data_4CQP # _entry.id 4CQP # _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 4CQP PDBE EBI-59776 WWPDB D_1290059776 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.content_type _pdbx_database_related.details PDB 4CQQ unspecified ;H5 (VN1194) SER227ASN/GLN196ARG MUTANT HAEMAGGLUTININ IN COMPLEX WITH AVIAN RECEPTOR ANALOGUE 3'SLN ; PDB 4CQR unspecified ;H5 (VN1194) SER227ASN/GLN196ARG MUTANT HAEMAGGLUTININ IN COMPLEX WITH HUMAN RECEPTOR ANALOGUE 6'SLN ; PDB 4CQS unspecified ;H5 (VN1194) ASN186LYS MUTANT HAEMAGGLUTININ IN COMPLEX WITH AVIAN RECEPTOR ANALOGUE 3'SLN ; PDB 4CQT unspecified ;H5 (VN1194) ASN186LYS MUTANT HAEMAGGLUTININ IN COMPLEX WITH AVIAN RECEPTOR ANALOGUE 3'SLN ; PDB 4CQU unspecified ;H5 (VN1194) ASN186LYS MUTANT HAEMAGGLUTININ IN COMPLEX WITH HUMAN RECEPTOR ANALOGUE 6'SLN ; PDB 4CQV unspecified 'CRYSTAL STRUCTURE OF H5 (TYTY) DEL133/ILE155THR MUTANT HAEMAGGLUTININ' PDB 4CQW unspecified ;H5 (TYTY) DEL133/ILE155THR MUTANT HAEMAGGLUTININ IN COMPLEX WITH AVIAN RECEPTOR ANALOGUE 3'SLN ; PDB 4CQX unspecified ;H5 (TYTY) DEL133/ILE155THR MUTANT HAEMAGGLUTININ IN COMPLEX WITH HUMAN RECEPTOR ANALOGUE 6'SLN ; PDB 4CQY unspecified 'H5 (TYTY) DEL133/ILE155THR MUTANT HAEMAGGLUTININ IN COMPLEX WITH AVIAN RECEPTOR ANALOGUE LSTA' PDB 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 4CQP _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 4CQP _cell.length_a 100.635 _cell.length_b 100.635 _cell.length_c 448.712 _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 4CQP _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' 37006.852 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 23 ? ? ? ? # 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 KRSYNNTNQEDLLVLWGIHHPNDAAEQTKLYRNPTTYISVGTSTLNQRLVPRIATRSKVNGQNGRMEFFWTILKPNDAIN FESNGNFIAPEYAYKIVKKGDSTIMKSELEYGNCNTKCQTPMGAINSSMPFHNIHPLTIGECPKYVKSNRLVLATGLRNS PQRETR ; ;DQICIGYHANNSTEQVDTIMEKNVTVTHAQDILEKTHNGKLCDLDGVKPLILRDCSVAGWLLGNPMCDEFINVPEWSYIV EKANPVNDLCYPGDFNDYEELKHLLSRINHFEKIQIIPKSSWSSHEASLGVSSACPYQGKSSFFRNVVWLIKKNSTYPTI KRSYNNTNQEDLLVLWGIHHPNDAAEQTKLYRNPTTYISVGTSTLNQRLVPRIATRSKVNGQNGRMEFFWTILKPNDAIN FESNGNFIAPEYAYKIVKKGDSTIMKSELEYGNCNTKCQTPMGAINSSMPFHNIHPLTIGECPKYVKSNRLVLATGLRNS PQRETR ; A ? 2 'polypeptide(L)' no no ;GLFGAIAGFIEGGWQGMVDGWYGYHHSNEQGSGYAADKESTQKAIDGVTNKVNSIIDKMNTQFEAVGREFNNLERRIENL NKKMEDGFLDVWTYNAELLVLMENERTLDFHDSNVKNLYDKVRLQLRDNAKELGNGCFEFYHKCDNECMESVRNGTYDYP QYSEEA ; ;GLFGAIAGFIEGGWQGMVDGWYGYHHSNEQGSGYAADKESTQKAIDGVTNKVNSIIDKMNTQFEAVGREFNNLERRIENL NKKMEDGFLDVWTYNAELLVLMENERTLDFHDSNVKNLYDKVRLQLRDNAKELGNGCFEFYHKCDNECMESVRNGTYDYP QYSEEA ; B ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 ASP n 1 2 GLN n 1 3 ILE n 1 4 CYS n 1 5 ILE n 1 6 GLY n 1 7 TYR n 1 8 HIS n 1 9 ALA n 1 10 ASN n 1 11 ASN n 1 12 SER n 1 13 THR n 1 14 GLU n 1 15 GLN n 1 16 VAL n 1 17 ASP n 1 18 THR n 1 19 ILE n 1 20 MET n 1 21 GLU n 1 22 LYS n 1 23 ASN n 1 24 VAL n 1 25 THR n 1 26 VAL n 1 27 THR n 1 28 HIS n 1 29 ALA n 1 30 GLN n 1 31 ASP n 1 32 ILE n 1 33 LEU n 1 34 GLU n 1 35 LYS n 1 36 THR n 1 37 HIS n 1 38 ASN n 1 39 GLY n 1 40 LYS n 1 41 LEU n 1 42 CYS n 1 43 ASP n 1 44 LEU n 1 45 ASP n 1 46 GLY n 1 47 VAL n 1 48 LYS n 1 49 PRO n 1 50 LEU n 1 51 ILE n 1 52 LEU n 1 53 ARG n 1 54 ASP n 1 55 CYS n 1 56 SER n 1 57 VAL n 1 58 ALA n 1 59 GLY n 1 60 TRP n 1 61 LEU n 1 62 LEU n 1 63 GLY n 1 64 ASN n 1 65 PRO n 1 66 MET n 1 67 CYS n 1 68 ASP n 1 69 GLU n 1 70 PHE n 1 71 ILE n 1 72 ASN n 1 73 VAL n 1 74 PRO n 1 75 GLU n 1 76 TRP n 1 77 SER n 1 78 TYR n 1 79 ILE n 1 80 VAL n 1 81 GLU n 1 82 LYS n 1 83 ALA n 1 84 ASN n 1 85 PRO n 1 86 VAL n 1 87 ASN n 1 88 ASP n 1 89 LEU n 1 90 CYS n 1 91 TYR n 1 92 PRO n 1 93 GLY n 1 94 ASP n 1 95 PHE n 1 96 ASN n 1 97 ASP n 1 98 TYR n 1 99 GLU n 1 100 GLU n 1 101 LEU n 1 102 LYS n 1 103 HIS n 1 104 LEU n 1 105 LEU n 1 106 SER n 1 107 ARG n 1 108 ILE n 1 109 ASN n 1 110 HIS n 1 111 PHE n 1 112 GLU n 1 113 LYS n 1 114 ILE n 1 115 GLN n 1 116 ILE n 1 117 ILE n 1 118 PRO n 1 119 LYS n 1 120 SER n 1 121 SER n 1 122 TRP n 1 123 SER n 1 124 SER n 1 125 HIS n 1 126 GLU n 1 127 ALA n 1 128 SER n 1 129 LEU n 1 130 GLY n 1 131 VAL n 1 132 SER n 1 133 SER n 1 134 ALA n 1 135 CYS n 1 136 PRO n 1 137 TYR n 1 138 GLN n 1 139 GLY n 1 140 LYS n 1 141 SER n 1 142 SER n 1 143 PHE n 1 144 PHE n 1 145 ARG n 1 146 ASN n 1 147 VAL n 1 148 VAL n 1 149 TRP n 1 150 LEU n 1 151 ILE n 1 152 LYS n 1 153 LYS n 1 154 ASN n 1 155 SER n 1 156 THR n 1 157 TYR n 1 158 PRO n 1 159 THR n 1 160 ILE n 1 161 LYS n 1 162 ARG n 1 163 SER n 1 164 TYR n 1 165 ASN n 1 166 ASN n 1 167 THR n 1 168 ASN n 1 169 GLN n 1 170 GLU n 1 171 ASP n 1 172 LEU n 1 173 LEU n 1 174 VAL n 1 175 LEU n 1 176 TRP n 1 177 GLY n 1 178 ILE n 1 179 HIS n 1 180 HIS n 1 181 PRO n 1 182 ASN n 1 183 ASP n 1 184 ALA n 1 185 ALA n 1 186 GLU n 1 187 GLN n 1 188 THR n 1 189 LYS n 1 190 LEU n 1 191 TYR n 1 192 ARG n 1 193 ASN n 1 194 PRO n 1 195 THR n 1 196 THR n 1 197 TYR n 1 198 ILE n 1 199 SER n 1 200 VAL n 1 201 GLY n 1 202 THR n 1 203 SER n 1 204 THR n 1 205 LEU n 1 206 ASN n 1 207 GLN n 1 208 ARG n 1 209 LEU n 1 210 VAL n 1 211 PRO n 1 212 ARG n 1 213 ILE n 1 214 ALA n 1 215 THR n 1 216 ARG n 1 217 SER n 1 218 LYS n 1 219 VAL n 1 220 ASN n 1 221 GLY n 1 222 GLN n 1 223 ASN 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 ? ? ? ? ? ? ? 'SER227ASN/GLN196ARG MUTANT' ? ? ? ? ? ? ? ? ? 2 1 sample ? ? ? 'INFLUENZA A VIRUS (A/VIETNAM/1194/2004(H5N1))' 644788 ? ? ? ? ? ? ? 'SER227ASN/GLN196ARG MUTANT' ? ? ? ? ? ? ? ? ? # loop_ _struct_ref.id _struct_ref.db_name _struct_ref.db_code _struct_ref.entity_id _struct_ref.pdbx_seq_one_letter_code _struct_ref.pdbx_align_begin _struct_ref.pdbx_db_accession _struct_ref.pdbx_db_isoform 1 UNP Q6DQ34_9INFA 1 ? ? Q6DQ34 ? 2 UNP Q6DQ34_9INFA 2 ? ? Q6DQ34 ? # loop_ _struct_ref_seq.align_id _struct_ref_seq.ref_id _struct_ref_seq.pdbx_PDB_id_code _struct_ref_seq.pdbx_strand_id _struct_ref_seq.seq_align_beg _struct_ref_seq.pdbx_seq_align_beg_ins_code _struct_ref_seq.seq_align_end _struct_ref_seq.pdbx_seq_align_end_ins_code _struct_ref_seq.pdbx_db_accession _struct_ref_seq.db_align_beg _struct_ref_seq.pdbx_db_align_beg_ins_code _struct_ref_seq.db_align_end _struct_ref_seq.pdbx_db_align_end_ins_code _struct_ref_seq.pdbx_auth_seq_align_beg _struct_ref_seq.pdbx_auth_seq_align_end 1 1 4CQP A 1 ? 326 ? Q6DQ34 17 ? 342 ? 1 326 2 2 4CQP 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 4CQP ARG A 192 ? UNP Q6DQ34 GLN 208 'engineered mutation' 192 1 1 4CQP ASN A 223 ? UNP Q6DQ34 SER 239 'engineered mutation' 223 2 1 4CQP THR A 325 ? UNP Q6DQ34 ARG 341 conflict 325 3 # loop_ _chem_comp.id _chem_comp.type _chem_comp.mon_nstd_flag _chem_comp.name _chem_comp.pdbx_synonyms _chem_comp.formula _chem_comp.formula_weight ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 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 4CQP _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 3.74 _exptl_crystal.density_percent_sol 67 _exptl_crystal.description NONE # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method ? _exptl_crystal_grow.temp ? _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH ? _exptl_crystal_grow.pdbx_pH_range ? _exptl_crystal_grow.pdbx_details '0.1 M HEPES/MOPS PH 7.0, 0.05 M MGCL2, 28-30% PEG 550 MME, SEEDED WITH CRUSHED WILD-TYPE VN1194 HA CRYSTALS.' # _diffrn.id 1 _diffrn.ambient_temp 100 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector CCD _diffrn_detector.type 'ADSC CCD' _diffrn_detector.pdbx_collection_date ? _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator ? _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 0.98 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'DIAMOND BEAMLINE I02' _diffrn_source.pdbx_synchrotron_site Diamond _diffrn_source.pdbx_synchrotron_beamline I02 _diffrn_source.pdbx_wavelength 0.98 _diffrn_source.pdbx_wavelength_list ? # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 4CQP _reflns.observed_criterion_sigma_I 2.1 _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 43.37 _reflns.d_resolution_high 2.65 _reflns.number_obs 26069 _reflns.number_all ? _reflns.percent_possible_obs 100.0 _reflns.pdbx_Rmerge_I_obs 0.10 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 9.70 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 8.1 # _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_ordinal 1 _reflns_shell.d_res_high 2.65 _reflns_shell.d_res_low 2.79 _reflns_shell.percent_possible_all 100.0 _reflns_shell.Rmerge_I_obs 0.62 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs 2.10 _reflns_shell.pdbx_redundancy 7.9 # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 4CQP _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 24721 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F . _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 149.57 _refine.ls_d_res_high 2.65 _refine.ls_percent_reflns_obs 99.89 _refine.ls_R_factor_obs 0.19555 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.19331 _refine.ls_R_factor_R_free 0.23790 _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 1327 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.959 _refine.correlation_coeff_Fo_to_Fc_free 0.936 _refine.B_iso_mean 101.640 _refine.aniso_B[1][1] 2.94 _refine.aniso_B[2][2] 2.94 _refine.aniso_B[3][3] -9.55 _refine.aniso_B[1][2] 1.47 _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 0.362 _refine.pdbx_overall_ESU_R_Free 0.260 _refine.overall_SU_ML 0.238 _refine.pdbx_overall_phase_error ? _refine.overall_SU_B 26.053 _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 3863 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 182 _refine_hist.number_atoms_solvent 23 _refine_hist.number_atoms_total 4068 _refine_hist.d_res_high 2.65 _refine_hist.d_res_low 149.57 # 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 0.006 0.019 ? 4156 'X-RAY DIFFRACTION' ? r_bond_other_d 0.001 0.020 ? 3806 'X-RAY DIFFRACTION' ? r_angle_refined_deg 1.070 1.989 ? 5648 'X-RAY DIFFRACTION' ? r_angle_other_deg 0.677 3.003 ? 8735 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 5.687 5.000 ? 483 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg 36.389 25.099 ? 202 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg 16.159 15.000 ? 679 'X-RAY DIFFRACTION' ? r_dihedral_angle_4_deg 11.542 15.000 ? 18 'X-RAY DIFFRACTION' ? r_chiral_restr 0.059 0.200 ? 629 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.003 0.020 ? 4622 'X-RAY DIFFRACTION' ? r_gen_planes_other 0.001 0.020 ? 950 '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 2.521 6.923 ? 1932 'X-RAY DIFFRACTION' ? r_mcbond_other 2.510 6.922 ? 1931 'X-RAY DIFFRACTION' ? r_mcangle_it 4.091 10.384 ? 2412 'X-RAY DIFFRACTION' ? r_mcangle_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scbond_it 3.307 7.631 ? 2223 '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 2.650 _refine_ls_shell.d_res_low 2.719 _refine_ls_shell.number_reflns_R_work 1796 _refine_ls_shell.R_factor_R_work 0.307 _refine_ls_shell.percent_reflns_obs 99.84 _refine_ls_shell.R_factor_R_free 0.308 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 101 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? # _struct.entry_id 4CQP _struct.title 'Crystal Structure of H5 (VN1194) Ser227Asn/Gln196Arg Mutant Haemagglutinin' _struct.pdbx_descriptor 'HAEMAGGLUTININ HA1, HAEMAGGLUTININ HA2' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 4CQP _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 ASN A 64 ? ILE A 71 ? ASN A 64 ILE A 71 5 ? 8 HELX_P HELX_P3 3 ASP A 97 ? SER A 106 ? ASP A 97 SER A 106 1 ? 10 HELX_P HELX_P4 4 PRO A 118 ? TRP A 122 ? PRO A 118 TRP A 122 5 ? 5 HELX_P HELX_P5 5 ASP A 183 ? ARG A 192 ? ASP A 183 ARG A 192 1 ? 10 HELX_P HELX_P6 6 ASP B 37 ? ASN B 60 ? ASP B 37 ASN B 60 1 ? 24 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 ? ? ? ? ? ? ? 2.071 ? disulf2 disulf ? ? A CYS 42 SG ? ? ? 1_555 A CYS 274 SG ? ? A CYS 42 A CYS 274 1_555 ? ? ? ? ? ? ? 2.052 ? 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 ? ? ? ? ? ? ? 2.072 ? disulf5 disulf ? ? A CYS 278 SG ? ? ? 1_555 A CYS 302 SG ? ? A CYS 278 A CYS 302 1_555 ? ? ? ? ? ? ? 2.057 ? disulf6 disulf ? ? B CYS 144 SG ? ? ? 1_555 B CYS 148 SG ? ? B CYS 144 B CYS 148 1_555 ? ? ? ? ? ? ? 2.062 ? covale1 covale ? ? A ASN 11 ND2 ? ? ? 1_555 C NAG . C1 ? ? A ASN 11 A NAG 1011 1_555 ? ? ? ? ? ? ? 1.461 ? covale2 covale ? ? A ASN 23 ND2 ? ? ? 1_555 D NAG . C1 ? ? A ASN 23 A NAG 1023 1_555 ? ? ? ? ? ? ? 1.443 ? covale3 covale ? ? A ASN 165 ND2 ? ? ? 1_555 F NAG . C1 ? ? A ASN 165 A NAG 1165 1_555 ? ? ? ? ? ? ? 1.443 ? covale4 covale ? ? A ASN 286 ND2 ? ? ? 1_555 K NAG . C1 ? ? A ASN 286 A NAG 1286 1_555 ? ? ? ? ? ? ? 1.447 ? covale5 covale ? ? D NAG . O4 ? ? ? 1_555 E NAG . C1 ? ? A NAG 1023 A NAG 1024 1_555 ? ? ? ? ? ? ? 1.441 ? covale6 covale ? ? F NAG . O4 ? ? ? 1_555 G NAG . C1 ? ? A NAG 1165 A NAG 1166 1_555 ? ? ? ? ? ? ? 1.440 ? covale7 covale ? ? G NAG . O4 ? ? ? 1_555 H MAN . C1 ? ? A NAG 1166 A MAN 1167 1_555 ? ? ? ? ? ? ? 1.450 ? covale8 covale ? ? H MAN . O3 ? ? ? 1_555 I BMA . C1 ? ? A MAN 1167 A BMA 1168 1_555 ? ? ? ? ? ? ? 1.450 ? covale9 covale ? ? H MAN . O6 ? ? ? 1_555 J MAN . C1 ? ? A MAN 1167 A MAN 1169 1_555 ? ? ? ? ? ? ? 1.452 ? covale10 covale ? ? B ASN 154 ND2 ? ? ? 1_555 M NAG . C1 ? ? B ASN 154 B NAG 1154 1_555 ? ? ? ? ? ? ? 1.441 ? covale11 covale ? ? M NAG . O4 ? ? ? 1_555 N NAG . C1 ? ? B NAG 1154 B NAG 1155 1_555 ? ? ? ? ? ? ? 1.443 ? covale12 covale ? ? N NAG . O4 ? ? ? 1_555 O BMA . C1 ? ? B NAG 1155 B BMA 1156 1_555 ? ? ? ? ? ? ? 1.447 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details BA ? 5 ? AA ? 2 ? AB ? 2 ? AC ? 3 ? AD ? 2 ? AE ? 3 ? AF ? 5 ? AG ? 5 ? AH ? 2 ? AI ? 4 ? AJ ? 3 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense BA 1 2 ? anti-parallel BA 2 3 ? anti-parallel BA 3 4 ? anti-parallel BA 4 5 ? anti-parallel AA 1 2 ? anti-parallel AB 1 2 ? anti-parallel AC 1 2 ? parallel AC 2 3 ? parallel AD 1 2 ? parallel AE 1 2 ? parallel AE 2 3 ? parallel AF 1 2 ? parallel AF 2 3 ? anti-parallel AF 3 4 ? anti-parallel AF 4 5 ? anti-parallel AG 1 2 ? parallel AG 2 3 ? anti-parallel AG 3 4 ? anti-parallel AG 4 5 ? anti-parallel AH 1 2 ? anti-parallel AI 1 2 ? anti-parallel AI 2 3 ? anti-parallel AI 3 4 ? anti-parallel AJ 1 2 ? anti-parallel AJ 2 3 ? anti-parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id BA 1 GLY B 31 ? ALA B 36 ? GLY B 31 ALA B 36 BA 2 TYR B 22 ? ASN B 28 ? TYR B 22 ASN B 28 BA 3 GLN A 2 ? TYR A 7 ? GLN A 2 TYR A 7 BA 4 CYS B 137 ? PHE B 140 ? CYS B 137 PHE B 140 BA 5 ALA B 130 ? GLU B 132 ? ALA B 130 GLU B 132 AA 1 GLN A 15 ? VAL A 16 ? GLN A 15 VAL A 16 AA 2 VAL A 24 ? THR A 25 ? VAL A 24 THR A 25 AB 1 ALA A 29 ? ASP A 31 ? ALA A 29 ASP A 31 AB 2 VAL A 312 ? ALA A 314 ? VAL A 312 ALA A 314 AC 1 LEU A 33 ? GLU A 34 ? LEU A 33 GLU A 34 AC 2 PHE A 291 ? HIS A 292 ? PHE A 291 HIS A 292 AC 3 LYS A 304 ? TYR A 305 ? LYS A 304 TYR A 305 AD 1 LEU A 41 ? LEU A 44 ? LEU A 41 LEU A 44 AD 2 TYR A 271 ? THR A 276 ? TYR A 271 THR A 276 AE 1 LEU A 50 ? ARG A 53 ? LEU A 50 ARG A 53 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 ASP A 171 ? HIS A 180 ? ASP A 171 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 ASP A 171 ? HIS A 180 ? ASP A 171 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 N LEU A 52 ? N LEU A 52 O VAL A 80 ? O 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 B 1163' AC2 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE MPO A 1322' AC3 Software ? ? ? ? 1 'Binding site for Mono-Saccharide NAG A1011 bound to ASN A 11' AC4 Software ? ? ? ? 2 'Binding site for Poly-Saccharide residues NAG A1023 through NAG A1024 bound to ASN A 23' AC5 Software ? ? ? ? 7 'Binding site for Poly-Saccharide residues NAG A1165 through MAN A1169 bound to ASN A 165' AC6 Software ? ? ? ? 1 'Binding site for Mono-Saccharide NAG A1286 bound to ASN A 286' AC7 Software ? ? ? ? 3 'Binding site for Poly-Saccharide residues NAG B1154 through BMA B1156 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 CYS A 4 ? CYS A 4 . ? 1_555 ? 2 AC1 5 TRP B 14 ? TRP B 14 . ? 1_555 ? 3 AC1 5 HIS B 25 ? HIS B 25 . ? 1_555 ? 4 AC1 5 ASN B 135 ? ASN B 135 . ? 1_555 ? 5 AC1 5 CYS B 137 ? CYS B 137 . ? 1_555 ? 6 AC2 5 LEU A 129 ? LEU A 129 . ? 1_555 ? 7 AC2 5 VAL A 131 ? VAL A 131 . ? 1_555 ? 8 AC2 5 SER A 132 ? SER A 132 . ? 1_555 ? 9 AC2 5 SER A 133 ? SER A 133 . ? 1_555 ? 10 AC2 5 GLN A 222 ? GLN A 222 . ? 1_555 ? 11 AC3 1 ASN A 11 ? ASN A 11 . ? 1_555 ? 12 AC4 2 LYS A 22 ? LYS A 22 . ? 1_555 ? 13 AC4 2 ASN A 23 ? ASN A 23 . ? 1_555 ? 14 AC5 7 ARG A 107 ? ARG A 107 . ? 6_555 ? 15 AC5 7 ASN A 165 ? ASN A 165 . ? 1_555 ? 16 AC5 7 ASN A 236 ? ASN A 236 . ? 1_555 ? 17 AC5 7 ALA A 238 ? ALA A 238 . ? 1_555 ? 18 AC5 7 MET A 282 ? MET A 282 . ? 4_545 ? 19 AC5 7 HIS A 295 ? HIS A 295 . ? 4_545 ? 20 AC5 7 LYS B 82 ? LYS B 82 . ? 4_545 ? 21 AC6 1 ASN A 286 ? ASN A 286 . ? 1_555 ? 22 AC7 3 GLU B 147 ? GLU B 147 . ? 1_555 ? 23 AC7 3 GLU B 150 ? GLU B 150 . ? 1_555 ? 24 AC7 3 ASN B 154 ? ASN B 154 . ? 1_555 ? # _database_PDB_matrix.entry_id 4CQP _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 4CQP _atom_sites.fract_transf_matrix[1][1] 0.009937 _atom_sites.fract_transf_matrix[1][2] 0.005737 _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] 0.011474 _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] 0.002229 _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 ? 36.842 -14.843 -83.153 1.00 98.91 ? 1 ASP A N 1 ATOM 2 C CA . ASP A 1 1 ? 35.960 -15.540 -82.184 1.00 95.61 ? 1 ASP A CA 1 ATOM 3 C C . ASP A 1 1 ? 36.828 -16.323 -81.217 1.00 91.47 ? 1 ASP A C 1 ATOM 4 O O . ASP A 1 1 ? 37.626 -17.153 -81.637 1.00 87.03 ? 1 ASP A O 1 ATOM 5 C CB . ASP A 1 1 ? 34.984 -16.479 -82.904 1.00 97.46 ? 1 ASP A CB 1 ATOM 6 C CG . ASP A 1 1 ? 34.048 -15.743 -83.859 1.00 103.82 ? 1 ASP A CG 1 ATOM 7 O OD1 . ASP A 1 1 ? 34.149 -14.504 -84.003 1.00 105.98 ? 1 ASP A OD1 1 ATOM 8 O OD2 . ASP A 1 1 ? 33.198 -16.413 -84.475 1.00 111.57 ? 1 ASP A OD2 1 ATOM 9 N N . GLN A 1 2 ? 36.680 -16.048 -79.923 1.00 90.84 ? 2 GLN A N 1 ATOM 10 C CA . GLN A 1 2 ? 37.509 -16.694 -78.918 1.00 87.94 ? 2 GLN A CA 1 ATOM 11 C C . GLN A 1 2 ? 36.788 -16.936 -77.609 1.00 83.12 ? 2 GLN A C 1 ATOM 12 O O . GLN A 1 2 ? 35.791 -16.283 -77.307 1.00 83.26 ? 2 GLN A O 1 ATOM 13 C CB . GLN A 1 2 ? 38.763 -15.860 -78.656 1.00 92.10 ? 2 GLN A CB 1 ATOM 14 C CG . GLN A 1 2 ? 38.551 -14.634 -77.784 1.00 95.97 ? 2 GLN A CG 1 ATOM 15 C CD . GLN A 1 2 ? 39.840 -13.876 -77.534 1.00 98.83 ? 2 GLN A CD 1 ATOM 16 O OE1 . GLN A 1 2 ? 40.156 -13.521 -76.396 1.00 97.66 ? 2 GLN A OE1 1 ATOM 17 N NE2 . GLN A 1 2 ? 40.597 -13.627 -78.600 1.00 101.31 ? 2 GLN A NE2 1 ATOM 18 N N . ILE A 1 3 ? 37.323 -17.873 -76.833 1.00 79.01 ? 3 ILE A N 1 ATOM 19 C CA . ILE A 1 3 ? 36.795 -18.192 -75.520 1.00 77.18 ? 3 ILE A CA 1 ATOM 20 C C . ILE A 1 3 ? 37.933 -18.231 -74.505 1.00 75.88 ? 3 ILE A C 1 ATOM 21 O O . ILE A 1 3 ? 39.008 -18.727 -74.800 1.00 76.09 ? 3 ILE A O 1 ATOM 22 C CB . ILE A 1 3 ? 36.008 -19.517 -75.535 1.00 77.51 ? 3 ILE A CB 1 ATOM 23 C CG1 . ILE A 1 3 ? 35.292 -19.720 -74.202 1.00 81.28 ? 3 ILE A CG1 1 ATOM 24 C CG2 . ILE A 1 3 ? 36.910 -20.701 -75.817 1.00 76.39 ? 3 ILE A CG2 1 ATOM 25 C CD1 . ILE A 1 3 ? 34.384 -20.928 -74.177 1.00 83.88 ? 3 ILE A CD1 1 ATOM 26 N N . CYS A 1 4 ? 37.676 -17.703 -73.312 1.00 79.79 ? 4 CYS A N 1 ATOM 27 C CA . CYS A 1 4 ? 38.694 -17.523 -72.281 1.00 82.26 ? 4 CYS A CA 1 ATOM 28 C C . CYS A 1 4 ? 38.245 -18.146 -70.981 1.00 79.13 ? 4 CYS A C 1 ATOM 29 O O . CYS A 1 4 ? 37.070 -18.088 -70.640 1.00 82.08 ? 4 CYS A O 1 ATOM 30 C CB . CYS A 1 4 ? 38.963 -16.030 -72.023 1.00 87.68 ? 4 CYS A CB 1 ATOM 31 S SG . CYS A 1 4 ? 39.445 -15.066 -73.484 1.00 105.88 ? 4 CYS A SG 1 ATOM 32 N N . ILE A 1 5 ? 39.193 -18.718 -70.247 1.00 74.96 ? 5 ILE A N 1 ATOM 33 C CA . ILE A 1 5 ? 38.948 -19.189 -68.896 1.00 69.44 ? 5 ILE A CA 1 ATOM 34 C C . ILE A 1 5 ? 39.400 -18.107 -67.942 1.00 66.71 ? 5 ILE A C 1 ATOM 35 O O . ILE A 1 5 ? 40.357 -17.399 -68.211 1.00 65.41 ? 5 ILE A O 1 ATOM 36 C CB . ILE A 1 5 ? 39.717 -20.482 -68.623 1.00 70.99 ? 5 ILE A CB 1 ATOM 37 C CG1 . ILE A 1 5 ? 39.395 -21.517 -69.705 1.00 74.02 ? 5 ILE A CG1 1 ATOM 38 C CG2 . ILE A 1 5 ? 39.397 -21.032 -67.241 1.00 70.85 ? 5 ILE A CG2 1 ATOM 39 C CD1 . ILE A 1 5 ? 37.927 -21.846 -69.839 1.00 76.76 ? 5 ILE A CD1 1 ATOM 40 N N . GLY A 1 6 ? 38.691 -17.973 -66.830 1.00 65.36 ? 6 GLY A N 1 ATOM 41 C CA . GLY A 1 6 ? 38.976 -16.927 -65.869 1.00 64.18 ? 6 GLY A CA 1 ATOM 42 C C . GLY A 1 6 ? 38.285 -17.158 -64.546 1.00 63.22 ? 6 GLY A C 1 ATOM 43 O O . GLY A 1 6 ? 37.627 -18.171 -64.340 1.00 64.97 ? 6 GLY A O 1 ATOM 44 N N . TYR A 1 7 ? 38.440 -16.205 -63.643 1.00 62.11 ? 7 TYR A N 1 ATOM 45 C CA . TYR A 1 7 ? 37.990 -16.377 -62.286 1.00 63.61 ? 7 TYR A CA 1 ATOM 46 C C . TYR A 1 7 ? 37.477 -15.071 -61.754 1.00 64.06 ? 7 TYR A C 1 ATOM 47 O O . TYR A 1 7 ? 37.705 -14.024 -62.328 1.00 65.59 ? 7 TYR A O 1 ATOM 48 C CB . TYR A 1 7 ? 39.128 -16.903 -61.398 1.00 65.93 ? 7 TYR A CB 1 ATOM 49 C CG . TYR A 1 7 ? 40.415 -16.090 -61.450 1.00 65.99 ? 7 TYR A CG 1 ATOM 50 C CD1 . TYR A 1 7 ? 41.374 -16.328 -62.418 1.00 64.13 ? 7 TYR A CD1 1 ATOM 51 C CD2 . TYR A 1 7 ? 40.659 -15.079 -60.521 1.00 67.73 ? 7 TYR A CD2 1 ATOM 52 C CE1 . TYR A 1 7 ? 42.538 -15.576 -62.467 1.00 67.79 ? 7 TYR A CE1 1 ATOM 53 C CE2 . TYR A 1 7 ? 41.820 -14.333 -60.559 1.00 68.04 ? 7 TYR A CE2 1 ATOM 54 C CZ . TYR A 1 7 ? 42.758 -14.588 -61.528 1.00 68.45 ? 7 TYR A CZ 1 ATOM 55 O OH . TYR A 1 7 ? 43.908 -13.836 -61.559 1.00 70.42 ? 7 TYR A OH 1 ATOM 56 N N . HIS A 1 8 ? 36.790 -15.170 -60.637 1.00 65.40 ? 8 HIS A N 1 ATOM 57 C CA . HIS A 1 8 ? 36.092 -14.068 -60.017 1.00 70.64 ? 8 HIS A CA 1 ATOM 58 C C . HIS A 1 8 ? 37.037 -12.989 -59.517 1.00 74.91 ? 8 HIS A C 1 ATOM 59 O O . HIS A 1 8 ? 38.168 -13.274 -59.118 1.00 76.41 ? 8 HIS A O 1 ATOM 60 C CB . HIS A 1 8 ? 35.306 -14.629 -58.829 1.00 69.73 ? 8 HIS A CB 1 ATOM 61 C CG . HIS A 1 8 ? 34.392 -13.650 -58.174 1.00 70.99 ? 8 HIS A CG 1 ATOM 62 N ND1 . HIS A 1 8 ? 33.410 -12.974 -58.863 1.00 74.67 ? 8 HIS A ND1 1 ATOM 63 C CD2 . HIS A 1 8 ? 34.278 -13.268 -56.881 1.00 71.46 ? 8 HIS A CD2 1 ATOM 64 C CE1 . HIS A 1 8 ? 32.740 -12.203 -58.024 1.00 75.28 ? 8 HIS A CE1 1 ATOM 65 N NE2 . HIS A 1 8 ? 33.247 -12.364 -56.815 1.00 72.57 ? 8 HIS A NE2 1 ATOM 66 N N . ALA A 1 9 ? 36.558 -11.749 -59.537 1.00 75.08 ? 9 ALA A N 1 ATOM 67 C CA . ALA A 1 9 ? 37.189 -10.672 -58.793 1.00 72.24 ? 9 ALA A CA 1 ATOM 68 C C . ALA A 1 9 ? 36.101 -9.757 -58.273 1.00 74.91 ? 9 ALA A C 1 ATOM 69 O O . ALA A 1 9 ? 34.989 -9.753 -58.788 1.00 78.64 ? 9 ALA A O 1 ATOM 70 C CB . ALA A 1 9 ? 38.155 -9.915 -59.675 1.00 71.10 ? 9 ALA A CB 1 ATOM 71 N N . ASN A 1 10 ? 36.417 -8.982 -57.248 1.00 76.49 ? 10 ASN A N 1 ATOM 72 C CA . ASN A 1 10 ? 35.447 -8.068 -56.673 1.00 78.29 ? 10 ASN A CA 1 ATOM 73 C C . ASN A 1 10 ? 36.125 -6.893 -55.975 1.00 79.51 ? 10 ASN A C 1 ATOM 74 O O . ASN A 1 10 ? 37.317 -6.690 -56.158 1.00 76.43 ? 10 ASN A O 1 ATOM 75 C CB . ASN A 1 10 ? 34.499 -8.832 -55.742 1.00 79.59 ? 10 ASN A CB 1 ATOM 76 C CG . ASN A 1 10 ? 35.187 -9.374 -54.516 1.00 79.45 ? 10 ASN A CG 1 ATOM 77 O OD1 . ASN A 1 10 ? 36.332 -9.040 -54.234 1.00 83.32 ? 10 ASN A OD1 1 ATOM 78 N ND2 . ASN A 1 10 ? 34.484 -10.217 -53.772 1.00 79.08 ? 10 ASN A ND2 1 ATOM 79 N N . ASN A 1 11 ? 35.367 -6.115 -55.202 1.00 87.00 ? 11 ASN A N 1 ATOM 80 C CA . ASN A 1 11 ? 35.900 -4.920 -54.534 1.00 94.13 ? 11 ASN A CA 1 ATOM 81 C C . ASN A 1 11 ? 36.362 -5.175 -53.089 1.00 92.08 ? 11 ASN A C 1 ATOM 82 O O . ASN A 1 11 ? 36.595 -4.234 -52.328 1.00 90.09 ? 11 ASN A O 1 ATOM 83 C CB . ASN A 1 11 ? 34.875 -3.772 -54.585 1.00 101.66 ? 11 ASN A CB 1 ATOM 84 C CG . ASN A 1 11 ? 33.545 -4.120 -53.922 1.00 111.57 ? 11 ASN A CG 1 ATOM 85 O OD1 . ASN A 1 11 ? 33.371 -5.207 -53.373 1.00 113.01 ? 11 ASN A OD1 1 ATOM 86 N ND2 . ASN A 1 11 ? 32.589 -3.177 -53.979 1.00 127.10 ? 11 ASN A ND2 1 ATOM 87 N N . SER A 1 12 ? 36.506 -6.449 -52.728 1.00 90.40 ? 12 SER A N 1 ATOM 88 C CA . SER A 1 12 ? 36.902 -6.852 -51.384 1.00 85.39 ? 12 SER A CA 1 ATOM 89 C C . SER A 1 12 ? 38.307 -6.355 -51.069 1.00 84.10 ? 12 SER A C 1 ATOM 90 O O . SER A 1 12 ? 39.184 -6.373 -51.935 1.00 79.14 ? 12 SER A O 1 ATOM 91 C CB . SER A 1 12 ? 36.851 -8.380 -51.253 1.00 85.20 ? 12 SER A CB 1 ATOM 92 O OG . SER A 1 12 ? 36.964 -8.801 -49.903 1.00 84.95 ? 12 SER A OG 1 ATOM 93 N N . THR A 1 13 ? 38.491 -5.885 -49.834 1.00 84.83 ? 13 THR A N 1 ATOM 94 C CA . THR A 1 13 ? 39.803 -5.491 -49.313 1.00 84.64 ? 13 THR A CA 1 ATOM 95 C C . THR A 1 13 ? 40.242 -6.400 -48.171 1.00 82.10 ? 13 THR A C 1 ATOM 96 O O . THR A 1 13 ? 41.311 -6.190 -47.602 1.00 82.07 ? 13 THR A O 1 ATOM 97 C CB . THR A 1 13 ? 39.795 -4.036 -48.790 1.00 87.78 ? 13 THR A CB 1 ATOM 98 O OG1 . THR A 1 13 ? 38.739 -3.871 -47.831 1.00 88.70 ? 13 THR A OG1 1 ATOM 99 C CG2 . THR A 1 13 ? 39.603 -3.059 -49.927 1.00 86.78 ? 13 THR A CG2 1 ATOM 100 N N . GLU A 1 14 ? 39.419 -7.403 -47.848 1.00 82.03 ? 14 GLU A N 1 ATOM 101 C CA . GLU A 1 14 ? 39.735 -8.406 -46.822 1.00 81.97 ? 14 GLU A CA 1 ATOM 102 C C . GLU A 1 14 ? 41.079 -9.074 -47.111 1.00 76.54 ? 14 GLU A C 1 ATOM 103 O O . GLU A 1 14 ? 41.352 -9.467 -48.243 1.00 79.70 ? 14 GLU A O 1 ATOM 104 C CB . GLU A 1 14 ? 38.652 -9.494 -46.764 1.00 85.49 ? 14 GLU A CB 1 ATOM 105 C CG . GLU A 1 14 ? 37.247 -9.016 -46.408 1.00 93.22 ? 14 GLU A CG 1 ATOM 106 C CD . GLU A 1 14 ? 37.002 -8.918 -44.909 1.00 104.75 ? 14 GLU A CD 1 ATOM 107 O OE1 . GLU A 1 14 ? 37.190 -9.939 -44.209 1.00 111.91 ? 14 GLU A OE1 1 ATOM 108 O OE2 . GLU A 1 14 ? 36.616 -7.823 -44.429 1.00 109.16 ? 14 GLU A OE2 1 ATOM 109 N N . GLN A 1 15 ? 41.906 -9.203 -46.082 1.00 74.42 ? 15 GLN A N 1 ATOM 110 C CA . GLN A 1 15 ? 43.227 -9.799 -46.207 1.00 72.21 ? 15 GLN A CA 1 ATOM 111 C C . GLN A 1 15 ? 43.363 -11.031 -45.316 1.00 68.08 ? 15 GLN A C 1 ATOM 112 O O . GLN A 1 15 ? 42.765 -11.098 -44.256 1.00 65.63 ? 15 GLN A O 1 ATOM 113 C CB . GLN A 1 15 ? 44.284 -8.783 -45.813 1.00 75.77 ? 15 GLN A CB 1 ATOM 114 C CG . GLN A 1 15 ? 44.111 -7.431 -46.475 1.00 82.65 ? 15 GLN A CG 1 ATOM 115 C CD . GLN A 1 15 ? 45.322 -6.539 -46.301 1.00 88.25 ? 15 GLN A CD 1 ATOM 116 O OE1 . GLN A 1 15 ? 45.873 -6.031 -47.277 1.00 91.31 ? 15 GLN A OE1 1 ATOM 117 N NE2 . GLN A 1 15 ? 45.746 -6.345 -45.055 1.00 90.29 ? 15 GLN A NE2 1 ATOM 118 N N . VAL A 1 16 ? 44.147 -12.006 -45.761 1.00 67.29 ? 16 VAL A N 1 ATOM 119 C CA . VAL A 1 16 ? 44.490 -13.171 -44.948 1.00 63.95 ? 16 VAL A CA 1 ATOM 120 C C . VAL A 1 16 ? 45.983 -13.337 -45.015 1.00 66.27 ? 16 VAL A C 1 ATOM 121 O O . VAL A 1 16 ? 46.609 -12.872 -45.966 1.00 67.07 ? 16 VAL A O 1 ATOM 122 C CB . VAL A 1 16 ? 43.815 -14.472 -45.442 1.00 64.49 ? 16 VAL A CB 1 ATOM 123 C CG1 . VAL A 1 16 ? 42.309 -14.350 -45.343 1.00 65.19 ? 16 VAL A CG1 1 ATOM 124 C CG2 . VAL A 1 16 ? 44.227 -14.824 -46.864 1.00 64.80 ? 16 VAL A CG2 1 ATOM 125 N N . ASP A 1 17 ? 46.554 -13.981 -44.000 1.00 72.02 ? 17 ASP A N 1 ATOM 126 C CA . ASP A 1 17 ? 47.983 -14.271 -43.980 1.00 71.70 ? 17 ASP A CA 1 ATOM 127 C C . ASP A 1 17 ? 48.188 -15.725 -44.354 1.00 72.33 ? 17 ASP A C 1 ATOM 128 O O . ASP A 1 17 ? 47.304 -16.569 -44.146 1.00 69.72 ? 17 ASP A O 1 ATOM 129 C CB . ASP A 1 17 ? 48.585 -14.003 -42.595 1.00 76.77 ? 17 ASP A CB 1 ATOM 130 C CG . ASP A 1 17 ? 48.725 -12.503 -42.274 1.00 84.47 ? 17 ASP A CG 1 ATOM 131 O OD1 . ASP A 1 17 ? 48.919 -11.686 -43.203 1.00 84.55 ? 17 ASP A OD1 1 ATOM 132 O OD2 . ASP A 1 17 ? 48.657 -12.142 -41.073 1.00 90.00 ? 17 ASP A OD2 1 ATOM 133 N N . THR A 1 18 ? 49.356 -16.003 -44.926 1.00 72.95 ? 18 THR A N 1 ATOM 134 C CA . THR A 1 18 ? 49.813 -17.366 -45.183 1.00 70.91 ? 18 THR A CA 1 ATOM 135 C C . THR A 1 18 ? 51.244 -17.473 -44.661 1.00 72.75 ? 18 THR A C 1 ATOM 136 O O . THR A 1 18 ? 51.776 -16.520 -44.106 1.00 76.81 ? 18 THR A O 1 ATOM 137 C CB . THR A 1 18 ? 49.749 -17.728 -46.689 1.00 71.80 ? 18 THR A CB 1 ATOM 138 O OG1 . THR A 1 18 ? 50.816 -17.098 -47.405 1.00 71.37 ? 18 THR A OG1 1 ATOM 139 C CG2 . THR A 1 18 ? 48.434 -17.285 -47.294 1.00 73.05 ? 18 THR A CG2 1 ATOM 140 N N . ILE A 1 19 ? 51.859 -18.636 -44.828 1.00 76.48 ? 19 ILE A N 1 ATOM 141 C CA . ILE A 1 19 ? 53.216 -18.865 -44.359 1.00 76.53 ? 19 ILE A CA 1 ATOM 142 C C . ILE A 1 19 ? 54.204 -18.063 -45.203 1.00 75.99 ? 19 ILE A C 1 ATOM 143 O O . ILE A 1 19 ? 55.142 -17.477 -44.673 1.00 73.01 ? 19 ILE A O 1 ATOM 144 C CB . ILE A 1 19 ? 53.570 -20.367 -44.422 1.00 80.57 ? 19 ILE A CB 1 ATOM 145 C CG1 . ILE A 1 19 ? 52.753 -21.165 -43.390 1.00 85.20 ? 19 ILE A CG1 1 ATOM 146 C CG2 . ILE A 1 19 ? 55.059 -20.582 -44.209 1.00 83.32 ? 19 ILE A CG2 1 ATOM 147 C CD1 . ILE A 1 19 ? 53.304 -21.178 -41.982 1.00 89.02 ? 19 ILE A CD1 1 ATOM 148 N N . MET A 1 20 ? 53.978 -18.044 -46.515 1.00 76.96 ? 20 MET A N 1 ATOM 149 C CA . MET A 1 20 ? 54.887 -17.399 -47.462 1.00 77.43 ? 20 MET A CA 1 ATOM 150 C C . MET A 1 20 ? 54.565 -15.949 -47.774 1.00 76.21 ? 20 MET A C 1 ATOM 151 O O . MET A 1 20 ? 55.386 -15.258 -48.371 1.00 77.89 ? 20 MET A O 1 ATOM 152 C CB . MET A 1 20 ? 54.885 -18.153 -48.779 1.00 79.53 ? 20 MET A CB 1 ATOM 153 C CG . MET A 1 20 ? 55.578 -19.491 -48.712 1.00 82.71 ? 20 MET A CG 1 ATOM 154 S SD . MET A 1 20 ? 56.089 -19.998 -50.356 1.00 86.85 ? 20 MET A SD 1 ATOM 155 C CE . MET A 1 20 ? 56.369 -21.747 -50.046 1.00 97.61 ? 20 MET A CE 1 ATOM 156 N N . GLU A 1 21 ? 53.375 -15.491 -47.412 1.00 74.70 ? 21 GLU A N 1 ATOM 157 C CA . GLU A 1 21 ? 52.980 -14.135 -47.734 1.00 77.07 ? 21 GLU A CA 1 ATOM 158 C C . GLU A 1 21 ? 51.943 -13.630 -46.774 1.00 77.26 ? 21 GLU A C 1 ATOM 159 O O . GLU A 1 21 ? 51.053 -14.359 -46.368 1.00 76.87 ? 21 GLU A O 1 ATOM 160 C CB . GLU A 1 21 ? 52.429 -14.051 -49.152 1.00 82.02 ? 21 GLU A CB 1 ATOM 161 C CG . GLU A 1 21 ? 52.210 -12.622 -49.632 1.00 86.99 ? 21 GLU A CG 1 ATOM 162 C CD . GLU A 1 21 ? 51.779 -12.550 -51.086 1.00 94.56 ? 21 GLU A CD 1 ATOM 163 O OE1 . GLU A 1 21 ? 51.770 -13.610 -51.755 1.00 99.20 ? 21 GLU A OE1 1 ATOM 164 O OE2 . GLU A 1 21 ? 51.447 -11.434 -51.556 1.00 95.04 ? 21 GLU A OE2 1 ATOM 165 N N . LYS A 1 22 ? 52.066 -12.355 -46.436 1.00 82.11 ? 22 LYS A N 1 ATOM 166 C CA . LYS A 1 22 ? 51.156 -11.720 -45.520 1.00 81.87 ? 22 LYS A CA 1 ATOM 167 C C . LYS A 1 22 ? 50.293 -10.723 -46.265 1.00 77.07 ? 22 LYS A C 1 ATOM 168 O O . LYS A 1 22 ? 50.664 -10.230 -47.326 1.00 76.02 ? 22 LYS A O 1 ATOM 169 C CB . LYS A 1 22 ? 51.954 -11.049 -44.414 1.00 88.43 ? 22 LYS A CB 1 ATOM 170 C CG . LYS A 1 22 ? 52.621 -12.051 -43.488 1.00 95.50 ? 22 LYS A CG 1 ATOM 171 C CD . LYS A 1 22 ? 53.289 -11.352 -42.313 1.00 109.02 ? 22 LYS A CD 1 ATOM 172 C CE . LYS A 1 22 ? 53.359 -12.237 -41.075 1.00 116.93 ? 22 LYS A CE 1 ATOM 173 N NZ . LYS A 1 22 ? 53.568 -11.456 -39.820 1.00 118.13 ? 22 LYS A NZ 1 ATOM 174 N N . ASN A 1 23 ? 49.118 -10.456 -45.720 1.00 79.45 ? 23 ASN A N 1 ATOM 175 C CA . ASN A 1 23 ? 48.234 -9.416 -46.241 1.00 84.99 ? 23 ASN A CA 1 ATOM 176 C C . ASN A 1 23 ? 47.873 -9.632 -47.702 1.00 80.69 ? 23 ASN A C 1 ATOM 177 O O . ASN A 1 23 ? 47.961 -8.721 -48.513 1.00 80.90 ? 23 ASN A O 1 ATOM 178 C CB . ASN A 1 23 ? 48.856 -8.023 -46.024 1.00 88.19 ? 23 ASN A CB 1 ATOM 179 C CG . ASN A 1 23 ? 48.803 -7.575 -44.574 1.00 92.64 ? 23 ASN A CG 1 ATOM 180 O OD1 . ASN A 1 23 ? 47.993 -8.071 -43.787 1.00 92.86 ? 23 ASN A OD1 1 ATOM 181 N ND2 . ASN A 1 23 ? 49.665 -6.623 -44.214 1.00 103.09 ? 23 ASN A ND2 1 ATOM 182 N N . VAL A 1 24 ? 47.469 -10.855 -48.021 1.00 77.49 ? 24 VAL A N 1 ATOM 183 C CA . VAL A 1 24 ? 46.993 -11.199 -49.351 1.00 71.00 ? 24 VAL A CA 1 ATOM 184 C C . VAL A 1 24 ? 45.522 -10.848 -49.412 1.00 71.45 ? 24 VAL A C 1 ATOM 185 O O . VAL A 1 24 ? 44.731 -11.357 -48.621 1.00 70.95 ? 24 VAL A O 1 ATOM 186 C CB . VAL A 1 24 ? 47.134 -12.702 -49.616 1.00 70.23 ? 24 VAL A CB 1 ATOM 187 C CG1 . VAL A 1 24 ? 46.644 -13.045 -51.016 1.00 70.77 ? 24 VAL A CG1 1 ATOM 188 C CG2 . VAL A 1 24 ? 48.579 -13.133 -49.423 1.00 70.05 ? 24 VAL A CG2 1 ATOM 189 N N . THR A 1 25 ? 45.156 -9.969 -50.336 1.00 71.65 ? 25 THR A N 1 ATOM 190 C CA . THR A 1 25 ? 43.762 -9.574 -50.494 1.00 70.59 ? 25 THR A CA 1 ATOM 191 C C . THR A 1 25 ? 42.989 -10.714 -51.147 1.00 68.56 ? 25 THR A C 1 ATOM 192 O O . THR A 1 25 ? 43.405 -11.221 -52.179 1.00 67.90 ? 25 THR A O 1 ATOM 193 C CB . THR A 1 25 ? 43.625 -8.318 -51.378 1.00 71.58 ? 25 THR A CB 1 ATOM 194 O OG1 . THR A 1 25 ? 44.541 -7.315 -50.931 1.00 73.28 ? 25 THR A OG1 1 ATOM 195 C CG2 . THR A 1 25 ? 42.207 -7.767 -51.321 1.00 71.09 ? 25 THR A CG2 1 ATOM 196 N N . VAL A 1 26 ? 41.869 -11.104 -50.550 1.00 67.34 ? 26 VAL A N 1 ATOM 197 C CA . VAL A 1 26 ? 41.017 -12.136 -51.127 1.00 67.77 ? 26 VAL A CA 1 ATOM 198 C C . VAL A 1 26 ? 39.582 -11.666 -51.338 1.00 70.76 ? 26 VAL A C 1 ATOM 199 O O . VAL A 1 26 ? 39.078 -10.779 -50.642 1.00 72.43 ? 26 VAL A O 1 ATOM 200 C CB . VAL A 1 26 ? 40.987 -13.413 -50.262 1.00 66.82 ? 26 VAL A CB 1 ATOM 201 C CG1 . VAL A 1 26 ? 42.369 -14.062 -50.228 1.00 66.76 ? 26 VAL A CG1 1 ATOM 202 C CG2 . VAL A 1 26 ? 40.479 -13.120 -48.862 1.00 65.07 ? 26 VAL A CG2 1 ATOM 203 N N . THR A 1 27 ? 38.920 -12.315 -52.284 1.00 70.19 ? 27 THR A N 1 ATOM 204 C CA . THR A 1 27 ? 37.543 -12.000 -52.628 1.00 70.81 ? 27 THR A CA 1 ATOM 205 C C . THR A 1 27 ? 36.574 -12.249 -51.476 1.00 71.22 ? 27 THR A C 1 ATOM 206 O O . THR A 1 27 ? 35.604 -11.516 -51.316 1.00 77.19 ? 27 THR A O 1 ATOM 207 C CB . THR A 1 27 ? 37.085 -12.826 -53.837 1.00 70.72 ? 27 THR A CB 1 ATOM 208 O OG1 . THR A 1 27 ? 37.068 -14.220 -53.502 1.00 69.42 ? 27 THR A OG1 1 ATOM 209 C CG2 . THR A 1 27 ? 38.019 -12.601 -55.008 1.00 71.61 ? 27 THR A CG2 1 ATOM 210 N N . HIS A 1 28 ? 36.831 -13.295 -50.697 1.00 70.89 ? 28 HIS A N 1 ATOM 211 C CA . HIS A 1 28 ? 36.001 -13.647 -49.547 1.00 69.74 ? 28 HIS A CA 1 ATOM 212 C C . HIS A 1 28 ? 36.829 -14.193 -48.404 1.00 69.87 ? 28 HIS A C 1 ATOM 213 O O . HIS A 1 28 ? 37.852 -14.831 -48.616 1.00 73.39 ? 28 HIS A O 1 ATOM 214 C CB . HIS A 1 28 ? 34.983 -14.704 -49.937 1.00 70.38 ? 28 HIS A CB 1 ATOM 215 C CG . HIS A 1 28 ? 34.093 -14.290 -51.059 1.00 73.83 ? 28 HIS A CG 1 ATOM 216 N ND1 . HIS A 1 28 ? 34.439 -14.464 -52.382 1.00 74.48 ? 28 HIS A ND1 1 ATOM 217 C CD2 . HIS A 1 28 ? 32.876 -13.699 -51.058 1.00 72.16 ? 28 HIS A CD2 1 ATOM 218 C CE1 . HIS A 1 28 ? 33.466 -14.009 -53.148 1.00 73.46 ? 28 HIS A CE1 1 ATOM 219 N NE2 . HIS A 1 28 ? 32.506 -13.542 -52.370 1.00 74.41 ? 28 HIS A NE2 1 ATOM 220 N N . ALA A 1 29 ? 36.357 -13.972 -47.187 1.00 74.09 ? 29 ALA A N 1 ATOM 221 C CA . ALA A 1 29 ? 37.059 -14.414 -45.995 1.00 74.19 ? 29 ALA A CA 1 ATOM 222 C C . ALA A 1 29 ? 36.063 -14.655 -44.881 1.00 73.26 ? 29 ALA A C 1 ATOM 223 O O . ALA A 1 29 ? 34.949 -14.176 -44.938 1.00 79.29 ? 29 ALA A O 1 ATOM 224 C CB . ALA A 1 29 ? 38.078 -13.372 -45.575 1.00 73.62 ? 29 ALA A CB 1 ATOM 225 N N . GLN A 1 30 ? 36.463 -15.412 -43.873 1.00 75.63 ? 30 GLN A N 1 ATOM 226 C CA . GLN A 1 30 ? 35.605 -15.644 -42.727 1.00 78.71 ? 30 GLN A CA 1 ATOM 227 C C . GLN A 1 30 ? 36.382 -15.423 -41.440 1.00 79.11 ? 30 GLN A C 1 ATOM 228 O O . GLN A 1 30 ? 37.318 -16.156 -41.130 1.00 80.42 ? 30 GLN A O 1 ATOM 229 C CB . GLN A 1 30 ? 35.003 -17.049 -42.758 1.00 81.09 ? 30 GLN A CB 1 ATOM 230 C CG . GLN A 1 30 ? 33.887 -17.232 -41.735 1.00 86.54 ? 30 GLN A CG 1 ATOM 231 C CD . GLN A 1 30 ? 33.119 -18.534 -41.881 1.00 89.07 ? 30 GLN A CD 1 ATOM 232 O OE1 . GLN A 1 30 ? 32.655 -19.096 -40.891 1.00 93.37 ? 30 GLN A OE1 1 ATOM 233 N NE2 . GLN A 1 30 ? 32.967 -19.012 -43.112 1.00 90.16 ? 30 GLN A NE2 1 ATOM 234 N N . ASP A 1 31 ? 35.995 -14.385 -40.710 1.00 81.66 ? 31 ASP A N 1 ATOM 235 C CA . ASP A 1 31 ? 36.534 -14.132 -39.393 1.00 80.79 ? 31 ASP A CA 1 ATOM 236 C C . ASP A 1 31 ? 35.991 -15.211 -38.459 1.00 79.64 ? 31 ASP A C 1 ATOM 237 O O . ASP A 1 31 ? 34.799 -15.517 -38.474 1.00 79.39 ? 31 ASP A O 1 ATOM 238 C CB . ASP A 1 31 ? 36.116 -12.746 -38.916 1.00 83.92 ? 31 ASP A CB 1 ATOM 239 C CG . ASP A 1 31 ? 36.812 -12.330 -37.644 1.00 90.34 ? 31 ASP A CG 1 ATOM 240 O OD1 . ASP A 1 31 ? 37.544 -13.146 -37.047 1.00 100.64 ? 31 ASP A OD1 1 ATOM 241 O OD2 . ASP A 1 31 ? 36.625 -11.170 -37.232 1.00 100.17 ? 31 ASP A OD2 1 ATOM 242 N N . ILE A 1 32 ? 36.874 -15.796 -37.662 1.00 77.14 ? 32 ILE A N 1 ATOM 243 C CA . ILE A 1 32 ? 36.481 -16.852 -36.735 1.00 76.10 ? 32 ILE A CA 1 ATOM 244 C C . ILE A 1 32 ? 36.826 -16.523 -35.278 1.00 75.05 ? 32 ILE A C 1 ATOM 245 O O . ILE A 1 32 ? 36.651 -17.358 -34.395 1.00 73.78 ? 32 ILE A O 1 ATOM 246 C CB . ILE A 1 32 ? 37.102 -18.206 -37.149 1.00 73.37 ? 32 ILE A CB 1 ATOM 247 C CG1 . ILE A 1 32 ? 38.622 -18.104 -37.299 1.00 72.54 ? 32 ILE A CG1 1 ATOM 248 C CG2 . ILE A 1 32 ? 36.491 -18.677 -38.453 1.00 73.87 ? 32 ILE A CG2 1 ATOM 249 C CD1 . ILE A 1 32 ? 39.291 -19.448 -37.476 1.00 72.03 ? 32 ILE A CD1 1 ATOM 250 N N . LEU A 1 33 ? 37.295 -15.304 -35.030 1.00 74.16 ? 33 LEU A N 1 ATOM 251 C CA . LEU A 1 33 ? 37.665 -14.884 -33.688 1.00 75.93 ? 33 LEU A CA 1 ATOM 252 C C . LEU A 1 33 ? 36.724 -13.792 -33.196 1.00 77.98 ? 33 LEU A C 1 ATOM 253 O O . LEU A 1 33 ? 36.530 -12.777 -33.869 1.00 78.44 ? 33 LEU A O 1 ATOM 254 C CB . LEU A 1 33 ? 39.098 -14.367 -33.679 1.00 74.44 ? 33 LEU A CB 1 ATOM 255 C CG . LEU A 1 33 ? 39.639 -13.996 -32.302 1.00 74.44 ? 33 LEU A CG 1 ATOM 256 C CD1 . LEU A 1 33 ? 39.836 -15.242 -31.461 1.00 76.60 ? 33 LEU A CD1 1 ATOM 257 C CD2 . LEU A 1 33 ? 40.943 -13.231 -32.426 1.00 76.44 ? 33 LEU A CD2 1 ATOM 258 N N . GLU A 1 34 ? 36.144 -14.008 -32.022 1.00 78.08 ? 34 GLU A N 1 ATOM 259 C CA . GLU A 1 34 ? 35.280 -13.013 -31.406 1.00 83.12 ? 34 GLU A CA 1 ATOM 260 C C . GLU A 1 34 ? 36.118 -12.073 -30.554 1.00 79.25 ? 34 GLU A C 1 ATOM 261 O O . GLU A 1 34 ? 36.809 -12.519 -29.647 1.00 78.13 ? 34 GLU A O 1 ATOM 262 C CB . GLU A 1 34 ? 34.211 -13.679 -30.537 1.00 86.09 ? 34 GLU A CB 1 ATOM 263 C CG . GLU A 1 34 ? 33.202 -12.706 -29.938 1.00 89.56 ? 34 GLU A CG 1 ATOM 264 C CD . GLU A 1 34 ? 32.594 -11.783 -30.978 1.00 94.80 ? 34 GLU A CD 1 ATOM 265 O OE1 . GLU A 1 34 ? 31.747 -12.241 -31.778 1.00 101.63 ? 34 GLU A OE1 1 ATOM 266 O OE2 . GLU A 1 34 ? 32.987 -10.600 -31.013 1.00 99.84 ? 34 GLU A OE2 1 ATOM 267 N N . LYS A 1 35 ? 36.050 -10.777 -30.848 1.00 79.51 ? 35 LYS A N 1 ATOM 268 C CA . LYS A 1 35 ? 36.820 -9.773 -30.113 1.00 79.74 ? 35 LYS A CA 1 ATOM 269 C C . LYS A 1 35 ? 35.975 -8.871 -29.214 1.00 78.24 ? 35 LYS A C 1 ATOM 270 O O . LYS A 1 35 ? 36.538 -8.159 -28.398 1.00 79.69 ? 35 LYS A O 1 ATOM 271 C CB . LYS A 1 35 ? 37.610 -8.895 -31.078 1.00 80.13 ? 35 LYS A CB 1 ATOM 272 C CG . LYS A 1 35 ? 38.569 -9.648 -31.973 1.00 82.47 ? 35 LYS A CG 1 ATOM 273 C CD . LYS A 1 35 ? 39.228 -8.704 -32.971 1.00 87.00 ? 35 LYS A CD 1 ATOM 274 C CE . LYS A 1 35 ? 39.457 -9.377 -34.313 1.00 91.22 ? 35 LYS A CE 1 ATOM 275 N NZ . LYS A 1 35 ? 38.173 -9.663 -35.021 1.00 91.28 ? 35 LYS A NZ 1 ATOM 276 N N . THR A 1 36 ? 34.648 -8.908 -29.352 1.00 78.12 ? 36 THR A N 1 ATOM 277 C CA . THR A 1 36 ? 33.756 -8.018 -28.604 1.00 83.09 ? 36 THR A CA 1 ATOM 278 C C . THR A 1 36 ? 32.947 -8.720 -27.508 1.00 86.29 ? 36 THR A C 1 ATOM 279 O O . THR A 1 36 ? 32.548 -9.879 -27.651 1.00 83.48 ? 36 THR A O 1 ATOM 280 C CB . THR A 1 36 ? 32.749 -7.325 -29.538 1.00 87.80 ? 36 THR A CB 1 ATOM 281 O OG1 . THR A 1 36 ? 31.843 -8.292 -30.080 1.00 89.72 ? 36 THR A OG1 1 ATOM 282 C CG2 . THR A 1 36 ? 33.464 -6.625 -30.676 1.00 91.69 ? 36 THR A CG2 1 ATOM 283 N N . HIS A 1 37 ? 32.706 -7.991 -26.420 1.00 86.49 ? 37 HIS A N 1 ATOM 284 C CA . HIS A 1 37 ? 31.814 -8.425 -25.347 1.00 85.29 ? 37 HIS A CA 1 ATOM 285 C C . HIS A 1 37 ? 30.898 -7.253 -24.969 1.00 87.08 ? 37 HIS A C 1 ATOM 286 O O . HIS A 1 37 ? 31.065 -6.149 -25.476 1.00 89.62 ? 37 HIS A O 1 ATOM 287 C CB . HIS A 1 37 ? 32.617 -8.920 -24.138 1.00 84.04 ? 37 HIS A CB 1 ATOM 288 C CG . HIS A 1 37 ? 33.610 -7.927 -23.613 1.00 85.04 ? 37 HIS A CG 1 ATOM 289 N ND1 . HIS A 1 37 ? 33.304 -7.020 -22.623 1.00 86.77 ? 37 HIS A ND1 1 ATOM 290 C CD2 . HIS A 1 37 ? 34.906 -7.704 -23.933 1.00 87.22 ? 37 HIS A CD2 1 ATOM 291 C CE1 . HIS A 1 37 ? 34.363 -6.280 -22.355 1.00 84.98 ? 37 HIS A CE1 1 ATOM 292 N NE2 . HIS A 1 37 ? 35.353 -6.679 -23.132 1.00 87.69 ? 37 HIS A NE2 1 ATOM 293 N N . ASN A 1 38 ? 29.927 -7.488 -24.094 1.00 89.13 ? 38 ASN A N 1 ATOM 294 C CA . ASN A 1 38 ? 28.974 -6.431 -23.718 1.00 92.67 ? 38 ASN A CA 1 ATOM 295 C C . ASN A 1 38 ? 29.401 -5.600 -22.502 1.00 91.87 ? 38 ASN A C 1 ATOM 296 O O . ASN A 1 38 ? 28.780 -4.582 -22.196 1.00 95.86 ? 38 ASN A O 1 ATOM 297 C CB . ASN A 1 38 ? 27.583 -7.016 -23.473 1.00 92.16 ? 38 ASN A CB 1 ATOM 298 C CG . ASN A 1 38 ? 27.527 -7.905 -22.249 1.00 92.87 ? 38 ASN A CG 1 ATOM 299 O OD1 . ASN A 1 38 ? 28.522 -8.094 -21.543 1.00 95.82 ? 38 ASN A OD1 1 ATOM 300 N ND2 . ASN A 1 38 ? 26.359 -8.462 -21.992 1.00 92.79 ? 38 ASN A ND2 1 ATOM 301 N N . GLY A 1 39 ? 30.423 -6.064 -21.791 1.00 87.43 ? 39 GLY A N 1 ATOM 302 C CA . GLY A 1 39 ? 31.025 -5.309 -20.693 1.00 84.58 ? 39 GLY A CA 1 ATOM 303 C C . GLY A 1 39 ? 30.282 -5.439 -19.377 1.00 85.06 ? 39 GLY A C 1 ATOM 304 O O . GLY A 1 39 ? 30.535 -4.674 -18.455 1.00 85.18 ? 39 GLY A O 1 ATOM 305 N N . LYS A 1 40 ? 29.386 -6.423 -19.286 1.00 87.84 ? 40 LYS A N 1 ATOM 306 C CA . LYS A 1 40 ? 28.463 -6.556 -18.163 1.00 88.93 ? 40 LYS A CA 1 ATOM 307 C C . LYS A 1 40 ? 28.501 -7.934 -17.526 1.00 89.92 ? 40 LYS A C 1 ATOM 308 O O . LYS A 1 40 ? 28.866 -8.916 -18.167 1.00 90.11 ? 40 LYS A O 1 ATOM 309 C CB . LYS A 1 40 ? 27.045 -6.304 -18.652 1.00 89.39 ? 40 LYS A CB 1 ATOM 310 C CG . LYS A 1 40 ? 26.818 -4.883 -19.114 1.00 94.03 ? 40 LYS A CG 1 ATOM 311 C CD . LYS A 1 40 ? 25.523 -4.739 -19.893 1.00 96.96 ? 40 LYS A CD 1 ATOM 312 C CE . LYS A 1 40 ? 25.323 -3.290 -20.307 1.00 99.95 ? 40 LYS A CE 1 ATOM 313 N NZ . LYS A 1 40 ? 24.311 -3.151 -21.384 1.00 104.25 ? 40 LYS A NZ 1 ATOM 314 N N . LEU A 1 41 ? 28.100 -8.001 -16.263 1.00 93.83 ? 41 LEU A N 1 ATOM 315 C CA . LEU A 1 41 ? 27.852 -9.281 -15.612 1.00 98.95 ? 41 LEU A CA 1 ATOM 316 C C . LEU A 1 41 ? 26.376 -9.623 -15.773 1.00 94.93 ? 41 LEU A C 1 ATOM 317 O O . LEU A 1 41 ? 25.508 -8.823 -15.431 1.00 94.07 ? 41 LEU A O 1 ATOM 318 C CB . LEU A 1 41 ? 28.246 -9.228 -14.138 1.00 103.54 ? 41 LEU A CB 1 ATOM 319 C CG . LEU A 1 41 ? 29.739 -8.984 -13.899 1.00 107.08 ? 41 LEU A CG 1 ATOM 320 C CD1 . LEU A 1 41 ? 30.007 -8.776 -12.418 1.00 110.67 ? 41 LEU A CD1 1 ATOM 321 C CD2 . LEU A 1 41 ? 30.587 -10.128 -14.446 1.00 108.53 ? 41 LEU A CD2 1 ATOM 322 N N . CYS A 1 42 ? 26.103 -10.812 -16.300 1.00 94.27 ? 42 CYS A N 1 ATOM 323 C CA . CYS A 1 42 ? 24.762 -11.177 -16.751 1.00 97.34 ? 42 CYS A CA 1 ATOM 324 C C . CYS A 1 42 ? 24.288 -12.453 -16.109 1.00 91.72 ? 42 CYS A C 1 ATOM 325 O O . CYS A 1 42 ? 25.083 -13.231 -15.584 1.00 86.77 ? 42 CYS A O 1 ATOM 326 C CB . CYS A 1 42 ? 24.760 -11.412 -18.264 1.00 102.55 ? 42 CYS A CB 1 ATOM 327 S SG . CYS A 1 42 ? 25.238 -10.004 -19.288 1.00 103.54 ? 42 CYS A SG 1 ATOM 328 N N . ASP A 1 43 ? 22.984 -12.683 -16.194 1.00 91.77 ? 43 ASP A N 1 ATOM 329 C CA . ASP A 1 43 ? 22.432 -13.974 -15.817 1.00 95.94 ? 43 ASP A CA 1 ATOM 330 C C . ASP A 1 43 ? 22.990 -14.992 -16.782 1.00 91.47 ? 43 ASP A C 1 ATOM 331 O O . ASP A 1 43 ? 23.294 -14.657 -17.919 1.00 89.99 ? 43 ASP A O 1 ATOM 332 C CB . ASP A 1 43 ? 20.903 -13.995 -15.902 1.00 100.06 ? 43 ASP A CB 1 ATOM 333 C CG . ASP A 1 43 ? 20.247 -12.968 -15.004 1.00 101.40 ? 43 ASP A CG 1 ATOM 334 O OD1 . ASP A 1 43 ? 20.953 -12.317 -14.211 1.00 105.50 ? 43 ASP A OD1 1 ATOM 335 O OD2 . ASP A 1 43 ? 19.017 -12.806 -15.102 1.00 103.96 ? 43 ASP A OD2 1 ATOM 336 N N . LEU A 1 44 ? 23.130 -16.225 -16.315 1.00 93.19 ? 44 LEU A N 1 ATOM 337 C CA . LEU A 1 44 ? 23.566 -17.330 -17.146 1.00 95.76 ? 44 LEU A CA 1 ATOM 338 C C . LEU A 1 44 ? 22.393 -18.297 -17.339 1.00 101.71 ? 44 LEU A C 1 ATOM 339 O O . LEU A 1 44 ? 22.031 -19.050 -16.426 1.00 98.17 ? 44 LEU A O 1 ATOM 340 C CB . LEU A 1 44 ? 24.760 -18.029 -16.502 1.00 93.57 ? 44 LEU A CB 1 ATOM 341 C CG . LEU A 1 44 ? 25.529 -18.998 -17.395 1.00 97.49 ? 44 LEU A CG 1 ATOM 342 C CD1 . LEU A 1 44 ? 26.192 -18.264 -18.555 1.00 99.13 ? 44 LEU A CD1 1 ATOM 343 C CD2 . LEU A 1 44 ? 26.566 -19.761 -16.584 1.00 98.13 ? 44 LEU A CD2 1 ATOM 344 N N . ASP A 1 45 ? 21.808 -18.258 -18.539 1.00 108.64 ? 45 ASP A N 1 ATOM 345 C CA . ASP A 1 45 ? 20.568 -18.972 -18.863 1.00 113.93 ? 45 ASP A CA 1 ATOM 346 C C . ASP A 1 45 ? 19.458 -18.591 -17.899 1.00 109.82 ? 45 ASP A C 1 ATOM 347 O O . ASP A 1 45 ? 18.793 -19.455 -17.336 1.00 108.21 ? 45 ASP A O 1 ATOM 348 C CB . ASP A 1 45 ? 20.776 -20.492 -18.874 1.00 121.52 ? 45 ASP A CB 1 ATOM 349 C CG . ASP A 1 45 ? 21.710 -20.942 -19.978 1.00 130.61 ? 45 ASP A CG 1 ATOM 350 O OD1 . ASP A 1 45 ? 22.648 -20.188 -20.317 1.00 136.54 ? 45 ASP A OD1 1 ATOM 351 O OD2 . ASP A 1 45 ? 21.500 -22.050 -20.515 1.00 140.18 ? 45 ASP A OD2 1 ATOM 352 N N . GLY A 1 46 ? 19.290 -17.285 -17.696 1.00 108.93 ? 46 GLY A N 1 ATOM 353 C CA . GLY A 1 46 ? 18.232 -16.747 -16.840 1.00 107.61 ? 46 GLY A CA 1 ATOM 354 C C . GLY A 1 46 ? 18.454 -16.880 -15.343 1.00 105.94 ? 46 GLY A C 1 ATOM 355 O O . GLY A 1 46 ? 17.618 -16.425 -14.566 1.00 108.46 ? 46 GLY A O 1 ATOM 356 N N . VAL A 1 47 ? 19.573 -17.489 -14.939 1.00 102.00 ? 47 VAL A N 1 ATOM 357 C CA . VAL A 1 47 ? 19.895 -17.718 -13.526 1.00 99.44 ? 47 VAL A CA 1 ATOM 358 C C . VAL A 1 47 ? 20.932 -16.696 -13.050 1.00 97.70 ? 47 VAL A C 1 ATOM 359 O O . VAL A 1 47 ? 22.108 -16.787 -13.401 1.00 96.79 ? 47 VAL A O 1 ATOM 360 C CB . VAL A 1 47 ? 20.443 -19.143 -13.311 1.00 97.80 ? 47 VAL A CB 1 ATOM 361 C CG1 . VAL A 1 47 ? 20.765 -19.394 -11.844 1.00 98.77 ? 47 VAL A CG1 1 ATOM 362 C CG2 . VAL A 1 47 ? 19.444 -20.165 -13.816 1.00 98.93 ? 47 VAL A CG2 1 ATOM 363 N N . LYS A 1 48 ? 20.491 -15.734 -12.243 1.00 96.70 ? 48 LYS A N 1 ATOM 364 C CA . LYS A 1 48 ? 21.351 -14.641 -11.778 1.00 94.79 ? 48 LYS A CA 1 ATOM 365 C C . LYS A 1 48 ? 22.515 -15.135 -10.918 1.00 94.34 ? 48 LYS A C 1 ATOM 366 O O . LYS A 1 48 ? 22.347 -16.058 -10.120 1.00 97.34 ? 48 LYS A O 1 ATOM 367 C CB . LYS A 1 48 ? 20.519 -13.603 -11.008 1.00 96.47 ? 48 LYS A CB 1 ATOM 368 C CG . LYS A 1 48 ? 21.311 -12.662 -10.114 1.00 99.19 ? 48 LYS A CG 1 ATOM 369 C CD . LYS A 1 48 ? 20.535 -11.410 -9.739 1.00 102.58 ? 48 LYS A CD 1 ATOM 370 C CE . LYS A 1 48 ? 21.470 -10.370 -9.141 1.00 105.66 ? 48 LYS A CE 1 ATOM 371 N NZ . LYS A 1 48 ? 20.761 -9.133 -8.711 1.00 110.94 ? 48 LYS A NZ 1 ATOM 372 N N . PRO A 1 49 ? 23.705 -14.519 -11.081 1.00 92.77 ? 49 PRO A N 1 ATOM 373 C CA . PRO A 1 49 ? 24.832 -14.881 -10.231 1.00 89.58 ? 49 PRO A CA 1 ATOM 374 C C . PRO A 1 49 ? 24.718 -14.290 -8.841 1.00 88.34 ? 49 PRO A C 1 ATOM 375 O O . PRO A 1 49 ? 23.973 -13.335 -8.629 1.00 88.25 ? 49 PRO A O 1 ATOM 376 C CB . PRO A 1 49 ? 26.021 -14.233 -10.939 1.00 89.29 ? 49 PRO A CB 1 ATOM 377 C CG . PRO A 1 49 ? 25.436 -13.033 -11.597 1.00 89.48 ? 49 PRO A CG 1 ATOM 378 C CD . PRO A 1 49 ? 24.088 -13.496 -12.076 1.00 91.34 ? 49 PRO A CD 1 ATOM 379 N N . LEU A 1 50 ? 25.478 -14.854 -7.912 1.00 88.29 ? 50 LEU A N 1 ATOM 380 C CA . LEU A 1 50 ? 25.649 -14.272 -6.590 1.00 86.55 ? 50 LEU A CA 1 ATOM 381 C C . LEU A 1 50 ? 26.769 -13.241 -6.667 1.00 85.29 ? 50 LEU A C 1 ATOM 382 O O . LEU A 1 50 ? 27.936 -13.588 -6.846 1.00 86.98 ? 50 LEU A O 1 ATOM 383 C CB . LEU A 1 50 ? 25.980 -15.364 -5.571 1.00 87.51 ? 50 LEU A CB 1 ATOM 384 C CG . LEU A 1 50 ? 26.342 -14.932 -4.151 1.00 89.44 ? 50 LEU A CG 1 ATOM 385 C CD1 . LEU A 1 50 ? 25.363 -13.901 -3.610 1.00 90.67 ? 50 LEU A CD1 1 ATOM 386 C CD2 . LEU A 1 50 ? 26.398 -16.155 -3.248 1.00 91.60 ? 50 LEU A CD2 1 ATOM 387 N N . ILE A 1 51 ? 26.404 -11.970 -6.556 1.00 84.84 ? 51 ILE A N 1 ATOM 388 C CA . ILE A 1 51 ? 27.367 -10.880 -6.618 1.00 83.42 ? 51 ILE A CA 1 ATOM 389 C C . ILE A 1 51 ? 27.604 -10.368 -5.206 1.00 84.30 ? 51 ILE A C 1 ATOM 390 O O . ILE A 1 51 ? 26.806 -9.596 -4.679 1.00 82.33 ? 51 ILE A O 1 ATOM 391 C CB . ILE A 1 51 ? 26.866 -9.768 -7.558 1.00 84.89 ? 51 ILE A CB 1 ATOM 392 C CG1 . ILE A 1 51 ? 26.834 -10.312 -8.988 1.00 90.15 ? 51 ILE A CG1 1 ATOM 393 C CG2 . ILE A 1 51 ? 27.748 -8.524 -7.483 1.00 83.50 ? 51 ILE A CG2 1 ATOM 394 C CD1 . ILE A 1 51 ? 25.964 -9.514 -9.930 1.00 95.08 ? 51 ILE A CD1 1 ATOM 395 N N . LEU A 1 52 ? 28.711 -10.801 -4.604 1.00 86.56 ? 52 LEU A N 1 ATOM 396 C CA . LEU A 1 52 ? 29.012 -10.479 -3.205 1.00 87.52 ? 52 LEU A CA 1 ATOM 397 C C . LEU A 1 52 ? 29.335 -9.009 -2.982 1.00 88.66 ? 52 LEU A C 1 ATOM 398 O O . LEU A 1 52 ? 29.368 -8.553 -1.846 1.00 88.19 ? 52 LEU A O 1 ATOM 399 C CB . LEU A 1 52 ? 30.166 -11.335 -2.687 1.00 85.53 ? 52 LEU A CB 1 ATOM 400 C CG . LEU A 1 52 ? 29.916 -12.845 -2.649 1.00 87.10 ? 52 LEU A CG 1 ATOM 401 C CD1 . LEU A 1 52 ? 31.205 -13.582 -2.331 1.00 88.25 ? 52 LEU A CD1 1 ATOM 402 C CD2 . LEU A 1 52 ? 28.838 -13.211 -1.641 1.00 88.47 ? 52 LEU A CD2 1 ATOM 403 N N . ARG A 1 53 ? 29.574 -8.272 -4.060 1.00 93.82 ? 53 ARG A N 1 ATOM 404 C CA . ARG A 1 53 ? 29.883 -6.854 -3.963 1.00 98.73 ? 53 ARG A CA 1 ATOM 405 C C . ARG A 1 53 ? 31.122 -6.651 -3.051 1.00 97.67 ? 53 ARG A C 1 ATOM 406 O O . ARG A 1 53 ? 32.206 -7.169 -3.360 1.00 101.42 ? 53 ARG A O 1 ATOM 407 C CB . ARG A 1 53 ? 28.632 -6.082 -3.514 1.00 101.85 ? 53 ARG A CB 1 ATOM 408 C CG . ARG A 1 53 ? 28.711 -4.582 -3.755 1.00 109.78 ? 53 ARG A CG 1 ATOM 409 C CD . ARG A 1 53 ? 27.602 -3.810 -3.049 1.00 116.31 ? 53 ARG A CD 1 ATOM 410 N NE . ARG A 1 53 ? 26.491 -3.488 -3.947 1.00 120.12 ? 53 ARG A NE 1 ATOM 411 C CZ . ARG A 1 53 ? 25.428 -4.260 -4.173 1.00 123.46 ? 53 ARG A CZ 1 ATOM 412 N NH1 . ARG A 1 53 ? 25.288 -5.436 -3.577 1.00 127.16 ? 53 ARG A NH1 1 ATOM 413 N NH2 . ARG A 1 53 ? 24.488 -3.850 -5.012 1.00 126.80 ? 53 ARG A NH2 1 ATOM 414 N N . ASP A 1 54 ? 30.964 -5.948 -1.930 1.00 96.96 ? 54 ASP A N 1 ATOM 415 C CA . ASP A 1 54 ? 32.074 -5.660 -1.019 1.00 93.39 ? 54 ASP A CA 1 ATOM 416 C C . ASP A 1 54 ? 32.336 -6.763 -0.006 1.00 90.01 ? 54 ASP A C 1 ATOM 417 O O . ASP A 1 54 ? 33.288 -6.672 0.757 1.00 97.19 ? 54 ASP A O 1 ATOM 418 C CB . ASP A 1 54 ? 31.810 -4.357 -0.261 1.00 95.04 ? 54 ASP A CB 1 ATOM 419 C CG . ASP A 1 54 ? 31.727 -3.161 -1.176 1.00 96.75 ? 54 ASP A CG 1 ATOM 420 O OD1 . ASP A 1 54 ? 32.596 -3.043 -2.073 1.00 98.23 ? 54 ASP A OD1 1 ATOM 421 O OD2 . ASP A 1 54 ? 30.795 -2.345 -0.999 1.00 97.77 ? 54 ASP A OD2 1 ATOM 422 N N . CYS A 1 55 ? 31.498 -7.789 0.028 1.00 91.85 ? 55 CYS A N 1 ATOM 423 C CA . CYS A 1 55 ? 31.728 -8.906 0.936 1.00 95.75 ? 55 CYS A CA 1 ATOM 424 C C . CYS A 1 55 ? 32.640 -9.934 0.300 1.00 92.32 ? 55 CYS A C 1 ATOM 425 O O . CYS A 1 55 ? 32.605 -10.161 -0.909 1.00 95.45 ? 55 CYS A O 1 ATOM 426 C CB . CYS A 1 55 ? 30.415 -9.564 1.370 1.00 99.60 ? 55 CYS A CB 1 ATOM 427 S SG . CYS A 1 55 ? 29.405 -8.453 2.371 1.00 115.17 ? 55 CYS A SG 1 ATOM 428 N N . SER A 1 56 ? 33.477 -10.535 1.133 1.00 92.41 ? 56 SER A N 1 ATOM 429 C CA . SER A 1 56 ? 34.252 -11.691 0.742 1.00 90.04 ? 56 SER A CA 1 ATOM 430 C C . SER A 1 56 ? 33.428 -12.926 1.062 1.00 88.48 ? 56 SER A C 1 ATOM 431 O O . SER A 1 56 ? 32.409 -12.852 1.751 1.00 88.36 ? 56 SER A O 1 ATOM 432 C CB . SER A 1 56 ? 35.565 -11.748 1.516 1.00 90.66 ? 56 SER A CB 1 ATOM 433 O OG . SER A 1 56 ? 35.374 -12.389 2.767 1.00 92.95 ? 56 SER A OG 1 ATOM 434 N N . VAL A 1 57 ? 33.899 -14.066 0.581 1.00 88.16 ? 57 VAL A N 1 ATOM 435 C CA . VAL A 1 57 ? 33.207 -15.325 0.787 1.00 89.90 ? 57 VAL A CA 1 ATOM 436 C C . VAL A 1 57 ? 33.141 -15.655 2.278 1.00 92.69 ? 57 VAL A C 1 ATOM 437 O O . VAL A 1 57 ? 32.129 -16.165 2.751 1.00 94.20 ? 57 VAL A O 1 ATOM 438 C CB . VAL A 1 57 ? 33.886 -16.456 -0.010 1.00 89.90 ? 57 VAL A CB 1 ATOM 439 C CG1 . VAL A 1 57 ? 33.281 -17.808 0.326 1.00 90.12 ? 57 VAL A CG1 1 ATOM 440 C CG2 . VAL A 1 57 ? 33.772 -16.176 -1.502 1.00 90.86 ? 57 VAL A CG2 1 ATOM 441 N N . ALA A 1 58 ? 34.205 -15.338 3.016 1.00 93.36 ? 58 ALA A N 1 ATOM 442 C CA . ALA A 1 58 ? 34.232 -15.549 4.468 1.00 92.95 ? 58 ALA A CA 1 ATOM 443 C C . ALA A 1 58 ? 33.234 -14.652 5.226 1.00 93.81 ? 58 ALA A C 1 ATOM 444 O O . ALA A 1 58 ? 32.524 -15.125 6.121 1.00 95.25 ? 58 ALA A O 1 ATOM 445 C CB . ALA A 1 58 ? 35.637 -15.341 5.003 1.00 91.48 ? 58 ALA A CB 1 ATOM 446 N N . GLY A 1 59 ? 33.188 -13.368 4.873 1.00 89.18 ? 59 GLY A N 1 ATOM 447 C CA . GLY A 1 59 ? 32.222 -12.443 5.458 1.00 89.02 ? 59 GLY A CA 1 ATOM 448 C C . GLY A 1 59 ? 30.787 -12.864 5.183 1.00 93.48 ? 59 GLY A C 1 ATOM 449 O O . GLY A 1 59 ? 29.887 -12.603 5.982 1.00 98.96 ? 59 GLY A O 1 ATOM 450 N N . TRP A 1 60 ? 30.570 -13.519 4.047 1.00 93.46 ? 60 TRP A N 1 ATOM 451 C CA . TRP A 1 60 ? 29.250 -14.006 3.680 1.00 92.66 ? 60 TRP A CA 1 ATOM 452 C C . TRP A 1 60 ? 28.866 -15.240 4.497 1.00 94.76 ? 60 TRP A C 1 ATOM 453 O O . TRP A 1 60 ? 27.788 -15.286 5.094 1.00 98.64 ? 60 TRP A O 1 ATOM 454 C CB . TRP A 1 60 ? 29.194 -14.306 2.176 1.00 92.93 ? 60 TRP A CB 1 ATOM 455 C CG . TRP A 1 60 ? 28.062 -15.199 1.770 1.00 91.50 ? 60 TRP A CG 1 ATOM 456 C CD1 . TRP A 1 60 ? 26.777 -15.125 2.191 1.00 90.37 ? 60 TRP A CD1 1 ATOM 457 C CD2 . TRP A 1 60 ? 28.122 -16.293 0.846 1.00 90.18 ? 60 TRP A CD2 1 ATOM 458 N NE1 . TRP A 1 60 ? 26.028 -16.114 1.603 1.00 95.51 ? 60 TRP A NE1 1 ATOM 459 C CE2 . TRP A 1 60 ? 26.831 -16.844 0.769 1.00 91.57 ? 60 TRP A CE2 1 ATOM 460 C CE3 . TRP A 1 60 ? 29.144 -16.859 0.077 1.00 89.25 ? 60 TRP A CE3 1 ATOM 461 C CZ2 . TRP A 1 60 ? 26.528 -17.938 -0.043 1.00 94.16 ? 60 TRP A CZ2 1 ATOM 462 C CZ3 . TRP A 1 60 ? 28.844 -17.948 -0.736 1.00 89.79 ? 60 TRP A CZ3 1 ATOM 463 C CH2 . TRP A 1 60 ? 27.547 -18.473 -0.791 1.00 92.36 ? 60 TRP A CH2 1 ATOM 464 N N . LEU A 1 61 ? 29.745 -16.235 4.528 1.00 93.81 ? 61 LEU A N 1 ATOM 465 C CA . LEU A 1 61 ? 29.438 -17.494 5.207 1.00 95.04 ? 61 LEU A CA 1 ATOM 466 C C . LEU A 1 61 ? 29.356 -17.353 6.726 1.00 97.01 ? 61 LEU A C 1 ATOM 467 O O . LEU A 1 61 ? 28.440 -17.891 7.348 1.00 99.15 ? 61 LEU A O 1 ATOM 468 C CB . LEU A 1 61 ? 30.448 -18.577 4.834 1.00 93.83 ? 61 LEU A CB 1 ATOM 469 C CG . LEU A 1 61 ? 30.397 -19.009 3.367 1.00 96.61 ? 61 LEU A CG 1 ATOM 470 C CD1 . LEU A 1 61 ? 31.445 -20.080 3.105 1.00 99.60 ? 61 LEU A CD1 1 ATOM 471 C CD2 . LEU A 1 61 ? 29.017 -19.506 2.955 1.00 98.08 ? 61 LEU A CD2 1 ATOM 472 N N . LEU A 1 62 ? 30.300 -16.629 7.317 1.00 95.06 ? 62 LEU A N 1 ATOM 473 C CA . LEU A 1 62 ? 30.299 -16.409 8.764 1.00 94.47 ? 62 LEU A CA 1 ATOM 474 C C . LEU A 1 62 ? 29.209 -15.445 9.226 1.00 94.72 ? 62 LEU A C 1 ATOM 475 O O . LEU A 1 62 ? 28.824 -15.468 10.390 1.00 95.26 ? 62 LEU A O 1 ATOM 476 C CB . LEU A 1 62 ? 31.661 -15.896 9.228 1.00 94.14 ? 62 LEU A CB 1 ATOM 477 C CG . LEU A 1 62 ? 32.802 -16.903 9.114 1.00 93.80 ? 62 LEU A CG 1 ATOM 478 C CD1 . LEU A 1 62 ? 34.132 -16.199 9.294 1.00 94.66 ? 62 LEU A CD1 1 ATOM 479 C CD2 . LEU A 1 62 ? 32.650 -18.023 10.134 1.00 94.81 ? 62 LEU A CD2 1 ATOM 480 N N . GLY A 1 63 ? 28.720 -14.600 8.324 1.00 94.87 ? 63 GLY A N 1 ATOM 481 C CA . GLY A 1 63 ? 27.664 -13.644 8.656 1.00 95.50 ? 63 GLY A CA 1 ATOM 482 C C . GLY A 1 63 ? 28.182 -12.324 9.197 1.00 94.88 ? 63 GLY A C 1 ATOM 483 O O . GLY A 1 63 ? 27.618 -11.775 10.134 1.00 96.72 ? 63 GLY A O 1 ATOM 484 N N . ASN A 1 64 ? 29.262 -11.813 8.612 1.00 94.00 ? 64 ASN A N 1 ATOM 485 C CA . ASN A 1 64 ? 29.736 -10.467 8.910 1.00 91.64 ? 64 ASN A CA 1 ATOM 486 C C . ASN A 1 64 ? 28.531 -9.525 8.861 1.00 93.98 ? 64 ASN A C 1 ATOM 487 O O . ASN A 1 64 ? 27.827 -9.489 7.857 1.00 96.56 ? 64 ASN A O 1 ATOM 488 C CB . ASN A 1 64 ? 30.802 -10.068 7.882 1.00 90.23 ? 64 ASN A CB 1 ATOM 489 C CG . ASN A 1 64 ? 31.329 -8.654 8.076 1.00 89.80 ? 64 ASN A CG 1 ATOM 490 O OD1 . ASN A 1 64 ? 30.582 -7.734 8.396 1.00 88.85 ? 64 ASN A OD1 1 ATOM 491 N ND2 . ASN A 1 64 ? 32.628 -8.474 7.853 1.00 91.33 ? 64 ASN A ND2 1 ATOM 492 N N . PRO A 1 65 ? 28.275 -8.771 9.944 1.00 96.54 ? 65 PRO A N 1 ATOM 493 C CA . PRO A 1 65 ? 27.034 -7.983 10.023 1.00 100.09 ? 65 PRO A CA 1 ATOM 494 C C . PRO A 1 65 ? 26.866 -6.912 8.935 1.00 101.73 ? 65 PRO A C 1 ATOM 495 O O . PRO A 1 65 ? 25.743 -6.473 8.679 1.00 103.38 ? 65 PRO A O 1 ATOM 496 C CB . PRO A 1 65 ? 27.100 -7.350 11.413 1.00 101.03 ? 65 PRO A CB 1 ATOM 497 C CG . PRO A 1 65 ? 28.538 -7.387 11.796 1.00 100.90 ? 65 PRO A CG 1 ATOM 498 C CD . PRO A 1 65 ? 29.112 -8.603 11.142 1.00 99.13 ? 65 PRO A CD 1 ATOM 499 N N . MET A 1 66 ? 27.967 -6.515 8.300 1.00 104.34 ? 66 MET A N 1 ATOM 500 C CA . MET A 1 66 ? 27.931 -5.645 7.117 1.00 108.83 ? 66 MET A CA 1 ATOM 501 C C . MET A 1 66 ? 27.517 -6.390 5.831 1.00 104.26 ? 66 MET A C 1 ATOM 502 O O . MET A 1 66 ? 27.461 -5.788 4.758 1.00 94.51 ? 66 MET A O 1 ATOM 503 C CB . MET A 1 66 ? 29.311 -5.006 6.896 1.00 112.22 ? 66 MET A CB 1 ATOM 504 C CG . MET A 1 66 ? 29.758 -4.041 7.982 1.00 114.74 ? 66 MET A CG 1 ATOM 505 S SD . MET A 1 66 ? 29.135 -2.375 7.699 1.00 124.64 ? 66 MET A SD 1 ATOM 506 C CE . MET A 1 66 ? 30.031 -1.445 8.947 1.00 125.57 ? 66 MET A CE 1 ATOM 507 N N . CYS A 1 67 ? 27.239 -7.688 5.943 1.00 105.69 ? 67 CYS A N 1 ATOM 508 C CA . CYS A 1 67 ? 26.911 -8.531 4.796 1.00 108.84 ? 67 CYS A CA 1 ATOM 509 C C . CYS A 1 67 ? 25.500 -9.109 4.914 1.00 108.70 ? 67 CYS A C 1 ATOM 510 O O . CYS A 1 67 ? 25.255 -10.258 4.539 1.00 105.34 ? 67 CYS A O 1 ATOM 511 C CB . CYS A 1 67 ? 27.939 -9.665 4.689 1.00 111.12 ? 67 CYS A CB 1 ATOM 512 S SG . CYS A 1 67 ? 29.616 -9.098 4.303 1.00 115.77 ? 67 CYS A SG 1 ATOM 513 N N . ASP A 1 68 ? 24.576 -8.304 5.434 1.00 110.37 ? 68 ASP A N 1 ATOM 514 C CA . ASP A 1 68 ? 23.192 -8.737 5.627 1.00 111.28 ? 68 ASP A CA 1 ATOM 515 C C . ASP A 1 68 ? 22.466 -8.936 4.304 1.00 110.85 ? 68 ASP A C 1 ATOM 516 O O . ASP A 1 68 ? 21.509 -9.700 4.236 1.00 112.70 ? 68 ASP A O 1 ATOM 517 C CB . ASP A 1 68 ? 22.413 -7.738 6.490 1.00 115.14 ? 68 ASP A CB 1 ATOM 518 C CG . ASP A 1 68 ? 22.702 -7.888 7.976 1.00 119.96 ? 68 ASP A CG 1 ATOM 519 O OD1 . ASP A 1 68 ? 23.565 -8.715 8.342 1.00 122.86 ? 68 ASP A OD1 1 ATOM 520 O OD2 . ASP A 1 68 ? 22.059 -7.175 8.781 1.00 120.30 ? 68 ASP A OD2 1 ATOM 521 N N . GLU A 1 69 ? 22.917 -8.258 3.254 1.00 106.94 ? 69 GLU A N 1 ATOM 522 C CA . GLU A 1 69 ? 22.358 -8.467 1.922 1.00 104.33 ? 69 GLU A CA 1 ATOM 523 C C . GLU A 1 69 ? 22.352 -9.947 1.529 1.00 102.76 ? 69 GLU A C 1 ATOM 524 O O . GLU A 1 69 ? 21.454 -10.397 0.808 1.00 103.82 ? 69 GLU A O 1 ATOM 525 C CB . GLU A 1 69 ? 23.144 -7.668 0.886 1.00 106.13 ? 69 GLU A CB 1 ATOM 526 C CG . GLU A 1 69 ? 22.578 -7.743 -0.524 1.00 108.80 ? 69 GLU A CG 1 ATOM 527 C CD . GLU A 1 69 ? 23.457 -7.060 -1.553 1.00 109.40 ? 69 GLU A CD 1 ATOM 528 O OE1 . GLU A 1 69 ? 24.352 -6.276 -1.157 1.00 112.98 ? 69 GLU A OE1 1 ATOM 529 O OE2 . GLU A 1 69 ? 23.249 -7.309 -2.763 1.00 103.88 ? 69 GLU A OE2 1 ATOM 530 N N . PHE A 1 70 ? 23.340 -10.697 2.014 1.00 99.84 ? 70 PHE A N 1 ATOM 531 C CA . PHE A 1 70 ? 23.498 -12.113 1.665 1.00 100.62 ? 70 PHE A CA 1 ATOM 532 C C . PHE A 1 70 ? 23.071 -13.056 2.794 1.00 102.86 ? 70 PHE A C 1 ATOM 533 O O . PHE A 1 70 ? 23.553 -14.187 2.899 1.00 99.21 ? 70 PHE A O 1 ATOM 534 C CB . PHE A 1 70 ? 24.946 -12.358 1.246 1.00 97.74 ? 70 PHE A CB 1 ATOM 535 C CG . PHE A 1 70 ? 25.457 -11.319 0.298 1.00 95.56 ? 70 PHE A CG 1 ATOM 536 C CD1 . PHE A 1 70 ? 25.055 -11.328 -1.031 1.00 94.59 ? 70 PHE A CD1 1 ATOM 537 C CD2 . PHE A 1 70 ? 26.270 -10.289 0.746 1.00 92.30 ? 70 PHE A CD2 1 ATOM 538 C CE1 . PHE A 1 70 ? 25.492 -10.356 -1.906 1.00 92.74 ? 70 PHE A CE1 1 ATOM 539 C CE2 . PHE A 1 70 ? 26.706 -9.312 -0.125 1.00 91.79 ? 70 PHE A CE2 1 ATOM 540 C CZ . PHE A 1 70 ? 26.319 -9.345 -1.453 1.00 90.69 ? 70 PHE A CZ 1 ATOM 541 N N . ILE A 1 71 ? 22.134 -12.591 3.612 1.00 106.49 ? 71 ILE A N 1 ATOM 542 C CA . ILE A 1 71 ? 21.622 -13.376 4.726 1.00 112.92 ? 71 ILE A CA 1 ATOM 543 C C . ILE A 1 71 ? 20.867 -14.619 4.221 1.00 113.33 ? 71 ILE A C 1 ATOM 544 O O . ILE A 1 71 ? 20.918 -15.668 4.854 1.00 113.18 ? 71 ILE A O 1 ATOM 545 C CB . ILE A 1 71 ? 20.745 -12.500 5.669 1.00 117.73 ? 71 ILE A CB 1 ATOM 546 C CG1 . ILE A 1 71 ? 20.675 -13.099 7.083 1.00 118.56 ? 71 ILE A CG1 1 ATOM 547 C CG2 . ILE A 1 71 ? 19.355 -12.253 5.082 1.00 119.20 ? 71 ILE A CG2 1 ATOM 548 C CD1 . ILE A 1 71 ? 21.820 -12.682 7.987 1.00 115.74 ? 71 ILE A CD1 1 ATOM 549 N N . ASN A 1 72 ? 20.183 -14.508 3.083 1.00 113.37 ? 72 ASN A N 1 ATOM 550 C CA . ASN A 1 72 ? 19.534 -15.670 2.462 1.00 115.91 ? 72 ASN A CA 1 ATOM 551 C C . ASN A 1 72 ? 19.481 -15.554 0.950 1.00 110.60 ? 72 ASN A C 1 ATOM 552 O O . ASN A 1 72 ? 18.543 -15.001 0.376 1.00 114.64 ? 72 ASN A O 1 ATOM 553 C CB . ASN A 1 72 ? 18.131 -15.892 3.038 1.00 120.30 ? 72 ASN A CB 1 ATOM 554 C CG . ASN A 1 72 ? 18.128 -16.887 4.179 1.00 124.43 ? 72 ASN A CG 1 ATOM 555 O OD1 . ASN A 1 72 ? 18.682 -17.981 4.061 1.00 126.86 ? 72 ASN A OD1 1 ATOM 556 N ND2 . ASN A 1 72 ? 17.510 -16.516 5.293 1.00 129.19 ? 72 ASN A ND2 1 ATOM 557 N N . VAL A 1 73 ? 20.502 -16.094 0.307 1.00 104.82 ? 73 VAL A N 1 ATOM 558 C CA . VAL A 1 73 ? 20.664 -15.906 -1.119 1.00 102.58 ? 73 VAL A CA 1 ATOM 559 C C . VAL A 1 73 ? 20.038 -17.076 -1.860 1.00 101.28 ? 73 VAL A C 1 ATOM 560 O O . VAL A 1 73 ? 20.183 -18.221 -1.439 1.00 101.57 ? 73 VAL A O 1 ATOM 561 C CB . VAL A 1 73 ? 22.153 -15.745 -1.508 1.00 99.97 ? 73 VAL A CB 1 ATOM 562 C CG1 . VAL A 1 73 ? 22.799 -14.658 -0.662 1.00 97.13 ? 73 VAL A CG1 1 ATOM 563 C CG2 . VAL A 1 73 ? 22.920 -17.057 -1.377 1.00 99.58 ? 73 VAL A CG2 1 ATOM 564 N N . PRO A 1 74 ? 19.336 -16.793 -2.969 1.00 100.52 ? 74 PRO A N 1 ATOM 565 C CA . PRO A 1 74 ? 18.800 -17.876 -3.785 1.00 102.29 ? 74 PRO A CA 1 ATOM 566 C C . PRO A 1 74 ? 19.892 -18.653 -4.519 1.00 102.81 ? 74 PRO A C 1 ATOM 567 O O . PRO A 1 74 ? 21.081 -18.380 -4.340 1.00 101.82 ? 74 PRO A O 1 ATOM 568 C CB . PRO A 1 74 ? 17.898 -17.144 -4.786 1.00 101.54 ? 74 PRO A CB 1 ATOM 569 C CG . PRO A 1 74 ? 18.464 -15.775 -4.874 1.00 99.18 ? 74 PRO A CG 1 ATOM 570 C CD . PRO A 1 74 ? 18.967 -15.468 -3.500 1.00 99.28 ? 74 PRO A CD 1 ATOM 571 N N . GLU A 1 75 ? 19.472 -19.618 -5.334 1.00 105.59 ? 75 GLU A N 1 ATOM 572 C CA . GLU A 1 75 ? 20.377 -20.374 -6.190 1.00 102.33 ? 75 GLU A CA 1 ATOM 573 C C . GLU A 1 75 ? 21.113 -19.415 -7.118 1.00 100.95 ? 75 GLU A C 1 ATOM 574 O O . GLU A 1 75 ? 20.535 -18.431 -7.573 1.00 100.39 ? 75 GLU A O 1 ATOM 575 C CB . GLU A 1 75 ? 19.586 -21.391 -7.013 1.00 104.04 ? 75 GLU A CB 1 ATOM 576 C CG . GLU A 1 75 ? 20.447 -22.361 -7.804 1.00 106.85 ? 75 GLU A CG 1 ATOM 577 C CD . GLU A 1 75 ? 19.643 -23.250 -8.735 1.00 109.57 ? 75 GLU A CD 1 ATOM 578 O OE1 . GLU A 1 75 ? 18.463 -23.527 -8.439 1.00 112.94 ? 75 GLU A OE1 1 ATOM 579 O OE2 . GLU A 1 75 ? 20.202 -23.679 -9.768 1.00 114.82 ? 75 GLU A OE2 1 ATOM 580 N N . TRP A 1 76 ? 22.385 -19.696 -7.389 1.00 99.38 ? 76 TRP A N 1 ATOM 581 C CA . TRP A 1 76 ? 23.179 -18.858 -8.291 1.00 99.14 ? 76 TRP A CA 1 ATOM 582 C C . TRP A 1 76 ? 23.760 -19.665 -9.454 1.00 100.15 ? 76 TRP A C 1 ATOM 583 O O . TRP A 1 76 ? 23.863 -20.893 -9.389 1.00 105.97 ? 76 TRP A O 1 ATOM 584 C CB . TRP A 1 76 ? 24.295 -18.136 -7.525 1.00 95.30 ? 76 TRP A CB 1 ATOM 585 C CG . TRP A 1 76 ? 25.268 -19.053 -6.854 1.00 94.20 ? 76 TRP A CG 1 ATOM 586 C CD1 . TRP A 1 76 ? 26.398 -19.583 -7.395 1.00 95.16 ? 76 TRP A CD1 1 ATOM 587 C CD2 . TRP A 1 76 ? 25.197 -19.548 -5.514 1.00 94.75 ? 76 TRP A CD2 1 ATOM 588 N NE1 . TRP A 1 76 ? 27.036 -20.382 -6.476 1.00 94.10 ? 76 TRP A NE1 1 ATOM 589 C CE2 . TRP A 1 76 ? 26.318 -20.376 -5.314 1.00 91.87 ? 76 TRP A CE2 1 ATOM 590 C CE3 . TRP A 1 76 ? 24.288 -19.378 -4.465 1.00 96.00 ? 76 TRP A CE3 1 ATOM 591 C CZ2 . TRP A 1 76 ? 26.554 -21.029 -4.114 1.00 92.58 ? 76 TRP A CZ2 1 ATOM 592 C CZ3 . TRP A 1 76 ? 24.525 -20.027 -3.275 1.00 94.64 ? 76 TRP A CZ3 1 ATOM 593 C CH2 . TRP A 1 76 ? 25.647 -20.845 -3.108 1.00 93.39 ? 76 TRP A CH2 1 ATOM 594 N N . SER A 1 77 ? 24.122 -18.961 -10.521 1.00 97.25 ? 77 SER A N 1 ATOM 595 C CA . SER A 1 77 ? 24.788 -19.573 -11.671 1.00 95.97 ? 77 SER A CA 1 ATOM 596 C C . SER A 1 77 ? 26.296 -19.557 -11.460 1.00 93.98 ? 77 SER A C 1 ATOM 597 O O . SER A 1 77 ? 26.968 -20.568 -11.653 1.00 95.32 ? 77 SER A O 1 ATOM 598 C CB . SER A 1 77 ? 24.435 -18.820 -12.951 1.00 95.65 ? 77 SER A CB 1 ATOM 599 O OG . SER A 1 77 ? 24.541 -17.416 -12.767 1.00 95.36 ? 77 SER A OG 1 ATOM 600 N N . TYR A 1 78 ? 26.816 -18.393 -11.074 1.00 90.19 ? 78 TYR A N 1 ATOM 601 C CA . TYR A 1 78 ? 28.213 -18.242 -10.672 1.00 87.02 ? 78 TYR A CA 1 ATOM 602 C C . TYR A 1 78 ? 28.312 -17.209 -9.549 1.00 86.34 ? 78 TYR A C 1 ATOM 603 O O . TYR A 1 78 ? 27.353 -16.499 -9.264 1.00 83.80 ? 78 TYR A O 1 ATOM 604 C CB . TYR A 1 78 ? 29.092 -17.836 -11.872 1.00 84.21 ? 78 TYR A CB 1 ATOM 605 C CG . TYR A 1 78 ? 28.658 -16.560 -12.583 1.00 81.37 ? 78 TYR A CG 1 ATOM 606 C CD1 . TYR A 1 78 ? 27.608 -16.568 -13.495 1.00 80.58 ? 78 TYR A CD1 1 ATOM 607 C CD2 . TYR A 1 78 ? 29.299 -15.350 -12.342 1.00 78.39 ? 78 TYR A CD2 1 ATOM 608 C CE1 . TYR A 1 78 ? 27.204 -15.407 -14.142 1.00 79.72 ? 78 TYR A CE1 1 ATOM 609 C CE2 . TYR A 1 78 ? 28.899 -14.186 -12.982 1.00 77.46 ? 78 TYR A CE2 1 ATOM 610 C CZ . TYR A 1 78 ? 27.853 -14.218 -13.883 1.00 78.32 ? 78 TYR A CZ 1 ATOM 611 O OH . TYR A 1 78 ? 27.462 -13.062 -14.524 1.00 77.33 ? 78 TYR A OH 1 ATOM 612 N N . ILE A 1 79 ? 29.476 -17.135 -8.918 1.00 86.79 ? 79 ILE A N 1 ATOM 613 C CA . ILE A 1 79 ? 29.733 -16.157 -7.869 1.00 86.05 ? 79 ILE A CA 1 ATOM 614 C C . ILE A 1 79 ? 30.766 -15.128 -8.342 1.00 87.38 ? 79 ILE A C 1 ATOM 615 O O . ILE A 1 79 ? 31.731 -15.481 -9.029 1.00 82.39 ? 79 ILE A O 1 ATOM 616 C CB . ILE A 1 79 ? 30.258 -16.852 -6.604 1.00 88.04 ? 79 ILE A CB 1 ATOM 617 C CG1 . ILE A 1 79 ? 29.205 -17.811 -6.049 1.00 90.11 ? 79 ILE A CG1 1 ATOM 618 C CG2 . ILE A 1 79 ? 30.641 -15.824 -5.549 1.00 90.55 ? 79 ILE A CG2 1 ATOM 619 C CD1 . ILE A 1 79 ? 29.746 -18.784 -5.025 1.00 91.03 ? 79 ILE A CD1 1 ATOM 620 N N . VAL A 1 80 ? 30.567 -13.865 -7.965 1.00 88.50 ? 80 VAL A N 1 ATOM 621 C CA . VAL A 1 80 ? 31.491 -12.785 -8.320 1.00 86.52 ? 80 VAL A CA 1 ATOM 622 C C . VAL A 1 80 ? 32.000 -12.086 -7.067 1.00 87.17 ? 80 VAL A C 1 ATOM 623 O O . VAL A 1 80 ? 31.258 -11.358 -6.408 1.00 90.29 ? 80 VAL A O 1 ATOM 624 C CB . VAL A 1 80 ? 30.819 -11.727 -9.215 1.00 86.88 ? 80 VAL A CB 1 ATOM 625 C CG1 . VAL A 1 80 ? 31.801 -10.610 -9.555 1.00 86.38 ? 80 VAL A CG1 1 ATOM 626 C CG2 . VAL A 1 80 ? 30.271 -12.371 -10.475 1.00 86.47 ? 80 VAL A CG2 1 ATOM 627 N N . GLU A 1 81 ? 33.272 -12.307 -6.758 1.00 88.11 ? 81 GLU A N 1 ATOM 628 C CA . GLU A 1 81 ? 33.937 -11.687 -5.619 1.00 89.03 ? 81 GLU A CA 1 ATOM 629 C C . GLU A 1 81 ? 34.910 -10.650 -6.155 1.00 84.62 ? 81 GLU A C 1 ATOM 630 O O . GLU A 1 81 ? 35.434 -10.807 -7.243 1.00 84.46 ? 81 GLU A O 1 ATOM 631 C CB . GLU A 1 81 ? 34.690 -12.763 -4.835 1.00 93.87 ? 81 GLU A CB 1 ATOM 632 C CG . GLU A 1 81 ? 35.228 -12.332 -3.479 1.00 100.53 ? 81 GLU A CG 1 ATOM 633 C CD . GLU A 1 81 ? 36.123 -13.388 -2.833 1.00 106.80 ? 81 GLU A CD 1 ATOM 634 O OE1 . GLU A 1 81 ? 36.788 -14.156 -3.574 1.00 102.92 ? 81 GLU A OE1 1 ATOM 635 O OE2 . GLU A 1 81 ? 36.166 -13.448 -1.578 1.00 108.78 ? 81 GLU A OE2 1 ATOM 636 N N . LYS A 1 82 ? 35.156 -9.588 -5.407 1.00 88.08 ? 82 LYS A N 1 ATOM 637 C CA . LYS A 1 82 ? 36.181 -8.628 -5.810 1.00 88.99 ? 82 LYS A CA 1 ATOM 638 C C . LYS A 1 82 ? 37.587 -9.146 -5.470 1.00 91.83 ? 82 LYS A C 1 ATOM 639 O O . LYS A 1 82 ? 37.750 -10.177 -4.802 1.00 89.87 ? 82 LYS A O 1 ATOM 640 C CB . LYS A 1 82 ? 35.932 -7.265 -5.165 1.00 89.52 ? 82 LYS A CB 1 ATOM 641 C CG . LYS A 1 82 ? 34.671 -6.593 -5.668 1.00 89.54 ? 82 LYS A CG 1 ATOM 642 C CD . LYS A 1 82 ? 34.616 -5.127 -5.277 1.00 91.04 ? 82 LYS A CD 1 ATOM 643 C CE . LYS A 1 82 ? 33.217 -4.546 -5.441 1.00 94.78 ? 82 LYS A CE 1 ATOM 644 N NZ . LYS A 1 82 ? 32.595 -4.880 -6.755 1.00 99.05 ? 82 LYS A NZ 1 ATOM 645 N N . ALA A 1 83 ? 38.600 -8.435 -5.957 1.00 94.73 ? 83 ALA A N 1 ATOM 646 C CA . ALA A 1 83 ? 39.992 -8.802 -5.694 1.00 94.94 ? 83 ALA A CA 1 ATOM 647 C C . ALA A 1 83 ? 40.352 -8.572 -4.224 1.00 97.95 ? 83 ALA A C 1 ATOM 648 O O . ALA A 1 83 ? 40.977 -9.425 -3.593 1.00 101.69 ? 83 ALA A O 1 ATOM 649 C CB . ALA A 1 83 ? 40.925 -8.015 -6.599 1.00 90.47 ? 83 ALA A CB 1 ATOM 650 N N . ASN A 1 84 ? 39.953 -7.421 -3.684 1.00 96.71 ? 84 ASN A N 1 ATOM 651 C CA . ASN A 1 84 ? 40.206 -7.095 -2.287 1.00 98.44 ? 84 ASN A CA 1 ATOM 652 C C . ASN A 1 84 ? 38.967 -6.528 -1.616 1.00 96.70 ? 84 ASN A C 1 ATOM 653 O O . ASN A 1 84 ? 38.876 -5.320 -1.402 1.00 95.65 ? 84 ASN A O 1 ATOM 654 C CB . ASN A 1 84 ? 41.379 -6.127 -2.177 1.00 104.32 ? 84 ASN A CB 1 ATOM 655 C CG . ASN A 1 84 ? 42.708 -6.813 -2.417 1.00 111.14 ? 84 ASN A CG 1 ATOM 656 O OD1 . ASN A 1 84 ? 43.232 -7.490 -1.533 1.00 116.24 ? 84 ASN A OD1 1 ATOM 657 N ND2 . ASN A 1 84 ? 43.252 -6.657 -3.619 1.00 114.32 ? 84 ASN A ND2 1 ATOM 658 N N . PRO A 1 85 ? 38.006 -7.408 -1.270 1.00 96.13 ? 85 PRO A N 1 ATOM 659 C CA . PRO A 1 85 ? 36.758 -6.949 -0.667 1.00 95.69 ? 85 PRO A CA 1 ATOM 660 C C . PRO A 1 85 ? 37.026 -6.376 0.711 1.00 97.20 ? 85 PRO A C 1 ATOM 661 O O . PRO A 1 85 ? 37.839 -6.935 1.446 1.00 97.26 ? 85 PRO A O 1 ATOM 662 C CB . PRO A 1 85 ? 35.910 -8.228 -0.566 1.00 95.98 ? 85 PRO A CB 1 ATOM 663 C CG . PRO A 1 85 ? 36.679 -9.312 -1.253 1.00 93.91 ? 85 PRO A CG 1 ATOM 664 C CD . PRO A 1 85 ? 38.105 -8.877 -1.274 1.00 93.67 ? 85 PRO A CD 1 ATOM 665 N N . VAL A 1 86 ? 36.364 -5.273 1.055 1.00 98.22 ? 86 VAL A N 1 ATOM 666 C CA . VAL A 1 86 ? 36.625 -4.606 2.337 1.00 100.58 ? 86 VAL A CA 1 ATOM 667 C C . VAL A 1 86 ? 36.034 -5.374 3.522 1.00 98.71 ? 86 VAL A C 1 ATOM 668 O O . VAL A 1 86 ? 36.657 -5.452 4.585 1.00 100.57 ? 86 VAL A O 1 ATOM 669 C CB . VAL A 1 86 ? 36.123 -3.139 2.363 1.00 101.80 ? 86 VAL A CB 1 ATOM 670 C CG1 . VAL A 1 86 ? 36.688 -2.362 1.180 1.00 102.69 ? 86 VAL A CG1 1 ATOM 671 C CG2 . VAL A 1 86 ? 34.601 -3.067 2.393 1.00 101.51 ? 86 VAL A CG2 1 ATOM 672 N N . ASN A 1 87 ? 34.848 -5.947 3.329 1.00 92.79 ? 87 ASN A N 1 ATOM 673 C CA . ASN A 1 87 ? 34.139 -6.634 4.403 1.00 92.37 ? 87 ASN A CA 1 ATOM 674 C C . ASN A 1 87 ? 34.476 -8.113 4.424 1.00 92.60 ? 87 ASN A C 1 ATOM 675 O O . ASN A 1 87 ? 33.739 -8.934 3.887 1.00 91.21 ? 87 ASN A O 1 ATOM 676 C CB . ASN A 1 87 ? 32.629 -6.436 4.262 1.00 92.33 ? 87 ASN A CB 1 ATOM 677 C CG . ASN A 1 87 ? 32.215 -4.985 4.423 1.00 92.15 ? 87 ASN A CG 1 ATOM 678 O OD1 . ASN A 1 87 ? 32.646 -4.303 5.352 1.00 94.89 ? 87 ASN A OD1 1 ATOM 679 N ND2 . ASN A 1 87 ? 31.378 -4.506 3.517 1.00 91.98 ? 87 ASN A ND2 1 ATOM 680 N N . ASP A 1 88 ? 35.603 -8.436 5.048 1.00 96.20 ? 88 ASP A N 1 ATOM 681 C CA . ASP A 1 88 ? 36.080 -9.811 5.168 1.00 97.18 ? 88 ASP A CA 1 ATOM 682 C C . ASP A 1 88 ? 35.821 -10.241 6.620 1.00 97.66 ? 88 ASP A C 1 ATOM 683 O O . ASP A 1 88 ? 34.662 -10.466 6.991 1.00 94.10 ? 88 ASP A O 1 ATOM 684 C CB . ASP A 1 88 ? 37.566 -9.879 4.740 1.00 100.64 ? 88 ASP A CB 1 ATOM 685 C CG . ASP A 1 88 ? 38.126 -11.310 4.669 1.00 103.28 ? 88 ASP A CG 1 ATOM 686 O OD1 . ASP A 1 88 ? 37.393 -12.248 4.290 1.00 100.04 ? 88 ASP A OD1 1 ATOM 687 O OD2 . ASP A 1 88 ? 39.333 -11.483 4.969 1.00 109.47 ? 88 ASP A OD2 1 ATOM 688 N N . LEU A 1 89 ? 36.872 -10.322 7.438 1.00 98.43 ? 89 LEU A N 1 ATOM 689 C CA . LEU A 1 89 ? 36.749 -10.702 8.840 1.00 98.76 ? 89 LEU A CA 1 ATOM 690 C C . LEU A 1 89 ? 36.850 -9.456 9.693 1.00 98.99 ? 89 LEU A C 1 ATOM 691 O O . LEU A 1 89 ? 37.944 -9.063 10.098 1.00 98.45 ? 89 LEU A O 1 ATOM 692 C CB . LEU A 1 89 ? 37.849 -11.692 9.241 1.00 98.23 ? 89 LEU A CB 1 ATOM 693 C CG . LEU A 1 89 ? 37.907 -13.017 8.478 1.00 97.25 ? 89 LEU A CG 1 ATOM 694 C CD1 . LEU A 1 89 ? 38.989 -13.912 9.062 1.00 96.71 ? 89 LEU A CD1 1 ATOM 695 C CD2 . LEU A 1 89 ? 36.558 -13.721 8.492 1.00 98.23 ? 89 LEU A CD2 1 ATOM 696 N N . CYS A 1 90 ? 35.697 -8.847 9.966 1.00 104.44 ? 90 CYS A N 1 ATOM 697 C CA . CYS A 1 90 ? 35.621 -7.636 10.781 1.00 105.17 ? 90 CYS A CA 1 ATOM 698 C C . CYS A 1 90 ? 36.529 -7.738 12.007 1.00 99.37 ? 90 CYS A C 1 ATOM 699 O O . CYS A 1 90 ? 37.365 -6.861 12.236 1.00 99.97 ? 90 CYS A O 1 ATOM 700 C CB . CYS A 1 90 ? 34.165 -7.330 11.182 1.00 112.09 ? 90 CYS A CB 1 ATOM 701 S SG . CYS A 1 90 ? 33.199 -8.673 11.940 1.00 121.47 ? 90 CYS A SG 1 ATOM 702 N N . TYR A 1 91 ? 36.374 -8.818 12.771 1.00 94.86 ? 91 TYR A N 1 ATOM 703 C CA . TYR A 1 91 ? 37.284 -9.133 13.871 1.00 94.56 ? 91 TYR A CA 1 ATOM 704 C C . TYR A 1 91 ? 38.453 -9.902 13.279 1.00 92.42 ? 91 TYR A C 1 ATOM 705 O O . TYR A 1 91 ? 38.246 -10.941 12.663 1.00 93.37 ? 91 TYR A O 1 ATOM 706 C CB . TYR A 1 91 ? 36.584 -9.979 14.936 1.00 95.56 ? 91 TYR A CB 1 ATOM 707 C CG . TYR A 1 91 ? 37.319 -10.069 16.260 1.00 95.11 ? 91 TYR A CG 1 ATOM 708 C CD1 . TYR A 1 91 ? 38.456 -10.849 16.393 1.00 96.05 ? 91 TYR A CD1 1 ATOM 709 C CD2 . TYR A 1 91 ? 36.864 -9.384 17.382 1.00 95.61 ? 91 TYR A CD2 1 ATOM 710 C CE1 . TYR A 1 91 ? 39.129 -10.943 17.600 1.00 96.14 ? 91 TYR A CE1 1 ATOM 711 C CE2 . TYR A 1 91 ? 37.530 -9.474 18.596 1.00 95.60 ? 91 TYR A CE2 1 ATOM 712 C CZ . TYR A 1 91 ? 38.661 -10.256 18.697 1.00 93.56 ? 91 TYR A CZ 1 ATOM 713 O OH . TYR A 1 91 ? 39.335 -10.360 19.886 1.00 92.60 ? 91 TYR A OH 1 ATOM 714 N N . PRO A 1 92 ? 39.688 -9.407 13.473 1.00 92.92 ? 92 PRO A N 1 ATOM 715 C CA . PRO A 1 92 ? 40.832 -10.000 12.794 1.00 91.33 ? 92 PRO A CA 1 ATOM 716 C C . PRO A 1 92 ? 41.079 -11.444 13.195 1.00 93.38 ? 92 PRO A C 1 ATOM 717 O O . PRO A 1 92 ? 40.773 -11.840 14.310 1.00 95.16 ? 92 PRO A O 1 ATOM 718 C CB . PRO A 1 92 ? 41.996 -9.128 13.253 1.00 91.62 ? 92 PRO A CB 1 ATOM 719 C CG . PRO A 1 92 ? 41.589 -8.681 14.609 1.00 94.20 ? 92 PRO A CG 1 ATOM 720 C CD . PRO A 1 92 ? 40.116 -8.414 14.476 1.00 94.25 ? 92 PRO A CD 1 ATOM 721 N N . GLY A 1 93 ? 41.636 -12.219 12.278 1.00 99.18 ? 93 GLY A N 1 ATOM 722 C CA . GLY A 1 93 ? 41.917 -13.619 12.536 1.00 102.32 ? 93 GLY A CA 1 ATOM 723 C C . GLY A 1 93 ? 42.208 -14.366 11.253 1.00 102.62 ? 93 GLY A C 1 ATOM 724 O O . GLY A 1 93 ? 42.611 -13.764 10.262 1.00 98.15 ? 93 GLY A O 1 ATOM 725 N N . ASP A 1 94 ? 41.994 -15.678 11.280 1.00 105.51 ? 94 ASP A N 1 ATOM 726 C CA . ASP A 1 94 ? 42.252 -16.533 10.133 1.00 106.78 ? 94 ASP A CA 1 ATOM 727 C C . ASP A 1 94 ? 41.042 -17.429 9.852 1.00 105.05 ? 94 ASP A C 1 ATOM 728 O O . ASP A 1 94 ? 40.128 -17.548 10.675 1.00 106.01 ? 94 ASP A O 1 ATOM 729 C CB . ASP A 1 94 ? 43.504 -17.388 10.381 1.00 113.06 ? 94 ASP A CB 1 ATOM 730 C CG . ASP A 1 94 ? 44.445 -17.413 9.182 1.00 120.89 ? 94 ASP A CG 1 ATOM 731 O OD1 . ASP A 1 94 ? 45.192 -16.425 9.004 1.00 122.77 ? 94 ASP A OD1 1 ATOM 732 O OD2 . ASP A 1 94 ? 44.433 -18.405 8.413 1.00 126.34 ? 94 ASP A OD2 1 ATOM 733 N N . PHE A 1 95 ? 41.053 -18.044 8.673 1.00 97.87 ? 95 PHE A N 1 ATOM 734 C CA . PHE A 1 95 ? 40.018 -18.965 8.247 1.00 90.97 ? 95 PHE A CA 1 ATOM 735 C C . PHE A 1 95 ? 40.729 -20.207 7.741 1.00 90.70 ? 95 PHE A C 1 ATOM 736 O O . PHE A 1 95 ? 41.349 -20.188 6.684 1.00 92.83 ? 95 PHE A O 1 ATOM 737 C CB . PHE A 1 95 ? 39.193 -18.320 7.142 1.00 88.07 ? 95 PHE A CB 1 ATOM 738 C CG . PHE A 1 95 ? 37.852 -18.948 6.940 1.00 90.36 ? 95 PHE A CG 1 ATOM 739 C CD1 . PHE A 1 95 ? 37.736 -20.274 6.572 1.00 94.92 ? 95 PHE A CD1 1 ATOM 740 C CD2 . PHE A 1 95 ? 36.698 -18.207 7.116 1.00 94.19 ? 95 PHE A CD2 1 ATOM 741 C CE1 . PHE A 1 95 ? 36.493 -20.849 6.381 1.00 96.89 ? 95 PHE A CE1 1 ATOM 742 C CE2 . PHE A 1 95 ? 35.451 -18.775 6.930 1.00 94.53 ? 95 PHE A CE2 1 ATOM 743 C CZ . PHE A 1 95 ? 35.348 -20.100 6.563 1.00 96.28 ? 95 PHE A CZ 1 ATOM 744 N N . ASN A 1 96 ? 40.652 -21.285 8.504 1.00 91.79 ? 96 ASN A N 1 ATOM 745 C CA . ASN A 1 96 ? 41.410 -22.489 8.202 1.00 93.18 ? 96 ASN A CA 1 ATOM 746 C C . ASN A 1 96 ? 40.909 -23.158 6.926 1.00 92.84 ? 96 ASN A C 1 ATOM 747 O O . ASN A 1 96 ? 39.704 -23.294 6.744 1.00 92.43 ? 96 ASN A O 1 ATOM 748 C CB . ASN A 1 96 ? 41.303 -23.465 9.375 1.00 98.57 ? 96 ASN A CB 1 ATOM 749 C CG . ASN A 1 96 ? 42.475 -24.416 9.452 1.00 101.95 ? 96 ASN A CG 1 ATOM 750 O OD1 . ASN A 1 96 ? 43.630 -23.992 9.456 1.00 101.43 ? 96 ASN A OD1 1 ATOM 751 N ND2 . ASN A 1 96 ? 42.186 -25.710 9.533 1.00 106.22 ? 96 ASN A ND2 1 ATOM 752 N N . ASP A 1 97 ? 41.836 -23.570 6.054 1.00 95.37 ? 97 ASP A N 1 ATOM 753 C CA . ASP A 1 97 ? 41.520 -24.228 4.767 1.00 93.52 ? 97 ASP A CA 1 ATOM 754 C C . ASP A 1 97 ? 40.542 -23.425 3.917 1.00 89.06 ? 97 ASP A C 1 ATOM 755 O O . ASP A 1 97 ? 39.630 -23.977 3.307 1.00 88.77 ? 97 ASP A O 1 ATOM 756 C CB . ASP A 1 97 ? 40.969 -25.646 4.987 1.00 99.40 ? 97 ASP A CB 1 ATOM 757 C CG . ASP A 1 97 ? 42.041 -26.642 5.400 1.00 107.42 ? 97 ASP A CG 1 ATOM 758 O OD1 . ASP A 1 97 ? 43.234 -26.407 5.109 1.00 114.14 ? 97 ASP A OD1 1 ATOM 759 O OD2 . ASP A 1 97 ? 41.680 -27.677 6.006 1.00 113.29 ? 97 ASP A OD2 1 ATOM 760 N N . TYR A 1 98 ? 40.746 -22.117 3.875 1.00 85.56 ? 98 TYR A N 1 ATOM 761 C CA . TYR A 1 98 ? 39.798 -21.208 3.243 1.00 85.48 ? 98 TYR A CA 1 ATOM 762 C C . TYR A 1 98 ? 39.709 -21.465 1.748 1.00 87.36 ? 98 TYR A C 1 ATOM 763 O O . TYR A 1 98 ? 38.623 -21.475 1.163 1.00 84.03 ? 98 TYR A O 1 ATOM 764 C CB . TYR A 1 98 ? 40.237 -19.773 3.515 1.00 84.30 ? 98 TYR A CB 1 ATOM 765 C CG . TYR A 1 98 ? 39.329 -18.699 2.982 1.00 83.55 ? 98 TYR A CG 1 ATOM 766 C CD1 . TYR A 1 98 ? 37.958 -18.739 3.199 1.00 84.55 ? 98 TYR A CD1 1 ATOM 767 C CD2 . TYR A 1 98 ? 39.852 -17.615 2.284 1.00 84.90 ? 98 TYR A CD2 1 ATOM 768 C CE1 . TYR A 1 98 ? 37.130 -17.736 2.715 1.00 86.11 ? 98 TYR A CE1 1 ATOM 769 C CE2 . TYR A 1 98 ? 39.038 -16.610 1.798 1.00 84.75 ? 98 TYR A CE2 1 ATOM 770 C CZ . TYR A 1 98 ? 37.679 -16.670 2.017 1.00 87.04 ? 98 TYR A CZ 1 ATOM 771 O OH . TYR A 1 98 ? 36.875 -15.666 1.527 1.00 92.07 ? 98 TYR A OH 1 ATOM 772 N N . GLU A 1 99 ? 40.867 -21.707 1.145 1.00 92.94 ? 99 GLU A N 1 ATOM 773 C CA . GLU A 1 99 ? 40.965 -21.893 -0.293 1.00 92.42 ? 99 GLU A CA 1 ATOM 774 C C . GLU A 1 99 ? 40.385 -23.247 -0.695 1.00 91.92 ? 99 GLU A C 1 ATOM 775 O O . GLU A 1 99 ? 39.778 -23.368 -1.758 1.00 92.84 ? 99 GLU A O 1 ATOM 776 C CB . GLU A 1 99 ? 42.417 -21.749 -0.762 1.00 96.50 ? 99 GLU A CB 1 ATOM 777 C CG . GLU A 1 99 ? 43.016 -20.353 -0.568 1.00 98.07 ? 99 GLU A CG 1 ATOM 778 C CD . GLU A 1 99 ? 43.412 -20.052 0.870 1.00 103.73 ? 99 GLU A CD 1 ATOM 779 O OE1 . GLU A 1 99 ? 43.649 -21.005 1.640 1.00 107.95 ? 99 GLU A OE1 1 ATOM 780 O OE2 . GLU A 1 99 ? 43.484 -18.859 1.238 1.00 108.32 ? 99 GLU A OE2 1 ATOM 781 N N . GLU A 1 100 ? 40.548 -24.258 0.157 1.00 91.93 ? 100 GLU A N 1 ATOM 782 C CA . GLU A 1 100 ? 39.903 -25.550 -0.084 1.00 90.76 ? 100 GLU A CA 1 ATOM 783 C C . GLU A 1 100 ? 38.386 -25.439 0.028 1.00 89.73 ? 100 GLU A C 1 ATOM 784 O O . GLU A 1 100 ? 37.661 -26.223 -0.581 1.00 95.99 ? 100 GLU A O 1 ATOM 785 C CB . GLU A 1 100 ? 40.430 -26.634 0.862 1.00 93.10 ? 100 GLU A CB 1 ATOM 786 C CG . GLU A 1 100 ? 41.747 -27.263 0.416 1.00 97.50 ? 100 GLU A CG 1 ATOM 787 C CD . GLU A 1 100 ? 41.627 -28.124 -0.842 1.00 96.88 ? 100 GLU A CD 1 ATOM 788 O OE1 . GLU A 1 100 ? 40.730 -28.996 -0.905 1.00 96.77 ? 100 GLU A OE1 1 ATOM 789 O OE2 . GLU A 1 100 ? 42.449 -27.941 -1.769 1.00 94.35 ? 100 GLU A OE2 1 ATOM 790 N N . LEU A 1 101 ? 37.902 -24.467 0.792 1.00 88.64 ? 101 LEU A N 1 ATOM 791 C CA . LEU A 1 101 ? 36.463 -24.250 0.902 1.00 90.79 ? 101 LEU A CA 1 ATOM 792 C C . LEU A 1 101 ? 35.922 -23.530 -0.330 1.00 87.61 ? 101 LEU A C 1 ATOM 793 O O . LEU A 1 101 ? 34.925 -23.957 -0.921 1.00 84.12 ? 101 LEU A O 1 ATOM 794 C CB . LEU A 1 101 ? 36.129 -23.466 2.170 1.00 94.13 ? 101 LEU A CB 1 ATOM 795 C CG . LEU A 1 101 ? 34.646 -23.177 2.411 1.00 96.34 ? 101 LEU A CG 1 ATOM 796 C CD1 . LEU A 1 101 ? 33.789 -24.434 2.284 1.00 97.08 ? 101 LEU A CD1 1 ATOM 797 C CD2 . LEU A 1 101 ? 34.486 -22.540 3.782 1.00 100.10 ? 101 LEU A CD2 1 ATOM 798 N N . LYS A 1 102 ? 36.580 -22.441 -0.717 1.00 86.41 ? 102 LYS A N 1 ATOM 799 C CA . LYS A 1 102 ? 36.254 -21.768 -1.975 1.00 86.27 ? 102 LYS A CA 1 ATOM 800 C C . LYS A 1 102 ? 36.192 -22.758 -3.130 1.00 86.34 ? 102 LYS A C 1 ATOM 801 O O . LYS A 1 102 ? 35.303 -22.678 -3.983 1.00 87.83 ? 102 LYS A O 1 ATOM 802 C CB . LYS A 1 102 ? 37.275 -20.681 -2.297 1.00 87.91 ? 102 LYS A CB 1 ATOM 803 C CG . LYS A 1 102 ? 37.034 -19.359 -1.589 1.00 92.58 ? 102 LYS A CG 1 ATOM 804 C CD . LYS A 1 102 ? 38.199 -18.403 -1.795 1.00 95.70 ? 102 LYS A CD 1 ATOM 805 C CE . LYS A 1 102 ? 37.747 -16.957 -1.718 1.00 101.57 ? 102 LYS A CE 1 ATOM 806 N NZ . LYS A 1 102 ? 38.888 -16.008 -1.588 1.00 107.27 ? 102 LYS A NZ 1 ATOM 807 N N . HIS A 1 103 ? 37.130 -23.697 -3.165 1.00 86.93 ? 103 HIS A N 1 ATOM 808 C CA . HIS A 1 103 ? 37.122 -24.693 -4.224 1.00 88.23 ? 103 HIS A CA 1 ATOM 809 C C . HIS A 1 103 ? 35.859 -25.546 -4.154 1.00 91.74 ? 103 HIS A C 1 ATOM 810 O O . HIS A 1 103 ? 35.333 -25.978 -5.178 1.00 93.93 ? 103 HIS A O 1 ATOM 811 C CB . HIS A 1 103 ? 38.360 -25.583 -4.171 1.00 89.11 ? 103 HIS A CB 1 ATOM 812 C CG . HIS A 1 103 ? 38.397 -26.600 -5.267 1.00 90.49 ? 103 HIS A CG 1 ATOM 813 N ND1 . HIS A 1 103 ? 38.824 -26.302 -6.544 1.00 88.14 ? 103 HIS A ND1 1 ATOM 814 C CD2 . HIS A 1 103 ? 38.013 -27.898 -5.291 1.00 90.96 ? 103 HIS A CD2 1 ATOM 815 C CE1 . HIS A 1 103 ? 38.720 -27.378 -7.301 1.00 88.34 ? 103 HIS A CE1 1 ATOM 816 N NE2 . HIS A 1 103 ? 38.232 -28.360 -6.564 1.00 91.22 ? 103 HIS A NE2 1 ATOM 817 N N . LEU A 1 104 ? 35.373 -25.783 -2.942 1.00 95.38 ? 104 LEU A N 1 ATOM 818 C CA . LEU A 1 104 ? 34.122 -26.509 -2.755 1.00 98.49 ? 104 LEU A CA 1 ATOM 819 C C . LEU A 1 104 ? 32.928 -25.740 -3.350 1.00 99.39 ? 104 LEU A C 1 ATOM 820 O O . LEU A 1 104 ? 32.032 -26.347 -3.936 1.00 101.52 ? 104 LEU A O 1 ATOM 821 C CB . LEU A 1 104 ? 33.899 -26.803 -1.267 1.00 99.31 ? 104 LEU A CB 1 ATOM 822 C CG . LEU A 1 104 ? 33.417 -28.206 -0.890 1.00 100.37 ? 104 LEU A CG 1 ATOM 823 C CD1 . LEU A 1 104 ? 34.402 -29.281 -1.328 1.00 100.17 ? 104 LEU A CD1 1 ATOM 824 C CD2 . LEU A 1 104 ? 33.205 -28.267 0.615 1.00 103.07 ? 104 LEU A CD2 1 ATOM 825 N N . LEU A 1 105 ? 32.934 -24.413 -3.221 1.00 98.99 ? 105 LEU A N 1 ATOM 826 C CA . LEU A 1 105 ? 31.859 -23.565 -3.761 1.00 99.67 ? 105 LEU A CA 1 ATOM 827 C C . LEU A 1 105 ? 31.780 -23.473 -5.281 1.00 101.52 ? 105 LEU A C 1 ATOM 828 O O . LEU A 1 105 ? 30.767 -23.020 -5.828 1.00 101.08 ? 105 LEU A O 1 ATOM 829 C CB . LEU A 1 105 ? 31.994 -22.142 -3.243 1.00 98.61 ? 105 LEU A CB 1 ATOM 830 C CG . LEU A 1 105 ? 31.703 -21.922 -1.780 1.00 98.96 ? 105 LEU A CG 1 ATOM 831 C CD1 . LEU A 1 105 ? 31.727 -20.427 -1.516 1.00 99.41 ? 105 LEU A CD1 1 ATOM 832 C CD2 . LEU A 1 105 ? 30.356 -22.521 -1.425 1.00 101.70 ? 105 LEU A CD2 1 ATOM 833 N N . SER A 1 106 ? 32.851 -23.855 -5.965 1.00 104.94 ? 106 SER A N 1 ATOM 834 C CA A SER A 1 106 ? 32.857 -23.884 -7.426 0.50 106.32 ? 106 SER A CA 1 ATOM 835 C CA B SER A 1 106 ? 32.841 -23.867 -7.421 0.50 104.99 ? 106 SER A CA 1 ATOM 836 C C . SER A 1 106 ? 31.951 -25.001 -7.931 1.00 106.58 ? 106 SER A C 1 ATOM 837 O O . SER A 1 106 ? 31.578 -25.026 -9.101 1.00 107.39 ? 106 SER A O 1 ATOM 838 C CB A SER A 1 106 ? 34.278 -24.091 -7.963 0.50 106.67 ? 106 SER A CB 1 ATOM 839 C CB B SER A 1 106 ? 34.266 -24.001 -7.959 0.50 103.86 ? 106 SER A CB 1 ATOM 840 O OG A SER A 1 106 ? 34.713 -25.430 -7.781 0.50 108.39 ? 106 SER A OG 1 ATOM 841 O OG B SER A 1 106 ? 35.095 -22.980 -7.425 0.50 100.58 ? 106 SER A OG 1 ATOM 842 N N . ARG A 1 107 ? 31.608 -25.928 -7.037 1.00 111.41 ? 107 ARG A N 1 ATOM 843 C CA . ARG A 1 107 ? 30.745 -27.057 -7.364 1.00 113.32 ? 107 ARG A CA 1 ATOM 844 C C . ARG A 1 107 ? 29.382 -26.937 -6.682 1.00 106.42 ? 107 ARG A C 1 ATOM 845 O O . ARG A 1 107 ? 28.621 -27.904 -6.652 1.00 102.71 ? 107 ARG A O 1 ATOM 846 C CB . ARG A 1 107 ? 31.430 -28.369 -6.958 1.00 122.25 ? 107 ARG A CB 1 ATOM 847 C CG . ARG A 1 107 ? 32.933 -28.374 -7.216 1.00 128.73 ? 107 ARG A CG 1 ATOM 848 C CD . ARG A 1 107 ? 33.499 -29.767 -7.452 1.00 138.77 ? 107 ARG A CD 1 ATOM 849 N NE . ARG A 1 107 ? 34.862 -29.696 -7.993 1.00 144.78 ? 107 ARG A NE 1 ATOM 850 C CZ . ARG A 1 107 ? 35.488 -30.678 -8.646 1.00 146.03 ? 107 ARG A CZ 1 ATOM 851 N NH1 . ARG A 1 107 ? 34.896 -31.852 -8.865 1.00 152.25 ? 107 ARG A NH1 1 ATOM 852 N NH2 . ARG A 1 107 ? 36.726 -30.484 -9.090 1.00 142.08 ? 107 ARG A NH2 1 ATOM 853 N N . ILE A 1 108 ? 29.074 -25.753 -6.148 1.00 99.77 ? 108 ILE A N 1 ATOM 854 C CA . ILE A 1 108 ? 27.835 -25.535 -5.400 1.00 101.03 ? 108 ILE A CA 1 ATOM 855 C C . ILE A 1 108 ? 27.029 -24.382 -5.982 1.00 98.58 ? 108 ILE A C 1 ATOM 856 O O . ILE A 1 108 ? 27.553 -23.282 -6.168 1.00 98.62 ? 108 ILE A O 1 ATOM 857 C CB . ILE A 1 108 ? 28.107 -25.241 -3.905 1.00 102.00 ? 108 ILE A CB 1 ATOM 858 C CG1 . ILE A 1 108 ? 28.686 -26.479 -3.219 1.00 105.64 ? 108 ILE A CG1 1 ATOM 859 C CG2 . ILE A 1 108 ? 26.823 -24.832 -3.191 1.00 101.43 ? 108 ILE A CG2 1 ATOM 860 C CD1 . ILE A 1 108 ? 29.286 -26.212 -1.854 1.00 107.25 ? 108 ILE A CD1 1 ATOM 861 N N . ASN A 1 109 ? 25.745 -24.640 -6.227 1.00 96.73 ? 109 ASN A N 1 ATOM 862 C CA . ASN A 1 109 ? 24.833 -23.644 -6.766 1.00 97.50 ? 109 ASN A CA 1 ATOM 863 C C . ASN A 1 109 ? 23.831 -23.094 -5.757 1.00 100.78 ? 109 ASN A C 1 ATOM 864 O O . ASN A 1 109 ? 23.280 -22.011 -5.976 1.00 100.52 ? 109 ASN A O 1 ATOM 865 C CB . ASN A 1 109 ? 24.087 -24.231 -7.962 1.00 101.19 ? 109 ASN A CB 1 ATOM 866 C CG . ASN A 1 109 ? 24.971 -24.353 -9.178 1.00 103.70 ? 109 ASN A CG 1 ATOM 867 O OD1 . ASN A 1 109 ? 25.465 -23.347 -9.683 1.00 104.30 ? 109 ASN A OD1 1 ATOM 868 N ND2 . ASN A 1 109 ? 25.192 -25.583 -9.649 1.00 107.80 ? 109 ASN A ND2 1 ATOM 869 N N . HIS A 1 110 ? 23.584 -23.823 -4.664 1.00 102.82 ? 110 HIS A N 1 ATOM 870 C CA . HIS A 1 110 ? 22.597 -23.378 -3.674 1.00 102.30 ? 110 HIS A CA 1 ATOM 871 C C . HIS A 1 110 ? 22.863 -23.869 -2.248 1.00 102.05 ? 110 HIS A C 1 ATOM 872 O O . HIS A 1 110 ? 23.207 -25.035 -2.014 1.00 99.13 ? 110 HIS A O 1 ATOM 873 C CB . HIS A 1 110 ? 21.193 -23.790 -4.126 1.00 104.10 ? 110 HIS A CB 1 ATOM 874 C CG . HIS A 1 110 ? 20.083 -23.060 -3.432 1.00 105.99 ? 110 HIS A CG 1 ATOM 875 N ND1 . HIS A 1 110 ? 18.798 -23.556 -3.364 1.00 108.85 ? 110 HIS A ND1 1 ATOM 876 C CD2 . HIS A 1 110 ? 20.061 -21.869 -2.789 1.00 104.37 ? 110 HIS A CD2 1 ATOM 877 C CE1 . HIS A 1 110 ? 18.034 -22.703 -2.708 1.00 108.41 ? 110 HIS A CE1 1 ATOM 878 N NE2 . HIS A 1 110 ? 18.776 -21.672 -2.346 1.00 105.71 ? 110 HIS A NE2 1 ATOM 879 N N . PHE A 1 111 ? 22.713 -22.941 -1.307 1.00 101.03 ? 111 PHE A N 1 ATOM 880 C CA . PHE A 1 111 ? 22.735 -23.243 0.108 1.00 103.64 ? 111 PHE A CA 1 ATOM 881 C C . PHE A 1 111 ? 21.358 -22.972 0.689 1.00 106.64 ? 111 PHE A C 1 ATOM 882 O O . PHE A 1 111 ? 