.0240 -0.0245 114 ASN B O 3457 C CB . ASN B 114 ? 0.4531 0.5521 0.5923 -0.0153 -0.0216 -0.0244 114 ASN B CB 3458 C CG . ASN B 114 ? 0.4783 0.5576 0.5928 -0.0417 -0.0240 -0.0236 114 ASN B CG 3459 O OD1 . ASN B 114 ? 0.5361 0.5537 0.5998 -0.0569 -0.0301 -0.0226 114 ASN B OD1 3460 N ND2 . ASN B 114 ? 0.4498 0.5731 0.5887 -0.0449 -0.0212 -0.0241 114 ASN B ND2 3461 N N . VAL B 115 ? 0.4223 0.5171 0.5884 0.0388 -0.0170 -0.0145 115 VAL B N 3462 C CA . VAL B 115 ? 0.4148 0.5244 0.5905 0.0520 -0.0171 -0.0115 115 VAL B CA 3463 C C . VAL B 115 ? 0.4366 0.5343 0.5967 0.0650 -0.0157 -0.0067 115 VAL B C 3464 O O . VAL B 115 ? 0.4323 0.5327 0.5848 0.0707 -0.0169 -0.0093 115 VAL B O 3465 C CB . VAL B 115 ? 0.4116 0.5241 0.5994 0.0578 -0.0186 -0.0033 115 VAL B CB 3466 C CG1 . VAL B 115 ? 0.4281 0.5432 0.6127 0.0667 -0.0205 0.0032 115 VAL B CG1 3467 C CG2 . VAL B 115 ? 0.4243 0.5407 0.6121 0.0596 -0.0222 -0.0107 115 VAL B CG2 3468 N N . LYS B 116 ? 0.4515 0.5441 0.6043 0.0748 -0.0134 0.0005 116 LYS B N 3469 C CA . LYS B 116 ? 0.4912 0.5832 0.6201 0.0998 -0.0122 0.0046 116 LYS B CA 3470 C C . LYS B 116 ? 0.5371 0.5782 0.6184 0.1047 -0.0179 -0.0074 116 LYS B C 3471 O O . LYS B 116 ? 0.5597 0.5981 0.6215 0.1237 -0.0191 -0.0080 116 LYS B O 3472 C CB . LYS B 116 ? 0.5197 0.6225 0.6394 0.1158 -0.0099 0.0117 116 LYS B CB 3473 C CG . LYS B 116 ? 0.5754 0.6818 0.6554 0.1571 -0.0095 0.0137 116 LYS B CG 3474 C CD . LYS B 116 ? 0.5899 0.7678 0.6925 0.1695 -0.0051 0.0274 116 LYS B CD 3475 C CE . LYS B 116 ? 0.6441 0.8774 0.7234 0.2142 -0.0020 0.0366 116 LYS B CE 3476 N NZ . LYS B 116 ? 0.6257 0.9645 0.7496 0.1970 0.0026 0.0593 116 LYS B NZ 3477 N N . ASN B 117 ? 0.5636 0.5610 0.6183 0.0833 -0.0233 -0.0156 117 ASN B N 3478 C CA . ASN B 117 ? 0.6398 0.5712 0.6296 0.0735 -0.0340 -0.0248 117 ASN B CA 3479 C C . ASN B 117 ? 0.6340 0.5875 0.6357 0.0528 -0.0370 -0.0294 117 ASN B C 3480 O O . ASN B 117 ? 0.6823 0.5939 0.6352 0.0556 -0.0453 -0.0345 117 ASN B O 3481 C CB . ASN B 117 ? 0.6752 0.5549 0.6251 0.0428 -0.0414 -0.0283 117 ASN B CB 3482 C CG . ASN B 117 ? 0.7115 0.5478 0.6242 0.0715 -0.0415 -0.0259 117 ASN B CG 3483 O OD1 . ASN B 117 ? 0.7250 0.5564 0.6164 0.1184 -0.0398 -0.0239 117 ASN B OD1 3484 N ND2 . ASN B 117 ? 0.7291 0.5445 0.6324 0.0470 -0.0436 -0.0255 117 ASN B ND2 3485 N N . LEU B 118 ? 0.5828 0.6003 0.6413 0.0373 -0.0318 -0.0281 118 LEU B N 3486 C CA . LEU B 118 ? 0.5867 0.6420 0.6589 0.0262 -0.0340 -0.0322 118 LEU B CA 3487 C C . LEU B 118 ? 0.5867 0.6468 0.6642 0.0566 -0.0311 -0.0295 118 LEU B C 3488 O O . LEU B 118 ? 0.6335 0.6845 0.6872 0.0538 -0.0367 -0.0344 118 LEU B O 3489 C CB . LEU B 118 ? 0.5497 0.6715 0.6697 0.0211 -0.0295 -0.0321 118 LEU B CB 3490 C CG . LEU B 118 ? 0.5566 0.7355 0.6899 0.0183 -0.0317 -0.0368 118 LEU B CG 3491 C CD1 . LEU B 118 ? 0.6115 0.7903 0.7083 -0.0191 -0.0413 -0.0414 118 LEU B CD1 3492 C CD2 . LEU B 118 ? 0.5339 0.7733 0.6961 0.0253 -0.0290 -0.0383 118 LEU B CD2 3493 N N . TYR B 119 ? 0.5545 0.6320 0.6589 0.0807 -0.0237 -0.0200 119 TYR B N 3494 C CA . TYR B 119 ? 0.5383 0.6324 0.6470 0.1054 -0.0205 -0.0131 119 TYR B CA 3495 C C . TYR B 119 ? 0.6008 0.6561 0.6581 0.1268 -0.0247 -0.0172 119 TYR B C 3496 O O . TYR B 119 ? 0.6372 0.6961 0.6832 0.1392 -0.0263 -0.0188 119 TYR B O 3497 C CB . TYR B 119 ? 0.5034 0.6289 0.6393 0.1142 -0.0145 0.0020 119 TYR B CB 3498 C CG . TYR B 119 ? 0.5006 0.6592 0.6390 0.1324 -0.0114 0.0140 119 TYR B CG 3499 C CD1 . TYR B 119 ? 0.4922 0.6667 0.6446 0.1271 -0.0122 0.0191 119 TYR B CD1 3500 C CD2 . TYR B 119 ? 0.5062 0.6852 0.6261 0.1590 -0.0085 0.0209 119 TYR B CD2 3501 C CE1 . TYR B 119 ? 0.4947 0.7028 0.6464 0.1380 -0.0098 0.0325 119 TYR B CE1 3502 C CE2 . TYR B 119 ? 0.5039 0.7337 0.6272 0.1750 -0.0051 0.0341 119 TYR B CE2 3503 C CZ . TYR B 119 ? 0.5007 0.7439 0.6418 0.1594 -0.0057 0.0406 119 TYR B CZ 3504 O OH . TYR B 119 ? 0.4981 0.7938 0.6398 0.1694 -0.0028 0.0560 119 TYR B OH 3505 N N . ASP B 120 ? 0.6477 0.6585 0.6635 0.1368 -0.0279 -0.0195 120 ASP B N 3506 C CA . ASP B 120 ? 0.7259 0.6807 0.6693 0.1697 -0.0351 -0.0252 120 ASP B CA 3507 C C . ASP B 120 ? 0.7746 0.6630 0.6629 0.1453 -0.0490 -0.0378 120 ASP B C 3508 O O . ASP B 120 ? 0.8047 0.6597 0.6448 0.1685 -0.0556 -0.0429 120 ASP B O 3509 C CB . ASP B 120 ? 0.7838 0.6952 0.6792 0.1942 -0.0377 -0.0255 120 ASP B CB 3510 C CG . ASP B 120 ? 0.7674 0.7613 0.7050 0.2262 -0.0257 -0.0112 120 ASP B CG 3511 O OD1 . ASP B 120 ? 0.7358 0.8012 0.7066 0.2422 -0.0187 -0.0011 120 ASP B OD1 3512 O OD2 . ASP B 120 ? 0.8041 0.7975 0.7386 0.2314 -0.0241 -0.0083 120 ASP B OD2 3513 N N . LYS B 121 ? 0.7851 0.6636 0.6788 0.0959 -0.0542 -0.0417 121 LYS B N 3514 C CA . LYS B 121 ? 0.8704 0.7097 0.7172 0.0556 -0.0688 -0.0499 121 LYS B CA 3515 C C . LYS B 121 ? 0.8587 0.7421 0.7296 0.0644 -0.0672 -0.0516 121 LYS B C 3516 O O . LYS B 121 ? 0.9487 0.7748 0.7542 0.0640 -0.0800 -0.0584 121 LYS B O 3517 C CB . LYS B 121 ? 0.8667 0.7472 0.7449 0.0010 -0.0697 -0.0487 121 LYS B CB 3518 C CG . LYS B 121 ? 0.9535 0.8059 0.7749 -0.0583 -0.0874 -0.0528 121 LYS B CG 3519 C CD . LYS B 121 ? 0.9436 0.8655 0.8034 -0.1054 -0.0852 -0.0482 121 LYS B CD 3520 C CE . LYS B 121 ? 1.0283 0.9555 0.8375 -0.1783 -0.1031 -0.0473 121 LYS B CE 3521 N NZ . LYS B 121 ? 1.0327 1.0323 0.8654 -0.1850 -0.1048 -0.0501 121 LYS B NZ 3522 N N . VAL B 122 ? 0.7642 0.7373 0.7175 0.0742 -0.0534 -0.0454 122 VAL B N 3523 C CA . VAL B 122 ? 0.7322 0.7478 0.7086 0.0868 -0.0511 -0.0456 122 VAL B CA 3524 C C . VAL B 122 ? 0.7636 0.7574 0.7143 0.1322 -0.0491 -0.0430 122 VAL B C 3525 O O . VAL B 122 ? 0.7971 0.7740 0.7158 0.1399 -0.0557 -0.0486 122 VAL B O 3526 C CB . VAL B 122 ? 0.6629 0.7575 0.7126 0.0909 -0.0400 -0.0388 122 VAL B CB 3527 C CG1 . VAL B 122 ? 0.6441 0.7718 0.7093 0.1111 -0.0376 -0.0370 122 VAL B CG1 3528 C CG2 . VAL B 122 ? 0.6487 0.7825 0.7168 0.0575 -0.0428 -0.0433 122 VAL B CG2 3529 N N . ARG B 123 ? 0.7438 0.7496 0.7070 0.1628 -0.0404 -0.0339 123 ARG B N 3530 C CA . ARG B 123 ? 0.7719 0.7839 0.7108 0.2108 -0.0374 -0.0290 123 ARG B CA 3531 C C . ARG B 123 ? 0.8763 0.7987 0.7191 0.2318 -0.0523 -0.0426 123 ARG B C 3532 O O . ARG B 123 ? 0.9010 0.8243 0.7190 0.2601 -0.0544 -0.0447 123 ARG B O 3533 C CB . ARG B 123 ? 0.7679 0.8155 0.7223 0.2360 -0.0286 -0.0170 123 ARG B CB 3534 C CG . ARG B 123 ? 0.7967 0.8945 0.7387 0.2866 -0.0231 -0.0073 123 ARG B CG 3535 C CD . ARG B 123 ? 0.7919 0.9535 0.7535 0.3059 -0.0146 0.0073 123 ARG B CD 3536 N NE . ARG B 123 ? 0.8476 0.9490 0.7697 0.3121 -0.0200 -0.0013 123 ARG B NE 3537 C CZ . ARG B 123 ? 0.9390 0.9683 0.7723 0.3578 -0.0295 -0.0131 123 ARG B CZ 3538 N NH1 . ARG B 123 ? 1.0084 1.0149 0.7789 0.4066 -0.0353 -0.0195 123 ARG B NH1 3539 N NH2 . ARG B 123 ? 0.9864 0.9554 0.7821 0.3578 -0.0350 -0.0190 123 ARG B NH2 3540 N N . LEU B 124 ? 0.9512 0.7864 0.7296 0.2162 -0.0646 -0.0514 124 LEU B N 3541 C CA . LEU B 124 ? 1.0917 0.8043 0.7473 0.2322 -0.0851 -0.0646 124 LEU B CA 3542 C C . LEU B 124 ? 1.1491 0.8220 0.7678 0.1958 -0.0997 -0.0738 124 LEU B C 3543 O O . LEU B 124 ? 1.2588 0.8289 0.7694 0.2145 -0.1182 -0.0842 124 LEU B O 3544 C CB . LEU B 124 ? 1.1640 0.7782 0.7477 0.2125 -0.0980 -0.0694 124 LEU B CB 3545 C CG . LEU B 124 ? 1.1660 0.7953 0.7533 0.2593 -0.0885 -0.0633 124 LEU B CG 3546 C CD1 . LEU B 124 ? 1.2052 0.7636 0.7549 0.2228 -0.0971 -0.0649 124 LEU B CD1 3547 C CD2 . LEU B 124 ? 1.2501 0.8338 0.7477 0.3432 -0.0943 -0.0681 124 LEU B CD2 3548 N N . GLN B 125 ? 1.0886 0.8396 0.7861 0.1470 -0.0936 -0.0704 125 GLN B N 3549 C CA . GLN B 125 ? 1.1166 0.8639 0.7945 0.1134 -0.1053 -0.0771 125 GLN B CA 3550 C C . GLN B 125 ? 1.0822 0.8851 0.7944 0.1563 -0.0959 -0.0754 125 GLN B C 3551 O O . GLN B 125 ? 1.1630 0.9105 0.8069 0.1708 -0.1086 -0.0836 125 GLN B O 3552 C CB . GLN B 125 ? 1.0584 0.8883 0.8047 0.0539 -0.1021 -0.0739 125 GLN B CB 3553 C CG . GLN B 125 ? 1.1117 0.9026 0.8229 -0.0013 -0.1130 -0.0738 125 GLN B CG 3554 C CD . GLN B 125 ? 1.0733 0.9643 0.8390 -0.0576 -0.1126 -0.0710 125 GLN B CD 3555 O OE1 . GLN B 125 ? 1.1240 1.0267 0.8586 -0.0983 -0.1266 -0.0742 125 GLN B OE1 3556 N NE2 . GLN B 125 ? 1.0015 0.9728 0.8441 -0.0572 -0.0977 -0.0649 125 GLN B NE2 3557 N N . LEU B 126 ? 