data_4CQR # _entry.id 4CQR # _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 4CQR PDBE EBI-59781 WWPDB D_1290059781 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.content_type _pdbx_database_related.details PDB 4CQP unspecified 'CRYSTAL STRUCTURE OF H5 (VN1194) SER227ASN/GLN196ARG MUTANT HAEMAGGLUTININ' PDB 4CQQ unspecified ;H5 (VN1194) SER227ASN/GLN196ARG MUTANT HAEMAGGLUTININ IN COMPLEX WITH AVIAN RECEPTOR ANALOGUE 3'SLN ; PDB 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 4CQR _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 4CQR _cell.length_a 101.077 _cell.length_b 101.077 _cell.length_c 451.337 _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 4CQR _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 BETA-D-MANNOSE 180.156 3 ? ? ? ? 5 non-polymer man ALPHA-D-MANNOSE 180.156 1 ? ? ? ? 6 non-polymer man 'O-SIALIC ACID' 309.270 1 ? ? ? ? 7 non-polymer man BETA-D-GALACTOSE 180.156 1 ? ? ? ? 8 non-polymer syn '3[N-MORPHOLINO]PROPANE SULFONIC ACID' 209.263 1 ? ? ? ? 9 water nat water 18.015 72 ? ? ? ? # 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 4CQR A 1 ? 326 ? Q6DQ34 17 ? 342 ? 1 326 2 2 4CQR 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 4CQR ARG A 192 ? UNP Q6DQ34 GLN 208 'engineered mutation' 192 1 1 4CQR ASN A 223 ? UNP Q6DQ34 SER 239 'engineered mutation' 223 2 1 4CQR 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 GAL D-saccharide . BETA-D-GALACTOSE ? 'C6 H12 O6' 180.156 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MAN D-saccharide . ALPHA-D-MANNOSE ? 'C6 H12 O6' 180.156 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 MPO non-polymer . '3[N-MORPHOLINO]PROPANE SULFONIC ACID' ? 'C7 H15 N O4 S' 209.263 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 SIA non-polymer . 'O-SIALIC ACID' ? 'C11 H19 N O9' 309.270 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 # _exptl.entry_id 4CQR _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 3.74 _exptl_crystal.density_percent_sol 67 _exptl_crystal.description NONE # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method ? _exptl_crystal_grow.temp ? _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH ? _exptl_crystal_grow.pdbx_pH_range ? _exptl_crystal_grow.pdbx_details '0.1 M HEPES/MOPS PH 7.0, 0.05 M MGCL2, 28-30% PEG 550 MME, SEEDED WITH CRUSHED WILD-TYPE VN1194 HA CRYSTALS.' # _diffrn.id 1 _diffrn.ambient_temp 100 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector CCD _diffrn_detector.type 'ADSC CCD' _diffrn_detector.pdbx_collection_date ? _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator ? _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 0.92 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'DIAMOND BEAMLINE I04-1' _diffrn_source.pdbx_synchrotron_site Diamond _diffrn_source.pdbx_synchrotron_beamline I04-1 _diffrn_source.pdbx_wavelength 0.92 _diffrn_source.pdbx_wavelength_list ? # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 4CQR _reflns.observed_criterion_sigma_I 2.1 _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 40.81 _reflns.d_resolution_high 2.45 _reflns.number_obs 33089 _reflns.number_all ? _reflns.percent_possible_obs 99.5 _reflns.pdbx_Rmerge_I_obs 0.07 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 10.50 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 5.3 # _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_ordinal 1 _reflns_shell.d_res_high 2.45 _reflns_shell.d_res_low 2.58 _reflns_shell.percent_possible_all 99.5 _reflns_shell.Rmerge_I_obs 0.62 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs 2.10 _reflns_shell.pdbx_redundancy 5.3 # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 4CQR _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 31397 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F . _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 150.45 _refine.ls_d_res_high 2.45 _refine.ls_percent_reflns_obs 99.17 _refine.ls_R_factor_obs 0.20197 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.20025 _refine.ls_R_factor_R_free 0.23486 _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 1671 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.958 _refine.correlation_coeff_Fo_to_Fc_free 0.937 _refine.B_iso_mean 88.757 _refine.aniso_B[1][1] 3.16 _refine.aniso_B[2][2] 3.16 _refine.aniso_B[3][3] -10.24 _refine.aniso_B[1][2] 1.58 _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 0.264 _refine.pdbx_overall_ESU_R_Free 0.213 _refine.overall_SU_ML 0.190 _refine.pdbx_overall_phase_error ? _refine.overall_SU_B 18.108 _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 201 _refine_hist.number_atoms_solvent 72 _refine_hist.number_atoms_total 4136 _refine_hist.d_res_high 2.45 _refine_hist.d_res_low 150.45 # 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 ? 4176 'X-RAY DIFFRACTION' ? r_bond_other_d 0.001 0.020 ? 3811 'X-RAY DIFFRACTION' ? r_angle_refined_deg 1.092 1.994 ? 5680 'X-RAY DIFFRACTION' ? r_angle_other_deg 0.771 3.003 ? 8751 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 5.477 5.000 ? 483 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg 37.135 25.099 ? 202 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg 14.597 15.000 ? 679 'X-RAY DIFFRACTION' ? r_dihedral_angle_4_deg 15.544 15.000 ? 18 'X-RAY DIFFRACTION' ? r_chiral_restr 0.101 0.200 ? 639 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.003 0.020 ? 4631 '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 1.581 4.893 ? 1932 'X-RAY DIFFRACTION' ? r_mcbond_other 1.577 4.892 ? 1931 'X-RAY DIFFRACTION' ? r_mcangle_it 2.620 7.339 ? 2412 'X-RAY DIFFRACTION' ? r_mcangle_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scbond_it 2.763 5.896 ? 2243 '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 2.450 _refine_ls_shell.d_res_low 2.514 _refine_ls_shell.number_reflns_R_work 2278 _refine_ls_shell.R_factor_R_work 0.325 _refine_ls_shell.percent_reflns_obs 99.05 _refine_ls_shell.R_factor_R_free 0.358 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 123 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? # _struct.entry_id 4CQR _struct.title ;H5 (VN1194) Ser227Asn/Gln196Arg Mutant Haemagglutinin in Complex with Human Receptor Analogue 6'SLN ; _struct.pdbx_descriptor 'HAEMAGGLUTININ HA1, HAEMAGGLUTININ HA2' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 4CQR _struct_keywords.pdbx_keywords 'VIRAL PROTEIN' _struct_keywords.text ;VIRAL PROTEIN, H5N1, INFLUENZA, 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 4 ? J N N 5 ? K N N 3 ? L N N 6 ? M N N 7 ? N N N 3 ? O N N 3 ? P N N 4 ? Q N N 8 ? R N N 9 ? S N N 9 ? # _struct_biol.id 1 # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 1 SER A 56 ? GLY A 63 ? SER A 56 GLY A 63 1 ? 8 HELX_P HELX_P2 2 ASN A 64 ? ILE A 71 ? ASN A 64 ILE A 71 5 ? 8 HELX_P HELX_P3 3 ASP A 97 ? SER A 106 ? ASP A 97 SER A 106 1 ? 10 HELX_P HELX_P4 4 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 ? MET B 59 ? ASP B 37 MET B 59 1 ? 23 HELX_P HELX_P7 7 GLU B 74 ? ARG B 127 ? GLU B 74 ARG B 127 1 ? 54 HELX_P HELX_P8 8 ASP B 145 ? ASN B 154 ? ASP B 145 ASN B 154 1 ? 10 # _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 ? ? ? ? ? ? ? 2.099 ? disulf2 disulf ? ? A CYS 42 SG ? ? ? 1_555 A CYS 274 SG ? ? A CYS 42 A CYS 274 1_555 ? ? ? ? ? ? ? 2.042 ? disulf3 disulf ? ? A CYS 55 SG ? ? ? 1_555 A CYS 67 SG ? ? A CYS 55 A CYS 67 1_555 ? ? ? ? ? ? ? 2.046 ? disulf4 disulf ? ? A CYS 90 SG ? ? ? 1_555 A CYS 135 SG ? ? A CYS 90 A CYS 135 1_555 ? ? ? ? ? ? ? 2.059 ? disulf5 disulf ? ? A CYS 278 SG ? ? ? 1_555 A CYS 302 SG ? ? A CYS 278 A CYS 302 1_555 ? ? ? ? ? ? ? 2.058 ? 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 1322 1_555 ? ? ? ? ? ? ? 1.451 ? covale2 covale ? ? A ASN 23 ND2 ? ? ? 1_555 D NAG . C1 ? ? A ASN 23 A NAG 1323 1_555 ? ? ? ? ? ? ? 1.438 ? covale3 covale ? ? A ASN 165 ND2 ? ? ? 1_555 F NAG . C1 ? ? A ASN 165 A NAG 1325 1_555 ? ? ? ? ? ? ? 1.432 ? covale4 covale ? ? A ASN 286 ND2 ? ? ? 1_555 K NAG . C1 ? ? A ASN 286 A NAG 1330 1_555 ? ? ? ? ? ? ? 1.444 ? covale5 covale ? ? D NAG . O4 ? ? ? 1_555 E NAG . C1 ? ? A NAG 1323 A NAG 1324 1_555 ? ? ? ? ? ? ? 1.443 ? covale6 covale ? ? F NAG . O4 ? ? ? 1_555 G NAG . C1 ? ? A NAG 1325 A NAG 1326 1_555 ? ? ? ? ? ? ? 1.434 ? covale7 covale ? ? G NAG . O4 ? ? ? 1_555 H BMA . C1 ? ? A NAG 1326 A BMA 1327 1_555 ? ? ? ? ? ? ? 1.449 ? covale8 covale ? ? H BMA . O6 ? ? ? 1_555 J MAN . C1 ? ? A BMA 1327 A MAN 1329 1_555 ? ? ? ? ? ? ? 1.449 ? covale9 covale ? ? H BMA . O3 ? ? ? 1_555 I BMA . C1 ? ? A BMA 1327 A BMA 1328 1_555 ? ? ? ? ? ? ? 1.439 ? covale10 covale ? ? L SIA . C2 ? ? ? 1_555 M GAL . O6 ? ? A SIA 1331 A GAL 1332 1_555 ? ? ? ? ? ? ? 1.429 ? covale11 covale ? ? B ASN 154 ND2 ? ? ? 1_555 N NAG . C1 ? ? B ASN 154 B NAG 1163 1_555 ? ? ? ? ? ? ? 1.444 ? covale12 covale ? ? N NAG . O4 ? ? ? 1_555 O NAG . C1 ? ? B NAG 1163 B NAG 1164 1_555 ? ? ? ? ? ? ? 1.442 ? covale13 covale ? ? O NAG . O4 ? ? ? 1_555 P BMA . C1 ? ? B NAG 1164 B BMA 1165 1_555 ? ? ? ? ? ? ? 1.445 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details BA ? 5 ? AA ? 2 ? AB ? 2 ? AC ? 3 ? AD ? 2 ? AE ? 3 ? AF ? 5 ? AG ? 5 ? AH ? 2 ? AI ? 4 ? AJ ? 3 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense BA 1 2 ? anti-parallel BA 2 3 ? anti-parallel BA 3 4 ? anti-parallel BA 4 5 ? anti-parallel AA 1 2 ? anti-parallel AB 1 2 ? anti-parallel AC 1 2 ? parallel AC 2 3 ? parallel AD 1 2 ? parallel AE 1 2 ? parallel AE 2 3 ? parallel AF 1 2 ? parallel AF 2 3 ? anti-parallel AF 3 4 ? anti-parallel AF 4 5 ? anti-parallel AG 1 2 ? parallel AG 2 3 ? anti-parallel AG 3 4 ? anti-parallel AG 4 5 ? anti-parallel AH 1 2 ? anti-parallel AI 1 2 ? anti-parallel AI 2 3 ? anti-parallel AI 3 4 ? anti-parallel AJ 1 2 ? anti-parallel AJ 2 3 ? anti-parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id BA 1 GLY B 31 ? ALA B 36 ? GLY B 31 ALA B 36 BA 2 TYR B 22 ? ASN B 28 ? TYR B 22 ASN B 28 BA 3 GLN A 2 ? TYR A 7 ? GLN A 2 TYR A 7 BA 4 CYS B 137 ? PHE B 140 ? CYS B 137 PHE B 140 BA 5 ALA B 130 ? GLU B 132 ? ALA B 130 GLU B 132 AA 1 GLN A 15 ? VAL A 16 ? GLN A 15 VAL A 16 AA 2 VAL A 24 ? THR A 25 ? VAL A 24 THR A 25 AB 1 ALA A 29 ? ASP A 31 ? ALA A 29 ASP A 31 AB 2 VAL A 312 ? ALA A 314 ? VAL A 312 ALA A 314 AC 1 LEU A 33 ? GLU A 34 ? LEU A 33 GLU A 34 AC 2 PHE A 291 ? HIS A 292 ? PHE A 291 HIS A 292 AC 3 LYS A 304 ? TYR A 305 ? LYS A 304 TYR A 305 AD 1 LEU A 41 ? LEU A 44 ? LEU A 41 LEU A 44 AD 2 TYR A 271 ? THR A 276 ? TYR A 271 THR A 276 AE 1 LEU A 50 ? ILE A 51 ? LEU A 50 ILE A 51 AE 2 ILE A 79 ? GLU A 81 ? ILE A 79 GLU A 81 AE 3 ILE A 264 ? LYS A 266 ? ILE A 264 LYS A 266 AF 1 GLY A 93 ? PHE A 95 ? GLY A 93 PHE A 95 AF 2 ARG A 225 ? LEU A 233 ? ARG A 225 LEU A 233 AF 3 LEU A 172 ? HIS A 180 ? LEU A 172 HIS A 180 AF 4 PHE A 247 ? PRO A 250 ? PHE A 247 PRO A 250 AF 5 VAL A 147 ? TRP A 149 ? VAL A 147 TRP A 149 AG 1 GLY A 93 ? PHE A 95 ? GLY A 93 PHE A 95 AG 2 ARG A 225 ? LEU A 233 ? ARG A 225 LEU A 233 AG 3 LEU A 172 ? HIS A 180 ? LEU A 172 HIS A 180 AG 4 TYR A 252 ? LYS A 259 ? TYR A 252 LYS A 259 AG 5 ILE A 108 ? GLN A 115 ? ILE A 108 GLN A 115 AH 1 SER A 132 ? TYR A 137 ? SER A 132 TYR A 137 AH 2 LYS A 140 ? SER A 142 ? LYS A 140 SER A 142 AI 1 ILE A 160 ? ASN A 165 ? ILE A 160 ASN A 165 AI 2 ALA A 238 ? SER A 243 ? ALA A 238 SER A 243 AI 3 ILE A 198 ? GLY A 201 ? ILE A 198 GLY A 201 AI 4 ASN A 206 ? LEU A 209 ? ASN A 206 LEU A 209 AJ 1 GLY A 283 ? ALA A 284 ? GLY A 283 ALA A 284 AJ 2 CYS A 278 ? THR A 280 ? CYS A 278 THR A 280 AJ 3 ILE A 299 ? GLY A 300 ? ILE A 299 GLY A 300 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id BA 1 2 N ALA B 35 ? N ALA B 35 O TYR B 24 ? O TYR B 24 BA 2 3 N SER B 27 ? N SER B 27 O GLN A 2 ? O GLN A 2 BA 3 4 N ILE A 3 ? N ILE A 3 O PHE B 138 ? O PHE B 138 BA 4 5 N GLU B 139 ? N GLU B 139 O LYS B 131 ? O LYS B 131 AA 1 2 N VAL A 16 ? N VAL A 16 O VAL A 24 ? O VAL A 24 AB 1 2 N GLN A 30 ? N GLN A 30 O LEU A 313 ? O LEU A 313 AC 1 2 N GLU A 34 ? N GLU A 34 O PHE A 291 ? O PHE A 291 AC 2 3 N HIS A 292 ? N HIS A 292 O LYS A 304 ? O LYS A 304 AD 1 2 O LEU A 41 ? O LEU A 41 N GLY A 272 ? N GLY A 272 AE 1 2 O LEU A 50 ? O LEU A 50 N VAL A 80 ? N VAL A 80 AE 2 3 N GLU A 81 ? N GLU A 81 O MET A 265 ? O MET A 265 AF 1 2 N ASP A 94 ? N ASP A 94 O MET A 226 ? O MET A 226 AF 2 3 N LEU A 233 ? N LEU A 233 O LEU A 172 ? O LEU A 172 AF 3 4 N GLY A 177 ? N GLY A 177 O ILE A 248 ? O ILE A 248 AF 4 5 N ALA A 249 ? N ALA A 249 O VAL A 148 ? O VAL A 148 AG 1 2 N ASP A 94 ? N ASP A 94 O MET A 226 ? O MET A 226 AG 2 3 N LEU A 233 ? N LEU A 233 O LEU A 172 ? O LEU A 172 AG 3 4 N LEU A 173 ? N LEU A 173 O TYR A 254 ? O TYR A 254 AG 4 5 O LYS A 258 ? O LYS A 258 N ASN A 109 ? N ASN A 109 AH 1 2 N TYR A 137 ? N TYR A 137 O LYS A 140 ? O LYS A 140 AI 1 2 N TYR A 164 ? N TYR A 164 O ILE A 239 ? O ILE A 239 AI 2 3 N GLU A 242 ? N GLU A 242 O SER A 199 ? O SER A 199 AI 3 4 N VAL A 200 ? N VAL A 200 O GLN A 207 ? O GLN A 207 AJ 1 2 N GLY A 283 ? N GLY A 283 O THR A 280 ? O THR A 280 AJ 2 3 N GLN A 279 ? N GLN A 279 O ILE A 299 ? O ILE A 299 # loop_ _struct_site.id _struct_site.pdbx_evidence_code _struct_site.pdbx_auth_asym_id _struct_site.pdbx_auth_comp_id _struct_site.pdbx_auth_seq_id _struct_site.pdbx_auth_ins_code _struct_site.pdbx_num_residues _struct_site.details AC1 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE MPO B 1166' AC2 Software ? ? ? ? 2 'Binding site for Mono-Saccharide NAG A1322 bound to ASN A 11' AC3 Software ? ? ? ? 2 'Binding site for Poly-Saccharide residues NAG A1323 through NAG A1324 bound to ASN A 23' AC4 Software ? ? ? ? 5 'Binding site for Poly-Saccharide residues NAG A1325 through MAN A1329 bound to ASN A 165' AC5 Software ? ? ? ? 1 'Binding site for Mono-Saccharide NAG A1330 bound to ASN A 286' AC6 Software ? ? ? ? 3 'Binding site for Poly-Saccharide residues NAG B1163 through BMA B1165 bound to ASN B 154' AC7 Software ? ? ? ? 11 'Binding site for Poly-Saccharide residues SIA A1331 through GAL A1332' # 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 TYR B 34 ? TYR B 34 . ? 1_555 ? 5 AC1 5 ASN B 135 ? ASN B 135 . ? 1_555 ? 6 AC2 2 ASN A 11 ? ASN A 11 . ? 1_555 ? 7 AC2 2 HOH R . ? HOH A 2007 . ? 1_555 ? 8 AC3 2 LYS A 22 ? LYS A 22 . ? 1_555 ? 9 AC3 2 ASN A 23 ? ASN A 23 . ? 1_555 ? 10 AC4 5 ASN A 165 ? ASN A 165 . ? 1_555 ? 11 AC4 5 SER A 217 ? SER A 217 . ? 2_545 ? 12 AC4 5 ASN A 236 ? ASN A 236 . ? 1_555 ? 13 AC4 5 HIS A 295 ? HIS A 295 . ? 4_545 ? 14 AC4 5 HOH R . ? HOH A 2034 . ? 4_545 ? 15 AC5 1 ASN A 286 ? ASN A 286 . ? 1_555 ? 16 AC6 3 GLU B 147 ? GLU B 147 . ? 1_555 ? 17 AC6 3 GLU B 150 ? GLU B 150 . ? 1_555 ? 18 AC6 3 ASN B 154 ? ASN B 154 . ? 1_555 ? 19 AC7 11 TYR A 91 ? TYR A 91 . ? 1_555 ? 20 AC7 11 LEU A 129 ? LEU A 129 . ? 1_555 ? 21 AC7 11 VAL A 131 ? VAL A 131 . ? 1_555 ? 22 AC7 11 SER A 132 ? SER A 132 . ? 1_555 ? 23 AC7 11 SER A 133 ? SER A 133 . ? 1_555 ? 24 AC7 11 HIS A 179 ? HIS A 179 . ? 1_555 ? 25 AC7 11 GLU A 186 ? GLU A 186 . ? 1_555 ? 26 AC7 11 LEU A 190 ? LEU A 190 . ? 1_555 ? 27 AC7 11 LYS A 218 ? LYS A 218 . ? 1_555 ? 28 AC7 11 GLY A 221 ? GLY A 221 . ? 1_555 ? 29 AC7 11 GLN A 222 ? GLN A 222 . ? 1_555 ? # _database_PDB_matrix.entry_id 4CQR _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 4CQR _atom_sites.fract_transf_matrix[1][1] 0.009893 _atom_sites.fract_transf_matrix[1][2] 0.005712 _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] 0.011424 _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] 0.002216 _atom_sites.fract_transf_vector[1] 0.00000 _atom_sites.fract_transf_vector[2] 0.00000 _atom_sites.fract_transf_vector[3] 0.00000 # loop_ _atom_type.symbol C N O S # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 N N . ASP A 1 1 ? 37.013 -15.325 -83.469 1.00 74.45 ? 1 ASP A N 1 ATOM 2 C CA . ASP A 1 1 ? 36.153 -15.925 -82.415 1.00 74.15 ? 1 ASP A CA 1 ATOM 3 C C . ASP A 1 1 ? 37.011 -16.639 -81.392 1.00 71.55 ? 1 ASP A C 1 ATOM 4 O O . ASP A 1 1 ? 37.878 -17.426 -81.760 1.00 68.85 ? 1 ASP A O 1 ATOM 5 C CB . ASP A 1 1 ? 35.173 -16.926 -83.019 1.00 74.97 ? 1 ASP A CB 1 ATOM 6 C CG . ASP A 1 1 ? 34.240 -16.295 -84.015 1.00 78.50 ? 1 ASP A CG 1 ATOM 7 O OD1 . ASP A 1 1 ? 34.344 -15.072 -84.257 1.00 79.14 ? 1 ASP A OD1 1 ATOM 8 O OD2 . ASP A 1 1 ? 33.396 -17.035 -84.559 1.00 83.71 ? 1 ASP A OD2 1 ATOM 9 N N . GLN A 1 2 ? 36.773 -16.361 -80.113 1.00 72.24 ? 2 GLN A N 1 ATOM 10 C CA . GLN A 1 2 ? 37.529 -17.012 -79.053 1.00 69.14 ? 2 GLN A CA 1 ATOM 11 C C . GLN A 1 2 ? 36.717 -17.303 -77.812 1.00 67.59 ? 2 GLN A C 1 ATOM 12 O O . GLN A 1 2 ? 35.678 -16.675 -77.554 1.00 67.94 ? 2 GLN A O 1 ATOM 13 C CB . GLN A 1 2 ? 38.766 -16.196 -78.671 1.00 70.48 ? 2 GLN A CB 1 ATOM 14 C CG . GLN A 1 2 ? 38.516 -14.803 -78.137 1.00 74.44 ? 2 GLN A CG 1 ATOM 15 C CD . GLN A 1 2 ? 39.814 -14.051 -77.887 1.00 76.49 ? 2 GLN A CD 1 ATOM 16 O OE1 . GLN A 1 2 ? 40.068 -13.583 -76.781 1.00 77.60 ? 2 GLN A OE1 1 ATOM 17 N NE2 . GLN A 1 2 ? 40.646 -13.938 -78.921 1.00 79.09 ? 2 GLN A NE2 1 ATOM 18 N N . ILE A 1 3 ? 37.207 -18.285 -77.063 1.00 63.21 ? 3 ILE A N 1 ATOM 19 C CA . ILE A 1 3 ? 36.673 -18.609 -75.763 1.00 63.34 ? 3 ILE A CA 1 ATOM 20 C C . ILE A 1 3 ? 37.833 -18.568 -74.785 1.00 62.90 ? 3 ILE A C 1 ATOM 21 O O . ILE A 1 3 ? 38.933 -19.031 -75.097 1.00 62.07 ? 3 ILE A O 1 ATOM 22 C CB . ILE A 1 3 ? 35.946 -19.970 -75.755 1.00 64.42 ? 3 ILE A CB 1 ATOM 23 C CG1 . ILE A 1 3 ? 35.285 -20.214 -74.402 1.00 65.68 ? 3 ILE A CG1 1 ATOM 24 C CG2 . ILE A 1 3 ? 36.882 -21.124 -76.073 1.00 63.49 ? 3 ILE A CG2 1 ATOM 25 C CD1 . ILE A 1 3 ? 34.123 -21.180 -74.486 1.00 67.99 ? 3 ILE A CD1 1 ATOM 26 N N . CYS A 1 4 ? 37.592 -17.983 -73.617 1.00 63.35 ? 4 CYS A N 1 ATOM 27 C CA . CYS A 1 4 ? 38.634 -17.773 -72.626 1.00 62.61 ? 4 CYS A CA 1 ATOM 28 C C . CYS A 1 4 ? 38.234 -18.446 -71.340 1.00 60.12 ? 4 CYS A C 1 ATOM 29 O O . CYS A 1 4 ? 37.048 -18.518 -71.017 1.00 60.41 ? 4 CYS A O 1 ATOM 30 C CB . CYS A 1 4 ? 38.833 -16.278 -72.360 1.00 65.42 ? 4 CYS A CB 1 ATOM 31 S SG . CYS A 1 4 ? 39.347 -15.320 -73.806 1.00 74.77 ? 4 CYS A SG 1 ATOM 32 N N . ILE A 1 5 ? 39.224 -18.929 -70.599 1.00 55.81 ? 5 ILE A N 1 ATOM 33 C CA . ILE A 1 5 ? 38.997 -19.430 -69.257 1.00 54.63 ? 5 ILE A CA 1 ATOM 34 C C . ILE A 1 5 ? 39.484 -18.406 -68.246 1.00 53.96 ? 5 ILE A C 1 ATOM 35 O O . ILE A 1 5 ? 40.536 -17.808 -68.428 1.00 53.48 ? 5 ILE A O 1 ATOM 36 C CB . ILE A 1 5 ? 39.735 -20.745 -69.036 1.00 53.21 ? 5 ILE A CB 1 ATOM 37 C CG1 . ILE A 1 5 ? 39.311 -21.750 -70.095 1.00 54.90 ? 5 ILE A CG1 1 ATOM 38 C CG2 . ILE A 1 5 ? 39.476 -21.276 -67.636 1.00 53.22 ? 5 ILE A CG2 1 ATOM 39 C CD1 . ILE A 1 5 ? 37.905 -22.266 -69.914 1.00 57.66 ? 5 ILE A CD1 1 ATOM 40 N N . GLY A 1 6 ? 38.716 -18.210 -67.179 1.00 54.32 ? 6 GLY A N 1 ATOM 41 C CA . GLY A 1 6 ? 39.056 -17.209 -66.182 1.00 54.03 ? 6 GLY A CA 1 ATOM 42 C C . GLY A 1 6 ? 38.391 -17.436 -64.853 1.00 53.35 ? 6 GLY A C 1 ATOM 43 O O . GLY A 1 6 ? 37.706 -18.433 -64.658 1.00 56.56 ? 6 GLY A O 1 ATOM 44 N N . TYR A 1 7 ? 38.587 -16.492 -63.943 1.00 52.75 ? 7 TYR A N 1 ATOM 45 C CA . TYR A 1 7 ? 38.113 -16.629 -62.584 1.00 53.78 ? 7 TYR A CA 1 ATOM 46 C C . TYR A 1 7 ? 37.563 -15.311 -62.054 1.00 55.69 ? 7 TYR A C 1 ATOM 47 O O . TYR A 1 7 ? 37.747 -14.259 -62.646 1.00 55.85 ? 7 TYR A O 1 ATOM 48 C CB . TYR A 1 7 ? 39.238 -17.158 -61.678 1.00 53.55 ? 7 TYR A CB 1 ATOM 49 C CG . TYR A 1 7 ? 40.517 -16.357 -61.744 1.00 53.60 ? 7 TYR A CG 1 ATOM 50 C CD1 . TYR A 1 7 ? 41.469 -16.605 -62.716 1.00 52.42 ? 7 TYR A CD1 1 ATOM 51 C CD2 . TYR A 1 7 ? 40.762 -15.334 -60.832 1.00 55.79 ? 7 TYR A CD2 1 ATOM 52 C CE1 . TYR A 1 7 ? 42.623 -15.841 -62.787 1.00 54.48 ? 7 TYR A CE1 1 ATOM 53 C CE2 . TYR A 1 7 ? 41.917 -14.577 -60.891 1.00 54.63 ? 7 TYR A CE2 1 ATOM 54 C CZ . TYR A 1 7 ? 42.843 -14.834 -61.862 1.00 54.29 ? 7 TYR A CZ 1 ATOM 55 O OH . TYR A 1 7 ? 43.987 -14.069 -61.905 1.00 55.67 ? 7 TYR A OH 1 ATOM 56 N N . HIS A 1 8 ? 36.895 -15.405 -60.917 1.00 56.72 ? 8 HIS A N 1 ATOM 57 C CA . HIS A 1 8 ? 36.152 -14.314 -60.319 1.00 60.08 ? 8 HIS A CA 1 ATOM 58 C C . HIS A 1 8 ? 37.051 -13.269 -59.659 1.00 61.45 ? 8 HIS A C 1 ATOM 59 O O . HIS A 1 8 ? 38.051 -13.597 -59.019 1.00 59.99 ? 8 HIS A O 1 ATOM 60 C CB . HIS A 1 8 ? 35.222 -14.924 -59.271 1.00 60.53 ? 8 HIS A CB 1 ATOM 61 C CG . HIS A 1 8 ? 34.362 -13.941 -58.548 1.00 62.17 ? 8 HIS A CG 1 ATOM 62 N ND1 . HIS A 1 8 ? 33.302 -13.295 -59.146 1.00 65.27 ? 8 HIS A ND1 1 ATOM 63 C CD2 . HIS A 1 8 ? 34.359 -13.550 -57.251 1.00 61.56 ? 8 HIS A CD2 1 ATOM 64 C CE1 . HIS A 1 8 ? 32.702 -12.523 -58.257 1.00 65.05 ? 8 HIS A CE1 1 ATOM 65 N NE2 . HIS A 1 8 ? 33.321 -12.663 -57.098 1.00 63.40 ? 8 HIS A NE2 1 ATOM 66 N N . ALA A 1 9 ? 36.673 -12.006 -59.810 1.00 63.23 ? 9 ALA A N 1 ATOM 67 C CA . ALA A 1 9 ? 37.244 -10.929 -59.010 1.00 62.69 ? 9 ALA A CA 1 ATOM 68 C C . ALA A 1 9 ? 36.102 -10.076 -58.491 1.00 65.19 ? 9 ALA A C 1 ATOM 69 O O . ALA A 1 9 ? 34.984 -10.162 -58.986 1.00 67.85 ? 9 ALA A O 1 ATOM 70 C CB . ALA A 1 9 ? 38.209 -10.102 -59.836 1.00 62.35 ? 9 ALA A CB 1 ATOM 71 N N . ASN A 1 10 ? 36.371 -9.272 -57.474 1.00 65.60 ? 10 ASN A N 1 ATOM 72 C CA . ASN A 1 10 ? 35.360 -8.386 -56.934 1.00 67.41 ? 10 ASN A CA 1 ATOM 73 C C . ASN A 1 10 ? 36.003 -7.203 -56.216 1.00 70.34 ? 10 ASN A C 1 ATOM 74 O O . ASN A 1 10 ? 37.205 -7.019 -56.305 1.00 68.31 ? 10 ASN A O 1 ATOM 75 C CB . ASN A 1 10 ? 34.408 -9.173 -56.027 1.00 66.79 ? 10 ASN A CB 1 ATOM 76 C CG . ASN A 1 10 ? 35.067 -9.660 -54.756 1.00 65.19 ? 10 ASN A CG 1 ATOM 77 O OD1 . ASN A 1 10 ? 36.252 -9.423 -54.520 1.00 64.00 ? 10 ASN A OD1 1 ATOM 78 N ND2 . ASN A 1 10 ? 34.296 -10.350 -53.924 1.00 64.15 ? 10 ASN A ND2 1 ATOM 79 N N . ASN A 1 11 ? 35.204 -6.404 -55.517 1.00 78.58 ? 11 ASN A N 1 ATOM 80 C CA . ASN A 1 11 ? 35.701 -5.191 -54.855 1.00 84.78 ? 11 ASN A CA 1 ATOM 81 C C . ASN A 1 11 ? 36.240 -5.429 -53.436 1.00 80.33 ? 11 ASN A C 1 ATOM 82 O O . ASN A 1 11 ? 36.505 -4.474 -52.703 1.00 80.70 ? 11 ASN A O 1 ATOM 83 C CB . ASN A 1 11 ? 34.605 -4.103 -54.841 1.00 94.50 ? 11 ASN A CB 1 ATOM 84 C CG . ASN A 1 11 ? 33.313 -4.562 -54.172 1.00 106.16 ? 11 ASN A CG 1 ATOM 85 O OD1 . ASN A 1 11 ? 33.268 -5.622 -53.543 1.00 106.43 ? 11 ASN A OD1 1 ATOM 86 N ND2 . ASN A 1 11 ? 32.248 -3.759 -54.314 1.00 123.65 ? 11 ASN A ND2 1 ATOM 87 N N . SER A 1 12 ? 36.402 -6.697 -53.062 1.00 76.05 ? 12 SER A N 1 ATOM 88 C CA . SER A 1 12 ? 36.820 -7.072 -51.715 1.00 73.26 ? 12 SER A CA 1 ATOM 89 C C . SER A 1 12 ? 38.235 -6.600 -51.407 1.00 71.98 ? 12 SER A C 1 ATOM 90 O O . SER A 1 12 ? 39.116 -6.656 -52.264 1.00 68.61 ? 12 SER A O 1 ATOM 91 C CB . SER A 1 12 ? 36.753 -8.593 -51.536 1.00 71.84 ? 12 SER A CB 1 ATOM 92 O OG . SER A 1 12 ? 37.149 -8.977 -50.230 1.00 69.91 ? 12 SER A OG 1 ATOM 93 N N . THR A 1 13 ? 38.420 -6.125 -50.174 1.00 73.00 ? 13 THR A N 1 ATOM 94 C CA . THR A 1 13 ? 39.719 -5.712 -49.650 1.00 72.05 ? 13 THR A CA 1 ATOM 95 C C . THR A 1 13 ? 40.161 -6.601 -48.489 1.00 70.14 ? 13 THR A C 1 ATOM 96 O O . THR A 1 13 ? 41.222 -6.369 -47.917 1.00 68.56 ? 13 THR A O 1 ATOM 97 C CB . THR A 1 13 ? 39.678 -4.247 -49.151 1.00 75.48 ? 13 THR A CB 1 ATOM 98 O OG1 . THR A 1 13 ? 38.696 -4.116 -48.112 1.00 76.66 ? 13 THR A OG1 1 ATOM 99 C CG2 . THR A 1 13 ? 39.343 -3.293 -50.289 1.00 75.18 ? 13 THR A CG2 1 ATOM 100 N N . GLU A 1 14 ? 39.349 -7.608 -48.150 1.00 69.93 ? 14 GLU A N 1 ATOM 101 C CA . GLU A 1 14 ? 39.684 -8.602 -47.123 1.00 70.18 ? 14 GLU A CA 1 ATOM 102 C C . GLU A 1 14 ? 41.026 -9.275 -47.415 1.00 65.85 ? 14 GLU A C 1 ATOM 103 O O . GLU A 1 14 ? 41.321 -9.613 -48.562 1.00 64.18 ? 14 GLU A O 1 ATOM 104 C CB . GLU A 1 14 ? 38.608 -9.691 -47.046 1.00 74.61 ? 14 GLU A CB 1 ATOM 105 C CG . GLU A 1 14 ? 37.227 -9.222 -46.613 1.00 80.43 ? 14 GLU A CG 1 ATOM 106 C CD . GLU A 1 14 ? 37.168 -8.833 -45.148 1.00 86.76 ? 14 GLU A CD 1 ATOM 107 O OE1 . GLU A 1 14 ? 37.706 -9.603 -44.317 1.00 89.69 ? 14 GLU A OE1 1 ATOM 108 O OE2 . GLU A 1 14 ? 36.589 -7.758 -44.833 1.00 91.42 ? 14 GLU A OE2 1 ATOM 109 N N . GLN A 1 15 ? 41.817 -9.475 -46.365 1.00 64.27 ? 15 GLN A N 1 ATOM 110 C CA . GLN A 1 15 ? 43.174 -9.999 -46.473 1.00 61.66 ? 15 GLN A CA 1 ATOM 111 C C . GLN A 1 15 ? 43.359 -11.224 -45.586 1.00 58.60 ? 15 GLN A C 1 ATOM 112 O O . GLN A 1 15 ? 42.800 -11.295 -44.501 1.00 57.32 ? 15 GLN A O 1 ATOM 113 C CB . GLN A 1 15 ? 44.170 -8.933 -46.037 1.00 64.24 ? 15 GLN A CB 1 ATOM 114 C CG . GLN A 1 15 ? 44.304 -7.764 -46.992 1.00 68.72 ? 15 GLN A CG 1 ATOM 115 C CD . GLN A 1 15 ? 45.300 -6.719 -46.520 1.00 72.39 ? 15 GLN A CD 1 ATOM 116 O OE1 . GLN A 1 15 ? 45.781 -5.912 -47.312 1.00 75.65 ? 15 GLN A OE1 1 ATOM 117 N NE2 . GLN A 1 15 ? 45.611 -6.724 -45.227 1.00 73.65 ? 15 GLN A NE2 1 ATOM 118 N N . VAL A 1 16 ? 44.154 -12.182 -46.047 1.00 56.71 ? 16 VAL A N 1 ATOM 119 C CA . VAL A 1 16 ? 44.498 -13.358 -45.251 1.00 54.71 ? 16 VAL A CA 1 ATOM 120 C C . VAL A 1 16 ? 46.002 -13.506 -45.272 1.00 54.99 ? 16 VAL A C 1 ATOM 121 O O . VAL A 1 16 ? 46.643 -13.040 -46.210 1.00 55.09 ? 16 VAL A O 1 ATOM 122 C CB . VAL A 1 16 ? 43.841 -14.644 -45.803 1.00 53.64 ? 16 VAL A CB 1 ATOM 123 C CG1 . VAL A 1 16 ? 42.335 -14.486 -45.835 1.00 54.85 ? 16 VAL A CG1 1 ATOM 124 C CG2 . VAL A 1 16 ? 44.367 -14.995 -47.189 1.00 52.96 ? 16 VAL A CG2 1 ATOM 125 N N . ASP A 1 17 ? 46.564 -14.146 -44.247 1.00 55.96 ? 17 ASP A N 1 ATOM 126 C CA . ASP A 1 17 ? 47.996 -14.450 -44.232 1.00 57.37 ? 17 ASP A CA 1 ATOM 127 C C . ASP A 1 17 ? 48.265 -15.902 -44.619 1.00 56.47 ? 17 ASP A C 1 ATOM 128 O O . ASP A 1 17 ? 47.437 -16.786 -44.386 1.00 52.92 ? 17 ASP A O 1 ATOM 129 C CB . ASP A 1 17 ? 48.586 -14.176 -42.849 1.00 60.96 ? 17 ASP A CB 1 ATOM 130 C CG . ASP A 1 17 ? 48.671 -12.677 -42.521 1.00 65.62 ? 17 ASP A CG 1 ATOM 131 O OD1 . ASP A 1 17 ? 48.923 -11.846 -43.432 1.00 64.10 ? 17 ASP A OD1 1 ATOM 132 O OD2 . ASP A 1 17 ? 48.502 -12.337 -41.326 1.00 70.75 ? 17 ASP A OD2 1 ATOM 133 N N . THR A 1 18 ? 49.429 -16.133 -45.224 1.00 58.46 ? 18 THR A N 1 ATOM 134 C CA . THR A 1 18 ? 49.948 -17.484 -45.472 1.00 57.69 ? 18 THR A CA 1 ATOM 135 C C . THR A 1 18 ? 51.397 -17.551 -44.995 1.00 59.17 ? 18 THR A C 1 ATOM 136 O O . THR A 1 18 ? 51.965 -16.549 -44.581 1.00 62.96 ? 18 THR A O 1 ATOM 137 C CB . THR A 1 18 ? 49.881 -17.868 -46.972 1.00 57.84 ? 18 THR A CB 1 ATOM 138 O OG1 . THR A 1 18 ? 50.812 -17.085 -47.724 1.00 58.14 ? 18 THR A OG1 1 ATOM 139 C CG2 . THR A 1 18 ? 48.500 -17.633 -47.529 1.00 59.47 ? 18 THR A CG2 1 ATOM 140 N N . ILE A 1 19 ? 51.993 -18.734 -45.059 1.00 62.59 ? 19 ILE A N 1 ATOM 141 C CA . ILE A 1 19 ? 53.371 -18.948 -44.613 1.00 61.03 ? 19 ILE A CA 1 ATOM 142 C C . ILE A 1 19 ? 54.356 -18.119 -45.445 1.00 61.85 ? 19 ILE A C 1 ATOM 143 O O . ILE A 1 19 ? 55.295 -17.524 -44.906 1.00 59.49 ? 19 ILE A O 1 ATOM 144 C CB . ILE A 1 19 ? 53.738 -20.442 -44.738 1.00 66.49 ? 19 ILE A CB 1 ATOM 145 C CG1 . ILE A 1 19 ? 52.871 -21.306 -43.810 1.00 71.93 ? 19 ILE A CG1 1 ATOM 146 C CG2 . ILE A 1 19 ? 55.203 -20.684 -44.438 1.00 69.26 ? 19 ILE A CG2 1 ATOM 147 C CD1 . ILE A 1 19 ? 53.166 -21.149 -42.333 1.00 72.26 ? 19 ILE A CD1 1 ATOM 148 N N . MET A 1 20 ? 54.131 -18.079 -46.757 1.00 61.34 ? 20 MET A N 1 ATOM 149 C CA . MET A 1 20 ? 55.031 -17.393 -47.684 1.00 63.62 ? 20 MET A CA 1 ATOM 150 C C . MET A 1 20 ? 54.644 -15.952 -48.010 1.00 63.88 ? 20 MET A C 1 ATOM 151 O O . MET A 1 20 ? 55.448 -15.218 -48.588 1.00 62.96 ? 20 MET A O 1 ATOM 152 C CB . MET A 1 20 ? 55.121 -18.163 -48.995 1.00 65.97 ? 20 MET A CB 1 ATOM 153 C CG . MET A 1 20 ? 55.844 -19.486 -48.880 1.00 69.34 ? 20 MET A CG 1 ATOM 154 S SD . MET A 1 20 ? 56.381 -20.066 -50.489 1.00 73.83 ? 20 MET A SD 1 ATOM 155 C CE . MET A 1 20 ? 56.350 -21.842 -50.219 1.00 84.28 ? 20 MET A CE 1 ATOM 156 N N . GLU A 1 21 ? 53.425 -15.549 -47.676 1.00 61.34 ? 21 GLU A N 1 ATOM 157 C CA . GLU A 1 21 ? 52.969 -14.219 -48.033 1.00 62.62 ? 21 GLU A CA 1 ATOM 158 C C . GLU A 1 21 ? 51.935 -13.714 -47.050 1.00 63.05 ? 21 GLU A C 1 ATOM 159 O O . GLU A 1 21 ? 50.987 -14.416 -46.705 1.00 63.59 ? 21 GLU A O 1 ATOM 160 C CB . GLU A 1 21 ? 52.392 -14.208 -49.445 1.00 64.02 ? 21 GLU A CB 1 ATOM 161 C CG . GLU A 1 21 ? 52.349 -12.820 -50.071 1.00 69.19 ? 21 GLU A CG 1 ATOM 162 C CD . GLU A 1 21 ? 51.828 -12.821 -51.505 1.00 74.05 ? 21 GLU A CD 1 ATOM 163 O OE1 . GLU A 1 21 ? 51.743 -13.919 -52.118 1.00 72.39 ? 21 GLU A OE1 1 ATOM 164 O OE2 . GLU A 1 21 ? 51.507 -11.715 -52.017 1.00 73.12 ? 21 GLU A OE2 1 ATOM 165 N N . LYS A 1 22 ? 52.130 -12.482 -46.604 1.00 64.94 ? 22 LYS A N 1 ATOM 166 C CA . LYS A 1 22 ? 51.207 -11.857 -45.689 1.00 66.92 ? 22 LYS A CA 1 ATOM 167 C C . LYS A 1 22 ? 50.308 -10.901 -46.460 1.00 62.33 ? 22 LYS A C 1 ATOM 168 O O . LYS A 1 22 ? 50.668 -10.425 -47.534 1.00 59.70 ? 22 LYS A O 1 ATOM 169 C CB . LYS A 1 22 ? 51.987 -11.136 -44.598 1.00 73.35 ? 22 LYS A CB 1 ATOM 170 C CG . LYS A 1 22 ? 52.701 -12.085 -43.648 1.00 79.44 ? 22 LYS A CG 1 ATOM 171 C CD . LYS A 1 22 ? 53.346 -11.323 -42.492 1.00 90.18 ? 22 LYS A CD 1 ATOM 172 C CE . LYS A 1 22 ? 53.418 -12.149 -41.211 1.00 94.05 ? 22 LYS A CE 1 ATOM 173 N NZ . LYS A 1 22 ? 53.615 -11.295 -40.002 1.00 95.15 ? 22 LYS A NZ 1 ATOM 174 N N . ASN A 1 23 ? 49.123 -10.651 -45.927 1.00 61.16 ? 23 ASN A N 1 ATOM 175 C CA . ASN A 1 23 ? 48.239 -9.625 -46.481 1.00 64.92 ? 23 ASN A CA 1 ATOM 176 C C . ASN A 1 23 ? 47.881 -9.855 -47.937 1.00 62.14 ? 23 ASN A C 1 ATOM 177 O O . ASN A 1 23 ? 47.976 -8.951 -48.756 1.00 63.27 ? 23 ASN A O 1 ATOM 178 C CB . ASN A 1 23 ? 48.866 -8.234 -46.295 1.00 67.61 ? 23 ASN A CB 1 ATOM 179 C CG . ASN A 1 23 ? 48.946 -7.829 -44.841 1.00 72.99 ? 23 ASN A CG 1 ATOM 180 O OD1 . ASN A 1 23 ? 48.321 -8.454 -43.981 1.00 71.14 ? 23 ASN A OD1 1 ATOM 181 N ND2 . ASN A 1 23 ? 49.710 -6.781 -44.555 1.00 83.70 ? 23 ASN A ND2 1 ATOM 182 N N . VAL A 1 24 ? 47.468 -11.080 -48.243 1.00 60.65 ? 24 VAL A N 1 ATOM 183 C CA . VAL A 1 24 ? 46.996 -11.442 -49.573 1.00 57.50 ? 24 VAL A CA 1 ATOM 184 C C . VAL A 1 24 ? 45.525 -11.063 -49.659 1.00 58.21 ? 24 VAL A C 1 ATOM 185 O O . VAL A 1 24 ? 44.728 -11.459 -48.810 1.00 58.78 ? 24 VAL A O 1 ATOM 186 C CB . VAL A 1 24 ? 47.143 -12.954 -49.815 1.00 55.84 ? 24 VAL A CB 1 ATOM 187 C CG1 . VAL A 1 24 ? 46.653 -13.324 -51.207 1.00 57.10 ? 24 VAL A CG1 1 ATOM 188 C CG2 . VAL A 1 24 ? 48.592 -13.383 -49.621 1.00 55.12 ? 24 VAL A CG2 1 ATOM 189 N N . THR A 1 25 ? 45.161 -10.272 -50.660 1.00 58.96 ? 25 THR A N 1 ATOM 190 C CA . THR A 1 25 ? 43.772 -9.845 -50.813 1.00 58.48 ? 25 THR A CA 1 ATOM 191 C C . THR A 1 25 ? 42.982 -10.953 -51.482 1.00 57.06 ? 25 THR A C 1 ATOM 192 O O . THR A 1 25 ? 43.390 -11.462 -52.528 1.00 56.91 ? 25 THR A O 1 ATOM 193 C CB . THR A 1 25 ? 43.663 -8.574 -51.656 1.00 59.24 ? 25 THR A CB 1 ATOM 194 O OG1 . THR A 1 25 ? 44.474 -7.564 -51.063 1.00 62.48 ? 25 THR A OG1 1 ATOM 195 C CG2 . THR A 1 25 ? 42.228 -8.083 -51.710 1.00 61.11 ? 25 THR A CG2 1 ATOM 196 N N . VAL A 1 26 ? 41.855 -11.314 -50.881 1.00 55.92 ? 26 VAL A N 1 ATOM 197 C CA . VAL A 1 26 ? 41.017 -12.386 -51.398 1.00 54.80 ? 26 VAL A CA 1 ATOM 198 C C . VAL A 1 26 ? 39.592 -11.925 -51.645 1.00 56.25 ? 26 VAL A C 1 ATOM 199 O O . VAL A 1 26 ? 39.123 -10.991 -51.018 1.00 60.34 ? 26 VAL A O 1 ATOM 200 C CB . VAL A 1 26 ? 40.989 -13.592 -50.450 1.00 53.27 ? 26 VAL A CB 1 ATOM 201 C CG1 . VAL A 1 26 ? 42.347 -14.280 -50.435 1.00 52.04 ? 26 VAL A CG1 1 ATOM 202 C CG2 . VAL A 1 26 ? 40.576 -13.179 -49.047 1.00 54.79 ? 26 VAL A CG2 1 ATOM 203 N N . THR A 1 27 ? 38.912 -12.620 -52.549 1.00 56.99 ? 27 THR A N 1 ATOM 204 C CA . THR A 1 27 ? 37.535 -12.319 -52.919 1.00 57.71 ? 27 THR A CA 1 ATOM 205 C C . THR A 1 27 ? 36.564 -12.584 -51.788 1.00 58.17 ? 27 THR A C 1 ATOM 206 O O . THR A 1 27 ? 35.547 -11.912 -51.677 1.00 63.24 ? 27 THR A O 1 ATOM 207 C CB . THR A 1 27 ? 37.085 -13.167 -54.119 1.00 58.35 ? 27 THR A CB 1 ATOM 208 O OG1 . THR A 1 27 ? 37.171 -14.563 -53.788 1.00 56.48 ? 27 THR A OG1 1 ATOM 209 C CG2 . THR A 1 27 ? 37.951 -12.873 -55.337 1.00 57.97 ? 27 THR A CG2 1 ATOM 210 N N . HIS A 1 28 ? 36.866 -13.589 -50.974 1.00 57.35 ? 28 HIS A N 1 ATOM 211 C CA . HIS A 1 28 ? 36.038 -13.954 -49.824 1.00 56.78 ? 28 HIS A CA 1 ATOM 212 C C . HIS A 1 28 ? 36.892 -14.510 -48.706 1.00 57.36 ? 28 HIS A C 1 ATOM 213 O O . HIS A 1 28 ? 37.906 -15.177 -48.952 1.00 56.51 ? 28 HIS A O 1 ATOM 214 C CB . HIS A 1 28 ? 35.009 -15.005 -50.208 1.00 56.39 ? 28 HIS A CB 1 ATOM 215 C CG . HIS A 1 28 ? 34.151 -14.604 -51.358 1.00 58.39 ? 28 HIS A CG 1 ATOM 216 N ND1 . HIS A 1 28 ? 34.567 -14.720 -52.667 1.00 57.36 ? 28 HIS A ND1 1 ATOM 217 C CD2 . HIS A 1 28 ? 32.911 -14.063 -51.398 1.00 59.27 ? 28 HIS A CD2 1 ATOM 218 C CE1 . HIS A 1 28 ? 33.612 -14.276 -53.465 1.00 58.87 ? 28 HIS A CE1 1 ATOM 219 N NE2 . HIS A 1 28 ? 32.598 -13.875 -52.721 1.00 59.78 ? 28 HIS A NE2 1 ATOM 220 N N . ALA A 1 29 ? 36.461 -14.241 -47.480 1.00 58.23 ? 29 ALA A N 1 ATOM 221 C CA . ALA A 1 29 ? 37.154 -14.689 -46.288 1.00 58.65 ? 29 ALA A CA 1 ATOM 222 C C . ALA A 1 29 ? 36.149 -14.890 -45.178 1.00 60.17 ? 29 ALA A C 1 ATOM 223 O O . ALA A 1 29 ? 35.008 -14.452 -45.276 1.00 64.15 ? 29 ALA A O 1 ATOM 224 C CB . ALA A 1 29 ? 38.195 -13.675 -45.869 1.00 59.95 ? 29 ALA A CB 1 ATOM 225 N N . GLN A 1 30 ? 36.575 -15.572 -44.128 1.00 61.73 ? 30 GLN A N 1 ATOM 226 C CA . GLN A 1 30 ? 35.710 -15.846 -42.994 1.00 63.91 ? 30 GLN A CA 1 ATOM 227 C C . GLN A 1 30 ? 36.488 -15.656 -41.701 1.00 62.85 ? 30 GLN A C 1 ATOM 228 O O . GLN A 1 30 ? 37.395 -16.427 -41.385 1.00 60.61 ? 30 GLN A O 1 ATOM 229 C CB . GLN A 1 30 ? 35.146 -17.261 -43.081 1.00 65.87 ? 30 GLN A CB 1 ATOM 230 C CG . GLN A 1 30 ? 34.264 -17.641 -41.898 1.00 69.47 ? 30 GLN A CG 1 ATOM 231 C CD . GLN A 1 30 ? 33.412 -18.869 -42.161 1.00 71.71 ? 30 GLN A CD 1 ATOM 232 O OE1 . GLN A 1 30 ? 33.242 -19.290 -43.302 1.00 73.00 ? 30 GLN A OE1 1 ATOM 233 N NE2 . GLN A 1 30 ? 32.866 -19.445 -41.099 1.00 73.06 ? 30 GLN A NE2 1 ATOM 234 N N . ASP A 1 31 ? 36.134 -14.603 -40.976 1.00 64.96 ? 31 ASP A N 1 ATOM 235 C CA . ASP A 1 31 ? 36.671 -14.351 -39.653 1.00 66.64 ? 31 ASP A CA 1 ATOM 236 C C . ASP A 1 31 ? 36.148 -15.450 -38.725 1.00 65.14 ? 31 ASP A C 1 ATOM 237 O O . ASP A 1 31 ? 34.964 -15.784 -38.769 1.00 65.64 ? 31 ASP A O 1 ATOM 238 C CB . ASP A 1 31 ? 36.214 -12.968 -39.181 1.00 69.77 ? 31 ASP A CB 1 ATOM 239 C CG . ASP A 1 31 ? 36.866 -12.537 -37.885 1.00 72.65 ? 31 ASP A CG 1 ATOM 240 O OD1 . ASP A 1 31 ? 37.693 -13.297 -37.333 1.00 74.63 ? 31 ASP A OD1 1 ATOM 241 O OD2 . ASP A 1 31 ? 36.547 -11.425 -37.415 1.00 76.30 ? 31 ASP A OD2 1 ATOM 242 N N . ILE A 1 32 ? 37.025 -16.020 -37.904 1.00 62.83 ? 32 ILE A N 1 ATOM 243 C CA . ILE A 1 32 ? 36.616 -17.075 -36.964 1.00 63.60 ? 32 ILE A CA 1 ATOM 244 C C . ILE A 1 32 ? 36.926 -16.748 -35.493 1.00 63.99 ? 32 ILE A C 1 ATOM 245 O O . ILE A 1 32 ? 36.732 -17.591 -34.614 1.00 65.53 ? 32 ILE A O 1 ATOM 246 C CB . ILE A 1 32 ? 37.220 -18.450 -37.349 1.00 60.65 ? 32 ILE A CB 1 ATOM 247 C CG1 . ILE A 1 32 ? 38.739 -18.405 -37.374 1.00 60.39 ? 32 ILE A CG1 1 ATOM 248 C CG2 . ILE A 1 32 ? 36.720 -18.884 -38.710 1.00 60.55 ? 32 ILE A CG2 1 ATOM 249 C CD1 . ILE A 1 32 ? 39.370 -19.764 -37.572 1.00 61.21 ? 32 ILE A CD1 1 ATOM 250 N N . LEU A 1 33 ? 37.368 -15.521 -35.230 1.00 62.02 ? 33 LEU A N 1 ATOM 251 C CA . LEU A 1 33 ? 37.734 -15.090 -33.887 1.00 63.36 ? 33 LEU A CA 1 ATOM 252 C C . LEU A 1 33 ? 36.817 -13.977 -33.386 1.00 66.63 ? 33 LEU A C 1 ATOM 253 O O . LEU A 1 33 ? 36.739 -12.907 -33.994 1.00 69.35 ? 33 LEU A O 1 ATOM 254 C CB . LEU A 1 33 ? 39.175 -14.586 -33.887 1.00 61.80 ? 33 LEU A CB 1 ATOM 255 C CG . LEU A 1 33 ? 39.741 -14.146 -32.539 1.00 61.14 ? 33 LEU A CG 1 ATOM 256 C CD1 . LEU A 1 33 ? 39.941 -15.350 -31.638 1.00 60.48 ? 33 LEU A CD1 1 ATOM 257 C CD2 . LEU A 1 33 ? 41.050 -13.398 -32.732 1.00 62.20 ? 33 LEU A CD2 1 ATOM 258 N N . GLU A 1 34 ? 36.136 -14.231 -32.272 1.00 68.66 ? 34 GLU A N 1 ATOM 259 C CA . GLU A 1 34 ? 35.291 -13.227 -31.633 1.00 70.64 ? 34 GLU A CA 1 ATOM 260 C C . GLU A 1 34 ? 36.150 -12.295 -30.781 1.00 69.85 ? 34 GLU A C 1 ATOM 261 O O . GLU A 1 34 ? 36.873 -12.752 -29.894 1.00 67.93 ? 34 GLU A O 1 ATOM 262 C CB . GLU A 1 34 ? 34.230 -13.900 -30.759 1.00 72.87 ? 34 GLU A CB 1 ATOM 263 C CG . GLU A 1 34 ? 33.293 -12.931 -30.059 1.00 76.09 ? 34 GLU A CG 1 ATOM 264 C CD . GLU A 1 34 ? 32.651 -11.941 -31.016 1.00 80.19 ? 34 GLU A CD 1 ATOM 265 O OE1 . GLU A 1 34 ? 31.984 -12.376 -31.981 1.00 82.85 ? 34 GLU A OE1 1 ATOM 266 O OE2 . GLU A 1 34 ? 32.827 -10.725 -30.810 1.00 84.13 ? 34 GLU A OE2 1 ATOM 267 N N . LYS A 1 35 ? 36.071 -10.993 -31.054 1.00 70.22 ? 35 LYS A N 1 ATOM 268 C CA . LYS A 1 35 ? 36.878 -10.004 -30.340 1.00 70.53 ? 35 LYS A CA 1 ATOM 269 C C . LYS A 1 35 ? 36.061 -9.093 -29.424 1.00 70.73 ? 35 LYS A C 1 ATOM 270 O O . LYS A 1 35 ? 36.639 -8.343 -28.645 1.00 68.97 ? 35 LYS A O 1 ATOM 271 C CB . LYS A 1 35 ? 37.650 -9.132 -31.326 1.00 72.30 ? 35 LYS A CB 1 ATOM 272 C CG . LYS A 1 35 ? 38.611 -9.875 -32.230 1.00 72.17 ? 35 LYS A CG 1 ATOM 273 C CD . LYS A 1 35 ? 39.225 -8.924 -33.250 1.00 74.93 ? 35 LYS A CD 1 ATOM 274 C CE . LYS A 1 35 ? 39.394 -9.580 -34.614 1.00 77.55 ? 35 LYS A CE 1 ATOM 275 N NZ . LYS A 1 35 ? 38.093 -9.924 -35.268 1.00 77.96 ? 35 LYS A NZ 1 ATOM 276 N N . THR A 1 36 ? 34.735 -9.153 -29.508 1.00 71.52 ? 36 THR A N 1 ATOM 277 C CA . THR A 1 36 ? 33.888 -8.251 -28.736 1.00 76.91 ? 36 THR A CA 1 ATOM 278 C C . THR A 1 36 ? 33.171 -8.941 -27.576 1.00 78.30 ? 36 THR A C 1 ATOM 279 O O . THR A 1 36 ? 32.897 -10.142 -27.622 1.00 76.29 ? 36 THR A O 1 ATOM 280 C CB . THR A 1 36 ? 32.828 -7.561 -29.624 1.00 79.64 ? 36 THR A CB 1 ATOM 281 O OG1 . THR A 1 36 ? 31.844 -8.513 -30.040 1.00 82.24 ? 36 THR A OG1 1 ATOM 282 C CG2 . THR A 1 36 ? 33.472 -6.939 -30.850 1.00 79.96 ? 36 THR A CG2 1 ATOM 283 N N . HIS A 1 37 ? 32.887 -8.149 -26.540 1.00 78.79 ? 37 HIS A N 1 ATOM 284 C CA . HIS A 1 37 ? 32.037 -8.540 -25.417 1.00 77.97 ? 37 HIS A CA 1 ATOM 285 C C . HIS A 1 37 ? 31.182 -7.327 -25.019 1.00 80.44 ? 37 HIS A C 1 ATOM 286 O O . HIS A 1 37 ? 31.393 -6.229 -25.529 1.00 81.12 ? 37 HIS A O 1 ATOM 287 C CB . HIS A 1 37 ? 32.890 -9.023 -24.242 1.00 76.37 ? 37 HIS A CB 1 ATOM 288 C CG . HIS A 1 37 ? 33.902 -8.025 -23.772 1.00 77.02 ? 37 HIS A CG 1 ATOM 289 N ND1 . HIS A 1 37 ? 33.648 -7.134 -22.754 1.00 79.62 ? 37 HIS A ND1 1 ATOM 290 C CD2 . HIS A 1 37 ? 35.169 -7.775 -24.179 1.00 77.74 ? 37 HIS A CD2 1 ATOM 291 C CE1 . HIS A 1 37 ? 34.712 -6.378 -22.549 1.00 79.12 ? 37 HIS A CE1 1 ATOM 292 N NE2 . HIS A 1 37 ? 35.651 -6.748 -23.400 1.00 78.45 ? 37 HIS A NE2 1 ATOM 293 N N . ASN A 1 38 ? 30.216 -7.513 -24.122 1.00 82.15 ? 38 ASN A N 1 ATOM 294 C CA . ASN A 1 38 ? 29.316 -6.407 -23.738 1.00 83.42 ? 38 ASN A CA 1 ATOM 295 C C . ASN A 1 38 ? 29.797 -5.611 -22.517 1.00 83.98 ? 38 ASN A C 1 ATOM 296 O O . ASN A 1 38 ? 29.249 -4.553 -22.206 1.00 85.27 ? 38 ASN A O 1 ATOM 297 C CB . ASN A 1 38 ? 27.874 -6.902 -23.530 1.00 82.87 ? 38 ASN A CB 1 ATOM 298 C CG . ASN A 1 38 ? 27.724 -7.808 -22.323 1.00 82.75 ? 38 ASN A CG 1 ATOM 299 O OD1 . ASN A 1 38 ? 28.687 -8.082 -21.605 1.00 81.74 ? 38 ASN A OD1 1 ATOM 300 N ND2 . ASN A 1 38 ? 26.506 -8.288 -22.098 1.00 83.12 ? 38 ASN A ND2 1 ATOM 301 N N . GLY A 1 39 ? 30.796 -6.139 -21.816 1.00 82.22 ? 39 GLY A N 1 ATOM 302 C CA . GLY A 1 39 ? 31.436 -5.423 -20.710 1.00 82.05 ? 39 GLY A CA 1 ATOM 303 C C . GLY A 1 39 ? 30.676 -5.518 -19.399 1.00 84.07 ? 39 GLY A C 1 ATOM 304 O O . GLY A 1 39 ? 30.952 -4.756 -18.467 1.00 82.26 ? 39 GLY A O 1 ATOM 305 N N . LYS A 1 40 ? 29.738 -6.470 -19.329 1.00 85.73 ? 40 LYS A N 1 ATOM 306 C CA . LYS A 1 40 ? 28.824 -6.618 -18.201 1.00 85.09 ? 40 LYS A CA 1 ATOM 307 C C . LYS A 1 40 ? 28.821 -8.024 -17.615 1.00 84.66 ? 40 LYS A C 1 ATOM 308 O O . LYS A 1 40 ? 29.129 -8.997 -18.297 1.00 84.12 ? 40 LYS A O 1 ATOM 309 C CB . LYS A 1 40 ? 27.408 -6.290 -18.650 1.00 87.52 ? 40 LYS A CB 1 ATOM 310 C CG . LYS A 1 40 ? 27.227 -4.848 -19.076 1.00 90.70 ? 40 LYS A CG 1 ATOM 311 C CD . LYS A 1 40 ? 25.891 -4.606 -19.765 1.00 92.04 ? 40 LYS A CD 1 ATOM 312 C CE . LYS A 1 40 ? 25.953 -3.320 -20.570 1.00 94.03 ? 40 LYS A CE 1 ATOM 313 N NZ . LYS A 1 40 ? 24.613 -2.727 -20.802 1.00 98.90 ? 40 LYS A NZ 1 ATOM 314 N N . LEU A 1 41 ? 28.458 -8.117 -16.341 1.00 87.90 ? 41 LEU A N 1 ATOM 315 C CA . LEU A 1 41 ? 28.185 -9.401 -15.705 1.00 89.57 ? 41 LEU A CA 1 ATOM 316 C C . LEU A 1 41 ? 26.696 -9.692 -15.858 1.00 89.15 ? 41 LEU A C 1 ATOM 317 O O . LEU A 1 41 ? 25.865 -8.842 -15.551 1.00 89.84 ? 41 LEU A O 1 ATOM 318 C CB . LEU A 1 41 ? 28.585 -9.365 -14.232 1.00 90.63 ? 41 LEU A CB 1 ATOM 319 C CG . LEU A 1 41 ? 30.056 -9.022 -13.989 1.00 90.69 ? 41 LEU A CG 1 ATOM 320 C CD1 . LEU A 1 41 ? 30.310 -8.853 -12.501 1.00 92.16 ? 41 LEU A CD1 1 ATOM 321 C CD2 . LEU A 1 41 ? 30.975 -10.082 -14.582 1.00 89.72 ? 41 LEU A CD2 1 ATOM 322 N N . CYS A 1 42 ? 26.369 -10.889 -16.339 1.00 89.33 ? 42 CYS A N 1 ATOM 323 C CA . CYS A 1 42 ? 25.009 -11.203 -16.774 1.00 93.53 ? 42 CYS A CA 1 ATOM 324 C C . CYS A 1 42 ? 24.506 -12.496 -16.169 1.00 90.58 ? 42 CYS A C 1 ATOM 325 O O . CYS A 1 42 ? 25.284 -13.294 -15.651 1.00 86.94 ? 42 CYS A O 1 ATOM 326 C CB . CYS A 1 42 ? 24.964 -11.349 -18.299 1.00 96.91 ? 42 CYS A CB 1 ATOM 327 S SG . CYS A 1 42 ? 25.547 -9.918 -19.235 1.00 99.89 ? 42 CYS A SG 1 ATOM 328 N N . ASP A 1 43 ? 23.196 -12.702 -16.262 1.00 92.47 ? 43 ASP A N 1 ATOM 329 C CA . ASP A 1 43 ? 22.598 -13.990 -15.924 1.00 92.71 ? 43 ASP A CA 1 ATOM 330 C C . ASP A 1 43 ? 23.121 -15.030 -16.908 1.00 90.17 ? 43 ASP A C 1 ATOM 331 O O . ASP A 1 43 ? 23.326 -14.732 -18.083 1.00 87.30 ? 43 ASP A O 1 ATOM 332 C CB . ASP A 1 43 ? 21.062 -13.940 -16.003 1.00 95.54 ? 43 ASP A CB 1 ATOM 333 C CG . ASP A 1 43 ? 20.449 -12.883 -15.093 1.00 96.87 ? 43 ASP A CG 1 ATOM 334 O OD1 . ASP A 1 43 ? 21.101 -12.478 -14.111 1.00 96.97 ? 43 ASP A OD1 1 ATOM 335 O OD2 . ASP A 1 43 ? 19.307 -12.453 -15.365 1.00 98.12 ? 43 ASP A OD2 1 ATOM 336 N N . LEU A 1 44 ? 23.342 -16.243 -16.418 1.00 91.50 ? 44 LEU A N 1 ATOM 337 C CA . LEU A 1 44 ? 23.781 -17.351 -17.254 1.00 93.12 ? 44 LEU A CA 1 ATOM 338 C C . LEU A 1 44 ? 22.590 -18.277 -17.550 1.00 98.47 ? 44 LEU A C 1 ATOM 339 O O . LEU A 1 44 ? 22.198 -19.096 -16.710 1.00 97.93 ? 44 LEU A O 1 ATOM 340 C CB . LEU A 1 44 ? 24.911 -18.110 -16.557 1.00 90.90 ? 44 LEU A CB 1 ATOM 341 C CG . LEU A 1 44 ? 25.698 -19.111 -17.404 1.00 91.55 ? 44 LEU A CG 1 ATOM 342 C CD1 . LEU A 1 44 ? 26.530 -18.394 -18.458 1.00 92.18 ? 44 LEU A CD1 1 ATOM 343 C CD2 . LEU A 1 44 ? 26.591 -19.974 -16.524 1.00 90.55 ? 44 LEU A CD2 1 ATOM 344 N N . ASP A 1 45 ? 22.027 -18.131 -18.750 1.00 101.92 ? 45 ASP A N 1 ATOM 345 C CA . ASP A 1 45 ? 20.821 -18.855 -19.167 1.00 106.35 ? 45 ASP A CA 1 ATOM 346 C C . ASP A 1 45 ? 19.700 -18.666 -18.148 1.00 105.82 ? 45 ASP A C 1 ATOM 347 O O . ASP A 1 45 ? 19.122 -19.635 -17.653 1.00 103.83 ? 45 ASP A O 1 ATOM 348 C CB . ASP A 1 45 ? 21.112 -20.343 -19.404 1.00 109.91 ? 45 ASP A CB 1 ATOM 349 C CG . ASP A 1 45 ? 22.091 -20.572 -20.551 1.00 115.67 ? 45 ASP A CG 1 ATOM 350 O OD1 . ASP A 1 45 ? 23.291 -20.241 -20.399 1.00 117.27 ? 45 ASP A OD1 1 ATOM 351 O OD2 . ASP A 1 45 ? 21.664 -21.091 -21.607 1.00 119.80 ? 45 ASP A OD2 1 ATOM 352 N N . GLY A 1 46 ? 19.429 -17.402 -17.826 1.00 104.76 ? 46 GLY A N 1 ATOM 353 C CA . GLY A 1 46 ? 18.337 -17.030 -16.926 1.00 104.98 ? 46 GLY A CA 1 ATOM 354 C C . GLY A 1 46 ? 18.701 -16.975 -15.454 1.00 102.91 ? 46 GLY A C 1 ATOM 355 O O . GLY A 1 46 ? 18.056 -16.253 -14.695 1.00 103.98 ? 46 GLY A O 1 ATOM 356 N N . VAL A 1 47 ? 19.735 -17.722 -15.055 1.00 98.30 ? 47 VAL A N 1 ATOM 357 C CA . VAL A 1 47 ? 20.106 -17.884 -13.645 1.00 95.42 ? 47 VAL A CA 1 ATOM 358 C C . VAL A 1 47 ? 21.165 -16.864 -13.212 1.00 94.07 ? 47 VAL A C 1 ATOM 359 O O . VAL A 1 47 ? 22.325 -16.946 -13.613 1.00 93.62 ? 47 VAL A O 1 ATOM 360 C CB . VAL A 1 47 ? 20.638 -19.305 -13.382 1.00 93.40 ? 47 VAL A CB 1 ATOM 361 C CG1 . VAL A 1 47 ? 21.003 -19.484 -11.914 1.00 94.01 ? 47 VAL A CG1 1 ATOM 362 C CG2 . VAL A 1 47 ? 19.610 -20.338 -13.813 1.00 94.56 ? 47 VAL A CG2 1 ATOM 363 N N . LYS A 1 48 ? 20.754 -15.923 -12.370 1.00 94.95 ? 48 LYS A N 1 ATOM 364 C CA . LYS A 1 48 ? 21.605 -14.829 -11.894 1.00 93.59 ? 48 LYS A CA 1 ATOM 365 C C . LYS A 1 48 ? 22.791 -15.322 -11.052 1.00 90.63 ? 48 LYS A C 1 ATOM 366 O O . LYS A 1 48 ? 22.648 -16.272 -10.284 1.00 91.39 ? 48 LYS A O 1 ATOM 367 C CB . LYS A 1 48 ? 20.736 -13.881 -11.063 1.00 97.43 ? 48 LYS A CB 1 ATOM 368 C CG . LYS A 1 48 ? 21.399 -12.615 -10.550 1.00 100.11 ? 48 LYS A CG 1 ATOM 369 C CD . LYS A 1 48 ? 20.585 -12.029 -9.406 1.00 106.22 ? 48 LYS A CD 1 ATOM 370 C CE . LYS A 1 48 ? 21.265 -10.828 -8.774 1.00 109.10 ? 48 LYS A CE 1 ATOM 371 N NZ . LYS A 1 48 ? 21.310 -9.669 -9.705 1.00 112.26 ? 48 LYS A NZ 1 ATOM 372 N N . PRO A 1 49 ? 23.968 -14.674 -11.190 1.00 87.26 ? 49 PRO A N 1 ATOM 373 C CA . PRO A 1 49 ? 25.100 -15.017 -10.326 1.00 83.91 ? 49 PRO A CA 1 ATOM 374 C C . PRO A 1 49 ? 24.968 -14.448 -8.919 1.00 83.83 ? 49 PRO A C 1 ATOM 375 O O . PRO A 1 49 ? 24.168 -13.538 -8.687 1.00 84.13 ? 49 PRO A O 1 ATOM 376 C CB . PRO A 1 49 ? 26.285 -14.347 -11.023 1.00 81.15 ? 49 PRO A CB 1 ATOM 377 C CG . PRO A 1 49 ? 25.690 -13.162 -11.696 1.00 82.72 ? 49 PRO A CG 1 ATOM 378 C CD . PRO A 1 49 ? 24.332 -13.622 -12.162 1.00 85.46 ? 49 PRO A CD 1 ATOM 379 N N . LEU A 1 50 ? 25.766 -14.985 -7.998 1.00 81.45 ? 50 LEU A N 1 ATOM 380 C CA . LEU A 1 50 ? 25.922 -14.412 -6.669 1.00 81.48 ? 50 LEU A CA 1 ATOM 381 C C . LEU A 1 50 ? 27.020 -13.361 -6.734 1.00 80.84 ? 50 LEU A C 1 ATOM 382 O O . LEU A 1 50 ? 28.194 -13.693 -6.899 1.00 81.84 ? 50 LEU A O 1 ATOM 383 C CB . LEU A 1 50 ? 26.289 -15.496 -5.653 1.00 81.63 ? 50 LEU A CB 1 ATOM 384 C CG . LEU A 1 50 ? 26.614 -15.045 -4.226 1.00 82.35 ? 50 LEU A CG 1 ATOM 385 C CD1 . LEU A 1 50 ? 25.429 -14.323 -3.607 1.00 84.51 ? 50 LEU A CD1 1 ATOM 386 C CD2 . LEU A 1 50 ? 27.020 -16.234 -3.367 1.00 83.19 ? 50 LEU A CD2 1 ATOM 387 N N . ILE A 1 51 ? 26.638 -12.096 -6.615 1.00 81.92 ? 51 ILE A N 1 ATOM 388 C CA . ILE A 1 51 ? 27.595 -10.993 -6.676 1.00 82.09 ? 51 ILE A CA 1 ATOM 389 C C . ILE A 1 51 ? 27.870 -10.495 -5.264 1.00 81.95 ? 51 ILE A C 1 ATOM 390 O O . ILE A 1 51 ? 27.086 -9.731 -4.696 1.00 82.44 ? 51 ILE A O 1 ATOM 391 C CB . ILE A 1 51 ? 27.080 -9.860 -7.588 1.00 83.37 ? 51 ILE A CB 1 ATOM 392 C CG1 . ILE A 1 51 ? 26.776 -10.444 -8.970 1.00 84.34 ? 51 ILE A CG1 1 ATOM 393 C CG2 . ILE A 1 51 ? 28.091 -8.717 -7.675 1.00 83.04 ? 51 ILE A CG2 1 ATOM 394 C CD1 . ILE A 1 51 ? 26.599 -9.418 -10.063 1.00 87.72 ? 51 ILE A CD1 1 ATOM 395 N N . LEU A 1 52 ? 29.000 -10.927 -4.709 1.00 80.64 ? 52 LEU A N 1 ATOM 396 C CA . LEU A 1 52 ? 29.330 -10.647 -3.312 1.00 80.60 ? 52 LEU A CA 1 ATOM 397 C C . LEU A 1 52 ? 29.646 -9.176 -3.047 1.00 81.39 ? 52 LEU A C 1 ATOM 398 O O . LEU A 1 52 ? 29.731 -8.763 -1.893 1.00 81.18 ? 52 LEU A O 1 ATOM 399 C CB . LEU A 1 52 ? 30.489 -11.533 -2.848 1.00 78.19 ? 52 LEU A CB 1 ATOM 400 C CG . LEU A 1 52 ? 30.211 -13.039 -2.879 1.00 78.95 ? 52 LEU A CG 1 ATOM 401 C CD1 . LEU A 1 52 ? 31.454 -13.836 -2.515 1.00 77.92 ? 52 LEU A CD1 1 ATOM 402 C CD2 . LEU A 1 52 ? 29.056 -13.402 -1.955 1.00 81.52 ? 52 LEU A CD2 1 ATOM 403 N N . ARG A 1 53 ? 29.816 -8.397 -4.113 1.00 83.48 ? 53 ARG A N 1 ATOM 404 C CA . ARG A 1 53 ? 30.025 -6.956 -4.019 1.00 89.10 ? 53 ARG A CA 1 ATOM 405 C C . ARG A 1 53 ? 31.271 -6.638 -3.169 1.00 90.03 ? 53 ARG A C 1 ATOM 406 O O . ARG A 1 53 ? 32.390 -6.935 -3.598 1.00 94.03 ? 53 ARG A O 1 ATOM 407 C CB . ARG A 1 53 ? 28.746 -6.259 -3.526 1.00 94.86 ? 53 ARG A CB 1 ATOM 408 C CG . ARG A 1 53 ? 28.755 -4.748 -3.723 1.00 101.09 ? 53 ARG A CG 1 ATOM 409 C CD . ARG A 1 53 ? 27.583 -4.049 -3.045 1.00 107.37 ? 53 ARG A CD 1 ATOM 410 N NE . ARG A 1 53 ? 26.520 -3.672 -3.980 1.00 111.82 ? 53 ARG A NE 1 ATOM 411 C CZ . ARG A 1 53 ? 25.475 -4.431 -4.314 1.00 114.59 ? 53 ARG A CZ 1 ATOM 412 N NH1 . ARG A 1 53 ? 25.311 -5.650 -3.811 1.00 116.41 ? 53 ARG A NH1 1 ATOM 413 N NH2 . ARG A 1 53 ? 24.576 -3.962 -5.171 1.00 117.94 ? 53 ARG A NH2 1 ATOM 414 N N . ASP A 1 54 ? 31.096 -6.068 -1.977 1.00 90.61 ? 54 ASP A N 1 ATOM 415 C CA . ASP A 1 54 ? 32.220 -5.767 -1.089 1.00 90.10 ? 54 ASP A CA 1 ATOM 416 C C . ASP A 1 54 ? 32.517 -6.885 -0.091 1.00 87.78 ? 54 ASP A C 1 ATOM 417 O O . ASP A 1 54 ? 33.448 -6.765 0.700 1.00 90.56 ? 54 ASP A O 1 ATOM 418 C CB . ASP A 1 54 ? 31.958 -4.467 -0.319 1.00 93.69 ? 54 ASP A CB 1 ATOM 419 C CG . ASP A 1 54 ? 31.979 -3.240 -1.212 1.00 96.59 ? 54 ASP A CG 1 ATOM 420 O OD1 . ASP A 1 54 ? 32.816 -3.194 -2.146 1.00 95.49 ? 54 ASP A OD1 1 ATOM 421 O OD2 . ASP A 1 54 ? 31.165 -2.317 -0.966 1.00 98.82 ? 54 ASP A OD2 1 ATOM 422 N N . CYS A 1 55 ? 31.737 -7.961 -0.110 1.00 87.30 ? 55 CYS A N 1 ATOM 423 C CA . CYS A 1 55 ? 31.974 -9.079 0.804 1.00 88.97 ? 55 CYS A CA 1 ATOM 424 C C . CYS A 1 55 ? 32.857 -10.149 0.158 1.00 84.74 ? 55 CYS A C 1 ATOM 425 O O . CYS A 1 55 ? 32.855 -10.322 -1.058 1.00 84.86 ? 55 CYS A O 1 ATOM 426 C CB . CYS A 1 55 ? 30.649 -9.689 1.288 1.00 91.43 ? 55 CYS A CB 1 ATOM 427 S SG . CYS A 1 55 ? 29.632 -8.534 2.249 1.00 102.04 ? 55 CYS A SG 1 ATOM 428 N N . SER A 1 56 ? 33.624 -10.846 0.989 1.00 82.18 ? 56 SER A N 1 ATOM 429 C CA . SER A 1 56 ? 34.372 -12.018 0.566 1.00 81.10 ? 56 SER A CA 1 ATOM 430 C C . SER A 1 56 ? 33.561 -13.274 0.866 1.00 80.57 ? 56 SER A C 1 ATOM 431 O O . SER A 1 56 ? 32.521 -13.212 1.516 1.00 81.10 ? 56 SER A O 1 ATOM 432 C CB . SER A 1 56 ? 35.703 -12.088 1.311 1.00 81.27 ? 56 SER A CB 1 ATOM 433 O OG . SER A 1 56 ? 35.498 -12.501 2.651 1.00 82.22 ? 56 SER A OG 1 ATOM 434 N N . VAL A 1 57 ? 34.052 -14.419 0.407 1.00 81.38 ? 57 VAL A N 1 ATOM 435 C CA . VAL A 1 57 ? 33.390 -15.698 0.674 1.00 83.17 ? 57 VAL A CA 1 ATOM 436 C C . VAL A 1 57 ? 33.327 -15.963 2.186 1.00 82.97 ? 57 VAL A C 1 ATOM 437 O O . VAL A 1 57 ? 32.321 -16.467 2.689 1.00 82.90 ? 57 VAL A O 1 ATOM 438 C CB . VAL A 1 57 ? 34.090 -16.862 -0.074 1.00 81.54 ? 57 VAL A CB 1 ATOM 439 C CG1 . VAL A 1 57 ? 33.586 -18.217 0.400 1.00 82.08 ? 57 VAL A CG1 1 ATOM 440 C CG2 . VAL A 1 57 ? 33.879 -16.718 -1.575 1.00 81.26 ? 57 VAL A CG2 1 ATOM 441 N N . ALA A 1 58 ? 34.395 -15.602 2.895 1.00 81.45 ? 58 ALA A N 1 ATOM 442 C CA . ALA A 1 58 ? 34.460 -15.746 4.350 1.00 82.40 ? 58 ALA A CA 1 ATOM 443 C C . ALA A 1 58 ? 33.451 -14.842 5.071 1.00 83.92 ? 58 ALA A C 1 ATOM 444 O O . ALA A 1 58 ? 32.714 -15.300 5.949 1.00 84.50 ? 58 ALA A O 1 ATOM 445 C CB . ALA A 1 58 ? 35.866 -15.453 4.838 1.00 80.83 ? 58 ALA A CB 1 ATOM 446 N N . GLY A 1 59 ? 33.428 -13.562 4.701 1.00 83.36 ? 59 GLY A N 1 ATOM 447 C CA . GLY A 1 59 ? 32.463 -12.616 5.254 1.00 84.18 ? 59 GLY A CA 1 ATOM 448 C C . GLY A 1 59 ? 31.033 -13.086 5.036 1.00 87.86 ? 59 GLY A C 1 ATOM 449 O O . GLY A 1 59 ? 30.191 -12.981 5.933 1.00 93.35 ? 59 GLY A O 1 ATOM 450 N N . TRP A 1 60 ? 30.762 -13.616 3.845 1.00 85.26 ? 60 TRP A N 1 ATOM 451 C CA . TRP A 1 60 ? 29.439 -14.126 3.514 1.00 84.26 ? 60 TRP A CA 1 ATOM 452 C C . TRP A 1 60 ? 29.095 -15.345 4.369 1.00 85.82 ? 60 TRP A C 1 ATOM 453 O O . TRP A 1 60 ? 28.037 -15.385 5.001 1.00 88.16 ? 60 TRP A O 1 ATOM 454 C CB . TRP A 1 60 ? 29.348 -14.458 2.016 1.00 84.23 ? 60 TRP A CB 1 ATOM 455 C CG . TRP A 1 60 ? 28.216 -15.376 1.642 1.00 84.15 ? 60 TRP A CG 1 ATOM 456 C CD1 . TRP A 1 60 ? 26.935 -15.324 2.100 1.00 86.70 ? 60 TRP A CD1 1 ATOM 457 C CD2 . TRP A 1 60 ? 28.269 -16.473 0.722 1.00 82.53 ? 60 TRP A CD2 1 ATOM 458 N NE1 . TRP A 1 60 ? 26.188 -16.324 1.529 1.00 88.80 ? 60 TRP A NE1 1 ATOM 459 C CE2 . TRP A 1 60 ? 26.984 -17.045 0.680 1.00 86.46 ? 60 TRP A CE2 1 ATOM 460 C CE3 . TRP A 1 60 ? 29.278 -17.026 -0.070 1.00 82.31 ? 60 TRP A CE3 1 ATOM 461 C CZ2 . TRP A 1 60 ? 26.680 -18.147 -0.124 1.00 87.43 ? 60 TRP A CZ2 1 ATOM 462 C CZ3 . TRP A 1 60 ? 28.976 -18.126 -0.869 1.00 82.22 ? 60 TRP A CZ3 1 ATOM 463 C CH2 . TRP A 1 60 ? 27.690 -18.670 -0.891 1.00 84.57 ? 60 TRP A CH2 1 ATOM 464 N N . LEU A 1 61 ? 29.993 -16.325 4.401 1.00 84.98 ? 61 LEU A N 1 ATOM 465 C CA . LEU A 1 61 ? 29.696 -17.606 5.051 1.00 86.05 ? 61 LEU A CA 1 ATOM 466 C C . LEU A 1 61 ? 29.633 -17.511 6.575 1.00 86.71 ? 61 LEU A C 1 ATOM 467 O O . LEU A 1 61 ? 28.695 -18.025 7.189 1.00 87.01 ? 61 LEU A O 1 ATOM 468 C CB . LEU A 1 61 ? 30.689 -18.687 4.615 1.00 84.23 ? 61 LEU A CB 1 ATOM 469 C CG . LEU A 1 61 ? 30.483 -19.157 3.173 1.00 84.48 ? 61 LEU A CG 1 ATOM 470 C CD1 . LEU A 1 61 ? 31.620 -20.062 2.722 1.00 86.14 ? 61 LEU A CD1 1 ATOM 471 C CD2 . LEU A 1 61 ? 29.150 -19.865 3.005 1.00 85.86 ? 61 LEU A CD2 1 ATOM 472 N N . LEU A 1 62 ? 30.618 -16.852 7.178 1.00 85.94 ? 62 LEU A N 1 ATOM 473 C CA . LEU A 1 62 ? 30.601 -16.608 8.625 1.00 86.92 ? 62 LEU A CA 1 ATOM 474 C C . LEU A 1 62 ? 29.472 -15.672 9.072 1.00 88.66 ? 62 LEU A C 1 ATOM 475 O O . LEU A 1 62 ? 29.047 -15.727 10.224 1.00 91.46 ? 62 LEU A O 1 ATOM 476 C CB . LEU A 1 62 ? 31.944 -16.049 9.092 1.00 84.81 ? 62 LEU A CB 1 ATOM 477 C CG . LEU A 1 62 ? 33.093 -17.054 9.053 1.00 84.04 ? 62 LEU A CG 1 ATOM 478 C CD1 . LEU A 1 62 ? 34.421 -16.347 9.252 1.00 83.45 ? 62 LEU A CD1 1 ATOM 479 C CD2 . LEU A 1 62 ? 32.907 -18.145 10.099 1.00 85.25 ? 62 LEU A CD2 1 ATOM 480 N N . GLY A 1 63 ? 28.991 -14.818 8.171 1.00 87.91 ? 63 GLY A N 1 ATOM 481 C CA . GLY A 1 63 ? 27.923 -13.876 8.493 1.00 88.87 ? 63 GLY A CA 1 ATOM 482 C C . GLY A 1 63 ? 28.429 -12.563 9.067 1.00 88.23 ? 63 GLY A C 1 ATOM 483 O O . GLY A 1 63 ? 27.923 -12.094 10.080 1.00 88.79 ? 63 GLY A O 1 ATOM 484 N N . ASN A 1 64 ? 29.431 -11.973 8.418 1.00 87.00 ? 64 ASN A N 1 ATOM 485 C CA . ASN A 1 64 ? 29.907 -10.634 8.758 1.00 87.14 ? 64 ASN A CA 1 ATOM 486 C C . ASN A 1 64 ? 28.719 -9.669 8.744 1.00 90.16 ? 64 ASN A C 1 ATOM 487 O O . ASN A 1 64 ? 28.015 -9.601 7.741 1.00 92.59 ? 64 ASN A O 1 ATOM 488 C CB . ASN A 1 64 ? 30.976 -10.203 7.741 1.00 85.44 ? 64 ASN A CB 1 ATOM 489 C CG . ASN A 1 64 ? 31.540 -8.814 8.007 1.00 84.27 ? 64 ASN A CG 1 ATOM 490 O OD1 . ASN A 1 64 ? 30.818 -7.890 8.367 1.00 84.20 ? 64 ASN A OD1 1 ATOM 491 N ND2 . ASN A 1 64 ? 32.841 -8.657 7.792 1.00 83.34 ? 64 ASN A ND2 1 ATOM 492 N N . PRO A 1 65 ? 28.486 -8.923 9.850 1.00 93.49 ? 65 PRO A N 1 ATOM 493 C CA . PRO A 1 65 ? 27.296 -8.049 9.952 1.00 97.12 ? 65 PRO A CA 1 ATOM 494 C C . PRO A 1 65 ? 27.099 -7.065 8.791 1.00 99.50 ? 65 PRO A C 1 ATOM 495 O O . PRO A 1 65 ? 25.970 -6.644 8.532 1.00 102.12 ? 65 PRO A O 1 ATOM 496 C CB . PRO A 1 65 ? 27.530 -7.274 11.254 1.00 97.26 ? 65 PRO A CB 1 ATOM 497 C CG . PRO A 1 65 ? 28.475 -8.106 12.044 1.00 95.18 ? 65 PRO A CG 1 ATOM 498 C CD . PRO A 1 65 ? 29.333 -8.836 11.056 1.00 92.98 ? 65 PRO A CD 1 ATOM 499 N N . MET A 1 66 ? 28.189 -6.708 8.112 1.00 100.94 ? 66 MET A N 1 ATOM 500 C CA . MET A 1 66 ? 28.145 -5.862 6.913 1.00 103.29 ? 66 MET A CA 1 ATOM 501 C C . MET A 1 66 ? 27.639 -6.595 5.661 1.00 101.43 ? 66 MET A C 1 ATOM 502 O O . MET A 1 66 ? 27.476 -5.979 4.608 1.00 99.91 ? 66 MET A O 1 ATOM 503 C CB . MET A 1 66 ? 29.545 -5.319 6.614 1.00 103.91 ? 66 MET A CB 1 ATOM 504 C CG . MET A 1 66 ? 30.125 -4.418 7.692 1.00 106.60 ? 66 MET A CG 1 ATOM 505 S SD . MET A 1 66 ? 29.419 -2.762 7.662 1.00 112.24 ? 66 MET A SD 1 ATOM 506 C CE . MET A 1 66 ? 30.767 -1.839 8.401 1.00 113.00 ? 66 MET A CE 1 ATOM 507 N N . CYS A 1 67 ? 27.403 -7.900 5.772 1.00 99.95 ? 67 CYS A N 1 ATOM 508 C CA . CYS A 1 67 ? 27.064 -8.734 4.625 1.00 100.13 ? 67 CYS A CA 1 ATOM 509 C C . CYS A 1 67 ? 25.662 -9.329 4.745 1.00 100.93 ? 67 CYS A C 1 ATOM 510 O O . CYS A 1 67 ? 25.422 -10.462 4.323 1.00 100.64 ? 67 CYS A O 1 ATOM 511 C CB . CYS A 1 67 ? 28.109 -9.843 4.490 1.00 98.43 ? 67 CYS A CB 1 ATOM 512 S SG . CYS A 1 67 ? 29.763 -9.189 4.183 1.00 99.18 ? 67 CYS A SG 1 ATOM 513 N N . ASP A 1 68 ? 24.738 -8.552 5.307 1.00 102.57 ? 68 ASP A N 1 ATOM 514 C CA . ASP A 1 68 ? 23.364 -9.014 5.518 1.00 103.88 ? 68 ASP A CA 1 ATOM 515 C C . ASP A 1 68 ? 22.587 -9.180 4.218 1.00 104.41 ? 68 ASP A C 1 ATOM 516 O O . ASP A 1 68 ? 21.618 -9.931 4.177 1.00 105.95 ? 68 ASP A O 1 ATOM 517 C CB . ASP A 1 68 ? 22.611 -8.067 6.454 1.00 105.90 ? 68 ASP A CB 1 ATOM 518 C CG . ASP A 1 68 ? 23.080 -8.172 7.888 1.00 106.94 ? 68 ASP A CG 1 ATOM 519 O OD1 . ASP A 1 68 ? 24.008 -8.965 8.152 1.00 106.54 ? 68 ASP A OD1 1 ATOM 520 O OD2 . ASP A 1 68 ? 22.523 -7.462 8.755 1.00 109.22 ? 68 ASP A OD2 1 ATOM 521 N N . GLU A 1 69 ? 23.010 -8.491 3.160 1.00 104.09 ? 69 GLU A N 1 ATOM 522 C CA . GLU A 1 69 ? 22.431 -8.695 1.831 1.00 104.24 ? 69 GLU A CA 1 ATOM 523 C C . GLU A 1 69 ? 22.418 -10.181 1.470 1.00 101.67 ? 69 GLU A C 1 ATOM 524 O O . GLU A 1 69 ? 21.484 -10.664 0.827 1.00 102.10 ? 69 GLU A O 1 ATOM 525 C CB . GLU A 1 69 ? 23.214 -7.916 0.768 1.00 104.01 ? 69 GLU A CB 1 ATOM 526 C CG . GLU A 1 69 ? 22.571 -7.929 -0.616 1.00 105.74 ? 69 GLU A CG 1 ATOM 527 C CD . GLU A 1 69 ? 23.460 -7.345 -1.701 1.00 104.28 ? 69 GLU A CD 1 ATOM 528 O OE1 . GLU A 1 69 ? 24.529 -6.782 -1.378 1.00 102.92 ? 69 GLU A OE1 1 ATOM 529 O OE2 . GLU A 1 69 ? 23.084 -7.451 -2.887 1.00 103.96 ? 69 GLU A OE2 1 ATOM 530 N N . PHE A 1 70 ? 23.453 -10.896 1.909 1.00 98.77 ? 70 PHE A N 1 ATOM 531 C CA . PHE A 1 70 ? 23.639 -12.301 1.570 1.00 97.86 ? 70 PHE A CA 1 ATOM 532 C C . PHE A 1 70 ? 23.300 -13.250 2.720 1.00 100.17 ? 70 PHE A C 1 ATOM 533 O O . PHE A 1 70 ? 23.862 -14.342 2.816 1.00 101.11 ? 70 PHE A O 1 ATOM 534 C CB . PHE A 1 70 ? 25.083 -12.517 1.113 1.00 93.85 ? 70 PHE A CB 1 ATOM 535 C CG . PHE A 1 70 ? 25.570 -11.462 0.159 1.00 91.86 ? 70 PHE A CG 1 ATOM 536 C CD1 . PHE A 1 70 ? 25.078 -11.406 -1.139 1.00 90.55 ? 70 PHE A CD1 1 ATOM 537 C CD2 . PHE A 1 70 ? 26.489 -10.504 0.568 1.00 89.55 ? 70 PHE A CD2 1 ATOM 538 C CE1 . PHE A 1 70 ? 25.512 -10.430 -2.016 1.00 90.11 ? 70 PHE A CE1 1 ATOM 539 C CE2 . PHE A 1 70 ? 26.925 -9.527 -0.305 1.00 88.65 ? 70 PHE A CE2 1 ATOM 540 C CZ . PHE A 1 70 ? 26.437 -9.489 -1.598 1.00 88.46 ? 70 PHE A CZ 1 ATOM 541 N N . ILE A 1 71 ? 22.370 -12.842 3.580 1.00 102.65 ? 71 ILE A N 1 ATOM 542 C CA . ILE A 1 71 ? 21.958 -13.671 4.711 1.00 105.00 ? 71 ILE A CA 1 ATOM 543 C C . ILE A 1 71 ? 21.180 -14.902 4.238 1.00 106.23 ? 71 ILE A C 1 ATOM 544 O O . ILE A 1 71 ? 21.254 -15.953 4.863 1.00 106.15 ? 71 ILE A O 1 ATOM 545 C CB . ILE A 1 71 ? 21.140 -12.855 5.753 1.00 108.95 ? 71 ILE A CB 1 ATOM 546 C CG1 . ILE A 1 71 ? 21.134 -13.558 7.121 1.00 109.53 ? 71 ILE A CG1 1 ATOM 547 C CG2 . ILE A 1 71 ? 19.721 -12.568 5.258 1.00 109.23 ? 71 ILE A CG2 1 ATOM 548 C CD1 . ILE A 1 71 ? 21.251 -12.604 8.293 1.00 108.72 ? 71 ILE A CD1 1 ATOM 549 N N . ASN A 1 72 ? 20.442 -14.767 3.136 1.00 107.60 ? 72 ASN A N 1 ATOM 550 C CA . ASN A 1 72 ? 19.770 -15.903 2.499 1.00 109.45 ? 72 ASN A CA 1 ATOM 551 C C . ASN A 1 72 ? 19.721 -15.720 0.990 1.00 107.30 ? 72 ASN A C 1 ATOM 552 O O . ASN A 1 72 ? 18.785 -15.127 0.449 1.00 110.88 ? 72 ASN A O 1 ATOM 553 C CB . ASN A 1 72 ? 18.357 -16.091 3.064 1.00 114.62 ? 72 ASN A CB 1 ATOM 554 C CG . ASN A 1 72 ? 18.354 -16.849 4.379 1.00 117.36 ? 72 ASN A CG 1 ATOM 555 O OD1 . ASN A 1 72 ? 19.036 -17.867 4.523 1.00 118.38 ? 72 ASN A OD1 1 ATOM 556 N ND2 . ASN A 1 72 ? 17.589 -16.358 5.348 1.00 120.17 ? 72 ASN A ND2 1 ATOM 557 N N . VAL A 1 73 ? 20.744 -16.237 0.317 1.00 103.73 ? 73 VAL A N 1 ATOM 558 C CA . VAL A 1 73 ? 20.907 -16.028 -1.119 1.00 99.97 ? 73 VAL A CA 1 ATOM 559 C C . VAL A 1 73 ? 20.285 -17.171 -1.903 1.00 98.54 ? 73 VAL A C 1 ATOM 560 O O . VAL A 1 73 ? 20.443 -18.333 -1.531 1.00 98.28 ? 73 VAL A O 1 ATOM 561 C CB . VAL A 1 73 ? 22.395 -15.884 -1.520 1.00 96.24 ? 73 VAL A CB 1 ATOM 562 C CG1 . VAL A 1 73 ? 23.055 -14.795 -0.694 1.00 95.24 ? 73 VAL A CG1 1 ATOM 563 C CG2 . VAL A 1 73 ? 23.152 -17.200 -1.380 1.00 94.77 ? 73 VAL A CG2 1 ATOM 564 N N . PRO A 1 74 ? 19.589 -16.848 -3.005 1.00 97.95 ? 74 PRO A N 1 ATOM 565 C CA . PRO A 1 74 ? 19.020 -17.902 -3.836 1.00 99.24 ? 74 PRO A CA 1 ATOM 566 C C . PRO A 1 74 ? 20.090 -18.672 -4.615 1.00 96.22 ? 74 PRO A C 1 ATOM 567 O O . PRO A 1 74 ? 21.283 -18.379 -4.497 1.00 92.39 ? 74 PRO A O 1 ATOM 568 C CB . PRO A 1 74 ? 18.093 -17.136 -4.788 1.00 100.80 ? 74 PRO A CB 1 ATOM 569 C CG . PRO A 1 74 ? 18.683 -15.773 -4.879 1.00 99.05 ? 74 PRO A CG 1 ATOM 570 C CD . PRO A 1 74 ? 19.314 -15.503 -3.545 1.00 98.14 ? 74 PRO A CD 1 ATOM 571 N N . GLU A 1 75 ? 19.644 -19.660 -5.388 1.00 97.44 ? 75 GLU A N 1 ATOM 572 C CA . GLU A 1 75 ? 20.512 -20.437 -6.268 1.00 96.45 ? 75 GLU A CA 1 ATOM 573 C C . GLU A 1 75 ? 21.264 -19.511 -7.225 1.00 93.78 ? 75 GLU A C 1 ATOM 574 O O . GLU A 1 75 ? 20.689 -18.559 -7.748 1.00 93.46 ? 75 GLU A O 1 ATOM 575 C CB . GLU A 1 75 ? 19.669 -21.438 -7.059 1.00 99.46 ? 75 GLU A CB 1 ATOM 576 C CG . GLU A 1 75 ? 20.450 -22.411 -7.932 1.00 99.55 ? 75 GLU A CG 1 ATOM 577 C CD . GLU A 1 75 ? 19.543 -23.357 -8.707 1.00 102.70 ? 75 GLU A CD 1 ATOM 578 O OE1 . GLU A 1 75 ? 18.321 -23.395 -8.429 1.00 108.46 ? 75 GLU A OE1 1 ATOM 579 O OE2 . GLU A 1 75 ? 20.051 -24.065 -9.601 1.00 101.32 ? 75 GLU A OE2 1 ATOM 580 N N . TRP A 1 76 ? 22.549 -19.781 -7.437 1.00 91.79 ? 76 TRP A N 1 ATOM 581 C CA . TRP A 1 76 ? 23.363 -18.961 -8.341 1.00 90.39 ? 76 TRP A CA 1 ATOM 582 C C . TRP A 1 76 ? 23.937 -19.798 -9.480 1.00 90.46 ? 76 TRP A C 1 ATOM 583 O O . TRP A 1 76 ? 23.963 -21.028 -9.416 1.00 95.42 ? 76 TRP A O 1 ATOM 584 C CB . TRP A 1 76 ? 24.483 -18.242 -7.580 1.00 86.27 ? 76 TRP A CB 1 ATOM 585 C CG . TRP A 1 76 ? 25.456 -19.169 -6.932 1.00 85.32 ? 76 TRP A CG 1 ATOM 586 C CD1 . TRP A 1 76 ? 26.564 -19.726 -7.501 1.00 84.80 ? 76 TRP A CD1 1 ATOM 587 C CD2 . TRP A 1 76 ? 25.409 -19.657 -5.589 1.00 84.91 ? 76 TRP A CD2 1 ATOM 588 N NE1 . TRP A 1 76 ? 27.210 -20.531 -6.594 1.00 83.92 ? 76 TRP A NE1 1 ATOM 589 C CE2 . TRP A 1 76 ? 26.519 -20.506 -5.413 1.00 83.65 ? 76 TRP A CE2 1 ATOM 590 C CE3 . TRP A 1 76 ? 24.535 -19.459 -4.516 1.00 87.05 ? 76 TRP A CE3 1 ATOM 591 C CZ2 . TRP A 1 76 ? 26.777 -21.154 -4.212 1.00 84.97 ? 76 TRP A CZ2 1 ATOM 592 C CZ3 . TRP A 1 76 ? 24.792 -20.105 -3.321 1.00 86.66 ? 76 TRP A CZ3 1 ATOM 593 C CH2 . TRP A 1 76 ? 25.901 -20.943 -3.179 1.00 86.00 ? 76 TRP A CH2 1 ATOM 594 N N . SER A 1 77 ? 24.382 -19.114 -10.528 1.00 89.82 ? 77 SER A N 1 ATOM 595 C CA . SER A 1 77 ? 25.009 -19.752 -11.684 1.00 87.18 ? 77 SER A CA 1 ATOM 596 C C . SER A 1 77 ? 26.515 -19.747 -11.498 1.00 84.97 ? 77 SER A C 1 ATOM 597 O O . SER A 1 77 ? 27.178 -20.764 -11.681 1.00 85.33 ? 77 SER A O 1 ATOM 598 C CB . SER A 1 77 ? 24.638 -18.998 -12.959 1.00 86.80 ? 77 SER A CB 1 ATOM 599 O OG . SER A 1 77 ? 24.681 -17.596 -12.749 1.00 86.62 ? 77 SER A OG 1 ATOM 600 N N . TYR A 1 78 ? 27.044 -18.582 -11.142 1.00 83.11 ? 78 TYR A N 1 ATOM 601 C CA . TYR A 1 78 ? 28.441 -18.440 -10.749 1.00 79.91 ? 78 TYR A CA 1 ATOM 602 C C . TYR A 1 78 ? 28.544 -17.402 -9.641 1.00 79.34 ? 78 TYR A C 1 ATOM 603 O O . TYR A 1 78 ? 27.563 -16.745 -9.302 1.00 82.34 ? 78 TYR A O 1 ATOM 604 C CB . TYR A 1 78 ? 29.315 -18.048 -11.951 1.00 77.64 ? 78 TYR A CB 1 ATOM 605 C CG . TYR A 1 78 ? 28.878 -16.791 -12.682 1.00 76.29 ? 78 TYR A CG 1 ATOM 606 C CD1 . TYR A 1 78 ? 27.805 -16.811 -13.574 1.00 76.26 ? 78 TYR A CD1 1 ATOM 607 C CD2 . TYR A 1 78 ? 29.544 -15.586 -12.489 1.00 74.26 ? 78 TYR A CD2 1 ATOM 608 C CE1 . TYR A 1 78 ? 27.407 -15.662 -14.245 1.00 75.84 ? 78 TYR A CE1 1 ATOM 609 C CE2 . TYR A 1 78 ? 29.151 -14.435 -13.152 1.00 73.65 ? 78 TYR A CE2 1 ATOM 610 C CZ . TYR A 1 78 ? 28.085 -14.476 -14.027 1.00 74.84 ? 78 TYR A CZ 1 ATOM 611 O OH . TYR A 1 78 ? 27.707 -13.323 -14.679 1.00 74.63 ? 78 TYR A OH 1 ATOM 612 N N . ILE A 1 79 ? 29.734 -17.268 -9.072 1.00 77.45 ? 79 ILE A N 1 ATOM 613 C CA . ILE A 1 79 ? 29.975 -16.332 -7.986 1.00 78.27 ? 79 ILE A CA 1 ATOM 614 C C . ILE A 1 79 ? 30.984 -15.276 -8.439 1.00 78.05 ? 79 ILE A C 1 ATOM 615 O O . ILE A 1 79 ? 31.949 -15.591 -9.138 1.00 74.76 ? 79 ILE A O 1 ATOM 616 C CB . ILE A 1 79 ? 30.505 -17.079 -6.751 1.00 79.01 ? 79 ILE A CB 1 ATOM 617 C CG1 . ILE A 1 79 ? 29.411 -17.989 -6.189 1.00 81.45 ? 79 ILE A CG1 1 ATOM 618 C CG2 . ILE A 1 79 ? 30.992 -16.104 -5.685 1.00 80.38 ? 79 ILE A CG2 1 ATOM 619 C CD1 . ILE A 1 79 ? 29.899 -18.945 -5.124 1.00 82.36 ? 79 ILE A CD1 1 ATOM 620 N N . VAL A 1 80 ? 30.755 -14.025 -8.047 1.00 78.62 ? 80 VAL A N 1 ATOM 621 C CA . VAL A 1 80 ? 31.664 -12.939 -8.395 1.00 78.44 ? 80 VAL A CA 1 ATOM 622 C C . VAL A 1 80 ? 32.161 -12.259 -7.131 1.00 78.88 ? 80 VAL A C 1 ATOM 623 O O . VAL A 1 80 ? 31.371 -11.782 -6.325 1.00 82.52 ? 80 VAL A O 1 ATOM 624 C CB . VAL A 1 80 ? 30.996 -11.898 -9.314 1.00 79.14 ? 80 VAL A CB 1 ATOM 625 C CG1 . VAL A 1 80 ? 31.962 -10.757 -9.621 1.00 78.37 ? 80 VAL A CG1 1 ATOM 626 C CG2 . VAL A 1 80 ? 30.524 -12.560 -10.600 1.00 78.43 ? 80 VAL A CG2 1 ATOM 627 N N . GLU A 1 81 ? 33.480 -12.213 -6.985 1.00 79.03 ? 81 GLU A N 1 ATOM 628 C CA . GLU A 1 81 ? 34.134 -11.654 -5.817 1.00 80.96 ? 81 GLU A CA 1 ATOM 629 C C . GLU A 1 81 ? 35.178 -10.671 -6.310 1.00 79.37 ? 81 GLU A C 1 ATOM 630 O O . GLU A 1 81 ? 35.856 -10.939 -7.287 1.00 79.70 ? 81 GLU A O 1 ATOM 631 C CB . GLU A 1 81 ? 34.805 -12.779 -5.028 1.00 84.21 ? 81 GLU A CB 1 ATOM 632 C CG . GLU A 1 81 ? 35.391 -12.368 -3.687 1.00 88.59 ? 81 GLU A CG 1 ATOM 633 C CD . GLU A 1 81 ? 36.222 -13.470 -3.045 1.00 93.41 ? 81 GLU A CD 1 ATOM 634 O OE1 . GLU A 1 81 ? 37.127 -14.015 -3.721 1.00 94.28 ? 81 GLU A OE1 1 ATOM 635 O OE2 . GLU A 1 81 ? 35.967 -13.794 -1.860 1.00 95.74 ? 81 GLU A OE2 1 ATOM 636 N N . LYS A 1 82 ? 35.309 -9.531 -5.647 1.00 82.23 ? 82 LYS A N 1 ATOM 637 C CA . LYS A 1 82 ? 36.370 -8.584 -5.986 1.00 83.17 ? 82 LYS A CA 1 ATOM 638 C C . LYS A 1 82 ? 37.745 -9.160 -5.620 1.00 83.63 ? 82 LYS A C 1 ATOM 639 O O . LYS A 1 82 ? 37.844 -10.203 -4.964 1.00 82.66 ? 82 LYS A O 1 ATOM 640 C CB . LYS A 1 82 ? 36.140 -7.241 -5.289 1.00 85.36 ? 82 LYS A CB 1 ATOM 641 C CG . LYS A 1 82 ? 34.944 -6.469 -5.828 1.00 87.48 ? 82 LYS A CG 1 ATOM 642 C CD . LYS A 1 82 ? 34.770 -5.140 -5.109 1.00 89.35 ? 82 LYS A CD 1 ATOM 643 C CE . LYS A 1 82 ? 33.980 -4.138 -5.936 1.00 92.48 ? 82 LYS A CE 1 ATOM 644 N NZ . LYS A 1 82 ? 32.593 -4.591 -6.218 1.00 96.24 ? 82 LYS A NZ 1 ATOM 645 N N . ALA A 1 83 ? 38.803 -8.486 -6.064 1.00 85.09 ? 83 ALA A N 1 ATOM 646 C CA . ALA A 1 83 ? 40.171 -8.926 -5.778 1.00 83.29 ? 83 ALA A CA 1 ATOM 647 C C . ALA A 1 83 ? 40.512 -8.749 -4.297 1.00 85.52 ? 83 ALA A C 1 ATOM 648 O O . ALA A 1 83 ? 41.102 -9.637 -3.681 1.00 86.29 ? 83 ALA A O 1 ATOM 649 C CB . ALA A 1 83 ? 41.162 -8.170 -6.647 1.00 81.49 ? 83 ALA A CB 1 ATOM 650 N N . ASN A 1 84 ? 40.129 -7.605 -3.732 1.00 86.83 ? 84 ASN A N 1 ATOM 651 C CA . ASN A 1 84 ? 40.378 -7.308 -2.325 1.00 88.80 ? 84 ASN A CA 1 ATOM 652 C C . ASN A 1 84 ? 39.124 -6.764 -1.643 1.00 87.86 ? 84 ASN A C 1 ATOM 653 O O . ASN A 1 84 ? 39.018 -5.561 -1.393 1.00 87.48 ? 84 ASN A O 1 ATOM 654 C CB . ASN A 1 84 ? 41.542 -6.316 -2.193 1.00 93.37 ? 84 ASN A CB 1 ATOM 655 C CG . ASN A 1 84 ? 42.853 -6.881 -2.726 1.00 96.34 ? 84 ASN A CG 1 ATOM 656 O OD1 . ASN A 1 84 ? 43.450 -7.773 -2.119 1.00 96.97 ? 84 ASN A OD1 1 ATOM 657 N ND2 . ASN A 1 84 ? 43.304 -6.369 -3.868 1.00 97.62 ? 84 ASN A ND2 1 ATOM 658 N N . PRO A 1 85 ? 38.163 -7.652 -1.332 1.00 87.19 ? 85 PRO A N 1 ATOM 659 C CA . PRO A 1 85 ? 36.930 -7.167 -0.711 1.00 88.63 ? 85 PRO A CA 1 ATOM 660 C C . PRO A 1 85 ? 37.222 -6.547 0.651 1.00 89.39 ? 85 PRO A C 1 ATOM 661 O O . PRO A 1 85 ? 38.069 -7.064 1.382 1.00 88.64 ? 85 PRO A O 1 ATOM 662 C CB . PRO A 1 85 ? 36.068 -8.437 -0.571 1.00 88.01 ? 85 PRO A CB 1 ATOM 663 C CG . PRO A 1 85 ? 36.742 -9.489 -1.396 1.00 85.85 ? 85 PRO A CG 1 ATOM 664 C CD . PRO A 1 85 ? 38.190 -9.122 -1.432 1.00 84.75 ? 85 PRO A CD 1 ATOM 665 N N . VAL A 1 86 ? 36.549 -5.445 0.982 1.00 91.12 ? 86 VAL A N 1 ATOM 666 C CA . VAL A 1 86 ? 36.789 -4.769 2.265 1.00 92.61 ? 86 VAL A CA 1 ATOM 667 C C . VAL A 1 86 ? 36.173 -5.530 3.441 1.00 91.35 ? 86 VAL A C 1 ATOM 668 O O . VAL A 1 86 ? 36.781 -5.612 4.511 1.00 90.89 ? 86 VAL A O 1 ATOM 669 C CB . VAL A 1 86 ? 36.290 -3.303 2.277 1.00 95.58 ? 86 VAL A CB 1 ATOM 670 C CG1 . VAL A 1 86 ? 36.884 -2.526 1.109 1.00 95.44 ? 86 VAL A CG1 1 ATOM 671 C CG2 . VAL A 1 86 ? 34.766 -3.229 2.267 1.00 98.16 ? 86 VAL A CG2 1 ATOM 672 N N . ASN A 1 87 ? 34.982 -6.091 3.232 1.00 88.73 ? 87 ASN A N 1 ATOM 673 C CA . ASN A 1 87 ? 34.270 -6.814 4.278 1.00 89.11 ? 87 ASN A CA 1 ATOM 674 C C . ASN A 1 87 ? 34.619 -8.294 4.255 1.00 88.33 ? 87 ASN A C 1 ATOM 675 O O . ASN A 1 87 ? 33.925 -9.101 3.647 1.00 89.29 ? 87 ASN A O 1 ATOM 676 C CB . ASN A 1 87 ? 32.760 -6.622 4.129 1.00 90.88 ? 87 ASN A CB 1 ATOM 677 C CG . ASN A 1 87 ? 32.337 -5.176 4.308 1.00 93.28 ? 87 ASN A CG 1 ATOM 678 O OD1 . ASN A 1 87 ? 32.798 -4.482 5.218 1.00 93.07 ? 87 ASN A OD1 1 ATOM 679 N ND2 . ASN A 1 87 ? 31.448 -4.715 3.439 1.00 95.50 ? 87 ASN A ND2 1 ATOM 680 N N . ASP A 1 88 ? 35.711 -8.637 4.925 1.00 90.28 ? 88 ASP A N 1 ATOM 681 C CA . ASP A 1 88 ? 36.182 -10.011 5.009 1.00 90.60 ? 88 ASP A CA 1 ATOM 682 C C . ASP A 1 88 ? 35.972 -10.456 6.464 1.00 92.02 ? 88 ASP A C 1 ATOM 683 O O . ASP A 1 88 ? 34.827 -10.607 6.897 1.00 92.11 ? 88 ASP A O 1 ATOM 684 C CB . ASP A 1 88 ? 37.646 -10.079 4.532 1.00 89.80 ? 88 ASP A CB 1 ATOM 685 C CG . ASP A 1 88 ? 38.188 -11.505 4.429 1.00 90.95 ? 88 ASP A CG 1 ATOM 686 O OD1 . ASP A 1 88 ? 37.428 -12.434 4.095 1.00 89.99 ? 88 ASP A OD1 1 ATOM 687 O OD2 . ASP A 1 88 ? 39.401 -11.691 4.669 1.00 93.47 ? 88 ASP A OD2 1 ATOM 688 N N . LEU A 1 89 ? 37.055 -10.635 7.218 1.00 91.60 ? 89 LEU A N 1 ATOM 689 C CA . LEU A 1 89 ? 36.976 -10.963 8.634 1.00 91.55 ? 89 LEU A CA 1 ATOM 690 C C . LEU A 1 89 ? 37.082 -9.669 9.436 1.00 91.07 ? 89 LEU A C 1 ATOM 691 O O . LEU A 1 89 ? 38.183 -9.155 9.655 1.00 89.26 ? 89 LEU A O 1 ATOM 692 C CB . LEU A 1 89 ? 38.108 -11.920 9.022 1.00 91.02 ? 89 LEU A CB 1 ATOM 693 C CG . LEU A 1 89 ? 38.237 -13.206 8.200 1.00 89.12 ? 89 LEU A CG 1 ATOM 694 C CD1 . LEU A 1 89 ? 39.492 -13.963 8.615 1.00 88.53 ? 89 LEU A CD1 1 ATOM 695 C CD2 . LEU A 1 89 ? 37.000 -14.080 8.340 1.00 88.03 ? 89 LEU A CD2 1 ATOM 696 N N . CYS A 1 90 ? 35.933 -9.150 9.867 1.00 93.25 ? 90 CYS A N 1 ATOM 697 C CA . CYS A 1 90 ? 35.885 -7.906 10.631 1.00 93.51 ? 90 CYS A CA 1 ATOM 698 C C . CYS A 1 90 ? 36.783 -7.994 11.867 1.00 91.01 ? 90 CYS A C 1 ATOM 699 O O . CYS A 1 90 ? 37.643 -7.138 12.072 1.00 90.42 ? 90 CYS A O 1 ATOM 700 C CB . CYS A 1 90 ? 34.441 -7.546 11.007 1.00 97.87 ? 90 CYS A CB 1 ATOM 701 S SG . CYS A 1 90 ? 33.428 -8.879 11.707 1.00 103.76 ? 90 CYS A SG 1 ATOM 702 N N . TYR A 1 91 ? 36.591 -9.038 12.668 1.00 88.85 ? 91 TYR A N 1 ATOM 703 C CA . TYR A 1 91 ? 37.509 -9.360 13.757 1.00 89.04 ? 91 TYR A CA 1 ATOM 704 C C . TYR A 1 91 ? 38.685 -10.119 13.151 1.00 87.21 ? 91 TYR A C 1 ATOM 705 O O . TYR A 1 91 ? 38.482 -11.137 12.492 1.00 88.23 ? 91 TYR A O 1 ATOM 706 C CB . TYR A 1 91 ? 36.807 -10.217 14.816 1.00 92.09 ? 91 TYR A CB 1 ATOM 707 C CG . TYR A 1 91 ? 37.489 -10.230 16.173 1.00 94.47 ? 91 TYR A CG 1 ATOM 708 C CD1 . TYR A 1 91 ? 38.664 -10.946 16.379 1.00 93.63 ? 91 TYR A CD1 1 ATOM 709 C CD2 . TYR A 1 91 ? 36.954 -9.530 17.253 1.00 95.28 ? 91 TYR A CD2 1 ATOM 710 C CE1 . TYR A 1 91 ? 39.283 -10.966 17.616 1.00 94.09 ? 91 TYR A CE1 1 ATOM 711 C CE2 . TYR A 1 91 ? 37.569 -9.546 18.495 1.00 95.51 ? 91 TYR A CE2 1 ATOM 712 C CZ . TYR A 1 91 ? 38.734 -10.265 18.669 1.00 94.33 ? 91 TYR A CZ 1 ATOM 713 O OH . TYR A 1 91 ? 39.352 -10.285 19.898 1.00 95.35 ? 91 TYR A OH 1 ATOM 714 N N . PRO A 1 92 ? 39.922 -9.641 13.371 1.00 87.64 ? 92 PRO A N 1 ATOM 715 C CA . PRO A 1 92 ? 41.063 -10.223 12.655 1.00 86.26 ? 92 PRO A CA 1 ATOM 716 C C . PRO A 1 92 ? 41.317 -11.693 12.979 1.00 87.54 ? 92 PRO A C 1 ATOM 717 O O . PRO A 1 92 ? 40.927 -12.172 14.044 1.00 89.79 ? 92 PRO A O 1 ATOM 718 C CB . PRO A 1 92 ? 42.243 -9.368 13.130 1.00 85.94 ? 92 PRO A CB 1 ATOM 719 C CG . PRO A 1 92 ? 41.836 -8.897 14.483 1.00 87.56 ? 92 PRO A CG 1 ATOM 720 C CD . PRO A 1 92 ? 40.359 -8.644 14.368 1.00 88.20 ? 92 PRO A CD 1 ATOM 721 N N . GLY A 1 93 ? 41.972 -12.397 12.060 1.00 90.54 ? 93 GLY A N 1 ATOM 722 C CA . GLY A 1 93 ? 42.358 -13.784 12.294 1.00 91.91 ? 93 GLY A CA 1 ATOM 723 C C . GLY A 1 93 ? 42.691 -14.562 11.037 1.00 91.72 ? 93 GLY A C 1 ATOM 724 O O . GLY A 1 93 ? 43.312 -14.032 10.116 1.00 90.02 ? 93 GLY A O 1 ATOM 725 N N . ASP A 1 94 ? 42.286 -15.831 11.020 1.00 93.57 ? 94 ASP A N 1 ATOM 726 C CA . ASP A 1 94 ? 42.500 -16.722 9.885 1.00 94.07 ? 94 ASP A CA 1 ATOM 727 C C . ASP A 1 94 ? 41.257 -17.555 9.632 1.00 91.62 ? 94 ASP A C 1 ATOM 728 O O . ASP A 1 94 ? 40.417 -17.722 10.518 1.00 92.79 ? 94 ASP A O 1 ATOM 729 C CB . ASP A 1 94 ? 43.676 -17.664 10.151 1.00 97.74 ? 94 ASP A CB 1 ATOM 730 C CG . ASP A 1 94 ? 45.017 -16.974 10.020 1.00 102.60 ? 94 ASP A CG 1 ATOM 731 O OD1 . ASP A 1 94 ? 45.361 -16.546 8.896 1.00 106.69 ? 94 ASP A OD1 1 ATOM 732 O OD2 . ASP A 1 94 ? 45.734 -16.868 11.038 1.00 106.65 ? 94 ASP A OD2 1 ATOM 733 N N . PHE A 1 95 ? 41.154 -18.067 8.410 1.00 87.76 ? 95 PHE A N 1 ATOM 734 C CA . PHE A 1 95 ? 40.113 -19.011 8.031 1.00 83.24 ? 95 PHE A CA 1 ATOM 735 C C . PHE A 1 95 ? 40.839 -20.254 7.539 1.00 81.63 ? 95 PHE A C 1 ATOM 736 O O . PHE A 1 95 ? 41.476 -20.231 6.495 1.00 81.78 ? 95 PHE A O 1 ATOM 737 C CB . PHE A 1 95 ? 39.240 -18.406 6.936 1.00 81.19 ? 95 PHE A CB 1 ATOM 738 C CG . PHE A 1 95 ? 37.932 -19.108 6.739 1.00 81.94 ? 95 PHE A CG 1 ATOM 739 C CD1 . PHE A 1 95 ? 37.885 -20.402 6.248 1.00 82.75 ? 95 PHE A CD1 1 ATOM 740 C CD2 . PHE A 1 95 ? 36.740 -18.467 7.028 1.00 83.18 ? 95 PHE A CD2 1 ATOM 741 C CE1 . PHE A 1 95 ? 36.674 -21.044 6.055 1.00 84.62 ? 95 PHE A CE1 1 ATOM 742 C CE2 . PHE A 1 95 ? 35.525 -19.106 6.838 1.00 83.30 ? 95 PHE A CE2 1 ATOM 743 C CZ . PHE A 1 95 ? 35.492 -20.397 6.355 1.00 83.42 ? 95 PHE A CZ 1 ATOM 744 N N . ASN A 1 96 ? 40.758 -21.332 8.303 1.00 82.97 ? 96 ASN A N 1 ATOM 745 C CA . ASN A 1 96 ? 41.535 -22.534 8.016 1.00 83.96 ? 96 ASN A CA 1 ATOM 746 C C . ASN A 1 96 ? 41.029 -23.279 6.778 1.00 81.69 ? 96 ASN A C 1 ATOM 747 O O . ASN A 1 96 ? 39.819 -23.429 6.590 1.00 79.89 ? 96 ASN A O 1 ATOM 748 C CB . ASN A 1 96 ? 41.522 -23.463 9.235 1.00 88.16 ? 96 ASN A CB 1 ATOM 749 C CG . ASN A 1 96 ? 42.653 -24.469 9.212 1.00 91.22 ? 96 ASN A CG 1 ATOM 750 O OD1 . ASN A 1 96 ? 43.831 -24.104 9.292 1.00 90.50 ? 96 ASN A OD1 1 ATOM 751 N ND2 . ASN A 1 96 ? 42.302 -25.746 9.108 1.00 93.51 ? 96 ASN A ND2 1 ATOM 752 N N . ASP A 1 97 ? 41.968 -23.748 5.953 1.00 81.83 ? 97 ASP A N 1 ATOM 753 C CA . ASP A 1 97 ? 41.674 -24.437 4.685 1.00 80.82 ? 97 ASP A CA 1 ATOM 754 C C . ASP A 1 97 ? 40.699 -23.648 3.810 1.00 77.19 ? 97 ASP A C 1 ATOM 755 O O . ASP A 1 97 ? 39.779 -24.215 3.210 1.00 75.13 ? 97 ASP A O 1 ATOM 756 C CB . ASP A 1 97 ? 41.147 -25.858 4.943 1.00 86.04 ? 97 ASP A CB 1 ATOM 757 C CG . ASP A 1 97 ? 42.259 -26.852 5.253 1.00 92.13 ? 97 ASP A CG 1 ATOM 758 O OD1 . ASP A 1 97 ? 43.379 -26.695 4.711 1.00 93.41 ? 97 ASP A OD1 1 ATOM 759 O OD2 . ASP A 1 97 ? 42.002 -27.804 6.030 1.00 97.25 ? 97 ASP A OD2 1 ATOM 760 N N . TYR A 1 98 ? 40.921 -22.339 3.742 1.00 74.75 ? 98 TYR A N 1 ATOM 761 C CA . TYR A 1 98 ? 39.988 -21.412 3.102 1.00 74.66 ? 98 TYR A CA 1 ATOM 762 C C . TYR A 1 98 ? 39.897 -21.667 1.612 1.00 75.08 ? 98 TYR A C 1 ATOM 763 O O . TYR A 1 98 ? 38.807 -21.679 1.048 1.00 75.94 ? 98 TYR A O 1 ATOM 764 C CB . TYR A 1 98 ? 40.433 -19.968 3.365 1.00 73.12 ? 98 TYR A CB 1 ATOM 765 C CG . TYR A 1 98 ? 39.504 -18.884 2.852 1.00 72.79 ? 98 TYR A CG 1 ATOM 766 C CD1 . TYR A 1 98 ? 38.132 -18.958 3.057 1.00 73.67 ? 98 TYR A CD1 1 ATOM 767 C CD2 . TYR A 1 98 ? 40.011 -17.760 2.188 1.00 71.84 ? 98 TYR A CD2 1 ATOM 768 C CE1 . TYR A 1 98 ? 37.285 -17.965 2.597 1.00 74.24 ? 98 TYR A CE1 1 ATOM 769 C CE2 . TYR A 1 98 ? 39.172 -16.761 1.723 1.00 71.47 ? 98 TYR A CE2 1 ATOM 770 C CZ . TYR A 1 98 ? 37.809 -16.869 1.932 1.00 74.86 ? 98 TYR A CZ 1 ATOM 771 O OH . TYR A 1 98 ? 36.956 -15.884 1.488 1.00 79.19 ? 98 TYR A OH 1 ATOM 772 N N . GLU A 1 99 ? 41.050 -21.892 0.987 1.00 76.54 ? 99 GLU A N 1 ATOM 773 C CA . GLU A 1 99 ? 41.116 -22.106 -0.458 1.00 76.46 ? 99 GLU A CA 1 ATOM 774 C C . GLU A 1 99 ? 40.495 -23.442 -0.863 1.00 75.37 ? 99 GLU A C 1 ATOM 775 O O . GLU A 1 99 ? 39.854 -23.529 -1.901 1.00 75.31 ? 99 GLU A O 1 ATOM 776 C CB . GLU A 1 99 ? 42.557 -22.012 -0.961 1.00 77.59 ? 99 GLU A CB 1 ATOM 777 C CG . GLU A 1 99 ? 43.155 -20.603 -0.925 1.00 78.47 ? 99 GLU A CG 1 ATOM 778 C CD . GLU A 1 99 ? 43.592 -20.152 0.463 1.00 81.78 ? 99 GLU A CD 1 ATOM 779 O OE1 . GLU A 1 99 ? 43.959 -21.006 1.299 1.00 83.64 ? 99 GLU A OE1 1 ATOM 780 O OE2 . GLU A 1 99 ? 43.570 -18.929 0.719 1.00 84.49 ? 99 GLU A OE2 1 ATOM 781 N N . GLU A 1 100 ? 40.673 -24.474 -0.041 1.00 75.32 ? 100 GLU A N 1 ATOM 782 C CA . GLU A 1 100 ? 40.024 -25.763 -0.285 1.00 75.81 ? 100 GLU A CA 1 ATOM 783 C C . GLU A 1 100 ? 38.505 -25.654 -0.186 1.00 77.91 ? 100 GLU A C 1 ATOM 784 O O . GLU A 1 100 ? 37.788 -26.375 -0.883 1.00 83.39 ? 100 GLU A O 1 ATOM 785 C CB . GLU A 1 100 ? 40.538 -26.839 0.677 1.00 76.41 ? 100 GLU A CB 1 ATOM 786 C CG . GLU A 1 100 ? 41.894 -27.423 0.301 1.00 77.22 ? 100 GLU A CG 1 ATOM 787 C CD . GLU A 1 100 ? 41.854 -28.315 -0.935 1.00 78.09 ? 100 GLU A CD 1 ATOM 788 O OE1 . GLU A 1 100 ? 40.992 -29.225 -1.014 1.00 79.97 ? 100 GLU A OE1 1 ATOM 789 O OE2 . GLU A 1 100 ? 42.700 -28.112 -1.832 1.00 75.86 ? 100 GLU A OE2 1 ATOM 790 N N . LEU A 1 101 ? 38.013 -24.761 0.671 1.00 77.70 ? 101 LEU A N 1 ATOM 791 C CA . LEU A 1 101 ? 36.571 -24.522 0.779 1.00 77.60 ? 101 LEU A CA 1 ATOM 792 C C . LEU A 1 101 ? 36.051 -23.785 -0.451 1.00 75.97 ? 101 LEU A C 1 ATOM 793 O O . LEU A 1 101 ? 35.045 -24.184 -1.036 1.00 74.41 ? 101 LEU A O 1 ATOM 794 C CB . LEU A 1 101 ? 36.235 -23.729 2.043 1.00 78.97 ? 101 LEU A CB 1 ATOM 795 C CG . LEU A 1 101 ? 34.746 -23.461 2.307 1.00 81.06 ? 101 LEU A CG 1 ATOM 796 C CD1 . LEU A 1 101 ? 33.923 -24.745 2.324 1.00 82.48 ? 101 LEU A CD1 1 ATOM 797 C CD2 . LEU A 1 101 ? 34.583 -22.703 3.615 1.00 82.90 ? 101 LEU A CD2 1 ATOM 798 N N . LYS A 1 102 ? 36.741 -22.719 -0.847 1.00 74.84 ? 102 LYS A N 1 ATOM 799 C CA . LYS A 1 102 ? 36.386 -21.991 -2.068 1.00 74.79 ? 102 LYS A CA 1 ATOM 800 C C . LYS A 1 102 ? 36.344 -22.909 -3.289 1.00 74.11 ? 102 LYS A C 1 ATOM 801 O O . LYS A 1 102 ? 35.487 -22.749 -4.161 1.00 73.86 ? 102 LYS A O 1 ATOM 802 C CB . LYS A 1 102 ? 37.354 -20.839 -2.317 1.00 75.81 ? 102 LYS A CB 1 ATOM 803 C CG . LYS A 1 102 ? 37.233 -19.724 -1.293 1.00 79.92 ? 102 LYS A CG 1 ATOM 804 C CD . LYS A 1 102 ? 38.309 -18.661 -1.463 1.00 81.50 ? 102 LYS A CD 1 ATOM 805 C CE . LYS A 1 102 ? 37.845 -17.538 -2.373 1.00 83.37 ? 102 LYS A CE 1 ATOM 806 N NZ . LYS A 1 102 ? 38.798 -16.396 -2.343 1.00 85.44 ? 102 LYS A NZ 1 ATOM 807 N N . HIS A 1 103 ? 37.259 -23.875 -3.346 1.00 73.43 ? 103 HIS A N 1 ATOM 808 C CA . HIS A 1 103 ? 37.260 -24.852 -4.430 1.00 74.41 ? 103 HIS A CA 1 ATOM 809 C C . HIS A 1 103 ? 36.021 -25.730 -4.363 1.00 76.55 ? 103 HIS A C 1 ATOM 810 O O . HIS A 1 103 ? 35.476 -26.124 -5.387 1.00 77.09 ? 103 HIS A O 1 ATOM 811 C CB . HIS A 1 103 ? 38.509 -25.732 -4.379 1.00 75.17 ? 103 HIS A CB 1 ATOM 812 C CG . HIS A 1 103 ? 38.533 -26.794 -5.433 1.00 75.13 ? 103 HIS A CG 1 ATOM 813 N ND1 . HIS A 1 103 ? 39.037 -26.576 -6.697 1.00 73.46 ? 103 HIS A ND1 1 ATOM 814 C CD2 . HIS A 1 103 ? 38.093 -28.075 -5.418 1.00 75.90 ? 103 HIS A CD2 1 ATOM 815 C CE1 . HIS A 1 103 ? 38.915 -27.679 -7.412 1.00 73.45 ? 103 HIS A CE1 1 ATOM 816 N NE2 . HIS A 1 103 ? 38.346 -28.603 -6.660 1.00 75.44 ? 103 HIS A NE2 1 ATOM 817 N N . LEU A 1 104 ? 35.595 -26.035 -3.145 1.00 79.97 ? 104 LEU A N 1 ATOM 818 C CA . LEU A 1 104 ? 34.392 -26.827 -2.915 1.00 84.37 ? 104 LEU A CA 1 ATOM 819 C C . LEU A 1 104 ? 33.136 -26.102 -3.428 1.00 85.90 ? 104 LEU A C 1 ATOM 820 O O . LEU A 1 104 ? 32.190 -26.745 -3.894 1.00 86.78 ? 104 LEU A O 1 ATOM 821 C CB . LEU A 1 104 ? 34.265 -27.136 -1.417 1.00 86.77 ? 104 LEU A CB 1 ATOM 822 C CG . LEU A 1 104 ? 33.607 -28.448 -0.999 1.00 90.20 ? 104 LEU A CG 1 ATOM 823 C CD1 . LEU A 1 104 ? 34.350 -29.653 -1.561 1.00 90.49 ? 104 LEU A CD1 1 ATOM 824 C CD2 . LEU A 1 104 ? 33.548 -28.505 0.521 1.00 91.51 ? 104 LEU A CD2 1 ATOM 825 N N . LEU A 1 105 ? 33.147 -24.768 -3.346 1.00 86.52 ? 105 LEU A N 1 ATOM 826 C CA . LEU A 1 105 ? 32.044 -23.920 -3.829 1.00 85.90 ? 105 LEU A CA 1 ATOM 827 C C . LEU A 1 105 ? 31.879 -23.891 -5.337 1.00 86.48 ? 105 LEU A C 1 ATOM 828 O O . LEU A 1 105 ? 30.802 -23.557 -5.834 1.00 93.27 ? 105 LEU A O 1 ATOM 829 C CB . LEU A 1 105 ? 32.240 -22.473 -3.387 1.00 83.46 ? 105 LEU A CB 1 ATOM 830 C CG . LEU A 1 105 ? 31.916 -22.131 -1.952 1.00 83.24 ? 105 LEU A CG 1 ATOM 831 C CD1 . LEU A 1 105 ? 32.136 -20.642 -1.754 1.00 83.25 ? 105 LEU A CD1 1 ATOM 832 C CD2 . LEU A 1 105 ? 30.484 -22.518 -1.639 1.00 86.83 ? 105 LEU A CD2 1 ATOM 833 N N . SER A 1 106 ? 32.942 -24.201 -6.066 1.00 94.53 ? 106 SER A N 1 ATOM 834 C CA A SER A 1 106 ? 32.879 -24.241 -7.526 0.50 95.51 ? 106 SER A CA 1 ATOM 835 C CA B SER A 1 106 ? 32.879 -24.238 -7.520 0.50 95.03 ? 106 SER A CA 1 ATOM 836 C C . SER A 1 106 ? 32.040 -25.428 -7.996 1.00 95.95 ? 106 SER A C 1 ATOM 837 O O . SER A 1 106 ? 31.678 -25.512 -9.168 1.00 96.98 ? 106 SER A O 1 ATOM 838 C CB A SER A 1 106 ? 34.287 -24.294 -8.140 0.50 95.55 ? 106 SER A CB 1 ATOM 839 C CB B SER A 1 106 ? 34.294 -24.294 -8.095 0.50 94.54 ? 106 SER A CB 1 ATOM 840 O OG A SER A 1 106 ? 34.892 -25.566 -7.973 0.50 95.48 ? 106 SER A OG 1 ATOM 841 O OG B SER A 1 106 ? 35.115 -23.325 -7.461 0.50 91.76 ? 106 SER A OG 1 ATOM 842 N N . ARG A 1 107 ? 31.740 -26.343 -7.075 1.00 98.13 ? 107 ARG A N 1 ATOM 843 C CA . ARG A 1 107 ? 30.857 -27.479 -7.342 1.00 101.97 ? 107 ARG A CA 1 ATOM 844 C C . ARG A 1 107 ? 29.473 -27.295 -6.687 1.00 97.91 ? 107 ARG A C 1 ATOM 845 O O . ARG A 1 107 ? 28.693 -28.247 -6.621 1.00 98.06 ? 107 ARG A O 1 ATOM 846 C CB . ARG A 1 107 ? 31.504 -28.792 -6.854 1.00 107.00 ? 107 ARG A CB 1 ATOM 847 C CG . ARG A 1 107 ? 32.512 -29.416 -7.815 1.00 111.66 ? 107 ARG A CG 1 ATOM 848 C CD . ARG A 1 107 ? 33.912 -28.831 -7.657 1.00 115.48 ? 107 ARG A CD 1 ATOM 849 N NE . ARG A 1 107 ? 34.777 -29.139 -8.807 1.00 121.15 ? 107 ARG A NE 1 ATOM 850 C CZ . ARG A 1 107 ? 35.701 -30.105 -8.861 1.00 122.53 ? 107 ARG A CZ 1 ATOM 851 N NH1 . ARG A 1 107 ? 35.939 -30.910 -7.826 1.00 123.73 ? 107 ARG A NH1 1 ATOM 852 N NH2 . ARG A 1 107 ? 36.407 -30.268 -9.974 1.00 124.35 ? 107 ARG A NH2 1 ATOM 853 N N . ILE A 1 108 ? 29.167 -26.080 -6.221 1.00 94.19 ? 108 ILE A N 1 ATOM 854 C CA . ILE A 1 108 ? 27.911 -25.806 -5.499 1.00 93.06 ? 108 ILE A CA 1 ATOM 855 C C . ILE A 1 108 ? 27.141 -24.622 -6.090 1.00 92.43 ? 108 ILE A C 1 ATOM 856 O O . ILE A 1 108 ? 27.713 -23.562 -6.328 1.00 93.53 ? 108 ILE A O 1 ATOM 857 C CB . ILE A 1 108 ? 28.173 -25.519 -4.003 1.00 90.97 ? 108 ILE A CB 1 ATOM 858 C CG1 . ILE A 1 108 ? 28.667 -26.780 -3.290 1.00 91.17 ? 108 ILE A CG1 1 ATOM 859 C CG2 . ILE A 1 108 ? 26.909 -25.018 -3.317 1.00 90.79 ? 108 ILE A CG2 1 ATOM 860 C CD1 . ILE A 1 108 ? 29.234 -26.530 -1.906 1.00 90.20 ? 108 ILE A CD1 1 ATOM 861 N N . ASN A 1 109 ? 25.837 -24.807 -6.290 1.00 93.03 ? 109 ASN A N 1 ATOM 862 C CA . ASN A 1 109 ? 24.958 -23.761 -6.817 1.00 93.64 ? 109 ASN A CA 1 ATOM 863 C C . ASN A 1 109 ? 23.962 -23.196 -5.802 1.00 93.32 ? 109 ASN A C 1 ATOM 864 O O . ASN A 1 109 ? 23.404 -22.117 -6.023 1.00 90.95 ? 109 ASN A O 1 ATOM 865 C CB . ASN A 1 109 ? 24.176 -24.295 -8.019 1.00 96.77 ? 109 ASN A CB 1 ATOM 866 C CG . ASN A 1 109 ? 25.062 -24.558 -9.215 1.00 98.07 ? 109 ASN A CG 1 ATOM 867 O OD1 . ASN A 1 109 ? 25.667 -23.637 -9.762 1.00 98.18 ? 109 ASN A OD1 1 ATOM 868 N ND2 . ASN A 1 109 ? 25.142 -25.817 -9.631 1.00 100.95 ? 109 ASN A ND2 1 ATOM 869 N N . HIS A 1 110 ? 23.715 -23.917 -4.709 1.00 92.98 ? 110 HIS A N 1 ATOM 870 C CA . HIS A 1 110 ? 22.744 -23.454 -3.722 1.00 94.40 ? 110 HIS A CA 1 ATOM 871 C C . HIS A 1 110 ? 23.012 -23.962 -2.308 1.00 93.38 ? 110 HIS A C 1 ATOM 872 O O . HIS A 1 110 ? 23.240 -25.157 -2.085 1.00 91.58 ? 110 HIS A O 1 ATOM 873 C CB . HIS A 1 110 ? 21.325 -23.840 -4.160 1.00 96.93 ? 110 HIS A CB 1 ATOM 874 C CG . HIS A 1 110 ? 20.241 -23.111 -3.427 1.00 98.76 ? 110 HIS A CG 1 ATOM 875 N ND1 . HIS A 1 110 ? 18.977 -23.635 -3.256 1.00 101.17 ? 110 HIS A ND1 1 ATOM 876 C CD2 . HIS A 1 110 ? 20.233 -21.903 -2.815 1.00 98.69 ? 110 HIS A CD2 1 ATOM 877 C CE1 . HIS A 1 110 ? 18.236 -22.780 -2.576 1.00 101.68 ? 110 HIS A CE1 1 ATOM 878 N NE2 . HIS A 1 110 ? 18.975 -21.721 -2.295 1.00 100.46 ? 110 HIS A NE2 1 ATOM 879 N N . PHE A 1 111 ? 22.989 -23.024 -1.365 1.00 92.90 ? 