20.707 -22.012 0.293 1.00 108.40 ? 111 PHE A O 1 ATOM 883 C CB . PHE A 1 111 ? 23.716 -22.327 0.834 1.00 101.92 ? 111 PHE A CB 1 ATOM 884 C CG . PHE A 1 111 ? 25.161 -22.736 0.724 1.00 100.69 ? 111 PHE A CG 1 ATOM 885 C CD1 . PHE A 1 111 ? 25.556 -24.060 0.886 1.00 101.54 ? 111 PHE A CD1 1 ATOM 886 C CD2 . PHE A 1 111 ? 26.141 -21.774 0.523 1.00 97.35 ? 111 PHE A CD2 1 ATOM 887 C CE1 . PHE A 1 111 ? 26.896 -24.412 0.814 1.00 99.19 ? 111 PHE A CE1 1 ATOM 888 C CE2 . PHE A 1 111 ? 27.475 -22.126 0.448 1.00 95.17 ? 111 PHE A CE2 1 ATOM 889 C CZ . PHE A 1 111 ? 27.855 -23.447 0.593 1.00 94.07 ? 111 PHE A CZ 1 ATOM 890 N N . GLU A 1 112 ? 20.917 -23.808 1.625 1.00 109.18 ? 112 GLU A N 1 ATOM 891 C CA . GLU A 1 112 ? 19.807 -23.438 2.505 1.00 112.32 ? 112 GLU A CA 1 ATOM 892 C C . GLU A 1 112 ? 20.353 -23.346 3.926 1.00 107.89 ? 112 GLU A C 1 ATOM 893 O O . GLU A 1 112 ? 20.875 -24.323 4.467 1.00 102.43 ? 112 GLU A O 1 ATOM 894 C CB . GLU A 1 112 ? 18.638 -24.432 2.433 1.00 117.00 ? 112 GLU A CB 1 ATOM 895 C CG . GLU A 1 112 ? 17.349 -23.901 3.064 1.00 122.99 ? 112 GLU A CG 1 ATOM 896 C CD . GLU A 1 112 ? 16.346 -24.993 3.442 1.00 132.12 ? 112 GLU A CD 1 ATOM 897 O OE1 . GLU A 1 112 ? 16.048 -25.866 2.594 1.00 133.73 ? 112 GLU A OE1 1 ATOM 898 O OE2 . GLU A 1 112 ? 15.837 -24.971 4.590 1.00 134.15 ? 112 GLU A OE2 1 ATOM 899 N N . LYS A 1 113 ? 20.243 -22.161 4.517 1.00 104.82 ? 113 LYS A N 1 ATOM 900 C CA . LYS A 1 113 ? 20.698 -21.939 5.884 1.00 107.41 ? 113 LYS A CA 1 ATOM 901 C C . LYS A 1 113 ? 19.716 -22.509 6.900 1.00 108.23 ? 113 LYS A C 1 ATOM 902 O O . LYS A 1 113 ? 18.513 -22.290 6.784 1.00 110.15 ? 113 LYS A O 1 ATOM 903 C CB . LYS A 1 113 ? 20.885 -20.447 6.142 1.00 106.79 ? 113 LYS A CB 1 ATOM 904 C CG . LYS A 1 113 ? 21.424 -20.136 7.525 1.00 108.79 ? 113 LYS A CG 1 ATOM 905 C CD . LYS A 1 113 ? 22.421 -18.994 7.498 1.00 109.60 ? 113 LYS A CD 1 ATOM 906 C CE . LYS A 1 113 ? 21.805 -17.737 6.919 1.00 111.19 ? 113 LYS A CE 1 ATOM 907 N NZ . LYS A 1 113 ? 22.657 -16.547 7.182 1.00 112.17 ? 113 LYS A NZ 1 ATOM 908 N N . ILE A 1 114 ? 20.230 -23.236 7.891 1.00 107.04 ? 114 ILE A N 1 ATOM 909 C CA . ILE A 1 114 ? 19.392 -23.760 8.964 1.00 110.60 ? 114 ILE A CA 1 ATOM 910 C C . ILE A 1 114 ? 20.050 -23.651 10.340 1.00 113.96 ? 114 ILE A C 1 ATOM 911 O O . ILE A 1 114 ? 21.276 -23.669 10.470 1.00 112.73 ? 114 ILE A O 1 ATOM 912 C CB . ILE A 1 114 ? 18.973 -25.225 8.721 1.00 111.59 ? 114 ILE A CB 1 ATOM 913 C CG1 . ILE A 1 114 ? 20.186 -26.157 8.708 1.00 112.64 ? 114 ILE A CG1 1 ATOM 914 C CG2 . ILE A 1 114 ? 18.176 -25.348 7.426 1.00 110.35 ? 114 ILE A CG2 1 ATOM 915 C CD1 . ILE A 1 114 ? 19.878 -27.523 9.281 1.00 115.86 ? 114 ILE A CD1 1 ATOM 916 N N . GLN A 1 115 ? 19.204 -23.547 11.361 1.00 115.72 ? 115 GLN A N 1 ATOM 917 C CA . GLN A 1 115 ? 19.645 -23.386 12.734 1.00 115.02 ? 115 GLN A CA 1 ATOM 918 C C . GLN A 1 115 ? 19.950 -24.750 13.329 1.00 114.63 ? 115 GLN A C 1 ATOM 919 O O . GLN A 1 115 ? 19.074 -25.612 13.374 1.00 116.02 ? 115 GLN A O 1 ATOM 920 C CB . GLN A 1 115 ? 18.546 -22.703 13.546 1.00 118.63 ? 115 GLN A CB 1 ATOM 921 C CG . GLN A 1 115 ? 18.934 -22.366 14.977 1.00 120.60 ? 115 GLN A CG 1 ATOM 922 C CD . GLN A 1 115 ? 17.917 -21.470 15.649 1.00 121.07 ? 115 GLN A CD 1 ATOM 923 O OE1 . GLN A 1 115 ? 18.259 -20.429 16.204 1.00 120.47 ? 115 GLN A OE1 1 ATOM 924 N NE2 . GLN A 1 115 ? 16.656 -21.865 15.588 1.00 125.74 ? 115 GLN A NE2 1 ATOM 925 N N . ILE A 1 116 ? 21.183 -24.949 13.783 1.00 112.52 ? 116 ILE A N 1 ATOM 926 C CA . ILE A 1 116 ? 21.562 -26.225 14.396 1.00 114.98 ? 116 ILE A CA 1 ATOM 927 C C . ILE A 1 116 ? 21.660 -26.131 15.925 1.00 117.90 ? 116 ILE A C 1 ATOM 928 O O . ILE A 1 116 ? 21.284 -27.072 16.627 1.00 121.41 ? 116 ILE A O 1 ATOM 929 C CB . ILE A 1 116 ? 22.852 -26.825 13.781 1.00 111.91 ? 116 ILE A CB 1 ATOM 930 C CG1 . ILE A 1 116 ? 24.010 -25.826 13.796 1.00 109.01 ? 116 ILE A CG1 1 ATOM 931 C CG2 . ILE A 1 116 ? 22.593 -27.275 12.351 1.00 112.10 ? 116 ILE A CG2 1 ATOM 932 C CD1 . ILE A 1 116 ? 25.348 -26.466 13.501 1.00 107.83 ? 116 ILE A CD1 1 ATOM 933 N N . ILE A 1 117 ? 22.145 -25.004 16.442 1.00 117.27 ? 117 ILE A N 1 ATOM 934 C CA . ILE A 1 117 ? 22.209 -24.792 17.888 1.00 120.72 ? 117 ILE A CA 1 ATOM 935 C C . ILE A 1 117 ? 21.603 -23.434 18.244 1.00 120.17 ? 117 ILE A C 1 ATOM 936 O O . ILE A 1 117 ? 22.285 -22.412 18.149 1.00 119.32 ? 117 ILE A O 1 ATOM 937 C CB . ILE A 1 117 ? 23.654 -24.884 18.416 1.00 122.13 ? 117 ILE A CB 1 ATOM 938 C CG1 . ILE A 1 117 ? 24.286 -26.215 17.991 1.00 123.31 ? 117 ILE A CG1 1 ATOM 939 C CG2 . ILE A 1 117 ? 23.674 -24.739 19.934 1.00 124.30 ? 117 ILE A CG2 1 ATOM 940 C CD1 . ILE A 1 117 ? 25.735 -26.379 18.400 1.00 124.22 ? 117 ILE A CD1 1 ATOM 941 N N . PRO A 1 118 ? 20.319 -23.422 18.664 1.00 123.26 ? 118 PRO A N 1 ATOM 942 C CA . PRO A 1 118 ? 19.617 -22.174 18.979 1.00 123.45 ? 118 PRO A CA 1 ATOM 943 C C . PRO A 1 118 ? 20.382 -21.296 19.957 1.00 123.15 ? 118 PRO A C 1 ATOM 944 O O . PRO A 1 118 ? 20.966 -21.802 20.916 1.00 125.53 ? 118 PRO A O 1 ATOM 945 C CB . PRO A 1 118 ? 18.309 -22.652 19.620 1.00 125.93 ? 118 PRO A CB 1 ATOM 946 C CG . PRO A 1 118 ? 18.091 -24.018 19.078 1.00 126.18 ? 118 PRO A CG 1 ATOM 947 C CD . PRO A 1 118 ? 19.457 -24.603 18.873 1.00 125.40 ? 118 PRO A CD 1 ATOM 948 N N . LYS A 1 119 ? 20.376 -19.991 19.710 1.00 123.03 ? 119 LYS A N 1 ATOM 949 C CA . LYS A 1 119 ? 21.062 -19.049 20.588 1.00 124.69 ? 119 LYS A CA 1 ATOM 950 C C . LYS A 1 119 ? 20.471 -19.121 21.999 1.00 127.90 ? 119 LYS A C 1 ATOM 951 O O . LYS A 1 119 ? 21.200 -19.120 22.989 1.00 128.49 ? 119 LYS A O 1 ATOM 952 C CB . LYS A 1 119 ? 20.956 -17.624 20.041 1.00 123.99 ? 119 LYS A CB 1 ATOM 953 C CG . LYS A 1 119 ? 22.170 -16.771 20.352 1.00 124.78 ? 119 LYS A CG 1 ATOM 954 C CD . LYS A 1 119 ? 21.937 -15.311 20.000 1.00 127.05 ? 119 LYS A CD 1 ATOM 955 C CE . LYS A 1 119 ? 23.247 -14.603 19.691 1.00 127.94 ? 119 LYS A CE 1 ATOM 956 N NZ . LYS A 1 119 ? 23.172 -13.135 19.926 1.00 128.17 ? 119 LYS A NZ 1 ATOM 957 N N . SER A 1 120 ? 19.143 -19.209 22.070 1.00 130.10 ? 120 SER A N 1 ATOM 958 C CA . SER A 1 120 ? 18.418 -19.310 23.335 1.00 129.58 ? 120 SER A CA 1 ATOM 959 C C . SER A 1 120 ? 18.826 -20.517 24.183 1.00 131.89 ? 120 SER A C 1 ATOM 960 O O . SER A 1 120 ? 18.718 -20.478 25.405 1.00 137.00 ? 120 SER A O 1 ATOM 961 C CB . SER A 1 120 ? 16.912 -19.378 23.068 1.00 130.08 ? 120 SER A CB 1 ATOM 962 O OG . SER A 1 120 ? 16.578 -20.541 22.328 1.00 131.66 ? 120 SER A OG 1 ATOM 963 N N . SER A 1 121 ? 19.308 -21.578 23.543 1.00 130.61 ? 121 SER A N 1 ATOM 964 C CA . SER A 1 121 ? 19.605 -22.827 24.242 1.00 130.90 ? 121 SER A CA 1 ATOM 965 C C . SER A 1 121 ? 20.914 -22.834 25.052 1.00 128.88 ? 121 SER A C 1 ATOM 966 O O . SER A 1 121 ? 21.332 -23.892 25.511 1.00 130.86 ? 121 SER A O 1 ATOM 967 C CB . SER A 1 121 ? 19.625 -23.985 23.240 1.00 131.92 ? 121 SER A CB 1 ATOM 968 O OG . SER A 1 121 ? 20.794 -23.941 22.439 1.00 130.53 ? 121 SER A OG 1 ATOM 969 N N . TRP A 1 122 ? 21.564 -21.685 25.227 1.00 125.78 ? 122 TRP A N 1 ATOM 970 C CA . TRP A 1 122 ? 22.777 -21.619 26.047 1.00 124.74 ? 122 TRP A CA 1 ATOM 971 C C . TRP A 1 122 ? 22.439 -21.097 27.435 1.00 126.07 ? 122 TRP A C 1 ATOM 972 O O . TRP A 1 122 ? 22.544 -19.900 27.705 1.00 125.90 ? 122 TRP A O 1 ATOM 973 C CB . TRP A 1 122 ? 23.836 -20.742 25.382 1.00 122.34 ? 122 TRP A CB 1 ATOM 974 C CG . TRP A 1 122 ? 24.339 -21.302 24.085 1.00 121.36 ? 122 TRP A CG 1 ATOM 975 C CD1 . TRP A 1 122 ? 24.015 -20.877 22.832 1.00 119.93 ? 122 TRP A CD1 1 ATOM 976 C CD2 . TRP A 1 122 ? 25.252 -22.395 23.913 1.00 120.83 ? 122 TRP A CD2 1 ATOM 977 N NE1 . TRP A 1 122 ? 24.672 -21.630 21.890 1.00 121.06 ? 122 TRP A NE1 1 ATOM 978 C CE2 . TRP A 1 122 ? 25.440 -22.568 22.526 1.00 119.51 ? 122 TRP A CE2 1 ATOM 979 C CE3 . TRP A 1 122 ? 25.932 -23.241 24.795 1.00 122.04 ? 122 TRP A CE3 1 ATOM 980 C CZ2 . TRP A 1 122 ? 26.278 -23.553 21.998 1.00 118.44 ? 122 TRP A CZ2 1 ATOM 981 C CZ3 . TRP A 1 122 ? 26.765 -24.223 24.268 1.00 122.52 ? 122 TRP A CZ3 1 ATOM 982 C CH2 . TRP A 1 122 ? 26.930 -24.368 22.882 1.00 119.93 ? 122 TRP A CH2 1 ATOM 983 N N . SER A 1 123 ? 22.040 -22.012 28.314 1.00 129.08 ? 123 SER A N 1 ATOM 984 C CA . SER A 1 123 ? 21.508 -21.657 29.635 1.00 131.70 ? 123 SER A CA 1 ATOM 985 C C . SER A 1 123 ? 22.560 -21.581 30.750 1.00 131.77 ? 123 SER A C 1 ATOM 986 O O . SER A 1 123 ? 22.322 -20.939 31.771 1.00 132.21 ? 123 SER A O 1 ATOM 987 C CB . SER A 1 123 ? 20.391 -22.631 30.032 1.00 133.11 ? 123 SER A CB 1 ATOM 988 O OG . SER A 1 123 ? 20.695 -23.952 29.622 1.00 133.85 ? 123 SER A OG 1 ATOM 989 N N . SER A 1 124 ? 23.708 -22.231 30.561 1.00 131.51 ? 124 SER A N 1 ATOM 990 C CA . SER A 1 124 ? 24.806 -22.181 31.535 1.00 129.50 ? 124 SER A CA 1 ATOM 991 C C . SER A 1 124 ? 25.914 -21.203 31.131 1.00 128.53 ? 124 SER A C 1 ATOM 992 O O . SER A 1 124 ? 26.916 -21.074 31.837 1.00 128.85 ? 124 SER A O 1 ATOM 993 C CB . SER A 1 124 ? 25.412 -23.573 31.716 1.00 130.28 ? 124 SER A CB 1 ATOM 994 O OG . SER A 1 124 ? 24.413 -24.524 32.027 1.00 132.30 ? 124 SER A OG 1 ATOM 995 N N . HIS A 1 125 ? 25.742 -20.531 29.993 1.00 127.36 ? 125 HIS A N 1 ATOM 996 C CA . HIS A 1 125 ? 26.733 -19.582 29.486 1.00 124.78 ? 125 HIS A CA 1 ATOM 997 C C . HIS A 1 125 ? 26.039 -18.336 28.955 1.00 126.79 ? 125 HIS A C 1 ATOM 998 O O . HIS A 1 125 ? 24.870 -18.383 28.564 1.00 127.07 ? 125 HIS A O 1 ATOM 999 C CB . HIS A 1 125 ? 27.554 -20.212 28.359 1.00 121.74 ? 125 HIS A CB 1 ATOM 1000 C CG . HIS A 1 125 ? 28.324 -21.429 28.769 1.00 120.36 ? 125 HIS A CG 1 ATOM 1001 N ND1 . HIS A 1 125 ? 27.747 -22.676 28.866 1.00 120.85 ? 125 HIS A ND1 1 ATOM 1002 C CD2 . HIS A 1 125 ? 29.631 -21.592 29.087 1.00 119.42 ? 125 HIS A CD2 1 ATOM 1003 C CE1 . HIS A 1 125 ? 28.662 -23.554 29.237 1.00 122.88 ? 125 HIS A CE1 1 ATOM 1004 N NE2 . HIS A 1 125 ? 29.814 -22.923 29.375 1.00 121.85 ? 125 HIS A NE2 1 ATOM 1005 N N . GLU A 1 126 ? 26.770 -17.225 28.932 1.00 128.45 ? 126 GLU A N 1 ATOM 1006 C CA . GLU A 1 126 ? 26.237 -15.971 28.417 1.00 130.43 ? 126 GLU A CA 1 ATOM 1007 C C . GLU A 1 126 ? 26.488 -15.869 26.913 1.00 129.21 ? 126 GLU A C 1 ATOM 1008 O O . GLU A 1 126 ? 27.633 -15.942 26.459 1.00 129.20 ? 126 GLU A O 1 ATOM 1009 C CB . GLU A 1 126 ? 26.863 -14.787 29.149 1.00 134.37 ? 126 GLU A CB 1 ATOM 1010 C CG . GLU A 1 126 ? 26.212 -13.447 28.841 1.00 137.10 ? 126 GLU A CG 1 ATOM 1011 C CD . GLU A 1 126 ? 24.710 -13.452 29.071 1.00 140.70 ? 126 GLU A CD 1 ATOM 1012 O OE1 . GLU A 1 126 ? 24.275 -13.742 30.211 1.00 136.91 ? 126 GLU A OE1 1 ATOM 1013 O OE2 . GLU A 1 126 ? 23.967 -13.165 28.104 1.00 143.75 ? 126 GLU A OE2 1 ATOM 1014 N N . ALA A 1 127 ? 25.411 -15.687 26.153 1.00 127.74 ? 127 ALA A N 1 ATOM 1015 C CA . ALA A 1 127 ? 25.459 -15.768 24.696 1.00 124.73 ? 127 ALA A CA 1 ATOM 1016 C C . ALA A 1 127 ? 24.965 -14.501 23.986 1.00 123.65 ? 127 ALA A C 1 ATOM 1017 O O . ALA A 1 127 ? 24.655 -14.546 22.798 1.00 123.86 ? 127 ALA A O 1 ATOM 1018 C CB . ALA A 1 127 ? 24.652 -16.974 24.234 1.00 125.96 ? 127 ALA A CB 1 ATOM 1019 N N . SER A 1 128 ? 24.905 -13.378 24.699 1.00 123.85 ? 128 SER A N 1 ATOM 1020 C CA . SER A 1 128 ? 24.462 -12.105 24.110 1.00 120.89 ? 128 SER A CA 1 ATOM 1021 C C . SER A 1 128 ? 25.427 -10.937 24.312 1.00 119.69 ? 128 SER A C 1 ATOM 1022 O O . SER A 1 128 ? 25.169 -9.844 23.814 1.00 117.97 ? 128 SER A O 1 ATOM 1023 C CB . SER A 1 128 ? 23.099 -11.729 24.671 1.00 123.25 ? 128 SER A CB 1 ATOM 1024 O OG . SER A 1 128 ? 22.187 -12.789 24.469 1.00 128.18 ? 128 SER A OG 1 ATOM 1025 N N . LEU A 1 129 ? 26.522 -11.163 25.039 1.00 121.17 ? 129 LEU A N 1 ATOM 1026 C CA . LEU A 1 129 ? 27.558 -10.146 25.236 1.00 121.21 ? 129 LEU A CA 1 ATOM 1027 C C . LEU A 1 129 ? 28.777 -10.432 24.370 1.00 119.45 ? 129 LEU A C 1 ATOM 1028 O O . LEU A 1 129 ? 29.787 -9.731 24.462 1.00 121.46 ? 129 LEU A O 1 ATOM 1029 C CB . LEU A 1 129 ? 27.987 -10.088 26.701 1.00 125.48 ? 129 LEU A CB 1 ATOM 1030 C CG . LEU A 1 129 ? 26.881 -10.031 27.761 1.00 128.67 ? 129 LEU A CG 1 ATOM 1031 C CD1 . LEU A 1 129 ? 27.503 -9.865 29.143 1.00 127.60 ? 129 LEU A CD1 1 ATOM 1032 C CD2 . LEU A 1 129 ? 25.875 -8.922 27.470 1.00 127.79 ? 129 LEU A CD2 1 ATOM 1033 N N . GLY A 1 130 ? 28.682 -11.462 23.532 1.00 116.77 ? 130 GLY A N 1 ATOM 1034 C CA . GLY A 1 130 ? 29.742 -11.792 22.594 1.00 111.77 ? 130 GLY A CA 1 ATOM 1035 C C . GLY A 1 130 ? 29.701 -10.863 21.399 1.00 108.36 ? 130 GLY A C 1 ATOM 1036 O O . GLY A 1 130 ? 29.341 -11.279 20.290 1.00 105.03 ? 130 GLY A O 1 ATOM 1037 N N . VAL A 1 131 ? 30.073 -9.604 21.633 1.00 103.44 ? 131 VAL A N 1 ATOM 1038 C CA . VAL A 1 131 ? 29.971 -8.555 20.622 1.00 101.32 ? 131 VAL A CA 1 ATOM 1039 C C . VAL A 1 131 ? 31.184 -7.632 20.669 1.00 98.11 ? 131 VAL A C 1 ATOM 1040 O O . VAL A 1 131 ? 31.730 -7.384 21.733 1.00 99.13 ? 131 VAL A O 1 ATOM 1041 C CB . VAL A 1 131 ? 28.672 -7.732 20.784 1.00 102.29 ? 131 VAL A CB 1 ATOM 1042 C CG1 . VAL A 1 131 ? 27.455 -8.584 20.440 1.00 102.30 ? 131 VAL A CG1 1 ATOM 1043 C CG2 . VAL A 1 131 ? 28.544 -7.167 22.192 1.00 102.04 ? 131 VAL A CG2 1 ATOM 1044 N N . SER A 1 132 ? 31.589 -7.131 19.504 1.00 98.11 ? 132 SER A N 1 ATOM 1045 C CA . SER A 1 132 ? 32.799 -6.325 19.358 1.00 96.52 ? 132 SER A CA 1 ATOM 1046 C C . SER A 1 132 ? 32.544 -5.057 18.548 1.00 96.04 ? 132 SER A C 1 ATOM 1047 O O . SER A 1 132 ? 31.737 -5.055 17.617 1.00 97.11 ? 132 SER A O 1 ATOM 1048 C CB . SER A 1 132 ? 33.887 -7.150 18.664 1.00 97.32 ? 132 SER A CB 1 ATOM 1049 O OG . SER A 1 132 ? 35.058 -6.379 18.426 1.00 97.19 ? 132 SER A OG 1 ATOM 1050 N N . SER A 1 133 ? 33.259 -3.989 18.894 1.00 96.11 ? 133 SER A N 1 ATOM 1051 C CA . SER A 1 133 ? 33.188 -2.730 18.155 1.00 96.88 ? 133 SER A CA 1 ATOM 1052 C C . SER A 1 133 ? 33.879 -2.837 16.802 1.00 95.52 ? 133 SER A C 1 ATOM 1053 O O . SER A 1 133 ? 33.695 -1.977 15.946 1.00 95.36 ? 133 SER A O 1 ATOM 1054 C CB . SER A 1 133 ? 33.829 -1.607 18.959 1.00 99.61 ? 133 SER A CB 1 ATOM 1055 O OG . SER A 1 133 ? 35.189 -1.900 19.218 1.00 102.70 ? 133 SER A OG 1 ATOM 1056 N N . ALA A 1 134 ? 34.684 -3.883 16.623 1.00 96.44 ? 134 ALA A N 1 ATOM 1057 C CA . ALA A 1 134 ? 35.284 -4.198 15.327 1.00 95.36 ? 134 ALA A CA 1 ATOM 1058 C C . ALA A 1 134 ? 34.253 -4.720 14.322 1.00 97.84 ? 134 ALA A C 1 ATOM 1059 O O . ALA A 1 134 ? 34.479 -4.636 13.113 1.00 96.08 ? 134 ALA A O 1 ATOM 1060 C CB . ALA A 1 134 ? 36.401 -5.215 15.501 1.00 95.83 ? 134 ALA A CB 1 ATOM 1061 N N . CYS A 1 135 ? 33.133 -5.252 14.823 1.00 100.64 ? 135 CYS A N 1 ATOM 1062 C CA . CYS A 1 135 ? 32.025 -5.719 13.985 1.00 102.01 ? 135 CYS A CA 1 ATOM 1063 C C . CYS A 1 135 ? 30.744 -4.925 14.247 1.00 99.56 ? 135 CYS A C 1 ATOM 1064 O O . CYS A 1 135 ? 29.793 -5.457 14.815 1.00 100.16 ? 135 CYS A O 1 ATOM 1065 C CB . CYS A 1 135 ? 31.768 -7.201 14.244 1.00 107.04 ? 135 CYS A CB 1 ATOM 1066 S SG . CYS A 1 135 ? 33.215 -8.240 13.966 1.00 119.85 ? 135 CYS A SG 1 ATOM 1067 N N . PRO A 1 136 ? 30.709 -3.650 13.821 1.00 96.63 ? 136 PRO A N 1 ATOM 1068 C CA . PRO A 1 136 ? 29.571 -2.799 14.134 1.00 96.79 ? 136 PRO A CA 1 ATOM 1069 C C . PRO A 1 136 ? 28.389 -3.007 13.194 1.00 97.24 ? 136 PRO A C 1 ATOM 1070 O O . PRO A 1 136 ? 28.576 -3.341 12.023 1.00 91.26 ? 136 PRO A O 1 ATOM 1071 C CB . PRO A 1 136 ? 30.138 -1.396 13.939 1.00 97.76 ? 136 PRO A CB 1 ATOM 1072 C CG . PRO A 1 136 ? 31.105 -1.568 12.816 1.00 94.35 ? 136 PRO A CG 1 ATOM 1073 C CD . PRO A 1 136 ? 31.712 -2.929 13.013 1.00 94.07 ? 136 PRO A CD 1 ATOM 1074 N N . TYR A 1 137 ? 27.186 -2.794 13.722 1.00 100.30 ? 137 TYR A N 1 ATOM 1075 C CA . TYR A 1 137 ? 25.956 -2.852 12.943 1.00 99.33 ? 137 TYR A CA 1 ATOM 1076 C C . TYR A 1 137 ? 25.008 -1.761 13.406 1.00 99.08 ? 137 TYR A C 1 ATOM 1077 O O . TYR A 1 137 ? 24.552 -1.777 14.548 1.00 100.56 ? 137 TYR A O 1 ATOM 1078 C CB . TYR A 1 137 ? 25.287 -4.204 13.116 1.00 102.19 ? 137 TYR A CB 1 ATOM 1079 C CG . TYR A 1 137 ? 23.961 -4.313 12.405 1.00 106.31 ? 137 TYR A CG 1 ATOM 1080 C CD1 . TYR A 1 137 ? 23.896 -4.327 11.009 1.00 107.95 ? 137 TYR A CD1 1 ATOM 1081 C CD2 . TYR A 1 137 ? 22.770 -4.406 13.124 1.00 107.62 ? 137 TYR A CD2 1 ATOM 1082 C CE1 . TYR A 1 137 ? 22.679 -4.432 10.352 1.00 110.41 ? 137 TYR A CE1 1 ATOM 1083 C CE2 . TYR A 1 137 ? 21.551 -4.515 12.477 1.00 109.72 ? 137 TYR A CE2 1 ATOM 1084 C CZ . TYR A 1 137 ? 21.507 -4.527 11.096 1.00 111.80 ? 137 TYR A CZ 1 ATOM 1085 O OH . TYR A 1 137 ? 20.292 -4.639 10.462 1.00 113.06 ? 137 TYR A OH 1 ATOM 1086 N N . GLN A 1 138 ? 24.711 -0.822 12.513 1.00 99.64 ? 138 GLN A N 1 ATOM 1087 C CA . GLN A 1 138 ? 23.899 0.344 12.842 1.00 104.31 ? 138 GLN A CA 1 ATOM 1088 C C . GLN A 1 138 ? 24.434 1.083 14.071 1.00 104.47 ? 138 GLN A C 1 ATOM 1089 O O . GLN A 1 138 ? 23.672 1.456 14.963 1.00 106.25 ? 138 GLN A O 1 ATOM 1090 C CB . GLN A 1 138 ? 22.437 -0.055 13.066 1.00 109.23 ? 138 GLN A CB 1 ATOM 1091 C CG . GLN A 1 138 ? 21.767 -0.686 11.858 1.00 110.39 ? 138 GLN A CG 1 ATOM 1092 C CD . GLN A 1 138 ? 20.343 -1.122 12.149 1.00 113.45 ? 138 GLN A CD 1 ATOM 1093 O OE1 . GLN A 1 138 ? 19.822 -0.907 13.247 1.00 114.84 ? 138 GLN A OE1 1 ATOM 1094 N NE2 . GLN A 1 138 ? 19.707 -1.745 11.167 1.00 114.29 ? 138 GLN A NE2 1 ATOM 1095 N N . GLY A 1 139 ? 25.750 1.274 14.114 1.00 104.42 ? 139 GLY A N 1 ATOM 1096 C CA . GLY A 1 139 ? 26.387 2.064 15.161 1.00 105.97 ? 139 GLY A CA 1 ATOM 1097 C C . GLY A 1 139 ? 26.741 1.321 16.436 1.00 107.96 ? 139 GLY A C 1 ATOM 1098 O O . GLY A 1 139 ? 27.581 1.794 17.205 1.00 110.77 ? 139 GLY A O 1 ATOM 1099 N N . LYS A 1 140 ? 26.109 0.171 16.669 1.00 107.80 ? 140 LYS A N 1 ATOM 1100 C CA . LYS A 1 140 ? 26.309 -0.596 17.898 1.00 108.27 ? 140 LYS A CA 1 ATOM 1101 C C . LYS A 1 140 ? 27.302 -1.708 17.633 1.00 106.57 ? 140 LYS A C 1 ATOM 1102 O O . LYS A 1 140 ? 27.542 -2.059 16.479 1.00 106.59 ? 140 LYS A O 1 ATOM 1103 C CB . LYS A 1 140 ? 24.992 -1.207 18.379 1.00 112.00 ? 140 LYS A CB 1 ATOM 1104 C CG . LYS A 1 140 ? 23.816 -0.248 18.353 1.00 118.06 ? 140 LYS A CG 1 ATOM 1105 C CD . LYS A 1 140 ? 22.543 -0.907 18.854 1.00 124.45 ? 140 LYS A CD 1 ATOM 1106 C CE . LYS A 1 140 ? 21.321 -0.079 18.487 1.00 128.90 ? 140 LYS A CE 1 ATOM 1107 N NZ . LYS A 1 140 ? 20.123 -0.432 19.301 1.00 131.79 ? 140 LYS A NZ 1 ATOM 1108 N N . SER A 1 141 ? 27.876 -2.258 18.701 1.00 106.04 ? 141 SER A N 1 ATOM 1109 C CA . SER A 1 141 ? 28.756 -3.422 18.585 1.00 103.47 ? 141 SER A CA 1 ATOM 1110 C C . SER A 1 141 ? 27.931 -4.667 18.266 1.00 103.67 ? 141 SER A C 1 ATOM 1111 O O . SER A 1 141 ? 26.837 -4.850 18.806 1.00 106.73 ? 141 SER A O 1 ATOM 1112 C CB . SER A 1 141 ? 29.549 -3.641 19.871 1.00 101.22 ? 141 SER A CB 1 ATOM 1113 O OG . SER A 1 141 ? 30.522 -2.630 20.031 1.00 102.27 ? 141 SER A OG 1 ATOM 1114 N N . SER A 1 142 ? 28.459 -5.506 17.379 1.00 98.20 ? 142 SER A N 1 ATOM 1115 C CA . SER A 1 142 ? 27.798 -6.740 16.977 1.00 95.99 ? 142 SER A CA 1 ATOM 1116 C C . SER A 1 142 ? 28.858 -7.808 16.715 1.00 92.73 ? 142 SER A C 1 ATOM 1117 O O . SER A 1 142 ? 29.985 -7.692 17.191 1.00 88.45 ? 142 SER A O 1 ATOM 1118 C CB . SER A 1 142 ? 26.927 -6.488 15.738 1.00 98.55 ? 142 SER A CB 1 ATOM 1119 O OG . SER A 1 142 ? 26.360 -7.686 15.235 1.00 99.87 ? 142 SER A OG 1 ATOM 1120 N N . PHE A 1 143 ? 28.497 -8.846 15.968 1.00 93.12 ? 143 PHE A N 1 ATOM 1121 C CA . PHE A 1 143 ? 29.402 -9.962 15.702 1.00 92.42 ? 143 PHE A CA 1 ATOM 1122 C C . PHE A 1 143 ? 28.888 -10.792 14.525 1.00 91.68 ? 143 PHE A C 1 ATOM 1123 O O . PHE A 1 143 ? 27.754 -10.616 14.088 1.00 91.55 ? 143 PHE A O 1 ATOM 1124 C CB . PHE A 1 143 ? 29.530 -10.832 16.963 1.00 92.90 ? 143 PHE A CB 1 ATOM 1125 C CG . PHE A 1 143 ? 30.708 -11.771 16.952 1.00 92.88 ? 143 PHE A CG 1 ATOM 1126 C CD1 . PHE A 1 143 ? 32.004 -11.285 16.820 1.00 92.57 ? 143 PHE A CD1 1 ATOM 1127 C CD2 . PHE A 1 143 ? 30.524 -13.139 17.095 1.00 92.93 ? 143 PHE A CD2 1 ATOM 1128 C CE1 . PHE A 1 143 ? 33.089 -12.146 16.816 1.00 92.49 ? 143 PHE A CE1 1 ATOM 1129 C CE2 . PHE A 1 143 ? 31.606 -14.003 17.093 1.00 93.47 ? 143 PHE A CE2 1 ATOM 1130 C CZ . PHE A 1 143 ? 32.892 -13.506 16.955 1.00 92.94 ? 143 PHE A CZ 1 ATOM 1131 N N . PHE A 1 144 ? 29.739 -11.672 14.004 1.00 93.78 ? 144 PHE A N 1 ATOM 1132 C CA . PHE A 1 144 ? 29.345 -12.643 12.982 1.00 92.56 ? 144 PHE A CA 1 ATOM 1133 C C . PHE A 1 144 ? 28.027 -13.313 13.372 1.00 92.99 ? 144 PHE A C 1 ATOM 1134 O O . PHE A 1 144 ? 27.915 -13.904 14.439 1.00 97.18 ? 144 PHE A O 1 ATOM 1135 C CB . PHE A 1 144 ? 30.412 -13.728 12.824 1.00 94.21 ? 144 PHE A CB 1 ATOM 1136 C CG . PHE A 1 144 ? 31.776 -13.210 12.450 1.00 95.69 ? 144 PHE A CG 1 ATOM 1137 C CD1 . PHE A 1 144 ? 32.031 -12.737 11.172 1.00 97.18 ? 144 PHE A CD1 1 ATOM 1138 C CD2 . PHE A 1 144 ? 32.812 -13.219 13.374 1.00 96.61 ? 144 PHE A CD2 1 ATOM 1139 C CE1 . PHE A 1 144 ? 33.291 -12.274 10.823 1.00 96.29 ? 144 PHE A CE1 1 ATOM 1140 C CE2 . PHE A 1 144 ? 34.072 -12.756 13.033 1.00 97.09 ? 144 PHE A CE2 1 ATOM 1141 C CZ . PHE A 1 144 ? 34.312 -12.282 11.754 1.00 97.05 ? 144 PHE A CZ 1 ATOM 1142 N N . ARG A 1 145 ? 27.042 -13.224 12.492 1.00 91.64 ? 145 ARG A N 1 ATOM 1143 C CA . ARG A 1 145 ? 25.680 -13.634 12.794 1.00 92.17 ? 145 ARG A CA 1 ATOM 1144 C C . ARG A 1 145 ? 25.438 -15.138 12.844 1.00 93.88 ? 145 ARG A C 1 ATOM 1145 O O . ARG A 1 145 ? 24.449 -15.585 13.432 1.00 99.93 ? 145 ARG A O 1 ATOM 1146 C CB . ARG A 1 145 ? 24.733 -13.038 11.762 1.00 91.90 ? 145 ARG A CB 1 ATOM 1147 C CG . ARG A 1 145 ? 24.753 -11.525 11.724 1.00 91.85 ? 145 ARG A CG 1 ATOM 1148 C CD . ARG A 1 145 ? 23.471 -11.023 11.094 1.00 96.02 ? 145 ARG A CD 1 ATOM 1149 N NE . ARG A 1 145 ? 23.416 -9.571 11.012 1.00 96.90 ? 145 ARG A NE 1 ATOM 1150 C CZ . ARG A 1 145 ? 23.241 -8.766 12.052 1.00 100.16 ? 145 ARG A CZ 1 ATOM 1151 N NH1 . ARG A 1 145 ? 23.130 -9.249 13.288 1.00 101.79 ? 145 ARG A NH1 1 ATOM 1152 N NH2 . ARG A 1 145 ? 23.195 -7.459 11.857 1.00 104.69 ? 145 ARG A NH2 1 ATOM 1153 N N . ASN A 1 146 ? 26.312 -15.916 12.220 1.00 93.53 ? 146 ASN A N 1 ATOM 1154 C CA . ASN A 1 146 ? 26.111 -17.364 12.128 1.00 96.09 ? 146 ASN A CA 1 ATOM 1155 C C . ASN A 1 146 ? 26.822 -18.134 13.233 1.00 95.60 ? 146 ASN A C 1 ATOM 1156 O O . ASN A 1 146 ? 26.659 -19.348 13.353 1.00 95.70 ? 146 ASN A O 1 ATOM 1157 C CB . ASN A 1 146 ? 26.544 -17.880 10.751 1.00 93.85 ? 146 ASN A CB 1 ATOM 1158 C CG . ASN A 1 146 ? 25.761 -17.239 9.623 1.00 96.62 ? 146 ASN A CG 1 ATOM 1159 O OD1 . ASN A 1 146 ? 24.594 -16.883 9.791 1.00 103.35 ? 146 ASN A OD1 1 ATOM 1160 N ND2 . ASN A 1 146 ? 26.396 -17.089 8.467 1.00 96.18 ? 146 ASN A ND2 1 ATOM 1161 N N . VAL A 1 147 ? 27.603 -17.427 14.041 1.00 94.65 ? 147 VAL A N 1 ATOM 1162 C CA . VAL A 1 147 ? 28.268 -18.045 15.176 1.00 97.05 ? 147 VAL A CA 1 ATOM 1163 C C . VAL A 1 147 ? 28.051 -17.238 16.443 1.00 98.08 ? 147 VAL A C 1 ATOM 1164 O O . VAL A 1 147 ? 27.695 -16.060 16.397 1.00 97.62 ? 147 VAL A O 1 ATOM 1165 C CB . VAL A 1 147 ? 29.773 -18.231 14.925 1.00 96.74 ? 147 VAL A CB 1 ATOM 1166 C CG1 . VAL A 1 147 ? 29.999 -19.334 13.904 1.00 98.14 ? 147 VAL A CG1 1 ATOM 1167 C CG2 . VAL A 1 147 ? 30.418 -16.928 14.467 1.00 94.69 ? 147 VAL A CG2 1 ATOM 1168 N N . VAL A 1 148 ? 28.279 -17.886 17.576 1.00 101.40 ? 148 VAL A N 1 ATOM 1169 C CA . VAL A 1 148 ? 27.987 -17.298 18.873 1.00 102.61 ? 148 VAL A CA 1 ATOM 1170 C C . VAL A 1 148 ? 29.269 -17.240 19.684 1.00 103.39 ? 148 VAL A C 1 ATOM 1171 O O . VAL A 1 148 ? 29.941 -18.258 19.861 1.00 108.10 ? 148 VAL A O 1 ATOM 1172 C CB . VAL A 1 148 ? 26.937 -18.134 19.629 1.00 104.27 ? 148 VAL A CB 1 ATOM 1173 C CG1 . VAL A 1 148 ? 26.457 -17.394 20.862 1.00 108.28 ? 148 VAL A CG1 1 ATOM 1174 C CG2 . VAL A 1 148 ? 25.757 -18.460 18.722 1.00 107.52 ? 148 VAL A CG2 1 ATOM 1175 N N . TRP A 1 149 ? 29.616 -16.049 20.163 1.00 101.34 ? 149 TRP A N 1 ATOM 1176 C CA . TRP A 1 149 ? 30.774 -15.894 21.031 1.00 102.39 ? 149 TRP A CA 1 ATOM 1177 C C . TRP A 1 149 ? 30.341 -16.071 22.491 1.00 104.39 ? 149 TRP A C 1 ATOM 1178 O O . TRP A 1 149 ? 29.902 -15.127 23.142 1.00 103.05 ? 149 TRP A O 1 ATOM 1179 C CB . TRP A 1 149 ? 31.432 -14.538 20.789 1.00 100.55 ? 149 TRP A CB 1 ATOM 1180 C CG . TRP A 1 149 ? 32.722 -14.333 21.509 1.00 99.97 ? 149 TRP A CG 1 ATOM 1181 C CD1 . TRP A 1 149 ? 33.396 -15.240 22.276 1.00 102.48 ? 149 TRP A CD1 1 ATOM 1182 C CD2 . TRP A 1 149 ? 33.527 -13.152 21.487 1.00 98.75 ? 149 TRP A CD2 1 ATOM 1183 N NE1 . TRP A 1 149 ? 34.559 -14.685 22.753 1.00 103.21 ? 149 TRP A NE1 1 ATOM 1184 C CE2 . TRP A 1 149 ? 34.665 -13.405 22.279 1.00 99.71 ? 149 TRP A CE2 1 ATOM 1185 C CE3 . TRP A 1 149 ? 33.394 -11.901 20.879 1.00 98.90 ? 149 TRP A CE3 1 ATOM 1186 C CZ2 . TRP A 1 149 ? 35.665 -12.455 22.478 1.00 99.39 ? 149 TRP A CZ2 1 ATOM 1187 C CZ3 . TRP A 1 149 ? 34.390 -10.956 21.078 1.00 99.22 ? 149 TRP A CZ3 1 ATOM 1188 C CH2 . TRP A 1 149 ? 35.510 -11.239 21.871 1.00 99.11 ? 149 TRP A CH2 1 ATOM 1189 N N . LEU A 1 150 ? 30.463 -17.300 22.987 1.00 107.72 ? 150 LEU A N 1 ATOM 1190 C CA . LEU A 1 150 ? 30.061 -17.639 24.346 1.00 110.80 ? 150 LEU A CA 1 ATOM 1191 C C . LEU A 1 150 ? 31.086 -17.125 25.333 1.00 111.19 ? 150 LEU A C 1 ATOM 1192 O O . LEU A 1 150 ? 32.283 -17.349 25.148 1.00 110.82 ? 150 LEU A O 1 ATOM 1193 C CB . LEU A 1 150 ? 29.950 -19.154 24.512 1.00 114.06 ? 150 LEU A CB 1 ATOM 1194 C CG . LEU A 1 150 ? 28.954 -19.869 23.599 1.00 116.47 ? 150 LEU A CG 1 ATOM 1195 C CD1 . LEU A 1 150 ? 29.084 -21.376 23.751 1.00 119.04 ? 150 LEU A CD1 1 ATOM 1196 C CD2 . LEU A 1 150 ? 27.533 -19.418 23.893 1.00 118.41 ? 150 LEU A CD2 1 ATOM 1197 N N . ILE A 1 151 ? 30.608 -16.444 26.375 1.00 112.02 ? 151 ILE A N 1 ATOM 1198 C CA . ILE A 1 151 ? 31.449 -16.034 27.501 1.00 112.63 ? 151 ILE A CA 1 ATOM 1199 C C . ILE A 1 151 ? 30.833 -16.477 28.830 1.00 112.70 ? 151 ILE A C 1 ATOM 1200 O O . ILE A 1 151 ? 29.664 -16.862 28.894 1.00 110.49 ? 151 ILE A O 1 ATOM 1201 C CB . ILE A 1 151 ? 31.683 -14.509 27.523 1.00 112.76 ? 151 ILE A CB 1 ATOM 1202 C CG1 . ILE A 1 151 ? 30.368 -13.757 27.728 1.00 115.76 ? 151 ILE A CG1 1 ATOM 1203 C CG2 . ILE A 1 151 ? 32.345 -14.052 26.232 1.00 109.46 ? 151 ILE A CG2 1 ATOM 1204 C CD1 . ILE A 1 151 ? 30.561 -12.306 28.109 1.00 116.89 ? 151 ILE A CD1 1 ATOM 1205 N N . LYS A 1 152 ? 31.631 -16.398 29.889 1.00 114.92 ? 152 LYS A N 1 ATOM 1206 C CA . LYS A 1 152 ? 31.240 -16.903 31.209 1.00 117.85 ? 152 LYS A CA 1 ATOM 1207 C C . LYS A 1 152 ? 29.927 -16.313 31.734 1.00 118.65 ? 152 LYS A C 1 ATOM 1208 O O . LYS A 1 152 ? 29.611 -15.152 31.478 1.00 115.79 ? 152 LYS A O 1 ATOM 1209 C CB . LYS A 1 152 ? 32.361 -16.645 32.223 1.00 117.83 ? 152 LYS A CB 1 ATOM 1210 C CG . LYS A 1 152 ? 32.582 -15.179 32.560 1.00 117.26 ? 152 LYS A CG 1 ATOM 1211 C CD . LYS A 1 152 ? 33.796 -14.995 33.454 1.00 118.35 ? 152 LYS A CD 1 ATOM 1212 C CE . LYS A 1 152 ? 33.741 -13.677 34.211 1.00 116.91 ? 152 LYS A CE 1 ATOM 1213 N NZ . LYS A 1 152 ? 35.026 -13.395 34.908 1.00 117.74 ? 152 LYS A NZ 1 ATOM 1214 N N . LYS A 1 153 ? 29.178 -17.127 32.478 1.00 123.55 ? 153 LYS A N 1 ATOM 1215 C CA . LYS A 1 153 ? 27.903 -16.713 33.072 1.00 126.60 ? 153 LYS A CA 1 ATOM 1216 C C . LYS A 1 153 ? 27.983 -16.781 34.594 1.00 127.01 ? 153 LYS A C 1 ATOM 1217 O O . LYS A 1 153 ? 28.151 -17.861 35.160 1.00 127.62 ? 153 LYS A O 1 ATOM 1218 C CB . LYS A 1 153 ? 26.772 -17.601 32.561 1.00 127.87 ? 153 LYS A CB 1 ATOM 1219 C CG . LYS A 1 153 ? 25.398 -17.253 33.108 1.00 129.16 ? 153 LYS A CG 1 ATOM 1220 C CD . LYS A 1 153 ? 24.300 -17.646 32.126 1.00 131.00 ? 153 LYS A CD 1 ATOM 1221 C CE . LYS A 1 153 ? 23.005 -18.024 32.830 1.00 133.75 ? 153 LYS A CE 1 ATOM 1222 N NZ . LYS A 1 153 ? 22.471 -16.944 33.704 1.00 135.15 ? 153 LYS A NZ 1 ATOM 1223 N N . ASN A 1 154 ? 27.859 -15.620 35.236 1.00 125.55 ? 154 ASN A N 1 ATOM 1224 C CA . ASN A 1 154 ? 28.039 -15.478 36.683 1.00 128.47 ? 154 ASN A CA 1 ATOM 1225 C C . ASN A 1 154 ? 29.397 -16.025 37.145 1.00 129.53 ? 154 ASN A C 1 ATOM 1226 O O . ASN A 1 154 ? 29.484 -16.769 38.123 1.00 129.57 ? 154 ASN A O 1 ATOM 1227 C CB . ASN A 1 154 ? 26.876 -16.128 37.454 1.00 129.70 ? 154 ASN A CB 1 ATOM 1228 C CG . ASN A 1 154 ? 26.791 -15.657 38.902 1.00 131.91 ? 154 ASN A CG 1 ATOM 1229 O OD1 . ASN A 1 154 ? 27.330 -14.609 39.259 1.00 132.97 ? 154 ASN A OD1 1 ATOM 1230 N ND2 . ASN A 1 154 ? 26.109 -16.432 39.742 1.00 132.97 ? 154 ASN A ND2 1 ATOM 1231 N N . SER A 1 155 ? 30.450 -15.642 36.423 1.00 129.63 ? 155 SER A N 1 ATOM 1232 C CA . SER A 1 155 ? 31.828 -16.050 36.732 1.00 131.41 ? 155 SER A CA 1 ATOM 1233 C C . SER A 1 155 ? 32.031 -17.571 36.733 1.00 132.16 ? 155 SER A C 1 ATOM 1234 O O . SER A 1 155 ? 32.700 -18.105 37.613 1.00 136.05 ? 155 SER A O 1 ATOM 1235 C CB . SER A 1 155 ? 32.284 -15.460 38.077 1.00 132.24 ? 155 SER A CB 1 ATOM 1236 O OG . SER A 1 155 ? 32.134 -14.052 38.104 1.00 131.00 ? 155 SER A OG 1 ATOM 1237 N N . THR A 1 156 ? 31.445 -18.263 35.758 1.00 130.55 ? 156 THR A N 1 ATOM 1238 C CA . THR A 1 156 ? 31.684 -19.699 35.576 1.00 129.89 ? 156 THR A CA 1 ATOM 1239 C C . THR A 1 156 ? 31.570 -20.086 34.106 1.00 128.49 ? 156 THR A C 1 ATOM 1240 O O . THR A 1 156 ? 30.648 -19.651 33.415 1.00 127.40 ? 156 THR A O 1 ATOM 1241 C CB . THR A 1 156 ? 30.683 -20.563 36.369 1.00 129.55 ? 156 THR A CB 1 ATOM 1242 O OG1 . THR A 1 156 ? 30.513 -20.024 37.681 1.00 129.85 ? 156 THR A OG1 1 ATOM 1243 C CG2 . THR A 1 156 ? 31.176 -22.009 36.478 1.00 130.61 ? 156 THR A CG2 1 ATOM 1244 N N . TYR A 1 157 ? 32.513 -20.902 33.642 1.00 127.64 ? 157 TYR A N 1 ATOM 1245 C CA . TYR A 1 157 ? 32.437 -21.507 32.319 1.00 127.09 ? 157 TYR A CA 1 ATOM 1246 C C . TYR A 1 157 ? 32.489 -23.024 32.501 1.00 125.54 ? 157 TYR A C 1 ATOM 1247 O O . TYR A 1 157 ? 33.564 -23.631 32.440 1.00 123.14 ? 157 TYR A O 1 ATOM 1248 C CB . TYR A 1 157 ? 33.572 -21.010 31.414 1.00 127.05 ? 157 TYR A CB 1 ATOM 1249 C CG . TYR A 1 157 ? 33.269 -21.084 29.921 1.00 127.80 ? 157 TYR A CG 1 ATOM 1250 C CD1 . TYR A 1 157 ? 33.242 -22.304 29.246 1.00 127.78 ? 157 TYR A CD1 1 ATOM 1251 C CD2 . TYR A 1 157 ? 33.016 -19.930 29.186 1.00 127.01 ? 157 TYR A CD2 1 ATOM 1252 C CE1 . TYR A 1 157 ? 32.973 -22.367 27.886 1.00 125.77 ? 157 TYR A CE1 1 ATOM 1253 C CE2 . TYR A 1 157 ? 32.748 -19.985 27.827 1.00 124.13 ? 157 TYR A CE2 1 ATOM 1254 C CZ . TYR A 1 157 ? 32.725 -21.204 27.179 1.00 123.67 ? 157 TYR A CZ 1 ATOM 1255 O OH . TYR A 1 157 ? 32.460 -21.244 25.824 1.00 119.90 ? 157 TYR A OH 1 ATOM 1256 N N . PRO A 1 158 ? 31.322 -23.640 32.753 1.00 124.92 ? 158 PRO A N 1 ATOM 1257 C CA . PRO A 1 158 ? 31.304 -25.091 32.868 1.00 126.28 ? 158 PRO A CA 1 ATOM 1258 C C . PRO A 1 158 ? 31.597 -25.729 31.522 1.00 124.74 ? 158 PRO A C 1 ATOM 1259 O O . PRO A 1 158 ? 31.327 -25.131 30.477 1.00 123.52 ? 158 PRO A O 1 ATOM 1260 C CB . PRO A 1 158 ? 29.872 -25.398 33.320 1.00 128.20 ? 158 PRO A CB 1 ATOM 1261 C CG . PRO A 1 158 ? 29.061 -24.248 32.842 1.00 126.68 ? 158 PRO A CG 1 ATOM 1262 C CD . PRO A 1 158 ? 29.971 -23.054 32.852 1.00 125.12 ? 158 PRO A CD 1 ATOM 1263 N N . THR A 1 159 ? 32.162 -26.927 31.550 1.00 125.38 ? 159 THR A N 1 ATOM 1264 C CA . THR A 1 159 ? 32.503 -27.620 30.323 1.00 123.32 ? 159 THR A CA 1 ATOM 1265 C C . THR A 1 159 ? 31.255 -27.768 29.456 1.00 122.06 ? 159 THR A C 1 ATOM 1266 O O . THR A 1 159 ? 30.200 -28.197 29.929 1.00 117.41 ? 159 THR A O 1 ATOM 1267 C CB . THR A 1 159 ? 33.129 -28.998 30.601 1.00 126.48 ? 159 THR A CB 1 ATOM 1268 O OG1 . THR A 1 159 ? 34.252 -28.839 31.474 1.00 127.70 ? 159 THR A OG1 1 ATOM 1269 C CG2 . THR A 1 159 ? 33.598 -29.656 29.309 1.00 126.32 ? 159 THR A CG2 1 ATOM 1270 N N . ILE A 1 160 ? 31.394 -27.373 28.195 1.00 121.85 ? 160 ILE A N 1 ATOM 1271 C CA . ILE A 1 160 ? 30.338 -27.493 27.195 1.00 122.50 ? 160 ILE A CA 1 ATOM 1272 C C . ILE A 1 160 ? 30.404 -28.878 26.562 1.00 124.44 ? 160 ILE A C 1 ATOM 1273 O O . ILE A 1 160 ? 31.481 -29.339 26.191 1.00 123.85 ? 160 ILE A O 1 ATOM 1274 C CB . ILE A 1 160 ? 30.492 -26.407 26.108 1.00 118.02 ? 160 ILE A CB 1 ATOM 1275 C CG1 . ILE A 1 160 ? 30.112 -25.046 26.694 1.00 117.89 ? 160 ILE A CG1 1 ATOM 1276 C CG2 . ILE A 1 160 ? 29.629 -26.720 24.894 1.00 117.25 ? 160 ILE A CG2 1 ATOM 1277 C CD1 . ILE A 1 160 ? 30.538 -23.859 25.860 1.00 115.61 ? 160 ILE A CD1 1 ATOM 1278 N N . LYS A 1 161 ? 29.254 -29.539 26.459 1.00 126.21 ? 161 LYS A N 1 ATOM 1279 C CA . LYS A 1 161 ? 29.151 -30.831 25.785 1.00 130.12 ? 161 LYS A CA 1 ATOM 1280 C C . LYS A 1 161 ? 27.884 -30.847 24.941 1.00 130.91 ? 161 LYS A C 1 ATOM 1281 O O . LYS A 1 161 ? 26.807 -31.176 25.434 1.00 132.15 ? 161 LYS A O 1 ATOM 1282 C CB . LYS A 1 161 ? 29.121 -31.982 26.796 1.00 136.21 ? 161 LYS A CB 1 ATOM 1283 C CG . LYS A 1 161 ? 30.426 -32.212 27.546 1.00 139.10 ? 161 LYS A CG 1 ATOM 1284 C CD . LYS A 1 161 ? 30.238 -33.160 28.725 1.00 142.82 ? 161 LYS A CD 1 ATOM 1285 C CE . LYS A 1 161 ? 31.506 -33.281 29.560 1.00 144.49 ? 161 LYS A CE 1 ATOM 1286 N NZ . LYS A 1 161 ? 31.254 -33.915 30.885 1.00 146.50 ? 161 LYS A NZ 1 ATOM 1287 N N . ARG A 1 162 ? 28.017 -30.478 23.671 1.00 129.75 ? 162 ARG A N 1 ATOM 1288 C CA . ARG A 1 162 ? 26.879 -30.415 22.766 1.00 130.60 ? 162 ARG A CA 1 ATOM 1289 C C . ARG A 1 162 ? 27.116 -31.286 21.551 1.00 132.45 ? 162 ARG A C 1 ATOM 1290 O O . ARG A 1 162 ? 28.250 -31.659 21.244 1.00 134.09 ? 162 ARG A O 1 ATOM 1291 C CB . ARG A 1 162 ? 26.635 -28.980 22.309 1.00 129.28 ? 162 ARG A CB 1 ATOM 1292 C CG . ARG A 1 162 ? 26.340 -27.995 23.425 1.00 131.16 ? 162 ARG A CG 1 ATOM 1293 C CD . ARG A 1 162 ? 25.058 -28.329 24.174 1.00 135.14 ? 162 ARG A CD 1 ATOM 1294 N NE . ARG A 1 162 ? 24.184 -27.161 24.255 1.00 135.51 ? 162 ARG A NE 1 ATOM 1295 C CZ . ARG A 1 162 ? 23.325 -26.787 23.307 1.00 133.94 ? 162 ARG A CZ 1 ATOM 1296 N NH1 . ARG A 1 162 ? 23.192 -27.492 22.182 1.00 130.96 ? 162 ARG A NH1 1 ATOM 1297 N NH2 . ARG A 1 162 ? 22.584 -25.697 23.485 1.00 133.51 ? 162 ARG A NH2 1 ATOM 1298 N N . SER A 1 163 ? 26.034 -31.592 20.847 1.00 130.68 ? 163 SER A N 1 ATOM 1299 C CA . SER A 1 163 ? 26.105 -32.490 19.718 1.00 126.47 ? 163 SER A CA 1 ATOM 1300 C C . SER A 1 163 ? 24.929 -32.285 18.774 1.00 125.03 ? 163 SER A C 1 ATOM 1301 O O . SER A 1 163 ? 23.777 -32.345 19.195 1.00 121.02 ? 163 SER A O 1 ATOM 1302 C CB . SER A 1 163 ? 26.126 -33.933 20.218 1.00 128.37 ? 163 SER A CB 1 ATOM 1303 O OG . SER A 1 163 ? 26.268 -34.834 19.137 1.00 133.71 ? 163 SER A OG 1 ATOM 1304 N N . TYR A 1 164 ? 25.225 -32.035 17.499 1.00 123.61 ? 164 TYR A N 1 ATOM 1305 C CA . TYR A 1 164 ? 24.190 -31.963 16.476 1.00 123.01 ? 164 TYR A CA 1 ATOM 1306 C C . TYR A 1 164 ? 24.249 -33.187 15.576 1.00 124.85 ? 164 TYR A C 1 ATOM 1307 O O . TYR A 1 164 ? 25.324 -33.707 15.294 1.00 126.92 ? 164 TYR A O 1 ATOM 1308 C CB . TYR A 1 164 ? 24.321 -30.701 15.633 1.00 119.78 ? 164 TYR A CB 1 ATOM 1309 C CG . TYR A 1 164 ? 23.326 -30.683 14.503 1.00 122.93 ? 164 TYR A CG 1 ATOM 1310 C CD1 . TYR A 1 164 ? 22.013 -30.273 14.710 1.00 125.13 ? 164 TYR A CD1 1 ATOM 1311 C CD2 . TYR A 1 164 ? 23.684 -31.123 13.233 1.00 123.73 ? 164 TYR A CD2 1 ATOM 1312 C CE1 . TYR A 1 164 ? 21.091 -30.275 13.675 1.00 127.30 ? 164 TYR A CE1 1 ATOM 1313 C CE2 . TYR A 1 164 ? 22.772 -31.128 12.191 1.00 124.95 ? 164 TYR A CE2 1 ATOM 1314 C CZ . TYR A 1 164 ? 21.479 -30.704 12.415 1.00 127.10 ? 164 TYR A CZ 1 ATOM 1315 O OH . TYR A 1 164 ? 20.581 -30.714 11.374 1.00 130.06 ? 164 TYR A OH 1 ATOM 1316 N N . ASN A 1 165 ? 23.080 -33.624 15.121 1.00 126.52 ? 165 ASN A N 1 ATOM 1317 C CA . ASN A 1 165 ? 22.948 -34.791 14.268 1.00 128.67 ? 165 ASN A CA 1 ATOM 1318 C C . ASN A 1 165 ? 22.322 -34.389 12.947 1.00 130.65 ? 165 ASN A C 1 ATOM 1319 O O . ASN A 1 165 ? 21.250 -33.789 12.923 1.00 132.75 ? 165 ASN A O 1 ATOM 1320 C CB . ASN A 1 165 ? 22.072 -35.819 14.968 1.00 133.22 ? 165 ASN A CB 1 ATOM 1321 C CG . ASN A 1 165 ? 21.763 -37.032 14.104 1.00 135.64 ? 165 ASN A CG 1 ATOM 1322 O OD1 . ASN A 1 165 ? 21.345 -36.915 12.948 1.00 131.86 ? 165 ASN A OD1 1 ATOM 1323 N ND2 . ASN A 1 165 ? 21.957 -38.219 14.680 1.00 139.79 ? 165 ASN A ND2 1 ATOM 1324 N N . ASN A 1 166 ? 22.990 -34.738 11.851 1.00 132.47 ? 166 ASN A N 1 ATOM 1325 C CA . ASN A 1 166 ? 22.520 -34.401 10.513 1.00 131.88 ? 166 ASN A CA 1 ATOM 1326 C C . ASN A 1 166 ? 21.413 -35.353 10.082 1.00 132.34 ? 166 ASN A C 1 ATOM 1327 O O . ASN A 1 166 ? 21.665 -36.356 9.417 1.00 131.10 ? 166 ASN A O 1 ATOM 1328 C CB . ASN A 1 166 ? 23.685 -34.447 9.515 1.00 132.09 ? 166 ASN A CB 1 ATOM 1329 C CG . ASN A 1 166 ? 23.365 -33.741 8.215 1.00 133.00 ? 166 ASN A CG 1 ATOM 1330 O OD1 . ASN A 1 166 ? 22.407 -32.976 8.140 1.00 135.03 ? 166 ASN A OD1 1 ATOM 1331 N ND2 . ASN A 1 166 ? 24.176 -33.976 7.188 1.00 131.41 ? 166 ASN A ND2 1 ATOM 1332 N N . THR A 1 167 ? 20.186 -35.034 10.479 1.00 132.67 ? 167 THR A N 1 ATOM 1333 C CA . THR A 1 167 ? 19.024 -35.858 10.154 1.00 136.94 ? 167 THR A CA 1 ATOM 1334 C C . THR A 1 167 ? 18.535 -35.598 8.733 1.00 136.84 ? 167 THR A C 1 ATOM 1335 O O . THR A 1 167 ? 18.185 -36.529 8.007 1.00 139.57 ? 167 THR A O 1 ATOM 1336 C CB . THR A 1 167 ? 17.869 -35.578 11.120 1.00 139.40 ? 167 THR A CB 1 ATOM 1337 O OG1 . THR A 1 167 ? 17.656 -34.164 11.201 1.00 138.70 ? 167 THR A OG1 1 ATOM 1338 C CG2 . THR A 1 167 ? 18.193 -36.122 12.495 1.00 140.69 ? 167 THR A CG2 1 ATOM 1339 N N . ASN A 1 168 ? 18.486 -34.322 8.361 1.00 135.05 ? 168 ASN A N 1 ATOM 1340 C CA . ASN A 1 168 ? 18.190 -33.900 6.980 1.00 132.62 ? 168 ASN A CA 1 ATOM 1341 C C . ASN A 1 168 ? 19.061 -34.557 5.892 1.00 129.17 ? 168 ASN A C 1 ATOM 1342 O O . ASN A 1 168 ? 20.202 -34.946 6.138 1.00 126.89 ? 168 ASN A O 1 ATOM 1343 C CB . ASN A 1 168 ? 18.260 -32.372 6.854 1.00 128.82 ? 168 ASN A CB 1 ATOM 1344 C CG . ASN A 1 168 ? 19.397 -31.767 7.653 1.00 127.11 ? 168 ASN A CG 1 ATOM 1345 O OD1 . ASN A 1 168 ? 19.283 -30.660 8.173 1.00 125.25 ? 168 ASN A OD1 1 ATOM 1346 N ND2 . ASN A 1 168 ? 20.492 -32.499 7.771 1.00 126.73 ? 168 ASN A ND2 1 ATOM 1347 N N . GLN A 1 169 ? 18.500 -34.625 4.687 1.00 127.05 ? 169 GLN A N 1 ATOM 1348 C CA . GLN A 1 169 ? 19.009 -35.462 3.591 1.00 129.11 ? 169 GLN A CA 1 ATOM 1349 C C . GLN A 1 169 ? 20.344 -35.028 2.964 1.00 127.49 ? 169 GLN A C 1 ATOM 1350 O O . GLN A 1 169 ? 21.021 -35.836 2.323 1.00 123.05 ? 169 GLN A O 1 ATOM 1351 C CB . GLN A 1 169 ? 17.952 -35.522 2.481 1.00 131.29 ? 169 GLN A CB 1 ATOM 1352 C CG . GLN A 1 169 ? 16.891 -36.587 2.665 1.00 134.70 ? 169 GLN A CG 1 ATOM 1353 C CD . GLN A 1 169 ? 17.159 -37.825 1.824 1.00 141.28 ? 169 GLN A CD 1 ATOM 1354 O OE1 . GLN A 1 169 ? 17.424 -37.736 0.612 1.00 131.37 ? 169 GLN A OE1 1 ATOM 1355 N NE2 . GLN A 1 169 ? 17.077 -38.996 2.459 1.00 146.79 ? 169 GLN A NE2 1 ATOM 1356 N N . GLU A 1 170 ? 20.703 -33.758 3.145 1.00 127.00 ? 170 GLU A N 1 ATOM 1357 C CA . GLU A 1 170 ? 21.839 -33.139 2.457 1.00 120.26 ? 170 GLU A CA 1 ATOM 1358 C C . GLU A 1 170 ? 23.172 -33.365 3.183 1.00 118.94 ? 170 GLU A C 1 ATOM 1359 O O . GLU A 1 170 ? 23.230 -34.009 4.228 1.00 120.05 ? 170 GLU A O 1 ATOM 1360 C CB . GLU A 1 170 ? 21.589 -31.627 2.317 1.00 118.71 ? 170 GLU A CB 1 ATOM 1361 C CG . GLU A 1 170 ? 20.577 -31.212 1.250 1.00 120.53 ? 170 GLU A CG 1 ATOM 1362 C CD . GLU A 1 170 ? 19.160 -31.699 1.513 1.00 123.70 ? 170 GLU A CD 1 ATOM 1363 O OE1 . GLU A 1 170 ? 18.932 -32.912 1.367 1.00 134.46 ? 170 GLU A OE1 1 ATOM 1364 O OE2 . GLU A 1 170 ? 18.265 -30.881 1.833 1.00 124.78 ? 170 GLU A OE2 1 ATOM 1365 N N . ASP A 1 171 ? 24.246 -32.854 2.591 1.00 119.84 ? 171 ASP A N 1 ATOM 1366 C CA . ASP A 1 171 ? 25.501 -32.637 3.300 1.00 117.85 ? 171 ASP A CA 1 ATOM 1367 C C . ASP A 1 171 ? 25.373 -31.271 3.944 1.00 114.75 ? 171 ASP A C 1 ATOM 1368 O O . ASP A 1 171 ? 24.692 -30.391 3.411 1.00 112.55 ? 171 ASP A O 1 ATOM 1369 C CB . ASP A 1 171 ? 26.697 -32.630 2.344 1.00 121.03 ? 171 ASP A CB 1 ATOM 1370 C CG . ASP A 1 171 ? 26.943 -33.983 1.689 1.00 125.66 ? 171 ASP A CG 1 ATOM 1371 O OD1 . ASP A 1 171 ? 27.146 -34.981 2.414 1.00 128.80 ? 171 ASP A OD1 1 ATOM 1372 O OD2 . ASP A 1 171 ? 26.956 -34.042 0.442 1.00 126.73 ? 171 ASP A OD2 1 ATOM 1373 N N . LEU A 1 172 ? 26.031 -31.090 5.082 1.00 113.66 ? 172 LEU A N 1 ATOM 1374 C CA . LEU A 1 172 ? 25.905 -29.858 5.843 1.00 110.34 ? 172 LEU A CA 1 ATOM 1375 C C . LEU A 1 172 ? 27.267 -29.218 6.038 1.00 107.60 ? 172 LEU A C 1 ATOM 1376 O O . LEU A 1 172 ? 28.213 -29.889 6.441 1.00 110.17 ? 172 LEU A O 1 ATOM 1377 C CB . LEU A 1 172 ? 25.268 -30.157 7.197 1.00 112.10 ? 172 LEU A CB 1 ATOM 1378 C CG . LEU A 1 172 ? 24.654 -28.971 7.949 1.00 112.46 ? 172 LEU A CG 1 ATOM 1379 C CD1 . LEU A 1 172 ? 23.339 -28.533 7.317 1.00 111.32 ? 172 LEU A CD1 1 ATOM 1380 C CD2 . LEU A 1 172 ? 24.446 -29.325 9.415 1.00 114.85 ? 172 LEU A CD2 1 ATOM 1381 N N . LEU A 1 173 ? 27.365 -27.925 5.737 1.00 103.32 ? 173 LEU A N 1 ATOM 1382 C CA . LEU A 1 173 ? 28.578 -27.169 6.008 1.00 99.90 ? 173 LEU A CA 1 ATOM 1383 C C . LEU A 1 173 ? 28.467 -26.556 7.385 1.00 101.29 ? 173 LEU A C 1 ATOM 1384 O O . LEU A 1 173 ? 27.695 -25.621 7.581 1.00 101.07 ? 173 LEU A O 1 ATOM 1385 C CB . LEU A 1 173 ? 28.782 -26.052 4.989 1.00 98.97 ? 173 LEU A CB 1 ATOM 1386 C CG . LEU A 1 173 ? 29.942 -25.102 5.320 1.00 97.78 ? 173 LEU A CG 1 ATOM 1387 C CD1 . LEU A 1 173 ? 31.261 -25.855 5.279 1.00 98.40 ? 173 LEU A CD1 1 ATOM 1388 C CD2 . LEU A 1 173 ? 29.983 -23.902 4.387 1.00 94.44 ? 173 LEU A CD2 1 ATOM 1389 N N . VAL A 1 174 ? 29.252 -27.073 8.326 1.00 101.22 ? 174 VAL A N 1 ATOM 1390 C CA . VAL A 1 174 ? 29.287 -26.556 9.685 1.00 100.50 ? 174 VAL A CA 1 ATOM 1391 C C . VAL A 1 174 ? 30.538 -25.715 9.885 1.00 97.43 ? 174 VAL A C 1 ATOM 1392 O O . VAL A 1 174 ? 31.623 -26.113 9.466 1.00 97.18 ? 174 VAL A O 1 ATOM 1393 C CB . VAL A 1 174 ? 29.290 -27.697 10.717 1.00 104.33 ? 174 VAL A CB 1 ATOM 1394 C CG1 . VAL A 1 174 ? 29.339 -27.137 12.130 1.00 105.78 ? 174 VAL A CG1 1 ATOM 1395 C CG2 . VAL A 1 174 ? 28.065 -28.579 10.535 1.00 106.38 ? 174 VAL A CG2 1 ATOM 1396 N N . LEU A 1 175 ? 30.373 -24.567 10.539 1.00 95.67 ? 175 LEU A N 1 ATOM 1397 C CA . LEU A 1 175 ? 31.466 -23.639 10.820 1.00 95.74 ? 175 LEU A CA 1 ATOM 1398 C C . LEU A 1 175 ? 31.539 -23.334 12.306 1.00 96.53 ? 175 LEU A C 1 ATOM 1399 O O . LEU A 1 175 ? 30.513 -23.228 12.975 1.00 97.73 ? 175 LEU A O 1 ATOM 1400 C CB . LEU A 1 175 ? 31.234 -22.321 10.094 1.00 95.83 ? 175 LEU A CB 1 ATOM 1401 C CG . LEU A 1 175 ? 31.141 -22.369 8.572 1.00 97.22 ? 175 LEU A CG 1 ATOM 1402 C CD1 . LEU A 1 175 ? 30.160 -21.307 8.097 1.00 98.24 ? 175 LEU A CD1 1 ATOM 1403 C CD2 . LEU A 1 175 ? 32.510 -22.178 7.934 1.00 96.11 ? 175 LEU A CD2 1 ATOM 1404 N N . TRP A 1 176 ? 32.753 -23.174 12.814 1.00 93.37 ? 176 TRP A N 1 ATOM 1405 C CA . TRP A 1 176 ? 32.950 -22.758 14.190 1.00 94.70 ? 176 TRP A CA 1 ATOM 1406 C C . TRP A 1 176 ? 34.265 -22.000 14.306 1.00 94.57 ? 176 TRP A C 1 ATOM 1407 O O . TRP A 1 176 ? 34.948 -21.787 13.312 1.00 94.02 ? 176 TRP A O 1 ATOM 1408 C CB . TRP A 1 176 ? 32.910 -23.972 15.126 1.00 97.68 ? 176 TRP A CB 1 ATOM 1409 C CG . TRP A 1 176 ? 34.016 -24.955 14.923 1.00 97.96 ? 176 TRP A CG 1 ATOM 1410 C CD1 . TRP A 1 176 ? 35.171 -25.044 15.641 1.00 98.22 ? 176 TRP A CD1 1 ATOM 1411 C CD2 . TRP A 1 176 ? 34.072 -25.997 13.944 1.00 98.53 ? 176 TRP A CD2 1 ATOM 1412 N NE1 . TRP A 1 176 ? 35.946 -26.075 15.172 1.00 97.63 ? 176 TRP A NE1 1 ATOM 1413 C CE2 . TRP A 1 176 ? 35.295 -26.678 14.129 1.00 98.70 ? 176 TRP A CE2 1 ATOM 1414 C CE3 . TRP A 1 176 ? 33.209 -26.421 12.926 1.00 99.24 ? 176 TRP A CE3 1 ATOM 1415 C CZ2 . TRP A 1 176 ? 35.679 -27.758 13.331 1.00 98.84 ? 176 TRP A CZ2 1 ATOM 1416 C CZ3 . TRP A 1 176 ? 33.590 -27.497 12.135 1.00 99.16 ? 176 TRP A CZ3 1 ATOM 1417 C CH2 . TRP A 1 176 ? 34.816 -28.152 12.342 1.00 99.11 ? 176 TRP A CH2 1 ATOM 1418 N N . GLY A 1 177 ? 34.611 -21.571 15.513 1.00 98.16 ? 177 GLY A N 1 ATOM 1419 C CA . GLY A 1 177 ? 35.852 -20.834 15.712 1.00 96.44 ? 177 GLY A CA 1 ATOM 1420 C C . GLY A 1 177 ? 36.400 -20.899 17.119 1.00 96.56 ? 177 GLY A C 1 ATOM 1421 O O . GLY A 1 177 ? 35.739 -21.376 18.043 1.00 97.64 ? 177 GLY A O 1 ATOM 1422 N N . ILE A 1 178 ? 37.621 -20.400 17.267 1.00 94.81 ? 178 ILE A N 1 ATOM 1423 C CA . ILE A 1 178 ? 38.284 -20.326 18.554 1.00 96.69 ? 178 ILE A CA 1 ATOM 1424 C C . ILE A 1 178 ? 38.806 -18.906 18.755 1.00 96.92 ? 178 ILE A C 1 ATOM 1425 O O . ILE A 1 178 ? 39.259 -18.268 17.805 1.00 94.90 ? 178 ILE A O 1 ATOM 1426 C CB . ILE A 1 178 ? 39.430 -21.355 18.658 1.00 98.72 ? 178 ILE A CB 1 ATOM 1427 C CG1 . ILE A 1 178 ? 40.045 -21.332 20.058 1.00 102.85 ? 178 ILE A CG1 1 ATOM 1428 C CG2 . ILE A 1 178 ? 40.506 -21.096 17.617 1.00 98.21 ? 178 ILE A CG2 1 ATOM 1429 C CD1 . ILE A 1 178 ? 41.006 -22.467 20.332 1.00 106.35 ? 178 ILE A CD1 1 ATOM 1430 N N . HIS A 1 179 ? 38.726 -18.411 19.990 1.00 98.99 ? 179 HIS A N 1 ATOM 1431 C CA . HIS A 1 179 ? 39.240 -17.082 20.323 1.00 98.86 ? 179 HIS A CA 1 ATOM 1432 C C . HIS A 1 179 ? 40.639 -17.155 20.933 1.00 98.99 ? 179 HIS A C 1 ATOM 1433 O O . HIS A 1 179 ? 40.883 -17.918 21.864 1.00 100.13 ? 179 HIS A O 1 ATOM 1434 C CB . HIS A 1 179 ? 38.293 -16.355 21.271 1.00 100.18 ? 179 HIS A CB 1 ATOM 1435 C CG . HIS A 1 179 ? 38.773 -14.996 21.667 1.00 99.44 ? 179 HIS A CG 1 ATOM 1436 N ND1 . HIS A 1 179 ? 38.627 -14.496 22.943 1.00 100.93 ? 179 HIS A ND1 1 ATOM 1437 C CD2 . HIS A 1 179 ? 39.419 -14.041 20.960 1.00 97.14 ? 179 HIS A CD2 1 ATOM 1438 C CE1 . HIS A 1 179 ? 39.148 -13.284 23.000 1.00 101.11 ? 179 HIS A CE1 1 ATOM 1439 N NE2 . HIS A 1 179 ? 39.634 -12.983 21.809 1.00 101.09 ? 179 HIS A NE2 1 ATOM 1440 N N . HIS A 1 180 ? 41.548 -16.361 20.381 1.00 99.28 ? 180 HIS A N 1 ATOM 1441 C CA . HIS A 1 180 ? 42.917 -16.277 20.848 1.00 100.52 ? 180 HIS A CA 1 ATOM 1442 C C . HIS A 1 180 ? 43.043 -14.928 21.509 1.00 104.51 ? 180 HIS A C 1 ATOM 1443 O O . HIS A 1 180 ? 43.298 -13.938 20.834 1.00 108.32 ? 180 HIS A O 1 ATOM 1444 C CB . HIS A 1 180 ? 43.896 -16.354 19.678 1.00 101.10 ? 180 HIS A CB 1 ATOM 1445 C CG . HIS A 1 180 ? 43.864 -17.659 18.951 1.00 102.73 ? 180 HIS A CG 1 ATOM 1446 N ND1 . HIS A 1 180 ? 44.145 -18.853 19.571 1.00 107.19 ? 180 HIS A ND1 1 ATOM 1447 C CD2 . HIS A 1 180 ? 43.586 -17.961 17.663 1.00 101.11 ? 180 HIS A CD2 1 ATOM 1448 C CE1 . HIS A 1 180 ? 44.035 -19.840 18.702 1.00 103.63 ? 180 HIS A CE1 1 ATOM 1449 N NE2 . HIS A 1 180 ? 43.698 -19.325 17.535 1.00 102.95 ? 180 HIS A NE2 1 ATOM 1450 N N . PRO A 1 181 ? 42.856 -14.872 22.831 1.00 108.09 ? 181 PRO A N 1 ATOM 1451 C CA . PRO A 1 181 ? 42.926 -13.578 23.495 1.00 108.85 ? 181 PRO A CA 1 ATOM 1452 C C . PRO A 1 181 ? 44.351 -13.048 23.573 1.00 108.14 ? 181 PRO A C 1 ATOM 1453 O O . PRO A 1 181 ? 45.300 -13.769 23.263 1.00 104.72 ? 181 PRO A O 1 ATOM 1454 C CB . PRO A 1 181 ? 42.379 -13.874 24.890 1.00 112.48 ? 181 PRO A CB 1 ATOM 1455 C CG . PRO A 1 181 ? 42.707 -15.308 25.122 1.00 113.10 ? 181 PRO A CG 1 ATOM 1456 C CD . PRO A 1 181 ? 42.657 -15.979 23.784 1.00 110.79 ? 181 PRO A CD 1 ATOM 1457 N N . ASN A 1 182 ? 44.486 -11.796 23.994 1.00 110.81 ? 182 ASN A N 1 ATOM 1458 C CA . ASN A 1 182 ? 45.780 -11.125 24.028 1.00 113.34 ? 182 ASN A CA 1 ATOM 1459 C C . ASN A 1 182 ? 46.682 -11.596 25.169 1.00 114.92 ? 182 ASN A C 1 ATOM 1460 O O . ASN A 1 182 ? 47.878 -11.815 24.962 1.00 115.78 ? 182 ASN A O 1 ATOM 1461 C CB . ASN A 1 182 ? 45.570 -9.613 24.121 1.00 115.29 ? 182 ASN A CB 1 ATOM 1462 C CG . ASN A 1 182 ? 46.873 -8.837 24.112 1.00 116.81 ? 182 ASN A CG 1 ATOM 1463 O OD1 . ASN A 1 182 ? 47.194 -8.145 25.073 1.00 120.49 ? 182 ASN A OD1 1 ATOM 1464 N ND2 . ASN A 1 182 ? 47.629 -8.946 23.030 1.00 118.12 ? 182 ASN A ND2 1 ATOM 1465 N N . ASP A 1 183 ? 46.109 -11.749 26.364 1.00 116.57 ? 183 ASP A N 1 ATOM 1466 C CA . ASP A 1 183 ? 46.882 -12.094 27.565 1.00 120.54 ? 183 ASP A CA 1 ATOM 1467 C C . ASP A 1 183 ? 46.087 -12.935 28.576 1.00 118.89 ? 183 ASP A C 1 ATOM 1468 O O . ASP A 1 183 ? 44.888 -13.171 28.404 1.00 113.98 ? 183 ASP A O 1 ATOM 1469 C CB . ASP A 1 183 ? 47.411 -10.814 28.234 1.00 123.28 ? 183 ASP A CB 1 ATOM 1470 C CG . ASP A 1 183 ? 46.301 -9.847 28.624 1.00 124.05 ? 183 ASP A CG 1 ATOM 1471 O OD1 . ASP A 1 183 ? 45.325 -10.273 29.275 1.00 127.37 ? 183 ASP A OD1 1 ATOM 1472 O OD2 . ASP A 1 183 ? 46.412 -8.650 28.288 1.00 124.14 ? 183 ASP A OD2 1 ATOM 1473 N N . ALA A 1 184 ? 46.773 -13.369 29.635 1.00 117.51 ? 184 ALA A N 1 ATOM 1474 C CA . ALA A 1 184 ? 46.181 -14.226 30.669 1.00 114.59 ? 184 ALA A CA 1 ATOM 1475 C C . ALA A 1 184 ? 45.027 -13.554 31.418 1.00 114.04 ? 184 ALA A C 1 ATOM 1476 O O . ALA A 1 184 ? 44.095 -14.231 31.862 1.00 110.02 ? 184 ALA A O 1 ATOM 1477 C CB . ALA A 1 184 ? 47.255 -14.681 31.647 1.00 113.18 ? 184 ALA A CB 1 ATOM 1478 N N . ALA A 1 185 ? 45.099 -12.230 31.555 1.00 116.00 ? 185 ALA A N 1 ATOM 1479 C CA . ALA A 1 185 ? 44.072 -11.453 32.249 1.00 116.28 ? 185 ALA A CA 1 ATOM 1480 C C . ALA A 1 185 ? 42.779 -11.399 31.444 1.00 118.39 ? 185 ALA A C 1 ATOM 1481 O O . ALA A 1 185 ? 41.684 -11.525 31.999 1.00 118.18 ? 185 ALA A O 1 ATOM 1482 C CB . ALA A 1 185 ? 44.574 -10.047 32.527 1.00 115.47 ? 185 ALA A CB 1 ATOM 1483 N N . GLU A 1 186 ? 42.915 -11.208 30.135 1.00 122.85 ? 186 GLU A N 1 ATOM 1484 C CA . GLU A 1 186 ? 41.768 -11.201 29.222 1.00 125.24 ? 186 GLU A CA 1 ATOM 1485 C C . GLU A 1 186 ? 41.104 -12.580 29.201 1.00 120.72 ? 186 GLU A C 1 ATOM 1486 O O . GLU A 1 186 ? 39.878 -12.687 29.229 1.00 118.26 ? 186 GLU A O 1 ATOM 1487 C CB . GLU A 1 186 ? 42.214 -10.795 27.812 1.00 131.35 ? 186 GLU A CB 1 ATOM 1488 C CG . GLU A 1 186 ? 41.104 -10.309 26.886 1.00 134.59 ? 186 GLU A CG 1 ATOM 1489 C CD . GLU A 1 186 ? 41.638 -9.825 25.540 1.00 139.74 ? 186 GLU A CD 1 ATOM 1490 O OE1 . GLU A 1 186 ? 42.554 -8.971 25.525 1.00 139.70 ? 186 GLU A OE1 1 ATOM 1491 O OE2 . GLU A 1 186 ? 41.155 -10.307 24.490 1.00 143.27 ? 186 GLU A OE2 1 ATOM 1492 N N . GLN A 1 187 ? 41.929 -13.626 29.167 1.00 116.78 ? 187 GLN A N 1 ATOM 1493 C CA . GLN A 1 187 ? 41.457 -15.012 29.238 1.00 114.81 ? 187 GLN A CA 1 ATOM 1494 C C . GLN A 1 187 ? 40.600 -15.245 30.486 1.00 117.07 ? 187 GLN A C 1 ATOM 1495 O O . GLN A 1 187 ? 39.453 -15.692 30.381 1.00 113.64 ? 187 GLN A O 1 ATOM 1496 C CB . GLN A 1 187 ? 42.652 -15.981 29.208 1.00 113.33 ? 187 GLN A CB 1 ATOM 1497 C CG . GLN A 1 187 ? 42.326 -17.445 29.488 1.00 112.92 ? 187 GLN A CG 1 ATOM 1498 C CD . GLN A 1 187 ? 41.502 -18.099 28.394 1.00 109.20 ? 187 GLN A CD 1 ATOM 1499 O OE1 . GLN A 1 187 ? 41.702 -17.839 27.211 1.00 104.87 ? 187 GLN A OE1 1 ATOM 1500 N NE2 . GLN A 1 187 ? 40.581 -18.971 28.788 1.00 109.74 ? 187 GLN A NE2 1 ATOM 1501 N N . THR A 1 188 ? 41.154 -14.934 31.660 1.00 120.16 ? 188 THR A N 1 ATOM 1502 C CA . THR A 1 188 ? 40.416 -15.100 32.917 1.00 122.60 ? 188 THR A CA 1 ATOM 1503 C C . THR A 1 188 ? 39.163 -14.221 32.949 1.00 117.87 ? 188 THR A C 1 ATOM 1504 O O . THR A 1 188 ? 38.121 -14.653 33.434 1.00 118.20 ? 188 THR A O 1 ATOM 1505 C CB . THR A 1 188 ? 41.278 -14.814 34.174 1.00 125.68 ? 188 THR A CB 1 ATOM 1506 O OG1 . THR A 1 188 ? 41.876 -13.518 34.071 1.00 130.20 ? 188 THR A OG1 1 ATOM 1507 C CG2 . THR A 1 188 ? 42.370 -15.876 34.352 1.00 126.66 ? 188 THR A CG2 1 ATOM 1508 N N . LYS A 1 189 ? 39.246 -13.004 32.420 1.00 113.60 ? 189 LYS A N 1 ATOM 1509 C CA . LYS A 1 189 ? 38.081 -12.122 32.425 1.00 114.10 ? 189 LYS A CA 1 ATOM 1510 C C . LYS A 1 189 ? 36.908 -12.730 31.655 1.00 112.91 ? 189 LYS A C 1 ATOM 1511 O O . LYS A 1 189 ? 35.782 -12.727 32.144 1.00 108.79 ? 189 LYS A O 1 ATOM 1512 C CB . LYS A 1 189 ? 38.412 -10.746 31.847 1.00 114.88 ? 189 LYS A CB 1 ATOM 1513 C CG . LYS A 1 189 ? 37.229 -9.781 31.901 1.00 117.55 ? 189 LYS A CG 1 ATOM 1514 C CD . LYS A 1 189 ? 37.213 -8.804 30.737 1.00 121.51 ? 189 LYS A CD 1 ATOM 1515 C CE . LYS A 1 189 ? 37.412 -7.369 31.193 1.00 125.30 ? 189 LYS A CE 1 ATOM 1516 N NZ . LYS A 1 189 ? 37.464 -6.455 30.018 1.00 125.66 ? 189 LYS A NZ 1 ATOM 1517 N N . LEU A 1 190 ? 37.181 -13.244 30.456 1.00 112.29 ? 190 LEU A N 1 ATOM 1518 C CA . LEU A 1 190 ? 36.135 -13.753 29.569 1.00 110.08 ? 190 LEU A CA 1 ATOM 1519 C C . LEU A 1 190 ? 35.671 -15.162 29.928 1.00 111.85 ? 190 LEU A C 1 ATOM 1520 O O . LEU A 1 190 ? 34.475 -15.460 29.861 1.00 109.34 ? 190 LEU A O 1 ATOM 1521 C CB . LEU A 1 190 ? 36.620 -13.749 28.116 1.00 109.64 ? 190 LEU A CB 1 ATOM 1522 C CG . LEU A 1 190 ? 37.040 -12.407 27.512 1.00 108.73 ? 190 LEU A CG 1 ATOM 1523 C CD1 . LEU A 1 190 ? 37.374 -12.586 26.040 1.00 105.41 ? 190 LEU A CD1 1 ATOM 1524 C CD2 . LEU A 1 190 ? 35.967 -11.344 27.695 1.00 108.57 ? 190 LEU A CD2 1 ATOM 1525 N N . TYR A 1 191 ? 36.618 -16.025 30.294 1.00 113.96 ? 191 TYR A N 1 ATOM 1526 C CA . TYR A 1 191 ? 36.344 -17.458 30.441 1.00 118.08 ? 191 TYR A CA 1 ATOM 1527 C C . TYR A 1 191 ? 36.738 -18.080 31.788 1.00 123.93 ? 191 TYR A C 1 ATOM 1528 O O . TYR A 1 191 ? 36.541 -19.280 31.983 1.00 126.85 ? 191 TYR A O 1 ATOM 1529 C CB . TYR A 1 191 ? 37.063 -18.215 29.321 1.00 117.43 ? 191 TYR A CB 1 ATOM 1530 C CG . TYR A 1 191 ? 36.939 -17.552 27.963 1.00 114.76 ? 191 TYR A CG 1 ATOM 1531 C CD1 . TYR A 1 191 ? 35.703 -17.440 27.335 1.00 115.03 ? 191 TYR A CD1 1 ATOM 1532 C CD2 . TYR A 1 191 ? 38.051 -17.020 27.317 1.00 111.11 ? 191 TYR A CD2 1 ATOM 1533 C CE1 . TYR A 1 191 ? 35.581 -16.832 26.096 1.00 112.28 ? 191 TYR A CE1 1 ATOM 1534 C CE2 . TYR A 1 191 ? 37.935 -16.407 26.083 1.00 108.96 ? 191 TYR A CE2 1 ATOM 1535 C CZ . TYR A 1 191 ? 36.696 -16.317 25.478 1.00 108.82 ? 191 TYR A CZ 1 ATOM 1536 O OH . TYR A 1 191 ? 36.565 -15.715 24.251 1.00 104.73 ? 191 TYR A OH 1 ATOM 1537 N N . ARG A 1 192 ? 37.284 -17.279 32.704 1.00 125.76 ? 192 ARG A N 1 ATOM 1538 C CA . ARG A 1 192 ? 37.834 -17.762 33.986 1.00 128.41 ? 192 ARG A CA 1 ATOM 1539 C C . ARG A 1 192 ? 39.034 -18.711 33.863 1.00 128.09 ? 192 ARG A C 1 ATOM 1540 O O . ARG A 1 192 ? 40.126 -18.404 34.350 1.00 127.02 ? 192 ARG A O 1 ATOM 1541 C CB . ARG A 1 192 ? 36.747 -18.397 34.872 1.00 132.17 ? 192 ARG A CB 1 ATOM 1542 C CG . ARG A 1 192 ? 36.021 -17.401 35.772 1.00 135.67 ? 192 ARG A CG 1 ATOM 1543 C CD . ARG A 1 192 ? 35.684 -18.000 37.126 1.00 138.63 ? 192 ARG A CD 1 ATOM 1544 N NE . ARG A 1 192 ? 36.883 -18.391 37.866 1.00 143.19 ? 192 ARG A NE 1 ATOM 1545 C CZ . ARG A 1 192 ? 36.879 -19.005 39.049 1.00 147.82 ? 192 ARG A CZ 1 ATOM 1546 N NH1 . ARG A 1 192 ? 35.734 -19.307 39.653 1.00 149.79 ? 192 ARG A NH1 1 ATOM 1547 N NH2 . ARG A 1 192 ? 38.030 -19.317 39.636 1.00 149.24 ? 192 ARG A NH2 1 ATOM 1548 N N . ASN A 1 193 ? 38.829 -19.855 33.216 1.00 129.13 ? 193 ASN A N 1 ATOM 1549 C CA . ASN A 1 193 ? 39.824 -20.928 33.199 1.00 129.39 ? 193 ASN A CA 1 ATOM 1550 C C . ASN A 1 193 ? 41.107 -20.490 32.504 1.00 126.82 ? 193 ASN A C 1 ATOM 1551 O O . ASN A 1 193 ? 41.053 -19.989 31.385 1.00 121.54 ? 193 ASN A O 1 ATOM 1552 C CB . ASN A 1 193 ? 39.263 -22.170 32.504 1.00 129.92 ? 193 ASN A CB 1 ATOM 1553 C CG . ASN A 1 193 ? 37.854 -22.512 32.958 1.00 132.96 ? 193 ASN A CG 1 ATOM 1554 O OD1 . ASN A 1 193 ? 37.140 -21.668 33.492 1.00 136.50 ? 193 ASN A OD1 1 ATOM 1555 N ND2 . ASN A 1 193 ? 37.444 -23.751 32.737 1.00 135.55 ? 193 ASN A ND2 1 ATOM 1556 N N . PRO A 1 194 ? 42.265 -20.666 33.166 1.00 128.84 ? 194 PRO A N 1 ATOM 1557 C CA . PRO A 1 194 ? 43.513 -20.218 32.549 1.00 127.65 ? 194 PRO A CA 1 ATOM 1558 C C . PRO A 1 194 ? 43.834 -20.966 31.255 1.00 125.38 ? 194 PRO A C 1 ATOM 1559 O O . PRO A 1 194 ? 44.202 -20.345 30.257 1.00 118.83 ? 194 PRO A O 1 ATOM 1560 C CB . PRO A 1 194 ? 44.567 -20.516 33.623 1.00 130.13 ? 194 PRO A CB 1 ATOM 1561 C CG . PRO A 1 194 ? 43.972 -21.589 34.464 1.00 132.61 ? 194 PRO A CG 1 ATOM 1562 C CD . PRO A 1 194 ? 42.495 -21.328 34.462 1.00 131.33 ? 194 PRO A CD 1 ATOM 1563 N N . THR A 1 195 ? 43.678 -22.287 31.281 1.00 127.88 ? 195 THR A N 1 ATOM 1564 C CA . THR A 1 195 ? 44.024 -23.143 30.147 1.00 129.16 ? 195 THR A CA 1 ATOM 1565 C C . THR A 1 195 ? 42.775 -23.853 29.644 1.00 127.36 ? 195 THR A C 1 ATOM 1566 O O . THR A 1 195 ? 42.052 -24.470 30.426 1.00 127.56 ? 195 THR A O 1 ATOM 1567 C CB . THR A 1 195 ? 45.064 -24.199 30.556 1.00 131.81 ? 195 THR A CB 1 ATOM 1568 O OG1 . THR A 1 195 ? 44.668 -24.793 31.798 1.00 133.91 ? 195 THR A OG1 1 ATOM 1569 C CG2 . THR A 1 195 ? 46.442 -23.566 30.721 1.00 131.13 ? 195 THR A CG2 1 ATOM 1570 N N . THR A 1 196 ? 42.528 -23.768 28.340 1.00 123.76 ? 196 THR A N 1 ATOM 1571 C CA . THR A 1 196 ? 41.270 -24.237 27.767 1.00 122.91 ? 196 THR A CA 1 ATOM 1572 C C . THR A 1 196 ? 41.472 -25.004 26.479 1.00 120.75 ? 196 THR A C 1 ATOM 1573 O O . THR A 1 196 ? 42.584 -25.115 25.967 1.00 117.83 ? 196 THR A O 1 ATOM 1574 C CB . THR A 1 196 ? 40.334 -23.057 27.462 1.00 122.62 ? 196 THR A CB 1 ATOM 1575 O OG1 . THR A 1 196 ? 41.070 -22.051 26.760 1.00 121.53 ? 196 THR A OG1 1 ATOM 1576 C CG2 . THR A 1 196 ? 39.765 -22.480 28.745 1.00 124.43 ? 196 THR A CG2 1 ATOM 1577 N N . TYR A 1 197 ? 40.372 -25.531 25.958 1.00 120.33 ? 197 TYR A N 1 ATOM 1578 C CA . TYR A 1 197 ? 40.412 -26.338 24.765 1.00 119.28 ? 197 TYR A CA 1 ATOM 1579 C C . TYR A 1 197 ? 39.046 -26.388 24.104 1.00 120.14 ? 197 TYR A C 1 ATOM 1580 O O . TYR A 1 197 ? 38.036 -26.047 24.717 1.00 120.20 ? 197 TYR A O 1 ATOM 1581 C CB . TYR A 1 197 ? 40.851 -27.756 25.128 1.00 122.85 ? 197 TYR A CB 1 ATOM 1582 C CG . TYR A 1 197 ? 39.815 -28.524 25.920 1.00 125.00 ? 197 TYR A CG 1 ATOM 1583 C CD1 . TYR A 1 197 ? 39.620 -28.282 27.279 1.00 125.02 ? 197 TYR A CD1 1 ATOM 1584 C CD2 . TYR A 1 197 ? 39.023 -29.489 25.305 1.00 126.11 ? 197 TYR A CD2 1 ATOM 1585 C CE1 . TYR A 1 197 ? 38.668 -28.984 28.000 1.00 127.18 ? 197 TYR A CE1 1 ATOM 1586 C CE2 . TYR A 1 197 ? 38.073 -30.195 26.017 1.00 128.96 ? 197 TYR A CE2 1 ATOM 1587 C CZ . TYR A 1 197 ? 37.897 -29.940 27.363 1.00 129.41 ? 197 TYR A CZ 1 ATOM 1588 O OH . TYR A 1 197 ? 36.946 -30.649 28.057 1.00 130.63 ? 197 TYR A OH 1 ATOM 1589 N N . ILE A 1 198 ? 39.038 -26.798 22.840 1.00 120.87 ? 198 ILE A N 1 ATOM 1590 C CA . ILE A 1 198 ? 37.814 -27.129 22.121 1.00 120.04 ? 198 ILE A CA 1 ATOM 1591 C C . ILE A 1 198 ? 38.100 -28.401 21.334 1.00 119.11 ? 198 ILE A C 1 ATOM 1592 O O . ILE A 1 198 ? 39.001 -28.418 20.493 1.00 118.63 ? 198 ILE A O 1 ATOM 1593 C CB . ILE A 1 198 ? 37.401 -26.030 21.120 1.00 120.70 ? 198 ILE A CB 1 ATOM 1594 C CG1 . ILE A 1 198 ? 37.305 -24.662 21.795 1.00 121.44 ? 198 ILE A CG1 1 ATOM 1595 C CG2 . ILE A 1 198 ? 36.064 -26.374 20.477 1.00 122.58 ? 198 ILE A CG2 1 ATOM 1596 C CD1 . ILE A 1 198 ? 37.432 -23.509 20.822 1.00 120.26 ? 198 ILE A CD1 1 ATOM 1597 N N . SER A 1 199 ? 37.349 -29.461 21.610 1.00 116.93 ? 199 SER A N 1 ATOM 1598 C CA . SER A 1 199 ? 37.489 -30.706 20.867 1.00 116.64 ? 199 SER A CA 1 ATOM 1599 C C . SER A 1 199 ? 36.272 -30.902 19.972 1.00 114.24 ? 199 SER A C 1 ATOM 1600 O O . SER A 1 199 ? 35.138 -30.723 20.411 1.00 113.77 ? 199 SER A O 1 ATOM 1601 C CB . SER A 1 199 ? 37.650 -31.889 21.820 1.00 120.71 ? 199 SER A CB 1 ATOM 1602 O OG . SER A 1 199 ? 36.410 -32.263 22.388 1.00 123.06 ? 199 SER A OG 1 ATOM 1603 N N . VAL A 1 200 ? 36.519 -31.265 18.718 1.00 113.28 ? 200 VAL A N 1 ATOM 1604 C CA . VAL A 1 200 ? 35.461 -31.442 17.733 1.00 113.31 ? 200 VAL A CA 1 ATOM 1605 C C . VAL A 1 200 ? 35.631 -32.801 17.085 1.00 116.97 ? 200 VAL A C 1 ATOM 1606 O O . VAL A 1 200 ? 36.717 -33.124 16.591 1.00 117.69 ? 200 VAL A O 1 ATOM 1607 C CB . VAL A 1 200 ? 35.523 -30.367 16.631 1.00 111.61 ? 200 VAL A CB 1 ATOM 1608 C CG1 . VAL A 1 200 ? 34.274 -30.420 15.759 1.00 111.22 ? 200 VAL A CG1 1 ATOM 1609 C CG2 . VAL A 1 200 ? 35.694 -28.983 17.239 1.00 110.58 ? 200 VAL A CG2 1 ATOM 1610 N N . GLY A 1 201 ? 34.556 -33.587 17.073 1.00 120.94 ? 201 GLY A N 1 ATOM 1611 C CA . GLY A 1 201 ? 34.600 -34.947 16.543 1.00 125.17 ? 201 GLY A CA 1 ATOM 1612 C C . GLY A 1 201 ? 33.454 -35.287 15.609 1.00 125.48 ? 201 GLY A C 1 ATOM 1613 O O . GLY A 1 201 ? 32.307 -34.935 15.869 1.00 127.04 ? 201 GLY A O 1 ATOM 1614 N N . THR A 1 202 ? 33.778 -35.959 14.509 1.00 126.35 ? 202 THR A N 1 ATOM 1615 C CA . THR A 1 202 ? 32.782 -36.599 13.650 1.00 127.80 ? 202 THR A CA 1 ATOM 1616 C C . THR A 1 202 ? 33.264 -38.020 13.393 1.00 130.67 ? 202 THR A C 1 ATOM 1617 O O . THR A 1 202 ? 34.103 -38.538 14.133 1.00 130.00 ? 202 THR A O 1 ATOM 1618 C CB . THR A 1 202 ? 32.595 -35.855 12.305 1.00 125.45 ? 202 THR A CB 1 ATOM 1619 O OG1 . THR A 1 202 ? 33.741 -36.054 11.467 1.00 123.23 ? 202 THR A OG1 1 ATOM 1620 C CG2 . THR A 1 202 ? 32.387 -34.376 12.530 1.00 124.55 ? 202 THR A CG2 1 ATOM 1621 N N . SER A 1 203 ? 32.738 -38.652 12.351 1.00 134.37 ? 203 SER A N 1 ATOM 1622 C CA . SER A 1 203 ? 33.219 -39.963 11.949 1.00 138.15 ? 203 SER A CA 1 ATOM 1623 C C . SER A 1 203 ? 34.666 -39.865 11.470 1.00 136.52 ? 203 SER A C 1 ATOM 1624 O O . SER A 1 203 ? 35.486 -40.723 11.790 1.00 138.09 ? 203 SER A O 1 ATOM 1625 C CB . SER A 1 203 ? 32.332 -40.547 10.852 1.00 140.07 ? 203 SER A CB 1 ATOM 1626 O OG . SER A 1 203 ? 32.527 -41.944 10.748 1.00 144.64 ? 203 SER A OG 1 ATOM 1627 N N . THR A 1 204 ? 34.975 -38.808 10.720 1.00 133.46 ? 204 THR A N 1 ATOM 1628 C CA . THR A 1 204 ? 36.323 -38.603 10.180 1.00 132.14 ? 204 THR A CA 1 ATOM 1629 C C . THR A 1 204 ? 37.146 -37.596 10.995 1.00 131.01 ? 204 THR A C 1 ATOM 1630 O O . THR A 1 204 ? 38.336 -37.807 11.217 1.00 134.41 ? 204 THR A O 1 ATOM 1631 C CB . THR A 1 204 ? 36.281 -38.153 8.702 1.00 127.19 ? 204 THR A CB 1 ATOM 1632 O OG1 . THR A 1 204 ? 35.741 -36.829 8.608 1.00 122.50 ? 204 THR A OG1 1 ATOM 1633 C CG2 . THR A 1 204 ? 35.437 -39.116 7.868 1.00 126.10 ? 204 THR A CG2 1 ATOM 1634 N N . LEU A 1 205 ? 36.516 -36.512 11.439 1.00 129.21 ? 205 LEU A N 1 ATOM 1635 C CA . LEU A 1 205 ? 37.226 -35.443 12.147 1.00 126.86 ? 205 LEU A CA 1 ATOM 1636 C C . LEU A 1 205 ? 37.509 -35.778 13.618 1.00 129.47 ? 205 LEU A C 1 ATOM 1637 O O . LEU A 1 205 ? 36.644 -36.307 14.320 1.00 130.84 ? 205 LEU A O 1 ATOM 1638 C CB . LEU A 1 205 ? 36.418 -34.147 12.065 1.00 124.56 ? 205 LEU A CB 1 ATOM 1639 C CG . LEU A 1 205 ? 37.109 -32.876 12.556 1.00 123.23 ? 205 LEU A CG 1 ATOM 1640 C CD1 . LEU A 1 205 ? 38.383 -32.607 11.767 1.00 121.02 ? 205 LEU A CD1 1 ATOM 1641 C CD2 . LEU A 1 205 ? 36.149 -31.702 12.456 1.00 121.51 ? 205 LEU A CD2 1 ATOM 1642 N N . ASN A 1 206 ? 38.720 -35.456 14.076 1.00 129.20 ? 206 ASN A N 1 ATOM 1643 C CA . ASN A 1 206 ? 39.105 -35.617 15.488 1.00 128.12 ? 206 ASN A CA 1 ATOM 1644 C C . ASN A 1 206 ? 40.143 -34.568 15.894 1.00 122.73 ? 206 ASN A C 1 ATOM 1645 O O . ASN A 1 206 ? 41.341 -34.852 15.940 1.00 119.79 ? 206 ASN A O 1 ATOM 1646 C CB . ASN A 1 206 ? 39.647 -37.032 15.735 1.00 130.70 ? 206 ASN A CB 1 ATOM 1647 C CG . ASN A 1 206 ? 40.312 -37.182 17.100 1.00 134.80 ? 206 ASN A CG 1 ATOM 1648 O OD1 . ASN A 1 206 ? 39.718 -36.877 18.139 1.00 132.79 ? 206 ASN A OD1 1 ATOM 1649 N ND2 . ASN A 1 206 ? 41.556 -37.653 17.101 1.00 136.63 ? 206 ASN A ND2 1 ATOM 1650 N N . GLN A 1 207 ? 39.683 -33.355 16.187 1.00 119.72 ? 207 GLN A N 1 ATOM 1651 C CA . GLN A 1 207 ? 40.603 -32.262 16.501 1.00 121.49 ? 207 GLN A CA 1 ATOM 1652 C C . GLN A 1 207 ? 40.471 -31.775 17.936 1.00 120.68 ? 207 GLN A C 1 ATOM 1653 O O . GLN A 1 207 ? 39.503 -32.077 18.633 1.00 119.63 ? 207 GLN A O 1 ATOM 1654 C CB . GLN A 1 207 ? 40.428 -31.090 15.526 1.00 121.30 ? 207 GLN A CB 1 ATOM 1655 C CG . GLN A 1 207 ? 39.124 -30.313 15.675 1.00 122.19 ? 207 GLN A CG 1 ATOM 1656 C CD . GLN A 1 207 ? 39.090 -29.043 14.838 1.00 118.57 ? 207 GLN A CD 1 ATOM 1657 O OE1 . GLN A 1 207 ? 38.580 -28.011 15.277 1.00 117.42 ? 207 GLN A OE1 1 ATOM 1658 N NE2 . GLN A 1 207 ? 39.630 -29.113 13.630 1.00 116.04 ? 207 GLN A NE2 1 ATOM 1659 N N . ARG A 1 208 ? 41.476 -31.017 18.355 1.00 120.00 ? 208 ARG A N 1 ATOM 1660 C CA . ARG A 1 208 ? 41.531 -30.441 19.683 1.00 121.76 ? 208 ARG A CA 1 ATOM 1661 C C . ARG A 1 208 ? 42.275 -29.122 19.575 1.00 121.00 ? 208 ARG A C 1 ATOM 1662 O O . ARG A 1 208 ? 43.503 -29.098 19.513 1.00 122.24 ? 208 ARG A O 1 ATOM 1663 C CB . ARG A 1 208 ? 42.255 -31.383 20.641 1.00 125.55 ? 208 ARG A CB 1 ATOM 1664 C CG . ARG A 1 208 ? 42.290 -30.927 22.090 1.00 127.69 ? 208 ARG A CG 1 ATOM 1665 C CD . ARG A 1 208 ? 43.044 -31.940 22.932 1.00 131.61 ? 208 ARG A CD 1 ATOM 1666 N NE . ARG A 1 208 ? 43.336 -31.453 24.280 1.00 134.68 ? 208 ARG A NE 1 ATOM 1667 C CZ . ARG A 1 208 ? 42.495 -31.498 25.312 1.00 136.83 ? 208 ARG A CZ 1 ATOM 1668 N NH1 . ARG A 1 208 ? 41.268 -31.998 25.184 1.00 138.58 ? 208 ARG A NH1 1 ATOM 1669 N NH2 . ARG A 1 208 ? 42.886 -31.029 26.490 1.00 137.98 ? 208 ARG A NH2 1 ATOM 1670 N N . LEU A 1 209 ? 41.524 -28.029 19.530 1.00 119.85 ? 209 LEU A N 1 ATOM 1671 C CA . LEU A 1 209 ? 42.111 -26.705 19.416 1.00 118.29 ? 209 LEU A CA 1 ATOM 1672 C C . LEU A 1 209 ? 42.439 -26.180 20.811 1.00 118.57 ? 209 LEU A C 1 ATOM 1673 O O . LEU A 1 209 ? 41.661 -26.369 21.744 1.00 116.08 ? 209 LEU A O 1 ATOM 1674 C CB . LEU A 1 209 ? 41.139 -25.752 18.718 1.00 118.37 ? 209 LEU A CB 1 ATOM 1675 C CG . LEU A 1 209 ? 40.541 -26.211 17.383 1.00 119.89 ? 209 LEU A CG 1 ATOM 1676 C CD1 . LEU A 1 209 ? 39.414 -25.278 16.968 1.00 119.68 ? 209 LEU A CD1 1 ATOM 1677 C CD2 . LEU A 1 209 ? 41.603 -26.290 16.296 1.00 118.82 ? 209 LEU A CD2 1 ATOM 1678 N N . VAL A 1 210 ? 43.598 -25.538 20.946 1.00 118.05 ? 210 VAL A N 1 ATOM 1679 C CA . VAL A 1 210 ? 43.958 -24.823 22.170 1.00 119.36 ? 210 VAL A CA 1 ATOM 1680 C C . VAL A 1 210 ? 44.282 -23.373 21.814 1.00 118.35 ? 210 VAL A C 1 ATOM 1681 O O . VAL A 1 210 ? 44.929 -23.117 20.791 1.00 118.80 ? 210 VAL A O 1 ATOM 1682 C CB . VAL A 1 210 ? 45.151 -25.467 22.923 1.00 121.71 ? 210 VAL A CB 1 ATOM 1683 C CG1 . VAL A 1 210 ? 44.730 -26.787 23.548 1.00 123.00 ? 210 VAL A CG1 1 ATOM 1684 C CG2 . VAL A 1 210 ? 46.361 -25.666 22.014 1.00 122.77 ? 210 VAL A CG2 1 ATOM 1685 N N . PRO A 1 211 ? 43.829 -22.415 22.645 1.00 115.70 ? 211 PRO A N 1 ATOM 1686 C CA . PRO A 1 211 ? 44.125 -21.028 22.316 1.00 113.06 ? 211 PRO A CA 1 ATOM 1687 C C . PRO A 1 211 ? 45.590 -20.688 22.547 1.00 112.84 ? 211 PRO A C 1 ATOM 1688 O O . PRO A 1 211 ? 46.141 -21.034 23.587 1.00 114.72 ? 211 PRO A O 1 ATOM 1689 C CB . PRO A 1 211 ? 43.237 -20.224 23.279 1.00 114.42 ? 211 PRO A CB 1 ATOM 1690 C CG . PRO A 1 211 ? 42.370 -21.207 23.983 1.00 115.27 ? 211 PRO A CG 1 ATOM 1691 C CD . PRO A 1 211 ? 43.059 -22.528 23.893 1.00 117.16 ? 211 PRO A CD 1 ATOM 1692 N N . ARG A 1 212 ? 46.217 -20.055 21.561 1.00 112.05 ? 212 ARG A N 1 ATOM 1693 C CA . ARG A 1 212 ? 47.526 -19.454 21.735 1.00 114.62 ? 212 ARG A CA 1 ATOM 1694 C C . ARG A 1 212 ? 47.395 -18.004 22.176 1.00 114.97 ? 212 ARG A C 1 ATOM 1695 O O . ARG A 1 212 ? 46.894 -17.164 21.432 1.00 114.32 ? 212 ARG A O 1 ATOM 1696 C CB . ARG A 1 212 ? 48.328 -19.548 20.442 1.00 114.49 ? 212 ARG A CB 1 ATOM 1697 C CG . ARG A 1 212 ? 48.710 -20.980 20.094 1.00 117.79 ? 212 ARG A CG 1 ATOM 1698 C CD . ARG A 1 212 ? 47.856 -21.531 18.976 1.00 116.03 ? 212 ARG A CD 1 ATOM 1699 N NE . ARG A 1 212 ? 48.195 -20.870 17.723 1.00 112.63 ? 212 ARG A NE 1 ATOM 1700 C CZ . ARG A 1 212 ? 47.474 -20.942 16.615 1.00 111.67 ? 212 ARG A CZ 1 ATOM 1701 N NH1 . ARG A 1 212 ? 46.353 -21.655 16.578 1.00 111.47 ? 212 ARG A NH1 1 ATOM 1702 N NH2 . ARG A 1 212 ? 47.879 -20.292 15.533 1.00 116.03 ? 212 ARG A NH2 1 ATOM 1703 N N . ILE A 1 213 ? 47.856 -17.728 23.393 1.00 118.49 ? 213 ILE A N 1 ATOM 1704 C CA . ILE A 1 213 ? 47.736 -16.410 24.007 1.00 120.03 ? 213 ILE A CA 1 ATOM 1705 C C . ILE A 1 213 ? 49.047 -15.647 23.876 1.00 121.87 ? 213 ILE A C 1 ATOM 1706 O O . ILE A 1 213 ? 50.026 -15.975 24.540 1.00 122.73 ? 213 ILE A O 1 ATOM 1707 C CB . ILE A 1 213 ? 47.368 -16.532 25.498 1.00 121.92 ? 213 ILE A CB 1 ATOM 1708 C CG1 . ILE A 1 213 ? 46.028 -17.266 25.638 1.00 123.22 ? 213 ILE A CG1 1 ATOM 1709 C CG2 . ILE A 1 213 ? 47.322 -15.156 26.156 1.00 123.50 ? 213 ILE A CG2 1 ATOM 1710 C CD1 . ILE A 1 213 ? 45.522 -17.387 27.060 1.00 125.21 ? 213 ILE A CD1 1 ATOM 1711 N N . ALA A 1 214 ? 49.052 -14.620 23.030 1.00 124.39 ? 214 ALA A N 1 ATOM 1712 C CA . ALA A 1 214 ? 50.259 -13.845 22.759 1.00 126.27 ? 214 ALA A CA 1 ATOM 1713 C C . ALA A 1 214 ? 49.952 -12.369 22.517 1.00 130.21 ? 214 ALA A C 1 ATOM 1714 O O . ALA A 1 214 ? 48.823 -11.997 22.180 1.00 131.02 ? 214 ALA A O 1 ATOM 1715 C CB . ALA A 1 214 ? 50.988 -14.429 21.558 1.00 124.37 ? 214 ALA A CB 1 ATOM 1716 N N . THR A 1 215 ? 50.971 -11.533 22.696 1.00 134.14 ? 215 THR A N 1 ATOM 1717 C CA . THR A 1 215 ? 50.883 -10.120 22.341 1.00 135.11 ? 215 THR A CA 1 ATOM 1718 C C . THR A 1 215 ? 50.854 -9.990 20.819 1.00 130.39 ? 215 THR A C 1 ATOM 1719 O O . THR A 1 215 ? 51.671 -10.594 20.121 1.00 134.70 ? 215 THR A O 1 ATOM 1720 C CB . THR A 1 215 ? 52.055 -9.308 22.938 1.00 137.74 ? 215 THR A CB 1 ATOM 1721 O OG1 . THR A 1 215 ? 51.852 -9.154 24.348 1.00 136.64 ? 215 THR A OG1 1 ATOM 1722 C CG2 . THR A 1 215 ? 52.160 -7.918 22.302 1.00 139.77 ? 215 THR A CG2 1 ATOM 1723 N N . ARG A 1 216 ? 49.900 -9.206 20.323 1.00 124.79 ? 216 ARG A N 1 ATOM 1724 C CA . ARG A 1 216 ? 49.705 -9.000 18.889 1.00 120.46 ? 216 ARG A CA 1 ATOM 1725 C C . ARG A 1 216 ? 49.557 -7.519 18.551 1.00 120.27 ? 216 ARG A C 1 ATOM 1726 O O . ARG A 1 216 ? 49.278 -6.691 19.419 1.00 123.32 ? 216 ARG A O 1 ATOM 1727 C CB . ARG A 1 216 ? 48.440 -9.728 18.419 1.00 117.42 ? 216 ARG A CB 1 ATOM 1728 C CG . ARG A 1 216 ? 48.656 -10.956 17.541 1.00 114.78 ? 216 ARG A CG 1 ATOM 1729 C CD . ARG A 1 216 ? 48.544 -12.266 18.300 1.00 115.30 ? 216 ARG A CD 1 ATOM 1730 N NE . ARG A 1 216 ? 47.377 -12.309 19.180 1.00 115.08 ? 216 ARG A NE 1 ATOM 1731 C CZ . ARG A 1 216 ? 47.041 -13.355 19.930 1.00 114.20 ? 216 ARG A CZ 1 ATOM 1732 N NH1 . ARG A 1 216 ? 47.757 -14.477 19.897 1.00 115.64 ? 216 ARG A NH1 1 ATOM 1733 N NH2 . ARG A 1 216 ? 45.969 -13.283 20.707 1.00 112.47 ? 216 ARG A NH2 1 ATOM 1734 N N . SER A 1 217 ? 49.735 -7.205 17.272 1.00 121.70 ? 217 SER A N 1 ATOM 1735 C CA . SER A 1 217 ? 49.413 -5.887 16.735 1.00 120.54 ? 217 SER A CA 1 ATOM 1736 C C . SER A 1 217 ? 47.890 -5.728 16.697 1.00 119.11 ? 217 SER A C 1 ATOM 1737 O O . SER A 1 217 ? 47.167 -6.698 16.465 1.00 117.31 ? 217 SER A O 1 ATOM 1738 C CB . SER A 1 217 ? 49.972 -5.737 15.311 1.00 121.05 ? 217 SER A CB 1 ATOM 1739 O OG . SER A 1 217 ? 51.029 -6.648 15.055 1.00 119.36 ? 217 SER A OG 1 ATOM 1740 N N . LYS A 1 218 ? 47.400 -4.513 16.918 1.00 118.38 ? 218 LYS A N 1 ATOM 1741 C CA . LYS A 1 218 ? 45.975 -4.239 16.742 1.00 116.49 ? 218 LYS A CA 1 ATOM 1742 C C . LYS A 1 218 ? 45.612 -4.257 15.263 1.00 115.23 ? 218 LYS A C 1 ATOM 1743 O O . LYS A 1 218 ? 46.374 -3.786 14.422 1.00 115.26 ? 218 LYS A O 1 ATOM 1744 C CB . LYS A 1 218 ? 45.583 -2.896 17.355 1.00 116.15 ? 218 LYS A CB 1 ATOM 1745 C CG . LYS A 1 218 ? 45.503 -2.933 18.866 1.00 118.16 ? 218 LYS A CG 1 ATOM 1746 C CD . LYS A 1 218 ? 44.996 -1.624 19.450 1.00 120.25 ? 218 LYS A CD 1 ATOM 1747 C CE . LYS A 1 218 ? 45.036 -1.668 20.972 1.00 123.37 ? 218 LYS A CE 1 ATOM 1748 N NZ . LYS A 1 218 ? 44.551 -0.414 21.616 1.00 124.80 ? 218 LYS A NZ 1 ATOM 1749 N N . VAL A 1 219 ? 44.459 -4.837 14.955 1.00 112.94 ? 219 VAL A N 1 ATOM 1750 C CA . VAL A 1 219 ? 43.882 -4.773 13.619 1.00 109.48 ? 219 VAL A CA 1 ATOM 1751 C C . VAL A 1 219 ? 42.398 -4.547 13.819 1.00 107.64 ? 219 VAL A C 1 ATOM 1752 O O . VAL A 1 219 ? 41.742 -5.326 14.502 1.00 106.34 ? 219 VAL A O 1 ATOM 1753 C CB . VAL A 1 219 ? 44.105 -6.072 12.835 1.00 109.48 ? 219 VAL A CB 1 ATOM 1754 C CG1 . VAL A 1 219 ? 43.493 -5.960 11.445 1.00 110.60 ? 219 VAL A CG1 1 ATOM 1755 C CG2 . VAL A 1 219 ? 45.590 -6.396 12.756 1.00 108.81 ? 219 VAL A CG2 1 ATOM 1756 N N . ASN A 1 220 ? 41.879 -3.470 13.242 1.00 109.03 ? 220 ASN A N 1 ATOM 1757 C CA . ASN A 1 220 ? 40.565 -2.949 13.619 1.00 109.68 ? 220 ASN A CA 1 ATOM 1758 C C . ASN A 1 220 ? 40.447 -2.825 15.139 1.00 105.12 ? 220 ASN A C 1 ATOM 1759 O O . ASN A 1 220 ? 39.396 -3.096 15.718 1.00 105.27 ? 220 ASN A O 1 ATOM 1760 C CB . ASN A 1 220 ? 39.440 -3.818 13.047 1.00 113.78 ? 220 ASN A CB 1 ATOM 1761 C CG . ASN A 1 220 ? 39.607 -4.080 11.563 1.00 118.39 ? 220 ASN A CG 1 ATOM 1762 O OD1 . ASN A 1 220 ? 39.557 -5.225 11.114 1.00 124.80 ? 220 ASN A OD1 1 ATOM 1763 N ND2 . ASN A 1 220 ? 39.825 -3.020 10.795 1.00 119.76 ? 220 ASN A ND2 1 ATOM 1764 N N . GLY A 1 221 ? 41.544 -2.417 15.771 1.00 105.84 ? 221 GLY A N 1 ATOM 1765 C CA . GLY A 1 221 ? 41.576 -2.174 17.210 1.00 105.89 ? 221 GLY A CA 1 ATOM 1766 C C . GLY A 1 221 ? 41.456 -3.403 18.091 1.00 103.12 ? 221 GLY A C 1 ATOM 1767 O O . GLY A 1 221 ? 41.012 -3.292 19.226 1.00 104.81 ? 221 GLY A O 1 ATOM 1768 N N . GLN A 1 222 ? 41.860 -4.567 17.587 1.00 102.12 ? 222 GLN A N 1 ATOM 1769 C CA . GLN A 1 222 ? 41.760 -5.808 18.354 1.00 102.94 ? 222 GLN A CA 1 ATOM 1770 C C . GLN A 1 222 ? 43.099 -6.506 18.500 1.00 103.11 ? 222 GLN A C 1 ATOM 1771 O O . GLN A 1 222 ? 43.794 -6.728 17.515 1.00 103.24 ? 222 GLN A O 1 ATOM 1772 C CB . GLN A 1 222 ? 40.778 -6.769 17.688 1.00 103.38 ? 222 GLN A CB 1 ATOM 1773 C CG . GLN A 1 222 ? 39.393 -6.192 17.454 1.00 102.99 ? 222 GLN A CG 1 ATOM 1774 C CD . GLN A 1 222 ? 38.803 -5.570 18.699 1.00 103.78 ? 222 GLN A CD 1 ATOM 1775 O OE1 . GLN A 1 222 ? 38.924 -6.116 19.797 1.00 104.76 ? 222 GLN A OE1 1 ATOM 1776 N NE2 . GLN A 1 222 ? 38.160 -4.420 18.536 1.00 105.21 ? 222 GLN A NE2 1 ATOM 1777 N N . ASN A 1 223 ? 43.437 -6.863 19.735 1.00 105.34 ? 223 ASN A N 1 ATOM 1778 C CA . ASN A 1 223 ? 44.650 -7.621 20.034 1.00 108.33 ? 223 ASN A CA 1 ATOM 1779 C C . ASN A 1 223 ? 44.420 -9.113 19.932 1.00 107.39 ? 223 ASN A C 1 ATOM 1780 O O . ASN A 1 223 ? 45.357 -9.881 19.717 1.00 109.03 ? 223 ASN A O 1 ATOM 1781 C CB . ASN A 1 223 ? 45.119 -7.312 21.443 1.00 113.80 ? 223 ASN A CB 1 ATOM 1782 C CG . ASN A 1 223 ? 45.467 -5.859 21.626 1.00 117.53 ? 223 ASN A CG 1 ATOM 1783 O OD1 . ASN A 1 223 ? 46.182 -5.281 20.809 1.00 119.50 ? 223 ASN A OD1 1 ATOM 1784 N ND2 . ASN A 1 223 ? 44.963 -5.255 22.697 1.00 119.92 ? 223 ASN A ND2 1 ATOM 1785 N N . GLY A 1 224 ? 43.170 -9.521 20.124 1.00 105.46 ? 224 GLY A N 1 ATOM 1786 C CA . GLY A 1 224 ? 42.790 -10.915 19.993 1.00 103.84 ? 224 GLY A CA 1 ATOM 1787 C C . GLY A 1 224 ? 42.747 -11.367 18.545 1.00 99.70 ? 224 GLY A C 1 ATOM 1788 O O . GLY A 1 224 ? 42.904 -10.566 17.623 1.00 94.65 ? 224 GLY A O 1 ATOM 1789 N N . ARG A 1 225 ? 42.549 -12.666 18.357 1.00 99.18 ? 225 ARG A N 1 ATOM 1790 C CA . ARG A 1 225 ? 42.379 -13.245 17.036 1.00 100.09 ? 225 ARG A CA 1 ATOM 1791 C C . ARG A 1 225 ? 41.318 -14.333 17.092 1.00 99.61 ? 225 ARG A C 1 ATOM 1792 O O . ARG A 1 225 ? 41.152 -14.992 18.107 1.00 100.77 ? 225 ARG A O 1 ATOM 1793 C CB . ARG A 1 225 ? 43.694 -13.841 16.521 1.00 99.53 ? 225 ARG A CB 1 ATOM 1794 C CG . ARG A 1 225 ? 44.824 -12.845 16.300 1.00 99.17 ? 225 ARG A CG 1 ATOM 1795 C CD . ARG A 1 225 ? 44.649 -12.053 15.019 1.00 99.52 ? 225 ARG A CD 1 ATOM 1796 N NE . ARG A 1 225 ? 45.736 -11.093 14.825 1.00 100.50 ? 225 ARG A NE 1 ATOM 1797 C CZ . ARG A 1 225 ? 45.776 -9.862 15.336 1.00 101.52 ? 225 ARG A CZ 1 ATOM 1798 N NH1 . ARG A 1 225 ? 44.788 -9.395 16.094 1.00 102.91 ? 225 ARG A NH1 1 ATOM 1799 N NH2 . ARG A 1 225 ? 46.825 -9.089 15.090 1.00 102.82 ? 225 ARG A NH2 1 ATOM 1800 N N . MET A 1 226 ? 40.605 -14.511 15.989 1.00 100.69 ? 226 MET A N 1 ATOM 1801 C CA . MET A 1 226 ? 39.654 -15.593 15.852 1.00 102.88 ? 226 MET A CA 1 ATOM 1802 C C . MET A 1 226 ? 40.134 -16.495 14.728 1.00 102.38 ? 226 MET A C 1 ATOM 1803 O O . MET A 1 226 ? 40.433 -16.015 13.645 1.00 102.79 ? 226 MET A O 1 ATOM 1804 C CB . MET A 1 226 ? 38.281 -15.032 15.506 1.00 104.97 ? 226 MET A CB 1 ATOM 1805 C CG . MET A 1 226 ? 37.737 -14.042 16.524 1.00 106.85 ? 226 MET A CG 1 ATOM 1806 S SD . MET A 1 226 ? 36.735 -14.803 17.808 1.00 110.08 ? 226 MET A SD 1 ATOM 1807 C CE . MET A 1 226 ? 36.143 -13.349 18.669 1.00 110.46 ? 226 MET A CE 1 ATOM 1808 N N . GLU A 1 227 ? 40.227 -17.795 14.993 1.00 103.64 ? 227 GLU A N 1 ATOM 1809 C CA . GLU A 1 227 ? 40.551 -18.783 13.967 1.00 101.56 ? 227 GLU A CA 1 ATOM 1810 C C . GLU A 1 227 ? 39.294 -19.554 13.657 1.00 99.63 ? 227 GLU A C 1 ATOM 1811 O O . GLU A 1 227 ? 38.718 -20.168 14.551 1.00 103.14 ? 227 GLU A O 1 ATOM 1812 C CB . GLU A 1 227 ? 41.615 -19.767 14.453 1.00 105.68 ? 227 GLU A CB 1 ATOM 1813 C CG . GLU A 1 227 ? 43.030 -19.432 14.025 1.00 110.97 ? 227 GLU A CG 1 ATOM 1814 C CD . GLU A 1 227 ? 43.910 -20.663 13.938 1.00 116.93 ? 227 GLU A CD 1 ATOM 1815 O OE1 . GLU A 1 227 ? 43.531 -21.610 13.217 1.00 122.73 ? 227 GLU A OE1 1 ATOM 1816 O OE2 . GLU A 1 227 ? 44.982 -20.682 14.576 1.00 118.87 ? 227 GLU A OE2 1 ATOM 1817 N N . PHE A 1 228 ? 38.869 -19.532 12.399 1.00 95.21 ? 228 PHE A N 1 ATOM 1818 C CA . PHE A 1 228 ? 37.653 -20.228 12.013 1.00 93.06 ? 228 PHE A CA 1 ATOM 1819 C C . PHE A 1 228 ? 37.957 -21.523 11.284 1.00 92.50 ? 228 PHE A C 1 ATOM 1820 O O . PHE A 1 228 ? 38.884 -21.598 10.478 1.00 92.08 ? 228 PHE A O 1 ATOM 1821 C CB . PHE A 1 228 ? 36.765 -19.315 11.183 1.00 93.20 ? 228 PHE A CB 1 ATOM 1822 C CG . PHE A 1 228 ? 36.211 -18.168 11.970 1.00 95.80 ? 228 PHE A CG 1 ATOM 1823 C CD1 . PHE A 1 228 ? 35.072 -18.330 12.742 1.00 97.50 ? 228 PHE A CD1 1 ATOM 1824 C CD2 . PHE A 1 228 ? 36.854 -16.937 11.979 1.00 96.43 ? 228 PHE A CD2 1 ATOM 1825 C CE1 . PHE A 1 228 ? 34.570 -17.277 13.491 1.00 97.64 ? 228 PHE A CE1 1 ATOM 1826 C CE2 . PHE A 1 228 ? 36.356 -15.881 12.725 1.00 95.66 ? 228 PHE A CE2 1 ATOM 1827 C CZ . PHE A 1 228 ? 35.214 -16.052 13.482 1.00 95.26 ? 228 PHE A CZ 1 ATOM 1828 N N . PHE A 1 229 ? 37.169 -22.545 11.602 1.00 93.15 ? 229 PHE A N 1 ATOM 1829 C CA . PHE A 1 229 ? 37.322 -23.868 11.027 1.00 94.67 ? 229 PHE A CA 1 ATOM 1830 C C . PHE A 1 229 ? 36.018 -24.309 10.421 1.00 95.20 ? 229 PHE A C 1 ATOM 1831 O O . PHE A 1 229 ? 34.968 -23.730 10.695 1.00 92.44 ? 229 PHE A O 1 ATOM 1832 C CB . PHE A 1 229 ? 37.731 -24.865 12.097 1.00 96.36 ? 229 PHE A CB 1 ATOM 1833 C CG . PHE A 1 229 ? 39.096 -24.628 12.627 1.00 99.11 ? 229 PHE A CG 1 ATOM 1834 C CD1 . PHE A 1 229 ? 39.307 -23.682 13.620 1.00 100.22 ? 229 PHE A CD1 1 ATOM 1835 C CD2 . PHE A 1 229 ? 40.181 -25.326 12.116 1.00 102.16 ? 229 PHE A CD2 1 ATOM 1836 C CE1 . PHE A 1 229 ? 40.578 -23.444 14.108 1.00 102.57 ? 229 PHE A CE1 1 ATOM 1837 C CE2 . PHE A 1 229 ? 41.456 -25.095 12.600 1.00 104.90 ? 229 PHE A CE2 1 ATOM 1838 C CZ . PHE A 1 229 ? 41.656 -24.152 13.598 1.00 103.87 ? 229 PHE A CZ 1 ATOM 1839 N N . TRP A 1 230 ? 36.094 -25.347 9.598 1.00 97.02 ? 230 TRP A N 1 ATOM 1840 C CA . TRP A 1 230 ? 34.902 -25.905 8.991 1.00 96.96 ? 230 TRP A CA 1 ATOM 1841 C C . TRP A 1 230 ? 35.021 -27.400 8.767 1.00 96.69 ? 230 TRP A C 1 ATOM 1842 O O . TRP A 1 230 ? 36.096 -27.979 8.880 1.00 96.96 ? 230 TRP A O 1 ATOM 1843 C CB . TRP A 1 230 ? 34.618 -25.206 7.670 1.00 94.86 ? 230 TRP A CB 1 ATOM 1844 C CG . TRP A 1 230 ? 35.716 -25.338 6.672 1.00 95.67 ? 230 TRP A CG 1 ATOM 1845 C CD1 . TRP A 1 230 ? 36.775 -24.501 6.511 1.00 94.95 ? 230 TRP A CD1 1 ATOM 1846 C CD2 . TRP A 1 230 ? 35.859 -26.362 5.686 1.00 95.17 ? 230 TRP A CD2 1 ATOM 1847 N NE1 . TRP A 1 230 ? 37.569 -24.936 5.483 1.00 93.45 ? 230 TRP A NE1 1 ATOM 1848 C CE2 . TRP A 1 230 ? 37.029 -26.080 4.961 1.00 94.64 ? 230 TRP A CE2 1 ATOM 1849 C CE3 . TRP A 1 230 ? 35.108 -27.491 5.345 1.00 97.12 ? 230 TRP A CE3 1 ATOM 1850 C CZ2 . TRP A 1 230 ? 37.470 -26.885 3.914 1.00 95.93 ? 230 TRP A CZ2 1 ATOM 1851 C CZ3 . TRP A 1 230 ? 35.544 -28.289 4.307 1.00 98.78 ? 230 TRP A CZ3 1 ATOM 1852 C CH2 . TRP A 1 230 ? 36.716 -27.983 3.602 1.00 97.37 ? 230 TRP A CH2 1 ATOM 1853 N N . THR A 1 231 ? 33.888 -28.017 8.472 1.00 97.04 ? 231 THR A N 1 ATOM 1854 C CA . THR A 1 231 ? 33.861 -29.389 8.016 1.00 98.95 ? 231 THR A CA 1 ATOM 1855 C C . THR A 1 231 ? 32.548 -29.619 7.294 1.00 100.08 ? 231 THR A C 1 ATOM 1856 O O . THR A 1 231 ? 31.598 -28.857 7.474 1.00 100.88 ? 231 THR A O 1 ATOM 1857 C CB . THR A 1 231 ? 34.013 -30.385 9.179 1.00 100.94 ? 231 THR A CB 1 ATOM 1858 O OG1 . THR A 1 231 ? 34.417 -31.658 8.669 1.00 104.38 ? 231 THR A OG1 1 ATOM 1859 C CG2 . THR A 1 231 ? 32.708 -30.538 9.962 1.00 102.50 ? 231 THR A CG2 1 ATOM 1860 N N . ILE A 1 232 ? 32.511 -30.653 6.464 1.00 102.80 ? 232 ILE A N 1 ATOM 1861 C CA . ILE A 1 232 ? 31.272 -31.091 5.842 1.00 105.47 ? 232 ILE A CA 1 ATOM 1862 C C . ILE A 1 232 ? 30.757 -32.259 6.656 1.00 108.03 ? 232 ILE A C 1 ATOM 1863 O O . ILE A 1 232 ? 31.446 -33.263 6.822 1.00 109.27 ? 232 ILE A O 1 ATOM 1864 C CB . ILE A 1 232 ? 31.465 -31.483 4.359 1.00 104.98 ? 232 ILE A CB 1 ATOM 1865 C CG1 . ILE A 1 232 ? 31.091 -30.309 3.454 1.00 103.98 ? 232 ILE A CG1 1 ATOM 1866 C CG2 . ILE A 1 232 ? 30.598 -32.680 3.970 1.00 107.03 ? 232 ILE A CG2 1 ATOM 1867 C CD1 . ILE A 1 232 ? 31.942 -29.080 3.660 1.00 104.71 ? 232 ILE A CD1 1 ATOM 1868 N N . LEU A 1 233 ? 29.544 -32.114 7.169 1.00 111.48 ? 233 LEU A N 1 ATOM 1869 C CA . LEU A 1 233 ? 28.922 -33.154 7.963 1.00 114.62 ? 233 LEU A CA 1 ATOM 1870 C C . LEU A 1 233 ? 28.078 -34.000 7.024 1.00 117.10 ? 233 LEU A C 1 ATOM 1871 O O . LEU A 1 233 ? 27.096 -33.515 6.456 1.00 117.05 ? 233 LEU A O 1 ATOM 1872 C CB . LEU A 1 233 ? 28.068 -32.523 9.069 1.00 115.42 ? 233 LEU A CB 1 ATOM 1873 C CG . LEU A 1 233 ? 27.578 -33.403 10.224 1.00 116.55 ? 233 LEU A CG 1 ATOM 1874 C CD1 . LEU A 1 233 ? 28.737 -33.977 11.025 1.00 116.30 ? 233 LEU A CD1 1 ATOM 1875 C CD2 . LEU A 1 233 ? 26.656 -32.594 11.122 1.00 115.87 ? 233 LEU A CD2 1 ATOM 1876 N N . LYS A 1 234 ? 28.480 -35.253 6.836 1.00 120.27 ? 234 LYS A N 1 ATOM 1877 C CA . LYS A 1 234 ? 27.728 -36.175 5.988 1.00 126.58 ? 234 LYS A CA 1 ATOM 1878 C C . LYS A 1 234 ? 26.344 -36.450 6.583 1.00 129.95 ? 234 LYS A C 1 ATOM 1879 O O . LYS A 1 234 ? 26.153 -36.311 7.794 1.00 131.50 ? 234 LYS A O 1 ATOM 1880 C CB . LYS A 1 234 ? 28.485 -37.497 5.806 1.00 131.17 ? 234 LYS A CB 1 ATOM 1881 C CG . LYS A 1 234 ? 29.275 -37.603 4.511 1.00 131.95 ? 234 LYS A CG 1 ATOM 1882 C CD . LYS A 1 234 ? 29.857 -39.004 4.342 1.00 138.41 ? 234 LYS A CD 1 ATOM 1883 C CE . LYS A 1 234 ? 29.457 -39.657 3.019 1.00 140.54 ? 234 LYS A CE 1 ATOM 1884 N NZ . LYS A 1 234 ? 30.066 -38.999 1.829 1.00 139.35 ? 234 LYS A NZ 1 ATOM 1885 N N . PRO A 1 235 ? 25.372 -36.842 5.735 1.00 131.20 ? 235 PRO A N 1 ATOM 1886 C CA . PRO A 1 235 ? 24.035 -37.130 6.256 1.00 129.02 ? 235 PRO A CA 1 ATOM 1887 C C . PRO A 1 235 ? 24.063 -38.273 7.253 1.00 130.42 ? 235 PRO A C 1 ATOM 1888 O O . PRO A 1 235 ? 24.841 -39.208 7.095 1.00 128.91 ? 235 PRO A O 1 ATOM 1889 C CB . PRO A 1 235 ? 23.242 -37.517 5.004 1.00 129.29 ? 235 PRO A CB 1 ATOM 1890 C CG . PRO A 1 235 ? 24.266 -37.959 4.016 1.00 127.89 ? 235 PRO A CG 1 ATOM 1891 C CD . PRO A 1 235 ? 25.469 -37.112 4.289 1.00 126.72 ? 235 PRO A CD 1 ATOM 1892 N N . ASN A 1 236 ? 23.240 -38.170 8.291 1.00 136.59 ? 236 ASN A N 1 ATOM 1893 C CA . ASN A 1 236 ? 23.101 -39.221 9.299 1.00 139.92 ? 236 ASN A CA 1 ATOM 1894 C C . ASN A 1 236 ? 24.349 -39.389 10.180 1.00 139.47 ? 236 ASN A C 1 ATOM 1895 O O . ASN A 1 236 ? 24.518 -40.414 10.837 1.00 140.50 ? 236 ASN A O 1 ATOM 1896 C CB . ASN A 1 236 ? 22.730 -40.552 8.619 1.00 143.44 ? 236 ASN A CB 1 ATOM 1897 C CG . ASN A 1 236 ? 21.804 -41.410 9.461 1.00 152.35 ? 236 ASN A CG 1 ATOM 1898 O OD1 . ASN A 1 236 ? 21.260 -40.963 10.472 1.00 156.38 ? 236 ASN A OD1 1 ATOM 1899 N ND2 . ASN A 1 236 ? 21.607 -42.652 9.036 1.00 157.34 ? 236 ASN A ND2 1 ATOM 1900 N N . ASP A 1 237 ? 25.211 -38.373 10.194 1.00 138.18 ? 237 ASP A N 1 ATOM 1901 C CA . ASP A 1 237 ? 26.412 -38.363 11.031 1.00 138.37 ? 237 ASP A CA 1 ATOM 1902 C C . ASP A 1 237 ? 26.309 -37.195 12.009 1.00 134.61 ? 237 ASP A C 1 ATOM 1903 O O . ASP A 1 237 ? 25.667 -36.188 11.712 1.00 131.97 ? 237 ASP A O 1 ATOM 1904 C CB . ASP A 1 237 ? 27.667 -38.227 10.160 1.00 138.10 ? 237 ASP A CB 1 ATOM 1905 C CG . ASP A 1 237 ? 28.962 -38.381 10.951 1.00 138.65 ? 237 ASP A CG 1 ATOM 1906 O OD1 . ASP A 1 237 ? 28.962 -39.076 11.991 1.00 141.55 ? 237 ASP A OD1 1 ATOM 1907 O OD2 . ASP A 1 237 ? 29.986 -37.809 10.520 1.00 136.36 ? 237 ASP A OD2 1 ATOM 1908 N N . ALA A 1 238 ? 26.943 -37.328 13.170 1.00 133.74 ? 238 ALA A N 1 ATOM 1909 C CA . ALA A 1 238 ? 26.799 -36.344 14.239 1.00 131.20 ? 238 ALA A CA 1 ATOM 1910 C C . ALA A 1 238 ? 28.135 -35.699 14.586 1.00 127.22 ? 238 ALA A C 1 ATOM 1911 O O . ALA A 1 238 ? 29.177 -36.358 14.555 1.00 128.32 ? 238 ALA A O 1 ATOM 1912 C CB . ALA A 1 238 ? 26.188 -36.993 15.471 1.00 132.80 ? 238 ALA A CB 1 ATOM 1913 N N . ILE A 1 239 ? 28.087 -34.409 14.917 1.00 123.26 ? 239 ILE A N 1 ATOM 1914 C CA . ILE A 1 239 ? 29.275 -33.650 15.323 1.00 120.66 ? 239 ILE A CA 1 ATOM 1915 C C . ILE A 1 239 ? 29.248 -33.337 16.834 1.00 121.11 ? 239 ILE A C 1 ATOM 1916 O O . ILE A 1 239 ? 28.250 -32.845 17.355 1.00 118.66 ? 239 ILE A O 1 ATOM 1917 C CB . ILE A 1 239 ? 29.435 -32.356 14.486 1.00 116.99 ? 239 ILE A CB 1 ATOM 1918 C CG1 . ILE A 1 239 ? 30.809 -31.726 14.737 1.00 115.23 ? 239 ILE A CG1 1 ATOM 1919 C CG2 . ILE A 1 239 ? 28.321 -31.351 14.772 1.00 116.96 ? 239 ILE A CG2 1 ATOM 1920 C CD1 . ILE A 1 239 ? 31.139 -30.587 13.799 1.00 111.42 ? 239 ILE A CD1 1 ATOM 1921 N N . ASN A 1 240 ? 30.357 -33.626 17.516 1.00 120.84 ? 240 ASN A N 1 ATOM 1922 C CA . ASN A 1 240 ? 30.455 -33.510 18.970 1.00 122.95 ? 240 ASN A CA 1 ATOM 1923 C C . ASN A 1 240 ? 31.368 -32.370 19.386 1.00 119.93 ? 240 ASN A C 1 ATOM 1924 O O . ASN A 1 240 ? 32.554 -32.392 19.084 1.00 121.12 ? 240 ASN A O 1 ATOM 1925 C CB . ASN A 1 240 ? 31.008 -34.808 19.554 1.00 127.40 ? 240 ASN A CB 1 ATOM 1926 C CG . ASN A 1 240 ? 30.240 -36.024 19.088 1.00 132.35 ? 240 ASN A CG 1 ATOM 1927 O OD1 . ASN A 1 240 ? 29.138 -36.286 19.563 1.00 135.03 ? 240 ASN A OD1 1 ATOM 1928 N ND2 . ASN A 1 240 ? 30.818 -36.774 18.151 1.00 133.77 ? 240 ASN A ND2 1 ATOM 1929 N N . PHE A 1 241 ? 30.820 -31.386 20.090 1.00 120.05 ? 241 PHE A N 1 ATOM 1930 C CA . PHE A 1 241 ? 31.615 -30.277 20.609 1.00 119.26 ? 241 PHE A CA 1 ATOM 1931 C C . PHE A 1 241 ? 31.846 -30.426 22.103 1.00 123.34 ? 241 PHE A C 1 ATOM 1932 O O . PHE A 1 241 ? 30.896 -30.602 22.866 1.00 124.45 ? 241 PHE A O 1 ATOM 1933 C CB . PHE A 1 241 ? 30.916 -28.948 20.343 1.00 116.82 ? 241 PHE A CB 1 ATOM 1934 C CG . PHE A 1 241 ? 30.857 -28.582 18.896 1.00 115.81 ? 241 PHE A CG 1 ATOM 1935 C CD1 . PHE A 1 241 ? 32.008 -28.198 18.221 1.00 115.20 ? 241 PHE A CD1 1 ATOM 1936 C CD2 . PHE A 1 241 ? 29.661 -28.633 18.199 1.00 116.66 ? 241 PHE A CD2 1 ATOM 1937 C CE1 . PHE A 1 241 ? 31.967 -27.862 16.879 1.00 112.34 ? 241 PHE A CE1 1 ATOM 1938 C CE2 . PHE A 1 241 ? 29.614 -28.300 16.855 1.00 114.49 ? 241 PHE A CE2 1 ATOM 1939 C CZ . PHE A 1 241 ? 30.767 -27.912 16.196 1.00 111.76 ? 241 PHE A CZ 1 ATOM 1940 N N . GLU A 1 242 ? 