0.9913 0.8960 0.8004 0.1737 -0.0755 -0.0638 126 LEU B N 3558 C CA . LEU B 126 ? 0.9780 0.9436 0.8245 0.2054 -0.0660 -0.0582 126 LEU B CA 3559 C C . LEU B 126 ? 1.0646 1.0039 0.8601 0.2645 -0.0659 -0.0575 126 LEU B C 3560 O O . LEU B 126 ? 1.1122 1.0623 0.8932 0.2880 -0.0673 -0.0592 126 LEU B O 3561 C CB . LEU B 126 ? 0.8640 0.9210 0.8026 0.2049 -0.0487 -0.0436 126 LEU B CB 3562 C CG . LEU B 126 ? 0.8016 0.8938 0.7860 0.1641 -0.0480 -0.0449 126 LEU B CG 3563 C CD1 . LEU B 126 ? 0.7388 0.8920 0.7847 0.1741 -0.0358 -0.0318 126 LEU B CD1 3564 C CD2 . LEU B 126 ? 0.8283 0.9274 0.7959 0.1373 -0.0588 -0.0557 126 LEU B CD2 3565 N N . ARG B 127 ? 1.1643 1.0776 0.9299 0.2937 -0.0645 -0.0550 127 ARG B N 3566 C CA . ARG B 127 ? 1.2759 1.1764 0.9816 0.3628 -0.0652 -0.0550 127 ARG B CA 3567 C C . ARG B 127 ? 1.2378 1.2486 1.0027 0.3903 -0.0501 -0.0405 127 ARG B C 3568 O O . ARG B 127 ? 1.1781 1.2806 1.0261 0.3728 -0.0352 -0.0228 127 ARG B O 3569 C CB . ARG B 127 ? 1.4176 1.1838 0.9939 0.3807 -0.0889 -0.0745 127 ARG B CB 3570 C CG . ARG B 127 ? 1.5027 1.1461 0.9973 0.3535 -0.1068 -0.0849 127 ARG B CG 3571 C CD . ARG B 127 ? 1.6362 1.1401 1.0129 0.3229 -0.1355 -0.1014 127 ARG B CD 3572 N NE . ARG B 127 ? 1.7966 1.2141 1.0556 0.3917 -0.1502 -0.1127 127 ARG B NE 3573 C CZ . ARG B 127 ? 1.9778 1.2486 1.1029 0.3774 -0.1799 -0.1280 127 ARG B CZ 3574 N NH1 . ARG B 127 ? 2.0401 1.2475 1.1373 0.2864 -0.1980 -0.1312 127 ARG B NH1 3575 N NH2 . ARG B 127 ? 2.0859 1.2750 1.0960 0.4531 -0.1936 -0.1392 127 ARG B NH2 3576 N N . ASP B 128 ? 1.3018 1.2977 1.0174 0.4275 -0.0560 -0.0467 128 ASP B N 3577 C CA . ASP B 128 ? 1.2583 1.3613 1.0232 0.4520 -0.0423 -0.0310 128 ASP B CA 3578 C C . ASP B 128 ? 1.1936 1.3132 0.9998 0.4154 -0.0423 -0.0316 128 ASP B C 3579 O O . ASP B 128 ? 1.1923 1.3736 1.0153 0.4372 -0.0355 -0.0221 128 ASP B O 3580 C CB . ASP B 128 ? 1.3635 1.4696 1.0526 0.5311 -0.0454 -0.0340 128 ASP B CB 3581 C CG . ASP B 128 ? 1.5226 1.4975 1.1017 0.5515 -0.0674 -0.0587 128 ASP B CG 3582 O OD1 . ASP B 128 ? 1.5442 1.4403 1.1129 0.4945 -0.0799 -0.0709 128 ASP B OD1 3583 O OD2 . ASP B 128 ? 1.6521 1.6061 1.1475 0.6252 -0.0738 -0.0652 128 ASP B OD2 3584 N N . ASN B 129 ? 1.1543 1.2297 0.9748 0.3621 -0.0496 -0.0415 129 ASN B N 3585 C CA . ASN B 129 ? 1.0911 1.1987 0.9547 0.3315 -0.0488 -0.0414 129 ASN B CA 3586 C C . ASN B 129 ? 0.9868 1.1675 0.9337 0.3071 -0.0353 -0.0242 129 ASN B C 3587 O O . ASN B 129 ? 0.9703 1.1724 0.9464 0.2870 -0.0356 -0.0249 129 ASN B O 3588 C CB . ASN B 129 ? 1.1510 1.1966 0.9821 0.2883 -0.0651 -0.0594 129 ASN B CB 3589 C CG . ASN B 129 ? 1.2762 1.2314 1.0070 0.3023 -0.0843 -0.0759 129 ASN B CG 3590 O OD1 . ASN B 129 ? 1.3694 1.2943 1.0453 0.3556 -0.0859 -0.0772 129 ASN B OD1 3591 N ND2 . ASN B 129 ? 1.3056 1.2197 1.0032 0.2544 -0.1010 -0.0881 129 ASN B ND2 3592 N N . ALA B 130 ? 0.9185 1.1327 0.8920 0.3111 -0.0258 -0.0090 130 ALA B N 3593 C CA . ALA B 130 ? 0.8431 1.1032 0.8733 0.2850 -0.0176 0.0082 130 ALA B CA 3594 C C . ALA B 130 ? 0.8154 1.1290 0.8612 0.2921 -0.0087 0.0301 130 ALA B C 3595 O O . ALA B 130 ? 0.8487 1.1631 0.8717 0.3150 -0.0080 0.0281 130 ALA B O 3596 C CB . ALA B 130 ? 0.8296 1.0589 0.8775 0.2513 -0.0214 -0.0011 130 ALA B CB 3597 N N . LYS B 131 ? 0.7764 1.1331 0.8511 0.2710 -0.0042 0.0518 131 LYS B N 3598 C CA . LYS B 131 ? 0.7714 1.1893 0.8606 0.2592 0.0016 0.0768 131 LYS B CA 3599 C C . LYS B 131 ? 0.7243 1.1142 0.8290 0.2315 -0.0001 0.0756 131 LYS B C 3600 O O . LYS B 131 ? 0.6982 1.0412 0.8114 0.2051 -0.0049 0.0714 131 LYS B O 3601 C CB . LYS B 131 ? 0.8282 1.2851 0.9249 0.2315 0.0021 0.1036 131 LYS B CB 3602 C CG . LYS B 131 ? 0.9124 1.4177 0.9969 0.2549 0.0052 0.1120 131 LYS B CG 3603 C CD . LYS B 131 ? 0.9843 1.4953 1.0638 0.2182 0.0018 0.1365 131 LYS B CD 3604 C CE . LYS B 131 ? 1.0277 1.6175 1.0979 0.2320 0.0067 0.1554 131 LYS B CE 3605 N NZ . LYS B 131 ? 1.0293 1.7386 1.1063 0.2289 0.0136 0.1819 131 LYS B NZ 3606 N N . GLU B 132 ? 0.6857 1.1071 0.7886 0.2439 0.0034 0.0789 132 GLU B N 3607 C CA . GLU B 132 ? 0.6502 1.0594 0.7691 0.2164 0.0026 0.0822 132 GLU B CA 3608 C C . GLU B 132 ? 0.6378 1.0955 0.7706 0.1747 0.0020 0.1121 132 GLU B C 3609 O O . GLU B 132 ? 0.6421 1.1911 0.7764 0.1749 0.0063 0.1346 132 GLU B O 3610 C CB . GLU B 132 ? 0.6604 1.0895 0.7655 0.2470 0.0055 0.0770 132 GLU B CB 3611 C CG . GLU B 132 ? 0.6470 1.0410 0.7638 0.2241 0.0036 0.0720 132 GLU B CG 3612 C CD . GLU B 132 ? 0.6724 1.0751 0.7648 0.2602 0.0052 0.0657 132 GLU B CD 3613 O OE1 . GLU B 132 ? 0.7194 1.1560 0.7786 0.3099 0.0071 0.0649 132 GLU B OE1 3614 O OE2 . GLU B 132 ? 0.6678 1.0403 0.7667 0.2443 0.0038 0.0609 132 GLU B OE2 3615 N N . LEU B 133 ? 0.6278 1.0250 0.7599 0.1390 -0.0054 0.1132 133 LEU B N 3616 C CA . LEU B 133 ? 0.6426 1.0487 0.7609 0.0921 -0.0124 0.1416 133 LEU B CA 3617 C C . LEU B 133 ? 0.6486 1.0913 0.7710 0.0562 -0.0147 0.1602 133 LEU B C 3618 O O . LEU B 133 ? 0.6657 1.1390 0.7694 0.0093 -0.0217 0.1897 133 LEU B O 3619 C CB . LEU B 133 ? 0.6698 0.9768 0.7610 0.0774 -0.0235 0.1345 133 LEU B CB 3620 C CG . LEU B 133 ? 0.6815 0.9634 0.7599 0.1018 -0.0242 0.1251 133 LEU B CG 3621 C CD1 . LEU B 133 ? 0.7356 0.9251 0.7726 0.0934 -0.0374 0.1219 133 LEU B CD1 3622 C CD2 . LEU B 133 ? 0.6927 1.0387 0.7643 0.0965 -0.0211 0.1480 133 LEU B CD2 3623 N N . GLY B 134 ? 0.6314 1.0685 0.7717 0.0724 -0.0108 0.1443 134 GLY B N 3624 C CA . GLY B 134 ? 0.6296 1.1081 0.7762 0.0432 -0.0126 0.1596 134 GLY B CA 3625 C C . GLY B 134 ? 0.6461 1.0371 0.7778 0.0077 -0.0238 0.1562 134 GLY B C 3626 O O . GLY B 134 ? 0.6475 1.0643 0.7787 -0.0244 -0.0279 0.1702 134 GLY B O 3627 N N . ASN B 135 ? 0.6454 0.9405 0.7611 0.0177 -0.0293 0.1373 135 ASN B N 3628 C CA . ASN B 135 ? 0.6798 0.8861 0.7675 -0.0032 -0.0417 0.1319 135 ASN B CA 3629 C C . ASN B 135 ? 0.6547 0.8112 0.7546 0.0334 -0.0386 0.1004 135 ASN B C 3630 O O . ASN B 135 ? 0.6681 0.7530 0.7384 0.0331 -0.0486 0.0919 135 ASN B O 3631 C CB . ASN B 135 ? 0.7569 0.8926 0.7851 -0.0307 -0.0577 0.1468 135 ASN B CB 3632 C CG . ASN B 135 ? 0.7657 0.8716 0.7854 0.0054 -0.0560 0.1328 135 ASN B CG 3633 O OD1 . ASN B 135 ? 0.7190 0.8812 0.7785 0.0374 -0.0428 0.1215 135 ASN B OD1 3634 N ND2 . ASN B 135 ? 0.8577 0.8684 0.8151 0.0036 -0.0714 0.1329 135 ASN B ND2 3635 N N . GLY B 136 ? 0.6047 0.7998 0.7381 0.0644 -0.0268 0.0843 136 GLY B N 3636 C CA . GLY B 136 ? 0.5832 0.7491 0.7258 0.0876 -0.0249 0.0584 136 GLY B CA 3637 C C . GLY B 136 ? 0.5816 0.7429 0.7196 0.1094 -0.0246 0.0467 136 GLY B C 3638 O O . GLY B 136 ? 0.5641 0.7220 0.7095 0.1223 -0.0236 0.0277 136 GLY B O 3639 N N . CYS B 137 ? 0.6135 0.7824 0.7377 0.1093 -0.0262 0.0596 137 CYS B N 3640 C CA . CYS B 137 ? 0.6322 0.7966 0.7488 0.1307 -0.0271 0.0495 137 CYS B CA 3641 C C . CYS B 137 ? 0.6095 0.8164 0.7370 0.1448 -0.0200 0.0500 137 CYS B C 3642 O O . CYS B 137 ? 0.5974 0.8424 0.7295 0.1415 -0.0154 0.0644 137 CYS B O 3643 C CB . CYS B 137 ? 0.6829 0.8051 0.7599 0.1269 -0.0370 0.0613 137 CYS B CB 3644 S SG . CYS B 137 ? 0.7648 0.8097 0.7984 0.1263 -0.0506 0.0569 137 CYS B SG 3645 N N . PHE B 138 ? 0.6063 0.8127 0.7326 0.1632 -0.0203 0.0340 138 PHE B N 3646 C CA . PHE B 138 ? 0.6119 0.8424 0.7350 0.1805 -0.0169 0.0312 138 PHE B CA 3647 C C . PHE B 138 ? 0.6402 0.8712 0.7525 0.1915 -0.0200 0.0314 138 PHE B C 3648 O O . PHE B 138 ? 0.6267 0.8472 0.7360 0.1971 -0.0245 0.0185 138 PHE B O 3649 C CB . PHE B 138 ? 0.6001 0.8189 0.7178 0.1860 -0.0182 0.0105 138 PHE B CB 3650 C CG . PHE B 138 ? 0.6013 0.8077 0.7165 0.1810 -0.0165 0.0092 138 PHE B CG 3651 C CD1 . PHE B 138 ? 0.6052 0.8218 0.7030 0.2017 -0.0133 0.0147 138 PHE B CD1 3652 C CD2 . PHE B 138 ? 0.5921 0.7812 0.7168 0.1623 -0.0184 0.0024 138 PHE B CD2 3653 C CE1 . PHE B 138 ? 0.6123 0.8144 0.6984 0.2053 -0.0128 0.0127 138 PHE B CE1 3654 C CE2 . PHE B 138 ? 0.5968 0.7700 0.7149 0.1587 -0.0173 0.0014 138 PHE B CE2 3655 C CZ . PHE B 138 ? 0.6072 0.7834 0.7043 0.1811 -0.0149 0.0064 138 PHE B CZ 3656 N N . GLU B 139 ? 0.6877 0.9419 0.7926 0.1974 -0.0174 0.0466 139 GLU B N 3657 C CA . GLU B 139 ? 0.7386 0.9924 0.8294 0.2094 -0.0200 0.0485 139 GLU B CA 3658 C C . GLU B 139 ? 0.7326 1.0075 0.8224 0.2318 -0.0179 0.0346 139 GLU B C 3659 O O . GLU B 139 ? 