111 PHE A N 1 ATOM 880 C CA . PHE A 1 111 ? 23.012 -23.329 0.056 1.00 93.87 ? 111 PHE A CA 1 ATOM 881 C C . PHE A 1 111 ? 21.647 -23.005 0.632 1.00 95.94 ? 111 PHE A C 1 ATOM 882 O O . PHE A 1 111 ? 21.019 -22.033 0.220 1.00 96.54 ? 111 PHE A O 1 ATOM 883 C CB . PHE A 1 111 ? 24.027 -22.454 0.797 1.00 92.38 ? 111 PHE A CB 1 ATOM 884 C CG . PHE A 1 111 ? 25.465 -22.893 0.668 1.00 90.66 ? 111 PHE A CG 1 ATOM 885 C CD1 . PHE A 1 111 ? 25.838 -24.229 0.785 1.00 90.57 ? 111 PHE A CD1 1 ATOM 886 C CD2 . PHE A 1 111 ? 26.462 -21.944 0.505 1.00 88.17 ? 111 PHE A CD2 1 ATOM 887 C CE1 . PHE A 1 111 ? 27.167 -24.604 0.699 1.00 88.24 ? 111 PHE A CE1 1 ATOM 888 C CE2 . PHE A 1 111 ? 27.788 -22.316 0.423 1.00 86.82 ? 111 PHE A CE2 1 ATOM 889 C CZ . PHE A 1 111 ? 28.143 -23.648 0.520 1.00 86.65 ? 111 PHE A CZ 1 ATOM 890 N N . GLU A 1 112 ? 21.199 -23.807 1.591 1.00 97.83 ? 112 GLU A N 1 ATOM 891 C CA . GLU A 1 112 ? 20.043 -23.451 2.406 1.00 100.66 ? 112 GLU A CA 1 ATOM 892 C C . GLU A 1 112 ? 20.487 -23.413 3.867 1.00 98.30 ? 112 GLU A C 1 ATOM 893 O O . GLU A 1 112 ? 20.828 -24.446 4.448 1.00 95.73 ? 112 GLU A O 1 ATOM 894 C CB . GLU A 1 112 ? 18.892 -24.442 2.198 1.00 104.56 ? 112 GLU A CB 1 ATOM 895 C CG . GLU A 1 112 ? 17.558 -23.975 2.768 1.00 108.55 ? 112 GLU A CG 1 ATOM 896 C CD . GLU A 1 112 ? 16.463 -25.029 2.654 1.00 114.13 ? 112 GLU A CD 1 ATOM 897 O OE1 . GLU A 1 112 ? 16.386 -25.707 1.604 1.00 116.01 ? 112 GLU A OE1 1 ATOM 898 O OE2 . GLU A 1 112 ? 15.674 -25.182 3.615 1.00 115.09 ? 112 GLU A OE2 1 ATOM 899 N N . LYS A 1 113 ? 20.502 -22.213 4.442 1.00 97.04 ? 113 LYS A N 1 ATOM 900 C CA . LYS A 1 113 ? 20.929 -22.019 5.826 1.00 97.70 ? 113 LYS A CA 1 ATOM 901 C C . LYS A 1 113 ? 19.899 -22.568 6.809 1.00 99.50 ? 113 LYS A C 1 ATOM 902 O O . LYS A 1 113 ? 18.705 -22.313 6.659 1.00 101.63 ? 113 LYS A O 1 ATOM 903 C CB . LYS A 1 113 ? 21.157 -20.533 6.099 1.00 97.26 ? 113 LYS A CB 1 ATOM 904 C CG . LYS A 1 113 ? 21.660 -20.237 7.501 1.00 98.63 ? 113 LYS A CG 1 ATOM 905 C CD . LYS A 1 113 ? 22.727 -19.151 7.504 1.00 98.86 ? 113 LYS A CD 1 ATOM 906 C CE . LYS A 1 113 ? 22.167 -17.789 7.140 1.00 99.20 ? 113 LYS A CE 1 ATOM 907 N NZ . LYS A 1 113 ? 23.234 -16.897 6.607 1.00 98.67 ? 113 LYS A NZ 1 ATOM 908 N N . ILE A 1 114 ? 20.362 -23.328 7.801 1.00 99.12 ? 114 ILE A N 1 ATOM 909 C CA . ILE A 1 114 ? 19.490 -23.803 8.875 1.00 102.39 ? 114 ILE A CA 1 ATOM 910 C C . ILE A 1 114 ? 20.144 -23.662 10.247 1.00 104.24 ? 114 ILE A C 1 ATOM 911 O O . ILE A 1 114 ? 21.367 -23.535 10.356 1.00 104.82 ? 114 ILE A O 1 ATOM 912 C CB . ILE A 1 114 ? 19.051 -25.268 8.670 1.00 103.12 ? 114 ILE A CB 1 ATOM 913 C CG1 . ILE A 1 114 ? 20.252 -26.216 8.677 1.00 102.08 ? 114 ILE A CG1 1 ATOM 914 C CG2 . ILE A 1 114 ? 18.259 -25.409 7.377 1.00 103.48 ? 114 ILE A CG2 1 ATOM 915 C CD1 . ILE A 1 114 ? 19.866 -27.650 8.971 1.00 103.04 ? 114 ILE A CD1 1 ATOM 916 N N . GLN A 1 115 ? 19.311 -23.692 11.286 1.00 105.82 ? 115 GLN A N 1 ATOM 917 C CA . GLN A 1 115 ? 19.769 -23.532 12.663 1.00 105.17 ? 115 GLN A CA 1 ATOM 918 C C . GLN A 1 115 ? 20.045 -24.893 13.289 1.00 105.21 ? 115 GLN A C 1 ATOM 919 O O . GLN A 1 115 ? 19.163 -25.750 13.321 1.00 106.25 ? 115 GLN A O 1 ATOM 920 C CB . GLN A 1 115 ? 18.718 -22.791 13.485 1.00 106.29 ? 115 GLN A CB 1 ATOM 921 C CG . GLN A 1 115 ? 19.254 -22.207 14.782 1.00 106.77 ? 115 GLN A CG 1 ATOM 922 C CD . GLN A 1 115 ? 18.155 -21.667 15.669 1.00 107.66 ? 115 GLN A CD 1 ATOM 923 O OE1 . GLN A 1 115 ? 17.992 -20.459 15.804 1.00 107.07 ? 115 GLN A OE1 1 ATOM 924 N NE2 . GLN A 1 115 ? 17.385 -22.564 16.267 1.00 109.70 ? 115 GLN A NE2 1 ATOM 925 N N . ILE A 1 116 ? 21.263 -25.080 13.792 1.00 104.02 ? 116 ILE A N 1 ATOM 926 C CA . ILE A 1 116 ? 21.663 -26.356 14.397 1.00 105.05 ? 116 ILE A CA 1 ATOM 927 C C . ILE A 1 116 ? 21.854 -26.278 15.915 1.00 106.73 ? 116 ILE A C 1 ATOM 928 O O . ILE A 1 116 ? 21.586 -27.251 16.619 1.00 108.58 ? 116 ILE A O 1 ATOM 929 C CB . ILE A 1 116 ? 22.930 -26.939 13.734 1.00 102.46 ? 116 ILE A CB 1 ATOM 930 C CG1 . ILE A 1 116 ? 24.080 -25.924 13.742 1.00 100.24 ? 116 ILE A CG1 1 ATOM 931 C CG2 . ILE A 1 116 ? 22.613 -27.378 12.311 1.00 102.41 ? 116 ILE A CG2 1 ATOM 932 C CD1 . ILE A 1 116 ? 25.426 -26.521 13.400 1.00 98.82 ? 116 ILE A CD1 1 ATOM 933 N N . ILE A 1 117 ? 22.324 -25.136 16.414 1.00 106.88 ? 117 ILE A N 1 ATOM 934 C CA . ILE A 1 117 ? 22.419 -24.903 17.856 1.00 109.29 ? 117 ILE A CA 1 ATOM 935 C C . ILE A 1 117 ? 21.860 -23.514 18.179 1.00 109.89 ? 117 ILE A C 1 ATOM 936 O O . ILE A 1 117 ? 22.562 -22.514 18.016 1.00 110.18 ? 117 ILE A O 1 ATOM 937 C CB . ILE A 1 117 ? 23.868 -25.019 18.376 1.00 108.74 ? 117 ILE A CB 1 ATOM 938 C CG1 . ILE A 1 117 ? 24.542 -26.280 17.821 1.00 107.57 ? 117 ILE A CG1 1 ATOM 939 C CG2 . ILE A 1 117 ? 23.885 -25.038 19.901 1.00 111.04 ? 117 ILE A CG2 1 ATOM 940 C CD1 . ILE A 1 117 ? 25.879 -26.601 18.456 1.00 107.47 ? 117 ILE A CD1 1 ATOM 941 N N . PRO A 1 118 ? 20.593 -23.450 18.638 1.00 111.78 ? 118 PRO A N 1 ATOM 942 C CA . PRO A 1 118 ? 19.949 -22.170 18.950 1.00 113.10 ? 118 PRO A CA 1 ATOM 943 C C . PRO A 1 118 ? 20.738 -21.337 19.959 1.00 113.91 ? 118 PRO A C 1 ATOM 944 O O . PRO A 1 118 ? 21.345 -21.890 20.879 1.00 113.96 ? 118 PRO A O 1 ATOM 945 C CB . PRO A 1 118 ? 18.598 -22.578 19.555 1.00 116.17 ? 118 PRO A CB 1 ATOM 946 C CG . PRO A 1 118 ? 18.371 -23.988 19.145 1.00 115.90 ? 118 PRO A CG 1 ATOM 947 C CD . PRO A 1 118 ? 19.715 -24.602 18.912 1.00 114.15 ? 118 PRO A CD 1 ATOM 948 N N . LYS A 1 119 ? 20.716 -20.020 19.781 1.00 114.66 ? 119 LYS A N 1 ATOM 949 C CA . LYS A 1 119 ? 21.452 -19.104 20.651 1.00 116.89 ? 119 LYS A CA 1 ATOM 950 C C . LYS A 1 119 ? 20.923 -19.150 22.087 1.00 120.77 ? 119 LYS A C 1 ATOM 951 O O . LYS A 1 119 ? 21.694 -19.087 23.048 1.00 122.24 ? 119 LYS A O 1 ATOM 952 C CB . LYS A 1 119 ? 21.361 -17.676 20.107 1.00 117.31 ? 119 LYS A CB 1 ATOM 953 C CG . LYS A 1 119 ? 22.505 -16.779 20.538 1.00 117.87 ? 119 LYS A CG 1 ATOM 954 C CD . LYS A 1 119 ? 22.368 -15.385 19.946 1.00 119.08 ? 119 LYS A CD 1 ATOM 955 C CE . LYS A 1 119 ? 23.716 -14.836 19.505 1.00 118.64 ? 119 LYS A CE 1 ATOM 956 N NZ . LYS A 1 119 ? 23.650 -13.387 19.169 1.00 119.49 ? 119 LYS A NZ 1 ATOM 957 N N . SER A 1 120 ? 19.604 -19.267 22.218 1.00 122.32 ? 120 SER A N 1 ATOM 958 C CA . SER A 1 120 ? 18.944 -19.317 23.520 1.00 124.03 ? 120 SER A CA 1 ATOM 959 C C . SER A 1 120 ? 19.262 -20.588 24.312 1.00 124.07 ? 120 SER A C 1 ATOM 960 O O . SER A 1 120 ? 19.194 -20.583 25.538 1.00 128.02 ? 120 SER A O 1 ATOM 961 C CB . SER A 1 120 ? 17.429 -19.205 23.339 1.00 125.75 ? 120 SER A CB 1 ATOM 962 O OG . SER A 1 120 ? 16.934 -20.279 22.557 1.00 125.92 ? 120 SER A OG 1 ATOM 963 N N . SER A 1 121 ? 19.620 -21.667 23.620 1.00 121.24 ? 121 SER A N 1 ATOM 964 C CA . SER A 1 121 ? 19.845 -22.963 24.270 1.00 120.85 ? 121 SER A CA 1 ATOM 965 C C . SER A 1 121 ? 21.141 -23.050 25.093 1.00 119.38 ? 121 SER A C 1 ATOM 966 O O . SER A 1 121 ? 21.464 -24.114 25.618 1.00 118.08 ? 121 SER A O 1 ATOM 967 C CB . SER A 1 121 ? 19.823 -24.083 23.227 1.00 119.50 ? 121 SER A CB 1 ATOM 968 O OG . SER A 1 121 ? 20.992 -24.056 22.421 1.00 116.81 ? 121 SER A OG 1 ATOM 969 N N . TRP A 1 122 ? 21.880 -21.946 25.194 1.00 118.23 ? 122 TRP A N 1 ATOM 970 C CA . TRP A 1 122 ? 23.076 -21.884 26.032 1.00 117.93 ? 122 TRP A CA 1 ATOM 971 C C . TRP A 1 122 ? 22.712 -21.364 27.415 1.00 121.75 ? 122 TRP A C 1 ATOM 972 O O . TRP A 1 122 ? 22.798 -20.166 27.683 1.00 124.20 ? 122 TRP A O 1 ATOM 973 C CB . TRP A 1 122 ? 24.129 -20.986 25.389 1.00 114.88 ? 122 TRP A CB 1 ATOM 974 C CG . TRP A 1 122 ? 24.678 -21.546 24.123 1.00 111.03 ? 122 TRP A CG 1 ATOM 975 C CD1 . TRP A 1 122 ? 24.449 -21.092 22.860 1.00 108.94 ? 122 TRP A CD1 1 ATOM 976 C CD2 . TRP A 1 122 ? 25.550 -22.675 23.993 1.00 109.66 ? 122 TRP A CD2 1 ATOM 977 N NE1 . TRP A 1 122 ? 25.131 -21.863 21.949 1.00 107.16 ? 122 TRP A NE1 1 ATOM 978 C CE2 . TRP A 1 122 ? 25.815 -22.842 22.619 1.00 107.24 ? 122 TRP A CE2 1 ATOM 979 C CE3 . TRP A 1 122 ? 26.137 -23.559 24.906 1.00 110.09 ? 122 TRP A CE3 1 ATOM 980 C CZ2 . TRP A 1 122 ? 26.640 -23.858 22.133 1.00 105.50 ? 122 TRP A CZ2 1 ATOM 981 C CZ3 . TRP A 1 122 ? 26.956 -24.569 24.423 1.00 108.64 ? 122 TRP A CZ3 1 ATOM 982 C CH2 . TRP A 1 122 ? 27.200 -24.709 23.049 1.00 106.76 ? 122 TRP A CH2 1 ATOM 983 N N . SER A 1 123 ? 22.314 -22.284 28.289 1.00 124.58 ? 123 SER A N 1 ATOM 984 C CA . SER A 1 123 ? 21.743 -21.947 29.593 1.00 127.30 ? 123 SER A CA 1 ATOM 985 C C . SER A 1 123 ? 22.785 -21.727 30.695 1.00 129.32 ? 123 SER A C 1 ATOM 986 O O . SER A 1 123 ? 22.512 -21.027 31.671 1.00 132.12 ? 123 SER A O 1 ATOM 987 C CB . SER A 1 123 ? 20.769 -23.046 30.022 1.00 128.82 ? 123 SER A CB 1 ATOM 988 O OG . SER A 1 123 ? 21.364 -24.325 29.887 1.00 126.59 ? 123 SER A OG 1 ATOM 989 N N . SER A 1 124 ? 23.965 -22.328 30.545 1.00 127.71 ? 124 SER A N 1 ATOM 990 C CA . SER A 1 124 ? 25.030 -22.225 31.550 1.00 128.21 ? 124 SER A CA 1 ATOM 991 C C . SER A 1 124 ? 26.130 -21.230 31.159 1.00 125.82 ? 124 SER A C 1 ATOM 992 O O . SER A 1 124 ? 27.102 -21.057 31.896 1.00 125.67 ? 124 SER A O 1 ATOM 993 C CB . SER A 1 124 ? 25.651 -23.602 31.785 1.00 128.38 ? 124 SER A CB 1 ATOM 994 O OG . SER A 1 124 ? 24.649 -24.592 31.931 1.00 129.72 ? 124 SER A OG 1 ATOM 995 N N . HIS A 1 125 ? 25.974 -20.587 30.002 1.00 123.56 ? 125 HIS A N 1 ATOM 996 C CA . HIS A 1 125 ? 26.961 -19.639 29.484 1.00 121.26 ? 125 HIS A CA 1 ATOM 997 C C . HIS A 1 125 ? 26.260 -18.410 28.931 1.00 122.35 ? 125 HIS A C 1 ATOM 998 O O . HIS A 1 125 ? 25.133 -18.497 28.439 1.00 123.90 ? 125 HIS A O 1 ATOM 999 C CB . HIS A 1 125 ? 27.783 -20.276 28.360 1.00 116.50 ? 125 HIS A CB 1 ATOM 1000 C CG . HIS A 1 125 ? 28.483 -21.538 28.753 1.00 115.24 ? 125 HIS A CG 1 ATOM 1001 N ND1 . HIS A 1 125 ? 27.855 -22.765 28.761 1.00 115.59 ? 125 HIS A ND1 1 ATOM 1002 C CD2 . HIS A 1 125 ? 29.760 -21.766 29.141 1.00 114.22 ? 125 HIS A CD2 1 ATOM 1003 C CE1 . HIS A 1 125 ? 28.713 -23.693 29.145 1.00 115.61 ? 125 HIS A CE1 1 ATOM 1004 N NE2 . HIS A 1 125 ? 29.877 -23.113 29.380 1.00 115.04 ? 125 HIS A NE2 1 ATOM 1005 N N . GLU A 1 126 ? 26.935 -17.267 28.996 1.00 122.64 ? 126 GLU A N 1 ATOM 1006 C CA . GLU A 1 126 ? 26.412 -16.047 28.398 1.00 122.71 ? 126 GLU A CA 1 ATOM 1007 C C . GLU A 1 126 ? 26.679 -16.096 26.902 1.00 119.55 ? 126 GLU A C 1 ATOM 1008 O O . GLU A 1 126 ? 27.824 -16.263 26.477 1.00 119.29 ? 126 GLU A O 1 ATOM 1009 C CB . GLU A 1 126 ? 27.069 -14.816 29.022 1.00 124.87 ? 126 GLU A CB 1 ATOM 1010 C CG . GLU A 1 126 ? 26.543 -13.483 28.504 1.00 125.44 ? 126 GLU A CG 1 ATOM 1011 C CD . GLU A 1 126 ? 25.040 -13.330 28.664 1.00 127.51 ? 126 GLU A CD 1 ATOM 1012 O OE1 . GLU A 1 126 ? 24.560 -13.295 29.820 1.00 127.32 ? 126 GLU A OE1 1 ATOM 1013 O OE2 . GLU A 1 126 ? 24.343 -13.241 27.627 1.00 127.12 ? 126 GLU A OE2 1 ATOM 1014 N N . ALA A 1 127 ? 25.618 -15.964 26.110 1.00 118.23 ? 127 ALA A N 1 ATOM 1015 C CA . ALA A 1 127 ? 25.712 -16.092 24.654 1.00 113.49 ? 127 ALA A CA 1 ATOM 1016 C C . ALA A 1 127 ? 25.326 -14.814 23.907 1.00 112.28 ? 127 ALA A C 1 ATOM 1017 O O . ALA A 1 127 ? 25.398 -14.778 22.678 1.00 110.66 ? 127 ALA A O 1 ATOM 1018 C CB . ALA A 1 127 ? 24.844 -17.250 24.185 1.00 112.82 ? 127 ALA A CB 1 ATOM 1019 N N . SER A 1 128 ? 24.938 -13.770 24.640 1.00 113.22 ? 128 SER A N 1 ATOM 1020 C CA . SER A 1 128 ? 24.454 -12.528 24.032 1.00 112.30 ? 128 SER A CA 1 ATOM 1021 C C . SER A 1 128 ? 25.404 -11.341 24.207 1.00 110.73 ? 128 SER A C 1 ATOM 1022 O O . SER A 1 128 ? 25.072 -10.224 23.810 1.00 110.23 ? 128 SER A O 1 ATOM 1023 C CB . SER A 1 128 ? 23.090 -12.180 24.612 1.00 116.11 ? 128 SER A CB 1 ATOM 1024 O OG . SER A 1 128 ? 22.211 -13.281 24.493 1.00 118.40 ? 128 SER A OG 1 ATOM 1025 N N . LEU A 1 129 ? 26.577 -11.582 24.790 1.00 109.25 ? 129 LEU A N 1 ATOM 1026 C CA . LEU A 1 129 ? 27.587 -10.539 24.979 1.00 108.51 ? 129 LEU A CA 1 ATOM 1027 C C . LEU A 1 129 ? 28.855 -10.815 24.176 1.00 105.31 ? 129 LEU A C 1 ATOM 1028 O O . LEU A 1 129 ? 29.877 -10.162 24.389 1.00 105.10 ? 129 LEU A O 1 ATOM 1029 C CB . LEU A 1 129 ? 27.940 -10.407 26.461 1.00 111.34 ? 129 LEU A CB 1 ATOM 1030 C CG . LEU A 1 129 ? 26.768 -10.128 27.406 1.00 114.68 ? 129 LEU A CG 1 ATOM 1031 C CD1 . LEU A 1 129 ? 27.268 -9.980 28.835 1.00 117.09 ? 129 LEU A CD1 1 ATOM 1032 C CD2 . LEU A 1 129 ? 25.994 -8.891 26.972 1.00 115.63 ? 129 LEU A CD2 1 ATOM 1033 N N . GLY A 1 130 ? 28.782 -11.772 23.251 1.00 102.60 ? 130 GLY A N 1 ATOM 1034 C CA . GLY A 1 130 ? 29.910 -12.114 22.394 1.00 98.84 ? 130 GLY A CA 1 ATOM 1035 C C . GLY A 1 130 ? 30.027 -11.199 21.189 1.00 96.67 ? 130 GLY A C 1 ATOM 1036 O O . GLY A 1 130 ? 29.808 -11.629 20.048 1.00 94.68 ? 130 GLY A O 1 ATOM 1037 N N . VAL A 1 131 ? 30.404 -9.946 21.450 1.00 96.41 ? 131 VAL A N 1 ATOM 1038 C CA . VAL A 1 131 ? 30.450 -8.891 20.433 1.00 94.52 ? 131 VAL A CA 1 ATOM 1039 C C . VAL A 1 131 ? 31.763 -8.103 20.473 1.00 93.85 ? 131 VAL A C 1 ATOM 1040 O O . VAL A 1 131 ? 32.538 -8.221 21.418 1.00 95.06 ? 131 VAL A O 1 ATOM 1041 C CB . VAL A 1 131 ? 29.263 -7.918 20.595 1.00 95.96 ? 131 VAL A CB 1 ATOM 1042 C CG1 . VAL A 1 131 ? 27.957 -8.622 20.258 1.00 95.66 ? 131 VAL A CG1 1 ATOM 1043 C CG2 . VAL A 1 131 ? 29.211 -7.340 22.005 1.00 97.93 ? 131 VAL A CG2 1 ATOM 1044 N N . SER A 1 132 ? 31.997 -7.300 19.438 1.00 93.03 ? 132 SER A N 1 ATOM 1045 C CA . SER A 1 132 ? 33.222 -6.507 19.319 1.00 92.47 ? 132 SER A CA 1 ATOM 1046 C C . SER A 1 132 ? 33.016 -5.251 18.473 1.00 92.31 ? 132 SER A C 1 ATOM 1047 O O . SER A 1 132 ? 32.180 -5.230 17.565 1.00 91.07 ? 132 SER A O 1 ATOM 1048 C CB . SER A 1 132 ? 34.339 -7.350 18.701 1.00 90.40 ? 132 SER A CB 1 ATOM 1049 O OG . SER A 1 132 ? 35.498 -6.568 18.466 1.00 89.97 ? 132 SER A OG 1 ATOM 1050 N N . SER A 1 133 ? 33.800 -4.216 18.773 1.00 93.72 ? 133 SER A N 1 ATOM 1051 C CA . SER A 1 133 ? 33.771 -2.959 18.015 1.00 94.38 ? 133 SER A CA 1 ATOM 1052 C C . SER A 1 133 ? 34.338 -3.122 16.601 1.00 92.92 ? 133 SER A C 1 ATOM 1053 O O . SER A 1 133 ? 34.089 -2.289 15.733 1.00 91.91 ? 133 SER A O 1 ATOM 1054 C CB . SER A 1 133 ? 34.538 -1.865 18.764 1.00 96.09 ? 133 SER A CB 1 ATOM 1055 O OG . SER A 1 133 ? 35.829 -2.313 19.146 1.00 95.59 ? 133 SER A OG 1 ATOM 1056 N N . ALA A 1 134 ? 35.095 -4.194 16.380 1.00 93.72 ? 134 ALA A N 1 ATOM 1057 C CA . ALA A 1 134 ? 35.619 -4.524 15.057 1.00 94.56 ? 134 ALA A CA 1 ATOM 1058 C C . ALA A 1 134 ? 34.530 -4.973 14.071 1.00 95.77 ? 134 ALA A C 1 ATOM 1059 O O . ALA A 1 134 ? 34.695 -4.816 12.858 1.00 93.48 ? 134 ALA A O 1 ATOM 1060 C CB . ALA A 1 134 ? 36.688 -5.598 15.177 1.00 94.74 ? 134 ALA A CB 1 ATOM 1061 N N . CYS A 1 135 ? 33.427 -5.518 14.588 1.00 98.20 ? 135 CYS A N 1 ATOM 1062 C CA . CYS A 1 135 ? 32.307 -5.964 13.757 1.00 99.37 ? 135 CYS A CA 1 ATOM 1063 C C . CYS A 1 135 ? 31.039 -5.143 14.017 1.00 98.75 ? 135 CYS A C 1 ATOM 1064 O O . CYS A 1 135 ? 30.040 -5.674 14.510 1.00 96.81 ? 135 CYS A O 1 ATOM 1065 C CB . CYS A 1 135 ? 32.028 -7.442 14.020 1.00 103.43 ? 135 CYS A CB 1 ATOM 1066 S SG . CYS A 1 135 ? 33.452 -8.510 13.733 1.00 109.37 ? 135 CYS A SG 1 ATOM 1067 N N . PRO A 1 136 ? 31.067 -3.844 13.666 1.00 97.55 ? 136 PRO A N 1 ATOM 1068 C CA . PRO A 1 136 ? 29.944 -2.977 13.999 1.00 97.99 ? 136 PRO A CA 1 ATOM 1069 C C . PRO A 1 136 ? 28.730 -3.218 13.111 1.00 96.54 ? 136 PRO A C 1 ATOM 1070 O O . PRO A 1 136 ? 28.881 -3.609 11.955 1.00 93.69 ? 136 PRO A O 1 ATOM 1071 C CB . PRO A 1 136 ? 30.506 -1.580 13.738 1.00 99.40 ? 136 PRO A CB 1 ATOM 1072 C CG . PRO A 1 136 ? 31.465 -1.789 12.617 1.00 97.00 ? 136 PRO A CG 1 ATOM 1073 C CD . PRO A 1 136 ? 32.097 -3.124 12.893 1.00 95.60 ? 136 PRO A CD 1 ATOM 1074 N N . TYR A 1 137 ? 27.543 -2.984 13.664 1.00 97.61 ? 137 TYR A N 1 ATOM 1075 C CA . TYR A 1 137 ? 26.300 -3.000 12.902 1.00 96.96 ? 137 TYR A CA 1 ATOM 1076 C C . TYR A 1 137 ? 25.390 -1.887 13.402 1.00 98.48 ? 137 TYR A C 1 ATOM 1077 O O . TYR A 1 137 ? 24.951 -1.914 14.552 1.00 100.17 ? 137 TYR A O 1 ATOM 1078 C CB . TYR A 1 137 ? 25.592 -4.344 13.050 1.00 97.50 ? 137 TYR A CB 1 ATOM 1079 C CG . TYR A 1 137 ? 24.254 -4.399 12.343 1.00 98.32 ? 137 TYR A CG 1 ATOM 1080 C CD1 . TYR A 1 137 ? 24.183 -4.417 10.950 1.00 97.33 ? 137 TYR A CD1 1 ATOM 1081 C CD2 . TYR A 1 137 ? 23.061 -4.432 13.063 1.00 99.42 ? 137 TYR A CD2 1 ATOM 1082 C CE1 . TYR A 1 137 ? 22.964 -4.468 10.296 1.00 97.67 ? 137 TYR A CE1 1 ATOM 1083 C CE2 . TYR A 1 137 ? 21.837 -4.485 12.417 1.00 100.42 ? 137 TYR A CE2 1 ATOM 1084 C CZ . TYR A 1 137 ? 21.795 -4.503 11.035 1.00 99.66 ? 137 TYR A CZ 1 ATOM 1085 O OH . TYR A 1 137 ? 20.586 -4.555 10.387 1.00 100.30 ? 137 TYR A OH 1 ATOM 1086 N N . GLN A 1 138 ? 25.114 -0.917 12.532 1.00 98.01 ? 138 GLN A N 1 ATOM 1087 C CA . GLN A 1 138 ? 24.301 0.247 12.878 1.00 100.59 ? 138 GLN A CA 1 ATOM 1088 C C . GLN A 1 138 ? 24.888 1.008 14.073 1.00 101.28 ? 138 GLN A C 1 ATOM 1089 O O . GLN A 1 138 ? 24.166 1.432 14.974 1.00 102.71 ? 138 GLN A O 1 ATOM 1090 C CB . GLN A 1 138 ? 22.848 -0.167 13.146 1.00 103.62 ? 138 GLN A CB 1 ATOM 1091 C CG . GLN A 1 138 ? 22.192 -0.907 11.987 1.00 103.76 ? 138 GLN A CG 1 ATOM 1092 C CD . GLN A 1 138 ? 20.730 -1.239 12.243 1.00 107.09 ? 138 GLN A CD 1 ATOM 1093 O OE1 . GLN A 1 138 ? 20.208 -1.030 13.342 1.00 109.17 ? 138 GLN A OE1 1 ATOM 1094 N NE2 . GLN A 1 138 ? 20.060 -1.765 11.224 1.00 107.32 ? 138 GLN A NE2 1 ATOM 1095 N N . GLY A 1 139 ? 26.210 1.165 14.069 1.00 100.07 ? 139 GLY A N 1 ATOM 1096 C CA . GLY A 1 139 ? 26.912 1.926 15.099 1.00 100.59 ? 139 GLY A CA 1 ATOM 1097 C C . GLY A 1 139 ? 27.200 1.179 16.389 1.00 100.43 ? 139 GLY A C 1 ATOM 1098 O O . GLY A 1 139 ? 27.851 1.729 17.276 1.00 101.42 ? 139 GLY A O 1 ATOM 1099 N N . LYS A 1 140 ? 26.734 -0.065 16.495 1.00 99.50 ? 140 LYS A N 1 ATOM 1100 C CA . LYS A 1 140 ? 26.860 -0.851 17.725 1.00 101.25 ? 140 LYS A CA 1 ATOM 1101 C C . LYS A 1 140 ? 27.751 -2.060 17.504 1.00 99.09 ? 140 LYS A C 1 ATOM 1102 O O . LYS A 1 140 ? 27.834 -2.578 16.393 1.00 97.35 ? 140 LYS A O 1 ATOM 1103 C CB . LYS A 1 140 ? 25.490 -1.344 18.193 1.00 103.41 ? 140 LYS A CB 1 ATOM 1104 C CG . LYS A 1 140 ? 24.506 -0.247 18.552 1.00 107.07 ? 140 LYS A CG 1 ATOM 1105 C CD . LYS A 1 140 ? 23.082 -0.783 18.593 1.00 109.06 ? 140 LYS A CD 1 ATOM 1106 C CE . LYS A 1 140 ? 22.064 0.335 18.768 1.00 112.24 ? 140 LYS A CE 1 ATOM 1107 N NZ . LYS A 1 140 ? 22.032 0.874 20.157 1.00 115.08 ? 140 LYS A NZ 1 ATOM 1108 N N . SER A 1 141 ? 28.394 -2.519 18.576 1.00 99.91 ? 141 SER A N 1 ATOM 1109 C CA . SER A 1 141 ? 29.267 -3.690 18.518 1.00 97.32 ? 141 SER A CA 1 ATOM 1110 C C . SER A 1 141 ? 28.461 -4.974 18.301 1.00 97.20 ? 141 SER A C 1 ATOM 1111 O O . SER A 1 141 ? 27.599 -5.324 19.110 1.00 99.42 ? 141 SER A O 1 ATOM 1112 C CB . SER A 1 141 ? 30.095 -3.797 19.797 1.00 97.71 ? 141 SER A CB 1 ATOM 1113 O OG . SER A 1 141 ? 31.003 -2.713 19.894 1.00 98.35 ? 141 SER A OG 1 ATOM 1114 N N . SER A 1 142 ? 28.750 -5.662 17.200 1.00 95.02 ? 142 SER A N 1 ATOM 1115 C CA . SER A 1 142 ? 28.059 -6.894 16.831 1.00 94.11 ? 142 SER A CA 1 ATOM 1116 C C . SER A 1 142 ? 29.099 -7.985 16.563 1.00 91.22 ? 142 SER A C 1 ATOM 1117 O O . SER A 1 142 ? 30.234 -7.880 17.025 1.00 89.20 ? 142 SER A O 1 ATOM 1118 C CB . SER A 1 142 ? 27.171 -6.643 15.606 1.00 94.65 ? 142 SER A CB 1 ATOM 1119 O OG . SER A 1 142 ? 26.400 -7.784 15.277 1.00 95.30 ? 142 SER A OG 1 ATOM 1120 N N . PHE A 1 143 ? 28.714 -9.033 15.836 1.00 90.51 ? 143 PHE A N 1 ATOM 1121 C CA . PHE A 1 143 ? 29.614 -10.154 15.559 1.00 89.72 ? 143 PHE A CA 1 ATOM 1122 C C . PHE A 1 143 ? 29.094 -11.029 14.422 1.00 89.62 ? 143 PHE A C 1 ATOM 1123 O O . PHE A 1 143 ? 27.921 -10.952 14.060 1.00 92.23 ? 143 PHE A O 1 ATOM 1124 C CB . PHE A 1 143 ? 29.786 -11.008 16.817 1.00 90.76 ? 143 PHE A CB 1 ATOM 1125 C CG . PHE A 1 143 ? 30.963 -11.941 16.765 1.00 90.13 ? 143 PHE A CG 1 ATOM 1126 C CD1 . PHE A 1 143 ? 32.256 -11.440 16.674 1.00 88.78 ? 143 PHE A CD1 1 ATOM 1127 C CD2 . PHE A 1 143 ? 30.783 -13.317 16.817 1.00 89.97 ? 143 PHE A CD2 1 ATOM 1128 C CE1 . PHE A 1 143 ? 33.345 -12.291 16.634 1.00 88.27 ? 143 PHE A CE1 1 ATOM 1129 C CE2 . PHE A 1 143 ? 31.871 -14.174 16.779 1.00 89.74 ? 143 PHE A CE2 1 ATOM 1130 C CZ . PHE A 1 143 ? 33.154 -13.661 16.687 1.00 88.55 ? 143 PHE A CZ 1 ATOM 1131 N N . PHE A 1 144 ? 29.977 -11.853 13.862 1.00 88.43 ? 144 PHE A N 1 ATOM 1132 C CA . PHE A 1 144 ? 29.601 -12.845 12.854 1.00 86.59 ? 144 PHE A CA 1 ATOM 1133 C C . PHE A 1 144 ? 28.281 -13.520 13.237 1.00 87.57 ? 144 PHE A C 1 ATOM 1134 O O . PHE A 1 144 ? 28.179 -14.151 14.283 1.00 90.12 ? 144 PHE A O 1 ATOM 1135 C CB . PHE A 1 144 ? 30.691 -13.911 12.707 1.00 85.99 ? 144 PHE A CB 1 ATOM 1136 C CG . PHE A 1 144 ? 32.023 -13.374 12.245 1.00 86.46 ? 144 PHE A CG 1 ATOM 1137 C CD1 . PHE A 1 144 ? 32.180 -12.869 10.963 1.00 85.70 ? 144 PHE A CD1 1 ATOM 1138 C CD2 . PHE A 1 144 ? 33.125 -13.379 13.096 1.00 87.23 ? 144 PHE A CD2 1 ATOM 1139 C CE1 . PHE A 1 144 ? 33.407 -12.383 10.538 1.00 85.24 ? 144 PHE A CE1 1 ATOM 1140 C CE2 . PHE A 1 144 ? 34.351 -12.891 12.676 1.00 86.59 ? 144 PHE A CE2 1 ATOM 1141 C CZ . PHE A 1 144 ? 34.493 -12.394 11.393 1.00 85.48 ? 144 PHE A CZ 1 ATOM 1142 N N . ARG A 1 145 ? 27.282 -13.392 12.377 1.00 87.18 ? 145 ARG A N 1 ATOM 1143 C CA . ARG A 1 145 ? 25.916 -13.784 12.706 1.00 87.67 ? 145 ARG A CA 1 ATOM 1144 C C . ARG A 1 145 ? 25.666 -15.288 12.789 1.00 88.85 ? 145 ARG A C 1 ATOM 1145 O O . ARG A 1 145 ? 24.669 -15.714 13.375 1.00 92.67 ? 145 ARG A O 1 ATOM 1146 C CB . ARG A 1 145 ? 24.953 -13.183 11.688 1.00 86.21 ? 145 ARG A CB 1 ATOM 1147 C CG . ARG A 1 145 ? 24.970 -11.666 11.656 1.00 86.12 ? 145 ARG A CG 1 ATOM 1148 C CD . ARG A 1 145 ? 23.676 -11.153 11.064 1.00 87.70 ? 145 ARG A CD 1 ATOM 1149 N NE . ARG A 1 145 ? 23.652 -9.703 10.931 1.00 88.54 ? 145 ARG A NE 1 ATOM 1150 C CZ . ARG A 1 145 ? 23.441 -8.856 11.933 1.00 91.43 ? 145 ARG A CZ 1 ATOM 1151 N NH1 . ARG A 1 145 ? 23.265 -9.290 13.178 1.00 92.45 ? 145 ARG A NH1 1 ATOM 1152 N NH2 . ARG A 1 145 ? 23.421 -7.555 11.689 1.00 93.71 ? 145 ARG A NH2 1 ATOM 1153 N N . ASN A 1 146 ? 26.551 -16.088 12.205 1.00 88.85 ? 146 ASN A N 1 ATOM 1154 C CA . ASN A 1 146 ? 26.332 -17.531 12.111 1.00 89.11 ? 146 ASN A CA 1 ATOM 1155 C C . ASN A 1 146 ? 27.024 -18.333 13.202 1.00 89.38 ? 146 ASN A C 1 ATOM 1156 O O . ASN A 1 146 ? 26.788 -19.535 13.330 1.00 90.10 ? 146 ASN A O 1 ATOM 1157 C CB . ASN A 1 146 ? 26.760 -18.037 10.734 1.00 88.22 ? 146 ASN A CB 1 ATOM 1158 C CG . ASN A 1 146 ? 25.938 -17.428 9.618 1.00 88.85 ? 146 ASN A CG 1 ATOM 1159 O OD1 . ASN A 1 146 ? 24.740 -17.195 9.778 1.00 92.55 ? 146 ASN A OD1 1 ATOM 1160 N ND2 . ASN A 1 146 ? 26.573 -17.164 8.486 1.00 88.29 ? 146 ASN A ND2 1 ATOM 1161 N N . VAL A 1 147 ? 27.868 -17.671 13.988 1.00 89.03 ? 147 VAL A N 1 ATOM 1162 C CA . VAL A 1 147 ? 28.538 -18.325 15.104 1.00 90.35 ? 147 VAL A CA 1 ATOM 1163 C C . VAL A 1 147 ? 28.380 -17.510 16.386 1.00 91.27 ? 147 VAL A C 1 ATOM 1164 O O . VAL A 1 147 ? 28.286 -16.285 16.346 1.00 92.73 ? 147 VAL A O 1 ATOM 1165 C CB . VAL A 1 147 ? 30.024 -18.591 14.795 1.00 90.29 ? 147 VAL A CB 1 ATOM 1166 C CG1 . VAL A 1 147 ? 30.149 -19.583 13.648 1.00 90.03 ? 147 VAL A CG1 1 ATOM 1167 C CG2 . VAL A 1 147 ? 30.765 -17.302 14.458 1.00 89.78 ? 147 VAL A CG2 1 ATOM 1168 N N . VAL A 1 148 ? 28.342 -18.203 17.518 1.00 92.11 ? 148 VAL A N 1 ATOM 1169 C CA . VAL A 1 148 ? 28.084 -17.583 18.815 1.00 93.55 ? 148 VAL A CA 1 ATOM 1170 C C . VAL A 1 148 ? 29.371 -17.530 19.624 1.00 93.26 ? 148 VAL A C 1 ATOM 1171 O O . VAL A 1 148 ? 29.974 -18.565 19.900 1.00 94.11 ? 148 VAL A O 1 ATOM 1172 C CB . VAL A 1 148 ? 27.036 -18.390 19.606 1.00 95.84 ? 148 VAL A CB 1 ATOM 1173 C CG1 . VAL A 1 148 ? 26.693 -17.696 20.916 1.00 98.78 ? 148 VAL A CG1 1 ATOM 1174 C CG2 . VAL A 1 148 ? 25.784 -18.601 18.766 1.00 96.44 ? 148 VAL A CG2 1 ATOM 1175 N N . TRP A 1 149 ? 29.792 -16.325 19.995 1.00 93.59 ? 149 TRP A N 1 ATOM 1176 C CA . TRP A 1 149 ? 30.964 -16.151 20.853 1.00 94.97 ? 149 TRP A CA 1 ATOM 1177 C C . TRP A 1 149 ? 30.552 -16.263 22.331 1.00 97.39 ? 149 TRP A C 1 ATOM 1178 O O . TRP A 1 149 ? 30.052 -15.306 22.923 1.00 97.92 ? 149 TRP A O 1 ATOM 1179 C CB . TRP A 1 149 ? 31.638 -14.809 20.546 1.00 94.10 ? 149 TRP A CB 1 ATOM 1180 C CG . TRP A 1 149 ? 32.917 -14.546 21.287 1.00 93.76 ? 149 TRP A CG 1 ATOM 1181 C CD1 . TRP A 1 149 ? 33.587 -15.397 22.120 1.00 94.59 ? 149 TRP A CD1 1 ATOM 1182 C CD2 . TRP A 1 149 ? 33.706 -13.355 21.216 1.00 93.23 ? 149 TRP A CD2 1 ATOM 1183 N NE1 . TRP A 1 149 ? 34.730 -14.798 22.589 1.00 95.28 ? 149 TRP A NE1 1 ATOM 1184 C CE2 . TRP A 1 149 ? 34.829 -13.545 22.047 1.00 93.87 ? 149 TRP A CE2 1 ATOM 1185 C CE3 . TRP A 1 149 ? 33.568 -12.141 20.536 1.00 93.13 ? 149 TRP A CE3 1 ATOM 1186 C CZ2 . TRP A 1 149 ? 35.809 -12.568 22.218 1.00 93.70 ? 149 TRP A CZ2 1 ATOM 1187 C CZ3 . TRP A 1 149 ? 34.544 -11.170 20.706 1.00 93.96 ? 149 TRP A CZ3 1 ATOM 1188 C CH2 . TRP A 1 149 ? 35.650 -11.391 21.540 1.00 93.79 ? 149 TRP A CH2 1 ATOM 1189 N N . LEU A 1 150 ? 30.766 -17.442 22.913 1.00 98.21 ? 150 LEU A N 1 ATOM 1190 C CA . LEU A 1 150 ? 30.323 -17.728 24.277 1.00 101.36 ? 150 LEU A CA 1 ATOM 1191 C C . LEU A 1 150 ? 31.349 -17.252 25.296 1.00 102.78 ? 150 LEU A C 1 ATOM 1192 O O . LEU A 1 150 ? 32.551 -17.425 25.087 1.00 101.99 ? 150 LEU A O 1 ATOM 1193 C CB . LEU A 1 150 ? 30.089 -19.230 24.457 1.00 102.33 ? 150 LEU A CB 1 ATOM 1194 C CG . LEU A 1 150 ? 29.024 -19.869 23.558 1.00 102.31 ? 150 LEU A CG 1 ATOM 1195 C CD1 . LEU A 1 150 ? 29.106 -21.388 23.607 1.00 102.71 ? 150 LEU A CD1 1 ATOM 1196 C CD2 . LEU A 1 150 ? 27.630 -19.401 23.949 1.00 104.31 ? 150 LEU A CD2 1 ATOM 1197 N N . ILE A 1 151 ? 30.863 -16.654 26.389 1.00 104.67 ? 151 ILE A N 1 ATOM 1198 C CA . ILE A 1 151 ? 31.705 -16.251 27.526 1.00 105.58 ? 151 ILE A CA 1 ATOM 1199 C C . ILE A 1 151 ? 31.104 -16.714 28.860 1.00 107.94 ? 151 ILE A C 1 ATOM 1200 O O . ILE A 1 151 ? 29.947 -17.136 28.923 1.00 108.03 ? 151 ILE A O 1 ATOM 1201 C CB . ILE A 1 151 ? 31.932 -14.721 27.569 1.00 105.83 ? 151 ILE A CB 1 ATOM 1202 C CG1 . ILE A 1 151 ? 30.614 -13.970 27.792 1.00 107.86 ? 151 ILE A CG1 1 ATOM 1203 C CG2 . ILE A 1 151 ? 32.595 -14.244 26.286 1.00 103.38 ? 151 ILE A CG2 1 ATOM 1204 C CD1 . ILE A 1 151 ? 30.783 -12.473 27.950 1.00 108.50 ? 151 ILE A CD1 1 ATOM 1205 N N . LYS A 1 152 ? 31.903 -16.613 29.920 1.00 109.92 ? 152 LYS A N 1 ATOM 1206 C CA . LYS A 1 152 ? 31.511 -17.060 31.264 1.00 113.12 ? 152 LYS A CA 1 ATOM 1207 C C . LYS A 1 152 ? 30.205 -16.439 31.775 1.00 116.15 ? 152 LYS A C 1 ATOM 1208 O O . LYS A 1 152 ? 29.890 -15.288 31.470 1.00 116.30 ? 152 LYS A O 1 ATOM 1209 C CB . LYS A 1 152 ? 32.632 -16.761 32.266 1.00 113.97 ? 152 LYS A CB 1 ATOM 1210 C CG . LYS A 1 152 ? 32.852 -15.280 32.534 1.00 114.40 ? 152 LYS A CG 1 ATOM 1211 C CD . LYS A 1 152 ? 34.031 -15.049 33.463 1.00 115.72 ? 152 LYS A CD 1 ATOM 1212 C CE . LYS A 1 152 ? 34.008 -13.648 34.049 1.00 116.60 ? 152 LYS A CE 1 ATOM 1213 N NZ . LYS A 1 152 ? 35.244 -13.371 34.829 1.00 118.05 ? 152 LYS A NZ 1 ATOM 1214 N N . LYS A 1 153 ? 29.469 -17.213 32.572 1.00 119.45 ? 153 LYS A N 1 ATOM 1215 C CA . LYS A 1 153 ? 28.194 -16.783 33.147 1.00 122.66 ? 153 LYS A CA 1 ATOM 1216 C C . LYS A 1 153 ? 28.252 -16.897 34.668 1.00 126.08 ? 153 LYS A C 1 ATOM 1217 O O . LYS A 1 153 ? 28.520 -17.972 35.205 1.00 125.28 ? 153 LYS A O 1 ATOM 1218 C CB . LYS A 1 153 ? 27.057 -17.638 32.587 1.00 122.97 ? 153 LYS A CB 1 ATOM 1219 C CG . LYS A 1 153 ? 25.670 -17.297 33.113 1.00 125.91 ? 153 LYS A CG 1 ATOM 1220 C CD . LYS A 1 153 ? 24.589 -17.794 32.161 1.00 125.69 ? 153 LYS A CD 1 ATOM 1221 C CE . LYS A 1 153 ? 23.304 -18.158 32.888 1.00 128.91 ? 153 LYS A CE 1 ATOM 1222 N NZ . LYS A 1 153 ? 22.764 -17.042 33.709 1.00 132.54 ? 153 LYS A NZ 1 ATOM 1223 N N . ASN A 1 154 ? 27.999 -15.779 35.348 1.00 129.17 ? 154 ASN A N 1 ATOM 1224 C CA . ASN A 1 154 ? 28.140 -15.676 36.803 1.00 134.06 ? 154 ASN A CA 1 ATOM 1225 C C . ASN A 1 154 ? 29.496 -16.206 37.288 1.00 134.17 ? 154 ASN A C 1 ATOM 1226 O O . ASN A 1 154 ? 29.571 -17.020 38.211 1.00 135.32 ? 154 ASN A O 1 ATOM 1227 C CB . ASN A 1 154 ? 26.975 -16.379 37.521 1.00 137.11 ? 154 ASN A CB 1 ATOM 1228 C CG . ASN A 1 154 ? 26.854 -15.977 38.985 1.00 142.18 ? 154 ASN A CG 1 ATOM 1229 O OD1 . ASN A 1 154 ? 26.468 -16.785 39.833 1.00 145.40 ? 154 ASN A OD1 1 ATOM 1230 N ND2 . ASN A 1 154 ? 27.185 -14.726 39.289 1.00 143.48 ? 154 ASN A ND2 1 ATOM 1231 N N . SER A 1 155 ? 30.560 -15.746 36.630 1.00 132.04 ? 155 SER A N 1 ATOM 1232 C CA . SER A 1 155 ? 31.939 -16.041 37.031 1.00 132.22 ? 155 SER A CA 1 ATOM 1233 C C . SER A 1 155 ? 32.357 -17.509 36.869 1.00 131.43 ? 155 SER A C 1 ATOM 1234 O O . SER A 1 155 ? 33.282 -17.953 37.542 1.00 134.34 ? 155 SER A O 1 ATOM 1235 C CB . SER A 1 155 ? 32.176 -15.594 38.485 1.00 134.73 ? 155 SER A CB 1 ATOM 1236 O OG . SER A 1 155 ? 31.717 -14.272 38.691 1.00 135.81 ? 155 SER A OG 1 ATOM 1237 N N . THR A 1 156 ? 31.685 -18.260 35.995 1.00 129.09 ? 156 THR A N 1 ATOM 1238 C CA . THR A 1 156 ? 32.062 -19.658 35.733 1.00 128.41 ? 156 THR A CA 1 ATOM 1239 C C . THR A 1 156 ? 31.798 -20.042 34.278 1.00 125.09 ? 156 THR A C 1 ATOM 1240 O O . THR A 1 156 ? 30.780 -19.652 33.707 1.00 125.37 ? 156 THR A O 1 ATOM 1241 C CB . THR A 1 156 ? 31.291 -20.667 36.620 1.00 131.07 ? 156 THR A CB 1 ATOM 1242 O OG1 . THR A 1 156 ? 29.948 -20.805 36.142 1.00 132.06 ? 156 THR A OG1 1 ATOM 1243 C CG2 . THR A 1 156 ? 31.266 -20.244 38.087 1.00 135.14 ? 156 THR A CG2 1 ATOM 1244 N N . TYR A 1 157 ? 32.718 -20.810 33.695 1.00 122.86 ? 157 TYR A N 1 ATOM 1245 C CA . TYR A 1 157 ? 32.551 -21.380 32.356 1.00 119.13 ? 157 TYR A CA 1 ATOM 1246 C C . TYR A 1 157 ? 32.635 -22.905 32.484 1.00 118.95 ? 157 TYR A C 1 ATOM 1247 O O . TYR A 1 157 ? 33.727 -23.478 32.420 1.00 117.65 ? 157 TYR A O 1 ATOM 1248 C CB . TYR A 1 157 ? 33.635 -20.847 31.409 1.00 116.45 ? 157 TYR A CB 1 ATOM 1249 C CG . TYR A 1 157 ? 33.356 -21.034 29.920 1.00 114.01 ? 157 TYR A CG 1 ATOM 1250 C CD1 . TYR A 1 157 ? 33.427 -22.291 29.320 1.00 112.35 ? 157 TYR A CD1 1 ATOM 1251 C CD2 . TYR A 1 157 ? 33.043 -19.943 29.108 1.00 112.00 ? 157 TYR A CD2 1 ATOM 1252 C CE1 . TYR A 1 157 ? 33.183 -22.455 27.966 1.00 110.12 ? 157 TYR A CE1 1 ATOM 1253 C CE2 . TYR A 1 157 ? 32.799 -20.099 27.755 1.00 108.66 ? 157 TYR A CE2 1 ATOM 1254 C CZ . TYR A 1 157 ? 32.871 -21.357 27.186 1.00 108.26 ? 157 TYR A CZ 1 ATOM 1255 O OH . TYR A 1 157 ? 32.631 -21.514 25.837 1.00 104.24 ? 157 TYR A OH 1 ATOM 1256 N N . PRO A 1 158 ? 31.483 -23.570 32.696 1.00 119.69 ? 158 PRO A N 1 ATOM 1257 C CA . PRO A 1 158 ? 31.503 -25.027 32.820 1.00 119.53 ? 158 PRO A CA 1 ATOM 1258 C C . PRO A 1 158 ? 31.758 -25.696 31.477 1.00 115.83 ? 158 PRO A C 1 ATOM 1259 O O . PRO A 1 158 ? 31.529 -25.086 30.430 1.00 113.63 ? 158 PRO A O 1 ATOM 1260 C CB . PRO A 1 158 ? 30.101 -25.359 33.342 1.00 121.92 ? 158 PRO A CB 1 ATOM 1261 C CG . PRO A 1 158 ? 29.243 -24.243 32.862 1.00 121.54 ? 158 PRO A CG 1 ATOM 1262 C CD . PRO A 1 158 ? 30.119 -23.022 32.823 1.00 120.85 ? 158 PRO A CD 1 ATOM 1263 N N . THR A 1 159 ? 32.233 -26.937 31.513 1.00 115.47 ? 159 THR A N 1 ATOM 1264 C CA . THR A 1 159 ? 32.576 -27.654 30.292 1.00 112.35 ? 159 THR A CA 1 ATOM 1265 C C . THR A 1 159 ? 31.341 -27.820 29.410 1.00 111.93 ? 159 THR A C 1 ATOM 1266 O O . THR A 1 159 ? 30.277 -28.216 29.888 1.00 113.11 ? 159 THR A O 1 ATOM 1267 C CB . THR A 1 159 ? 33.194 -29.036 30.592 1.00 112.68 ? 159 THR A CB 1 ATOM 1268 O OG1 . THR A 1 159 ? 34.323 -28.879 31.457 1.00 112.41 ? 159 THR A OG1 1 ATOM 1269 C CG2 . THR A 1 159 ? 33.646 -29.722 29.304 1.00 110.41 ? 159 THR A CG2 1 ATOM 1270 N N . ILE A 1 160 ? 31.501 -27.490 28.129 1.00 109.70 ? 160 ILE A N 1 ATOM 1271 C CA . ILE A 1 160 ? 30.448 -27.633 27.123 1.00 109.71 ? 160 ILE A CA 1 ATOM 1272 C C . ILE A 1 160 ? 30.532 -29.018 26.482 1.00 110.61 ? 160 ILE A C 1 ATOM 1273 O O . ILE A 1 160 ? 31.604 -29.442 26.061 1.00 109.27 ? 160 ILE A O 1 ATOM 1274 C CB . ILE A 1 160 ? 30.584 -26.551 26.020 1.00 106.34 ? 160 ILE A CB 1 ATOM 1275 C CG1 . ILE A 1 160 ? 30.277 -25.167 26.599 1.00 106.66 ? 160 ILE A CG1 1 ATOM 1276 C CG2 . ILE A 1 160 ? 29.659 -26.848 24.843 1.00 104.88 ? 160 ILE A CG2 1 ATOM 1277 C CD1 . ILE A 1 160 ? 30.670 -24.012 25.705 1.00 104.00 ? 160 ILE A CD1 1 ATOM 1278 N N . LYS A 1 161 ? 29.401 -29.718 26.418 1.00 112.94 ? 161 LYS A N 1 ATOM 1279 C CA . LYS A 1 161 ? 29.317 -31.003 25.726 1.00 114.28 ? 161 LYS A CA 1 ATOM 1280 C C . LYS A 1 161 ? 28.068 -31.022 24.858 1.00 115.14 ? 161 LYS A C 1 ATOM 1281 O O . LYS A 1 161 ? 27.012 -31.483 25.292 1.00 117.64 ? 161 LYS A O 1 ATOM 1282 C CB . LYS A 1 161 ? 29.266 -32.162 26.724 1.00 118.21 ? 161 LYS A CB 1 ATOM 1283 C CG . LYS A 1 161 ? 30.545 -32.382 27.516 1.00 120.24 ? 161 LYS A CG 1 ATOM 1284 C CD . LYS A 1 161 ? 30.337 -33.418 28.614 1.00 123.64 ? 161 LYS A CD 1 ATOM 1285 C CE . LYS A 1 161 ? 31.536 -33.505 29.547 1.00 125.40 ? 161 LYS A CE 1 ATOM 1286 N NZ . LYS A 1 161 ? 31.212 -34.219 30.814 1.00 128.66 ? 161 LYS A NZ 1 ATOM 1287 N N . ARG A 1 162 ? 28.192 -30.507 23.637 1.00 114.16 ? 162 ARG A N 1 ATOM 1288 C CA . ARG A 1 162 ? 27.073 -30.469 22.700 1.00 114.07 ? 162 ARG A CA 1 ATOM 1289 C C . ARG A 1 162 ? 27.299 -31.407 21.534 1.00 113.07 ? 162 ARG A C 1 ATOM 1290 O O . ARG A 1 162 ? 28.436 -31.716 21.178 1.00 112.73 ? 162 ARG A O 1 ATOM 1291 C CB . ARG A 1 162 ? 26.862 -29.056 22.158 1.00 112.60 ? 162 ARG A CB 1 ATOM 1292 C CG . ARG A 1 162 ? 26.413 -28.035 23.188 1.00 114.97 ? 162 ARG A CG 1 ATOM 1293 C CD . ARG A 1 162 ? 25.161 -28.460 23.942 1.00 117.85 ? 162 ARG A CD 1 ATOM 1294 N NE . ARG A 1 162 ? 24.292 -27.314 24.208 1.00 118.37 ? 162 ARG A NE 1 ATOM 1295 C CZ . ARG A 1 162 ? 23.316 -26.892 23.405 1.00 116.83 ? 162 ARG A CZ 1 ATOM 1296 N NH1 . ARG A 1 162 ? 23.040 -27.519 22.263 1.00 114.69 ? 162 ARG A NH1 1 ATOM 1297 N NH2 . ARG A 1 162 ? 22.600 -25.831 23.752 1.00 117.78 ? 162 ARG A NH2 1 ATOM 1298 N N . SER A 1 163 ? 26.197 -31.844 20.937 1.00 112.78 ? 163 SER A N 1 ATOM 1299 C CA . SER A 1 163 ? 26.238 -32.718 19.781 1.00 110.44 ? 163 SER A CA 1 ATOM 1300 C C . SER A 1 163 ? 25.114 -32.350 18.821 1.00 109.42 ? 163 SER A C 1 ATOM 1301 O O . SER A 1 163 ? 23.999 -32.059 19.249 1.00 108.88 ? 163 SER A O 1 ATOM 1302 C CB . SER A 1 163 ? 26.101 -34.174 20.224 1.00 112.03 ? 163 SER A CB 1 ATOM 1303 O OG . SER A 1 163 ? 26.187 -35.053 19.117 1.00 113.91 ? 163 SER A OG 1 ATOM 1304 N N . TYR A 1 164 ? 25.416 -32.332 17.526 1.00 108.25 ? 164 TYR A N 1 ATOM 1305 C CA . TYR A 1 164 ? 24.382 -32.176 16.511 1.00 109.21 ? 164 TYR A CA 1 ATOM 1306 C C . TYR A 1 164 ? 24.410 -33.344 15.538 1.00 110.90 ? 164 TYR A C 1 ATOM 1307 O O . TYR A 1 164 ? 25.472 -33.846 15.184 1.00 110.84 ? 164 TYR A O 1 ATOM 1308 C CB . TYR A 1 164 ? 24.527 -30.865 15.747 1.00 107.14 ? 164 TYR A CB 1 ATOM 1309 C CG . TYR A 1 164 ? 23.566 -30.787 14.585 1.00 107.73 ? 164 TYR A CG 1 ATOM 1310 C CD1 . TYR A 1 164 ? 22.222 -30.485 14.785 1.00 110.00 ? 164 TYR A CD1 1 ATOM 1311 C CD2 . TYR A 1 164 ? 23.990 -31.061 13.291 1.00 107.65 ? 164 TYR A CD2 1 ATOM 1312 C CE1 . TYR A 1 164 ? 21.333 -30.434 13.723 1.00 110.71 ? 164 TYR A CE1 1 ATOM 1313 C CE2 . TYR A 1 164 ? 23.112 -31.013 12.224 1.00 108.25 ? 164 TYR A CE2 1 ATOM 1314 C CZ . TYR A 1 164 ? 21.787 -30.699 12.442 1.00 110.20 ? 164 TYR A CZ 1 ATOM 1315 O OH . TYR A 1 164 ? 20.924 -30.653 11.374 1.00 111.09 ? 164 TYR A OH 1 ATOM 1316 N N . ASN A 1 165 ? 23.224 -33.747 15.099 1.00 114.91 ? 165 ASN A N 1 ATOM 1317 C CA . ASN A 1 165 ? 23.043 -34.902 14.242 1.00 119.02 ? 165 ASN A CA 1 ATOM 1318 C C . ASN A 1 165 ? 22.493 -34.471 12.890 1.00 117.52 ? 165 ASN A C 1 ATOM 1319 O O . ASN A 1 165 ? 21.482 -33.771 12.826 1.00 117.95 ? 165 ASN A O 1 ATOM 1320 C CB . ASN A 1 165 ? 22.063 -35.849 14.917 1.00 125.51 ? 165 ASN A CB 1 ATOM 1321 C CG . ASN A 1 165 ? 21.981 -37.193 14.236 1.00 131.11 ? 165 ASN A CG 1 ATOM 1322 O OD1 . ASN A 1 165 ? 21.375 -37.328 13.171 1.00 127.09 ? 165 ASN A OD1 1 ATOM 1323 N ND2 . ASN A 1 165 ? 22.586 -38.205 14.854 1.00 140.12 ? 165 ASN A ND2 1 ATOM 1324 N N . ASN A 1 166 ? 23.153 -34.888 11.813 1.00 114.75 ? 166 ASN A N 1 ATOM 1325 C CA . ASN A 1 166 ? 22.701 -34.548 10.471 1.00 113.32 ? 166 ASN A CA 1 ATOM 1326 C C . ASN A 1 166 ? 21.593 -35.492 10.021 1.00 114.19 ? 166 ASN A C 1 ATOM 1327 O O . ASN A 1 166 ? 21.852 -36.501 9.361 1.00 112.84 ? 166 ASN A O 1 ATOM 1328 C CB . ASN A 1 166 ? 23.865 -34.575 9.478 1.00 111.91 ? 166 ASN A CB 1 ATOM 1329 C CG . ASN A 1 166 ? 23.551 -33.825 8.199 1.00 111.97 ? 166 ASN A CG 1 ATOM 1330 O OD1 . ASN A 1 166 ? 22.686 -32.951 8.183 1.00 111.69 ? 166 ASN A OD1 1 ATOM 1331 N ND2 . ASN A 1 166 ? 24.264 -34.150 7.123 1.00 111.37 ? 166 ASN A ND2 1 ATOM 1332 N N . THR A 1 167 ? 20.359 -35.157 10.396 1.00 114.83 ? 167 THR A N 1 ATOM 1333 C CA . THR A 1 167 ? 19.192 -35.980 10.074 1.00 117.79 ? 167 THR A CA 1 ATOM 1334 C C . THR A 1 167 ? 18.730 -35.760 8.633 1.00 117.80 ? 167 THR A C 1 ATOM 1335 O O . THR A 1 167 ? 18.410 -36.720 7.924 1.00 118.14 ? 167 THR A O 1 ATOM 1336 C CB . THR A 1 167 ? 18.016 -35.697 11.033 1.00 118.88 ? 167 THR A CB 1 ATOM 1337 O OG1 . THR A 1 167 ? 17.694 -34.300 11.011 1.00 116.95 ? 167 THR A OG1 1 ATOM 1338 C CG2 . THR A 1 167 ? 18.377 -36.114 12.445 1.00 119.12 ? 167 THR A CG2 1 ATOM 1339 N N . ASN A 1 168 ? 18.678 -34.494 8.221 1.00 115.43 ? 168 ASN A N 1 ATOM 1340 C CA . ASN A 1 168 ? 18.375 -34.125 6.826 1.00 113.32 ? 168 ASN A CA 1 ATOM 1341 C C . ASN A 1 168 ? 19.271 -34.817 5.789 1.00 108.99 ? 168 ASN A C 1 ATOM 1342 O O . ASN A 1 168 ? 20.383 -35.238 6.095 1.00 107.59 ? 168 ASN A O 1 ATOM 1343 C CB . ASN A 1 168 ? 18.387 -32.597 6.627 1.00 111.79 ? 168 ASN A CB 1 ATOM 1344 C CG . ASN A 1 168 ? 19.413 -31.890 7.494 1.00 110.70 ? 168 ASN A CG 1 ATOM 1345 O OD1 . ASN A 1 168 ? 19.166 -30.790 7.985 1.00 109.56 ? 168 ASN A OD1 1 ATOM 1346 N ND2 . ASN A 1 168 ? 20.563 -32.521 7.696 1.00 109.76 ? 168 ASN A ND2 1 ATOM 1347 N N . GLN A 1 169 ? 18.759 -34.924 4.564 1.00 107.80 ? 169 GLN A N 1 ATOM 1348 C CA . GLN A 1 169 ? 19.376 -35.739 3.509 1.00 108.21 ? 169 GLN A CA 1 ATOM 1349 C C . GLN A 1 169 ? 20.668 -35.165 2.916 1.00 105.39 ? 169 GLN A C 1 ATOM 1350 O O . GLN A 1 169 ? 21.476 -35.917 2.373 1.00 103.16 ? 169 GLN A O 1 ATOM 1351 C CB . GLN A 1 169 ? 18.379 -35.972 2.360 1.00 110.78 ? 169 GLN A CB 1 ATOM 1352 C CG . GLN A 1 169 ? 17.768 -37.364 2.289 1.00 113.70 ? 169 GLN A CG 1 ATOM 1353 C CD . GLN A 1 169 ? 17.204 -37.667 0.904 1.00 116.05 ? 169 GLN A CD 1 ATOM 1354 O OE1 . GLN A 1 169 ? 17.867 -38.286 0.068 1.00 113.26 ? 169 GLN A OE1 1 ATOM 1355 N NE2 . GLN A 1 169 ? 15.986 -37.206 0.647 1.00 118.26 ? 169 GLN A NE2 1 ATOM 1356 N N . GLU A 1 170 ? 20.855 -33.850 3.024 1.00 103.63 ? 170 GLU A N 1 ATOM 1357 C CA . GLU A 1 170 ? 21.936 -33.139 2.335 1.00 101.55 ? 170 GLU A CA 1 ATOM 1358 C C . GLU A 1 170 ? 23.165 -32.923 3.214 1.00 100.18 ? 170 GLU A C 1 ATOM 1359 O O . GLU A 1 170 ? 23.031 -32.579 4.387 1.00 102.36 ? 170 GLU A O 1 ATOM 1360 C CB . GLU A 1 170 ? 21.444 -31.773 1.860 1.00 100.91 ? 170 GLU A CB 1 ATOM 1361 C CG . GLU A 1 170 ? 20.186 -31.812 1.006 1.00 103.40 ? 170 GLU A CG 1 ATOM 1362 C CD . GLU A 1 170 ? 18.903 -31.747 1.814 1.00 105.30 ? 170 GLU A CD 1 ATOM 1363 O OE1 . GLU A 1 170 ? 18.924 -32.110 3.009 1.00 109.02 ? 170 GLU A OE1 1 ATOM 1364 O OE2 . GLU A 1 170 ? 17.867 -31.333 1.255 1.00 104.29 ? 170 GLU A OE2 1 ATOM 1365 N N . ASP A 1 171 ? 24.354 -33.136 2.643 1.00 99.45 ? 171 ASP A N 1 ATOM 1366 C CA . ASP A 1 171 ? 25.628 -32.807 3.296 1.00 97.35 ? 171 ASP A CA 1 ATOM 1367 C C . ASP A 1 171 ? 25.531 -31.427 3.924 1.00 94.03 ? 171 ASP A C 1 ATOM 1368 O O . ASP A 1 171 ? 24.915 -30.527 3.356 1.00 92.17 ? 171 ASP A O 1 ATOM 1369 C CB . ASP A 1 171 ? 26.793 -32.793 2.283 1.00 99.88 ? 171 ASP A CB 1 ATOM 1370 C CG . ASP A 1 171 ? 27.272 -34.193 1.879 1.00 103.26 ? 171 ASP A CG 1 ATOM 1371 O OD1 . ASP A 1 171 ? 26.955 -35.183 2.569 1.00 108.38 ? 171 ASP A OD1 1 ATOM 1372 O OD2 . ASP A 1 171 ? 27.993 -34.295 0.862 1.00 103.67 ? 171 ASP A OD2 1 ATOM 1373 N N . LEU A 1 172 ? 26.153 -31.258 5.085 1.00 93.85 ? 172 LEU A N 1 ATOM 1374 C CA . LEU A 1 172 ? 26.049 -30.011 5.833 1.00 93.73 ? 172 LEU A CA 1 ATOM 1375 C C . LEU A 1 172 ? 27.420 -29.360 6.021 1.00 91.63 ? 172 LEU A C 1 ATOM 1376 O O . LEU A 1 172 ? 28.375 -30.017 6.441 1.00 91.49 ? 172 LEU A O 1 ATOM 1377 C CB . LEU A 1 172 ? 25.400 -30.283 7.190 1.00 95.44 ? 172 LEU A CB 1 ATOM 1378 C CG . LEU A 1 172 ? 24.824 -29.075 7.938 1.00 96.58 ? 172 LEU A CG 1 ATOM 1379 C CD1 . LEU A 1 172 ? 23.519 -28.603 7.314 1.00 97.19 ? 172 LEU A CD1 1 ATOM 1380 C CD2 . LEU A 1 172 ? 24.610 -29.422 9.402 1.00 98.28 ? 172 LEU A CD2 1 ATOM 1381 N N . LEU A 1 173 ? 27.509 -28.072 5.698 1.00 89.21 ? 173 LEU A N 1 ATOM 1382 C CA . LEU A 1 173 ? 28.716 -27.297 5.950 1.00 87.88 ? 173 LEU A CA 1 ATOM 1383 C C . LEU A 1 173 ? 28.635 -26.671 7.332 1.00 87.93 ? 173 LEU A C 1 ATOM 1384 O O . LEU A 1 173 ? 27.873 -25.733 7.538 1.00 88.02 ? 173 LEU A O 1 ATOM 1385 C CB . LEU A 1 173 ? 28.892 -26.196 4.905 1.00 87.30 ? 173 LEU A CB 1 ATOM 1386 C CG . LEU A 1 173 ? 30.024 -25.193 5.171 1.00 86.49 ? 173 LEU A CG 1 ATOM 1387 C CD1 . LEU A 1 173 ? 31.349 -25.909 5.378 1.00 86.38 ? 173 LEU A CD1 1 ATOM 1388 C CD2 . LEU A 1 173 ? 30.139 -24.187 4.038 1.00 85.98 ? 173 LEU A CD2 1 ATOM 1389 N N . VAL A 1 174 ? 29.436 -27.181 8.264 1.00 88.04 ? 174 VAL A N 1 ATOM 1390 C CA . VAL A 1 174 ? 29.479 -26.674 9.634 1.00 86.85 ? 174 VAL A CA 1 ATOM 1391 C C . VAL A 1 174 ? 30.724 -25.804 9.843 1.00 84.88 ? 174 VAL A C 1 ATOM 1392 O O . VAL A 1 174 ? 31.835 -26.203 9.485 1.00 83.30 ? 174 VAL A O 1 ATOM 1393 C CB . VAL A 1 174 ? 29.484 -27.831 10.653 1.00 88.01 ? 174 VAL A CB 1 ATOM 1394 C CG1 . VAL A 1 174 ? 29.395 -27.296 12.073 1.00 89.25 ? 174 VAL A CG1 1 ATOM 1395 C CG2 . VAL A 1 174 ? 28.335 -28.787 10.372 1.00 89.29 ? 174 VAL A CG2 1 ATOM 1396 N N . LEU A 1 175 ? 30.520 -24.625 10.429 1.00 84.27 ? 175 LEU A N 1 ATOM 1397 C CA . LEU A 1 175 ? 31.587 -23.666 10.705 1.00 84.46 ? 175 LEU A CA 1 ATOM 1398 C C . LEU A 1 175 ? 31.663 -23.357 12.192 1.00 85.15 ? 175 LEU A C 1 ATOM 1399 O O . LEU A 1 175 ? 30.642 -23.066 12.817 1.00 87.63 ? 175 LEU A O 1 ATOM 1400 C CB . LEU A 1 175 ? 31.304 -22.360 9.974 1.00 84.49 ? 175 LEU A CB 1 ATOM 1401 C CG . LEU A 1 175 ? 31.353 -22.400 8.450 1.00 84.46 ? 175 LEU A CG 1 ATOM 1402 C CD1 . LEU A 1 175 ? 30.310 -21.452 7.880 1.00 85.39 ? 175 LEU A CD1 1 ATOM 1403 C CD2 . LEU A 1 175 ? 32.746 -22.047 7.955 1.00 82.61 ? 175 LEU A CD2 1 ATOM 1404 N N . TRP A 1 176 ? 32.868 -23.407 12.752 1.00 83.46 ? 176 TRP A N 1 ATOM 1405 C CA . TRP A 1 176 ? 33.096 -22.978 14.130 1.00 84.14 ? 176 TRP A CA 1 ATOM 1406 C C . TRP A 1 176 ? 34.414 -22.213 14.216 1.00 83.58 ? 176 TRP A C 1 ATOM 1407 O O . TRP A 1 176 ? 35.024 -21.915 13.194 1.00 82.55 ? 176 TRP A O 1 ATOM 1408 C CB . TRP A 1 176 ? 33.066 -24.177 15.086 1.00 85.64 ? 176 TRP A CB 1 ATOM 1409 C CG . TRP A 1 176 ? 34.175 -25.154 14.897 1.00 85.83 ? 176 TRP A CG 1 ATOM 1410 C CD1 . TRP A 1 176 ? 35.322 -25.240 15.628 1.00 86.71 ? 176 TRP A CD1 1 ATOM 1411 C CD2 . TRP A 1 176 ? 34.243 -26.196 13.920 1.00 85.49 ? 176 TRP A CD2 1 ATOM 1412 N NE1 . TRP A 1 176 ? 36.105 -26.269 15.165 1.00 86.33 ? 176 TRP A NE1 1 ATOM 1413 C CE2 . TRP A 1 176 ? 35.465 -26.874 14.117 1.00 85.83 ? 176 TRP A CE2 1 ATOM 1414 C CE3 . TRP A 1 176 ? 33.387 -26.626 12.900 1.00 85.51 ? 176 TRP A CE3 1 ATOM 1415 C CZ2 . TRP A 1 176 ? 35.858 -27.952 13.325 1.00 86.07 ? 176 TRP A CZ2 1 ATOM 1416 C CZ3 . TRP A 1 176 ? 33.774 -27.702 12.116 1.00 85.68 ? 176 TRP A CZ3 1 ATOM 1417 C CH2 . TRP A 1 176 ? 35.000 -28.351 12.332 1.00 86.17 ? 176 TRP A CH2 1 ATOM 1418 N N . GLY A 1 177 ? 34.843 -21.869 15.425 1.00 85.84 ? 177 GLY A N 1 ATOM 1419 C CA . GLY A 1 177 ? 36.100 -21.141 15.589 1.00 85.98 ? 177 GLY A CA 1 ATOM 1420 C C . GLY A 1 177 ? 36.644 -21.136 17.000 1.00 87.28 ? 177 GLY A C 1 ATOM 1421 O O . GLY A 1 177 ? 36.025 -21.666 17.921 1.00 88.44 ? 177 GLY A O 1 ATOM 1422 N N . ILE A 1 178 ? 37.813 -20.528 17.159 1.00 87.03 ? 178 ILE A N 1 ATOM 1423 C CA . ILE A 1 178 ? 38.464 -20.436 18.452 1.00 89.32 ? 178 ILE A CA 1 ATOM 1424 C C . ILE A 1 178 ? 39.044 -19.037 18.629 1.00 90.39 ? 178 ILE A C 1 ATOM 1425 O O . ILE A 1 178 ? 39.580 -18.461 17.687 1.00 89.23 ? 178 ILE A O 1 ATOM 1426 C CB . ILE A 1 178 ? 39.563 -21.513 18.612 1.00 91.07 ? 178 ILE A CB 1 ATOM 1427 C CG1 . ILE A 1 178 ? 40.125 -21.501 20.037 1.00 94.14 ? 178 ILE A CG1 1 ATOM 1428 C CG2 . ILE A 1 178 ? 40.686 -21.319 17.603 1.00 90.19 ? 178 ILE A CG2 1 ATOM 1429 C CD1 . ILE A 1 178 ? 40.985 -22.699 20.376 1.00 95.86 ? 178 ILE A CD1 1 ATOM 1430 N N . HIS A 1 179 ? 38.925 -18.497 19.839 1.00 92.12 ? 179 HIS A N 1 ATOM 1431 C CA . HIS A 1 179 ? 39.432 -17.164 20.142 1.00 92.60 ? 179 HIS A CA 1 ATOM 1432 C C . HIS A 1 179 ? 40.804 -17.260 20.793 1.00 93.69 ? 179 HIS A C 1 ATOM 1433 O O . HIS A 1 179 ? 40.983 -17.986 21.772 1.00 95.17 ? 179 HIS A O 1 ATOM 1434 C CB . HIS A 1 179 ? 38.462 -16.420 21.063 1.00 93.28 ? 179 HIS A CB 1 ATOM 1435 C CG . HIS A 1 179 ? 38.947 -15.071 21.495 1.00 92.87 ? 179 HIS A CG 1 ATOM 1436 N ND1 . HIS A 1 179 ? 39.064 -14.713 22.820 1.00 94.79 ? 179 HIS A ND1 1 ATOM 1437 C CD2 . HIS A 1 179 ? 39.344 -13.993 20.779 1.00 92.28 ? 179 HIS A CD2 1 ATOM 1438 C CE1 . HIS A 1 179 ? 39.508 -13.472 22.903 1.00 94.96 ? 179 HIS A CE1 1 ATOM 1439 N NE2 . HIS A 1 179 ? 39.686 -13.012 21.678 1.00 93.69 ? 179 HIS A NE2 1 ATOM 1440 N N . HIS A 1 180 ? 41.765 -16.533 20.230 1.00 93.15 ? 180 HIS A N 1 ATOM 1441 C CA . HIS A 1 180 ? 43.099 -16.419 20.797 1.00 94.68 ? 180 HIS A CA 1 ATOM 1442 C C . HIS A 1 180 ? 43.175 -15.076 21.508 1.00 96.91 ? 180 HIS A C 1 ATOM 1443 O O . HIS A 1 180 ? 43.241 -14.041 20.853 1.00 97.25 ? 180 HIS A O 1 ATOM 1444 C CB . HIS A 1 180 ? 44.161 -16.479 19.699 1.00 93.67 ? 180 HIS A CB 1 ATOM 1445 C CG . HIS A 1 180 ? 44.108 -17.726 18.875 1.00 93.33 ? 180 HIS A CG 1 ATOM 1446 N ND1 . HIS A 1 180 ? 44.059 -18.982 19.435 1.00 95.12 ? 180 HIS A ND1 1 ATOM 1447 C CD2 . HIS A 1 180 ? 44.101 -17.912 17.535 1.00 92.41 ? 180 HIS A CD2 1 ATOM 1448 C CE1 . HIS A 1 180 ? 44.020 -19.891 18.478 1.00 93.62 ? 180 HIS A CE1 1 ATOM 1449 N NE2 . HIS A 1 180 ? 44.046 -19.267 17.315 1.00 92.91 ? 180 HIS A NE2 1 ATOM 1450 N N . PRO A 1 181 ? 43.152 -15.079 22.849 1.00 98.94 ? 181 PRO A N 1 ATOM 1451 C CA . PRO A 1 181 ? 43.174 -13.807 23.559 1.00 100.89 ? 181 PRO A CA 1 ATOM 1452 C C . PRO A 1 181 ? 44.570 -13.195 23.622 1.00 101.77 ? 181 PRO A C 1 ATOM 1453 O O . PRO A 1 181 ? 45.563 -13.867 23.339 1.00 99.76 ? 181 PRO A O 1 ATOM 1454 C CB . PRO A 1 181 ? 42.680 -14.178 24.959 1.00 103.40 ? 181 PRO A CB 1 ATOM 1455 C CG . PRO A 1 181 ? 43.041 -15.611 25.132 1.00 103.23 ? 181 PRO A CG 1 ATOM 1456 C CD . PRO A 1 181 ? 43.191 -16.229 23.768 1.00 101.08 ? 181 PRO A CD 1 ATOM 1457 N N . ASN A 1 182 ? 44.625 -11.922 23.995 1.00 104.08 ? 182 ASN A N 1 ATOM 1458 C CA . ASN A 1 182 ? 45.868 -11.162 24.010 1.00 105.45 ? 182 ASN A CA 1 ATOM 1459 C C . ASN A 1 182 ? 46.830 -11.597 25.119 1.00 107.34 ? 182 ASN A C 1 ATOM 1460 O O . ASN A 1 182 ? 48.031 -11.744 24.876 1.00 107.34 ? 182 ASN A O 1 ATOM 1461 C CB . ASN A 1 182 ? 45.549 -9.667 24.132 1.00 106.65 ? 182 ASN A CB 1 ATOM 1462 C CG . ASN A 1 182 ? 46.792 -8.799 24.157 1.00 108.05 ? 182 ASN A CG 1 ATOM 1463 O OD1 . ASN A 1 182 ? 46.957 -7.968 25.050 1.00 110.70 ? 182 ASN A OD1 1 ATOM 1464 N ND2 . ASN A 1 182 ? 47.675 -8.987 23.183 1.00 107.19 ? 182 ASN A ND2 1 ATOM 1465 N N . ASP A 1 183 ? 46.298 -11.803 26.326 1.00 109.28 ? 183 ASP A N 1 ATOM 1466 C CA . ASP A 1 183 ? 47.113 -12.168 27.496 1.00 111.35 ? 183 ASP A CA 1 ATOM 1467 C C . ASP A 1 183 ? 46.356 -13.054 28.496 1.00 111.07 ? 183 ASP A C 1 ATOM 1468 O O . ASP A 1 183 ? 45.165 -13.316 28.330 1.00 109.42 ? 183 ASP A O 1 ATOM 1469 C CB . ASP A 1 183 ? 47.650 -10.901 28.191 1.00 113.75 ? 183 ASP A CB 1 ATOM 1470 C CG . ASP A 1 183 ? 46.550 -9.907 28.565 1.00 114.98 ? 183 ASP A CG 1 ATOM 1471 O OD1 . ASP A 1 183 ? 45.417 -10.327 28.884 1.00 115.48 ? 183 ASP A OD1 1 ATOM 1472 O OD2 . ASP A 1 183 ? 46.829 -8.690 28.557 1.00 116.30 ? 183 ASP A OD2 1 ATOM 1473 N N . ALA A 1 184 ? 47.061 -13.506 29.532 1.00 112.44 ? 184 ALA A N 1 ATOM 1474 C CA . ALA A 1 184 ? 46.476 -14.370 30.565 1.00 113.08 ? 184 ALA A CA 1 ATOM 1475 C C . ALA A 1 184 ? 45.326 -13.708 31.332 1.00 114.15 ? 184 ALA A C 1 ATOM 1476 O O . ALA A 1 184 ? 44.401 -14.390 31.776 1.00 113.80 ? 184 ALA A O 1 ATOM 1477 C CB . ALA A 1 184 ? 47.555 -14.833 31.536 1.00 113.86 ? 184 ALA A CB 1 ATOM 1478 N N . ALA A 1 185 ? 45.389 -12.386 31.486 1.00 115.53 ? 185 ALA A N 1 ATOM 1479 C CA . ALA A 1 185 ? 44.350 -11.633 32.194 1.00 117.34 ? 185 ALA A CA 1 ATOM 1480 C C . ALA A 1 185 ? 43.042 -11.620 31.405 1.00 115.51 ? 185 ALA A C 1 ATOM 1481 O O . ALA A 1 185 ? 41.964 -11.811 31.969 1.00 117.34 ? 185 ALA A O 1 ATOM 1482 C CB . ALA A 1 185 ? 44.817 -10.212 32.465 1.00 118.86 ? 185 ALA A CB 1 ATOM 1483 N N . GLU A 1 186 ? 43.149 -11.397 30.100 1.00 112.65 ? 186 GLU A N 1 ATOM 1484 C CA . GLU A 1 186 ? 41.993 -11.427 29.202 1.00 109.84 ? 186 GLU A CA 1 ATOM 1485 C C . GLU A 1 186 ? 41.339 -12.814 29.167 1.00 107.87 ? 186 GLU A C 1 ATOM 1486 O O . GLU A 1 186 ? 40.114 -12.927 29.140 1.00 106.16 ? 186 GLU A O 1 ATOM 1487 C CB . GLU A 1 186 ? 42.428 -11.005 27.799 1.00 107.96 ? 186 GLU A CB 1 ATOM 1488 C CG . GLU A 1 186 ? 41.309 -10.862 26.779 1.00 106.55 ? 186 GLU A CG 1 ATOM 1489 C CD . GLU A 1 186 ? 41.782 -10.165 25.515 1.00 105.17 ? 186 GLU A CD 1 ATOM 1490 O OE1 . GLU A 1 186 ? 42.126 -8.964 25.592 1.00 105.19 ? 186 GLU A OE1 1 ATOM 1491 O OE2 . GLU A 1 186 ? 41.831 -10.820 24.449 1.00 102.39 ? 186 GLU A OE2 1 ATOM 1492 N N . GLN A 1 187 ? 42.165 -13.859 29.176 1.00 106.97 ? 187 GLN A N 1 ATOM 1493 C CA . GLN A 1 187 ? 41.685 -15.246 29.200 1.00 106.63 ? 187 GLN A CA 1 ATOM 1494 C C . GLN A 1 187 ? 40.750 -15.502 30.389 1.00 110.25 ? 187 GLN A C 1 ATOM 1495 O O . GLN A 1 187 ? 39.626 -15.977 30.211 1.00 109.25 ? 187 GLN A O 1 ATOM 1496 C CB . GLN A 1 187 ? 42.880 -16.213 29.232 1.00 105.79 ? 187 GLN A CB 1 ATOM 1497 C CG . GLN A 1 187 ? 42.540 -17.685 29.432 1.00 105.22 ? 187 GLN A CG 1 ATOM 1498 C CD . GLN A 1 187 ? 41.724 -18.278 28.298 1.00 102.22 ? 187 GLN A CD 1 ATOM 1499 O OE1 . GLN A 1 187 ? 41.990 -18.031 27.121 1.00 98.74 ? 187 GLN A OE1 1 ATOM 1500 N NE2 . GLN A 1 187 ? 40.735 -19.088 28.651 1.00 102.63 ? 187 GLN A NE2 1 ATOM 1501 N N . THR A 1 188 ? 41.219 -15.179 31.593 1.00 114.10 ? 188 THR A N 1 ATOM 1502 C CA . THR A 1 188 ? 40.418 -15.360 32.806 1.00 117.23 ? 188 THR A CA 1 ATOM 1503 C C . THR A 1 188 ? 39.233 -14.388 32.849 1.00 117.82 ? 188 THR A C 1 ATOM 1504 O O . THR A 1 188 ? 38.154 -14.743 33.319 1.00 119.69 ? 188 THR A O 1 ATOM 1505 C CB . THR A 1 188 ? 41.265 -15.196 34.090 1.00 120.61 ? 188 THR A CB 1 ATOM 1506 O OG1 . THR A 1 188 ? 41.815 -13.875 34.149 1.00 121.02 ? 188 THR A OG1 1 ATOM 1507 C CG2 . THR A 1 188 ? 42.397 -16.222 34.129 1.00 120.71 ? 188 THR A CG2 1 ATOM 1508 N N . LYS A 1 189 ? 39.435 -13.171 32.351 1.00 116.68 ? 189 LYS A N 1 ATOM 1509 C CA . LYS A 1 189 ? 38.372 -12.168 32.304 1.00 117.79 ? 189 LYS A CA 1 ATOM 1510 C C . LYS A 1 189 ? 37.164 -12.637 31.479 1.00 116.09 ? 189 LYS A C 1 ATOM 1511 O O . LYS A 1 189 ? 36.022 -12.366 31.851 1.00 116.08 ? 189 LYS A O 1 ATOM 1512 C CB . LYS A 1 189 ? 38.921 -10.854 31.741 1.00 118.71 ? 189 LYS A CB 1 ATOM 1513 C CG . LYS A 1 189 ? 37.938 -9.692 31.729 1.00 121.65 ? 189 LYS A CG 1 ATOM 1514 C CD . LYS A 1 189 ? 38.472 -8.539 30.889 1.00 122.63 ? 189 LYS A CD 1 ATOM 1515 C CE . LYS A 1 189 ? 37.396 -7.510 30.572 1.00 124.11 ? 189 LYS A CE 1 ATOM 1516 N NZ . LYS A 1 189 ? 37.622 -6.885 29.239 1.00 122.25 ? 189 LYS A NZ 1 ATOM 1517 N N . LEU A 1 190 ? 37.420 -13.335 30.370 1.00 113.13 ? 190 LEU A N 1 ATOM 1518 C CA . LEU A 1 190 ? 36.354 -13.811 29.477 1.00 111.99 ? 190 LEU A CA 1 ATOM 1519 C C . LEU A 1 190 ? 35.881 -15.232 29.791 1.00 112.22 ? 190 LEU A C 1 ATOM 1520 O O . LEU A 1 190 ? 34.686 -15.526 29.696 1.00 111.18 ? 190 LEU A O 1 ATOM 1521 C CB . LEU A 1 190 ? 36.809 -13.767 28.010 1.00 108.79 ? 190 LEU A CB 1 ATOM 1522 C CG . LEU A 1 190 ? 37.316 -12.445 27.423 1.00 108.40 ? 190 LEU A CG 1 ATOM 1523 C CD1 . LEU A 1 190 ? 37.263 -12.492 25.906 1.00 105.53 ? 190 LEU A CD1 1 ATOM 1524 C CD2 . LEU A 1 190 ? 36.528 -11.252 27.938 1.00 110.76 ? 190 LEU A CD2 1 ATOM 1525 N N . TYR A 1 191 ? 36.817 -16.109 30.150 1.00 112.98 ? 191 TYR A N 1 ATOM 1526 C CA . TYR A 1 191 ? 36.539 -17.547 30.229 1.00 112.90 ? 191 TYR A CA 1 ATOM 1527 C C . TYR A 1 191 ? 36.858 -18.215 31.571 1.00 117.30 ? 191 TYR A C 1 ATOM 1528 O O . TYR A 1 191 ? 36.720 -19.435 31.683 1.00 118.56 ? 191 TYR A O 1 ATOM 1529 C CB . TYR A 1 191 ? 37.318 -18.274 29.131 1.00 109.39 ? 191 TYR A CB 1 ATOM 1530 C CG . TYR A 1 191 ? 37.211 -17.625 27.769 1.00 105.24 ? 191 TYR A CG 1 ATOM 1531 C CD1 . TYR A 1 191 ? 35.995 -17.586 27.093 1.00 104.14 ? 191 TYR A CD1 1 ATOM 1532 C CD2 . TYR A 1 191 ? 38.319 -17.041 27.164 1.00 102.58 ? 191 TYR A CD2 1 ATOM 1533 C CE1 . TYR A 1 191 ? 35.887 -16.991 25.846 1.00 101.10 ? 191 TYR A CE1 1 ATOM 1534 C CE2 . TYR A 1 191 ? 38.220 -16.443 25.922 1.00 100.07 ? 191 TYR A CE2 1 ATOM 1535 C CZ . TYR A 1 191 ? 36.999 -16.422 25.268 1.00 98.81 ? 191 TYR A CZ 1 ATOM 1536 O OH . TYR A 1 191 ? 36.882 -15.830 24.039 1.00 96.30 ? 191 TYR A OH 1 ATOM 1537 N N . ARG A 1 192 ? 37.274 -17.443 32.577 1.00 120.47 ? 192 ARG A N 1 ATOM 1538 C CA . ARG A 1 192 ? 37.693 -17.992 33.880 1.00 124.28 ? 192 ARG A CA 1 ATOM 1539 C C . ARG A 1 192 ? 38.915 -18.910 33.778 1.00 121.83 ? 192 ARG A C 1 ATOM 1540 O O . ARG A 1 192 ? 40.003 -18.561 34.239 1.00 121.58 ? 192 ARG A O 1 ATOM 1541 C CB . ARG A 1 192 ? 36.536 -18.741 34.565 1.00 129.18 ? 192 ARG A CB 1 ATOM 1542 C CG . ARG A 1 192 ? 35.804 -17.956 35.642 1.00 134.70 ? 192 ARG A CG 1 ATOM 1543 C CD . ARG A 1 192 ? 36.331 -18.242 37.045 1.00 139.94 ? 192 ARG A CD 1 ATOM 1544 N NE . ARG A 1 192 ? 37.191 -17.184 37.575 1.00 145.78 ? 192 ARG A NE 1 ATOM 1545 C CZ . ARG A 1 192 ? 36.783 -15.957 37.909 1.00 149.90 ? 192 ARG A CZ 1 ATOM 1546 N NH1 . ARG A 1 192 ? 35.516 -15.587 37.739 1.00 151.80 ? 192 ARG A NH1 1 ATOM 1547 N NH2 . ARG A 1 192 ? 37.656 -15.081 38.400 1.00 150.87 ? 192 ARG A NH2 1 ATOM 1548 N N . ASN A 1 193 ? 38.714 -20.080 33.172 1.00 119.18 ? 193 ASN A N 1 ATOM 1549 C CA . ASN A 1 193 ? 39.733 -21.125 33.092 1.00 117.86 ? 193 ASN A CA 1 ATOM 1550 C C . ASN A 1 193 ? 40.988 -20.646 32.364 1.00 115.80 ? 193 ASN A C 1 ATOM 1551 O O . ASN A 1 193 ? 40.887 -20.046 31.297 1.00 113.03 ? 193 ASN A O 1 ATOM 1552 C CB . ASN A 1 193 ? 39.161 -22.354 32.380 1.00 116.16 ? 193 ASN A CB 1 ATOM 1553 C CG . ASN A 1 193 ? 37.863 -22.843 33.008 1.00 118.34 ? 193 ASN A CG 1 ATOM 1554 O OD1 . ASN A 1 193 ? 37.734 -22.890 34.234 1.00 121.66 ? 193 ASN A OD1 1 ATOM 1555 N ND2 . ASN A 1 193 ? 36.892 -23.200 32.173 1.00 115.92 ? 193 ASN A ND2 1 ATOM 1556 N N . PRO A 1 194 ? 42.177 -20.893 32.945 1.00 117.61 ? 194 PRO A N 1 ATOM 1557 C CA . PRO A 1 194 ? 43.415 -20.446 32.303 1.00 116.32 ? 194 PRO A CA 1 ATOM 1558 C C . PRO A 1 194 ? 43.843 -21.329 31.126 1.00 113.85 ? 194 PRO A C 1 ATOM 1559 O O . PRO A 1 194 ? 44.274 -20.806 30.099 1.00 110.93 ? 194 PRO A O 1 ATOM 1560 C CB . PRO A 1 194 ? 44.440 -20.502 33.441 1.00 118.89 ? 194 PRO A CB 1 ATOM 1561 C CG . PRO A 1 194 ? 43.929 -21.554 34.361 1.00 120.78 ? 194 PRO A CG 1 ATOM 1562 C CD . PRO A 1 194 ? 42.430 -21.555 34.239 1.00 120.42 ? 194 PRO A CD 1 ATOM 1563 N N . THR A 1 195 ? 43.724 -22.649 31.280 1.00 114.74 ? 195 THR A N 1 ATOM 1564 C CA . THR A 1 195 ? 44.074 -23.604 30.224 1.00 112.90 ? 195 THR A CA 1 ATOM 1565 C C . THR A 1 195 ? 42.804 -24.221 29.644 1.00 111.22 ? 195 THR A C 1 ATOM 1566 O O . THR A 1 195 ? 42.062 -24.898 30.354 1.00 112.32 ? 195 THR A O 1 ATOM 1567 C CB . THR A 1 195 ? 44.968 -24.741 30.763 1.00 114.55 ? 195 THR A CB 1 ATOM 1568 O OG1 . THR A 1 195 ? 46.094 -24.189 31.455 1.00 115.23 ? 195 THR A OG1 1 ATOM 1569 C CG2 . THR A 1 195 ? 45.464 -25.631 29.621 1.00 113.32 ? 195 THR A CG2 1 ATOM 1570 N N . THR A 1 196 ? 42.561 -23.993 28.355 1.00 108.48 ? 196 THR A N 1 ATOM 1571 C CA . THR A 1 196 ? 41.316 -24.427 27.719 1.00 106.57 ? 196 THR A CA 1 ATOM 1572 C C . THR A 1 196 ? 41.558 -25.158 26.405 1.00 104.33 ? 196 THR A C 1 ATOM 1573 O O . THR A 1 196 ? 42.687 -25.253 25.923 1.00 101.50 ? 196 THR A O 1 ATOM 1574 C CB . THR A 1 196 ? 40.388 -23.230 27.445 1.00 105.24 ? 196 THR A CB 1 ATOM 1575 O OG1 . THR A 1 196 ? 41.070 -22.287 26.613 1.00 102.73 ? 196 THR A OG1 1 ATOM 1576 C CG2 . THR A 1 196 ? 39.978 -22.560 28.745 1.00 107.51 ? 196 THR A CG2 1 ATOM 1577 N N . TYR A 1 197 ? 40.476 -25.676 25.837 1.00 104.30 ? 197 TYR A N 1 ATOM 1578 C CA . TYR A 1 197 ? 40.537 -26.413 24.592 1.00 103.25 ? 197 TYR A CA 1 ATOM 1579 C C . TYR A 1 197 ? 39.171 -26.457 23.938 1.00 104.27 ? 197 TYR A C 1 ATOM 1580 O O . TYR A 1 197 ? 38.161 -26.118 24.556 1.00 105.40 ? 197 TYR A O 1 ATOM 1581 C CB . TYR A 1 197 ? 41.003 -27.847 24.854 1.00 104.29 ? 197 TYR A CB 1 ATOM 1582 C CG . TYR A 1 197 ? 40.037 -28.645 25.704 1.00 105.62 ? 197 TYR A CG 1 ATOM 1583 C CD1 . TYR A 1 197 ? 39.993 -28.477 27.088 1.00 108.57 ? 197 TYR A CD1 1 ATOM 1584 C CD2 . TYR A 1 197 ? 39.157 -29.556 25.125 1.00 104.75 ? 197 TYR A CD2 1 ATOM 1585 C CE1 . TYR A 1 197 ? 39.105 -29.198 27.871 1.00 110.19 ? 197 TYR A CE1 1 ATOM 1586 C CE2 . TYR A 1 197 ? 38.267 -30.284 25.897 1.00 107.09 ? 197 TYR A CE2 1 ATOM 1587 C CZ . TYR A 1 197 ? 38.244 -30.100 27.271 1.00 110.27 ? 197 TYR A CZ 1 ATOM 1588 O OH . TYR A 1 197 ? 37.358 -30.820 28.039 1.00 112.23 ? 197 TYR A OH 1 ATOM 1589 N N . ILE A 1 198 ? 39.160 -26.867 22.674 1.00 103.68 ? 198 ILE A N 1 ATOM 1590 C CA . ILE A 1 198 ? 37.938 -27.225 21.972 1.00 103.65 ? 198 ILE A CA 1 ATOM 1591 C C . ILE A 1 198 ? 38.230 -28.524 21.242 1.00 103.15 ? 198 ILE A C 1 ATOM 1592 O O . ILE A 1 198 ? 39.132 -28.573 20.407 1.00 103.47 ? 198 ILE A O 1 ATOM 1593 C CB . ILE A 1 198 ? 37.526 -26.164 20.932 1.00 103.34 ? 198 ILE A CB 1 ATOM 1594 C CG1 . ILE A 1 198 ? 37.386 -24.782 21.573 1.00 103.39 ? 198 ILE A CG1 1 ATOM 1595 C CG2 . ILE A 1 198 ? 36.217 -26.558 20.258 1.00 103.72 ? 198 ILE A CG2 1 ATOM 1596 C CD1 . ILE A 1 198 ? 37.543 -23.657 20.576 1.00 101.80 ? 198 ILE A CD1 1 ATOM 1597 N N . SER A 1 199 ? 37.488 -29.576 21.564 1.00 103.38 ? 199 SER A N 1 ATOM 1598 C CA . SER A 1 199 ? 37.639 -30.845 20.873 1.00 103.49 ? 199 SER A CA 1 ATOM 1599 C C . SER A 1 199 ? 36.436 -31.068 19.969 1.00 102.01 ? 199 SER A C 1 ATOM 1600 O O . SER A 1 199 ? 35.295 -30.909 20.394 1.00 102.39 ? 199 SER A O 1 ATOM 1601 C CB . SER A 1 199 ? 37.793 -31.993 21.868 1.00 106.80 ? 199 SER A CB 1 ATOM 1602 O OG . SER A 1 199 ? 36.592 -32.223 22.575 1.00 109.81 ? 199 SER A OG 1 ATOM 1603 N N . VAL A 1 200 ? 36.702 -31.423 18.717 1.00 100.81 ? 200 VAL A N 1 ATOM 1604 C CA . VAL A 1 200 ? 35.655 -31.637 17.730 1.00 99.90 ? 200 VAL A CA 1 ATOM 1605 C C . VAL A 1 200 ? 35.818 -33.029 17.146 1.00 100.42 ? 200 VAL A C 1 ATOM 1606 O O . VAL A 1 200 ? 36.926 -33.430 16.786 1.00 100.92 ? 200 VAL A O 1 ATOM 1607 C CB . VAL A 1 200 ? 35.733 -30.600 16.595 1.00 98.89 ? 200 VAL A CB 1 ATOM 1608 C CG1 . VAL A 1 200 ? 34.456 -30.617 15.764 1.00 98.78 ? 200 VAL A CG1 1 ATOM 1609 C CG2 . VAL A 1 200 ? 35.987 -29.210 17.163 1.00 98.88 ? 200 VAL A CG2 1 ATOM 1610 N N . GLY A 1 201 ? 34.713 -33.761 17.057 1.00 101.77 ? 201 GLY A N 1 ATOM 1611 C CA . GLY A 1 201 ? 34.724 -35.112 16.515 1.00 102.89 ? 201 GLY A CA 1 ATOM 1612 C C . GLY A 1 201 ? 33.561 -35.360 15.578 1.00 102.81 ? 201 GLY A C 1 ATOM 1613 O O . GLY A 1 201 ? 32.450 -34.904 15.827 1.00 103.07 ? 201 GLY A O 1 ATOM 1614 N N . THR A 1 202 ? 33.835 -36.059 14.482 1.00 103.86 ? 202 THR A N 1 ATOM 1615 C CA . THR A 1 202 ? 32.795 -36.596 13.606 1.00 105.42 ? 202 THR A CA 1 ATOM 1616 C C . THR A 1 202 ? 33.164 -38.048 13.320 1.00 109.37 ? 202 THR A C 1 ATOM 1617 O O . THR A 1 202 ? 33.946 -38.650 14.061 1.00 111.34 ? 202 THR A O 1 ATOM 1618 C CB . THR A 1 202 ? 32.667 -35.802 12.281 1.00 102.05 ? 202 THR A CB 1 ATOM 1619 O OG1 . THR A 1 202 ? 33.828 -36.011 11.465 1.00 99.95 ? 202 THR A OG1 1 ATOM 1620 C CG2 . THR A 1 202 ? 32.494 -34.326 12.547 1.00 100.15 ? 202 THR A CG2 1 ATOM 1621 N N . SER A 1 203 ? 32.594 -38.614 12.260 1.00 111.76 ? 203 SER A N 1 ATOM 1622 C CA . SER A 1 203 ? 32.981 -39.939 11.798 1.00 113.52 ? 203 SER A CA 1 ATOM 1623 C C . SER A 1 203 ? 34.461 -39.972 11.428 1.00 112.17 ? 203 SER A C 1 ATOM 1624 O O . SER A 1 203 ? 35.157 -40.934 11.740 1.00 114.03 ? 203 SER A O 1 ATOM 1625 C CB . SER A 1 203 ? 32.135 -40.343 10.591 1.00 114.87 ? 203 SER A CB 1 ATOM 1626 O OG . SER A 1 203 ? 32.531 -41.604 10.087 1.00 118.90 ? 203 SER A OG 1 ATOM 1627 N N . THR A 1 204 ? 34.928 -38.912 10.770 1.00 109.84 ? 204 THR A N 1 ATOM 1628 C CA . THR A 1 204 ? 36.314 -38.817 10.307 1.00 108.32 ? 204 THR A CA 1 ATOM 1629 C C . THR A 1 204 ? 37.157 -37.882 11.174 1.00 107.86 ? 204 THR A C 1 ATOM 1630 O O . THR A 1 204 ? 38.308 -38.186 11.484 1.00 109.38 ? 204 THR A O 1 ATOM 1631 C CB . THR A 1 204 ? 36.376 -38.320 8.847 1.00 105.94 ? 204 THR A CB 1 ATOM 1632 O OG1 . THR A 1 204 ? 35.919 -36.963 8.773 1.00 102.96 ? 204 THR A OG1 1 ATOM 1633 C CG2 . THR A 1 204 ? 35.516 -39.194 7.942 1.00 105.90 ? 204 THR A CG2 1 ATOM 1634 N N . LEU A 1 205 ? 36.577 -36.750 11.565 1.00 106.65 ? 205 LEU A N 1 ATOM 1635 C CA . LEU A 1 205 ? 37.316 -35.690 12.254 1.00 104.63 ? 205 LEU A CA 1 ATOM 1636 C C . LEU A 1 205 ? 37.715 -36.065 13.692 1.00 104.22 ? 205 LEU A C 1 ATOM 1637 O O . LEU A 1 205 ? 36.922 -36.642 14.437 1.00 104.30 ? 205 LEU A O 1 ATOM 1638 C CB . LEU A 1 205 ? 36.485 -34.401 12.264 1.00 103.78 ? 205 LEU A CB 1 ATOM 1639 C CG . LEU A 1 205 ? 37.251 -33.095 12.492 1.00 104.84 ? 205 LEU A CG 1 ATOM 1640 C CD1 . LEU A 1 205 ? 38.187 -32.797 11.327 1.00 103.14 ? 205 LEU A CD1 1 ATOM 1641 C CD2 . LEU A 1 205 ? 36.282 -31.942 12.707 1.00 104.56 ? 205 LEU A CD2 1 ATOM 1642 N N . ASN A 1 206 ? 38.954 -35.738 14.061 1.00 101.67 ? 206 ASN A N 1 ATOM 1643 C CA . ASN A 1 206 ? 39.442 -35.915 15.426 1.00 101.09 ? 206 ASN A CA 1 ATOM 1644 C C . ASN A 1 206 ? 40.348 -34.744 15.815 1.00 99.23 ? 206 ASN A C 1 ATOM 1645 O O . ASN A 1 206 ? 41.577 -34.849 15.823 1.00 97.31 ? 206 ASN A O 1 ATOM 1646 C CB . ASN A 1 206 ? 40.174 -37.249 15.577 1.00 102.85 ? 206 ASN A CB 1 ATOM 1647 C CG . ASN A 1 206 ? 40.631 -37.509 17.003 1.00 105.40 ? 206 ASN A CG 1 ATOM 1648 O OD1 . ASN A 1 206 ? 39.996 -37.075 17.968 1.00 105.42 ? 206 ASN A OD1 1 ATOM 1649 N ND2 . ASN A 1 206 ? 41.743 -38.216 17.142 1.00 107.63 ? 206 ASN A ND2 1 ATOM 1650 N N . GLN A 1 207 ? 39.710 -33.632 16.155 1.00 97.45 ? 207 GLN A N 1 ATOM 1651 C CA . GLN A 1 207 ? 40.397 -32.369 16.354 1.00 98.38 ? 207 GLN A CA 1 ATOM 1652 C C . GLN A 1 207 ? 40.498 -31.997 17.836 1.00 99.54 ? 207 GLN A C 1 ATOM 1653 O O . GLN A 1 207 ? 39.633 -32.348 18.632 1.00 99.76 ? 207 GLN A O 1 ATOM 1654 C CB . GLN A 1 207 ? 39.633 -31.291 15.591 1.00 97.47 ? 207 GLN A CB 1 ATOM 1655 C CG . GLN A 1 207 ? 40.226 -29.899 15.653 1.00 97.24 ? 207 GLN A CG 1 ATOM 1656 C CD . GLN A 1 207 ? 39.415 -28.921 14.838 1.00 97.01 ? 207 GLN A CD 1 ATOM 1657 O OE1 . GLN A 1 207 ? 38.739 -28.052 15.386 1.00 99.31 ? 207 GLN A OE1 1 ATOM 1658 N NE2 . GLN A 1 207 ? 39.454 -29.075 13.519 1.00 96.19 ? 207 GLN A NE2 1 ATOM 1659 N N . ARG A 1 208 ? 41.569 -31.298 18.194 1.00 100.61 ? 208 ARG A N 1 ATOM 1660 C CA . ARG A 1 208 ? 41.686 -30.677 19.510 1.00 103.93 ? 208 ARG A CA 1 ATOM 1661 C C . ARG A 1 208 ? 42.439 -29.360 19.374 1.00 103.69 ? 208 ARG A C 1 ATOM 1662 O O . ARG A 1 208 ? 43.653 -29.345 19.157 1.00 104.09 ? 208 ARG A O 1 ATOM 1663 C CB . ARG A 1 208 ? 42.395 -31.594 20.507 1.00 108.09 ? 208 ARG A CB 1 ATOM 1664 C CG . ARG A 1 208 ? 42.277 -31.131 21.954 1.00 111.77 ? 208 ARG A CG 1 ATOM 1665 C CD . ARG A 1 208 ? 43.111 -31.985 22.898 1.00 115.55 ? 208 ARG A CD 1 ATOM 1666 N NE . ARG A 1 208 ? 42.846 -31.680 24.306 1.00 119.14 ? 208 ARG A NE 1 ATOM 1667 C CZ . ARG A 1 208 ? 41.780 -32.098 24.994 1.00 121.92 ? 208 ARG A CZ 1 ATOM 1668 N NH1 . ARG A 1 208 ? 40.840 -32.844 24.417 1.00 122.21 ? 208 ARG A NH1 1 ATOM 1669 N NH2 . ARG A 1 208 ? 41.646 -31.762 26.274 1.00 123.81 ? 208 ARG A NH2 1 ATOM 1670 N N . LEU A 1 209 ? 41.706 -28.258 19.490 1.00 103.16 ? 209 LEU A N 1 ATOM 1671 C CA . LEU A 1 209 ? 42.282 -26.929 19.365 1.00 103.01 ? 209 LEU A CA 1 ATOM 1672 C C . LEU A 1 209 ? 42.631 -26.392 20.746 1.00 103.93 ? 209 LEU A C 1 ATOM 1673 O O . LEU A 1 209 ? 41.883 -26.594 21.698 1.00 104.71 ? 209 LEU A O 1 ATOM 1674 C CB . LEU A 1 209 ? 41.287 -25.987 18.684 1.00 102.64 ? 209 LEU A CB 1 ATOM 1675 C CG . LEU A 1 209 ? 40.695 -26.444 17.346 1.00 101.84 ? 209 LEU A CG 1 ATOM 1676 C CD1 . LEU A 1 209 ? 39.541 -25.536 16.943 1.00 101.50 ? 209 LEU A CD1 1 ATOM 1677 C CD2 . LEU A 1 209 ? 41.759 -26.483 16.257 1.00 101.11 ? 209 LEU A CD2 1 ATOM 1678 N N . VAL A 1 210 ? 43.771 -25.720 20.850 1.00 104.39 ? 210 VAL A N 1 ATOM 1679 C CA . VAL A 1 210 ? 44.134 -25.002 22.068 1.00 107.48 ? 210 VAL A CA 1 ATOM 1680 C C . VAL A 1 210 ? 44.446 -23.547 21.717 1.00 107.15 ? 210 VAL A C 1 ATOM 1681 O O . VAL A 1 210 ? 45.108 -23.283 20.706 1.00 105.72 ? 210 VAL A O 1 ATOM 1682 C CB . VAL A 1 210 ? 45.326 -25.651 22.817 1.00 109.34 ? 210 VAL A CB 1 ATOM 1683 C CG1 . VAL A 1 210 ? 44.921 -27.007 23.372 1.00 110.23 ? 210 VAL A CG1 1 ATOM 1684 C CG2 . VAL A 1 210 ? 46.556 -25.783 21.926 1.00 109.17 ? 210 VAL A CG2 1 ATOM 1685 N N . PRO A 1 211 ? 43.953 -22.595 22.535 1.00 107.95 ? 211 PRO A N 1 ATOM 1686 C CA . PRO A 1 211 ? 44.280 -21.194 22.274 1.00 107.40 ? 211 PRO A CA 1 ATOM 1687 C C . PRO A 1 211 ? 45.770 -20.899 22.423 1.00 107.38 ? 211 PRO A C 1 ATOM 1688 O O . PRO A 1 211 ? 46.466 -21.559 23.198 1.00 107.88 ? 211 PRO A O 1 ATOM 1689 C CB . PRO A 1 211 ? 43.476 -20.430 23.331 1.00 108.39 ? 211 PRO A CB 1 ATOM 1690 C CG . PRO A 1 211 ? 42.403 -21.363 23.749 1.00 109.04 ? 211 PRO A CG 1 ATOM 1691 C CD . PRO A 1 211 ? 42.989 -22.734 23.639 1.00 109.22 ? 211 PRO A CD 1 ATOM 1692 N N . ARG A 1 212 ? 46.232 -19.901 21.681 1.00 105.89 ? 212 ARG A N 1 ATOM 1693 C CA . ARG A 1 212 ? 47.636 -19.558 21.602 1.00 107.36 ? 212 ARG A CA 1 ATOM 1694 C C . ARG A 1 212 ? 47.803 -18.104 22.026 1.00 109.31 ? 212 ARG A C 1 ATOM 1695 O O . ARG A 1 212 ? 47.429 -17.191 21.292 1.00 108.40 ? 212 ARG A O 1 ATOM 1696 C CB . ARG A 1 212 ? 48.143 -19.805 20.174 1.00 106.14 ? 212 ARG A CB 1 ATOM 1697 C CG . ARG A 1 212 ? 48.777 -21.182 19.992 1.00 107.15 ? 212 ARG A CG 1 ATOM 1698 C CD . ARG A 1 212 ? 48.542 -21.840 18.636 1.00 105.79 ? 212 ARG A CD 1 ATOM 1699 N NE . ARG A 1 212 ? 48.512 -20.905 17.509 1.00 104.46 ? 212 ARG A NE 1 ATOM 1700 C CZ . ARG A 1 212 ? 47.554 -20.850 16.580 1.00 103.72 ? 212 ARG A CZ 1 ATOM 1701 N NH1 . ARG A 1 212 ? 46.514 -21.682 16.598 1.00 102.86 ? 212 ARG A NH1 1 ATOM 1702 N NH2 . ARG A 1 212 ? 47.638 -19.955 15.605 1.00 104.92 ? 212 ARG A NH2 1 ATOM 1703 N N . ILE A 1 213 ? 48.341 -17.901 23.228 1.00 114.23 ? 213 ILE A N 1 ATOM 1704 C CA . ILE A 1 213 ? 48.547 -16.556 23.775 1.00 116.77 ? 213 ILE A CA 1 ATOM 1705 C C . ILE A 1 213 ? 49.790 -15.937 23.146 1.00 119.08 ? 213 ILE A C 1 ATOM 1706 O O . ILE A 1 213 ? 50.801 -16.616 22.954 1.00 121.91 ? 213 ILE A O 1 ATOM 1707 C CB . ILE A 1 213 ? 48.728 -16.559 25.312 1.00 118.37 ? 213 ILE A CB 1 ATOM 1708 C CG1 . ILE A 1 213 ? 47.617 -17.360 26.010 1.00 119.02 ? 213 ILE A CG1 1 ATOM 1709 C CG2 . ILE A 1 213 ? 48.779 -15.132 25.844 1.00 119.37 ? 213 ILE A CG2 1 ATOM 1710 C CD1 . ILE A 1 213 ? 46.212 -17.002 25.577 1.00 117.23 ? 213 ILE A CD1 1 ATOM 1711 N N . ALA A 1 214 ? 49.706 -14.649 22.830 1.00 120.16 ? 214 ALA A N 1 ATOM 1712 C CA . ALA A 1 214 ? 50.814 -13.932 22.208 1.00 121.28 ? 214 ALA A CA 1 ATOM 1713 C C . ALA A 1 214 ? 50.498 -12.445 22.096 1.00 122.99 ? 214 ALA A C 1 ATOM 1714 O O . ALA A 1 214 ? 49.384 -12.061 21.725 1.00 120.75 ? 214 ALA A O 1 ATOM 1715 C CB . ALA A 1 214 ? 51.115 -14.508 20.829 1.00 119.37 ? 214 ALA A CB 1 ATOM 1716 N N . THR A 1 215 ? 51.483 -11.615 22.430 1.00 125.92 ? 215 THR A N 1 ATOM 1717 C CA . THR A 1 215 ? 51.401 -10.185 22.172 1.00 126.13 ? 215 THR A CA 1 ATOM 1718 C C . THR A 1 215 ? 51.413 -9.988 20.660 1.00 122.27 ? 215 THR A C 1 ATOM 1719 O O . THR A 1 215 ? 52.328 -10.450 19.979 1.00 122.77 ? 215 THR A O 1 ATOM 1720 C CB . THR A 1 215 ? 52.580 -9.431 22.814 1.00 129.65 ? 215 THR A CB 1 ATOM 1721 O OG1 . THR A 1 215 ? 52.528 -9.594 24.235 1.00 132.06 ? 215 THR A OG1 1 ATOM 1722 C CG2 . THR A 1 215 ? 52.533 -7.939 22.475 1.00 131.16 ? 215 THR A CG2 1 ATOM 1723 N N . ARG A 1 216 ? 50.386 -9.320 20.144 1.00 118.33 ? 216 ARG A N 1 ATOM 1724 C CA . ARG A 1 216 ? 50.215 -9.153 18.704 1.00 114.80 ? 216 ARG A CA 1 ATOM 1725 C C . ARG A 1 216 ? 49.897 -7.712 18.338 1.00 114.27 ? 216 ARG A C 1 ATOM 1726 O O . ARG A 1 216 ? 49.410 -6.939 19.161 1.00 114.62 ? 216 ARG A O 1 ATOM 1727 C CB . ARG A 1 216 ? 49.083 -10.049 18.205 1.00 112.41 ? 216 ARG A CB 1 ATOM 1728 C CG . ARG A 1 216 ? 49.404 -11.532 18.197 1.00 110.75 ? 216 ARG A CG 1 ATOM 1729 C CD . ARG A 1 216 ? 48.163 -12.337 17.857 1.00 108.55 ? 216 ARG A CD 1 ATOM 1730 N NE . ARG A 1 216 ? 47.186 -12.304 18.946 1.00 108.93 ? 216 ARG A NE 1 ATOM 1731 C CZ . ARG A 1 216 ? 46.979 -13.277 19.836 1.00 107.92 ? 216 ARG A CZ 1 ATOM 1732 N NH1 . ARG A 1 216 ? 47.668 -14.414 19.800 1.00 106.94 ? 216 ARG A NH1 1 ATOM 1733 N NH2 . ARG A 1 216 ? 46.059 -13.114 20.776 1.00 108.61 ? 216 ARG A NH2 1 ATOM 1734 N N . SER A 1 217 ? 50.165 -7.368 17.084 1.00 114.50 ? 217 SER A N 1 ATOM 1735 C CA . SER A 1 217 ? 49.790 -6.069 16.541 1.00 115.27 ? 217 SER A CA 1 ATOM 1736 C C . SER A 1 217 ? 48.271 -5.900 16.562 1.00 113.67 ? 217 SER A C 1 ATOM 1737 O O . SER A 1 217 ? 47.524 -6.881 16.541 1.00 110.72 ? 217 SER A O 1 ATOM 1738 C CB . SER A 1 217 ? 50.302 -5.937 15.105 1.00 115.73 ? 217 SER A CB 1 ATOM 1739 O OG . SER A 1 217 ? 51.702 -6.151 15.042 1.00 118.92 ? 217 SER A OG 1 ATOM 1740 N N . LYS A 1 218 ? 47.818 -4.653 16.614 1.00 113.59 ? 218 LYS A N 1 ATOM 1741 C CA . LYS A 1 218 ? 46.391 -4.366 16.526 1.00 110.64 ? 218 LYS A CA 1 ATOM 1742 C C . LYS A 1 218 ? 45.956 -4.377 15.070 1.00 109.52 ? 218 LYS A C 1 ATOM 1743 O O . LYS A 1 218 ? 46.623 -3.801 14.210 1.00 111.18 ? 218 LYS A O 1 ATOM 1744 C CB . LYS A 1 218 ? 46.048 -3.021 17.170 1.00 110.44 ? 218 LYS A CB 1 ATOM 1745 C CG . LYS A 1 218 ? 45.963 -3.083 18.682 1.00 110.95 ? 218 LYS A CG 1 ATOM 1746 C CD . LYS A 1 218 ? 45.212 -1.894 19.249 1.00 111.81 ? 218 LYS A CD 1 ATOM 1747 C CE . LYS A 1 218 ? 45.162 -1.964 20.765 1.00 114.08 ? 218 LYS A CE 1 ATOM 1748 N NZ . LYS A 1 218 ? 44.263 -0.931 21.344 1.00 116.09 ? 218 LYS A NZ 1 ATOM 1749 N N . VAL A 1 219 ? 44.841 -5.051 14.806 1.00 106.95 ? 219 VAL A N 1 ATOM 1750 C CA . VAL A 1 219 ? 44.251 -5.109 13.477 1.00 103.59 ? 219 VAL A CA 1 ATOM 1751 C C . VAL A 1 219 ? 42.759 -4.848 13.644 1.00 102.41 ? 219 VAL A C 1 ATOM 1752 O O . VAL A 1 219 ? 42.085 -5.552 14.391 1.00 102.40 ? 219 VAL A O 1 ATOM 1753 C CB . VAL A 1 219 ? 44.486 -6.486 12.827 1.00 102.97 ? 219 VAL A CB 1 ATOM 1754 C CG1 . VAL A 1 219 ? 43.885 -6.534 11.428 1.00 101.99 ? 219 VAL A CG1 1 ATOM 1755 C CG2 . VAL A 1 219 ? 45.976 -6.806 12.785 1.00 103.06 ? 219 VAL A CG2 1 ATOM 1756 N N . ASN A 1 220 ? 42.255 -3.821 12.966 1.00 102.04 ? 220 ASN A N 1 ATOM 1757 C CA . ASN A 1 220 ? 40.898 -3.318 13.201 1.00 103.11 ? 220 ASN A CA 1 ATOM 1758 C C . ASN A 1 220 ? 40.628 -3.073 14.695 1.00 102.38 ? 220 ASN A C 1 ATOM 1759 O O . ASN A 1 220 ? 39.523 -3.308 15.187 1.00 103.23 ? 220 ASN A O 1 ATOM 1760 C CB . ASN A 1 220 ? 39.855 -4.273 12.610 1.00 104.69 ? 220 ASN A CB 1 ATOM 1761 C CG . ASN A 1 220 ? 40.183 -4.692 11.186 1.00 105.69 ? 220 ASN A CG 1 ATOM 1762 O OD1 . ASN A 1 220 ? 40.181 -5.881 10.859 1.00 104.97 ? 220 ASN A OD1 1 ATOM 1763 N ND2 . ASN A 1 220 ? 40.474 -3.715 10.333 1.00 106.44 ? 220 ASN A ND2 1 ATOM 1764 N N . GLY A 1 221 ? 41.653 -2.606 15.406 1.00 101.06 ? 221 GLY A N 1 ATOM 1765 C CA . GLY A 1 221 ? 41.545 -2.289 16.824 1.00 101.08 ? 221 GLY A CA 1 ATOM 1766 C C . GLY A 1 221 ? 41.608 -3.463 17.788 1.00 99.66 ? 221 GLY A C 1 ATOM 1767 O O . GLY A 1 221 ? 41.390 -3.283 18.983 1.00 101.51 ? 221 GLY A O 1 ATOM 1768 N N . GLN A 1 222 ? 41.922 -4.658 17.297 1.00 97.05 ? 222 GLN A N 1 ATOM 1769 C CA . GLN A 1 222 ? 41.887 -5.850 18.142 1.00 97.57 ? 222 GLN A CA 1 ATOM 1770 C C . GLN A 1 222 ? 43.244 -6.527 18.283 1.00 97.46 ? 222 GLN A C 1 ATOM 1771 O O . GLN A 1 222 ? 43.990 -6.653 17.312 1.00 95.48 ? 222 GLN A O 1 ATOM 1772 C CB . GLN A 1 222 ? 40.872 -6.856 17.596 1.00 96.90 ? 222 GLN A CB 1 ATOM 1773 C CG . GLN A 1 222 ? 39.462 -6.302 17.451 1.00 97.83 ? 222 GLN A CG 1 ATOM 1774 C CD . GLN A 1 222 ? 38.929 -5.684 18.733 1.00 99.89 ? 222 GLN A CD 1 ATOM 1775 O OE1 . GLN A 1 222 ? 39.208 -6.168 19.835 1.00 99.75 ? 222 GLN A OE1 1 ATOM 1776 N NE2 . GLN A 1 222 ? 38.154 -4.610 18.596 1.00 101.05 ? 222 GLN A NE2 1 ATOM 1777 N N . ASN A 1 223 ? 43.541 -6.959 19.509 1.00 99.18 ? 223 ASN A N 1 ATOM 1778 C CA . ASN A 1 223 ? 44.737 -7.740 19.820 1.00 100.75 ? 223 ASN A CA 1 ATOM 1779 C C . ASN A 1 223 ? 44.459 -9.222 19.668 1.00 99.24 ? 223 ASN A C 1 ATOM 1780 O O . ASN A 1 223 ? 45.305 -9.979 19.195 1.00 99.06 ? 223 ASN A O 1 ATOM 1781 C CB . ASN A 1 223 ? 45.184 -7.481 21.257 1.00 104.07 ? 223 ASN A CB 1 ATOM 1782 C CG . ASN A 1 223 ? 45.672 -6.067 21.468 1.00 106.94 ? 223 ASN A CG 1 ATOM 1783 O OD1 . ASN A 1 223 ? 46.767 -5.707 21.037 1.00 108.82 ? 223 ASN A OD1 1 ATOM 1784 N ND2 . ASN A 1 223 ? 44.867 -5.258 22.145 1.00 108.47 ? 223 ASN A ND2 1 ATOM 1785 N N . GLY A 1 224 ? 43.268 -9.632 20.095 1.00 99.02 ? 224 GLY A N 1 ATOM 1786 C CA . GLY A 1 224 ? 42.838 -11.014 19.966 1.00 97.46 ? 224 GLY A CA 1 ATOM 1787 C C . GLY A 1 224 ? 42.721 -11.445 18.519 1.00 94.49 ? 224 GLY A C 1 ATOM 1788 O O . GLY A 1 224 ? 42.652 -10.607 17.616 1.00 93.33 ? 224 GLY A O 1 ATOM 1789 N N . ARG A 1 225 ? 42.704 -12.758 18.306 1.00 93.73 ? 225 ARG A N 1 ATOM 1790 C CA . ARG A 1 225 ? 42.535 -13.339 16.975 1.00 92.26 ? 225 ARG A CA 1 ATOM 1791 C C . ARG A 1 225 ? 41.449 -14.403 16.996 1.00 91.67 ? 225 ARG A C 1 ATOM 1792 O O . ARG A 1 225 ? 41.205 -15.030 18.022 1.00 93.28 ? 225 ARG A O 1 ATOM 1793 C CB . ARG A 1 225 ? 43.845 -13.960 16.486 1.00 91.14 ? 225 ARG A CB 1 ATOM 1794 C CG . ARG A 1 225 ? 44.971 -12.966 16.267 1.00 92.10 ? 225 ARG A CG 1 ATOM 1795 C CD . ARG A 1 225 ? 44.773 -12.173 14.988 1.00 92.29 ? 225 ARG A CD 1 ATOM 1796 N NE . ARG A 1 225 ? 45.903 -11.283 14.729 1.00 94.45 ? 225 ARG A NE 1 ATOM 1797 C CZ . ARG A 1 225 ? 46.039 -10.050 15.215 1.00 95.52 ? 225 ARG A CZ 1 ATOM 1798 N NH1 . ARG A 1 225 ? 45.111 -9.516 16.005 1.00 96.09 ? 225 ARG A NH1 1 ATOM 1799 N NH2 . ARG A 1 225 ? 47.118 -9.342 14.905 1.00 96.57 ? 225 ARG A NH2 1 ATOM 1800 N N . MET A 1 226 ? 40.796 -14.586 15.856 1.00 91.47 ? 226 MET A N 1 ATOM 1801 C CA . MET A 1 226 ? 39.821 -15.646 15.677 1.00 92.30 ? 226 MET A CA 1 ATOM 1802 C C . MET A 1 226 ? 40.298 -16.541 14.548 1.00 91.26 ? 226 MET A C 1 ATOM 1803 O O . MET A 1 226 ? 40.572 -16.064 13.451 1.00 91.13 ? 226 MET A O 1 ATOM 1804 C CB . MET A 1 226 ? 38.459 -15.067 15.312 1.00 94.73 ? 226 MET A CB 1 ATOM 1805 C CG . MET A 1 226 ? 37.848 -14.174 16.376 1.00 98.77 ? 226 MET A CG 1 ATOM 1806 S SD . MET A 1 226 ? 37.025 -15.082 17.695 1.00 104.07 ? 226 MET A SD 1 ATOM 1807 C CE . MET A 1 226 ? 36.329 -13.715 18.616 1.00 105.85 ? 226 MET A CE 1 ATOM 1808 N N . GLU A 1 227 ? 40.398 -17.835 14.824 1.00 91.41 ? 227 GLU A N 1 ATOM 1809 C CA . GLU A 1 227 ? 40.780 -18.826 13.831 1.00 89.14 ? 227 GLU A CA 1 ATOM 1810 C C . GLU A 1 227 ? 39.558 -19.686 13.568 1.00 88.25 ? 227 GLU A C 1 ATOM 1811 O O . GLU A 1 227 ? 39.044 -20.323 14.484 1.00 91.06 ? 227 GLU A O 1 ATOM 1812 C CB . GLU A 1 227 ? 41.935 -19.671 14.366 1.00 91.06 ? 227 GLU A CB 1 ATOM 1813 C CG . GLU A 1 227 ? 42.691 -20.463 13.310 1.00 92.95 ? 227 GLU A CG 1 ATOM 1814 C CD . GLU A 1 227 ? 44.047 -20.945 13.799 1.00 95.13 ? 227 GLU A CD 1 ATOM 1815 O OE1 . GLU A 1 227 ? 44.336 -20.815 15.007 1.00 96.07 ? 227 GLU A OE1 1 ATOM 1816 O OE2 . GLU A 1 227 ? 44.835 -21.452 12.972 1.00 97.81 ? 227 GLU A OE2 1 ATOM 1817 N N . PHE A 1 228 ? 39.072 -19.685 12.332 1.00 85.72 ? 228 PHE A N 1 ATOM 1818 C CA . PHE A 1 228 ? 37.850 -20.412 12.000 1.00 84.24 ? 228 PHE A CA 1 ATOM 1819 C C . PHE A 1 228 ? 38.159 -21.712 11.279 1.00 82.71 ? 228 PHE A C 1 ATOM 1820 O O . PHE A 1 228 ? 39.136 -21.804 10.529 1.00 81.43 ? 228 PHE A O 1 ATOM 1821 C CB . PHE A 1 228 ? 36.919 -19.536 11.170 1.00 84.54 ? 228 PHE A CB 1 ATOM 1822 C CG . PHE A 1 228 ? 36.430 -18.327 11.912 1.00 86.29 ? 228 PHE A CG 1 ATOM 1823 C CD1 . PHE A 1 228 ? 35.300 -18.399 12.710 1.00 87.36 ? 228 PHE A CD1 1 ATOM 1824 C CD2 . PHE A 1 228 ? 37.119 -17.126 11.838 1.00 87.29 ? 228 PHE A CD2 1 ATOM 1825 C CE1 . PHE A 1 228 ? 34.855 -17.290 13.409 1.00 88.57 ? 228 PHE A CE1 1 ATOM 1826 C CE2 . PHE A 1 228 ? 36.679 -16.011 12.533 1.00 88.44 ? 228 PHE A CE2 1 ATOM 1827 C CZ . PHE A 1 228 ? 35.546 -16.095 13.322 1.00 88.58 ? 228 PHE A CZ 1 ATOM 1828 N N . PHE A 1 229 ? 37.324 -22.716 11.533 1.00 80.96 ? 229 PHE A N 1 ATOM 1829 C CA . PHE A 1 229 ? 37.491 -24.043 10.962 1.00 80.30 ? 229 PHE A CA 1 ATOM 1830 C C . PHE A 1 229 ? 36.175 -24.500 10.372 1.00 81.65 ? 229 PHE A C 1 ATOM 1831 O O . PHE A 1 229 ? 35.124 -23.918 10.645 1.00 82.48 ? 229 PHE A O 1 ATOM 1832 C CB . PHE A 1 229 ? 37.946 -25.031 12.031 1.00 81.17 ? 229 PHE A CB 1 ATOM 1833 C CG . PHE A 1 229 ? 39.292 -24.714 12.602 1.00 81.61 ? 229 PHE A CG 1 ATOM 1834 C CD1 . PHE A 1 229 ? 39.427 -23.761 13.600 1.00 82.46 ? 229 PHE A CD1 1 ATOM 1835 C CD2 . PHE A 1 229 ? 40.426 -25.353 12.129 1.00 82.19 ? 229 PHE A CD2 1 ATOM 1836 C CE1 . PHE A 1 229 ? 40.670 -23.451 14.120 1.00 82.75 ? 229 PHE A CE1 1 ATOM 1837 C CE2 . PHE A 1 229 ? 41.674 -25.048 12.644 1.00 83.15 ? 229 PHE A CE2 1 ATOM 1838 C CZ . PHE A 1 229 ? 41.797 -24.096 13.642 1.00 82.92 ? 229 PHE A CZ 1 ATOM 1839 N N . TRP A 1 230 ? 36.234 -25.544 9.557 1.00 82.82 ? 230 TRP A N 1 ATOM 1840 C CA . TRP A 1 230 ? 35.033 -26.070 8.936 1.00 82.62 ? 230 TRP A CA 1 ATOM 1841 C C . TRP A 1 230 ? 35.127 -27.563 8.688 1.00 83.22 ? 230 TRP A C 1 ATOM 1842 O O . TRP A 1 230 ? 36.196 -28.157 8.791 1.00 82.99 ? 230 TRP A O 1 ATOM 1843 C CB . TRP A 1 230 ? 34.760 -25.340 7.623 1.00 81.88 ? 230 TRP A CB 1 ATOM 1844 C CG . TRP A 1 230 ? 35.855 -25.472 6.607 1.00 80.93 ? 230 TRP A CG 1 ATOM 1845 C CD1 . TRP A 1 230 ? 36.963 -24.685 6.489 1.00 80.45 ? 230 TRP A CD1 1 ATOM 1846 C CD2 . TRP A 1 230 ? 35.935 -26.439 5.556 1.00 80.29 ? 230 TRP A CD2 1 ATOM 1847 N NE1 . TRP A 1 230 ? 37.729 -25.105 5.433 1.00 79.39 ? 230 TRP A NE1 1 ATOM 1848 C CE2 . TRP A 1 230 ? 37.121 -26.181 4.844 1.00 79.64 ? 230 TRP A CE2 1 ATOM 1849 C CE3 . TRP A 1 230 ? 35.116 -27.498 5.147 1.00 80.99 ? 230 TRP A CE3 1 ATOM 1850 C CZ2 . TRP A 1 230 ? 37.512 -26.946 3.747 1.00 80.68 ? 230 TRP A CZ2 1 ATOM 1851 C CZ3 . TRP A 1 230 ? 35.506 -28.257 4.055 1.00 81.03 ? 230 TRP A CZ3 1 ATOM 1852 C CH2 . TRP A 1 230 ? 36.695 -27.979 3.370 1.00 80.70 ? 230 TRP A CH2 1 ATOM 1853 N N . THR A 1 231 ? 33.983 -28.161 8.382 1.00 84.10 ? 231 THR A N 1 ATOM 1854 C CA . THR A 1 231 ? 33.927 -29.544 7.945 1.00 84.27 ? 231 THR A CA 1 ATOM 1855 C C . THR A 1 231 ? 32.629 -29.792 7.189 1.00 84.54 ? 231 THR A C 1 ATOM 1856 O O . THR A 1 231 ? 31.683 -29.010 7.289 1.00 83.04 ? 231 THR A O 1 ATOM 1857 C CB . THR A 1 231 ? 34.051 -30.521 9.133 1.00 85.50 ? 231 THR A CB 1 ATOM 1858 O OG1 . THR A 1 231 ? 34.403 -31.821 8.647 1.00 86.97 ? 231 THR A OG1 1 ATOM 1859 C CG2 . THR A 1 231 ? 32.750 -30.605 9.933 1.00 85.59 ? 231 THR A CG2 1 ATOM 1860 N N . ILE A 1 232 ? 32.608 -30.870 6.415 1.00 87.29 ? 232 ILE A N 1 ATOM 1861 C CA . ILE A 1 232 ? 31.398 -31.331 5.747 1.00 88.81 ? 232 ILE A CA 1 ATOM 1862 C C . ILE A 1 232 ? 30.879 -32.497 6.561 1.00 90.18 ? 232 ILE A C 1 ATOM 1863 O O . ILE A 1 232 ? 31.528 -33.534 6.655 1.00 92.79 ? 232 ILE A O 1 ATOM 1864 C CB . ILE A 1 232 ? 31.663 -31.737 4.273 1.00 88.97 ? 232 ILE A CB 1 ATOM 1865 C CG1 . ILE A 1 232 ? 31.327 -30.582 3.324 1.00 87.61 ? 232 ILE A CG1 1 ATOM 1866 C CG2 . ILE A 1 232 ? 30.820 -32.939 3.850 1.00 91.21 ? 232 ILE A CG2 1 ATOM 1867 C CD1 . ILE A 1 232 ? 31.932 -29.256 3.712 1.00 86.91 ? 232 ILE A CD1 1 ATOM 1868 N N . LEU A 1 233 ? 29.714 -32.310 7.165 1.00 92.22 ? 233 LEU A N 1 ATOM 1869 C CA . LEU A 1 233 ? 29.085 -33.347 7.966 1.00 93.09 ? 233 LEU A CA 1 ATOM 1870 C C . LEU A 1 233 ? 28.197 -34.186 7.056 1.00 94.52 ? 233 LEU A C 1 ATOM 1871 O O . LEU A 1 233 ? 27.238 -33.675 6.477 1.00 93.34 ? 233 LEU A O 1 ATOM 1872 C CB . LEU A 1 233 ? 28.264 -32.703 9.082 1.00 93.98 ? 233 LEU A CB 1 ATOM 1873 C CG . LEU A 1 233 ? 27.745 -33.582 10.221 1.00 95.70 ? 233 LEU A CG 1 ATOM 1874 C CD1 . LEU A 1 233 ? 28.892 -34.181 11.022 1.00 95.97 ? 233 LEU A CD1 1 ATOM 1875 C CD2 . LEU A 1 233 ? 26.832 -32.760 11.119 1.00 95.70 ? 233 LEU A CD2 1 ATOM 1876 N N . LYS A 1 234 ? 28.534 -35.467 6.921 1.00 97.82 ? 234 LYS A N 1 ATOM 1877 C CA . LYS A 1 234 ? 27.772 -36.408 6.088 1.00 101.80 ? 234 LYS A CA 1 ATOM 1878 C C . LYS A 1 234 ? 26.339 -36.589 6.603 1.00 103.61 ? 234 LYS A C 1 ATOM 1879 O O . LYS A 1 234 ? 26.033 -36.181 7.726 1.00 104.23 ? 234 LYS A O 1 ATOM 1880 C CB . LYS A 1 234 ? 28.480 -37.772 6.070 1.00 105.35 ? 234 LYS A CB 1 ATOM 1881 C CG . LYS A 1 234 ? 29.801 -37.805 5.311 1.00 106.75 ? 234 LYS A CG 1 ATOM 1882 C CD . LYS A 1 234 ? 29.606 -37.586 3.819 1.00 109.29 ? 234 LYS A CD 1 ATOM 1883 C CE . LYS A 1 234 ? 30.734 -38.207 3.006 1.00 112.23 ? 234 LYS A CE 1 ATOM 1884 N NZ . LYS A 1 234 ? 32.077 -37.678 3.381 1.00 111.63 ? 234 LYS A NZ 1 ATOM 1885 N N . PRO A 1 235 ? 25.450 -37.199 5.788 1.00 105.35 ? 235 PRO A N 1 ATOM 1886 C CA . PRO A 1 235 ? 24.128 -37.531 6.338 1.00 105.63 ? 235 PRO A CA 1 ATOM 1887 C C . PRO A 1 235 ? 24.253 -38.592 7.419 1.00 107.11 ? 235 PRO A C 1 ATOM 1888 O O . PRO A 1 235 ? 25.168 -39.413 7.363 1.00 106.61 ? 235 PRO A O 1 ATOM 1889 C CB . PRO A 1 235 ? 23.359 -38.087 5.135 1.00 106.35 ? 235 PRO A CB 1 ATOM 1890 C CG . PRO A 1 235 ? 24.398 -38.488 4.144 1.00 105.62 ? 235 PRO A CG 1 ATOM 1891 C CD . PRO A 1 235 ? 25.598 -37.625 4.382 1.00 103.85 ? 235 PRO A CD 1 ATOM 1892 N N . ASN A 1 236 ? 23.358 -38.566 8.403 1.00 109.58 ? 236 ASN A N 1 ATOM 1893 C CA . ASN A 1 236 ? 23.338 -39.582 9.459 1.00 112.29 ? 236 ASN A CA 1 ATOM 1894 C C . ASN A 1 236 ? 24.594 -39.603 10.338 1.00 112.22 ? 236 ASN A C 1 ATOM 1895 O O . ASN A 1 236 ? 24.842 -40.581 11.042 1.00 114.66 ? 236 ASN A O 1 ATOM 1896 C CB . ASN A 1 236 ? 23.112 -40.982 8.850 1.00 114.23 ? 236 ASN A CB 1 ATOM 1897 C CG . ASN A 1 236 ? 21.725 -41.523 9.114 1.00 117.63 ? 236 ASN A CG 1 ATOM 1898 O OD1 . ASN A 1 236 ? 21.134 -41.283 10.169 1.00 119.00 ? 236 ASN A OD1 1 ATOM 1899 N ND2 . ASN A 1 236 ? 21.206 -42.284 8.162 1.00 119.41 ? 236 ASN A ND2 1 ATOM 1900 N N . ASP A 1 237 ? 25.379 -38.531 10.301 1.00 110.47 ? 237 ASP A N 1 ATOM 1901 C CA . ASP A 1 237 ? 26.587 -38.440 11.112 1.00 109.91 ? 237 ASP A CA 1 ATOM 1902 C C . ASP A 1 237 ? 26.417 -37.304 12.102 1.00 107.79 ? 237 ASP A C 1 ATOM 1903 O O . ASP A 1 237 ? 25.672 -36.356 11.849 1.00 107.05 ? 237 ASP A O 1 ATOM 1904 C CB . ASP A 1 237 ? 27.816 -38.197 10.231 1.00 109.75 ? 237 ASP A CB 1 ATOM 1905 C CG . ASP A 1 237 ? 29.130 -38.432 10.969 1.00 110.63 ? 237 ASP A CG 1 ATOM 1906 O OD1 . ASP A 1 237 ? 29.131 -39.134 12.004 1.00 112.77 ? 237 ASP A OD1 1 ATOM 1907 O OD2 . ASP A 1 237 ? 30.170 -37.918 10.504 1.00 110.34 ? 237 ASP A OD2 1 ATOM 1908 N N . ALA A 1 238 ? 27.105 -37.409 13.232 1.00 107.23 ? 238 ALA A N 1 ATOM 1909 C CA . ALA A 1 238 ? 26.969 -36.433 14.300 1.00 106.85 ? 238 ALA A CA 1 ATOM 1910 C C . ALA A 1 238 ? 28.291 -35.732 14.544 1.00 103.92 ? 238 ALA A C 1 ATOM 1911 O O . ALA A 1 238 ? 29.342 -36.374 14.548 1.00 105.38 ? 238 ALA A O 1 ATOM 1912 C CB . ALA A 1 238 ? 26.493 -37.116 15.575 1.00 109.16 ? 238 ALA A CB 1 ATOM 1913 N N . ILE A 1 239 ? 28.236 -34.416 14.737 1.00 101.31 ? 239 ILE A N 1 ATOM 1914 C CA . ILE A 1 239 ? 29.411 -33.652 15.165 1.00 99.85 ? 239 ILE A CA 1 ATOM 1915 C C . ILE A 1 239 ? 29.369 -33.437 16.687 1.00 102.05 ? 