data_4CQQ # _entry.id 4CQQ # _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 4CQQ PDBE EBI-59780 WWPDB D_1290059780 # 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 4CQR unspecified ;H5 (VN1194) SER227ASN/GLN196ARG MUTANT HAEMAGGLUTININ IN COMPLEX WITH HUMAN RECEPTOR ANALOGUE 6'SLN ; PDB 4CQS unspecified ;H5 (VN1194) ASN186LYS MUTANT HAEMAGGLUTININ IN COMPLEX WITH AVIAN RECEPTOR ANALOGUE 3'SLN ; PDB 4CQT unspecified ;H5 (VN1194) ASN186LYS MUTANT HAEMAGGLUTININ IN COMPLEX WITH AVIAN RECEPTOR ANALOGUE 3'SLN ; PDB 4CQU unspecified ;H5 (VN1194) ASN186LYS MUTANT HAEMAGGLUTININ IN COMPLEX WITH HUMAN RECEPTOR ANALOGUE 6'SLN ; PDB 4CQV unspecified 'CRYSTAL STRUCTURE OF H5 (TYTY) DEL133/ILE155THR MUTANT HAEMAGGLUTININ' PDB 4CQW unspecified ;H5 (TYTY) DEL133/ILE155THR MUTANT HAEMAGGLUTININ IN COMPLEX WITH AVIAN RECEPTOR ANALOGUE 3'SLN ; PDB 4CQX unspecified ;H5 (TYTY) DEL133/ILE155THR MUTANT HAEMAGGLUTININ IN COMPLEX WITH HUMAN RECEPTOR ANALOGUE 6'SLN ; PDB 4CQY unspecified 'H5 (TYTY) DEL133/ILE155THR MUTANT HAEMAGGLUTININ IN COMPLEX WITH AVIAN RECEPTOR ANALOGUE LSTA' PDB 4CQZ unspecified 'CRYSTAL STRUCTURE OF H5 (VN1194) GLN196ARG MUTANT HAEMAGGLUTININ' PDB 4CR0 unspecified 'CRYSTAL STRUCTURE OF H5 (VN1194) ASN186LYS/GLY143ARG MUTANT HAEMAGGLUTININ' # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 4CQQ _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 4CQQ _cell.length_a 101.668 _cell.length_b 101.668 _cell.length_c 452.440 _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 4CQQ _symmetry.space_group_name_H-M 'H 3 2' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 155 # loop_ _entity.id _entity.type _entity.src_method _entity.pdbx_description _entity.formula_weight _entity.pdbx_number_of_molecules _entity.pdbx_ec _entity.pdbx_mutation _entity.pdbx_fragment _entity.details 1 polymer nat 'HAEMAGGLUTININ HA1' 37006.852 1 ? YES 'HA1 OF TRYPSIN RELEASED ECTODOMAIN, RESIDUES 17-342' ? 2 polymer nat 'HAEMAGGLUTININ HA2' 19097.990 1 ? ? 'HA2 OF TRYPSIN RELEASED ECTODOMAIN, RESIDUES 347-512' ? 3 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 8 ? ? ? ? 4 non-polymer man ALPHA-D-MANNOSE 180.156 2 ? ? ? ? 5 non-polymer man BETA-D-MANNOSE 180.156 2 ? ? ? ? 6 non-polymer 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 97 ? ? ? ? # 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 4CQQ A 1 ? 326 ? Q6DQ34 17 ? 342 ? 1 326 2 2 4CQQ 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 4CQQ ARG A 192 ? UNP Q6DQ34 GLN 208 'engineered mutation' 192 1 1 4CQQ ASN A 223 ? UNP Q6DQ34 SER 239 'engineered mutation' 223 2 1 4CQQ 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 4CQQ _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 3.74 _exptl_crystal.density_percent_sol 67 _exptl_crystal.description NONE # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method ? _exptl_crystal_grow.temp ? _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH ? _exptl_crystal_grow.pdbx_pH_range ? _exptl_crystal_grow.pdbx_details '0.1 M HEPES/MOPS PH 7.0, 0.05 M MGCL2, 28-30% PEG 550 MME, SEEDED WITH CRUSHED WILD-TYPE VN1194 HA CRYSTALS' # _diffrn.id 1 _diffrn.ambient_temp 100 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator ? _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 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 4CQQ _reflns.observed_criterion_sigma_I 2.6 _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 37.70 _reflns.d_resolution_high 2.55 _reflns.number_obs 29806 _reflns.number_all ? _reflns.percent_possible_obs 99.3 _reflns.pdbx_Rmerge_I_obs 0.08 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 14.70 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 9.3 # _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_ordinal 1 _reflns_shell.d_res_high 2.55 _reflns_shell.d_res_low 2.69 _reflns_shell.percent_possible_all 97.3 _reflns_shell.Rmerge_I_obs 0.69 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs 2.60 _reflns_shell.pdbx_redundancy 8.3 # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 4CQQ _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 28286 _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 150.81 _refine.ls_d_res_high 2.55 _refine.ls_percent_reflns_obs 99.19 _refine.ls_R_factor_obs 0.19888 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.19646 _refine.ls_R_factor_R_free 0.24565 _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 1519 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.957 _refine.correlation_coeff_Fo_to_Fc_free 0.934 _refine.B_iso_mean 87.509 _refine.aniso_B[1][1] 2.79 _refine.aniso_B[2][2] 2.79 _refine.aniso_B[3][3] -9.04 _refine.aniso_B[1][2] 1.39 _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 0.306 _refine.pdbx_overall_ESU_R_Free 0.245 _refine.overall_SU_ML 0.199 _refine.pdbx_overall_phase_error ? _refine.overall_SU_B 18.991 _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 97 _refine_hist.number_atoms_total 4161 _refine_hist.d_res_high 2.55 _refine_hist.d_res_low 150.81 # loop_ _refine_ls_restr.type _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.number _refine_ls_restr.pdbx_refine_id _refine_ls_restr.pdbx_restraint_function r_bond_refined_d 0.005 0.019 ? 4172 'X-RAY DIFFRACTION' ? r_bond_other_d 0.001 0.020 ? 3808 'X-RAY DIFFRACTION' ? r_angle_refined_deg 1.051 1.994 ? 5673 'X-RAY DIFFRACTION' ? r_angle_other_deg 0.675 3.003 ? 8742 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 5.646 5.000 ? 481 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg 37.962 25.099 ? 202 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg 14.947 15.000 ? 678 'X-RAY DIFFRACTION' ? r_dihedral_angle_4_deg 13.723 15.000 ? 18 'X-RAY DIFFRACTION' ? r_chiral_restr 0.057 0.200 ? 637 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.003 0.020 ? 4624 'X-RAY DIFFRACTION' ? r_gen_planes_other 0.001 0.020 ? 949 '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 1.425 4.670 ? 1930 'X-RAY DIFFRACTION' ? r_mcbond_other 1.421 4.669 ? 1929 'X-RAY DIFFRACTION' ? r_mcangle_it 2.356 7.004 ? 2409 'X-RAY DIFFRACTION' ? r_mcangle_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scbond_it 2.591 5.652 ? 2241 'X-RAY DIFFRACTION' ? r_scbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scangle_it ? ? ? ? 'X-RAY DIFFRACTION' ? r_scangle_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_long_range_B_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_long_range_B_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_rigid_bond_restr ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_free ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_bonded ? ? ? ? 'X-RAY DIFFRACTION' ? # _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_ls_shell.pdbx_total_number_of_bins_used 20 _refine_ls_shell.d_res_high 2.550 _refine_ls_shell.d_res_low 2.616 _refine_ls_shell.number_reflns_R_work 2012 _refine_ls_shell.R_factor_R_work 0.327 _refine_ls_shell.percent_reflns_obs 95.90 _refine_ls_shell.R_factor_R_free 0.378 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 91 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? # _struct.entry_id 4CQQ _struct.title ;H5 (VN1194) Ser227Asn/Gln196Arg Mutant Haemagglutinin in Complex with Avian Receptor Analogue 3'SLN ; _struct.pdbx_descriptor 'HAEMAGGLUTININ HA1, HAEMAGGLUTININ HA2' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 4CQQ _struct_keywords.pdbx_keywords 'VIRAL PROTEIN' _struct_keywords.text ;VIRAL PROTEIN, SIALIC ACID, GLYCOPROTEIN, VIRUS RECEPTOR, AVIAN FLU, SIALYLLACTOSAMINE, 3SLN, 3'SLN, 6SLN, 6'SLN, LSTA ; # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 3 ? D N N 3 ? E N N 3 ? F N N 3 ? G N N 3 ? H N N 4 ? I N N 5 ? J N N 4 ? K N N 3 ? L N N 6 ? M N N 7 ? N N N 3 ? O N N 3 ? P N N 5 ? Q N N 8 ? R N N 9 ? S N N 9 ? # _struct_biol.id 1 # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 1 SER A 56 ? GLY A 63 ? SER A 56 GLY A 63 1 ? 8 HELX_P HELX_P2 2 ASN A 64 ? ILE A 71 ? ASN A 64 ILE A 71 5 ? 8 HELX_P HELX_P3 3 ASP A 97 ? SER A 106 ? ASP A 97 SER A 106 1 ? 10 HELX_P HELX_P4 4 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 HELX_P HELX_P9 9 ASP B 158 ? TYR B 162 ? ASP B 158 TYR B 162 5 ? 5 # _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 ? ? ? ? ? ? ? 2.096 ? disulf2 disulf ? ? A CYS 42 SG ? ? ? 1_555 A CYS 274 SG ? ? A CYS 42 A CYS 274 1_555 ? ? ? ? ? ? ? 2.033 ? disulf3 disulf ? ? A CYS 55 SG ? ? ? 1_555 A CYS 67 SG ? ? A CYS 55 A CYS 67 1_555 ? ? ? ? ? ? ? 2.045 ? disulf4 disulf ? ? A CYS 90 SG ? ? ? 1_555 A CYS 135 SG ? ? A CYS 90 A CYS 135 1_555 ? ? ? ? ? ? ? 2.058 ? disulf5 disulf ? ? A CYS 278 SG ? ? ? 1_555 A CYS 302 SG ? ? A CYS 278 A CYS 302 1_555 ? ? ? ? ? ? ? 2.053 ? disulf6 disulf ? ? B CYS 144 SG ? ? ? 1_555 B CYS 148 SG ? ? B CYS 144 B CYS 148 1_555 ? ? ? ? ? ? ? 2.053 ? covale1 covale ? ? A ASN 11 ND2 ? ? ? 1_555 C NAG . C1 ? ? A ASN 11 A NAG 1011 1_555 ? ? ? ? ? ? ? 1.450 ? covale2 covale ? ? A ASN 23 ND2 ? ? ? 1_555 D NAG . C1 ? ? A ASN 23 A NAG 1023 1_555 ? ? ? ? ? ? ? 1.442 ? covale3 covale ? ? A ASN 165 ND2 ? ? ? 1_555 F NAG . C1 ? ? A ASN 165 A NAG 1165 1_555 ? ? ? ? ? ? ? 1.444 ? covale4 covale ? ? A ASN 286 ND2 ? ? ? 1_555 K NAG . C1 ? ? A ASN 286 A NAG 1286 1_555 ? ? ? ? ? ? ? 1.449 ? covale5 covale ? ? D NAG . O4 ? ? ? 1_555 E NAG . C1 ? ? A NAG 1023 A NAG 1024 1_555 ? ? ? ? ? ? ? 1.444 ? covale6 covale ? ? F NAG . O4 ? ? ? 1_555 G NAG . C1 ? ? A NAG 1165 A NAG 1166 1_555 ? ? ? ? ? ? ? 1.440 ? covale7 covale ? ? G NAG . O4 ? ? ? 1_555 H MAN . C1 ? ? A NAG 1166 A MAN 1167 1_555 ? ? ? ? ? ? ? 1.450 ? covale8 covale ? ? H MAN . O3 ? ? ? 1_555 I BMA . C1 ? ? A MAN 1167 A BMA 1168 1_555 ? ? ? ? ? ? ? 1.445 ? covale9 covale ? ? H MAN . O6 ? ? ? 1_555 J MAN . C1 ? ? A MAN 1167 A MAN 1169 1_555 ? ? ? ? ? ? ? 1.449 ? covale10 covale ? ? L SIA . C2 ? ? ? 1_555 M GAL . O3 ? ? A SIA 1322 A GAL 1323 1_555 ? ? ? ? ? ? ? 1.435 ? covale11 covale ? ? B ASN 154 ND2 ? ? ? 1_555 N NAG . C1 ? ? B ASN 154 B NAG 1154 1_555 ? ? ? ? ? ? ? 1.439 ? covale12 covale ? ? N NAG . O4 ? ? ? 1_555 O NAG . C1 ? ? B NAG 1154 B NAG 1155 1_555 ? ? ? ? ? ? ? 1.444 ? covale13 covale ? ? O NAG . O4 ? ? ? 1_555 P BMA . C1 ? ? B NAG 1155 B BMA 1156 1_555 ? ? ? ? ? ? ? 1.447 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details BA ? 5 ? AA ? 2 ? AB ? 2 ? AC ? 3 ? AD ? 2 ? AE ? 3 ? AF ? 5 ? AG ? 5 ? AH ? 2 ? AI ? 4 ? AJ ? 3 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense BA 1 2 ? anti-parallel BA 2 3 ? anti-parallel BA 3 4 ? anti-parallel BA 4 5 ? anti-parallel AA 1 2 ? anti-parallel AB 1 2 ? anti-parallel AC 1 2 ? parallel AC 2 3 ? parallel AD 1 2 ? parallel AE 1 2 ? parallel AE 2 3 ? parallel AF 1 2 ? parallel AF 2 3 ? anti-parallel AF 3 4 ? anti-parallel AF 4 5 ? anti-parallel AG 1 2 ? parallel AG 2 3 ? anti-parallel AG 3 4 ? anti-parallel AG 4 5 ? anti-parallel AH 1 2 ? anti-parallel AI 1 2 ? anti-parallel AI 2 3 ? anti-parallel AI 3 4 ? anti-parallel AJ 1 2 ? anti-parallel AJ 2 3 ? anti-parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id BA 1 GLY B 31 ? ALA B 36 ? GLY B 31 ALA B 36 BA 2 TYR B 22 ? ASN B 28 ? TYR B 22 ASN B 28 BA 3 GLN A 2 ? TYR A 7 ? GLN A 2 TYR A 7 BA 4 CYS B 137 ? PHE B 140 ? CYS B 137 PHE B 140 BA 5 ALA B 130 ? GLU B 132 ? ALA B 130 GLU B 132 AA 1 GLN A 15 ? VAL A 16 ? GLN A 15 VAL A 16 AA 2 VAL A 24 ? THR A 25 ? VAL A 24 THR A 25 AB 1 ALA A 29 ? ASP A 31 ? ALA A 29 ASP A 31 AB 2 VAL A 312 ? ALA A 314 ? VAL A 312 ALA A 314 AC 1 LEU A 33 ? GLU A 34 ? LEU A 33 GLU A 34 AC 2 PHE A 291 ? HIS A 292 ? PHE A 291 HIS A 292 AC 3 LYS A 304 ? TYR A 305 ? LYS A 304 TYR A 305 AD 1 LEU A 41 ? LEU A 44 ? LEU A 41 LEU A 44 AD 2 TYR A 271 ? THR A 276 ? TYR A 271 THR A 276 AE 1 LEU A 50 ? ILE A 51 ? LEU A 50 ILE A 51 AE 2 ILE A 79 ? GLU A 81 ? ILE A 79 GLU A 81 AE 3 ILE A 264 ? LYS A 266 ? ILE A 264 LYS A 266 AF 1 GLY A 93 ? PHE A 95 ? GLY A 93 PHE A 95 AF 2 ARG A 225 ? LEU A 233 ? ARG A 225 LEU A 233 AF 3 LEU A 172 ? HIS A 180 ? LEU A 172 HIS A 180 AF 4 PHE A 247 ? PRO A 250 ? PHE A 247 PRO A 250 AF 5 VAL A 147 ? TRP A 149 ? VAL A 147 TRP A 149 AG 1 GLY A 93 ? PHE A 95 ? GLY A 93 PHE A 95 AG 2 ARG A 225 ? LEU A 233 ? ARG A 225 LEU A 233 AG 3 LEU A 172 ? HIS A 180 ? LEU A 172 HIS A 180 AG 4 TYR A 252 ? LYS A 259 ? TYR A 252 LYS A 259 AG 5 ILE A 108 ? GLN A 115 ? ILE A 108 GLN A 115 AH 1 SER A 132 ? TYR A 137 ? SER A 132 TYR A 137 AH 2 LYS A 140 ? SER A 142 ? LYS A 140 SER A 142 AI 1 ILE A 160 ? ASN A 165 ? ILE A 160 ASN A 165 AI 2 ALA A 238 ? SER A 243 ? ALA A 238 SER A 243 AI 3 ILE A 198 ? GLY A 201 ? ILE A 198 GLY A 201 AI 4 ASN A 206 ? LEU A 209 ? ASN A 206 LEU A 209 AJ 1 GLY A 283 ? ALA A 284 ? GLY A 283 ALA A 284 AJ 2 CYS A 278 ? THR A 280 ? CYS A 278 THR A 280 AJ 3 ILE A 299 ? GLY A 300 ? ILE A 299 GLY A 300 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id BA 1 2 N ALA B 35 ? N ALA B 35 O TYR B 24 ? O TYR B 24 BA 2 3 N SER B 27 ? N SER B 27 O GLN A 2 ? O GLN A 2 BA 3 4 N ILE A 3 ? N ILE A 3 O PHE B 138 ? O PHE B 138 BA 4 5 N GLU B 139 ? N GLU B 139 O LYS B 131 ? O LYS B 131 AA 1 2 N VAL A 16 ? N VAL A 16 O VAL A 24 ? O VAL A 24 AB 1 2 N GLN A 30 ? N GLN A 30 O LEU A 313 ? O LEU A 313 AC 1 2 N GLU A 34 ? N GLU A 34 O PHE A 291 ? O PHE A 291 AC 2 3 N HIS A 292 ? N HIS A 292 O LYS A 304 ? O LYS A 304 AD 1 2 O LEU A 41 ? O LEU A 41 N GLY A 272 ? N GLY A 272 AE 1 2 O LEU A 50 ? O LEU A 50 N VAL A 80 ? N VAL A 80 AE 2 3 N GLU A 81 ? N GLU A 81 O MET A 265 ? O MET A 265 AF 1 2 N ASP A 94 ? N ASP A 94 O MET A 226 ? O MET A 226 AF 2 3 N LEU A 233 ? N LEU A 233 O LEU A 172 ? O LEU A 172 AF 3 4 N GLY A 177 ? N GLY A 177 O ILE A 248 ? O ILE A 248 AF 4 5 N ALA A 249 ? N ALA A 249 O VAL A 148 ? O VAL A 148 AG 1 2 N ASP A 94 ? N ASP A 94 O MET A 226 ? O MET A 226 AG 2 3 N LEU A 233 ? N LEU A 233 O LEU A 172 ? O LEU A 172 AG 3 4 N LEU A 173 ? N LEU A 173 O TYR A 254 ? O TYR A 254 AG 4 5 O LYS A 258 ? O LYS A 258 N ASN A 109 ? N ASN A 109 AH 1 2 N TYR A 137 ? N TYR A 137 O LYS A 140 ? O LYS A 140 AI 1 2 N TYR A 164 ? N TYR A 164 O ILE A 239 ? O ILE A 239 AI 2 3 N GLU A 242 ? N GLU A 242 O SER A 199 ? O SER A 199 AI 3 4 N VAL A 200 ? N VAL A 200 O GLN A 207 ? O GLN A 207 AJ 1 2 N GLY A 283 ? N GLY A 283 O THR A 280 ? O THR A 280 AJ 2 3 N GLN A 279 ? N GLN A 279 O ILE A 299 ? O ILE A 299 # loop_ _struct_site.id _struct_site.pdbx_evidence_code _struct_site.pdbx_auth_asym_id _struct_site.pdbx_auth_comp_id _struct_site.pdbx_auth_seq_id _struct_site.pdbx_auth_ins_code _struct_site.pdbx_num_residues _struct_site.details AC1 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE MPO B 1163' AC2 Software ? ? ? ? 1 'Binding site for Mono-Saccharide NAG A1011 bound to ASN A 11' AC3 Software ? ? ? ? 1 'Binding site for Poly-Saccharide residues NAG A1023 through NAG A1024 bound to ASN A 23' AC4 Software ? ? ? ? 5 'Binding site for Poly-Saccharide residues NAG A1165 through MAN A1169 bound to ASN A 165' AC5 Software ? ? ? ? 1 'Binding site for Mono-Saccharide NAG A1286 bound to ASN A 286' AC6 Software ? ? ? ? 3 'Binding site for Poly-Saccharide residues NAG B1154 through BMA B1156 bound to ASN B 154' AC7 Software ? ? ? ? 11 'Binding site for Poly-Saccharide residues SIA A1322 through GAL A1323' # loop_ _struct_site_gen.id _struct_site_gen.site_id _struct_site_gen.pdbx_num_res _struct_site_gen.label_comp_id _struct_site_gen.label_asym_id _struct_site_gen.label_seq_id _struct_site_gen.pdbx_auth_ins_code _struct_site_gen.auth_comp_id _struct_site_gen.auth_asym_id _struct_site_gen.auth_seq_id _struct_site_gen.label_atom_id _struct_site_gen.label_alt_id _struct_site_gen.symmetry _struct_site_gen.details 1 AC1 7 CYS A 4 ? CYS A 4 . ? 1_555 ? 2 AC1 7 TRP B 14 ? TRP B 14 . ? 1_555 ? 3 AC1 7 HIS B 25 ? HIS B 25 . ? 1_555 ? 4 AC1 7 TYR B 34 ? TYR B 34 . ? 1_555 ? 5 AC1 7 ASN B 135 ? ASN B 135 . ? 1_555 ? 6 AC1 7 CYS B 137 ? CYS B 137 . ? 1_555 ? 7 AC1 7 HOH S . ? HOH B 2046 . ? 1_555 ? 8 AC2 1 ASN A 11 ? ASN A 11 . ? 1_555 ? 9 AC3 1 ASN A 23 ? ASN A 23 . ? 1_555 ? 10 AC4 5 ARG A 107 ? ARG A 107 . ? 6_555 ? 11 AC4 5 ASN A 165 ? ASN A 165 . ? 1_555 ? 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 GLU B 78 ? GLU B 78 . ? 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 GLY A 221 ? GLY A 221 . ? 1_555 ? 28 AC7 11 GLN A 222 ? GLN A 222 . ? 1_555 ? 29 AC7 11 HOH R . ? HOH A 2035 . ? 1_555 ? # _database_PDB_matrix.entry_id 4CQQ _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 4CQQ _atom_sites.fract_transf_matrix[1][1] 0.009836 _atom_sites.fract_transf_matrix[1][2] 0.005679 _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] 0.011358 _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] 0.002210 _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 ? 37.109 -15.512 -83.841 1.00 68.28 ? 1 ASP A N 1 ATOM 2 C CA . ASP A 1 1 ? 36.292 -16.074 -82.729 1.00 68.39 ? 1 ASP A CA 1 ATOM 3 C C . ASP A 1 1 ? 37.179 -16.791 -81.730 1.00 66.41 ? 1 ASP A C 1 ATOM 4 O O . ASP A 1 1 ? 38.098 -17.513 -82.128 1.00 63.34 ? 1 ASP A O 1 ATOM 5 C CB . ASP A 1 1 ? 35.257 -17.066 -83.259 1.00 68.98 ? 1 ASP A CB 1 ATOM 6 C CG . ASP A 1 1 ? 34.274 -16.435 -84.208 1.00 71.12 ? 1 ASP A CG 1 ATOM 7 O OD1 . ASP A 1 1 ? 34.392 -15.227 -84.504 1.00 71.63 ? 1 ASP A OD1 1 ATOM 8 O OD2 . ASP A 1 1 ? 33.373 -17.164 -84.660 1.00 74.98 ? 1 ASP A OD2 1 ATOM 9 N N . GLN A 1 2 ? 36.892 -16.598 -80.442 1.00 66.22 ? 2 GLN A N 1 ATOM 10 C CA . GLN A 1 2 ? 37.652 -17.255 -79.392 1.00 63.85 ? 2 GLN A CA 1 ATOM 11 C C . GLN A 1 2 ? 36.869 -17.546 -78.133 1.00 61.89 ? 2 GLN A C 1 ATOM 12 O O . GLN A 1 2 ? 35.843 -16.917 -77.858 1.00 64.26 ? 2 GLN A O 1 ATOM 13 C CB . GLN A 1 2 ? 38.890 -16.442 -79.026 1.00 65.66 ? 2 GLN A CB 1 ATOM 14 C CG . GLN A 1 2 ? 38.650 -15.079 -78.415 1.00 68.86 ? 2 GLN A CG 1 ATOM 15 C CD . GLN A 1 2 ? 39.965 -14.368 -78.145 1.00 70.16 ? 2 GLN A CD 1 ATOM 16 O OE1 . GLN A 1 2 ? 40.275 -14.024 -77.010 1.00 70.57 ? 2 GLN A OE1 1 ATOM 17 N NE2 . GLN A 1 2 ? 40.759 -14.168 -79.198 1.00 71.45 ? 2 GLN A NE2 1 ATOM 18 N N . ILE A 1 3 ? 37.378 -18.521 -77.384 1.00 57.68 ? 3 ILE A N 1 ATOM 19 C CA . ILE A 1 3 ? 36.876 -18.843 -76.065 1.00 57.67 ? 3 ILE A CA 1 ATOM 20 C C . ILE A 1 3 ? 38.042 -18.789 -75.086 1.00 56.19 ? 3 ILE A C 1 ATOM 21 O O . ILE A 1 3 ? 39.156 -19.188 -75.419 1.00 55.24 ? 3 ILE A O 1 ATOM 22 C CB . ILE A 1 3 ? 36.155 -20.213 -76.040 1.00 58.74 ? 3 ILE A CB 1 ATOM 23 C CG1 . ILE A 1 3 ? 35.428 -20.412 -74.710 1.00 59.62 ? 3 ILE A CG1 1 ATOM 24 C CG2 . ILE A 1 3 ? 37.108 -21.374 -76.268 1.00 57.27 ? 3 ILE A CG2 1 ATOM 25 C CD1 . ILE A 1 3 ? 34.327 -21.445 -74.794 1.00 60.74 ? 3 ILE A CD1 1 ATOM 26 N N . CYS A 1 4 ? 37.782 -18.271 -73.891 1.00 56.17 ? 4 CYS A N 1 ATOM 27 C CA . CYS A 1 4 ? 38.816 -18.022 -72.906 1.00 54.64 ? 4 CYS A CA 1 ATOM 28 C C . CYS A 1 4 ? 38.407 -18.657 -71.594 1.00 54.13 ? 4 CYS A C 1 ATOM 29 O O . CYS A 1 4 ? 37.216 -18.674 -71.254 1.00 54.57 ? 4 CYS A O 1 ATOM 30 C CB . CYS A 1 4 ? 38.992 -16.514 -72.678 1.00 57.93 ? 4 CYS A CB 1 ATOM 31 S SG . CYS A 1 4 ? 39.489 -15.547 -74.127 1.00 64.82 ? 4 CYS A SG 1 ATOM 32 N N . ILE A 1 5 ? 39.394 -19.150 -70.848 1.00 50.16 ? 5 ILE A N 1 ATOM 33 C CA . ILE A 1 5 ? 39.171 -19.650 -69.501 1.00 48.28 ? 5 ILE A CA 1 ATOM 34 C C . ILE A 1 5 ? 39.668 -18.625 -68.500 1.00 48.03 ? 5 ILE A C 1 ATOM 35 O O . ILE A 1 5 ? 40.723 -18.031 -68.692 1.00 46.99 ? 5 ILE A O 1 ATOM 36 C CB . ILE A 1 5 ? 39.911 -20.970 -69.277 1.00 46.77 ? 5 ILE A CB 1 ATOM 37 C CG1 . ILE A 1 5 ? 39.449 -21.990 -70.302 1.00 49.26 ? 5 ILE A CG1 1 ATOM 38 C CG2 . ILE A 1 5 ? 39.701 -21.487 -67.862 1.00 45.82 ? 5 ILE A CG2 1 ATOM 39 C CD1 . ILE A 1 5 ? 37.981 -22.329 -70.196 1.00 52.11 ? 5 ILE A CD1 1 ATOM 40 N N . GLY A 1 6 ? 38.910 -18.432 -67.423 1.00 48.27 ? 6 GLY A N 1 ATOM 41 C CA . GLY A 1 6 ? 39.235 -17.404 -66.448 1.00 48.30 ? 6 GLY A CA 1 ATOM 42 C C . GLY A 1 6 ? 38.577 -17.630 -65.115 1.00 47.61 ? 6 GLY A C 1 ATOM 43 O O . GLY A 1 6 ? 37.922 -18.639 -64.904 1.00 49.12 ? 6 GLY A O 1 ATOM 44 N N . TYR A 1 7 ? 38.742 -16.669 -64.223 1.00 47.45 ? 7 TYR A N 1 ATOM 45 C CA . TYR A 1 7 ? 38.306 -16.823 -62.861 1.00 48.48 ? 7 TYR A CA 1 ATOM 46 C C . TYR A 1 7 ? 37.783 -15.504 -62.304 1.00 50.73 ? 7 TYR A C 1 ATOM 47 O O . TYR A 1 7 ? 37.976 -14.447 -62.894 1.00 51.60 ? 7 TYR A O 1 ATOM 48 C CB . TYR A 1 7 ? 39.460 -17.365 -62.011 1.00 48.00 ? 7 TYR A CB 1 ATOM 49 C CG . TYR A 1 7 ? 40.734 -16.546 -62.085 1.00 48.32 ? 7 TYR A CG 1 ATOM 50 C CD1 . TYR A 1 7 ? 41.681 -16.767 -63.073 1.00 48.01 ? 7 TYR A CD1 1 ATOM 51 C CD2 . TYR A 1 7 ? 40.986 -15.545 -61.157 1.00 50.87 ? 7 TYR A CD2 1 ATOM 52 C CE1 . TYR A 1 7 ? 42.834 -15.995 -63.140 1.00 49.61 ? 7 TYR A CE1 1 ATOM 53 C CE2 . TYR A 1 7 ? 42.137 -14.780 -61.210 1.00 49.95 ? 7 TYR A CE2 1 ATOM 54 C CZ . TYR A 1 7 ? 43.056 -15.005 -62.194 1.00 49.65 ? 7 TYR A CZ 1 ATOM 55 O OH . TYR A 1 7 ? 44.183 -14.216 -62.224 1.00 49.33 ? 7 TYR A OH 1 ATOM 56 N N . HIS A 1 8 ? 37.121 -15.600 -61.158 1.00 51.78 ? 8 HIS A N 1 ATOM 57 C CA . HIS A 1 8 ? 36.373 -14.506 -60.544 1.00 55.49 ? 8 HIS A CA 1 ATOM 58 C C . HIS A 1 8 ? 37.271 -13.432 -59.949 1.00 56.02 ? 8 HIS A C 1 ATOM 59 O O . HIS A 1 8 ? 38.334 -13.726 -59.404 1.00 56.71 ? 8 HIS A O 1 ATOM 60 C CB . HIS A 1 8 ? 35.499 -15.096 -59.423 1.00 55.51 ? 8 HIS A CB 1 ATOM 61 C CG . HIS A 1 8 ? 34.591 -14.111 -58.755 1.00 57.33 ? 8 HIS A CG 1 ATOM 62 N ND1 . HIS A 1 8 ? 33.559 -13.480 -59.416 1.00 60.75 ? 8 HIS A ND1 1 ATOM 63 C CD2 . HIS A 1 8 ? 34.526 -13.688 -57.469 1.00 57.20 ? 8 HIS A CD2 1 ATOM 64 C CE1 . HIS A 1 8 ? 32.913 -12.694 -58.572 1.00 60.75 ? 8 HIS A CE1 1 ATOM 65 N NE2 . HIS A 1 8 ? 33.479 -12.803 -57.384 1.00 58.39 ? 8 HIS A NE2 1 ATOM 66 N N . ALA A 1 9 ? 36.823 -12.185 -60.043 1.00 57.42 ? 9 ALA A N 1 ATOM 67 C CA . ALA A 1 9 ? 37.399 -11.087 -59.269 1.00 56.94 ? 9 ALA A CA 1 ATOM 68 C C . ALA A 1 9 ? 36.268 -10.209 -58.758 1.00 59.47 ? 9 ALA A C 1 ATOM 69 O O . ALA A 1 9 ? 35.178 -10.210 -59.319 1.00 63.26 ? 9 ALA A O 1 ATOM 70 C CB . ALA A 1 9 ? 38.355 -10.281 -60.120 1.00 56.28 ? 9 ALA A CB 1 ATOM 71 N N . ASN A 1 10 ? 36.519 -9.473 -57.689 1.00 59.42 ? 10 ASN A N 1 ATOM 72 C CA . ASN A 1 10 ? 35.536 -8.542 -57.173 1.00 63.58 ? 10 ASN A CA 1 ATOM 73 C C . ASN A 1 10 ? 36.196 -7.382 -56.436 1.00 67.42 ? 10 ASN A C 1 ATOM 74 O O . ASN A 1 10 ? 37.406 -7.256 -56.460 1.00 66.23 ? 10 ASN A O 1 ATOM 75 C CB . ASN A 1 10 ? 34.535 -9.282 -56.289 1.00 63.33 ? 10 ASN A CB 1 ATOM 76 C CG . ASN A 1 10 ? 35.157 -9.839 -55.032 1.00 61.92 ? 10 ASN A CG 1 ATOM 77 O OD1 . ASN A 1 10 ? 36.341 -9.643 -54.756 1.00 61.36 ? 10 ASN A OD1 1 ATOM 78 N ND2 . ASN A 1 10 ? 34.355 -10.551 -54.260 1.00 62.03 ? 10 ASN A ND2 1 ATOM 79 N N . ASN A 1 11 ? 35.404 -6.535 -55.787 1.00 76.63 ? 11 ASN A N 1 ATOM 80 C CA . ASN A 1 11 ? 35.938 -5.335 -55.137 1.00 83.60 ? 11 ASN A CA 1 ATOM 81 C C . ASN A 1 11 ? 36.433 -5.574 -53.699 1.00 79.37 ? 