0.7617 1.0613 0.8474 0.2436 -0.0134 0.0394 139 GLU B O 3660 C CB . GLU B 139 ? 0.8064 1.0729 0.8821 0.1947 -0.0201 0.0769 139 GLU B CB 3661 C CG . GLU B 139 ? 0.8835 1.1234 0.9292 0.1994 -0.0264 0.0837 139 GLU B CG 3662 C CD . GLU B 139 ? 0.9699 1.2142 0.9888 0.1692 -0.0296 0.1164 139 GLU B CD 3663 O OE1 . GLU B 139 ? 0.9755 1.2903 1.0094 0.1651 -0.0219 0.1315 139 GLU B OE1 3664 O OE2 . GLU B 139 ? 1.0794 1.2568 1.0532 0.1488 -0.0415 0.1281 139 GLU B OE2 3665 N N . PHE B 140 ? 0.7320 0.9998 0.8177 0.2403 -0.0227 0.0174 140 PHE B N 3666 C CA . PHE B 140 ? 0.7462 1.0214 0.8197 0.2532 -0.0250 0.0024 140 PHE B CA 3667 C C . PHE B 140 ? 0.7860 1.0813 0.8478 0.2737 -0.0227 0.0118 140 PHE B C 3668 O O . PHE B 140 ? 0.7759 1.0784 0.8377 0.2749 -0.0217 0.0267 140 PHE B O 3669 C CB . PHE B 140 ? 0.7196 1.0010 0.7932 0.2468 -0.0322 -0.0161 140 PHE B CB 3670 C CG . PHE B 140 ? 0.7019 0.9776 0.7837 0.2242 -0.0351 -0.0259 140 PHE B CG 3671 C CD1 . PHE B 140 ? 0.6860 0.9675 0.7832 0.2215 -0.0341 -0.0227 140 PHE B CD1 3672 C CD2 . PHE B 140 ? 0.7219 0.9775 0.7837 0.2057 -0.0409 -0.0379 140 PHE B CD2 3673 C CE1 . PHE B 140 ? 0.6768 0.9635 0.7826 0.2020 -0.0360 -0.0309 140 PHE B CE1 3674 C CE2 . PHE B 140 ? 0.7162 0.9685 0.7814 0.1787 -0.0442 -0.0444 140 PHE B CE2 3675 C CZ . PHE B 140 ? 0.6933 0.9707 0.7872 0.1775 -0.0403 -0.0406 140 PHE B CZ 3676 N N . TYR B 141 ? 0.8384 1.1334 0.8787 0.2909 -0.0240 0.0034 141 TYR B N 3677 C CA . TYR B 141 ? 0.8919 1.2107 0.9182 0.3149 -0.0224 0.0095 141 TYR B CA 3678 C C . TYR B 141 ? 0.9035 1.2201 0.9239 0.3163 -0.0293 -0.0044 141 TYR B C 3679 O O . TYR B 141 ? 0.9569 1.2940 0.9780 0.3282 -0.0276 0.0047 141 TYR B O 3680 C CB . TYR B 141 ? 0.9239 1.2401 0.9162 0.3441 -0.0226 0.0050 141 TYR B CB 3681 C CG . TYR B 141 ? 0.9335 1.2822 0.9320 0.3529 -0.0143 0.0220 141 TYR B CG 3682 C CD1 . TYR B 141 ? 0.9263 1.3367 0.9496 0.3445 -0.0057 0.0498 141 TYR B CD1 3683 C CD2 . TYR B 141 ? 0.9691 1.2882 0.9419 0.3654 -0.0170 0.0122 141 TYR B CD2 3684 C CE1 . TYR B 141 ? 0.9342 1.3967 0.9652 0.3457 0.0010 0.0682 141 TYR B CE1 3685 C CE2 . TYR B 141 ? 0.9637 1.3293 0.9431 0.3781 -0.0093 0.0281 141 TYR B CE2 3686 C CZ . TYR B 141 ? 0.9478 1.3956 0.9610 0.3666 0.0002 0.0565 141 TYR B CZ 3687 O OH . TYR B 141 ? 0.9434 1.4592 0.9645 0.3729 0.0071 0.0749 141 TYR B OH 3688 N N . HIS B 142 ? 1.1126 1.6045 0.9224 0.4767 -0.0964 -0.1132 142 HIS B N 3689 C CA . HIS B 142 ? 1.1225 1.6384 0.9228 0.4794 -0.1240 -0.1378 142 HIS B CA 3690 C C . HIS B 142 ? 1.0449 1.5740 0.9042 0.4440 -0.1092 -0.1092 142 HIS B C 3691 O O . HIS B 142 ? 0.9827 1.4798 0.8855 0.4063 -0.0876 -0.0856 142 HIS B O 3692 C CB . HIS B 142 ? 1.1763 1.6504 0.9600 0.4521 -0.1706 -0.2027 142 HIS B CB 3693 C CG . HIS B 142 ? 1.1340 1.5428 0.9624 0.3909 -0.1702 -0.2118 142 HIS B CG 3694 N ND1 . HIS B 142 ? 1.0892 1.4992 0.9760 0.3385 -0.1791 -0.2172 142 HIS B ND1 3695 C CD2 . HIS B 142 ? 1.1401 1.4857 0.9571 0.3838 -0.1587 -0.2122 142 HIS B CD2 3696 C CE1 . HIS B 142 ? 1.0764 1.4196 0.9831 0.3010 -0.1712 -0.2197 142 HIS B CE1 3697 N NE2 . HIS B 142 ? 1.1077 1.4099 0.9706 0.3288 -0.1600 -0.2178 142 HIS B NE2 3698 N N . LYS B 143 ? 1.0510 1.6297 0.9036 0.4636 -0.1220 -0.1126 143 LYS B N 3699 C CA . LYS B 143 ? 1.0168 1.6045 0.9153 0.4368 -0.1130 -0.0930 143 LYS B CA 3700 C C . LYS B 143 ? 0.9761 1.5381 0.9199 0.3770 -0.1402 -0.1294 143 LYS B C 3701 O O . LYS B 143 ? 0.9987 1.5529 0.9329 0.3617 -0.1748 -0.1770 143 LYS B O 3702 C CB . LYS B 143 ? 1.0603 1.7237 0.9373 0.4839 -0.1202 -0.0859 143 LYS B CB 3703 C CG . LYS B 143 ? 1.1238 1.7993 0.9543 0.5468 -0.0778 -0.0332 143 LYS B CG 3704 C CD . LYS B 143 ? 1.1591 1.8744 0.9801 0.5840 -0.0617 -0.0015 143 LYS B CD 3705 C CE . LYS B 143 ? 1.1817 1.9958 1.0046 0.6027 -0.1121 -0.0434 143 LYS B CE 3706 N NZ . LYS B 143 ? 1.1446 1.9748 1.0277 0.5616 -0.1195 -0.0457 143 LYS B NZ 3707 N N . CYS B 144 ? 0.9008 1.4397 0.8869 0.3453 -0.1211 -0.1058 144 CYS B N 3708 C CA . CYS B 144 ? 0.8580 1.3686 0.8871 0.2933 -0.1339 -0.1266 144 CYS B CA 3709 C C . CYS B 144 ? 0.8154 1.3618 0.8796 0.2889 -0.1233 -0.1039 144 CYS B C 3710 O O . CYS B 144 ? 0.7936 1.2993 0.8586 0.2891 -0.0935 -0.0707 144 CYS B O 3711 C CB . CYS B 144 ? 0.8447 1.2769 0.8756 0.2691 -0.1162 -0.1188 144 CYS B CB 3712 S SG . CYS B 144 ? 0.8648 1.2431 0.9295 0.2179 -0.1225 -0.1381 144 CYS B SG 3713 N N . ASP B 145 ? 0.8159 1.4435 0.9061 0.2877 -0.1494 -0.1237 145 ASP B N 3714 C CA . ASP B 145 ? 0.7876 1.4758 0.9141 0.2934 -0.1396 -0.0999 145 ASP B CA 3715 C C . ASP B 145 ? 0.7457 1.3986 0.9221 0.2432 -0.1303 -0.0981 145 ASP B C 3716 O O . ASP B 145 ? 0.7517 1.3271 0.9281 0.2076 -0.1305 -0.1140 145 ASP B O 3717 C CB . ASP B 145 ? 0.8082 1.6268 0.9537 0.3136 -0.1734 -0.1207 145 ASP B CB 3718 C CG . ASP B 145 ? 0.8326 1.6844 1.0239 0.2567 -0.2182 -0.1765 145 ASP B CG 3719 O OD1 . ASP B 145 ? 0.8447 1.6041 1.0421 0.2085 -0.2177 -0.1955 145 ASP B OD1 3720 O OD2 . ASP B 145 ? 0.8716 1.8414 1.0899 0.2609 -0.2546 -0.2029 145 ASP B OD2 3721 N N . ASN B 146 ? 0.7151 1.4271 0.9275 0.2495 -0.1181 -0.0743 146 ASN B N 3722 C CA . ASN B 146 ? 0.6917 1.3691 0.9414 0.2160 -0.0984 -0.0605 146 ASN B CA 3723 C C . ASN B 146 ? 0.7220 1.3936 1.0240 0.1521 -0.1166 -0.0925 146 ASN B C 3724 O O . ASN B 146 ? 0.7320 1.3259 1.0376 0.1273 -0.0961 -0.0837 146 ASN B O 3725 C CB . ASN B 146 ? 0.6678 1.4246 0.9427 0.2465 -0.0782 -0.0242 146 ASN B CB 3726 C CG . ASN B 146 ? 0.6663 1.3901 0.8718 0.3124 -0.0511 0.0110 146 ASN B CG 3727 O OD1 . ASN B 146 ? 0.6668 1.2917 0.8157 0.3215 -0.0405 0.0133 146 ASN B OD1 3728 N ND2 . ASN B 146 ? 0.6748 1.4820 0.8848 0.3587 -0.0376 0.0402 146 ASN B ND2 3729 N N . GLU B 147 ? 0.7864 1.5307 1.1210 0.1273 -0.1544 -0.1308 147 GLU B N 3730 C CA . GLU B 147 ? 0.8569 1.5661 1.2291 0.0595 -0.1727 -0.1685 147 GLU B CA 3731 C C . GLU B 147 ? 0.8670 1.4357 1.1724 0.0569 -0.1695 -0.1867 147 GLU B C 3732 O O . GLU B 147 ? 0.8989 1.3802 1.2091 0.0202 -0.1547 -0.1896 147 GLU B O 3733 C CB . GLU B 147 ? 0.9304 1.7403 1.3413 0.0315 -0.2227 -0.2173 147 GLU B CB 3734 C CG . GLU B 147 ? 0.9520 1.9090 1.4656 -0.0013 -0.2301 -0.2095 147 GLU B CG 3735 C CD . GLU B 147 ? 0.9277 1.9848 1.4451 0.0651 -0.2060 -0.1577 147 GLU B CD 3736 O OE1 . GLU B 147 ? 0.9375 2.0136 1.3904 0.1319 -0.2122 -0.1523 147 GLU B OE1 3737 O OE2 . GLU B 147 ? 0.9222 2.0292 1.4982 0.0564 -0.1756 -0.1188 147 GLU B OE2 3738 N N . CYS B 148 ? 0.8501 1.4038 1.0917 0.1020 -0.1793 -0.1940 148 CYS B N 3739 C CA . CYS B 148 ? 0.8769 1.3234 1.0554 0.1139 -0.1729 -0.2032 148 CYS B CA 3740 C C . CYS B 148 ? 0.8199 1.1944 0.9895 0.1182 -0.1355 -0.1669 148 CYS B C 3741 O O . CYS B 148 ? 0.8464 1.1353 0.9959 0.1036 -0.1263 -0.1736 148 CYS B O 3742 C CB . CYS B 148 ? 0.8972 1.3680 1.0206 0.1672 -0.1818 -0.2045 148 CYS B CB 3743 S SG . CYS B 148 ? 0.9666 1.3453 1.0244 0.1950 -0.1650 -0.1989 148 CYS B SG 3744 N N . MET B 149 ? 0.7396 1.1447 0.9151 0.1430 -0.1150 -0.1304 149 MET B N 3745 C CA . MET B 149 ? 0.7040 1.0477 0.8664 0.1485 -0.0863 -0.1026 149 MET B CA 3746 C C . MET B 149 ? 0.7253 1.0363 0.9167 0.1176 -0.0726 -0.0983 149 MET B C 3747 O O . MET B 149 ? 0.7364 0.9715 0.9006 0.1176 -0.0589 -0.0949 149 MET B O 3748 C CB . MET B 149 ? 0.6669 1.0375 0.8235 0.1783 -0.0684 -0.0699 149 MET B CB 3749 C CG . MET B 149 ? 0.6572 1.0343 0.7783 0.2093 -0.0681 -0.0624 149 MET B CG 3750 S SD . MET B 149 ? 0.6503 0.9611 0.7376 0.2078 -0.0648 -0.0670 149 MET B SD 3751 C CE . MET B 149 ? 0.6469 0.9822 0.7100 0.2388 -0.0534 -0.0457 149 MET B CE 3752 N N . GLU B 150 ? 0.7460 1.1234 0.9942 0.0943 -0.0737 -0.0951 150 GLU B N 3753 C CA . GLU B 150 ? 0.7821 1.1373 1.0692 0.0606 -0.0526 -0.0829 150 GLU B CA 3754 C C . GLU B 150 ? 0.8350 1.0978 1.1037 0.0285 -0.0561 -0.1094 150 GLU B C 3755 O O . GLU B 150 ? 0.8598 1.0486 1.1165 0.0233 -0.0273 -0.0915 150 GLU B O 3756 C CB . GLU B 150 ? 0.7926 1.2629 1.1620 0.0333 -0.0558 -0.0758 150 GLU B CB 3757 C CG . GLU B 150 ? 0.8428 1.3070 1.2723 -0.0130 -0.0292 -0.0586 150 GLU B CG 3758 C CD . GLU B 150 ? 0.8530 1.2637 1.2561 0.0190 0.0169 -0.0122 150 GLU B CD 3759 O OE1 . GLU B 150 ? 0.8396 1.2207 1.1802 0.0731 0.0233 0.0016 150 GLU B OE1 3760 O OE2 . GLU B 150 ? 