239 ILE A C 1 ATOM 1916 O O . ILE A 1 239 ? 28.332 -33.073 17.247 1.00 101.77 ? 239 ILE A O 1 ATOM 1917 C CB . ILE A 1 239 ? 29.563 -32.313 14.401 1.00 96.77 ? 239 ILE A CB 1 ATOM 1918 C CG1 . ILE A 1 239 ? 30.937 -31.697 14.691 1.00 95.95 ? 239 ILE A CG1 1 ATOM 1919 C CG2 . ILE A 1 239 ? 28.450 -31.329 14.750 1.00 96.53 ? 239 ILE A CG2 1 ATOM 1920 C CD1 . ILE A 1 239 ? 31.342 -30.608 13.724 1.00 93.93 ? 239 ILE A CD1 1 ATOM 1921 N N . ASN A 1 240 ? 30.506 -33.673 17.339 1.00 102.54 ? 240 ASN A N 1 ATOM 1922 C CA . ASN A 1 240 ? 30.598 -33.680 18.795 1.00 104.03 ? 240 ASN A CA 1 ATOM 1923 C C . ASN A 1 240 ? 31.558 -32.618 19.295 1.00 102.76 ? 240 ASN A C 1 ATOM 1924 O O . ASN A 1 240 ? 32.756 -32.706 19.046 1.00 102.09 ? 240 ASN A O 1 ATOM 1925 C CB . ASN A 1 240 ? 31.093 -35.041 19.266 1.00 106.48 ? 240 ASN A CB 1 ATOM 1926 C CG . ASN A 1 240 ? 30.114 -36.151 18.960 1.00 109.05 ? 240 ASN A CG 1 ATOM 1927 O OD1 . ASN A 1 240 ? 28.957 -36.099 19.378 1.00 109.82 ? 240 ASN A OD1 1 ATOM 1928 N ND2 . ASN A 1 240 ? 30.573 -37.167 18.230 1.00 109.87 ? 240 ASN A ND2 1 ATOM 1929 N N . PHE A 1 241 ? 31.034 -31.626 20.011 1.00 103.47 ? 241 PHE A N 1 ATOM 1930 C CA . PHE A 1 241 ? 31.858 -30.561 20.575 1.00 103.00 ? 241 PHE A CA 1 ATOM 1931 C C . PHE A 1 241 ? 32.100 -30.779 22.061 1.00 104.86 ? 241 PHE A C 1 ATOM 1932 O O . PHE A 1 241 ? 31.224 -31.256 22.779 1.00 107.49 ? 241 PHE A O 1 ATOM 1933 C CB . PHE A 1 241 ? 31.196 -29.202 20.359 1.00 102.22 ? 241 PHE A CB 1 ATOM 1934 C CG . PHE A 1 241 ? 31.162 -28.775 18.924 1.00 101.85 ? 241 PHE A CG 1 ATOM 1935 C CD1 . PHE A 1 241 ? 32.298 -28.255 18.316 1.00 101.38 ? 241 PHE A CD1 1 ATOM 1936 C CD2 . PHE A 1 241 ? 30.004 -28.905 18.172 1.00 102.34 ? 241 PHE A CD2 1 ATOM 1937 C CE1 . PHE A 1 241 ? 32.278 -27.863 16.989 1.00 100.07 ? 241 PHE A CE1 1 ATOM 1938 C CE2 . PHE A 1 241 ? 29.977 -28.516 16.844 1.00 101.14 ? 241 PHE A CE2 1 ATOM 1939 C CZ . PHE A 1 241 ? 31.115 -27.993 16.251 1.00 100.11 ? 241 PHE A CZ 1 ATOM 1940 N N . GLU A 1 242 ? 33.303 -30.440 22.508 1.00 104.98 ? 242 GLU A N 1 ATOM 1941 C CA . GLU A 1 242 ? 33.604 -30.356 23.929 1.00 108.19 ? 242 GLU A CA 1 ATOM 1942 C C . GLU A 1 242 ? 34.619 -29.241 24.153 1.00 106.24 ? 242 GLU A C 1 ATOM 1943 O O . GLU A 1 242 ? 35.657 -29.203 23.492 1.00 104.14 ? 242 GLU A O 1 ATOM 1944 C CB . GLU A 1 242 ? 34.131 -31.689 24.473 1.00 111.84 ? 242 GLU A CB 1 ATOM 1945 C CG . GLU A 1 242 ? 34.217 -31.741 25.995 1.00 116.34 ? 242 GLU A CG 1 ATOM 1946 C CD . GLU A 1 242 ? 34.989 -32.943 26.510 1.00 118.64 ? 242 GLU A CD 1 ATOM 1947 O OE1 . GLU A 1 242 ? 34.801 -34.056 25.975 1.00 120.05 ? 242 GLU A OE1 1 ATOM 1948 O OE2 . GLU A 1 242 ? 35.783 -32.775 27.460 1.00 119.00 ? 242 GLU A OE2 1 ATOM 1949 N N . SER A 1 243 ? 34.309 -28.333 25.078 1.00 106.22 ? 243 SER A N 1 ATOM 1950 C CA . SER A 1 243 ? 35.184 -27.199 25.364 1.00 105.25 ? 243 SER A CA 1 ATOM 1951 C C . SER A 1 243 ? 34.944 -26.617 26.749 1.00 107.28 ? 243 SER A C 1 ATOM 1952 O O . SER A 1 243 ? 33.865 -26.776 27.317 1.00 109.99 ? 243 SER A O 1 ATOM 1953 C CB . SER A 1 243 ? 34.974 -26.102 24.325 1.00 102.81 ? 243 SER A CB 1 ATOM 1954 O OG . SER A 1 243 ? 35.747 -24.959 24.641 1.00 102.90 ? 243 SER A OG 1 ATOM 1955 N N . ASN A 1 244 ? 35.959 -25.935 27.277 1.00 107.45 ? 244 ASN A N 1 ATOM 1956 C CA . ASN A 1 244 ? 35.844 -25.207 28.549 1.00 109.57 ? 244 ASN A CA 1 ATOM 1957 C C . ASN A 1 244 ? 36.314 -23.752 28.423 1.00 108.28 ? 244 ASN A C 1 ATOM 1958 O O . ASN A 1 244 ? 36.741 -23.142 29.403 1.00 108.80 ? 244 ASN A O 1 ATOM 1959 C CB . ASN A 1 244 ? 36.617 -25.933 29.658 1.00 111.23 ? 244 ASN A CB 1 ATOM 1960 C CG . ASN A 1 244 ? 38.107 -26.004 29.386 1.00 110.74 ? 244 ASN A CG 1 ATOM 1961 O OD1 . ASN A 1 244 ? 38.542 -26.012 28.232 1.00 109.93 ? 244 ASN A OD1 1 ATOM 1962 N ND2 . ASN A 1 244 ? 38.898 -26.059 30.449 1.00 111.33 ? 244 ASN A ND2 1 ATOM 1963 N N . GLY A 1 245 ? 36.219 -23.203 27.212 1.00 106.30 ? 245 GLY A N 1 ATOM 1964 C CA . GLY A 1 245 ? 36.581 -21.814 26.957 1.00 105.44 ? 245 GLY A CA 1 ATOM 1965 C C . GLY A 1 245 ? 37.091 -21.571 25.551 1.00 103.52 ? 245 GLY A C 1 ATOM 1966 O O . GLY A 1 245 ? 37.569 -22.493 24.880 1.00 103.10 ? 245 GLY A O 1 ATOM 1967 N N . ASN A 1 246 ? 36.983 -20.315 25.118 1.00 102.59 ? 246 ASN A N 1 ATOM 1968 C CA . ASN A 1 246 ? 37.491 -19.840 23.822 1.00 99.23 ? 246 ASN A CA 1 ATOM 1969 C C . ASN A 1 246 ? 36.734 -20.380 22.609 1.00 96.35 ? 246 ASN A C 1 ATOM 1970 O O . ASN A 1 246 ? 37.144 -20.157 21.475 1.00 94.14 ? 246 ASN A O 1 ATOM 1971 C CB . ASN A 1 246 ? 38.998 -20.110 23.673 1.00 99.33 ? 246 ASN A CB 1 ATOM 1972 C CG . ASN A 1 246 ? 39.826 -19.446 24.763 1.00 101.26 ? 246 ASN A CG 1 ATOM 1973 O OD1 . ASN A 1 246 ? 40.349 -18.351 24.575 1.00 102.82 ? 246 ASN A OD1 1 ATOM 1974 N ND2 . ASN A 1 246 ? 39.959 -20.111 25.902 1.00 102.36 ? 246 ASN A ND2 1 ATOM 1975 N N . PHE A 1 247 ? 35.608 -21.044 22.852 1.00 96.87 ? 247 PHE A N 1 ATOM 1976 C CA . PHE A 1 247 ? 34.846 -21.711 21.805 1.00 94.97 ? 247 PHE A CA 1 ATOM 1977 C C . PHE A 1 247 ? 33.926 -20.723 21.097 1.00 93.78 ? 247 PHE A C 1 ATOM 1978 O O . PHE A 1 247 ? 33.147 -20.018 21.738 1.00 95.76 ? 247 PHE A O 1 ATOM 1979 C CB . PHE A 1 247 ? 34.045 -22.867 22.426 1.00 97.18 ? 247 PHE A CB 1 ATOM 1980 C CG . PHE A 1 247 ? 33.233 -23.677 21.444 1.00 96.28 ? 247 PHE A CG 1 ATOM 1981 C CD1 . PHE A 1 247 ? 33.726 -24.002 20.191 1.00 94.32 ? 247 PHE A CD1 1 ATOM 1982 C CD2 . PHE A 1 247 ? 31.983 -24.158 21.807 1.00 98.23 ? 247 PHE A CD2 1 ATOM 1983 C CE1 . PHE A 1 247 ? 32.977 -24.760 19.308 1.00 94.40 ? 247 PHE A CE1 1 ATOM 1984 C CE2 . PHE A 1 247 ? 31.230 -24.919 20.931 1.00 97.71 ? 247 PHE A CE2 1 ATOM 1985 C CZ . PHE A 1 247 ? 31.728 -25.221 19.679 1.00 96.29 ? 247 PHE A CZ 1 ATOM 1986 N N . ILE A 1 248 ? 34.048 -20.657 19.775 1.00 91.64 ? 248 ILE A N 1 ATOM 1987 C CA . ILE A 1 248 ? 33.119 -19.906 18.947 1.00 90.76 ? 248 ILE A CA 1 ATOM 1988 C C . ILE A 1 248 ? 32.204 -20.958 18.340 1.00 91.32 ? 248 ILE A C 1 ATOM 1989 O O . ILE A 1 248 ? 32.603 -21.697 17.442 1.00 90.37 ? 248 ILE A O 1 ATOM 1990 C CB . ILE A 1 248 ? 33.837 -19.102 17.843 1.00 89.32 ? 248 ILE A CB 1 ATOM 1991 C CG1 . ILE A 1 248 ? 35.055 -18.355 18.398 1.00 89.55 ? 248 ILE A CG1 1 ATOM 1992 C CG2 . ILE A 1 248 ? 32.878 -18.117 17.193 1.00 89.15 ? 248 ILE A CG2 1 ATOM 1993 C CD1 . ILE A 1 248 ? 34.740 -17.383 19.511 1.00 91.57 ? 248 ILE A CD1 1 ATOM 1994 N N . ALA A 1 249 ? 30.984 -21.043 18.856 1.00 93.61 ? 249 ALA A N 1 ATOM 1995 C CA . ALA A 1 249 ? 30.091 -22.154 18.540 1.00 94.77 ? 249 ALA A CA 1 ATOM 1996 C C . ALA A 1 249 ? 29.245 -21.884 17.300 1.00 94.04 ? 249 ALA A C 1 ATOM 1997 O O . ALA A 1 249 ? 28.876 -20.746 17.038 1.00 94.58 ? 249 ALA A O 1 ATOM 1998 C CB . ALA A 1 249 ? 29.190 -22.442 19.727 1.00 97.07 ? 249 ALA A CB 1 ATOM 1999 N N . PRO A 1 250 ? 28.928 -22.937 16.532 1.00 94.22 ? 250 PRO A N 1 ATOM 2000 C CA . PRO A 1 250 ? 28.021 -22.751 15.407 1.00 94.49 ? 250 PRO A CA 1 ATOM 2001 C C . PRO A 1 250 ? 26.605 -22.453 15.873 1.00 96.54 ? 250 PRO A C 1 ATOM 2002 O O . PRO A 1 250 ? 26.144 -23.069 16.828 1.00 100.13 ? 250 PRO A O 1 ATOM 2003 C CB . PRO A 1 250 ? 28.060 -24.107 14.691 1.00 93.79 ? 250 PRO A CB 1 ATOM 2004 C CG . PRO A 1 250 ? 28.507 -25.082 15.715 1.00 94.32 ? 250 PRO A CG 1 ATOM 2005 C CD . PRO A 1 250 ? 29.415 -24.324 16.632 1.00 94.90 ? 250 PRO A CD 1 ATOM 2006 N N . GLU A 1 251 ? 25.935 -21.505 15.224 1.00 97.17 ? 251 GLU A N 1 ATOM 2007 C CA . GLU A 1 251 ? 24.494 -21.327 15.400 1.00 100.77 ? 251 GLU A CA 1 ATOM 2008 C C . GLU A 1 251 ? 23.774 -21.820 14.152 1.00 99.65 ? 251 GLU A C 1 ATOM 2009 O O . GLU A 1 251 ? 22.896 -22.686 14.229 1.00 97.53 ? 251 GLU A O 1 ATOM 2010 C CB . GLU A 1 251 ? 24.130 -19.866 15.665 1.00 104.14 ? 251 GLU A CB 1 ATOM 2011 C CG . GLU A 1 251 ? 22.700 -19.697 16.170 1.00 108.68 ? 251 GLU A CG 1 ATOM 2012 C CD . GLU A 1 251 ? 22.246 -18.251 16.237 1.00 112.31 ? 251 GLU A CD 1 ATOM 2013 O OE1 . GLU A 1 251 ? 23.078 -17.337 16.024 1.00 114.28 ? 251 GLU A OE1 1 ATOM 2014 O OE2 . GLU A 1 251 ? 21.044 -18.033 16.507 1.00 113.68 ? 251 GLU A OE2 1 ATOM 2015 N N . TYR A 1 252 ? 24.160 -21.256 13.008 1.00 98.11 ? 252 TYR A N 1 ATOM 2016 C CA . TYR A 1 252 ? 23.620 -21.647 11.714 1.00 96.64 ? 252 TYR A CA 1 ATOM 2017 C C . TYR A 1 252 ? 24.687 -22.359 10.881 1.00 95.21 ? 252 TYR A C 1 ATOM 2018 O O . TYR A 1 252 ? 25.857 -21.968 10.879 1.00 92.00 ? 252 TYR A O 1 ATOM 2019 C CB . TYR A 1 252 ? 23.120 -20.417 10.950 1.00 96.53 ? 252 TYR A CB 1 ATOM 2020 C CG . TYR A 1 252 ? 22.044 -19.621 11.659 1.00 98.63 ? 252 TYR A CG 1 ATOM 2021 C CD1 . TYR A 1 252 ? 20.724 -20.064 11.680 1.00 100.74 ? 252 TYR A CD1 1 ATOM 2022 C CD2 . TYR A 1 252 ? 22.342 -18.422 12.301 1.00 98.46 ? 252 TYR A CD2 1 ATOM 2023 C CE1 . TYR A 1 252 ? 19.734 -19.339 12.326 1.00 101.41 ? 252 TYR A CE1 1 ATOM 2024 C CE2 . TYR A 1 252 ? 21.359 -17.690 12.947 1.00 99.76 ? 252 TYR A CE2 1 ATOM 2025 C CZ . TYR A 1 252 ? 20.055 -18.154 12.958 1.00 101.55 ? 252 TYR A CZ 1 ATOM 2026 O OH . TYR A 1 252 ? 19.071 -17.433 13.601 1.00 102.44 ? 252 TYR A OH 1 ATOM 2027 N N . ALA A 1 253 ? 24.266 -23.414 10.185 1.00 94.85 ? 253 ALA A N 1 ATOM 2028 C CA . ALA A 1 253 ? 25.096 -24.103 9.202 1.00 92.32 ? 253 ALA A CA 1 ATOM 2029 C C . ALA A 1 253 ? 24.356 -24.110 7.860 1.00 93.37 ? 253 ALA A C 1 ATOM 2030 O O . ALA A 1 253 ? 23.169 -23.781 7.805 1.00 95.63 ? 253 ALA A O 1 ATOM 2031 C CB . ALA A 1 253 ? 25.388 -25.522 9.665 1.00 91.79 ? 253 ALA A CB 1 ATOM 2032 N N . TYR A 1 254 ? 25.056 -24.475 6.787 1.00 91.53 ? 254 TYR A N 1 ATOM 2033 C CA . TYR A 1 254 ? 24.489 -24.453 5.440 1.00 91.62 ? 254 TYR A CA 1 ATOM 2034 C C . TYR A 1 254 ? 24.278 -25.858 4.889 1.00 91.70 ? 254 TYR A C 1 ATOM 2035 O O . TYR A 1 254 ? 25.209 -26.658 4.860 1.00 90.59 ? 254 TYR A O 1 ATOM 2036 C CB . TYR A 1 254 ? 25.420 -23.708 4.485 1.00 90.74 ? 254 TYR A CB 1 ATOM 2037 C CG . TYR A 1 254 ? 25.642 -22.245 4.796 1.00 90.49 ? 254 TYR A CG 1 ATOM 2038 C CD1 . TYR A 1 254 ? 26.669 -21.845 5.643 1.00 90.15 ? 254 TYR A CD1 1 ATOM 2039 C CD2 . TYR A 1 254 ? 24.847 -21.259 4.213 1.00 91.00 ? 254 TYR A CD2 1 ATOM 2040 C CE1 . TYR A 1 254 ? 26.890 -20.506 5.917 1.00 90.90 ? 254 TYR A CE1 1 ATOM 2041 C CE2 . TYR A 1 254 ? 25.057 -19.917 4.480 1.00 91.65 ? 254 TYR A CE2 1 ATOM 2042 C CZ . TYR A 1 254 ? 26.081 -19.545 5.332 1.00 92.66 ? 254 TYR A CZ 1 ATOM 2043 O OH . TYR A 1 254 ? 26.297 -18.211 5.603 1.00 96.01 ? 254 TYR A OH 1 ATOM 2044 N N . LYS A 1 255 ? 23.058 -26.152 4.443 1.00 93.85 ? 255 LYS A N 1 ATOM 2045 C CA . LYS A 1 255 ? 22.789 -27.385 3.698 1.00 95.34 ? 255 LYS A CA 1 ATOM 2046 C C . LYS A 1 255 ? 23.218 -27.200 2.254 1.00 93.56 ? 255 LYS A C 1 ATOM 2047 O O . LYS A 1 255 ? 22.993 -26.146 1.666 1.00 91.59 ? 255 LYS A O 1 ATOM 2048 C CB . LYS A 1 255 ? 21.304 -27.744 3.718 1.00 98.50 ? 255 LYS A CB 1 ATOM 2049 C CG . LYS A 1 255 ? 20.787 -28.275 5.043 1.00 100.39 ? 255 LYS A CG 1 ATOM 2050 C CD . LYS A 1 255 ? 19.424 -28.934 4.885 1.00 103.19 ? 255 LYS A CD 1 ATOM 2051 C CE . LYS A 1 255 ? 18.338 -27.943 4.487 1.00 104.62 ? 255 LYS A CE 1 ATOM 2052 N NZ . LYS A 1 255 ? 17.031 -28.616 4.240 1.00 107.06 ? 255 LYS A NZ 1 ATOM 2053 N N . ILE A 1 256 ? 23.826 -28.237 1.690 1.00 94.67 ? 256 ILE A N 1 ATOM 2054 C CA . ILE A 1 256 ? 24.217 -28.248 0.288 1.00 95.05 ? 256 ILE A CA 1 ATOM 2055 C C . ILE A 1 256 ? 23.106 -28.926 -0.500 1.00 96.61 ? 256 ILE A C 1 ATOM 2056 O O . ILE A 1 256 ? 23.061 -30.149 -0.587 1.00 97.70 ? 256 ILE A O 1 ATOM 2057 C CB . ILE A 1 256 ? 25.538 -29.014 0.094 1.00 95.21 ? 256 ILE A CB 1 ATOM 2058 C CG1 . ILE A 1 256 ? 26.670 -28.299 0.838 1.00 94.76 ? 256 ILE A CG1 1 ATOM 2059 C CG2 . ILE A 1 256 ? 25.870 -29.143 -1.388 1.00 95.98 ? 256 ILE A CG2 1 ATOM 2060 C CD1 . ILE A 1 256 ? 27.922 -29.130 1.025 1.00 94.75 ? 256 ILE A CD1 1 ATOM 2061 N N . VAL A 1 257 ? 22.204 -28.132 -1.068 1.00 97.91 ? 257 VAL A N 1 ATOM 2062 C CA . VAL A 1 257 ? 21.027 -28.695 -1.742 1.00 102.25 ? 257 VAL A CA 1 ATOM 2063 C C . VAL A 1 257 ? 21.274 -28.979 -3.228 1.00 103.87 ? 257 VAL A C 1 ATOM 2064 O O . VAL A 1 257 ? 20.862 -30.030 -3.736 1.00 104.12 ? 257 VAL A O 1 ATOM 2065 C CB . VAL A 1 257 ? 19.751 -27.838 -1.539 1.00 103.19 ? 257 VAL A CB 1 ATOM 2066 C CG1 . VAL A 1 257 ? 19.358 -27.819 -0.070 1.00 104.04 ? 257 VAL A CG1 1 ATOM 2067 C CG2 . VAL A 1 257 ? 19.920 -26.419 -2.060 1.00 102.04 ? 257 VAL A CG2 1 ATOM 2068 N N . LYS A 1 258 ? 21.950 -28.055 -3.910 1.00 103.53 ? 258 LYS A N 1 ATOM 2069 C CA . LYS A 1 258 ? 22.277 -28.214 -5.330 1.00 105.63 ? 258 LYS A CA 1 ATOM 2070 C C . LYS A 1 258 ? 23.778 -28.272 -5.561 1.00 103.72 ? 258 LYS A C 1 ATOM 2071 O O . LYS A 1 258 ? 24.497 -27.338 -5.215 1.00 103.26 ? 258 LYS A O 1 ATOM 2072 C CB . LYS A 1 258 ? 21.682 -27.068 -6.156 1.00 107.43 ? 258 LYS A CB 1 ATOM 2073 C CG . LYS A 1 258 ? 20.432 -27.447 -6.930 1.00 112.01 ? 258 LYS A CG 1 ATOM 2074 C CD . LYS A 1 258 ? 20.787 -28.178 -8.217 1.00 114.39 ? 258 LYS A CD 1 ATOM 2075 C CE . LYS A 1 258 ? 21.070 -27.212 -9.360 1.00 114.99 ? 258 LYS A CE 1 ATOM 2076 N NZ . LYS A 1 258 ? 19.816 -26.763 -10.028 1.00 116.02 ? 258 LYS A NZ 1 ATOM 2077 N N . LYS A 1 259 ? 24.239 -29.375 -6.146 1.00 104.63 ? 259 LYS A N 1 ATOM 2078 C CA . LYS A 1 259 ? 25.611 -29.493 -6.633 1.00 105.44 ? 259 LYS A CA 1 ATOM 2079 C C . LYS A 1 259 ? 25.615 -29.346 -8.149 1.00 106.82 ? 259 LYS A C 1 ATOM 2080 O O . LYS A 1 259 ? 24.624 -29.648 -8.807 1.00 110.04 ? 259 LYS A O 1 ATOM 2081 C CB . LYS A 1 259 ? 26.212 -30.840 -6.228 1.00 107.52 ? 259 LYS A CB 1 ATOM 2082 C CG . LYS A 1 259 ? 26.753 -30.862 -4.808 1.00 109.42 ? 259 LYS A CG 1 ATOM 2083 C CD . LYS A 1 259 ? 27.011 -32.277 -4.316 1.00 111.24 ? 259 LYS A CD 1 ATOM 2084 C CE . LYS A 1 259 ? 27.491 -32.274 -2.874 1.00 112.14 ? 259 LYS A CE 1 ATOM 2085 N NZ . LYS A 1 259 ? 27.414 -33.619 -2.241 1.00 113.86 ? 259 LYS A NZ 1 ATOM 2086 N N . GLY A 1 260 ? 26.725 -28.874 -8.705 1.00 107.57 ? 260 GLY A N 1 ATOM 2087 C CA . GLY A 1 260 ? 26.829 -28.707 -10.153 1.00 108.53 ? 260 GLY A CA 1 ATOM 2088 C C . GLY A 1 260 ? 27.870 -27.696 -10.578 1.00 107.39 ? 260 GLY A C 1 ATOM 2089 O O . GLY A 1 260 ? 28.677 -27.246 -9.770 1.00 107.66 ? 260 GLY A O 1 ATOM 2090 N N . ASP A 1 261 ? 27.833 -27.331 -11.856 1.00 108.95 ? 261 ASP A N 1 ATOM 2091 C CA . ASP A 1 261 ? 28.858 -26.478 -12.452 1.00 108.46 ? 261 ASP A CA 1 ATOM 2092 C C . ASP A 1 261 ? 28.711 -25.024 -12.026 1.00 103.29 ? 261 ASP A C 1 ATOM 2093 O O . ASP A 1 261 ? 27.655 -24.415 -12.182 1.00 101.84 ? 261 ASP A O 1 ATOM 2094 C CB . ASP A 1 261 ? 28.834 -26.581 -13.985 1.00 113.39 ? 261 ASP A CB 1 ATOM 2095 C CG . ASP A 1 261 ? 29.508 -27.845 -14.502 1.00 118.28 ? 261 ASP A CG 1 ATOM 2096 O OD1 . ASP A 1 261 ? 30.230 -28.510 -13.726 1.00 121.49 ? 261 ASP A OD1 1 ATOM 2097 O OD2 . ASP A 1 261 ? 29.324 -28.168 -15.696 1.00 122.08 ? 261 ASP A OD2 1 ATOM 2098 N N . SER A 1 262 ? 29.796 -24.482 -11.493 1.00 99.05 ? 262 SER A N 1 ATOM 2099 C CA . SER A 1 262 ? 29.831 -23.120 -10.990 1.00 97.94 ? 262 SER A CA 1 ATOM 2100 C C . SER A 1 262 ? 31.287 -22.689 -10.991 1.00 95.96 ? 262 SER A C 1 ATOM 2101 O O . SER A 1 262 ? 32.164 -23.463 -11.378 1.00 98.61 ? 262 SER A O 1 ATOM 2102 C CB . SER A 1 262 ? 29.243 -23.062 -9.573 1.00 98.14 ? 262 SER A CB 1 ATOM 2103 O OG . SER A 1 262 ? 29.356 -21.772 -8.990 1.00 97.49 ? 262 SER A OG 1 ATOM 2104 N N . THR A 1 263 ? 31.544 -21.458 -10.569 1.00 93.16 ? 263 THR A N 1 ATOM 2105 C CA . THR A 1 263 ? 32.903 -20.944 -10.499 1.00 87.87 ? 263 THR A CA 1 ATOM 2106 C C . THR A 1 263 ? 32.922 -19.660 -9.693 1.00 83.51 ? 263 THR A C 1 ATOM 2107 O O . THR A 1 263 ? 31.906 -18.982 -9.590 1.00 82.95 ? 263 THR A O 1 ATOM 2108 C CB . THR A 1 263 ? 33.481 -20.677 -11.909 1.00 85.94 ? 263 THR A CB 1 ATOM 2109 O OG1 . THR A 1 263 ? 34.871 -20.370 -11.805 1.00 85.53 ? 263 THR A OG1 1 ATOM 2110 C CG2 . THR A 1 263 ? 32.770 -19.518 -12.599 1.00 84.93 ? 263 THR A CG2 1 ATOM 2111 N N . ILE A 1 264 ? 34.077 -19.342 -9.115 1.00 81.10 ? 264 ILE A N 1 ATOM 2112 C CA . ILE A 1 264 ? 34.289 -18.058 -8.454 1.00 77.72 ? 264 ILE A CA 1 ATOM 2113 C C . ILE A 1 264 ? 35.118 -17.181 -9.385 1.00 76.62 ? 264 ILE A C 1 ATOM 2114 O O . ILE A 1 264 ? 36.275 -17.471 -9.674 1.00 77.93 ? 264 ILE A O 1 ATOM 2115 C CB . ILE A 1 264 ? 34.998 -18.208 -7.099 1.00 76.45 ? 264 ILE A CB 1 ATOM 2116 C CG1 . ILE A 1 264 ? 34.248 -19.216 -6.229 1.00 78.90 ? 264 ILE A CG1 1 ATOM 2117 C CG2 . ILE A 1 264 ? 35.085 -16.864 -6.390 1.00 74.50 ? 264 ILE A CG2 1 ATOM 2118 C CD1 . ILE A 1 264 ? 34.860 -19.428 -4.866 1.00 80.58 ? 264 ILE A CD1 1 ATOM 2119 N N . MET A 1 265 ? 34.505 -16.103 -9.839 1.00 76.20 ? 265 MET A N 1 ATOM 2120 C CA . MET A 1 265 ? 35.076 -15.213 -10.829 1.00 74.71 ? 265 MET A CA 1 ATOM 2121 C C . MET A 1 265 ? 35.594 -13.983 -10.102 1.00 75.54 ? 265 MET A C 1 ATOM 2122 O O . MET A 1 265 ? 34.919 -13.466 -9.220 1.00 77.30 ? 265 MET A O 1 ATOM 2123 C CB . MET A 1 265 ? 33.955 -14.829 -11.786 1.00 75.64 ? 265 MET A CB 1 ATOM 2124 C CG . MET A 1 265 ? 34.355 -14.227 -13.108 1.00 74.51 ? 265 MET A CG 1 ATOM 2125 S SD . MET A 1 265 ? 32.893 -14.118 -14.163 1.00 75.31 ? 265 MET A SD 1 ATOM 2126 C CE . MET A 1 265 ? 32.819 -15.798 -14.782 1.00 75.11 ? 265 MET A CE 1 ATOM 2127 N N . LYS A 1 266 ? 36.799 -13.539 -10.440 1.00 77.46 ? 266 LYS A N 1 ATOM 2128 C CA . LYS A 1 266 ? 37.367 -12.331 -9.854 1.00 79.55 ? 266 LYS A CA 1 ATOM 2129 C C . LYS A 1 266 ? 37.101 -11.173 -10.795 1.00 78.73 ? 266 LYS A C 1 ATOM 2130 O O . LYS A 1 266 ? 37.533 -11.196 -11.943 1.00 79.39 ? 266 LYS A O 1 ATOM 2131 C CB . LYS A 1 266 ? 38.868 -12.481 -9.641 1.00 84.04 ? 266 LYS A CB 1 ATOM 2132 C CG . LYS A 1 266 ? 39.264 -13.633 -8.736 1.00 88.98 ? 266 LYS A CG 1 ATOM 2133 C CD . LYS A 1 266 ? 39.068 -13.281 -7.270 1.00 93.84 ? 266 LYS A CD 1 ATOM 2134 C CE . LYS A 1 266 ? 39.245 -14.501 -6.384 1.00 98.03 ? 266 LYS A CE 1 ATOM 2135 N NZ . LYS A 1 266 ? 38.260 -15.572 -6.717 1.00 100.40 ? 266 LYS A NZ 1 ATOM 2136 N N . SER A 1 267 ? 36.386 -10.163 -10.311 1.00 80.06 ? 267 SER A N 1 ATOM 2137 C CA . SER A 1 267 ? 35.985 -9.036 -11.145 1.00 80.80 ? 267 SER A CA 1 ATOM 2138 C C . SER A 1 267 ? 35.514 -7.872 -10.290 1.00 82.55 ? 267 SER A C 1 ATOM 2139 O O . SER A 1 267 ? 34.879 -8.075 -9.260 1.00 87.02 ? 267 SER A O 1 ATOM 2140 C CB . SER A 1 267 ? 34.860 -9.460 -12.087 1.00 81.11 ? 267 SER A CB 1 ATOM 2141 O OG . SER A 1 267 ? 34.301 -8.340 -12.750 1.00 83.06 ? 267 SER A OG 1 ATOM 2142 N N . GLU A 1 268 ? 35.823 -6.656 -10.728 1.00 84.79 ? 268 GLU A N 1 ATOM 2143 C CA . GLU A 1 268 ? 35.389 -5.447 -10.034 1.00 87.43 ? 268 GLU A CA 1 ATOM 2144 C C . GLU A 1 268 ? 34.023 -4.969 -10.535 1.00 87.90 ? 268 GLU A C 1 ATOM 2145 O O . GLU A 1 268 ? 33.403 -4.103 -9.921 1.00 92.72 ? 268 GLU A O 1 ATOM 2146 C CB . GLU A 1 268 ? 36.430 -4.334 -10.198 1.00 89.71 ? 268 GLU A CB 1 ATOM 2147 C CG . GLU A 1 268 ? 37.852 -4.735 -9.815 1.00 90.31 ? 268 GLU A CG 1 ATOM 2148 C CD . GLU A 1 268 ? 37.963 -5.288 -8.399 1.00 92.27 ? 268 GLU A CD 1 ATOM 2149 O OE1 . GLU A 1 268 ? 37.521 -4.606 -7.440 1.00 89.82 ? 268 GLU A OE1 1 ATOM 2150 O OE2 . GLU A 1 268 ? 38.496 -6.414 -8.249 1.00 91.57 ? 268 GLU A OE2 1 ATOM 2151 N N . LEU A 1 269 ? 33.550 -5.551 -11.632 1.00 86.13 ? 269 LEU A N 1 ATOM 2152 C CA . LEU A 1 269 ? 32.278 -5.168 -12.231 1.00 88.15 ? 269 LEU A CA 1 ATOM 2153 C C . LEU A 1 269 ? 31.108 -5.554 -11.335 1.00 91.23 ? 269 LEU A C 1 ATOM 2154 O O . LEU A 1 269 ? 31.192 -6.519 -10.575 1.00 89.65 ? 269 LEU A O 1 ATOM 2155 C CB . LEU A 1 269 ? 32.107 -5.840 -13.594 1.00 86.94 ? 269 LEU A CB 1 ATOM 2156 C CG . LEU A 1 269 ? 33.154 -5.500 -14.655 1.00 86.44 ? 269 LEU A CG 1 ATOM 2157 C CD1 . LEU A 1 269 ? 33.102 -6.494 -15.803 1.00 85.34 ? 269 LEU A CD1 1 ATOM 2158 C CD2 . LEU A 1 269 ? 32.958 -4.078 -15.157 1.00 89.36 ? 269 LEU A CD2 1 ATOM 2159 N N . GLU A 1 270 ? 30.027 -4.781 -11.431 1.00 96.06 ? 270 GLU A N 1 ATOM 2160 C CA . GLU A 1 270 ? 28.775 -5.070 -10.735 1.00 99.82 ? 270 GLU A CA 1 ATOM 2161 C C . GLU A 1 270 ? 27.775 -5.661 -11.740 1.00 96.04 ? 270 GLU A C 1 ATOM 2162 O O . GLU A 1 270 ? 28.119 -5.877 -12.901 1.00 92.94 ? 270 GLU A O 1 ATOM 2163 C CB . GLU A 1 270 ? 28.218 -3.794 -10.084 1.00 107.69 ? 270 GLU A CB 1 ATOM 2164 C CG . GLU A 1 270 ? 29.205 -3.029 -9.195 1.00 112.80 ? 270 GLU A CG 1 ATOM 2165 C CD . GLU A 1 270 ? 29.369 -3.623 -7.796 1.00 115.31 ? 270 GLU A CD 1 ATOM 2166 O OE1 . GLU A 1 270 ? 29.686 -4.827 -7.678 1.00 115.44 ? 270 GLU A OE1 1 ATOM 2167 O OE2 . GLU A 1 270 ? 29.180 -2.880 -6.806 1.00 117.05 ? 270 GLU A OE2 1 ATOM 2168 N N . TYR A 1 271 ? 26.547 -5.920 -11.293 1.00 95.89 ? 271 TYR A N 1 ATOM 2169 C CA . TYR A 1 271 ? 25.523 -6.577 -12.119 1.00 94.15 ? 271 TYR A CA 1 ATOM 2170 C C . TYR A 1 271 ? 25.084 -5.721 -13.307 1.00 95.78 ? 271 TYR A C 1 ATOM 2171 O O . TYR A 1 271 ? 24.938 -4.506 -13.187 1.00 95.89 ? 271 TYR A O 1 ATOM 2172 C CB . TYR A 1 271 ? 24.305 -6.916 -11.257 1.00 96.09 ? 271 TYR A CB 1 ATOM 2173 C CG . TYR A 1 271 ? 23.242 -7.754 -11.938 1.00 96.06 ? 271 TYR A CG 1 ATOM 2174 C CD1 . TYR A 1 271 ? 23.557 -8.970 -12.541 1.00 93.07 ? 271 TYR A CD1 1 ATOM 2175 C CD2 . TYR A 1 271 ? 21.913 -7.341 -11.949 1.00 98.20 ? 271 TYR A CD2 1 ATOM 2176 C CE1 . TYR A 1 271 ? 22.579 -9.740 -13.152 1.00 94.39 ? 271 TYR A CE1 1 ATOM 2177 C CE2 . TYR A 1 271 ? 20.929 -8.106 -12.548 1.00 99.91 ? 271 TYR A CE2 1 ATOM 2178 C CZ . TYR A 1 271 ? 21.261 -9.304 -13.148 1.00 98.27 ? 271 TYR A CZ 1 ATOM 2179 O OH . TYR A 1 271 ? 20.267 -10.050 -13.741 1.00 97.83 ? 271 TYR A OH 1 ATOM 2180 N N . GLY A 1 272 ? 24.856 -6.373 -14.445 1.00 97.43 ? 272 GLY A N 1 ATOM 2181 C CA . GLY A 1 272 ? 24.557 -5.677 -15.699 1.00 99.90 ? 272 GLY A CA 1 ATOM 2182 C C . GLY A 1 272 ? 23.106 -5.672 -16.151 1.00 104.59 ? 272 GLY A C 1 ATOM 2183 O O . GLY A 1 272 ? 22.782 -5.011 -17.137 1.00 104.89 ? 272 GLY A O 1 ATOM 2184 N N . ASN A 1 273 ? 22.237 -6.396 -15.440 1.00 108.13 ? 273 ASN A N 1 ATOM 2185 C CA . ASN A 1 273 ? 20.820 -6.551 -15.829 1.00 113.39 ? 273 ASN A CA 1 ATOM 2186 C C . ASN A 1 273 ? 20.712 -7.108 -17.247 1.00 112.50 ? 273 ASN A C 1 ATOM 2187 O O . ASN A 1 273 ? 20.203 -6.450 -18.152 1.00 115.02 ? 273 ASN A O 1 ATOM 2188 C CB . ASN A 1 273 ? 20.059 -5.220 -15.717 1.00 117.11 ? 273 ASN A CB 1 ATOM 2189 C CG . ASN A 1 273 ? 20.258 -4.539 -14.375 1.00 118.57 ? 273 ASN A CG 1 ATOM 2190 O OD1 . ASN A 1 273 ? 21.163 -3.718 -14.216 1.00 117.78 ? 273 ASN A OD1 1 ATOM 2191 N ND2 . ASN A 1 273 ? 19.418 -4.881 -13.401 1.00 119.49 ? 273 ASN A ND2 1 ATOM 2192 N N . CYS A 1 274 ? 21.184 -8.337 -17.424 1.00 110.14 ? 274 CYS A N 1 ATOM 2193 C CA . CYS A 1 274 ? 21.537 -8.844 -18.746 1.00 108.91 ? 274 CYS A CA 1 ATOM 2194 C C . CYS A 1 274 ? 21.497 -10.373 -18.779 1.00 101.17 ? 274 CYS A C 1 ATOM 2195 O O . CYS A 1 274 ? 21.544 -11.013 -17.734 1.00 101.56 ? 274 CYS A O 1 ATOM 2196 C CB . CYS A 1 274 ? 22.940 -8.321 -19.084 1.00 111.72 ? 274 CYS A CB 1 ATOM 2197 S SG . CYS A 1 274 ? 23.891 -9.302 -20.259 1.00 122.80 ? 274 CYS A SG 1 ATOM 2198 N N . ASN A 1 275 ? 21.410 -10.954 -19.972 1.00 96.06 ? 275 ASN A N 1 ATOM 2199 C CA . ASN A 1 275 ? 21.433 -12.414 -20.122 1.00 95.20 ? 275 ASN A CA 1 ATOM 2200 C C . ASN A 1 275 ? 22.424 -12.874 -21.200 1.00 93.45 ? 275 ASN A C 1 ATOM 2201 O O . ASN A 1 275 ? 22.649 -12.170 -22.185 1.00 94.38 ? 275 ASN A O 1 ATOM 2202 C CB . ASN A 1 275 ? 20.028 -12.934 -20.434 1.00 98.03 ? 275 ASN A CB 1 ATOM 2203 C CG . ASN A 1 275 ? 19.910 -14.440 -20.283 1.00 97.30 ? 275 ASN A CG 1 ATOM 2204 O OD1 . ASN A 1 275 ? 20.277 -15.004 -19.261 1.00 95.90 ? 275 ASN A OD1 1 ATOM 2205 N ND2 . ASN A 1 275 ? 19.384 -15.094 -21.303 1.00 101.31 ? 275 ASN A ND2 1 ATOM 2206 N N . THR A 1 276 ? 23.015 -14.053 -21.006 1.00 91.80 ? 276 THR A N 1 ATOM 2207 C CA . THR A 1 276 ? 24.039 -14.571 -21.915 1.00 88.44 ? 276 THR A CA 1 ATOM 2208 C C . THR A 1 276 ? 24.219 -16.081 -21.752 1.00 88.62 ? 276 THR A C 1 ATOM 2209 O O . THR A 1 276 ? 23.828 -16.645 -20.737 1.00 91.10 ? 276 THR A O 1 ATOM 2210 C CB . THR A 1 276 ? 25.399 -13.870 -21.672 1.00 86.53 ? 276 THR A CB 1 ATOM 2211 O OG1 . THR A 1 276 ? 26.325 -14.217 -22.708 1.00 86.37 ? 276 THR A OG1 1 ATOM 2212 C CG2 . THR A 1 276 ? 26.001 -14.261 -20.313 1.00 86.00 ? 276 THR A CG2 1 ATOM 2213 N N . LYS A 1 277 ? 24.817 -16.722 -22.752 1.00 89.43 ? 277 LYS A N 1 ATOM 2214 C CA . LYS A 1 277 ? 25.166 -18.147 -22.679 1.00 92.72 ? 277 LYS A CA 1 ATOM 2215 C C . LYS A 1 277 ? 26.652 -18.373 -22.370 1.00 88.08 ? 277 LYS A C 1 ATOM 2216 O O . LYS A 1 277 ? 27.090 -19.511 -22.218 1.00 86.67 ? 277 LYS A O 1 ATOM 2217 C CB . LYS A 1 277 ? 24.805 -18.861 -23.991 1.00 97.98 ? 277 LYS A CB 1 ATOM 2218 C CG . LYS A 1 277 ? 23.338 -19.262 -24.118 1.00 106.14 ? 277 LYS A CG 1 ATOM 2219 C CD . LYS A 1 277 ? 23.151 -20.282 -25.235 1.00 111.11 ? 277 LYS A CD 1 ATOM 2220 C CE . LYS A 1 277 ? 21.701 -20.725 -25.389 1.00 118.22 ? 277 LYS A CE 1 ATOM 2221 N NZ . LYS A 1 277 ? 21.212 -21.530 -24.233 1.00 121.92 ? 277 LYS A NZ 1 ATOM 2222 N N . CYS A 1 278 ? 27.420 -17.290 -22.289 1.00 84.90 ? 278 CYS A N 1 ATOM 2223 C CA . CYS A 1 278 ? 28.860 -17.370 -22.081 1.00 82.44 ? 278 CYS A CA 1 ATOM 2224 C C . CYS A 1 278 ? 29.326 -16.111 -21.358 1.00 78.32 ? 278 CYS A C 1 ATOM 2225 O O . CYS A 1 278 ? 29.064 -14.998 -21.819 1.00 78.37 ? 278 CYS A O 1 ATOM 2226 C CB . CYS A 1 278 ? 29.570 -17.514 -23.429 1.00 83.69 ? 278 CYS A CB 1 ATOM 2227 S SG . CYS A 1 278 ? 31.382 -17.484 -23.367 1.00 86.50 ? 278 CYS A SG 1 ATOM 2228 N N . GLN A 1 279 ? 29.997 -16.282 -20.222 1.00 74.70 ? 279 GLN A N 1 ATOM 2229 C CA . GLN A 1 279 ? 30.403 -15.142 -19.401 1.00 73.69 ? 279 GLN A CA 1 ATOM 2230 C C . GLN A 1 279 ? 31.889 -15.176 -19.098 1.00 71.61 ? 279 GLN A C 1 ATOM 2231 O O . GLN A 1 279 ? 32.448 -16.237 -18.826 1.00 71.37 ? 279 GLN A O 1 ATOM 2232 C CB . GLN A 1 279 ? 29.621 -15.114 -18.083 1.00 74.92 ? 279 GLN A CB 1 ATOM 2233 C CG . GLN A 1 279 ? 29.884 -13.879 -17.225 1.00 73.87 ? 279 GLN A CG 1 ATOM 2234 C CD . GLN A 1 279 ? 29.168 -12.637 -17.732 1.00 75.04 ? 279 GLN A CD 1 ATOM 2235 O OE1 . GLN A 1 279 ? 27.943 -12.622 -17.847 1.00 76.34 ? 279 GLN A OE1 1 ATOM 2236 N NE2 . GLN A 1 279 ? 29.927 -11.582 -18.019 1.00 73.56 ? 279 GLN A NE2 1 ATOM 2237 N N . THR A 1 280 ? 32.511 -14.001 -19.139 1.00 69.27 ? 280 THR A N 1 ATOM 2238 C CA . THR A 1 280 ? 33.897 -13.829 -18.735 1.00 68.91 ? 280 THR A CA 1 ATOM 2239 C C . THR A 1 280 ? 33.983 -12.758 -17.644 1.00 69.77 ? 280 THR A C 1 ATOM 2240 O O . THR A 1 280 ? 33.040 -11.985 -17.461 1.00 69.80 ? 280 THR A O 1 ATOM 2241 C CB . THR A 1 280 ? 34.783 -13.403 -19.920 1.00 68.38 ? 280 THR A CB 1 ATOM 2242 O OG1 . THR A 1 280 ? 34.752 -11.977 -20.073 1.00 66.46 ? 280 THR A OG1 1 ATOM 2243 C CG2 . THR A 1 280 ? 34.317 -14.076 -21.212 1.00 68.91 ? 280 THR A CG2 1 ATOM 2244 N N . PRO A 1 281 ? 35.117 -12.703 -16.919 1.00 69.93 ? 281 PRO A N 1 ATOM 2245 C CA . PRO A 1 281 ? 35.300 -11.689 -15.878 1.00 70.30 ? 281 PRO A CA 1 ATOM 2246 C C . PRO A 1 281 ? 35.262 -10.239 -16.354 1.00 71.30 ? 281 PRO A C 1 ATOM 2247 O O . PRO A 1 281 ? 35.125 -9.342 -15.522 1.00 70.95 ? 281 PRO A O 1 ATOM 2248 C CB . PRO A 1 281 ? 36.678 -12.014 -15.305 1.00 70.04 ? 281 PRO A CB 1 ATOM 2249 C CG . PRO A 1 281 ? 36.881 -13.455 -15.588 1.00 70.44 ? 281 PRO A CG 1 ATOM 2250 C CD . PRO A 1 281 ? 36.165 -13.738 -16.869 1.00 69.01 ? 281 PRO A CD 1 ATOM 2251 N N . MET A 1 282 ? 35.383 -9.996 -17.658 1.00 73.45 ? 282 MET A N 1 ATOM 2252 C CA . MET A 1 282 ? 35.292 -8.624 -18.167 1.00 78.07 ? 282 MET A CA 1 ATOM 2253 C C . MET A 1 282 ? 34.082 -8.351 -19.056 1.00 76.92 ? 282 MET A C 1 ATOM 2254 O O . MET A 1 282 ? 33.926 -7.236 -19.554 1.00 77.27 ? 282 MET A O 1 ATOM 2255 C CB . MET A 1 282 ? 36.585 -8.212 -18.871 1.00 82.97 ? 282 MET A CB 1 ATOM 2256 C CG . MET A 1 282 ? 37.003 -9.062 -20.051 1.00 87.07 ? 282 MET A CG 1 ATOM 2257 S SD . MET A 1 282 ? 38.635 -8.554 -20.639 1.00 98.47 ? 282 MET A SD 1 ATOM 2258 C CE . MET A 1 282 ? 39.600 -8.691 -19.130 1.00 96.54 ? 282 MET A CE 1 ATOM 2259 N N . GLY A 1 283 ? 33.209 -9.344 -19.220 1.00 74.22 ? 283 GLY A N 1 ATOM 2260 C CA . GLY A 1 283 ? 32.000 -9.165 -20.015 1.00 74.38 ? 283 GLY A CA 1 ATOM 2261 C C . GLY A 1 283 ? 31.512 -10.456 -20.630 1.00 73.56 ? 283 GLY A C 1 ATOM 2262 O O . GLY A 1 283 ? 32.249 -11.433 -20.689 1.00 71.40 ? 283 GLY A O 1 ATOM 2263 N N . ALA A 1 284 ? 30.266 -10.448 -21.093 1.00 75.59 ? 284 ALA A N 1 ATOM 2264 C CA . ALA A 1 284 ? 29.642 -11.628 -21.688 1.00 76.83 ? 284 ALA A CA 1 ATOM 2265 C C . ALA A 1 284 ? 29.877 -11.708 -23.198 1.00 77.42 ? 284 ALA A C 1 ATOM 2266 O O . ALA A 1 284 ? 30.130 -10.695 -23.853 1.00 75.68 ? 284 ALA A O 1 ATOM 2267 C CB . ALA A 1 284 ? 28.155 -11.627 -21.396 1.00 79.31 ? 284 ALA A CB 1 ATOM 2268 N N . ILE A 1 285 ? 29.765 -12.921 -23.738 1.00 78.23 ? 285 ILE A N 1 ATOM 2269 C CA . ILE A 1 285 ? 30.024 -13.190 -25.154 1.00 79.65 ? 285 ILE A CA 1 ATOM 2270 C C . ILE A 1 285 ? 28.792 -13.792 -25.819 1.00 82.24 ? 285 ILE A C 1 ATOM 2271 O O . ILE A 1 285 ? 28.210 -14.750 -25.316 1.00 83.82 ? 285 ILE A O 1 ATOM 2272 C CB . ILE A 1 285 ? 31.202 -14.180 -25.341 1.00 76.96 ? 285 ILE A CB 1 ATOM 2273 C CG1 . ILE A 1 285 ? 32.523 -13.527 -24.941 1.00 76.35 ? 285 ILE A CG1 1 ATOM 2274 C CG2 . ILE A 1 285 ? 31.290 -14.653 -26.783 1.00 76.30 ? 285 ILE A CG2 1 ATOM 2275 C CD1 . ILE A 1 285 ? 33.677 -14.502 -24.826 1.00 76.18 ? 285 ILE A CD1 1 ATOM 2276 N N . ASN A 1 286 ? 28.419 -13.231 -26.963 1.00 85.91 ? 286 ASN A N 1 ATOM 2277 C CA . ASN A 1 286 ? 27.326 -13.749 -27.772 1.00 92.95 ? 286 ASN A CA 1 ATOM 2278 C C . ASN A 1 286 ? 27.752 -13.802 -29.242 1.00 89.73 ? 286 ASN A C 1 ATOM 2279 O O . ASN A 1 286 ? 27.668 -12.809 -29.959 1.00 88.13 ? 286 ASN A O 1 ATOM 2280 C CB . ASN A 1 286 ? 26.081 -12.876 -27.579 1.00 101.40 ? 286 ASN A CB 1 ATOM 2281 C CG . ASN A 1 286 ? 25.006 -13.148 -28.611 1.00 112.95 ? 286 ASN A CG 1 ATOM 2282 O OD1 . ASN A 1 286 ? 24.612 -14.297 -28.825 1.00 110.30 ? 286 ASN A OD1 1 ATOM 2283 N ND2 . ASN A 1 286 ? 24.526 -12.083 -29.257 1.00 127.77 ? 286 ASN A ND2 1 ATOM 2284 N N . SER A 1 287 ? 28.241 -14.960 -29.675 1.00 88.33 ? 287 SER A N 1 ATOM 2285 C CA . SER A 1 287 ? 28.604 -15.157 -31.076 1.00 89.48 ? 287 SER A CA 1 ATOM 2286 C C . SER A 1 287 ? 28.656 -16.637 -31.453 1.00 89.52 ? 287 SER A C 1 ATOM 2287 O O . SER A 1 287 ? 28.604 -17.507 -30.587 1.00 86.77 ? 287 SER A O 1 ATOM 2288 C CB . SER A 1 287 ? 29.946 -14.474 -31.395 1.00 88.10 ? 287 SER A CB 1 ATOM 2289 O OG . SER A 1 287 ? 31.057 -15.245 -30.975 1.00 83.10 ? 287 SER A OG 1 ATOM 2290 N N . SER A 1 288 ? 28.755 -16.898 -32.756 1.00 91.53 ? 288 SER A N 1 ATOM 2291 C CA . SER A 1 288 ? 28.889 -18.257 -33.288 1.00 92.15 ? 288 SER A CA 1 ATOM 2292 C C . SER A 1 288 ? 30.324 -18.597 -33.692 1.00 86.00 ? 288 SER A C 1 ATOM 2293 O O . SER A 1 288 ? 30.568 -19.660 -34.260 1.00 84.78 ? 288 SER A O 1 ATOM 2294 C CB . SER A 1 288 ? 27.968 -18.441 -34.497 1.00 97.11 ? 288 SER A CB 1 ATOM 2295 O OG . SER A 1 288 ? 26.609 -18.445 -34.100 1.00 104.93 ? 288 SER A OG 1 ATOM 2296 N N . MET A 1 289 ? 31.270 -17.710 -33.396 1.00 81.76 ? 289 MET A N 1 ATOM 2297 C CA . MET A 1 289 ? 32.671 -17.954 -33.737 1.00 80.31 ? 289 MET A CA 1 ATOM 2298 C C . MET A 1 289 ? 33.190 -19.168 -32.971 1.00 78.36 ? 289 MET A C 1 ATOM 2299 O O . MET A 1 289 ? 32.778 -19.403 -31.841 1.00 80.27 ? 289 MET A O 1 ATOM 2300 C CB . MET A 1 289 ? 33.553 -16.757 -33.374 1.00 82.14 ? 289 MET A CB 1 ATOM 2301 C CG . MET A 1 289 ? 33.181 -15.434 -34.019 1.00 84.79 ? 289 MET A CG 1 ATOM 2302 S SD . MET A 1 289 ? 33.345 -15.428 -35.806 1.00 85.08 ? 289 MET A SD 1 ATOM 2303 C CE . MET A 1 289 ? 33.671 -13.682 -36.052 1.00 81.83 ? 289 MET A CE 1 ATOM 2304 N N . PRO A 1 290 ? 34.092 -19.948 -33.584 1.00 76.64 ? 290 PRO A N 1 ATOM 2305 C CA . PRO A 1 290 ? 34.700 -21.045 -32.838 1.00 75.38 ? 290 PRO A CA 1 ATOM 2306 C C . PRO A 1 290 ? 35.764 -20.594 -31.835 1.00 72.76 ? 290 PRO A C 1 ATOM 2307 O O . PRO A 1 290 ? 36.118 -21.371 -30.950 1.00 74.55 ? 290 PRO A O 1 ATOM 2308 C CB . PRO A 1 290 ? 35.334 -21.896 -33.938 1.00 74.88 ? 290 PRO A CB 1 ATOM 2309 C CG . PRO A 1 290 ? 35.639 -20.918 -35.016 1.00 74.02 ? 290 PRO A CG 1 ATOM 2310 C CD . PRO A 1 290 ? 34.463 -19.995 -35.011 1.00 74.02 ? 290 PRO A CD 1 ATOM 2311 N N . PHE A 1 291 ? 36.269 -19.366 -31.974 1.00 67.82 ? 291 PHE A N 1 ATOM 2312 C CA . PHE A 1 291 ? 37.315 -18.847 -31.089 1.00 66.59 ? 291 PHE A CA 1 ATOM 2313 C C . PHE A 1 291 ? 36.960 -17.475 -30.559 1.00 63.91 ? 291 PHE A C 1 ATOM 2314 O O . PHE A 1 291 ? 36.206 -16.749 -31.182 1.00 64.27 ? 291 PHE A O 1 ATOM 2315 C CB . PHE A 1 291 ? 38.642 -18.681 -31.838 1.00 67.13 ? 291 PHE A CB 1 ATOM 2316 C CG . PHE A 1 291 ? 39.264 -19.961 -32.288 1.00 68.64 ? 291 PHE A CG 1 ATOM 2317 C CD1 . PHE A 1 291 ? 39.806 -20.851 -31.366 1.00 71.90 ? 291 PHE A CD1 1 ATOM 2318 C CD2 . PHE A 1 291 ? 39.341 -20.268 -33.639 1.00 70.33 ? 291 PHE A CD2 1 ATOM 2319 C CE1 . PHE A 1 291 ? 40.397 -22.033 -31.785 1.00 72.78 ? 291 PHE A CE1 1 ATOM 2320 C CE2 . PHE A 1 291 ? 39.929 -21.450 -34.066 1.00 71.84 ? 291 PHE A CE2 1 ATOM 2321 C CZ . PHE A 1 291 ? 40.455 -22.330 -33.138 1.00 72.30 ? 291 PHE A CZ 1 ATOM 2322 N N . HIS A 1 292 ? 37.553 -17.109 -29.427 1.00 63.83 ? 292 HIS A N 1 ATOM 2323 C CA . HIS A 1 292 ? 37.555 -15.718 -28.964 1.00 62.91 ? 292 HIS A CA 1 ATOM 2324 C C . HIS A 1 292 ? 38.876 -15.413 -28.280 1.00 61.29 ? 292 HIS A C 1 ATOM 2325 O O . HIS A 1 292 ? 39.644 -16.330 -27.980 1.00 58.74 ? 292 HIS A O 1 ATOM 2326 C CB . HIS A 1 292 ? 36.408 -15.462 -27.987 1.00 65.11 ? 292 HIS A CB 1 ATOM 2327 C CG . HIS A 1 292 ? 36.565 -16.176 -26.681 1.00 66.91 ? 292 HIS A CG 1 ATOM 2328 N ND1 . HIS A 1 292 ? 37.077 -15.568 -25.558 1.00 66.04 ? 292 HIS A ND1 1 ATOM 2329 C CD2 . HIS A 1 292 ? 36.301 -17.456 -26.328 1.00 67.22 ? 292 HIS A CD2 1 ATOM 2330 C CE1 . HIS A 1 292 ? 37.108 -16.438 -24.565 1.00 67.38 ? 292 HIS A CE1 1 ATOM 2331 N NE2 . HIS A 1 292 ? 36.643 -17.591 -25.006 1.00 68.61 ? 292 HIS A NE2 1 ATOM 2332 N N . ASN A 1 293 ? 39.127 -14.127 -28.021 1.00 60.64 ? 293 ASN A N 1 ATOM 2333 C CA . ASN A 1 293 ? 40.343 -13.702 -27.319 1.00 60.38 ? 293 ASN A CA 1 ATOM 2334 C C . ASN A 1 293 ? 40.085 -12.744 -26.148 1.00 62.88 ? 293 ASN A C 1 ATOM 2335 O O . ASN A 1 293 ? 40.954 -11.952 -25.787 1.00 63.69 ? 293 ASN A O 1 ATOM 2336 C CB . ASN A 1 293 ? 41.310 -13.063 -28.313 1.00 61.01 ? 293 ASN A CB 1 ATOM 2337 C CG . ASN A 1 293 ? 40.820 -11.732 -28.841 1.00 60.41 ? 293 ASN A CG 1 ATOM 2338 O OD1 . ASN A 1 293 ? 39.702 -11.320 -28.576 1.00 61.47 ? 293 ASN A OD1 1 ATOM 2339 N ND2 . ASN A 1 293 ? 41.660 -11.059 -29.602 1.00 61.55 ? 293 ASN A ND2 1 ATOM 2340 N N . ILE A 1 294 ? 38.893 -12.820 -25.562 1.00 63.69 ? 294 ILE A N 1 ATOM 2341 C CA . ILE A 1 294 ? 38.502 -11.935 -24.463 1.00 66.09 ? 294 ILE A CA 1 ATOM 2342 C C . ILE A 1 294 ? 39.208 -12.256 -23.145 1.00 65.79 ? 294 ILE A C 1 ATOM 2343 O O . ILE A 1 294 ? 39.854 -11.392 -22.567 1.00 66.00 ? 294 ILE A O 1 ATOM 2344 C CB . ILE A 1 294 ? 36.966 -11.938 -24.251 1.00 67.84 ? 294 ILE A CB 1 ATOM 2345 C CG1 . ILE A 1 294 ? 36.279 -11.098 -25.330 1.00 68.78 ? 294 ILE A CG1 1 ATOM 2346 C CG2 . ILE A 1 294 ? 36.592 -11.376 -22.888 1.00 70.43 ? 294 ILE A CG2 1 ATOM 2347 C CD1 . ILE A 1 294 ? 35.809 -11.894 -26.515 1.00 69.66 ? 294 ILE A CD1 1 ATOM 2348 N N . HIS A 1 295 ? 39.067 -13.490 -22.671 1.00 66.23 ? 295 HIS A N 1 ATOM 2349 C CA . HIS A 1 295 ? 39.618 -13.892 -21.380 1.00 66.98 ? 295 HIS A CA 1 ATOM 2350 C C . HIS A 1 295 ? 39.568 -15.427 -21.250 1.00 66.65 ? 295 HIS A C 1 ATOM 2351 O O . HIS A 1 295 ? 38.604 -16.045 -21.695 1.00 65.02 ? 295 HIS A O 1 ATOM 2352 C CB . HIS A 1 295 ? 38.788 -13.237 -20.279 1.00 70.07 ? 295 HIS A CB 1 ATOM 2353 C CG . HIS A 1 295 ? 39.433 -13.259 -18.935 1.00 72.70 ? 295 HIS A CG 1 ATOM 2354 N ND1 . HIS A 1 295 ? 39.395 -14.363 -18.117 1.00 74.90 ? 295 HIS A ND1 1 ATOM 2355 C CD2 . HIS A 1 295 ? 40.112 -12.309 -18.254 1.00 75.71 ? 295 HIS A CD2 1 ATOM 2356 C CE1 . HIS A 1 295 ? 40.037 -14.100 -16.994 1.00 76.17 ? 295 HIS A CE1 1 ATOM 2357 N NE2 . HIS A 1 295 ? 40.480 -12.860 -17.051 1.00 76.12 ? 295 HIS A NE2 1 ATOM 2358 N N . PRO A 1 296 ? 40.597 -16.049 -20.643 1.00 68.26 ? 296 PRO A N 1 ATOM 2359 C CA . PRO A 1 296 ? 40.629 -17.517 -20.589 1.00 69.00 ? 296 PRO A CA 1 ATOM 2360 C C . PRO A 1 296 ? 39.620 -18.159 -19.634 1.00 71.92 ? 296 PRO A C 1 ATOM 2361 O O . PRO A 1 296 ? 39.162 -19.272 -19.891 1.00 71.50 ? 296 PRO A O 1 ATOM 2362 C CB . PRO A 1 296 ? 42.062 -17.826 -20.132 1.00 69.62 ? 296 PRO A CB 1 ATOM 2363 C CG . PRO A 1 296 ? 42.515 -16.609 -19.420 1.00 70.80 ? 296 PRO A CG 1 ATOM 2364 C CD . PRO A 1 296 ? 41.831 -15.454 -20.096 1.00 70.53 ? 296 PRO A CD 1 ATOM 2365 N N . LEU A 1 297 ? 39.307 -17.483 -18.531 1.00 74.08 ? 297 LEU A N 1 ATOM 2366 C CA . LEU A 1 297 ? 38.367 -18.007 -17.531 1.00 77.34 ? 297 LEU A CA 1 ATOM 2367 C C . LEU A 1 297 ? 36.911 -17.712 -17.888 1.00 76.38 ? 297 LEU A C 1 ATOM 2368 O O . LEU A 1 297 ? 36.392 -16.650 -17.572 1.00 79.07 ? 297 LEU A O 1 ATOM 2369 C CB . LEU A 1 297 ? 38.697 -17.442 -16.142 1.00 77.89 ? 297 LEU A CB 1 ATOM 2370 C CG . LEU A 1 297 ? 40.135 -17.681 -15.659 1.00 81.22 ? 297 LEU A CG 1 ATOM 2371 C CD1 . LEU A 1 297 ? 40.423 -16.928 -14.363 1.00 81.97 ? 297 LEU A CD1 1 ATOM 2372 C CD2 . LEU A 1 297 ? 40.419 -19.170 -15.491 1.00 83.56 ? 297 LEU A CD2 1 ATOM 2373 N N . THR A 1 298 ? 36.249 -18.655 -18.547 1.00 75.48 ? 298 THR A N 1 ATOM 2374 C CA . THR A 1 298 ? 34.849 -18.474 -18.911 1.00 74.28 ? 298 THR A CA 1 ATOM 2375 C C . THR A 1 298 ? 33.971 -19.552 -18.288 1.00 76.02 ? 298 THR A C 1 ATOM 2376 O O . THR A 1 298 ? 34.465 -20.557 -17.775 1.00 75.19 ? 298 THR A O 1 ATOM 2377 C CB . THR A 1 298 ? 34.647 -18.472 -20.439 1.00 72.87 ? 298 THR A CB 1 ATOM 2378 O OG1 . THR A 1 298 ? 34.785 -19.799 -20.952 1.00 74.91 ? 298 THR A OG1 1 ATOM 2379 C CG2 . THR A 1 298 ? 35.659 -17.577 -21.111 1.00 72.38 ? 298 THR A CG2 1 ATOM 2380 N N . ILE A 1 299 ? 32.663 -19.314 -18.331 1.00 77.24 ? 299 ILE A N 1 ATOM 2381 C CA . ILE A 1 299 ? 31.669 -20.282 -17.890 1.00 79.58 ? 299 ILE A CA 1 ATOM 2382 C C . ILE A 1 299 ? 30.511 -20.239 -18.872 1.00 81.34 ? 299 ILE A C 1 ATOM 2383 O O . ILE A 1 299 ? 30.169 -19.164 -19.370 1.00 79.53 ? 299 ILE A O 1 ATOM 2384 C CB . ILE A 1 299 ? 31.188 -19.995 -16.449 1.00 82.41 ? 299 ILE A CB 1 ATOM 2385 C CG1 . ILE A 1 299 ? 30.144 -21.023 -16.016 1.00 84.90 ? 299 ILE A CG1 1 ATOM 2386 C CG2 . ILE A 1 299 ? 30.623 -18.584 -16.311 1.00 82.28 ? 299 ILE A CG2 1 ATOM 2387 C CD1 . ILE A 1 299 ? 29.927 -21.062 -14.522 1.00 87.29 ? 299 ILE A CD1 1 ATOM 2388 N N . GLY A 1 300 ? 29.925 -21.406 -19.152 1.00 85.21 ? 300 GLY A N 1 ATOM 2389 C CA . GLY A 1 300 ? 28.850 -21.537 -20.134 1.00 88.14 ? 300 GLY A CA 1 ATOM 2390 C C . GLY A 1 300 ? 29.310 -22.209 -21.416 1.00 90.99 ? 300 GLY A C 1 ATOM 2391 O O . GLY A 1 300 ? 30.399 -22.775 -21.471 1.00 92.83 ? 300 GLY A O 1 ATOM 2392 N N . GLU A 1 301 ? 28.477 -22.146 -22.452 1.00 96.03 ? 301 GLU A N 1 ATOM 2393 C CA . GLU A 1 301 ? 28.822 -22.722 -23.752 1.00 99.83 ? 301 GLU A CA 1 ATOM 2394 C C . GLU A 1 301 ? 29.568 -21.647 -24.527 1.00 95.06 ? 301 GLU A C 1 ATOM 2395 O O . GLU A 1 301 ? 28.953 -20.748 -25.102 1.00 95.16 ? 301 GLU A O 1 ATOM 2396 C CB . GLU A 1 301 ? 27.570 -23.189 -24.512 1.00 107.36 ? 301 GLU A CB 1 ATOM 2397 C CG . GLU A 1 301 ? 27.659 -24.620 -25.033 1.00 114.19 ? 301 GLU A CG 1 ATOM 2398 C CD . GLU A 1 301 ? 27.472 -25.663 -23.933 1.00 121.67 ? 301 GLU A CD 1 ATOM 2399 O OE1 . GLU A 1 301 ? 26.381 -25.709 -23.317 1.00 122.49 ? 301 GLU A OE1 1 ATOM 2400 O OE2 . GLU A 1 301 ? 28.421 -26.438 -23.673 1.00 125.90 ? 301 GLU A OE2 1 ATOM 2401 N N . CYS A 1 302 ? 30.897 -21.738 -24.519 1.00 91.53 ? 302 CYS A N 1 ATOM 2402 C CA . CYS A 1 302 ? 31.753 -20.667 -25.020 1.00 86.40 ? 302 CYS A CA 1 ATOM 2403 C C . CYS A 1 302 ? 32.589 -21.080 -26.220 1.00 81.64 ? 302 CYS A C 1 ATOM 2404 O O . CYS A 1 302 ? 32.829 -22.266 -26.442 1.00 80.10 ? 302 CYS A O 1 ATOM 2405 C CB . CYS A 1 302 ? 32.698 -20.204 -23.914 1.00 88.56 ? 302 CYS A CB 1 ATOM 2406 S SG . CYS A 1 302 ? 31.893 -19.310 -22.566 1.00 94.42 ? 302 CYS A SG 1 ATOM 2407 N N . PRO A 1 303 ? 33.049 -20.093 -27.001 1.00 77.82 ? 303 PRO A N 1 ATOM 2408 C CA . PRO A 1 303 ? 34.090 -20.390 -27.977 1.00 76.02 ? 303 PRO A CA 1 ATOM 2409 C C . PRO A 1 303 ? 35.395 -20.700 -27.256 1.00 74.67 ? 303 PRO A C 1 ATOM 2410 O O . PRO A 1 303 ? 35.487 -20.492 -26.053 1.00 75.88 ? 303 PRO A O 1 ATOM 2411 C CB . PRO A 1 303 ? 34.205 -19.096 -28.799 1.00 74.23 ? 303 PRO A CB 1 ATOM 2412 C CG . PRO A 1 303 ? 33.027 -18.260 -28.427 1.00 75.00 ? 303 PRO A CG 1 ATOM 2413 C CD . PRO A 1 303 ? 32.612 -18.688 -27.060 1.00 76.22 ? 303 PRO A CD 1 ATOM 2414 N N . LYS A 1 304 ? 36.392 -21.193 -27.976 1.00 74.87 ? 304 LYS A N 1 ATOM 2415 C CA . LYS A 1 304 ? 37.668 -21.515 -27.360 1.00 76.16 ? 304 LYS A CA 1 ATOM 2416 C C . LYS A 1 304 ? 38.564 -20.296 -27.315 1.00 72.19 ? 304 LYS A C 1 ATOM 2417 O O . LYS A 1 304 ? 38.637 -19.528 -28.274 1.00 71.84 ? 304 LYS A O 1 ATOM 2418 C CB . LYS A 1 304 ? 38.355 -22.662 -28.096 1.00 81.23 ? 304 LYS A CB 1 ATOM 2419 C CG . LYS A 1 304 ? 37.644 -23.999 -27.918 1.00 89.68 ? 304 LYS A CG 1 ATOM 2420 C CD . LYS A 1 304 ? 37.636 -24.461 -26.456 1.00 95.68 ? 304 LYS A CD 1 ATOM 2421 C CE . LYS A 1 304 ? 36.884 -25.769 -26.263 1.00 99.30 ? 304 LYS A CE 1 ATOM 2422 N NZ . LYS A 1 304 ? 35.465 -25.673 -26.710 1.00 99.86 ? 304 LYS A NZ 1 ATOM 2423 N N . TYR A 1 305 ? 39.240 -20.119 -26.187 1.00 69.15 ? 305 TYR A N 1 ATOM 2424 C CA . TYR A 1 305 ? 40.089 -18.969 -25.997 1.00 67.78 ? 305 TYR A CA 1 ATOM 2425 C C . TYR A 1 305 ? 41.437 -19.192 -26.666 1.00 67.91 ? 305 TYR A C 1 ATOM 2426 O O . TYR A 1 305 ? 42.053 -20.243 -26.489 1.00 70.29 ? 305 TYR A O 1 ATOM 2427 C CB . TYR A 1 305 ? 40.288 -18.674 -24.508 1.00 67.92 ? 305 TYR A CB 1 ATOM 2428 C CG . TYR A 1 305 ? 41.210 -17.507 -24.265 1.00 65.98 ? 305 TYR A CG 1 ATOM 2429 C CD1 . TYR A 1 305 ? 40.755 -16.200 -24.393 1.00 64.51 ? 305 TYR A CD1 1 ATOM 2430 C CD2 . TYR A 1 305 ? 42.544 -17.708 -23.945 1.00 67.33 ? 305 TYR A CD2 1 ATOM 2431 C CE1 . TYR A 1 305 ? 41.603 -15.126 -24.189 1.00 65.09 ? 305 TYR A CE1 1 ATOM 2432 C CE2 . TYR A 1 305 ? 43.400 -16.639 -23.734 1.00 68.52 ? 305 TYR A CE2 1 ATOM 2433 C CZ . TYR A 1 305 ? 42.924 -15.350 -23.856 1.00 67.15 ? 305 TYR A CZ 1 ATOM 2434 O OH . TYR A 1 305 ? 43.769 -14.283 -23.652 1.00 68.12 ? 305 TYR A OH 1 ATOM 2435 N N . VAL A 1 306 ? 41.879 -18.193 -27.431 1.00 66.27 ? 306 VAL A N 1 ATOM 2436 C CA . VAL A 1 306 ? 43.248 -18.124 -27.945 1.00 65.43 ? 306 VAL A CA 1 ATOM 2437 C C . VAL A 1 306 ? 43.802 -16.724 -27.711 1.00 64.78 ? 306 VAL A C 1 ATOM 2438 O O . VAL A 1 306 ? 43.044 -15.777 -27.604 1.00 65.73 ? 306 VAL A O 1 ATOM 2439 C CB . VAL A 1 306 ? 43.321 -18.461 -29.448 1.00 65.29 ? 306 VAL A CB 1 ATOM 2440 C CG1 . VAL A 1 306 ? 42.845 -19.880 -29.695 1.00 67.34 ? 306 VAL A CG1 1 ATOM 2441 C CG2 . VAL A 1 306 ? 42.493 -17.491 -30.279 1.00 64.05 ? 306 VAL A CG2 1 ATOM 2442 N N . LYS A 1 307 ? 45.123 -16.599 -27.655 1.00 68.65 ? 307 LYS A N 1 ATOM 2443 C CA . LYS A 1 307 ? 45.787 -15.296 -27.505 1.00 71.96 ? 307 LYS A CA 1 ATOM 2444 C C . LYS A 1 307 ? 46.043 -14.540 -28.824 1.00 72.02 ? 307 LYS A C 1 ATOM 2445 O O . LYS A 1 307 ? 46.851 -13.620 -28.842 1.00 80.67 ? 307 LYS A O 1 ATOM 2446 C CB . LYS A 1 307 ? 47.113 -15.462 -26.743 1.00 74.05 ? 307 LYS A CB 1 ATOM 2447 C CG . LYS A 1 307 ? 46.921 -15.598 -25.247 1.00 76.89 ? 307 LYS A CG 1 ATOM 2448 C CD . LYS A 1 307 ? 48.084 -16.305 -24.571 1.00 81.85 ? 307 LYS A CD 1 ATOM 2449 C CE . LYS A 1 307 ? 49.199 -15.344 -24.209 1.00 86.09 ? 307 LYS A CE 1 ATOM 2450 N NZ . LYS A 1 307 ? 50.367 -16.074 -23.641 1.00 91.60 ? 307 LYS A NZ 1 ATOM 2451 N N . SER A 1 308 ? 45.364 -14.898 -29.913 1.00 68.49 ? 308 SER A N 1 ATOM 2452 C CA . SER A 1 308 ? 45.541 -14.195 -31.190 1.00 66.71 ? 308 SER A CA 1 ATOM 2453 C C . SER A 1 308 ? 44.823 -12.852 -31.205 1.00 66.28 ? 308 SER A C 1 ATOM 2454 O O . SER A 1 308 ? 43.843 -12.649 -30.489 1.00 66.82 ? 308 SER A O 1 ATOM 2455 C CB . SER A 1 308 ? 45.011 -15.025 -32.371 1.00 63.74 ? 308 SER A CB 1 ATOM 2456 O OG . SER A 1 308 ? 45.343 -16.389 -32.244 1.00 64.44 ? 308 SER A OG 1 ATOM 2457 N N . ASN A 1 309 ? 45.314 -11.956 -32.052 1.00 68.72 ? 309 ASN A N 1 ATOM 2458 C CA . ASN A 1 309 ? 44.613 -10.728 -32.402 1.00 71.93 ? 309 ASN A CA 1 ATOM 2459 C C . ASN A 1 309 ? 43.754 -10.887 -33.652 1.00 69.11 ? 309 ASN A C 1 ATOM 2460 O O . ASN A 1 309 ? 42.862 -10.074 -33.901 1.00 70.41 ? 309 ASN A O 1 ATOM 2461 C CB . ASN A 1 309 ? 45.623 -9.603 -32.633 1.00 77.84 ? 309 ASN A CB 1 ATOM 2462 C CG . ASN A 1 309 ? 46.269 -9.129 -31.345 1.00 84.95 ? 309 ASN A CG 1 ATOM 2463 O OD1 . ASN A 1 309 ? 45.594 -8.948 -30.321 1.00 86.32 ? 309 ASN A OD1 1 ATOM 2464 N ND2 . ASN A 1 309 ? 47.583 -8.915 -31.387 1.00 90.24 ? 309 ASN A ND2 1 ATOM 2465 N N . ARG A 1 310 ? 44.023 -11.937 -34.427 1.00 66.38 ? 310 ARG A N 1 ATOM 2466 C CA . ARG A 1 310 ? 43.435 -12.103 -35.751 1.00 66.46 ? 310 ARG A CA 1 ATOM 2467 C C . ARG A 1 310 ? 43.467 -13.570 -36.237 1.00 63.54 ? 310 ARG A C 1 ATOM 2468 O O . ARG A 1 310 ? 44.532 -14.187 -36.314 1.00 64.60 ? 310 ARG A O 1 ATOM 2469 C CB . ARG A 1 310 ? 44.202 -11.215 -36.734 1.00 69.93 ? 310 ARG A CB 1 ATOM 2470 C CG . ARG A 1 310 ? 43.499 -10.981 -38.055 1.00 74.08 ? 310 ARG A CG 1 ATOM 2471 C CD . ARG A 1 310 ? 44.312 -10.081 -38.968 1.00 79.25 ? 310 ARG A CD 1 ATOM 2472 N NE . ARG A 1 310 ? 43.936 -10.276 -40.369 1.00 85.63 ? 310 ARG A NE 1 ATOM 2473 C CZ . ARG A 1 310 ? 42.856 -9.754 -40.951 1.00 88.23 ? 310 ARG A CZ 1 ATOM 2474 N NH1 . ARG A 1 310 ? 42.012 -8.984 -40.269 1.00 91.77 ? 310 ARG A NH1 1 ATOM 2475 N NH2 . ARG A 1 310 ? 42.618 -10.003 -42.231 1.00 89.27 ? 310 ARG A NH2 1 ATOM 2476 N N . LEU A 1 311 ? 42.301 -14.128 -36.543 1.00 60.02 ? 311 LEU A N 1 ATOM 2477 C CA . LEU A 1 311 ? 42.218 -15.418 -37.240 1.00 61.28 ? 311 LEU A CA 1 ATOM 2478 C C . LEU A 1 311 ? 41.196 -15.311 -38.369 1.00 59.09 ? 311 LEU A C 1 ATOM 2479 O O . LEU A 1 311 ? 39.988 -15.253 -38.122 1.00 59.19 ? 311 LEU A O 1 ATOM 2480 C CB . LEU A 1 311 ? 41.835 -16.569 -36.299 1.00 60.76 ? 311 LEU A CB 1 ATOM 2481 C CG . LEU A 1 311 ? 42.821 -16.926 -35.191 1.00 61.83 ? 311 LEU A CG 1 ATOM 2482 C CD1 . LEU A 1 311 ? 42.187 -17.892 -34.214 1.00 62.27 ? 311 LEU A CD1 1 ATOM 2483 C CD2 . LEU A 1 311 ? 44.096 -17.527 -35.751 1.00 63.91 ? 311 LEU A CD2 1 ATOM 2484 N N . VAL A 1 312 ? 41.696 -15.288 -39.602 1.00 57.38 ? 312 VAL A N 1 ATOM 2485 C CA . VAL A 1 312 ? 40.855 -15.152 -40.787 1.00 56.12 ? 312 VAL A CA 1 ATOM 2486 C C . VAL A 1 312 ? 41.220 -16.204 -41.823 1.00 54.21 ? 312 VAL A C 1 ATOM 2487 O O . VAL A 1 312 ? 42.359 -16.242 -42.275 1.00 51.65 ? 312 VAL A O 1 ATOM 2488 C CB . VAL A 1 312 ? 41.018 -13.761 -41.414 1.00 56.30 ? 312 VAL A CB 1 ATOM 2489 C CG1 . VAL A 1 312 ? 40.169 -13.648 -42.670 1.00 56.99 ? 312 VAL A CG1 1 ATOM 2490 C CG2 . VAL A 1 312 ? 40.665 -12.689 -40.391 1.00 56.30 ? 312 VAL A CG2 1 ATOM 2491 N N . LEU A 1 313 ? 40.245 -17.052 -42.169 1.00 54.14 ? 313 LEU A N 1 ATOM 2492 C CA . LEU A 1 313 ? 40.400 -18.098 -43.185 1.00 54.37 ? 313 LEU A CA 1 ATOM 2493 C C . LEU A 1 313 ? 40.011 -17.584 -44.557 1.00 54.92 ? 313 LEU A C 1 ATOM 2494 O O . LEU A 1 313 ? 38.963 -16.954 -44.709 1.00 55.86 ? 313 LEU A O 1 ATOM 2495 C CB . LEU A 1 313 ? 39.484 -19.293 -42.903 1.00 54.61 ? 313 LEU A CB 1 ATOM 2496 C CG . LEU A 1 313 ? 39.812 -20.269 -41.783 1.00 56.40 ? 313 LEU A CG 1 ATOM 2497 C CD1 . LEU A 1 313 ? 38.604 -21.152 -41.523 1.00 56.67 ? 313 LEU A CD1 1 ATOM 2498 C CD2 . LEU A 1 313 ? 41.018 -21.128 -42.139 1.00 58.32 ? 313 LEU A CD2 1 ATOM 2499 N N . ALA A 1 314 ? 40.839 -17.884 -45.555 1.00 54.23 ? 314 ALA A N 1 ATOM 2500 C CA . ALA A 1 314 ? 40.470 -17.674 -46.947 1.00 54.11 ? 314 ALA A CA 1 ATOM 2501 C C . ALA A 1 314 ? 39.408 -18.688 -47.318 1.00 55.23 ? 314 ALA A C 1 ATOM 2502 O O . ALA A 1 314 ? 39.513 -19.864 -46.953 1.00 55.07 ? 314 ALA A O 1 ATOM 2503 C CB . ALA A 1 314 ? 41.681 -17.846 -47.852 1.00 55.08 ? 314 ALA A CB 1 ATOM 2504 N N . THR A 1 315 ? 38.378 -18.223 -48.019 1.00 55.89 ? 315 THR A N 1 ATOM 2505 C CA . THR A 1 315 ? 37.396 -19.101 -48.658 1.00 56.71 ? 315 THR A CA 1 ATOM 2506 C C . THR A 1 315 ? 37.484 -18.926 -50.167 1.00 55.36 ? 315 THR A C 1 ATOM 2507 O O . THR A 1 315 ? 37.517 -19.892 -50.924 1.00 54.61 ? 315 THR A O 1 ATOM 2508 C CB . THR A 1 315 ? 35.965 -18.759 -48.214 1.00 58.63 ? 315 THR A CB 1 ATOM 2509 O OG1 . THR A 1 315 ? 35.823 -17.334 -48.153 1.00 59.87 ? 315 THR A OG1 1 ATOM 2510 C CG2 . THR A 1 315 ? 35.667 -19.353 -46.844 1.00 58.68 ? 315 THR A CG2 1 ATOM 2511 N N . GLY A 1 316 ? 37.523 -17.677 -50.600 1.00 54.33 ? 316 GLY A N 1 ATOM 2512 C CA . GLY A 1 316 ? 37.642 -17.374 -52.006 1.00 53.88 ? 316 GLY A CA 1 ATOM 2513 C C . GLY A 1 316 ? 39.078 -17.394 -52.464 1.00 52.77 ? 316 GLY A C 1 ATOM 2514 O O . GLY A 1 316 ? 39.948 -17.971 -51.810 1.00 50.55 ? 316 GLY A O 1 ATOM 2515 N N . LEU A 1 317 ? 39.324 -16.729 -53.581 1.00 53.87 ? 317 LEU A N 1 ATOM 2516 C CA . LEU A 1 317 ? 40.607 -16.803 -54.249 1.00 56.26 ? 317 LEU A CA 1 ATOM 2517 C C . LEU A 1 317 ? 41.272 -15.430 -54.304 1.00 56.20 ? 317 LEU A C 1 ATOM 2518 O O . LEU A 1 317 ? 40.664 -14.423 -53.967 1.00 55.60 ? 317 LEU A O 1 ATOM 2519 C CB . LEU A 1 317 ? 40.445 -17.426 -55.646 1.00 57.54 ? 317 LEU A CB 1 ATOM 2520 C CG . LEU A 1 317 ? 39.360 -16.883 -56.572 1.00 58.00 ? 317 LEU A CG 1 ATOM 2521 C CD1 . LEU A 1 317 ? 39.770 -15.515 -57.067 1.00 61.22 ? 317 LEU A CD1 1 ATOM 2522 C CD2 . LEU A 1 317 ? 39.140 -17.805 -57.755 1.00 58.07 ? 317 LEU A CD2 1 ATOM 2523 N N . ARG A 1 318 ? 42.531 -15.424 -54.716 1.00 55.80 ? 318 ARG A N 1 ATOM 2524 C CA . ARG A 1 318 ? 43.349 -14.223 -54.770 1.00 58.03 ? 318 ARG A CA 1 ATOM 2525 C C . ARG A 1 318 ? 42.715 -13.195 -55.684 1.00 59.01 ? 318 ARG A C 1 ATOM 2526 O O . ARG A 1 318 ? 42.548 -13.431 -56.881 1.00 58.34 ? 318 ARG A O 1 ATOM 2527 C CB . ARG A 1 318 ? 44.756 -14.578 -55.266 1.00 60.53 ? 318 ARG A CB 1 ATOM 2528 C CG . ARG A 1 318 ? 45.729 -13.416 -55.310 1.00 65.39 ? 318 ARG A CG 1 ATOM 2529 C CD . ARG A 1 318 ? 47.056 -13.848 -55.901 1.00 68.88 ? 318 ARG A CD 1 ATOM 2530 N NE . ARG A 1 318 ? 47.814 -14.672 -54.963 1.00 71.22 ? 318 ARG A NE 1 ATOM 2531 C CZ . ARG A 1 318 ? 48.697 -14.205 -54.081 1.00 73.74 ? 318 ARG A CZ 1 ATOM 2532 N NH1 . ARG A 1 318 ? 48.958 -12.901 -53.999 1.00 74.80 ? 318 ARG A NH1 1 ATOM 2533 N NH2 . ARG A 1 318 ? 49.333 -15.055 -53.278 1.00 75.10 ? 318 ARG A NH2 1 ATOM 2534 N N . ASN A 1 319 ? 42.378 -12.050 -55.104 1.00 62.84 ? 319 ASN A N 1 ATOM 2535 C CA . ASN A 1 319 ? 41.651 -10.994 -55.795 1.00 65.70 ? 319 ASN A CA 1 ATOM 2536 C C . ASN A 1 319 ? 42.597 -10.108 -56.584 1.00 73.55 ? 319 ASN A C 1 ATOM 2537 O O . ASN A 1 319 ? 43.717 -9.837 -56.152 1.00 76.89 ? 319 ASN A O 1 ATOM 2538 C CB . ASN A 1 319 ? 40.870 -10.155 -54.786 1.00 64.06 ? 319 ASN A CB 1 ATOM 2539 C CG . ASN A 1 319 ? 39.737 -9.373 -55.417 1.00 64.12 ? 319 ASN A CG 1 ATOM 2540 O OD1 . ASN A 1 319 ? 39.422 -9.532 -56.591 1.00 61.86 ? 319 ASN A OD1 1 ATOM 2541 N ND2 . ASN A 1 319 ? 39.116 -8.513 -54.625 1.00 65.80 ? 319 ASN A ND2 1 ATOM 2542 N N . SER A 1 320 ? 42.130 -9.662 -57.746 1.00 83.84 ? 320 SER A N 1 ATOM 2543 C CA . SER A 1 320 ? 42.944 -8.891 -58.686 1.00 90.91 ? 320 SER A CA 1 ATOM 2544 C C . SER A 1 320 ? 42.811 -7.388 -58.424 1.00 95.63 ? 320 SER A C 1 ATOM 2545 O O . SER A 1 320 ? 41.738 -6.934 -58.024 1.00 93.28 ? 320 SER A O 1 ATOM 2546 C CB . SER A 1 320 ? 42.507 -9.208 -60.119 1.00 89.81 ? 320 SER A CB 1 ATOM 2547 O OG . SER A 1 320 ? 42.389 -10.607 -60.292 1.00 87.17 ? 320 SER A OG 1 ATOM 2548 N N . PRO A 1 321 ? 43.901 -6.619 -58.647 1.00 104.30 ? 321 PRO A N 1 ATOM 2549 C CA . PRO A 1 321 ? 43.892 -5.156 -58.506 1.00 110.53 ? 321 PRO A CA 1 ATOM 2550 C C . PRO A 1 321 ? 43.491 -4.425 -59.789 1.00 112.28 ? 321 PRO A C 1 ATOM 2551 O O . PRO A 1 321 ? 42.653 -4.913 -60.546 1.00 110.73 ? 321 PRO A O 1 ATOM 2552 C CB . PRO A 1 321 ? 45.348 -4.840 -58.161 1.00 111.91 ? 321 PRO A CB 1 ATOM 2553 C CG . PRO A 1 321 ? 46.123 -5.880 -58.895 1.00 111.31 ? 321 PRO A CG 1 ATOM 2554 C CD . PRO A 1 321 ? 45.262 -7.121 -58.929 1.00 107.14 ? 321 PRO A CD 1 ATOM 2555 N N . GLY B 2 1 ? 51.006 -18.668 -57.967 1.00 60.30 ? 1 GLY B N 1 ATOM 2556 C CA . GLY B 2 1 ? 50.571 -19.913 -57.277 1.00 57.07 ? 1 GLY B CA 1 ATOM 2557 C C . GLY B 2 1 ? 51.205 -21.168 -57.850 1.00 55.26 ? 1 GLY B C 1 ATOM 2558 O O . GLY B 2 1 ? 51.764 -21.165 -58.948 1.00 55.69 ? 1 GLY B O 1 ATOM 2559 N N . LEU B 2 2 ? 51.081 -22.259 -57.115 1.00 53.07 ? 2 LEU B N 1 ATOM 2560 C CA . LEU B 2 2 ? 51.756 -23.478 -57.490 1.00 53.32 ? 2 LEU B CA 1 ATOM 2561 C C . LEU B 2 2 ? 51.354 -23.980 -58.877 1.00 53.17 ? 2 LEU B C 1 ATOM 2562 O O . LEU B 2 2 ? 52.180 -24.581 -59.568 1.00 53.02 ? 2 LEU B O 1 ATOM 2563 C CB . LEU B 2 2 ? 51.482 -24.560 -56.465 1.00 52.30 ? 2 LEU B CB 1 ATOM 2564 C CG . LEU B 2 2 ? 52.108 -24.375 -55.105 1.00 52.11 ? 2 LEU B CG 1 ATOM 2565 C CD1 . LEU B 2 2 ? 51.649 -25.522 -54.224 1.00 51.40 ? 2 LEU B CD1 1 ATOM 2566 C CD2 . LEU B 2 2 ? 53.627 -24.323 -55.207 1.00 54.62 ? 2 LEU B CD2 1 ATOM 2567 N N . PHE B 2 3 ? 50.109 -23.719 -59.283 1.00 50.88 ? 3 PHE B N 1 ATOM 2568 C CA . PHE B 2 3 ? 49.560 -24.315 -60.512 1.00 51.85 ? 3 PHE B CA 1 ATOM 2569 C C . PHE B 2 3 ? 49.608 -23.421 -61.730 1.00 53.32 ? 3 PHE B C 1 ATOM 2570 O O . PHE B 2 3 ? 49.246 -23.853 -62.822 1.00 54.97 ? 3 PHE B O 1 ATOM 2571 C CB . PHE B 2 3 ? 48.148 -24.868 -60.257 1.00 50.68 ? 3 PHE B CB 1 ATOM 2572 C CG . PHE B 2 3 ? 48.160 -26.002 -59.283 1.00 50.08 ? 3 PHE B CG 1 ATOM 2573 C CD1 . PHE B 2 3 ? 48.368 -27.291 -59.716 1.00 50.22 ? 3 PHE B CD1 1 ATOM 2574 C CD2 . PHE B 2 3 ? 48.075 -25.757 -57.920 1.00 50.33 ? 3 PHE B CD2 1 ATOM 2575 C CE1 . PHE B 2 3 ? 48.450 -28.329 -58.811 1.00 51.70 ? 3 PHE B CE1 1 ATOM 2576 C CE2 . PHE B 2 3 ? 48.164 -26.790 -57.006 1.00 50.45 ? 3 PHE B CE2 1 ATOM 2577 C CZ . PHE B 2 3 ? 48.351 -28.076 -57.452 1.00 50.87 ? 3 PHE B CZ 1 ATOM 2578 N N . GLY B 2 4 ? 50.079 -22.188 -61.544 1.00 54.82 ? 4 GLY B N 1 ATOM 2579 C CA . GLY B 2 4 ? 50.441 -21.317 -62.649 1.00 55.46 ? 4 GLY B CA 1 ATOM 2580 C C . GLY B 2 4 ? 49.305 -20.572 -63.318 1.00 55.40 ? 4 GLY B C 1 ATOM 2581 O O . GLY B 2 4 ? 49.552 -19.708 -64.165 1.00 59.07 ? 4 GLY B O 1 ATOM 2582 N N . ALA B 2 5 ? 48.060 -20.877 -62.964 1.00 53.06 ? 5 ALA B N 1 ATOM 2583 C CA . ALA B 2 5 ? 46.927 -20.260 -63.649 1.00 52.29 ? 5 ALA B CA 1 ATOM 2584 C C . ALA B 2 5 ? 46.604 -18.879 -63.088 1.00 52.42 ? 5 ALA B C 1 ATOM 2585 O O . ALA B 2 5 ? 46.772 -17.883 -63.781 1.00 54.14 ? 5 ALA B O 1 ATOM 2586 C CB . ALA B 2 5 ? 45.704 -21.167 -63.594 1.00 51.94 ? 5 ALA B CB 1 ATOM 2587 N N . ILE B 2 6 ? 46.156 -18.822 -61.836 1.00 51.99 ? 6 ILE B N 1 ATOM 2588 C CA . ILE B 2 6 ? 45.699 -17.566 -61.230 1.00 53.58 ? 6 ILE B CA 1 ATOM 2589 C C . ILE B 2 6 ? 46.860 -16.583 -61.046 1.00 55.24 ? 6 ILE B C 1 ATOM 2590 O O . ILE B 2 6 ? 47.874 -16.914 -60.447 1.00 54.51 ? 6 ILE B O 1 ATOM 2591 C CB . ILE B 2 6 ? 45.008 -17.820 -59.872 1.00 53.29 ? 6 ILE B CB 1 ATOM 2592 C CG1 . ILE B 2 6 ? 43.684 -18.546 -60.094 1.00 51.97 ? 6 ILE B CG1 1 ATOM 2593 C CG2 . ILE B 2 6 ? 44.783 -16.511 -59.115 1.00 54.02 ? 6 ILE B CG2 1 ATOM 2594 C CD1 . ILE B 2 6 ? 43.031 -19.044 -58.826 1.00 51.91 ? 6 ILE B CD1 1 ATOM 2595 N N . ALA B 2 7 ? 46.698 -15.370 -61.567 1.00 57.47 ? 7 ALA B N 1 ATOM 2596 C CA . ALA B 2 7 ? 47.786 -14.388 -61.603 1.00 59.79 ? 7 ALA B CA 1 ATOM 2597 C C . ALA B 2 7 ? 49.074 -15.028 -62.124 1.00 61.14 ? 7 ALA B C 1 ATOM 2598 O O . ALA B 2 7 ? 50.154 -14.778 -61.606 1.00 62.39 ? 7 ALA B O 1 ATOM 2599 C CB . ALA B 2 7 ? 48.001 -13.785 -60.222 1.00 60.00 ? 7 ALA B CB 1 ATOM 2600 N N . GLY B 2 8 ? 48.930 -15.892 -63.125 1.00 62.00 ? 8 GLY B N 1 ATOM 2601 C CA . GLY B 2 8 ? 50.055 -16.498 -63.830 1.00 63.10 ? 8 GLY B CA 1 ATOM 2602 C C . GLY B 2 8 ? 49.849 -16.276 -65.318 1.00 64.37 ? 8 GLY B C 1 ATOM 2603 O O . GLY B 2 8 ? 49.994 -15.156 -65.797 1.00 66.94 ? 8 GLY B O 1 ATOM 2604 N N . PHE B 2 9 ? 49.481 -17.324 -66.051 1.00 62.67 ? 9 PHE B N 1 ATOM 2605 C CA . PHE B 2 9 ? 49.205 -17.168 -67.471 1.00 63.77 ? 9 PHE B CA 1 ATOM 2606 C C . PHE B 2 9 ? 47.811 -16.552 -67.688 1.00 63.14 ? 9 PHE B C 1 ATOM 2607 O O . PHE B 2 9 ? 47.498 -16.068 -68.772 1.00 64.09 ? 9 PHE B O 1 ATOM 2608 C CB . PHE B 2 9 ? 49.436 -18.478 -68.253 1.00 64.04 ? 9 PHE B CB 1 ATOM 2609 C CG . PHE B 2 9 ? 48.407 -19.551 -68.015 1.00 62.24 ? 9 PHE B CG 1 ATOM 2610 C CD1 . PHE B 2 9 ? 47.216 -19.554 -68.716 1.00 62.07 ? 9 PHE B CD1 1 ATOM 2611 C CD2 . PHE B 2 9 ? 48.659 -20.591 -67.132 1.00 61.93 ? 9 PHE B CD2 1 ATOM 2612 C CE1 . PHE B 2 9 ? 46.264 -20.548 -68.505 1.00 62.42 ? 9 PHE B CE1 1 ATOM 2613 C CE2 . PHE B 2 9 ? 47.725 -21.595 -66.924 1.00 60.91 ? 9 PHE B CE2 1 ATOM 2614 C CZ . PHE B 2 9 ? 46.523 -21.571 -67.608 1.00 61.36 ? 9 PHE B CZ 1 ATOM 2615 N N . ILE B 2 10 ? 46.982 -16.559 -66.652 1.00 61.71 ? 10 ILE B N 1 ATOM 2616 C CA . ILE B 2 10 ? 45.766 -15.758 -66.653 1.00 63.25 ? 10 ILE B CA 1 ATOM 2617 C C . ILE B 2 10 ? 46.038 -14.564 -65.741 1.00 66.40 ? 10 ILE B C 1 ATOM 2618 O O . ILE B 2 10 ? 46.071 -14.702 -64.517 1.00 67.52 ? 10 ILE B O 1 ATOM 2619 C CB . ILE B 2 10 ? 44.543 -16.568 -66.195 1.00 60.01 ? 10 ILE B CB 1 ATOM 2620 C CG1 . ILE B 2 10 ? 44.451 -17.867 -66.991 1.00 59.28 ? 10 ILE B CG1 1 ATOM 2621 C CG2 . ILE B 2 10 ? 43.275 -15.762 -66.406 1.00 60.34 ? 10 ILE B CG2 1 ATOM 2622 C CD1 . ILE B 2 10 ? 43.378 -18.811 -66.507 1.00 58.28 ? 10 ILE B CD1 1 ATOM 2623 N N . GLU B 2 11 ? 46.268 -13.404 -66.353 1.00 70.32 ? 11 GLU B N 1 ATOM 2624 C CA . GLU B 2 11 ? 46.811 -12.236 -65.647 1.00 74.23 ? 11 GLU B CA 1 ATOM 2625 C C . GLU B 2 11 ? 45.963 -11.781 -64.466 1.00 71.24 ? 11 GLU B C 1 ATOM 2626 O O . GLU B 2 11 ? 46.495 -11.412 -63.419 1.00 71.45 ? 11 GLU B O 1 ATOM 2627 C CB . GLU B 2 11 ? 47.007 -11.052 -66.605 1.00 81.02 ? 11 GLU B CB 1 ATOM 2628 C CG . GLU B 2 11 ? 48.459 -10.744 -66.953 1.00 88.11 ? 11 GLU B CG 1 ATOM 2629 C CD . GLU B 2 11 ? 48.693 -9.256 -67.213 1.00 96.28 ? 11 GLU B CD 1 ATOM 2630 O OE1 . GLU B 2 11 ? 47.883 -8.631 -67.945 1.00 99.14 ? 11 GLU B OE1 1 ATOM 2631 O OE2 . GLU B 2 11 ? 49.687 -8.710 -66.674 1.00 99.89 ? 11 GLU B OE2 1 ATOM 2632 N N . GLY B 2 12 ? 44.649 -11.800 -64.640 1.00 68.61 ? 12 GLY B N 1 ATOM 2633 C CA . GLY B 2 12 ? 43.741 -11.335 -63.598 1.00 68.10 ? 12 GLY B CA 1 ATOM 2634 C C . GLY B 2 12 ? 42.337 -11.886 -63.720 1.00 65.39 ? 12 GLY B C 1 ATOM 2635 O O . GLY B 2 12 ? 41.942 -12.393 -64.770 1.00 65.15 ? 12 GLY B O 1 ATOM 2636 N N . GLY B 2 13 ? 41.586 -11.784 -62.632 1.00 64.14 ? 13 GLY B N 1 ATOM 2637 C CA . GLY B 2 13 ? 40.201 -12.229 -62.595 1.00 63.25 ? 13 GLY B CA 1 ATOM 2638 C C . GLY B 2 13 ? 39.252 -11.286 -63.318 1.00 63.67 ? 13 GLY B C 1 ATOM 2639 O O . GLY B 2 13 ? 39.678 -10.288 -63.888 1.00 65.42 ? 13 GLY B O 1 ATOM 2640 N N . TRP B 2 14 ? 37.965 -11.627 -63.286 1.00 62.80 ? 14 TRP B N 1 ATOM 2641 C CA . TRP B 2 14 ? 36.921 -10.934 -64.031 1.00 63.94 ? 14 TRP B CA 1 ATOM 2642 C C . TRP B 2 14 ? 35.861 -10.370 -63.096 1.00 66.65 ? 14 TRP B C 1 ATOM 2643 O O . TRP B 2 14 ? 35.095 -11.117 -62.493 1.00 64.35 ? 14 TRP B O 1 ATOM 2644 C CB . TRP B 2 14 ? 36.235 -11.895 -65.009 1.00 61.90 ? 14 TRP B CB 1 ATOM 2645 C CG . TRP B 2 14 ? 37.089 -12.346 -66.149 1.00 60.48 ? 14 TRP B CG 1 ATOM 2646 C CD1 . TRP B 2 14 ? 38.121 -11.665 -66.721 1.00 61.06 ? 14 TRP B CD1 1 ATOM 2647 C CD2 . TRP B 2 14 ? 36.957 -13.567 -66.893 1.00 58.58 ? 14 TRP B CD2 1 ATOM 2648 N NE1 . TRP B 2 14 ? 38.648 -12.387 -67.762 1.00 59.61 ? 14 TRP B NE1 1 ATOM 2649 C CE2 . TRP B 2 14 ? 37.949 -13.557 -67.892 1.00 58.38 ? 14 TRP B CE2 1 ATOM 2650 C CE3 . TRP B 2 14 ? 36.098 -14.667 -66.809 1.00 57.17 ? 14 TRP B CE3 1 ATOM 2651 C CZ2 . TRP B 2 14 ? 38.119 -14.613 -68.789 1.00 57.46 ? 14 TRP B CZ2 1 ATOM 2652 C CZ3 . TRP B 2 14 ? 36.261 -15.708 -67.707 1.00 55.86 ? 14 TRP B CZ3 1 ATOM 2653 C CH2 . TRP B 2 14 ? 37.265 -15.676 -68.681 1.00 56.30 ? 14 TRP B CH2 1 ATOM 2654 N N . GLN B 2 15 ? 35.807 -9.044 -62.997 1.00 72.22 ? 15 GLN B N 1 ATOM 2655 C CA . GLN B 2 15 ? 34.713 -8.368 -62.295 1.00 76.45 ? 15 GLN B CA 1 ATOM 2656 C C . GLN B 2 15 ? 33.377 -8.767 -62.918 1.00 76.16 ? 15 GLN B C 1 ATOM 2657 O O . GLN B 2 15 ? 32.370 -8.852 -62.225 1.00 78.25 ? 15 GLN B O 1 ATOM 2658 C CB . GLN B 2 15 ? 34.864 -6.842 -62.366 1.00 80.71 ? 15 GLN B CB 1 ATOM 2659 C CG . GLN B 2 15 ? 36.120 -6.271 -61.716 1.00 83.34 ? 15 GLN B CG 1 ATOM 2660 C CD . GLN B 2 15 ? 36.049 -6.226 -60.201 1.00 85.42 ? 15 GLN B CD 1 ATOM 2661 O OE1 . GLN B 2 15 ? 36.907 -6.783 -59.516 1.00 86.84 ? 15 GLN B OE1 1 ATOM 2662 N NE2 . GLN B 2 15 ? 35.026 -5.563 -59.669 1.00 88.67 ? 15 GLN B NE2 1 ATOM 2663 N N . GLY B 2 16 ? 33.384 -9.013 -64.226 1.00 75.77 ? 16 GLY B N 1 ATOM 2664 C CA . GLY B 2 16 ? 32.168 -9.320 -64.974 1.00 77.30 ? 16 GLY B CA 1 ATOM 2665 C C . GLY B 2 16 ? 31.531 -10.680 -64.732 1.00 76.95 ? 16 GLY B C 1 ATOM 2666 O O . GLY B 2 16 ? 30.367 -10.882 -65.082 1.00 78.64 ? 16 GLY B O 1 ATOM 2667 N N . MET B 2 17 ? 32.277 -11.619 -64.152 1.00 74.66 ? 17 MET B N 1 ATOM 2668 C CA . MET B 2 17 ? 31.735 -12.943 -63.871 1.00 75.14 ? 17 MET B CA 1 ATOM 2669 C C . MET B 2 17 ? 31.258 -13.039 -62.426 1.00 76.17 ? 17 MET B C 1 ATOM 2670 O O . MET B 2 17 ? 32.049 -13.204 -61.495 1.00 74.82 ? 17 MET B O 1 ATOM 2671 C CB . MET B 2 17 ? 32.762 -14.031 -64.149 1.00 75.69 ? 17 MET B CB 1 ATOM 2672 C CG . MET B 2 17 ? 32.140 -15.412 -64.098 1.00 76.47 ? 17 MET B CG 1 ATOM 2673 S SD . MET B 2 17 ? 33.291 -16.664 -64.623 1.00 75.85 ? 17 MET B SD 1 ATOM 2674 C CE . MET B 2 17 ? 34.585 -16.368 -63.423 1.00 77.62 ? 17 MET B CE 1 ATOM 2675 N N . VAL B 2 18 ? 29.945 -12.980 -62.265 1.00 78.71 ? 18 VAL B N 1 ATOM 2676 C CA . VAL B 2 18 ? 29.315 -12.732 -60.977 1.00 81.09 ? 18 VAL B CA 1 ATOM 2677 C C . VAL B 2 18 ? 28.784 -14.008 -60.329 1.00 80.57 ? 18 VAL B C 1 ATOM 2678 O O . VAL B 2 18 ? 28.685 -14.090 -59.108 1.00 80.74 ? 18 VAL B O 1 ATOM 2679 C CB . VAL B 2 18 ? 28.170 -11.716 -61.173 1.00 85.91 ? 18 VAL B CB 1 ATOM 2680 C CG1 . VAL B 2 18 ? 27.190 -11.730 -60.011 1.00 90.57 ? 18 VAL B CG1 1 ATOM 2681 C CG2 . VAL B 2 18 ? 28.748 -10.322 -61.381 1.00 86.88 ? 18 VAL B CG2 1 ATOM 2682 N N . ASP B 2 19 ? 28.473 -15.005 -61.149 1.00 80.27 ? 19 ASP B N 1 ATOM 2683 C CA . ASP B 2 19 ? 27.692 -16.165 -60.712 1.00 80.99 ? 19 ASP B CA 1 ATOM 2684 C C . ASP B 2 19 ? 28.531 -17.434 -60.523 1.00 76.68 ? 19 ASP B C 1 ATOM 2685 O O . ASP B 2 19 ? 27.997 -18.536 -60.513 1.00 79.48 ? 19 ASP B O 1 ATOM 2686 C CB . ASP B 2 19 ? 26.553 -16.419 -61.717 1.00 84.53 ? 19 ASP B CB 1 ATOM 2687 C CG . ASP B 2 19 ? 27.039 -16.486 -63.167 1.00 85.53 ? 19 ASP B CG 1 ATOM 2688 O OD1 . ASP B 2 19 ? 28.260 -16.320 -63.419 1.00 82.16 ? 19 ASP B OD1 1 ATOM 2689 O OD2 . ASP B 2 19 ? 26.190 -16.697 -64.061 1.00 89.24 ? 19 ASP B OD2 1 ATOM 2690 N N . GLY B 2 20 ? 29.838 -17.289 -60.365 1.00 70.53 ? 20 GLY B N 1 ATOM 2691 C CA . GLY B 2 20 ? 30.680 -18.449 -60.126 1.00 68.19 ? 20 GLY B CA 1 ATOM 2692 C C . GLY B 2 20 ? 32.120 -18.071 -59.860 1.00 65.47 ? 20 GLY B C 1 ATOM 2693 O O . GLY B 2 20 ? 32.527 -16.935 -60.098 1.00 66.43 ? 20 GLY B O 1 ATOM 2694 N N . TRP B 2 21 ? 32.896 -19.019 -59.354 1.00 63.07 ? 21 TRP B N 1 ATOM 2695 C CA . TRP B 2 21 ? 34.300 -18.749 -59.070 1.00 60.44 ? 21 TRP B CA 1 ATOM 2696 C C . TRP B 2 21 ? 35.143 -18.895 -60.326 1.00 55.92 ? 21 TRP B C 1 ATOM 2697 O O . TRP B 2 21 ? 36.134 -18.204 -60.485 1.00 54.47 ? 21 TRP B O 1 ATOM 2698 C CB . TRP B 2 21 ? 34.828 -19.652 -57.948 1.00 62.36 ? 21 TRP B CB 1 ATOM 2699 C CG . TRP B 2 21 ? 34.732 -19.063 -56.554 1.00 65.32 ? 21 TRP B CG 1 ATOM 2700 C CD1 . TRP B 2 21 ? 34.834 -17.744 -56.199 1.00 67.87 ? 21 TRP B CD1 1 ATOM 2701 C CD2 . TRP B 2 21 ? 34.570 -19.785 -55.339 1.00 67.89 ? 21 TRP B CD2 1 ATOM 2702 N NE1 . TRP B 2 21 ? 34.725 -17.603 -54.839 1.00 68.99 ? 21 TRP B NE1 1 ATOM 2703 C CE2 . TRP B 2 21 ? 34.560 -18.843 -54.286 1.00 69.05 ? 21 TRP B CE2 1 ATOM 2704 C CE3 . TRP B 2 21 ? 34.437 -21.141 -55.033 1.00 71.29 ? 21 TRP B CE3 1 ATOM 2705 C CZ2 . TRP B 2 21 ? 34.413 -19.213 -52.954 1.00 71.86 ? 21 TRP B CZ2 1 ATOM 2706 C CZ3 . TRP B 2 21 ? 34.296 -21.514 -53.700 1.00 74.02 ? 21 TRP B CZ3 1 ATOM 2707 C CH2 . TRP B 2 21 ? 34.283 -20.551 -52.677 1.00 73.73 ? 21 TRP B CH2 1 ATOM 2708 N N . TYR B 2 22 ? 34.744 -19.799 -61.213 1.00 54.35 ? 22 TYR B N 1 ATOM 2709 C CA . TYR B 2 22 ? 35.461 -20.047 -62.454 1.00 52.77 ? 22 TYR B CA 1 ATOM 2710 C C . TYR B 2 22 ? 34.487 -20.193 -63.591 1.00 52.92 ? 22 TYR B C 1 ATOM 2711 O O . TYR B 2 22 ? 33.352 -20.631 -63.393 1.00 54.36 ? 22 TYR B O 1 ATOM 2712 C CB . TYR B 2 22 ? 36.258 -21.353 -62.377 1.00 51.54 ? 22 TYR B CB 1 ATOM 2713 C CG . TYR B 2 22 ? 36.715 -21.735 -61.001 1.00 51.39 ? 22 TYR B CG 1 ATOM 2714 C CD1 . TYR B 2 22 ? 37.689 -20.999 -60.348 1.00 51.07 ? 22 TYR B CD1 1 ATOM 2715 C CD2 . TYR B 2 22 ? 36.193 -22.855 -60.357 1.00 52.45 ? 22 TYR B CD2 1 ATOM 2716 C CE1 . TYR B 2 22 ? 38.128 -21.357 -59.088 1.00 50.85 ? 22 TYR B CE1 1 ATOM 2717 C CE2 . TYR B 2 22 ? 36.627 -23.221 -59.096 1.00 52.02 ? 22 TYR B CE2 1 ATOM 2718 C CZ . TYR B 2 22 ? 37.595 -22.467 -58.470 1.00 51.30 ? 22 TYR B CZ 1 ATOM 2719 O OH . TYR B 2 22 ? 38.036 -22.804 -57.218 1.00 50.96 ? 22 TYR B OH 1 ATOM 2720 N N . GLY B 2 23 ? 34.940 -19.878 -64.797 1.00 53.12 ? 23 GLY B N 1 ATOM 2721 C CA . GLY B 2 23 ? 34.062 -19.983 -65.952 1.00 54.60 ? 23 GLY B CA 1 ATOM 2722 C C . GLY B 2 23 ? 34.702 -19.552 -67.244 1.00 55.18 ? 23 GLY B C 1 ATOM 2723 O O . GLY B 2 23 ? 35.932 -19.569 -67.378 1.00 54.83 ? 23 GLY B O 1 ATOM 2724 N N . TYR B 2 24 ? 33.849 -19.165 -68.189 1.00 56.95 ? 24 TYR B N 1 ATOM 2725 C CA . TYR B 2 24 ? 34.250 -18.893 -69.564 1.00 57.09 ? 24 TYR B CA 1 ATOM 2726 C C . TYR B 2 24 ? 33.827 -17.509 -69.986 1.00 57.81 ? 24 TYR B C 1 ATOM 2727 O O . TYR B 2 24 ? 32.797 -17.001 -69.540 1.00 58.26 ? 24 TYR B O 1 ATOM 2728 C CB . TYR B 2 24 ? 33.576 -19.875 -70.524 1.00 58.52 ? 24 TYR B CB 1 ATOM 2729 C CG . TYR B 2 24 ? 33.644 -21.307 -70.079 1.00 59.47 ? 24 TYR B CG 1 ATOM 2730 C CD1 . TYR B 2 24 ? 32.677 -21.833 -69.237 1.00 59.72 ? 24 TYR B CD1 1 ATOM 2731 C CD2 . TYR B 2 24 ? 34.685 -22.137 -70.490 1.00 59.51 ? 24 TYR B CD2 1 ATOM 2732 C CE1 . TYR B 2 24 ? 32.734 -23.141 -68.817 1.00 60.77 ? 24 TYR B CE1 1 ATOM 2733 C CE2 . TYR B 2 24 ? 34.748 -23.453 -70.074 1.00 59.81 ? 24 TYR B CE2 1 ATOM 2734 C CZ . TYR B 2 24 ? 33.774 -23.945 -69.235 1.00 61.43 ? 24 TYR B CZ 1 ATOM 2735 O OH . TYR B 2 24 ? 33.823 -25.252 -68.813 1.00 65.85 ? 24 TYR B OH 1 ATOM 2736 N N . HIS B 2 25 ? 34.619 -16.918 -70.873 1.00 58.27 ? 25 HIS B N 1 ATOM 2737 C CA . HIS B 2 25 ? 34.210 -15.728 -71.610 1.00 59.90 ? 25 HIS B CA 1 ATOM 2738 C C . HIS B 2 25 ? 34.302 -16.036 -73.089 1.00 59.59 ? 25 HIS B C 1 ATOM 2739 O O . HIS B 2 25 ? 35.290 -16.585 -73.527 1.00 58.17 ? 25 HIS B O 1 ATOM 2740 C CB . HIS B 2 25 ? 35.117 -14.549 -71.301 1.00 59.77 ? 25 HIS B CB 1 ATOM 2741 C CG . HIS B 2 25 ? 34.710 -13.301 -72.006 1.00 61.95 ? 25 HIS B CG 1 ATOM 2742 N ND1 . HIS B 2 25 ? 35.334 -12.858 -73.150 1.00 62.62 ? 25 HIS B ND1 1 ATOM 2743 C CD2 . HIS B 2 25 ? 33.707 -12.426 -71.758 1.00 63.26 ? 25 HIS B CD2 1 ATOM 2744 C CE1 . HIS B 2 25 ? 34.754 -11.743 -73.558 1.00 63.90 ? 25 HIS B CE1 1 ATOM 2745 N NE2 . HIS B 2 25 ? 33.761 -11.464 -72.734 1.00 64.46 ? 25 HIS B NE2 1 ATOM 2746 N N . HIS B 2 26 ? 33.277 -15.689 -73.858 1.00 62.02 ? 26 HIS B N 1 ATOM 2747 C CA . HIS B 2 26 ? 33.289 -15.959 -75.297 1.00 63.13 ? 26 HIS B CA 1 ATOM 2748 C C . HIS B 2 26 ? 33.110 -14.671 -76.089 1.00 64.53 ? 26 HIS B C 1 ATOM 2749 O O . HIS B 2 26 ? 32.552 -13.707 -75.589 1.00 64.49 ? 26 HIS B O 1 ATOM 2750 C CB . HIS B 2 26 ? 32.206 -16.976 -75.668 1.00 63.77 ? 26 HIS B CB 1 ATOM 2751 C CG . HIS B 2 26 ? 30.833 -16.401 -75.694 1.00 65.59 ? 26 HIS B CG 1 ATOM 2752 N ND1 . HIS B 2 26 ? 30.072 -16.253 -74.558 1.00 68.12 ? 26 HIS B ND1 1 ATOM 2753 C CD2 . HIS B 2 26 ? 30.095 -15.902 -76.711 1.00 67.85 ? 26 HIS B CD2 1 ATOM 2754 C CE1 . HIS B 2 26 ? 28.916 -15.693 -74.872 1.00 69.58 ? 26 HIS B CE1 1 ATOM 2755 N NE2 . HIS B 2 26 ? 28.905 -15.473 -76.174 1.00 70.78 ? 26 HIS B NE2 1 ATOM 2756 N N . SER B 2 27 ? 33.612 -14.678 -77.319 1.00 66.67 ? 27 SER B N 1 ATOM 2757 C CA . SER B 2 27 ? 33.540 -13.545 -78.244 1.00 68.81 ? 27 SER B CA 1 ATOM 2758 C C . SER B 2 27 ? 33.377 -14.057 -79.667 1.00 68.91 ? 27 SER B C 1 ATOM 2759 O O . SER B 2 27 ? 34.227 -14.802 -80.163 1.00 66.84 ? 27 SER B O 1 ATOM 2760 C CB . SER B 2 27 ? 34.821 -12.715 -78.175 1.00 69.69 ? 27 SER B CB 1 ATOM 2761 O OG . SER B 2 27 ? 34.587 -11.492 -77.523 1.00 73.06 ? 27 SER B OG 1 ATOM 2762 N N . ASN B 2 28 ? 32.291 -13.654 -80.317 1.00 70.38 ? 28 ASN B N 1 ATOM 2763 C CA . ASN B 2 28 ? 32.049 -14.009 -81.709 1.00 70.83 ? 28 ASN B CA 1 ATOM 2764 C C . ASN B 2 28 ? 31.231 -12.911 -82.387 1.00 74.38 ? 28 ASN B C 1 ATOM 2765 O O . ASN B 2 28 ? 31.082 -11.827 -81.825 1.00 74.96 ? 28 ASN B O 1 ATOM 2766 C CB . ASN B 2 28 ? 31.391 -15.394 -81.796 1.00 69.13 ? 28 ASN B CB 1 ATOM 2767 C CG . ASN B 2 28 ? 30.048 -15.459 -81.101 1.00 68.22 ? 28 ASN B CG 1 ATOM 2768 O OD1 . ASN B 2 28 ? 29.378 -14.446 -80.920 1.00 70.72 ? 28 ASN B OD1 1 ATOM 2769 N ND2 . ASN B 2 28 ? 29.639 -16.661 -80.722 1.00 66.27 ? 28 ASN B ND2 1 ATOM 2770 N N . GLU B 2 29 ? 30.722 -13.167 -83.589 1.00 78.23 ? 29 GLU B N 1 ATOM 2771 C CA . GLU B 2 29 ? 29.987 -12.139 -84.325 1.00 82.69 ? 29 GLU B CA 1 ATOM 2772 C C . GLU B 2 29 ? 28.659 -11.776 -83.664 1.00 83.38 ? 29 GLU B C 1 ATOM 2773 O O . GLU B 2 29 ? 28.196 -10.648 -83.798 1.00 84.43 ? 29 GLU B O 1 ATOM 2774 C CB . GLU B 2 29 ? 29.743 -12.568 -85.773 1.00 87.38 ? 29 GLU B CB 1 ATOM 2775 C CG . GLU B 2 29 ? 31.016 -12.657 -86.608 1.00 90.15 ? 29 GLU B CG 1 ATOM 2776 C CD . GLU B 2 29 ? 30.752 -12.914 -88.089 1.00 94.06 ? 29 GLU B CD 1 ATOM 2777 O OE1 . GLU B 2 29 ? 29.889 -12.229 -88.700 1.00 96.41 ? 29 GLU B OE1 1 ATOM 2778 O OE2 . GLU B 2 29 ? 31.424 -13.810 -88.646 1.00 97.16 ? 29 GLU B OE2 1 ATOM 2779 N N . GLN B 2 30 ? 28.058 -12.728 -82.953 1.00 83.43 ? 30 GLN B N 1 ATOM 2780 C CA . GLN B 2 30 ? 26.767 -12.507 -82.285 1.00 85.64 ? 30 GLN B CA 1 ATOM 2781 C C . GLN B 2 30 ? 26.895 -11.689 -81.001 1.00 84.21 ? 30 GLN B C 1 ATOM 2782 O O . GLN B 2 30 ? 25.906 -11.127 -80.526 1.00 85.31 ? 30 GLN B O 1 ATOM 2783 C CB . GLN B 2 30 ? 26.084 -13.839 -81.962 1.00 87.61 ? 30 GLN B CB 1 ATOM 2784 C CG . GLN B 2 30 ? 25.589 -14.613 -83.175 1.00 91.07 ? 30 GLN B CG 1 ATOM 2785 C CD . GLN B 2 30 ? 25.862 -16.110 -83.056 1.00 93.64 ? 30 GLN B CD 1 ATOM 2786 O OE1 . GLN B 2 30 ? 27.021 -16.540 -82.981 1.00 94.00 ? 30 GLN B OE1 1 ATOM 2787 N NE2 . GLN B 2 30 ? 24.800 -16.911 -83.043 1.00 96.23 ? 30 GLN B NE2 1 ATOM 2788 N N . GLY B 2 31 ? 28.097 -11.634 -80.434 1.00 80.88 ? 31 GLY B N 1 ATOM 2789 C CA . GLY B 2 31 ? 28.335 -10.875 -79.205 1.00 80.60 ? 31 GLY B CA 1 ATOM 2790 C C . GLY B 2 31 ? 29.322 -11.539 -78.272 1.00 76.90 ? 31 GLY B C 1 ATOM 2791 O O . GLY B 2 31 ? 30.111 -12.378 -78.690 1.00 76.44 ? 31 GLY B O 1 ATOM 2792 N N . SER B 2 32 ? 29.275 -11.167 -76.997 1.00 75.72 ? 32 SER B N 1 ATOM 2793 C CA . SER B 2 32 ? 30.205 -11.720 -76.016 1.00 72.29 ? 32 SER B CA 1 ATOM 2794 C C . SER B 2 32 ? 29.606 -11.745 -74.623 1.00 71.72 ? 32 SER B C 1 ATOM 2795 O O . SER B 2 32 ? 28.598 -11.100 -74.365 1.00 74.32 ? 32 SER B O 1 ATOM 2796 C CB . SER B 2 32 ? 31.495 -10.903 -76.000 1.00 71.96 ? 32 SER B CB 1 ATOM 2797 O OG . SER B 2 32 ? 31.259 -9.613 -75.481 1.00 73.88 ? 32 SER B OG 1 ATOM 2798 N N . GLY B 2 33 ? 30.231 -12.499 -73.729 1.00 70.14 ? 33 GLY B N 1 ATOM 2799 C CA . GLY B 2 33 ? 29.760 -12.594 -72.355 1.00 70.56 ? 33 GLY B CA 1 ATOM 2800 C C . GLY B 2 33 ? 30.416 -13.672 -71.513 1.00 67.29 ? 33 GLY B C 1 ATOM 2801 O O . GLY B 2 33 ? 31.228 -14.447 -71.998 1.00 65.49 ? 33 GLY B O 1 ATOM 2802 N N . TYR B 2 34 ? 30.032 -13.704 -70.240 1.00 68.23 ? 34 TYR B N 1 ATOM 2803 C CA . TYR B 2 34 ? 30.595 -14.609 -69.244 1.00 66.38 ? 34 TYR B CA 1 ATOM 2804 C C . TYR B 2 34 ? 29.623 -15.723 -68.919 1.00 66.75 ? 34 TYR B C 1 ATOM 2805 O O . TYR B 2 34 ? 28.425 -15.510 -68.886 1.00 69.66 ? 34 TYR B O 1 ATOM 2806 C CB . TYR B 2 34 ? 30.888 -13.846 -67.952 1.00 66.14 ? 34 TYR B CB 1 ATOM 2807 C CG . TYR B 2 34 ? 31.852 -12.700 -68.122 1.00 66.88 ? 34 TYR B CG 1 ATOM 2808 C CD1 . TYR B 2 34 ? 33.223 -12.905 -68.052 1.00 65.45 ? 34 TYR B CD1 1 ATOM 2809 C CD2 . TYR B 2 34 ? 31.394 -11.406 -68.361 1.00 70.21 ? 34 TYR B CD2 1 ATOM 2810 C CE1 . TYR B 2 34 ? 34.111 -11.854 -68.211 1.00 66.38 ? 34 TYR B CE1 1 ATOM 2811 C CE2 . TYR B 2 34 ? 32.278 -10.350 -68.518 1.00 70.49 ? 34 TYR B CE2 1 ATOM 2812 C CZ . TYR B 2 34 ? 33.632 -10.583 -68.441 1.00 69.28 ? 34 TYR B CZ 1 ATOM 2813 O OH . TYR B 2 34 ? 34.518 -9.549 -68.592 1.00 72.26 ? 34 TYR B OH 1 ATOM 2814 N N . ALA B 2 35 ? 30.149 -16.907 -68.656 1.00 66.29 ? 35 ALA B N 1 ATOM 2815 C CA . ALA B 2 35 ? 29.341 -18.003 -68.144 1.00 67.76 ? 35 ALA B CA 1 ATOM 2816 C C . ALA B 2 35 ? 30.149 -18.809 -67.112 1.00 68.16 ? 35 ALA B C 1 ATOM 2817 O O . ALA B 2 35 ? 31.251 -19.287 -67.392 1.00 66.06 ? 35 ALA B O 1 ATOM 2818 C CB . ALA B 2 35 ? 28.883 -18.893 -69.279 1.00 67.82 ? 35 ALA B CB 1 ATOM 2819 N N . ALA B 2 36 ? 29.588 -18.931 -65.915 1.00 70.97 ? 36 ALA B N 1 ATOM 2820 C CA . ALA B 2 36 ? 30.187 -19.694 -64.833 1.00 70.80 ? 36 ALA B CA 1 ATOM 2821 C C . ALA B 2 36 ? 30.134 -21.182 -65.150 1.00 71.88 ? 36 ALA B C 1 ATOM 2822 O O . ALA B 2 36 ? 29.142 -21.657 -65.695 1.00 74.76 ? 36 ALA B O 1 ATOM 2823 C CB . ALA B 2 36 ? 29.439 -19.411 -63.536 1.00 72.19 ? 36 ALA B CB 1 ATOM 2824 N N . ASP B 2 37 ? 31.203 -21.906 -64.825 1.00 71.31 ? 37 ASP B N 1 ATOM 2825 C CA . ASP B 2 37 ? 31.204 -23.363 -64.892 1.00 71.96 ? 37 ASP B CA 1 ATOM 2826 C C . ASP B 2 37 ? 30.649 -23.868 -63.560 1.00 75.93 ? 37 ASP B C 1 ATOM 2827 O O . ASP B 2 37 ? 31.318 -23.772 -62.529 1.00 73.99 ? 37 ASP B O 1 ATOM 2828 C CB . ASP B 2 37 ? 32.620 -23.885 -65.122 1.00 72.54 ? 37 ASP B CB 1 ATOM 2829 C CG . ASP B 2 37 ? 32.667 -25.390 -65.334 1.00 74.89 ? 37 ASP B CG 1 ATOM 2830 O OD1 . ASP B 2 37 ? 32.376 -25.845 -66.462 1.00 77.51 ? 37 ASP B OD1 1 ATOM 2831 O OD2 . ASP B 2 37 ? 33.011 -26.118 -64.378 1.00 74.50 ? 37 ASP B OD2 1 ATOM 2832 N N . LYS B 2 38 ? 29.415 -24.377 -63.586 1.00 81.65 ? 38 LYS B N 1 ATOM 2833 C CA . LYS B 2 38 ? 28.706 -24.812 -62.380 1.00 85.05 ? 38 LYS B CA 1 ATOM 2834 C C . LYS B 2 38 ? 29.458 -25.913 -61.629 1.00 81.89 ? 38 LYS B C 1 ATOM 2835 O O . LYS B 2 38 ? 29.621 -25.832 -60.413 1.00 80.17 ? 38 LYS B O 1 ATOM 2836 C CB . LYS B 2 38 ? 27.293 -25.302 -62.742 1.00 93.31 ? 38 LYS B CB 1 ATOM 2837 C CG . LYS B 2 38 ? 26.486 -25.878 -61.571 1.00 100.50 ? 38 LYS B CG 1 ATOM 2838 C CD . LYS B 2 38 ? 25.588 -27.057 -61.968 1.00 106.72 ? 38 LYS B CD 1 ATOM 2839 C CE . LYS B 2 38 ? 24.114 -26.678 -62.092 1.00 111.02 ? 38 LYS B CE 1 ATOM 2840 N NZ . LYS B 2 38 ? 23.844 -25.727 -63.205 1.00 111.60 ? 38 LYS B NZ 1 ATOM 2841 N N . GLU B 2 39 ? 29.906 -26.932 -62.354 1.00 80.77 ? 39 GLU B N 1 ATOM 2842 C CA . GLU B 2 39 ? 30.495 -28.122 -61.736 1.00 81.62 ? 39 GLU B CA 1 ATOM 2843 C C . GLU B 2 39 ? 31.759 -27.831 -60.929 1.00 75.77 ? 39 GLU B C 1 ATOM 2844 O O . GLU B 2 39 ? 31.860 -28.244 -59.772 1.00 76.48 ? 39 GLU B O 1 ATOM 2845 C CB . GLU B 2 39 ? 30.796 -29.200 -62.790 1.00 86.41 ? 39 GLU B CB 1 ATOM 2846 C CG . GLU B 2 39 ? 31.827 -30.236 -62.342 1.00 90.23 ? 39 GLU B CG 1 ATOM 2847 C CD . GLU B 2 39 ? 31.871 -31.462 -63.234 1.00 95.13 ? 39 GLU B CD 1 ATOM 2848 O OE1 . GLU B 2 39 ? 30.842 -32.170 -63.322 1.00 99.29 ? 39 GLU B OE1 1 ATOM 2849 O OE2 . GLU B 2 39 ? 32.942 -31.724 -63.830 1.00 95.81 ? 39 GLU B OE2 1 ATOM 2850 N N . SER B 2 40 ? 32.731 -27.157 -61.538 1.00 69.06 ? 40 SER B N 1 ATOM 2851 C CA . SER B 2 40 ? 33.974 -26.863 -60.834 1.00 65.07 ? 40 SER B CA 1 ATOM 2852 C C . SER B 2 40 ? 33.727 -25.885 -59.692 1.00 63.02 ? 40 SER B C 1 ATOM 2853 O O . SER B 2 40 ? 34.308 -26.036 -58.615 1.00 60.74 ? 40 SER B O 1 ATOM 2854 C CB . SER B 2 40 ? 35.065 -26.348 -61.780 1.00 63.33 ? 40 SER B CB 1 ATOM 2855 O OG . SER B 2 40 ? 34.581 -25.331 -62.627 1.00 64.78 ? 40 SER B OG 1 ATOM 2856 N N . THR B 2 41 ? 32.845 -24.910 -59.914 1.00 61.85 ? 41 THR B N 1 ATOM 2857 C CA . THR B 2 41 ? 32.474 -23.969 -58.863 1.00 61.17 ? 41 THR B CA 1 ATOM 2858 C C . THR B 2 41 ? 31.893 -24.698 -57.659 1.00 61.58 ? 41 THR B C 1 ATOM 2859 O O . THR B 2 41 ? 32.296 -24.445 -56.537 1.00 60.58 ? 41 THR B O 1 ATOM 2860 C CB . THR B 2 41 ? 31.471 -22.890 -59.356 1.00 63.12 ? 41 THR B CB 1 ATOM 2861 O OG1 . THR B 2 41 ? 32.088 -22.068 -60.358 1.00 62.25 ? 41 THR B OG1 1 ATOM 2862 C CG2 . THR B 2 41 ? 31.024 -21.991 -58.207 1.00 63.50 ? 41 THR B CG2 1 ATOM 2863 N N . GLN B 2 42 ? 30.956 -25.609 -57.888 1.00 64.87 ? 42 GLN B N 1 ATOM 2864 C CA . GLN B 2 42 ? 30.307 -26.332 -56.786 1.00 67.67 ? 42 GLN B CA 1 ATOM 2865 C C . GLN B 2 42 ? 31.262 -27.273 -56.054 1.00 67.26 ? 42 GLN B C 1 ATOM 2866 O O . GLN B 2 42 ? 31.171 -27.407 -54.837 1.00 67.70 ? 42 GLN B O 1 ATOM 2867 C CB . GLN B 2 42 ? 29.092 -27.124 -57.284 1.00 71.17 ? 42 GLN B CB 1 ATOM 2868 C CG . GLN B 2 42 ? 28.284 -27.785 -56.174 1.00 74.90 ? 42 GLN B CG 1 ATOM 2869 C CD . GLN B 2 42 ? 27.723 -26.789 -55.168 1.00 76.90 ? 42 GLN B CD 1 ATOM 2870 O OE1 . GLN B 2 42 ? 27.939 -26.917 -53.963 1.00 76.39 ? 42 GLN B OE1 1 ATOM 2871 N NE2 . GLN B 2 42 ? 26.995 -25.790 -55.664 1.00 78.43 ? 42 GLN B NE2 1 ATOM 2872 N N . LYS B 2 43 ? 32.149 -27.940 -56.789 1.00 67.35 ? 43 LYS B N 1 ATOM 2873 C CA . LYS B 2 43 ? 33.220 -28.723 -56.161 1.00 69.47 ? 43 LYS B CA 1 ATOM 2874 C C . LYS B 2 43 ? 34.081 -27.843 -55.253 1.00 65.44 ? 43 LYS B C 1 ATOM 2875 O O . LYS B 2 43 ? 34.483 -28.271 -54.170 1.00 67.11 ? 43 LYS B O 1 ATOM 2876 C CB . LYS B 2 43 ? 34.101 -29.428 -57.209 1.00 73.36 ? 43 LYS B CB 1 ATOM 2877 C CG . LYS B 2 43 ? 33.406 -30.601 -57.901 1.00 82.65 ? 43 LYS B CG 1 ATOM 2878 C CD . LYS B 2 43 ? 34.155 -31.106 -59.134 1.00 87.51 ? 43 LYS B CD 1 ATOM 2879 C CE . LYS B 2 43 ? 35.399 -31.924 -58.776 1.00 90.48 ? 43 LYS B CE 1 ATOM 2880 N NZ . LYS B 2 43 ? 35.079 -33.249 -58.161 1.00 92.89 ? 43 LYS B NZ 1 ATOM 2881 N N . ALA B 2 44 ? 34.349 -26.613 -55.677 1.00 59.90 ? 44 ALA B N 1 ATOM 2882 C CA . ALA B 2 44 ? 35.128 -25.707 -54.850 1.00 59.13 ? 44 ALA B CA 1 ATOM 2883 C C . ALA B 2 44 ? 34.370 -25.299 -53.588 1.00 59.82 ? 44 ALA B C 1 ATOM 2884 O O . ALA B 2 44 ? 34.939 -25.278 -52.505 1.00 61.24 ? 44 ALA B O 1 ATOM 2885 C CB . ALA B 2 44 ? 35.562 -24.476 -55.640 1.00 58.35 ? 44 ALA B CB 1 ATOM 2886 N N . ILE B 2 45 ? 33.090 -24.979 -53.718 1.00 60.32 ? 45 ILE B N 1 ATOM 2887 C CA . ILE B 2 45 ? 32.300 -24.584 -52.562 1.00 62.57 ? 45 ILE B CA 1 ATOM 2888 C C . ILE B 2 45 ? 32.210 -25.713 -51.535 1.00 64.48 ? 45 ILE B C 1 ATOM 2889 O O . ILE B 2 45 ? 32.271 -25.466 -50.331 1.00 65.66 ? 45 ILE B O 1 ATOM 2890 C CB . ILE B 2 45 ? 30.891 -24.112 -52.985 1.00 65.74 ? 45 ILE B CB 1 ATOM 2891 C CG1 . ILE B 2 45 ? 30.987 -22.746 -53.672 1.00 65.03 ? 45 ILE B CG1 1 ATOM 2892 C CG2 . ILE B 2 45 ? 29.950 -24.036 -51.789 1.00 67.42 ? 45 ILE B CG2 1 ATOM 2893 C CD1 . ILE B 2 45 ? 29.718 -22.354 -54.398 1.00 68.20 ? 45 ILE B CD1 1 ATOM 2894 N N . ASP B 2 46 ? 32.067 -26.949 -52.007 1.00 65.23 ? 46 ASP B N 1 ATOM 2895 C CA . ASP B 2 46 ? 32.021 -28.107 -51.114 1.00 66.55 ? 46 ASP B CA 1 ATOM 2896 C C . ASP B 2 46 ? 33.341 -28.315 -50.371 1.00 63.26 ? 46 ASP B C 1 ATOM 2897 O O . ASP B 2 46 ? 33.343 -28.606 -49.179 1.00 65.56 ? 46 ASP B O 1 ATOM 2898 C CB . ASP B 2 46 ? 31.645 -29.376 -51.889 1.00 69.23 ? 46 ASP B CB 1 ATOM 2899 C CG . ASP B 2 46 ? 30.249 -29.299 -52.500 1.00 74.46 ? 46 ASP B CG 1 ATOM 2900 O OD1 . ASP B 2 46 ? 29.479 -28.382 -52.129 1.00 77.00 ? 46 ASP B OD1 1 ATOM 2901 O OD2 . ASP B 2 46 ? 29.919 -30.152 -53.358 1.00 77.87 ? 46 ASP B OD2 1 ATOM 2902 N N . GLY B 2 47 ? 34.460 -28.163 -51.066 1.00 59.12 ? 47 GLY B N 1 ATOM 2903 C CA . GLY B 2 47 ? 35.765 -28.404 -50.461 1.00 57.74 ? 47 GLY B CA 1 ATOM 2904 C C . GLY B 2 47 ? 36.103 -27.393 -49.385 1.00 57.77 ? 47 GLY B C 1 ATOM 2905 O O . GLY B 2 47 ? 36.519 -27.757 -48.280 1.00 57.07 ? 47 GLY B O 1 ATOM 2906 N N . VAL B 2 48 ? 35.917 -26.115 -49.712 1.00 57.94 ? 48 VAL B N 1 ATOM 2907 C CA . VAL B 2 48 ? 36.184 -25.030 -48.779 1.00 57.45 ? 48 VAL B CA 1 ATOM 2908 C C . VAL B 2 48 ? 35.252 -25.116 -47.571 1.00 59.42 ? 48 VAL B C 1 ATOM 2909 O O . VAL B 2 48 ? 35.684 -24.899 -46.447 1.00 59.95 ? 48 VAL B O 1 ATOM 2910 C CB . VAL B 2 48 ? 36.066 -23.663 -49.476 1.00 58.13 ? 48 VAL B CB 1 ATOM 2911 C CG1 . VAL B 2 48 ? 36.111 -22.530 -48.471 1.00 59.09 ? 48 VAL B CG1 1 ATOM 2912 C CG2 . VAL B 2 48 ? 37.199 -23.498 -50.486 1.00 57.29 ? 48 VAL B CG2 1 ATOM 2913 N N . THR B 2 49 ? 33.989 -25.466 -47.799 1.00 60.58 ? 49 THR B N 1 ATOM 2914 C CA . THR B 2 49 ? 33.023 -25.602 -46.708 1.00 63.03 ? 49 THR B CA 1 ATOM 2915 C C . THR B 2 49 ? 33.376 -26.755 -45.769 1.00 64.26 ? 49 THR B C 1 ATOM 2916 O O . THR B 2 49 ? 33.313 -26.618 -44.547 1.00 65.79 ? 49 THR B O 1 ATOM 2917 C CB . THR B 2 49 ? 31.599 -25.822 -47.249 1.00 64.99 ? 49 THR B CB 1 ATOM 2918 O OG1 . THR B 2 49 ? 31.268 -24.765 -48.152 1.00 63.17 ? 49 THR B OG1 1 ATOM 2919 C CG2 . THR B 2 49 ? 30.588 -25.868 -46.125 1.00 67.49 ? 49 THR B CG2 1 ATOM 2920 N N . ASN B 2 50 ? 33.739 -27.896 -46.335 1.00 64.86 ? 50 ASN B N 1 ATOM 2921 C CA . ASN B 2 50 ? 34.201 -29.015 -45.515 1.00 66.80 ? 50 ASN B CA 1 ATOM 2922 C C . ASN B 2 50 ? 35.451 -28.642 -44.722 1.00 65.01 ? 50 ASN B C 1 ATOM 2923 O O . ASN B 2 50 ? 35.616 -29.055 -43.577 1.00 65.49 ? 50 ASN B O 1 ATOM 2924 C CB . ASN B 2 50 ? 34.466 -30.250 -46.378 1.00 67.38 ? 50 ASN B CB 1 ATOM 2925 C CG . ASN B 2 50 ? 33.192 -30.835 -46.964 1.00 71.25 ? 50 ASN B CG 1 ATOM 2926 O OD1 . ASN B 2 50 ? 32.094 -30.562 -46.484 1.00 75.46 ? 50 ASN B OD1 1 ATOM 2927 N ND2 . ASN B 2 50 ? 33.330 -31.638 -48.008 1.00 71.84 ? 50 ASN B ND2 1 ATOM 2928 N N . LYS B 2 51 ? 36.325 -27.848 -45.333 1.00 63.31 ? 51 LYS B N 1 ATOM 2929 C CA . LYS B 2 51 ? 37.566 -27.453 -44.681 1.00 62.07 ? 51 LYS B CA 1 ATOM 2930 C C . LYS B 2 51 ? 37.258 -26.625 -43.443 1.00 62.19 ? 51 LYS B C 1 ATOM 2931 O O . LYS B 2 51 ? 37.750 -26.914 -42.354 1.00 61.74 ? 51 LYS B O 1 ATOM 2932 C CB . LYS B 2 51 ? 38.449 -26.658 -45.643 1.00 61.07 ? 51 LYS B CB 1 ATOM 2933 C CG . LYS B 2 51 ? 39.681 -26.061 -44.990 1.00 61.52 ? 51 LYS B CG 1 ATOM 2934 C CD . LYS B 2 51 ? 40.522 -25.309 -45.998 1.00 61.57 ? 51 LYS B CD 1 ATOM 2935 C CE . LYS B 2 51 ? 41.185 -26.252 -46.978 1.00 60.46 ? 51 LYS B CE 1 ATOM 2936 N NZ . LYS B 2 51 ? 42.288 -25.548 -47.673 1.00 60.68 ? 51 LYS B NZ 1 ATOM 2937 N N . VAL B 2 52 ? 36.436 -25.597 -43.622 1.00 61.34 ? 52 VAL B N 1 ATOM 2938 C CA . VAL B 2 52 ? 36.094 -24.710 -42.531 1.00 62.45 ? 52 VAL B CA 1 ATOM 2939 C C . VAL B 2 52 ? 35.499 -25.536 -41.384 1.00 64.99 ? 52 VAL B C 1 ATOM 2940 O O . VAL B 2 52 ? 35.982 -25.473 -40.250 1.00 65.32 ? 52 VAL B O 1 ATOM 2941 C CB . VAL B 2 52 ? 35.120 -23.598 -42.988 1.00 63.90 ? 52 VAL B CB 1 ATOM 2942 C CG1 . VAL B 2 52 ? 34.691 -22.735 -41.806 1.00 66.44 ? 52 VAL B CG1 1 ATOM 2943 C CG2 . VAL B 2 52 ? 35.764 -22.725 -44.054 1.00 61.64 ? 52 VAL B CG2 1 ATOM 2944 N N . ASN B 2 53 ? 34.481 -26.339 -41.681 1.00 66.53 ? 53 ASN B N 1 ATOM 2945 C CA . ASN B 2 53 ? 33.863 -27.173 -40.648 1.00 69.89 ? 53 ASN B CA 1 ATOM 2946 C C . ASN B 2 53 ? 34.878 -28.118 -40.005 1.00 69.17 ? 53 ASN B C 1 ATOM 2947 O O . ASN B 2 53 ? 34.853 -28.325 -38.797 1.00 70.64 ? 53 ASN B O 1 ATOM 2948 C CB . ASN B 2 53 ? 32.677 -27.967 -41.206 1.00 72.34 ? 53 ASN B CB 1 ATOM 2949 C CG . ASN B 2 53 ? 31.584 -27.075 -41.764 1.00 74.21 ? 53 ASN B CG 1 ATOM 2950 O OD1 . ASN B 2 53 ? 31.381 -25.962 -41.296 1.00 75.64 ? 53 ASN B OD1 1 ATOM 2951 N ND2 . ASN B 2 53 ? 30.880 -27.560 -42.776 1.00 75.83 ? 53 ASN B ND2 1 ATOM 2952 N N . SER B 2 54 ? 35.779 -28.677 -40.806 1.00 68.25 ? 54 SER B N 1 ATOM 2953 C CA . SER B 2 54 ? 36.818 -29.560 -40.270 1.00 69.48 ? 54 SER B CA 1 ATOM 2954 C C . SER B 2 54 ? 37.702 -28.824 -39.269 1.00 69.99 ? 54 SER B C 1 ATOM 2955 O O . SER B 2 54 ? 38.024 -29.365 -38.213 1.00 70.88 ? 54 SER B O 1 ATOM 2956 C CB . SER B 2 54 ? 37.681 -30.167 -41.386 1.00 67.49 ? 