33.110 -30.365 22.510 1.00 126.48 ? 242 GLU A N 1 ATOM 1941 C CA . GLU A 1 242 ? 33.466 -30.294 23.921 1.00 133.27 ? 242 GLU A CA 1 ATOM 1942 C C . GLU A 1 242 ? 34.399 -29.101 24.109 1.00 129.72 ? 242 GLU A C 1 ATOM 1943 O O . GLU A 1 242 ? 35.372 -28.956 23.368 1.00 129.38 ? 242 GLU A O 1 ATOM 1944 C CB . GLU A 1 242 ? 34.146 -31.589 24.395 1.00 140.80 ? 242 GLU A CB 1 ATOM 1945 C CG . GLU A 1 242 ? 33.672 -32.068 25.765 1.00 149.14 ? 242 GLU A CG 1 ATOM 1946 C CD . GLU A 1 242 ? 34.695 -32.913 26.517 1.00 153.61 ? 242 GLU A CD 1 ATOM 1947 O OE1 . GLU A 1 242 ? 35.850 -32.464 26.676 1.00 153.62 ? 242 GLU A OE1 1 ATOM 1948 O OE2 . GLU A 1 242 ? 34.334 -34.019 26.979 1.00 154.43 ? 242 GLU A OE2 1 ATOM 1949 N N . SER A 1 243 ? 34.100 -28.246 25.085 1.00 127.54 ? 243 SER A N 1 ATOM 1950 C CA . SER A 1 243 ? 34.954 -27.091 25.367 1.00 124.36 ? 243 SER A CA 1 ATOM 1951 C C . SER A 1 243 ? 34.739 -26.516 26.759 1.00 124.11 ? 243 SER A C 1 ATOM 1952 O O . SER A 1 243 ? 33.654 -26.636 27.325 1.00 127.01 ? 243 SER A O 1 ATOM 1953 C CB . SER A 1 243 ? 34.718 -25.992 24.334 1.00 121.51 ? 243 SER A CB 1 ATOM 1954 O OG . SER A 1 243 ? 35.453 -24.828 24.663 1.00 120.12 ? 243 SER A OG 1 ATOM 1955 N N . ASN A 1 244 ? 35.782 -25.882 27.292 1.00 122.20 ? 244 ASN A N 1 ATOM 1956 C CA . ASN A 1 244 ? 35.712 -25.188 28.580 1.00 122.69 ? 244 ASN A CA 1 ATOM 1957 C C . ASN A 1 244 ? 36.101 -23.710 28.471 1.00 121.09 ? 244 ASN A C 1 ATOM 1958 O O . ASN A 1 244 ? 36.464 -23.087 29.467 1.00 120.97 ? 244 ASN A O 1 ATOM 1959 C CB . ASN A 1 244 ? 36.598 -25.894 29.614 1.00 123.65 ? 244 ASN A CB 1 ATOM 1960 C CG . ASN A 1 244 ? 38.071 -25.854 29.254 1.00 123.33 ? 244 ASN A CG 1 ATOM 1961 O OD1 . ASN A 1 244 ? 38.444 -25.497 28.133 1.00 123.16 ? 244 ASN A OD1 1 ATOM 1962 N ND2 . ASN A 1 244 ? 38.918 -26.231 30.203 1.00 122.55 ? 244 ASN A ND2 1 ATOM 1963 N N . GLY A 1 245 ? 36.021 -23.155 27.262 1.00 121.18 ? 245 GLY A N 1 ATOM 1964 C CA . GLY A 1 245 ? 36.320 -21.743 27.041 1.00 119.28 ? 245 GLY A CA 1 ATOM 1965 C C . GLY A 1 245 ? 36.797 -21.443 25.639 1.00 115.51 ? 245 GLY A C 1 ATOM 1966 O O . GLY A 1 245 ? 37.201 -22.347 24.913 1.00 120.07 ? 245 GLY A O 1 ATOM 1967 N N . ASN A 1 246 ? 36.748 -20.163 25.271 1.00 114.25 ? 246 ASN A N 1 ATOM 1968 C CA . ASN A 1 246 ? 37.253 -19.661 23.980 1.00 112.28 ? 246 ASN A CA 1 ATOM 1969 C C . ASN A 1 246 ? 36.466 -20.137 22.756 1.00 110.11 ? 246 ASN A C 1 ATOM 1970 O O . ASN A 1 246 ? 36.878 -19.903 21.624 1.00 108.14 ? 246 ASN A O 1 ATOM 1971 C CB . ASN A 1 246 ? 38.743 -20.001 23.800 1.00 112.00 ? 246 ASN A CB 1 ATOM 1972 C CG . ASN A 1 246 ? 39.622 -19.348 24.849 1.00 111.43 ? 246 ASN A CG 1 ATOM 1973 O OD1 . ASN A 1 246 ? 40.029 -18.200 24.703 1.00 109.82 ? 246 ASN A OD1 1 ATOM 1974 N ND2 . ASN A 1 246 ? 39.932 -20.085 25.900 1.00 112.36 ? 246 ASN A ND2 1 ATOM 1975 N N . PHE A 1 247 ? 35.318 -20.764 22.986 1.00 111.23 ? 247 PHE A N 1 ATOM 1976 C CA . PHE A 1 247 ? 34.594 -21.447 21.928 1.00 107.23 ? 247 PHE A CA 1 ATOM 1977 C C . PHE A 1 247 ? 33.703 -20.474 21.177 1.00 104.46 ? 247 PHE A C 1 ATOM 1978 O O . PHE A 1 247 ? 32.918 -19.744 21.778 1.00 102.96 ? 247 PHE A O 1 ATOM 1979 C CB . PHE A 1 247 ? 33.768 -22.595 22.528 1.00 111.61 ? 247 PHE A CB 1 ATOM 1980 C CG . PHE A 1 247 ? 33.002 -23.412 21.516 1.00 112.80 ? 247 PHE A CG 1 ATOM 1981 C CD1 . PHE A 1 247 ? 33.570 -23.774 20.299 1.00 110.52 ? 247 PHE A CD1 1 ATOM 1982 C CD2 . PHE A 1 247 ? 31.715 -23.853 21.804 1.00 113.96 ? 247 PHE A CD2 1 ATOM 1983 C CE1 . PHE A 1 247 ? 32.862 -24.532 19.385 1.00 110.31 ? 247 PHE A CE1 1 ATOM 1984 C CE2 . PHE A 1 247 ? 31.004 -24.614 20.893 1.00 113.57 ? 247 PHE A CE2 1 ATOM 1985 C CZ . PHE A 1 247 ? 31.578 -24.952 19.682 1.00 112.88 ? 247 PHE A CZ 1 ATOM 1986 N N . ILE A 1 248 ? 33.852 -20.450 19.858 1.00 103.50 ? 248 ILE A N 1 ATOM 1987 C CA . ILE A 1 248 ? 32.931 -19.724 19.005 1.00 103.03 ? 248 ILE A CA 1 ATOM 1988 C C . ILE A 1 248 ? 32.028 -20.775 18.390 1.00 103.34 ? 248 ILE A C 1 ATOM 1989 O O . ILE A 1 248 ? 32.441 -21.532 17.515 1.00 102.85 ? 248 ILE A O 1 ATOM 1990 C CB . ILE A 1 248 ? 33.651 -18.915 17.914 1.00 102.69 ? 248 ILE A CB 1 ATOM 1991 C CG1 . ILE A 1 248 ? 34.842 -18.141 18.498 1.00 103.72 ? 248 ILE A CG1 1 ATOM 1992 C CG2 . ILE A 1 248 ? 32.675 -17.971 17.234 1.00 101.33 ? 248 ILE A CG2 1 ATOM 1993 C CD1 . ILE A 1 248 ? 34.499 -17.217 19.648 1.00 106.52 ? 248 ILE A CD1 1 ATOM 1994 N N . ALA A 1 249 ? 30.798 -20.832 18.880 1.00 105.78 ? 249 ALA A N 1 ATOM 1995 C CA . ALA A 1 249 ? 29.889 -21.917 18.547 1.00 107.29 ? 249 ALA A CA 1 ATOM 1996 C C . ALA A 1 249 ? 29.050 -21.579 17.325 1.00 105.15 ? 249 ALA A C 1 ATOM 1997 O O . ALA A 1 249 ? 28.784 -20.409 17.061 1.00 104.38 ? 249 ALA A O 1 ATOM 1998 C CB . ALA A 1 249 ? 28.983 -22.214 19.729 1.00 110.39 ? 249 ALA A CB 1 ATOM 1999 N N . PRO A 1 250 ? 28.626 -22.609 16.577 1.00 103.75 ? 250 PRO A N 1 ATOM 2000 C CA . PRO A 1 250 ? 27.706 -22.407 15.468 1.00 104.82 ? 250 PRO A CA 1 ATOM 2001 C C . PRO A 1 250 ? 26.273 -22.225 15.927 1.00 107.45 ? 250 PRO A C 1 ATOM 2002 O O . PRO A 1 250 ? 25.814 -22.967 16.788 1.00 115.00 ? 250 PRO A O 1 ATOM 2003 C CB . PRO A 1 250 ? 27.819 -23.709 14.674 1.00 104.90 ? 250 PRO A CB 1 ATOM 2004 C CG . PRO A 1 250 ? 28.268 -24.723 15.651 1.00 105.00 ? 250 PRO A CG 1 ATOM 2005 C CD . PRO A 1 250 ? 29.107 -23.998 16.655 1.00 104.76 ? 250 PRO A CD 1 ATOM 2006 N N . GLU A 1 251 ? 25.580 -21.241 15.367 1.00 108.12 ? 251 GLU A N 1 ATOM 2007 C CA . GLU A 1 251 ? 24.133 -21.161 15.503 1.00 113.08 ? 251 GLU A CA 1 ATOM 2008 C C . GLU A 1 251 ? 23.485 -21.675 14.221 1.00 113.38 ? 251 GLU A C 1 ATOM 2009 O O . GLU A 1 251 ? 22.575 -22.509 14.268 1.00 113.12 ? 251 GLU A O 1 ATOM 2010 C CB . GLU A 1 251 ? 23.672 -19.733 15.798 1.00 115.97 ? 251 GLU A CB 1 ATOM 2011 C CG . GLU A 1 251 ? 22.244 -19.676 16.328 1.00 122.12 ? 251 GLU A CG 1 ATOM 2012 C CD . GLU A 1 251 ? 21.689 -18.268 16.438 1.00 126.37 ? 251 GLU A CD 1 ATOM 2013 O OE1 . GLU A 1 251 ? 22.482 -17.306 16.560 1.00 128.72 ? 251 GLU A OE1 1 ATOM 2014 O OE2 . GLU A 1 251 ? 20.447 -18.129 16.408 1.00 128.28 ? 251 GLU A OE2 1 ATOM 2015 N N . TYR A 1 252 ? 23.964 -21.172 13.083 1.00 110.58 ? 252 TYR A N 1 ATOM 2016 C CA . TYR A 1 252 ? 23.453 -21.563 11.772 1.00 108.20 ? 252 TYR A CA 1 ATOM 2017 C C . TYR A 1 252 ? 24.503 -22.327 10.966 1.00 107.02 ? 252 TYR A C 1 ATOM 2018 O O . TYR A 1 252 ? 25.704 -22.091 11.099 1.00 104.98 ? 252 TYR A O 1 ATOM 2019 C CB . TYR A 1 252 ? 22.997 -20.327 10.988 1.00 106.51 ? 252 TYR A CB 1 ATOM 2020 C CG . TYR A 1 252 ? 21.908 -19.532 11.676 1.00 108.19 ? 252 TYR A CG 1 ATOM 2021 C CD1 . TYR A 1 252 ? 20.581 -19.954 11.645 1.00 109.60 ? 252 TYR A CD1 1 ATOM 2022 C CD2 . TYR A 1 252 ? 22.206 -18.358 12.364 1.00 106.65 ? 252 TYR A CD2 1 ATOM 2023 C CE1 . TYR A 1 252 ? 19.585 -19.226 12.281 1.00 110.06 ? 252 TYR A CE1 1 ATOM 2024 C CE2 . TYR A 1 252 ? 21.219 -17.627 12.999 1.00 106.11 ? 252 TYR A CE2 1 ATOM 2025 C CZ . TYR A 1 252 ? 19.910 -18.063 12.958 1.00 108.20 ? 252 TYR A CZ 1 ATOM 2026 O OH . TYR A 1 252 ? 18.933 -17.332 13.602 1.00 106.13 ? 252 TYR A OH 1 ATOM 2027 N N . ALA A 1 253 ? 24.029 -23.252 10.139 1.00 107.53 ? 253 ALA A N 1 ATOM 2028 C CA . ALA A 1 253 ? 24.865 -23.966 9.181 1.00 106.03 ? 253 ALA A CA 1 ATOM 2029 C C . ALA A 1 253 ? 24.163 -23.957 7.829 1.00 106.18 ? 253 ALA A C 1 ATOM 2030 O O . ALA A 1 253 ? 22.997 -23.575 7.744 1.00 109.91 ? 253 ALA A O 1 ATOM 2031 C CB . ALA A 1 253 ? 25.096 -25.391 9.652 1.00 108.21 ? 253 ALA A CB 1 ATOM 2032 N N . TYR A 1 254 ? 24.867 -24.381 6.781 1.00 104.27 ? 254 TYR A N 1 ATOM 2033 C CA . TYR A 1 254 ? 24.331 -24.351 5.422 1.00 101.49 ? 254 TYR A CA 1 ATOM 2034 C C . TYR A 1 254 ? 24.122 -25.755 4.863 1.00 101.47 ? 254 TYR A C 1 ATOM 2035 O O . TYR A 1 254 ? 25.075 -26.520 4.740 1.00 100.09 ? 254 TYR A O 1 ATOM 2036 C CB . TYR A 1 254 ? 25.290 -23.598 4.503 1.00 99.80 ? 254 TYR A CB 1 ATOM 2037 C CG . TYR A 1 254 ? 25.473 -22.127 4.815 1.00 97.14 ? 254 TYR A CG 1 ATOM 2038 C CD1 . TYR A 1 254 ? 26.454 -21.700 5.703 1.00 98.63 ? 254 TYR A CD1 1 ATOM 2039 C CD2 . TYR A 1 254 ? 24.689 -21.161 4.193 1.00 95.89 ? 254 TYR A CD2 1 ATOM 2040 C CE1 . TYR A 1 254 ? 26.638 -20.351 5.976 1.00 98.67 ? 254 TYR A CE1 1 ATOM 2041 C CE2 . TYR A 1 254 ? 24.863 -19.812 4.453 1.00 95.98 ? 254 TYR A CE2 1 ATOM 2042 C CZ . TYR A 1 254 ? 25.839 -19.409 5.343 1.00 98.84 ? 254 TYR A CZ 1 ATOM 2043 O OH . TYR A 1 254 ? 26.005 -18.065 5.606 1.00 100.36 ? 254 TYR A OH 1 ATOM 2044 N N . LYS A 1 255 ? 22.875 -26.088 4.531 1.00 104.72 ? 255 LYS A N 1 ATOM 2045 C CA . LYS A 1 255 ? 22.567 -27.310 3.777 1.00 107.19 ? 255 LYS A CA 1 ATOM 2046 C C . LYS A 1 255 ? 23.030 -27.130 2.338 1.00 103.46 ? 255 LYS A C 1 ATOM 2047 O O . LYS A 1 255 ? 22.781 -26.091 1.730 1.00 99.10 ? 255 LYS A O 1 ATOM 2048 C CB . LYS A 1 255 ? 21.059 -27.592 3.760 1.00 111.67 ? 255 LYS A CB 1 ATOM 2049 C CG . LYS A 1 255 ? 20.441 -27.998 5.091 1.00 116.30 ? 255 LYS A CG 1 ATOM 2050 C CD . LYS A 1 255 ? 18.925 -27.792 5.101 1.00 118.77 ? 255 LYS A CD 1 ATOM 2051 C CE . LYS A 1 255 ? 18.173 -28.812 4.253 1.00 121.63 ? 255 LYS A CE 1 ATOM 2052 N NZ . LYS A 1 255 ? 17.351 -29.769 5.048 1.00 127.36 ? 255 LYS A NZ 1 ATOM 2053 N N . ILE A 1 256 ? 23.695 -28.143 1.795 1.00 102.97 ? 256 ILE A N 1 ATOM 2054 C CA . ILE A 1 256 ? 24.097 -28.125 0.396 1.00 105.02 ? 256 ILE A CA 1 ATOM 2055 C C . ILE A 1 256 ? 23.016 -28.818 -0.421 1.00 108.74 ? 256 ILE A C 1 ATOM 2056 O O . ILE A 1 256 ? 22.947 -30.049 -0.452 1.00 110.12 ? 256 ILE A O 1 ATOM 2057 C CB . ILE A 1 256 ? 25.434 -28.846 0.186 1.00 103.99 ? 256 ILE A CB 1 ATOM 2058 C CG1 . ILE A 1 256 ? 26.555 -28.091 0.895 1.00 103.20 ? 256 ILE A CG1 1 ATOM 2059 C CG2 . ILE A 1 256 ? 25.744 -28.959 -1.299 1.00 104.48 ? 256 ILE A CG2 1 ATOM 2060 C CD1 . ILE A 1 256 ? 27.744 -28.956 1.246 1.00 104.42 ? 256 ILE A CD1 1 ATOM 2061 N N . VAL A 1 257 ? 22.178 -28.026 -1.082 1.00 110.35 ? 257 VAL A N 1 ATOM 2062 C CA . VAL A 1 257 ? 21.019 -28.571 -1.790 1.00 114.78 ? 257 VAL A CA 1 ATOM 2063 C C . VAL A 1 257 ? 21.293 -28.837 -3.273 1.00 115.16 ? 257 VAL A C 1 ATOM 2064 O O . VAL A 1 257 ? 20.762 -29.797 -3.833 1.00 115.39 ? 257 VAL A O 1 ATOM 2065 C CB . VAL A 1 257 ? 19.748 -27.701 -1.608 1.00 115.65 ? 257 VAL A CB 1 ATOM 2066 C CG1 . VAL A 1 257 ? 19.311 -27.708 -0.156 1.00 119.00 ? 257 VAL A CG1 1 ATOM 2067 C CG2 . VAL A 1 257 ? 19.954 -26.273 -2.083 1.00 114.12 ? 257 VAL A CG2 1 ATOM 2068 N N . LYS A 1 258 ? 22.126 -28.000 -3.894 1.00 117.99 ? 258 LYS A N 1 ATOM 2069 C CA . LYS A 1 258 ? 22.449 -28.125 -5.321 1.00 119.83 ? 258 LYS A CA 1 ATOM 2070 C C . LYS A 1 258 ? 23.943 -28.182 -5.594 1.00 117.74 ? 258 LYS A C 1 ATOM 2071 O O . LYS A 1 258 ? 24.672 -27.241 -5.287 1.00 119.11 ? 258 LYS A O 1 ATOM 2072 C CB . LYS A 1 258 ? 21.858 -26.951 -6.096 1.00 120.55 ? 258 LYS A CB 1 ATOM 2073 C CG . LYS A 1 258 ? 20.396 -27.138 -6.452 1.00 126.14 ? 258 LYS A CG 1 ATOM 2074 C CD . LYS A 1 258 ? 20.243 -27.693 -7.855 1.00 125.32 ? 258 LYS A CD 1 ATOM 2075 C CE . LYS A 1 258 ? 20.366 -26.583 -8.877 1.00 122.46 ? 258 LYS A CE 1 ATOM 2076 N NZ . LYS A 1 258 ? 20.262 -27.095 -10.265 1.00 124.37 ? 258 LYS A NZ 1 ATOM 2077 N N . LYS A 1 259 ? 24.383 -29.290 -6.182 1.00 118.51 ? 259 LYS A N 1 ATOM 2078 C CA . LYS A 1 259 ? 25.728 -29.411 -6.734 1.00 118.39 ? 259 LYS A CA 1 ATOM 2079 C C . LYS A 1 259 ? 25.697 -29.010 -8.210 1.00 116.93 ? 259 LYS A C 1 ATOM 2080 O O . LYS A 1 259 ? 24.649 -28.623 -8.724 1.00 112.46 ? 259 LYS A O 1 ATOM 2081 C CB . LYS A 1 259 ? 26.229 -30.847 -6.578 1.00 122.46 ? 259 LYS A CB 1 ATOM 2082 C CG . LYS A 1 259 ? 26.593 -31.224 -5.150 1.00 126.95 ? 259 LYS A CG 1 ATOM 2083 C CD . LYS A 1 259 ? 28.087 -31.051 -4.887 1.00 127.81 ? 259 LYS A CD 1 ATOM 2084 C CE . LYS A 1 259 ? 28.443 -31.262 -3.422 1.00 130.65 ? 259 LYS A CE 1 ATOM 2085 N NZ . LYS A 1 259 ? 27.793 -32.464 -2.824 1.00 133.08 ? 259 LYS A NZ 1 ATOM 2086 N N . GLY A 1 260 ? 26.843 -29.079 -8.883 1.00 120.90 ? 260 GLY A N 1 ATOM 2087 C CA . GLY A 1 260 ? 26.907 -28.814 -10.320 1.00 122.35 ? 260 GLY A CA 1 ATOM 2088 C C . GLY A 1 260 ? 27.985 -27.833 -10.738 1.00 120.85 ? 260 GLY A C 1 ATOM 2089 O O . GLY A 1 260 ? 29.010 -27.701 -10.071 1.00 119.40 ? 260 GLY A O 1 ATOM 2090 N N . ASP A 1 261 ? 27.743 -27.155 -11.860 1.00 122.22 ? 261 ASP A N 1 ATOM 2091 C CA . ASP A 1 261 ? 28.726 -26.265 -12.474 1.00 118.21 ? 261 ASP A CA 1 ATOM 2092 C C . ASP A 1 261 ? 28.563 -24.855 -11.962 1.00 110.77 ? 261 ASP A C 1 ATOM 2093 O O . ASP A 1 261 ? 27.484 -24.275 -12.044 1.00 107.29 ? 261 ASP A O 1 ATOM 2094 C CB . ASP A 1 261 ? 28.590 -26.252 -14.002 1.00 125.46 ? 261 ASP A CB 1 ATOM 2095 C CG . ASP A 1 261 ? 29.284 -27.431 -14.668 1.00 134.71 ? 261 ASP A CG 1 ATOM 2096 O OD1 . ASP A 1 261 ? 29.754 -28.339 -13.946 1.00 142.67 ? 261 ASP A OD1 1 ATOM 2097 O OD2 . ASP A 1 261 ? 29.361 -27.445 -15.918 1.00 137.23 ? 261 ASP A OD2 1 ATOM 2098 N N . SER A 1 262 ? 29.651 -24.314 -11.435 1.00 104.00 ? 262 SER A N 1 ATOM 2099 C CA . SER A 1 262 ? 29.696 -22.937 -10.979 1.00 104.39 ? 262 SER A CA 1 ATOM 2100 C C . SER A 1 262 ? 31.155 -22.527 -10.915 1.00 103.71 ? 262 SER A C 1 ATOM 2101 O O . SER A 1 262 ? 32.047 -23.324 -11.216 1.00 108.42 ? 262 SER A O 1 ATOM 2102 C CB . SER A 1 262 ? 29.043 -22.798 -9.601 1.00 107.37 ? 262 SER A CB 1 ATOM 2103 O OG . SER A 1 262 ? 29.117 -21.466 -9.113 1.00 105.20 ? 262 SER A OG 1 ATOM 2104 N N . THR A 1 263 ? 31.402 -21.286 -10.528 1.00 97.91 ? 263 THR A N 1 ATOM 2105 C CA . THR A 1 263 ? 32.761 -20.808 -10.393 1.00 93.58 ? 263 THR A CA 1 ATOM 2106 C C . THR A 1 263 ? 32.765 -19.559 -9.541 1.00 89.11 ? 263 THR A C 1 ATOM 2107 O O . THR A 1 263 ? 31.735 -18.898 -9.405 1.00 85.74 ? 263 THR A O 1 ATOM 2108 C CB . THR A 1 263 ? 33.394 -20.521 -11.775 1.00 95.66 ? 263 THR A CB 1 ATOM 2109 O OG1 . THR A 1 263 ? 34.808 -20.354 -11.634 1.00 99.65 ? 263 THR A OG1 1 ATOM 2110 C CG2 . THR A 1 263 ? 32.796 -19.273 -12.423 1.00 94.46 ? 263 THR A CG2 1 ATOM 2111 N N . ILE A 1 264 ? 33.920 -19.257 -8.952 1.00 90.00 ? 264 ILE A N 1 ATOM 2112 C CA . ILE A 1 264 ? 34.134 -17.980 -8.275 1.00 88.99 ? 264 ILE A CA 1 ATOM 2113 C C . ILE A 1 264 ? 34.978 -17.111 -9.197 1.00 87.34 ? 264 ILE A C 1 ATOM 2114 O O . ILE A 1 264 ? 36.128 -17.429 -9.497 1.00 89.32 ? 264 ILE A O 1 ATOM 2115 C CB . ILE A 1 264 ? 34.814 -18.146 -6.905 1.00 86.84 ? 264 ILE A CB 1 ATOM 2116 C CG1 . ILE A 1 264 ? 34.004 -19.115 -6.043 1.00 91.10 ? 264 ILE A CG1 1 ATOM 2117 C CG2 . ILE A 1 264 ? 34.936 -16.800 -6.202 1.00 83.47 ? 264 ILE A CG2 1 ATOM 2118 C CD1 . ILE A 1 264 ? 34.578 -19.329 -4.662 1.00 94.15 ? 264 ILE A CD1 1 ATOM 2119 N N . MET A 1 265 ? 34.379 -16.014 -9.638 1.00 85.82 ? 265 MET A N 1 ATOM 2120 C CA . MET A 1 265 ? 34.943 -15.140 -10.647 1.00 82.63 ? 265 MET A CA 1 ATOM 2121 C C . MET A 1 265 ? 35.414 -13.885 -9.951 1.00 81.84 ? 265 MET A C 1 ATOM 2122 O O . MET A 1 265 ? 34.730 -13.380 -9.070 1.00 86.27 ? 265 MET A O 1 ATOM 2123 C CB . MET A 1 265 ? 33.835 -14.794 -11.630 1.00 85.22 ? 265 MET A CB 1 ATOM 2124 C CG . MET A 1 265 ? 34.257 -14.086 -12.891 1.00 86.92 ? 265 MET A CG 1 ATOM 2125 S SD . MET A 1 265 ? 32.860 -13.982 -14.028 1.00 90.01 ? 265 MET A SD 1 ATOM 2126 C CE . MET A 1 265 ? 32.819 -15.665 -14.652 1.00 89.87 ? 265 MET A CE 1 ATOM 2127 N N . LYS A 1 266 ? 36.588 -13.394 -10.326 1.00 83.80 ? 266 LYS A N 1 ATOM 2128 C CA . LYS A 1 266 ? 37.131 -12.178 -9.741 1.00 83.62 ? 266 LYS A CA 1 ATOM 2129 C C . LYS A 1 266 ? 36.872 -11.039 -10.701 1.00 83.09 ? 266 LYS A C 1 ATOM 2130 O O . LYS A 1 266 ? 37.273 -11.100 -11.859 1.00 88.40 ? 266 LYS A O 1 ATOM 2131 C CB . LYS A 1 266 ? 38.627 -12.315 -9.484 1.00 86.21 ? 266 LYS A CB 1 ATOM 2132 C CG . LYS A 1 266 ? 38.984 -13.338 -8.425 1.00 93.08 ? 266 LYS A CG 1 ATOM 2133 C CD . LYS A 1 266 ? 38.630 -12.845 -7.030 1.00 100.76 ? 266 LYS A CD 1 ATOM 2134 C CE . LYS A 1 266 ? 39.168 -13.782 -5.961 1.00 105.58 ? 266 LYS A CE 1 ATOM 2135 N NZ . LYS A 1 266 ? 38.649 -15.168 -6.143 1.00 106.78 ? 266 LYS A NZ 1 ATOM 2136 N N . SER A 1 267 ? 36.194 -10.004 -10.220 1.00 82.73 ? 267 SER A N 1 ATOM 2137 C CA . SER A 1 267 ? 35.776 -8.903 -11.070 1.00 83.32 ? 267 SER A CA 1 ATOM 2138 C C . SER A 1 267 ? 35.339 -7.731 -10.220 1.00 85.22 ? 267 SER A C 1 ATOM 2139 O O . SER A 1 267 ? 34.762 -7.910 -9.150 1.00 95.51 ? 267 SER A O 1 ATOM 2140 C CB . SER A 1 267 ? 34.617 -9.344 -11.971 1.00 84.61 ? 267 SER A CB 1 ATOM 2141 O OG . SER A 1 267 ? 34.124 -8.275 -12.762 1.00 84.93 ? 267 SER A OG 1 ATOM 2142 N N . GLU A 1 268 ? 35.608 -6.529 -10.705 1.00 86.23 ? 268 GLU A N 1 ATOM 2143 C CA . GLU A 1 268 ? 35.186 -5.328 -10.015 1.00 88.42 ? 268 GLU A CA 1 ATOM 2144 C C . GLU A 1 268 ? 33.839 -4.835 -10.562 1.00 88.35 ? 268 GLU A C 1 ATOM 2145 O O . GLU A 1 268 ? 33.277 -3.857 -10.072 1.00 90.49 ? 268 GLU A O 1 ATOM 2146 C CB . GLU A 1 268 ? 36.278 -4.260 -10.117 1.00 89.69 ? 268 GLU A CB 1 ATOM 2147 C CG . GLU A 1 268 ? 37.655 -4.731 -9.640 1.00 92.15 ? 268 GLU A CG 1 ATOM 2148 C CD . GLU A 1 268 ? 37.703 -5.130 -8.163 1.00 95.06 ? 268 GLU A CD 1 ATOM 2149 O OE1 . GLU A 1 268 ? 37.356 -4.296 -7.295 1.00 92.18 ? 268 GLU A OE1 1 ATOM 2150 O OE2 . GLU A 1 268 ? 38.111 -6.277 -7.862 1.00 96.35 ? 268 GLU A OE2 1 ATOM 2151 N N . LEU A 1 269 ? 33.300 -5.535 -11.554 1.00 89.42 ? 269 LEU A N 1 ATOM 2152 C CA . LEU A 1 269 ? 32.001 -5.181 -12.118 1.00 91.92 ? 269 LEU A CA 1 ATOM 2153 C C . LEU A 1 269 ? 30.844 -5.551 -11.188 1.00 98.18 ? 269 LEU A C 1 ATOM 2154 O O . LEU A 1 269 ? 31.008 -6.334 -10.242 1.00 100.62 ? 269 LEU A O 1 ATOM 2155 C CB . LEU A 1 269 ? 31.810 -5.856 -13.475 1.00 90.44 ? 269 LEU A CB 1 ATOM 2156 C CG . LEU A 1 269 ? 32.801 -5.451 -14.570 1.00 89.15 ? 269 LEU A CG 1 ATOM 2157 C CD1 . LEU A 1 269 ? 32.596 -6.307 -15.810 1.00 89.28 ? 269 LEU A CD1 1 ATOM 2158 C CD2 . LEU A 1 269 ? 32.666 -3.971 -14.903 1.00 89.82 ? 269 LEU A CD2 1 ATOM 2159 N N . GLU A 1 270 ? 29.682 -4.959 -11.472 1.00 102.35 ? 270 GLU A N 1 ATOM 2160 C CA . GLU A 1 270 ? 28.436 -5.234 -10.758 1.00 106.28 ? 270 GLU A CA 1 ATOM 2161 C C . GLU A 1 270 ? 27.382 -5.774 -11.740 1.00 101.88 ? 270 GLU A C 1 ATOM 2162 O O . GLU A 1 270 ? 27.668 -5.973 -12.927 1.00 100.27 ? 270 GLU A O 1 ATOM 2163 C CB . GLU A 1 270 ? 27.924 -3.959 -10.065 1.00 114.87 ? 270 GLU A CB 1 ATOM 2164 C CG . GLU A 1 270 ? 28.951 -3.222 -9.201 1.00 120.70 ? 270 GLU A CG 1 ATOM 2165 C CD . GLU A 1 270 ? 29.157 -3.836 -7.818 1.00 123.25 ? 270 GLU A CD 1 ATOM 2166 O OE1 . GLU A 1 270 ? 29.154 -5.082 -7.685 1.00 123.17 ? 270 GLU A OE1 1 ATOM 2167 O OE2 . GLU A 1 270 ? 29.332 -3.059 -6.853 1.00 123.60 ? 270 GLU A OE2 1 ATOM 2168 N N . TYR A 1 271 ? 26.166 -6.003 -11.247 1.00 99.37 ? 271 TYR A N 1 ATOM 2169 C CA . TYR A 1 271 ? 25.099 -6.596 -12.059 1.00 95.83 ? 271 TYR A CA 1 ATOM 2170 C C . TYR A 1 271 ? 24.674 -5.693 -13.208 1.00 94.90 ? 271 TYR A C 1 ATOM 2171 O O . TYR A 1 271 ? 24.555 -4.487 -13.042 1.00 96.47 ? 271 TYR A O 1 ATOM 2172 C CB . TYR A 1 271 ? 23.886 -6.916 -11.190 1.00 96.59 ? 271 TYR A CB 1 ATOM 2173 C CG . TYR A 1 271 ? 22.844 -7.751 -11.887 1.00 96.34 ? 271 TYR A CG 1 ATOM 2174 C CD1 . TYR A 1 271 ? 23.184 -8.960 -12.488 1.00 95.46 ? 271 TYR A CD1 1 ATOM 2175 C CD2 . TYR A 1 271 ? 21.514 -7.339 -11.939 1.00 97.37 ? 271 TYR A CD2 1 ATOM 2176 C CE1 . TYR A 1 271 ? 22.233 -9.731 -13.130 1.00 96.87 ? 271 TYR A CE1 1 ATOM 2177 C CE2 . TYR A 1 271 ? 20.553 -8.106 -12.572 1.00 97.24 ? 271 TYR A CE2 1 ATOM 2178 C CZ . TYR A 1 271 ? 20.914 -9.299 -13.167 1.00 97.20 ? 271 TYR A CZ 1 ATOM 2179 O OH . TYR A 1 271 ? 19.957 -10.051 -13.797 1.00 92.47 ? 271 TYR A OH 1 ATOM 2180 N N . GLY A 1 272 ? 24.433 -6.291 -14.368 1.00 98.15 ? 272 GLY A N 1 ATOM 2181 C CA . GLY A 1 272 ? 24.148 -5.536 -15.587 1.00 100.47 ? 272 GLY A CA 1 ATOM 2182 C C . GLY A 1 272 ? 22.740 -5.660 -16.132 1.00 103.22 ? 272 GLY A C 1 ATOM 2183 O O . GLY A 1 272 ? 22.403 -4.974 -17.089 1.00 102.24 ? 272 GLY A O 1 ATOM 2184 N N . ASN A 1 273 ? 21.924 -6.528 -15.528 1.00 109.13 ? 273 ASN A N 1 ATOM 2185 C CA . ASN A 1 273 ? 20.521 -6.752 -15.938 1.00 113.13 ? 273 ASN A CA 1 ATOM 2186 C C . ASN A 1 273 ? 20.387 -7.309 -17.362 1.00 108.80 ? 273 ASN A C 1 ATOM 2187 O O . ASN A 1 273 ? 19.566 -6.845 -18.147 1.00 111.51 ? 273 ASN A O 1 ATOM 2188 C CB . ASN A 1 273 ? 19.681 -5.468 -15.794 1.00 117.42 ? 273 ASN A CB 1 ATOM 2189 C CG . ASN A 1 273 ? 19.896 -4.762 -14.463 1.00 120.50 ? 273 ASN A CG 1 ATOM 2190 O OD1 . ASN A 1 273 ? 20.992 -4.269 -14.172 1.00 121.57 ? 273 ASN A OD1 1 ATOM 2191 N ND2 . ASN A 1 273 ? 18.845 -4.689 -13.657 1.00 121.25 ? 273 ASN A ND2 1 ATOM 2192 N N . CYS A 1 274 ? 21.200 -8.307 -17.680 1.00 104.75 ? 274 CYS A N 1 ATOM 2193 C CA . CYS A 1 274 ? 21.226 -8.910 -19.007 1.00 105.59 ? 274 CYS A CA 1 ATOM 2194 C C . CYS A 1 274 ? 21.162 -10.414 -18.852 1.00 100.79 ? 274 CYS A C 1 ATOM 2195 O O . CYS A 1 274 ? 21.313 -10.936 -17.746 1.00 100.75 ? 274 CYS A O 1 ATOM 2196 C CB . CYS A 1 274 ? 22.521 -8.534 -19.744 1.00 110.89 ? 274 CYS A CB 1 ATOM 2197 S SG . CYS A 1 274 ? 23.993 -8.495 -18.668 1.00 128.56 ? 274 CYS A SG 1 ATOM 2198 N N . ASN A 1 275 ? 20.952 -11.102 -19.967 1.00 97.16 ? 275 ASN A N 1 ATOM 2199 C CA . ASN A 1 275 ? 21.066 -12.548 -20.016 1.00 96.66 ? 275 ASN A CA 1 ATOM 2200 C C . ASN A 1 275 ? 22.129 -12.918 -21.050 1.00 96.14 ? 275 ASN A C 1 ATOM 2201 O O . ASN A 1 275 ? 22.431 -12.130 -21.942 1.00 98.04 ? 275 ASN A O 1 ATOM 2202 C CB . ASN A 1 275 ? 19.708 -13.168 -20.354 1.00 96.82 ? 275 ASN A CB 1 ATOM 2203 C CG . ASN A 1 275 ? 19.702 -14.681 -20.232 1.00 97.48 ? 275 ASN A CG 1 ATOM 2204 O OD1 . ASN A 1 275 ? 20.343 -15.255 -19.356 1.00 97.78 ? 275 ASN A OD1 1 ATOM 2205 N ND2 . ASN A 1 275 ? 18.968 -15.335 -21.116 1.00 103.34 ? 275 ASN A ND2 1 ATOM 2206 N N . THR A 1 276 ? 22.721 -14.097 -20.905 1.00 95.08 ? 276 THR A N 1 ATOM 2207 C CA . THR A 1 276 ? 23.750 -14.560 -21.825 1.00 95.04 ? 276 THR A CA 1 ATOM 2208 C C . THR A 1 276 ? 23.996 -16.052 -21.648 1.00 95.95 ? 276 THR A C 1 ATOM 2209 O O . THR A 1 276 ? 23.669 -16.618 -20.610 1.00 98.27 ? 276 THR A O 1 ATOM 2210 C CB . THR A 1 276 ? 25.084 -13.819 -21.607 1.00 97.22 ? 276 THR A CB 1 ATOM 2211 O OG1 . THR A 1 276 ? 26.036 -14.237 -22.592 1.00 104.42 ? 276 THR A OG1 1 ATOM 2212 C CG2 . THR A 1 276 ? 25.657 -14.113 -20.223 1.00 99.18 ? 276 THR A CG2 1 ATOM 2213 N N . LYS A 1 277 ? 24.590 -16.676 -22.660 1.00 97.96 ? 277 LYS A N 1 ATOM 2214 C CA . LYS A 1 277 ? 24.932 -18.095 -22.605 1.00 100.08 ? 277 LYS A CA 1 ATOM 2215 C C . LYS A 1 277 ? 26.419 -18.289 -22.317 1.00 94.28 ? 277 LYS A C 1 ATOM 2216 O O . LYS A 1 277 ? 26.885 -19.417 -22.207 1.00 93.44 ? 277 LYS A O 1 ATOM 2217 C CB . LYS A 1 277 ? 24.557 -18.799 -23.920 1.00 106.59 ? 277 LYS A CB 1 ATOM 2218 C CG . LYS A 1 277 ? 23.230 -18.361 -24.551 1.00 116.54 ? 277 LYS A CG 1 ATOM 2219 C CD . LYS A 1 277 ? 22.025 -18.431 -23.606 1.00 123.13 ? 277 LYS A CD 1 ATOM 2220 C CE . LYS A 1 277 ? 21.590 -19.862 -23.306 1.00 128.26 ? 277 LYS A CE 1 ATOM 2221 N NZ . LYS A 1 277 ? 21.058 -20.581 -24.502 1.00 129.76 ? 277 LYS A NZ 1 ATOM 2222 N N . CYS A 1 278 ? 27.163 -17.194 -22.199 1.00 93.68 ? 278 CYS A N 1 ATOM 2223 C CA . CYS A 1 278 ? 28.610 -17.266 -21.981 1.00 93.93 ? 278 CYS A CA 1 ATOM 2224 C C . CYS A 1 278 ? 29.104 -15.988 -21.315 1.00 86.45 ? 278 CYS A C 1 ATOM 2225 O O . CYS A 1 278 ? 28.879 -14.893 -21.834 1.00 83.92 ? 278 CYS A O 1 ATOM 2226 C CB . CYS A 1 278 ? 29.333 -17.495 -23.308 1.00 95.83 ? 278 CYS A CB 1 ATOM 2227 S SG . CYS A 1 278 ? 31.143 -17.429 -23.224 1.00 105.74 ? 278 CYS A SG 1 ATOM 2228 N N . GLN A 1 279 ? 29.767 -16.137 -20.167 1.00 80.36 ? 279 GLN A N 1 ATOM 2229 C CA . GLN A 1 279 ? 30.166 -14.996 -19.339 1.00 79.01 ? 279 GLN A CA 1 ATOM 2230 C C . GLN A 1 279 ? 31.651 -15.020 -19.038 1.00 77.24 ? 279 GLN A C 1 ATOM 2231 O O . GLN A 1 279 ? 32.208 -16.077 -18.752 1.00 76.19 ? 279 GLN A O 1 ATOM 2232 C CB . GLN A 1 279 ? 29.406 -15.017 -18.020 1.00 78.72 ? 279 GLN A CB 1 ATOM 2233 C CG . GLN A 1 279 ? 29.674 -13.821 -17.119 1.00 78.96 ? 279 GLN A CG 1 ATOM 2234 C CD . GLN A 1 279 ? 28.970 -12.565 -17.592 1.00 80.01 ? 279 GLN A CD 1 ATOM 2235 O OE1 . GLN A 1 279 ? 27.739 -12.533 -17.700 1.00 75.84 ? 279 GLN A OE1 1 ATOM 2236 N NE2 . GLN A 1 279 ? 29.744 -11.516 -17.868 1.00 79.12 ? 279 GLN A NE2 1 ATOM 2237 N N . THR A 1 280 ? 32.279 -13.849 -19.095 1.00 74.51 ? 280 THR A N 1 ATOM 2238 C CA . THR A 1 280 ? 33.661 -13.688 -18.662 1.00 77.12 ? 280 THR A CA 1 ATOM 2239 C C . THR A 1 280 ? 33.714 -12.652 -17.540 1.00 76.41 ? 280 THR A C 1 ATOM 2240 O O . THR A 1 280 ? 32.727 -11.964 -17.292 1.00 79.32 ? 280 THR A O 1 ATOM 2241 C CB . THR A 1 280 ? 34.576 -13.213 -19.807 1.00 78.72 ? 280 THR A CB 1 ATOM 2242 O OG1 . THR A 1 280 ? 34.443 -11.793 -19.979 1.00 81.17 ? 280 THR A OG1 1 ATOM 2243 C CG2 . THR A 1 280 ? 34.231 -13.927 -21.095 1.00 77.73 ? 280 THR A CG2 1 ATOM 2244 N N . PRO A 1 281 ? 34.867 -12.536 -16.862 1.00 75.62 ? 281 PRO A N 1 ATOM 2245 C CA . PRO A 1 281 ? 35.013 -11.540 -15.802 1.00 76.93 ? 281 PRO A CA 1 ATOM 2246 C C . PRO A 1 281 ? 35.008 -10.104 -16.280 1.00 77.67 ? 281 PRO A C 1 ATOM 2247 O O . PRO A 1 281 ? 34.967 -9.193 -15.447 1.00 78.29 ? 281 PRO A O 1 ATOM 2248 C CB . PRO A 1 281 ? 36.373 -11.870 -15.181 1.00 75.38 ? 281 PRO A CB 1 ATOM 2249 C CG . PRO A 1 281 ? 36.618 -13.288 -15.523 1.00 76.33 ? 281 PRO A CG 1 ATOM 2250 C CD . PRO A 1 281 ? 35.974 -13.504 -16.855 1.00 75.71 ? 281 PRO A CD 1 ATOM 2251 N N . MET A 1 282 ? 35.064 -9.886 -17.589 1.00 79.29 ? 282 MET A N 1 ATOM 2252 C CA . MET A 1 282 ? 34.977 -8.526 -18.103 1.00 84.73 ? 282 MET A CA 1 ATOM 2253 C C . MET A 1 282 ? 33.787 -8.281 -18.999 1.00 82.25 ? 282 MET A C 1 ATOM 2254 O O . MET A 1 282 ? 33.648 -7.187 -19.534 1.00 85.50 ? 282 MET A O 1 ATOM 2255 C CB . MET A 1 282 ? 36.267 -8.107 -18.798 1.00 90.91 ? 282 MET A CB 1 ATOM 2256 C CG . MET A 1 282 ? 36.881 -9.114 -19.741 1.00 97.84 ? 282 MET A CG 1 ATOM 2257 S SD . MET A 1 282 ? 38.558 -8.582 -20.128 1.00 108.39 ? 282 MET A SD 1 ATOM 2258 C CE . MET A 1 282 ? 39.292 -8.647 -18.490 1.00 107.06 ? 282 MET A CE 1 ATOM 2259 N N . GLY A 1 283 ? 32.909 -9.270 -19.128 1.00 79.67 ? 283 GLY A N 1 ATOM 2260 C CA . GLY A 1 283 ? 31.716 -9.114 -19.944 1.00 79.94 ? 283 GLY A CA 1 ATOM 2261 C C . GLY A 1 283 ? 31.255 -10.408 -20.570 1.00 81.16 ? 283 GLY A C 1 ATOM 2262 O O . GLY A 1 283 ? 31.968 -11.412 -20.545 1.00 81.10 ? 283 GLY A O 1 ATOM 2263 N N . ALA A 1 284 ? 30.059 -10.369 -21.146 1.00 81.24 ? 284 ALA A N 1 ATOM 2264 C CA . ALA A 1 284 ? 29.433 -11.552 -21.722 1.00 81.51 ? 284 ALA A CA 1 ATOM 2265 C C . ALA A 1 284 ? 29.636 -11.623 -23.231 1.00 83.41 ? 284 ALA A C 1 ATOM 2266 O O . ALA A 1 284 ? 29.816 -10.598 -23.894 1.00 80.97 ? 284 ALA A O 1 ATOM 2267 C CB . ALA A 1 284 ? 27.954 -11.561 -21.400 1.00 80.48 ? 284 ALA A CB 1 ATOM 2268 N N . ILE A 1 285 ? 29.569 -12.845 -23.759 1.00 84.27 ? 285 ILE A N 1 ATOM 2269 C CA . ILE A 1 285 ? 29.819 -13.111 -25.169 1.00 85.08 ? 285 ILE A CA 1 ATOM 2270 C C . ILE A 1 285 ? 28.586 -13.691 -25.845 1.00 88.44 ? 285 ILE A C 1 ATOM 2271 O O . ILE A 1 285 ? 28.042 -14.705 -25.414 1.00 91.46 ? 285 ILE A O 1 ATOM 2272 C CB . ILE A 1 285 ? 30.987 -14.098 -25.347 1.00 83.83 ? 285 ILE A CB 1 ATOM 2273 C CG1 . ILE A 1 285 ? 32.285 -13.463 -24.863 1.00 80.46 ? 285 ILE A CG1 1 ATOM 2274 C CG2 . ILE A 1 285 ? 31.131 -14.512 -26.806 1.00 85.90 ? 285 ILE A CG2 1 ATOM 2275 C CD1 . ILE A 1 285 ? 33.427 -14.443 -24.727 1.00 81.17 ? 285 ILE A CD1 1 ATOM 2276 N N . ASN A 1 286 ? 28.170 -13.034 -26.921 1.00 94.42 ? 286 ASN A N 1 ATOM 2277 C CA . ASN A 1 286 ? 27.078 -13.490 -27.766 1.00 97.35 ? 286 ASN A CA 1 ATOM 2278 C C . ASN A 1 286 ? 27.595 -13.663 -29.198 1.00 96.58 ? 286 ASN A C 1 ATOM 2279 O O . ASN A 1 286 ? 27.603 -12.718 -29.981 1.00 92.81 ? 286 ASN A O 1 ATOM 2280 C CB . ASN A 1 286 ? 25.951 -12.460 -27.706 1.00 102.65 ? 286 ASN A CB 1 ATOM 2281 C CG . ASN A 1 286 ? 24.797 -12.789 -28.626 1.00 114.38 ? 286 ASN A CG 1 ATOM 2282 O OD1 . ASN A 1 286 ? 24.429 -13.954 -28.792 1.00 114.17 ? 286 ASN A OD1 1 ATOM 2283 N ND2 . ASN A 1 286 ? 24.212 -11.746 -29.228 1.00 129.87 ? 286 ASN A ND2 1 ATOM 2284 N N . SER A 1 287 ? 28.062 -14.862 -29.529 1.00 94.73 ? 287 SER A N 1 ATOM 2285 C CA . SER A 1 287 ? 28.531 -15.128 -30.882 1.00 99.40 ? 287 SER A CA 1 ATOM 2286 C C . SER A 1 287 ? 28.634 -16.615 -31.192 1.00 102.07 ? 287 SER A C 1 ATOM 2287 O O . SER A 1 287 ? 28.762 -17.441 -30.290 1.00 101.20 ? 287 SER A O 1 ATOM 2288 C CB . SER A 1 287 ? 29.895 -14.473 -31.114 1.00 99.23 ? 287 SER A CB 1 ATOM 2289 O OG . SER A 1 287 ? 30.940 -15.306 -30.658 1.00 97.03 ? 287 SER A OG 1 ATOM 2290 N N . SER A 1 288 ? 28.603 -16.935 -32.484 1.00 103.70 ? 288 SER A N 1 ATOM 2291 C CA . SER A 1 288 ? 28.745 -18.311 -32.953 1.00 105.16 ? 288 SER A CA 1 ATOM 2292 C C . SER A 1 288 ? 30.158 -18.602 -33.457 1.00 98.95 ? 288 SER A C 1 ATOM 2293 O O . SER A 1 288 ? 30.376 -19.590 -34.154 1.00 98.81 ? 288 SER A O 1 ATOM 2294 C CB . SER A 1 288 ? 27.746 -18.578 -34.076 1.00 110.04 ? 288 SER A CB 1 ATOM 2295 O OG . SER A 1 288 ? 28.078 -17.811 -35.218 1.00 115.89 ? 288 SER A OG 1 ATOM 2296 N N . MET A 1 289 ? 31.114 -17.749 -33.104 1.00 94.41 ? 289 MET A N 1 ATOM 2297 C CA . MET A 1 289 ? 32.490 -17.934 -33.544 1.00 94.25 ? 289 MET A CA 1 ATOM 2298 C C . MET A 1 289 ? 33.099 -19.075 -32.763 1.00 91.38 ? 289 MET A C 1 ATOM 2299 O O . MET A 1 289 ? 32.791 -19.249 -31.591 1.00 94.63 ? 289 MET A O 1 ATOM 2300 C CB . MET A 1 289 ? 33.343 -16.695 -33.280 1.00 98.40 ? 289 MET A CB 1 ATOM 2301 C CG . MET A 1 289 ? 32.829 -15.397 -33.870 1.00 102.75 ? 289 MET A CG 1 ATOM 2302 S SD . MET A 1 289 ? 33.199 -15.198 -35.612 1.00 100.74 ? 289 MET A SD 1 ATOM 2303 C CE . MET A 1 289 ? 33.534 -13.434 -35.627 1.00 99.50 ? 289 MET A CE 1 ATOM 2304 N N . PRO A 1 290 ? 33.988 -19.845 -33.399 1.00 91.25 ? 290 PRO A N 1 ATOM 2305 C CA . PRO A 1 290 ? 34.668 -20.923 -32.690 1.00 89.20 ? 290 PRO A CA 1 ATOM 2306 C C . PRO A 1 290 ? 35.639 -20.445 -31.617 1.00 85.70 ? 290 PRO A C 1 ATOM 2307 O O . PRO A 1 290 ? 35.853 -21.164 -30.647 1.00 89.92 ? 290 PRO A O 1 ATOM 2308 C CB . PRO A 1 290 ? 35.448 -21.625 -33.798 1.00 89.47 ? 290 PRO A CB 1 ATOM 2309 C CG . PRO A 1 290 ? 35.692 -20.553 -34.799 1.00 90.17 ? 290 PRO A CG 1 ATOM 2310 C CD . PRO A 1 290 ? 34.424 -19.756 -34.803 1.00 89.03 ? 290 PRO A CD 1 ATOM 2311 N N . PHE A 1 291 ? 36.224 -19.260 -31.805 1.00 81.09 ? 291 PHE A N 1 ATOM 2312 C CA . PHE A 1 291 ? 37.230 -18.715 -30.889 1.00 80.62 ? 291 PHE A CA 1 ATOM 2313 C C . PHE A 1 291 ? 36.843 -17.344 -30.356 1.00 77.01 ? 291 PHE A C 1 ATOM 2314 O O . PHE A 1 291 ? 36.033 -16.647 -30.963 1.00 78.24 ? 291 PHE A O 1 ATOM 2315 C CB . PHE A 1 291 ? 38.551 -18.507 -31.616 1.00 84.72 ? 291 PHE A CB 1 ATOM 2316 C CG . PHE A 1 291 ? 39.204 -19.762 -32.086 1.00 90.12 ? 291 PHE A CG 1 ATOM 2317 C CD1 . PHE A 1 291 ? 39.892 -20.572 -31.198 1.00 93.87 ? 291 PHE A CD1 1 ATOM 2318 C CD2 . PHE A 1 291 ? 39.176 -20.112 -33.431 1.00 95.49 ? 291 PHE A CD2 1 ATOM 2319 C CE1 . PHE A 1 291 ? 40.519 -21.726 -31.634 1.00 93.76 ? 291 PHE A CE1 1 ATOM 2320 C CE2 . PHE A 1 291 ? 39.801 -21.266 -33.875 1.00 96.43 ? 291 PHE A CE2 1 ATOM 2321 C CZ . PHE A 1 291 ? 40.470 -22.073 -32.975 1.00 94.79 ? 291 PHE A CZ 1 ATOM 2322 N N . HIS A 1 292 ? 37.466 -16.953 -29.243 1.00 74.26 ? 292 HIS A N 1 ATOM 2323 C CA . HIS A 1 292 ? 37.444 -15.567 -28.766 1.00 72.13 ? 292 HIS A CA 1 ATOM 2324 C C . HIS A 1 292 ? 38.760 -15.228 -28.082 1.00 71.05 ? 292 HIS A C 1 ATOM 2325 O O . HIS A 1 292 ? 39.527 -16.130 -27.750 1.00 73.47 ? 292 HIS A O 1 ATOM 2326 C CB . HIS A 1 292 ? 36.286 -15.342 -27.805 1.00 77.61 ? 292 HIS A CB 1 ATOM 2327 C CG . HIS A 1 292 ? 36.464 -16.002 -26.473 1.00 82.33 ? 292 HIS A CG 1 ATOM 2328 N ND1 . HIS A 1 292 ? 37.148 -15.410 -25.437 1.00 84.27 ? 292 HIS A ND1 1 ATOM 2329 C CD2 . HIS A 1 292 ? 36.032 -17.194 -26.002 1.00 85.49 ? 292 HIS A CD2 1 ATOM 2330 C CE1 . HIS A 1 292 ? 37.143 -16.214 -24.391 1.00 86.17 ? 292 HIS A CE1 1 ATOM 2331 N NE2 . HIS A 1 292 ? 36.468 -17.302 -24.706 1.00 86.92 ? 292 HIS A NE2 1 ATOM 2332 N N . ASN A 1 293 ? 39.028 -13.939 -27.871 1.00 69.72 ? 293 ASN A N 1 ATOM 2333 C CA . ASN A 1 293 ? 40.277 -13.508 -27.223 1.00 70.17 ? 293 ASN A CA 1 ATOM 2334 C C . ASN A 1 293 ? 40.068 -12.525 -26.071 1.00 72.36 ? 293 ASN A C 1 ATOM 2335 O O . ASN A 1 293 ? 40.938 -11.716 -25.753 1.00 75.02 ? 293 ASN A O 1 ATOM 2336 C CB . ASN A 1 293 ? 41.216 -12.893 -28.253 1.00 71.97 ? 293 ASN A CB 1 ATOM 2337 C CG . ASN A 1 293 ? 40.766 -11.518 -28.719 1.00 71.56 ? 293 ASN A CG 1 ATOM 2338 O OD1 . ASN A 1 293 ? 39.656 -11.066 -28.427 1.00 71.79 ? 293 ASN A OD1 1 ATOM 2339 N ND2 . ASN A 1 293 ? 41.638 -10.844 -29.449 1.00 70.93 ? 293 ASN A ND2 1 ATOM 2340 N N . ILE A 1 294 ? 38.917 -12.625 -25.434 1.00 72.75 ? 294 ILE A N 1 ATOM 2341 C CA . ILE A 1 294 ? 38.508 -11.702 -24.395 1.00 73.84 ? 294 ILE A CA 1 ATOM 2342 C C . ILE A 1 294 ? 39.126 -12.029 -23.041 1.00 73.89 ? 294 ILE A C 1 ATOM 2343 O O . ILE A 1 294 ? 39.761 -11.176 -22.435 1.00 80.32 ? 294 ILE A O 1 ATOM 2344 C CB . ILE A 1 294 ? 36.975 -11.682 -24.325 1.00 76.04 ? 294 ILE A CB 1 ATOM 2345 C CG1 . ILE A 1 294 ? 36.434 -11.027 -25.599 1.00 76.25 ? 294 ILE A CG1 1 ATOM 2346 C CG2 . ILE A 1 294 ? 36.494 -10.941 -23.098 1.00 78.25 ? 294 ILE A CG2 1 ATOM 2347 C CD1 . ILE A 1 294 ? 35.074 -11.540 -25.981 1.00 79.92 ? 294 ILE A CD1 1 ATOM 2348 N N . HIS A 1 295 ? 38.950 -13.257 -22.567 1.00 76.96 ? 295 HIS A N 1 ATOM 2349 C CA . HIS A 1 295 ? 39.507 -13.659 -21.276 1.00 76.61 ? 295 HIS A CA 1 ATOM 2350 C C . HIS A 1 295 ? 39.484 -15.196 -21.125 1.00 77.38 ? 295 HIS A C 1 ATOM 2351 O O . HIS A 1 295 ? 38.547 -15.841 -21.596 1.00 75.51 ? 295 HIS A O 1 ATOM 2352 C CB . HIS A 1 295 ? 38.689 -12.993 -20.168 1.00 81.13 ? 295 HIS A CB 1 ATOM 2353 C CG . HIS A 1 295 ? 39.295 -13.105 -18.809 1.00 81.70 ? 295 HIS A CG 1 ATOM 2354 N ND1 . HIS A 1 295 ? 39.180 -14.241 -18.045 1.00 84.45 ? 295 HIS A ND1 1 ATOM 2355 C CD2 . HIS A 1 295 ? 40.000 -12.223 -18.065 1.00 85.23 ? 295 HIS A CD2 1 ATOM 2356 C CE1 . HIS A 1 295 ? 39.799 -14.064 -16.893 1.00 83.57 ? 295 HIS A CE1 1 ATOM 2357 N NE2 . HIS A 1 295 ? 40.306 -12.847 -16.880 1.00 83.32 ? 295 HIS A NE2 1 ATOM 2358 N N . PRO A 1 296 ? 40.498 -15.785 -20.459 1.00 75.44 ? 296 PRO A N 1 ATOM 2359 C CA . PRO A 1 296 ? 40.563 -17.251 -20.341 1.00 75.36 ? 296 PRO A CA 1 ATOM 2360 C C . PRO A 1 296 ? 39.480 -17.912 -19.488 1.00 78.93 ? 296 PRO A C 1 ATOM 2361 O O . PRO A 1 296 ? 39.023 -18.999 -19.820 1.00 78.48 ? 296 PRO A O 1 ATOM 2362 C CB . PRO A 1 296 ? 41.920 -17.500 -19.682 1.00 74.35 ? 296 PRO A CB 1 ATOM 2363 C CG . PRO A 1 296 ? 42.669 -16.229 -19.796 1.00 76.87 ? 296 PRO A CG 1 ATOM 2364 C CD . PRO A 1 296 ? 41.659 -15.141 -19.825 1.00 77.05 ? 296 PRO A CD 1 ATOM 2365 N N . LEU A 1 297 ? 39.129 -17.292 -18.368 1.00 85.22 ? 297 LEU A N 1 ATOM 2366 C CA . LEU A 1 297 ? 38.150 -17.855 -17.429 1.00 90.03 ? 297 LEU A CA 1 ATOM 2367 C C . LEU A 1 297 ? 36.711 -17.546 -17.826 1.00 87.77 ? 297 LEU A C 1 ATOM 2368 O O . LEU A 1 297 ? 36.185 -16.495 -17.497 1.00 90.79 ? 297 LEU A O 1 ATOM 2369 C CB . LEU A 1 297 ? 38.418 -17.338 -16.008 1.00 91.76 ? 297 LEU A CB 1 ATOM 2370 C CG . LEU A 1 297 ? 39.841 -17.547 -15.471 1.00 97.20 ? 297 LEU A CG 1 ATOM 2371 C CD1 . LEU A 1 297 ? 40.060 -16.764 -14.181 1.00 98.68 ? 297 LEU A CD1 1 ATOM 2372 C CD2 . LEU A 1 297 ? 40.144 -19.028 -15.260 1.00 99.54 ? 297 LEU A CD2 1 ATOM 2373 N N . THR A 1 298 ? 36.069 -18.470 -18.526 1.00 87.93 ? 298 THR A N 1 ATOM 2374 C CA . THR A 1 298 ? 34.678 -18.280 -18.916 1.00 89.81 ? 298 THR A CA 1 ATOM 2375 C C . THR A 1 298 ? 33.784 -19.316 -18.222 1.00 87.00 ? 298 THR A C 1 ATOM 2376 O O . THR A 1 298 ? 34.273 -20.297 -17.673 1.00 85.53 ? 298 THR A O 1 ATOM 2377 C CB . THR A 1 298 ? 34.508 -18.333 -20.454 1.00 90.62 ? 298 THR A CB 1 ATOM 2378 O OG1 . THR A 1 298 ? 34.567 -19.686 -20.919 1.00 97.89 ? 298 THR A OG1 1 ATOM 2379 C CG2 . THR A 1 298 ? 35.596 -17.544 -21.138 1.00 93.15 ? 298 THR A CG2 1 ATOM 2380 N N . ILE A 1 299 ? 32.479 -19.072 -18.235 1.00 83.06 ? 299 ILE A N 1 ATOM 2381 C CA . ILE A 1 299 ? 31.503 -20.013 -17.707 1.00 86.07 ? 299 ILE A CA 1 ATOM 2382 C C . ILE A 1 299 ? 30.357 -20.037 -18.714 1.00 88.82 ? 299 ILE A C 1 ATOM 2383 O O . ILE A 1 299 ? 29.929 -18.981 -19.185 1.00 89.00 ? 299 ILE A O 1 ATOM 2384 C CB . ILE A 1 299 ? 31.037 -19.613 -16.275 1.00 91.68 ? 299 ILE A CB 1 ATOM 2385 C CG1 . ILE A 1 299 ? 29.901 -20.513 -15.753 1.00 92.92 ? 299 ILE A CG1 1 ATOM 2386 C CG2 . ILE A 1 299 ? 30.595 -18.155 -16.207 1.00 93.99 ? 299 ILE A CG2 1 ATOM 2387 C CD1 . ILE A 1 299 ? 30.376 -21.746 -15.012 1.00 94.97 ? 299 ILE A CD1 1 ATOM 2388 N N . GLY A 1 300 ? 29.900 -21.239 -19.074 1.00 91.76 ? 300 GLY A N 1 ATOM 2389 C CA . GLY A 1 300 ? 28.793 -21.416 -20.021 1.00 94.44 ? 300 GLY A CA 1 ATOM 2390 C C . GLY A 1 300 ? 29.171 -22.105 -21.327 1.00 99.87 ? 300 GLY A C 1 ATOM 2391 O O . GLY A 1 300 ? 30.174 -22.820 -21.407 1.00 97.00 ? 300 GLY A O 1 ATOM 2392 N N . GLU A 1 301 ? 28.341 -21.888 -22.346 1.00 109.07 ? 301 GLU A N 1 ATOM 2393 C CA . GLU A 1 301 ? 28.564 -22.398 -23.700 1.00 114.75 ? 301 GLU A CA 1 ATOM 2394 C C . GLU A 1 301 ? 29.440 -21.395 -24.441 1.00 108.81 ? 301 GLU A C 1 ATOM 2395 O O . GLU A 1 301 ? 28.934 -20.491 -25.105 1.00 110.62 ? 301 GLU A O 1 ATOM 2396 C CB . GLU A 1 301 ? 27.219 -22.554 -24.426 1.00 124.97 ? 301 GLU A CB 1 ATOM 2397 C CG . GLU A 1 301 ? 27.307 -23.135 -25.837 1.00 136.87 ? 301 GLU A CG 1 ATOM 2398 C CD . GLU A 1 301 ? 27.014 -24.627 -25.906 1.00 146.34 ? 301 GLU A CD 1 ATOM 2399 O OE1 . GLU A 1 301 ? 27.105 -25.318 -24.866 1.00 153.98 ? 301 GLU A OE1 1 ATOM 2400 O OE2 . GLU A 1 301 ? 26.683 -25.110 -27.012 1.00 151.22 ? 301 GLU A OE2 1 ATOM 2401 N N . CYS A 1 302 ? 30.752 -21.559 -24.331 1.00 104.97 ? 302 CYS A N 1 ATOM 2402 C CA . CYS A 1 302 ? 31.682 -20.531 -24.778 1.00 102.32 ? 302 CYS A CA 1 ATOM 2403 C C . CYS A 1 302 ? 32.543 -20.942 -25.965 1.00 94.38 ? 302 CYS A C 1 ATOM 2404 O O . CYS A 1 302 ? 32.831 -22.122 -26.152 1.00 90.84 ? 302 CYS A O 1 ATOM 2405 C CB . CYS A 1 302 ? 32.587 -20.120 -23.618 1.00 106.66 ? 302 CYS A CB 1 ATOM 2406 S SG . CYS A 1 302 ? 31.725 -19.187 -22.329 1.00 121.45 ? 302 CYS A SG 1 ATOM 2407 N N . PRO A 1 303 ? 32.958 -19.956 -26.776 1.00 89.25 ? 303 PRO A N 1 ATOM 2408 C CA . PRO A 1 303 ? 34.037 -20.202 -27.733 1.00 88.84 ? 303 PRO A CA 1 ATOM 2409 C C . PRO A 1 303 ? 35.353 -20.501 -27.013 1.00 86.83 ? 303 PRO A C 1 ATOM 2410 O O . PRO A 1 303 ? 35.444 -20.324 -25.801 1.00 94.05 ? 303 PRO A O 1 ATOM 2411 C CB . PRO A 1 303 ? 34.132 -18.890 -28.528 1.00 87.94 ? 303 PRO A CB 1 ATOM 2412 C CG . PRO A 1 303 ? 32.877 -18.145 -28.251 1.00 89.61 ? 303 PRO A CG 1 ATOM 2413 C CD . PRO A 1 303 ? 32.349 -18.624 -26.935 1.00 88.78 ? 303 PRO A CD 1 ATOM 2414 N N . LYS A 1 304 ? 36.362 -20.943 -27.750 1.00 85.74 ? 304 LYS A N 1 ATOM 2415 C CA . LYS A 1 304 ? 37.628 -21.326 -27.147 1.00 87.95 ? 304 LYS A CA 1 ATOM 2416 C C . LYS A 1 304 ? 38.537 -20.120 -27.071 1.00 84.95 ? 304 LYS A C 1 ATOM 2417 O O . LYS A 1 304 ? 38.666 -19.375 -28.037 1.00 88.26 ? 304 LYS A O 1 ATOM 2418 C CB . LYS A 1 304 ? 38.295 -22.446 -27.942 1.00 93.93 ? 304 LYS A CB 1 ATOM 2419 C CG . LYS A 1 304 ? 37.387 -23.649 -28.199 1.00 105.23 ? 304 LYS A CG 1 ATOM 2420 C CD . LYS A 1 304 ? 37.065 -24.437 -26.927 1.00 110.38 ? 304 LYS A CD 1 ATOM 2421 C CE . LYS A 1 304 ? 35.614 -24.903 -26.898 1.00 113.72 ? 304 LYS A CE 1 ATOM 2422 N NZ . LYS A 1 304 ? 35.325 -25.726 -25.689 1.00 118.40 ? 304 LYS A NZ 1 ATOM 2423 N N . TYR A 1 305 ? 39.159 -19.920 -25.917 1.00 76.95 ? 305 TYR A N 1 ATOM 2424 C CA . TYR A 1 305 ? 40.004 -18.772 -25.746 1.00 73.45 ? 305 TYR A CA 1 ATOM 2425 C C . TYR A 1 305 ? 41.324 -19.010 -26.439 1.00 76.13 ? 305 TYR A C 1 ATOM 2426 O O . TYR A 1 305 ? 41.946 -20.045 -26.239 1.00 83.72 ? 305 TYR A O 1 ATOM 2427 C CB . TYR A 1 305 ? 40.245 -18.467 -24.269 1.00 72.71 ? 305 TYR A CB 1 ATOM 2428 C CG . TYR A 1 305 ? 41.151 -17.276 -24.069 1.00 71.13 ? 305 TYR A CG 1 ATOM 2429 C CD1 . TYR A 1 305 ? 40.705 -15.990 -24.341 1.00 71.01 ? 305 TYR A CD1 1 ATOM 2430 C CD2 . TYR A 1 305 ? 42.459 -17.435 -23.639 1.00 70.48 ? 305 TYR A CD2 1 ATOM 2431 C CE1 . TYR A 1 305 ? 41.540 -14.899 -24.180 1.00 72.76 ? 305 TYR A CE1 1 ATOM 2432 C CE2 . TYR A 1 305 ? 43.295 -16.346 -23.469 1.00 71.34 ? 305 TYR A CE2 1 ATOM 2433 C CZ . TYR A 1 305 ? 42.829 -15.081 -23.746 1.00 71.84 ? 305 TYR A CZ 1 ATOM 2434 O OH . TYR A 1 305 ? 43.643 -13.988 -23.591 1.00 74.54 ? 305 TYR A OH 1 ATOM 2435 N N . VAL A 1 306 ? 41.737 -18.052 -27.266 1.00 79.38 ? 306 VAL A N 1 ATOM 2436 C CA . VAL A 1 306 ? 43.116 -17.981 -27.769 1.00 74.20 ? 306 VAL A CA 1 ATOM 2437 C C . VAL A 1 306 ? 43.661 -16.588 -27.512 1.00 73.03 ? 306 VAL A C 1 ATOM 2438 O O . VAL A 1 306 ? 42.902 -15.648 -27.317 1.00 80.39 ? 306 VAL A O 1 ATOM 2439 C CB . VAL A 1 306 ? 43.216 -18.314 -29.273 1.00 72.06 ? 306 VAL A CB 1 ATOM 2440 C CG1 . VAL A 1 306 ? 42.760 -19.741 -29.521 1.00 73.25 ? 306 VAL A CG1 1 ATOM 2441 C CG2 . VAL A 1 306 ? 42.397 -17.347 -30.114 1.00 72.08 ? 306 VAL A CG2 1 ATOM 2442 N N . LYS A 1 307 ? 44.979 -16.460 -27.529 1.00 76.15 ? 307 LYS A N 1 ATOM 2443 C CA . LYS A 1 307 ? 45.637 -15.181 -27.309 1.00 79.41 ? 307 LYS A CA 1 ATOM 2444 C C . LYS A 1 307 ? 45.876 -14.352 -28.581 1.00 80.94 ? 307 LYS A C 1 ATOM 2445 O O . LYS A 1 307 ? 46.593 -13.366 -28.522 1.00 93.95 ? 307 LYS A O 1 ATOM 2446 C CB . LYS A 1 307 ? 46.970 -15.414 -26.589 1.00 84.01 ? 307 LYS A CB 1 ATOM 2447 C CG . LYS A 1 307 ? 46.827 -15.484 -25.082 1.00 91.20 ? 307 LYS A CG 1 ATOM 2448 C CD . LYS A 1 307 ? 48.010 -16.174 -24.421 1.00 98.32 ? 307 LYS A CD 1 ATOM 2449 C CE . LYS A 1 307 ? 49.294 -15.381 -24.581 1.00 103.71 ? 307 LYS A CE 1 ATOM 2450 N NZ . LYS A 1 307 ? 50.421 -15.995 -23.823 1.00 108.66 ? 307 LYS A NZ 1 ATOM 2451 N N . SER A 1 308 ? 45.281 -14.719 -29.715 1.00 81.49 ? 308 SER A N 1 ATOM 2452 C CA . SER A 1 308 ? 45.511 -13.992 -30.978 1.00 81.67 ? 308 SER A CA 1 ATOM 2453 C C . SER A 1 308 ? 44.793 -12.652 -31.015 1.00 79.86 ? 308 SER A C 1 ATOM 2454 O O . SER A 1 308 ? 43.809 -12.451 -30.315 1.00 81.95 ? 308 SER A O 1 ATOM 2455 C CB . SER A 1 308 ? 45.033 -14.807 -32.192 1.00 79.58 ? 308 SER A CB 1 ATOM 2456 O OG . SER A 1 308 ? 45.272 -16.186 -32.018 1.00 82.81 ? 308 SER A OG 1 ATOM 2457 N N . ASN A 1 309 ? 45.278 -11.756 -31.868 1.00 83.54 ? 309 ASN A N 1 ATOM 2458 C CA . ASN A 1 309 ? 44.570 -10.515 -32.191 1.00 86.97 ? 309 ASN A CA 1 ATOM 2459 C C . ASN A 1 309 ? 43.728 -10.628 -33.454 1.00 81.38 ? 309 ASN A C 1 ATOM 2460 O O . ASN A 1 309 ? 42.883 -9.770 -33.721 1.00 80.34 ? 309 ASN A O 1 ATOM 2461 C CB . ASN A 1 309 ? 45.573 -9.378 -32.352 1.00 95.00 ? 309 ASN A CB 1 ATOM 2462 C CG . ASN A 1 309 ? 46.231 -9.001 -31.036 1.00 106.12 ? 309 ASN A CG 1 ATOM 2463 O OD1 . ASN A 1 309 ? 45.545 -8.714 -30.044 1.00 107.42 ? 309 ASN A OD1 1 ATOM 2464 N ND2 . ASN A 1 309 ? 47.567 -8.998 -31.014 1.00 110.52 ? 309 ASN A ND2 1 ATOM 2465 N N . ARG A 1 310 ? 43.951 -11.699 -34.214 1.00 78.23 ? 310 ARG A N 1 ATOM 2466 C CA . ARG A 1 310 ? 43.383 -11.847 -35.548 1.00 76.10 ? 310 ARG A CA 1 ATOM 2467 C C . ARG A 1 310 ? 43.414 -13.316 -36.008 1.00 74.13 ? 310 ARG A C 1 ATOM 2468 O O . ARG A 1 310 ? 44.472 -13.954 -35.984 1.00 71.76 ? 310 ARG A O 1 ATOM 2469 C CB . ARG A 1 310 ? 44.192 -10.986 -36.519 1.00 78.56 ? 310 ARG A CB 1 ATOM 2470 C CG . ARG A 1 310 ? 43.516 -10.745 -37.848 1.00 85.25 ? 310 ARG A CG 1 ATOM 2471 C CD . ARG A 1 310 ? 44.442 -10.077 -38.854 1.00 91.62 ? 310 ARG A CD 1 ATOM 2472 N NE . ARG A 1 310 ? 43.968 -10.315 -40.216 1.00 96.14 ? 310 ARG A NE 1 ATOM 2473 C CZ . ARG A 1 310 ? 42.899 -9.730 -40.758 1.00 101.03 ? 310 ARG A CZ 1 ATOM 2474 N NH1 . ARG A 1 310 ? 42.170 -8.850 -40.073 1.00 100.80 ? 310 ARG A NH1 1 ATOM 2475 N NH2 . ARG A 1 310 ? 42.552 -10.028 -42.002 1.00 103.45 ? 310 ARG A NH2 1 ATOM 2476 N N . LEU A 1 311 ? 42.256 -13.848 -36.404 1.00 70.02 ? 311 LEU A N 1 ATOM 2477 C CA . LEU A 1 311 ? 42.165 -15.162 -37.068 1.00 69.20 ? 311 LEU A CA 1 ATOM 2478 C C . LEU A 1 311 ? 41.120 -15.131 -38.182 1.00 69.51 ? 311 LEU A C 1 ATOM 2479 O O . LEU A 1 311 ? 39.909 -15.128 -37.932 1.00 69.94 ? 311 LEU A O 1 ATOM 2480 C CB . LEU A 1 311 ? 41.798 -16.278 -36.094 1.00 68.45 ? 311 LEU A CB 1 ATOM 2481 C CG . LEU A 1 311 ? 42.801 -16.669 -35.017 1.00 66.76 ? 311 LEU A CG 1 ATOM 2482 C CD1 . LEU A 1 311 ? 42.160 -17.667 -34.063 1.00 65.51 ? 311 LEU A CD1 1 ATOM 2483 C CD2 . LEU A 1 311 ? 44.062 -17.244 -35.633 1.00 67.50 ? 311 LEU A CD2 1 ATOM 2484 N N . VAL A 1 312 ? 41.606 -15.134 -39.413 1.00 68.45 ? 312 VAL A N 1 ATOM 2485 C CA . VAL A 1 312 ? 40.760 -14.975 -40.572 1.00 68.39 ? 312 VAL A CA 1 ATOM 2486 C C . VAL A 1 312 ? 41.106 -16.027 -41.600 1.00 66.90 ? 312 VAL A C 1 ATOM 2487 O O . VAL A 1 312 ? 42.250 -16.106 -42.038 1.00 66.68 ? 312 VAL A O 1 ATOM 2488 C CB . VAL A 1 312 ? 40.966 -13.590 -41.191 1.00 69.09 ? 312 VAL A CB 1 ATOM 2489 C CG1 . VAL A 1 312 ? 40.119 -13.433 -42.448 1.00 69.57 ? 312 VAL A CG1 1 ATOM 2490 C CG2 . VAL A 1 312 ? 40.650 -12.515 -40.154 1.00 69.08 ? 312 VAL A CG2 1 ATOM 2491 N N . LEU A 1 313 ? 40.105 -16.822 -41.972 1.00 67.31 ? 313 LEU A N 1 ATOM 2492 C CA . LEU A 1 313 ? 40.245 -17.853 -42.989 1.00 68.63 ? 313 LEU A CA 1 ATOM 2493 C C . LEU A 1 313 ? 39.919 -17.319 -44.364 1.00 67.84 ? 313 LEU A C 1 ATOM 2494 O O . LEU A 1 313 ? 38.937 -16.604 -44.538 1.00 68.47 ? 313 LEU A O 1 ATOM 2495 C CB . LEU A 1 313 ? 39.295 -19.024 -42.708 1.00 69.73 ? 313 LEU A CB 1 ATOM 2496 C CG . LEU A 1 313 ? 39.768 -20.028 -41.662 1.00 71.18 ? 313 LEU A CG 1 ATOM 2497 C CD1 . LEU A 1 313 ? 38.690 -21.067 -41.407 1.00 71.39 ? 313 LEU A CD1 1 ATOM 2498 C CD2 . LEU A 1 313 ? 41.061 -20.690 -42.115 1.00 71.51 ? 313 LEU A CD2 1 ATOM 2499 N N . ALA A 1 314 ? 40.730 -17.695 -45.345 1.00 66.90 ? 314 ALA A N 1 ATOM 2500 C CA . ALA A 1 314 ? 40.398 -17.448 -46.734 1.00 65.55 ? 314 ALA A CA 1 ATOM 2501 C C . ALA A 1 314 ? 39.298 -18.407 -47.101 1.00 68.04 ? 314 ALA A C 1 ATOM 2502 O O . ALA A 1 314 ? 39.361 -19.582 -46.747 1.00 69.14 ? 314 ALA A O 1 ATOM 2503 C CB . ALA A 1 314 ? 41.600 -17.687 -47.624 1.00 65.35 ? 314 ALA A CB 1 ATOM 2504 N N . THR A 1 315 ? 38.282 -17.898 -47.783 1.00 69.28 ? 315 THR A N 1 ATOM 2505 C CA . THR A 1 315 ? 37.301 -18.744 -48.448 1.00 72.69 ? 315 THR A CA 1 ATOM 2506 C C . THR A 1 315 ? 37.396 -18.546 -49.945 1.00 69.57 ? 315 THR A C 1 ATOM 2507 O O . THR A 1 315 ? 37.410 -19.501 -50.708 1.00 69.53 ? 315 THR A O 1 ATOM 2508 C CB . THR A 1 315 ? 35.875 -18.414 -47.997 1.00 74.64 ? 315 THR A CB 1 ATOM 2509 O OG1 . THR A 1 315 ? 35.692 -16.992 -47.996 1.00 80.28 ? 315 THR A OG1 1 ATOM 2510 C CG2 . THR A 1 315 ? 35.639 -18.960 -46.603 1.00 75.51 ? 315 THR A CG2 1 ATOM 2511 N N . GLY A 1 316 ? 37.459 -17.292 -50.358 1.00 67.35 ? 316 GLY A N 1 ATOM 2512 C CA . GLY A 1 316 ? 37.564 -16.964 -51.755 1.00 67.45 ? 316 GLY A CA 1 ATOM 2513 C C . GLY A 1 316 ? 38.977 -17.081 -52.263 1.00 65.68 ? 316 GLY A C 1 ATOM 2514 O O . GLY A 1 316 ? 39.834 -17.683 -51.636 1.00 64.25 ? 316 GLY A O 1 ATOM 2515 N N . LEU A 1 317 ? 39.220 -16.483 -53.413 1.00 71.60 ? 317 LEU A N 1 ATOM 2516 C CA . LEU A 1 317 ? 40.518 -16.581 -54.045 1.00 73.50 ? 317 LEU A CA 1 ATOM 2517 C C . LEU A 1 317 ? 41.214 -15.226 -54.030 1.00 70.05 ? 317 LEU A C 1 ATOM 2518 O O . LEU A 1 317 ? 40.642 -14.220 -53.632 1.00 67.75 ? 317 LEU A O 1 ATOM 2519 C CB . LEU A 1 317 ? 40.392 -17.181 -55.460 1.00 74.29 ? 317 LEU A CB 1 ATOM 2520 C CG . LEU A 1 317 ? 39.291 -16.712 -56.403 1.00 75.26 ? 317 LEU A CG 1 ATOM 2521 C CD1 . LEU A 1 317 ? 39.632 -15.340 -56.940 1.00 82.29 ? 317 LEU A CD1 1 ATOM 2522 C CD2 . LEU A 1 317 ? 39.122 -17.673 -57.560 1.00 75.24 ? 317 LEU A CD2 1 ATOM 2523 N N . ARG A 1 318 ? 42.474 -15.237 -54.428 1.00 71.26 ? 318 ARG A N 1 ATOM 2524 C CA . ARG A 1 318 ? 43.297 -14.045 -54.449 1.00 72.72 ? 318 ARG A CA 1 ATOM 2525 C C . ARG A 1 318 ? 42.661 -13.011 -55.349 1.00 69.11 ? 318 ARG A C 1 ATOM 2526 O O . ARG A 1 318 ? 42.450 -13.258 -56.530 1.00 67.41 ? 318 ARG A O 1 ATOM 2527 C CB . ARG A 1 318 ? 44.709 -14.397 -54.941 1.00 76.10 ? 318 ARG A CB 1 ATOM 2528 C CG . ARG A 1 318 ? 45.647 -13.210 -55.093 1.00 80.78 ? 318 ARG A CG 1 ATOM 2529 C CD . ARG A 1 318 ? 46.964 -13.645 -55.701 1.00 80.89 ? 318 ARG A CD 1 ATOM 2530 N NE . ARG A 1 318 ? 47.689 -14.513 -54.779 1.00 84.71 ? 318 ARG A NE 1 ATOM 2531 C CZ . ARG A 1 318 ? 48.557 -14.094 -53.862 1.00 88.06 ? 318 ARG A CZ 1 ATOM 2532 N NH1 . ARG A 1 318 ? 48.836 -12.796 -53.723 1.00 88.28 ? 318 ARG A NH1 1 ATOM 2533 N NH2 . ARG A 1 318 ? 49.155 -14.985 -53.075 1.00 88.14 ? 318 ARG A NH2 1 ATOM 2534 N N . ASN A 1 319 ? 42.368 -11.854 -54.771 1.00 75.41 ? 319 ASN A N 1 ATOM 2535 C CA . ASN A 1 319 ? 41.703 -10.755 -55.465 1.00 79.05 ? 319 ASN A CA 1 ATOM 2536 C C . ASN A 1 319 ? 42.729 -9.892 -56.182 1.00 88.97 ? 319 ASN A C 1 ATOM 2537 O O . ASN A 1 319 ? 43.742 -9.495 -55.601 1.00 91.58 ? 319 ASN A O 1 ATOM 2538 C CB . ASN A 1 319 ? 40.923 -9.905 -54.462 1.00 75.60 ? 319 ASN A CB 1 ATOM 2539 C CG . ASN A 1 319 ? 39.769 -9.155 -55.093 1.00 74.62 ? 319 ASN A CG 1 ATOM 2540 O OD1 . ASN A 1 319 ? 39.475 -9.309 -56.274 1.00 71.99 ? 319 ASN A OD1 1 ATOM 2541 N ND2 . ASN A 1 319 ? 39.096 -8.338 -54.291 1.00 75.32 ? 319 ASN A ND2 1 ATOM 2542 N N . SER A 1 320 ? 42.461 -9.610 -57.450 1.00 104.60 ? 320 SER A N 1 ATOM 2543 C CA . SER A 1 320 ? 43.409 -8.907 -58.307 1.00 117.04 ? 320 SER A CA 1 ATOM 2544 C C . SER A 1 320 ? 43.105 -7.400 -58.350 1.00 125.04 ? 320 SER A C 1 ATOM 2545 O O . SER A 1 320 ? 41.937 -7.009 -58.314 1.00 122.82 ? 320 SER A O 1 ATOM 2546 C CB . SER A 1 320 ? 43.366 -9.511 -59.717 1.00 116.52 ? 320 SER A CB 1 ATOM 2547 O OG . SER A 1 320 ? 42.059 -9.960 -60.037 1.00 108.70 ? 320 SER A OG 1 ATOM 2548 N N . PRO A 1 321 ? 44.157 -6.551 -58.396 1.00 136.64 ? 321 PRO A N 1 ATOM 2549 C CA . PRO A 1 321 ? 43.950 -5.119 -58.664 1.00 138.40 ? 321 PRO A CA 1 ATOM 2550 C C . PRO A 1 321 ? 43.487 -4.850 -60.093 1.00 135.31 ? 321 PRO A C 1 ATOM 2551 O O . PRO A 1 321 ? 42.829 -3.841 -60.342 1.00 138.65 ? 321 PRO A O 1 ATOM 2552 C CB . PRO A 1 321 ? 45.337 -4.504 -58.431 1.00 138.51 ? 321 PRO A CB 1 ATOM 2553 C CG . PRO A 1 321 ? 46.052 -5.474 -57.555 1.00 139.46 ? 321 PRO A CG 1 ATOM 2554 C CD . PRO A 1 321 ? 45.536 -6.827 -57.949 1.00 138.85 ? 321 PRO A CD 1 ATOM 2555 N N . GLY B 2 1 ? 50.728 -18.554 -57.669 1.00 80.04 ? 1 GLY B N 1 ATOM 2556 C CA . GLY B 2 1 ? 50.335 -19.798 -56.948 1.00 76.05 ? 1 GLY B CA 1 ATOM 2557 C C . GLY B 2 1 ? 51.020 -21.022 -57.522 1.00 73.15 ? 1 GLY B C 1 ATOM 2558 O O . GLY B 2 1 ? 51.711 -20.955 -58.547 1.00 73.66 ? 1 GLY B O 1 ATOM 2559 N N . LEU B 2 2 ? 50.819 -22.154 -56.869 1.00 67.26 ? 2 LEU B N 1 ATOM 2560 C CA . LEU B 2 2 ? 51.521 -23.353 -57.268 1.00 66.85 ? 2 LEU B CA 1 ATOM 2561 C C . LEU B 2 2 ? 51.140 -23.831 -58.664 1.00 66.06 ? 2 LEU B C 1 ATOM 2562 O O . LEU B 2 2 ? 51.964 -24.408 -59.361 1.00 65.97 ? 2 LEU B O 1 ATOM 2563 C CB . LEU B 2 2 ? 51.268 -24.465 -56.269 1.00 65.30 ? 2 LEU B CB 1 ATOM 2564 C CG . LEU B 2 2 ? 51.887 -24.255 -54.900 1.00 62.56 ? 2 LEU B CG 1 ATOM 2565 C CD1 . LEU B 2 2 ? 51.443 -25.377 -53.982 1.00 61.23 ? 2 LEU B CD1 1 ATOM 2566 C CD2 . LEU B 2 2 ? 53.403 -24.181 -54.993 1.00 63.35 ? 2 LEU B CD2 1 ATOM 2567 N N . PHE B 2 3 ? 49.904 -23.580 -59.080 1.00 64.21 ? 3 PHE B N 1 ATOM 2568 C CA . PHE B 2 3 ? 49.396 -24.201 -60.302 1.00 65.72 ? 3 PHE B CA 1 ATOM 2569 C C . PHE B 2 3 ? 49.504 -23.311 -61.517 1.00 69.19 ? 3 PHE B C 1 ATOM 2570 O O . PHE B 2 3 ? 49.217 -23.739 -62.629 1.00 74.77 ? 3 PHE B O 1 ATOM 2571 C CB . PHE B 2 3 ? 47.996 -24.761 -60.054 1.00 63.14 ? 3 PHE B CB 1 ATOM 2572 C CG . PHE B 2 3 ? 48.017 -25.874 -59.045 1.00 62.71 ? 3 PHE B CG 1 ATOM 2573 C CD1 . PHE B 2 3 ? 47.939 -25.597 -57.691 1.00 62.51 ? 3 PHE B CD1 1 ATOM 2574 C CD2 . PHE B 2 3 ? 48.249 -27.177 -59.442 1.00 62.53 ? 3 PHE B CD2 1 ATOM 2575 C CE1 . PHE B 2 3 ? 48.034 -26.609 -56.754 1.00 61.16 ? 3 PHE B CE1 1 ATOM 2576 C CE2 . PHE B 2 3 ? 48.345 -28.190 -58.511 1.00 64.49 ? 3 PHE B CE2 1 ATOM 2577 C CZ . PHE B 2 3 ? 48.237 -27.907 -57.166 1.00 61.75 ? 3 PHE B CZ 1 ATOM 2578 N N . GLY B 2 4 ? 49.967 -22.083 -61.291 1.00 71.67 ? 4 GLY B N 1 ATOM 2579 C CA . GLY B 2 4 ? 50.369 -21.188 -62.356 1.00 70.69 ? 4 GLY B CA 1 ATOM 2580 C C . GLY B 2 4 ? 49.261 -20.417 -63.032 1.00 69.97 ? 4 GLY B C 1 ATOM 2581 O O . GLY B 2 4 ? 49.545 -19.606 -63.901 1.00 76.26 ? 4 GLY B O 1 ATOM 2582 N N . ALA B 2 5 ? 48.006 -20.643 -62.657 1.00 67.65 ? 5 ALA B N 1 ATOM 2583 C CA . ALA B 2 5 ? 46.889 -20.013 -63.376 1.00 66.64 ? 5 ALA B CA 1 ATOM 2584 C C . ALA B 2 5 ? 46.547 -18.652 -62.811 1.00 66.41 ? 5 ALA B C 1 ATOM 2585 O O . ALA B 2 5 ? 46.682 -17.645 -63.499 1.00 68.87 ? 5 ALA B O 1 ATOM 2586 C CB . ALA B 2 5 ? 45.658 -20.905 -63.365 1.00 66.15 ? 5 ALA B CB 1 ATOM 2587 N N . ILE B 2 6 ? 46.094 -18.630 -61.560 1.00 65.54 ? 6 ILE B N 1 ATOM 2588 C CA . ILE B 2 6 ? 45.657 -17.396 -60.923 1.00 67.14 ? 6 ILE B CA 1 ATOM 2589 C C . ILE B 2 6 ? 46.843 -16.460 -60.705 1.00 67.98 ? 6 ILE B C 1 ATOM 2590 O O . ILE B 2 6 ? 47.820 -16.830 -60.059 1.00 68.65 ? 6 ILE B O 1 ATOM 2591 C CB . ILE B 2 6 ? 44.926 -17.672 -59.596 1.00 66.33 ? 6 ILE B CB 1 ATOM 2592 C CG1 . ILE B 2 6 ? 43.575 -18.305 -59.897 1.00 66.89 ? 6 ILE B CG1 1 ATOM 2593 C CG2 . ILE B 2 6 ? 44.717 -16.383 -58.810 1.00 66.56 ? 6 ILE B CG2 1 ATOM 2594 C CD1 . ILE B 2 6 ? 42.840 -18.812 -58.676 1.00 68.46 ? 6 ILE B CD1 1 ATOM 2595 N N . ALA B 2 7 ? 46.729 -15.249 -61.252 1.00 69.27 ? 7 ALA B N 1 ATOM 2596 C CA . ALA B 2 7 ? 47.805 -14.257 -61.248 1.00 71.67 ? 7 ALA B CA 1 ATOM 2597 C C . ALA B 2 7 ? 49.091 -14.874 -61.785 1.00 75.89 ? 7 ALA B C 1 ATOM 2598 O O . ALA B 2 7 ? 50.183 -14.656 -61.249 1.00 76.12 ? 7 ALA B O 1 ATOM 2599 C CB . ALA B 2 7 ? 48.008 -13.688 -59.851 1.00 70.92 ? 7 ALA B CB 1 ATOM 2600 N N . GLY B 2 8 ? 48.928 -15.667 -62.839 1.00 76.53 ? 8 GLY B N 1 ATOM 2601 C CA . GLY B 2 8 ? 50.026 -16.298 -63.537 1.00 77.72 ? 8 GLY B CA 1 ATOM 2602 C C . GLY B 2 8 ? 49.777 -16.075 -65.009 1.00 79.65 ? 8 GLY B C 1 ATOM 2603 O O . GLY B 2 8 ? 49.829 -14.940 -65.466 1.00 86.92 ? 8 GLY B O 1 ATOM 2604 N N . PHE B 2 9 ? 49.472 -17.138 -65.751 1.00 77.38 ? 9 PHE B N 1 ATOM 2605 C CA . PHE B 2 9 ? 49.202 -16.995 -67.172 1.00 76.62 ? 9 PHE B CA 1 ATOM 2606 C C . PHE B 2 9 ? 47.818 -16.392 -67.392 1.00 76.31 ? 9 PHE B C 1 ATOM 2607 O O . PHE B 2 9 ? 47.522 -15.913 -68.483 1.00 78.78 ? 9 PHE B O 1 ATOM 2608 C CB . PHE B 2 9 ? 49.430 -18.304 -67.957 1.00 79.12 ? 9 PHE B CB 1 ATOM 2609 C CG . PHE B 2 9 ? 48.450 -19.398 -67.656 1.00 78.55 ? 9 PHE B CG 1 ATOM 2610 C CD1 . PHE B 2 9 ? 47.198 -19.407 -68.242 1.00 80.88 ? 9 PHE B CD1 1 ATOM 2611 C CD2 . PHE B 2 9 ? 48.801 -20.449 -66.827 1.00 81.71 ? 9 PHE B CD2 1 ATOM 2612 C CE1 . PHE B 2 9 ? 46.292 -20.419 -67.971 1.00 81.54 ? 9 PHE B CE1 1 ATOM 2613 C CE2 . PHE B 2 9 ? 47.904 -21.468 -66.552 1.00 81.79 ? 9 PHE B CE2 1 ATOM 2614 C CZ . PHE B 2 9 ? 46.645 -21.450 -67.123 1.00 80.58 ? 9 PHE B CZ 1 ATOM 2615 N N . ILE B 2 10 ? 46.975 -16.422 -66.361 1.00 73.94 ? 10 ILE B N 1 ATOM 2616 C CA . ILE B 2 10 ? 45.784 -15.582 -66.330 1.00 74.50 ? 10 ILE B CA 1 ATOM 2617 C C . ILE B 2 10 ? 46.099 -14.427 -65.383 1.00 78.75 ? 10 ILE B C 1 ATOM 2618 O O . ILE B 2 10 ? 46.101 -14.594 -64.165 1.00 79.73 ? 10 ILE B O 1 ATOM 2619 C CB . ILE B 2 10 ? 44.526 -16.351 -65.882 1.00 72.23 ? 10 ILE B CB 1 ATOM 2620 C CG1 . ILE B 2 10 ? 44.332 -17.603 -66.735 1.00 71.09 ? 10 ILE B CG1 1 ATOM 2621 C CG2 . ILE B 2 10 ? 43.292 -15.477 -66.021 1.00 70.86 ? 10 ILE B CG2 1 ATOM 2622 C CD1 . ILE B 2 10 ? 43.238 -18.514 -66.234 1.00 70.20 ? 10 ILE B CD1 1 ATOM 2623 N N . GLU B 2 11 ? 46.393 -13.266 -65.967 1.00 85.83 ? 11 GLU B N 1 ATOM 2624 C CA . GLU B 2 11 ? 46.879 -12.089 -65.233 1.00 90.36 ? 11 GLU B CA 1 ATOM 2625 C C . GLU B 2 11 ? 46.001 -11.667 -64.065 1.00 85.12 ? 11 GLU B C 1 ATOM 2626 O O . GLU B 2 11 ? 46.500 -11.334 -62.990 1.00 86.84 ? 11 GLU B O 1 ATOM 2627 C CB . GLU B 2 11 ? 47.005 -10.888 -66.176 1.00 102.57 ? 11 GLU B CB 1 ATOM 2628 C CG . GLU B 2 11 ? 48.419 -10.549 -66.620 1.00 113.33 ? 11 GLU B CG 1 ATOM 2629 C CD . GLU B 2 11 ? 48.471 -9.227 -67.376 1.00 124.98 ? 11 GLU B CD 1 ATOM 2630 O OE1 . GLU B 2 11 ? 47.652 -9.036 -68.308 1.00 127.00 ? 11 GLU B OE1 1 ATOM 2631 O OE2 . GLU B 2 11 ? 49.323 -8.375 -67.032 1.00 134.44 ? 11 GLU B OE2 1 ATOM 2632 N N . GLY B 2 12 ? 44.695 -11.653 -64.286 1.00 81.56 ? 12 GLY B N 1 ATOM 2633 C CA . GLY B 2 12 ? 43.775 -11.120 -63.292 1.00 81.14 ? 12 GLY B CA 1 ATOM 2634 C C . GLY B 2 12 ? 42.380 -11.694 -63.373 1.00 78.26 ? 12 GLY B C 1 ATOM 2635 O O . GLY B 2 12 ? 42.010 -12.342 -64.352 1.00 76.22 ? 12 GLY B O 1 ATOM 2636 N N . GLY B 2 13 ? 41.609 -11.457 -62.321 1.00 78.09 ? 13 GLY B N 1 ATOM 2637 C CA . GLY B 2 13 ? 40.224 -11.903 -62.264 1.00 79.73 ? 13 GLY B CA 1 ATOM 2638 C C . GLY B 2 13 ? 39.255 -10.975 -62.987 1.00 79.13 ? 13 GLY B C 1 ATOM 2639 O O . GLY B 2 13 ? 39.649 -9.930 -63.507 1.00 79.25 ? 13 GLY B O 1 ATOM 2640 N N . TRP B 2 14 ? 37.983 -11.377 -62.993 1.00 76.90 ? 14 TRP B N 1 ATOM 2641 C CA . TRP B 2 14 ? 36.930 -10.712 -63.731 1.00 74.75 ? 14 TRP B CA 1 ATOM 2642 C C . TRP B 2 14 ? 35.893 -10.133 -62.792 1.00 78.96 ? 14 TRP B C 1 ATOM 2643 O O . TRP B 2 14 ? 35.119 -10.872 -62.177 1.00 76.64 ? 14 TRP B O 1 ATOM 2644 C CB . TRP B 2 14 ? 36.244 -11.703 -64.674 1.00 71.52 ? 14 TRP B CB 1 ATOM 2645 C CG . TRP B 2 14 ? 37.104 -12.150 -65.813 1.00 70.25 ? 14 TRP B CG 1 ATOM 2646 C CD1 . TRP B 2 14 ? 38.151 -11.470 -66.371 1.00 68.99 ? 14 TRP B CD1 1 ATOM 2647 C CD2 . TRP B 2 14 ? 36.978 -13.370 -66.557 1.00 69.36 ? 14 TRP B CD2 1 ATOM 2648 N NE1 . TRP B 2 14 ? 38.688 -12.199 -67.407 1.00 69.56 ? 14 TRP B NE1 1 ATOM 2649 C CE2 . TRP B 2 14 ? 37.987 -13.367 -67.540 1.00 68.61 ? 14 TRP B CE2 1 ATOM 2650 C CE3 . TRP B 2 14 ? 36.114 -14.468 -66.481 1.00 69.16 ? 14 TRP B CE3 1 ATOM 2651 C CZ2 . TRP B 2 14 ? 38.156 -14.416 -68.436 1.00 69.69 ? 14 TRP B CZ2 1 ATOM 2652 C CZ3 . TRP B 2 14 ? 36.281 -15.510 -67.377 1.00 68.48 ? 14 TRP B CZ3 1 ATOM 2653 C CH2 . TRP B 2 14 ? 37.294 -15.477 -68.341 1.00 69.16 ? 14 TRP B CH2 1 ATOM 2654 N N . GLN B 2 15 ? 35.870 -8.804 -62.696 1.00 83.75 ? 15 GLN B N 1 ATOM 2655 C CA . GLN B 2 15 ? 34.778 -8.106 -62.019 1.00 88.92 ? 15 GLN B CA 1 ATOM 2656 C C . GLN B 2 15 ? 33.442 -8.494 -62.662 1.00 89.26 ? 15 GLN B C 1 ATOM 2657 O O . GLN B 2 15 ? 32.420 -8.584 -61.983 1.00 92.75 ? 15 GLN B O 1 ATOM 2658 C CB . GLN B 2 15 ? 34.958 -6.589 -62.113 1.00 93.76 ? 15 GLN B CB 1 ATOM 2659 C CG . GLN B 2 15 ? 36.189 -6.037 -61.411 1.00 96.90 ? 15 GLN B CG 1 ATOM 2660 C CD . GLN B 2 15 ? 36.005 -5.901 -59.914 1.00 100.66 ? 15 GLN B CD 1 ATOM 2661 O OE1 . GLN B 2 15 ? 35.125 -5.181 -59.442 1.00 105.14 ? 15 GLN B OE1 1 ATOM 2662 N NE2 . GLN B 2 15 ? 36.851 -6.585 -59.157 1.00 102.39 ? 15 GLN B NE2 1 ATOM 2663 N N . GLY B 2 16 ? 33.466 -8.724 -63.973 1.00 88.74 ? 16 GLY B N 1 ATOM 2664 C CA . GLY B 2 16 ? 32.258 -9.003 -64.742 1.00 92.20 ? 16 GLY B CA 1 ATOM 2665 C C . GLY B 2 16 ? 31.572 -10.318 -64.429 1.00 92.97 ? 16 GLY B C 1 ATOM 2666 O O . GLY B 2 16 ? 30.358 -10.441 -64.610 1.00 94.08 ? 16 GLY B O 1 ATOM 2667 N N . MET B 2 17 ? 32.336 -11.308 -63.975 1.00 92.54 ? 17 MET B N 1 ATOM 2668 C CA . MET B 2 17 ? 31.755 -12.598 -63.625 1.00 93.68 ? 17 MET B CA 1 ATOM 2669 C C . MET B 2 17 ? 31.339 -12.600 -62.160 1.00 95.49 ? 17 MET B C 1 ATOM 2670 O O . MET B 2 17 ? 32.175 -12.632 -61.257 1.00 97.08 ? 17 MET B O 1 ATOM 2671 C CB . MET B 2 17 ? 32.721 -13.738 -63.897 1.00 92.48 ? 17 MET B CB 1 ATOM 2672 C CG . MET B 2 17 ? 32.080 -15.092 -63.660 1.00 94.81 ? 17 MET B CG 1 ATOM 2673 S SD . MET B 2 17 ? 33.067 -16.430 -64.322 1.00 92.93 ? 17 MET B SD 1 ATOM 2674 C CE . MET B 2 17 ? 34.558 -16.191 -63.361 1.00 93.69 ? 17 MET B CE 1 ATOM 2675 N N . VAL B 2 18 ? 30.032 -12.579 -61.947 1.00 97.76 ? 18 VAL B N 1 ATOM 2676 C CA . VAL B 2 18 ? 29.456 -12.376 -60.630 1.00 98.35 ? 18 VAL B CA 1 ATOM 2677 C C . VAL B 2 18 ? 28.774 -13.637 -60.096 1.00 97.17 ? 18 VAL B C 1 ATOM 2678 O O . VAL B 2 18 ? 28.618 -13.778 -58.892 1.00 97.88 ? 18 VAL B O 1 ATOM 2679 C CB . VAL B 2 18 ? 28.434 -11.219 -60.673 1.00 102.07 ? 18 VAL B CB 1 ATOM 2680 C CG1 . VAL B 2 18 ? 28.088 -10.752 -59.268 1.00 108.45 ? 18 VAL B CG1 1 ATOM 2681 C CG2 . VAL B 2 18 ? 28.984 -10.055 -61.484 1.00 102.42 ? 18 VAL B CG2 1 ATOM 2682 N N . ASP B 2 19 ? 28.390 -14.558 -60.979 1.00 98.22 ? 19 ASP B N 1 ATOM 2683 C CA . ASP B 2 19 ? 27.563 -15.714 -60.595 1.00 96.58 ? 19 ASP B CA 1 ATOM 2684 C C . ASP B 2 19 ? 28.369 -17.000 -60.337 1.00 90.82 ? 19 ASP B C 1 ATOM 2685 O O . ASP B 2 19 ? 27.801 -18.088 -60.294 1.00 90.92 ? 19 ASP B O 1 ATOM 2686 C CB . ASP B 2 19 ? 26.461 -15.957 -61.650 1.00 100.12 ? 19 ASP B CB 1 ATOM 2687 C CG . ASP B 2 19 ? 27.017 -16.301 -63.038 1.00 102.91 ? 19 ASP B CG 1 ATOM 2688 O OD1 . ASP B 2 19 ? 28.079 -15.765 -63.438 1.00 104.31 ? 19 ASP B OD1 1 ATOM 2689 O OD2 . ASP B 2 19 ? 26.375 -17.106 -63.743 1.00 106.82 ? 19 ASP B OD2 1 ATOM 2690 N N . GLY B 2 20 ? 29.680 -16.879 -60.148 1.00 84.15 ? 20 GLY B N 1 ATOM 2691 C CA . GLY B 2 20 ? 30.506 -18.043 -59.844 1.00 81.79 ? 20 GLY B CA 1 ATOM 2692 C C . GLY B 2 20 ? 31.953 -17.688 -59.571 1.00 78.88 ? 20 GLY B C 1 ATOM 2693 O O . GLY B 2 20 ? 32.354 -16.542 -59.744 1.00 79.83 ? 20 GLY B O 1 ATOM 2694 N N . TRP B 2 21 ? 32.738 -18.677 -59.154 1.00 76.42 ? 21 TRP B N 1 ATOM 2695 C CA . TRP B 2 21 ? 34.165 -18.465 -58.865 1.00 75.55 ? 21 TRP B CA 1 ATOM 2696 C C . TRP B 2 21 ? 35.064 -18.634 -60.092 1.00 69.38 ? 21 TRP B C 1 ATOM 2697 O O . TRP B 2 21 ? 36.082 -17.959 -60.219 1.00 63.28 ? 21 TRP B O 1 ATOM 2698 C CB . TRP B 2 21 ? 34.645 -19.405 -57.750 1.00 76.07 ? 21 TRP B CB 1 ATOM 2699 C CG . TRP B 2 21 ? 34.564 -18.828 -56.364 1.00 78.07 ? 21 TRP B CG 1 ATOM 2700 C CD1 . TRP B 2 21 ? 34.693 -17.513 -55.995 1.00 80.67 ? 21 TRP B CD1 1 ATOM 2701 C CD2 . TRP B 2 21 ? 34.389 -19.560 -55.163 1.00 79.64 ? 21 TRP B CD2 1 ATOM 2702 N NE1 . TRP B 2 21 ? 34.589 -17.384 -54.632 1.00 79.60 ? 21 TRP B NE1 1 ATOM 2703 C CE2 . TRP B 2 21 ? 34.402 -18.629 -54.096 1.00 81.09 ? 21 TRP B CE2 1 ATOM 2704 C CE3 . TRP B 2 21 ? 34.225 -20.913 -54.879 1.00 81.59 ? 21 TRP B CE3 1 ATOM 2705 C CZ2 . TRP B 2 21 ? 34.253 -19.013 -52.772 1.00 84.29 ? 21 TRP B CZ2 1 ATOM 2706 C CZ3 . TRP B 2 21 ? 34.076 -21.298 -53.563 1.00 88.42 ? 21 TRP B CZ3 1 ATOM 2707 C CH2 . TRP B 2 21 ? 34.089 -20.351 -52.520 1.00 88.65 ? 21 TRP B CH2 1 ATOM 2708 N N . TYR B 2 22 ? 34.693 -19.558 -60.973 1.00 66.98 ? 22 TYR B N 1 ATOM 2709 C CA . TYR B 2 22 ? 35.412 -19.774 -62.212 1.00 64.52 ? 22 TYR B CA 1 ATOM 2710 C C . TYR B 2 22 ? 34.419 -19.912 -63.329 1.00 63.87 ? 22 TYR B C 1 ATOM 2711 O O . TYR B 2 22 ? 33.267 -20.295 -63.107 1.00 64.07 ? 22 TYR B O 1 ATOM 2712 C CB . TYR B 2 22 ? 36.221 -21.065 -62.155 1.00 66.15 ? 22 TYR B CB 1 ATOM 2713 C CG . TYR B 2 22 ? 36.623 -21.488 -60.771 1.00 66.02 ? 22 TYR B CG 1 ATOM 2714 C CD1 . TYR B 2 22 ? 37.613 -20.797 -60.081 1.00 64.25 ? 22 TYR B CD1 1 ATOM 2715 C CD2 . TYR B 2 22 ? 36.016 -22.577 -60.151 1.00 65.07 ? 22 TYR B CD2 1 ATOM 2716 C CE1 . TYR B 2 22 ? 37.990 -21.175 -58.811 1.00 64.35 ? 22 TYR B CE1 1 ATOM 2717 C CE2 . TYR B 2 22 ? 36.394 -22.970 -58.886 1.00 65.38 ? 22 TYR B CE2 1 ATOM 2718 C CZ . TYR B 2 22 ? 37.382 -22.266 -58.223 1.00 65.47 ? 22 TYR B CZ 1 ATOM 2719 O OH . TYR B 2 22 ? 37.769 -22.635 -56.962 1.00 65.56 ? 22 TYR B OH 1 ATOM 2720 N N . GLY B 2 23 ? 34.877 -19.642 -64.541 1.00 62.22 ? 23 GLY B N 1 ATOM 2721 C CA . GLY B 2 23 ? 34.004 -19.737 -65.686 1.00 64.30 ? 23 GLY B CA 1 ATOM 2722 C C . GLY B 2 23 ? 34.637 -19.251 -66.957 1.00 64.59 ? 23 GLY B C 1 ATOM 2723 O O . GLY B 2 23 ? 35.856 -19.151 -67.060 1.00 64.36 ? 23 GLY B O 1 ATOM 2724 N N . TYR B 2 24 ? 33.783 -18.950 -67.927 1.00 68.33 ? 24 TYR B N 1 ATOM 2725 C CA . TYR B 2 24 ? 34.206 -18.652 -69.280 1.00 68.89 ? 24 TYR B CA 1 ATOM 2726 C C . TYR B 2 24 ? 33.785 -17.253 -69.673 1.00 69.16 ? 24 TYR B C 1 ATOM 2727 O O . TYR B 2 24 ? 32.783 -16.735 -69.192 1.00 69.60 ? 24 TYR B O 1 ATOM 2728 C CB . TYR B 2 24 ? 33.571 -19.637 -70.258 1.00 71.52 ? 24 TYR B CB 1 ATOM 2729 C CG . TYR B 2 24 ? 33.604 -21.068 -69.797 1.00 74.85 ? 24 TYR B CG 1 ATOM 2730 C CD1 . TYR B 2 24 ? 32.624 -21.560 -68.944 1.00 76.70 ? 24 TYR B CD1 1 ATOM 2731 C CD2 . TYR B 2 24 ? 34.606 -21.935 -70.217 1.00 76.99 ? 24 TYR B CD2 1 ATOM 2732 C CE1 . TYR B 2 24 ? 32.640 -22.874 -68.516 1.00 78.97 ? 24 TYR B CE1 1 ATOM 2733 C CE2 . TYR B 2 24 ? 34.632 -23.255 -69.792 1.00 78.46 ? 24 TYR B CE2 1 ATOM 2734 C CZ . TYR B 2 24 ? 33.648 -23.717 -68.939 1.00 79.46 ? 24 TYR B CZ 1 ATOM 2735 O OH . TYR B 2 24 ? 33.661 -25.019 -68.505 1.00 82.55 ? 24 TYR B OH 1 ATOM 2736 N N . HIS B 2 25 ? 34.572 -16.650 -70.552 1.00 70.73 ? 25 HIS B N 1 ATOM 2737 C CA . HIS B 2 25 ? 34.163 -15.468 -71.286 1.00 72.11 ? 25 HIS B CA 1 ATOM 2738 C C . HIS B 2 25 ? 34.267 -15.787 -72.767 1.00 72.20 ? 25 HIS B C 1 ATOM 2739 O O . HIS B 2 25 ? 35.249 -16.361 -73.195 1.00 69.51 ? 25 HIS B O 1 ATOM 2740 C CB . HIS B 2 25 ? 35.064 -14.290 -70.951 1.00 71.15 ? 25 HIS B CB 1 ATOM 2741 C CG . HIS B 2 25 ? 34.684 -13.035 -71.661 1.00 73.68 ? 25 HIS B CG 1 ATOM 2742 N ND1 . HIS B 2 25 ? 35.328 -12.602 -72.798 1.00 74.82 ? 25 HIS B ND1 1 ATOM 2743 C CD2 . HIS B 2 25 ? 33.706 -12.131 -71.411 1.00 75.97 ? 25 HIS B CD2 1 ATOM 2744 C CE1 . HIS B 2 25 ? 34.775 -11.474 -73.210 1.00 76.96 ? 25 HIS B CE1 1 ATOM 2745 N NE2 . HIS B 2 25 ? 33.789 -11.167 -72.385 1.00 77.33 ? 25 HIS B NE2 1 ATOM 2746 N N . HIS B 2 26 ? 33.257 -15.429 -73.552 1.00 76.99 ? 26 HIS B N 1 ATOM 2747 C CA . HIS B 2 26 ? 33.306 -15.669 -74.994 1.00 78.50 ? 26 HIS B CA 1 ATOM 2748 C C . HIS B 2 26 ? 33.176 -14.362 -75.752 1.00 79.38 ? 26 HIS B C 1 ATOM 2749 O O . HIS B 2 26 ? 32.624 -13.397 -75.241 1.00 78.77 ? 26 HIS B O 1 ATOM 2750 C CB . HIS B 2 26 ? 32.214 -16.644 -75.426 1.00 80.06 ? 26 HIS B CB 1 ATOM 2751 C CG . HIS B 2 26 ? 30.842 -16.061 -75.395 1.00 84.18 ? 26 HIS B CG 1 ATOM 2752 N ND1 . HIS B 2 26 ? 30.153 -15.845 -74.222 1.00 89.67 ? 26 HIS B ND1 1 ATOM 2753 C CD2 . HIS B 2 26 ? 30.035 -15.632 -76.390 1.00 88.73 ? 26 HIS B CD2 1 ATOM 2754 C CE1 . HIS B 2 26 ? 28.976 -15.312 -74.496 1.00 90.33 ? 26 HIS B CE1 1 ATOM 2755 N NE2 . HIS B 2 26 ? 28.878 -15.176 -75.805 1.00 92.40 ? 26 HIS B NE2 1 ATOM 2756 N N . SER B 2 27 ? 33.711 -14.346 -76.966 1.00 80.65 ? 27 SER B N 1 ATOM 2757 C CA . SER B 2 27 ? 33.613 -13.206 -77.870 1.00 82.62 ? 27 SER B CA 1 ATOM 2758 C C . SER B 2 27 ? 33.429 -13.711 -79.286 1.00 82.48 ? 27 SER B C 1 ATOM 2759 O O . SER B 2 27 ? 34.262 -14.475 -79.785 1.00 79.69 ? 27 SER B O 1 ATOM 2760 C CB . SER B 2 27 ? 34.891 -12.377 -77.819 1.00 84.93 ? 27 SER B CB 1 ATOM 2761 O OG . SER B 2 27 ? 34.689 -11.208 -77.062 1.00 91.61 ? 27 SER B OG 1 ATOM 2762 N N . ASN B 2 28 ? 32.350 -13.286 -79.933 1.00 81.28 ? 28 ASN B N 1 ATOM 2763 C CA . ASN B 2 28 ? 32.098 -13.654 -81.318 1.00 80.23 ? 28 ASN B CA 1 ATOM 2764 C C . ASN B 2 28 ? 31.236 -12.597 -82.005 1.00 83.88 ? 28 ASN B C 1 ATOM 2765 O O . ASN B 2 28 ? 30.989 -11.538 -81.433 1.00 84.18 ? 28 ASN B O 1 ATOM 2766 C CB . ASN B 2 28 ? 31.473 -15.051 -81.383 1.00 77.87 ? 28 ASN B CB 1 ATOM 2767 C CG . ASN B 2 28 ? 30.099 -15.111 -80.759 1.00 78.05 ? 28 ASN B CG 1 ATOM 2768 O OD1 . ASN B 2 28 ? 29.414 -14.101 -80.637 1.00 81.17 ? 28 ASN B OD1 1 ATOM 2769 N ND2 . ASN B 2 28 ? 29.683 -16.306 -80.370 1.00 76.95 ? 28 ASN B ND2 1 ATOM 2770 N N . GLU B 2 29 ? 30.781 -12.873 -83.222 1.00 89.12 ? 29 GLU B N 1 ATOM 2771 C CA . GLU B 2 29 ? 30.061 -11.871 -83.998 1.00 93.99 ? 29 GLU B CA 1 ATOM 2772 C C . GLU B 2 29 ? 28.752 -11.459 -83.332 1.00 96.05 ? 29 GLU B C 1 ATOM 2773 O O . GLU B 2 29 ? 28.343 -10.301 -83.428 1.00 97.68 ? 29 GLU B O 1 ATOM 2774 C CB . GLU B 2 29 ? 29.791 -12.378 -85.411 1.00 102.07 ? 29 GLU B CB 1 ATOM 2775 C CG . GLU B 2 29 ? 31.051 -12.593 -86.243 1.00 107.10 ? 29 GLU B CG 1 ATOM 2776 C CD . GLU B 2 29 ? 30.767 -12.751 -87.736 1.00 113.78 ? 29 GLU B CD 1 ATOM 2777 O OE1 . GLU B 2 29 ? 29.884 -12.043 -88.283 1.00 111.15 ? 29 GLU B OE1 1 ATOM 2778 O OE2 . GLU B 2 29 ? 31.443 -13.592 -88.369 1.00 120.67 ? 29 GLU B OE2 1 ATOM 2779 N N . GLN B 2 30 ? 28.106 -12.404 -82.653 1.00 95.00 ? 30 GLN B N 1 ATOM 2780 C CA . GLN B 2 30 ? 26.847 -12.134 -81.954 1.00 95.31 ? 30 GLN B CA 1 ATOM 2781 C C . GLN B 2 30 ? 27.031 -11.319 -80.672 1.00 93.48 ? 30 GLN B C 1 ATOM 2782 O O . GLN B 2 30 ? 26.087 -10.685 -80.203 1.00 95.74 ? 30 GLN B O 1 ATOM 2783 C CB . GLN B 2 30 ? 26.128 -13.437 -81.615 1.00 97.06 ? 30 GLN B CB 1 ATOM 2784 C CG . GLN B 2 30 ? 25.665 -14.238 -82.817 1.00 100.84 ? 30 GLN B CG 1 ATOM 2785 C CD . GLN B 2 30 ? 25.781 -15.730 -82.573 1.00 105.00 ? 30 GLN B CD 1 ATOM 2786 O OE1 . GLN B 2 30 ? 26.881 -16.287 -82.601 1.00 108.78 ? 30 GLN B OE1 1 ATOM 2787 N NE2 . GLN B 2 30 ? 24.652 -16.383 -82.318 1.00 107.76 ? 30 GLN B NE2 1 ATOM 2788 N N . GLY B 2 31 ? 28.226 -11.342 -80.094 1.00 90.75 ? 31 GLY B N 1 ATOM 2789 C CA . GLY B 2 31 ? 28.500 -10.544 -78.896 1.00 90.14 ? 31 GLY B CA 1 ATOM 2790 C C . GLY B 2 31 ? 29.409 -11.237 -77.915 1.00 84.12 ? 31 GLY B C 1 ATOM 2791 O O . GLY B 2 31 ? 30.102 -12.173 -78.272 1.00 83.16 ? 31 GLY B O 1 ATOM 2792 N N . SER B 2 32 ? 29.395 -10.783 -76.669 1.00 82.95 ? 32 SER B N 1 ATOM 2793 C CA . SER B 2 32 ? 30.289 -11.338 -75.669 1.00 81.97 ? 32 SER B CA 1 ATOM 2794 C C . SER B 2 32 ? 29.678 -11.350 -74.288 1.00 82.64 ? 32 SER B C 1 ATOM 2795 O O . SER B 2 32 ? 28.688 -10.668 -74.039 1.00 88.27 ? 32 SER B O 1 ATOM 2796 C CB . SER B 2 32 ? 31.587 -10.536 -75.633 1.00 81.77 ? 32 SER B CB 1 ATOM 2797 O OG . SER B 2 32 ? 31.364 -9.257 -75.098 1.00 83.30 ? 32 SER B OG 1 ATOM 2798 N N . GLY B 2 33 ? 30.282 -12.131 -73.396 1.00 80.88 ? 33 GLY B N 1 ATOM 2799 C CA . GLY B 2 33 ? 29.853 -12.189 -72.006 1.00 80.16 ? 33 GLY B CA 1 ATOM 2800 C C . GLY B 2 33 ? 30.492 -13.297 -71.192 1.00 78.51 ? 33 GLY B C 1 ATOM 2801 O O . GLY B 2 33 ? 31.373 -14.011 -71.665 1.00 77.04 ? 33 GLY B O 1 ATOM 2802 N N . TYR B 2 34 ? 30.028 -13.435 -69.952 1.00 80.81 ? 34 TYR B N 1 ATOM 2803 C CA . TYR B 2 34 ? 30.593 -14.384 -69.000 1.00 76.84 ? 34 TYR B CA 1 ATOM 2804 C C . TYR B 2 34 ? 29.611 -15.499 -68.693 1.00 76.06 ? 34 TYR B C 1 ATOM 2805 O O . TYR B 2 34 ? 28.406 -15.311 -68.766 1.00 75.58 ? 34 TYR B O 1 ATOM 2806 C CB . TYR B 2 34 ? 30.953 -13.677 -67.696 1.00 75.99 ? 34 TYR B CB 1 ATOM 2807 C CG . TYR B 2 34 ? 31.876 -12.493 -67.858 1.00 75.97 ? 34 TYR B CG 1 ATOM 2808 C CD1 . TYR B 2 34 ? 31.368 -11.218 -68.067 1.00 79.27 ? 34 TYR B CD1 1 ATOM 2809 C CD2 . TYR B 2 34 ? 33.252 -12.640 -67.785 1.00 73.06 ? 34 TYR B CD2 1 ATOM 2810 C CE1 . TYR B 2 34 ? 32.203 -10.126 -68.206 1.00 78.42 ? 34 TYR B CE1 1 ATOM 2811 C CE2 . TYR B 2 34 ? 34.093 -11.549 -67.929 1.00 74.11 ? 34 TYR B CE2 1 ATOM 2812 C CZ . TYR B 2 34 ? 33.558 -10.295 -68.136 1.00 75.55 ? 34 TYR B CZ 1 ATOM 2813 O OH . TYR B 2 34 ? 34.376 -9.205 -68.276 1.00 78.36 ? 34 TYR B OH 1 ATOM 2814 N N . ALA B 2 35 ? 30.146 -16.658 -68.337 1.00 75.55 ? 35 ALA B N 1 ATOM 2815 C CA . ALA B 2 35 ? 29.338 -17.779 -67.888 1.00 77.31 ? 35 ALA B CA 1 ATOM 2816 C C . ALA B 2 35 ? 30.120 -18.552 -66.833 1.00 78.70 ? 35 ALA B C 1 ATOM 2817 O O . ALA B 2 35 ? 31.214 -19.043 -67.097 1.00 77.25 ? 35 ALA B O 1 ATOM 2818 C CB . ALA B 2 35 ? 28.997 -18.679 -69.051 1.00 76.63 ? 35 ALA B CB 1 ATOM 2819 N N . ALA B 2 36 ? 29.562 -18.642 -65.633 1.00 82.26 ? 36 ALA B N 1 ATOM 2820 C CA . ALA B 2 36 ? 30.177 -19.401 -64.555 1.00 80.37 ? 36 ALA B CA 1 ATOM 2821 C C . ALA B 2 36 ? 30.124 -20.884 -64.885 1.00 82.19 ? 36 ALA B C 1 ATOM 2822 O O . ALA B 2 36 ? 29.149 -21.351 -65.460 1.00 86.76 ? 36 ALA B O 1 ATOM 2823 C CB . ALA B 2 36 ? 29.450 -19.135 -63.251 1.00 81.03 ? 36 ALA B CB 1 ATOM 2824 N N . ASP B 2 37 ? 31.182 -21.613 -64.543 1.00 83.68 ? 37 ASP B N 1 ATOM 2825 C CA . ASP B 2 37 ? 31.169 -23.070 -64.615 1.00 85.29 ? 37 ASP B CA 1 ATOM 2826 C C . ASP B 2 37 ? 30.621 -23.584 -63.290 1.00 89.61 ? 37 ASP B C 1 ATOM 2827 O O . ASP B 2 37 ? 31.300 -23.512 -62.261 1.00 90.51 ? 37 ASP B O 1 ATOM 2828 C CB . ASP B 2 37 ? 32.576 -23.614 -64.855 1.00 82.86 ? 37 ASP B CB 1 ATOM 2829 C CG . ASP B 2 37 ? 32.590 -25.114 -65.072 1.00 83.05 ? 37 ASP B CG 1 ATOM 2830 O OD1 . ASP B 2 37 ? 32.375 -25.564 -66.214 1.00 84.70 ? 37 ASP B OD1 1 ATOM 2831 O OD2 . ASP B 2 37 ? 32.829 -25.846 -64.098 1.00 84.94 ? 37 ASP B OD2 1 ATOM 2832 N N . LYS B 2 38 ? 29.392 -24.091 -63.314 1.00 95.27 ? 38 LYS B N 1 ATOM 2833 C CA . LYS B 2 38 ? 28.695 -24.473 -62.089 1.00 100.62 ? 38 LYS B CA 1 ATOM 2834 C C . LYS B 2 38 ? 29.322 -25.679 -61.392 1.00 99.06 ? 38 LYS B C 1 ATOM 2835 O O . LYS B 2 38 ? 29.373 -25.716 -60.165 1.00 96.12 ? 38 LYS B O 1 ATOM 2836 C CB . LYS B 2 38 ? 27.219 -24.752 -62.370 1.00 111.27 ? 38 LYS B CB 1 ATOM 2837 C CG . LYS B 2 38 ? 26.432 -23.537 -62.847 1.00 118.50 ? 38 LYS B CG 1 ATOM 2838 C CD . LYS B 2 38 ? 24.928 -23.798 -62.839 1.00 125.98 ? 38 LYS B CD 1 ATOM 2839 C CE . LYS B 2 38 ? 24.496 -24.734 -63.963 1.00 129.55 ? 38 LYS B CE 1 ATOM 2840 N NZ . LYS B 2 38 ? 23.083 -25.184 -63.807 1.00 135.29 ? 38 LYS B NZ 1 ATOM 2841 N N . GLU B 2 39 ? 29.798 -26.657 -62.161 1.00 99.77 ? 39 GLU B N 1 ATOM 2842 C CA . GLU B 2 39 ? 30.377 -27.862 -61.567 1.00 103.43 ? 39 GLU B CA 1 ATOM 2843 C C . GLU B 2 39 ? 31.581 -27.540 -60.686 1.00 97.92 ? 39 GLU B C 1 ATOM 2844 O O . GLU B 2 39 ? 31.572 -27.833 -59.486 1.00 98.68 ? 39 GLU B O 1 ATOM 2845 C CB . GLU B 2 39 ? 30.787 -28.892 -62.632 1.00 111.52 ? 39 GLU B CB 1 ATOM 2846 C CG . GLU B 2 39 ? 31.668 -30.013 -62.070 1.00 118.68 ? 39 GLU B CG 1 ATOM 2847 C CD . GLU B 2 39 ? 31.770 -31.240 -62.965 1.00 126.15 ? 39 GLU B CD 1 ATOM 2848 O OE1 . GLU B 2 39 ? 31.884 -31.088 -64.203 1.00 127.06 ? 39 GLU B OE1 1 ATOM 2849 O OE2 . GLU B 2 39 ? 31.750 -32.365 -62.418 1.00 132.84 ? 39 GLU B OE2 1 ATOM 2850 N N . SER B 2 40 ? 32.617 -26.957 -61.284 1.00 90.11 ? 40 SER B N 1 ATOM 2851 C CA . SER B 2 40 ? 33.856 -26.695 -60.557 1.00 84.36 ? 40 SER B CA 1 ATOM 2852 C C . SER B 2 40 ? 33.642 -25.678 -59.448 1.00 79.17 ? 40 SER B C 1 ATOM 2853 O O . SER B 2 40 ? 34.274 -25.773 -58.404 1.00 78.37 ? 40 SER B O 1 ATOM 2854 C CB . SER B 2 40 ? 34.970 -26.241 -61.497 1.00 81.38 ? 40 SER B CB 1 ATOM 2855 O OG . SER B 2 40 ? 34.527 -25.204 -62.339 1.00 83.27 ? 40 SER B OG 1 ATOM 2856 N N . THR B 2 41 ? 32.742 -24.722 -59.666 1.00 77.32 ? 41 THR B N 1 ATOM 2857 C CA . THR B 2 41 ? 32.389 -23.754 -58.625 1.00 74.86 ? 41 THR B CA 1 ATOM 2858 C C . THR B 2 41 ? 31.760 -24.439 -57.422 1.00 73.82 ? 41 THR B C 1 ATOM 2859 O O . THR B 2 41 ? 32.156 -24.183 -56.299 1.00 72.29 ? 41 THR B O 1 ATOM 2860 C CB . THR B 2 41 ? 31.418 -22.677 -59.146 1.00 74.15 ? 41 THR B CB 1 ATOM 2861 O OG1 . THR B 2 41 ? 32.081 -21.872 -60.121 1.00 73.84 ? 41 THR B OG1 1 ATOM 2862 C CG2 . THR B 2 41 ? 30.954 -21.778 -58.025 1.00 74.40 ? 41 THR B CG2 1 ATOM 2863 N N . GLN B 2 42 ? 30.778 -25.301 -57.659 1.00 76.75 ? 42 GLN B N 1 ATOM 2864 C CA . GLN B 2 42 ? 30.124 -26.032 -56.572 1.00 80.91 ? 42 GLN B CA 1 ATOM 2865 C C . GLN B 2 42 ? 31.093 -26.947 -55.812 1.00 79.51 ? 42 GLN B C 1 ATOM 2866 O O . GLN B 2 42 ? 31.019 -27.043 -54.590 1.00 77.00 ? 42 GLN B O 1 ATOM 2867 C CB . GLN B 2 42 ? 28.939 -26.850 -57.102 1.00 86.54 ? 42 GLN B CB 1 ATOM 2868 C CG . GLN B 2 42 ? 28.059 -27.460 -56.019 1.00 91.52 ? 42 GLN B CG 1 ATOM 2869 C CD . GLN B 2 42 ? 27.563 -26.431 -55.016 1.00 93.41 ? 42 GLN B CD 1 ATOM 2870 O OE1 . GLN B 2 42 ? 27.782 -26.562 -53.813 1.00 91.52 ? 42 GLN B OE1 1 ATOM 2871 N NE2 . GLN B 2 42 ? 26.909 -25.390 -55.513 1.00 96.07 ? 42 GLN B NE2 1 ATOM 2872 N N . LYS B 2 43 ? 31.986 -27.617 -56.538 1.00 80.90 ? 43 LYS B N 1 ATOM 2873 C CA . LYS B 2 43 ? 33.065 -28.394 -55.916 1.00 82.27 ? 43 LYS B CA 1 ATOM 2874 C C . LYS B 2 43 ? 33.901 -27.526 -54.995 1.00 77.11 ? 43 LYS B C 1 ATOM 2875 O O . LYS B 2 43 ? 34.245 -27.937 -53.890 1.00 79.78 ? 43 LYS B O 1 ATOM 2876 C CB . LYS B 2 43 ? 33.976 -29.030 -56.970 1.00 87.95 ? 43 LYS B CB 1 ATOM 2877 C CG . LYS B 2 43 ? 33.447 -30.342 -57.524 1.00 98.38 ? 43 LYS B CG 1 ATOM 2878 C CD . LYS B 2 43 ? 34.140 -30.730 -58.825 1.00 106.16 ? 43 LYS B CD 1 ATOM 2879 C CE . LYS B 2 43 ? 33.775 -32.142 -59.263 1.00 111.25 ? 43 LYS B CE 1 ATOM 2880 N NZ . LYS B 2 43 ? 34.246 -33.162 -58.281 1.00 113.63 ? 43 LYS B NZ 1 ATOM 2881 N N . ALA B 2 44 ? 34.231 -26.327 -55.451 1.00 71.18 ? 44 ALA B N 1 ATOM 2882 C CA . ALA B 2 44 ? 34.994 -25.403 -54.631 1.00 70.26 ? 44 ALA B CA 1 ATOM 2883 C C . ALA B 2 44 ? 34.225 -25.034 -53.369 1.00 69.16 ? 44 ALA B C 1 ATOM 2884 O O . ALA B 2 44 ? 34.771 -25.061 -52.267 1.00 72.18 ? 44 ALA B O 1 ATOM 2885 C CB . ALA B 2 44 ? 35.359 -24.153 -55.421 1.00 69.01 ? 44 ALA B CB 1 ATOM 2886 N N . ILE B 2 45 ? 32.955 -24.693 -53.533 1.00 68.49 ? 45 ILE B N 1 ATOM 2887 C CA . ILE B 2 45 ? 32.125 -24.314 -52.403 1.00 71.56 ? 45 ILE B CA 1 ATOM 2888 C C . ILE B 2 45 ? 32.084 -25.419 -51.345 1.00 73.63 ? 45 ILE B C 1 ATOM 2889 O O . ILE B 2 45 ? 32.248 -25.146 -50.157 1.00 73.01 ? 45 ILE B O 1 ATOM 2890 C CB . ILE B 2 45 ? 30.698 -23.956 -52.861 1.00 75.83 ? 45 ILE B CB 1 ATOM 2891 C CG1 . ILE B 2 45 ? 30.690 -22.563 -53.498 1.00 77.10 ? 45 ILE B CG1 1 ATOM 2892 C CG2 . ILE B 2 45 ? 29.721 -23.999 -51.697 1.00 76.09 ? 45 ILE B CG2 1 ATOM 2893 C CD1 . ILE B 2 45 ? 29.437 -22.271 -54.303 1.00 80.80 ? 45 ILE B CD1 1 ATOM 2894 N N . ASP B 2 46 ? 31.870 -26.661 -51.775 1.00 74.99 ? 46 ASP B N 1 ATOM 2895 C CA . ASP B 2 46 ? 31.775 -27.782 -50.842 1.00 76.59 ? 46 ASP B CA 1 ATOM 2896 C C . ASP B 2 46 ? 33.094 -28.002 -50.125 1.00 71.73 ? 46 ASP B C 1 ATOM 2897 O O . ASP B 2 46 ? 33.129 -28.184 -48.914 1.00 70.65 ? 46 ASP B O 1 ATOM 2898 C CB . ASP B 2 46 ? 31.346 -29.054 -51.570 1.00 84.08 ? 46 ASP B CB 1 ATOM 2899 C CG . ASP B 2 46 ? 29.960 -28.929 -52.189 1.00 93.58 ? 46 ASP B CG 1 ATOM 2900 O OD1 . ASP B 2 46 ? 29.168 -28.108 -51.672 1.00 100.13 ? 46 ASP B OD1 1 ATOM 2901 O OD2 . ASP B 2 46 ? 29.663 -29.637 -53.188 1.00 98.06 ? 46 ASP B OD2 1 ATOM 2902 N N . GLY B 2 47 ? 34.184 -27.956 -50.875 1.00 69.37 ? 47 GLY B N 1 ATOM 2903 C CA . GLY B 2 47 ? 35.502 -28.124 -50.299 1.00 69.23 ? 47 GLY B CA 1 ATOM 2904 C C . GLY B 2 47 ? 35.763 -27.126 -49.196 1.00 70.74 ? 47 GLY B C 1 ATOM 2905 O O . GLY B 2 47 ? 36.103 -27.502 -48.069 1.00 73.18 ? 47 GLY B O 1 ATOM 2906 N N . VAL B 2 48 ? 35.578 -25.850 -49.511 1.00 70.70 ? 48 VAL B N 1 ATOM 2907 C CA . VAL B 2 48 ? 35.874 -24.791 -48.555 1.00 70.34 ? 48 VAL B CA 1 ATOM 2908 C C . VAL B 2 48 ? 34.941 -24.844 -47.342 1.00 68.93 ? 48 VAL B C 1 ATOM 2909 O O . VAL B 2 48 ? 35.369 -24.590 -46.222 1.00 68.98 ? 48 VAL B O 1 ATOM 2910 C CB . VAL B 2 48 ? 35.823 -23.410 -49.231 1.00 72.33 ? 48 VAL B CB 1 ATOM 2911 C CG1 . VAL B 2 48 ? 35.937 -22.296 -48.206 1.00 74.01 ? 48 VAL B CG1 1 ATOM 2912 C CG2 . VAL B 2 48 ? 36.951 -23.291 -50.240 1.00 73.93 ? 48 VAL B CG2 1 ATOM 2913 N N . THR B 2 49 ? 33.679 -25.185 -47.561 1.00 68.73 ? 49 THR B N 1 ATOM 2914 C CA . THR B 2 49 ? 32.729 -25.322 -46.464 1.00 73.02 ? 49 THR B CA 1 ATOM 2915 C C . THR B 2 49 ? 33.156 -26.450 -45.527 1.00 73.44 ? 49 THR B C 1 ATOM 2916 O O . THR B 2 49 ? 33.292 -26.254 -44.320 1.00 75.49 ? 49 THR B O 1 ATOM 2917 C CB . THR B 2 49 ? 31.317 -25.622 -46.996 1.00 77.40 ? 49 THR B CB 1 ATOM 2918 O OG1 . THR B 2 49 ? 30.945 -24.611 -47.936 1.00 76.22 ? 49 THR B OG1 1 ATOM 2919 C CG2 . THR B 2 49 ? 30.298 -25.672 -45.874 1.00 78.34 ? 49 THR B CG2 1 ATOM 2920 N N . ASN B 2 50 ? 33.378 -27.630 -46.086 1.00 75.15 ? 50 ASN B N 1 ATOM 2921 C CA . ASN B 2 50 ? 33.856 -28.757 -45.291 1.00 79.90 ? 50 ASN B CA 1 ATOM 2922 C C . ASN B 2 50 ? 35.118 -28.396 -44.517 1.00 76.21 ? 50 ASN B C 1 ATOM 2923 O O . ASN B 2 50 ? 35.257 -28.741 -43.354 1.00 74.47 ? 50 ASN B O 1 ATOM 2924 C CB . ASN B 2 50 ? 34.126 -29.974 -46.174 1.00 82.64 ? 50 ASN B CB 1 ATOM 2925 C CG . ASN B 2 50 ? 32.862 -30.546 -46.786 1.00 88.74 ? 50 ASN B CG 1 ATOM 2926 O OD1 . ASN B 2 50 ? 31.754 -30.082 -46.510 1.00 94.50 ? 50 ASN B OD1 1 ATOM 2927 N ND2 . ASN B 2 50 ? 33.022 -31.558 -47.629 1.00 92.24 ? 50 ASN B ND2 1 ATOM 2928 N N . LYS B 2 51 ? 36.034 -27.690 -45.164 1.00 76.48 ? 51 LYS B N 1 ATOM 2929 C CA . LYS B 2 51 ? 37.270 -27.301 -44.508 1.00 76.55 ? 51 LYS B CA 1 ATOM 2930 C C . LYS B 2 51 ? 36.971 -26.476 -43.269 1.00 75.57 ? 51 LYS B C 1 ATOM 2931 O O . LYS B 2 51 ? 37.490 -26.751 -42.196 1.00 77.42 ? 51 LYS B O 1 ATOM 2932 C CB . LYS B 2 51 ? 38.170 -26.505 -45.455 1.00 76.41 ? 51 LYS B CB 1 ATOM 2933 C CG . LYS B 2 51 ? 39.352 -25.855 -44.754 1.00 76.30 ? 51 LYS B CG 1 ATOM 2934 C CD . LYS B 2 51 ? 40.231 -25.092 -45.723 1.00 80.31 ? 51 LYS B CD 1 ATOM 2935 C CE . LYS B 2 51 ? 40.982 -26.019 -46.656 1.00 79.49 ? 51 LYS B CE 1 ATOM 2936 N NZ . LYS B 2 51 ? 42.141 -25.307 -47.249 1.00 81.37 ? 51 LYS B NZ 1 ATOM 2937 N N . VAL B 2 52 ? 36.141 -25.458 -43.424 1.00 76.17 ? 52 VAL B N 1 ATOM 2938 C CA . VAL B 2 52 ? 35.837 -24.565 -42.319 1.00 78.50 ? 52 VAL B CA 1 ATOM 2939 C C . VAL B 2 52 ? 35.248 -25.362 -41.151 1.00 79.35 ? 52 VAL B C 1 ATOM 2940 O O . VAL B 2 52 ? 35.753 -25.311 -40.022 1.00 76.88 ? 52 VAL B O 1 ATOM 2941 C CB . VAL B 2 52 ? 34.868 -23.452 -42.768 1.00 81.16 ? 52 VAL B CB 1 ATOM 2942 C CG1 . VAL B 2 52 ? 34.265 -22.725 -41.571 1.00 83.44 ? 52 VAL B CG1 1 ATOM 2943 C CG2 . VAL B 2 52 ? 35.597 -22.474 -43.672 1.00 81.01 ? 52 VAL B CG2 1 ATOM 2944 N N . ASN B 2 53 ? 34.198 -26.119 -41.435 1.00 77.12 ? 53 ASN B N 1 ATOM 2945 C CA . ASN B 2 53 ? 33.561 -26.915 -40.405 1.00 78.86 ? 53 ASN B CA 1 ATOM 2946 C C . ASN B 2 53 ? 34.548 -27.908 -39.783 1.00 77.52 ? 53 ASN B C 1 ATOM 2947 O O . ASN B 2 53 ? 34.466 -28.201 -38.597 1.00 81.51 ? 53 ASN B O 1 ATOM 2948 C CB . ASN B 2 53 ? 32.333 -27.626 -40.969 1.00 80.17 ? 53 ASN B CB 1 ATOM 2949 C CG . ASN B 2 53 ? 31.346 -26.665 -41.608 1.00 82.85 ? 53 ASN B CG 1 ATOM 2950 O OD1 . ASN B 2 53 ? 31.384 -25.465 -41.359 1.00 85.43 ? 53 ASN B OD1 1 ATOM 2951 N ND2 . ASN B 2 53 ? 30.468 -27.188 -42.449 1.00 86.89 ? 53 ASN B ND2 1 ATOM 2952 N N . SER B 2 54 ? 35.491 -28.404 -40.576 1.00 76.76 ? 54 SER B N 1 ATOM 2953 C CA . SER B 2 54 ? 36.523 -29.307 -40.065 1.00 78.17 ? 54 SER B CA 1 ATOM 2954 C C . SER B 2 54 ? 37.393 -28.593 -39.035 1.00 79.68 ? 54 SER B C 1 ATOM 2955 O O . SER B 2 54 ? 37.665 -29.132 -37.971 1.00 79.27 ? 54 SER B O 1 ATOM 2956 C CB . SER B 2 54 ? 37.392 -29.876 -41.200 1.00 76.72 ? 54 SER B CB 1 ATOM 2957 O OG . SER B 2 54 ? 36.732 -30.931 -41.883 1.00 77.42 ? 54 SER B OG 1 ATOM 2958 N N . ILE B 2 55 ? 37.807 -27.374 -39.358 1.00 83.73 ? 55 ILE B N 1 ATOM 2959 C CA . ILE B 2 55 ? 38.594 -26.545 -38.450 1.00 86.34 ? 55 ILE B CA 1 ATOM 2960 C C . ILE B 2 55 ? 37.830 -26.263 -37.162 1.00 89.15 ? 55 ILE B C 1 ATOM 2961 O O . ILE B 2 55 ? 38.328 -26.525 -36.069 1.00 91.02 ? 55 ILE B O 1 ATOM 2962 C CB . ILE B 2 55 ? 38.997 -25.216 -39.133 1.00 90.01 ? 55 ILE B CB 1 ATOM 2963 C CG1 . ILE B 2 55 ? 40.135 -25.480 -40.125 1.00 88.35 ? 55 ILE B CG1 1 ATOM 2964 C CG2 . ILE B 2 55 ? 39.400 -24.156 -38.107 1.00 90.07 ? 55 ILE B CG2 1 ATOM 2965 C CD1 . ILE B 2 55 ? 40.314 -24.397 -41.158 1.00 88.87 ? 55 ILE B CD1 1 ATOM 2966 N N . ILE B 2 56 ? 36.623 -25.727 -37.300 1.00 90.73 ? 56 ILE B N 1 ATOM 2967 C CA . ILE B 2 56 ? 35.778 -25.425 -36.147 1.00 92.75 ? 56 ILE B CA 1 ATOM 2968 C C . ILE B 2 56 ? 35.593 -26.661 -35.251 1.00 100.07 ? 56 ILE B C 1 ATOM 2969 O O . ILE B 2 56 ? 35.608 -26.550 -34.022 1.00 101.55 ? 56 ILE B O 1 ATOM 2970 C CB . ILE B 2 56 ? 34.410 -24.873 -36.609 1.00 92.53 ? 56 ILE B CB 1 ATOM 2971 C CG1 . ILE B 2 56 ? 34.593 -23.464 -37.178 1.00 89.83 ? 56 ILE B CG1 1 ATOM 2972 C CG2 . ILE B 2 56 ? 33.391 -24.870 -35.472 1.00 93.59 ? 56 ILE B CG2 1 ATOM 2973 C CD1 . ILE B 2 56 ? 33.365 -22.903 -37.861 1.00 92.39 ? 56 ILE B CD1 1 ATOM 2974 N N . ASP B 2 57 ? 35.438 -27.832 -35.873 1.00 105.98 ? 57 ASP B N 1 ATOM 2975 C CA . ASP B 2 57 ? 35.192 -29.084 -35.149 1.00 110.09 ? 57 ASP B CA 1 ATOM 2976 C C . ASP B 2 57 ? 36.414 -29.565 -34.352 1.00 105.95 ? 57 ASP B C 1 ATOM 2977 O O . ASP B 2 57 ? 36.295 -29.897 -33.176 1.00 103.80 ? 57 ASP B O 1 ATOM 2978 C CB . ASP B 2 57 ? 34.739 -30.177 -36.123 1.00 117.27 ? 57 ASP B CB 1 ATOM 2979 C CG . ASP B 2 57 ? 34.185 -31.402 -35.417 1.00 128.91 ? 57 ASP B CG 1 ATOM 2980 O OD1 . ASP B 2 57 ? 33.338 -31.237 -34.511 1.00 136.65 ? 57 ASP B OD1 1 ATOM 2981 O OD2 . ASP B 2 57 ? 34.586 -32.532 -35.777 1.00 133.17 ? 57 ASP B OD2 1 ATOM 2982 N N . LYS B 2 58 ? 37.582 -29.599 -34.992 1.00 103.76 ? 58 LYS B N 1 ATOM 2983 C CA . LYS B 2 58 ? 38.828 -30.005 -34.328 1.00 103.05 ? 58 LYS B CA 1 ATOM 2984 C C . LYS B 2 58 ? 39.106 -29.211 -33.057 1.00 107.82 ? 58 LYS B C 1 ATOM 2985 O O . LYS B 2 58 ? 39.591 -29.754 -32.067 1.00 109.61 ? 58 LYS B O 1 ATOM 2986 C CB . LYS B 2 58 ? 40.028 -29.826 -35.266 1.00 101.68 ? 58 LYS B CB 1 ATOM 2987 C CG . LYS B 2 58 ? 40.107 -30.786 -36.440 1.00 103.76 ? 58 LYS B CG 1 ATOM 2988 C CD . LYS B 2 58 ? 40.251 -32.240 -36.012 1.00 105.43 ? 58 LYS B CD 1 ATOM 2989 C CE . LYS B 2 58 ? 38.903 -32.941 -35.893 1.00 108.39 ? 58 LYS B CE 1 ATOM 2990 N NZ . LYS B 2 58 ? 39.032 -34.419 -36.001 1.00 112.07 ? 58 LYS B NZ 1 ATOM 2991 N N . MET B 2 59 ? 38.797 -27.922 -33.090 1.00 112.98 ? 59 MET B N 1 ATOM 2992 C CA . MET B 2 59 ? 39.200 -27.017 -32.028 1.00 116.61 ? 59 MET B CA 1 ATOM 2993 C C . MET B 2 59 ? 38.215 -26.961 -30.860 1.00 120.35 ? 59 MET B C 1 ATOM 2994 O O . MET B 2 59 ? 38.550 -26.404 -29.822 1.00 118.21 ? 59 MET B O 1 ATOM 2995 C CB . MET B 2 59 ? 39.385 -25.610 -32.596 1.00 117.93 ? 59 MET B CB 1 ATOM 2996 C CG . MET B 2 59 ? 40.331 -25.517 -33.788 1.00 115.82 ? 59 MET B CG 1 ATOM 2997 S SD . MET B 2 59 ? 42.081 -25.810 -33.464 1.00 115.54 ? 59 MET B SD 1 ATOM 2998 C CE . MET B 2 59 ? 42.347 -25.071 -31.857 1.00 116.37 ? 59 MET B CE 1 ATOM 2999 N N . ASN B 2 60 ? 37.016 -27.525 -31.009 1.00 127.14 ? 60 ASN B N 1 ATOM 3000 C CA . ASN B 2 60 ? 35.987 -27.371 -29.967 1.00 134.77 ? 60 ASN B CA 1 ATOM 3001 C C . ASN B 2 60 ? 36.182 -28.259 -28.726 1.00 133.91 ? 60 ASN B C 1 ATOM 3002 O O . ASN B 2 60 ? 35.594 -27.993 -27.677 1.00 133.10 ? 60 ASN B O 1 ATOM 3003 C CB . ASN B 2 60 ? 34.557 -27.476 -30.544 1.00 137.95 ? 60 ASN B CB 1 ATOM 3004 C CG . ASN B 2 60 ? 