0.9027 1.2978 1.3458 -0.0107 0.0480 0.0103 150 GLU B OE2 3761 N N . SER B 151 ? 0.8682 1.1266 1.1209 0.0168 -0.0887 -0.1503 151 SER B N 3762 C CA . SER B 151 ? 0.9639 1.1177 1.1826 -0.0078 -0.0924 -0.1797 151 SER B CA 3763 C C . SER B 151 ? 0.9792 1.0365 1.1230 0.0344 -0.0723 -0.1671 151 SER B C 3764 O O . SER B 151 ? 1.0679 1.0217 1.1762 0.0265 -0.0567 -0.1725 151 SER B O 3765 C CB . SER B 151 ? 1.0103 1.1776 1.2101 -0.0171 -0.1350 -0.2308 151 SER B CB 3766 O OG . SER B 151 ? 0.9927 1.1542 1.1266 0.0383 -0.1450 -0.2354 151 SER B OG 3767 N N . VAL B 152 ? 0.9158 1.0082 1.0353 0.0789 -0.0722 -0.1502 152 VAL B N 3768 C CA . VAL B 152 ? 0.9102 0.9459 0.9744 0.1172 -0.0576 -0.1373 152 VAL B CA 3769 C C . VAL B 152 ? 0.9245 0.9236 0.9896 0.1219 -0.0265 -0.1063 152 VAL B C 3770 O O . VAL B 152 ? 0.9525 0.8781 0.9717 0.1421 -0.0100 -0.1007 152 VAL B O 3771 C CB . VAL B 152 ? 0.8471 0.9387 0.8992 0.1498 -0.0675 -0.1298 152 VAL B CB 3772 C CG1 . VAL B 152 ? 0.8523 0.9119 0.8645 0.1813 -0.0575 -0.1188 152 VAL B CG1 3773 C CG2 . VAL B 152 ? 0.8554 0.9804 0.8943 0.1587 -0.0907 -0.1533 152 VAL B CG2 3774 N N . ARG B 153 ? 0.9038 0.9551 1.0111 0.1138 -0.0163 -0.0839 153 ARG B N 3775 C CA . ARG B 153 ? 0.9489 0.9701 1.0517 0.1255 0.0160 -0.0520 153 ARG B CA 3776 C C . ARG B 153 ? 1.0542 1.0169 1.1727 0.0952 0.0418 -0.0441 153 ARG B C 3777 O O . ARG B 153 ? 1.1219 1.0210 1.2054 0.1176 0.0732 -0.0198 153 ARG B O 3778 C CB . ARG B 153 ? 0.9188 1.0089 1.0569 0.1309 0.0246 -0.0281 153 ARG B CB 3779 C CG . ARG B 153 ? 0.8701 0.9948 0.9868 0.1576 0.0070 -0.0317 153 ARG B CG 3780 C CD . ARG B 153 ? 0.8584 1.0237 0.9867 0.1761 0.0230 -0.0048 153 ARG B CD 3781 N NE . ARG B 153 ? 0.8390 1.0457 0.9640 0.1879 0.0075 -0.0093 153 ARG B NE 3782 C CZ . ARG B 153 ? 0.8282 1.1129 0.9930 0.1833 0.0014 -0.0062 153 ARG B CZ 3783 N NH1 . ARG B 153 ? 0.8279 1.1747 1.0541 0.1567 0.0036 -0.0032 153 ARG B NH1 3784 N NH2 . ARG B 153 ? 0.8336 1.1384 0.9775 0.2058 -0.0059 -0.0049 153 ARG B NH2 3785 N N . ASN B 154 ? 1.1270 1.1108 1.2964 0.0441 0.0290 -0.0647 154 ASN B N 3786 C CA . ASN B 154 ? 1.2453 1.1588 1.4350 -0.0025 0.0509 -0.0649 154 ASN B CA 3787 C C . ASN B 154 ? 1.3052 1.0829 1.4104 0.0229 0.0680 -0.0692 154 ASN B C 3788 O O . ASN B 154 ? 1.3766 1.0743 1.4621 0.0271 0.1110 -0.0389 154 ASN B O 3789 C CB . ASN B 154 ? 1.3348 1.2834 1.5754 -0.0624 0.0167 -0.1071 154 ASN B CB 3790 C CG . ASN B 154 ? 1.3986 1.4779 1.7421 -0.1038 0.0117 -0.0966 154 ASN B CG 3791 O OD1 . ASN B 154 ? 1.3630 1.5174 1.7317 -0.0755 0.0299 -0.0586 154 ASN B OD1 3792 N ND2 . ASN B 154 ? 1.5801 1.6908 1.9802 -0.1686 -0.0152 -0.1332 154 ASN B ND2 3793 N N . GLY B 155 ? 1.2752 1.0317 1.3253 0.0490 0.0382 -0.1021 155 GLY B N 3794 C CA . GLY B 155 ? 1.3466 0.9780 1.3143 0.0716 0.0478 -0.1161 155 GLY B CA 3795 C C . GLY B 155 ? 1.3902 0.9831 1.3532 0.0318 0.0189 -0.1647 155 GLY B C 3796 O O . GLY B 155 ? 1.4810 0.9625 1.3635 0.0542 0.0220 -0.1843 155 GLY B O 3797 N N . THR B 156 ? 1.3293 1.0174 1.3694 -0.0187 -0.0113 -0.1859 156 THR B N 3798 C CA . THR B 156 ? 1.3927 1.0575 1.4383 -0.0665 -0.0453 -0.2386 156 THR B CA 3799 C C . THR B 156 ? 1.3459 1.0742 1.3565 -0.0292 -0.0899 -0.2731 156 THR B C 3800 O O . THR B 156 ? 1.3980 1.1282 1.4068 -0.0583 -0.1265 -0.3215 156 THR B O 3801 C CB . THR B 156 ? 1.3810 1.1374 1.5405 -0.1445 -0.0555 -0.2431 156 THR B CB 3802 O OG1 . THR B 156 ? 1.4006 1.1252 1.6042 -0.1722 -0.0054 -0.1968 156 THR B OG1 3803 C CG2 . THR B 156 ? 1.5037 1.2199 1.6722 -0.2097 -0.0924 -0.3050 156 THR B CG2 3804 N N . TYR B 157 ? 1.2749 1.0563 1.2573 0.0340 -0.0870 -0.2491 157 TYR B N 3805 C CA . TYR B 157 ? 1.2376 1.0899 1.1950 0.0710 -0.1194 -0.2696 157 TYR B CA 3806 C C . TYR B 157 ? 1.3760 1.1413 1.2551 0.0825 -0.1404 -0.3171 157 TYR B C 3807 O O . TYR B 157 ? 1.4324 1.1003 1.2307 0.1248 -0.1231 -0.3156 157 TYR B O 3808 C CB . TYR B 157 ? 1.1407 1.0350 1.0732 0.1309 -0.1059 -0.2363 157 TYR B CB 3809 C CG . TYR B 157 ? 1.0954 1.0542 1.0007 0.1704 -0.1283 -0.2488 157 TYR B CG 3810 C CD1 . TYR B 157 ? 1.0254 1.0878 0.9744 0.1644 -0.1466 -0.2484 157 TYR B CD1 3811 C CD2 . TYR B 157 ? 1.1298 1.0490 0.9609 0.2223 -0.1260 -0.2554 157 TYR B CD2 3812 C CE1 . TYR B 157 ? 1.0052 1.1218 0.9234 0.2068 -0.1590 -0.2522 157 TYR B CE1 3813 C CE2 . TYR B 157 ? 1.1066 1.0908 0.9139 0.2631 -0.1390 -0.2589 157 TYR B CE2 3814 C CZ . TYR B 157 ? 1.0407 1.1192 0.8910 0.2539 -0.1541 -0.2565 157 TYR B CZ 3815 O OH . TYR B 157 ? 1.0175 1.1553 0.8382 0.3006 -0.1592 -0.2528 157 TYR B OH 3816 N N . ASP B 158 ? 1.4501 1.2540 1.3460 0.0518 -0.1792 -0.3605 158 ASP B N 3817 C CA . ASP B 158 ? 1.6300 1.3410 1.4438 0.0577 -0.2061 -0.4167 158 ASP B CA 3818 C C . ASP B 158 ? 1.6544 1.3894 1.3875 0.1433 -0.2122 -0.4156 158 ASP B C 3819 O O . ASP B 158 ? 1.6190 1.4563 1.3572 0.1668 -0.2393 -0.4267 158 ASP B O 3820 C CB . ASP B 158 ? 1.6695 1.4311 1.5298 -0.0036 -0.2534 -0.4697 158 ASP B CB 3821 C CG . ASP B 158 ? 1.8414 1.4507 1.6432 -0.0461 -0.2712 -0.5299 158 ASP B CG 3822 O OD1 . ASP B 158 ? 1.9060 1.4008 1.7198 -0.0945 -0.2394 -0.5193 158 ASP B OD1 3823 O OD2 . ASP B 158 ? 1.9402 1.5328 1.6750 -0.0281 -0.3145 -0.5873 158 ASP B OD2 3824 N N . TYR B 159 ? 1.7414 1.3901 1.4005 0.1954 -0.1824 -0.3964 159 TYR B N 3825 C CA . TYR B 159 ? 1.7560 1.4435 1.3509 0.2793 -0.1778 -0.3823 159 TYR B CA 3826 C C . TYR B 159 ? 1.8741 1.5518 1.3936 0.3124 -0.2127 -0.4314 159 TYR B C 3827 O O . TYR B 159 ? 1.8321 1.6210 1.3552 0.3546 -0.2212 -0.4189 159 TYR B O 3828 C CB . TYR B 159 ? 1.8125 1.4126 1.3379 0.3323 -0.1417 -0.3572 159 TYR B CB 3829 C CG . TYR B 159 ? 1.8451 1.4705 1.2905 0.4221 -0.1368 -0.3501 159 TYR B CG 3830 C CD1 . TYR B 159 ? 1.7226 1.4828 1.2117 0.4600 -0.1216 -0.3029 159 TYR B CD1 3831 C CD2 . TYR B 159 ? 2.0046 1.5177 1.3294 0.4687 -0.1457 -0.3903 159 TYR B CD2 3832 C CE1 . TYR B 159 ? 1.7521 1.5557 1.1819 0.5404 -0.1118 -0.2891 159 TYR B CE1 3833 C CE2 . TYR B 159 ? 2.0306 1.5777 1.2793 0.5614 -0.1361 -0.3777 159 TYR B CE2 3834 C CZ . TYR B 159 ? 1.8976 1.6006 1.2066 0.5963 -0.1173 -0.3236 159 TYR B CZ 3835 O OH . TYR B 159 ? 1.9188 1.6753 1.1662 0.6862 -0.1026 -0.3039 159 TYR B OH 3836 N N . PRO B 160 ? 2.0616 1.5983 1.5059 0.2948 -0.2313 -0.4876 160 PRO B N 3837 C CA . PRO B 160 ? 2.1896 1.7033 1.5417 0.3341 -0.2694 -0.5430 160 PRO B CA 3838 C C . PRO B 160 ? 2.1201 1.7740 1.5319 0.3107 -0.3127 -0.5658 160 PRO B C 3839 O O . PRO B 160 ? 2.1563 1.8582 1.5025 0.3750 -0.3333 -0.5832 160 PRO B O 3840 C CB . PRO B 160 ? 2.3910 1.7088 1.6673 0.2927 -0.2833 -0.6043 160 PRO B CB 3841 C CG . PRO B 160 ? 2.3889 1.6120 1.6846 0.2686 -0.2348 -0.5637 160 PRO B CG 3842 C CD . PRO B 160 ? 2.1746 1.5551 1.6064 0.2391 -0.2167 -0.5040 160 PRO B CD 3843 N N . GLN B 161 ? 2.0269 1.7511 1.5561 0.2296 -0.3228 -0.5612 161 GLN B N 3844 C CA . GLN B 161 ? 1.9478 1.8211 1.5405 0.2122 -0.3609 -0.5761 161 GLN B CA 3845 C C . GLN B 161 ? 1.8066 1.8077 1.3973 0.2897 -0.3441 -0.5262 161 GLN B C 3846 O O . GLN B 161 ? 1.8022 1.8966 1.3775 0.3221 -0.3740 -0.5440 161 GLN B O 3847 C CB . GLN B 161 ? 1.8691 1.8108 1.5948 0.1252 -0.3593 -0.5595 161 GLN B CB 3848 C CG . GLN B 161 ? 1.8636 1.9362 1.6493 0.0912 -0.4100 -0.5967 161 GLN B CG 3849 C CD . GLN B 161 ? 1.7540 1.9257 1.6743 0.0256 -0.3980 -0.5628 161 GLN B CD 3850 O OE1 . GLN B 161 ? 1.8198 1.9967 1.8068 -0.0562 -0.4209 -0.5968 161 GLN B OE1 3851 N NE2 . GLN B 161 ? 1.6048 1.8543 1.5649 0.0610 -0.3603 -0.4951 161 GLN B NE2 3852 N N . TYR B 162 ? 1.6804 1.6854 1.2868 0.3179 -0.2955 -0.4635 162 TYR B N 3853 C CA . TYR B 162 ? 1.5673 1.6716 1.1730 0.3827 -0.2707 -0.4118 162 TYR B CA 3854 C C . TYR B 162 ? 1.5884 1.6379 1.1080 0.4530 -0.2450 -0.3969 162 TYR B C 3855 O O . TYR B 162 ? 1.5697 1.6653 1.0309 0.5239 -0.2420 -0.3889 162 TYR B O 3856 C CB . TYR B 162 ? 1.4299 1.5997 1.1344 0.3519 -0.2378 -0.3523 162 TYR B CB 3857 C CG . TYR B 162 ? 1.3796 1.5990 1.1702 0.2878 -0.2531 -0.3572 162 TYR B CG 3858 C CD1 . TYR B 162 ? 1.3425 1.6719 1.1598 0.2999 -0.2702 -0.3544 162 TYR B CD1 3859 C CD2 . TYR B 162 ? 1.3643 1.5284 1.2068 0.2245 -0.2449 -0.3576 162 TYR B CD2 3860 C CE1 . TYR B 162 ? 1.2827 1.6754 1.1791 0.2516 -0.2816 -0.3540 162 TYR B CE1 3861 C CE2 . TYR B 162 ? 