11 ASN A C 1 ATOM 82 O O . ASN A 1 11 ? 36.599 -4.627 -52.930 1.00 80.75 ? 11 ASN A O 1 ATOM 83 C CB . ASN A 1 11 ? 34.904 -4.191 -55.191 1.00 93.80 ? 11 ASN A CB 1 ATOM 84 C CG . ASN A 1 11 ? 33.600 -4.525 -54.474 1.00 106.42 ? 11 ASN A CG 1 ATOM 85 O OD1 . ASN A 1 11 ? 33.478 -5.572 -53.832 1.00 105.77 ? 11 ASN A OD1 1 ATOM 86 N ND2 . ASN A 1 11 ? 32.610 -3.623 -54.586 1.00 123.91 ? 11 ASN A ND2 1 ATOM 87 N N . SER A 1 12 ? 36.689 -6.835 -53.354 1.00 73.29 ? 12 SER A N 1 ATOM 88 C CA . SER A 1 12 ? 37.066 -7.218 -51.997 1.00 69.53 ? 12 SER A CA 1 ATOM 89 C C . SER A 1 12 ? 38.460 -6.724 -51.638 1.00 69.43 ? 12 SER A C 1 ATOM 90 O O . SER A 1 12 ? 39.368 -6.735 -52.474 1.00 66.98 ? 12 SER A O 1 ATOM 91 C CB . SER A 1 12 ? 37.018 -8.744 -51.837 1.00 66.92 ? 12 SER A CB 1 ATOM 92 O OG . SER A 1 12 ? 37.212 -9.133 -50.489 1.00 64.45 ? 12 SER A OG 1 ATOM 93 N N . THR A 1 13 ? 38.604 -6.289 -50.386 1.00 70.09 ? 13 THR A N 1 ATOM 94 C CA . THR A 1 13 ? 39.875 -5.841 -49.828 1.00 69.02 ? 13 THR A CA 1 ATOM 95 C C . THR A 1 13 ? 40.303 -6.730 -48.667 1.00 67.89 ? 13 THR A C 1 ATOM 96 O O . THR A 1 13 ? 41.348 -6.501 -48.066 1.00 66.76 ? 13 THR A O 1 ATOM 97 C CB . THR A 1 13 ? 39.769 -4.387 -49.321 1.00 73.25 ? 13 THR A CB 1 ATOM 98 O OG1 . THR A 1 13 ? 38.759 -4.297 -48.305 1.00 75.05 ? 13 THR A OG1 1 ATOM 99 C CG2 . THR A 1 13 ? 39.416 -3.440 -50.464 1.00 73.67 ? 13 THR A CG2 1 ATOM 100 N N . GLU A 1 14 ? 39.499 -7.741 -48.349 1.00 68.45 ? 14 GLU A N 1 ATOM 101 C CA . GLU A 1 14 ? 39.859 -8.715 -47.324 1.00 67.47 ? 14 GLU A CA 1 ATOM 102 C C . GLU A 1 14 ? 41.174 -9.418 -47.650 1.00 61.68 ? 14 GLU A C 1 ATOM 103 O O . GLU A 1 14 ? 41.428 -9.774 -48.798 1.00 61.48 ? 14 GLU A O 1 ATOM 104 C CB . GLU A 1 14 ? 38.756 -9.753 -47.164 1.00 73.39 ? 14 GLU A CB 1 ATOM 105 C CG . GLU A 1 14 ? 37.465 -9.191 -46.592 1.00 82.55 ? 14 GLU A CG 1 ATOM 106 C CD . GLU A 1 14 ? 37.016 -9.937 -45.349 1.00 91.61 ? 14 GLU A CD 1 ATOM 107 O OE1 . GLU A 1 14 ? 37.783 -9.943 -44.357 1.00 95.14 ? 14 GLU A OE1 1 ATOM 108 O OE2 . GLU A 1 14 ? 35.908 -10.525 -45.364 1.00 100.95 ? 14 GLU A OE2 1 ATOM 109 N N . GLN A 1 15 ? 41.995 -9.615 -46.624 1.00 58.60 ? 15 GLN A N 1 ATOM 110 C CA . GLN A 1 15 ? 43.340 -10.154 -46.769 1.00 55.53 ? 15 GLN A CA 1 ATOM 111 C C . GLN A 1 15 ? 43.555 -11.359 -45.862 1.00 52.36 ? 15 GLN A C 1 ATOM 112 O O . GLN A 1 15 ? 43.023 -11.411 -44.765 1.00 49.81 ? 15 GLN A O 1 ATOM 113 C CB . GLN A 1 15 ? 44.362 -9.095 -46.383 1.00 58.61 ? 15 GLN A CB 1 ATOM 114 C CG . GLN A 1 15 ? 44.301 -7.820 -47.198 1.00 63.14 ? 15 GLN A CG 1 ATOM 115 C CD . GLN A 1 15 ? 45.415 -6.856 -46.853 1.00 65.03 ? 15 GLN A CD 1 ATOM 116 O OE1 . GLN A 1 15 ? 45.893 -6.109 -47.705 1.00 67.32 ? 15 GLN A OE1 1 ATOM 117 N NE2 . GLN A 1 15 ? 45.834 -6.865 -45.596 1.00 66.46 ? 15 GLN A NE2 1 ATOM 118 N N . VAL A 1 16 ? 44.357 -12.314 -46.318 1.00 50.31 ? 16 VAL A N 1 ATOM 119 C CA . VAL A 1 16 ? 44.745 -13.455 -45.494 1.00 49.23 ? 16 VAL A CA 1 ATOM 120 C C . VAL A 1 16 ? 46.249 -13.599 -45.526 1.00 50.51 ? 16 VAL A C 1 ATOM 121 O O . VAL A 1 16 ? 46.900 -13.090 -46.441 1.00 50.53 ? 16 VAL A O 1 ATOM 122 C CB . VAL A 1 16 ? 44.095 -14.764 -45.978 1.00 47.76 ? 16 VAL A CB 1 ATOM 123 C CG1 . VAL A 1 16 ? 42.582 -14.622 -45.975 1.00 48.37 ? 16 VAL A CG1 1 ATOM 124 C CG2 . VAL A 1 16 ? 44.597 -15.156 -47.361 1.00 47.56 ? 16 VAL A CG2 1 ATOM 125 N N . ASP A 1 17 ? 46.793 -14.277 -44.517 1.00 52.02 ? 17 ASP A N 1 ATOM 126 C CA . ASP A 1 17 ? 48.222 -14.578 -44.457 1.00 52.35 ? 17 ASP A CA 1 ATOM 127 C C . ASP A 1 17 ? 48.476 -16.039 -44.820 1.00 51.97 ? 17 ASP A C 1 ATOM 128 O O . ASP A 1 17 ? 47.629 -16.904 -44.568 1.00 48.25 ? 17 ASP A O 1 ATOM 129 C CB . ASP A 1 17 ? 48.755 -14.317 -43.053 1.00 55.57 ? 17 ASP A CB 1 ATOM 130 C CG . ASP A 1 17 ? 48.871 -12.834 -42.726 1.00 60.08 ? 17 ASP A CG 1 ATOM 131 O OD1 . ASP A 1 17 ? 49.105 -12.022 -43.650 1.00 63.28 ? 17 ASP A OD1 1 ATOM 132 O OD2 . ASP A 1 17 ? 48.756 -12.484 -41.526 1.00 61.82 ? 17 ASP A OD2 1 ATOM 133 N N . THR A 1 18 ? 49.643 -16.295 -45.417 1.00 53.53 ? 18 THR A N 1 ATOM 134 C CA . THR A 1 18 ? 50.146 -17.656 -45.684 1.00 51.37 ? 18 THR A CA 1 ATOM 135 C C . THR A 1 18 ? 51.594 -17.746 -45.191 1.00 51.99 ? 18 THR A C 1 ATOM 136 O O . THR A 1 18 ? 52.144 -16.768 -44.701 1.00 56.16 ? 18 THR A O 1 ATOM 137 C CB . THR A 1 18 ? 50.085 -18.000 -47.196 1.00 51.91 ? 18 THR A CB 1 ATOM 138 O OG1 . THR A 1 18 ? 51.138 -17.329 -47.906 1.00 53.59 ? 18 THR A OG1 1 ATOM 139 C CG2 . THR A 1 18 ? 48.758 -17.582 -47.785 1.00 50.97 ? 18 THR A CG2 1 ATOM 140 N N . ILE A 1 19 ? 52.220 -18.907 -45.324 1.00 54.39 ? 19 ILE A N 1 ATOM 141 C CA . ILE A 1 19 ? 53.608 -19.093 -44.874 1.00 55.38 ? 19 ILE A CA 1 ATOM 142 C C . ILE A 1 19 ? 54.585 -18.242 -45.689 1.00 56.08 ? 19 ILE A C 1 ATOM 143 O O . ILE A 1 19 ? 55.534 -17.678 -45.147 1.00 57.66 ? 19 ILE A O 1 ATOM 144 C CB . ILE A 1 19 ? 54.026 -20.578 -44.997 1.00 59.93 ? 19 ILE A CB 1 ATOM 145 C CG1 . ILE A 1 19 ? 53.204 -21.469 -44.058 1.00 64.07 ? 19 ILE A CG1 1 ATOM 146 C CG2 . ILE A 1 19 ? 55.503 -20.770 -44.711 1.00 62.11 ? 19 ILE A CG2 1 ATOM 147 C CD1 . ILE A 1 19 ? 53.514 -21.299 -42.582 1.00 64.84 ? 19 ILE A CD1 1 ATOM 148 N N . MET A 1 20 ? 54.349 -18.155 -46.994 1.00 55.41 ? 20 MET A N 1 ATOM 149 C CA . MET A 1 20 ? 55.282 -17.498 -47.900 1.00 56.50 ? 20 MET A CA 1 ATOM 150 C C . MET A 1 20 ? 54.942 -16.048 -48.196 1.00 56.35 ? 20 MET A C 1 ATOM 151 O O . MET A 1 20 ? 55.777 -15.319 -48.735 1.00 54.05 ? 20 MET A O 1 ATOM 152 C CB . MET A 1 20 ? 55.338 -18.246 -49.225 1.00 58.80 ? 20 MET A CB 1 ATOM 153 C CG . MET A 1 20 ? 56.005 -19.603 -49.141 1.00 60.73 ? 20 MET A CG 1 ATOM 154 S SD . MET A 1 20 ? 56.494 -20.182 -50.768 1.00 65.13 ? 20 MET A SD 1 ATOM 155 C CE . MET A 1 20 ? 56.594 -21.951 -50.445 1.00 72.16 ? 20 MET A CE 1 ATOM 156 N N . GLU A 1 21 ? 53.719 -15.637 -47.878 1.00 55.06 ? 21 GLU A N 1 ATOM 157 C CA . GLU A 1 21 ? 53.267 -14.306 -48.228 1.00 56.03 ? 21 GLU A CA 1 ATOM 158 C C . GLU A 1 21 ? 52.218 -13.810 -47.248 1.00 56.70 ? 21 GLU A C 1 ATOM 159 O O . GLU A 1 21 ? 51.345 -14.568 -46.810 1.00 55.95 ? 21 GLU A O 1 ATOM 160 C CB . GLU A 1 21 ? 52.701 -14.311 -49.640 1.00 57.12 ? 21 GLU A CB 1 ATOM 161 C CG . GLU A 1 21 ? 52.546 -12.925 -50.237 1.00 61.12 ? 21 GLU A CG 1 ATOM 162 C CD . GLU A 1 21 ? 52.038 -12.950 -51.674 1.00 65.30 ? 21 GLU A CD 1 ATOM 163 O OE1 . GLU A 1 21 ? 51.911 -14.062 -52.251 1.00 62.66 ? 21 GLU A OE1 1 ATOM 164 O OE2 . GLU A 1 21 ? 51.771 -11.848 -52.221 1.00 65.19 ? 21 GLU A OE2 1 ATOM 165 N N . LYS A 1 22 ? 52.307 -12.528 -46.914 1.00 57.85 ? 22 LYS A N 1 ATOM 166 C CA . LYS A 1 22 ? 51.385 -11.922 -45.973 1.00 59.88 ? 22 LYS A CA 1 ATOM 167 C C . LYS A 1 22 ? 50.499 -10.920 -46.692 1.00 57.39 ? 22 LYS A C 1 ATOM 168 O O . LYS A 1 22 ? 50.856 -10.409 -47.746 1.00 55.95 ? 22 LYS A O 1 ATOM 169 C CB . LYS A 1 22 ? 52.171 -11.274 -44.839 1.00 65.50 ? 22 LYS A CB 1 ATOM 170 C CG . LYS A 1 22 ? 53.064 -12.275 -44.125 1.00 69.86 ? 22 LYS A CG 1 ATOM 171 C CD . LYS A 1 22 ? 53.744 -11.696 -42.895 1.00 78.20 ? 22 LYS A CD 1 ATOM 172 C CE . LYS A 1 22 ? 52.937 -11.939 -41.627 1.00 82.00 ? 22 LYS A CE 1 ATOM 173 N NZ . LYS A 1 22 ? 53.621 -11.408 -40.409 1.00 83.54 ? 22 LYS A NZ 1 ATOM 174 N N . ASN A 1 23 ? 49.319 -10.675 -46.144 1.00 57.62 ? 23 ASN A N 1 ATOM 175 C CA . ASN A 1 23 ? 48.418 -9.661 -46.687 1.00 59.92 ? 23 ASN A CA 1 ATOM 176 C C . ASN A 1 23 ? 48.087 -9.891 -48.157 1.00 57.35 ? 23 ASN A C 1 ATOM 177 O O . ASN A 1 23 ? 48.173 -8.979 -48.975 1.00 58.42 ? 23 ASN A O 1 ATOM 178 C CB . ASN A 1 23 ? 49.010 -8.256 -46.472 1.00 64.90 ? 23 ASN A CB 1 ATOM 179 C CG . ASN A 1 23 ? 49.144 -7.895 -45.007 1.00 70.72 ? 23 ASN A CG 1 ATOM 180 O OD1 . ASN A 1 23 ? 48.611 -8.588 -44.137 1.00 71.31 ? 23 ASN A OD1 1 ATOM 181 N ND2 . ASN A 1 23 ? 49.855 -6.802 -44.723 1.00 81.32 ? 23 ASN A ND2 1 ATOM 182 N N . VAL A 1 24 ? 47.705 -11.125 -48.471 1.00 56.46 ? 24 VAL A N 1 ATOM 183 C CA . VAL A 1 24 ? 47.216 -11.506 -49.796 1.00 54.01 ? 24 VAL A CA 1 ATOM 184 C C . VAL A 1 24 ? 45.728 -11.169 -49.894 1.00 54.36 ? 24 VAL A C 1 ATOM 185 O O . VAL A 1 24 ? 44.939 -11.660 -49.098 1.00 55.76 ? 24 VAL A O 1 ATOM 186 C CB . VAL A 1 24 ? 47.385 -13.020 -50.009 1.00 53.15 ? 24 VAL A CB 1 ATOM 187 C CG1 . VAL A 1 24 ? 46.810 -13.447 -51.352 1.00 54.20 ? 24 VAL A CG1 1 ATOM 188 C CG2 . VAL A 1 24 ? 48.852 -13.414 -49.893 1.00 52.33 ? 24 VAL A CG2 1 ATOM 189 N N . THR A 1 25 ? 45.340 -10.329 -50.848 1.00 53.50 ? 25 THR A N 1 ATOM 190 C CA . THR A 1 25 ? 43.932 -9.951 -50.994 1.00 53.67 ? 25 THR A CA 1 ATOM 191 C C . THR A 1 25 ? 43.151 -11.070 -51.660 1.00 53.30 ? 25 THR A C 1 ATOM 192 O O . THR A 1 25 ? 43.557 -11.566 -52.717 1.00 54.17 ? 25 THR A O 1 ATOM 193 C CB . THR A 1 25 ? 43.752 -8.699 -51.867 1.00 55.27 ? 25 THR A CB 1 ATOM 194 O OG1 . THR A 1 25 ? 44.600 -7.652 -51.392 1.00 59.14 ? 25 THR A OG1 1 ATOM 195 C CG2 . THR A 1 25 ? 42.323 -8.226 -51.822 1.00 56.98 ? 25 THR A CG2 1 ATOM 196 N N . VAL A 1 26 ? 42.023 -11.446 -51.061 1.00 52.61 ? 26 VAL A N 1 ATOM 197 C CA . VAL A 1 26 ? 41.178 -12.504 -51.604 1.00 51.28 ? 26 VAL A CA 1 ATOM 198 C C . VAL A 1 26 ? 39.753 -12.046 -51.856 1.00 52.90 ? 26 VAL A C 1 ATOM 199 O O . VAL A 1 26 ? 39.297 -11.073 -51.270 1.00 56.92 ? 26 VAL A O 1 ATOM 200 C CB . VAL A 1 26 ? 41.152 -13.731 -50.684 1.00 49.84 ? 26 VAL A CB 1 ATOM 201 C CG1 . VAL A 1 26 ? 42.545 -14.329 -50.588 1.00 49.08 ? 26 VAL A CG1 1 ATOM 202 C CG2 . VAL A 1 26 ? 40.612 -13.375 -49.307 1.00 50.39 ? 26 VAL A CG2 1 ATOM 203 N N . THR A 1 27 ? 39.057 -12.779 -52.722 1.00 52.40 ? 27 THR A N 1 ATOM 204 C CA . THR A 1 27 ? 37.695 -12.446 -53.130 1.00 52.78 ? 27 THR A CA 1 ATOM 205 C C . THR A 1 27 ? 36.699 -12.727 -52.031 1.00 53.69 ? 27 THR A C 1 ATOM 206 O O . THR A 1 27 ? 35.696 -12.026 -51.914 1.00 57.74 ? 27 THR A O 1 ATOM 207 C CB . THR A 1 27 ? 37.251 -13.247 -54.370 1.00 52.97 ? 27 THR A CB 1 ATOM 208 O OG1 . THR A 1 27 ? 37.216 -14.652 -54.070 1.00 50.52 ? 27 THR A OG1 1 ATOM 209 C CG2 . THR A 1 27 ? 38.189 -12.993 -55.536 1.00 52.40 ? 27 THR A CG2 1 ATOM 210 N N . HIS A 1 28 ? 36.958 -13.776 -51.252 1.00 52.47 ? 28 HIS A N 1 ATOM 211 C CA . HIS A 1 28 ? 36.143 -14.122 -50.079 1.00 51.51 ? 28 HIS A CA 1 ATOM 212 C C . HIS A 1 28 ? 36.992 -14.718 -48.970 1.00 51.75 ? 28 HIS A C 1 ATOM 213 O O . HIS A 1 28 ? 37.994 -15.388 -49.229 1.00 50.40 ? 28 HIS A O 1 ATOM 214 C CB . HIS A 1 28 ? 35.071 -15.136 -50.448 1.00 51.03 ? 28 HIS A CB 1 ATOM 215 C CG . HIS A 1 28 ? 34.275 -14.755 -51.648 1.00 52.58 ? 28 HIS A CG 1 ATOM 216 N ND1 . HIS A 1 28 ? 34.726 -14.970 -52.933 1.00 51.75 ? 28 HIS A ND1 1 ATOM 217 C CD2 . HIS A 1 28 ? 33.069 -14.153 -51.764 1.00 53.39 ? 28 HIS A CD2 1 ATOM 218 C CE1 . HIS A 1 28 ? 33.823 -14.528 -53.789 1.00 52.71 ? 28 HIS A CE1 1 ATOM 219 N NE2 . HIS A 1 28 ? 32.810 -14.027 -53.106 1.00 54.01 ? 28 HIS A NE2 1 ATOM 220 N N . ALA A 1 29 ? 36.552 -14.498 -47.738 1.00 54.22 ? 29 ALA A N 1 ATOM 221 C CA . ALA A 1 29 ? 37.267 -14.947 -46.546 1.00 54.32 ? 29 ALA A CA 1 ATOM 222 C C . ALA A 1 29 ? 36.280 -15.179 -45.410 1.00 55.38 ? 29 ALA A C 1 ATOM 223 O O . ALA A 1 29 ? 35.110 -14.832 -45.523 1.00 59.04 ? 29 ALA A O 1 ATOM 224 C CB . ALA A 1 29 ? 38.304 -13.919 -46.136 1.00 54.51 ? 29 ALA A CB 1 ATOM 225 N N . GLN A 1 30 ? 36.748 -15.784 -44.327 1.00 55.51 ? 30 GLN A N 1 ATOM 226 C CA . GLN A 1 30 ? 35.904 -16.024 -43.165 1.00 59.01 ? 30 GLN A CA 1 ATOM 227 C C . GLN A 1 30 ? 36.695 -15.806 -41.878 1.00 57.68 ? 30 GLN A C 1 ATOM 228 O O . GLN A 1 30 ? 37.631 -16.545 -41.580 1.00 56.39 ? 30 GLN A O 1 ATOM 229 C CB . GLN A 1 30 ? 35.320 -17.442 -43.200 1.00 60.52 ? 30 GLN A CB 1 ATOM 230 C CG . GLN A 1 30 ? 34.292 -17.710 -42.104 1.00 63.38 ? 30 GLN A CG 1 ATOM 231 C CD . GLN A 1 30 ? 33.575 -19.045 -42.258 1.00 65.49 ? 30 GLN A CD 1 ATOM 232 O OE1 . GLN A 1 30 ? 33.419 -19.569 -43.362 1.00 67.47 ? 30 GLN A OE1 1 ATOM 233 N NE2 . GLN A 1 30 ? 33.132 -19.597 -41.143 1.00 66.75 ? 30 GLN A NE2 1 ATOM 234 N N . ASP A 1 31 ? 36.319 -14.774 -41.137 1.00 58.94 ? 31 ASP A N 1 ATOM 235 C CA . ASP A 1 31 ? 36.853 -14.531 -39.807 1.00 60.62 ? 31 ASP A CA 1 ATOM 236 C C . ASP A 1 31 ? 36.318 -15.636 -38.892 1.00 60.14 ? 31 ASP A C 1 ATOM 237 O O . ASP A 1 31 ? 35.140 -15.996 -38.981 1.00 61.06 ? 31 ASP A O 1 ATOM 238 C CB . ASP A 1 31 ? 36.397 -13.154 -39.321 1.00 62.71 ? 31 ASP A CB 1 ATOM 239 C CG . ASP A 1 31 ? 37.097 -12.701 -38.055 1.00 65.09 ? 31 ASP A CG 1 ATOM 240 O OD1 . ASP A 1 31 ? 37.936 -13.440 -37.497 1.00 63.09 ? 31 ASP A OD1 1 ATOM 241 O OD2 . ASP A 1 31 ? 36.796 -11.573 -37.612 1.00 70.92 ? 31 ASP A OD2 1 ATOM 242 N N . ILE A 1 32 ? 37.182 -16.183 -38.037 1.00 56.77 ? 32 ILE A N 1 ATOM 243 C CA . ILE A 1 32 ? 36.768 -17.226 -37.088 1.00 56.72 ? 32 ILE A CA 1 ATOM 244 C C . ILE A 1 32 ? 37.099 -16.899 -35.619 1.00 57.43 ? 32 ILE A C 1 ATOM 245 O O . ILE A 1 32 ? 36.951 -17.753 -34.743 1.00 57.51 ? 32 ILE A O 1 ATOM 246 C CB . ILE A 1 32 ? 37.372 -18.597 -37.472 1.00 54.72 ? 32 ILE A CB 1 ATOM 247 C CG1 . ILE A 1 32 ? 38.897 -18.517 -37.576 1.00 53.55 ? 32 ILE A CG1 1 ATOM 248 C CG2 . ILE A 1 32 ? 36.801 -19.069 -38.795 1.00 54.67 ? 32 ILE A CG2 1 ATOM 249 C CD1 . ILE A 1 32 ? 39.570 -19.865 -37.670 1.00 51.74 ? 32 ILE A CD1 1 ATOM 250 N N . LEU A 1 33 ? 37.517 -15.663 -35.354 1.00 57.55 ? 33 LEU A N 1 ATOM 251 C CA . LEU A 1 33 ? 37.907 -15.234 -34.015 1.00 58.69 ? 33 LEU A CA 1 ATOM 252 C C . LEU A 1 33 ? 36.972 -14.149 -33.506 1.00 62.51 ? 33 LEU A C 1 ATOM 253 O O . LEU A 1 33 ? 36.860 -13.086 -34.117 1.00 63.66 ? 33 LEU A O 1 ATOM 254 C CB . LEU A 1 33 ? 39.330 -14.683 -34.041 1.00 57.53 ? 33 LEU A CB 1 ATOM 255 C CG . LEU A 1 33 ? 39.888 -14.184 -32.710 1.00 57.84 ? 33 LEU A CG 1 ATOM 256 C CD1 . LEU A 1 33 ? 40.099 -15.351 -31.757 1.00 57.97 ? 33 LEU A CD1 1 ATOM 257 C CD2 . LEU A 1 33 ? 41.188 -13.428 -32.934 1.00 58.21 ? 33 LEU A CD2 1 ATOM 258 N N . GLU A 1 34 ? 36.312 -14.409 -32.380 1.00 66.03 ? 34 GLU A N 1 ATOM 259 C CA . GLU A 1 34 ? 35.451 -13.405 -31.765 1.00 68.38 ? 34 GLU A CA 1 ATOM 260 C C . GLU A 1 34 ? 36.296 -12.443 -30.939 1.00 66.40 ? 34 GLU A C 1 ATOM 261 O O . GLU A 1 34 ? 36.987 -12.859 -30.015 1.00 65.16 ? 34 GLU A O 1 ATOM 262 C CB . GLU A 1 34 ? 34.377 -14.055 -30.890 1.00 69.75 ? 34 GLU A CB 1 ATOM 263 C CG . GLU A 1 34 ? 33.446 -13.053 -30.230 1.00 71.58 ? 34 GLU A CG 1 ATOM 264 C CD . GLU A 1 34 ? 32.893 -12.044 -31.216 1.00 74.54 ? 34 GLU A CD 1 ATOM 265 O OE1 . GLU A 1 34 ? 32.146 -12.455 -32.127 1.00 76.54 ? 34 GLU A OE1 1 ATOM 266 O OE2 . GLU A 1 34 ? 33.223 -10.847 -31.092 1.00 76.73 ? 34 GLU A OE2 1 ATOM 267 N N . LYS A 1 35 ? 36.224 -11.160 -31.277 1.00 67.30 ? 35 LYS A N 1 ATOM 268 C CA . LYS A 1 35 ? 37.062 -10.138 -30.656 1.00 68.58 ? 35 LYS A CA 1 ATOM 269 C C . LYS A 1 35 ? 36.304 -9.217 -29.688 1.00 71.20 ? 35 LYS A C 1 ATOM 270 O O . LYS A 1 35 ? 36.937 -8.509 -28.903 1.00 72.15 ? 35 LYS A O 1 ATOM 271 C CB . LYS A 1 35 ? 37.759 -9.306 -31.743 1.00 69.97 ? 35 LYS A CB 1 ATOM 272 C CG . LYS A 1 35 ? 39.019 -9.950 -32.307 1.00 69.78 ? 35 LYS A CG 1 ATOM 273 C CD . LYS A 1 35 ? 39.603 -9.159 -33.475 1.00 72.10 ? 35 LYS A CD 1 ATOM 274 C CE . LYS A 1 35 ? 39.418 -9.864 -34.819 1.00 73.95 ? 35 LYS A CE 1 ATOM 275 N NZ . LYS A 1 35 ? 38.001 -10.211 -35.147 1.00 74.36 ? 35 LYS A NZ 1 ATOM 276 N N . THR A 1 36 ? 34.970 -9.237 -29.725 1.00 71.12 ? 36 THR A N 1 ATOM 277 C CA . THR A 1 36 ? 34.171 -8.323 -28.912 1.00 74.44 ? 36 THR A CA 1 ATOM 278 C C . THR A 1 36 ? 33.424 -9.015 -27.776 1.00 75.26 ? 36 THR A C 1 ATOM 279 O O . THR A 1 36 ? 33.143 -10.211 -27.840 1.00 72.36 ? 36 THR A O 1 ATOM 280 C CB . THR A 1 36 ? 33.123 -7.571 -29.757 1.00 76.78 ? 36 THR A CB 1 ATOM 281 O OG1 . THR A 1 36 ? 32.068 -8.466 -30.126 1.00 78.45 ? 36 THR A OG1 1 ATOM 282 C CG2 . THR A 1 36 ? 33.752 -6.981 -31.006 1.00 76.90 ? 36 THR A CG2 1 ATOM 283 N N . HIS A 1 37 ? 33.110 -8.222 -26.749 1.00 76.79 ? 37 HIS A N 1 ATOM 284 C CA . HIS A 1 37 ? 32.260 -8.617 -25.625 1.00 77.30 ? 37 HIS A CA 1 ATOM 285 C C . HIS A 1 37 ? 31.400 -7.406 -25.230 1.00 81.26 ? 37 HIS A C 1 ATOM 286 O O . HIS A 1 37 ? 31.647 -6.297 -25.704 1.00 83.17 ? 37 HIS A O 1 ATOM 287 C CB . HIS A 1 37 ? 33.113 -9.087 -24.440 1.00 74.82 ? 37 HIS A CB 1 ATOM 288 C CG . HIS A 1 37 ? 34.072 -8.057 -23.926 1.00 75.23 ? 37 HIS A CG 1 ATOM 289 N ND1 . HIS A 1 37 ? 33.769 -7.217 -22.877 1.00 76.95 ? 37 HIS A ND1 1 ATOM 290 C CD2 . HIS A 1 37 ? 35.333 -7.738 -24.306 1.00 74.89 ? 37 HIS A CD2 1 ATOM 291 C CE1 . HIS A 1 37 ? 34.796 -6.424 -22.631 1.00 76.64 ? 37 HIS A CE1 1 ATOM 292 N NE2 . HIS A 1 37 ? 35.761 -6.722 -23.483 1.00 76.01 ? 37 HIS A NE2 1 ATOM 293 N N . ASN A 1 38 ? 30.399 -7.610 -24.375 1.00 83.40 ? 38 ASN A N 1 ATOM 294 C CA . ASN A 1 38 ? 29.487 -6.519 -23.981 1.00 86.66 ? 38 ASN A CA 1 ATOM 295 C C . ASN A 1 38 ? 29.935 -5.737 -22.734 1.00 88.27 ? 38 ASN A C 1 ATOM 296 O O . ASN A 1 38 ? 29.381 -4.683 -22.425 1.00 90.58 ? 38 ASN A O 1 ATOM 297 C CB . ASN A 1 38 ? 28.046 -7.036 -23.808 1.00 86.92 ? 38 ASN A CB 1 ATOM 298 C CG . ASN A 1 38 ? 27.857 -7.876 -22.556 1.00 86.05 ? 38 ASN A CG 1 ATOM 299 O OD1 . ASN A 1 38 ? 28.798 -8.119 -21.797 1.00 85.72 ? 38 ASN A OD1 1 ATOM 300 N ND2 . ASN A 1 38 ? 26.630 -8.328 -22.338 1.00 85.74 ? 38 ASN A ND2 1 ATOM 301 N N . GLY A 1 39 ? 30.905 -6.278 -22.003 1.00 86.96 ? 39 GLY A N 1 ATOM 302 C CA . GLY A 1 39 ? 31.567 -5.548 -20.915 1.00 87.50 ? 39 GLY A CA 1 ATOM 303 C C . GLY A 1 39 ? 30.821 -5.592 -19.596 1.00 88.88 ? 39 GLY A C 1 ATOM 304 O O . GLY A 1 39 ? 31.058 -4.759 -18.716 1.00 87.85 ? 39 GLY A O 1 ATOM 305 N N . LYS A 1 40 ? 29.936 -6.580 -19.459 1.00 89.56 ? 40 LYS A N 1 ATOM 306 C CA . LYS A 1 40 ? 29.037 -6.684 -18.320 1.00 90.42 ? 40 LYS A CA 1 ATOM 307 C C . LYS A 1 40 ? 29.052 -8.077 -17.703 1.00 89.43 ? 40 LYS A C 1 ATOM 308 O O . LYS A 1 40 ? 29.372 -9.059 -18.368 1.00 90.03 ? 40 LYS A O 1 ATOM 309 C CB . LYS A 1 40 ? 27.619 -6.346 -18.772 1.00 93.70 ? 40 LYS A CB 1 ATOM 310 C CG . LYS A 1 40 ? 27.468 -4.916 -19.257 1.00 97.10 ? 40 LYS A CG 1 ATOM 311 C CD . LYS A 1 40 ? 26.075 -4.613 -19.784 1.00 99.27 ? 40 LYS A CD 1 ATOM 312 C CE . LYS A 1 40 ? 26.082 -3.312 -20.575 1.00 102.17 ? 40 LYS A CE 1 ATOM 313 N NZ . LYS A 1 40 ? 24.733 -2.693 -20.701 1.00 107.79 ? 40 LYS A NZ 1 ATOM 314 N N . LEU A 1 41 ? 28.708 -8.150 -16.423 1.00 91.87 ? 41 LEU A N 1 ATOM 315 C CA . LEU A 1 41 ? 28.414 -9.423 -15.772 1.00 92.04 ? 41 LEU A CA 1 ATOM 316 C C . LEU A 1 41 ? 26.920 -9.692 -15.940 1.00 91.02 ? 41 LEU A C 1 ATOM 317 O O . LEU A 1 41 ? 26.101 -8.796 -15.736 1.00 92.18 ? 41 LEU A O 1 ATOM 318 C CB . LEU A 1 41 ? 28.797 -9.365 -14.295 1.00 94.18 ? 41 LEU A CB 1 ATOM 319 C CG . LEU A 1 41 ? 30.264 -9.000 -14.047 1.00 95.51 ? 41 LEU A CG 1 ATOM 320 C CD1 . LEU A 1 41 ? 30.505 -8.755 -12.565 1.00 96.62 ? 41 LEU A CD1 1 ATOM 321 C CD2 . LEU A 1 41 ? 31.206 -10.073 -14.587 1.00 92.51 ? 41 LEU A CD2 1 ATOM 322 N N . CYS A 1 42 ? 26.568 -10.914 -16.326 1.00 88.31 ? 42 CYS A N 1 ATOM 323 C CA . CYS A 1 42 ? 25.201 -11.214 -16.750 1.00 90.91 ? 42 CYS A CA 1 ATOM 324 C C . CYS A 1 42 ? 24.702 -12.535 -16.215 1.00 88.19 ? 42 CYS A C 1 ATOM 325 O O . CYS A 1 42 ? 25.486 -13.385 -15.804 1.00 84.49 ? 42 CYS A O 1 ATOM 326 C CB . CYS A 1 42 ? 25.127 -11.268 -18.280 1.00 93.60 ? 42 CYS A CB 1 ATOM 327 S SG . CYS A 1 42 ? 25.671 -9.764 -19.115 1.00 94.40 ? 42 CYS A SG 1 ATOM 328 N N . ASP A 1 43 ? 23.384 -12.703 -16.252 1.00 90.39 ? 43 ASP A N 1 ATOM 329 C CA . ASP A 1 43 ? 22.761 -13.984 -15.942 1.00 90.48 ? 43 ASP A CA 1 ATOM 330 C C . ASP A 1 43 ? 23.262 -15.021 -16.931 1.00 87.84 ? 43 ASP A C 1 ATOM 331 O O . ASP A 1 43 ? 23.320 -14.763 -18.132 1.00 86.68 ? 43 ASP A O 1 ATOM 332 C CB . ASP A 1 43 ? 21.230 -13.906 -16.041 1.00 93.98 ? 43 ASP A CB 1 ATOM 333 C CG . ASP A 1 43 ? 20.615 -12.927 -15.053 1.00 95.60 ? 43 ASP A CG 1 ATOM 334 O OD1 . ASP A 1 43 ? 21.302 -12.498 -14.107 1.00 94.47 ? 43 ASP A OD1 1 ATOM 335 O OD2 . ASP A 1 43 ? 19.431 -12.580 -15.231 1.00 98.86 ? 43 ASP A OD2 1 ATOM 336 N N . LEU A 1 44 ? 23.638 -16.183 -16.416 1.00 88.46 ? 44 LEU A N 1 ATOM 337 C CA . LEU A 1 44 ? 24.045 -17.298 -17.253 1.00 89.18 ? 44 LEU A CA 1 ATOM 338 C C . LEU A 1 44 ? 22.849 -18.217 -17.469 1.00 93.97 ? 44 LEU A C 1 ATOM 339 O O . LEU A 1 44 ? 22.458 -18.973 -16.576 1.00 94.74 ? 44 LEU A O 1 ATOM 340 C CB . LEU A 1 44 ? 25.199 -18.065 -16.600 1.00 86.97 ? 44 LEU A CB 1 ATOM 341 C CG . LEU A 1 44 ? 25.699 -19.332 -17.308 1.00 87.55 ? 44 LEU A CG 1 ATOM 342 C CD1 . LEU A 1 44 ? 26.232 -19.012 -18.698 1.00 87.88 ? 44 LEU A CD1 1 ATOM 343 C CD2 . LEU A 1 44 ? 26.771 -20.031 -16.485 1.00 85.16 ? 44 LEU A CD2 1 ATOM 344 N N . ASP A 1 45 ? 22.259 -18.137 -18.657 1.00 99.70 ? 45 ASP A N 1 ATOM 345 C CA . ASP A 1 45 ? 21.190 -19.049 -19.050 1.00 105.26 ? 45 ASP A CA 1 ATOM 346 C C . ASP A 1 45 ? 19.944 -18.835 -18.188 1.00 105.44 ? 45 ASP A C 1 ATOM 347 O O . ASP A 1 45 ? 19.261 -19.791 -17.820 1.00 104.18 ? 45 ASP A O 1 ATOM 348 C CB . ASP A 1 45 ? 21.688 -20.498 -18.938 1.00 108.65 ? 45 ASP A CB 1 ATOM 349 C CG . ASP A 1 45 ? 21.051 -21.410 -19.950 1.00 114.39 ? 45 ASP A CG 1 ATOM 350 O OD1 . ASP A 1 45 ? 21.518 -21.416 -21.113 1.00 119.62 ? 45 ASP A OD1 1 ATOM 351 O OD2 . ASP A 1 45 ? 20.098 -22.127 -19.579 1.00 119.66 ? 45 ASP A OD2 1 ATOM 352 N N . GLY A 1 46 ? 19.668 -17.570 -17.864 1.00 105.39 ? 46 GLY A N 1 ATOM 353 C CA . GLY A 1 46 ? 18.559 -17.196 -16.982 1.00 105.47 ? 46 GLY A CA 1 ATOM 354 C C . GLY A 1 46 ? 18.954 -17.061 -15.520 1.00 104.42 ? 46 GLY A C 1 ATOM 355 O O . GLY A 1 46 ? 18.440 -16.190 -14.817 1.00 104.63 ? 46 GLY A O 1 ATOM 356 N N . VAL A 1 47 ? 19.876 -17.916 -15.071 1.00 100.99 ? 47 VAL A N 1 ATOM 357 C CA . VAL A 1 47 ? 20.262 -18.015 -13.661 1.00 98.10 ? 47 VAL A CA 1 ATOM 358 C C . VAL A 1 47 ? 21.307 -16.964 -13.279 1.00 96.06 ? 47 VAL A C 1 ATOM 359 O O . VAL A 1 47 ? 22.450 -17.026 -13.728 1.00 95.74 ? 47 VAL A O 1 ATOM 360 C CB . VAL A 1 47 ? 20.834 -19.413 -13.352 1.00 95.73 ? 47 VAL A CB 1 ATOM 361 C CG1 . VAL A 1 47 ? 21.250 -19.514 -11.889 1.00 96.77 ? 47 VAL A CG1 1 ATOM 362 C CG2 . VAL A 1 47 ? 19.819 -20.491 -13.703 1.00 96.72 ? 47 VAL A CG2 1 ATOM 363 N N . LYS A 1 48 ? 20.912 -16.023 -12.428 1.00 97.06 ? 48 LYS A N 1 ATOM 364 C CA . LYS A 1 48 ? 21.772 -14.913 -12.008 1.00 96.86 ? 48 LYS A CA 1 ATOM 365 C C . LYS A 1 48 ? 22.942 -15.375 -11.130 1.00 93.74 ? 48 LYS A C 1 ATOM 366 O O . LYS A 1 48 ? 22.800 -16.319 -10.350 1.00 93.60 ? 48 LYS A O 1 ATOM 367 C CB . LYS A 1 48 ? 20.931 -13.876 -11.243 1.00 100.98 ? 48 LYS A CB 1 ATOM 368 C CG . LYS A 1 48 ? 21.669 -12.601 -10.860 1.00 101.85 ? 48 LYS A CG 1 ATOM 369 C CD . LYS A 1 48 ? 20.843 -11.683 -9.977 1.00 105.84 ? 48 LYS A CD 1 ATOM 370 C CE . LYS A 1 48 ? 21.708 -10.561 -9.426 1.00 105.87 ? 