34.179 -28.883 -30.978 1.00 142.91 ? 60 ASN B CG 1 ATOM 3005 O OD1 . ASN B 2 60 ? 34.498 -29.869 -30.310 1.00 143.97 ? 60 ASN B OD1 1 ATOM 3006 N ND2 . ASN B 2 60 ? 33.464 -28.977 -32.096 1.00 144.80 ? 60 ASN B ND2 1 ATOM 3007 N N . THR B 2 61 ? 36.992 -29.310 -28.846 1.00 135.52 ? 61 THR B N 1 ATOM 3008 C CA . THR B 2 61 ? 37.465 -30.054 -27.671 1.00 139.61 ? 61 THR B CA 1 ATOM 3009 C C . THR B 2 61 ? 38.873 -29.563 -27.369 1.00 132.42 ? 61 THR B C 1 ATOM 3010 O O . THR B 2 61 ? 39.843 -29.967 -28.015 1.00 124.05 ? 61 THR B O 1 ATOM 3011 C CB . THR B 2 61 ? 37.442 -31.590 -27.860 1.00 144.95 ? 61 THR B CB 1 ATOM 3012 O OG1 . THR B 2 61 ? 37.402 -31.910 -29.257 1.00 150.93 ? 61 THR B OG1 1 ATOM 3013 C CG2 . THR B 2 61 ? 36.222 -32.204 -27.170 1.00 146.39 ? 61 THR B CG2 1 ATOM 3014 N N . GLN B 2 62 ? 38.962 -28.674 -26.386 1.00 132.67 ? 62 GLN B N 1 ATOM 3015 C CA . GLN B 2 62 ? 40.188 -27.934 -26.109 1.00 130.79 ? 62 GLN B CA 1 ATOM 3016 C C . GLN B 2 62 ? 40.189 -27.379 -24.678 1.00 130.49 ? 62 GLN B C 1 ATOM 3017 O O . GLN B 2 62 ? 39.128 -27.196 -24.066 1.00 134.98 ? 62 GLN B O 1 ATOM 3018 C CB . GLN B 2 62 ? 40.349 -26.818 -27.153 1.00 125.19 ? 62 GLN B CB 1 ATOM 3019 C CG . GLN B 2 62 ? 41.067 -25.557 -26.692 1.00 122.16 ? 62 GLN B CG 1 ATOM 3020 C CD . GLN B 2 62 ? 41.136 -24.510 -27.779 1.00 120.70 ? 62 GLN B CD 1 ATOM 3021 O OE1 . GLN B 2 62 ? 40.988 -24.824 -28.959 1.00 123.34 ? 62 GLN B OE1 1 ATOM 3022 N NE2 . GLN B 2 62 ? 41.358 -23.255 -27.389 1.00 117.86 ? 62 GLN B NE2 1 ATOM 3023 N N . PHE B 2 63 ? 41.392 -27.114 -24.167 1.00 122.11 ? 63 PHE B N 1 ATOM 3024 C CA . PHE B 2 63 ? 41.595 -26.684 -22.784 1.00 118.41 ? 63 PHE B CA 1 ATOM 3025 C C . PHE B 2 63 ? 40.757 -25.466 -22.395 1.00 116.22 ? 63 PHE B C 1 ATOM 3026 O O . PHE B 2 63 ? 40.632 -24.503 -23.152 1.00 116.16 ? 63 PHE B O 1 ATOM 3027 C CB . PHE B 2 63 ? 43.080 -26.392 -22.522 1.00 113.01 ? 63 PHE B CB 1 ATOM 3028 C CG . PHE B 2 63 ? 43.406 -26.165 -21.073 1.00 109.08 ? 63 PHE B CG 1 ATOM 3029 C CD1 . PHE B 2 63 ? 43.560 -27.244 -20.206 1.00 107.69 ? 63 PHE B CD1 1 ATOM 3030 C CD2 . PHE B 2 63 ? 43.552 -24.875 -20.569 1.00 110.34 ? 63 PHE B CD2 1 ATOM 3031 C CE1 . PHE B 2 63 ? 43.856 -27.041 -18.867 1.00 108.75 ? 63 PHE B CE1 1 ATOM 3032 C CE2 . PHE B 2 63 ? 43.850 -24.665 -19.227 1.00 108.55 ? 63 PHE B CE2 1 ATOM 3033 C CZ . PHE B 2 63 ? 44.004 -25.750 -18.377 1.00 109.25 ? 63 PHE B CZ 1 ATOM 3034 N N . GLU B 2 64 ? 40.193 -25.537 -21.195 1.00 115.19 ? 64 GLU B N 1 ATOM 3035 C CA . GLU B 2 64 ? 39.423 -24.450 -20.608 1.00 114.79 ? 64 GLU B CA 1 ATOM 3036 C C . GLU B 2 64 ? 39.837 -24.316 -19.140 1.00 111.03 ? 64 GLU B C 1 ATOM 3037 O O . GLU B 2 64 ? 39.835 -25.290 -18.386 1.00 106.82 ? 64 GLU B O 1 ATOM 3038 C CB . GLU B 2 64 ? 37.918 -24.709 -20.753 1.00 117.69 ? 64 GLU B CB 1 ATOM 3039 C CG . GLU B 2 64 ? 37.550 -26.182 -20.877 1.00 120.78 ? 64 GLU B CG 1 ATOM 3040 C CD . GLU B 2 64 ? 36.059 -26.427 -20.814 1.00 121.05 ? 64 GLU B CD 1 ATOM 3041 O OE1 . GLU B 2 64 ? 35.447 -26.076 -19.785 1.00 120.57 ? 64 GLU B OE1 1 ATOM 3042 O OE2 . GLU B 2 64 ? 35.505 -26.982 -21.786 1.00 120.19 ? 64 GLU B OE2 1 ATOM 3043 N N . ALA B 2 65 ? 40.213 -23.102 -18.754 1.00 111.22 ? 65 ALA B N 1 ATOM 3044 C CA . ALA B 2 65 ? 40.746 -22.839 -17.423 1.00 113.54 ? 65 ALA B CA 1 ATOM 3045 C C . ALA B 2 65 ? 39.648 -22.711 -16.366 1.00 117.03 ? 65 ALA B C 1 ATOM 3046 O O . ALA B 2 65 ? 38.487 -22.429 -16.682 1.00 115.75 ? 65 ALA B O 1 ATOM 3047 C CB . ALA B 2 65 ? 41.594 -21.575 -17.448 1.00 113.19 ? 65 ALA B CB 1 ATOM 3048 N N . VAL B 2 66 ? 40.033 -22.929 -15.112 1.00 116.35 ? 66 VAL B N 1 ATOM 3049 C CA . VAL B 2 66 ? 39.170 -22.629 -13.973 1.00 118.77 ? 66 VAL B CA 1 ATOM 3050 C C . VAL B 2 66 ? 39.992 -21.969 -12.876 1.00 117.68 ? 66 VAL B C 1 ATOM 3051 O O . VAL B 2 66 ? 41.203 -22.192 -12.774 1.00 117.84 ? 66 VAL B O 1 ATOM 3052 C CB . VAL B 2 66 ? 38.452 -23.883 -13.425 1.00 120.11 ? 66 VAL B CB 1 ATOM 3053 C CG1 . VAL B 2 66 ? 37.198 -24.181 -14.242 1.00 120.85 ? 66 VAL B CG1 1 ATOM 3054 C CG2 . VAL B 2 66 ? 39.391 -25.078 -13.403 1.00 118.38 ? 66 VAL B CG2 1 ATOM 3055 N N . GLY B 2 67 ? 39.327 -21.144 -12.073 1.00 114.53 ? 67 GLY B N 1 ATOM 3056 C CA . GLY B 2 67 ? 39.982 -20.424 -10.993 1.00 114.17 ? 67 GLY B CA 1 ATOM 3057 C C . GLY B 2 67 ? 40.353 -21.333 -9.836 1.00 111.09 ? 67 GLY B C 1 ATOM 3058 O O . GLY B 2 67 ? 39.574 -22.199 -9.436 1.00 114.11 ? 67 GLY B O 1 ATOM 3059 N N . ARG B 2 68 ? 41.561 -21.146 -9.316 1.00 105.18 ? 68 ARG B N 1 ATOM 3060 C CA . ARG B 2 68 ? 41.995 -21.802 -8.090 1.00 102.56 ? 68 ARG B CA 1 ATOM 3061 C C . ARG B 2 68 ? 42.747 -20.786 -7.245 1.00 101.81 ? 68 ARG B C 1 ATOM 3062 O O . ARG B 2 68 ? 43.687 -20.144 -7.722 1.00 101.14 ? 68 ARG B O 1 ATOM 3063 C CB . ARG B 2 68 ? 42.912 -22.985 -8.387 1.00 101.38 ? 68 ARG B CB 1 ATOM 3064 C CG . ARG B 2 68 ? 42.284 -24.070 -9.234 1.00 99.09 ? 68 ARG B CG 1 ATOM 3065 C CD . ARG B 2 68 ? 43.258 -25.206 -9.487 1.00 97.31 ? 68 ARG B CD 1 ATOM 3066 N NE . ARG B 2 68 ? 42.829 -26.006 -10.627 1.00 97.05 ? 68 ARG B NE 1 ATOM 3067 C CZ . ARG B 2 68 ? 42.968 -25.643 -11.900 1.00 94.92 ? 68 ARG B CZ 1 ATOM 3068 N NH1 . ARG B 2 68 ? 43.543 -24.491 -12.232 1.00 95.37 ? 68 ARG B NH1 1 ATOM 3069 N NH2 . ARG B 2 68 ? 42.520 -26.441 -12.856 1.00 98.58 ? 68 ARG B NH2 1 ATOM 3070 N N . GLU B 2 69 ? 42.326 -20.652 -5.992 1.00 100.53 ? 69 GLU B N 1 ATOM 3071 C CA . GLU B 2 69 ? 42.943 -19.734 -5.058 1.00 98.19 ? 69 GLU B CA 1 ATOM 3072 C C . GLU B 2 69 ? 44.092 -20.462 -4.382 1.00 91.08 ? 69 GLU B C 1 ATOM 3073 O O . GLU B 2 69 ? 44.049 -21.676 -4.220 1.00 88.23 ? 69 GLU B O 1 ATOM 3074 C CB . GLU B 2 69 ? 41.925 -19.311 -3.999 1.00 106.96 ? 69 GLU B CB 1 ATOM 3075 C CG . GLU B 2 69 ? 42.017 -17.855 -3.557 1.00 114.41 ? 69 GLU B CG 1 ATOM 3076 C CD . GLU B 2 69 ? 40.975 -16.970 -4.224 1.00 118.32 ? 69 GLU B CD 1 ATOM 3077 O OE1 . GLU B 2 69 ? 40.535 -17.301 -5.348 1.00 116.99 ? 69 GLU B OE1 1 ATOM 3078 O OE2 . GLU B 2 69 ? 40.586 -15.950 -3.612 1.00 121.19 ? 69 GLU B OE2 1 ATOM 3079 N N . PHE B 2 70 ? 45.119 -19.719 -3.993 1.00 88.98 ? 70 PHE B N 1 ATOM 3080 C CA . PHE B 2 70 ? 46.179 -20.251 -3.142 1.00 88.18 ? 70 PHE B CA 1 ATOM 3081 C C . PHE B 2 70 ? 46.605 -19.187 -2.139 1.00 89.93 ? 70 PHE B C 1 ATOM 3082 O O . PHE B 2 70 ? 46.473 -17.997 -2.399 1.00 89.65 ? 70 PHE B O 1 ATOM 3083 C CB . PHE B 2 70 ? 47.364 -20.691 -3.987 1.00 88.39 ? 70 PHE B CB 1 ATOM 3084 C CG . PHE B 2 70 ? 47.016 -21.721 -5.021 1.00 86.52 ? 70 PHE B CG 1 ATOM 3085 C CD1 . PHE B 2 70 ? 46.584 -21.336 -6.282 1.00 87.83 ? 70 PHE B CD1 1 ATOM 3086 C CD2 . PHE B 2 70 ? 47.110 -23.072 -4.731 1.00 85.64 ? 70 PHE B CD2 1 ATOM 3087 C CE1 . PHE B 2 70 ? 46.255 -22.281 -7.238 1.00 86.01 ? 70 PHE B CE1 1 ATOM 3088 C CE2 . PHE B 2 70 ? 46.785 -24.024 -5.680 1.00 84.58 ? 70 PHE B CE2 1 ATOM 3089 C CZ . PHE B 2 70 ? 46.357 -23.629 -6.935 1.00 85.24 ? 70 PHE B CZ 1 ATOM 3090 N N . ASN B 2 71 ? 47.097 -19.611 -0.981 1.00 92.61 ? 71 ASN B N 1 ATOM 3091 C CA . ASN B 2 71 ? 47.456 -18.655 0.074 1.00 96.56 ? 71 ASN B CA 1 ATOM 3092 C C . ASN B 2 71 ? 48.917 -18.232 -0.050 1.00 96.72 ? 71 ASN B C 1 ATOM 3093 O O . ASN B 2 71 ? 49.590 -18.604 -1.006 1.00 94.92 ? 71 ASN B O 1 ATOM 3094 C CB . ASN B 2 71 ? 47.119 -19.205 1.477 1.00 97.15 ? 71 ASN B CB 1 ATOM 3095 C CG . ASN B 2 71 ? 48.108 -20.253 1.962 1.00 96.67 ? 71 ASN B CG 1 ATOM 3096 O OD1 . ASN B 2 71 ? 49.313 -20.130 1.762 1.00 99.11 ? 71 ASN B OD1 1 ATOM 3097 N ND2 . ASN B 2 71 ? 47.599 -21.287 2.616 1.00 96.89 ? 71 ASN B ND2 1 ATOM 3098 N N . ASN B 2 72 ? 49.400 -17.471 0.927 1.00 100.20 ? 72 ASN B N 1 ATOM 3099 C CA . ASN B 2 72 ? 50.733 -16.881 0.866 1.00 100.95 ? 72 ASN B CA 1 ATOM 3100 C C . ASN B 2 72 ? 51.891 -17.887 0.935 1.00 99.32 ? 72 ASN B C 1 ATOM 3101 O O . ASN B 2 72 ? 52.995 -17.566 0.502 1.00 102.20 ? 72 ASN B O 1 ATOM 3102 C CB . ASN B 2 72 ? 50.893 -15.840 1.978 1.00 104.80 ? 72 ASN B CB 1 ATOM 3103 C CG . ASN B 2 72 ? 51.885 -14.753 1.620 1.00 108.12 ? 72 ASN B CG 1 ATOM 3104 O OD1 . ASN B 2 72 ? 51.776 -14.136 0.564 1.00 110.21 ? 72 ASN B OD1 1 ATOM 3105 N ND2 . ASN B 2 72 ? 52.852 -14.503 2.499 1.00 110.89 ? 72 ASN B ND2 1 ATOM 3106 N N . LEU B 2 73 ? 51.645 -19.080 1.482 1.00 96.58 ? 73 LEU B N 1 ATOM 3107 C CA . LEU B 2 73 ? 52.667 -20.134 1.601 1.00 95.06 ? 73 LEU B CA 1 ATOM 3108 C C . LEU B 2 73 ? 52.387 -21.339 0.686 1.00 93.11 ? 73 LEU B C 1 ATOM 3109 O O . LEU B 2 73 ? 52.842 -22.457 0.951 1.00 91.16 ? 73 LEU B O 1 ATOM 3110 C CB . LEU B 2 73 ? 52.776 -20.596 3.054 1.00 97.14 ? 73 LEU B CB 1 ATOM 3111 C CG . LEU B 2 73 ? 53.192 -19.526 4.076 1.00 100.42 ? 73 LEU B CG 1 ATOM 3112 C CD1 . LEU B 2 73 ? 52.918 -20.007 5.490 1.00 99.19 ? 73 LEU B CD1 1 ATOM 3113 C CD2 . LEU B 2 73 ? 54.658 -19.146 3.908 1.00 101.23 ? 73 LEU B CD2 1 ATOM 3114 N N . GLU B 2 74 ? 51.639 -21.097 -0.389 1.00 91.25 ? 74 GLU B N 1 ATOM 3115 C CA . GLU B 2 74 ? 51.412 -22.083 -1.438 1.00 89.09 ? 74 GLU B CA 1 ATOM 3116 C C . GLU B 2 74 ? 51.836 -21.487 -2.777 1.00 87.21 ? 74 GLU B C 1 ATOM 3117 O O . GLU B 2 74 ? 51.204 -21.725 -3.808 1.00 84.10 ? 74 GLU B O 1 ATOM 3118 C CB . GLU B 2 74 ? 49.938 -22.467 -1.474 1.00 90.08 ? 74 GLU B CB 1 ATOM 3119 C CG . GLU B 2 74 ? 49.490 -23.281 -0.276 1.00 92.32 ? 74 GLU B CG 1 ATOM 3120 C CD . GLU B 2 74 ? 47.981 -23.412 -0.184 1.00 95.62 ? 74 GLU B CD 1 ATOM 3121 O OE1 . GLU B 2 74 ? 47.265 -22.460 -0.571 1.00 98.10 ? 74 GLU B OE1 1 ATOM 3122 O OE2 . GLU B 2 74 ? 47.508 -24.467 0.286 1.00 97.23 ? 74 GLU B OE2 1 ATOM 3123 N N . ARG B 2 75 ? 52.907 -20.701 -2.753 1.00 87.15 ? 75 ARG B N 1 ATOM 3124 C CA . ARG B 2 75 ? 53.334 -19.973 -3.935 1.00 86.78 ? 75 ARG B CA 1 ATOM 3125 C C . ARG B 2 75 ? 53.819 -20.906 -5.025 1.00 83.37 ? 75 ARG B C 1 ATOM 3126 O O . ARG B 2 75 ? 53.543 -20.682 -6.197 1.00 84.27 ? 75 ARG B O 1 ATOM 3127 C CB . ARG B 2 75 ? 54.425 -18.947 -3.592 1.00 91.61 ? 75 ARG B CB 1 ATOM 3128 C CG . ARG B 2 75 ? 53.940 -17.762 -2.776 1.00 95.43 ? 75 ARG B CG 1 ATOM 3129 C CD . ARG B 2 75 ? 52.797 -17.037 -3.468 1.00 98.16 ? 75 ARG B CD 1 ATOM 3130 N NE . ARG B 2 75 ? 52.386 -15.825 -2.765 1.00 107.75 ? 75 ARG B NE 1 ATOM 3131 C CZ . ARG B 2 75 ? 51.333 -15.077 -3.101 1.00 110.48 ? 75 ARG B CZ 1 ATOM 3132 N NH1 . ARG B 2 75 ? 50.570 -15.411 -4.141 1.00 108.70 ? 75 ARG B NH1 1 ATOM 3133 N NH2 . ARG B 2 75 ? 51.041 -13.990 -2.394 1.00 111.21 ? 75 ARG B NH2 1 ATOM 3134 N N . ARG B 2 76 ? 54.541 -21.953 -4.646 1.00 82.08 ? 76 ARG B N 1 ATOM 3135 C CA . ARG B 2 76 ? 55.044 -22.902 -5.626 1.00 79.38 ? 76 ARG B CA 1 ATOM 3136 C C . ARG B 2 76 ? 53.906 -23.497 -6.443 1.00 77.08 ? 76 ARG B C 1 ATOM 3137 O O . ARG B 2 76 ? 53.938 -23.448 -7.660 1.00 76.61 ? 76 ARG B O 1 ATOM 3138 C CB . ARG B 2 76 ? 55.822 -24.022 -4.947 1.00 79.22 ? 76 ARG B CB 1 ATOM 3139 C CG . ARG B 2 76 ? 57.183 -23.621 -4.416 1.00 80.65 ? 76 ARG B CG 1 ATOM 3140 C CD . ARG B 2 76 ? 57.737 -24.724 -3.529 1.00 80.96 ? 76 ARG B CD 1 ATOM 3141 N NE . ARG B 2 76 ? 56.816 -25.015 -2.429 1.00 80.30 ? 76 ARG B NE 1 ATOM 3142 C CZ . ARG B 2 76 ? 56.813 -26.130 -1.701 1.00 78.85 ? 76 ARG B CZ 1 ATOM 3143 N NH1 . ARG B 2 76 ? 57.700 -27.094 -1.931 1.00 81.74 ? 76 ARG B NH1 1 ATOM 3144 N NH2 . ARG B 2 76 ? 55.914 -26.282 -0.737 1.00 75.57 ? 76 ARG B NH2 1 ATOM 3145 N N . ILE B 2 77 ? 52.902 -24.053 -5.773 1.00 79.60 ? 77 ILE B N 1 ATOM 3146 C CA . ILE B 2 77 ? 51.778 -24.667 -6.480 1.00 82.41 ? 77 ILE B CA 1 ATOM 3147 C C . ILE B 2 77 ? 50.895 -23.644 -7.194 1.00 83.53 ? 77 ILE B C 1 ATOM 3148 O O . ILE B 2 77 ? 50.270 -23.967 -8.196 1.00 85.95 ? 77 ILE B O 1 ATOM 3149 C CB . ILE B 2 77 ? 50.913 -25.569 -5.578 1.00 84.31 ? 77 ILE B CB 1 ATOM 3150 C CG1 . ILE B 2 77 ? 50.326 -24.785 -4.407 1.00 92.26 ? 77 ILE B CG1 1 ATOM 3151 C CG2 . ILE B 2 77 ? 51.734 -26.738 -5.062 1.00 84.98 ? 77 ILE B CG2 1 ATOM 3152 C CD1 . ILE B 2 77 ? 49.344 -25.592 -3.580 1.00 95.72 ? 77 ILE B CD1 1 ATOM 3153 N N . GLU B 2 78 ? 50.844 -22.417 -6.691 1.00 84.54 ? 78 GLU B N 1 ATOM 3154 C CA . GLU B 2 78 ? 50.167 -21.344 -7.409 1.00 85.46 ? 78 GLU B CA 1 ATOM 3155 C C . GLU B 2 78 ? 50.884 -21.079 -8.727 1.00 81.93 ? 78 GLU B C 1 ATOM 3156 O O . GLU B 2 78 ? 50.260 -20.899 -9.768 1.00 79.16 ? 78 GLU B O 1 ATOM 3157 C CB . GLU B 2 78 ? 50.154 -20.064 -6.577 1.00 92.45 ? 78 GLU B CB 1 ATOM 3158 C CG . GLU B 2 78 ? 49.536 -18.858 -7.273 1.00 99.52 ? 78 GLU B CG 1 ATOM 3159 C CD . GLU B 2 78 ? 49.697 -17.575 -6.473 1.00 114.04 ? 78 GLU B CD 1 ATOM 3160 O OE1 . GLU B 2 78 ? 50.784 -17.363 -5.882 1.00 121.51 ? 78 GLU B OE1 1 ATOM 3161 O OE2 . GLU B 2 78 ? 48.736 -16.770 -6.430 1.00 123.23 ? 78 GLU B OE2 1 ATOM 3162 N N . ASN B 2 79 ? 52.203 -21.037 -8.662 1.00 80.44 ? 79 ASN B N 1 ATOM 3163 C CA . ASN B 2 79 ? 53.010 -20.756 -9.821 1.00 82.22 ? 79 ASN B CA 1 ATOM 3164 C C . ASN B 2 79 ? 52.924 -21.911 -10.797 1.00 80.01 ? 79 ASN B C 1 ATOM 3165 O O . ASN B 2 79 ? 52.880 -21.714 -12.002 1.00 79.15 ? 79 ASN B O 1 ATOM 3166 C CB . ASN B 2 79 ? 54.453 -20.544 -9.398 1.00 87.58 ? 79 ASN B CB 1 ATOM 3167 C CG . ASN B 2 79 ? 55.324 -20.085 -10.536 1.00 89.73 ? 79 ASN B CG 1 ATOM 3168 O OD1 . ASN B 2 79 ? 55.080 -19.034 -11.122 1.00 92.44 ? 79 ASN B OD1 1 ATOM 3169 N ND2 . ASN B 2 79 ? 56.353 -20.863 -10.852 1.00 90.72 ? 79 ASN B ND2 1 ATOM 3170 N N . LEU B 2 80 ? 52.891 -23.120 -10.254 1.00 80.46 ? 80 LEU B N 1 ATOM 3171 C CA . LEU B 2 80 ? 52.703 -24.323 -11.043 1.00 78.52 ? 80 LEU B CA 1 ATOM 3172 C C . LEU B 2 80 ? 51.408 -24.184 -11.809 1.00 74.37 ? 80 LEU B C 1 ATOM 3173 O O . LEU B 2 80 ? 51.356 -24.448 -12.991 1.00 74.43 ? 80 LEU B O 1 ATOM 3174 C CB . LEU B 2 80 ? 52.644 -25.540 -10.116 1.00 83.15 ? 80 LEU B CB 1 ATOM 3175 C CG . LEU B 2 80 ? 52.942 -26.926 -10.684 1.00 85.33 ? 80 LEU B CG 1 ATOM 3176 C CD1 . LEU B 2 80 ? 53.097 -27.905 -9.535 1.00 86.69 ? 80 LEU B CD1 1 ATOM 3177 C CD2 . LEU B 2 80 ? 51.848 -27.406 -11.614 1.00 86.38 ? 80 LEU B CD2 1 ATOM 3178 N N . ASN B 2 81 ? 50.367 -23.744 -11.115 1.00 76.78 ? 81 ASN B N 1 ATOM 3179 C CA . ASN B 2 81 ? 49.036 -23.589 -11.689 1.00 74.85 ? 81 ASN B CA 1 ATOM 3180 C C . ASN B 2 81 ? 48.999 -22.525 -12.773 1.00 75.41 ? 81 ASN B C 1 ATOM 3181 O O . ASN B 2 81 ? 48.340 -22.710 -13.785 1.00 69.85 ? 81 ASN B O 1 ATOM 3182 C CB . ASN B 2 81 ? 48.038 -23.239 -10.589 1.00 76.05 ? 81 ASN B CB 1 ATOM 3183 C CG . ASN B 2 81 ? 46.613 -23.162 -11.091 1.00 76.77 ? 81 ASN B CG 1 ATOM 3184 O OD1 . ASN B 2 81 ? 46.093 -24.120 -11.654 1.00 81.41 ? 81 ASN B OD1 1 ATOM 3185 N ND2 . ASN B 2 81 ? 45.968 -22.028 -10.876 1.00 77.54 ? 81 ASN B ND2 1 ATOM 3186 N N . LYS B 2 82 ? 49.710 -21.418 -12.562 1.00 80.52 ? 82 LYS B N 1 ATOM 3187 C CA . LYS B 2 82 ? 49.745 -20.342 -13.548 1.00 84.40 ? 82 LYS B CA 1 ATOM 3188 C C . LYS B 2 82 ? 50.476 -20.811 -14.797 1.00 83.30 ? 82 LYS B C 1 ATOM 3189 O O . LYS B 2 82 ? 49.981 -20.645 -15.904 1.00 79.70 ? 82 LYS B O 1 ATOM 3190 C CB . LYS B 2 82 ? 50.395 -19.073 -12.987 1.00 90.49 ? 82 LYS B CB 1 ATOM 3191 C CG . LYS B 2 82 ? 50.138 -17.829 -13.837 1.00 97.99 ? 82 LYS B CG 1 ATOM 3192 C CD . LYS B 2 82 ? 50.851 -16.576 -13.315 1.00 107.19 ? 82 LYS B CD 1 ATOM 3193 C CE . LYS B 2 82 ? 49.929 -15.578 -12.600 1.00 112.54 ? 82 LYS B CE 1 ATOM 3194 N NZ . LYS B 2 82 ? 49.839 -15.767 -11.120 1.00 113.05 ? 82 LYS B NZ 1 ATOM 3195 N N . LYS B 2 83 ? 51.641 -21.422 -14.610 1.00 87.46 ? 83 LYS B N 1 ATOM 3196 C CA . LYS B 2 83 ? 52.447 -21.910 -15.734 1.00 88.78 ? 83 LYS B CA 1 ATOM 3197 C C . LYS B 2 83 ? 51.771 -23.033 -16.512 1.00 86.05 ? 83 LYS B C 1 ATOM 3198 O O . LYS B 2 83 ? 52.052 -23.229 -17.688 1.00 86.49 ? 83 LYS B O 1 ATOM 3199 C CB . LYS B 2 83 ? 53.846 -22.343 -15.261 1.00 92.60 ? 83 LYS B CB 1 ATOM 3200 C CG . LYS B 2 83 ? 54.985 -21.371 -15.585 1.00 100.73 ? 83 LYS B CG 1 ATOM 3201 C CD . LYS B 2 83 ? 54.552 -19.914 -15.784 1.00 106.35 ? 83 LYS B CD 1 ATOM 3202 C CE . LYS B 2 83 ? 55.727 -19.009 -16.138 1.00 111.77 ? 83 LYS B CE 1 ATOM 3203 N NZ . LYS B 2 83 ? 56.506 -18.609 -14.930 1.00 117.95 ? 83 LYS B NZ 1 ATOM 3204 N N . MET B 2 84 ? 50.875 -23.756 -15.858 1.00 86.63 ? 84 MET B N 1 ATOM 3205 C CA . MET B 2 84 ? 50.163 -24.852 -16.485 1.00 84.71 ? 84 MET B CA 1 ATOM 3206 C C . MET B 2 84 ? 49.043 -24.307 -17.368 1.00 84.17 ? 84 MET B C 1 ATOM 3207 O O . MET B 2 84 ? 48.851 -24.769 -18.490 1.00 84.22 ? 84 MET B O 1 ATOM 3208 C CB . MET B 2 84 ? 49.612 -25.768 -15.393 1.00 88.23 ? 84 MET B CB 1 ATOM 3209 C CG . MET B 2 84 ? 49.194 -27.158 -15.836 1.00 90.23 ? 84 MET B CG 1 ATOM 3210 S SD . MET B 2 84 ? 47.415 -27.300 -16.054 1.00 94.35 ? 84 MET B SD 1 ATOM 3211 C CE . MET B 2 84 ? 46.811 -27.217 -14.373 1.00 96.43 ? 84 MET B CE 1 ATOM 3212 N N . GLU B 2 85 ? 48.317 -23.309 -16.871 1.00 85.07 ? 85 GLU B N 1 ATOM 3213 C CA . GLU B 2 85 ? 47.210 -22.733 -17.627 1.00 85.11 ? 85 GLU B CA 1 ATOM 3214 C C . GLU B 2 85 ? 47.743 -21.948 -18.817 1.00 84.50 ? 85 GLU B C 1 ATOM 3215 O O . GLU B 2 85 ? 47.272 -22.122 -19.933 1.00 85.51 ? 85 GLU B O 1 ATOM 3216 C CB . GLU B 2 85 ? 46.302 -21.877 -16.734 1.00 89.03 ? 85 GLU B CB 1 ATOM 3217 C CG . GLU B 2 85 ? 45.729 -22.665 -15.552 1.00 96.79 ? 85 GLU B CG 1 ATOM 3218 C CD . GLU B 2 85 ? 44.228 -22.494 -15.330 1.00 102.42 ? 85 GLU B CD 1 ATOM 3219 O OE1 . GLU B 2 85 ? 43.813 -21.433 -14.809 1.00 109.29 ? 85 GLU B OE1 1 ATOM 3220 O OE2 . GLU B 2 85 ? 43.464 -23.442 -15.636 1.00 100.88 ? 85 GLU B OE2 1 ATOM 3221 N N . ASP B 2 86 ? 48.746 -21.112 -18.580 1.00 84.62 ? 86 ASP B N 1 ATOM 3222 C CA . ASP B 2 86 ? 49.401 -20.375 -19.653 1.00 83.80 ? 86 ASP B CA 1 ATOM 3223 C C . ASP B 2 86 ? 50.048 -21.301 -20.677 1.00 81.21 ? 86 ASP B C 1 ATOM 3224 O O . ASP B 2 86 ? 50.093 -20.986 -21.861 1.00 81.59 ? 86 ASP B O 1 ATOM 3225 C CB . ASP B 2 86 ? 50.474 -19.439 -19.091 1.00 90.38 ? 86 ASP B CB 1 ATOM 3226 C CG . ASP B 2 86 ? 49.932 -18.071 -18.745 1.00 100.53 ? 86 ASP B CG 1 ATOM 3227 O OD1 . ASP B 2 86 ? 49.282 -17.453 -19.620 1.00 107.39 ? 86 ASP B OD1 1 ATOM 3228 O OD2 . ASP B 2 86 ? 50.172 -17.599 -17.608 1.00 111.48 ? 86 ASP B OD2 1 ATOM 3229 N N . GLY B 2 87 ? 50.576 -22.425 -20.212 1.00 79.70 ? 87 GLY B N 1 ATOM 3230 C CA . GLY B 2 87 ? 51.239 -23.376 -21.079 1.00 77.28 ? 87 GLY B CA 1 ATOM 3231 C C . GLY B 2 87 ? 50.289 -23.875 -22.141 1.00 77.55 ? 87 GLY B C 1 ATOM 3232 O O . GLY B 2 87 ? 50.613 -23.867 -23.324 1.00 79.67 ? 87 GLY B O 1 ATOM 3233 N N . PHE B 2 88 ? 49.102 -24.288 -21.719 1.00 76.39 ? 88 PHE B N 1 ATOM 3234 C CA . PHE B 2 88 ? 48.115 -24.813 -22.648 1.00 74.42 ? 88 PHE B CA 1 ATOM 3235 C C . PHE B 2 88 ? 47.541 -23.743 -23.587 1.00 74.04 ? 88 PHE B C 1 ATOM 3236 O O . PHE B 2 88 ? 47.323 -24.015 -24.767 1.00 76.27 ? 88 PHE B O 1 ATOM 3237 C CB . PHE B 2 88 ? 47.000 -25.532 -21.887 1.00 73.15 ? 88 PHE B CB 1 ATOM 3238 C CG . PHE B 2 88 ? 47.397 -26.886 -21.363 1.00 71.55 ? 88 PHE B CG 1 ATOM 3239 C CD1 . PHE B 2 88 ? 47.798 -27.885 -22.230 1.00 71.30 ? 88 PHE B CD1 1 ATOM 3240 C CD2 . PHE B 2 88 ? 47.357 -27.166 -20.007 1.00 74.04 ? 88 PHE B CD2 1 ATOM 3241 C CE1 . PHE B 2 88 ? 48.162 -29.137 -21.764 1.00 72.68 ? 88 PHE B CE1 1 ATOM 3242 C CE2 . PHE B 2 88 ? 47.714 -28.418 -19.532 1.00 74.30 ? 88 PHE B CE2 1 ATOM 3243 C CZ . PHE B 2 88 ? 48.118 -29.405 -20.414 1.00 75.13 ? 88 PHE B CZ 1 ATOM 3244 N N . LEU B 2 89 ? 47.320 -22.533 -23.086 1.00 73.38 ? 89 LEU B N 1 ATOM 3245 C CA . LEU B 2 89 ? 46.806 -21.450 -23.929 1.00 76.59 ? 89 LEU B CA 1 ATOM 3246 C C . LEU B 2 89 ? 47.780 -21.105 -25.055 1.00 76.51 ? 89 LEU B C 1 ATOM 3247 O O . LEU B 2 89 ? 47.362 -20.851 -26.177 1.00 74.90 ? 89 LEU B O 1 ATOM 3248 C CB . LEU B 2 89 ? 46.503 -20.198 -23.104 1.00 84.43 ? 89 LEU B CB 1 ATOM 3249 C CG . LEU B 2 89 ? 45.440 -20.393 -22.004 1.00 95.36 ? 89 LEU B CG 1 ATOM 3250 C CD1 . LEU B 2 89 ? 45.414 -19.180 -21.082 1.00 100.32 ? 89 LEU B CD1 1 ATOM 3251 C CD2 . LEU B 2 89 ? 44.047 -20.699 -22.565 1.00 95.53 ? 89 LEU B CD2 1 ATOM 3252 N N . ASP B 2 90 ? 49.076 -21.094 -24.752 1.00 76.35 ? 90 ASP B N 1 ATOM 3253 C CA . ASP B 2 90 ? 50.095 -20.900 -25.771 1.00 76.49 ? 90 ASP B CA 1 ATOM 3254 C C . ASP B 2 90 ? 50.029 -22.014 -26.817 1.00 74.14 ? 90 ASP B C 1 ATOM 3255 O O . ASP B 2 90 ? 50.097 -21.756 -28.014 1.00 72.36 ? 90 ASP B O 1 ATOM 3256 C CB . ASP B 2 90 ? 51.495 -20.858 -25.147 1.00 80.90 ? 90 ASP B CB 1 ATOM 3257 C CG . ASP B 2 90 ? 51.749 -19.587 -24.342 1.00 88.48 ? 90 ASP B CG 1 ATOM 3258 O OD1 . ASP B 2 90 ? 50.888 -18.684 -24.346 1.00 93.53 ? 90 ASP B OD1 1 ATOM 3259 O OD2 . ASP B 2 90 ? 52.816 -19.493 -23.696 1.00 95.18 ? 90 ASP B OD2 1 ATOM 3260 N N . VAL B 2 91 ? 49.891 -23.250 -26.360 1.00 71.90 ? 91 VAL B N 1 ATOM 3261 C CA . VAL B 2 91 ? 49.826 -24.379 -27.267 1.00 70.74 ? 91 VAL B CA 1 ATOM 3262 C C . VAL B 2 91 ? 48.621 -24.262 -28.204 1.00 69.08 ? 91 VAL B C 1 ATOM 3263 O O . VAL B 2 91 ? 48.754 -24.443 -29.414 1.00 70.18 ? 91 VAL B O 1 ATOM 3264 C CB . VAL B 2 91 ? 49.767 -25.714 -26.505 1.00 70.20 ? 91 VAL B CB 1 ATOM 3265 C CG1 . VAL B 2 91 ? 49.461 -26.862 -27.458 1.00 70.21 ? 91 VAL B CG1 1 ATOM 3266 C CG2 . VAL B 2 91 ? 51.087 -25.967 -25.802 1.00 71.37 ? 91 VAL B CG2 1 ATOM 3267 N N . TRP B 2 92 ? 47.457 -23.954 -27.648 1.00 65.41 ? 92 TRP B N 1 ATOM 3268 C CA . TRP B 2 92 ? 46.256 -23.807 -28.459 1.00 65.91 ? 92 TRP B CA 1 ATOM 3269 C C . TRP B 2 92 ? 46.288 -22.567 -29.354 1.00 66.84 ? 92 TRP B C 1 ATOM 3270 O O . TRP B 2 92 ? 45.796 -22.596 -30.473 1.00 69.20 ? 92 TRP B O 1 ATOM 3271 C CB . TRP B 2 92 ? 45.013 -23.821 -27.568 1.00 65.92 ? 92 TRP B CB 1 ATOM 3272 C CG . TRP B 2 92 ? 44.777 -25.180 -27.042 1.00 68.03 ? 92 TRP B CG 1 ATOM 3273 C CD1 . TRP B 2 92 ? 44.919 -25.595 -25.762 1.00 69.31 ? 92 TRP B CD1 1 ATOM 3274 C CD2 . TRP B 2 92 ? 44.430 -26.339 -27.806 1.00 69.68 ? 92 TRP B CD2 1 ATOM 3275 N NE1 . TRP B 2 92 ? 44.654 -26.937 -25.668 1.00 72.11 ? 92 TRP B NE1 1 ATOM 3276 C CE2 . TRP B 2 92 ? 44.355 -27.419 -26.911 1.00 69.20 ? 92 TRP B CE2 1 ATOM 3277 C CE3 . TRP B 2 92 ? 44.170 -26.564 -29.162 1.00 73.63 ? 92 TRP B CE3 1 ATOM 3278 C CZ2 . TRP B 2 92 ? 44.021 -28.710 -27.319 1.00 73.60 ? 92 TRP B CZ2 1 ATOM 3279 C CZ3 . TRP B 2 92 ? 43.828 -27.854 -29.573 1.00 74.10 ? 92 TRP B CZ3 1 ATOM 3280 C CH2 . TRP B 2 92 ? 43.757 -28.908 -28.650 1.00 75.33 ? 92 TRP B CH2 1 ATOM 3281 N N . THR B 2 93 ? 46.861 -21.480 -28.859 1.00 67.34 ? 93 THR B N 1 ATOM 3282 C CA . THR B 2 93 ? 47.017 -20.284 -29.655 1.00 67.28 ? 93 THR B CA 1 ATOM 3283 C C . THR B 2 93 ? 47.884 -20.622 -30.865 1.00 68.33 ? 93 THR B C 1 ATOM 3284 O O . THR B 2 93 ? 47.512 -20.327 -31.998 1.00 69.42 ? 93 THR B O 1 ATOM 3285 C CB . THR B 2 93 ? 47.619 -19.137 -28.821 1.00 68.34 ? 93 THR B CB 1 ATOM 3286 O OG1 . THR B 2 93 ? 46.630 -18.658 -27.908 1.00 68.42 ? 93 THR B OG1 1 ATOM 3287 C CG2 . THR B 2 93 ? 48.063 -17.984 -29.684 1.00 70.12 ? 93 THR B CG2 1 ATOM 3288 N N . TYR B 2 94 ? 49.025 -21.256 -30.617 1.00 68.37 ? 94 TYR B N 1 ATOM 3289 C CA . TYR B 2 94 ? 49.915 -21.698 -31.688 1.00 66.15 ? 94 TYR B CA 1 ATOM 3290 C C . TYR B 2 94 ? 49.188 -22.598 -32.679 1.00 67.84 ? 94 TYR B C 1 ATOM 3291 O O . TYR B 2 94 ? 49.300 -22.412 -33.885 1.00 69.01 ? 94 TYR B O 1 ATOM 3292 C CB . TYR B 2 94 ? 51.111 -22.437 -31.105 1.00 64.95 ? 94 TYR B CB 1 ATOM 3293 C CG . TYR B 2 94 ? 51.954 -23.153 -32.128 1.00 65.42 ? 94 TYR B CG 1 ATOM 3294 C CD1 . TYR B 2 94 ? 51.661 -24.471 -32.505 1.00 63.35 ? 94 TYR B CD1 1 ATOM 3295 C CD2 . TYR B 2 94 ? 53.056 -22.525 -32.715 1.00 64.29 ? 94 TYR B CD2 1 ATOM 3296 C CE1 . TYR B 2 94 ? 52.436 -25.135 -33.440 1.00 63.26 ? 94 TYR B CE1 1 ATOM 3297 C CE2 . TYR B 2 94 ? 53.826 -23.178 -33.654 1.00 65.49 ? 94 TYR B CE2 1 ATOM 3298 C CZ . TYR B 2 94 ? 53.514 -24.485 -34.015 1.00 65.42 ? 94 TYR B CZ 1 ATOM 3299 O OH . TYR B 2 94 ? 54.285 -25.140 -34.948 1.00 67.78 ? 94 TYR B OH 1 ATOM 3300 N N . ASN B 2 95 ? 48.442 -23.570 -32.169 1.00 68.63 ? 95 ASN B N 1 ATOM 3301 C CA . ASN B 2 95 ? 47.685 -24.470 -33.031 1.00 68.29 ? 95 ASN B CA 1 ATOM 3302 C C . ASN B 2 95 ? 46.706 -23.740 -33.929 1.00 68.77 ? 95 ASN B C 1 ATOM 3303 O O . ASN B 2 95 ? 46.610 -24.040 -35.113 1.00 70.48 ? 95 ASN B O 1 ATOM 3304 C CB . ASN B 2 95 ? 46.912 -25.500 -32.210 1.00 68.45 ? 95 ASN B CB 1 ATOM 3305 C CG . ASN B 2 95 ? 47.800 -26.604 -31.672 1.00 73.10 ? 95 ASN B CG 1 ATOM 3306 O OD1 . ASN B 2 95 ? 48.986 -26.673 -31.982 1.00 72.63 ? 95 ASN B OD1 1 ATOM 3307 N ND2 . ASN B 2 95 ? 47.217 -27.485 -30.860 1.00 76.02 ? 95 ASN B ND2 1 ATOM 3308 N N . ALA B 2 96 ? 45.958 -22.806 -33.358 1.00 69.89 ? 96 ALA B N 1 ATOM 3309 C CA . ALA B 2 96 ? 44.953 -22.077 -34.117 1.00 69.08 ? 96 ALA B CA 1 ATOM 3310 C C . ALA B 2 96 ? 45.630 -21.236 -35.192 1.00 66.59 ? 96 ALA B C 1 ATOM 3311 O O . ALA B 2 96 ? 45.270 -21.307 -36.357 1.00 69.43 ? 96 ALA B O 1 ATOM 3312 C CB . ALA B 2 96 ? 44.121 -21.195 -33.197 1.00 70.46 ? 96 ALA B CB 1 ATOM 3313 N N . GLU B 2 97 ? 46.636 -20.470 -34.805 1.00 68.11 ? 97 GLU B N 1 ATOM 3314 C CA . GLU B 2 97 ? 47.273 -19.545 -35.734 1.00 72.40 ? 97 GLU B CA 1 ATOM 3315 C C . GLU B 2 97 ? 47.931 -20.279 -36.891 1.00 71.16 ? 97 GLU B C 1 ATOM 3316 O O . GLU B 2 97 ? 47.844 -19.850 -38.039 1.00 72.51 ? 97 GLU B O 1 ATOM 3317 C CB . GLU B 2 97 ? 48.266 -18.640 -34.999 1.00 74.76 ? 97 GLU B CB 1 ATOM 3318 C CG . GLU B 2 97 ? 47.556 -17.660 -34.073 1.00 79.44 ? 97 GLU B CG 1 ATOM 3319 C CD . GLU B 2 97 ? 48.456 -16.592 -33.488 1.00 86.99 ? 97 GLU B CD 1 ATOM 3320 O OE1 . GLU B 2 97 ? 49.681 -16.637 -33.716 1.00 96.46 ? 97 GLU B OE1 1 ATOM 3321 O OE2 . GLU B 2 97 ? 47.933 -15.695 -32.793 1.00 92.81 ? 97 GLU B OE2 1 ATOM 3322 N N . LEU B 2 98 ? 48.550 -21.409 -36.586 1.00 70.49 ? 98 LEU B N 1 ATOM 3323 C CA . LEU B 2 98 ? 49.263 -22.170 -37.585 1.00 71.09 ? 98 LEU B CA 1 ATOM 3324 C C . LEU B 2 98 ? 48.293 -22.824 -38.536 1.00 68.99 ? 98 LEU B C 1 ATOM 3325 O O . LEU B 2 98 ? 48.500 -22.812 -39.740 1.00 72.53 ? 98 LEU B O 1 ATOM 3326 C CB . LEU B 2 98 ? 50.114 -23.243 -36.929 1.00 74.51 ? 98 LEU B CB 1 ATOM 3327 C CG . LEU B 2 98 ? 51.071 -23.958 -37.877 1.00 77.25 ? 98 LEU B CG 1 ATOM 3328 C CD1 . LEU B 2 98 ? 52.203 -23.022 -38.281 1.00 78.63 ? 98 LEU B CD1 1 ATOM 3329 C CD2 . LEU B 2 98 ? 51.605 -25.225 -37.223 1.00 77.75 ? 98 LEU B CD2 1 ATOM 3330 N N . LEU B 2 99 ? 47.238 -23.404 -37.989 1.00 67.78 ? 99 LEU B N 1 ATOM 3331 C CA . LEU B 2 99 ? 46.243 -24.085 -38.800 1.00 68.59 ? 99 LEU B CA 1 ATOM 3332 C C . LEU B 2 99 ? 45.679 -23.118 -39.832 1.00 68.24 ? 99 LEU B C 1 ATOM 3333 O O . LEU B 2 99 ? 45.617 -23.425 -41.019 1.00 68.64 ? 99 LEU B O 1 ATOM 3334 C CB . LEU B 2 99 ? 45.123 -24.634 -37.916 1.00 71.23 ? 99 LEU B CB 1 ATOM 3335 C CG . LEU B 2 99 ? 44.054 -25.480 -38.611 1.00 75.56 ? 99 LEU B CG 1 ATOM 3336 C CD1 . LEU B 2 99 ? 44.677 -26.652 -39.352 1.00 77.49 ? 99 LEU B CD1 1 ATOM 3337 C CD2 . LEU B 2 99 ? 43.036 -25.974 -37.593 1.00 79.18 ? 99 LEU B CD2 1 ATOM 3338 N N . VAL B 2 100 ? 45.289 -21.937 -39.373 1.00 65.91 ? 100 VAL B N 1 ATOM 3339 C CA . VAL B 2 100 ? 44.816 -20.906 -40.272 1.00 64.02 ? 100 VAL B CA 1 ATOM 3340 C C . VAL B 2 100 ? 45.850 -20.553 -41.353 1.00 62.48 ? 100 VAL B C 1 ATOM 3341 O O . VAL B 2 100 ? 45.507 -20.543 -42.532 1.00 59.16 ? 100 VAL B O 1 ATOM 3342 C CB . VAL B 2 100 ? 44.392 -19.649 -39.489 1.00 65.05 ? 100 VAL B CB 1 ATOM 3343 C CG1 . VAL B 2 100 ? 44.237 -18.455 -40.420 1.00 64.58 ? 100 VAL B CG1 1 ATOM 3344 C CG2 . VAL B 2 100 ? 43.087 -19.933 -38.759 1.00 65.23 ? 100 VAL B CG2 1 ATOM 3345 N N . LEU B 2 101 ? 47.092 -20.257 -40.960 1.00 60.46 ? 101 LEU B N 1 ATOM 3346 C CA . LEU B 2 101 ? 48.138 -19.948 -41.935 1.00 62.17 ? 101 LEU B CA 1 ATOM 3347 C C . LEU B 2 101 ? 48.261 -21.061 -42.974 1.00 63.97 ? 101 LEU B C 1 ATOM 3348 O O . LEU B 2 101 ? 48.201 -20.815 -44.178 1.00 64.64 ? 101 LEU B O 1 ATOM 3349 C CB . LEU B 2 101 ? 49.491 -19.759 -41.256 1.00 64.27 ? 101 LEU B CB 1 ATOM 3350 C CG . LEU B 2 101 ? 49.715 -18.483 -40.449 1.00 67.29 ? 101 LEU B CG 1 ATOM 3351 C CD1 . LEU B 2 101 ? 51.166 -18.395 -40.014 1.00 67.92 ? 101 LEU B CD1 1 ATOM 3352 C CD2 . LEU B 2 101 ? 49.331 -17.240 -41.239 1.00 70.41 ? 101 LEU B CD2 1 ATOM 3353 N N . MET B 2 102 ? 48.421 -22.287 -42.500 1.00 62.80 ? 102 MET B N 1 ATOM 3354 C CA . MET B 2 102 ? 48.604 -23.417 -43.387 1.00 65.24 ? 102 MET B CA 1 ATOM 3355 C C . MET B 2 102 ? 47.403 -23.628 -44.288 1.00 66.72 ? 102 MET B C 1 ATOM 3356 O O . MET B 2 102 ? 47.561 -23.832 -45.495 1.00 69.15 ? 102 MET B O 1 ATOM 3357 C CB . MET B 2 102 ? 48.869 -24.683 -42.590 1.00 69.64 ? 102 MET B CB 1 ATOM 3358 C CG . MET B 2 102 ? 50.275 -24.762 -42.025 1.00 76.19 ? 102 MET B CG 1 ATOM 3359 S SD . MET B 2 102 ? 50.527 -26.290 -41.103 1.00 85.62 ? 102 MET B SD 1 ATOM 3360 C CE . MET B 2 102 ? 52.296 -26.496 -41.329 1.00 90.91 ? 102 MET B CE 1 ATOM 3361 N N . GLU B 2 103 ? 46.205 -23.577 -43.718 1.00 64.81 ? 103 GLU B N 1 ATOM 3362 C CA . GLU B 2 103 ? 45.020 -23.857 -44.501 1.00 66.76 ? 103 GLU B CA 1 ATOM 3363 C C . GLU B 2 103 ? 44.651 -22.727 -45.451 1.00 64.54 ? 103 GLU B C 1 ATOM 3364 O O . GLU B 2 103 ? 44.031 -22.966 -46.485 1.00 65.88 ? 103 GLU B O 1 ATOM 3365 C CB . GLU B 2 103 ? 43.856 -24.274 -43.605 1.00 73.30 ? 103 GLU B CB 1 ATOM 3366 C CG . GLU B 2 103 ? 44.044 -25.672 -42.997 1.00 79.97 ? 103 GLU B CG 1 ATOM 3367 C CD . GLU B 2 103 ? 44.282 -26.775 -44.037 1.00 85.16 ? 103 GLU B CD 1 ATOM 3368 O OE1 . GLU B 2 103 ? 43.697 -26.701 -45.140 1.00 84.74 ? 103 GLU B OE1 1 ATOM 3369 O OE2 . GLU B 2 103 ? 45.057 -27.723 -43.757 1.00 93.63 ? 103 GLU B OE2 1 ATOM 3370 N N . ASN B 2 104 ? 45.060 -21.509 -45.139 1.00 63.84 ? 104 ASN B N 1 ATOM 3371 C CA . ASN B 2 104 ? 44.925 -20.423 -46.103 1.00 65.15 ? 104 ASN B CA 1 ATOM 3372 C C . ASN B 2 104 ? 45.788 -20.644 -47.337 1.00 64.95 ? 104 ASN B C 1 ATOM 3373 O O . ASN B 2 104 ? 45.323 -20.477 -48.454 1.00 63.37 ? 104 ASN B O 1 ATOM 3374 C CB . ASN B 2 104 ? 45.283 -19.092 -45.459 1.00 66.80 ? 104 ASN B CB 1 ATOM 3375 C CG . ASN B 2 104 ? 44.203 -18.607 -44.539 1.00 66.01 ? 104 ASN B CG 1 ATOM 3376 O OD1 . ASN B 2 104 ? 43.120 -19.180 -44.496 1.00 65.86 ? 104 ASN B OD1 1 ATOM 3377 N ND2 . ASN B 2 104 ? 44.487 -17.557 -43.797 1.00 67.46 ? 104 ASN B ND2 1 ATOM 3378 N N . GLU B 2 105 ? 47.041 -21.023 -47.128 1.00 64.66 ? 105 GLU B N 1 ATOM 3379 C CA . GLU B 2 105 ? 47.899 -21.401 -48.231 1.00 66.89 ? 105 GLU B CA 1 ATOM 3380 C C . GLU B 2 105 ? 47.214 -22.443 -49.088 1.00 63.44 ? 105 GLU B C 1 ATOM 3381 O O . GLU B 2 105 ? 47.127 -22.296 -50.297 1.00 63.17 ? 105 GLU B O 1 ATOM 3382 C CB . GLU B 2 105 ? 49.235 -21.949 -47.730 1.00 74.11 ? 105 GLU B CB 1 ATOM 3383 C CG . GLU B 2 105 ? 50.336 -21.924 -48.773 1.00 84.24 ? 105 GLU B CG 1 ATOM 3384 C CD . GLU B 2 105 ? 51.690 -21.557 -48.184 1.00 99.06 ? 105 GLU B CD 1 ATOM 3385 O OE1 . GLU B 2 105 ? 52.354 -22.455 -47.615 1.00 115.96 ? 105 GLU B OE1 1 ATOM 3386 O OE2 . GLU B 2 105 ? 52.095 -20.370 -48.293 1.00 101.85 ? 105 GLU B OE2 1 ATOM 3387 N N . ARG B 2 106 ? 46.707 -23.494 -48.466 1.00 64.50 ? 106 ARG B N 1 ATOM 3388 C CA . ARG B 2 106 ? 46.112 -24.570 -49.240 1.00 67.03 ? 106 ARG B CA 1 ATOM 3389 C C . ARG B 2 106 ? 44.834 -24.114 -49.943 1.00 65.09 ? 106 ARG B C 1 ATOM 3390 O O . ARG B 2 106 ? 44.547 -24.539 -51.055 1.00 67.54 ? 106 ARG B O 1 ATOM 3391 C CB . ARG B 2 106 ? 45.884 -25.806 -48.377 1.00 69.62 ? 106 ARG B CB 1 ATOM 3392 C CG . ARG B 2 106 ? 47.188 -26.433 -47.896 1.00 75.95 ? 106 ARG B CG 1 ATOM 3393 C CD . ARG B 2 106 ? 47.025 -27.887 -47.459 1.00 86.94 ? 106 ARG B CD 1 ATOM 3394 N NE . ARG B 2 106 ? 47.493 -28.860 -48.469 1.00 94.29 ? 106 ARG B NE 1 ATOM 3395 C CZ . ARG B 2 106 ? 46.722 -29.584 -49.287 1.00 96.67 ? 106 ARG B CZ 1 ATOM 3396 N NH1 . ARG B 2 106 ? 45.393 -29.479 -49.273 1.00 100.25 ? 106 ARG B NH1 1 ATOM 3397 N NH2 . ARG B 2 106 ? 47.292 -30.432 -50.140 1.00 103.34 ? 106 ARG B NH2 1 ATOM 3398 N N . THR B 2 107 ? 44.083 -23.222 -49.320 1.00 64.91 ? 107 THR B N 1 ATOM 3399 C CA . THR B 2 107 ? 42.839 -22.765 -49.917 1.00 63.33 ? 107 THR B CA 1 ATOM 3400 C C . THR B 2 107 ? 43.115 -21.966 -51.190 1.00 63.43 ? 107 THR B C 1 ATOM 3401 O O . THR B 2 107 ? 42.459 -22.168 -52.216 1.00 60.47 ? 107 THR B O 1 ATOM 3402 C CB . THR B 2 107 ? 42.009 -21.941 -48.918 1.00 62.93 ? 107 THR B CB 1 ATOM 3403 O OG1 . THR B 2 107 ? 41.468 -22.818 -47.922 1.00 61.81 ? 107 THR B OG1 1 ATOM 3404 C CG2 . THR B 2 107 ? 40.861 -21.227 -49.616 1.00 64.81 ? 107 THR B CG2 1 ATOM 3405 N N . LEU B 2 108 ? 44.086 -21.063 -51.129 1.00 61.39 ? 108 LEU B N 1 ATOM 3406 C CA . LEU B 2 108 ? 44.416 -20.271 -52.294 1.00 60.77 ? 108 LEU B CA 1 ATOM 3407 C C . LEU B 2 108 ? 44.921 -21.163 -53.438 1.00 61.69 ? 108 LEU B C 1 ATOM 3408 O O . LEU B 2 108 ? 44.515 -20.992 -54.586 1.00 58.51 ? 108 LEU B O 1 ATOM 3409 C CB . LEU B 2 108 ? 45.425 -19.193 -51.932 1.00 62.42 ? 108 LEU B CB 1 ATOM 3410 C CG . LEU B 2 108 ? 44.942 -18.145 -50.917 1.00 64.05 ? 108 LEU B CG 1 ATOM 3411 C CD1 . LEU B 2 108 ? 46.015 -17.082 -50.715 1.00 65.84 ? 108 LEU B CD1 1 ATOM 3412 C CD2 . LEU B 2 108 ? 43.633 -17.493 -51.327 1.00 63.68 ? 108 LEU B CD2 1 ATOM 3413 N N . ASP B 2 109 ? 45.771 -22.135 -53.108 1.00 63.93 ? 109 ASP B N 1 ATOM 3414 C CA . ASP B 2 109 ? 46.264 -23.115 -54.084 1.00 65.78 ? 109 ASP B CA 1 ATOM 3415 C C . ASP B 2 109 ? 45.146 -23.977 -54.699 1.00 64.39 ? 109 ASP B C 1 ATOM 3416 O O . ASP B 2 109 ? 45.199 -24.337 -55.874 1.00 66.66 ? 109 ASP B O 1 ATOM 3417 C CB . ASP B 2 109 ? 47.291 -24.036 -53.428 1.00 72.32 ? 109 ASP B CB 1 ATOM 3418 C CG . ASP B 2 109 ? 48.589 -23.309 -53.031 1.00 83.25 ? 109 ASP B CG 1 ATOM 3419 O OD1 . ASP B 2 109 ? 48.965 -22.322 -53.723 1.00 83.09 ? 109 ASP B OD1 1 ATOM 3420 O OD2 . ASP B 2 109 ? 49.237 -23.761 -52.035 1.00 86.01 ? 109 ASP B OD2 1 ATOM 3421 N N . PHE B 2 110 ? 44.155 -24.317 -53.886 1.00 59.76 ? 110 PHE B N 1 ATOM 3422 C CA . PHE B 2 110 ? 43.008 -25.101 -54.311 1.00 58.35 ? 110 PHE B CA 1 ATOM 3423 C C . PHE B 2 110 ? 42.282 -24.386 -55.446 1.00 60.10 ? 110 PHE B C 1 ATOM 3424 O O . PHE B 2 110 ? 41.962 -24.993 -56.470 1.00 59.86 ? 110 PHE B O 1 ATOM 3425 C CB . PHE B 2 110 ? 42.094 -25.318 -53.096 1.00 56.97 ? 110 PHE B CB 1 ATOM 3426 C CG . PHE B 2 110 ? 40.785 -25.978 -53.400 1.00 57.94 ? 110 PHE B CG 1 ATOM 3427 C CD1 . PHE B 2 110 ? 40.730 -27.228 -53.998 1.00 60.10 ? 110 PHE B CD1 1 ATOM 3428 C CD2 . PHE B 2 110 ? 39.587 -25.368 -53.029 1.00 59.08 ? 110 PHE B CD2 1 ATOM 3429 C CE1 . PHE B 2 110 ? 39.500 -27.839 -54.268 1.00 60.73 ? 110 PHE B CE1 1 ATOM 3430 C CE2 . PHE B 2 110 ? 38.359 -25.986 -53.281 1.00 59.16 ? 110 PHE B CE2 1 ATOM 3431 C CZ . PHE B 2 110 ? 38.316 -27.225 -53.903 1.00 57.78 ? 110 PHE B CZ 1 ATOM 3432 N N . HIS B 2 111 ? 42.041 -23.093 -55.257 1.00 59.73 ? 111 HIS B N 1 ATOM 3433 C CA . HIS B 2 111 ? 41.389 -22.271 -56.265 1.00 60.47 ? 111 HIS B CA 1 ATOM 3434 C C . HIS B 2 111 ? 42.220 -22.189 -57.542 1.00 62.15 ? 111 HIS B C 1 ATOM 3435 O O . HIS B 2 111 ? 41.683 -22.292 -58.652 1.00 66.05 ? 111 HIS B O 1 ATOM 3436 C CB . HIS B 2 111 ? 41.152 -20.858 -55.735 1.00 60.42 ? 111 HIS B CB 1 ATOM 3437 C CG . HIS B 2 111 ? 40.026 -20.760 -54.756 1.00 62.69 ? 111 HIS B CG 1 ATOM 3438 N ND1 . HIS B 2 111 ? 38.740 -21.146 -55.065 1.00 63.33 ? 111 HIS B ND1 1 ATOM 3439 C CD2 . HIS B 2 111 ? 39.986 -20.294 -53.485 1.00 63.33 ? 111 HIS B CD2 1 ATOM 3440 C CE1 . HIS B 2 111 ? 37.958 -20.930 -54.023 1.00 64.90 ? 111 HIS B CE1 1 ATOM 3441 N NE2 . HIS B 2 111 ? 38.689 -20.417 -53.049 1.00 63.30 ? 111 HIS B NE2 1 ATOM 3442 N N . ASP B 2 112 ? 43.523 -21.985 -57.375 1.00 59.48 ? 112 ASP B N 1 ATOM 3443 C CA . ASP B 2 112 ? 44.458 -21.948 -58.487 1.00 60.68 ? 112 ASP B CA 1 ATOM 3444 C C . ASP B 2 112 ? 44.325 -23.265 -59.276 1.00 61.73 ? 112 ASP B C 1 ATOM 3445 O O . ASP B 2 112 ? 44.215 -23.276 -60.503 1.00 61.83 ? 112 ASP B O 1 ATOM 3446 C CB . ASP B 2 112 ? 45.881 -21.764 -57.930 1.00 64.44 ? 112 ASP B CB 1 ATOM 3447 C CG . ASP B 2 112 ? 46.890 -21.295 -58.977 1.00 68.23 ? 112 ASP B CG 1 ATOM 3448 O OD1 . ASP B 2 112 ? 46.506 -20.971 -60.119 1.00 69.28 ? 112 ASP B OD1 1 ATOM 3449 O OD2 . ASP B 2 112 ? 48.093 -21.249 -58.641 1.00 71.30 ? 112 ASP B OD2 1 ATOM 3450 N N . SER B 2 113 ? 44.292 -24.373 -58.551 1.00 61.49 ? 113 SER B N 1 ATOM 3451 C CA . SER B 2 113 ? 44.185 -25.692 -59.156 1.00 62.32 ? 113 SER B CA 1 ATOM 3452 C C . SER B 2 113 ? 42.897 -25.877 -59.958 1.00 63.32 ? 113 SER B C 1 ATOM 3453 O O . SER B 2 113 ? 42.908 -26.443 -61.059 1.00 61.19 ? 113 SER B O 1 ATOM 3454 C CB . SER B 2 113 ? 44.260 -26.758 -58.069 1.00 63.53 ? 113 SER B CB 1 ATOM 3455 O OG . SER B 2 113 ? 43.885 -28.020 -58.566 1.00 66.98 ? 113 SER B OG 1 ATOM 3456 N N . ASN B 2 114 ? 41.784 -25.419 -59.401 1.00 61.77 ? 114 ASN B N 1 ATOM 3457 C CA . ASN B 2 114 ? 40.502 -25.565 -60.077 1.00 62.01 ? 114 ASN B CA 1 ATOM 3458 C C . ASN B 2 114 ? 40.492 -24.803 -61.399 1.00 61.14 ? 114 ASN B C 1 ATOM 3459 O O . ASN B 2 114 ? 39.989 -25.319 -62.401 1.00 61.48 ? 114 ASN B O 1 ATOM 3460 C CB . ASN B 2 114 ? 39.351 -25.111 -59.178 1.00 63.75 ? 114 ASN B CB 1 ATOM 3461 C CG . ASN B 2 114 ? 39.215 -25.961 -57.927 1.00 65.99 ? 114 ASN B CG 1 ATOM 3462 O OD1 . ASN B 2 114 ? 39.549 -27.147 -57.920 1.00 66.30 ? 114 ASN B OD1 1 ATOM 3463 N ND2 . ASN B 2 114 ? 38.730 -25.353 -56.857 1.00 66.23 ? 114 ASN B ND2 1 ATOM 3464 N N . VAL B 2 115 ? 41.064 -23.595 -61.399 1.00 57.41 ? 115 VAL B N 1 ATOM 3465 C CA . VAL B 2 115 ? 41.169 -22.789 -62.618 1.00 55.84 ? 115 VAL B CA 1 ATOM 3466 C C . VAL B 2 115 ? 42.069 -23.463 -63.650 1.00 56.92 ? 115 VAL B C 1 ATOM 3467 O O . VAL B 2 115 ? 41.706 -23.587 -64.815 1.00 56.08 ? 115 VAL B O 1 ATOM 3468 C CB . VAL B 2 115 ? 41.757 -21.400 -62.335 1.00 55.63 ? 115 VAL B CB 1 ATOM 3469 C CG1 . VAL B 2 115 ? 42.076 -20.685 -63.636 1.00 57.92 ? 115 VAL B CG1 1 ATOM 3470 C CG2 . VAL B 2 115 ? 40.799 -20.555 -61.519 1.00 57.50 ? 115 VAL B CG2 1 ATOM 3471 N N . LYS B 2 116 ? 43.259 -23.868 -63.216 1.00 57.47 ? 116 LYS B N 1 ATOM 3472 C CA . LYS B 2 116 ? 44.184 -24.599 -64.075 1.00 61.61 ? 116 LYS B CA 1 ATOM 3473 C C . LYS B 2 116 ? 43.521 -25.824 -64.713 1.00 61.99 ? 116 LYS B C 1 ATOM 3474 O O . LYS B 2 116 ? 43.681 -26.079 -65.896 1.00 63.34 ? 116 LYS B O 1 ATOM 3475 C CB . LYS B 2 116 ? 45.407 -25.030 -63.260 1.00 65.15 ? 116 LYS B CB 1 ATOM 3476 C CG . LYS B 2 116 ? 46.482 -25.763 -64.033 1.00 69.80 ? 116 LYS B CG 1 ATOM 3477 C CD . LYS B 2 116 ? 46.930 -24.974 -65.254 1.00 74.35 ? 116 LYS B CD 1 ATOM 3478 C CE . LYS B 2 116 ? 48.129 -25.622 -65.924 1.00 79.89 ? 116 LYS B CE 1 ATOM 3479 N NZ . LYS B 2 116 ? 49.313 -25.603 -65.031 1.00 83.40 ? 116 LYS B NZ 1 ATOM 3480 N N . ASN B 2 117 ? 42.756 -26.561 -63.919 1.00 64.21 ? 117 ASN B N 1 ATOM 3481 C CA . ASN B 2 117 ? 42.088 -27.767 -64.392 1.00 65.51 ? 117 ASN B CA 1 ATOM 3482 C C . ASN B 2 117 ? 40.955 -27.480 -65.365 1.00 65.83 ? 117 ASN B C 1 ATOM 3483 O O . ASN B 2 117 ? 40.713 -28.258 -66.293 1.00 68.18 ? 117 ASN B O 1 ATOM 3484 C CB . ASN B 2 117 ? 41.602 -28.604 -63.203 1.00 64.21 ? 117 ASN B CB 1 ATOM 3485 C CG . ASN B 2 117 ? 42.746 -29.272 -62.473 1.00 66.52 ? 117 ASN B CG 1 ATOM 3486 O OD1 . ASN B 2 117 ? 43.833 -29.433 -63.021 1.00 69.13 ? 117 ASN B OD1 1 ATOM 3487 N ND2 . ASN B 2 117 ? 42.514 -29.661 -61.234 1.00 70.63 ? 117 ASN B ND2 1 ATOM 3488 N N . LEU B 2 118 ? 40.275 -26.363 -65.157 1.00 63.90 ? 118 LEU B N 1 ATOM 3489 C CA . LEU B 2 118 ? 39.241 -25.924 -66.071 1.00 66.54 ? 118 LEU B CA 1 ATOM 3490 C C . LEU B 2 118 ? 39.867 -25.508 -67.401 1.00 68.80 ? 118 LEU B C 1 ATOM 3491 O O . LEU B 2 118 ? 39.397 -25.890 -68.470 1.00 69.97 ? 118 LEU B O 1 ATOM 3492 C CB . LEU B 2 118 ? 38.493 -24.763 -65.446 1.00 67.05 ? 118 LEU B CB 1 ATOM 3493 C CG . LEU B 2 118 ? 37.235 -24.257 -66.118 1.00 71.28 ? 118 LEU B CG 1 ATOM 3494 C CD1 . LEU B 2 118 ? 36.211 -25.364 -66.306 1.00 74.50 ? 118 LEU B CD1 1 ATOM 3495 C CD2 . LEU B 2 118 ? 36.672 -23.138 -65.253 1.00 73.61 ? 118 LEU B CD2 1 ATOM 3496 N N . TYR B 2 119 ? 40.946 -24.738 -67.331 1.00 68.79 ? 119 TYR B N 1 ATOM 3497 C CA . TYR B 2 119 ? 41.685 -24.381 -68.525 1.00 69.51 ? 119 TYR B CA 1 ATOM 3498 C C . TYR B 2 119 ? 42.096 -25.629 -69.303 1.00 72.64 ? 119 TYR B C 1 ATOM 3499 O O . TYR B 2 119 ? 41.988 -25.667 -70.524 1.00 75.37 ? 119 TYR B O 1 ATOM 3500 C CB . TYR B 2 119 ? 42.908 -23.545 -68.162 1.00 69.05 ? 119 TYR B CB 1 ATOM 3501 C CG . TYR B 2 119 ? 43.740 -23.130 -69.356 1.00 70.98 ? 119 TYR B CG 1 ATOM 3502 C CD1 . TYR B 2 119 ? 43.334 -22.092 -70.181 1.00 70.38 ? 119 TYR B CD1 1 ATOM 3503 C CD2 . TYR B 2 119 ? 44.935 -23.776 -69.658 1.00 71.91 ? 119 TYR B CD2 1 ATOM 3504 C CE1 . TYR B 2 119 ? 44.087 -21.707 -71.274 1.00 73.44 ? 119 TYR B CE1 1 ATOM 3505 C CE2 . TYR B 2 119 ? 45.695 -23.395 -70.745 1.00 73.43 ? 119 TYR B CE2 1 ATOM 3506 C CZ . TYR B 2 119 ? 45.263 -22.363 -71.548 1.00 75.44 ? 119 TYR B CZ 1 ATOM 3507 O OH . TYR B 2 119 ? 46.009 -21.981 -72.628 1.00 79.84 ? 119 TYR B OH 1 ATOM 3508 N N . ASP B 2 120 ? 42.554 -26.655 -68.602 1.00 74.29 ? 120 ASP B N 1 ATOM 3509 C CA . ASP B 2 120 ? 42.989 -27.874 -69.273 1.00 80.11 ? 120 ASP B CA 1 ATOM 3510 C C . ASP B 2 120 ? 41.814 -28.655 -69.869 1.00 79.62 ? 120 ASP B C 1 ATOM 3511 O O . ASP B 2 120 ? 41.929 -29.204 -70.950 1.00 83.29 ? 120 ASP B O 1 ATOM 3512 C CB . ASP B 2 120 ? 43.828 -28.752 -68.331 1.00 84.45 ? 120 ASP B CB 1 ATOM 3513 C CG . ASP B 2 120 ? 45.238 -28.191 -68.093 1.00 88.37 ? 120 ASP B CG 1 ATOM 3514 O OD1 . ASP B 2 120 ? 45.858 -27.688 -69.052 1.00 93.71 ? 120 ASP B OD1 1 ATOM 3515 O OD2 . ASP B 2 120 ? 45.740 -28.261 -66.947 1.00 92.89 ? 120 ASP B OD2 1 ATOM 3516 N N . LYS B 2 121 ? 40.686 -28.689 -69.176 1.00 80.79 ? 121 LYS B N 1 ATOM 3517 C CA . LYS B 2 121 ? 39.487 -29.363 -69.676 1.00 84.58 ? 121 LYS B CA 1 ATOM 3518 C C . LYS B 2 121 ? 39.099 -28.837 -71.052 1.00 84.55 ? 121 LYS B C 1 ATOM 3519 O O . LYS B 2 121 ? 38.721 -29.606 -71.935 1.00 91.33 ? 121 LYS B O 1 ATOM 3520 C CB . LYS B 2 121 ? 38.338 -29.134 -68.702 1.00 90.03 ? 121 LYS B CB 1 ATOM 3521 C CG . LYS B 2 121 ? 37.057 -29.896 -68.972 1.00 98.56 ? 121 LYS B CG 1 ATOM 3522 C CD . LYS B 2 121 ? 36.034 -29.540 -67.894 1.00 105.69 ? 121 LYS B CD 1 ATOM 3523 C CE . LYS B 2 121 ? 34.742 -30.336 -68.022 1.00 114.75 ? 121 LYS B CE 1 ATOM 3524 N NZ . LYS B 2 121 ? 34.014 -30.055 -69.296 1.00 119.29 ? 121 LYS B NZ 1 ATOM 3525 N N . VAL B 2 122 ? 39.214 -27.525 -71.226 1.00 79.26 ? 122 VAL B N 1 ATOM 3526 C CA . VAL B 2 122 ? 38.882 -26.871 -72.483 1.00 78.68 ? 122 VAL B CA 1 ATOM 3527 C C . VAL B 2 122 ? 39.977 -27.073 -73.526 1.00 79.97 ? 122 VAL B C 1 ATOM 3528 O O . VAL B 2 122 ? 39.696 -27.380 -74.684 1.00 82.04 ? 122 VAL B O 1 ATOM 3529 C CB . VAL B 2 122 ? 38.621 -25.369 -72.257 1.00 77.30 ? 122 VAL B CB 1 ATOM 3530 C CG1 . VAL B 2 122 ? 38.414 -24.632 -73.574 1.00 77.75 ? 122 VAL B CG1 1 ATOM 3531 C CG2 . VAL B 2 122 ? 37.410 -25.201 -71.351 1.00 77.49 ? 122 VAL B CG2 1 ATOM 3532 N N . ARG B 2 123 ? 41.224 -26.896 -73.125 1.00 79.21 ? 123 ARG B N 1 ATOM 3533 C CA . ARG B 2 123 ? 42.334 -27.144 -74.028 1.00 82.43 ? 123 ARG B CA 1 ATOM 3534 C C . ARG B 2 123 ? 42.242 -28.551 -74.646 1.00 87.65 ? 123 ARG B C 1 ATOM 3535 O O . ARG B 2 123 ? 42.406 -28.717 -75.860 1.00 88.92 ? 123 ARG B O 1 ATOM 3536 C CB . ARG B 2 123 ? 43.652 -26.980 -73.284 1.00 82.26 ? 123 ARG B CB 1 ATOM 3537 C CG . ARG B 2 123 ? 44.864 -26.999 -74.191 1.00 86.39 ? 123 ARG B CG 1 ATOM 3538 C CD . ARG B 2 123 ? 46.140 -26.770 -73.405 1.00 89.40 ? 123 ARG B CD 1 ATOM 3539 N NE . ARG B 2 123 ? 46.258 -27.691 -72.274 1.00 93.85 ? 123 ARG B NE 1 ATOM 3540 C CZ . ARG B 2 123 ? 46.587 -28.981 -72.362 1.00 95.32 ? 123 ARG B CZ 1 ATOM 3541 N NH1 . ARG B 2 123 ? 46.840 -29.554 -73.536 1.00 97.43 ? 123 ARG B NH1 1 ATOM 3542 N NH2 . ARG B 2 123 ? 46.659 -29.707 -71.256 1.00 96.42 ? 123 ARG B NH2 1 ATOM 3543 N N . LEU B 2 124 ? 41.955 -29.549 -73.808 1.00 89.81 ? 124 LEU B N 1 ATOM 3544 C CA . LEU B 2 124 ? 41.883 -30.950 -74.246 1.00 95.88 ? 124 LEU B CA 1 ATOM 3545 C C . LEU B 2 124 ? 40.723 -31.234 -75.205 1.00 97.62 ? 124 LEU B C 1 ATOM 3546 O O . LEU B 2 124 ? 40.729 -32.244 -75.902 1.00 99.67 ? 124 LEU B O 1 ATOM 3547 C CB . LEU B 2 124 ? 41.782 -31.887 -73.037 1.00 98.37 ? 124 LEU B CB 1 ATOM 3548 C CG . LEU B 2 124 ? 43.032 -31.966 -72.143 1.00 101.35 ? 124 LEU B CG 1 ATOM 3549 C CD1 . LEU B 2 124 ? 42.711 -32.532 -70.759 1.00 101.37 ? 124 LEU B CD1 1 ATOM 3550 C CD2 . LEU B 2 124 ? 44.133 -32.773 -72.817 1.00 104.62 ? 124 LEU B CD2 1 ATOM 3551 N N . GLN B 2 125 ? 39.725 -30.356 -75.214 1.00 98.05 ? 125 GLN B N 1 ATOM 3552 C CA . GLN B 2 125 ? 38.611 -30.456 -76.146 1.00 98.18 ? 125 GLN B CA 1 ATOM 3553 C C . GLN B 2 125 ? 38.967 -29.825 -77.474 1.00 99.40 ? 125 GLN B C 1 ATOM 3554 O O . GLN B 2 125 ? 38.745 -30.419 -78.528 1.00 105.05 ? 125 GLN B O 1 ATOM 3555 C CB . GLN B 2 125 ? 37.380 -29.749 -75.595 1.00 98.53 ? 125 GLN B CB 1 ATOM 3556 C CG . GLN B 2 125 ? 36.618 -30.536 -74.553 1.00 102.39 ? 125 GLN B CG 1 ATOM 3557 C CD . GLN B 2 125 ? 35.289 -29.889 -74.246 1.00 106.97 ? 125 GLN B CD 1 ATOM 3558 O OE1 . GLN B 2 125 ? 34.273 -30.212 -74.866 1.00 116.56 ? 125 GLN B OE1 1 ATOM 3559 N NE2 . GLN B 2 125 ? 35.294 -28.938 -73.321 1.00 104.82 ? 125 GLN B NE2 1 ATOM 3560 N N . LEU B 2 126 ? 39.512 -28.615 -77.417 1.00 98.18 ? 126 LEU B N 1 ATOM 3561 C CA . LEU B 2 126 ? 39.776 -27.836 -78.622 1.00 99.54 ? 126 LEU B CA 1 ATOM 3562 C C . LEU B 2 126 ? 40.875 -28.450 -79.472 1.00 106.37 ? 126 LEU B C 1 ATOM 3563 O O . LEU B 2 126 ? 40.743 -28.524 -80.692 1.00 112.95 ? 126 LEU B O 1 ATOM 3564 C CB . LEU B 2 126 ? 40.134 -26.394 -78.269 1.00 94.54 ? 126 LEU B CB 1 ATOM 3565 C CG . LEU B 2 126 ? 39.088 -25.595 -77.490 1.00 90.46 ? 126 LEU B CG 1 ATOM 3566 C CD1 . LEU B 2 126 ? 39.443 -24.118 -77.526 1.00 90.35 ? 126 LEU B CD1 1 ATOM 3567 C CD2 . LEU B 2 126 ? 37.688 -25.808 -78.033 1.00 90.69 ? 126 LEU B CD2 1 ATOM 3568 N N . ARG B 2 127 ? 41.955 -28.878 -78.828 1.00 113.67 ? 127 ARG B N 1 ATOM 3569 C CA . ARG B 2 127 ? 43.035 -29.593 -79.512 1.00 121.77 ? 127 ARG B CA 1 ATOM 3570 C C . ARG B 2 127 ? 43.673 -28.705 -80.601 1.00 120.99 ? 127 ARG B C 1 ATOM 3571 O O . ARG B 2 127 ? 44.141 -27.607 -80.298 1.00 116.17 ? 127 ARG B O 1 ATOM 3572 C CB . ARG B 2 127 ? 42.523 -30.943 -80.063 1.00 128.87 ? 127 ARG B CB 1 ATOM 3573 C CG . ARG B 2 127 ? 41.683 -31.745 -79.072 1.00 130.42 ? 127 ARG B CG 1 ATOM 3574 C CD . ARG B 2 127 ? 42.142 -33.186 -78.932 1.00 133.47 ? 127 ARG B CD 1 ATOM 3575 N NE . ARG B 2 127 ? 41.594 -34.082 -79.950 1.00 140.74 ? 127 ARG B NE 1 ATOM 3576 C CZ . ARG B 2 127 ? 40.406 -34.687 -79.879 1.00 145.95 ? 127 ARG B CZ 1 ATOM 3577 N NH1 . ARG B 2 127 ? 39.591 -34.483 -78.843 1.00 145.91 ? 127 ARG B NH1 1 ATOM 3578 N NH2 . ARG B 2 127 ? 40.022 -35.499 -80.859 1.00 148.19 ? 127 ARG B NH2 1 ATOM 3579 N N . ASP B 2 128 ? 43.685 -29.164 -81.851 1.00 123.99 ? 128 ASP B N 1 ATOM 3580 C CA . ASP B 2 128 ? 44.264 -28.391 -82.953 1.00 122.98 ? 128 ASP B CA 1 ATOM 3581 C C . ASP B 2 128 ? 43.313 -27.325 -83.540 1.00 118.95 ? 128 ASP B C 1 ATOM 3582 O O . ASP B 2 128 ? 43.756 -26.470 -84.303 1.00 119.78 ? 128 ASP B O 1 ATOM 3583 C CB . ASP B 2 128 ? 44.795 -29.322 -84.069 1.00 131.06 ? 128 ASP B CB 1 ATOM 3584 C CG . ASP B 2 128 ? 43.854 -30.485 -84.387 1.00 136.58 ? 128 ASP B CG 1 ATOM 3585 O OD1 . ASP B 2 128 ? 43.277 -31.064 -83.444 1.00 138.07 ? 128 ASP B OD1 1 ATOM 3586 O OD2 . ASP B 2 128 ? 43.708 -30.830 -85.582 1.00 140.79 ? 128 ASP B OD2 1 ATOM 3587 N N . ASN B 2 129 ? 42.029 -27.354 -83.172 1.00 116.24 ? 129 ASN B N 1 ATOM 3588 C CA . ASN B 2 129 ? 41.014 -26.464 -83.786 1.00 114.82 ? 129 ASN B CA 1 ATOM 3589 C C . ASN B 2 129 ? 40.975 -25.017 -83.278 1.00 109.33 ? 129 ASN B C 1 ATOM 3590 O O . ASN B 2 129 ? 40.153 -24.216 -83.744 1.00 105.76 ? 129 ASN B O 1 ATOM 3591 C CB . ASN B 2 129 ? 39.609 -27.053 -83.622 1.00 119.03 ? 129 ASN B CB 1 ATOM 3592 C CG . ASN B 2 129 ? 39.467 -28.424 -84.254 1.00 127.85 ? 129 ASN B CG 1 ATOM 3593 O OD1 . ASN B 2 129 ? 40.437 -29.174 -84.373 1.00 139.07 ? 129 ASN B OD1 1 ATOM 3594 N ND2 . ASN B 2 129 ? 38.248 -28.763 -84.654 1.00 126.63 ? 129 ASN B ND2 1 ATOM 3595 N N . ALA B 2 130 ? 41.833 -24.688 -82.315 1.00 103.12 ? 130 ALA B N 1 ATOM 3596 C CA . ALA B 2 130 ? 41.917 -23.328 -81.798 1.00 98.63 ? 130 ALA B CA 1 ATOM 3597 C C . ALA B 2 130 ? 43.360 -22.995 -81.500 1.00 95.19 ? 130 ALA B C 1 ATOM 3598 O O . ALA B 2 130 ? 44.128 -23.875 -81.146 1.00 96.91 ? 130 ALA B O 1 ATOM 3599 C CB . ALA B 2 130 ? 41.081 -23.194 -80.536 1.00 97.47 ? 130 ALA B CB 1 ATOM 3600 N N . LYS B 2 131 ? 43.731 -21.730 -81.650 1.00 93.30 ? 131 LYS B N 1 ATOM 3601 C CA . LYS B 2 131 ? 45.053 -21.284 -81.247 1.00 94.79 ? 131 LYS B CA 1 ATOM 3602 C C . LYS B 2 131 ? 45.049 -20.984 -79.756 1.00 89.99 ? 131 LYS B C 1 ATOM 3603 O O . LYS B 2 131 ? 44.193 -20.259 -79.261 1.00 85.58 ? 131 LYS B O 1 ATOM 3604 C CB . LYS B 2 131 ? 45.484 -20.043 -82.031 1.00 102.04 ? 131 LYS B CB 1 ATOM 3605 C CG . LYS B 2 131 ? 46.849 -19.495 -81.608 1.00 109.53 ? 131 LYS B CG 1 ATOM 3606 C CD . LYS B 2 131 ? 47.733 -19.134 -82.799 1.00 117.80 ? 131 LYS B CD 1 ATOM 3607 C CE . LYS B 2 131 ? 47.355 -17.802 -83.439 1.00 122.05 ? 131 LYS B CE 1 ATOM 3608 N NZ . LYS B 2 131 ? 46.051 -17.827 -84.169 1.00 122.54 ? 131 LYS B NZ 1 ATOM 3609 N N . GLU B 2 132 ? 46.011 -21.549 -79.045 1.00 89.51 ? 132 GLU B N 1 ATOM 3610 C CA . GLU B 2 132 ? 46.155 -21.289 -77.629 1.00 88.09 ? 132 GLU B CA 1 ATOM 3611 C C . GLU B 2 132 ? 46.928 -19.980 -77.472 1.00 87.86 ? 132 GLU B C 1 ATOM 3612 O O . GLU B 2 132 ? 48.106 -19.918 -77.770 1.00 90.23 ? 132 GLU B O 1 ATOM 3613 C CB . GLU B 2 132 ? 46.886 -22.448 -76.975 1.00 89.99 ? 132 GLU B CB 1 ATOM 3614 C CG . GLU B 2 132 ? 46.803 -22.466 -75.461 1.00 90.11 ? 132 GLU B CG 1 ATOM 3615 C CD . GLU B 2 132 ? 47.626 -23.583 -74.838 1.00 91.33 ? 132 GLU B CD 1 ATOM 3616 O OE1 . GLU B 2 132 ? 48.433 -24.220 -75.562 1.00 93.74 ? 132 GLU B OE1 1 ATOM 3617 O OE2 . GLU B 2 132 ? 47.467 -23.814 -73.618 1.00 89.20 ? 132 GLU B OE2 1 ATOM 3618 N N . LEU B 2 133 ? 46.252 -18.936 -77.011 1.00 87.55 ? 133 LEU B N 1 ATOM 3619 C CA . LEU B 2 133 ? 46.808 -17.580 -77.030 1.00 88.25 ? 133 LEU B CA 1 ATOM 3620 C C . LEU B 2 133 ? 47.906 -17.327 -76.009 1.00 87.81 ? 133 LEU B C 1 ATOM 3621 O O . LEU B 2 133 ? 48.697 -16.412 -76.184 1.00 87.32 ? 133 LEU B O 1 ATOM 3622 C CB . LEU B 2 133 ? 45.688 -16.545 -76.834 1.00 90.44 ? 133 LEU B CB 1 ATOM 3623 C CG . LEU B 2 133 ? 44.969 -15.993 -78.077 1.00 92.98 ? 133 LEU B CG 1 ATOM 3624 C CD1 . LEU B 2 133 ? 45.535 -14.637 -78.470 1.00 95.31 ? 133 LEU B CD1 1 ATOM 3625 C CD2 . LEU B 2 133 ? 45.015 -16.946 -79.264 1.00 94.14 ? 133 LEU B CD2 1 ATOM 3626 N N . GLY B 2 134 ? 47.936 -18.114 -74.938 1.00 89.17 ? 134 GLY B N 1 ATOM 3627 C CA . GLY B 2 134 ? 48.953 -17.971 -73.892 1.00 88.20 ? 134 GLY B CA 1 ATOM 3628 C C . GLY B 2 134 ? 48.509 -17.168 -72.680 1.00 86.62 ? 134 GLY B C 1 ATOM 3629 O O . GLY B 2 134 ? 49.311 -16.911 -71.785 1.00 88.31 ? 134 GLY B O 1 ATOM 3630 N N . ASN B 2 135 ? 47.233 -16.795 -72.628 1.00 83.50 ? 135 ASN B N 1 ATOM 3631 C CA . ASN B 2 135 ? 46.737 -15.883 -71.593 1.00 83.20 ? 135 ASN B CA 1 ATOM 3632 C C . ASN B 2 135 ? 45.409 -16.319 -70.972 1.00 81.56 ? 135 ASN B C 1 ATOM 3633 O O . ASN B 2 135 ? 44.713 -15.505 -70.354 1.00 76.00 ? 135 ASN B O 1 ATOM 3634 C CB . ASN B 2 135 ? 46.571 -14.485 -72.193 1.00 83.90 ? 135 ASN B CB 1 ATOM 3635 C CG . ASN B 2 135 ? 45.565 -14.453 -73.328 1.00 83.68 ? 135 ASN B CG 1 ATOM 3636 O OD1 . ASN B 2 135 ? 45.130 -15.492 -73.830 1.00 81.12 ? 135 ASN B OD1 1 ATOM 3637 N ND2 . ASN B 2 135 ? 45.198 -13.259 -73.744 1.00 87.10 ? 135 ASN B ND2 1 ATOM 3638 N N . GLY B 2 136 ? 45.071 -17.597 -71.142 1.00 81.04 ? 136 GLY B N 1 ATOM 3639 C CA . GLY B 2 136 ? 43.766 -18.124 -70.749 1.00 78.56 ? 136 GLY B CA 1 ATOM 3640 C C . GLY B 2 136 ? 42.769 -18.252 -71.893 1.00 77.08 ? 136 GLY B C 1 ATOM 3641 O O . GLY B 2 136 ? 41.730 -18.886 -71.732 1.00 73.95 ? 136 GLY B O 1 ATOM 3642 N N . CYS B 2 137 ? 43.085 -17.672 -73.050 1.00 78.89 ? 137 CYS B N 1 ATOM 3643 C CA . CYS B 2 137 ? 42.136 -17.607 -74.154 1.00 80.41 ? 137 CYS B CA 1 ATOM 3644 C C . CYS B 2 137 ? 42.455 -18.551 -75.291 1.00 77.67 ? 137 CYS B C 1 ATOM 3645 O O . CYS B 2 137 ? 43.586 -18.967 -75.482 1.00 75.71 ? 137 CYS B O 1 ATOM 3646 C CB . CYS B 2 137 ? 42.043 -16.185 -74.700 1.00 86.67 ? 137 CYS B CB 1 ATOM 3647 S SG . CYS B 2 137 ? 41.514 -14.979 -73.463 1.00 98.46 ? 137 CYS B SG 1 ATOM 3648 N N . PHE B 2 138 ? 41.422 -18.859 -76.056 1.00 78.01 ? 138 PHE B N 1 ATOM 3649 C CA . PHE B 2 138 ? 41.531 -19.737 -77.190 1.00 80.82 ? 138 PHE B CA 1 ATOM 3650 C C . PHE B 2 138 ? 40.854 -19.068 -78.366 1.00 81.72 ? 138 PHE B C 1 ATOM 3651 O O . PHE B 2 138 ? 39.656 -18.856 -78.331 1.00 81.83 ? 138 PHE B O 1 ATOM 3652 C CB . PHE B 2 138 ? 40.831 -21.062 -76.899 1.00 81.44 ? 138 PHE B CB 1 ATOM 3653 C CG . PHE B 2 138 ? 41.472 -21.855 -75.805 1.00 82.99 ? 138 PHE B CG 1 ATOM 3654 C CD1 . PHE B 2 138 ? 42.595 -22.630 -76.061 1.00 82.52 ? 138 PHE B CD1 1 ATOM 3655 C CD2 . PHE B 2 138 ? 40.952 -21.834 -74.514 1.00 84.41 ? 138 PHE B CD2 1 ATOM 3656 C CE1 . PHE B 2 138 ? 43.187 -23.371 -75.053 1.00 82.10 ? 138 PHE B CE1 1 ATOM 3657 C CE2 . PHE B 2 138 ? 41.546 -22.571 -73.499 1.00 82.47 ? 138 PHE B CE2 1 ATOM 3658 C CZ . PHE B 2 138 ? 42.668 -23.335 -73.769 1.00 82.73 ? 138 PHE B CZ 1 ATOM 3659 N N . GLU B 2 139 ? 41.621 -18.743 -79.400 1.00 85.67 ? 139 GLU B N 1 ATOM 3660 C CA . GLU B 2 139 ? 41.065 -18.190 -80.626 1.00 91.27 ? 139 GLU B CA 1 ATOM 3661 C C . GLU B 2 139 ? 40.746 -19.329 -81.596 1.00 90.74 ? 139 GLU B C 1 ATOM 3662 O O . GLU B 2 139 ? 41.618 -20.128 -81.929 1.00 92.70 ? 139 GLU B O 1 ATOM 3663 C CB . GLU B 2 139 ? 42.057 -17.214 -81.248 1.00 96.88 ? 139 GLU B CB 1 ATOM 3664 C CG . GLU B 2 139 ? 41.540 -16.490 -82.475 1.00 104.82 ? 139 GLU B CG 1 ATOM 3665 C CD . GLU B 2 139 ? 42.594 -15.615 -83.131 1.00 114.94 ? 139 GLU B CD 1 ATOM 3666 O OE1 . GLU B 2 139 ? 43.780 -16.019 -83.188 1.00 117.98 ? 139 GLU B OE1 1 ATOM 3667 O OE2 . GLU B 2 139 ? 42.230 -14.515 -83.601 1.00 126.80 ? 139 GLU B OE2 1 ATOM 3668 N N . PHE B 2 140 ? 39.495 -19.398 -82.043 1.00 89.44 ? 140 PHE B N 1 ATOM 3669 C CA . PHE B 2 140 ? 39.044 -20.470 -82.933 1.00 91.45 ? 140 PHE B CA 1 ATOM 3670 C C . PHE B 2 140 ? 39.462 -20.228 -84.381 1.00 96.87 ? 140 PHE B C 1 ATOM 3671 O O . PHE B 2 140 ? 39.541 -19.078 -84.826 1.00 98.35 ? 140 PHE B O 1 ATOM 3672 C CB . PHE B 2 140 ? 37.526 -20.595 -82.872 1.00 88.31 ? 140 PHE B CB 1 ATOM 3673 C CG . PHE B 2 140 ? 37.015 -21.067 -81.552 1.00 88.20 ? 140 PHE B CG 1 ATOM 3674 C CD1 . PHE B 2 140 ? 36.748 -20.167 -80.533 1.00 89.55 ? 140 PHE B CD1 1 ATOM 3675 C CD2 . PHE B 2 140 ? 36.794 -22.416 -81.327 1.00 89.80 ? 140 PHE B CD2 1 ATOM 3676 C CE1 . PHE B 2 140 ? 36.267 -20.605 -79.313 1.00 89.93 ? 140 PHE B CE1 1 ATOM 3677 C CE2 . PHE B 2 140 ? 36.315 -22.865 -80.109 1.00 89.53 ? 140 PHE B CE2 1 ATOM 3678 C CZ . PHE B 2 140 ? 36.051 -21.959 -79.100 1.00 90.08 ? 140 PHE B CZ 1 ATOM 3679 N N . TYR B 2 141 ? 39.720 -21.309 -85.118 1.00 100.14 ? 141 TYR B N 1 ATOM 3680 C CA . TYR B 2 141 ? 40.039 -21.194 -86.545 1.00 104.23 ? 141 TYR B CA 1 ATOM 3681 C C . TYR B 2 141 ? 38.763 -21.092 -87.352 1.00 107.56 ? 141 TYR B C 1 ATOM 3682 O O . TYR B 2 141 ? 38.694 -20.329 -88.312 1.00 112.57 ? 141 TYR B O 1 ATOM 3683 C CB . TYR B 2 141 ? 40.916 -22.353 -87.035 1.00 102.81 ? 141 TYR B CB 1 ATOM 3684 C CG . TYR B 2 141 ? 42.289 -22.308 -86.427 1.00 104.41 ? 141 TYR B CG 1 ATOM 3685 C CD1 . TYR B 2 141 ? 43.050 -21.141 -86.477 1.00 106.55 ? 141 TYR B CD1 1 ATOM 3686 C CD2 . TYR B 2 141 ? 42.814 -23.407 -85.754 1.00 106.94 ? 141 TYR B CD2 1 ATOM 3687 C CE1 . TYR B 2 141 ? 44.301 -21.075 -85.894 1.00 109.03 ? 141 TYR B CE1 1 ATOM 3688 C CE2 . TYR B 2 141 ? 44.070 -23.353 -85.172 1.00 107.95 ? 141 TYR B CE2 1 ATOM 3689 C CZ . TYR B 2 141 ? 44.808 -22.183 -85.245 1.00 110.03 ? 141 TYR B CZ 1 ATOM 3690 O OH . TYR B 2 141 ? 46.053 -22.119 -84.669 1.00 111.26 ? 141 TYR B OH 1 ATOM 3691 N N . HIS B 2 142 ? 37.757 -21.859 -86.952 1.00 107.97 ? 142 HIS B N 1 ATOM 3692 C CA . HIS B 2 142 ? 36.420 -21.721 -87.515 1.00 109.63 ? 142 HIS B CA 1 ATOM 3693 C C . HIS B 2 142 ? 35.676 -20.603 -86.804 1.00 109.01 ? 142 HIS B C 1 ATOM 3694 O O . HIS B 2 142 ? 36.036 -20.205 -85.699 1.00 109.06 ? 142 HIS B O 1 ATOM 3695 C CB . HIS B 2 142 ? 35.631 -23.033 -87.407 1.00 111.47 ? 142 HIS B CB 1 ATOM 3696 C CG . HIS B 2 142 ? 35.553 -23.592 -86.019 1.00 108.87 ? 142 HIS B CG 1 ATOM 3697 N ND1 . HIS B 2 142 ? 34.441 -23.444 -85.218 1.00 107.53 ? 142 HIS B ND1 1 ATOM 3698 C CD2 . HIS B 2 142 ? 36.445 -24.311 -85.295 1.00 108.23 ? 142 HIS B CD2 1 ATOM 3699 C CE1 . HIS B 2 142 ? 34.654 -24.043 -84.060 1.00 107.22 ? 142 HIS B CE1 1 ATOM 3700 N NE2 . HIS B 2 142 ? 35.862 -24.577 -84.081 1.00 106.47 ? 142 HIS B NE2 1 ATOM 3701 N N . LYS B 2 143 ? 34.646 -20.087 -87.457 1.00 111.52 ? 143 LYS B N 1 ATOM 3702 C CA . LYS B 2 143 ? 33.708 -19.191 -86.801 1.00 113.83 ? 143 LYS B CA 1 ATOM 3703 C C . LYS B 2 143 ? 32.966 -20.030 -85.747 1.00 111.44 ? 143 LYS B C 1 ATOM 3704 O O . LYS B 2 143 ? 32.574 -21.165 -86.030 1.00 112.02 ? 143 LYS B O 1 ATOM 3705 C CB . LYS B 2 143 ? 32.736 -18.610 -87.831 1.00 119.98 ? 143 LYS B CB 1 ATOM 3706 C CG . LYS B 2 143 ? 32.145 -17.262 -87.462 1.00 126.22 ? 143 LYS B CG 1 ATOM 3707 C CD . LYS B 2 143 ? 30.755 -17.070 -88.060 1.00 132.00 ? 143 LYS B CD 1 ATOM 3708 C CE . LYS B 2 143 ? 29.680 -17.722 -87.197 1.00 135.11 ? 143 LYS B CE 1 ATOM 3709 N NZ . LYS B 2 143 ? 28.302 -17.508 -87.723 1.00 137.45 ? 143 LYS B NZ 1 ATOM 3710 N N . CYS B 2 144 ? 32.801 -19.491 -84.537 1.00 107.31 ? 144 CYS B N 1 ATOM 3711 C CA . CYS B 2 144 ? 32.167 -20.224 -83.426 1.00 104.40 ? 144 CYS B CA 1 ATOM 3712 C C . CYS B 2 144 ? 31.041 -19.391 -82.809 1.00 100.78 ? 144 CYS B C 1 ATOM 3713 O O . CYS B 2 144 ? 31.290 -18.480 -82.027 1.00 99.38 ? 144 CYS B O 1 ATOM 3714 C CB . CYS B 2 144 ? 33.220 -20.596 -82.372 1.00 104.32 ? 144 CYS B CB 1 ATOM 3715 S SG . CYS B 2 144 ? 32.656 -21.573 -80.948 1.00 110.76 ? 144 CYS B SG 1 ATOM 3716 N N . ASP B 2 145 ? 29.801 -19.710 -83.178 1.00 101.45 ? 145 ASP B N 1 ATOM 3717 C CA . ASP B 2 145 ? 28.622 -18.964 -82.721 1.00 99.25 ? 145 ASP B CA 1 ATOM 3718 C C . ASP B 2 145 ? 28.231 -19.356 -81.291 1.00 95.94 ? 145 ASP B C 1 ATOM 3719 O O . ASP B 2 145 ? 28.889 -20.190 -80.677 1.00 92.71 ? 145 ASP B O 1 ATOM 3720 C CB . ASP B 2 145 ? 27.452 -19.175 -83.692 1.00 101.83 ? 145 ASP B CB 1 ATOM 3721 C CG . ASP B 2 145 ? 26.898 -20.591 -83.661 1.00 106.15 ? 145 ASP B CG 1 ATOM 3722 O OD1 . ASP B 2 145 ? 27.508 -21.479 -83.030 1.00 108.32 ? 145 ASP B OD1 1 ATOM 3723 O OD2 . ASP B 2 145 ? 25.838 -20.815 -84.278 1.00 113.21 ? 145 ASP B OD2 1 ATOM 3724 N N . ASN B 2 146 ? 27.161 -18.764 -80.766 1.00 94.71 ? 146 ASN B N 1 ATOM 3725 C CA . ASN B 2 146 ? 26.770 -18.993 -79.371 1.00 95.72 ? 146 ASN B CA 1 ATOM 3726 C C . ASN B 2 146 ? 26.497 -20.460 -79.015 1.00 98.82 ? 146 ASN B C 1 ATOM 3727 O O . ASN B 2 146 ? 26.782 -20.884 -77.895 1.00 97.37 ? 146 ASN B O 1 ATOM 3728 C CB . ASN B 2 146 ? 25.558 -18.132 -78.994 1.00 94.84 ? 146 ASN B CB 1 ATOM 3729 C CG . ASN B 2 146 ? 25.894 -16.649 -78.863 1.00 93.09 ? 146 ASN B CG 1 ATOM 3730 O OD1 . ASN B 2 146 ? 27.055 -16.246 -78.725 1.00 88.62 ? 146 ASN B OD1 1 ATOM 3731 N ND2 . ASN B 2 146 ? 24.863 -15.827 -78.893 1.00 95.54 ? 146 ASN B ND2 1 ATOM 3732 N N . GLU B 2 147 ? 25.963 -21.230 -79.961 1.00 105.51 ? 147 GLU B N 1 ATOM 3733 C CA . GLU B 2 147 ? 25.699 -22.657 -79.730 1.00 112.61 ? 147 GLU B CA 1 ATOM 3734 C C . GLU B 2 147 ? 26.992 -23.479 -79.731 1.00 109.60 ? 147 GLU B C 1 ATOM 3735 O O . GLU B 2 147 ? 27.142 -24.426 -78.955 1.00 108.06 ? 147 GLU B O 1 ATOM 3736 C CB . GLU B 2 147 ? 24.722 -23.215 -80.768 1.00 122.29 ? 147 GLU B CB 1 ATOM 3737 C CG . GLU B 2 147 ? 23.277 -22.769 -80.577 1.00 130.84 ? 147 GLU B CG 1 ATOM 3738 C CD . GLU B 2 147 ? 22.967 -21.420 -81.214 1.00 136.63 ? 147 GLU B CD 1 ATOM 3739 O OE1 . GLU B 2 147 ? 23.318 -21.211 -82.401 1.00 137.14 ? 147 GLU B OE1 1 ATOM 3740 O OE2 . GLU B 2 147 ? 22.363 -20.568 -80.526 1.00 140.98 ? 147 GLU B OE2 1 ATOM 3741 N N . CYS B 2 148 ? 27.912 -23.119 -80.618 1.00 107.27 ? 148 CYS B N 1 ATOM 3742 C CA . CYS B 2 148 ? 29.266 -23.665 -80.601 1.00 106.47 ? 148 CYS B CA 1 ATOM 3743 C C . CYS B 2 148 ? 29.918 -23.411 -79.226 1.00 101.54 ? 148 CYS B C 1 ATOM 3744 O O . CYS B 2 148 ? 30.454 -24.328 -78.597 1.00 101.78 ? 148 CYS B O 1 ATOM 3745 C CB . CYS B 2 148 ? 30.079 -23.034 -81.741 1.00 108.09 ? 148 CYS B CB 1 ATOM 3746 S SG . CYS B 2 148 ? 31.861 -23.314 -81.715 1.00 117.56 ? 148 CYS B SG 1 ATOM 3747 N N . MET B 2 149 ? 29.830 -22.168 -78.756 1.00 94.53 ? 149 MET B N 1 ATOM 3748 C CA . MET B 2 149 ? 30.380 -21.783 -77.463 1.00 90.32 ? 149 MET B CA 1 ATOM 3749 C C . MET B 2 149 ? 29.767 -22.586 -76.320 1.00 90.01 ? 149 MET B C 1 ATOM 3750 O O . MET B 2 149 ? 30.478 -23.083 -75.452 1.00 86.67 ? 149 MET B O 1 ATOM 3751 C CB . MET B 2 149 ? 30.154 -20.291 -77.209 1.00 90.67 ? 149 MET B CB 1 ATOM 3752 C CG . MET B 2 149 ? 30.898 -19.346 -78.150 1.00 90.67 ? 149 MET B CG 1 ATOM 3753 S SD . MET B 2 149 ? 32.703 -19.407 -78.030 1.00 89.19 ? 149 MET B SD 1 ATOM 3754 C CE . MET B 2 149 ? 33.156 -17.969 -78.997 1.00 84.57 ? 149 MET B CE 1 ATOM 3755 N N . GLU B 2 150 ? 28.446 -22.709 -76.313 1.00 94.96 ? 150 GLU B N 1 ATOM 3756 C CA . GLU B 2 150 ? 27.776 -23.481 -75.271 1.00 98.88 ? 150 GLU B CA 1 ATOM 3757 C C . GLU B 2 150 ? 28.285 -24.919 -75.257 1.00 98.04 ? 150 GLU B C 1 ATOM 3758 O O . GLU B 2 150 ? 28.472 -25.496 -74.186 1.00 93.15 ? 150 GLU B O 1 ATOM 3759 C CB . GLU B 2 150 ? 26.255 -23.434 -75.452 1.00 106.17 ? 150 GLU B CB 1 ATOM 3760 C CG . GLU B 2 150 ? 25.444 -24.289 -74.475 1.00 113.62 ? 150 GLU B CG 1 ATOM 3761 C CD . GLU B 2 150 ? 25.631 -23.914 -73.012 1.00 117.40 ? 150 GLU B CD 1 ATOM 3762 O OE1 . GLU B 2 150 ? 26.135 -22.810 -72.720 1.00 123.67 ? 150 GLU B OE1 1 ATOM 3763 O OE2 . GLU B 2 150 ? 25.264 -24.731 -72.140 1.00 121.57 ? 150 GLU B OE2 1 ATOM 3764 N N . SER B 2 151 ? 28.525 -25.476 -76.445 1.00 99.66 ? 151 SER B N 1 ATOM 3765 C CA . SER B 2 151 ? 29.010 -26.853 -76.583 1.00 102.89 ? 151 SER B CA 1 ATOM 3766 C C . SER B 2 151 ? 30.394 -27.032 -75.966 1.00 102.00 ? 151 SER B C 1 ATOM 3767 O O . SER B 2 151 ? 30.724 -28.117 -75.480 1.00 105.81 ? 151 SER B O 1 ATOM 3768 C CB . SER B 2 151 ? 29.064 -27.267 -78.053 1.00 105.12 ? 151 SER B CB 1 ATOM 3769 O OG . SER B 2 151 ? 30.266 -26.825 -78.659 1.00 104.58 ? 151 SER B OG 1 ATOM 3770 N N . VAL B 2 152 ? 31.204 -25.975 -76.007 1.00 97.22 ? 152 VAL B N 1 ATOM 3771 C CA . VAL B 2 152 ? 32.503 -25.980 -75.340 1.00 94.60 ? 152 VAL B CA 1 ATOM 3772 C C . VAL B 2 152 ? 32.341 -25.968 -73.822 1.00 94.56 ? 152 VAL B C 1 ATOM 3773 O O . VAL B 2 152 ? 33.080 -26.646 -73.113 1.00 95.23 ? 152 VAL B O 1 ATOM 3774 C CB . VAL B 2 152 ? 33.369 -24.782 -75.758 1.00 92.54 ? 152 VAL B CB 1 ATOM 3775 C CG1 . VAL B 2 152 ? 34.688 -24.787 -74.992 1.00 91.56 ? 152 VAL B CG1 1 ATOM 3776 C CG2 . VAL B 2 152 ? 33.621 -24.814 -77.257 1.00 93.03 ? 152 VAL B CG2 1 ATOM 3777 N N . ARG B 2 153 ? 31.380 -25.198 -73.327 1.00 95.71 ? 153 ARG B N 1 ATOM 3778 C CA . ARG B 2 153 ? 31.051 -25.228 -71.904 1.00 100.00 ? 153 ARG B CA 1 ATOM 3779 C C . ARG B 2 153 ? 30.343 -26.528 -71.517 1.00 104.90 ? 153 ARG B C 1 ATOM 3780 O O . ARG B 2 153 ? 30.484 -26.985 -70.389 1.00 104.94 ? 153 ARG B O 1 ATOM 3781 C CB . ARG B 2 153 ? 30.170 -24.046 -71.525 1.00 103.22 ? 153 ARG B CB 1 ATOM 3782 C CG . ARG B 2 153 ? 30.763 -22.696 -71.871 1.00 103.49 ? 153 ARG B CG 1 ATOM 3783 C CD . ARG B 2 153 ? 29.902 -21.571 -71.325 1.00 105.97 ? 153 ARG B CD 1 ATOM 3784 N NE . ARG B 2 153 ? 29.930 -20.409 -72.210 1.00 106.92 ? 153 ARG B NE 1 ATOM 3785 C CZ . ARG B 2 153 ? 28.968 -20.068 -73.065 1.00 107.53 ? 153 ARG B CZ 1 ATOM 3786 N NH1 . ARG B 2 153 ? 27.851 -20.781 -73.171 1.00 108.94 ? 153 ARG B NH1 1 ATOM 3787 N NH2 . ARG B 2 153 ? 29.124 -18.987 -73.820 1.00 109.36 ? 153 ARG B NH2 1 ATOM 3788 N N . ASN B 2 154 ? 29.567 -27.098 -72.443 1.00 111.25 ? 154 ASN B N 1 ATOM 3789 C CA . ASN B 2 154 ? 28.930 -28.412 -72.253 1.00 113.58 ? 154 ASN B CA 1 ATOM 3790 C C . ASN B 2 154 ? 29.928 -29.495 -71.905 1.00 113.53 ? 154 ASN B C 1 ATOM 3791 O O . ASN B 2 154 ? 29.693 -30.305 -71.013 1.00 115.87 ? 154 ASN B O 1 ATOM 3792 C CB . ASN B 2 154 ? 28.233 -28.874 -73.540 1.00 118.47 ? 154 ASN B CB 1 ATOM 3793 C CG . ASN B 2 154 ? 26.828 -28.341 -73.683 1.00 123.05 ? 154 ASN B CG 1 ATOM 3794 O OD1 . ASN B 2 154 ? 26.382 -27.501 -72.901 1.00 126.66 ? 154 ASN B OD1 1 ATOM 3795 N ND2 . ASN B 2 154 ? 26.117 -28.835 -74.698 1.00 125.04 ? 154 ASN B ND2 1 ATOM 3796 N N . GLY B 2 155 ? 31.038 -29.499 -72.636 1.00 112.51 ? 155 GLY B N 1 ATOM 3797 C CA . GLY B 2 155 ? 31.944 -30.635 -72.682 1.00 111.81 ? 155 GLY B CA 1 ATOM 3798 C C . GLY B 2 155 ? 31.687 -31.444 -73.939 1.00 114.47 ? 155 GLY B C 1 ATOM 3799 O O . GLY B 2 155 ? 32.425 -32.379 -74.235 1.00 118.03 ? 155 GLY B O 1 ATOM 3800 N N . THR B 2 156 ? 30.659 -31.060 -74.695 1.00 115.52 ? 156 THR B N 1 ATOM 3801 C CA . THR B 2 156 ? 30.194 -31.823 -75.845 1.00 117.75 ? 156 THR B CA 1 ATOM 3802 C C . THR B 2 156 ? 30.541 -31.086 -77.118 1.00 116.96 ? 156 THR B C 1 ATOM 3803 O O . THR B 2 156 ? 29.709 -30.941 -78.007 1.00 119.25 ? 156 THR B O 1 ATOM 3804 C CB . THR B 2 156 ? 28.667 -32.020 -75.799 1.00 123.34 ? 156 THR B CB 1 ATOM 3805 O OG1 . THR B 2 156 ? 28.257 -32.289 -74.454 1.00 124.22 ? 156 THR B OG1 1 ATOM 3806 C CG2 . THR B 2 156 ? 28.231 -33.183 -76.712 1.00 130.38 ? 156 THR B CG2 1 ATOM 3807 N N . TYR B 2 157 ? 31.776 -30.616 -77.205 1.00 117.30 ? 157 TYR B N 1 ATOM 3808 C CA . TYR B 2 157 ? 32.230 -29.907 -78.392 1.00 117.79 ? 157 TYR B CA 1 ATOM 3809 C C . TYR B 2 157 ? 32.724 -30.924 -79.412 1.00 124.79 ? 157 TYR B C 1 ATOM 3810 O O . TYR B 2 157 ? 33.754 -31.566 -79.204 1.00 123.63 ? 157 TYR B O 1 ATOM 3811 C CB . TYR B 2 157 ? 33.334 -28.924 -78.020 1.00 111.53 ? 157 TYR B CB 1 ATOM 3812 C CG . TYR B 2 157 ? 34.054 -28.312 -79.195 1.00 107.01 ? 157 TYR B CG 1 ATOM 3813 C CD1 . TYR B 2 157 ? 33.518 -27.231 -79.883 1.00 104.25 ? 157 TYR B CD1 1 ATOM 3814 C CD2 . TYR B 2 157 ? 35.288 -28.802 -79.603 1.00 106.43 ? 157 TYR B CD2 1 ATOM 3815 C CE1 . TYR B 2 157 ? 34.189 -26.661 -80.952 1.00 102.89 ? 157 TYR B CE1 1 ATOM 3816 C CE2 . TYR B 2 157 ? 35.964 -28.240 -80.671 1.00 105.78 ? 157 TYR B CE2 1 ATOM 3817 C CZ . TYR B 2 157 ? 35.413 -27.171 -81.343 1.00 102.71 ? 157 TYR B CZ 1 ATOM 3818 O OH . TYR B 2 157 ? 36.097 -26.621 -82.401 1.00 100.76 ? 157 TYR B OH 1 ATOM 3819 N N . ASP B 2 158 ? 31.981 -31.079 -80.504 1.00 136.43 ? 158 ASP B N 1 ATOM 3820 C CA . ASP B 2 158 ? 32.351 -32.034 -81.556 1.00 146.03 ? 158 ASP B CA 1 ATOM 3821 C C . ASP B 2 158 ? 33.568 -31.552 -82.341 1.00 149.12 ? 158 ASP B C 1 ATOM 3822 O O . ASP B 2 158 ? 33.450 -30.803 -83.313 1.00 144.52 ? 158 ASP B O 1 ATOM 3823 C CB . ASP B 2 158 ? 31.174 -32.334 -82.500 1.00 146.62 ? 158 ASP B CB 1 ATOM 3824 C CG . ASP B 2 158 ? 30.391 -33.564 -82.080 1.00 147.26 ? 158 ASP B CG 1 ATOM 3825 O OD1 . ASP B 2 158 ? 30.269 -33.824 -80.864 1.00 144.35 ? 158 ASP B OD1 1 ATOM 3826 O OD2 . ASP B 2 158 ? 29.908 -34.284 -82.974 1.00 152.91 ? 158 ASP B OD2 1 ATOM 3827 N N . TYR B 2 159 ? 34.737 -31.996 -81.884 1.00 154.88 ? 159 TYR B N 1 ATOM 3828 C CA . TYR B 2 159 ? 36.010 -31.705 -82.537 1.00 158.87 ? 159 TYR B CA 1 ATOM 3829 C C . TYR B 2 159 ? 36.024 -32.104 -84.028 1.00 167.91 ? 159 TYR B C 1 ATOM 3830 O O . TYR B 2 159 ? 36.388 -31.279 -84.873 1.00 166.27 ? 159 TYR B O 1 ATOM 3831 C CB . TYR B 2 159 ? 37.169 -32.364 -81.757 1.00 157.07 ? 159 TYR B CB 1 ATOM 3832 C CG . TYR B 2 159 ? 38.345 -32.796 -82.607 1.00 160.29 ? 159 TYR B CG 1 ATOM 3833 C CD1 . TYR B 2 159 ? 39.328 -31.888 -82.989 1.00 156.98 ? 159 TYR B CD1 1 ATOM 3834 C CD2 . TYR B 2 159 ? 38.470 -34.120 -83.036 1.00 163.71 ? 159 TYR B CD2 1 ATOM 3835 C CE1 . TYR B 2 159 ? 40.402 -32.286 -83.774 1.00 157.50 ? 159 TYR B CE1 1 ATOM 3836 C CE2 . TYR B 2 159 ? 39.540 -34.524 -83.819 1.00 163.70 ? 159 TYR B CE2 1 ATOM 3837 C CZ . TYR B 2 159 ? 40.505 -33.603 -84.184 1.00 160.69 ? 159 TYR B CZ 1 ATOM 3838 O OH . TYR B 2 159 ? 41.570 -34.001 -84.959 1.00 161.19 ? 159 TYR B OH 1 ATOM 3839 N N . PRO B 2 160 ? 35.615 -33.354 -84.357 1.00 176.98 ? 160 PRO B N 1 ATOM 3840 C CA . PRO B 2 160 ? 35.694 -33.824 -85.755 1.00 176.18 ? 160 PRO B CA 1 ATOM 3841 C C . PRO B 2 160 ? 34.856 -32.995 -86.732 1.00 170.51 ? 160 PRO B C 1 ATOM 3842 O O . PRO B 2 160 ? 35.303 -32.715 -87.847 1.00 165.67 ? 160 PRO B O 1 ATOM 3843 C CB . PRO B 2 160 ? 35.162 -35.266 -85.683 1.00 181.07 ? 160 PRO B CB 1 ATOM 3844 C CG . PRO B 2 160 ? 35.252 -35.655 -84.246 1.00 181.57 ? 160 PRO B CG 1 ATOM 3845 C CD . PRO B 2 160 ? 35.042 -34.389 -83.473 1.00 178.61 ? 160 PRO B CD 1 ATOM 3846 N N . GLN B 2 161 ? 33.651 -32.622 -86.303 1.00 167.21 ? 161 GLN B N 1 ATOM 3847 C CA . GLN B 2 161 ? 32.756 -31.752 -87.072 1.00 163.83 ? 161 GLN B CA 1 ATOM 3848 C C . GLN B 2 161 ? 33.471 -30.491 -87.562 1.00 154.80 ? 161 GLN B C 1 ATOM 3849 O O . GLN B 2 161 ? 33.330 -30.098 -88.721 1.00 151.00 ? 161 GLN B O 1 ATOM 3850 C CB . GLN B 2 161 ? 31.556 -31.359 -86.205 1.00 162.71 ? 161 GLN B CB 1 ATOM 3851 C CG . GLN B 2 161 ? 30.534 -30.462 -86.884 1.00 160.04 ? 161 GLN B CG 1 ATOM 3852 C CD . GLN B 2 161 ? 29.541 -29.886 -85.898 1.00 157.29 ? 161 GLN B CD 1 ATOM 3853 O OE1 . GLN B 2 161 ? 29.263 -30.486 -84.858 1.00 155.76 ? 161 GLN B OE1 1 ATOM 3854 N NE2 . GLN B 2 161 ? 29.003 -28.714 -86.215 1.00 154.37 ? 161 GLN B NE2 1 ATOM 3855 N N . TYR B 2 162 ? 34.221 -29.861 -86.662 1.00 146.19 ? 162 TYR B N 1 ATOM 3856 C CA . TYR B 2 162 ? 35.062 -28.726 -87.008 1.00 138.24 ? 162 TYR B CA 1 ATOM 3857 C C . TYR B 2 162 ? 36.480 -29.238 -87.261 1.00 132.70 ? 162 TYR B C 1 ATOM 3858 O O . TYR B 2 162 ? 37.226 -28.691 -88.070 1.00 123.22 ? 162 TYR B O 1 ATOM 3859 C CB . TYR B 2 162 ? 35.061 -27.694 -85.876 1.00 135.63 ? 162 TYR B CB 1 ATOM 3860 C CG . TYR B 2 162 ? 33.687 -27.277 -85.372 1.00 136.10 ? 162 TYR B CG 1 ATOM 3861 C CD1 . TYR B 2 162 ? 32.930 -26.314 -86.043 1.00 134.78 ? 162 TYR B CD1 1 ATOM 3862 C CD2 . TYR B 2 162 ? 33.160 -27.825 -84.203 1.00 135.86 ? 162 TYR B CD2 1 ATOM 3863 C CE1 . TYR B 2 162 ? 31.685 -25.926 -85.569 1.00 135.56 ? 162 TYR B CE1 1 ATOM 3864 C CE2 . TYR B 2 162 ? 31.919 -27.444 -83.722 1.00 136.00 ? 162 TYR B CE2 1 ATOM 3865 C CZ . TYR B 2 162 ? 31.185 -26.496 -84.405 1.00 137.54 ? 162 TYR B CZ 1 ATOM 3866 O OH . TYR B 2 162 ? 29.953 -26.123 -83.916 1.00 138.98 ? 162 TYR B OH 1 HETATM 3867 C C1 . NAG C 3 . ? 31.255 -3.353 -53.410 1.00 141.51 ? 1011 NAG A C1 1 HETATM 3868 C C2 . NAG C 3 . ? 30.573 -2.156 -52.727 1.00 148.16 ? 1011 NAG A C2 1 HETATM 3869 C C3 . NAG C 3 . ? 29.112 -2.416 -52.357 1.00 153.79 ? 1011 NAG A C3 1 HETATM 3870 C C4 . NAG C 3 . ? 28.350 -3.007 -53.533 1.00 158.07 ? 1011 NAG A C4 1 HETATM 3871 C C5 . NAG C 3 . ? 29.079 -4.254 -54.035 1.00 158.15 ? 1011 NAG A C5 1 HETATM 3872 C C6 . NAG C 3 . ? 28.387 -4.845 -55.266 1.00 158.79 ? 1011 NAG A C6 1 HETATM 3873 C C7 . NAG C 3 . ? 32.226 -0.742 -51.582 1.00 140.82 ? 1011 NAG A C7 1 HETATM 3874 C C8 . NAG C 3 . ? 32.919 -0.400 -50.294 1.00 138.23 ? 1011 NAG A C8 1 HETATM 3875 N N2 . NAG C 3 . ? 31.320 -1.727 -51.550 1.00 143.14 ? 1011 NAG A N2 1 HETATM 3876 O O3 . NAG C 3 . ? 28.486 -1.210 -51.984 1.00 158.64 ? 1011 NAG A O3 1 HETATM 3877 O O4 . NAG C 3 . ? 27.018 -3.291 -53.148 1.00 152.74 ? 1011 NAG A O4 1 HETATM 3878 O O5 . NAG C 3 . ? 30.412 -3.934 -54.395 1.00 149.62 ? 1011 NAG A O5 1 HETATM 3879 O O6 . NAG C 3 . ? 28.251 -6.240 -55.120 1.00 156.80 ? 1011 NAG A O6 1 HETATM 3880 O O7 . NAG C 3 . ? 32.514 -0.113 -52.600 1.00 139.20 ? 1011 NAG A O7 1 HETATM 3881 C C1 . NAG D 3 . ? 49.712 -6.096 -42.872 1.00 111.43 ? 1023 NAG A C1 1 HETATM 3882 C C2 . NAG D 3 . ? 51.038 -5.465 -42.455 1.00 116.99 ? 1023 NAG A C2 1 HETATM 3883 C C3 . NAG D 3 . ? 50.941 -4.767 -41.099 1.00 124.09 ? 1023 NAG A C3 1 HETATM 3884 C C4 . NAG D 3 . ? 49.630 -4.016 -40.885 1.00 127.47 ? 1023 NAG A C4 1 HETATM 3885 C C5 . NAG D 3 . ? 48.455 -4.906 -41.278 1.00 121.39 ? 1023 NAG A C5 1 HETATM 3886 C C6 . NAG D 3 . ? 47.071 -4.300 -41.022 1.00 116.80 ? 1023 NAG A C6 1 HETATM 3887 C C7 . NAG D 3 . ? 52.983 -6.736 -43.299 1.00 118.63 ? 1023 NAG A C7 1 HETATM 3888 C C8 . NAG D 3 . ? 53.958 -7.848 -43.030 1.00 117.21 ? 1023 NAG A C8 1 HETATM 3889 N N2 . NAG D 3 . ? 52.057 -6.500 -42.361 1.00 117.02 ? 1023 NAG A N2 1 HETATM 3890 O O3 . NAG D 3 . ? 52.026 -3.880 -40.935 1.00 129.04 ? 1023 NAG A O3 1 HETATM 3891 O O4 . NAG D 3 . ? 49.583 -3.669 -39.519 1.00 141.77 ? 1023 NAG A O4 1 HETATM 3892 O O5 . NAG D 3 . ? 48.627 -5.210 -42.648 1.00 114.79 ? 1023 NAG A O5 1 HETATM 3893 O O6 . NAG D 3 . ? 46.820 -3.238 -41.914 1.00 115.43 ? 1023 NAG A O6 1 HETATM 3894 O O7 . NAG D 3 . ? 53.076 -6.105 -44.351 1.00 118.43 ? 1023 NAG A O7 1 HETATM 3895 C C1 . NAG E 3 . ? 49.218 -2.289 -39.319 1.00 153.45 ? 1024 NAG A C1 1 HETATM 3896 C C2 . NAG E 3 . ? 49.060 -2.048 -37.817 1.00 153.27 ? 1024 NAG A C2 1 HETATM 3897 C C3 . NAG E 3 . ? 48.878 -0.564 -37.477 1.00 156.54 ? 1024 NAG A C3 1 HETATM 3898 C C4 . NAG E 3 . ? 49.750 0.361 -38.329 1.00 158.76 ? 1024 NAG A C4 1 HETATM 3899 C C5 . NAG E 3 . ? 49.695 -0.052 -39.796 1.00 154.76 ? 1024 NAG A C5 1 HETATM 3900 C C6 . NAG E 3 . ? 50.553 0.831 -40.696 1.00 154.26 ? 1024 NAG A C6 1 HETATM 3901 C C7 . NAG E 3 . ? 48.068 -4.097 -36.875 1.00 145.25 ? 1024 NAG A C7 1 HETATM 3902 C C8 . NAG E 3 . ? 46.827 -4.785 -36.379 1.00 139.95 ? 1024 NAG A C8 1 HETATM 3903 N N2 . NAG E 3 . ? 47.940 -2.835 -37.309 1.00 150.58 ? 1024 NAG A N2 1 HETATM 3904 O O3 . NAG E 3 . ? 49.181 -0.351 -36.116 1.00 157.30 ? 1024 NAG A O3 1 HETATM 3905 O O4 . NAG E 3 . ? 49.311 1.694 -38.174 1.00 160.66 ? 1024 NAG A O4 1 HETATM 3906 O O5 . NAG E 3 . ? 50.156 -1.384 -39.865 1.00 154.07 ? 1024 NAG A O5 1 HETATM 3907 O O6 . NAG E 3 . ? 51.915 0.528 -40.507 1.00 152.45 ? 1024 NAG A O6 1 HETATM 3908 O O7 . NAG E 3 . ? 49.136 -4.710 -36.864 1.00 142.41 ? 1024 NAG A O7 1 HETATM 3909 C C1 . NAG F 3 . ? 21.668 -39.448 13.982 1.00 143.38 ? 1165 NAG A C1 1 HETATM 3910 C C2 . NAG F 3 . ? 22.520 -40.682 14.260 1.00 145.24 ? 1165 NAG A C2 1 HETATM 3911 C C3 . NAG F 3 . ? 22.033 -41.849 13.422 1.00 150.63 ? 1165 NAG A C3 1 HETATM 3912 C C4 . NAG F 3 . ? 20.543 -42.069 13.651 1.00 156.23 ? 1165 NAG A C4 1 HETATM 3913 C C5 . NAG F 3 . ? 19.750 -40.778 13.454 1.00 152.13 ? 1165 NAG A C5 1 HETATM 3914 C C6 . NAG F 3 . ? 18.258 -40.935 13.773 1.00 152.63 ? 1165 NAG A C6 1 HETATM 3915 C C7 . NAG F 3 . ? 24.867 -40.647 14.963 1.00 138.27 ? 1165 NAG A C7 1 HETATM 3916 C C8 . NAG F 3 . ? 26.300 -40.405 14.600 1.00 135.54 ? 1165 NAG A C8 1 HETATM 3917 N N2 . NAG F 3 . ? 23.939 -40.462 14.016 1.00 139.27 ? 1165 NAG A N2 1 HETATM 3918 O O3 . NAG F 3 . ? 22.735 -43.014 13.781 1.00 152.89 ? 1165 NAG A O3 1 HETATM 3919 O O4 . NAG F 3 . ? 20.112 -43.043 12.731 1.00 165.79 ? 1165 NAG A O4 1 HETATM 3920 O O5 . NAG F 3 . ? 20.312 -39.758 14.253 1.00 148.58 ? 1165 NAG A O5 1 HETATM 3921 O O6 . NAG F 3 . ? 18.027 -41.299 15.118 1.00 148.91 ? 1165 NAG A O6 1 HETATM 3922 O O7 . NAG F 3 . ? 24.610 -40.997 16.114 1.00 141.74 ? 1165 NAG A O7 1 HETATM 3923 C C1 . NAG G 3 . ? 19.505 -44.172 13.387 1.00 175.55 ? 1166 NAG A C1 1 HETATM 3924 C C2 . NAG G 3 . ? 19.047 -45.114 12.271 1.00 177.88 ? 1166 NAG A C2 1 HETATM 3925 C C3 . NAG G 3 . ? 18.651 -46.500 12.765 1.00 184.61 ? 1166 NAG A C3 1 HETATM 3926 C C4 . NAG G 3 . ? 19.642 -47.024 13.806 1.00 188.29 ? 1166 NAG A C4 1 HETATM 3927 C C5 . NAG G 3 . ? 19.835 -45.972 14.900 1.00 183.69 ? 1166 NAG A C5 1 HETATM 3928 C C6 . NAG G 3 . ? 20.769 -46.457 16.003 1.00 182.56 ? 1166 NAG A C6 1 HETATM 3929 C C7 . NAG G 3 . ? 18.034 -43.842 10.421 1.00 172.21 ? 1166 NAG A C7 1 HETATM 3930 C C8 . NAG G 3 . ? 16.763 -43.291 9.834 1.00 172.11 ? 1166 NAG A C8 1 HETATM 3931 N N2 . NAG G 3 . ? 17.919 -44.518 11.568 1.00 176.57 ? 1166 NAG A N2 1 HETATM 3932 O O3 . NAG G 3 . ? 18.625 -47.362 11.651 1.00 185.84 ? 1166 NAG A O3 1 HETATM 3933 O O4 . NAG G 3 . ? 19.344 -48.328 14.312 1.00 202.29 ? 1166 NAG A O4 1 HETATM 3934 O O5 . NAG G 3 . ? 20.379 -44.814 14.300 1.00 178.16 ? 1166 NAG A O5 1 HETATM 3935 O O6 . NAG G 3 . ? 20.904 -45.446 16.971 1.00 178.84 ? 1166 NAG A O6 1 HETATM 3936 O O7 . NAG G 3 . ? 19.104 -43.655 9.840 1.00 164.66 ? 1166 NAG A O7 1 HETATM 3937 C C1 . MAN H 4 . ? 17.999 -48.576 14.794 1.00 209.65 ? 1167 MAN A C1 1 HETATM 3938 C C2 . MAN H 4 . ? 18.011 -49.821 15.693 1.00 213.68 ? 1167 MAN A C2 1 HETATM 3939 C C3 . MAN H 4 . ? 18.162 -51.102 14.861 1.00 218.11 ? 1167 MAN A C3 1 HETATM 3940 C C4 . MAN H 4 . ? 17.107 -51.141 13.751 1.00 218.27 ? 1167 MAN A C4 1 HETATM 3941 C C5 . MAN H 4 . ? 17.289 -49.888 12.907 1.00 213.69 ? 1167 MAN A C5 1 HETATM 3942 C C6 . MAN H 4 . ? 16.366 -49.824 11.697 1.00 213.41 ? 1167 MAN A C6 1 HETATM 3943 O O2 . MAN H 4 . ? 16.813 -49.872 16.480 1.00 211.77 ? 1167 MAN A O2 1 HETATM 3944 O O3 . MAN H 4 . ? 18.095 -52.277 15.696 1.00 223.64 ? 1167 MAN A O3 1 HETATM 3945 O O4 . MAN H 4 . ? 17.222 -52.305 12.921 1.00 218.18 ? 1167 MAN A O4 1 HETATM 3946 O O5 . MAN H 4 . ? 17.039 -48.757 13.746 1.00 213.32 ? 1167 MAN A O5 1 HETATM 3947 O O6 . MAN H 4 . ? 16.498 -50.992 10.874 1.00 214.75 ? 1167 MAN A O6 1 HETATM 3948 C C1 . BMA I 5 . ? 18.829 -53.374 15.096 1.00 222.79 ? 1168 BMA A C1 1 HETATM 3949 C C2 . BMA I 5 . ? 20.012 -53.783 15.966 1.00 221.02 ? 1168 BMA A C2 1 HETATM 3950 C C3 . BMA I 5 . ? 20.821 -54.840 15.217 1.00 219.32 ? 1168 BMA A C3 1 HETATM 3951 C C4 . BMA I 5 . ? 19.911 -55.985 14.785 1.00 221.77 ? 1168 BMA A C4 1 HETATM 3952 C C5 . BMA I 5 . ? 18.657 -55.488 14.064 1.00 221.72 ? 1168 BMA A C5 1 HETATM 3953 C C6 . BMA I 5 . ? 17.679 -56.626 13.781 1.00 222.27 ? 1168 BMA A C6 1 HETATM 3954 O O2 . BMA I 5 . ? 19.554 -54.292 17.200 1.00 218.20 ? 1168 BMA A O2 1 HETATM 3955 O O3 . BMA I 5 . ? 21.844 -55.348 16.043 1.00 220.55 ? 1168 BMA A O3 1 HETATM 3956 O O4 . BMA I 5 . ? 20.615 -56.902 13.972 1.00 216.46 ? 1168 BMA A O4 1 HETATM 3957 O O5 . BMA I 5 . ? 18.018 -54.509 14.865 1.00 226.73 ? 1168 BMA A O5 1 HETATM 3958 O O6 . BMA I 5 . ? 17.109 -57.077 14.989 1.00 221.94 ? 1168 BMA A O6 1 HETATM 3959 C C1 . MAN J 4 . ? 15.754 -50.921 9.629 1.00 214.38 ? 1169 MAN A C1 1 HETATM 3960 C C2 . MAN J 4 . ? 16.695 -50.505 8.483 1.00 208.94 ? 1169 MAN A C2 1 HETATM 3961 C C3 . MAN J 4 . ? 16.665 -49.017 8.138 1.00 202.89 ? 1169 MAN A C3 1 HETATM 3962 C C4 . MAN J 4 . ? 15.246 -48.468 8.118 1.00 206.02 ? 1169 MAN A C4 1 HETATM 3963 C C5 . MAN J 4 . ? 14.529 -48.783 9.426 1.00 211.60 ? 1169 MAN A C5 1 HETATM 3964 C C6 . MAN J 4 . ? 13.065 -48.355 9.392 1.00 212.35 ? 1169 MAN A C6 1 HETATM 3965 O O2 . MAN J 4 . ? 16.397 -51.257 7.323 1.00 206.85 ? 1169 MAN A O2 1 HETATM 3966 O O3 . MAN J 4 . ? 17.251 -48.816 6.871 1.00 195.93 ? 1169 MAN A O3 1 HETATM 3967 O O4 . MAN J 4 . ? 15.322 -47.072 7.939 1.00 200.14 ? 1169 MAN A O4 1 HETATM 3968 O O5 . MAN J 4 . ? 14.538 -50.178 9.692 1.00 215.92 ? 1169 MAN A O5 1 HETATM 3969 O O6 . MAN J 4 . ? 12.628 -48.092 10.709 1.00 210.97 ? 1169 MAN A O6 1 HETATM 3970 C C1 . NAG K 3 . ? 23.107 -11.758 -30.162 1.00 149.85 ? 1286 NAG A C1 1 HETATM 3971 C C2 . NAG K 3 . ? 21.589 -11.808 -29.933 1.00 155.93 ? 1286 NAG A C2 1 HETATM 3972 C C3 . NAG K 3 . ? 20.867 -12.010 -31.268 1.00 160.24 ? 1286 NAG A C3 1 HETATM 3973 C C4 . NAG K 3 . ? 21.312 -10.978 -32.304 1.00 163.60 ? 1286 NAG A C4 1 HETATM 3974 C C5 . NAG K 3 . ? 22.836 -10.939 -32.387 1.00 160.16 ? 1286 NAG A C5 1 HETATM 3975 C C6 . NAG K 3 . ? 23.329 -9.836 -33.322 1.00 157.31 ? 1286 NAG A C6 1 HETATM 3976 C C7 . NAG K 3 . ? 21.125 -12.675 -27.672 1.00 149.25 ? 1286 NAG A C7 1 HETATM 3977 C C8 . NAG K 3 . ? 20.669 -13.838 -26.836 1.00 144.83 ? 1286 NAG A C8 1 HETATM 3978 N N2 . NAG K 3 . ? 21.175 -12.849 -28.997 1.00 154.34 ? 1286 NAG A N2 1 HETATM 3979 O O3 . NAG K 3 . ? 19.469 -11.943 -31.086 1.00 163.39 ? 1286 NAG A O3 1 HETATM 3980 O O4 . NAG K 3 . ? 20.761 -11.282 -33.568 1.00 166.29 ? 1286 NAG A O4 1 HETATM 3981 O O5 . NAG K 3 . ? 23.354 -10.713 -31.091 1.00 156.32 ? 1286 NAG A O5 1 HETATM 3982 O O6 . NAG K 3 . ? 23.988 -10.404 -34.431 1.00 152.12 ? 1286 NAG A O6 1 HETATM 3983 O O7 . NAG K 3 . ? 21.438 -11.623 -27.116 1.00 147.94 ? 1286 NAG A O7 1 HETATM 3984 S S1 . MPO L 6 . ? 35.374 -4.393 22.056 1.00 160.23 ? 1322 MPO A S1 1 HETATM 3985 O O1 . MPO L 6 . ? 34.077 -3.947 22.498 1.00 153.03 ? 1322 MPO A O1 1 HETATM 3986 O O2 . MPO L 6 . ? 36.392 -3.565 22.638 1.00 164.94 ? 1322 MPO A O2 1 HETATM 3987 O O4 . MPO L 6 . ? 32.234 -9.621 26.141 1.00 144.59 ? 1322 MPO A O4 1 HETATM 3988 N N1 . MPO L 6 . ? 33.925 -7.498 25.305 1.00 146.01 ? 1322 MPO A N1 1 HETATM 3989 C C1 . MPO L 6 . ? 35.644 -5.989 22.476 1.00 155.04 ? 1322 MPO A C1 1 HETATM 3990 O O3 . MPO L 6 . ? 35.463 -4.242 20.432 1.00 160.19 ? 1322 MPO A O3 1 HETATM 3991 C C2 . MPO L 6 . ? 35.586 -6.220 23.987 1.00 149.63 ? 1322 MPO A C2 1 HETATM 3992 C C3 . MPO L 6 . ? 34.150 -6.277 24.510 1.00 147.01 ? 1322 MPO A C3 1 HETATM 3993 C C4 . MPO L 6 . ? 33.611 -8.632 24.419 1.00 142.80 ? 1322 MPO A C4 1 HETATM 3994 C C5 . MPO L 6 . ? 33.318 -9.877 25.249 1.00 143.58 ? 1322 MPO A C5 1 HETATM 3995 C C6 . MPO L 6 . ? 32.518 -8.551 27.041 1.00 145.74 ? 1322 MPO A C6 1 HETATM 3996 C C7 . MPO L 6 . ? 32.813 -7.280 26.248 1.00 149.01 ? 1322 MPO A C7 1 HETATM 3997 C C1 . NAG M 3 . ? 24.756 -28.459 -74.987 1.00 129.70 ? 1154 NAG B C1 1 HETATM 3998 C C2 . NAG M 3 . ? 23.739 -29.609 -75.113 1.00 135.28 ? 1154 NAG B C2 1 HETATM 3999 C C3 . NAG M 3 . ? 23.312 -29.949 -76.541 1.00 137.98 ? 1154 NAG B C3 1 HETATM 4000 C C4 . NAG M 3 . ? 23.282 -28.720 -77.436 1.00 138.71 ? 1154 NAG B C4 1 HETATM 4001 C C5 . NAG M 3 . ? 24.612 -27.994 -77.324 1.00 132.17 ? 1154 NAG B C5 1 HETATM 4002 C C6 . NAG M 3 . ? 24.717 -26.828 -78.302 1.00 130.89 ? 1154 NAG B C6 1 HETATM 4003 C C7 . NAG M 3 . ? 24.413 -30.894 -73.137 1.00 135.03 ? 1154 NAG B C7 1 HETATM 4004 C C8 . NAG M 3 . ? 24.914 -32.195 -72.576 1.00 136.14 ? 1154 NAG B C8 1 HETATM 4005 N N2 . NAG M 3 . ? 24.224 -30.821 -74.459 1.00 135.29 ? 1154 NAG B N2 1 HETATM 4006 O O3 . NAG M 3 . ? 22.029 -30.533 -76.501 1.00 142.59 ? 1154 NAG B O3 1 HETATM 4007 O O4 . NAG M 3 . ? 22.972 -29.080 -78.773 1.00 143.37 ? 1154 NAG B O4 1 HETATM 4008 O O5 . NAG M 3 . ? 24.681 -27.489 -76.012 1.00 128.65 ? 1154 NAG B O5 1 HETATM 4009 O O6 . NAG M 3 . ? 23.922 -25.753 -77.848 1.00 130.09 ? 1154 NAG B O6 1 HETATM 4010 O O7 . NAG M 3 . ? 24.201 -29.953 -72.373 1.00 130.97 ? 1154 NAG B O7 1 HETATM 4011 C C1 . NAG N 3 . ? 21.684 -28.555 -79.157 1.00 145.17 ? 1155 NAG B C1 1 HETATM 4012 C C2 . NAG N 3 . ? 21.329 -29.017 -80.574 1.00 147.89 ? 1155 NAG B C2 1 HETATM 4013 C C3 . NAG N 3 . ? 19.873 -28.673 -80.924 1.00 153.25 ? 1155 NAG B C3 1 HETATM 4014 C C4 . NAG N 3 . ? 18.912 -29.092 -79.807 1.00 156.24 ? 1155 NAG B C4 1 HETATM 4015 C C5 . NAG N 3 . ? 19.400 -28.457 -78.505 1.00 153.86 ? 1155 NAG B C5 1 HETATM 4016 C C6 . NAG N 3 . ? 18.487 -28.706 -77.302 1.00 156.71 ? 1155 NAG B C6 1 HETATM 4017 C C7 . NAG N 3 . ? 23.520 -28.654 -81.697 1.00 140.85 ? 1155 NAG B C7 1 HETATM 4018 C C8 . NAG N 3 . ? 24.230 -28.011 -82.857 1.00 137.77 ? 1155 NAG B C8 1 HETATM 4019 N N2 . NAG N 3 . ? 22.196 -28.466 -81.616 1.00 145.06 ? 1155 NAG B N2 1 HETATM 4020 O O3 . NAG N 3 . ? 19.539 -29.283 -82.154 1.00 156.99 ? 1155 NAG B O3 1 HETATM 4021 O O4 . NAG N 3 . ? 17.571 -28.703 -80.059 1.00 158.46 ? 1155 NAG B O4 1 HETATM 4022 O O5 . NAG N 3 . ? 20.688 -28.966 -78.236 1.00 148.56 ? 1155 NAG B O5 1 HETATM 4023 O O6 . NAG N 3 . ? 17.700 -29.862 -77.483 1.00 161.99 ? 1155 NAG B O6 1 HETATM 4024 O O7 . NAG N 3 . ? 24.172 -29.308 -80.884 1.00 137.83 ? 1155 NAG B O7 1 HETATM 4025 C C1 . BMA O 5 . ? 16.888 -29.580 -80.985 1.00 164.66 ? 1156 BMA B C1 1 HETATM 4026 C C2 . BMA O 5 . ? 15.424 -29.705 -80.569 1.00 170.27 ? 1156 BMA B C2 1 HETATM 4027 C C3 . BMA O 5 . ? 14.618 -30.526 -81.578 1.00 175.06 ? 1156 BMA B C3 1 HETATM 4028 C C4 . BMA O 5 . ? 14.901 -30.107 -83.017 1.00 172.87 ? 1156 BMA B C4 1 HETATM 4029 C C5 . BMA O 5 . ? 16.399 -30.011 -83.289 1.00 166.83 ? 1156 BMA B C5 1 HETATM 4030 C C6 . BMA O 5 . ? 16.681 -29.558 -84.726 1.00 166.02 ? 1156 BMA B C6 1 HETATM 4031 O O2 . BMA O 5 . ? 14.850 -28.399 -80.440 1.00 171.62 ? 1156 BMA B O2 1 HETATM 4032 O O3 . BMA O 5 . ? 13.215 -30.382 -81.324 1.00 179.76 ? 1156 BMA B O3 1 HETATM 4033 O O4 . BMA O 5 . ? 14.306 -31.061 -83.901 1.00 177.87 ? 1156 BMA B O4 1 HETATM 4034 O O5 . BMA O 5 . ? 16.974 -29.113 -82.337 1.00 163.00 ? 1156 BMA B O5 1 HETATM 4035 O O6 . BMA O 5 . ? 17.497 -28.380 -84.764 1.00 159.28 ? 1156 BMA B O6 1 HETATM 4036 S S1 . MPO P 6 . ? 38.179 -10.491 -70.753 1.00 147.23 ? 1163 MPO B S1 1 HETATM 4037 O O1 . MPO P 6 . ? 38.940 -10.000 -69.636 1.00 155.06 ? 1163 MPO B O1 1 HETATM 4038 O O2 . MPO P 6 . ? 37.298 -9.448 -71.214 1.00 141.50 ? 1163 MPO B O2 1 HETATM 4039 O O4 . MPO P 6 . ? 43.848 -9.296 -71.882 1.00 124.66 ? 1163 MPO B O4 1 HETATM 4040 N N1 . MPO P 6 . ? 42.091 -10.992 -71.127 1.00 123.76 ? 1163 MPO B N1 1 HETATM 4041 C C1 . MPO P 6 . ? 39.219 -10.928 -71.971 1.00 132.84 ? 1163 MPO B C1 1 HETATM 4042 O O3 . MPO P 6 . ? 37.297 -11.786 -70.288 1.00 145.96 ? 1163 MPO B O3 1 HETATM 4043 C C2 . MPO P 6 . ? 39.988 -12.205 -71.641 1.00 120.82 ? 1163 MPO B C2 1 HETATM 4044 C C3 . MPO P 6 . ? 41.133 -12.009 -70.649 1.00 123.32 ? 1163 MPO B C3 1 HETATM 4045 C C4 . MPO P 6 . ? 43.137 -11.609 -71.963 1.00 118.71 ? 1163 MPO B C4 1 HETATM 4046 C C5 . MPO P 6 . ? 44.105 -10.555 -72.499 1.00 117.49 ? 1163 MPO B C5 1 HETATM 4047 C C6 . MPO P 6 . ? 43.831 -9.375 -70.453 1.00 129.19 ? 1163 MPO B C6 1 HETATM 4048 C C7 . MPO P 6 . ? 42.702 -10.291 -69.981 1.00 129.43 ? 1163 MPO B C7 1 HETATM 4049 O O . HOH Q 7 . ? 40.057 -14.028 -65.018 1.00 75.81 ? 2001 HOH A O 1 HETATM 4050 O O . HOH Q 7 . ? 40.358 -12.082 -58.472 1.00 68.68 ? 2002 HOH A O 1 HETATM 4051 O O . HOH Q 7 . ? 51.374 -18.115 -50.088 1.00 78.41 ? 2003 HOH A O 1 HETATM 4052 O O . HOH Q 7 . ? 50.631 -21.050 -45.031 1.00 74.73 ? 2004 HOH A O 1 HETATM 4053 O O . HOH Q 7 . ? 40.043 -12.034 -36.512 1.00 72.54 ? 2005 HOH A O 1 HETATM 4054 O O . HOH Q 7 . ? 30.227 -11.359 -28.062 1.00 74.53 ? 2006 HOH A O 1 HETATM 4055 O O . HOH Q 7 . ? 31.393 -8.375 -6.382 1.00 84.03 ? 2007 HOH A O 1 HETATM 4056 O O . HOH Q 7 . ? 18.356 -16.726 9.380 1.00 76.88 ? 