1.3061 1.5316 1.2320 0.1719 -0.2534 -0.3550 162 TYR B CE2 3862 C CZ . TYR B 162 ? 1.2648 1.6097 1.2193 0.1861 -0.2729 -0.3537 162 TYR B CZ 3863 O OH . TYR B 162 ? 1.1999 1.6224 1.2369 0.1437 -0.2795 -0.3472 162 TYR B OH # _database_PDB_caveat.id 1 _database_PDB_caveat.text 'NAG B1163 HAS WRONG CHIRALITY AT ATOM C1' # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 ASP 1 1 1 ASP ASP A . n A 1 2 GLN 2 2 2 GLN GLN A . n A 1 3 ILE 3 3 3 ILE ILE A . n A 1 4 CYS 4 4 4 CYS CYS A . n A 1 5 ILE 5 5 5 ILE ILE A . n A 1 6 GLY 6 6 6 GLY GLY A . n A 1 7 TYR 7 7 7 TYR TYR A . n A 1 8 HIS 8 8 8 HIS HIS A . n A 1 9 ALA 9 9 9 ALA ALA A . n A 1 10 ASN 10 10 10 ASN ASN A . n A 1 11 ASN 11 11 11 ASN ASN A . n A 1 12 SER 12 12 12 SER SER A . n A 1 13 THR 13 13 13 THR THR A . n A 1 14 GLU 14 14 14 GLU GLU A . n A 1 15 GLN 15 15 15 GLN GLN A . n A 1 16 VAL 16 16 16 VAL VAL A . n A 1 17 ASP 17 17 17 ASP ASP A . n A 1 18 THR 18 18 18 THR THR A . n A 1 19 ILE 19 19 19 ILE ILE A . n A 1 20 MET 20 20 20 MET MET A . n A 1 21 GLU 21 21 21 GLU GLU A . n A 1 22 LYS 22 22 22 LYS LYS A . n A 1 23 ASN 23 23 23 ASN ASN A . n A 1 24 VAL 24 24 24 VAL VAL A . n A 1 25 THR 25 25 25 THR THR A . n A 1 26 VAL 26 26 26 VAL VAL A . n A 1 27 THR 27 27 27 THR THR A . n A 1 28 HIS 28 28 28 HIS HIS A . n A 1 29 ALA 29 29 29 ALA ALA A . n A 1 30 GLN 30 30 30 GLN GLN A . n A 1 31 ASP 31 31 31 ASP ASP A . n A 1 32 ILE 32 32 32 ILE ILE A . n A 1 33 LEU 33 33 33 LEU LEU A . n A 1 34 GLU 34 34 34 GLU GLU A . n A 1 35 LYS 35 35 35 LYS LYS A . n A 1 36 THR 36 36 36 THR THR A . n A 1 37 HIS 37 37 37 HIS HIS A . n A 1 38 ASN 38 38 38 ASN ASN A . n A 1 39 GLY 39 39 39 GLY GLY A . n A 1 40 LYS 40 40 40 LYS LYS A . n A 1 41 LEU 41 41 41 LEU LEU A . n A 1 42 CYS 42 42 42 CYS CYS A . n A 1 43 ASP 43 43 43 ASP ASP A . n A 1 44 LEU 44 44 44 LEU LEU A . n A 1 45 ASP 45 45 45 ASP ASP A . n A 1 46 GLY 46 46 46 GLY GLY A . n A 1 47 VAL 47 47 47 VAL VAL A . n A 1 48 LYS 48 48 48 LYS LYS A . n A 1 49 PRO 49 49 49 PRO PRO A . n A 1 50 LEU 50 50 50 LEU LEU A . n A 1 51 ILE 51 51 51 ILE ILE A . n A 1 52 LEU 52 52 52 LEU LEU A . n A 1 53 ARG 53 53 53 ARG ARG A . n A 1 54 ASP 54 54 54 ASP ASP A . n A 1 55 CYS 55 55 55 CYS CYS A . n A 1 56 SER 56 56 56 SER SER A . n A 1 57 VAL 57 57 57 VAL VAL A . n A 1 58 ALA 58 58 58 ALA ALA A . n A 1 59 GLY 59 59 59 GLY GLY A . n A 1 60 TRP 60 60 60 TRP TRP A . n A 1 61 LEU 61 61 61 LEU LEU A . n A 1 62 LEU 62 62 62 LEU LEU A . n A 1 63 GLY 63 63 63 GLY GLY A . n A 1 64 ASN 64 64 64 ASN ASN A . n A 1 65 PRO 65 65 65 PRO PRO A . n A 1 66 MET 66 66 66 MET MET A . n A 1 67 CYS 67 67 67 CYS CYS A . n A 1 68 ASP 68 68 68 ASP ASP A . n A 1 69 GLU 69 69 69 GLU GLU A . n A 1 70 PHE 70 70 70 PHE PHE A . n A 1 71 ILE 71 71 71 ILE ILE A . n A 1 72 ASN 72 72 72 ASN ASN A . n A 1 73 VAL 73 73 73 VAL VAL A . n A 1 74 PRO 74 74 74 PRO PRO A . n A 1 75 GLU 75 75 75 GLU GLU A . n A 1 76 TRP 76 76 76 TRP TRP A . n A 1 77 SER 77 77 77 SER SER A . n A 1 78 TYR 78 78 78 TYR TYR A . n A 1 79 ILE 79 79 79 ILE ILE A . n A 1 80 VAL 80 80 80 VAL VAL A . n A 1 81 GLU 81 81 81 GLU GLU A . n A 1 82 LYS 82 82 82 LYS LYS A . n A 1 83 ALA 83 83 83 ALA ALA A . n A 1 84 ASN 84 84 84 ASN ASN A . n A 1 85 PRO 85 85 85 PRO PRO A . n A 1 86 VAL 86 86 86 VAL VAL A . n A 1 87 ASN 87 87 87 ASN ASN A . n A 1 88 ASP 88 88 88 ASP ASP A . n A 1 89 LEU 89 89 89 LEU LEU A . n A 1 90 CYS 90 90 90 CYS CYS A . n A 1 91 TYR 91 91 91 TYR TYR A . n A 1 92 PRO 92 92 92 PRO PRO A . n A 1 93 GLY 93 93 93 GLY GLY A . n A 1 94 ASP 94 94 94 ASP ASP A . n A 1 95 PHE 95 95 95 PHE PHE A . n A 1 96 ASN 96 96 96 ASN ASN A . n A 1 97 ASP 97 97 97 ASP ASP A . n A 1 98 TYR 98 98 98 TYR TYR A . n A 1 99 GLU 99 99 99 GLU GLU A . n A 1 100 GLU 100 100 100 GLU GLU A . n A 1 101 LEU 101 101 101 LEU LEU A . n A 1 102 LYS 102 102 102 LYS LYS A . n A 1 103 HIS 103 103 103 HIS HIS A . n A 1 104 LEU 104 104 104 LEU LEU A . n A 1 105 LEU 105 105 105 LEU LEU A . n A 1 106 SER 106 106 106 SER SER A . n A 1 107 ARG 107 107 107 ARG ARG A . n A 1 108 ILE 108 108 108 ILE ILE A . n A 1 109 ASN 109 109 109 ASN ASN A . n A 1 110 HIS 110 110 110 HIS HIS A . n A 1 111 PHE 111 111 111 PHE PHE A . n A 1 112 GLU 112 112 112 GLU GLU A . n A 1 113 LYS 113 113 113 LYS LYS A . n A 1 114 ILE 114 114 114 ILE ILE A . n A 1 115 GLN 115 115 115 GLN GLN A . n A 1 116 ILE 116 116 116 ILE ILE A . n A 1 117 ILE 117 117 117 ILE ILE A . n A 1 118 PRO 118 118 118 PRO PRO A . n A 1 119 LYS 119 119 119 LYS LYS A . n A 1 120 SER 120 120 120 SER SER A . n A 1 121 SER 121 121 121 SER SER A . n A 1 122 TRP 122 122 122 TRP TRP A . n A 1 123 SER 123 123 123 SER SER A . n A 1 124 SER 124 124 124 SER SER A . n A 1 125 HIS 125 125 125 HIS HIS A . n A 1 126 GLU 126 126 126 GLU GLU A . n A 1 127 ALA 127 127 127 ALA ALA A . n A 1 128 SER 128 128 128 SER SER A . n A 1 129 LEU 129 129 129 LEU LEU A . n A 1 130 GLY 130 130 130 GLY GLY A . n A 1 131 VAL 131 131 131 VAL VAL A . n A 1 132 SER 132 132 132 SER SER A . n A 1 133 SER 133 133 133 SER SER A . n A 1 134 ALA 134 134 134 ALA ALA A . n A 1 135 CYS 135 135 135 CYS CYS A . n A 1 136 PRO 136 136 136 PRO PRO A . n A 1 137 TYR 137 137 137 TYR TYR A . n A 1 138 GLN 138 138 138 GLN GLN A . n A 1 139 GLY 139 139 139 GLY GLY A . n A 1 140 LYS 140 140 140 LYS LYS A . n A 1 141 SER 141 141 141 SER SER A . n A 1 142 SER 142 142 142 SER SER A . n A 1 143 PHE 143 143 143 PHE PHE A . n A 1 144 PHE 144 144 144 PHE PHE A . n A 1 145 ARG 145 145 145 ARG ARG A . n A 1 146 ASN 146 146 146 ASN ASN A . n A 1 147 VAL 147 147 147 VAL VAL A . n A 1 148 VAL 148 148 148 VAL VAL A . n A 1 149 TRP 149 149 149 TRP TRP A . n A 1 150 LEU 150 150 150 LEU LEU A . n A 1 151 ILE 151 151 151 ILE ILE A . n A 1 152 LYS 152 152 152 LYS LYS A . n A 1 153 LYS 153 153 153 LYS LYS A . n A 1 154 ASN 154 154 154 ASN ASN A . n A 1 155 SER 155 155 155 SER SER A . n A 1 156 THR 156 156 156 THR THR A . n A 1 157 TYR 157 157 157 TYR TYR A . n A 1 158 PRO 158 158 158 PRO PRO A . n A 1 159 THR 159 159 159 THR THR A . n A 1 160 ILE 160 160 160 ILE ILE A . n A 1 161 LYS 161 161 161 LYS LYS A . n A 1 162 ARG 162 162 162 ARG ARG A . n A 1 163 SER 163 163 163 SER SER A . n A 1 164 TYR 164 164 164 TYR TYR A . n A 1 165 ASN 165 165 165 ASN ASN A . n A 1 166 ASN 166 166 166 ASN ASN A . n A 1 167 THR 167 167 167 THR THR A . n A 1 168 ASN 168 168 168 ASN ASN A . n A 1 169 GLN 169 169 169 GLN GLN A . n A 1 170 GLU 170 170 170 GLU GLU A . n A 1 171 ASP 171 171 171 ASP ASP A . n A 1 172 LEU 172 172 172 LEU LEU A . n A 1 173 LEU 173 173 173 LEU LEU A . n A 1 174 VAL 174 174 174 VAL VAL A . n A 1 175 LEU 175 175 175 LEU LEU A . n A 1 176 TRP 176 176 176 TRP TRP A . n A 1 177 GLY 177 177 177 GLY GLY A . n A 1 178 ILE 178 178 178 ILE ILE A . n A 1 179 HIS 179 179 179 HIS HIS A . n A 1 180 HIS 180 180 180 HIS HIS A . n A 1 181 PRO 181 181 181 PRO PRO A . n A 1 182 LYS 182 182 182 LYS LYS A . n A 1 183 ASP 183 183 183 ASP ASP A . n A 1 184 ALA 184 184 184 ALA ALA A . n A 1 185 ALA 185 185 185 ALA ALA A . n A 1 186 GLU 186 186 186 GLU GLU A . n A 1 187 GLN 187 187 187 GLN GLN A . n A 1 188 THR 188 188 188 THR THR A . n A 1 189 LYS 189 189 189 LYS LYS A . n A 1 190 LEU 190 190 190 LEU LEU A . n A 1 191 TYR 191 191 191 TYR TYR A . n A 1 192 GLN 192 192 192 GLN GLN A . n A 1 193 ASN 193 193 193 ASN ASN A . n A 1 194 PRO 194 194 194 PRO PRO A . n A 1 195 THR 195 195 195 THR THR A . n A 1 196 THR 196 196 196 THR THR A . n A 1 197 TYR 197 197 197 TYR TYR A . n A 1 198 ILE 198 198 198 ILE ILE A . n A 1 199 SER 199 199 199 SER SER A . n A 1 200 VAL 200 200 200 VAL VAL A . n A 1 201 GLY 201 201 201 GLY GLY A . n A 1 202 THR 202 202 202 THR THR A . n A 1 203 SER 203 203 203 SER SER A . n A 1 204 THR 204 204 204 THR THR A . n A 1 205 LEU 205 205 205 LEU LEU A . n A 1 206 ASN 206 206 206 ASN ASN A . n A 1 207 GLN 207 207 207 GLN GLN A . n A 1 208 ARG 208 208 208 ARG ARG A . n A 1 209 LEU 209 209 209 LEU LEU A . n A 1 210 VAL 210 210 210 VAL VAL A . n A 1 211 PRO 211 211 211 PRO PRO A . n A 1 212 ARG 212 212 212 ARG ARG A . n A 1 213 ILE 213 213 213 ILE ILE A . n A 1 214 ALA 214 214 214 ALA ALA A . n A 1 215 THR 215 215 215 THR THR A . n A 1 216 ARG 216 216 