54 SER B CB 1 ATOM 2957 O OG . SER B 2 54 ? 37.013 -31.248 -42.001 1.00 68.74 ? 54 SER B OG 1 ATOM 2958 N N . ILE B 2 55 ? 38.078 -27.592 -39.608 1.00 69.69 ? 55 ILE B N 1 ATOM 2959 C CA . ILE B 2 55 ? 38.893 -26.752 -38.737 1.00 71.67 ? 55 ILE B CA 1 ATOM 2960 C C . ILE B 2 55 ? 38.145 -26.438 -37.445 1.00 75.49 ? 55 ILE B C 1 ATOM 2961 O O . ILE B 2 55 ? 38.686 -26.602 -36.356 1.00 77.48 ? 55 ILE B O 1 ATOM 2962 C CB . ILE B 2 55 ? 39.309 -25.442 -39.458 1.00 72.58 ? 55 ILE B CB 1 ATOM 2963 C CG1 . ILE B 2 55 ? 40.358 -25.754 -40.530 1.00 70.93 ? 55 ILE B CG1 1 ATOM 2964 C CG2 . ILE B 2 55 ? 39.851 -24.406 -38.478 1.00 73.77 ? 55 ILE B CG2 1 ATOM 2965 C CD1 . ILE B 2 55 ? 40.589 -24.634 -41.513 1.00 70.27 ? 55 ILE B CD1 1 ATOM 2966 N N . ILE B 2 56 ? 36.902 -25.990 -37.566 1.00 78.82 ? 56 ILE B N 1 ATOM 2967 C CA . ILE B 2 56 ? 36.092 -25.682 -36.393 1.00 82.39 ? 56 ILE B CA 1 ATOM 2968 C C . ILE B 2 56 ? 35.967 -26.914 -35.495 1.00 86.15 ? 56 ILE B C 1 ATOM 2969 O O . ILE B 2 56 ? 36.162 -26.820 -34.283 1.00 87.18 ? 56 ILE B O 1 ATOM 2970 C CB . ILE B 2 56 ? 34.686 -25.189 -36.793 1.00 84.38 ? 56 ILE B CB 1 ATOM 2971 C CG1 . ILE B 2 56 ? 34.787 -23.829 -37.496 1.00 82.85 ? 56 ILE B CG1 1 ATOM 2972 C CG2 . ILE B 2 56 ? 33.769 -25.112 -35.572 1.00 87.43 ? 56 ILE B CG2 1 ATOM 2973 C CD1 . ILE B 2 56 ? 33.542 -23.428 -38.259 1.00 84.15 ? 56 ILE B CD1 1 ATOM 2974 N N . ASP B 2 57 ? 35.655 -28.060 -36.101 1.00 89.55 ? 57 ASP B N 1 ATOM 2975 C CA . ASP B 2 57 ? 35.427 -29.311 -35.363 1.00 93.97 ? 57 ASP B CA 1 ATOM 2976 C C . ASP B 2 57 ? 36.653 -29.768 -34.572 1.00 91.27 ? 57 ASP B C 1 ATOM 2977 O O . ASP B 2 57 ? 36.542 -30.100 -33.400 1.00 91.69 ? 57 ASP B O 1 ATOM 2978 C CB . ASP B 2 57 ? 34.985 -30.426 -36.320 1.00 97.40 ? 57 ASP B CB 1 ATOM 2979 C CG . ASP B 2 57 ? 34.463 -31.655 -35.589 1.00 105.18 ? 57 ASP B CG 1 ATOM 2980 O OD1 . ASP B 2 57 ? 33.528 -31.511 -34.768 1.00 111.46 ? 57 ASP B OD1 1 ATOM 2981 O OD2 . ASP B 2 57 ? 34.981 -32.769 -35.837 1.00 107.17 ? 57 ASP B OD2 1 ATOM 2982 N N . LYS B 2 58 ? 37.820 -29.771 -35.211 1.00 89.77 ? 58 LYS B N 1 ATOM 2983 C CA . LYS B 2 58 ? 39.056 -30.208 -34.558 1.00 90.57 ? 58 LYS B CA 1 ATOM 2984 C C . LYS B 2 58 ? 39.448 -29.363 -33.352 1.00 93.68 ? 58 LYS B C 1 ATOM 2985 O O . LYS B 2 58 ? 40.075 -29.865 -32.424 1.00 93.88 ? 58 LYS B O 1 ATOM 2986 C CB . LYS B 2 58 ? 40.220 -30.220 -35.553 1.00 88.32 ? 58 LYS B CB 1 ATOM 2987 C CG . LYS B 2 58 ? 40.133 -31.317 -36.594 1.00 88.62 ? 58 LYS B CG 1 ATOM 2988 C CD . LYS B 2 58 ? 40.258 -32.702 -35.984 1.00 90.25 ? 58 LYS B CD 1 ATOM 2989 C CE . LYS B 2 58 ? 39.165 -33.618 -36.511 1.00 92.42 ? 58 LYS B CE 1 ATOM 2990 N NZ . LYS B 2 58 ? 39.308 -35.022 -36.034 1.00 94.88 ? 58 LYS B NZ 1 ATOM 2991 N N . MET B 2 59 ? 39.088 -28.084 -33.367 1.00 98.49 ? 59 MET B N 1 ATOM 2992 C CA . MET B 2 59 ? 39.434 -27.178 -32.272 1.00 103.85 ? 59 MET B CA 1 ATOM 2993 C C . MET B 2 59 ? 38.360 -27.134 -31.170 1.00 111.19 ? 59 MET B C 1 ATOM 2994 O O . MET B 2 59 ? 38.497 -26.375 -30.212 1.00 113.36 ? 59 MET B O 1 ATOM 2995 C CB . MET B 2 59 ? 39.680 -25.766 -32.818 1.00 102.47 ? 59 MET B CB 1 ATOM 2996 C CG . MET B 2 59 ? 40.692 -25.686 -33.959 1.00 99.86 ? 59 MET B CG 1 ATOM 2997 S SD . MET B 2 59 ? 42.439 -25.898 -33.544 1.00 100.37 ? 59 MET B SD 1 ATOM 2998 C CE . MET B 2 59 ? 42.732 -24.789 -32.169 1.00 102.35 ? 59 MET B CE 1 ATOM 2999 N N . ASN B 2 60 ? 37.308 -27.947 -31.293 1.00 117.63 ? 60 ASN B N 1 ATOM 3000 C CA . ASN B 2 60 ? 36.199 -27.931 -30.327 1.00 123.85 ? 60 ASN B CA 1 ATOM 3001 C C . ASN B 2 60 ? 36.562 -28.583 -28.987 1.00 125.24 ? 60 ASN B C 1 ATOM 3002 O O . ASN B 2 60 ? 35.986 -28.249 -27.954 1.00 124.05 ? 60 ASN B O 1 ATOM 3003 C CB . ASN B 2 60 ? 34.929 -28.573 -30.924 1.00 127.51 ? 60 ASN B CB 1 ATOM 3004 C CG . ASN B 2 60 ? 34.816 -30.067 -30.633 1.00 131.26 ? 60 ASN B CG 1 ATOM 3005 O OD1 . ASN B 2 60 ? 35.787 -30.819 -30.744 1.00 132.31 ? 60 ASN B OD1 1 ATOM 3006 N ND2 . ASN B 2 60 ? 33.616 -30.504 -30.265 1.00 134.69 ? 60 ASN B ND2 1 ATOM 3007 N N . THR B 2 61 ? 37.503 -29.523 -29.019 1.00 111.73 ? 61 THR B N 1 ATOM 3008 C CA . THR B 2 61 ? 37.988 -30.174 -27.811 1.00 115.05 ? 61 THR B CA 1 ATOM 3009 C C . THR B 2 61 ? 39.355 -29.578 -27.522 1.00 112.66 ? 61 THR B C 1 ATOM 3010 O O . THR B 2 61 ? 40.354 -29.961 -28.131 1.00 115.11 ? 61 THR B O 1 ATOM 3011 C CB . THR B 2 61 ? 38.088 -31.709 -27.966 1.00 121.59 ? 61 THR B CB 1 ATOM 3012 O OG1 . THR B 2 61 ? 36.906 -32.220 -28.600 1.00 126.55 ? 61 THR B OG1 1 ATOM 3013 C CG2 . THR B 2 61 ? 38.255 -32.375 -26.601 1.00 122.53 ? 61 THR B CG2 1 ATOM 3014 N N . GLN B 2 62 ? 39.380 -28.624 -26.599 1.00 109.77 ? 62 GLN B N 1 ATOM 3015 C CA . GLN B 2 62 ? 40.575 -27.837 -26.319 1.00 107.14 ? 62 GLN B CA 1 ATOM 3016 C C . GLN B 2 62 ? 40.557 -27.333 -24.867 1.00 105.92 ? 62 GLN B C 1 ATOM 3017 O O . GLN B 2 62 ? 39.489 -27.205 -24.251 1.00 110.65 ? 62 GLN B O 1 ATOM 3018 C CB . GLN B 2 62 ? 40.671 -26.685 -27.331 1.00 105.72 ? 62 GLN B CB 1 ATOM 3019 C CG . GLN B 2 62 ? 41.376 -25.423 -26.850 1.00 103.69 ? 62 GLN B CG 1 ATOM 3020 C CD . GLN B 2 62 ? 41.439 -24.350 -27.917 1.00 106.01 ? 62 GLN B CD 1 ATOM 3021 O OE1 . GLN B 2 62 ? 41.187 -24.613 -29.093 1.00 106.17 ? 62 GLN B OE1 1 ATOM 3022 N NE2 . GLN B 2 62 ? 41.774 -23.129 -27.511 1.00 107.44 ? 62 GLN B NE2 1 ATOM 3023 N N . PHE B 2 63 ? 41.749 -27.051 -24.344 1.00 96.36 ? 63 PHE B N 1 ATOM 3024 C CA . PHE B 2 63 ? 41.946 -26.722 -22.934 1.00 92.77 ? 63 PHE B CA 1 ATOM 3025 C C . PHE B 2 63 ? 41.077 -25.566 -22.441 1.00 95.66 ? 63 PHE B C 1 ATOM 3026 O O . PHE B 2 63 ? 40.967 -24.535 -23.105 1.00 99.73 ? 63 PHE B O 1 ATOM 3027 C CB . PHE B 2 63 ? 43.416 -26.386 -22.681 1.00 86.88 ? 63 PHE B CB 1 ATOM 3028 C CG . PHE B 2 63 ? 43.767 -26.285 -21.234 1.00 81.60 ? 63 PHE B CG 1 ATOM 3029 C CD1 . PHE B 2 63 ? 43.932 -27.431 -20.471 1.00 79.52 ? 63 PHE B CD1 1 ATOM 3030 C CD2 . PHE B 2 63 ? 43.924 -25.042 -20.628 1.00 81.97 ? 63 PHE B CD2 1 ATOM 3031 C CE1 . PHE B 2 63 ? 44.253 -27.343 -19.130 1.00 79.69 ? 63 PHE B CE1 1 ATOM 3032 C CE2 . PHE B 2 63 ? 44.243 -24.946 -19.282 1.00 78.09 ? 63 PHE B CE2 1 ATOM 3033 C CZ . PHE B 2 63 ? 44.410 -26.100 -18.534 1.00 78.16 ? 63 PHE B CZ 1 ATOM 3034 N N . GLU B 2 64 ? 40.466 -25.758 -21.274 1.00 96.46 ? 64 GLU B N 1 ATOM 3035 C CA . GLU B 2 64 ? 39.676 -24.726 -20.610 1.00 98.01 ? 64 GLU B CA 1 ATOM 3036 C C . GLU B 2 64 ? 40.273 -24.458 -19.236 1.00 95.99 ? 64 GLU B C 1 ATOM 3037 O O . GLU B 2 64 ? 40.438 -25.380 -18.438 1.00 93.40 ? 64 GLU B O 1 ATOM 3038 C CB . GLU B 2 64 ? 38.228 -25.180 -20.440 1.00 101.96 ? 64 GLU B CB 1 ATOM 3039 C CG . GLU B 2 64 ? 37.512 -25.529 -21.734 1.00 105.69 ? 64 GLU B CG 1 ATOM 3040 C CD . GLU B 2 64 ? 36.117 -26.081 -21.493 1.00 111.53 ? 64 GLU B CD 1 ATOM 3041 O OE1 . GLU B 2 64 ? 35.561 -25.850 -20.396 1.00 109.15 ? 64 GLU B OE1 1 ATOM 3042 O OE2 . GLU B 2 64 ? 35.578 -26.748 -22.403 1.00 115.80 ? 64 GLU B OE2 1 ATOM 3043 N N . ALA B 2 65 ? 40.590 -23.197 -18.962 1.00 96.66 ? 65 ALA B N 1 ATOM 3044 C CA . ALA B 2 65 ? 41.172 -22.815 -17.679 1.00 95.96 ? 65 ALA B CA 1 ATOM 3045 C C . ALA B 2 65 ? 40.095 -22.720 -16.592 1.00 98.85 ? 65 ALA B C 1 ATOM 3046 O O . ALA B 2 65 ? 38.935 -22.399 -16.874 1.00 93.84 ? 65 ALA B O 1 ATOM 3047 C CB . ALA B 2 65 ? 41.919 -21.495 -17.811 1.00 94.37 ? 65 ALA B CB 1 ATOM 3048 N N . VAL B 2 66 ? 40.494 -23.015 -15.356 1.00 99.56 ? 66 VAL B N 1 ATOM 3049 C CA . VAL B 2 66 ? 39.606 -22.946 -14.199 1.00 102.46 ? 66 VAL B CA 1 ATOM 3050 C C . VAL B 2 66 ? 40.294 -22.155 -13.088 1.00 100.06 ? 66 VAL B C 1 ATOM 3051 O O . VAL B 2 66 ? 41.519 -22.185 -12.964 1.00 101.01 ? 66 VAL B O 1 ATOM 3052 C CB . VAL B 2 66 ? 39.226 -24.360 -13.701 1.00 107.04 ? 66 VAL B CB 1 ATOM 3053 C CG1 . VAL B 2 66 ? 38.450 -24.302 -12.388 1.00 113.38 ? 66 VAL B CG1 1 ATOM 3054 C CG2 . VAL B 2 66 ? 38.400 -25.085 -14.754 1.00 110.84 ? 66 VAL B CG2 1 ATOM 3055 N N . GLY B 2 67 ? 39.500 -21.442 -12.291 1.00 100.16 ? 67 GLY B N 1 ATOM 3056 C CA . GLY B 2 67 ? 40.018 -20.672 -11.166 1.00 97.34 ? 67 GLY B CA 1 ATOM 3057 C C . GLY B 2 67 ? 40.452 -21.546 -10.000 1.00 94.59 ? 67 GLY B C 1 ATOM 3058 O O . GLY B 2 67 ? 39.697 -22.406 -9.540 1.00 96.96 ? 67 GLY B O 1 ATOM 3059 N N . ARG B 2 68 ? 41.683 -21.332 -9.539 1.00 87.94 ? 68 ARG B N 1 ATOM 3060 C CA . ARG B 2 68 ? 42.200 -21.963 -8.326 1.00 87.14 ? 68 ARG B CA 1 ATOM 3061 C C . ARG B 2 68 ? 42.985 -20.928 -7.538 1.00 87.45 ? 68 ARG B C 1 ATOM 3062 O O . ARG B 2 68 ? 43.823 -20.217 -8.099 1.00 88.36 ? 68 ARG B O 1 ATOM 3063 C CB . ARG B 2 68 ? 43.135 -23.118 -8.656 1.00 83.96 ? 68 ARG B CB 1 ATOM 3064 C CG . ARG B 2 68 ? 42.477 -24.284 -9.353 1.00 84.23 ? 68 ARG B CG 1 ATOM 3065 C CD . ARG B 2 68 ? 43.472 -25.405 -9.591 1.00 81.80 ? 68 ARG B CD 1 ATOM 3066 N NE . ARG B 2 68 ? 43.007 -26.281 -10.657 1.00 82.62 ? 68 ARG B NE 1 ATOM 3067 C CZ . ARG B 2 68 ? 43.124 -26.019 -11.957 1.00 79.78 ? 68 ARG B CZ 1 ATOM 3068 N NH1 . ARG B 2 68 ? 43.716 -24.916 -12.395 1.00 75.87 ? 68 ARG B NH1 1 ATOM 3069 N NH2 . ARG B 2 68 ? 42.641 -26.878 -12.835 1.00 85.60 ? 68 ARG B NH2 1 ATOM 3070 N N . GLU B 2 69 ? 42.727 -20.863 -6.237 1.00 86.26 ? 69 GLU B N 1 ATOM 3071 C CA . GLU B 2 69 ? 43.392 -19.907 -5.374 1.00 83.51 ? 69 GLU B CA 1 ATOM 3072 C C . GLU B 2 69 ? 44.339 -20.612 -4.429 1.00 76.91 ? 69 GLU B C 1 ATOM 3073 O O . GLU B 2 69 ? 44.149 -21.778 -4.100 1.00 74.24 ? 69 GLU B O 1 ATOM 3074 C CB . GLU B 2 69 ? 42.355 -19.091 -4.612 1.00 91.98 ? 69 GLU B CB 1 ATOM 3075 C CG . GLU B 2 69 ? 41.706 -18.038 -5.494 1.00 97.10 ? 69 GLU B CG 1 ATOM 3076 C CD . GLU B 2 69 ? 40.370 -17.570 -4.969 1.00 105.13 ? 69 GLU B CD 1 ATOM 3077 O OE1 . GLU B 2 69 ? 39.348 -18.219 -5.290 1.00 109.47 ? 69 GLU B OE1 1 ATOM 3078 O OE2 . GLU B 2 69 ? 40.349 -16.557 -4.237 1.00 109.37 ? 69 GLU B OE2 1 ATOM 3079 N N . PHE B 2 70 ? 45.372 -19.891 -4.013 1.00 75.00 ? 70 PHE B N 1 ATOM 3080 C CA . PHE B 2 70 ? 46.423 -20.440 -3.168 1.00 73.20 ? 70 PHE B CA 1 ATOM 3081 C C . PHE B 2 70 ? 46.864 -19.390 -2.166 1.00 74.06 ? 70 PHE B C 1 ATOM 3082 O O . PHE B 2 70 ? 46.867 -18.202 -2.474 1.00 74.35 ? 70 PHE B O 1 ATOM 3083 C CB . PHE B 2 70 ? 47.606 -20.865 -4.033 1.00 70.71 ? 70 PHE B CB 1 ATOM 3084 C CG . PHE B 2 70 ? 47.243 -21.841 -5.120 1.00 68.58 ? 70 PHE B CG 1 ATOM 3085 C CD1 . PHE B 2 70 ? 47.194 -23.202 -4.861 1.00 67.03 ? 70 PHE B CD1 1 ATOM 3086 C CD2 . PHE B 2 70 ? 46.945 -21.394 -6.404 1.00 67.86 ? 70 PHE B CD2 1 ATOM 3087 C CE1 . PHE B 2 70 ? 46.856 -24.102 -5.860 1.00 67.28 ? 70 PHE B CE1 1 ATOM 3088 C CE2 . PHE B 2 70 ? 46.602 -22.289 -7.406 1.00 66.43 ? 70 PHE B CE2 1 ATOM 3089 C CZ . PHE B 2 70 ? 46.560 -23.645 -7.133 1.00 66.25 ? 70 PHE B CZ 1 ATOM 3090 N N . ASN B 2 71 ? 47.229 -19.820 -0.963 1.00 76.70 ? 71 ASN B N 1 ATOM 3091 C CA . ASN B 2 71 ? 47.609 -18.873 0.089 1.00 78.11 ? 71 ASN B CA 1 ATOM 3092 C C . ASN B 2 71 ? 49.053 -18.415 -0.087 1.00 76.63 ? 71 ASN B C 1 ATOM 3093 O O . ASN B 2 71 ? 49.724 -18.814 -1.035 1.00 74.79 ? 71 ASN B O 1 ATOM 3094 C CB . ASN B 2 71 ? 47.340 -19.448 1.496 1.00 81.24 ? 71 ASN B CB 1 ATOM 3095 C CG . ASN B 2 71 ? 48.347 -20.507 1.918 1.00 80.78 ? 71 ASN B CG 1 ATOM 3096 O OD1 . ASN B 2 71 ? 49.543 -20.390 1.666 1.00 82.22 ? 71 ASN B OD1 1 ATOM 3097 N ND2 . ASN B 2 71 ? 47.863 -21.540 2.586 1.00 84.34 ? 71 ASN B ND2 1 ATOM 3098 N N . ASN B 2 72 ? 49.531 -17.588 0.835 1.00 81.29 ? 72 ASN B N 1 ATOM 3099 C CA . ASN B 2 72 ? 50.851 -16.979 0.714 1.00 81.91 ? 72 ASN B CA 1 ATOM 3100 C C . ASN B 2 72 ? 52.023 -17.968 0.810 1.00 78.89 ? 72 ASN B C 1 ATOM 3101 O O . ASN B 2 72 ? 53.123 -17.656 0.353 1.00 81.18 ? 72 ASN B O 1 ATOM 3102 C CB . ASN B 2 72 ? 51.012 -15.871 1.764 1.00 87.02 ? 72 ASN B CB 1 ATOM 3103 C CG . ASN B 2 72 ? 52.233 -15.008 1.516 1.00 88.62 ? 72 ASN B CG 1 ATOM 3104 O OD1 . ASN B 2 72 ? 52.559 -14.692 0.374 1.00 91.70 ? 72 ASN B OD1 1 ATOM 3105 N ND2 . ASN B 2 72 ? 52.919 -14.627 2.587 1.00 92.26 ? 72 ASN B ND2 1 ATOM 3106 N N . LEU B 2 73 ? 51.793 -19.139 1.405 1.00 76.15 ? 73 LEU B N 1 ATOM 3107 C CA . LEU B 2 73 ? 52.817 -20.188 1.495 1.00 74.99 ? 73 LEU B CA 1 ATOM 3108 C C . LEU B 2 73 ? 52.512 -21.396 0.582 1.00 72.58 ? 73 LEU B C 1 ATOM 3109 O O . LEU B 2 73 ? 52.892 -22.537 0.881 1.00 71.79 ? 73 LEU B O 1 ATOM 3110 C CB . LEU B 2 73 ? 52.982 -20.630 2.952 1.00 79.10 ? 73 LEU B CB 1 ATOM 3111 C CG . LEU B 2 73 ? 53.527 -19.568 3.922 1.00 81.80 ? 73 LEU B CG 1 ATOM 3112 C CD1 . LEU B 2 73 ? 53.383 -20.045 5.357 1.00 83.19 ? 73 LEU B CD1 1 ATOM 3113 C CD2 . LEU B 2 73 ? 54.981 -19.212 3.615 1.00 80.66 ? 73 LEU B CD2 1 ATOM 3114 N N . GLU B 2 74 ? 51.834 -21.125 -0.533 1.00 69.08 ? 74 GLU B N 1 ATOM 3115 C CA . GLU B 2 74 ? 51.601 -22.109 -1.584 1.00 66.94 ? 74 GLU B CA 1 ATOM 3116 C C . GLU B 2 74 ? 52.006 -21.506 -2.930 1.00 64.91 ? 74 GLU B C 1 ATOM 3117 O O . GLU B 2 74 ? 51.368 -21.754 -3.953 1.00 63.14 ? 74 GLU B O 1 ATOM 3118 C CB . GLU B 2 74 ? 50.126 -22.519 -1.605 1.00 68.52 ? 74 GLU B CB 1 ATOM 3119 C CG . GLU B 2 74 ? 49.673 -23.321 -0.396 1.00 71.85 ? 74 GLU B CG 1 ATOM 3120 C CD . GLU B 2 74 ? 48.171 -23.574 -0.387 1.00 76.46 ? 74 GLU B CD 1 ATOM 3121 O OE1 . GLU B 2 74 ? 47.408 -22.729 -0.907 1.00 78.69 ? 74 GLU B OE1 1 ATOM 3122 O OE2 . GLU B 2 74 ? 47.741 -24.619 0.143 1.00 77.93 ? 74 GLU B OE2 1 ATOM 3123 N N . ARG B 2 75 ? 53.074 -20.714 -2.925 1.00 67.04 ? 75 ARG B N 1 ATOM 3124 C CA . ARG B 2 75 ? 53.507 -20.003 -4.122 1.00 67.14 ? 75 ARG B CA 1 ATOM 3125 C C . ARG B 2 75 ? 54.027 -20.939 -5.201 1.00 64.25 ? 75 ARG B C 1 ATOM 3126 O O . ARG B 2 75 ? 53.844 -20.685 -6.380 1.00 65.99 ? 75 ARG B O 1 ATOM 3127 C CB . ARG B 2 75 ? 54.588 -18.970 -3.779 1.00 74.01 ? 75 ARG B CB 1 ATOM 3128 C CG . ARG B 2 75 ? 54.109 -17.803 -2.927 1.00 80.81 ? 75 ARG B CG 1 ATOM 3129 C CD . ARG B 2 75 ? 53.002 -17.021 -3.619 1.00 88.33 ? 75 ARG B CD 1 ATOM 3130 N NE . ARG B 2 75 ? 52.663 -15.782 -2.923 1.00 100.10 ? 75 ARG B NE 1 ATOM 3131 C CZ . ARG B 2 75 ? 51.691 -14.950 -3.293 1.00 105.92 ? 75 ARG B CZ 1 ATOM 3132 N NH1 . ARG B 2 75 ? 50.945 -15.217 -4.364 1.00 105.42 ? 75 ARG B NH1 1 ATOM 3133 N NH2 . ARG B 2 75 ? 51.462 -13.842 -2.590 1.00 108.37 ? 75 ARG B NH2 1 ATOM 3134 N N . ARG B 2 76 ? 54.689 -22.017 -4.807 1.00 64.84 ? 76 ARG B N 1 ATOM 3135 C CA . ARG B 2 76 ? 55.222 -22.963 -5.780 1.00 63.22 ? 76 ARG B CA 1 ATOM 3136 C C . ARG B 2 76 ? 54.124 -23.597 -6.633 1.00 63.18 ? 76 ARG B C 1 ATOM 3137 O O . ARG B 2 76 ? 54.188 -23.536 -7.853 1.00 63.36 ? 76 ARG B O 1 ATOM 3138 C CB . ARG B 2 76 ? 56.018 -24.045 -5.076 1.00 64.35 ? 76 ARG B CB 1 ATOM 3139 C CG . ARG B 2 76 ? 57.323 -23.563 -4.487 1.00 64.36 ? 76 ARG B CG 1 ATOM 3140 C CD . ARG B 2 76 ? 57.949 -24.696 -3.700 1.00 66.73 ? 76 ARG B CD 1 ATOM 3141 N NE . ARG B 2 76 ? 57.126 -25.022 -2.542 1.00 64.43 ? 76 ARG B NE 1 ATOM 3142 C CZ . ARG B 2 76 ? 57.101 -26.196 -1.926 1.00 65.85 ? 76 ARG B CZ 1 ATOM 3143 N NH1 . ARG B 2 76 ? 57.857 -27.202 -2.341 1.00 70.81 ? 76 ARG B NH1 1 ATOM 3144 N NH2 . ARG B 2 76 ? 56.301 -26.364 -0.887 1.00 65.48 ? 76 ARG B NH2 1 ATOM 3145 N N . ILE B 2 77 ? 53.122 -24.199 -5.995 1.00 65.40 ? 77 ILE B N 1 ATOM 3146 C CA . ILE B 2 77 ? 51.995 -24.779 -6.731 1.00 67.02 ? 77 ILE B CA 1 ATOM 3147 C C . ILE B 2 77 ? 51.104 -23.720 -7.408 1.00 67.82 ? 77 ILE B C 1 ATOM 3148 O O . ILE B 2 77 ? 50.461 -24.004 -8.423 1.00 68.60 ? 77 ILE B O 1 ATOM 3149 C CB . ILE B 2 77 ? 51.137 -25.727 -5.869 1.00 69.05 ? 77 ILE B CB 1 ATOM 3150 C CG1 . ILE B 2 77 ? 50.432 -24.976 -4.743 1.00 74.36 ? 77 ILE B CG1 1 ATOM 3151 C CG2 . ILE B 2 77 ? 51.992 -26.850 -5.302 1.00 72.78 ? 77 ILE B CG2 1 ATOM 3152 C CD1 . ILE B 2 77 ? 49.610 -25.879 -3.841 1.00 79.54 ? 77 ILE B CD1 1 ATOM 3153 N N . GLU B 2 78 ? 51.058 -22.508 -6.868 1.00 65.23 ? 78 GLU B N 1 ATOM 3154 C CA . GLU B 2 78 ? 50.370 -21.429 -7.560 1.00 64.86 ? 78 GLU B CA 1 ATOM 3155 C C . GLU B 2 78 ? 51.084 -21.170 -8.884 1.00 64.12 ? 78 GLU B C 1 ATOM 3156 O O . GLU B 2 78 ? 50.442 -20.989 -9.925 1.00 62.50 ? 78 GLU B O 1 ATOM 3157 C CB . GLU B 2 78 ? 50.339 -20.158 -6.715 1.00 70.66 ? 78 GLU B CB 1 ATOM 3158 C CG . GLU B 2 78 ? 49.805 -18.931 -7.442 1.00 77.71 ? 78 GLU B CG 1 ATOM 3159 C CD . GLU B 2 78 ? 49.588 -17.744 -6.517 1.00 89.34 ? 78 GLU B CD 1 ATOM 3160 O OE1 . GLU B 2 78 ? 50.436 -17.496 -5.625 1.00 96.82 ? 78 GLU B OE1 1 ATOM 3161 O OE2 . GLU B 2 78 ? 48.563 -17.049 -6.684 1.00 97.36 ? 78 GLU B OE2 1 ATOM 3162 N N . ASN B 2 79 ? 52.413 -21.166 -8.838 1.00 61.60 ? 79 ASN B N 1 ATOM 3163 C CA . ASN B 2 79 ? 53.219 -20.905 -10.013 1.00 63.35 ? 79 ASN B CA 1 ATOM 3164 C C . ASN B 2 79 ? 53.113 -22.058 -10.998 1.00 63.00 ? 79 ASN B C 1 ATOM 3165 O O . ASN B 2 79 ? 53.061 -21.850 -12.207 1.00 64.00 ? 79 ASN B O 1 ATOM 3166 C CB . ASN B 2 79 ? 54.675 -20.695 -9.616 1.00 67.97 ? 79 ASN B CB 1 ATOM 3167 C CG . ASN B 2 79 ? 55.530 -20.245 -10.776 1.00 73.22 ? 79 ASN B CG 1 ATOM 3168 O OD1 . ASN B 2 79 ? 55.220 -19.259 -11.439 1.00 80.30 ? 79 ASN B OD1 1 ATOM 3169 N ND2 . ASN B 2 79 ? 56.620 -20.953 -11.021 1.00 77.81 ? 79 ASN B ND2 1 ATOM 3170 N N . LEU B 2 80 ? 53.074 -23.273 -10.465 1.00 63.05 ? 80 LEU B N 1 ATOM 3171 C CA . LEU B 2 80 ? 52.896 -24.473 -11.267 1.00 63.36 ? 80 LEU B CA 1 ATOM 3172 C C . LEU B 2 80 ? 51.589 -24.361 -12.021 1.00 62.57 ? 80 LEU B C 1 ATOM 3173 O O . LEU B 2 80 ? 51.523 -24.633 -13.214 1.00 62.16 ? 80 LEU B O 1 ATOM 3174 C CB . LEU B 2 80 ? 52.869 -25.702 -10.358 1.00 66.22 ? 80 LEU B CB 1 ATOM 3175 C CG . LEU B 2 80 ? 53.185 -27.061 -10.965 1.00 69.72 ? 80 LEU B CG 1 ATOM 3176 C CD1 . LEU B 2 80 ? 53.339 -28.102 -9.869 1.00 72.26 ? 80 LEU B CD1 1 ATOM 3177 C CD2 . LEU B 2 80 ? 52.107 -27.475 -11.946 1.00 73.20 ? 80 LEU B CD2 1 ATOM 3178 N N . ASN B 2 81 ? 50.548 -23.943 -11.309 1.00 65.64 ? 81 ASN B N 1 ATOM 3179 C CA . ASN B 2 81 ? 49.216 -23.800 -11.885 1.00 64.08 ? 81 ASN B CA 1 ATOM 3180 C C . ASN B 2 81 ? 49.196 -22.763 -12.983 1.00 64.11 ? 81 ASN B C 1 ATOM 3181 O O . ASN B 2 81 ? 48.576 -22.968 -14.014 1.00 62.92 ? 81 ASN B O 1 ATOM 3182 C CB . ASN B 2 81 ? 48.214 -23.398 -10.812 1.00 65.83 ? 81 ASN B CB 1 ATOM 3183 C CG . ASN B 2 81 ? 46.817 -23.233 -11.358 1.00 66.70 ? 81 ASN B CG 1 ATOM 3184 O OD1 . ASN B 2 81 ? 46.148 -24.213 -11.686 1.00 69.46 ? 81 ASN B OD1 1 ATOM 3185 N ND2 . ASN B 2 81 ? 46.366 -21.992 -11.456 1.00 64.88 ? 81 ASN B ND2 1 ATOM 3186 N N . LYS B 2 82 ? 49.877 -21.648 -12.747 1.00 66.89 ? 82 LYS B N 1 ATOM 3187 C CA . LYS B 2 82 ? 49.911 -20.562 -13.706 1.00 70.16 ? 82 LYS B CA 1 ATOM 3188 C C . LYS B 2 82 ? 50.606 -21.022 -14.979 1.00 69.54 ? 82 LYS B C 1 ATOM 3189 O O . LYS B 2 82 ? 50.117 -20.784 -16.076 1.00 66.96 ? 82 LYS B O 1 ATOM 3190 C CB . LYS B 2 82 ? 50.641 -19.354 -13.122 1.00 76.32 ? 82 LYS B CB 1 ATOM 3191 C CG . LYS B 2 82 ? 50.498 -18.079 -13.944 1.00 86.02 ? 82 LYS B CG 1 ATOM 3192 C CD . LYS B 2 82 ? 51.532 -17.038 -13.525 1.00 96.03 ? 82 LYS B CD 1 ATOM 3193 C CE . LYS B 2 82 ? 51.282 -15.679 -14.167 1.00 103.99 ? 82 LYS B CE 1 ATOM 3194 N NZ . LYS B 2 82 ? 51.147 -15.744 -15.653 1.00 106.11 ? 82 LYS B NZ 1 ATOM 3195 N N . LYS B 2 83 ? 51.745 -21.688 -14.815 1.00 70.01 ? 83 LYS B N 1 ATOM 3196 C CA . LYS B 2 83 ? 52.560 -22.129 -15.942 1.00 72.60 ? 83 LYS B CA 1 ATOM 3197 C C . LYS B 2 83 ? 51.879 -23.220 -16.753 1.00 67.94 ? 83 LYS B C 1 ATOM 3198 O O . LYS B 2 83 ? 52.022 -23.268 -17.971 1.00 68.35 ? 83 LYS B O 1 ATOM 3199 C CB . LYS B 2 83 ? 53.925 -22.600 -15.446 1.00 79.23 ? 83 LYS B CB 1 ATOM 3200 C CG . LYS B 2 83 ? 54.826 -21.443 -15.044 1.00 87.20 ? 83 LYS B CG 1 ATOM 3201 C CD . LYS B 2 83 ? 55.875 -21.123 -16.100 1.00 98.87 ? 83 LYS B CD 1 ATOM 3202 C CE . LYS B 2 83 ? 57.218 -21.792 -15.801 1.00 107.88 ? 83 LYS B CE 1 ATOM 3203 N NZ . LYS B 2 83 ? 57.313 -23.249 -16.119 1.00 108.25 ? 83 LYS B NZ 1 ATOM 3204 N N . MET B 2 84 ? 51.136 -24.088 -16.077 1.00 65.19 ? 84 MET B N 1 ATOM 3205 C CA . MET B 2 84 ? 50.322 -25.080 -16.757 1.00 64.93 ? 84 MET B CA 1 ATOM 3206 C C . MET B 2 84 ? 49.249 -24.420 -17.614 1.00 60.19 ? 84 MET B C 1 ATOM 3207 O O . MET B 2 84 ? 49.128 -24.737 -18.800 1.00 62.37 ? 84 MET B O 1 ATOM 3208 C CB . MET B 2 84 ? 49.648 -26.015 -15.757 1.00 68.72 ? 84 MET B CB 1 ATOM 3209 C CG . MET B 2 84 ? 49.011 -27.224 -16.421 1.00 74.62 ? 84 MET B CG 1 ATOM 3210 S SD . MET B 2 84 ? 47.574 -27.861 -15.559 1.00 81.94 ? 84 MET B SD 1 ATOM 3211 C CE . MET B 2 84 ? 46.464 -26.462 -15.611 1.00 80.93 ? 84 MET B CE 1 ATOM 3212 N N . GLU B 2 85 ? 48.480 -23.510 -17.020 1.00 77.64 ? 85 GLU B N 1 ATOM 3213 C CA . GLU B 2 85 ? 47.379 -22.859 -17.730 1.00 76.78 ? 85 GLU B CA 1 ATOM 3214 C C . GLU B 2 85 ? 47.930 -22.150 -18.959 1.00 72.99 ? 85 GLU B C 1 ATOM 3215 O O . GLU B 2 85 ? 47.475 -22.383 -20.077 1.00 70.37 ? 85 GLU B O 1 ATOM 3216 C CB . GLU B 2 85 ? 46.642 -21.857 -16.840 1.00 81.75 ? 85 GLU B CB 1 ATOM 3217 C CG . GLU B 2 85 ? 46.074 -22.424 -15.537 1.00 88.04 ? 85 GLU B CG 1 ATOM 3218 C CD . GLU B 2 85 ? 44.621 -22.864 -15.620 1.00 92.14 ? 85 GLU B CD 1 ATOM 3219 O OE1 . GLU B 2 85 ? 44.344 -23.867 -16.306 1.00 94.98 ? 85 GLU B OE1 1 ATOM 3220 O OE2 . GLU B 2 85 ? 43.758 -22.221 -14.982 1.00 96.22 ? 85 GLU B OE2 1 ATOM 3221 N N . ASP B 2 86 ? 48.940 -21.316 -18.740 1.00 71.81 ? 86 ASP B N 1 ATOM 3222 C CA . ASP B 2 86 ? 49.565 -20.545 -19.809 1.00 71.25 ? 86 ASP B CA 1 ATOM 3223 C C . ASP B 2 86 ? 50.183 -21.408 -20.881 1.00 66.87 ? 86 ASP B C 1 ATOM 3224 O O . ASP B 2 86 ? 50.106 -21.077 -22.059 1.00 66.90 ? 86 ASP B O 1 ATOM 3225 C CB . ASP B 2 86 ? 50.654 -19.629 -19.250 1.00 75.08 ? 86 ASP B CB 1 ATOM 3226 C CG . ASP B 2 86 ? 50.118 -18.303 -18.823 1.00 81.00 ? 86 ASP B CG 1 ATOM 3227 O OD1 . ASP B 2 86 ? 49.355 -17.697 -19.612 1.00 86.52 ? 86 ASP B OD1 1 ATOM 3228 O OD2 . ASP B 2 86 ? 50.462 -17.858 -17.709 1.00 86.54 ? 86 ASP B OD2 1 ATOM 3229 N N . GLY B 2 87 ? 50.814 -22.496 -20.465 1.00 63.63 ? 87 GLY B N 1 ATOM 3230 C CA . GLY B 2 87 ? 51.428 -23.426 -21.393 1.00 62.01 ? 87 GLY B CA 1 ATOM 3231 C C . GLY B 2 87 ? 50.448 -23.969 -22.408 1.00 59.96 ? 87 GLY B C 1 ATOM 3232 O O . GLY B 2 87 ? 50.744 -24.011 -23.597 1.00 58.78 ? 87 GLY B O 1 ATOM 3233 N N . PHE B 2 88 ? 49.275 -24.381 -21.944 1.00 60.55 ? 88 PHE B N 1 ATOM 3234 C CA . PHE B 2 88 ? 48.253 -24.912 -22.844 1.00 60.30 ? 88 PHE B CA 1 ATOM 3235 C C . PHE B 2 88 ? 47.672 -23.830 -23.759 1.00 60.99 ? 88 PHE B C 1 ATOM 3236 O O . PHE B 2 88 ? 47.459 -24.083 -24.946 1.00 60.96 ? 88 PHE B O 1 ATOM 3237 C CB . PHE B 2 88 ? 47.142 -25.614 -22.059 1.00 61.11 ? 88 PHE B CB 1 ATOM 3238 C CG . PHE B 2 88 ? 47.529 -26.971 -21.550 1.00 60.95 ? 88 PHE B CG 1 ATOM 3239 C CD1 . PHE B 2 88 ? 47.831 -27.993 -22.433 1.00 60.98 ? 88 PHE B CD1 1 ATOM 3240 C CD2 . PHE B 2 88 ? 47.586 -27.232 -20.191 1.00 62.48 ? 88 PHE B CD2 1 ATOM 3241 C CE1 . PHE B 2 88 ? 48.190 -29.251 -21.975 1.00 62.03 ? 88 PHE B CE1 1 ATOM 3242 C CE2 . PHE B 2 88 ? 47.935 -28.488 -19.725 1.00 63.45 ? 88 PHE B CE2 1 ATOM 3243 C CZ . PHE B 2 88 ? 48.241 -29.499 -20.619 1.00 63.90 ? 88 PHE B CZ 1 ATOM 3244 N N . LEU B 2 89 ? 47.436 -22.630 -23.233 1.00 63.00 ? 89 LEU B N 1 ATOM 3245 C CA . LEU B 2 89 ? 46.976 -21.519 -24.076 1.00 65.35 ? 89 LEU B CA 1 ATOM 3246 C C . LEU B 2 89 ? 47.961 -21.240 -25.218 1.00 63.43 ? 89 LEU B C 1 ATOM 3247 O O . LEU B 2 89 ? 47.562 -21.029 -26.356 1.00 61.07 ? 89 LEU B O 1 ATOM 3248 C CB . LEU B 2 89 ? 46.783 -20.239 -23.266 1.00 70.18 ? 89 LEU B CB 1 ATOM 3249 C CG . LEU B 2 89 ? 45.776 -20.245 -22.108 1.00 76.73 ? 89 LEU B CG 1 ATOM 3250 C CD1 . LEU B 2 89 ? 45.799 -18.874 -21.434 1.00 80.69 ? 89 LEU B CD1 1 ATOM 3251 C CD2 . LEU B 2 89 ? 44.359 -20.636 -22.542 1.00 77.75 ? 89 LEU B CD2 1 ATOM 3252 N N . ASP B 2 90 ? 49.250 -21.243 -24.907 1.00 64.17 ? 90 ASP B N 1 ATOM 3253 C CA . ASP B 2 90 ? 50.277 -21.032 -25.918 1.00 64.30 ? 90 ASP B CA 1 ATOM 3254 C C . ASP B 2 90 ? 50.291 -22.157 -26.960 1.00 61.61 ? 90 ASP B C 1 ATOM 3255 O O . ASP B 2 90 ? 50.467 -21.907 -28.147 1.00 62.46 ? 90 ASP B O 1 ATOM 3256 C CB . ASP B 2 90 ? 51.650 -20.873 -25.258 1.00 66.48 ? 90 ASP B CB 1 ATOM 3257 C CG . ASP B 2 90 ? 51.782 -19.558 -24.496 1.00 73.08 ? 90 ASP B CG 1 ATOM 3258 O OD1 . ASP B 2 90 ? 50.879 -18.694 -24.611 1.00 75.17 ? 90 ASP B OD1 1 ATOM 3259 O OD2 . ASP B 2 90 ? 52.792 -19.381 -23.779 1.00 78.96 ? 90 ASP B OD2 1 ATOM 3260 N N . VAL B 2 91 ? 50.090 -23.390 -26.517 1.00 59.42 ? 91 VAL B N 1 ATOM 3261 C CA . VAL B 2 91 ? 50.029 -24.519 -27.431 1.00 57.61 ? 91 VAL B CA 1 ATOM 3262 C C . VAL B 2 91 ? 48.822 -24.377 -28.365 1.00 56.81 ? 91 VAL B C 1 ATOM 3263 O O . VAL B 2 91 ? 48.957 -24.509 -29.580 1.00 57.81 ? 91 VAL B O 1 ATOM 3264 C CB . VAL B 2 91 ? 49.977 -25.862 -26.668 1.00 56.88 ? 91 VAL B CB 1 ATOM 3265 C CG1 . VAL B 2 91 ? 49.657 -27.013 -27.609 1.00 56.43 ? 91 VAL B CG1 1 ATOM 3266 C CG2 . VAL B 2 91 ? 51.302 -26.110 -25.960 1.00 57.73 ? 91 VAL B CG2 1 ATOM 3267 N N . TRP B 2 92 ? 47.652 -24.093 -27.806 1.00 56.17 ? 92 TRP B N 1 ATOM 3268 C CA . TRP B 2 92 ? 46.450 -23.953 -28.632 1.00 55.84 ? 92 TRP B CA 1 ATOM 3269 C C . TRP B 2 92 ? 46.472 -22.703 -29.517 1.00 55.16 ? 92 TRP B C 1 ATOM 3270 O O . TRP B 2 92 ? 46.008 -22.738 -30.653 1.00 55.04 ? 92 TRP B O 1 ATOM 3271 C CB . TRP B 2 92 ? 45.198 -24.018 -27.768 1.00 56.42 ? 92 TRP B CB 1 ATOM 3272 C CG . TRP B 2 92 ? 44.978 -25.403 -27.246 1.00 57.67 ? 92 TRP B CG 1 ATOM 3273 C CD1 . TRP B 2 92 ? 45.098 -25.825 -25.958 1.00 58.68 ? 92 TRP B CD1 1 ATOM 3274 C CD2 . TRP B 2 92 ? 44.644 -26.563 -28.015 1.00 57.78 ? 92 TRP B CD2 1 ATOM 3275 N NE1 . TRP B 2 92 ? 44.836 -27.168 -25.872 1.00 59.68 ? 92 TRP B NE1 1 ATOM 3276 C CE2 . TRP B 2 92 ? 44.556 -27.644 -27.124 1.00 59.49 ? 92 TRP B CE2 1 ATOM 3277 C CE3 . TRP B 2 92 ? 44.396 -26.787 -29.372 1.00 58.28 ? 92 TRP B CE3 1 ATOM 3278 C CZ2 . TRP B 2 92 ? 44.225 -28.931 -27.543 1.00 61.74 ? 92 TRP B CZ2 1 ATOM 3279 C CZ3 . TRP B 2 92 ? 44.062 -28.063 -29.785 1.00 58.81 ? 92 TRP B CZ3 1 ATOM 3280 C CH2 . TRP B 2 92 ? 43.977 -29.117 -28.874 1.00 61.10 ? 92 TRP B CH2 1 ATOM 3281 N N . THR B 2 93 ? 47.037 -21.614 -29.019 1.00 55.38 ? 93 THR B N 1 ATOM 3282 C CA . THR B 2 93 ? 47.201 -20.430 -29.838 1.00 56.64 ? 93 THR B CA 1 ATOM 3283 C C . THR B 2 93 ? 48.073 -20.762 -31.048 1.00 56.28 ? 93 THR B C 1 ATOM 3284 O O . THR B 2 93 ? 47.721 -20.417 -32.173 1.00 57.31 ? 93 THR B O 1 ATOM 3285 C CB . THR B 2 93 ? 47.785 -19.252 -29.040 1.00 58.14 ? 93 THR B CB 1 ATOM 3286 O OG1 . THR B 2 93 ? 46.880 -18.911 -27.983 1.00 59.94 ? 93 THR B OG1 1 ATOM 3287 C CG2 . THR B 2 93 ? 47.958 -18.040 -29.918 1.00 59.69 ? 93 THR B CG2 1 ATOM 3288 N N . TYR B 2 94 ? 49.184 -21.457 -30.814 1.00 56.66 ? 94 TYR B N 1 ATOM 3289 C CA . TYR B 2 94 ? 50.087 -21.879 -31.888 1.00 55.66 ? 94 TYR B CA 1 ATOM 3290 C C . TYR B 2 94 ? 49.347 -22.751 -32.889 1.00 54.39 ? 94 TYR B C 1 ATOM 3291 O O . TYR B 2 94 ? 49.366 -22.485 -34.085 1.00 52.61 ? 94 TYR B O 1 ATOM 3292 C CB . TYR B 2 94 ? 51.312 -22.604 -31.312 1.00 56.69 ? 94 TYR B CB 1 ATOM 3293 C CG . TYR B 2 94 ? 52.180 -23.299 -32.341 1.00 58.36 ? 94 TYR B CG 1 ATOM 3294 C CD1 . TYR B 2 94 ? 51.919 -24.625 -32.721 1.00 58.06 ? 94 TYR B CD1 1 ATOM 3295 C CD2 . TYR B 2 94 ? 53.264 -22.652 -32.930 1.00 59.07 ? 94 TYR B CD2 1 ATOM 3296 C CE1 . TYR B 2 94 ? 52.699 -25.271 -33.659 1.00 57.34 ? 94 TYR B CE1 1 ATOM 3297 C CE2 . TYR B 2 94 ? 54.052 -23.297 -33.873 1.00 60.01 ? 94 TYR B CE2 1 ATOM 3298 C CZ . TYR B 2 94 ? 53.759 -24.609 -34.233 1.00 59.65 ? 94 TYR B CZ 1 ATOM 3299 O OH . TYR B 2 94 ? 54.525 -25.275 -35.161 1.00 62.75 ? 94 TYR B OH 1 ATOM 3300 N N . ASN B 2 95 ? 48.664 -23.773 -32.390 1.00 55.97 ? 95 ASN B N 1 ATOM 3301 C CA . ASN B 2 95 ? 47.897 -24.677 -33.249 1.00 55.21 ? 95 ASN B CA 1 ATOM 3302 C C . ASN B 2 95 ? 46.911 -23.945 -34.142 1.00 55.41 ? 95 ASN B C 1 ATOM 3303 O O . ASN B 2 95 ? 46.829 -24.228 -35.336 1.00 56.86 ? 95 ASN B O 1 ATOM 3304 C CB . ASN B 2 95 ? 47.146 -25.718 -32.419 1.00 56.12 ? 95 ASN B CB 1 ATOM 3305 C CG . ASN B 2 95 ? 48.071 -26.758 -31.806 1.00 58.99 ? 95 ASN B CG 1 ATOM 3306 O OD1 . ASN B 2 95 ? 49.269 -26.784 -32.077 1.00 59.07 ? 95 ASN B OD1 1 ATOM 3307 N ND2 . ASN B 2 95 ? 47.508 -27.626 -30.977 1.00 61.49 ? 95 ASN B ND2 1 ATOM 3308 N N . ALA B 2 96 ? 46.158 -23.015 -33.568 1.00 55.94 ? 96 ALA B N 1 ATOM 3309 C CA . ALA B 2 96 ? 45.158 -22.275 -34.335 1.00 56.37 ? 96 ALA B CA 1 ATOM 3310 C C . ALA B 2 96 ? 45.828 -21.426 -35.408 1.00 54.41 ? 96 ALA B C 1 ATOM 3311 O O . ALA B 2 96 ? 45.459 -21.481 -36.570 1.00 52.52 ? 96 ALA B O 1 ATOM 3312 C CB . ALA B 2 96 ? 44.327 -21.392 -33.418 1.00 58.98 ? 96 ALA B CB 1 ATOM 3313 N N . GLU B 2 97 ? 46.827 -20.650 -35.016 1.00 55.92 ? 97 GLU B N 1 ATOM 3314 C CA . GLU B 2 97 ? 47.455 -19.719 -35.949 1.00 58.65 ? 97 GLU B CA 1 ATOM 3315 C C . GLU B 2 97 ? 48.145 -20.445 -37.101 1.00 58.15 ? 97 GLU B C 1 ATOM 3316 O O . GLU B 2 97 ? 48.099 -19.982 -38.241 1.00 58.96 ? 97 GLU B O 1 ATOM 3317 C CB . GLU B 2 97 ? 48.412 -18.780 -35.212 1.00 61.62 ? 97 GLU B CB 1 ATOM 3318 C CG . GLU B 2 97 ? 47.663 -17.700 -34.427 1.00 66.20 ? 97 GLU B CG 1 ATOM 3319 C CD . GLU B 2 97 ? 48.561 -16.834 -33.568 1.00 71.78 ? 97 GLU B CD 1 ATOM 3320 O OE1 . GLU B 2 97 ? 49.787 -17.069 -33.537 1.00 77.81 ? 97 GLU B OE1 1 ATOM 3321 O OE2 . GLU B 2 97 ? 48.045 -15.909 -32.911 1.00 77.57 ? 97 GLU B OE2 1 ATOM 3322 N N . LEU B 2 98 ? 48.744 -21.600 -36.810 1.00 57.25 ? 98 LEU B N 1 ATOM 3323 C CA . LEU B 2 98 ? 49.482 -22.349 -37.815 1.00 56.54 ? 98 LEU B CA 1 ATOM 3324 C C . LEU B 2 98 ? 48.524 -23.016 -38.770 1.00 54.32 ? 98 LEU B C 1 ATOM 3325 O O . LEU B 2 98 ? 48.757 -23.029 -39.976 1.00 53.80 ? 98 LEU B O 1 ATOM 3326 C CB . LEU B 2 98 ? 50.363 -23.409 -37.170 1.00 58.97 ? 98 LEU B CB 1 ATOM 3327 C CG . LEU B 2 98 ? 51.316 -24.137 -38.122 1.00 61.45 ? 98 LEU B CG 1 ATOM 3328 C CD1 . LEU B 2 98 ? 52.433 -23.199 -38.564 1.00 62.54 ? 98 LEU B CD1 1 ATOM 3329 C CD2 . LEU B 2 98 ? 51.888 -25.390 -37.457 1.00 62.58 ? 98 LEU B CD2 1 ATOM 3330 N N . LEU B 2 99 ? 47.446 -23.577 -38.230 1.00 52.58 ? 99 LEU B N 1 ATOM 3331 C CA . LEU B 2 99 ? 46.451 -24.238 -39.057 1.00 52.57 ? 99 LEU B CA 1 ATOM 3332 C C . LEU B 2 99 ? 45.895 -23.240 -40.066 1.00 52.07 ? 99 LEU B C 1 ATOM 3333 O O . LEU B 2 99 ? 45.788 -23.539 -41.257 1.00 51.28 ? 99 LEU B O 1 ATOM 3334 C CB . LEU B 2 99 ? 45.325 -24.818 -38.195 1.00 55.19 ? 99 LEU B CB 1 ATOM 3335 C CG . LEU B 2 99 ? 44.272 -25.663 -38.925 1.00 58.25 ? 99 LEU B CG 1 ATOM 3336 C CD1 . LEU B 2 99 ? 44.902 -26.807 -39.697 1.00 59.18 ? 99 LEU B CD1 1 ATOM 3337 C CD2 . LEU B 2 99 ? 43.247 -26.202 -37.943 1.00 61.36 ? 99 LEU B CD2 1 ATOM 3338 N N . VAL B 2 100 ? 45.571 -22.038 -39.594 1.00 51.47 ? 100 VAL B N 1 ATOM 3339 C CA . VAL B 2 100 ? 45.034 -21.006 -40.472 1.00 49.99 ? 100 VAL B CA 1 ATOM 3340 C C . VAL B 2 100 ? 46.028 -20.623 -41.567 1.00 48.69 ? 100 VAL B C 1 ATOM 3341 O O . VAL B 2 100 ? 45.652 -20.583 -42.741 1.00 47.06 ? 100 VAL B O 1 ATOM 3342 C CB . VAL B 2 100 ? 44.556 -19.785 -39.670 1.00 51.36 ? 100 VAL B CB 1 ATOM 3343 C CG1 . VAL B 2 100 ? 44.314 -18.580 -40.576 1.00 52.52 ? 100 VAL B CG1 1 ATOM 3344 C CG2 . VAL B 2 100 ? 43.283 -20.157 -38.925 1.00 52.54 ? 100 VAL B CG2 1 ATOM 3345 N N . LEU B 2 101 ? 47.280 -20.348 -41.196 1.00 48.82 ? 101 LEU B N 1 ATOM 3346 C CA . LEU B 2 101 ? 48.319 -20.040 -42.189 1.00 49.63 ? 101 LEU B CA 1 ATOM 3347 C C . LEU B 2 101 ? 48.466 -21.174 -43.217 1.00 50.06 ? 101 LEU B C 1 ATOM 3348 O O . LEU B 2 101 ? 48.463 -20.938 -44.421 1.00 51.37 ? 101 LEU B O 1 ATOM 3349 C CB . LEU B 2 101 ? 49.672 -19.791 -41.517 1.00 51.01 ? 101 LEU B CB 1 ATOM 3350 C CG . LEU B 2 101 ? 49.838 -18.521 -40.687 1.00 53.91 ? 101 LEU B CG 1 ATOM 3351 C CD1 . LEU B 2 101 ? 51.250 -18.434 -40.139 1.00 55.77 ? 101 LEU B CD1 1 ATOM 3352 C CD2 . LEU B 2 101 ? 49.527 -17.277 -41.497 1.00 56.24 ? 101 LEU B CD2 1 ATOM 3353 N N . MET B 2 102 ? 48.587 -22.405 -42.741 1.00 50.20 ? 102 MET B N 1 ATOM 3354 C CA . MET B 2 102 ? 48.807 -23.536 -43.636 1.00 51.68 ? 102 MET B CA 1 ATOM 3355 C C . MET B 2 102 ? 47.630 -23.787 -44.555 1.00 51.09 ? 102 MET B C 1 ATOM 3356 O O . MET B 2 102 ? 47.814 -24.037 -45.751 1.00 52.83 ? 102 MET B O 1 ATOM 3357 C CB . MET B 2 102 ? 49.098 -24.798 -42.843 1.00 54.42 ? 102 MET B CB 1 ATOM 3358 C CG . MET B 2 102 ? 50.492 -24.843 -42.252 1.00 58.54 ? 102 MET B CG 1 ATOM 3359 S SD . MET B 2 102 ? 50.695 -26.390 -41.356 1.00 65.12 ? 102 MET B SD 1 ATOM 3360 C CE . MET B 2 102 ? 52.454 -26.648 -41.578 1.00 69.27 ? 102 MET B CE 1 ATOM 3361 N N . GLU B 2 103 ? 46.422 -23.738 -44.012 1.00 50.64 ? 103 GLU B N 1 ATOM 3362 C CA . GLU B 2 103 ? 45.251 -24.054 -44.820 1.00 52.23 ? 103 GLU B CA 1 ATOM 3363 C C . GLU B 2 103 ? 44.850 -22.908 -45.753 1.00 51.70 ? 103 GLU B C 1 ATOM 3364 O O . GLU B 2 103 ? 44.319 -23.157 -46.833 1.00 51.17 ? 103 GLU B O 1 ATOM 3365 C CB . GLU B 2 103 ? 44.097 -24.525 -43.945 1.00 55.47 ? 103 GLU B CB 1 ATOM 3366 C CG . GLU B 2 103 ? 44.367 -25.890 -43.305 1.00 60.16 ? 103 GLU B CG 1 ATOM 3367 C CD . GLU B 2 103 ? 44.463 -27.040 -44.314 1.00 64.19 ? 103 GLU B CD 1 ATOM 3368 O OE1 . GLU B 2 103 ? 43.762 -27.009 -45.353 1.00 65.81 ? 103 GLU B OE1 1 ATOM 3369 O OE2 . GLU B 2 103 ? 45.242 -27.992 -44.070 1.00 70.30 ? 103 GLU B OE2 1 ATOM 3370 N N . ASN B 2 104 ? 45.129 -21.664 -45.365 1.00 51.63 ? 104 ASN B N 1 ATOM 3371 C CA . ASN B 2 104 ? 44.993 -20.541 -46.290 1.00 52.23 ? 104 ASN B CA 1 ATOM 3372 C C . ASN B 2 104 ? 45.866 -20.743 -47.526 1.00 52.01 ? 104 ASN B C 1 ATOM 3373 O O . ASN B 2 104 ? 45.419 -20.533 -48.639 1.00 50.51 ? 104 ASN B O 1 ATOM 3374 C CB . ASN B 2 104 ? 45.367 -19.210 -45.624 1.00 53.26 ? 104 ASN B CB 1 ATOM 3375 C CG . ASN B 2 104 ? 44.303 -18.714 -44.665 1.00 54.29 ? 104 ASN B CG 1 ATOM 3376 O OD1 . ASN B 2 104 ? 43.179 -19.207 -44.658 1.00 52.01 ? 104 ASN B OD1 1 ATOM 3377 N ND2 . ASN B 2 104 ? 44.659 -17.728 -43.847 1.00 56.71 ? 104 ASN B ND2 1 ATOM 3378 N N . GLU B 2 105 ? 47.114 -21.148 -47.328 1.00 53.06 ? 105 GLU B N 1 ATOM 3379 C CA . GLU B 2 105 ? 47.973 -21.465 -48.455 1.00 54.24 ? 105 GLU B CA 1 ATOM 3380 C C . GLU B 2 105 ? 47.336 -22.569 -49.297 1.00 51.32 ? 105 GLU B C 1 ATOM 3381 O O . GLU B 2 105 ? 47.198 -22.444 -50.500 1.00 50.02 ? 105 GLU B O 1 ATOM 3382 C CB . GLU B 2 105 ? 49.342 -21.911 -47.967 1.00 59.65 ? 105 GLU B CB 1 ATOM 3383 C CG . GLU B 2 105 ? 50.445 -21.733 -48.984 1.00 67.65 ? 105 GLU B CG 1 ATOM 3384 C CD . GLU B 2 105 ? 51.782 -21.569 -48.306 1.00 78.90 ? 105 GLU B CD 1 ATOM 3385 O OE1 . GLU B 2 105 ? 52.181 -22.528 -47.603 1.00 88.53 ? 105 GLU B OE1 1 ATOM 3386 O OE2 . GLU B 2 105 ? 52.411 -20.484 -48.447 1.00 81.74 ? 105 GLU B OE2 1 ATOM 3387 N N . ARG B 2 106 ? 46.910 -23.647 -48.666 1.00 51.56 ? 106 ARG B N 1 ATOM 3388 C CA . ARG B 2 106 ? 46.294 -24.720 -49.440 1.00 53.67 ? 106 ARG B CA 1 ATOM 3389 C C . ARG B 2 106 ? 45.030 -24.263 -50.173 1.00 50.21 ? 106 ARG B C 1 ATOM 3390 O O . ARG B 2 106 ? 44.814 -24.654 -51.314 1.00 50.41 ? 106 ARG B O 1 ATOM 3391 C CB . ARG B 2 106 ? 46.053 -25.959 -48.576 1.00 57.16 ? 106 ARG B CB 1 ATOM 3392 C CG . ARG B 2 106 ? 47.353 -26.534 -48.016 1.00 61.19 ? 106 ARG B CG 1 ATOM 3393 C CD . ARG B 2 106 ? 47.244 -28.006 -47.645 1.00 67.77 ? 106 ARG B CD 1 ATOM 3394 N NE . ARG B 2 106 ? 47.749 -28.905 -48.699 1.00 73.79 ? 106 ARG B NE 1 ATOM 3395 C CZ . ARG B 2 106 ? 47.016 -29.734 -49.447 1.00 77.75 ? 106 ARG B CZ 1 ATOM 3396 N NH1 . ARG B 2 106 ? 45.697 -29.825 -49.302 1.00 81.24 ? 106 ARG B NH1 1 ATOM 3397 N NH2 . ARG B 2 106 ? 47.615 -30.503 -50.351 1.00 84.64 ? 106 ARG B NH2 1 ATOM 3398 N N . THR B 2 107 ? 44.225 -23.402 -49.555 1.00 50.32 ? 107 THR B N 1 ATOM 3399 C CA . THR B 2 107 ? 42.972 -22.937 -50.188 1.00 48.69 ? 107 THR B CA 1 ATOM 3400 C C . THR B 2 107 ? 43.259 -22.107 -51.452 1.00 48.57 ? 107 THR B C 1 ATOM 3401 O O . THR B 2 107 ? 42.650 -22.326 -52.499 1.00 45.73 ? 107 THR B O 1 ATOM 3402 C CB . THR B 2 107 ? 42.092 -22.156 -49.198 1.00 49.54 ? 107 THR B CB 1 ATOM 3403 O OG1 . THR B 2 107 ? 41.595 -23.050 -48.193 1.00 48.93 ? 107 THR B OG1 1 ATOM 3404 C CG2 . THR B 2 107 ? 40.900 -21.509 -49.906 1.00 52.17 ? 107 THR B CG2 1 ATOM 3405 N N . LEU B 2 108 ? 44.210 -21.184 -51.368 1.00 47.71 ? 108 LEU B N 1 ATOM 3406 C CA . LEU B 2 108 ? 44.572 -20.393 -52.531 1.00 48.99 ? 108 LEU B CA 1 ATOM 3407 C C . LEU B 2 108 ? 45.081 -21.288 -53.675 1.00 49.07 ? 108 LEU B C 1 ATOM 3408 O O . LEU B 2 108 ? 44.638 -21.147 -54.819 1.00 48.50 ? 108 LEU B O 1 ATOM 3409 C CB . LEU B 2 108 ? 45.599 -19.320 -52.161 1.00 50.29 ? 108 LEU B CB 1 ATOM 3410 C CG . LEU B 2 108 ? 45.146 -18.279 -51.129 1.00 53.00 ? 108 LEU B CG 1 ATOM 3411 C CD1 . LEU B 2 108 ? 46.202 -17.201 -50.969 1.00 56.45 ? 108 LEU B CD1 1 ATOM 3412 C CD2 . LEU B 2 108 ? 43.812 -17.637 -51.495 1.00 54.68 ? 108 LEU B CD2 1 ATOM 3413 N N . ASP B 2 109 ? 45.984 -22.217 -53.362 1.00 48.19 ? 109 ASP B N 1 ATOM 3414 C CA . ASP B 2 109 ? 46.464 -23.189 -54.349 1.00 48.50 ? 109 ASP B CA 1 ATOM 3415 C C . ASP B 2 109 ? 45.331 -24.075 -54.940 1.00 47.21 ? 109 ASP B C 1 ATOM 3416 O O . ASP B 2 109 ? 45.342 -24.409 -56.121 1.00 49.27 ? 109 ASP B O 1 ATOM 3417 C CB . ASP B 2 109 ? 47.527 -24.089 -53.719 1.00 52.29 ? 109 ASP B CB 1 ATOM 3418 C CG . ASP B 2 109 ? 48.846 -23.345 -53.372 1.00 57.94 ? 109 ASP B CG 1 ATOM 3419 O OD1 . ASP B 2 109 ? 49.226 -22.369 -54.080 1.00 57.81 ? 109 ASP B OD1 1 ATOM 3420 O OD2 . ASP B 2 109 ? 49.520 -23.793 -52.393 1.00 61.21 ? 109 ASP B OD2 1 ATOM 3421 N N . PHE B 2 110 ? 44.367 -24.459 -54.114 1.00 44.68 ? 110 PHE B N 1 ATOM 3422 C CA . PHE B 2 110 ? 43.211 -25.252 -54.550 1.00 44.35 ? 110 PHE B CA 1 ATOM 3423 C C . PHE B 2 110 ? 42.468 -24.558 -55.678 1.00 44.46 ? 110 PHE B C 1 ATOM 3424 O O . PHE B 2 110 ? 42.171 -25.169 -56.702 1.00 45.86 ? 110 PHE B O 1 ATOM 3425 C CB . PHE B 2 110 ? 42.300 -25.478 -53.340 1.00 45.38 ? 110 PHE B CB 1 ATOM 3426 C CG . PHE B 2 110 ? 41.029 -26.213 -53.632 1.00 48.00 ? 110 PHE B CG 1 ATOM 3427 C CD1 . PHE B 2 110 ? 41.044 -27.483 -54.191 1.00 49.89 ? 110 PHE B CD1 1 ATOM 3428 C CD2 . PHE B 2 110 ? 39.805 -25.658 -53.284 1.00 48.58 ? 110 PHE B CD2 1 ATOM 3429 C CE1 . PHE B 2 110 ? 39.860 -28.164 -54.438 1.00 51.66 ? 110 PHE B CE1 1 ATOM 3430 C CE2 . PHE B 2 110 ? 38.620 -26.342 -53.527 1.00 51.36 ? 110 PHE B CE2 1 ATOM 3431 C CZ . PHE B 2 110 ? 38.648 -27.596 -54.104 1.00 52.49 ? 110 PHE B CZ 1 ATOM 3432 N N . HIS B 2 111 ? 42.199 -23.264 -55.504 1.00 44.44 ? 111 HIS B N 1 ATOM 3433 C CA . HIS B 2 111 ? 41.520 -22.466 -56.526 1.00 44.13 ? 111 HIS B CA 1 ATOM 3434 C C . HIS B 2 111 ? 42.332 -22.392 -57.820 1.00 44.03 ? 111 HIS B C 1 ATOM 3435 O O . HIS B 2 111 ? 41.788 -22.541 -58.928 1.00 44.96 ? 111 HIS B O 1 ATOM 3436 C CB . HIS B 2 111 ? 41.250 -21.049 -56.009 1.00 44.61 ? 111 HIS B CB 1 ATOM 3437 C CG . HIS B 2 111 ? 40.163 -20.974 -54.988 1.00 44.69 ? 111 HIS B CG 1 ATOM 3438 N ND1 . HIS B 2 111 ? 38.864 -21.328 -55.267 1.00 46.74 ? 111 HIS B ND1 1 ATOM 3439 C CD2 . HIS B 2 111 ? 40.174 -20.564 -53.698 1.00 45.16 ? 111 HIS B CD2 1 ATOM 3440 C CE1 . HIS B 2 111 ? 38.120 -21.149 -54.190 1.00 49.04 ? 111 HIS B CE1 1 ATOM 3441 N NE2 . HIS B 2 111 ? 38.891 -20.684 -53.224 1.00 47.69 ? 111 HIS B NE2 1 ATOM 3442 N N . ASP B 2 112 ? 43.632 -22.168 -57.670 1.00 42.73 ? 112 ASP B N 1 ATOM 3443 C CA . ASP B 2 112 ? 44.550 -22.121 -58.791 1.00 43.65 ? 112 ASP B CA 1 ATOM 3444 C C . ASP B 2 112 ? 44.489 -23.454 -59.549 1.00 44.85 ? 112 ASP B C 1 ATOM 3445 O O . ASP B 2 112 ? 44.381 -23.498 -60.778 1.00 46.61 ? 112 ASP B O 1 ATOM 3446 C CB . ASP B 2 112 ? 45.963 -21.860 -58.254 1.00 46.01 ? 112 ASP B CB 1 ATOM 3447 C CG . ASP B 2 112 ? 46.944 -21.475 -59.335 1.00 49.47 ? 112 ASP B CG 1 ATOM 3448 O OD1 . ASP B 2 112 ? 46.499 -21.183 -60.468 1.00 51.34 ? 112 ASP B OD1 1 ATOM 3449 O OD2 . ASP B 2 112 ? 48.166 -21.450 -59.042 1.00 51.93 ? 112 ASP B OD2 1 ATOM 3450 N N . SER B 2 113 ? 44.538 -24.551 -58.807 1.00 44.78 ? 113 SER B N 1 ATOM 3451 C CA . SER B 2 113 ? 44.414 -25.874 -59.403 1.00 45.96 ? 113 SER B CA 1 ATOM 3452 C C . SER B 2 113 ? 43.086 -26.061 -60.158 1.00 45.50 ? 113 SER B C 1 ATOM 3453 O O . SER B 2 113 ? 43.059 -26.589 -61.271 1.00 45.69 ? 113 SER B O 1 ATOM 3454 C CB . SER B 2 113 ? 44.562 -26.938 -58.323 1.00 47.03 ? 113 SER B CB 1 ATOM 3455 O OG . SER B 2 113 ? 44.094 -28.174 -58.785 1.00 51.30 ? 113 SER B OG 1 ATOM 3456 N N . ASN B 2 114 ? 41.980 -25.639 -59.566 1.00 44.77 ? 114 ASN B N 1 ATOM 3457 C CA . ASN B 2 114 ? 40.697 -25.789 -60.257 1.00 46.03 ? 114 ASN B CA 1 ATOM 3458 C C . ASN B 2 114 ? 40.661 -25.004 -61.565 1.00 45.37 ? 114 ASN B C 1 ATOM 3459 O O . ASN B 2 114 ? 40.086 -25.475 -62.546 1.00 45.16 ? 114 ASN B O 1 ATOM 3460 C CB . ASN B 2 114 ? 39.528 -25.370 -59.381 1.00 47.25 ? 114 ASN B CB 1 ATOM 3461 C CG . ASN B 2 114 ? 39.386 -26.228 -58.154 1.00 49.29 ? 114 ASN B CG 1 ATOM 3462 O OD1 . ASN B 2 114 ? 39.667 -27.434 -58.173 1.00 51.03 ? 114 ASN B OD1 1 ATOM 3463 N ND2 . ASN B 2 114 ? 38.951 -25.611 -57.071 1.00 49.73 ? 114 ASN B ND2 1 ATOM 3464 N N . VAL B 2 115 ? 41.288 -23.825 -61.587 1.00 44.46 ? 115 VAL B N 1 ATOM 3465 C CA . VAL B 2 115 ? 41.327 -23.019 -62.810 1.00 44.62 ? 115 VAL B CA 1 ATOM 3466 C C . VAL B 2 115 ? 42.184 -23.709 -63.861 1.00 45.12 ? 115 VAL B C 1 ATOM 3467 O O . VAL B 2 115 ? 41.776 -23.859 -65.004 1.00 45.48 ? 115 VAL B O 1 ATOM 3468 C CB . VAL B 2 115 ? 41.882 -21.602 -62.552 1.00 45.14 ? 115 VAL B CB 1 ATOM 3469 C CG1 . VAL B 2 115 ? 42.143 -20.883 -63.866 1.00 46.63 ? 115 VAL B CG1 1 ATOM 3470 C CG2 . VAL B 2 115 ? 40.905 -20.789 -61.724 1.00 46.63 ? 115 VAL B CG2 1 ATOM 3471 N N . LYS B 2 116 ? 43.387 -24.109 -63.464 1.00 46.03 ? 116 LYS B N 1 ATOM 3472 C CA . LYS B 2 116 ? 44.287 -24.824 -64.345 1.00 48.60 ? 116 LYS B CA 1 ATOM 3473 C C . LYS B 2 116 ? 43.633 -26.058 -64.960 1.00 49.14 ? 116 LYS B C 1 ATOM 3474 O O . LYS B 2 116 ? 43.775 -26.314 -66.156 1.00 50.06 ? 116 LYS B O 1 ATOM 3475 C CB . LYS B 2 116 ? 45.536 -25.217 -63.557 1.00 52.28 ? 116 LYS B CB 1 ATOM 3476 C CG . LYS B 2 116 ? 46.512 -26.115 -64.281 1.00 56.75 ? 116 LYS B CG 1 ATOM 3477 C CD . LYS B 2 116 ? 47.153 -25.405 -65.459 1.00 61.26 ? 116 LYS B CD 1 ATOM 3478 C CE . LYS B 2 116 ? 48.485 -26.066 -65.814 1.00 67.56 ? 116 LYS B CE 1 ATOM 3479 N NZ . LYS B 2 116 ? 49.553 -25.037 -65.937 1.00 70.65 ? 116 LYS B NZ 1 ATOM 3480 N N . ASN B 2 117 ? 42.913 -26.826 -64.151 1.00 49.91 ? 117 ASN B N 1 ATOM 3481 C CA . ASN B 2 117 ? 42.244 -28.028 -64.660 1.00 52.61 ? 117 ASN B CA 1 ATOM 3482 C C . ASN B 2 117 ? 41.129 -27.691 -65.636 1.00 53.58 ? 117 ASN B C 1 ATOM 3483 O O . ASN B 2 117 ? 40.920 -28.405 -66.615 1.00 56.03 ? 117 ASN B O 1 ATOM 3484 C CB . ASN B 2 117 ? 41.724 -28.899 -63.512 1.00 52.96 ? 117 ASN B CB 1 ATOM 3485 C CG . ASN B 2 117 ? 42.850 -29.488 -62.683 1.00 54.21 ? 117 ASN B CG 1 ATOM 3486 O OD1 . ASN B 2 117 ? 43.970 -29.651 -63.161 1.00 54.56 ? 117 ASN B OD1 1 ATOM 3487 N ND2 . ASN B 2 117 ? 42.562 -29.798 -61.434 1.00 55.73 ? 117 ASN B ND2 1 ATOM 3488 N N . LEU B 2 118 ? 40.427 -26.592 -65.384 1.00 53.02 ? 118 LEU B N 1 ATOM 3489 C CA . LEU B 2 118 ? 39.352 -26.176 -66.278 1.00 55.18 ? 118 LEU B CA 1 ATOM 3490 C C . LEU B 2 118 ? 39.937 -25.755 -67.621 1.00 55.49 ? 118 LEU B C 1 ATOM 3491 O O . LEU B 2 118 ? 39.429 -26.125 -68.677 1.00 57.07 ? 118 LEU B O 1 ATOM 3492 C CB . LEU B 2 118 ? 38.559 -25.047 -65.639 1.00 56.04 ? 118 LEU B CB 1 ATOM 3493 C CG . LEU B 2 118 ? 37.352 -24.518 -66.383 1.00 58.64 ? 118 LEU B CG 1 ATOM 3494 C CD1 . LEU B 2 118 ? 36.382 -25.629 -66.760 1.00 62.06 ? 118 LEU B CD1 1 ATOM 3495 C CD2 . LEU B 2 118 ? 36.689 -23.481 -65.499 1.00 60.17 ? 118 LEU B CD2 1 ATOM 3496 N N . TYR B 2 119 ? 41.039 -25.015 -67.574 1.00 54.22 ? 119 TYR B N 1 ATOM 3497 C CA . TYR B 2 119 ? 41.757 -24.644 -68.779 1.00 53.23 ? 119 TYR B CA 1 ATOM 3498 C C . TYR B 2 119 ? 42.242 -25.876 -69.541 1.00 56.11 ? 119 TYR B C 1 ATOM 3499 O O . TYR B 2 119 ? 42.189 -25.914 -70.764 1.00 57.27 ? 119 TYR B O 1 ATOM 3500 C CB . TYR B 2 119 ? 42.929 -23.724 -68.430 1.00 51.80 ? 119 TYR B CB 1 ATOM 3501 C CG . TYR B 2 119 ? 43.772 -23.334 -69.619 1.00 52.98 ? 119 TYR B CG 1 ATOM 3502 C CD1 . TYR B 2 119 ? 43.387 -22.297 -70.461 1.00 52.99 ? 119 TYR B CD1 1 ATOM 3503 C CD2 . TYR B 2 119 ? 44.957 -24.003 -69.901 1.00 53.77 ? 119 TYR B CD2 1 ATOM 3504 C CE1 . TYR B 2 119 ? 44.157 -21.940 -71.553 1.00 54.73 ? 119 TYR B CE1 1 ATOM 3505 C CE2 . TYR B 2 119 ? 45.730 -23.653 -70.985 1.00 55.24 ? 119 TYR B CE2 1 ATOM 3506 C CZ . TYR B 2 119 ? 45.327 -22.627 -71.808 1.00 56.79 ? 119 TYR B CZ 1 ATOM 3507 O OH . TYR B 2 119 ? 46.103 -22.285 -72.881 1.00 59.37 ? 119 TYR B OH 1 ATOM 3508 N N . ASP B 2 120 ? 42.718 -26.890 -68.834 1.00 60.12 ? 120 ASP B N 1 ATOM 3509 C CA . ASP B 2 120 ? 43.191 -28.103 -69.521 1.00 64.02 ? 120 ASP B CA 1 ATOM 3510 C C . ASP B 2 120 ? 42.028 -28.906 -70.113 1.00 63.32 ? 120 ASP B C 1 ATOM 3511 O O . ASP B 2 120 ? 42.117 -29.394 -71.230 1.00 64.22 ? 120 ASP B O 1 ATOM 3512 C CB . ASP B 2 120 ? 44.071 -28.955 -68.593 1.00 66.98 ? 120 ASP B CB 1 ATOM 3513 C CG . ASP B 2 120 ? 45.444 -28.314 -68.339 1.00 69.69 ? 120 ASP B CG 1 ATOM 3514 O OD1 . ASP B 2 120 ? 45.979 -27.657 -69.264 1.00 71.00 ? 120 ASP B OD1 1 ATOM 3515 O OD2 . ASP B 2 120 ? 45.997 -28.466 -67.220 1.00 72.40 ? 120 ASP B OD2 1 ATOM 3516 N N . LYS B 2 121 ? 40.934 -29.018 -69.373 1.00 63.12 ? 121 LYS B N 1 ATOM 3517 C CA . LYS B 2 121 ? 39.731 -29.694 -69.867 1.00 67.36 ? 121 LYS B CA 1 ATOM 3518 C C . LYS B 2 121 ? 39.308 -29.142 -71.227 1.00 67.33 ? 121 LYS B C 1 ATOM 3519 O O . LYS B 2 121 ? 38.977 -29.900 -72.125 1.00 71.15 ? 121 LYS B O 1 ATOM 3520 C CB . LYS B 2 121 ? 38.604 -29.516 -68.853 1.00 69.47 ? 121 LYS B CB 1 ATOM 3521 C CG . LYS B 2 121 ? 37.280 -30.182 -69.172 1.00 73.67 ? 121 LYS B CG 1 ATOM 3522 C CD . LYS B 2 121 ? 36.260 -29.805 -68.099 1.00 75.68 ? 121 LYS B CD 1 ATOM 3523 C CE . LYS B 2 121 ? 34.973 -30.602 -68.222 1.00 82.92 ? 121 LYS B CE 1 ATOM 3524 N NZ . LYS B 2 121 ? 34.282 -30.367 -69.526 1.00 86.02 ? 121 LYS B NZ 1 ATOM 3525 N N . VAL B 2 122 ? 39.340 -27.818 -71.371 1.00 64.01 ? 122 VAL B N 1 ATOM 3526 C CA . VAL B 2 122 ? 39.021 -27.161 -72.632 1.00 62.26 ? 122 VAL B CA 1 ATOM 3527 C C . VAL B 2 122 ? 40.114 -27.358 -73.674 1.00 63.32 ? 122 VAL B C 1 ATOM 3528 O O . VAL B 2 122 ? 39.825 -27.639 -74.835 1.00 64.27 ? 122 VAL B O 1 ATOM 3529 C CB . VAL B 2 122 ? 38.772 -25.656 -72.421 1.00 59.82 ? 122 VAL B CB 1 ATOM 3530 C CG1 . VAL B 2 122 ? 38.713 -24.908 -73.750 1.00 58.68 ? 122 VAL B CG1 1 ATOM 3531 C CG2 . VAL B 2 122 ? 37.483 -25.466 -71.635 1.00 60.45 ? 122 VAL B CG2 1 ATOM 3532 N N . ARG B 2 123 ? 41.366 -27.196 -73.275 1.00 63.15 ? 123 ARG B N 1 ATOM 3533 C CA . ARG B 2 123 ? 42.479 -27.426 -74.193 1.00 66.43 ? 123 ARG B CA 1 ATOM 3534 C C . ARG B 2 123 ? 42.416 -28.837 -74.812 1.00 70.20 ? 123 ARG B C 1 ATOM 3535 O O . ARG B 2 123 ? 42.602 -28.997 -76.019 1.00 71.82 ? 123 ARG B O 1 ATOM 3536 C CB . ARG B 2 123 ? 43.812 -27.218 -73.474 1.00 67.42 ? 123 ARG B CB 1 ATOM 3537 C CG . ARG B 2 123 ? 45.005 -27.203 -74.409 1.00 71.95 ? 123 ARG B CG 1 ATOM 3538 C CD . ARG B 2 123 ? 46.323 -27.025 -73.671 1.00 74.23 ? 123 ARG B CD 1 ATOM 3539 N NE . ARG B 2 123 ? 46.452 -27.895 -72.501 1.00 75.37 ? 123 ARG B NE 1 ATOM 3540 C CZ . ARG B 2 123 ? 46.711 -29.201 -72.538 1.00 77.41 ? 123 ARG B CZ 1 ATOM 3541 N NH1 . ARG B 2 123 ? 46.861 -29.844 -73.691 1.00 80.09 ? 123 ARG B NH1 1 ATOM 3542 N NH2 . ARG B 2 123 ? 46.808 -29.875 -71.402 1.00 77.94 ? 123 ARG B NH2 1 ATOM 3543 N N . LEU B 2 124 ? 42.125 -29.844 -73.988 1.00 72.55 ? 124 LEU B N 1 ATOM 3544 C CA . LEU B 2 124 ? 42.054 -31.242 -74.443 1.00 78.72 ? 124 LEU B CA 1 ATOM 3545 C C . LEU B 2 124 ? 40.877 -31.524 -75.392 1.00 81.66 ? 124 LEU B C 1 ATOM 3546 O O . LEU B 2 124 ? 40.880 -32.527 -76.105 1.00 86.16 ? 124 LEU B O 1 ATOM 3547 C CB . LEU B 2 124 ? 41.989 -32.195 -73.241 1.00 80.40 ? 124 LEU B CB 1 ATOM 3548 C CG . LEU B 2 124 ? 43.231 -32.206 -72.335 1.00 81.03 ? 124 LEU B CG 1 ATOM 3549 C CD1 . LEU B 2 124 ? 42.920 -32.713 -70.924 1.00 81.31 ? 124 LEU B CD1 1 ATOM 3550 C CD2 . LEU B 2 124 ? 44.352 -33.015 -72.972 1.00 85.04 ? 124 LEU B CD2 1 ATOM 3551 N N . GLN B 2 125 ? 39.872 -30.654 -75.390 1.00 80.93 ? 125 GLN B N 1 ATOM 3552 C CA . GLN B 2 125 ? 38.750 -30.772 -76.317 1.00 82.69 ? 125 GLN B CA 1 ATOM 3553 C C . GLN B 2 125 ? 39.075 -30.168 -77.664 1.00 82.41 ? 125 GLN B C 1 ATOM 3554 O O . GLN B 2 125 ? 38.902 -30.811 -78.694 1.00 88.15 ? 125 GLN B O 1 ATOM 3555 C CB . GLN B 2 125 ? 37.522 -30.076 -75.760 1.00 81.89 ? 125 GLN B CB 1 ATOM 3556 C CG . GLN B 2 125 ? 36.885 -30.811 -74.604 1.00 85.54 ? 125 GLN B CG 1 ATOM 3557 C CD . GLN B 2 125 ? 35.517 -30.264 -74.290 1.00 86.79 ? 125 GLN B CD 1 ATOM 3558 O OE1 . GLN B 2 125 ? 34.515 -30.769 -74.793 1.00 92.50 ? 125 GLN B OE1 1 ATOM 3559 N NE2 . GLN B 2 125 ? 35.466 -29.205 -73.489 1.00 83.46 ? 125 GLN B NE2 1 ATOM 3560 N N . LEU B 2 126 ? 39.550 -28.930 -77.648 1.00 79.44 ? 126 LEU B N 1 ATOM 3561 C CA . LEU B 2 126 ? 39.809 -28.192 -78.877 1.00 81.14 ? 126 LEU B CA 1 ATOM 3562 C C . LEU B 2 126 ? 40.952 -28.799 -79.674 1.00 87.01 ? 126 LEU B C 1 ATOM 3563 O O . LEU B 2 126 ? 40.880 -28.871 -80.897 1.00 92.32 ? 126 LEU B O 1 ATOM 3564 C CB . LEU B 2 126 ? 40.090 -26.715 -78.579 1.00 76.13 ? 126 LEU B CB 1 ATOM 3565 C CG . LEU B 2 126 ? 38.995 -25.999 -77.784 1.00 72.19 ? 126 LEU B CG 1 ATOM 3566 C CD1 . LEU B 2 126 ? 39.292 -24.515 -77.673 1.00 69.75 ? 126 LEU B CD1 1 ATOM 3567 C CD2 . LEU B 2 126 ? 37.628 -26.230 -78.405 1.00 74.66 ? 126 LEU B CD2 1 ATOM 3568 N N . ARG B 2 127 ? 41.992 -29.249 -78.981 1.00 94.13 ? 127 ARG B N 1 ATOM 3569 C CA . ARG B 2 127 ? 43.145 -29.890 -79.627 1.00 100.53 ? 127 ARG B CA 1 ATOM 3570 C C . ARG B 2 127 ? 43.759 -28.966 -80.696 1.00 100.60 ? 127 ARG B C 1 ATOM 3571 O O . ARG B 2 127 ? 44.358 -27.949 -80.350 1.00 99.85 ? 127 ARG B O 1 ATOM 3572 C CB . ARG B 2 127 ? 42.765 -31.284 -80.175 1.00 106.05 ? 127 ARG B CB 1 ATOM 3573 C CG . ARG B 2 127 ? 42.605 -32.349 -79.091 1.00 108.46 ? 127 ARG B CG 1 ATOM 3574 C CD . ARG B 2 127 ? 41.541 -33.388 -79.420 1.00 111.58 ? 127 ARG B CD 1 ATOM 3575 N NE . ARG B 2 127 ? 41.894 -34.219 -80.569 1.00 119.04 ? 127 ARG B NE 1 ATOM 3576 C CZ . ARG B 2 127 ? 41.194 -35.276 -80.988 1.00 126.93 ? 127 ARG B CZ 1 ATOM 3577 N NH1 . ARG B 2 127 ? 40.085 -35.651 -80.355 1.00 129.32 ? 127 ARG B NH1 1 ATOM 3578 N NH2 . ARG B 2 127 ? 41.607 -35.971 -82.048 1.00 130.55 ? 127 ARG B NH2 1 ATOM 3579 N N . ASP B 2 128 ? 43.586 -29.287 -81.977 1.00 103.15 ? 128 ASP B N 1 ATOM 3580 C CA . ASP B 2 128 ? 44.210 -28.512 -83.054 1.00 102.51 ? 128 ASP B CA 1 ATOM 3581 C C . ASP B 2 128 ? 43.209 -27.642 -83.829 1.00 98.36 ? 128 ASP B C 1 ATOM 3582 O O . ASP B 2 128 ? 43.564 -27.045 -84.842 1.00 99.40 ? 128 ASP B O 1 ATOM 3583 C CB . ASP B 2 128 ? 44.972 -29.442 -84.004 1.00 109.58 ? 128 ASP B CB 1 ATOM 3584 C CG . ASP B 2 128 ? 44.121 -30.596 -84.506 1.00 114.86 ? 128 ASP B CG 1 ATOM 3585 O OD1 . ASP B 2 128 ? 43.075 -30.346 -85.140 1.00 115.50 ? 128 ASP B OD1 1 ATOM 3586 O OD2 . ASP B 2 128 ? 44.494 -31.758 -84.253 1.00 123.60 ? 128 ASP B OD2 1 ATOM 3587 N N . ASN B 2 129 ? 41.970 -27.559 -83.349 1.00 94.36 ? 129 ASN B N 1 ATOM 3588 C CA . ASN B 2 129 ? 40.956 -26.706 -83.973 1.00 91.78 ? 129 ASN B CA 1 ATOM 3589 C C . ASN B 2 129 ? 40.965 -25.254 -83.465 1.00 88.07 ? 129 ASN B C 1 ATOM 3590 O O . ASN B 2 129 ? 40.058 -24.482 -83.800 1.00 85.52 ? 129 ASN B O 1 ATOM 3591 C CB . ASN B 2 129 ? 39.559 -27.307 -83.770 1.00 94.51 ? 129 ASN B CB 1 ATOM 3592 C CG . ASN B 2 129 ? 39.394 -28.655 -84.451 1.00 101.77 ? 129 ASN B CG 1 ATOM 3593 O OD1 . ASN B 2 129 ? 40.360 -29.243 -84.939 1.00 109.35 ? 129 ASN B OD1 1 ATOM 3594 N ND2 . ASN B 2 129 ? 38.162 -29.157 -84.479 1.00 102.53 ? 129 ASN B ND2 1 ATOM 3595 N N . ALA B 2 130 ? 41.983 -24.877 -82.683 1.00 84.59 ? 130 ALA B N 1 ATOM 3596 C CA . ALA B 2 130 ? 42.051 -23.535 -82.094 1.00 81.04 ? 130 ALA B CA 1 ATOM 3597 C C . ALA B 2 130 ? 43.476 -23.160 -81.727 1.00 81.38 ? 130 ALA B C 1 ATOM 3598 O O . ALA B 2 130 ? 44.231 -24.013 -81.289 1.00 84.87 ? 130 ALA B O 1 ATOM 3599 C CB . ALA B 2 130 ? 41.174 -23.474 -80.854 1.00 78.66 ? 130 ALA B CB 1 ATOM 3600 N N . LYS B 2 131 ? 43.839 -21.889 -81.890 1.00 81.88 ? 131 LYS B N 1 ATOM 3601 C CA . LYS B 2 131 ? 45.161 -21.413 -81.473 1.00 84.46 ? 131 LYS B CA 1 ATOM 3602 C C . LYS B 2 131 ? 45.170 -21.141 -79.978 1.00 80.88 ? 131 LYS B C 1 ATOM 3603 O O . LYS B 2 131 ? 44.344 -20.390 -79.474 1.00 80.26 ? 131 LYS B O 1 ATOM 3604 C CB . LYS B 2 131 ? 45.561 -20.136 -82.212 1.00 90.78 ? 131 LYS B CB 1 ATOM 3605 C CG . LYS B 2 131 ? 45.721 -20.325 -83.710 1.00 100.33 ? 131 LYS B CG 1 ATOM 3606 C CD . LYS B 2 131 ? 46.542 -19.219 -84.371 1.00 110.29 ? 131 LYS B CD 1 ATOM 3607 C CE . LYS B 2 131 ? 47.538 -19.798 -85.377 1.00 116.70 ? 131 LYS B CE 1 ATOM 3608 N NZ . LYS B 2 131 ? 48.422 -18.776 -86.006 1.00 120.80 ? 131 LYS B NZ 1 ATOM 3609 N N . GLU B 2 132 ? 46.109 -21.753 -79.271 1.00 78.85 ? 132 GLU B N 1 ATOM 3610 C CA . GLU B 2 132 ? 46.301 -21.471 -77.865 1.00 74.42 ? 132 GLU B CA 1 ATOM 3611 C C . GLU B 2 132 ? 47.093 -20.165 -77.756 1.00 75.09 ? 132 GLU B C 1 ATOM 3612 O O . GLU B 2 132 ? 48.274 -20.131 -78.082 1.00 79.39 ? 132 GLU B O 1 ATOM 3613 C CB . GLU B 2 132 ? 47.045 -22.624 -77.212 1.00 74.25 ? 132 GLU B CB 1 ATOM 3614 C CG . GLU B 2 132 ? 46.982 -22.624 -75.701 1.00 72.44 ? 132 GLU B CG 1 ATOM 3615 C CD . GLU B 2 132 ? 47.770 -23.758 -75.074 1.00 74.45 ? 132 GLU B CD 1 ATOM 3616 O OE1 . GLU B 2 132 ? 48.389 -24.561 -75.815 1.00 78.39 ? 132 GLU B OE1 1 ATOM 3617 O OE2 . GLU B 2 132 ? 47.771 -23.842 -73.827 1.00 73.98 ? 132 GLU B OE2 1 ATOM 3618 N N . LEU B 2 133 ? 46.440 -19.096 -77.302 1.00 71.84 ? 133 LEU B N 1 ATOM 3619 C CA . LEU B 2 133 ? 47.030 -17.755 -77.350 1.00 73.03 ? 133 LEU B CA 1 ATOM 3620 C C . LEU B 2 133 ? 48.064 -17.481 -76.274 1.00 75.12 ? 133 LEU B C 1 ATOM 3621 O O . LEU B 2 133 ? 48.926 -16.627 -76.465 1.00 80.09 ? 133 LEU B O 1 ATOM 3622 C CB . LEU B 2 133 ? 45.940 -16.684 -77.275 1.00 72.73 ? 133 LEU B CB 1 ATOM 3623 C CG . LEU B 2 133 ? 45.016 -16.601 -78.490 1.00 72.19 ? 133 LEU B CG 1 ATOM 3624 C CD1 . LEU B 2 133 ? 43.965 -15.535 -78.248 1.00 73.92 ? 133 LEU B CD1 1 ATOM 3625 C CD2 . LEU B 2 133 ? 45.794 -16.299 -79.761 1.00 73.98 ? 133 LEU B CD2 1 ATOM 3626 N N . GLY B 2 134 ? 47.965 -18.183 -75.146 1.00 73.17 ? 134 GLY B N 1 ATOM 3627 C CA . GLY B 2 134 ? 48.943 -18.067 -74.061 1.00 73.65 ? 134 GLY B CA 1 ATOM 3628 C C . GLY B 2 134 ? 48.460 -17.309 -72.836 1.00 72.17 ? 134 GLY B C 1 ATOM 3629 O O . GLY B 2 134 ? 49.204 -17.171 -71.874 1.00 73.48 ? 134 GLY B O 1 ATOM 3630 N N . ASN B 2 135 ? 47.213 -16.840 -72.858 1.00 70.25 ? 135 ASN B N 1 ATOM 3631 C CA . ASN B 2 135 ? 46.690 -15.941 -71.819 1.00 69.12 ? 135 ASN B CA 1 ATOM 3632 C C . ASN B 2 135 ? 45.363 -16.423 -71.209 1.00 65.34 ? 135 ASN B C 1 ATOM 3633 O O . ASN B 2 135 ? 44.651 -15.656 -70.556 1.00 63.53 ? 135 ASN B O 1 ATOM 3634 C CB . ASN B 2 135 ? 46.499 -14.550 -72.420 1.00 72.56 ? 135 ASN B CB 1 ATOM 3635 C CG . ASN B 2 135 ? 45.499 -14.545 -73.564 1.00 73.00 ? 135 ASN B CG 1 ATOM 3636 O OD1 . ASN B 2 135 ? 45.066 -15.598 -74.033 1.00 71.81 ? 135 ASN B OD1 1 ATOM 3637 N ND2 . ASN B 2 135 ? 45.131 -13.360 -74.018 1.00 76.72 ? 135 ASN B ND2 1 ATOM 3638 N N . GLY B 2 136 ? 45.037 -17.692 -71.430 1.00 62.69 ? 136 GLY B N 1 ATOM 3639 C CA . GLY B 2 136 ? 43.768 -18.251 -71.002 1.00 60.01 ? 136 GLY B CA 1 ATOM 3640 C C . GLY B 2 136 ? 42.786 -18.448 -72.141 1.00 58.75 ? 136 GLY B C 1 ATOM 3641 O O . GLY B 2 136 ? 41.766 -19.095 -71.960 1.00 57.12 ? 136 GLY B O 1 ATOM 3642 N N . CYS B 2 137 ? 43.103 -17.918 -73.318 1.00 61.79 ? 137 CYS B N 1 ATOM 3643 C CA . CYS B 2 137 ? 42.158 -17.905 -74.432 1.00 64.10 ? 137 CYS B CA 1 ATOM 3644 C C . CYS B 2 137 ? 42.564 -18.820 -75.573 1.00 63.08 ? 137 CYS B C 1 ATOM 3645 O O . CYS B 2 137 ? 43.740 -19.100 -75.784 1.00 63.82 ? 137 CYS B O 1 ATOM 3646 C CB . CYS B 2 137 ? 41.979 -16.485 -74.975 1.00 67.14 ? 137 CYS B CB 1 ATOM 3647 S SG . CYS B 2 137 ? 41.445 -15.288 -73.737 1.00 73.44 ? 137 CYS B SG 1 ATOM 3648 N N . PHE B 2 138 ? 41.549 -19.257 -76.308 1.00 62.47 ? 138 PHE B N 1 ATOM 3649 C CA . PHE B 2 138 ? 41.702 -20.063 -77.491 1.00 63.14 ? 138 PHE B CA 1 ATOM 3650 C C . PHE B 2 138 ? 40.996 -19.354 -78.632 1.00 65.29 ? 138 PHE B C 1 ATOM 3651 O O . PHE B 2 138 ? 39.832 -19.039 -78.523 1.00 64.85 ? 138 PHE B O 1 ATOM 3652 C CB . PHE B 2 138 ? 41.059 -21.429 -77.280 1.00 62.19 ? 138 PHE B CB 1 ATOM 3653 C CG . PHE B 2 138 ? 41.676 -22.220 -76.170 1.00 61.84 ? 138 PHE B CG 1 ATOM 3654 C CD1 . PHE B 2 138 ? 42.800 -23.010 -76.401 1.00 61.97 ? 138 PHE B CD1 1 ATOM 3655 C CD2 . PHE B 2 138 ? 41.138 -22.177 -74.888 1.00 60.41 ? 138 PHE B CD2 1 ATOM 3656 C CE1 . PHE B 2 138 ? 43.366 -23.744 -75.376 1.00 61.54 ? 138 PHE B CE1 1 ATOM 3657 C CE2 . PHE B 2 138 ? 41.705 -22.909 -73.861 1.00 60.48 ? 138 PHE B CE2 1 ATOM 3658 C CZ . PHE B 2 138 ? 42.824 -23.688 -74.104 1.00 60.61 ? 138 PHE B CZ 1 ATOM 3659 N N . GLU B 2 139 ? 41.705 -19.131 -79.728 1.00 70.12 ? 139 GLU B N 1 ATOM 3660 C CA . GLU B 2 139 ? 41.156 -18.476 -80.895 1.00 72.77 ? 139 GLU B CA 1 ATOM 3661 C C . GLU B 2 139 ? 40.841 -19.548 -81.928 1.00 73.04 ? 139 GLU B C 1 ATOM 3662 O O . GLU B 2 139 ? 41.724 -20.295 -82.339 1.00 76.06 ? 139 GLU B O 1 ATOM 3663 C CB . GLU B 2 139 ? 42.186 -17.492 -81.427 1.00 78.70 ? 139 GLU B CB 1 ATOM 3664 C CG . GLU B 2 139 ? 41.722 -16.611 -82.565 1.00 84.80 ? 139 GLU B CG 1 ATOM 3665 C CD . GLU B 2 139 ? 42.853 -15.740 -83.073 1.00 93.57 ? 139 GLU B CD 1 ATOM 3666 O OE1 . GLU B 2 139 ? 43.338 -14.875 -82.307 1.00 97.79 ? 139 GLU B OE1 1 ATOM 3667 O OE2 . GLU B 2 139 ? 43.270 -15.932 -84.235 1.00 102.65 ? 139 GLU B OE2 1 ATOM 3668 N N . PHE B 2 140 ? 39.579 -19.626 -82.340 1.00 73.77 ? 140 PHE B N 1 ATOM 3669 C CA . PHE B 2 140 ? 39.113 -20.686 -83.237 1.00 74.86 ? 140 PHE B CA 1 ATOM 3670 C C . PHE B 2 140 ? 39.533 -20.488 -84.697 1.00 77.47 ? 140 PHE B C 1 ATOM 3671 O O . PHE B 2 140 ? 39.673 -19.357 -85.162 1.00 77.13 ? 140 PHE B O 1 ATOM 3672 C CB . PHE B 2 140 ? 37.593 -20.794 -83.156 1.00 72.56 ? 140 PHE B CB 1 ATOM 3673 C CG . PHE B 2 140 ? 37.100 -21.322 -81.849 1.00 71.78 ? 140 PHE B CG 1 ATOM 3674 C CD1 . PHE B 2 140 ? 36.843 -20.464 -80.790 1.00 72.34 ? 140 PHE B CD1 1 ATOM 3675 C CD2 . PHE B 2 140 ? 36.888 -22.681 -81.673 1.00 73.16 ? 140 PHE B CD2 1 ATOM 3676 C CE1 . PHE B 2 140 ? 36.377 -20.952 -79.579 1.00 71.73 ? 140 PHE B CE1 1 ATOM 3677 C CE2 . PHE B 2 140 ? 36.427 -23.179 -80.465 1.00 73.35 ? 140 PHE B CE2 1 ATOM 3678 C CZ . PHE B 2 140 ? 36.173 -22.314 -79.415 1.00 72.40 ? 140 PHE B CZ 1 ATOM 3679 N N . TYR B 2 141 ? 39.731 -21.593 -85.415 1.00 81.60 ? 141 TYR B N 1 ATOM 3680 C CA . TYR B 2 141 ? 40.026 -21.528 -86.859 1.00 86.80 ? 141 TYR B CA 1 ATOM 3681 C C . TYR B 2 141 ? 38.756 -21.412 -87.688 1.00 87.51 ? 141 TYR B C 1 ATOM 3682 O O . TYR B 2 141 ? 38.788 -20.917 -88.810 1.00 94.91 ? 141 TYR B O 1 ATOM 3683 C CB . TYR B 2 141 ? 40.809 -22.751 -87.327 1.00 87.08 ? 141 TYR B CB 1 ATOM 3684 C CG . TYR B 2 141 ? 42.193 -22.830 -86.749 1.00 89.37 ? 141 TYR B CG 1 ATOM 3685 C CD1 . TYR B 2 141 ? 43.113 -21.806 -86.955 1.00 90.23 ? 141 TYR B CD1 1 ATOM 3686 C CD2 . TYR B 2 141 ? 42.587 -23.928 -85.988 1.00 90.70 ? 141 TYR B CD2 1 ATOM 3687 C CE1 . TYR B 2 141 ? 44.384 -21.875 -86.420 1.00 93.99 ? 141 TYR B CE1 1 ATOM 3688 C CE2 . TYR B 2 141 ? 43.856 -24.006 -85.451 1.00 92.24 ? 141 TYR B CE2 1 ATOM 3689 C CZ . TYR B 2 141 ? 44.750 -22.981 -85.669 1.00 94.92 ? 141 TYR B CZ 1 ATOM 3690 O OH . TYR B 2 141 ? 46.013 -23.077 -85.132 1.00 97.66 ? 141 TYR B OH 1 ATOM 3691 N N . HIS B 2 142 ? 37.649 -21.880 -87.128 1.00 99.35 ? 142 HIS B N 1 ATOM 3692 C CA . HIS B 2 142 ? 36.348 -21.789 -87.768 1.00 101.15 ? 142 HIS B CA 1 ATOM 3693 C C . HIS B 2 142 ? 35.508 -20.761 -87.033 1.00 98.76 ? 142 HIS B C 1 ATOM 3694 O O . HIS B 2 142 ? 35.843 -20.354 -85.921 1.00 95.48 ? 142 HIS B O 1 ATOM 3695 C CB . HIS B 2 142 ? 35.646 -23.151 -87.741 1.00 103.62 ? 142 HIS B CB 1 ATOM 3696 C CG . HIS B 2 142 ? 35.581 -23.776 -86.380 1.00 100.75 ? 142 HIS B CG 1 ATOM 3697 N ND1 . HIS B 2 142 ? 34.460 -23.706 -85.580 1.00 99.99 ? 142 HIS B ND1 1 ATOM 3698 C CD2 . HIS B 2 142 ? 36.502 -24.477 -85.676 1.00 98.95 ? 142 HIS B CD2 1 ATOM 3699 C CE1 . HIS B 2 142 ? 34.693 -24.341 -84.445 1.00 98.25 ? 142 HIS B CE1 1 ATOM 3700 N NE2 . HIS B 2 142 ? 35.925 -24.815 -84.477 1.00 97.39 ? 142 HIS B NE2 1 ATOM 3701 N N . LYS B 2 143 ? 34.421 -20.331 -87.660 1.00 102.53 ? 143 LYS B N 1 ATOM 3702 C CA . LYS B 2 143 ? 33.421 -19.539 -86.961 1.00 101.43 ? 143 LYS B CA 1 ATOM 3703 C C . LYS B 2 143 ? 32.807 -20.418 -85.880 1.00 98.71 ? 143 LYS B C 1 ATOM 3704 O O . LYS B 2 143 ? 32.406 -21.553 -86.149 1.00 100.71 ? 143 LYS B O 1 ATOM 3705 C CB . LYS B 2 143 ? 32.333 -19.042 -87.911 1.00 106.62 ? 143 LYS B CB 1 ATOM 3706 C CG . LYS B 2 143 ? 32.624 -17.687 -88.538 1.00 109.81 ? 143 LYS B CG 1 ATOM 3707 C CD . LYS B 2 143 ? 31.793 -17.442 -89.796 1.00 116.75 ? 143 LYS B CD 1 ATOM 3708 C CE . LYS B 2 143 ? 30.306 -17.726 -89.597 1.00 119.80 ? 143 LYS B CE 1 ATOM 3709 N NZ . LYS B 2 143 ? 29.721 -17.040 -88.407 1.00 118.07 ? 143 LYS B NZ 1 ATOM 3710 N N . CYS B 2 144 ? 32.763 -19.898 -84.657 1.00 92.91 ? 144 CYS B N 1 ATOM 3711 C CA . CYS B 2 144 ? 32.158 -20.603 -83.537 1.00 89.17 ? 144 CYS B CA 1 ATOM 3712 C C . CYS B 2 144 ? 31.010 -19.746 -83.007 1.00 88.06 ? 144 CYS B C 1 ATOM 3713 O O . CYS B 2 144 ? 31.229 -18.796 -82.258 1.00 86.40 ? 144 CYS B O 1 ATOM 3714 C CB . CYS B 2 144 ? 33.216 -20.878 -82.461 1.00 84.89 ? 144 CYS B CB 1 ATOM 3715 S SG . CYS B 2 144 ? 32.748 -22.047 -81.157 1.00 85.80 ? 144 CYS B SG 1 ATOM 3716 N N . ASP B 2 145 ? 29.789 -20.069 -83.429 1.00 90.33 ? 145 ASP B N 1 ATOM 3717 C CA . ASP B 2 145 ? 28.593 -19.349 -82.973 1.00 91.40 ? 145 ASP B CA 1 ATOM 3718 C C . ASP B 2 145 ? 28.237 -19.755 -81.535 1.00 88.07 ? 145 ASP B C 1 ATOM 3719 O O . ASP B 2 145 ? 28.942 -20.556 -80.928 1.00 87.52 ? 145 ASP B O 1 ATOM 3720 C CB . ASP B 2 145 ? 27.412 -19.567 -83.940 1.00 96.72 ? 145 ASP B CB 1 ATOM 3721 C CG . ASP B 2 145 ? 26.986 -21.030 -84.054 1.00 100.48 ? 145 ASP B CG 1 ATOM 3722 O OD1 . ASP B 2 145 ? 27.462 -21.878 -83.270 1.00 99.71 ? 145 ASP B OD1 1 ATOM 3723 O OD2 . ASP B 2 145 ? 26.166 -21.334 -84.944 1.00 106.40 ? 145 ASP B OD2 1 ATOM 3724 N N . ASN B 2 146 ? 27.156 -19.202 -80.994 1.00 87.24 ? 146 ASN B N 1 ATOM 3725 C CA . ASN B 2 146 ? 26.801 -19.427 -79.592 1.00 85.49 ? 146 ASN B CA 1 ATOM 3726 C C . ASN B 2 146 ? 26.574 -20.886 -79.220 1.00 88.38 ? 146 ASN B C 1 ATOM 3727 O O . ASN B 2 146 ? 26.964 -21.312 -78.136 1.00 86.51 ? 146 ASN B O 1 ATOM 3728 C CB . ASN B 2 146 ? 25.565 -18.607 -79.210 1.00 85.52 ? 146 ASN B CB 1 ATOM 3729 C CG . ASN B 2 146 ? 25.838 -17.114 -79.179 1.00 82.79 ? 146 ASN B CG 1 ATOM 3730 O OD1 . ASN B 2 146 ? 26.994 -16.657 -79.203 1.00 77.92 ? 146 ASN B OD1 1 ATOM 3731 N ND2 . ASN B 2 146 ? 24.770 -16.340 -79.121 1.00 84.20 ? 146 ASN B ND2 1 ATOM 3732 N N . GLU B 2 147 ? 25.947 -21.651 -80.106 1.00 95.91 ? 147 GLU B N 1 ATOM 3733 C CA . GLU B 2 147 ? 25.745 -23.088 -79.850 1.00 101.71 ? 147 GLU B CA 1 ATOM 3734 C C . GLU B 2 147 ? 27.065 -23.876 -79.980 1.00 97.97 ? 147 GLU B C 1 ATOM 3735 O O . GLU B 2 147 ? 27.274 -24.872 -79.283 1.00 98.01 ? 147 GLU B O 1 ATOM 3736 C CB . GLU B 2 147 ? 24.626 -23.700 -80.716 1.00 110.70 ? 147 GLU B CB 1 ATOM 3737 C CG . GLU B 2 147 ? 24.445 -23.118 -82.117 1.00 116.97 ? 147 GLU B CG 1 ATOM 3738 C CD . GLU B 2 147 ? 23.578 -21.861 -82.163 1.00 120.02 ? 147 GLU B CD 1 ATOM 3739 O OE1 . GLU B 2 147 ? 22.945 -21.512 -81.140 1.00 121.60 ? 147 GLU B OE1 1 ATOM 3740 O OE2 . GLU B 2 147 ? 23.529 -21.218 -83.237 1.00 123.05 ? 147 GLU B OE2 1 ATOM 3741 N N . CYS B 2 148 ? 27.951 -23.421 -80.862 1.00 94.46 ? 148 CYS B N 1 ATOM 3742 C CA . CYS B 2 148 ? 29.321 -23.930 -80.907 1.00 91.49 ? 148 CYS B CA 1 ATOM 3743 C C . CYS B 2 148 ? 30.029 -23.643 -79.575 1.00 85.77 ? 148 CYS B C 1 ATOM 3744 O O . CYS B 2 148 ? 30.688 -24.521 -79.007 1.00 86.55 ? 148 CYS B O 1 ATOM 3745 C CB . CYS B 2 148 ? 30.081 -23.293 -82.074 1.00 92.17 ? 148 CYS B CB 1 ATOM 3746 S SG . CYS B 2 148 ? 31.854 -23.633 -82.126 1.00 94.75 ? 148 CYS B SG 1 ATOM 3747 N N . MET B 2 149 ? 29.878 -22.420 -79.069 1.00 79.32 ? 149 MET B N 1 ATOM 3748 C CA . MET B 2 149 ? 30.462 -22.053 -77.783 1.00 74.45 ? 149 MET B CA 1 ATOM 3749 C C . MET B 2 149 ? 29.882 -22.893 -76.653 1.00 75.50 ? 149 MET B C 1 ATOM 3750 O O . MET B 2 149 ? 30.621 -23.400 -75.812 1.00 73.26 ? 149 MET B O 1 ATOM 3751 C CB . MET B 2 149 ? 30.250 -20.570 -77.487 1.00 72.11 ? 149 MET B CB 1 ATOM 3752 C CG . MET B 2 149 ? 30.974 -19.632 -78.435 1.00 71.35 ? 149 MET B CG 1 ATOM 3753 S SD . MET B 2 149 ? 32.757 -19.798 -78.307 1.00 72.22 ? 149 MET B SD 1 ATOM 3754 C CE . MET B 2 149 ? 33.300 -18.486 -79.400 1.00 71.57 ? 149 MET B CE 1 ATOM 3755 N N . GLU B 2 150 ? 28.562 -23.051 -76.642 1.00 80.52 ? 150 GLU B N 1 ATOM 3756 C CA . GLU B 2 150 ? 27.899 -23.848 -75.614 1.00 84.10 ? 150 GLU B CA 1 ATOM 3757 C C . GLU B 2 150 ? 28.466 -25.264 -75.557 1.00 84.80 ? 150 GLU B C 1 ATOM 3758 O O . GLU B 2 150 ? 28.655 -25.810 -74.472 1.00 82.34 ? 150 GLU B O 1 ATOM 3759 C CB . GLU B 2 150 ? 26.381 -23.868 -75.850 1.00 91.67 ? 150 GLU B CB 1 ATOM 3760 C CG . GLU B 2 150 ? 25.569 -24.767 -74.916 1.00 98.16 ? 150 GLU B CG 1 ATOM 3761 C CD . GLU B 2 150 ? 25.717 -24.431 -73.436 1.00 98.74 ? 150 GLU B CD 1 ATOM 3762 O OE1 . GLU B 2 150 ? 26.204 -23.331 -73.090 1.00 96.98 ? 150 GLU B OE1 1 ATOM 3763 O OE2 . GLU B 2 150 ? 25.330 -25.281 -72.604 1.00 103.72 ? 150 GLU B OE2 1 ATOM 3764 N N . SER B 2 151 ? 28.758 -25.836 -76.724 1.00 87.36 ? 151 SER B N 1 ATOM 3765 C CA . SER B 2 151 ? 29.292 -27.198 -76.814 1.00 91.72 ? 151 SER B CA 1 ATOM 3766 C C . SER B 2 151 ? 30.678 -27.330 -76.186 1.00 88.65 ? 151 SER B C 1 ATOM 3767 O O . SER B 2 151 ? 31.030 -28.397 -75.682 1.00 91.22 ? 151 SER B O 1 ATOM 3768 C CB . SER B 2 151 ? 29.354 -27.660 -78.272 1.00 95.73 ? 151 SER B CB 1 ATOM 3769 O OG . SER B 2 151 ? 30.453 -27.074 -78.945 1.00 92.90 ? 151 SER B OG 1 ATOM 3770 N N . VAL B 2 152 ? 31.466 -26.256 -76.230 1.00 85.02 ? 152 VAL B N 1 ATOM 3771 C CA . VAL B 2 152 ? 32.782 -26.240 -75.581 1.00 81.32 ? 152 VAL B CA 1 ATOM 3772 C C . VAL B 2 152 ? 32.622 -26.256 -74.063 1.00 81.79 ? 152 VAL B C 1 ATOM 3773 O O . VAL B 2 152 ? 33.343 -26.969 -73.366 1.00 80.84 ? 152 VAL B O 1 ATOM 3774 C CB . VAL B 2 152 ? 33.620 -25.019 -75.999 1.00 76.82 ? 152 VAL B CB 1 ATOM 3775 C CG1 . VAL B 2 152 ? 34.951 -25.002 -75.259 1.00 75.60 ? 152 VAL B CG1 1 ATOM 3776 C CG2 . VAL B 2 152 ? 33.851 -25.029 -77.501 1.00 78.31 ? 152 VAL B CG2 1 ATOM 3777 N N . ARG B 2 153 ? 31.666 -25.483 -73.560 1.00 82.88 ? 153 ARG B N 1 ATOM 3778 C CA . ARG B 2 153 ? 31.355 -25.496 -72.134 1.00 85.45 ? 153 ARG B CA 1 ATOM 3779 C C . ARG B 2 153 ? 30.703 -26.814 -71.721 1.00 92.98 ? 153 ARG B C 1 ATOM 3780 O O . ARG B 2 153 ? 30.913 -27.272 -70.603 1.00 95.45 ? 153 ARG B O 1 ATOM 3781 C CB . ARG B 2 153 ? 30.433 -24.339 -71.761 1.00 84.81 ? 153 ARG B CB 1 ATOM 3782 C CG . ARG B 2 153 ? 30.933 -22.969 -72.180 1.00 81.02 ? 153 ARG B CG 1 ATOM 3783 C CD . ARG B 2 153 ? 30.010 -21.880 -71.664 1.00 81.91 ? 153 ARG B CD 1 ATOM 3784 N NE . ARG B 2 153 ? 29.954 -20.763 -72.601 1.00 81.73 ? 153 ARG B NE 1 ATOM 3785 C CZ . ARG B 2 153 ? 28.945 -20.498 -73.428 1.00 83.22 ? 153 ARG B CZ 1 ATOM 3786 N NH1 . ARG B 2 153 ? 27.845 -21.251 -73.452 1.00 84.97 ? 153 ARG B NH1 1 ATOM 3787 N NH2 . ARG B 2 153 ? 29.038 -19.451 -74.238 1.00 84.24 ? 153 ARG B NH2 1 ATOM 3788 N N . ASN B 2 154 ? 29.902 -27.399 -72.617 1.00 100.98 ? 154 ASN B N 1 ATOM 3789 C CA . ASN B 2 154 ? 29.264 -28.714 -72.404 1.00 109.32 ? 154 ASN B CA 1 ATOM 3790 C C . ASN B 2 154 ? 30.225 -29.828 -72.025 1.00 108.36 ? 154 ASN B C 1 ATOM 3791 O O . ASN B 2 154 ? 29.915 -30.657 -71.173 1.00 112.30 ? 154 ASN B O 1 ATOM 3792 C CB . ASN B 2 154 ? 28.559 -29.189 -73.685 1.00 119.29 ? 154 ASN B CB 1 ATOM 3793 C CG . ASN B 2 154 ? 27.128 -28.722 -73.788 1.00 131.22 ? 154 ASN B CG 1 ATOM 3794 O OD1 . ASN B 2 154 ? 26.652 -27.947 -72.960 1.00 134.61 ? 154 ASN B OD1 1 ATOM 3795 N ND2 . ASN B 2 154 ? 26.426 -29.201 -74.819 1.00 146.72 ? 154 ASN B ND2 1 ATOM 3796 N N . GLY B 2 155 ? 31.384 -29.844 -72.680 1.00 102.34 ? 155 GLY B N 1 ATOM 3797 C CA . GLY B 2 155 ? 32.241 -31.022 -72.723 1.00 101.54 ? 155 GLY B CA 1 ATOM 3798 C C . GLY B 2 155 ? 31.947 -31.840 -73.972 1.00 103.07 ? 155 GLY B C 1 ATOM 3799 O O . GLY B 2 155 ? 32.400 -32.975 -74.094 1.00 107.01 ? 155 GLY B O 1 ATOM 3800 N N . THR B 2 156 ? 31.214 -31.244 -74.912 1.00 99.78 ? 156 THR B N 1 ATOM 3801 C CA . THR B 2 156 ? 30.655 -31.950 -76.064 1.00 103.80 ? 156 THR B CA 1 ATOM 3802 C C . THR B 2 156 ? 31.230 -31.473 -77.399 1.00 102.35 ? 156 THR B C 1 ATOM 3803 O O . THR B 2 156 ? 30.866 -31.997 -78.446 1.00 105.31 ? 156 THR B O 1 ATOM 3804 C CB . THR B 2 156 ? 29.120 -31.769 -76.072 1.00 105.99 ? 156 THR B CB 1 ATOM 3805 O OG1 . THR B 2 156 ? 28.566 -32.426 -74.927 1.00 108.23 ? 156 THR B OG1 1 ATOM 3806 C CG2 . THR B 2 156 ? 28.466 -32.337 -77.326 1.00 111.86 ? 156 THR B CG2 1 ATOM 3807 N N . TYR B 2 157 ? 32.134 -30.496 -77.368 1.00 99.61 ? 157 TYR B N 1 ATOM 3808 C CA . TYR B 2 157 ? 32.639 -29.882 -78.599 1.00 99.50 ? 157 TYR B CA 1 ATOM 3809 C C . TYR B 2 157 ? 33.063 -30.939 -79.607 1.00 107.06 ? 157 TYR B C 1 ATOM 3810 O O . TYR B 2 157 ? 34.101 -31.578 -79.445 1.00 107.75 ? 157 TYR B O 1 ATOM 3811 C CB . TYR B 2 157 ? 33.818 -28.959 -78.306 1.00 92.83 ? 157 TYR B CB 1 ATOM 3812 C CG . TYR B 2 157 ? 34.481 -28.407 -79.551 1.00 90.15 ? 157 TYR B CG 1 ATOM 3813 C CD1 . TYR B 2 157 ? 33.863 -27.419 -80.315 1.00 88.20 ? 157 TYR B CD1 1 ATOM 3814 C CD2 . TYR B 2 157 ? 35.724 -28.872 -79.963 1.00 89.39 ? 157 TYR B CD2 1 ATOM 3815 C CE1 . TYR B 2 157 ? 34.469 -26.910 -81.450 1.00 87.14 ? 157 TYR B CE1 1 ATOM 3816 C CE2 . TYR B 2 157 ? 36.338 -28.367 -81.096 1.00 88.21 ? 157 TYR B CE2 1 ATOM 3817 C CZ . TYR B 2 157 ? 35.709 -27.389 -81.836 1.00 86.79 ? 157 TYR B CZ 1 ATOM 3818 O OH . TYR B 2 157 ? 36.328 -26.893 -82.958 1.00 85.62 ? 157 TYR B OH 1 ATOM 3819 N N . ASP B 2 158 ? 32.252 -31.113 -80.644 1.00 115.89 ? 158 ASP B N 1 ATOM 3820 C CA . ASP B 2 158 ? 32.486 -32.164 -81.628 1.00 125.71 ? 158 ASP B CA 1 ATOM 3821 C C . ASP B 2 158 ? 33.696 -31.800 -82.491 1.00 126.96 ? 158 ASP B C 1 ATOM 3822 O O . ASP B 2 158 ? 33.582 -31.088 -83.493 1.00 126.60 ? 158 ASP B O 1 ATOM 3823 C CB . ASP B 2 158 ? 31.234 -32.406 -82.484 1.00 130.44 ? 158 ASP B CB 1 ATOM 3824 C CG . ASP B 2 158 ? 31.150 -33.824 -82.996 1.00 137.35 ? 158 ASP B CG 1 ATOM 3825 O OD1 . ASP B 2 158 ? 31.162 -34.754 -82.164 1.00 140.71 ? 158 ASP B OD1 1 ATOM 3826 O OD2 . ASP B 2 158 ? 31.080 -34.014 -84.225 1.00 141.08 ? 158 ASP B OD2 1 ATOM 3827 N N . TYR B 2 159 ? 34.860 -32.284 -82.066 1.00 130.31 ? 159 TYR B N 1 ATOM 3828 C CA . TYR B 2 159 ? 36.126 -31.981 -82.728 1.00 131.04 ? 159 TYR B CA 1 ATOM 3829 C C . TYR B 2 159 ? 36.125 -32.387 -84.213 1.00 137.81 ? 159 TYR B C 1 ATOM 3830 O O . TYR B 2 159 ? 36.457 -31.561 -85.067 1.00 137.65 ? 159 TYR B O 1 ATOM 3831 C CB . TYR B 2 159 ? 37.298 -32.613 -81.951 1.00 130.44 ? 159 TYR B CB 1 ATOM 3832 C CG . TYR B 2 159 ? 38.577 -32.777 -82.740 1.00 132.11 ? 159 TYR B CG 1 ATOM 3833 C CD1 . TYR B 2 159 ? 38.801 -33.923 -83.504 1.00 137.88 ? 159 TYR B CD1 1 ATOM 3834 C CD2 . TYR B 2 159 ? 39.567 -31.798 -82.715 1.00 127.36 ? 159 TYR B CD2 1 ATOM 3835 C CE1 . TYR B 2 159 ? 39.967 -34.084 -84.229 1.00 138.39 ? 159 TYR B CE1 1 ATOM 3836 C CE2 . TYR B 2 159 ? 40.740 -31.951 -83.436 1.00 129.24 ? 159 TYR B CE2 1 ATOM 3837 C CZ . TYR B 2 159 ? 40.936 -33.097 -84.192 1.00 134.83 ? 159 TYR B CZ 1 ATOM 3838 O OH . TYR B 2 159 ? 42.096 -33.267 -84.913 1.00 135.87 ? 159 TYR B OH 1 ATOM 3839 N N . PRO B 2 160 ? 35.732 -33.644 -84.529 1.00 146.44 ? 160 PRO B N 1 ATOM 3840 C CA . PRO B 2 160 ? 35.739 -34.101 -85.933 1.00 150.96 ? 160 PRO B CA 1 ATOM 3841 C C . PRO B 2 160 ? 34.846 -33.285 -86.880 1.00 150.00 ? 160 PRO B C 1 ATOM 3842 O O . PRO B 2 160 ? 35.127 -33.216 -88.077 1.00 152.38 ? 160 PRO B O 1 ATOM 3843 C CB . PRO B 2 160 ? 35.235 -35.550 -85.840 1.00 157.47 ? 160 PRO B CB 1 ATOM 3844 C CG . PRO B 2 160 ? 35.484 -35.960 -84.430 1.00 156.55 ? 160 PRO B CG 1 ATOM 3845 C CD . PRO B 2 160 ? 35.282 -34.715 -83.619 1.00 150.09 ? 160 PRO B CD 1 ATOM 3846 N N . GLN B 2 161 ? 33.785 -32.682 -86.346 1.00 146.97 ? 161 GLN B N 1 ATOM 3847 C CA . GLN B 2 161 ? 32.902 -31.814 -87.130 1.00 146.41 ? 161 GLN B CA 1 ATOM 3848 C C . GLN B 2 161 ? 33.642 -30.592 -87.684 1.00 140.01 ? 161 GLN B C 1 ATOM 3849 O O . GLN B 2 161 ? 33.245 -30.038 -88.709 1.00 141.68 ? 161 GLN B O 1 ATOM 3850 C CB . GLN B 2 161 ? 31.713 -31.363 -86.276 1.00 146.47 ? 161 GLN B CB 1 ATOM 3851 C CG . GLN B 2 161 ? 30.613 -30.632 -87.031 1.00 148.43 ? 161 GLN B CG 1 ATOM 3852 C CD . GLN B 2 161 ? 29.432 -30.285 -86.142 1.00 148.84 ? 161 GLN B CD 1 ATOM 3853 O OE1 . GLN B 2 161 ? 29.103 -31.019 -85.209 1.00 150.34 ? 161 GLN B OE1 1 ATOM 3854 N NE2 . GLN B 2 161 ? 28.786 -29.161 -86.428 1.00 147.97 ? 161 GLN B NE2 1 ATOM 3855 N N . TYR B 2 162 ? 34.707 -30.177 -87.000 1.00 133.30 ? 162 TYR B N 1 ATOM 3856 C CA . TYR B 2 162 ? 35.547 -29.076 -87.459 1.00 128.51 ? 162 TYR B CA 1 ATOM 3857 C C . TYR B 2 162 ? 36.984 -29.559 -87.625 1.00 125.36 ? 162 TYR B C 1 ATOM 3858 O O . TYR B 2 162 ? 37.690 -29.152 -88.547 1.00 121.25 ? 162 TYR B O 1 ATOM 3859 C CB . TYR B 2 162 ? 35.496 -27.915 -86.462 1.00 124.31 ? 162 TYR B CB 1 ATOM 3860 C CG . TYR B 2 162 ? 34.104 -27.568 -85.959 1.00 125.62 ? 162 TYR B CG 1 ATOM 3861 C CD1 . TYR B 2 162 ? 33.256 -26.741 -86.696 1.00 127.51 ? 162 TYR B CD1 1 ATOM 3862 C CD2 . TYR B 2 162 ? 33.643 -28.056 -84.737 1.00 125.34 ? 162 TYR B CD2 1 ATOM 3863 C CE1 . TYR B 2 162 ? 31.988 -26.416 -86.233 1.00 127.76 ? 162 TYR B CE1 1 ATOM 3864 C CE2 . TYR B 2 162 ? 32.378 -27.736 -84.266 1.00 125.84 ? 162 TYR B CE2 1 ATOM 3865 C CZ . TYR B 2 162 ? 31.554 -26.917 -85.015 1.00 126.88 ? 162 TYR B CZ 1 ATOM 3866 O OH . TYR B 2 162 ? 30.299 -26.599 -84.548 1.00 126.45 ? 162 TYR B OH 1 HETATM 3867 C C1 . NAG C 3 . ? 30.938 -4.042 -53.757 1.00 112.51 ? 1322 NAG A C1 1 HETATM 3868 C C2 . NAG C 3 . ? 30.043 -2.898 -53.273 1.00 124.55 ? 1322 NAG A C2 1 HETATM 3869 C C3 . NAG C 3 . ? 28.737 -3.430 -52.671 1.00 130.25 ? 1322 NAG A C3 1 HETATM 3870 C C4 . NAG C 3 . ? 28.067 -4.471 -53.565 1.00 132.83 ? 1322 NAG A C4 1 HETATM 3871 C C5 . NAG C 3 . ? 29.078 -5.504 -54.069 1.00 129.37 ? 1322 NAG A C5 1 HETATM 3872 C C6 . NAG C 3 . ? 28.445 -6.446 -55.096 1.00 127.54 ? 1322 NAG A C6 1 HETATM 3873 C C7 . NAG C 3 . ? 31.641 -1.154 -52.650 1.00 124.53 ? 1322 NAG A C7 1 HETATM 3874 C C8 . NAG C 3 . ? 32.305 -0.398 -51.536 1.00 121.51 ? 1322 NAG A C8 1 HETATM 3875 N N2 . NAG C 3 . ? 30.756 -2.087 -52.297 1.00 124.90 ? 1322 NAG A N2 1 HETATM 3876 O O3 . NAG C 3 . ? 27.824 -2.375 -52.456 1.00 130.63 ? 1322 NAG A O3 1 HETATM 3877 O O4 . NAG C 3 . ? 27.031 -5.103 -52.841 1.00 133.85 ? 1322 NAG A O4 1 HETATM 3878 O O5 . NAG C 3 . ? 30.190 -4.844 -54.655 1.00 122.59 ? 1322 NAG A O5 1 HETATM 3879 O O6 . NAG C 3 . ? 28.575 -7.787 -54.677 1.00 123.42 ? 1322 NAG A O6 1 HETATM 3880 O O7 . NAG C 3 . ? 31.926 -0.903 -53.821 1.00 124.94 ? 1322 NAG A O7 1 HETATM 3881 C C1 . NAG D 3 . ? 49.825 -6.292 -43.208 1.00 83.77 ? 1323 NAG A C1 1 HETATM 3882 C C2 . NAG D 3 . ? 51.150 -5.683 -42.760 1.00 97.20 ? 1323 NAG A C2 1 HETATM 3883 C C3 . NAG D 3 . ? 51.013 -5.093 -41.358 1.00 103.18 ? 1323 NAG A C3 1 HETATM 3884 C C4 . NAG D 3 . ? 49.789 -4.195 -41.225 1.00 108.23 ? 1323 NAG A C4 1 HETATM 3885 C C5 . NAG D 3 . ? 48.541 -4.867 -41.787 1.00 103.55 ? 1323 NAG A C5 1 HETATM 3886 C C6 . NAG D 3 . ? 47.354 -3.905 -41.846 1.00 102.30 ? 1323 NAG A C6 1 HETATM 3887 C C7 . NAG D 3 . ? 53.103 -6.833 -43.741 1.00 95.80 ? 1323 NAG A C7 1 HETATM 3888 C C8 . NAG D 3 . ? 54.133 -7.915 -43.576 1.00 94.61 ? 1323 NAG A C8 1 HETATM 3889 N N2 . NAG D 3 . ? 52.212 -6.684 -42.754 1.00 98.63 ? 1323 NAG A N2 1 HETATM 3890 O O3 . NAG D 3 . ? 52.161 -4.341 -41.047 1.00 103.24 ? 1323 NAG A O3 1 HETATM 3891 O O4 . NAG D 3 . ? 49.600 -3.888 -39.858 1.00 124.85 ? 1323 NAG A O4 1 HETATM 3892 O O5 . NAG D 3 . ? 48.810 -5.319 -43.095 1.00 93.46 ? 1323 NAG A O5 1 HETATM 3893 O O6 . NAG D 3 . ? 46.372 -4.295 -40.913 1.00 104.56 ? 1323 NAG A O6 1 HETATM 3894 O O7 . NAG D 3 . ? 53.118 -6.145 -44.759 1.00 94.07 ? 1323 NAG A O7 1 HETATM 3895 C C1 . NAG E 3 . ? 49.825 -2.487 -39.596 1.00 138.87 ? 1324 NAG A C1 1 HETATM 3896 C C2 . NAG E 3 . ? 49.633 -2.209 -38.106 1.00 141.30 ? 1324 NAG A C2 1 HETATM 3897 C C3 . NAG E 3 . ? 49.930 -0.749 -37.769 1.00 145.31 ? 1324 NAG A C3 1 HETATM 3898 C C4 . NAG E 3 . ? 51.242 -0.287 -38.396 1.00 147.54 ? 1324 NAG A C4 1 HETATM 3899 C C5 . NAG E 3 . ? 51.306 -0.675 -39.872 1.00 145.69 ? 1324 NAG A C5 1 HETATM 3900 C C6 . NAG E 3 . ? 52.645 -0.306 -40.504 1.00 143.66 ? 1324 NAG A C6 1 HETATM 3901 C C7 . NAG E 3 . ? 47.986 -3.748 -37.140 1.00 133.69 ? 1324 NAG A C7 1 HETATM 3902 C C8 . NAG E 3 . ? 46.556 -3.978 -36.741 1.00 133.27 ? 1324 NAG A C8 1 HETATM 3903 N N2 . NAG E 3 . ? 48.286 -2.561 -37.678 1.00 138.25 ? 1324 NAG A N2 1 HETATM 3904 O O3 . NAG E 3 . ? 50.008 -0.585 -36.370 1.00 143.63 ? 1324 NAG A O3 1 HETATM 3905 O O4 . NAG E 3 . ? 51.354 1.112 -38.249 1.00 150.43 ? 1324 NAG A O4 1 HETATM 3906 O O5 . NAG E 3 . ? 51.117 -2.069 -39.986 1.00 143.46 ? 1324 NAG A O5 1 HETATM 3907 O O6 . NAG E 3 . ? 52.440 0.603 -41.563 1.00 142.18 ? 1324 NAG A O6 1 HETATM 3908 O O7 . NAG E 3 . ? 48.816 -4.641 -36.964 1.00 125.41 ? 1324 NAG A O7 1 HETATM 3909 C C1 . NAG F 3 . ? 22.544 -39.534 14.323 1.00 100.24 ? 1325 NAG A C1 1 HETATM 3910 C C2 . NAG F 3 . ? 23.321 -40.779 14.743 1.00 110.39 ? 1325 NAG A C2 1 HETATM 3911 C C3 . NAG F 3 . ? 22.934 -41.967 13.860 1.00 112.91 ? 1325 NAG A C3 1 HETATM 3912 C C4 . NAG F 3 . ? 21.422 -42.106 13.756 1.00 115.01 ? 1325 NAG A C4 1 HETATM 3913 C C5 . NAG F 3 . ? 20.820 -40.778 13.337 1.00 114.91 ? 1325 NAG A C5 1 HETATM 3914 C C6 . NAG F 3 . ? 19.302 -40.802 13.176 1.00 117.41 ? 1325 NAG A C6 1 HETATM 3915 C C7 . NAG F 3 . ? 25.640 -41.258 15.336 1.00 121.20 ? 1325 NAG A C7 1 HETATM 3916 C C8 . NAG F 3 . ? 27.088 -40.916 15.151 1.00 122.41 ? 1325 NAG A C8 1 HETATM 3917 N N2 . NAG F 3 . ? 24.751 -40.537 14.651 1.00 116.57 ? 1325 NAG A N2 1 HETATM 3918 O O3 . NAG F 3 . ? 23.468 -43.175 14.352 1.00 118.46 ? 1325 NAG A O3 1 HETATM 3919 O O4 . NAG F 3 . ? 21.119 -43.097 12.803 1.00 125.91 ? 1325 NAG A O4 1 HETATM 3920 O O5 . NAG F 3 . ? 21.172 -39.864 14.338 1.00 107.07 ? 1325 NAG A O5 1 HETATM 3921 O O6 . NAG F 3 . ? 18.679 -41.097 14.406 1.00 121.23 ? 1325 NAG A O6 1 HETATM 3922 O O7 . NAG F 3 . ? 25.322 -42.172 16.094 1.00 127.20 ? 1325 NAG A O7 1 HETATM 3923 C C1 . NAG G 3 . ? 20.197 -44.050 13.348 1.00 135.37 ? 1326 NAG A C1 1 HETATM 3924 C C2 . NAG G 3 . ? 19.769 -45.011 12.244 1.00 141.43 ? 1326 NAG A C2 1 HETATM 3925 C C3 . NAG G 3 . ? 18.831 -46.096 12.765 1.00 146.04 ? 1326 NAG A C3 1 HETATM 3926 C C4 . NAG G 3 . ? 19.329 -46.708 14.080 1.00 151.22 ? 1326 NAG A C4 1 HETATM 3927 C C5 . NAG G 3 . ? 19.836 -45.632 15.043 1.00 145.35 ? 1326 NAG A C5 1 HETATM 3928 C C6 . NAG G 3 . ? 20.484 -46.246 16.281 1.00 143.66 ? 1326 NAG A C6 1 HETATM 3929 C C7 . NAG G 3 . ? 18.099 -43.697 10.861 1.00 143.90 ? 1326 NAG A C7 1 HETATM 3930 C C8 . NAG G 3 . ? 17.061 -43.543 11.943 1.00 141.07 ? 1326 NAG A C8 1 HETATM 3931 N N2 . NAG G 3 . ? 19.266 -44.342 11.041 1.00 144.02 ? 1326 NAG A N2 1 HETATM 3932 O O3 . NAG G 3 . ? 18.694 -47.062 11.746 1.00 142.60 ? 1326 NAG A O3 1 HETATM 3933 O O4 . NAG G 3 . ? 18.299 -47.410 14.759 1.00 164.15 ? 1326 NAG A O4 1 HETATM 3934 O O5 . NAG G 3 . ? 20.773 -44.801 14.392 1.00 140.08 ? 1326 NAG A O5 1 HETATM 3935 O O6 . NAG G 3 . ? 21.009 -45.224 17.097 1.00 139.76 ? 1326 NAG A O6 1 HETATM 3936 O O7 . NAG G 3 . ? 17.844 -43.196 9.768 1.00 139.88 ? 1326 NAG A O7 1 HETATM 3937 C C1 . BMA H 4 . ? 17.857 -48.659 14.172 1.00 174.08 ? 1327 BMA A C1 1 HETATM 3938 C C2 . BMA H 4 . ? 18.162 -49.951 14.941 1.00 173.72 ? 1327 BMA A C2 1 HETATM 3939 C C3 . BMA H 4 . ? 18.161 -51.205 14.073 1.00 177.85 ? 1327 BMA A C3 1 HETATM 3940 C C4 . BMA H 4 . ? 17.119 -51.114 12.962 1.00 183.69 ? 1327 BMA A C4 1 HETATM 3941 C C5 . BMA H 4 . ? 17.362 -49.874 12.107 1.00 183.98 ? 1327 BMA A C5 1 HETATM 3942 C C6 . BMA H 4 . ? 16.388 -49.781 10.937 1.00 183.12 ? 1327 BMA A C6 1 HETATM 3943 O O2 . BMA H 4 . ? 17.182 -50.080 15.980 1.00 165.45 ? 1327 BMA A O2 1 HETATM 3944 O O3 . BMA H 4 . ? 17.874 -52.320 14.930 1.00 175.68 ? 1327 BMA A O3 1 HETATM 3945 O O4 . BMA H 4 . ? 17.163 -52.288 12.139 1.00 184.13 ? 1327 BMA A O4 1 HETATM 3946 O O5 . BMA H 4 . ? 17.208 -48.687 12.892 1.00 182.75 ? 1327 BMA A O5 1 HETATM 3947 O O6 . BMA H 4 . ? 16.371 -51.016 10.207 1.00 182.56 ? 1327 BMA A O6 1 HETATM 3948 C C1 . BMA I 4 . ? 18.573 -53.523 14.561 1.00 168.80 ? 1328 BMA A C1 1 HETATM 3949 C C2 . BMA I 4 . ? 19.950 -53.565 15.218 1.00 165.18 ? 1328 BMA A C2 1 HETATM 3950 C C3 . BMA I 4 . ? 20.651 -54.885 14.902 1.00 160.89 ? 1328 BMA A C3 1 HETATM 3951 C C4 . BMA I 4 . ? 19.724 -56.066 15.182 1.00 160.75 ? 1328 BMA A C4 1 HETATM 3952 C C5 . BMA I 4 . ? 18.359 -55.873 14.518 1.00 159.92 ? 1328 BMA A C5 1 HETATM 3953 C C6 . BMA I 4 . ? 17.386 -56.999 14.862 1.00 154.23 ? 1328 BMA A C6 1 HETATM 3954 O O2 . BMA I 4 . ? 19.816 -53.408 16.614 1.00 165.77 ? 1328 BMA A O2 1 HETATM 3955 O O3 . BMA I 4 . ? 21.828 -55.009 15.670 1.00 156.05 ? 1328 BMA A O3 1 HETATM 3956 O O4 . BMA I 4 . ? 20.324 -57.262 14.728 1.00 154.83 ? 1328 BMA A O4 1 HETATM 3957 O O5 . BMA I 4 . ? 17.813 -54.646 14.952 1.00 165.23 ? 1328 BMA A O5 1 HETATM 3958 O O6 . BMA I 4 . ? 16.043 -56.594 14.707 1.00 148.51 ? 1328 BMA A O6 1 HETATM 3959 C C1 . MAN J 5 . ? 15.620 -50.976 8.968 1.00 181.93 ? 1329 MAN A C1 1 HETATM 3960 C C2 . MAN J 5 . ? 16.588 -50.612 7.833 1.00 180.30 ? 1329 MAN A C2 1 HETATM 3961 C C3 . MAN J 5 . ? 16.589 -49.127 7.477 1.00 177.26 ? 1329 MAN A C3 1 HETATM 3962 C C4 . MAN J 5 . ? 15.161 -48.625 7.322 1.00 179.30 ? 1329 MAN A C4 1 HETATM 3963 C C5 . MAN J 5 . ? 14.379 -48.849 8.611 1.00 177.92 ? 1329 MAN A C5 1 HETATM 3964 C C6 . MAN J 5 . ? 12.913 -48.456 8.430 1.00 171.24 ? 1329 MAN A C6 1 HETATM 3965 O O2 . MAN J 5 . ? 16.274 -51.383 6.692 1.00 178.40 ? 1329 MAN A O2 1 HETATM 3966 O O3 . MAN J 5 . ? 17.301 -48.927 6.276 1.00 171.32 ? 1329 MAN A O3 1 HETATM 3967 O O4 . MAN J 5 . ? 15.171 -47.250 7.006 1.00 177.13 ? 1329 MAN A O4 1 HETATM 3968 O O5 . MAN J 5 . ? 14.414 -50.210 9.017 1.00 183.01 ? 1329 MAN A O5 1 HETATM 3969 O O6 . MAN J 5 . ? 12.659 -47.204 9.028 1.00 163.21 ? 1329 MAN A O6 1 HETATM 3970 C C1 . NAG K 3 . ? 23.522 -12.093 -30.295 1.00 121.74 ? 1330 NAG A C1 1 HETATM 3971 C C2 . NAG K 3 . ? 22.197 -11.446 -29.862 1.00 133.34 ? 1330 NAG A C2 1 HETATM 3972 C C3 . NAG K 3 . ? 21.288 -11.038 -31.031 1.00 136.12 ? 1330 NAG A C3 1 HETATM 3973 C C4 . NAG K 3 . ? 22.047 -10.532 -32.261 1.00 138.16 ? 1330 NAG A C4 1 HETATM 3974 C C5 . NAG K 3 . ? 23.261 -11.409 -32.554 1.00 134.88 ? 1330 NAG A C5 1 HETATM 3975 C C6 . NAG K 3 . ? 24.086 -10.909 -33.739 1.00 131.64 ? 1330 NAG A C6 1 HETATM 3976 C C7 . NAG K 3 . ? 21.390 -12.199 -27.655 1.00 132.08 ? 1330 NAG A C7 1 HETATM 3977 C C8 . NAG K 3 . ? 20.613 -13.232 -26.889 1.00 128.22 ? 1330 NAG A C8 1 HETATM 3978 N N2 . NAG K 3 . ? 21.475 -12.360 -28.981 1.00 132.86 ? 1330 NAG A N2 1 HETATM 3979 O O3 . NAG K 3 . ? 20.394 -10.036 -30.593 1.00 133.94 ? 1330 NAG A O3 1 HETATM 3980 O O4 . NAG K 3 . ? 21.178 -10.514 -33.374 1.00 142.18 ? 1330 NAG A O4 1 HETATM 3981 O O5 . NAG K 3 . ? 24.076 -11.409 -31.405 1.00 130.20 ? 1330 NAG A O5 1 HETATM 3982 O O6 . NAG K 3 . ? 24.420 -11.998 -34.570 1.00 130.27 ? 1330 NAG A O6 1 HETATM 3983 O O7 . NAG K 3 . ? 21.906 -11.264 -27.041 1.00 131.30 ? 1330 NAG A O7 1 HETATM 3984 C C1 . SIA L 6 . ? 35.947 -4.993 21.837 1.00 108.52 ? 1331 SIA A C1 1 HETATM 3985 C C2 . SIA L 6 . ? 36.228 -5.157 23.323 1.00 101.46 ? 1331 SIA A C2 1 HETATM 3986 C C3 . SIA L 6 . ? 34.911 -5.020 24.089 1.00 97.76 ? 1331 SIA A C3 1 HETATM 3987 C C4 . SIA L 6 . ? 34.039 -6.246 23.890 1.00 96.25 ? 1331 SIA A C4 1 HETATM 3988 C C5 . SIA L 6 . ? 34.816 -7.466 24.354 1.00 96.17 ? 1331 SIA A C5 1 HETATM 3989 C C6 . SIA L 6 . ? 36.094 -7.593 23.522 1.00 91.82 ? 