2008 HOH A O 1 HETATM 4057 O O . HOH Q 7 . ? 27.702 -13.604 24.774 1.00 95.58 ? 2009 HOH A O 1 HETATM 4058 O O . HOH Q 7 . ? 41.472 -21.260 -45.658 1.00 64.32 ? 2010 HOH A O 1 HETATM 4059 O O . HOH Q 7 . ? 43.856 -18.155 -55.005 1.00 62.57 ? 2011 HOH A O 1 HETATM 4060 O O . HOH Q 7 . ? 46.517 -17.773 -55.692 1.00 72.87 ? 2012 HOH A O 1 HETATM 4061 O O . HOH R 7 . ? 49.387 -19.205 -60.123 1.00 65.26 ? 2001 HOH B O 1 HETATM 4062 O O . HOH R 7 . ? 52.455 -25.861 -61.820 1.00 76.94 ? 2002 HOH B O 1 HETATM 4063 O O . HOH R 7 . ? 30.718 -17.186 -55.798 1.00 69.92 ? 2003 HOH B O 1 HETATM 4064 O O . HOH R 7 . ? 36.620 -33.701 -42.368 1.00 73.23 ? 2004 HOH B O 1 HETATM 4065 O O . HOH R 7 . ? 47.448 -19.799 -10.281 1.00 73.08 ? 2005 HOH B O 1 HETATM 4066 O O . HOH R 7 . ? 51.641 -19.595 -28.730 1.00 74.98 ? 2006 HOH B O 1 HETATM 4067 O O . HOH R 7 . ? 47.333 -26.736 -35.670 1.00 63.67 ? 2007 HOH B O 1 HETATM 4068 O O . HOH R 7 . ? 46.901 -17.028 -38.378 1.00 74.57 ? 2008 HOH B O 1 HETATM 4069 O O . HOH R 7 . ? 49.324 -31.795 -51.925 1.00 69.56 ? 2009 HOH B O 1 HETATM 4070 O O . HOH R 7 . ? 41.669 -28.764 -57.417 1.00 68.42 ? 2010 HOH B O 1 HETATM 4071 O O . HOH R 7 . ? 45.681 -19.475 -73.437 1.00 76.37 ? 2011 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 ? 1.6174 1.2229 0.9178 0.4627 -0.0238 0.0064 1 ASP A N 2 C CA . ASP A 1 ? 1.5436 1.2057 0.8836 0.4500 -0.0356 -0.0080 1 ASP A CA 3 C C . ASP A 1 ? 1.4763 1.1468 0.8524 0.4178 -0.0252 -0.0030 1 ASP A C 4 O O . ASP A 1 ? 1.4234 1.0820 0.8012 0.4046 -0.0173 0.0031 1 ASP A O 5 C CB . ASP A 1 ? 1.5547 1.2526 0.8958 0.4561 -0.0502 -0.0224 1 ASP A CB 6 C CG . ASP A 1 ? 1.6479 1.3431 0.9538 0.4902 -0.0625 -0.0292 1 ASP A CG 7 O OD1 . ASP A 1 ? 1.6961 1.3574 0.9733 0.5105 -0.0595 -0.0221 1 ASP A OD1 8 O OD2 . ASP A 1 ? 1.7358 1.4623 1.0410 0.4972 -0.0753 -0.0423 1 ASP A OD2 9 N N . GLN A 2 ? 1.4526 1.1429 0.8558 0.4066 -0.0253 -0.0055 2 GLN A N 10 C CA . GLN A 2 ? 1.4029 1.1000 0.8386 0.3780 -0.0157 -0.0006 2 GLN A CA 11 C C . GLN A 2 ? 1.3157 1.0562 0.7863 0.3654 -0.0231 -0.0111 2 GLN A C 12 O O . GLN A 2 ? 1.3110 1.0715 0.7811 0.3792 -0.0333 -0.0201 2 GLN A O 13 C CB . GLN A 2 ? 1.4722 1.1276 0.8996 0.3733 0.0007 0.0147 2 GLN A CB 14 C CG . GLN A 2 ? 1.5225 1.1731 0.9508 0.3794 0.0012 0.0153 2 GLN A CG 15 C CD . GLN A 2 ? 1.5748 1.1848 0.9955 0.3714 0.0185 0.0295 2 GLN A CD 16 O OE1 . GLN A 2 ? 1.5512 1.1666 0.9927 0.3586 0.0232 0.0311 2 GLN A OE1 17 N NE2 . GLN A 2 ? 1.6298 1.1994 1.0201 0.3781 0.0284 0.0393 2 GLN A NE2 18 N N . ILE A 3 ? 1.2496 1.0034 0.7489 0.3398 -0.0176 -0.0098 3 ILE A N 19 C CA . ILE A 3 ? 1.2030 0.9941 0.7354 0.3244 -0.0222 -0.0183 3 ILE A CA 20 C C . ILE A 3 ? 1.1844 0.9626 0.7363 0.3044 -0.0094 -0.0080 3 ILE A C 21 O O . ILE A 3 ? 1.1952 0.9512 0.7447 0.2947 0.0009 0.0015 3 ILE A O 22 C CB . ILE A 3 ? 1.1891 1.0183 0.7375 0.3124 -0.0313 -0.0315 3 ILE A CB 23 C CG1 . ILE A 3 ? 1.2134 1.0822 0.7927 0.2984 -0.0367 -0.0418 3 ILE A CG1 24 C CG2 . ILE A 3 ? 1.1786 0.9940 0.7299 0.2950 -0.0230 -0.0252 3 ILE A CG2 25 C CD1 . ILE A 3 ? 1.2287 1.1362 0.8220 0.2858 -0.0453 -0.0566 3 ILE A CD1 26 N N . CYS A 4 ? 1.2221 1.0163 0.7932 0.2992 -0.0105 -0.0107 4 CYS A N 27 C CA . CYS A 4 ? 1.2513 1.0343 0.8397 0.2829 0.0007 -0.0017 4 CYS A CA 28 C C . CYS A 4 ? 1.1889 1.0083 0.8096 0.2651 -0.0034 -0.0097 4 CYS A C 29 O O . CYS A 4 ? 1.2131 1.0639 0.8419 0.2693 -0.0143 -0.0217 4 CYS A O 30 C CB . CYS A 4 ? 1.3321 1.0910 0.9083 0.2946 0.0056 0.0046 4 CYS A CB 31 S SG . CYS A 4 ? 1.5937 1.3033 1.1259 0.3167 0.0119 0.0143 4 CYS A SG 32 N N . ILE A 5 ? 1.1315 0.9469 0.7698 0.2458 0.0056 -0.0033 5 ILE A N 33 C CA . ILE A 5 ? 1.0428 0.8860 0.7095 0.2285 0.0038 -0.0087 5 ILE A CA 34 C C . ILE A 5 ? 1.0081 0.8433 0.6832 0.2280 0.0093 -0.0035 5 ILE A C 35 O O . ILE A 5 ? 1.0056 0.8104 0.6694 0.2320 0.0186 0.0068 5 ILE A O 36 C CB . ILE A 5 ? 1.0591 0.9011 0.7371 0.2093 0.0100 -0.0051 5 ILE A CB 37 C CG1 . ILE A 5 ? 1.1017 0.9444 0.7665 0.2104 0.0060 -0.0092 5 ILE A CG1 38 C CG2 . ILE A 5 ? 1.0398 0.9087 0.7436 0.1918 0.0080 -0.0110 5 ILE A CG2 39 C CD1 . ILE A 5 ? 1.1249 1.0000 0.7916 0.2128 -0.0066 -0.0242 5 ILE A CD1 40 N N . GLY A 6 ? 0.9752 0.8382 0.6698 0.2223 0.0038 -0.0112 6 GLY A N 41 C CA . GLY A 6 ? 0.9592 0.8174 0.6620 0.2222 0.0076 -0.0079 6 GLY A CA 42 C C . GLY A 6 ? 0.9273 0.8196 0.6554 0.2109 0.0023 -0.0167 6 GLY A C 43 O O . GLY A 6 ? 0.9367 0.8558 0.6762 0.2012 -0.0033 -0.0252 6 GLY A O 44 N N . TYR A 7 ? 0.9114 0.8015 0.6470 0.2115 0.0047 -0.0149 7 TYR A N 45 C CA . TYR A 7 ? 0.9128 0.8316 0.6727 0.1994 0.0018 -0.0215 7 TYR A CA 46 C C . TYR A 7 ? 0.9180 0.8394 0.6765 0.2114 -0.0014 -0.0246 7 TYR A C 47 O O . TYR A 7 ? 0.9530 0.8478 0.6912 0.2268 0.0009 -0.0196 7 TYR A O 48 C CB . TYR A 7 ? 0.9388 0.8509 0.7151 0.1802 0.0110 -0.0140 7 TYR A CB 49 C CG . TYR A 7 ? 0.9529 0.8324 0.7221 0.1815 0.0218 -0.0023 7 TYR A CG 50 C CD1 . TYR A 7 ? 0.9427 0.7960 0.6980 0.1827 0.0292 0.0064 7 TYR A CD1 51 C CD2 . TYR A 7 ? 0.9736 0.8496 0.7501 0.1808 0.0249 -0.0008 7 TYR A CD2 52 C CE1 . TYR A 7 ? 1.0000 0.8262 0.7494 0.1822 0.0399 0.0158 7 TYR A CE1 53 C CE2 . TYR A 7 ? 0.9892 0.8368 0.7592 0.1799 0.0353 0.0085 7 TYR A CE2 54 C CZ . TYR A 7 ? 1.0067 0.8304 0.7637 0.1800 0.0430 0.0165 7 TYR A CZ 55 O OH . TYR A 7 ? 1.0422 0.8402 0.7934 0.1773 0.0543 0.0245 7 TYR A OH 56 N N . HIS A 8 ? 0.9181 0.8702 0.6967 0.2039 -0.0062 -0.0329 8 HIS A N 57 C CA . HIS A 8 ? 0.9806 0.9429 0.7604 0.2150 -0.0110 -0.0385 8 HIS A CA 58 C C . HIS A 8 ? 1.0461 0.9784 0.8217 0.2160 -0.0024 -0.0290 8 HIS A C 59 O O . HIS A 8 ? 1.0672 0.9849 0.8511 0.2012 0.0069 -0.0205 8 HIS A O 60 C CB . HIS A 8 ? 0.9471 0.9499 0.7524 0.2017 -0.0161 -0.0489 8 HIS A CB 61 C CG . HIS A 8 ? 0.9557 0.9773 0.7644 0.2133 -0.0226 -0.0573 8 HIS A CG 62 N ND1 . HIS A 8 ? 1.0046 1.0346 0.7980 0.2358 -0.0315 -0.0650 8 HIS A ND1 63 C CD2 . HIS A 8 ? 0.9515 0.9868 0.7769 0.2064 -0.0219 -0.0599 8 HIS A CD2 64 C CE1 . HIS A 8 ? 1.0041 1.0519 0.8043 0.2428 -0.0359 -0.0719 8 HIS A CE1 65 N NE2 . HIS A 8 ? 0.9621 1.0132 0.7820 0.2246 -0.0301 -0.0689 8 HIS A NE2 66 N N . ALA A 9 ? 1.0559 0.9795 0.8174 0.2338 -0.0055 -0.0311 9 ALA A N 67 C CA . ALA A 9 ? 1.0277 0.9294 0.7875 0.2332 0.0013 -0.0255 9 ALA A CA 68 C C . ALA A 9 ? 1.0574 0.9742 0.8146 0.2483 -0.0069 -0.0346 9 ALA A C 69 O O . ALA A 9 ? 1.1007 1.0369 0.8503 0.2640 -0.0171 -0.0436 9 ALA A O 70 C CB . ALA A 9 ? 1.0379 0.8924 0.7711 0.2407 0.0107 -0.0145 9 ALA A CB 71 N N . ASN A 10 ? 1.0777 0.9874 0.8412 0.2442 -0.0028 -0.0330 10 ASN A N 72 C CA . ASN A 10 ? 1.0973 1.0196 0.8577 0.2589 -0.0100 -0.0414 10 ASN A CA 73 C C . ASN A 10 ? 1.1253 1.0173 0.8783 0.2585 -0.0023 -0.0356 10 ASN A C 74 O O . ASN A 10 ? 1.0999 0.9586 0.8457 0.2493 0.0087 -0.0253 10 ASN A O 75 C CB . ASN A 10 ? 1.0869 1.0608 0.8764 0.2497 -0.0182 -0.0532 10 ASN A CB 76 C CG . ASN A 10 ? 1.0730 1.0568 0.8891 0.2250 -0.0119 -0.0503 10 ASN A CG 77 O OD1 . ASN A 10 ? 1.1319 1.0873 0.9467 0.2160 -0.0023 -0.0407 10 ASN A OD1 78 N ND2 . ASN A 10 ? 1.0468 1.0716 0.8864 0.2136 -0.0171 -0.0593 10 ASN A ND2 79 N N . ASN A 11 ? 1.2159 1.1199 0.9697 0.2684 -0.0077 -0.0429 11 ASN A N 80 C CA . ASN A 11 ? 1.3197 1.1936 1.0634 0.2695 -0.0009 -0.0388 11 ASN A CA 81 C C . ASN A 11 ? 1.2775 1.1696 1.0514 0.2474 0.0030 -0.0392 11 ASN A C 82 O O . ASN A 11 ? 1.2588 1.1355 1.0288 0.2477 0.0066 -0.0387 11 ASN A O 83 C CB . ASN A 11 ? 1.4245 1.2929 1.1453 0.2964 -0.0085 -0.0457 11 ASN A CB 84 C CG . ASN A 11 ? 1.5255 1.4468 1.2668 0.3022 -0.0210 -0.0596 11 ASN A CG 85 O OD1 . ASN A 11 ? 1.5204 1.4809 1.2926 0.2845 -0.0233 -0.0640 11 ASN A OD1 86 N ND2 . ASN A 11 ? 1.7285 1.6501 1.4507 0.3278 -0.0287 -0.0670 11 ASN A ND2 87 N N . SER A 12 ? 1.2370 1.1596 1.0384 0.2287 0.0024 -0.0403 12 SER A N 88 C CA . SER A 12 ? 1.1576 1.0998 0.9869 0.2083 0.0054 -0.0410 12 SER A CA 89 C C . SER A 12 ? 1.1530 1.0623 0.9800 0.1963 0.0172 -0.0314 12 SER A C 90 O O . SER A 12 ? 1.1040 0.9850 0.9179 0.1944 0.0245 -0.0232 12 SER A O 91 C CB . SER A 12 ? 1.1372 1.1107 0.9895 0.1919 0.0034 -0.0429 12 SER A CB 92 O OG . SER A 12 ? 1.1181 1.1145 0.9953 0.1752 0.0043 -0.0455 12 SER A OG 93 N N . THR A 13 ? 1.1563 1.0708 0.9959 0.1884 0.0191 -0.0333 13 THR A N 94 C CA . THR A 13 ? 1.1603 1.0522 1.0032 0.1739 0.0299 -0.0265 13 THR A CA 95 C C . THR A 13 ? 1.1085 1.0288 0.9821 0.1536 0.0307 -0.0274 13 THR A C 96 O O . THR A 13 ? 1.1094 1.0189 0.9902 0.1407 0.0385 -0.0233 13 THR A O 97 C CB . THR A 13 ? 1.2129 1.0811 1.0410 0.1813 0.0325 -0.0278 13 THR A CB 98 O OG1 . THR A 13 ? 1.2113 1.1081 1.0506 0.1870 0.0239 -0.0370 13 THR A OG1 99 C CG2 . THR A 13 ? 1.2252 1.0550 1.0171 0.2007 0.0341 -0.0251 13 THR A CG2 100 N N . GLU A 14 ? 1.0903 1.0462 0.9804 0.1509 0.0231 -0.0333 14 GLU A N 101 C CA . GLU A 14 ? 1.0726 1.0538 0.9879 0.1327 0.0235 -0.0341 14 GLU A CA 102 C C . GLU A 14 ? 1.0069 0.9748 0.9263 0.1198 0.0316 -0.0256 14 GLU A C 103 O O . GLU A 14 ? 1.0549 1.0099 0.9634 0.1231 0.0335 -0.0210 14 GLU A O 104 C CB . GLU A 14 ? 1.1022 1.1177 1.0283 0.1314 0.0155 -0.0412 14 GLU A CB 105 C CG . GLU A 14 ? 1.1923 1.2309 1.1187 0.1429 0.0070 -0.0517 14 GLU A CG 106 C CD . GLU A 14 ? 1.3252 1.3853 1.2694 0.1341 0.0059 -0.0570 14 GLU A CD 107 O OE1 . GLU A 14 ? 1.4045 1.4823 1.3652 0.1181 0.0070 -0.0573 14 GLU A OE1 108 O OE2 . GLU A 14 ? 1.3835 1.4411 1.3231 0.1439 0.0040 -0.0609 14 GLU A OE2 109 N N . GLN A 15 ? 0.9734 0.9461 0.9081 0.1062 0.0359 -0.0239 15 GLN A N 110 C CA . GLN A 15 ? 0.9464 0.9108 0.8866 0.0948 0.0432 -0.0170 15 GLN A CA 111 C C . GLN A 15 ? 0.8796 0.8686 0.8386 0.0825 0.0413 -0.0182 15 GLN A C 112 O O . GLN A 15 ? 0.8383 0.8470 0.8083 0.0790 0.0370 -0.0237 15 GLN A O 113 C CB . GLN A 15 ? 0.9979 0.9437 0.9373 0.0899 0.0512 -0.0143 15 GLN A CB 114 C CG . GLN A 15 ? 1.1020 1.0190 1.0195 0.1012 0.0540 -0.0137 15 GLN A CG 115 C CD . GLN A 15 ? 1.1816 1.0760 1.0955 0.0932 0.0643 -0.0104 15 GLN A CD 116 O OE1 . GLN A 15 ? 1.2357 1.1019 1.1317 0.0957 0.0715 -0.0058 15 GLN A OE1 117 N NE2 . GLN A 15 ? 1.1979 1.1048 1.1280 0.0827 0.0655 -0.0134 15 GLN A NE2 118 N N . VAL A 16 ? 0.8700 0.8563 0.8305 0.0765 0.0447 -0.0131 16 VAL A N 119 C CA . VAL A 16 ? 0.8177 0.8207 0.7914 0.0657 0.0442 -0.0129 16 VAL A CA 120 C C . VAL A 16 ? 0.8493 0.8424 0.8262 0.0600 0.0516 -0.0069 16 VAL A C 121 O O . VAL A 16 ? 0.8687 0.8433 0.8364 0.0636 0.0569 -0.0027 16 VAL A O 122 C CB . VAL A 16 ? 0.8228 0.8347 0.7928 0.0650 0.0400 -0.0139 16 VAL A CB 123 C CG1 . VAL A 16 ? 0.8268 0.8544 0.7958 0.0695 0.0327 -0.0217 16 VAL A CG1 124 C CG2 . VAL A 16 ? 0.8368 0.8314 0.7938 0.0700 0.0428 -0.0085 16 VAL A CG2 125 N N . ASP A 17 ? 0.9138 0.9198 0.9029 0.0515 0.0520 -0.0070 17 ASP A N 126 C CA . ASP A 17 ? 0.9093 0.9118 0.9031 0.0469 0.0581 -0.0027 17 ASP A CA 127 C C . ASP A 17 ? 0.9181 0.9222 0.9081 0.0462 0.0573 0.0005 17 ASP A C 128 O O . ASP A 17 ? 0.8835 0.8949 0.8708 0.0452 0.0522 -0.0016 17 ASP A O 129 C CB . ASP A 17 ? 0.9643 0.9800 0.9726 0.0399 0.0588 -0.0053 17 ASP A CB 130 C CG . ASP A 17 ? 1.0629 1.0729 1.0738 0.0392 0.0617 -0.0081 17 ASP A CG 131 O OD1 . ASP A 17 ? 1.0733 1.0650 1.0744 0.0427 0.0664 -0.0061 17 ASP A OD1 132 O OD2 . ASP A 17 ? 1.1255 1.1474 1.1466 0.0350 0.0598 -0.0122 17 ASP A OD2 133 N N . THR A 18 ? 0.9288 0.9257 0.9174 0.0463 0.0629 0.0051 18 THR A N 134 C CA . THR A 18 ? 0.9043 0.9013 0.8886 0.0464 0.0630 0.0084 18 THR A CA 135 C C . THR A 18 ? 0.9221 0.9262 0.9159 0.0438 0.0676 0.0097 18 THR A C 136 O O . THR A 18 ? 0.9680 0.9781 0.9722 0.0404 0.0704 0.0075 18 THR A O 137 C CB . THR A 18 ? 0.9256 0.9069 0.8956 0.0522 0.0649 0.0124 18 THR A CB 138 O OG1 . THR A 18 ? 0.9234 0.8956 0.8928 0.0538 0.0723 0.0157 18 THR A OG1 139 C CG2 . THR A 18 ? 0.9461 0.9221 0.9075 0.0564 0.0607 0.0100 18 THR A CG2 140 N N . ILE A 19 ? 0.9709 0.9749 0.9602 0.0458 0.0682 0.0127 19 ILE A N 141 C CA . ILE A 19 ? 0.9653 0.9794 0.9629 0.0456 0.0717 0.0131 19 ILE A CA 142 C C . ILE A 19 ? 0.9584 0.9693 0.9594 0.0458 0.0794 0.0144 19 ILE A C 143 O O . ILE A 19 ? 0.9124 0.9356 0.9260 0.0421 0.0831 0.0118 19 ILE A O 144 C CB . ILE A 19 ? 1.0206 1.0323 1.0084 0.0502 0.0701 0.0160 19 ILE A CB 145 C CG1 . ILE A 19 ? 1.0801 1.0940 1.0631 0.0479 0.0640 0.0142 19 ILE A CG1 146 C CG2 . ILE A 19 ? 1.0493 1.0723 1.0442 0.0531 0.0739 0.0162 19 ILE A CG2 147 C CD1 . ILE A 19 ? 1.1201 1.1494 1.1130 0.0464 0.0623 0.0114 19 ILE A CD1 148 N N . MET A 20 ? 0.9801 0.9747 0.9692 0.0494 0.0821 0.0179 20 MET A N 149 C CA . MET A 20 ? 0.9885 0.9766 0.9770 0.0494 0.0905 0.0198 20 MET A CA 150 C C . MET A 20 ? 0.9772 0.9542 0.9642 0.0460 0.0944 0.0186 20 MET A C 151 O O . MET A 20 ? 1.0006 0.9718 0.9871 0.0434 0.1028 0.0193 20 MET A O 152 C CB . MET A 20 ? 1.0249 0.9986 0.9984 0.0558 0.0921 0.0246 20 MET A CB 153 C CG . MET A 20 ? 1.0635 1.0440 1.0353 0.0601 0.0913 0.0262 20 MET A CG 154 S SD . MET A 20 ? 1.1259 1.0911 1.0830 0.0668 0.0970 0.0313 20 MET A SD 155 C CE . MET A 20 ? 1.2635 1.2320 1.2132 0.0735 0.0924 0.0328 20 MET A CE 156 N N . GLU A 21 ? 0.9604 0.9332 0.9447 0.0465 0.0888 0.0166 21 GLU A N 157 C CA . GLU A 21 ? 0.9972 0.9556 0.9757 0.0459 0.0918 0.0157 21 GLU A CA 158 C C . GLU A 21 ? 0.9963 0.9602 0.9789 0.0453 0.0852 0.0113 21 GLU A C 159 O O . GLU A 21 ? 0.9884 0.9608 0.9715 0.0476 0.0775 0.0101 21 GLU A O 160 C CB . GLU A 21 ? 1.0734 1.0102 1.0329 0.0535 0.0929 0.0195 21 GLU A CB 161 C CG . GLU A 21 ? 1.1469 1.0631 1.0951 0.0546 0.0976 0.0194 21 GLU A CG 162 C CD . GLU A 21 ? 1.2574 1.1508 1.1844 0.0634 0.0991 0.0235 21 GLU A CD 163 O OE1 . GLU A 21 ? 1.3170 1.2120 1.2400 0.0674 0.0971 0.0263 21 GLU A OE1 164 O OE2 . GLU A 21 ? 1.2754 1.1478 1.1879 0.0670 0.1021 0.0238 21 GLU A OE2 165 N N . LYS A 22 ? 1.0593 1.0173 1.0434 0.0417 0.0889 0.0087 22 LYS A N 166 C CA . LYS A 22 ? 1.0538 1.0160 1.0411 0.0417 0.0835 0.0042 22 LYS A CA 167 C C . LYS A 22 ? 1.0061 0.9463 0.9761 0.0490 0.0835 0.0044 22 LYS A C 168 O O . LYS A 22 ? 1.0044 0.9235 0.9606 0.0514 0.0901 0.0078 22 LYS A O 169 C CB . LYS A 22 ? 1.1287 1.1013 1.1299 0.0326 0.0870 0.0002 22 LYS A CB 170 C CG . LYS A 22 ? 1.2046 1.2017 1.2221 0.0280 0.0846 -0.0010 22 LYS A CG 171 C CD . LYS A 22 ? 1.3667 1.3769 1.3984 0.0196 0.0867 -0.0063 22 LYS A CD 172 C CE . LYS A 22 ? 1.4547 1.4887 1.4994 0.0183 0.0803 -0.0088 22 LYS A CE 173 N NZ . LYS A 22 ? 1.4620 1.5078 1.5185 0.0118 0.0799 -0.0147 22 LYS A NZ 174 N N . ASN A 23 ? 1.0347 0.9800 1.0042 0.0535 0.0762 0.0006 23 ASN A N 175 C CA . ASN A 23 ? 1.1167 1.0432 1.0694 0.0628 0.0750 -0.0006 23 ASN A CA 176 C C . ASN A 23 ? 1.0740 0.9836 1.0083 0.0725 0.0751 0.0035 23 ASN A C 177 O O . ASN A 23 ? 1.0913 0.9750 1.0074 0.0779 0.0802 0.0056 23 ASN A O 178 C CB . ASN A 23 ? 1.1653 1.0731 1.1123 0.0587 0.0828 -0.0015 23 ASN A CB 179 C CG . ASN A 23 ? 1.2119 1.1345 1.1733 0.0523 0.0805 -0.0070 23 ASN A CG 180 O OD1 . ASN A 23 ? 1.2045 1.1478 1.1760 0.0541 0.0722 -0.0105 23 ASN A OD1 181 N ND2 . ASN A 23 ? 1.3478 1.2597 1.3094 0.0440 0.0883 -0.0084 23 ASN A ND2 182 N N . VAL A 24 ? 1.0281 0.9509 0.9654 0.0745 0.0698 0.0042 24 VAL A N 183 C CA . VAL A 24 ? 0.9553 0.8661 0.8761 0.0840 0.0683 0.0070 24 VAL A CA 184 C C . VAL A 24 ? 0.9623 0.8771 0.8753 0.0948 0.0596 0.0019 24 VAL A C 185 O O . VAL A 24 ? 0.9444 0.8825 0.8690 0.0930 0.0524 -0.0033 24 VAL A O 186 C CB . VAL A 24 ? 0.9395 0.8631 0.8660 0.0809 0.0660 0.0089 24 VAL A CB 187 C CG1 . VAL A 24 ? 0.9561 0.8674 0.8653 0.0904 0.0643 0.0111 24 VAL A CG1 188 C CG2 . VAL A 24 ? 0.9336 0.8584 0.8695 0.0718 0.0734 0.0128 24 VAL A CG2 189 N N . THR A 25 ? 0.9791 0.8716 0.8715 0.1066 0.0605 0.0029 25 THR A N 190 C CA . THR A 25 ? 0.9674 0.8645 0.8503 0.1199 0.0518 -0.0027 25 THR A CA 191 C C . THR A 25 ? 0.9364 0.8495 0.8191 0.1239 0.0447 -0.0047 25 THR A C 192 O O . THR A 25 ? 0.9352 0.8364 0.8084 0.1253 0.0476 0.0001 25 THR A O 193 C CB . THR A 25 ? 0.9997 0.8644 0.8557 0.1337 0.0548 -0.0007 25 THR A CB 194 O OG1 . THR A 25 ? 1.0291 0.8732 0.8822 0.1272 0.0639 0.0019 25 THR A OG1 195 C CG2 . THR A 25 ? 0.9939 0.8661 0.8411 0.1493 0.0452 -0.0078 25 THR A CG2 196 N N . VAL A 26 ? 0.9086 0.8488 0.8011 0.1249 0.0360 -0.0123 26 VAL A N 197 C CA . VAL A 26 ? 0.9086 0.8660 0.8005 0.1273 0.0292 -0.0162 26 VAL A CA 198 C C . VAL A 26 ? 0.9442 0.9154 0.8291 0.1413 0.0201 -0.0248 26 VAL A C 199 O O . VAL A 26 ? 0.9629 0.9398 0.8496 0.1468 0.0174 -0.0294 26 VAL A O 200 C CB . VAL A 26 ? 0.8819 0.8641 0.7928 0.1121 0.0276 -0.0186 26 VAL A CB 201 C CG1 . VAL A 26 ? 0.8837 0.8538 0.7990 0.1013 0.0354 -0.0106 26 VAL A CG1 202 C CG2 . VAL A 26 ? 0.8477 0.8508 0.7738 0.1069 0.0245 -0.0248 26 VAL A CG2 203 N N . THR A 27 ? 0.9369 0.9157 0.8141 0.1472 0.0150 -0.0278 27 THR A N 204 C CA . THR A 27 ? 0.9410 0.9376 0.8116 0.1616 0.0056 -0.0372 27 THR A CA 205 C C . THR A 27 ? 0.9276 0.9611 0.8171 0.1554 -0.0005 -0.0476 27 THR A C 206 O O . THR A 27 ? 0.9995 1.0470 0.8864 0.1681 -0.0069 -0.0555 27 THR A O 207 C CB . THR A 27 ? 0.9415 0.9429 0.8026 0.1662 0.0015 -0.0393 27 THR A CB 208 O OG1 . THR A 27 ? 0.9136 0.9347 0.7895 0.1490 0.0014 -0.0414 27 THR A OG1 209 C CG2 . THR A 27 ? 0.9714 0.9365 0.8127 0.1727 0.0078 -0.0292 27 THR A CG2 210 N N . HIS A 28 ? 0.9128 0.9613 0.8195 0.1367 0.0017 -0.0477 28 HIS A N 211 C CA . HIS A 28 ? 0.8813 0.9631 0.8053 0.1277 -0.0023 -0.0570 28 HIS A CA 212 C C . HIS A 28 ? 0.8784 0.9594 0.8169 0.1096 0.0037 -0.0524 28 HIS A C 213 O O . HIS A 28 ? 0.9293 0.9928 0.8663 0.1014 0.0095 -0.0442 28 HIS A O 214 C CB . HIS A 28 ? 0.8793 0.9886 0.8061 0.1232 -0.0079 -0.0661 28 HIS A CB 215 C CG . HIS A 28 ? 0.9253 1.0412 0.8389 0.1412 -0.0150 -0.0724 28 HIS A CG 216 N ND1 . HIS A 28 ? 0.9458 1.0410 0.8430 0.1491 -0.0145 -0.0672 28 HIS A ND1 217 C CD2 . HIS A 28 ? 0.8954 1.0372 0.8091 0.1543 -0.0232 -0.0837 28 HIS A CD2 218 C CE1 . HIS A 28 ? 0.9323 1.0396 0.8193 0.1663 -0.0223 -0.0750 28 HIS A CE1 219 N NE2 . HIS A 28 ? 0.9313 1.0678 0.8282 0.1703 -0.0279 -0.0854 28 HIS A NE2 220 N N . ALA A 29 ? 0.9208 1.0220 0.8724 0.1044 0.0019 -0.0583 29 ALA A N 221 C CA . ALA A 29 ? 0.9175 1.0194 0.8817 0.0889 0.0068 -0.0549 29 ALA A CA 222 C C . ALA A 29 ? 0.8909 1.0245 0.8682 0.0814 0.0031 -0.0648 29 ALA A C 223 O O . ALA A 29 ? 0.9602 1.1144 0.9381 0.0901 -0.0028 -0.0741 29 ALA A O 224 C CB . ALA A 29 ? 0.9177 0.9979 0.8818 0.0922 0.0117 -0.0479 29 ALA A CB 225 N N . GLN A 30 ? 0.9164 1.0542 0.9028 0.0659 0.0067 -0.0633 30 GLN A N 226 C CA . GLN A 30 ? 0.9424 1.1079 0.9401 0.0571 0.0047 -0.0721 30 GLN A CA 227 C C . GLN A 30 ? 0.9467 1.1064 0.9528 0.0498 0.0087 -0.0678 30 GLN A C 228 O O . GLN A 30 ? 0.9679 1.1140 0.9737 0.0401 0.0134 -0.0609 30 GLN A O 229 C CB . GLN A 30 ? 0.9677 1.1482 0.9651 0.0429 0.0049 -0.0772 30 GLN A CB 230 C CG . GLN A 30 ? 1.0226 1.2354 1.0302 0.0340 0.0029 -0.0885 30 GLN A CG 231 C CD . GLN A 30 ? 1.0501 1.2789 1.0553 0.0191 0.0035 -0.0957 30 GLN A CD 232 O OE1 . GLN A 30 ? 1.0977 1.3421 1.1080 0.0048 0.0057 -0.1013 30 GLN A OE1 233 N NE2 . GLN A 30 ? 1.0684 1.2926 1.0645 0.0218 0.0019 -0.0961 30 GLN A NE2 234 N N . ASP A 31 ? 0.9734 1.1434 0.9860 0.0558 0.0065 -0.0723 31 ASP A N 235 C CA . ASP A 31 ? 0.9596 1.1292 0.9809 0.0489 0.0093 -0.0706 31 ASP A CA 236 C C . ASP A 31 ? 0.9361 1.1260 0.9638 0.0335 0.0100 -0.0757 31 ASP A C 237 O O . ASP A 31 ? 0.9242 1.1385 0.9540 0.0312 0.0068 -0.0852 31 ASP A O 238 C CB . ASP A 31 ? 0.9962 1.1717 1.0207 0.0600 0.0064 -0.0753 31 ASP A CB 239 C CG . ASP A 31 ? 1.0763 1.2477 1.1087 0.0542 0.0094 -0.0729 31 ASP A CG 240 O OD1 . ASP A 31 ? 1.2067 1.3742 1.2430 0.0419 0.0132 -0.0684 31 ASP A OD1 241 O OD2 . ASP A 31 ? 1.2004 1.3719 1.2338 0.0627 0.0079 -0.0759 31 ASP A OD2 242 N N . ILE A 32 ? 0.9073 1.0870 0.9367 0.0231 0.0144 -0.0699 32 ILE A N 243 C CA . ILE A 32 ? 0.8895 1.0817 0.9204 0.0082 0.0162 -0.0734 32 ILE A CA 244 C C . ILE A 32 ? 0.8724 1.0682 0.9108 0.0036 0.0178 -0.0733 32 ILE A C 245 O O . ILE A 32 ? 0.8547 1.0565 0.8921 -0.0085 0.0202 -0.0751 32 ILE A O 246 C CB . ILE A 32 ? 0.8642 1.0390 0.8844 -0.0009 0.0201 -0.0671 32 ILE A CB 247 C CG1 . ILE A 32 ? 0.8630 1.0124 0.8806 0.0034 0.0231 -0.0562 32 ILE A CG1 248 C CG2 . ILE A 32 ? 0.8726 1.0490 0.8853 0.0009 0.0184 -0.0698 32 ILE A CG2 249 C CD1 . ILE A 32 ? 0.8660 0.9985 0.8722 -0.0041 0.0269 -0.0501 32 ILE A CD1 250 N N . LEU A 33 ? 0.8610 1.0518 0.9051 0.0130 0.0168 -0.0716 33 LEU A N 251 C CA . LEU A 33 ? 0.8798 1.0739 0.9311 0.0097 0.0178 -0.0719 33 LEU A CA 252 C C . LEU A 33 ? 0.8972 1.1100 0.9555 0.0165 0.0142 -0.0805 33 LEU A C 253 O O . LEU A 33 ? 0.9048 1.1140 0.9617 0.0291 0.0116 -0.0817 33 LEU A O 254 C CB . LEU A 33 ? 0.8679 1.0408 0.9198 0.0135 0.0203 -0.0637 33 LEU A CB 255 C CG . LEU A 33 ? 0.8645 1.0402 0.9236 0.0097 0.0213 -0.0639 33 LEU A CG 256 C CD1 . LEU A 33 ? 0.8920 1.0701 0.9483 -0.0015 0.0234 -0.0624 33 LEU A CD1 257 C CD2 . LEU A 33 ? 0.8948 1.0535 0.9559 0.0141 0.0235 -0.0582 33 LEU A CD2 258 N N . GLU A 34 ? 0.8906 1.1217 0.9543 0.0087 0.0143 -0.0863 34 GLU A N 259 C CA . GLU A 34 ? 0.9458 1.1961 1.0164 0.0150 0.0111 -0.0949 34 GLU A CA 260 C C . GLU A 34 ? 0.8992 1.1382 0.9736 0.0184 0.0118 -0.0918 34 GLU A C 261 O O . GLU A 34 ? 0.8860 1.1205 0.9622 0.0096 0.0146 -0.0883 34 GLU A O 262 C CB . GLU A 34 ? 0.9730 1.2504 1.0476 0.0042 0.0115 -0.1036 34 GLU A CB 263 C CG . GLU A 34 ? 1.0064 1.3081 1.0885 0.0115 0.0080 -0.1138 34 GLU A CG 264 C CD . GLU A 34 ? 1.0715 1.3783 1.1522 0.0285 0.0029 -0.1182 34 GLU A CD 265 O OE1 . GLU A 34 ? 1.1530 1.4759 1.2324 0.0292 0.0008 -0.1238 34 GLU A OE1 266 O OE2 . GLU A 34 ? 1.1406 1.4335 1.2195 0.0413 0.0011 -0.1161 34 GLU A OE2 267 N N . LYS A 35 ? 0.9045 1.1381 0.9784 0.0315 0.0094 -0.0935 35 LYS A N 268 C CA . LYS A 35 ? 0.9108 1.1321 0.9870 0.0344 0.0105 -0.0916 35 LYS A CA 269 C C . LYS A 35 ? 0.8850 1.1227 0.9652 0.0400 0.0077 -0.1003 35 LYS A C 270 O O . LYS A 35 ? 0.9052 1.1352 0.9876 0.0400 0.0087 -0.0999 35 LYS A O 271 C CB . LYS A 35 ? 0.9271 1.1217 0.9958 0.0438 0.0116 -0.0859 35 LYS A CB 272 C CG . LYS A 35 ? 0.9637 1.1413 1.0285 0.0393 0.0149 -0.0772 35 LYS A CG 273 C CD . LYS A 35 ? 1.0326 1.1844 1.0886 0.0484 0.0169 -0.0726 35 LYS A CD 274 C CE . LYS A 35 ? 1.0920 1.2331 1.1409 0.0498 0.0180 -0.0671 35 LYS A CE 275 N NZ . LYS A 35 ? 1.0896 1.2445 1.1340 0.0567 0.0135 -0.0722 35 LYS A NZ 276 N N . THR A 36 ? 0.8753 1.1366 0.9565 0.0447 0.0041 -0.1089 36 THR A N 277 C CA . THR A 36 ? 0.9311 1.2102 1.0155 0.0526 0.0010 -0.1182 36 THR A CA 278 C C . THR A 36 ? 0.9586 1.2681 1.0518 0.0417 0.0015 -0.1256 36 THR A C 279 O O . THR A 36 ? 0.9179 1.2412 1.0129 0.0308 0.0030 -0.1268 36 THR A O 280 C CB . THR A 36 ? 0.9900 1.2774 1.0684 0.0698 -0.0039 -0.1246 36 THR A CB 281 O OG1 . THR A 36 ? 1.0052 1.3172 1.0866 0.0658 -0.0055 -0.1297 36 THR A OG1 282 C CG2 . THR A 36 ? 1.0544 1.3092 1.1203 0.0811 -0.0037 -0.1174 36 THR A CG2 283 N N . HIS A 37 ? 0.9569 1.2752 1.0540 0.0443 0.0007 -0.1307 37 HIS A N 284 C CA . HIS A 37 ? 0.9292 1.2777 1.0337 0.0361 0.0012 -0.1392 37 HIS A CA 285 C C . HIS A 37 ? 0.9457 1.3112 1.0518 0.0505 -0.0029 -0.1492 37 HIS A C 286 O O . HIS A 37 ? 0.9856 1.3346 1.0849 0.0662 -0.0057 -0.1484 37 HIS A O 287 C CB . HIS A 37 ? 0.9151 1.2561 1.0219 0.0222 0.0053 -0.1346 37 HIS A CB 288 C CG . HIS A 37 ? 0.9354 1.2547 1.0411 0.0275 0.0052 -0.1303 37 HIS A CG 289 N ND1 . HIS A 37 ? 0.9538 1.2810 1.0621 0.0325 0.0039 -0.1364 37 HIS A ND1 290 C CD2 . HIS A 37 ? 0.9735 1.2646 1.0759 0.0275 0.0067 -0.1213 37 HIS A CD2 291 C CE1 . HIS A 37 ? 0.9397 1.2435 1.0457 0.0349 0.0045 -0.1315 37 HIS A CE1 292 N NE2 . HIS A 37 ? 0.9819 1.2648 1.0850 0.0314 0.0064 -0.1226 37 HIS A NE2 293 N N . ASN A 38 ? 0.9587 1.3559 1.0719 0.0457 -0.0027 -0.1588 38 ASN A N 294 C CA . ASN A 38 ? 0.9963 1.4137 1.1112 0.0605 -0.0068 -0.1695 38 ASN A CA 295 C C . ASN A 38 ? 0.9893 1.3973 1.1042 0.0624 -0.0061 -0.1695 38 ASN A C 296 O O . ASN A 38 ? 1.0371 1.4546 1.1505 0.0768 -0.0095 -0.1772 38 ASN A O 297 C CB . ASN A 38 ? 0.9721 1.4340 1.0954 0.0558 -0.0071 -0.1822 38 ASN A CB 298 C CG . ASN A 38 ? 0.9746 1.4503 1.1039 0.0354 -0.0015 -0.1836 38 ASN A CG 299 O OD1 . ASN A 38 ? 1.0204 1.4731 1.1473 0.0264 0.0019 -0.1751 38 ASN A OD1 300 N ND2 . ASN A 38 ? 0.9586 1.4725 1.0947 0.0281 -0.0001 -0.1949 38 ASN A ND2 301 N N . GLY A 39 ? 0.9385 1.3293 1.0543 0.0485 -0.0020 -0.1617 39 GLY A N 302 C CA . GLY A 39 ? 0.9066 1.2851 1.0218 0.0492 -0.0013 -0.1607 39 GLY A CA 303 C C . GLY A 39 ? 0.9016 1.3075 1.0229 0.0435 -0.0002 -0.1692 39 GLY A C 304 O O . GLY A 39 ? 0.9051 1.3055 1.0257 0.0468 -0.0006 -0.1709 39 GLY A O 305 N N . LYS A 40 ? 0.9255 1.3603 1.0520 0.0337 0.0018 -0.1747 40 LYS A N 306 C CA . LYS A 40 ? 0.9270 1.3928 1.0590 0.0283 0.0035 -0.1846 40 LYS A CA 307 C C . LYS A 40 ? 0.9371 1.4101 1.0695 0.0067 0.0097 -0.1827 40 LYS A C 308 O O . LYS A 40 ? 0.9441 1.4066 1.0732 -0.0032 0.0121 -0.1763 40 LYS A O 309 C CB . LYS A 40 ? 0.9195 1.4205 1.0563 0.0381 0.0004 -0.1971 40 LYS A CB 310 C CG . LYS A 40 ? 0.9814 1.4770 1.1143 0.0622 -0.0058 -0.2009 40 LYS A CG 311 C CD . LYS A 40 ? 1.0064 1.5352 1.1425 0.0745 -0.0100 -0.2123 40 LYS A CD 312 C CE . LYS A 40 ? 1.0505 1.5691 1.1779 0.1009 -0.0163 -0.2157 40 LYS A CE 313 N NZ . LYS A 40 ? 1.0972 1.6398 1.2242 0.1163 -0.0216 -0.2242 40 LYS A NZ 314 N N . LEU A 41 ? 0.9805 1.4699 1.1148 -0.0002 0.0126 -0.1883 41 LEU A N 315 C CA . LEU A 41 ? 1.0429 1.5423 1.1747 -0.0205 0.0193 -0.1888 41 LEU A CA 316 C C . LEU A 41 ? 0.9763 1.5163 1.1144 -0.0249 0.0212 -0.2019 41 LEU A C 317 O O . LEU A 41 ? 0.9540 1.5212 1.0991 -0.0150 0.0187 -0.2127 41 LEU A O 318 C CB . LEU A 41 ? 1.1039 1.5979 1.2323 -0.0265 0.0222 -0.1877 41 LEU A CB 319 C CG . LEU A 41 ? 1.1626 1.6205 1.2855 -0.0239 0.0205 -0.1761 41 LEU A CG 320 C CD1 . LEU A 41 ? 1.2093 1.6664 1.3295 -0.0272 0.0222 -0.1772 41 LEU A CD1 321 C CD2 . LEU A 41 ? 1.1913 1.6259 1.3063 -0.0343 0.0233 -0.1655 41 LEU A CD2 322 N N . CYS A 42 ? 0.9673 1.5120 1.1025 -0.0399 0.0256 -0.2015 42 CYS A N 323 C CA . CYS A 42 ? 0.9910 1.5748 1.1329 -0.0448 0.0271 -0.2144 42 CYS A CA 324 C C . CYS A 42 ? 0.9178 1.5131 1.0542 -0.0696 0.0366 -0.2180 42 CYS A C 325 O O . CYS A 42 ? 0.8688 1.4351 0.9928 -0.0825 0.0418 -0.2083 42 CYS A O 326 C CB . CYS A 42 ? 1.0581 1.6379 1.2005 -0.0399 0.0235 -0.2124 42 CYS A CB 327 S SG . CYS A 42 ? 1.0755 1.6386 1.2201 -0.0113 0.0133 -0.2082 42 CYS A SG 328 N N . ASP A 43 ? 0.9018 1.5392 1.0460 -0.0763 0.0391 -0.2325 43 ASP A N 329 C CA . ASP A 43 ? 0.9531 1.6017 1.0905 -0.1025 0.0494 -0.2373 43 ASP A CA 330 C C . ASP A 43 ? 0.9091 1.5302 1.0360 -0.1125 0.0514 -0.2283 43 ASP A C 331 O O . ASP A 43 ? 0.8918 1.5048 1.0225 -0.0991 0.0445 -0.2245 43 ASP A O 332 C CB . ASP A 43 ? 0.9827 1.6865 1.1326 -0.1080 0.0515 -0.2563 43 ASP A CB 333 C CG . ASP A 43 ? 0.9856 1.7210 1.1464 -0.0963 0.0492 -0.2668 43 ASP A CG 334 O OD1 . ASP A 43 ? 1.0461 1.7591 1.2033 -0.0868 0.0471 -0.2593 43 ASP A OD1 335 O OD2 . ASP A 43 ? 0.9975 1.7818 1.1706 -0.0962 0.0494 -0.2833 43 ASP A OD2 336 N N . LEU A 44 ? 0.9415 1.5462 1.0529 -0.1355 0.0611 -0.2248 44 LEU A N 337 C CA . LEU A 44 ? 0.9873 1.5656 1.0855 -0.1474 0.0645 -0.2175 44 LEU A CA 338 C C . LEU A 44 ? 1.0538 1.6608 1.1499 -0.1702 0.0729 -0.2305 44 LEU A C 339 O O . LEU A 44 ? 1.0126 1.6204 1.0969 -0.1911 0.0833 -0.2341 44 LEU A O 340 C CB . LEU A 44 ? 0.9827 1.5128 1.0598 -0.1546 0.0690 -0.2024 44 LEU A CB 341 C CG . LEU A 44 ? 1.0495 1.5435 1.1114 -0.1603 0.0705 -0.1916 44 LEU A CG 342 C CD1 . LEU A 44 ? 1.0698 1.5543 1.1423 -0.1393 0.0602 -0.1850 44 LEU A CD1 343 C CD2 . LEU A 44 ? 1.0797 1.5304 1.1184 -0.1676 0.0758 -0.1789 44 LEU A CD2 344 N N . ASP A 45 ? 1.1303 1.7605 1.2369 -0.1665 0.0687 -0.2379 45 ASP A N 345 C CA . ASP A 45 ? 1.1837 1.8515 1.2936 -0.1859 0.0750 -0.2537 45 ASP A CA 346 C C . ASP A 45 ? 1.1122 1.8267 1.2338 -0.1917 0.0789 -0.2696 45 ASP A C 347 O O . ASP A 45 ? 1.0899 1.8177 1.2038 -0.2173 0.0903 -0.2780 45 ASP A O 348 C CB . ASP A 45 ? 1.2976 1.9355 1.3841 -0.2133 0.0863 -0.2491 45 ASP A CB 349 C CG . ASP A 45 ? 1.4293 2.0278 1.5053 -0.2080 0.0825 -0.2361 45 ASP A CG 350 O OD1 . ASP A 45 ? 1.5104 2.0869 1.5906 -0.1853 0.0734 -0.2245 45 ASP A OD1 351 O OD2 . ASP A 45 ? 1.5580 2.1474 1.6208 -0.2272 0.0892 -0.2379 45 ASP A OD2 352 N N . GLY A 46 ? 1.0879 1.8247 1.2262 -0.1679 0.0700 -0.2734 46 GLY A N 353 C CA . GLY A 46 ? 1.0508 1.8354 1.2023 -0.1684 0.0721 -0.2891 46 GLY A CA 354 C C . GLY A 46 ? 1.0375 1.8087 1.1789 -0.1794 0.0802 -0.2857 46 GLY A C 355 O O . GLY A 46 ? 1.0533 1.8628 1.2048 -0.1798 0.0824 -0.2983 46 GLY A O 356 N N . VAL A 47 ? 1.0122 1.7303 1.1331 -0.1871 0.0843 -0.2692 47 VAL A N 357 C CA . VAL A 47 ? 0.9907 1.6899 1.0978 -0.1974 0.0920 -0.2645 47 VAL A CA 358 C C . VAL A 47 ? 0.9769 1.6497 1.0856 -0.1739 0.0833 -0.2525 47 VAL A C 359 O O . VAL A 47 ? 0.9827 1.6129 1.0820 -0.1663 0.0792 -0.2374 47 VAL A O 360 C CB . VAL A 47 ? 0.9934 1.6498 1.0727 -0.2214 0.1029 -0.2547 47 VAL A CB 361 C CG1 . VAL A 47 ? 1.0186 1.6540 1.0805 -0.2308 0.1108 -0.2498 47 VAL A CG1 362 C CG2 . VAL A 47 ? 1.0014 1.6806 1.0770 -0.2467 0.1123 -0.2668 47 VAL A CG2 363 N N . LYS A 48 ? 0.9515 1.6508 1.0718 -0.1631 0.0808 -0.2602 48 LYS A N 364 C CA . LYS A 48 ? 0.9331 1.6122 1.0562 -0.1410 0.0724 -0.2515 48 LYS A CA 365 C C . LYS A 48 ? 0.9497 1.5819 1.0530 -0.1476 0.0763 -0.2368 48 LYS A C 366 O O . LYS A 48 ? 0.9951 1.6204 1.0828 -0.1680 0.0867 -0.2371 48 LYS A O 367 C CB . LYS A 48 ? 0.9366 1.6551 1.0739 -0.1302 0.0703 -0.2643 48 LYS A CB 368 C CG . LYS A 48 ? 0.9788 1.6758 1.1141 -0.1145 0.0654 -0.2570 48 LYS A CG 369 C CD . LYS A 48 ? 1.0043 1.7382 1.1550 -0.0966 0.0600 -0.2694 48 LYS A CD 370 C CE . LYS A 48 ? 1.0534 1.7596 1.2016 -0.0785 0.0534 -0.2609 48 LYS A CE 371 N NZ . LYS A 48 ? 1.1062 1.8431 1.2658 -0.0603 0.0484 -0.2725 48 LYS A NZ 372 N N . PRO A 49 ? 0.9409 1.5407 1.0434 -0.1302 0.0681 -0.2244 49 PRO A N 373 C CA . PRO A 49 ? 0.9195 1.4794 1.0047 -0.1335 0.0704 -0.2117 49 PRO A CA 374 C C . PRO A 49 ? 0.9009 1.4695 0.9860 -0.1308 0.0716 -0.2155 49 PRO A C 375 O O . PRO A 49 ? 0.8838 1.4850 0.9842 -0.1208 0.0683 -0.2261 49 PRO A O 376 C CB . PRO A 49 ? 0.9237 1.4558 1.0130 -0.1147 0.0606 -0.2005 49 PRO A CB 377 C CG . PRO A 49 ? 0.9103 1.4702 1.0194 -0.0971 0.0528 -0.2088 49 PRO A CG 378 C CD . PRO A 49 ? 0.9191 1.5166 1.0348 -0.1075 0.0570 -0.2217 49 PRO A CD 379 N N . LEU A 50 ? 0.9165 1.4550 0.9829 -0.1382 0.0759 -0.2068 50 LEU A N 380 C CA . LEU A 50 ? 0.8952 1.4342 0.9592 -0.1334 0.0758 -0.2078 50 LEU A CA 381 C C . LEU A 50 ? 0.8832 1.4030 0.9545 -0.1127 0.0652 -0.2001 50 LEU A C 382 O O . LEU A 50 ? 0.9191 1.4051 0.9807 -0.1103 0.0628 -0.1882 50 LEU A O 383 C CB . LEU A 50 ? 0.9245 1.4382 0.9624 -0.1498 0.0851 -0.2021 50 LEU A CB 384 C CG . LEU A 50 ? 0.9536 1.4607 0.9841 -0.1455 0.0851 -0.2011 50 LEU A CG 385 C CD1 . LEU A 50 ? 0.9500 1.4970 0.9979 -0.1395 0.0840 -0.2144 50 LEU A CD1 386 C CD2 . LEU A 50 ? 0.9981 1.4828 0.9995 -0.1637 0.0961 -0.1972 50 LEU A CD2 387 N N . ILE A 51 ? 0.8647 1.4064 0.9523 -0.0976 0.0590 -0.2075 51 ILE A N 388 C CA . ILE A 51 ? 0.8503 1.3751 0.9444 -0.0792 0.0498 -0.2020 51 ILE A CA 389 C C . ILE A 51 ? 0.8635 1.3866 0.9531 -0.0764 0.0499 -0.2036 51 ILE A C 390 O O . ILE A 51 ? 0.8272 1.3761 0.9249 -0.0707 0.0494 -0.2138 51 ILE A O 391 C CB . ILE A 51 ? 0.8568 1.4005 0.9680 -0.0628 0.0428 -0.2086 51 ILE A CB 392 C CG1 . ILE A 51 ? 0.9239 1.4638 1.0375 -0.0647 0.0420 -0.2053 51 ILE A CG1 393 C CG2 . ILE A 51 ? 0.8439 1.3696 0.9592 -0.0451 0.0347 -0.2048 51 ILE A CG2 394 C CD1 . ILE A 51 ? 0.9729 1.5390 1.1005 -0.0516 0.0370 -0.2143 51 ILE A CD1 395 N N . LEU A 52 ? 0.9064 1.3997 0.9826 -0.0793 0.0502 -0.1939 52 LEU A N 396 C CA . LEU A 52 ? 0.9222 1.4118 0.9912 -0.0780 0.0506 -0.1948 52 LEU A CA 397 C C . LEU A 52 ? 0.9316 1.4243 1.0128 -0.0610 0.0425 -0.1981 52 LEU A C 398 O O . LEU A 52 ? 0.9256 1.4215 1.0036 -0.0586 0.0423 -0.2016 52 LEU A O 399 C CB . LEU A 52 ? 0.9141 1.3712 0.9644 -0.0834 0.0520 -0.1837 52 LEU A CB 400 C CG . LEU A 52 ? 0.9441 1.3904 0.9748 -0.1007 0.0612 -0.1798 52 LEU A CG 401 C CD1 . LEU A 52 ? 0.9768 1.3877 0.9884 -0.1007 0.0604 -0.1681 52 LEU A CD1 402 C CD2 . LEU A 52 ? 0.9585 1.4230 0.9801 -0.1133 0.0702 -0.1881 52 LEU A CD2 403 N N . ARG A 53 ? 0.9940 1.4837 1.0870 -0.0495 0.0362 -0.1971 53 ARG A N 404 C CA . ARG A 53 ? 1.0539 1.5418 1.1554 -0.0338 0.0292 -0.2003 53 ARG A CA 405 C C . ARG A 53 ? 1.0505 1.5156 1.1449 -0.0326 0.0266 -0.1947 53 ARG A C 406 O O . ARG A 53 ? 1.1071 1.5498 1.1967 -0.0353 0.0254 -0.1854 53 ARG A O 407 C CB . ARG A 53 ? 1.0811 1.5994 1.1893 -0.0275 0.0297 -0.2130 53 ARG A CB 408 C CG . ARG A 53 ? 1.1799 1.6959 1.2952 -0.0093 0.0226 -0.2173 53 ARG A CG 409 C CD . ARG A 53 ? 1.2523 1.7960 1.3711 -0.0016 0.0229 -0.2299 53 ARG A CD 410 N NE . ARG A 53 ? 1.2894 1.8580 1.4167 0.0071 0.0217 -0.2379 53 ARG A NE 411 C CZ . ARG A 53 ? 1.3202 1.9190 1.4518 -0.0014 0.0265 -0.2440 53 ARG A CZ 412 N NH1 . ARG A 53 ? 1.3667 1.9717 1.4931 -0.0203 0.0341 -0.2426 53 ARG A NH1 413 N NH2 . ARG A 53 ? 1.3518 1.9744 1.4915 0.0091 0.0240 -0.2522 53 ARG A NH2 414 N N . ASP A 54 ? 1.0393 1.5120 1.1327 -0.0284 0.0258 -0.2008 54 ASP A N 415 C CA . ASP A 54 ? 1.0020 1.4570 1.0895 -0.0266 0.0227 -0.1975 54 ASP A CA 416 C C . ASP A 54 ? 0.9660 1.4156 1.0385 -0.0375 0.0273 -0.1936 54 ASP A C 417 O O . ASP A 54 ? 1.0634 1.4996 1.1296 -0.0358 0.0246 -0.1907 54 ASP A O 418 C CB . ASP A 54 ? 1.0188 1.4820 1.1102 -0.0165 0.0194 -0.2063 54 ASP A CB 419 C CG . ASP A 54 ? 1.0382 1.4988 1.1392 -0.0038 0.0146 -0.2095 54 ASP A CG 420 O OD1 . ASP A 54 ? 1.0625 1.5037 1.1660 -0.0018 0.0116 -0.2030 54 ASP A OD1 421 O OD2 . ASP A 54 ? 1.0446 1.5214 1.1488 0.0047 0.0140 -0.2186 54 ASP A OD2 422 N N . CYS A 55 ? 0.9883 1.4480 1.0535 -0.0486 0.0346 -0.1941 55 CYS A N 423 C CA . CYS A 55 ? 1.0476 1.4969 1.0936 -0.0592 0.0401 -0.1897 55 CYS A CA 424 C C . CYS A 55 ? 1.0156 1.4403 1.0519 -0.0636 0.0403 -0.1787 55 CYS A C 425 O O . CYS A 55 ? 1.0536 1.4761 1.0968 -0.0642 0.0398 -0.1756 55 CYS A O 426 C CB . CYS A 55 ? 1.0923 1.5610 1.1312 -0.0714 0.0494 -0.1959 55 CYS A CB 427 S SG . CYS A 55 ? 1.2768 1.7751 1.3239 -0.0657 0.0498 -0.2092 55 CYS A SG 428 N N . SER A 56 ? 1.0286 1.4347 1.0478 -0.0651 0.0405 -0.1729 56 SER A N 429 C CA . SER A 56 ? 1.0117 1.3938 1.0157 -0.0692 0.0419 -0.1629 56 SER A CA 430 C C . SER A 56 ? 1.0001 1.3786 0.9832 -0.0836 0.0522 -0.1622 56 SER A C 431 O O . SER A 56 ? 0.9938 1.3890 0.9744 -0.0903 0.0580 -0.1695 56 SER A O 432 C CB . SER A 56 ? 1.0290 1.3934 1.0223 -0.0619 0.0367 -0.1579 56 SER A CB 433 O OG . SER A 56 ? 1.0676 1.4258 1.0381 -0.0669 0.0417 -0.1579 56 SER A OG 434 N N . VAL A 57 ? 1.0092 1.3648 0.9759 -0.0885 0.0550 -0.1536 57 VAL A N 435 C CA . VAL A 57 ? 1.0425 1.3880 0.9853 -0.1037 0.0657 -0.1521 57 VAL A CA 436 C C . VAL A 57 ? 1.0883 1.4258 1.0077 -0.1071 0.0705 -0.1530 57 VAL A C 437 O O . VAL A 57 ? 1.1098 1.4528 1.0164 -0.1207 0.0804 -0.1574 57 VAL A O 438 C CB . VAL A 57 ? 1.0575 1.3743 0.9839 -0.1061 0.0671 -0.1420 57 VAL A CB 439 C CG1 . VAL A 57 ? 1.0768 1.3756 0.9719 -0.1223 0.0790 -0.1400 57 VAL A CG1 440 C CG2 . VAL A 57 ? 1.0592 1.3855 1.0077 -0.1045 0.0638 -0.1420 57 VAL A CG2 441 N N . ALA A 58 ? 1.1024 1.4284 1.0164 -0.0950 0.0635 -0.1496 58 ALA A N 442 C CA . ALA A 58 ? 1.1073 1.4256 0.9989 -0.0956 0.0666 -0.1505 58 ALA A CA 443 C C . ALA A 58 ? 1.1043 1.4513 1.0086 -0.0983 0.0689 -0.1613 58 ALA A C 444 O O . ALA A 58 ? 1.1293 1.4756 1.0142 -0.1082 0.0778 -0.1642 58 ALA A O 445 C CB . ALA A 58 ? 1.0954 1.3991 0.9812 -0.0805 0.0572 -0.1456 58 ALA A CB 446 N N . GLY A 59 ? 1.0278 1.3982 0.9623 -0.0893 0.0613 -0.1674 59 GLY A N 447 C CA . GLY A 59 ? 1.0120 1.4106 0.9598 -0.0896 0.0627 -0.1783 59 GLY A CA 448 C C . GLY A 59 ? 1.0619 1.4794 1.0104 -0.1040 0.0731 -0.1845 59 GLY A C 449 O O . GLY A 59 ? 1.1252 1.5619 1.0727 -0.1089 0.0784 -0.1928 59 GLY A O 450 N N . TRP A 60 ? 1.0623 1.4762 1.0128 -0.1113 0.0760 -0.1813 60 TRP A N 451 C CA . TRP A 60 ? 1.0452 1.4785 0.9968 -0.1265 0.0859 -0.1880 60 TRP A CA 452 C C . TRP A 60 ? 1.0880 1.5052 1.0073 -0.1436 0.0985 -0.1863 60 TRP A C 453 O O . TRP A 60 ? 1.1312 1.5690 1.0478 -0.1548 0.1073 -0.1951 60 TRP A O 454 C CB . TRP A 60 ? 1.0448 1.4783 1.0081 -0.1286 0.0845 -0.1854 60 TRP A CB 455 C CG . TRP A 60 ? 1.0249 1.4697 0.9818 -0.1475 0.0957 -0.1902 60 TRP A CG 456 C CD1 . TRP A 60 ? 0.9990 1.4746 0.9600 -0.1584 0.1037 -0.2018 60 TRP A CD1 457 C CD2 . TRP A 60 ? 1.0181 1.4449 0.9636 -0.1583 0.1004 -0.1844 60 TRP A CD2 458 N NE1 . TRP A 60 ? 1.0655 1.5446 1.0187 -0.1768 0.1135 -0.2042 60 TRP A NE1 459 C CE2 . TRP A 60 ? 1.0295 1.4774 0.9724 -0.1771 0.1115 -0.1934 60 TRP A CE2 460 C CE3 . TRP A 60 ? 1.0194 1.4152 0.9565 -0.1541 0.0964 -0.1731 60 TRP A CE3 461 C CZ2 . TRP A 60 ? 1.0698 1.5069 1.0010 -0.1926 0.1189 -0.1916 60 TRP A CZ2 462 C CZ3 . TRP A 60 ? 1.0343 1.4182 0.9592 -0.1681 0.1034 -0.1706 60 TRP A CZ3 463 C CH2 . TRP A 60 ? 1.0613 1.4650 0.9831 -0.1875 0.1145 -0.1798 60 TRP A CH2 464 N N . LEU A 61 ? 1.0972 1.4767 0.9904 -0.1454 0.0998 -0.1752 61 LEU A N 465 C CA . LEU A 61 ? 1.1328 1.4889 0.9895 -0.1616 0.1125 -0.1723 61 LEU A CA 466 C C . LEU A 61 ? 1.1645 1.5181 1.0034 -0.1613 0.1161 -0.1748 61 LEU A C 467 O O . LEU A 61 ? 1.1963 1.5531 1.0177 -0.1777 0.1286 -0.1798 61 LEU A O 468 C CB . LEU A 61 ? 1.1407 1.4537 0.9707 -0.1605 0.1123 -0.1596 61 LEU A CB 469 C CG . LEU A 61 ? 1.1733 1.4842 1.0132 -0.1651 0.1121 -0.1569 61 LEU A CG 470 C CD1 . LEU A 61 ? 1.2358 1.5022 1.0464 -0.1622 0.1118 -0.1443 61 LEU A CD1 471 C CD2 . LEU A 61 ? 1.1857 1.5147 1.0262 -0.1866 0.1242 -0.1651 61 LEU A CD2 472 N N . LEU A 62 ? 1.1399 1.4887 0.9832 -0.1437 0.1055 -0.1721 62 LEU A N 473 C CA . LEU A 62 ? 1.1384 1.4853 0.9657 -0.1412 0.1074 -0.1747 62 LEU A CA 474 C C . LEU A 62 ? 1.1212 1.5078 0.9700 -0.1437 0.1097 -0.1875 62 LEU A C 475 O O . LEU A 62 ? 1.1328 1.5210 0.9655 -0.1479 0.1157 -0.1913 62 LEU A O 476 C CB . LEU A 62 ? 1.1392 1.4718 0.9661 -0.1214 0.0947 -0.1691 62 LEU A CB 477 C CG . LEU A 62 ? 1.1574 1.4502 0.9565 -0.1164 0.0926 -0.1570 62 LEU A CG 478 C CD1 . LEU A 62 ? 1.1656 1.4557 0.9753 -0.0963 0.0783 -0.1541 62 LEU A CD1 479 C CD2 . LEU A 62 ? 1.1952 1.4579 0.9491 -0.1252 0.1035 -0.1529 62 LEU A CD2 480 N N . GLY A 63 ? 1.1013 1.5190 0.9843 -0.1401 0.1048 -0.1943 63 GLY A N 481 C CA . GLY A 63 ? 1.0891 1.5462 0.9932 -0.1399 0.1061 -0.2072 63 GLY A CA 482 C C . GLY A 63 ? 1.0727 1.5394 0.9928 -0.1212 0.0948 -0.2104 63 GLY A C 483 O O . GLY A 63 ? 1.0897 1.5744 1.0106 -0.1202 0.0971 -0.2184 63 GLY A O 484 N N . ASN A 64 ? 1.0617 1.5161 0.9939 -0.1070 0.0830 -0.2046 64 ASN A N 485 C CA . ASN A 64 ? 1.0227 1.4866 0.9728 -0.0905 0.0723 -0.2086 64 ASN A CA 486 C C . ASN A 64 ? 1.0332 1.5336 1.0042 -0.0888 0.0736 -0.2212 64 ASN A C 487 O O . ASN A 64 ? 1.0549 1.5728 1.0411 -0.0918 0.0752 -0.2248 64 ASN A O 488 C CB . ASN A 64 ? 1.0041 1.4554 0.9690 -0.0796 0.0616 -0.2024 64 ASN A CB 489 C CG . ASN A 64 ? 0.9904 1.4487 0.9729 -0.0643 0.0512 -0.2069 64 ASN A CG 490 O OD1 . ASN A 64 ? 0.9672 1.4475 0.9612 -0.0601 0.0509 -0.2164 64 ASN A OD1 491 N ND2 . ASN A 64 ? 1.0155 1.4550 0.9995 -0.0561 0.0429 -0.2006 64 ASN A ND2 492 N N . PRO A 65 ? 1.0616 1.5743 1.0323 -0.0831 0.0728 -0.2285 65 PRO A N 493 C CA . PRO A 65 ? 1.0892 1.6378 1.0759 -0.0813 0.0754 -0.2412 65 PRO A CA 494 C C . PRO A 65 ? 1.0960 1.6601 1.1092 -0.0685 0.0671 -0.2458 65 PRO A C 495 O O . PRO A 65 ? 1.1021 1.6972 1.1285 -0.0672 0.0697 -0.2560 65 PRO A O 496 C CB . PRO A 65 ? 1.1029 1.6540 1.0816 -0.0751 0.0743 -0.2462 65 PRO A CB 497 C CG . PRO A 65 ? 1.1157 1.6349 1.0831 -0.0683 0.0667 -0.2370 65 PRO A CG 498 C CD . PRO A 65 ? 1.1053 1.6007 1.0605 -0.0770 0.0692 -0.2259 65 PRO A CD 499 N N . MET A 66 ? 1.1340 1.6768 1.1535 -0.0588 0.0577 -0.2387 66 MET A N 500 C CA . MET A 66 ? 1.1819 1.7314 1.2220 -0.0477 0.0507 -0.2408 66 MET A CA 501 C C . MET A 66 ? 1.1202 1.6746 1.1665 -0.0553 0.0539 -0.2379 66 MET A C 502 O O . MET A 66 ? 0.9903 1.5490 1.0516 -0.0465 0.0486 -0.2389 66 MET A O 503 C CB . MET A 66 ? 1.2325 1.7559 1.2754 -0.0371 0.0407 -0.2343 66 MET A CB 504 C CG . MET A 66 ? 1.2666 1.7861 1.3068 -0.0280 0.0358 -0.2388 66 MET A CG 505 S SD . MET A 66 ? 1.3815 1.9167 1.4376 -0.0118 0.0303 -0.2499 66 MET A SD 506 C CE . MET A 66 ? 1.4005 1.9213 1.4494 -0.0041 0.0244 -0.2526 66 MET A CE 507 N N . CYS A 67 ? 1.1438 1.6954 1.1765 -0.0716 0.0629 -0.2343 67 CYS A N 508 C CA . CYS A 67 ? 1.1823 1.7354 1.2176 -0.0810 0.0667 -0.2313 67 CYS A CA 509 C C . CYS A 67 ? 1.1708 1.7541 1.2054 -0.0951 0.0775 -0.2405 67 CYS A C 510 O O . CYS A 67 ? 1.1331 1.7115 1.1578 -0.1108 0.0852 -0.2374 67 CYS A O 511 C CB . CYS A 67 ? 1.2289 1.7471 1.2459 -0.0892 0.0683 -0.2183 67 CYS A CB 512 S SG . CYS A 67 ? 1.2965 1.7847 1.3176 -0.0743 0.0560 -0.2083 67 CYS A SG 513 N N . ASP A 68 ? 1.1780 1.7929 1.2226 -0.0897 0.0782 -0.2527 68 ASP A N 514 C CA . ASP A 68 ? 1.1773 1.8274 1.2235 -0.1027 0.0886 -0.2639 68 ASP A CA 515 C C . ASP A 68 ? 1.1592 1.8319 1.2208 -0.1055 0.0890 -0.2686 68 ASP A C 516 O O . ASP A 68 ? 1.1755 1.8711 1.2356 -0.1220 0.0990 -0.2754 68 ASP A O 517 C CB . ASP A 68 ? 1.2133 1.8941 1.2676 -0.0934 0.0883 -0.2765 68 ASP A CB 518 C CG . ASP A 68 ? 1.2849 1.9528 1.3203 -0.0981 0.0929 -0.2750 68 ASP A CG 519 O OD1 . ASP A 68 ? 1.3398 1.9733 1.3551 -0.1066 0.0953 -0.2639 68 ASP A OD1 520 O OD2 . ASP A 68 ? 1.2799 1.9718 1.3193 -0.0922 0.0939 -0.2853 68 ASP A OD2 521 N N . GLU A 69 ? 1.1072 1.7734 1.1827 -0.0901 0.0787 -0.2654 69 GLU A N 522 C CA . GLU A 69 ? 1.0640 1.7475 1.1525 -0.0912 0.0780 -0.2686 69 GLU A CA 523 C C . GLU A 69 ? 1.0522 1.7241 1.1283 -0.1133 0.0870 -0.2630 69 GLU A C 524 O O . GLU A 69 ? 1.0543 1.7522 1.1381 -0.1224 0.0915 -0.2703 69 GLU A O 525 C CB . GLU A 69 ? 1.0896 1.7547 1.1882 -0.0727 0.0662 -0.2622 69 GLU A CB 526 C CG . GLU A 69 ? 1.1131 1.7959 1.2249 -0.0703 0.0641 -0.2657 69 GLU A CG 527 C CD . GLU A 69 ? 1.1269 1.7852 1.2446 -0.0538 0.0537 -0.2578 69 GLU A CD 528 O OE1 . GLU A 69 ? 1.1812 1.8155 1.2961 -0.0422 0.0476 -0.2524 69 GLU A OE1 529 O OE2 . GLU A 69 ? 1.0531 1.7162 1.1775 -0.0533 0.0520 -0.2573 69 GLU A OE2 530 N N . PHE A 70 ? 1.0349 1.6678 1.0906 -0.1214 0.0895 -0.2508 70 PHE A N 531 C CA . PHE A 70 ? 1.0574 1.6698 1.0960 -0.1407 0.0977 -0.2437 70 PHE A CA 532 C C . PHE A 70 ? 1.0946 1.7036 1.1101 -0.1608 0.1110 -0.2455 70 PHE A C 533 O O . PHE A 70 ? 1.0670 1.6437 1.0587 -0.1742 0.1175 -0.2364 70 PHE A O 534 C CB . PHE A 70 ? 1.0386 1.6070 1.0679 -0.1339 0.0910 -0.2283 70 PHE A CB 535 C CG . PHE A 70 ? 1.0042 1.5727 1.0538 -0.1141 0.0786 -0.2264 70 PHE A CG 536 C CD1 . PHE A 70 ? 0.9831 1.5645 1.0464 -0.1127 0.0763 -0.2286 70 PHE A CD1 537 C CD2 . PHE A 70 ? 0.9653 1.5222 1.0194 -0.0974 0.0698 -0.2235 70 PHE A CD2 538 C CE1 . PHE A 70 ? 0.9552 1.5343 1.0342 -0.0945 0.0658 -0.2268 70 PHE A CE1 539 C CE2 . PHE A 70 ? 0.9544 1.5089 1.0244 -0.0807 0.0598 -0.2223 70 PHE A CE2 540 C CZ . PHE A 70 ? 0.9332 1.4977 1.0148 -0.0790 0.0580 -0.2236 70 PHE A CZ 541 N N . ILE A 71 ? 1.1277 1.7696 1.1489 -0.1625 0.1155 -0.2576 71 ILE A N 542 C CA . ILE A 71 ? 1.2163 1.8583 1.2159 -0.1819 0.1291 -0.2609 71 ILE A CA 543 C C . ILE A 71 ? 1.2227 1.8708 1.2124 -0.2072 0.1420 -0.2644 71 ILE A C 544 O O . ILE A 71 ? 1.2385 1.8622 1.1997 -0.2258 0.1536 -0.2602 71 ILE A O 545 C CB . ILE A 71 ? 1.2609 1.9412 1.2713 -0.1769 0.1309 -0.2744 71 ILE A CB 546 C CG1 . ILE A 71 ? 1.2849 1.9517 1.2684 -0.1910 0.1423 -0.2737 71 ILE A CG1 547 C CG2 . ILE A 71 ? 1.2540 1.9881 1.2870 -0.1812 0.1343 -0.2907 71 ILE A CG2 548 C CD1 . ILE A 71 ? 1.2649 1.8977 1.2350 -0.1769 0.1351 -0.2637 71 ILE A CD1 549 N N . ASN A 72 ? 1.2059 1.8845 1.2171 -0.2079 0.1401 -0.2722 72 ASN A N 550 C CA . ASN A 72 ? 1.2390 1.9230 1.2422 -0.2321 0.1514 -0.2758 72 ASN A CA 551 C C . ASN A 72 ? 1.1612 1.8567 1.1843 -0.2254 0.1436 -0.2765 72 ASN A C 552 O O . ASN A 72 ? 1.1887 1.9307 1.2365 -0.2211 0.1410 -0.2899 72 ASN A O 553 C CB . ASN A 72 ? 1.2791 2.0071 1.2846 -0.2511 0.1646 -0.2927 72 ASN A CB 554 C CG . ASN A 72 ? 1.3518 2.0532 1.3230 -0.2735 0.1799 -0.2895 72 ASN A CG 555 O OD1 . ASN A 72 ? 1.4062 2.0640 1.3498 -0.2874 0.1862 -0.2787 72 ASN A OD1 556 N ND2 . ASN A 72 ? 1.4043 2.1295 1.3748 -0.2765 0.1860 -0.2986 72 ASN A ND2 557 N N . VAL A 73 ? 1.1063 1.7592 1.1174 -0.2238 0.1397 -0.2623 73 VAL A N 558 C CA . VAL A 73 ? 1.0707 1.7277 1.0991 -0.2142 0.1309 -0.2606 73 VAL A CA 559 C C . VAL A 73 ? 1.0553 1.7170 1.0760 -0.2377 0.1409 -0.2646 73 VAL A C 560 O O . VAL A 73 ? 1.0782 1.7104 1.0706 -0.2582 0.1523 -0.2595 73 VAL A O 561 C CB . VAL A 73 ? 1.0549 1.6661 1.0774 -0.1977 0.1203 -0.2436 73 VAL A CB 562 C CG1 . VAL A 73 ? 1.0194 1.6244 1.0467 -0.1778 0.1118 -0.2404 73 VAL A CG1 563 C CG2 . VAL A 73 ? 1.0766 1.6397 1.0674 -0.2123 0.1274 -0.2309 73 VAL A CG2 564 N N . PRO A 74 ? 1.0260 1.7235 1.0699 -0.2347 0.1368 -0.2742 74 PRO A N 565 C CA . PRO A 74 ? 1.0490 1.7508 1.0867 -0.2565 0.1452 -0.2783 74 PRO A CA 566 C C . PRO A 74 ? 1.0789 1.7289 1.0986 -0.2575 0.1430 -0.2621 74 PRO A C 567 O O . PRO A 74 ? 1.0815 1.6936 1.0936 -0.2418 0.1354 -0.2479 74 PRO A O 568 C CB . PRO A 74 ? 1.0113 1.7660 1.0809 -0.2460 0.1378 -0.2924 74 PRO A CB 569 C CG . PRO A 74 ? 0.9755 1.7305 1.0623 -0.2142 0.1227 -0.2880 74 PRO A CG 570 C CD . PRO A 74 ? 0.9875 1.7227 1.0619 -0.2107 0.1245 -0.2824 74 PRO A CD 571 N N . GLU A 75 ? 1.1162 1.7665 1.1293 -0.2763 0.1499 -0.2653 75 GLU A N 572 C CA . GLU A 75 ? 1.0949 1.7006 1.0924 -0.2772 0.1479 -0.2518 75 GLU A CA 573 C C . GLU A 75 ? 1.0710 1.6747 1.0899 -0.2489 0.1315 -0.2449 75 GLU A C 574 O O . GLU A 75 ? 1.0411 1.6856 1.0877 -0.2349 0.1236 -0.2546 75 GLU A O 575 C CB . GLU A 75 ? 1.1145 1.7316 1.1067 -0.3012 0.1573 -0.2601 75 GLU A CB 576 C CG . GLU A 75 ? 1.1739 1.7416 1.1442 -0.3060 0.1578 -0.2467 75 GLU A CG 577 C CD . GLU A 75 ? 1.2044 1.7862 1.1724 -0.3283 0.1656 -0.2561 75 GLU A CD 578 O OE1 . GLU A 75 ? 1.2339 1.8525 1.2050 -0.3495 0.1762 -0.2719 75 GLU A OE1 579 O OE2 . GLU A 75 ? 1.2810 1.8377 1.2438 -0.3251 0.1614 -0.2481 75 GLU A OE2 580 N N . TRP A 76 ? 1.0720 1.6277 1.0765 -0.2402 0.1267 -0.2285 76 TRP A N 581 C CA . TRP A 76 ? 1.0654 1.6143 1.0872 -0.2156 0.1125 -0.2211 76 TRP A CA 582 C C . TRP A 76 ? 1.0912 1.6108 1.1032 -0.2188 0.1116 -0.2122 76 TRP A C 583 O O . TRP A 76 ? 1.1826 1.6746 1.1689 -0.2374 0.1212 -0.2080 76 TRP A O 584 C CB . TRP A 76 ? 1.0257 1.5498 1.0453 -0.1971 0.1051 -0.2105 76 TRP A CB 585 C CG . TRP A 76 ? 1.0380 1.5142 1.0270 -0.2041 0.1102 -0.1976 76 TRP A CG 586 C CD1 . TRP A 76 ? 1.0680 1.5040 1.0434 -0.1990 0.1070 -0.1842 76 TRP A CD1 587 C CD2 . TRP A 76 ? 1.0568 1.5201 1.0232 -0.2158 0.1193 -0.1973 76 TRP A CD2 588 N NE1 . TRP A 76 ? 1.0769 1.4761 1.0222 -0.2057 0.1129 -0.1756 76 TRP A NE1 589 C CE2 . TRP A 76 ? 1.0462 1.4599 0.9845 -0.2161 0.1207 -0.1831 76 TRP A CE2 590 C CE3 . TRP A 76 ? 1.0642 1.5532 1.0303 -0.2256 0.1267 -0.2078 76 TRP A CE3 591 C CZ2 . TRP A 76 ? 1.0740 1.4612 0.9824 -0.2249 0.1287 -0.1789 76 TRP A CZ2 592 C CZ3 . TRP A 76 ? 1.0654 1.5279 1.0025 -0.2359 0.1353 -0.2034 76 TRP A CZ3 593 C CH2 . TRP A 76 ? 1.0766 1.4877 0.9843 -0.2351 0.1362 -0.1889 76 TRP A CH2 594 N N . SER A 77 ? 1.0467 1.5710 1.0773 -0.2003 0.1005 -0.2095 77 SER A N 595 C CA . SER A 77 ? 1.0423 1.5386 1.0656 -0.1995 0.0980 -0.2003 77 SER A CA 596 C C . SER A 77 ? 1.0362 1.4877 1.0471 -0.1868 0.0930 -0.1839 77 SER A C 597 O O . SER A 77 ? 1.0728 1.4876 1.0614 -0.1941 0.0969 -0.1743 77 SER A O 598 C CB . SER A 77 ? 1.0211 1.5443 1.0690 -0.1856 0.0889 -0.2057 77 SER A CB 599 O OG . SER A 77 ? 1.0051 1.5454 1.0728 -0.1636 0.0793 -0.2076 77 SER A OG 600 N N . TYR A 78 ? 0.9820 1.4377 1.0071 -0.1675 0.0844 -0.1817 78 TYR A N 601 C CA . TYR A 78 ? 0.9566 1.3771 0.9727 -0.1556 0.0796 -0.1686 78 TYR A CA 602 C C . TYR A 78 ? 0.9412 1.3734 0.9660 -0.1452 0.0760 -0.1714 78 TYR A C 603 O O . TYR A 78 ? 0.8925 1.3593 0.9323 -0.1439 0.0758 -0.1826 78 TYR A O 604 C CB . TYR A 78 ? 0.9223 1.3289 0.9485 -0.1400 0.0706 -0.1607 78 TYR A CB 605 C CG . TYR A 78 ? 0.8679 1.3034 0.9205 -0.1250 0.0624 -0.1675 78 TYR A CG 606 C CD1 . TYR A 78 ? 0.8451 1.3081 0.9085 -0.1283 0.0628 -0.1768 78 TYR A CD1 607 C CD2 . TYR A 78 ? 0.8267 1.2607 0.8912 -0.1071 0.0545 -0.1652 78 TYR A CD2 608 C CE1 . TYR A 78 ? 0.8193 1.3064 0.9031 -0.1122 0.0550 -0.1830 78 TYR A CE1 609 C CE2 . TYR A 78 ? 0.8015 1.2566 0.8852 -0.0926 0.0477 -0.1711 78 TYR A CE2 610 C CZ . TYR A 78 ? 0.8008 1.2817 0.8933 -0.0941 0.0477 -0.1797 78 TYR A CZ 611 O OH . TYR A 78 ? 0.7769 1.2763 0.8850 -0.0774 0.0405 -0.1855 78 TYR A OH 612 N N . ILE A 79 ? 0.9594 1.3639 0.9744 -0.1372 0.0729 -0.1617 79 ILE A N 613 C CA . ILE A 79 ? 0.9453 1.3570 0.9673 -0.1268 0.0688 -0.1636 79 ILE A CA 614 C C . ILE A 79 ? 0.9600 1.3633 0.9967 -0.1075 0.0582 -0.1581 79 ILE A C 615 O O . ILE A 79 ? 0.9064 1.2856 0.9384 -0.1034 0.0554 -0.1488 79 ILE A O 616 C CB . ILE A 79 ? 0.9865 1.3745 0.9841 -0.1333 0.0739 -0.1582 79 ILE A CB 617 C CG1 . ILE A 79 ? 1.0164 1.4107 0.9968 -0.1540 0.0859 -0.1641 79 ILE A CG1 618 C CG2 . ILE A 79 ? 1.0138 1.4080 1.0186 -0.1216 0.0687 -0.1598 79 ILE A CG2 619 C CD1 . ILE A 79 ? 1.0497 1.4111 0.9979 -0.1618 0.0925 -0.1569 79 ILE A CD1 620 N N . VAL A 80 ? 0.9625 1.3847 1.0153 -0.0962 0.0530 -0.1643 80 VAL A N 621 C CA . VAL A 80 ? 0.9362 1.3498 1.0013 -0.0796 0.0441 -0.1605 80 VAL A CA 622 C C . VAL A 80 ? 0.9455 1.3567 1.0098 -0.0734 0.0415 -0.1613 80 VAL A C 623 O O . VAL A 80 ? 0.9757 1.4080 1.0468 -0.0709 0.0415 -0.1700 80 VAL A O 624 C CB . VAL A 80 ? 0.9274 1.3623 1.0114 -0.0690 0.0393 -0.1675 80 VAL A CB 625 C CG1 . VAL A 80 ? 0.9228 1.3437 1.0155 -0.0536 0.0316 -0.1635 80 VAL A CG1 626 C CG2 . VAL A 80 ? 0.9198 1.3601 1.0054 -0.0742 0.0412 -0.1679 80 VAL A CG2 627 N N . GLU A 81 ? 0.9685 1.3551 1.0244 -0.0704 0.0391 -0.1527 81 GLU A N 628 C CA . GLU A 81 ? 0.9818 1.3645 1.0365 -0.0643 0.0358 -0.1531 81 GLU A CA 629 C C . GLU A 81 ? 0.9241 1.2990 0.9919 -0.0519 0.0282 -0.1508 81 GLU A C 630 O O . GLU A 81 ? 0.9246 1.2885 0.9958 -0.0495 0.0264 -0.1453 81 GLU A O 631 C CB . GLU A 81 ? 1.0573 1.4189 1.0906 -0.0699 0.0386 -0.1460 81 GLU A CB 632 C CG . GLU A 81 ? 1.1439 1.5037 1.1721 -0.0654 0.0362 -0.1474 81 GLU A CG 633 C CD . GLU A 81 ? 1.2387 1.5753 1.2440 -0.0674 0.0376 -0.1397 81 GLU A CD 634 O OE1 . GLU A 81 ? 1.1980 1.5167 1.1959 -0.0673 0.0374 -0.1319 81 GLU A OE1 635 O OE2 . GLU A 81 ? 1.2681 1.6037 1.2615 -0.0679 0.0387 -0.1415 81 GLU A OE2 636 N N . LYS A 82 ? 0.9642 1.3440 1.0384 -0.0447 0.0243 -0.1553 82 LYS A N 637 C CA . LYS A 82 ? 0.9758 1.3455 1.0598 -0.0352 0.0183 -0.1536 82 LYS A CA 638 C C . LYS A 82 ? 1.0200 1.3724 1.0967 -0.0355 0.0163 -0.1465 82 LYS A C 639 O O . LYS A 82 ? 1.0020 1.3487 1.0640 -0.0408 0.0190 -0.1429 82 LYS A O 640 C CB . LYS A 82 ? 0.9766 1.3560 1.0686 -0.0279 0.0151 -0.1618 82 LYS A CB 641 C CG . LYS A 82 ? 0.9687 1.3648 1.0685 -0.0235 0.0156 -0.1691 82 LYS A CG 642 C CD . LYS A 82 ? 0.9849 1.3835 1.0907 -0.0135 0.0118 -0.1762 82 LYS A CD 643 C CE . LYS A 82 ? 1.0240 1.4431 1.1342 -0.0075 0.0124 -0.1851 82 LYS A CE 644 N NZ . LYS A 82 ? 1.0749 1.4996 1.1890 -0.0065 0.0132 -0.1840 82 LYS A NZ 645 N N . ALA A 83 ? 1.0565 1.4005 1.1422 -0.0294 0.0118 -0.1448 83 ALA A N 646 C CA . ALA A 83 ? 1.0644 1.3969 1.1460 -0.0282 0.0092 -0.1397 83 ALA A CA 647 C C . ALA A 83 ? 1.1028 1.4397 1.1792 -0.0271 0.0071 -0.1438 83 ALA A C 648 O O . ALA A 83 ? 1.1562 1.4873 1.2203 -0.0277 0.0068 -0.1400 83 ALA A O 649 C CB . ALA A 83 ? 1.0061 1.3316 1.0999 -0.0237 0.0059 -0.1386 83 ALA A CB 650 N N . ASN A 84 ? 1.0816 1.4277 1.1654 -0.0244 0.0055 -0.1516 84 ASN A N 651 C CA . ASN A 84 ? 1.1033 1.4546 1.1826 -0.0232 0.0034 -0.1565 84 ASN A CA 652 C C . ASN A 84 ? 1.0770 1.4410 1.1562 -0.0233 0.0054 -0.1639 84 ASN A C 653 O O . ASN A 84 ? 1.0597 1.4277 1.1469 -0.0189 0.0030 -0.1706 84 ASN A O 654 C CB . ASN A 84 ? 1.1755 1.5241 1.2641 -0.0192 -0.0017 -0.1595 84 ASN A CB 655 C CG . ASN A 84 ? 1.2648 1.6064 1.3516 -0.0187 -0.0041 -0.1538 84 ASN A CG 656 O OD1 . ASN A 84 ? 1.3328 1.6750 1.4090 -0.0177 -0.0057 -0.1525 84 ASN A OD1 657 N ND2 . ASN A 84 ? 1.3043 1.6394 1.4001 -0.0185 -0.0042 -0.1504 84 ASN A ND2 658 N N . PRO A 85 ? 1.0713 1.4412 1.1401 -0.0288 0.0105 -0.1633 85 PRO A N 659 C CA . PRO A 85 ? 1.0602 1.4461 1.1296 -0.0294 0.0132 -0.1712 85 PRO A CA 660 C C . PRO A 85 ? 1.0794 1.4690 1.1449 -0.0265 0.0108 -0.1766 85 PRO A C 661 O O . PRO A 85 ? 1.0863 1.4680 1.1412 -0.0275 0.0096 -0.1732 85 PRO A O 662 C CB . PRO A 85 ? 1.0669 1.4563 1.1236 -0.0387 0.0202 -0.1686 85 PRO A CB 663 C CG . PRO A 85 ? 1.0490 1.4212 1.0980 -0.0420 0.0208 -0.1590 85 PRO A CG 664 C CD . PRO A 85 ? 1.0482 1.4093 1.1017 -0.0350 0.0144 -0.1560 85 PRO A CD 665 N N . VAL A 86 ? 1.0863 1.4871 1.1587 -0.0219 0.0098 -0.1851 86 VAL A N 666 C CA . VAL A 86 ? 1.1163 1.5201 1.1854 -0.0187 0.0072 -0.1910 86 VAL A CA 667 C C . VAL A 86 ? 1.0948 1.5064 1.1494 -0.0239 0.0117 -0.1923 86 VAL A C 668 O O . VAL A 86 ? 1.1227 1.5303 1.1682 -0.0232 0.0097 -0.1927 86 VAL A O 669 C CB . VAL A 86 ? 1.1264 1.5367 1.2048 -0.0111 0.0049 -0.2000 86 VAL A CB 670 C CG1 . VAL A 86 ? 1.1383 1.5364 1.2270 -0.0065 0.0015 -0.1986 86 VAL A CG1 671 C CG2 . VAL A 86 ? 1.1163 1.5451 1.1954 -0.0104 0.0092 -0.2058 86 VAL A CG2 672 N N . ASN A 87 ? 1.0171 1.4399 1.0688 -0.0295 0.0181 -0.1933 87 ASN A N 673 C CA . ASN A 87 ? 1.0140 1.4446 1.0512 -0.0363 0.0241 -0.1954 87 ASN A CA 674 C C . ASN A 87 ? 1.0277 1.4437 1.0472 -0.0449 0.0286 -0.1866 87 ASN A C 675 O O . ASN A 87 ? 1.0106 1.4293 1.0258 -0.0535 0.0351 -0.1847 87 ASN A O 676 C CB . ASN A 87 ? 1.0038 1.4575 1.0469 -0.0390 0.0295 -0.2031 87 ASN A CB 677 C CG . ASN A 87 ? 0.9928 1.4598 1.0485 -0.0284 0.0254 -0.2125 87 ASN A CG 678 O OD1 . ASN A 87 ? 1.0294 1.4935 1.0826 -0.0231 0.0219 -0.2160 87 ASN A OD1 679 N ND2 . ASN A 87 ? 0.9821 1.4629 1.0500 -0.0244 0.0255 -0.2170 87 ASN A ND2 680 N N . ASP A 88 ? 1.0824 1.4825 1.0903 -0.0421 0.0251 -0.1818 88 ASP A N 681 C CA . ASP A 88 ? 1.1081 1.4896 1.0947 -0.0472 0.0284 -0.1731 88 ASP A CA 682 C C . ASP A 88 ? 1.1223 1.5015 1.0868 -0.0500 0.0325 -0.1749 88 ASP A C 683 O O . ASP A 88 ? 1.0758 1.4653 1.0343 -0.0583 0.0404 -0.1790 88 ASP A O 684 C CB . ASP A 88 ? 1.1562 1.5227 1.1448 -0.0397 0.0209 -0.1668 88 ASP A CB 685 C CG . ASP A 88 ? 1.2044 1.5496 1.1702 -0.0421 0.0235 -0.1573 88 ASP A CG 686 O OD1 . ASP A 88 ? 1.1695 1.5080 1.1233 -0.0513 0.0313 -0.1537 88 ASP A OD1 687 O OD2 . ASP A 88 ? 1.2884 1.6233 1.2476 -0.0344 0.0177 -0.1538 88 ASP A OD2 688 N N . LEU A 89 ? 1.1398 1.5075 1.0925 -0.0431 0.0274 -0.1726 89 LEU A N 689 C CA . LEU A 89 ? 1.1533 1.5163 1.0828 -0.0439 0.0304 -0.1738 89 LEU A CA 690 C C . LEU A 89 ? 1.1474 1.5254 1.0883 -0.0367 0.0247 -0.1826 89 LEU A C 691 O O . LEU A 89 ? 1.1414 1.5159 1.0836 -0.0279 0.0165 -0.1830 89 LEU A O 692 C CB . LEU A 89 ? 1.1628 1.5020 1.0674 -0.0390 0.0281 -0.1657 89 LEU A CB 693 C CG . LEU A 89 ? 1.1631 1.4813 1.0505 -0.0446 0.0334 -0.1562 89 LEU A CG 694 C CD1 . LEU A 89 ? 1.1737 1.4680 1.0328 -0.0365 0.0305 -0.1492 89 LEU A CD1 695 C CD2 . LEU A 89 ? 1.1807 1.4973 1.0544 -0.0594 0.0459 -0.1565 89 LEU A CD2 696 N N . CYS A 90 ? 1.2078 1.6037 1.1566 -0.0405 0.0291 -0.1904 90 CYS A N 697 C CA . CYS A 90 ? 1.2093 1.6191 1.1675 -0.0339 0.0246 -0.1995 90 CYS A CA 698 C C . CYS A 90 ? 1.1447 1.5449 1.0859 -0.0280 0.0201 -0.1992 90 CYS A C 699 O O . CYS A 90 ? 1.1480 1.5508 1.0996 -0.0199 0.0115 -0.2031 90 CYS A O 700 C CB . CYS A 90 ? 1.2901 1.7191 1.2499 -0.0393 0.0321 -0.2073 90 CYS A CB 701 S SG . CYS A 90 ? 1.4194 1.8451 1.3509 -0.0526 0.0453 -0.2052 90 CYS A SG 702 N N . TYR A 91 ? 1.1009 1.4890 1.0143 -0.0323 0.0261 -0.1948 91 TYR A N 703 C CA . TYR A 91 ? 1.1083 1.4841 1.0006 -0.0252 0.0217 -0.1931 91 TYR A CA 704 C C . TYR A 91 ? 1.0893 1.4474 0.9748 -0.0205 0.0169 -0.1843 91 TYR A C 705 O O . TYR A 91 ? 1.1101 1.4542 0.9835 -0.0265 0.0229 -0.1768 91 TYR A O 706 C CB . TYR A 91 ? 1.1342 1.5010 0.9955 -0.0312 0.0310 -0.1919 91 TYR A CB 707 C CG . TYR A 91 ? 1.1391 1.4966 0.9782 -0.0224 0.0265 -0.1925 91 TYR A CG 708 C CD1 . TYR A 91 ? 1.1641 1.5017 0.9838 -0.0145 0.0214 -0.1853 91 TYR A CD1 709 C CD2 . TYR A 91 ? 1.1423 1.5116 0.9787 -0.0209 0.0270 -0.2006 91 TYR A CD2 710 C CE1 . TYR A 91 ? 1.1748 1.5052 0.9730 -0.0048 0.0166 -0.1864 91 TYR A CE1 711 C CE2 . TYR A 91 ? 1.1521 1.5131 0.9671 -0.0123 0.0226 -0.2014 91 TYR A CE2 712 C CZ . TYR A 91 ? 1.1390 1.4809 0.9350 -0.0041 0.0172 -0.1944 91 TYR A CZ 713 O OH . TYR A 91 ? 1.1367 1.4714 0.9105 0.0061 0.0120 -0.1956 91 TYR A OH 714 N N . PRO A 92 ? 1.0927 1.4525 0.9854 -0.0100 0.0063 -0.1861 92 PRO A N 715 C CA . PRO A 92 ? 1.0768 1.4254 0.9680 -0.0044 0.0010 -0.1792 92 PRO A CA 716 C C . PRO A 92 ? 1.1225 1.4474 0.9782 -0.0024 0.0047 -0.1705 92 PRO A C 717 O O . PRO A 92 ? 1.1564 1.4730 0.9864 -0.0018 0.0082 -0.1708 92 PRO A O 718 C CB . PRO A 92 ? 1.0727 1.4324 0.9761 0.0057 -0.0103 -0.1857 92 PRO A CB 719 C CG . PRO A 92 ? 1.1068 1.4726 0.9996 0.0072 -0.0100 -0.1925 92 PRO A CG 720 C CD . PRO A 92 ? 1.1038 1.4754 1.0017 -0.0028 -0.0007 -0.1948 92 PRO A CD 721 N N . GLY A 93 ? 1.2014 1.5132 1.0536 -0.0009 0.0041 -0.1627 93 GLY A N 722 C CA . GLY A 93 ? 1.2623 1.5472 1.0781 0.0022 0.0075 -0.1538 93 GLY A CA 723 C C . GLY A 93 ? 1.2700 1.5422 1.0870 0.0007 0.0090 -0.1458 93 GLY A C 724 O O . GLY A 93 ? 1.1989 1.4847 1.0455 0.0014 0.0041 -0.1473 93 GLY A O 725 N N . ASP A 94 ? 1.3274 1.5714 1.1101 -0.0017 0.0163 -0.1375 94 ASP A N 726 C CA . ASP A 94 ? 1.3506 1.5781 1.1285 -0.0029 0.0184 -0.1294 94 ASP A CA 727 C C . ASP A 94 ? 1.3418 1.5503 1.0993 -0.0188 0.0321 -0.1249 94 ASP A C 728 O O . ASP A 94 ? 1.3605 1.5656 1.1018 -0.0276 0.0402 -0.1273 94 ASP A O 729 C CB . ASP A 94 ? 1.4459 1.6530 1.1969 0.0133 0.0122 -0.1233 94 ASP A CB 730 C CG . ASP A 94 ? 1.5371 1.7489 1.3074 0.0201 0.0055 -0.1204 94 ASP A CG 731 O OD1 . ASP A 94 ? 1.5418 1.7795 1.3433 0.0265 -0.0040 -0.1266 94 ASP A OD1 732 O OD2 . ASP A 94 ? 1.6190 1.8084 1.3730 0.0183 0.0101 -0.1125 94 ASP A OD2 733 N N . PHE A 95 ? 1.2542 1.4515 1.0131 -0.0230 0.0349 -0.1190 95 PHE A N 734 C CA . PHE A 95 ? 1.1793 1.3580 0.9191 -0.0389 0.0477 -0.1150 95 PHE A CA 735 C C . PHE A 95 ? 1.1969 1.3420 0.9074 -0.0330 0.0485 -0.1051 95 PHE A C 736 O O . PHE A 95 ? 1.2171 1.3652 0.9447 -0.0278 0.0431 -0.1023 95 PHE A O 737 C CB . PHE A 95 ? 1.1224 1.3253 0.8984 -0.0507 0.0501 -0.1194 95 PHE A CB 738 C CG . PHE A 95 ? 1.1576 1.3544 0.9213 -0.0698 0.0636 -0.1199 95 PHE A CG 739 C CD1 . PHE A 95 ? 1.2368 1.4013 0.9683 -0.0772 0.0720 -0.1124 95 PHE A CD1 740 C CD2 . PHE A 95 ? 1.1904 1.4145 0.9741 -0.0807 0.0683 -0.1287 95 PHE A CD2 741 C CE1 . PHE A 95 ? 1.2668 1.4272 0.9873 -0.0972 0.0852 -0.1142 95 PHE A CE1 742 C CE2 . PHE A 95 ? 1.1980 1.4215 0.9723 -0.0993 0.0809 -0.1308 95 PHE A CE2 743 C CZ . PHE A 95 ? 1.2411 1.4330 0.9840 -0.1086 0.0897 -0.1238 95 PHE A CZ 744 N N . ASN A 96 ? 1.2375 1.3485 0.9016 -0.0334 0.0554 -0.0998 96 ASN A N 745 C CA . ASN A 96 ? 1.2791 1.3532 0.9081 -0.0244 0.0556 -0.0903 96 ASN A CA 746 C C . ASN A 96 ? 1.2790 1.3402 0.9082 -0.0374 0.0632 -0.0859 96 ASN A C 747 O O . ASN A 96 ? 1.2733 1.3358 0.9028 -0.0573 0.0743 -0.0884 96 ASN A O 748 C CB . ASN A 96 ? 1.3782 1.4146 0.9525 -0.0227 0.0628 -0.0859 96 ASN A CB 749 C CG . ASN A 96 ? 1.4446 1.4471 0.9820 -0.0030 0.0576 -0.0776 96 ASN A CG 750 O OD1 . ASN A 96 ? 1.4278 1.4457 0.9803 0.0166 0.0443 -0.0786 96 ASN A OD1 751 N ND2 . ASN A 96 ? 1.5308 1.4868 1.0182 -0.0081 0.0684 -0.0700 96 ASN A ND2 752 N N . ASP A 97 ? 1.3146 1.3651 0.9438 -0.0261 0.0571 -0.0802 97 ASP A N 753 C CA . ASP A 97 ? 1.2959 1.3328 0.9248 -0.0360 0.0630 -0.0757 97 ASP A CA 754 C C . ASP A 97 ? 1.2145 1.2841 0.8854 -0.0525 0.0659 -0.0821 97 ASP A C 755 O O . ASP A 97 ? 1.2162 1.2763 0.8803 -0.0695 0.0759 -0.0815 97 ASP A O 756 C CB . ASP A 97 ? 1.4036 1.3937 0.9795 -0.0465 0.0763 -0.0693 97 ASP A CB 757 C CG . ASP A 97 ? 1.5338 1.4837 1.0641 -0.0274 0.0732 -0.0609 97 ASP A CG 758 O OD1 . ASP A 97 ? 1.6115 1.5707 1.1546 -0.0071 0.0608 -0.0593 97 ASP A OD1 759 O OD2 . ASP A 97 ? 1.6390 1.5471 1.1186 -0.0328 0.0836 -0.0562 97 ASP A OD2 760 N N . TYR A 98 ? 1.1434 1.2511 0.8565 -0.0470 0.0569 -0.0888 98 TYR A N 761 C CA . TYR A 98 ? 1.1189 1.2587 0.8701 -0.0597 0.0587 -0.0959 98 TYR A CA 762 C C . TYR A 98 ? 1.1382 1.2773 0.9037 -0.0647 0.0597 -0.0930 98 TYR A C 763 O O . TYR A 98 ? 1.0898 1.2380 0.8651 -0.0802 0.0669 -0.0963 98 TYR A O 764 C CB . TYR A 98 ? 1.0804 1.2543 0.8683 -0.0498 0.0481 -0.1028 98 TYR A CB 765 C CG . TYR A 98 ? 1.0477 1.2539 0.8729 -0.0589 0.0487 -0.1106 98 TYR A CG 766 C CD1 . TYR A 98 ? 1.0583 1.2726 0.8815 -0.0746 0.0584 -0.1156 98 TYR A CD1 767 C CD2 . TYR A 98 ? 1.0453 1.2741 0.9064 -0.0512 0.0398 -0.1137 98 TYR A CD2 768 C CE1 . TYR A 98 ? 1.0567 1.3021 0.9130 -0.0801 0.0580 -0.1234 98 TYR A CE1 769 C CE2 . TYR A 98 ? 1.0245 1.2795 0.9160 -0.0571 0.0399 -0.1207 98 TYR A CE2 770 C CZ . TYR A 98 ? 1.0513 1.3153 0.9406 -0.0704 0.0485 -0.1256 98 TYR A CZ 771 O OH . TYR A 98 ? 1.0962 1.3875 1.0146 -0.0736 0.0480 -0.1331 98 TYR A OH 772 N N . GLU A 99 ? 1.2122 1.3413 0.9778 -0.0511 0.0524 -0.0873 99 GLU A N 773 C CA . GLU A 99 ? 1.2010 1.3294 0.9809 -0.0532 0.0520 -0.0841 99 GLU A CA 774 C C . GLU A 99 ? 1.2169 1.3126 0.9630 -0.0651 0.0628 -0.0786 99 GLU A C 775 O O . GLU A 99 ? 1.2231 1.3230 0.9812 -0.0758 0.0668 -0.0791 99 GLU A O 776 C CB . GLU A 99 ? 1.2495 1.3783 1.0389 -0.0350 0.0414 -0.0803 99 GLU A CB 777 C CG . GLU A 99 ? 1.2461 1.4082 1.0720 -0.0258 0.0314 -0.0867 99 GLU A CG 778 C CD . GLU A 99 ? 1.3199 1.4859 1.1355 -0.0175 0.0274 -0.0900 99 GLU A CD 779 O OE1 . GLU A 99 ? 1.3944 1.5347 1.1727 -0.0125 0.0297 -0.0856 99 GLU A OE1 780 O OE2 . GLU A 99 ? 1.3599 1.5531 1.2028 -0.0155 0.0220 -0.0972 99 GLU A OE2 781 N N . GLU A 100 ? 1.2430 1.3050 0.9451 -0.0635 0.0678 -0.0738 100 GLU A N 782 C CA . GLU A 100 ? 1.2524 1.2790 0.9170 -0.0775 0.0800 -0.0693 100 GLU A CA 783 C C . GLU A 100 ? 1.2331 1.2732 0.9032 -0.1010 0.0911 -0.0763 100 GLU A C 784 O O . GLU A 100 ? 1.3224 1.3470 0.9778 -0.1171 0.1009 -0.0756 100 GLU A O 785 C CB . GLU A 100 ? 1.3144 1.2973 0.9257 -0.0695 0.0834 -0.0624 100 GLU A CB 786 C CG . GLU A 100 ? 1.3840 1.3428 0.9778 -0.0494 0.0761 -0.0542 100 GLU A CG 787 C CD . GLU A 100 ? 1.3872 1.3235 0.9704 -0.0563 0.0813 -0.0492 100 GLU A CD 788 O OE1 . GLU A 100 ? 1.4048 1.3137 0.9583 -0.0744 0.0940 -0.0480 100 GLU A OE1 789 O OE2 . GLU A 100 ? 1.3454 1.2908 0.9488 -0.0441 0.0730 -0.0468 100 GLU A OE2 790 N N . LEU A 101 ? 1.2020 1.2724 0.8935 -0.1031 0.0896 -0.0839 101 LEU A N 791 C CA . LEU A 101 ? 1.2194 1.3098 0.9204 -0.1239 0.0993 -0.0922 101 LEU A CA 792 C C . LEU A 101 ? 1.1539 1.2780 0.8971 -0.1292 0.0965 -0.0978 101 LEU A C 793 O O . LEU A 101 ? 1.1088 1.2362 0.8512 -0.1468 0.1053 -0.1013 101 LEU A O 794 C CB . LEU A 101 ? 1.2528 1.3636 0.9603 -0.1229 0.0987 -0.0987 101 LEU A CB 795 C CG . LEU A 101 ? 1.2689 1.4048 0.9869 -0.1428 0.1085 -0.1085 101 LEU A CG 796 C CD1 . LEU A 101 ? 1.2980 1.4083 0.9822 -0.1647 0.1240 -0.1077 101 LEU A CD1 797 C CD2 . LEU A 101 ? 1.3125 1.4614 1.0295 -0.1395 0.1080 -0.1135 101 LEU A CD2 798 N N . LYS A 102 ? 1.1187 1.2675 0.8971 -0.1143 0.0844 -0.0990 102 LYS A N 799 C CA . LYS A 102 ? 1.0960 1.2711 0.9108 -0.1157 0.0806 -0.1027 102 LYS A CA 800 C C . LYS A 102 ? 1.1078 1.2624 0.9102 -0.1230 0.0852 -0.0977 102 LYS A C 801 O O . LYS A 102 ? 1.1158 1.2872 0.9341 -0.1343 0.0888 -0.1026 102 LYS A O 802 C CB . LYS A 102 ? 1.1013 1.2928 0.9461 -0.0975 0.0676 -0.1022 102 LYS A CB 803 C CG . LYS A 102 ? 1.1418 1.3640 1.0119 -0.0929 0.0627 -0.1102 102 LYS A CG 804 C CD . LYS A 102 ? 1.1705 1.4022 1.0635 -0.0762 0.0510 -0.1093 102 LYS A CD 805 C CE . LYS A 102 ? 1.2235 1.4872 1.1487 -0.0739 0.0466 -0.1181 102 LYS A CE 806 N NZ . LYS A 102 ? 1.2876 1.5583 1.2299 -0.0598 0.0366 -0.1185 102 LYS A NZ 807 N N . HIS A 103 ? 1.1370 1.2558 0.9102 -0.1156 0.0847 -0.0884 103 HIS A N 808 C CA . HIS A 103 ? 1.1665 1.2619 0.9241 -0.1219 0.0893 -0.0833 103 HIS A CA 809 C C . HIS A 103 ? 1.2219 1.3068 0.9570 -0.1453 0.1033 -0.0870 103 HIS A C 810 O O . HIS A 103 ? 1.2491 1.3332 0.9867 -0.1565 0.1077 -0.0880 103 HIS A O 811 C CB . HIS A 103 ? 1.2010 1.2578 0.9271 -0.1081 0.0865 -0.0730 103 HIS A CB 812 C CG . HIS A 103 ? 1.2330 1.2636 0.9416 -0.1133 0.0910 -0.0676 103 HIS A CG 813 N ND1 . HIS A 103 ? 1.1912 1.2329 0.9250 -0.1067 0.0846 -0.0660 103 HIS A ND1 814 C CD2 . HIS A 103 ? 1.2653 1.2581 0.9327 -0.1255 0.1018 -0.0640 103 HIS A CD2 815 C CE1 . HIS A 103 ? 1.2113 1.2243 0.9210 -0.1137 0.0907 -0.0615 103 HIS A CE1 816 N NE2 . HIS A 103 ? 1.2716 1.2540 0.9405 -0.1255 0.1012 -0.0603 103 HIS A NE2 817 N N . LEU A 104 ? 1.2778 1.3554 0.9906 -0.1536 0.1106 -0.0895 104 LEU A N 818 C CA . LEU A 104 ? 1.3262 1.3974 1.0185 -0.1783 0.1252 -0.0946 104 LEU A CA 819 C C . LEU A 104 ? 1.3091 1.4271 1.0402 -0.1910 0.1266 -0.1063 104 LEU A C 820 O O . LEU A 104 ? 1.3380 1.4564 1.0631 -0.2101 0.1359 -0.1107 104 LEU A O 821 C CB . LEU A 104 ? 1.3522 1.4077 1.0136 -0.1833 0.1326 -0.0952 104 LEU A CB 822 C CG . LEU A 104 ? 1.3973 1.4094 1.0068 -0.2020 0.1483 -0.0925 104 LEU A CG 823 C CD1 . LEU A 104 ? 1.4238 1.3856 0.9967 -0.1927 0.1477 -0.0809 104 LEU A CD1 824 C CD2 . LEU A 104 ? 1.4437 1.4453 1.0272 -0.2050 0.1545 -0.0937 104 LEU A CD2 825 N N . LEU A 105 ? 1.2785 1.4350 1.0479 -0.1797 0.1172 -0.1116 105 LEU A N 826 C CA . LEU A 105 ? 1.2596 1.4616 1.0658 -0.1870 0.1168 -0.1229 105 LEU A CA 827 C C . LEU A 105 ? 1.2720 1.4852 1.0999 -0.1862 0.1127 -0.1233 105 LEU A C 828 O O . LEU A 105 ? 1.2470 1.4946 1.0990 -0.1943 0.1140 -0.1330 105 LEU A O 829 C CB . LEU A 105 ? 1.2250 1.4594 1.0625 -0.1725 0.1072 -0.1276 105 LEU A CB 830 C CG . LEU A 105 ? 1.2316 1.4703 1.0580 -0.1749 0.1111 -0.1315 105 LEU A CG 831 C CD1 . LEU A 105 ? 1.2140 1.4879 1.0755 -0.1610 0.1013 -0.1376 105 LEU A CD1 832 C CD2 . LEU A 105 ? 1.2681 1.5153 1.0808 -0.1985 0.1253 -0.1397 105 LEU A CD2 833 N N . SER A 106 ? 1.3267 1.5134 1.1471 -0.1750 0.1072 -0.1134 106 SER A N 834 C CA A SER A 106 ? 1.3370 1.5292 1.1736 -0.1741 0.1038 -0.1126 106 SER A CA 835 C CA B SER A 106 ? 1.3198 1.5127 1.1569 -0.1741 0.1038 -0.1128 106 SER A CA 836 C C . SER A 106 ? 1.3505 1.5319 1.1671 -0.1960 0.1154 -0.1157 106 SER A C 837 O O . SER A 106 ? 1.3519 1.5454 1.1832 -0.1999 0.1145 -0.1185 106 SER A O 838 C CB A SER A 106 ? 1.3524 1.5175 1.1831 -0.1569 0.0959 -0.1013 106 SER A CB 839 C CB B SER A 106 ? 1.3152 1.4828 1.1483 -0.1564 0.0954 -0.1017 106 SER A CB 840 O OG A SER A 106 ? 1.4025 1.5239 1.1919 -0.1615 0.1025 -0.0934 106 SER A OG 841 O OG B SER A 106 ? 1.2639 1.4428 1.1148 -0.1385 0.0856 -0.1002 106 SER A OG 842 N N . ARG A 107 ? 1.4316 1.5889 1.2128 -0.2107 0.1268 -0.1155 107 ARG A N 843 C CA . ARG A 107 ? 1.4687 1.6116 1.2255 -0.2348 0.1399 -0.1190 107 ARG A CA 844 C C . ARG A 107 ? 1.3702 1.5424 1.1308 -0.2552 0.1500 -0.1318 107 ARG A C 845 O O . ARG A 107 ? 1.3360 1.4951 1.0715 -0.2786 0.1633 -0.1360 107 ARG A O 846 C CB . ARG A 107 ? 1.6181 1.7027 1.3240 -0.2376 0.1470 -0.1084 107 ARG A CB 847 C CG . ARG A 107 ? 1.7109 1.7688 1.4113 -0.2129 0.1361 -0.0959 107 ARG A CG 848 C CD . ARG A 107 ? 1.8720 1.8748 1.5260 -0.2153 0.1423 -0.0864 107 ARG A CD 849 N NE . ARG A 107 ? 1.9523 1.9394 1.6092 -0.1912 0.1308 -0.0763 107 ARG A NE 850 C CZ . ARG A 107 ? 1.9906 1.9385 1.6194 -0.1875 0.1322 -0.0682 107 ARG A CZ 851 N NH1 . ARG A 107 ? 2.0922 2.0076 1.6849 -0.2068 0.1447 -0.0683 107 ARG A NH1 852 N NH2 . ARG A 107 ? 1.9404 1.8815 1.5766 -0.1645 0.1212 -0.0605 107 ARG A NH2 853 N N . ILE A 108 ? 1.2627 1.4742 1.0537 -0.2469 0.1441 -0.1386 108 ILE A N 854 C CA . ILE A 108 ? 1.2665 1.5095 1.0629 -0.2636 0.1530 -0.1512 108 ILE A CA 855 C C . ILE A 108 ? 1.2012 1.5011 1.0432 -0.2593 0.1463 -0.1632 108 ILE A C 856 O O . ILE A 108 ? 1.1871 1.5036 1.0565 -0.2378 0.1335 -0.1614 108 ILE A O 857 C CB . ILE A 108 ? 1.2857 1.5211 1.0689 -0.2581 0.1541 -0.1493 108 ILE A CB 858 C CG1 . ILE A 108 ? 1.3676 1.5466 1.0996 -0.2646 0.1630 -0.1393 108 ILE A CG1 859 C CG2 . ILE A 108 ? 1.2614 1.5363 1.0563 -0.2729 0.1619 -0.1634 108 ILE A CG2 860 C CD1 . ILE A 108 ? 1.3982 1.5623 1.1144 -0.2530 0.1610 -0.1344 108 ILE A CD1 861 N N . ASN A 109 ? 1.1661 1.4952 1.0140 -0.2799 0.1553 -0.1760 109 ASN A N 862 C CA . ASN A 109 ? 1.1438 1.5291 1.0317 -0.2764 0.1499 -0.1892 109 ASN A CA 863 C C . ASN A 109 ? 1.1690 1.5928 1.0676 -0.2838 0.1552 -0.2020 109 ASN A C 864 O O . ASN A 109 ? 1.1393 1.6084 1.0715 -0.2730 0.1480 -0.2115 109 ASN A O 865 C CB . ASN A 109 ? 1.1841 1.5837 1.0771 -0.2917 0.1542 -0.1965 109 ASN A CB 866 C CG . ASN A 109 ? 1.2226 1.5992 1.1184 -0.2784 0.1452 -0.1863 109 ASN A CG 867 O OD1 . ASN A 109 ? 1.2172 1.6069 1.1388 -0.2559 0.1322 -0.1835 109 ASN A OD1 868 N ND2 . ASN A 109 ? 1.2962 1.6362 1.1633 -0.2924 0.1526 -0.1808 109 ASN A ND2 869 N N . HIS A 110 ? 1.2108 1.6162 1.0796 -0.3012 0.1681 -0.2024 110 HIS A N 870 C CA . HIS A 110 ? 1.1893 1.6314 1.0662 -0.3102 0.1747 -0.2151 110 HIS A CA 871 C C . HIS A 110 ? 1.2084 1.6183 1.0509 -0.3180 0.1841 -0.2098 110 HIS A C 872 O O . HIS A 110 ? 1.2000 1.5633 1.0031 -0.3317 0.1939 -0.2019 110 HIS A O 873 C CB . HIS A 110 ? 1.1964 1.6773 1.0817 -0.3348 0.1854 -0.2315 110 HIS A CB 874 C CG . HIS A 110 ? 1.1953 1.7301 1.1019 -0.3391 0.1888 -0.2475 110 HIS A CG 875 N ND1 . HIS A 110 ? 1.2203 1.7887 1.1269 -0.3659 0.2024 -0.2635 110 HIS A ND1 876 C CD2 . HIS A 110 ? 1.1585 1.7203 1.0869 -0.3201 0.1806 -0.2508 110 HIS A CD2 877 C CE1 . HIS A 110 ? 1.1918 1.8074 1.1201 -0.3621 0.2021 -0.2759 110 HIS A CE1 878 N NE2 . HIS A 110 ? 1.1549 1.7659 1.0958 -0.3341 0.1889 -0.2682 110 HIS A NE2 879 N N . PHE A 111 ? 1.1829 1.6167 1.0392 -0.3076 0.1807 -0.2142 111 PHE A N 880 C CA . PHE A 111 ? 1.2318 1.6461 1.0599 -0.3152 0.1898 -0.2125 111 PHE A CA 881 C C . PHE A 111 ? 1.2498 1.7118 1.0901 -0.3317 0.1998 -0.2296 111 PHE A C 882 O O . PHE A 111 ? 1.2424 1.7560 1.1203 -0.3234 0.1931 -0.2409 111 PHE A O 883 C CB . PHE A 111 ? 1.2112 1.6159 1.0454 -0.2889 0.1774 -0.2043 111 PHE A CB 884 C CG . PHE A 111 ? 1.2202 1.5729 1.0328 -0.2745 0.1704 -0.1874 111 PHE A CG 885 C CD1 . PHE A 111 ? 1.2623 1.5644 1.0312 -0.2870 0.1801 -0.1783 111 PHE A CD1 886 C CD2 . PHE A 111 ? 1.1703 1.5241 1.0043 -0.2479 0.1543 -0.1810 111 PHE A CD2 887 C CE1 . PHE A 111 ? 1.2541 1.5113 1.0032 -0.2712 0.1729 -0.1635 111 PHE A CE1 888 C CE2 . PHE A 111 ? 1.1629 1.4742 0.9790 -0.2344 0.1477 -0.1669 111 PHE A CE2 889 C CZ . PHE A 111 ? 1.1786 1.4428 0.9527 -0.2450 0.1565 -0.1582 111 PHE A CZ 890 N N . GLU A 112 ? 1.2988 1.7435 1.1059 -0.3542 0.2161 -0.2317 112 GLU A N 891 C CA . GLU A 112 ? 1.3219 1.8083 1.1375 -0.3665 0.2254 -0.2465 112 GLU A CA 892 C C . GLU A 112 ? 1.2837 1.7415 1.0740 -0.3598 0.2274 -0.2391 112 GLU A C 893 O O . GLU A 112 ? 1.2468 1.6514 0.9934 -0.3690 0.2362 -0.2287 112 GLU A O 894 C CB . GLU A 112 ? 1.3821 1.8810 1.1824 -0.4022 0.2448 -0.2587 112 GLU A CB 895 C CG . GLU A 112 ? 1.4315 1.9897 1.2520 -0.4139 0.2528 -0.2775 112 GLU A CG 896 C CD . GLU A 112 ? 1.5557 2.1150 1.3494 -0.4524 0.2757 -0.2880 112 GLU A CD 897 O OE1 . GLU A 112 ? 1.5818 2.1331 1.3664 -0.4726 0.2832 -0.2907 112 GLU A OE1 898 O OE2 . GLU A 112 ? 1.5824 2.1509 1.3638 -0.4636 0.2868 -0.2943 112 GLU A OE2 899 N N . LYS A 113 ? 1.2250 1.7165 1.0410 -0.3424 0.2190 -0.2444 113 LYS A N 900 C CA . LYS A 113 ? 1.2714 1.7424 1.0673 -0.3346 0.2199 -0.2391 113 LYS A CA 901 C C . LYS A 113 ? 1.2873 1.7653 1.0596 -0.3607 0.2391 -0.2485 113 LYS A C 902 O O . LYS A 113 ? 1.2878 1.8161 1.0812 -0.3749 0.2463 -0.2646 113 LYS A O 903 C CB . LYS A 113 ? 1.2406 1.7453 1.0717 -0.3077 0.2046 -0.2425 113 LYS A CB 904 C CG . LYS A 113 ? 1.2788 1.7635 1.0912 -0.2976 0.2037 -0.2373 113 LYS A CG 905 C CD . LYS A 113 ? 1.2820 1.7662 1.1162 -0.2667 0.1847 -0.2310 113 LYS A CD 906 C CE . LYS A 113 ? 1.2691 1.8072 1.1486 -0.2539 0.1751 -0.2427 113 LYS A CE 907 N NZ . LYS A 113 ? 1.2762 1.8135 1.1723 -0.2265 0.1593 -0.2385 113 LYS A NZ 908 N N . ILE A 114 ? 1.3037 1.7319 1.0315 -0.3665 0.2476 -0.2388 114 ILE A N 909 C CA . ILE A 114 ? 1.3577 1.7864 1.0583 -0.3907 0.2665 -0.2464 114 ILE A CA 910 C C . ILE A 114 ? 1.4209 1.8166 1.0924 -0.3794 0.2664 -0.2378 114 ILE A C 911 O O . ILE A 114 ? 1.4244 1.7784 1.0804 -0.3590 0.2556 -0.2232 114 ILE A O 912 C CB . ILE A 114 ? 1.3943 1.7898 1.0559 -0.4231 0.2858 -0.2461 114 ILE A CB 913 C CG1 . ILE A 114 ? 1.4477 1.7680 1.0642 -0.4171 0.2847 -0.2270 114 ILE A CG1 914 C CG2 . ILE A 114 ? 1.3560 1.7902 1.0468 -0.4374 0.2874 -0.2572 114 ILE A CG2 915 C CD1 . ILE A 114 ? 1.5237 1.7957 1.0829 -0.4464 0.3068 -0.2247 114 ILE A CD1 916 N N . GLN A 115 ? 1.4386 1.8555 1.1028 -0.3931 0.2787 -0.2479 115 GLN A N 917 C CA . GLN A 115 ? 1.4466 1.8390 1.0845 -0.3840 0.2799 -0.2424 115 GLN A CA 918 C C . GLN A 115 ? 1.4844 1.8111 1.0600 -0.4014 0.2956 -0.2321 115 GLN A C 919 O O . GLN A 115 ? 1.5106 1.8337 1.0638 -0.4323 0.3152 -0.2390 115 GLN A O 920 C CB . GLN A 115 ? 1.4690 1.9134 1.1251 -0.3918 0.2874 -0.2583 115 GLN A CB 921 C CG . GLN A 115 ? 1.5072 1.9337 1.1412 -0.3805 0.2873 -0.2542 115 GLN A CG 922 C CD . GLN A 115 ? 1.4851 1.9695 1.1455 -0.3826 0.2909 -0.2705 115 GLN A CD 923 O OE1 . GLN A 115 ? 1.4663 1.9664 1.1446 -0.3592 0.2785 -0.2708 115 GLN A OE1 924 N NE2 . GLN A 115 ? 1.5323 2.0499 1.1955 -0.4108 0.3081 -0.2848 115 GLN A NE2 925 N N . ILE A 116 ? 1.4848 1.7595 1.0310 -0.3818 0.2873 -0.2165 116 ILE A N 926 C CA . ILE A 116 ? 1.5601 1.7667 1.0420 -0.3939 0.3010 -0.2056 116 ILE A CA 927 C C . ILE A 116 ? 1.6136 1.8019 1.0640 -0.3899 0.3065 -0.2038 116 ILE A C 928 O O . ILE A 116 ? 1.6867 1.8386 1.0878 -0.4113 0.3256 -0.2028 116 ILE A O 929 C CB . ILE A 116 ? 1.5467 1.6991 1.0063 -0.3772 0.2906 -0.1889 116 ILE A CB 930 C CG1 . ILE A 116 ? 1.4985 1.6582 0.9851 -0.3406 0.2670 -0.1816 116 ILE A CG1 931 C CG2 . ILE A 116 ? 1.5414 1.7006 1.0172 -0.3895 0.2916 -0.1907 116 ILE A CG2 932 C CD1 . ILE A 116 ? 1.5122 1.6159 0.9690 -0.3229 0.2581 -0.1653 116 ILE A CD1 933 N N . ILE A 117 ? 1.5889 1.8010 1.0658 -0.3635 0.2906 -0.2038 117 ILE A N 934 C CA . ILE A 117 ? 1.6448 1.8456 1.0965 -0.3582 0.2945 -0.2034 117 ILE A CA 935 C C . ILE A 117 ? 1.5999 1.8659 1.0999 -0.3498 0.2875 -0.2168 117 ILE A C 936 O O . ILE A 117 ? 1.5723 1.8570 1.1044 -0.3227 0.2682 -0.2150 117 ILE A O 937 C CB . ILE A 117 ? 1.6889 1.8400 1.1114 -0.3305 0.2814 -0.1878 117 ILE A CB 938 C CG1 . ILE A 117 ? 1.7415 1.8278 1.1159 -0.3355 0.2870 -0.1745 117 ILE A CG1 939 C CG2 . ILE A 117 ? 1.7309 1.8686 1.1234 -0.3261 0.2863 -0.1877 117 ILE A CG2 940 C CD1 . ILE A 117 ? 1.7783 1.8175 1.1239 -0.3068 0.2735 -0.1598 117 ILE A CD1 941 N N . PRO A 118 ? 1.6264 1.9267 1.1301 -0.3734 0.3039 -0.2308 118 PRO A N 942 C CA . PRO A 118 ? 1.5926 1.9570 1.1408 -0.3664 0.2988 -0.2450 118 PRO A CA 943 C C . PRO A 118 ? 1.5901 1.9499 1.1392 -0.3387 0.2852 -0.2406 118 PRO A C 944 O O . PRO A 118 ? 1.6508 1.9637 1.1551 -0.3355 0.2891 -0.2312 118 PRO A O 945 C CB . PRO A 118 ? 1.6237 2.0063 1.1548 -0.3979 0.3225 -0.2576 118 PRO A CB 946 C CG . PRO A 118 ? 1.6507 1.9963 1.1472 -0.4254 0.3387 -0.2538 118 PRO A CG 947 C CD . PRO A 118 ? 1.6736 1.9533 1.1379 -0.4086 0.3289 -0.2345 118 PRO A CD 948 N N . LYS A 119 ? 1.5566 1.9635 1.1546 -0.3188 0.2695 -0.2476 119 LYS A N 949 C CA . LYS A 119 ? 1.5758 1.9830 1.1789 -0.2931 0.2560 -0.2453 119 LYS A CA 950 C C . LYS A 119 ? 1.6254 2.0329 1.2011 -0.3030 0.2698 -0.2509 119 LYS A C 951 O O . LYS A 119 ? 1.6533 2.0284 1.2003 -0.2903 0.2663 -0.2434 119 LYS A O 952 C CB . LYS A 119 ? 1.5307 1.9903 1.1899 -0.2736 0.2395 -0.2540 119 LYS A CB 953 C CG . LYS A 119 ? 1.5425 1.9885 1.2099 -0.2436 0.2197 -0.2467 119 LYS A CG 954 C CD . LYS A 119 ? 1.5383 2.0337 1.2553 -0.2262 0.2061 -0.2568 119 LYS A CD 955 C CE . LYS A 119 ? 1.5500 2.0298 1.2813 -0.1999 0.1856 -0.2484 119 LYS A CE 956 N NZ . LYS A 119 ? 1.5302 2.0450 1.2946 -0.1811 0.1737 -0.2573 119 LYS A NZ 957 N N . SER A 120 ? 1.6378 2.0833 1.2221 -0.3261 0.2857 -0.2648 120 SER A N 958 C CA . SER A 120 ? 1.6374 2.0886 1.1975 -0.3394 0.3015 -0.2721 120 SER A CA 959 C C . SER A 120 ? 1.7101 2.0959 1.2053 -0.3516 0.3154 -0.2605 120 SER A C 960 O O . SER A 120 ? 1.7871 2.1625 1.2557 -0.3520 0.3226 -0.2615 120 SER A O 961 C CB . SER A 120 ? 1.6196 2.1233 1.1997 -0.3658 0.3179 -0.2895 120 SER A CB 962 O OG . SER A 120 ? 1.6518 2.1367 1.2138 -0.3921 0.3316 -0.2879 120 SER A OG 963 N N . SER A 121 ? 1.7182 2.0582 1.1860 -0.3603 0.3190 -0.2495 121 SER A N 964 C CA . SER A 121 ? 1.7660 2.0400 1.1675 -0.3737 0.3341 -0.2388 121 SER A CA 965 C C . SER A 121 ? 1.7686 1.9921 1.1363 -0.3470 0.3220 -0.2242 121 SER A C 966 O O . SER A 121 ? 1.8332 1.9957 1.1434 -0.3529 0.3317 -0.2134 121 SER A O 967 C CB . SER A 121 ? 1.7967 2.0374 1.1781 -0.3924 0.3427 -0.2327 121 SER A CB 968 O OG . SER A 121 ? 1.7838 2.0014 1.1745 -0.3691 0.3237 -0.2205 121 SER A OG 969 N N . TRP A 122 ? 1.7103 1.9575 1.1111 -0.3177 0.3013 -0.2244 122 TRP A N 970 C CA . TRP A 122 ? 1.7204 1.9270 1.0923 -0.2923 0.2892 -0.2128 122 TRP A CA 971 C C . TRP A 122 ? 1.7375 1.9553 1.0972 -0.2891 0.2937 -0.2190 122 TRP A C 972 O O . TRP A 122 ? 1.7103 1.9666 1.1068 -0.2709 0.2800 -0.2256 122 TRP A O 973 C CB . TRP A 122 ? 1.6720 1.8926 1.0838 -0.2627 0.2636 -0.2087 122 TRP A CB 974 C CG . TRP A 122 ? 1.6632 1.8662 1.0816 -0.2629 0.2583 -0.2008 122 TRP A CG 975 C CD1 . TRP A 122 ? 1.6168 1.8575 1.0827 -0.2659 0.2525 -0.2063 122 TRP A CD1 976 C CD2 . TRP A 122 ? 1.6914 1.8339 1.0656 -0.2590 0.2584 -0.1862 122 TRP A CD2 977 N NE1 . TRP A 122 ? 1.6455 1.8536 1.1008 -0.2649 0.2490 -0.1960 122 TRP A NE1 978 C CE2 . TRP A 122 ? 1.6645 1.8124 1.0640 -0.2604 0.2525 -0.1837 122 TRP A CE2 979 C CE3 . TRP A 122 ? 1.7465 1.8300 1.0605 -0.2528 0.2625 -0.1752 122 TRP A CE3 980 C CZ2 . TRP A 122 ? 1.6783 1.7758 1.0462 -0.2564 0.2509 -0.1707 122 TRP A CZ2 981 C CZ3 . TRP A 122 ? 1.7805 1.8131 1.0617 -0.2477 0.2606 -0.1623 122 TRP A CZ3 982 C CH2 . TRP A 122 ? 1.7358 1.7763 1.0447 -0.2497 0.2549 -0.1603 122 TRP A CH2 983 N N . SER A 123 ? 1.8059 1.9872 1.1114 -0.3071 0.3134 -0.2168 123 SER A N 984 C CA . SER A 123 ? 1.8408 2.0327 1.1305 -0.3099 0.3224 -0.2238 123 SER A CA 985 C C . SER A 123 ? 1.8672 2.0193 1.1204 -0.2850 0.3126 -0.2142 123 SER A C 986 O O . SER A 123 ? 1.8666 2.0367 1.1199 -0.2788 0.3128 -0.2205 123 SER A O 987 C CB . SER A 123 ? 1.8762 2.0542 1.1272 -0.3454 0.3512 -0.2285 123 SER A CB 988 O OG . SER A 123 ? 1.9206 2.0399 1.1251 -0.3588 0.3615 -0.2172 123 SER A OG 989 N N . SER A 124 ? 1.8916 1.9915 1.1136 -0.2702 0.3038 -0.1997 124 SER A N 990 C CA . SER A 124 ? 1.8895 1.9531 1.0777 -0.2437 0.2922 -0.1908 124 SER A CA 991 C C . SER A 124 ? 1.8558 1.9412 1.0864 -0.2122 0.2646 -0.1891 124 SER A C 992 O O . SER A 124 ? 1.8747 1.9366 1.0842 -0.1883 0.2522 -0.1830 124 SER A O 993 C CB . SER A 124 ? 1.9473 1.9361 1.0666 -0.2451 0.3005 -0.1762 124 SER A CB 994 O OG . SER A 124 ? 1.9954 1.9590 1.0723 -0.2765 0.3273 -0.1775 124 SER A OG 995 N N . HIS A 125 ? 1.8070 1.9366 1.0956 -0.2125 0.2554 -0.1949 125 HIS A N 996 C CA . HIS A 125 ? 1.7529 1.9042 1.0838 -0.1859 0.2308 -0.1942 125 HIS A CA 997 C C . HIS A 125 ? 1.7357 1.9515 1.1302 -0.1874 0.2249 -0.2075 125 HIS A C 998 O O . HIS A 125 ? 1.7246 1.9682 1.1354 -0.2092 0.2384 -0.2159 125 HIS A O 999 C CB . HIS A 125 ? 1.7233 1.8487 1.0535 -0.1804 0.2231 -0.1837 125 HIS A CB 1000 C CG . HIS A 125 ? 1.7485 1.8088 1.0160 -0.1752 0.2269 -0.1702 125 HIS A CG 1001 N ND1 . HIS A 125 ? 1.7847 1.8041 1.0030 -0.1974 0.2478 -0.1653 125 HIS A ND1 1002 C CD2 . HIS A 125 ? 1.7546 1.7835 0.9992 -0.1495 0.2124 -0.1610 125 HIS A CD2 1003 C CE1 . HIS A 125 ? 1.8473 1.8092 1.0125 -0.1845 0.2461 -0.1530 125 HIS A CE1 1004 N NE2 . HIS A 125 ? 1.8267 1.7953 1.0077 -0.1546 0.2243 -0.1504 125 HIS A NE2 1005 N N . GLU A 126 ? 1.7376 1.9765 1.1666 -0.1640 0.2049 -0.2100 126 GLU A N 1006 C CA . GLU A 126 ? 1.7248 2.0196 1.2112 -0.1614 0.1974 -0.2219 126 GLU A CA 1007 C C . GLU A 126 ? 1.6932 2.0003 1.2158 -0.1603 0.1888 -0.2197 126 GLU A C 1008 O O . GLU A 126 ? 1.6996 1.9863 1.2232 -0.1450 0.1752 -0.2112 126 GLU A O 1009 C CB . GLU A 126 ? 1.7637 2.0748 1.2668 -0.1382 0.1812 -0.2264 126 GLU A CB 1010 C CG . GLU A 126 ? 1.7632 2.1281 1.3178 -0.1349 0.1754 -0.2396 126 GLU A CG 1011 C CD . GLU A 126 ? 1.7973 2.1924 1.3562 -0.1550 0.1930 -0.2504 126 GLU A CD 1012 O OE1 . GLU A 126 ? 1.7628 2.1491 1.2901 -0.1619 0.2046 -0.2526 126 GLU A OE1 1013 O OE2 . GLU A 126 ? 1.8131 2.2418 1.4067 -0.1636 0.1952 -0.2571 126 GLU A OE2 1014 N N . ALA A 127 ? 1.6529 1.9954 1.2052 -0.1761 0.1966 -0.2282 127 ALA A N 1015 C CA . ALA A 127 ? 1.6018 1.9542 1.1833 -0.1790 0.1920 -0.2263 127 ALA A CA 1016 C C . ALA A 127 ? 1.5521 1.9570 1.1889 -0.1726 0.1830 -0.2376 127 ALA A C 1017 O O . ALA A 127 ? 1.5412 1.9620 1.2031 -0.1788 0.1825 -0.2388 127 ALA A O 1018 C CB . ALA A 127 ? 1.6288 1.9682 1.1888 -0.2057 0.2108 -0.2249 127 ALA A CB 1019 N N . SER A 128 ? 1.5408 1.9705 1.1943 -0.1593 0.1757 -0.2456 128 SER A N 1020 C CA . SER A 128 ? 1.4721 1.9475 1.1735 -0.1505 0.1668 -0.2564 128 SER A CA 1021 C C . SER A 128 ? 1.4499 1.9276 1.1700 -0.1259 0.1479 -0.2566 128 SER A C 1022 O O . SER A 128 ? 1.4056 1.9149 1.1619 -0.1167 0.1397 -0.2647 128 SER A O 1023 C CB . SER A 128 ? 1.4866 2.0005 1.1957 -0.1609 0.1787 -0.2702 128 SER A CB 1024 O OG . SER A 128 ? 1.5541 2.0688 1.2472 -0.1859 0.1970 -0.2715 128 SER A OG 1025 N N . LEU A 129 ? 1.4884 1.9327 1.1827 -0.1153 0.1413 -0.2485 129 LEU A N 1026 C CA . LEU A 129 ? 1.4839 1.9281 1.1935 -0.0937 0.1235 -0.2488 129 LEU A CA 1027 C C . LEU A 129 ? 1.4679 1.8891 1.1816 -0.0853 0.1121 -0.2386 129 LEU A C 1028 O O . LEU A 129 ? 1.4909 1.9088 1.2151 -0.0691 0.0976 -0.2381 129 LEU A O 1029 C CB . LEU A 129 ? 1.5529 1.9814 1.2332 -0.0858 0.1224 -0.2489 129 LEU A CB 1030 C CG . LEU A 129 ? 1.5931 2.0368 1.2590 -0.0949 0.1356 -0.2573 129 LEU A CG 1031 C CD1 . LEU A 129 ? 1.5945 2.0207 1.2331 -0.0834 0.1314 -0.2568 129 LEU A CD1 1032 C CD2 . LEU A 129 ? 1.5543 2.0435 1.2576 -0.0946 0.1358 -0.2707 129 LEU A CD2 1033 N N . GLY A 130 ? 1.4419 1.8477 1.1470 -0.0971 0.1189 -0.2311 130 GLY A N 1034 C CA . GLY A 130 ? 1.3836 1.7696 1.0936 -0.0902 0.1093 -0.2217 130 GLY A CA 1035 C C . GLY A 130 ? 1.3167 1.7294 1.0711 -0.0852 0.1004 -0.2262 130 GLY A C 1036 O O . GLY A 130 ? 1.2696 1.6857 1.0355 -0.0942 0.1043 -0.2239 130 GLY A O 1037 N N . VAL A 131 ? 1.2413 1.6708 1.0183 -0.0709 0.0887 -0.2327 131 VAL A N 1038 C CA . VAL A 131 ? 1.1933 1.6468 1.0096 -0.0649 0.0807 -0.2381 131 VAL A CA 1039 C C . VAL A 131 ? 1.1498 1.5986 0.9793 -0.0482 0.0650 -0.2383 131 VAL A C 1040 O O . VAL A 131 ? 1.1698 1.6113 0.9852 -0.0404 0.0605 -0.2397 131 VAL A O 1041 C CB . VAL A 131 ? 1.1878 1.6762 1.0223 -0.0677 0.0861 -0.2505 131 VAL A CB 1042 C CG1 . VAL A 131 ? 1.1859 1.6859 1.0151 -0.0857 0.1012 -0.2520 131 VAL A CG1 1043 C CG2 . VAL A 131 ? 1.1869 1.6808 1.0094 -0.0618 0.0861 -0.2574 131 VAL A CG2 1044 N N . SER A 132 ? 1.1395 1.5929 0.9953 -0.0435 0.0572 -0.2373 132 SER A N 1045 C CA . SER A 132 ? 1.1167 1.5647 0.9859 -0.0305 0.0434 -0.2373 132 SER A CA 1046 C C . SER A 132 ? 1.0936 1.5603 0.9951 -0.0251 0.0378 -0.2445 132 SER A C 1047 O O . SER A 132 ? 1.0983 1.5772 1.0143 -0.0302 0.0423 -0.2455 132 SER A O 1048 C CB . SER A 132 ? 1.1361 1.5621 0.9994 -0.0297 0.0390 -0.2266 132 SER A CB 1049 O OG . SER A 132 ? 1.1300 1.5541 1.0086 -0.0188 0.0264 -0.2275 132 SER A OG 1050 N N . SER A 133 ? 1.0912 1.5586 1.0020 -0.0146 0.0279 -0.2497 133 SER A N 1051 C CA . SER A 133 ? 1.0887 1.5667 1.0255 -0.0083 0.0220 -0.2561 133 SER A CA 1052 C C . SER A 133 ? 1.0697 1.5384 1.0213 -0.0084 0.0174 -0.2495 133 SER A C 1053 O O . SER A 133 ? 1.0592 1.5338 1.0302 -0.0048 0.0146 -0.2531 133 SER A O 1054 C CB . SER A 133 ? 1.1228 1.6001 1.0617 0.0012 0.0135 -0.2637 133 SER A CB 1055 O OG . SER A 133 ? 1.1695 1.6317 1.1011 0.0038 0.0062 -0.2591 133 SER A OG 1056 N N . ALA A 134 ? 1.0903 1.5433 1.0307 -0.0116 0.0168 -0.2401 134 ALA A N 1057 C CA . ALA A 134 ? 1.0756 1.5199 1.0276 -0.0128 0.0140 -0.2329 134 ALA A CA 1058 C C . ALA A 134 ? 1.1028 1.5536 1.0610 -0.0206 0.0220 -0.2301 134 ALA A C 1059 O O . ALA A 134 ? 1.0763 1.5247 1.0494 -0.0205 0.0197 -0.2267 134 ALA A O 1060 C CB . ALA A 134 ? 1.0931 1.5194 1.0287 -0.0125 0.0112 -0.2242 134 ALA A CB 1061 N N . CYS A 135 ? 1.1390 1.5991 1.0857 -0.0279 0.0315 -0.2321 135 CYS A N 1062 C CA . CYS A 135 ? 1.1504 1.6221 1.1033 -0.0366 0.0398 -0.2319 135 CYS A CA 1063 C C . CYS A 135 ? 1.1071 1.6054 1.0703 -0.0357 0.0438 -0.2430 135 CYS A C 1064 O O . CYS A 135 ? 1.1146 1.6244 1.0668 -0.0442 0.0533 -0.2462 135 CYS A O 1065 C CB . CYS A 135 ? 1.2260 1.6863 1.1547 -0.0488 0.0495 -0.2250 135 CYS A CB 1066 S SG . CYS A 135 ? 1.4044 1.8325 1.3167 -0.0477 0.0451 -0.2119 135 CYS A SG 1067 N N . PRO A 136 ? 1.0603 1.5680 1.0431 -0.0253 0.0371 -0.2495 136 PRO A N 1068 C CA . PRO A 136 ? 1.0515 1.5836 1.0424 -0.0208 0.0396 -0.2608 136 PRO A CA 1069 C C . PRO A 136 ? 1.0460 1.5998 1.0488 -0.0251 0.0456 -0.2640 136 PRO A C 1070 O O . PRO A 136 ? 0.9693 1.5176 0.9806 -0.0272 0.0444 -0.2585 136 PRO A O 1071 C CB . PRO A 136 ? 1.0614 1.5882 1.0649 -0.0071 0.0296 -0.2653 136 PRO A CB 1072 C CG . PRO A 136 ? 1.0216 1.5302 1.0329 -0.0072 0.0243 -0.2568 136 PRO A CG 1073 C CD . PRO A 136 ? 1.0276 1.5224 1.0243 -0.0170 0.0274 -0.2469 136 PRO A CD 1074 N N . TYR A 137 ? 1.0757 1.6560 1.0792 -0.0259 0.0518 -0.2738 137 TYR A N 1075 C CA . TYR A 137 ? 1.0498 1.6582 1.0660 -0.0284 0.0570 -0.2801 137 TYR A CA 1076 C C . TYR A 137 ? 1.0349 1.6704 1.0591 -0.0173 0.0567 -0.2934 137 TYR A C 1077 O O . TYR A 137 ? 1.0532 1.7000 1.0676 -0.0199 0.0618 -0.2991 137 TYR A O 1078 C CB . TYR A 137 ? 1.0867 1.7043 1.0917 -0.0469 0.0692 -0.2784 137 TYR A CB 1079 C CG . TYR A 137 ? 1.1228 1.7750 1.1416 -0.0514 0.0753 -0.2870 137 TYR A CG 1080 C CD1 . TYR A 137 ? 1.1375 1.7929 1.1713 -0.0492 0.0719 -0.2849 137 TYR A CD1 1081 C CD2 . TYR A 137 ? 1.1295 1.8132 1.1462 -0.0577 0.0846 -0.2978 137 TYR A CD2 1082 C CE1 . TYR A 137 ? 1.1528 1.8428 1.1994 -0.0526 0.0768 -0.2938 137 TYR A CE1 1083 C CE2 . TYR A 137 ? 1.1393 1.8596 1.1700 -0.0620 0.0901 -0.3072 137 TYR A CE2 1084 C CZ . TYR A 137 ? 1.1594 1.8833 1.2050 -0.0591 0.0858 -0.3054 137 TYR A CZ 1085 O OH . TYR A 137 ? 1.1577 1.9208 1.2173 -0.0627 0.0907 -0.3158 137 TYR A OH 1086 N N . GLN A 138 ? 1.0337 1.6783 1.0739 -0.0040 0.0507 -0.2983 138 GLN A N 1087 C CA . GLN A 138 ? 