216 ARG ARG A . n A 1 217 SER 217 217 217 SER SER A . n A 1 218 LYS 218 218 218 LYS LYS A . n A 1 219 VAL 219 219 219 VAL VAL A . n A 1 220 ASN 220 220 220 ASN ASN A . n A 1 221 GLY 221 221 221 GLY GLY A . n A 1 222 GLN 222 222 222 GLN GLN A . n A 1 223 SER 223 223 223 SER SER A . n A 1 224 GLY 224 224 224 GLY GLY A . n A 1 225 ARG 225 225 225 ARG ARG A . n A 1 226 MET 226 226 226 MET MET A . n A 1 227 GLU 227 227 227 GLU GLU A . n A 1 228 PHE 228 228 228 PHE PHE A . n A 1 229 PHE 229 229 229 PHE PHE A . n A 1 230 TRP 230 230 230 TRP TRP A . n A 1 231 THR 231 231 231 THR THR A . n A 1 232 ILE 232 232 232 ILE ILE A . n A 1 233 LEU 233 233 233 LEU LEU A . n A 1 234 LYS 234 234 234 LYS LYS A . n A 1 235 PRO 235 235 235 PRO PRO A . n A 1 236 ASN 236 236 236 ASN ASN A . n A 1 237 ASP 237 237 237 ASP ASP A . n A 1 238 ALA 238 238 238 ALA ALA A . n A 1 239 ILE 239 239 239 ILE ILE A . n A 1 240 ASN 240 240 240 ASN ASN A . n A 1 241 PHE 241 241 241 PHE PHE A . n A 1 242 GLU 242 242 242 GLU GLU A . n A 1 243 SER 243 243 243 SER SER A . n A 1 244 ASN 244 244 244 ASN ASN A . n A 1 245 GLY 245 245 245 GLY GLY A . n A 1 246 ASN 246 246 246 ASN ASN A . n A 1 247 PHE 247 247 247 PHE PHE A . n A 1 248 ILE 248 248 248 ILE ILE A . n A 1 249 ALA 249 249 249 ALA ALA A . n A 1 250 PRO 250 250 250 PRO PRO A . n A 1 251 GLU 251 251 251 GLU GLU A . n A 1 252 TYR 252 252 252 TYR TYR A . n A 1 253 ALA 253 253 253 ALA ALA A . n A 1 254 TYR 254 254 254 TYR TYR A . n A 1 255 LYS 255 255 255 LYS LYS A . n A 1 256 ILE 256 256 256 ILE ILE A . n A 1 257 VAL 257 257 257 VAL VAL A . n A 1 258 LYS 258 258 258 LYS LYS A . n A 1 259 LYS 259 259 259 LYS LYS A . n A 1 260 GLY 260 260 260 GLY GLY A . n A 1 261 ASP 261 261 261 ASP ASP A . n A 1 262 SER 262 262 262 SER SER A . n A 1 263 THR 263 263 263 THR THR A . n A 1 264 ILE 264 264 264 ILE ILE A . n A 1 265 MET 265 265 265 MET MET A . n A 1 266 LYS 266 266 266 LYS LYS A . n A 1 267 SER 267 267 267 SER SER A . n A 1 268 GLU 268 268 268 GLU GLU A . n A 1 269 LEU 269 269 269 LEU LEU A . n A 1 270 GLU 270 270 270 GLU GLU A . n A 1 271 TYR 271 271 271 TYR TYR A . n A 1 272 GLY 272 272 272 GLY GLY A . n A 1 273 ASN 273 273 273 ASN ASN A . n A 1 274 CYS 274 274 274 CYS CYS A . n A 1 275 ASN 275 275 275 ASN ASN A . n A 1 276 THR 276 276 276 THR THR A . n A 1 277 LYS 277 277 277 LYS LYS A . n A 1 278 CYS 278 278 278 CYS CYS A . n A 1 279 GLN 279 279 279 GLN GLN A . n A 1 280 THR 280 280 280 THR THR A . n A 1 281 PRO 281 281 281 PRO PRO A . n A 1 282 MET 282 282 282 MET MET A . n A 1 283 GLY 283 283 283 GLY GLY A . n A 1 284 ALA 284 284 284 ALA ALA A . n A 1 285 ILE 285 285 285 ILE ILE A . n A 1 286 ASN 286 286 286 ASN ASN A . n A 1 287 SER 287 287 287 SER SER A . n A 1 288 SER 288 288 288 SER SER A . n A 1 289 MET 289 289 289 MET MET A . n A 1 290 PRO 290 290 290 PRO PRO A . n A 1 291 PHE 291 291 291 PHE PHE A . n A 1 292 HIS 292 292 292 HIS HIS A . n A 1 293 ASN 293 293 293 ASN ASN A . n A 1 294 ILE 294 294 294 ILE ILE A . n A 1 295 HIS 295 295 295 HIS HIS A . n A 1 296 PRO 296 296 296 PRO PRO A . n A 1 297 LEU 297 297 297 LEU LEU A . n A 1 298 THR 298 298 298 THR THR A . n A 1 299 ILE 299 299 299 ILE ILE A . n A 1 300 GLY 300 300 300 GLY GLY A . n A 1 301 GLU 301 301 301 GLU GLU A . n A 1 302 CYS 302 302 302 CYS CYS A . n A 1 303 PRO 303 303 303 PRO PRO A . n A 1 304 LYS 304 304 304 LYS LYS A . n A 1 305 TYR 305 305 305 TYR TYR A . n A 1 306 VAL 306 306 306 VAL VAL A . n A 1 307 LYS 307 307 307 LYS LYS A . n A 1 308 SER 308 308 308 SER SER A . n A 1 309 ASN 309 309 309 ASN ASN A . n A 1 310 ARG 310 310 310 ARG ARG A . n A 1 311 LEU 311 311 311 LEU LEU A . n A 1 312 VAL 312 312 312 VAL VAL A . n A 1 313 LEU 313 313 313 LEU LEU A . n A 1 314 ALA 314 314 314 ALA ALA A . n A 1 315 THR 315 315 315 THR THR A . n A 1 316 GLY 316 316 316 GLY GLY A . n A 1 317 LEU 317 317 317 LEU LEU A . n A 1 318 ARG 318 318 318 ARG ARG A . n A 1 319 ASN 319 319 319 ASN ASN A . n A 1 320 SER 320 320 320 SER SER A . n A 1 321 PRO 321 321 321 PRO PRO A . n A 1 322 GLN 322 322 ? ? ? A . n A 1 323 ARG 323 323 ? ? ? A . n A 1 324 GLU 324 324 ? ? ? A . n A 1 325 THR 325 325 ? ? ? A . n A 1 326 ARG 326 326 ? ? ? A . n B 2 1 GLY 1 1 1 GLY GLY B . n B 2 2 LEU 2 2 2 LEU LEU B . n B 2 3 PHE 3 3 3 PHE PHE B . n B 2 4 GLY 4 4 4 GLY GLY B . n B 2 5 ALA 5 5 5 ALA ALA B . n B 2 6 ILE 6 6 6 ILE ILE B . n B 2 7 ALA 7 7 7 ALA ALA B . n B 2 8 GLY 8 8 8 GLY GLY B . n B 2 9 PHE 9 9 9 PHE PHE B . n B 2 10 ILE 10 10 10 ILE ILE B . n B 2 11 GLU 11 11 11 GLU GLU B . n B 2 12 GLY 12 12 12 GLY GLY B . n B 2 13 GLY 13 13 13 GLY GLY B . n B 2 14 TRP 14 14 14 TRP TRP B . n B 2 15 GLN 15 15 15 GLN GLN B . n B 2 16 GLY 16 16 16 GLY GLY B . n B 2 17 MET 17 17 17 MET MET B . n B 2 18 VAL 18 18 18 VAL VAL B . n B 2 19 ASP 19 19 19 ASP ASP B . n B 2 20 GLY 20 20 20 GLY GLY B . n B 2 21 TRP 21 21 21 TRP TRP B . n B 2 22 TYR 22 22 22 TYR TYR B . n B 2 23 GLY 23 23 23 GLY GLY B . n B 2 24 TYR 24 24 24 TYR TYR B . n B 2 25 HIS 25 25 25 HIS HIS B . n B 2 26 HIS 26 26 26 HIS HIS B . n B 2 27 SER 27 27 27 SER SER B . n B 2 28 ASN 28 28 28 ASN ASN B . n B 2 29 GLU 29 29 29 GLU GLU B . n B 2 30 GLN 30 30 30 GLN GLN B . n B 2 31 GLY 31 31 31 GLY GLY B . n B 2 32 SER 32 32 32 SER SER B . n B 2 33 GLY 33 33 33 GLY GLY B . n B 2 34 TYR 34 34 34 TYR TYR B . n B 2 35 ALA 35 35 35 ALA ALA B . n B 2 36 ALA 36 36 36 ALA ALA B . n B 2 37 ASP 37 37 37 ASP ASP B . n B 2 38 LYS 38 38 38 LYS LYS B . n B 2 39 GLU 39 39 39 GLU GLU B . n B 2 40 SER 40 40 40 SER SER B . n B 2 41 THR 41 41 41 THR THR B . n B 2 42 GLN 42 42 42 GLN GLN B . n B 2 43 LYS 43 43 43 LYS LYS B . n B 2 44 ALA 44 44 44 ALA ALA B . n B 2 45 ILE 45 45 45 ILE ILE B . n B 2 46 ASP 46 46 46 ASP ASP B . n B 2 47 GLY 47 47 47 GLY GLY B . n B 2 48 VAL 48 48 48 VAL VAL B . n B 2 49 THR 49 49 49 THR THR B . n B 2 50 ASN 50 50 50 ASN ASN B . n B 2 51 LYS 51 51 51 LYS LYS B . n B 2 52 VAL 52 52 52 VAL VAL B . n B 2 53 ASN 53 53 53 ASN ASN B . n B 2 54 SER 54 54 54 SER SER B . n B 2 55 ILE 55 55 55 ILE ILE B . n B 2 56 ILE 56 56 56 ILE ILE B . n B 2 57 ASP 57 57 57 ASP ASP B . n B 2 58 LYS 58 58 58 LYS LYS B . n B 2 59 MET 59 59 59 MET MET B . n B 2 60 ASN 60 60 60 ASN ASN B . n B 2 61 THR 61 61 61 THR THR B . n B 2 62 GLN 62 62 62 GLN GLN B . n B 2 63 PHE 63 63 63 PHE PHE B . n B 2 64 GLU 64 64 64 GLU GLU B . n B 2 65 ALA 65 65 65 ALA ALA B . n B 2 66 VAL 66 66 66 VAL VAL B . n B 2 67 GLY 67 67 67 GLY GLY B . n B 2 68 ARG 68 68 68 ARG ARG B . n B 2 69 GLU 69 69 69 GLU GLU B . n B 2 70 PHE 70 70 70 PHE PHE B . n B 2 71 ASN 71 71 71 ASN ASN B . n B 2 72 ASN 72 72 72 ASN ASN B . n B 2 73 LEU 73 73 73 LEU LEU B . n B 2 74 GLU 74 74 74 GLU GLU B . n B 2 75 ARG 75 75 75 ARG ARG B . n B 2 76 ARG 76 76 76 ARG ARG B . n B 2 77 ILE 77 77 77 ILE ILE B . n B 2 78 GLU 78 78 78 GLU GLU B . n B 2 79 ASN 79 79 79 ASN ASN B . n B 2 80 LEU 80 80 80 LEU LEU B . n B 2 81 ASN 81 81 81 ASN ASN B . n B 2 82 LYS 82 82 82 LYS LYS B . n B 2 83 LYS 83 83 83 LYS LYS B . n B 2 84 MET 84 84 84 MET MET B . n B 2 85 GLU 85 85 85 GLU GLU B . n B 2 86 ASP 86 86 86 ASP ASP B . n B 2 87 GLY 87 87 87 GLY GLY B . n B 2 88 PHE 88 88 88 PHE PHE B . n B 2 89 LEU 89 89 89 LEU LEU B . n B 2 90 ASP 90 90 90 ASP ASP B . n B 2 91 VAL 91 91 91 VAL VAL B . n B 2 92 TRP 92 92 92 TRP TRP B . n B 2 93 THR 93 93 93 THR THR B . n B 2 94 TYR 94 94 94 TYR TYR B . n B 2 95 ASN 95 95 95 ASN ASN B . n B 2 96 ALA 96 96 96 ALA ALA B . n B 2 97 GLU 97 97 97 GLU GLU B . n B 2 98 LEU 98 98 98 LEU LEU B . n B 2 99 LEU 99 99 99 LEU LEU B . n B 2 100 VAL 100 100 100 VAL VAL B . n B 2 101 LEU 101 101 101 LEU LEU B . n B 2 102 MET 102 102 102 MET MET B . n B 2 103 GLU 103 103 103 GLU GLU B . n B 2 104 ASN 104 104 104 ASN ASN B . n B 2 105 GLU 105 105 105 GLU GLU B . n B 2 106 ARG 106 106 106 ARG ARG B . n B 2 107 THR 107 107 107 THR THR B . n B 2 108 LEU 108 108 108 LEU LEU B . n B 2 109 ASP 109 109 109 ASP ASP B . n B 2 110 PHE 110 110 110 PHE PHE B . n B 2 111 HIS 111 111 111 HIS HIS B . n B 2 112 ASP 112 112 112 ASP ASP B . n B 2 113 SER 113 113 113 SER SER B . n B 2 114 ASN 114 114 114 ASN ASN B . n B 2 115 VAL 115 115 115 VAL VAL B . n B 2 116 LYS 116 116 116 LYS