48 LYS A CE 1 ATOM 371 N NZ . LYS A 1 48 ? 20.907 -9.495 -8.768 1.00 111.10 ? 48 LYS A NZ 1 ATOM 372 N N . PRO A 1 49 ? 24.107 -14.705 -11.251 1.00 91.41 ? 49 PRO A N 1 ATOM 373 C CA . PRO A 1 49 ? 25.242 -15.054 -10.395 1.00 88.23 ? 49 PRO A CA 1 ATOM 374 C C . PRO A 1 49 ? 25.140 -14.465 -8.999 1.00 86.78 ? 49 PRO A C 1 ATOM 375 O O . PRO A 1 49 ? 24.401 -13.506 -8.787 1.00 87.30 ? 49 PRO A O 1 ATOM 376 C CB . PRO A 1 49 ? 26.428 -14.413 -11.117 1.00 85.20 ? 49 PRO A CB 1 ATOM 377 C CG . PRO A 1 49 ? 25.835 -13.216 -11.775 1.00 87.36 ? 49 PRO A CG 1 ATOM 378 C CD . PRO A 1 49 ? 24.483 -13.679 -12.246 1.00 90.05 ? 49 PRO A CD 1 ATOM 379 N N . LEU A 1 50 ? 25.900 -15.036 -8.069 1.00 84.17 ? 50 LEU A N 1 ATOM 380 C CA . LEU A 1 50 ? 26.079 -14.454 -6.747 1.00 83.94 ? 50 LEU A CA 1 ATOM 381 C C . LEU A 1 50 ? 27.161 -13.390 -6.839 1.00 83.42 ? 50 LEU A C 1 ATOM 382 O O . LEU A 1 50 ? 28.331 -13.706 -7.065 1.00 81.90 ? 50 LEU A O 1 ATOM 383 C CB . LEU A 1 50 ? 26.482 -15.528 -5.735 1.00 82.78 ? 50 LEU A CB 1 ATOM 384 C CG . LEU A 1 50 ? 26.771 -15.084 -4.297 1.00 82.89 ? 50 LEU A CG 1 ATOM 385 C CD1 . LEU A 1 50 ? 25.597 -14.332 -3.695 1.00 85.38 ? 50 LEU A CD1 1 ATOM 386 C CD2 . LEU A 1 50 ? 27.122 -16.287 -3.435 1.00 83.10 ? 50 LEU A CD2 1 ATOM 387 N N . ILE A 1 51 ? 26.769 -12.130 -6.681 1.00 85.52 ? 51 ILE A N 1 ATOM 388 C CA . ILE A 1 51 ? 27.715 -11.020 -6.753 1.00 86.06 ? 51 ILE A CA 1 ATOM 389 C C . ILE A 1 51 ? 28.010 -10.520 -5.342 1.00 86.62 ? 51 ILE A C 1 ATOM 390 O O . ILE A 1 51 ? 27.242 -9.746 -4.764 1.00 87.39 ? 51 ILE A O 1 ATOM 391 C CB . ILE A 1 51 ? 27.194 -9.899 -7.677 1.00 88.02 ? 51 ILE A CB 1 ATOM 392 C CG1 . ILE A 1 51 ? 27.029 -10.470 -9.091 1.00 89.58 ? 51 ILE A CG1 1 ATOM 393 C CG2 . ILE A 1 51 ? 28.140 -8.700 -7.678 1.00 87.48 ? 51 ILE A CG2 1 ATOM 394 C CD1 . ILE A 1 51 ? 26.716 -9.449 -10.162 1.00 92.75 ? 51 ILE A CD1 1 ATOM 395 N N . LEU A 1 52 ? 29.141 -10.970 -4.803 1.00 84.91 ? 52 LEU A N 1 ATOM 396 C CA . LEU A 1 52 ? 29.508 -10.701 -3.413 1.00 85.27 ? 52 LEU A CA 1 ATOM 397 C C . LEU A 1 52 ? 29.844 -9.237 -3.144 1.00 87.23 ? 52 LEU A C 1 ATOM 398 O O . LEU A 1 52 ? 29.897 -8.827 -1.984 1.00 88.36 ? 52 LEU A O 1 ATOM 399 C CB . LEU A 1 52 ? 30.687 -11.585 -2.992 1.00 81.85 ? 52 LEU A CB 1 ATOM 400 C CG . LEU A 1 52 ? 30.431 -13.096 -3.010 1.00 81.03 ? 52 LEU A CG 1 ATOM 401 C CD1 . LEU A 1 52 ? 31.706 -13.860 -2.689 1.00 79.33 ? 52 LEU A CD1 1 ATOM 402 C CD2 . LEU A 1 52 ? 29.314 -13.488 -2.050 1.00 83.30 ? 52 LEU A CD2 1 ATOM 403 N N . ARG A 1 53 ? 30.083 -8.466 -4.204 1.00 88.32 ? 53 ARG A N 1 ATOM 404 C CA . ARG A 1 53 ? 30.310 -7.029 -4.094 1.00 93.19 ? 53 ARG A CA 1 ATOM 405 C C . ARG A 1 53 ? 31.574 -6.749 -3.260 1.00 94.41 ? 53 ARG A C 1 ATOM 406 O O . ARG A 1 53 ? 32.663 -7.148 -3.664 1.00 94.84 ? 53 ARG A O 1 ATOM 407 C CB . ARG A 1 53 ? 29.057 -6.348 -3.533 1.00 98.55 ? 53 ARG A CB 1 ATOM 408 C CG . ARG A 1 53 ? 28.950 -4.863 -3.843 1.00 103.04 ? 53 ARG A CG 1 ATOM 409 C CD . ARG A 1 53 ? 27.880 -4.191 -2.993 1.00 108.71 ? 53 ARG A CD 1 ATOM 410 N NE . ARG A 1 53 ? 26.905 -3.478 -3.815 1.00 111.83 ? 53 ARG A NE 1 ATOM 411 C CZ . ARG A 1 53 ? 25.903 -4.056 -4.477 1.00 113.53 ? 53 ARG A CZ 1 ATOM 412 N NH1 . ARG A 1 53 ? 25.720 -5.373 -4.435 1.00 112.49 ? 53 ARG A NH1 1 ATOM 413 N NH2 . ARG A 1 53 ? 25.073 -3.309 -5.194 1.00 117.08 ? 53 ARG A NH2 1 ATOM 414 N N . ASP A 1 54 ? 31.445 -6.088 -2.110 1.00 96.44 ? 54 ASP A N 1 ATOM 415 C CA . ASP A 1 54 ? 32.593 -5.823 -1.240 1.00 96.13 ? 54 ASP A CA 1 ATOM 416 C C . ASP A 1 54 ? 32.882 -6.949 -0.243 1.00 94.53 ? 54 ASP A C 1 ATOM 417 O O . ASP A 1 54 ? 33.885 -6.890 0.465 1.00 95.19 ? 54 ASP A O 1 ATOM 418 C CB . ASP A 1 54 ? 32.384 -4.515 -0.466 1.00 99.26 ? 54 ASP A CB 1 ATOM 419 C CG . ASP A 1 54 ? 32.341 -3.297 -1.369 1.00 100.21 ? 54 ASP A CG 1 ATOM 420 O OD1 . ASP A 1 54 ? 33.080 -3.270 -2.379 1.00 97.16 ? 54 ASP A OD1 1 ATOM 421 O OD2 . ASP A 1 54 ? 31.572 -2.359 -1.054 1.00 102.16 ? 54 ASP A OD2 1 ATOM 422 N N . CYS A 1 55 ? 32.014 -7.959 -0.171 1.00 94.33 ? 55 CYS A N 1 ATOM 423 C CA . CYS A 1 55 ? 32.223 -9.088 0.748 1.00 94.61 ? 55 CYS A CA 1 ATOM 424 C C . CYS A 1 55 ? 33.089 -10.175 0.107 1.00 89.93 ? 55 CYS A C 1 ATOM 425 O O . CYS A 1 55 ? 33.223 -10.235 -1.109 1.00 89.18 ? 55 CYS A O 1 ATOM 426 C CB . CYS A 1 55 ? 30.885 -9.686 1.215 1.00 95.97 ? 55 CYS A CB 1 ATOM 427 S SG . CYS A 1 55 ? 29.873 -8.560 2.210 1.00 103.49 ? 55 CYS A SG 1 ATOM 428 N N . SER A 1 56 ? 33.679 -11.021 0.944 1.00 87.61 ? 56 SER A N 1 ATOM 429 C CA . SER A 1 56 ? 34.437 -12.177 0.485 1.00 85.15 ? 56 SER A CA 1 ATOM 430 C C . SER A 1 56 ? 33.677 -13.449 0.833 1.00 84.72 ? 56 SER A C 1 ATOM 431 O O . SER A 1 56 ? 32.681 -13.413 1.551 1.00 84.72 ? 56 SER A O 1 ATOM 432 C CB . SER A 1 56 ? 35.807 -12.214 1.156 1.00 85.20 ? 56 SER A CB 1 ATOM 433 O OG . SER A 1 56 ? 35.687 -12.608 2.514 1.00 86.68 ? 56 SER A OG 1 ATOM 434 N N . VAL A 1 57 ? 34.172 -14.579 0.342 1.00 83.44 ? 57 VAL A N 1 ATOM 435 C CA . VAL A 1 57 ? 33.528 -15.867 0.595 1.00 82.64 ? 57 VAL A CA 1 ATOM 436 C C . VAL A 1 57 ? 33.500 -16.150 2.104 1.00 83.21 ? 57 VAL A C 1 ATOM 437 O O . VAL A 1 57 ? 32.535 -16.717 2.618 1.00 82.44 ? 57 VAL A O 1 ATOM 438 C CB . VAL A 1 57 ? 34.228 -17.005 -0.187 1.00 79.47 ? 57 VAL A CB 1 ATOM 439 C CG1 . VAL A 1 57 ? 33.645 -18.364 0.169 1.00 79.50 ? 57 VAL A CG1 1 ATOM 440 C CG2 . VAL A 1 57 ? 34.109 -16.760 -1.685 1.00 79.60 ? 57 VAL A CG2 1 ATOM 441 N N . ALA A 1 58 ? 34.551 -15.728 2.804 1.00 83.26 ? 58 ALA A N 1 ATOM 442 C CA . ALA A 1 58 ? 34.623 -15.853 4.260 1.00 84.68 ? 58 ALA A CA 1 ATOM 443 C C . ALA A 1 58 ? 33.605 -14.948 4.970 1.00 85.93 ? 58 ALA A C 1 ATOM 444 O O . ALA A 1 58 ? 32.786 -15.427 5.763 1.00 87.07 ? 58 ALA A O 1 ATOM 445 C CB . ALA A 1 58 ? 36.030 -15.541 4.740 1.00 83.62 ? 58 ALA A CB 1 ATOM 446 N N . GLY A 1 59 ? 33.657 -13.648 4.682 1.00 84.37 ? 59 GLY A N 1 ATOM 447 C CA . GLY A 1 59 ? 32.694 -12.695 5.231 1.00 84.45 ? 59 GLY A CA 1 ATOM 448 C C . GLY A 1 59 ? 31.262 -13.157 5.009 1.00 86.63 ? 59 GLY A C 1 ATOM 449 O O . GLY A 1 59 ? 30.409 -13.000 5.879 1.00 90.65 ? 59 GLY A O 1 ATOM 450 N N . TRP A 1 60 ? 31.002 -13.741 3.842 1.00 84.45 ? 60 TRP A N 1 ATOM 451 C CA . TRP A 1 60 ? 29.683 -14.267 3.516 1.00 84.27 ? 60 TRP A CA 1 ATOM 452 C C . TRP A 1 60 ? 29.331 -15.469 4.390 1.00 85.22 ? 60 TRP A C 1 ATOM 453 O O . TRP A 1 60 ? 28.319 -15.460 5.096 1.00 87.41 ? 60 TRP A O 1 ATOM 454 C CB . TRP A 1 60 ? 29.621 -14.635 2.026 1.00 83.71 ? 60 TRP A CB 1 ATOM 455 C CG . TRP A 1 60 ? 28.487 -15.542 1.637 1.00 84.14 ? 60 TRP A CG 1 ATOM 456 C CD1 . TRP A 1 60 ? 27.207 -15.503 2.100 1.00 86.59 ? 60 TRP A CD1 1 ATOM 457 C CD2 . TRP A 1 60 ? 28.535 -16.606 0.681 1.00 82.20 ? 60 TRP A CD2 1 ATOM 458 N NE1 . TRP A 1 60 ? 26.459 -16.487 1.503 1.00 87.09 ? 60 TRP A NE1 1 ATOM 459 C CE2 . TRP A 1 60 ? 27.252 -17.178 0.628 1.00 84.13 ? 60 TRP A CE2 1 ATOM 460 C CE3 . TRP A 1 60 ? 29.540 -17.131 -0.135 1.00 80.38 ? 60 TRP A CE3 1 ATOM 461 C CZ2 . TRP A 1 60 ? 26.947 -18.252 -0.204 1.00 84.74 ? 60 TRP A CZ2 1 ATOM 462 C CZ3 . TRP A 1 60 ? 29.237 -18.201 -0.962 1.00 79.68 ? 60 TRP A CZ3 1 ATOM 463 C CH2 . TRP A 1 60 ? 27.953 -18.749 -0.991 1.00 81.94 ? 60 TRP A CH2 1 ATOM 464 N N . LEU A 1 61 ? 30.176 -16.494 4.352 1.00 84.05 ? 61 LEU A N 1 ATOM 465 C CA . LEU A 1 61 ? 29.858 -17.772 4.994 1.00 84.57 ? 61 LEU A CA 1 ATOM 466 C C . LEU A 1 61 ? 29.815 -17.688 6.515 1.00 86.25 ? 61 LEU A C 1 ATOM 467 O O . LEU A 1 61 ? 28.888 -18.203 7.144 1.00 87.19 ? 61 LEU A O 1 ATOM 468 C CB . LEU A 1 61 ? 30.841 -18.858 4.553 1.00 82.16 ? 61 LEU A CB 1 ATOM 469 C CG . LEU A 1 61 ? 30.680 -19.323 3.104 1.00 81.06 ? 61 LEU A CG 1 ATOM 470 C CD1 . LEU A 1 61 ? 31.704 -20.404 2.788 1.00 80.48 ? 61 LEU A CD1 1 ATOM 471 C CD2 . LEU A 1 61 ? 29.270 -19.825 2.829 1.00 82.01 ? 61 LEU A CD2 1 ATOM 472 N N . LEU A 1 62 ? 30.812 -17.035 7.101 1.00 85.97 ? 62 LEU A N 1 ATOM 473 C CA . LEU A 1 62 ? 30.823 -16.787 8.543 1.00 86.23 ? 62 LEU A CA 1 ATOM 474 C C . LEU A 1 62 ? 29.706 -15.833 8.969 1.00 88.90 ? 62 LEU A C 1 ATOM 475 O O . LEU A 1 62 ? 29.265 -15.872 10.117 1.00 91.40 ? 62 LEU A O 1 ATOM 476 C CB . LEU A 1 62 ? 32.174 -16.226 8.975 1.00 83.97 ? 62 LEU A CB 1 ATOM 477 C CG . LEU A 1 62 ? 33.333 -17.206 8.811 1.00 81.59 ? 62 LEU A CG 1 ATOM 478 C CD1 . LEU A 1 62 ? 34.652 -16.460 8.843 1.00 80.97 ? 62 LEU A CD1 1 ATOM 479 C CD2 . LEU A 1 62 ? 33.297 -18.283 9.886 1.00 82.53 ? 62 LEU A CD2 1 ATOM 480 N N . GLY A 1 63 ? 29.253 -14.984 8.048 1.00 88.98 ? 63 GLY A N 1 ATOM 481 C CA . GLY A 1 63 ? 28.180 -14.033 8.333 1.00 91.63 ? 63 GLY A CA 1 ATOM 482 C C . GLY A 1 63 ? 28.671 -12.734 8.955 1.00 91.61 ? 63 GLY A C 1 ATOM 483 O O . GLY A 1 63 ? 28.140 -12.292 9.969 1.00 92.70 ? 63 GLY A O 1 ATOM 484 N N . ASN A 1 64 ? 29.695 -12.133 8.349 1.00 89.77 ? 64 ASN A N 1 ATOM 485 C CA . ASN A 1 64 ? 30.130 -10.783 8.689 1.00 89.68 ? 64 ASN A CA 1 ATOM 486 C C . ASN A 1 64 ? 28.907 -9.874 8.660 1.00 93.79 ? 64 ASN A C 1 ATOM 487 O O . ASN A 1 64 ? 28.157 -9.899 7.684 1.00 94.21 ? 64 ASN A O 1 ATOM 488 C CB . ASN A 1 64 ? 31.177 -10.309 7.671 1.00 87.74 ? 64 ASN A CB 1 ATOM 489 C CG . ASN A 1 64 ? 31.736 -8.924 7.973 1.00 87.14 ? 64 ASN A CG 1 ATOM 490 O OD1 . ASN A 1 64 ? 31.002 -7.995 8.303 1.00 88.12 ? 64 ASN A OD1 1 ATOM 491 N ND2 . ASN A 1 64 ? 33.047 -8.776 7.819 1.00 85.16 ? 64 ASN A ND2 1 ATOM 492 N N . PRO A 1 65 ? 28.688 -9.079 9.729 1.00 97.91 ? 65 PRO A N 1 ATOM 493 C CA . PRO A 1 65 ? 27.476 -8.245 9.814 1.00 102.28 ? 65 PRO A CA 1 ATOM 494 C C . PRO A 1 65 ? 27.346 -7.172 8.723 1.00 104.74 ? 65 PRO A C 1 ATOM 495 O O . PRO A 1 65 ? 26.252 -6.646 8.518 1.00 106.65 ? 65 PRO A O 1 ATOM 496 C CB . PRO A 1 65 ? 27.579 -7.601 11.204 1.00 103.50 ? 65 PRO A CB 1 ATOM 497 C CG . PRO A 1 65 ? 29.016 -7.702 11.582 1.00 101.25 ? 65 PRO A CG 1 ATOM 498 C CD . PRO A 1 65 ? 29.535 -8.945 10.928 1.00 98.27 ? 65 PRO A CD 1 ATOM 499 N N . MET A 1 66 ? 28.448 -6.861 8.039 1.00 106.15 ? 66 MET A N 1 ATOM 500 C CA . MET A 1 66 ? 28.429 -5.992 6.854 1.00 108.62 ? 66 MET A CA 1 ATOM 501 C C . MET A 1 66 ? 27.897 -6.702 5.598 1.00 107.36 ? 66 MET A C 1 ATOM 502 O O . MET A 1 66 ? 27.725 -6.070 4.554 1.00 107.10 ? 66 MET A O 1 ATOM 503 C CB . MET A 1 66 ? 29.844 -5.482 6.555 1.00 108.13 ? 66 MET A CB 1 ATOM 504 C CG . MET A 1 66 ? 30.455 -4.609 7.640 1.00 109.88 ? 66 MET A CG 1 ATOM 505 S SD . MET A 1 66 ? 29.842 -2.914 7.598 1.00 114.25 ? 66 MET A SD 1 ATOM 506 C CE . MET A 1 66 ? 31.107 -2.084 8.559 1.00 115.19 ? 66 MET A CE 1 ATOM 507 N N . CYS A 1 67 ? 27.650 -8.008 5.696 1.00 106.47 ? 67 CYS A N 1 ATOM 508 C CA . CYS A 1 67 ? 27.251 -8.823 4.549 1.00 105.24 ? 67 CYS A CA 1 ATOM 509 C C . CYS A 1 67 ? 25.855 -9.410 4.730 1.00 106.39 ? 67 CYS A C 1 ATOM 510 O O . CYS A 1 67 ? 25.589 -10.546 4.326 1.00 105.53 ? 67 CYS A O 1 ATOM 511 C CB . CYS A 1 67 ? 28.270 -9.941 4.350 1.00 101.63 ? 67 CYS A CB 1 ATOM 512 S SG . CYS A 1 67 ? 29.942 -9.311 4.111 1.00 101.13 ? 67 CYS A SG 1 ATOM 513 N N . ASP A 1 68 ? 24.966 -8.625 5.331 1.00 107.86 ? 68 ASP A N 1 ATOM 514 C CA . ASP A 1 68 ? 23.581 -9.043 5.535 1.00 109.18 ? 68 ASP A CA 1 ATOM 515 C C . ASP A 1 68 ? 22.854 -9.245 4.208 1.00 108.97 ? 68 ASP A C 1 ATOM 516 O O . ASP A 1 68 ? 21.925 -10.045 4.133 1.00 110.49 ? 68 ASP A O 1 ATOM 517 C CB . ASP A 1 68 ? 22.826 -8.026 6.400 1.00 110.77 ? 68 ASP A CB 1 ATOM 518 C CG . ASP A 1 68 ? 23.279 -8.041 7.848 1.00 111.11 ? 68 ASP A CG 1 ATOM 519 O OD1 . ASP A 1 68 ? 24.105 -8.904 8.208 1.00 109.26 ? 68 ASP A OD1 1 ATOM 520 O OD2 . ASP A 1 68 ? 22.807 -7.189 8.633 1.00 114.49 ? 68 ASP A OD2 1 ATOM 521 N N . GLU A 1 69 ? 23.281 -8.528 3.168 1.00 107.21 ? 69 GLU A N 1 ATOM 522 C CA . GLU A 1 69 ? 22.736 -8.717 1.820 1.00 107.25 ? 69 GLU A CA 1 ATOM 523 C C . GLU A 1 69 ? 22.685 -10.200 1.436 1.00 105.16 ? 69 GLU A C 1 ATOM 524 O O . GLU A 1 69 ? 21.738 -10.649 0.785 1.00 105.44 ? 69 GLU A O 1 ATOM 525 C CB . GLU A 1 69 ? 23.571 -7.941 0.789 1.00 106.10 ? 69 GLU A CB 1 ATOM 526 C CG . GLU A 1 69 ? 23.051 -8.023 -0.647 1.00 106.22 ? 69 GLU A CG 1 ATOM 527 C CD . GLU A 1 69 ? 23.898 -7.249 -1.649 1.00 104.42 ? 69 GLU A CD 1 ATOM 528 O OE1 . GLU A 1 69 ? 24.869 -6.572 -1.243 1.00 104.20 ? 69 GLU A OE1 1 ATOM 529 O OE2 . GLU A 1 69 ? 23.586 -7.317 -2.857 1.00 103.38 ? 69 GLU A OE2 1 ATOM 530 N N . PHE A 1 70 ? 23.698 -10.951 1.863 1.00 102.40 ? 70 PHE A N 1 ATOM 531 C CA . PHE A 1 70 ? 23.854 -12.350 1.478 1.00 100.89 ? 70 PHE A CA 1 ATOM 532 C C . PHE A 1 70 ? 23.512 -13.309 2.616 1.00 101.57 ? 70 PHE A C 1 ATOM 533 O O . PHE A 1 70 ? 24.143 -14.359 2.767 1.00 99.49 ? 70 PHE A O 1 ATOM 534 C CB . PHE A 1 70 ? 25.288 -12.577 0.999 1.00 97.51 ? 70 PHE A CB 1 ATOM 535 C CG . PHE A 1 70 ? 25.781 -11.506 0.069 1.00 95.30 ? 70 PHE A CG 1 ATOM 536 C CD1 . PHE A 1 70 ? 25.250 -11.384 -1.205 1.00 93.51 ? 70 PHE A CD1 1 ATOM 537 C CD2 . PHE A 1 70 ? 26.745 -10.597 0.481 1.00 93.90 ? 70 PHE A CD2 1 ATOM 538 C CE1 . PHE A 1 70 ? 25.690 -10.394 -2.061 1.00 93.15 ? 70 PHE A CE1 1 ATOM 539 C CE2 . PHE A 1 70 ? 27.189 -9.604 -0.371 1.00 92.92 ? 70 PHE A CE2 1 ATOM 540 C CZ . PHE A 1 70 ? 26.662 -9.502 -1.644 1.00 92.56 ? 70 PHE A CZ 1 ATOM 541 N N . ILE A 1 71 ? 22.499 -12.955 3.399 1.00 105.23 ? 71 ILE A N 1 ATOM 542 C CA . ILE A 1 71 ? 22.114 -13.749 4.564 1.00 107.71 ? 71 ILE A CA 1 ATOM 543 C C . ILE A 1 71 ? 21.325 -14.997 4.166 1.00 109.00 ? 71 ILE A C 1 ATOM 544 O O . ILE A 1 71 ? 21.376 -15.997 4.872 1.00 108.91 ? 71 ILE A O 1 ATOM 545 C CB . ILE A 1 71 ? 21.325 -12.900 5.598 1.00 112.43 ? 71 ILE A CB 1 ATOM 546 C CG1 . ILE A 1 71 ? 21.328 -13.582 6.974 1.00 112.71 ? 71 ILE A CG1 1 ATOM 547 C CG2 . ILE A 1 71 ? 19.902 -12.608 5.121 1.00 114.50 ? 71 ILE A CG2 1 ATOM 548 C CD1 . ILE A 1 71 ? 21.005 -12.646 8.115 1.00 113.39 ? 71 ILE A CD1 1 ATOM 549 N N . ASN A 1 72 ? 20.602 -14.936 3.047 1.00 111.66 ? 72 ASN A N 1 ATOM 550 C CA . ASN A 1 72 ? 19.928 -16.116 2.480 1.00 112.99 ? 72 ASN A CA 1 ATOM 551 C C . ASN A 1 72 ? 19.858 -16.046 0.960 1.00 110.27 ? 72 ASN A C 1 ATOM 552 O O . ASN A 1 72 ? 18.828 -15.703 0.375 1.00 113.21 ? 72 ASN A O 1 ATOM 553 C CB . ASN A 1 72 ? 18.532 -16.299 3.085 1.00 117.73 ? 72 ASN A CB 1 ATOM 554 C CG . ASN A 1 72 ? 18.559 -17.103 4.371 1.00 120.88 ? 72 ASN A CG 1 ATOM 555 O OD1 . ASN A 1 72 ? 19.301 -18.082 4.488 1.00 120.94 ? 72 ASN A OD1 1 ATOM 556 N ND2 . ASN A 1 72 ? 17.752 -16.696 5.345 1.00 125.11 ? 72 ASN A ND2 1 ATOM 557 N N . VAL A 1 73 ? 20.975 -16.387 0.331 1.00 106.07 ? 73 VAL A N 1 ATOM 558 C CA . VAL A 1 73 ? 21.133 -16.224 -1.110 1.00 103.35 ? 73 VAL A CA 1 ATOM 559 C C . VAL A 1 73 ? 20.488 -17.371 -1.879 1.00 102.64 ? 73 VAL A C 1 ATOM 560 O O . VAL A 1 73 ? 20.652 -18.535 -1.513 1.00 102.65 ? 73 VAL A O 1 ATOM 561 C CB . VAL A 1 73 ? 22.620 -16.115 -1.518 1.00 99.43 ? 73 VAL A CB 1 ATOM 562 C CG1 . VAL A 1 73 ? 23.292 -14.980 -0.761 1.00 98.47 ? 73 VAL A CG1 1 ATOM 563 C CG2 . VAL A 1 73 ? 23.362 -17.430 -1.295 1.00 97.98 ? 73 VAL A CG2 1 ATOM 564 N N . PRO A 1 74 ? 19.767 -17.047 -2.963 1.00 102.55 ? 74 PRO A N 1 ATOM 565 C CA . PRO A 1 74 ? 19.182 -18.099 -3.777 1.00 102.99 ? 74 PRO A CA 1 ATOM 566 C C . PRO A 1 74 ? 20.234 -18.794 -4.637 1.00 98.52 ? 74 PRO A C 1 ATOM 567 O O . PRO A 1 74 ? 21.411 -18.436 -4.595 1.00 93.00 ? 74 PRO A O 1 ATOM 568 C CB . PRO A 1 74 ? 18.184 -17.339 -4.654 1.00 105.39 ? 74 PRO A CB 1 ATOM 569 C CG . PRO A 1 74 ? 18.805 -15.997 -4.825 1.00 104.47 ? 74 PRO A CG 1 ATOM 570 C CD . PRO A 1 74 ? 19.543 -15.711 -3.546 1.00 103.41 ? 74 PRO A CD 1 ATOM 571 N N . GLU A 1 75 ? 19.786 -19.785 -5.401 1.00 99.43 ? 75 GLU A N 1 ATOM 572 C CA . GLU A 1 75 ? 20.629 -20.536 -6.323 1.00 97.21 ? 75 GLU A CA 1 ATOM 573 C C . GLU A 1 75 ? 21.374 -19.602 -7.279 1.00 95.74 ? 75 GLU A C 1 ATOM 574 O O . GLU A 1 75 ? 20.788 -18.662 -7.814 1.00 95.65 ? 75 GLU A O 1 ATOM 575 C CB . GLU A 1 75 ? 19.752 -21.504 -7.117 1.00 99.95 ? 75 GLU A CB 1 ATOM 576 C CG . GLU A 1 75 ? 20.496 -22.474 -8.020 1.00 99.35 ? 75 GLU A CG 1 ATOM 577 C CD . GLU A 1 75 ? 19.563 -23.427 -8.746 1.00 102.28 ? 75 GLU A CD 1 ATOM 578 O OE1 . GLU A 1 75 ? 18.365 -23.502 -8.388 1.00 107.23 ? 75 GLU A OE1 1 ATOM 579 O OE2 . GLU A 1 75 ? 20.029 -24.105 -9.683 1.00 103.34 ? 75 GLU A OE2 1 ATOM 580 N N . TRP A 1 76 ? 22.665 -19.860 -7.483 1.00 93.52 ? 76 TRP A N 1 ATOM 581 C CA . TRP A 1 76 ? 23.470 -19.069 -8.416 1.00 93.08 ? 76 TRP A CA 1 ATOM 582 C C . TRP A 1 76 ? 24.007 -19.921 -9.571 1.00 91.42 ? 76 TRP A C 1 ATOM 583 O O . TRP A 1 76 ? 23.944 -21.155 -9.541 1.00 93.48 ? 76 TRP A O 1 ATOM 584 C CB . TRP A 1 76 ? 24.624 -18.370 -7.686 1.00 90.92 ? 76 TRP A CB 1 ATOM 585 C CG . TRP A 1 76 ? 25.607 -19.315 -7.069 1.00 90.11 ? 76 TRP A CG 1 ATOM 586 C CD1 . TRP A 1 76 ? 26.696 -19.878 -7.671 1.00 88.98 ? 76 TRP A CD1 1 ATOM 587 C CD2 . TRP A 1 76 ? 25.587 -19.814 -5.729 1.00 89.63 ? 76 TRP A CD2 1 ATOM 588 N NE1 . TRP A 1 76 ? 27.356 -20.696 -6.784 1.00 87.88 ? 76 TRP A NE1 1 ATOM 589 C CE2 . TRP A 1 76 ? 26.694 -20.676 -5.587 1.00 87.71 ? 76 TRP A CE2 1 ATOM 590 C CE3 . TRP A 1 76 ? 24.740 -19.616 -4.633 1.00 92.06 ? 76 TRP A CE3 1 ATOM 591 C CZ2 . TRP A 1 76 ? 26.977 -21.335 -4.396 1.00 88.56 ? 76 TRP A CZ2 1 ATOM 592 C CZ3 . TRP A 1 76 ? 25.021 -20.274 -3.447 1.00 91.60 ? 76 TRP A CZ3 1 ATOM 593 C CH2 . TRP A 1 76 ? 26.128 -21.123 -3.338 1.00 90.63 ? 76 TRP A CH2 1 ATOM 594 N N . SER A 1 77 ? 24.517 -19.238 -10.593 1.00 89.15 ? 77 SER A N 1 ATOM 595 C CA . SER A 1 77 ? 25.142 -19.880 -11.750 1.00 86.44 ? 77 SER A CA 1 ATOM 596 C C . SER A 1 77 ? 26.651 -19.877 -11.566 1.00 84.20 ? 77 SER A C 1 ATOM 597 O O . SER A 1 77 ? 27.310 -20.906 -11.695 1.00 83.63 ? 77 SER A O 1 ATOM 598 C CB . SER A 1 77 ? 24.779 -19.129 -13.029 1.00 85.84 ? 77 SER A CB 1 ATOM 599 O OG . SER A 1 77 ? 24.843 -17.726 -12.833 1.00 85.31 ? 77 SER A OG 1 ATOM 600 N N . TYR A 1 78 ? 27.185 -18.699 -11.270 1.00 82.33 ? 78 TYR A N 1 ATOM 601 C CA . TYR A 1 78 ? 28.582 -18.547 -10.894 1.00 79.36 ? 78 TYR A CA 1 ATOM 602 C C . TYR A 1 78 ? 28.665 -17.503 -9.788 1.00 78.83 ? 78 TYR A C 1 ATOM 603 O O . TYR A 1 78 ? 27.671 -16.856 -9.473 1.00 80.56 ? 78 TYR A O 1 ATOM 604 C CB . TYR A 1 78 ? 29.439 -18.148 -12.112 1.00 76.33 ? 78 TYR A CB 1 ATOM 605 C CG . TYR A 1 78 ? 29.015 -16.865 -12.816 1.00 74.90 ? 78 TYR A CG 1 ATOM 606 C CD1 . TYR A 1 78 ? 27.948 -16.850 -13.716 1.00 74.39 ? 78 TYR A CD1 1 ATOM 607 C CD2 . TYR A 1 78 ? 29.690 -15.672 -12.584 1.00 73.83 ? 78 TYR A CD2 1 ATOM 608 C CE1 . TYR A 1 78 ? 27.564 -15.677 -14.356 1.00 74.83 ? 78 TYR A CE1 1 ATOM 609 C CE2 . TYR A 1 78 ? 29.316 -14.499 -13.217 1.00 74.10 ? 78 TYR A CE2 1 ATOM 610 C CZ . TYR A 1 78 ? 28.254 -14.502 -14.103 1.00 75.33 ? 78 TYR A CZ 1 ATOM 611 O OH . TYR A 1 78 ? 27.899 -13.316 -14.720 1.00 74.99 ? 78 TYR A OH 1 ATOM 612 N N . ILE A 1 79 ? 29.847 -17.352 -9.202 1.00 76.90 ? 79 ILE A N 1 ATOM 613 C CA . ILE A 1 79 ? 30.064 -16.391 -8.124 1.00 78.72 ? 79 ILE A CA 1 ATOM 614 C C . ILE A 1 79 ? 31.098 -15.358 -8.560 1.00 77.75 ? 79 ILE A C 1 ATOM 615 O O . ILE A 1 79 ? 32.074 -15.697 -9.227 1.00 74.89 ? 79 ILE A O 1 ATOM 616 C CB . ILE A 1 79 ? 30.564 -17.098 -6.850 1.00 80.20 ? 79 ILE A CB 1 ATOM 617 C CG1 . ILE A 1 79 ? 29.514 -18.089 -6.335 1.00 82.75 ? 79 ILE A CG1 1 ATOM 618 C CG2 . ILE A 1 79 ? 30.899 -16.082 -5.766 1.00 81.72 ? 79 ILE A CG2 1 ATOM 619 C CD1 . ILE A 1 79 ? 30.061 -19.088 -5.338 1.00 83.07 ? 79 ILE A CD1 1 ATOM 620 N N . VAL A 1 80 ? 30.888 -14.100 -8.181 1.00 79.82 ? 80 VAL A N 1 ATOM 621 C CA . VAL A 1 80 ? 31.832 -13.032 -8.513 1.00 80.20 ? 80 VAL A CA 1 ATOM 622 C C . VAL A 1 80 ? 32.368 -12.384 -7.245 1.00 79.65 ? 80 VAL A C 1 ATOM 623 O O . VAL A 1 80 ? 31.611 -11.827 -6.458 1.00 83.22 ? 80 VAL A O 1 ATOM 624 C CB . VAL A 1 80 ? 31.194 -11.949 -9.409 1.00 81.70 ? 80 VAL A CB 1 ATOM 625 C CG1 . VAL A 1 80 ? 32.194 -10.830 -9.699 1.00 80.87 ? 80 VAL A CG1 1 ATOM 626 C CG2 . VAL A 1 80 ? 30.688 -12.567 -10.703 1.00 81.44 ? 80 VAL A CG2 1 ATOM 627 N N . GLU A 1 81 ? 33.683 -12.450 -7.077 1.00 78.93 ? 81 GLU A N 1 ATOM 628 C CA . GLU A 1 81 ? 34.365 -11.906 -5.918 1.00 80.08 ? 81 GLU A CA 1 ATOM 629 C C . GLU A 1 81 ? 35.445 -10.959 -6.403 1.00 78.67 ? 81 GLU A C 1 ATOM 630 O O . GLU A 1 81 ? 36.136 -11.259 -7.367 1.00 80.44 ? 81 GLU A O 1 ATOM 631 C CB . GLU A 1 81 ? 35.005 -13.042 -5.122 1.00 81.86 ? 81 GLU A CB 1 ATOM 632 C CG . GLU A 1 81 ? 35.653 -12.607 -3.819 1.00 85.76 ? 81 GLU A CG 1 ATOM 633 C CD . GLU A 1 81 ? 36.515 -13.688 -3.191 1.00 87.04 ? 81 GLU A CD 1 ATOM 634 O OE1 . GLU A 1 81 ? 37.352 -14.285 -3.906 1.00 84.15 ? 81 GLU A OE1 1 ATOM 635 O OE2 . GLU A 1 81 ? 36.349 -13.935 -1.975 1.00 88.69 ? 81 GLU A OE2 1 ATOM 636 N N . LYS A 1 82 ? 35.607 -9.827 -5.734 1.00 79.71 ? 82 LYS A N 1 ATOM 637 C CA . LYS A 1 82 ? 36.686 -8.901 -6.073 1.00 80.88 ? 82 LYS A CA 1 ATOM 638 C C . LYS A 1 82 ? 38.071 -9.460 -5.717 1.00 80.41 ? 82 LYS A C 1 ATOM 639 O O . LYS A 1 82 ? 38.203 -10.496 -5.046 1.00 77.67 ? 82 LYS A O 1 ATOM 640 C CB . LYS A 1 82 ? 36.474 -7.549 -5.380 1.00 82.80 ? 82 LYS A CB 1 ATOM 641 C CG . LYS A 1 82 ? 35.259 -6.790 -5.879 1.00 84.04 ? 82 LYS A CG 1 ATOM 642 C CD . LYS A 1 82 ? 35.218 -5.386 -5.301 1.00 86.49 ? 82 LYS A CD 1 ATOM 643 C CE . LYS A 1 82 ? 33.897 -4.686 -5.586 1.00 88.74 ? 82 LYS A CE 1 ATOM 644 N NZ . LYS A 1 82 ? 33.614 -4.608 -7.044 1.00 90.37 ? 82 LYS A NZ 1 ATOM 645 N N . ALA A 1 83 ? 39.100 -8.761 -6.186 1.00 81.96 ? 83 ALA A N 1 ATOM 646 C CA . ALA A 1 83 ? 40.482 -9.124 -5.893 1.00 83.36 ? 83 ALA A CA 1 ATOM 647 C C . ALA A 1 83 ? 40.840 -8.835 -4.426 1.00 87.75 ? 83 ALA A C 1 ATOM 648 O O . ALA A 1 83 ? 41.502 -9.651 -3.775 1.00 87.88 ? 83 ALA A O 1 ATOM 649 C CB . ALA A 1 83 ? 41.427 -8.391 -6.835 1.00 81.65 ? 83 ALA A CB 1 ATOM 650 N N . ASN A 1 84 ? 40.390 -7.688 -3.910 1.00 90.80 ? 84 ASN A N 1 ATOM 651 C CA . ASN A 1 84 ? 40.673 -7.291 -2.523 1.00 94.27 ? 84 ASN A CA 1 ATOM 652 C C . ASN A 1 84 ? 39.432 -6.781 -1.784 1.00 93.66 ? 84 ASN A C 1 ATOM 653 O O . ASN A 1 84 ? 39.355 -5.598 -1.442 1.00 93.44 ? 84 ASN A O 1 ATOM 654 C CB . ASN A 1 84 ? 41.767 -6.214 -2.497 1.00 99.27 ? 84 ASN A CB 1 ATOM 655 C CG . ASN A 1 84 ? 43.064 -6.679 -3.140 1.00 101.83 ? 84 ASN A CG 1 ATOM 656 O OD1 . ASN A 1 84 ? 43.567 -7.764 -2.839 1.00 102.50 ? 84 ASN A OD1 1 ATOM 657 N ND2 . ASN A 1 84 ? 43.615 -5.857 -4.031 1.00 104.26 ? 84 ASN A ND2 1 ATOM 658 N N . PRO A 1 85 ? 38.457 -7.674 -1.520 1.00 92.50 ? 85 PRO A N 1 ATOM 659 C CA . PRO A 1 85 ? 37.229 -7.230 -0.848 1.00 93.22 ? 85 PRO A CA 1 ATOM 660 C C . PRO A 1 85 ? 37.524 -6.618 0.519 1.00 93.09 ? 85 PRO A C 1 ATOM 661 O O . PRO A 1 85 ? 38.361 -7.143 1.248 1.00 94.31 ? 85 PRO A O 1 ATOM 662 C CB . PRO A 1 85 ? 36.411 -8.525 -0.705 1.00 91.89 ? 85 PRO A CB 1 ATOM 663 C CG . PRO A 1 85 ? 36.996 -9.482 -1.687 1.00 88.62 ? 