1.0834 1.7499 1.1298 0.0107 0.0486 -0.3110 138 GLN A CA 1088 C C . GLN A 138 ? 1.0936 1.7464 1.1293 0.0178 0.0450 -0.3135 138 GLN A C 1089 O O . GLN A 138 ? 1.1105 1.7839 1.1428 0.0216 0.0485 -0.3232 138 GLN A O 1090 C CB . GLN A 138 ? 1.1306 1.8385 1.1809 0.0048 0.0581 -0.3213 138 GLN A CB 1091 C CG . GLN A 138 ? 1.1349 1.8623 1.1972 -0.0016 0.0616 -0.3217 138 GLN A CG 1092 C CD . GLN A 138 ? 1.1574 1.9292 1.2239 -0.0099 0.0718 -0.3334 138 GLN A CD 1093 O OE1 . GLN A 138 ? 1.1714 1.9599 1.2320 -0.0099 0.0765 -0.3414 138 GLN A OE1 1094 N NE2 . GLN A 138 ? 1.1578 1.9502 1.2345 -0.0177 0.0756 -0.3351 138 GLN A NE2 1095 N N . GLY A 139 ? 1.1058 1.7255 1.1363 0.0193 0.0381 -0.3054 139 GLY A N 1096 C CA . GLY A 139 ? 1.1334 1.7383 1.1548 0.0265 0.0332 -0.3083 139 GLY A CA 1097 C C . GLY A 139 ? 1.1658 1.7654 1.1708 0.0165 0.0373 -0.3054 139 GLY A C 1098 O O . GLY A 139 ? 1.2099 1.7922 1.2068 0.0207 0.0320 -0.3053 139 GLY A O 1099 N N . LYS A 140 ? 1.1613 1.7748 1.1598 0.0031 0.0470 -0.3036 140 LYS A N 1100 C CA . LYS A 140 ? 1.1759 1.7832 1.1546 -0.0063 0.0525 -0.3010 140 LYS A CA 1101 C C . LYS A 140 ? 1.1664 1.7479 1.1348 -0.0163 0.0525 -0.2880 140 LYS A C 1102 O O . LYS A 140 ? 1.1656 1.7408 1.1435 -0.0190 0.0509 -0.2818 140 LYS A O 1103 C CB . LYS A 140 ? 1.2154 1.8510 1.1889 -0.0162 0.0649 -0.3073 140 LYS A CB 1104 C CG . LYS A 140 ? 1.2767 1.9453 1.2637 -0.0062 0.0659 -0.3209 140 LYS A CG 1105 C CD . LYS A 140 ? 1.3486 2.0488 1.3313 -0.0179 0.0790 -0.3282 140 LYS A CD 1106 C CE . LYS A 140 ? 1.3862 2.1248 1.3865 -0.0074 0.0797 -0.3419 140 LYS A CE 1107 N NZ . LYS A 140 ? 1.4129 2.1859 1.4086 -0.0162 0.0918 -0.3521 140 LYS A NZ 1108 N N . SER A 141 ? 1.1717 1.7378 1.1195 -0.0206 0.0539 -0.2839 141 SER A N 1109 C CA . SER A 141 ? 1.1524 1.6937 1.0854 -0.0289 0.0546 -0.2719 141 SER A CA 1110 C C . SER A 141 ? 1.1560 1.7030 1.0802 -0.0445 0.0669 -0.2685 141 SER A C 1111 O O . SER A 141 ? 1.1899 1.7567 1.1086 -0.0516 0.0767 -0.2752 141 SER A O 1112 C CB . SER A 141 ? 1.1374 1.6609 1.0477 -0.0269 0.0525 -0.2695 141 SER A CB 1113 O OG . SER A 141 ? 1.1508 1.6660 1.0691 -0.0146 0.0406 -0.2717 141 SER A OG 1114 N N . SER A 142 ? 1.0928 1.6230 1.0154 -0.0504 0.0668 -0.2587 142 SER A N 1115 C CA . SER A 142 ? 1.0680 1.5987 0.9805 -0.0664 0.0783 -0.2547 142 SER A CA 1116 C C . SER A 142 ? 1.0439 1.5410 0.9385 -0.0703 0.0770 -0.2417 142 SER A C 1117 O O . SER A 142 ? 0.9994 1.4764 0.8848 -0.0615 0.0690 -0.2369 142 SER A O 1118 C CB . SER A 142 ? 1.0841 1.6391 1.0211 -0.0686 0.0799 -0.2596 142 SER A CB 1119 O OG . SER A 142 ? 1.1036 1.6588 1.0322 -0.0853 0.0905 -0.2561 142 SER A OG 1120 N N . PHE A 143 ? 1.0525 1.5444 0.9413 -0.0832 0.0849 -0.2366 143 PHE A N 1121 C CA . PHE A 143 ? 1.0615 1.5201 0.9298 -0.0870 0.0850 -0.2243 143 PHE A CA 1122 C C . PHE A 143 ? 1.0509 1.5098 0.9227 -0.0996 0.0919 -0.2209 143 PHE A C 1123 O O . PHE A 143 ? 1.0351 1.5214 0.9220 -0.1073 0.0980 -0.2288 143 PHE A O 1124 C CB . PHE A 143 ? 1.0874 1.5241 0.9182 -0.0927 0.0925 -0.2205 143 PHE A CB 1125 C CG . PHE A 143 ? 1.1080 1.5073 0.9139 -0.0897 0.0894 -0.2082 143 PHE A CG 1126 C CD1 . PHE A 143 ? 1.1045 1.4939 0.9188 -0.0740 0.0754 -0.2044 143 PHE A CD1 1127 C CD2 . PHE A 143 ? 1.1283 1.5020 0.9007 -0.1025 0.1007 -0.2012 143 PHE A CD2 1128 C CE1 . PHE A 143 ? 1.1214 1.4797 0.9131 -0.0693 0.0721 -0.1941 143 PHE A CE1 1129 C CE2 . PHE A 143 ? 1.1556 1.4935 0.9024 -0.0973 0.0975 -0.1901 143 PHE A CE2 1130 C CZ . PHE A 143 ? 1.1474 1.4792 0.9046 -0.0798 0.0827 -0.1867 143 PHE A CZ 1131 N N . PHE A 144 ? 1.0917 1.5215 0.9499 -0.1008 0.0904 -0.2100 144 PHE A N 1132 C CA . PHE A 144 ? 1.0796 1.5029 0.9343 -0.1140 0.0978 -0.2057 144 PHE A CA 1133 C C . PHE A 144 ? 1.0859 1.5208 0.9265 -0.1333 0.1136 -0.2115 144 PHE A C 1134 O O . PHE A 144 ? 1.1541 1.5737 0.9648 -0.1401 0.1218 -0.2102 144 PHE A O 1135 C CB . PHE A 144 ? 1.1225 1.5060 0.9510 -0.1135 0.0968 -0.1928 144 PHE A CB 1136 C CG . PHE A 144 ? 1.1407 1.5137 0.9813 -0.0961 0.0822 -0.1873 144 PHE A CG 1137 C CD1 . PHE A 144 ? 1.1471 1.5295 1.0158 -0.0913 0.0752 -0.1867 144 PHE A CD1 1138 C CD2 . PHE A 144 ? 1.1646 1.5188 0.9874 -0.0849 0.0759 -0.1834 144 PHE A CD2 1139 C CE1 . PHE A 144 ? 1.1353 1.5087 1.0147 -0.0772 0.0630 -0.1823 144 PHE A CE1 1140 C CE2 . PHE A 144 ? 1.1686 1.5168 1.0035 -0.0703 0.0630 -0.1798 144 PHE A CE2 1141 C CZ . PHE A 144 ? 1.1554 1.5133 1.0189 -0.0672 0.0570 -0.1793 144 PHE A CZ 1142 N N . ARG A 145 ? 1.0529 1.5150 0.9142 -0.1421 0.1181 -0.2182 145 ARG A N 1143 C CA . ARG A 145 ? 1.0539 1.5383 0.9099 -0.1604 0.1326 -0.2272 145 ARG A CA 1144 C C . ARG A 145 ? 1.0956 1.5537 0.9178 -0.1815 0.1469 -0.2217 145 ARG A C 1145 O O . ARG A 145 ? 1.1730 1.6423 0.9817 -0.1986 0.1608 -0.2286 145 ARG A O 1146 C CB . ARG A 145 ? 1.0254 1.5506 0.9157 -0.1616 0.1316 -0.2373 145 ARG A CB 1147 C CG . ARG A 145 ? 1.0060 1.5576 0.9264 -0.1417 0.1195 -0.2444 145 ARG A CG 1148 C CD . ARG A 145 ? 1.0350 1.6318 0.9815 -0.1444 0.1223 -0.2575 145 ARG A CD 1149 N NE . ARG A 145 ? 1.0300 1.6496 1.0020 -0.1243 0.1112 -0.2647 145 ARG A NE 1150 C CZ . ARG A 145 ? 1.0673 1.6987 1.0396 -0.1157 0.1097 -0.2713 145 ARG A CZ 1151 N NH1 . ARG A 145 ? 1.0983 1.7219 1.0474 -0.1249 0.1182 -0.2715 145 ARG A NH1 1152 N NH2 . ARG A 145 ? 1.1120 1.7604 1.1055 -0.0972 0.0997 -0.2776 145 ARG A NH2 1153 N N . ASN A 146 ? 1.1077 1.5307 0.9154 -0.1809 0.1443 -0.2100 146 ASN A N 1154 C CA . ASN A 146 ? 1.1615 1.5546 0.9350 -0.2005 0.1578 -0.2043 146 ASN A CA 1155 C C . ASN A 146 ? 1.1851 1.5337 0.9138 -0.1998 0.1620 -0.1951 146 ASN A C 1156 O O . ASN A 146 ? 1.2086 1.5261 0.9012 -0.2158 0.1745 -0.1901 146 ASN A O 1157 C CB . ASN A 146 ? 1.1357 1.5147 0.9156 -0.2012 0.1540 -0.1974 146 ASN A CB 1158 C CG . ASN A 146 ? 1.1434 1.5645 0.9632 -0.2029 0.1511 -0.2066 146 ASN A CG 1159 O OD1 . ASN A 146 ? 1.2112 1.6699 1.0456 -0.2122 0.1578 -0.2190 146 ASN A OD1 1160 N ND2 . ASN A 146 ? 1.1338 1.5498 0.9709 -0.1930 0.1411 -0.2011 146 ASN A ND2 1161 N N . VAL A 147 ? 1.1742 1.5188 0.9034 -0.1811 0.1516 -0.1931 147 VAL A N 1162 C CA . VAL A 147 ? 1.2315 1.5375 0.9186 -0.1774 0.1541 -0.1855 147 VAL A CA 1163 C C . VAL A 147 ? 1.2384 1.5617 0.9265 -0.1708 0.1531 -0.1925 147 VAL A C 1164 O O . VAL A 147 ? 1.2078 1.5697 0.9317 -0.1635 0.1463 -0.2017 147 VAL A O 1165 C CB . VAL A 147 ? 1.2413 1.5153 0.9192 -0.1585 0.1411 -0.1738 147 VAL A CB 1166 C CG1 . VAL A 147 ? 1.2735 1.5194 0.9361 -0.1667 0.1453 -0.1653 147 VAL A CG1 1167 C CG2 . VAL A 147 ? 1.1922 1.4931 0.9125 -0.1392 0.1238 -0.1766 147 VAL A CG2 1168 N N . VAL A 148 ? 1.3049 1.5969 0.9510 -0.1725 0.1597 -0.1879 148 VAL A N 1169 C CA . VAL A 148 ? 1.3181 1.6225 0.9581 -0.1689 0.1613 -0.1943 148 VAL A CA 1170 C C . VAL A 148 ? 1.3448 1.6204 0.9632 -0.1485 0.1503 -0.1867 148 VAL A C 1171 O O . VAL A 148 ? 1.4317 1.6644 1.0114 -0.1470 0.1525 -0.1763 148 VAL A O 1172 C CB . VAL A 148 ? 1.3536 1.6488 0.9594 -0.1916 0.1817 -0.1976 148 VAL A CB 1173 C CG1 . VAL A 148 ? 1.3969 1.7137 1.0034 -0.1889 0.1838 -0.2063 148 VAL A CG1 1174 C CG2 . VAL A 148 ? 1.3812 1.7007 1.0034 -0.2142 0.1936 -0.2046 148 VAL A CG2 1175 N N . TRP A 149 ? 1.3029 1.6022 0.9454 -0.1324 0.1382 -0.1923 149 TRP A N 1176 C CA . TRP A 149 ? 1.3291 1.6077 0.9535 -0.1134 0.1275 -0.1875 149 TRP A CA 1177 C C . TRP A 149 ? 1.3686 1.6381 0.9598 -0.1170 0.1366 -0.1903 149 TRP A C 1178 O O . TRP A 149 ? 1.3366 1.6343 0.9446 -0.1140 0.1350 -0.1997 149 TRP A O 1179 C CB . TRP A 149 ? 1.2830 1.5892 0.9483 -0.0953 0.1100 -0.1926 149 TRP A CB 1180 C CG . TRP A 149 ? 1.2854 1.5752 0.9377 -0.0758 0.0973 -0.1888 149 TRP A CG 1181 C CD1 . TRP A 149 ? 1.3439 1.5973 0.9525 -0.0700 0.0984 -0.1809 149 TRP A CD1 1182 C CD2 . TRP A 149 ? 1.2534 1.5628 0.9360 -0.0592 0.0813 -0.1935 149 TRP A CD2 1183 N NE1 . TRP A 149 ? 1.3520 1.6054 0.9640 -0.0500 0.0833 -0.1811 149 TRP A NE1 1184 C CE2 . TRP A 149 ? 1.2811 1.5687 0.9387 -0.0445 0.0730 -0.1889 149 TRP A CE2 1185 C CE3 . TRP A 149 ? 1.2298 1.5718 0.9563 -0.0554 0.0734 -0.2014 149 TRP A CE3 1186 C CZ2 . TRP A 149 ? 1.2661 1.5667 0.9436 -0.0280 0.0575 -0.1930 149 TRP A CZ2 1187 C CZ3 . TRP A 149 ? 1.2254 1.5755 0.9689 -0.0396 0.0587 -0.2046 149 TRP A CZ3 1188 C CH2 . TRP A 149 ? 1.2381 1.5692 0.9584 -0.0270 0.0511 -0.2008 149 TRP A CH2 1189 N N . LEU A 150 ? 1.4412 1.6689 0.9829 -0.1234 0.1467 -0.1820 150 LEU A N 1190 C CA . LEU A 150 ? 1.4985 1.7102 1.0012 -0.1282 0.1574 -0.1832 150 LEU A CA 1191 C C . LEU A 150 ? 1.5093 1.7134 1.0021 -0.1052 0.1438 -0.1821 150 LEU A C 1192 O O . LEU A 150 ? 1.5143 1.6975 0.9987 -0.0886 0.1318 -0.1746 150 LEU A O 1193 C CB . LEU A 150 ? 1.5745 1.7370 1.0223 -0.1413 0.1725 -0.1737 150 LEU A CB 1194 C CG . LEU A 150 ? 1.6042 1.7677 1.0534 -0.1670 0.1880 -0.1746 150 LEU A CG 1195 C CD1 . LEU A 150 ? 1.6757 1.7817 1.0656 -0.1773 0.2013 -0.1639 150 LEU A CD1 1196 C CD2 . LEU A 150 ? 1.6100 1.8121 1.0770 -0.1864 0.2010 -0.1873 150 LEU A CD2 1197 N N . ILE A 151 ? 1.5132 1.7361 1.0070 -0.1043 0.1458 -0.1903 151 ILE A N 1198 C CA . ILE A 151 ? 1.5290 1.7434 1.0069 -0.0847 0.1352 -0.1903 151 ILE A CA 1199 C C . ILE A 151 ? 1.5502 1.7471 0.9849 -0.0922 0.1491 -0.1915 151 ILE A C 1200 O O . ILE A 151 ? 1.5239 1.7247 0.9496 -0.1136 0.1666 -0.1948 151 ILE A O 1201 C CB . ILE A 151 ? 1.5011 1.7572 1.0261 -0.0715 0.1202 -0.2003 151 ILE A CB 1202 C CG1 . ILE A 151 ? 1.5189 1.8121 1.0676 -0.0840 0.1291 -0.2121 151 ILE A CG1 1203 C CG2 . ILE A 151 ? 1.4413 1.7116 1.0061 -0.0641 0.1071 -0.1991 151 ILE A CG2 1204 C CD1 . ILE A 151 ? 1.5113 1.8371 1.0931 -0.0699 0.1162 -0.2221 151 ILE A CD1 1205 N N . LYS A 152 ? 1.5928 1.7723 1.0014 -0.0747 0.1411 -0.1895 152 LYS A N 1206 C CA . LYS A 152 ? 1.6541 1.8093 1.0143 -0.0787 0.1531 -0.1888 152 LYS A CA 1207 C C . LYS A 152 ? 1.6490 1.8362 1.0229 -0.0944 0.1654 -0.2001 152 LYS A C 1208 O O . LYS A 152 ? 1.5822 1.8137 1.0035 -0.0920 0.1583 -0.2101 152 LYS A O 1209 C CB . LYS A 152 ? 1.6655 1.8066 1.0048 -0.0537 0.1389 -0.1872 152 LYS A CB 1210 C CG . LYS A 152 ? 1.6301 1.8137 1.0116 -0.0409 0.1243 -0.1983 152 LYS A CG 1211 C CD . LYS A 152 ? 1.6549 1.8252 1.0165 -0.0165 0.1091 -0.1970 152 LYS A CD 1212 C CE . LYS A 152 ? 1.6165 1.8215 1.0042 -0.0081 0.1004 -0.2091 152 LYS A CE 1213 N NZ . LYS A 152 ? 1.6328 1.8314 1.0094 0.0159 0.0831 -0.2094 152 LYS A NZ 1214 N N . LYS A 153 ? 1.7336 1.8969 1.0637 -0.1100 0.1844 -0.1985 153 LYS A N 1215 C CA . LYS A 153 ? 1.7606 1.9523 1.0974 -0.1262 0.1984 -0.2093 153 LYS A CA 1216 C C . LYS A 153 ? 1.7868 1.9581 1.0810 -0.1193 0.2025 -0.2095 153 LYS A C 1217 O O . LYS A 153 ? 1.8294 1.9527 1.0671 -0.1228 0.2126 -0.2007 153 LYS A O 1218 C CB . LYS A 153 ? 1.7823 1.9691 1.1072 -0.1557 0.2203 -0.2095 153 LYS A CB 1219 C CG . LYS A 153 ? 1.7851 2.0050 1.1176 -0.1745 0.2364 -0.2217 153 LYS A CG 1220 C CD . LYS A 153 ? 1.7947 2.0361 1.1465 -0.2011 0.2511 -0.2266 153 LYS A CD 1221 C CE . LYS A 153 ? 1.8341 2.0839 1.1641 -0.2265 0.2748 -0.2346 153 LYS A CE 1222 N NZ . LYS A 153 ? 1.8313 2.1219 1.1817 -0.2203 0.2734 -0.2468 153 LYS A NZ 1223 N N . ASN A 154 ? 1.7482 1.9543 1.0679 -0.1092 0.1946 -0.2196 154 ASN A N 1224 C CA . ASN A 154 ? 1.8012 1.9934 1.0867 -0.0989 0.1949 -0.2211 154 ASN A CA 1225 C C . ASN A 154 ? 1.8427 1.9905 1.0886 -0.0775 0.1831 -0.2102 154 ASN A C 1226 O O . ASN A 154 ? 1.8746 1.9835 1.0651 -0.0763 0.1916 -0.2046 154 ASN A O 1227 C CB . ASN A 154 ? 1.8332 2.0138 1.0810 -0.1213 0.2194 -0.2232 154 ASN A CB 1228 C CG . ASN A 154 ? 1.8681 2.0498 1.0939 -0.1123 0.2202 -0.2285 154 ASN A CG 1229 O OD1 . ASN A 154 ? 1.8656 2.0703 1.1165 -0.0925 0.2032 -0.2342 154 ASN A OD1 1230 N ND2 . ASN A 154 ? 1.9064 2.0622 1.0838 -0.1279 0.2405 -0.2271 154 ASN A ND2 1231 N N . SER A 155 ? 1.8320 1.9869 1.1063 -0.0602 0.1636 -0.2077 155 SER A N 1232 C CA . SER A 155 ? 1.8754 1.9971 1.1206 -0.0372 0.1495 -0.1992 155 SER A CA 1233 C C . SER A 155 ? 1.9235 1.9883 1.1097 -0.0414 0.1605 -0.1859 155 SER A C 1234 O O . SER A 155 ? 2.0012 2.0294 1.1387 -0.0263 0.1579 -0.1799 155 SER A O 1235 C CB . SER A 155 ? 1.8907 2.0142 1.1195 -0.0190 0.1406 -0.2042 155 SER A CB 1236 O OG . SER A 155 ? 1.8419 2.0140 1.1216 -0.0146 0.1304 -0.2166 155 SER A OG 1237 N N . THR A 156 ? 1.9052 1.9613 1.0937 -0.0613 0.1730 -0.1816 156 THR A N 1238 C CA . THR A 156 ? 1.9336 1.9336 1.0681 -0.0656 0.1830 -0.1688 156 THR A CA 1239 C C . THR A 156 ? 1.9061 1.9095 1.0663 -0.0778 0.1848 -0.1651 156 THR A C 1240 O O . THR A 156 ? 1.8665 1.9062 1.0679 -0.0967 0.1916 -0.1724 156 THR A O 1241 C CB . THR A 156 ? 1.9583 1.9250 1.0388 -0.0866 0.2078 -0.1668 156 THR A CB 1242 O OG1 . THR A 156 ? 1.9645 1.9387 1.0306 -0.0796 0.2082 -0.1728 156 THR A OG1 1243 C CG2 . THR A 156 ? 2.0177 1.9156 1.0294 -0.0841 0.2156 -0.1528 156 THR A CG2 1244 N N . TYR A 157 ? 1.9164 1.8823 1.0512 -0.0657 0.1785 -0.1542 157 TYR A N 1245 C CA . TYR A 157 ? 1.9082 1.8661 1.0547 -0.0774 0.1823 -0.1489 157 TYR A CA 1246 C C . TYR A 157 ? 1.9344 1.8256 1.0100 -0.0832 0.1968 -0.1369 157 TYR A C 1247 O O . TYR A 157 ? 1.9262 1.7813 0.9713 -0.0629 0.1872 -0.1275 157 TYR A O 1248 C CB . TYR A 157 ? 1.8877 1.8651 1.0746 -0.0569 0.1602 -0.1476 157 TYR A CB 1249 C CG . TYR A 157 ? 1.8790 1.8730 1.1040 -0.0709 0.1618 -0.1471 157 TYR A CG 1250 C CD1 . TYR A 157 ? 1.9031 1.8562 1.0958 -0.0808 0.1720 -0.1374 157 TYR A CD1 1251 C CD2 . TYR A 157 ? 1.8288 1.8772 1.1198 -0.0736 0.1532 -0.1563 157 TYR A CD2 1252 C CE1 . TYR A 157 ? 1.8609 1.8297 1.0880 -0.0932 0.1731 -0.1373 157 TYR A CE1 1253 C CE2 . TYR A 157 ? 1.7762 1.8395 1.1005 -0.0850 0.1543 -0.1559 157 TYR A CE2 1254 C CZ . TYR A 157 ? 1.7936 1.8183 1.0869 -0.0950 0.1640 -0.1466 157 TYR A CZ 1255 O OH . TYR A 157 ? 1.7295 1.7699 1.0563 -0.1061 0.1646 -0.1467 157 TYR A OH 1256 N N . PRO A 158 ? 1.9419 1.8159 0.9888 -0.1109 0.2203 -0.1377 158 PRO A N 1257 C CA . PRO A 158 ? 2.0047 1.8114 0.9818 -0.1194 0.2361 -0.1265 158 PRO A CA 1258 C C . PRO A 158 ? 1.9875 1.7796 0.9725 -0.1236 0.2347 -0.1199 158 PRO A C 1259 O O . PRO A 158 ? 1.9372 1.7745 0.9817 -0.1316 0.2294 -0.1257 158 PRO A O 1260 C CB . PRO A 158 ? 2.0362 1.8407 0.9941 -0.1525 0.2620 -0.1320 158 PRO A CB 1261 C CG . PRO A 158 ? 1.9688 1.8453 0.9992 -0.1652 0.2598 -0.1457 158 PRO A CG 1262 C CD . PRO A 158 ? 1.9200 1.8360 0.9978 -0.1362 0.2339 -0.1494 158 PRO A CD 1263 N N . THR A 159 ? 2.0374 1.7655 0.9611 -0.1168 0.2392 -0.1078 159 THR A N 1264 C CA . THR A 159 ? 2.0178 1.7258 0.9421 -0.1191 0.2380 -0.1007 159 THR A CA 1265 C C . THR A 159 ? 1.9866 1.7146 0.9365 -0.1552 0.2555 -0.1065 159 THR A C 1266 O O . THR A 159 ? 1.9417 1.6558 0.8634 -0.1817 0.2773 -0.1095 159 THR A O 1267 C CB . THR A 159 ? 2.1113 1.7397 0.9548 -0.1088 0.2442 -0.0870 159 THR A CB 1268 O OG1 . THR A 159 ? 2.1397 1.7534 0.9589 -0.0740 0.2276 -0.0830 159 THR A OG1 1269 C CG2 . THR A 159 ? 2.1147 1.7239 0.9610 -0.1075 0.2406 -0.0799 159 THR A CG2 1270 N N . ILE A 160 ? 1.9539 1.7172 0.9585 -0.1556 0.2453 -0.1087 160 ILE A N 1271 C CA . ILE A 160 ? 1.9449 1.7308 0.9787 -0.1863 0.2585 -0.1144 160 ILE A CA 1272 C C . ILE A 160 ? 2.0053 1.7323 0.9904 -0.1977 0.2706 -0.1044 160 ILE A C 1273 O O . ILE A 160 ? 2.0150 1.7096 0.9812 -0.1760 0.2591 -0.0945 160 ILE A O 1274 C CB . ILE A 160 ? 1.8407 1.6896 0.9538 -0.1796 0.2413 -0.1212 160 ILE A CB 1275 C CG1 . ILE A 160 ? 1.8040 1.7114 0.9641 -0.1755 0.2340 -0.1331 160 ILE A CG1 1276 C CG2 . ILE A 160 ? 1.8178 1.6819 0.9551 -0.2065 0.2523 -0.1248 160 ILE A CG2 1277 C CD1 . ILE A 160 ? 1.7334 1.6954 0.9637 -0.1611 0.2138 -0.1386 160 ILE A CD1 1278 N N . LYS A 161 ? 2.0394 1.7529 1.0032 -0.2319 0.2942 -0.1076 161 LYS A N 1279 C CA . LYS A 161 ? 2.1215 1.7812 1.0413 -0.2481 0.3081 -0.0999 161 LYS A CA 1280 C C . LYS A 161 ? 2.1087 1.8031 1.0621 -0.2844 0.3233 -0.1101 161 LYS A C 1281 O O . LYS A 161 ? 2.1330 1.8235 1.0647 -0.3136 0.3450 -0.1164 161 LYS A O 1282 C CB . LYS A 161 ? 2.2537 1.8370 1.0846 -0.2539 0.3261 -0.0915 161 LYS A CB 1283 C CG . LYS A 161 ? 2.3202 1.8587 1.1065 -0.2166 0.3119 -0.0801 161 LYS A CG 1284 C CD . LYS A 161 ? 2.4193 1.8880 1.1190 -0.2225 0.3305 -0.0737 161 LYS A CD 1285 C CE . LYS A 161 ? 2.4673 1.8980 1.1248 -0.1826 0.3149 -0.0639 161 LYS A CE 1286 N NZ . LYS A 161 ? 2.5372 1.9113 1.1178 -0.1861 0.3313 -0.0597 161 LYS A NZ 1287 N N . ARG A 162 ? 2.0644 1.7945 1.0710 -0.2824 0.3120 -0.1124 162 ARG A N 1288 C CA . ARG A 162 ? 2.0495 1.8188 1.0937 -0.3135 0.3233 -0.1229 162 ARG A CA 1289 C C . ARG A 162 ? 2.0866 1.8258 1.1200 -0.3204 0.3252 -0.1165 162 ARG A C 1290 O O . ARG A 162 ? 2.1260 1.8286 1.1402 -0.2964 0.3128 -0.1049 162 ARG A O 1291 C CB . ARG A 162 ? 1.9783 1.8291 1.1046 -0.3059 0.3078 -0.1343 162 ARG A CB 1292 C CG . ARG A 162 ? 1.9841 1.8714 1.1280 -0.2990 0.3050 -0.1422 162 ARG A CG 1293 C CD . ARG A 162 ? 2.0420 1.9313 1.1615 -0.3305 0.3295 -0.1510 162 ARG A CD 1294 N NE . ARG A 162 ? 2.0026 1.9656 1.1805 -0.3367 0.3276 -0.1662 162 ARG A NE 1295 C CZ . ARG A 162 ? 1.9489 1.9639 1.1762 -0.3537 0.3301 -0.1774 162 ARG A CZ 1296 N NH1 . ARG A 162 ? 1.9152 1.9182 1.1425 -0.3682 0.3350 -0.1754 162 ARG A NH1 1297 N NH2 . ARG A 162 ? 1.9056 1.9854 1.1817 -0.3552 0.3274 -0.1911 162 ARG A NH2 1298 N N . SER A 163 ? 2.0534 1.8110 1.1007 -0.3532 0.3406 -0.1250 163 SER A N 1299 C CA . SER A 163 ? 2.0147 1.7424 1.0482 -0.3647 0.3455 -0.1202 163 SER A CA 1300 C C . SER A 163 ? 1.9635 1.7437 1.0435 -0.3948 0.3544 -0.1338 163 SER A C 1301 O O . SER A 163 ? 1.9071 1.7067 0.9844 -0.4238 0.3727 -0.1448 163 SER A O 1302 C CB . SER A 163 ? 2.0957 1.7391 1.0426 -0.3788 0.3654 -0.1109 163 SER A CB 1303 O OG . SER A 163 ? 2.1807 1.7897 1.1101 -0.3882 0.3697 -0.1057 163 SER A OG 1304 N N . TYR A 164 ? 1.9228 1.7279 1.0457 -0.3872 0.3413 -0.1337 164 TYR A N 1305 C CA . TYR A 164 ? 1.8871 1.7369 1.0497 -0.4140 0.3488 -0.1459 164 TYR A CA 1306 C C . TYR A 164 ? 1.9385 1.7395 1.0657 -0.4300 0.3587 -0.1399 164 TYR A C 1307 O O . TYR A 164 ? 1.9906 1.7423 1.0894 -0.4097 0.3499 -0.1263 164 TYR A O 1308 C CB . TYR A 164 ? 1.7971 1.7164 1.0374 -0.3959 0.3277 -0.1521 164 TYR A CB 1309 C CG . TYR A 164 ? 1.8099 1.7726 1.0884 -0.4204 0.3340 -0.1640 164 TYR A CG 1310 C CD1 . TYR A 164 ? 1.8111 1.8272 1.1161 -0.4445 0.3459 -0.1805 164 TYR A CD1 1311 C CD2 . TYR A 164 ? 1.8217 1.7720 1.1075 -0.4195 0.3287 -0.1593 164 TYR A CD2 1312 C CE1 . TYR A 164 ? 1.8129 1.8715 1.1524 -0.4662 0.3513 -0.1926 164 TYR A CE1 1313 C CE2 . TYR A 164 ? 1.8126 1.8028 1.1321 -0.4415 0.3341 -0.1707 164 TYR A CE2 1314 C CZ . TYR A 164 ? 1.8127 1.8576 1.1590 -0.4646 0.3452 -0.1876 164 TYR A CZ 1315 O OH . TYR A 164 ? 1.8248 1.9122 1.2046 -0.4852 0.3498 -0.1998 164 TYR A OH 1316 N N . ASN A 165 ? 1.9533 1.7706 1.0834 -0.4663 0.3769 -0.1512 165 ASN A N 1317 C CA . ASN A 165 ? 2.0059 1.7802 1.1028 -0.4873 0.3891 -0.1482 165 ASN A CA 1318 C C . ASN A 165 ? 1.9911 1.8251 1.1481 -0.4993 0.3845 -0.1595 165 ASN A C 1319 O O . ASN A 165 ? 1.9829 1.8800 1.1811 -0.5174 0.3900 -0.1754 165 ASN A O 1320 C CB . ASN A 165 ? 2.0972 1.8304 1.1342 -0.5243 0.4181 -0.1522 165 ASN A CB 1321 C CG . ASN A 165 ? 2.1537 1.8443 1.1554 -0.5520 0.4337 -0.1517 165 ASN A CG 1322 O OD1 . ASN A 165 ? 2.0790 1.8086 1.1225 -0.5632 0.4308 -0.1597 165 ASN A OD1 1323 N ND2 . ASN A 165 ? 2.2609 1.8685 1.1822 -0.5633 0.4509 -0.1424 165 ASN A ND2 1324 N N . ASN A 166 ? 2.0196 1.8335 1.1799 -0.4884 0.3746 -0.1517 166 ASN A N 1325 C CA . ASN A 166 ? 1.9772 1.8423 1.1914 -0.4966 0.3687 -0.1610 166 ASN A CA 1326 C C . ASN A 166 ? 1.9929 1.8501 1.1851 -0.5393 0.3920 -0.1712 166 ASN A C 1327 O O . ASN A 166 ? 2.0053 1.8132 1.1625 -0.5487 0.3982 -0.1649 166 ASN A O 1328 C CB . ASN A 166 ? 1.9838 1.8278 1.2071 -0.4690 0.3500 -0.1486 166 ASN A CB 1329 C CG . ASN A 166 ? 1.9526 1.8589 1.2418 -0.4675 0.3382 -0.1573 166 ASN A CG 1330 O OD1 . ASN A 166 ? 1.9412 1.9130 1.2763 -0.4790 0.3393 -0.1721 166 ASN A OD1 1331 N ND2 . ASN A 166 ? 1.9378 1.8242 1.2311 -0.4519 0.3265 -0.1483 166 ASN A ND2 1332 N N . THR A 167 ? 1.9739 1.8806 1.1862 -0.5653 0.4051 -0.1877 167 THR A N 1333 C CA . THR A 167 ? 2.0329 1.9419 1.2285 -0.6092 0.4285 -0.2006 167 THR A CA 1334 C C . THR A 167 ? 1.9959 1.9587 1.2446 -0.6169 0.4216 -0.2113 167 THR A C 1335 O O . THR A 167 ? 2.0457 1.9851 1.2724 -0.6424 0.4339 -0.2143 167 THR A O 1336 C CB . THR A 167 ? 2.0492 1.9979 1.2494 -0.6344 0.4452 -0.2159 167 THR A CB 1337 O OG1 . THR A 167 ? 1.9918 2.0190 1.2592 -0.6140 0.4286 -0.2246 167 THR A OG1 1338 C CG2 . THR A 167 ? 2.1087 1.9937 1.2433 -0.6356 0.4579 -0.2062 167 THR A CG2 1339 N N . ASN A 168 ? 1.9268 1.9609 1.2436 -0.5950 0.4025 -0.2177 168 ASN A N 1340 C CA . ASN A 168 ? 1.8607 1.9468 1.2313 -0.5934 0.3913 -0.2261 168 ASN A CA 1341 C C . ASN A 168 ? 1.8379 1.8773 1.1927 -0.5835 0.3834 -0.2134 168 ASN A C 1342 O O . ASN A 168 ? 1.8421 1.8193 1.1599 -0.5628 0.3773 -0.1958 168 ASN A O 1343 C CB . ASN A 168 ? 1.7668 1.9231 1.2047 -0.5636 0.3696 -0.2309 168 ASN A CB 1344 C CG . ASN A 168 ? 1.7553 1.8870 1.1872 -0.5280 0.3545 -0.2162 168 ASN A CG 1345 O OD1 . ASN A 168 ? 1.7047 1.8819 1.1722 -0.5116 0.3449 -0.2213 168 ASN A OD1 1346 N ND2 . ASN A 168 ? 1.7900 1.8497 1.1755 -0.5157 0.3525 -0.1987 168 ASN A ND2 1347 N N . GLN A 169 ? 1.7892 1.8635 1.1745 -0.5969 0.3828 -0.2234 169 GLN A N 1348 C CA . GLN A 169 ? 1.8361 1.8678 1.2016 -0.5987 0.3813 -0.2154 169 GLN A CA 1349 C C . GLN A 169 ? 1.8160 1.8305 1.1974 -0.5584 0.3576 -0.1993 169 GLN A C 1350 O O . GLN A 169 ? 1.7874 1.7495 1.1386 -0.5553 0.3568 -0.1885 169 GLN A O 1351 C CB . GLN A 169 ? 1.8345 1.9190 1.2349 -0.6237 0.3862 -0.2329 169 GLN A CB 1352 C CG . GLN A 169 ? 1.8945 1.9655 1.2581 -0.6705 0.4132 -0.2453 169 GLN A CG 1353 C CD . GLN A 169 ? 2.0117 2.0230 1.3333 -0.6867 0.4216 -0.2393 169 GLN A CD 1354 O OE1 . GLN A 169 ? 1.8730 1.8974 1.2212 -0.6762 0.4091 -0.2383 169 GLN A OE1 1355 N NE2 . GLN A 169 ? 2.1269 2.0702 1.3804 -0.7128 0.4435 -0.2355 169 GLN A NE2 1356 N N . GLU A 170 ? 1.7795 1.8383 1.2075 -0.5286 0.3390 -0.1986 170 GLU A N 1357 C CA . GLU A 170 ? 1.6854 1.7437 1.1402 -0.4922 0.3160 -0.1869 170 GLU A CA 1358 C C . GLU A 170 ? 1.7019 1.6992 1.1181 -0.4665 0.3091 -0.1683 170 GLU A C 1359 O O . GLU A 170 ? 1.7475 1.6999 1.1138 -0.4751 0.3217 -0.1637 170 GLU A O 1360 C CB . GLU A 170 ? 1.6185 1.7519 1.1398 -0.4730 0.2997 -0.1957 170 GLU A CB 1361 C CG . GLU A 170 ? 1.6045 1.8018 1.1733 -0.4856 0.2985 -0.2118 170 GLU A CG 1362 C CD . GLU A 170 ? 1.6380 1.8621 1.1999 -0.5239 0.3191 -0.2293 170 GLU A CD 1363 O OE1 . GLU A 170 ? 1.8022 1.9848 1.3219 -0.5507 0.3354 -0.2289 170 GLU A OE1 1364 O OE2 . GLU A 170 ? 1.6187 1.9056 1.2166 -0.5278 0.3194 -0.2441 170 GLU A OE2 1365 N N . ASP A 171 ? 1.7063 1.7023 1.1447 -0.4348 0.2894 -0.1582 171 ASP A N 1366 C CA . ASP A 171 ? 1.6981 1.6604 1.1191 -0.4044 0.2778 -0.1439 171 ASP A CA 1367 C C . ASP A 171 ? 1.6258 1.6428 1.0912 -0.3889 0.2671 -0.1502 171 ASP A C 1368 O O . ASP A 171 ? 1.5605 1.6385 1.0773 -0.3910 0.2617 -0.1617 171 ASP A O 1369 C CB . ASP A 171 ? 1.7421 1.6852 1.1714 -0.3782 0.2615 -0.1321 171 ASP A CB 1370 C CG . ASP A 171 ? 1.8356 1.7203 1.2187 -0.3897 0.2707 -0.1248 171 ASP A CG 1371 O OD1 . ASP A 171 ? 1.9155 1.7401 1.2383 -0.3970 0.2829 -0.1177 171 ASP A OD1 1372 O OD2 . ASP A 171 ? 1.8378 1.7344 1.2429 -0.3903 0.2655 -0.1259 171 ASP A OD2 1373 N N . LEU A 172 ? 1.6268 1.6210 1.0707 -0.3725 0.2638 -0.1428 172 LEU A N 1374 C CA . LEU A 172 ? 1.5577 1.5979 1.0368 -0.3592 0.2553 -0.1487 172 LEU A CA 1375 C C . LEU A 172 ? 1.5229 1.5536 1.0116 -0.3237 0.2359 -0.1377 172 LEU A C 1376 O O . LEU A 172 ? 1.5873 1.5648 1.0339 -0.3117 0.2349 -0.1255 172 LEU A O 1377 C CB . LEU A 172 ? 1.5951 1.6236 1.0405 -0.3759 0.2710 -0.1529 172 LEU A CB 1378 C CG . LEU A 172 ? 1.5684 1.6535 1.0511 -0.3727 0.2679 -0.1640 172 LEU A CG 1379 C CD1 . LEU A 172 ? 1.5194 1.6662 1.0442 -0.3930 0.2733 -0.1809 172 LEU A CD1 1380 C CD2 . LEU A 172 ? 1.6217 1.6804 1.0617 -0.3812 0.2808 -0.1634 172 LEU A CD2 1381 N N . LEU A 173 ? 1.4335 1.5157 0.9765 -0.3068 0.2208 -0.1428 173 LEU A N 1382 C CA . LEU A 173 ? 1.3862 1.4669 0.9426 -0.2754 0.2031 -0.1350 173 LEU A CA 1383 C C . LEU A 173 ? 1.4008 1.4935 0.9544 -0.2699 0.2033 -0.1384 173 LEU A C 1384 O O . LEU A 173 ? 1.3699 1.5115 0.9588 -0.2735 0.2024 -0.1496 173 LEU A O 1385 C CB . LEU A 173 ? 1.3403 1.4663 0.9537 -0.2603 0.1872 -0.1385 173 LEU A CB 1386 C CG . LEU A 173 ? 1.3170 1.4490 0.9493 -0.2305 0.1696 -0.1331 173 LEU A CG 1387 C CD1 . LEU A 173 ? 1.3526 1.4346 0.9518 -0.2149 0.1643 -0.1193 173 LEU A CD1 1388 C CD2 . LEU A 173 ? 1.2411 1.4187 0.9284 -0.2185 0.1561 -0.1383 173 LEU A CD2 1389 N N . VAL A 174 ? 1.4290 1.4770 0.9397 -0.2596 0.2039 -0.1290 174 VAL A N 1390 C CA . VAL A 174 ? 1.4207 1.4742 0.9236 -0.2521 0.2033 -0.1310 174 VAL A CA 1391 C C . VAL A 174 ? 1.3734 1.4329 0.8954 -0.2206 0.1837 -0.1256 174 VAL A C 1392 O O . VAL A 174 ? 1.3844 1.4146 0.8935 -0.2047 0.1753 -0.1156 174 VAL A O 1393 C CB . VAL A 174 ? 1.5094 1.5076 0.9470 -0.2617 0.2178 -0.1249 174 VAL A CB 1394 C CG1 . VAL A 174 ? 1.5284 1.5330 0.9578 -0.2529 0.2167 -0.1270 174 VAL A CG1 1395 C CG2 . VAL A 174 ? 1.5457 1.5351 0.9610 -0.2959 0.2390 -0.1309 174 VAL A CG2 1396 N N . LEU A 175 ? 1.3285 1.4264 0.8802 -0.2123 0.1770 -0.1329 175 LEU A N 1397 C CA . LEU A 175 ? 1.3187 1.4277 0.8914 -0.1850 0.1591 -0.1302 175 LEU A CA 1398 C C . LEU A 175 ? 1.3359 1.4417 0.8899 -0.1785 0.1598 -0.1319 175 LEU A C 1399 O O . LEU A 175 ? 1.3476 1.4681 0.8977 -0.1940 0.1709 -0.1396 175 LEU A O 1400 C CB . LEU A 175 ? 1.2823 1.4444 0.9142 -0.1791 0.1484 -0.1385 175 LEU A CB 1401 C CG . LEU A 175 ? 1.2874 1.4610 0.9456 -0.1830 0.1456 -0.1383 175 LEU A CG 1402 C CD1 . LEU A 175 ? 1.2671 1.4937 0.9719 -0.1888 0.1441 -0.1505 175 LEU A CD1 1403 C CD2 . LEU A 175 ? 1.2738 1.4356 0.9423 -0.1611 0.1305 -0.1299 175 LEU A CD2 1404 N N . TRP A 176 ? 1.3050 1.3940 0.8485 -0.1554 0.1477 -0.1254 176 TRP A N 1405 C CA . TRP A 176 ? 1.3265 1.4155 0.8561 -0.1459 0.1455 -0.1274 176 TRP A CA 1406 C C . TRP A 176 ? 1.3158 1.4133 0.8641 -0.1186 0.1265 -0.1250 176 TRP A C 1407 O O . TRP A 176 ? 1.2983 1.4029 0.8710 -0.1090 0.1163 -0.1222 176 TRP A O 1408 C CB . TRP A 176 ? 1.4023 1.4405 0.8685 -0.1521 0.1584 -0.1207 176 TRP A CB 1409 C CG . TRP A 176 ? 1.4348 1.4246 0.8628 -0.1382 0.1544 -0.1086 176 TRP A CG 1410 C CD1 . TRP A 176 ? 1.4535 1.4208 0.8575 -0.1142 0.1441 -0.1025 176 TRP A CD1 1411 C CD2 . TRP A 176 ? 1.4591 1.4174 0.8672 -0.1462 0.1605 -0.1016 176 TRP A CD2 1412 N NE1 . TRP A 176 ? 1.4716 1.3960 0.8417 -0.1055 0.1432 -0.0921 176 TRP A NE1 1413 C CE2 . TRP A 176 ? 1.4875 1.4038 0.8588 -0.1250 0.1533 -0.0911 176 TRP A CE2 1414 C CE3 . TRP A 176 ? 1.4636 1.4259 0.8811 -0.1687 0.1710 -0.1039 176 TRP A CE3 1415 C CZ2 . TRP A 176 ? 1.5121 1.3885 0.8548 -0.1252 0.1566 -0.0823 176 TRP A CZ2 1416 C CZ3 . TRP A 176 ? 1.4853 1.4076 0.8747 -0.1703 0.1744 -0.0952 176 TRP A CZ3 1417 C CH2 . TRP A 176 ? 1.5116 1.3905 0.8636 -0.1485 0.1673 -0.0844 176 TRP A CH2 1418 N N . GLY A 177 ? 1.3645 1.4630 0.9021 -0.1070 0.1220 -0.1268 177 GLY A N 1419 C CA . GLY A 177 ? 1.3334 1.4426 0.8882 -0.0825 0.1042 -0.1263 177 GLY A CA 1420 C C . GLY A 177 ? 1.3515 1.4437 0.8738 -0.0690 0.1012 -0.1251 177 GLY A C 1421 O O . GLY A 177 ? 1.3826 1.4569 0.8705 -0.0786 0.1130 -0.1254 177 GLY A O 1422 N N . ILE A 178 ? 1.3232 1.4224 0.8568 -0.0469 0.0852 -0.1245 178 ILE A N 1423 C CA . ILE A 178 ? 1.3589 1.4480 0.8670 -0.0306 0.0791 -0.1247 178 ILE A CA 1424 C C . ILE A 178 ? 1.3333 1.4640 0.8852 -0.0186 0.0644 -0.1336 178 ILE A C 1425 O O . ILE A 178 ? 1.2866 1.4408 0.8782 -0.0147 0.0552 -0.1357 178 ILE A O 1426 C CB . ILE A 178 ? 1.4115 1.4612 0.8784 -0.0128 0.0740 -0.1149 178 ILE A CB 1427 C CG1 . ILE A 178 ? 1.4777 1.5162 0.9140 0.0046 0.0681 -0.1156 178 ILE A CG1 1428 C CG2 . ILE A 178 ? 1.3903 1.4539 0.8874 0.0009 0.0602 -0.1133 178 ILE A CG2 1429 C CD1 . ILE A 178 ? 1.5534 1.5483 0.9389 0.0228 0.0652 -0.1060 178 ILE A CD1 1430 N N . HIS A 179 ? 1.3599 1.4981 0.9031 -0.0135 0.0629 -0.1391 179 HIS A N 1431 C CA . HIS A 179 ? 1.3342 1.5083 0.9136 -0.0023 0.0494 -0.1482 179 HIS A CA 1432 C C . HIS A 179 ? 1.3438 1.5099 0.9075 0.0207 0.0357 -0.1468 179 HIS A C 1433 O O . HIS A 179 ? 1.3828 1.5203 0.9013 0.0289 0.0379 -0.1425 179 HIS A O 1434 C CB . HIS A 179 ? 1.3432 1.5355 0.9274 -0.0105 0.0550 -0.1567 179 HIS A CB 1435 C CG . HIS A 179 ? 1.3118 1.5372 0.9293 0.0002 0.0421 -0.1665 179 HIS A CG 1436 N ND1 . HIS A 179 ? 1.3319 1.5641 0.9389 0.0047 0.0411 -0.1728 179 HIS A ND1 1437 C CD2 . HIS A 179 ? 1.2602 1.5115 0.9190 0.0067 0.0301 -0.1712 179 HIS A CD2 1438 C CE1 . HIS A 179 ? 1.3132 1.5743 0.9541 0.0132 0.0289 -0.1812 179 HIS A CE1 1439 N NE2 . HIS A 179 ? 1.2986 1.5712 0.9710 0.0140 0.0224 -0.1805 179 HIS A NE2 1440 N N . HIS A 180 ? 1.3267 1.5184 0.9270 0.0309 0.0220 -0.1510 180 HIS A N 1441 C CA . HIS A 180 ? 1.3436 1.5378 0.9380 0.0522 0.0077 -0.1523 180 HIS A CA 1442 C C . HIS A 180 ? 1.3733 1.6012 0.9966 0.0554 -0.0007 -0.1641 180 HIS A C 1443 O O . HIS A 180 ? 1.3977 1.6542 1.0639 0.0535 -0.0074 -0.1704 180 HIS A O 1444 C CB . HIS A 180 ? 1.3414 1.5423 0.9576 0.0596 -0.0011 -0.1496 180 HIS A CB 1445 C CG . HIS A 180 ? 1.3824 1.5498 0.9709 0.0579 0.0061 -0.1382 180 HIS A CG 1446 N ND1 . HIS A 180 ? 1.4692 1.5986 1.0049 0.0680 0.0091 -0.1304 180 HIS A ND1 1447 C CD2 . HIS A 180 ? 1.3580 1.5218 0.9618 0.0477 0.0110 -0.1334 180 HIS A CD2 1448 C CE1 . HIS A 180 ? 1.4386 1.5413 0.9575 0.0635 0.0159 -0.1213 180 HIS A CE1 1449 N NE2 . HIS A 180 ? 1.4089 1.5331 0.9696 0.0509 0.0170 -0.1231 180 HIS A NE2 1450 N N . PRO A 181 ? 1.4286 1.6515 1.0269 0.0600 0.0002 -0.1674 181 PRO A N 1451 C CA . PRO A 181 ? 1.4193 1.6730 1.0436 0.0624 -0.0072 -0.1791 181 PRO A CA 1452 C C . PRO A 181 ? 1.3985 1.6712 1.0391 0.0792 -0.0240 -0.1850 181 PRO A C 1453 O O . PRO A 181 ? 1.3631 1.6251 0.9905 0.0914 -0.0300 -0.1798 181 PRO A O 1454 C CB . PRO A 181 ? 1.4832 1.7213 1.0694 0.0636 -0.0010 -0.1797 181 PRO A CB 1455 C CG . PRO A 181 ? 1.5207 1.7196 1.0569 0.0716 0.0030 -0.1688 181 PRO A CG 1456 C CD . PRO A 181 ? 1.4933 1.6801 1.0362 0.0642 0.0077 -0.1606 181 PRO A CD 1457 N N . ASN A 182 ? 1.4134 1.7149 1.0819 0.0797 -0.0311 -0.1964 182 ASN A N 1458 C CA . ASN A 182 ? 1.4305 1.7555 1.1202 0.0919 -0.0463 -0.2045 182 ASN A CA 1459 C C . ASN A 182 ? 1.4634 1.7825 1.1204 0.1111 -0.0551 -0.2061 182 ASN A C 1460 O O . ASN A 182 ? 1.4712 1.7979 1.1302 0.1246 -0.0658 -0.2072 182 ASN A O 1461 C CB . ASN A 182 ? 1.4330 1.7872 1.1601 0.0846 -0.0498 -0.2169 182 ASN A CB 1462 C CG . ASN A 182 ? 1.4358 1.8157 1.1869 0.0936 -0.0643 -0.2268 182 ASN A CG 1463 O OD1 . ASN A 182 ? 1.4773 1.8715 1.2291 0.0989 -0.0711 -0.2367 182 ASN A OD1 1464 N ND2 . ASN A 182 ? 1.4436 1.8301 1.2144 0.0944 -0.0686 -0.2248 182 ASN A ND2 1465 N N . ASP A 183 ? 1.4985 1.8052 1.1253 0.1128 -0.0505 -0.2066 183 ASP A N 1466 C CA . ASP A 183 ? 1.5615 1.8629 1.1554 0.1318 -0.0591 -0.2091 183 ASP A CA 1467 C C . ASP A 183 ? 1.5685 1.8367 1.1120 0.1327 -0.0485 -0.2023 183 ASP A C 1468 O O . ASP A 183 ? 1.5136 1.7665 1.0505 0.1165 -0.0341 -0.1970 183 ASP A O 1469 C CB . ASP A 183 ? 1.5763 1.9117 1.1960 0.1360 -0.0706 -0.2241 183 ASP A CB 1470 C CG . ASP A 183 ? 1.5778 1.9225 1.2131 0.1213 -0.0634 -0.2303 183 ASP A CG 1471 O OD1 . ASP A 183 ? 1.6361 1.9606 1.2428 0.1166 -0.0526 -0.2257 183 ASP A OD1 1472 O OD2 . ASP A 183 ? 1.5568 1.9284 1.2316 0.1145 -0.0682 -0.2401 183 ASP A OD2 1473 N N . ALA A 184 ? 1.5663 1.8246 1.0741 0.1516 -0.0558 -0.2031 184 ALA A N 1474 C CA . ALA A 184 ? 1.5592 1.7820 1.0126 0.1551 -0.0465 -0.1964 184 ALA A CA 1475 C C . ALA A 184 ? 1.5497 1.7777 1.0057 0.1409 -0.0371 -0.2015 184 ALA A C 1476 O O . ALA A 184 ? 1.5204 1.7190 0.9409 0.1330 -0.0229 -0.1946 184 ALA A O 1477 C CB . ALA A 184 ? 1.5559 1.7711 0.9732 0.1811 -0.0585 -0.1979 184 ALA A CB 1478 N N . ALA A 185 ? 1.5488 1.8134 1.0453 0.1375 -0.0445 -0.2140 185 ALA A N 1479 C CA . ALA A 185 ? 1.5471 1.8211 1.0500 0.1259 -0.0372 -0.2205 185 ALA A CA 1480 C C . ALA A 185 ? 1.5686 1.8404 1.0891 0.1037 -0.0221 -0.2166 185 ALA A C 1481 O O . ALA A 185 ? 1.5754 1.8368 1.0781 0.0934 -0.0093 -0.2156 185 ALA A O 1482 C CB . ALA A 185 ? 1.5117 1.8232 1.0523 0.1290 -0.0498 -0.2351 185 ALA A CB 1483 N N . GLU A 186 ? 1.6096 1.8931 1.1652 0.0965 -0.0235 -0.2151 186 GLU A N 1484 C CA . GLU A 186 ? 1.6337 1.9172 1.2077 0.0770 -0.0104 -0.2116 186 GLU A CA 1485 C C . GLU A 186 ? 1.6023 1.8496 1.1348 0.0701 0.0041 -0.1995 186 GLU A C 1486 O O . GLU A 186 ? 1.5740 1.8172 1.1021 0.0542 0.0183 -0.1986 186 GLU A O 1487 C CB . GLU A 186 ? 1.6915 1.9919 1.3073 0.0734 -0.0162 -0.2118 186 GLU A CB 1488 C CG . GLU A 186 ? 1.7183 2.0306 1.3649 0.0554 -0.0067 -0.2127 186 GLU A CG 1489 C CD . GLU A 186 ? 1.7650 2.0931 1.4514 0.0536 -0.0135 -0.2134 186 GLU A CD 1490 O OE1 . GLU A 186 ? 1.7504 2.0977 1.4600 0.0615 -0.0259 -0.2210 186 GLU A OE1 1491 O OE2 . GLU A 186 ? 1.8097 2.1306 1.5032 0.0438 -0.0060 -0.2066 186 GLU A OE2 1492 N N . GLN A 187 ? 1.5717 1.7929 1.0725 0.0823 0.0007 -0.1911 187 GLN A N 1493 C CA . GLN A 187 ? 1.5765 1.7561 1.0295 0.0778 0.0140 -0.1793 187 GLN A CA 1494 C C . GLN A 187 ? 1.6234 1.7860 1.0388 0.0728 0.0254 -0.1797 187 GLN A C 1495 O O . GLN A 187 ? 1.5888 1.7377 0.9915 0.0544 0.0420 -0.1762 187 GLN A O 1496 C CB . GLN A 187 ? 1.5770 1.7311 0.9978 0.0974 0.0057 -0.1716 187 GLN A CB 1497 C CG . GLN A 187 ? 1.6089 1.7122 0.9695 0.0969 0.0184 -0.1595 187 GLN A CG 1498 C CD . GLN A 187 ? 1.5664 1.6534 0.9292 0.0767 0.0326 -0.1519 187 GLN A CD 1499 O OE1 . GLN A 187 ? 1.4929 1.5980 0.8938 0.0724 0.0286 -0.1520 187 GLN A OE1 1500 N NE2 . GLN A 187 ? 1.5991 1.6511 0.9193 0.0639 0.0499 -0.1456 187 GLN A NE2 1501 N N . THR A 188 ? 1.6675 1.8325 1.0656 0.0885 0.0167 -0.1848 188 THR A N 1502 C CA . THR A 188 ? 1.7159 1.8652 1.0771 0.0853 0.0268 -0.1858 188 THR A CA 1503 C C . THR A 188 ? 1.6371 1.8127 1.0286 0.0658 0.0365 -0.1936 188 THR A C 1504 O O . THR A 188 ? 1.6553 1.8149 1.0207 0.0525 0.0525 -0.1915 188 THR A O 1505 C CB . THR A 188 ? 1.7614 1.9124 1.1014 0.1072 0.0141 -0.1911 188 THR A CB 1506 O OG1 . THR A 188 ? 1.7882 1.9821 1.1768 0.1134 -0.0013 -0.2030 188 THR A OG1 1507 C CG2 . THR A 188 ? 1.7988 1.9180 1.0957 0.1284 0.0067 -0.1828 188 THR A CG2 1508 N N . LYS A 189 ? 1.5521 1.7671 0.9970 0.0640 0.0276 -0.2029 189 LYS A N 1509 C CA . LYS A 189 ? 1.5403 1.7811 1.0138 0.0484 0.0357 -0.2110 189 LYS A CA 1510 C C . LYS A 189 ? 1.5280 1.7607 1.0014 0.0272 0.0529 -0.2057 189 LYS A C 1511 O O . LYS A 189 ? 1.4784 1.7131 0.9422 0.0142 0.0664 -0.2085 189 LYS A O 1512 C CB . LYS A 189 ? 1.5192 1.7985 1.0474 0.0507 0.0232 -0.2211 189 LYS A CB 1513 C CG . LYS A 189 ? 1.5353 1.8405 1.0904 0.0380 0.0306 -0.2302 189 LYS A CG 1514 C CD . LYS A 189 ? 1.5592 1.8921 1.1656 0.0338 0.0246 -0.2355 189 LYS A CD 1515 C CE . LYS A 189 ? 1.5893 1.9488 1.2225 0.0405 0.0145 -0.2482 189 LYS A CE 1516 N NZ . LYS A 189 ? 1.5718 1.9524 1.2502 0.0370 0.0091 -0.2526 189 LYS A NZ 1517 N N . LEU A 190 ? 1.5188 1.7444 1.0034 0.0237 0.0525 -0.1988 190 LEU A N 1518 C CA . LEU A 190 ? 1.4900 1.7122 0.9803 0.0034 0.0673 -0.1949 190 LEU A CA 1519 C C . LEU A 190 ? 1.5440 1.7250 0.9809 -0.0057 0.0831 -0.1854 190 LEU A C 1520 O O . LEU A 190 ? 1.5140 1.6949 0.9455 -0.0253 0.0994 -0.1862 190 LEU A O 1521 C CB . LEU A 190 ? 1.4712 1.7009 0.9936 0.0032 0.0606 -0.1914 190 LEU A CB 1522 C CG . LEU A 190 ? 1.4298 1.6964 1.0050 0.0091 0.0469 -0.2000 190 LEU A CG 1523 C CD1 . LEU A 190 ? 1.3785 1.6474 0.9791 0.0062 0.0438 -0.1951 190 LEU A CD1 1524 C CD2 . LEU A 190 ? 1.4083 1.7056 1.0113 -0.0003 0.0516 -0.2106 190 LEU A CD2 1525 N N . TYR A 191 ? 1.5957 1.7419 0.9924 0.0086 0.0785 -0.1770 191 TYR A N 1526 C CA . TYR A 191 ? 1.6817 1.7808 1.0240 0.0015 0.0928 -0.1663 191 TYR A CA 1527 C C . TYR A 191 ? 1.7872 1.8505 1.0711 0.0145 0.0941 -0.1622 191 TYR A C 1528 O O . TYR A 191 ? 1.8563 1.8747 1.0886 0.0095 0.1065 -0.1531 191 TYR A O 1529 C CB . TYR A 191 ? 1.6805 1.7602 1.0210 0.0059 0.0884 -0.1572 191 TYR A CB 1530 C CG . TYR A 191 ? 1.6161 1.7303 1.0141 -0.0020 0.0836 -0.1608 191 TYR A CG 1531 C CD1 . TYR A 191 ? 1.6070 1.7370 1.0267 -0.0251 0.0967 -0.1639 191 TYR A CD1 1532 C CD2 . TYR A 191 ? 1.5530 1.6853 0.9833 0.0137 0.0661 -0.1619 191 TYR A CD2 1533 C CE1 . TYR A 191 ? 1.5454 1.7055 1.0151 -0.0307 0.0920 -0.1672 191 TYR A CE1 1534 C CE2 . TYR A 191 ? 1.4998 1.6606 0.9795 0.0066 0.0623 -0.1649 191 TYR A CE2 1535 C CZ . TYR A 191 ? 1.4876 1.6610 0.9859 -0.0149 0.0751 -0.1672 191 TYR A CZ 1536 O OH . TYR A 191 ? 1.4114 1.6117 0.9562 -0.0205 0.0712 -0.1701 191 TYR A OH 1537 N N . ARG A 192 ? 1.8025 1.8836 1.0921 0.0310 0.0818 -0.1692 192 ARG A N 1538 C CA . ARG A 192 ? 1.8640 1.9146 1.1005 0.0481 0.0794 -0.1662 192 ARG A CA 1539 C C . ARG A 192 ? 1.8838 1.8991 1.0841 0.0688 0.0705 -0.1565 192 ARG A C 1540 O O . ARG A 192 ? 1.8683 1.8912 1.0668 0.0925 0.0537 -0.1593 192 ARG A O 1541 C CB . ARG A 192 ? 1.9369 1.9584 1.1265 0.0328 0.0999 -0.1636 192 ARG A CB 1542 C CG . ARG A 192 ? 1.9655 2.0176 1.1717 0.0271 0.1027 -0.1747 192 ARG A CG 1543 C CD . ARG A 192 ? 2.0347 2.0520 1.1805 0.0280 0.1141 -0.1720 192 ARG A CD 1544 N NE . ARG A 192 ? 2.1149 2.1048 1.2208 0.0553 0.1012 -0.1674 192 ARG A NE 1545 C CZ . ARG A 192 ? 2.2061 2.1585 1.2518 0.0627 0.1078 -0.1634 192 ARG A CZ 1546 N NH1 . ARG A 192 ? 2.2456 2.1825 1.2633 0.0431 0.1282 -0.1634 192 ARG A NH1 1547 N NH2 . ARG A 192 ? 2.2423 2.1735 1.2547 0.0902 0.0940 -0.1600 192 ARG A NH2 1548 N N . ASN A 193 ? 1.9189 1.8971 1.0902 0.0602 0.0816 -0.1460 193 ASN A N 1549 C CA . ASN A 193 ? 1.9518 1.8875 1.0768 0.0799 0.0763 -0.1358 193 ASN A CA 1550 C C . ASN A 193 ? 1.8982 1.8605 1.0597 0.1002 0.0550 -0.1380 193 ASN A C 1551 O O . ASN A 193 ? 1.8043 1.7967 1.0169 0.0907 0.0518 -0.1407 193 ASN A O 1552 C CB . ASN A 193 ? 1.9846 1.8763 1.0755 0.0636 0.0935 -0.1248 193 ASN A CB 1553 C CG . ASN A 193 ? 2.0373 1.9113 1.1032 0.0366 0.1167 -0.1245 193 ASN A CG 1554 O OD1 . ASN A 193 ? 2.0637 1.9691 1.1535 0.0262 0.1202 -0.1335 193 ASN A OD1 1555 N ND2 . ASN A 193 ? 2.1032 1.9267 1.1202 0.0246 0.1331 -0.1147 193 ASN A ND2 1556 N N . PRO A 194 ? 1.9358 1.8886 1.0711 0.1285 0.0406 -0.1376 194 PRO A N 1557 C CA . PRO A 194 ? 1.8985 1.8814 1.0701 0.1473 0.0204 -0.1415 194 PRO A CA 1558 C C . PRO A 194 ? 1.8740 1.8413 1.0488 0.1460 0.0214 -0.1330 194 PRO A C 1559 O O . PRO A 194 ? 1.7615 1.7642 0.9892 0.1435 0.0127 -0.1372 194 PRO A O 1560 C CB . PRO A 194 ? 1.9486 1.9171 1.0786 0.1778 0.0076 -0.1419 194 PRO A CB 1561 C CG . PRO A 194 ? 2.0229 1.9346 1.0812 0.1765 0.0231 -0.1326 194 PRO A CG 1562 C CD . PRO A 194 ? 2.0021 1.9159 1.0720 0.1448 0.0423 -0.1337 194 PRO A CD 1563 N N . THR A 195 ? 1.9434 1.8557 1.0596 0.1471 0.0326 -0.1212 195 THR A N 1564 C CA . THR A 195 ? 1.9696 1.8593 1.0787 0.1482 0.0340 -0.1123 195 THR A CA 1565 C C . THR A 195 ? 1.9634 1.8212 1.0543 0.1195 0.0563 -0.1050 195 THR A C 1566 O O . THR A 195 ? 1.9953 1.8148 1.0364 0.1108 0.0713 -0.1007 195 THR A O 1567 C CB . THR A 195 ? 2.0371 1.8845 1.0866 0.1777 0.0269 -0.1045 195 THR A CB 1568 O OG1 . THR A 195 ? 2.0993 1.9038 1.0851 0.1814 0.0366 -0.1004 195 THR A OG1 1569 C CG2 . THR A 195 ? 2.0070 1.8928 1.0825 0.2064 0.0032 -0.1125 195 THR A CG2 1570 N N . THR A 196 ? 1.8995 1.7731 1.0298 0.1045 0.0587 -0.1042 196 THR A N 1571 C CA . THR A 196 ? 1.8961 1.7521 1.0219 0.0743 0.0789 -0.1003 196 THR A CA 1572 C C . THR A 196 ? 1.8753 1.7120 1.0007 0.0706 0.0813 -0.0925 196 THR A C 1573 O O . THR A 196 ? 1.8347 1.6748 0.9676 0.0914 0.0671 -0.0903 196 THR A O 1574 C CB . THR A 196 ? 1.8547 1.7624 1.0419 0.0520 0.0820 -0.1106 196 THR A CB 1575 O OG1 . THR A 196 ? 1.8051 1.7604 1.0522 0.0619 0.0646 -0.1172 196 THR A OG1 1576 C CG2 . THR A 196 ? 1.8768 1.7952 1.0559 0.0487 0.0860 -0.1174 196 THR A CG2 1577 N N . TYR A 197 ? 1.8790 1.6972 0.9960 0.0434 0.0997 -0.0892 197 TYR A N 1578 C CA . TYR A 197 ? 1.8749 1.6704 0.9867 0.0366 0.1046 -0.0818 197 TYR A CA 1579 C C . TYR A 197 ? 1.8775 1.6796 1.0075 0.0021 0.1223 -0.0838 197 TYR A C 1580 O O . TYR A 197 ? 1.8739 1.6873 1.0060 -0.0161 0.1336 -0.0894 197 TYR A O 1581 C CB . TYR A 197 ? 1.9690 1.6956 1.0033 0.0492 0.1106 -0.0702 197 TYR A CB 1582 C CG . TYR A 197 ? 2.0306 1.7112 1.0078 0.0298 0.1324 -0.0665 197 TYR A CG 1583 C CD1 . TYR A 197 ? 2.0411 1.7168 0.9923 0.0342 0.1348 -0.0695 197 TYR A CD1 1584 C CD2 . TYR A 197 ? 2.0669 1.7090 1.0156 0.0057 0.1513 -0.0606 197 TYR A CD2 1585 C CE1 . TYR A 197 ? 2.1004 1.7334 0.9983 0.0151 0.1559 -0.0663 197 TYR A CE1 1586 C CE2 . TYR A 197 ? 2.1347 1.7346 1.0305 -0.0146 0.1726 -0.0580 197 TYR A CE2 1587 C CZ . TYR A 197 ? 2.1506 1.7458 1.0208 -0.0099 0.1752 -0.0607 197 TYR A CZ 1588 O OH . TYR A 197 ? 2.1982 1.7507 1.0146 -0.0314 0.1976 -0.0583 197 TYR A OH 1589 N N . ILE A 198 ? 1.8835 1.6813 1.0278 -0.0060 0.1242 -0.0800 198 ILE A N 1590 C CA . ILE A 198 ? 1.8714 1.6668 1.0228 -0.0378 0.1418 -0.0807 198 ILE A CA 1591 C C . ILE A 198 ? 1.8893 1.6348 1.0015 -0.0384 0.1479 -0.0702 198 ILE A C 1592 O O . ILE A 198 ? 1.8753 1.6263 1.0057 -0.0224 0.1351 -0.0670 198 ILE A O 1593 C CB . ILE A 198 ? 1.8344 1.6905 1.0612 -0.0493 0.1361 -0.0895 198 ILE A CB 1594 C CG1 . ILE A 198 ? 1.8128 1.7194 1.0819 -0.0443 0.1269 -0.1000 198 ILE A CG1 1595 C CG2 . ILE A 198 ? 1.8560 1.7129 1.0885 -0.0820 0.1545 -0.0917 198 ILE A CG2 1596 C CD1 . ILE A 198 ? 1.7563 1.7174 1.0958 -0.0434 0.1147 -0.1071 198 ILE A CD1 1597 N N . SER A 199 ? 1.8965 1.5925 0.9538 -0.0570 0.1678 -0.0653 199 SER A N 1598 C CA . SER A 199 ? 1.9239 1.5680 0.9398 -0.0609 0.1760 -0.0558 199 SER A CA 1599 C C . SER A 199 ? 1.8839 1.5373 0.9192 -0.0962 0.1922 -0.0595 199 SER A C 1600 O O . SER A 199 ? 1.8731 1.5388 0.9109 -0.1212 0.2066 -0.0660 199 SER A O 1601 C CB . SER A 199 ? 2.0285 1.5997 0.9581 -0.0545 0.1868 -0.0467 199 SER A CB 1602 O OG . SER A 199 ? 2.0750 1.6261 0.9748 -0.0845 0.2091 -0.0489 199 SER A OG 1603 N N . VAL A 200 ? 1.8683 1.5180 0.9178 -0.0978 0.1896 -0.0560 200 VAL A N 1604 C CA . VAL A 200 ? 1.8572 1.5193 0.9288 -0.1291 0.2028 -0.0601 200 VAL A CA 1605 C C . VAL A 200 ? 1.9408 1.5421 0.9615 -0.1339 0.2123 -0.0505 200 VAL A C 1606 O O . VAL A 200 ? 1.9590 1.5417 0.9711 -0.1099 0.2000 -0.0431 200 VAL A O 1607 C CB . VAL A 200 ? 1.7879 1.5145 0.9383 -0.1277 0.1891 -0.0669 200 VAL A CB 1608 C CG1 . VAL A 200 ? 1.7677 1.5148 0.9434 -0.1607 0.2029 -0.0734 200 VAL A CG1 1609 C CG2 . VAL A 200 ? 1.7407 1.5222 0.9388 -0.1151 0.1756 -0.0751 200 VAL A CG2 1610 N N . GLY A 201 ? 2.0122 1.5837 0.9993 -0.1652 0.2343 -0.0513 201 GLY A N 1611 C CA . GLY A 201 ? 2.1060 1.6128 1.0370 -0.1735 0.2463 -0.0427 201 GLY A CA 1612 C C . GLY A 201 ? 2.1025 1.6174 1.0478 -0.2102 0.2625 -0.0484 201 GLY A C 1613 O O . GLY A 201 ? 2.1059 1.6509 1.0702 -0.2375 0.2748 -0.0582 201 GLY A O 1614 N N . THR A 202 ? 2.1242 1.6149 1.0616 -0.2101 0.2619 -0.0431 202 THR A N 1615 C CA . THR A 202 ? 2.1471 1.6283 1.0803 -0.2447 0.2792 -0.0469 202 THR A CA 1616 C C . THR A 202 ? 2.2350 1.6345 1.0955 -0.2418 0.2876 -0.0354 202 THR A C 1617 O O . THR A 202 ? 2.2617 1.6098 1.0678 -0.2179 0.2844 -0.0257 202 THR A O 1618 C CB . THR A 202 ? 2.0717 1.6150 1.0798 -0.2495 0.2688 -0.0539 202 THR A CB 1619 O OG1 . THR A 202 ? 2.0471 1.5762 1.0588 -0.2235 0.2536 -0.0453 202 THR A OG1 1620 C CG2 . THR A 202 ? 2.0114 1.6313 1.0895 -0.2435 0.2564 -0.0636 202 THR A CG2 1621 N N . SER A 203 ? 2.2869 1.6736 1.1448 -0.2651 0.2981 -0.0368 203 SER A N 1622 C CA . SER A 203 ? 2.3821 1.6924 1.1746 -0.2617 0.3050 -0.0262 203 SER A CA 1623 C C . SER A 203 ? 2.3602 1.6658 1.1611 -0.2206 0.2826 -0.0170 203 SER A C 1624 O O . SER A 203 ? 2.4226 1.6636 1.1606 -0.1995 0.2819 -0.0061 203 SER A O 1625 C CB . SER A 203 ? 2.4067 1.7125 1.2028 -0.2962 0.3197 -0.0313 203 SER A CB 1626 O OG . SER A 203 ? 2.5192 1.7396 1.2366 -0.3011 0.3331 -0.0222 203 SER A OG 1627 N N . THR A 204 ? 2.2730 1.6474 1.1505 -0.2089 0.2646 -0.0219 204 THR A N 1628 C CA . THR A 204 ? 2.2487 1.6288 1.1432 -0.1721 0.2432 -0.0151 204 THR A CA 1629 C C . THR A 204 ? 2.2123 1.6300 1.1356 -0.1415 0.2246 -0.0156 204 THR A C 1630 O O . THR A 204 ? 2.2706 1.6655 1.1709 -0.1084 0.2118 -0.0080 204 THR A O 1631 C CB . THR A 204 ? 2.1500 1.5761 1.1066 -0.1773 0.2350 -0.0192 204 THR A CB 1632 O OG1 . THR A 204 ? 2.0400 1.5438 1.0708 -0.1856 0.2281 -0.0301 204 THR A OG1 1633 C CG2 . THR A 204 ? 2.1557 1.5488 1.0868 -0.2087 0.2530 -0.0200 204 THR A CG2 1634 N N . LEU A 205 ? 2.1538 1.6294 1.1262 -0.1522 0.2230 -0.0253 205 LEU A N 1635 C CA . LEU A 205 ? 2.0990 1.6161 1.1052 -0.1260 0.2053 -0.0276 205 LEU A CA 1636 C C . LEU A 205 ? 2.1638 1.6418 1.1135 -0.1129 0.2084 -0.0233 205 LEU A C 1637 O O . LEU A 205 ? 2.2060 1.6520 1.1135 -0.1348 0.2268 -0.0240 205 LEU A O 1638 C CB . LEU A 205 ? 2.0214 1.6125 1.0989 -0.1419 0.2028 -0.0398 205 LEU A CB 1639 C CG . LEU A 205 ? 1.9718 1.6143 1.0961 -0.1177 0.1836 -0.0438 205 LEU A CG 1640 C CD1 . LEU A 205 ? 1.9304 1.5866 1.0813 -0.0895 0.1642 -0.0397 205 LEU A CD1 1641 C CD2 . LEU A 205 ? 1.9075 1.6151 1.0942 -0.1362 0.1841 -0.0559 205 LEU A CD2 1642 N N . ASN A 206 ? 2.1593 1.6414 1.1085 -0.0774 0.1905 -0.0196 206 ASN A N 1643 C CA . ASN A 206 ? 2.1711 1.6242 1.0729 -0.0599 0.1898 -0.0164 206 ASN A CA 1644 C C . ASN A 206 ? 2.0733 1.5739 1.0159 -0.0283 0.1670 -0.0196 206 ASN A C 1645 O O . ASN A 206 ? 2.0486 1.5318 0.9712 0.0035 0.1537 -0.0139 206 ASN A O 1646 C CB . ASN A 206 ? 2.2601 1.6298 1.0761 -0.0460 0.1965 -0.0047 206 ASN A CB 1647 C CG . ASN A 206 ? 2.3383 1.6785 1.1052 -0.0192 0.1913 -0.0006 206 ASN A CG 1648 O OD1 . ASN A 206 ? 2.3149 1.6589 1.0717 -0.0294 0.1988 -0.0044 206 ASN A OD1 1649 N ND2 . ASN A 206 ? 2.3811 1.6932 1.1169 0.0164 0.1782 0.0067 206 ASN A ND2 1650 N N . GLN A 207 ? 1.9962 1.5572 0.9953 -0.0370 0.1626 -0.0294 207 GLN A N 1651 C CA . GLN A 207 ? 1.9876 1.5977 1.0308 -0.0109 0.1416 -0.0340 207 GLN A CA 1652 C C . GLN A 207 ? 1.9791 1.5966 1.0097 -0.0056 0.1411 -0.0380 207 GLN A C 1653 O O . GLN A 207 ? 1.9831 1.5790 0.9832 -0.0261 0.1576 -0.0389 207 GLN A O 1654 C CB . GLN A 207 ? 1.9349 1.6134 1.0604 -0.0195 0.1326 -0.0424 207 GLN A CB 1655 C CG . GLN A 207 ? 1.9212 1.6381 1.0835 -0.0482 0.1424 -0.0519 207 GLN A CG 1656 C CD . GLN A 207 ? 1.8271 1.6104 1.0676 -0.0505 0.1310 -0.0603 207 GLN A CD 1657 O OE1 . GLN A 207 ? 1.7861 1.6120 1.0635 -0.0572 0.1292 -0.0690 207 GLN A OE1 1658 N NE2 . GLN A 207 ? 1.7848 1.5752 1.0488 -0.0445 0.1236 -0.0576 207 GLN A NE2 1659 N N . ARG A 208 ? 1.9518 1.6010 1.0066 0.0217 0.1222 -0.0411 208 ARG A N 1660 C CA . ARG A 208 ? 1.9721 1.6340 1.0204 0.0311 0.1182 -0.0456 208 ARG A CA 1661 C C . ARG A 208 ? 1.9193 1.6456 1.0328 0.0473 0.0979 -0.0540 208 ARG A C 1662 O O . ARG A 208 ? 1.9329 1.6641 1.0476 0.0753 0.0819 -0.0526 208 ARG A O 1663 C CB . ARG A 208 ? 2.0637 1.6688 1.0379 0.0557 0.1173 -0.0376 208 ARG A CB 1664 C CG . ARG A 208 ? 2.0945 1.7051 1.0522 0.0658 0.1143 -0.0416 208 ARG A CG 1665 C CD . ARG A 208 ? 2.1900 1.7405 1.0703 0.0925 0.1130 -0.0330 208 ARG A CD 1666 N NE . ARG A 208 ? 2.2301 1.7901 1.0972 0.1091 0.1058 -0.0371 208 ARG A NE 1667 C CZ . ARG A 208 ? 2.2737 1.8151 1.1099 0.0949 0.1193 -0.0380 208 ARG A CZ 1668 N NH1 . ARG A 208 ? 2.3119 1.8258 1.1278 0.0620 0.1415 -0.0358 208 ARG A NH1 1669 N NH2 . ARG A 208 ? 2.2883 1.8403 1.1142 0.1132 0.1105 -0.0419 208 ARG A NH2 1670 N N . LEU A 209 ? 1.8704 1.6461 1.0374 0.0294 0.0989 -0.0634 209 LEU A N 1671 C CA . LEU A 209 ? 1.8101 1.6454 1.0389 0.0409 0.0816 -0.0721 209 LEU A CA 1672 C C . LEU A 209 ? 1.8143 1.6592 1.0318 0.0559 0.0745 -0.0769 209 LEU A C 1673 O O . LEU A 209 ? 1.7992 1.6255 0.9857 0.0451 0.0862 -0.0773 209 LEU A O 1674 C CB . LEU A 209 ? 1.7761 1.6571 1.0644 0.0163 0.0858 -0.0801 209 LEU A CB 1675 C CG . LEU A 209 ? 1.7931 1.6681 1.0942 -0.0032 0.0951 -0.0769 209 LEU A CG 1676 C CD1 . LEU A 209 ? 1.7589 1.6778 1.1108 -0.0269 0.1006 -0.0859 209 LEU A CD1 1677 C CD2 . LEU A 209 ? 1.7710 1.6518 1.0921 0.0127 0.0825 -0.0733 209 LEU A CD2 1678 N N . VAL A 210 ? 1.7899 1.6640 1.0315 0.0802 0.0557 -0.0811 210 VAL A N 1679 C CA . VAL A 210 ? 1.7994 1.6936 1.0420 0.0941 0.0466 -0.0880 210 VAL A CA 1680 C C . VAL A 210 ? 1.7422 1.6991 1.0553 0.0947 0.0332 -0.0990 210 VAL A C 1681 O O . VAL A 210 ? 1.7292 1.7074 1.0772 0.0998 0.0242 -0.0997 210 VAL A O 1682 C CB . VAL A 210 ? 1.8539 1.7211 1.0493 0.1260 0.0359 -0.0839 210 VAL A CB 1683 C CG1 . VAL A 210 ? 1.9180 1.7190 1.0366 0.1255 0.0504 -0.0738 210 VAL A CG1 1684 C CG2 . VAL A 210 ? 1.8596 1.7354 1.0696 0.1459 0.0222 -0.0820 210 VAL A CG2 1685 N N . PRO A 211 ? 1.6929 1.6776 1.0255 0.0891 0.0324 -0.1077 211 PRO A N 1686 C CA . PRO A 211 ? 1.6203 1.6597 1.0158 0.0891 0.0205 -0.1183 211 PRO A CA 1687 C C . PRO A 211 ? 1.6080 1.6667 1.0127 0.1155 0.0016 -0.1224 211 PRO A C 1688 O O . PRO A 211 ? 1.6492 1.6927 1.0169 0.1338 -0.0036 -0.1221 211 PRO A O 1689 C CB . PRO A 211 ? 1.6289 1.6859 1.0327 0.0777 0.0257 -0.1260 211 PRO A CB 1690 C CG . PRO A 211 ? 1.6723 1.6860 1.0214 0.0682 0.0420 -0.1194 211 PRO A CG 1691 C CD . PRO A 211 ? 1.7289 1.6959 1.0266 0.0827 0.0424 -0.1086 211 PRO A CD 1692 N N . ARG A 212 ? 1.5712 1.6629 1.0233 0.1174 -0.0082 -0.1265 212 ARG A N 1693 C CA . ARG A 212 ? 1.5864 1.7087 1.0597 0.1378 -0.0258 -0.1340 212 ARG A CA 1694 C C . ARG A 212 ? 1.5625 1.7275 1.0784 0.1315 -0.0317 -0.1466 212 ARG A C 1695 O O . ARG A 212 ? 1.5316 1.7209 1.0912 0.1152 -0.0293 -0.1508 212 ARG A O 1696 C CB . ARG A 212 ? 1.5719 1.7064 1.0718 0.1425 -0.0325 -0.1323 212 ARG A CB 1697 C CG . ARG A 212 ? 1.6428 1.7354 1.0974 0.1544 -0.0296 -0.1207 212 ARG A CG 1698 C CD . ARG A 212 ? 1.6272 1.6983 1.0832 0.1349 -0.0163 -0.1124 212 ARG A CD 1699 N NE . ARG A 212 ? 1.5557 1.6596 1.0642 0.1292 -0.0217 -0.1158 212 ARG A NE 1700 C CZ . ARG A 212 ? 1.5384 1.6389 1.0656 0.1106 -0.0126 -0.1119 212 ARG A CZ 1701 N NH1 . ARG A 212 ? 1.5558 1.6239 1.0554 0.0945 0.0025 -0.1051 212 ARG A NH1 1702 N NH2 . ARG A 212 ? 1.5684 1.6986 1.1416 0.1076 -0.0185 -0.1154 212 ARG A NH2 1703 N N . ILE A 213 ? 1.6099 1.7820 1.1103 0.1457 -0.0396 -0.1527 213 ILE A N 1704 C CA . ILE A 213 ? 1.6065 1.8144 1.1395 0.1411 -0.0450 -0.1650 213 ILE A CA 1705 C C . ILE A 213 ? 1.6063 1.8520 1.1722 0.1547 -0.0619 -0.1751 213 ILE A C 1706 O O . ILE A 213 ? 1.6241 1.8707 1.1683 0.1758 -0.0724 -0.1774 213 ILE A O 1707 C CB . ILE A 213 ? 1.6481 1.8412 1.1431 0.1467 -0.0425 -0.1665 213 ILE A CB 1708 C CG1 . ILE A 213 ? 1.6874 1.8444 1.1500 0.1304 -0.0240 -0.1576 213 ILE A CG1 1709 C CG2 . ILE A 213 ? 1.6449 1.8749 1.1725 0.1435 -0.0490 -0.1799 213 ILE A CG2 1710 C CD1 . ILE A 213 ? 1.7308 1.8713 1.1552 0.1327 -0.0189 -0.1587 213 ILE A CD1 1711 N N . ALA A 214 ? 1.6108 1.8877 1.2278 0.1424 -0.0642 -0.1816 214 ALA A N 1712 C CA . ALA A 214 ? 1.6107 1.9244 1.2624 0.1509 -0.0783 -0.1919 214 ALA A CA 1713 C C . ALA A 214 ? 1.6343 1.9797 1.3335 0.1353 -0.0792 -0.2026 214 ALA A C 1714 O O . ALA A 214 ? 1.6423 1.9823 1.3535 0.1180 -0.0689 -0.2006 214 ALA A O 1715 C CB . ALA A 214 ? 1.5840 1.8967 1.2446 0.1558 -0.0810 -0.1864 214 ALA A CB 1716 N N . THR A 215 ? 1.6646 2.0430 1.3891 0.1418 -0.0915 -0.2147 215 THR A N 1717 C CA . THR A 215 ? 1.6528 2.0592 1.4216 0.1278 -0.0931 -0.2253 215 THR A CA 1718 C C . THR A 215 ? 1.5821 1.9912 1.3808 0.1164 -0.0890 -0.2212 215 THR A C 1719 O O . THR A 215 ? 1.6360 2.0464 1.4357 0.1241 -0.0930 -0.2175 215 THR A O 1720 C CB . THR A 215 ? 1.6693 2.1094 1.4549 0.1365 -0.1068 -0.2403 215 THR A CB 1721 O OG1 . THR A 215 ? 1.6633 2.1023 1.4262 0.1434 -0.1095 -0.2455 215 THR A OG1 1722 C CG2 . THR A 215 ? 1.6711 2.1369 1.5025 0.1213 -0.1081 -0.2507 215 THR A CG2 1723 N N . ARG A 216 ? 1.5034 1.9133 1.3247 0.0994 -0.0813 -0.2220 216 ARG A N 1724 C CA . ARG A 216 ? 1.4393 1.8499 1.2878 0.0879 -0.0765 -0.2181 216 ARG A CA 1725 C C . ARG A 216 ? 1.4179 1.8485 1.3032 0.0756 -0.0772 -0.2284 216 ARG A C 1726 O O . ARG A 216 ? 1.4529 1.8922 1.3406 0.0736 -0.0787 -0.2371 216 ARG A O 1727 C CB . ARG A 216 ? 1.4147 1.7986 1.2480 0.0789 -0.0638 -0.2062 216 ARG A CB 1728 C CG . ARG A 216 ? 1.3924 1.7572 1.2115 0.0825 -0.0607 -0.1945 216 ARG A CG 1729 C CD . ARG A 216 ? 1.4237 1.7611 1.1962 0.0927 -0.0578 -0.1860 216 ARG A CD 1730 N NE . ARG A 216 ? 1.4324 1.7560 1.1842 0.0858 -0.0492 -0.1850 216 ARG A NE 1731 C CZ . ARG A 216 ? 1.4450 1.7408 1.1532 0.0911 -0.0439 -0.1780 216 ARG A CZ 1732 N NH1 . ARG A 216 ? 1.4799 1.7557 1.1583 0.1047 -0.0465 -0.1706 216 ARG A NH1 1733 N NH2 . ARG A 216 ? 1.4313 1.7181 1.1241 0.0828 -0.0353 -0.1784 216 ARG A NH2 1734 N N . SER A 217 ? 1.4258 1.8611 1.3373 0.0679 -0.0757 -0.2270 217 SER A N 1735 C CA . SER A 217 ? 1.3974 1.8431 1.3394 0.0553 -0.0738 -0.2343 217 SER A CA 1736 C C . SER A 217 ? 1.3856 1.8168 1.3233 0.0464 -0.0636 -0.2300 217 SER A C 1737 O O . SER A 217 ? 1.3744 1.7883 1.2946 0.0457 -0.0565 -0.2196 217 SER A O 1738 C CB . SER A 217 ? 1.3941 1.8445 1.3606 0.0500 -0.0737 -0.2324 217 SER A CB 1739 O OG . SER A 217 ? 1.3737 1.8279 1.3335 0.0600 -0.0790 -0.2288 217 SER A OG 1740 N N . LYS A 218 ? 1.3690 1.8075 1.3216 0.0396 -0.0627 -0.2386 218 LYS A N 1741 C CA . LYS A 218 ? 1.3478 1.7774 1.3007 0.0319 -0.0536 -0.2361 218 LYS A CA 1742 C C . LYS A 218 ? 1.3283 1.7519 1.2978 0.0247 -0.0483 -0.2298 218 LYS A C 1743 O O . LYS A 218 ? 1.3204 1.7496 1.3096 0.0226 -0.0518 -0.2320 218 LYS A O 1744 C CB . LYS A 218 ? 1.3373 1.7755 1.3002 0.0288 -0.0546 -0.2475 218 LYS A CB 1745 C CG . LYS A 218 ? 1.3685 1.8097 1.3113 0.0349 -0.0571 -0.2525 218 LYS A CG 1746 C CD . LYS A 218 ? 1.3900 1.8379 1.3411 0.0318 -0.0572 -0.2635 218 LYS A CD 1747 C CE . LYS A 218 ? 1.4350 1.8867 1.3658 0.0385 -0.0606 -0.2691 218 LYS A CE 1748 N NZ . LYS A 218 ? 1.4493 1.9066 1.3859 0.0364 -0.0608 -0.2802 218 LYS A NZ 1749 N N . VAL A 219 ? 1.3060 1.7189 1.2665 0.0206 -0.0397 -0.2224 219 VAL A N 1750 C CA . VAL A 219 ? 1.2586 1.6671 1.2342 0.0137 -0.0342 -0.2176 219 VAL A CA 1751 C C . VAL A 219 ? 1.2365 1.6445 1.2087 0.0088 -0.0263 -0.2185 219 VAL A C 1752 O O . VAL A 219 ? 1.2288 1.6316 1.1802 0.0082 -0.0212 -0.2152 219 VAL A O 1753 C CB . VAL A 219 ? 1.2656 1.6624 1.2319 0.0140 -0.0316 -0.2062 219 VAL A CB 1754 C CG1 . VAL A 219 ? 1.2755 1.6690 1.2578 0.0070 -0.0263 -0.2020 219 VAL A CG1 1755 C CG2 . VAL A 219 ? 1.2558 1.6556 1.2229 0.0212 -0.0397 -0.2058 219 VAL A CG2 1756 N N . ASN A 220 ? 1.2461 1.6592 1.2372 0.0055 -0.0252 -0.2237 220 ASN A N 1757 C CA . ASN A 220 ? 1.2530 1.6712 1.2432 0.0035 -0.0197 -0.2284 220 ASN A CA 1758 C C . ASN A 220 ? 1.1990 1.6216 1.1735 0.0069 -0.0208 -0.2342 220 ASN A C 1759 O O . ASN A 220 ? 1.2040 1.6291 1.1668 0.0050 -0.0145 -0.2346 220 ASN A O 1760 C CB . ASN A 220 ? 1.3077 1.7235 1.2922 -0.0020 -0.0108 -0.2214 220 ASN A CB 1761 C CG . ASN A 220 ? 1.3634 1.7740 1.3609 -0.0048 -0.0100 -0.2150 220 ASN A CG 1762 O OD1 . ASN A 220 ? 1.4503 1.8532 1.4386 -0.0081 -0.0062 -0.2065 220 ASN A OD1 1763 N ND2 . ASN A 220 ? 1.3736 1.7861 1.3905 -0.0036 -0.0132 -0.2191 220 ASN A ND2 1764 N N . GLY A 221 ? 1.2073 1.6322 1.1818 0.0115 -0.0288 -0.2393 221 GLY A N 1765 C CA . GLY A 221 ? 1.2111 1.6406 1.1716 0.0157 -0.0313 -0.2460 221 GLY A CA 1766 C C . GLY A 221 ? 1.1871 1.6106 1.1204 0.0181 -0.0285 -0.2401 221 GLY A C 1767 O O . GLY A 221 ? 1.2125 1.6383 1.1314 0.0201 -0.0272 -0.2444 221 GLY A O 1768 N N . GLN A 222 ? 1.1810 1.5945 1.1047 0.0183 -0.0274 -0.2303 222 GLN A N 1769 C CA . GLN A 222 ? 1.2057 1.6073 1.0985 0.0208 -0.0239 -0.2237 222 GLN A CA 1770 C C . GLN A 222 ? 1.2137 1.6093 1.0949 0.0298 -0.0316 -0.2200 222 GLN A C 1771 O O . GLN A 222 ? 1.2117 1.6064 1.1048 0.0304 -0.0347 -0.2161 222 GLN A O 1772 C CB . GLN A 222 ? 1.2179 1.6084 1.1016 0.0127 -0.0131 -0.2147 222 GLN A CB 1773 C CG . GLN A 222 ? 1.2059 1.6060 1.1013 0.0045 -0.0053 -0.2187 222 GLN A CG 1774 C CD . GLN A 222 ? 1.2156 1.6244 1.1034 0.0059 -0.0040 -0.2270 222 GLN A CD 1775 O OE1 . GLN A 222 ? 1.2388 1.6404 1.1012 0.0090 -0.0031 -0.2262 222 GLN A OE1 1776 N NE2 . GLN A 222 ? 1.2222 1.6452 1.1300 0.0046 -0.0037 -0.2352 222 GLN A NE2 1777 N N . ASN A 223 ? 1.2511 1.6433 1.1080 0.0376 -0.0346 -0.2216 223 ASN A N 1778 C CA . ASN A 223 ? 1.2963 1.6831 1.1367 0.0490 -0.0422 -0.2185 223 ASN A CA 1779 C C . ASN A 223 ? 1.3030 1.6653 1.1119 0.0505 -0.0355 -0.2063 223 ASN A C 1780 O O . ASN A 223 ? 1.3303 1.6848 1.1276 0.0597 -0.0405 -0.2013 223 ASN A O 1781 C CB . ASN A 223 ? 1.3682 1.7618 1.1939 0.0584 -0.0490 -0.2263 223 ASN A CB 1782 C CG . ASN A 223 ? 1.3987 1.8146 1.2522 0.0570 -0.0560 -0.2392 223 ASN A CG 1783 O OD1 . ASN A 223 ? 1.4112 1.8386 1.2908 0.0552 -0.0613 -0.2429 223 ASN A OD1 1784 N ND2 . ASN A 223 ? 1.4298 1.8502 1.2763 0.0572 -0.0555 -0.2465 223 ASN A ND2 1785 N N . GLY A 224 ? 1.2878 1.6380 1.0813 0.0415 -0.0240 -0.2022 224 GLY A N 1786 C CA . GLY A 224 ? 1.2867 1.6103 1.0486 0.0394 -0.0152 -0.1910 224 GLY A CA 1787 C C . GLY A 224 ? 1.2316 1.5495 1.0070 0.0330 -0.0119 -0.1839 224 GLY A C 1788 O O . GLY A 224 ? 1.1505 1.4852 0.9604 0.0296 -0.0155 -0.1875 224 GLY A O 1789 N N . ARG A 225 ? 1.2439 1.5353 0.9893 0.0314 -0.0047 -0.1738 225 ARG A N 1790 C CA . ARG A 225 ? 1.2559 1.5383 1.0088 0.0243 0.0001 -0.1665 225 ARG A CA 1791 C C . ARG A 225 ? 1.2684 1.5257 0.9904 0.0129 0.0143 -0.1593 225 ARG A C 1792 O O . ARG A 225 ? 1.3019 1.5398 0.9871 0.0151 0.0188 -0.1568 225 ARG A O 1793 C CB . ARG A 225 ? 1.2536 1.5271 1.0011 0.0370 -0.0083 -0.1612 225 ARG A CB 1794 C CG . ARG A 225 ? 1.2295 1.5294 1.0092 0.0461 -0.0215 -0.1687 225 ARG A CG 1795 C CD . ARG A 225 ? 1.2151 1.5317 1.0347 0.0369 -0.0214 -0.1710 225 ARG A CD 1796 N NE . ARG A 225 ? 1.2103 1.5500 1.0583 0.0434 -0.0326 -0.1787 225 ARG A NE 1797 C CZ . ARG A 225 ? 1.2098 1.5698 1.0777 0.0424 -0.0372 -0.1893 225 ARG A CZ 1798 N NH1 . ARG A 225 ? 1.2281 1.5900 1.0919 0.0368 -0.0323 -0.1934 225 ARG A NH1 1799 N NH2 . ARG A 225 ? 1.2122 1.5909 1.1036 0.0466 -0.0464 -0.1963 225 ARG A NH2 1800 N N . MET A 226 ? 1.2774 1.5350 1.0135 0.0002 0.0215 -0.1564 226 MET A N 1801 C CA . MET A 226 ? 1.3218 1.5565 1.0306 -0.0128 0.0353 -0.1501 226 MET A CA 1802 C C . MET A 226 ? 1.3240 1.5395 1.0266 -0.0122 0.0357 -0.1412 226 MET A C 1803 O O . MET A 226 ? 1.3133 1.5442 1.0482 -0.0118 0.0304 -0.1419 226 MET A O 1804 C CB . MET A 226 ? 1.3340 1.5891 1.0654 -0.0293 0.0441 -0.1560 226 MET A CB 1805 C CG . MET A 226 ? 1.3474 1.6242 1.0882 -0.0296 0.0438 -0.1657 226 MET A CG 1806 S SD . MET A 226 ? 1.4079 1.6678 1.1069 -0.0396 0.0580 -0.1655 226 MET A SD 1807 C CE . MET A 226 ? 1.3931 1.6873 1.1166 -0.0385 0.0553 -0.1785 226 MET A CE 1808 N N . GLU A 227 ? 1.3662 1.5461 1.0254 -0.0116 0.0420 -0.1327 227 GLU A N 1809 C CA . GLU A 227 ? 1.3517 1.5083 0.9987 -0.0121 0.0443 -0.1238 227 GLU A CA 1810 C C . GLU A 227 ? 1.3387 1.4785 0.9681 -0.0326 0.0603 -0.1210 227 GLU A C 1811 O O . GLU A 227 ? 1.4022 1.5210 0.9956 -0.0393 0.0702 -0.1196 227 GLU A O 1812 C CB . GLU A 227 ? 1.4285 1.5526 1.0341 0.0048 0.0401 -0.1163 227 GLU A CB 1813 C CG . GLU A 227 ? 1.4848 1.6220 1.1096 0.0238 0.0249 -0.1165 227 GLU A CG 1814 C CD . GLU A 227 ? 1.5850 1.6873 1.1705 0.0381 0.0231 -0.1073 227 GLU A CD 1815 O OE1 . GLU A 227 ? 1.6739 1.7492 1.2402 0.0299 0.0319 -0.0998 227 GLU A OE1 1816 O OE2 . GLU A 227 ? 1.6136 1.7162 1.1870 0.0581 0.0126 -0.1081 227 GLU A OE2 1817 N N . PHE A 228 ? 1.2715 1.4207 0.9252 -0.0431 0.0631 -0.1205 228 PHE A N 1818 C CA . PHE A 228 ? 1.2523 1.3904 0.8931 -0.0640 0.0781 -0.1194 228 PHE A CA 1819 C C . PHE A 228 ? 1.2674 1.3685 0.8786 -0.0659 0.0830 -0.1096 228 PHE A C 1820 O O . PHE A 228 ? 1.2596 1.3578 0.8812 -0.0543 0.0742 -0.1052 228 PHE A O 1821 C CB . PHE A 228 ? 1.2265 1.4022 0.9125 -0.0757 0.0792 -0.1272 228 PHE A CB 1822 C CG . PHE A 228 ? 1.2416 1.4491 0.9493 -0.0763 0.0776 -0.1372 228 PHE A CG 1823 C CD1 . PHE A 228 ? 1.2673 1.4773 0.9600 -0.0905 0.0896 -0.1418 228 PHE A CD1 1824 C CD2 . PHE A 228 ? 1.2298 1.4632 0.9708 -0.0629 0.0646 -0.1423 228 PHE A CD2 1825 C CE1 . PHE A 228 ? 1.2530 1.4922 0.9645 -0.0897 0.0880 -0.1513 228 PHE A CE1 1826 C CE2 . PHE A 228 ? 1.2055 1.4653 0.9638 -0.0626 0.0631 -0.1516 228 PHE A CE2 1827 C CZ . PHE A 228 ? 1.2042 1.4672 0.9479 -0.0752 0.0745 -0.1560 228 PHE A CZ 1828 N N . PHE A 229 ? 1.2983 1.3702 0.8708 -0.0811 0.0977 -0.1065 229 PHE A N 1829 C CA . PHE A 229 ? 1.3435 1.3738 0.8799 -0.0853 0.1048 -0.0974 229 PHE A CA 1830 C C . PHE A 229 ? 1.3501 1.3807 0.8865 -0.1117 0.1197 -0.1001 229 PHE A C 1831 O O . PHE A 229 ? 1.2992 1.3584 0.8548 -0.1261 0.1260 -0.1088 229 PHE A O 1832 C CB . PHE A 229 ? 1.4002 1.3839 0.8773 -0.0780 0.1096 -0.0905 229 PHE A CB 1833 C CG . PHE A 229 ? 1.4377 1.4184 0.9095 -0.0505 0.0946 -0.0876 229 PHE A CG 1834 C CD1 . PHE A 229 ? 1.4383 1.4446 0.9251 -0.0407 0.0869 -0.0940 229 PHE A CD1 1835 C CD2 . PHE A 229 ? 1.4912 1.4460 0.9444 -0.0339 0.0878 -0.0796 229 PHE A CD2 1836 C CE1 . PHE A 229 ? 1.4688 1.4761 0.9523 -0.0158 0.0726 -0.0928 229 PHE A CE1 1837 C CE2 . PHE A 229 ? 1.5261 1.4833 0.9764 -0.0079 0.0735 -0.0784 229 PHE A CE2 1838 C CZ . PHE A 229 ? 1.4988 1.4831 0.9647 0.0007 0.0659 -0.0854 229 PHE A CZ 1839 N N . TRP A 230 ? 1.3910 1.3904 0.9051 -0.1176 0.1254 -0.0933 230 TRP A N 1840 C CA . TRP A 230 ? 1.3925 1.3891 0.9023 -0.1438 0.1402 -0.0961 230 TRP A CA 1841 C C . TRP A 230 ? 1.4254 1.3663 0.8820 -0.1506 0.1507 -0.0870 230 TRP A C 1842 O O . TRP A 230 ? 1.4505 1.3564 0.8773 -0.1323 0.1448 -0.0780 230 TRP A O 1843 C CB . TRP A 230 ? 1.3357 1.3713 0.8973 -0.1477 0.1345 -0.1010 230 TRP A CB 1844 C CG . TRP A 230 ? 1.3460 1.3720 0.9169 -0.1316 0.1235 -0.0938 230 TRP A CG 1845 C CD1 . TRP A 230 ? 1.3211 1.3662 0.9205 -0.1097 0.1076 -0.0930 230 TRP A CD1 1846 C CD2 . TRP A 230 ? 1.3563 1.3521 0.9076 -0.1367 0.1280 -0.0872 230 TRP A CD2 1847 N NE1 . TRP A 230 ? 1.3068 1.3372 0.9068 -0.1008 0.1020 -0.0863 230 TRP A NE1 1848 C CE2 . TRP A 230 ? 1.3420 1.3415 0.9123 -0.1163 0.1140 -0.0823 230 TRP A CE2 1849 C CE3 . TRP A 230 ? 1.4018 1.3676 0.9207 -0.1575 0.1430 -0.0854 230 TRP A CE3 1850 C CZ2 . TRP A 230 ? 1.3707 1.3453 0.9290 -0.1145 0.1142 -0.0754 230 TRP A CZ2 1851 C CZ3 . TRP A 230 ? 1.4360 1.3752 0.9420 -0.1562 0.1430 -0.0785 230 TRP A CZ3 1852 C CH2 . TRP A 230 ? 1.4100 1.3538 0.9357 -0.1340 0.1285 -0.0734 230 TRP A CH2 1853 N N . THR A 231 ? 1.4368 1.3700 0.8804 -0.1773 0.1666 -0.0903 231 THR A N 1854 C CA . THR A 231 ? 1.4932 1.3757 0.8909 -0.1879 0.1776 -0.0831 231 THR A CA 1855 C C . THR A 231 ? 1.4977 1.3967 0.9082 -0.2183 0.1912 -0.0910 231 THR A C 1856 O O . THR A 231 ? 1.4821 1.4255 0.9253 -0.2313 0.1944 -0.1017 231 THR A O 1857 C CB . THR A 231 ? 1.5595 1.3859 0.8899 -0.1882 0.1881 -0.0766 231 THR A CB 1858 O OG1 . THR A 231 ? 1.6371 1.4078 0.9210 -0.1886 0.1940 -0.0671 231 THR A OG1 1859 C CG2 . THR A 231 ? 1.5837 1.4128 0.8979 -0.2156 0.2060 -0.0842 231 THR A CG2 1860 N N . ILE A 232 ? 1.5521 1.4168 0.9371 -0.2287 0.1986 -0.0862 232 ILE A N 1861 C CA . ILE A 232 ? 1.5823 1.4554 0.9697 -0.2599 0.2135 -0.0938 232 ILE A CA 1862 C C . ILE A 232 ? 1.6529 1.4748 0.9769 -0.2802 0.2332 -0.0918 232 ILE A C 1863 O O . ILE A 232 ? 1.7063 1.4682 0.9772 -0.2730 0.2364 -0.0811 232 ILE A O 1864 C CB . ILE A 232 ? 1.5735 1.4423 0.9732 -0.2615 0.2104 -0.0911 232 ILE A CB 1865 C CG1 . ILE A 232 ? 1.5164 1.4501 0.9842 -0.2600 0.1999 -0.1001 232 ILE A CG1 1866 C CG2 . ILE A 232 ? 1.6223 1.4590 0.9853 -0.2918 0.2294 -0.0930 232 ILE A CG2 1867 C CD1 . ILE A 232 ? 1.5022 1.4677 1.0086 -0.2320 0.1814 -0.0990 232 ILE A CD1 1868 N N . LEU A 233 ? 1.6874 1.5328 1.0156 -0.3053 0.2466 -0.1025 233 LEU A N 1869 C CA . LEU A 233 ? 1.7617 1.5621 1.0312 -0.3288 0.2675 -0.1023 233 LEU A CA 1870 C C . LEU A 233 ? 1.7998 1.5902 1.0591 -0.3592 0.2823 -0.1072 233 LEU A C 1871 O O . LEU A 233 ? 1.7674 1.6104 1.0696 -0.3776 0.2853 -0.1197 233 LEU A O 1872 C CB . LEU A 233 ? 1.7572 1.5910 1.0372 -0.3403 0.2748 -0.1123 233 LEU A CB 1873 C CG . LEU A 233 ? 1.8078 1.5953 1.0254 -0.3597 0.2952 -0.1114 233 LEU A CG 1874 C CD1 . LEU A 233 ? 1.8444 1.5683 1.0061 -0.3358 0.2912 -0.0969 233 LEU A CD1 1875 C CD2 . LEU A 233 ? 1.7753 1.6104 1.0170 -0.3711 0.3008 -0.1235 233 LEU A CD2 1876 N N . LYS A 234 ? 1.8815 1.6047 1.0834 -0.3633 0.2909 -0.0976 234 LYS A N 1877 C CA . LYS A 234 ? 1.9733 1.6786 1.1575 -0.3935 0.3062 -0.1019 234 LYS A CA 1878 C C . LYS A 234 ? 2.0172 1.7329 1.1875 -0.4312 0.3282 -0.1143 234 LYS A C 1879 O O . LYS A 234 ? 2.0454 1.7554 1.1958 -0.4330 0.3347 -0.1152 234 LYS A O 1880 C CB . LYS A 234 ? 2.0811 1.7042 1.1984 -0.3890 0.3118 -0.0885 234 LYS A CB 1881 C CG . LYS A 234 ? 2.0865 1.7055 1.2217 -0.3716 0.2982 -0.0821 234 LYS A CG 1882 C CD . LYS A 234 ? 2.2199 1.7554 1.2838 -0.3707 0.3066 -0.0704 234 LYS A CD 1883 C CE . LYS A 234 ? 2.2491 1.7765 1.3142 -0.3905 0.3130 -0.0734 234 LYS A CE 1884 N NZ . LYS A 234 ? 2.2025 1.7696 1.3227 -0.3693 0.2934 -0.0721 234 LYS A NZ 1885 N N . PRO A 235 ? 2.0238 1.7565 1.2046 -0.4620 0.3400 -0.1246 235 PRO A N 1886 C CA . PRO A 235 ? 1.9956 1.7421 1.1644 -0.5001 0.3619 -0.1381 235 PRO A CA 1887 C C . PRO A 235 ? 2.0659 1.7354 1.1539 -0.5146 0.3815 -0.1311 235 PRO A C 1888 O O . PRO A 235 ? 2.0876 1.6871 1.1232 -0.5062 0.3831 -0.1182 235 PRO A O 1889 C CB . PRO A 235 ? 1.9854 1.7537 1.1734 -0.5269 0.3691 -0.1484 235 PRO A CB 1890 C CG . PRO A 235 ? 1.9836 1.7140 1.1615 -0.5069 0.3574 -0.1359 235 PRO A CG 1891 C CD . PRO A 235 ? 1.9592 1.6965 1.1591 -0.4641 0.3348 -0.1247 235 PRO A CD 1892 N N . ASN A 236 ? 2.1437 1.8255 1.2205 -0.5346 0.3962 -0.1395 236 ASN A N 1893 C CA . ASN A 236 ? 2.2356 1.8464 1.2342 -0.5527 0.4177 -0.1346 236 ASN A CA 1894 C C . ASN A 236 ? 2.2651 1.8164 1.2177 -0.5184 0.4086 -0.1171 236 ASN A C 1895 O O . ASN A 236 ? 2.3283 1.8041 1.2061 -0.5260 0.4237 -0.1090 236 ASN A O 1896 C CB . ASN A 236 ? 2.3144 1.8713 1.2643 -0.5836 0.4366 -0.1349 236 ASN A CB 1897 C CG . ASN A 236 ? 2.4591 1.9783 1.3513 -0.6230 0.4660 -0.1413 236 ASN A CG 1898 O OD1 . ASN A 236 ? 2.5003 2.0446 1.3967 -0.6313 0.4733 -0.1480 236 ASN A OD1 1899 N ND2 . ASN A 236 ? 2.5612 2.0190 1.3982 -0.6487 0.4838 -0.1396 236 ASN A ND2 1900 N N . ASP A 237 ? 2.2226 1.8085 1.2192 -0.4806 0.3842 -0.1120 237 ASP A N 1901 C CA . ASP A 237 ? 2.2504 1.7935 1.2134 -0.4454 0.3728 -0.0975 237 ASP A CA 1902 C C . ASP A 237 ? 2.1735 1.7681 1.1730 -0.4324 0.3643 -0.1028 237 ASP A C 1903 O O . ASP A 237 ? 2.0935 1.7627 1.1583 -0.4381 0.3585 -0.1150 237 ASP A O 1904 C CB . ASP A 237 ? 2.2435 1.7795 1.2241 -0.4107 0.3506 -0.0867 237 ASP A CB 1905 C CG . ASP A 237 ? 2.2801 1.7679 1.2202 -0.3742 0.3393 -0.0721 237 ASP A CG 1906 O OD1 . ASP A 237 ? 2.3572 1.7888 1.2323 -0.3782 0.3524 -0.0669 237 ASP A OD1 1907 O OD2 . ASP A 237 ? 2.2340 1.7406 1.2066 -0.3415 0.3174 -0.0664 237 ASP A OD2 1908 N N . ALA A 238 ? 2.1905 1.7445 1.1463 -0.4138 0.3633 -0.0938 238 ALA A N 1909 C CA . ALA A 238 ? 2.1369 1.7311 1.1169 -0.4041 0.3580 -0.0989 238 ALA A CA 1910 C C . ALA A 238 ? 2.0823 1.6774 1.0741 -0.3600 0.3340 -0.0891 238 ALA A C 1911 O O . ALA A 238 ? 2.1289 1.6682 1.0784 -0.3383 0.3279 -0.0761 238 ALA A O 1912 C CB . ALA A 238 ? 2.1918 1.7438 1.1104 -0.4252 0.3804 -0.0997 238 ALA A CB 1913 N N . ILE A 239 ? 1.9918 1.6511 1.0405 -0.3472 0.3208 -0.0963 239 ILE A N 1914 C CA . ILE A 239 ? 1.9498 1.6191 1.0156 -0.3081 0.2983 -0.0897 239 ILE A CA 1915 C C . ILE A 239 ? 1.9652 1.6290 1.0073 -0.3012 0.3011 -0.0903 239 ILE A C 1916 O O . ILE A 239 ? 1.9159 1.6161 0.9765 -0.3204 0.3107 -0.1012 239 ILE A O 1917 C CB . ILE A 239 ? 1.8514 1.5941 0.9996 -0.2945 0.2785 -0.0964 239 ILE A CB 1918 C CG1 . ILE A 239 ? 1.8236 1.5695 0.9851 -0.2550 0.2556 -0.0890 239 ILE A CG1 1919 C CG2 . ILE A 239 ? 1.8130 1.6216 1.0096 -0.3108 0.2823 -0.1112 239 ILE A CG2 1920 C CD1 . ILE A 239 ? 1.7312 1.5370 0.9652 -0.2408 0.2365 -0.0936 239 ILE A CD1 1921 N N . ASN A 240 ? 1.9903 1.6098 0.9913 -0.2728 0.2922 -0.0792 240 ASN A N 1922 C CA . ASN A 240 ? 2.0342 1.6366 1.0009 -0.2639 0.2950 -0.0779 240 ASN A CA 1923 C C . ASN A 240 ? 1.9697 1.6110 0.9759 -0.2298 0.2714 -0.0781 240 ASN A C 1924 O O . ASN A 240 ? 1.9895 1.6177 0.9950 -0.2010 0.2546 -0.0702 240 ASN A O 1925 C CB . ASN A 240 ? 2.1488 1.6640 1.0278 -0.2568 0.3044 -0.0651 240 ASN A CB 1926 C CG . ASN A 240 ? 2.2428 1.7099 1.0758 -0.2897 0.3278 -0.0639 240 ASN A CG 1927 O OD1 . ASN A 240 ? 2.2844 1.7477 1.0985 -0.3213 0.3488 -0.0706 240 ASN A OD1 1928 N ND2 . ASN A 240 ? 2.2792 1.7097 1.0936 -0.2831 0.3248 -0.0558 240 ASN A ND2 1929 N N . PHE A 241 ? 1.9441 1.6334 0.9837 -0.2335 0.2704 -0.0878 241 PHE A N 1930 C CA . PHE A 241 ? 1.9109 1.6358 0.9848 -0.2038 0.2496 -0.0892 241 PHE A CA 1931 C C . PHE A 241 ? 1.9892 1.6831 1.0142 -0.1929 0.2528 -0.0862 241 PHE A C 1932 O O . PHE A 241 ? 2.0131 1.7008 1.0148 -0.2145 0.2703 -0.0909 241 PHE A O 1933 C CB . PHE A 241 ? 1.8298 1.6316 0.9773 -0.2117 0.2439 -0.1025 241 PHE A CB 1934 C CG . PHE A 241 ? 1.7869 1.6250 0.9883 -0.2154 0.2362 -0.1057 241 PHE A CG 1935 C CD1 . PHE A 241 ? 1.7674 1.6141 0.9954 -0.1892 0.2159 -0.1006 241 PHE A CD1 1936 C CD2 . PHE A 241 ? 1.7812 1.6455 1.0057 -0.2451 0.2493 -0.1142 241 PHE A CD2 1937 C CE1 . PHE A 241 ? 1.7050 1.5828 0.9804 -0.1923 0.2092 -0.1031 241 PHE A CE1 1938 C CE2 . PHE A 241 ? 1.7271 1.6237 0.9992 -0.2471 0.2417 -0.1170 241 PHE A CE2 1939 C CZ . PHE A 241 ? 1.6827 1.5844 0.9794 -0.2206 0.2218 -0.1110 241 PHE A CZ 1940 N N . GLU A 242 ? 2.0403 1.7159 1.0495 -0.1594 0.2361 -0.0788 242 GLU A N 1941 C CA . GLU A 242 ? 2.1455 1.8012 1.1171 -0.1433 0.2344 -0.0770 242 GLU A CA 1942 C C . GLU A 242 ? 2.0688 1.7715 1.0886 -0.1134 0.2098 -0.0806 242 GLU A C 1943 O O . GLU A 242 ? 2.0541 1.7651 1.0965 -0.0932 0.1933 -0.0771 242 GLU A O 1944 C CB . GLU A 242 ? 2.2951 1.8709 1.1838 -0.1299 0.2396 -0.0640 242 GLU A CB 1945 C CG . GLU A 242 ? 2.4351 1.9699 1.2615 -0.1373 0.2556 -0.0626 242 GLU A CG 1946 C CD . GLU A 242 ? 2.5386 2.0066 1.2914 -0.1090 0.2515 -0.0508 242 GLU A CD 1947 O OE1 . GLU A 242 ? 2.5297 2.0113 1.2959 -0.0746 0.2296 -0.0488 242 GLU A OE1 1948 O OE2 . GLU A 242 ? 2.5955 1.9970 1.2750 -0.1210 0.2706 -0.0441 242 GLU A OE2 1949 N N . SER A 243 ? 2.0257 1.7593 1.0611 -0.1116 0.2078 -0.0882 243 SER A N 1950 C CA . SER A 243 ? 1.9568 1.7334 1.0348 -0.0851 0.1855 -0.0928 243 SER A CA 1951 C C . SER A 243 ? 1.9536 1.7410 1.0212 -0.0803 0.1860 -0.0983 243 SER A C 1952 O O . SER A 243 ? 1.9967 1.7809 1.0481 -0.1028 0.2035 -0.1023 243 SER A O 1953 C CB . SER A 243 ? 1.8732 1.7138 1.0298 -0.0911 0.1760 -0.1015 243 SER A CB 1954 O OG . SER A 243 ? 1.8289 1.7100 1.0251 -0.0689 0.1565 -0.1071 243 SER A OG 1955 N N . ASN A 244 ? 1.9211 1.7230 0.9990 -0.0513 0.1668 -0.0992 244 ASN A N 1956 C CA . ASN A 244 ? 1.9232 1.7410 0.9976 -0.0433 0.1638 -0.1053 244 ASN A CA 1957 C C . ASN A 244 ? 1.8592 1.7404 1.0013 -0.0310 0.1449 -0.1155 244 ASN A C 1958 O O . ASN A 244 ? 1.8537 1.7479 0.9948 -0.0159 0.1361 -0.1200 244 ASN A O 1959 C CB . ASN A 244 ? 1.9736 1.7416 0.9829 -0.0189 0.1598 -0.0974 244 ASN A CB 1960 C CG . ASN A 244 ? 1.9668 1.7356 0.9836 0.0128 0.1379 -0.0935 244 ASN A CG 1961 O OD1 . ASN A 244 ? 1.9395 1.7370 1.0033 0.0145 0.1280 -0.0948 244 ASN A OD1 1962 N ND2 . ASN A 244 ? 1.9830 1.7210 0.9523 0.0385 0.1305 -0.0892 244 ASN A ND2 1963 N N . GLY A 245 ? 1.8291 1.7474 1.0276 -0.0378 0.1391 -0.1192 245 GLY A N 1964 C CA . GLY A 245 ? 1.7650 1.7402 1.0269 -0.0288 0.1229 -0.1289 245 GLY A CA 1965 C C . GLY A 245 ? 1.6945 1.6923 1.0022 -0.0262 0.1125 -0.1284 245 GLY A C 1966 O O . GLY A 245 ? 1.7685 1.7367 1.0568 -0.0245 0.1138 -0.1198 245 GLY A O 1967 N N . ASN A 246 ? 1.6420 1.6904 1.0084 -0.0255 0.1026 -0.1378 246 ASN A N 1968 C CA . ASN A 246 ? 1.5924 1.6669 1.0068 -0.0217 0.0913 -0.1387 246 ASN A CA 1969 C C . ASN A 246 ? 1.5613 1.6341 0.9882 -0.0423 0.1024 -0.1361 246 ASN A C 1970 O O . ASN A 246 ? 1.5205 1.6079 0.9803 -0.0396 0.0946 -0.1352 246 ASN A O 1971 C CB . ASN A 246 ? 1.5980 1.6564 1.0010 0.0025 0.0763 -0.1326 246 ASN A CB 1972 C CG . ASN A 246 ? 1.5870 1.6579 0.9888 0.0239 0.0623 -0.1376 246 ASN A CG 1973 O OD1 . ASN A 246 ? 1.5388 1.6487 0.9853 0.0304 0.0498 -0.1458 246 ASN A OD1 1974 N ND2 . ASN A 246 ? 1.6281 1.6643 0.9767 0.0349 0.0643 -0.1329 246 ASN A ND2 1975 N N . PHE A 247 ? 1.5892 1.6463 0.9909 -0.0636 0.1208 -0.1357 247 PHE A N 1976 C CA . PHE A 247 ? 1.5409 1.5894 0.9440 -0.0839 0.1329 -0.1328 247 PHE A CA 1977 C C . PHE A 247 ? 1.4704 1.5688 0.9297 -0.0976 0.1336 -0.1428 247 PHE A C 1978 O O . PHE A 247 ? 1.4368 1.5636 0.9118 -0.1046 0.1376 -0.1519 247 PHE A O 1979 C CB . PHE A 247 ? 1.6279 1.6364 0.9761 -0.1025 0.1535 -0.1289 247 PHE A CB 1980 C CG . PHE A 247 ? 1.6489 1.6448 0.9924 -0.1257 0.1676 -0.1265 247 PHE A CG 1981 C CD1 . PHE A 247 ? 1.6187 1.6065 0.9740 -0.1214 0.1613 -0.1207 247 PHE A CD1 1982 C CD2 . PHE A 247 ? 1.6709 1.6628 0.9963 -0.1526 0.1877 -0.1307 247 PHE A CD2 1983 C CE1 . PHE A 247 ? 1.6219 1.5978 0.9716 -0.1431 0.1742 -0.1190 247 PHE A CE1 1984 C CE2 . PHE A 247 ? 1.6709 1.6527 0.9915 -0.1754 0.2010 -0.1298 247 PHE A CE2 1985 C CZ . PHE A 247 ? 1.6611 1.6342 0.9936 -0.1704 0.1939 -0.1239 247 PHE A CZ 1986 N N . ILE A 248 ? 1.4451 1.5540 0.9336 -0.0996 0.1292 -0.1411 248 ILE A N 1987 C CA . ILE A 248 ? 1.4096 1.5601 0.9451 -0.1133 0.1315 -0.1496 248 ILE A CA 1988 C C . ILE A 248 ? 1.4256 1.5587 0.9420 -0.1367 0.1483 -0.1472 248 ILE A C 1989 O O . ILE A 248 ? 1.4306 1.5400 0.9371 -0.1374 0.1483 -0.1396 248 ILE A O 1990 C CB . ILE A 248 ? 1.3815 1.5570 0.9633 -0.1004 0.1157 -0.1503 248 ILE A CB 1991 C CG1 . ILE A 248 ? 1.3894 1.5713 0.9804 -0.0767 0.0990 -0.1508 248 ILE A CG1 1992 C CG2 . ILE A 248 ? 1.3337 1.5539 0.9624 -0.1109 0.1169 -0.1603 248 ILE A CG2 1993 C CD1 . ILE A 248 ? 1.4149 1.6193 1.0130 -0.0735 0.0975 -0.1597 248 ILE A CD1 1994 N N . ALA A 249 ? 1.4547 1.5996 0.9647 -0.1564 0.1631 -0.1543 249 ALA A N 1995 C CA . ALA A 249 ? 1.4890 1.6145 0.9729 -0.1818 0.1817 -0.1533 249 ALA A CA 1996 C C . ALA A 249 ? 1.4349 1.5985 0.9619 -0.1960 0.1840 -0.1607 249 ALA A C 1997 O O . ALA A 249 ? 1.3941 1.6038 0.9679 -0.1900 0.1753 -0.1693 249 ALA A O 1998 C CB . ALA A 249 ? 1.5409 1.6601 0.9934 -0.1976 0.1981 -0.1581 249 ALA A CB 1999 N N . PRO A 250 ? 1.4298 1.5729 0.9391 -0.2146 0.1957 -0.1576 250 PRO A N 2000 C CA . PRO A 250 ? 1.4192 1.5984 0.9649 -0.2305 0.1997 -0.1657 250 PRO A CA 2001 C C . PRO A 250 ? 1.4392 1.6516 0.9919 -0.2525 0.2145 -0.1786 250 PRO A C 2002 O O . PRO A 250 ? 1.5564 1.7446 1.0684 -0.2681 0.2300 -0.1785 250 PRO A O 2003 C CB . PRO A 250 ? 1.4438 1.5827 0.9593 -0.2433 0.2083 -0.1575 250 PRO A CB 2004 C CG . PRO A 250 ? 1.4845 1.5666 0.9385 -0.2436 0.2168 -0.1483 250 PRO A CG 2005 C CD . PRO A 250 ? 1.4813 1.5641 0.9350 -0.2188 0.2039 -0.1460 250 PRO A CD 2006 N N . GLU A 251 ? 1.4128 1.6799 1.0153 -0.2532 0.2098 -0.1899 251 GLU A N 2007 C CA . GLU A 251 ? 1.4593 1.7640 1.0731 -0.2757 0.2241 -0.2037 251 GLU A CA 2008 C C . GLU A 251 ? 1.4540 1.7718 1.0820 -0.2936 0.2304 -0.2075 251 GLU A C 2009 O O . GLU A 251 ? 1.4585 1.7735 1.0661 -0.3205 0.2484 -0.2127 251 GLU A O 2010 C CB . GLU A 251 ? 1.4634 1.8226 1.1203 -0.2639 0.2156 -0.2155 251 GLU A CB 2011 C CG . GLU A 251 ? 1.5280 1.9237 1.1884 -0.2849 0.2313 -0.2299 251 GLU A CG 2012 C CD . GLU A 251 ? 1.5478 2.0006 1.2529 -0.2726 0.2228 -0.2428 251 GLU A CD 2013 O OE1 . GLU A 251 ? 1.5706 2.0263 1.2940 -0.2475 0.2062 -0.2397 251 GLU A OE1 2014 O OE2 . GLU A 251 ? 1.5527 2.0477 1.2737 -0.2882 0.2331 -0.2566 251 GLU A OE2 2015 N N . TYR A 252 ? 1.4026 1.7343 1.0648 -0.2793 0.2159 -0.2053 252 TYR A N 2016 C CA . TYR A 252 ? 1.3622 1.7077 1.0411 -0.2927 0.2191 -0.2087 252 TYR A CA 2017 C C . TYR A 252 ? 1.3684 1.6685 1.0295 -0.2863 0.2135 -0.1946 252 TYR A C 2018 O O . TYR A 252 ? 1.3522 1.6278 1.0087 -0.2640 0.2006 -0.1843 252 TYR A O 2019 C CB . TYR A 252 ? 1.3032 1.7061 1.0376 -0.2818 0.2076 -0.2191 252 TYR A CB 2020 C CG . TYR A 252 ? 1.3013 1.7534 1.0560 -0.2862 0.2124 -0.2342 252 TYR A CG 2021 C CD1 . TYR A 252 ? 1.3090 1.7908 1.0645 -0.3118 0.2283 -0.2470 252 TYR A CD1 2022 C CD2 . TYR A 252 ? 1.2698 1.7398 1.0425 -0.2650 0.2013 -0.2365 252 TYR A CD2 2023 C CE1 . TYR A 252 ? 1.2926 1.8222 1.0670 -0.3148 0.2327 -0.2616 252 TYR A CE1 2024 C CE2 . TYR A 252 ? 1.2426 1.7568 1.0324 -0.2675 0.2055 -0.2504 252 TYR A CE2 2025 C CZ . TYR A 252 ? 1.2584 1.8032 1.0494 -0.2918 0.2211 -0.2629 252 TYR A CZ 2026 O OH . TYR A 252 ? 1.2108 1.8023 1.0193 -0.2932 0.2252 -0.2775 252 TYR A OH 2027 N N . ALA A 253 ? 1.3816 1.6719 1.0321 -0.3065 0.2237 -0.1952 253 ALA A N 2028 C CA . ALA A 253 ? 1.3792 1.6322 1.0171 -0.3020 0.2190 -0.1837 253 ALA A CA 2029 C C . ALA A 253 ? 1.3602 1.6452 1.0291 -0.3133 0.2196 -0.1913 253 ALA A C 2030 O O . ALA A 253 ? 1.3838 1.7154 1.0768 -0.3270 0.2258 -0.2055 253 ALA A O 2031 C CB . ALA A 253 ? 1.4470 1.6394 1.0249 -0.3165 0.2331 -0.1747 253 ALA A CB 2032 N N . TYR A 254 ? 1.3441 1.6055 1.0120 -0.3070 0.2130 -0.1825 254 TYR A N 2033 C CA . TYR A 254 ? 1.2899 1.5792 0.9870 -0.3146 0.2116 -0.1887 254 TYR A CA 2034 C C . TYR A 254 ? 1.3131 1.5663 0.9759 -0.3375 0.2250 -0.1854 254 TYR A C 2035 O O . TYR A 254 ? 1.3237 1.5249 0.9542 -0.3313 0.2238 -0.1722 254 TYR A O 2036 C CB . TYR A 254 ? 1.2563 1.5513 0.9844 -0.2884 0.1925 -0.1821 254 TYR A CB 2037 C CG . TYR A 254 ? 1.1978 1.5298 0.9634 -0.2664 0.1786 -0.1863 254 TYR A CG 2038 C CD1 . TYR A 254 ? 1.2261 1.5388 0.9826 -0.2473 0.1703 -0.1788 254 TYR A CD1 2039 C CD2 . TYR A 254 ? 1.1499 1.5348 0.9586 -0.2638 0.1735 -0.1982 254 TYR A CD2 2040 C CE1 . TYR A 254 ? 1.2053 1.5492 0.9943 -0.2283 0.1581 -0.1831 254 TYR A CE1 2041 C CE2 . TYR A 254 ? 1.1313 1.5452 0.9705 -0.2433 0.1613 -0.2019 254 TYR A CE2 2042 C CZ . TYR A 254 ? 1.1778 1.5704 1.0072 -0.2265 0.1539 -0.1944 254 TYR A CZ 2043 O OH . TYR A 254 ? 1.1785 1.5980 1.0366 -0.2076 0.1424 -0.1987 254 TYR A OH 2044 N N . LYS A 255 ? 1.3429 1.6243 1.0119 -0.3636 0.2379 -0.1983 255 LYS A N 2045 C CA . LYS A 255 ? 1.3913 1.6463 1.0350 -0.3870 0.2499 -0.1977 255 LYS A CA 2046 C C . LYS A 255 ? 1.3330 1.5947 1.0035 -0.3742 0.2369 -0.1941 255 LYS A C 2047 O O . LYS A 255 ? 1.2458 1.5566 0.9631 -0.3617 0.2253 -0.2012 255 LYS A O 2048 C CB . LYS A 255 ? 1.4335 1.7266 1.0831 -0.4190 0.2664 -0.2151 255 LYS A CB 2049 C CG . LYS A 255 ? 1.5058 1.7898 1.1234 -0.4391 0.2838 -0.2201 255 LYS A CG 2050 C CD . LYS A 255 ? 1.5089 1.8533 1.1506 -0.4642 0.2956 -0.2408 255 LYS A CD 2051 C CE . LYS A 255 ? 1.5494 1.8925 1.1795 -0.4957 0.3098 -0.2486 255 LYS A CE 2052 N NZ . LYS A 255 ? 1.6410 1.9674 1.2307 -0.5316 0.3344 -0.2559 255 LYS A NZ 2053 N N . ILE A 256 ? 1.3544 1.5650 0.9930 -0.3768 0.2392 -0.1831 256 ILE A N 2054 C CA . ILE A 256 ? 1.3726 1.5858 1.0318 -0.3677 0.2290 -0.1796 256 ILE A CA 2055 C C . ILE A 256 ? 1.4145 1.6433 1.0740 -0.3966 0.2413 -0.1907 256 ILE A C 2056 O O . ILE A 256 ? 1.4606 1.6457 1.0776 -0.4170 0.2549 -0.1874 256 ILE A O 2057 C CB . ILE A 256 ? 1.3915 1.5427 1.0170 -0.3533 0.2241 -0.1622 256 ILE A CB 2058 C CG1 . ILE A 256 ? 1.3828 1.5252 1.0132 -0.3234 0.2102 -0.1526 256 ILE A CG1 2059 C CG2 . ILE A 256 ? 1.3912 1.5439 1.0348 -0.3478 0.2161 -0.1595 256 ILE A CG2 2060 C CD1 . ILE A 256 ? 1.4351 1.5132 1.0190 -0.3123 0.2097 -0.1371 256 ILE A CD1 2061 N N . VAL A 257 ? 1.3990 1.6892 1.1046 -0.3979 0.2365 -0.2042 257 VAL A N 2062 C CA . VAL A 257 ? 1.4446 1.7611 1.1554 -0.4260 0.2479 -0.2180 257 VAL A CA 2063 C C . VAL A 257 ? 1.4470 1.7593 1.1694 -0.4222 0.2407 -0.2153 257 VAL A C 2064 O O . VAL A 257 ? 1.4593 1.7611 1.1640 -0.4470 0.2522 -0.2203 257 VAL A O 2065 C CB . VAL A 257 ? 1.4179 1.8078 1.1684 -0.4333 0.2494 -0.2374 257 VAL A CB 2066 C CG1 . VAL A 257 ? 1.4662 1.8571 1.1982 -0.4447 0.2612 -0.2418 257 VAL A CG1 2067 C CG2 . VAL A 257 ? 1.3672 1.8015 1.1672 -0.4029 0.2297 -0.2392 257 VAL A CG2 2068 N N . LYS A 258 ? 1.4713 1.7903 1.2216 -0.3923 0.2223 -0.2075 258 LYS A N 2069 C CA . LYS A 258 ? 1.4909 1.8076 1.2547 -0.3854 0.2140 -0.2043 258 LYS A CA 2070 C C . LYS A 258 ? 1.4842 1.7539 1.2355 -0.3609 0.2026 -0.1859 258 LYS A C 2071 O O . LYS A 258 ? 1.4933 1.7692 1.2629 -0.3355 0.1899 -0.1799 258 LYS A O 2072 C CB . LYS A 258 ? 1.4611 1.8419 1.2773 -0.3732 0.2023 -0.2158 258 LYS A CB 2073 C CG . LYS A 258 ? 1.5110 1.9401 1.3417 -0.3982 0.2121 -0.2351 258 LYS A CG 2074 C CD . LYS A 258 ? 1.4994 1.9284 1.3339 -0.4059 0.2112 -0.2373 258 LYS A CD 2075 C CE . LYS A 258 ? 1.4364 1.9027 1.3138 -0.3800 0.1935 -0.2390 258 LYS A CE 2076 N NZ . LYS A 258 ? 1.4596 1.9253 1.3404 -0.3856 0.1918 -0.2407 258 LYS A NZ 2077 N N . LYS A 259 ? 1.5197 1.7435 1.2396 -0.3690 0.2077 -0.1779 259 LYS A N 2078 C CA . LYS A 259 ? 1.5340 1.7190 1.2455 -0.3464 0.1967 -0.1623 259 LYS A CA 2079 C C . LYS A 259 ? 1.4955 1.7068 1.2406 -0.3383 0.1866 -0.1649 259 LYS A C 2080 O O . LYS A 259 ? 1.4136 1.6724 1.1870 -0.3486 0.1876 -0.1787 259 LYS A O 2081 C CB . LYS A 259 ? 1.6261 1.7447 1.2822 -0.3578 0.2076 -0.1522 259 LYS A CB 2082 C CG . LYS A 259 ? 1.7081 1.7897 1.3256 -0.3581 0.2148 -0.1456 259 LYS A CG 2083 C CD . LYS A 259 ? 1.7338 1.7814 1.3409 -0.3279 0.2024 -0.1300 259 LYS A CD 2084 C CE . LYS A 259 ? 1.7913 1.8088 1.3641 -0.3246 0.2074 -0.1245 259 LYS A CE 2085 N NZ . LYS A 259 ? 1.8517 1.8311 1.3739 -0.3523 0.2271 -0.1264 259 LYS A NZ 2086 N N . GLY A 260 ? 1.5565 1.7388 1.2985 -0.3189 0.1768 -0.1523 260 GLY A N 2087 C CA . GLY A 260 ? 1.5603 1.7599 1.3284 -0.3112 0.1681 -0.1532 260 GLY A CA 2088 C C . GLY A 260 ? 1.5311 1.7354 1.3252 -0.2805 0.1514 -0.1444 260 GLY A C 2089 O O . GLY A 260 ? 1.5251 1.7038 1.3077 -0.2646 0.1467 -0.1340 260 GLY A O 2090 N N . ASP A 261 ? 1.5261 1.7635 1.3542 -0.2727 0.1429 -0.1492 261 ASP A N 2091 C CA . ASP A 261 ? 1.4665 1.7068 1.3183 -0.2460 0.1284 -0.1415 261 ASP A CA 2092 C C . ASP A 261 ? 1.3484 1.6274 1.2328 -0.2318 0.1202 -0.1468 261 ASP A C 2093 O O . ASP A 261 ? 1.2826 1.6042 1.1897 -0.2375 0.1207 -0.1594 261 ASP A O 2094 C CB . ASP A 261 ? 1.5491 1.8005 1.4173 -0.2438 0.1236 -0.1432 261 ASP A CB 2095 C CG . ASP A 261 ? 1.6916 1.8969 1.5300 -0.2474 0.1269 -0.1333 261 ASP A CG 2096 O OD1 . ASP A 261 ? 1.8181 1.9823 1.6204 -0.2533 0.1341 -0.1261 261 ASP A OD1 2097 O OD2 . ASP A 261 ? 1.7186 1.9275 1.5680 -0.2432 0.1223 -0.1329 261 ASP A OD2 2098 N N . SER A 262 ? 1.2674 1.5312 1.1530 -0.2129 0.1126 -0.1377 262 SER A N 2099 C CA . SER A 262 ? 1.2527 1.5466 1.1670 -0.1973 0.1040 -0.1413 262 SER A CA 2100 C C . SER A 262 ? 1.2516 1.5222 1.1665 -0.1764 0.0946 -0.1295 262 SER A C 2101 O O . SER A 262 ? 1.3300 1.5651 1.2242 -0.1738 0.0949 -0.1194 262 SER A O 2102 C CB . SER A 262 ? 1.2879 1.5952 1.1963 -0.2063 0.1104 -0.1481 262 SER A CB 2103 O OG . SER A 262 ? 1.2433 1.5769 1.1770 -0.1908 0.1021 -0.1515 262 SER A OG 2104 N N . THR A 263 ? 1.1637 1.4548 1.1017 -0.1616 0.0866 -0.1314 263 THR A N 2105 C CA . THR A 263 ? 1.1137 1.3875 1.0544 -0.1434 0.0781 -0.1223 263 THR A CA 2106 C C . THR A 263 ? 1.0434 1.3396 1.0029 -0.1333 0.0726 -0.1270 263 THR A C 2107 O O . THR A 263 ? 0.9847 1.3123 0.9606 -0.1365 0.0734 -0.1371 263 THR A O 2108 C CB . THR A 263 ? 1.1362 1.4066 1.0917 -0.1322 0.0709 -0.1174 263 THR A CB 2109 O OG1 . THR A 263 ? 1.1947 1.4443 1.1473 -0.1177 0.0647 -0.1081 263 THR A OG1 2110 C CG2 . THR A 263 ? 1.0991 1.4035 1.0862 -0.1248 0.0650 -0.1252 263 THR A CG2 2111 N N . ILE A 264 ? 1.0609 1.3416 1.0171 -0.1209 0.0672 -0.1204 264 ILE A N 2112 C CA . ILE A 264 ? 1.0357 1.3346 1.0107 -0.1095 0.0607 -0.1243 264 ILE A CA 2113 C C . ILE A 264 ? 1.0076 1.3077 1.0032 -0.0948 0.0517 -0.1210 264 ILE A C 2114 O O . ILE A 264 ? 1.0419 1.3209 1.0310 -0.0879 0.0485 -0.1127 264 ILE A O 2115 C CB . ILE A 264 ? 1.0192 1.3032 0.9770 -0.1064 0.0608 -0.1210 264 ILE A CB 2116 C CG1 . ILE A 264 ? 1.0839 1.3610 1.0163 -0.1221 0.0712 -0.1233 264 ILE A CG1 2117 C CG2 . ILE A 264 ? 0.9632 1.2675 0.9406 -0.0962 0.0545 -0.1264 264 ILE A CG2 2118 C CD1 . ILE A 264 ? 1.1348 1.3959 1.0466 -0.1190 0.0719 -0.1202 264 ILE A CD1 2119 N N . MET A 265 ? 0.9724 1.2973 0.9912 -0.0898 0.0481 -0.1280 265 MET A N 2120 C CA . MET A 265 ? 0.9255 1.2517 0.9624 -0.0778 0.0411 -0.1262 265 MET A CA 2121 C C . MET A 265 ? 0.9090 1.2424 0.9583 -0.0671 0.0354 -0.1289 265 MET A C 2122 O O . MET A 265 ? 0.9585 1.3084 1.0109 -0.0682 0.0363 -0.1361 265 MET A O 2123 C CB . MET A 265 ? 0.9469 1.2938 0.9971 -0.0790 0.0414 -0.1328 265 MET A CB 2124 C CG . MET A 265 ? 0.9647 1.3092 1.0287 -0.0680 0.0357 -0.1304 265 MET A CG 2125 S SD . MET A 265 ? 0.9926 1.3609 1.0665 -0.0700 0.0364 -0.1385 265 MET A SD 2126 C CE . MET A 265 ? 1.0019 1.3545 1.0584 -0.0845 0.0428 -0.1332 265 MET A CE 2127 N N . LYS A 266 ? 0.9357 1.2570 0.9912 -0.0576 0.0301 -0.1238 266 LYS A N 2128 C CA . LYS A 266 ? 0.9282 1.2542 0.9948 -0.0487 0.0251 -0.1268 266 LYS A CA 2129 C C . LYS A 266 ? 0.9134 1.2470 0.9965 -0.0410 0.0216 -0.1303 266 LYS A C 2130 O O . LYS A 266 ? 0.9827 1.3069 1.0691 -0.0383 0.0206 -0.1257 266 LYS A O 2131 C CB . LYS A 266 ? 0.9678 1.2773 1.0304 -0.0440 0.0219 -0.1204 266 LYS A CB 2132 C CG . LYS A 266 ? 1.0644 1.3644 1.1078 -0.0481 0.0242 -0.1171 266 LYS A CG 2133 C CD . LYS A 266 ? 1.1585 1.4695 1.2003 -0.0485 0.0240 -0.1234 266 LYS A CD 2134 C CE . LYS A 266 ? 1.2310 1.5292 1.2515 -0.0501 0.0255 -0.1195 266 LYS A CE 2135 N NZ . LYS A 266 ? 1.2576 1.5426 1.2570 -0.0592 0.0323 -0.1151 266 LYS A NZ 2136 N N . SER A 267 ? 0.9011 1.2500 0.9924 -0.0368 0.0201 -0.1383 267 SER A N 2137 C CA . SER A 267 ? 0.9029 1.2575 1.0054 -0.0280 0.0172 -0.1424 267 SER A CA 2138 C C . SER A 267 ? 0.9213 1.2875 1.0290 -0.0219 0.0151 -0.1507 267 SER A C 2139 O O . SER A 267 ? 1.0484 1.4276 1.1528 -0.0260 0.0171 -0.1555 267 SER A O 2140 C CB . SER A 267 ? 0.9146 1.2821 1.0183 -0.0304 0.0194 -0.1452 267 SER A CB 2141 O OG . SER A 267 ? 0.9137 1.2873 1.0259 -0.0196 0.0161 -0.1498 267 SER A OG 2142 N N . GLU A 268 ? 0.9344 1.2938 1.0483 -0.0120 0.0116 -0.1524 268 GLU A N 2143 C CA . GLU A 268 ? 0.9587 1.3255 1.0753 -0.0045 0.0094 -0.1605 268 GLU A CA 2144 C C . GLU A 268 ? 0.9513 1.3348 1.0709 0.0032 0.0089 -0.1677 268 GLU A C 2145 O O . GLU A 268 ? 0.9754 1.3671 1.0959 0.0114 0.0071 -0.1754 268 GLU A O 2146 C CB . GLU A 268 ? 0.9810 1.3279 1.0991 0.0012 0.0066 -0.1590 268 GLU A CB 2147 C CG . GLU A 268 ? 1.0164 1.3514 1.1333 -0.0055 0.0065 -0.1532 268 GLU A CG 2148 C CD . GLU A 268 ? 1.0514 1.3959 1.1645 -0.0106 0.0068 -0.1557 268 GLU A CD 2149 O OE1 . GLU A 268 ? 1.0126 1.3636 1.1261 -0.0071 0.0056 -0.1627 268 GLU A OE1 2150 O OE2 . GLU A 268 ? 1.0699 1.4133 1.1776 -0.0173 0.0084 -0.1505 268 GLU A OE2 2151 N N . LEU A 269 ? 0.9624 1.3523 1.0828 0.0012 0.0102 -0.1661 269 LEU A N 2152 C CA . LEU A 269 ? 0.9862 1.3964 1.1099 0.0089 0.0092 -0.1739 269 LEU A CA 2153 C C . LEU A 269 ? 