1331 SIA A C6 1 HETATM 3990 C C7 . SIA L 6 . ? 36.990 -8.767 23.915 1.00 88.88 ? 1331 SIA A C7 1 HETATM 3991 C C8 . SIA L 6 . ? 38.373 -8.703 23.258 1.00 88.00 ? 1331 SIA A C8 1 HETATM 3992 C C9 . SIA L 6 . ? 39.060 -10.062 23.302 1.00 86.86 ? 1331 SIA A C9 1 HETATM 3993 C C10 . SIA L 6 . ? 33.938 -9.700 24.826 1.00 102.83 ? 1331 SIA A C10 1 HETATM 3994 C C11 . SIA L 6 . ? 32.979 -10.774 24.404 1.00 102.96 ? 1331 SIA A C11 1 HETATM 3995 N N5 . SIA L 6 . ? 33.942 -8.601 24.075 1.00 99.12 ? 1331 SIA A N5 1 HETATM 3996 O O1A . SIA L 6 . ? 35.283 -3.997 21.458 1.00 111.55 ? 1331 SIA A O1A 1 HETATM 3997 O O1B . SIA L 6 . ? 36.381 -5.845 21.028 1.00 111.15 ? 1331 SIA A O1B 1 HETATM 3998 O O4 . SIA L 6 . ? 32.817 -6.111 24.618 1.00 94.20 ? 1331 SIA A O4 1 HETATM 3999 O O6 . SIA L 6 . ? 36.870 -6.399 23.639 1.00 92.48 ? 1331 SIA A O6 1 HETATM 4000 O O7 . SIA L 6 . ? 37.153 -8.795 25.332 1.00 87.97 ? 1331 SIA A O7 1 HETATM 4001 O O8 . SIA L 6 . ? 38.286 -8.293 21.886 1.00 90.41 ? 1331 SIA A O8 1 HETATM 4002 O O9 . SIA L 6 . ? 40.339 -9.994 22.662 1.00 85.43 ? 1331 SIA A O9 1 HETATM 4003 O O10 . SIA L 6 . ? 34.676 -9.837 25.789 1.00 103.09 ? 1331 SIA A O10 1 HETATM 4004 C C1 . GAL M 7 . ? 37.940 -0.355 22.939 1.00 124.10 ? 1332 GAL A C1 1 HETATM 4005 C C2 . GAL M 7 . ? 38.917 0.086 21.840 1.00 122.63 ? 1332 GAL A C2 1 HETATM 4006 C C3 . GAL M 7 . ? 39.514 -1.041 20.972 1.00 118.67 ? 1332 GAL A C3 1 HETATM 4007 C C4 . GAL M 7 . ? 39.604 -2.409 21.655 1.00 116.87 ? 1332 GAL A C4 1 HETATM 4008 C C5 . GAL M 7 . ? 38.371 -2.640 22.512 1.00 115.22 ? 1332 GAL A C5 1 HETATM 4009 C C6 . GAL M 7 . ? 38.376 -4.000 23.191 1.00 109.52 ? 1332 GAL A C6 1 HETATM 4010 O O1 . GAL M 7 . ? 37.918 0.626 23.977 1.00 121.75 ? 1332 GAL A O1 1 HETATM 4011 O O2 . GAL M 7 . ? 38.212 0.999 20.984 1.00 118.55 ? 1332 GAL A O2 1 HETATM 4012 O O3 . GAL M 7 . ? 40.827 -0.657 20.541 1.00 114.00 ? 1332 GAL A O3 1 HETATM 4013 O O4 . GAL M 7 . ? 40.787 -2.519 22.461 1.00 111.76 ? 1332 GAL A O4 1 HETATM 4014 O O5 . GAL M 7 . ? 38.306 -1.616 23.503 1.00 122.91 ? 1332 GAL A O5 1 HETATM 4015 O O6 . GAL M 7 . ? 37.093 -4.127 23.805 1.00 107.35 ? 1332 GAL A O6 1 HETATM 4016 C C1 . NAG N 3 . ? 25.043 -28.876 -75.080 1.00 105.44 ? 1163 NAG B C1 1 HETATM 4017 C C2 . NAG N 3 . ? 24.052 -30.054 -75.139 1.00 113.43 ? 1163 NAG B C2 1 HETATM 4018 C C3 . NAG N 3 . ? 23.576 -30.456 -76.537 1.00 118.58 ? 1163 NAG B C3 1 HETATM 4019 C C4 . NAG N 3 . ? 23.469 -29.251 -77.459 1.00 124.83 ? 1163 NAG B C4 1 HETATM 4020 C C5 . NAG N 3 . ? 24.802 -28.509 -77.438 1.00 118.71 ? 1163 NAG B C5 1 HETATM 4021 C C6 . NAG N 3 . ? 24.898 -27.390 -78.475 1.00 115.45 ? 1163 NAG B C6 1 HETATM 4022 C C7 . NAG N 3 . ? 24.688 -31.312 -73.147 1.00 113.25 ? 1163 NAG B C7 1 HETATM 4023 C C8 . NAG N 3 . ? 25.297 -32.569 -72.593 1.00 110.08 ? 1163 NAG B C8 1 HETATM 4024 N N2 . NAG N 3 . ? 24.618 -31.218 -74.474 1.00 112.78 ? 1163 NAG B N2 1 HETATM 4025 O O3 . NAG N 3 . ? 22.320 -31.094 -76.438 1.00 114.31 ? 1163 NAG B O3 1 HETATM 4026 O O4 . NAG N 3 . ? 23.072 -29.664 -78.758 1.00 131.93 ? 1163 NAG B O4 1 HETATM 4027 O O5 . NAG N 3 . ? 24.924 -27.951 -76.148 1.00 112.02 ? 1163 NAG B O5 1 HETATM 4028 O O6 . NAG N 3 . ? 24.214 -26.245 -78.015 1.00 114.71 ? 1163 NAG B O6 1 HETATM 4029 O O7 . NAG N 3 . ? 24.285 -30.431 -72.387 1.00 113.25 ? 1163 NAG B O7 1 HETATM 4030 C C1 . NAG O 3 . ? 21.813 -29.058 -79.116 1.00 136.67 ? 1164 NAG B C1 1 HETATM 4031 C C2 . NAG O 3 . ? 21.461 -29.417 -80.558 1.00 136.97 ? 1164 NAG B C2 1 HETATM 4032 C C3 . NAG O 3 . ? 20.053 -28.941 -80.928 1.00 144.43 ? 1164 NAG B C3 1 HETATM 4033 C C4 . NAG O 3 . ? 19.028 -29.265 -79.838 1.00 149.98 ? 1164 NAG B C4 1 HETATM 4034 C C5 . NAG O 3 . ? 19.547 -28.812 -78.474 1.00 145.40 ? 1164 NAG B C5 1 HETATM 4035 C C6 . NAG O 3 . ? 18.584 -29.132 -77.332 1.00 140.37 ? 1164 NAG B C6 1 HETATM 4036 C C7 . NAG O 3 . ? 23.641 -29.359 -81.692 1.00 128.55 ? 1164 NAG B C7 1 HETATM 4037 C C8 . NAG O 3 . ? 24.522 -28.646 -82.677 1.00 124.63 ? 1164 NAG B C8 1 HETATM 4038 N N2 . NAG O 3 . ? 22.429 -28.840 -81.481 1.00 133.24 ? 1164 NAG B N2 1 HETATM 4039 O O3 . NAG O 3 . ? 19.668 -29.527 -82.152 1.00 142.22 ? 1164 NAG B O3 1 HETATM 4040 O O4 . NAG O 3 . ? 17.770 -28.671 -80.129 1.00 159.26 ? 1164 NAG B O4 1 HETATM 4041 O O5 . NAG O 3 . ? 20.778 -29.463 -78.240 1.00 143.12 ? 1164 NAG B O5 1 HETATM 4042 O O6 . NAG O 3 . ? 18.534 -30.524 -77.122 1.00 134.25 ? 1164 NAG B O6 1 HETATM 4043 O O7 . NAG O 3 . ? 24.054 -30.368 -81.123 1.00 130.11 ? 1164 NAG B O7 1 HETATM 4044 C C1 . BMA P 4 . ? 16.918 -29.559 -80.887 1.00 168.00 ? 1165 BMA B C1 1 HETATM 4045 C C2 . BMA P 4 . ? 15.495 -29.516 -80.340 1.00 168.47 ? 1165 BMA B C2 1 HETATM 4046 C C3 . BMA P 4 . ? 14.612 -30.504 -81.101 1.00 169.60 ? 1165 BMA B C3 1 HETATM 4047 C C4 . BMA P 4 . ? 14.767 -30.365 -82.617 1.00 168.84 ? 1165 BMA B C4 1 HETATM 4048 C C5 . BMA P 4 . ? 16.229 -30.254 -83.056 1.00 166.76 ? 1165 BMA B C5 1 HETATM 4049 C C6 . BMA P 4 . ? 16.343 -29.950 -84.552 1.00 162.73 ? 1165 BMA B C6 1 HETATM 4050 O O2 . BMA P 4 . ? 14.968 -28.188 -80.450 1.00 165.15 ? 1165 BMA B O2 1 HETATM 4051 O O3 . BMA P 4 . ? 13.242 -30.300 -80.732 1.00 169.52 ? 1165 BMA B O3 1 HETATM 4052 O O4 . BMA P 4 . ? 14.180 -31.506 -83.252 1.00 166.21 ? 1165 BMA B O4 1 HETATM 4053 O O5 . BMA P 4 . ? 16.892 -29.248 -82.282 1.00 169.98 ? 1165 BMA B O5 1 HETATM 4054 O O6 . BMA P 4 . ? 17.086 -28.747 -84.783 1.00 157.67 ? 1165 BMA B O6 1 HETATM 4055 S S1 . MPO Q 8 . ? 38.142 -10.908 -71.162 1.00 130.35 ? 1166 MPO B S1 1 HETATM 4056 O O1 . MPO Q 8 . ? 39.190 -10.174 -70.502 1.00 139.84 ? 1166 MPO B O1 1 HETATM 4057 O O2 . MPO Q 8 . ? 37.557 -10.070 -72.174 1.00 136.21 ? 1166 MPO B O2 1 HETATM 4058 O O4 . MPO Q 8 . ? 44.322 -10.106 -72.956 1.00 124.78 ? 1166 MPO B O4 1 HETATM 4059 N N1 . MPO Q 8 . ? 42.087 -11.014 -71.415 1.00 122.69 ? 1166 MPO B N1 1 HETATM 4060 C C1 . MPO Q 8 . ? 38.736 -12.304 -71.853 1.00 115.56 ? 1166 MPO B C1 1 HETATM 4061 O O3 . MPO Q 8 . ? 36.978 -11.277 -70.073 1.00 132.16 ? 1166 MPO B O3 1 HETATM 4062 C C2 . MPO Q 8 . ? 40.184 -12.578 -71.452 1.00 111.51 ? 1166 MPO B C2 1 HETATM 4063 C C3 . MPO Q 8 . ? 41.172 -11.780 -72.295 1.00 116.13 ? 1166 MPO B C3 1 HETATM 4064 C C4 . MPO Q 8 . ? 42.185 -9.600 -71.844 1.00 129.26 ? 1166 MPO B C4 1 HETATM 4065 C C5 . MPO Q 8 . ? 43.058 -9.450 -73.092 1.00 127.29 ? 1166 MPO B C5 1 HETATM 4066 C C6 . MPO Q 8 . ? 44.555 -10.701 -71.677 1.00 124.31 ? 1166 MPO B C6 1 HETATM 4067 C C7 . MPO Q 8 . ? 43.417 -11.655 -71.312 1.00 123.00 ? 1166 MPO B C7 1 HETATM 4068 O O . HOH R 9 . ? 38.714 -13.676 -82.201 1.00 77.25 ? 2001 HOH A O 1 HETATM 4069 O O . HOH R 9 . ? 42.984 -12.924 -76.433 1.00 78.98 ? 2002 HOH A O 1 HETATM 4070 O O . HOH R 9 . ? 41.508 -15.740 -70.002 1.00 63.72 ? 2003 HOH A O 1 HETATM 4071 O O . HOH R 9 . ? 40.095 -14.351 -65.410 1.00 60.01 ? 2004 HOH A O 1 HETATM 4072 O O . HOH R 9 . ? 40.356 -12.405 -58.676 1.00 54.66 ? 2005 HOH A O 1 HETATM 4073 O O . HOH R 9 . ? 31.511 -11.311 -54.672 1.00 69.11 ? 2006 HOH A O 1 HETATM 4074 O O . HOH R 9 . ? 32.110 -6.758 -56.109 1.00 63.43 ? 2007 HOH A O 1 HETATM 4075 O O . HOH R 9 . ? 32.601 -2.161 -57.160 1.00 77.56 ? 2008 HOH A O 1 HETATM 4076 O O . HOH R 9 . ? 34.359 -10.264 -49.612 1.00 79.67 ? 2009 HOH A O 1 HETATM 4077 O O . HOH R 9 . ? 46.304 -10.491 -43.711 1.00 71.70 ? 2010 HOH A O 1 HETATM 4078 O O . HOH R 9 . ? 44.774 -14.859 -42.197 1.00 54.19 ? 2011 HOH A O 1 HETATM 4079 O O . HOH R 9 . ? 51.594 -18.477 -50.400 1.00 73.16 ? 2012 HOH A O 1 HETATM 4080 O O . HOH R 9 . ? 52.534 -16.586 -51.918 1.00 68.23 ? 2013 HOH A O 1 HETATM 4081 O O . HOH R 9 . ? 31.765 -17.501 -50.590 1.00 71.18 ? 2014 HOH A O 1 HETATM 4082 O O . HOH R 9 . ? 34.571 -11.709 -47.261 1.00 72.11 ? 2015 HOH A O 1 HETATM 4083 O O . HOH R 9 . ? 32.416 -18.125 -45.577 1.00 73.61 ? 2016 HOH A O 1 HETATM 4084 O O . HOH R 9 . ? 33.841 -13.189 -41.592 1.00 70.77 ? 2017 HOH A O 1 HETATM 4085 O O . HOH R 9 . ? 40.129 -12.310 -36.749 1.00 58.72 ? 2018 HOH A O 1 HETATM 4086 O O . HOH R 9 . ? 40.253 -9.679 -37.816 1.00 74.60 ? 2019 HOH A O 1 HETATM 4087 O O . HOH R 9 . ? 30.507 -11.328 -28.018 1.00 65.79 ? 2020 HOH A O 1 HETATM 4088 O O . HOH R 9 . ? 27.841 -5.160 -15.540 1.00 78.28 ? 2021 HOH A O 1 HETATM 4089 O O . HOH R 9 . ? 25.488 -13.882 5.736 1.00 72.28 ? 2022 HOH A O 1 HETATM 4090 O O . HOH R 9 . ? 25.108 -6.765 2.909 1.00 78.96 ? 2023 HOH A O 1 HETATM 4091 O O . HOH R 9 . ? 25.921 -5.401 0.491 1.00 77.89 ? 2024 HOH A O 1 HETATM 4092 O O . HOH R 9 . ? 18.147 -18.049 8.894 1.00 75.95 ? 2025 HOH A O 1 HETATM 4093 O O . HOH R 9 . ? 38.002 -14.476 -0.332 1.00 69.36 ? 2026 HOH A O 1 HETATM 4094 O O . HOH R 9 . ? 43.110 -24.653 1.767 1.00 71.99 ? 2027 HOH A O 1 HETATM 4095 O O . HOH R 9 . ? 46.756 -18.039 -56.050 1.00 59.26 ? 2028 HOH A O 1 HETATM 4096 O O . HOH R 9 . ? 28.120 -13.994 24.945 1.00 75.77 ? 2029 HOH A O 1 HETATM 4097 O O . HOH R 9 . ? 28.039 0.428 11.878 1.00 79.83 ? 2030 HOH A O 1 HETATM 4098 O O . HOH R 9 . ? 27.412 -0.657 21.319 1.00 78.83 ? 2031 HOH A O 1 HETATM 4099 O O . HOH R 9 . ? 26.634 -12.677 16.141 1.00 73.31 ? 2032 HOH A O 1 HETATM 4100 O O . HOH R 9 . ? 23.718 -35.282 4.194 1.00 80.59 ? 2033 HOH A O 1 HETATM 4101 O O . HOH R 9 . ? 39.613 -12.941 -13.466 1.00 79.63 ? 2034 HOH A O 1 HETATM 4102 O O . HOH R 9 . ? 40.602 -8.748 -24.060 1.00 73.79 ? 2035 HOH A O 1 HETATM 4103 O O . HOH R 9 . ? 41.765 -8.541 -30.867 1.00 72.92 ? 2036 HOH A O 1 HETATM 4104 O O . HOH R 9 . ? 37.553 -21.421 -19.347 1.00 77.02 ? 2037 HOH A O 1 HETATM 4105 O O . HOH R 9 . ? 45.116 -15.304 -39.446 1.00 62.70 ? 2038 HOH A O 1 HETATM 4106 O O . HOH R 9 . ? 41.572 -21.411 -45.907 1.00 56.42 ? 2039 HOH A O 1 HETATM 4107 O O . HOH R 9 . ? 32.443 -19.863 -49.660 1.00 77.22 ? 2040 HOH A O 1 HETATM 4108 O O . HOH R 9 . ? 44.057 -18.222 -55.353 1.00 54.03 ? 2041 HOH A O 1 HETATM 4109 O O . HOH R 9 . ? 48.327 -16.959 -57.692 1.00 62.48 ? 2042 HOH A O 1 HETATM 4110 O O . HOH S 9 . ? 49.271 -19.389 -60.292 1.00 60.00 ? 2001 HOH B O 1 HETATM 4111 O O . HOH S 9 . ? 52.587 -25.891 -61.916 1.00 69.05 ? 2002 HOH B O 1 HETATM 4112 O O . HOH S 9 . ? 45.694 -13.158 -69.417 1.00 71.90 ? 2003 HOH B O 1 HETATM 4113 O O . HOH S 9 . ? 49.437 -11.480 -63.332 1.00 76.72 ? 2004 HOH B O 1 HETATM 4114 O O . HOH S 9 . ? 41.815 -8.980 -65.524 1.00 70.72 ? 2005 HOH B O 1 HETATM 4115 O O . HOH S 9 . ? 41.364 -13.579 -68.226 1.00 69.86 ? 2006 HOH B O 1 HETATM 4116 O O . HOH S 9 . ? 35.494 -8.748 -66.194 1.00 65.85 ? 2007 HOH B O 1 HETATM 4117 O O . HOH S 9 . ? 28.474 -15.389 -65.664 1.00 77.13 ? 2008 HOH B O 1 HETATM 4118 O O . HOH S 9 . ? 31.097 -17.217 -55.798 1.00 65.65 ? 2009 HOH B O 1 HETATM 4119 O O . HOH S 9 . ? 32.689 -21.430 -47.544 1.00 77.67 ? 2010 HOH B O 1 HETATM 4120 O O . HOH S 9 . ? 34.149 -31.309 -41.924 1.00 70.29 ? 2011 HOH B O 1 HETATM 4121 O O . HOH S 9 . ? 36.869 -33.895 -42.519 1.00 67.71 ? 2012 HOH B O 1 HETATM 4122 O O . HOH S 9 . ? 51.953 -27.035 -1.175 1.00 68.90 ? 2013 HOH B O 1 HETATM 4123 O O . HOH S 9 . ? 47.683 -19.585 -10.463 1.00 66.45 ? 2014 HOH B O 1 HETATM 4124 O O . HOH S 9 . ? 53.467 -24.130 -23.858 1.00 62.58 ? 2015 HOH B O 1 HETATM 4125 O O . HOH S 9 . ? 51.930 -19.760 -28.975 1.00 69.17 ? 2016 HOH B O 1 HETATM 4126 O O . HOH S 9 . ? 47.522 -26.791 -35.983 1.00 56.08 ? 2017 HOH B O 1 HETATM 4127 O O . HOH S 9 . ? 47.051 -17.296 -38.607 1.00 60.96 ? 2018 HOH B O 1 HETATM 4128 O O . HOH S 9 . ? 45.895 -27.065 -52.225 1.00 51.53 ? 2019 HOH B O 1 HETATM 4129 O O . HOH S 9 . ? 44.451 -29.269 -51.382 1.00 59.54 ? 2020 HOH B O 1 HETATM 4130 O O . HOH S 9 . ? 49.418 -31.870 -52.327 1.00 57.83 ? 2021 HOH B O 1 HETATM 4131 O O . HOH S 9 . ? 51.741 -22.307 -52.388 1.00 56.62 ? 2022 HOH B O 1 HETATM 4132 O O . HOH S 9 . ? 41.978 -29.002 -57.674 1.00 58.12 ? 2023 HOH B O 1 HETATM 4133 O O . HOH S 9 . ? 38.258 -27.385 -62.165 1.00 62.45 ? 2024 HOH B O 1 HETATM 4134 O O . HOH S 9 . ? 37.403 -29.302 -57.404 1.00 77.41 ? 2025 HOH B O 1 HETATM 4135 O O . HOH S 9 . ? 41.667 -31.090 -66.683 1.00 66.93 ? 2026 HOH B O 1 HETATM 4136 O O . HOH S 9 . ? 44.822 -30.317 -65.390 1.00 61.52 ? 2027 HOH B O 1 HETATM 4137 O O . HOH S 9 . ? 45.684 -19.820 -73.712 1.00 59.18 ? 2028 HOH B O 1 HETATM 4138 O O . HOH S 9 . ? 38.452 -32.567 -72.038 1.00 71.88 ? 2029 HOH B O 1 HETATM 4139 O O . HOH S 9 . ? 47.716 -23.968 -80.748 1.00 75.53 ? 2030 HOH B O 1 # loop_ _atom_site_anisotrop.id _atom_site_anisotrop.type_symbol _atom_site_anisotrop.pdbx_label_atom_id _atom_site_anisotrop.pdbx_label_alt_id _atom_site_anisotrop.pdbx_label_comp_id _atom_site_anisotrop.pdbx_label_asym_id _atom_site_anisotrop.pdbx_label_seq_id _atom_site_anisotrop.pdbx_PDB_ins_code _atom_site_anisotrop.U[1][1] _atom_site_anisotrop.U[2][2] _atom_site_anisotrop.U[3][3] _atom_site_anisotrop.U[1][2] _atom_site_anisotrop.U[1][3] _atom_site_anisotrop.U[2][3] _atom_site_anisotrop.pdbx_auth_seq_id _atom_site_anisotrop.pdbx_auth_comp_id _atom_site_anisotrop.pdbx_auth_asym_id _atom_site_anisotrop.pdbx_auth_atom_id 1 N N . ASP A 1 ? 0.9780 0.9962 0.8546 0.3521 -0.1019 0.0035 1 ASP A N 2 C CA . ASP A 1 ? 0.9399 1.0226 0.8547 0.3467 -0.1049 -0.0082 1 ASP A CA 3 C C . ASP A 1 ? 0.8999 0.9714 0.8471 0.3088 -0.0962 -0.0060 1 ASP A C 4 O O . ASP A 1 ? 0.8649 0.9236 0.8273 0.2805 -0.0904 -0.0025 1 ASP A O 5 C CB . ASP A 1 ? 0.9144 1.0767 0.8574 0.3440 -0.1111 -0.0213 1 ASP A CB 6 C CG . ASP A 1 ? 0.9610 1.1466 0.8751 0.3833 -0.1208 -0.0253 1 ASP A CG 7 O OD1 . ASP A 1 ? 1.0014 1.1358 0.8696 0.4150 -0.1227 -0.0171 1 ASP A OD1 8 O OD2 . ASP A 1 ? 0.9969 1.2520 0.9316 0.3824 -0.1262 -0.0372 1 ASP A OD2 9 N N . GLN A 2 ? 0.9041 0.9806 0.8600 0.3103 -0.0954 -0.0083 2 GLN A N 10 C CA . GLN A 2 ? 0.8579 0.9260 0.8429 0.2772 -0.0877 -0.0066 2 GLN A CA 11 C C . GLN A 2 ? 0.8141 0.9290 0.8251 0.2753 -0.0895 -0.0160 2 GLN A C 12 O O . GLN A 2 ? 0.8124 0.9555 0.8134 0.3034 -0.0961 -0.0223 2 GLN A O 13 C CB . GLN A 2 ? 0.9077 0.9014 0.8687 0.2714 -0.0804 0.0057 2 GLN A CB 14 C CG . GLN A 2 ? 0.9822 0.9394 0.9067 0.2992 -0.0820 0.0091 2 GLN A CG 15 C CD . GLN A 2 ? 1.0421 0.9244 0.9398 0.2874 -0.0733 0.0204 2 GLN A CD 16 O OE1 . GLN A 2 ? 1.0641 0.9253 0.9591 0.2838 -0.0698 0.0219 2 GLN A OE1 17 N NE2 . GLN A 2 ? 1.0946 0.9385 0.9719 0.2796 -0.0694 0.0276 2 GLN A NE2 18 N N . ILE A 3 ? 0.7452 0.8685 0.7879 0.2426 -0.0833 -0.0172 3 ILE A N 19 C CA . ILE A 3 ? 0.7277 0.8847 0.7942 0.2346 -0.0828 -0.0243 3 ILE A CA 20 C C . ILE A 3 ? 0.7363 0.8464 0.8071 0.2151 -0.0748 -0.0158 3 ILE A C 21 O O . ILE A 3 ? 0.7355 0.8140 0.8090 0.1948 -0.0690 -0.0089 3 ILE A O 22 C CB . ILE A 3 ? 0.7094 0.9301 0.8083 0.2131 -0.0830 -0.0365 3 ILE A CB 23 C CG1 . ILE A 3 ? 0.7063 0.9633 0.8258 0.2060 -0.0823 -0.0447 3 ILE A CG1 24 C CG2 . ILE A 3 ? 0.6990 0.9015 0.8120 0.1804 -0.0760 -0.0330 3 ILE A CG2 25 C CD1 . ILE A 3 ? 0.7038 1.0346 0.8451 0.1944 -0.0844 -0.0602 3 ILE A CD1 26 N N . CYS A 4 ? 0.7430 0.8508 0.8132 0.2229 -0.0748 -0.0167 4 CYS A N 27 C CA . CYS A 4 ? 0.7475 0.8126 0.8188 0.2078 -0.0680 -0.0092 4 CYS A CA 28 C C . CYS A 4 ? 0.6947 0.7947 0.7950 0.1930 -0.0663 -0.0160 4 CYS A C 29 O O . CYS A 4 ? 0.6790 0.8278 0.7886 0.2034 -0.0710 -0.0258 4 CYS A O 30 C CB . CYS A 4 ? 0.8108 0.8283 0.8467 0.2309 -0.0684 -0.0029 4 CYS A CB 31 S SG . CYS A 4 ? 0.9623 0.9256 0.9531 0.2485 -0.0689 0.0060 4 CYS A SG 32 N N . ILE A 5 ? 0.6434 0.7205 0.7566 0.1691 -0.0594 -0.0112 5 ILE A N 33 C CA . ILE A 5 ? 0.6141 0.7127 0.7491 0.1558 -0.0569 -0.0157 5 ILE A CA 34 C C . ILE A 5 ? 0.6213 0.6848 0.7441 0.1631 -0.0549 -0.0104 5 ILE A C 35 O O . ILE A 5 ? 0.6369 0.6527 0.7424 0.1616 -0.0513 -0.0017 5 ILE A O 36 C CB . ILE A 5 ? 0.5898 0.6872 0.7448 0.1259 -0.0507 -0.0146 5 ILE A CB 37 C CG1 . ILE A 5 ? 0.5996 0.7247 0.7618 0.1171 -0.0518 -0.0199 5 ILE A CG1 38 C CG2 . ILE A 5 ? 0.5774 0.6938 0.7509 0.1125 -0.0477 -0.0190 5 ILE A CG2 39 C CD1 . ILE A 5 ? 0.6109 0.7938 0.7861 0.1162 -0.0551 -0.0326 5 ILE A CD1 40 N N . GLY A 6 ? 0.6147 0.7033 0.7458 0.1692 -0.0565 -0.0163 6 GLY A N 41 C CA . GLY A 6 ? 0.6258 0.6831 0.7439 0.1773 -0.0548 -0.0124 6 GLY A CA 42 C C . GLY A 6 ? 0.6001 0.6902 0.7368 0.1741 -0.0549 -0.0193 6 GLY A C 43 O O . GLY A 6 ? 0.6176 0.7541 0.7775 0.1623 -0.0553 -0.0271 6 GLY A O 44 N N . TYR A 7 ? 0.6054 0.6696 0.7292 0.1833 -0.0538 -0.0167 7 TYR A N 45 C CA . TYR A 7 ? 0.6048 0.6938 0.7448 0.1793 -0.0530 -0.0221 7 TYR A CA 46 C C . TYR A 7 ? 0.6404 0.7181 0.7576 0.2070 -0.0563 -0.0237 7 TYR A C 47 O O . TYR A 7 ? 0.6663 0.7048 0.7508 0.2269 -0.0579 -0.0190 7 TYR A O 48 C CB . TYR A 7 ? 0.6047 0.6713 0.7585 0.1529 -0.0460 -0.0168 7 TYR A CB 49 C CG . TYR A 7 ? 0.6315 0.6408 0.7643 0.1508 -0.0420 -0.0074 7 TYR A CG 50 C CD1 . TYR A 7 ? 0.6268 0.6113 0.7537 0.1406 -0.0394 -0.0012 7 TYR A CD1 51 C CD2 . TYR A 7 ? 0.6738 0.6549 0.7909 0.1578 -0.0403 -0.0055 7 TYR A CD2 52 C CE1 . TYR A 7 ? 0.6757 0.6122 0.7821 0.1361 -0.0349 0.0060 7 TYR A CE1 53 C CE2 . TYR A 7 ? 0.6836 0.6136 0.7786 0.1523 -0.0356 0.0017 7 TYR A CE2 54 C CZ . TYR A 7 ? 0.6876 0.5972 0.7777 0.1407 -0.0328 0.0071 7 TYR A CZ 55 O OH . TYR A 7 ? 0.7282 0.5913 0.7956 0.1323 -0.0273 0.0129 7 TYR A OH 56 N N . HIS A 8 ? 0.6379 0.7474 0.7698 0.2075 -0.0568 -0.0304 8 HIS A N 57 C CA . HIS A 8 ? 0.6860 0.7971 0.7997 0.2352 -0.0605 -0.0344 8 HIS A CA 58 C C . HIS A 8 ? 0.7326 0.7811 0.8210 0.2379 -0.0564 -0.0266 8 HIS A C 59 O O . HIS A 8 ? 0.7180 0.7440 0.8172 0.2131 -0.0503 -0.0216 8 HIS A O 60 C CB . HIS A 8 ? 0.6627 0.8327 0.8044 0.2291 -0.0612 -0.0447 8 HIS A CB 61 C CG . HIS A 8 ? 0.6840 0.8667 0.8116 0.2575 -0.0651 -0.0506 8 HIS A CG 62 N ND1 . HIS A 8 ? 0.7201 0.9294 0.8303 0.2919 -0.0725 -0.0573 8 HIS A ND1 63 C CD2 . HIS A 8 ? 0.6779 0.8547 0.8066 0.2576 -0.0629 -0.0518 8 HIS A CD2 64 C CE1 . HIS A 8 ? 0.7183 0.9354 0.8178 0.3134 -0.0746 -0.0621 8 HIS A CE1 65 N NE2 . HIS A 8 ? 0.7001 0.8974 0.8112 0.2921 -0.0687 -0.0589 8 HIS A NE2 66 N N . ALA A 9 ? 0.7767 0.7973 0.8283 0.2689 -0.0595 -0.0263 9 ALA A N 67 C CA . ALA A 9 ? 0.7976 0.7633 0.8209 0.2737 -0.0556 -0.0217 9 ALA A CA 68 C C . ALA A 9 ? 0.8308 0.8108 0.8352 0.3082 -0.0608 -0.0288 9 ALA A C 69 O O . ALA A 9 ? 0.8485 0.8744 0.8551 0.3315 -0.0677 -0.0360 9 ALA A O 70 C CB . ALA A 9 ? 0.8305 0.7250 0.8135 0.2751 -0.0519 -0.0124 9 ALA A CB 71 N N . ASN A 10 ? 0.8541 0.7985 0.8399 0.3117 -0.0575 -0.0275 10 ASN A N 72 C CA . ASN A 10 ? 0.8823 0.8338 0.8453 0.3465 -0.0619 -0.0339 10 ASN A CA 73 C C . ASN A 10 ? 0.9570 0.8363 0.8793 0.3509 -0.0566 -0.0291 10 ASN A C 74 O O . ASN A 10 ? 0.9537 0.7789 0.8630 0.3275 -0.0497 -0.0211 10 ASN A O 75 C CB . ASN A 10 ? 0.8340 0.8641 0.8397 0.3432 -0.0650 -0.0445 10 ASN A CB 76 C CG . ASN A 10 ? 0.8048 0.8344 0.8376 0.3113 -0.0587 -0.0433 10 ASN A CG 77 O OD1 . ASN A 10 ? 0.8113 0.7867 0.8336 0.2917 -0.0524 -0.0351 10 ASN A OD1 78 N ND2 . ASN A 10 ? 0.7594 0.8518 0.8262 0.3054 -0.0601 -0.0521 10 ASN A ND2 79 N N . ASN A 11 ? 1.0684 0.9482 0.9690 0.3803 -0.0595 -0.0347 11 ASN A N 80 C CA . ASN A 11 ? 1.1867 0.9934 1.0410 0.3877 -0.0543 -0.0310 11 ASN A CA 81 C C . ASN A 11 ? 1.1207 0.9311 1.0005 0.3596 -0.0487 -0.0319 11 ASN A C 82 O O . ASN A 11 ? 1.1536 0.9135 0.9990 0.3655 -0.0446 -0.0311 11 ASN A O 83 C CB . ASN A 11 ? 1.3287 1.1243 1.1376 0.4379 -0.0601 -0.0363 11 ASN A CB 84 C CG . ASN A 11 ? 1.4358 1.3178 1.2798 0.4562 -0.0672 -0.0482 11 ASN A CG 85 O OD1 . ASN A 11 ? 1.4010 1.3429 1.2998 0.4283 -0.0665 -0.0522 11 ASN A OD1 86 N ND2 . ASN A 11 ? 1.6667 1.5553 1.4761 0.5040 -0.0738 -0.0543 11 ASN A ND2 87 N N . SER A 12 ? 1.0288 0.8958 0.9649 0.3297 -0.0481 -0.0337 12 SER A N 88 C CA . SER A 12 ? 0.9800 0.8597 0.9438 0.3047 -0.0436 -0.0350 12 SER A CA 89 C C . SER A 12 ? 0.9922 0.8065 0.9361 0.2795 -0.0352 -0.0275 12 SER A C 90 O O . SER A 12 ? 0.9635 0.7456 0.8976 0.2643 -0.0318 -0.0209 12 SER A O 91 C CB . SER A 12 ? 0.9206 0.8670 0.9420 0.2779 -0.0442 -0.0375 12 SER A CB 92 O OG . SER A 12 ? 0.8846 0.8418 0.9299 0.2555 -0.0400 -0.0385 12 SER A OG 93 N N . THR A 13 ? 1.0125 0.8110 0.9502 0.2751 -0.0316 -0.0295 13 THR A N 94 C CA . THR A 13 ? 1.0225 0.7698 0.9454 0.2483 -0.0233 -0.0247 13 THR A CA 95 C C . THR A 13 ? 0.9701 0.7566 0.9384 0.2201 -0.0208 -0.0263 13 THR A C 96 O O . THR A 13 ? 0.9619 0.7185 0.9244 0.1968 -0.0143 -0.0238 13 THR A O 97 C CB . THR A 13 ? 1.1058 0.7894 0.9728 0.2661 -0.0200 -0.0258 13 THR A CB 98 O OG1 . THR A 13 ? 1.1070 0.8228 0.9829 0.2858 -0.0238 -0.0330 13 THR A OG1 99 C CG2 . THR A 13 ? 1.1378 0.7695 0.9493 0.2950 -0.0214 -0.0233 13 THR A CG2 100 N N . GLU A 14 ? 0.9311 0.7842 0.9418 0.2216 -0.0255 -0.0310 14 GLU A N 101 C CA . GLU A 14 ? 0.9077 0.7990 0.9600 0.1961 -0.0233 -0.0321 14 GLU A CA 102 C C . GLU A 14 ? 0.8516 0.7316 0.9188 0.1650 -0.0185 -0.0256 14 GLU A C 103 O O . GLU A 14 ? 0.8321 0.7075 0.8990 0.1616 -0.0192 -0.0218 14 GLU A O 104 C CB . GLU A 14 ? 0.9281 0.8887 1.0182 0.1996 -0.0282 -0.0378 14 GLU A CB 105 C CG . GLU A 14 ? 0.9937 0.9842 1.0781 0.2283 -0.0330 -0.0464 14 GLU A CG 106 C CD . GLU A 14 ? 1.0740 1.0638 1.1586 0.2271 -0.0306 -0.0500 14 GLU A CD 107 O OE1 . GLU A 14 ? 1.0968 1.1022 1.2088 0.2010 -0.0270 -0.0488 14 GLU A OE1 108 O OE2 . GLU A 14 ? 1.1488 1.1209 1.2038 0.2537 -0.0324 -0.0539 14 GLU A OE2 109 N N . GLN A 15 ? 0.8278 0.7066 0.9075 0.1440 -0.0141 -0.0250 15 GLN A N 110 C CA . GLN A 15 ? 0.7940 0.6640 0.8848 0.1167 -0.0094 -0.0200 15 GLN A CA 111 C C . GLN A 15 ? 0.7280 0.6407 0.8576 0.1000 -0.0090 -0.0207 15 GLN A C 112 O O . GLN A 15 ? 0.7016 0.6347 0.8416 0.1032 -0.0096 -0.0248 15 GLN A O 113 C CB . GLN A 15 ? 0.8528 0.6747 0.9135 0.1062 -0.0033 -0.0191 15 GLN A CB 114 C CG . GLN A 15 ? 0.9432 0.7100 0.9577 0.1160 -0.0014 -0.0171 15 GLN A CG 115 C CD . GLN A 15 ? 1.0177 0.7346 0.9983 0.1006 0.0062 -0.0174 15 GLN A CD 116 O OE1 . GLN A 15 ? 1.0881 0.7560 1.0301 0.0980 0.0103 -0.0152 15 GLN A OE1 117 N NE2 . GLN A 15 ? 1.0259 0.7542 1.0183 0.0888 0.0087 -0.0206 15 GLN A NE2 118 N N . VAL A 16 ? 0.6945 0.6182 0.8420 0.0833 -0.0076 -0.0167 16 VAL A N 119 C CA . VAL A 16 ? 0.6490 0.6039 0.8257 0.0681 -0.0064 -0.0164 16 VAL A CA 120 C C . VAL A 16 ? 0.6572 0.5986 0.8337 0.0498 -0.0022 -0.0125 16 VAL A C 121 O O . VAL A 16 ? 0.6718 0.5889 0.8323 0.0468 -0.0006 -0.0099 16 VAL A O 122 C CB . VAL A 16 ? 0.6170 0.6054 0.8157 0.0680 -0.0091 -0.0164 16 VAL A CB 123 C CG1 . VAL A 16 ? 0.6246 0.6352 0.8242 0.0850 -0.0132 -0.0220 16 VAL A CG1 124 C CG2 . VAL A 16 ? 0.6126 0.5911 0.8084 0.0647 -0.0093 -0.0120 16 VAL A CG2 125 N N . ASP A 17 ? 0.6581 0.6170 0.8509 0.0382 -0.0002 -0.0126 17 ASP A N 126 C CA . ASP A 17 ? 0.6755 0.6329 0.8713 0.0226 0.0032 -0.0100 17 ASP A CA 127 C C . ASP A 17 ? 0.6502 0.6302 0.8651 0.0186 0.0023 -0.0067 17 ASP A C 128 O O . ASP A 17 ? 0.5949 0.5933 0.8226 0.0226 0.0004 -0.0071 17 ASP A O 129 C CB . ASP A 17 ? 0.7190 0.6808 0.9164 0.0141 0.0058 -0.0125 17 ASP A CB 130 C CG . ASP A 17 ? 0.7965 0.7281 0.9686 0.0136 0.0084 -0.0158 17 ASP A CG 131 O OD1 . ASP A 17 ? 0.7949 0.6967 0.9440 0.0129 0.0102 -0.0153 17 ASP A OD1 132 O OD2 . ASP A 17 ? 0.8605 0.7953 1.0325 0.0132 0.0092 -0.0191 17 ASP A OD2 133 N N . THR A 18 ? 0.6767 0.6541 0.8904 0.0100 0.0043 -0.0042 18 THR A N 134 C CA . THR A 18 ? 0.6565 0.6518 0.8837 0.0070 0.0041 -0.0012 18 THR A CA 135 C C . THR A 18 ? 0.6719 0.6761 0.9002 -0.0024 0.0070 -0.0013 18 THR A C 136 O O . THR A 18 ? 0.7252 0.7226 0.9445 -0.0096 0.0094 -0.0042 18 THR A O 137 C CB . THR A 18 ? 0.6611 0.6506 0.8862 0.0096 0.0030 0.0016 18 THR A CB 138 O OG1 . THR A 18 ? 0.6738 0.6487 0.8865 0.0036 0.0052 0.0021 18 THR A OG1 139 C CG2 . THR A 18 ? 0.6842 0.6688 0.9065 0.0196 -0.0001 0.0006 18 THR A CG2 140 N N . ILE A 19 ? 0.7071 0.7270 0.9438 -0.0020 0.0069 0.0011 19 ILE A N 141 C CA . ILE A 19 ? 0.6811 0.7180 0.9197 -0.0073 0.0089 0.0002 19 ILE A CA 142 C C . ILE A 19 ? 0.6953 0.7292 0.9256 -0.0168 0.0114 -0.0017 19 ILE A C 143 O O . ILE A 19 ? 0.6627 0.7076 0.8899 -0.0265 0.0141 -0.0056 19 ILE A O 144 C CB . ILE A 19 ? 0.7443 0.7939 0.9880 -0.0003 0.0080 0.0035 19 ILE A CB 145 C CG1 . ILE A 19 ? 0.8124 0.8617 1.0588 0.0056 0.0070 0.0049 19 ILE A CG1 146 C CG2 . ILE A 19 ? 0.7716 0.8439 1.0160 -0.0016 0.0093 0.0020 19 ILE A CG2 147 C CD1 . ILE A 19 ? 0.8121 0.8732 1.0604 0.0048 0.0077 0.0027 19 ILE A CD1 148 N N . MET A 20 ? 0.6952 0.7153 0.9204 -0.0155 0.0110 0.0006 20 MET A N 149 C CA . MET A 20 ? 0.7291 0.7442 0.9439 -0.0256 0.0141 -0.0007 20 MET A CA 150 C C . MET A 20 ? 0.7493 0.7332 0.9445 -0.0320 0.0163 -0.0025 20 MET A C 151 O O . MET A 20 ? 0.7452 0.7206 0.9263 -0.0445 0.0205 -0.0046 20 MET A O 152 C CB . MET A 20 ? 0.7580 0.7736 0.9749 -0.0206 0.0129 0.0028 20 MET A CB 153 C CG . MET A 20 ? 0.7884 0.8299 1.0163 -0.0148 0.0120 0.0041 20 MET A CG 154 S SD . MET A 20 ? 0.8455 0.8884 1.0711 -0.0130 0.0122 0.0064 20 MET A SD 155 C CE . MET A 20 ? 0.9716 1.0265 1.2042 0.0021 0.0097 0.0097 20 MET A CE 156 N N . GLU A 21 ? 0.7246 0.6904 0.9157 -0.0233 0.0141 -0.0020 21 GLU A N 157 C CA . GLU A 21 ? 0.7607 0.6914 0.9274 -0.0242 0.0158 -0.0031 21 GLU A CA 158 C C . GLU A 21 ? 0.7704 0.6915 0.9339 -0.0154 0.0141 -0.0050 21 GLU A C 159 O O . GLU A 21 ? 0.7672 0.7027 0.9461 -0.0037 0.0099 -0.0039 21 GLU A O 160 C CB . GLU A 21 ? 0.7873 0.7000 0.9452 -0.0158 0.0139 0.0003 21 GLU A CB 161 C CG . GLU A 21 ? 0.8778 0.7489 1.0021 -0.0186 0.0172 -0.0003 21 GLU A CG 162 C CD . GLU A 21 ? 0.9485 0.8026 1.0625 -0.0089 0.0151 0.0033 21 GLU A CD 163 O OE1 . GLU A 21 ? 0.9130 0.7902 1.0472 -0.0043 0.0119 0.0059 21 GLU A OE1 164 O OE2 . GLU A 21 ? 0.9604 0.7752 1.0426 -0.0052 0.0168 0.0035 21 GLU A OE2 165 N N . LYS A 22 ? 0.8102 0.7062 0.9510 -0.0224 0.0179 -0.0084 22 LYS A N 166 C CA . LYS A 22 ? 0.8421 0.7255 0.9752 -0.0133 0.0167 -0.0107 22 LYS A CA 167 C C . LYS A 22 ? 0.8062 0.6509 0.9111 -0.0001 0.0159 -0.0100 22 LYS A C 168 O O . LYS A 22 ? 0.7885 0.6075 0.8724 -0.0038 0.0183 -0.0083 22 LYS A O 169 C CB . LYS A 22 ? 0.9282 0.8073 1.0514 -0.0283 0.0216 -0.0155 22 LYS A CB 170 C CG . LYS A 22 ? 0.9821 0.9033 1.1329 -0.0358 0.0211 -0.0167 22 LYS A CG 171 C CD . LYS A 22 ? 1.1218 1.0418 1.2629 -0.0498 0.0255 -0.0225 22 LYS A CD 172 C CE . LYS A 22 ? 1.1502 1.1068 1.3164 -0.0475 0.0231 -0.0235 22 LYS A CE 173 N NZ . LYS A 22 ? 1.1697 1.1206 1.3250 -0.0564 0.0263 -0.0292 22 LYS A NZ 174 N N . ASN A 23 ? 0.7928 0.6350 0.8961 0.0168 0.0124 -0.0114 23 ASN A N 175 C CA . ASN A 23 ? 0.8633 0.6685 0.9349 0.0339 0.0113 -0.0117 23 ASN A CA 176 C C . ASN A 23 ? 0.8316 0.6309 0.8984 0.0440 0.0085 -0.0080 23 ASN A C 177 O O . ASN A 23 ? 0.8712 0.6293 0.9034 0.0472 0.0108 -0.0068 23 ASN A O 178 C CB . ASN A 23 ? 0.9277 0.6835 0.9578 0.0241 0.0181 -0.0140 23 ASN A CB 179 C CG . ASN A 23 ? 0.9956 0.7528 1.0250 0.0185 0.0203 -0.0186 23 ASN A CG 180 O OD1 . ASN A 23 ? 0.9517 0.7430 1.0084 0.0268 0.0162 -0.0198 23 ASN A OD1 181 N ND2 . ASN A 23 ? 1.1549 0.8743 1.1511 0.0028 0.0274 -0.0216 23 ASN A ND2 182 N N . VAL A 24 ? 0.7890 0.6274 0.8879 0.0482 0.0039 -0.0064 24 VAL A N 183 C CA . VAL A 24 ? 0.7485 0.5889 0.8473 0.0584 0.0005 -0.0037 24 VAL A CA 184 C C . VAL A 24 ? 0.7598 0.6020 0.8501 0.0836 -0.0048 -0.0062 24 VAL A C 185 O O . VAL A 24 ? 0.7508 0.6229 0.8599 0.0903 -0.0077 -0.0098 24 VAL A O 186 C CB . VAL A 24 ? 0.7023 0.5830 0.8362 0.0512 -0.0016 -0.0019 24 VAL A CB 187 C CG1 . VAL A 24 ? 0.7178 0.6009 0.8508 0.0605 -0.0050 0.0003 24 VAL A CG1 188 C CG2 . VAL A 24 ? 0.6887 0.5742 0.8315 0.0305 0.0029 -0.0002 24 VAL A CG2 189 N N . THR A 25 ? 0.7896 0.6010 0.8497 0.0983 -0.0059 -0.0050 25 THR A N 190 C CA . THR A 25 ? 0.7859 0.6016 0.8344 0.1264 -0.0115 -0.0082 25 THR A CA 191 C C . THR A 25 ? 0.7428 0.6049 0.8203 0.1329 -0.0171 -0.0092 25 THR A C 192 O O . THR A 25 ? 0.7392 0.6018 0.8212 0.1261 -0.0171 -0.0057 25 THR A O 193 C CB . THR A 25 ? 0.8297 0.5919 0.8292 0.1430 -0.0107 -0.0064 25 THR A CB 194 O OG1 . THR A 25 ? 0.8973 0.6114 0.8654 0.1320 -0.0039 -0.0060 25 THR A OG1 195 C CG2 . THR A 25 ? 0.8559 0.6254 0.8408 0.1767 -0.0170 -0.0106 25 THR A CG2 196 N N . VAL A 26 ? 0.7093 0.6109 0.8047 0.1448 -0.0213 -0.0147 26 VAL A N 197 C CA . VAL A 26 ? 0.6701 0.6199 0.7921 0.1476 -0.0257 -0.0177 26 VAL A CA 198 C C . VAL A 26 ? 0.6844 0.6560 0.7969 0.1761 -0.0318 -0.0240 26 VAL A C 199 O O . VAL A 26 ? 0.7465 0.7063 0.8399 0.1935 -0.0327 -0.0271 26 VAL A O 200 C CB . VAL A 26 ? 0.6256 0.6153 0.7831 0.1291 -0.0243 -0.0200 26 VAL A CB 201 C CG1 . VAL A 26 ? 0.6109 0.5874 0.7791 0.1047 -0.0195 -0.0141 26 VAL A CG1 202 C CG2 . VAL A 26 ? 0.6415 0.6396 0.8008 0.1331 -0.0237 -0.0244 26 VAL A CG2 203 N N . THR A 27 ? 0.6779 0.6842 0.8034 0.1808 -0.0358 -0.0265 27 THR A N 204 C CA . THR A 27 ? 0.6779 0.7171 0.7976 0.2080 -0.0422 -0.0339 27 THR A CA 205 C C . THR A 27 ? 0.6612 0.7486 0.8005 0.2112 -0.0436 -0.0427 27 THR A C 206 O O . THR A 27 ? 0.7233 0.8294 0.8502 0.2382 -0.0482 -0.0494 27 THR A O 207 C CB . THR A 27 ? 0.6702 0.7432 0.8037 0.2068 -0.0455 -0.0358 27 THR A CB 208 O OG1 . THR A 27 ? 0.6231 0.7317 0.7912 0.1792 -0.0428 -0.0376 27 THR A OG1 209 C CG2 . THR A 27 ? 0.6873 0.7152 0.8000 0.2061 -0.0445 -0.0275 27 THR A CG2 210 N N . HIS A 28 ? 0.6342 0.7425 0.8023 0.1846 -0.0396 -0.0432 28 HIS A N 211 C CA . HIS A 28 ? 0.6058 0.7586 0.7930 0.1819 -0.0396 -0.0513 28 HIS A CA 212 C C . HIS A 28 ? 0.6123 0.7528 0.8143 0.1561 -0.0336 -0.0474 28 HIS A C 213 O O . HIS A 28 ? 0.6061 0.7263 0.8148 0.1355 -0.0300 -0.0406 28 HIS A O 214 C CB . HIS A 28 ? 0.5725 0.7872 0.7827 0.1758 -0.0416 -0.0597 28 HIS A CB 215 C CG . HIS A 28 ? 0.5943 0.8309 0.7932 0.2005 -0.0479 -0.0646 28 HIS A CG 216 N ND1 . HIS A 28 ? 0.5907 0.8077 0.7812 0.2011 -0.0493 -0.0594 28 HIS A ND1 217 C CD2 . HIS A 28 ? 0.5935 0.8716 0.7867 0.2275 -0.0535 -0.0745 28 HIS A CD2 218 C CE1 . HIS A 28 ? 0.6043 0.8486 0.7841 0.2273 -0.0555 -0.0655 28 HIS A CE1 219 N NE2 . HIS A 28 ? 0.6024 0.8854 0.7835 0.2445 -0.0584 -0.0750 28 HIS A NE2 220 N N . ALA A 29 ? 0.6172 0.7724 0.8231 0.1590 -0.0329 -0.0522 29 ALA A N 221 C CA . ALA A 29 ? 0.6212 0.7681 0.8392 0.1378 -0.0278 -0.0495 29 ALA A CA 222 C C . ALA A 29 ? 0.6216 0.8116 0.8529 0.1387 -0.0277 -0.0583 29 ALA A C 223 O O . ALA A 29 ? 0.6621 0.8849 0.8904 0.1587 -0.0318 -0.0666 29 ALA A O 224 C CB . ALA A 29 ? 0.6619 0.7561 0.8596 0.1403 -0.0255 -0.0432 29 ALA A CB 225 N N . GLN A 30 ? 0.6361 0.8283 0.8810 0.1177 -0.0231 -0.0569 30 GLN A N 226 C CA . GLN A 30 ? 0.6467 0.8779 0.9039 0.1144 -0.0218 -0.0649 30 GLN A CA 227 C C . GLN A 30 ? 0.6417 0.8481 0.8981 0.1052 -0.0180 -0.0610 30 GLN A C 228 O O . GLN A 30 ? 0.6167 0.8066 0.8797 0.0848 -0.0139 -0.0549 30 GLN A O 229 C CB . GLN A 30 ? 0.6521 0.9232 0.9275 0.0929 -0.0191 -0.0695 30 GLN A CB 230 C CG . GLN A 30 ? 0.6802 0.9925 0.9669 0.0847 -0.0164 -0.0782 30 GLN A CG 231 C CD . GLN A 30 ? 0.6896 1.0466 0.9883 0.0650 -0.0135 -0.0859 30 GLN A CD 232 O OE1 . GLN A 30 ? 0.7030 1.0685 1.0021 0.0627 -0.0149 -0.0867 30 GLN A OE1 233 N NE2 . GLN A 30 ? 0.6949 1.0799 1.0012 0.0492 -0.0089 -0.0921 30 GLN A NE2 234 N N . ASP A 31 ? 0.6727 0.8765 0.9189 0.1223 -0.0195 -0.0647 31 ASP A N 235 C CA . ASP A 31 ? 0.6996 0.8873 0.9452 0.1151 -0.0162 -0.0631 31 ASP A CA 236 C C . ASP A 31 ? 0.6608 0.8878 0.9266 0.0969 -0.0128 -0.0676 31 ASP A C 237 O O . ASP A 31 ? 0.6489 0.9216 0.9236 0.0997 -0.0139 -0.0764 31 ASP A O 238 C CB . ASP A 31 ? 0.7487 0.9266 0.9756 0.1399 -0.0187 -0.0676 31 ASP A CB 239 C CG . ASP A 31 ? 0.7944 0.9492 1.0167 0.1332 -0.0153 -0.0658 31 ASP A CG 240 O OD1 . ASP A 31 ? 0.8173 0.9663 1.0518 0.1106 -0.0114 -0.0611 31 ASP A OD1 241 O OD2 . ASP A 31 ? 0.8511 0.9930 1.0552 0.1520 -0.0165 -0.0695 31 ASP A OD2 242 N N . ILE A 32 ? 0.6355 0.8456 0.9063 0.0781 -0.0084 -0.0623 32 ILE A N 243 C CA . ILE A 32 ? 0.6316 0.8697 0.9153 0.0598 -0.0042 -0.0656 32 ILE A CA 244 C C . ILE A 32 ? 0.6392 0.8700 0.9220 0.0571 -0.0017 -0.0655 32 ILE A C 245 O O . ILE A 32 ? 0.6511 0.8979 0.9409 0.0415 0.0024 -0.0671 32 ILE A O 246 C CB . ILE A 32 ? 0.5958 0.8247 0.8838 0.0379 -0.0004 -0.0598 32 ILE A CB 247 C CG1 . ILE A 32 ? 0.6089 0.7949 0.8906 0.0341 0.0005 -0.0497 32 ILE A CG1 248 C CG2 . ILE A 32 ? 0.5893 0.8323 0.8791 0.0382 -0.0023 -0.0617 32 ILE A CG2 249 C CD1 . ILE A 32 ? 0.6227 0.7980 0.9050 0.0162 0.0042 -0.0441 32 ILE A CD1 250 N N . LEU A 33 ? 0.6267 0.8319 0.8980 0.0717 -0.0038 -0.0642 33 LEU A N 251 C CA . LEU A 33 ? 0.6477 0.8433 0.9163 0.0698 -0.0017 -0.0644 33 LEU A CA 252 C C . LEU A 33 ? 0.6875 0.8959 0.9483 0.0903 -0.0040 -0.0725 33 LEU A C 253 O O . LEU A 33 ? 0.7339 0.9228 0.9782 0.1099 -0.0073 -0.0733 33 LEU A O 254 C CB . LEU A 33 ? 0.6461 0.7977 0.9041 0.0664 -0.0009 -0.0568 33 LEU A CB 255 C CG . LEU A 33 ? 0.6428 0.7829 0.8972 0.0622 0.0015 -0.0568 33 LEU A CG 256 C CD1 . LEU A 33 ? 0.6246 0.7814 0.8920 0.0447 0.0050 -0.0550 33 LEU A CD1 257 C CD2 . LEU A 33 ? 0.6741 0.7746 0.9146 0.0600 0.0022 -0.0519 33 LEU A CD2 258 N N . GLU A 34 ? 0.7002 0.9390 0.9697 0.0865 -0.0021 -0.0785 34 GLU A N 259 C CA . GLU A 34 ? 0.7228 0.9764 0.9849 0.1064 -0.0040 -0.0867 34 GLU A CA 260 C C . GLU A 34 ? 0.7308 0.9448 0.9782 0.1095 -0.0028 -0.0836 34 GLU A C 261 O O . GLU A 34 ? 0.7072 0.9132 0.9608 0.0920 0.0007 -0.0799 34 GLU A O 262 C CB . GLU A 34 ? 0.7287 1.0340 1.0061 0.0987 -0.0017 -0.0951 34 GLU A CB 263 C CG . GLU A 34 ? 0.7639 1.0920 1.0352 0.1204 -0.0037 -0.1048 34 GLU A CG 264 C CD . GLU A 34 ? 0.8199 1.1502 1.0767 0.1511 -0.0094 -0.1094 34 GLU A CD 265 O OE1 . GLU A 34 ? 0.8408 1.2024 1.1049 0.1543 -0.0117 -0.1130 34 GLU A OE1 266 O OE2 . GLU A 34 ? 0.8879 1.1860 1.1228 0.1723 -0.0114 -0.1095 34 GLU A OE2 267 N N . LYS A 35 ? 0.7518 0.9396 0.9767 0.1319 -0.0055 -0.0855 35 LYS A N 268 C CA . LYS A 35 ? 0.7765 0.9217 0.9817 0.1336 -0.0036 -0.0837 35 LYS A CA 269 C C . LYS A 35 ? 0.7806 0.9335 0.9732 0.1530 -0.0043 -0.0920 35 LYS A C 270 O O . LYS A 35 ? 0.7743 0.8954 0.9509 0.1522 -0.0020 -0.0918 35 LYS A O 271 C CB . LYS A 35 ? 0.8249 0.9181 1.0040 0.1406 -0.0042 -0.0787 35 LYS A CB 272 C CG . LYS A 35 ? 0.8243 0.9054 1.0126 0.1224 -0.0034 -0.0705 35 LYS A CG 273 C CD . LYS A 35 ? 0.8853 0.9169 1.0447 0.1301 -0.0036 -0.0669 35 LYS A CD 274 C CE . LYS A 35 ? 0.9147 0.9497 1.0821 0.1263 -0.0054 -0.0619 35 LYS A CE 275 N NZ . LYS A 35 ? 0.9045 0.9767 1.0809 0.1431 -0.0098 -0.0664 35 LYS A NZ 276 N N . THR A 36 ? 0.7738 0.9707 0.9728 0.1702 -0.0072 -0.1002 36 THR A N 277 C CA . THR A 36 ? 0.8432 1.0507 1.0284 0.1934 -0.0084 -0.1090 36 THR A CA 278 C C . THR A 36 ? 0.8349 1.0961 1.0440 0.1836 -0.0064 -0.1158 36 THR A C 279 O O . THR A 36 ? 0.7877 1.0885 1.0223 0.1643 -0.0049 -0.1160 36 THR A O 280 C CB . THR A 36 ? 0.8790 1.0995 1.0473 0.2276 -0.0137 -0.1155 36 THR A CB 281 O OG1 . THR A 36 ? 0.8814 1.1672 1.0763 0.2255 -0.0157 -0.1212 36 THR A OG1 282 C CG2 . THR A 36 ? 0.9099 1.0762 1.0519 0.2370 -0.0153 -0.1086 36 THR A CG2 283 N N . HIS A 37 ? 0.8464 1.1042 1.0430 0.1963 -0.0057 -0.1214 37 HIS A N 284 C CA . HIS A 37 ? 0.8131 1.1225 1.0267 0.1933 -0.0040 -0.1298 37 HIS A CA 285 C C . HIS A 37 ? 0.8504 1.1643 1.0418 0.2276 -0.0067 -0.1394 37 HIS A C 286 O O . HIS A 37 ? 0.8850 1.1525 1.0446 0.2508 -0.0091 -0.1381 37 HIS A O 287 C CB . HIS A 37 ? 0.7939 1.0903 1.0174 0.1662 0.0010 -0.1249 37 HIS A CB 288 C CG . HIS A 37 ? 0.8297 1.0675 1.0292 0.1687 0.0023 -0.1207 37 HIS A CG 289 N ND1 . HIS A 37 ? 0.8704 1.1004 1.0543 0.1819 0.0031 -0.1268 37 HIS A ND1 290 C CD2 . HIS A 37 ? 0.8603 1.0462 1.0475 0.1579 0.0034 -0.1121 37 HIS A CD2 291 C CE1 . HIS A 37 ? 0.8902 1.0639 1.0519 0.1778 0.0049 -0.1221 37 HIS A CE1 292 N NE2 . HIS A 37 ? 0.8896 1.0377 1.0534 0.1626 0.0053 -0.1135 37 HIS A NE2 293 N N . ASN A 38 ? 0.8499 1.2173 1.0542 0.2315 -0.0060 -0.1492 38 ASN A N 294 C CA . ASN A 38 ? 0.8694 1.2479 1.0525 0.2675 -0.0089 -0.1596 38 ASN A CA 295 C C . ASN A 38 ? 0.8955 1.2355 1.0599 0.2696 -0.0060 -0.1596 38 ASN A C 296 O O . ASN A 38 ? 0.9231 1.2551 1.0616 0.3009 -0.0080 -0.1668 38 ASN A O 297 C CB . ASN A 38 ? 0.8264 1.2914 1.0309 0.2757 -0.0103 -0.1728 38 ASN A CB 298 C CG . ASN A 38 ? 0.8025 1.3079 1.0336 0.2462 -0.0047 -0.1759 38 ASN A CG 299 O OD1 . ASN A 38 ? 0.8009 1.2703 1.0346 0.2219 -0.0005 -0.1677 38 ASN A OD1 300 N ND2 . ASN A 38 ? 0.7754 1.3580 1.0247 0.2477 -0.0045 -0.1882 38 ASN A ND2 301 N N . GLY A 39 ? 0.8764 1.1947 1.0527 0.2376 -0.0014 -0.1522 39 GLY A N 302 C CA . GLY A 39 ? 0.8936 1.1718 1.0523 0.2351 0.0017 -0.1514 39 GLY A CA 303 C C . GLY A 39 ? 0.9005 1.2235 1.0705 0.2366 0.0036 -0.1605 39 GLY A C 304 O O . GLY A 39 ? 0.8929 1.1879 1.0447 0.2419 0.0055 -0.1624 39 GLY A O 305 N N . LYS A 40 ? 0.8887 1.2812 1.0874 0.2296 0.0037 -0.1664 40 LYS A N 306 C CA . LYS A 40 ? 0.8589 1.3050 1.0693 0.2314 0.0057 -0.1768 40 LYS A CA 307 C C . LYS A 40 ? 0.8298 1.3158 1.0712 0.1949 0.0107 -0.1753 40 LYS A C 308 O O . LYS A 40 ? 0.8167 1.3064 1.0730 0.1735 0.0117 -0.1689 40 LYS A O 309 C CB . LYS A 40 ? 0.8712 1.3736 1.0807 0.2624 0.0015 -0.1896 40 LYS A CB 310 C CG . LYS A 40 ? 0.9367 1.4011 1.1085 0.3049 -0.0033 -0.1928 40 LYS A CG 311 C CD . LYS A 40 ? 0.9350 1.4570 1.1051 0.3388 -0.0085 -0.2047 40 LYS A CD 312 C CE . LYS A 40 ? 0.9928 1.4598 1.1199 0.3794 -0.0135 -0.2037 40 LYS A CE 313 N NZ . LYS A 40 ? 1.0416 1.5599 1.1561 0.4238 -0.0189 -0.2176 40 LYS A NZ 314 N N . LEU A 41 ? 0.8598 1.3727 1.1073 0.1886 0.0142 -0.1812 41 LEU A N 315 C CA . LEU A 41 ? 0.8586 1.4147 1.1299 0.1570 0.0197 -0.1822 41 LEU A CA 316 C C . LEU A 41 ? 0.8229 1.4572 1.1073 0.1647 0.0197 -0.1963 41 LEU A C 317 O O . LEU A 41 ? 0.8246 1.4876 1.1013 0.1928 0.0172 -0.2074 41 LEU A O 318 C CB . LEU A 41 ? 0.8764 1.4212 1.1458 0.1448 0.0240 -0.1814 41 LEU A CB 319 C CG . LEU A 41 ? 0.9047 1.3799 1.1612 0.1371 0.0240 -0.1695 41 LEU A CG 320 C CD1 . LEU A 41 ? 0.9259 1.3965 1.1791 0.1295 0.0276 -0.1710 41 LEU A CD1 321 C CD2 . LEU A 41 ? 0.8967 1.3497 1.1627 0.1107 0.0256 -0.1576 41 LEU A CD2 322 N N . CYS A 42 ? 0.8076 1.4769 1.1095 0.1396 0.0229 -0.1966 42 CYS A N 323 C CA . CYS A 42 ? 0.8311 1.5773 1.1454 0.1442 0.0227 -0.2106 42 CYS A CA 324 C C . CYS A 42 ? 0.7728 1.5660 1.1029 0.1066 0.0311 -0.2153 42 CYS A C 325 O O . CYS A 42 ? 0.7382 1.4969 1.0681 0.0769 0.0366 -0.2054 42 CYS A O 326 C CB . CYS A 42 ? 0.8736 1.6193 1.1894 0.1512 0.0183 -0.2084 42 CYS A CB 327 S SG . CYS A 42 ? 0.9396 1.6245 1.2311 0.1930 0.0093 -0.2021 42 CYS A SG 328 N N . ASP A 43 ? 0.7666 1.6391 1.1076 0.1082 0.0323 -0.2311 43 ASP A N 329 C CA . ASP A 43 ? 0.7496 1.6707 1.1023 0.0688 0.0413 -0.2375 43 ASP A CA 330 C C . ASP A 43 ? 0.7261 1.6199 1.0802 0.0421 0.0436 -0.2280 43 ASP A C 331 O O . ASP A 43 ? 0.6950 1.5734 1.0485 0.0588 0.0374 -0.2244 43 ASP A O 332 C CB . ASP A 43 ? 0.7488 1.7682 1.1130 0.0763 0.0418 -0.2584 43 ASP A CB 333 C CG . ASP A 43 ? 0.7554 1.8081 1.1172 0.1073 0.0390 -0.2694 43 ASP A CG 334 O OD1 . ASP A 43 ? 0.7749 1.7818 1.1278 0.1100 0.0399 -0.2621 43 ASP A OD1 335 O OD2 . ASP A 43 ? 0.7444 1.8716 1.1123 0.1301 0.0357 -0.2859 43 ASP A OD2 336 N N . LEU A 44 ? 0.7467 1.6308 1.0991 0.0016 0.0529 -0.2239 44 LEU A N 337 C CA . LEU A 44 ? 0.7770 1.6347 1.1265 -0.0262 0.0566 -0.2158 44 LEU A CA 338 C C . LEU A 44 ? 0.8192 1.7475 1.1748 -0.0540 0.0638 -0.2305 44 LEU A C 339 O O . LEU A 44 ? 0.8074 1.7556 1.1580 -0.0864 0.0739 -0.2356 44 LEU A O 340 C CB . LEU A 44 ? 0.7758 1.5660 1.1119 -0.0511 0.0625 -0.2006 44 LEU A CB 341 C CG . LEU A 44 ? 0.8030 1.5451 1.1304 -0.0720 0.0648 -0.1885 44 LEU A CG 342 C CD1 . LEU A 44 ? 0.8239 1.5249 1.1536 -0.0449 0.0551 -0.1788 44 LEU A CD1 343 C CD2 . LEU A 44 ? 0.8141 1.5020 1.1245 -0.0966 0.0719 -0.1765 44 LEU A CD2 344 N N . ASP A 45 ? 0.8475 1.8133 1.2117 -0.0422 0.0590 -0.2378 45 ASP A N 345 C CA . ASP A 45 ? 0.8752 1.9190 1.2468 -0.0654 0.0647 -0.2545 45 ASP A CA 346 C C . ASP A 45 ? 0.8406 1.9609 1.2191 -0.0686 0.0692 -0.2723 45 ASP A C 347 O O . ASP A 45 ? 0.8050 1.9598 1.1801 -0.1084 0.0804 -0.2809 45 ASP A O 348 C CB . ASP A 45 ? 0.9338 1.9491 1.2932 -0.1131 0.0752 -0.2490 45 ASP A CB 349 C CG . ASP A 45 ? 1.0298 1.9813 1.3838 -0.1090 0.0707 -0.2339 45 ASP A CG 350 O OD1 . ASP A 45 ? 1.0770 1.9546 1.4240 -0.0949 0.0665 -0.2171 45 ASP A OD1 351 O OD2 . ASP A 45 ? 1.0725 2.0502 1.4290 -0.1209 0.0715 -0.2395 45 ASP A OD2 352 N N . GLY A 46 ? 0.8177 1.9602 1.2025 -0.0265 0.0608 -0.2775 46 GLY A N 353 C CA . GLY A 46 ? 0.7918 2.0126 1.1843 -0.0204 0.0632 -0.2954 46 GLY A CA 354 C C . GLY A 46 ? 0.7776 1.9696 1.1628 -0.0297 0.0685 -0.2908 46 GLY A C 355 O O . GLY A 46 ? 0.7741 2.0127 1.1640 -0.0093 0.0669 -0.3022 46 GLY A O 356 N N . VAL A 47 ? 0.7487 1.8651 1.1212 -0.0580 0.0744 -0.2744 47 VAL A N 357 C CA . VAL A 47 ? 0.7247 1.8129 1.0879 -0.0730 0.0807 -0.2696 47 VAL A CA 358 C C . VAL A 47 ? 0.7319 1.7525 1.0899 -0.0402 0.0727 -0.2558 47 VAL A C 359 O O . VAL A 47 ? 0.7535 1.7000 1.1036 -0.0389 0.0697 -0.2391 47 VAL A O 360 C CB . VAL A 47 ? 0.7197 1.7624 1.0666 -0.1210 0.0921 -0.2598 47 VAL A CB 361 C CG1 . VAL A 47 ? 0.7409 1.7552 1.0757 -0.1349 0.0986 -0.2548 47 VAL A CG1 362 C CG2 . VAL A 47 ? 0.7141 1.8179 1.0608 -0.1582 0.1017 -0.2740 47 VAL A CG2 363 N N . LYS A 48 ? 0.7328 1.7810 1.0938 -0.0155 0.0699 -0.2639 48 LYS A N 364 C CA . LYS A 48 ? 0.7368 1.7286 1.0905 0.0160 0.0628 -0.2542 48 LYS A CA 365 C C . LYS A 48 ? 0.7273 1.6470 1.0692 -0.0061 0.0675 -0.2382 48 LYS A C 366 O O . LYS A 48 ? 0.7354 1.6637 1.0732 -0.0398 0.0770 -0.2389 48 LYS A O 367 C CB . LYS A 48 ? 0.7667 1.8118 1.1234 0.0423 0.0609 -0.2689 48 LYS A CB 368 C CG . LYS A 48 ? 0.8210 1.8159 1.1668 0.0774 0.0541 -0.2628 48 LYS A CG 369 C CD . LYS A 48 ? 0.8815 1.9263 1.2280 0.0912 0.0557 -0.2766 48 LYS A CD 370 C CE . LYS A 48 ? 0.9413 1.9313 1.2728 0.1218 0.0504 -0.2708 48 LYS A CE 371 N NZ . LYS A 48 ? 0.9920 1.9608 1.3126 0.1655 0.0406 -0.2710 48 LYS A NZ 372 N N . PRO A 49 ? 0.7107 1.5599 1.0448 0.0128 0.0611 -0.2244 49 PRO A N 373 C CA . PRO A 49 ? 0.6921 1.4805 1.0156 -0.0033 0.0643 -0.2107 49 PRO A CA 374 C C . PRO A 49 ? 0.6893 1.4864 1.0094 0.0036 0.0661 -0.2155 49 PRO A C 375 O O . PRO A 49 ? 0.6780 1.5165 1.0022 0.0285 0.0629 -0.2278 49 PRO A O 376 C CB . PRO A 49 ? 0.6809 1.4040 0.9985 0.0170 0.0564 -0.1978 49 PRO A CB 377 C CG . PRO A 49 ? 0.6923 1.4384 1.0125 0.0535 0.0487 -0.2066 49 PRO A CG 378 C CD . PRO A 49 ? 0.6976 1.5198 1.0297 0.0483 0.0511 -0.2209 49 PRO A CD 379 N N . LEU A 50 ? 0.6755 1.4330 0.9862 -0.0165 0.0708 -0.2057 50 LEU A N 380 C CA . LEU A 50 ? 0.6795 1.4315 0.9851 -0.0096 0.0717 -0.2073 50 LEU A CA 381 C C . LEU A 50 ? 0.6926 1.3876 0.9914 0.0153 0.0640 -0.1985 50 LEU A C 382 O O . LEU A 50 ? 0.7253 1.3666 1.0177 0.0065 0.0631 -0.1850 50 LEU A O 383 C CB . LEU A 50 ? 0.6903 1.4254 0.9858 -0.0423 0.0805 -0.2009 50 LEU A CB 384 C CG . LEU A 50 ? 0.7057 1.4288 0.9944 -0.0386 0.0818 -0.2005 50 LEU A CG 385 C CD1 . LEU A 50 ? 0.7103 1.4943 1.0064 -0.0247 0.0824 -0.2171 50 LEU A CD1 386 C CD2 . LEU A 50 ? 0.7283 1.4296 1.0029 -0.0706 0.0904 -0.1927 50 LEU A CD2 387 N N . ILE A 51 ? 0.7026 1.4095 1.0003 0.0462 0.0588 -0.2068 51 ILE A N 388 C CA . ILE A 51 ? 0.7271 1.3787 1.0132 0.0686 0.0525 -0.2004 51 ILE A CA 389 C C . ILE A 51 ? 0.7317 1.3722 1.0097 0.0704 0.0544 -0.2020 51 ILE A C 390 O O . ILE A 51 ? 0.7287 1.3993 1.0042 0.0892 0.0539 -0.2135 51 ILE A O 391 C CB . ILE A 51 ? 0.7428 1.4008 1.0242 0.1039 0.0457 -0.2076 51 ILE A CB 392 C CG1 . ILE A 51 ? 0.7467 1.4206 1.0374 0.1003 0.0440 -0.2064 51 ILE A CG1 393 C CG2 . ILE A 51 ? 0.7665 1.3596 1.0292 0.1234 0.0407 -0.2013 51 ILE A CG2 394 C CD1 . ILE A 51 ? 0.7962 1.4589 1.0780 0.1340 0.0366 -0.2091 51 ILE A CD1 395 N N . LEU A 52 ? 0.7310 1.3294 1.0038 0.0522 0.0564 -0.1907 52 LEU A N 396 C CA . LEU A 52 ? 0.7358 1.3252 1.0014 0.0490 0.0588 -0.1914 52 LEU A CA 397 C C . LEU A 52 ? 0.7594 1.3211 1.0119 0.0754 0.0541 -0.1951 52 LEU A C 398 O O . LEU A 52 ? 0.7595 1.3196 1.0053 0.0768 0.0559 -0.1985 52 LEU A O 399 C CB . LEU A 52 ? 0.7184 1.2721 0.9802 0.0247 0.0616 -0.1784 52 LEU A CB 400 C CG . LEU A 52 ? 0.7209 1.2922 0.9866 -0.0030 0.0680 -0.1744 52 LEU A CG 401 C CD1 . LEU A 52 ? 0.7252 1.2540 0.9815 -0.0202 0.0696 -0.1608 52 LEU A CD1 402 C CD2 . LEU A 52 ? 0.7360 1.3576 1.0039 -0.0133 0.0747 -0.1848 52 LEU A CD2 403 N N . ARG A 53 ? 0.7965 1.3334 1.0420 0.0955 0.0488 -0.1946 53 ARG A N 404 C CA . ARG A 53 ? 0.8853 1.3893 1.1107 0.1215 0.0451 -0.1989 53 ARG A CA 405 C C . ARG A 53 ? 0.9164 1.3742 1.1301 0.1104 0.0461 -0.1926 53 ARG A C 406 O O . ARG A 53 ? 0.9792 1.4013 1.1923 0.0966 0.0452 -0.1823 53 ARG A O 407 C CB . ARG A 53 ? 0.9458 1.4913 1.1670 0.1457 0.0451 -0.2135 53 ARG A CB 408 C CG . ARG A 53 ? 1.0462 1.5549 1.2399 0.1788 0.0411 -0.2188 53 ARG A CG 409 C CD . ARG A 53 ? 1.1153 1.6627 1.3014 0.2048 0.0412 -0.2334 53 ARG A CD 410 N NE . ARG A 53 ? 1.1621 1.7412 1.3452 0.2346 0.0373 -0.2419 53 ARG A NE 411 C CZ . ARG A 53 ? 1.1662 1.8155 1.3721 0.2324 0.0378 -0.2486 53 ARG A CZ 412 N NH1 . ARG A 53 ? 1.1669 1.8580 1.3979 0.1995 0.0430 -0.2474 53 ARG A NH1 413 N NH2 . ARG A 53 ? 1.2011 1.8786 1.4016 0.2632 0.0334 -0.2571 53 ARG A NH2 414 N N . ASP A 54 ? 0.9253 1.3873 1.1302 0.1159 0.0480 -0.1994 54 ASP A N 415 C CA . ASP A 54 ? 0.9347 1.3598 1.1287 0.1045 0.0492 -0.1951 54 ASP A CA 416 C C . ASP A 54 ? 0.8939 1.3397 1.1015 0.0789 0.0532 -0.1902 54 ASP A C 417 O O . ASP A 54 ? 0.9393 1.3618 1.1398 0.0688 0.0540 -0.1868 54 ASP A O 418 C CB . ASP A 54 ? 0.9922 1.4033 1.1644 0.1247 0.0492 -0.2051 54 ASP A CB 419 C CG . ASP A 54 ? 1.0511 1.4209 1.1981 0.1495 0.0459 -0.2083 54 ASP A CG 420 O OD1 . ASP A 54 ? 1.0514 1.3838 1.1931 0.1436 0.0440 -0.2006 54 ASP A OD1 421 O OD2 . ASP A 54 ? 1.0839 1.4572 1.2135 0.1756 0.0454 -0.2187 54 ASP A OD2 422 N N . CYS A 55 ? 0.8683 1.3566 1.0921 0.0679 0.0561 -0.1903 55 CYS A N 423 C CA . CYS A 55 ? 0.8828 1.3846 1.1129 0.0437 0.0609 -0.1852 55 CYS A CA 424 C C . CYS A 55 ? 0.8350 1.3155 1.0692 0.0253 0.0608 -0.1722 55 CYS A C 425 O O . CYS A 55 ? 0.8371 1.3112 1.0762 0.0278 0.0584 -0.1689 55 CYS A O 426 C CB . CYS A 55 ? 0.8927 1.4494 1.1319 0.0379 0.0660 -0.1933 55 CYS A CB 427 S SG . CYS A 55 ? 1.0185 1.6065 1.2523 0.0600 0.0665 -0.2092 55 CYS A SG 428 N N . SER A 56 ? 0.8077 1.2768 1.0381 0.0087 0.0633 -0.1650 56 SER A N 429 C CA . SER A 56 ? 0.7996 1.2519 1.0300 -0.0075 0.0642 -0.1531 56 SER A CA 430 C C . SER A 56 ? 0.7839 1.2625 1.0149 -0.0248 0.0708 -0.1525 56 SER A C 431 O O . SER A 56 ? 0.7786 1.2913 1.0115 -0.0262 0.0749 -0.1615 56 SER A O 432 C CB . SER A 56 ? 0.8138 1.2388 1.0352 -0.0132 0.0630 -0.1459 56 SER A CB 433 O OG . SER A 56 ? 0.8232 1.2624 1.0383 -0.0218 0.0674 -0.1472 56 SER A OG 434 N N . VAL A 57 ? 0.8015 1.2629 1.0278 -0.0388 0.0726 -0.1424 57 VAL A N 435 C CA . VAL A 57 ? 0.8218 1.2974 1.0407 -0.0590 0.0803 -0.1409 57 VAL A CA 436 C C . VAL A 57 ? 0.8213 1.3030 1.0281 -0.0678 0.0854 -0.1420 57 VAL A C 437 O O . VAL A 57 ? 0.8125 1.3217 1.0155 -0.0811 0.0925 -0.1478 57 VAL A O 438 C CB . VAL A 57 ? 0.8149 1.2595 1.0237 -0.0703 0.0813 -0.1288 57 VAL A CB 439 C CG1 . VAL A 57 ? 0.8275 1.2732 1.0181 -0.0931 0.0907 -0.1261 57 VAL A CG1 440 C CG2 . VAL A 57 ? 0.8068 1.2530 1.0279 -0.0646 0.0777 -0.1293 57 VAL A CG2 441 N N . ALA A 58 ? 0.8119 1.2704 1.0124 -0.0612 0.0820 -0.1371 58 ALA A N 442 C CA . ALA A 58 ? 0.8267 1.2889 1.0153 -0.0669 0.0857 -0.1378 58 ALA A CA 443 C C . ALA A 58 ? 0.8311 1.3292 1.0283 -0.0608 0.0872 -0.1512 58 ALA A C 444 O O . ALA A 58 ? 0.8336 1.3532 1.0238 -0.0725 0.0940 -0.1552 58 ALA A O 445 C CB . ALA A 58 ? 0.8182 1.2530 1.0001 -0.0594 0.0807 -0.1310 58 ALA A CB 446 N N . GLY A 59 ? 0.8187 1.3211 1.0277 -0.0422 0.0814 -0.1581 59 GLY A N 447 C CA . GLY A 59 ? 0.8166 1.3507 1.0313 -0.0312 0.0821 -0.1713 59 GLY A CA 448 C C . GLY A 59 ? 0.8463 1.4244 1.0677 -0.0384 0.0876 -0.1796 59 GLY A C 449 O O . GLY A 59 ? 0.9048 1.5164 1.1258 -0.0408 0.0921 -0.1886 59 GLY A O 450 N N . TRP A 60 ? 0.8104 1.3913 1.0378 -0.0429 0.0875 -0.1772 60 TRP A N 451 C CA . TRP A 60 ? 0.7804 1.4069 1.0143 -0.0526 0.0929 -0.1859 60 TRP A CA 452 C C . TRP A 60 ? 0.8011 1.4376 1.0220 -0.0807 0.1028 -0.1842 60 TRP A C 453 O O . TRP A 60 ? 0.8156 1.4962 1.0380 -0.0880 0.1087 -0.1951 60 TRP A O 454 C CB . TRP A 60 ? 0.7784 1.4019 1.0199 -0.0526 0.0905 -0.1830 60 TRP A CB 455 C CG . TRP A 60 ? 0.7631 1.4272 1.0071 -0.0722 0.0977 -0.1893 60 TRP A CG 456 C CD1 . TRP A 60 ? 0.7743 1.4959 1.0238 -0.0768 0.1029 -0.2034 60 TRP A CD1 457 C CD2 . TRP A 60 ? 0.7481 1.4001 0.9877 -0.0910 0.1009 -0.1829 60 TRP A CD2 458 N NE1 . TRP A 60 ? 0.7923 1.5405 1.0413 -0.0998 0.1096 -0.2067 60 TRP A NE1 459 C CE2 . TRP A 60 ? 0.7799 1.4834 1.0217 -0.1090 0.1086 -0.1940 60 TRP A CE2 460 C CE3 . TRP A 60 ? 0.7635 1.3677 0.9963 -0.0946 0.0983 -0.1694 60 TRP A CE3 461 C CZ2 . TRP A 60 ? 0.7939 1.4985 1.0295 -0.1324 0.1142 -0.1922 60 TRP A CZ2 462 C CZ3 . TRP A 60 ? 0.7646 1.3681 0.9913 -0.1151 0.1035 -0.1669 60 TRP A CZ3 463 C CH2 . TRP A 60 ? 0.7782 1.4297 1.0055 -0.1345 0.1115 -0.1782 60 TRP A CH2 464 N N . LEU A 61 ? 0.8098 1.4043 1.0148 -0.0956 0.1050 -0.1708 61 LEU A N 465 C CA . LEU A 61 ? 0.8310 1.4234 1.0153 -0.1234 0.1153 -0.1677 61 LEU A CA 466 C C . LEU A 61 ? 0.8406 1.4399 1.0139 -0.1276 0.1195 -0.1702 61 LEU A C 467 O O . LEU A 61 ? 0.8375 1.4660 1.0025 -0.1465 0.1286 -0.1773 61 LEU A O 468 C CB . LEU A 61 ? 0.8319 1.3720 0.9964 -0.1340 0.1163 -0.1523 61 LEU A CB 469 C CG . LEU A 61 ? 0.8343 1.3716 1.0040 -0.1392 0.1158 -0.1506 61 LEU A CG 470 C CD1 . LEU A 61 ? 0.8804 1.3623 1.0304 -0.1433 0.1151 -0.1351 61 LEU A CD1 471 C CD2 . LEU A 61 ? 0.8405 1.4153 1.0064 -0.1634 0.1257 -0.1601 61 LEU A CD2 472 N N . LEU A 62 ? 0.8395 1.4139 1.0120 -0.1116 0.1133 -0.1654 62 LEU A N 473 C CA . LEU A 62 ? 0.8522 1.4344 1.0160 -0.1125 0.1161 -0.1685 62 LEU A CA 474 C C . LEU A 62 ? 0.8518 1.4856 1.0311 -0.1040 0.1170 -0.1846 62 LEU A C 475 O O . LEU A 62 ? 0.8837 1.5361 1.0552 -0.1117 0.1225 -0.1897 62 LEU A O 476 C CB . LEU A 62 ? 0.8382 1.3857 0.9986 -0.0971 0.1087 -0.1609 62 LEU A CB 477 C CG . LEU A 62 ? 0.8504 1.3524 0.9903 -0.1041 0.1086 -0.1457 62 LEU A CG 478 C CD1 . LEU A 62 ? 0.8500 1.3284 0.9925 -0.0871 0.0999 -0.1407 62 LEU A CD1 479 C CD2 . LEU A 62 ? 0.8779 1.3713 0.9897 -0.1230 0.1179 -0.1414 62 LEU A CD2 480 N N . GLY A 63 ? 0.8283 1.4847 1.0272 -0.0866 0.1116 -0.1927 63 GLY A N 481 C CA . GLY A 63 ? 0.8199 1.5255 1.0314 -0.0728 0.1115 -0.2086 63 GLY A CA 482 C C . GLY A 63 ? 0.8156 1.5079 1.0287 -0.0482 0.1048 -0.2117 63 GLY A C 483 O O . GLY A 63 ? 0.8147 1.5324 1.0264 -0.0439 0.1072 -0.2207 63 GLY A O 484 N N . ASN A 64 ? 0.8133 1.4651 1.0273 -0.0335 0.0969 -0.2048 64 ASN A N 485 C CA . ASN A 64 ? 0.8215 1.4557 1.0335 -0.0112 0.0909 -0.2089 64 ASN A CA 486 C C . ASN A 64 ? 0.8446 1.5184 1.0626 0.0095 0.0903 -0.2244 64 ASN A C 487 O O . ASN A 64 ? 0.8652 1.5608 1.0921 0.0181 0.0889 -0.2291 64 ASN A O 488 C CB . ASN A 64 ? 0.8150 1.4047 1.0267 -0.0015 0.0838 -0.2008 64 ASN A CB 489 C CG . ASN A 64 ? 0.8113 1.3753 1.0152 0.0178 0.0787 -0.2051 64 ASN A CG 490 O OD1 . ASN A 64 ? 0.8056 1.3867 1.0068 0.0346 0.0785 -0.2166 64 ASN A OD1 491 N ND2 . ASN A 64 ? 0.8154 1.3378 1.0133 0.0154 0.0749 -0.1966 64 ASN A ND2 492 N N . PRO A 65 ? 0.8852 1.5699 1.0970 0.0193 0.0912 -0.2328 65 PRO A N 493 C CA . PRO A 65 ? 0.9164 1.6426 1.1310 0.0414 0.0911 -0.2486 65 PRO A CA 494 C C . PRO A 65 ? 0.9502 1.6663 1.1643 0.0699 0.0845 -0.2531 65 PRO A C 495 O O . PRO A 65 ? 0.9676 1.7266 1.1858 0.0883 0.0842 -0.2654 65 PRO A O 496 C CB . PRO A 65 ? 0.9251 1.6423 1.1280 0.0493 0.0915 -0.2536 65 PRO A CB 497 C CG . PRO A 65 ? 0.9085 1.6015 1.1065 0.0241 0.0945 -0.2422 65 PRO A CG 498 C CD . PRO A 65 ? 0.8907 1.5506 1.0914 0.0120 0.0921 -0.2286 65 PRO A CD 499 N N . MET A 66 ? 0.9890 1.6502 1.1961 0.0738 0.0793 -0.2437 66 MET A N 500 C CA . MET A 66 ? 1.0271 1.6683 1.2292 0.0980 0.0735 -0.2457 66 MET A CA 501 C C . MET A 66 ? 0.9908 1.6556 1.2076 0.0941 0.0728 -0.2434 66 MET A C 502 O O . MET A 66 ? 0.9763 1.6303 1.1894 0.1149 0.0681 -0.2454 66 MET A O 503 C CB . MET A 66 ? 1.0616 1.6363 1.2500 0.0979 0.0695 -0.2364 66 MET A CB 504 C CG . MET A 66 ? 1.1116 1.6571 1.2818 0.1028 0.0697 -0.2398 66 MET A CG 505 S SD . MET A 66 ? 1.1950 1.7287 1.3409 0.1409 0.0673 -0.2540 66 MET A SD 506 C CE . MET A 66 ? 1.2346 1.7045 1.3546 0.1356 0.0671 -0.2520 66 MET A CE 507 N N . CYS A 67 ? 0.9580 1.6516 1.1879 0.0672 0.0779 -0.2394 67 CYS A N 508 C CA . CYS A 67 ? 0.9506 1.6614 1.1925 0.0574 0.0783 -0.2362 67 CYS A CA 509 C C . CYS A 67 ? 0.9332 1.7150 1.1867 0.0497 0.0838 -0.2477 67 CYS A C 510 O O . CYS A 67 ? 0.9210 1.7208 1.1821 0.0257 0.0882 -0.2444 67 CYS A O 511 C CB . CYS A 67 ? 0.9410 1.6161 1.1828 0.0297 0.0802 -0.2208 67 CYS A CB 512 S SG . CYS A 67 ? 0.9784 1.5810 1.2092 0.0371 0.0736 -0.2089 67 CYS A SG 513 N N . ASP A 68 ? 0.9406 1.7631 1.1935 0.0698 0.0840 -0.2620 68 ASP A N 514 C CA . ASP A 68 ? 0.9277 1.8273 1.1918 0.0632 0.0895 -0.2757 68 ASP A CA 515 C C . ASP A 68 ? 0.9178 1.8560 1.1934 0.0709 0.0873 -0.2817 68 ASP A C 516 O O . ASP A 68 ? 0.9131 1.9132 1.1995 0.0537 0.0931 -0.2905 68 ASP A O 517 C CB . ASP A 68 ? 0.9428 1.8783 1.2025 0.0867 0.0896 -0.2903 68 ASP A CB 518 C CG . ASP A 68 ? 0.9646 1.8825 1.2161 0.0717 0.0942 -0.2873 68 ASP A CG 519 O OD1 . ASP A 68 ? 0.9741 1.8518 1.2222 0.0449 0.0969 -0.2737 68 ASP A OD1 520 O OD2 . ASP A 68 ? 0.9860 1.9309 1.2330 0.0882 0.0949 -0.2987 68 ASP A OD2 521 N N . GLU A 69 ? 0.9269 1.8295 1.1985 0.0951 0.0794 -0.2774 69 GLU A N 522 C CA . GLU A 69 ? 0.9159 1.8476 1.1973 0.1020 0.0766 -0.2809 69 GLU A CA 523 C C . GLU A 69 ? 0.8750 1.8209 1.1672 0.0619 0.0831 -0.2750 69 GLU A C 524 O O . GLU A 69 ? 0.8577 1.8602 1.1613 0.0557 0.0852 -0.2839 69 GLU A O 525 C CB . GLU A 69 ? 0.9360 1.8083 1.2076 0.1263 0.0681 -0.2724 69 GLU A CB 526 C CG . GLU A 69 ? 0.9455 1.8477 1.2247 0.1405 0.0640 -0.2771 69 GLU A CG 527 C CD . GLU A 69 ? 0.9525 1.7893 1.2203 0.1577 0.0569 -0.2665 69 GLU A CD 528 O OE1 . GLU A 69 ? 0.9625 1.7330 1.2151 0.1611 0.0550 -0.2573 69 GLU A OE1 529 O OE2 . GLU A 69 ? 0.9409 1.7947 1.2143 0.1665 0.0536 -0.2680 69 GLU A OE2 530 N N . PHE A 70 ? 0.8575 1.7521 1.1434 0.0352 0.0865 -0.2606 70 PHE A N 531 C CA . PHE A 70 ? 0.8471 1.7364 1.1347 -0.0013 0.0927 -0.2525 70 PHE A CA 532 C C . PHE A 70 ? 0.8706 1.7823 1.1530 -0.0340 0.1034 -0.2546 70 PHE A C 533 O O . PHE A 70 ? 0.8966 1.7758 1.1693 -0.0635 0.1089 -0.2435 70 PHE A O 534 C CB . PHE A 70 ? 0.8244 1.6372 1.1042 -0.0059 0.0890 -0.2342 70 PHE A CB 535 C CG . PHE A 70 ? 0.8098 1.5908 1.0898 0.0252 0.0792 -0.2315 70 PHE A CG 536 C CD1 . PHE A 70 ? 0.7839 1.5845 1.0719 0.0358 0.0756 -0.2350 70 PHE A CD1 537 C CD2 . PHE A 70 ? 0.8004 1.5324 1.0699 0.0429 0.0743 -0.2263 70 PHE A CD2 538 C CE1 . PHE A 70 ? 0.7909 1.5583 1.0747 0.0643 0.0673 -0.2323 70 PHE A CE1 539 C CE2 . PHE A 70 ? 0.8019 1.5002 1.0661 0.0687 0.0667 -0.2243 70 PHE A CE2 540 C CZ . PHE A 70 ? 0.7922 1.5064 1.0627 0.0801 0.0632 -0.2269 70 PHE A CZ 541 N N . ILE A 71 ? 0.8829 1.8487 1.1685 -0.0281 0.1065 -0.2689 71 ILE A N 542 C CA . ILE A 71 ? 0.9067 1.8973 1.1855 -0.0592 0.1173 -0.2724 71 ILE A CA 543 C C . ILE A 71 ? 0.9086 1.9392 1.1883 -0.0942 0.1266 -0.2773 71 ILE A C 544 O O . ILE A 71 ? 0.9165 1.9354 1.1815 -0.1291 0.1365 -0.2729 71 ILE A O 545 C CB . ILE A 71 ? 0.9384 1.9804 1.2207 -0.0427 0.1183 -0.2877 71 ILE A CB 546 C CG1 . ILE A 71 ? 0.9494 1.9926 1.2196 -0.0724 0.1284 -0.2866 71 ILE A CG1 547 C CG2 . ILE A 71 ? 0.9081 2.0368 1.2053 -0.0310 0.1186 -0.3073 71 ILE A CG2 548 C CD1 . ILE A 71 ? 0.9410 1.9821 1.2076 -0.0516 0.1260 -0.2907 71 ILE A CD1 549 N N . ASN A 72 ? 0.9064 1.9819 1.2001 -0.0849 0.1237 -0.2868 72 ASN A N 550 C CA . ASN A 72 ? 0.9179 2.0287 1.2120 -0.1187 0.1320 -0.2917 72 ASN A CA 551 C C . ASN A 72 ? 0.8852 2.0006 1.1912 -0.1030 0.1246 -0.2917 72 ASN A C 552 O O . ASN A 72 ? 0.9037 2.0841 1.2250 -0.0821 0.1206 -0.3067 72 ASN A O 553 C CB . ASN A 72 ? 0.9508 2.1532 1.2509 -0.1343 0.1407 -0.3125 72 ASN A CB 554 C CG . ASN A 72 ? 0.9943 2.1885 1.2762 -0.1688 0.1527 -0.3111 72 ASN A CG 555 O OD1 . ASN A 72 ? 1.0335 2.1698 1.2946 -0.1994 0.1594 -0.2974 72 ASN A OD1 556 N ND2 . ASN A 72 ? 1.0093 2.2601 1.2964 -0.1627 0.1556 -0.3253 72 ASN A ND2 557 N N . VAL A 73 ? 0.8656 1.9124 1.1632 -0.1115 0.1226 -0.2748 73 VAL A N 558 C CA . VAL A 73 ? 0.8177 1.8557 1.1248 -0.0952 0.1148 -0.2719 73 VAL A CA 559 C C . VAL A 73 ? 0.7894 1.8586 1.0961 -0.1285 0.1224 -0.2767 73 VAL A C 560 O O . VAL A 73 ? 0.7993 1.8461 1.0886 -0.1672 0.1329 -0.2713 73 VAL A O 561 C CB . VAL A 73 ? 0.8029 1.7517 1.1019 -0.0841 0.1078 -0.2517 73 VAL A CB 562 C CG1 . VAL A 73 ? 0.8020 1.7183 1.0983 -0.0565 0.1015 -0.2477 73 VAL A CG1 563 C CG2 . VAL A 73 ? 0.8080 1.7040 1.0887 -0.1200 0.1154 -0.2376 73 VAL A CG2 564 N N . PRO A 74 ? 0.7606 1.8785 1.0827 -0.1134 0.1175 -0.2869 74 PRO A N 565 C CA . PRO A 74 ? 0.7668 1.9151 1.0885 -0.1456 0.1245 -0.2923 74 PRO A CA 566 C C . PRO A 74 ? 0.7591 1.8291 1.0679 -0.1606 0.1243 -0.2738 74 PRO A C 567 O O . PRO A 74 ? 0.7371 1.7339 1.0391 -0.1455 0.1185 -0.2572 74 PRO A O 568 C CB . PRO A 74 ? 0.7556 1.9760 1.0983 -0.1162 0.1167 -0.3077 74 PRO A CB 569 C CG . PRO A 74 ? 0.7432 1.9295 1.0907 -0.0662 0.1036 -0.3016 74 PRO A CG 570 C CD . PRO A 74 ? 0.7494 1.8931 1.0863 -0.0655 0.1055 -0.2940 74 PRO A CD 571 N N . GLU A 75 ? 0.7696 1.8584 1.0742 -0.1910 0.1311 -0.2778 75 GLU A N 572 C CA . GLU A 75 ? 0.7835 1.8060 1.0753 -0.2049 0.1312 -0.2625 75 GLU A CA 573 C C . GLU A 75 ? 0.7563 1.7452 1.0617 -0.1642 0.1169 -0.2532 75 GLU A C 574 O O . GLU A 75 ? 0.7300 1.7667 1.0544 -0.1335 0.1087 -0.2634 75 GLU A O 575 C CB . GLU A 75 ? 0.8089 1.8732 1.0968 -0.2398 0.1400 -0.2730 75 GLU A CB 576 C CG . GLU A 75 ? 0.8385 1.8359 1.1082 -0.2596 0.1425 -0.2587 75 GLU A CG 577 C CD . GLU A 75 ? 0.8655 1.9071 1.1295 -0.2958 0.1518 -0.2710 75 GLU A CD 578 O OE1 . GLU A 75 ? 0.9081 2.0330 1.1799 -0.3121 0.1582 -0.2908 75 GLU A OE1 579 O OE2 . GLU A 75 ? 0.8677 1.8631 1.1190 -0.3087 0.1529 -0.2617 75 GLU A OE2 580 N N . TRP A 76 ? 0.7626 1.6694 1.0557 -0.1633 0.1142 -0.2342 76 TRP A N 581 C CA . TRP A 76 ? 0.7542 1.6235 1.0568 -0.1292 0.1019 -0.2247 76 TRP A CA 582 C C . TRP A 76 ? 0.7712 1.5995 1.0662 -0.1436 0.1024 -0.2143 76 TRP A C 583 O O . TRP A 76 ? 0.8460 1.6563 1.1229 -0.1787 0.1121 -0.2110 76 TRP A O 584 C CB . TRP A 76 ? 0.7226 1.5351 1.0204 -0.1081 0.0962 -0.2125 76 TRP A CB 585 C CG . TRP A 76 ? 0.7380 1.4893 1.0146 -0.1314 0.1023 -0.1981 76 TRP A CG 586 C CD1 . TRP A 76 ? 0.7560 1.4447 1.0212 -0.1361 0.1008 -0.1827 76 TRP A CD1 587 C CD2 . TRP A 76 ? 0.7391 1.4863 1.0007 -0.1512 0.1106 -0.1980 76 TRP A CD2 588 N NE1 . TRP A 76 ? 0.7666 1.4127 1.0094 -0.1553 0.1073 -0.1731 76 TRP A NE1 589 C CE2 . TRP A 76 ? 0.7533 1.4323 0.9927 -0.1654 0.1136 -0.1819 76 TRP A CE2 590 C CE3 . TRP A 76 ? 0.7496 1.5449 1.0129 -0.1573 0.1160 -0.2102 76 TRP A CE3 591 C CZ2 . TRP A 76 ? 0.7855 1.4404 1.0026 -0.1842 0.1215 -0.1771 76 TRP A CZ2 592 C CZ3 . TRP A 76 ? 0.7595 1.5309 1.0023 -0.1788 0.1243 -0.2055 76 TRP A CZ3 593 C CH2 . TRP A 76 ? 0.7827 1.4831 1.0016 -0.1916 0.1269 -0.1889 76 TRP A CH2 594 N N . SER A 77 ? 0.7653 1.5766 1.0709 -0.1161 0.0922 -0.2095 77 SER A N 595 C CA . SER A 77 ? 0.7470 1.5181 1.0472 -0.1242 0.0910 -0.1993 77 SER A CA 596 C C . SER A 77 ? 0.7493 1.4412 1.0381 -0.1171 0.0875 -0.1808 77 SER A C 597 O O . SER A 77 ? 0.7743 1.4212 1.0465 -0.1376 0.0921 -0.1702 77 SER A O 598 C CB . SER A 77 ? 0.7272 1.5266 1.0443 -0.0979 0.0819 -0.2050 77 SER A CB 599 O OG . SER A 77 ? 0.7198 1.5252 1.0462 -0.0598 0.0729 -0.2075 77 SER A OG 600 N N . TYR A 78 ? 0.7286 1.4048 1.0243 -0.0875 0.0796 -0.1779 78 TYR A N 601 C CA . TYR A 78 ? 0.7129 1.3245 0.9990 -0.0808 0.0765 -0.1630 78 TYR A CA 602 C C . TYR A 78 ? 0.7036 1.3186 0.9922 -0.0624 0.0736 -0.1661 78 TYR A C 603 O O . TYR A 78 ? 0.7226 1.3861 1.0200 -0.0512 0.0731 -0.1789 78 TYR A O 604 C CB . TYR A 78 ? 0.6954 1.2695 0.9850 -0.0636 0.0685 -0.1539 78 TYR A CB 605 C CG . TYR A 78 ? 0.6663 1.2635 0.9690 -0.0333 0.0602 -0.1613 78 TYR A CG 606 C CD1 . TYR A 78 ? 0.6467 1.2919 0.9591 -0.0302 0.0595 -0.1718 78 TYR A CD1 607 C CD2 . TYR A 78 ? 0.6503 1.2194 0.9518 -0.0077 0.0535 -0.1582 78 TYR A CD2 608 C CE1 . TYR A 78 ? 0.6329 1.2963 0.9524 0.0012 0.0516 -0.1782 78 TYR A CE1 609 C CE2 . TYR A 78 ? 0.6372 1.2185 0.9427 0.0213 0.0466 -0.1645 78 TYR A CE2 610 C CZ . TYR A 78 ? 0.6340 1.2616 0.9480 0.0275 0.0454 -0.1740 78 TYR A CZ 611 O OH . TYR A 78 ? 0.6287 1.2650 0.9419 0.0600 0.0383 -0.1798 78 TYR A OH 612 N N . ILE A 79 ? 0.6991 1.2647 0.9788 -0.0590 0.0717 -0.1549 79 ILE A N 613 C CA . ILE A 79 ? 0.7108 1.2729 0.9901 -0.0443 0.0694 -0.1569 79 ILE A CA 614 C C . ILE A 79 ? 0.7208 1.2440 1.0008 -0.0207 0.0609 -0.1508 79 ILE A C 615 O O . ILE A 79 ? 0.6929 1.1782 0.9695 -0.0232 0.0586 -0.1403 79 ILE A O 616 C CB . ILE A 79 ? 0.7320 1.2728 0.9972 -0.0632 0.0755 -0.1505 79 ILE A CB 617 C CG1 . ILE A 79 ? 0.7519 1.3308 1.0119 -0.0877 0.0852 -0.1583 79 ILE A CG1 618 C CG2 . ILE A 79 ? 0.7533 1.2833 1.0173 -0.0480 0.0723 -0.1510 79 ILE A CG2 619 C CD1 . ILE A 79 ? 0.7796 1.3306 1.0189 -0.1090 0.0925 -0.1507 79 ILE A CD1 620 N N . VAL A 80 ? 0.7246 1.2564 1.0062 0.0015 0.0569 -0.1579 80 VAL A N 621 C CA . VAL A 80 ? 0.7374 1.2291 1.0139 0.0213 0.0504 -0.1536 80 VAL A CA 622 C C . VAL A 80 ? 0.7509 1.2271 1.0193 0.0259 0.0506 -0.1543 80 VAL A C 623 O O . VAL A 80 ? 0.7874 1.2922 1.0559 0.0335 0.0520 -0.1639 80 VAL A O 624 C CB . VAL A 80 ? 0.7416 1.2458 1.0194 0.0475 0.0451 -0.1614 80 VAL A CB 625 C CG1 . VAL A 80 ? 0.7526 1.2073 1.0179 0.0649 0.0398 -0.1570 80 VAL A CG1 626 C CG2 . VAL A 80 ? 0.7239 1.2460 1.0102 0.0431 0.0445 -0.1611 80 VAL A CG2 627 N N . GLU A 81 ? 0.7692 1.2029 1.0307 0.0213 0.0490 -0.1448 81 GLU A N 628 C CA . GLU A 81 ? 0.8020 1.2190 1.0551 0.0224 0.0492 -0.1448 81 GLU A CA 629 C C . GLU A 81 ? 0.7985 1.1744 1.0428 0.0329 0.0445 -0.1415 81 GLU A C 630 O O . GLU A 81 ? 0.8094 1.1641 1.0547 0.0297 0.0424 -0.1343 81 GLU A O 631 C CB . GLU A 81 ? 0.8462 1.2564 1.0970 0.0017 0.0531 -0.1366 81 GLU A CB 632 C CG . GLU A 81 ? 0.9072 1.3085 1.1502 0.0008 0.0539 -0.1372 81 GLU A CG 633 C CD . GLU A 81 ? 0.9743 1.3637 1.2113 -0.0157 0.0566 -0.1278 81 GLU A CD 634 O OE1 . GLU A 81 ? 0.9934 1.3602 1.2285 -0.0201 0.0548 -0.1188 81 GLU A OE1 635 O OE2 . GLU A 81 ? 1.0011 1.4035 1.2331 -0.0228 0.0606 -0.1296 81 GLU A OE2 636 N N . LYS A 82 ? 0.8425 1.2060 1.0759 0.0442 0.0436 -0.1474 82 LYS A N 637 C CA . LYS A 82 ? 0.8730 1.1941 1.0929 0.0492 0.0408 -0.1452 82 LYS A CA 638 C C . LYS A 82 ? 0.8843 1.1884 1.1049 0.0312 0.0412 -0.1366 82 LYS A C 639 O O . LYS A 82 ? 0.8639 1.1851 1.0918 0.0185 0.0435 -0.1323 82 LYS A O 640 C CB . LYS A 82 ? 0.9106 1.2192 1.1134 0.0639 0.0408 -0.1545 82 LYS A CB 641 C CG . LYS A 82 ? 0.9368 1.2545 1.1325 0.0881 0.0392 -0.1631 82 LYS A CG 642 C CD . LYS A 82 ? 0.9747 1.2728 1.1472 0.1045 0.0396 -0.1720 82 LYS A CD 643 C CE . LYS A 82 ? 1.0246 1.3103 1.1788 0.1331 0.0370 -0.1786 82 LYS A CE 644 N NZ . LYS A 82 ? 1.0495 1.3879 1.2193 0.1466 0.0360 -0.1843 82 LYS A NZ 645 N N . ALA A 83 ? 0.9172 1.1882 1.1275 0.0306 0.0393 -0.1345 83 ALA A N 646 C CA . ALA A 83 ? 0.8978 1.1584 1.1084 0.0156 0.0391 -0.1280 83 ALA A CA 647 C C . ALA A 83 ? 0.9252 1.1932 1.1309 0.0099 0.0410 -0.1314 83 ALA A C 648 O O . ALA A 83 ? 0.9294 1.2090 1.1402 -0.0003 0.0416 -0.1261 83 ALA A O 649 C CB . ALA A 83 ? 0.8893 1.1176 1.0893 0.0144 0.0374 -0.1270 83 ALA A CB 650 N N . ASN A 84 ? 0.9489 1.2083 1.1420 0.0182 0.0419 -0.1404 84 ASN A N 651 C CA . ASN A 84 ? 0.9738 1.2395 1.1608 0.0136 0.0437 -0.1450 84 ASN A CA 652 C C . ASN A 84 ? 0.9590 1.2377 1.1417 0.0264 0.0455 -0.1538 84 ASN A C 653 O O . ASN A 84 ? 0.9668 1.2253 1.1317 0.0352 0.0460 -0.1617 84 ASN A O 654 C CB . ASN A 84 ? 1.0467 1.2838 1.2170 0.0069 0.0437 -0.1483 84 ASN A CB 655 C CG . ASN A 84 ? 1.0836 1.3175 1.2593 -0.0064 0.0420 -0.1411 84 ASN A CG 656 O OD1 . ASN A 84 ? 1.0819 1.3360 1.2666 -0.0147 0.0416 -0.1363 84 ASN A OD1 657 N ND2 . ASN A 84 ? 1.1108 1.3193 1.2789 -0.0071 0.0412 -0.1405 84 ASN A ND2 658 N N . PRO A 85 ? 0.9347 1.2470 1.1311 0.0269 0.0470 -0.1530 85 PRO A N 659 C CA . PRO A 85 ? 0.9470 1.2796 1.1410 0.0394 0.0488 -0.1625 85 PRO A CA 660 C C . PRO A 85 ? 0.9615 1.2906 1.1444 0.0378 0.0505 -0.1682 85 PRO A C 661 O O . PRO A 85 ? 0.9508 1.2814 1.1358 0.0234 0.0513 -0.1636 85 PRO A O 662 C CB . PRO A 85 ? 0.9206 1.2922 1.1311 0.0323 0.0512 -0.1601 85 PRO A CB 663 C CG . PRO A 85 ? 0.8933 1.2569 1.1117 0.0198 0.0504 -0.1491 85 PRO A CG 664 C CD . PRO A 85 ? 0.8925 1.2245 1.1031 0.0147 0.0480 -0.1444 85 PRO A CD 665 N N . VAL A 86 ? 0.9897 1.3136 1.1588 0.0538 0.0510 -0.1783 86 VAL A N 666 C CA . VAL A 86 ? 1.0149 1.3330 1.1710 0.0528 0.0530 -0.1847 86 VAL A CA 667 C C . VAL A 86 ? 0.9814 1.3397 1.1496 0.0470 0.0558 -0.1861 86 VAL A C 668 O O . VAL A 86 ? 0.9764 1.3353 1.1415 0.0364 0.0572 -0.1859 86 VAL A O 669 C CB . VAL A 86 ? 1.0692 1.3622 1.2004 0.0734 0.0531 -0.1954 86 VAL A CB 670 C CG1 . VAL A 86 ? 1.0890 1.3354 1.2017 0.0781 0.0514 -0.1939 86 VAL A CG1 671 C CG2 . VAL A 86 ? 1.0896 1.4150 1.2250 0.0941 0.0533 -0.2027 86 VAL A CG2 672 N N . ASN A 87 ? 0.9325 1.3257 1.1132 0.0528 0.0570 -0.1881 87 ASN A N 673 C CA . ASN A 87 ? 0.9212 1.3537 1.1110 0.0456 0.0609 -0.1905 87 ASN A CA 674 C C . ASN A 87 ? 0.9035 1.3474 1.1051 0.0249 0.0628 -0.1799 87 ASN A C 675 O O . ASN A 87 ? 0.9052 1.3706 1.1170 0.0208 0.0644 -0.1780 87 ASN A O 676 C CB . ASN A 87 ? 0.9297 1.3991 1.1244 0.0609 0.0622 -0.2003 87 ASN A CB 677 C CG . ASN A 87 ? 0.9698 1.4273 1.1472 0.0855 0.0606 -0.2114 87 ASN A CG 678 O OD1 . ASN A 87 ? 0.9783 1.4164 1.1416 0.0866 0.0614 -0.2149 87 ASN A OD1 679 N ND2 . ASN A 87 ? 0.9948 1.4630 1.1707 0.1065 0.0586 -0.2174 87 ASN A ND2 680 N N . ASP A 88 ? 0.9350 1.3633 1.1320 0.0125 0.0629 -0.1734 88 ASP A N 681 C CA . ASP A 88 ? 0.9368 1.3680 1.1375 -0.0041 0.0646 -0.1628 88 ASP A CA 682 C C . ASP A 88 ? 0.9506 1.3998 1.1459 -0.0124 0.0689 -0.1642 88 ASP A C 683 O O . ASP A 88 ? 0.9413 1.4192 1.1393 -0.0128 0.0731 -0.1705 88 ASP A O 684 C CB . ASP A 88 ? 0.9378 1.3390 1.1352 -0.0083 0.0606 -0.1543 88 ASP A CB 685 C CG . ASP A 88 ? 0.9531 1.3521 1.1503 -0.0205 0.0617 -0.1427 88 ASP A CG 686 O OD1 . ASP A 88 ? 0.9362 1.3468 1.1362 -0.0263 0.0651 -0.1397 88 ASP A OD1 687 O OD2 . ASP A 88 ? 0.9914 1.3768 1.1831 -0.0240 0.0594 -0.1370 88 ASP A OD2 688 N N . LEU A 89 ? 0.9525 1.3882 1.1399 -0.0187 0.0680 -0.1591 89 LEU A N 689 C CA . LEU A 89 ? 0.9499 1.3991 1.1296 -0.0251 0.0716 -0.1602 89 LEU A CA 690 C C . LEU A 89 ? 0.9454 1.3942 1.1206 -0.0168 0.0702 -0.1702 89 LEU A C 691 O O . LEU A 89 ? 0.9303 1.3615 1.0996 -0.0169 0.0670 -0.1696 89 LEU A O 692 C CB . LEU A 89 ? 0.9507 1.3866 1.1211 -0.0340 0.0710 -0.1493 89 LEU A CB 693 C CG . LEU A 89 ? 0.9306 1.3565 1.0989 -0.0410 0.0721 -0.1383 89 LEU A CG 694 C CD1 . LEU A 89 ? 0.9328 1.3433 1.0879 -0.0435 0.0703 -0.1284 89 LEU A CD1 695 C CD2 . LEU A 89 ? 0.9126 1.3544 1.0777 -0.0507 0.0792 -0.1386 89 LEU A CD2 696 N N . CYS A 90 ? 0.9656 1.4353 1.1421 -0.0099 0.0731 -0.1802 90 CYS A N 697 C CA . CYS A 90 ? 0.9724 1.4396 1.1410 -0.0002 0.0725 -0.1906 90 CYS A CA 698 C C . CYS A 90 ? 0.9451 1.4084 1.1047 -0.0089 0.0728 -0.1888 90 CYS A C 699 O O . CYS A 90 ? 0.9468 1.3906 1.0982 -0.0072 0.0701 -0.1920 90 CYS A O 700 C CB . CYS A 90 ? 1.0169 1.5142 1.1877 0.0094 0.0760 -0.2014 90 CYS A CB 701 S SG . CYS A 90 ? 1.0756 1.6142 1.2524 -0.0049 0.0830 -0.2001 90 CYS A SG 702 N N . TYR A 91 ? 0.9121 1.3931 1.0706 -0.0191 0.0765 -0.1841 91 TYR A N 703 C CA . TYR A 91 ? 0.9188 1.3968 1.0676 -0.0266 0.0764 -0.1801 91 TYR A CA 704 C C . TYR A 91 ? 0.9017 1.3623 1.0494 -0.0319 0.0729 -0.1685 91 TYR A C 705 O O . TYR A 91 ? 0.9148 1.3733 1.0644 -0.0362 0.0742 -0.1602 91 TYR A O 706 C CB . TYR A 91 ? 0.9521 1.4517 1.0952 -0.0346 0.0823 -0.1791 91 TYR A CB 707 C CG . TYR A 91 ? 0.9858 1.4869 1.1168 -0.0381 0.0824 -0.1789 91 TYR A CG 708 C CD1 . TYR A 91 ? 0.9823 1.4711 1.1043 -0.0424 0.0799 -0.1690 91 TYR A CD1 709 C CD2 . TYR A 91 ? 0.9920 1.5089 1.1195 -0.0354 0.0849 -0.1890 91 TYR A CD2 710 C CE1 . TYR A 91 ? 0.9903 1.4841 1.1006 -0.0440 0.0796 -0.1692 91 TYR A CE1 711 C CE2 . TYR A 91 ? 0.9978 1.5173 1.1140 -0.0388 0.0850 -0.1890 91 TYR A CE2 712 C CZ . TYR A 91 ? 0.9892 1.4979 1.0971 -0.0431 0.0822 -0.1791 91 TYR A CZ 713 O OH . TYR A 91 ? 1.0041 1.5187 1.1002 -0.0448 0.0818 -0.1796 91 TYR A OH 714 N N . PRO A 92 ? 0.9124 1.3620 1.0554 -0.0319 0.0687 -0.1686 92 PRO A N 715 C CA . PRO A 92 ? 0.8990 1.3365 1.0422 -0.0343 0.0647 -0.1593 92 PRO A CA 716 C C . PRO A 92 ? 0.9172 1.3570 1.0518 -0.0380 0.0661 -0.1477 92 PRO A C 717 O O . PRO A 92 ? 0.9458 1.3953 1.0705 -0.0408 0.0698 -0.1471 92 PRO A O 718 C CB . PRO A 92 ? 0.8972 1.3327 1.0355 -0.0356 0.0610 -0.1647 92 PRO A CB 719 C CG . PRO A 92 ? 0.9159 1.3639 1.0471 -0.0359 0.0637 -0.1725 92 PRO A CG 720 C CD . PRO A 92 ? 0.9213 1.3729 1.0570 -0.0313 0.0679 -0.1775 92 PRO A CD 721 N N . GLY A 93 ? 0.9590 1.3870 1.0939 -0.0375 0.0635 -0.1386 93 GLY A N 722 C CA . GLY A 93 ? 0.9833 1.4055 1.1032 -0.0381 0.0645 -0.1271 93 GLY A CA 723 C C . GLY A 93 ? 0.9861 1.3922 1.1067 -0.0367 0.0629 -0.1179 93 GLY A C 724 O O . GLY A 93 ? 0.9619 1.3644 1.0939 -0.0338 0.0584 -0.1191 93 GLY A O 725 N N . ASP A 94 ? 1.0187 1.4127 1.1238 -0.0397 0.0673 -0.1090 94 ASP A N 726 C CA . ASP A 94 ? 1.0328 1.4076 1.1336 -0.0388 0.0669 -0.0997 94 ASP A CA 727 C C . ASP A 94 ? 1.0076 1.3732 1.1001 -0.0492 0.0746 -0.0970 94 ASP A C 728 O O . ASP A 94 ? 1.0229 1.3961 1.1067 -0.0569 0.0805 -0.1001 94 ASP A O 729 C CB . ASP A 94 ? 1.0909 1.4533 1.1697 -0.0303 0.0642 -0.0897 94 ASP A CB 730 C CG . ASP A 94 ? 1.1444 1.5204 1.2335 -0.0213 0.0563 -0.0924 94 ASP A CG 731 O OD1 . ASP A 94 ? 1.1910 1.5663 1.2963 -0.0205 0.0527 -0.0937 94 ASP A OD1 732 O OD2 . ASP A 94 ? 1.1943 1.5834 1.2743 -0.0160 0.0539 -0.0938 94 ASP A OD2 733 N N . PHE A 95 ? 0.9628 1.3142 1.0576 -0.0508 0.0747 -0.0921 95 PHE A N 734 C CA . PHE A 95 ? 0.9129 1.2536 0.9963 -0.0631 0.0824 -0.0891 95 PHE A CA 735 C C . PHE A 95 ? 0.9117 1.2197 0.9701 -0.0605 0.0827 -0.0766 95 PHE A C 736 O O . PHE A 95 ? 0.9133 1.2133 0.9806 -0.0534 0.0777 -0.0731 95 PHE A O 737 C CB . PHE A 95 ? 0.8737 1.2287 0.9824 -0.0667 0.0822 -0.0961 95 PHE A CB 738 C CG . PHE A 95 ? 0.8841 1.2434 0.9860 -0.0824 0.0908 -0.0980 95 PHE A CG 739 C CD1 . PHE A 95 ? 0.9108 1.2436 0.9898 -0.0920 0.0958 -0.0893 95 PHE A CD1 740 C CD2 . PHE A 95 ? 0.8843 1.2754 1.0009 -0.0879 0.0941 -0.1095 95 PHE A CD2 741 C CE1 . PHE A 95 ? 0.9353 1.2737 1.0063 -0.1106 0.1047 -0.0925 95 PHE A CE1 742 C CE2 . PHE A 95 ? 0.8835 1.2866 0.9949 -0.1044 0.1023 -0.1130 95 PHE A CE2 743 C CZ . PHE A 95 ? 0.9013 1.2784 0.9900 -0.1176 0.1080 -0.1048 95 PHE A CZ 744 N N . ASN A 96 ? 0.9475 1.2340 0.9712 -0.0653 0.0889 -0.0698 96 ASN A N 745 C CA . ASN A 96 ? 0.9833 1.2326 0.9743 -0.0587 0.0894 -0.0574 96 ASN A CA 746 C C . ASN A 96 ? 0.9639 1.1912 0.9487 -0.0683 0.0936 -0.0536 96 ASN A C 747 O O . ASN A 96 ? 0.9386 1.1712 0.9255 -0.0867 0.1010 -0.0584 96 ASN A O 748 C CB . ASN A 96 ? 1.0586 1.2843 1.0069 -0.0607 0.0958 -0.0513 96 ASN A CB 749 C CG . ASN A 96 ? 1.1217 1.3113 1.0331 -0.0441 0.0936 -0.0390 96 ASN A CG 750 O OD1 . ASN A 96 ? 1.1059 1.3077 1.0251 -0.0245 0.0845 -0.0377 96 ASN A OD1 751 N ND2 . ASN A 96 ? 1.1800 1.3251 1.0480 -0.0517 0.1021 -0.0307 96 ASN A ND2 752 N N . ASP A 97 ? 0.9754 1.1814 0.9523 -0.0560 0.0890 -0.0456 97 ASP A N 753 C CA . ASP A 97 ? 0.9722 1.1556 0.9431 -0.0627 0.0919 -0.0415 97 ASP A CA 754 C C . ASP A 97 ? 0.9041 1.1160 0.9127 -0.0747 0.0920 -0.0511 97 ASP A C 755 O O . ASP A 97 ? 0.8833 1.0863 0.8849 -0.0908 0.0988 -0.0519 97 ASP A O 756 C CB . ASP A 97 ? 1.0691 1.2092 0.9908 -0.0758 0.1029 -0.0343 97 ASP A CB 757 C CG . ASP A 97 ? 1.1750 1.2732 1.0523 -0.0580 0.1018 -0.0221 97 ASP A CG 758 O OD1 . ASP A 97 ? 1.1874 1.2879 1.0739 -0.0374 0.0929 -0.0183 97 ASP A OD1 759 O OD2 . ASP A 97 ? 1.2674 1.3299 1.0977 -0.0643 0.1103 -0.0165 97 ASP A OD2 760 N N . TYR A 98 ? 0.8500 1.0950 0.8951 -0.0664 0.0845 -0.0588 98 TYR A N 761 C CA . TYR A 98 ? 0.8282 1.1019 0.9065 -0.0729 0.0840 -0.0689 98 TYR A CA 762 C C . TYR A 98 ? 0.8338 1.0982 0.9206 -0.0744 0.0828 -0.0666 98 TYR A C 763 O O . TYR A 98 ? 0.8376 1.1140 0.9337 -0.0861 0.0869 -0.0720 98 TYR A O 764 C CB . TYR A 98 ? 0.7907 1.0906 0.8970 -0.0613 0.0764 -0.0764 98 TYR A CB 765 C CG . TYR A 98 ? 0.7683 1.0944 0.9031 -0.0631 0.0754 -0.0873 98 TYR A CG 766 C CD1 . TYR A 98 ? 0.7726 1.1172 0.9096 -0.0746 0.0819 -0.0942 98 TYR A CD1 767 C CD2 . TYR A 98 ? 0.7467 1.0796 0.9032 -0.0524 0.0682 -0.0913 98 TYR A CD2 768 C CE1 . TYR A 98 ? 0.7630 1.1342 0.9236 -0.0717 0.0803 -0.1045 98 TYR A CE1 769 C CE2 . TYR A 98 ? 0.7293 1.0806 0.9056 -0.0504 0.0673 -0.1008 98 TYR A CE2 770 C CZ . TYR A 98 ? 0.7646 1.1363 0.9432 -0.0580 0.0729 -0.1074 98 TYR A CZ 771 O OH . TYR A 98 ? 0.8067 1.1996 1.0026 -0.0519 0.0715 -0.1173 98 TYR A OH 772 N N . GLU A 99 ? 0.8596 1.1057 0.9429 -0.0623 0.0772 -0.0592 99 GLU A N 773 C CA . GLU A 99 ? 0.8591 1.0953 0.9506 -0.0619 0.0753 -0.0565 99 GLU A CA 774 C C . GLU A 99 ? 0.8637 1.0725 0.9276 -0.0756 0.0835 -0.0512 99 GLU A C 775 O O . GLU A 99 ? 0.8585 1.0702 0.9325 -0.0838 0.0851 -0.0535 99 GLU A O 776 C CB . GLU A 99 ? 0.8759 1.1026 0.9695 -0.0455 0.0675 -0.0506 99 GLU A CB 777 C CG . GLU A 99 ? 0.8690 1.1216 0.9911 -0.0365 0.0600 -0.0575 99 GLU A CG 778 C CD . GLU A 99 ? 0.9077 1.1737 1.0259 -0.0321 0.0587 -0.0604 99 GLU A CD 779 O OE1 . GLU A 99 ? 0.9443 1.1976 1.0363 -0.0291 0.0609 -0.0543 99 GLU A OE1 780 O OE2 . GLU A 99 ? 0.9281 1.2152 1.0667 -0.0312 0.0556 -0.0689 99 GLU A OE2 781 N N . GLU A 100 ? 0.8852 1.0657 0.9109 -0.0785 0.0892 -0.0443 100 GLU A N 782 C CA . GLU A 100 ? 0.9140 1.0617 0.9048 -0.0952 0.0991 -0.0399 100 GLU A CA 783 C C . GLU A 100 ? 0.9298 1.1015 0.9291 -0.1188 0.1072 -0.0498 100 GLU A C 784 O O . GLU A 100 ? 1.0073 1.1672 0.9939 -0.1361 0.1141 -0.0504 100 GLU A O 785 C CB . GLU A 100 ? 0.9519 1.0584 0.8929 -0.0922 0.1042 -0.0305 100 GLU A CB 786 C CG . GLU A 100 ? 0.9801 1.0544 0.8995 -0.0702 0.0987 -0.0196 100 GLU A CG 787 C CD . GLU A 100 ? 1.0086 1.0489 0.9096 -0.0747 0.1019 -0.0143 100 GLU A CD 788 O OE1 . GLU A 100 ? 1.0526 1.0637 0.9220 -0.0955 0.1127 -0.0134 100 GLU A OE1 789 O OE2 . GLU A 100 ? 0.9743 1.0171 0.8909 -0.0587 0.0940 -0.0114 100 GLU A OE2 790 N N . LEU A 101 ? 0.9081 1.1159 0.9282 -0.1198 0.1064 -0.0584 101 LEU A N 791 C CA . LEU A 101 ? 0.8914 1.1329 0.9240 -0.1392 0.1130 -0.0698 101 LEU A CA 792 C C . LEU A 101 ? 0.8484 1.1208 0.9174 -0.1371 0.1084 -0.0773 101 LEU A C 793 O O . LEU A 101 ? 0.8245 1.1095 0.8933 -0.1546 0.1145 -0.0828 101 LEU A O 794 C CB . LEU A 101 ? 0.8949 1.1670 0.9387 -0.1373 0.1130 -0.0771 101 LEU A CB 795 C CG . LEU A 101 ? 0.9036 1.2171 0.9594 -0.1553 0.1199 -0.0901 101 LEU A CG 796 C CD1 . LEU A 101 ? 0.9382 1.2355 0.9601 -0.1838 0.1329 -0.0898 101 LEU A CD1 797 C CD2 . LEU A 101 ? 0.9157 1.2545 0.9795 -0.1503 0.1193 -0.0962 101 LEU A CD2 798 N N . LYS A 102 ? 0.8205 1.1050 0.9181 -0.1165 0.0980 -0.0780 102 LYS A N 799 C CA . LYS A 102 ? 0.8026 1.1089 0.9301 -0.1110 0.0929 -0.0837 102 LYS A CA 800 C C . LYS A 102 ? 0.8045 1.0896 0.9218 -0.1194 0.0953 -0.0786 102 LYS A C 801 O O . LYS A 102 ? 0.7886 1.0964 0.9214 -0.1257 0.0961 -0.0854 102 LYS A O 802 C CB . LYS A 102 ? 0.8073 1.1161 0.9569 -0.0893 0.0824 -0.0832 102 LYS A CB 803 C CG . LYS A 102 ? 0.8471 1.1799 1.0097 -0.0814 0.0799 -0.0908 102 LYS A CG 804 C CD . LYS A 102 ? 0.8638 1.1921 1.0406 -0.0640 0.0711 -0.0902 102 LYS A CD 805 C CE . LYS A 102 ? 0.8744 1.2192 1.0742 -0.0553 0.0667 -0.0980 102 LYS A CE 806 N NZ . LYS A 102 ? 0.9001 1.2382 1.1079 -0.0421 0.0600 -0.0993 102 LYS A NZ 807 N N . HIS A 103 ? 0.8194 1.0618 0.9088 -0.1183 0.0964 -0.0672 103 HIS A N 808 C CA . HIS A 103 ? 0.8462 1.0617 0.9193 -0.1267 0.0996 -0.0618 103 HIS A CA 809 C C . HIS A 103 ? 0.8796 1.0967 0.9323 -0.1541 0.1113 -0.0667 103 HIS A C 810 O O . HIS A 103 ? 0.8855 1.1044 0.9393 -0.1657 0.1142 -0.0691 103 HIS A O 811 C CB . HIS A 103 ? 0.8824 1.0497 0.9239 -0.1168 0.0987 -0.0487 103 HIS A CB 812 C CG . HIS A 103 ? 0.9006 1.0343 0.9196 -0.1247 0.1027 -0.0429 103 HIS A CG 813 N ND1 . HIS A 103 ? 0.8740 1.0064 0.9107 -0.1141 0.0961 -0.0407 103 HIS A ND1 814 C CD2 . HIS A 103 ? 0.9361 1.0340 0.9136 -0.1434 0.1133 -0.0395 103 HIS A CD2 815 C CE1 . HIS A 103 ? 0.8944 0.9932 0.9033 -0.1247 0.1019 -0.0360 103 HIS A CE1 816 N NE2 . HIS A 103 ? 0.9399 1.0155 0.9112 -0.1430 0.1126 -0.0352 103 HIS A NE2 817 N N . LEU A 104 ? 0.9295 1.1467 0.9622 -0.1659 0.1185 -0.0686 104 LEU A N 818 C CA . LEU A 104 ? 0.9909 1.2130 1.0016 -0.1960 0.1312 -0.0749 104 LEU A CA 819 C C . LEU A 104 ? 0.9782 1.2609 1.0248 -0.2050 0.1313 -0.0898 104 LEU A C 820 O O . LEU A 104 ? 0.9893 1.2823 1.0256 -0.2296 0.1399 -0.0960 104 LEU A O 821 C CB . LEU A 104 ? 1.0334 1.2462 1.0173 -0.2046 0.1382 -0.0743 104 LEU A CB 822 C CG . LEU A 104 ? 1.1036 1.2853 1.0381 -0.2356 0.1534 -0.0737 104 LEU A CG 823 C CD1 . LEU A 104 ? 1.1448 1.2586 1.0346 -0.2367 0.1569 -0.0609 104 LEU A CD1 824 C CD2 . LEU A 104 ? 1.1286 1.3060 1.0422 -0.2396 0.1584 -0.0734 104 LEU A CD2 825 N N . LEU A 105 ? 0.9601 1.2820 1.0455 -0.1846 0.1219 -0.0958 105 LEU A N 826 C CA . LEU A 105 ? 0.9215 1.3018 1.0407 -0.1846 0.1200 -0.1098 105 LEU A CA 827 C C . LEU A 105 ? 0.9212 1.3089 1.0559 -0.1821 0.1162 -0.1112 105 LEU A C 828 O O . LEU A 105 ? 0.9852 1.4200 1.1387 -0.1876 0.1172 -0.1232 105 LEU A O 829 C CB . LEU A 105 ? 0.8713 1.2793 1.0205 -0.1593 0.1106 -0.1145 105 LEU A CB 830 C CG . LEU A 105 ? 0.8634 1.2899 1.0095 -0.1612 0.1138 -0.1197 105 LEU A CG 831 C CD1 . LEU A 105 ? 0.8467 1.2956 1.0210 -0.1349 0.1040 -0.1247 105 LEU A CD1 832 C CD2 . LEU A 105 ? 0.8961 1.3645 1.0387 -0.1849 0.1238 -0.1320 105 LEU A CD2 833 N N . SER A 106 ? 0.9776 1.6201 0.9941 -0.1601 0.1187 -0.1161 106 SER A N 834 C CA A SER A 106 ? 0.9825 1.6513 0.9951 -0.1676 0.1187 -0.1166 106 SER A CA 835 C CA B SER A 106 ? 0.9764 1.6451 0.9890 -0.1676 0.1187 -0.1165 106 SER A CA 836 C C . SER A 106 ? 0.9982 1.6597 0.9879 -0.1827 0.1219 -0.1289 106 SER A C 837 O O . SER A 106 ? 1.0064 1.6892 0.9891 -0.1923 0.1204 -0.1303 106 SER A O 838 C CB A SER A 106 ? 0.9835 1.6527 0.9941 -0.1578 0.1219 -0.1176 106 SER A CB 839 C CB B SER A 106 ? 0.9711 1.6394 0.9818 -0.1575 0.1219 -0.1176 106 SER A CB 840 O OG A SER A 106 ? 0.9998 1.6381 0.9898 -0.1549 0.1285 -0.1319 106 SER A OG 841 O OG B SER A 106 ? 0.9282 1.5973 0.9607 -0.1445 0.1179 -0.1068 106 SER A OG 842 N N . ARG A 107 ? 1.0406 1.6705 1.0174 -0.1856 0.1253 -0.1373 107 ARG A N 843 C CA . ARG A 107 ? 1.0994 1.7183 1.0565 -0.2016 0.1272 -0.1481 107 ARG A CA 844 C C . ARG A 107 ? 1.0417 1.6691 1.0094 -0.2127 0.1257 -0.1431 107 ARG A C 845 O O . ARG A 107 ? 1.0521 1.6672 1.0067 -0.2270 0.1272 -0.1505 107 ARG A O 846 C CB . ARG A 107 ? 1.1857 1.7605 1.1194 -0.1988 0.1324 -0.1611 107 ARG A CB 847 C CG . ARG A 107 ? 1.2525 1.8195 1.1704 -0.1934 0.1357 -0.1718 107 ARG A CG 848 C CD . ARG A 107 ? 1.2964 1.8643 1.2269 -0.1740 0.1373 -0.1667 107 ARG A CD 849 N NE . ARG A 107 ? 1.3689 1.9441 1.2902 -0.1691 0.1421 -0.1745 107 ARG A NE 850 C CZ . ARG A 107 ? 1.4000 1.9480 1.3077 -0.1602 0.1479 -0.1870 107 ARG A CZ 851 N NH1 . ARG A 107 ? 1.4306 1.9392 1.3316 -0.1553 0.1479 -0.1924 107 ARG A NH1 852 N NH2 . ARG A 107 ? 1.4213 1.9818 1.3217 -0.1555 0.1540 -0.1939 107 ARG A NH2 853 N N . ILE A 108 ? 0.9792 1.6280 0.9718 -0.2064 0.1229 -0.1307 108 ILE A N 854 C CA . ILE A 108 ? 0.9567 1.6158 0.9632 -0.2136 0.1236 -0.1258 108 ILE A CA 855 C C . ILE A 108 ? 0.9251 1.6275 0.9593 -0.2152 0.1170 -0.1145 108 ILE A C 856 O O . ILE A 108 ? 0.9294 1.6462 0.9783 -0.2037 0.1124 -0.1059 108 ILE A O 857 C CB . ILE A 108 ? 0.9372 1.5731 0.9462 -0.2021 0.1280 -0.1232 108 ILE A CB 858 C CG1 . ILE A 108 ? 0.9635 1.5555 0.9452 -0.2032 0.1335 -0.1327 108 ILE A CG1 859 C CG2 . ILE A 108 ? 0.9234 1.5762 0.9500 -0.2069 0.1307 -0.1175 108 ILE A CG2 860 C CD1 . ILE A 108 ? 0.9615 1.5262 0.9394 -0.1903 0.1357 -0.1301 108 ILE A CD1 861 N N . ASN A 109 ? 0.9231 1.6455 0.9661 -0.2297 0.1158 -0.1138 109 ASN A N 862 C CA . ASN A 109 ? 0.9073 1.6713 0.9793 -0.2319 0.1084 -0.1027 109 ASN A CA 863 C C . ASN A 109 ? 0.8910 1.6668 0.9881 -0.2297 0.1122 -0.0970 109 ASN A C 864 O O . ASN A 109 ? 0.8410 1.6480 0.9666 -0.2253 0.1064 -0.0869 109 ASN A O 865 C CB . ASN A 109 ? 0.9410 1.7269 1.0088 -0.2504 0.1014 -0.1049 109 ASN A CB 866 C CG . ASN A 109 ? 0.9656 1.7492 1.0113 -0.2513 0.0971 -0.1090 109 ASN A CG 867 O OD1 . ASN A 109 ? 0.9592 1.7583 1.0127 -0.2417 0.0924 -0.1004 109 ASN A OD1 868 N ND2 . ASN A 109 ? 1.0183 1.7817 1.0356 -0.2629 0.0991 -0.1221 109 ASN A ND2 869 N N . HIS A 110 ? 0.8984 1.6496 0.9847 -0.2325 0.1223 -0.1031 110 HIS A N 870 C CA . HIS A 110 ? 0.9054 1.6684 1.0130 -0.2307 0.1289 -0.0988 110 HIS A CA 871 C C . HIS A 110 ? 0.9109 1.6375 0.9998 -0.2263 0.1408 -0.1040 110 HIS A C 872 O O . HIS A 110 ? 0.9065 1.6041 0.9689 -0.2356 0.1452 -0.1114 110 HIS A O 873 C CB . HIS A 110 ? 0.9216 1.7150 1.0462 -0.2492 0.1281 -0.0974 110 HIS A CB 874 C CG . HIS A 110 ? 0.9254 1.7448 1.0822 -0.2457 0.1340 -0.0910 110 HIS A CG 875 N ND1 . HIS A 110 ? 0.9445 1.7835 1.1161 -0.2614 0.1393 -0.0906 110 HIS A ND1 876 C CD2 . HIS A 110 ? 0.9143 1.7432 1.0923 -0.2279 0.1360 -0.0853 110 HIS A CD2 877 C CE1 . HIS A 110 ? 0.9333 1.7952 1.1350 -0.2524 0.1457 -0.0850 110 HIS A CE1 878 N NE2 . HIS A 110 ? 0.9192 1.7738 1.1239 -0.2316 0.1437 -0.0825 110 HIS A NE2 879 N N . PHE A 111 ? 0.9005 1.6274 1.0019 -0.2118 0.1451 -0.1000 111 PHE A N 880 C CA . PHE A 111 ? 0.9278 1.6258 1.0130 -0.2078 0.1567 -0.1034 111 PHE A CA 881 C C . PHE A 111 ? 0.9377 1.6618 1.0457 -0.2117 0.1664 -0.1003 111 PHE A C 882 O O . PHE A 111 ? 0.9225 1.6825 1.0632 -0.2068 0.1625 -0.0945 111 PHE A O 883 C CB . PHE A 111 ? 0.9178 1.5945 0.9975 -0.1873 0.1547 -0.1025 111 PHE A CB 884 C CG . PHE A 111 ? 0.9153 1.5591 0.9703 -0.1817 0.1485 -0.1060 111 PHE A CG 885 C CD1 . PHE A 111 ? 0.9338 1.5475 0.9602 -0.1910 0.1517 -0.1124 111 PHE A CD1 886 C CD2 . PHE A 111 ? 0.8819 1.5238 0.9443 -0.1665 0.1396 -0.1024 111 PHE A CD2 887 C CE1 . PHE A 111 ? 0.9200 1.5050 0.9278 -0.1837 0.1464 -0.1157 111 PHE A CE1 888 C CE2 . PHE A 111 ? 0.8796 1.4949 0.9241 -0.1607 0.1346 -0.1050 111 PHE A CE2 889 C CZ . PHE A 111 ? 0.8955 1.4832 0.9136 -0.1685 0.1382 -0.1119 111 PHE A CZ 890 N N . GLU A 112 ? 0.9729 1.6795 1.0648 -0.2201 0.1791 -0.1033 112 GLU A N 891 C CA . GLU A 112 ? 0.9954 1.7230 1.1061 -0.2206 0.1923 -0.1007 112 GLU A CA 892 C C . GLU A 112 ? 0.9863 1.6784 1.0704 -0.2100 0.2034 -0.1037 112 GLU A C 893 O O . GLU A 112 ? 0.9761 1.6336 1.0275 -0.2182 0.2086 -0.1065 112 GLU A O 894 C CB . GLU A 112 ? 1.0361 1.7819 1.1547 -0.2438 0.1990 -0.0998 112 GLU A CB 895 C CG . GLU A 112 ? 1.0643 1.8460 1.2143 -0.2452 0.2122 -0.0957 112 GLU A CG 896 C CD . GLU A 112 ? 1.1265 1.9251 1.2848 -0.2701 0.2193 -0.0937 112 GLU A CD 897 O OE1 . GLU A 112 ? 1.1481 1.9526 1.3072 -0.2861 0.2077 -0.0941 112 GLU A OE1 898 O OE2 . GLU A 112 ? 1.1346 1.9404 1.2978 -0.2745 0.2365 -0.0919 112 GLU A OE2 899 N N . LYS A 113 ? 0.9640 1.6626 1.0605 -0.1916 0.2056 -0.1031 113 LYS A N 900 C CA . LYS A 113 ? 0.9925 1.6577 1.0620 -0.1800 0.2145 -0.1067 113 LYS A CA 901 C C . LYS A 113 ? 1.0168 1.6847 1.0789 -0.1897 0.2346 -0.1069 113 LYS A C 902 O O . LYS A 113 ? 1.0199 1.7277 1.1140 -0.1946 0.2435 -0.1043 113 LYS A O 903 C CB . LYS A 113 ? 0.9793 1.6511 1.0652 -0.1580 0.2104 -0.1071 113 LYS A CB 904 C CG . LYS A 113 ? 1.0190 1.6543 1.0743 -0.1451 0.2172 -0.1121 113 LYS A CG 905 C CD . LYS A 113 ? 1.0273 1.6461 1.0827 -0.1261 0.2024 -0.1132 113 LYS A CD 906 C CE . LYS A 113 ? 1.0076 1.6591 1.1026 -0.1131 0.1994 -0.1116 113 LYS A CE 907 N NZ . LYS A 113 ? 1.0010 1.6436 1.1042 -0.1009 0.1802 -0.1092 113 LYS A NZ 908 N N . ILE A 114 ? 1.0393 1.6662 1.0605 -0.1930 0.2415 -0.1091 114 ILE A N 909 C CA . ILE A 114 ? 1.0856 1.7108 1.0938 -0.2016 0.2620 -0.1083 114 ILE A CA 910 C C . ILE A 114 ? 1.1370 1.7199 1.1037 -0.1900 0.2680 -0.1115 114 ILE A C 911 O O . ILE A 114 ? 1.1636 1.7119 1.1072 -0.1795 0.2544 -0.1139 114 ILE A O 912 C CB . ILE A 114 ? 1.1004 1.7202 1.0976 -0.2270 0.2667 -0.1048 114 ILE A CB 913 C CG1 . ILE A 114 ? 1.1170 1.6868 1.0747 -0.2307 0.2554 -0.1063 114 ILE A CG1 914 C CG2 . ILE A 114 ? 1.0770 1.7404 1.1143 -0.2402 0.2610 -0.1021 114 ILE A CG2 915 C CD1 . ILE A 114 ? 1.1430 1.6933 1.0786 -0.2534 0.2632 -0.1030 114 ILE A CD1 916 N N . GLN A 115 ? 