85 PRO A CG 1 ATOM 664 C CD . PRO A 1 85 ? 38.448 -9.126 -1.776 1.00 88.95 ? 85 PRO A CD 1 ATOM 665 N N . VAL A 1 86 ? 36.858 -5.518 0.859 1.00 94.15 ? 86 VAL A N 1 ATOM 666 C CA . VAL A 1 86 ? 37.126 -4.837 2.133 1.00 96.23 ? 86 VAL A CA 1 ATOM 667 C C . VAL A 1 86 ? 36.507 -5.564 3.336 1.00 95.86 ? 86 VAL A C 1 ATOM 668 O O . VAL A 1 86 ? 37.088 -5.564 4.424 1.00 95.33 ? 86 VAL A O 1 ATOM 669 C CB . VAL A 1 86 ? 36.676 -3.352 2.124 1.00 99.33 ? 86 VAL A CB 1 ATOM 670 C CG1 . VAL A 1 86 ? 37.280 -2.619 0.932 1.00 99.63 ? 86 VAL A CG1 1 ATOM 671 C CG2 . VAL A 1 86 ? 35.156 -3.223 2.135 1.00 100.58 ? 86 VAL A CG2 1 ATOM 672 N N . ASN A 1 87 ? 35.342 -6.183 3.131 1.00 93.58 ? 87 ASN A N 1 ATOM 673 C CA . ASN A 1 87 ? 34.640 -6.904 4.189 1.00 92.42 ? 87 ASN A CA 1 ATOM 674 C C . ASN A 1 87 ? 34.963 -8.391 4.178 1.00 91.94 ? 87 ASN A C 1 ATOM 675 O O . ASN A 1 87 ? 34.165 -9.217 3.733 1.00 92.60 ? 87 ASN A O 1 ATOM 676 C CB . ASN A 1 87 ? 33.136 -6.696 4.063 1.00 93.87 ? 87 ASN A CB 1 ATOM 677 C CG . ASN A 1 87 ? 32.730 -5.260 4.305 1.00 97.44 ? 87 ASN A CG 1 ATOM 678 O OD1 . ASN A 1 87 ? 33.133 -4.644 5.298 1.00 98.97 ? 87 ASN A OD1 1 ATOM 679 N ND2 . ASN A 1 87 ? 31.923 -4.714 3.401 1.00 98.69 ? 87 ASN A ND2 1 ATOM 680 N N . ASP A 1 88 ? 36.151 -8.716 4.673 1.00 92.78 ? 88 ASP A N 1 ATOM 681 C CA . ASP A 1 88 ? 36.588 -10.096 4.841 1.00 91.01 ? 88 ASP A CA 1 ATOM 682 C C . ASP A 1 88 ? 36.335 -10.477 6.315 1.00 92.49 ? 88 ASP A C 1 ATOM 683 O O . ASP A 1 88 ? 35.194 -10.383 6.785 1.00 92.84 ? 88 ASP A O 1 ATOM 684 C CB . ASP A 1 88 ? 38.062 -10.221 4.412 1.00 89.08 ? 88 ASP A CB 1 ATOM 685 C CG . ASP A 1 88 ? 38.516 -11.664 4.241 1.00 88.40 ? 88 ASP A CG 1 ATOM 686 O OD1 . ASP A 1 88 ? 37.659 -12.564 4.137 1.00 86.65 ? 88 ASP A OD1 1 ATOM 687 O OD2 . ASP A 1 88 ? 39.745 -11.899 4.207 1.00 90.51 ? 88 ASP A OD2 1 ATOM 688 N N . LEU A 1 89 ? 37.377 -10.890 7.039 1.00 91.43 ? 89 LEU A N 1 ATOM 689 C CA . LEU A 1 89 ? 37.274 -11.179 8.467 1.00 92.30 ? 89 LEU A CA 1 ATOM 690 C C . LEU A 1 89 ? 37.402 -9.879 9.272 1.00 92.80 ? 89 LEU A C 1 ATOM 691 O O . LEU A 1 89 ? 38.510 -9.371 9.477 1.00 91.77 ? 89 LEU A O 1 ATOM 692 C CB . LEU A 1 89 ? 38.370 -12.165 8.892 1.00 90.58 ? 89 LEU A CB 1 ATOM 693 C CG . LEU A 1 89 ? 38.453 -13.495 8.142 1.00 87.48 ? 89 LEU A CG 1 ATOM 694 C CD1 . LEU A 1 89 ? 39.642 -14.295 8.652 1.00 86.98 ? 89 LEU A CD1 1 ATOM 695 C CD2 . LEU A 1 89 ? 37.163 -14.289 8.281 1.00 86.31 ? 89 LEU A CD2 1 ATOM 696 N N . CYS A 1 90 ? 36.267 -9.354 9.729 1.00 93.98 ? 90 CYS A N 1 ATOM 697 C CA . CYS A 1 90 ? 36.235 -8.090 10.465 1.00 95.07 ? 90 CYS A CA 1 ATOM 698 C C . CYS A 1 90 ? 37.069 -8.159 11.749 1.00 92.83 ? 90 CYS A C 1 ATOM 699 O O . CYS A 1 90 ? 37.851 -7.254 12.032 1.00 93.73 ? 90 CYS A O 1 ATOM 700 C CB . CYS A 1 90 ? 34.791 -7.673 10.764 1.00 98.12 ? 90 CYS A CB 1 ATOM 701 S SG . CYS A 1 90 ? 33.756 -8.950 11.523 1.00 101.47 ? 90 CYS A SG 1 ATOM 702 N N . TYR A 1 91 ? 36.905 -9.237 12.510 1.00 90.80 ? 91 TYR A N 1 ATOM 703 C CA . TYR A 1 91 ? 37.806 -9.551 13.612 1.00 91.55 ? 91 TYR A CA 1 ATOM 704 C C . TYR A 1 91 ? 38.982 -10.328 13.031 1.00 89.78 ? 91 TYR A C 1 ATOM 705 O O . TYR A 1 91 ? 38.777 -11.378 12.427 1.00 89.31 ? 91 TYR A O 1 ATOM 706 C CB . TYR A 1 91 ? 37.088 -10.395 14.665 1.00 94.21 ? 91 TYR A CB 1 ATOM 707 C CG . TYR A 1 91 ? 37.757 -10.395 16.025 1.00 97.91 ? 91 TYR A CG 1 ATOM 708 C CD1 . TYR A 1 91 ? 38.922 -11.123 16.253 1.00 98.32 ? 91 TYR A CD1 1 ATOM 709 C CD2 . TYR A 1 91 ? 37.222 -9.666 17.088 1.00 99.96 ? 91 TYR A CD2 1 ATOM 710 C CE1 . TYR A 1 91 ? 39.533 -11.125 17.499 1.00 100.57 ? 91 TYR A CE1 1 ATOM 711 C CE2 . TYR A 1 91 ? 37.826 -9.665 18.338 1.00 101.63 ? 91 TYR A CE2 1 ATOM 712 C CZ . TYR A 1 91 ? 38.983 -10.395 18.537 1.00 101.08 ? 91 TYR A CZ 1 ATOM 713 O OH . TYR A 1 91 ? 39.586 -10.396 19.775 1.00 102.08 ? 91 TYR A OH 1 ATOM 714 N N . PRO A 1 92 ? 40.219 -9.834 13.220 1.00 90.67 ? 92 PRO A N 1 ATOM 715 C CA . PRO A 1 92 ? 41.373 -10.423 12.527 1.00 89.04 ? 92 PRO A CA 1 ATOM 716 C C . PRO A 1 92 ? 41.632 -11.889 12.867 1.00 89.74 ? 92 PRO A C 1 ATOM 717 O O . PRO A 1 92 ? 41.238 -12.359 13.934 1.00 91.56 ? 92 PRO A O 1 ATOM 718 C CB . PRO A 1 92 ? 42.542 -9.564 13.012 1.00 89.83 ? 92 PRO A CB 1 ATOM 719 C CG . PRO A 1 92 ? 42.116 -9.090 14.357 1.00 91.65 ? 92 PRO A CG 1 ATOM 720 C CD . PRO A 1 92 ? 40.642 -8.831 14.214 1.00 92.55 ? 92 PRO A CD 1 ATOM 721 N N . GLY A 1 93 ? 42.296 -12.598 11.957 1.00 91.65 ? 93 GLY A N 1 ATOM 722 C CA . GLY A 1 93 ? 42.645 -13.998 12.181 1.00 91.67 ? 93 GLY A CA 1 ATOM 723 C C . GLY A 1 93 ? 42.948 -14.776 10.915 1.00 91.14 ? 93 GLY A C 1 ATOM 724 O O . GLY A 1 93 ? 43.545 -14.244 9.979 1.00 89.65 ? 93 GLY A O 1 ATOM 725 N N . ASP A 1 94 ? 42.548 -16.048 10.906 1.00 91.80 ? 94 ASP A N 1 ATOM 726 C CA . ASP A 1 94 ? 42.723 -16.930 9.752 1.00 90.86 ? 94 ASP A CA 1 ATOM 727 C C . ASP A 1 94 ? 41.461 -17.729 9.483 1.00 89.73 ? 94 ASP A C 1 ATOM 728 O O . ASP A 1 94 ? 40.598 -17.882 10.362 1.00 89.36 ? 94 ASP A O 1 ATOM 729 C CB . ASP A 1 94 ? 43.859 -17.923 9.991 1.00 92.71 ? 94 ASP A CB 1 ATOM 730 C CG . ASP A 1 94 ? 45.202 -17.251 10.114 1.00 95.81 ? 94 ASP A CG 1 ATOM 731 O OD1 . ASP A 1 94 ? 45.646 -16.629 9.127 1.00 97.72 ? 94 ASP A OD1 1 ATOM 732 O OD2 . ASP A 1 94 ? 45.817 -17.354 11.196 1.00 99.88 ? 94 ASP A OD2 1 ATOM 733 N N . PHE A 1 95 ? 41.373 -18.236 8.255 1.00 84.89 ? 95 PHE A N 1 ATOM 734 C CA . PHE A 1 95 ? 40.357 -19.197 7.867 1.00 81.27 ? 95 PHE A CA 1 ATOM 735 C C . PHE A 1 95 ? 41.118 -20.427 7.401 1.00 80.11 ? 95 PHE A C 1 ATOM 736 O O . PHE A 1 95 ? 41.830 -20.387 6.400 1.00 78.32 ? 95 PHE A O 1 ATOM 737 C CB . PHE A 1 95 ? 39.486 -18.627 6.752 1.00 79.50 ? 95 PHE A CB 1 ATOM 738 C CG . PHE A 1 95 ? 38.155 -19.307 6.606 1.00 79.70 ? 95 PHE A CG 1 ATOM 739 C CD1 . PHE A 1 95 ? 38.072 -20.630 6.209 1.00 80.15 ? 95 PHE A CD1 1 ATOM 740 C CD2 . PHE A 1 95 ? 36.980 -18.616 6.851 1.00 81.14 ? 95 PHE A CD2 1 ATOM 741 C CE1 . PHE A 1 95 ? 36.843 -21.251 6.061 1.00 81.63 ? 95 PHE A CE1 1 ATOM 742 C CE2 . PHE A 1 95 ? 35.749 -19.230 6.708 1.00 81.79 ? 95 PHE A CE2 1 ATOM 743 C CZ . PHE A 1 95 ? 35.679 -20.552 6.314 1.00 81.81 ? 95 PHE A CZ 1 ATOM 744 N N . ASN A 1 96 ? 40.982 -21.514 8.146 1.00 81.64 ? 96 ASN A N 1 ATOM 745 C CA . ASN A 1 96 ? 41.751 -22.722 7.889 1.00 82.34 ? 96 ASN A CA 1 ATOM 746 C C . ASN A 1 96 ? 41.262 -23.459 6.643 1.00 79.55 ? 96 ASN A C 1 ATOM 747 O O . ASN A 1 96 ? 40.058 -23.659 6.468 1.00 76.92 ? 96 ASN A O 1 ATOM 748 C CB . ASN A 1 96 ? 41.684 -23.643 9.109 1.00 86.35 ? 96 ASN A CB 1 ATOM 749 C CG . ASN A 1 96 ? 42.808 -24.657 9.135 1.00 89.16 ? 96 ASN A CG 1 ATOM 750 O OD1 . ASN A 1 96 ? 43.983 -24.300 9.273 1.00 90.11 ? 96 ASN A OD1 1 ATOM 751 N ND2 . ASN A 1 96 ? 42.453 -25.934 9.010 1.00 90.82 ? 96 ASN A ND2 1 ATOM 752 N N . ASP A 1 97 ? 42.209 -23.866 5.794 1.00 79.87 ? 97 ASP A N 1 ATOM 753 C CA . ASP A 1 97 ? 41.925 -24.539 4.516 1.00 78.74 ? 97 ASP A CA 1 ATOM 754 C C . ASP A 1 97 ? 40.919 -23.766 3.663 1.00 74.99 ? 97 ASP A C 1 ATOM 755 O O . ASP A 1 97 ? 40.003 -24.345 3.070 1.00 74.29 ? 97 ASP A O 1 ATOM 756 C CB . ASP A 1 97 ? 41.452 -25.984 4.749 1.00 83.43 ? 97 ASP A CB 1 ATOM 757 C CG . ASP A 1 97 ? 42.584 -26.911 5.162 1.00 87.61 ? 97 ASP A CG 1 ATOM 758 O OD1 . ASP A 1 97 ? 43.701 -26.769 4.620 1.00 89.59 ? 97 ASP A OD1 1 ATOM 759 O OD2 . ASP A 1 97 ? 42.353 -27.791 6.018 1.00 93.03 ? 97 ASP A OD2 1 ATOM 760 N N . TYR A 1 98 ? 41.115 -22.454 3.600 1.00 72.36 ? 98 TYR A N 1 ATOM 761 C CA . TYR A 1 98 ? 40.188 -21.548 2.926 1.00 72.77 ? 98 TYR A CA 1 ATOM 762 C C . TYR A 1 98 ? 40.092 -21.859 1.439 1.00 73.29 ? 98 TYR A C 1 ATOM 763 O O . TYR A 1 98 ? 39.005 -21.839 0.858 1.00 73.99 ? 98 TYR A O 1 ATOM 764 C CB . TYR A 1 98 ? 40.656 -20.103 3.132 1.00 72.01 ? 98 TYR A CB 1 ATOM 765 C CG . TYR A 1 98 ? 39.699 -19.021 2.669 1.00 72.41 ? 98 TYR A CG 1 ATOM 766 C CD1 . TYR A 1 98 ? 38.332 -19.106 2.931 1.00 73.23 ? 98 TYR A CD1 1 ATOM 767 C CD2 . TYR A 1 98 ? 40.171 -17.887 1.997 1.00 71.23 ? 98 TYR A CD2 1 ATOM 768 C CE1 . TYR A 1 98 ? 37.461 -18.110 2.519 1.00 74.29 ? 98 TYR A CE1 1 ATOM 769 C CE2 . TYR A 1 98 ? 39.309 -16.887 1.581 1.00 71.64 ? 98 TYR A CE2 1 ATOM 770 C CZ . TYR A 1 98 ? 37.954 -17.001 1.847 1.00 74.90 ? 98 TYR A CZ 1 ATOM 771 O OH . TYR A 1 98 ? 37.076 -16.014 1.456 1.00 78.19 ? 98 TYR A OH 1 ATOM 772 N N . GLU A 1 99 ? 41.236 -22.169 0.838 1.00 73.71 ? 99 GLU A N 1 ATOM 773 C CA . GLU A 1 99 ? 41.307 -22.406 -0.597 1.00 74.74 ? 99 GLU A CA 1 ATOM 774 C C . GLU A 1 99 ? 40.625 -23.713 -0.956 1.00 74.66 ? 99 GLU A C 1 ATOM 775 O O . GLU A 1 99 ? 39.876 -23.778 -1.929 1.00 74.74 ? 99 GLU A O 1 ATOM 776 C CB . GLU A 1 99 ? 42.757 -22.412 -1.086 1.00 75.62 ? 99 GLU A CB 1 ATOM 777 C CG . GLU A 1 99 ? 43.436 -21.042 -1.056 1.00 76.69 ? 99 GLU A CG 1 ATOM 778 C CD . GLU A 1 99 ? 43.849 -20.599 0.341 1.00 79.09 ? 99 GLU A CD 1 ATOM 779 O OE1 . GLU A 1 99 ? 44.355 -21.443 1.119 1.00 80.12 ? 99 GLU A OE1 1 ATOM 780 O OE2 . GLU A 1 99 ? 43.666 -19.404 0.655 1.00 78.12 ? 99 GLU A OE2 1 ATOM 781 N N . GLU A 1 100 ? 40.872 -24.752 -0.163 1.00 74.62 ? 100 GLU A N 1 ATOM 782 C CA . GLU A 1 100 ? 40.212 -26.035 -0.380 1.00 73.55 ? 100 GLU A CA 1 ATOM 783 C C . GLU A 1 100 ? 38.692 -25.894 -0.255 1.00 74.18 ? 100 GLU A C 1 ATOM 784 O O . GLU A 1 100 ? 37.945 -26.608 -0.930 1.00 74.75 ? 100 GLU A O 1 ATOM 785 C CB . GLU A 1 100 ? 40.752 -27.105 0.578 1.00 73.07 ? 100 GLU A CB 1 ATOM 786 C CG . GLU A 1 100 ? 42.101 -27.683 0.167 1.00 72.35 ? 100 GLU A CG 1 ATOM 787 C CD . GLU A 1 100 ? 42.013 -28.630 -1.022 1.00 73.22 ? 100 GLU A CD 1 ATOM 788 O OE1 . GLU A 1 100 ? 41.113 -29.499 -1.026 1.00 74.61 ? 100 GLU A OE1 1 ATOM 789 O OE2 . GLU A 1 100 ? 42.844 -28.519 -1.954 1.00 70.37 ? 100 GLU A OE2 1 ATOM 790 N N . LEU A 1 101 ? 38.237 -24.964 0.585 1.00 73.39 ? 101 LEU A N 1 ATOM 791 C CA . LEU A 1 101 ? 36.805 -24.697 0.702 1.00 74.61 ? 101 LEU A CA 1 ATOM 792 C C . LEU A 1 101 ? 36.280 -23.989 -0.543 1.00 72.01 ? 101 LEU A C 1 ATOM 793 O O . LEU A 1 101 ? 35.305 -24.428 -1.145 1.00 68.78 ? 101 LEU A O 1 ATOM 794 C CB . LEU A 1 101 ? 36.488 -23.871 1.949 1.00 76.04 ? 101 LEU A CB 1 ATOM 795 C CG . LEU A 1 101 ? 34.998 -23.620 2.205 1.00 77.50 ? 101 LEU A CG 1 ATOM 796 C CD1 . LEU A 1 101 ? 34.185 -24.908 2.186 1.00 78.26 ? 101 LEU A CD1 1 ATOM 797 C CD2 . LEU A 1 101 ? 34.837 -22.906 3.533 1.00 80.65 ? 101 LEU A CD2 1 ATOM 798 N N . LYS A 1 102 ? 36.928 -22.893 -0.923 1.00 71.45 ? 102 LYS A N 1 ATOM 799 C CA . LYS A 1 102 ? 36.590 -22.199 -2.170 1.00 71.48 ? 102 LYS A CA 1 ATOM 800 C C . LYS A 1 102 ? 36.514 -23.159 -3.357 1.00 70.48 ? 102 LYS A C 1 ATOM 801 O O . LYS A 1 102 ? 35.607 -23.073 -4.182 1.00 71.18 ? 102 LYS A O 1 ATOM 802 C CB . LYS A 1 102 ? 37.618 -21.119 -2.485 1.00 71.98 ? 102 LYS A CB 1 ATOM 803 C CG . LYS A 1 102 ? 37.408 -19.800 -1.768 1.00 74.65 ? 102 LYS A CG 1 ATOM 804 C CD . LYS A 1 102 ? 38.601 -18.890 -2.028 1.00 76.27 ? 102 LYS A CD 1 ATOM 805 C CE . LYS A 1 102 ? 38.205 -17.427 -2.077 1.00 78.61 ? 102 LYS A CE 1 ATOM 806 N NZ . LYS A 1 102 ? 39.402 -16.545 -2.161 1.00 79.79 ? 102 LYS A NZ 1 ATOM 807 N N . HIS A 1 103 ? 37.472 -24.072 -3.450 1.00 69.47 ? 103 HIS A N 1 ATOM 808 C CA . HIS A 1 103 ? 37.459 -25.045 -4.528 1.00 69.58 ? 103 HIS A CA 1 ATOM 809 C C . HIS A 1 103 ? 36.207 -25.920 -4.454 1.00 71.32 ? 103 HIS A C 1 ATOM 810 O O . HIS A 1 103 ? 35.653 -26.301 -5.476 1.00 71.29 ? 103 HIS A O 1 ATOM 811 C CB . HIS A 1 103 ? 38.717 -25.914 -4.506 1.00 68.91 ? 103 HIS A CB 1 ATOM 812 C CG . HIS A 1 103 ? 38.706 -26.999 -5.536 1.00 69.10 ? 103 HIS A CG 1 ATOM 813 N ND1 . HIS A 1 103 ? 39.159 -26.809 -6.825 1.00 68.00 ? 103 HIS A ND1 1 ATOM 814 C CD2 . HIS A 1 103 ? 38.263 -28.277 -5.477 1.00 69.67 ? 103 HIS A CD2 1 ATOM 815 C CE1 . HIS A 1 103 ? 39.011 -27.928 -7.509 1.00 66.85 ? 103 HIS A CE1 1 ATOM 816 N NE2 . HIS A 1 103 ? 38.472 -28.834 -6.714 1.00 68.47 ? 103 HIS A NE2 1 ATOM 817 N N . LEU A 1 104 ? 35.776 -26.231 -3.239 1.00 73.80 ? 104 LEU A N 1 ATOM 818 C CA . LEU A 1 104 ? 34.571 -27.027 -3.017 1.00 78.42 ? 104 LEU A CA 1 ATOM 819 C C . LEU A 1 104 ? 33.323 -26.308 -3.561 1.00 81.16 ? 104 LEU A C 1 ATOM 820 O O . LEU A 1 104 ? 32.365 -26.954 -3.980 1.00 83.07 ? 104 LEU A O 1 ATOM 821 C CB . LEU A 1 104 ? 34.419 -27.310 -1.512 1.00 81.26 ? 104 LEU A CB 1 ATOM 822 C CG . LEU A 1 104 ? 33.971 -28.683 -1.006 1.00 83.15 ? 104 LEU A CG 1 ATOM 823 C CD1 . LEU A 1 104 ? 34.869 -29.806 -1.500 1.00 83.60 ? 104 LEU A CD1 1 ATOM 824 C CD2 . LEU A 1 104 ? 33.960 -28.658 0.513 1.00 84.35 ? 104 LEU A CD2 1 ATOM 825 N N . LEU A 1 105 ? 33.352 -24.974 -3.551 1.00 83.99 ? 105 LEU A N 1 ATOM 826 C CA . LEU A 1 105 ? 32.243 -24.139 -4.040 1.00 85.53 ? 105 LEU A CA 1 ATOM 827 C C . LEU A 1 105 ? 32.080 -24.102 -5.548 1.00 86.93 ? 105 LEU A C 1 ATOM 828 O O . LEU A 1 105 ? 31.028 -23.696 -6.040 1.00 92.41 ? 105 LEU A O 1 ATOM 829 C CB . LEU A 1 105 ? 32.416 -22.685 -3.594 1.00 84.38 ? 105 LEU A CB 1 ATOM 830 C CG . LEU A 1 105 ? 32.126 -22.305 -2.157 1.00 84.23 ? 105 LEU A CG 1 ATOM 831 C CD1 . LEU A 1 105 ? 32.217 -20.792 -2.033 1.00 84.31 ? 105 LEU A CD1 1 ATOM 832 C CD2 . LEU A 1 105 ? 30.755 -22.801 -1.736 1.00 86.55 ? 105 LEU A CD2 1 ATOM 833 N N . SER A 1 106 ? 33.116 -24.470 -6.289 1.00 94.36 ? 106 SER A N 1 ATOM 834 C CA . SER A 1 106 ? 32.984 -24.568 -7.736 1.00 97.86 ? 106 SER A CA 1 ATOM 835 C C . SER A 1 106 ? 32.076 -25.743 -8.124 1.00 98.75 ? 106 SER A C 1 ATOM 836 O O . SER A 1 106 ? 31.590 -25.807 -9.251 1.00 103.62 ? 106 SER A O 1 ATOM 837 C CB . SER A 1 106 ? 34.358 -24.688 -8.402 1.00 98.14 ? 106 SER A CB 1 ATOM 838 O OG . SER A 1 106 ? 35.059 -25.824 -7.937 1.00 99.20 ? 106 SER A OG 1 ATOM 839 N N . ARG A 1 107 ? 31.858 -26.664 -7.184 1.00 100.88 ? 107 ARG A N 1 ATOM 840 C CA . ARG A 1 107 ? 30.916 -27.774 -7.355 1.00 104.76 ? 107 ARG A CA 1 ATOM 841 C C . ARG A 1 107 ? 29.525 -27.491 -6.763 1.00 99.88 ? 107 ARG A C 1 ATOM 842 O O . ARG A 1 107 ? 28.695 -28.399 -6.698 1.00 98.79 ? 107 ARG A O 1 ATOM 843 C CB . ARG A 1 107 ? 31.472 -29.046 -6.695 1.00 112.27 ? 107 ARG A CB 1 ATOM 844 C CG . ARG A 1 107 ? 32.492 -29.819 -7.518 1.00 118.68 ? 107 ARG A CG 1 ATOM 845 C CD . ARG A 1 107 ? 32.837 -31.137 -6.828 1.00 125.94 ? 107 ARG A CD 1 ATOM 846 N NE . ARG A 1 107 ? 33.416 -32.125 -7.742 1.00 132.68 ? 107 ARG A NE 1 ATOM 847 C CZ . ARG A 1 107 ? 33.599 -33.417 -7.457 1.00 136.26 ? 107 ARG A CZ 1 ATOM 848 N NH1 . ARG A 1 107 ? 33.249 -33.915 -6.269 1.00 135.27 ? 107 ARG A NH1 1 ATOM 849 N NH2 . ARG A 1 107 ? 34.135 -34.222 -8.371 1.00 136.63 ? 107 ARG A NH2 1 ATOM 850 N N . ILE A 1 108 ? 29.269 -26.252 -6.336 1.00 95.14 ? 108 ILE A N 1 ATOM 851 C CA . ILE A 1 108 ? 28.039 -25.920 -5.603 1.00 94.15 ? 108 ILE A CA 1 ATOM 852 C C . ILE A 1 108 ? 27.297 -24.718 -6.203 1.00 93.31 ? 108 ILE A C 1 ATOM 853 O O . ILE A 1 108 ? 27.902 -23.681 -6.479 1.00 93.25 ? 108 ILE A O 1 ATOM 854 C CB . ILE A 1 108 ? 28.341 -25.644 -4.107 1.00 92.48 ? 108 ILE A CB 1 ATOM 855 C CG1 . ILE A 1 108 ? 28.829 -26.920 -3.412 1.00 91.81 ? 108 ILE A CG1 1 ATOM 856 C CG2 . ILE A 1 108 ? 27.106 -25.120 -3.389 1.00 92.25 ? 108 ILE A CG2 1 ATOM 857 C CD1 . ILE A 1 108 ? 29.376 -26.702 -2.016 1.00 90.81 ? 108 ILE A CD1 1 ATOM 858 N N . ASN A 1 109 ? 25.983 -24.870 -6.377 1.00 93.37 ? 109 ASN A N 1 ATOM 859 C CA . ASN A 1 109 ? 25.112 -23.810 -6.898 1.00 93.07 ? 109 ASN A CA 1 ATOM 860 C C . ASN A 1 109 ? 24.139 -23.222 -5.874 1.00 92.86 ? 109 ASN A C 1 ATOM 861 O O . ASN A 1 109 ? 23.616 -22.128 -6.092 1.00 91.70 ? 109 ASN A O 1 ATOM 862 C CB . ASN A 1 109 ? 24.297 -24.337 -8.078 1.00 95.01 ? 109 ASN A CB 1 ATOM 863 C CG . ASN A 1 109 ? 25.156 -24.673 -9.273 1.00 96.20 ? 109 ASN A CG 1 ATOM 864 O OD1 . ASN A 1 109 ? 25.654 -23.781 -9.962 1.00 96.18 ? 109 ASN A OD1 1 ATOM 865 N ND2 . ASN A 1 109 ? 25.330 -25.965 -9.535 1.00 97.88 ? 109 ASN A ND2 1 ATOM 866 N N . HIS A 1 110 ? 23.873 -23.942 -4.781 1.00 91.92 ? 110 HIS A N 1 ATOM 867 C CA . HIS A 1 110 ? 22.892 -23.480 -3.793 1.00 92.43 ? 110 HIS A CA 1 ATOM 868 C C . HIS A 1 110 ? 23.114 -24.031 -2.389 1.00 91.63 ? 110 HIS A C 1 ATOM 869 O O . HIS A 1 110 ? 23.247 -25.239 -2.192 1.00 91.11 ? 110 HIS A O 1 ATOM 870 C CB . HIS A 1 110 ? 21.480 -23.843 -4.255 1.00 94.65 ? 110 HIS A CB 1 ATOM 871 C CG . HIS A 1 110 ? 20.395 -23.133 -3.508 1.00 95.94 ? 110 HIS A CG 1 ATOM 872 N ND1 . HIS A 1 110 ? 19.147 -23.684 -3.311 1.00 97.59 ? 110 HIS A ND1 1 ATOM 873 C CD2 . HIS A 1 110 ? 20.371 -21.919 -2.908 1.00 95.23 ? 110 HIS A CD2 1 ATOM 874 C CE1 . HIS A 1 110 ? 18.399 -22.837 -2.628 1.00 98.23 ? 110 HIS A CE1 1 ATOM 875 N NE2 . HIS A 1 110 ? 19.118 -21.759 -2.371 1.00 97.35 ? 110 HIS A NE2 1 ATOM 876 N N . PHE A 1 111 ? 23.150 -23.122 -1.420 1.00 92.23 ? 111 PHE A N 1 ATOM 877 C CA . PHE A 1 111 ? 23.141 -23.483 -0.010 1.00 93.51 ? 111 PHE A CA 1 ATOM 878 C C . PHE A 1 111 ? 21.763 -23.175 0.550 1.00 96.50 ? 111 PHE A C 1 ATOM 879 O O . PHE A 1 111 ? 21.071 -22.298 0.039 1.00 97.08 ? 111 PHE A O 1 ATOM 880 C CB . PHE A 1 111 ? 24.160 -22.659 0.785 1.00 91.47 ? 111 PHE A CB 1 ATOM 881 C CG . PHE A 1 111 ? 25.585 -23.133 0.665 1.00 89.20 ? 111 PHE A CG 1 ATOM 882 C CD1 . PHE A 1 111 ? 25.931 -24.457 0.915 1.00 88.99 ? 111 PHE A CD1 1 ATOM 883 C CD2 . PHE A 1 111 ? 26.596 -22.233 0.356 1.00 86.63 ? 111 PHE A CD2 1 ATOM 884 C CE1 . PHE A 1 111 ? 27.249 -24.874 0.825 1.00 86.00 ? 111 PHE A CE1 1 ATOM 885 C CE2 . PHE A 1 111 ? 27.912 -22.646 0.269 1.00 84.11 ? 111 PHE A CE2 1 ATOM 886 C CZ . PHE A 1 111 ? 28.240 -23.968 0.506 1.00 84.17 ? 111 PHE A CZ 1 ATOM 887 N N . GLU A 1 112 ? 21.374 -23.894 1.599 1.00 99.02 ? 112 GLU A N 1 ATOM 888 C CA . GLU A 1 112 ? 20.219 -23.511 2.414 1.00 103.31 ? 112 GLU A CA 1 ATOM 889 C C . GLU A 1 112 ? 20.636 -23.487 3.881 1.00 100.96 ? 112 GLU A C 1 ATOM 890 O O . GLU A 1 112 ? 20.975 -24.522 4.456 1.00 98.91 ? 112 GLU A O 1 ATOM 891 C CB . GLU A 1 112 ? 19.038 -24.466 2.209 1.00 107.47 ? 112 GLU A CB 1 ATOM 892 C CG . GLU A 1 112 ? 17.738 -23.971 2.834 1.00 111.49 ? 112 GLU A CG 1 ATOM 893 C CD . GLU A 1 112 ? 16.655 -25.037 2.872 1.00 116.69 ? 112 GLU A CD 1 ATOM 894 O OE1 . GLU A 1 112 ? 16.500 -25.764 1.864 1.00 118.22 ? 112 GLU A OE1 1 ATOM 895 O OE2 . GLU A 1 112 ? 15.959 -25.144 3.910 1.00 116.65 ? 112 GLU A OE2 1 ATOM 896 N N . LYS A 1 113 ? 20.612 -22.301 4.478 1.00 99.99 ? 113 LYS A N 1 ATOM 897 C CA . LYS A 1 113 ? 21.043 -22.129 5.859 1.00 101.73 ? 113 LYS A CA 1 ATOM 898 C C . LYS A 1 113 ? 20.016 -22.694 6.839 1.00 103.95 ? 113 LYS A C 1 ATOM 899 O O . LYS A 1 113 ? 18.819 -22.445 6.701 1.00 105.95 ? 113 LYS A O 1 ATOM 900 C CB . LYS A 1 113 ? 21.279 -20.651 6.147 1.00 102.51 ? 113 LYS A CB 1 ATOM 901 C CG . LYS A 1 113 ? 21.818 -20.375 7.539 1.00 104.31 ? 113 LYS A CG 1 ATOM 902 C CD . LYS A 1 113 ? 22.806 -19.217 7.540 1.00 105.30 ? 113 LYS A CD 1 ATOM 903 C CE . LYS A 1 113 ? 22.148 -17.894 7.183 1.00 106.32 ? 113 LYS A CE 1 ATOM 904 N NZ . LYS A 1 113 ? 23.151 -16.904 6.700 1.00 105.37 ? 113 LYS A NZ 1 ATOM 905 N N . ILE A 1 114 ? 20.489 -23.466 7.815 1.00 103.88 ? 114 ILE A N 1 ATOM 906 C CA . ILE A 1 114 ? 19.630 -23.961 8.888 1.00 107.26 ? 114 ILE A CA 1 ATOM 907 C C . ILE A 1 114 ? 20.315 -23.824 10.244 1.00 108.56 ? 114 ILE A C 1 ATOM 908 O O . ILE A 1 114 ? 21.545 -23.782 10.331 1.00 108.58 ? 114 ILE A O 1 ATOM 909 C CB . ILE A 1 114 ? 19.213 -25.431 8.678 1.00 108.33 ? 114 ILE A CB 1 ATOM 910 C CG1 . ILE A 1 114 ? 20.436 -26.354 8.633 1.00 107.57 ? 114 ILE A CG1 1 ATOM 911 C CG2 . ILE A 1 114 ? 18.381 -25.571 7.408 1.00 108.66 ? 114 ILE A CG2 1 ATOM 912 C CD1 . ILE A 1 114 ? 20.119 -27.776 9.043 1.00 109.41 ? 114 ILE A CD1 1 ATOM 913 N N . GLN A 1 115 ? 19.503 -23.766 11.296 1.00 109.31 ? 115 GLN A N 1 ATOM 914 C CA . GLN A 1 115 ? 20.003 -23.619 12.657 1.00 109.30 ? 115 GLN A CA 1 ATOM 915 C C . GLN A 1 115 ? 20.248 -24.988 13.279 1.00 109.35 ? 115 GLN A C 1 ATOM 916 O O . GLN A 1 115 ? 19.349 -25.831 13.297 1.00 109.83 ? 115 GLN A O 1 ATOM 917 C CB . GLN A 1 115 ? 18.996 -22.844 13.506 1.00 110.78 ? 115 GLN A CB 1 ATOM 918 C CG . GLN A 1 115 ? 19.538 -22.429 14.862 1.00 111.07 ? 115 GLN A CG 1 ATOM 919 C CD . GLN A 1 115 ? 18.496 -21.761 15.732 1.00 112.73 ? 115 GLN A CD 1 ATOM 920 O OE1 . GLN A 1 115 ? 18.678 -20.627 16.174 1.00 113.11 ? 115 GLN A OE1 1 ATOM 921 N NE2 . GLN A 1 115 ? 17.398 -22.461 15.986 1.00 113.83 ? 115 GLN A NE2 1 ATOM 922 N N . ILE A 1 116 ? 21.456 -25.198 13.799 1.00 107.55 ? 116 ILE A N 1 ATOM 923 C CA . ILE A 1 116 ? 21.812 -26.478 14.423 1.00 108.02 ? 116 ILE A CA 1 ATOM 924 C C . ILE A 1 116 ? 21.987 -26.383 15.942 1.00 110.25 ? 116 ILE A C 1 ATOM 925 O O . ILE A 1 116 ? 21.664 -27.332 16.654 1.00 113.61 ? 116 ILE A O 1 ATOM 926 C CB . ILE A 1 116 ? 23.069 -27.116 13.784 1.00 104.66 ? 116 ILE A CB 1 ATOM 927 C CG1 . ILE A 1 116 ? 24.209 -26.102 13.659 1.00 101.91 ? 116 ILE A CG1 1 ATOM 928 C CG2 . ILE A 1 116 ? 22.726 -27.692 12.418 1.00 103.73 ? 116 ILE A CG2 1 ATOM 929 C CD1 . ILE A 1 116 ? 25.554 -26.738 13.401 1.00 99.88 ? 116 ILE A CD1 1 ATOM 930 N N . ILE A 1 117 ? 22.495 -25.255 16.436 1.00 110.72 ? 117 ILE A N 1 ATOM 931 C CA . ILE A 1 117 ? 22.608 -25.022 17.880 1.00 112.76 ? 117 ILE A CA 1 ATOM 932 C C . ILE A 1 117 ? 22.036 -23.644 18.226 1.00 113.46 ? 117 ILE A C 1 ATOM 933 O O . ILE A 1 117 ? 22.729 -22.634 18.075 1.00 112.26 ? 117 ILE A O 1 ATOM 934 C CB . ILE A 1 117 ? 24.068 -25.131 18.367 1.00 112.68 ? 117 ILE A CB 1 ATOM 935 C CG1 . ILE A 1 117 ? 24.648 -26.503 17.998 1.00 111.81 ? 117 ILE A CG1 1 ATOM 936 C CG2 . ILE A 1 117 ? 24.145 -24.898 19.874 1.00 115.65 ? 117 ILE A CG2 1 ATOM 937 C CD1 . ILE A 1 117 ? 26.064 -26.741 18.482 1.00 111.07 ? 117 ILE A CD1 1 ATOM 938 N N . PRO A 1 118 ? 20.770 -23.598 18.697 1.00 115.87 ? 118 PRO A N 1 ATOM 939 C CA . PRO A 1 118 ? 20.123 -22.306 18.949 1.00 117.05 ? 118 PRO A CA 1 ATOM 940 C C . PRO A 1 118 ? 20.867 -21.452 19.967 1.00 118.28 ? 118 PRO A C 1 ATOM 941 O O . PRO A 1 118 ? 21.403 -21.970 20.949 1.00 118.90 ? 118 PRO A O 1 ATOM 942 C CB . PRO A 1 118 ? 18.731 -22.685 19.481 1.00 119.74 ? 118 PRO A CB 1 ATOM 943 C CG . PRO A 1 118 ? 18.538 -24.124 19.155 1.00 119.25 ? 118 PRO A CG 1 ATOM 944 C CD . PRO A 1 118 ? 19.901 -24.735 19.056 1.00 117.67 ? 118 PRO A CD 1 ATOM 945 N N . LYS A 1 119 ? 20.883 -20.147 19.721 1.00 119.38 ? 119 LYS A N 1 ATOM 946 C CA . LYS A 1 119 ? 21.612 -19.198 20.558 1.00 120.95 ? 119 LYS A CA 1 ATOM 947 C C . LYS A 1 119 ? 21.074 -19.163 21.991 1.00 123.58 ? 119 LYS A C 1 ATOM 948 O O . LYS A 1 119 ? 21.834 -18.980 22.944 1.00 125.69 ? 119 LYS A O 1 ATOM 949 C CB . LYS A 1 119 ? 21.540 -17.806 19.928 1.00 121.58 ? 119 LYS A CB 1 ATOM 950 C CG . LYS A 1 119 ? 22.560 -16.820 20.461 1.00 122.56 ? 119 LYS A CG 1 ATOM 951 C CD . LYS A 1 119 ? 22.623 -15.590 19.573 1.00 122.78 ? 