1.0549 1.4953 1.1803 0.0036 0.0119 -0.1827 269 LEU A C 2154 O O . LEU A 269 ? 1.0861 1.5291 1.2080 -0.0084 0.0157 -0.1812 269 LEU A O 2155 C CB . LEU A 269 ? 0.9675 1.3769 1.0917 0.0076 0.0096 -0.1700 269 LEU A CB 2156 C CG . LEU A 269 ? 0.9611 1.3427 1.0833 0.0138 0.0074 -0.1621 269 LEU A CG 2157 C CD1 . LEU A 269 ? 0.9628 1.3449 1.0847 0.0108 0.0083 -0.1582 269 LEU A CD1 2158 C CD2 . LEU A 269 ? 0.9730 1.3463 1.0936 0.0300 0.0037 -0.1663 269 LEU A CD2 2159 N N . GLU A 270 ? 1.0988 1.5618 1.2283 0.0135 0.0101 -0.1922 270 GLU A N 2160 C CA . GLU A 270 ? 1.1360 1.6334 1.2689 0.0094 0.0129 -0.2027 270 GLU A CA 2161 C C . GLU A 270 ? 1.0702 1.5926 1.2081 0.0085 0.0136 -0.2081 270 GLU A C 2162 O O . GLU A 270 ? 1.0540 1.5642 1.1914 0.0110 0.0118 -0.2029 270 GLU A O 2163 C CB . GLU A 270 ? 1.2406 1.7490 1.3748 0.0236 0.0098 -0.2118 270 GLU A CB 2164 C CG . GLU A 270 ? 1.3245 1.8078 1.4539 0.0263 0.0082 -0.2079 270 GLU A CG 2165 C CD . GLU A 270 ? 1.3560 1.8440 1.4830 0.0130 0.0124 -0.2076 270 GLU A CD 2166 O OE1 . GLU A 270 ? 1.3541 1.8466 1.4792 -0.0020 0.0171 -0.2040 270 GLU A OE1 2167 O OE2 . GLU A 270 ? 1.3621 1.8471 1.4869 0.0180 0.0110 -0.2111 270 GLU A OE2 2168 N N . TYR A 271 ? 1.0248 1.5834 1.1674 0.0046 0.0164 -0.2193 271 TYR A N 2169 C CA . TYR A 271 ? 0.9682 1.5565 1.1165 0.0011 0.0177 -0.2267 271 TYR A CA 2170 C C . TYR A 271 ? 0.9530 1.5476 1.1050 0.0218 0.0106 -0.2310 271 TYR A C 2171 O O . TYR A 271 ? 0.9736 1.5669 1.1248 0.0399 0.0057 -0.2351 271 TYR A O 2172 C CB . TYR A 271 ? 0.9624 1.5916 1.1158 -0.0075 0.0227 -0.2396 271 TYR A CB 2173 C CG . TYR A 271 ? 0.9464 1.6084 1.1057 -0.0171 0.0258 -0.2480 271 TYR A CG 2174 C CD1 . TYR A 271 ? 0.9414 1.5899 1.0958 -0.0339 0.0302 -0.2409 271 TYR A CD1 2175 C CD2 . TYR A 271 ? 0.9409 1.6486 1.1103 -0.0094 0.0245 -0.2638 271 TYR A CD2 2176 C CE1 . TYR A 271 ? 0.9477 1.6260 1.1070 -0.0443 0.0334 -0.2494 271 TYR A CE1 2177 C CE2 . TYR A 271 ? 0.9256 1.6672 1.1016 -0.0193 0.0275 -0.2730 271 TYR A CE2 2178 C CZ . TYR A 271 ? 0.9320 1.6582 1.1028 -0.0376 0.0321 -0.2659 271 TYR A CZ 2179 O OH . TYR A 271 ? 0.8590 1.6188 1.0358 -0.0487 0.0353 -0.2759 271 TYR A OH 2180 N N . GLY A 272 ? 0.9919 1.5916 1.1456 0.0193 0.0101 -0.2304 272 GLY A N 2181 C CA . GLY A 272 ? 1.0209 1.6214 1.1750 0.0393 0.0032 -0.2328 272 GLY A CA 2182 C C . GLY A 272 ? 1.0378 1.6838 1.2001 0.0442 0.0016 -0.2469 272 GLY A C 2183 O O . GLY A 272 ? 1.0247 1.6741 1.1859 0.0636 -0.0049 -0.2503 272 GLY A O 2184 N N . ASN A 273 ? 1.0987 1.7796 1.2680 0.0269 0.0075 -0.2557 273 ASN A N 2185 C CA . ASN A 273 ? 1.1291 1.8609 1.3085 0.0280 0.0070 -0.2716 273 ASN A CA 2186 C C . ASN A 273 ? 1.0732 1.8074 1.2533 0.0275 0.0047 -0.2708 273 ASN A C 2187 O O . ASN A 273 ? 1.0966 1.8585 1.2816 0.0439 -0.0013 -0.2809 273 ASN A O 2188 C CB . ASN A 273 ? 1.1730 1.9320 1.3564 0.0535 0.0003 -0.2841 273 ASN A CB 2189 C CG . ASN A 273 ? 1.2153 1.9669 1.3961 0.0572 0.0016 -0.2842 273 ASN A CG 2190 O OD1 . ASN A 273 ? 1.2463 1.9548 1.4180 0.0612 0.0005 -0.2723 273 ASN A OD1 2191 N ND2 . ASN A 273 ? 1.2076 2.0028 1.3966 0.0560 0.0040 -0.2986 273 ASN A ND2 2192 N N . CYS A 274 ? 1.0336 1.7387 1.2078 0.0098 0.0092 -0.2591 274 CYS A N 2193 C CA . CYS A 274 ? 1.0459 1.7471 1.2189 0.0077 0.0076 -0.2565 274 CYS A CA 2194 C C . CYS A 274 ? 0.9845 1.6893 1.1559 -0.0215 0.0167 -0.2557 274 CYS A C 2195 O O . CYS A 274 ? 0.9863 1.6872 1.1546 -0.0386 0.0240 -0.2541 274 CYS A O 2196 C CB . CYS A 274 ? 1.1332 1.7838 1.2963 0.0182 0.0036 -0.2404 274 CYS A CB 2197 S SG . CYS A 274 ? 1.3755 1.9793 1.5301 0.0101 0.0077 -0.2249 274 CYS A SG 2198 N N . ASN A 275 ? 0.9368 1.6465 1.1081 -0.0269 0.0163 -0.2567 275 ASN A N 2199 C CA . ASN A 275 ? 0.9351 1.6373 1.1003 -0.0539 0.0249 -0.2537 275 ASN A CA 2200 C C . ASN A 275 ? 0.9459 1.6056 1.1013 -0.0521 0.0228 -0.2390 275 ASN A C 2201 O O . ASN A 275 ? 0.9733 1.6221 1.1295 -0.0313 0.0149 -0.2353 275 ASN A O 2202 C CB . ASN A 275 ? 0.9175 1.6699 1.0915 -0.0661 0.0278 -0.2710 275 ASN A CB 2203 C CG . ASN A 275 ? 0.9314 1.6763 1.0963 -0.0972 0.0386 -0.2698 275 ASN A CG 2204 O OD1 . ASN A 275 ? 0.9487 1.6645 1.1019 -0.1122 0.0459 -0.2608 275 ASN A OD1 2205 N ND2 . ASN A 275 ? 0.9960 1.7662 1.1643 -0.1066 0.0396 -0.2794 275 ASN A ND2 2206 N N . THR A 276 ? 0.9449 1.5785 1.0891 -0.0730 0.0302 -0.2304 276 THR A N 2207 C CA . THR A 276 ? 0.9609 1.5548 1.0952 -0.0726 0.0291 -0.2166 276 THR A CA 2208 C C . THR A 276 ? 0.9830 1.5590 1.1037 -0.0982 0.0385 -0.2121 276 THR A C 2209 O O . THR A 276 ? 1.0115 1.5945 1.1276 -0.1154 0.0462 -0.2159 276 THR A O 2210 C CB . THR A 276 ? 1.0035 1.5571 1.1331 -0.0583 0.0254 -0.2021 276 THR A CB 2211 O OG1 . THR A 276 ? 1.1089 1.6284 1.2301 -0.0569 0.0243 -0.1900 276 THR A OG1 2212 C CG2 . THR A 276 ? 1.0362 1.5730 1.1590 -0.0696 0.0312 -0.1964 276 THR A CG2 2213 N N . LYS A 277 ? 1.0199 1.5701 1.1320 -0.1002 0.0381 -0.2037 277 LYS A N 2214 C CA . LYS A 277 ? 1.0605 1.5865 1.1558 -0.1223 0.0467 -0.1980 277 LYS A CA 2215 C C . LYS A 277 ? 1.0077 1.4849 1.0897 -0.1192 0.0473 -0.1806 277 LYS A C 2216 O O . LYS A 277 ? 1.0119 1.4621 1.0764 -0.1340 0.0538 -0.1739 277 LYS A O 2217 C CB . LYS A 277 ? 1.1422 1.6728 1.2349 -0.1282 0.0465 -0.2014 277 LYS A CB 2218 C CG . LYS A 277 ? 1.2462 1.8270 1.3550 -0.1235 0.0422 -0.2184 277 LYS A CG 2219 C CD . LYS A 277 ? 1.3125 1.9364 1.4293 -0.1370 0.0475 -0.2343 277 LYS A CD 2220 C CE . LYS A 277 ? 1.3821 2.0057 1.4857 -0.1682 0.0594 -0.2392 277 LYS A CE 2221 N NZ . LYS A 277 ? 1.3973 2.0334 1.4997 -0.1775 0.0598 -0.2463 277 LYS A NZ 2222 N N . CYS A 278 ? 1.0015 1.4675 1.0905 -0.0998 0.0407 -0.1740 278 CYS A N 2223 C CA . CYS A 278 ? 1.0215 1.4464 1.1009 -0.0953 0.0404 -0.1589 278 CYS A CA 2224 C C . CYS A 278 ? 0.9241 1.3478 1.0127 -0.0794 0.0353 -0.1567 278 CYS A C 2225 O O . CYS A 278 ? 0.8841 1.3201 0.9842 -0.0631 0.0289 -0.1602 278 CYS A O 2226 C CB . CYS A 278 ? 1.0548 1.4563 1.1299 -0.0885 0.0374 -0.1503 278 CYS A CB 2227 S SG . CYS A 278 ? 1.1979 1.5552 1.2647 -0.0799 0.0360 -0.1334 278 CYS A SG 2228 N N . GLN A 279 ? 0.8548 1.2623 0.9364 -0.0839 0.0383 -0.1513 279 GLN A N 2229 C CA . GLN A 279 ? 0.8347 1.2430 0.9241 -0.0720 0.0345 -0.1508 279 GLN A CA 2230 C C . GLN A 279 ? 0.8260 1.2005 0.9083 -0.0681 0.0337 -0.1383 279 GLN A C 2231 O O . GLN A 279 ? 0.8241 1.1786 0.8923 -0.0782 0.0382 -0.1318 279 GLN A O 2232 C CB . GLN A 279 ? 0.8240 1.2532 0.9138 -0.0808 0.0386 -0.1591 279 GLN A CB 2233 C CG . GLN A 279 ? 0.8232 1.2560 0.9208 -0.0688 0.0347 -0.1603 279 GLN A CG 2234 C CD . GLN A 279 ? 0.8241 1.2803 0.9359 -0.0529 0.0285 -0.1687 279 GLN A CD 2235 O OE1 . GLN A 279 ? 0.7581 1.2469 0.8764 -0.0547 0.0291 -0.1802 279 GLN A OE1 2236 N NE2 . GLN A 279 ? 0.8171 1.2568 0.9324 -0.0371 0.0229 -0.1637 279 GLN A NE2 2237 N N . THR A 280 ? 0.7906 1.1590 0.8814 -0.0533 0.0283 -0.1358 280 THR A N 2238 C CA . THR A 280 ? 0.8333 1.1765 0.9205 -0.0494 0.0272 -0.1266 280 THR A CA 2239 C C . THR A 280 ? 0.8195 1.1706 0.9132 -0.0435 0.0251 -0.1306 280 THR A C 2240 O O . THR A 280 ? 0.8463 1.2202 0.9475 -0.0398 0.0238 -0.1398 280 THR A O 2241 C CB . THR A 280 ? 0.8588 1.1834 0.9490 -0.0387 0.0236 -0.1195 280 THR A CB 2242 O OG1 . THR A 280 ? 0.8844 1.2152 0.9845 -0.0257 0.0191 -0.1235 280 THR A OG1 2243 C CG2 . THR A 280 ? 0.8480 1.1707 0.9346 -0.0413 0.0244 -0.1181 280 THR A CG2 2244 N N . PRO A 281 ? 0.8162 1.1500 0.9070 -0.0421 0.0244 -0.1245 281 PRO A N 2245 C CA . PRO A 281 ? 0.8290 1.1685 0.9253 -0.0367 0.0222 -0.1284 281 PRO A CA 2246 C C . PRO A 281 ? 0.8346 1.1757 0.9409 -0.0235 0.0177 -0.1316 281 PRO A C 2247 O O . PRO A 281 ? 0.8393 1.1859 0.9495 -0.0188 0.0159 -0.1362 281 PRO A O 2248 C CB . PRO A 281 ? 0.8180 1.1379 0.9082 -0.0382 0.0223 -0.1208 281 PRO A CB 2249 C CG . PRO A 281 ? 0.8384 1.1459 0.9160 -0.0466 0.0259 -0.1144 281 PRO A CG 2250 C CD . PRO A 281 ? 0.8286 1.1395 0.9085 -0.0468 0.0263 -0.1150 281 PRO A CD 2251 N N . MET A 282 ? 0.8568 1.1908 0.9650 -0.0174 0.0160 -0.1291 282 MET A N 2252 C CA . MET A 282 ? 0.9248 1.2565 1.0380 -0.0042 0.0123 -0.1322 282 MET A CA 2253 C C . MET A 282 ? 0.8877 1.2348 1.0026 0.0028 0.0106 -0.1383 282 MET A C 2254 O O . MET A 282 ? 0.9302 1.2727 1.0456 0.0157 0.0074 -0.1406 282 MET A O 2255 C CB . MET A 282 ? 1.0119 1.3179 1.1242 0.0001 0.0116 -0.1244 282 MET A CB 2256 C CG . MET A 282 ? 1.1053 1.3986 1.2137 -0.0047 0.0134 -0.1163 282 MET A CG 2257 S SD . MET A 282 ? 1.2473 1.5149 1.3562 -0.0018 0.0135 -0.1087 282 MET A SD 2258 C CE . MET A 282 ? 1.2288 1.4995 1.3394 -0.0078 0.0136 -0.1095 282 MET A CE 2259 N N . GLY A 283 ? 0.8491 1.2145 0.9637 -0.0054 0.0127 -0.1416 283 GLY A N 2260 C CA . GLY A 283 ? 0.8447 1.2306 0.9622 0.0008 0.0106 -0.1492 283 GLY A CA 2261 C C . GLY A 283 ? 0.8581 1.2525 0.9731 -0.0105 0.0136 -0.1490 283 GLY A C 2262 O O . GLY A 283 ? 0.8648 1.2429 0.9736 -0.0217 0.0171 -0.1413 283 GLY A O 2263 N N . ALA A 284 ? 0.8492 1.2694 0.9682 -0.0070 0.0119 -0.1581 284 ALA A N 2264 C CA . ALA A 284 ? 0.8489 1.2821 0.9661 -0.0190 0.0148 -0.1607 284 ALA A CA 2265 C C . ALA A 284 ? 0.8777 1.2992 0.9922 -0.0118 0.0120 -0.1566 284 ALA A C 2266 O O . ALA A 284 ? 0.8494 1.2625 0.9646 0.0050 0.0071 -0.1555 284 ALA A O 2267 C CB . ALA A 284 ? 0.8199 1.2940 0.9440 -0.0216 0.0152 -0.1752 284 ALA A CB 2268 N N . ILE A 285 ? 0.8910 1.3106 1.0004 -0.0248 0.0155 -0.1546 285 ILE A N 2269 C CA . ILE A 285 ? 0.9067 1.3136 1.0121 -0.0203 0.0136 -0.1500 285 ILE A CA 2270 C C . ILE A 285 ? 0.9388 1.3751 1.0465 -0.0254 0.0134 -0.1604 285 ILE A C 2271 O O . ILE A 285 ? 0.9731 1.4231 1.0789 -0.0431 0.0186 -0.1653 285 ILE A O 2272 C CB . ILE A 285 ? 0.9051 1.2797 1.0004 -0.0303 0.0177 -0.1377 285 ILE A CB 2273 C CG1 . ILE A 285 ? 0.8714 1.2197 0.9660 -0.0237 0.0170 -0.1282 285 ILE A CG1 2274 C CG2 . ILE A 285 ? 0.9365 1.3004 1.0270 -0.0274 0.0163 -0.1339 285 ILE A CG2 2275 C CD1 . ILE A 285 ? 0.8924 1.2140 0.9776 -0.0330 0.0210 -0.1175 285 ILE A CD1 2276 N N . ASN A 286 ? 1.0109 1.4555 1.1212 -0.0099 0.0076 -0.1641 286 ASN A N 2277 C CA . ASN A 286 ? 1.0378 1.5107 1.1505 -0.0117 0.0059 -0.1743 286 ASN A CA 2278 C C . ASN A 286 ? 1.0376 1.4887 1.1431 -0.0046 0.0034 -0.1671 286 ASN A C 2279 O O . ASN A 286 ? 0.9916 1.4386 1.0963 0.0149 -0.0025 -0.1667 286 ASN A O 2280 C CB . ASN A 286 ? 1.0899 1.5987 1.2118 0.0038 0.0001 -0.1877 286 ASN A CB 2281 C CG . ASN A 286 ? 1.2256 1.7689 1.3515 0.0052 -0.0030 -0.2000 286 ASN A CG 2282 O OD1 . ASN A 286 ? 1.2192 1.7740 1.3446 -0.0136 0.0015 -0.2038 286 ASN A OD1 2283 N ND2 . ASN A 286 ? 1.4155 1.9750 1.5438 0.0281 -0.0108 -0.2070 286 ASN A ND2 2284 N N . SER A 287 ? 1.0223 1.4565 1.1202 -0.0199 0.0081 -0.1608 287 SER A N 2285 C CA . SER A 287 ? 1.0906 1.5050 1.1812 -0.0145 0.0062 -0.1543 287 SER A CA 2286 C C . SER A 287 ? 1.1302 1.5358 1.2121 -0.0338 0.0118 -0.1520 287 SER A C 2287 O O . SER A 287 ? 1.1221 1.5231 1.1998 -0.0510 0.0181 -0.1508 287 SER A O 2288 C CB . SER A 287 ? 1.1030 1.4791 1.1884 -0.0028 0.0054 -0.1405 287 SER A CB 2289 O OG . SER A 287 ? 1.0860 1.4357 1.1650 -0.0157 0.0110 -0.1301 287 SER A OG 2290 N N . SER A 288 ? 1.1543 1.5548 1.2311 -0.0300 0.0096 -0.1511 288 SER A N 2291 C CA . SER A 288 ? 1.1804 1.5684 1.2465 -0.0466 0.0145 -0.1486 288 SER A CA 2292 C C . SER A 288 ? 1.1198 1.4648 1.1749 -0.0433 0.0161 -0.1330 288 SER A C 2293 O O . SER A 288 ? 1.1266 1.4568 1.1710 -0.0516 0.0187 -0.1297 288 SER A O 2294 C CB . SER A 288 ? 1.2337 1.6464 1.3009 -0.0459 0.0110 -0.1592 288 SER A CB 2295 O OG . SER A 288 ? 1.3117 1.7139 1.3779 -0.0253 0.0046 -0.1548 288 SER A OG 2296 N N . MET A 289 ? 1.0680 1.3938 1.1254 -0.0317 0.0148 -0.1240 289 MET A N 2297 C CA . MET A 289 ? 1.0810 1.3701 1.1299 -0.0280 0.0165 -0.1103 289 MET A CA 2298 C C . MET A 289 ? 1.0537 1.3252 1.0931 -0.0437 0.0229 -0.1045 289 MET A C 2299 O O . MET A 289 ? 1.0910 1.3723 1.1320 -0.0531 0.0256 -0.1082 289 MET A O 2300 C CB . MET A 289 ? 1.1361 1.4120 1.1905 -0.0135 0.0142 -0.1038 289 MET A CB 2301 C CG . MET A 289 ? 1.1857 1.4728 1.2456 0.0041 0.0084 -0.1087 289 MET A CG 2302 S SD . MET A 289 ? 1.1693 1.4377 1.2206 0.0172 0.0058 -0.1032 289 MET A SD 2303 C CE . MET A 289 ? 1.1566 1.4147 1.2094 0.0371 0.0025 -0.1013 289 MET A CE 2304 N N . PRO A 290 ? 1.0652 1.3091 1.0929 -0.0455 0.0253 -0.0953 290 PRO A N 2305 C CA . PRO A 290 ? 1.0506 1.2733 1.0654 -0.0572 0.0310 -0.0890 290 PRO A CA 2306 C C . PRO A 290 ? 1.0087 1.2208 1.0269 -0.0529 0.0315 -0.0826 290 PRO A C 2307 O O . PRO A 290 ? 1.0678 1.2716 1.0770 -0.0627 0.0356 -0.0809 290 PRO A O 2308 C CB . PRO A 290 ? 1.0667 1.2634 1.0693 -0.0549 0.0320 -0.0808 290 PRO A CB 2309 C CG . PRO A 290 ? 1.0719 1.2702 1.0839 -0.0386 0.0271 -0.0789 290 PRO A CG 2310 C CD . PRO A 290 ? 1.0430 1.2728 1.0668 -0.0354 0.0230 -0.0902 290 PRO A CD 2311 N N . PHE A 291 ? 0.9470 1.1580 0.9761 -0.0388 0.0278 -0.0793 291 PHE A N 2312 C CA . PHE A 291 ? 0.9425 1.1445 0.9760 -0.0345 0.0280 -0.0739 291 PHE A CA 2313 C C . PHE A 291 ? 0.8862 1.1058 0.9340 -0.0268 0.0245 -0.0794 291 PHE A C 2314 O O . PHE A 291 ? 0.8951 1.1290 0.9487 -0.0201 0.0212 -0.0853 291 PHE A O 2315 C CB . PHE A 291 ? 1.0022 1.1824 1.0343 -0.0253 0.0278 -0.0644 291 PHE A CB 2316 C CG . PHE A 291 ? 1.0824 1.2420 1.0999 -0.0296 0.0310 -0.0577 291 PHE A CG 2317 C CD1 . PHE A 291 ? 1.1372 1.2844 1.1451 -0.0348 0.0339 -0.0534 291 PHE A CD1 2318 C CD2 . PHE A 291 ? 1.1552 1.3061 1.1668 -0.0268 0.0309 -0.0556 291 PHE A CD2 2319 C CE1 . PHE A 291 ? 1.1483 1.2742 1.1400 -0.0368 0.0367 -0.0471 291 PHE A CE1 2320 C CE2 . PHE A 291 ? 1.1789 1.3092 1.1756 -0.0299 0.0339 -0.0494 291 PHE A CE2 2321 C CZ . PHE A 291 ? 1.1660 1.2833 1.1523 -0.0346 0.0368 -0.0452 291 PHE A CZ 2322 N N . HIS A 292 ? 0.8509 1.0681 0.9025 -0.0267 0.0251 -0.0775 292 HIS A N 2323 C CA . HIS A 292 ? 0.8170 1.0433 0.8803 -0.0181 0.0221 -0.0808 292 HIS A CA 2324 C C . HIS A 292 ? 0.8072 1.0198 0.8726 -0.0160 0.0230 -0.0747 292 HIS A C 2325 O O . HIS A 292 ? 0.8441 1.0450 0.9024 -0.0213 0.0254 -0.0692 292 HIS A O 2326 C CB . HIS A 292 ? 0.8766 1.1273 0.9450 -0.0224 0.0214 -0.0904 292 HIS A CB 2327 C CG . HIS A 292 ? 0.9375 1.1886 1.0020 -0.0329 0.0245 -0.0901 292 HIS A CG 2328 N ND1 . HIS A 292 ? 0.9616 1.2097 1.0304 -0.0305 0.0241 -0.0885 292 HIS A ND1 2329 C CD2 . HIS A 292 ? 0.9804 1.2330 1.0349 -0.0460 0.0285 -0.0914 292 HIS A CD2 2330 C CE1 . HIS A 292 ? 0.9881 1.2362 1.0498 -0.0402 0.0271 -0.0885 292 HIS A CE1 2331 N NE2 . HIS A 292 ? 1.0005 1.2498 1.0524 -0.0499 0.0302 -0.0900 292 HIS A NE2 2332 N N . ASN A 293 ? 0.7872 1.0008 0.8610 -0.0081 0.0210 -0.0761 293 ASN A N 2333 C CA . ASN A 293 ? 0.7950 0.9987 0.8724 -0.0070 0.0219 -0.0721 293 ASN A CA 2334 C C . ASN A 293 ? 0.8167 1.0311 0.9015 -0.0057 0.0203 -0.0777 293 ASN A C 2335 O O . ASN A 293 ? 0.8510 1.0588 0.9406 -0.0027 0.0203 -0.0766 293 ASN A O 2336 C CB . ASN A 293 ? 0.8230 1.0104 0.9011 -0.0001 0.0226 -0.0669 293 ASN A CB 2337 C CG . ASN A 293 ? 0.8171 1.0038 0.8981 0.0087 0.0209 -0.0707 293 ASN A CG 2338 O OD1 . ASN A 293 ? 0.8150 1.0152 0.8976 0.0115 0.0184 -0.0775 293 ASN A OD1 2339 N ND2 . ASN A 293 ? 0.8149 0.9850 0.8950 0.0134 0.0227 -0.0667 293 ASN A ND2 2340 N N . ILE A 294 ? 0.8155 1.0474 0.9012 -0.0088 0.0193 -0.0845 294 ILE A N 2341 C CA . ILE A 294 ? 0.8232 1.0672 0.9152 -0.0067 0.0177 -0.0909 294 ILE A CA 2342 C C . ILE A 294 ? 0.8234 1.0683 0.9156 -0.0131 0.0188 -0.0900 294 ILE A C 2343 O O . ILE A 294 ? 0.9041 1.1462 1.0013 -0.0101 0.0179 -0.0907 294 ILE A O 2344 C CB . ILE A 294 ? 0.8433 1.1092 0.9366 -0.0068 0.0163 -0.0995 294 ILE A CB 2345 C CG1 . ILE A 294 ? 0.8461 1.1118 0.9394 0.0038 0.0138 -0.1015 294 ILE A CG1 2346 C CG2 . ILE A 294 ? 0.8647 1.1451 0.9634 -0.0058 0.0151 -0.1065 294 ILE A CG2 2347 C CD1 . ILE A 294 ? 0.8854 1.1727 0.9784 0.0020 0.0128 -0.1086 294 ILE A CD1 2348 N N . HIS A 295 ? 0.8641 1.1111 0.9488 -0.0219 0.0210 -0.0887 295 HIS A N 2349 C CA . HIS A 295 ? 0.8611 1.1072 0.9425 -0.0268 0.0220 -0.0877 295 HIS A CA 2350 C C . HIS A 295 ? 0.8783 1.1169 0.9451 -0.0354 0.0253 -0.0838 295 HIS A C 2351 O O . HIS A 295 ? 0.8550 1.0978 0.9162 -0.0412 0.0274 -0.0859 295 HIS A O 2352 C CB . HIS A 295 ? 0.9109 1.1743 0.9973 -0.0276 0.0211 -0.0956 295 HIS A CB 2353 C CG . HIS A 295 ? 0.9192 1.1819 1.0031 -0.0304 0.0212 -0.0953 295 HIS A CG 2354 N ND1 . HIS A 295 ? 0.9587 1.2196 1.0303 -0.0384 0.0241 -0.0939 295 HIS A ND1 2355 C CD2 . HIS A 295 ? 0.9617 1.2247 1.0521 -0.0262 0.0190 -0.0967 295 HIS A CD2 2356 C CE1 . HIS A 295 ? 0.9481 1.2086 1.0186 -0.0376 0.0231 -0.0941 295 HIS A CE1 2357 N NE2 . HIS A 295 ? 0.9398 1.2031 1.0228 -0.0306 0.0199 -0.0961 295 HIS A NE2 2358 N N . PRO A 296 ? 0.8602 1.0872 0.9191 -0.0362 0.0260 -0.0788 296 PRO A N 2359 C CA . PRO A 296 ? 0.8698 1.0836 0.9099 -0.0427 0.0295 -0.0744 296 PRO A CA 2360 C C . PRO A 296 ? 0.9167 1.1364 0.9458 -0.0533 0.0332 -0.0789 296 PRO A C 2361 O O . PRO A 296 ? 0.9191 1.1297 0.9333 -0.0613 0.0372 -0.0775 296 PRO A O 2362 C CB . PRO A 296 ? 0.8626 1.0653 0.8973 -0.0377 0.0282 -0.0693 296 PRO A CB 2363 C CG . PRO A 296 ? 0.8860 1.0961 0.9387 -0.0299 0.0246 -0.0705 296 PRO A CG 2364 C CD . PRO A 296 ? 0.8791 1.1042 0.9443 -0.0304 0.0236 -0.0774 296 PRO A CD 2365 N N . LEU A 297 ? 0.9900 1.2233 1.0246 -0.0541 0.0324 -0.0842 297 LEU A N 2366 C CA . LEU A 297 ? 1.0522 1.2922 1.0762 -0.0648 0.0367 -0.0890 297 LEU A CA 2367 C C . LEU A 297 ? 1.0135 1.2752 1.0462 -0.0706 0.0381 -0.0975 297 LEU A C 2368 O O . LEU A 297 ? 1.0403 1.3218 1.0875 -0.0666 0.0356 -0.1042 297 LEU A O 2369 C CB . LEU A 297 ? 1.0717 1.3176 1.0970 -0.0626 0.0354 -0.0914 297 LEU A CB 2370 C CG . LEU A 297 ? 1.1484 1.3783 1.1664 -0.0556 0.0330 -0.0848 297 LEU A CG 2371 C CD1 . LEU A 297 ? 1.1617 1.4021 1.1857 -0.0522 0.0304 -0.0889 297 LEU A CD1 2372 C CD2 . LEU A 297 ? 1.1946 1.4015 1.1860 -0.0602 0.0372 -0.0787 297 LEU A CD2 2373 N N . THR A 298 ? 1.0197 1.2783 1.0429 -0.0796 0.0421 -0.0980 298 THR A N 2374 C CA . THR A 298 ? 1.0325 1.3157 1.0640 -0.0857 0.0434 -0.1075 298 THR A CA 2375 C C . THR A 298 ? 1.0012 1.2874 1.0170 -0.1029 0.0511 -0.1122 298 THR A C 2376 O O . THR A 298 ? 0.9974 1.2602 0.9922 -0.1097 0.0556 -0.1065 298 THR A O 2377 C CB . THR A 298 ? 1.0412 1.3244 1.0776 -0.0825 0.0415 -0.1069 298 THR A CB 2378 O OG1 . THR A 298 ? 1.1456 1.4102 1.1636 -0.0929 0.0465 -0.1028 298 THR A OG1 2379 C CG2 . THR A 298 ? 1.0740 1.3457 1.1197 -0.0677 0.0360 -0.1002 298 THR A CG2 2380 N N . ILE A 299 ? 0.9387 1.2539 0.9635 -0.1096 0.0528 -0.1231 299 ILE A N 2381 C CA . ILE A 299 ? 0.9788 1.3010 0.9904 -0.1284 0.0611 -0.1295 299 ILE A CA 2382 C C . ILE A 299 ? 1.0016 1.3499 1.0233 -0.1339 0.0615 -0.1391 299 ILE A C 2383 O O . ILE A 299 ? 0.9886 1.3622 1.0309 -0.1224 0.0553 -0.1450 299 ILE A O 2384 C CB . ILE A 299 ? 1.0441 1.3821 1.0571 -0.1322 0.0636 -0.1355 299 ILE A CB 2385 C CG1 . ILE A 299 ? 1.0604 1.4095 1.0606 -0.1535 0.0735 -0.1439 299 ILE A CG1 2386 C CG2 . ILE A 299 ? 1.0547 1.4237 1.0928 -0.1191 0.0569 -0.1430 299 ILE A CG2 2387 C CD1 . ILE A 299 ? 1.1083 1.4226 1.0774 -0.1659 0.0816 -0.1369 299 ILE A CD1 2388 N N . GLY A 300 ? 1.0467 1.3873 1.0524 -0.1507 0.0685 -0.1407 300 GLY A N 2389 C CA . GLY A 300 ? 1.0692 1.4360 1.0831 -0.1584 0.0695 -0.1511 300 GLY A CA 2390 C C . GLY A 300 ? 1.1474 1.4942 1.1530 -0.1588 0.0688 -0.1456 300 GLY A C 2391 O O . GLY A 300 ? 1.1298 1.4389 1.1170 -0.1589 0.0706 -0.1342 300 GLY A O 2392 N N . GLU A 301 ? 1.2506 1.6241 1.2693 -0.1583 0.0660 -0.1544 301 GLU A N 2393 C CA . GLU A 301 ? 1.3286 1.6888 1.3425 -0.1573 0.0643 -0.1509 301 GLU A CA 2394 C C . GLU A 301 ? 1.2518 1.6039 1.2784 -0.1336 0.0548 -0.1428 301 GLU A C 2395 O O . GLU A 301 ? 1.2604 1.6381 1.3046 -0.1217 0.0483 -0.1491 301 GLU A O 2396 C CB . GLU A 301 ? 1.4429 1.8396 1.4658 -0.1668 0.0651 -0.1656 301 GLU A CB 2397 C CG . GLU A 301 ? 1.5992 1.9850 1.6163 -0.1674 0.0637 -0.1638 301 GLU A CG 2398 C CD . GLU A 301 ? 1.7325 2.1013 1.7263 -0.1920 0.0737 -0.1657 301 GLU A CD 2399 O OE1 . GLU A 301 ? 1.8412 2.1921 1.8172 -0.2067 0.0821 -0.1637 301 GLU A OE1 2400 O OE2 . GLU A 301 ? 1.7941 2.1659 1.7855 -0.1966 0.0733 -0.1695 301 GLU A OE2 2401 N N . CYS A 302 ? 1.2185 1.5351 1.2349 -0.1267 0.0542 -0.1295 302 CYS A N 2402 C CA . CYS A 302 ? 1.1837 1.4921 1.2118 -0.1062 0.0466 -0.1220 302 CYS A CA 2403 C C . CYS A 302 ? 1.0943 1.3767 1.1150 -0.1002 0.0449 -0.1128 302 CYS A C 2404 O O . CYS A 302 ? 1.0633 1.3229 1.0653 -0.1103 0.0498 -0.1082 302 CYS A O 2405 C CB . CYS A 302 ? 1.2436 1.5384 1.2707 -0.1006 0.0462 -0.1155 302 CYS A CB 2406 S SG . CYS A 302 ? 1.4156 1.7424 1.4564 -0.1009 0.0457 -0.1258 302 CYS A SG 2407 N N . PRO A 303 ? 1.0247 1.3085 1.0580 -0.0835 0.0384 -0.1100 303 PRO A N 2408 C CA . PRO A 303 ? 1.0307 1.2873 1.0576 -0.0759 0.0371 -0.0996 303 PRO A CA 2409 C C . PRO A 303 ? 1.0172 1.2470 1.0349 -0.0742 0.0389 -0.0892 303 PRO A C 2410 O O . PRO A 303 ? 1.1075 1.3404 1.1256 -0.0766 0.0401 -0.0900 303 PRO A O 2411 C CB . PRO A 303 ? 1.0113 1.2767 1.0534 -0.0587 0.0306 -0.1000 303 PRO A CB 2412 C CG . PRO A 303 ? 1.0171 1.3160 1.0716 -0.0573 0.0280 -0.1119 303 PRO A CG 2413 C CD . PRO A 303 ? 1.0037 1.3140 1.0554 -0.0711 0.0326 -0.1172 303 PRO A CD 2414 N N . LYS A 304 ? 1.0143 1.2195 1.0237 -0.0692 0.0389 -0.0801 304 LYS A N 2415 C CA . LYS A 304 ? 1.0534 1.2354 1.0531 -0.0664 0.0402 -0.0712 304 LYS A CA 2416 C C . LYS A 304 ? 1.0095 1.1936 1.0246 -0.0527 0.0358 -0.0678 304 LYS A C 2417 O O . LYS A 304 ? 1.0471 1.2340 1.0724 -0.0439 0.0328 -0.0672 304 LYS A O 2418 C CB . LYS A 304 ? 1.1438 1.2993 1.1257 -0.0673 0.0427 -0.0637 304 LYS A CB 2419 C CG . LYS A 304 ? 1.2946 1.4446 1.2590 -0.0821 0.0477 -0.0675 304 LYS A CG 2420 C CD . LYS A 304 ? 1.3678 1.5109 1.3154 -0.0948 0.0532 -0.0693 304 LYS A CD 2421 C CE . LYS A 304 ? 1.4062 1.5649 1.3497 -0.1118 0.0577 -0.0796 304 LYS A CE 2422 N NZ . LYS A 304 ? 1.4758 1.6237 1.3993 -0.1258 0.0646 -0.0810 304 LYS A NZ 2423 N N . TYR A 305 ? 0.9087 1.0907 0.9243 -0.0513 0.0357 -0.0660 305 TYR A N 2424 C CA . TYR A 305 ? 0.8586 1.0436 0.8885 -0.0407 0.0322 -0.0642 305 TYR A CA 2425 C C . TYR A 305 ? 0.8997 1.0666 0.9263 -0.0336 0.0320 -0.0560 305 TYR A C 2426 O O . TYR A 305 ? 1.0059 1.1572 1.0179 -0.0352 0.0340 -0.0509 305 TYR A O 2427 C CB . TYR A 305 ? 0.8466 1.0376 0.8786 -0.0417 0.0318 -0.0660 305 TYR A CB 2428 C CG . TYR A 305 ? 0.8207 1.0148 0.8670 -0.0323 0.0286 -0.0651 305 TYR A CG 2429 C CD1 . TYR A 305 ? 0.8103 1.0167 0.8710 -0.0274 0.0261 -0.0700 305 TYR A CD1 2430 C CD2 . TYR A 305 ? 0.8165 1.0008 0.8606 -0.0282 0.0281 -0.0601 305 TYR A CD2 2431 C CE1 . TYR A 305 ? 0.8292 1.0351 0.9004 -0.0206 0.0242 -0.0696 305 TYR A CE1 2432 C CE2 . TYR A 305 ? 0.8214 1.0102 0.8790 -0.0219 0.0258 -0.0606 305 TYR A CE2 2433 C CZ . TYR A 305 ? 0.8203 1.0184 0.8908 -0.0191 0.0243 -0.0652 305 TYR A CZ 2434 O OH . TYR A 305 ? 0.8505 1.0497 0.9319 -0.0145 0.0230 -0.0661 305 TYR A OH 2435 N N . VAL A 306 ? 0.9365 1.1046 0.9751 -0.0254 0.0299 -0.0550 306 VAL A N 2436 C CA . VAL A 306 ? 0.8746 1.0303 0.9143 -0.0185 0.0300 -0.0484 306 VAL A CA 2437 C C . VAL A 306 ? 0.8521 1.0153 0.9074 -0.0129 0.0282 -0.0504 306 VAL A C 2438 O O . VAL A 306 ? 0.9391 1.1130 1.0025 -0.0124 0.0267 -0.0558 306 VAL A O 2439 C CB . VAL A 306 ? 0.8528 0.9974 0.8880 -0.0155 0.0310 -0.0445 306 VAL A CB 2440 C CG1 . VAL A 306 ? 0.8769 1.0114 0.8947 -0.0219 0.0332 -0.0428 306 VAL A CG1 2441 C CG2 . VAL A 306 ? 0.8476 1.0000 0.8913 -0.0122 0.0294 -0.0484 306 VAL A CG2 2442 N N . LYS A 307 ? 0.8925 1.0499 0.9508 -0.0089 0.0287 -0.0465 307 LYS A N 2443 C CA . LYS A 307 ? 0.9277 1.0903 0.9993 -0.0057 0.0281 -0.0487 307 LYS A CA 2444 C C . LYS A 307 ? 0.9480 1.1032 1.0242 -0.0015 0.0297 -0.0473 307 LYS A C 2445 O O . LYS A 307 ? 1.1099 1.2652 1.1944 -0.0001 0.0306 -0.0486 307 LYS A O 2446 C CB . LYS A 307 ? 0.9846 1.1490 1.0583 -0.0044 0.0281 -0.0471 307 LYS A CB 2447 C CG . LYS A 307 ? 1.0725 1.2467 1.1461 -0.0070 0.0261 -0.0508 307 LYS A CG 2448 C CD . LYS A 307 ? 1.1638 1.3386 1.2334 -0.0041 0.0253 -0.0485 307 LYS A CD 2449 C CE . LYS A 307 ? 1.2255 1.4068 1.3082 -0.0010 0.0255 -0.0497 307 LYS A CE 2450 N NZ . LYS A 307 ? 1.2870 1.4745 1.3671 0.0032 0.0238 -0.0493 307 LYS A NZ 2451 N N . SER A 308 ? 0.9597 1.1075 1.0291 0.0000 0.0302 -0.0451 308 SER A N 2452 C CA . SER A 308 ? 0.9650 1.1028 1.0353 0.0049 0.0320 -0.0431 308 SER A CA 2453 C C . SER A 308 ? 0.9402 1.0797 1.0145 0.0081 0.0309 -0.0480 308 SER A C 2454 O O . SER A 308 ? 0.9625 1.1130 1.0384 0.0073 0.0281 -0.0532 308 SER A O 2455 C CB . SER A 308 ? 0.9446 1.0740 1.0050 0.0065 0.0324 -0.0397 308 SER A CB 2456 O OG . SER A 308 ? 0.9891 1.1160 1.0414 0.0032 0.0328 -0.0364 308 SER A OG 2457 N N . ASN A 309 ? 0.9909 1.1182 1.0649 0.0121 0.0334 -0.0464 309 ASN A N 2458 C CA . ASN A 309 ? 1.0370 1.1589 1.1087 0.0178 0.0327 -0.0501 309 ASN A CA 2459 C C . ASN A 309 ? 0.9716 1.0867 1.0338 0.0245 0.0315 -0.0490 309 ASN A C 2460 O O . ASN A 309 ? 0.9605 1.0736 1.0184 0.0316 0.0296 -0.0528 309 ASN A O 2461 C CB . ASN A 309 ? 1.1427 1.2511 1.2156 0.0178 0.0370 -0.0495 309 ASN A CB 2462 C CG . ASN A 309 ? 1.2773 1.3949 1.3600 0.0117 0.0373 -0.0531 309 ASN A CG 2463 O OD1 . ASN A 309 ? 1.2892 1.4174 1.3751 0.0116 0.0340 -0.0581 309 ASN A OD1 2464 N ND2 . ASN A 309 ? 1.3319 1.4475 1.4198 0.0069 0.0413 -0.0512 309 ASN A ND2 2465 N N . ARG A 310 ? 0.9341 1.0460 0.9921 0.0233 0.0324 -0.0443 310 ARG A N 2466 C CA . ARG A 310 ? 0.9131 1.0168 0.9615 0.0295 0.0318 -0.0426 310 ARG A CA 2467 C C . ARG A 310 ? 0.8892 0.9942 0.9334 0.0256 0.0318 -0.0390 310 ARG A C 2468 O O . ARG A 310 ? 0.8608 0.9602 0.9056 0.0219 0.0348 -0.0341 310 ARG A O 2469 C CB . ARG A 310 ? 0.9531 1.0359 0.9958 0.0344 0.0362 -0.0385 310 ARG A CB 2470 C CG . ARG A 310 ? 1.0456 1.1174 1.0761 0.0436 0.0352 -0.0377 310 ARG A CG 2471 C CD . ARG A 310 ? 1.1371 1.1850 1.1591 0.0469 0.0409 -0.0325 310 ARG A CD 2472 N NE . ARG A 310 ? 1.2019 1.2396 1.2112 0.0548 0.0401 -0.0301 310 ARG A NE 2473 C CZ . ARG A 310 ? 1.2682 1.3030 1.2675 0.0656 0.0362 -0.0335 310 ARG A CZ 2474 N NH1 . ARG A 310 ? 1.2632 1.3037 1.2630 0.0703 0.0330 -0.0394 310 ARG A NH1 2475 N NH2 . ARG A 310 ? 1.3054 1.3320 1.2931 0.0728 0.0353 -0.0314 310 ARG A NH2 2476 N N . LEU A 311 ? 0.8360 0.9490 0.8755 0.0266 0.0286 -0.0422 311 LEU A N 2477 C CA . LEU A 311 ? 0.8290 0.9394 0.8609 0.0232 0.0289 -0.0394 311 LEU A CA 2478 C C . LEU A 311 ? 0.8347 0.9469 0.8596 0.0291 0.0260 -0.0425 311 LEU A C 2479 O O . LEU A 311 ? 0.8338 0.9633 0.8603 0.0287 0.0223 -0.0498 311 LEU A O 2480 C CB . LEU A 311 ? 0.8157 0.9372 0.8478 0.0133 0.0284 -0.0417 311 LEU A CB 2481 C CG . LEU A 311 ? 0.7940 0.9134 0.8291 0.0081 0.0306 -0.0384 311 LEU A CG 2482 C CD1 . LEU A 311 ? 0.7765 0.9049 0.8077 -0.0010 0.0301 -0.0416 311 LEU A CD1 2483 C CD2 . LEU A 311 ? 0.8103 0.9140 0.8403 0.0098 0.0338 -0.0309 311 LEU A CD2 2484 N N . VAL A 312 ? 0.8292 0.9253 0.8463 0.0346 0.0278 -0.0374 312 VAL A N 2485 C CA . VAL A 312 ? 0.8313 0.9269 0.8403 0.0425 0.0249 -0.0398 312 VAL A CA 2486 C C . VAL A 312 ? 0.8193 0.9037 0.8190 0.0410 0.0267 -0.0350 312 VAL A C 2487 O O . VAL A 312 ? 0.8231 0.8906 0.8198 0.0418 0.0310 -0.0278 312 VAL A O 2488 C CB . VAL A 312 ? 0.8462 0.9280 0.8508 0.0542 0.0255 -0.0385 312 VAL A CB 2489 C CG1 . VAL A 312 ? 0.8567 0.9365 0.8501 0.0648 0.0220 -0.0408 312 VAL A CG1 2490 C CG2 . VAL A 312 ? 0.8411 0.9310 0.8528 0.0562 0.0240 -0.0434 312 VAL A CG2 2491 N N . LEU A 313 ? 0.8223 0.9177 0.8175 0.0383 0.0235 -0.0399 313 LEU A N 2492 C CA . LEU A 313 ? 0.8459 0.9313 0.8305 0.0368 0.0246 -0.0367 313 LEU A CA 2493 C C . LEU A 313 ? 0.8410 0.9195 0.8172 0.0485 0.0225 -0.0368 313 LEU A C 2494 O O . LEU A 313 ? 0.8446 0.9356 0.8214 0.0559 0.0179 -0.0434 313 LEU A O 2495 C CB . LEU A 313 ? 0.8559 0.9557 0.8380 0.0260 0.0229 -0.0430 313 LEU A CB 2496 C CG . LEU A 313 ? 0.8754 0.9721 0.8571 0.0136 0.0264 -0.0407 313 LEU A CG 2497 C CD1 . LEU A 313 ? 0.8754 0.9848 0.8521 0.0017 0.0257 -0.0481 313 LEU A CD1 2498 C CD2 . LEU A 313 ? 0.8903 0.9635 0.8634 0.0145 0.0307 -0.0312 313 LEU A CD2 2499 N N . ALA A 314 ? 0.8387 0.8975 0.8056 0.0512 0.0258 -0.0297 314 ALA A N 2500 C CA . ALA A 314 ? 0.8280 0.8788 0.7838 0.0615 0.0240 -0.0295 314 ALA A CA 2501 C C . ALA A 314 ? 0.8560 0.9217 0.8076 0.0572 0.0197 -0.0366 314 ALA A C 2502 O O . ALA A 314 ? 0.8697 0.9370 0.8204 0.0455 0.0213 -0.0366 314 ALA A O 2503 C CB . ALA A 314 ? 0.8365 0.8631 0.7836 0.0641 0.0294 -0.0203 314 ALA A CB 2504 N N . THR A 315 ? 0.8693 0.9459 0.8171 0.0666 0.0143 -0.0431 315 THR A N 2505 C CA . THR A 315 ? 0.9099 1.0001 0.8521 0.0640 0.0102 -0.0503 315 THR A CA 2506 C C . THR A 315 ? 0.8799 0.9554 0.8081 0.0765 0.0089 -0.0475 315 THR A C 2507 O O . THR A 315 ? 0.8842 0.9541 0.8037 0.0727 0.0093 -0.0469 315 THR A O 2508 C CB . THR A 315 ? 0.9211 1.0438 0.8712 0.0648 0.0038 -0.0631 315 THR A CB 2509 O OG1 . THR A 315 ? 0.9917 1.1154 0.9430 0.0803 0.0008 -0.0640 315 THR A OG1 2510 C CG2 . THR A 315 ? 0.9229 1.0617 0.8844 0.0489 0.0057 -0.0671 315 THR A CG2 2511 N N . GLY A 316 ? 0.8561 0.9231 0.7800 0.0918 0.0076 -0.0457 316 GLY A N 2512 C CA . GLY A 316 ? 0.8682 0.9183 0.7762 0.1053 0.0068 -0.0425 316 GLY A CA 2513 C C . GLY A 316 ? 0.8586 0.8777 0.7591 0.1045 0.0145 -0.0304 316 GLY A C 2514 O O . GLY A 316 ? 0.8400 0.8535 0.7475 0.0929 0.0198 -0.0253 316 GLY A O 2515 N N . LEU A 317 ? 0.9453 0.9446 0.8306 0.1177 0.0153 -0.0262 317 LEU A N 2516 C CA . LEU A 317 ? 0.9814 0.9528 0.8584 0.1174 0.0232 -0.0156 317 LEU A CA 2517 C C . LEU A 317 ? 0.9463 0.8969 0.8183 0.1250 0.0283 -0.0100 317 LEU A C 2518 O O . LEU A 317 ? 0.9158 0.8705 0.7877 0.1323 0.0253 -0.0140 317 LEU A O 2519 C CB . LEU A 317 ? 1.0001 0.9616 0.8610 0.1236 0.0219 -0.0145 317 LEU A CB 2520 C CG . LEU A 317 ? 1.0151 0.9816 0.8627 0.1389 0.0145 -0.0208 317 LEU A CG 2521 C CD1 . LEU A 317 ? 1.1172 1.0594 0.9500 0.1540 0.0172 -0.0157 317 LEU A CD1 2522 C CD2 . LEU A 317 ? 1.0198 0.9833 0.8556 0.1401 0.0127 -0.0213 317 LEU A CD2 2523 N N . ARG A 318 ? 0.9706 0.8990 0.8381 0.1223 0.0367 -0.0012 318 ARG A N 2524 C CA . ARG A 318 ? 0.9983 0.9047 0.8600 0.1258 0.0439 0.0042 318 ARG A CA 2525 C C . ARG A 318 ? 0.9649 0.8552 0.8058 0.1424 0.0415 0.0032 318 ARG A C 2526 O O . ARG A 318 ? 0.9520 0.8322 0.7770 0.1511 0.0403 0.0046 318 ARG A O 2527 C CB . ARG A 318 ? 1.0479 0.9365 0.9072 0.1199 0.0535 0.0127 318 ARG A CB 2528 C CG . ARG A 318 ? 1.1176 0.9823 0.9694 0.1211 0.0627 0.0179 318 ARG A CG 2529 C CD . ARG A 318 ? 1.1242 0.9757 0.9736 0.1156 0.0721 0.0249 318 ARG A CD 2530 N NE . ARG A 318 ? 1.1598 1.0293 1.0295 0.1033 0.0736 0.0251 318 ARG A NE 2531 C CZ . ARG A 318 ? 1.1962 1.0702 1.0794 0.0944 0.0791 0.0255 318 ARG A CZ 2532 N NH1 . ARG A 318 ? 1.2050 1.0655 1.0839 0.0944 0.0844 0.0257 318 ARG A NH1 2533 N NH2 . ARG A 318 ? 1.1862 1.0774 1.0855 0.0858 0.0792 0.0253 318 ARG A NH2 2534 N N . ASN A 319 ? 1.0464 0.9331 0.8857 0.1475 0.0410 0.0008 319 ASN A N 2535 C CA . ASN A 319 ? 1.1057 0.9753 0.9226 0.1654 0.0383 -0.0007 319 ASN A CA 2536 C C . ASN A 319 ? 1.2511 1.0816 1.0479 0.1684 0.0489 0.0077 319 ASN A C 2537 O O . ASN A 319 ? 1.2853 1.1054 1.0889 0.1573 0.0577 0.0117 319 ASN A O 2538 C CB . ASN A 319 ? 1.0561 0.9378 0.8784 0.1701 0.0331 -0.0075 319 ASN A CB 2539 C CG . ASN A 319 ? 1.0518 0.9298 0.8538 0.1914 0.0254 -0.0128 319 ASN A CG 2540 O OD1 . ASN A 319 ? 1.0274 0.8960 0.8117 0.2030 0.0230 -0.0120 319 ASN A OD1 2541 N ND2 . ASN A 319 ? 1.0572 0.9437 0.8610 0.1980 0.0211 -0.0188 319 ASN A ND2 2542 N N . SER A 320 ? 1.4645 1.2740 1.2359 0.1829 0.0484 0.0099 320 SER A N 2543 C CA . SER A 320 ? 1.6427 1.4128 1.3913 0.1853 0.0595 0.0181 320 SER A CA 2544 C C . SER A 320 ? 1.7619 1.5032 1.4860 0.1984 0.0613 0.0179 320 SER A C 2545 O O . SER A 320 ? 1.7340 1.4830 1.4497 0.2139 0.0515 0.0117 320 SER A O 2546 C CB . SER A 320 ? 1.6453 1.4050 1.3769 0.1937 0.0589 0.0213 320 SER A CB 2547 O OG . SER A 320 ? 1.5397 1.3209 1.2694 0.2061 0.0461 0.0141 320 SER A OG 2548 N N . PRO A 321 ? 1.9239 1.6322 1.6356 0.1918 0.0741 0.0241 321 PRO A N 2549 C CA . PRO A 321 ? 1.9694 1.6400 1.6493 0.2048 0.0777 0.0251 321 PRO A CA 2550 C C . PRO A 321 ? 1.9513 1.5941 1.5956 0.2249 0.0762 0.0278 321 PRO A C 2551 O O . PRO A 321 ? 2.0111 1.6299 1.6270 0.2429 0.0736 0.0264 321 PRO A O 2552 C CB . PRO A 321 ? 1.9804 1.6245 1.6577 0.1879 0.0936 0.0308 321 PRO A CB 2553 C CG . PRO A 321 ? 1.9682 1.6470 1.6836 0.1673 0.0949 0.0299 321 PRO A CG 2554 C CD . PRO A 321 ? 1.9460 1.6546 1.6753 0.1707 0.0854 0.0285 321 PRO A CD 2555 N N . GLY B 1 ? 0.8937 1.1308 1.0168 0.0065 -0.0371 0.0798 1 GLY B N 2556 C CA . GLY B 1 ? 0.8484 1.0674 0.9736 0.0341 -0.0283 0.0636 1 GLY B CA 2557 C C . GLY B 1 ? 0.7991 1.0620 0.9182 0.0684 -0.0202 0.0666 1 GLY B C 2558 O O . GLY B 1 ? 0.7890 1.1026 0.9069 0.0752 -0.0201 0.0799 1 GLY B O 2559 N N . LEU B 2 ? 0.7355 0.9755 0.8447 0.0921 -0.0138 0.0545 2 LEU B N 2560 C CA . LEU B 2 ? 0.7275 0.9960 0.8165 0.1308 -0.0070 0.0566 2 LEU B CA 2561 C C . LEU B 2 ? 0.7269 0.9817 0.8013 0.1529 -0.0063 0.0513 2 LEU B C 2562 O O . LEU B 2 ? 0.7176 1.0148 0.7744 0.1837 -0.0025 0.0592 2 LEU B O 2563 C CB . LEU B 2 ? 0.7284 0.9548 0.7979 0.1501 -0.0023 0.0438 2 LEU B CB 2564 C CG . LEU B 2 ? 0.6825 0.9335 0.7609 0.1385 -0.0014 0.0503 2 LEU B CG 2565 C CD1 . LEU B 2 ? 0.6913 0.8882 0.7469 0.1565 0.0029 0.0364 2 LEU B CD1 2566 C CD2 . LEU B 2 ? 0.6617 1.0049 0.7404 0.1500 0.0006 0.0714 2 LEU B CD2 2567 N N . PHE B 3 ? 0.7198 0.9207 0.7993 0.1395 -0.0100 0.0384 3 PHE B N 2568 C CA . PHE B 3 ? 0.7530 0.9303 0.8136 0.1596 -0.0101 0.0302 3 PHE B CA 2569 C C . PHE B 3 ? 0.7808 0.9923 0.8557 0.1509 -0.0135 0.0404 3 PHE B C 2570 O O . PHE B 3 ? 0.8597 1.0616 0.9198 0.1683 -0.0137 0.0357 3 PHE B O 2571 C CB . PHE B 3 ? 0.7481 0.8526 0.7985 0.1533 -0.0121 0.0106 3 PHE B CB 2572 C CG . PHE B 3 ? 0.7636 0.8318 0.7874 0.1658 -0.0090 0.0025 3 PHE B CG 2573 C CD1 . PHE B 3 ? 0.7570 0.8212 0.7967 0.1485 -0.0079 0.0020 3 PHE B CD1 2574 C CD2 . PHE B 3 ? 0.7879 0.8244 0.7635 0.1977 -0.0077 -0.0033 3 PHE B CD2 2575 C CE1 . PHE B 3 ? 0.7594 0.7919 0.7727 0.1602 -0.0050 -0.0036 3 PHE B CE1 2576 C CE2 . PHE B 3 ? 0.8378 0.8332 0.7794 0.2105 -0.0058 -0.0093 3 PHE B CE2 2577 C CZ . PHE B 3 ? 0.7957 0.7919 0.7587 0.1908 -0.0041 -0.0089 3 PHE B CZ 2578 N N . GLY B 4 ? 0.7924 1.0406 0.8902 0.1227 -0.0171 0.0552 4 GLY B N 2579 C CA . GLY B 4 ? 0.7635 1.0528 0.8695 0.1109 -0.0210 0.0705 4 GLY B CA 2580 C C . GLY B 4 ? 0.7664 1.0133 0.8788 0.0951 -0.0268 0.0638 4 GLY B C 2581 O O . GLY B 4 ? 0.8364 1.1093 0.9518 0.0831 -0.0309 0.0770 4 GLY B O 2582 N N . ALA B 5 ? 0.7568 0.9443 0.8695 0.0951 -0.0274 0.0451 5 ALA B N 2583 C CA . ALA B 5 ? 0.7530 0.9095 0.8698 0.0878 -0.0323 0.0385 5 ALA B CA 2584 C C . ALA B 5 ? 0.7557 0.8896 0.8777 0.0622 -0.0388 0.0426 5 ALA B C 2585 O O . ALA B 5 ? 0.7872 0.9246 0.9051 0.0498 -0.0446 0.0538 5 ALA B O 2586 C CB . ALA B 5 ? 0.7619 0.8780 0.8736 0.0994 -0.0308 0.0186 5 ALA B CB 2587 N N . ILE B 6 ? 0.7538 0.8587 0.8779 0.0559 -0.0384 0.0337 6 ILE B N 2588 C CA . ILE B 6 ? 0.7874 0.8581 0.9057 0.0384 -0.0451 0.0344 6 ILE B CA 2589 C C . ILE B 6 ? 0.7971 0.8817 0.9042 0.0131 -0.0515 0.0535 6 ILE B C 2590 O O . ILE B 6 ? 0.7937 0.9102 0.9046 0.0061 -0.0491 0.0609 6 ILE B O 2591 C CB . ILE B 6 ? 0.7855 0.8280 0.9067 0.0407 -0.0426 0.0205 6 ILE B CB 2592 C CG1 . ILE B 6 ? 0.7940 0.8254 0.9221 0.0563 -0.0395 0.0050 6 ILE B CG1 2593 C CG2 . ILE B 6 ? 0.8062 0.8113 0.9115 0.0266 -0.0499 0.0224 6 ILE B CG2 2594 C CD1 . ILE B 6 ? 0.8170 0.8345 0.9496 0.0578 -0.0360 -0.0071 6 ILE B CD1 2595 N N . ALA B 7 ? 0.8278 0.8877 0.9167 -0.0019 -0.0606 0.0622 7 ALA B N 2596 C CA . ALA B 7 ? 0.8624 0.9297 0.9310 -0.0350 -0.0700 0.0834 7 ALA B CA 2597 C C . ALA B 7 ? 0.8841 1.0320 0.9676 -0.0391 -0.0657 0.1000 7 ALA B C 2598 O O . ALA B 7 ? 0.8763 1.0605 0.9556 -0.0636 -0.0691 0.1157 7 ALA B O 2599 C CB . ALA B 7 ? 0.8706 0.9028 0.9211 -0.0558 -0.0761 0.0832 7 ALA B CB 2600 N N . GLY B 8 ? 0.8769 1.0560 0.9751 -0.0128 -0.0584 0.0963 8 GLY B N 2601 C CA . GLY B 8 ? 0.8630 1.1199 0.9701 -0.0048 -0.0533 0.1107 8 GLY B CA 2602 C C . GLY B 8 ? 0.8855 1.1508 0.9899 0.0028 -0.0546 0.1154 8 GLY B C 2603 O O . GLY B 8 ? 0.9875 1.2382 1.0770 -0.0234 -0.0639 0.1285 8 GLY B O 2604 N N . PHE B 9 ? 0.8492 1.1295 0.9613 0.0376 -0.0466 0.1044 9 PHE B N 2605 C CA . PHE B 9 ? 0.8377 1.1268 0.9468 0.0473 -0.0476 0.1074 9 PHE B CA 2606 C C . PHE B 9 ? 0.8577 1.0791 0.9627 0.0453 -0.0527 0.0938 9 PHE B C 2607 O O . PHE B 9 ? 0.8914 1.1110 0.9908 0.0460 -0.0561 0.0985 9 PHE B O 2608 C CB . PHE B 9 ? 0.8572 1.1828 0.9662 0.0856 -0.0390 0.1013 9 PHE B CB 2609 C CG . PHE B 9 ? 0.8676 1.1438 0.9730 0.1104 -0.0347 0.0759 9 PHE B CG 2610 C CD1 . PHE B 9 ? 0.9123 1.1443 1.0165 0.1151 -0.0373 0.0612 9 PHE B CD1 2611 C CD2 . PHE B 9 ? 0.9096 1.1866 1.0083 0.1277 -0.0289 0.0684 9 PHE B CD2 2612 C CE1 . PHE B 9 ? 0.9364 1.1280 1.0336 0.1295 -0.0353 0.0405 9 PHE B CE1 2613 C CE2 . PHE B 9 ? 0.9318 1.1570 1.0189 0.1439 -0.0270 0.0471 9 PHE B CE2 2614 C CZ . PHE B 9 ? 0.9303 1.1144 1.0169 0.1416 -0.0307 0.0336 9 PHE B CZ 2615 N N . ILE B 10 ? 0.8435 1.0157 0.9501 0.0454 -0.0529 0.0778 10 ILE B N 2616 C CA . ILE B 10 ? 0.8721 0.9884 0.9700 0.0426 -0.0587 0.0691 10 ILE B CA 2617 C C . ILE B 10 ? 0.9437 1.0258 1.0225 0.0157 -0.0668 0.0782 10 ILE B C 2618 O O . ILE B 10 ? 0.9604 1.0276 1.0412 0.0116 -0.0654 0.0715 10 ILE B O 2619 C CB . ILE B 10 ? 0.8483 0.9398 0.9564 0.0622 -0.0541 0.0464 10 ILE B CB 2620 C CG1 . ILE B 10 ? 0.8232 0.9391 0.9390 0.0827 -0.0485 0.0378 10 ILE B CG1 2621 C CG2 . ILE B 10 ? 0.8470 0.8993 0.9459 0.0667 -0.0595 0.0396 10 ILE B CG2 2622 C CD1 . ILE B 10 ? 0.8170 0.9129 0.9375 0.0924 -0.0456 0.0184 10 ILE B CD1 2623 N N . GLU B 11 ? 1.0473 1.1124 1.1016 -0.0043 -0.0763 0.0941 11 GLU B N 2624 C CA . GLU B 11 ? 1.1296 1.1534 1.1502 -0.0372 -0.0877 0.1066 11 GLU B CA 2625 C C . GLU B 11 ? 1.0918 1.0477 1.0946 -0.0306 -0.0908 0.0911 11 GLU B C 2626 O O . GLU B 11 ? 1.1252 1.0615 1.1127 -0.0515 -0.0954 0.0945 11 GLU B O 2627 C CB . GLU B 11 ? 1.3064 1.3001 1.2906 -0.0568 -0.0994 0.1236 11 GLU B CB 2628 C CG . GLU B 11 ? 1.4289 1.4727 1.4044 -0.0952 -0.1051 0.1516 11 GLU B CG 2629 C CD . GLU B 11 ? 1.6093 1.6035 1.5360 -0.1222 -0.1197 0.1693 11 GLU B CD 2630 O OE1 . GLU B 11 ? 1.6451 1.6144 1.5660 -0.0989 -0.1193 0.1634 11 GLU B OE1 2631 O OE2 . GLU B 11 ? 1.7470 1.7245 1.6366 -0.1687 -0.1327 0.1899 11 GLU B OE2 2632 N N . GLY B 12 ? 1.0570 0.9823 1.0596 -0.0009 -0.0886 0.0749 12 GLY B N 2633 C CA . GLY B 12 ? 1.0792 0.9450 1.0589 0.0118 -0.0918 0.0616 12 GLY B CA 2634 C C . GLY B 12 ? 1.0322 0.9079 1.0335 0.0481 -0.0840 0.0424 12 GLY B C 2635 O O . GLY B 12 ? 0.9849 0.8999 1.0113 0.0615 -0.0786 0.0393 12 GLY B O 2636 N N . GLY B 13 ? 1.0447 0.8886 1.0339 0.0627 -0.0840 0.0303 13 GLY B N 2637 C CA . GLY B 13 ? 1.0533 0.9162 1.0600 0.0944 -0.0776 0.0145 13 GLY B CA 2638 C C . GLY B 13 ? 1.0652 0.9000 1.0415 0.1206 -0.0832 0.0135 13 GLY B C 2639 O O . GLY B 13 ? 1.0971 0.8824 1.0316 0.1146 -0.0929 0.0246 13 GLY B O 2640 N N . TRP B 14 ? 1.0196 0.8885 1.0137 0.1488 -0.0775 0.0014 14 TRP B N 2641 C CA . TRP B 14 ? 1.0008 0.8654 0.9740 0.1805 -0.0807 -0.0003 14 TRP B CA 2642 C C . TRP B 14 ? 1.0687 0.9163 1.0151 0.2144 -0.0811 -0.0094 14 TRP B C 2643 O O . TRP B 14 ? 1.0110 0.9126 0.9884 0.2243 -0.0735 -0.0189 14 TRP B O 2644 C CB . TRP B 14 ? 0.9212 0.8585 0.9377 0.1861 -0.0742 -0.0049 14 TRP B CB 2645 C CG . TRP B 14 ? 0.8949 0.8466 0.9276 0.1644 -0.0744 0.0035 14 TRP B CG 2646 C CD1 . TRP B 14 ? 0.8992 0.8139 0.9082 0.1483 -0.0806 0.0173 14 TRP B CD1 2647 C CD2 . TRP B 14 ? 0.8526 0.8602 0.9227 0.1570 -0.0690 -0.0004 14 TRP B CD2 2648 N NE1 . TRP B 14 ? 0.8850 0.8385 0.9193 0.1357 -0.0777 0.0221 14 TRP B NE1 2649 C CE2 . TRP B 14 ? 0.8448 0.8488 0.9132 0.1427 -0.0710 0.0103 14 TRP B CE2 2650 C CE3 . TRP B 14 ? 0.8238 0.8815 0.9223 0.1586 -0.0640 -0.0112 14 TRP B CE3 2651 C CZ2 . TRP B 14 ? 0.8377 0.8813 0.9291 0.1370 -0.0675 0.0087 14 TRP B CZ2 2652 C CZ3 . TRP B 14 ? 0.7991 0.8869 0.9159 0.1471 -0.0623 -0.0126 14 TRP B CZ3 2653 C CH2 . TRP B 14 ? 0.8126 0.8907 0.9245 0.1398 -0.0637 -0.0037 14 TRP B CH2 2654 N N . GLN B 15 ? 1.1764 0.9470 1.0586 0.2330 -0.0909 -0.0056 15 GLN B N 2655 C CA . GLN B 15 ? 1.2616 1.0123 1.1045 0.2791 -0.0921 -0.0139 15 GLN B CA 2656 C C . GLN B 15 ? 1.2292 1.0616 1.1008 0.3135 -0.0855 -0.0192 15 GLN B C 2657 O O . GLN B 15 ? 1.2581 1.1329 1.1332 0.3454 -0.0805 -0.0272 15 GLN B O 2658 C CB . GLN B 15 ? 1.3894 1.0299 1.1433 0.2975 -0.1060 -0.0081 15 GLN B CB 2659 C CG . GLN B 15 ? 1.4727 1.0256 1.1836 0.2607 -0.1160 -0.0016 15 GLN B CG 2660 C CD . GLN B 15 ? 1.5369 1.0624 1.2253 0.2737 -0.1157 -0.0116 15 GLN B CD 2661 O OE1 . GLN B 15 ? 1.6242 1.1114 1.2592 0.3220 -0.1186 -0.0192 15 GLN B OE1 2662 N NE2 . GLN B 15 ? 1.5397 1.0856 1.2651 0.2339 -0.1121 -0.0112 15 GLN B NE2 2663 N N . GLY B 16 ? 1.2064 1.0671 1.0981 0.3056 -0.0858 -0.0134 16 GLY B N 2664 C CA . GLY B 16 ? 1.2175 1.1544 1.1313 0.3343 -0.0818 -0.0163 16 GLY B CA 2665 C C . GLY B 16 ? 1.1726 1.2110 1.1487 0.3227 -0.0722 -0.0235 16 GLY B C 2666 O O . GLY B 16 ? 1.1592 1.2691 1.1464 0.3502 -0.0694 -0.0263 16 GLY B O 2667 N N . MET B 17 ? 1.1524 1.1992 1.1646 0.2813 -0.0682 -0.0252 17 MET B N 2668 C CA . MET B 17 ? 1.1241 1.2510 1.1843 0.2639 -0.0612 -0.0311 17 MET B CA 2669 C C . MET B 17 ? 1.1443 1.2820 1.2018 0.2744 -0.0572 -0.0366 17 MET B C 2670 O O . MET B 17 ? 1.1819 1.2731 1.2335 0.2579 -0.0565 -0.0377 17 MET B O 2671 C CB . MET B 17 ? 1.0988 1.2248 1.1900 0.2199 -0.0592 -0.0305 17 MET B CB 2672 C CG . MET B 17 ? 1.0940 1.2875 1.2208 0.1989 -0.0547 -0.0359 17 MET B CG 2673 S SD . MET B 17 ? 1.0673 1.2507 1.2131 0.1588 -0.0544 -0.0359 17 MET B SD 2674 C CE . MET B 17 ? 1.1024 1.2198 1.2375 0.1480 -0.0525 -0.0333 17 MET B CE 2675 N N . VAL B 18 ? 1.1479 1.3562 1.2102 0.3022 -0.0545 -0.0389 18 VAL B N 2676 C CA . VAL B 18 ? 1.1518 1.3801 1.2048 0.3240 -0.0506 -0.0430 18 VAL B CA 2677 C C . VAL B 18 ? 1.0908 1.4120 1.1892 0.2980 -0.0445 -0.0445 18 VAL B C 2678 O O . VAL B 18 ? 1.0953 1.4287 1.1949 0.2998 -0.0405 -0.0471 18 VAL B O 2679 C CB . VAL B 18 ? 1.2080 1.4504 1.2198 0.3858 -0.0524 -0.0427 18 VAL B CB 2680 C CG1 . VAL B 18 ? 1.2999 1.5357 1.2849 0.4169 -0.0496 -0.0472 18 VAL B CG1 2681 C CG2 . VAL B 18 ? 1.2606 1.4099 1.2210 0.4075 -0.0606 -0.0394 18 VAL B CG2 2682 N N . ASP B 19 ? 1.0735 1.4546 1.2037 0.2707 -0.0450 -0.0421 19 ASP B N 2683 C CA . ASP B 19 ? 1.0115 1.4834 1.1746 0.2420 -0.0422 -0.0412 19 ASP B CA 2684 C C . ASP B 19 ? 0.9425 1.3842 1.1240 0.1878 -0.0419 -0.0432 19 ASP B C 2685 O O . ASP B 19 ? 0.9187 1.4174 1.1185 0.1535 -0.0426 -0.0415 19 ASP B O 2686 C CB . ASP B 19 ? 1.0215 1.5841 1.1986 0.2432 -0.0452 -0.0366 19 ASP B CB 2687 C CG . ASP B 19 ? 1.0672 1.5952 1.2477 0.2209 -0.0506 -0.0364 19 ASP B CG 2688 O OD1 . ASP B 19 ? 1.1196 1.5604 1.2832 0.2282 -0.0519 -0.0377 19 ASP B OD1 2689 O OD2 . ASP B 19 ? 1.0899 1.6815 1.2872 0.1944 -0.0542 -0.0339 19 ASP B OD2 2690 N N . GLY B 20 ? 0.8913 1.2441 1.0621 0.1799 -0.0417 -0.0457 20 GLY B N 2691 C CA . GLY B 20 ? 0.8685 1.1897 1.0495 0.1385 -0.0409 -0.0474 20 GLY B CA 2692 C C . GLY B 20 ? 0.8639 1.1011 1.0320 0.1382 -0.0402 -0.0481 20 GLY B C 2693 O O . GLY B 20 ? 0.8957 1.0928 1.0448 0.1628 -0.0422 -0.0464 20 GLY B O 2694 N N . TRP B 21 ? 0.8399 1.0506 1.0130 0.1094 -0.0386 -0.0494 21 TRP B N 2695 C CA . TRP B 21 ? 0.8534 1.0003 1.0170 0.1063 -0.0378 -0.0481 21 TRP B CA 2696 C C . TRP B 21 ? 0.7852 0.9056 0.9451 0.0996 -0.0406 -0.0447 21 TRP B C 2697 O O . TRP B 21 ? 0.7240 0.8065 0.8738 0.1043 -0.0418 -0.0399 21 TRP B O 2698 C CB . TRP B 21 ? 0.8629 0.9975 1.0302 0.0855 -0.0339 -0.0502 21 TRP B CB 2699 C CG . TRP B 21 ? 0.8909 1.0205 1.0549 0.0962 -0.0309 -0.0517 21 TRP B CG 2700 C CD1 . TRP B 21 ? 0.9379 1.0417 1.0854 0.1204 -0.0324 -0.0512 21 TRP B CD1 2701 C CD2 . TRP B 21 ? 0.9049 1.0466 1.0744 0.0826 -0.0268 -0.0539 21 TRP B CD2 2702 N NE1 . TRP B 21 ? 0.9265 1.0280 1.0698 0.1248 -0.0293 -0.0540 21 TRP B NE1 2703 C CE2 . TRP B 21 ? 0.9303 1.0600 1.0909 0.1018 -0.0252 -0.0552 21 TRP B CE2 2704 C CE3 . TRP B 21 ? 0.9237 1.0784 1.0979 0.0554 -0.0255 -0.0545 21 TRP B CE3 2705 C CZ2 . TRP B 21 ? 0.9664 1.1063 1.1298 0.0958 -0.0209 -0.0571 21 TRP B CZ2 2706 C CZ3 . TRP B 21 ? 1.0073 1.1695 1.1827 0.0471 -0.0216 -0.0553 21 TRP B CZ3 2707 C CH2 . TRP B 21 ? 1.0115 1.1713 1.1853 0.0679 -0.0187 -0.0566 21 TRP B CH2 2708 N N . TYR B 22 ? 0.7462 0.8881 0.9105 0.0865 -0.0425 -0.0463 22 TYR B N 2709 C CA . TYR B 22 ? 0.7232 0.8469 0.8814 0.0846 -0.0450 -0.0437 22 TYR B CA 2710 C C . TYR B 22 ? 0.7021 0.8617 0.8628 0.0854 -0.0493 -0.0450 22 TYR B C 2711 O O . TYR B 22 ? 0.6886 0.8905 0.8554 0.0772 -0.0505 -0.0478 22 TYR B O 2712 C CB . TYR B 22 ? 0.7553 0.8540 0.9041 0.0675 -0.0439 -0.0457 22 TYR B CB 2713 C CG . TYR B 22 ? 0.7597 0.8416 0.9073 0.0592 -0.0398 -0.0471 22 TYR B CG 2714 C CD1 . TYR B 22 ? 0.7436 0.8050 0.8926 0.0668 -0.0369 -0.0427 22 TYR B CD1 2715 C CD2 . TYR B 22 ? 0.7482 0.8344 0.8896 0.0403 -0.0400 -0.0518 22 TYR B CD2 2716 C CE1 . TYR B 22 ? 0.7494 0.7981 0.8974 0.0601 -0.0332 -0.0439 22 TYR B CE1 2717 C CE2 . TYR B 22 ? 0.7588 0.8283 0.8972 0.0336 -0.0362 -0.0526 22 TYR B CE2 2718 C CZ . TYR B 22 ? 0.7638 0.8163 0.9075 0.0457 -0.0323 -0.0491 22 TYR B CZ 2719 O OH . TYR B 22 ? 0.7704 0.8091 0.9115 0.0400 -0.0286 -0.0498 22 TYR B OH 2720 N N . GLY B 23 ? 0.6865 0.8357 0.8419 0.0929 -0.0518 -0.0417 23 GLY B N 2721 C CA . GLY B 23 ? 0.7014 0.8841 0.8577 0.0943 -0.0564 -0.0426 23 GLY B CA 2722 C C . GLY B 23 ? 0.7122 0.8800 0.8620 0.1061 -0.0585 -0.0376 23 GLY B C 2723 O O . GLY B 23 ? 0.7222 0.8573 0.8658 0.1072 -0.0567 -0.0331 23 GLY B O 2724 N N . TYR B 24 ? 0.7480 0.9484 0.8996 0.1145 -0.0624 -0.0372 24 TYR B N 2725 C CA . TYR B 24 ? 0.7598 0.9533 0.9045 0.1234 -0.0652 -0.0328 24 TYR B CA 2726 C C . TYR B 24 ? 0.7614 0.9630 0.9036 0.1485 -0.0667 -0.0266 24 TYR B C 2727 O O . TYR B 24 ? 0.7570 0.9859 0.9017 0.1623 -0.0669 -0.0280 24 TYR B O 2728 C CB . TYR B 24 ? 0.7859 1.0050 0.9267 0.1105 -0.0702 -0.0381 24 TYR B CB 2729 C CG . TYR B 24 ? 0.8365 1.0414 0.9661 0.0843 -0.0716 -0.0456 24 TYR B CG 2730 C CD1 . TYR B 24 ? 0.8492 1.0816 0.9835 0.0656 -0.0731 -0.0494 24 TYR B CD1 2731 C CD2 . TYR B 24 ? 0.8848 1.0477 0.9927 0.0795 -0.0720 -0.0478 24 TYR B CD2 2732 C CE1 . TYR B 24 ? 0.8925 1.1012 1.0070 0.0375 -0.0761 -0.0549 24 TYR B CE1 2733 C CE2 . TYR B 24 ? 0.9210 1.0554 1.0048 0.0587 -0.0748 -0.0548 24 TYR B CE2 2734 C CZ . TYR B 24 ? 0.9271 1.0794 1.0127 0.0351 -0.0774 -0.0582 24 TYR B CZ 2735 O OH . TYR B 24 ? 0.9898 1.1039 1.0428 0.0104 -0.0818 -0.0639 24 TYR B OH 2736 N N . HIS B 25 ? 0.7927 0.9701 0.9247 0.1563 -0.0682 -0.0188 25 HIS B N 2737 C CA . HIS B 25 ? 0.8139 0.9920 0.9339 0.1790 -0.0717 -0.0122 25 HIS B CA 2738 C C . HIS B 25 ? 0.8097 1.0040 0.9296 0.1780 -0.0745 -0.0100 25 HIS B C 2739 O O . HIS B 25 ? 0.7803 0.9611 0.8995 0.1656 -0.0734 -0.0079 25 HIS B O 2740 C CB . HIS B 25 ? 0.8270 0.9514 0.9251 0.1848 -0.0728 -0.0021 25 HIS B CB 2741 C CG . HIS B 25 ? 0.8733 0.9806 0.9456 0.2084 -0.0780 0.0054 25 HIS B CG 2742 N ND1 . HIS B 25 ? 0.8974 0.9888 0.9567 0.2065 -0.0814 0.0160 25 HIS B ND1 2743 C CD2 . HIS B 25 ? 0.9104 1.0137 0.9622 0.2379 -0.0805 0.0044 25 HIS B CD2 2744 C CE1 . HIS B 25 ? 0.9414 1.0116 0.9711 0.2309 -0.0865 0.0213 25 HIS B CE1 2745 N NE2 . HIS B 25 ? 0.9468 1.0222 0.9693 0.2533 -0.0860 0.0139 25 HIS B NE2 2746 N N . HIS B 26 ? 0.8597 1.0872 0.9783 0.1941 -0.0780 -0.0101 26 HIS B N 2747 C CA . HIS B 26 ? 0.8743 1.1176 0.9908 0.1946 -0.0812 -0.0080 26 HIS B CA 2748 C C . HIS B 26 ? 0.8948 1.1276 0.9938 0.2196 -0.0842 0.0021 26 HIS B C 2749 O O . HIS B 26 ? 0.8947 1.1181 0.9802 0.2411 -0.0851 0.0044 26 HIS B O 2750 C CB . HIS B 26 ? 0.8727 1.1693 1.0000 0.1852 -0.0844 -0.0171 26 HIS B CB 2751 C CG . HIS B 26 ? 0.9064 1.2542 1.0378 0.2041 -0.0866 -0.0171 26 HIS B CG 2752 N ND1 . HIS B 26 ? 0.9667 1.3360 1.1043 0.2106 -0.0842 -0.0193 26 HIS B ND1 2753 C CD2 . HIS B 26 ? 0.9514 1.3400 1.0801 0.2220 -0.0906 -0.0142 26 HIS B CD2 2754 C CE1 . HIS B 26 ? 0.9562 1.3821 1.0940 0.2342 -0.0864 -0.0175 26 HIS B CE1 2755 N NE2 . HIS B 26 ? 0.9798 1.4182 1.1126 0.2412 -0.0904 -0.0144 26 HIS B NE2 2756 N N . SER B 27 ? 0.9138 1.1435 1.0069 0.2188 -0.0862 0.0082 27 SER B N 2757 C CA . SER B 27 ? 0.9496 1.1675 1.0220 0.2396 -0.0900 0.0189 27 SER B CA 2758 C C . SER B 27 ? 0.9343 1.1874 1.0121 0.2400 -0.0924 0.0184 27 SER B C 2759 O O . SER B 27 ? 0.8976 1.1499 0.9803 0.2243 -0.0910 0.0183 27 SER B O 2760 C CB . SER B 27 ? 1.0047 1.1669 1.0554 0.2323 -0.0907 0.0331 27 SER B CB 2761 O OG . SER B 27 ? 1.1139 1.2307 1.1361 0.2462 -0.0936 0.0380 27 SER B OG 2762 N N . ASN B 28 ? 0.9097 1.1954 0.9832 0.2613 -0.0960 0.0182 28 ASN B N 2763 C CA . ASN B 28 ? 0.8844 1.2041 0.9601 0.2631 -0.0993 0.0181 28 ASN B CA 2764 C C . ASN B 28 ? 0.9305 1.2666 0.9900 0.2950 -0.1032 0.0248 28 ASN B C 2765 O O . ASN B 28 ? 0.9505 1.2586 0.9894 0.3176 -0.1035 0.0303 28 ASN B O 2766 C CB . ASN B 28 ? 0.8329 1.1988 0.9269 0.2432 -0.1009 0.0043 28 ASN B CB 2767 C CG . ASN B 28 ? 0.8143 1.2320 0.9193 0.2480 -0.1026 -0.0019 28 ASN B CG 2768 O OD1 . ASN B 28 ? 0.8507 1.2844 0.9492 0.2770 -0.1028 0.0034 28 ASN B OD1 2769 N ND2 . ASN B 28 ? 0.7873 1.2325 0.9038 0.2203 -0.1045 -0.0121 28 ASN B ND2 2770 N N . GLU B 29 ? 0.9824 1.3589 1.0447 0.2996 -0.1067 0.0242 29 GLU B N 2771 C CA . GLU B 29 ? 1.0452 1.4368 1.0889 0.3327 -0.1104 0.0320 29 GLU B CA 2772 C C . GLU B 29 ? 1.0577 1.4910 1.1006 0.3596 -0.1110 0.0285 29 GLU B C 2773 O O . GLU B 29 ? 1.0937 1.5107 1.1071 0.3971 -0.1127 0.0364 29 GLU B O 2774 C CB . GLU B 29 ? 1.1310 1.5664 1.1806 0.3302 -0.1143 0.0310 29 GLU B CB 2775 C CG . GLU B 29 ? 1.2084 1.6091 1.2518 0.3149 -0.1134 0.0371 29 GLU B CG 2776 C CD . GLU B 29 ? 1.2825 1.7185 1.3221 0.3223 -0.1177 0.0387 29 GLU B CD 2777 O OE1 . GLU B 29 ? 1.2433 1.7067 1.2732 0.3486 -0.1212 0.0432 29 GLU B OE1 2778 O OE2 . GLU B 29 ? 1.3688 1.8048 1.4114 0.3050 -0.1177 0.0354 29 GLU B OE2 2779 N N . GLN B 30 ? 1.0178 1.5042 1.0874 0.3417 -0.1101 0.0177 30 GLN B N 2780 C CA . GLN B 30 ? 1.0006 1.5467 1.0739 0.3652 -0.1099 0.0156 30 GLN B CA 2781 C C . GLN B 30 ? 1.0003 1.4964 1.0551 0.3860 -0.1058 0.0174 30 GLN B C 2782 O O . GLN B 30 ? 1.0216 1.5522 1.0640 0.4231 -0.1054 0.0187 30 GLN B O 2783 C CB . GLN B 30 ? 0.9871 1.6087 1.0919 0.3311 -0.1114 0.0059 30 GLN B CB 2784 C CG . GLN B 30 ? 1.0131 1.6909 1.1275 0.3106 -0.1182 0.0032 30 GLN B CG 2785 C CD . GLN B 30 ? 1.0587 1.7443 1.1864 0.2583 -0.1216 -0.0068 30 GLN B CD 2786 O OE1 . GLN B 30 ? 1.1312 1.7488 1.2529 0.2367 -0.1203 -0.0110 30 GLN B OE1 2787 N NE2 . GLN B 30 ? 1.0617 1.8304 1.2022 0.2378 -0.1266 -0.0096 30 GLN B NE2 2788 N N . GLY B 31 ? 0.9929 1.4123 1.0428 0.3645 -0.1031 0.0178 31 GLY B N 2789 C CA . GLY B 31 ? 1.0126 1.3738 1.0386 0.3805 -0.1009 0.0196 31 GLY B CA 2790 C C . GLY B 31 ? 0.9418 1.2688 0.9854 0.3437 -0.0970 0.0146 31 GLY B C 2791 O O . GLY B 31 ? 0.9224 1.2502 0.9873 0.3095 -0.0961 0.0120 31 GLY B O 2792 N N . SER B 32 ? 0.9417 1.2380 0.9718 0.3544 -0.0948 0.0130 32 SER B N 2793 C CA . SER B 32 ? 0.9367 1.1979 0.9802 0.3223 -0.0912 0.0092 32 SER B CA 2794 C C . SER B 32 ? 0.9386 1.2162 0.9852 0.3324 -0.0879 0.0027 32 SER B C 2795 O O . SER B 32 ? 1.0076 1.3101 1.0361 0.3712 -0.0885 0.0028 32 SER B O 2796 C CB . SER B 32 ? 0.9746 1.1456 0.9867 0.3147 -0.0935 0.0190 32 SER B CB 2797 O OG . SER B 32 ? 1.0283 1.1437 0.9931 0.3461 -0.0971 0.0235 32 SER B OG 2798 N N . GLY B 33 ? 0.9133 1.1794 0.9803 0.3008 -0.0842 -0.0024 33 GLY B N 2799 C CA . GLY B 33 ? 0.8994 1.1765 0.9699 0.3061 -0.0806 -0.0080 33 GLY B CA 2800 C C . GLY B 33 ? 0.8710 1.1441 0.9680 0.2666 -0.0766 -0.0137 33 GLY B C 2801 O O . GLY B 33 ? 0.8547 1.1096 0.9630 0.2378 -0.0766 -0.0135 33 GLY B O 2802 N N . TYR B 34 ? 0.8921 1.1836 0.9948 0.2695 -0.0732 -0.0185 34 TYR B N 2803 C CA . TYR B 34 ? 0.8389 1.1204 0.9604 0.2364 -0.0694 -0.0235 34 TYR B CA 2804 C C . TYR B 34 ? 0.7946 1.1529 0.9426 0.2173 -0.0682 -0.0289 34 TYR B C 2805 O O . TYR B 34 ? 0.7640 1.1914 0.9162 0.2352 -0.0690 -0.0281 34 TYR B O 2806 C CB . TYR B 34 ? 0.8500 1.0841 0.9531 0.2490 -0.0672 -0.0238 34 TYR B CB 2807 C CG . TYR B 34 ? 0.8898 1.0412 0.9557 0.2616 -0.0711 -0.0169 34 TYR B CG 2808 C CD1 . TYR B 34 ? 0.9536 1.0791 0.9794 0.3014 -0.0754 -0.0132 34 TYR B CD1 2809 C CD2 . TYR B 34 ? 0.8707 0.9699 0.9352 0.2334 -0.0715 -0.0127 34 TYR B CD2 2810 C CE1 . TYR B 34 ? 0.9872 1.0251 0.9673 0.3066 -0.0816 -0.0055 34 TYR B CE1 2811 C CE2 . TYR B 34 ? 0.9203 0.9485 0.9470 0.2362 -0.0770 -0.0037 34 TYR B CE2 2812 C CZ . TYR B 34 ? 0.9654 0.9574 0.9476 0.2700 -0.0828 -0.0001 34 TYR B CZ 2813 O OH . TYR B 34 ? 1.0445 0.9546 0.9781 0.2671 -0.0908 0.0100 34 TYR B OH 2814 N N . ALA B 35 ? 0.7878 1.1342 0.9485 0.1803 -0.0671 -0.0330 35 ALA B N 2815 C CA . ALA B 35 ? 0.7862 1.1889 0.9623 0.1526 -0.0677 -0.0368 35 ALA B CA 2816 C C . ALA B 35 ? 0.8178 1.1777 0.9948 0.1270 -0.0644 -0.0405 35 ALA B C 2817 O O . ALA B 35 ? 0.8202 1.1251 0.9899 0.1127 -0.0644 -0.0418 35 ALA B O 2818 C CB . ALA B 35 ? 0.7677 1.1985 0.9455 0.1280 -0.0740 -0.0380 35 ALA B CB 2819 N N . ALA B 36 ? 0.8505 1.2403 1.0347 0.1247 -0.0612 -0.0413 36 ALA B N 2820 C CA . ALA B 36 ? 0.8381 1.1932 1.0222 0.1008 -0.0581 -0.0443 36 ALA B CA 2821 C C . ALA B 36 ? 0.8631 1.2179 1.0417 0.0591 -0.0630 -0.0471 36 ALA B C 2822 O O . ALA B 36 ? 0.9027 1.3114 1.0824 0.0421 -0.0688 -0.0460 36 ALA B O 2823 C CB . ALA B 36 ? 0.8302 1.2265 1.0221 0.1092 -0.0540 -0.0438 36 ALA B CB 2824 N N . ASP B 37 ? 0.9073 1.1988 1.0734 0.0433 -0.0618 -0.0501 37 ASP B N 2825 C CA . ASP B 37 ? 0.9413 1.2126 1.0867 0.0060 -0.0673 -0.0535 37 ASP B CA 2826 C C . ASP B 37 ? 0.9882 1.2808 1.1358 -0.0160 -0.0659 -0.0527 37 ASP B C 2827 O O . ASP B 37 ? 1.0101 1.2698 1.1592 -0.0096 -0.0598 -0.0535 37 ASP B O 2828 C CB . ASP B 37 ? 0.9438 1.1375 1.0671 0.0078 -0.0663 -0.0565 37 ASP B CB 2829 C CG . ASP B 37 ? 0.9720 1.1264 1.0571 -0.0237 -0.0737 -0.0610 37 ASP B CG 2830 O OD1 . ASP B 37 ? 1.0019 1.1498 1.0666 -0.0321 -0.0813 -0.0633 37 ASP B OD1 2831 O OD2 . ASP B 37 ? 1.0118 1.1347 1.0808 -0.0394 -0.0729 -0.0624 37 ASP B OD2 2832 N N . LYS B 38 ? 1.0396 1.3932 1.1870 -0.0440 -0.0720 -0.0499 38 LYS B N 2833 C CA . LYS B 38 ? 1.0922 1.4864 1.2446 -0.0663 -0.0709 -0.0462 38 LYS B CA 2834 C C . LYS B 38 ? 1.1058 1.4301 1.2277 -0.0982 -0.0730 -0.0487 38 LYS B C 2835 O O . LYS B 38 ? 1.0658 1.3925 1.1939 -0.1007 -0.0677 -0.0470 38 LYS B O 2836 C CB . LYS B 38 ? 1.1934 1.6833 1.3513 -0.0942 -0.0783 -0.0394 38 LYS B CB 2837 C CG . LYS B 38 ? 1.2470 1.8219 1.4337 -0.0564 -0.0751 -0.0355 38 LYS B CG 2838 C CD . LYS B 38 ? 1.2989 1.9925 1.4954 -0.0824 -0.0808 -0.0259 38 LYS B CD 2839 C CE . LYS B 38 ? 1.3487 2.0502 1.5235 -0.1283 -0.0946 -0.0244 38 LYS B CE 2840 N NZ . LYS B 38 ? 1.3801 2.2002 1.5599 -0.1689 -0.1022 -0.0124 38 LYS B NZ 2841 N N . GLU B 39 ? 1.1497 1.4081 1.2329 -0.1190 -0.0811 -0.0528 39 GLU B N 2842 C CA . GLU B 39 ? 1.2363 1.4169 1.2766 -0.1449 -0.0847 -0.0553 39 GLU B CA 2843 C C . GLU B 39 ? 1.1796 1.3126 1.2282 -0.1142 -0.0737 -0.0578 39 GLU B C 2844 O O . GLU B 39 ? 1.1912 1.3198 1.2383 -0.1257 -0.0705 -0.0558 39 GLU B O 2845 C CB . GLU B 39 ? 1.3828 1.4868 1.3677 -0.1609 -0.0956 -0.0607 39 GLU B CB 2846 C CG . GLU B 39 ? 1.5250 1.5288 1.4553 -0.1700 -0.0979 -0.0646 39 GLU B CG 2847 C CD . GLU B 39 ? 1.6721 1.5934 1.5277 -0.1932 -0.1124 -0.0698 39 GLU B CD 2848 O OE1 . GLU B 39 ? 1.6876 1.6039 1.5363 -0.1795 -0.1162 -0.0737 39 GLU B OE1 2849 O OE2 . GLU B 39 ? 1.7989 1.6528 1.5957 -0.2245 -0.1207 -0.0701 39 GLU B OE2 2850 N N . SER B 40 ? 1.0886 1.1907 1.1444 -0.0782 -0.0687 -0.0609 40 SER B N 2851 C CA . SER B 40 ? 1.0280 1.0894 1.0880 -0.0529 -0.0600 -0.0616 40 SER B CA 2852 C C . SER B 40 ? 0.9345 1.0403 1.0333 -0.0395 -0.0518 -0.0584 40 SER B C 2853 O O . SER B 40 ? 0.9331 1.0140 1.0307 -0.0356 -0.0466 -0.0583 40 SER B O 2854 C CB . SER B 40 ? 0.9993 1.0338 1.0590 -0.0220 -0.0574 -0.0624 40 SER B CB 2855 O OG . SER B 40 ? 0.9988 1.0788 1.0862 -0.0080 -0.0575 -0.0603 40 SER B OG 2856 N N . THR B 41 ? 0.8803 1.0497 1.0078 -0.0298 -0.0512 -0.0560 41 THR B N 2857 C CA . THR B 41 ? 0.8273 1.0360 0.9809 -0.0125 -0.0447 -0.0539 41 THR B CA 2858 C C . THR B 41 ? 0.8072 1.0390 0.9585 -0.0375 -0.0439 -0.0521 41 THR B C 2859 O O . THR B 41 ? 0.7897 1.0100 0.9469 -0.0284 -0.0380 -0.0523 41 THR B O 2860 C CB . THR B 41 ? 0.7902 1.0631 0.9639 0.0086 -0.0450 -0.0516 41 THR B CB 2861 O OG1 . THR B 41 ? 0.7955 1.0409 0.9694 0.0338 -0.0453 -0.0520 41 THR B OG1 2862 C CG2 . THR B 41 ? 0.7765 1.0857 0.9647 0.0308 -0.0392 -0.0502 41 THR B CG2 2863 N N . GLN B 42 ? 0.8367 1.1024 0.9769 -0.0723 -0.0508 -0.0493 42 GLN B N 2864 C CA . GLN B 42 ? 0.8827 1.1749 1.0164 -0.1043 -0.0516 -0.0449 42 GLN B CA 2865 C C . GLN B 42 ? 0.9018 1.1130 1.0063 -0.1180 -0.0508 -0.0472 42 GLN B C 2866 O O . GLN B 42 ? 0.8651 1.0863 0.9741 -0.1235 -0.0463 -0.0447 42 GLN B O 2867 C CB . GLN B 42 ? 0.9427 1.2837 1.0619 -0.1488 -0.0622 -0.0391 42 GLN B CB 2868 C CG . GLN B 42 ? 0.9898 1.3820 1.1055 -0.1865 -0.0639 -0.0305 42 GLN B CG 2869 C CD . GLN B 42 ? 0.9739 1.4464 1.1289 -0.1555 -0.0533 -0.0270 42 GLN B CD 2870 O OE1 . GLN B 42 ? 0.9529 1.4160 1.1083 -0.1569 -0.0479 -0.0257 42 GLN B OE1 2871 N NE2 . GLN B 42 ? 0.9734 1.5209 1.1560 -0.1233 -0.0507 -0.0257 42 GLN B NE2 2872 N N . LYS B 43 ? 0.9562 1.0900 1.0278 -0.1196 -0.0551 -0.0517 43 LYS B N 2873 C CA . LYS B 43 ? 1.0107 1.0649 1.0501 -0.1195 -0.0534 -0.0542 43 LYS B CA 2874 C C . LYS B 43 ? 0.9354 0.9906 1.0038 -0.0866 -0.0425 -0.0548 43 LYS B C 2875 O O . LYS B 43 ? 0.9802 1.0126 1.0387 -0.0919 -0.0392 -0.0538 43 LYS B O 2876 C CB . LYS B 43 ? 1.1206 1.1007 1.1202 -0.1107 -0.0583 -0.0590 43 LYS B CB 2877 C CG . LYS B 43 ? 1.2871 1.2221 1.2286 -0.1493 -0.0716 -0.0597 43 LYS B CG 2878 C CD . LYS B 43 ? 1.4176 1.2937 1.3221 -0.1329 -0.0769 -0.0655 43 LYS B CD 2879 C CE . LYS B 43 ? 1.5323 1.3355 1.3592 -0.1698 -0.0921 -0.0676 43 LYS B CE 2880 N NZ . LYS B 43 ? 1.6066 1.3317 1.3791 -0.1798 -0.0940 -0.0675 43 LYS B NZ 2881 N N . ALA B 44 ? 0.8427 0.9202 0.9414 -0.0550 -0.0381 -0.0558 44 ALA B N 2882 C CA . ALA B 44 ? 0.8250 0.9000 0.9445 -0.0288 -0.0303 -0.0557 44 ALA B CA 2883 C C . ALA B 44 ? 0.7908 0.9092 0.9279 -0.0320 -0.0263 -0.0541 44 ALA B C 2884 O O . ALA B 44 ? 0.8356 0.9353 0.9717 -0.0286 -0.0217 -0.0541 44 ALA B O 2885 C CB . ALA B 44 ? 0.7995 0.8845 0.9379 -0.0010 -0.0293 -0.0555 44 ALA B CB 2886 N N . ILE B 45 ? 0.7560 0.9384 0.9078 -0.0364 -0.0280 -0.0520 45 ILE B N 2887 C CA . ILE B 45 ? 0.7715 1.0090 0.9385 -0.0341 -0.0238 -0.0495 45 ILE B CA 2888 C C . ILE B 45 ? 0.8065 1.0324 0.9585 -0.0648 -0.0233 -0.0467 45 ILE B C 2889 O O . ILE B 45 ? 0.7952 1.0251 0.9538 -0.0556 -0.0176 -0.0466 45 ILE B O 2890 C CB . ILE B 45 ? 0.7920 1.1153 0.9737 -0.0343 -0.0261 -0.0456 45 ILE B CB 2891 C CG1 . ILE B 45 ? 0.8002 1.1353 0.9940 0.0082 -0.0246 -0.0482 45 ILE B CG1 2892 C CG2 . ILE B 45 ? 0.7686 1.1623 0.9602 -0.0413 -0.0226 -0.0403 45 ILE B CG2 2893 C CD1 . ILE B 45 ? 0.8173 1.2315 1.0212 0.0128 -0.0279 -0.0444 45 ILE B CD1 2894 N N . ASP B 46 ? 0.8398 1.0443 0.9649 -0.1020 -0.0305 -0.0442 46 ASP B N 2895 C CA . ASP B 46 ? 0.8758 1.0590 0.9752 -0.1359 -0.0322 -0.0401 46 ASP B CA 2896 C C . ASP B 46 ? 0.8434 0.9538 0.9284 -0.1203 -0.0273 -0.0439 46 ASP B C 2897 O O . ASP B 46 ? 0.8291 0.9418 0.9135 -0.1255 -0.0231 -0.0415 46 ASP B O 2898 C CB . ASP B 46 ? 0.9942 1.1485 1.0518 -0.1804 -0.0440 -0.0370 46 ASP B CB 2899 C CG . ASP B 46 ? 1.0813 1.3216 1.1526 -0.2042 -0.0501 -0.0308 46 ASP B CG 2900 O OD1 . ASP B 46 ? 1.1213 1.4529 1.2304 -0.1912 -0.0442 -0.0264 46 ASP B OD1 2901 O OD2 . ASP B 46 ? 1.1552 1.3743 1.1964 -0.2334 -0.0610 -0.0300 46 ASP B OD2 2902 N N . GLY B 47 ? 0.8358 0.8902 0.9100 -0.0996 -0.0276 -0.0488 47 GLY B N 2903 C CA . GLY B 47 ? 0.8567 0.8554 0.9183 -0.0813 -0.0230 -0.0508 47 GLY B CA 2904 C C . GLY B 47 ? 0.8558 0.8832 0.9489 -0.0606 -0.0150 -0.0509 47 GLY B C 2905 O O . GLY B 47 ? 0.8950 0.9061 0.9795 -0.0642 -0.0116 -0.0496 47 GLY B O 2906 N N . VAL B 48 ? 0.8329 0.8975 0.9560 -0.0388 -0.0130 -0.0525 48 VAL B N 2907 C CA . VAL B 48 ? 0.8179 0.8955 0.9594 -0.0172 -0.0077 -0.0536 48 VAL B CA 2908 C C . VAL B 48 ? 0.7837 0.9033 0.9321 -0.0254 -0.0044 -0.0520 48 VAL B C 2909 O O . VAL B 48 ? 0.7867 0.8978 0.9364 -0.0170 -0.0002 -0.0527 48 VAL B O 2910 C CB . VAL B 48 ? 0.8327 0.9258 0.9897 0.0081 -0.0087 -0.0555 48 VAL B CB 2911 C CG1 . VAL B 48 ? 0.8510 0.9480 1.0133 0.0288 -0.0058 -0.0573 48 VAL B CG1 2912 C CG2 . VAL B 48 ? 0.8679 0.9223 1.0186 0.0153 -0.0112 -0.0550 48 VAL B CG2 2913 N N . THR B 49 ? 0.7628 0.9339 0.9149 -0.0432 -0.0066 -0.0486 49 THR B N 2914 C CA . THR B 49 ? 0.7965 1.0228 0.9551 -0.0538 -0.0035 -0.0443 49 THR B CA 2915 C C . THR B 49 ? 0.8214 1.0103 0.9589 -0.0796 -0.0028 -0.0412 49 THR B C 2916 O O . THR B 49 ? 0.8435 1.0395 0.9853 -0.0718 0.0025 -0.0409 49 THR B O 2917 C CB . THR B 49 ? 0.8255 1.1255 0.9898 -0.0756 -0.0075 -0.0380 49 THR B CB 2918 O OG1 . THR B 49 ? 0.7946 1.1268 0.9748 -0.0480 -0.0083 -0.0408 49 THR B OG1 2919 C CG2 . THR B 49 ? 0.8088 1.1853 0.9825 -0.0847 -0.0037 -0.0310 49 THR B CG2 2920 N N . ASN B 50 ? 0.8684 1.0108 0.9763 -0.1082 -0.0088 -0.0390 50 ASN B N 2921 C CA . ASN B 50 ? 0.9570 1.0469 1.0319 -0.1295 -0.0095 -0.0360 50 ASN B CA 2922 C C . ASN B 50 ? 0.9224 0.9725 1.0006 -0.1004 -0.0030 -0.0403 50 ASN B C 2923 O O . ASN B 50 ? 0.9052 0.9487 0.9756 -0.1061 0.0004 -0.0376 50 ASN B O 2924 C CB . ASN B 50 ? 1.0301 1.0516 1.0582 -0.1535 -0.0184 -0.0353 50 ASN B CB 2925 C CG . ASN B 50 ? 1.1010 1.1556 1.1149 -0.1950 -0.0275 -0.0292 50 ASN B CG 2926 O OD1 . ASN B 50 ? 1.1351 1.2770 1.1784 -0.2062 -0.0262 -0.0237 50 ASN B OD1 2927 N ND2 . ASN B 50 ? 1.1845 1.1717 1.1487 -0.2173 -0.0375 -0.0295 50 ASN B ND2 2928 N N . LYS B 51 ? 0.9296 0.9580 1.0183 -0.0719 -0.0019 -0.0455 51 LYS B N 2929 C CA . LYS B 51 ? 0.9389 0.9393 1.0304 -0.0488 0.0027 -0.0476 51 LYS B CA 2930 C C . LYS B 51 ? 0.9070 0.9445 1.0199 -0.0393 0.0078 -0.0482 51 LYS B C 2931 O O . LYS B 51 ? 0.9383 0.9599 1.0435 -0.0386 0.0112 -0.0472 51 LYS B O 2932 C CB . LYS B 51 ? 0.9379 0.9256 1.0396 -0.0255 0.0017 -0.0503 51 LYS B CB 2933 C CG . LYS B 51 ? 0.9381 0.9146 1.0465 -0.0069 0.0050 -0.0503 51 LYS B CG 2934 C CD . LYS B 51 ? 0.9886 0.9590 1.1039 0.0084 0.0027 -0.0497 51 LYS B CD 2935 C CE . LYS B 51 ? 0.9946 0.9372 1.0887 0.0111 0.0011 -0.0473 51 LYS B CE 2936 N NZ . LYS B 51 ? 1.0144 0.9616 1.1156 0.0259 0.0003 -0.0435 51 LYS B NZ 2937 N N . VAL B 52 ? 0.8916 0.9763 1.0264 -0.0280 0.0082 -0.0503 52 VAL B N 2938 C CA . VAL B 52 ? 0.9073 1.0218 1.0537 -0.0110 0.0123 -0.0523 52 VAL B CA 2939 C C . VAL B 52 ? 0.9113 1.0507 1.0528 -0.0298 0.0159 -0.0476 52 VAL B C 2940 O O . VAL B 52 ? 0.8856 1.0118 1.0234 -0.0239 0.0195 -0.0483 52 VAL B O 2941 C CB . VAL B 52 ? 0.9210 1.0821 1.0807 0.0096 0.0116 -0.0548 52 VAL B CB 2942 C CG1 . VAL B 52 ? 0.9368 1.1348 1.0987 0.0296 0.0158 -0.0566 52 VAL B CG1 2943 C CG2 . VAL B 52 ? 0.9314 1.0569 1.0897 0.0299 0.0077 -0.0589 52 VAL B CG2 2944 N N . ASN B 53 ? 0.8716 1.0479 1.0107 -0.0562 0.0140 -0.0416 53 ASN B N 2945 C CA . ASN B 53 ? 0.8868 1.0917 1.0179 -0.0814 0.0160 -0.0342 53 ASN B CA 2946 C C . ASN B 53 ? 0.9015 1.0383 1.0055 -0.0952 0.0161 -0.0326 53 ASN B C 2947 O O . ASN B 53 ? 0.9506 1.0969 1.0496 -0.1021 0.0199 -0.0289 53 ASN B O 2948 C CB . ASN B 53 ? 0.8884 1.1426 1.0151 -0.1170 0.0111 -0.0255 53 ASN B CB 2949 C CG . ASN B 53 ? 0.8880 1.2194 1.0408 -0.0988 0.0114 -0.0260 53 ASN B CG 2950 O OD1 . ASN B 53 ? 0.9084 1.2599 1.0775 -0.0581 0.0159 -0.0323 53 ASN B OD1 2951 N ND2 . ASN B 53 ? 0.9270 1.2973 1.0770 -0.1283 0.0053 -0.0193 53 ASN B ND2 2952 N N . SER B 54 ? 0.9206 0.9914 1.0046 -0.0949 0.0123 -0.0351 54 SER B N 2953 C CA . SER B 54 ? 0.9710 0.9759 1.0232 -0.0976 0.0125 -0.0337 54 SER B CA 2954 C C . SER B 54 ? 0.9851 0.9899 1.0526 -0.0709 0.0187 -0.0371 54 SER B C 2955 O O . SER B 54 ? 0.9898 0.9795 1.0424 -0.0761 0.0215 -0.0339 54 SER B O 2956 C CB . SER B 54 ? 0.9827 0.9247 1.0076 -0.0920 0.0077 -0.0359 54 SER B CB 2957 O OG . SER B 54 ? 1.0122 0.9279 1.0014 -0.1231 0.0001 -0.0320 54 SER B OG 2958 N N . ILE B 55 ? 1.0233 1.0422 1.1159 -0.0451 0.0197 -0.0430 55 ILE B N 2959 C CA . ILE B 55 ? 1.0533 1.0711 1.1559 -0.0244 0.0229 -0.0463 55 ILE B CA 2960 C C . ILE B 55 ? 1.0737 1.1296 1.1839 -0.0248 0.0272 -0.0461 55 ILE B C 2961 O O . ILE B 55 ? 1.1040 1.1482 1.2061 -0.0241 0.0302 -0.0448 55 ILE B O 2962 C CB . ILE B 55 ? 1.0938 1.1142 1.2119 -0.0038 0.0202 -0.0514 55 ILE B CB 2963 C CG1 . ILE B 55 ? 1.0867 1.0732 1.1969 -0.0006 0.0172 -0.0497 55 ILE B CG1 2964 C CG2 . ILE B 55 ? 1.0925 1.1154 1.2142 0.0120 0.0209 -0.0551 55 ILE B CG2 2965 C CD1 . ILE B 55 ? 1.0884 1.0783 1.2100 0.0105 0.0130 -0.0519 55 ILE B CD1 2966 N N . ILE B 56 ? 1.0722 1.1787 1.1964 -0.0229 0.0276 -0.0467 56 ILE B N 2967 C CA . ILE B 56 ? 1.0793 1.2352 1.2096 -0.0181 0.0322 -0.0457 56 ILE B CA 2968 C C . ILE B 56 ? 1.1756 1.3339 1.2925 -0.0458 0.0349 -0.0374 56 ILE B C 2969 O O . ILE B 56 ? 1.1901 1.3621 1.3060 -0.0397 0.0392 -0.0369 56 ILE B O 2970 C CB . ILE B 56 ? 1.0494 1.2729 1.1936 -0.0111 0.0323 -0.0450 56 ILE B CB 2971 C CG1 . ILE B 56 ? 1.0175 1.2304 1.1652 0.0241 0.0298 -0.0538 56 ILE B CG1 2972 C CG2 . ILE B 56 ? 1.0385 1.3305 1.1869 -0.0099 0.0377 -0.0402 56 ILE B CG2 2973 C CD1 . ILE B 56 ? 1.0267 1.3001 1.1836 0.0382 0.0294 -0.0533 56 ILE B CD1 2974 N N . ASP B 57 ? 1.2632 1.4005 1.3630 -0.0765 0.0311 -0.0307 57 ASP B N 2975 C CA . ASP B 57 ? 1.3274 1.4540 1.4017 -0.1088 0.0311 -0.0210 57 ASP B CA 2976 C C . ASP B 57 ? 1.3025 1.3678 1.3554 -0.1008 0.0331 -0.0218 57 ASP B C 2977 O O . ASP B 57 ? 1.2744 1.3497 1.3197 -0.1082 0.0367 -0.0170 57 ASP B O 2978 C CB . ASP B 57 ? 1.4355 1.5378 1.4826 -0.1452 0.0234 -0.0142 57 ASP B CB 2979 C CG . ASP B 57 ? 1.5967 1.6919 1.6094 -0.1874 0.0207 -0.0018 57 ASP B CG 2980 O OD1 . ASP B 57 ? 1.6665 1.8312 1.6942 -0.1981 0.0247 0.0051 57 ASP B OD1 2981 O OD2 . ASP B 57 ? 1.6923 1.7104 1.6570 -0.2093 0.0140 0.0018 57 ASP B OD2 2982 N N . LYS B 58 ? 1.2965 1.3063 1.3396 -0.0844 0.0310 -0.0266 58 LYS B N 2983 C CA . LYS B 58 ? 1.3098 1.2723 1.3332 -0.0710 0.0329 -0.0265 58 LYS B CA 2984 C C . LYS B 58 ? 1.3540 1.3456 1.3972 -0.0542 0.0383 -0.0293 58 LYS B C 2985 O O . LYS B 58 ? 1.3886 1.3615 1.4145 -0.0543 0.0409 -0.0258 58 LYS B O 2986 C CB . LYS B 58 ? 1.3056 1.2320 1.3256 -0.0491 0.0306 -0.0307 58 LYS B CB 2987 C CG . LYS B 58 ? 1.3589 1.2379 1.3457 -0.0578 0.0252 -0.0286 58 LYS B CG 2988 C CD . LYS B 58 ? 1.4186 1.2375 1.3497 -0.0710 0.0231 -0.0221 58 LYS B CD 2989 C CE . LYS B 58 ? 1.4623 1.2828 1.3733 -0.1124 0.0188 -0.0158 58 LYS B CE 2990 N NZ . LYS B 58 ? 1.5613 1.2971 1.3997 -0.1298 0.0120 -0.0098 58 LYS B NZ 2991 N N . MET B 59 ? 1.3962 1.4276 1.4690 -0.0381 0.0390 -0.0359 59 MET B N 2992 C CA . MET B 59 ? 1.4344 1.4791 1.5170 -0.0190 0.0416 -0.0407 59 MET B CA 2993 C C . MET B 59 ? 1.4657 1.5552 1.5520 -0.0223 0.0464 -0.0387 59 MET B C 2994 O O . MET B 59 ? 1.4369 1.5311 1.5234 -0.0077 0.0485 -0.0424 59 MET B O 2995 C CB . MET B 59 ? 1.4446 1.4944 1.5420 0.0015 0.0381 -0.0490 59 MET B CB 2996 C CG . MET B 59 ? 1.4286 1.4464 1.5255 0.0041 0.0333 -0.0495 59 MET B CG 2997 S SD . MET B 59 ? 1.4397 1.4257 1.5247 0.0091 0.0322 -0.0462 59 MET B SD 2998 C CE . MET B 59 ? 1.4473 1.4436 1.5308 0.0165 0.0331 -0.0496 59 MET B CE 2999 N N . ASN B 60 ? 1.5390 1.6656 1.6260 -0.0428 0.0475 -0.0320 60 ASN B N 3000 C CA . ASN B 60 ? 1.6128 1.8014 1.7064 -0.0440 0.0525 -0.0283 60 ASN B CA 3001 C C . ASN B 60 ? 1.6105 1.7906 1.6868 -0.0597 0.0561 -0.0206 60 ASN B C 3002 O O . ASN B 60 ? 1.5823 1.8111 1.6638 -0.0541 0.0610 -0.0185 60 ASN B O 3003 C CB . ASN B 60 ? 1.6275 1.8824 1.7317 -0.0599 0.0522 -0.0217 60 ASN B CB 3004 C CG . ASN B 60 ? 1.7008 1.9434 1.7855 -0.1055 0.0484 -0.0093 60 ASN B CG 3005 O OD1 . ASN B 60 ? 1.7341 1.9424 1.7937 -0.1275 0.0484 -0.0020 60 ASN B OD1 3006 N ND2 . ASN B 60 ? 1.7150 1.9818 1.8048 -0.1209 0.0439 -0.0065 60 ASN B ND2 3007 N N . THR B 61 ? 1.6600 1.7780 1.7112 -0.0757 0.0537 -0.0160 61 THR B N 3008 C CA . THR B 61 ? 1.7270 1.8213 1.7561 -0.0825 0.0566 -0.0101 61 THR B CA 3009 C C . THR B 61 ? 1.6482 1.7050 1.6782 -0.0538 0.0569 -0.0183 61 THR B C 3010 O O . THR B 61 ? 1.5637 1.5706 1.5791 -0.0489 0.0537 -0.0188 61 THR B O 3011 C CB . THR B 61 ? 1.8257 1.8691 1.8126 -0.1160 0.0528 0.0015 61 THR B CB 3012 O OG1 . THR B 61 ? 1.9154 1.9273 1.8920 -0.1260 0.0465 0.0007 61 THR B OG1 3013 C CG2 . THR B 61 ? 1.8327 1.9203 1.8093 -0.1515 0.0538 0.0147 61 THR B CG2 3014 N N . GLN B 62 ? 1.6370 1.7226 1.6811 -0.0346 0.0601 -0.0239 62 GLN B N 3015 C CA . GLN B 62 ? 1.6201 1.6824 1.6669 -0.0116 0.0584 -0.0318 62 GLN B CA 3016 C C . GLN B 62 ? 1.6085 1.6939 1.6557 0.0009 0.0616 -0.0350 62 GLN B C 3017 O O . GLN B 62 ? 1.6491 1.7782 1.7012 0.0009 0.0655 -0.0341 62 GLN B O 3018 C CB . GLN B 62 ? 1.5446 1.6052 1.6069 0.0021 0.0533 -0.0406 62 GLN B CB 3019 C CG . GLN B 62 ? 1.5080 1.5621 1.5716 0.0215 0.0495 -0.0496 62 GLN B CG 3020 C CD . GLN B 62 ? 1.4908 1.5347 1.5606 0.0302 0.0431 -0.0562 62 GLN B CD 3021 O OE1 . GLN B 62 ? 1.5233 1.5624 1.6004 0.0233 0.0419 -0.0538 62 GLN B OE1 3022 N NE2 . GLN B 62 ? 1.4612 1.4953 1.5218 0.0445 0.0378 -0.0645 62 GLN B NE2 3023 N N . PHE B 63 ? 1.5125 1.5740 1.5531 0.0120 0.0595 -0.0380 63 PHE B N 3024 C CA . PHE B 63 ? 1.4634 1.5374 1.4984 0.0223 0.0612 -0.0411 63 PHE B CA 3025 C C . PHE B 63 ? 1.4249 1.5269 1.4639 0.0387 0.0606 -0.0506 63 PHE B C 3026 O O . PHE B 63 ? 1.4258 1.5203 1.4676 0.0492 0.0554 -0.0584 63 PHE B O 3027 C CB . PHE B 63 ? 1.4056 1.4548 1.4334 0.0294 0.0564 -0.0430 63 PHE B CB 3028 C CG . PHE B 63 ? 1.3562 1.4143 1.3739 0.0363 0.0575 -0.0447 63 PHE B CG 3029 C CD1 . PHE B 63 ? 1.3416 1.4016 1.3487 0.0318 0.0634 -0.0360 63 PHE B CD1 3030 C CD2 . PHE B 63 ? 1.3745 1.4318 1.3861 0.0473 0.0516 -0.0551 63 PHE B CD2 3031 C CE1 . PHE B 63 ? 1.3544 1.4250 1.3526 0.0386 0.0645 -0.0374 63 PHE B CE1 3032 C CE2 . PHE B 63 ? 1.3546 1.4173 1.3527 0.0533 0.0517 -0.0574 63 PHE B CE2 3033 C CZ . PHE B 63 ? 1.3605 1.4348 1.3558 0.0492 0.0588 -0.0485 63 PHE B CZ 3034 N N . GLU B 64 ? 1.4038 1.5354 1.4374 0.0438 0.0659 -0.0495 64 GLU B N 3035 C CA . GLU B 64 ? 1.3918 1.5505 1.4193 0.0676 0.0661 -0.0586 64 GLU B CA 3036 C C . GLU B 64 ? 1.3495 1.5079 1.3612 0.0768 0.0675 -0.0609 64 GLU B C 3037 O O . GLU B 64 ? 1.2904 1.4652 1.3031 0.0639 0.0736 -0.0514 64 GLU B O 3038 C CB . GLU B 64 ? 1.4042 1.6246 1.4430 0.0672 0.0728 -0.0527 64 GLU B CB 3039 C CG . GLU B 64 ? 1.4340 1.6739 1.4810 0.0333 0.0779 -0.0368 64 GLU B CG 3040 C CD . GLU B 64 ? 1.4091 1.7252 1.4652 0.0260 0.0836 -0.0279 64 GLU B CD 3041 O OE1 . GLU B 64 ? 1.3872 1.7538 1.4402 0.0425 0.0887 -0.0277 64 GLU B OE1 3042 O OE2 . GLU B 64 ? 1.3905 1.7209 1.4552 0.0032 0.0825 -0.0201 64 GLU B OE2 3043 N N . ALA B 65 ? 1.3674 1.5001 1.3585 0.0975 0.0604 -0.0735 65 ALA B N 3044 C CA . ALA B 65 ? 1.4067 1.5300 1.3774 0.1056 0.0590 -0.0777 65 ALA B CA 3045 C C . ALA B 65 ? 1.4383 1.6082 1.4001 0.1266 0.0664 -0.0790 65 ALA B C 3046 O O . ALA B 65 ? 1.4082 1.6166 1.3732 0.1427 0.0705 -0.0798 65 ALA B O 3047 C CB . ALA B 65 ? 1.4301 1.4990 1.3717 0.1142 0.0456 -0.0901 65 ALA B CB 3048 N N . VAL B 66 ? 1.4324 1.6058 1.3826 0.1278 0.0685 -0.0782 66 VAL B N 3049 C CA . VAL B 66 ? 1.4546 1.6687 1.3894 0.1524 0.0742 -0.0811 66 VAL B CA 3050 C C . VAL B 66 ? 1.4645 1.6404 1.3664 0.1645 0.0672 -0.0914 66 VAL B C 3051 O O . VAL B 66 ? 1.4787 1.6186 1.3799 0.1447 0.0613 -0.0901 66 VAL B O 3052 C CB . VAL B 66 ? 1.4430 1.7216 1.3991 0.1362 0.0868 -0.0645 66 VAL B CB 3053 C CG1 . VAL B 66 ? 1.4267 1.7617 1.4033 0.1319 0.0928 -0.0561 66 VAL B CG1 3054 C CG2 . VAL B 66 ? 1.4256 1.6794 1.3927 0.1033 0.0878 -0.0529 66 VAL B CG2 3055 N N . GLY B 67 ? 1.4312 1.6181 1.3021 0.1987 0.0672 -0.1015 67 GLY B N 3056 C CA . GLY B 67 ? 1.4543 1.5998 1.2838 0.2123 0.0589 -0.1130 67 GLY B CA 3057 C C . GLY B 67 ? 1.4013 1.5772 1.2425 0.1986 0.0661 -0.1037 67 GLY B C 3058 O O . GLY B 67 ? 1.4104 1.6507 1.2745 0.1968 0.0791 -0.0916 67 GLY B O 3059 N N . ARG B 68 ? 1.3471 1.4787 1.1704 0.1859 0.0567 -0.1078 68 ARG B N 3060 C CA . ARG B 68 ? 1.3065 1.4596 1.1306 0.1791 0.0614 -0.1016 68 ARG B CA 3061 C C . ARG B 68 ? 1.3296 1.4330 1.1057 0.1885 0.0477 -0.1160 68 ARG B C 3062 O O . ARG B 68 ? 1.3453 1.3946 1.1030 0.1731 0.0331 -0.1222 68 ARG B O 3063 C CB . ARG B 68 ? 1.2792 1.4373 1.1357 0.1461 0.0645 -0.0865 68 ARG B CB 3064 C CG . ARG B 68 ? 1.2275 1.4176 1.1198 0.1315 0.0752 -0.0720 68 ARG B CG 3065 C CD . ARG B 68 ? 1.2031 1.3829 1.1113 0.1068 0.0767 -0.0587 68 ARG B CD 3066 N NE . ARG B 68 ? 1.1910 1.3751 1.1212 0.0916 0.0816 -0.0486 68 ARG B NE 3067 C CZ . ARG B 68 ? 1.1683 1.3302 1.1082 0.0872 0.0761 -0.0525 68 ARG B CZ 3068 N NH1 . ARG B 68 ? 1.1875 1.3197 1.1165 0.0942 0.0650 -0.0650 68 ARG B NH1 3069 N NH2 . ARG B 68 ? 1.2080 1.3738 1.1639 0.0730 0.0805 -0.0432 68 ARG B NH2 3070 N N . GLU B 69 ? 1.3146 1.4379 1.0672 0.2109 0.0517 -0.1203 69 GLU B N 3071 C CA . GLU B 69 ? 1.3190 1.3936 1.0183 0.2205 0.0383 -0.1344 69 GLU B CA 3072 C C . GLU B 69 ? 1.2206 1.3052 0.9347 0.1924 0.0373 -0.1251 69 GLU B C 3073 O O . GLU B 69 ? 1.1541 1.2894 0.9089 0.1811 0.0507 -0.1093 69 GLU B O 3074 C CB . GLU B 69 ? 1.4339 1.5310 1.0992 0.2629 0.0440 -0.1429 69 GLU B CB 3075 C CG . GLU B 69 ? 1.5802 1.6004 1.1664 0.2905 0.0270 -0.1648 69 GLU B CG 3076 C CD . GLU B 69 ? 1.6474 1.6469 1.2012 0.3302 0.0255 -0.1757 69 GLU B CD 3077 O OE1 . GLU B 69 ? 1.6078 1.6346 1.2026 0.3232 0.0322 -0.1677 69 GLU B OE1 3078 O OE2 . GLU B 69 ? 1.7226 1.6771 1.2050 0.3713 0.0174 -0.1925 69 GLU B OE2 3079 N N . PHE B 70 ? 1.2238 1.2581 0.8991 0.1804 0.0204 -0.1341 70 PHE B N 3080 C CA . PHE B 70 ? 1.2064 1.2572 0.8867 0.1602 0.0183 -0.1267 70 PHE B CA 3081 C C . PHE B 70 ? 1.2660 1.2688 0.8821 0.1654 0.0018 -0.1421 70 PHE B C 3082 O O . PHE B 70 ? 1.3019 1.2390 0.8655 0.1727 -0.0132 -0.1574 70 PHE B O 3083 C CB . PHE B 70 ? 1.1986 1.2516 0.9083 0.1251 0.0128 -0.1152 70 PHE B CB 3084 C CG . PHE B 70 ? 1.1463 1.2328 0.9083 0.1205 0.0268 -0.1014 70 PHE B CG 3085 C CD1 . PHE B 70 ? 1.1673 1.2324 0.9376 0.1196 0.0248 -0.1045 70 PHE B CD1 3086 C CD2 . PHE B 70 ? 1.1090 1.2406 0.9042 0.1173 0.0409 -0.0853 70 PHE B CD2 3087 C CE1 . PHE B 70 ? 1.1212 1.2127 0.9343 0.1139 0.0363 -0.0924 70 PHE B CE1 3088 C CE2 . PHE B 70 ? 1.0782 1.2267 0.9087 0.1115 0.0514 -0.0732 70 PHE B CE2 3089 C CZ . PHE B 70 ? 1.0893 1.2194 0.9300 0.1090 0.0490 -0.0770 70 PHE B CZ 3090 N N . ASN B 71 ? 1.2922 1.3212 0.9052 0.1623 0.0035 -0.1383 71 ASN B N 3091 C CA . ASN B 71 ? 1.3793 1.3628 0.9267 0.1670 -0.0125 -0.1531 71 ASN B CA 3092 C C . ASN B 71 ? 1.3978 1.3516 0.9256 0.1246 -0.0332 -0.1518 71 ASN B C 3093 O O . ASN B 71 ? 1.3565 1.3281 0.9217 0.0969 -0.0344 -0.1399 71 ASN B O 3094 C CB . ASN B 71 ? 1.3721 1.4001 0.9190 0.1886 -0.0008 -0.1511 71 ASN B CB 3095 C CG . ASN B 71 ? 1.3365 1.4155 0.9209 0.1642 0.0042 -0.1345 71 ASN B CG 3096 O OD1 . ASN B 71 ? 1.3714 1.4409 0.9533 0.1327 -0.0092 -0.1307 71 ASN B OD1 3097 N ND2 . ASN B 71 ? 1.3098 1.4464 0.9251 0.1792 0.0229 -0.1231 71 ASN B ND2 3098 N N . ASN B 72 ? 1.4753 1.3894 0.9425 0.1189 -0.0499 -0.1628 72 ASN B N 3099 C CA . ASN B 72 ? 1.5053 1.3894 0.9409 0.0731 -0.0736 -0.1619 72 ASN B CA 3100 C C . ASN B 72 ? 1.4396 1.4037 0.9305 0.0435 -0.0690 -0.1412 72 ASN B C 3101 O O . ASN B 72 ? 1.4782 1.4426 0.9622 0.0024 -0.0856 -0.1344 72 ASN B O 3102 C CB . ASN B 72 ? 1.6056 1.4229 0.9537 0.0734 -0.0938 -0.1791 72 ASN B CB 3103 C CG . ASN B 72 ? 1.6918 1.4386 0.9777 0.0249 -0.1247 -0.1835 72 ASN B CG 3104 O OD1 . ASN B 72 ? 1.7420 1.4361 1.0095 0.0134 -0.1341 -0.1865 72 ASN B OD1 3105 N ND2 . ASN B 72 ? 1.7392 1.4851 0.9890 -0.0069 -0.1417 -0.1828 72 ASN B ND2 3106 N N . LEU B 73 ? 1.3660 1.3980 0.9055 0.0648 -0.0476 -0.1302 73 LEU B N 3107 C CA . LEU B 73 ? 1.3071 1.4127 0.8922 0.0484 -0.0412 -0.1104 73 LEU B CA 3108 C C . LEU B 73 ? 1.2464 1.3961 0.8955 0.0596 -0.0206 -0.0946 73 LEU B C 3109 O O . LEU B 73 ? 1.1925 1.3970 0.8742 0.0641 -0.0090 -0.0789 73 LEU B O 3110 C CB . LEU B 73 ? 1.3251 1.4640 0.9017 0.0624 -0.0356 -0.1088 73 LEU B CB 3111 C CG . LEU B 73 ? 1.4026 1.5011 0.9119 0.0494 -0.0569 -0.1232 73 LEU B CG 3112 C CD1 . LEU B 73 ? 1.3797 1.5070 0.8822 0.0744 -0.0469 -0.1240 73 LEU B CD1 3113 C CD2 . LEU B 73 ? 1.4120 1.5260 0.9084 0.0024 -0.0782 -0.1154 73 LEU B CD2 3114 N N . GLU B 74 ? 1.2294 1.3489 0.8888 0.0650 -0.0174 -0.0991 74 GLU B N 3115 C CA . GLU B 74 ? 1.1755 1.3233 0.8861 0.0695 -0.0022 -0.0858 74 GLU B CA 3116 C C . GLU B 74 ? 1.1585 1.2829 0.8723 0.0472 -0.0138 -0.0862 74 GLU B C 3117 O O . GLU B 74 ? 1.1136 1.2299 0.8519 0.0541 -0.0056 -0.0847 74 GLU B O 3118 C CB . GLU B 74 ? 1.1849 1.3290 0.9088 0.0975 0.0147 -0.0890 74 GLU B CB 3119 C CG . GLU B 74 ? 1.2004 1.3789 0.9283 0.1163 0.0288 -0.0833 74 GLU B CG 3120 C CD . GLU B 74 ? 1.2392 1.4225 0.9716 0.1399 0.0424 -0.0867 74 GLU B CD 3121 O OE1 . GLU B 74 ? 1.2873 1.4400 1.0001 0.1511 0.0372 -0.1006 74 GLU B OE1 3122 O OE2 . GLU B 74 ? 1.2408 1.4610 0.9925 0.1474 0.0578 -0.0743 74 GLU B OE2 3123 N N . ARG B 75 ? 1.1697 1.2855 0.8563 0.0170 -0.0338 -0.0871 75 ARG B N 3124 C CA . ARG B 75 ? 1.1756 1.2659 0.8557 -0.0097 -0.0479 -0.0871 75 ARG B CA 3125 C C . ARG B 75 ? 1.0981 1.2393 0.8304 -0.0130 -0.0378 -0.0698 75 ARG B C 3126 O O . ARG B 75 ? 1.1127 1.2330 0.8563 -0.0174 -0.0384 -0.0704 75 ARG B O 3127 C CB . ARG B 75 ? 1.2578 1.3322 0.8909 -0.0499 -0.0737 -0.0889 75 ARG B CB 3128 C CG . ARG B 75 ? 1.3567 1.3512 0.9182 -0.0497 -0.0894 -0.1092 75 ARG B CG 3129 C CD . ARG B 75 ? 1.4251 1.3435 0.9611 -0.0302 -0.0898 -0.1243 75 ARG B CD 3130 N NE . ARG B 75 ? 1.6038 1.4336 1.0564 -0.0250 -0.1071 -0.1444 75 ARG B NE 3131 C CZ . ARG B 75 ? 1.6766 1.4326 1.0887 0.0025 -0.1088 -0.1603 75 ARG B CZ 3132 N NH1 . ARG B 75 ? 1.6361 1.4039 1.0900 0.0230 -0.0943 -0.1578 75 ARG B NH1 3133 N NH2 . ARG B 75 ? 1.7442 1.4131 1.0683 0.0122 -0.1258 -0.1788 75 ARG B NH2 3134 N N . ARG B 76 ? 1.0515 1.2568 0.8103 -0.0071 -0.0289 -0.0546 76 ARG B N 3135 C CA . ARG B 76 ? 0.9893 1.2394 0.7874 -0.0023 -0.0194 -0.0383 76 ARG B CA 3136 C C . ARG B 76 ? 0.9615 1.1838 0.7834 0.0199 -0.0036 -0.0404 76 ARG B C 3137 O O . ARG B 76 ? 0.9521 1.1689 0.7896 0.0137 -0.0044 -0.0375 76 ARG B O 3138 C CB . ARG B 76 ? 0.9618 1.2747 0.7734 0.0129 -0.0104 -0.0229 76 ARG B CB 3139 C CG . ARG B 76 ? 0.9665 1.3337 0.7643 -0.0108 -0.0256 -0.0147 76 ARG B CG 3140 C CD . ARG B 76 ? 0.9493 1.3727 0.7542 0.0136 -0.0149 -0.0018 76 ARG B CD 3141 N NE . ARG B 76 ? 0.9561 1.3454 0.7493 0.0336 -0.0051 -0.0109 76 ARG B NE 3142 C CZ . ARG B 76 ? 0.9290 1.3410 0.7260 0.0617 0.0089 -0.0019 76 ARG B CZ 3143 N NH1 . ARG B 76 ? 0.9450 1.4087 0.7522 0.0789 0.0149 0.0158 76 ARG B NH1 3144 N NH2 . ARG B 76 ? 0.9012 1.2836 0.6866 0.0748 0.0167 -0.0097 76 ARG B NH2 3145 N N . ILE B 77 ? 0.9973 1.2064 0.8206 0.0429 0.0101 -0.0443 77 ILE B N 3146 C CA . ILE B 77 ? 1.0325 1.2226 0.8759 0.0583 0.0241 -0.0442 77 ILE B CA 3147 C C . ILE B 77 ? 1.0633 1.2106 0.8997 0.0543 0.0184 -0.0582 77 ILE B C 3148 O O . ILE B 77 ? 1.0905 1.2287 0.9466 0.0585 0.0254 -0.0564 77 ILE B O 3149 C CB . ILE B 77 ? 1.0543 1.2502 0.8989 0.0779 0.0395 -0.0412 77 ILE B CB 3150 C CG1 . ILE B 77 ? 1.1669 1.3518 0.9866 0.0838 0.0362 -0.0543 77 ILE B CG1 3151 C CG2 . ILE B 77 ? 1.0513 1.2792 0.8983 0.0862 0.0462 -0.0255 77 ILE B CG2 3152 C CD1 . ILE B 77 ? 1.2054 1.4037 1.0276 0.1007 0.0515 -0.0502 77 ILE B CD1 3153 N N . GLU B 78 ? 1.0978 1.2145 0.8999 0.0477 0.0049 -0.0720 78 GLU B N 3154 C CA . GLU B 78 ? 1.1321 1.1996 0.9155 0.0468 -0.0033 -0.0851 78 GLU B CA 3155 C C . GLU B 78 ? 1.0851 1.1479 0.8799 0.0240 -0.0123 -0.0793 78 GLU B C 3156 O O . GLU B 78 ? 1.0536 1.0955 0.8586 0.0279 -0.0101 -0.0822 78 GLU B O 3157 C CB . GLU B 78 ? 1.2549 1.2756 0.9821 0.0445 -0.0194 -0.1009 78 GLU B CB 3158 C CG . GLU B 78 ? 1.3783 1.3336 1.0695 0.0474 -0.0306 -0.1151 78 GLU B CG 3159 C CD . GLU B 78 ? 1.6078 1.4990 1.2261 0.0431 -0.0504 -0.1305 78 GLU B CD 3160 O OE1 . GLU B 78 ? 1.7086 1.6025 1.3058 0.0151 -0.0639 -0.1272 78 GLU B OE1 3161 O OE2 . GLU B 78 ? 1.7564 1.5933 1.3325 0.0692 -0.0535 -0.1458 78 GLU B OE2 3162 N N . ASN B 79 ? 1.0581 1.1477 0.8506 0.0000 -0.0226 -0.0702 79 ASN B N 3163 C CA . ASN B 79 ? 1.0747 1.1731 0.8761 -0.0244 -0.0322 -0.0621 79 ASN B CA 3164 C C . ASN B 79 ? 1.0204 1.1527 0.8670 -0.0098 -0.0164 -0.0503 79 ASN B C 3165 O O . ASN B 79 ? 1.0090 1.1312 0.8670 -0.0169 -0.0185 -0.0486 79 ASN B O 3166 C CB . ASN B 79 ? 1.1327 1.2726 0.9224 -0.0534 -0.0461 -0.0518 79 ASN B CB 3167 C CG . ASN B 79 ? 1.1531 1.3099 0.9464 -0.0844 -0.0586 -0.0420 79 ASN B CG 3168 O OD1 . ASN B 79 ? 1.2150 1.3169 0.9805 -0.1040 -0.0720 -0.0499 79 ASN B OD1 3169 N ND2 . ASN B 79 ? 1.1300 1.3639 0.9530 -0.0870 -0.0545 -0.0237 79 ASN B ND2 3170 N N . LEU B 80 ? 1.0087 1.1743 0.8741 0.0109 -0.0015 -0.0421 80 LEU B N 3171 C CA . LEU B 80 ? 0.9695 1.1505 0.8632 0.0278 0.0130 -0.0319 80 LEU B CA 3172 C C . LEU B 80 ? 0.9276 1.0689 0.8294 0.0342 0.0187 -0.0406 80 LEU B C 3173 O O . LEU B 80 ? 0.9238 1.0621 0.8419 0.0336 0.0210 -0.0366 80 LEU B O 3174 C CB . LEU B 80 ? 1.0211 1.2218 0.9164 0.0486 0.0263 -0.0241 80 LEU B CB 3175 C CG . LEU B 80 ? 1.0404 1.2555 0.9463 0.0664 0.0376 -0.0098 80 LEU B CG 3176 C CD1 . LEU B 80 ? 1.0575 1.2858 0.9505 0.0838 0.0463 -0.0019 80 LEU B CD1 3177 C CD2 . LEU B 80 ? 1.0625 1.2414 0.9781 0.0714 0.0462 -0.0117 80 LEU B CD2 3178 N N . ASN B 81 ? 0.9707 1.0873 0.8592 0.0421 0.0207 -0.0523 81 ASN B N 3179 C CA . ASN B 81 ? 0.9522 1.0449 0.8470 0.0517 0.0267 -0.0598 81 ASN B CA 3180 C C . ASN B 81 ? 0.9717 1.0337 0.8600 0.0416 0.0154 -0.0673 81 ASN B C 3181 O O . ASN B 81 ? 0.8978 0.9531 0.8031 0.0456 0.0206 -0.0670 81 ASN B O 3182 C CB . ASN B 81 ? 0.9756 1.0616 0.8524 0.0669 0.0303 -0.0697 81 ASN B CB 3183 C CG . ASN B 81 ? 0.9837 1.0646 0.8684 0.0803 0.0380 -0.0748 81 ASN B CG 3184 O OD1 . ASN B 81 ? 1.0287 1.1268 0.9378 0.0798 0.0487 -0.0657 81 ASN B OD1 3185 N ND2 . ASN B 81 ? 1.0105 1.0673 0.8684 0.0934 0.0317 -0.0889 81 ASN B ND2 3186 N N . LYS B 82 ? 1.0533 1.0937 0.9124 0.0260 -0.0010 -0.0733 82 LYS B N 3187 C CA . LYS B 82 ? 1.1212 1.1224 0.9633 0.0127 -0.0141 -0.0793 82 LYS B CA 3188 C C . LYS B 82 ? 1.0887 1.1157 0.9607 -0.0018 -0.0137 -0.0666 82 LYS B C 3189 O O . LYS B 82 ? 1.0454 1.0554 0.9275 0.0001 -0.0127 -0.0682 82 LYS B O 3190 C CB . LYS B 82 ? 1.2283 1.1904 1.0197 -0.0078 -0.0347 -0.0868 82 LYS B CB 3191 C CG . LYS B 82 ? 1.3563 1.2549 1.1118 -0.0175 -0.0495 -0.0958 82 LYS B CG 3192 C CD . LYS B 82 ? 1.5123 1.3572 1.2031 -0.0453 -0.0736 -0.1019 82 LYS B CD 3193 C CE . LYS B 82 ? 1.6272 1.3949 1.2538 -0.0219 -0.0812 -0.1215 82 LYS B CE 3194 N NZ . LYS B 82 ? 1.6359 1.4135 1.2459 -0.0072 -0.0780 -0.1274 82 LYS B NZ 3195 N N . LYS B 83 ? 1.1217 1.1948 1.0066 -0.0123 -0.0140 -0.0535 83 LYS B N 3196 C CA . LYS B 83 ? 1.1187 1.2265 1.0280 -0.0203 -0.0132 -0.0400 83 LYS B CA 3197 C C . LYS B 83 ? 1.0732 1.1852 1.0111 0.0019 0.0029 -0.0362 83 LYS B C 3198 O O . LYS B 83 ? 1.0708 1.1920 1.0235 -0.0006 0.0032 -0.0299 83 LYS B O 3199 C CB . LYS B 83 ? 1.1460 1.3140 1.0584 -0.0291 -0.0164 -0.0257 83 LYS B CB 3200 C CG . LYS B 83 ? 1.2468 1.4363 1.1441 -0.0652 -0.0353 -0.0188 83 LYS B CG 3201 C CD . LYS B 83 ? 1.3522 1.4748 1.2139 -0.0904 -0.0520 -0.0313 83 LYS B CD 3202 C CE . LYS B 83 ? 1.4216 1.5635 1.2617 -0.1353 -0.0728 -0.0212 83 LYS B CE 3203 N NZ . LYS B 83 ? 1.5036 1.6636 1.3142 -0.1592 -0.0857 -0.0188 83 LYS B NZ 3204 N N . MET B 84 ? 1.0820 1.1862 1.0232 0.0207 0.0153 -0.0394 84 MET B N 3205 C CA . MET B 84 ? 1.0533 1.1538 1.0116 0.0350 0.0284 -0.0351 84 MET B CA 3206 C C . MET B 84 ? 1.0540 1.1259 1.0184 0.0340 0.0283 -0.0440 84 MET B C 3207 O O . MET B 84 ? 1.0512 1.1194 1.0294 0.0350 0.0319 -0.0401 84 MET B O 3208 C CB . MET B 84 ? 1.0983 1.2023 1.0518 0.0478 0.0395 -0.0329 84 MET B CB 3209 C CG . MET B 84 ? 1.1248 1.2215 1.0822 0.0569 0.0509 -0.0238 84 MET B CG 3210 S SD . MET B 84 ? 1.1807 1.2598 1.1442 0.0542 0.0583 -0.0291 84 MET B SD 3211 C CE . MET B 84 ? 1.2058 1.2999 1.1583 0.0588 0.0630 -0.0321 84 MET B CE 3212 N N . GLU B 85 ? 1.0771 1.1285 1.0267 0.0352 0.0237 -0.0562 85 GLU B N 3213 C CA . GLU B 85 ? 1.0844 1.1140 1.0354 0.0408 0.0236 -0.0647 85 GLU B CA 3214 C C . GLU B 85 ? 1.0838 1.0941 1.0326 0.0280 0.0126 -0.0654 85 GLU B C 3215 O O . GLU B 85 ? 1.0924 1.0995 1.0570 0.0297 0.0157 -0.0643 85 GLU B O 3216 C CB . GLU B 85 ? 1.1474 1.1611 1.0742 0.0549 0.0219 -0.0774 85 GLU B CB 3217 C CG . GLU B 85 ? 1.2352 1.2768 1.1655 0.0663 0.0335 -0.0749 85 GLU B CG 3218 C CD . GLU B 85 ? 1.3029 1.3571 1.2314 0.0854 0.0410 -0.0809 85 GLU B CD 3219 O OE1 . GLU B 85 ? 1.4056 1.4422 1.3048 0.1024 0.0353 -0.0930 85 GLU B OE1 3220 O OE2 . GLU B 85 ? 1.2661 1.3495 1.2174 0.0838 0.0520 -0.0725 85 GLU B OE2 3221 N N . ASP B 86 ? 1.0960 1.0957 1.0233 0.0117 -0.0011 -0.0659 86 ASP B N 3222 C CA . ASP B 86 ? 1.0924 1.0781 1.0137 -0.0076 -0.0133 -0.0632 86 ASP B CA 3223 C C . ASP B 86 ? 1.0361 1.0598 0.9897 -0.0111 -0.0073 -0.0497 86 ASP B C 3224 O O . ASP B 86 ? 1.0415 1.0573 1.0011 -0.0182 -0.0112 -0.0478 86 ASP B O 3225 C CB . ASP B 86 ? 1.1902 1.1654 1.0783 -0.0333 -0.0306 -0.0623 86 ASP B CB 3226 C CG . ASP B 86 ? 1.3582 1.2658 1.1957 -0.0352 -0.0441 -0.0768 86 ASP B CG 3227 O OD1 . ASP B 86 ? 1.4620 1.3304 1.2879 -0.0297 -0.0476 -0.0829 86 ASP B OD1 3228 O OD2 . ASP B 86 ? 1.5144 1.4037 1.3175 -0.0402 -0.0523 -0.0823 86 ASP B OD2 3229 N N . GLY B 87 ? 0.9994 1.0612 0.9675 -0.0032 0.0017 -0.0403 87 GLY B N 3230 C CA . GLY B 87 ? 0.9518 1.0455 0.9390 0.0021 0.0074 -0.0278 87 GLY B CA 3231 C C . GLY B 87 ? 0.9574 1.0305 0.9587 0.0129 0.0154 -0.0303 87 GLY B C 3232 O O . GLY B 87 ? 0.9793 1.0582 0.9897 0.0099 0.0133 -0.0256 87 GLY B O 3233 N N . PHE B 88 ? 0.9488 1.0028 0.9510 0.0233 0.0239 -0.0368 88 PHE B N 3234 C CA . PHE B 88 ? 0.9249 0.9644 0.9381 0.0289 0.0307 -0.0380 88 PHE B CA 3235 C C . PHE B 88 ? 0.9250 0.9465 0.9418 0.0234 0.0241 -0.0458 88 PHE B C 3236 O O . PHE B 88 ? 0.9509 0.9685 0.9785 0.0234 0.0255 -0.0437 88 PHE B O 3237 C CB . PHE B 88 ? 0.9108 0.9465 0.9221 0.0353 0.0404 -0.0397 88 PHE B CB 3238 C CG . PHE B 88 ? 0.8925 0.9314 0.8945 0.0411 0.0477 -0.0298 88 PHE B CG 3239 C CD1 . PHE B 88 ? 0.8949 0.9228 0.8912 0.0461 0.0504 -0.0216 88 PHE B CD1 3240 C CD2 . PHE B 88 ? 