1.1586 1.7458 1.1162 -0.1924 0.2886 -0.1113 115 GLN A N 917 C CA . GLN A 115 ? 1.1772 1.7264 1.0922 -0.1824 0.2963 -0.1145 115 GLN A CA 918 C C . GLN A 115 ? 1.2054 1.7155 1.0765 -0.1989 0.3005 -0.1102 115 GLN A C 919 O O . GLN A 115 ? 1.2130 1.7366 1.0875 -0.2184 0.3138 -0.1049 115 GLN A O 920 C CB . GLN A 115 ? 1.1795 1.7541 1.1051 -0.1748 0.3182 -0.1172 115 GLN A CB 921 C CG . GLN A 115 ? 1.2111 1.7496 1.0960 -0.1583 0.3230 -0.1235 115 GLN A CG 922 C CD . GLN A 115 ? 1.2133 1.7748 1.1026 -0.1526 0.3489 -0.1271 115 GLN A CD 923 O OE1 . GLN A 115 ? 1.1951 1.7706 1.1024 -0.1329 0.3506 -0.1345 115 GLN A OE1 924 N NE2 . GLN A 115 ? 1.2429 1.8085 1.1168 -0.1697 0.3698 -0.1219 115 GLN A NE2 925 N N . ILE A 116 ? 1.2196 1.6813 1.0513 -0.1915 0.2881 -0.1117 116 ILE A N 926 C CA . ILE A 116 ? 1.2615 1.6803 1.0498 -0.2053 0.2887 -0.1067 116 ILE A CA 927 C C . ILE A 116 ? 1.3104 1.6940 1.0508 -0.1995 0.2983 -0.1068 116 ILE A C 928 O O . ILE A 116 ? 1.3520 1.7134 1.0603 -0.2144 0.3087 -0.1004 116 ILE A O 929 C CB . ILE A 116 ? 1.2422 1.6300 1.0210 -0.2046 0.2658 -0.1067 116 ILE A CB 930 C CG1 . ILE A 116 ? 1.2191 1.5929 0.9967 -0.1821 0.2487 -0.1119 116 ILE A CG1 931 C CG2 . ILE A 116 ? 1.2196 1.6369 1.0348 -0.2162 0.2597 -0.1061 116 ILE A CG2 932 C CD1 . ILE A 116 ? 1.2181 1.5564 0.9803 -0.1795 0.2286 -0.1113 116 ILE A CD1 933 N N . ILE A 117 ? 1.3171 1.6934 1.0505 -0.1786 0.2939 -0.1135 117 ILE A N 934 C CA . ILE A 117 ? 1.3734 1.7190 1.0601 -0.1718 0.3034 -0.1155 117 ILE A CA 935 C C . ILE A 117 ? 1.3663 1.7386 1.0705 -0.1543 0.3142 -0.1244 117 ILE A C 936 O O . ILE A 117 ? 1.3690 1.7355 1.0816 -0.1362 0.2987 -0.1311 117 ILE A O 937 C CB . ILE A 117 ? 1.3981 1.6898 1.0438 -0.1628 0.2820 -0.1159 117 ILE A CB 938 C CG1 . ILE A 117 ? 1.3933 1.6615 1.0324 -0.1759 0.2678 -0.1086 117 ILE A CG1 939 C CG2 . ILE A 117 ? 1.4577 1.7140 1.0472 -0.1607 0.2920 -0.1161 117 ILE A CG2 940 C CD1 . ILE A 117 ? 1.4238 1.6382 1.0213 -0.1693 0.2484 -0.1069 117 ILE A CD1 941 N N . PRO A 118 ? 1.3782 1.7797 1.0893 -0.1597 0.3408 -0.1243 118 PRO A N 942 C CA . PRO A 118 ? 1.3793 1.8082 1.1098 -0.1421 0.3537 -0.1337 118 PRO A CA 943 C C . PRO A 118 ? 1.4167 1.8058 1.1057 -0.1227 0.3471 -0.1431 118 PRO A C 944 O O . PRO A 118 ? 1.4505 1.7946 1.0847 -0.1265 0.3446 -0.1411 118 PRO A O 945 C CB . PRO A 118 ? 1.4092 1.8653 1.1394 -0.1542 0.3858 -0.1304 118 PRO A CB 946 C CG . PRO A 118 ? 1.4056 1.8624 1.1357 -0.1803 0.3870 -0.1182 118 PRO A CG 947 C CD . PRO A 118 ? 1.4087 1.8182 1.1103 -0.1827 0.3605 -0.1151 118 PRO A CD 948 N N . LYS A 119 ? 1.4124 1.8170 1.1273 -0.1025 0.3429 -0.1530 119 LYS A N 949 C CA . LYS A 119 ? 1.4646 1.8322 1.1446 -0.0834 0.3341 -0.1636 119 LYS A CA 950 C C . LYS A 119 ? 1.5363 1.8862 1.1663 -0.0820 0.3584 -0.1688 119 LYS A C 951 O O . LYS A 119 ? 1.5890 1.8914 1.1643 -0.0765 0.3504 -0.1730 119 LYS A O 952 C CB . LYS A 119 ? 1.4475 1.8386 1.1710 -0.0630 0.3265 -0.1728 119 LYS A CB 953 C CG . LYS A 119 ? 1.4768 1.8265 1.1754 -0.0458 0.3042 -0.1814 119 LYS A CG 954 C CD . LYS A 119 ? 1.4693 1.8416 1.2137 -0.0271 0.2963 -0.1891 119 LYS A CD 955 C CE . LYS A 119 ? 1.4715 1.8169 1.2192 -0.0194 0.2635 -0.1888 119 LYS A CE 956 N NZ . LYS A 119 ? 1.4668 1.8237 1.2494 -0.0003 0.2550 -0.1969 119 LYS A NZ 957 N N . SER A 120 ? 1.5364 1.9258 1.1853 -0.0875 0.3879 -0.1683 120 SER A N 958 C CA . SER A 120 ? 1.5752 1.9564 1.1810 -0.0871 0.4162 -0.1728 120 SER A CA 959 C C . SER A 120 ? 1.6082 1.9515 1.1545 -0.1064 0.4201 -0.1622 120 SER A C 960 O O . SER A 120 ? 1.6855 2.0019 1.1766 -0.1042 0.4347 -0.1662 120 SER A O 961 C CB . SER A 120 ? 1.5625 2.0026 1.2126 -0.0899 0.4474 -0.1727 120 SER A CB 962 O OG . SER A 120 ? 1.5448 2.0139 1.2258 -0.1132 0.4507 -0.1581 120 SER A OG 963 N N . SER A 121 ? 1.5708 1.9097 1.1260 -0.1250 0.4066 -0.1490 121 SER A N 964 C CA . SER A 121 ? 1.5943 1.8986 1.0989 -0.1450 0.4097 -0.1368 121 SER A CA 965 C C . SER A 121 ? 1.6179 1.8583 1.0595 -0.1390 0.3882 -0.1378 121 SER A C 966 O O . SER A 121 ? 1.6272 1.8336 1.0255 -0.1543 0.3862 -0.1268 121 SER A O 967 C CB . SER A 121 ? 1.5624 1.8797 1.0983 -0.1657 0.4007 -0.1237 121 SER A CB 968 O OG . SER A 121 ? 1.5308 1.8283 1.0790 -0.1599 0.3684 -0.1241 121 SER A OG 969 N N . TRP A 122 ? 1.6101 1.8339 1.0482 -0.1176 0.3707 -0.1501 122 TRP A N 970 C CA . TRP A 122 ? 1.6450 1.8106 1.0253 -0.1107 0.3493 -0.1523 122 TRP A CA 971 C C . TRP A 122 ? 1.7183 1.8641 1.0434 -0.1023 0.3681 -0.1617 122 TRP A C 972 O O . TRP A 122 ? 1.7502 1.8941 1.0749 -0.0826 0.3659 -0.1769 122 TRP A O 973 C CB . TRP A 122 ? 1.6005 1.7574 1.0070 -0.0937 0.3182 -0.1599 122 TRP A CB 974 C CG . TRP A 122 ? 1.5332 1.7020 0.9834 -0.1014 0.2983 -0.1508 122 TRP A CG 975 C CD1 . TRP A 122 ? 1.4713 1.6821 0.9857 -0.0977 0.2941 -0.1522 122 TRP A CD1 976 C CD2 . TRP A 122 ? 1.5325 1.6701 0.9639 -0.1136 0.2802 -0.1391 122 TRP A CD2 977 N NE1 . TRP A 122 ? 1.4431 1.6510 0.9774 -0.1069 0.2756 -0.1431 122 TRP A NE1 978 C CE2 . TRP A 122 ? 1.4751 1.6386 0.9609 -0.1161 0.2671 -0.1355 122 TRP A CE2 979 C CE3 . TRP A 122 ? 1.5734 1.6629 0.9465 -0.1221 0.2733 -0.1312 122 TRP A CE3 980 C CZ2 . TRP A 122 ? 1.4601 1.6033 0.9450 -0.1255 0.2490 -0.1260 122 TRP A CZ2 981 C CZ3 . TRP A 122 ? 1.5613 1.6303 0.9362 -0.1314 0.2538 -0.1205 122 TRP A CZ3 982 C CH2 . TRP A 122 ? 1.5099 1.6059 0.9408 -0.1325 0.2426 -0.1189 122 TRP A CH2 983 N N . SER A 123 ? 1.7759 1.9052 1.0523 -0.1180 0.3864 -0.1524 123 SER A N 984 C CA . SER A 123 ? 1.8324 1.9497 1.0546 -0.1136 0.4118 -0.1597 123 SER A CA 985 C C . SER A 123 ? 1.9033 1.9583 1.0518 -0.1056 0.3926 -0.1646 123 SER A C 986 O O . SER A 123 ? 1.9570 1.9994 1.0636 -0.0943 0.4070 -0.1772 123 SER A O 987 C CB . SER A 123 ? 1.8531 1.9844 1.0571 -0.1362 0.4424 -0.1457 123 SER A CB 988 O OG . SER A 123 ? 1.8407 1.9428 1.0262 -0.1558 0.4258 -0.1278 123 SER A OG 989 N N . SER A 124 ? 1.9012 1.9175 1.0336 -0.1111 0.3601 -0.1550 124 SER A N 990 C CA . SER A 124 ? 1.9503 1.9065 1.0146 -0.1054 0.3372 -0.1571 124 SER A CA 991 C C . SER A 124 ? 1.9186 1.8592 1.0029 -0.0867 0.3029 -0.1685 124 SER A C 992 O O . SER A 124 ? 1.9492 1.8415 0.9843 -0.0812 0.2791 -0.1708 124 SER A O 993 C CB . SER A 124 ? 1.9763 1.8960 1.0056 -0.1241 0.3226 -0.1373 124 SER A CB 994 O OG . SER A 124 ? 1.9896 1.9271 1.0121 -0.1441 0.3519 -0.1242 124 SER A OG 995 N N . HIS A 125 ? 1.8524 1.8338 1.0085 -0.0780 0.2996 -0.1744 125 HIS A N 996 C CA . HIS A 125 ? 1.8168 1.7895 1.0010 -0.0620 0.2683 -0.1832 125 HIS A CA 997 C C . HIS A 125 ? 1.8002 1.8135 1.0348 -0.0465 0.2807 -0.1979 125 HIS A C 998 O O . HIS A 125 ? 1.7918 1.8513 1.0644 -0.0503 0.3075 -0.1970 125 HIS A O 999 C CB . HIS A 125 ? 1.7398 1.7183 0.9682 -0.0692 0.2433 -0.1706 125 HIS A CB 1000 C CG . HIS A 125 ? 1.7496 1.6905 0.9383 -0.0834 0.2297 -0.1554 125 HIS A CG 1001 N ND1 . HIS A 125 ? 1.7549 1.7026 0.9345 -0.1021 0.2481 -0.1420 125 HIS A ND1 1002 C CD2 . HIS A 125 ? 1.7619 1.6577 0.9201 -0.0817 0.1981 -0.1508 125 HIS A CD2 1003 C CE1 . HIS A 125 ? 1.7810 1.6871 0.9246 -0.1105 0.2287 -0.1299 125 HIS A CE1 1004 N NE2 . HIS A 125 ? 1.7883 1.6635 0.9192 -0.0980 0.1982 -0.1349 125 HIS A NE2 1005 N N . GLU A 126 ? 1.8090 1.8047 1.0460 -0.0293 0.2595 -0.2107 126 GLU A N 1006 C CA . GLU A 126 ? 1.7817 1.8111 1.0698 -0.0134 0.2656 -0.2237 126 GLU A CA 1007 C C . GLU A 126 ? 1.7055 1.7698 1.0669 -0.0162 0.2508 -0.2146 126 GLU A C 1008 O O . GLU A 126 ? 1.7058 1.7514 1.0752 -0.0182 0.2209 -0.2077 126 GLU A O 1009 C CB . GLU A 126 ? 1.8296 1.8230 1.0920 0.0049 0.2465 -0.2404 126 GLU A CB 1010 C CG . GLU A 126 ? 1.8112 1.8327 1.1224 0.0229 0.2516 -0.2547 126 GLU A CG 1011 C CD . GLU A 126 ? 1.8204 1.8806 1.1436 0.0270 0.2920 -0.2618 126 GLU A CD 1012 O OE1 . GLU A 126 ? 1.8429 1.8843 1.1104 0.0304 0.3129 -0.2717 126 GLU A OE1 1013 O OE2 . GLU A 126 ? 1.7768 1.8874 1.1656 0.0268 0.3026 -0.2573 126 GLU A OE2 1014 N N . ALA A 127 ? 1.6538 1.7700 1.0684 -0.0165 0.2721 -0.2141 127 ALA A N 1015 C CA . ALA A 127 ? 1.5591 1.7122 1.0406 -0.0211 0.2614 -0.2048 127 ALA A CA 1016 C C . ALA A 127 ? 1.5143 1.7000 1.0517 -0.0053 0.2602 -0.2136 127 ALA A C 1017 O O . ALA A 127 ? 1.4651 1.6819 1.0574 -0.0080 0.2505 -0.2062 127 ALA A O 1018 C CB . ALA A 127 ? 1.5333 1.7203 1.0329 -0.0395 0.2830 -0.1926 127 ALA A CB 1019 N N . SER A 128 ? 1.5345 1.7112 1.0563 0.0113 0.2692 -0.2293 128 SER A N 1020 C CA . SER A 128 ? 1.4959 1.7014 1.0694 0.0277 0.2700 -0.2383 128 SER A CA 1021 C C . SER A 128 ? 1.4897 1.6603 1.0572 0.0438 0.2423 -0.2487 128 SER A C 1022 O O . SER A 128 ? 1.4654 1.6520 1.0709 0.0588 0.2407 -0.2569 128 SER A O 1023 C CB . SER A 128 ? 1.5367 1.7663 1.1088 0.0362 0.3048 -0.2492 128 SER A CB 1024 O OG . SER A 128 ? 1.5528 1.8149 1.1310 0.0195 0.3301 -0.2386 128 SER A OG 1025 N N . LEU A 129 ? 1.5020 1.6249 1.0240 0.0403 0.2194 -0.2477 129 LEU A N 1026 C CA . LEU A 129 ? 1.5068 1.5939 1.0220 0.0526 0.1898 -0.2562 129 LEU A CA 1027 C C . LEU A 129 ? 1.4609 1.5411 0.9993 0.0442 0.1574 -0.2424 129 LEU A C 1028 O O . LEU A 129 ? 1.4724 1.5195 1.0012 0.0503 0.1297 -0.2462 129 LEU A O 1029 C CB . LEU A 129 ? 1.5857 1.6194 1.0254 0.0575 0.1875 -0.2689 129 LEU A CB 1030 C CG . LEU A 129 ? 1.6384 1.6738 1.0452 0.0667 0.2210 -0.2844 129 LEU A CG 1031 C CD1 . LEU A 129 ? 1.7147 1.6926 1.0415 0.0709 0.2147 -0.2969 129 LEU A CD1 1032 C CD2 . LEU A 129 ? 1.6257 1.6880 1.0799 0.0851 0.2307 -0.2970 129 LEU A CD2 1033 N N . GLY A 130 ? 1.4055 1.5174 0.9754 0.0304 0.1613 -0.2269 130 GLY A N 1034 C CA . GLY A 130 ? 1.3493 1.4609 0.9451 0.0228 0.1349 -0.2139 130 GLY A CA 1035 C C . GLY A 130 ? 1.2907 1.4322 0.9501 0.0292 0.1226 -0.2109 130 GLY A C 1036 O O . GLY A 130 ? 1.2383 1.4180 0.9411 0.0213 0.1262 -0.1999 130 GLY A O 1037 N N . VAL A 131 ? 1.2933 1.4146 0.9553 0.0428 0.1067 -0.2205 131 VAL A N 1038 C CA . VAL A 131 ? 1.2424 1.3875 0.9615 0.0503 0.0949 -0.2184 131 VAL A CA 1039 C C . VAL A 131 ? 1.2439 1.3570 0.9649 0.0546 0.0612 -0.2182 131 VAL A C 1040 O O . VAL A 131 ? 1.2885 1.3591 0.9644 0.0543 0.0472 -0.2229 131 VAL A O 1041 C CB . VAL A 131 ? 1.2506 1.4108 0.9844 0.0648 0.1131 -0.2311 131 VAL A CB 1042 C CG1 . VAL A 131 ? 1.2269 1.4308 0.9771 0.0594 0.1445 -0.2279 131 VAL A CG1 1043 C CG2 . VAL A 131 ? 1.3081 1.4242 0.9884 0.0768 0.1155 -0.2497 131 VAL A CG2 1044 N N . SER A 132 ? 1.2090 1.3432 0.9827 0.0577 0.0475 -0.2116 132 SER A N 1045 C CA . SER A 132 ? 1.2060 1.3160 0.9912 0.0599 0.0154 -0.2089 132 SER A CA 1046 C C . SER A 132 ? 1.1806 1.3094 1.0174 0.0682 0.0071 -0.2071 132 SER A C 1047 O O . SER A 132 ? 1.1380 1.3085 1.0137 0.0682 0.0217 -0.2011 132 SER A O 1048 C CB . SER A 132 ? 1.1737 1.2900 0.9710 0.0467 -0.0002 -0.1927 132 SER A CB 1049 O OG . SER A 132 ? 1.1669 1.2674 0.9842 0.0476 -0.0302 -0.1878 132 SER A OG 1050 N N . SER A 133 ? 1.2091 1.3057 1.0460 0.0744 -0.0182 -0.2114 133 SER A N 1051 C CA . SER A 133 ? 1.1982 1.3052 1.0827 0.0815 -0.0310 -0.2082 133 SER A CA 1052 C C . SER A 133 ? 1.1503 1.2938 1.0863 0.0704 -0.0415 -0.1867 133 SER A C 1053 O O . SER A 133 ? 1.1158 1.2802 1.0961 0.0738 -0.0463 -0.1798 133 SER A O 1054 C CB . SER A 133 ? 1.2416 1.2997 1.1095 0.0890 -0.0574 -0.2183 133 SER A CB 1055 O OG . SER A 133 ? 1.2513 1.2836 1.0972 0.0792 -0.0793 -0.2131 133 SER A OG 1056 N N . ALA A 134 ? 1.1606 1.3108 1.0896 0.0577 -0.0447 -0.1761 134 ALA A N 1057 C CA . ALA A 134 ? 1.1446 1.3312 1.1170 0.0471 -0.0505 -0.1570 134 ALA A CA 1058 C C . ALA A 134 ? 1.1349 1.3695 1.1345 0.0441 -0.0273 -0.1506 134 ALA A C 1059 O O . ALA A 134 ? 1.0813 1.3480 1.1225 0.0386 -0.0318 -0.1363 134 ALA A O 1060 C CB . ALA A 134 ? 1.1553 1.3339 1.1105 0.0364 -0.0585 -0.1499 134 ALA A CB 1061 N N . CYS A 135 ? 1.1718 1.4117 1.1477 0.0470 -0.0029 -0.1607 135 CYS A N 1062 C CA . CYS A 135 ? 1.1634 1.4482 1.1640 0.0436 0.0187 -0.1558 135 CYS A CA 1063 C C . CYS A 135 ? 1.1497 1.4425 1.1600 0.0567 0.0326 -0.1663 135 CYS A C 1064 O O . CYS A 135 ? 1.1282 1.4298 1.1205 0.0582 0.0559 -0.1746 135 CYS A O 1065 C CB . CYS A 135 ? 1.2225 1.5137 1.1939 0.0336 0.0372 -0.1564 135 CYS A CB 1066 S SG . CYS A 135 ? 1.3041 1.5860 1.2653 0.0204 0.0229 -0.1454 135 CYS A SG 1067 N N . PRO A 136 ? 1.1248 1.4158 1.1660 0.0662 0.0184 -0.1651 136 PRO A N 1068 C CA . PRO A 136 ? 1.1262 1.4197 1.1771 0.0816 0.0296 -0.1766 136 PRO A CA 1069 C C . PRO A 136 ? 1.0788 1.4232 1.1660 0.0803 0.0482 -0.1698 136 PRO A C 1070 O O . PRO A 136 ? 1.0223 1.3991 1.1383 0.0689 0.0443 -0.1538 136 PRO A O 1071 C CB . PRO A 136 ? 1.1417 1.4164 1.2185 0.0900 0.0045 -0.1742 136 PRO A CB 1072 C CG . PRO A 136 ? 1.0962 1.3888 1.2004 0.0759 -0.0126 -0.1539 136 PRO A CG 1073 C CD . PRO A 136 ? 1.0907 1.3793 1.1624 0.0631 -0.0078 -0.1521 136 PRO A CD 1074 N N . TYR A 137 ? 1.0907 1.4423 1.1759 0.0921 0.0683 -0.1824 137 TYR A N 1075 C CA . TYR A 137 ? 1.0530 1.4528 1.1782 0.0937 0.0840 -0.1771 137 TYR A CA 1076 C C . TYR A 137 ? 1.0688 1.4645 1.2084 0.1148 0.0913 -0.1904 137 TYR A C 1077 O O . TYR A 137 ? 1.1079 1.4837 1.2146 0.1243 0.1077 -0.2078 137 TYR A O 1078 C CB . TYR A 137 ? 1.0569 1.4819 1.1656 0.0824 0.1092 -0.1775 137 TYR A CB 1079 C CG . TYR A 137 ? 1.0365 1.5125 1.1868 0.0831 0.1254 -0.1727 137 TYR A CG 1080 C CD1 . TYR A 137 ? 0.9974 1.5104 1.1903 0.0743 0.1154 -0.1555 137 TYR A CD1 1081 C CD2 . TYR A 137 ? 1.0471 1.5358 1.1945 0.0923 0.1507 -0.1848 137 TYR A CD2 1082 C CE1 . TYR A 137 ? 0.9733 1.5332 1.2047 0.0742 0.1275 -0.1504 137 TYR A CE1 1083 C CE2 . TYR A 137 ? 1.0290 1.5673 1.2190 0.0927 0.1643 -0.1795 137 TYR A CE2 1084 C CZ . TYR A 137 ? 0.9939 1.5669 1.2259 0.0834 0.1515 -0.1622 137 TYR A CZ 1085 O OH . TYR A 137 ? 0.9713 1.5936 1.2459 0.0831 0.1624 -0.1564 137 TYR A OH 1086 N N . GLN A 138 ? 1.0408 1.4545 1.2286 0.1222 0.0792 -0.1820 138 GLN A N 1087 C CA . GLN A 138 ? 1.0680 1.4771 1.2769 0.1442 0.0828 -0.1936 138 GLN A CA 1088 C C . GLN A 138 ? 1.1085 1.4598 1.2798 0.1578 0.0744 -0.2122 138 GLN A C 1089 O O . GLN A 138 ? 1.1353 1.4737 1.2935 0.1749 0.0900 -0.2311 138 GLN A O 1090 C CB . GLN A 138 ? 1.0910 1.5362 1.3101 0.1507 0.1135 -0.2014 138 GLN A CB 1091 C CG . GLN A 138 ? 1.0613 1.5634 1.3179 0.1367 0.1205 -0.1839 138 GLN A CG 1092 C CD . GLN A 138 ? 1.0850 1.6255 1.3584 0.1428 0.1495 -0.1907 138 GLN A CD 1093 O OE1 . GLN A 138 ? 1.1230 1.6489 1.3761 0.1570 0.1681 -0.2089 138 GLN A OE1 1094 N NE2 . GLN A 138 ? 1.0588 1.6496 1.3694 0.1316 0.1535 -0.1760 138 GLN A NE2 1095 N N . GLY A 139 ? 1.1102 1.4276 1.2643 0.1497 0.0496 -0.2071 139 GLY A N 1096 C CA . GLY A 139 ? 1.1473 1.4075 1.2673 0.1599 0.0354 -0.2229 139 GLY A CA 1097 C C . GLY A 139 ? 1.1771 1.4054 1.2334 0.1575 0.0468 -0.2386 139 GLY A C 1098 O O . GLY A 139 ? 1.2175 1.3962 1.2397 0.1641 0.0333 -0.2520 139 GLY A O 1099 N N . LYS A 140 ? 1.1622 1.4170 1.2014 0.1472 0.0700 -0.2365 140 LYS A N 1100 C CA . LYS A 140 ? 1.2139 1.4414 1.1916 0.1444 0.0838 -0.2498 140 LYS A CA 1101 C C . LYS A 140 ? 1.1929 1.4217 1.1506 0.1233 0.0771 -0.2363 140 LYS A C 1102 O O . LYS A 140 ? 1.1474 1.4122 1.1391 0.1108 0.0744 -0.2185 140 LYS A O 1103 C CB . LYS A 140 ? 1.2348 1.4894 1.2052 0.1502 0.1195 -0.2596 140 LYS A CB 1104 C CG . LYS A 140 ? 1.2752 1.5301 1.2629 0.1736 0.1313 -0.2757 140 LYS A CG 1105 C CD . LYS A 140 ? 1.2801 1.5809 1.2827 0.1766 0.1663 -0.2784 140 LYS A CD 1106 C CE . LYS A 140 ? 1.3077 1.6168 1.3401 0.2013 0.1779 -0.2925 140 LYS A CE 1107 N NZ . LYS A 140 ? 1.3760 1.6388 1.3579 0.2185 0.1872 -0.3182 140 LYS A NZ 1108 N N . SER A 141 ? 1.2353 1.4241 1.1366 0.1199 0.0745 -0.2452 141 SER A N 1109 C CA . SER A 141 ? 1.2116 1.3962 1.0901 0.1018 0.0678 -0.2339 141 SER A CA 1110 C C . SER A 141 ? 1.1985 1.4197 1.0748 0.0908 0.0948 -0.2276 141 SER A C 1111 O O . SER A 141 ? 1.2363 1.4573 1.0839 0.0945 0.1195 -0.2385 141 SER A O 1112 C CB . SER A 141 ? 1.2550 1.3852 1.0724 0.1023 0.0569 -0.2452 141 SER A CB 1113 O OG . SER A 141 ? 1.2729 1.3692 1.0949 0.1087 0.0275 -0.2485 141 SER A OG 1114 N N . SER A 142 ? 1.1505 1.4027 1.0570 0.0767 0.0901 -0.2102 142 SER A N 1115 C CA . SER A 142 ? 1.1266 1.4133 1.0357 0.0641 0.1118 -0.2028 142 SER A CA 1116 C C . SER A 142 ? 1.0980 1.3763 0.9915 0.0479 0.1003 -0.1913 142 SER A C 1117 O O . SER A 142 ? 1.0927 1.3344 0.9622 0.0479 0.0803 -0.1921 142 SER A O 1118 C CB . SER A 142 ? 1.0971 1.4355 1.0638 0.0639 0.1192 -0.1938 142 SER A CB 1119 O OG . SER A 142 ? 1.0930 1.4648 1.0632 0.0514 0.1400 -0.1880 142 SER A OG 1120 N N . PHE A 143 ? 1.0733 1.3846 0.9810 0.0346 0.1124 -0.1812 143 PHE A N 1121 C CA . PHE A 143 ? 1.0704 1.3745 0.9642 0.0204 0.1040 -0.1714 143 PHE A CA 1122 C C . PHE A 143 ? 1.0450 1.3918 0.9682 0.0074 0.1148 -0.1605 143 PHE A C 1123 O O . PHE A 143 ? 1.0592 1.4395 1.0054 0.0076 0.1316 -0.1610 143 PHE A O 1124 C CB . PHE A 143 ? 1.1147 1.3832 0.9507 0.0166 0.1115 -0.1779 143 PHE A CB 1125 C CG . PHE A 143 ? 1.1195 1.3678 0.9374 0.0064 0.0966 -0.1696 143 PHE A CG 1126 C CD1 . PHE A 143 ? 1.1079 1.3347 0.9308 0.0098 0.0697 -0.1664 143 PHE A CD1 1127 C CD2 . PHE A 143 ? 1.1233 1.3740 0.9213 -0.0065 0.1089 -0.1647 143 PHE A CD2 1128 C CE1 . PHE A 143 ? 1.1110 1.3215 0.9214 0.0020 0.0562 -0.1589 143 PHE A CE1 1129 C CE2 . PHE A 143 ? 1.1319 1.3627 0.9151 -0.0140 0.0948 -0.1576 143 PHE A CE2 1130 C CZ . PHE A 143 ? 1.1207 1.3326 0.9111 -0.0090 0.0688 -0.1548 143 PHE A CZ 1131 N N . PHE A 144 ? 1.0307 1.3757 0.9534 -0.0033 0.1044 -0.1512 144 PHE A N 1132 C CA . PHE A 144 ? 0.9901 1.3682 0.9316 -0.0169 0.1135 -0.1425 144 PHE A CA 1133 C C . PHE A 144 ? 1.0012 1.3949 0.9314 -0.0228 0.1392 -0.1467 144 PHE A C 1134 O O . PHE A 144 ? 1.0555 1.4238 0.9448 -0.0254 0.1491 -0.1518 144 PHE A O 1135 C CB . PHE A 144 ? 0.9944 1.3547 0.9181 -0.0264 0.1039 -0.1367 144 PHE A CB 1136 C CG . PHE A 144 ? 0.9982 1.3490 0.9378 -0.0224 0.0800 -0.1309 144 PHE A CG 1137 C CD1 . PHE A 144 ? 0.9639 1.3464 0.9462 -0.0234 0.0724 -0.1224 144 PHE A CD1 1138 C CD2 . PHE A 144 ? 1.0305 1.3416 0.9424 -0.0185 0.0648 -0.1330 144 PHE A CD2 1139 C CE1 . PHE A 144 ? 0.9547 1.3310 0.9531 -0.0208 0.0521 -0.1158 144 PHE A CE1 1140 C CE2 . PHE A 144 ? 1.0180 1.3235 0.9487 -0.0157 0.0430 -0.1267 144 PHE A CE2 1141 C CZ . PHE A 144 ? 0.9782 1.3170 0.9528 -0.0171 0.0376 -0.1180 144 PHE A CZ 1142 N N . ARG A 145 ? 0.9698 1.4060 0.9368 -0.0259 0.1491 -0.1432 145 ARG A N 1143 C CA . ARG A 145 ? 0.9688 1.4267 0.9356 -0.0300 0.1733 -0.1467 145 ARG A CA 1144 C C . ARG A 145 ? 0.9913 1.4488 0.9356 -0.0475 0.1858 -0.1435 145 ARG A C 1145 O O . ARG A 145 ? 1.0405 1.5067 0.9740 -0.0521 0.2066 -0.1466 145 ARG A O 1146 C CB . ARG A 145 ? 0.9174 1.4231 0.9353 -0.0284 0.1769 -0.1426 145 ARG A CB 1147 C CG . ARG A 145 ? 0.9075 1.4145 0.9501 -0.0105 0.1669 -0.1457 145 ARG A CG 1148 C CD . ARG A 145 ? 0.8977 1.4501 0.9845 -0.0071 0.1771 -0.1439 145 ARG A CD 1149 N NE . ARG A 145 ? 0.8985 1.4525 1.0131 0.0103 0.1662 -0.1458 145 ARG A NE 1150 C CZ . ARG A 145 ? 0.9458 1.4789 1.0491 0.0269 0.1713 -0.1578 145 ARG A CZ 1151 N NH1 . ARG A 145 ? 0.9806 1.4898 1.0422 0.0285 0.1876 -0.1688 145 ARG A NH1 1152 N NH2 . ARG A 145 ? 0.9647 1.4989 1.0968 0.0422 0.1595 -0.1587 145 ARG A NH2 1153 N N . ASN A 146 ? 0.9965 1.4443 0.9350 -0.0571 0.1739 -0.1371 146 ASN A N 1154 C CA . ASN A 146 ? 1.0057 1.4527 0.9273 -0.0741 0.1834 -0.1336 146 ASN A CA 1155 C C . ASN A 146 ? 1.0413 1.4421 0.9126 -0.0769 0.1829 -0.1355 146 ASN A C 1156 O O . ASN A 146 ? 1.0592 1.4530 0.9113 -0.0907 0.1918 -0.1327 146 ASN A O 1157 C CB . ASN A 146 ? 0.9802 1.4459 0.9260 -0.0833 0.1727 -0.1264 146 ASN A CB 1158 C CG . ASN A 146 ? 0.9570 1.4699 0.9490 -0.0840 0.1740 -0.1228 146 ASN A CG 1159 O OD1 . ASN A 146 ? 0.9905 1.5285 0.9973 -0.0847 0.1883 -0.1244 146 ASN A OD1 1160 N ND2 . ASN A 146 ? 0.9377 1.4639 0.9529 -0.0838 0.1590 -0.1173 146 ASN A ND2 1161 N N . VAL A 147 ? 1.0550 1.4230 0.9047 -0.0644 0.1710 -0.1397 147 VAL A N 1162 C CA . VAL A 147 ? 1.1034 1.4258 0.9035 -0.0659 0.1680 -0.1410 147 VAL A CA 1163 C C . VAL A 147 ? 1.1330 1.4316 0.9034 -0.0540 0.1720 -0.1498 147 VAL A C 1164 O O . VAL A 147 ? 1.1421 1.4495 0.9318 -0.0411 0.1676 -0.1552 147 VAL A O 1165 C CB . VAL A 147 ? 1.1119 1.4103 0.9084 -0.0644 0.1446 -0.1366 147 VAL A CB 1166 C CG1 . VAL A 147 ? 1.0956 1.4126 0.9125 -0.0764 0.1439 -0.1299 147 VAL A CG1 1167 C CG2 . VAL A 147 ? 1.0962 1.3973 0.9178 -0.0509 0.1261 -0.1378 147 VAL A CG2 1168 N N . VAL A 148 ? 1.1704 1.4373 0.8920 -0.0587 0.1801 -0.1512 148 VAL A N 1169 C CA . VAL A 148 ? 1.2091 1.4519 0.8936 -0.0492 0.1875 -0.1603 148 VAL A CA 1170 C C . VAL A 148 ? 1.2351 1.4283 0.8799 -0.0437 0.1656 -0.1616 148 VAL A C 1171 O O . VAL A 148 ? 1.2638 1.4313 0.8808 -0.0526 0.1590 -0.1549 148 VAL A O 1172 C CB . VAL A 148 ? 1.2485 1.4915 0.9015 -0.0596 0.2144 -0.1602 148 VAL A CB 1173 C CG1 . VAL A 148 ? 1.3061 1.5273 0.9197 -0.0489 0.2252 -0.1710 148 VAL A CG1 1174 C CG2 . VAL A 148 ? 1.2249 1.5190 0.9205 -0.0679 0.2345 -0.1572 148 VAL A CG2 1175 N N . TRP A 149 ? 1.2446 1.4235 0.8878 -0.0290 0.1530 -0.1698 149 TRP A N 1176 C CA . TRP A 149 ? 1.2908 1.4222 0.8956 -0.0236 0.1306 -0.1720 149 TRP A CA 1177 C C . TRP A 149 ? 1.3531 1.4514 0.8960 -0.0224 0.1432 -0.1797 149 TRP A C 1178 O O . TRP A 149 ? 1.3649 1.4592 0.8963 -0.0113 0.1511 -0.1917 149 TRP A O 1179 C CB . TRP A 149 ? 1.2715 1.4008 0.9032 -0.0101 0.1092 -0.1771 149 TRP A CB 1180 C CG . TRP A 149 ? 1.2925 1.3766 0.8935 -0.0053 0.0821 -0.1786 149 TRP A CG 1181 C CD1 . TRP A 149 ? 1.3310 1.3776 0.8854 -0.0110 0.0730 -0.1750 149 TRP A CD1 1182 C CD2 . TRP A 149 ? 1.2840 1.3564 0.9018 0.0053 0.0583 -0.1828 149 TRP A CD2 1183 N NE1 . TRP A 149 ? 1.3550 1.3686 0.8965 -0.0043 0.0447 -0.1772 149 TRP A NE1 1184 C CE2 . TRP A 149 ? 1.3193 1.3479 0.8995 0.0052 0.0353 -0.1822 149 TRP A CE2 1185 C CE3 . TRP A 149 ? 1.2610 1.3548 0.9226 0.0143 0.0531 -0.1863 149 TRP A CE3 1186 C CZ2 . TRP A 149 ? 1.3223 1.3292 0.9085 0.0129 0.0075 -0.1853 149 TRP A CZ2 1187 C CZ3 . TRP A 149 ? 1.2778 1.3480 0.9442 0.0218 0.0260 -0.1890 149 TRP A CZ3 1188 C CH2 . TRP A 149 ? 1.3021 1.3299 0.9315 0.0206 0.0035 -0.1888 149 TRP A CH2 1189 N N . LEU A 150 ? 1.3853 1.4588 0.8874 -0.0336 0.1452 -0.1726 150 LEU A N 1190 C CA . LEU A 150 ? 1.4560 1.4996 0.8954 -0.0356 0.1596 -0.1770 150 LEU A CA 1191 C C . LEU A 150 ? 1.5062 1.4997 0.8993 -0.0274 0.1358 -0.1825 150 LEU A C 1192 O O . LEU A 150 ? 1.5011 1.4750 0.8989 -0.0275 0.1078 -0.1763 150 LEU A O 1193 C CB . LEU A 150 ? 1.4788 1.5157 0.8934 -0.0529 0.1710 -0.1649 150 LEU A CB 1194 C CG . LEU A 150 ? 1.4503 1.5328 0.9041 -0.0644 0.1944 -0.1589 150 LEU A CG 1195 C CD1 . LEU A 150 ? 1.4672 1.5354 0.8999 -0.0819 0.1971 -0.1459 150 LEU A CD1 1196 C CD2 . LEU A 150 ? 1.4673 1.5761 0.9200 -0.0624 0.2256 -0.1668 150 LEU A CD2 1197 N N . ILE A 151 ? 1.5514 1.5251 0.9003 -0.0201 0.1472 -0.1946 151 ILE A N 1198 C CA . ILE A 151 ? 1.5988 1.5207 0.8921 -0.0137 0.1264 -0.2013 151 ILE A CA 1199 C C . ILE A 151 ? 1.6620 1.5564 0.8829 -0.0183 0.1464 -0.2046 151 ILE A C 1200 O O . ILE A 151 ? 1.6556 1.5749 0.8742 -0.0244 0.1789 -0.2037 151 ILE A O 1201 C CB . ILE A 151 ? 1.5992 1.5156 0.9064 0.0031 0.1134 -0.2167 151 ILE A CB 1202 C CG1 . ILE A 151 ? 1.6166 1.5554 0.9261 0.0124 0.1441 -0.2309 151 ILE A CG1 1203 C CG2 . ILE A 151 ? 1.5369 1.4784 0.9127 0.0063 0.0925 -0.2114 151 ILE A CG2 1204 C CD1 . ILE A 151 ? 1.6260 1.5530 0.9434 0.0298 0.1320 -0.2476 151 ILE A CD1 1205 N N . LYS A 152 ? 1.7234 1.5673 0.8857 -0.0159 0.1263 -0.2077 152 LYS A N 1206 C CA . LYS A 152 ? 1.8011 1.6117 0.8853 -0.0208 0.1410 -0.2097 152 LYS A CA 1207 C C . LYS A 152 ? 1.8395 1.6669 0.9067 -0.0138 0.1769 -0.2247 152 LYS A C 1208 O O . LYS A 152 ? 1.8253 1.6701 0.9236 0.0006 0.1804 -0.2394 152 LYS A O 1209 C CB . LYS A 152 ? 1.8499 1.6035 0.8769 -0.0166 0.1090 -0.2137 152 LYS A CB 1210 C CG . LYS A 152 ? 1.8604 1.6005 0.8859 0.0002 0.0964 -0.2335 152 LYS A CG 1211 C CD . LYS A 152 ? 1.9139 1.5974 0.8855 0.0023 0.0606 -0.2363 152 LYS A CD 1212 C CE . LYS A 152 ? 1.9398 1.6013 0.8889 0.0175 0.0544 -0.2590 152 LYS A CE 1213 N NZ . LYS A 152 ? 1.9910 1.5989 0.8953 0.0185 0.0142 -0.2613 152 LYS A NZ 1214 N N . LYS A 153 ? 1.9001 1.7210 0.9174 -0.0239 0.2034 -0.2203 153 LYS A N 1215 C CA . LYS A 153 ? 1.9416 1.7800 0.9388 -0.0186 0.2416 -0.2331 153 LYS A CA 1216 C C . LYS A 153 ? 2.0323 1.8223 0.9359 -0.0198 0.2465 -0.2384 153 LYS A C 1217 O O . LYS A 153 ? 2.0460 1.8105 0.9036 -0.0349 0.2437 -0.2232 153 LYS A O 1218 C CB . LYS A 153 ? 1.9180 1.8046 0.9496 -0.0318 0.2753 -0.2214 153 LYS A CB 1219 C CG . LYS A 153 ? 1.9504 1.8635 0.9699 -0.0275 0.3179 -0.2323 153 LYS A CG 1220 C CD . LYS A 153 ? 1.9061 1.8798 0.9898 -0.0368 0.3448 -0.2230 153 LYS A CD 1221 C CE . LYS A 153 ? 1.9494 1.9433 1.0054 -0.0437 0.3885 -0.2232 153 LYS A CE 1222 N NZ . LYS A 153 ? 2.0057 1.9964 1.0338 -0.0246 0.4082 -0.2452 153 LYS A NZ 1223 N N . ASN A 154 ? 2.0859 1.8617 0.9603 -0.0036 0.2534 -0.2600 154 ASN A N 1224 C CA . ASN A 154 ? 2.1957 1.9214 0.9768 -0.0020 0.2549 -0.2690 154 ASN A CA 1225 C C . ASN A 154 ? 2.2307 1.9024 0.9648 -0.0103 0.2142 -0.2578 154 ASN A C 1226 O O . ASN A 154 ? 2.2789 1.9189 0.9440 -0.0222 0.2173 -0.2481 154 ASN A O 1227 C CB . ASN A 154 ? 2.2441 1.9829 0.9824 -0.0120 0.2988 -0.2648 154 ASN A CB 1228 C CG . ASN A 154 ? 2.3539 2.0496 0.9988 -0.0059 0.3092 -0.2800 154 ASN A CG 1229 O OD1 . ASN A 154 ? 2.4198 2.1015 1.0030 -0.0189 0.3294 -0.2707 154 ASN A OD1 1230 N ND2 . ASN A 154 ? 2.3822 2.0549 1.0143 0.0134 0.2951 -0.3033 154 ASN A ND2 1231 N N . SER A 155 ? 2.1927 1.8563 0.9680 -0.0044 0.1759 -0.2578 155 SER A N 1232 C CA . SER A 155 ? 2.2226 1.8376 0.9637 -0.0091 0.1329 -0.2493 155 SER A CA 1233 C C . SER A 155 ? 2.2153 1.8254 0.9531 -0.0273 0.1244 -0.2233 155 SER A C 1234 O O . SER A 155 ? 2.2836 1.8484 0.9724 -0.0329 0.0961 -0.2149 155 SER A O 1235 C CB . SER A 155 ? 2.3040 1.8635 0.9516 -0.0044 0.1253 -0.2629 155 SER A CB 1236 O OG . SER A 155 ? 2.3176 1.8787 0.9641 0.0130 0.1357 -0.2887 155 SER A OG 1237 N N . THR A 156 ? 2.1540 1.8083 0.9426 -0.0364 0.1473 -0.2109 156 THR A N 1238 C CA . THR A 156 ? 2.1458 1.7956 0.9375 -0.0531 0.1391 -0.1872 156 THR A CA 1239 C C . THR A 156 ? 2.0578 1.7588 0.9361 -0.0570 0.1465 -0.1785 156 THR A C 1240 O O . THR A 156 ? 2.0328 1.7784 0.9522 -0.0538 0.1751 -0.1859 156 THR A O 1241 C CB . THR A 156 ? 2.2048 1.8417 0.9335 -0.0682 0.1669 -0.1763 156 THR A CB 1242 O OG1 . THR A 156 ? 2.1892 1.8760 0.9524 -0.0726 0.2088 -0.1772 156 THR A OG1 1243 C CG2 . THR A 156 ? 2.3018 1.8939 0.9391 -0.0647 0.1692 -0.1867 156 THR A CG2 1244 N N . TYR A 157 ? 2.0232 1.7171 0.9277 -0.0634 0.1204 -0.1632 157 TYR A N 1245 C CA . TYR A 157 ? 1.9376 1.6738 0.9149 -0.0692 0.1260 -0.1535 157 TYR A CA 1246 C C . TYR A 157 ? 1.9480 1.6678 0.9036 -0.0864 0.1267 -0.1333 157 TYR A C 1247 O O . TYR A 157 ? 1.9411 1.6340 0.8951 -0.0883 0.0966 -0.1225 157 TYR A O 1248 C CB . TYR A 157 ? 1.8814 1.6262 0.9170 -0.0594 0.0939 -0.1551 157 TYR A CB 1249 C CG . TYR A 157 ? 1.8071 1.6024 0.9223 -0.0614 0.1022 -0.1510 157 TYR A CG 1250 C CD1 . TYR A 157 ? 1.7770 1.5802 0.9116 -0.0739 0.1035 -0.1356 157 TYR A CD1 1251 C CD2 . TYR A 157 ? 1.7511 1.5840 0.9205 -0.0506 0.1072 -0.1626 157 TYR A CD2 1252 C CE1 . TYR A 157 ? 1.7116 1.5587 0.9140 -0.0759 0.1103 -0.1331 157 TYR A CE1 1253 C CE2 . TYR A 157 ? 1.6710 1.5488 0.9088 -0.0528 0.1135 -0.1584 157 TYR A CE2 1254 C CZ . TYR A 157 ? 1.6585 1.5435 0.9114 -0.0656 0.1152 -0.1442 157 TYR A CZ 1255 O OH . TYR A 157 ? 1.5720 1.4999 0.8887 -0.0682 0.1209 -0.1411 157 TYR A OH 1256 N N . PRO A 158 ? 1.9580 1.6929 0.8969 -0.0992 0.1608 -0.1276 158 PRO A N 1257 C CA . PRO A 158 ? 1.9687 1.6859 0.8869 -0.1168 0.1620 -0.1078 158 PRO A CA 1258 C C . PRO A 158 ? 1.8903 1.6339 0.8769 -0.1215 0.1541 -0.0992 158 PRO A C 1259 O O . PRO A 158 ? 1.8272 1.6133 0.8768 -0.1143 0.1588 -0.1079 158 PRO A O 1260 C CB . PRO A 158 ? 2.0031 1.7365 0.8926 -0.1289 0.2033 -0.1059 158 PRO A CB 1261 C CG . PRO A 158 ? 1.9684 1.7493 0.9003 -0.1178 0.2260 -0.1234 158 PRO A CG 1262 C CD . PRO A 158 ? 1.9603 1.7298 0.9019 -0.0981 0.1994 -0.1386 158 PRO A CD 1263 N N . THR A 159 ? 1.8994 1.6163 0.8717 -0.1331 0.1418 -0.0823 159 THR A N 1264 C CA . THR A 159 ? 1.8343 1.5695 0.8652 -0.1368 0.1325 -0.0751 159 THR A CA 1265 C C . THR A 159 ? 1.7969 1.5827 0.8733 -0.1459 0.1642 -0.0769 159 THR A C 1266 O O . THR A 159 ? 1.8183 1.6105 0.8690 -0.1588 0.1922 -0.0726 159 THR A O 1267 C CB . THR A 159 ? 1.8619 1.5551 0.8643 -0.1480 0.1160 -0.0567 159 THR A CB 1268 O OG1 . THR A 159 ? 1.8882 1.5349 0.8479 -0.1397 0.0851 -0.0539 159 THR A OG1 1269 C CG2 . THR A 159 ? 1.8073 1.5172 0.8706 -0.1490 0.1050 -0.0520 159 THR A CG2 1270 N N . ILE A 160 ? 1.7338 1.5563 0.8778 -0.1394 0.1589 -0.0829 160 ILE A N 1271 C CA . ILE A 160 ? 1.7008 1.5729 0.8949 -0.1474 0.1833 -0.0846 160 ILE A CA 1272 C C . ILE A 160 ? 1.7090 1.5753 0.9185 -0.1621 0.1803 -0.0718 160 ILE A C 1273 O O . ILE A 160 ? 1.6942 1.5410 0.9165 -0.1576 0.1549 -0.0679 160 ILE A O 1274 C CB . ILE A 160 ? 1.6231 1.5368 0.8805 -0.1332 0.1779 -0.0971 160 ILE A CB 1275 C CG1 . ILE A 160 ? 1.6280 1.5503 0.8743 -0.1195 0.1849 -0.1109 160 ILE A CG1 1276 C CG2 . ILE A 160 ? 1.5704 1.5327 0.8818 -0.1424 0.1968 -0.0968 160 ILE A CG2 1277 C CD1 . ILE A 160 ? 1.5670 1.5178 0.8667 -0.1039 0.1724 -0.1217 160 ILE A CD1 1278 N N . LYS A 161 ? 1.7329 1.6161 0.9421 -0.1795 0.2062 -0.0656 161 LYS A N 1279 C CA . LYS A 161 ? 1.7448 1.6251 0.9722 -0.1950 0.2055 -0.0551 161 LYS A CA 1280 C C . LYS A 161 ? 1.7233 1.6557 0.9958 -0.2058 0.2309 -0.0582 161 LYS A C 1281 O O . LYS A 161 ? 1.7580 1.6982 1.0136 -0.2221 0.2551 -0.0516 161 LYS A O 1282 C CB . LYS A 161 ? 1.8293 1.6634 0.9988 -0.2109 0.2073 -0.0393 161 LYS A CB 1283 C CG . LYS A 161 ? 1.8879 1.6668 1.0137 -0.2023 0.1783 -0.0331 161 LYS A CG 1284 C CD . LYS A 161 ? 1.9668 1.7011 1.0298 -0.2189 0.1828 -0.0163 161 LYS A CD 1285 C CE . LYS A 161 ? 2.0237 1.7034 1.0376 -0.2098 0.1537 -0.0099 161 LYS A CE 1286 N NZ . LYS A 161 ? 2.1024 1.7408 1.0452 -0.2249 0.1610 0.0057 161 LYS A NZ 1287 N N . ARG A 162 ? 1.6796 1.6485 1.0096 -0.1973 0.2249 -0.0672 162 ARG A N 1288 C CA . ARG A 162 ? 1.6456 1.6657 1.0227 -0.2067 0.2448 -0.0703 162 ARG A CA 1289 C C . ARG A 162 ? 1.6206 1.6445 1.0309 -0.2158 0.2349 -0.0671 162 ARG A C 1290 O O . ARG A 162 ? 1.6239 1.6226 1.0367 -0.2080 0.2115 -0.0669 162 ARG A O 1291 C CB . ARG A 162 ? 1.5990 1.6625 1.0167 -0.1905 0.2477 -0.0835 162 ARG A CB 1292 C CG . ARG A 162 ? 1.6365 1.7035 1.0282 -0.1809 0.2617 -0.0899 162 ARG A CG 1293 C CD . ARG A 162 ? 1.6781 1.7543 1.0455 -0.1965 0.2920 -0.0842 162 ARG A CD 1294 N NE . ARG A 162 ? 1.6685 1.7806 1.0484 -0.1868 0.3127 -0.0945 162 ARG A NE 1295 C CZ . ARG A 162 ? 1.6133 1.7794 1.0461 -0.1880 0.3284 -0.0989 162 ARG A CZ 1296 N NH1 . ARG A 162 ? 1.5633 1.7548 1.0396 -0.2001 0.3260 -0.0941 162 ARG A NH1 1297 N NH2 . ARG A 162 ? 1.6130 1.8073 1.0549 -0.1765 0.3462 -0.1086 162 ARG A NH2 1298 N N . SER A 163 ? 1.5972 1.6539 1.0341 -0.2322 0.2529 -0.0651 163 SER A N 1299 C CA . SER A 163 ? 1.5550 1.6181 1.0231 -0.2426 0.2458 -0.0639 163 SER A CA 1300 C C . SER A 163 ? 1.5064 1.6273 1.0238 -0.2500 0.2614 -0.0689 163 SER A C 1301 O O . SER A 163 ? 1.4901 1.6380 1.0090 -0.2578 0.2837 -0.0673 163 SER A O 1302 C CB . SER A 163 ? 1.5991 1.6232 1.0343 -0.2629 0.2474 -0.0513 163 SER A CB 1303 O OG . SER A 163 ? 1.6135 1.6384 1.0760 -0.2724 0.2392 -0.0517 163 SER A OG 1304 N N . TYR A 164 ? 1.4713 1.6124 1.0291 -0.2467 0.2497 -0.0751 164 TYR A N 1305 C CA . TYR A 164 ? 1.4513 1.6436 1.0547 -0.2563 0.2608 -0.0784 164 TYR A CA 1306 C C . TYR A 164 ? 1.4709 1.6557 1.0873 -0.2717 0.2530 -0.0770 164 TYR A C 1307 O O . TYR A 164 ? 1.4831 1.6365 1.0917 -0.2656 0.2349 -0.0787 164 TYR A O 1308 C CB . TYR A 164 ? 1.3987 1.6306 1.0417 -0.2383 0.2555 -0.0880 164 TYR A CB 1309 C CG . TYR A 164 ? 1.3737 1.6558 1.0637 -0.2484 0.2624 -0.0904 164 TYR A CG 1310 C CD1 . TYR A 164 ? 1.3836 1.7046 1.0913 -0.2578 0.2833 -0.0884 164 TYR A CD1 1311 C CD2 . TYR A 164 ? 1.3610 1.6521 1.0772 -0.2491 0.2482 -0.0945 164 TYR A CD2 1312 C CE1 . TYR A 164 ? 1.3622 1.7298 1.1144 -0.2678 0.2874 -0.0896 164 TYR A CE1 1313 C CE2 . TYR A 164 ? 1.3406 1.6759 1.0964 -0.2594 0.2525 -0.0964 164 TYR A CE2 1314 C CZ . TYR A 164 ? 1.3464 1.7198 1.1209 -0.2689 0.2709 -0.0935 164 TYR A CZ 1315 O OH . TYR A 164 ? 1.3292 1.7472 1.1447 -0.2794 0.2727 -0.0945 164 TYR A OH 1316 N N . ASN A 165 ? 1.5042 1.7194 1.1423 -0.2913 0.2667 -0.0744 165 ASN A N 1317 C CA . ASN A 165 ? 1.5554 1.7634 1.2035 -0.3095 0.2611 -0.0734 165 ASN A CA 1318 C C . ASN A 165 ? 1.5033 1.7619 1.2002 -0.3117 0.2599 -0.0808 165 ASN A C 1319 O O . ASN A 165 ? 1.4842 1.7892 1.2081 -0.3147 0.2736 -0.0805 165 ASN A O 1320 C CB . ASN A 165 ? 1.6470 1.8450 1.2769 -0.3349 0.2768 -0.0623 165 ASN A CB 1321 C CG . ASN A 165 ? 1.7249 1.9011 1.3555 -0.3552 0.2689 -0.0604 165 ASN A CG 1322 O OD1 . ASN A 165 ? 1.6519 1.8600 1.3169 -0.3660 0.2683 -0.0650 165 ASN A OD1 1323 N ND2 . ASN A 165 ? 1.8711 1.9905 1.4625 -0.3606 0.2616 -0.0535 165 ASN A ND2 1324 N N . ASN A 166 ? 1.4673 1.7174 1.1753 -0.3097 0.2437 -0.0874 166 ASN A N 1325 C CA . ASN A 166 ? 1.4208 1.7151 1.1699 -0.3126 0.2405 -0.0942 166 ASN A CA 1326 C C . ASN A 166 ? 1.4240 1.7303 1.1844 -0.3403 0.2468 -0.0912 166 ASN A C 1327 O O . ASN A 166 ? 1.4169 1.6994 1.1712 -0.3510 0.2367 -0.0945 166 ASN A O 1328 C CB . ASN A 166 ? 1.4054 1.6873 1.1596 -0.2991 0.2219 -0.1032 166 ASN A CB 1329 C CG . ASN A 166 ? 1.3765 1.7076 1.1704 -0.2960 0.2182 -0.1095 166 ASN A CG 1330 O OD1 . ASN A 166 ? 1.3499 1.7244 1.1693 -0.2961 0.2271 -0.1074 166 ASN A OD1 1331 N ND2 . ASN A 166 ? 1.3694 1.6939 1.1683 -0.2923 0.2051 -0.1172 166 ASN A ND2 1332 N N . THR A 167 ? 1.4140 1.7573 1.1918 -0.3517 0.2635 -0.0852 167 THR A N 1333 C CA . THR A 167 ? 1.4408 1.8009 1.2336 -0.3799 0.2706 -0.0804 167 THR A CA 1334 C C . THR A 167 ? 1.4134 1.8157 1.2467 -0.3853 0.2618 -0.0873 167 THR A C 1335 O O . THR A 167 ? 1.4189 1.8142 1.2556 -0.4053 0.2549 -0.0888 167 THR A O 1336 C CB . THR A 167 ? 1.4427 1.8313 1.2428 -0.3902 0.2934 -0.0705 167 THR A CB 1337 O OG1 . THR A 167 ? 1.3928 1.8286 1.2221 -0.3724 0.3004 -0.0737 167 THR A OG1 1338 C CG2 . THR A 167 ? 1.4762 1.8197 1.2301 -0.3900 0.3024 -0.0623 167 THR A CG2 1339 N N . ASN A 168 ? 1.3598 1.8040 1.2219 -0.3680 0.2613 -0.0912 168 ASN A N 1340 C CA . ASN A 168 ? 1.3080 1.7918 1.2060 -0.3696 0.2506 -0.0971 168 ASN A CA 1341 C C . ASN A 168 ? 1.2671 1.7221 1.1518 -0.3700 0.2322 -0.1061 168 ASN A C 1342 O O . ASN A 168 ? 1.2755 1.6839 1.1287 -0.3599 0.2261 -0.1092 168 ASN A O 1343 C CB . ASN A 168 ? 1.2653 1.7905 1.1917 -0.3475 0.2511 -0.0988 168 ASN A CB 1344 C CG . ASN A 168 ? 1.2680 1.7670 1.1711 -0.3227 0.2519 -0.1000 168 ASN A CG 1345 O OD1 . ASN A 168 ? 1.2408 1.7641 1.1580 -0.3085 0.2599 -0.0986 168 ASN A OD1 1346 N ND2 . ASN A 168 ? 1.2844 1.7331 1.1528 -0.3173 0.2429 -0.1029 168 ASN A ND2 1347 N N . GLN A 169 ? 1.2342 1.7184 1.1435 -0.3815 0.2236 -0.1103 169 GLN A N 1348 C CA . GLN A 169 ? 1.2523 1.7112 1.1481 -0.3867 0.2082 -0.1200 169 GLN A CA 1349 C C . GLN A 169 ? 1.2220 1.6717 1.1108 -0.3622 0.1974 -0.1282 169 GLN A C 1350 O O . GLN A 169 ? 1.2119 1.6278 1.0801 -0.3613 0.1878 -0.1366 169 GLN A O 1351 C CB . GLN A 169 ? 1.2640 1.7590 1.1863 -0.4073 0.2015 -0.1224 169 GLN A CB 1352 C CG . GLN A 169 ? 1.3125 1.7838 1.2237 -0.4362 0.1998 -0.1225 169 GLN A CG 1353 C CD . GLN A 169 ? 1.3288 1.8236 1.2569 -0.4530 0.1863 -0.1294 169 GLN A CD 1354 O OE1 . GLN A 169 ? 1.3098 1.7760 1.2176 -0.4533 0.1738 -0.1410 169 GLN A OE1 1355 N NE2 . GLN A 169 ? 1.3268 1.8745 1.2922 -0.4660 0.1886 -0.1228 169 GLN A NE2 1356 N N . GLU A 170 ? 1.1837 1.6632 1.0906 -0.3427 0.1994 -0.1256 170 GLU A N 1357 C CA . GLU A 170 ? 1.1559 1.6379 1.0646 -0.3217 0.1893 -0.1312 170 GLU A CA 1358 C C . GLU A 170 ? 1.1583 1.6038 1.0441 -0.3009 0.1895 -0.1310 170 GLU A C 1359 O O . GLU A 170 ? 1.1904 1.6290 1.0699 -0.2956 0.1984 -0.1248 170 GLU A O 1360 C CB . GLU A 170 ? 1.1181 1.6537 1.0625 -0.3130 0.1887 -0.1275 170 GLU A CB 1361 C CG . GLU A 170 ? 1.1260 1.7042 1.0985 -0.3319 0.1868 -0.1259 170 GLU A CG 1362 C CD . GLU A 170 ? 1.1360 1.7379 1.1272 -0.3441 0.1999 -0.1177 170 GLU A CD 1363 O OE1 . GLU A 170 ? 1.1981 1.7735 1.1706 -0.3447 0.2114 -0.1143 170 GLU A OE1 1364 O OE2 . GLU A 170 ? 1.0965 1.7446 1.1214 -0.3531 0.1988 -0.1140 170 GLU A OE2 1365 N N . ASP A 171 ? 1.1607 1.5838 1.0342 -0.2894 0.1796 -0.1381 171 ASP A N 1366 C CA . ASP A 171 ? 1.1486 1.5433 1.0070 -0.2680 0.1765 -0.1378 171 ASP A CA 1367 C C . ASP A 171 ? 1.0927 1.5127 0.9673 -0.2538 0.1804 -0.1313 171 ASP A C 1368 O O . ASP A 171 ? 1.0454 1.5087 0.9481 -0.2532 0.1809 -0.1294 171 ASP A O 1369 C CB . ASP A 171 ? 1.1821 1.5719 1.0410 -0.2553 0.1661 -0.1455 171 ASP A CB 1370 C CG . ASP A 171 ? 1.2455 1.5963 1.0815 -0.2624 0.1618 -0.1542 171 ASP A CG 1371 O OD1 . ASP A 171 ? 1.3282 1.6457 1.1442 -0.2743 0.1649 -0.1530 171 ASP A OD1 1372 O OD2 . ASP A 171 ? 1.2496 1.6022 1.0872 -0.2556 0.1556 -0.1623 171 ASP A OD2 1373 N N . LEU A 172 ? 1.1063 1.4974 0.9623 -0.2420 0.1819 -0.1281 172 LEU A N 1374 C CA . LEU A 172 ? 1.0959 1.5037 0.9617 -0.2288 0.1858 -0.1233 172 LEU A CA 1375 C C . LEU A 172 ? 1.0762 1.4675 0.9376 -0.2073 0.1754 -0.1242 172 LEU A C 1376 O O . LEU A 172 ? 1.0956 1.4472 0.9336 -0.2023 0.1697 -0.1253 172 LEU A O 1377 C CB . LEU A 172 ? 1.1300 1.5206 0.9756 -0.2356 0.1980 -0.1182 172 LEU A CB 1378 C CG . LEU A 172 ? 1.1325 1.5474 0.9898 -0.2265 0.2069 -0.1148 172 LEU A CG 1379 C CD1 . LEU A 172 ? 1.1115 1.5775 1.0040 -0.2357 0.2148 -0.1135 172 LEU A CD1 1380 C CD2 . LEU A 172 ? 1.1747 1.5597 0.9999 -0.2294 0.2177 -0.1108 172 LEU A CD2 1381 N N . LEU A 173 ? 1.0273 1.4491 0.9133 -0.1951 0.1721 -0.1229 173 LEU A N 1382 C CA . LEU A 173 ? 1.0143 1.4242 0.9004 -0.1758 0.1621 -0.1224 173 LEU A CA 1383 C C . LEU A 173 ? 1.0246 1.4195 0.8969 -0.1675 0.1658 -0.1196 173 LEU A C 1384 O O . LEU A 173 ? 1.0118 1.4326 0.8998 -0.1648 0.1718 -0.1181 173 LEU A O 1385 C CB . LEU A 173 ? 0.9835 1.4313 0.9022 -0.1677 0.1555 -0.1214 173 LEU A CB 1386 C CG . LEU A 173 ? 0.9735 1.4146 0.8982 -0.1491 0.1450 -0.1192 173 LEU A CG 1387 C CD1 . LEU A 173 ? 0.9903 1.3952 0.8964 -0.1427 0.1369 -0.1211 173 LEU A CD1 1388 C CD2 . LEU A 173 ? 0.9437 1.4225 0.9007 -0.1439 0.1387 -0.1165 173 LEU A CD2 1389 N N . VAL A 174 ? 1.0502 1.4024 0.8924 -0.1627 0.1617 -0.1192 174 VAL A N 1390 C CA . VAL A 174 ? 1.0491 1.3805 0.8702 -0.1549 0.1637 -0.1172 174 VAL A CA 1391 C C . VAL A 174 ? 1.0270 1.3468 0.8512 -0.1366 0.1485 -0.1172 174 VAL A C 1392 O O . VAL A 174 ? 1.0126 1.3161 0.8363 -0.1314 0.1367 -0.1173 174 VAL A O 1393 C CB . VAL A 174 ? 1.0913 1.3802 0.8725 -0.1635 0.1678 -0.1150 174 VAL A CB 1394 C CG1 . VAL A 174 ? 1.1224 1.3915 0.8772 -0.1570 0.1716 -0.1132 174 VAL A CG1 1395 C CG2 . VAL A 174 ? 1.1046 1.4032 0.8847 -0.1838 0.1812 -0.1141 174 VAL A CG2 1396 N N . LEU A 175 ? 1.0151 1.3434 0.8436 -0.1270 0.1490 -0.1174 175 LEU A N 1397 C CA . LEU A 175 ? 1.0196 1.3374 0.8522 -0.1110 0.1340 -0.1172 175 LEU A CA 1398 C C . LEU A 175 ? 1.0501 1.3359 0.8493 -0.1049 0.1337 -0.1182 175 LEU A C 1399 O O . LEU A 175 ? 1.0827 1.3747 0.8720 -0.1075 0.1475 -0.1201 175 LEU A O 1400 C CB . LEU A 175 ? 0.9948 1.3510 0.8645 -0.1041 0.1322 -0.1173 175 LEU A CB 1401 C CG . LEU A 175 ? 0.9721 1.3620 0.8749 -0.1082 0.1297 -0.1154 175 LEU A CG 1402 C CD1 . LEU A 175 ? 0.9602 1.3911 0.8930 -0.1088 0.1359 -0.1145 175 LEU A CD1 1403 C CD2 . LEU A 175 ? 0.9457 1.3312 0.8617 -0.0984 0.1134 -0.1130 175 LEU A CD2 1404 N N . TRP A 176 ? 1.0456 1.2981 0.8275 -0.0965 0.1180 -0.1170 176 TRP A N 1405 C CA . TRP A 176 ? 1.0760 1.2962 0.8245 -0.0894 0.1135 -0.1182 176 TRP A CA 1406 C C . TRP A 176 ? 1.0703 1.2777 0.8277 -0.0760 0.0913 -0.1176 176 TRP A C 1407 O O . TRP A 176 ? 1.0385 1.2672 0.8309 -0.0723 0.0825 -0.1157 176 TRP A O 1408 C CB . TRP A 176 ? 1.1227 1.3044 0.8266 -0.0976 0.1174 -0.1156 176 TRP A CB 1409 C CG . TRP A 176 ? 1.1357 1.2919 0.8338 -0.0977 0.1032 -0.1115 176 TRP A CG 1410 C CD1 . TRP A 176 ? 1.1655 1.2857 0.8433 -0.0895 0.0848 -0.1088 176 TRP A CD1 1411 C CD2 . TRP A 176 ? 1.1237 1.2876 0.8370 -0.1056 0.1056 -0.1101 176 TRP A CD2 1412 N NE1 . TRP A 176 ? 1.1637 1.2703 0.8462 -0.0907 0.0762 -0.1054 176 TRP A NE1 1413 C CE2 . TRP A 176 ? 1.1422 1.2739 0.8450 -0.1002 0.0893 -0.1069 176 TRP A CE2 1414 C CE3 . TRP A 176 ? 1.1068 1.3010 0.8413 -0.1166 0.1191 -0.1117 176 TRP A CE3 1415 C CZ2 . TRP A 176 ? 1.1431 1.2711 0.8560 -0.1041 0.0876 -0.1065 176 TRP A CZ2 1416 C CZ3 . TRP A 176 ? 1.1085 1.2974 0.8496 -0.1219 0.1166 -0.1115 176 TRP A CZ3 1417 C CH2 . TRP A 176 ? 1.1294 1.2850 0.8596 -0.1149 0.1017 -0.1095 176 TRP A CH2 1418 N N . GLY A 177 ? 1.1208 1.2944 0.8464 -0.0694 0.0822 -0.1189 177 GLY A N 1419 C CA . GLY A 177 ? 1.1244 1.2842 0.8583 -0.0580 0.0591 -0.1179 177 GLY A CA 1420 C C . GLY A 177 ? 1.1707 1.2852 0.8604 -0.0536 0.0468 -0.1186 177 GLY A C 1421 O O . GLY A 177 ? 1.2067 1.2988 0.8549 -0.0591 0.0575 -0.1197 177 GLY A O 1422 N N . ILE A 178 ? 1.1690 1.2705 0.8675 -0.0446 0.0236 -0.1172 178 ILE A N 1423 C CA . ILE A 178 ? 1.2258 1.2839 0.8841 -0.0401 0.0070 -0.1176 178 ILE A CA 1424 C C . ILE A 178 ? 1.2349 1.2918 0.9076 -0.0303 -0.0109 -0.1211 178 ILE A C 1425 O O . ILE A 178 ? 1.1962 1.2792 0.9148 -0.0267 -0.0195 -0.1184 178 ILE A O 1426 C CB . ILE A 178 ? 1.2595 1.2919 0.9088 -0.0408 -0.0091 -0.1098 178 ILE A CB 1427 C CG1 . ILE A 178 ? 1.3302 1.3153 0.9316 -0.0377 -0.0268 -0.1092 178 ILE A CG1 1428 C CG2 . ILE A 178 ? 1.2247 1.2782 0.9239 -0.0352 -0.0249 -0.1052 178 ILE A CG2 1429 C CD1 . ILE A 178 ? 1.3675 1.3228 0.9521 -0.0392 -0.0407 -0.1008 178 ILE A CD1 1430 N N . HIS A 179 ? 1.2808 1.3064 0.9128 -0.0266 -0.0162 -0.1272 179 HIS A N 1431 C CA . HIS A 179 ? 1.2871 1.3046 0.9266 -0.0178 -0.0346 -0.1322 179 HIS A CA 1432 C C . HIS A 179 ? 1.3170 1.3004 0.9424 -0.0149 -0.0648 -0.1276 179 HIS A C 1433 O O . HIS A 179 ? 1.3631 1.3110 0.9420 -0.0173 -0.0698 -0.1263 179 HIS A O 1434 C CB . HIS A 179 ? 1.3127 1.3157 0.9158 -0.0144 -0.0226 -0.1439 179 HIS A CB 1435 C CG . HIS A 179 ? 1.3126 1.2996 0.9166 -0.0053 -0.0423 -0.1509 179 HIS A CG 1436 N ND1 . HIS A 179 ? 1.3686 1.3129 0.9201 -0.0015 -0.0521 -0.1592 179 HIS A ND1 1437 C CD2 . HIS A 179 ? 1.2837 1.2895 0.9330 -0.0001 -0.0548 -0.1509 179 HIS A CD2 1438 C CE1 . HIS A 179 ? 1.3688 1.3053 0.9338 0.0059 -0.0703 -0.1651 179 HIS A CE1 1439 N NE2 . HIS A 179 ? 1.3204 1.2938 0.9457 0.0066 -0.0724 -0.1595 179 HIS A NE2 1440 N N . HIS A 180 ? 1.2922 1.2876 0.9593 -0.0104 -0.0853 -0.1240 180 HIS A N 1441 C CA . HIS A 180 ? 1.3223 1.2902 0.9850 -0.0074 -0.1167 -0.1196 180 HIS A CA 1442 C C . HIS A 180 ? 1.3621 1.3095 1.0107 -0.0022 -0.1318 -0.1283 180 HIS A C 1443 O O . HIS A 180 ? 1.3459 1.3153 1.0340 0.0007 -0.1358 -0.1294 180 HIS A O 1444 C CB . HIS A 180 ? 1.2802 1.2770 1.0020 -0.0066 -0.1295 -0.1093 180 HIS A CB 1445 C CG . HIS A 180 ? 1.2629 1.2811 1.0021 -0.0104 -0.1143 -0.1028 180 HIS A CG 1446 N ND1 . HIS A 180 ? 1.3057 1.2993 1.0091 -0.0134 -0.1106 -0.1004 180 HIS A ND1 1447 C CD2 . HIS A 180 ? 1.2219 1.2813 1.0081 -0.0118 -0.1026 -0.0984 180 HIS A CD2 1448 C CE1 . HIS A 180 ? 1.2703 1.2877 0.9991 -0.0161 -0.0975 -0.0959 180 HIS A CE1 1449 N NE2 . HIS A 180 ? 1.2314 1.2893 1.0093 -0.0151 -0.0920 -0.0952 180 HIS A NE2 1450 N N . PRO A 181 ? 1.4219 1.3253 1.0121 -0.0013 -0.1406 -0.1346 181 PRO A N 1451 C CA . PRO A 181 ? 1.4606 1.3406 1.0323 0.0040 -0.1545 -0.1454 181 PRO A CA 1452 C C . PRO A 181 ? 1.4678 1.3355 1.0633 0.0056 -0.1913 -0.1404 181 PRO A C 1453 O O . PRO A 181 ? 1.4333 1.3058 1.0513 0.0032 -0.2068 -0.1285 181 PRO A O 1454 C CB . PRO A 181 ? 1.5320 1.3688 1.0279 0.0034 -0.1498 -0.1535 181 PRO A CB 1455 C CG . PRO A 181 ? 1.5390 1.3662 1.0172 -0.0026 -0.1504 -0.1421 181 PRO A CG 1456 C CD . PRO A 181 ? 1.4775 1.3480 1.0151 -0.0052 -0.1406 -0.1316 181 PRO A CD 1457 N N . ASN A 182 ? 1.5034 1.3555 1.0954 0.0097 -0.2051 -0.1497 182 ASN A N 1458 C CA . ASN A 182 ? 1.5150 1.3574 1.1343 0.0099 -0.2404 -0.1455 182 ASN A CA 1459 C C . ASN A 182 ? 1.5663 1.3664 1.1459 0.0080 -0.2699 -0.1430 182 ASN A C 1460 O O . ASN A 182 ? 1.5532 1.3585 1.1668 0.0058 -0.2953 -0.1313 182 ASN A O 1461 C CB . ASN A 182 ? 1.5319 1.3651 1.1551 0.0144 -0.2465 -0.1574 182 ASN A CB 1462 C CG . ASN A 182 ? 1.5438 1.3655 1.1962 0.0128 -0.2840 -0.1530 182 ASN A CG 1463 O OD1 . ASN A 182 ? 1.6010 1.3839 1.2214 0.0149 -0.3039 -0.1640 182 ASN A OD1 1464 N ND2 . ASN A 182 ? 1.5013 1.3569 1.2144 0.0088 -0.2938 -0.1371 182 ASN A ND2 1465 N N . ASP A 183 ? 1.6280 1.3877 1.1362 0.0089 -0.2662 -0.1533 183 ASP A N 1466 C CA . ASP A 183 ? 1.6854 1.3997 1.1457 0.0069 -0.2951 -0.1516 183 ASP A CA 1467 C C . ASP A 183 ? 1.7168 1.4009 1.1024 0.0054 -0.2781 -0.1561 183 ASP A C 1468 O O . ASP A 183 ? 1.6959 1.3943 1.0671 0.0059 -0.2431 -0.1616 183 ASP A O 1469 C CB . ASP A 183 ? 1.7318 1.4129 1.1772 0.0086 -0.3261 -0.1617 183 ASP A CB 1470 C CG . ASP A 183 ? 1.7627 1.4300 1.1760 0.0141 -0.3084 -0.1813 183 ASP A CG 1471 O OD1 . ASP A 183 ? 1.7833 1.4484 1.1559 0.0161 -0.2769 -0.1891 183 ASP A OD1 1472 O OD2 . ASP A 183 ? 1.7770 1.4351 1.2067 0.0165 -0.3263 -0.1891 183 ASP A OD2 1473 N N . ALA A 184 ? 1.7634 1.4063 1.1024 0.0029 -0.3037 -0.1525 184 ALA A N 1474 C CA . ALA A 184 ? 1.8078 1.4176 1.0713 0.0001 -0.2914 -0.1541 184 ALA A CA 1475 C C . ALA A 184 ? 1.8478 1.4364 1.0528 0.0030 -0.2700 -0.1730 184 ALA A C 1476 O O . ALA A 184 ? 1.8612 1.4428 1.0200 0.0006 -0.2426 -0.1748 184 ALA A O 1477 C CB . ALA A 184 ? 1.8442 1.4119 1.0701 -0.0029 -0.3285 -0.1460 184 ALA A CB 1478 N N . ALA A 185 ? 1.8677 1.4460 1.0758 0.0081 -0.2822 -0.1870 185 ALA A N 1479 C CA . ALA A 185 ? 1.9147 1.4726 1.0712 0.0134 -0.2628 -0.2073 185 ALA A CA 1480 C C . ALA A 185 ? 1.8682 1.4683 1.0525 0.0167 -0.2191 -0.2118 185 ALA A C 1481 O O . ALA A 185 ? 1.9098 1.5024 1.0461 0.0180 -0.1898 -0.2211 185 ALA A O 1482 C CB . ALA A 185 ? 1.9405 1.4758 1.0998 0.0186 -0.2894 -0.2211 185 ALA A CB 1483 N N . GLU A 186 ? 1.7910 1.4364 1.0530 0.0175 -0.2151 -0.2046 186 GLU A N 1484 C CA . GLU A 186 ? 1.7289 1.4188 1.0259 0.0197 -0.1774 -0.2062 186 GLU A CA 1485 C C . GLU A 186 ? 1.7054 1.4090 0.9840 0.0130 -0.1497 -0.1970 186 GLU A C 1486 O O . GLU A 186 ? 1.6822 1.4023 0.9492 0.0139 -0.1156 -0.2034 186 GLU A O 1487 C CB . GLU A 186 ? 1.6624 1.3956 1.0439 0.0202 -0.1839 -0.1973 186 GLU A CB 1488 C CG . GLU A 186 ? 1.6150 1.3950 1.0383 0.0226 -0.1501 -0.1987 186 GLU A CG 1489 C CD . GLU A 186 ? 1.5604 1.3760 1.0595 0.0237 -0.1607 -0.1916 186 GLU A CD 1490 O OE1 . GLU A 186 ? 1.5609 1.3636 1.0724 0.0287 -0.1795 -0.1987 186 GLU A OE1 1491 O OE2 . GLU A 186 ? 1.4970 1.3516 1.0415 0.0191 -0.1508 -0.1787 186 GLU A OE2 1492 N N . GLN A 187 ? 1.6967 1.3930 0.9746 0.0062 -0.1653 -0.1817 187 GLN A N 1493 C CA . GLN A 187 ? 1.6971 1.3990 0.9552 -0.0013 -0.1440 -0.1715 187 GLN A CA 1494 C C . GLN A 187 ? 1.7788 1.4510 0.9593 -0.0032 -0.1236 -0.1800 187 GLN A C 1495 O O . GLN A 187 ? 1.7607 1.4540 0.9361 -0.0065 -0.0891 -0.1806 187 GLN A O 1496 C CB . GLN A 187 ? 1.6898 1.3774 0.9525 -0.0062 -0.1708 -0.1551 187 GLN A CB 1497 C CG . GLN A 187 ? 1.6941 1.3755 0.9284 -0.0142 -0.1553 -0.1439 187 GLN A CG 1498 C CD . GLN A 187 ? 1.6263 1.3532 0.9046 -0.0178 -0.1236 -0.1396 187 GLN A CD 1499 O OE1 . GLN A 187 ? 1.5478 1.3123 0.8917 -0.0154 -0.1243 -0.1369 187 GLN A OE1 1500 N NE2 . GLN A 187 ? 1.6449 1.3684 0.8861 -0.0248 -0.0963 -0.1382 187 GLN A NE2 1501 N N . THR A 188 ? 1.8635 1.4877 0.9839 -0.0018 -0.1450 -0.1862 188 THR A N 1502 C CA . THR A 188 ? 1.9407 1.5331 0.9805 -0.0035 -0.1269 -0.1947 188 THR A CA 1503 C C . THR A 188 ? 1.9448 1.5519 0.9800 0.0045 -0.0973 -0.2138 188 THR A C 1504 O O . THR A 188 ? 1.9809 1.5897 0.9772 0.0024 -0.0648 -0.2181 188 THR A O 1505 C CB . THR A 188 ? 2.0250 1.5598 0.9977 -0.0038 -0.1600 -0.1975 188 THR A CB 1506 O OG1 . THR A 188 ? 2.0298 1.5525 1.0159 0.0044 -0.1847 -0.2108 188 THR A OG1 1507 C CG2 . THR A 188 ? 2.0305 1.5498 1.0061 -0.0108 -0.1894 -0.1776 188 THR A CG2 1508 N N . LYS A 189 ? 1.9126 1.5311 0.9897 0.0136 -0.1084 -0.2244 189 LYS A N 1509 C CA . LYS A 189 ? 1.9203 1.5534 1.0018 0.0234 -0.0830 -0.2427 189 LYS A CA 1510 C C . LYS A 189 ? 1.8694 1.5531 0.9883 0.0216 -0.0426 -0.2388 189 LYS A C 1511 O O . LYS A 189 ? 1.8748 1.5654 0.9705 0.0263 -0.0117 -0.2509 189 LYS A O 1512 C CB . LYS A 189 ? 1.9141 1.5519 1.0445 0.0323 -0.1061 -0.2508 189 LYS A CB 1513 C CG . LYS A 189 ? 1.9464 1.5930 1.0826 0.0446 -0.0854 -0.2707 189 LYS A CG 1514 C CD . LYS A 189 ? 1.9337 1.5928 1.1329 0.0511 -0.1073 -0.2733 189 LYS A CD 1515 C CE . LYS A 189 ? 1.9381 1.6170 1.1605 0.0636 -0.0836 -0.2891 189 LYS A CE 1516 N NZ . LYS A 189 ? 1.8745 1.5907 1.1799 0.0655 -0.0924 -0.2814 189 LYS A NZ 1517 N N . LEU A 190 ? 1.8009 1.5200 0.9774 0.0148 -0.0431 -0.2223 190 LEU A N 1518 C CA . LEU A 190 ? 1.7567 1.5249 0.9734 0.0115 -0.0089 -0.2175 190 LEU A CA 1519 C C . LEU A 190 ? 1.7708 1.5385 0.9546 -0.0008 0.0112 -0.2061 190 LEU A C 1520 O O . LEU A 190 ? 1.7492 1.5423 0.9327 -0.0036 0.0454 -0.2079 190 LEU A O 1521 C CB . LEU A 190 ? 1.6758 1.4844 0.9731 0.0105 -0.0186 -0.2069 190 LEU A CB 1522 C CG . LEU A 190 ? 1.6527 1.4696 0.9964 0.0200 -0.0387 -0.2133 190 LEU A CG 1523 C CD1 . LEU A 190 ? 1.5741 1.4417 0.9939 0.0180 -0.0335 -0.2031 190 LEU A CD1 1524 C CD2 . LEU A 190 ? 1.6913 1.4997 1.0175 0.0317 -0.0270 -0.2326 190 LEU A CD2 1525 N N . TYR A 191 ? 1.7982 1.5374 0.9572 -0.0084 -0.0108 -0.1935 191 TYR A N 1526 C CA . TYR A 191 ? 1.8037 1.5430 0.9432 -0.0211 0.0033 -0.1792 191 TYR A CA 1527 C C . TYR A 191 ? 1.9030 1.5911 0.9629 -0.0271 -0.0059 -0.1746 191 TYR A C 1528 O O . TYR A 191 ? 1.9268 1.6096 0.9685 -0.0383 0.0023 -0.1610 191 TYR A O 1529 C CB . TYR A 191 ? 1.7337 1.4933 0.9293 -0.0258 -0.0119 -0.1640 191 TYR A CB 1530 C CG . TYR A 191 ? 1.6397 1.4468 0.9121 -0.0206 -0.0082 -0.1664 191 TYR A CG 1531 C CD1 . TYR A 191 ? 1.6022 1.4508 0.9038 -0.0222 0.0239 -0.1696 191 TYR A CD1 1532 C CD2 . TYR A 191 ? 1.5902 1.4015 0.9059 -0.0147 -0.0373 -0.1645 191 TYR A CD2 1533 C CE1 . TYR A 191 ? 1.5272 1.4181 0.8961 -0.0179 0.0259 -0.1707 191 TYR A CE1 1534 C CE2 . TYR A 191 ? 1.5219 1.3758 0.9045 -0.0109 -0.0337 -0.1652 191 TYR A CE2 1535 C CZ . TYR A 191 ? 1.4848 1.3774 0.8921 -0.0124 -0.0025 -0.1682 191 TYR A CZ 1536 O OH . TYR A 191 ? 1.4181 1.3520 0.8888 -0.0091 0.0000 -0.1679 191 TYR A OH 1537 N N . ARG A 192 ? 1.9724 1.6215 0.9835 -0.0205 -0.0236 -0.1855 192 ARG A N 1538 C CA . ARG A 192 ? 2.0646 1.6614 0.9960 -0.0260 -0.0375 -0.1809 192 ARG A CA 1539 C C . ARG A 192 ? 2.0377 1.6151 0.9761 -0.0321 -0.0703 -0.1625 192 ARG A C 1540 O O . ARG A 192 ? 2.0503 1.5958 0.9735 -0.0285 -0.1065 -0.1625 192 ARG A O 1541 C CB . ARG A 192 ? 2.1459 1.7390 1.0232 -0.0350 -0.0014 -0.1786 192 ARG A CB 1542 C CG . ARG A 192 ? 2.2435 1.8165 1.0579 -0.0292 0.0163 -0.1966 192 ARG A CG 1543 C CD . ARG A 192 ? 2.3596 1.8736 1.0839 -0.0334 -0.0021 -0.1946 192 ARG A CD 1544 N NE . ARG A 192 ? 2.4525 1.9319 1.1546 -0.0233 -0.0354 -0.2083 192 ARG A NE 1545 C CZ . ARG A 192 ? 2.5109 1.9861 1.1986 -0.0115 -0.0278 -0.2310 192 ARG A CZ 1546 N NH1 . ARG A 192 ? 2.5210 2.0279 1.2187 -0.0066 0.0131 -0.2428 192 ARG A NH1 1547 N NH2 . ARG A 192 ? 2.5424 1.9814 1.2084 -0.0042 -0.0623 -0.2422 192 ARG A NH2 1548 N N . ASN A 193 ? 1.9896 1.5864 0.9525 -0.0412 -0.0577 -0.1472 193 ASN A N 1549 C CA . ASN A 193 ? 1.9773 1.5556 0.9451 -0.0466 -0.0837 -0.1292 193 ASN A CA 1550 C C . ASN A 193 ? 1.9283 1.5161 0.9554 -0.0385 -0.1178 -0.1277 193 ASN A C 1551 O O . ASN A 193 ? 1.8582 1.4867 0.9496 -0.0332 -0.1111 -0.1332 193 ASN A O 1552 C CB . ASN A 193 ? 1.9391 1.5419 0.9324 -0.0565 -0.0603 -0.1163 193 ASN A CB 1553 C CG . ASN A 193 ? 1.9847 1.5843 0.9274 -0.0664 -0.0243 -0.1161 193 ASN A CG 1554 O OD1 . ASN A 193 ? 2.0640 1.6252 0.9333 -0.0696 -0.0248 -0.1165 193 ASN A OD1 1555 N ND2 . ASN A 193 ? 1.9275 1.5682 0.9087 -0.0720 0.0069 -0.1152 193 ASN A ND2 1556 N N . PRO A 194 ? 1.9704 1.5217 0.9766 -0.0379 -0.1548 -0.1193 194 PRO A N 1557 C CA . PRO A 194 ? 1.9311 1.4931 0.9955 -0.0309 -0.1877 -0.1166 194 PRO A CA 1558 C C . PRO A 194 ? 1.8673 1.4609 0.9976 -0.0320 -0.1873 -0.1034 194 PRO A C 1559 O O . PRO A 194 ? 1.7963 1.4246 0.9939 -0.0264 -0.1928 -0.1052 194 PRO A O 1560 C CB . PRO A 194 ? 1.9974 1.5084 1.0114 -0.0310 -0.2263 -0.1115 194 PRO A CB 1561 C CG . PRO A 194 ? 2.0561 1.5339 0.9992 -0.0399 -0.2147 -0.1029 194 PRO A CG 1562 C CD . PRO A 194 ? 2.0493 1.5487 0.9774 -0.0440 -0.1688 -0.1112 194 PRO A CD 1563 N N . THR A 195 ? 1.8901 1.4702 0.9994 -0.0391 -0.1807 -0.0903 195 THR A N 1564 C CA . THR A 195 ? 1.8401 1.4448 1.0049 -0.0399 -0.1787 -0.0791 195 THR A CA 1565 C C . THR A 195 ? 1.8083 1.4388 0.9789 -0.0477 -0.1388 -0.0797 195 THR A C 1566 O O . THR A 195 ? 1.8476 1.4558 0.9644 -0.0566 -0.1226 -0.0756 195 THR A O 1567 C CB . THR A 195 ? 1.8808 1.4485 1.0231 -0.0417 -0.2043 -0.0627 195 THR A CB 1568 O OG1 . THR A 195 ? 1.9025 1.4431 1.0325 -0.0359 -0.2431 -0.0614 195 THR A OG1 1569 C CG2 . THR A 195 ? 1.8358 1.4287 1.0410 -0.0395 -0.2047 -0.0535 195 THR A CG2 1570 N N . THR A 196 ? 1.7361 1.4138 0.9716 -0.0452 -0.1238 -0.0839 196 THR A N 1571 C CA . THR A 196 ? 1.6985 1.4055 0.9452 -0.0528 -0.0872 -0.0859 196 THR A CA 1572 C C . THR A 196 ? 1.6398 1.3777 0.9467 -0.0533 -0.0829 -0.0801 196 THR A C 1573 O O . THR A 196 ? 1.5904 1.3313 0.9347 -0.0463 -0.1059 -0.0754 196 THR A O 1574 C CB . THR A 196 ? 1.6666 1.4051 0.9269 -0.0500 -0.0659 -0.1005 196 THR A CB 1575 O OG1 . THR A 196 ? 1.6068 1.3722 0.9244 -0.0405 -0.0808 -0.1054 196 THR A OG1 1576 C CG2 . THR A 196 ? 1.7268 1.4349 0.9233 -0.0493 -0.0644 -0.1086 196 THR A CG2 1577 N N . TYR A 197 ? 1.6287 1.3899 0.9442 -0.0618 -0.0529 -0.0809 197 TYR A N 1578 C CA . TYR A 197 ? 1.5895 1.3784 0.9552 -0.0637 -0.0456 -0.0773 197 TYR A CA 1579 C C . TYR A 197 ? 1.5862 1.4099 0.9656 -0.0724 -0.0120 -0.0826 197 TYR A C 1580 O O . TYR A 197 ? 1.6115 1.4347 0.9583 -0.0777 0.0068 -0.0871 197 TYR A O 1581 C CB . TYR A 197 ? 1.6204 1.3758 0.9663 -0.0685 -0.0551 -0.0649 197 TYR A CB 1582 C CG . TYR A 197 ? 1.6652 1.3938 0.9539 -0.0820 -0.0374 -0.0594 197 TYR A CG 1583 C CD1 . TYR A 197 ? 1.7367 1.4267 0.9619 -0.0842 -0.0443 -0.0565 197 TYR A CD1 1584 C CD2 . TYR A 197 ? 1.6472 1.3888 0.9440 -0.0937 -0.0138 -0.0567 197 TYR A CD2 1585 C CE1 . TYR A 197 ? 1.7827 1.4495 0.9543 -0.0976 -0.0265 -0.0501 197 TYR A CE1 1586 C CE2 . TYR A 197 ? 1.7012 1.4197 0.9479 -0.1078 0.0029 -0.0501 197 TYR A CE2 1587 C CZ . TYR A 197 ? 1.7746 1.4565 0.9587 -0.1097 -0.0026 -0.0463 197 TYR A CZ 1588 O OH . TYR A 197 ? 1.8235 1.4839 0.9569 -0.1247 0.0155 -0.0384 197 TYR A OH 1589 N N . ILE A 198 ? 1.5519 1.4069 0.9807 -0.0735 -0.0049 -0.0825 198 ILE A N 1590 C CA . ILE A 198 ? 1.5367 1.4217 0.9797 -0.0840 0.0237 -0.0850 198 ILE A CA 1591 C C . ILE A 198 ? 1.5258 1.4071 0.9863 -0.0892 0.0227 -0.0788 198 ILE A C 1592 O O . ILE A 198 ? 1.5127 1.4058 1.0129 -0.0811 0.0094 -0.0790 198 ILE A O 1593 C CB . ILE A 198 ? 1.4995 1.4346 0.9921 -0.0794 0.0339 -0.0941 198 ILE A CB 1594 C CG1 . ILE A 198 ? 1.5033 1.4403 0.9846 -0.0715 0.0314 -0.1016 198 ILE A CG1 1595 C CG2 . ILE A 198 ? 1.4897 1.4556 0.9957 -0.0912 0.0619 -0.0961 198 ILE A CG2 1596 C CD1 . ILE A 198 ? 1.4522 1.4289 0.9866 -0.0630 0.0286 -0.1078 198 ILE A CD1 1597 N N . SER A 199 ? 1.5444 1.4082 0.9752 -0.1027 0.0369 -0.0733 199 SER A N 1598 C CA . SER A 199 ? 1.5434 1.4005 0.9885 -0.1087 0.0373 -0.0686 199 SER A CA 1599 C C . SER A 199 ? 1.5051 1.3980 0.9727 -0.1209 0.0629 -0.0731 199 SER A C 1600 O O . SER A 199 ? 1.5136 1.4152 0.9613 -0.1314 0.0827 -0.0735 199 SER A O 1601 C CB . SER A 199 ? 1.6189 1.4243 1.0149 -0.1162 0.0303 -0.0571 199 SER A CB 1602 O OG . SER A 199 ? 1.6725 1.4707 1.0291 -0.1313 0.0514 -0.0538 199 SER A OG 1603 N N . VAL A 200 ? 1.4686 1.3834 0.9784 -0.1192 0.0623 -0.0767 200 VAL A N 1604 C CA . VAL A 200 ? 1.4372 1.3869 0.9716 -0.1306 0.0829 -0.0815 200 VAL A CA 1605 C C . VAL A 200 ? 1.4486 1.3803 0.9866 -0.1379 0.0816 -0.0791 200 VAL A C 1606 O O . VAL A 200 ? 1.4552 1.3724 1.0071 -0.1274 0.0651 -0.0791 200 VAL A O 1607 C CB . VAL A 200 ? 1.3918 1.3902 0.9754 -0.1220 0.0843 -0.0900 200 VAL A CB 1608 C CG1 . VAL A 200 ? 1.3710 1.4074 0.9747 -0.1347 0.1057 -0.0943 200 VAL A CG1 1609 C CG2 . VAL A 200 ? 1.3888 1.3960 0.9721 -0.1105 0.0777 -0.0923 200 VAL A CG2 1610 N N . GLY A 201 ? 1.4691 1.4018 0.9960 -0.1557 0.0988 -0.0774 201 GLY A N 1611 C CA . GLY A 201 ? 1.4896 1.4022 1.0174 -0.1649 0.0984 -0.0760 201 GLY A CA 1612 C C . GLY A 201 ? 1.4707 1.4163 1.0192 -0.1806 0.1169 -0.0812 201 GLY A C 1613 O O . GLY A 201 ? 1.4673 1.4368 1.0123 -0.1912 0.1335 -0.0804 201 GLY A O 1614 N N . THR A 202 ? 1.4756 1.4237 1.0471 -0.1813 0.1136 -0.0870 202 THR A N 1615 C CA . THR A 202 ? 1.4837 1.4525 1.0691 -0.1987 0.1274 -0.0914 202 THR A CA 1616 C C . THR A 202 ? 1.5508 1.4789 1.1258 -0.2045 0.1201 -0.0913 202 THR A C 1617 O O . THR A 202 ? 1.5988 1.4816 1.1499 -0.1983 0.1077 -0.0848 202 THR A O 1618 C CB . THR A 202 ? 1.4095 1.4303 1.0377 -0.1936 0.1313 -0.1020 202 THR A CB 1619 O OG1 . THR A 202 ? 1.3782 1.3941 1.0252 -0.1791 0.1184 -0.1086 202 THR A OG1 1620 C CG2 . THR A 202 ? 1.3694 1.4255 1.0102 -0.1845 0.1349 -0.1020 202 THR A CG2 1621 N N . SER A 203 ? 1.5706 1.5131 1.1628 -0.2162 0.1267 -0.0986 203 SER A N 1622 C CA . SER A 203 ? 1.6071 1.5125 1.1935 -0.2198 0.1193 -0.1020 203 SER A CA 1623 C C . SER A 203 ? 1.5905 1.4818 1.1898 -0.1962 0.1036 -0.1079 203 SER A C 1624 O O . SER A 203 ? 1.6344 1.4795 1.2185 -0.1915 0.0925 -0.1054 203 SER A O 1625 C CB . SER A 203 ? 1.6100 1.5394 1.2152 -0.2351 0.1282 -0.1116 203 SER A CB 1626 O OG . SER A 203 ? 1.6756 1.5671 1.2748 -0.2375 0.1207 -0.1173 203 SER A OG 1627 N N . THR A 204 ? 1.5373 1.4697 1.1664 -0.1815 0.1029 -0.1147 204 THR A N 1628 C CA . THR A 204 ? 1.5126 1.4420 1.1611 -0.1592 0.0902 -0.1203 204 THR A CA 1629 C C . THR A 204 ? 1.5065 1.4364 1.1551 -0.1427 0.0797 -0.1129 204 THR A C 1630 O O . THR A 204 ? 1.5347 1.4380 1.1834 -0.1275 0.0651 -0.1107 204 THR A O 1631 C CB . THR A 204 ? 1.4556 1.4307 1.1389 -0.1545 0.0958 -0.1327 204 THR A CB 1632 O OG1 . THR A 204 ? 1.3970 1.4186 1.0964 -0.1543 0.1022 -0.1309 204 THR A OG1 1633 C CG2 . THR A 204 ? 1.4555 1.4310 1.1372 -0.1716 0.1047 -0.1413 204 THR A CG2 1634 N N . LEU A 205 ? 1.4810 1.4407 1.1305 -0.1456 0.0862 -0.1093 205 LEU A N 1635 C CA . LEU A 205 ? 1.4525 1.4178 1.1050 -0.1306 0.0760 -0.1045 205 LEU A CA 1636 C C . LEU A 205 ? 1.4755 1.3931 1.0911 -0.1287 0.0645 -0.0937 205 LEU A C 1637 O O . LEU A 205 ? 1.4958 1.3888 1.0783 -0.1435 0.0712 -0.0873 205 LEU A O 1638 C CB . LEU A 205 ? 1.4246 1.4319 1.0866 -0.1346 0.0868 -0.1051 205 LEU A CB 1639 C CG . LEU A 205 ? 1.4264 1.4523 1.1047 -0.1184 0.0769 -0.1041 205 LEU A CG 1640 C CD1 . LEU A 205 ? 1.3831 1.4348 1.1009 -0.1055 0.0705 -0.1101 205 LEU A CD1 1641 C CD2 . LEU A 205 ? 1.4114 1.4692 1.0921 -0.1234 0.0880 -0.1043 205 LEU A CD2 1642 N N . ASN A 206 ? 1.4451 1.3507 1.0670 -0.1111 0.0468 -0.0909 206 ASN A N 1643 C CA . ASN A 206 ? 1.4634 1.3265 1.0511 -0.1075 0.0323 -0.0802 206 ASN A CA 1644 C C . ASN A 206 ? 1.4314 1.3071 1.0320 -0.0917 0.0177 -0.0788 206 ASN A C 1645 O O . ASN A 206 ? 1.4059 1.2698 1.0218 -0.0767 -0.0005 -0.0770 206 ASN A O 1646 C CB . ASN A 206 ? 1.5044 1.3216 1.0819 -0.1036 0.0195 -0.0761 206 ASN A CB 1647 C CG . ASN A 206 ? 1.5652 1.3357 1.1038 -0.1014 0.0030 -0.0632 206 ASN A CG 1648 O OD1 . ASN A 206 ? 1.5792 1.3424 1.0839 -0.1104 0.0073 -0.0569 206 ASN A OD1 1649 N ND2 . ASN A 206 ? 1.6026 1.3413 1.1456 -0.0888 -0.0162 -0.0592 206 ASN A ND2 1650 N N . GLN A 207 ? 1.4027 1.3019 0.9979 -0.0952 0.0254 -0.0796 207 GLN A N 1651 C CA . GLN A 207 ? 1.4032 1.3202 1.0146 -0.0823 0.0136 -0.0803 207 GLN A CA 1652 C C . GLN A 207 ? 1.4426 1.3274 1.0122 -0.0816 0.0026 -0.0732 207 GLN A C 1653 O O . GLN A 207 ? 1.4658 1.3298 0.9946 -0.0937 0.0125 -0.0693 207 GLN A O 1654 C CB . GLN A 207 ? 1.3664 1.3329 1.0042 -0.0852 0.0290 -0.0877 207 GLN A CB 1655 C CG . GLN A 207 ? 1.3493 1.3374 1.0080 -0.0734 0.0183 -0.0889 207 GLN A CG 1656 C CD . GLN A 207 ? 1.3218 1.3568 1.0073 -0.0766 0.0334 -0.0951 207 GLN A CD 1657 O OE1 . GLN A 207 ? 1.3527 1.3951 1.0255 -0.0788 0.0392 -0.0963 207 GLN A OE1 1658 N NE2 . GLN A 207 ? 1.2892 1.3552 1.0103 -0.0767 0.0399 -0.0993 207 GLN A NE2 1659 N N . ARG A 208 ? 1.4541 1.3353 1.0334 -0.0682 -0.0180 -0.0713 208 ARG A N 1660 C CA . ARG A 208 ? 1.5170 1.3730 1.0587 -0.0666 -0.0298 -0.0670 208 ARG A CA 1661 C C . ARG A 208 ? 1.4966 1.3756 1.0677 -0.0545 -0.0439 -0.0705 208 ARG A C 1662 O O . ARG A 208 ? 1.4929 1.3709 1.0912 -0.0432 -0.0639 -0.0677 208 ARG A O 1663 C CB . ARG A 208 ? 1.5988 1.4030 1.1052 -0.0648 -0.0494 -0.0566 208 ARG A CB 1664 C CG . ARG A 208 ? 1.6734 1.4461 1.1271 -0.0671 -0.0583 -0.0519 208 ARG A CG 1665 C CD . ARG A 208 ? 1.7492 1.4710 1.1702 -0.0644 -0.0820 -0.0401 208 ARG A CD 1666 N NE . ARG A 208 ? 1.8260 1.5142 1.1867 -0.0694 -0.0880 -0.0352 208 ARG A NE 1667 C CZ . ARG A 208 ? 1.8841 1.5533 1.1951 -0.0836 -0.0701 -0.0317 208 ARG A CZ 1668 N NH1 . ARG A 208 ? 1.8823 1.5628 1.1985 -0.0954 -0.0459 -0.0320 208 ARG A NH1 1669 N NH2 . ARG A 208 ? 1.9367 1.5758 1.1915 -0.0867 -0.0762 -0.0278 208 ARG A NH2 1670 N N . LEU A 209 ? 1.4838 1.3840 1.0517 -0.0570 -0.0333 -0.0764 209 LEU A N 1671 C CA . LEU A 209 ? 1.4662 1.3870 1.0608 -0.0473 -0.0457 -0.0799 209 LEU A CA 1672 C C . LEU A 209 ? 1.5033 1.3889 1.0566 -0.0442 -0.0637 -0.0778 209 LEU A C 1673 O O . LEU A 209 ? 1.5385 1.3986 1.0416 -0.0514 -0.0552 -0.0775 209 LEU A O 1674 C CB . LEU A 209 ? 1.4408 1.4027 1.0565 -0.0506 -0.0255 -0.0879 209 LEU A CB 1675 C CG . LEU A 209 ? 1.4073 1.4053 1.0569 -0.0562 -0.0059 -0.0907 209 LEU A CG 1676 C CD1 . LEU A 209 ? 1.3877 1.4203 1.0485 -0.0607 0.0132 -0.0971 209 LEU A CD1 1677 C CD2 . LEU A 209 ? 1.3744 1.3945 1.0728 -0.0478 -0.0163 -0.0897 209 LEU A CD2 1678 N N . VAL A 210 ? 1.5028 1.3871 1.0767 -0.0341 -0.0884 -0.0762 210 VAL A N 1679 C CA . VAL A 210 ? 1.5637 1.4178 1.1021 -0.0310 -0.1079 -0.0762 210 VAL A CA 1680 C C . VAL A 210 ? 1.5395 1.4198 1.1119 -0.0246 -0.1162 -0.0821 210 VAL A C 1681 O O . VAL A 210 ? 1.4928 1.4044 1.1198 -0.0195 -0.1215 -0.0806 210 VAL A O 1682 C CB . VAL A 210 ? 1.6054 1.4212 1.1278 -0.0262 -0.1373 -0.0665 210 VAL A CB 1683 C CG1 . VAL A 210 ? 1.6426 1.4244 1.1214 -0.0335 -0.1303 -0.0597 210 VAL A CG1 1684 C CG2 . VAL A 210 ? 1.5763 1.4135 1.1583 -0.0169 -0.1535 -0.0619 210 VAL A CG2 1685 N N . PRO A 211 ? 1.5649 1.4321 1.1045 -0.0250 -0.1164 -0.0889 211 PRO A N 1686 C CA . PRO A 211 ? 1.5416 1.4277 1.1115 -0.0190 -0.1270 -0.0944 211 PRO A CA 1687 C C . PRO A 211 ? 1.5371 1.4131 1.1297 -0.0124 -0.1611 -0.0882 211 PRO A C 1688 O O . PRO A 211 ? 1.5634 1.4057 1.1299 -0.0116 -0.1805 -0.0817 211 PRO A O 1689 C CB . PRO A 211 ? 1.5786 1.4418 1.0979 -0.0201 -0.1215 -0.1038 211 PRO A CB 1690 C CG . PRO A 211 ? 1.6052 1.4564 1.0814 -0.0281 -0.0968 -0.1039 211 PRO A CG 1691 C CD . PRO A 211 ? 1.6121 1.4499 1.0879 -0.0311 -0.1037 -0.0927 211 PRO A CD 1692 N N . ARG A 212 ? 1.4917 1.3975 1.1340 -0.0084 -0.1687 -0.0894 212 ARG A N 1693 C CA . ARG A 212 ? 1.4983 1.4052 1.1756 -0.0032 -0.1989 -0.0825 212 ARG A CA 1694 C C . ARG A 212 ? 1.5253 1.4257 1.2024 -0.0015 -0.2153 -0.0883 212 ARG A C 1695 O O . ARG A 212 ? 1.4932 1.4232 1.2023 -0.0013 -0.2054 -0.0924 212 ARG A O 1696 C CB . ARG A 212 ? 1.4458 1.3978 1.1893 -0.0010 -0.1923 -0.0764 212 ARG A CB 1697 C CG . ARG A 212 ? 1.4576 1.4046 1.2090 0.0013 -0.1952 -0.0684 212 ARG A CG 1698 C CD . ARG A 212 ? 1.4147 1.3999 1.2051 0.0011 -0.1718 -0.0676 212 ARG A CD 1699 N NE . ARG A 212 ? 1.3665 1.3966 1.2060 0.0013 -0.1632 -0.0689 212 ARG A NE 1700 C CZ . ARG A 212 ? 1.3433 1.4034 1.1942 -0.0029 -0.1369 -0.0735 212 ARG A CZ 1701 N NH1 . ARG A 212 ? 1.3453 1.3976 1.1652 -0.0082 -0.1153 -0.0780 212 ARG A NH1 1702 N NH2 . ARG A 212 ? 1.3311 1.4297 1.2258 -0.0028 -0.1329 -0.0727 212 ARG A NH2 1703 N N . ILE A 213 ? 1.6141 1.4733 1.2527 -0.0007 -0.2412 -0.0888 213 ILE A N 1704 C CA . ILE A 213 ? 1.6537 1.4982 1.2849 0.0005 -0.2603 -0.0957 213 ILE A CA 1705 C C . ILE A 213 ? 1.6545 1.5216 1.3483 0.0025 -0.2852 -0.0877 213 ILE A C 1706 O O . ILE A 213 ? 1.6793 1.5521 1.4005 0.0040 -0.3005 -0.0767 213 ILE A O 1707 C CB . ILE A 213 ? 1.7148 1.5045 1.2784 -0.0001 -0.2816 -0.0995 213 ILE A CB 1708 C CG1 . ILE A 213 ? 1.7525 1.5185 1.2514 -0.0032 -0.2575 -0.1043 213 ILE A CG1 1709 C CG2 . ILE A 213 ? 1.7370 1.5096 1.2888 0.0012 -0.2983 -0.1099 213 ILE A CG2 1710 C CD1 . ILE A 213 ? 1.7236 1.5117 1.2188 -0.0041 -0.2214 -0.1146 213 ILE A CD1 1711 N N . ALA A 214 ? 1.6559 1.5360 1.3738 0.0025 -0.2888 -0.0928 214 ALA A N 1712 C CA . ALA A 214 ? 1.6418 1.5452 1.4209 0.0025 -0.3111 -0.0844 214 ALA A CA 1713 C C . ALA A 214 ? 1.6590 1.5649 1.4493 0.0016 -0.3148 -0.0920 214 ALA A C 1714 O O . ALA A 214 ? 1.6287 1.5466 1.4127 0.0023 -0.2894 -0.1001 214 ALA A O 1715 C CB . ALA A 214 ? 1.5808 1.5339 1.4207 0.0029 -0.2954 -0.0739 214 ALA A CB 1716 N N . THR A 215 ? 1.6943 1.5878 1.5025 0.0000 -0.3479 -0.0890 215 THR A N 1717 C CA . THR A 215 ? 1.6877 1.5857 1.5189 -0.0015 -0.3557 -0.0934 215 THR A CA 1718 C C . THR A 215 ? 1.5980 1.5509 1.4968 -0.0030 -0.3385 -0.0834 215 THR A C 1719 O O . THR A 215 ? 1.5785 1.5612 1.5251 -0.0046 -0.3443 -0.0698 215 THR A O 1720 C CB . THR A 215 ? 1.7373 1.6109 1.5777 -0.0049 -0.3978 -0.0904 215 THR A CB 1721 O OG1 . THR A 215 ? 1.8087 1.6289 1.5801 -0.0038 -0.4142 -0.1004 215 THR A OG1 1722 C CG2 . THR A 215 ? 1.7459 1.6232 1.6145 -0.0074 -0.4069 -0.0938 215 THR A CG2 1723 N N . ARG A 216 ? 1.5426 1.5091 1.4445 -0.0021 -0.3171 -0.0902 216 ARG A N 1724 C CA . ARG A 216 ? 1.4622 1.4795 1.4202 -0.0039 -0.2982 -0.0811 216 ARG A CA 1725 C C . ARG A 216 ? 1.4464 1.4685 1.4268 -0.0050 -0.3022 -0.0834 216 ARG A C 1726 O O . ARG A 216 ? 1.4745 1.4612 1.4196 -0.0024 -0.3098 -0.0962 216 ARG A O 1727 C CB . ARG A 216 ? 1.4307 1.4675 1.3727 -0.0017 -0.2619 -0.0850 216 ARG A CB 1728 C CG . ARG A 216 ? 1.4110 1.4524 1.3446 -0.0013 -0.2544 -0.0799 216 ARG A CG 1729 C CD . ARG A 216 ? 1.3869 1.4402 1.2975 -0.0006 -0.2202 -0.0857 216 ARG A CD 1730 N NE . ARG A 216 ? 1.4242 1.4410 1.2737 0.0013 -0.2128 -0.0991 216 ARG A NE 1731 C CZ . ARG A 216 ? 1.4377 1.4252 1.2375 0.0015 -0.2095 -0.1029 216 ARG A CZ 1732 N NH1 . ARG A 216 ? 1.4244 1.4115 1.2274 0.0007 -0.2142 -0.0945 216 ARG A NH1 1733 N NH2 . ARG A 216 ? 1.4742 1.4321 1.2202 0.0028 -0.2006 -0.1149 216 ARG A NH2 1734 N N . SER A 217 ? 1.4156 1.4810 1.4540 -0.0088 -0.2965 -0.0708 217 SER A N 1735 C CA . SER A 217 ? 1.4134 1.4884 1.4781 -0.0103 -0.2974 -0.0700 217 SER A CA 1736 C C . SER A 217 ? 1.4050 1.4756 1.4385 -0.0046 -0.2715 -0.0832 217 SER A C 1737 O O . SER A 217 ? 1.3735 1.4517 1.3817 -0.0018 -0.2470 -0.0880 217 SER A O 1738 C CB . SER A 217 ? 1.3805 1.5069 1.5097 -0.0161 -0.2917 -0.0520 217 SER A CB 1739 O OG . SER A 217 ? 1.4064 1.5426 1.5693 -0.0209 -0.3128 -0.0393 217 SER A OG 1740 N N . LYS A 218 ? 1.4068 1.4649 1.4441 -0.0028 -0.2775 -0.0886 218 LYS A N 1741 C CA . LYS A 218 ? 1.3755 1.4348 1.3935 0.0037 -0.2533 -0.0998 218 LYS A CA 1742 C C . LYS A 218 ? 1.3292 1.4395 1.3925 0.0009 -0.2332 -0.0876 218 LYS A C 1743 O O . LYS A 218 ? 1.3265 1.4602 1.4378 -0.0050 -0.2441 -0.0730 218 LYS A O 1744 C CB . LYS A 218 ? 1.3895 1.4131 1.3936 0.0087 -0.2677 -0.1118 218 LYS A CB 1745 C CG . LYS A 218 ? 1.4342 1.4052 1.3762 0.0141 -0.2775 -0.1298 218 LYS A CG 1746 C CD . LYS A 218 ? 1.4629 1.4017 1.3838 0.0224 -0.2804 -0.1463 218 LYS A CD 1747 C CE . LYS A 218 ? 1.5316 1.4170 1.3857 0.0274 -0.2897 -0.1651 218 LYS A CE 1748 N NZ . LYS A 218 ? 1.5763 1.4310 1.4037 0.0380 -0.2859 -0.1845 218 LYS A NZ 1749 N N . VAL A 219 ? 1.2965 1.4238 1.3432 0.0042 -0.2042 -0.0931 219 VAL A N 1750 C CA . VAL A 219 ? 1.2268 1.4003 1.3088 0.0017 -0.1841 -0.0836 219 VAL A CA 1751 C C . VAL A 219 ? 1.2197 1.3910 1.2805 0.0088 -0.1637 -0.0960 219 VAL A C 1752 O O . VAL A 219 ? 1.2385 1.3945 1.2576 0.0127 -0.1491 -0.1082 219 VAL A O 1753 C CB . VAL A 219 ? 1.2068 1.4108 1.2950 -0.0033 -0.1683 -0.0759 219 VAL A CB 1754 C CG1 . VAL A 219 ? 1.1678 1.4183 1.2890 -0.0067 -0.1489 -0.0667 219 VAL A CG1 1755 C CG2 . VAL A 219 ? 1.2007 1.4058 1.3093 -0.0081 -0.1878 -0.0651 219 VAL A CG2 1756 N N . ASN A 220 ? 1.1999 1.3864 1.2907 0.0106 -0.1631 -0.0921 220 ASN A N 1757 C CA . ASN A 220 ? 1.2197 1.4014 1.2966 0.0196 -0.1480 -0.1042 220 ASN A CA 1758 C C . ASN A 220 ? 1.2432 1.3762 1.2708 0.0284 -0.1526 -0.1240 220 ASN A C 1759 O O . ASN A 220 ? 1.2650 1.3934 1.2640 0.0354 -0.1324 -0.1370 220 ASN A O 1760 C CB . ASN A 220 ? 1.2290 1.4455 1.3033 0.0185 -0.1184 -0.1041 220 ASN A CB 1761 C CG . ASN A 220 ? 1.2133 1.4751 1.3273 0.0092 -0.1135 -0.0863 220 ASN A CG 1762 O OD1 . ASN A 220 ? 1.2004 1.4808 1.3070 0.0039 -0.0995 -0.0839 220 ASN A OD1 1763 N ND2 . ASN A 220 ? 1.2038 1.4819 1.3585 0.0069 -0.1251 -0.0737 220 ASN A ND2 1764 N N . GLY A 221 ? 1.2415 1.3391 1.2593 0.0275 -0.1792 -0.1259 221 GLY A N 1765 C CA . GLY A 221 ? 1.2749 1.3223 1.2433 0.0350 -0.1876 -0.1446 221 GLY A CA 1766 C C . GLY A 221 ? 1.2807 1.3086 1.1975 0.0342 -0.1803 -0.1527 221 GLY A C 1767 O O . GLY A 221 ? 1.3336 1.3208 1.2024 0.0404 -0.1836 -0.1689 221 GLY A O 1768 N N . GLN A 222 ? 1.2364 1.2906 1.1605 0.0267 -0.1710 -0.1417 222 GLN A N 1769 C CA . GLN A 222 ? 1.2648 1.3015 1.1409 0.0255 -0.1623 -0.1476 222 GLN A CA 1770 C C . GLN A 222 ? 1.2655 1.2940 1.1436 0.0185 -0.1830 -0.1374 222 GLN A C 1771 O O . GLN A 222 ? 1.2151 1.2735 1.1391 0.0127 -0.1898 -0.1224 222 GLN A O 1772 C CB . GLN A 222 ? 1.2457 1.3156 1.1206 0.0238 -0.1300 -0.1460 222 GLN A CB 1773 C CG . GLN A 222 ? 1.2527 1.3357 1.1288 0.0308 -0.1078 -0.1553 222 GLN A CG 1774 C CD . GLN A 222 ? 1.3077 1.3498 1.1378 0.0405 -0.1076 -0.1740 222 GLN A CD 1775 O OE1 . GLN A 222 ? 1.3341 1.3413 1.1147 0.0404 -0.1121 -0.1816 222 GLN A OE1 1776 N NE2 . GLN A 222 ? 1.3163 1.3617 1.1615 0.0494 -0.1023 -0.1817 222 GLN A NE2 1777 N N . ASN A 223 ? 1.3175 1.3060 1.1450 0.0195 -0.1926 -0.1456 223 ASN A N 1778 C CA . ASN A 223 ? 1.3429 1.3199 1.1654 0.0142 -0.2119 -0.1370 223 ASN A CA 1779 C C . ASN A 223 ? 1.3237 1.3155 1.1316 0.0112 -0.1912 -0.1325 223 ASN A C 1780 O O . ASN A 223 ? 1.3082 1.3157 1.1399 0.0069 -0.1978 -0.1205 223 ASN A O 1781 C CB . ASN A 223 ? 1.4199 1.3432 1.1911 0.0163 -0.2350 -0.1474 223 ASN A CB 1782 C CG . ASN A 223 ? 1.4585 1.3612 1.2437 0.0179 -0.2615 -0.1516 223 ASN A CG 1783 O OD1 . ASN A 223 ? 1.4655 1.3768 1.2922 0.0127 -0.2856 -0.1399 223 ASN A OD1 1784 N ND2 . ASN A 223 ? 1.4985 1.3732 1.2496 0.0250 -0.2570 -0.1686 223 ASN A ND2 1785 N N . GLY A 224 ? 1.3358 1.3216 1.1048 0.0136 -0.1661 -0.1426 224 GLY A N 1786 C CA . GLY A 224 ? 1.3174 1.3152 1.0704 0.0096 -0.1447 -0.1391 224 GLY A CA 1787 C C . GLY A 224 ? 1.2464 1.2934 1.0506 0.0056 -0.1297 -0.1282 224 GLY A C 1788 O O . GLY A 224 ? 1.2079 1.2826 1.0555 0.0064 -0.1297 -0.1247 224 GLY A O 1789 N N . ARG A 225 ? 1.2363 1.2918 1.0331 0.0011 -0.1176 -0.1230 225 ARG A N 1790 C CA . ARG A 225 ? 1.1899 1.2888 1.0269 -0.0031 -0.1016 -0.1147 225 ARG A CA 1791 C C . ARG A 225 ? 1.1894 1.2936 1.0000 -0.0072 -0.0745 -0.1182 225 ARG A C 1792 O O . ARG A 225 ? 1.2360 1.3090 0.9991 -0.0080 -0.0714 -0.1229 225 ARG A O 1793 C CB . ARG A 225 ? 1.1636 1.2707 1.0286 -0.0050 -0.1168 -0.1033 225 ARG A CB 1794 C CG . ARG A 225 ? 1.1622 1.2730 1.0640 -0.0031 -0.1425 -0.0968 225 ARG A CG 1795 C CD . ARG A 225 ? 1.1342 1.2865 1.0857 -0.0045 -0.1354 -0.0912 225 ARG A CD 1796 N NE . ARG A 225 ? 1.1471 1.3048 1.1367 -0.0047 -0.1596 -0.0827 225 ARG A NE 1797 C CZ . ARG A 225 ? 1.1665 1.3056 1.1570 -0.0029 -0.1773 -0.0856 225 ARG A CZ 1798 N NH1 . ARG A 225 ? 1.1946 1.3078 1.1487 0.0011 -0.1727 -0.0984 225 ARG A NH1 1799 N NH2 . ARG A 225 ? 1.1646 1.3110 1.1937 -0.0051 -0.1994 -0.0759 225 ARG A NH2 1800 N N . MET A 226 ? 1.1636 1.3070 1.0047 -0.0107 -0.0557 -0.1153 226 MET A N 1801 C CA . MET A 226 ? 1.1762 1.3299 1.0009 -0.0166 -0.0313 -0.1171 226 MET A CA 1802 C C . MET A 226 ? 1.1446 1.3239 0.9991 -0.0215 -0.0280 -0.1088 226 MET A C 1803 O O . MET A 226 ? 1.1180 1.3295 1.0151 -0.0214 -0.0299 -0.1035 226 MET A O 1804 C CB . MET A 226 ? 1.1957 1.3744 1.0291 -0.0169 -0.0110 -0.1225 226 MET A CB 1805 C CG . MET A 226 ? 1.2641 1.4200 1.0689 -0.0104 -0.0099 -0.1328 226 MET A CG 1806 S SD . MET A 226 ? 1.3623 1.4874 1.1044 -0.0136 0.0072 -0.1405 226 MET A SD 1807 C CE . MET A 226 ? 1.3970 1.5059 1.1188 -0.0032 0.0096 -0.1540 226 MET A CE 1808 N N . GLU A 227 ? 1.1596 1.3232 0.9902 -0.0256 -0.0231 -0.1077 227 GLU A N 1809 C CA . GLU A 227 ? 1.1170 1.2999 0.9699 -0.0295 -0.0181 -0.1023 227 GLU A CA 1810 C C . GLU A 227 ? 1.1077 1.3003 0.9453 -0.0379 0.0059 -0.1057 227 GLU A C 1811 O O . GLU A 227 ? 1.1655 1.3314 0.9630 -0.0415 0.0128 -0.1087 227 GLU A O 1812 C CB . GLU A 227 ? 1.1554 1.3091 0.9953 -0.0269 -0.0341 -0.0982 227 GLU A CB 1813 C CG . GLU A 227 ? 1.1621 1.3356 1.0338 -0.0268 -0.0341 -0.0930 227 GLU A CG 1814 C CD . GLU A 227 ? 1.1977 1.3473 1.0697 -0.0207 -0.0550 -0.0879 227 GLU A CD 1815 O OE1 . GLU A 227 ? 1.2315 1.3456 1.0730 -0.0182 -0.0699 -0.0879 227 GLU A OE1 1816 O OE2 . GLU A 227 ? 1.2156 1.3823 1.1184 -0.0180 -0.0568 -0.0838 227 GLU A OE2 1817 N N . PHE A 228 ? 1.0526 1.2833 0.9211 -0.0421 0.0183 -0.1047 228 PHE A N 1818 C CA . PHE A 228 ? 1.0327 1.2765 0.8914 -0.0515 0.0398 -0.1078 228 PHE A CA 1819 C C . PHE A 228 ? 1.0112 1.2577 0.8736 -0.0571 0.0443 -0.1061 228 PHE A C 1820 O O . PHE A 228 ? 0.9829 1.2402 0.8707 -0.0532 0.0356 -0.1027 228 PHE A O 1821 C CB . PHE A 228 ? 1.0141 1.2970 0.9009 -0.0532 0.0502 -0.1087 228 PHE A CB 1822 C CG . PHE A 228 ? 1.0396 1.3178 0.9210 -0.0471 0.0485 -0.1122 228 PHE A CG 1823 C CD1 . PHE A 228 ? 1.0651 1.3348 0.9195 -0.0496 0.0633 -0.1180 228 PHE A CD1 1824 C CD2 . PHE A 228 ? 1.0443 1.3250 0.9473 -0.0386 0.0325 -0.1101 228 PHE A CD2 1825 C CE1 . PHE A 228 ? 1.0843 1.3484 0.9326 -0.0422 0.0630 -0.1232 228 PHE A CE1 1826 C CE2 . PHE A 228 ? 1.0637 1.3360 0.9605 -0.0321 0.0302 -0.1149 228 PHE A CE2 1827 C CZ . PHE A 228 ? 1.0778 1.3414 0.9464 -0.0329 0.0459 -0.1223 228 PHE A CZ 1828 N N . PHE A 229 ? 1.0011 1.2370 0.8380 -0.0663 0.0583 -0.1087 229 PHE A N 1829 C CA . PHE A 229 ? 0.9950 1.2265 0.8296 -0.0724 0.0631 -0.1086 229 PHE A CA 1830 C C . PHE A 229 ? 1.0048 1.2578 0.8398 -0.0850 0.0821 -0.1115 229 PHE A C 1831 O O . PHE A 229 ? 1.0117 1.2781 0.8439 -0.0887 0.0922 -0.1129 229 PHE A O 1832 C CB . PHE A 229 ? 1.0335 1.2193 0.8314 -0.0725 0.0568 -0.1072 229 PHE A CB 1833 C CG . PHE A 229 ? 1.0462 1.2101 0.8446 -0.0608 0.0356 -0.1036 229 PHE A CG 1834 C CD1 . PHE A 229 ? 1.0666 1.2158 0.8507 -0.0551 0.0256 -0.1032 229 PHE A CD1 1835 C CD2 . PHE A 229 ? 1.0498 1.2086 0.8645 -0.0551 0.0253 -0.1012 229 PHE A CD2 1836 C CE1 . PHE A 229 ? 1.0763 1.2057 0.8622 -0.0456 0.0038 -0.0996 229 PHE A CE1 1837 C CE2 . PHE A 229 ? 1.0657 1.2078 0.8859 -0.0446 0.0046 -0.0970 229 PHE A CE2 1838 C CZ . PHE A 229 ? 1.0725 1.1997 0.8783 -0.0406 -0.0071 -0.0958 229 PHE A CZ 1839 N N . TRP A 230 ? 1.0170 1.2734 0.8565 -0.0913 0.0867 -0.1129 230 TRP A N 1840 C CA . TRP A 230 ? 1.0076 1.2833 0.8481 -0.1049 0.1024 -0.1157 230 TRP A CA 1841 C C . TRP A 230 ? 1.0276 1.2818 0.8526 -0.1129 0.1055 -0.1180 230 TRP A C 1842 O O . TRP A 230 ? 1.0347 1.2641 0.8543 -0.1059 0.0957 -0.1177 230 TRP A O 1843 C CB . TRP A 230 ? 0.9712 1.2924 0.8476 -0.1054 0.1052 -0.1162 230 TRP A CB 1844 C CG . TRP A 230 ? 0.9489 1.2800 0.8462 -0.0992 0.0973 -0.1163 230 TRP A CG 1845 C CD1 . TRP A 230 ? 0.9345 1.2711 0.8511 -0.0870 0.0852 -0.1126 230 TRP A CD1 1846 C CD2 . TRP A 230 ? 0.9372 1.2750 0.8384 -0.1052 0.1020 -0.1205 230 TRP A CD2 1847 N NE1 . TRP A 230 ? 0.9115 1.2603 0.8448 -0.0847 0.0838 -0.1137 230 TRP A NE1 1848 C CE2 . TRP A 230 ? 0.9183 1.2669 0.8409 -0.0950 0.0941 -0.1195 230 TRP A CE2 1849 C CE3 . TRP A 230 ? 0.9512 1.2865 0.8396 -0.1186 0.1121 -0.1255 230 TRP A CE3 1850 C CZ2 . TRP A 230 ? 0.9264 1.2833 0.8557 -0.0964 0.0976 -0.1243 230 TRP A CZ2 1851 C CZ3 . TRP A 230 ? 0.9480 1.2885 0.8422 -0.1205 0.1133 -0.1309 230 TRP A CZ3 1852 C CH2 . TRP A 230 ? 0.9340 1.2850 0.8473 -0.1088 0.1069 -0.1308 230 TRP A CH2 1853 N N . THR A 231 ? 1.0375 1.3010 0.8569 -0.1276 0.1186 -0.1201 231 THR A N 1854 C CA . THR A 231 ? 1.0492 1.2955 0.8572 -0.1373 0.1218 -0.1234 231 THR A CA 1855 C C . THR A 231 ? 1.0404 1.3146 0.8569 -0.1536 0.1344 -0.1262 231 THR A C 1856 O O . THR A 231 ? 1.0090 1.3106 0.8356 -0.1577 0.1418 -0.1242 231 THR A O 1857 C CB . THR A 231 ? 1.0931 1.2910 0.8645 -0.1408 0.1203 -0.1204 231 THR A CB 1858 O OG1 . THR A 231 ? 1.1218 1.2970 0.8859 -0.1452 0.1185 -0.1239 231 THR A OG1 1859 C CG2 . THR A 231 ? 1.1015 1.2975 0.8529 -0.1546 0.1333 -0.1172 231 THR A CG2 1860 N N . ILE A 232 ? 1.0786 1.3456 0.8924 -0.1622 0.1358 -0.1312 232 ILE A N 1861 C CA . ILE A 232 ? 1.0899 1.3766 0.9078 -0.1802 0.1455 -0.1340 232 ILE A CA 1862 C C . ILE A 232 ? 1.1291 1.3795 0.9177 -0.1939 0.1505 -0.1323 232 ILE A C 1863 O O . ILE A 232 ? 1.1805 1.3936 0.9516 -0.1934 0.1453 -0.1346 232 ILE A O 1864 C CB . ILE A 232 ? 1.0821 1.3845 0.9140 -0.1823 0.1431 -0.1418 232 ILE A CB 1865 C CG1 . ILE A 232 ? 1.0382 1.3907 0.8998 -0.1803 0.1436 -0.1411 232 ILE A CG1 1866 C CG2 . ILE A 232 ? 1.1178 1.4103 0.9377 -0.2019 0.1484 -0.1467 232 ILE A CG2 1867 C CD1 . ILE A 232 ? 1.0196 1.3860 0.8966 -0.1639 0.1385 -0.1353 232 ILE A CD1 1868 N N . LEU A 233 ? 1.1525 1.4143 0.9372 -0.2057 0.1610 -0.1276 233 LEU A N 1869 C CA . LEU A 233 ? 1.1825 1.4142 0.9405 -0.2213 0.1677 -0.1237 233 LEU A CA 1870 C C . LEU A 233 ? 1.1941 1.4376 0.9597 -0.2414 0.1724 -0.1277 233 LEU A C 1871 O O . LEU A 233 ? 1.1574 1.4428 0.9461 -0.2498 0.1787 -0.1281 233 LEU A O 1872 C CB . LEU A 233 ? 1.1930 1.4340 0.9436 -0.2242 0.1787 -0.1166 233 LEU A CB 1873 C CG . LEU A 233 ? 1.2370 1.4444 0.9546 -0.2380 0.1868 -0.1096 233 LEU A CG 1874 C CD1 . LEU A 233 ? 1.2689 1.4231 0.9543 -0.2289 0.1759 -0.1067 233 LEU A CD1 1875 C CD2 . LEU A 233 ? 1.2304 1.4592 0.9466 -0.2396 0.2008 -0.1045 233 LEU A CD2 1876 N N . LYS A 234 ? 1.2549 1.4602 1.0017 -0.2487 0.1679 -0.1307 234 LYS A N 1877 C CA . LYS A 234 ? 1.3036 1.5112 1.0531 -0.2689 0.1700 -0.1356 234 LYS A CA 1878 C C . LYS A 234 ? 1.3221 1.5435 1.0713 -0.2908 0.1821 -0.1282 234 LYS A C 1879 O O . LYS A 234 ? 1.3335 1.5534 1.0734 -0.2898 0.1900 -0.1195 234 LYS A O 1880 C CB . LYS A 234 ? 1.3742 1.5288 1.0997 -0.2708 0.1623 -0.1399 234 LYS A CB 1881 C CG . LYS A 234 ? 1.3937 1.5384 1.1241 -0.2514 0.1519 -0.1495 234 LYS A CG 1882 C CD . LYS A 234 ? 1.4066 1.5873 1.1586 -0.2538 0.1513 -0.1600 234 LYS A CD 1883 C CE . LYS A 234 ? 1.4525 1.6110 1.2008 -0.2416 0.1437 -0.1717 234 LYS A CE 1884 N NZ . LYS A 234 ? 1.4462 1.5966 1.1985 -0.2167 0.1381 -0.1698 234 LYS A NZ 1885 N N . PRO A 235 ? 1.3360 1.5715 1.0953 -0.3111 0.1837 -0.1318 235 PRO A N 1886 C CA . PRO A 235 ? 1.3360 1.5816 1.0959 -0.3339 0.1951 -0.1235 235 PRO A CA 1887 C C . PRO A 235 ? 1.3837 1.5765 1.1094 -0.3431 0.1972 -0.1162 235 PRO A C 1888 O O . PRO A 235 ? 1.3996 1.5468 1.1044 -0.3379 0.1871 -0.1203 235 PRO A O 1889 C CB . PRO A 235 ? 1.3331 1.5982 1.1097 -0.3536 0.1918 -0.1300 235 PRO A CB 1890 C CG . PRO A 235 ? 1.3330 1.5773 1.1029 -0.3431 0.1788 -0.1425 235 PRO A CG 1891 C CD . PRO A 235 ? 1.3114 1.5538 1.0805 -0.3150 0.1754 -0.1433 235 PRO A CD 1892 N N . ASN A 236 ? 1.4149 1.6137 1.1349 -0.3559 0.2104 -0.1050 236 ASN A N 1893 C CA . ASN A 236 ? 1.4768 1.6272 1.1627 -0.3681 0.2136 -0.0954 236 ASN A CA 1894 C C . ASN A 236 ? 1.5016 1.6063 1.1561 -0.3482 0.2062 -0.0928 236 ASN A C 1895 O O . ASN A 236 ? 1.5591 1.6146 1.1827 -0.3559 0.2035 -0.0858 236 ASN A O 1896 C CB . ASN A 236 ? 1.5137 1.6339 1.1925 -0.3893 0.2065 -0.0984 236 ASN A CB 1897 C CG . ASN A 236 ? 1.5505 1.6840 1.2349 -0.4195 0.2182 -0.0889 236 ASN A CG 1898 O OD1 . ASN A 236 ? 1.5677 1.7091 1.2447 -0.4260 0.2325 -0.0767 236 ASN A OD1 1899 N ND2 . ASN A 236 ? 1.5684 1.7036 1.2650 -0.4389 0.2122 -0.0948 236 ASN A ND2 1900 N N . ASP A 237 ? 1.4713 1.5916 1.1345 -0.3236 0.2016 -0.0974 237 ASP A N 1901 C CA . ASP A 237 ? 1.4857 1.5673 1.1231 -0.3043 0.1927 -0.0948 237 ASP A CA 1902 C C . ASP A 237 ? 1.4543 1.5546 1.0868 -0.2942 0.2015 -0.0890 237 ASP A C 1903 O O . ASP A 237 ? 1.4203 1.5688 1.0783 -0.2940 0.2114 -0.0908 237 ASP A O 1904 C CB . ASP A 237 ? 1.4797 1.5592 1.1310 -0.2833 0.1777 -0.1056 237 ASP A CB 1905 C CG . ASP A 237 ? 1.5147 1.5476 1.1413 -0.2659 0.1651 -0.1028 237 ASP A CG 1906 O OD1 . ASP A 237 ? 1.5662 1.5579 1.1606 -0.2730 0.1649 -0.0931 237 ASP A OD1 1907 O OD2 . ASP A 237 ? 1.5045 1.5429 1.1450 -0.2456 0.1548 -0.1093 237 ASP A OD2 1908 N N . ALA A 238 ? 1.4715 1.5322 1.0704 -0.2857 0.1971 -0.0822 238 ALA A N 1909 C CA . ALA A 238 ? 1.4682 1.5381 1.0536 -0.2769 0.2050 -0.0773 238 ALA A CA 1910 C C . ALA A 238 ? 1.4379 1.4927 1.0178 -0.2517 0.1895 -0.0807 238 ALA A C 1911 O O . ALA A 238 ? 1.4737 1.4898 1.0404 -0.2443 0.1739 -0.0805 238 ALA A O 1912 C CB . ALA A 238 ? 1.5221 1.5589 1.0667 -0.2917 0.2146 -0.0646 238 ALA A CB 1913 N N . ILE A 239 ? 1.3905 1.4761 0.9828 -0.2385 0.1932 -0.0840 239 ILE A N 1914 C CA . ILE A 239 ? 1.3794 1.4502 0.9641 -0.2164 0.1787 -0.0859 239 ILE A CA 1915 C C . ILE A 239 ? 1.4306 1.4740 0.9729 -0.2150 0.1826 -0.0786 239 ILE A C 1916 O O . ILE A 239 ? 1.4237 1.4852 0.9580 -0.2231 0.2007 -0.0764 239 ILE A O 1917 C CB . ILE A 239 ? 1.3127 1.4279 0.9360 -0.2015 0.1763 -0.0942 239 ILE A CB 1918 C CG1 . ILE A 239 ? 1.3099 1.4064 0.9292 -0.1804 0.1577 -0.0957 239 ILE A CG1 1919 C CG2 . ILE A 239 ? 1.2947 1.4465 0.9267 -0.2035 0.1933 -0.0949 239 ILE A CG2 1920 C CD1 . ILE A 239 ? 1.2584 1.3925 0.9181 -0.1668 0.1513 -0.1026 239 ILE A CD1 1921 N N . ASN A 240 ? 1.4602 1.4606 0.9754 -0.2044 0.1654 -0.0750 240 ASN A N 1922 C CA . ASN A 240 ? 1.5069 1.4719 0.9738 -0.2043 0.1655 -0.0671 240 ASN A CA 1923 C C . ASN A 240 ? 1.4951 1.4533 0.9560 -0.1836 0.1505 -0.0707 240 ASN A C 1924 O O . ASN A 240 ? 1.4900 1.4302 0.9586 -0.1712 0.1295 -0.0715 240 ASN A O 1925 C CB . ASN A 240 ? 1.5667 1.4787 1.0004 -0.2124 0.1552 -0.0570 240 ASN A CB 1926 C CG . ASN A 240 ? 1.5999 1.5108 1.0327 -0.2355 0.1693 -0.0519 240 ASN A CG 1927 O OD1 . ASN A 240 ? 1.6074 1.5350 1.0304 -0.2503 0.1899 -0.0479 240 ASN A OD1 1928 N ND2 . ASN A 240 ? 1.6132 1.5043 1.0571 -0.2388 0.1585 -0.0522 240 ASN A ND2 1929 N N . PHE A 241 ? 1.5039 1.4760 0.9516 -0.1799 0.1611 -0.0732 241 PHE A N 1930 C CA . PHE A 241 ? 1.5041 1.4672 0.9424 -0.1617 0.1467 -0.0774 241 PHE A CA 1931 C C . PHE A 241 ? 1.5630 1.4799 0.9414 -0.1626 0.1423 -0.0701 241 PHE A C 1932 O O . PHE A 241 ? 1.6105 1.5179 0.9557 -0.1765 0.1600 -0.0641 241 PHE A O 1933 C CB . PHE A 241 ? 1.4714 1.4779 0.9347 -0.1543 0.1589 -0.0869 241 PHE A CB 1934 C CG . PHE A 241 ? 1.4330 1.4830 0.9537 -0.1503 0.1580 -0.0933 241 PHE A CG 1935 C CD1 . PHE A 241 ? 1.4174 1.4702 0.9645 -0.1357 0.1374 -0.0969 241 PHE A CD1 1936 C CD2 . PHE A 241 ? 1.4169 1.5059 0.9656 -0.1619 0.1771 -0.0949 241 PHE A CD2 1937 C CE1 . PHE A 241 ? 1.3711 1.4636 0.9676 -0.1327 0.1370 -0.1016 241 PHE A CE1 1938 C CE2 . PHE A 241 ? 1.3723 1.5002 0.9702 -0.1587 0.1748 -0.1001 241 PHE A CE2 1939 C CZ . PHE A 241 ? 1.3515 1.4805 0.9717 -0.1441 0.1554 -0.1033 241 PHE A CZ 1940 N N . GLU A 242 ? 1.5783 1.4674 0.9433 -0.1486 0.1182 -0.0700 242 GLU A N 1941 C CA . GLU A 242 ? 1.6519 1.4995 0.9594 -0.1467 0.1108 -0.0650 242 GLU A CA 1942 C C . GLU A 242 ? 1.6272 1.4700 0.9395 -0.1281 0.0887 -0.0718 242 GLU A C 1943 O O . GLU A 242 ? 1.5893 1.4334 0.9343 -0.1182 0.0679 -0.0725 242 GLU A O 1944 C CB . GLU A 242 ? 1.7264 1.5249 0.9979 -0.1548 0.0983 -0.0515 242 GLU A CB 1945 C CG . GLU A 242 ? 1.8205 1.5755 1.0245 -0.1571 0.0941 -0.0439 242 GLU A CG 1946 C CD . GLU A 242 ? 1.8778 1.5808 1.0493 -0.1616 0.0744 -0.0295 242 GLU A CD 1947 O OE1 . GLU A 242 ? 1.8933 1.5906 1.0774 -0.1723 0.0782 -0.0226 242 GLU A OE1 1948 O OE2 . GLU A 242 ? 1.9075 1.5736 1.0403 -0.1543 0.0538 -0.0250 242 GLU A OE2 1949 N N . SER A 243 ? 1.6393 1.4769 0.9196 -0.1236 0.0938 -0.0771 243 SER A N 1950 C CA . SER A 243 ? 1.6287 1.4597 0.9106 -0.1074 0.0728 -0.0845 243 SER A CA 1951 C C . SER A 243 ? 1.6833 1.4870 0.9059 -0.1055 0.0753 -0.0877 243 SER A C 1952 O O . SER A 243 ? 1.7275 1.5331 0.9185 -0.1148 0.1007 -0.0876 243 SER A O 1953 C CB . SER A 243 ? 1.5627 1.4418 0.9018 -0.0984 0.0780 -0.0957 243 SER A CB 1954 O OG . SER A 243 ? 1.5661 1.4375 0.9061 -0.0842 0.0582 -0.1026 243 SER A OG 1955 N N . ASN A 244 ? 