119 LYS A CD 1 ATOM 952 C CE . LYS A 1 119 ? 23.505 -14.512 20.180 1.00 124.45 ? 119 LYS A CE 1 ATOM 953 N NZ . LYS A 1 119 ? 23.561 -13.298 19.319 1.00 124.08 ? 119 LYS A NZ 1 ATOM 954 N N . SER A 1 120 ? 19.763 -19.348 22.133 1.00 124.80 ? 120 SER A N 1 ATOM 955 C CA . SER A 1 120 ? 19.106 -19.375 23.441 1.00 125.81 ? 120 SER A CA 1 ATOM 956 C C . SER A 1 120 ? 19.499 -20.587 24.288 1.00 126.51 ? 120 SER A C 1 ATOM 957 O O . SER A 1 120 ? 19.401 -20.546 25.508 1.00 130.01 ? 120 SER A O 1 ATOM 958 C CB . SER A 1 120 ? 17.590 -19.375 23.256 1.00 126.63 ? 120 SER A CB 1 ATOM 959 O OG . SER A 1 120 ? 17.177 -20.519 22.529 1.00 125.33 ? 120 SER A OG 1 ATOM 960 N N . SER A 1 121 ? 19.949 -21.658 23.639 1.00 125.66 ? 121 SER A N 1 ATOM 961 C CA . SER A 1 121 ? 20.250 -22.918 24.323 1.00 126.40 ? 121 SER A CA 1 ATOM 962 C C . SER A 1 121 ? 21.438 -22.878 25.290 1.00 125.74 ? 121 SER A C 1 ATOM 963 O O . SER A 1 121 ? 21.652 -23.839 26.027 1.00 125.96 ? 121 SER A O 1 ATOM 964 C CB . SER A 1 121 ? 20.518 -24.015 23.295 1.00 125.13 ? 121 SER A CB 1 ATOM 965 O OG . SER A 1 121 ? 19.491 -24.080 22.327 1.00 126.76 ? 121 SER A OG 1 ATOM 966 N N . TRP A 1 122 ? 22.215 -21.798 25.280 1.00 124.17 ? 122 TRP A N 1 ATOM 967 C CA . TRP A 1 122 ? 23.393 -21.698 26.142 1.00 124.36 ? 122 TRP A CA 1 ATOM 968 C C . TRP A 1 122 ? 23.028 -21.132 27.507 1.00 128.04 ? 122 TRP A C 1 ATOM 969 O O . TRP A 1 122 ? 23.207 -19.945 27.766 1.00 130.58 ? 122 TRP A O 1 ATOM 970 C CB . TRP A 1 122 ? 24.460 -20.840 25.474 1.00 121.79 ? 122 TRP A CB 1 ATOM 971 C CG . TRP A 1 122 ? 24.935 -21.421 24.190 1.00 119.30 ? 122 TRP A CG 1 ATOM 972 C CD1 . TRP A 1 122 ? 24.687 -20.948 22.936 1.00 117.60 ? 122 TRP A CD1 1 ATOM 973 C CD2 . TRP A 1 122 ? 25.730 -22.600 24.026 1.00 118.07 ? 122 TRP A CD2 1 ATOM 974 N NE1 . TRP A 1 122 ? 25.289 -21.750 21.999 1.00 115.66 ? 122 TRP A NE1 1 ATOM 975 C CE2 . TRP A 1 122 ? 25.936 -22.773 22.640 1.00 115.95 ? 122 TRP A CE2 1 ATOM 976 C CE3 . TRP A 1 122 ? 26.294 -23.523 24.915 1.00 118.70 ? 122 TRP A CE3 1 ATOM 977 C CZ2 . TRP A 1 122 ? 26.683 -23.834 22.120 1.00 114.18 ? 122 TRP A CZ2 1 ATOM 978 C CZ3 . TRP A 1 122 ? 27.036 -24.578 24.399 1.00 117.23 ? 122 TRP A CZ3 1 ATOM 979 C CH2 . TRP A 1 122 ? 27.225 -24.723 23.012 1.00 115.77 ? 122 TRP A CH2 1 ATOM 980 N N . SER A 1 123 ? 22.522 -22.002 28.376 1.00 129.79 ? 123 SER A N 1 ATOM 981 C CA . SER A 1 123 ? 22.013 -21.602 29.689 1.00 133.29 ? 123 SER A CA 1 ATOM 982 C C . SER A 1 123 ? 23.102 -21.495 30.762 1.00 134.95 ? 123 SER A C 1 ATOM 983 O O . SER A 1 123 ? 22.927 -20.780 31.748 1.00 137.93 ? 123 SER A O 1 ATOM 984 C CB . SER A 1 123 ? 20.926 -22.581 30.145 1.00 135.23 ? 123 SER A CB 1 ATOM 985 O OG . SER A 1 123 ? 21.282 -23.916 29.832 1.00 133.23 ? 123 SER A OG 1 ATOM 986 N N . SER A 1 124 ? 24.213 -22.207 30.576 1.00 133.31 ? 124 SER A N 1 ATOM 987 C CA . SER A 1 124 ? 25.331 -22.181 31.527 1.00 133.43 ? 124 SER A CA 1 ATOM 988 C C . SER A 1 124 ? 26.416 -21.173 31.143 1.00 131.74 ? 124 SER A C 1 ATOM 989 O O . SER A 1 124 ? 27.353 -20.950 31.910 1.00 132.14 ? 124 SER A O 1 ATOM 990 C CB . SER A 1 124 ? 25.961 -23.569 31.632 1.00 132.47 ? 124 SER A CB 1 ATOM 991 O OG . SER A 1 124 ? 24.970 -24.560 31.823 1.00 133.12 ? 124 SER A OG 1 ATOM 992 N N . HIS A 1 125 ? 26.294 -20.580 29.955 1.00 129.34 ? 125 HIS A N 1 ATOM 993 C CA . HIS A 1 125 ? 27.286 -19.636 29.439 1.00 127.45 ? 125 HIS A CA 1 ATOM 994 C C . HIS A 1 125 ? 26.603 -18.393 28.871 1.00 127.43 ? 125 HIS A C 1 ATOM 995 O O . HIS A 1 125 ? 25.438 -18.442 28.475 1.00 127.47 ? 125 HIS A O 1 ATOM 996 C CB . HIS A 1 125 ? 28.123 -20.298 28.339 1.00 123.62 ? 125 HIS A CB 1 ATOM 997 C CG . HIS A 1 125 ? 28.797 -21.569 28.760 1.00 122.95 ? 125 HIS A CG 1 ATOM 998 N ND1 . HIS A 1 125 ? 28.157 -22.790 28.749 1.00 123.22 ? 125 HIS A ND1 1 ATOM 999 C CD2 . HIS A 1 125 ? 30.062 -21.811 29.178 1.00 122.22 ? 125 HIS A CD2 1 ATOM 1000 C CE1 . HIS A 1 125 ? 28.995 -23.727 29.158 1.00 123.33 ? 125 HIS A CE1 1 ATOM 1001 N NE2 . HIS A 1 125 ? 30.159 -23.160 29.421 1.00 122.51 ? 125 HIS A NE2 1 ATOM 1002 N N . GLU A 1 126 ? 27.339 -17.285 28.818 1.00 126.66 ? 126 GLU A N 1 ATOM 1003 C CA . GLU A 1 126 ? 26.812 -16.028 28.285 1.00 126.16 ? 126 GLU A CA 1 ATOM 1004 C C . GLU A 1 126 ? 27.032 -15.928 26.768 1.00 123.00 ? 126 GLU A C 1 ATOM 1005 O O . GLU A 1 126 ? 28.164 -15.778 26.293 1.00 122.23 ? 126 GLU A O 1 ATOM 1006 C CB . GLU A 1 126 ? 27.457 -14.843 29.007 1.00 127.81 ? 126 GLU A CB 1 ATOM 1007 C CG . GLU A 1 126 ? 26.965 -13.474 28.556 1.00 128.29 ? 126 GLU A CG 1 ATOM 1008 C CD . GLU A 1 126 ? 25.456 -13.327 28.634 1.00 130.19 ? 126 GLU A CD 1 ATOM 1009 O OE1 . GLU A 1 126 ? 24.920 -13.256 29.765 1.00 129.97 ? 126 GLU A OE1 1 ATOM 1010 O OE2 . GLU A 1 126 ? 24.812 -13.278 27.558 1.00 128.39 ? 126 GLU A OE2 1 ATOM 1011 N N . ALA A 1 127 ? 25.939 -15.990 26.014 1.00 121.57 ? 127 ALA A N 1 ATOM 1012 C CA . ALA A 1 127 ? 26.005 -16.075 24.555 1.00 117.17 ? 127 ALA A CA 1 ATOM 1013 C C . ALA A 1 127 ? 25.723 -14.749 23.843 1.00 117.41 ? 127 ALA A C 1 ATOM 1014 O O . ALA A 1 127 ? 25.853 -14.668 22.619 1.00 117.30 ? 127 ALA A O 1 ATOM 1015 C CB . ALA A 1 127 ? 25.037 -17.141 24.063 1.00 115.50 ? 127 ALA A CB 1 ATOM 1016 N N . SER A 1 128 ? 25.349 -13.718 24.598 1.00 120.12 ? 128 SER A N 1 ATOM 1017 C CA . SER A 1 128 ? 24.904 -12.450 24.013 1.00 119.29 ? 128 SER A CA 1 ATOM 1018 C C . SER A 1 128 ? 25.858 -11.282 24.272 1.00 117.42 ? 128 SER A C 1 ATOM 1019 O O . SER A 1 128 ? 25.519 -10.134 23.988 1.00 116.66 ? 128 SER A O 1 ATOM 1020 C CB . SER A 1 128 ? 23.509 -12.111 24.535 1.00 123.49 ? 128 SER A CB 1 ATOM 1021 O OG . SER A 1 128 ? 22.574 -13.074 24.086 1.00 124.93 ? 128 SER A OG 1 ATOM 1022 N N . LEU A 1 129 ? 27.044 -11.575 24.802 1.00 115.49 ? 129 LEU A N 1 ATOM 1023 C CA . LEU A 1 129 ? 28.072 -10.556 25.000 1.00 114.76 ? 129 LEU A CA 1 ATOM 1024 C C . LEU A 1 129 ? 29.316 -10.845 24.162 1.00 112.26 ? 129 LEU A C 1 ATOM 1025 O O . LEU A 1 129 ? 30.352 -10.207 24.345 1.00 112.21 ? 129 LEU A O 1 ATOM 1026 C CB . LEU A 1 129 ? 28.444 -10.461 26.480 1.00 117.85 ? 129 LEU A CB 1 ATOM 1027 C CG . LEU A 1 129 ? 27.309 -10.126 27.455 1.00 120.59 ? 129 LEU A CG 1 ATOM 1028 C CD1 . LEU A 1 129 ? 27.854 -10.019 28.870 1.00 122.94 ? 129 LEU A CD1 1 ATOM 1029 C CD2 . LEU A 1 129 ? 26.589 -8.843 27.060 1.00 121.03 ? 129 LEU A CD2 1 ATOM 1030 N N . GLY A 1 130 ? 29.204 -11.790 23.231 1.00 110.08 ? 130 GLY A N 1 ATOM 1031 C CA . GLY A 1 130 ? 30.307 -12.145 22.347 1.00 107.56 ? 130 GLY A CA 1 ATOM 1032 C C . GLY A 1 130 ? 30.416 -11.248 21.125 1.00 106.69 ? 130 GLY A C 1 ATOM 1033 O O . GLY A 1 130 ? 30.170 -11.693 19.993 1.00 103.88 ? 130 GLY A O 1 ATOM 1034 N N . VAL A 1 131 ? 30.811 -9.994 21.356 1.00 107.43 ? 131 VAL A N 1 ATOM 1035 C CA . VAL A 1 131 ? 30.895 -8.977 20.301 1.00 105.51 ? 131 VAL A CA 1 ATOM 1036 C C . VAL A 1 131 ? 32.187 -8.161 20.382 1.00 104.53 ? 131 VAL A C 1 ATOM 1037 O O . VAL A 1 131 ? 32.903 -8.217 21.377 1.00 107.83 ? 131 VAL A O 1 ATOM 1038 C CB . VAL A 1 131 ? 29.689 -8.011 20.354 1.00 107.66 ? 131 VAL A CB 1 ATOM 1039 C CG1 . VAL A 1 131 ? 28.386 -8.780 20.175 1.00 107.69 ? 131 VAL A CG1 1 ATOM 1040 C CG2 . VAL A 1 131 ? 29.672 -7.215 21.655 1.00 110.23 ? 131 VAL A CG2 1 ATOM 1041 N N . SER A 1 132 ? 32.463 -7.399 19.327 1.00 102.76 ? 132 SER A N 1 ATOM 1042 C CA . SER A 1 132 ? 33.673 -6.576 19.238 1.00 101.74 ? 132 SER A CA 1 ATOM 1043 C C . SER A 1 132 ? 33.449 -5.343 18.364 1.00 101.82 ? 132 SER A C 1 ATOM 1044 O O . SER A 1 132 ? 32.642 -5.366 17.429 1.00 101.07 ? 132 SER A O 1 ATOM 1045 C CB . SER A 1 132 ? 34.834 -7.397 18.672 1.00 98.25 ? 132 SER A CB 1 ATOM 1046 O OG . SER A 1 132 ? 35.910 -6.562 18.276 1.00 96.86 ? 132 SER A OG 1 ATOM 1047 N N . SER A 1 133 ? 34.182 -4.274 18.665 1.00 102.82 ? 133 SER A N 1 ATOM 1048 C CA . SER A 1 133 ? 34.089 -3.030 17.903 1.00 103.18 ? 133 SER A CA 1 ATOM 1049 C C . SER A 1 133 ? 34.726 -3.139 16.512 1.00 100.88 ? 133 SER A C 1 ATOM 1050 O O . SER A 1 133 ? 34.504 -2.276 15.663 1.00 99.82 ? 133 SER A O 1 ATOM 1051 C CB . SER A 1 133 ? 34.739 -1.888 18.679 1.00 105.62 ? 133 SER A CB 1 ATOM 1052 O OG . SER A 1 133 ? 36.065 -2.227 19.036 1.00 106.35 ? 133 SER A OG 1 ATOM 1053 N N . ALA A 1 134 ? 35.517 -4.188 16.284 1.00 100.08 ? 134 ALA A N 1 ATOM 1054 C CA . ALA A 1 134 ? 36.070 -4.468 14.952 1.00 98.87 ? 134 ALA A CA 1 ATOM 1055 C C . ALA A 1 134 ? 35.006 -4.935 13.946 1.00 98.24 ? 134 ALA A C 1 ATOM 1056 O O . ALA A 1 134 ? 35.194 -4.785 12.737 1.00 95.30 ? 134 ALA A O 1 ATOM 1057 C CB . ALA A 1 134 ? 37.186 -5.495 15.048 1.00 97.74 ? 134 ALA A CB 1 ATOM 1058 N N . CYS A 1 135 ? 33.903 -5.498 14.448 1.00 100.87 ? 135 CYS A N 1 ATOM 1059 C CA . CYS A 1 135 ? 32.766 -5.917 13.617 1.00 101.57 ? 135 CYS A CA 1 ATOM 1060 C C . CYS A 1 135 ? 31.507 -5.089 13.925 1.00 100.61 ? 135 CYS A C 1 ATOM 1061 O O . CYS A 1 135 ? 30.555 -5.600 14.521 1.00 98.79 ? 135 CYS A O 1 ATOM 1062 C CB . CYS A 1 135 ? 32.464 -7.403 13.840 1.00 104.37 ? 135 CYS A CB 1 ATOM 1063 S SG . CYS A 1 135 ? 33.853 -8.517 13.533 1.00 109.55 ? 135 CYS A SG 1 ATOM 1064 N N . PRO A 1 136 ? 31.492 -3.809 13.509 1.00 98.85 ? 136 PRO A N 1 ATOM 1065 C CA . PRO A 1 136 ? 30.375 -2.935 13.849 1.00 100.57 ? 136 PRO A CA 1 ATOM 1066 C C . PRO A 1 136 ? 29.110 -3.210 13.037 1.00 99.86 ? 136 PRO A C 1 ATOM 1067 O O . PRO A 1 136 ? 29.195 -3.669 11.902 1.00 96.81 ? 136 PRO A O 1 ATOM 1068 C CB . PRO A 1 136 ? 30.918 -1.547 13.502 1.00 101.33 ? 136 PRO A CB 1 ATOM 1069 C CG . PRO A 1 136 ? 31.844 -1.802 12.366 1.00 98.18 ? 136 PRO A CG 1 ATOM 1070 C CD . PRO A 1 136 ? 32.507 -3.104 12.703 1.00 96.88 ? 136 PRO A CD 1 ATOM 1071 N N . TYR A 1 137 ? 27.952 -2.923 13.628 1.00 102.63 ? 137 TYR A N 1 ATOM 1072 C CA . TYR A 1 137 ? 26.674 -2.954 12.913 1.00 103.35 ? 137 TYR A CA 1 ATOM 1073 C C . TYR A 1 137 ? 25.749 -1.851 13.431 1.00 105.38 ? 137 TYR A C 1 ATOM 1074 O O . TYR A 1 137 ? 25.348 -1.868 14.598 1.00 108.64 ? 137 TYR A O 1 ATOM 1075 C CB . TYR A 1 137 ? 25.998 -4.318 13.065 1.00 103.82 ? 137 TYR A CB 1 ATOM 1076 C CG . TYR A 1 137 ? 24.646 -4.404 12.383 1.00 104.68 ? 137 TYR A CG 1 ATOM 1077 C CD1 . TYR A 1 137 ? 24.549 -4.480 10.993 1.00 103.45 ? 137 TYR A CD1 1 ATOM 1078 C CD2 . TYR A 1 137 ? 23.466 -4.405 13.127 1.00 105.71 ? 137 TYR A CD2 1 ATOM 1079 C CE1 . TYR A 1 137 ? 23.315 -4.555 10.365 1.00 103.70 ? 137 TYR A CE1 1 ATOM 1080 C CE2 . TYR A 1 137 ? 22.231 -4.481 12.506 1.00 106.47 ? 137 TYR A CE2 1 ATOM 1081 C CZ . TYR A 1 137 ? 22.162 -4.556 11.127 1.00 105.45 ? 137 TYR A CZ 1 ATOM 1082 O OH . TYR A 1 137 ? 20.941 -4.633 10.507 1.00 106.41 ? 137 TYR A OH 1 ATOM 1083 N N . GLN A 1 138 ? 25.417 -0.900 12.558 1.00 104.55 ? 138 GLN A N 1 ATOM 1084 C CA . GLN A 1 138 ? 24.584 0.249 12.915 1.00 107.29 ? 138 GLN A CA 1 ATOM 1085 C C . GLN A 1 138 ? 25.108 0.974 14.167 1.00 109.41 ? 138 GLN A C 1 ATOM 1086 O O . GLN A 1 138 ? 24.356 1.264 15.101 1.00 110.53 ? 138 GLN A O 1 ATOM 1087 C CB . GLN A 1 138 ? 23.122 -0.180 13.093 1.00 109.53 ? 138 GLN A CB 1 ATOM 1088 C CG . GLN A 1 138 ? 22.508 -0.802 11.844 1.00 108.30 ? 138 GLN A CG 1 ATOM 1089 C CD . GLN A 1 138 ? 21.020 -1.096 11.982 1.00 109.67 ? 138 GLN A CD 1 ATOM 1090 O OE1 . GLN A 1 138 ? 20.412 -0.843 13.021 1.00 110.86 ? 138 GLN A OE1 1 ATOM 1091 N NE2 . GLN A 1 138 ? 20.429 -1.639 10.926 1.00 109.33 ? 138 GLN A NE2 1 ATOM 1092 N N . GLY A 1 139 ? 26.413 1.244 14.173 1.00 108.56 ? 139 GLY A N 1 ATOM 1093 C CA . GLY A 1 139 ? 27.050 2.036 15.222 1.00 109.92 ? 139 GLY A CA 1 ATOM 1094 C C . GLY A 1 139 ? 27.476 1.267 16.457 1.00 109.95 ? 139 GLY A C 1 ATOM 1095 O O . GLY A 1 139 ? 28.210 1.802 17.291 1.00 110.00 ? 139 GLY A O 1 ATOM 1096 N N . LYS A 1 140 ? 27.025 0.020 16.577 1.00 109.29 ? 140 LYS A N 1 ATOM 1097 C CA . LYS A 1 140 ? 27.273 -0.782 17.772 1.00 111.65 ? 140 LYS A CA 1 ATOM 1098 C C . LYS A 1 140 ? 28.176 -1.959 17.456 1.00 107.82 ? 140 LYS A C 1 ATOM 1099 O O . LYS A 1 140 ? 28.298 -2.362 16.304 1.00 105.63 ? 140 LYS A O 1 ATOM 1100 C CB . LYS A 1 140 ? 25.955 -1.301 18.356 1.00 115.09 ? 140 LYS A CB 1 ATOM 1101 C CG . LYS A 1 140 ? 24.895 -0.229 18.575 1.00 119.61 ? 140 LYS A CG 1 ATOM 1102 C CD . LYS A 1 140 ? 23.780 -0.683 19.514 1.00 124.08 ? 140 LYS A CD 1 ATOM 1103 C CE . LYS A 1 140 ? 23.126 -1.991 19.077 1.00 123.64 ? 140 LYS A CE 1 ATOM 1104 N NZ . LYS A 1 140 ? 22.735 -2.010 17.637 1.00 122.84 ? 140 LYS A NZ 1 ATOM 1105 N N . SER A 1 141 ? 28.797 -2.510 18.495 1.00 108.21 ? 141 SER A N 1 ATOM 1106 C CA . SER A 1 141 ? 29.669 -3.675 18.363 1.00 105.42 ? 141 SER A CA 1 ATOM 1107 C C . SER A 1 141 ? 28.851 -4.939 18.089 1.00 104.31 ? 141 SER A C 1 ATOM 1108 O O . SER A 1 141 ? 27.881 -5.218 18.788 1.00 107.45 ? 141 SER A O 1 ATOM 1109 C CB . SER A 1 141 ? 30.500 -3.850 19.635 1.00 106.05 ? 141 SER A CB 1 ATOM 1110 O OG . SER A 1 141 ? 31.365 -2.744 19.831 1.00 106.35 ? 141 SER A OG 1 ATOM 1111 N N . SER A 1 142 ? 29.249 -5.697 17.072 1.00 102.08 ? 142 SER A N 1 ATOM 1112 C CA . SER A 1 142 ? 28.530 -6.905 16.658 1.00 101.56 ? 142 SER A CA 1 ATOM 1113 C C . SER A 1 142 ? 29.526 -8.047 16.424 1.00 99.23 ? 142 SER A C 1 ATOM 1114 O O . SER A 1 142 ? 30.659 -7.985 16.905 1.00 98.44 ? 142 SER A O 1 ATOM 1115 C CB . SER A 1 142 ? 27.718 -6.613 15.388 1.00 101.40 ? 142 SER A CB 1 ATOM 1116 O OG . SER A 1 142 ? 26.687 -7.563 15.200 1.00 102.19 ? 142 SER A OG 1 ATOM 1117 N N . PHE A 1 143 ? 29.108 -9.087 15.701 1.00 97.77 ? 143 PHE A N 1 ATOM 1118 C CA . PHE A 1 143 ? 29.985 -10.231 15.409 1.00 96.08 ? 143 PHE A CA 1 ATOM 1119 C C . PHE A 1 143 ? 29.460 -11.080 14.252 1.00 94.57 ? 143 PHE A C 1 ATOM 1120 O O . PHE A 1 143 ? 28.294 -10.975 13.877 1.00 96.80 ? 143 PHE A O 1 ATOM 1121 C CB . PHE A 1 143 ? 30.138 -11.108 16.659 1.00 97.13 ? 143 PHE A CB 1 ATOM 1122 C CG . PHE A 1 143 ? 31.357 -11.995 16.642 1.00 95.70 ? 143 PHE A CG 1 ATOM 1123 C CD1 . PHE A 1 143 ? 32.634 -11.445 16.610 1.00 94.63 ? 143 PHE A CD1 1 ATOM 1124 C CD2 . PHE A 1 143 ? 31.229 -13.379 16.681 1.00 94.69 ? 143 PHE A CD2 1 ATOM 1125 C CE1 . PHE A 1 143 ? 33.757 -12.258 16.605 1.00 93.60 ? 143 PHE A CE1 1 ATOM 1126 C CE2 . PHE A 1 143 ? 32.350 -14.196 16.676 1.00 93.70 ? 143 PHE A CE2 1 ATOM 1127 C CZ . PHE A 1 143 ? 33.617 -13.635 16.640 1.00 93.01 ? 143 PHE A CZ 1 ATOM 1128 N N . PHE A 1 144 ? 30.334 -11.911 13.687 1.00 92.24 ? 144 PHE A N 1 ATOM 1129 C CA . PHE A 1 144 ? 29.941 -12.908 12.689 1.00 89.83 ? 144 PHE A CA 1 ATOM 1130 C C . PHE A 1 144 ? 28.628 -13.581 13.113 1.00 90.69 ? 144 PHE A C 1 ATOM 1131 O O . PHE A 1 144 ? 28.566 -14.240 14.146 1.00 93.86 ? 144 PHE A O 1 ATOM 1132 C CB . PHE A 1 144 ? 31.027 -13.980 12.527 1.00 89.13 ? 144 PHE A CB 1 ATOM 1133 C CG . PHE A 1 144 ? 32.376 -13.447 12.087 1.00 89.06 ? 144 PHE A CG 1 ATOM 1134 C CD1 . PHE A 1 144 ? 32.565 -12.951 10.804 1.00 88.46 ? 144 PHE A CD1 1 ATOM 1135 C CD2 . PHE A 1 144 ? 33.466 -13.464 12.957 1.00 89.74 ? 144 PHE A CD2 1 ATOM 1136 C CE1 . PHE A 1 144 ? 33.807 -12.476 10.400 1.00 87.69 ? 144 PHE A CE1 1 ATOM 1137 C CE2 . PHE A 1 144 ? 34.707 -12.989 12.558 1.00 88.65 ? 144 PHE A CE2 1 ATOM 1138 C CZ . PHE A 1 144 ? 34.878 -12.495 11.278 1.00 87.68 ? 144 PHE A CZ 1 ATOM 1139 N N . ARG A 1 145 ? 27.586 -13.412 12.309 1.00 89.66 ? 145 ARG A N 1 ATOM 1140 C CA . ARG A 1 145 ? 26.227 -13.808 12.681 1.00 89.67 ? 145 ARG A CA 1 ATOM 1141 C C . ARG A 1 145 ? 25.952 -15.311 12.783 1.00 90.92 ? 145 ARG A C 1 ATOM 1142 O O . ARG A 1 145 ? 24.938 -15.712 13.351 1.00 94.26 ? 145 ARG A O 1 ATOM 1143 C CB . ARG A 1 145 ? 25.233 -13.215 11.684 1.00 88.34 ? 145 ARG A CB 1 ATOM 1144 C CG . ARG A 1 145 ? 25.219 -11.698 11.645 1.00 88.63 ? 145 ARG A CG 1 ATOM 1145 C CD . ARG A 1 145 ? 23.900 -11.219 11.078 1.00 90.03 ? 145 ARG A CD 1 ATOM 1146 N NE . ARG A 1 145 ? 23.852 -9.777 10.857 1.00 90.85 ? 145 ARG A NE 1 ATOM 1147 C CZ . ARG A 1 145 ? 23.631 -8.870 11.804 1.00 93.23 ? 145 ARG A CZ 1 ATOM 1148 N NH1 . ARG A 1 145 ? 23.470 -9.227 13.076 1.00 94.86 ? 145 ARG A NH1 1 ATOM 1149 N NH2 . ARG A 1 145 ? 23.590 -7.586 11.477 1.00 94.71 ? 145 ARG A NH2 1 ATOM 1150 N N . ASN A 1 146 ? 26.824 -16.141 12.224 1.00 91.74 ? 146 ASN A N 1 ATOM 1151 C CA . ASN A 1 146 ? 26.552 -17.578 12.134 1.00 92.29 ? 146 ASN A CA 1 ATOM 1152 C C . ASN A 1 146 ? 27.229 -18.397 13.219 1.00 92.24 ? 146 ASN A C 1 ATOM 1153 O O . ASN A 1 146 ? 26.944 -19.586 13.373 1.00 92.05 ? 146 ASN A O 1 ATOM 1154 C CB . ASN A 1 146 ? 26.940 -18.101 10.746 1.00 90.32 ? 146 ASN A CB 1 ATOM 1155 C CG . ASN A 1 146 ? 26.112 -17.473 9.646 1.00 91.58 ? 146 ASN A CG 1 ATOM 1156 O OD1 . ASN A 1 146 ? 24.930 -17.177 9.842 1.00 95.39 ? 146 ASN A OD1 1 ATOM 1157 N ND2 . ASN A 1 146 ? 26.722 -17.263 8.483 1.00 91.46 ? 146 ASN A ND2 1 ATOM 1158 N N . VAL A 1 147 ? 28.112 -17.758 13.977 1.00 92.96 ? 147 VAL A N 1 ATOM 1159 C CA . VAL A 1 147 ? 28.799 -18.420 15.074 1.00 94.26 ? 147 VAL A CA 1 ATOM 1160 C C . VAL A 1 147 ? 28.631 -17.618 16.361 1.00 95.77 ? 147 VAL A C 1 ATOM 1161 O O . VAL A 1 147 ? 28.444 -16.404 16.324 1.00 96.28 ? 147 VAL A O 1 ATOM 1162 C CB . VAL A 1 147 ? 30.287 -18.642 14.744 1.00 93.83 ? 147 VAL A CB 1 ATOM 1163 C CG1 . VAL A 1 147 ? 30.423 -19.651 13.614 1.00 92.81 ? 147 VAL A CG1 1 ATOM 1164 C CG2 . VAL A 1 147 ? 30.977 -17.334 14.369 1.00 92.83 ? 147 VAL A CG2 1 ATOM 1165 N N . VAL A 1 148 ? 28.689 -18.306 17.493 1.00 98.28 ? 148 VAL A N 1 ATOM 1166 C CA . VAL A 1 148 ? 28.413 -17.696 18.792 1.00 101.03 ? 148 VAL A CA 1 ATOM 1167 C C . VAL A 1 148 ? 29.693 -17.639 19.622 1.00 101.78 ? 148 VAL A C 1 ATOM 1168 O O . VAL A 1 148 ? 30.256 -18.679 19.969 1.00 103.57 ? 148 VAL A O 1 ATOM 1169 C CB . VAL A 1 148 ? 27.342 -18.504 19.557 1.00 104.12 ? 148 VAL A CB 1 ATOM 1170 C CG1 . VAL A 1 148 ? 26.933 -17.791 20.843 1.00 108.13 ? 148 VAL A CG1 1 ATOM 1171 C CG2 . VAL A 1 148 ? 26.126 -18.753 18.675 1.00 103.69 ? 148 VAL A CG2 1 ATOM 1172 N N . TRP A 1 149 ? 30.155 -16.427 19.928 1.00 101.69 ? 149 TRP A N 1 ATOM 1173 C CA . TRP A 1 149 ? 31.327 -16.234 20.784 1.00 102.87 ? 149 TRP A CA 1 ATOM 1174 C C . TRP A 1 149 ? 30.903 -16.344 22.258 1.00 106.53 ? 149 TRP A C 1 ATOM 1175 O O . TRP A 1 149 ? 30.379 -15.391 22.831 1.00 108.88 ? 149 TRP A O 1 ATOM 1176 C CB . TRP A 1 149 ? 31.968 -14.870 20.500 1.00 102.04 ? 149 TRP A CB 1 ATOM 1177 C CG . TRP A 1 149 ? 33.267 -14.599 21.230 1.00 102.76 ? 149 TRP A CG 1 ATOM 1178 C CD1 . TRP A 1 149 ? 33.903 -15.413 22.130 1.00 103.77 ? 149 TRP A CD1 1 ATOM 1179 C CD2 . TRP A 1 149 ? 34.066 -13.413 21.136 1.00 102.15 ? 149 TRP A CD2 1 ATOM 1180 N NE1 . TRP A 1 149 ? 35.055 -14.814 22.579 1.00 104.24 ? 149 TRP A NE1 1 ATOM 1181 C CE2 . TRP A 1 149 ? 35.178 -13.586 21.987 1.00 102.72 ? 149 TRP A CE2 1 ATOM 1182 C CE3 . TRP A 1 149 ? 33.955 -12.224 20.405 1.00 101.69 ? 149 TRP A CE3 1 ATOM 1183 C CZ2 . TRP A 1 149 ? 36.170 -12.616 22.128 1.00 102.37 ? 149 TRP A CZ2 1 ATOM 1184 C CZ3 . TRP A 1 149 ? 34.943 -11.260 20.548 1.00 102.02 ? 149 TRP A CZ3 1 ATOM 1185 C CH2 . TRP A 1 149 ? 36.036 -11.464 21.402 1.00 102.25 ? 149 TRP A CH2 1 ATOM 1186 N N . LEU A 1 150 ? 31.139 -17.506 22.865 1.00 107.58 ? 150 LEU A N 1 ATOM 1187 C CA . LEU A 1 150 ? 30.675 -17.779 24.228 1.00 110.71 ? 150 LEU A CA 1 ATOM 1188 C C . LEU A 1 150 ? 31.684 -17.308 25.268 1.00 112.18 ? 150 LEU A C 1 ATOM 1189 O O . LEU A 1 150 ? 32.887 -17.518 25.098 1.00 111.25 ? 150 LEU A O 1 ATOM 1190 C CB . LEU A 1 150 ? 30.419 -19.277 24.415 1.00 111.66 ? 150 LEU A CB 1 ATOM 1191 C CG . LEU A 1 150 ? 29.320 -19.892 23.540 1.00 111.67 ? 150 LEU A CG 1 ATOM 1192 C CD1 . LEU A 1 150 ? 29.359 -21.413 23.601 1.00 111.88 ? 150 LEU A CD1 1 ATOM 1193 C CD2 . LEU A 1 150 ? 27.946 -19.379 23.947 1.00 113.32 ? 150 LEU A CD2 1 ATOM 1194 N N . ILE A 1 151 ? 31.181 -16.675 26.334 1.00 114.32 ? 151 ILE A N 1 ATOM 1195 C CA . ILE A 1 151 ? 31.993 -16.289 27.501 1.00 115.95 ? 151 ILE A CA 1 ATOM 1196 C C . ILE A 1 151 ? 31.367 -16.785 28.812 1.00 119.13 ? 151 ILE A C 1 ATOM 1197 O O . ILE A 1 151 ? 30.222 -17.241 28.838 1.00 119.11 ? 151 ILE A O 1 ATOM 1198 C CB . ILE A 1 151 ? 32.209 -14.759 27.578 1.00 115.96 ? 151 ILE A CB 1 ATOM 1199 C CG1 . ILE A 1 151 ? 30.917 -14.034 27.976 1.00 117.75 ? 151 ILE A CG1 1 ATOM 1200 C CG2 . ILE A 1 151 ? 32.730 -14.228 26.250 1.00 112.95 ? 151 ILE A CG2 1 ATOM 1201 C CD1 . ILE A 1 151 ? 31.066 -12.532 28.095 1.00 118.59 ? 151 ILE A CD1 1 ATOM 1202 N N . LYS A 1 152 ? 32.128 -16.674 29.898 1.00 122.82 ? 152 LYS A N 1 ATOM 1203 C CA . LYS A 1 152 ? 31.707 -17.174 31.216 1.00 126.91 ? 152 LYS A CA 1 ATOM 1204 C C . LYS A 1 152 ? 30.457 -16.485 31.775 1.00 131.00 ? 152 LYS A C 1 ATOM 1205 O O . LYS A 1 152 ? 30.188 -15.321 31.472 1.00 131.11 ? 152 LYS A O 1 ATOM 1206 C CB . LYS A 1 152 ? 32.853 -17.044 32.227 1.00 128.11 ? 152 LYS A CB 1 ATOM 1207 C CG . LYS A 1 152 ? 33.223 -15.611 32.589 1.00 129.47 ? 152 LYS A CG 1 ATOM 1208 C CD . LYS A 1 152 ? 34.551 -15.553 33.331 1.00 131.07 ? 152 LYS A CD 1 ATOM 1209 C CE . LYS A 1 152 ? 34.998 -14.121 33.584 1.00 131.60 ? 152 LYS A CE 1 ATOM 1210 N NZ . LYS A 1 152 ? 34.232 -13.468 34.676 1.00 135.08 ? 152 LYS A NZ 1 ATOM 1211 N N . LYS A 1 153 ? 29.713 -17.223 32.601 1.00 135.19 ? 153 LYS A N 1 ATOM 1212 C CA . LYS A 1 153 ? 28.499 -16.730 33.256 1.00 138.49 ? 153 LYS A CA 1 ATOM 1213 C C . LYS A 1 153 ? 28.645 -16.876 34.769 1.00 141.05 ? 153 LYS A C 1 ATOM 1214 O O . LYS A 1 153 ? 28.921 -17.971 35.263 1.00 140.28 ? 153 LYS A O 1 ATOM 1215 C CB . LYS A 1 153 ? 27.281 -17.522 32.775 1.00 139.60 ? 153 LYS A CB 1 ATOM 1216 C CG . LYS A 1 153 ? 25.941 -16.921 33.172 1.00 143.82 ? 153 LYS A CG 1 ATOM 1217 C CD . LYS A 1 153 ? 24.823 -17.950 33.075 1.00 145.80 ? 153 LYS A CD 1 ATOM 1218 C CE . LYS A 1 153 ? 23.447 -17.302 33.124 1.00 148.64 ? 153 LYS A CE 1 ATOM 1219 N NZ . LYS A 1 153 ? 23.078 -16.679 31.821 1.00 147.38 ? 153 LYS A NZ 1 ATOM 1220 N N . ASN A 1 154 ? 28.449 -15.773 35.493 1.00 143.57 ? 154 ASN A N 1 ATOM 1221 C CA . ASN A 1 154 ? 28.662 -15.714 36.947 1.00 147.93 ? 154 ASN A CA 1 ATOM 1222 C C . ASN A 1 154 ? 30.052 -16.239 37.351 1.00 147.37 ? 154 ASN A C 1 ATOM 1223 O O . ASN A 1 154 ? 30.189 -16.984 38.322 1.00 148.85 ? 154 ASN A O 1 ATOM 1224 C CB . ASN A 1 154 ? 27.539 -16.457 37.699 1.00 150.43 ? 154 ASN A CB 1 ATOM 1225 C CG . ASN A 1 154 ? 27.411 -16.024 39.157 1.00 156.76 ? 154 ASN A CG 1 ATOM 1226 O OD1 . ASN A 1 154 ? 28.039 -15.057 39.589 1.00 159.30 ? 154 ASN A OD1 1 ATOM 1227 N ND2 . ASN A 1 154 ? 26.590 -16.742 39.924 1.00 159.50 ? 154 ASN A ND2 1 ATOM 1228 N N . SER A 1 155 ? 31.071 -15.836 36.587 1.00 144.11 ? 155 SER A N 1 ATOM 1229 C CA . SER A 1 155 ? 32.467 -16.237 36.817 1.00 143.29 ? 155 SER A CA 1 ATOM 1230 C C . SER A 1 155 ? 32.660 -17.753 36.765 1.00 142.02 ? 155 SER A C 1 ATOM 1231 O O . SER A 1 155 ? 33.346 -18.320 37.611 1.00 146.32 ? 