LYS B . n B 2 117 ASN 117 117 117 ASN ASN B . n B 2 118 LEU 118 118 118 LEU LEU B . n B 2 119 TYR 119 119 119 TYR TYR B . n B 2 120 ASP 120 120 120 ASP ASP B . n B 2 121 LYS 121 121 121 LYS LYS B . n B 2 122 VAL 122 122 122 VAL VAL B . n B 2 123 ARG 123 123 123 ARG ARG B . n B 2 124 LEU 124 124 124 LEU LEU B . n B 2 125 GLN 125 125 125 GLN GLN B . n B 2 126 LEU 126 126 126 LEU LEU B . n B 2 127 ARG 127 127 127 ARG ARG B . n B 2 128 ASP 128 128 128 ASP ASP B . n B 2 129 ASN 129 129 129 ASN ASN B . n B 2 130 ALA 130 130 130 ALA ALA B . n B 2 131 LYS 131 131 131 LYS LYS B . n B 2 132 GLU 132 132 132 GLU GLU B . n B 2 133 LEU 133 133 133 LEU LEU B . n B 2 134 GLY 134 134 134 GLY GLY B . n B 2 135 ASN 135 135 135 ASN ASN B . n B 2 136 GLY 136 136 136 GLY GLY B . n B 2 137 CYS 137 137 137 CYS CYS B . n B 2 138 PHE 138 138 138 PHE PHE B . n B 2 139 GLU 139 139 139 GLU GLU B . n B 2 140 PHE 140 140 140 PHE PHE B . n B 2 141 TYR 141 141 141 TYR TYR B . n B 2 142 HIS 142 142 142 HIS HIS B . n B 2 143 LYS 143 143 143 LYS LYS B . n B 2 144 CYS 144 144 144 CYS CYS B . n B 2 145 ASP 145 145 145 ASP ASP B . n B 2 146 ASN 146 146 146 ASN ASN B . n B 2 147 GLU 147 147 147 GLU GLU B . n B 2 148 CYS 148 148 148 CYS CYS B . n B 2 149 MET 149 149 149 MET MET B . n B 2 150 GLU 150 150 150 GLU GLU B . n B 2 151 SER 151 151 151 SER SER B . n B 2 152 VAL 152 152 152 VAL VAL B . n B 2 153 ARG 153 153 153 ARG ARG B . n B 2 154 ASN 154 154 154 ASN ASN B . n B 2 155 GLY 155 155 155 GLY GLY B . n B 2 156 THR 156 156 156 THR THR B . n B 2 157 TYR 157 157 157 TYR TYR B . n B 2 158 ASP 158 158 158 ASP ASP B . n B 2 159 TYR 159 159 159 TYR TYR B . n B 2 160 PRO 160 160 160 PRO PRO B . n B 2 161 GLN 161 161 161 GLN GLN B . n B 2 162 TYR 162 162 162 TYR TYR B . n B 2 163 SER 163 163 ? ? ? B . n B 2 164 GLU 164 164 ? ? ? B . n B 2 165 GLU 165 165 ? ? ? B . n B 2 166 ALA 166 166 ? ? ? B . n # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code C 3 NAG 1 1322 1322 NAG NAG A . D 3 NAG 1 1323 1323 NAG NAG A . E 3 NAG 2 1324 1324 NAG NAG A . F 3 NAG 1 1325 1325 NAG NAG A . G 3 NAG 2 1326 1326 NAG NAG A . H 4 MAN 3 1327 1327 MAN MAN A . I 5 BMA 4 1328 1328 BMA BMA A . J 4 MAN 5 1329 1329 MAN MAN A . K 3 NAG 1 1330 1330 NAG NAG A . L 6 MPO 1 1331 1331 MPO MPO A . M 3 NAG 1 1163 1163 NAG NAG B . N 3 NAG 2 1164 1164 NAG NAG B . O 5 BMA 3 1165 1165 BMA BMA B . P 6 MPO 1 1166 1166 MPO MPO B . Q 7 HOH 1 2001 2001 HOH HOH A . Q 7 HOH 2 2002 2002 HOH HOH A . Q 7 HOH 3 2003 2003 HOH HOH A . Q 7 HOH 4 2004 2004 HOH HOH A . Q 7 HOH 5 2005 2005 HOH HOH A . Q 7 HOH 6 2006 2006 HOH HOH A . Q 7 HOH 7 2007 2007 HOH HOH A . Q 7 HOH 8 2008 2008 HOH HOH A . Q 7 HOH 9 2009 2009 HOH HOH A . Q 7 HOH 10 2010 2010 HOH HOH A . Q 7 HOH 11 2011 2011 HOH HOH A . Q 7 HOH 12 2012 2012 HOH HOH A . Q 7 HOH 13 2013 2013 HOH HOH A . Q 7 HOH 14 2014 2014 HOH HOH A . Q 7 HOH 15 2015 2015 HOH HOH A . Q 7 HOH 16 2016 2016 HOH HOH A . Q 7 HOH 17 2017 2017 HOH HOH A . Q 7 HOH 18 2018 2018 HOH HOH A . Q 7 HOH 19 2019 2019 HOH HOH A . Q 7 HOH 20 2020 2020 HOH HOH A . Q 7 HOH 21 2021 2021 HOH HOH A . Q 7 HOH 22 2022 2022 HOH HOH A . Q 7 HOH 23 2023 2023 HOH HOH A . Q 7 HOH 24 2024 2024 HOH HOH A . Q 7 HOH 25 2025 2025 HOH HOH A . Q 7 HOH 26 2026 2026 HOH HOH A . Q 7 HOH 27 2027 2027 HOH HOH A . Q 7 HOH 28 2028 2028 HOH HOH A . Q 7 HOH 29 2029 2029 HOH HOH A . Q 7 HOH 30 2030 2030 HOH HOH A . Q 7 HOH 31 2031 2031 HOH HOH A . Q 7 HOH 32 2032 2032 HOH HOH A . Q 7 HOH 33 2033 2033 HOH HOH A . Q 7 HOH 34 2034 2034 HOH HOH A . Q 7 HOH 35 2035 2035 HOH HOH A . Q 7 HOH 36 2036 2036 HOH HOH A . Q 7 HOH 37 2037 2037 HOH HOH A . Q 7 HOH 38 2038 2038 HOH HOH A . Q 7 HOH 39 2039 2039 HOH HOH A . Q 7 HOH 40 2040 2040 HOH HOH A . Q 7 HOH 41 2041 2041 HOH HOH A . Q 7 HOH 42 2042 2042 HOH HOH A . Q 7 HOH 43 2043 2043 HOH HOH A . Q 7 HOH 44 2044 2044 HOH HOH A . Q 7 HOH 45 2045 2045 HOH HOH A . Q 7 HOH 46 2046 2046 HOH HOH A . Q 7 HOH 47 2047 2047 HOH HOH A . Q 7 HOH 48 2048 2048 HOH HOH A . Q 7 HOH 49 2049 2049 HOH HOH A . Q 7 HOH 50 2050 2050 HOH HOH A . Q 7 HOH 51 2051 2051 HOH HOH A . Q 7 HOH 52 2052 2052 HOH HOH A . Q 7 HOH 53 2053 2053 HOH HOH A . Q 7 HOH 54 2054 2054 HOH HOH A . Q 7 HOH 55 2055 2055 HOH HOH A . Q 7 HOH 56 2056 2056 HOH HOH A . Q 7 HOH 57 2057 2057 HOH HOH A . Q 7 HOH 58 2058 2058 HOH HOH A . Q 7 HOH 59 2059 2059 HOH HOH A . Q 7 HOH 60 2060 2060 HOH HOH A . Q 7 HOH 61 2061 2061 HOH HOH A . Q 7 HOH 62 2062 2062 HOH HOH A . Q 7 HOH 63 2063 2063 HOH HOH A . Q 7 HOH 64 2064 2064 HOH HOH A . Q 7 HOH 65 2065 2065 HOH HOH A . Q 7 HOH 66 2066 2066 HOH HOH A . Q 7 HOH 67 2067 2067 HOH HOH A . Q 7 HOH 68 2068 2068 HOH HOH A . Q 7 HOH 69 2069 2069 HOH HOH A . Q 7 HOH 70 2070 2070 HOH HOH A . Q 7 HOH 71 2071 2071 HOH HOH A . Q 7 HOH 72 2072 2072 HOH HOH A . Q 7 HOH 73 2073 2073 HOH HOH A . Q 7 HOH 74 2074 2074 HOH HOH A . Q 7 HOH 75 2075 2075 HOH HOH A . Q 7 HOH 76 2076 2076 HOH HOH A . Q 7 HOH 77 2077 2077 HOH HOH A . Q 7 HOH 78 2078 2078 HOH HOH A . Q 7 HOH 79 2079 2079 HOH HOH A . Q 7 HOH 80 2080 2080 HOH HOH A . Q 7 HOH 81 2081 2081 HOH HOH A . Q 7 HOH 82 2082 2082 HOH HOH A . Q 7 HOH 83 2083 2083 HOH HOH A . Q 7 HOH 84 2084 2084 HOH HOH A . Q 7 HOH 85 2085 2085 HOH HOH A . Q 7 HOH 86 2086 2086 HOH HOH A . Q 7 HOH 87 2087 2087 HOH HOH A . Q 7 HOH 88 2088 2088 HOH HOH A . Q 7 HOH 89 2089 2089 HOH HOH A . Q 7 HOH 90 2090 2090 HOH HOH A . Q 7 HOH 91 2091 2091 HOH HOH A . Q 7 HOH 92 2092 2092 HOH HOH A . Q 7 HOH 93 2093 2093 HOH HOH A . Q 7 HOH 94 2094 2094 HOH HOH A . Q 7 HOH 95 2095 2095 HOH HOH A . Q 7 HOH 96 2096 2096 HOH HOH A . Q 7 HOH 97 2097 2097 HOH HOH A . Q 7 HOH 98 2098 2098 HOH HOH A . Q 7 HOH 99 2099 2099 HOH HOH A . Q 7 HOH 100 2100 2100 HOH HOH A . Q 7 HOH 101 2101 2101 HOH HOH A . Q 7 HOH 102 2102 2102 HOH HOH A . Q 7 HOH 103 2103 2103 HOH HOH A . Q 7 HOH 104 2104 2104 HOH HOH A . Q 7 HOH 105 2105 2105 HOH HOH A . R 7 HOH 1 2001 2001 HOH HOH B . R 7 HOH 2 2002 2002 HOH HOH B . R 7 HOH 3 2003 2003 HOH HOH B . R 7 HOH 4 2004 2004 HOH HOH B . R 7 HOH 5 2005 2005 HOH HOH B . R 7 HOH 6 2006 2006 HOH HOH B . R 7 HOH 7 2007 2007 HOH HOH B . R 7 HOH 8 2008 2008 HOH HOH B . R 7 HOH 9 2009 2009 HOH HOH B . R 7 HOH 10 2010 2010 HOH HOH B . R 7 HOH 11 2011 2011 HOH HOH B . R 7 HOH 12 2012 2012 HOH HOH B . R 7 HOH 13 2013 2013 HOH HOH B . R 7 HOH 14 2014 2014 HOH HOH B . R 7 HOH 15 2015 2015 HOH HOH B . R 7 HOH 16 2016 2016 HOH HOH B . R 7 HOH 17 2017 2017 HOH HOH B . R 7 HOH 18 2018 2018 HOH HOH B . R 7 HOH 19 2019 2019 HOH HOH B . R 7 HOH 20 2020 2020 HOH HOH B . R 7 HOH 21 2021 2021 HOH HOH B . R 7 HOH 22 2022 2022 HOH HOH B . R 7 HOH 23 2023 2023 HOH HOH B . R 7 HOH 24 2024 2024 HOH HOH B . R 7 HOH 25 2025 2025 HOH HOH B . R 7 HOH 26 2026 2026 HOH HOH B . R 7 HOH 27 2027 2027 HOH HOH B . R 7 HOH 28 2028 2028 HOH HOH B . R 7 HOH 29 2029 2029 HOH HOH B . R 7 HOH 30 2030 2030 HOH HOH B . R 7 HOH 31 2031 2031 HOH HOH B . R 7 HOH 32 2032 2032 HOH HOH B . R 7 HOH 33 2033 2033 HOH HOH B . R 7 HOH 34 2034 2034 HOH HOH B . R 7 HOH 35 2035 2035 HOH HOH B . R 7 HOH 36 2036 2036 HOH HOH B . R 7 HOH 37 2037 2037 HOH HOH B . R 7 HOH 38 2038 2038 HOH HOH B . R 7 HOH 39 2039 2039 HOH HOH B . R 7 HOH 40 2040 2040 HOH HOH B . R 7 HOH 41 2041 2041 HOH HOH B . R 7 HOH 42 2042 2042 HOH HOH B . R 7 HOH 43 2043 2043 HOH HOH B . R 7 HOH 44 2044 2044 HOH HOH B . R 7 HOH 45 2045 2045 HOH HOH B . R 7 HOH 46 2046 2046 HOH HOH B . R 7 HOH 47 2047 2047 HOH HOH B . R 7 HOH 48 2048 2048 HOH HOH B . R 7 HOH 49 2049 2049 HOH HOH B . R 7 HOH 50 2050 2050 HOH HOH B . R 7 HOH 51 2051 2051 HOH HOH B . R 7 HOH 52 2052 2052 HOH HOH B . R 7 HOH 53 2053 2053 HOH HOH B . R 7 HOH 54 2054 2054 HOH HOH B . R 7 HOH 55 2055 2055 HOH HOH B . R 7 HOH 56 2056 2056 HOH HOH B . R 7 HOH 57 2057 2057 HOH HOH B . R 7 HOH 58 2058 2058 HOH HOH B . R 7 HOH 59 2059 2059 HOH HOH B . # loop_ _pdbx_struct_mod_residue.id _pdbx_struct_mod_residue.label_asym_id _pdbx_struct_mod_residue.label_comp_id _pdbx_struct_mod_residue.label_seq_id _pdbx_struct_mod_residue.auth_asym_id _pdbx_struct_mod_residue.auth_comp_id _pdbx_struct_mod_residue.auth_seq_id _pdbx_struct_mod_residue.PDB_ins_code _pdbx_struct_mod_residue.parent_comp_id _pdbx_struct_mod_residue.details 1 A ASN 11 A ASN 11 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 23 A ASN 23 ? ASN 'GLYCOSYLATION SITE' 3 A ASN 165 A ASN 165 ? ASN 'GLYCOSYLATION SITE' 4 A ASN 286 A ASN 286 ? ASN 'GLYCOSYLATION SITE' 5 B ASN 154 B ASN 154 ? ASN 'GLYCOSYLATION SITE' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_and_software_defined_assembly _pdbx_struct_assembly.method_details PISA _pdbx_struct_assembly.oligomeric_details hexameric _pdbx_struct_assembly.oligomeric_count 6 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1,2,3 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R # 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)' 36270 ? 