0.9248 0.9716 0.9167 0.0443 0.0515 -0.0287 88 PHE B CD2 3241 C CE1 . PHE B 88 ? 0.9235 0.9404 0.8977 0.0560 0.0560 -0.0127 88 PHE B CE1 3242 C CE2 . PHE B 88 ? 0.9351 0.9769 0.9109 0.0511 0.0576 -0.0189 88 PHE B CE2 3243 C CZ . PHE B 88 ? 0.9561 0.9788 0.9198 0.0579 0.0595 -0.0109 88 PHE B CZ 3244 N N . LEU B 89 ? 0.9274 0.9323 0.9284 0.0206 0.0161 -0.0550 89 LEU B N 3245 C CA . LEU B 89 ? 0.9797 0.9575 0.9727 0.0194 0.0085 -0.0624 89 LEU B CA 3246 C C . LEU B 89 ? 0.9781 0.9551 0.9740 0.0037 -0.0001 -0.0556 89 LEU B C 3247 O O . LEU B 89 ? 0.9594 0.9248 0.9615 0.0044 -0.0012 -0.0568 89 LEU B O 3248 C CB . LEU B 89 ? 1.1012 1.0466 1.0601 0.0231 -0.0007 -0.0737 89 LEU B CB 3249 C CG . LEU B 89 ? 1.2388 1.1920 1.1924 0.0435 0.0078 -0.0808 89 LEU B CG 3250 C CD1 . LEU B 89 ? 1.3290 1.2445 1.2381 0.0503 -0.0028 -0.0919 89 LEU B CD1 3251 C CD2 . LEU B 89 ? 1.2302 1.1992 1.2002 0.0597 0.0174 -0.0831 89 LEU B CD2 3252 N N . ASP B 90 ? 0.9709 0.9679 0.9623 -0.0109 -0.0061 -0.0472 90 ASP B N 3253 C CA . ASP B 90 ? 0.9647 0.9801 0.9614 -0.0269 -0.0131 -0.0369 90 ASP B CA 3254 C C . ASP B 90 ? 0.9191 0.9564 0.9415 -0.0132 -0.0025 -0.0303 90 ASP B C 3255 O O . ASP B 90 ? 0.8950 0.9307 0.9237 -0.0179 -0.0056 -0.0275 90 ASP B O 3256 C CB . ASP B 90 ? 1.0101 1.0639 0.9997 -0.0436 -0.0201 -0.0261 90 ASP B CB 3257 C CG . ASP B 90 ? 1.1279 1.1521 1.0818 -0.0670 -0.0358 -0.0312 90 ASP B CG 3258 O OD1 . ASP B 90 ? 1.2194 1.1859 1.1485 -0.0661 -0.0418 -0.0435 90 ASP B OD1 3259 O OD2 . ASP B 90 ? 1.2046 1.2621 1.1497 -0.0851 -0.0429 -0.0226 90 ASP B OD2 3260 N N . VAL B 91 ? 0.8836 0.9344 0.9139 0.0035 0.0090 -0.0277 91 VAL B N 3261 C CA . VAL B 91 ? 0.8637 0.9201 0.9039 0.0175 0.0174 -0.0222 91 VAL B CA 3262 C C . VAL B 91 ? 0.8496 0.8778 0.8974 0.0183 0.0194 -0.0296 91 VAL B C 3263 O O . VAL B 91 ? 0.8610 0.8904 0.9152 0.0200 0.0190 -0.0261 91 VAL B O 3264 C CB . VAL B 91 ? 0.8594 0.9162 0.8918 0.0336 0.0275 -0.0186 91 VAL B CB 3265 C CG1 . VAL B 91 ? 0.8670 0.9061 0.8945 0.0466 0.0341 -0.0153 91 VAL B CG1 3266 C CG2 . VAL B 91 ? 0.8644 0.9580 0.8892 0.0390 0.0264 -0.0090 91 VAL B CG2 3267 N N . TRP B 92 ? 0.8096 0.8196 0.8561 0.0189 0.0214 -0.0389 92 TRP B N 3268 C CA . TRP B 92 ? 0.8182 0.8141 0.8721 0.0209 0.0231 -0.0449 92 TRP B CA 3269 C C . TRP B 92 ? 0.8347 0.8178 0.8873 0.0155 0.0138 -0.0486 92 TRP B C 3270 O O . TRP B 92 ? 0.8631 0.8418 0.9244 0.0170 0.0143 -0.0492 92 TRP B O 3271 C CB . TRP B 92 ? 0.8188 0.8150 0.8708 0.0261 0.0284 -0.0515 92 TRP B CB 3272 C CG . TRP B 92 ? 0.8435 0.8467 0.8944 0.0259 0.0372 -0.0456 92 TRP B CG 3273 C CD1 . TRP B 92 ? 0.8605 0.8702 0.9027 0.0276 0.0411 -0.0437 92 TRP B CD1 3274 C CD2 . TRP B 92 ? 0.8674 0.8626 0.9174 0.0220 0.0417 -0.0399 92 TRP B CD2 3275 N NE1 . TRP B 92 ? 0.9005 0.9045 0.9349 0.0245 0.0477 -0.0365 92 TRP B NE1 3276 C CE2 . TRP B 92 ? 0.8676 0.8586 0.9031 0.0200 0.0474 -0.0342 92 TRP B CE2 3277 C CE3 . TRP B 92 ? 0.9191 0.9050 0.9735 0.0190 0.0403 -0.0391 92 TRP B CE3 3278 C CZ2 . TRP B 92 ? 0.9367 0.9053 0.9546 0.0130 0.0504 -0.0276 92 TRP B CZ2 3279 C CZ3 . TRP B 92 ? 0.9359 0.9036 0.9759 0.0128 0.0436 -0.0334 92 TRP B CZ3 3280 C CH2 . TRP B 92 ? 0.9630 0.9177 0.9813 0.0088 0.0479 -0.0277 92 TRP B CH2 3281 N N . THR B 93 ? 0.8502 0.8223 0.8861 0.0075 0.0041 -0.0508 93 THR B N 3282 C CA . THR B 93 ? 0.8618 0.8102 0.8845 -0.0018 -0.0072 -0.0526 93 THR B CA 3283 C C . THR B 93 ? 0.8632 0.8326 0.9004 -0.0110 -0.0086 -0.0418 93 THR B C 3284 O O . THR B 93 ? 0.8790 0.8380 0.9205 -0.0104 -0.0104 -0.0424 93 THR B O 3285 C CB . THR B 93 ? 0.8947 0.8178 0.8841 -0.0156 -0.0202 -0.0550 93 THR B CB 3286 O OG1 . THR B 93 ? 0.9118 0.8073 0.8805 0.0004 -0.0196 -0.0672 93 THR B OG1 3287 C CG2 . THR B 93 ? 0.9350 0.8280 0.9014 -0.0338 -0.0346 -0.0527 93 THR B CG2 3288 N N . TYR B 94 ? 0.8501 0.8542 0.8933 -0.0158 -0.0072 -0.0314 94 TYR B N 3289 C CA . TYR B 94 ? 0.8074 0.8436 0.8622 -0.0175 -0.0069 -0.0197 94 TYR B CA 3290 C C . TYR B 94 ? 0.8266 0.8561 0.8948 -0.0006 0.0021 -0.0217 94 TYR B C 3291 O O . TYR B 94 ? 0.8386 0.8713 0.9123 -0.0025 -0.0004 -0.0184 94 TYR B O 3292 C CB . TYR B 94 ? 0.7765 0.8586 0.8326 -0.0141 -0.0042 -0.0085 94 TYR B CB 3293 C CG . TYR B 94 ? 0.7662 0.8886 0.8307 -0.0032 -0.0008 0.0035 94 TYR B CG 3294 C CD1 . TYR B 94 ? 0.7424 0.8578 0.8068 0.0238 0.0101 0.0031 94 TYR B CD1 3295 C CD2 . TYR B 94 ? 0.7368 0.9036 0.8024 -0.0199 -0.0094 0.0162 94 TYR B CD2 3296 C CE1 . TYR B 94 ? 0.7314 0.8782 0.7941 0.0411 0.0129 0.0131 94 TYR B CE1 3297 C CE2 . TYR B 94 ? 0.7344 0.9476 0.8062 -0.0045 -0.0055 0.0280 94 TYR B CE2 3298 C CZ . TYR B 94 ? 0.7386 0.9395 0.8077 0.0298 0.0060 0.0254 94 TYR B CZ 3299 O OH . TYR B 94 ? 0.7559 0.9974 0.8222 0.0521 0.0096 0.0361 94 TYR B OH 3300 N N . ASN B 95 ? 0.8399 0.8585 0.9091 0.0127 0.0114 -0.0263 95 ASN B N 3301 C CA . ASN B 95 ? 0.8387 0.8440 0.9119 0.0223 0.0178 -0.0279 95 ASN B CA 3302 C C . ASN B 95 ? 0.8474 0.8372 0.9285 0.0177 0.0146 -0.0347 95 ASN B C 3303 O O . ASN B 95 ? 0.8682 0.8561 0.9536 0.0203 0.0150 -0.0329 95 ASN B O 3304 C CB . ASN B 95 ? 0.8480 0.8393 0.9137 0.0278 0.0257 -0.0307 95 ASN B CB 3305 C CG . ASN B 95 ? 0.9108 0.9064 0.9604 0.0393 0.0302 -0.0229 95 ASN B CG 3306 O OD1 . ASN B 95 ? 0.8985 0.9164 0.9449 0.0478 0.0284 -0.0152 95 ASN B OD1 3307 N ND2 . ASN B 95 ? 0.9582 0.9357 0.9943 0.0408 0.0358 -0.0236 95 ASN B ND2 3308 N N . ALA B 96 ? 0.8662 0.8444 0.9450 0.0147 0.0116 -0.0426 96 ALA B N 3309 C CA . ALA B 96 ? 0.8593 0.8249 0.9406 0.0169 0.0089 -0.0491 96 ALA B CA 3310 C C . ALA B 96 ? 0.8311 0.7896 0.9095 0.0097 0.0003 -0.0453 96 ALA B C 3311 O O . ALA B 96 ? 0.8645 0.8226 0.9509 0.0120 0.0005 -0.0449 96 ALA B O 3312 C CB . ALA B 96 ? 0.8847 0.8387 0.9539 0.0235 0.0070 -0.0581 96 ALA B CB 3313 N N . GLU B 97 ? 0.8559 0.8110 0.9208 -0.0024 -0.0081 -0.0412 97 GLU B N 3314 C CA . GLU B 97 ? 0.9160 0.8632 0.9716 -0.0163 -0.0184 -0.0355 97 GLU B CA 3315 C C . GLU B 97 ? 0.8836 0.8629 0.9572 -0.0161 -0.0151 -0.0255 97 GLU B C 3316 O O . GLU B 97 ? 0.9021 0.8760 0.9768 -0.0192 -0.0189 -0.0234 97 GLU B O 3317 C CB . GLU B 97 ? 0.9566 0.8961 0.9880 -0.0377 -0.0301 -0.0306 97 GLU B CB 3318 C CG . GLU B 97 ? 1.0429 0.9330 1.0424 -0.0351 -0.0366 -0.0422 97 GLU B CG 3319 C CD . GLU B 97 ? 1.1602 1.0239 1.1214 -0.0618 -0.0524 -0.0383 97 GLU B CD 3320 O OE1 . GLU B 97 ? 1.2674 1.1650 1.2327 -0.0867 -0.0579 -0.0245 97 GLU B OE1 3321 O OE2 . GLU B 97 ? 1.2650 1.0746 1.1869 -0.0580 -0.0601 -0.0484 97 GLU B OE2 3322 N N . LEU B 98 ? 0.8618 0.8718 0.9446 -0.0084 -0.0077 -0.0197 98 LEU B N 3323 C CA . LEU B 98 ? 0.8569 0.8968 0.9475 -0.0004 -0.0043 -0.0104 98 LEU B CA 3324 C C . LEU B 98 ? 0.8348 0.8554 0.9312 0.0128 0.0013 -0.0165 98 LEU B C 3325 O O . LEU B 98 ? 0.8755 0.9047 0.9755 0.0150 0.0000 -0.0123 98 LEU B O 3326 C CB . LEU B 98 ? 0.8913 0.9609 0.9790 0.0127 0.0020 -0.0036 98 LEU B CB 3327 C CG . LEU B 98 ? 0.9139 1.0209 1.0006 0.0283 0.0048 0.0077 98 LEU B CG 3328 C CD1 . LEU B 98 ? 0.9133 1.0698 1.0046 0.0099 -0.0038 0.0211 98 LEU B CD1 3329 C CD2 . LEU B 98 ? 0.9206 1.0401 0.9934 0.0529 0.0127 0.0114 98 LEU B CD2 3330 N N . LEU B 99 ? 0.8271 0.8255 0.9228 0.0190 0.0071 -0.0253 99 LEU B N 3331 C CA . LEU B 99 ? 0.8422 0.8246 0.9395 0.0249 0.0109 -0.0301 99 LEU B CA 3332 C C . LEU B 99 ? 0.8365 0.8141 0.9421 0.0203 0.0057 -0.0332 99 LEU B C 3333 O O . LEU B 99 ? 0.8408 0.8188 0.9485 0.0240 0.0056 -0.0316 99 LEU B O 3334 C CB . LEU B 99 ? 0.8809 0.8499 0.9755 0.0236 0.0159 -0.0368 99 LEU B CB 3335 C CG . LEU B 99 ? 0.9412 0.8976 1.0322 0.0215 0.0184 -0.0396 99 LEU B CG 3336 C CD1 . LEU B 99 ? 0.9780 0.9172 1.0490 0.0291 0.0196 -0.0348 99 LEU B CD1 3337 C CD2 . LEU B 99 ? 0.9884 0.9440 1.0758 0.0137 0.0224 -0.0425 99 LEU B CD2 3338 N N . VAL B 100 ? 0.8104 0.7789 0.9148 0.0149 0.0007 -0.0377 100 VAL B N 3339 C CA . VAL B 100 ? 0.7911 0.7474 0.8941 0.0140 -0.0054 -0.0401 100 VAL B CA 3340 C C . VAL B 100 ? 0.7689 0.7336 0.8714 0.0064 -0.0110 -0.0306 100 VAL B C 3341 O O . VAL B 100 ? 0.7251 0.6898 0.8330 0.0099 -0.0115 -0.0303 100 VAL B O 3342 C CB . VAL B 100 ? 0.8181 0.7499 0.9037 0.0143 -0.0116 -0.0463 100 VAL B CB 3343 C CG1 . VAL B 100 ? 0.8254 0.7324 0.8960 0.0135 -0.0207 -0.0464 100 VAL B CG1 3344 C CG2 . VAL B 100 ? 0.8178 0.7540 0.9065 0.0274 -0.0052 -0.0552 100 VAL B CG2 3345 N N . LEU B 101 ? 0.7407 0.7196 0.8367 -0.0055 -0.0155 -0.0216 101 LEU B N 3346 C CA . LEU B 101 ? 0.7545 0.7571 0.8506 -0.0158 -0.0208 -0.0092 101 LEU B CA 3347 C C . LEU B 101 ? 0.7654 0.7914 0.8737 0.0005 -0.0134 -0.0061 101 LEU B C 3348 O O . LEU B 101 ? 0.7720 0.8008 0.8831 0.0006 -0.0157 -0.0032 101 LEU B O 3349 C CB . LEU B 101 ? 0.7725 0.8071 0.8623 -0.0315 -0.0253 0.0026 101 LEU B CB 3350 C CG . LEU B 101 ? 0.8273 0.8358 0.8936 -0.0565 -0.0374 0.0033 101 LEU B CG 3351 C CD1 . LEU B 101 ? 0.8206 0.8771 0.8828 -0.0778 -0.0429 0.0188 101 LEU B CD1 3352 C CD2 . LEU B 101 ? 0.8878 0.8545 0.9331 -0.0702 -0.0485 0.0030 101 LEU B CD2 3353 N N . MET B 102 ? 0.7472 0.7831 0.8558 0.0155 -0.0053 -0.0069 102 MET B N 3354 C CA . MET B 102 ? 0.7764 0.8210 0.8816 0.0345 0.0003 -0.0047 102 MET B CA 3355 C C . MET B 102 ? 0.8043 0.8195 0.9112 0.0378 0.0012 -0.0137 102 MET B C 3356 O O . MET B 102 ? 0.8334 0.8552 0.9387 0.0452 0.0007 -0.0107 102 MET B O 3357 C CB . MET B 102 ? 0.8379 0.8791 0.9290 0.0512 0.0073 -0.0052 102 MET B CB 3358 C CG . MET B 102 ? 0.9071 0.9933 0.9943 0.0572 0.0077 0.0067 102 MET B CG 3359 S SD . MET B 102 ? 1.0401 1.1120 1.1012 0.0836 0.0158 0.0058 102 MET B SD 3360 C CE . MET B 102 ? 1.0850 1.2302 1.1391 0.1054 0.0168 0.0232 102 MET B CE 3361 N N . GLU B 103 ? 0.7876 0.7777 0.8972 0.0323 0.0022 -0.0236 103 GLU B N 3362 C CA . GLU B 103 ? 0.8171 0.7910 0.9283 0.0329 0.0027 -0.0306 103 GLU B CA 3363 C C . GLU B 103 ? 0.7847 0.7616 0.9058 0.0291 -0.0028 -0.0311 103 GLU B C 3364 O O . GLU B 103 ? 0.8023 0.7760 0.9248 0.0318 -0.0031 -0.0336 103 GLU B O 3365 C CB . GLU B 103 ? 0.9043 0.8662 1.0147 0.0277 0.0059 -0.0382 103 GLU B CB 3366 C CG . GLU B 103 ? 1.0006 0.9467 1.0913 0.0301 0.0105 -0.0372 103 GLU B CG 3367 C CD . GLU B 103 ? 1.0813 1.0061 1.1483 0.0382 0.0103 -0.0355 103 GLU B CD 3368 O OE1 . GLU B 103 ? 1.0761 0.9981 1.1454 0.0351 0.0075 -0.0380 103 GLU B OE1 3369 O OE2 . GLU B 103 ? 1.2030 1.1109 1.2436 0.0508 0.0126 -0.0320 103 GLU B OE2 3370 N N . ASN B 104 ? 0.7755 0.7533 0.8969 0.0218 -0.0082 -0.0281 104 ASN B N 3371 C CA . ASN B 104 ? 0.7945 0.7660 0.9147 0.0182 -0.0150 -0.0261 104 ASN B CA 3372 C C . ASN B 104 ? 0.7845 0.7762 0.9070 0.0185 -0.0161 -0.0166 104 ASN B C 3373 O O . ASN B 104 ? 0.7645 0.7536 0.8895 0.0221 -0.0176 -0.0175 104 ASN B O 3374 C CB . ASN B 104 ? 0.8266 0.7798 0.9316 0.0066 -0.0232 -0.0238 104 ASN B CB 3375 C CG . ASN B 104 ? 0.8280 0.7564 0.9239 0.0143 -0.0234 -0.0347 104 ASN B CG 3376 O OD1 . ASN B 104 ? 0.8198 0.7563 0.9263 0.0261 -0.0172 -0.0422 104 ASN B OD1 3377 N ND2 . ASN B 104 ? 0.8637 0.7639 0.9355 0.0070 -0.0311 -0.0347 104 ASN B ND2 3378 N N . GLU B 105 ? 0.7724 0.7909 0.8933 0.0170 -0.0150 -0.0069 105 GLU B N 3379 C CA . GLU B 105 ? 0.7902 0.8398 0.9116 0.0237 -0.0143 0.0030 105 GLU B CA 3380 C C . GLU B 105 ? 0.7516 0.7883 0.8706 0.0416 -0.0093 -0.0043 105 GLU B C 3381 O O . GLU B 105 ? 0.7461 0.7880 0.8663 0.0450 -0.0111 -0.0023 105 GLU B O 3382 C CB . GLU B 105 ? 0.8692 0.9598 0.9869 0.0289 -0.0115 0.0139 105 GLU B CB 3383 C CG . GLU B 105 ? 0.9805 1.1221 1.0982 0.0332 -0.0126 0.0288 105 GLU B CG 3384 C CD . GLU B 105 ? 1.1492 1.3474 1.2672 0.0205 -0.0156 0.0451 105 GLU B CD 3385 O OE1 . GLU B 105 ? 1.3551 1.5828 1.4680 0.0401 -0.0095 0.0484 105 GLU B OE1 3386 O OE2 . GLU B 105 ? 1.1795 1.3923 1.2980 -0.0101 -0.0250 0.0555 105 GLU B OE2 3387 N N . ARG B 106 ? 0.7747 0.7904 0.8854 0.0502 -0.0041 -0.0124 106 ARG B N 3388 C CA . ARG B 106 ? 0.8188 0.8126 0.9152 0.0617 -0.0018 -0.0186 106 ARG B CA 3389 C C . ARG B 106 ? 0.7951 0.7763 0.9017 0.0524 -0.0050 -0.0258 106 ARG B C 3390 O O . ARG B 106 ? 0.8310 0.8055 0.9296 0.0579 -0.0062 -0.0276 106 ARG B O 3391 C CB . ARG B 106 ? 0.8683 0.8340 0.9431 0.0672 0.0022 -0.0237 106 ARG B CB 3392 C CG . ARG B 106 ? 0.9500 0.9287 1.0072 0.0859 0.0058 -0.0161 106 ARG B CG 3393 C CD . ARG B 106 ? 1.1171 1.0513 1.1349 0.0988 0.0086 -0.0206 106 ARG B CD 3394 N NE . ARG B 106 ? 1.2302 1.1434 1.2089 0.1252 0.0085 -0.0197 106 ARG B NE 3395 C CZ . ARG B 106 ? 1.2862 1.1516 1.2354 0.1243 0.0050 -0.0269 106 ARG B CZ 3396 N NH1 . ARG B 106 ? 1.3353 1.1792 1.2945 0.0955 0.0015 -0.0342 106 ARG B NH1 3397 N NH2 . ARG B 106 ? 1.3933 1.2349 1.2982 0.1536 0.0044 -0.0261 106 ARG B NH2 3398 N N . THR B 107 ? 0.7886 0.7685 0.9091 0.0414 -0.0068 -0.0298 107 THR B N 3399 C CA . THR B 107 ? 0.7668 0.7443 0.8952 0.0382 -0.0094 -0.0357 107 THR B CA 3400 C C . THR B 107 ? 0.7642 0.7495 0.8965 0.0411 -0.0138 -0.0309 107 THR B C 3401 O O . THR B 107 ? 0.7262 0.7125 0.8590 0.0438 -0.0150 -0.0337 107 THR B O 3402 C CB . THR B 107 ? 0.7594 0.7367 0.8949 0.0347 -0.0099 -0.0406 107 THR B CB 3403 O OG1 . THR B 107 ? 0.7462 0.7228 0.8794 0.0301 -0.0055 -0.0449 107 THR B OG1 3404 C CG2 . THR B 107 ? 0.7790 0.7633 0.9201 0.0391 -0.0129 -0.0446 107 THR B CG2 3405 N N . LEU B 108 ? 0.7363 0.7279 0.8684 0.0373 -0.0171 -0.0224 108 LEU B N 3406 C CA . LEU B 108 ? 0.7263 0.7245 0.8580 0.0358 -0.0222 -0.0153 108 LEU B CA 3407 C C . LEU B 108 ? 0.7326 0.7487 0.8628 0.0456 -0.0196 -0.0114 108 LEU B C 3408 O O . LEU B 108 ? 0.6916 0.7088 0.8228 0.0492 -0.0218 -0.0117 108 LEU B O 3409 C CB . LEU B 108 ? 0.7489 0.7494 0.8733 0.0215 -0.0282 -0.0044 108 LEU B CB 3410 C CG . LEU B 108 ? 0.7845 0.7524 0.8967 0.0140 -0.0333 -0.0089 108 LEU B CG 3411 C CD1 . LEU B 108 ? 0.8156 0.7767 0.9093 -0.0077 -0.0426 0.0035 108 LEU B CD1 3412 C CD2 . LEU B 108 ? 0.7902 0.7331 0.8963 0.0249 -0.0359 -0.0174 108 LEU B CD2 3413 N N . ASP B 109 ? 0.7594 0.7874 0.8822 0.0537 -0.0151 -0.0083 109 ASP B N 3414 C CA . ASP B 109 ? 0.7840 0.8217 0.8935 0.0715 -0.0125 -0.0060 109 ASP B CA 3415 C C . ASP B 109 ? 0.7810 0.7873 0.8785 0.0768 -0.0124 -0.0177 109 ASP B C 3416 O O . ASP B 109 ? 0.8131 0.8200 0.8996 0.0874 -0.0135 -0.0174 109 ASP B O 3417 C CB . ASP B 109 ? 0.8681 0.9175 0.9622 0.0864 -0.0076 -0.0016 109 ASP B CB 3418 C CG . ASP B 109 ? 0.9869 1.0852 1.0910 0.0804 -0.0084 0.0135 109 ASP B CG 3419 O OD1 . ASP B 109 ? 0.9722 1.0980 1.0868 0.0678 -0.0131 0.0236 109 ASP B OD1 3420 O OD2 . ASP B 109 ? 1.0198 1.1302 1.1178 0.0862 -0.0051 0.0164 109 ASP B OD2 3421 N N . PHE B 110 ? 0.7305 0.7128 0.8274 0.0670 -0.0119 -0.0269 110 PHE B N 3422 C CA . PHE B 110 ? 0.7252 0.6831 0.8089 0.0619 -0.0138 -0.0360 110 PHE B CA 3423 C C . PHE B 110 ? 0.7381 0.7096 0.8358 0.0585 -0.0178 -0.0371 110 PHE B C 3424 O O . PHE B 110 ? 0.7438 0.7048 0.8258 0.0612 -0.0204 -0.0402 110 PHE B O 3425 C CB . PHE B 110 ? 0.7099 0.6579 0.7969 0.0467 -0.0127 -0.0417 110 PHE B CB 3426 C CG . PHE B 110 ? 0.7295 0.6660 0.8058 0.0316 -0.0161 -0.0483 110 PHE B CG 3427 C CD1 . PHE B 110 ? 0.7818 0.6819 0.8200 0.0295 -0.0194 -0.0511 110 PHE B CD1 3428 C CD2 . PHE B 110 ? 0.7278 0.6908 0.8262 0.0190 -0.0169 -0.0509 110 PHE B CD2 3429 C CE1 . PHE B 110 ? 0.7979 0.6884 0.8214 0.0065 -0.0250 -0.0555 110 PHE B CE1 3430 C CE2 . PHE B 110 ? 0.7298 0.6982 0.8197 0.0002 -0.0207 -0.0542 110 PHE B CE2 3431 C CZ . PHE B 110 ? 0.7369 0.6687 0.7897 -0.0104 -0.0254 -0.0560 110 PHE B CZ 3432 N N . HIS B 111 ? 0.7199 0.7093 0.8404 0.0544 -0.0191 -0.0346 111 HIS B N 3433 C CA . HIS B 111 ? 0.7222 0.7230 0.8525 0.0553 -0.0230 -0.0346 111 HIS B CA 3434 C C . HIS B 111 ? 0.7426 0.7511 0.8678 0.0639 -0.0245 -0.0277 111 HIS B C 3435 O O . HIS B 111 ? 0.7917 0.8032 0.9147 0.0669 -0.0271 -0.0300 111 HIS B O 3436 C CB . HIS B 111 ? 0.7171 0.7207 0.8579 0.0545 -0.0251 -0.0326 111 HIS B CB 3437 C CG . HIS B 111 ? 0.7432 0.7495 0.8891 0.0527 -0.0239 -0.0399 111 HIS B CG 3438 N ND1 . HIS B 111 ? 0.7438 0.7683 0.8941 0.0515 -0.0242 -0.0457 111 HIS B ND1 3439 C CD2 . HIS B 111 ? 0.7534 0.7536 0.8992 0.0524 -0.0226 -0.0413 111 HIS B CD2 3440 C CE1 . HIS B 111 ? 0.7580 0.7948 0.9129 0.0518 -0.0224 -0.0493 111 HIS B CE1 3441 N NE2 . HIS B 111 ? 0.7452 0.7635 0.8963 0.0542 -0.0212 -0.0476 111 HIS B NE2 3442 N N . ASP B 112 ? 0.7058 0.7249 0.8291 0.0671 -0.0231 -0.0181 112 ASP B N 3443 C CA . ASP B 112 ? 0.7157 0.7558 0.8340 0.0761 -0.0237 -0.0087 112 ASP B CA 3444 C C . ASP B 112 ? 0.7400 0.7682 0.8372 0.0912 -0.0222 -0.0151 112 ASP B C 3445 O O . ASP B 112 ? 0.7409 0.7750 0.8332 0.0983 -0.0243 -0.0144 112 ASP B O 3446 C CB . ASP B 112 ? 0.7545 0.8212 0.8727 0.0757 -0.0218 0.0038 112 ASP B CB 3447 C CG . ASP B 112 ? 0.7893 0.8955 0.9076 0.0783 -0.0235 0.0188 112 ASP B CG 3448 O OD1 . ASP B 112 ? 0.8022 0.9091 0.9212 0.0801 -0.0262 0.0194 112 ASP B OD1 3449 O OD2 . ASP B 112 ? 0.8159 0.9598 0.9335 0.0776 -0.0221 0.0315 112 ASP B OD2 3450 N N . SER B 113 ? 0.7517 0.7553 0.8296 0.0955 -0.0196 -0.0217 113 SER B N 3451 C CA . SER B 113 ? 0.7849 0.7572 0.8258 0.1090 -0.0205 -0.0285 113 SER B CA 3452 C C . SER B 113 ? 0.8056 0.7590 0.8414 0.0969 -0.0260 -0.0374 113 SER B C 3453 O O . SER B 113 ? 0.7918 0.7311 0.8020 0.1077 -0.0290 -0.0400 113 SER B O 3454 C CB . SER B 113 ? 0.8213 0.7579 0.8348 0.1110 -0.0185 -0.0335 113 SER B CB 3455 O OG . SER B 113 ? 0.8980 0.7836 0.8632 0.1171 -0.0223 -0.0418 113 SER B OG 3456 N N . ASN B 114 ? 0.7773 0.7350 0.8347 0.0760 -0.0277 -0.0417 114 ASN B N 3457 C CA . ASN B 114 ? 0.7817 0.7372 0.8373 0.0622 -0.0332 -0.0482 114 ASN B CA 3458 C C . ASN B 114 ? 0.7584 0.7378 0.8269 0.0708 -0.0354 -0.0448 114 ASN B C 3459 O O . ASN B 114 ? 0.7718 0.7419 0.8224 0.0691 -0.0403 -0.0492 114 ASN B O 3460 C CB . ASN B 114 ? 0.7898 0.7637 0.8686 0.0435 -0.0334 -0.0509 114 ASN B CB 3461 C CG . ASN B 114 ? 0.8308 0.7823 0.8943 0.0308 -0.0319 -0.0538 114 ASN B CG 3462 O OD1 . ASN B 114 ? 0.8616 0.7712 0.8862 0.0296 -0.0337 -0.0564 114 ASN B OD1 3463 N ND2 . ASN B 114 ? 0.8182 0.7924 0.9059 0.0236 -0.0290 -0.0533 114 ASN B ND2 3464 N N . VAL B 115 ? 0.6941 0.6995 0.7878 0.0777 -0.0331 -0.0364 115 VAL B N 3465 C CA . VAL B 115 ? 0.6646 0.6899 0.7672 0.0850 -0.0354 -0.0307 115 VAL B CA 3466 C C . VAL B 115 ? 0.6861 0.7100 0.7667 0.1009 -0.0351 -0.0276 115 VAL B C 3467 O O . VAL B 115 ? 0.6775 0.7033 0.7501 0.1055 -0.0385 -0.0297 115 VAL B O 3468 C CB . VAL B 115 ? 0.6504 0.6918 0.7713 0.0843 -0.0349 -0.0201 115 VAL B CB 3469 C CG1 . VAL B 115 ? 0.6737 0.7311 0.7958 0.0902 -0.0378 -0.0115 115 VAL B CG1 3470 C CG2 . VAL B 115 ? 0.6711 0.7089 0.8048 0.0771 -0.0364 -0.0236 115 VAL B CG2 3471 N N . LYS B 116 ? 0.6962 0.7218 0.7656 0.1124 -0.0309 -0.0221 116 LYS B N 3472 C CA . LYS B 116 ? 0.7566 0.7858 0.7985 0.1361 -0.0295 -0.0188 116 LYS B CA 3473 C C . LYS B 116 ? 0.7896 0.7743 0.7914 0.1423 -0.0338 -0.0316 116 LYS B C 3474 O O . LYS B 116 ? 0.8129 0.7982 0.7956 0.1574 -0.0359 -0.0318 116 LYS B O 3475 C CB . LYS B 116 ? 0.8016 0.8412 0.8324 0.1508 -0.0240 -0.0123 116 LYS B CB 3476 C CG . LYS B 116 ? 0.8665 0.9205 0.8650 0.1845 -0.0213 -0.0072 116 LYS B CG 3477 C CD . LYS B 116 ? 0.9025 1.0058 0.9166 0.1896 -0.0217 0.0045 116 LYS B CD 3478 C CE . LYS B 116 ? 0.9718 1.1075 0.9561 0.2275 -0.0176 0.0124 116 LYS B CE 3479 N NZ . LYS B 116 ? 0.9994 1.1808 0.9886 0.2372 -0.0120 0.0250 116 LYS B NZ 3480 N N . ASN B 117 ? 0.8367 0.7810 0.8220 0.1275 -0.0362 -0.0415 117 ASN B N 3481 C CA . ASN B 117 ? 0.8874 0.7780 0.8237 0.1240 -0.0432 -0.0527 117 ASN B CA 3482 C C . ASN B 117 ? 0.8854 0.7850 0.8309 0.1065 -0.0501 -0.0571 117 ASN B C 3483 O O . ASN B 117 ? 0.9404 0.8063 0.8440 0.1097 -0.0568 -0.0635 117 ASN B O 3484 C CB . ASN B 117 ? 0.8934 0.7400 0.8063 0.1058 -0.0451 -0.0591 117 ASN B CB 3485 C CG . ASN B 117 ? 0.9412 0.7628 0.8233 0.1303 -0.0401 -0.0568 117 ASN B CG 3486 O OD1 . ASN B 117 ? 0.9780 0.8073 0.8411 0.1641 -0.0368 -0.0523 117 ASN B OD1 3487 N ND2 . ASN B 117 ? 1.0032 0.8012 0.8792 0.1158 -0.0394 -0.0588 117 ASN B ND2 3488 N N . LEU B 118 ? 0.8302 0.7731 0.8248 0.0909 -0.0490 -0.0536 118 LEU B N 3489 C CA . LEU B 118 ? 0.8516 0.8167 0.8599 0.0797 -0.0544 -0.0557 118 LEU B CA 3490 C C . LEU B 118 ? 0.8749 0.8565 0.8828 0.1010 -0.0542 -0.0507 118 LEU B C 3491 O O . LEU B 118 ? 0.8991 0.8728 0.8868 0.1003 -0.0603 -0.0554 118 LEU B O 3492 C CB . LEU B 118 ? 0.8292 0.8354 0.8829 0.0686 -0.0523 -0.0523 118 LEU B CB 3493 C CG . LEU B 118 ? 0.8664 0.9057 0.9361 0.0591 -0.0573 -0.0539 118 LEU B CG 3494 C CD1 . LEU B 118 ? 0.9200 0.9477 0.9629 0.0343 -0.0654 -0.0616 118 LEU B CD1 3495 C CD2 . LEU B 118 ? 0.8733 0.9460 0.9775 0.0587 -0.0539 -0.0504 118 LEU B CD2 3496 N N . TYR B 119 ? 0.8597 0.8666 0.8875 0.1171 -0.0479 -0.0401 119 TYR B N 3497 C CA . TYR B 119 ? 0.8619 0.8913 0.8878 0.1361 -0.0471 -0.0324 119 TYR B CA 3498 C C . TYR B 119 ? 0.9284 0.9268 0.9046 0.1558 -0.0494 -0.0386 119 TYR B C 3499 O O . TYR B 119 ? 0.9654 0.9689 0.9293 0.1651 -0.0527 -0.0394 119 TYR B O 3500 C CB . TYR B 119 ? 0.8378 0.9012 0.8847 0.1440 -0.0410 -0.0176 119 TYR B CB 3501 C CG . TYR B 119 ? 0.8509 0.9492 0.8968 0.1599 -0.0401 -0.0059 119 TYR B CG 3502 C CD1 . TYR B 119 ? 0.8301 0.9489 0.8951 0.1526 -0.0432 0.0003 119 TYR B CD1 3503 C CD2 . TYR B 119 ? 0.8651 0.9795 0.8877 0.1849 -0.0360 0.0000 119 TYR B CD2 3504 C CE1 . TYR B 119 ? 0.8579 1.0111 0.9212 0.1642 -0.0426 0.0126 119 TYR B CE1 3505 C CE2 . TYR B 119 ? 0.8697 1.0279 0.8924 0.1995 -0.0347 0.0125 119 TYR B CE2 3506 C CZ . TYR B 119 ? 0.8819 1.0586 0.9259 0.1863 -0.0382 0.0190 119 TYR B CZ 3507 O OH . TYR B 119 ? 0.9228 1.1447 0.9659 0.1978 -0.0372 0.0330 119 TYR B OH 3508 N N . ASP B 120 ? 0.9737 0.9344 0.9147 0.1648 -0.0481 -0.0435 120 ASP B N 3509 C CA . ASP B 120 ? 1.0830 0.9994 0.9612 0.1902 -0.0512 -0.0503 120 ASP B CA 3510 C C . ASP B 120 ? 1.1076 0.9712 0.9465 0.1718 -0.0625 -0.0639 120 ASP B C 3511 O O . ASP B 120 ? 1.1766 1.0155 0.9727 0.1892 -0.0674 -0.0686 120 ASP B O 3512 C CB . ASP B 120 ? 1.1614 1.0447 1.0027 0.2098 -0.0474 -0.0511 120 ASP B CB 3513 C CG . ASP B 120 ? 1.1825 1.1272 1.0480 0.2362 -0.0374 -0.0360 120 ASP B CG 3514 O OD1 . ASP B 120 ? 1.2300 1.2238 1.1069 0.2539 -0.0348 -0.0264 120 ASP B OD1 3515 O OD2 . ASP B 120 ? 1.2361 1.1851 1.1083 0.2372 -0.0325 -0.0322 120 ASP B OD2 3516 N N . LYS B 121 ? 1.1223 0.9735 0.9738 0.1354 -0.0672 -0.0691 121 LYS B N 3517 C CA . LYS B 121 ? 1.1937 1.0083 1.0115 0.1077 -0.0795 -0.0792 121 LYS B CA 3518 C C . LYS B 121 ? 1.1778 1.0254 1.0092 0.1104 -0.0832 -0.0786 121 LYS B C 3519 O O . LYS B 121 ? 1.2942 1.1010 1.0750 0.1064 -0.0933 -0.0867 121 LYS B O 3520 C CB . LYS B 121 ? 1.2463 1.0790 1.0953 0.0677 -0.0817 -0.0797 121 LYS B CB 3521 C CG . LYS B 121 ? 1.3750 1.1806 1.1891 0.0287 -0.0954 -0.0871 121 LYS B CG 3522 C CD . LYS B 121 ? 1.4383 1.2853 1.2922 -0.0059 -0.0950 -0.0840 121 LYS B CD 3523 C CE . LYS B 121 ? 1.5689 1.4025 1.3884 -0.0530 -0.1094 -0.0879 121 LYS B CE 3524 N NZ . LYS B 121 ? 1.6126 1.4819 1.4379 -0.0613 -0.1169 -0.0888 121 LYS B NZ 3525 N N . VAL B 122 ? 1.0678 0.9828 0.9611 0.1170 -0.0759 -0.0689 122 VAL B N 3526 C CA . VAL B 122 ? 1.0426 0.9938 0.9533 0.1216 -0.0784 -0.0662 122 VAL B CA 3527 C C . VAL B 122 ? 1.0697 1.0159 0.9530 0.1566 -0.0761 -0.0633 122 VAL B C 3528 O O . VAL B 122 ? 1.1080 1.0445 0.9646 0.1617 -0.0826 -0.0681 122 VAL B O 3529 C CB . VAL B 122 ? 0.9830 0.9959 0.9581 0.1176 -0.0726 -0.0560 122 VAL B CB 3530 C CG1 . VAL B 122 ? 0.9726 1.0198 0.9618 0.1268 -0.0746 -0.0514 122 VAL B CG1 3531 C CG2 . VAL B 122 ? 0.9738 0.9995 0.9708 0.0894 -0.0752 -0.0594 122 VAL B CG2 3532 N N . ARG B 123 ? 1.0534 1.0136 0.9427 0.1811 -0.0670 -0.0547 123 ARG B N 3533 C CA . ARG B 123 ? 1.1005 1.0692 0.9623 0.2181 -0.0638 -0.0499 123 ARG B CA 3534 C C . ARG B 123 ? 1.2166 1.1146 0.9993 0.2341 -0.0721 -0.0641 123 ARG B C 3535 O O . ARG B 123 ? 1.2413 1.1399 0.9975 0.2544 -0.0750 -0.0655 123 ARG B O 3536 C CB . ARG B 123 ? 1.0854 1.0825 0.9575 0.2395 -0.0538 -0.0384 123 ARG B CB 3537 C CG . ARG B 123 ? 1.1303 1.1662 0.9859 0.2785 -0.0486 -0.0282 123 ARG B CG 3538 C CD . ARG B 123 ? 1.1480 1.2300 1.0187 0.2948 -0.0392 -0.0139 123 ARG B CD 3539 N NE . ARG B 123 ? 1.2314 1.2639 1.0706 0.3009 -0.0385 -0.0225 123 ARG B NE 3540 C CZ . ARG B 123 ? 1.2920 1.2690 1.0606 0.3349 -0.0404 -0.0325 123 ARG B CZ 3541 N NH1 . ARG B 123 ? 1.3402 1.3028 1.0591 0.3689 -0.0430 -0.0365 123 ARG B NH1 3542 N NH2 . ARG B 123 ? 1.3310 1.2605 1.0719 0.3368 -0.0402 -0.0387 123 ARG B NH2 3543 N N . LEU B 124 ? 1.2808 1.1117 1.0198 0.2237 -0.0770 -0.0744 124 LEU B N 3544 C CA . LEU B 124 ? 1.4188 1.1595 1.0647 0.2363 -0.0874 -0.0882 124 LEU B CA 3545 C C . LEU B 124 ? 1.4595 1.1704 1.0791 0.2088 -0.1013 -0.0982 124 LEU B C 3546 O O . LEU B 124 ? 1.5373 1.1750 1.0748 0.2219 -0.1115 -0.1089 124 LEU B O 3547 C CB . LEU B 124 ? 1.4889 1.1583 1.0905 0.2244 -0.0910 -0.0951 124 LEU B CB 3548 C CG . LEU B 124 ? 1.5227 1.2036 1.1247 0.2598 -0.0793 -0.0877 124 LEU B CG 3549 C CD1 . LEU B 124 ? 1.5455 1.1758 1.1305 0.2361 -0.0814 -0.0917 124 LEU B CD1 3550 C CD2 . LEU B 124 ? 1.6004 1.2470 1.1277 0.3187 -0.0783 -0.0898 124 LEU B CD2 3551 N N . GLN B 125 ? 1.4254 1.1912 1.1089 0.1721 -0.1024 -0.0945 125 GLN B N 3552 C CA . GLN B 125 ? 1.4328 1.1941 1.1035 0.1452 -0.1147 -0.1011 125 GLN B CA 3553 C C . GLN B 125 ? 1.4274 1.2340 1.1152 0.1723 -0.1117 -0.0964 125 GLN B C 3554 O O . GLN B 125 ? 1.5288 1.2988 1.1637 0.1771 -0.1217 -0.1046 125 GLN B O 3555 C CB . GLN B 125 ? 1.3995 1.2134 1.1308 0.1011 -0.1164 -0.0976 125 GLN B CB 3556 C CG . GLN B 125 ? 1.4717 1.2426 1.1759 0.0610 -0.1244 -0.1032 125 GLN B CG 3557 C CD . GLN B 125 ? 1.4896 1.3268 1.2479 0.0209 -0.1273 -0.0992 125 GLN B CD 3558 O OE1 . GLN B 125 ? 1.6164 1.4575 1.3548 -0.0101 -0.1400 -0.1030 125 GLN B OE1 3559 N NE2 . GLN B 125 ? 1.4214 1.3156 1.2456 0.0235 -0.1159 -0.0909 125 GLN B NE2 3560 N N . LEU B 126 ? 1.3638 1.2460 1.1206 0.1875 -0.0991 -0.0826 126 LEU B N 3561 C CA . LEU B 126 ? 1.3556 1.2898 1.1366 0.2068 -0.0961 -0.0748 126 LEU B CA 3562 C C . LEU B 126 ? 1.4664 1.3804 1.1947 0.2510 -0.0943 -0.0756 126 LEU B C 3563 O O . LEU B 126 ? 1.5564 1.4725 1.2628 0.2626 -0.0993 -0.0783 126 LEU B O 3564 C CB . LEU B 126 ? 1.2427 1.2507 1.0986 0.2075 -0.0850 -0.0582 126 LEU B CB 3565 C CG . LEU B 126 ? 1.1655 1.1994 1.0721 0.1744 -0.0856 -0.0564 126 LEU B CG 3566 C CD1 . LEU B 126 ? 1.1269 1.2181 1.0879 0.1800 -0.0779 -0.0404 126 LEU B CD1 3567 C CD2 . LEU B 126 ? 1.1716 1.2035 1.0707 0.1493 -0.0967 -0.0654 126 LEU B CD2 3568 N N . ARG B 127 ? 1.5707 1.4707 1.2774 0.2787 -0.0871 -0.0726 127 ARG B N 3569 C CA . ARG B 127 ? 1.6994 1.5813 1.3459 0.3293 -0.0849 -0.0735 127 ARG B CA 3570 C C . ARG B 127 ? 1.6507 1.6143 1.3322 0.3528 -0.0777 -0.0589 127 ARG B C 3571 O O . ARG B 127 ? 1.5426 1.5813 1.2899 0.3462 -0.0682 -0.0415 127 ARG B O 3572 C CB . ARG B 127 ? 1.8555 1.6355 1.4054 0.3344 -0.0996 -0.0932 127 ARG B CB 3573 C CG . ARG B 127 ? 1.9141 1.6128 1.4284 0.2968 -0.1098 -0.1056 127 ARG B CG 3574 C CD . ARG B 127 ? 2.0261 1.6158 1.4293 0.3260 -0.1174 -0.1184 127 ARG B CD 3575 N NE . ARG B 127 ? 2.1763 1.6811 1.4900 0.3245 -0.1343 -0.1335 127 ARG B NE 3576 C CZ . ARG B 127 ? 2.2802 1.7135 1.5516 0.2728 -0.1518 -0.1449 127 ARG B CZ 3577 N NH1 . ARG B 127 ? 2.2610 1.7062 1.5767 0.2198 -0.1536 -0.1424 127 ARG B NH1 3578 N NH2 . ARG B 127 ? 2.3654 1.7181 1.5470 0.2722 -0.1684 -0.1580 127 ARG B NH2 3579 N N . ASP B 128 ? 1.7107 1.6564 1.3440 0.3771 -0.0832 -0.0652 128 ASP B N 3580 C CA . ASP B 128 ? 1.6629 1.6859 1.3239 0.3992 -0.0769 -0.0509 128 ASP B CA 3581 C C . ASP B 128 ? 1.5794 1.6421 1.2979 0.3631 -0.0803 -0.0460 128 ASP B C 3582 O O . ASP B 128 ? 1.5563 1.6870 1.3078 0.3731 -0.0748 -0.0307 128 ASP B O 3583 C CB . ASP B 128 ? 1.8020 1.7945 1.3830 0.4493 -0.0802 -0.0588 128 ASP B CB 3584 C CG . ASP B 128 ? 1.9363 1.8170 1.4359 0.4407 -0.0966 -0.0832 128 ASP B CG 3585 O OD1 . ASP B 128 ? 1.9854 1.7976 1.4630 0.4132 -0.1035 -0.0942 128 ASP B OD1 3586 O OD2 . ASP B 128 ? 2.0120 1.8722 1.4652 0.4593 -0.1037 -0.0905 128 ASP B OD2 3587 N N . ASN B 129 ? 1.5540 1.5798 1.2827 0.3224 -0.0894 -0.0572 129 ASN B N 3588 C CA . ASN B 129 ? 1.5098 1.5707 1.2820 0.2948 -0.0938 -0.0543 129 ASN B CA 3589 C C . ASN B 129 ? 1.3937 1.5179 1.2423 0.2762 -0.0861 -0.0372 129 ASN B C 3590 O O . ASN B 129 ? 1.3289 1.4803 1.2091 0.2594 -0.0893 -0.0339 129 ASN B O 3591 C CB . ASN B 129 ? 1.5867 1.5979 1.3380 0.2588 -0.1072 -0.0709 129 ASN B CB 3592 C CG . ASN B 129 ? 1.7533 1.6875 1.4171 0.2680 -0.1193 -0.0882 129 ASN B CG 3593 O OD1 . ASN B 129 ? 1.9263 1.8227 1.5350 0.3050 -0.1171 -0.0915 129 ASN B OD1 3594 N ND2 . ASN B 129 ? 1.7527 1.6622 1.3967 0.2349 -0.1333 -0.0990 129 ASN B ND2 3595 N N . ALA B 130 ? 1.3013 1.4439 1.1728 0.2799 -0.0770 -0.0266 130 ALA B N 3596 C CA . ALA B 130 ? 1.2097 1.3983 1.1395 0.2622 -0.0714 -0.0101 130 ALA B CA 3597 C C . ALA B 130 ? 1.1494 1.3786 1.0888 0.2780 -0.0620 0.0074 130 ALA B C 3598 O O . ALA B 130 ? 1.1851 1.4026 1.0945 0.2993 -0.0585 0.0042 130 ALA B O 3599 C CB . ALA B 130 ? 1.1957 1.3601 1.1478 0.2336 -0.0732 -0.0170 130 ALA B CB 3600 N N . LYS B 131 ? 1.0977 1.3744 1.0731 0.2670 -0.0589 0.0271 131 LYS B N 3601 C CA . LYS B 131 ? 1.0965 1.4206 1.0844 0.2702 -0.0517 0.0472 131 LYS B CA 3602 C C . LYS B 131 ? 1.0343 1.3413 1.0436 0.2475 -0.0501 0.0477 131 LYS B C 3603 O O . LYS B 131 ? 0.9792 1.2627 1.0099 0.2232 -0.0539 0.0452 131 LYS B O 3604 C CB . LYS B 131 ? 1.1643 1.5403 1.1725 0.2600 -0.0514 0.0705 131 LYS B CB 3605 C CG . LYS B 131 ? 1.2357 1.6700 1.2560 0.2526 -0.0460 0.0951 131 LYS B CG 3606 C CD . LYS B 131 ? 1.3186 1.8231 1.3342 0.2635 -0.0437 0.1167 131 LYS B CD 3607 C CE . LYS B 131 ? 1.3666 1.8747 1.3962 0.2359 -0.0495 0.1319 131 LYS B CE 3608 N NZ . LYS B 131 ? 1.3900 1.8515 1.4146 0.2422 -0.0549 0.1146 131 LYS B NZ 3609 N N . GLU B 132 ? 1.0267 1.3476 1.0267 0.2596 -0.0445 0.0511 132 GLU B N 3610 C CA . GLU B 132 ? 1.0060 1.3163 1.0246 0.2396 -0.0427 0.0529 132 GLU B CA 3611 C C . GLU B 132 ? 0.9779 1.3377 1.0228 0.2163 -0.0419 0.0783 132 GLU B C 3612 O O . GLU B 132 ? 0.9883 1.4095 1.0306 0.2249 -0.0378 0.0964 132 GLU B O 3613 C CB . GLU B 132 ? 1.0400 1.3459 1.0331 0.2640 -0.0376 0.0470 132 GLU B CB 3614 C CG . GLU B 132 ? 1.0457 1.3260 1.0521 0.2459 -0.0364 0.0428 132 GLU B CG 3615 C CD . GLU B 132 ? 1.0716 1.3500 1.0485 0.2739 -0.0312 0.0391 132 GLU B CD 3616 O OE1 . GLU B 132 ? 1.1026 1.4101 1.0490 0.3107 -0.0277 0.0431 132 GLU B OE1 3617 O OE2 . GLU B 132 ? 1.0532 1.3017 1.0343 0.2624 -0.0305 0.0326 132 GLU B OE2 3618 N N . LEU B 133 ? 0.9766 1.3093 1.0405 0.1867 -0.0468 0.0802 133 LEU B N 3619 C CA . LEU B 133 ? 0.9735 1.3317 1.0478 0.1593 -0.0499 0.1039 133 LEU B CA 3620 C C . LEU B 133 ? 0.9559 1.3443 1.0361 0.1415 -0.0480 0.1192 133 LEU B C 3621 O O . LEU B 133 ? 0.9372 1.3628 1.0178 0.1176 -0.0510 0.1433 133 LEU B O 3622 C CB . LEU B 133 ? 1.0175 1.3225 1.0962 0.1396 -0.0571 0.0997 133 LEU B CB 3623 C CG . LEU B 133 ? 1.0540 1.3519 1.1270 0.1445 -0.0618 0.1010 133 LEU B CG 3624 C CD1 . LEU B 133 ? 1.0835 1.3907 1.1473 0.1204 -0.0674 0.1264 133 LEU B CD1 3625 C CD2 . LEU B 133 ? 1.0610 1.3888 1.1272 0.1718 -0.0585 0.0947 133 LEU B CD2 3626 N N . GLY B 134 ? 0.9780 1.3501 1.0598 0.1495 -0.0440 0.1065 134 GLY B N 3627 C CA . GLY B 134 ? 0.9533 1.3569 1.0408 0.1345 -0.0420 0.1196 134 GLY B CA 3628 C C . GLY B 134 ? 0.9472 1.3019 1.0419 0.1033 -0.0472 0.1173 134 GLY B C 3629 O O . GLY B 134 ? 0.9603 1.3371 1.0580 0.0849 -0.0474 0.1289 134 GLY B O 3630 N N . ASN B 135 ? 0.9285 1.2208 1.0233 0.0999 -0.0515 0.1024 135 ASN B N 3631 C CA . ASN B 135 ? 0.9417 1.1841 1.0354 0.0760 -0.0573 0.1007 135 ASN B CA 3632 C C . ASN B 135 ? 0.9360 1.1279 1.0349 0.0884 -0.0562 0.0762 135 ASN B C 3633 O O . ASN B 135 ? 0.8817 1.0302 0.9756 0.0779 -0.0611 0.0726 135 ASN B O 3634 C CB . ASN B 135 ? 0.9631 1.1834 1.0411 0.0553 -0.0665 0.1151 135 ASN B CB 3635 C CG . ASN B 135 ? 0.9663 1.1711 1.0422 0.0746 -0.0676 0.1063 135 ASN B CG 3636 O OD1 . ASN B 135 ? 0.9256 1.1451 1.0115 0.0994 -0.0621 0.0919 135 ASN B OD1 3637 N ND2 . ASN B 135 ? 1.0274 1.1982 1.0838 0.0627 -0.0758 0.1153 135 ASN B ND2 3638 N N . GLY B 136 ? 0.9265 1.1237 1.0290 0.1107 -0.0507 0.0607 136 GLY B N 3639 C CA . GLY B 136 ? 0.9062 1.0671 1.0117 0.1179 -0.0508 0.0398 136 GLY B CA 3640 C C . GLY B 136 ? 0.8896 1.0469 0.9923 0.1291 -0.0536 0.0316 136 GLY B C 3641 O O . GLY B 136 ? 0.8553 0.9961 0.9585 0.1328 -0.0542 0.0157 136 GLY B O 3642 N N . CYS B 137 ? 0.9073 1.0844 1.0058 0.1318 -0.0559 0.0434 137 CYS B N 3643 C CA . CYS B 137 ? 0.9278 1.1036 1.0237 0.1416 -0.0593 0.0374 137 CYS B CA 3644 C C . CYS B 137 ? 0.8893 1.0873 0.9743 0.1582 -0.0577 0.0348 137 CYS B C 3645 O O . CYS B 137 ? 0.8585 1.0818 0.9363 0.1660 -0.0537 0.0432 137 CYS B O 3646 C CB . CYS B 137 ? 1.0100 1.1814 1.1017 0.1351 -0.0646 0.0515 137 CYS B CB 3647 S SG . CYS B 137 ? 1.1759 1.3028 1.2623 0.1229 -0.0689 0.0525 137 CYS B SG 3648 N N . PHE B 138 ? 0.8971 1.0888 0.9780 0.1653 -0.0612 0.0236 138 PHE B N 3649 C CA . PHE B 138 ? 0.9354 1.1372 0.9981 0.1812 -0.0618 0.0185 138 PHE B CA 3650 C C . PHE B 138 ? 0.9419 1.1563 1.0070 0.1843 -0.0664 0.0215 138 PHE B C 3651 O O . PHE B 138 ? 0.9439 1.1498 1.0156 0.1792 -0.0707 0.0130 138 PHE B O 3652 C CB . PHE B 138 ? 0.9592 1.1313 1.0040 0.1819 -0.0640 -0.0014 138 PHE B CB 3653 C CG . PHE B 138 ? 0.9888 1.1412 1.0230 0.1826 -0.0598 -0.0054 138 PHE B CG 3654 C CD1 . PHE B 138 ? 0.9904 1.1461 0.9988 0.2039 -0.0560 -0.0029 138 PHE B CD1 3655 C CD2 . PHE B 138 ? 1.0087 1.1424 1.0560 0.1659 -0.0595 -0.0112 138 PHE B CD2 3656 C CE1 . PHE B 138 ? 0.9961 1.1333 0.9902 0.2092 -0.0522 -0.0062 138 PHE B CE1 3657 C CE2 . PHE B 138 ? 0.9944 1.1089 1.0303 0.1671 -0.0557 -0.0144 138 PHE B CE2 3658 C CZ . PHE B 138 ? 1.0066 1.1214 1.0153 0.1891 -0.0522 -0.0118 138 PHE B CZ 3659 N N . GLU B 139 ? 0.9848 1.2264 1.0440 0.1938 -0.0655 0.0348 139 GLU B N 3660 C CA . GLU B 139 ? 1.0521 1.3063 1.1096 0.1993 -0.0698 0.0384 139 GLU B CA 3661 C C . GLU B 139 ? 1.0518 1.3072 1.0888 0.2148 -0.0720 0.0248 139 GLU B C 3662 O O . GLU B 139 ? 1.0808 1.3437 1.0979 0.2301 -0.0688 0.0248 139 GLU B O 3663 C CB . GLU B 139 ? 1.1136 1.3961 1.1715 0.1976 -0.0686 0.0618 139 GLU B CB 3664 C CG . GLU B 139 ? 1.2123 1.5042 1.2662 0.2026 -0.0731 0.0683 139 GLU B CG 3665 C CD . GLU B 139 ? 1.3326 1.6533 1.3812 0.1964 -0.0727 0.0936 139 GLU B CD 3666 O OE1 . GLU B 139 ? 1.3598 1.7168 1.4061 0.1984 -0.0678 0.1040 139 GLU B OE1 3667 O OE2 . GLU B 139 ? 1.4885 1.7979 1.5315 0.1900 -0.0777 0.1046 139 GLU B OE2 3668 N N . PHE B 140 ? 1.0376 1.2864 1.0741 0.2121 -0.0781 0.0137 140 PHE B N 3669 C CA . PHE B 140 ? 1.0743 1.3160 1.0844 0.2201 -0.0831 -0.0004 140 PHE B CA 3670 C C . PHE B 140 ? 1.1378 1.4055 1.1372 0.2375 -0.0836 0.0082 140 PHE B C 3671 O O . PHE B 140 ? 1.1427 1.4348 1.1593 0.2378 -0.0827 0.0234 140 PHE B O 3672 C CB . PHE B 140 ? 1.0342 1.2723 1.0490 0.2053 -0.0907 -0.0130 140 PHE B CB 3673 C CG . PHE B 140 ? 1.0380 1.2554 1.0577 0.1872 -0.0912 -0.0226 140 PHE B CG 3674 C CD1 . PHE B 140 ? 1.0430 1.2680 1.0914 0.1802 -0.0877 -0.0166 140 PHE B CD1 3675 C CD2 . PHE B 140 ? 1.0797 1.2641 1.0680 0.1770 -0.0960 -0.0374 140 PHE B CD2 3676 C CE1 . PHE B 140 ? 1.0506 1.2623 1.1041 0.1644 -0.0877 -0.0249 140 PHE B CE1 3677 C CE2 . PHE B 140 ? 1.0815 1.2480 1.0723 0.1570 -0.0969 -0.0447 140 PHE B CE2 3678 C CZ . PHE B 140 ? 1.0698 1.2557 1.0971 0.1512 -0.0921 -0.0382 140 PHE B CZ 3679 N N . TYR B 141 ? 1.1948 1.4513 1.1588 0.2527 -0.0858 -0.0014 141 TYR B N 3680 C CA . TYR B 141 ? 1.2427 1.5250 1.1926 0.2718 -0.0867 0.0048 141 TYR B CA 3681 C C . TYR B 141 ? 1.2847 1.5687 1.2334 0.2642 -0.0955 -0.0038 141 TYR B C 3682 O O . TYR B 141 ? 1.3348 1.6495 1.2927 0.2715 -0.0960 0.0067 141 TYR B O 3683 C CB . TYR B 141 ? 1.2443 1.5135 1.1487 0.2987 -0.0854 -0.0016 141 TYR B CB 3684 C CG . TYR B 141 ? 1.2560 1.5470 1.1642 0.3124 -0.0755 0.0118 141 TYR B CG 3685 C CD1 . TYR B 141 ? 1.2541 1.5989 1.1956 0.3080 -0.0692 0.0359 141 TYR B CD1 3686 C CD2 . TYR B 141 ? 1.3102 1.5680 1.1851 0.3270 -0.0737 0.0016 141 TYR B CD2 3687 C CE1 . TYR B 141 ? 1.2729 1.6500 1.2195 0.3149 -0.0613 0.0505 141 TYR B CE1 3688 C CE2 . TYR B 141 ? 1.3106 1.6002 1.1907 0.3413 -0.0645 0.0151 141 TYR B CE2 3689 C CZ . TYR B 141 ? 1.3022 1.6575 1.2211 0.3335 -0.0583 0.0400 141 TYR B CZ 3690 O OH . TYR B 141 ? 1.3013 1.6999 1.2260 0.3427 -0.0502 0.0555 141 TYR B OH 3691 N N . HIS B 142 ? 1.3040 1.5589 1.2396 0.2474 -0.1031 -0.0212 142 HIS B N 3692 C CA . HIS B 142 ? 1.3186 1.5883 1.2585 0.2342 -0.1122 -0.0279 142 HIS B CA 3693 C C . HIS B 142 ? 1.2876 1.5842 1.2702 0.2227 -0.1102 -0.0201 142 HIS B C 3694 O O . HIS B 142 ? 1.2845 1.5729 1.2864 0.2182 -0.1041 -0.0148 142 HIS B O 3695 C CB . HIS B 142 ? 1.3668 1.5998 1.2688 0.2145 -0.1232 -0.0476 142 HIS B CB 3696 C CG . HIS B 142 ? 1.3453 1.5459 1.2455 0.1955 -0.1226 -0.0544 142 HIS B CG 3697 N ND1 . HIS B 142 ? 1.3152 1.5322 1.2384 0.1681 -0.1264 -0.0574 142 HIS B ND1 3698 C CD2 . HIS B 142 ? 1.3598 1.5166 1.2358 0.2019 -0.1185 -0.0580 142 HIS B CD2 3699 C CE1 . HIS B 142 ? 1.3259 1.5077 1.2402 0.1555 -0.1248 -0.0625 142 HIS B CE1 3700 N NE2 . HIS B 142 ? 1.3396 1.4814 1.2245 0.1759 -0.1202 -0.0633 142 HIS B NE2 3701 N N . LYS B 143 ? 1.3051 1.6342 1.2981 0.2215 -0.1158 -0.0193 143 LYS B N 3702 C CA . LYS B 143 ? 1.3158 1.6709 1.3383 0.2164 -0.1157 -0.0151 143 LYS B CA 3703 C C . LYS B 143 ? 1.2878 1.6363 1.3100 0.1917 -0.1195 -0.0280 143 LYS B C 3704 O O . LYS B 143 ? 1.3076 1.6452 1.3034 0.1740 -0.1278 -0.0404 143 LYS B O 3705 C CB . LYS B 143 ? 1.3779 1.7758 1.4048 0.2253 -0.1214 -0.0120 143 LYS B CB 3706 C CG . LYS B 143 ? 1.4418 1.8632 1.4906 0.2392 -0.1189 -0.0011 143 LYS B CG 3707 C CD . LYS B 143 ? 1.4956 1.9713 1.5486 0.2437 -0.1262 -0.0035 143 LYS B CD 3708 C CE . LYS B 143 ? 1.5214 2.0283 1.5837 0.2221 -0.1306 -0.0140 143 LYS B CE 3709 N NZ . LYS B 143 ? 1.5252 2.1035 1.5939 0.2260 -0.1377 -0.0138 143 LYS B NZ 3710 N N . CYS B 144 ? 1.2275 1.5777 1.2723 0.1886 -0.1146 -0.0245 144 CYS B N 3711 C CA . CYS B 144 ? 1.1907 1.5388 1.2373 0.1644 -0.1171 -0.0342 144 CYS B CA 3712 C C . CYS B 144 ? 1.1198 1.5160 1.1931 0.1669 -0.1169 -0.0302 144 CYS B C 3713 O O . CYS B 144 ? 1.0995 1.4884 1.1883 0.1812 -0.1100 -0.0229 144 CYS B O 3714 C CB . CYS B 144 ? 1.2066 1.5075 1.2495 0.1607 -0.1102 -0.0351 144 CYS B CB 3715 S SG . CYS B 144 ? 1.2941 1.5810 1.3333 0.1301 -0.1127 -0.0458 144 CYS B SG 3716 N N . ASP B 145 ? 1.1112 1.5586 1.1849 0.1540 -0.1251 -0.0345 145 ASP B N 3717 C CA . ASP B 145 ? 1.0545 1.5660 1.1507 0.1627 -0.1252 -0.0298 145 ASP B CA 3718 C C . ASP B 145 ? 1.0062 1.5263 1.1128 0.1432 -0.1234 -0.0334 145 ASP B C 3719 O O . ASP B 145 ? 0.9857 1.4560 1.0810 0.1219 -0.1225 -0.0395 145 ASP B O 3720 C CB . ASP B 145 ? 1.0651 1.6450 1.1590 0.1553 -0.1350 -0.0308 145 ASP B CB 3721 C CG . ASP B 145 ? 1.1221 1.7128 1.1982 0.1084 -0.1460 -0.0405 145 ASP B CG 3722 O OD1 . ASP B 145 ? 1.1750 1.7072 1.2336 0.0851 -0.1462 -0.0476 145 ASP B OD1 3723 O OD2 . ASP B 145 ? 1.1903 1.8467 1.2645 0.0935 -0.1556 -0.0403 145 ASP B OD2 3724 N N . ASN B 146 ? 0.9627 1.5484 1.0875 0.1534 -0.1228 -0.0290 146 ASN B N 3725 C CA . ASN B 146 ? 0.9659 1.5685 1.1024 0.1397 -0.1199 -0.0305 146 ASN B CA 3726 C C . ASN B 146 ? 1.0092 1.6119 1.1337 0.0885 -0.1276 -0.0382 146 ASN B C 3727 O O . ASN B 146 ? 1.0002 1.5745 1.1250 0.0726 -0.1243 -0.0409 146 ASN B O 3728 C CB . ASN B 146 ? 0.9205 1.6089 1.0743 0.1650 -0.1185 -0.0236 146 ASN B CB 3729 C CG . ASN B 146 ? 0.9078 1.5695 1.0597 0.2171 -0.1107 -0.0167 146 ASN B CG 3730 O OD1 . ASN B 146 ? 0.8815 1.4618 1.0238 0.2263 -0.1059 -0.0158 146 ASN B OD1 3731 N ND2 . ASN B 146 ? 0.9149 1.6454 1.0697 0.2512 -0.1105 -0.0107 146 ASN B ND2 3732 N N . GLU B 147 ? 1.0913 1.7187 1.1988 0.0613 -0.1391 -0.0414 147 GLU B N 3733 C CA . GLU B 147 ? 1.1957 1.8070 1.2758 0.0073 -0.1500 -0.0482 147 GLU B CA 3734 C C . GLU B 147 ? 1.2064 1.7062 1.2516 -0.0008 -0.1496 -0.0571 147 GLU B C 3735 O O . GLU B 147 ? 1.2088 1.6660 1.2310 -0.0323 -0.1531 -0.0621 147 GLU B O 3736 C CB . GLU B 147 ? 1.3058 1.9720 1.3687 -0.0230 -0.1648 -0.0485 147 GLU B CB 3737 C CG . GLU B 147 ? 1.3617 2.1561 1.4534 -0.0281 -0.1678 -0.0388 147 GLU B CG 3738 C CD . GLU B 147 ? 1.4056 2.2603 1.5253 0.0267 -0.1607 -0.0313 147 GLU B CD 3739 O OE1 . GLU B 147 ? 1.4238 2.2545 1.5324 0.0434 -0.1630 -0.0330 147 GLU B OE1 3740 O OE2 . GLU B 147 ? 1.4285 2.3521 1.5758 0.0556 -0.1532 -0.0234 147 GLU B OE2 3741 N N . CYS B 148 ? 1.1938 1.6503 1.2318 0.0295 -0.1457 -0.0580 148 CYS B N 3742 C CA . CYS B 148 ? 1.2234 1.5887 1.2333 0.0366 -0.1421 -0.0637 148 CYS B CA 3743 C C . CYS B 148 ? 1.1641 1.5020 1.1918 0.0450 -0.1311 -0.0615 148 CYS B C 3744 O O . CYS B 148 ? 1.1954 1.4757 1.1962 0.0287 -0.1320 -0.0675 148 CYS B O 3745 C CB . CYS B 148 ? 1.2487 1.5994 1.2589 0.0724 -0.1376 -0.0604 148 CYS B CB 3746 S SG . CYS B 148 ? 1.4031 1.6726 1.3912 0.0953 -0.1292 -0.0616 148 CYS B SG 3747 N N . MET B 149 ? 1.0498 1.4253 1.1166 0.0710 -0.1218 -0.0530 149 MET B N 3748 C CA . MET B 149 ? 0.9983 1.3517 1.0816 0.0795 -0.1122 -0.0504 149 MET B CA 3749 C C . MET B 149 ? 0.9928 1.3541 1.0731 0.0471 -0.1150 -0.0546 149 MET B C 3750 O O . MET B 149 ? 0.9703 1.2819 1.0406 0.0396 -0.1113 -0.0576 149 MET B O 3751 C CB . MET B 149 ? 0.9811 1.3696 1.0941 0.1117 -0.1051 -0.0411 149 MET B CB 3752 C CG . MET B 149 ? 0.9877 1.3575 1.0999 0.1417 -0.1019 -0.0339 149 MET B CG 3753 S SD . MET B 149 ? 0.9962 1.2954 1.0973 0.1476 -0.0952 -0.0307 149 MET B SD 3754 C CE . MET B 149 ? 0.9367 1.2368 1.0398 0.1771 -0.0932 -0.0171 149 MET B CE 3755 N N . GLU B 150 ? 1.0299 1.4600 1.1180 0.0271 -0.1218 -0.0534 150 GLU B N 3756 C CA . GLU B 150 ? 1.0749 1.5236 1.1587 -0.0098 -0.1258 -0.0547 150 GLU B CA 3757 C C . GLU B 150 ? 1.1063 1.4769 1.1420 -0.0454 -0.1340 -0.0631 150 GLU B C 3758 O O . GLU B 150 ? 1.0584 1.3973 1.0837 -0.0642 -0.1328 -0.0648 150 GLU B O 3759 C CB . GLU B 150 ? 1.1285 1.6797 1.2256 -0.0294 -0.1335 -0.0494 150 GLU B CB 3760 C CG . GLU B 150 ? 1.2136 1.7996 1.3040 -0.0766 -0.1397 -0.0477 150 GLU B CG 3761 C CD . GLU B 150 ? 1.2535 1.8409 1.3664 -0.0641 -0.1286 -0.0452 150 GLU B CD 3762 O OE1 . GLU B 150 ? 1.3274 1.9070 1.4645 -0.0172 -0.1168 -0.0436 150 GLU B OE1 3763 O OE2 . GLU B 150 ? 1.3082 1.9010 1.4097 -0.1038 -0.1328 -0.0442 150 GLU B OE2 3764 N N . SER B 151 ? 1.1507 1.4847 1.1513 -0.0508 -0.1426 -0.0684 151 SER B N 3765 C CA . SER B 151 ? 1.2420 1.4873 1.1800 -0.0778 -0.1524 -0.0775 151 SER B CA 3766 C C . SER B 151 ? 1.2613 1.4279 1.1865 -0.0528 -0.1426 -0.0808 151 SER B C 3767 O O . SER B 151 ? 1.3493 1.4450 1.2261 -0.0730 -0.1480 -0.0868 151 SER B O 3768 C CB . SER B 151 ? 1.2916 1.5114 1.1911 -0.0781 -0.1628 -0.0831 151 SER B CB 3769 O OG . SER B 151 ? 1.2969 1.4787 1.1980 -0.0323 -0.1535 -0.0841 151 SER B OG 3770 N N . VAL B 152 ? 1.1842 1.3626 1.1472 -0.0099 -0.1292 -0.0758 152 VAL B N 3771 C CA . VAL B 152 ? 1.1695 1.2954 1.1295 0.0133 -0.1190 -0.0757 152 VAL B CA 3772 C C . VAL B 152 ? 1.1610 1.2920 1.1397 -0.0001 -0.1139 -0.0738 152 VAL B C 3773 O O . VAL B 152 ? 1.1968 1.2712 1.1502 -0.0014 -0.1117 -0.0770 152 VAL B O 3774 C CB . VAL B 152 ? 1.1259 1.2704 1.1197 0.0536 -0.1081 -0.0678 152 VAL B CB 3775 C CG1 . VAL B 152 ? 1.1272 1.2320 1.1197 0.0719 -0.0985 -0.0654 152 VAL B CG1 3776 C CG2 . VAL B 152 ? 1.1399 1.2805 1.1144 0.0687 -0.1123 -0.0687 152 VAL B CG2 3777 N N . ARG B 153 ? 1.1388 1.3392 1.1587 -0.0060 -0.1118 -0.0683 153 ARG B N 3778 C CA . ARG B 153 ? 1.1833 1.3974 1.2189 -0.0204 -0.1078 -0.0664 153 ARG B CA 3779 C C . ARG B 153 ? 1.2631 1.4614 1.2613 -0.0681 -0.1191 -0.0704 153 ARG B C 3780 O O . ARG B 153 ? 1.2743 1.4481 1.2650 -0.0826 -0.1170 -0.0707 153 ARG B O 3781 C CB . ARG B 153 ? 1.1812 1.4773 1.2635 -0.0073 -0.1028 -0.0594 153 ARG B CB 3782 C CG . ARG B 153 ? 1.1746 1.4756 1.2822 0.0356 -0.0943 -0.0543 153 ARG B CG 3783 C CD . ARG B 153 ? 1.1743 1.5393 1.3128 0.0542 -0.0900 -0.0485 153 ARG B CD 3784 N NE . ARG B 153 ? 1.1783 1.5582 1.3258 0.0881 -0.0885 -0.0435 153 ARG B NE 3785 C CZ . ARG B 153 ? 1.1649 1.6033 1.3176 0.0957 -0.0932 -0.0409 153 ARG B CZ 3786 N NH1 . ARG B 153 ? 1.1626 1.6611 1.3156 0.0686 -0.1003 -0.0421 153 ARG B NH1 3787 N NH2 . ARG B 153 ? 1.1874 1.6257 1.3420 0.1290 -0.0915 -0.0358 153 ARG B NH2 3788 N N . ASN B 154 ? 1.3479 1.5596 1.3196 -0.0955 -0.1322 -0.0724 154 ASN B N 3789 C CA . ASN B 154 ? 1.4042 1.5868 1.3244 -0.1494 -0.1471 -0.0752 154 ASN B CA 3790 C C . ASN B 154 ? 1.4621 1.5298 1.3217 -0.1535 -0.1497 -0.0827 154 ASN B C 3791 O O . ASN B 154 ? 1.5128 1.5482 1.3417 -0.1880 -0.1552 -0.0826 154 ASN B O 3792 C CB . ASN B 154 ? 1.4735 1.6666 1.3612 -0.1751 -0.1625 -0.0774 154 ASN B CB 3793 C CG . ASN B 154 ? 1.4784 1.7916 1.4053 -0.1961 -0.1667 -0.0684 154 ASN B CG 3794 O OD1 . ASN B 154 ? 1.4802 1.8720 1.4602 -0.1819 -0.1566 -0.0608 154 ASN B OD1 3795 N ND2 . ASN B 154 ? 1.5082 1.8383 1.4046 -0.2281 -0.1822 -0.0691 154 ASN B ND2 3796 N N . GLY B 155 ? 1.4754 1.4849 1.3146 -0.1158 -0.1459 -0.0883 155 GLY B N 3797 C CA . GLY B 155 ? 1.5284 1.4266 1.2933 -0.1120 -0.1512 -0.0967 155 GLY B CA 3798 C C . GLY B 155 ? 1.6009 1.4494 1.2990 -0.1277 -0.1676 -0.1041 155 GLY B C 3799 O O . GLY B 155 ? 1.7043 1.4530 1.3274 -0.1165 -0.1737 -0.1124 155 GLY B O 3800 N N . THR B 156 ? 1.5833 1.5015 1.3046 -0.1494 -0.1748 -0.1012 156 THR B N 3801 C CA . THR B 156 ? 1.6454 1.5255 1.3031 -0.1753 -0.1931 -0.1076 156 THR B CA 3802 C C . THR B 156 ? 1.6161 1.5286 1.2991 -0.1345 -0.1880 -0.1086 156 THR B C 3803 O O . THR B 156 ? 1.6283 1.5879 1.3147 -0.1534 -0.1975 -0.1077 156 THR B O 3804 C CB . THR B 156 ? 1.6929 1.6393 1.3540 -0.2385 -0.2077 -0.1016 156 THR B CB 3805 O OG1 . THR B 156 ? 1.6973 1.6560 1.3662 -0.2720 -0.2072 -0.0956 156 THR B OG1 3806 C CG2 . THR B 156 ? 1.8378 1.7112 1.4050 -0.2823 -0.2320 -0.1090 156 THR B CG2 3807 N N . TYR B 157 ? 1.6213 1.5142 1.3213 -0.0801 -0.1734 -0.1090 157 TYR B N 3808 C CA . TYR B 157 ? 1.6105 1.5326 1.3322 -0.0408 -0.1678 -0.1079 157 TYR B CA 3809 C C . TYR B 157 ? 1.7575 1.5909 1.3929 -0.0314 -0.1793 -0.1189 157 TYR B C 3810 O O . TYR B 157 ? 1.7856 1.5407 1.3711 -0.0047 -0.1766 -0.1242 157 TYR B O 3811 C CB . TYR B 157 ? 1.5045 1.4528 1.2802 0.0071 -0.1483 -0.1005 157 TYR B CB 3812 C CG . TYR B 157 ? 1.4377 1.4037 1.2244 0.0479 -0.1424 -0.0977 157 TYR B CG 3813 C CD1 . TYR B 157 ? 1.3605 1.4024 1.1983 0.0537 -0.1399 -0.0904 157 TYR B CD1 3814 C CD2 . TYR B 157 ? 1.4633 1.3739 1.2067 0.0835 -0.1391 -0.1010 157 TYR B CD2 3815 C CE1 . TYR B 157 ? 1.3353 1.3929 1.1811 0.0882 -0.1349 -0.0861 157 TYR B CE1 3816 C CE2 . TYR B 157 ? 1.4427 1.3795 1.1970 0.1194 -0.1333 -0.0962 157 TYR B CE2 3817 C CZ . TYR B 157 ? 1.3628 1.3709 1.1687 0.1189 -0.1315 -0.0885 157 TYR B CZ 3818 O OH . TYR B 157 ? 1.3274 1.3600 1.1411 0.1517 -0.1263 -0.0823 157 TYR B OH 3819 N N . ASP B 158 ? 1.9081 1.7540 1.5214 -0.0505 -0.1923 -0.1223 158 ASP B N 3820 C CA . ASP B 158 ? 2.0893 1.8469 1.6124 -0.0418 -0.2053 -0.1339 158 ASP B CA 3821 C C . ASP B 158 ? 2.1246 1.8841 1.6574 0.0223 -0.1922 -0.1331 158 ASP B C 3822 O O . ASP B 158 ? 2.0336 1.8541 1.6033 0.0383 -0.1892 -0.1289 158 ASP B O 3823 C CB . ASP B 158 ? 2.1009 1.8745 1.5955 -0.0852 -0.2247 -0.1373 158 ASP B CB 3824 C CG . ASP B 158 ? 2.1600 1.8611 1.5741 -0.1486 -0.2466 -0.1434 158 ASP B CG 3825 O OD1 . ASP B 158 ? 2.1261 1.8145 1.5440 -0.1725 -0.2450 -0.1400 158 ASP B OD1 3826 O OD2 . ASP B 158 ? 2.2719 1.9247 1.6133 -0.1771 -0.2667 -0.1510 158 ASP B OD2 3827 N N . TYR B 159 ? 2.2297 1.9272 1.7277 0.0585 -0.1846 -0.1357 159 TYR B N 3828 C CA . TYR B 159 ? 2.2794 1.9804 1.7763 0.1196 -0.1725 -0.1334 159 TYR B CA 3829 C C . TYR B 159 ? 2.4233 2.0943 1.8620 0.1365 -0.1829 -0.1414 159 TYR B C 3830 O O . TYR B 159 ? 2.3664 2.1025 1.8485 0.1662 -0.1739 -0.1341 159 TYR B O 3831 C CB . TYR B 159 ? 2.2934 1.9289 1.7455 0.1536 -0.1656 -0.1357 159 TYR B CB 3832 C CG . TYR B 159 ? 2.3668 1.9641 1.7595 0.2135 -0.1623 -0.1394 159 TYR B CG 3833 C CD1 . TYR B 159 ? 2.2793 1.9566 1.7285 0.2581 -0.1454 -0.1267 159 TYR B CD1 3834 C CD2 . TYR B 159 ? 2.4892 1.9693 1.7619 0.2257 -0.1773 -0.1547 159 TYR B CD2 3835 C CE1 . TYR B 159 ? 2.3101 1.9680 1.7060 0.3153 -0.1418 -0.1281 159 TYR B CE1 3836 C CE2 . TYR B 159 ? 2.5198 1.9682 1.7321 0.2886 -0.1739 -0.1582 159 TYR B CE2 3837 C CZ . TYR B 159 ? 2.4271 1.9730 1.7055 0.3344 -0.1553 -0.1444 159 TYR B CZ 3838 O OH . TYR B 159 ? 2.4582 1.9881 1.6782 0.3990 -0.1512 -0.1459 159 TYR B OH 3839 N N . PRO B 160 ? 2.6069 2.1754 1.9421 0.1155 -0.2028 -0.1560 160 PRO B N 3840 C CA . PRO B 160 ? 2.6344 2.1597 1.8999 0.1350 -0.2141 -0.1656 160 PRO B CA 3841 C C . PRO B 160 ? 2.5138 2.1276 1.8370 0.1155 -0.2167 -0.1605 160 PRO B C 3842 O O . PRO B 160 ? 2.4471 2.0814 1.7663 0.1527 -0.2135 -0.1604 160 PRO B O 3843 C CB . PRO B 160 ? 2.7820 2.1738 1.9239 0.0985 -0.2386 -0.1813 160 PRO B CB 3844 C CG . PRO B 160 ? 2.8034 2.1558 1.9397 0.0801 -0.2362 -0.1796 160 PRO B CG 3845 C CD . PRO B 160 ? 2.6782 2.1598 1.9482 0.0696 -0.2177 -0.1639 160 PRO B CD 3846 N N . GLN B 161 ? 2.4366 2.1062 1.8102 0.0601 -0.2225 -0.1557 161 GLN B N 3847 C CA . GLN B 161 ? 2.3410 2.1075 1.7762 0.0423 -0.2241 -0.1490 161 GLN B CA 3848 C C . GLN B 161 ? 2.1728 2.0232 1.6857 0.0926 -0.2042 -0.1369 161 GLN B C 3849 O O . GLN B 161 ? 2.1102 1.9969 1.6302 0.1059 -0.2061 -0.1356 161 GLN B O 3850 C CB . GLN B 161 ? 2.2846 2.1196 1.7780 -0.0111 -0.2268 -0.1414 161 GLN B CB 3851 C CG . GLN B 161 ? 2.1943 2.1371 1.7494 -0.0270 -0.2286 -0.1335 161 GLN B CG 3852 C CD . GLN B 161 ? 2.1088 2.1364 1.7312 -0.0620 -0.2257 -0.1234 161 GLN B CD 3853 O OE1 . GLN B 161 ? 2.1058 2.1031 1.7094 -0.0964 -0.2305 -0.1247 161 GLN B OE1 3854 N NE2 . GLN B 161 ? 2.0117 2.1453 1.7083 -0.0501 -0.2179 -0.1127 161 GLN B NE2 3855 N N . TYR B 162 ? 2.0359 1.9152 1.6034 0.1163 -0.1864 -0.1271 162 TYR B N 3856 C CA . TYR B 162 ? 1.8927 1.8382 1.5216 0.1593 -0.1688 -0.1137 162 TYR B CA 3857 C C . TYR B 162 ? 1.8548 1.7519 1.4354 0.2081 -0.1620 -0.1157 162 TYR B C 3858 O O . TYR B 162 ? 1.7164 1.6527 1.3128 0.2453 -0.1532 -0.1075 162 TYR B O 3859 C CB . TYR B 162 ? 1.8125 1.8179 1.5228 0.1536 -0.1551 -0.1006 162 TYR B CB 3860 C CG . TYR B 162 ? 1.7883 1.8421 1.5406 0.1116 -0.1606 -0.0987 162 TYR B CG 3861 C CD1 . TYR B 162 ? 1.7314 1.8602 1.5296 0.1097 -0.1607 -0.0911 162 TYR B CD1 3862 C CD2 . TYR B 162 ? 1.7956 1.8261 1.5403 0.0772 -0.1651 -0.1029 162 TYR B CD2 3863 C CE1 . TYR B 162 ? 1.7107 1.8951 1.5450 0.0789 -0.1649 -0.0881 162 TYR B CE1 3864 C CE2 . TYR B 162 ? 1.7650 1.8539 1.5484 0.0420 -0.1692 -0.0992 162 TYR B CE2 3865 C CZ . TYR B 162 ? 1.7430 1.9119 1.5711 0.0451 -0.1689 -0.0919 162 TYR B CZ 3866 O OH . TYR B 162 ? 1.7265 1.9637 1.5903 0.0169 -0.1724 -0.0873 162 TYR B OH 3867 C C1 . NAG C . ? 1.8882 1.8613 1.6272 0.3367 -0.0407 -0.0817 1011 NAG A C1 3868 C C2 . NAG C . ? 1.9768 1.9488 1.7039 0.3563 -0.0453 -0.0884 1011 NAG A C2 3869 C C3 . NAG C . ? 2.0230 2.0536 1.7666 0.3680 -0.0585 -0.1051 1011 NAG A C3 3870 C C4 . NAG C . ? 2.0716 2.1255 1.8089 0.3818 -0.0676 -0.1118 1011 NAG A C4 3871 C C5 . NAG C . ? 2.0674 2.1219 1.8196 0.3574 -0.0619 -0.1048 1011 NAG A C5 3872 C C6 . NAG C . ? 2.0715 2.1459 1.8157 0.3702 -0.0704 -0.1112 1011 NAG A C6 3873 C C7 . NAG C . ? 1.9116 1.8140 1.6248 0.3411 -0.0273 -0.0736 1011 NAG A C7 3874 C C8 . NAG C . ? 1.8763 1.7711 1.6047 0.3223 -0.0197 -0.0707 1011 NAG A C8 3875 N N2 . NAG C . ? 1.9148 1.8712 1.6525 0.3397 -0.0368 -0.0835 1011 NAG A N2 3876 O O3 . NAG C . ? 2.0931 2.1165 1.8179 0.3922 -0.0633 -0.1109 1011 NAG A O3 3877 O O4 . NAG C . ? 1.9781 2.0914 1.7337 0.3899 -0.0791 -0.1288 1011 NAG A O4 3878 O O5 . NAG C . ? 1.9837 1.9823 1.7187 0.3496 -0.0501 -0.0889 1011 NAG A O5 3879 O O6 . NAG C . ? 2.0231 2.1371 1.7977 0.3463 -0.0711 -0.1159 1011 NAG A O6 3880 O O7 . NAG C . ? 1.9172 1.7761 1.5955 0.3563 -0.0242 -0.0672 1011 NAG A O7 3881 C C1 . NAG D . ? 1.4455 1.3691 1.4193 0.0375 0.0869 -0.0140 1023 NAG A C1 3882 C C2 . NAG D . ? 1.5146 1.4353 1.4951 0.0237 0.0965 -0.0159 1023 NAG A C2 3883 C C3 . NAG D . ? 1.5985 1.5280 1.5882 0.0182 0.0945 -0.0223 1023 NAG A C3 3884 C C4 . NAG D . ? 1.6499 1.5669 1.6262 0.0291 0.0887 -0.0248 1023 NAG A C4 3885 C C5 . NAG D . ? 1.5698 1.4979 1.5447 0.0416 0.0792 -0.0229 1023 NAG A C5 3886 C C6 . NAG D . ? 1.5164 1.4405 1.4810 0.0538 0.0720 -0.0267 1023 NAG A C6 3887 C C7 . NAG D . ? 1.5258 1.4617 1.5200 0.0128 0.1060 -0.0109 1023 NAG A C7 3888 C C8 . NAG D . ? 1.4926 1.4554 1.5054 0.0075 0.1061 -0.0107 1023 NAG A C8 3889 N N2 . NAG D . ? 1.5019 1.4447 1.4996 0.0163 0.0982 -0.0145 1023 NAG A N2 3890 O O3 . NAG D . ? 1.6650 1.5838 1.6542 0.0060 0.1045 -0.0250 1023 NAG A O3 3891 O O4 . NAG D . ? 1.8219 1.7539 1.8109 0.0235 0.0858 -0.0308 1023 NAG A O4 3892 O O5 . NAG D . ? 1.4958 1.4080 1.4576 0.0463 0.0827 -0.0172 1023 NAG A O5 3893 O O6 . NAG D . ? 1.5190 1.4091 1.4578 0.0629 0.0760 -0.0253 1023 NAG A O6 3894 O O7 . NAG D . ? 1.5385 1.4472 1.5142 0.0145 0.1130 -0.0079 1023 NAG A O7 3895 C C1 . NAG E . ? 1.9834 1.8908 1.9561 0.0261 0.0884 -0.0342 1024 NAG A C1 3896 C C2 . NAG E . ? 1.9699 1.8965 1.9573 0.0212 0.0840 -0.0408 1024 NAG A C2 3897 C C3 . NAG E . ? 2.0257 1.9256 1.9964 0.0216 0.0878 -0.0452 1024 NAG A C3 3898 C C4 . NAG E . ? 2.0723 1.9363 2.0234 0.0148 0.1002 -0.0433 1024 NAG A C4 3899 C C5 . NAG E . ? 2.0315 1.8800 1.9686 0.0223 0.1027 -0.0361 1024 NAG A C5 3900 C C6 . NAG E . ? 2.0450 1.8560 1.9602 0.0150 0.1161 -0.0339 1024 NAG A C6 3901 C C7 . NAG E . ? 1.8410 1.8213 1.8565 0.0262 0.0685 -0.0412 1024 NAG A C7 3902 C C8 . NAG E . ? 1.7650 1.7662 1.7862 0.0337 0.0587 -0.0432 1024 NAG A C8 3903 N N2 . NAG E . ? 1.9246 1.8755 1.9213 0.0300 0.0730 -0.0420 1024 NAG A N2 3904 O O3 . NAG E . ? 2.0242 1.9419 2.0107 0.0124 0.0865 -0.0513 1024 NAG A O3 3905 O O4 . NAG E . ? 2.1145 1.9470 2.0427 0.0192 0.1029 -0.0465 1024 NAG A O4 3906 O O5 . NAG E . ? 2.0052 1.8844 1.9643 0.0179 0.1000 -0.0334 1024 NAG A O5 3907 O O6 . NAG E . ? 2.0110 1.8373 1.9440 -0.0032 0.1239 -0.0352 1024 NAG A O6 3908 O O7 . NAG E . ? 1.7979 1.7883 1.8248 0.0171 0.0721 -0.0392 1024 NAG A O7 3909 C C1 . NAG F . ? 2.3377 1.8948 1.2153 -0.5912 0.4680 -0.1416 1165 NAG A C1 3910 C C2 . NAG F . ? 2.4250 1.8777 1.2157 -0.5833 0.4752 -0.1243 1165 NAG A C2 3911 C C3 . NAG F . ? 2.5194 1.9303 1.2737 -0.6170 0.4938 -0.1268 1165 NAG A C3 3912 C C4 . NAG F . ? 2.5811 2.0196 1.3352 -0.6667 0.5201 -0.1447 1165 NAG A C4 3913 C C5 . NAG F . ? 2.4629 2.0109 1.3065 -0.6705 0.5109 -0.1619 1165 NAG A C5 3914 C C6 . NAG F . ? 2.4566 2.0398 1.3027 -0.7184 0.5367 -0.1813 1165 NAG A C6 3915 C C7 . NAG F . ? 2.3766 1.7549 1.1220 -0.5095 0.4449 -0.0954 1165 NAG A C7 3916 C C8 . NAG F . ? 2.3435 1.7086 1.0978 -0.4638 0.4191 -0.0818 1165 NAG A C8 3917 N N2 . NAG F . ? 2.3556 1.7868 1.1491 -0.5376 0.4504 -0.1089 1165 NAG A N2 3918 O O3 . NAG F . ? 2.6108 1.9204 1.2778 -0.6111 0.5028 -0.1114 1165 NAG A O3 3919 O O4 . NAG F . ? 2.7200 2.1292 1.4500 -0.6974 0.5349 -0.1486 1165 NAG A O4 3920 O O5 . NAG F . ? 2.3998 1.9756 1.2698 -0.6359 0.4932 -0.1571 1165 NAG A O5 3921 O O6 . NAG F . ? 2.4421 1.9840 1.2319 -0.7306 0.5551 -0.1795 1165 NAG A O6 3922 O O7 . NAG F . ? 2.4498 1.7913 1.1442 -0.5188 0.4600 -0.0940 1165 NAG A O7 3923 C C1 . NAG G . ? 2.8919 2.2344 1.5440 -0.7348 0.5658 -0.1502 1166 NAG A C1 3924 C C2 . NAG G . ? 2.9348 2.2539 1.5698 -0.7675 0.5795 -0.1559 1166 NAG A C2 3925 C C3 . NAG G . ? 3.0819 2.3100 1.6223 -0.8043 0.6113 -0.1542 1166 NAG A C3 3926 C C4 . NAG G . ? 3.1863 2.3212 1.6468 -0.7770 0.6120 -0.1340 1166 NAG A C4 3927 C C5 . NAG G . ? 3.1039 2.2815 1.5941 -0.7509 0.5998 -0.1327 1166 NAG A C5 3928 C C6 . NAG G . ? 3.1452 2.2347 1.5564 -0.7236 0.6004 -0.1141 1166 NAG A C6 3929 C C7 . NAG G . ? 2.7625 2.2390 1.5416 -0.7798 0.5609 -0.1817 1166 NAG A C7 3930 C C8 . NAG G . ? 2.7075 2.2782 1.5536 -0.8100 0.5658 -0.2052 1166 NAG A C8 3931 N N2 . NAG G . ? 2.8626 2.2758 1.5705 -0.7950 0.5816 -0.1773 1166 NAG A N2 3932 O O3 . NAG G . ? 3.1155 2.3094 1.6363 -0.8217 0.6175 -0.1545 1166 NAG A O3 3933 O O4 . NAG G . ? 3.4272 2.4675 1.7914 -0.8084 0.6417 -0.1307 1166 NAG A O4 3934 O O5 . NAG G . ? 2.9813 2.2333 1.5547 -0.7148 0.5689 -0.1324 1166 NAG A O5 3935 O O6 . NAG G . ? 3.0725 2.2071 1.5155 -0.7010 0.5888 -0.1145 1166 NAG A O6 3936 O O7 . NAG G . ? 2.6677 2.1298 1.4587 -0.7428 0.5387 -0.1683 1166 NAG A O7 3937 C C1 . MAN H . ? 3.5186 2.5760 1.8710 -0.8608 0.6713 -0.1480 1167 MAN A C1 3938 C C2 . MAN H . ? 3.6457 2.5887 1.8846 -0.8806 0.6994 -0.1390 1167 MAN A C2 3939 C C3 . MAN H . ? 3.7499 2.6106 1.9265 -0.8991 0.7126 -0.1339 1167 MAN A C3 3940 C C4 . MAN H . ? 3.7140 2.6372 1.9419 -0.9423 0.7221 -0.1544 1167 MAN A C4 3941 C C5 . MAN H . ? 3.5834 2.6147 1.9210 -0.9136 0.6906 -0.1601 1167 MAN A C5 3942 C C6 . MAN H . ? 3.5379 2.6375 1.9333 -0.9479 0.6945 -0.1797 1167 MAN A C6 3943 O O2 . MAN H . ? 3.6184 2.5814 1.8463 -0.9252 0.7267 -0.1544 1167 MAN A O2 3944 O O3 . MAN H . ? 3.8935 2.6440 1.9599 -0.9206 0.7410 -0.1264 1167 MAN A O3 3945 O O4 . MAN H . ? 3.7556 2.6055 1.9287 -0.9607 0.7340 -0.1509 1167 MAN A O4 3946 O O5 . MAN H . ? 3.5374 2.6411 1.9268 -0.9007 0.6818 -0.1658 1167 MAN A O5 3947 O O6 . MAN H . ? 3.5967 2.6244 1.9385 -0.9663 0.7060 -0.1760 1167 MAN A O6 3948 C C1 . BMA I . ? 3.9383 2.5914 1.9352 -0.9118 0.7429 -0.1124 1168 BMA A C1 3949 C C2 . BMA I . ? 3.9738 2.5321 1.8918 -0.8684 0.7361 -0.0893 1168 BMA A C2 3950 C C3 . BMA I . ? 4.0046 2.4701 1.8586 -0.8542 0.7346 -0.0753 1168 BMA A C3 3951 C C4 . BMA I . ? 4.0729 2.4834 1.8702 -0.9117 0.7680 -0.0851 1168 BMA A C4 3952 C C5 . BMA I . ? 4.0101 2.5234 1.8906 -0.9577 0.7757 -0.1096 1168 BMA A C5 3953 C C6 . BMA I . ? 4.0547 2.5149 1.8758 -1.0194 0.8117 -0.1214 1168 BMA A C6 3954 O O2 . BMA I . ? 3.9828 2.4820 1.8259 -0.8917 0.7629 -0.0888 1168 BMA A O2 3955 O O3 . BMA I . ? 4.0795 2.4502 1.8502 -0.8167 0.7313 -0.0550 1168 BMA A O3 3956 O O4 . BMA I . ? 4.0489 2.3809 1.7946 -0.8991 0.7654 -0.0736 1168 BMA A O4 3957 O O5 . BMA I . ? 4.0281 2.6233 1.9632 -0.9649 0.7757 -0.1207 1168 BMA A O5 3958 O O6 . BMA I . ? 4.0903 2.4996 1.8428 -1.0490 0.8407 -0.1234 1168 BMA A O6 3959 C C1 . MAN J . ? 3.5517 2.6437 1.9501 -0.9936 0.7063 -0.1935 1169 MAN A C1 3960 C C2 . MAN J . ? 3.4601 2.5729 1.9059 -0.9516 0.6750 -0.1837 1169 MAN A C2 3961 C C3 . MAN J . ? 3.3092 2.5380 1.8618 -0.9240 0.6474 -0.1910 1169 MAN A C3 3962 C C4 . MAN J . ? 3.2976 2.6218 1.9083 -0.9629 0.6591 -0.2167 1169 MAN A C4 3963 C C5 . MAN J . ? 3.3915 2.6932 1.9552 -0.9945 0.6862 -0.2230 1169 MAN A C5 3964 C C6 . MAN J . ? 3.3520 2.7473 1.9688 -1.0370 0.7005 -0.2504 1169 MAN A C6 3965 O O2 . MAN J . ? 3.4420 2.5385 1.8789 -0.9777 0.6830 -0.1905 1169 MAN A O2 3966 O O3 . MAN J . ? 3.2008 2.4494 1.7942 -0.9001 0.6254 -0.1867 1169 MAN A O3 3967 O O4 . MAN J . ? 3.1610 2.5820 1.8615 -0.9318 0.6329 -0.2210 1169 MAN A O4 3968 O O5 . MAN J . ? 3.5144 2.7092 1.9802 -1.0232 0.7127 -0.2168 1169 MAN A O5 3969 O O6 . MAN J . ? 3.3375 2.7398 1.9385 -1.0469 0.7140 -0.2541 1169 MAN A O6 3970 C C1 . NAG K . ? 1.6555 2.2505 1.7876 0.0366 -0.0162 -0.2199 1286 NAG A C1 3971 C C2 . NAG K . ? 1.7089 2.3626 1.8533 0.0358 -0.0183 -0.2400 1286 NAG A C2 3972 C C3 . NAG K . ? 1.7555 2.4328 1.9000 0.0441 -0.0242 -0.2489 1286 NAG A C3 3973 C C4 . NAG K . ? 1.8107 2.4614 1.9441 0.0732 -0.0323 -0.2417 1286 NAG A C4 3974 C C5 . NAG K . ? 1.7910 2.3818 1.9124 0.0709 -0.0285 -0.2213 1286 NAG A C5 3975 C C6 . NAG K . ? 1.7696 2.3299 1.8777 0.0982 -0.0349 -0.2138 1286 NAG A C6 3976 C C7 . NAG K . ? 1.6112 2.2926 1.7670 0.0005 -0.0055 -0.2478 1286 NAG A C7 3977 C C8 . NAG K . ? 1.5476 2.2484 1.7067 -0.0294 0.0042 -0.2542 1286 NAG A C8 3978 N N2 . NAG K . ? 1.6793 2.3544 1.8305 0.0079 -0.0098 -0.2462 1286 NAG A N2 3979 O O3 . NAG K . ? 1.7717 2.5075 1.9288 0.0459 -0.0270 -0.2689 1286 NAG A O3 3980 O O4 . NAG K . ? 1.8396 2.5076 1.9710 0.0798 -0.0374 -0.2485 1286 NAG A O4 3981 O O5 . NAG K . ? 1.7459 2.3234 1.8701 0.0630 -0.0236 -0.2159 1286 NAG A O5 3982 O O6 . NAG K . ? 1.7160 2.2490 1.8149 0.0952 -0.0341 -0.2043 1286 NAG A O6 3983 O O7 . NAG K . ? 1.5984 2.2687 1.7540 0.0165 -0.0085 -0.2443 1286 NAG A O7 3997 C C1 . NAG M . ? 1.5163 1.9687 1.4428 -0.2511 -0.1885 -0.0596 1154 NAG B C1 3998 C C2 . NAG M . ? 1.5990 2.0659 1.4752 -0.3276 -0.2104 -0.0562 1154 NAG B C2 3999 C C3 . NAG M . ? 1.6436 2.1141 1.4849 -0.3486 -0.2265 -0.0590 1154 NAG B C3 4000 C C4 . NAG M . ? 1.6104 2.1534 1.5067 -0.2925 -0.2159 -0.0574 1154 NAG B C4 4001 C C5 . NAG M . ? 1.5420 2.0183 1.4616 -0.2253 -0.1970 -0.0638 1154 NAG B C5 4002 C C6 . NAG M . ? 1.4961 2.0209 1.4561 -0.1723 -0.1883 -0.0620 1154 NAG B C6 4003 C C7 . NAG M . ? 1.6547 1.9983 1.4775 -0.3688 -0.2107 -0.0582 1154 NAG B C7 4004 C C8 . NAG M . ? 1.7379 1.9537 1.4813 -0.4066 -0.2213 -0.0638 1154 NAG B C8 4005 N N2 . NAG M . ? 1.6593 2.0119 1.4693 -0.3656 -0.2190 -0.0616 1154 NAG B N2 4006 O O3 . NAG M . ? 1.6826 2.2292 1.5060 -0.4178 -0.2442 -0.0492 1154 NAG B O3 4007 O O4 . NAG M . ? 1.6825 2.2214 1.5435 -0.3105 -0.2308 -0.0610 1154 NAG B O4 4008 O O5 . NAG M . ? 1.4744 1.9789 1.4347 -0.2100 -0.1835 -0.0585 1154 NAG B O5 4009 O O6 . NAG M . ? 1.4281 2.0676 1.4471 -0.1502 -0.1793 -0.0512 1154 NAG B O6 4010 O O7 . NAG M . ? 1.5524 1.9814 1.4423 -0.3401 -0.1955 -0.0511 1154 NAG B O7 4011 C C1 . NAG N . ? 1.6443 2.3280 1.5434 -0.3244 -0.2356 -0.0493 1155 NAG B C1 4012 C C2 . NAG N . ? 1.6946 2.3730 1.5515 -0.3499 -0.2535 -0.0531 1155 NAG B C2 4013 C C3 . NAG N . ? 1.6980 2.5377 1.5869 -0.3769 -0.2620 -0.0390 1155 NAG B C3 4014 C C4 . NAG N . ? 1.7057 2.6293 1.6015 -0.4335 -0.2683 -0.0258 1155 NAG B C4 4015 C C5 . NAG N . ? 1.6605 2.5823 1.6030 -0.3897 -0.2468 -0.0241 1155 NAG B C5 4016 C C6 . NAG N . ? 1.6592 2.6770 1.6182 -0.4340 -0.2491 -0.0098 1155 NAG B C6 4017 C C7 . NAG N . ? 1.6720 2.1746 1.5052 -0.2591 -0.2381 -0.0731 1155 NAG B C7 4018 C C8 . NAG N . ? 1.6374 2.1180 1.4794 -0.2048 -0.2308 -0.0779 1155 NAG B C8 4019 N N2 . NAG N . ? 1.6748 2.3016 1.5352 -0.2923 -0.2454 -0.0618 1155 NAG B N2 4020 O O3 . NAG N . ? 1.7667 2.5919 1.6063 -0.4129 -0.2818 -0.0428 1155 NAG B O3 4021 O O4 . NAG N . ? 1.6650 2.7596 1.5960 -0.4526 -0.2743 -0.0102 1155 NAG B O4 4022 O O5 . NAG N . ? 1.6599 2.4215 1.5631 -0.3782 -0.2429 -0.0380 1155 NAG B O5 4023 O O6 . NAG N . ? 1.7387 2.7722 1.6437 -0.5237 -0.2737 -0.0034 1155 NAG B O6 4024 O O7 . NAG N . ? 1.6742 2.0873 1.4755 -0.2695 -0.2369 -0.0785 1155 NAG B O7 4025 C C1 . BMA O . ? 1.7567 2.8654 1.6342 -0.5222 -0.3001 -0.0082 1156 BMA B C1 4026 C C2 . BMA O . ? 1.7625 3.0462 1.6606 -0.5801 -0.3110 0.0130 1156 BMA B C2 4027 C C3 . BMA O . ? 1.8300 3.1474 1.6743 -0.6576 -0.3396 0.0178 1156 BMA B C3 4028 C C4 . BMA O . ? 1.8112 3.1048 1.6524 -0.6156 -0.3404 0.0075 1156 BMA B C4 4029 C C5 . BMA O . ? 1.8019 2.9147 1.6222 -0.5554 -0.3278 -0.0139 1156 BMA B C5 4030 C C6 . BMA O . ? 1.7973 2.8944 1.6163 -0.5125 -0.3279 -0.0224 1156 BMA B C6 4031 O O2 . BMA O . ? 1.7000 3.1414 1.6793 -0.5152 -0.2928 0.0243 1156 BMA B O2 4032 O O3 . BMA O . ? 1.8108 3.3297 1.6898 -0.6991 -0.3469 0.0409 1156 BMA B O3 4033 O O4 . BMA O . ? 1.8986 3.1874 1.6722 -0.6956 -0.3699 0.0089 1156 BMA B O4 4034 O O5 . BMA O . ? 1.7321 2.8478 1.6132 -0.4869 -0.3012 -0.0138 1156 BMA B O5 4035 O O6 . BMA O . ? 1.6984 2.7800 1.5733 -0.4181 -0.3019 -0.0274 1156 BMA B O6 # _database_PDB_caveat.id 1 _database_PDB_caveat.text 'NAG B1154 HAS WRONG CHIRALITY AT ATOM C1' # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 ASP 1 1 1 ASP ASP A . n A 1 2 GLN 2 2 2 GLN GLN A . n A 1 3 ILE 3 3 3 ILE ILE A . n A 1 4 CYS 4 4 4 CYS CYS A . n A 1 5 ILE 5 5 5 ILE ILE A . n A 1 6 GLY 6 6 6 GLY GLY A . n A 1 7 TYR 7 7 7 TYR TYR A . n A 1 8 HIS 8 8 8 HIS HIS A . n A 1 9 ALA 9 9 9 ALA ALA A . n A 1 10 ASN 10 10 10 ASN ASN A . n A 1 11 ASN 11 11 11 ASN ASN A . n A 1 12 SER 12 12 12 SER SER A . n A 1 13 THR 13 13 13 THR THR A . n A 1 14 GLU 14 14 14 GLU GLU A . n A 1 15 GLN 15 15 15 GLN GLN A . n A 1 16 VAL 16 16 16 VAL VAL A . n A 1 17 ASP 17 17 17 ASP ASP A . n A 1 18 THR 18 18 18 THR THR A . n A 1 19 ILE 19 19 19 ILE ILE A . n A 1 20 MET 20 20 20 MET MET A . n A 1 21 GLU 21 21 21 GLU GLU A . n A 1 22 LYS 22 22 22 LYS LYS A . n A 1 23 ASN 23 23 23 ASN ASN A . n A 1 24 VAL 24 24 24 VAL VAL A . n A 1 25 THR 25 25 25 THR THR A . n A 1 26 VAL 26 26 26 VAL VAL A . n A 1 27 THR 27 27 27 THR THR A . n A 1 28 HIS 28 28 28 HIS HIS A . n A 1 29 ALA 29 29 29 ALA ALA A . n A 1 30 GLN 30 30 30 GLN GLN A . n A 1 31 ASP 31 31 31 ASP ASP A . n A 1 32 ILE 32 32 32 ILE ILE A . n A 1 33 LEU 33 33 33 LEU LEU A . n A 1 34 GLU 34 34 34 GLU GLU A . n A 1 35 LYS 35 35 35 LYS LYS A . n A 1 36 THR 36 36 36 THR THR A . n A 1 37 HIS 37 37 37 HIS HIS A . n A 1 38 ASN 38 38 38 ASN ASN A . n A 1 39 GLY 39 39 39 GLY GLY A . n A 1 40 LYS 40 40 40 LYS LYS A . n A 1 41 LEU 41 41 41 LEU LEU A . n A 1 42 CYS 42 42 42 CYS CYS A . n A 1 43 ASP 43 43 43 ASP ASP A . n A 1 44 LEU 44 44 44 LEU LEU A . n A 1 45 ASP 45 45 45 ASP ASP A . n A 1 46 GLY 46 46 46 GLY GLY A . n A 1 47 VAL 47 47 47 VAL VAL A . n A 1 48 LYS 48 48 48 LYS LYS A . n A 1 49 PRO 49 49 49 PRO PRO A . n A 1 50 LEU 50 50 50 LEU LEU A . n A 1 51 ILE 51 51 51 ILE ILE A . n A 1 52 LEU 52 52 52 LEU LEU A . n A 1 53 ARG 53 53 53 ARG ARG A . n A 1 54 ASP 54 54 54 ASP ASP A . n A 1 55 CYS 55 55 55 CYS CYS A . n A 1 56 SER 56 56 56 SER SER A . n A 1 57 VAL 57 57 57 VAL VAL A . n A 1 58 ALA 58 58 58 ALA ALA A . n A 1 59 GLY 59 59 59 GLY GLY A . n A 1 60 TRP 60 60 60 TRP TRP A . n A 1 61 LEU 61 61 61 LEU LEU A . n A 1 62 LEU 62 62 62 LEU LEU A . n A 1 63 GLY 63 63 63 GLY GLY A . n A 1 64 ASN 64 64 64 ASN ASN A . n A 1 65 PRO 65 65 65 PRO PRO A . n A 1 66 MET 66 66 66 MET MET A . n A 1 67 CYS 67 67 67 CYS CYS A . n A 1 68 ASP 68 68 68 ASP ASP A . n A 1 69 GLU 69 69 69 GLU GLU A . n A 1 70 PHE 70 70 70 PHE PHE A . n A 1 71 ILE 71 71 71 ILE ILE A . n A 1 72 ASN 72 72 72 ASN ASN A . n A 1 73 VAL 73 73 73 VAL VAL A . n A 1 74 PRO 74 74 74 PRO PRO A . n A 1 75 GLU 75 75 75 GLU GLU A . n A 1 76 TRP 76 76 76 TRP TRP A . n A 1 77 SER 77 77 77 SER SER A . n A 1 78 TYR 78 78 78 TYR TYR A . n A 1 79 ILE 79 79 79 ILE ILE A . n A 1 80 VAL 80 80 80 VAL VAL A . n A 1 81 GLU 81 81 81 GLU GLU A . n A 1 82 LYS 82 82 82 LYS LYS A . n A 1 83 ALA 83 83 83 ALA ALA A . n A 1 84 ASN 84 84 84 ASN ASN A . n A 1 85 PRO 85 85 85 PRO PRO A . n A 1 86 VAL 86 86 86 VAL VAL A . n A 1 87 ASN 87 87 87 ASN ASN A . n A 1 88 ASP 88 88 88 ASP ASP A . n A 1 89 LEU 89 89 89 LEU LEU A . n A 1 90 CYS 90 90 90 CYS CYS A . n A 1 91 TYR 91 91 91 TYR TYR A . n A 1 92 PRO 92 92 92 PRO PRO A . n A 1 93 GLY 93 93 93 GLY GLY A . n A 1 94 ASP 94 94 94 ASP ASP A . n A 1 95 PHE 95 95 95 PHE PHE A . n A 1 96 ASN 96 96 96 ASN ASN A . n A 1 97 ASP 97 97 97 ASP ASP A . n A 1 98 TYR 98 98 98 TYR TYR A . n A 1 99 GLU 99 99 99 GLU GLU A . n A 1 100 GLU 100 100 100 GLU GLU A . n A 1 101 LEU 101 101 101 LEU LEU A . n A 1 102 LYS 102 102 102 LYS LYS A . n A 1 103 HIS 103 103 103 HIS HIS A . n A 1 104 LEU 104 104 104 LEU LEU A . n A 1 105 LEU 105 105 105 LEU LEU A . n A 1 106 SER 106 106 106 SER SER A . n A 1 107 ARG 107 107 107 ARG ARG A . n A 1 108 ILE 108 108 108 ILE ILE A . n A 1 109 ASN 109 109 109 ASN ASN A . n A 1 110 HIS 110 110 110 HIS HIS A . n A 1 111 PHE 111 111 111 PHE PHE A . n A 1 112 GLU 112 112 112 GLU GLU A . n A 1 113 LYS 113 113 113 LYS LYS A . n A 1 114 ILE 114 114 114 ILE ILE A . n A 1 115 GLN 115 115 115 GLN GLN A . n A 1 116 ILE 116 116 116 ILE ILE A . n A 1 117 ILE 117 117 117 ILE ILE A . n A 1 118 PRO 118 118 118 PRO PRO A . n A 1 119 LYS 119 119 119 LYS LYS A . n A 1 120 SER 120 120 120 SER SER A . n A 1 121 SER 121 121 121 SER SER A . n A 1 122 TRP 122 122 122 TRP TRP A . n A 1 123 SER 123 123 123 SER SER A . n A 1 124 SER 124 124 124 SER SER A . n A 1 125 HIS 125 125 125 HIS HIS A . n A 1 126 GLU 126 126 126 GLU GLU A . n A 1 127 ALA 127 127 127 ALA ALA A . n A 1 128 SER 128 128 128 SER SER A . n A 1 129 LEU 129 129 129 LEU LEU A . n A 1 130 GLY 130 130 130 GLY GLY A . n A 1 131 VAL 131 131 131 VAL VAL A . n A 1 132 SER 132 132 132 SER SER A . n A 1 133 SER 133 133 133 SER SER A . n A 1 134 ALA 134 134 134 ALA ALA A . n A 1 135 CYS 135 135 135 CYS CYS A . n A 1 136 PRO 136 136 136 PRO PRO A . n A 1 137 TYR 137 137 137 TYR TYR A . n A 1 138 GLN 138 138 138 GLN GLN A . n A 1 139 GLY 139 139 139 GLY GLY A . n A 1 140 LYS 140 140 140 LYS LYS A . n A 1 141 SER 141 141 141 SER SER A . n A 1 142 SER 142 142 142 SER SER A . n A 1 143 PHE 143 143 143 PHE PHE A . n A 1 144 PHE 144 144 144 PHE PHE A . n A 1 145 ARG 145 145 145 ARG ARG A . n A 1 146 ASN 146 146 146 ASN ASN A . n A 1 147 VAL 147 147 147 VAL VAL A . n A 1 148 VAL 148 148 148 VAL VAL A . n A 1 149 TRP 149 149 149 TRP TRP A . n A 1 150 LEU 150 150 150 LEU LEU A . n A 1 151 ILE 151 151 151 ILE ILE A . n A 1 152 LYS 152 152 152 LYS LYS A . n A 1 153 LYS 153 153 153 LYS LYS A . n A 1 154 ASN 154 154 154 ASN ASN A . n A 1 155 SER 155 155 155 SER SER A . n A 1 156 THR 156 156 156 THR THR A . n A 1 157 TYR 157 157 157 TYR TYR A . n A 1 158 PRO 158 158 158 PRO PRO A . n A 1 159 THR 159 159 159 THR THR A . n A 1 160 ILE 160 160 160 ILE ILE A . n A 1 161 LYS 161 161 161 LYS LYS A . n A 1 162 ARG 162 162 162 ARG ARG A . n A 1 163 SER 163 163 163 SER SER A . n A 1 164 TYR 164 164 164 TYR TYR A . n A 1 165 ASN 165 165 165 ASN ASN A . n A 1 166 ASN 166 166 166 ASN ASN A . n A 1 167 THR 167 167 167 THR THR A . n A 1 168 ASN 168 168 168 ASN ASN A . n A 1 169 GLN 169 169 169 GLN GLN A . n A 1 170 GLU 170 170 170 GLU GLU A . n A 1 171 ASP 171 171 171 ASP ASP A . n A 1 172 LEU 172 172 172 LEU LEU A . n A 1 173 LEU 173 173 173 LEU LEU A . n A 1 174 VAL 174 174 174 VAL VAL A . n A 1 175 LEU 175 175 175 LEU LEU A . n A 1 176 TRP 176 176 176 TRP TRP A . n A 1 177 GLY 177 177 177 GLY GLY A . n A 1 178 ILE 178 178 178 ILE ILE A . n A 1 179 HIS 179 179 179 HIS HIS A . n A 1 180 HIS 180 180 180 HIS HIS A . n A 1 181 PRO 181 181 181 PRO PRO A . n A 1 182 ASN 182 182 182 ASN ASN A . n A 1 183 ASP 183 183 183 ASP ASP A . n A 1 184 ALA 184 184 184 ALA ALA A . n A 1 185 ALA 185 185 185 ALA ALA A . n A 1 186 GLU 186 186 186 GLU GLU A . n A 1 187 GLN 187 187 187 GLN GLN A . n A 1 188 THR 188 188 188 THR THR A . n A 1 189 LYS 189 189 189 LYS LYS A . n A 1 190 LEU 190 190 190 LEU LEU A . n A 1 191 TYR 191 191 191 TYR TYR A . n A 1 192 ARG 192 192 192 ARG ARG A . n A 1 193 ASN 193 193 193 ASN ASN A . n A 1 194 PRO 194 194 194 PRO PRO A . n A 1 195 THR 195 195 195 THR THR A . n A 1 196 THR 196 196 196 THR THR A . n A 1 197 TYR 197 197 197 TYR TYR A . n A 1 198 ILE 198 198 198 ILE ILE A . n A 1 199 SER 199 199 199 SER SER A . n A 1 200 VAL 200 200 200 VAL VAL A . n A 1 201 GLY 201 201 201 GLY GLY A . n A 1 202 THR 202 202 202 THR THR A . n A 1 203 SER 203 203 203 SER SER A . n A 1 204 THR 204 204 204 THR THR A . n A 1 205 LEU 205 205 205 LEU LEU A . n A 1 206 ASN 206 206 206 ASN ASN A . n A 1 207 GLN 207 207 207 GLN GLN A . n A 1 208 ARG 208 208 208 ARG ARG A . n A 1 209 LEU 209 209 209 LEU LEU A . n A 1 210 VAL 210 210 210 VAL VAL A . n A 1 211 PRO 211 211 211 PRO PRO A . n A 1 212 ARG 212 212 212 ARG ARG A . n A 1 213 ILE 213 213 213 ILE ILE A . n A 1 214 ALA 214 214 214 ALA ALA A . n A 1 215 THR 215 215 215 THR THR A . n A 1 216 ARG 216 216 216 ARG ARG A . n A 1 217 SER 217 217 217 SER SER A . n A 1 218 LYS 218 218 218 LYS LYS A . n A 1 219 VAL 219 219 219 VAL VAL A . n A 1 220 ASN 220 220 220 ASN ASN A . n A 1 221 GLY 221 221 221 GLY GLY A . n A 1 222 GLN 222 222 222 GLN GLN A . n A 1 223 ASN 223 223 223 ASN ASN A . n A 1 224 GLY 224 224 224 GLY GLY A . n A 1 225 ARG 225 225 225 ARG ARG A . n A 1 226 MET 226 226 226 MET MET A . n A 1 227 GLU 227 227 227 GLU GLU A . n A 1 228 PHE 228 228 228 PHE PHE A . n A 1 229 PHE 229 229 229 PHE PHE A . n A 1 230 TRP 230 230 230 TRP TRP A . n A 1 231 THR 231 231 231 THR THR A . n A 1 232 ILE 232 232 232 ILE ILE A . n A 1 233 LEU 233 233 233 LEU LEU A . n A 1 234 LYS 234 234 234 LYS LYS A . n A 1 235 PRO 235 235 235 PRO PRO A . n A 1 236 ASN 236 236 236 ASN ASN A . n A 1 237 ASP 237 237 237 ASP ASP A . n A 1 238 ALA 238 238 238 ALA ALA A . n A 1 239 ILE 239 239 239 ILE ILE A . n A 1 240 ASN 240 240 240 ASN ASN A . n A 1 241 PHE 241 241 241 PHE PHE A . n A 1 242 GLU 242 242 242 GLU GLU A . n A 1 243 SER 243 243 243 SER SER A . n A 1 244 ASN 244 244 244 ASN ASN A . n A 1 245 GLY 245 245 245 GLY GLY A . n A 1 246 ASN 246 246 246 ASN ASN A . n A 1 247 PHE 247 247 247 PHE PHE A . n A 1 248 ILE 248 248 248 ILE ILE A . n A 1 249 ALA 249 249 249 ALA ALA A . n A 1 250 PRO 250 250 250 PRO PRO A . n A 1 251 GLU 251 251 251 GLU GLU A . n A 1 252 TYR 252 252 252 TYR TYR A . n A 1 253 ALA 253 253 253 ALA ALA A . n A 1 254 TYR 254 254 254 TYR TYR A . n A 1 255 LYS 255 255 255 LYS LYS A . n A 1 256 ILE 256 256 256 ILE ILE A . n A 1 257 VAL 257 257 257 VAL VAL A . n A 1 258 LYS 258 258 258 LYS LYS A . n A 1 259 LYS 259 259 259 LYS LYS A . n A 1 260 GLY 260 260 260 GLY GLY A . n A 1 261 ASP 261 261 261 ASP ASP A . n A 1 262 SER 262 262 262 SER SER A . n A 1 263 THR 263 263 263 THR THR A . n A 1 264 ILE 264 264 264 ILE ILE A . n A 1 265 MET 265 265 265 MET MET A . n A 1 266 LYS 266 266 266 LYS LYS A . n A 1 267 SER 267 267 267 SER SER A . n A 1 268 GLU 268 268 268 GLU GLU A . n A 1 269 LEU 269 269 269 LEU LEU A . n A 1 270 GLU 270 270 270 GLU GLU A . n A 1 271 TYR 271 271 271 TYR TYR A . n A 1 272 GLY 272 272 272 GLY GLY A . n A 1 273 ASN 273 273 273 ASN ASN A . n A 1 274 CYS 274 274 274 CYS CYS A . n A 1 275 ASN 275 275 275 ASN ASN A . n A 1 276 THR 276 276 276 THR THR A . n A 1 277 LYS 277 277 277 LYS LYS A . n A 1 278 CYS 278 278 278 CYS CYS A . n A 1 279 GLN 279 279 279 GLN GLN A . n A 1 280 THR 280 280 280 THR THR A . n A 1 281 PRO 281 281 281 PRO PRO A . n A 1 282 MET 282 282 282 MET MET A . n A 1 283 GLY 283 283 283 GLY GLY A . n A 1 284 ALA 284 284 284 ALA ALA A . n A 1 285 ILE 285 285 285 ILE ILE A . n A 1 286 ASN 286 286 286 ASN ASN A . n A 1 287 SER 287 287 287 SER SER A . n A 1 288 SER 288 288 288 SER SER A . n A 1 289 MET 289 289 289 MET MET A . n A 1 290 PRO 290 290 290 PRO PRO A . n A 1 291 PHE 291 291 291 PHE PHE A . n A 1 292 HIS 292 292 292 HIS HIS A . n A 1 293 ASN 293 293 293 ASN ASN A . n A 1 294 ILE 294 294 294 ILE ILE A . n A 1 295 HIS 295 295 295 HIS HIS A . n A 1 296 PRO 296 296 296 PRO PRO A . n A 1 297 LEU 297 297 297 LEU LEU A . n A 1 298 THR 298 298 298 THR THR A . n A 1 299 ILE 299 299 299 ILE ILE A . n A 1 300 GLY 300 300 300 GLY GLY A . n A 1 301 GLU 301 301 301 GLU GLU A . n A 1 302 CYS 302 302 302 CYS CYS A . n A 1 303 PRO 303 303 303 PRO PRO A . n A 1 304 LYS 304 304 304 LYS LYS A . n A 1 305 TYR 305 305 305 TYR TYR A . n A 1 306 VAL 306 306 306 VAL VAL A . n A 1 307 LYS 307 307 307 LYS LYS A . n A 1 308 SER 308 308 308 SER SER A . n A 1 309 ASN 309 309 309 ASN ASN A . n A 1 310 ARG 310 310 310 ARG ARG A . n A 1 311 LEU 311 311 311 LEU LEU A . n A 1 312 VAL 312 312 312 VAL VAL A . n A 1 313 LEU 313 313 313 LEU LEU A . n A 1 314 ALA 314 314 314 ALA ALA A . n A 1 315 THR 315 315 315 THR THR A . n A 1 316 GLY 316 316 316 GLY GLY A . n A 1 317 LEU 317 317 317 LEU LEU A . n A 1 318 ARG 318 318 318 ARG ARG A . n A 1 319 ASN 319 319 319 ASN ASN A . n A 1 320 SER 320 320 320 SER SER A . n A 1 321 PRO 321 321 321 PRO PRO A . n A 1 322 GLN 322 322 ? ? ? A . n A 1 323 ARG 323 323 ? ? ? A . n A 1 324 GLU 324 324 ? ? ? A . n A 1 325 THR 325 325 ? ? ? A . n A 1 326 ARG 326 326 ? ? ? A . n B 2 1 GLY 1 1 1 GLY GLY B . n B 2 2 LEU 2 2 2 LEU LEU B . n B 2 3 PHE 3 3 3 PHE PHE B . n B 2 4 GLY 4 4 4 GLY GLY B . n B 2 5 ALA 5 5 5 ALA ALA B . n B 2 6 ILE 6 6 6 ILE ILE B . n B 2 7 ALA 7 7 7 ALA ALA B . n B 2 8 GLY 8 8 8 GLY GLY B . n B 2 9 PHE 9 9 9 PHE PHE B . n B 2 10 ILE 10 10 10 ILE ILE B . n B 2 11 GLU 11 11 11 GLU GLU B . n B 2 12 GLY 12 12 12 GLY GLY B . n B 2 13 GLY 13 13 13 GLY GLY B . n B 2 14 TRP 14 14 14 TRP TRP B . n B 2 15 GLN 15 15 15 GLN GLN B . n B 2 16 GLY 16 16 16 GLY GLY B . n B 2 17 MET 17 17 17 MET MET B . n B 2 18 VAL 18 18 18 VAL VAL B . n B 2 19 ASP 19 19 19 ASP ASP B . n B 2 20 GLY 20 20 20 GLY GLY B . n B 2 21 TRP 21 21 21 TRP TRP B . n B 2 22 TYR 22 22 22 TYR TYR B . n B 2 23 GLY 23 23 23 GLY GLY B . n B 2 24 TYR 24 24 24 TYR TYR B . n B 2 25 HIS 25 25 25 HIS HIS B . n B 2 26 HIS 26 26 26 HIS HIS B . n B 2 27 SER 27 27 27 SER SER B . n B 2 28 ASN 28 28 28 ASN ASN B . n B 2 29 GLU 29 29 29 GLU GLU B . n B 2 30 GLN 30 30 30 GLN GLN B . n B 2 31 GLY 31 31 31 GLY GLY B . n B 2 32 SER 32 32 32 SER SER B . n B 2 33 GLY 33 33 33 GLY GLY B . n B 2 34 TYR 34 34 34 TYR TYR B . n B 2 35 ALA 35 35 35 ALA ALA B . n B 2 36 ALA 36 36 36 ALA ALA B . n B 2 37 ASP 37 37 37 ASP ASP B . n B 2 38 LYS 38 38 38 LYS LYS B . n B 2 39 GLU 39 39 39 GLU GLU B . n B 2 40 SER 40 40 40 SER SER B . n B 2 41 THR 41 41 41 THR THR B . n B 2 42 GLN 42 42 42 GLN GLN B . n B 2 43 LYS 43 43 43 LYS LYS B . n B 2 44 ALA 44 44 44 ALA ALA B . n B 2 45 ILE 45 45 45 ILE ILE B . n B 2 46 ASP 46 46 46 ASP ASP B . n B 2 47 GLY 47 47 47 GLY GLY B . n B 2 48 VAL 48 48 48 VAL VAL B . n B 2 49 THR 49 49 49 THR THR B . n B 2 50 ASN 50 50 50 ASN ASN B . n B 2 51 LYS 51 51 51 LYS LYS B . n B 2 52 VAL 52 52 52 VAL VAL B . n B 2 53 ASN 53 53 53 ASN ASN B . n B 2 54 SER 54 54 54 SER SER B . n B 2 55 ILE 55 55 55 ILE ILE B . n B 2 56 ILE 56 56 56 ILE ILE B . n B 2 57 ASP 57 57 57 ASP ASP B . n B 2 58 LYS 58 58 58 LYS LYS B . n B 2 59 MET 59 59 59 MET MET B . n B 2 60 ASN 60 60 60 ASN ASN B . n B 2 61 THR 61 61 61 THR THR B . n B 2 62 GLN 62 62 62 GLN GLN B . n B 2 63 PHE 63 63 63 PHE PHE B . n B 2 64 GLU 64 64 64 GLU GLU B . n B 2 65 ALA 65 65 65 ALA ALA B . n B 2 66 VAL 66 66 66 VAL VAL B . n B 2 67 GLY 67 67 67 GLY GLY B . n B 2 68 ARG 68 68 68 ARG ARG B . n B 2 69 GLU 69 69 69 GLU GLU B . n B 2 70 PHE 70 70 70 PHE PHE B . n B 2 71 ASN 71 71 71 ASN ASN B . n B 2 72 ASN 72 72 72 ASN ASN B . n B 2 73 LEU 73 73 73 LEU LEU B . n B 2 74 GLU 74 74 74 GLU GLU B . n B 2 75 ARG 75 75 75 ARG ARG B . n B 2 76 ARG 76 76 76 ARG ARG B . n B 2 77 ILE 77 77 77 ILE ILE B . n B 2 78 GLU 78 78 78 GLU GLU B . n B 2 79 ASN 79 79 79 ASN ASN B . n B 2 80 LEU 80 80 80 LEU LEU B . n B 2 81 ASN 81 81 81 ASN ASN B . n B 2 82 LYS 82 82 82 LYS LYS B . n B 2 83 LYS 83 83 83 LYS LYS B . n B 2 84 MET 84 84 84 MET MET B . n B 2 85 GLU 85 85 85 GLU GLU B . n B 2 86 ASP 86 86 86 ASP ASP B . n B 2 87 GLY 87 87 87 GLY GLY B . n B 2 88 PHE 88 88 88 PHE PHE B . n B 2 89 LEU 89 89 89 LEU LEU B . n B 2 90 ASP 90 90 90 ASP ASP B . n B 2 91 VAL 91 91 91 VAL VAL B . n B 2 92 TRP 92 92 92 TRP TRP B . n B 2 93 THR 93 93 93 THR THR B . n B 2 94 TYR 94 94 94 TYR TYR B . n B 2 95 ASN 95 95 95 ASN ASN B . n B 2 96 ALA 96 96 96 ALA ALA B . n B 2 97 GLU 97 97 97 GLU GLU B . n B 2 98 LEU 98 98 98 LEU LEU B . n B 2 99 LEU 99 99 99 LEU LEU B . n B 2 100 VAL 100 100 100 VAL VAL B . n B 2 101 LEU 101 101 101 LEU LEU B . n B 2 102 MET 102 102 102 MET MET B . n B 2 103 GLU 103 103 103 GLU GLU B . n B 2 104 ASN 104 104 104 ASN ASN B . n B 2 105 GLU 105 105 105 GLU GLU B . n B 2 106 ARG 106 106 106 ARG ARG B . n B 2 107 THR 107 107 107 THR THR B . n B 2 108 LEU 108 108 108 LEU LEU B . n B 2 109 ASP 109 109 109 ASP ASP B . n B 2 110 PHE 110 110 110 PHE PHE B . n B 2 111 HIS 111 111 111 HIS HIS B . n B 2 112 ASP 112 112 112 ASP ASP B . n B 2 113 SER 113 113 113 SER SER B . n B 2 114 ASN 114 114 114 ASN ASN B . n B 2 115 VAL 115 115 115 VAL VAL B . n B 2 116 LYS 116 116 116 LYS LYS B . n B 2 117 ASN 117 117 117 ASN ASN B . n B 2 118 LEU 118 118 118 LEU LEU B . n B 2 119 TYR 119 119 119 TYR TYR B . n B 2 120 ASP 120 120 120 ASP ASP B . n B 2 121 LYS 121 121 121 LYS LYS B . n B 2 122 VAL 122 122 122 VAL VAL B . n B 2 123 ARG 123 123 123 ARG ARG B . n B 2 124 LEU 124 124 124 LEU LEU B . n B 2 125 GLN 125 125 125 GLN GLN B . n B 2 126 LEU 126 126 126 LEU LEU B . n B 2 127 ARG 127 127 127 ARG ARG B . n B 2 128 ASP 128 128 128 ASP ASP B . n B 2 129 ASN 129 129 129 ASN ASN B . n B 2 130 ALA 130 130 130 ALA ALA B . n B 2 131 LYS 131 131 131 LYS LYS B . n B 2 132 GLU 132 132 132 GLU GLU B . n B 2 133 LEU 133 133 133 LEU LEU B . n B 2 134 GLY 134 134 134 GLY GLY B . n B 2 135 ASN 135 135 135 ASN ASN B . n B 2 136 GLY 136 136 136 GLY GLY B . n B 2 137 CYS 137 137 137 CYS CYS B . n B 2 138 PHE 138 138 138 PHE PHE B . n B 2 139 GLU 139 139 139 GLU GLU B . n B 2 140 PHE 140 140 140 PHE PHE B . n B 2 141 TYR 141 141 141 TYR TYR B . n B 2 142 HIS 142 142 142 HIS HIS B . n B 2 143 LYS 143 143 143 LYS LYS B . n B 2 144 CYS 144 144 144 CYS CYS B . n B 2 145 ASP 145 145 145 ASP ASP B . n B 2 146 ASN 146 146 146 ASN ASN B . n B 2 147 GLU 147 147 147 GLU GLU B . n B 2 148 CYS 148 148 148 CYS CYS B . n B 2 149 MET 149 149 149 MET MET B . n B 2 150 GLU 150 150 150 GLU GLU B . n B 2 151 SER 151 151 151 SER SER B . n B 2 152 VAL 152 152 152 VAL VAL B . n B 2 153 ARG 153 153 153 ARG ARG B . n B 2 154 ASN 154 154 154 ASN ASN B . n B 2 155 GLY 155 155 155 GLY GLY B . n B 2 156 THR 156 156 156 THR THR B . n B 2 157 TYR 157 157 157 TYR TYR B . n B 2 158 ASP 158 158 158 ASP ASP B . n B 2 159 TYR 159 159 159 TYR TYR B . n B 2 160 PRO 160 160 160 PRO PRO B . n B 2 161 GLN 161 161 161 GLN GLN B . n B 2 162 TYR 162 162 162 TYR TYR B . n B 2 163 SER 163 163 ? ? ? B . n B 2 164 GLU 164 164 ? ? ? B . n B 2 165 GLU 165 165 ? ? ? B . n B 2 166 ALA 166 166 ? ? ? B . n # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code C 3 NAG 1 1011 1011 NAG NAG A . D 3 NAG 1 1023 1023 NAG NAG A . E 3 NAG 2 1024 1024 NAG NAG A . F 3 NAG 1 1165 1165 NAG NAG A . G 3 NAG 2 1166 1166 NAG NAG A . H 4 MAN 3 1167 1167 MAN MAN A . I 5 BMA 4 1168 1168 BMA BMA A . J 4 MAN 5 1169 1169 MAN MAN A . K 3 NAG 1 1286 1286 NAG NAG A . L 6 MPO 1 1322 1322 MPO MPO A . M 3 NAG 1 1154 1154 NAG NAG B . N 3 NAG 2 1155 1155 NAG NAG B . O 5 BMA 3 1156 1156 BMA BMA B . P 6 MPO 1 1163 1163 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 . 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 . # 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)' 36150 ? 1 MORE -32.9 ? 1 'SSA (A^2)' 64000 ? # 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 50.3175000000 0.8660254038 -0.5000000000 0.0000000000 -87.1524665098 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 100.6350000000 -0.8660254038 -0.5000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 2014-05-28 2 'Structure model' 1 1 2014-06-11 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # _pdbx_audit_revision_group.ordinal 1 _pdbx_audit_revision_group.revision_ordinal 2 _pdbx_audit_revision_group.data_content_type 'Structure model' _pdbx_audit_revision_group.group 'Database references' # loop_ _pdbx_refine_tls.pdbx_refine_id _pdbx_refine_tls.id _pdbx_refine_tls.details _pdbx_refine_tls.method _pdbx_refine_tls.origin_x _pdbx_refine_tls.origin_y _pdbx_refine_tls.origin_z _pdbx_refine_tls.T[1][1] _pdbx_refine_tls.T[2][2] _pdbx_refine_tls.T[3][3] _pdbx_refine_tls.T[1][2] _pdbx_refine_tls.T[1][3] _pdbx_refine_tls.T[2][3] _pdbx_refine_tls.L[1][1] _pdbx_refine_tls.L[2][2] _pdbx_refine_tls.L[3][3] _pdbx_refine_tls.L[1][2] _pdbx_refine_tls.L[1][3] _pdbx_refine_tls.L[2][3] _pdbx_refine_tls.S[1][1] _pdbx_refine_tls.S[1][2] _pdbx_refine_tls.S[1][3] _pdbx_refine_tls.S[2][1] _pdbx_refine_tls.S[2][2] _pdbx_refine_tls.S[2][3] _pdbx_refine_tls.S[3][1] _pdbx_refine_tls.S[3][2] _pdbx_refine_tls.S[3][3] 'X-RAY DIFFRACTION' 1 ? refined 33.0718 -18.0030 -2.9123 0.1641 0.4710 0.0920 -0.1246 0.0753 -0.1370 0.3545 0.7185 2.4414 -0.2670 -0.3298 0.7653 -0.0989 -0.2349 0.0601 0.3027 -0.1381 0.1080 0.5534 -0.4749 0.2370 'X-RAY DIFFRACTION' 2 ? refined 39.8722 -22.7919 -53.3592 0.1134 0.1115 0.2502 0.0381 -0.0176 -0.0460 1.0947 0.5549 8.9723 -0.4464 1.1403 -1.2792 0.0326 0.0905 0.0502 -0.0440 -0.1245 0.1290 0.2298 -0.3292 0.0919 # 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 1286 ? ? ? ? 'X-RAY DIFFRACTION' 2 2 B 1 ? ? B 1156 ? ? ? ? # 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 4CQP _pdbx_entry_details.compound_details ? _pdbx_entry_details.source_details ? _pdbx_entry_details.nonpolymer_details ? _pdbx_entry_details.sequence_details 'MULTIBASIC SITE REMOVED' # _pdbx_validate_close_contact.id 1 _pdbx_validate_close_contact.PDB_model_num 1 _pdbx_validate_close_contact.auth_atom_id_1 OD1 _pdbx_validate_close_contact.auth_asym_id_1 A _pdbx_validate_close_contact.auth_comp_id_1 ASN _pdbx_validate_close_contact.auth_seq_id_1 166 _pdbx_validate_close_contact.PDB_ins_code_1 ? _pdbx_validate_close_contact.label_alt_id_1 ? _pdbx_validate_close_contact.auth_atom_id_2 ND2 _pdbx_validate_close_contact.auth_asym_id_2 A _pdbx_validate_close_contact.auth_comp_id_2 ASN _pdbx_validate_close_contact.auth_seq_id_2 168 _pdbx_validate_close_contact.PDB_ins_code_2 ? _pdbx_validate_close_contact.label_alt_id_2 ? _pdbx_validate_close_contact.dist 2.01 # 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 ? ? 56.90 -117.77 2 1 PRO A 74 ? ? -69.90 -176.94 3 1 ASP A 88 ? ? -105.39 -105.87 4 1 CYS A 135 ? ? -117.31 70.81 5 1 ARG A 192 ? ? 63.19 -61.22 6 1 ARG B 127 ? ? 61.46 -122.80 7 1 THR B 156 ? ? -109.09 46.56 # _pdbx_validate_chiral.id 1 _pdbx_validate_chiral.PDB_model_num 1 _pdbx_validate_chiral.auth_atom_id C1 _pdbx_validate_chiral.label_alt_id ? _pdbx_validate_chiral.auth_asym_id B _pdbx_validate_chiral.auth_comp_id NAG _pdbx_validate_chiral.auth_seq_id 1154 _pdbx_validate_chiral.PDB_ins_code ? _pdbx_validate_chiral.details 'WRONG HAND' _pdbx_validate_chiral.omega . # loop_ _pdbx_unobs_or_zero_occ_residues.id _pdbx_unobs_or_zero_occ_residues.PDB_model_num _pdbx_unobs_or_zero_occ_residues.polymer_flag _pdbx_unobs_or_zero_occ_residues.occupancy_flag _pdbx_unobs_or_zero_occ_residues.auth_asym_id _pdbx_unobs_or_zero_occ_residues.auth_comp_id _pdbx_unobs_or_zero_occ_residues.auth_seq_id _pdbx_unobs_or_zero_occ_residues.PDB_ins_code _pdbx_unobs_or_zero_occ_residues.label_asym_id _pdbx_unobs_or_zero_occ_residues.label_comp_id _pdbx_unobs_or_zero_occ_residues.label_seq_id 1 1 Y 1 A GLN 322 ? A GLN 322 2 1 Y 1 A ARG 323 ? A ARG 323 3 1 Y 1 A GLU 324 ? A GLU 324 4 1 Y 1 A THR 325 ? A THR 325 5 1 Y 1 A ARG 326 ? A ARG 326 6 1 Y 1 B SER 163 ? B SER 163 7 1 Y 1 B GLU 164 ? B GLU 164 8 1 Y 1 B GLU 165 ? B GLU 165 9 1 Y 1 B ALA 166 ? B ALA 166 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 3 N-ACETYL-D-GLUCOSAMINE NAG 4 ALPHA-D-MANNOSE MAN 5 BETA-D-MANNOSE BMA 6 '3[N-MORPHOLINO]PROPANE SULFONIC ACID' MPO 7 water HOH #