155 SER A O 1 ATOM 1232 C CB . SER A 1 155 ? 32.978 -15.699 38.163 1.00 147.17 ? 155 SER A CB 1 ATOM 1233 O OG . SER A 1 155 ? 32.684 -14.325 38.319 1.00 148.65 ? 155 SER A OG 1 ATOM 1234 N N . THR A 1 156 ? 32.044 -18.410 35.788 1.00 138.64 ? 156 THR A N 1 ATOM 1235 C CA . THR A 1 156 ? 32.197 -19.856 35.625 1.00 137.49 ? 156 THR A CA 1 ATOM 1236 C C . THR A 1 156 ? 32.026 -20.243 34.166 1.00 134.89 ? 156 THR A C 1 ATOM 1237 O O . THR A 1 156 ? 31.029 -19.888 33.538 1.00 136.45 ? 156 THR A O 1 ATOM 1238 C CB . THR A 1 156 ? 31.168 -20.652 36.458 1.00 138.79 ? 156 THR A CB 1 ATOM 1239 O OG1 . THR A 1 156 ? 31.058 -20.084 37.768 1.00 142.90 ? 156 THR A OG1 1 ATOM 1240 C CG2 . THR A 1 156 ? 31.578 -22.119 36.581 1.00 137.45 ? 156 THR A CG2 1 ATOM 1241 N N . TYR A 1 157 ? 33.010 -20.958 33.630 1.00 133.50 ? 157 TYR A N 1 ATOM 1242 C CA . TYR A 1 157 ? 32.902 -21.562 32.310 1.00 129.22 ? 157 TYR A CA 1 ATOM 1243 C C . TYR A 1 157 ? 33.044 -23.069 32.508 1.00 129.21 ? 157 TYR A C 1 ATOM 1244 O O . TYR A 1 157 ? 34.154 -23.604 32.469 1.00 128.30 ? 157 TYR A O 1 ATOM 1245 C CB . TYR A 1 157 ? 33.981 -21.014 31.370 1.00 126.89 ? 157 TYR A CB 1 ATOM 1246 C CG . TYR A 1 157 ? 33.686 -21.200 29.888 1.00 124.31 ? 157 TYR A CG 1 ATOM 1247 C CD1 . TYR A 1 157 ? 33.746 -22.457 29.291 1.00 122.79 ? 157 TYR A CD1 1 ATOM 1248 C CD2 . TYR A 1 157 ? 33.355 -20.112 29.083 1.00 122.83 ? 157 TYR A CD2 1 ATOM 1249 C CE1 . TYR A 1 157 ? 33.483 -22.624 27.938 1.00 120.82 ? 157 TYR A CE1 1 ATOM 1250 C CE2 . TYR A 1 157 ? 33.092 -20.271 27.732 1.00 119.66 ? 157 TYR A CE2 1 ATOM 1251 C CZ . TYR A 1 157 ? 33.156 -21.528 27.162 1.00 118.83 ? 157 TYR A CZ 1 ATOM 1252 O OH . TYR A 1 157 ? 32.897 -21.683 25.817 1.00 115.73 ? 157 TYR A OH 1 ATOM 1253 N N . PRO A 1 158 ? 31.919 -23.759 32.763 1.00 130.44 ? 158 PRO A N 1 ATOM 1254 C CA . PRO A 1 158 ? 31.985 -25.206 32.918 1.00 130.06 ? 158 PRO A CA 1 ATOM 1255 C C . PRO A 1 158 ? 32.108 -25.875 31.559 1.00 125.18 ? 158 PRO A C 1 ATOM 1256 O O . PRO A 1 158 ? 31.773 -25.267 30.539 1.00 122.55 ? 158 PRO A O 1 ATOM 1257 C CB . PRO A 1 158 ? 30.653 -25.548 33.587 1.00 132.89 ? 158 PRO A CB 1 ATOM 1258 C CG . PRO A 1 158 ? 29.716 -24.489 33.118 1.00 132.66 ? 158 PRO A CG 1 ATOM 1259 C CD . PRO A 1 158 ? 30.538 -23.253 32.876 1.00 131.89 ? 158 PRO A CD 1 ATOM 1260 N N . THR A 1 159 ? 32.590 -27.113 31.550 1.00 124.87 ? 159 THR A N 1 ATOM 1261 C CA . THR A 1 159 ? 32.833 -27.836 30.306 1.00 121.95 ? 159 THR A CA 1 ATOM 1262 C C . THR A 1 159 ? 31.552 -27.940 29.475 1.00 121.33 ? 159 THR A C 1 ATOM 1263 O O . THR A 1 159 ? 30.478 -28.232 30.008 1.00 122.35 ? 159 THR A O 1 ATOM 1264 C CB . THR A 1 159 ? 33.394 -29.249 30.577 1.00 121.94 ? 159 THR A CB 1 ATOM 1265 O OG1 . THR A 1 159 ? 34.550 -29.155 31.418 1.00 122.74 ? 159 THR A OG1 1 ATOM 1266 C CG2 . THR A 1 159 ? 33.779 -29.945 29.278 1.00 118.65 ? 159 THR A CG2 1 ATOM 1267 N N . ILE A 1 160 ? 31.683 -27.673 28.177 1.00 119.94 ? 160 ILE A N 1 ATOM 1268 C CA . ILE A 1 160 ? 30.590 -27.798 27.212 1.00 118.93 ? 160 ILE A CA 1 ATOM 1269 C C . ILE A 1 160 ? 30.671 -29.164 26.547 1.00 118.62 ? 160 ILE A C 1 ATOM 1270 O O . ILE A 1 160 ? 31.748 -29.585 26.137 1.00 117.36 ? 160 ILE A O 1 ATOM 1271 C CB . ILE A 1 160 ? 30.690 -26.717 26.111 1.00 115.84 ? 160 ILE A CB 1 ATOM 1272 C CG1 . ILE A 1 160 ? 30.510 -25.326 26.715 1.00 117.49 ? 160 ILE A CG1 1 ATOM 1273 C CG2 . ILE A 1 160 ? 29.644 -26.949 25.028 1.00 114.96 ? 160 ILE A CG2 1 ATOM 1274 C CD1 . ILE A 1 160 ? 30.990 -24.201 25.826 1.00 115.23 ? 160 ILE A CD1 1 ATOM 1275 N N . LYS A 1 161 ? 29.537 -29.853 26.449 1.00 120.50 ? 161 LYS A N 1 ATOM 1276 C CA . LYS A 1 161 ? 29.451 -31.110 25.703 1.00 120.60 ? 161 LYS A CA 1 ATOM 1277 C C . LYS A 1 161 ? 28.165 -31.120 24.894 1.00 120.18 ? 161 LYS A C 1 ATOM 1278 O O . LYS A 1 161 ? 27.114 -31.524 25.392 1.00 122.72 ? 161 LYS A O 1 ATOM 1279 C CB . LYS A 1 161 ? 29.484 -32.320 26.641 1.00 124.98 ? 161 LYS A CB 1 ATOM 1280 C CG . LYS A 1 161 ? 30.836 -32.602 27.277 1.00 127.31 ? 161 LYS A CG 1 ATOM 1281 C CD . LYS A 1 161 ? 30.761 -33.783 28.236 1.00 130.70 ? 161 LYS A CD 1 ATOM 1282 C CE . LYS A 1 161 ? 32.015 -33.899 29.090 1.00 132.91 ? 161 LYS A CE 1 ATOM 1283 N NZ . LYS A 1 161 ? 31.866 -34.896 30.187 1.00 137.19 ? 161 LYS A NZ 1 ATOM 1284 N N . ARG A 1 162 ? 28.253 -30.664 23.650 1.00 118.57 ? 162 ARG A N 1 ATOM 1285 C CA . ARG A 1 162 ? 27.096 -30.583 22.773 1.00 118.38 ? 162 ARG A CA 1 ATOM 1286 C C . ARG A 1 162 ? 27.357 -31.400 21.526 1.00 116.52 ? 162 ARG A C 1 ATOM 1287 O O . ARG A 1 162 ? 28.500 -31.520 21.082 1.00 115.13 ? 162 ARG A O 1 ATOM 1288 C CB . ARG A 1 162 ? 26.809 -29.130 22.403 1.00 118.55 ? 162 ARG A CB 1 ATOM 1289 C CG . ARG A 1 162 ? 26.577 -28.223 23.604 1.00 122.89 ? 162 ARG A CG 1 ATOM 1290 C CD . ARG A 1 162 ? 25.251 -28.501 24.295 1.00 126.68 ? 162 ARG A CD 1 ATOM 1291 N NE . ARG A 1 162 ? 24.118 -28.105 23.459 1.00 127.17 ? 162 ARG A NE 1 ATOM 1292 C CZ . ARG A 1 162 ? 23.551 -26.897 23.448 1.00 127.29 ? 162 ARG A CZ 1 ATOM 1293 N NH1 . ARG A 1 162 ? 23.990 -25.916 24.234 1.00 127.75 ? 162 ARG A NH1 1 ATOM 1294 N NH2 . ARG A 1 162 ? 22.528 -26.670 22.636 1.00 127.10 ? 162 ARG A NH2 1 ATOM 1295 N N . SER A 1 163 ? 26.288 -31.952 20.960 1.00 115.57 ? 163 SER A N 1 ATOM 1296 C CA . SER A 1 163 ? 26.398 -32.886 19.853 1.00 112.63 ? 163 SER A CA 1 ATOM 1297 C C . SER A 1 163 ? 25.242 -32.719 18.865 1.00 111.87 ? 163 SER A C 1 ATOM 1298 O O . SER A 1 163 ? 24.083 -32.833 19.250 1.00 112.65 ? 163 SER A O 1 ATOM 1299 C CB . SER A 1 163 ? 26.413 -34.311 20.403 1.00 113.48 ? 163 SER A CB 1 ATOM 1300 O OG . SER A 1 163 ? 26.648 -35.255 19.377 1.00 115.40 ? 163 SER A OG 1 ATOM 1301 N N . TYR A 1 164 ? 25.556 -32.441 17.598 1.00 109.61 ? 164 TYR A N 1 ATOM 1302 C CA . TYR A 1 164 ? 24.527 -32.371 16.561 1.00 109.31 ? 164 TYR A CA 1 ATOM 1303 C C . TYR A 1 164 ? 24.599 -33.570 15.621 1.00 110.96 ? 164 TYR A C 1 ATOM 1304 O O . TYR A 1 164 ? 25.681 -34.026 15.258 1.00 110.27 ? 164 TYR A O 1 ATOM 1305 C CB . TYR A 1 164 ? 24.621 -31.081 15.751 1.00 105.96 ? 164 TYR A CB 1 ATOM 1306 C CG . TYR A 1 164 ? 23.667 -31.089 14.580 1.00 106.58 ? 164 TYR A CG 1 ATOM 1307 C CD1 . TYR A 1 164 ? 22.300 -30.923 14.768 1.00 109.12 ? 164 TYR A CD1 1 ATOM 1308 C CD2 . TYR A 1 164 ? 24.127 -31.313 13.287 1.00 107.44 ? 164 TYR A CD2 1 ATOM 1309 C CE1 . TYR A 1 164 ? 21.420 -30.951 13.699 1.00 110.05 ? 164 TYR A CE1 1 ATOM 1310 C CE2 . TYR A 1 164 ? 23.257 -31.343 12.210 1.00 108.32 ? 164 TYR A CE2 1 ATOM 1311 C CZ . TYR A 1 164 ? 21.906 -31.161 12.419 1.00 110.06 ? 164 TYR A CZ 1 ATOM 1312 O OH . TYR A 1 164 ? 21.053 -31.193 11.342 1.00 111.73 ? 164 TYR A OH 1 ATOM 1313 N N . ASN A 1 165 ? 23.426 -34.049 15.219 1.00 114.23 ? 165 ASN A N 1 ATOM 1314 C CA . ASN A 1 165 ? 23.287 -35.211 14.360 1.00 116.95 ? 165 ASN A CA 1 ATOM 1315 C C . ASN A 1 165 ? 22.637 -34.792 13.050 1.00 115.96 ? 165 ASN A C 1 ATOM 1316 O O . ASN A 1 165 ? 21.537 -34.241 13.052 1.00 118.16 ? 165 ASN A O 1 ATOM 1317 C CB . ASN A 1 165 ? 22.425 -36.244 15.079 1.00 122.80 ? 165 ASN A CB 1 ATOM 1318 C CG . ASN A 1 165 ? 22.120 -37.469 14.234 1.00 127.38 ? 165 ASN A CG 1 ATOM 1319 O OD1 . ASN A 1 165 ? 21.767 -37.372 13.060 1.00 123.88 ? 165 ASN A OD1 1 ATOM 1320 N ND2 . ASN A 1 165 ? 22.243 -38.642 14.850 1.00 136.42 ? 165 ASN A ND2 1 ATOM 1321 N N . ASN A 1 166 ? 23.315 -35.054 11.936 1.00 113.09 ? 166 ASN A N 1 ATOM 1322 C CA . ASN A 1 166 ? 22.787 -34.687 10.628 1.00 111.44 ? 166 ASN A CA 1 ATOM 1323 C C . ASN A 1 166 ? 21.722 -35.672 10.165 1.00 112.71 ? 166 ASN A C 1 ATOM 1324 O O . ASN A 1 166 ? 22.029 -36.689 9.532 1.00 110.52 ? 166 ASN A O 1 ATOM 1325 C CB . ASN A 1 166 ? 23.904 -34.596 9.587 1.00 108.78 ? 166 ASN A CB 1 ATOM 1326 C CG . ASN A 1 166 ? 23.416 -34.040 8.263 1.00 108.33 ? 166 ASN A CG 1 ATOM 1327 O OD1 . ASN A 1 166 ? 22.377 -33.375 8.201 1.00 108.47 ? 166 ASN A OD1 1 ATOM 1328 N ND2 . ASN A 1 166 ? 24.164 -34.309 7.193 1.00 106.03 ? 166 ASN A ND2 1 ATOM 1329 N N . THR A 1 167 ? 20.470 -35.355 10.491 1.00 114.00 ? 167 THR A N 1 ATOM 1330 C CA . THR A 1 167 ? 19.321 -36.140 10.041 1.00 116.18 ? 167 THR A CA 1 ATOM 1331 C C . THR A 1 167 ? 18.820 -35.705 8.655 1.00 116.52 ? 167 THR A C 1 ATOM 1332 O O . THR A 1 167 ? 17.922 -36.337 8.095 1.00 118.84 ? 167 THR A O 1 ATOM 1333 C CB . THR A 1 167 ? 18.155 -36.063 11.049 1.00 117.92 ? 167 THR A CB 1 ATOM 1334 O OG1 . THR A 1 167 ? 17.742 -34.701 11.213 1.00 116.97 ? 167 THR A OG1 1 ATOM 1335 C CG2 . THR A 1 167 ? 18.579 -36.632 12.394 1.00 117.79 ? 167 THR A CG2 1 ATOM 1336 N N . ASN A 1 168 ? 19.401 -34.639 8.103 1.00 113.36 ? 168 ASN A N 1 ATOM 1337 C CA . ASN A 1 168 ? 19.061 -34.193 6.755 1.00 110.83 ? 168 ASN A CA 1 ATOM 1338 C C . ASN A 1 168 ? 19.600 -35.155 5.715 1.00 109.34 ? 168 ASN A C 1 ATOM 1339 O O . ASN A 1 168 ? 20.598 -35.833 5.953 1.00 112.14 ? 168 ASN A O 1 ATOM 1340 C CB . ASN A 1 168 ? 19.643 -32.811 6.473 1.00 108.62 ? 168 ASN A CB 1 ATOM 1341 C CG . ASN A 1 168 ? 19.116 -31.753 7.415 1.00 108.20 ? 168 ASN A CG 1 ATOM 1342 O OD1 . ASN A 1 168 ? 17.977 -31.299 7.276 1.00 109.76 ? 168 ASN A OD1 1 ATOM 1343 N ND2 . ASN A 1 168 ? 19.946 -31.340 8.371 1.00 105.45 ? 168 ASN A ND2 1 ATOM 1344 N N . GLN A 1 169 ? 18.946 -35.203 4.560 1.00 107.20 ? 169 GLN A N 1 ATOM 1345 C CA . GLN A 1 169 ? 19.441 -35.995 3.434 1.00 106.29 ? 169 GLN A CA 1 ATOM 1346 C C . GLN A 1 169 ? 20.751 -35.432 2.845 1.00 102.96 ? 169 GLN A C 1 ATOM 1347 O O . GLN A 1 169 ? 21.542 -36.182 2.276 1.00 100.68 ? 169 GLN A O 1 ATOM 1348 C CB . GLN A 1 169 ? 18.382 -36.084 2.324 1.00 107.37 ? 169 GLN A CB 1 ATOM 1349 C CG . GLN A 1 169 ? 17.523 -37.344 2.320 1.00 108.39 ? 169 GLN A CG 1 ATOM 1350 C CD . GLN A 1 169 ? 17.295 -37.874 0.902 1.00 109.17 ? 169 GLN A CD 1 ATOM 1351 O OE1 . GLN A 1 169 ? 16.203 -37.752 0.344 1.00 109.27 ? 169 GLN A OE1 1 ATOM 1352 N NE2 . GLN A 1 169 ? 18.340 -38.446 0.306 1.00 107.00 ? 169 GLN A NE2 1 ATOM 1353 N N . GLU A 1 170 ? 20.976 -34.126 3.002 1.00 101.04 ? 170 GLU A N 1 ATOM 1354 C CA . GLU A 1 170 ? 22.065 -33.414 2.319 1.00 97.92 ? 170 GLU A CA 1 ATOM 1355 C C . GLU A 1 170 ? 23.293 -33.165 3.190 1.00 96.56 ? 170 GLU A C 1 ATOM 1356 O O . GLU A 1 170 ? 23.157 -32.796 4.355 1.00 98.70 ? 170 GLU A O 1 ATOM 1357 C CB . GLU A 1 170 ? 21.566 -32.057 1.828 1.00 96.87 ? 170 GLU A CB 1 ATOM 1358 C CG . GLU A 1 170 ? 20.307 -32.119 0.980 1.00 98.71 ? 170 GLU A CG 1 ATOM 1359 C CD . GLU A 1 170 ? 19.039 -31.940 1.784 1.00 100.24 ? 170 GLU A CD 1 ATOM 1360 O OE1 . GLU A 1 170 ? 19.004 -32.358 2.961 1.00 103.63 ? 170 GLU A OE1 1 ATOM 1361 O OE2 . GLU A 1 170 ? 18.072 -31.382 1.236 1.00 98.86 ? 170 GLU A OE2 1 ATOM 1362 N N . ASP A 1 171 ? 24.482 -33.363 2.614 1.00 95.56 ? 171 ASP A N 1 ATOM 1363 C CA . ASP A 1 171 ? 25.756 -32.996 3.244 1.00 93.94 ? 171 ASP A CA 1 ATOM 1364 C C . ASP A 1 171 ? 25.625 -31.628 3.889 1.00 92.60 ? 171 ASP A C 1 ATOM 1365 O O . ASP A 1 171 ? 24.990 -30.735 3.326 1.00 92.08 ? 171 ASP A O 1 ATOM 1366 C CB . ASP A 1 171 ? 26.892 -32.899 2.204 1.00 95.13 ? 171 ASP A CB 1 ATOM 1367 C CG . ASP A 1 171 ? 27.382 -34.257 1.695 1.00 96.27 ? 171 ASP A CG 1 ATOM 1368 O OD1 . ASP A 1 171 ? 27.308 -35.271 2.419 1.00 100.22 ? 171 ASP A OD1 1 ATOM 1369 O OD2 . ASP A 1 171 ? 27.882 -34.294 0.554 1.00 96.67 ? 171 ASP A OD2 1 ATOM 1370 N N . LEU A 1 172 ? 26.249 -31.458 5.050 1.00 92.98 ? 172 LEU A N 1 ATOM 1371 C CA . LEU A 1 172 ? 26.160 -30.212 5.796 1.00 93.41 ? 172 LEU A CA 1 ATOM 1372 C C . LEU A 1 172 ? 27.537 -29.586 5.989 1.00 91.06 ? 172 LEU A C 1 ATOM 1373 O O . LEU A 1 172 ? 28.468 -30.254 6.435 1.00 90.33 ? 172 LEU A O 1 ATOM 1374 C CB . LEU A 1 172 ? 25.518 -30.476 7.159 1.00 96.45 ? 172 LEU A CB 1 ATOM 1375 C CG . LEU A 1 172 ? 25.103 -29.233 7.957 1.00 98.86 ? 172 LEU A CG 1 ATOM 1376 C CD1 . LEU A 1 172 ? 23.818 -28.627 7.408 1.00 99.75 ? 172 LEU A CD1 1 ATOM 1377 C CD2 . LEU A 1 172 ? 24.937 -29.568 9.433 1.00 101.48 ? 172 LEU A CD2 1 ATOM 1378 N N . LEU A 1 173 ? 27.657 -28.304 5.650 1.00 89.64 ? 173 LEU A N 1 ATOM 1379 C CA . LEU A 1 173 ? 28.871 -27.540 5.923 1.00 88.44 ? 173 LEU A CA 1 ATOM 1380 C C . LEU A 1 173 ? 28.760 -26.890 7.285 1.00 89.25 ? 173 LEU A C 1 ATOM 1381 O O . LEU A 1 173 ? 27.919 -26.023 7.486 1.00 91.30 ? 173 LEU A O 1 ATOM 1382 C CB . LEU A 1 173 ? 29.081 -26.447 4.878 1.00 88.41 ? 173 LEU A CB 1 ATOM 1383 C CG . LEU A 1 173 ? 30.233 -25.468 5.153 1.00 87.94 ? 173 LEU A CG 1 ATOM 1384 C CD1 . LEU A 1 173 ? 31.539 -26.214 5.383 1.00 88.24 ? 173 LEU A CD1 1 ATOM 1385 C CD2 . LEU A 1 173 ? 30.387 -24.477 4.010 1.00 86.87 ? 173 LEU A CD2 1 ATOM 1386 N N . VAL A 1 174 ? 29.624 -27.297 8.210 1.00 89.86 ? 174 VAL A N 1 ATOM 1387 C CA . VAL A 1 174 ? 29.642 -26.745 9.560 1.00 88.60 ? 174 VAL A CA 1 ATOM 1388 C C . VAL A 1 174 ? 30.886 -25.883 9.753 1.00 86.68 ? 174 VAL A C 1 ATOM 1389 O O . VAL A 1 174 ? 31.988 -26.282 9.370 1.00 85.25 ? 174 VAL A O 1 ATOM 1390 C CB . VAL A 1 174 ? 29.639 -27.860 10.622 1.00 89.58 ? 174 VAL A CB 1 ATOM 1391 C CG1 . VAL A 1 174 ? 29.410 -27.270 12.005 1.00 91.69 ? 174 VAL A CG1 1 ATOM 1392 C CG2 . VAL A 1 174 ? 28.578 -28.901 10.297 1.00 90.20 ? 174 VAL A CG2 1 ATOM 1393 N N . LEU A 1 175 ? 30.692 -24.710 10.352 1.00 86.17 ? 175 LEU A N 1 ATOM 1394 C CA . LEU A 1 175 ? 31.775 -23.783 10.659 1.00 85.78 ? 175 LEU A CA 1 ATOM 1395 C C . LEU A 1 175 ? 31.853 -23.564 12.159 1.00 86.72 ? 175 LEU A C 1 ATOM 1396 O O . LEU A 1 175 ? 30.827 -23.408 12.815 1.00 87.43 ? 175 LEU A O 1 ATOM 1397 C CB . LEU A 1 175 ? 31.523 -22.433 9.993 1.00 85.72 ? 175 LEU A CB 1 ATOM 1398 C CG . LEU A 1 175 ? 31.397 -22.423 8.471 1.00 86.77 ? 175 LEU A CG 1 ATOM 1399 C CD1 . LEU A 1 175 ? 30.853 -21.085 7.985 1.00 87.37 ? 175 LEU A CD1 1 ATOM 1400 C CD2 . LEU A 1 175 ? 32.737 -22.731 7.823 1.00 85.21 ? 175 LEU A CD2 1 ATOM 1401 N N . TRP A 1 176 ? 33.068 -23.549 12.695 1.00 86.39 ? 176 TRP A N 1 ATOM 1402 C CA . TRP A 1 176 ? 33.299 -23.125 14.073 1.00 88.49 ? 176 TRP A CA 1 ATOM 1403 C C . TRP A 1 176 ? 34.631 -22.388 14.163 1.00 87.94 ? 176 TRP A C 1 ATOM 1404 O O . TRP A 1 176 ? 35.299 -22.184 13.153 1.00 86.06 ? 176 TRP A O 1 ATOM 1405 C CB . TRP A 1 176 ? 33.256 -24.321 15.035 1.00 90.45 ? 176 TRP A CB 1 ATOM 1406 C CG . TRP A 1 176 ? 34.384 -25.287 14.870 1.00 90.59 ? 176 TRP A CG 1 ATOM 1407 C CD1 . TRP A 1 176 ? 35.518 -25.362 15.625 1.00 91.19 ? 176 TRP A CD1 1 ATOM 1408 C CD2 . TRP A 1 176 ? 34.486 -26.323 13.888 1.00 89.69 ? 176 TRP A CD2 1 ATOM 1409 N NE1 . TRP A 1 176 ? 36.324 -26.380 15.173 1.00 90.50 ? 176 TRP A NE1 1 ATOM 1410 C CE2 . TRP A 1 176 ? 35.712 -26.988 14.109 1.00 89.75 ? 176 TRP A CE2 1 ATOM 1411 C CE3 . TRP A 1 176 ? 33.659 -26.754 12.843 1.00 88.62 ? 176 TRP A CE3 1 ATOM 1412 C CZ2 . TRP A 1 176 ? 36.131 -28.059 13.323 1.00 89.19 ? 176 TRP A CZ2 1 ATOM 1413 C CZ3 . TRP A 1 176 ? 34.074 -27.818 12.065 1.00 88.64 ? 176 TRP A CZ3 1 ATOM 1414 C CH2 . TRP A 1 176 ? 35.302 -28.458 12.305 1.00 88.99 ? 176 TRP A CH2 1 ATOM 1415 N N . GLY A 1 177 ? 35.012 -21.976 15.367 1.00 91.34 ? 177 GLY A N 1 ATOM 1416 C CA . GLY A 1 177 ? 36.269 -21.252 15.548 1.00 91.81 ? 177 GLY A CA 1 ATOM 1417 C C . GLY A 1 177 ? 36.806 -21.257 16.962 1.00 92.66 ? 177 GLY A C 1 ATOM 1418 O O . GLY A 1 177 ? 36.123 -21.665 17.901 1.00 94.32 ? 177 GLY A O 1 ATOM 1419 N N . ILE A 1 178 ? 38.043 -20.794 17.093 1.00 92.52 ? 178 ILE A N 1 ATOM 1420 C CA . ILE A 1 178 ? 38.703 -20.657 18.382 1.00 95.20 ? 178 ILE A CA 1 ATOM 1421 C C . ILE A 1 178 ? 39.206 -19.222 18.517 1.00 96.28 ? 178 ILE A C 1 ATOM 1422 O O . ILE A 1 178 ? 39.604 -18.604 17.530 1.00 94.19 ? 178 ILE A O 1 ATOM 1423 C CB . ILE A 1 178 ? 39.869 -21.665 18.540 1.00 95.87 ? 178 ILE A CB 1 ATOM 1424 C CG1 . ILE A 1 178 ? 40.411 -21.650 19.972 1.00 98.82 ? 178 ILE A CG1 1 ATOM 1425 C CG2 . ILE A 1 178 ? 40.997 -21.377 17.556 1.00 94.40 ? 178 ILE A CG2 1 ATOM 1426 C CD1 . ILE A 1 178 ? 41.378 -22.775 20.273 1.00 100.24 ? 178 ILE A CD1 1 ATOM 1427 N N . HIS A 1 179 ? 39.170 -18.694 19.738 1.00 98.42 ? 179 HIS A N 1 ATOM 1428 C CA . HIS A 1 179 ? 39.684 -17.358 20.016 1.00 100.28 ? 179 HIS A CA 1 ATOM 1429 C C . HIS A 1 179 ? 41.035 -17.437 20.722 1.00 102.46 ? 179 HIS A C 1 ATOM 1430 O O . HIS A 1 179 ? 41.176 -18.116 21.745 1.00 104.47 ? 179 HIS A O 1 ATOM 1431 C CB . HIS A 1 179 ? 38.698 -16.567 20.878 1.00 101.86 ? 179 HIS A CB 1 ATOM 1432 C CG . HIS A 1 179 ? 39.245 -15.267 21.375 1.00 102.39 ? 179 HIS A CG 1 ATOM 1433 N ND1 . HIS A 1 179 ? 39.322 -14.955 22.715 1.00 105.81 ? 179 HIS A ND1 1 ATOM 1434 C CD2 . HIS A 1 179 ? 39.764 -14.207 20.713 1.00 101.71 ? 179 HIS A CD2 1 ATOM 1435 C CE1 . HIS A 1 179 ? 39.849 -13.753 22.857 1.00 106.64 ? 179 HIS A CE1 1 ATOM 1436 N NE2 . HIS A 1 179 ? 40.127 -13.277 21.657 1.00 104.89 ? 179 HIS A NE2 1 ATOM 1437 N N . HIS A 1 180 ? 42.022 -16.740 20.168 1.00 101.92 ? 180 HIS A N 1 ATOM 1438 C CA . HIS A 1 180 ? 43.319 -16.612 20.806 1.00 104.51 ? 180 HIS A CA 1 ATOM 1439 C C . HIS A 1 180 ? 43.331 -15.301 21.573 1.00 106.51 ? 180 HIS A C 1 ATOM 1440 O O . HIS A 1 180 ? 43.220 -14.234 20.971 1.00 105.75 ? 180 HIS A O 1 ATOM 1441 C CB . HIS A 1 180 ? 44.439 -16.627 19.773 1.00 104.10 ? 180 HIS A CB 1 ATOM 1442 C CG . HIS A 1 180 ? 44.448 -17.855 18.921 1.00 104.36 ? 180 HIS A CG 1 ATOM 1443 N ND1 . HIS A 1 180 ? 44.235 -19.115 19.434 1.00 106.55 ? 180 HIS A ND1 1 ATOM 1444 C CD2 . HIS A 1 180 ? 44.643 -18.018 17.592 1.00 103.37 ? 180 HIS A CD2 1 ATOM 1445 C CE1 . HIS A 1 180 ? 44.296 -20.003 18.458 1.00 103.97 ? 180 HIS A CE1 1 ATOM 1446 N NE2 . HIS A 1 180 ? 44.543 -19.363 17.330 1.00 102.81 ? 180 HIS A NE2 1 ATOM 1447 N N . PRO A 1 181 ? 43.453 -15.373 22.907 1.00 108.97 ? 181 PRO A N 1 ATOM 1448 C CA . PRO A 1 181 ? 43.470 -14.158 23.699 1.00 110.70 ? 181 PRO A CA 1 ATOM 1449 C C . PRO A 1 181 ? 44.823 -13.460 23.623 1.00 110.35 ? 181 PRO A C 1 ATOM 1450 O O . PRO A 1 181 ? 45.794 -14.022 23.112 1.00 108.19 ? 181 PRO A O 1 ATOM 1451 C CB . PRO A 1 181 ? 43.214 -14.671 25.113 1.00 114.36 ? 181 PRO A CB 1 ATOM 1452 C CG . PRO A 1 181 ? 43.852 -16.016 25.126 1.00 114.47 ? 181 PRO A CG 1 ATOM 1453 C CD . PRO A 1 181 ? 43.667 -16.572 23.739 1.00 111.08 ? 181 PRO A CD 1 ATOM 1454 N N . ASN A 1 182 ? 44.880 -12.246 24.147 1.00 112.24 ? 182 ASN A N 1 ATOM 1455 C CA . ASN A 1 182 ? 46.098 -11.458 24.094 1.00 113.55 ? 182 ASN A CA 1 ATOM 1456 C C . ASN A 1 182 ? 47.160 -11.907 25.096 1.00 115.65 ? 182 ASN A C 1 ATOM 1457 O O . ASN A 1 182 ? 48.321 -12.111 24.731 1.00 115.39 ? 182 ASN A O 1 ATOM 1458 C CB . ASN A 1 182 ? 45.781 -9.987 24.329 1.00 115.43 ? 182 ASN A CB 1 ATOM 1459 C CG . ASN A 1 182 ? 46.579 -9.095 23.429 1.00 115.40 ? 182 ASN A CG 1 ATOM 1460 O OD1 . ASN A 1 182 ? 46.323 -9.061 22.233 1.00 112.85 ? 182 ASN A OD1 1 ATOM 1461 N ND2 . ASN A 1 182 ? 47.575 -8.403 23.983 1.00 117.89 ? 182 ASN A ND2 1 ATOM 1462 N N . ASP A 1 183 ? 46.750 -12.044 26.357 1.00 117.11 ? 183 ASP A N 1 ATOM 1463 C CA . ASP A 1 183 ? 47.664 -12.377 27.452 1.00 119.81 ? 183 ASP A CA 1 ATOM 1464 C C . ASP A 1 183 ? 47.011 -13.325 28.462 1.00 119.51 ? 183 ASP A C 1 ATOM 1465 O O . ASP A 1 183 ? 45.830 -13.661 28.342 1.00 116.87 ? 183 ASP A O 1 ATOM 1466 C CB . ASP A 1 183 ? 48.167 -11.093 28.145 1.00 123.05 ? 183 ASP A CB 1 ATOM 1467 C CG . ASP A 1 183 ? 47.035 -10.169 28.602 1.00 124.21 ? 183 ASP A CG 1 ATOM 1468 O OD1 . ASP A 1 183 ? 45.968 -10.663 29.025 1.00 125.02 ? 183 ASP A OD1 1 ATOM 1469 O OD2 . ASP A 1 183 ? 47.225 -8.936 28.555 1.00 124.95 ? 183 ASP A OD2 1 ATOM 1470 N N . ALA A 1 184 ? 47.789 -13.750 29.456 1.00 121.32 ? 184 ALA A N 1 ATOM 1471 C CA . ALA A 1 184 ? 47.292 -14.637 30.516 1.00 123.13 ? 184 ALA A CA 1 ATOM 1472 C C . ALA A 1 184 ? 46.098 -14.048 31.286 1.00 124.72 ? 184 ALA A C 1 ATOM 1473 O O . ALA A 1 184 ? 45.228 -14.790 31.753 1.00 124.12 ? 184 ALA A O 1 ATOM 1474 C CB . ALA A 1 184 ? 48.419 -14.994 31.478 1.00 124.51 ? 184 ALA A CB 1 ATOM 1475 N N . ALA A 1 185 ? 46.061 -12.721 31.405 1.00 126.05 ? 185 ALA A N 1 ATOM 1476 C CA . ALA A 1 185 ? 44.993 -12.023 32.127 1.00 127.52 ? 185 ALA A CA 1 ATOM 1477 C C . ALA A 1 185 ? 43.669 -11.999 31.360 1.00 124.77 ? 185 ALA A C 1 ATOM 1478 O O . ALA A 1 185 ? 42.600 -12.107 31.961 1.00 125.33 ? 185 ALA A O 1 ATOM 1479 C CB . ALA A 1 185 ? 45.428 -10.604 32.460 1.00 129.60 ? 185 ALA A CB 1 ATOM 1480 N N . GLU A 1 186 ? 43.739 -11.850 30.040 1.00 122.06 ? 186 GLU A N 1 ATOM 1481 C CA . GLU A 1 186 ? 42.530 -11.798 29.212 1.00 120.08 ? 186 GLU A CA 1 ATOM 1482 C C . GLU A 1 186 ? 41.837 -13.160 29.124 1.00 118.13 ? 186 GLU A C 1 ATOM 1483 O O . GLU A 1 186 ? 40.612 -13.232 28.996 1.00 116.46 ? 186 GLU A O 1 ATOM 1484 C CB . GLU A 1 186 ? 42.854 -11.281 27.809 1.00 118.14 ? 186 GLU A CB 1 ATOM 1485 C CG . GLU A 1 186 ? 41.627 -10.831 27.031 1.00 117.42 ? 186 GLU A CG 1 ATOM 1486 C CD . GLU A 1 186 ? 41.981 -10.120 25.737 1.00 116.08 ? 186 GLU A CD 1 ATOM 1487 O OE1 . GLU A 1 186 ? 42.423 -10.792 24.774 1.00 114.22 ? 186 GLU A OE1 1 ATOM 1488 O OE2 . GLU A 1 186 ? 41.802 -8.885 25.682 1.00 116.48 ? 186 GLU A OE2 1 ATOM 1489 N N . GLN A 1 187 ? 42.627 -14.230 29.185 1.00 117.56 ? 187 GLN A N 1 ATOM 1490 C CA . GLN A 1 187 ? 42.098 -15.592 29.246 1.00 116.74 ? 187 GLN A CA 1 ATOM 1491 C C . GLN A 1 187 ? 41.166 -15.752 30.448 1.00 119.90 ? 187 GLN A C 1 ATOM 1492 O O . GLN A 1 187 ? 40.030 -16.209 30.304 1.00 118.95 ? 187 GLN A O 1 ATOM 1493 C CB . GLN A 1 187 ? 43.248 -16.605 29.332 1.00 116.17 ? 187 GLN A CB 1 ATOM 1494 C CG . GLN A 1 187 ? 42.822 -18.057 29.514 1.00 115.39 ? 187 GLN A CG 1 ATOM 1495 C CD . GLN A 1 187 ? 42.055 -18.609 28.324 1.00 111.37 ? 187 GLN A CD 1 ATOM 1496 O OE1 . GLN A 1 187 ? 42.425 -18.383 27.175 1.00 108.01 ? 187 GLN A OE1 1 ATOM 1497 N NE2 . GLN A 1 187 ? 40.988 -19.352 28.598 1.00 111.10 ? 187 GLN A NE2 1 ATOM 1498 N N . THR A 1 188 ? 41.651 -15.372 31.629 1.00 123.74 ? 188 THR A N 1 ATOM 1499 C CA . THR A 1 188 ? 40.850 -15.473 32.848 1.00 126.41 ? 188 THR A CA 1 ATOM 1500 C C . THR A 1 188 ? 39.675 -14.491 32.801 1.00 126.02 ? 188 THR A C 1 ATOM 1501 O O . THR A 1 188 ? 38.556 -14.829 33.183 1.00 127.12 ? 188 THR A O 1 ATOM 1502 C CB . THR A 1 188 ? 41.687 -15.226 34.125 1.00 130.80 ? 188 THR A CB 1 ATOM 1503 O OG1 . THR A 1 188 ? 42.235 -13.903 34.106 1.00 132.56 ? 188 THR A OG1 1 ATOM 1504 C CG2 . THR A 1 188 ? 42.818 -16.244 34.241 1.00 131.04 ? 188 THR A CG2 1 ATOM 1505 N N . LYS A 1 189 ? 39.934 -13.285 32.305 1.00 124.39 ? 189 LYS A N 1 ATOM 1506 C CA . LYS A 1 189 ? 38.917 -12.237 32.230 1.00 124.88 ? 189 LYS A CA 1 ATOM 1507 C C . LYS A 1 189 ? 37.699 -12.629 31.375 1.00 123.67 ? 189 LYS A C 1 ATOM 1508 O O . LYS A 1 189 ? 36.593 -12.158 31.637 1.00 124.60 ? 189 LYS A O 1 ATOM 1509 C CB . LYS A 1 189 ? 39.563 -10.944 31.716 1.00 124.76 ? 189 LYS A CB 1 ATOM 1510 C CG . LYS A 1 189 ? 