1.6984 1.4777 0.9065 -0.0936 0.0490 -0.0909 244 ASN A N 1956 C CA . ASN A 244 ? 1.7533 1.5053 0.9048 -0.0896 0.0479 -0.0971 244 ASN A CA 1957 C C . ASN A 244 ? 1.7257 1.4886 0.8998 -0.0743 0.0335 -0.1106 244 ASN A C 1958 O O . ASN A 244 ? 1.7570 1.4881 0.8886 -0.0682 0.0186 -0.1156 244 ASN A O 1959 C CB . ASN A 244 ? 1.8127 1.5093 0.9043 -0.0931 0.0262 -0.0859 244 ASN A CB 1960 C CG . ASN A 244 ? 1.8042 1.4840 0.9195 -0.0844 -0.0114 -0.0809 244 ASN A CG 1961 O OD1 . ASN A 244 ? 1.7635 1.4722 0.9410 -0.0797 -0.0177 -0.0811 244 ASN A OD1 1962 N ND2 . ASN A 244 ? 1.8434 1.4773 0.9092 -0.0822 -0.0366 -0.0759 244 ASN A ND2 1963 N N . GLY A 245 ? 1.6644 1.4708 0.9038 -0.0690 0.0375 -0.1161 245 GLY A N 1964 C CA . GLY A 245 ? 1.6396 1.4596 0.9072 -0.0558 0.0255 -0.1276 245 GLY A CA 1965 C C . GLY A 245 ? 1.5787 1.4355 0.9190 -0.0513 0.0163 -0.1263 245 GLY A C 1966 O O . GLY A 245 ? 1.5634 1.4255 0.9282 -0.0558 0.0102 -0.1166 245 GLY A O 1967 N N . ASN A 246 ? 1.5482 1.4287 0.9211 -0.0421 0.0156 -0.1363 246 ASN A N 1968 C CA . ASN A 246 ? 1.4715 1.3871 0.9116 -0.0371 0.0059 -0.1353 246 ASN A CA 1969 C C . ASN A 246 ? 1.4063 1.3654 0.8893 -0.0439 0.0280 -0.1318 246 ASN A C 1970 O O . ASN A 246 ? 1.3511 1.3395 0.8864 -0.0414 0.0215 -0.1294 246 ASN A O 1971 C CB . ASN A 246 ? 1.4736 1.3720 0.9284 -0.0340 -0.0261 -0.1270 246 ASN A CB 1972 C CG . ASN A 246 ? 1.5231 1.3816 0.9427 -0.0275 -0.0526 -0.1304 246 ASN A CG 1973 O OD1 . ASN A 246 ? 1.5327 1.3967 0.9774 -0.0199 -0.0688 -0.1354 246 ASN A OD1 1974 N ND2 . ASN A 246 ? 1.5706 1.3874 0.9313 -0.0314 -0.0584 -0.1271 246 ASN A ND2 1975 N N . PHE A 247 ? 1.4186 1.3827 0.8791 -0.0531 0.0540 -0.1314 247 PHE A N 1976 C CA . PHE A 247 ? 1.3710 1.3718 0.8658 -0.0621 0.0739 -0.1277 247 PHE A CA 1977 C C . PHE A 247 ? 1.3283 1.3728 0.8621 -0.0581 0.0899 -0.1353 247 PHE A C 1978 O O . PHE A 247 ? 1.3591 1.4046 0.8748 -0.0542 0.1032 -0.1434 247 PHE A O 1979 C CB . PHE A 247 ? 1.4173 1.4034 0.8716 -0.0754 0.0934 -0.1226 247 PHE A CB 1980 C CG . PHE A 247 ? 1.3849 1.4039 0.8695 -0.0872 0.1126 -0.1184 247 PHE A CG 1981 C CD1 . PHE A 247 ? 1.3376 1.3780 0.8679 -0.0877 0.1041 -0.1153 247 PHE A CD1 1982 C CD2 . PHE A 247 ? 1.4133 1.4405 0.8783 -0.0987 0.1391 -0.1176 247 PHE A CD2 1983 C CE1 . PHE A 247 ? 1.3217 1.3892 0.8757 -0.0993 0.1201 -0.1126 247 PHE A CE1 1984 C CE2 . PHE A 247 ? 1.3880 1.4440 0.8805 -0.1112 0.1547 -0.1136 247 PHE A CE2 1985 C CZ . PHE A 247 ? 1.3493 1.4241 0.8850 -0.1115 0.1444 -0.1116 247 PHE A CZ 1986 N N . ILE A 248 ? 1.2718 1.3515 0.8586 -0.0584 0.0879 -0.1327 248 ILE A N 1987 C CA . ILE A 248 ? 1.2324 1.3564 0.8596 -0.0567 0.1027 -0.1372 248 ILE A CA 1988 C C . ILE A 248 ? 1.2282 1.3761 0.8655 -0.0706 0.1232 -0.1327 248 ILE A C 1989 O O . ILE A 248 ? 1.2056 1.3632 0.8648 -0.0765 0.1180 -0.1269 248 ILE A O 1990 C CB . ILE A 248 ? 1.1894 1.3372 0.8672 -0.0492 0.0862 -0.1361 248 ILE A CB 1991 C CG1 . ILE A 248 ? 1.2051 1.3235 0.8737 -0.0386 0.0603 -0.1375 248 ILE A CG1 1992 C CG2 . ILE A 248 ? 1.1619 1.3494 0.8758 -0.0453 0.0987 -0.1407 248 ILE A CG2 1993 C CD1 . ILE A 248 ? 1.2482 1.3449 0.8861 -0.0302 0.0604 -0.1472 248 ILE A CD1 1994 N N . ALA A 249 ? 1.2599 1.4164 0.8803 -0.0760 0.1465 -0.1356 249 ALA A N 1995 C CA . ALA A 249 ? 1.2691 1.4412 0.8904 -0.0918 0.1656 -0.1305 249 ALA A CA 1996 C C . ALA A 249 ? 1.2254 1.4490 0.8987 -0.0952 0.1765 -0.1310 249 ALA A C 1997 O O . ALA A 249 ? 1.2150 1.4637 0.9149 -0.0854 0.1785 -0.1364 249 ALA A O 1998 C CB . ALA A 249 ? 1.3172 1.4753 0.8956 -0.0978 0.1863 -0.1316 249 ALA A CB 1999 N N . PRO A 250 ? 1.2183 1.4561 0.9054 -0.1094 0.1824 -0.1254 250 PRO A N 2000 C CA . PRO A 250 ? 1.1905 1.4768 0.9228 -0.1147 0.1926 -0.1256 250 PRO A CA 2001 C C . PRO A 250 ? 1.2078 1.5185 0.9418 -0.1183 0.2164 -0.1281 250 PRO A C 2002 O O . PRO A 250 ? 1.2711 1.5636 0.9698 -0.1263 0.2303 -0.1265 250 PRO A O 2003 C CB . PRO A 250 ? 1.1810 1.4665 0.9161 -0.1305 0.1926 -0.1199 250 PRO A CB 2004 C CG . PRO A 250 ? 1.2192 1.4582 0.9063 -0.1361 0.1912 -0.1163 250 PRO A CG 2005 C CD . PRO A 250 ? 1.2450 1.4533 0.9073 -0.1207 0.1779 -0.1190 250 PRO A CD 2006 N N . GLU A 251 ? 1.1884 1.5400 0.9635 -0.1121 0.2212 -0.1312 251 GLU A N 2007 C CA . GLU A 251 ? 1.2181 1.6032 1.0075 -0.1166 0.2445 -0.1326 251 GLU A CA 2008 C C . GLU A 251 ? 1.1765 1.6029 1.0070 -0.1302 0.2484 -0.1277 251 GLU A C 2009 O O . GLU A 251 ? 1.1464 1.5848 0.9746 -0.1464 0.2640 -0.1239 251 GLU A O 2010 C CB . GLU A 251 ? 1.2494 1.6510 1.0566 -0.0986 0.2478 -0.1403 251 GLU A CB 2011 C CG . GLU A 251 ? 1.2949 1.7251 1.1095 -0.1005 0.2746 -0.1430 251 GLU A CG 2012 C CD . GLU A 251 ? 1.3247 1.7764 1.1660 -0.0815 0.2780 -0.1511 251 GLU A CD 2013 O OE1 . GLU A 251 ? 1.3517 1.7902 1.2001 -0.0670 0.2588 -0.1547 251 GLU A OE1 2014 O OE2 . GLU A 251 ? 1.3267 1.8087 1.1837 -0.0810 0.3000 -0.1536 251 GLU A OE2 2015 N N . TYR A 252 ? 1.1379 1.5853 1.0046 -0.1244 0.2333 -0.1272 252 TYR A N 2016 C CA . TYR A 252 ? 1.0946 1.5793 0.9981 -0.1363 0.2326 -0.1229 252 TYR A CA 2017 C C . TYR A 252 ? 1.0835 1.5513 0.9827 -0.1416 0.2154 -0.1202 252 TYR A C 2018 O O . TYR A 252 ? 1.0529 1.4983 0.9443 -0.1302 0.1997 -0.1212 252 TYR A O 2019 C CB . TYR A 252 ? 1.0639 1.5902 1.0138 -0.1260 0.2296 -0.1236 252 TYR A CB 2020 C CG . TYR A 252 ? 1.0796 1.6267 1.0411 -0.1178 0.2467 -0.1274 252 TYR A CG 2021 C CD1 . TYR A 252 ? 1.0902 1.6695 1.0680 -0.1299 0.2658 -0.1252 252 TYR A CD1 2022 C CD2 . TYR A 252 ? 1.0827 1.6177 1.0407 -0.0980 0.2438 -0.1335 252 TYR A CD2 2023 C CE1 . TYR A 252 ? 1.0867 1.6882 1.0783 -0.1210 0.2833 -0.1291 252 TYR A CE1 2024 C CE2 . TYR A 252 ? 1.0895 1.6428 1.0582 -0.0886 0.2606 -0.1387 252 TYR A CE2 2025 C CZ . TYR A 252 ? 1.0948 1.6826 1.0810 -0.0996 0.2813 -0.1365 252 TYR A CZ 2026 O OH . TYR A 252 ? 1.0946 1.7034 1.0942 -0.0890 0.2999 -0.1421 252 TYR A OH 2027 N N . ALA A 253 ? 1.0733 1.5522 0.9784 -0.1591 0.2186 -0.1172 253 ALA A N 2028 C CA . ALA A 253 ? 1.0439 1.5139 0.9501 -0.1645 0.2046 -0.1162 253 ALA A CA 2029 C C . ALA A 253 ? 1.0303 1.5440 0.9735 -0.1742 0.2040 -0.1146 253 ALA A C 2030 O O . ALA A 253 ? 1.0399 1.5875 1.0060 -0.1791 0.2147 -0.1132 253 ALA A O 2031 C CB . ALA A 253 ? 1.0614 1.4940 0.9320 -0.1770 0.2069 -0.1153 253 ALA A CB 2032 N N . TYR A 254 ? 1.0051 1.5186 0.9542 -0.1767 0.1916 -0.1149 254 TYR A N 2033 C CA . TYR A 254 ? 0.9832 1.5353 0.9627 -0.1856 0.1881 -0.1136 254 TYR A CA 2034 C C . TYR A 254 ? 0.9909 1.5347 0.9583 -0.2048 0.1892 -0.1153 254 TYR A C 2035 O O . TYR A 254 ? 0.9962 1.5063 0.9396 -0.2052 0.1835 -0.1183 254 TYR A O 2036 C CB . TYR A 254 ? 0.9635 1.5252 0.9589 -0.1741 0.1732 -0.1127 254 TYR A CB 2037 C CG . TYR A 254 ? 0.9513 1.5230 0.9638 -0.1563 0.1688 -0.1104 254 TYR A CG 2038 C CD1 . TYR A 254 ? 0.9639 1.5033 0.9583 -0.1423 0.1635 -0.1117 254 TYR A CD1 2039 C CD2 . TYR A 254 ? 0.9325 1.5448 0.9801 -0.1536 0.1679 -0.1066 254 TYR A CD2 2040 C CE1 . TYR A 254 ? 0.9663 1.5117 0.9757 -0.1268 0.1578 -0.1102 254 TYR A CE1 2041 C CE2 . TYR A 254 ? 0.9335 1.5515 0.9971 -0.1370 0.1628 -0.1046 254 TYR A CE2 2042 C CZ . TYR A 254 ? 0.9644 1.5480 1.0082 -0.1240 0.1578 -0.1069 254 TYR A CZ 2043 O OH . TYR A 254 ? 1.0010 1.5871 1.0599 -0.1084 0.1513 -0.1057 254 TYR A OH 2044 N N . LYS A 255 ? 1.0020 1.5763 0.9877 -0.2204 0.1956 -0.1138 255 LYS A N 2045 C CA . LYS A 255 ? 1.0243 1.5950 1.0032 -0.2399 0.1937 -0.1161 255 LYS A CA 2046 C C . LYS A 255 ? 0.9911 1.5799 0.9839 -0.2390 0.1805 -0.1182 255 LYS A C 2047 O O . LYS A 255 ? 0.9453 1.5689 0.9658 -0.2317 0.1756 -0.1148 255 LYS A O 2048 C CB . LYS A 255 ? 1.0491 1.6482 1.0451 -0.2587 0.2038 -0.1130 255 LYS A CB 2049 C CG . LYS A 255 ? 1.0855 1.6655 1.0632 -0.2659 0.2192 -0.1104 255 LYS A CG 2050 C CD . LYS A 255 ? 1.1071 1.7127 1.1012 -0.2891 0.2279 -0.1070 255 LYS A CD 2051 C CE . LYS A 255 ? 1.0911 1.7535 1.1303 -0.2877 0.2311 -0.1032 255 LYS A CE 2052 N NZ . LYS A 255 ? 1.1057 1.7966 1.1656 -0.3116 0.2375 -0.0993 255 LYS A NZ 2053 N N . ILE A 256 ? 1.0202 1.5843 0.9925 -0.2463 0.1749 -0.1238 256 ILE A N 2054 C CA . ILE A 256 ? 1.0178 1.5967 0.9970 -0.2476 0.1642 -0.1272 256 ILE A CA 2055 C C . ILE A 256 ? 1.0277 1.6278 1.0152 -0.2696 0.1636 -0.1288 256 ILE A C 2056 O O . ILE A 256 ? 1.0569 1.6316 1.0238 -0.2836 0.1641 -0.1346 256 ILE A O 2057 C CB . ILE A 256 ? 1.0420 1.5816 0.9941 -0.2416 0.1593 -0.1343 256 ILE A CB 2058 C CG1 . ILE A 256 ? 1.0438 1.5653 0.9915 -0.2203 0.1575 -0.1317 256 ILE A CG1 2059 C CG2 . ILE A 256 ? 1.0455 1.6004 1.0008 -0.2445 0.1509 -0.1392 256 ILE A CG2 2060 C CD1 . ILE A 256 ? 1.0663 1.5452 0.9887 -0.2135 0.1542 -0.1374 256 ILE A CD1 2061 N N . VAL A 257 ? 1.0188 1.6643 1.0372 -0.2730 0.1611 -0.1234 257 VAL A N 2062 C CA . VAL A 257 ? 1.0614 1.7315 1.0922 -0.2950 0.1592 -0.1236 257 VAL A CA 2063 C C . VAL A 257 ? 1.0803 1.7596 1.1065 -0.3022 0.1464 -0.1287 257 VAL A C 2064 O O . VAL A 257 ? 1.0902 1.7612 1.1045 -0.3211 0.1433 -0.1347 257 VAL A O 2065 C CB . VAL A 257 ? 1.0451 1.7614 1.1141 -0.2975 0.1631 -0.1147 257 VAL A CB 2066 C CG1 . VAL A 257 ? 1.0597 1.7653 1.1280 -0.2947 0.1786 -0.1116 257 VAL A CG1 2067 C CG2 . VAL A 257 ? 1.0113 1.7596 1.1061 -0.2809 0.1557 -0.1088 257 VAL A CG2 2068 N N . LYS A 258 ? 1.0686 1.7631 1.1022 -0.2877 0.1391 -0.1265 258 LYS A N 2069 C CA . LYS A 258 ? 1.0945 1.7986 1.1203 -0.2926 0.1281 -0.1308 258 LYS A CA 2070 C C . LYS A 258 ? 1.0872 1.7637 1.0902 -0.2775 0.1274 -0.1364 258 LYS A C 2071 O O . LYS A 258 ? 1.0777 1.7562 1.0894 -0.2594 0.1281 -0.1307 258 LYS A O 2072 C CB . LYS A 258 ? 1.0910 1.8436 1.1472 -0.2913 0.1191 -0.1212 258 LYS A CB 2073 C CG . LYS A 258 ? 1.1352 1.9168 1.2038 -0.3130 0.1115 -0.1205 258 LYS A CG 2074 C CD . LYS A 258 ? 1.1767 1.9506 1.2191 -0.3240 0.1019 -0.1295 258 LYS A CD 2075 C CE . LYS A 258 ? 1.1717 1.9755 1.2217 -0.3172 0.0909 -0.1231 258 LYS A CE 2076 N NZ . LYS A 258 ? 1.1608 2.0089 1.2383 -0.3302 0.0794 -0.1144 258 LYS A NZ 2077 N N . LYS A 259 ? 1.1165 1.7673 1.0917 -0.2851 0.1258 -0.1478 259 LYS A N 2078 C CA . LYS A 259 ? 1.1396 1.7710 1.0958 -0.2720 0.1251 -0.1542 259 LYS A CA 2079 C C . LYS A 259 ? 1.1499 1.8063 1.1025 -0.2777 0.1171 -0.1567 259 LYS A C 2080 O O . LYS A 259 ? 1.1845 1.8585 1.1382 -0.2954 0.1111 -0.1583 259 LYS A O 2081 C CB . LYS A 259 ? 1.1920 1.7747 1.1185 -0.2736 0.1298 -0.1664 259 LYS A CB 2082 C CG . LYS A 259 ? 1.2270 1.7796 1.1508 -0.2614 0.1364 -0.1632 259 LYS A CG 2083 C CD . LYS A 259 ? 1.2751 1.7797 1.1716 -0.2673 0.1396 -0.1730 259 LYS A CD 2084 C CE . LYS A 259 ? 1.2980 1.7731 1.1899 -0.2562 0.1447 -0.1680 259 LYS A CE 2085 N NZ . LYS A 259 ? 1.3427 1.7730 1.2104 -0.2659 0.1473 -0.1737 259 LYS A NZ 2086 N N . GLY A 260 ? 1.1602 1.8189 1.1080 -0.2635 0.1167 -0.1566 260 GLY A N 2087 C CA . GLY A 260 ? 1.1674 1.8491 1.1073 -0.2682 0.1105 -0.1584 260 GLY A CA 2088 C C . GLY A 260 ? 1.1450 1.8427 1.0927 -0.2517 0.1107 -0.1505 260 GLY A C 2089 O O . GLY A 260 ? 1.1490 1.8352 1.1065 -0.2358 0.1152 -0.1459 260 GLY A O 2090 N N . ASP A 261 ? 1.1574 1.8820 1.1003 -0.2566 0.1048 -0.1481 261 ASP A N 2091 C CA . ASP A 261 ? 1.1445 1.8852 1.0912 -0.2437 0.1057 -0.1405 261 ASP A CA 2092 C C . ASP A 261 ? 1.0590 1.8256 1.0398 -0.2350 0.1007 -0.1215 261 ASP A C 2093 O O . ASP A 261 ? 1.0259 1.8189 1.0247 -0.2429 0.0923 -0.1119 261 ASP A O 2094 C CB . ASP A 261 ? 1.2074 1.9677 1.1332 -0.2532 0.1014 -0.1435 261 ASP A CB 2095 C CG . ASP A 261 ? 1.2908 2.0227 1.1805 -0.2544 0.1090 -0.1634 261 ASP A CG 2096 O OD1 . ASP A 261 ? 1.3444 2.0430 1.2288 -0.2444 0.1177 -0.1727 261 ASP A OD1 2097 O OD2 . ASP A 261 ? 1.3437 2.0855 1.2093 -0.2647 0.1058 -0.1700 261 ASP A OD2 2098 N N . SER A 262 ? 1.0050 1.7629 0.9957 -0.2184 0.1053 -0.1165 262 SER A N 2099 C CA . SER A 262 ? 0.9749 1.7499 0.9964 -0.2084 0.1005 -0.1001 262 SER A CA 2100 C C . SER A 262 ? 0.9509 1.7201 0.9751 -0.1937 0.1044 -0.0962 262 SER A C 2101 O O . SER A 262 ? 0.9958 1.7508 1.0000 -0.1911 0.1115 -0.1062 262 SER A O 2102 C CB . SER A 262 ? 0.9779 1.7373 1.0138 -0.2051 0.1019 -0.1000 262 SER A CB 2103 O OG . SER A 262 ? 0.9570 1.7269 1.0202 -0.1936 0.0978 -0.0867 262 SER A OG 2104 N N . THR A 263 ? 1.2142 1.3026 1.0231 -0.2109 0.0765 -0.0571 263 THR A N 2105 C CA . THR A 263 ? 1.1379 1.2223 0.9783 -0.1565 0.0658 -0.0546 263 THR A CA 2106 C C . THR A 263 ? 1.0271 1.2041 0.9416 -0.1423 0.0636 -0.0715 263 THR A C 2107 O O . THR A 263 ? 0.9829 1.2295 0.9395 -0.1630 0.0681 -0.0861 263 THR A O 2108 C CB . THR A 263 ? 1.1064 1.1775 0.9814 -0.1302 0.0600 -0.0543 263 THR A CB 2109 O OG1 . THR A 263 ? 1.0974 1.1639 0.9884 -0.0836 0.0511 -0.0525 263 THR A OG1 2110 C CG2 . THR A 263 ? 1.0402 1.1905 0.9962 -0.1348 0.0611 -0.0713 263 THR A CG2 2111 N N . ILE A 264 ? 0.9920 1.1722 0.9171 -0.1060 0.0570 -0.0711 264 ILE A N 2112 C CA . ILE A 264 ? 0.9002 1.1596 0.8931 -0.0912 0.0556 -0.0889 264 ILE A CA 2113 C C . ILE A 264 ? 0.8635 1.1378 0.9101 -0.0626 0.0512 -0.0973 264 ILE A C 2114 O O . ILE A 264 ? 0.8937 1.1404 0.9269 -0.0362 0.0456 -0.0913 264 ILE A O 2115 C CB . ILE A 264 ? 0.8895 1.1563 0.8588 -0.0765 0.0530 -0.0872 264 ILE A CB 2116 C CG1 . ILE A 264 ? 0.9552 1.1883 0.8542 -0.1067 0.0585 -0.0756 264 ILE A CG1 2117 C CG2 . ILE A 264 ? 0.8154 1.1640 0.8515 -0.0691 0.0536 -0.1083 264 ILE A CG2 2118 C CD1 . ILE A 264 ? 0.9860 1.2226 0.8532 -0.0912 0.0561 -0.0721 264 ILE A CD1 2119 N N . MET A 265 ? 0.8250 1.1439 0.9262 -0.0671 0.0543 -0.1121 265 MET A N 2120 C CA . MET A 265 ? 0.7909 1.1136 0.9340 -0.0478 0.0530 -0.1201 265 MET A CA 2121 C C . MET A 265 ? 0.7738 1.1414 0.9551 -0.0365 0.0550 -0.1383 265 MET A C 2122 O O . MET A 265 ? 0.7786 1.1858 0.9727 -0.0449 0.0583 -0.1490 265 MET A O 2123 C CB . MET A 265 ? 0.7925 1.1254 0.9560 -0.0579 0.0562 -0.1245 265 MET A CB 2124 C CG . MET A 265 ? 0.7759 1.0907 0.9642 -0.0416 0.0555 -0.1267 265 MET A CG 2125 S SD . MET A 265 ? 0.7779 1.1081 0.9755 -0.0513 0.0578 -0.1289 265 MET A SD 2126 C CE . MET A 265 ? 0.8091 1.0878 0.9570 -0.0725 0.0561 -0.1091 265 MET A CE 2127 N N . LYS A 266 ? 0.7944 1.1588 0.9898 -0.0204 0.0537 -0.1437 266 LYS A N 2128 C CA . LYS A 266 ? 0.7988 1.2001 1.0237 -0.0171 0.0582 -0.1638 266 LYS A CA 2129 C C . LYS A 266 ? 0.7843 1.1733 1.0339 -0.0167 0.0642 -0.1751 266 LYS A C 2130 O O . LYS A 266 ? 0.8024 1.1618 1.0524 -0.0119 0.0638 -0.1704 266 LYS A O 2131 C CB . LYS A 266 ? 0.8523 1.2679 1.0729 -0.0053 0.0553 -0.1673 266 LYS A CB 2132 C CG . LYS A 266 ? 0.9250 1.3462 1.1097 0.0054 0.0483 -0.1555 266 LYS A CG 2133 C CD . LYS A 266 ? 0.9703 1.4357 1.1596 -0.0010 0.0505 -0.1657 266 LYS A CD 2134 C CE . LYS A 266 ? 1.0421 1.4992 1.1832 0.0102 0.0441 -0.1503 266 LYS A CE 2135 N NZ . LYS A 266 ? 1.1062 1.5037 1.2047 -0.0002 0.0431 -0.1288 266 LYS A NZ 2136 N N . SER A 267 ? 0.7906 1.1975 1.0538 -0.0189 0.0699 -0.1899 267 SER A N 2137 C CA . SER A 267 ? 0.8055 1.1878 1.0766 -0.0120 0.0759 -0.2000 267 SER A CA 2138 C C . SER A 267 ? 0.8209 1.2199 1.0958 -0.0090 0.0825 -0.2198 267 SER A C 2139 O O . SER A 267 ? 0.8631 1.3022 1.1411 -0.0116 0.0807 -0.2227 267 SER A O 2140 C CB . SER A 267 ? 0.8142 1.1852 1.0824 -0.0061 0.0725 -0.1887 267 SER A CB 2141 O OG . SER A 267 ? 0.8452 1.1968 1.1141 0.0092 0.0775 -0.1989 267 SER A OG 2142 N N . GLU A 268 ? 0.8641 1.2261 1.1316 -0.0044 0.0912 -0.2338 268 GLU A N 2143 C CA . GLU A 268 ? 0.9019 1.2601 1.1597 0.0023 0.0988 -0.2540 268 GLU A CA 2144 C C . GLU A 268 ? 0.9151 1.2620 1.1626 0.0292 0.0979 -0.2554 268 GLU A C 2145 O O . GLU A 268 ? 0.9790 1.3294 1.2145 0.0441 0.1019 -0.2712 268 GLU A O 2146 C CB . GLU A 268 ? 0.9533 1.2640 1.1913 -0.0095 0.1113 -0.2706 268 GLU A CB 2147 C CG . GLU A 268 ? 0.9478 1.2870 1.1965 -0.0351 0.1126 -0.2737 268 GLU A CG 2148 C CD . GLU A 268 ? 0.9446 1.3510 1.2103 -0.0409 0.1074 -0.2766 268 GLU A CD 2149 O OE1 . GLU A 268 ? 0.9106 1.3296 1.1725 -0.0406 0.1120 -0.2918 268 GLU A OE1 2150 O OE2 . GLU A 268 ? 0.9198 1.3625 1.1971 -0.0427 0.0987 -0.2635 268 GLU A OE2 2151 N N . LEU A 269 ? 0.8943 1.2338 1.1445 0.0380 0.0923 -0.2405 269 LEU A N 2152 C CA . LEU A 269 ? 0.9220 1.2647 1.1628 0.0671 0.0903 -0.2427 269 LEU A CA 2153 C C . LEU A 269 ? 0.9305 1.3512 1.1847 0.0712 0.0849 -0.2477 269 LEU A C 2154 O O . LEU A 269 ? 0.8905 1.3550 1.1606 0.0462 0.0812 -0.2409 269 LEU A O 2155 C CB . LEU A 269 ? 0.9102 1.2392 1.1540 0.0701 0.0854 -0.2261 269 LEU A CB 2156 C CG . LEU A 269 ? 0.9325 1.1897 1.1622 0.0667 0.0904 -0.2206 269 LEU A CG 2157 C CD1 . LEU A 269 ? 0.9151 1.1725 1.1549 0.0629 0.0839 -0.2023 269 LEU A CD1 2158 C CD2 . LEU A 269 ? 1.0031 1.1967 1.1953 0.0935 0.0989 -0.2325 269 LEU A CD2 2159 N N . GLU A 270 ? 0.9903 1.4276 1.2317 0.1046 0.0849 -0.2605 270 GLU A N 2160 C CA . GLU A 270 ? 1.0042 1.5309 1.2576 0.1114 0.0800 -0.2690 270 GLU A CA 2161 C C . GLU A 270 ? 0.9400 1.5105 1.1987 0.1206 0.0741 -0.2628 270 GLU A C 2162 O O . GLU A 270 ? 0.9171 1.4428 1.1715 0.1216 0.0734 -0.2504 270 GLU A O 2163 C CB . GLU A 270 ? 1.1092 1.6406 1.3421 0.1481 0.0834 -0.2919 270 GLU A CB 2164 C CG . GLU A 270 ? 1.1958 1.6746 1.4155 0.1385 0.0916 -0.3018 270 GLU A CG 2165 C CD . GLU A 270 ? 1.1985 1.7392 1.4435 0.1076 0.0904 -0.3043 270 GLU A CD 2166 O OE1 . GLU A 270 ? 1.1831 1.7528 1.4504 0.0743 0.0862 -0.2881 270 GLU A OE1 2167 O OE2 . GLU A 270 ? 1.2189 1.7735 1.4551 0.1186 0.0938 -0.3225 270 GLU A OE2 2168 N N . TYR A 271 ? 0.9034 1.5688 1.1711 0.1248 0.0704 -0.2735 271 TYR A N 2169 C CA . TYR A 271 ? 0.8573 1.5884 1.1315 0.1244 0.0658 -0.2720 271 TYR A CA 2170 C C . TYR A 271 ? 0.8907 1.6016 1.1469 0.1762 0.0638 -0.2776 271 TYR A C 2171 O O . TYR A 271 ? 0.9092 1.5928 1.1415 0.2233 0.0651 -0.2913 271 TYR A O 2172 C CB . TYR A 271 ? 0.8380 1.6898 1.1231 0.1147 0.0640 -0.2879 271 TYR A CB 2173 C CG . TYR A 271 ? 0.8064 1.7456 1.0979 0.0982 0.0614 -0.2900 271 TYR A CG 2174 C CD1 . TYR A 271 ? 0.7767 1.6914 1.0681 0.0519 0.0626 -0.2712 271 TYR A CD1 2175 C CD2 . TYR A 271 ? 0.7953 1.8470 1.0888 0.1285 0.0582 -0.3133 271 TYR A CD2 2176 C CE1 . TYR A 271 ? 0.7668 1.7609 1.0588 0.0292 0.0623 -0.2758 271 TYR A CE1 2177 C CE2 . TYR A 271 ? 0.7829 1.9308 1.0823 0.1076 0.0570 -0.3194 271 TYR A CE2 2178 C CZ . TYR A 271 ? 0.7730 1.8896 1.0712 0.0542 0.0599 -0.3008 271 TYR A CZ 2179 O OH . TYR A 271 ? 0.7353 1.9476 1.0344 0.0272 0.0607 -0.3097 271 TYR A OH 2180 N N . GLY A 272 ? 0.9071 1.6269 1.1678 0.1686 0.0609 -0.2672 272 GLY A N 2181 C CA . GLY A 272 ? 0.9540 1.6468 1.1948 0.2165 0.0588 -0.2688 272 GLY A CA 2182 C C . GLY A 272 ? 0.9756 1.7809 1.2174 0.2473 0.0530 -0.2846 272 GLY A C 2183 O O . GLY A 272 ? 0.9924 1.7809 1.2119 0.2971 0.0503 -0.2876 272 GLY A O 2184 N N . ASN A 273 ? 0.9740 1.8973 1.2372 0.2178 0.0516 -0.2960 273 ASN A N 2185 C CA . ASN A 273 ? 0.9933 2.0531 1.2619 0.2359 0.0468 -0.3152 273 ASN A CA 2186 C C . ASN A 273 ? 0.9820 2.0410 1.2517 0.2297 0.0449 -0.3051 273 ASN A C 2187 O O . ASN A 273 ? 1.0128 2.0903 1.2673 0.2861 0.0401 -0.3128 273 ASN A O 2188 C CB . ASN A 273 ? 1.0348 2.1344 1.2803 0.3169 0.0421 -0.3381 273 ASN A CB 2189 C CG . ASN A 273 ? 1.0614 2.1437 1.2999 0.3284 0.0445 -0.3483 273 ASN A CG 2190 O OD1 . ASN A 273 ? 1.1008 2.0596 1.3147 0.3496 0.0482 -0.3410 273 ASN A OD1 2191 N ND2 . ASN A 273 ? 1.0247 2.2332 1.2823 0.3101 0.0437 -0.3668 273 ASN A ND2 2192 N N . CYS A 274 ? 0.9559 1.9911 1.2378 0.1634 0.0486 -0.2882 274 CYS A N 2193 C CA . CYS A 274 ? 0.9572 1.9442 1.2366 0.1533 0.0480 -0.2725 274 CYS A CA 2194 C C . CYS A 274 ? 0.8495 1.8598 1.1347 0.0771 0.0524 -0.2639 274 CYS A C 2195 O O . CYS A 274 ? 0.8501 1.8738 1.1350 0.0306 0.0569 -0.2634 274 CYS A O 2196 C CB . CYS A 274 ? 1.0468 1.8830 1.3148 0.1695 0.0493 -0.2519 274 CYS A CB 2197 S SG . CYS A 274 ? 1.2156 1.9662 1.4842 0.1321 0.0506 -0.2262 274 CYS A SG 2198 N N . ASN A 275 ? 0.7865 1.7940 1.0692 0.0644 0.0520 -0.2572 275 ASN A N 2199 C CA . ASN A 275 ? 0.7790 1.7848 1.0531 -0.0080 0.0577 -0.2483 275 ASN A CA 2200 C C . ASN A 275 ? 0.7968 1.6916 1.0624 -0.0150 0.0573 -0.2251 275 ASN A C 2201 O O . ASN A 275 ? 0.8170 1.6814 1.0876 0.0316 0.0526 -0.2215 275 ASN A O 2202 C CB . ASN A 275 ? 0.7666 1.9167 1.0416 -0.0344 0.0600 -0.2711 275 ASN A CB 2203 C CG . ASN A 275 ? 0.7657 1.9144 1.0169 -0.1208 0.0696 -0.2665 275 ASN A CG 2204 O OD1 . ASN A 275 ? 0.7682 1.8739 1.0018 -0.1624 0.0752 -0.2586 275 ASN A OD1 2205 N ND2 . ASN A 275 ? 0.8052 1.9962 1.0480 -0.1481 0.0724 -0.2721 275 ASN A ND2 2206 N N . THR A 276 ? 0.8034 1.6347 1.0497 -0.0707 0.0623 -0.2095 276 THR A N 2207 C CA . THR A 276 ? 0.8002 1.5251 1.0350 -0.0766 0.0616 -0.1880 276 THR A CA 2208 C C . THR A 276 ? 0.8289 1.5112 1.0272 -0.1418 0.0682 -0.1774 276 THR A C 2209 O O . THR A 276 ? 0.8584 1.5664 1.0366 -0.1822 0.0740 -0.1823 276 THR A O 2210 C CB . THR A 276 ? 0.8076 1.4309 1.0493 -0.0423 0.0583 -0.1729 276 THR A CB 2211 O OG1 . THR A 276 ? 0.8358 1.3754 1.0705 -0.0398 0.0567 -0.1559 276 THR A OG1 2212 C CG2 . THR A 276 ? 0.8169 1.4040 1.0469 -0.0676 0.0610 -0.1666 276 THR A CG2 2213 N N . LYS A 277 ? 0.8686 1.4785 1.0507 -0.1507 0.0679 -0.1630 277 LYS A N 2214 C CA . LYS A 277 ? 0.9509 1.4889 1.0832 -0.2039 0.0741 -0.1503 277 LYS A CA 2215 C C . LYS A 277 ? 0.9372 1.3563 1.0532 -0.1885 0.0708 -0.1284 277 LYS A C 2216 O O . LYS A 277 ? 0.9617 1.3048 1.0266 -0.2204 0.0747 -0.1160 277 LYS A O 2217 C CB . LYS A 277 ? 1.0235 1.5608 1.1387 -0.2268 0.0767 -0.1510 277 LYS A CB 2218 C CG . LYS A 277 ? 1.0922 1.7423 1.1983 -0.2719 0.0844 -0.1736 277 LYS A CG 2219 C CD . LYS A 277 ? 1.1754 1.7994 1.2469 -0.3115 0.0900 -0.1725 277 LYS A CD 2220 C CE . LYS A 277 ? 1.2286 1.9753 1.2878 -0.3654 0.0997 -0.1987 277 LYS A CE 2221 N NZ . LYS A 277 ? 1.2898 2.0430 1.2995 -0.4332 0.1123 -0.2057 277 LYS A NZ 2222 N N . CYS A 278 ? 0.8899 1.2935 1.0423 -0.1392 0.0642 -0.1254 278 CYS A N 2223 C CA . CYS A 278 ? 0.8914 1.2054 1.0355 -0.1212 0.0606 -0.1092 278 CYS A CA 2224 C C . CYS A 278 ? 0.8225 1.1518 1.0014 -0.0854 0.0578 -0.1147 278 CYS A C 2225 O O . CYS A 278 ? 0.8022 1.1639 1.0117 -0.0541 0.0561 -0.1237 278 CYS A O 2226 C CB . CYS A 278 ? 0.9247 1.1856 1.0696 -0.1042 0.0570 -0.0991 278 CYS A CB 2227 S SG . CYS A 278 ? 0.9899 1.1658 1.1309 -0.0764 0.0520 -0.0843 278 CYS A SG 2228 N N . GLN A 279 ? 0.7899 1.0919 0.9566 -0.0896 0.0580 -0.1100 279 GLN A N 2229 C CA . GLN A 279 ? 0.7620 1.0813 0.9567 -0.0636 0.0570 -0.1178 279 GLN A CA 2230 C C . GLN A 279 ? 0.7566 1.0180 0.9462 -0.0507 0.0545 -0.1085 279 GLN A C 2231 O O . GLN A 279 ? 0.7789 0.9982 0.9345 -0.0638 0.0533 -0.0967 279 GLN A O 2232 C CB . GLN A 279 ? 0.7600 1.1343 0.9523 -0.0808 0.0601 -0.1278 279 GLN A CB 2233 C CG . GLN A 279 ? 0.7304 1.1270 0.9495 -0.0545 0.0598 -0.1390 279 GLN A CG 2234 C CD . GLN A 279 ? 0.7227 1.1615 0.9671 -0.0233 0.0598 -0.1539 279 GLN A CD 2235 O OE1 . GLN A 279 ? 0.7155 1.2217 0.9633 -0.0262 0.0602 -0.1647 279 GLN A OE1 2236 N NE2 . GLN A 279 ? 0.7134 1.1130 0.9684 0.0070 0.0599 -0.1559 279 GLN A NE2 2237 N N . THR A 280 ? 0.7187 0.9785 0.9349 -0.0247 0.0545 -0.1154 280 THR A N 2238 C CA . THR A 280 ? 0.7240 0.9535 0.9408 -0.0151 0.0535 -0.1132 280 THR A CA 2239 C C . THR A 280 ? 0.7197 0.9777 0.9537 -0.0080 0.0569 -0.1273 280 THR A C 2240 O O . THR A 280 ? 0.7055 0.9956 0.9512 -0.0018 0.0596 -0.1383 280 THR A O 2241 C CB . THR A 280 ? 0.7256 0.9211 0.9513 0.0004 0.0532 -0.1109 280 THR A CB 2242 O OG1 . THR A 280 ? 0.6938 0.8938 0.9376 0.0147 0.0582 -0.1234 280 THR A OG1 2243 C CG2 . THR A 280 ? 0.7414 0.9189 0.9581 -0.0026 0.0509 -0.1015 280 THR A CG2 2244 N N . PRO A 281 ? 0.7244 0.9754 0.9572 -0.0063 0.0568 -0.1288 281 PRO A N 2245 C CA . PRO A 281 ? 0.7163 0.9922 0.9627 -0.0033 0.0611 -0.1439 281 PRO A CA 2246 C C . PRO A 281 ? 0.7290 0.9930 0.9870 0.0091 0.0676 -0.1575 281 PRO A C 2247 O O . PRO A 281 ? 0.7186 0.9970 0.9802 0.0117 0.0724 -0.1717 281 PRO A O 2248 C CB . PRO A 281 ? 0.7153 0.9898 0.9561 -0.0037 0.0593 -0.1433 281 PRO A CB 2249 C CG . PRO A 281 ? 0.7366 0.9889 0.9510 -0.0046 0.0526 -0.1257 281 PRO A CG 2250 C CD . PRO A 281 ? 0.7278 0.9549 0.9396 -0.0065 0.0520 -0.1174 281 PRO A CD 2251 N N . MET A 282 ? 0.7681 0.9986 1.0242 0.0170 0.0686 -0.1535 282 MET A N 2252 C CA . MET A 282 ? 0.8382 1.0393 1.0887 0.0303 0.0761 -0.1647 282 MET A CA 2253 C C . MET A 282 ? 0.8267 1.0242 1.0719 0.0503 0.0748 -0.1627 282 MET A C 2254 O O . MET A 282 ? 0.8487 1.0103 1.0770 0.0687 0.0807 -0.1702 282 MET A O 2255 C CB . MET A 282 ? 0.9158 1.0772 1.1596 0.0235 0.0815 -0.1662 282 MET A CB 2256 C CG . MET A 282 ? 0.9718 1.1189 1.2175 0.0225 0.0764 -0.1519 282 MET A CG 2257 S SD . MET A 282 ? 1.1267 1.2490 1.3658 0.0089 0.0839 -0.1588 282 MET A SD 2258 C CE . MET A 282 ? 1.0833 1.2540 1.3308 -0.0057 0.0845 -0.1711 282 MET A CE 2259 N N . GLY A 283 ? 0.7778 1.0120 1.0302 0.0466 0.0681 -0.1543 283 GLY A N 2260 C CA . GLY A 283 ? 0.7742 1.0279 1.0241 0.0651 0.0662 -0.1555 283 GLY A CA 2261 C C . GLY A 283 ? 0.7546 1.0325 1.0079 0.0487 0.0608 -0.1441 283 GLY A C 2262 O O . GLY A 283 ? 0.7357 0.9917 0.9856 0.0283 0.0587 -0.1325 283 GLY A O 2263 N N . ALA A 284 ? 0.7646 1.0885 1.0188 0.0590 0.0589 -0.1491 284 ALA A N 2264 C CA . ALA A 284 ? 0.7709 1.1248 1.0235 0.0371 0.0559 -0.1424 284 ALA A CA 2265 C C . ALA A 284 ? 0.7906 1.1106 1.0404 0.0476 0.0544 -0.1339 284 ALA A C 2266 O O . ALA A 284 ? 0.7798 1.0682 1.0275 0.0779 0.0556 -0.1356 284 ALA A O 2267 C CB . ALA A 284 ? 0.7717 1.2138 1.0281 0.0373 0.0554 -0.1563 284 ALA A CB 2268 N N . ILE A 285 ? 0.8030 1.1239 1.0456 0.0210 0.0527 -0.1250 285 ILE A N 2269 C CA . ILE A 285 ? 0.8322 1.1224 1.0718 0.0261 0.0509 -0.1164 285 ILE A CA 2270 C C . ILE A 285 ? 0.8461 1.1959 1.0830 0.0135 0.0502 -0.1216 285 ILE A C 2271 O O . ILE A 285 ? 0.8591 1.2417 1.0840 -0.0226 0.0521 -0.1240 285 ILE A O 2272 C CB . ILE A 285 ? 0.8235 1.0510 1.0498 0.0065 0.0498 -0.1016 285 ILE A CB 2273 C CG1 . ILE A 285 ? 0.8288 1.0117 1.0603 0.0204 0.0506 -0.0994 285 ILE A CG1 2274 C CG2 . ILE A 285 ? 0.8242 1.0296 1.0453 0.0071 0.0479 -0.0939 285 ILE A CG2 2275 C CD1 . ILE A 285 ? 0.8458 0.9863 1.0624 0.0080 0.0481 -0.0885 285 ILE A CD1 2276 N N . ASN A 286 ? 0.8863 1.2491 1.1289 0.0408 0.0485 -0.1241 286 ASN A N 2277 C CA . ASN A 286 ? 0.9541 1.3818 1.1958 0.0314 0.0477 -0.1309 286 ASN A CA 2278 C C . ASN A 286 ? 0.9272 1.3150 1.1670 0.0446 0.0456 -0.1214 286 ASN A C 2279 O O . ASN A 286 ? 0.9070 1.2919 1.1495 0.0860 0.0439 -0.1230 286 ASN A O 2280 C CB . ASN A 286 ? 1.0275 1.5473 1.2780 0.0620 0.0464 -0.1497 286 ASN A CB 2281 C CG . ASN A 286 ? 1.1465 1.7465 1.3985 0.0646 0.0446 -0.1598 286 ASN A CG 2282 O OD1 . ASN A 286 ? 1.1043 1.7365 1.3503 0.0178 0.0473 -0.1618 286 ASN A OD1 2283 N ND2 . ASN A 286 ? 1.3240 1.9538 1.5768 0.1200 0.0408 -0.1671 286 ASN A ND2 2284 N N . SER A 287 ? 0.9266 1.2751 1.1544 0.0113 0.0462 -0.1110 287 SER A N 2285 C CA . SER A 287 ? 0.9525 1.2693 1.1781 0.0193 0.0443 -0.1029 287 SER A CA 2286 C C . SER A 287 ? 0.9672 1.2635 1.1707 -0.0240 0.0459 -0.0976 287 SER A C 2287 O O . SER A 287 ? 0.9431 1.2287 1.1249 -0.0596 0.0491 -0.0973 287 SER A O 2288 C CB . SER A 287 ? 0.9601 1.1982 1.1890 0.0451 0.0434 -0.0913 287 SER A CB 2289 O OG . SER A 287 ? 0.9197 1.0994 1.1382 0.0241 0.0434 -0.0812 287 SER A OG 2290 N N . SER A 288 ? 0.9975 1.2809 1.1992 -0.0199 0.0444 -0.0934 288 SER A N 2291 C CA . SER A 288 ? 1.0265 1.2752 1.1994 -0.0570 0.0463 -0.0884 288 SER A CA 2292 C C . SER A 288 ? 0.9830 1.1397 1.1447 -0.0467 0.0434 -0.0727 288 SER A C 2293 O O . SER A 288 ? 0.9912 1.1062 1.1238 -0.0677 0.0441 -0.0677 288 SER A O 2294 C CB . SER A 288 ? 1.0689 1.3757 1.2450 -0.0628 0.0468 -0.0974 288 SER A CB 2295 O OG . SER A 288 ? 1.1341 1.5398 1.3131 -0.0822 0.0503 -0.1156 288 SER A OG 2296 N N . MET A 289 ? 0.9328 1.0607 1.1130 -0.0158 0.0408 -0.0670 289 MET A N 2297 C CA . MET A 289 ? 0.9393 1.0001 1.1119 -0.0049 0.0381 -0.0559 289 MET A CA 2298 C C . MET A 289 ? 0.9434 0.9557 1.0783 -0.0261 0.0379 -0.0501 289 MET A C 2299 O O . MET A 289 ? 0.9687 0.9905 1.0906 -0.0430 0.0403 -0.0531 289 MET A O 2300 C CB . MET A 289 ? 0.9588 1.0084 1.1536 0.0224 0.0378 -0.0552 289 MET A CB 2301 C CG . MET A 289 ? 0.9784 1.0501 1.1930 0.0482 0.0395 -0.0593 289 MET A CG 2302 S SD . MET A 289 ? 0.9869 1.0443 1.2016 0.0607 0.0381 -0.0537 289 MET A SD 2303 C CE . MET A 289 ? 0.9506 0.9892 1.1695 0.0930 0.0425 -0.0550 289 MET A CE 2304 N N . PRO A 290 ? 0.9478 0.9054 1.0588 -0.0220 0.0349 -0.0421 290 PRO A N 2305 C CA . PRO A 290 ? 0.9671 0.8668 1.0301 -0.0299 0.0339 -0.0359 290 PRO A CA 2306 C C . PRO A 290 ? 0.9328 0.8265 1.0050 -0.0073 0.0307 -0.0341 290 PRO A C 2307 O O . PRO A 290 ? 0.9820 0.8377 1.0130 -0.0097 0.0298 -0.0299 290 PRO A O 2308 C CB . PRO A 290 ? 0.9875 0.8361 1.0214 -0.0228 0.0308 -0.0298 290 PRO A CB 2309 C CG . PRO A 290 ? 0.9490 0.8321 1.0314 -0.0015 0.0286 -0.0315 290 PRO A CG 2310 C CD . PRO A 290 ? 0.9167 0.8617 1.0340 -0.0099 0.0325 -0.0389 290 PRO A CD 2311 N N . PHE A 291 ? 0.8438 0.7714 0.9617 0.0131 0.0300 -0.0381 291 PHE A N 2312 C CA . PHE A 291 ? 0.8227 0.7560 0.9516 0.0295 0.0285 -0.0404 291 PHE A CA 2313 C C . PHE A 291 ? 0.7624 0.7372 0.9287 0.0305 0.0331 -0.0487 291 PHE A C 2314 O O . PHE A 291 ? 0.7538 0.7485 0.9397 0.0308 0.0360 -0.0518 291 PHE A O 2315 C CB . PHE A 291 ? 0.8289 0.7557 0.9659 0.0506 0.0252 -0.0403 291 PHE A CB 2316 C CG . PHE A 291 ? 0.8756 0.7608 0.9716 0.0612 0.0194 -0.0338 291 PHE A CG 2317 C CD1 . PHE A 291 ? 0.9404 0.7974 0.9941 0.0722 0.0152 -0.0306 291 PHE A CD1 2318 C CD2 . PHE A 291 ? 0.9028 0.7730 0.9963 0.0649 0.0179 -0.0310 291 PHE A CD2 2319 C CE1 . PHE A 291 ? 0.9850 0.7924 0.9879 0.0901 0.0096 -0.0249 291 PHE A CE1 2320 C CE2 . PHE A 291 ? 0.9515 0.7775 1.0007 0.0787 0.0124 -0.0261 291 PHE A CE2 2321 C CZ . PHE A 291 ? 0.9849 0.7762 0.9857 0.0931 0.0083 -0.0231 291 PHE A CZ 2322 N N . HIS A 292 ? 0.7563 0.7417 0.9271 0.0346 0.0335 -0.0530 292 HIS A N 2323 C CA . HIS A 292 ? 0.7261 0.7387 0.9255 0.0380 0.0388 -0.0625 292 HIS A CA 2324 C C . HIS A 292 ? 0.7018 0.7221 0.9047 0.0441 0.0390 -0.0684 292 HIS A C 2325 O O . HIS A 292 ? 0.6782 0.6920 0.8618 0.0509 0.0335 -0.0650 292 HIS A O 2326 C CB . HIS A 292 ? 0.7446 0.7819 0.9474 0.0286 0.0412 -0.0669 292 HIS A CB 2327 C CG . HIS A 292 ? 0.7732 0.8113 0.9579 0.0202 0.0393 -0.0657 292 HIS A CG 2328 N ND1 . HIS A 292 ? 0.7528 0.8089 0.9473 0.0235 0.0410 -0.0730 292 HIS A ND1 2329 C CD2 . HIS A 292 ? 0.7962 0.8125 0.9453 0.0081 0.0366 -0.0580 292 HIS A CD2 2330 C CE1 . HIS A 292 ? 0.7797 0.8308 0.9496 0.0173 0.0383 -0.0690 292 HIS A CE1 2331 N NE2 . HIS A 292 ? 0.8160 0.8369 0.9538 0.0077 0.0361 -0.0593 292 HIS A NE2 2332 N N . ASN A 293 ? 0.6832 0.7171 0.9039 0.0427 0.0458 -0.0788 293 ASN A N 2333 C CA . ASN A 293 ? 0.6716 0.7259 0.8967 0.0411 0.0484 -0.0891 293 ASN A CA 2334 C C . ASN A 293 ? 0.6954 0.7653 0.9283 0.0332 0.0548 -0.1000 293 ASN A C 2335 O O . ASN A 293 ? 0.6996 0.7837 0.9366 0.0251 0.0613 -0.1128 293 ASN A O 2336 C CB . ASN A 293 ? 0.6787 0.7308 0.9084 0.0382 0.0535 -0.0951 293 ASN A CB 2337 C CG . ASN A 293 ? 0.6799 0.7056 0.9097 0.0311 0.0639 -0.0996 293 ASN A CG 2338 O OD1 . ASN A 293 ? 0.6979 0.7114 0.9264 0.0356 0.0654 -0.0980 293 ASN A OD1 2339 N ND2 . ASN A 293 ? 0.6994 0.7154 0.9239 0.0213 0.0714 -0.1060 293 ASN A ND2 2340 N N . ILE A 294 ? 0.7051 0.7768 0.9379 0.0331 0.0537 -0.0972 294 ILE A N 2341 C CA . ILE A 294 ? 0.7287 0.8152 0.9671 0.0291 0.0592 -0.1078 294 ILE A CA 2342 C C . ILE A 294 ? 0.7155 0.8305 0.9538 0.0243 0.0574 -0.1133 294 ILE A C 2343 O O . ILE A 294 ? 0.7120 0.8404 0.9554 0.0176 0.0638 -0.1268 294 ILE A O 2344 C CB . ILE A 294 ? 0.7478 0.8430 0.9868 0.0323 0.0580 -0.1055 294 ILE A CB 2345 C CG1 . ILE A 294 ? 0.7665 0.8429 1.0039 0.0447 0.0618 -0.1064 294 ILE A CG1 2346 C CG2 . ILE A 294 ? 0.7713 0.8907 1.0141 0.0298 0.0611 -0.1158 294 ILE A CG2 2347 C CD1 . ILE A 294 ? 0.7798 0.8516 1.0155 0.0475 0.0567 -0.0954 294 ILE A CD1 2348 N N . HIS A 295 ? 0.7237 0.8436 0.9491 0.0269 0.0496 -0.1035 295 HIS A N 2349 C CA . HIS A 295 ? 0.7279 0.8719 0.9453 0.0280 0.0468 -0.1065 295 HIS A CA 2350 C C . HIS A 295 ? 0.7423 0.8646 0.9256 0.0351 0.0384 -0.0916 295 HIS A C 2351 O O . HIS A 295 ? 0.7356 0.8309 0.9039 0.0275 0.0375 -0.0815 295 HIS A O 2352 C CB . HIS A 295 ? 0.7573 0.9211 0.9840 0.0192 0.0512 -0.1142 295 HIS A CB 2353 C CG . HIS A 295 ? 0.7808 0.9760 1.0054 0.0191 0.0506 -0.1217 295 HIS A CG 2354 N ND1 . HIS A 295 ? 0.8167 1.0128 1.0164 0.0232 0.0443 -0.1124 295 HIS A ND1 2355 C CD2 . HIS A 295 ? 0.8044 1.0293 1.0430 0.0142 0.0564 -0.1382 295 HIS A CD2 2356 C CE1 . HIS A 295 ? 0.8200 1.0514 1.0227 0.0255 0.0448 -0.1221 295 HIS A CE1 2357 N NE2 . HIS A 295 ? 0.8030 1.0571 1.0321 0.0182 0.0521 -0.1389 295 HIS A NE2 2358 N N . PRO A 296 ? 0.7661 0.8980 0.9293 0.0502 0.0331 -0.0913 296 PRO A N 2359 C CA . PRO A 296 ? 0.8062 0.8965 0.9188 0.0629 0.0258 -0.0761 296 PRO A CA 2360 C C . PRO A 296 ? 0.8620 0.9283 0.9422 0.0487 0.0268 -0.0676 296 PRO A C 2361 O O . PRO A 296 ? 0.8913 0.9026 0.9229 0.0445 0.0252 -0.0544 296 PRO A O 2362 C CB . PRO A 296 ? 0.8102 0.9273 0.9078 0.0916 0.0195 -0.0812 296 PRO A CB 2363 C CG . PRO A 296 ? 0.7897 0.9713 0.9292 0.0828 0.0249 -0.0996 296 PRO A CG 2364 C CD . PRO A 296 ? 0.7734 0.9542 0.9521 0.0582 0.0339 -0.1061 296 PRO A CD 2365 N N . LEU A 297 ? 0.8699 0.9743 0.9704 0.0385 0.0305 -0.0763 297 LEU A N 2366 C CA . LEU A 297 ? 0.9249 1.0173 0.9964 0.0213 0.0325 -0.0704 297 LEU A CA 2367 C C . LEU A 297 ? 0.9050 1.0040 0.9931 -0.0069 0.0385 -0.0720 297 LEU A C 2368 O O . LEU A 297 ? 0.9105 1.0548 1.0390 -0.0136 0.0426 -0.0841 297 LEU A O 2369 C CB . LEU A 297 ? 0.9119 1.0502 0.9975 0.0247 0.0332 -0.0804 297 LEU A CB 2370 C CG . LEU A 297 ? 0.9536 1.1077 1.0245 0.0547 0.0270 -0.0829 297 LEU A CG 2371 C CD1 . LEU A 297 ? 0.9360 1.1483 1.0303 0.0538 0.0291 -0.0966 297 LEU A CD1 2372 C CD2 . LEU A 297 ? 1.0283 1.1221 1.0243 0.0743 0.0205 -0.0656 297 LEU A CD2 2373 N N . THR A 298 ? 0.9198 0.9762 0.9718 -0.0222 0.0392 -0.0615 298 THR A N 2374 C CA . THR A 298 ? 0.8928 0.9716 0.9579 -0.0498 0.0448 -0.0658 298 THR A CA 2375 C C . THR A 298 ? 0.9416 0.9958 0.9508 -0.0831 0.0494 -0.0594 298 THR A C 2376 O O . THR A 298 ? 0.9709 0.9664 0.9194 -0.0825 0.0483 -0.0479 298 THR A O 2377 C CB . THR A 298 ? 0.8750 0.9414 0.9524 -0.0487 0.0444 -0.0641 298 THR A CB 2378 O OG1 . THR A 298 ? 0.9418 0.9425 0.9618 -0.0570 0.0434 -0.0513 298 THR A OG1 2379 C CG2 . THR A 298 ? 0.8530 0.9276 0.9696 -0.0200 0.0412 -0.0683 298 THR A CG2 2380 N N . ILE A 299 ? 0.9364 1.0374 0.9608 -0.1115 0.0551 -0.0683 299 ILE A N 2381 C CA . ILE A 299 ? 0.9877 1.0770 0.9590 -0.1554 0.0625 -0.0663 299 ILE A CA 2382 C C . ILE A 299 ? 0.9906 1.1226 0.9774 -0.1806 0.0671 -0.0755 299 ILE A C 2383 O O . ILE A 299 ? 0.9259 1.1231 0.9729 -0.1614 0.0646 -0.0870 299 ILE A O 2384 C CB . ILE A 299 ? 1.0075 1.1429 0.9810 -0.1699 0.0661 -0.0736 299 ILE A CB 2385 C CG1 . ILE A 299 ? 1.0637 1.1875 0.9748 -0.2242 0.0761 -0.0729 299 ILE A CG1 2386 C CG2 . ILE A 299 ? 0.9495 1.1802 0.9966 -0.1558 0.0652 -0.0917 299 ILE A CG2 2387 C CD1 . ILE A 299 ? 1.0942 1.2369 0.9856 -0.2396 0.0798 -0.0748 299 ILE A CD1 2388 N N . GLY A 300 ? 1.0735 1.1655 0.9986 -0.2229 0.0743 -0.0712 300 GLY A N 2389 C CA . GLY A 300 ? 1.0935 1.2299 1.0255 -0.2525 0.0795 -0.0816 300 GLY A CA 2390 C C . GLY A 300 ? 1.1619 1.2287 1.0668 -0.2492 0.0780 -0.0719 300 GLY A C 2391 O O . GLY A 300 ? 1.2283 1.2041 1.0949 -0.2284 0.0740 -0.0566 300 GLY A O 2392 N N . GLU A 301 ? 1.2029 1.3192 1.1267 -0.2664 0.0809 -0.0823 301 GLU A N 2393 C CA . GLU A 301 ? 1.2766 1.3367 1.1797 -0.2643 0.0797 -0.0753 301 GLU A CA 2394 C C . GLU A 301 ? 1.1866 1.2674 1.1580 -0.2075 0.0690 -0.0734 301 GLU A C 2395 O O . GLU A 301 ? 1.1431 1.3039 1.1686 -0.1944 0.0672 -0.0851 301 GLU A O 2396 C CB . GLU A 301 ? 1.3607 1.4698 1.2486 -0.3133 0.0888 -0.0891 301 GLU A CB 2397 C CG . GLU A 301 ? 1.5107 1.5176 1.3106 -0.3541 0.0969 -0.0811 301 GLU A CG 2398 C CD . GLU A 301 ? 1.6600 1.5948 1.3682 -0.4030 0.1084 -0.0765 301 GLU A CD 2399 O OE1 . GLU A 301 ? 1.6500 1.6544 1.3496 -0.4528 0.1186 -0.0914 301 GLU A OE1 2400 O OE2 . GLU A 301 ? 1.7784 1.5875 1.4176 -0.3898 0.1074 -0.0584 301 GLU A OE2 2401 N N . CYS A 302 ? 1.1685 1.1782 1.1309 -0.1733 0.0623 -0.0598 302 CYS A N 2402 C CA . CYS A 302 ? 1.0784 1.1052 1.0991 -0.1254 0.0542 -0.0591 302 CYS A CA 2403 C C . CYS A 302 ? 1.0403 1.0117 1.0498 -0.1071 0.0498 -0.0501 302 CYS A C 2404 O O . CYS A 302 ? 1.0649 0.9650 1.0135 -0.1207 0.0512 -0.0415 302 CYS A O 2405 C CB . CYS A 302 ? 1.1053 1.1232 1.1362 -0.0999 0.0503 -0.0561 302 CYS A CB 2406 S SG . CYS A 302 ? 1.1434 1.2380 1.2061 -0.1084 0.0537 -0.0689 302 CYS A SG 2407 N N . PRO A 303 ? 0.9660 0.9639 1.0271 -0.0757 0.0453 -0.0524 303 PRO A N 2408 C CA . PRO A 303 ? 0.9615 0.9117 1.0153 -0.0538 0.0404 -0.0444 303 PRO A CA 2409 C C . PRO A 303 ? 0.9657 0.8741 0.9972 -0.0314 0.0357 -0.0376 303 PRO A C 2410 O O . PRO A 303 ? 0.9770 0.8984 1.0077 -0.0311 0.0363 -0.0395 303 PRO A O 2411 C CB . PRO A 303 ? 0.9052 0.8986 1.0165 -0.0302 0.0388 -0.0501 303 PRO A CB 2412 C CG . PRO A 303 ? 0.8841 0.9418 1.0238 -0.0375 0.0426 -0.0608 303 PRO A CG 2413 C CD . PRO A 303 ? 0.9040 0.9698 1.0222 -0.0590 0.0453 -0.0630 303 PRO A CD 2414 N N . LYS A 304 ? 0.9885 0.8551 1.0014 -0.0102 0.0308 -0.0314 304 LYS A N 2415 C CA . LYS A 304 ? 1.0210 0.8622 1.0105 0.0183 0.0250 -0.0276 304 LYS A CA 2416 C C . LYS A 304 ? 0.9334 0.8295 0.9801 0.0406 0.0228 -0.0360 304 LYS A C 2417 O O . LYS A 304 ? 0.9076 0.8284 0.9937 0.0434 0.0240 -0.0403 304 LYS A O 2418 C CB . LYS A 304 ? 1.1255 0.9007 1.0601 0.0358 0.0203 -0.0194 304 LYS A CB 2419 C CG . LYS A 304 ? 1.2859 0.9825 1.1390 0.0116 0.0245 -0.0111 304 LYS A CG 2420 C CD . LYS A 304 ? 1.3884 1.0550 1.1920 0.0089 0.0259 -0.0068 304 LYS A CD 2421 C CE . LYS A 304 ? 1.4964 1.0716 1.2048 -0.0237 0.0334 0.0011 304 LYS A CE 2422 N NZ . LYS A 304 ? 1.4887 1.0919 1.2137 -0.0775 0.0433 -0.0055 304 LYS A NZ 2423 N N . TYR A 305 ? 0.8898 0.8029 0.9347 0.0536 0.0209 -0.0392 305 TYR A N 2424 C CA . TYR A 305 ? 0.8388 0.8059 0.9306 0.0658 0.0213 -0.0505 305 TYR A CA 2425 C C . TYR A 305 ? 0.8402 0.8126 0.9276 0.0922 0.0157 -0.0527 305 TYR A C 2426 O O . TYR A 305 ? 0.8951 0.8394 0.9361 0.1155 0.0089 -0.0472 305 TYR A O 2427 C CB . TYR A 305 ? 0.8308 0.8258 0.9241 0.0668 0.0219 -0.0561 305 TYR A CB 2428 C CG . TYR A 305 ? 0.7740 0.8245 0.9086 0.0728 0.0243 -0.0707 305 TYR A CG 2429 C CD1 . TYR A 305 ? 0.7342 0.8081 0.9088 0.0560 0.0323 -0.0800 305 TYR A CD1 2430 C CD2 . TYR A 305 ? 0.7844 0.8633 0.9107 0.0953 0.0194 -0.0771 305 TYR A CD2 2431 C CE1 . TYR A 305 ? 0.7206 0.8322 0.9204 0.0536 0.0374 -0.0949 305 TYR A CE1 2432 C CE2 . TYR A 305 ? 0.7686 0.9056 0.9292 0.0915 0.0239 -0.0942 305 TYR A CE2 2433 C CZ . TYR A 305 ? 0.7366 0.8835 0.9315 0.0666 0.0340 -0.1029 305 TYR A CZ 2434 O OH . TYR A 305 ? 0.7266 0.9182 0.9434 0.0552 0.0413 -0.1211 305 TYR A OH 2435 N N . VAL A 306 ? 0.7942 0.8009 0.9231 0.0896 0.0192 -0.0616 306 VAL A N 2436 C CA . VAL A 306 ? 0.7714 0.8089 0.9059 0.1085 0.0160 -0.0696 306 VAL A CA 2437 C C . VAL A 306 ? 0.7317 0.8232 0.9064 0.0938 0.0241 -0.0859 306 VAL A C 2438 O O . VAL A 306 ? 0.7384 0.8248 0.9341 0.0729 0.0321 -0.0881 306 VAL A O 2439 C CB . VAL A 306 ? 0.7783 0.7927 0.9098 0.1131 0.0142 -0.0644 306 VAL A CB 2440 C CG1 . VAL A 306 ? 0.8416 0.7940 0.9228 0.1243 0.0078 -0.0505 306 VAL A CG1 2441 C CG2 . VAL A 306 ? 0.7536 0.7629 0.9172 0.0897 0.0223 -0.0643 306 VAL A CG2 2442 N N . LYS A 307 ? 0.7619 0.9053 0.9411 0.1047 0.0227 -0.0989 307 LYS A N 2443 C CA . LYS A 307 ? 0.7773 0.9718 0.9853 0.0821 0.0331 -0.1178 307 LYS A CA 2444 C C . LYS A 307 ? 0.7745 0.9656 0.9964 0.0639 0.0412 -0.1226 307 LYS A C 2445 O O . LYS A 307 ? 0.8667 1.0988 1.0994 0.0425 0.0508 -0.1401 307 LYS A O 2446 C CB . LYS A 307 ? 0.7792 1.0498 0.9846 0.0962 0.0295 -0.1344 307 LYS A CB 2447 C CG . LYS A 307 ? 0.8129 1.0972 1.0112 0.1023 0.0270 -0.1357 307 LYS A CG 2448 C CD . LYS A 307 ? 0.8601 1.2096 1.0403 0.1357 0.0175 -0.1455 307 LYS A CD 2449 C CE . LYS A 307 ? 0.8729 1.3192 1.0788 0.1165 0.0254 -0.1735 307 LYS A CE 2450 N NZ . LYS A 307 ? 0.9214 1.4495 1.1097 0.1562 0.0145 -0.1856 307 LYS A NZ 2451 N N . SER A 308 ? 0.7477 0.8901 0.9646 0.0683 0.0388 -0.1083 308 SER A N 2452 C CA . SER A 308 ? 0.7256 0.8584 0.9506 0.0529 0.0465 -0.1108 308 SER A CA 2453 C C . SER A 308 ? 0.7300 0.8290 0.9595 0.0279 0.0596 -0.1129 308 SER A C 2454 O O . SER A 308 ? 0.7445 0.8201 0.9743 0.0283 0.0602 -0.1080 308 SER A O 2455 C CB . SER A 308 ? 0.7041 0.7975 0.9204 0.0679 0.0395 -0.0951 308 SER A CB 2456 O OG . SER A 308 ? 0.7184 0.8150 0.9151 0.0957 0.0270 -0.0895 308 SER A OG 2457 N N . ASN A 309 ? 0.7639 0.8573 0.9900 0.0079 0.0705 -0.1206 309 ASN A N 2458 C CA . ASN A 309 ? 0.8275 0.8655 1.0403 -0.0084 0.0831 -0.1196 309 ASN A CA 2459 C C . ASN A 309 ? 0.8088 0.8010 1.0160 0.0055 0.0802 -0.1036 309 ASN A C 2460 O O . ASN A 309 ? 0.8465 0.7900 1.0386 0.0069 0.0866 -0.0989 309 ASN A O 2461 C CB . ASN A 309 ? 0.9064 0.9488 1.1025 -0.0430 0.0996 -0.1373 309 ASN A CB 2462 C CG . ASN A 309 ? 0.9827 1.0656 1.1796 -0.0637 0.1065 -0.1564 309 ASN A CG 2463 O OD1 . ASN A 309 ? 1.0037 1.0736 1.2025 -0.0574 0.1055 -0.1554 309 ASN A OD1 2464 N ND2 . ASN A 309 ? 1.0308 1.1716 1.2263 -0.0901 0.1139 -0.1760 309 ASN A ND2 2465 N N . ARG A 310 ? 0.7657 0.7752 0.9810 0.0193 0.0702 -0.0962 310 ARG A N 2466 C CA . ARG A 310 ? 0.7792 0.7560 0.9898 0.0286 0.0682 -0.0839 310 ARG A CA 2467 C C . ARG A 310 ? 0.7350 0.7271 0.9521 0.0480 0.0544 -0.0751 310 ARG A C 2468 O O . ARG A 310 ? 0.7363 0.7635 0.9546 0.0528 0.0498 -0.0811 310 ARG A O 2469 C CB . ARG A 310 ? 0.8319 0.7969 1.0282 0.0092 0.0801 -0.0904 310 ARG A CB 2470 C CG . ARG A 310 ? 0.9035 0.8239 1.0874 0.0175 0.0815 -0.0782 310 ARG A CG 2471 C CD . ARG A 310 ? 0.9833 0.8845 1.1435 -0.0058 0.0951 -0.0844 310 ARG A CD 2472 N NE . ARG A 310 ? 1.0740 0.9515 1.2279 0.0063 0.0926 -0.0724 310 ARG A NE 2473 C CZ . ARG A 310 ? 1.1310 0.9564 1.2650 0.0220 0.0947 -0.0611 310 ARG A CZ 2474 N NH1 . ARG A 310 ? 1.1942 0.9827 1.3100 0.0306 0.0992 -0.0604 310 ARG A NH1 2475 N NH2 . ARG A 310 ? 1.1490 0.9636 1.2792 0.0329 0.0918 -0.0516 310 ARG A NH2 2476 N N . LEU A 311 ? 0.6991 0.6666 0.9148 0.0595 0.0485 -0.0629 311 LEU A N 2477 C CA . LEU A 311 ? 0.7181 0.6819 0.9283 0.0723 0.0386 -0.0547 311 LEU A CA 2478 C C . LEU A 311 ? 0.6983 0.6390 0.9079 0.0740 0.0393 -0.0460 311 LEU A C 2479 O O . LEU A 311 ? 0.7017 0.6357 0.9116 0.0742 0.0392 -0.0421 311 LEU A O 2480 C CB . LEU A 311 ? 0.7171 0.6765 0.9148 0.0797 0.0303 -0.0506 311 LEU A CB 2481 C CG . LEU A 311 ? 0.7252 0.7080 0.9159 0.0873 0.0268 -0.0577 311 LEU A CG 2482 C CD1 . LEU A 311 ? 0.7455 0.7070 0.9134 0.0918 0.0212 -0.0513 311 LEU A CD1 2483 C CD2 . LEU A 311 ? 0.7477 0.7513 0.9294 0.1040 0.0212 -0.0624 311 LEU A CD2 2484 N N . VAL A 312 ? 0.6777 0.6159 0.8865 0.0759 0.0400 -0.0447 312 VAL A N 2485 C CA . VAL A 312 ? 0.6678 0.5896 0.8749 0.0799 0.0406 -0.0372 312 VAL A CA 2486 C C . VAL A 312 ? 0.6446 0.5676 0.8477 0.0862 0.0338 -0.0337 312 VAL A C 2487 O O . VAL A 312 ? 0.6081 0.5433 0.8112 0.0870 0.0339 -0.0381 312 VAL A O 2488 C CB . VAL A 312 ? 0.6778 0.5824 0.8788 0.0757 0.0513 -0.0384 312 VAL A CB 2489 C CG1 . VAL A 312 ? 0.6932 0.5838 0.8883 0.0866 0.0508 -0.0301 312 VAL A CG1 2490 C CG2 . VAL A 312 ? 0.6845 0.5758 0.8790 0.0717 0.0590 -0.0429 312 VAL A CG2 2491 N N . LEU A 313 ? 0.6485 0.5632 0.8453 0.0885 0.0286 -0.0280 313 LEU A N 2492 C CA . LEU A 313 ? 0.6578 0.5643 0.8437 0.0931 0.0228 -0.0251 313 LEU A CA 2493 C C . LEU A 313 ? 0.6614 0.5709 0.8545 0.0951 0.0256 -0.0216 313 LEU A C 2494 O O . LEU A 313 ? 0.6699 0.5848 0.8678 0.0953 0.0289 -0.0194 313 LEU A O 2495 C CB . LEU A 313 ? 0.6733 0.5632 0.8386 0.0864 0.0184 -0.0228 313 LEU A CB 2496 C CG . LEU A 313 ? 0.7127 0.5797 0.8506 0.0866 0.0144 -0.0236 313 LEU A CG 2497 C CD1 . LEU A 313 ? 0.7318 0.5779 0.8434 0.0677 0.0150 -0.0219 313 LEU A CD1 2498 C CD2 . LEU A 313 ? 0.7508 0.5997 0.8652 0.1053 0.0082 -0.0246 313 LEU A CD2 2499 N N . ALA A 314 ? 0.6532 0.5634 0.8440 0.1002 0.0237 -0.0218 314 ALA A N 2500 C CA . ALA A 314 ? 0.6506 0.5619 0.8435 0.1029 0.0249 -0.0177 314 ALA A CA 2501 C C . ALA A 314 ? 0.6684 0.5774 0.8526 0.1002 0.0201 -0.0158 314 ALA A C 2502 O O . ALA A 314 ? 0.6779 0.5706 0.8438 0.0968 0.0152 -0.0177 314 ALA A O 2503 C CB . ALA A 314 ? 0.6610 0.5790 0.8529 0.1071 0.0239 -0.0201 314 ALA A CB 2504 N N . THR A 315 ? 0.6701 0.5937 0.8599 0.1016 0.0223 -0.0134 315 THR A N 2505 C CA . THR A 315 ? 0.6788 0.6147 0.8612 0.0942 0.0193 -0.0149 315 THR A CA 2506 C C . THR A 315 ? 0.6575 0.6024 0.8433 0.1032 0.0191 -0.0122 315 THR A C 2507 O O . THR A 315 ? 0.6526 0.5940 0.8284 0.0976 0.0158 -0.0141 315 THR A O 2508 C CB . THR A 315 ? 0.6904 0.6594 0.8777 0.0900 0.0213 -0.0180 315 THR A CB 2509 O OG1 . THR A 315 ? 0.7002 0.6774 0.8972 0.1091 0.0252 -0.0150 315 THR A OG1 2510 C CG2 . THR A 315 ? 0.6963 0.6593 0.8742 0.0727 0.0213 -0.0222 315 THR A CG2 2511 N N . GLY A 316 ? 0.6408 0.5901 0.8333 0.1172 0.0235 -0.0077 316 GLY A N 2512 C CA . GLY A 316 ? 0.6344 0.5878 0.8251 0.1271 0.0243 -0.0037 316 GLY A CA 2513 C C . GLY A 316 ? 0.6269 0.5618 0.8161 0.1249 0.0253 -0.0027 316 GLY A C 2514 O O . GLY A 316 ? 0.6011 0.5285 0.7908 0.1184 0.0228 -0.0071 316 GLY A O 2515 N N . LEU A 317 ? 0.6436 0.5757 0.8274 0.1321 0.0290 0.0020 317 LEU A N 2516 C CA . LEU A 317 ? 0.6755 0.6044 0.8578 0.1271 0.0304 0.0008 317 LEU A CA 2517 C C . LEU A 317 ? 0.6869 0.5938 0.8545 0.1217 0.0415 0.0037 317 LEU A C 2518 O O . LEU A 317 ? 0.6928 0.5750 0.8449 0.1273 0.0477 0.0085 317 LEU A O 2519 C CB . LEU A 317 ? 0.6867 0.6305 0.8692 0.1324 0.0262 0.0020 317 LEU A CB 2520 C CG . LEU A 317 ? 0.6923 0.6434 0.8682 0.1449 0.0278 0.0086 317 LEU A CG 2521 C CD1 . LEU A 317 ? 0.7489 0.6731 0.9041 0.1501 0.0374 0.0163 317 LEU A CD1 2522 C CD2 . LEU A 317 ? 0.6842 0.6584 0.8639 0.1464 0.0221 0.0064 317 LEU A CD2 2523 N N . ARG A 318 ? 0.6796 0.5949 0.8459 0.1100 0.0445 -0.0010 318 ARG A N 2524 C CA . ARG A 318 ? 0.7214 0.6170 0.8665 0.0925 0.0578 -0.0019 318 ARG A CA 2525 C C . ARG A 318 ? 0.7583 0.6125 0.8712 0.0993 0.0661 0.0094 318 ARG A C 2526 O O . ARG A 318 ? 0.7483 0.6100 0.8585 0.1078 0.0637 0.0144 318 ARG A O 2527 C CB . ARG A 318 ? 0.7388 0.6713 0.8898 0.0775 0.0587 -0.0120 318 ARG A CB 2528 C CG . ARG A 318 ? 0.8121 0.7345 0.9378 0.0473 0.0748 -0.0175 318 ARG A CG 2529 C CD . ARG A 318 ? 0.8341 0.8141 0.9688 0.0331 0.0749 -0.0304 318 ARG A CD 2530 N NE . ARG A 318 ? 0.8368 0.8726 0.9965 0.0381 0.0662 -0.0451 318 ARG A NE 2531 C CZ . ARG A 318 ? 0.8594 0.9249 1.0173 0.0158 0.0737 -0.0590 318 ARG A CZ 2532 N NH1 . ARG A 318 ? 0.8921 0.9291 1.0208 -0.0205 0.0920 -0.0612 318 ARG A NH1 2533 N NH2 . ARG A 318 ? 0.8514 0.9726 1.0296 0.0301 0.0635 -0.0719 318 ARG A NH2 2534 N N . ASN A 319 ? 0.8330 0.6395 0.9153 0.0982 0.0761 0.0132 319 ASN A N 2535 C CA . ASN A 319 ? 0.9027 0.6545 0.9390 0.1148 0.0839 0.0249 319 ASN A CA 2536 C C . ASN A 319 ? 1.0317 0.7404 1.0224 0.0905 0.0994 0.0268 319 ASN A C 2537 O O . ASN A 319 ? 1.0758 0.7850 1.0607 0.0550 0.1089 0.0168 319 ASN A O 2538 C CB . ASN A 319 ? 0.9042 0.6140 0.9158 0.1292 0.0880 0.0272 319 ASN A CB 2539 C CG . ASN A 319 ? 0.9336 0.6016 0.9012 0.1667 0.0897 0.0388 319 ASN A CG 2540 O OD1 . ASN A 319 ? 0.9043 0.5814 0.8649 0.1832 0.0865 0.0457 319 ASN A OD1 2541 N ND2 . ASN A 319 ? 0.9806 0.6047 0.9148 0.1847 0.0943 0.0402 319 ASN A ND2 2542 N N . SER A 320 ? 1.1851 0.8605 1.1400 0.1082 0.1024 0.0383 320 SER A N 2543 C CA . SER A 320 ? 1.3071 0.9367 1.2105 0.0841 0.1177 0.0418 320 SER A CA 2544 C C . SER A 320 ? 1.4306 0.9533 1.2497 0.0800 0.1361 0.0486 320 SER A C 2545 O O . SER A 320 ? 1.4219 0.9054 1.2170 0.1174 0.1333 0.0560 320 SER A O 2546 C CB . SER A 320 ? 1.2897 0.9323 1.1903 0.1073 0.1118 0.0517 320 SER A CB 2547 O OG . SER A 320 ? 1.2046 0.9332 1.1743 0.1162 0.0946 0.0454 320 SER A OG 2548 N N . PRO A 321 ? 1.5732 1.0485 1.3411 0.0337 0.1557 0.0443 321 PRO A N 2549 C CA . PRO A 321 ? 1.7269 1.0787 1.3941 0.0215 0.1773 0.0502 321 PRO A CA 2550 C C . PRO A 321 ? 1.8045 1.0712 1.3902 0.0421 0.1860 0.0676 321 PRO A C 2551 O O . PRO A 321 ? 1.7670 1.0652 1.3751 0.0889 0.1713 0.0782 321 PRO A O 2552 C CB . PRO A 321 ? 1.7473 1.1042 1.4004 -0.0492 0.1953 0.0331 321 PRO A CB 2553 C CG . PRO A 321 ? 1.6829 1.1458 1.4007 -0.0660 0.1862 0.0251 321 PRO A CG 2554 C CD . PRO A 321 ? 1.5770 1.1177 1.3760 -0.0138 0.1597 0.0300 321 PRO A CD 2555 N N . GLY B 1 ? 0.5876 0.6878 1.0156 -0.0227 -0.1201 0.1180 1 GLY B N 2556 C CA . GLY B 1 ? 0.5536 0.6380 0.9767 0.0022 -0.1098 0.0954 1 GLY B CA 2557 C C . GLY B 1 ? 0.5058 0.6482 0.9457 0.0238 -0.0999 0.0926 1 GLY B C 2558 O O . GLY B 1 ? 0.4855 0.6872 0.9433 0.0267 -0.0962 0.1049 1 GLY B O 2559 N N . LEU B 2 ? 0.4892 0.6105 0.9168 0.0419 -0.0962 0.0760 2 LEU B N 2560 C CA . LEU B 2 ? 0.4783 0.6397 0.9081 0.0676 -0.0913 0.0715 2 LEU B CA 2561 C C . LEU B 2 ? 0.4668 0.6540 0.8995 0.0862 -0.0804 0.0671 2 LEU B C 2562 O O . LEU B 2 ? 0.4451 0.6863 0.8830 0.1075 -0.0785 0.0711 2 LEU B O 2563 C CB . LEU B 2 ? 0.4901 0.6033 0.8938 0.0827 -0.0909 0.0533 2 LEU B CB 2564 C CG . LEU B 2 ? 0.4957 0.5913 0.8929 0.0736 -0.1019 0.0559 2 LEU B CG 2565 C CD1 . LEU B 2 ? 0.5155 0.5567 0.8809 0.0895 -0.0994 0.0377 2 LEU B CD1 2566 C CD2 . LEU B 2 ? 0.4978 0.6637 0.9138 0.0768 -0.1105 0.0713 2 LEU B CD2 2567 N N . PHE B 3 ? 0.4510 0.6039 0.8785 0.0812 -0.0743 0.0589 3 PHE B N 2568 C CA . PHE B 3 ? 0.4598 0.6259 0.8844 0.0992 -0.0657 0.0508 3 PHE B CA 2569 C C . PHE B 3 ? 0.4582 0.6662 0.9013 0.0934 -0.0627 0.0654 3 PHE B C 2570 O O . PHE B 3 ? 0.4746 0.6987 0.9154 0.1098 -0.0565 0.0599 3 PHE B O 2571 C CB . PHE B 3 ? 0.4699 0.5802 0.8753 0.0996 -0.0613 0.0314 3 PHE B CB 2572 C CG . PHE B 3 ? 0.4840 0.5546 0.8642 0.1072 -0.0639 0.0185 3 PHE B CG 2573 C CD1 . PHE B 3 ? 0.4960 0.5595 0.8525 0.1301 -0.0652 0.0080 3 PHE B CD1 2574 C CD2 . PHE B 3 ? 0.5008 0.5371 0.8744 0.0935 -0.0672 0.0179 3 PHE B CD2 2575 C CE1 . PHE B 3 ? 0.5408 0.5584 0.8653 0.1370 -0.0702 -0.0024 3 PHE B CE1 2576 C CE2 . PHE B 3 ? 0.5238 0.5223 0.8707 0.1002 -0.0701 0.0080 3 PHE B CE2 2577 C CZ . PHE B 3 ? 0.5415 0.5285 0.8629 0.1208 -0.0719 -0.0016 3 PHE B CZ 2578 N N . GLY B 4 ? 0.4685 0.6895 0.9249 0.0690 -0.0692 0.0845 4 GLY B N 2579 C CA . GLY B 4 ? 0.4568 0.7227 0.9278 0.0591 -0.0688 0.1045 4 GLY B CA 2580 C C . GLY B 4 ? 0.4683 0.7042 0.9323 0.0539 -0.0660 0.1022 4 GLY B C 2581 O O . GLY B 4 ? 0.5044 0.7658 0.9742 0.0422 -0.0674 0.1204 4 GLY B O 2582 N N . ALA B 5 ? 0.4598 0.6460 0.9100 0.0619 -0.0625 0.0814 5 ALA B N 2583 C CA . ALA B 5 ? 0.4586 0.6260 0.9022 0.0633 -0.0596 0.0772 5 ALA B CA 2584 C C . ALA B 5 ? 0.4794 0.6038 0.9086 0.0452 -0.0696 0.0855 5 ALA B C 2585 O O . ALA B 5 ? 0.5016 0.6292 0.9263 0.0351 -0.0748 0.1015 5 ALA B O 2586 C CB . ALA B 5 ? 0.4638 0.6097 0.8998 0.0785 -0.0524 0.0535 5 ALA B CB 2587 N N . ILE B 6 ? 0.4933 0.5730 0.9090 0.0425 -0.0737 0.0750 6 ILE B N 2588 C CA . ILE B 6 ? 0.5394 0.5667 0.9296 0.0338 -0.0850 0.0782 6 ILE B CA 2589 C C . ILE B 6 ? 0.5663 0.5836 0.9489 0.0077 -0.1015 0.1015 6 ILE B C 2590 O O . ILE B 6 ? 0.5479 0.5818 0.9415 -0.0048 -0.1063 0.1087 6 ILE B O 2591 C CB . ILE B 6 ? 0.5539 0.5419 0.9291 0.0407 -0.0849 0.0616 6 ILE B CB 2592 C CG1 . ILE B 6 ? 0.5321 0.5313 0.9112 0.0594 -0.0711 0.0427 6 ILE B CG1 2593 C CG2 . ILE B 6 ? 0.5945 0.5234 0.9347 0.0361 -0.1003 0.0654 6 ILE B CG2 2594 C CD1 . ILE B 6 ? 0.5418 0.5195 0.9108 0.0640 -0.0674 0.0287 6 ILE B CD1 2595 N N . ALA B 7 ? 0.6116 0.6005 0.9717 -0.0017 -0.1121 0.1139 7 ALA B N 2596 C CA . ALA B 7 ? 0.6479 0.6272 0.9968 -0.0346 -0.1304 0.1405 7 ALA B CA 2597 C C . ALA B 7 ? 0.6249 0.6856 1.0124 -0.0486 -0.1247 0.1577 7 ALA B C 2598 O O . ALA B 7 ? 0.6350 0.7085 1.0272 -0.0752 -0.1372 0.1746 7 ALA B O 2599 C CB . ALA B 7 ? 0.6817 0.5974 1.0008 -0.0488 -0.1497 0.1402 7 ALA B CB 2600 N N . GLY B 8 ? 0.6083 0.7265 1.0210 -0.0276 -0.1065 0.1521 8 GLY B N 2601 C CA . GLY B 8 ? 0.5836 0.7865 1.0275 -0.0301 -0.0991 0.1674 8 GLY B CA 2602 C C . GLY B 8 ? 0.5872 0.8240 1.0344 -0.0233 -0.0906 0.1770 8 GLY B C 2603 O O . GLY B 8 ? 0.6296 0.8525 1.0614 -0.0469 -0.1004 0.1983 8 GLY B O 2604 N N . PHE B 9 ? 0.5491 0.8222 1.0097 0.0085 -0.0745 0.1615 9 PHE B N 2605 C CA . PHE B 9 ? 0.5532 0.8559 1.0140 0.0195 -0.0664 0.1678 9 PHE B CA 2606 C C . PHE B 9 ? 0.5743 0.8139 1.0108 0.0270 -0.0683 0.1545 9 PHE B C 2607 O O . PHE B 9 ? 0.5866 0.8338 1.0149 0.0310 -0.0659 0.1623 9 PHE B O 2608 C CB . PHE B 9 ? 0.5306 0.8948 1.0079 0.0522 -0.0519 0.1574 9 PHE B CB 2609 C CG . PHE B 9 ? 0.5215 0.8515 0.9917 0.0797 -0.0461 0.1249 9 PHE B CG 2610 C CD1 . PHE B 9 ? 0.5307 0.8372 0.9904 0.0938 -0.0421 0.1105 9 PHE B CD1 2611 C CD2 . PHE B 9 ? 0.5190 0.8433 0.9909 0.0900 -0.0458 0.1103 9 PHE B CD2 2612 C CE1 . PHE B 9 ? 0.5460 0.8263 0.9994 0.1117 -0.0388 0.0835 9 PHE B CE1 2613 C CE2 . PHE B 9 ? 0.5216 0.8109 0.9820 0.1086 -0.0426 0.0836 9 PHE B CE2 2614 C CZ . PHE B 9 ? 0.5365 0.8060 0.9890 0.1167 -0.0394 0.0710 9 PHE B CZ 2615 N N . ILE B 10 ? 0.5797 0.7619 1.0031 0.0312 -0.0724 0.1351 10 ILE B N 2616 C CA . ILE B 10 ? 0.6271 0.7528 1.0233 0.0382 -0.0772 0.1256 10 ILE B CA 2617 C C . ILE B 10 ? 0.6969 0.7621 1.0638 0.0146 -0.0958 0.1380 10 ILE B C 2618 O O . ILE B 10 ? 0.7223 0.7584 1.0847 0.0107 -0.1011 0.1294 10 ILE B O 2619 C CB . ILE B 10 ? 0.5899 0.7019 0.9882 0.0621 -0.0689 0.0961 10 ILE B CB 2620 C CG1 . ILE B 10 ? 0.5565 0.7186 0.9773 0.0798 -0.0556 0.0846 10 ILE B CG1 2621 C CG2 . ILE B 10 ? 0.6148 0.6899 0.9879 0.0762 -0.0722 0.0871 10 ILE B CG2 2622 C CD1 . ILE B 10 ? 0.5466 0.6985 0.9694 0.0935 -0.0497 0.0592 10 ILE B CD1 2623 N N . GLU B 11 ? 0.7628 0.8047 1.1045 -0.0021 -0.1075 0.1592 11 GLU B N 2624 C CA . GLU B 11 ? 0.8441 0.8255 1.1510 -0.0329 -0.1305 0.1773 11 GLU B CA 2625 C C . GLU B 11 ? 0.8454 0.7464 1.1151 -0.0198 -0.1419 0.1583 11 GLU B C 2626 O O . GLU B 11 ? 0.8668 0.7283 1.1197 -0.0394 -0.1576 0.1635 11 GLU B O 2627 C CB . GLU B 11 ? 0.9496 0.9051 1.2236 -0.0524 -0.1432 0.2027 11 GLU B CB 2628 C CG . GLU B 11 ? 1.0205 1.0196 1.3076 -0.0967 -0.1508 0.2384 11 GLU B CG 2629 C CD . GLU B 11 ? 1.1660 1.0944 1.3979 -0.1315 -0.1763 0.2658 11 GLU B CD 2630 O OE1 . GLU B 11 ? 1.2297 1.1125 1.4247 -0.1154 -0.1790 0.2638 11 GLU B OE1 2631 O OE2 . GLU B 11 ? 1.2197 1.1347 1.4410 -0.1761 -0.1958 0.2898 11 GLU B OE2 2632 N N . GLY B 12 ? 0.8231 0.7052 1.0788 0.0148 -0.1347 0.1367 12 GLY B N 2633 C CA . GLY B 12 ? 0.8513 0.6678 1.0686 0.0352 -0.1438 0.1186 12 GLY B CA 2634 C C . GLY B 12 ? 0.8063 0.6459 1.0325 0.0745 -0.1277 0.0926 12 GLY B C 2635 O O . GLY B 12 ? 0.7779 0.6680 1.0294 0.0860 -0.1138 0.0888 12 GLY B O 2636 N N . GLY B 13 ? 0.8087 0.6153 1.0129 0.0945 -0.1303 0.0754 13 GLY B N 2637 C CA . GLY B 13 ? 0.7853 0.6214 0.9964 0.1293 -0.1164 0.0527 13 GLY B CA 2638 C C . GLY B 13 ? 0.8116 0.6236 0.9839 0.1586 -0.1230 0.0488 13 GLY B C 2639 O O . GLY B 13 ? 0.8625 0.6252 0.9980 0.1511 -0.1390 0.0642 13 GLY B O 2640 N N . TRP B 14 ? 0.7856 0.6354 0.9650 0.1909 -0.1114 0.0294 14 TRP B N 2641 C CA . TRP B 14 ? 0.8105 0.6583 0.9608 0.2257 -0.1146 0.0223 14 TRP B CA 2642 C C . TRP B 14 ? 0.8661 0.6918 0.9746 0.2660 -0.1198 0.0061 14 TRP B C 2643 O O . TRP B 14 ? 0.8087 0.6918 0.9448 0.2781 -0.1051 -0.0081 14 TRP B O 2644 C CB . TRP B 14 ? 0.7397 0.6731 0.9393 0.2318 -0.0961 0.0134 14 TRP B CB 2645 C CG . TRP B 14 ? 0.7036 0.6607 0.9338 0.2058 -0.0916 0.0270 14 TRP B CG 2646 C CD1 . TRP B 14 ? 0.7307 0.6476 0.9416 0.1861 -0.1026 0.0479 14 TRP B CD1 2647 C CD2 . TRP B 14 ? 0.6393 0.6672 0.9195 0.1982 -0.0760 0.0212 14 TRP B CD2 2648 N NE1 . TRP B 14 ? 0.6830 0.6502 0.9318 0.1708 -0.0922 0.0556 14 TRP B NE1 2649 C CE2 . TRP B 14 ? 0.6334 0.6630 0.9217 0.1802 -0.0770 0.0380 14 TRP B CE2 2650 C CE3 . TRP B 14 ? 0.5899 0.6779 0.9044 0.2033 -0.0631 0.0046 14 TRP B CE3 2651 C CZ2 . TRP B 14 ? 0.5909 0.6757 0.9165 0.1741 -0.0656 0.0360 14 TRP B CZ2 2652 C CZ3 . TRP B 14 ? 0.5468 0.6803 0.8955 0.1919 -0.0547 0.0030 14 TRP B CZ3 2653 C CH2 . TRP B 14 ? 0.5525 0.6820 0.9047 0.1810 -0.0560 0.0173 14 TRP B CH2 2654 N N . GLN B 15 ? 0.9884 0.7304 1.0251 0.2876 -0.1417 0.0092 15 GLN B N 2655 C CA . GLN B 15 ? 1.0670 0.7865 1.0512 0.3390 -0.1487 -0.0074 15 GLN B CA 2656 C C . GLN B 15 ? 1.0246 0.8336 1.0355 0.3742 -0.1322 -0.0225 15 GLN B C 2657 O O . GLN B 15 ? 1.0394 0.8892 1.0447 0.4099 -0.1253 -0.0379 15 GLN B O 2658 C CB . GLN B 15 ? 1.1911 0.7940 1.0815 0.3603 -0.1791 -0.0016 15 GLN B CB 2659 C CG . GLN B 15 ? 1.2702 0.7748 1.1215 0.3240 -0.2019 0.0144 15 GLN B CG 2660 C CD . GLN B 15 ? 1.3160 0.7888 1.1407 0.3381 -0.2077 0.0034 15 GLN B CD 2661 O OE1 . GLN B 15 ? 1.3217 0.7989 1.1789 0.3003 -0.2048 0.0101 15 GLN B OE1 2662 N NE2 . GLN B 15 ? 1.3879 0.8308 1.1504 0.3967 -0.2161 -0.0140 15 GLN B NE2 2663 N N . GLY B 16 ? 0.9981 0.8429 1.0380 0.3636 -0.1265 -0.0170 16 GLY B N 2664 C CA . GLY B 16 ? 0.9825 0.9094 1.0452 0.3940 -0.1147 -0.0299 16 GLY B CA 2665 C C . GLY B 16 ? 0.9180 0.9542 1.0515 0.3822 -0.0919 -0.0401 16 GLY B C 2666 O O . GLY B 16 ? 0.9096 1.0205 1.0580 0.4092 -0.0842 -0.0519 16 GLY B O 2667 N N . MET B 17 ? 0.8722 0.9182 1.0462 0.3409 -0.0828 -0.0350 17 MET B N 2668 C CA . MET B 17 ? 0.8296 0.9640 1.0614 0.3238 -0.0644 -0.0426 17 MET B CA 2669 C C . MET B 17 ? 0.8411 0.9890 1.0641 0.3357 -0.0594 -0.0497 17 MET B C 2670 O O . MET B 17 ? 0.8398 0.9447 1.0582 0.3157 -0.0608 -0.0447 17 MET B O 2671 C CB . MET B 17 ? 0.8206 0.9588 1.0965 0.2760 -0.0577 -0.0339 17 MET B CB 2672 C CG . MET B 17 ? 0.7876 1.0052 1.1128 0.2569 -0.0431 -0.0415 17 MET B CG 2673 S SD . MET B 17 ? 0.7691 0.9816 1.1311 0.2124 -0.0390 -0.0340 17 MET B SD 2674 C CE . MET B 17 ? 0.8218 0.9629 1.1645 0.1976 -0.0442 -0.0241 17 MET B CE 2675 N N . VAL B 18 ? 0.8501 1.0675 1.0729 0.3688 -0.0530 -0.0608 18 VAL B N 2676 C CA . VAL B 18 ? 0.8826 1.1164 1.0822 0.3966 -0.0497 -0.0676 18 VAL B CA 2677 C C . VAL B 18 ? 0.8290 1.1521 1.0801 0.3695 -0.0310 -0.0687 18 VAL B C 2678 O O . VAL B 18 ? 0.8341 1.1597 1.0740 0.3744 -0.0261 -0.0696 18 VAL B O 2679 C CB . VAL B 18 ? 0.9491 1.2087 1.1064 0.4592 -0.0556 -0.0782 18 VAL B CB 2680 C CG1 . VAL B 18 ? 0.9896 1.3141 1.1377 0.4920 -0.0462 -0.0863 18 VAL B CG1 2681 C CG2 . VAL B 18 ? 1.0256 1.1673 1.1081 0.4889 -0.0786 -0.0765 18 VAL B CG2 2682 N N . ASP B 19 ? 0.7859 1.1756 1.0882 0.3390 -0.0225 -0.0677 19 ASP B N 2683 C CA . ASP B 19 ? 0.7494 1.2329 1.0949 0.3131 -0.0079 -0.0679 19 ASP B CA 2684 C C . ASP B 19 ? 0.6921 1.1527 1.0686 0.2564 -0.0036 -0.0607 19 ASP B C 2685 O O . ASP B 19 ? 0.6951 1.2190 1.1056 0.2241 0.0042 -0.0591 19 ASP B O 2686 C CB . ASP B 19 ? 0.7526 1.3325 1.1267 0.3191 -0.0051 -0.0727 19 ASP B CB 2687 C CG . ASP B 19 ? 0.7721 1.3214 1.1563 0.3069 -0.0136 -0.0725 19 ASP B CG 2688 O OD1 . ASP B 19 ? 0.7636 1.2240 1.1342 0.2942 -0.0203 -0.0672 19 ASP B OD1 2689 O OD2 . ASP B 19 ? 0.7883 1.4086 1.1940 0.3107 -0.0137 -0.0769 19 ASP B OD2 2690 N N . GLY B 20 ? 0.6497 1.0197 1.0106 0.2440 -0.0104 -0.0557 20 GLY B N 2691 C CA . GLY B 20 ? 0.6209 0.9665 1.0036 0.1989 -0.0075 -0.0500 20 GLY B CA 2692 C C . GLY B 20 ? 0.6233 0.8786 0.9858 0.1934 -0.0160 -0.0440 20 GLY B C 2693 O O . GLY B 20 ? 0.6611 0.8682 0.9947 0.2167 -0.0261 -0.0424 20 GLY B O 2694 N N . TRP B 21 ? 0.5969 0.8285 0.9710 0.1617 -0.0137 -0.0398 21 TRP B N 2695 C CA . TRP B 21 ? 0.5924 0.7518 0.9522 0.1541 -0.0220 -0.0331 21 TRP B CA 2696 C C . TRP B 21 ? 0.5360 0.6801 0.9087 0.1429 -0.0273 -0.0281 21 TRP B C 2697 O O . TRP B 21 ? 0.5375 0.6357 0.8964 0.1444 -0.0363 -0.0203 21 TRP B O 2698 C CB . TRP B 21 ? 0.6222 0.7631 0.9842 0.1309 -0.0181 -0.0309 21 TRP B CB 2699 C CG . TRP B 21 ? 0.6766 0.7941 1.0111 0.1461 -0.0185 -0.0315 21 TRP B CG 2700 C CD1 . TRP B 21 ? 0.7339 0.8114 1.0335 0.1745 -0.0282 -0.0320 21 TRP B CD1 2701 C CD2 . TRP B 21 ? 0.7078 0.8317 1.0399 0.1342 -0.0109 -0.0315 21 TRP B CD2 2702 N NE1 . TRP B 21 ? 0.7614 0.8223 1.0374 0.1840 -0.0271 -0.0338 21 TRP B NE1 2703 C CE2 . TRP B 21 ? 0.7442 0.8373 1.0422 0.1594 -0.0150 -0.0330 21 TRP B CE2 2704 C CE3 . TRP B 21 ? 0.7380 0.8837 1.0870 0.1043 -0.0027 -0.0300 21 TRP B CE3 2705 C CZ2 . TRP B 21 ? 0.7843 0.8768 1.0694 0.1576 -0.0089 -0.0329 21 TRP B CZ2 2706 C CZ3 . TRP B 21 ? 0.7782 0.9205 1.1137 0.0988 0.0033 -0.0283 21 TRP B CZ3 2707 C CH2 . TRP B 21 ? 0.7917 0.9118 1.0979 0.1262 0.0014 -0.0297 21 TRP B CH2 2708 N N . TYR B 22 ? 0.4946 0.6792 0.8912 0.1306 -0.0230 -0.0317 22 TYR B N 2709 C CA . TYR B 22 ? 0.4736 0.6512 0.8803 0.1244 -0.0269 -0.0282 22 TYR B CA 2710 C C . TYR B 22 ? 0.4554 0.6807 0.8745 0.1315 -0.0257 -0.0346 22 TYR B C 2711 O O . TYR B 22 ? 0.4551 0.7264 0.8838 0.1281 -0.0212 -0.0416 22 TYR B O 2712 C CB . TYR B 22 ? 0.4592 0.6239 0.8753 0.1007 -0.0263 -0.0274 22 TYR B CB 2713 C CG . TYR B 22 ? 0.4696 0.6059 0.8773 0.0891 -0.0250 -0.0256 22 TYR B CG 2714 C CD1 . TYR B 22 ? 0.4828 0.5797 0.8780 0.0933 -0.0298 -0.0181 22 TYR B CD1 2715 C CD2 . TYR B 22 ? 0.4792 0.6255 0.8883 0.0709 -0.0207 -0.0304 22 TYR B CD2 2716 C CE1 . TYR B 22 ? 0.4918 0.5624 0.8778 0.0842 -0.0297 -0.0171 22 TYR B CE1 2717 C CE2 . TYR B 22 ? 0.4872 0.6044 0.8848 0.0612 -0.0196 -0.0282 22 TYR B CE2 2718 C CZ . TYR B 22 ? 0.4939 0.5745 0.8809 0.0702 -0.0237 -0.0225 22 TYR B CZ 2719 O OH . TYR B 22 ? 0.5035 0.5552 0.8777 0.0627 -0.0236 -0.0210 22 TYR B OH 2720 N N . GLY B 23 ? 0.4597 0.6795 0.8792 0.1389 -0.0299 -0.0311 23 GLY B N 2721 C CA . GLY B 23 ? 0.4610 0.7236 0.8900 0.1477 -0.0303 -0.0377 23 GLY B CA 2722 C C . GLY B 23 ? 0.4737 0.7244 0.8983 0.1578 -0.0346 -0.0317 23 GLY B C 2723 O O . GLY B 23 ? 0.4806 0.7007 0.9021 0.1508 -0.0361 -0.0219 23 GLY B O 2724 N N . TYR B 24 ? 0.4857 0.7680 0.9103 0.1750 -0.0364 -0.0367 24 TYR B N 2725 C CA . TYR B 24 ? 0.4894 0.7699 0.9097 0.1852 -0.0397 -0.0321 24 TYR B CA 2726 C C . TYR B 24 ? 0.5085 0.7813 0.9067 0.2121 -0.0440 -0.0286 24 TYR B C 2727 O O . TYR B 24 ? 0.5108 0.8016 0.9013 0.2295 -0.0446 -0.0361 24 TYR B O 2728 C CB . TYR B 24 ? 0.4890 0.8107 0.9238 0.1817 -0.0410 -0.0431 24 TYR B CB 2729 C CG . TYR B 24 ? 0.4965 0.8205 0.9425 0.1557 -0.0409 -0.0496 24 TYR B CG 2730 C CD1 . TYR B 24 ? 0.4876 0.8384 0.9432 0.1403 -0.0398 -0.0569 24 TYR B CD1 2731 C CD2 . TYR B 24 ? 0.5070 0.8056 0.9485 0.1476 -0.0429 -0.0473 24 TYR B CD2 2732 C CE1 . TYR B 24 ? 0.5032 0.8453 0.9605 0.1126 -0.0422 -0.0610 24 TYR B CE1 2733 C CE2 . TYR B 24 ? 0.5155 0.8020 0.9551 0.1268 -0.0461 -0.0540 24 TYR B CE2 2734 C CZ . TYR B 24 ? 0.5285 0.8313 0.9743 0.1068 -0.0465 -0.0603 24 TYR B CZ 2735 O OH . TYR B 24 ? 0.5951 0.8759 1.0312 0.0822 -0.0521 -0.0650 24 TYR B OH 2736 N N . HIS B 25 ? 0.5273 0.7751 0.9117 0.2171 -0.0474 -0.0165 25 HIS B N 2737 C CA . HIS B 25 ? 0.5610 0.7969 0.9179 0.2425 -0.0536 -0.0127 25 HIS B CA 2738 C C . HIS B 25 ? 0.5470 0.8071 0.9100 0.2474 -0.0531 -0.0114 25 HIS B C 2739 O O . HIS B 25 ? 0.5262 0.7849 0.8992 0.2326 -0.0501 -0.0029 25 HIS B O 2740 C CB . HIS B 25 ? 0.5919 0.7641 0.9152 0.2404 -0.0609 0.0051 25 HIS B CB 2741 C CG . HIS B 25 ? 0.6422 0.7862 0.9252 0.2660 -0.0704 0.0100 25 HIS B CG 2742 N ND1 . HIS B 25 ? 0.6607 0.7898 0.9289 0.2637 -0.0736 0.0254 25 HIS B ND1 2743 C CD2 . HIS B 25 ? 0.6751 0.8040 0.9246 0.2977 -0.0778 0.0013 25 HIS B CD2 2744 C CE1 . HIS B 25 ? 0.7022 0.7987 0.9269 0.2901 -0.0837 0.0267 25 HIS B CE1 2745 N NE2 . HIS B 25 ? 0.7143 0.8093 0.9256 0.3137 -0.0870 0.0110 25 HIS B NE2 2746 N N . HIS B 26 ? 0.5719 0.8578 0.9267 0.2717 -0.0565 -0.0201 26 HIS B N 2747 C CA . HIS B 26 ? 0.5778 0.8861 0.9346 0.2796 -0.0571 -0.0201 26 HIS B CA 2748 C C . HIS B 26 ? 0.6159 0.8999 0.9361 0.3056 -0.0637 -0.0117 26 HIS B C 2749 O O . HIS B 26 ? 0.6321 0.8928 0.9254 0.3246 -0.0695 -0.0131 26 HIS B O 2750 C CB . HIS B 26 ? 0.5585 0.9249 0.9397 0.2813 -0.0575 -0.0396 26 HIS B CB 2751 C CG . HIS B 26 ? 0.5722 0.9728 0.9473 0.3066 -0.0619 -0.0509 26 HIS B CG 2752 N ND1 . HIS B 26 ? 0.5960 1.0159 0.9762 0.3096 -0.0606 -0.0581 26 HIS B ND1 2753 C CD2 . HIS B 26 ? 0.5975 1.0211 0.9594 0.3342 -0.0676 -0.0560 26 HIS B CD2 2754 C CE1 . HIS B 26 ? 0.6043 1.0636 0.9758 0.3398 -0.0650 -0.0672 26 HIS B CE1 2755 N NE2 . HIS B 26 ? 0.6230 1.0832 0.9831 0.3549 -0.0700 -0.0666 26 HIS B NE2 2756 N N . SER B 27 ? 0.6444 0.9306 0.9583 0.3085 -0.0634 -0.0028 27 SER B N 2757 C CA . SER B 27 ? 0.6929 0.9531 0.9682 0.3303 -0.0698 0.0079 27 SER B CA 2758 C C . SER B 27 ? 0.6796 0.9775 0.9613 0.3420 -0.0683 0.0040 27 SER B C 2759 O O . SER B 27 ? 0.6433 0.9557 0.9406 0.3278 -0.0623 0.0105 27 SER B O 2760 C CB . SER B 27 ? 0.7315 0.9362 0.9803 0.3123 -0.0716 0.0352 27 SER B CB 2761 O OG . SER B 27 ? 0.8080 0.9535 1.0143 0.3216 -0.0825 0.0406 27 SER B OG 2762 N N . ASN B 28 ? 0.6976 1.0127 0.9638 0.3717 -0.0747 -0.0073 28 ASN B N 2763 C CA . ASN B 28 ? 0.6930 1.0395 0.9585 0.3869 -0.0758 -0.0118 28 ASN B CA 2764 C C . ASN B 28 ? 0.7549 1.0898 0.9814 0.4227 -0.0849 -0.0129 28 ASN B C 2765 O O . ASN B 28 ? 0.7884 1.0787 0.9812 0.4346 -0.0906 -0.0066 28 ASN B O 2766 C CB . ASN B 28 ? 0.6396 1.0436 0.9433 0.3801 -0.0758 -0.0340 28 ASN B CB 2767 C CG . ASN B 28 ? 0.6108 1.0523 0.9291 0.3879 -0.0806 -0.0528 28 ASN B CG 2768 O OD1 . ASN B 28 ? 0.6517 1.0877 0.9475 0.4135 -0.0851 -0.0539 28 ASN B OD1 2769 N ND2 . ASN B 28 ? 0.5616 1.0428 0.9136 0.3668 -0.0809 -0.0670 28 ASN B ND2 2770 N N . GLU B 29 ? 0.7933 1.1617 1.0175 0.4424 -0.0881 -0.0211 29 GLU B N 2771 C CA . GLU B 29 ? 0.8674 1.2239 1.0504 0.4799 -0.0974 -0.0219 29 GLU B CA 2772 C C . GLU B 29 ? 0.8683 1.2504 1.0493 0.5062 -0.1049 -0.0409 29 GLU B C 2773 O O . GLU B 29 ? 0.9079 1.2578 1.0423 0.5398 -0.1137 -0.0389 29 GLU B O 2774 C CB . GLU B 29 ? 0.9157 1.3067 1.0975 0.4960 -0.0996 -0.0276 29 GLU B CB 2775 C CG . GLU B 29 ? 0.9624 1.3303 1.1325 0.4825 -0.0922 -0.0059 29 GLU B CG 2776 C CD . GLU B 29 ? 1.0070 1.4021 1.1647 0.5057 -0.0954 -0.0107 29 GLU B CD 2777 O OE1 . GLU B 29 ? 1.0465 1.4415 1.1751 0.5383 -0.1047 -0.0169 29 GLU B OE1 2778 O OE2 . GLU B 29 ? 1.0344 1.4499 1.2075 0.4948 -0.0893 -0.0088 29 GLU B OE2 2779 N N . GLN B 30 ? 0.8341 1.2744 1.0613 0.4919 -0.1021 -0.0580 30 GLN B N 2780 C CA . GLN B 30 ? 0.8446 1.3318 1.0776 0.5151 -0.1071 -0.0750 30 GLN B CA 2781 C C . GLN B 30 ? 0.8492 1.2912 1.0590 0.5211 -0.1064 -0.0692 30 GLN B C 2782 O O . GLN B 30 ? 0.8600 1.3267 1.0546 0.5548 -0.1118 -0.0801 30 GLN B O 2783 C CB . GLN B 30 ? 0.8233 1.3927 1.1126 0.4906 -0.1051 -0.0917 30 GLN B CB 2784 C CG . GLN B 30 ? 0.8445 1.4655 1.1504 0.4908 -0.1119 -0.1029 30 GLN B CG 2785 C CD . GLN B 30 ? 0.8560 1.5001 1.2018 0.4464 -0.1104 -0.1086 30 GLN B CD 2786 O OE1 . GLN B 30 ? 0.8769 1.4724 1.2225 0.4231 -0.1038 -0.0983 30 GLN B OE1 2787 N NE2 . GLN B 30 ? 0.8541 1.5719 1.2301 0.4346 -0.1183 -0.1242 30 GLN B NE2 2788 N N . GLY B 31 ? 0.8292 1.2093 1.0345 0.4911 -0.1010 -0.0528 31 GLY B N 2789 C CA . GLY B 31 ? 0.8525 1.1789 1.0310 0.4933 -0.1028 -0.0467 31 GLY B CA 2790 C C . GLY B 31 ? 0.8014 1.1102 1.0102 0.4490 -0.0937 -0.0383 31 GLY B C 2791 O O . GLY B 31 ? 0.7827 1.1008 1.0209 0.4182 -0.0867 -0.0318 31 GLY B O 2792 N N . SER B 32 ? 0.7986 1.0821 0.9964 0.4500 -0.0946 -0.0393 32 SER B N 2793 C CA . SER B 32 ? 0.7538 1.0169 0.9759 0.4107 -0.0874 -0.0315 32 SER B CA 2794 C C . SER B 32 ? 0.7398 1.0180 0.9673 0.4171 -0.0857 -0.0423 32 SER B C 2795 O O . SER B 32 ? 0.7764 1.0691 0.9784 0.4560 -0.0913 -0.0529 32 SER B O 2796 C CB . SER B 32 ? 0.7914 0.9670 0.9757 0.3944 -0.0930 -0.0083 32 SER B CB 2797 O OG . SER B 32 ? 0.8582 0.9669 0.9820 0.4207 -0.1064 -0.0054 32 SER B OG 2798 N N . GLY B 33 ? 0.7098 0.9875 0.9677 0.3823 -0.0779 -0.0394 33 GLY B N 2799 C CA . GLY B 33 ? 0.7085 1.0005 0.9719 0.3850 -0.0748 -0.0476 33 GLY B CA 2800 C C . GLY B 33 ? 0.6515 0.9514 0.9537 0.3434 -0.0654 -0.0453 33 GLY B C 2801 O O . GLY B 33 ? 0.6211 0.9194 0.9477 0.3138 -0.0614 -0.0389 33 GLY B O 2802 N N . TYR B 34 ? 0.6602 0.9692 0.9632 0.3459 -0.0623 -0.0509 34 TYR B N 2803 C CA . TYR B 34 ? 0.6278 0.9361 0.9583 0.3108 -0.0546 -0.0487 34 TYR B CA 2804 C C . TYR B 34 ? 0.5915 0.9827 0.9621 0.2982 -0.0459 -0.0601 34 TYR B C 2805 O O . TYR B 34 ? 0.6082 1.0588 0.9798 0.3225 -0.0454 -0.0693 34 TYR B O 2806 C CB . TYR B 34 ? 0.6536 0.9081 0.9511 0.3204 -0.0583 -0.0454 34 TYR B CB 2807 C CG . TYR B 34 ? 0.7090 0.8727 0.9596 0.3256 -0.0711 -0.0320 34 TYR B CG 2808 C CD1 . TYR B 34 ? 0.7038 0.8223 0.9609 0.2905 -0.0723 -0.0173 34 TYR B CD1 2809 C CD2 . TYR B 34 ? 0.7831 0.9060 0.9785 0.3651 -0.0839 -0.0329 34 TYR B CD2 2810 C CE1 . TYR B 34 ? 0.7553 0.7965 0.9701 0.2873 -0.0858 -0.0016 34 TYR B CE1 2811 C CE2 . TYR B 34 ? 0.8346 0.8646 0.9793 0.3632 -0.0992 -0.0182 34 TYR B CE2 2812 C CZ . TYR B 34 ? 0.8275 0.8202 0.9847 0.3207 -0.1000 -0.0015 34 TYR B CZ 2813 O OH . TYR B 34 ? 0.9101 0.8171 1.0184 0.3108 -0.1166 0.0164 34 TYR B OH 2814 N N . ALA B 35 ? 0.5745 0.9698 0.9744 0.2597 -0.0405 -0.0582 35 ALA B N 2815 C CA . ALA B 35 ? 0.5617 1.0207 0.9922 0.2379 -0.0346 -0.0653 35 ALA B CA 2816 C C . ALA B 35 ? 0.5756 1.0006 1.0138 0.2049 -0.0299 -0.0602 35 ALA B C 2817 O O . ALA B 35 ? 0.5637 0.9433 1.0029 0.1862 -0.0316 -0.0548 35 ALA B O 2818 C CB . ALA B 35 ? 0.5396 1.0440 0.9934 0.2226 -0.0378 -0.0711 35 ALA B CB 2819 N N . ALA B 36 ? 0.6014 1.0526 1.0424 0.2018 -0.0240 -0.0617 36 ALA B N 2820 C CA . ALA B 36 ? 0.6071 1.0307 1.0522 0.1728 -0.0196 -0.0575 36 ALA B CA 2821 C C . ALA B 36 ? 0.6075 1.0493 1.0742 0.1334 -0.0203 -0.0589 36 ALA B C 2822 O O . ALA B 36 ? 0.6185 1.1207 1.1013 0.1244 -0.0221 -0.0638 36 ALA B O 2823 C CB . ALA B 36 ? 0.6156 1.0720 1.0553 0.1831 -0.0126 -0.0584 36 ALA B CB 2824 N N . ASP B 37 ? 0.6202 1.0071 1.0823 0.1110 -0.0214 -0.0549 37 ASP B N 2825 C CA . ASP B 37 ? 0.6271 1.0122 1.0950 0.0750 -0.0249 -0.0566 37 ASP B CA 2826 C C . ASP B 37 ? 0.6701 1.0753 1.1397 0.0529 -0.0189 -0.0537 37 ASP B C 2827 O O . ASP B 37 ? 0.6625 1.0281 1.1208 0.0528 -0.0148 -0.0492 37 ASP B O 2828 C CB . ASP B 37 ? 0.6612 0.9787 1.1163 0.0689 -0.0295 -0.0541 37 ASP B CB 2829 C CG . ASP B 37 ? 0.6997 0.9992 1.1468 0.0388 -0.0374 -0.0579 37 ASP B CG 2830 O OD1 . ASP B 37 ? 0.7295 1.0396 1.1758 0.0362 -0.0458 -0.0637 37 ASP B OD1 2831 O OD2 . ASP B 37 ? 0.7093 0.9767 1.1446 0.0191 -0.0373 -0.0553 37 ASP B OD2 2832 N N . LYS B 38 ? 0.7156 1.1875 1.1991 0.0334 -0.0189 -0.0549 38 LYS B N 2833 C CA . LYS B 38 ? 0.7446 1.2550 1.2318 0.0104 -0.0119 -0.0491 38 LYS B CA 2834 C C . LYS B 38 ? 0.7318 1.1783 1.2011 -0.0232 -0.0145 -0.0443 38 LYS B C 2835 O O . LYS B 38 ? 0.7164 1.1520 1.1777 -0.0246 -0.0065 -0.0389 38 LYS B O 2836 C CB . LYS B 38 ? 0.8122 1.4136 1.3197 -0.0134 -0.0142 -0.0485 38 LYS B CB 2837 C CG . LYS B 38 ? 0.8834 1.5388 1.3964 -0.0458 -0.0069 -0.0386 38 LYS B CG 2838 C CD . LYS B 38 ? 0.9430 1.6462 1.4657 -0.0993 -0.0173 -0.0338 38 LYS B CD 2839 C CE . LYS B 38 ? 0.9432 1.7788 1.4964 -0.0981 -0.0125 -0.0305 38 LYS B CE 2840 N NZ . LYS B 38 ? 0.9349 1.8046 1.5009 -0.0537 -0.0150 -0.0417 38 LYS B NZ 2841 N N . GLU B 39 ? 0.7368 1.1379 1.1942 -0.0463 -0.0270 -0.0472 39 GLU B N 2842 C CA . GLU B 39 ? 0.7777 1.1147 1.2089 -0.0779 -0.0332 -0.0437 39 GLU B CA 2843 C C . GLU B 39 ? 0.7300 1.0030 1.1461 -0.0586 -0.0280 -0.0419 39 GLU B C 2844 O O . GLU B 39 ? 0.7500 1.0030 1.1528 -0.0749 -0.0242 -0.0360 39 GLU B O 2845 C CB . GLU B 39 ? 0.8612 1.1507 1.2711 -0.0959 -0.0511 -0.0498 39 GLU B CB 2846 C CG . GLU B 39 ? 0.9532 1.1514 1.3236 -0.1087 -0.0599 -0.0496 39 GLU B CG 2847 C CD . GLU B 39 ? 1.0435 1.1913 1.3796 -0.1297 -0.0812 -0.0559 39 GLU B CD 2848 O OE1 . GLU B 39 ? 1.0917 1.2598 1.4210 -0.1706 -0.0916 -0.0532 39 GLU B OE1 2849 O OE2 . GLU B 39 ? 1.0800 1.1683 1.3922 -0.1054 -0.0889 -0.0629 39 GLU B OE2 2850 N N . SER B 40 ? 0.6545 0.8979 1.0716 -0.0266 -0.0288 -0.0455 40 SER B N 2851 C CA . SER B 40 ? 0.6255 0.8160 1.0307 -0.0113 -0.0262 -0.0425 40 SER B CA 2852 C C . SER B 40 ? 0.5910 0.8012 1.0022 0.0016 -0.0155 -0.0380 40 SER B C 2853 O O . SER B 40 ? 0.5787 0.7532 0.9759 -0.0019 -0.0134 -0.0343 40 SER B O 2854 C CB . SER B 40 ? 0.6113 0.7771 1.0177 0.0149 -0.0301 -0.0440 40 SER B CB 2855 O OG . SER B 40 ? 0.6103 0.8167 1.0342 0.0347 -0.0278 -0.0451 40 SER B OG 2856 N N . THR B 41 ? 0.5528 0.8176 0.9794 0.0196 -0.0101 -0.0391 41 THR B N 2857 C CA . THR B 41 ? 0.5391 0.8228 0.9625 0.0385 -0.0017 -0.0367 41 THR B CA 2858 C C . THR B 41 ? 0.5396 0.8425 0.9578 0.0145 0.0051 -0.0320 41 THR B C 2859 O O . THR B 41 ? 0.5408 0.8166 0.9442 0.0215 0.0090 -0.0290 41 THR B O 2860 C CB . THR B 41 ? 0.5406 0.8838 0.9739 0.0672 0.0014 -0.0403 41 THR B CB 2861 O OG1 . THR B 41 ? 0.5399 0.8548 0.9706 0.0905 -0.0053 -0.0424 41 THR B OG1 2862 C CG2 . THR B 41 ? 0.5442 0.9045 0.9641 0.0926 0.0085 -0.0394 41 THR B CG2 2863 N N . GLN B 42 ? 0.5626 0.9118 0.9905 -0.0163 0.0053 -0.0300 42 GLN B N 2864 C CA . GLN B 42 ? 0.5909 0.9671 1.0131 -0.0458 0.0119 -0.0217 42 GLN B CA 2865 C C . GLN B 42 ? 0.6209 0.9179 1.0166 -0.0685 0.0074 -0.0180 42 GLN B C 2866 O O . GLN B 42 ? 0.6310 0.9269 1.0142 -0.0758 0.0148 -0.0113 42 GLN B O 2867 C CB . GLN B 42 ? 0.6073 1.0523 1.0445 -0.0823 0.0096 -0.0176 42 GLN B CB 2868 C CG . GLN B 42 ? 0.6408 1.1310 1.0743 -0.1173 0.0173 -0.0049 42 GLN B CG 2869 C CD . GLN B 42 ? 0.6424 1.1968 1.0826 -0.0852 0.0339 -0.0015 42 GLN B CD 2870 O OE1 . GLN B 42 ? 0.6481 1.1839 1.0707 -0.0885 0.0414 0.0052 42 GLN B OE1 2871 N NE2 . GLN B 42 ? 0.6308 1.2584 1.0908 -0.0499 0.0386 -0.0069 42 GLN B NE2 2872 N N . LYS B 43 ? 0.6474 0.8808 1.0308 -0.0764 -0.0048 -0.0224 43 LYS B N 2873 C CA . LYS B 43 ? 0.7111 0.8642 1.0643 -0.0861 -0.0107 -0.0209 43 LYS B CA 2874 C C . LYS B 43 ? 0.6702 0.7966 1.0196 -0.0564 -0.0047 -0.0206 43 LYS B C 2875 O O . LYS B 43 ? 0.7109 0.8004 1.0386 -0.0649 -0.0036 -0.0163 43 LYS B O 2876 C CB . LYS B 43 ? 0.7845 0.8803 1.1225 -0.0858 -0.0252 -0.0276 43 LYS B CB 2877 C CG . LYS B 43 ? 0.9084 1.0004 1.2314 -0.1213 -0.0373 -0.0283 43 LYS B CG 2878 C CD . LYS B 43 ? 0.9915 1.0357 1.2979 -0.1097 -0.0520 -0.0376 43 LYS B CD 2879 C CE . LYS B 43 ? 1.0718 1.0296 1.3364 -0.1027 -0.0616 -0.0399 43 LYS B CE 2880 N NZ . LYS B 43 ? 1.1355 1.0395 1.3545 -0.1409 -0.0732 -0.0360 43 LYS B NZ 2881 N N . ALA B 44 ? 0.5900 0.7305 0.9556 -0.0236 -0.0029 -0.0243 44 ALA B N 2882 C CA . ALA B 44 ? 0.5929 0.7038 0.9502 0.0008 -0.0013 -0.0234 44 ALA B CA 2883 C C . ALA B 44 ? 0.5947 0.7337 0.9444 0.0057 0.0087 -0.0199 44 ALA B C 2884 O O . ALA B 44 ? 0.6314 0.7331 0.9622 0.0090 0.0090 -0.0176 44 ALA B O 2885 C CB . ALA B 44 ? 0.5792 0.6904 0.9474 0.0297 -0.0052 -0.0261 44 ALA B CB 2886 N N . ILE B 45 ? 0.5732 0.7827 0.9361 0.0088 0.0167 -0.0196 45 ILE B N 2887 C CA . ILE B 45 ? 0.5911 0.8410 0.9454 0.0191 0.0277 -0.0159 45 ILE B CA 2888 C C . ILE B 45 ? 0.6231 0.8640 0.9630 -0.0142 0.0326 -0.0073 45 ILE B C 2889 O O . ILE B 45 ? 0.6472 0.8794 0.9682 -0.0035 0.0385 -0.0042 45 ILE B O 2890 C CB . ILE B 45 ? 0.5935 0.9376 0.9667 0.0307 0.0357 -0.0165 45 ILE B CB 2891 C CG1 . ILE B 45 ? 0.5858 0.9265 0.9585 0.0744 0.0306 -0.0250 45 ILE B CG1 2892 C CG2 . ILE B 45 ? 0.5969 1.0023 0.9625 0.0355 0.0492 -0.0100 45 ILE B CG2 2893 C CD1 . ILE B 45 ? 0.5902 1.0193 0.9817 0.0887 0.0352 -0.0275 45 ILE B CD1 2894 N N . ASP B 46 ? 0.6334 0.8697 0.9755 -0.0544 0.0282 -0.0032 46 ASP B N 2895 C CA . ASP B 46 ? 0.6653 0.8785 0.9846 -0.0909 0.0294 0.0065 46 ASP B CA 2896 C C . ASP B 46 ? 0.6629 0.7870 0.9537 -0.0825 0.0234 0.0047 46 ASP B C 2897 O O . ASP B 46 ? 0.7039 0.8142 0.9728 -0.0901 0.0289 0.0115 46 ASP B O 2898 C CB . ASP B 46 ? 0.7016 0.9105 1.0182 -0.1364 0.0200 0.0104 46 ASP B CB 2899 C CG . ASP B 46 ? 0.7257 1.0328 1.0707 -0.1529 0.0248 0.0147 46 ASP B CG 2900 O OD1 . ASP B 46 ? 0.7250 1.1115 1.0894 -0.1294 0.0381 0.0164 46 ASP B OD1 2901 O OD2 . ASP B 46 ? 0.7694 1.0748 1.1143 -0.1871 0.0135 0.0158 46 ASP B OD2 2902 N N . GLY B 47 ? 0.6284 0.6987 0.9194 -0.0662 0.0124 -0.0037 47 GLY B N 2903 C CA . GLY B 47 ? 0.6437 0.6394 0.9106 -0.0578 0.0050 -0.0052 47 GLY B CA 2904 C C . GLY B 47 ? 0.6482 0.6379 0.9089 -0.0305 0.0096 -0.0054 47 GLY B C 2905 O O . GLY B 47 ? 0.6602 0.6129 0.8954 -0.0337 0.0097 -0.0021 47 GLY B O 2906 N N . VAL B 48 ? 0.6348 0.6543 0.9125 -0.0026 0.0113 -0.0097 48 VAL B N 2907 C CA . VAL B 48 ? 0.6378 0.6434 0.9014 0.0261 0.0114 -0.0113 48 VAL B CA 2908 C C . VAL B 48 ? 0.6573 0.6957 0.9047 0.0260 0.0240 -0.0063 48 VAL B C 2909 O O . VAL B 48 ? 0.6837 0.6883 0.9060 0.0377 0.0231 -0.0058 48 VAL B O 2910 C CB . VAL B 48 ? 0.6374 0.6593 0.9119 0.0553 0.0074 -0.0166 48 VAL B CB 2911 C CG1 . VAL B 48 ? 0.6649 0.6675 0.9129 0.0861 0.0049 -0.0190 48 VAL B CG1 2912 C CG2 . VAL B 48 ? 0.6347 0.6208 0.9211 0.0549 -0.0052 -0.0182 48 VAL B CG2 2913 N N . THR B 49 ? 0.6440 0.7528 0.9052 0.0116 0.0354 -0.0015 49 THR B N 2914 C CA . THR B 49 ? 0.6623 0.8214 0.9113 0.0090 0.0496 0.0065 49 THR B CA 2915 C C . THR B 49 ? 0.6995 0.8181 0.9239 -0.0220 0.0508 0.0155 49 THR B C 2916 O O . THR B 49 ? 0.7279 0.8435 0.9282 -0.0114 0.0576 0.0196 49 THR B O 2917 C CB . THR B 49 ? 0.6460 0.9035 0.9200 -0.0066 0.0606 0.0125 49 THR B CB 2918 O OG1 . THR B 49 ? 0.6052 0.8972 0.8978 0.0258 0.0585 0.0033 49 THR B OG1 2919 C CG2 . THR B 49 ? 0.6578 0.9851 0.9216 -0.0064 0.0770 0.0231 49 THR B CG2 2920 N N . ASN B 50 ? 0.7194 0.8018 0.9431 -0.0576 0.0430 0.0183 50 ASN B N 2921 C CA . ASN B 50 ? 0.7741 0.7996 0.9644 -0.0843 0.0401 0.0259 50 ASN B CA 2922 C C . ASN B 50 ? 0.7827 0.7374 0.9500 -0.0570 0.0328 0.0196 50 ASN B C 2923 O O . ASN B 50 ? 0.8084 0.7347 0.9451 -0.0622 0.0355 0.0256 50 ASN B O 2924 C CB . ASN B 50 ? 0.7982 0.7813 0.9808 -0.1197 0.0280 0.0270 50 ASN B CB 2925 C CG . ASN B 50 ? 0.8217 0.8675 1.0180 -0.1583 0.0320 0.0363 50 ASN B CG 2926 O OD1 . ASN B 50 ? 0.8443 0.9702 1.0527 -0.1660 0.0463 0.0460 50 ASN B OD1 2927 N ND2 . ASN B 50 ? 0.8410 0.8548 1.0336 -0.1818 0.0185 0.0336 50 ASN B ND2 2928 N N . LYS B 51 ? 0.7649 0.6943 0.9462 -0.0299 0.0227 0.0087 51 LYS B N 2929 C CA . LYS B 51 ? 0.7753 0.6443 0.9387 -0.0079 0.0125 0.0036 51 LYS B CA 2930 C C . LYS B 51 ? 0.7798 0.6584 0.9246 0.0154 0.0190 0.0042 51 LYS B C 2931 O O . LYS B 51 ? 0.7974 0.6355 0.9128 0.0174 0.0170 0.0063 51 LYS B O 2932 C CB . LYS B 51 ? 0.7603 0.6150 0.9452 0.0111 0.0004 -0.0045 51 LYS B CB 2933 C CG . LYS B 51 ? 0.7872 0.5926 0.9576 0.0308 -0.0120 -0.0079 51 LYS B CG 2934 C CD . LYS B 51 ? 0.7821 0.5826 0.9749 0.0415 -0.0241 -0.0115 51 LYS B CD 2935 C CE . LYS B 51 ? 0.7664 0.5590 0.9716 0.0285 -0.0292 -0.0116 51 LYS B CE 2936 N NZ . LYS B 51 ? 0.7649 0.5531 0.9874 0.0393 -0.0416 -0.0119 51 LYS B NZ 2937 N N . VAL B 52 ? 0.7479 0.6780 0.9049 0.0370 0.0255 0.0016 52 VAL B N 2938 C CA . VAL B 52 ? 0.7675 0.7056 0.8998 0.0679 0.0298 0.0000 52 VAL B CA 2939 C C . VAL B 52 ? 0.8006 0.7581 0.9105 0.0526 0.0439 0.0106 52 VAL B C 2940 O O . VAL B 52 ? 0.8293 0.7457 0.9068 0.0650 0.0413 0.0105 52 VAL B O 2941 C CB . VAL B 52 ? 0.7629 0.7597 0.9055 0.0972 0.0352 -0.0046 52 VAL B CB 2942 C CG1 . VAL B 52 ? 0.8048 0.8085 0.9111 0.1360 0.0390 -0.0073 52 VAL B CG1 2943 C CG2 . VAL B 52 ? 0.7397 0.7063 0.8960 0.1113 0.0197 -0.0132 52 VAL B CG2 2944 N N . ASN B 53 ? 0.7947 0.8135 0.9197 0.0224 0.0573 0.0211 53 ASN B N 2945 C CA . ASN B 53 ? 0.8365 0.8795 0.9395 -0.0003 0.0707 0.0355 53 ASN B CA 2946 C C . ASN B 53 ? 0.8665 0.8236 0.9382 -0.0199 0.0617 0.0386 53 ASN B C 2947 O O . ASN B 53 ? 0.9000 0.8448 0.9393 -0.0173 0.0678 0.0453 53 ASN B O 2948 C CB . ASN B 53 ? 0.8343 0.9548 0.9595 -0.0410 0.0824 0.0489 53 ASN B CB 2949 C CG . ASN B 53 ? 0.8151 1.0341 0.9704 -0.0188 0.0923 0.0467 53 ASN B CG 2950 O OD1 . ASN B 53 ? 0.8284 1.0709 0.9746 0.0284 0.0966 0.0395 53 ASN B OD1 2951 N ND2 . ASN B 53 ? 0.8075 1.0803 0.9934 -0.0502 0.0940 0.0519 53 ASN B ND2 2952 N N . SER B 54 ? 0.8722 0.7712 0.9499 -0.0348 0.0469 0.0332 54 SER B N 2953 C CA . SER B 54 ? 0.9266 0.7424 0.9708 -0.0457 0.0359 0.0341 54 SER B CA 2954 C C . SER B 54 ? 0.9546 0.7276 0.9773 -0.0104 0.0293 0.0266 54 SER B C 2955 O O . SER B 54 ? 0.9916 0.7241 0.9775 -0.0137 0.0289 0.0316 54 SER B O 2956 C CB . SER B 54 ? 0.9145 0.6826 0.9672 -0.0565 0.0201 0.0273 54 SER B CB 2957 O OG . SER B 54 ? 0.9286 0.7049 0.9782 -0.0960 0.0213 0.0357 54 SER B OG 2958 N N . ILE B 55 ? 0.9428 0.7208 0.9842 0.0213 0.0221 0.0154 55 ILE B N 2959 C CA . ILE B 55 ? 0.9893 0.7251 1.0088 0.0527 0.0114 0.0080 55 ILE B CA 2960 C C . ILE B 55 ? 1.0412 0.7976 1.0296 0.0692 0.0237 0.0123 55 ILE B C 2961 O O . ILE B 55 ? 1.0926 0.8045 1.0465 0.0775 0.0191 0.0126 55 ILE B O 2962 C CB . ILE B 55 ? 0.9939 0.7294 1.0345 0.0772 -0.0011 -0.0025 55 ILE B CB 2963 C CG1 . ILE B 55 ? 0.9733 0.6832 1.0387 0.0642 -0.0148 -0.0055 55 ILE B CG1 2964 C CG2 . ILE B 55 ? 1.0324 0.7280 1.0424 0.1083 -0.0135 -0.0092 55 ILE B CG2 2965 C CD1 . ILE B 55 ? 0.9527 0.6738 1.0436 0.0772 -0.0244 -0.0111 55 ILE B CD1 2966 N N . ILE B 56 ? 1.0558 0.8843 1.0548 0.0770 0.0391 0.0157 56 ILE B N 2967 C CA . ILE B 56 ? 1.0990 0.9632 1.0683 0.0977 0.0532 0.0208 56 ILE B CA 2968 C C . ILE B 56 ? 1.1577 1.0137 1.1017 0.0679 0.0634 0.0355 56 ILE B C 2969 O O . ILE B 56 ? 1.1923 1.0226 1.0977 0.0858 0.0645 0.0367 56 ILE B O 2970 C CB . ILE B 56 ? 1.0848 1.0475 1.0739 0.1088 0.0702 0.0243 56 ILE B CB 2971 C CG1 . ILE B 56 ? 1.0636 1.0222 1.0621 0.1471 0.0582 0.0090 56 ILE B CG1 2972 C CG2 . ILE B 56 ? 1.1151 1.1328 1.0741 0.1269 0.0886 0.0334 56 ILE B CG2 2973 C CD1 . ILE B 56 ? 1.0401 1.0919 1.0651 0.1566 0.0712 0.0104 56 ILE B CD1 2974 N N . ASP B 57 ? 1.1907 1.0613 1.1505 0.0222 0.0687 0.0469 57 ASP B N 2975 C CA . ASP B 57 ? 1.2608 1.1189 1.1906 -0.0141 0.0768 0.0640 57 ASP B CA 2976 C C . ASP B 57 ? 1.2724 1.0331 1.1622 -0.0089 0.0626 0.0601 57 ASP B C 2977 O O . ASP B 57 ? 1.2947 1.0431 1.1459 -0.0088 0.0696 0.0694 57 ASP B O 2978 C CB . ASP B 57 ? 1.2942 1.1657 1.2410 -0.0661 0.0774 0.0748 57 ASP B CB 2979 C CG . ASP B 57 ? 1.4055 1.2739 1.3168 -0.1107 0.0860 0.0969 57 ASP B CG 2980 O OD1 . ASP B 57 ? 1.4647 1.4028 1.3675 -0.1122 0.1048 0.1111 57 ASP B OD1 2981 O OD2 . ASP B 57 ? 1.4631 1.2586 1.3502 -0.1434 0.0732 0.1008 57 ASP B OD2 2982 N N . LYS B 58 ? 1.2712 0.9694 1.1701 -0.0025 0.0429 0.0471 58 LYS B N 2983 C CA . LYS B 58 ? 1.3211 0.9346 1.1854 0.0056 0.0274 0.0424 58 LYS B CA 2984 C C . LYS B 58 ? 1.3757 0.9701 1.2135 0.0428 0.0242 0.0362 58 LYS B C 2985 O O . LYS B 58 ? 1.4098 0.9492 1.2080 0.0460 0.0179 0.0378 58 LYS B O 2986 C CB . LYS B 58 ? 1.2994 0.8713 1.1851 0.0107 0.0075 0.0298 58 LYS B CB 2987 C CG . LYS B 58 ? 1.3044 0.8657 1.1971 -0.0219 0.0049 0.0341 58 LYS B CG 2988 C CD . LYS B 58 ? 1.3623 0.8638 1.2028 -0.0461 0.0021 0.0443 58 LYS B CD 2989 C CE . LYS B 58 ? 1.3842 0.9068 1.2203 -0.0912 0.0107 0.0585 58 LYS B CE 2990 N NZ . LYS B 58 ? 1.4607 0.9084 1.2357 -0.1194 0.0033 0.0693 58 LYS B NZ 2991 N N . MET B 59 ? 1.4186 1.0517 1.2717 0.0729 0.0262 0.0283 59 MET B N 2992 C CA . MET B 59 ? 1.5058 1.1130 1.3268 0.1113 0.0192 0.0203 59 MET B CA 2993 C C . MET B 59 ? 1.5950 1.2458 1.3840 0.1230 0.0397 0.0304 59 MET B C 2994 O O . MET B 59 ? 1.6401 1.2721 1.3951 0.1593 0.0350 0.0236 59 MET B O 2995 C CB . MET B 59 ? 1.4816 1.0907 1.3211 0.1412 0.0054 0.0058 59 MET B CB 2996 C CG . MET B 59 ? 1.4462 1.0274 1.3206 0.1293 -0.0131 -0.0014 59 MET B CG 2997 S SD . MET B 59 ? 1.4838 0.9870 1.3427 0.1311 -0.0397 -0.0079 59 MET B SD 2998 C CE . MET B 59 ? 1.5382 1.0009 1.3496 0.1680 -0.0539 -0.0162 59 MET B CE 2999 N N . ASN B 60 ? 1.6541 1.3643 1.4509 0.0918 0.0611 0.0475 60 ASN B N 3000 C CA . ASN B 60 ? 1.7200 1.4937 1.4920 0.0998 0.0836 0.0610 60 ASN B CA 3001 C C . ASN B 60 ? 1.7713 1.4968 1.4904 0.0979 0.0851 0.0697 60 ASN B C 3002 O O . ASN B 60 ? 1.7552 1.5151 1.4429 0.1223 0.0985 0.0755 60 ASN B O 3003 C CB . ASN B 60 ? 1.7261 1.5917 1.5271 0.0604 0.1049 0.0796 60 ASN B CB 3004 C CG . ASN B 60 ? 1.7869 1.6331 1.5672 0.0059 0.1110 0.1009 60 ASN B CG 3005 O OD1 . ASN B 60 ? 1.8352 1.5927 1.5992 -0.0126 0.0947 0.0979 60 ASN B OD1 3006 N ND2 . ASN B 60 ? 1.8034 1.7338 1.5803 -0.0199 0.1334 0.1234 60 ASN B ND2 3007 N N . THR B 61 ? 1.2131 1.6309 1.4011 -0.1338 -0.1431 -0.2305 61 THR B N 3008 C CA . THR B 61 ? 1.2911 1.6178 1.4626 -0.1460 -0.1353 -0.2285 61 THR B CA 3009 C C . THR B 61 ? 1.2765 1.5650 1.4390 -0.1016 -0.1233 -0.2181 61 THR B C 3010 O O . THR B 61 ? 1.3257 1.5878 1.4603 -0.0801 -0.1291 -0.2385 61 THR B O 3011 C CB . THR B 61 ? 1.4208 1.6555 1.5438 -0.1789 -0.1565 -0.2581 61 THR B CB 3012 O OG1 . THR B 61 ? 1.4681 1.7490 1.5911 -0.2270 -0.1726 -0.2710 61 THR B OG1 3013 C CG2 . THR B 61 ? 1.4736 1.6100 1.5718 -0.2049 -0.1568 -0.2461 61 THR B CG2 3014 N N . GLN B 62 ? 1.2288 1.5280 1.4141 -0.0879 -0.1080 -0.1903 62 GLN B N 3015 C CA . GLN B 62 ? 