1 MORE -27.5 ? 1 'SSA (A^2)' 64030 ? # loop_ _pdbx_struct_oper_list.id _pdbx_struct_oper_list.type _pdbx_struct_oper_list.name _pdbx_struct_oper_list.symmetry_operation _pdbx_struct_oper_list.matrix[1][1] _pdbx_struct_oper_list.matrix[1][2] _pdbx_struct_oper_list.matrix[1][3] _pdbx_struct_oper_list.vector[1] _pdbx_struct_oper_list.matrix[2][1] _pdbx_struct_oper_list.matrix[2][2] _pdbx_struct_oper_list.matrix[2][3] _pdbx_struct_oper_list.vector[2] _pdbx_struct_oper_list.matrix[3][1] _pdbx_struct_oper_list.matrix[3][2] _pdbx_struct_oper_list.matrix[3][3] _pdbx_struct_oper_list.vector[3] 1 'identity operation' 1_555 x,y,z 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 2 'crystal symmetry operation' 2_545 -y,x-y-1,z -0.5000000000 -0.8660254038 0.0000000000 50.6005000000 0.8660254038 -0.5000000000 0.0000000000 -87.6426368884 0.0000000000 0.0000000000 1.0000000000 0.0000000000 3 'crystal symmetry operation' 3_655 -x+y+1,-x,z -0.5000000000 0.8660254038 0.0000000000 101.2010000000 -0.8660254038 -0.5000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 # _pdbx_struct_special_symmetry.id 1 _pdbx_struct_special_symmetry.PDB_model_num 1 _pdbx_struct_special_symmetry.auth_asym_id B _pdbx_struct_special_symmetry.auth_comp_id HOH _pdbx_struct_special_symmetry.auth_seq_id 2019 _pdbx_struct_special_symmetry.PDB_ins_code ? _pdbx_struct_special_symmetry.label_asym_id R _pdbx_struct_special_symmetry.label_comp_id HOH _pdbx_struct_special_symmetry.label_seq_id . # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 2014-05-28 2 'Structure model' 1 1 2014-06-11 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # _pdbx_audit_revision_group.ordinal 1 _pdbx_audit_revision_group.revision_ordinal 2 _pdbx_audit_revision_group.data_content_type 'Structure model' _pdbx_audit_revision_group.group 'Database references' # loop_ _pdbx_refine_tls.pdbx_refine_id _pdbx_refine_tls.id _pdbx_refine_tls.details _pdbx_refine_tls.method _pdbx_refine_tls.origin_x _pdbx_refine_tls.origin_y _pdbx_refine_tls.origin_z _pdbx_refine_tls.T[1][1] _pdbx_refine_tls.T[2][2] _pdbx_refine_tls.T[3][3] _pdbx_refine_tls.T[1][2] _pdbx_refine_tls.T[1][3] _pdbx_refine_tls.T[2][3] _pdbx_refine_tls.L[1][1] _pdbx_refine_tls.L[2][2] _pdbx_refine_tls.L[3][3] _pdbx_refine_tls.L[1][2] _pdbx_refine_tls.L[1][3] _pdbx_refine_tls.L[2][3] _pdbx_refine_tls.S[1][1] _pdbx_refine_tls.S[1][2] _pdbx_refine_tls.S[1][3] _pdbx_refine_tls.S[2][1] _pdbx_refine_tls.S[2][2] _pdbx_refine_tls.S[2][3] _pdbx_refine_tls.S[3][1] _pdbx_refine_tls.S[3][2] _pdbx_refine_tls.S[3][3] 'X-RAY DIFFRACTION' 1 ? refined 34.3315 -13.9472 -18.7509 0.0561 0.3742 0.2091 -0.0094 0.0319 -0.1156 0.4325 0.2580 5.1949 -0.0072 -0.7144 0.7762 0.0417 -0.1712 0.0761 -0.0127 -0.2524 0.1096 -0.1143 -0.7594 0.2107 'X-RAY DIFFRACTION' 2 ? refined 32.1727 -21.4185 16.5998 0.4984 0.8139 0.0957 -0.1713 0.1466 -0.1308 1.5623 3.0280 3.3784 0.2815 0.4221 0.2313 -0.1009 -0.4014 0.0950 0.8760 -0.1460 0.1081 0.6724 -0.4868 0.2469 'X-RAY DIFFRACTION' 3 ? refined 35.5368 -14.6665 -26.9314 0.2049 0.1734 0.2814 0.0045 0.0292 -0.0690 1.4997 0.4032 11.8063 -0.2098 -1.4499 2.1494 0.1660 -0.3471 0.1871 0.0700 -0.0787 0.0157 0.5100 -0.2384 -0.0873 'X-RAY DIFFRACTION' 4 ? refined 36.1465 -20.9071 -58.7550 0.1334 0.2133 0.3367 0.0555 -0.0257 -0.0405 1.3533 1.8448 6.8248 -1.0483 1.8190 -1.0876 -0.0406 0.1035 0.0332 0.1160 -0.1104 0.0933 -0.1910 -0.7873 0.1510 'X-RAY DIFFRACTION' 5 ? refined 48.1038 -22.6464 -10.3648 0.1197 0.1257 0.0775 0.0187 0.0289 -0.0206 7.3223 5.3521 12.6748 1.5987 5.5643 2.2985 0.1830 -0.0487 -0.0289 0.3776 -0.2576 0.4252 -0.0658 -0.1932 0.0746 'X-RAY DIFFRACTION' 6 ? refined 44.5191 -23.8461 -56.7609 0.0797 0.1563 0.2594 0.0343 -0.0127 0.0036 1.4088 0.5953 14.9225 -0.7282 2.5958 -1.1516 0.0804 0.1601 0.0655 -0.0467 -0.2527 -0.0140 0.4215 0.2450 0.1722 'X-RAY DIFFRACTION' 7 ? refined 31.5501 -25.9591 -80.7636 0.4318 0.6832 0.5106 0.1171 -0.1676 -0.2357 7.3612 6.6820 14.0253 -5.9041 -2.4456 -1.5301 0.4187 1.4353 -1.2050 -0.5327 -0.3921 1.2356 1.6175 -1.1583 -0.0266 # loop_ _pdbx_refine_tls_group.pdbx_refine_id _pdbx_refine_tls_group.id _pdbx_refine_tls_group.refine_tls_id _pdbx_refine_tls_group.beg_auth_asym_id _pdbx_refine_tls_group.beg_auth_seq_id _pdbx_refine_tls_group.beg_label_asym_id _pdbx_refine_tls_group.beg_label_seq_id _pdbx_refine_tls_group.end_auth_asym_id _pdbx_refine_tls_group.end_auth_seq_id _pdbx_refine_tls_group.end_label_asym_id _pdbx_refine_tls_group.end_label_seq_id _pdbx_refine_tls_group.selection _pdbx_refine_tls_group.selection_details 'X-RAY DIFFRACTION' 1 1 A 1 ? ? A 105 ? ? ? ? 'X-RAY DIFFRACTION' 2 2 A 106 ? ? A 262 ? ? ? ? 'X-RAY DIFFRACTION' 3 3 A 263 ? ? A 321 ? ? ? ? 'X-RAY DIFFRACTION' 4 4 B 1 ? ? B 60 ? ? ? ? 'X-RAY DIFFRACTION' 5 5 B 61 ? ? B 84 ? ? ? ? 'X-RAY DIFFRACTION' 6 6 B 85 ? ? B 141 ? ? ? ? 'X-RAY DIFFRACTION' 7 7 B 142 ? ? B 163 ? ? ? ? # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal REFMAC refinement 5.8.0046 ? 1 xia2 'data reduction' . ? 2 SCALA 'data scaling' . ? 3 PHASER phasing . ? 4 # _pdbx_entry_details.entry_id 4CQS _pdbx_entry_details.compound_details ? _pdbx_entry_details.source_details ? _pdbx_entry_details.nonpolymer_details ? _pdbx_entry_details.sequence_details 'MULTIBASIC SITE REMOVED' # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 ARG A 53 ? ? 58.25 -112.33 2 1 ASP A 88 ? ? -107.97 -107.60 3 1 CYS A 135 ? ? -119.03 68.78 4 1 SER A 142 ? ? -142.11 -157.81 5 1 GLN A 192 ? ? 66.62 -69.12 6 1 THR A 202 ? ? -130.64 -158.46 7 1 ALA A 214 ? ? -170.18 146.77 8 1 ASN A 273 ? ? 50.84 70.32 9 1 ARG B 127 ? ? 51.33 -119.92 10 1 TYR B 157 ? ? -51.01 107.53 # _pdbx_validate_chiral.id 1 _pdbx_validate_chiral.PDB_model_num 1 _pdbx_validate_chiral.auth_atom_id C1 _pdbx_validate_chiral.label_alt_id ? _pdbx_validate_chiral.auth_asym_id B _pdbx_validate_chiral.auth_comp_id NAG _pdbx_validate_chiral.auth_seq_id 1163 _pdbx_validate_chiral.PDB_ins_code ? _pdbx_validate_chiral.details 'WRONG HAND' _pdbx_validate_chiral.omega . # loop_ _pdbx_distant_solvent_atoms.id _pdbx_distant_solvent_atoms.PDB_model_num _pdbx_distant_solvent_atoms.auth_atom_id _pdbx_distant_solvent_atoms.label_alt_id _pdbx_distant_solvent_atoms.auth_asym_id _pdbx_distant_solvent_atoms.auth_comp_id _pdbx_distant_solvent_atoms.auth_seq_id _pdbx_distant_solvent_atoms.PDB_ins_code _pdbx_distant_solvent_atoms.neighbor_macromolecule_distance _pdbx_distant_solvent_atoms.neighbor_ligand_distance 1 1 O ? A HOH 2052 ? 5.95 . 2 1 O ? B HOH 2059 ? 7.89 . # loop_ _pdbx_unobs_or_zero_occ_residues.id _pdbx_unobs_or_zero_occ_residues.PDB_model_num _pdbx_unobs_or_zero_occ_residues.polymer_flag _pdbx_unobs_or_zero_occ_residues.occupancy_flag _pdbx_unobs_or_zero_occ_residues.auth_asym_id _pdbx_unobs_or_zero_occ_residues.auth_comp_id _pdbx_unobs_or_zero_occ_residues.auth_seq_id _pdbx_unobs_or_zero_occ_residues.PDB_ins_code _pdbx_unobs_or_zero_occ_residues.label_asym_id _pdbx_unobs_or_zero_occ_residues.label_comp_id _pdbx_unobs_or_zero_occ_residues.label_seq_id 1 1 Y 1 A GLN 322 ? A GLN 322 2 1 Y 1 A ARG 323 ? A ARG 323 3 1 Y 1 A GLU 324 ? A GLU 324 4 1 Y 1 A THR 325 ? A THR 325 5 1 Y 1 A ARG 326 ? A ARG 326 6 1 Y 1 B SER 163 ? B SER 163 7 1 Y 1 B GLU 164 ? B GLU 164 8 1 Y 1 B GLU 165 ? B GLU 165 9 1 Y 1 B ALA 166 ? B ALA 166 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 3 N-ACETYL-D-GLUCOSAMINE NAG 4 ALPHA-D-MANNOSE MAN 5 BETA-D-MANNOSE BMA 6 '3[N-MORPHOLINO]PROPANE SULFONIC ACID' MPO 7 water HOH #