38.616 -9.797 31.396 1.00 125.50 ? 189 LYS A CG 1 ATOM 1511 C CD . LYS A 1 189 ? 39.398 -8.518 31.111 1.00 126.32 ? 189 LYS A CD 1 ATOM 1512 C CE . LYS A 1 189 ? 39.055 -7.916 29.755 1.00 123.76 ? 189 LYS A CE 1 ATOM 1513 N NZ . LYS A 1 189 ? 37.620 -7.543 29.631 1.00 124.52 ? 189 LYS A NZ 1 ATOM 1514 N N . LEU A 1 190 ? 37.903 -13.489 30.372 1.00 120.59 ? 190 LEU A N 1 ATOM 1515 C CA . LEU A 1 190 ? 36.820 -13.938 29.476 1.00 119.06 ? 190 LEU A CA 1 ATOM 1516 C C . LEU A 1 190 ? 36.292 -15.337 29.807 1.00 119.81 ? 190 LEU A C 1 ATOM 1517 O O . LEU A 1 190 ? 35.081 -15.567 29.804 1.00 119.42 ? 190 LEU A O 1 ATOM 1518 C CB . LEU A 1 190 ? 37.286 -13.913 28.010 1.00 115.09 ? 190 LEU A CB 1 ATOM 1519 C CG . LEU A 1 190 ? 37.110 -12.596 27.246 1.00 113.84 ? 190 LEU A CG 1 ATOM 1520 C CD1 . LEU A 1 190 ? 37.566 -11.393 28.064 1.00 117.01 ? 190 LEU A CD1 1 ATOM 1521 C CD2 . LEU A 1 190 ? 37.861 -12.660 25.928 1.00 110.26 ? 190 LEU A CD2 1 ATOM 1522 N N . TYR A 1 191 ? 37.207 -16.266 30.073 1.00 121.05 ? 191 TYR A N 1 ATOM 1523 C CA . TYR A 1 191 ? 36.868 -17.686 30.230 1.00 121.36 ? 191 TYR A CA 1 ATOM 1524 C C . TYR A 1 191 ? 37.207 -18.274 31.609 1.00 125.57 ? 191 TYR A C 1 ATOM 1525 O O . TYR A 1 191 ? 36.792 -19.391 31.929 1.00 127.28 ? 191 TYR A O 1 ATOM 1526 C CB . TYR A 1 191 ? 37.586 -18.482 29.141 1.00 118.74 ? 191 TYR A CB 1 ATOM 1527 C CG . TYR A 1 191 ? 37.521 -17.820 27.779 1.00 115.21 ? 191 TYR A CG 1 ATOM 1528 C CD1 . TYR A 1 191 ? 36.321 -17.754 27.076 1.00 114.25 ? 191 TYR A CD1 1 ATOM 1529 C CD2 . TYR A 1 191 ? 38.652 -17.240 27.204 1.00 113.25 ? 191 TYR A CD2 1 ATOM 1530 C CE1 . TYR A 1 191 ? 36.249 -17.150 25.830 1.00 110.96 ? 191 TYR A CE1 1 ATOM 1531 C CE2 . TYR A 1 191 ? 38.588 -16.633 25.959 1.00 110.86 ? 191 TYR A CE2 1 ATOM 1532 C CZ . TYR A 1 191 ? 37.380 -16.591 25.280 1.00 109.06 ? 191 TYR A CZ 1 ATOM 1533 O OH . TYR A 1 191 ? 37.292 -15.987 24.053 1.00 106.23 ? 191 TYR A OH 1 ATOM 1534 N N . ARG A 1 192 ? 37.958 -17.519 32.413 1.00 127.56 ? 192 ARG A N 1 ATOM 1535 C CA . ARG A 1 192 ? 38.394 -17.924 33.757 1.00 129.63 ? 192 ARG A CA 1 ATOM 1536 C C . ARG A 1 192 ? 39.422 -19.058 33.748 1.00 127.68 ? 192 ARG A C 1 ATOM 1537 O O . ARG A 1 192 ? 40.558 -18.863 34.186 1.00 128.53 ? 192 ARG A O 1 ATOM 1538 C CB . ARG A 1 192 ? 37.205 -18.251 34.666 1.00 133.36 ? 192 ARG A CB 1 ATOM 1539 C CG . ARG A 1 192 ? 37.359 -17.648 36.058 1.00 138.96 ? 192 ARG A CG 1 ATOM 1540 C CD . ARG A 1 192 ? 36.182 -17.980 36.948 1.00 141.96 ? 192 ARG A CD 1 ATOM 1541 N NE . ARG A 1 192 ? 36.289 -19.338 37.479 1.00 143.89 ? 192 ARG A NE 1 ATOM 1542 C CZ . ARG A 1 192 ? 36.870 -19.675 38.632 1.00 147.70 ? 192 ARG A CZ 1 ATOM 1543 N NH1 . ARG A 1 192 ? 37.412 -18.756 39.432 1.00 150.44 ? 192 ARG A NH1 1 ATOM 1544 N NH2 . ARG A 1 192 ? 36.904 -20.954 38.994 1.00 148.21 ? 192 ARG A NH2 1 ATOM 1545 N N . ASN A 1 193 ? 39.027 -20.232 33.261 1.00 124.76 ? 193 ASN A N 1 ATOM 1546 C CA . ASN A 1 193 ? 39.949 -21.362 33.120 1.00 123.66 ? 193 ASN A CA 1 ATOM 1547 C C . ASN A 1 193 ? 41.241 -20.923 32.429 1.00 122.26 ? 193 ASN A C 1 ATOM 1548 O O . ASN A 1 193 ? 41.190 -20.327 31.355 1.00 119.85 ? 193 ASN A O 1 ATOM 1549 C CB . ASN A 1 193 ? 39.301 -22.490 32.315 1.00 121.35 ? 193 ASN A CB 1 ATOM 1550 C CG . ASN A 1 193 ? 38.067 -23.058 32.991 1.00 122.79 ? 193 ASN A CG 1 ATOM 1551 O OD1 . ASN A 1 193 ? 36.975 -23.055 32.423 1.00 119.91 ? 193 ASN A OD1 1 ATOM 1552 N ND2 . ASN A 1 193 ? 38.234 -23.537 34.216 1.00 126.60 ? 193 ASN A ND2 1 ATOM 1553 N N . PRO A 1 194 ? 42.402 -21.199 33.047 1.00 124.32 ? 194 PRO A N 1 ATOM 1554 C CA . PRO A 1 194 ? 43.666 -20.750 32.464 1.00 123.11 ? 194 PRO A CA 1 ATOM 1555 C C . PRO A 1 194 ? 44.099 -21.589 31.259 1.00 120.33 ? 194 PRO A C 1 ATOM 1556 O O . PRO A 1 194 ? 44.540 -21.031 30.255 1.00 116.72 ? 194 PRO A O 1 ATOM 1557 C CB . PRO A 1 194 ? 44.658 -20.892 33.622 1.00 126.82 ? 194 PRO A CB 1 ATOM 1558 C CG . PRO A 1 194 ? 44.095 -21.968 34.482 1.00 128.75 ? 194 PRO A CG 1 ATOM 1559 C CD . PRO A 1 194 ? 42.602 -21.947 34.303 1.00 127.84 ? 194 PRO A CD 1 ATOM 1560 N N . THR A 1 195 ? 43.974 -22.911 31.367 1.00 120.91 ? 195 THR A N 1 ATOM 1561 C CA . THR A 1 195 ? 44.289 -23.823 30.268 1.00 118.32 ? 195 THR A CA 1 ATOM 1562 C C . THR A 1 195 ? 42.988 -24.352 29.678 1.00 117.20 ? 195 THR A C 1 ATOM 1563 O O . THR A 1 195 ? 42.195 -24.974 30.386 1.00 119.55 ? 195 THR A O 1 ATOM 1564 C CB . THR A 1 195 ? 45.131 -25.020 30.755 1.00 119.26 ? 195 THR A CB 1 ATOM 1565 O OG1 . THR A 1 195 ? 46.290 -24.546 31.447 1.00 120.91 ? 195 THR A OG1 1 ATOM 1566 C CG2 . THR A 1 195 ? 45.569 -25.897 29.584 1.00 116.51 ? 195 THR A CG2 1 ATOM 1567 N N . THR A 1 196 ? 42.768 -24.101 28.388 1.00 114.62 ? 196 THR A N 1 ATOM 1568 C CA . THR A 1 196 ? 41.541 -24.535 27.719 1.00 112.54 ? 196 THR A CA 1 ATOM 1569 C C . THR A 1 196 ? 41.830 -25.307 26.437 1.00 110.05 ? 196 THR A C 1 ATOM 1570 O O . THR A 1 196 ? 42.975 -25.404 25.995 1.00 108.47 ? 196 THR A O 1 ATOM 1571 C CB . THR A 1 196 ? 40.619 -23.345 27.384 1.00 111.83 ? 196 THR A CB 1 ATOM 1572 O OG1 . THR A 1 196 ? 41.298 -22.439 26.507 1.00 109.30 ? 196 THR A OG1 1 ATOM 1573 C CG2 . THR A 1 196 ? 40.205 -22.617 28.653 1.00 115.39 ? 196 THR A CG2 1 ATOM 1574 N N . TYR A 1 197 ? 40.769 -25.861 25.860 1.00 109.05 ? 197 TYR A N 1 ATOM 1575 C CA . TYR A 1 197 ? 40.856 -26.636 24.634 1.00 105.98 ? 197 TYR A CA 1 ATOM 1576 C C . TYR A 1 197 ? 39.498 -26.689 23.959 1.00 105.99 ? 197 TYR A C 1 ATOM 1577 O O . TYR A 1 197 ? 38.484 -26.331 24.558 1.00 106.56 ? 197 TYR A O 1 ATOM 1578 C CB . TYR A 1 197 ? 41.313 -28.066 24.940 1.00 106.25 ? 197 TYR A CB 1 ATOM 1579 C CG . TYR A 1 197 ? 40.308 -28.877 25.740 1.00 106.54 ? 197 TYR A CG 1 ATOM 1580 C CD1 . TYR A 1 197 ? 40.173 -28.697 27.116 1.00 108.90 ? 197 TYR A CD1 1 ATOM 1581 C CD2 . TYR A 1 197 ? 39.493 -29.821 25.120 1.00 104.69 ? 197 TYR A CD2 1 ATOM 1582 C CE1 . TYR A 1 197 ? 39.256 -29.432 27.851 1.00 109.90 ? 197 TYR A CE1 1 ATOM 1583 C CE2 . TYR A 1 197 ? 38.575 -30.563 25.845 1.00 106.01 ? 197 TYR A CE2 1 ATOM 1584 C CZ . TYR A 1 197 ? 38.459 -30.364 27.212 1.00 108.91 ? 197 TYR A CZ 1 ATOM 1585 O OH . TYR A 1 197 ? 37.545 -31.095 27.936 1.00 109.61 ? 197 TYR A OH 1 ATOM 1586 N N . ILE A 1 198 ? 39.492 -27.125 22.704 1.00 105.86 ? 198 ILE A N 1 ATOM 1587 C CA . ILE A 1 198 ? 38.260 -27.464 21.999 1.00 105.37 ? 198 ILE A CA 1 ATOM 1588 C C . ILE A 1 198 ? 38.502 -28.765 21.252 1.00 104.40 ? 198 ILE A C 1 ATOM 1589 O O . ILE A 1 198 ? 39.405 -28.838 20.418 1.00 103.94 ? 198 ILE A O 1 ATOM 1590 C CB . ILE A 1 198 ? 37.849 -26.387 20.976 1.00 104.19 ? 198 ILE A CB 1 ATOM 1591 C CG1 . ILE A 1 198 ? 37.702 -25.016 21.642 1.00 104.99 ? 198 ILE A CG1 1 ATOM 1592 C CG2 . ILE A 1 198 ? 36.541 -26.774 20.297 1.00 103.54 ? 198 ILE A CG2 1 ATOM 1593 C CD1 . ILE A 1 198 ? 37.856 -23.868 20.671 1.00 103.68 ? 198 ILE A CD1 1 ATOM 1594 N N . SER A 1 199 ? 37.704 -29.786 21.558 1.00 104.79 ? 199 SER A N 1 ATOM 1595 C CA . SER A 1 199 ? 37.801 -31.072 20.873 1.00 103.96 ? 199 SER A CA 1 ATOM 1596 C C . SER A 1 199 ? 36.586 -31.290 19.978 1.00 102.00 ? 199 SER A C 1 ATOM 1597 O O . SER A 1 199 ? 35.446 -31.172 20.421 1.00 101.88 ? 199 SER A O 1 ATOM 1598 C CB . SER A 1 199 ? 37.935 -32.213 21.882 1.00 105.89 ? 199 SER A CB 1 ATOM 1599 O OG . SER A 1 199 ? 36.889 -32.175 22.828 1.00 108.07 ? 199 SER A OG 1 ATOM 1600 N N . VAL A 1 200 ? 36.849 -31.605 18.715 1.00 101.64 ? 200 VAL A N 1 ATOM 1601 C CA . VAL A 1 200 ? 35.803 -31.810 17.721 1.00 101.17 ? 200 VAL A CA 1 ATOM 1602 C C . VAL A 1 200 ? 35.979 -33.190 17.099 1.00 101.28 ? 200 VAL A C 1 ATOM 1603 O O . VAL A 1 200 ? 37.090 -33.562 16.705 1.00 101.07 ? 200 VAL A O 1 ATOM 1604 C CB . VAL A 1 200 ? 35.870 -30.747 16.602 1.00 99.61 ? 200 VAL A CB 1 ATOM 1605 C CG1 . VAL A 1 200 ? 34.558 -30.705 15.831 1.00 99.77 ? 200 VAL A CG1 1 ATOM 1606 C CG2 . VAL A 1 200 ? 36.196 -29.374 17.174 1.00 99.26 ? 200 VAL A CG2 1 ATOM 1607 N N . GLY A 1 201 ? 34.887 -33.945 17.006 1.00 101.36 ? 201 GLY A N 1 ATOM 1608 C CA . GLY A 1 201 ? 34.933 -35.293 16.449 1.00 101.39 ? 201 GLY A CA 1 ATOM 1609 C C . GLY A 1 201 ? 33.737 -35.614 15.575 1.00 101.03 ? 201 GLY A C 1 ATOM 1610 O O . GLY A 1 201 ? 32.608 -35.254 15.900 1.00 102.10 ? 201 GLY A O 1 ATOM 1611 N N . THR A 1 202 ? 34.000 -36.271 14.450 1.00 100.25 ? 202 THR A N 1 ATOM 1612 C CA . THR A 1 202 ? 32.957 -36.887 13.632 1.00 100.47 ? 202 THR A CA 1 ATOM 1613 C C . THR A 1 202 ? 33.372 -38.337 13.414 1.00 103.00 ? 202 THR A C 1 ATOM 1614 O O . THR A 1 202 ? 34.217 -38.857 14.148 1.00 103.38 ? 202 THR A O 1 ATOM 1615 C CB . THR A 1 202 ? 32.777 -36.172 12.271 1.00 97.48 ? 202 THR A CB 1 ATOM 1616 O OG1 . THR A 1 202 ? 33.923 -36.396 11.438 1.00 94.87 ? 202 THR A OG1 1 ATOM 1617 C CG2 . THR A 1 202 ? 32.570 -34.690 12.468 1.00 96.46 ? 202 THR A CG2 1 ATOM 1618 N N . SER A 1 203 ? 32.780 -38.991 12.419 1.00 104.41 ? 203 SER A N 1 ATOM 1619 C CA . SER A 1 203 ? 33.230 -40.317 12.013 1.00 105.77 ? 203 SER A CA 1 ATOM 1620 C C . SER A 1 203 ? 34.670 -40.263 11.504 1.00 104.57 ? 203 SER A C 1 ATOM 1621 O O . SER A 1 203 ? 35.471 -41.136 11.819 1.00 106.40 ? 203 SER A O 1 ATOM 1622 C CB . SER A 1 203 ? 32.308 -40.893 10.938 1.00 105.99 ? 203 SER A CB 1 ATOM 1623 O OG . SER A 1 203 ? 32.144 -39.980 9.873 1.00 104.32 ? 203 SER A OG 1 ATOM 1624 N N . THR A 1 204 ? 34.997 -39.232 10.731 1.00 103.14 ? 204 THR A N 1 ATOM 1625 C CA . THR A 1 204 ? 36.350 -39.072 10.202 1.00 102.75 ? 204 THR A CA 1 ATOM 1626 C C . THR A 1 204 ? 37.191 -38.168 11.098 1.00 103.59 ? 204 THR A C 1 ATOM 1627 O O . THR A 1 204 ? 38.290 -38.542 11.500 1.00 109.09 ? 204 THR A O 1 ATOM 1628 C CB . THR A 1 204 ? 36.342 -38.492 8.774 1.00 99.74 ? 204 THR A CB 1 ATOM 1629 O OG1 . THR A 1 204 ? 35.853 -37.144 8.799 1.00 97.65 ? 204 THR A OG1 1 ATOM 1630 C CG2 . THR A 1 204 ? 35.468 -39.341 7.850 1.00 99.08 ? 204 THR A CG2 1 ATOM 1631 N N . LEU A 1 205 ? 36.663 -36.990 11.422 1.00 101.30 ? 205 LEU A N 1 ATOM 1632 C CA . LEU A 1 205 ? 37.439 -35.958 12.117 1.00 99.15 ? 205 LEU A CA 1 ATOM 1633 C C . LEU A 1 205 ? 37.826 -36.334 13.560 1.00 100.10 ? 205 LEU A C 1 ATOM 1634 O O . LEU A 1 205 ? 37.058 -36.982 14.282 1.00 99.28 ? 205 LEU A O 1 ATOM 1635 C CB . LEU A 1 205 ? 36.675 -34.627 12.106 1.00 98.25 ? 205 LEU A CB 1 ATOM 1636 C CG . LEU A 1 205 ? 37.458 -33.354 12.458 1.00 98.20 ? 205 LEU A CG 1 ATOM 1637 C CD1 . LEU A 1 205 ? 38.574 -33.084 11.455 1.00 96.07 ? 205 LEU A CD1 1 ATOM 1638 C CD2 . LEU A 1 205 ? 36.520 -32.160 12.537 1.00 97.10 ? 205 LEU A CD2 1 ATOM 1639 N N . ASN A 1 206 ? 39.030 -35.919 13.954 1.00 98.99 ? 206 ASN A N 1 ATOM 1640 C CA . ASN A 1 206 ? 39.554 -36.130 15.305 1.00 99.71 ? 206 ASN A CA 1 ATOM 1641 C C . ASN A 1 206 ? 40.477 -34.970 15.693 1.00 98.11 ? 206 ASN A C 1 ATOM 1642 O O . ASN A 1 206 ? 41.701 -35.070 15.594 1.00 97.22 ? 206 ASN A O 1 ATOM 1643 C CB . ASN A 1 206 ? 40.300 -37.463 15.385 1.00 101.35 ? 206 ASN A CB 1 ATOM 1644 C CG . ASN A 1 206 ? 40.950 -37.691 16.738 1.00 104.56 ? 206 ASN A CG 1 ATOM 1645 O OD1 . ASN A 1 206 ? 40.293 -37.620 17.778 1.00 106.21 ? 206 ASN A OD1 1 ATOM 1646 N ND2 . ASN A 1 206 ? 42.251 -37.954 16.731 1.00 106.15 ? 206 ASN A ND2 1 ATOM 1647 N N . GLN A 1 207 ? 39.873 -33.879 16.150 1.00 97.07 ? 207 GLN A N 1 ATOM 1648 C CA . GLN A 1 207 ? 40.574 -32.617 16.350 1.00 97.08 ? 207 GLN A CA 1 ATOM 1649 C C . GLN A 1 207 ? 40.691 -32.242 17.830 1.00 99.76 ? 207 GLN A C 1 ATOM 1650 O O . GLN A 1 207 ? 39.841 -32.604 18.642 1.00 99.67 ? 207 GLN A O 1 ATOM 1651 C CB . GLN A 1 207 ? 39.817 -31.529 15.591 1.00 95.48 ? 207 GLN A CB 1 ATOM 1652 C CG . GLN A 1 207 ? 40.422 -30.139 15.646 1.00 95.18 ? 207 GLN A CG 1 ATOM 1653 C CD . GLN A 1 207 ? 39.562 -29.128 14.919 1.00 94.54 ? 207 GLN A CD 1 ATOM 1654 O OE1 . GLN A 1 207 ? 38.865 -28.325 15.540 1.00 96.68 ? 207 GLN A OE1 1 ATOM 1655 N NE2 . GLN A 1 207 ? 39.588 -29.179 13.594 1.00 93.29 ? 207 GLN A NE2 1 ATOM 1656 N N . ARG A 1 208 ? 41.759 -31.525 18.171 1.00 101.44 ? 208 ARG A N 1 ATOM 1657 C CA . ARG A 1 208 ? 41.893 -30.909 19.490 1.00 104.97 ? 208 ARG A CA 1 ATOM 1658 C C . ARG A 1 208 ? 42.667 -29.595 19.382 1.00 105.13 ? 208 ARG A C 1 ATOM 1659 O O . ARG A 1 208 ? 43.881 -29.595 19.177 1.00 104.95 ? 208 ARG A O 1 ATOM 1660 C CB . ARG A 1 208 ? 42.587 -31.850 20.477 1.00 108.37 ? 208 ARG A CB 1 ATOM 1661 C CG . ARG A 1 208 ? 42.443 -31.413 21.931 1.00 111.62 ? 208 ARG A CG 1 ATOM 1662 C CD . ARG A 1 208 ? 43.459 -32.090 22.839 1.00 114.71 ? 208 ARG A CD 1 ATOM 1663 N NE . ARG A 1 208 ? 43.163 -31.872 24.256 1.00 117.25 ? 208 ARG A NE 1 ATOM 1664 C CZ . ARG A 1 208 ? 42.213 -32.507 24.946 1.00 118.72 ? 208 ARG A CZ 1 ATOM 1665 N NH1 . ARG A 1 208 ? 41.433 -33.415 24.365 1.00 117.96 ? 208 ARG A NH1 1 ATOM 1666 N NH2 . ARG A 1 208 ? 42.035 -32.228 26.234 1.00 121.77 ? 208 ARG A NH2 1 ATOM 1667 N N . LEU A 1 209 ? 41.955 -28.481 19.523 1.00 105.66 ? 209 LEU A N 1 ATOM 1668 C CA . LEU A 1 209 ? 42.548 -27.156 19.386 1.00 106.22 ? 209 LEU A CA 1 ATOM 1669 C C . LEU A 1 209 ? 42.944 -26.607 20.748 1.00 108.62 ? 209 LEU A C 1 ATOM 1670 O O . LEU A 1 209 ? 42.231 -26.806 21.729 1.00 109.08 ? 209 LEU A O 1 ATOM 1671 C CB . LEU A 1 209 ? 41.553 -26.198 18.730 1.00 105.85 ? 209 LEU A CB 1 ATOM 1672 C CG . LEU A 1 209 ? 40.944 -26.630 17.392 1.00 104.41 ? 209 LEU A CG 1 ATOM 1673 C CD1 . LEU A 1 209 ? 39.839 -25.664 16.985 1.00 103.65 ? 209 LEU A CD1 1 ATOM 1674 C CD2 . LEU A 1 209 ? 42.009 -26.726 16.309 1.00 103.06 ? 209 LEU A CD2 1 ATOM 1675 N N . VAL A 1 210 ? 44.084 -25.921 20.799 1.00 110.10 ? 210 VAL A N 1 ATOM 1676 C CA . VAL A 1 210 ? 44.512 -25.203 22.002 1.00 113.36 ? 210 VAL A CA 1 ATOM 1677 C C . VAL A 1 210 ? 44.787 -23.743 21.641 1.00 113.30 ? 210 VAL A C 1 ATOM 1678 O O . VAL A 1 210 ? 45.423 -23.469 20.617 1.00 111.05 ? 210 VAL A O 1 ATOM 1679 C CB . VAL A 1 210 ? 45.759 -25.831 22.676 1.00 114.22 ? 210 VAL A CB 1 ATOM 1680 C CG1 . VAL A 1 210 ? 45.402 -27.171 23.296 1.00 114.83 ? 210 VAL A CG1 1 ATOM 1681 C CG2 . VAL A 1 210 ? 46.922 -25.982 21.699 1.00 113.30 ? 210 VAL A CG2 1 ATOM 1682 N N . PRO A 1 211 ? 44.292 -22.799 22.465 1.00 114.40 ? 211 PRO A N 1 ATOM 1683 C CA . PRO A 1 211 ? 44.575 -21.396 22.168 1.00 113.85 ? 211 PRO A CA 1 ATOM 1684 C C . PRO A 1 211 ? 46.049 -21.066 22.366 1.00 113.95 ? 211 PRO A C 1 ATOM 1685 O O . PRO A 1 211 ? 46.702 -21.645 23.239 1.00 114.42 ? 211 PRO A O 1 ATOM 1686 C CB . PRO A 1 211 ? 43.712 -20.622 23.177 1.00 115.79 ? 211 PRO A CB 1 ATOM 1687 C CG . PRO A 1 211 ? 42.762 -21.612 23.750 1.00 116.30 ? 211 PRO A CG 1 ATOM 1688 C CD . PRO A 1 211 ? 43.428 -22.947 23.649 1.00 115.83 ? 211 PRO A CD 1 ATOM 1689 N N . ARG A 1 212 ? 46.555 -20.146 21.553 1.00 111.86 ? 212 ARG A N 1 ATOM 1690 C CA . ARG A 1 212 ? 47.955 -19.766 21.583 1.00 113.26 ? 212 ARG A CA 1 ATOM 1691 C C . ARG A 1 212 ? 48.098 -18.295 21.947 1.00 114.49 ? 212 ARG A C 1 ATOM 1692 O O . ARG A 1 212 ? 47.629 -17.419 21.219 1.00 111.59 ? 212 ARG A O 1 ATOM 1693 C CB . ARG A 1 212 ? 48.595 -20.046 20.227 1.00 110.86 ? 212 ARG A CB 1 ATOM 1694 C CG . ARG A 1 212 ? 48.757 -21.530 19.938 1.00 110.23 ? 212 ARG A CG 1 ATOM 1695 C CD . ARG A 1 212 ? 49.240 -21.748 18.521 1.00 107.89 ? 212 ARG A CD 1 ATOM 1696 N NE . ARG A 1 212 ? 48.196 -21.409 17.561 1.00 106.67 ? 212 ARG A NE 1 ATOM 1697 C CZ . ARG A 1 212 ? 48.406 -21.108 16.283 1.00 105.91 ? 212 ARG A CZ 1 ATOM 1698 N NH1 . ARG A 1 212 ? 49.639 -21.091 15.784 1.00 107.50 ? 212 ARG A NH1 1 ATOM 1699 N NH2 . ARG A 1 212 ? 47.372 -20.817 15.498 1.00 103.47 ? 212 ARG A NH2 1 ATOM 1700 N N . ILE A 1 213 ? 48.743 -18.041 23.086 1.00 118.06 ? 213 ILE A N 1 ATOM 1701 C CA . ILE A 1 213 ? 48.990 -16.681 23.557 1.00 120.21 ? 213 ILE A CA 1 ATOM 1702 C C . ILE A 1 213 ? 50.256 -16.140 22.888 1.00 120.60 ? 213 ILE A C 1 ATOM 1703 O O . ILE A 1 213 ? 51.282 -16.825 22.831 1.00 120.81 ? 213 ILE A O 1 ATOM 1704 C CB . ILE A 1 213 ? 49.135 -16.615 25.100 1.00 122.66 ? 213 ILE A CB 1 ATOM 1705 C CG1 . ILE A 1 213 ? 47.786 -16.877 25.787 1.00 123.15 ? 213 ILE A CG1 1 ATOM 1706 C CG2 . ILE A 1 213 ? 49.674 -15.256 25.539 1.00 123.91 ? 213 ILE A CG2 1 ATOM 1707 C CD1 . ILE A 1 213 ? 47.340 -18.324 25.784 1.00 122.67 ? 213 ILE A CD1 1 ATOM 1708 N N . ALA A 1 214 ? 50.165 -14.914 22.378 1.00 120.03 ? 214 ALA A N 1 ATOM 1709 C CA . ALA A 1 214 ? 51.305 -14.224 21.782 1.00 119.92 ? 214 ALA A CA 1 ATOM 1710 C C . ALA A 1 214 ? 51.013 -12.736 21.645 1.00 119.87 ? 214 ALA A C 1 ATOM 1711 O O . ALA A 1 214 ? 49.855 -12.320 21.526 1.00 117.37 ? 214 ALA A O 1 ATOM 1712 C CB . ALA A 1 214 ? 51.644 -14.817 20.422 1.00 118.08 ? 214 ALA A CB 1 ATOM 1713 N N . THR A 1 215 ? 52.076 -11.941 21.660 1.00 120.85 ? 215 THR A N 1 ATOM 1714 C CA . THR A 1 215 ? 51.961 -10.500 21.510 1.00 121.28 ? 215 THR A CA 1 ATOM 1715 C C . THR A 1 215 ? 51.812 -10.163 20.032 1.00 118.50 ? 215 THR A C 1 ATOM 1716 O O . THR A 1 215 ? 52.747 -10.327 19.249 1.00 118.07 ? 215 THR A O 1 ATOM 1717 C CB . THR A 1 215 ? 53.193 -9.788 22.093 1.00 123.90 ? 215 THR A CB 1 ATOM 1718 O OG1 . THR A 1 215 ? 53.425 -10.267 23.422 1.00 125.14 ? 215 THR A OG1 1 ATOM 1719 C CG2 . THR A 1 215 ? 52.993 -8.271 22.117 1.00 124.50 ? 215 THR A CG2 1 ATOM 1720 N N . ARG A 1 216 ? 50.624 -9.702 19.657 1.00 117.01 ? 216 ARG A N 1 ATOM 1721 C CA . ARG A 1 216 ? 50.311 -9.411 18.263 1.00 114.64 ? 216 ARG A CA 1 ATOM 1722 C C . ARG A 1 216 ? 50.229 -7.909 18.024 1.00 115.08 ? 216 ARG A C 1 ATOM 1723 O O . ARG A 1 216 ? 49.941 -7.142 18.941 1.00 115.37 ? 216 ARG A O 1 ATOM 1724 C CB . ARG A 1 216 ? 48.973 -10.052 17.870 1.00 112.77 ? 216 ARG A CB 1 ATOM 1725 C CG . ARG A 1 216 ? 49.070 -11.435 17.236 1.00 111.20 ? 216 ARG A CG 1 ATOM 1726 C CD . ARG A 1 216 ? 48.969 -12.579 18.233 1.00 111.88 ? 216 ARG A CD 1 ATOM 1727 N NE . ARG A 1 216 ? 47.736 -12.536 19.022 1.00 113.39 ? 216 ARG A NE 1 ATOM 1728 C CZ . ARG A 1 216 ? 47.281 -13.534 19.781 1.00 113.83 ? 216 ARG A CZ 1 ATOM 1729 N NH1 . ARG A 1 216 ? 47.925 -14.695 19.853 1.00 113.61 ? 216 ARG A NH1 1 ATOM 1730 N NH2 . ARG A 1 216 ? 46.155 -13.373 20.467 1.00 114.22 ? 216 ARG A NH2 1 ATOM 1731 N N . SER A 1 217 ? 50.481 -7.503 16.783 1.00 114.60 ? 217 SER A N 1 ATOM 1732 C CA . SER A 1 217 ? 50.167 -6.149 16.333 1.00 115.51 ? 217 SER A CA 1 ATOM 1733 C C . SER A 1 217 ? 48.651 -6.014 16.222 1.00 113.59 ? 217 SER A C 1 ATOM 1734 O O . SER A 1 217 ? 47.952 -6.999 15.987 1.00 112.02 ? 217 SER A O 1 ATOM 1735 C CB . SER A 1 217 ? 50.811 -5.868 14.973 1.00 115.08 ? 217 SER A CB 1 ATOM 1736 O OG . SER A 1 217 ? 52.187 -6.209 14.978 1.00 117.13 ? 217 SER A OG 1 ATOM 1737 N N . LYS A 1 218 ? 48.141 -4.801 16.401 1.00 114.22 ? 218 LYS A N 1 ATOM 1738 C CA . LYS A 1 218 ? 46.709 -4.556 16.251 1.00 112.89 ? 218 LYS A CA 1 ATOM 1739 C C . LYS A 1 218 ? 46.314 -4.634 14.778 1.00 110.80 ? 218 LYS A C 1 ATOM 1740 O O . LYS A 1 218 ? 47.012 -4.111 13.912 1.00 111.61 ? 218 LYS A O 1 ATOM 1741 C CB . LYS A 1 218 ? 46.310 -3.192 16.827 1.00 114.29 ? 218 LYS A CB 1 ATOM 1742 C CG . LYS A 1 218 ? 46.229 -3.159 18.346 1.00 116.21 ? 218 LYS A CG 1 ATOM 1743 C CD . LYS A 1 218 ? 45.596 -1.872 18.851 1.00 117.70 ? 218 LYS A CD 1 ATOM 1744 C CE . LYS A 1 218 ? 45.274 -1.936 20.338 1.00 120.01 ? 218 LYS A CE 1 ATOM 1745 N NZ . LYS A 1 218 ? 46.481 -1.823 21.205 1.00 122.65 ? 218 LYS A NZ 1 ATOM 1746 N N . VAL A 1 219 ? 45.205 -5.313 14.507 1.00 108.31 ? 219 VAL A N 1 ATOM 1747 C CA . VAL A 1 219 ? 44.605 -5.342 13.179 1.00 105.55 ? 219 VAL A CA 1 ATOM 1748 C C . VAL A 1 219 ? 43.122 -5.052 13.354 1.00 104.63 ? 219 VAL A C 1 ATOM 1749 O O . VAL A 1 219 ? 42.434 -5.767 14.077 1.00 104.92 ? 219 VAL A O 1 ATOM 1750 C CB . VAL A 1 219 ? 44.794 -6.715 12.512 1.00 105.33 ? 219 VAL A CB 1 ATOM 1751 C CG1 . VAL A 1 219 ? 44.083 -6.765 11.165 1.00 103.36 ? 219 VAL A CG1 1 ATOM 1752 C CG2 . VAL A 1 219 ? 46.277 -7.020 12.352 1.00 106.28 ? 219 VAL A CG2 1 ATOM 1753 N N . ASN A 1 220 ? 42.635 -4.000 12.701 1.00 104.18 ? 220 ASN A N 1 ATOM 1754 C CA . ASN A 1 220 ? 41.296 -3.464 12.972 1.00 104.77 ? 220 ASN A CA 1 ATOM 1755 C C . ASN A 1 220 ? 41.086 -3.155 14.463 1.00 104.49 ? 220 ASN A C 1 ATOM 1756 O O . ASN A 1 220 ? 39.998 -3.359 15.006 1.00 104.94 ? 220 ASN A O 1 ATOM 1757 C CB . ASN A 1 220 ? 40.205 -4.419 12.467 1.00 105.09 ? 220 ASN A CB 1 ATOM 1758 C CG . ASN A 1 220 ? 40.200 -4.565 10.958 1.00 104.93 ? 220 ASN A CG 1 ATOM 1759 O OD1 . ASN A 1 220 ? 41.239 -4.468 10.298 1.00 104.01 ? 220 ASN A OD1 1 ATOM 1760 N ND2 . ASN A 1 220 ? 39.021 -4.811 10.405 1.00 105.55 ? 220 ASN A ND2 1 ATOM 1761 N N . GLY A 1 221 ? 42.137 -2.670 15.119 1.00 103.40 ? 221 GLY A N 1 ATOM 1762 C CA . GLY A 1 221 ? 42.057 -2.265 16.517 1.00 104.33 ? 221 GLY A CA 1 ATOM 1763 C C . GLY A 1 221 ? 41.991 -3.394 17.531 1.00 103.81 ? 221 GLY A C 1 ATOM 1764 O O . GLY A 1 221 ? 41.683 -3.156 18.699 1.00 105.17 ? 221 GLY A O 1 ATOM 1765 N N . GLN A 1 222 ? 42.287 -4.618 17.106 1.00 101.86 ? 222 GLN A N 1 ATOM 1766 C CA . GLN A 1 222 ? 42.244 -5.766 18.008 1.00 103.38 ? 222 GLN A CA 1 ATOM 1767 C C . GLN A 1 222 ? 43.546 -6.549 17.958 1.00 103.30 ? 222 GLN A C 1 ATOM 1768 O O . GLN A 1 222 ? 44.096 -6.782 16.881 1.00 102.64 ? 222 GLN A O 1 ATOM 1769 C CB . GLN A 1 222 ? 41.073 -6.691 17.662 1.00 102.68 ? 222 GLN A CB 1 ATOM 1770 C CG . GLN A 1 222 ? 39.710 -6.010 17.625 1.00 103.99 ? 222 GLN A CG 1 ATOM 1771 C CD . GLN A 1 222 ? 39.335 -5.321 18.928 1.00 108.01 ? 222 GLN A CD 1 ATOM 1772 O OE1 . GLN A 1 222 ? 39.732 -5.744 20.019 1.00 107.58 ? 222 GLN A OE1 1 ATOM 1773 N NE2 . GLN A 1 222 ? 38.559 -4.247 18.815 1.00 110.49 ? 222 GLN A NE2 1 ATOM 1774 N N . ASN A 1 223 ? 44.030 -6.945 19.132 1.00 105.18 ? 223 ASN A N 1 ATOM 1775 C CA . ASN A 1 223 ? 45.236 -7.757 19.249 1.00 105.96 ? 223 ASN A CA 1 ATOM 1776 C C . ASN A 1 223 ? 44.921 -9.250 19.248 1.00 104.95 ? 223 ASN A C 1 ATOM 1777 O O . ASN A 1 223 ? 45.750 -10.065 18.839 1.00 103.74 ? 223 ASN A O 1 ATOM 1778 C CB . ASN A 1 223 ? 45.976 -7.414 20.533 1.00 109.67 ? 223 ASN A CB 1 ATOM 1779 C CG . ASN A 1 223 ? 46.576 -6.033 20.517 1.00 111.57 ? 223 ASN A CG 1 ATOM 1780 O OD1 . ASN A 1 223 ? 47.390 -5.711 19.652 1.00 113.32 ? 223 ASN A OD1 1 ATOM 1781 N ND2 . ASN A 1 223 ? 46.200 -5.213 21.492 1.00 112.80 ? 223 ASN A ND2 1 ATOM 1782 N N . GLY A 1 224 ? 43.728 -9.602 19.723 1.00 105.68 ? 224 GLY A N 1 ATOM 1783 C CA . GLY A 1 224 ? 43.256 -10.985 19.705 1.00 104.18 ? 224 GLY A CA 1 ATOM 1784 C C . GLY A 1 224 ? 43.073 -11.510 18.294 1.00 100.75 ? 224 GLY A C 1 ATOM 1785 O O . GLY A 1 224 ? 42.968 -10.732 17.347 1.00 99.76 ? 224 GLY A O 1 ATOM 1786 N N . ARG A 1 225 ? 43.038 -12.834 18.155 1.00 99.90 ? 225 ARG A N 1 ATOM 1787 C CA . ARG A 1 225 ? 42.873 -13.477 16.848 1.00 98.67 ? 225 ARG A CA 1 ATOM 1788 C C . ARG A 1 225 ? 41.808 -14.568 16.891 1.00 97.94 ? 