1.2056 1.4826 1.3827 -0.0556 -0.0983 -0.1748 62 GLN B CA 3016 C C . GLN B 62 ? 1.1947 1.4446 1.3852 -0.0526 -0.0841 -0.1538 62 GLN B C 3017 O O . GLN B 62 ? 1.2360 1.5181 1.4501 -0.0665 -0.0803 -0.1492 62 GLN B O 3018 C CB . GLN B 62 ? 1.1689 1.5027 1.3452 -0.0384 -0.1052 -0.1598 62 GLN B CB 3019 C CG . GLN B 62 ? 1.1519 1.4682 1.3195 -0.0210 -0.1011 -0.1294 62 GLN B CG 3020 C CD . GLN B 62 ? 1.1777 1.5267 1.3234 -0.0174 -0.1185 -0.1079 62 GLN B CD 3021 O OE1 . GLN B 62 ? 1.1665 1.5634 1.3039 -0.0252 -0.1292 -0.1175 62 GLN B OE1 3022 N NE2 . GLN B 62 ? 1.2143 1.5277 1.3404 -0.0096 -0.1263 -0.0772 62 GLN B NE2 3023 N N . PHE B 63 ? 1.0925 1.3011 1.2678 -0.0351 -0.0765 -0.1447 63 PHE B N 3024 C CA . PHE B 63 ? 1.0574 1.2311 1.2365 -0.0330 -0.0640 -0.1289 63 PHE B CA 3025 C C . PHE B 63 ? 1.0741 1.2846 1.2759 -0.0233 -0.0608 -0.1146 63 PHE B C 3026 O O . PHE B 63 ? 1.1187 1.3513 1.3194 -0.0039 -0.0720 -0.1054 63 PHE B O 3027 C CB . PHE B 63 ? 0.9987 1.1441 1.1583 -0.0150 -0.0597 -0.1215 63 PHE B CB 3028 C CG . PHE B 63 ? 0.9468 1.0499 1.1038 -0.0146 -0.0491 -0.1095 63 PHE B CG 3029 C CD1 . PHE B 63 ? 0.9426 0.9930 1.0857 -0.0242 -0.0501 -0.1171 63 PHE B CD1 3030 C CD2 . PHE B 63 ? 0.9508 1.0545 1.1091 -0.0059 -0.0439 -0.0902 63 PHE B CD2 3031 C CE1 . PHE B 63 ? 0.9588 0.9745 1.0945 -0.0268 -0.0419 -0.1033 63 PHE B CE1 3032 C CE2 . PHE B 63 ? 0.9143 0.9850 1.0677 -0.0062 -0.0343 -0.0822 63 PHE B CE2 3033 C CZ . PHE B 63 ? 0.9298 0.9650 1.0747 -0.0175 -0.0310 -0.0876 63 PHE B CZ 3034 N N . GLU B 64 ? 1.0781 1.2940 1.2930 -0.0352 -0.0500 -0.1144 64 GLU B N 3035 C CA . GLU B 64 ? 1.0755 1.3373 1.3114 -0.0141 -0.0471 -0.1127 64 GLU B CA 3036 C C . GLU B 64 ? 1.0674 1.2882 1.2915 -0.0101 -0.0338 -0.1045 64 GLU B C 3037 O O . GLU B 64 ? 1.0448 1.2442 1.2599 -0.0405 -0.0227 -0.1022 64 GLU B O 3038 C CB . GLU B 64 ? 1.0843 1.4386 1.3511 -0.0354 -0.0435 -0.1273 64 GLU B CB 3039 C CG . GLU B 64 ? 1.1094 1.5169 1.3895 -0.0455 -0.0578 -0.1376 64 GLU B CG 3040 C CD . GLU B 64 ? 1.1368 1.6542 1.4466 -0.0808 -0.0536 -0.1516 64 GLU B CD 3041 O OE1 . GLU B 64 ? 1.0794 1.6607 1.4070 -0.0831 -0.0401 -0.1560 64 GLU B OE1 3042 O OE2 . GLU B 64 ? 1.1779 1.7305 1.4914 -0.1104 -0.0642 -0.1601 64 GLU B OE2 3043 N N . ALA B 65 ? 1.0865 1.2853 1.3011 0.0244 -0.0404 -0.0988 65 ALA B N 3044 C CA . ALA B 65 ? 1.0952 1.2558 1.2948 0.0296 -0.0303 -0.0939 65 ALA B CA 3045 C C . ALA B 65 ? 1.1017 1.3312 1.3230 0.0353 -0.0184 -0.1109 65 ALA B C 3046 O O . ALA B 65 ? 1.0025 1.3126 1.2505 0.0556 -0.0245 -0.1293 65 ALA B O 3047 C CB . ALA B 65 ? 1.1058 1.2054 1.2745 0.0561 -0.0480 -0.0827 65 ALA B CB 3048 N N . VAL B 66 ? 1.1202 1.3337 1.3291 0.0179 -0.0023 -0.1066 66 VAL B N 3049 C CA . VAL B 66 ? 1.1250 1.4202 1.3479 0.0161 0.0128 -0.1229 66 VAL B CA 3050 C C . VAL B 66 ? 1.1179 1.3681 1.3158 0.0385 0.0158 -0.1245 66 VAL B C 3051 O O . VAL B 66 ? 1.1690 1.3302 1.3386 0.0295 0.0131 -0.1049 66 VAL B O 3052 C CB . VAL B 66 ? 1.1710 1.5035 1.3924 -0.0498 0.0288 -0.1123 66 VAL B CB 3053 C CG1 . VAL B 66 ? 1.2157 1.6495 1.4428 -0.0658 0.0478 -0.1243 66 VAL B CG1 3054 C CG2 . VAL B 66 ? 1.1962 1.5779 1.4376 -0.0773 0.0222 -0.1156 66 VAL B CG2 3055 N N . GLY B 67 ? 1.0912 1.4154 1.2991 0.0704 0.0196 -0.1528 67 GLY B N 3056 C CA . GLY B 67 ? 1.0767 1.3651 1.2568 0.0935 0.0206 -0.1624 67 GLY B CA 3057 C C . GLY B 67 ? 1.0443 1.3412 1.2084 0.0418 0.0447 -0.1455 67 GLY B C 3058 O O . GLY B 67 ? 1.0390 1.4291 1.2160 0.0001 0.0632 -0.1447 67 GLY B O 3059 N N . ARG B 68 ? 1.0036 1.2044 1.1335 0.0382 0.0406 -0.1285 68 ARG B N 3060 C CA . ARG B 68 ? 1.0029 1.1998 1.1082 0.0001 0.0563 -0.1128 68 ARG B CA 3061 C C . ARG B 68 ? 1.0347 1.1788 1.1092 0.0279 0.0492 -0.1227 68 ARG B C 3062 O O . ARG B 68 ? 1.0802 1.1387 1.1384 0.0468 0.0296 -0.1169 68 ARG B O 3063 C CB . ARG B 68 ? 0.9923 1.1156 1.0821 -0.0397 0.0526 -0.0768 68 ARG B CB 3064 C CG . ARG B 68 ? 0.9840 1.1294 1.0871 -0.0756 0.0528 -0.0662 68 ARG B CG 3065 C CD . ARG B 68 ? 0.9934 1.0460 1.0686 -0.0994 0.0396 -0.0397 68 ARG B CD 3066 N NE . ARG B 68 ? 1.0041 1.0476 1.0877 -0.1182 0.0298 -0.0378 68 ARG B NE 3067 C CZ . ARG B 68 ? 0.9631 0.9989 1.0693 -0.0910 0.0210 -0.0484 68 ARG B CZ 3068 N NH1 . ARG B 68 ? 0.9119 0.9415 1.0294 -0.0506 0.0184 -0.0558 68 ARG B NH1 3069 N NH2 . ARG B 68 ? 1.0377 1.0683 1.1466 -0.1118 0.0114 -0.0499 68 ARG B NH2 3070 N N . GLU B 69 ? 1.0060 1.2055 1.0660 0.0217 0.0639 -0.1362 69 GLU B N 3071 C CA . GLU B 69 ? 0.9979 1.1520 1.0232 0.0454 0.0563 -0.1510 69 GLU B CA 3072 C C . GLU B 69 ? 0.9329 1.0608 0.9286 0.0012 0.0656 -0.1212 69 GLU B C 3073 O O . GLU B 69 ? 0.8874 1.0511 0.8825 -0.0438 0.0789 -0.0970 69 GLU B O 3074 C CB . GLU B 69 ? 1.0743 1.3194 1.1011 0.0888 0.0609 -0.2023 69 GLU B CB 3075 C CG . GLU B 69 ? 1.1404 1.3699 1.1791 0.1559 0.0349 -0.2375 69 GLU B CG 3076 C CD . GLU B 69 ? 1.1895 1.5571 1.2478 0.2081 0.0403 -0.2956 69 GLU B CD 3077 O OE1 . GLU B 69 ? 1.1857 1.6847 1.2888 0.1963 0.0576 -0.3011 69 GLU B OE1 3078 O OE2 . GLU B 69 ? 1.2590 1.6109 1.2855 0.2615 0.0251 -0.3396 69 GLU B OE2 3079 N N . PHE B 70 ? 0.9431 1.0001 0.9067 0.0113 0.0525 -0.1213 70 PHE B N 3080 C CA . PHE B 70 ? 0.9388 0.9691 0.8734 -0.0223 0.0549 -0.0942 70 PHE B CA 3081 C C . PHE B 70 ? 0.9682 0.9803 0.8655 -0.0072 0.0482 -0.1173 70 PHE B C 3082 O O . PHE B 70 ? 0.9923 0.9563 0.8764 0.0261 0.0295 -0.1438 70 PHE B O 3083 C CB . PHE B 70 ? 0.9291 0.8909 0.8665 -0.0337 0.0400 -0.0630 70 PHE B CB 3084 C CG . PHE B 70 ? 0.8907 0.8565 0.8584 -0.0414 0.0409 -0.0477 70 PHE B CG 3085 C CD1 . PHE B 70 ? 0.8726 0.8409 0.8333 -0.0709 0.0440 -0.0241 70 PHE B CD1 3086 C CD2 . PHE B 70 ? 0.8772 0.8318 0.8695 -0.0214 0.0329 -0.0565 70 PHE B CD2 3087 C CE1 . PHE B 70 ? 0.8741 0.8298 0.8523 -0.0788 0.0390 -0.0146 70 PHE B CE1 3088 C CE2 . PHE B 70 ? 0.8486 0.8098 0.8655 -0.0290 0.0329 -0.0467 70 PHE B CE2 3089 C CZ . PHE B 70 ? 0.8490 0.8090 0.8591 -0.0569 0.0359 -0.0282 70 PHE B CZ 3090 N N . ASN B 71 ? 1.0017 1.0406 0.8720 -0.0336 0.0580 -0.1070 71 ASN B N 3091 C CA . ASN B 71 ? 1.0361 1.0656 0.8663 -0.0222 0.0520 -0.1331 71 ASN B CA 3092 C C . ASN B 71 ? 1.0542 0.9969 0.8603 -0.0327 0.0290 -0.1157 71 ASN B C 3093 O O . ASN B 71 ? 1.0360 0.9447 0.8609 -0.0441 0.0202 -0.0870 71 ASN B O 3094 C CB . ASN B 71 ? 1.0568 1.1674 0.8627 -0.0497 0.0720 -0.1311 71 ASN B CB 3095 C CG . ASN B 71 ? 1.0667 1.1505 0.8522 -0.0931 0.0681 -0.0807 71 ASN B CG 3096 O OD1 . ASN B 71 ? 1.1091 1.1278 0.8872 -0.0933 0.0496 -0.0637 71 ASN B OD1 3097 N ND2 . ASN B 71 ? 1.0982 1.2375 0.8687 -0.1316 0.0815 -0.0568 71 ASN B ND2 3098 N N . ASN B 72 ? 1.1350 1.0562 0.8977 -0.0317 0.0187 -0.1359 72 ASN B N 3099 C CA . ASN B 72 ? 1.1758 1.0271 0.9092 -0.0512 -0.0060 -0.1235 72 ASN B CA 3100 C C . ASN B 72 ? 1.1265 1.0019 0.8689 -0.0848 -0.0047 -0.0803 72 ASN B C 3101 O O . ASN B 72 ? 1.1664 1.0162 0.9019 -0.1038 -0.0228 -0.0656 72 ASN B O 3102 C CB . ASN B 72 ? 1.2704 1.0894 0.9466 -0.0454 -0.0209 -0.1600 72 ASN B CB 3103 C CG . ASN B 72 ? 1.3320 1.0677 0.9674 -0.0752 -0.0534 -0.1508 72 ASN B CG 3104 O OD1 . ASN B 72 ? 1.3866 1.0705 1.0272 -0.0865 -0.0707 -0.1339 72 ASN B OD1 3105 N ND2 . ASN B 72 ? 1.3946 1.1262 0.9847 -0.0965 -0.0626 -0.1600 72 ASN B ND2 3106 N N . LEU B 73 ? 1.0716 0.9988 0.8229 -0.0930 0.0118 -0.0609 73 LEU B N 3107 C CA . LEU B 73 ? 1.0527 0.9904 0.8063 -0.1088 0.0038 -0.0236 73 LEU B CA 3108 C C . LEU B 73 ? 1.0121 0.9463 0.7994 -0.1018 0.0060 -0.0004 73 LEU B C 3109 O O . LEU B 73 ? 1.0064 0.9381 0.7832 -0.1067 -0.0030 0.0267 73 LEU B O 3110 C CB . LEU B 73 ? 1.1076 1.0758 0.8221 -0.1263 0.0061 -0.0135 73 LEU B CB 3111 C CG . LEU B 73 ? 1.1537 1.1260 0.8283 -0.1355 -0.0010 -0.0360 73 LEU B CG 3112 C CD1 . LEU B 73 ? 1.1704 1.1860 0.8046 -0.1534 0.0061 -0.0283 73 LEU B CD1 3113 C CD2 . LEU B 73 ? 1.1437 1.1047 0.8162 -0.1463 -0.0242 -0.0256 73 LEU B CD2 3114 N N . GLU B 74 ? 0.9611 0.8834 0.7804 -0.0883 0.0116 -0.0125 74 GLU B N 3115 C CA . GLU B 74 ? 0.9267 0.8401 0.7765 -0.0812 0.0103 0.0027 74 GLU B CA 3116 C C . GLU B 74 ? 0.8960 0.7978 0.7725 -0.0687 0.0022 -0.0048 74 GLU B C 3117 O O . GLU B 74 ? 0.8659 0.7634 0.7696 -0.0593 0.0058 -0.0074 74 GLU B O 3118 C CB . GLU B 74 ? 0.9372 0.8692 0.7971 -0.0874 0.0276 -0.0025 74 GLU B CB 3119 C CG . GLU B 74 ? 0.9830 0.9379 0.8090 -0.1172 0.0346 0.0141 74 GLU B CG 3120 C CD . GLU B 74 ? 1.0201 1.0289 0.8561 -0.1359 0.0543 0.0060 74 GLU B CD 3121 O OE1 . GLU B 74 ? 1.0255 1.0713 0.8929 -0.1123 0.0656 -0.0265 74 GLU B OE1 3122 O OE2 . GLU B 74 ? 1.0454 1.0627 0.8527 -0.1769 0.0547 0.0327 74 GLU B OE2 3123 N N . ARG B 75 ? 0.9269 0.8301 0.7901 -0.0770 -0.0103 -0.0061 75 ARG B N 3124 C CA . ARG B 75 ? 0.9264 0.8248 0.7998 -0.0826 -0.0205 -0.0077 75 ARG B CA 3125 C C . ARG B 75 ? 0.8666 0.8023 0.7724 -0.0715 -0.0238 0.0025 75 ARG B C 3126 O O . ARG B 75 ? 0.8827 0.8199 0.8045 -0.0718 -0.0252 0.0008 75 ARG B O 3127 C CB . ARG B 75 ? 1.0245 0.9233 0.8644 -0.1123 -0.0365 -0.0070 75 ARG B CB 3128 C CG . ARG B 75 ? 1.1449 0.9847 0.9409 -0.1197 -0.0426 -0.0261 75 ARG B CG 3129 C CD . ARG B 75 ? 1.2628 1.0402 1.0533 -0.1018 -0.0481 -0.0431 75 ARG B CD 3130 N NE . ARG B 75 ? 1.4534 1.1591 1.1910 -0.0977 -0.0659 -0.0698 75 ARG B NE 3131 C CZ . ARG B 75 ? 1.5557 1.1944 1.2746 -0.0678 -0.0809 -0.0941 75 ARG B CZ 3132 N NH1 . ARG B 75 ? 1.5357 1.1804 1.2895 -0.0459 -0.0770 -0.0904 75 ARG B NH1 3133 N NH2 . ARG B 75 ? 1.6313 1.1940 1.2924 -0.0540 -0.1048 -0.1260 75 ARG B NH2 3134 N N . ARG B 76 ? 0.8635 0.8273 0.7730 -0.0570 -0.0295 0.0104 76 ARG B N 3135 C CA . ARG B 76 ? 0.8229 0.8216 0.7577 -0.0316 -0.0387 0.0091 76 ARG B CA 3136 C C . ARG B 76 ? 0.8288 0.7897 0.7818 -0.0179 -0.0322 0.0052 76 ARG B C 3137 O O . ARG B 76 ? 0.8153 0.8024 0.7899 -0.0119 -0.0327 -0.0026 76 ARG B O 3138 C CB . ARG B 76 ? 0.8365 0.8483 0.7600 -0.0045 -0.0564 0.0136 76 ARG B CB 3139 C CG . ARG B 76 ? 0.8157 0.8986 0.7309 -0.0121 -0.0668 0.0138 76 ARG B CG 3140 C CD . ARG B 76 ? 0.8514 0.9341 0.7499 0.0253 -0.0905 0.0185 76 ARG B CD 3141 N NE . ARG B 76 ? 0.8626 0.8618 0.7238 0.0115 -0.0885 0.0368 76 ARG B NE 3142 C CZ . ARG B 76 ? 0.9105 0.8528 0.7388 0.0343 -0.1120 0.0511 76 ARG B CZ 3143 N NH1 . ARG B 76 ? 0.9732 0.9166 0.8006 0.0876 -0.1449 0.0433 76 ARG B NH1 3144 N NH2 . ARG B 76 ? 0.9387 0.8220 0.7273 0.0040 -0.1067 0.0719 76 ARG B NH2 3145 N N . ILE B 77 ? 0.8780 0.7884 0.8186 -0.0206 -0.0268 0.0115 77 ILE B N 3146 C CA . ILE B 77 ? 0.9032 0.7857 0.8577 -0.0195 -0.0215 0.0086 77 ILE B CA 3147 C C . ILE B 77 ? 0.9019 0.7975 0.8776 -0.0285 -0.0064 -0.0021 77 ILE B C 3148 O O . ILE B 77 ? 0.9052 0.8002 0.9012 -0.0235 -0.0051 -0.0080 77 ILE B O 3149 C CB . ILE B 77 ? 0.9525 0.7909 0.8801 -0.0368 -0.0222 0.0226 77 ILE B CB 3150 C CG1 . ILE B 77 ? 1.0169 0.8767 0.9317 -0.0623 -0.0028 0.0239 77 ILE B CG1 3151 C CG2 . ILE B 77 ? 1.0260 0.8211 0.9180 -0.0228 -0.0498 0.0367 77 ILE B CG2 3152 C CD1 . ILE B 77 ? 1.0993 0.9421 0.9808 -0.0953 -0.0015 0.0422 77 ILE B CD1 3153 N N . GLU B 78 ? 0.8717 0.7705 0.8362 -0.0378 -0.0009 -0.0070 78 GLU B N 3154 C CA . GLU B 78 ? 0.8671 0.7582 0.8391 -0.0352 0.0001 -0.0187 78 GLU B CA 3155 C C . GLU B 78 ? 0.8513 0.7532 0.8318 -0.0380 -0.0112 -0.0137 78 GLU B C 3156 O O . GLU B 78 ? 0.8269 0.7262 0.8216 -0.0324 -0.0130 -0.0173 78 GLU B O 3157 C CB . GLU B 78 ? 0.9585 0.8259 0.9004 -0.0384 -0.0037 -0.0294 78 GLU B CB 3158 C CG . GLU B 78 ? 1.0643 0.8929 0.9954 -0.0283 -0.0179 -0.0416 78 GLU B CG 3159 C CD . GLU B 78 ? 1.2401 1.0236 1.1306 -0.0191 -0.0295 -0.0622 78 GLU B CD 3160 O OE1 . GLU B 78 ? 1.3482 1.1213 1.2093 -0.0380 -0.0332 -0.0592 78 GLU B OE1 3161 O OE2 . GLU B 78 ? 1.3516 1.1110 1.2367 0.0124 -0.0388 -0.0858 78 GLU B OE2 3162 N N . ASN B 79 ? 0.8129 0.7439 0.7839 -0.0491 -0.0192 -0.0059 79 ASN B N 3163 C CA . ASN B 79 ? 0.8191 0.7938 0.7942 -0.0618 -0.0281 -0.0013 79 ASN B CA 3164 C C . ASN B 79 ? 0.7927 0.8026 0.7985 -0.0371 -0.0255 -0.0097 79 ASN B C 3165 O O . ASN B 79 ? 0.7940 0.8302 0.8075 -0.0430 -0.0280 -0.0106 79 ASN B O 3166 C CB . ASN B 79 ? 0.8631 0.8953 0.8242 -0.0819 -0.0359 0.0046 79 ASN B CB 3167 C CG . ASN B 79 ? 0.9060 1.0114 0.8647 -0.1112 -0.0438 0.0107 79 ASN B CG 3168 O OD1 . ASN B 79 ? 1.0156 1.0860 0.9493 -0.1437 -0.0524 0.0225 79 ASN B OD1 3169 N ND2 . ASN B 79 ? 0.9216 1.1345 0.9003 -0.0996 -0.0448 0.0021 79 ASN B ND2 3170 N N . LEU B 80 ? 0.7943 0.7938 0.8075 -0.0113 -0.0253 -0.0156 80 LEU B N 3171 C CA . LEU B 80 ? 0.7922 0.7942 0.8209 0.0161 -0.0310 -0.0283 80 LEU B CA 3172 C C . LEU B 80 ? 0.7875 0.7612 0.8286 0.0082 -0.0234 -0.0301 80 LEU B C 3173 O O . LEU B 80 ? 0.7692 0.7687 0.8237 0.0166 -0.0266 -0.0406 80 LEU B O 3174 C CB . LEU B 80 ? 0.8515 0.8015 0.8633 0.0361 -0.0422 -0.0275 80 LEU B CB 3175 C CG . LEU B 80 ? 0.9029 0.8359 0.9102 0.0753 -0.0645 -0.0454 80 LEU B CG 3176 C CD1 . LEU B 80 ? 0.9732 0.8299 0.9425 0.0903 -0.0873 -0.0365 80 LEU B CD1 3177 C CD2 . LEU B 80 ? 0.9548 0.8555 0.9707 0.0696 -0.0624 -0.0535 80 LEU B CD2 3178 N N . ASN B 81 ? 0.8403 0.7764 0.8772 -0.0058 -0.0137 -0.0235 81 ASN B N 3179 C CA . ASN B 81 ? 0.8178 0.7469 0.8702 -0.0094 -0.0076 -0.0284 81 ASN B CA 3180 C C . ASN B 81 ? 0.8106 0.7574 0.8677 -0.0109 -0.0125 -0.0288 81 ASN B C 3181 O O . ASN B 81 ? 0.7864 0.7456 0.8586 -0.0070 -0.0146 -0.0344 81 ASN B O 3182 C CB . ASN B 81 ? 0.8445 0.7640 0.8926 -0.0175 0.0034 -0.0287 81 ASN B CB 3183 C CG . ASN B 81 ? 0.8411 0.7824 0.9106 -0.0154 0.0084 -0.0393 81 ASN B CG 3184 O OD1 . ASN B 81 ? 0.8692 0.8201 0.9497 -0.0263 0.0103 -0.0406 81 ASN B OD1 3185 N ND2 . ASN B 81 ? 0.8167 0.7619 0.8863 -0.0004 0.0049 -0.0484 81 ASN B ND2 3186 N N . LYS B 82 ? 0.8555 0.7958 0.8904 -0.0228 -0.0190 -0.0201 82 LYS B N 3187 C CA . LYS B 82 ? 0.9048 0.8379 0.9229 -0.0359 -0.0329 -0.0118 82 LYS B CA 3188 C C . LYS B 82 ? 0.8743 0.8672 0.9008 -0.0447 -0.0354 -0.0096 82 LYS B C 3189 O O . LYS B 82 ? 0.8394 0.8384 0.8663 -0.0477 -0.0425 -0.0071 82 LYS B O 3190 C CB . LYS B 82 ? 1.0088 0.9065 0.9843 -0.0604 -0.0466 0.0004 82 LYS B CB 3191 C CG . LYS B 82 ? 1.1624 1.0096 1.0964 -0.0808 -0.0729 0.0149 82 LYS B CG 3192 C CD . LYS B 82 ? 1.3201 1.1307 1.1981 -0.1249 -0.0928 0.0324 82 LYS B CD 3193 C CE . LYS B 82 ? 1.4750 1.1893 1.2871 -0.1494 -0.1318 0.0508 82 LYS B CE 3194 N NZ . LYS B 82 ? 1.4918 1.2369 1.3030 -0.1650 -0.1399 0.0676 82 LYS B NZ 3195 N N . LYS B 83 ? 0.8600 0.9078 0.8924 -0.0439 -0.0315 -0.0142 83 LYS B N 3196 C CA . LYS B 83 ? 0.8610 0.9960 0.9016 -0.0448 -0.0335 -0.0222 83 LYS B CA 3197 C C . LYS B 83 ? 0.7923 0.9322 0.8570 -0.0144 -0.0314 -0.0433 83 LYS B C 3198 O O . LYS B 83 ? 0.7774 0.9753 0.8444 -0.0183 -0.0341 -0.0500 83 LYS B O 3199 C CB . LYS B 83 ? 0.9195 1.1277 0.9633 -0.0365 -0.0336 -0.0317 83 LYS B CB 3200 C CG . LYS B 83 ? 1.0197 1.2586 1.0350 -0.0840 -0.0385 -0.0105 83 LYS B CG 3201 C CD . LYS B 83 ? 1.1270 1.4952 1.1346 -0.1186 -0.0419 -0.0079 83 LYS B CD 3202 C CE . LYS B 83 ? 1.1903 1.6910 1.2178 -0.0983 -0.0403 -0.0299 83 LYS B CE 3203 N NZ . LYS B 83 ? 1.1685 1.7141 1.2306 -0.0239 -0.0402 -0.0706 83 LYS B NZ 3204 N N . MET B 84 ? 0.7740 0.8539 0.8491 0.0080 -0.0289 -0.0523 84 MET B N 3205 C CA . MET B 84 ? 0.7726 0.8348 0.8597 0.0245 -0.0318 -0.0695 84 MET B CA 3206 C C . MET B 84 ? 0.7100 0.7723 0.8045 0.0088 -0.0303 -0.0627 84 MET B C 3207 O O . MET B 84 ? 0.7241 0.8218 0.8240 0.0127 -0.0348 -0.0749 84 MET B O 3208 C CB . MET B 84 ? 0.8463 0.8361 0.9287 0.0300 -0.0334 -0.0706 84 MET B CB 3209 C CG . MET B 84 ? 0.9322 0.8906 1.0125 0.0386 -0.0448 -0.0888 84 MET B CG 3210 S SD . MET B 84 ? 1.0513 0.9405 1.1214 0.0071 -0.0440 -0.0766 84 MET B SD 3211 C CE . MET B 84 ? 1.0103 0.9539 1.1106 -0.0118 -0.0233 -0.0656 84 MET B CE 3212 N N . GLU B 85 ? 0.9581 1.0347 0.9570 0.0930 -0.0282 -0.0428 85 GLU B N 3213 C CA . GLU B 85 ? 0.9440 1.0345 0.9389 0.1107 -0.0271 -0.0517 85 GLU B CA 3214 C C . GLU B 85 ? 0.9133 0.9514 0.9086 0.1022 -0.0395 -0.0563 85 GLU B C 3215 O O . GLU B 85 ? 0.8684 0.9191 0.8864 0.0951 -0.0324 -0.0525 85 GLU B O 3216 C CB . GLU B 85 ? 1.0188 1.1178 0.9696 0.1545 -0.0344 -0.0684 85 GLU B CB 3217 C CG . GLU B 85 ? 1.0769 1.2438 1.0247 0.1653 -0.0229 -0.0635 85 GLU B CG 3218 C CD . GLU B 85 ? 1.0883 1.3626 1.0498 0.1732 -0.0060 -0.0560 85 GLU B CD 3219 O OE1 . GLU B 85 ? 1.1030 1.4092 1.0969 0.1317 0.0057 -0.0381 85 GLU B OE1 3220 O OE2 . GLU B 85 ? 1.1308 1.4628 1.0624 0.2208 -0.0063 -0.0670 85 GLU B OE2 3221 N N . ASP B 86 ? 0.9270 0.9088 0.8926 0.0953 -0.0595 -0.0620 86 ASP B N 3222 C CA . ASP B 86 ? 0.9409 0.8724 0.8940 0.0753 -0.0759 -0.0628 86 ASP B CA 3223 C C . ASP B 86 ? 0.8569 0.8215 0.8622 0.0481 -0.0654 -0.0473 86 ASP B C 3224 O O . ASP B 86 ? 0.8604 0.8099 0.8718 0.0396 -0.0685 -0.0467 86 ASP B O 3225 C CB . ASP B 86 ? 1.0251 0.9000 0.9277 0.0534 -0.1027 -0.0651 86 ASP B CB 3226 C CG . ASP B 86 ? 1.1593 0.9452 0.9730 0.0793 -0.1262 -0.0838 86 ASP B CG 3227 O OD1 . ASP B 86 ? 1.2527 0.9982 1.0365 0.1020 -0.1311 -0.0930 86 ASP B OD1 3228 O OD2 . ASP B 86 ? 1.2589 1.0076 1.0217 0.0818 -0.1418 -0.0902 86 ASP B OD2 3229 N N . GLY B 87 ? 0.7939 0.7977 0.8259 0.0411 -0.0549 -0.0357 87 GLY B N 3230 C CA . GLY B 87 ? 0.7544 0.7842 0.8177 0.0314 -0.0464 -0.0227 87 GLY B CA 3231 C C . GLY B 87 ? 0.7232 0.7514 0.8034 0.0351 -0.0333 -0.0216 87 GLY B C 3232 O O . GLY B 87 ? 0.7032 0.7316 0.7985 0.0276 -0.0338 -0.0175 87 GLY B O 3233 N N . PHE B 88 ? 0.7294 0.7666 0.8048 0.0426 -0.0226 -0.0234 88 PHE B N 3234 C CA . PHE B 88 ? 0.7189 0.7670 0.8050 0.0359 -0.0122 -0.0197 88 PHE B CA 3235 C C . PHE B 88 ? 0.7260 0.7728 0.8186 0.0438 -0.0170 -0.0300 88 PHE B C 3236 O O . PHE B 88 ? 0.7209 0.7666 0.8289 0.0348 -0.0134 -0.0264 88 PHE B O 3237 C CB . PHE B 88 ? 0.7218 0.8038 0.7962 0.0297 -0.0017 -0.0139 88 PHE B CB 3238 C CG . PHE B 88 ? 0.7358 0.7937 0.7862 0.0137 0.0017 0.0005 88 PHE B CG 3239 C CD1 . PHE B 88 ? 0.7574 0.7702 0.7895 0.0010 0.0015 0.0104 88 PHE B CD1 3240 C CD2 . PHE B 88 ? 0.7585 0.8257 0.7897 0.0160 0.0027 0.0035 88 PHE B CD2 3241 C CE1 . PHE B 88 ? 0.8048 0.7661 0.7860 -0.0055 -0.0004 0.0224 88 PHE B CE1 3242 C CE2 . PHE B 88 ? 0.7973 0.8244 0.7891 0.0038 0.0028 0.0171 88 PHE B CE2 3243 C CZ . PHE B 88 ? 0.8342 0.8001 0.7938 -0.0052 0.0000 0.0263 88 PHE B CZ 3244 N N . LEU B 89 ? 0.7639 0.7982 0.8317 0.0648 -0.0276 -0.0434 89 LEU B N 3245 C CA . LEU B 89 ? 0.8086 0.8163 0.8583 0.0807 -0.0374 -0.0544 89 LEU B CA 3246 C C . LEU B 89 ? 0.7945 0.7630 0.8526 0.0558 -0.0472 -0.0492 89 LEU B C 3247 O O . LEU B 89 ? 0.7636 0.7273 0.8295 0.0562 -0.0464 -0.0500 89 LEU B O 3248 C CB . LEU B 89 ? 0.9049 0.8679 0.8936 0.1133 -0.0550 -0.0709 89 LEU B CB 3249 C CG . LEU B 89 ? 0.9778 0.9906 0.9471 0.1518 -0.0479 -0.0789 89 LEU B CG 3250 C CD1 . LEU B 89 ? 1.0818 1.0173 0.9669 0.1922 -0.0719 -0.0980 89 LEU B CD1 3251 C CD2 . LEU B 89 ? 0.9525 1.0573 0.9445 0.1714 -0.0309 -0.0771 89 LEU B CD2 3252 N N . ASP B 90 ? 0.8087 0.7644 0.8651 0.0335 -0.0564 -0.0422 90 ASP B N 3253 C CA . ASP B 90 ? 0.8089 0.7596 0.8748 0.0056 -0.0653 -0.0327 90 ASP B CA 3254 C C . ASP B 90 ? 0.7469 0.7371 0.8569 0.0047 -0.0485 -0.0231 90 ASP B C 3255 O O . ASP B 90 ? 0.7551 0.7436 0.8746 -0.0058 -0.0515 -0.0195 90 ASP B O 3256 C CB . ASP B 90 ? 0.8355 0.7996 0.8909 -0.0193 -0.0784 -0.0240 90 ASP B CB 3257 C CG . ASP B 90 ? 0.9630 0.8609 0.9529 -0.0317 -0.1039 -0.0323 90 ASP B CG 3258 O OD1 . ASP B 90 ? 1.0282 0.8570 0.9708 -0.0126 -0.1136 -0.0461 90 ASP B OD1 3259 O OD2 . ASP B 90 ? 1.0386 0.9491 1.0125 -0.0576 -0.1169 -0.0251 90 ASP B OD2 3260 N N . VAL B 91 ? 0.7071 0.7202 0.8304 0.0151 -0.0338 -0.0186 91 VAL B N 3261 C CA . VAL B 91 ? 0.6772 0.6976 0.8142 0.0170 -0.0228 -0.0108 91 VAL B CA 3262 C C . VAL B 91 ? 0.6665 0.6802 0.8119 0.0145 -0.0175 -0.0153 91 VAL B C 3263 O O . VAL B 91 ? 0.6762 0.6874 0.8329 0.0110 -0.0167 -0.0122 91 VAL B O 3264 C CB . VAL B 91 ? 0.6767 0.6898 0.7947 0.0246 -0.0144 -0.0045 91 VAL B CB 3265 C CG1 . VAL B 91 ? 0.6857 0.6710 0.7874 0.0242 -0.0088 0.0020 91 VAL B CG1 3266 C CG2 . VAL B 91 ? 0.6852 0.7145 0.7938 0.0368 -0.0194 0.0006 91 VAL B CG2 3267 N N . TRP B 92 ? 0.6569 0.6814 0.7958 0.0198 -0.0138 -0.0220 92 TRP B N 3268 C CA . TRP B 92 ? 0.6437 0.6877 0.7903 0.0208 -0.0086 -0.0251 92 TRP B CA 3269 C C . TRP B 92 ? 0.6429 0.6657 0.7871 0.0321 -0.0187 -0.0340 92 TRP B C 3270 O O . TRP B 92 ? 0.6351 0.6646 0.7917 0.0296 -0.0156 -0.0334 92 TRP B O 3271 C CB . TRP B 92 ? 0.6370 0.7315 0.7753 0.0279 -0.0017 -0.0272 92 TRP B CB 3272 C CG . TRP B 92 ? 0.6510 0.7591 0.7811 0.0002 0.0064 -0.0131 92 TRP B CG 3273 C CD1 . TRP B 92 ? 0.6672 0.7815 0.7808 -0.0031 0.0079 -0.0087 92 TRP B CD1 3274 C CD2 . TRP B 92 ? 0.6597 0.7559 0.7797 -0.0322 0.0098 -0.0003 92 TRP B CD2 3275 N NE1 . TRP B 92 ? 0.6922 0.7947 0.7808 -0.0376 0.0112 0.0071 92 TRP B NE1 3276 C CE2 . TRP B 92 ? 0.6970 0.7807 0.7826 -0.0572 0.0108 0.0123 92 TRP B CE2 3277 C CE3 . TRP B 92 ? 0.6681 0.7528 0.7937 -0.0442 0.0096 0.0018 92 TRP B CE3 3278 C CZ2 . TRP B 92 ? 0.7539 0.7968 0.7953 -0.0977 0.0079 0.0276 92 TRP B CZ2 3279 C CZ3 . TRP B 92 ? 0.6969 0.7505 0.7869 -0.0814 0.0084 0.0156 92 TRP B CZ3 3280 C CH2 . TRP B 92 ? 0.7519 0.7767 0.7931 -0.1097 0.0058 0.0286 92 TRP B CH2 3281 N N . THR B 93 ? 0.6673 0.6529 0.7840 0.0401 -0.0336 -0.0412 93 THR B N 3282 C CA . THR B 93 ? 0.7083 0.6455 0.7984 0.0418 -0.0494 -0.0467 93 THR B CA 3283 C C . THR B 93 ? 0.6928 0.6344 0.8110 0.0142 -0.0490 -0.0347 93 THR B C 3284 O O . THR B 93 ? 0.7091 0.6399 0.8287 0.0149 -0.0506 -0.0358 93 THR B O 3285 C CB . THR B 93 ? 0.7693 0.6405 0.7994 0.0418 -0.0725 -0.0533 93 THR B CB 3286 O OG1 . THR B 93 ? 0.8050 0.6724 0.8000 0.0812 -0.0730 -0.0670 93 THR B OG1 3287 C CG2 . THR B 93 ? 0.8319 0.6269 0.8094 0.0341 -0.0946 -0.0561 93 THR B CG2 3288 N N . TYR B 94 ? 0.6827 0.6498 0.8202 -0.0031 -0.0467 -0.0235 94 TYR B N 3289 C CA . TYR B 94 ? 0.6531 0.6478 0.8139 -0.0177 -0.0453 -0.0115 94 TYR B CA 3290 C C . TYR B 94 ? 0.6268 0.6306 0.8093 -0.0064 -0.0311 -0.0116 94 TYR B C 3291 O O . TYR B 94 ? 0.6015 0.6051 0.7924 -0.0118 -0.0328 -0.0094 94 TYR B O 3292 C CB . TYR B 94 ? 0.6487 0.6874 0.8179 -0.0199 -0.0440 -0.0010 94 TYR B CB 3293 C CG . TYR B 94 ? 0.6475 0.7352 0.8346 -0.0150 -0.0396 0.0104 94 TYR B CG 3294 C CD1 . TYR B 94 ? 0.6458 0.7280 0.8323 0.0129 -0.0266 0.0103 94 TYR B CD1 3295 C CD2 . TYR B 94 ? 0.6382 0.7766 0.8294 -0.0386 -0.0509 0.0226 94 TYR B CD2 3296 C CE1 . TYR B 94 ? 0.6244 0.7432 0.8110 0.0322 -0.0245 0.0181 94 TYR B CE1 3297 C CE2 . TYR B 94 ? 0.6229 0.8283 0.8289 -0.0241 -0.0459 0.0333 94 TYR B CE2 3298 C CZ . TYR B 94 ? 0.6242 0.8159 0.8264 0.0191 -0.0322 0.0289 94 TYR B CZ 3299 O OH . TYR B 94 ? 0.6451 0.8936 0.8457 0.0483 -0.0290 0.0367 94 TYR B OH 3300 N N . ASN B 95 ? 0.6457 0.6523 0.8285 0.0029 -0.0194 -0.0128 95 ASN B N 3301 C CA . ASN B 95 ? 0.6360 0.6397 0.8220 0.0018 -0.0103 -0.0108 95 ASN B CA 3302 C C . ASN B 95 ? 0.6331 0.6427 0.8296 0.0010 -0.0104 -0.0171 95 ASN B C 3303 O O . ASN B 95 ? 0.6496 0.6567 0.8543 -0.0026 -0.0084 -0.0145 95 ASN B O 3304 C CB . ASN B 95 ? 0.6555 0.6548 0.8220 -0.0049 -0.0034 -0.0080 95 ASN B CB 3305 C CG . ASN B 95 ? 0.7101 0.6829 0.8485 0.0020 -0.0043 -0.0009 95 ASN B CG 3306 O OD1 . ASN B 95 ? 0.7097 0.6860 0.8487 0.0187 -0.0080 0.0017 95 ASN B OD1 3307 N ND2 . ASN B 95 ? 0.7588 0.7121 0.8653 -0.0100 -0.0020 0.0038 95 ASN B ND2 3308 N N . ALA B 96 ? 0.6402 0.6570 0.8284 0.0120 -0.0135 -0.0262 96 ALA B N 3309 C CA . ALA B 96 ? 0.6430 0.6697 0.8293 0.0254 -0.0148 -0.0337 96 ALA B CA 3310 C C . ALA B 96 ? 0.6328 0.6206 0.8138 0.0229 -0.0257 -0.0338 96 ALA B C 3311 O O . ALA B 96 ? 0.6026 0.5972 0.7957 0.0219 -0.0229 -0.0329 96 ALA B O 3312 C CB . ALA B 96 ? 0.6811 0.7200 0.8400 0.0555 -0.0189 -0.0453 96 ALA B CB 3313 N N . GLU B 97 ? 0.6726 0.6217 0.8304 0.0148 -0.0399 -0.0326 97 GLU B N 3314 C CA . GLU B 97 ? 0.7268 0.6372 0.8643 -0.0005 -0.0550 -0.0287 97 GLU B CA 3315 C C . GLU B 97 ? 0.6953 0.6429 0.8712 -0.0185 -0.0475 -0.0163 97 GLU B C 3316 O O . GLU B 97 ? 0.7107 0.6463 0.8834 -0.0245 -0.0522 -0.0140 97 GLU B O 3317 C CB . GLU B 97 ? 0.7958 0.6588 0.8868 -0.0220 -0.0763 -0.0255 97 GLU B CB 3318 C CG . GLU B 97 ? 0.9017 0.6911 0.9225 0.0052 -0.0920 -0.0410 97 GLU B CG 3319 C CD . GLU B 97 ? 1.0159 0.7389 0.9724 -0.0214 -0.1173 -0.0383 97 GLU B CD 3320 O OE1 . GLU B 97 ? 1.0743 0.8311 1.0510 -0.0669 -0.1213 -0.0220 97 GLU B OE1 3321 O OE2 . GLU B 97 ? 1.1436 0.7833 1.0204 0.0052 -0.1352 -0.0522 97 GLU B OE2 3322 N N . LEU B 98 ? 0.6619 0.6498 0.8638 -0.0196 -0.0368 -0.0093 98 LEU B N 3323 C CA . LEU B 98 ? 0.6344 0.6572 0.8568 -0.0212 -0.0313 0.0007 98 LEU B CA 3324 C C . LEU B 98 ? 0.6054 0.6207 0.8378 -0.0099 -0.0212 -0.0037 98 LEU B C 3325 O O . LEU B 98 ? 0.5924 0.6182 0.8335 -0.0107 -0.0211 0.0005 98 LEU B O 3326 C CB . LEU B 98 ? 0.6543 0.7084 0.8780 -0.0096 -0.0260 0.0071 98 LEU B CB 3327 C CG . LEU B 98 ? 0.6691 0.7678 0.8977 0.0058 -0.0231 0.0167 98 LEU B CG 3328 C CD1 . LEU B 98 ? 0.6589 0.8201 0.8973 -0.0180 -0.0338 0.0300 98 LEU B CD1 3329 C CD2 . LEU B 98 ? 0.6882 0.7945 0.8950 0.0375 -0.0182 0.0184 98 LEU B CD2 3330 N N . LEU B 99 ? 0.5884 0.5933 0.8162 -0.0046 -0.0138 -0.0103 99 LEU B N 3331 C CA . LEU B 99 ? 0.5880 0.5920 0.8173 -0.0065 -0.0071 -0.0119 99 LEU B CA 3332 C C . LEU B 99 ? 0.5765 0.5858 0.8163 -0.0039 -0.0103 -0.0165 99 LEU B C 3333 O O . LEU B 99 ? 0.5638 0.5740 0.8104 -0.0059 -0.0083 -0.0145 99 LEU B O 3334 C CB . LEU B 99 ? 0.6214 0.6359 0.8397 -0.0152 -0.0017 -0.0137 99 LEU B CB 3335 C CG . LEU B 99 ? 0.6611 0.6826 0.8695 -0.0345 0.0018 -0.0105 99 LEU B CG 3336 C CD1 . LEU B 99 ? 0.7006 0.6689 0.8792 -0.0388 -0.0010 -0.0047 99 LEU B CD1 3337 C CD2 . LEU B 99 ? 0.6952 0.7481 0.8881 -0.0568 0.0048 -0.0064 99 LEU B CD2 3338 N N . VAL B 100 ? 0.5752 0.5765 0.8037 0.0054 -0.0175 -0.0234 100 VAL B N 3339 C CA . VAL B 100 ? 0.5650 0.5523 0.7822 0.0167 -0.0242 -0.0290 100 VAL B CA 3340 C C . VAL B 100 ? 0.5549 0.5219 0.7732 0.0012 -0.0318 -0.0205 100 VAL B C 3341 O O . VAL B 100 ? 0.5301 0.5017 0.7565 0.0036 -0.0300 -0.0203 100 VAL B O 3342 C CB . VAL B 100 ? 0.6071 0.5631 0.7814 0.0412 -0.0359 -0.0398 100 VAL B CB 3343 C CG1 . VAL B 100 ? 0.6520 0.5577 0.7860 0.0567 -0.0501 -0.0447 100 VAL B CG1 3344 C CG2 . VAL B 100 ? 0.6016 0.6145 0.7803 0.0643 -0.0256 -0.0473 100 VAL B CG2 3345 N N . LEU B 101 ? 0.5621 0.5208 0.7721 -0.0179 -0.0405 -0.0114 101 LEU B N 3346 C CA . LEU B 101 ? 0.5677 0.5382 0.7798 -0.0406 -0.0478 0.0019 101 LEU B CA 3347 C C . LEU B 101 ? 0.5465 0.5626 0.7930 -0.0310 -0.0341 0.0063 101 LEU B C 3348 O O . LEU B 101 ? 0.5598 0.5813 0.8107 -0.0346 -0.0354 0.0101 101 LEU B O 3349 C CB . LEU B 101 ? 0.5812 0.5735 0.7835 -0.0680 -0.0581 0.0150 101 LEU B CB 3350 C CG . LEU B 101 ? 0.6575 0.5868 0.8039 -0.0914 -0.0800 0.0149 101 LEU B CG 3351 C CD1 . LEU B 101 ? 0.6670 0.6430 0.8090 -0.1296 -0.0902 0.0321 101 LEU B CD1 3352 C CD2 . LEU B 101 ? 0.7303 0.5849 0.8218 -0.1065 -0.0993 0.0156 101 LEU B CD2 3353 N N . MET B 102 ? 0.5385 0.5736 0.7952 -0.0165 -0.0235 0.0053 102 MET B N 3354 C CA . MET B 102 ? 0.5504 0.6019 0.8112 -0.0001 -0.0158 0.0080 102 MET B CA 3355 C C . MET B 102 ? 0.5504 0.5782 0.8125 0.0019 -0.0114 0.0007 102 MET B C 3356 O O . MET B 102 ? 0.5690 0.6053 0.8330 0.0086 -0.0104 0.0035 102 MET B O 3357 C CB . MET B 102 ? 0.5946 0.6371 0.8359 0.0183 -0.0110 0.0072 102 MET B CB 3358 C CG . MET B 102 ? 0.6316 0.7219 0.8708 0.0284 -0.0140 0.0164 102 MET B CG 3359 S SD . MET B 102 ? 0.7416 0.7963 0.9365 0.0619 -0.0107 0.0133 102 MET B SD 3360 C CE . MET B 102 ? 0.7663 0.9113 0.9543 0.0998 -0.0129 0.0248 102 MET B CE 3361 N N . GLU B 103 ? 0.5509 0.5627 0.8106 -0.0032 -0.0090 -0.0074 103 GLU B N 3362 C CA . GLU B 103 ? 0.5709 0.5826 0.8310 -0.0068 -0.0055 -0.0119 103 GLU B CA 3363 C C . GLU B 103 ? 0.5574 0.5778 0.8291 -0.0022 -0.0090 -0.0148 103 GLU B C 3364 O O . GLU B 103 ? 0.5472 0.5742 0.8230 -0.0028 -0.0070 -0.0157 103 GLU B O 3365 C CB . GLU B 103 ? 0.6112 0.6339 0.8624 -0.0182 -0.0019 -0.0152 103 GLU B CB 3366 C CG . GLU B 103 ? 0.6921 0.6824 0.9113 -0.0301 -0.0017 -0.0101 103 GLU B CG 3367 C CD . GLU B 103 ? 0.7710 0.7151 0.9528 -0.0353 -0.0054 -0.0069 103 GLU B CD 3368 O OE1 . GLU B 103 ? 0.7869 0.7407 0.9728 -0.0455 -0.0059 -0.0080 103 GLU B OE1 3369 O OE2 . GLU B 103 ? 0.8810 0.7720 1.0181 -0.0239 -0.0097 -0.0041 103 GLU B OE2 3370 N N . ASN B 104 ? 0.5637 0.5707 0.8271 0.0015 -0.0174 -0.0158 104 ASN B N 3371 C CA . ASN B 104 ? 0.5821 0.5695 0.8328 0.0055 -0.0261 -0.0164 104 ASN B CA 3372 C C . ASN B 104 ? 0.5714 0.5700 0.8348 -0.0066 -0.0264 -0.0058 104 ASN B C 3373 O O . ASN B 104 ? 0.5516 0.5503 0.8171 -0.0022 -0.0264 -0.0067 104 ASN B O 3374 C CB . ASN B 104 ? 0.6260 0.5629 0.8345 0.0039 -0.0426 -0.0168 104 ASN B CB 3375 C CG . ASN B 104 ? 0.6539 0.5753 0.8336 0.0338 -0.0452 -0.0307 104 ASN B CG 3376 O OD1 . ASN B 104 ? 0.6029 0.5726 0.8006 0.0536 -0.0341 -0.0381 104 ASN B OD1 3377 N ND2 . ASN B 104 ? 0.7228 0.5825 0.8495 0.0363 -0.0618 -0.0330 104 ASN B ND2 3378 N N . GLU B 105 ? 0.5748 0.5959 0.8452 -0.0174 -0.0265 0.0048 105 GLU B N 3379 C CA . GLU B 105 ? 0.5738 0.6320 0.8552 -0.0196 -0.0251 0.0157 105 GLU B CA 3380 C C . GLU B 105 ? 0.5346 0.5925 0.8228 0.0003 -0.0153 0.0087 105 GLU B C 3381 O O . GLU B 105 ? 0.5143 0.5793 0.8068 0.0025 -0.0152 0.0103 105 GLU B O 3382 C CB . GLU B 105 ? 0.6242 0.7334 0.9088 -0.0208 -0.0252 0.0273 105 GLU B CB 3383 C CG . GLU B 105 ? 0.7004 0.8785 0.9913 -0.0284 -0.0282 0.0439 105 GLU B CG 3384 C CD . GLU B 105 ? 0.8188 1.0699 1.1091 -0.0443 -0.0338 0.0599 105 GLU B CD 3385 O OE1 . GLU B 105 ? 0.9324 1.2084 1.2228 -0.0139 -0.0269 0.0565 105 GLU B OE1 3386 O OE2 . GLU B 105 ? 0.8485 1.1283 1.1287 -0.0906 -0.0476 0.0770 105 GLU B OE2 3387 N N . ARG B 106 ? 0.5471 0.5867 0.8252 0.0095 -0.0097 0.0019 106 ARG B N 3388 C CA . ARG B 106 ? 0.5869 0.6042 0.8481 0.0170 -0.0066 -0.0029 106 ARG B CA 3389 C C . ARG B 106 ? 0.5388 0.5575 0.8114 0.0060 -0.0062 -0.0085 106 ARG B C 3390 O O . ARG B 106 ? 0.5450 0.5590 0.8112 0.0092 -0.0062 -0.0092 106 ARG B O 3391 C CB . ARG B 106 ? 0.6567 0.6335 0.8815 0.0167 -0.0066 -0.0059 106 ARG B CB 3392 C CG . ARG B 106 ? 0.7160 0.6909 0.9180 0.0421 -0.0079 -0.0014 106 ARG B CG 3393 C CD . ARG B 106 ? 0.8470 0.7481 0.9799 0.0530 -0.0128 -0.0043 106 ARG B CD 3394 N NE . ARG B 106 ? 0.9545 0.8168 1.0323 0.0883 -0.0186 -0.0058 106 ARG B NE 3395 C CZ . ARG B 106 ? 1.0489 0.8358 1.0695 0.0800 -0.0267 -0.0101 106 ARG B CZ 3396 N NH1 . ARG B 106 ? 1.1029 0.8633 1.1205 0.0291 -0.0293 -0.0106 106 ARG B NH1 3397 N NH2 . ARG B 106 ? 1.1720 0.9148 1.1290 0.1239 -0.0341 -0.0132 106 ARG B NH2 3398 N N . THR B 107 ? 0.5327 0.5629 0.8163 0.0004 -0.0067 -0.0130 107 THR B N 3399 C CA . THR B 107 ? 0.5032 0.5539 0.7928 0.0018 -0.0063 -0.0188 107 THR B CA 3400 C C . THR B 107 ? 0.5016 0.5479 0.7961 0.0107 -0.0102 -0.0167 107 THR B C 3401 O O . THR B 107 ? 0.4601 0.5191 0.7582 0.0116 -0.0087 -0.0186 107 THR B O 3402 C CB . THR B 107 ? 0.5075 0.5804 0.7945 0.0119 -0.0071 -0.0254 107 THR B CB 3403 O OG1 . THR B 107 ? 0.4933 0.5885 0.7772 -0.0035 -0.0026 -0.0250 107 THR B OG1 3404 C CG2 . THR B 107 ? 0.5287 0.6384 0.8151 0.0295 -0.0079 -0.0316 107 THR B CG2 3405 N N . LEU B 108 ? 0.4990 0.5267 0.7871 0.0102 -0.0172 -0.0105 108 LEU B N 3406 C CA . LEU B 108 ? 0.5199 0.5394 0.8021 0.0082 -0.0236 -0.0041 108 LEU B CA 3407 C C . LEU B 108 ? 0.5066 0.5530 0.8047 0.0082 -0.0175 0.0014 108 LEU B C 3408 O O . LEU B 108 ? 0.4974 0.5475 0.7977 0.0130 -0.0174 0.0004 108 LEU B O 3409 C CB . LEU B 108 ? 0.5535 0.5465 0.8107 -0.0103 -0.0368 0.0069 108 LEU B CB 3410 C CG . LEU B 108 ? 0.6208 0.5575 0.8356 -0.0047 -0.0489 0.0000 108 LEU B CG 3411 C CD1 . LEU B 108 ? 0.6956 0.5854 0.8638 -0.0380 -0.0687 0.0143 108 LEU B CD1 3412 C CD2 . LEU B 108 ? 0.6600 0.5699 0.8477 0.0283 -0.0524 -0.0131 108 LEU B CD2 3413 N N . ASP B 109 ? 0.4892 0.5523 0.7896 0.0108 -0.0135 0.0061 109 ASP B N 3414 C CA . ASP B 109 ? 0.4892 0.5686 0.7848 0.0269 -0.0098 0.0083 109 ASP B CA 3415 C C . ASP B 109 ? 0.4881 0.5363 0.7692 0.0311 -0.0077 -0.0026 109 ASP B C 3416 O O . ASP B 109 ? 0.5166 0.5659 0.7897 0.0413 -0.0079 -0.0027 109 ASP B O 3417 C CB . ASP B 109 ? 0.5376 0.6313 0.8178 0.0447 -0.0082 0.0121 109 ASP B CB 3418 C CG . ASP B 109 ? 0.5835 0.7405 0.8775 0.0360 -0.0112 0.0277 109 ASP B CG 3419 O OD1 . ASP B 109 ? 0.5663 0.7588 0.8715 0.0154 -0.0160 0.0397 109 ASP B OD1 3420 O OD2 . ASP B 109 ? 0.6220 0.7955 0.9083 0.0458 -0.0106 0.0298 109 ASP B OD2 3421 N N . PHE B 110 ? 0.4659 0.4929 0.7388 0.0180 -0.0073 -0.0097 110 PHE B N 3422 C CA . PHE B 110 ? 0.4743 0.4840 0.7266 0.0034 -0.0089 -0.0154 110 PHE B CA 3423 C C . PHE B 110 ? 0.4591 0.4983 0.7317 0.0031 -0.0086 -0.0174 110 PHE B C 3424 O O . PHE B 110 ? 0.4871 0.5137 0.7417 0.0001 -0.0112 -0.0190 110 PHE B O 3425 C CB . PHE B 110 ? 0.4868 0.5030 0.7343 -0.0198 -0.0087 -0.0175 110 PHE B CB 3426 C CG . PHE B 110 ? 0.5256 0.5486 0.7497 -0.0521 -0.0128 -0.0181 110 PHE B CG 3427 C CD1 . PHE B 110 ? 0.5911 0.5489 0.7558 -0.0695 -0.0223 -0.0168 110 PHE B CD1 3428 C CD2 . PHE B 110 ? 0.5004 0.5970 0.7486 -0.0658 -0.0100 -0.0188 110 PHE B CD2 3429 C CE1 . PHE B 110 ? 0.6234 0.5853 0.7541 -0.1163 -0.0307 -0.0136 110 PHE B CE1 3430 C CE2 . PHE B 110 ? 0.5307 0.6630 0.7579 -0.1063 -0.0150 -0.0149 110 PHE B CE2 3431 C CZ . PHE B 110 ? 0.5879 0.6502 0.7563 -0.1401 -0.0263 -0.0109 110 PHE B CZ 3432 N N . HIS B 111 ? 0.4412 0.5083 0.7388 0.0103 -0.0077 -0.0179 111 HIS B N 3433 C CA . HIS B 111 ? 0.4274 0.5156 0.7339 0.0194 -0.0091 -0.0202 111 HIS B CA 3434 C C . HIS B 111 ? 0.4292 0.5072 0.7365 0.0261 -0.0102 -0.0144 111 HIS B C 3435 O O . HIS B 111 ? 0.4375 0.5260 0.7447 0.0282 -0.0104 -0.0167 111 HIS B O 3436 C CB . HIS B 111 ? 0.4346 0.5226 0.7376 0.0365 -0.0132 -0.0224 111 HIS B CB 3437 C CG . HIS B 111 ? 0.4248 0.5482 0.7251 0.0441 -0.0116 -0.0299 111 HIS B CG 3438 N ND1 . HIS B 111 ? 0.4270 0.6157 0.7333 0.0435 -0.0086 -0.0341 111 HIS B ND1 3439 C CD2 . HIS B 111 ? 0.4361 0.5535 0.7261 0.0529 -0.0131 -0.0326 111 HIS B CD2 3440 C CE1 . HIS B 111 ? 0.4416 0.6775 0.7443 0.0534 -0.0072 -0.0380 111 HIS B CE1 3441 N NE2 . HIS B 111 ? 0.4448 0.6310 0.7364 0.0626 -0.0097 -0.0385 111 HIS B NE2 3442 N N . ASP B 112 ? 0.4147 0.4864 0.7223 0.0277 -0.0113 -0.0053 112 ASP B N 3443 C CA . ASP B 112 ? 0.4205 0.5088 0.7291 0.0334 -0.0119 0.0039 112 ASP B CA 3444 C C . ASP B 112 ? 0.4434 0.5250 0.7358 0.0475 -0.0093 -0.0015 112 ASP B C 3445 O O . ASP B 112 ? 0.4637 0.5534 0.7539 0.0555 -0.0096 -0.0013 112 ASP B O 3446 C CB . ASP B 112 ? 0.4417 0.5548 0.7516 0.0280 -0.0136 0.0173 112 ASP B CB 3447 C CG . ASP B 112 ? 0.4687 0.6297 0.7812 0.0257 -0.0156 0.0327 112 ASP B CG 3448 O OD1 . ASP B 112 ? 0.4931 0.6517 0.8059 0.0276 -0.0164 0.0325 112 ASP B OD1 3449 O OD2 . ASP B 112 ? 0.4815 0.6960 0.7955 0.0204 -0.0166 0.0468 112 ASP B OD2 3450 N N . SER B 113 ? 0.4609 0.5127 0.7278 0.0509 -0.0095 -0.0067 113 SER B N 3451 C CA . SER B 113 ? 0.5072 0.5139 0.7253 0.0631 -0.0138 -0.0131 113 SER B CA 3452 C C . SER B 113 ? 0.5091 0.5008 0.7189 0.0412 -0.0176 -0.0196 113 SER B C 3453 O O . SER B 113 ? 0.5287 0.4983 0.7089 0.0517 -0.0222 -0.0224 113 SER B O 3454 C CB . SER B 113 ? 0.5547 0.5064 0.7257 0.0639 -0.0183 -0.0166 113 SER B CB 3455 O OG . SER B 113 ? 0.6594 0.5327 0.7573 0.0617 -0.0293 -0.0233 113 SER B OG 3456 N N . ASN B 114 ? 0.4850 0.4993 0.7169 0.0134 -0.0165 -0.0215 114 ASN B N 3457 C CA . ASN B 114 ? 0.4968 0.5280 0.7239 -0.0094 -0.0202 -0.0250 114 ASN B CA 3458 C C . ASN B 114 ? 0.4696 0.5320 0.7222 0.0088 -0.0178 -0.0249 114 ASN B C 3459 O O . ASN B 114 ? 0.4749 0.5329 0.7082 -0.0005 -0.0227 -0.0277 114 ASN B O 3460 C CB . ASN B 114 ? 0.4864 0.5733 0.7355 -0.0324 -0.0182 -0.0254 114 ASN B CB 3461 C CG . ASN B 114 ? 0.5304 0.5928 0.7497 -0.0608 -0.0218 -0.0232 114 ASN B CG 3462 O OD1 . ASN B 114 ? 0.5973 0.5850 0.7565 -0.0782 -0.0314 -0.0222 114 ASN B OD1 3463 N ND2 . ASN B 114 ? 0.5090 0.6238 0.7567 -0.0621 -0.0165 -0.0227 114 ASN B ND2 3464 N N . VAL B 115 ? 0.4396 0.5249 0.7248 0.0290 -0.0130 -0.0203 115 VAL B N 3465 C CA . VAL B 115 ? 0.4306 0.5351 0.7295 0.0427 -0.0129 -0.0175 115 VAL B CA 3466 C C . VAL B 115 ? 0.4474 0.5383 0.7286 0.0560 -0.0136 -0.0147 115 VAL B C 3467 O O . VAL B 115 ? 0.4530 0.5477 0.7275 0.0598 -0.0154 -0.0173 115 VAL B O 3468 C CB . VAL B 115 ? 0.4316 0.5400 0.7435 0.0500 -0.0138 -0.0096 115 VAL B CB 3469 C CG1 . VAL B 115 ? 0.4486 0.5634 0.7598 0.0574 -0.0164 -0.0026 115 VAL B CG1 3470 C CG2 . VAL B 115 ? 0.4497 0.5618 0.7603 0.0544 -0.0160 -0.0157 115 VAL B CG2 3471 N N . LYS B 116 ? 0.4648 0.5490 0.7350 0.0693 -0.0124 -0.0095 116 LYS B N 3472 C CA . LYS B 116 ? 0.5064 0.5909 0.7491 0.0980 -0.0133 -0.0076 116 LYS B CA 3473 C C . LYS B 116 ? 0.5520 0.5755 0.7397 0.1027 -0.0211 -0.0196 116 LYS B C 3474 O O . LYS B 116 ? 0.5706 0.5930 0.7383 0.1228 -0.0236 -0.0212 116 LYS B O 3475 C CB . LYS B 116 ? 0.5531 0.6506 0.7826 0.1192 -0.0117 -0.0020 116 LYS B CB 3476 C CG . LYS B 116 ? 0.6220 0.7277 0.8066 0.1678 -0.0135 -0.0022 116 LYS B CG 3477 C CD . LYS B 116 ? 0.6422 0.8311 0.8543 0.1790 -0.0093 0.0103 116 LYS B CD 3478 C CE . LYS B 116 ? 0.7134 0.9620 0.8914 0.2362 -0.0084 0.0156 116 LYS B CE 3479 N NZ . LYS B 116 ? 0.6926 1.0729 0.9190 0.2224 -0.0026 0.0397 116 LYS B NZ 3480 N N . ASN B 117 ? 0.5916 0.5597 0.7450 0.0790 -0.0277 -0.0266 117 ASN B N 3481 C CA . ASN B 117 ? 0.6772 0.5668 0.7550 0.0662 -0.0419 -0.0350 117 ASN B CA 3482 C C . ASN B 117 ? 0.6732 0.5923 0.7703 0.0399 -0.0437 -0.0367 117 ASN B C 3483 O O . ASN B 117 ? 0.7392 0.6093 0.7805 0.0414 -0.0547 -0.0418 117 ASN B O 3484 C CB . ASN B 117 ? 0.7210 0.5446 0.7467 0.0311 -0.0520 -0.0369 117 ASN B CB 3485 C CG . ASN B 117 ? 0.7683 0.5413 0.7502 0.0663 -0.0538 -0.0373 117 ASN B CG 3486 O OD1 . ASN B 117 ? 0.7800 0.5520 0.7410 0.1221 -0.0524 -0.0384 117 ASN B OD1 3487 N ND2 . ASN B 117 ? 0.8017 0.5469 0.7688 0.0375 -0.0567 -0.0356 117 ASN B ND2 3488 N N . LEU B 118 ? 0.6173 0.6136 0.7835 0.0221 -0.0347 -0.0331 118 LEU B N 3489 C CA . LEU B 118 ? 0.6228 0.6650 0.8088 0.0065 -0.0357 -0.0345 118 LEU B CA 3490 C C . LEU B 118 ? 0.6200 0.6719 0.8166 0.0396 -0.0327 -0.0337 118 LEU B C 3491 O O . LEU B 118 ? 0.6503 0.6944 0.8236 0.0341 -0.0392 -0.0375 118 LEU B O 3492 C CB . LEU B 118 ? 0.5893 0.7093 0.8309 0.0001 -0.0280 -0.0324 118 LEU B CB 3493 C CG . LEU B 118 ? 0.5927 0.7816 0.8537 -0.0055 -0.0286 -0.0341 118 LEU B CG 3494 C CD1 . LEU B 118 ? 0.6481 0.8412 0.8687 -0.0517 -0.0403 -0.0351 118 LEU B CD1 3495 C CD2 . LEU B 118 ? 0.5783 0.8349 0.8731 0.0065 -0.0229 -0.0340 118 LEU B CD2 3496 N N . TYR B 119 ? 0.5872 0.6596 0.8133 0.0683 -0.0245 -0.0267 119 TYR B N 3497 C CA . TYR B 119 ? 0.5652 0.6593 0.7979 0.0950 -0.0218 -0.0215 119 TYR B CA 3498 C C . TYR B 119 ? 0.6373 0.6852 0.8094 0.1196 -0.0289 -0.0277 119 TYR B C 3499 O O . TYR B 119 ? 0.6532 0.7082 0.8148 0.1338 -0.0308 -0.0290 119 TYR B O 3500 C CB . TYR B 119 ? 0.5236 0.6576 0.7871 0.1060 -0.0152 -0.0077 119 TYR B CB 3501 C CG . TYR B 119 ? 0.5225 0.6996 0.7908 0.1249 -0.0131 0.0032 119 TYR B CG 3502 C CD1 . TYR B 119 ? 0.5090 0.7076 0.7968 0.1156 -0.0134 0.0098 119 TYR B CD1 3503 C CD2 . TYR B 119 ? 0.5313 0.7345 0.7771 0.1567 -0.0116 0.0079 119 TYR B CD2 3504 C CE1 . TYR B 119 ? 0.5156 0.7592 0.8047 0.1258 -0.0122 0.0228 119 TYR B CE1 3505 C CE2 . TYR B 119 ? 0.5265 0.7946 0.7779 0.1735 -0.0090 0.0204 119 TYR B CE2 3506 C CZ . TYR B 119 ? 0.5316 0.8191 0.8069 0.1522 -0.0092 0.0289 119 TYR B CZ 3507 O OH . TYR B 119 ? 0.5403 0.8974 0.8181 0.1622 -0.0074 0.0443 119 TYR B OH 3508 N N . ASP B 120 ? 0.7248 0.7154 0.8442 0.1310 -0.0347 -0.0324 120 ASP B N 3509 C CA . ASP B 120 ? 0.8270 0.7471 0.8583 0.1683 -0.0463 -0.0409 120 ASP B CA 3510 C C . ASP B 120 ? 0.8661 0.7062 0.8335 0.1366 -0.0629 -0.0512 120 ASP B C 3511 O O . ASP B 120 ? 0.9074 0.7109 0.8220 0.1614 -0.0716 -0.0573 120 ASP B O 3512 C CB . ASP B 120 ? 0.9024 0.7689 0.8736 0.2003 -0.0514 -0.0437 120 ASP B CB 3513 C CG . ASP B 120 ? 0.8872 0.8534 0.9074 0.2403 -0.0374 -0.0318 120 ASP B CG 3514 O OD1 . ASP B 120 ? 0.8622 0.9141 0.9212 0.2592 -0.0294 -0.0228 120 ASP B OD1 3515 O OD2 . ASP B 120 ? 0.9224 0.8891 0.9394 0.2478 -0.0355 -0.0292 120 ASP B OD2 3516 N N . LYS B 121 ? 0.8681 0.6922 0.8379 0.0786 -0.0684 -0.0513 121 LYS B N 3517 C CA . LYS B 121 ? 0.9573 0.7317 0.8702 0.0288 -0.0860 -0.0557 121 LYS B CA 3518 C C . LYS B 121 ? 0.9263 0.7574 0.8745 0.0343 -0.0825 -0.0565 121 LYS B C 3519 O O . LYS B 121 ? 1.0215 0.7868 0.8951 0.0260 -0.0993 -0.0627 121 LYS B O 3520 C CB . LYS B 121 ? 0.9591 0.7772 0.9034 -0.0362 -0.0862 -0.0498 121 LYS B CB 3521 C CG . LYS B 121 ? 1.0361 0.8373 0.9258 -0.1065 -0.1055 -0.0483 121 LYS B CG 3522 C CD . LYS B 121 ? 1.0129 0.9094 0.9532 -0.1608 -0.1007 -0.0391 121 LYS B CD 3523 C CE . LYS B 121 ? 1.1254 1.0237 1.0014 -0.2473 -0.1228 -0.0318 121 LYS B CE 3524 N NZ . LYS B 121 ? 1.1413 1.0972 1.0299 -0.2566 -0.1264 -0.0330 121 LYS B NZ 3525 N N . VAL B 122 ? 0.8147 0.7540 0.8634 0.0487 -0.0635 -0.0501 122 VAL B N 3526 C CA . VAL B 122 ? 0.7629 0.7567 0.8459 0.0598 -0.0592 -0.0495 122 VAL B CA 3527 C C . VAL B 122 ? 0.7927 0.7647 0.8485 0.1119 -0.0585 -0.0508 122 VAL B C 3528 O O . VAL B 122 ? 0.8197 0.7771 0.8452 0.1179 -0.0658 -0.0556 122 VAL B O 3529 C CB . VAL B 122 ? 0.6703 0.7599 0.8428 0.0636 -0.0438 -0.0417 122 VAL B CB 3530 C CG1 . VAL B 122 ? 0.6334 0.7651 0.8311 0.0847 -0.0398 -0.0392 122 VAL B CG1 3531 C CG2 . VAL B 122 ? 0.6567 0.7912 0.8489 0.0245 -0.0454 -0.0422 122 VAL B CG2 3532 N N . ARG B 123 ? 0.7827 0.7680 0.8489 0.1503 -0.0499 -0.0454 123 ARG B N 3533 C CA . ARG B 123 ? 0.8303 0.8251 0.8685 0.2062 -0.0486 -0.0444 123 ARG B CA 3534 C C . ARG B 123 ? 0.9538 0.8380 0.8757 0.2307 -0.0682 -0.0596 123 ARG B C 3535 O O . ARG B 123 ? 0.9834 0.8688 0.8766 0.2629 -0.0716 -0.0631 123 ARG B O 3536 C CB . ARG B 123 ? 0.8212 0.8630 0.8774 0.2395 -0.0389 -0.0346 123 ARG B CB 3537 C CG . ARG B 123 ? 0.8600 0.9679 0.9058 0.2968 -0.0340 -0.0277 123 ARG B CG 3538 C CD . ARG B 123 ? 0.8578 1.0420 0.9208 0.3252 -0.0254 -0.0149 123 ARG B CD 3539 N NE . ARG B 123 ? 0.9141 1.0236 0.9259 0.3373 -0.0322 -0.0248 123 ARG B NE 3540 C CZ . ARG B 123 ? 1.0067 1.0238 0.9107 0.3909 -0.0460 -0.0402 123 ARG B CZ 3541 N NH1 . ARG B 123 ? 1.0758 1.0602 0.9071 0.4424 -0.0551 -0.0498 123 ARG B NH1 3542 N NH2 . ARG B 123 ? 1.0546 0.9974 0.9094 0.3958 -0.0533 -0.0468 123 ARG B NH2 3543 N N . LEU B 124 ? 1.0459 0.8226 0.8883 0.2132 -0.0841 -0.0681 124 LEU B N 3544 C CA . LEU B 124 ? 1.2224 0.8508 0.9179 0.2315 -0.1107 -0.0826 124 LEU B CA 3545 C C . LEU B 124 ? 1.2875 0.8706 0.9446 0.1835 -0.1269 -0.0880 124 LEU B C 3546 O O . LEU B 124 ? 1.4280 0.8883 0.9575 0.2030 -0.1507 -0.0997 124 LEU B O 3547 C CB . LEU B 124 ? 1.3140 0.8219 0.9191 0.2121 -0.1277 -0.0870 124 LEU B CB 3548 C CG . LEU B 124 ? 1.3128 0.8426 0.9232 0.2707 -0.1172 -0.0845 124 LEU B CG 3549 C CD1 . LEU B 124 ? 1.3555 0.8074 0.9267 0.2289 -0.1266 -0.0837 124 LEU B CD1 3550 C CD2 . LEU B 124 ? 1.4212 0.8903 0.9198 0.3700 -0.1278 -0.0952 124 LEU B CD2 3551 N N . GLN B 125 ? 1.2136 0.8927 0.9689 0.1248 -0.1162 -0.0798 125 GLN B N 3552 C CA . GLN B 125 ? 1.2432 0.9187 0.9798 0.0795 -0.1287 -0.0824 125 GLN B CA 3553 C C . GLN B 125 ? 1.2046 0.9444 0.9823 0.1250 -0.1181 -0.0831 125 GLN B C 3554 O O . GLN B 125 ? 1.3264 0.9986 1.0242 0.1332 -0.1350 -0.0918 125 GLN B O 3555 C CB . GLN B 125 ? 1.1718 0.9469 0.9925 0.0105 -0.1214 -0.0732 125 GLN B CB 3556 C CG . GLN B 125 ? 1.2543 0.9748 1.0212 -0.0548 -0.1369 -0.0702 125 GLN B CG 3557 C CD . GLN B 125 ? 1.2076 1.0487 1.0414 -0.1213 -0.1334 -0.0609 125 GLN B CD 3558 O OE1 . GLN B 125 ? 1.2968 1.1363 1.0814 -0.1813 -0.1523 -0.0588 125 GLN B OE1 3559 N NE2 . GLN B 125 ? 1.0929 1.0461 1.0321 -0.1078 -0.1106 -0.0549 125 GLN B NE2 3560 N N . LEU B 126 ? 1.0887 0.9499 0.9799 0.1507 -0.0926 -0.0728 126 LEU B N 3561 C CA . LEU B 126 ? 1.0706 1.0046 1.0077 0.1832 -0.0819 -0.0689 126 LEU B CA 3562 C C . LEU B 126 ? 1.1790 1.0773 1.0497 0.2522 -0.0858 -0.0741 126 LEU B C 3563 O O . LEU B 126 ? 1.2530 1.1538 1.1010 0.2729 -0.0899 -0.0780 126 LEU B O 3564 C CB . LEU B 126 ? 0.9319 0.9802 0.9807 0.1852 -0.0596 -0.0537 126 LEU B CB 3565 C CG . LEU B 126 ? 0.8491 0.9389 0.9548 0.1374 -0.0557 -0.0503 126 LEU B CG 3566 C CD1 . LEU B 126 ? 0.7673 0.9336 0.9491 0.1478 -0.0403 -0.0369 126 LEU B CD1 3567 C CD2 . LEU B 126 ? 0.8830 0.9798 0.9739 0.1018 -0.0665 -0.0567 126 LEU B CD2 3568 N N . ARG B 127 ? 1.2895 1.1624 1.1245 0.2937 -0.0848 -0.0745 127 ARG B N 3569 C CA . ARG B 127 ? 1.4015 1.2568 1.1615 0.3763 -0.0889 -0.0800 127 ARG B CA 3570 C C . ARG B 127 ? 1.3332 1.3240 1.1651 0.4081 -0.0713 -0.0669 127 ARG B C 3571 O O . ARG B 127 ? 1.2537 1.3629 1.1773 0.4009 -0.0524 -0.0480 127 ARG B O 3572 C CB . ARG B 127 ? 1.5788 1.2677 1.1827 0.3948 -0.1192 -0.1008 127 ARG B CB 3573 C CG . ARG B 127 ? 1.6957 1.2346 1.1909 0.3797 -0.1408 -0.1107 127 ARG B CG 3574 C CD . ARG B 127 ? 1.8367 1.2044 1.1983 0.3298 -0.1754 -0.1239 127 ARG B CD 3575 N NE . ARG B 127 ? 2.0127 1.2738 1.2366 0.3953 -0.1972 -0.1396 127 ARG B NE 3576 C CZ . ARG B 127 ? 2.2274 1.3042 1.2909 0.3647 -0.2350 -0.1526 127 ARG B CZ 3577 N NH1 . ARG B 127 ? 2.2979 1.2923 1.3234 0.2592 -0.2551 -0.1486 127 ARG B NH1 3578 N NH2 . ARG B 127 ? 2.3517 1.3269 1.2816 0.4373 -0.2554 -0.1685 127 ARG B NH2 3579 N N . ASP B 128 ? 1.3886 1.3580 1.1726 0.4349 -0.0796 -0.0749 128 ASP B N 3580 C CA . ASP B 128 ? 1.3197 1.4165 1.1588 0.4667 -0.0646 -0.0613 128 ASP B CA 3581 C C . ASP B 128 ? 1.2332 1.3648 1.1390 0.4142 -0.0603 -0.0557 128 ASP B C 3582 O O . ASP B 128 ? 1.2070 1.4244 1.1455 0.4333 -0.0514 -0.0448 128 ASP B O 3583 C CB . ASP B 128 ? 1.4524 1.5244 1.1867 0.5559 -0.0748 -0.0731 128 ASP B CB 3584 C CG . ASP B 128 ? 1.6204 1.5171 1.2267 0.5590 -0.1031 -0.0985 128 ASP B CG 3585 O OD1 . ASP B 128 ? 1.6286 1.5042 1.2559 0.5063 -0.1081 -0.1008 128 ASP B OD1 3586 O OD2 . ASP B 128 ? 1.8168 1.5901 1.2893 0.6129 -0.1232 -0.1154 128 ASP B OD2 3587 N N . ASN B 129 ? 1.1953 1.2722 1.1179 0.3508 -0.0669 -0.0616 129 ASN B N 3588 C CA . ASN B 129 ? 1.1282 1.2485 1.1105 0.3092 -0.0632 -0.0569 129 ASN B CA 3589 C C . ASN B 129 ? 1.0179 1.2281 1.1001 0.2813 -0.0461 -0.0377 129 ASN B C 3590 O O . ASN B 129 ? 0.9634 1.2006 1.0853 0.2539 -0.0445 -0.0348 129 ASN B O 3591 C CB . ASN B 129 ? 1.2004 1.2450 1.1456 0.2570 -0.0802 -0.0707 129 ASN B CB 3592 C CG . ASN B 129 ? 1.3714 1.3010 1.1945 0.2703 -0.1044 -0.0883 129 ASN B CG 3593 O OD1 . ASN B 129 ? 1.5023 1.3941 1.2583 0.3333 -0.1087 -0.0942 129 ASN B OD1 3594 N ND2 . ASN B 129 ? 1.4129 1.2878 1.1948 0.2111 -0.1230 -0.0959 129 ASN B ND2 3595 N N . ALA B 130 ? 0.9513 1.2020 1.0607 0.2909 -0.0362 -0.0246 130 ALA B N 3596 C CA . ALA B 130 ? 0.8656 1.1707 1.0428 0.2595 -0.0262 -0.0062 130 ALA B CA 3597 C C . ALA B 130 ? 0.8423 1.2145 1.0355 0.2719 -0.0178 0.0136 130 ALA B C 3598 O O . ALA B 130 ? 0.8972 1.2678 1.0596 0.3023 -0.0181 0.0091 130 ALA B O 3599 C CB . ALA B 130 ? 0.8447 1.1071 1.0369 0.2242 -0.0289 -0.0139 130 ALA B CB 3600 N N . LYS B 131 ? 0.8175 1.2465 1.0471 0.2464 -0.0132 0.0369 131 LYS B N 3601 C CA . LYS B 131 ? 0.8193 1.3272 1.0627 0.2378 -0.0081 0.0616 131 LYS B CA 3602 C C . LYS B 131 ? 0.7800 1.2550 1.0381 0.2086 -0.0089 0.0626 131 LYS B C 3603 O O . LYS B 131 ? 0.7873 1.2061 1.0561 0.1774 -0.0130 0.0606 131 LYS B O 3604 C CB . LYS B 131 ? 0.8758 1.4417 1.1317 0.2047 -0.0088 0.0906 131 LYS B CB 3605 C CG . LYS B 131 ? 0.9828 1.6021 1.2273 0.2326 -0.0067 0.0942 131 LYS B CG 3606 C CD . LYS B 131 ? 1.0786 1.7854 1.3266 0.1956 -0.0077 0.1310 131 LYS B CD 3607 C CE . LYS B 131 ? 1.1193 1.9546 1.3602 0.2361 -0.0007 0.1419 131 LYS B CE 3608 N NZ . LYS B 131 ? 1.1334 2.0807 1.3757 0.1893 -0.0022 0.1835 131 LYS B NZ 3609 N N . GLU B 132 ? 0.7433 1.2570 0.9957 0.2265 -0.0055 0.0651 132 GLU B N 3610 C CA . GLU B 132 ? 0.6882 1.1845 0.9549 0.1987 -0.0059 0.0692 132 GLU B CA 3611 C C . GLU B 132 ? 0.6699 1.2308 0.9523 0.1494 -0.0080 0.1021 132 GLU B C 3612 O O . GLU B 132 ? 0.6865 1.3599 0.9699 0.1508 -0.0051 0.1242 132 GLU B O 3613 C CB . GLU B 132 ? 0.6868 1.2021 0.9324 0.2401 -0.0030 0.0605 132 GLU B CB 3614 C CG . GLU B 132 ? 0.6747 1.1479 0.9298 0.2182 -0.0038 0.0567 132 GLU B CG 3615 C CD . GLU B 132 ? 0.7058 1.1936 0.9292 0.2652 -0.0025 0.0488 132 GLU B CD 3616 O OE1 . GLU B 132 ? 0.7552 1.2835 0.9397 0.3237 -0.0020 0.0450 132 GLU B OE1 3617 O OE2 . GLU B 132 ? 0.7091 1.1643 0.9376 0.2503 -0.0030 0.0456 132 GLU B OE2 3618 N N . LEU B 133 ? 0.6528 1.1426 0.9344 0.1059 -0.0159 0.1063 133 LEU B N 3619 C CA . LEU B 133 ? 0.6673 1.1749 0.9325 0.0493 -0.0259 0.1382 133 LEU B CA 3620 C C . LEU B 133 ? 0.6789 1.2319 0.9434 0.0121 -0.0294 0.1580 133 LEU B C 3621 O O . LEU B 133 ? 0.7302 1.3381 0.9747 -0.0418 -0.0387 0.1915 133 LEU B O 3622 C CB . LEU B 133 ? 0.7131 1.1021 0.9482 0.0281 -0.0383 0.1334 133 LEU B CB 3623 C CG . LEU B 133 ? 0.7179 1.0788 0.9462 0.0534 -0.0382 0.1227 133 LEU B CG 3624 C CD1 . LEU B 133 ? 0.7908 1.0400 0.9777 0.0471 -0.0516 0.1167 133 LEU B CD1 3625 C CD2 . LEU B 133 ? 0.7189 1.1545 0.9376 0.0379 -0.0392 0.1482 133 LEU B CD2 3626 N N . GLY B 134 ? 0.6565 1.1869 0.9368 0.0334 -0.0240 0.1397 134 GLY B N 3627 C CA . GLY B 134 ? 0.6448 1.2258 0.9278 0.0050 -0.0262 0.1558 134 GLY B CA 3628 C C . GLY B 134 ? 0.6673 1.1429 0.9320 -0.0314 -0.0371 0.1523 134 GLY B C 3629 O O . GLY B 134 ? 0.6740 1.1804 0.9374 -0.0592 -0.0407 0.1648 134 GLY B O 3630 N N . ASN B 135 ? 0.6878 1.0472 0.9340 -0.0248 -0.0429 0.1348 135 ASN B N 3631 C CA . ASN B 135 ? 0.7214 0.9736 0.9311 -0.0491 -0.0565 0.1316 135 ASN B CA 3632 C C . ASN B 135 ? 0.6907 0.8769 0.9152 -0.0048 -0.0500 0.0981 135 ASN B C 3633 O O . ASN B 135 ? 0.7088 0.8080 0.8969 -0.0056 -0.0607 0.0907 135 ASN B O 3634 C CB . ASN B 135 ? 0.8143 0.9871 0.9557 -0.0850 -0.0770 0.1490 135 ASN B CB 3635 C CG . ASN B 135 ? 0.8295 0.9747 0.9695 -0.0471 -0.0738 0.1351 135 ASN B CG 3636 O OD1 . ASN B 135 ? 0.7794 0.9778 0.9714 -0.0040 -0.0568 0.1160 135 ASN B OD1 3637 N ND2 . ASN B 135 ? 0.9320 0.9837 0.9992 -0.0638 -0.0931 0.1448 135 ASN B ND2 3638 N N . GLY B 136 ? 0.6292 0.8578 0.8947 0.0330 -0.0350 0.0794 136 GLY B N 3639 C CA . GLY B 136 ? 0.6047 0.7938 0.8817 0.0612 -0.0303 0.0528 136 GLY B CA 3640 C C . GLY B 136 ? 0.5882 0.7768 0.8673 0.0839 -0.0284 0.0411 136 GLY B C 3641 O O . GLY B 136 ? 0.5660 0.7489 0.8554 0.0996 -0.0249 0.0222 136 GLY B O 3642 N N . CYS B 137 ? 0.6258 0.8290 0.8928 0.0799 -0.0318 0.0544 137 CYS B N 3643 C CA . CYS B 137 ? 0.6570 0.8571 0.9213 0.1007 -0.0318 0.0448 137 CYS B CA 3644 C C . CYS B 137 ? 0.6219 0.8742 0.9006 0.1147 -0.0247 0.0447 137 CYS B C 3645 O O . CYS B 137 ? 0.6139 0.9149 0.8962 0.1112 -0.0213 0.0587 137 CYS B O 3646 C CB . CYS B 137 ? 0.7251 0.8792 0.9465 0.0927 -0.0444 0.0578 137 CYS B CB 3647 S SG . CYS B 137 ? 0.8536 0.9149 1.0219 0.0924 -0.0593 0.0552 137 CYS B SG 3648 N N . PHE B 138 ? 0.6146 0.8639 0.8953 0.1334 -0.0238 0.0291 138 PHE B N 3649 C CA . PHE B 138 ? 0.6138 0.8923 0.8929 0.1510 -0.0207 0.0254 138 PHE B CA 3650 C C . PHE B 138 ? 0.6429 0.9223 0.9155 0.1570 -0.0244 0.0268 138 PHE B C 3651 O O . PHE B 138 ? 0.6436 0.9059 0.9147 0.1612 -0.0278 0.0159 138 PHE B O 3652 C CB . PHE B 138 ? 0.6115 0.8697 0.8819 0.1600 -0.0209 0.0041 138 PHE B CB 3653 C CG . PHE B 138 ? 0.6154 0.8564 0.8778 0.1593 -0.0195 0.0010 138 PHE B CG 3654 C CD1 . PHE B 138 ? 0.6201 0.8744 0.8601 0.1850 -0.0178 0.0036 138 PHE B CD1 3655 C CD2 . PHE B 138 ? 0.6023 0.8196 0.8734 0.1405 -0.0202 -0.0048 138 PHE B CD2 3656 C CE1 . PHE B 138 ? 0.6270 0.8615 0.8496 0.1930 -0.0178 -0.0001 138 PHE B CE1 3657 C CE2 . PHE B 138 ? 0.6138 0.8106 0.8735 0.1401 -0.0195 -0.0072 138 PHE B CE2 3658 C CZ . PHE B 138 ? 0.6228 0.8237 0.8565 0.1669 -0.0187 -0.0050 138 PHE B CZ 3659 N N . GLU B 139 ? 0.6953 1.0070 0.9621 0.1608 -0.0236 0.0410 139 GLU B N 3660 C CA . GLU B 139 ? 0.7328 1.0438 0.9884 0.1674 -0.0274 0.0443 139 GLU B CA 3661 C C . GLU B 139 ? 0.7277 1.0628 0.9847 0.1909 -0.0244 0.0301 139 GLU B C 3662 O O . GLU B 139 ? 0.7571 1.1240 1.0088 0.2052 -0.0206 0.0328 139 GLU B O 3663 C CB . GLU B 139 ? 0.8073 1.1372 1.0457 0.1462 -0.0311 0.0733 139 GLU B CB 3664 C CG . GLU B 139 ? 0.8991 1.2112 1.1115 0.1482 -0.0381 0.0814 139 GLU B CG 3665 C CD . GLU B 139 ? 1.0123 1.3458 1.1971 0.1124 -0.0444 0.1153 139 GLU B CD 3666 O OE1 . GLU B 139 ? 1.0903 1.3828 1.2427 0.0741 -0.0550 0.1336 139 GLU B OE1 3667 O OE2 . GLU B 139 ? 1.1058 1.4996 1.2949 0.1177 -0.0405 0.1254 139 GLU B OE2 3668 N N . PHE B 140 ? 0.7415 1.0648 0.9968 0.1984 -0.0280 0.0149 140 PHE B N 3669 C CA . PHE B 140 ? 0.7566 1.0874 1.0005 0.2111 -0.0298 -0.0001 140 PHE B CA 3670 C C . PHE B 140 ? 0.7833 1.1421 1.0183 0.2287 -0.0289 0.0085 140 PHE B C 3671 O O . PHE B 140 ? 0.7739 1.1449 1.0117 0.2261 -0.0289 0.0246 140 PHE B O 3672 C CB . PHE B 140 ? 0.7261 1.0591 0.9718 0.2030 -0.0353 -0.0155 140 PHE B CB 3673 C CG . PHE B 140 ? 0.7190 1.0401 0.9681 0.1823 -0.0371 -0.0248 140 PHE B CG 3674 C CD1 . PHE B 140 ? 0.7192 1.0446 0.9849 0.1801 -0.0349 -0.0210 140 PHE B CD1 3675 C CD2 . PHE B 140 ? 0.7546 1.0493 0.9758 0.1642 -0.0438 -0.0369 140 PHE B CD2 3676 C CE1 . PHE B 140 ? 0.7096 1.0360 0.9800 0.1612 -0.0358 -0.0284 140 PHE B CE1 3677 C CE2 . PHE B 140 ? 0.7618 1.0456 0.9795 0.1368 -0.0470 -0.0424 140 PHE B CE2 3678 C CZ . PHE B 140 ? 0.7298 1.0408 0.9801 0.1357 -0.0411 -0.0379 140 PHE B CZ 3679 N N . TYR B 141 ? 0.8441 1.2017 1.0547 0.2474 -0.0308 -0.0020 141 TYR B N 3680 C CA . TYR B 141 ? 0.9034 1.2925 1.1020 0.2696 -0.0302 0.0034 141 TYR B CA 3681 C C . TYR B 141 ? 0.9151 1.2993 1.1106 0.2668 -0.0364 -0.0075 141 TYR B C 3682 O O . TYR B 141 ? 0.9997 1.4117 1.1947 0.2794 -0.0355 0.0002 141 TYR B O 3683 C CB . TYR B 141 ? 0.9223 1.3073 1.0790 0.3043 -0.0320 -0.0050 141 TYR B CB 3684 C CG . TYR B 141 ? 0.9375 1.3625 1.0956 0.3208 -0.0248 0.0085 141 TYR B CG 3685 C CD1 . TYR B 141 ? 0.9111 1.4181 1.0993 0.3115 -0.0166 0.0367 141 TYR B CD1 3686 C CD2 . TYR B 141 ? 0.9810 1.3643 1.1008 0.3420 -0.0286 -0.0048 141 TYR B CD2 3687 C CE1 . TYR B 141 ? 0.9361 1.5078 1.1274 0.3206 -0.0107 0.0522 141 TYR B CE1 3688 C CE2 . TYR B 141 ? 0.9820 1.4201 1.1025 0.3642 -0.0218 0.0076 141 TYR B CE2 3689 C CZ . TYR B 141 ? 0.9666 1.5115 1.1285 0.3524 -0.0120 0.0366 141 TYR B CZ 3690 O OH . TYR B 141 ? 0.9738 1.5993 1.1374 0.3696 -0.0060 0.0516 141 TYR B OH 3691 N N . HIS B 142 ? 1.0748 1.5999 1.1002 0.3547 -0.1357 -0.1387 142 HIS B N 3692 C CA . HIS B 142 ? 1.0887 1.6433 1.1115 0.3685 -0.1595 -0.1446 142 HIS B CA 3693 C C . HIS B 142 ? 1.0433 1.6041 1.1050 0.3450 -0.1351 -0.1133 142 HIS B C 3694 O O . HIS B 142 ? 1.0014 1.5317 1.0947 0.3102 -0.1086 -0.0954 142 HIS B O 3695 C CB . HIS B 142 ? 1.1227 1.6617 1.1526 0.3492 -0.2139 -0.1909 142 HIS B CB 3696 C CG . HIS B 142 ? 1.0916 1.5757 1.1607 0.2949 -0.2184 -0.1971 142 HIS B CG 3697 N ND1 . HIS B 142 ? 1.0641 1.5518 1.1833 0.2526 -0.2236 -0.1926 142 HIS B ND1 3698 C CD2 . HIS B 142 ? 1.0902 1.5190 1.1504 0.2829 -0.2163 -0.2050 142 HIS B CD2 3699 C CE1 . HIS B 142 ? 1.0552 1.4850 1.1929 0.2150 -0.2223 -0.1953 142 HIS B CE1 3700 N NE2 . HIS B 142 ? 1.0697 1.4611 1.1694 0.2352 -0.2186 -0.2031 142 HIS B NE2 3701 N N . LYS B 143 ? 1.0783 1.6843 1.1329 0.3706 -0.1449 -0.1088 143 LYS B N 3702 C CA . LYS B 143 ? 1.0488 1.6678 1.1372 0.3549 -0.1309 -0.0856 143 LYS B CA 3703 C C . LYS B 143 ? 0.9990 1.6075 1.1439 0.2984 -0.1593 -0.1088 143 LYS B C 3704 O O . LYS B 143 ? 1.0178 1.6376 1.1710 0.2838 -0.2020 -0.1480 143 LYS B O 3705 C CB . LYS B 143 ? 1.0997 1.7866 1.1646 0.4043 -0.1420 -0.0817 143 LYS B CB 3706 C CG . LYS B 143 ? 1.1615 1.8401 1.1709 0.4586 -0.0929 -0.0360 143 LYS B CG 3707 C CD . LYS B 143 ? 1.2409 1.9916 1.2033 0.5290 -0.1098 -0.0382 143 LYS B CD 3708 C CE . LYS B 143 ? 1.2393 2.0703 1.2424 0.5248 -0.1508 -0.0626 143 LYS B CE 3709 N NZ . LYS B 143 ? 1.2094 2.0246 1.2522 0.4959 -0.1271 -0.0359 143 LYS B NZ 3710 N N . CYS B 144 ? 0.9235 1.5040 1.1026 0.2659 -0.1328 -0.0851 144 CYS B N 3711 C CA . CYS B 144 ? 0.8631 1.4326 1.0923 0.2154 -0.1500 -0.0975 144 CYS B CA 3712 C C . CYS B 144 ? 0.8250 1.4362 1.0847 0.2136 -0.1368 -0.0740 144 CYS B C 3713 O O . CYS B 144 ? 0.8121 1.3967 1.0739 0.2134 -0.1008 -0.0437 144 CYS B O 3714 C CB . CYS B 144 ? 0.8282 1.3324 1.0647 0.1865 -0.1323 -0.0930 144 CYS B CB 3715 S SG . CYS B 144 ? 0.8385 1.3062 1.1153 0.1323 -0.1512 -0.1078 144 CYS B SG 3716 N N . ASP B 145 ? 0.8225 1.5055 1.1040 0.2149 -0.1669 -0.0918 145 ASP B N 3717 C CA . ASP B 145 ? 0.8055 1.5500 1.1172 0.2198 -0.1586 -0.0731 145 ASP B CA 3718 C C . ASP B 145 ? 0.7515 1.4776 1.1172 0.1639 -0.1539 -0.0688 145 ASP B C 3719 O O . ASP B 145 ? 0.7646 1.4240 1.1369 0.1266 -0.1556 -0.0784 145 ASP B O 3720 C CB . ASP B 145 ? 0.8330 1.6870 1.1548 0.2426 -0.1941 -0.0985 145 ASP B CB 3721 C CG . ASP B 145 ? 0.8587 1.7373 1.2216 0.1898 -0.2389 -0.1481 145 ASP B CG 3722 O OD1 . ASP B 145 ? 0.8678 1.6713 1.2493 0.1369 -0.2390 -0.1564 145 ASP B OD1 3723 O OD2 . ASP B 145 ? 0.8997 1.8711 1.2717 0.2029 -0.2735 -0.1810 145 ASP B OD2 3724 N N . ASN B 146 ? 0.7099 1.4973 1.1075 0.1657 -0.1461 -0.0525 146 ASN B N 3725 C CA . ASN B 146 ? 0.6768 1.4516 1.1199 0.1214 -0.1344 -0.0410 146 ASN B CA 3726 C C . ASN B 146 ? 0.7027 1.4681 1.1870 0.0586 -0.1591 -0.0693 146 ASN B C 3727 O O . ASN B 146 ? 0.6969 1.3983 1.1919 0.0251 -0.1449 -0.0596 146 ASN B O 3728 C CB . ASN B 146 ? 0.6398 1.5014 1.1080 0.1419 -0.1239 -0.0206 146 ASN B CB 3729 C CG . ASN B 146 ? 0.6323 1.4634 1.0498 0.1998 -0.0880 0.0146 146 ASN B CG 3730 O OD1 . ASN B 146 ? 0.6154 1.3553 0.9899 0.2102 -0.0651 0.0258 146 ASN B OD1 3731 N ND2 . ASN B 146 ? 0.6239 1.5311 1.0441 0.2375 -0.0809 0.0311 146 ASN B ND2 3732 N N . GLU B 147 ? 0.7726 1.5966 1.2750 0.0438 -0.1945 -0.1054 147 GLU B N 3733 C CA . GLU B 147 ? 0.8456 1.6399 1.3791 -0.0219 -0.2155 -0.1364 147 GLU B CA 3734 C C . GLU B 147 ? 0.8559 1.5274 1.3393 -0.0260 -0.2194 -0.1495 147 GLU B C 3735 O O . GLU B 147 ? 0.8806 1.4754 1.3680 -0.0705 -0.2178 -0.1559 147 GLU B O 3736 C CB . GLU B 147 ? 0.9119 1.8089 1.4851 -0.0463 -0.2535 -0.1800 147 GLU B CB 3737 C CG . GLU B 147 ? 0.9723 1.9542 1.5177 0.0144 -0.2768 -0.1981 147 GLU B CG 3738 C CD . GLU B 147 ? 0.9681 2.0664 1.5259 0.0650 -0.2642 -0.1717 147 GLU B CD 3739 O OE1 . GLU B 147 ? 0.9629 2.0952 1.5622 0.0466 -0.2428 -0.1459 147 GLU B OE1 3740 O OE2 . GLU B 147 ? 1.0011 2.1551 1.5191 0.1304 -0.2743 -0.1752 147 GLU B OE2 3741 N N . CYS B 148 ? 0.8346 1.4883 1.2661 0.0249 -0.2212 -0.1509 148 CYS B N 3742 C CA . CYS B 148 ? 0.8468 1.4010 1.2285 0.0345 -0.2183 -0.1564 148 CYS B CA 3743 C C . CYS B 148 ? 0.7957 1.2872 1.1761 0.0270 -0.1843 -0.1242 148 CYS B C 3744 O O . CYS B 148 ? 0.8381 1.2503 1.2001 0.0096 -0.1838 -0.1307 148 CYS B O 3745 C CB . CYS B 148 ? 0.8671 1.4356 1.1995 0.0926 -0.2186 -0.1571 148 CYS B CB 3746 S SG . CYS B 148 ? 0.9487 1.4271 1.2243 0.1147 -0.2075 -0.1582 148 CYS B SG 3747 N N . MET B 149 ? 0.6983 1.2236 1.0919 0.0450 -0.1564 -0.0916 149 MET B N 3748 C CA . MET B 149 ? 0.6515 1.1309 1.0464 0.0393 -0.1266 -0.0667 149 MET B CA 3749 C C . MET B 149 ? 0.6622 1.1188 1.0876 -0.0040 -0.1259 -0.0633 149 MET B C 3750 O O . MET B 149 ? 0.6620 1.0520 1.0694 -0.0110 -0.1159 -0.0592 149 MET B O 3751 C CB . MET B 149 ? 0.6087 1.1227 1.0083 0.0649 -0.0980 -0.0373 149 MET B CB 3752 C CG . MET B 149 ? 0.6127 1.1253 0.9730 0.1055 -0.0848 -0.0320 149 MET B CG 3753 S SD . MET B 149 ? 0.6559 1.1042 0.9838 0.1083 -0.0718 -0.0401 149 MET B SD 3754 C CE . MET B 149 ? 0.6571 1.1145 0.9478 0.1473 -0.0450 -0.0252 149 MET B CE 3755 N N . GLU B 150 ? 0.6906 1.2086 1.1603 -0.0306 -0.1347 -0.0645 150 GLU B N 3756 C CA . GLU B 150 ? 0.7302 1.2322 1.2328 -0.0780 -0.1282 -0.0579 150 GLU B CA 3757 C C . GLU B 150 ? 0.7821 1.1846 1.2551 -0.1056 -0.1388 -0.0779 150 GLU B C 3758 O O . GLU B 150 ? 0.7753 1.1133 1.2397 -0.1230 -0.1203 -0.0617 150 GLU B O 3759 C CB . GLU B 150 ? 0.7722 1.3771 1.3339 -0.1075 -0.1388 -0.0641 150 GLU B CB 3760 C CG . GLU B 150 ? 0.8422 1.4414 1.4461 -0.1680 -0.1288 -0.0585 150 GLU B CG 3761 C CD . GLU B 150 ? 0.8603 1.4283 1.4630 -0.1630 -0.0930 -0.0183 150 GLU B CD 3762 O OE1 . GLU B 150 ? 0.8427 1.4173 1.4249 -0.1158 -0.0778 0.0024 150 GLU B OE1 3763 O OE2 . GLU B 150 ? 0.9295 1.4625 1.5488 -0.2074 -0.0781 -0.0082 150 GLU B OE2 3764 N N . SER B 151 ? 0.8289 1.2137 1.2766 -0.1016 -0.1671 -0.1121 151 SER B N 3765 C CA . SER B 151 ? 0.9336 1.2118 1.3397 -0.1204 -0.1793 -0.1356 151 SER B CA 3766 C C . SER B 151 ? 0.9429 1.1344 1.2912 -0.0840 -0.1629 -0.1215 151 SER B C 3767 O O . SER B 151 ? 1.0214 1.1130 1.3316 -0.0954 -0.1590 -0.1245 151 SER B O 3768 C CB . SER B 151 ? 0.9895 1.2742 1.3736 -0.1128 -0.2154 -0.1790 151 SER B CB 3769 O OG . SER B 151 ? 0.9674 1.2551 1.3074 -0.0538 -0.2181 -0.1793 151 SER B OG 3770 N N . VAL B 152 ? 0.8871 1.1173 1.2259 -0.0394 -0.1521 -0.1078 152 VAL B N 3771 C CA . VAL B 152 ? 0.8712 1.0515 1.1672 -0.0055 -0.1367 -0.0985 152 VAL B CA 3772 C C . VAL B 152 ? 0.8818 1.0378 1.1880 -0.0171 -0.1110 -0.0706 152 VAL B C 3773 O O . VAL B 152 ? 0.9078 0.9932 1.1706 -0.0022 -0.1037 -0.0679 152 VAL B O 3774 C CB . VAL B 152 ? 0.7966 1.0328 1.0895 0.0328 -0.1275 -0.0941 152 VAL B CB 3775 C CG1 . VAL B 152 ? 0.8011 1.0096 1.0618 0.0613 -0.1128 -0.0911 152 VAL B CG1 3776 C CG2 . VAL B 152 ? 0.8146 1.0732 1.0878 0.0525 -0.1485 -0.1171 152 VAL B CG2 3777 N N . ARG B 153 ? 0.8586 1.0754 1.2153 -0.0359 -0.0972 -0.0494 153 ARG B N 3778 C CA . ARG B 153 ? 0.8923 1.0949 1.2595 -0.0457 -0.0723 -0.0217 153 ARG B CA 3779 C C . ARG B 153 ? 1.0119 1.1471 1.3739 -0.0856 -0.0695 -0.0180 153 ARG B C 3780 O O . ARG B 153 ? 1.0704 1.1496 1.4067 -0.0810 -0.0485 0.0025 153 ARG B O 3781 C CB . ARG B 153 ? 0.8388 1.1266 1.2571 -0.0509 -0.0582 -0.0008 153 ARG B CB 3782 C CG . ARG B 153 ? 0.7747 1.1110 1.1928 -0.0167 -0.0545 -0.0018 153 ARG B CG 3783 C CD . ARG B 153 ? 0.7530 1.1531 1.2060 -0.0139 -0.0374 0.0207 153 ARG B CD 3784 N NE . ARG B 153 ? 0.7361 1.1800 1.1894 0.0094 -0.0387 0.0178 153 ARG B NE 3785 C CZ . ARG B 153 ? 0.7268 1.2325 1.2025 0.0092 -0.0493 0.0174 153 ARG B CZ 3786 N NH1 . ARG B 153 ? 0.7228 1.2699 1.2358 -0.0225 -0.0618 0.0146 153 ARG B NH1 3787 N NH2 . ARG B 153 ? 0.7376 1.2670 1.1963 0.0418 -0.0450 0.0192 153 ARG B NH2 3788 N N . ASN B 154 ? 1.1038 1.2448 1.4882 -0.1252 -0.0886 -0.0389 154 ASN B N 3789 C CA . ASN B 154 ? 1.2360 1.3015 1.6162 -0.1768 -0.0852 -0.0430 154 ASN B CA 3790 C C . ASN B 154 ? 1.2978 1.2225 1.5967 -0.1584 -0.0785 -0.0442 154 ASN B C 3791 O O . ASN B 154 ? 1.3815 1.2245 1.6607 -0.1840 -0.0546 -0.0246 154 ASN B O 3792 C CB . ASN B 154 ? 1.3452 1.4358 1.7516 -0.2167 -0.1160 -0.0823 154 ASN B CB 3793 C CG . ASN B 154 ? 1.4279 1.6397 1.9181 -0.2605 -0.1169 -0.0811 154 ASN B CG 3794 O OD1 . ASN B 154 ? 1.4358 1.7154 1.9633 -0.2560 -0.0941 -0.0484 154 ASN B OD1 3795 N ND2 . ASN B 154 ? 1.6026 1.8506 2.1215 -0.2997 -0.1450 -0.1206 154 ASN B ND2 3796 N N . GLY B 155 ? 1.2479 1.1456 1.4951 -0.1099 -0.0971 -0.0653 155 GLY B N 3797 C CA . GLY B 155 ? 1.3095 1.0771 1.4714 -0.0864 -0.1003 -0.0780 155 GLY B CA 3798 C C . GLY B 155 ? 1.3491 1.0707 1.4965 -0.1144 -0.1295 -0.1191 155 GLY B C 3799 O O . GLY B 155 ? 1.4663 1.0602 1.5394 -0.1055 -0.1326 -0.1338 155 GLY B O 3800 N N . THR B 156 ? 1.2518 1.0769 1.4623 -0.1407 -0.1516 -0.1397 156 THR B N 3801 C CA . THR B 156 ? 1.3081 1.1153 1.5208 -0.1772 -0.1820 -0.1840 156 THR B CA 3802 C C . THR B 156 ? 1.2738 1.1429 1.4721 -0.1317 -0.2144 -0.2146 156 THR B C 3803 O O . THR B 156 ? 1.3146 1.1788 1.5077 -0.1499 -0.2444 -0.2565 156 THR B O 3804 C CB . THR B 156 ? 1.2767 1.1714 1.5790 -0.2489 -0.1823 -0.1874 156 THR B CB 3805 O OG1 . THR B 156 ? 1.3265 1.1496 1.6362 -0.2985 -0.1493 -0.1613 156 THR B OG1 3806 C CG2 . THR B 156 ? 1.3397 1.2524 1.6582 -0.2879 -0.2192 -0.2420 156 THR B CG2 3807 N N . TYR B 157 ? 1.2227 1.1493 1.4127 -0.0741 -0.2070 -0.1956 157 TYR B N 3808 C CA . TYR B 157 ? 1.2010 1.1975 1.3819 -0.0317 -0.2286 -0.2155 157 TYR B CA 3809 C C . TYR B 157 ? 1.3429 1.2653 1.4596 -0.0161 -0.2581 -0.2584 157 TYR B C 3810 O O . TYR B 157 ? 1.4040 1.2397 1.4503 0.0218 -0.2553 -0.2617 157 TYR B O 3811 C CB . TYR B 157 ? 1.1096 1.1429 1.2747 0.0228 -0.2095 -0.1913 157 TYR B CB 3812 C CG . TYR B 157 ? 1.0626 1.1541 1.2087 0.0672 -0.2234 -0.2070 157 TYR B CG 3813 C CD1 . TYR B 157 ? 0.9923 1.1804 1.1786 0.0678 -0.2274 -0.2043 157 TYR B CD1 3814 C CD2 . TYR B 157 ? 1.0872 1.1397 1.1694 0.1147 -0.2295 -0.2218 157 TYR B CD2 3815 C CE1 . TYR B 157 ? 0.9716 1.2065 1.1329 0.1117 -0.2339 -0.2128 157 TYR B CE1 3816 C CE2 . TYR B 157 ? 1.0586 1.1698 1.1233 0.1555 -0.2372 -0.2324 157 TYR B CE2 3817 C CZ . TYR B 157 ? 0.9989 1.1965 1.1021 0.1524 -0.2378 -0.2263 157 TYR B CZ 3818 O OH . TYR B 157 ? 0.9755 1.2243 1.0535 0.1962 -0.2396 -0.2315 157 TYR B OH 3819 N N . ASP B 158 ? 1.4342 1.3971 1.5721 -0.0399 -0.2875 -0.2938 158 ASP B N 3820 C CA . ASP B 158 ? 1.6030 1.4930 1.6803 -0.0308 -0.3195 -0.3425 158 ASP B CA 3821 C C . ASP B 158 ? 1.6284 1.5448 1.6509 0.0472 -0.3286 -0.3482 158 ASP B C 3822 O O . ASP B 158 ? 1.5851 1.6013 1.6236 0.0725 -0.3434 -0.3579 158 ASP B O 3823 C CB . ASP B 158 ? 1.6297 1.5753 1.7512 -0.0797 -0.3514 -0.3856 158 ASP B CB 3824 C CG . ASP B 158 ? 1.7759 1.6008 1.8421 -0.1053 -0.3779 -0.4391 158 ASP B CG 3825 O OD1 . ASP B 158 ? 1.8733 1.5632 1.9098 -0.1412 -0.3602 -0.4341 158 ASP B OD1 3826 O OD2 . ASP B 158 ? 1.8194 1.6764 1.8646 -0.0868 -0.4148 -0.4864 158 ASP B OD2 3827 N N . TYR B 159 ? 1.7213 1.5533 1.6766 0.0890 -0.3165 -0.3395 159 TYR B N 3828 C CA . TYR B 159 ? 1.7364 1.6007 1.6419 0.1626 -0.3187 -0.3414 159 TYR B CA 3829 C C . TYR B 159 ? 1.8332 1.7059 1.6971 0.1903 -0.3551 -0.3870 159 TYR B C 3830 O O . TYR B 159 ? 1.7956 1.7680 1.6665 0.2294 -0.3572 -0.3835 159 TYR B O 3831 C CB . TYR B 159 ? 1.7809 1.5571 1.6182 0.2042 -0.3026 -0.3303 159 TYR B CB 3832 C CG . TYR B 159 ? 1.8211 1.6089 1.5894 0.2804 -0.3118 -0.3463 159 TYR B CG 3833 C CD1 . TYR B 159 ? 1.9535 1.6474 1.6378 0.3102 -0.3394 -0.3872 159 TYR B CD1 3834 C CD2 . TYR B 159 ? 1.7203 1.6129 1.5060 0.3212 -0.2913 -0.3228 159 TYR B CD2 3835 C CE1 . TYR B 159 ? 1.9757 1.6888 1.5938 0.3866 -0.3472 -0.4012 159 TYR B CE1 3836 C CE2 . TYR B 159 ? 1.7543 1.6739 1.4825 0.3892 -0.2965 -0.3366 159 TYR B CE2 3837 C CZ . TYR B 159 ? 1.8820 1.7157 1.5253 0.4260 -0.3249 -0.3744 159 TYR B CZ 3838 O OH . TYR B 159 ? 1.9041 1.7719 1.4866 0.5004 -0.3296 -0.3877 159 TYR B OH 3839 N N . PRO B 160 ? 1.9945 1.7583 1.8113 0.1698 -0.3816 -0.4303 160 PRO B N 3840 C CA . PRO B 160 ? 2.0667 1.8331 1.8359 0.1997 -0.4202 -0.4814 160 PRO B CA 3841 C C . PRO B 160 ? 1.9887 1.8922 1.8185 0.1876 -0.4401 -0.4952 160 PRO B C 3842 O O . PRO B 160 ? 2.0156 1.9665 1.8076 0.2378 -0.4638 -0.5221 160 PRO B O 3843 C CB . PRO B 160 ? 2.2167 1.8283 1.9384 0.1566 -0.4402 -0.5257 160 PRO B CB 3844 C CG . PRO B 160 ? 2.2451 1.7500 1.9532 0.1364 -0.4055 -0.4893 160 PRO B CG 3845 C CD . PRO B 160 ? 2.0939 1.7174 1.8916 0.1187 -0.3747 -0.4355 160 PRO B CD 3846 N N . GLN B 161 ? 1.8993 1.8692 1.8157 0.1295 -0.4297 -0.4761 161 GLN B N 3847 C CA . GLN B 161 ? 1.8268 1.9374 1.7986 0.1273 -0.4448 -0.4831 161 GLN B CA 3848 C C . GLN B 161 ? 1.7167 1.9242 1.6789 0.1976 -0.4264 -0.4477 161 GLN B C 3849 O O . GLN B 161 ? 1.7042 2.0086 1.6704 0.2276 -0.4426 -0.4597 161 GLN B O 3850 C CB . GLN B 161 ? 1.7792 1.9441 1.8419 0.0595 -0.4306 -0.4620 161 GLN B CB 3851 C CG . GLN B 161 ? 1.7368 2.0481 1.8547 0.0561 -0.4503 -0.4762 161 GLN B CG 3852 C CD . GLN B 161 ? 1.6932 2.0630 1.8990 -0.0085 -0.4364 -0.4577 161 GLN B CD 3853 O OE1 . GLN B 161 ? 1.7307 2.0226 1.9589 -0.0725 -0.4262 -0.4582 161 GLN B OE1 3854 N NE2 . GLN B 161 ? 1.6221 2.1282 1.8719 0.0132 -0.4329 -0.4388 161 GLN B NE2 3855 N N . TYR B 162 ? 1.6447 1.8273 1.5927 0.2230 -0.3906 -0.4052 162 TYR B N 3856 C CA . TYR B 162 ? 1.5621 1.8212 1.4993 0.2799 -0.3656 -0.3718 162 TYR B CA 3857 C C . TYR B 162 ? 1.5614 1.7720 1.4296 0.3314 -0.3597 -0.3754 162 TYR B C 3858 O O . TYR B 162 ? 1.5032 1.7675 1.3363 0.3875 -0.3553 -0.3725 162 TYR B O 3859 C CB . TYR B 162 ? 1.4753 1.7762 1.4718 0.2579 -0.3238 -0.3190 162 TYR B CB 3860 C CG . TYR B 162 ? 1.4571 1.7945 1.5214 0.2055 -0.3257 -0.3119 162 TYR B CG 3861 C CD1 . TYR B 162 ? 1.4406 1.8749 1.5294 0.2186 -0.3314 -0.3087 162 TYR B CD1 3862 C CD2 . TYR B 162 ? 1.4607 1.7418 1.5600 0.1494 -0.3192 -0.3060 162 TYR B CD2 3863 C CE1 . TYR B 162 ? 1.4065 1.8909 1.5570 0.1778 -0.3333 -0.3031 162 TYR B CE1 3864 C CE2 . TYR B 162 ? 1.4296 1.7580 1.5937 0.1029 -0.3183 -0.2983 162 TYR B CE2 3865 C CZ . TYR B 162 ? 1.3980 1.8332 1.5897 0.1174 -0.3266 -0.2984 162 TYR B CZ 3866 O OH . TYR B 162 ? 1.3503 1.8482 1.6060 0.0779 -0.3261 -0.2919 162 TYR B OH # _database_PDB_caveat.id 1 _database_PDB_caveat.text 'NAG B1163 HAS WRONG CHIRALITY AT ATOM C1' # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 ASP 1 1 1 ASP ASP A . n A 1 2 GLN 2 2 2 GLN GLN A . n A 1 3 ILE 3 3 3 ILE ILE A . n A 1 4 CYS 4 4 4 CYS CYS A . n A 1 5 ILE 5 5 5 ILE ILE A . n A 1 6 GLY 6 6 6 GLY GLY A . n A 1 7 TYR 7 7 7 TYR TYR A . n A 1 8 HIS 8 8 8 HIS HIS A . n A 1 9 ALA 9 9 9 ALA ALA A . n A 1 10 ASN 10 10 10 ASN ASN A . n A 1 11 ASN 11 11 11 ASN ASN A . n A 1 12 SER 12 12 12 SER SER A . n A 1 13 THR 13 13 13 THR THR A . n A 1 14 GLU 14 14 14 GLU GLU A . n A 1 15 GLN 15 15 15 GLN GLN A . n A 1 16 VAL 16 16 16 VAL VAL A . n A 1 17 ASP 17 17 17 ASP ASP A . n A 1 18 THR 18 18 18 THR THR A . n A 1 19 ILE 19 19 19 ILE ILE A . n A 1 20 MET 20 20 20 MET MET A . n A 1 21 GLU 21 21 21 GLU GLU A . n A 1 22 LYS 22 22 22 LYS LYS A . n A 1 23 ASN 23 23 23 ASN ASN A . n A 1 24 VAL 24 24 24 VAL VAL A . n A 1 25 THR 25 25 25 THR THR A . n A 1 26 VAL 26 26 26 VAL VAL A . n A 1 27 THR 27 27 27 THR THR A . n A 1 28 HIS 28 28 28 HIS HIS A . n A 1 29 ALA 29 29 29 ALA ALA A . n A 1 30 GLN 30 30 30 GLN GLN A . n A 1 31 ASP 31 31 31 ASP ASP A . n A 1 32 ILE 32 32 32 ILE ILE A . n A 1 33 LEU 33 33 33 LEU LEU A . n A 1 34 GLU 34 34 34 GLU GLU A . n A 1 35 LYS 35 35 35 LYS LYS A . n A 1 36 THR 36 36 36 THR THR A . n A 1 37 HIS 37 37 37 HIS HIS A . n A 1 38 ASN 38 38 38 ASN ASN A . n A 1 39 GLY 39 39 39 GLY GLY A . n A 1 40 LYS 40 40 40 LYS LYS A . n A 1 41 LEU 41 41 41 LEU LEU A . n A 1 42 CYS 42 42 42 CYS CYS A . n A 1 43 ASP 43 43 43 ASP ASP A . n A 1 44 LEU 44 44 44 LEU LEU A . n A 1 45 ASP 45 45 45 ASP ASP A . n A 1 46 GLY 46 46 46 GLY GLY A . n A 1 47 VAL 47 47 47 VAL VAL A . n A 1 48 LYS 48 48 48 LYS LYS A . n A 1 49 PRO 49 49 49 PRO PRO A . n A 1 50 LEU 50 50 50 LEU LEU A . n A 1 51 ILE 51 51 51 ILE ILE A . n A 1 52 LEU 52 52 52 LEU LEU A . n A 1 53 ARG 53 53 53 ARG ARG A . n A 1 54 ASP 54 54 54 ASP ASP A . n A 1 55 CYS 55 55 55 CYS CYS A . n A 1 56 SER 56 56 56 SER SER A . n A 1 57 VAL 57 57 57 VAL VAL A . n A 1 58 ALA 58 58 58 ALA ALA A . n A 1 59 GLY 59 59 59 GLY GLY A . n A 1 60 TRP 60 60 60 TRP TRP A . n A 1 61 LEU 61 61 61 LEU LEU A . n A 1 62 LEU 62 62 62 LEU LEU A . n A 1 63 GLY 63 63 63 GLY GLY A . n A 1 64 ASN 64 64 64 ASN ASN A . n A 1 65 PRO 65 65 65 PRO PRO A . n A 1 66 MET 66 66 66 MET MET A . n A 1 67 CYS 67 67 67 CYS CYS A . n A 1 68 ASP 68 68 68 ASP ASP A . n A 1 69 GLU 69 69 69 GLU GLU A . n A 1 70 PHE 70 70 70 PHE PHE A . n A 1 71 ILE 71 71 71 ILE ILE A . n A 1 72 ASN 72 72 72 ASN ASN A . n A 1 73 VAL 73 73 73 VAL VAL A . n A 1 74 PRO 74 74 74 PRO PRO A . n A 1 75 GLU 75 75 75 GLU GLU A . n A 1 76 TRP 76 76 76 TRP TRP A . n A 1 77 SER 77 77 77 SER SER A . n A 1 78 TYR 78 78 78 TYR TYR A . n A 1 79 ILE 79 79 79 ILE ILE A . n A 1 80 VAL 80 80 80 VAL VAL A . n A 1 81 GLU 81 81 81 GLU GLU A . n A 1 82 LYS 82 82 82 LYS LYS A . n A 1 83 ALA 83 83 83 ALA ALA A . n A 1 84 ASN 84 84 84 ASN ASN A . n A 1 85 PRO 85 85 85 PRO PRO A . n A 1 86 VAL 86 86 86 VAL VAL A . n A 1 87 ASN 87 87 87 ASN ASN A . n A 1 88 ASP 88 88 88 ASP ASP A . n A 1 89 LEU 89 89 89 LEU LEU A . n A 1 90 CYS 90 90 90 CYS CYS A . n A 1 91 TYR 91 91 91 TYR TYR A . n A 1 92 PRO 92 92 92 PRO PRO A . n A 1 93 GLY 93 93 93 GLY GLY A . n A 1 94 ASP 94 94 94 ASP ASP A . n A 1 95 PHE 95 95 95 PHE PHE A . n A 1 96 ASN 96 96 96 ASN ASN A . n A 1 97 ASP 97 97 97 ASP ASP A . n A 1 98 TYR 98 98 98 TYR TYR A . n A 1 99 GLU 99 99 99 GLU GLU A . n A 1 100 GLU 100 100 100 GLU GLU A . n A 1 101 LEU 101 101 101 LEU LEU A . n A 1 102 LYS 102 102 102 LYS LYS A . n A 1 103 HIS 103 103 103 HIS HIS A . n A 1 104 LEU 104 104 104 LEU LEU A . n A 1 105 LEU 105 105 105 LEU LEU A . n A 1 106 SER 106 106 106 SER SER A . n A 1 107 ARG 107 107 107 ARG ARG A . n A 1 108 ILE 108 108 108 ILE ILE A . n A 1 109 ASN 109 109 109 ASN ASN A . n A 1 110 HIS 110 110 110 HIS HIS A . n A 1 111 PHE 111 111 111 PHE PHE A . n A 1 112 GLU 112 112 112 GLU GLU A . n A 1 113 LYS 113 113 113 LYS LYS A . n A 1 114 ILE 114 114 114 ILE ILE A . n A 1 115 GLN 115 115 115 GLN GLN A . n A 1 116 ILE 116 116 116 ILE ILE A . n A 1 117 ILE 117 117 117 ILE ILE A . n A 1 118 PRO 118 118 118 PRO PRO A . n A 1 119 LYS 119 119 119 LYS LYS A . n A 1 120 SER 120 120 120 SER SER A . n A 1 121 SER 121 121 121 SER SER A . n A 1 122 TRP 122 122 122 TRP TRP A . n A 1 123 SER 123 123 123 SER SER A . n A 1 124 SER 124 124 124 SER SER A . n A 1 125 HIS 125 125 125 HIS HIS A . n A 1 126 GLU 126 126 126 GLU GLU A . n A 1 127 ALA 127 127 127 ALA ALA A . n A 1 128 SER 128 128 128 SER SER A . n A 1 129 LEU 129 129 129 LEU LEU A . n A 1 130 GLY 130 130 130 GLY GLY A . n A 1 131 VAL 131 131 131 VAL VAL A . n A 1 132 SER 132 132 132 SER SER A . n A 1 133 SER 133 133 133 SER SER A . n A 1 134 ALA 134 134 134 ALA ALA A . n A 1 135 CYS 135 135 135 CYS CYS A . n A 1 136 PRO 136 136 136 PRO PRO A . n A 1 137 TYR 137 137 137 TYR TYR A . n A 1 138 GLN 138 138 138 GLN GLN A . n A 1 139 GLY 139 139 139 GLY GLY A . n A 1 140 LYS 140 140 140 LYS LYS A . n A 1 141 SER 141 141 141 SER SER A . n A 1 142 SER 142 142 142 SER SER A . n A 1 143 PHE 143 143 143 PHE PHE A . n A 1 144 PHE 144 144 144 PHE PHE A . n A 1 145 ARG 145 145 145 ARG ARG A . n A 1 146 ASN 146 146 146 ASN ASN A . n A 1 147 VAL 147 147 147 VAL VAL A . n A 1 148 VAL 148 148 148 VAL VAL A . n A 1 149 TRP 149 149 149 TRP TRP A . n A 1 150 LEU 150 150 150 LEU LEU A . n A 1 151 ILE 151 151 151 ILE ILE A . n A 1 152 LYS 152 152 152 LYS LYS A . n A 1 153 LYS 153 153 153 LYS LYS A . n A 1 154 ASN 154 154 154 ASN ASN A . n A 1 155 SER 155 155 155 SER SER A . n A 1 156 THR 156 156 156 THR THR A . n A 1 157 TYR 157 157 157 TYR TYR A . n A 1 158 PRO 158 158 158 PRO PRO A . n A 1 159 THR 159 159 159 THR THR A . n A 1 160 ILE 160 160 160 ILE ILE A . n A 1 161 LYS 161 161 161 LYS LYS A . n A 1 162 ARG 162 162 162 ARG ARG A . n A 1 163 SER 163 163 163 SER SER A . n A 1 164 TYR 164 164 164 TYR TYR A . n A 1 165 ASN 165 165 165 ASN ASN A . n A 1 166 ASN 166 166 166 ASN ASN A . n A 1 167 THR 167 167 167 THR THR A . n A 1 168 ASN 168 168 168 ASN ASN A . n A 1 169 GLN 169 169 169 GLN GLN A . n A 1 170 GLU 170 170 170 GLU GLU A . n A 1 171 ASP 171 171 171 ASP ASP A . n A 1 172 LEU 172 172 172 LEU LEU A . n A 1 173 LEU 173 173 173 LEU LEU A . n A 1 174 VAL 174 174 174 VAL VAL A . n A 1 175 LEU 175 175 175 LEU LEU A . n A 1 176 TRP 176 176 176 TRP TRP A . n A 1 177 GLY 177 177 177 GLY GLY A . n A 1 178 ILE 178 178 178 ILE ILE A . n A 1 179 HIS 179 179 179 HIS HIS A . n A 1 180 HIS 180 180 180 HIS HIS A . n A 1 181 PRO 181 181 181 PRO PRO A . n A 1 182 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 1322 1322 NAG NAG A . D 3 NAG 1 1323 1323 NAG NAG A . E 3 NAG 2 1324 1324 NAG NAG A . F 3 NAG 1 1325 1325 NAG NAG A . G 3 NAG 2 1326 1326 NAG NAG A . H 4 BMA 3 1327 1327 BMA BMA A . I 4 BMA 4 1328 1328 BMA BMA A . J 5 MAN 5 1329 1329 MAN MAN A . K 3 NAG 1 1330 1330 NAG NAG A . L 6 SIA 1 1331 1331 SIA SIA A . M 7 GAL 2 1332 1332 GAL GAL A . N 3 NAG 1 1163 1163 NAG NAG B . O 3 NAG 2 1164 1164 NAG NAG B . P 4 BMA 3 1165 1165 BMA BMA B . Q 8 MPO 1 1166 1166 MPO MPO B . R 9 HOH 1 2001 2001 HOH HOH A . R 9 HOH 2 2002 2002 HOH HOH A . R 9 HOH 3 2003 2003 HOH HOH A . R 9 HOH 4 2004 2004 HOH HOH A . R 9 HOH 5 2005 2005 HOH HOH A . R 9 HOH 6 2006 2006 HOH HOH A . R 9 HOH 7 2007 2007 HOH HOH A . R 9 HOH 8 2008 2008 HOH HOH A . R 9 HOH 9 2009 2009 HOH HOH A . R 9 HOH 10 2010 2010 HOH HOH A . R 9 HOH 11 2011 2011 HOH HOH A . R 9 HOH 12 2012 2012 HOH HOH A . R 9 HOH 13 2013 2013 HOH HOH A . R 9 HOH 14 2014 2014 HOH HOH A . R 9 HOH 15 2015 2015 HOH HOH A . R 9 HOH 16 2016 2016 HOH HOH A . R 9 HOH 17 2017 2017 HOH HOH A . R 9 HOH 18 2018 2018 HOH HOH A . R 9 HOH 19 2019 2019 HOH HOH A . R 9 HOH 20 2020 2020 HOH HOH A . R 9 HOH 21 2021 2021 HOH HOH A . R 9 HOH 22 2022 2022 HOH HOH A . R 9 HOH 23 2023 2023 HOH HOH A . R 9 HOH 24 2024 2024 HOH HOH A . R 9 HOH 25 2025 2025 HOH HOH A . R 9 HOH 26 2026 2026 HOH HOH A . R 9 HOH 27 2027 2027 HOH HOH A . R 9 HOH 28 2028 2028 HOH HOH A . R 9 HOH 29 2029 2029 HOH HOH A . R 9 HOH 30 2030 2030 HOH HOH A . R 9 HOH 31 2031 2031 HOH HOH A . R 9 HOH 32 2032 2032 HOH HOH A . R 9 HOH 33 2033 2033 HOH HOH A . R 9 HOH 34 2034 2034 HOH HOH A . R 9 HOH 35 2035 2035 HOH HOH A . R 9 HOH 36 2036 2036 HOH HOH A . R 9 HOH 37 2037 2037 HOH HOH A . R 9 HOH 38 2038 2038 HOH HOH A . R 9 HOH 39 2039 2039 HOH HOH A . R 9 HOH 40 2040 2040 HOH HOH A . R 9 HOH 41 2041 2041 HOH HOH A . R 9 HOH 42 2042 2042 HOH HOH A . S 9 HOH 1 2001 2001 HOH HOH B . S 9 HOH 2 2002 2002 HOH HOH B . S 9 HOH 3 2003 2003 HOH HOH B . S 9 HOH 4 2004 2004 HOH HOH B . S 9 HOH 5 2005 2005 HOH HOH B . S 9 HOH 6 2006 2006 HOH HOH B . S 9 HOH 7 2007 2007 HOH HOH B . S 9 HOH 8 2008 2008 HOH HOH B . S 9 HOH 9 2009 2009 HOH HOH B . S 9 HOH 10 2010 2010 HOH HOH B . S 9 HOH 11 2011 2011 HOH HOH B . S 9 HOH 12 2012 2012 HOH HOH B . S 9 HOH 13 2013 2013 HOH HOH B . S 9 HOH 14 2014 2014 HOH HOH B . S 9 HOH 15 2015 2015 HOH HOH B . S 9 HOH 16 2016 2016 HOH HOH B . S 9 HOH 17 2017 2017 HOH HOH B . S 9 HOH 18 2018 2018 HOH HOH B . S 9 HOH 19 2019 2019 HOH HOH B . S 9 HOH 20 2020 2020 HOH HOH B . S 9 HOH 21 2021 2021 HOH HOH B . S 9 HOH 22 2022 2022 HOH HOH B . S 9 HOH 23 2023 2023 HOH HOH B . S 9 HOH 24 2024 2024 HOH HOH B . S 9 HOH 25 2025 2025 HOH HOH B . S 9 HOH 26 2026 2026 HOH HOH B . S 9 HOH 27 2027 2027 HOH HOH B . S 9 HOH 28 2028 2028 HOH HOH B . S 9 HOH 29 2029 2029 HOH HOH B . S 9 HOH 30 2030 2030 HOH HOH B . # loop_ _pdbx_struct_mod_residue.id _pdbx_struct_mod_residue.label_asym_id _pdbx_struct_mod_residue.label_comp_id _pdbx_struct_mod_residue.label_seq_id _pdbx_struct_mod_residue.auth_asym_id _pdbx_struct_mod_residue.auth_comp_id _pdbx_struct_mod_residue.auth_seq_id _pdbx_struct_mod_residue.PDB_ins_code _pdbx_struct_mod_residue.parent_comp_id _pdbx_struct_mod_residue.details 1 A ASN 11 A ASN 11 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 23 A ASN 23 ? ASN 'GLYCOSYLATION SITE' 3 A ASN 165 A ASN 165 ? ASN 'GLYCOSYLATION SITE' 4 A ASN 286 A ASN 286 ? ASN 'GLYCOSYLATION SITE' 5 B ASN 154 B ASN 154 ? ASN 'GLYCOSYLATION SITE' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_and_software_defined_assembly _pdbx_struct_assembly.method_details PISA _pdbx_struct_assembly.oligomeric_details hexameric _pdbx_struct_assembly.oligomeric_count 6 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1,2,3 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S # loop_ _pdbx_struct_assembly_prop.biol_id _pdbx_struct_assembly_prop.type _pdbx_struct_assembly_prop.value _pdbx_struct_assembly_prop.details 1 'ABSA (A^2)' 37560 ? 1 MORE -26.8 ? 1 'SSA (A^2)' 64190 ? # 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 50.5385000000 0.8660254038 -0.5000000000 0.0000000000 -87.5352497383 0.0000000000 0.0000000000 1.0000000000 0.0000000000 3 'crystal symmetry operation' 3_655 -x+y+1,-x,z -0.5000000000 0.8660254038 0.0000000000 101.0770000000 -0.8660254038 -0.5000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 2014-05-28 2 'Structure model' 1 1 2014-06-11 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # _pdbx_audit_revision_group.ordinal 1 _pdbx_audit_revision_group.revision_ordinal 2 _pdbx_audit_revision_group.data_content_type 'Structure model' _pdbx_audit_revision_group.group 'Database references' # loop_ _pdbx_refine_tls.pdbx_refine_id _pdbx_refine_tls.id _pdbx_refine_tls.details _pdbx_refine_tls.method _pdbx_refine_tls.origin_x _pdbx_refine_tls.origin_y _pdbx_refine_tls.origin_z _pdbx_refine_tls.T[1][1] _pdbx_refine_tls.T[2][2] _pdbx_refine_tls.T[3][3] _pdbx_refine_tls.T[1][2] _pdbx_refine_tls.T[1][3] _pdbx_refine_tls.T[2][3] _pdbx_refine_tls.L[1][1] _pdbx_refine_tls.L[2][2] _pdbx_refine_tls.L[3][3] _pdbx_refine_tls.L[1][2] _pdbx_refine_tls.L[1][3] _pdbx_refine_tls.L[2][3] _pdbx_refine_tls.S[1][1] _pdbx_refine_tls.S[1][2] _pdbx_refine_tls.S[1][3] _pdbx_refine_tls.S[2][1] _pdbx_refine_tls.S[2][2] _pdbx_refine_tls.S[2][3] _pdbx_refine_tls.S[3][1] _pdbx_refine_tls.S[3][2] _pdbx_refine_tls.S[3][3] 'X-RAY DIFFRACTION' 1 ? refined 34.3145 -13.9468 -18.7249 0.0364 0.3957 0.3219 0.0409 0.0262 -0.1132 0.4250 0.3894 4.3410 -0.0906 -0.4930 0.8329 0.0259 -0.1598 0.0894 0.0220 -0.2234 0.1317 -0.2421 -0.9201 0.1975 'X-RAY DIFFRACTION' 2 ? refined 32.1046 -21.4246 16.6523 0.5840 0.7734 0.2744 -0.0778 0.1251 -0.1277 1.9523 2.4615 1.8459 0.2531 0.6003 -0.3670 -0.0972 -0.2244 0.0971 0.9631 -0.0035 0.0501 0.2775 -0.5029 0.1006 'X-RAY DIFFRACTION' 3 ? refined 35.5577 -14.6567 -26.9173 0.1572 0.2278 0.3721 0.0258 0.0451 -0.0761 1.3877 0.4070 10.1862 -0.1644 -0.9090 2.0227 0.1535 -0.3678 0.1810 0.0361 -0.1184 0.0278 0.2396 -0.5170 -0.0351 'X-RAY DIFFRACTION' 4 ? refined 36.1479 -20.8185 -58.7041 0.1422 0.2590 0.5241 0.1003 -0.0214 -0.0259 1.5320 1.6339 8.0726 -1.1466 2.1619 -0.8295 -0.0486 0.0813 -0.0066 0.2893 -0.1078 0.0873 -0.3023 -0.9654 0.1564 'X-RAY DIFFRACTION' 5 ? refined 48.0591 -22.6582 -10.2925 0.1200 0.0383 0.1608 -0.0170 0.0062 -0.0310 7.5134 2.5332 17.0203 1.6914 6.1551 2.1470 0.0458 -0.2282 -0.0657 0.3427 -0.2292 0.3110 -0.0856 -0.3037 0.1834 'X-RAY DIFFRACTION' 6 ? refined 44.4850 -23.8151 -56.7180 0.0774 0.1317 0.3643 0.0319 -0.0083 -0.0056 1.6047 0.6062 17.7587 -0.6806 3.3501 -1.5010 0.1045 0.1870 0.0478 -0.0054 -0.2331 0.0178 0.5246 0.2722 0.1286 'X-RAY DIFFRACTION' 7 ? refined 31.5095 -25.8075 -80.7455 0.3378 0.7011 0.6315 0.0340 -0.2281 -0.1863 5.7673 3.4378 11.8553 -4.0495 -2.1987 1.6041 0.6847 1.2478 -1.0745 -0.4633 -0.4541 1.0240 1.4472 -1.1374 -0.2306 # loop_ _pdbx_refine_tls_group.pdbx_refine_id _pdbx_refine_tls_group.id _pdbx_refine_tls_group.refine_tls_id _pdbx_refine_tls_group.beg_auth_asym_id _pdbx_refine_tls_group.beg_auth_seq_id _pdbx_refine_tls_group.beg_label_asym_id _pdbx_refine_tls_group.beg_label_seq_id _pdbx_refine_tls_group.end_auth_asym_id _pdbx_refine_tls_group.end_auth_seq_id _pdbx_refine_tls_group.end_label_asym_id _pdbx_refine_tls_group.end_label_seq_id _pdbx_refine_tls_group.selection _pdbx_refine_tls_group.selection_details 'X-RAY DIFFRACTION' 1 1 A 1 ? ? A 105 ? ? ? ? 'X-RAY DIFFRACTION' 2 2 A 106 ? ? A 262 ? ? ? ? 'X-RAY DIFFRACTION' 3 3 A 263 ? ? A 321 ? ? ? ? 'X-RAY DIFFRACTION' 4 4 B 1 ? ? B 60 ? ? ? ? 'X-RAY DIFFRACTION' 5 5 B 61 ? ? B 84 ? ? ? ? 'X-RAY DIFFRACTION' 6 6 B 85 ? ? B 141 ? ? ? ? 'X-RAY DIFFRACTION' 7 7 B 142 ? ? B 163 ? ? ? ? # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal REFMAC refinement 5.8.0046 ? 1 xia2 'data reduction' . ? 2 SCALA 'data scaling' . ? 3 PHASER phasing . ? 4 # _pdbx_entry_details.entry_id 4CQR _pdbx_entry_details.compound_details ? _pdbx_entry_details.source_details ? _pdbx_entry_details.nonpolymer_details ? _pdbx_entry_details.sequence_details 'MULTIBASIC SITE REMOVED' # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 ARG A 53 ? ? 58.39 -110.83 2 1 ASP A 88 ? ? -110.87 -110.04 3 1 CYS A 135 ? ? -114.96 66.30 4 1 SER A 142 ? ? -127.64 -160.00 5 1 ARG A 192 ? ? 62.41 -69.64 6 1 ALA A 214 ? ? -173.88 136.20 7 1 ARG B 127 ? ? 55.92 -108.27 8 1 TYR B 157 ? ? -48.70 106.08 # loop_ _pdbx_validate_chiral.id _pdbx_validate_chiral.PDB_model_num _pdbx_validate_chiral.auth_atom_id _pdbx_validate_chiral.label_alt_id _pdbx_validate_chiral.auth_asym_id _pdbx_validate_chiral.auth_comp_id _pdbx_validate_chiral.auth_seq_id _pdbx_validate_chiral.PDB_ins_code _pdbx_validate_chiral.details _pdbx_validate_chiral.omega 1 1 C1 ? A BMA 1327 ? PLANAR . 2 1 C1 ? B NAG 1163 ? 'WRONG HAND' . # 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 BETA-D-MANNOSE BMA 5 ALPHA-D-MANNOSE MAN 6 'O-SIALIC ACID' SIA 7 BETA-D-GALACTOSE GAL 8 '3[N-MORPHOLINO]PROPANE SULFONIC ACID' MPO 9 water HOH #