225 ARG A C 1 ATOM 1789 O O . ARG A 1 225 ? 41.634 -15.242 17.905 1.00 100.54 ? 225 ARG A O 1 ATOM 1790 C CB . ARG A 1 225 ? 44.195 -14.091 16.379 1.00 97.64 ? 225 ARG A CB 1 ATOM 1791 C CG . ARG A 1 225 ? 45.300 -13.087 16.102 1.00 98.07 ? 225 ARG A CG 1 ATOM 1792 C CD . ARG A 1 225 ? 45.113 -12.376 14.773 1.00 96.31 ? 225 ARG A CD 1 ATOM 1793 N NE . ARG A 1 225 ? 46.229 -11.469 14.510 1.00 97.10 ? 225 ARG A NE 1 ATOM 1794 C CZ . ARG A 1 225 ? 46.326 -10.220 14.965 1.00 98.03 ? 225 ARG A CZ 1 ATOM 1795 N NH1 . ARG A 1 225 ? 45.367 -9.682 15.717 1.00 98.28 ? 225 ARG A NH1 1 ATOM 1796 N NH2 . ARG A 1 225 ? 47.400 -9.499 14.662 1.00 98.97 ? 225 ARG A NH2 1 ATOM 1797 N N . MET A 1 226 ? 41.104 -14.730 15.778 1.00 95.77 ? 226 MET A N 1 ATOM 1798 C CA . MET A 1 226 ? 40.131 -15.795 15.619 1.00 95.66 ? 226 MET A CA 1 ATOM 1799 C C . MET A 1 226 ? 40.602 -16.703 14.491 1.00 93.91 ? 226 MET A C 1 ATOM 1800 O O . MET A 1 226 ? 40.974 -16.222 13.428 1.00 94.03 ? 226 MET A O 1 ATOM 1801 C CB . MET A 1 226 ? 38.766 -15.208 15.272 1.00 96.77 ? 226 MET A CB 1 ATOM 1802 C CG . MET A 1 226 ? 38.143 -14.367 16.375 1.00 99.43 ? 226 MET A CG 1 ATOM 1803 S SD . MET A 1 226 ? 37.280 -15.338 17.622 1.00 102.21 ? 226 MET A SD 1 ATOM 1804 C CE . MET A 1 226 ? 36.495 -14.021 18.546 1.00 104.35 ? 226 MET A CE 1 ATOM 1805 N N . GLU A 1 227 ? 40.583 -18.012 14.726 1.00 93.17 ? 227 GLU A N 1 ATOM 1806 C CA . GLU A 1 227 ? 40.997 -18.994 13.729 1.00 91.88 ? 227 GLU A CA 1 ATOM 1807 C C . GLU A 1 227 ? 39.822 -19.922 13.443 1.00 90.67 ? 227 GLU A C 1 ATOM 1808 O O . GLU A 1 227 ? 39.391 -20.670 14.320 1.00 91.20 ? 227 GLU A O 1 ATOM 1809 C CB . GLU A 1 227 ? 42.201 -19.779 14.247 1.00 93.59 ? 227 GLU A CB 1 ATOM 1810 C CG . GLU A 1 227 ? 42.891 -20.643 13.205 1.00 94.41 ? 227 GLU A CG 1 ATOM 1811 C CD . GLU A 1 227 ? 44.219 -21.202 13.692 1.00 96.22 ? 227 GLU A CD 1 ATOM 1812 O OE1 . GLU A 1 227 ? 44.537 -21.054 14.891 1.00 96.03 ? 227 GLU A OE1 1 ATOM 1813 O OE2 . GLU A 1 227 ? 44.954 -21.789 12.869 1.00 97.30 ? 227 GLU A OE2 1 ATOM 1814 N N . PHE A 1 228 ? 39.296 -19.862 12.222 1.00 88.12 ? 228 PHE A N 1 ATOM 1815 C CA . PHE A 1 228 ? 38.061 -20.574 11.889 1.00 86.37 ? 228 PHE A CA 1 ATOM 1816 C C . PHE A 1 228 ? 38.333 -21.875 11.146 1.00 84.57 ? 228 PHE A C 1 ATOM 1817 O O . PHE A 1 228 ? 39.189 -21.931 10.261 1.00 83.24 ? 228 PHE A O 1 ATOM 1818 C CB . PHE A 1 228 ? 37.134 -19.674 11.076 1.00 85.34 ? 228 PHE A CB 1 ATOM 1819 C CG . PHE A 1 228 ? 36.675 -18.456 11.824 1.00 86.29 ? 228 PHE A CG 1 ATOM 1820 C CD1 . PHE A 1 228 ? 35.566 -18.514 12.657 1.00 87.42 ? 228 PHE A CD1 1 ATOM 1821 C CD2 . PHE A 1 228 ? 37.365 -17.256 11.715 1.00 86.81 ? 228 PHE A CD2 1 ATOM 1822 C CE1 . PHE A 1 228 ? 35.148 -17.395 13.359 1.00 88.43 ? 228 PHE A CE1 1 ATOM 1823 C CE2 . PHE A 1 228 ? 36.951 -16.132 12.412 1.00 88.04 ? 228 PHE A CE2 1 ATOM 1824 C CZ . PHE A 1 228 ? 35.841 -16.203 13.237 1.00 88.78 ? 228 PHE A CZ 1 ATOM 1825 N N . PHE A 1 229 ? 37.595 -22.915 11.528 1.00 83.90 ? 229 PHE A N 1 ATOM 1826 C CA . PHE A 1 229 ? 37.745 -24.250 10.957 1.00 83.50 ? 229 PHE A CA 1 ATOM 1827 C C . PHE A 1 229 ? 36.422 -24.723 10.382 1.00 83.53 ? 229 PHE A C 1 ATOM 1828 O O . PHE A 1 229 ? 35.374 -24.120 10.631 1.00 83.15 ? 229 PHE A O 1 ATOM 1829 C CB . PHE A 1 229 ? 38.226 -25.231 12.026 1.00 84.55 ? 229 PHE A CB 1 ATOM 1830 C CG . PHE A 1 229 ? 39.610 -24.943 12.523 1.00 85.73 ? 229 PHE A CG 1 ATOM 1831 C CD1 . PHE A 1 229 ? 39.823 -23.980 13.498 1.00 87.39 ? 229 PHE A CD1 1 ATOM 1832 C CD2 . PHE A 1 229 ? 40.704 -25.625 12.007 1.00 85.87 ? 229 PHE A CD2 1 ATOM 1833 C CE1 . PHE A 1 229 ? 41.103 -23.704 13.955 1.00 88.12 ? 229 PHE A CE1 1 ATOM 1834 C CE2 . PHE A 1 229 ? 41.985 -25.354 12.459 1.00 86.93 ? 229 PHE A CE2 1 ATOM 1835 C CZ . PHE A 1 229 ? 42.186 -24.393 13.435 1.00 87.79 ? 229 PHE A CZ 1 ATOM 1836 N N . TRP A 1 230 ? 36.472 -25.805 9.610 1.00 84.17 ? 230 TRP A N 1 ATOM 1837 C CA . TRP A 1 230 ? 35.277 -26.323 8.961 1.00 83.68 ? 230 TRP A CA 1 ATOM 1838 C C . TRP A 1 230 ? 35.347 -27.811 8.662 1.00 83.82 ? 230 TRP A C 1 ATOM 1839 O O . TRP A 1 230 ? 36.417 -28.412 8.675 1.00 83.67 ? 230 TRP A O 1 ATOM 1840 C CB . TRP A 1 230 ? 35.016 -25.553 7.666 1.00 82.62 ? 230 TRP A CB 1 ATOM 1841 C CG . TRP A 1 230 ? 36.091 -25.674 6.631 1.00 82.03 ? 230 TRP A CG 1 ATOM 1842 C CD1 . TRP A 1 230 ? 37.176 -24.860 6.473 1.00 81.76 ? 230 TRP A CD1 1 ATOM 1843 C CD2 . TRP A 1 230 ? 36.173 -26.654 5.592 1.00 81.74 ? 230 TRP A CD2 1 ATOM 1844 N NE1 . TRP A 1 230 ? 37.930 -25.274 5.406 1.00 79.80 ? 230 TRP A NE1 1 ATOM 1845 C CE2 . TRP A 1 230 ? 37.336 -26.375 4.847 1.00 81.27 ? 230 TRP A CE2 1 ATOM 1846 C CE3 . TRP A 1 230 ? 35.378 -27.746 5.222 1.00 82.37 ? 230 TRP A CE3 1 ATOM 1847 C CZ2 . TRP A 1 230 ? 37.723 -27.149 3.748 1.00 82.80 ? 230 TRP A CZ2 1 ATOM 1848 C CZ3 . TRP A 1 230 ? 35.762 -28.512 4.130 1.00 82.37 ? 230 TRP A CZ3 1 ATOM 1849 C CH2 . TRP A 1 230 ? 36.924 -28.212 3.408 1.00 82.15 ? 230 TRP A CH2 1 ATOM 1850 N N . THR A 1 231 ? 34.182 -28.395 8.403 1.00 84.63 ? 231 THR A N 1 ATOM 1851 C CA . THR A 1 231 ? 34.095 -29.766 7.915 1.00 84.60 ? 231 THR A CA 1 ATOM 1852 C C . THR A 1 231 ? 32.788 -29.982 7.160 1.00 84.84 ? 231 THR A C 1 ATOM 1853 O O . THR A 1 231 ? 31.852 -29.192 7.281 1.00 84.13 ? 231 THR A O 1 ATOM 1854 C CB . THR A 1 231 ? 34.190 -30.784 9.067 1.00 85.30 ? 231 THR A CB 1 ATOM 1855 O OG1 . THR A 1 231 ? 34.341 -32.103 8.532 1.00 84.82 ? 231 THR A OG1 1 ATOM 1856 C CG2 . THR A 1 231 ? 32.950 -30.738 9.948 1.00 85.81 ? 231 THR A CG2 1 ATOM 1857 N N . ILE A 1 232 ? 32.747 -31.045 6.364 1.00 85.94 ? 232 ILE A N 1 ATOM 1858 C CA . ILE A 1 232 ? 31.509 -31.508 5.757 1.00 86.29 ? 232 ILE A CA 1 ATOM 1859 C C . ILE A 1 232 ? 31.023 -32.666 6.599 1.00 87.71 ? 232 ILE A C 1 ATOM 1860 O O . ILE A 1 232 ? 31.671 -33.705 6.673 1.00 88.12 ? 232 ILE A O 1 ATOM 1861 C CB . ILE A 1 232 ? 31.697 -31.938 4.283 1.00 85.55 ? 232 ILE A CB 1 ATOM 1862 C CG1 . ILE A 1 232 ? 31.415 -30.761 3.350 1.00 84.21 ? 232 ILE A CG1 1 ATOM 1863 C CG2 . ILE A 1 232 ? 30.753 -33.075 3.903 1.00 87.24 ? 232 ILE A CG2 1 ATOM 1864 C CD1 . ILE A 1 232 ? 32.328 -29.583 3.565 1.00 84.04 ? 232 ILE A CD1 1 ATOM 1865 N N . LEU A 1 233 ? 29.885 -32.467 7.247 1.00 91.25 ? 233 LEU A N 1 ATOM 1866 C CA . LEU A 1 233 ? 29.264 -33.505 8.052 1.00 93.19 ? 233 LEU A CA 1 ATOM 1867 C C . LEU A 1 233 ? 28.341 -34.306 7.146 1.00 93.88 ? 233 LEU A C 1 ATOM 1868 O O . LEU A 1 233 ? 27.360 -33.775 6.622 1.00 92.94 ? 233 LEU A O 1 ATOM 1869 C CB . LEU A 1 233 ? 28.482 -32.877 9.205 1.00 94.82 ? 233 LEU A CB 1 ATOM 1870 C CG . LEU A 1 233 ? 27.888 -33.808 10.263 1.00 97.48 ? 233 LEU A CG 1 ATOM 1871 C CD1 . LEU A 1 233 ? 28.975 -34.547 11.034 1.00 97.93 ? 233 LEU A CD1 1 ATOM 1872 C CD2 . LEU A 1 233 ? 27.014 -33.000 11.209 1.00 98.29 ? 233 LEU A CD2 1 ATOM 1873 N N . LYS A 1 234 ? 28.664 -35.579 6.960 1.00 95.40 ? 234 LYS A N 1 ATOM 1874 C CA . LYS A 1 234 ? 27.911 -36.444 6.056 1.00 99.03 ? 234 LYS A CA 1 ATOM 1875 C C . LYS A 1 234 ? 26.501 -36.749 6.589 1.00 101.03 ? 234 LYS A C 1 ATOM 1876 O O . LYS A 1 234 ? 26.192 -36.428 7.740 1.00 101.19 ? 234 LYS A O 1 ATOM 1877 C CB . LYS A 1 234 ? 28.709 -37.731 5.805 1.00 102.86 ? 234 LYS A CB 1 ATOM 1878 C CG . LYS A 1 234 ? 29.905 -37.514 4.879 1.00 104.20 ? 234 LYS A CG 1 ATOM 1879 C CD . LYS A 1 234 ? 30.539 -38.817 4.418 1.00 108.35 ? 234 LYS A CD 1 ATOM 1880 C CE . LYS A 1 234 ? 29.591 -39.625 3.538 1.00 113.11 ? 234 LYS A CE 1 ATOM 1881 N NZ . LYS A 1 234 ? 30.300 -40.604 2.667 1.00 115.25 ? 234 LYS A NZ 1 ATOM 1882 N N . PRO A 1 235 ? 25.627 -37.340 5.743 1.00 103.06 ? 235 PRO A N 1 ATOM 1883 C CA . PRO A 1 235 ? 24.309 -37.734 6.257 1.00 103.29 ? 235 PRO A CA 1 ATOM 1884 C C . PRO A 1 235 ? 24.444 -38.784 7.347 1.00 105.07 ? 235 PRO A C 1 ATOM 1885 O O . PRO A 1 235 ? 25.357 -39.608 7.284 1.00 105.48 ? 235 PRO A O 1 ATOM 1886 C CB . PRO A 1 235 ? 23.599 -38.334 5.033 1.00 104.63 ? 235 PRO A CB 1 ATOM 1887 C CG . PRO A 1 235 ? 24.662 -38.585 4.018 1.00 103.17 ? 235 PRO A CG 1 ATOM 1888 C CD . PRO A 1 235 ? 25.765 -37.614 4.298 1.00 101.50 ? 235 PRO A CD 1 ATOM 1889 N N . ASN A 1 236 ? 23.560 -38.738 8.345 1.00 106.98 ? 236 ASN A N 1 ATOM 1890 C CA . ASN A 1 236 ? 23.546 -39.722 9.433 1.00 107.87 ? 236 ASN A CA 1 ATOM 1891 C C . ASN A 1 236 ? 24.767 -39.699 10.357 1.00 107.11 ? 236 ASN A C 1 ATOM 1892 O O . ASN A 1 236 ? 24.876 -40.534 11.253 1.00 108.88 ? 236 ASN A O 1 ATOM 1893 C CB . ASN A 1 236 ? 23.361 -41.145 8.870 1.00 109.76 ? 236 ASN A CB 1 ATOM 1894 C CG . ASN A 1 236 ? 21.990 -41.713 9.155 1.00 112.97 ? 236 ASN A CG 1 ATOM 1895 O OD1 . ASN A 1 236 ? 21.488 -41.624 10.274 1.00 115.37 ? 236 ASN A OD1 1 ATOM 1896 N ND2 . ASN A 1 236 ? 21.383 -42.319 8.144 1.00 114.04 ? 236 ASN A ND2 1 ATOM 1897 N N . ASP A 1 237 ? 25.683 -38.758 10.147 1.00 105.09 ? 237 ASP A N 1 ATOM 1898 C CA . ASP A 1 237 ? 26.837 -38.620 11.025 1.00 104.82 ? 237 ASP A CA 1 ATOM 1899 C C . ASP A 1 237 ? 26.546 -37.513 12.030 1.00 103.88 ? 237 ASP A C 1 ATOM 1900 O O . ASP A 1 237 ? 25.647 -36.692 11.825 1.00 102.12 ? 237 ASP A O 1 ATOM 1901 C CB . ASP A 1 237 ? 28.104 -38.306 10.218 1.00 103.62 ? 237 ASP A CB 1 ATOM 1902 C CG . ASP A 1 237 ? 29.390 -38.612 10.986 1.00 104.00 ? 237 ASP A CG 1 ATOM 1903 O OD1 . ASP A 1 237 ? 29.349 -39.379 11.974 1.00 105.33 ? 237 ASP A OD1 1 ATOM 1904 O OD2 . ASP A 1 237 ? 30.451 -38.086 10.593 1.00 102.94 ? 237 ASP A OD2 1 ATOM 1905 N N . ALA A 1 238 ? 27.302 -37.505 13.121 1.00 104.26 ? 238 ALA A N 1 ATOM 1906 C CA . ALA A 1 238 ? 27.112 -36.525 14.180 1.00 104.77 ? 238 ALA A CA 1 ATOM 1907 C C . ALA A 1 238 ? 28.434 -35.859 14.525 1.00 103.04 ? 238 ALA A C 1 ATOM 1908 O O . ALA A 1 238 ? 29.467 -36.527 14.604 1.00 104.82 ? 238 ALA A O 1 ATOM 1909 C CB . ALA A 1 238 ? 26.520 -37.198 15.410 1.00 106.22 ? 238 ALA A CB 1 ATOM 1910 N N . ILE A 1 239 ? 28.399 -34.543 14.715 1.00 101.10 ? 239 ILE A N 1 ATOM 1911 C CA . ILE A 1 239 ? 29.573 -33.801 15.177 1.00 100.20 ? 239 ILE A CA 1 ATOM 1912 C C . ILE A 1 239 ? 29.508 -33.604 16.705 1.00 102.56 ? 239 ILE A C 1 ATOM 1913 O O . ILE A 1 239 ? 28.432 -33.384 17.266 1.00 102.21 ? 239 ILE A O 1 ATOM 1914 C CB . ILE A 1 239 ? 29.725 -32.455 14.431 1.00 97.66 ? 239 ILE A CB 1 ATOM 1915 C CG1 . ILE A 1 239 ? 31.143 -31.907 14.604 1.00 97.40 ? 239 ILE A CG1 1 ATOM 1916 C CG2 . ILE A 1 239 ? 28.690 -31.437 14.896 1.00 97.96 ? 239 ILE A CG2 1 ATOM 1917 C CD1 . ILE A 1 239 ? 31.485 -30.785 13.648 1.00 95.51 ? 239 ILE A CD1 1 ATOM 1918 N N . ASN A 1 240 ? 30.663 -33.702 17.365 1.00 103.30 ? 240 ASN A N 1 ATOM 1919 C CA . ASN A 1 240 ? 30.749 -33.646 18.827 1.00 105.46 ? 240 ASN A CA 1 ATOM 1920 C C . ASN A 1 240 ? 31.698 -32.560 19.300 1.00 105.20 ? 240 ASN A C 1 ATOM 1921 O O . ASN A 1 240 ? 32.895 -32.621 19.025 1.00 104.53 ? 240 ASN A O 1 ATOM 1922 C CB . ASN A 1 240 ? 31.250 -34.974 19.371 1.00 106.82 ? 240 ASN A CB 1 ATOM 1923 C CG . ASN A 1 240 ? 30.337 -36.125 19.027 1.00 109.15 ? 240 ASN A CG 1 ATOM 1924 O OD1 . ASN A 1 240 ? 29.199 -36.182 19.492 1.00 109.46 ? 240 ASN A OD1 1 ATOM 1925 N ND2 . ASN A 1 240 ? 30.832 -37.059 18.214 1.00 109.42 ? 240 ASN A ND2 1 ATOM 1926 N N . PHE A 1 241 ? 31.168 -31.585 20.031 1.00 106.78 ? 241 PHE A N 1 ATOM 1927 C CA . PHE A 1 241 ? 31.976 -30.500 20.568 1.00 107.26 ? 241 PHE A CA 1 ATOM 1928 C C . PHE A 1 241 ? 32.137 -30.625 22.077 1.00 110.12 ? 241 PHE A C 1 ATOM 1929 O O . PHE A 1 241 ? 31.149 -30.702 22.807 1.00 112.31 ? 241 PHE A O 1 ATOM 1930 C CB . PHE A 1 241 ? 31.343 -29.155 20.225 1.00 106.92 ? 241 PHE A CB 1 ATOM 1931 C CG . PHE A 1 241 ? 31.411 -28.814 18.766 1.00 106.36 ? 241 PHE A CG 1 ATOM 1932 C CD1 . PHE A 1 241 ? 32.579 -28.299 18.216 1.00 105.42 ? 241 PHE A CD1 1 ATOM 1933 C CD2 . PHE A 1 241 ? 30.315 -29.011 17.940 1.00 106.18 ? 241 PHE A CD2 1 ATOM 1934 C CE1 . PHE A 1 241 ? 32.652 -27.981 16.871 1.00 104.44 ? 241 PHE A CE1 1 ATOM 1935 C CE2 . PHE A 1 241 ? 30.380 -28.694 16.594 1.00 105.44 ? 241 PHE A CE2 1 ATOM 1936 C CZ . PHE A 1 241 ? 31.551 -28.180 16.058 1.00 104.42 ? 241 PHE A CZ 1 ATOM 1937 N N . GLU A 1 242 ? 33.387 -30.661 22.530 1.00 110.87 ? 242 GLU A N 1 ATOM 1938 C CA . GLU A 1 242 ? 33.709 -30.535 23.947 1.00 113.57 ? 242 GLU A CA 1 ATOM 1939 C C . GLU A 1 242 ? 34.768 -29.442 24.122 1.00 112.75 ? 242 GLU A C 1 ATOM 1940 O O . GLU A 1 242 ? 35.781 -29.435 23.421 1.00 110.40 ? 242 GLU A O 1 ATOM 1941 C CB . GLU A 1 242 ? 34.187 -31.874 24.533 1.00 116.28 ? 242 GLU A CB 1 ATOM 1942 C CG . GLU A 1 242 ? 34.569 -31.816 26.014 1.00 120.03 ? 242 GLU A CG 1 ATOM 1943 C CD . GLU A 1 242 ? 34.998 -33.160 26.583 1.00 121.50 ? 242 GLU A CD 1 ATOM 1944 O OE1 . GLU A 1 242 ? 34.275 -34.160 26.385 1.00 121.98 ? 242 GLU A OE1 1 ATOM 1945 O OE2 . GLU A 1 242 ? 36.057 -33.213 27.246 1.00 121.14 ? 242 GLU A OE2 1 ATOM 1946 N N . SER A 1 243 ? 34.520 -28.518 25.052 1.00 114.00 ? 243 SER A N 1 ATOM 1947 C CA . SER A 1 243 ? 35.456 -27.428 25.333 1.00 113.91 ? 243 SER A CA 1 ATOM 1948 C C . SER A 1 243 ? 35.219 -26.823 26.709 1.00 117.49 ? 243 SER A C 1 ATOM 1949 O O . SER A 1 243 ? 34.129 -26.947 27.262 1.00 121.94 ? 243 SER A O 1 ATOM 1950 C CB . SER A 1 243 ? 35.323 -26.332 24.279 1.00 111.25 ? 243 SER A CB 1 ATOM 1951 O OG . SER A 1 243 ? 36.177 -25.240 24.574 1.00 110.34 ? 243 SER A OG 1 ATOM 1952 N N . ASN A 1 244 ? 36.245 -26.159 27.241 1.00 118.16 ? 244 ASN A N 1 ATOM 1953 C CA . ASN A 1 244 ? 36.155 -25.451 28.531 1.00 120.85 ? 244 ASN A CA 1 ATOM 1954 C C . ASN A 1 244 ? 36.581 -23.976 28.430 1.00 119.79 ? 244 ASN A C 1 ATOM 1955 O O . ASN A 1 244 ? 36.939 -23.354 29.438 1.00 120.27 ? 244 ASN A O 1 ATOM 1956 C CB . ASN A 1 244 ? 36.989 -26.174 29.600 1.00 122.44 ? 244 ASN A CB 1 ATOM 1957 C CG . ASN A 1 244 ? 38.462 -26.263 29.236 1.00 121.72 ? 244 ASN A CG 1 ATOM 1958 O OD1 . ASN A 1 244 ? 38.838 -26.122 28.066 1.00 118.82 ? 244 ASN A OD1 1 ATOM 1959 N ND2 . ASN A 1 244 ? 39.304 -26.507 30.234 1.00 121.91 ? 244 ASN A ND2 1 ATOM 1960 N N . GLY A 1 245 ? 36.528 -23.427 27.216 1.00 116.14 ? 245 GLY A N 1 ATOM 1961 C CA . GLY A 1 245 ? 36.860 -22.026 26.977 1.00 115.67 ? 245 GLY A CA 1 ATOM 1962 C C . GLY A 1 245 ? 37.379 -21.769 25.575 1.00 113.62 ? 245 GLY A C 1 ATOM 1963 O O . GLY A 1 245 ? 37.847 -22.686 24.895 1.00 113.64 ? 245 GLY A O 1 ATOM 1964 N N . ASN A 1 246 ? 37.292 -20.507 25.153 1.00 112.45 ? 246 ASN A N 1 ATOM 1965 C CA . ASN A 1 246 ? 37.815 -20.035 23.861 1.00 109.27 ? 246 ASN A CA 1 ATOM 1966 C C . ASN A 1 246 ? 37.052 -20.568 22.647 1.00 106.15 ? 246 ASN A C 1 ATOM 1967 O O . ASN A 1 246 ? 37.535 -20.492 21.523 1.00 103.63 ? 246 ASN A O 1 ATOM 1968 C CB . ASN A 1 246 ? 39.316 -20.345 23.722 1.00 108.57 ? 246 ASN A CB 1 ATOM 1969 C CG . ASN A 1 246 ? 40.133 -19.824 24.894 1.00 110.78 ? 246 ASN A CG 1 ATOM 1970 O OD1 . ASN A 1 246 ? 39.985 -20.286 26.025 1.00 111.31 ? 246 ASN A OD1 1 ATOM 1971 N ND2 . ASN A 1 246 ? 41.009 -18.864 24.623 1.00 110.60 ? 246 ASN A ND2 1 ATOM 1972 N N . PHE A 1 247 ? 35.840 -21.063 22.878 1.00 107.03 ? 247 PHE A N 1 ATOM 1973 C CA . PHE A 1 247 ? 35.060 -21.736 21.849 1.00 103.41 ? 247 PHE A CA 1 ATOM 1974 C C . PHE A 1 247 ? 34.156 -20.758 21.104 1.00 102.14 ? 247 PHE A C 1 ATOM 1975 O O . PHE A 1 247 ? 33.381 -20.024 21.714 1.00 103.89 ? 247 PHE A O 1 ATOM 1976 C CB . PHE A 1 247 ? 34.230 -22.849 22.503 1.00 105.20 ? 247 PHE A CB 1 ATOM 1977 C CG . PHE A 1 247 ? 33.446 -23.697 21.536 1.00 103.75 ? 247 PHE A CG 1 ATOM 1978 C CD1 . PHE A 1 247 ? 34.011 -24.150 20.350 1.00 101.24 ? 247 PHE A CD1 1 ATOM 1979 C CD2 . PHE A 1 247 ? 32.147 -24.081 21.840 1.00 104.92 ? 247 PHE A CD2 1 ATOM 1980 C CE1 . PHE A 1 247 ? 33.286 -24.940 19.477 1.00 100.02 ? 247 PHE A CE1 1 ATOM 1981 C CE2 . PHE A 1 247 ? 31.421 -24.875 20.970 1.00 103.31 ? 247 PHE A CE2 1 ATOM 1982 C CZ . PHE A 1 247 ? 31.990 -25.304 19.788 1.00 101.23 ? 247 PHE A CZ 1 ATOM 1983 N N . ILE A 1 248 ? 34.279 -20.739 19.781 1.00 101.14 ? 248 ILE A N 1 ATOM 1984 C CA . ILE A 1 248 ? 33.352 -20.014 18.926 1.00 99.65 ? 248 ILE A CA 1 ATOM 1985 C C . ILE A 1 248 ? 32.438 -21.080 18.343 1.00 98.62 ? 248 ILE A C 1 ATOM 1986 O O . ILE A 1 248 ? 32.851 -21.863 17.486 1.00 96.52 ? 248 ILE A O 1 ATOM 1987 C CB . ILE A 1 248 ? 34.074 -19.230 17.807 1.00 98.21 ? 248 ILE A CB 1 ATOM 1988 C CG1 . ILE A 1 248 ? 35.305 -18.486 18.348 1.00 99.00 ? 248 ILE A CG1 1 ATOM 1989 C CG2 . ILE A 1 248 ? 33.119 -18.246 17.153 1.00 98.05 ? 248 ILE A CG2 1 ATOM 1990 C CD1 . ILE A 1 248 ? 35.008 -17.502 19.459 1.00 101.50 ? 248 ILE A CD1 1 ATOM 1991 N N . ALA A 1 249 ? 31.203 -21.124 18.831 1.00 99.89 ? 249 ALA A N 1 ATOM 1992 C CA . ALA A 1 249 ? 30.299 -22.241 18.547 1.00 100.93 ? 249 ALA A CA 1 ATOM 1993 C C . ALA A 1 249 ? 29.424 -22.009 17.308 1.00 99.36 ? 249 ALA A C 1 ATOM 1994 O O . ALA A 1 249 ? 29.058 -20.873 17.011 1.00 99.31 ? 249 ALA A O 1 ATOM 1995 C CB . ALA A 1 249 ? 29.420 -22.510 19.759 1.00 103.54 ? 249 ALA A CB 1 ATOM 1996 N N . PRO A 1 250 ? 29.082 -23.091 16.585 1.00 98.23 ? 250 PRO A N 1 ATOM 1997 C CA . PRO A 1 250 ? 28.125 -22.985 15.481 1.00 97.73 ? 250 PRO A CA 1 ATOM 1998 C C . PRO A 1 250 ? 26.745 -22.517 15.939 1.00 100.96 ? 250 PRO A C 1 ATOM 1999 O O . PRO A 1 250 ? 26.250 -22.992 16.956 1.00 104.26 ? 250 PRO A O 1 ATOM 2000 C CB . PRO A 1 250 ? 28.021 -24.422 14.958 1.00 95.94 ? 250 PRO A CB 1 ATOM 2001 C CG . PRO A 1 250 ? 29.257 -25.103 15.410 1.00 95.78 ? 250 PRO A CG 1 ATOM 2002 C CD . PRO A 1 250 ? 29.671 -24.439 16.684 1.00 97.71 ? 250 PRO A CD 1 ATOM 2003 N N . GLU A 1 251 ? 26.147 -21.586 15.199 1.00 102.15 ? 251 GLU A N 1 ATOM 2004 C CA . GLU A 1 251 ? 24.741 -21.214 15.379 1.00 104.95 ? 251 GLU A CA 1 ATOM 2005 C C . GLU A 1 251 ? 23.990 -21.789 14.174 1.00 102.85 ? 251 GLU A C 1 ATOM 2006 O O . GLU A 1 251 ? 23.123 -22.658 14.320 1.00 100.65 ? 251 GLU A O 1 ATOM 2007 C CB . GLU A 1 251 ? 24.589 -19.682 15.461 1.00 107.47 ? 251 GLU A CB 1 ATOM 2008 C CG . GLU A 1 251 ? 23.715 -19.160 16.598 1.00 113.28 ? 251 GLU A CG 1 ATOM 2009 C CD . GLU A 1 251 ? 22.229 -19.133 16.276 1.00 116.49 ? 251 GLU A CD 1 ATOM 2010 O OE1 . GLU A 1 251 ? 21.674 -20.194 15.932 1.00 118.56 ? 251 GLU A OE1 1 ATOM 2011 O OE2 . GLU A 1 251 ? 21.611 -18.051 16.389 1.00 117.86 ? 251 GLU A OE2 1 ATOM 2012 N N . TYR A 1 252 ? 24.365 -21.316 12.983 1.00 99.88 ? 252 TYR A N 1 ATOM 2013 C CA . TYR A 1 252 ? 23.792 -21.776 11.722 1.00 98.47 ? 252 TYR A CA 1 ATOM 2014 C C . TYR A 1 252 ? 24.820 -22.560 10.912 1.00 96.56 ? 252 TYR A C 1 ATOM 2015 O O . TYR A 1 252 ? 26.029 -22.360 11.054 1.00 93.80 ? 252 TYR A O 1 ATOM 2016 C CB . TYR A 1 252 ? 23.308 -20.584 10.895 1.00 98.51 ? 252 TYR A CB 1 ATOM 2017 C CG . TYR A 1 252 ? 22.251 -19.746 11.574 1.00 102.89 ? 252 TYR A CG 1 ATOM 2018 C CD1 . TYR A 1 252 ? 20.910 -20.122 11.540 1.00 105.71 ? 252 TYR A CD1 1 ATOM 2019 C CD2 . TYR A 1 252 ? 22.587 -18.579 12.256 1.00 103.92 ? 252 TYR A CD2 1 ATOM 2020 C CE1 . TYR A 1 252 ? 19.935 -19.360 12.168 1.00 107.57 ? 252 TYR A CE1 1 ATOM 2021 C CE2 . TYR A 1 252 ? 21.619 -17.809 12.883 1.00 106.01 ? 252 TYR A CE2 1 ATOM 2022 C CZ . TYR A 1 252 ? 20.293 -18.205 12.835 1.00 107.68 ? 252 TYR A CZ 1 ATOM 2023 O OH . TYR A 1 252 ? 19.323 -17.448 13.455 1.00 109.26 ? 252 TYR A OH 1 ATOM 2024 N N . ALA A 1 253 ? 24.328 -23.451 10.057 1.00 97.14 ? 253 ALA A N 1 ATOM 2025 C CA . ALA A 1 253 ? 25.172 -24.191 9.120 1.00 95.43 ? 253 ALA A CA 1 ATOM 2026 C C . ALA A 1 253 ? 24.434 -24.392 7.793 1.00 95.56 ? 253 ALA A C 1 ATOM 2027 O O . ALA A 1 253 ? 23.208 -24.506 7.772 1.00 98.34 ? 253 ALA A O 1 ATOM 2028 C CB . ALA A 1 253 ? 25.574 -25.528 9.722 1.00 96.08 ? 253 ALA A CB 1 ATOM 2029 N N . TYR A 1 254 ? 25.187 -24.440 6.697 1.00 94.11 ? 254 TYR A N 1 ATOM 2030 C CA . TYR A 1 254 ? 24.614 -24.480 5.352 1.00 93.77 ? 254 TYR A CA 1 ATOM 2031 C C . TYR A 1 254 ? 24.412 -25.907 4.824 1.00 94.36 ? 254 TYR A C 1 ATOM 2032 O O . TYR A 1 254 ? 25.342 -26.713 4.829 1.00 93.81 ? 254 TYR A O 1 ATOM 2033 C CB . TYR A 1 254 ? 25.523 -23.727 4.379 1.00 92.48 ? 254 TYR A CB 1 ATOM 2034 C CG . TYR A 1 254 ? 25.734 -22.257 4.688 1.00 91.74 ? 254 TYR A CG 1 ATOM 2035 C CD1 . TYR A 1 254 ? 26.780 -21.839 5.506 1.00 90.85 ? 254 TYR A CD1 1 ATOM 2036 C CD2 . TYR A 1 254 ? 24.906 -21.283 4.133 1.00 92.03 ? 254 TYR A CD2 1 ATOM 2037 C CE1 . TYR A 1 254 ? 26.984 -20.493 5.775 1.00 90.82 ? 254 TYR A CE1 1 ATOM 2038 C CE2 . TYR A 1 254 ? 25.102 -19.936 4.394 1.00 92.15 ? 254 TYR A CE2 1 ATOM 2039 C CZ . TYR A 1 254 ? 26.141 -19.543 5.214 1.00 92.18 ? 254 TYR A CZ 1 ATOM 2040 O OH . TYR A 1 254 ? 26.326 -18.202 5.474 1.00 93.86 ? 254 TYR A OH 1 ATOM 2041 N N . LYS A 1 255 ? 23.202 -26.205 4.354 1.00 96.22 ? 255 LYS A N 1 ATOM 2042 C CA . LYS A 1 255 ? 22.932 -27.458 3.646 1.00 97.20 ? 255 LYS A CA 1 ATOM 2043 C C . LYS A 1 255 ? 23.331 -27.318 2.183 1.00 95.40 ? 255 LYS A C 1 ATOM 2044 O O . LYS A 1 255 ? 23.022 -26.311 1.548 1.00 93.22 ? 255 LYS A O 1 ATOM 2045 C CB . LYS A 1 255 ? 21.445 -27.825 3.706 1.00 100.82 ? 255 LYS A CB 1 ATOM 2046 C CG . LYS A 1 255 ? 20.881 -27.988 5.105 1.00 102.48 ? 255 LYS A CG 1 ATOM 2047 C CD . LYS A 1 255 ? 19.700 -28.951 5.143 1.00 105.42 ? 255 LYS A CD 1 ATOM 2048 C CE . LYS A 1 255 ? 18.470 -28.408 4.437 1.00 107.31 ? 255 LYS A CE 1 ATOM 2049 N NZ . LYS A 1 255 ? 17.308 -29.328 4.609 1.00 110.68 ? 255 LYS A NZ 1 ATOM 2050 N N . ILE A 1 256 ? 24.006 -28.337 1.655 1.00 95.80 ? 256 ILE A N 1 ATOM 2051 C CA . ILE A 1 256 ? 24.365 -28.393 0.241 1.00 95.66 ? 256 ILE A CA 1 ATOM 2052 C C . ILE A 1 256 ? 23.246 -29.086 -0.529 1.00 97.25 ? 256 ILE A C 1 ATOM 2053 O O . ILE A 1 256 ? 23.223 -30.313 -0.638 1.00 96.19 ? 256 ILE A O 1 ATOM 2054 C CB . ILE A 1 256 ? 25.671 -29.177 0.023 1.00 95.66 ? 256 ILE A CB 1 ATOM 2055 C CG1 . ILE A 1 256 ? 26.825 -28.511 0.771 1.00 95.52 ? 256 ILE A CG1 1 ATOM 2056 C CG2 . ILE A 1 256 ? 25.994 -29.268 -1.464 1.00 95.64 ? 256 ILE A CG2 1 ATOM 2057 C CD1 . ILE A 1 256 ? 28.036 -29.402 0.950 1.00 95.55 ? 256 ILE A CD1 1 ATOM 2058 N N . VAL A 1 257 ? 22.324 -28.298 -1.068 1.00 98.97 ? 257 VAL A N 1 ATOM 2059 C CA . VAL A 1 257 ? 21.141 -28.858 -1.731 1.00 103.17 ? 257 VAL A CA 1 ATOM 2060 C C . VAL A 1 257 ? 21.373 -29.150 -3.218 1.00 105.06 ? 257 VAL A C 1 ATOM 2061 O O . VAL A 1 257 ? 20.862 -30.148 -3.743 1.00 106.51 ? 257 VAL A O 1 ATOM 2062 C CB . VAL A 1 257 ? 19.883 -27.971 -1.538 1.00 104.87 ? 257 VAL A CB 1 ATOM 2063 C CG1 . VAL A 1 257 ? 19.371 -28.090 -0.110 1.00 105.56 ? 257 VAL A CG1 1 ATOM 2064 C CG2 . VAL A 1 257 ? 20.152 -26.511 -1.881 1.00 104.06 ? 257 VAL A CG2 1 ATOM 2065 N N . LYS A 1 258 ? 22.149 -28.291 -3.882 1.00 103.99 ? 258 LYS A N 1 ATOM 2066 C CA . LYS A 1 258 ? 22.410 -28.415 -5.317 1.00 105.64 ? 258 LYS A CA 1 ATOM 2067 C C . LYS A 1 258 ? 23.897 -28.453 -5.612 1.00 102.18 ? 258 LYS A C 1 ATOM 2068 O O . LYS A 1 258 ? 24.634 -27.568 -5.189 1.00 101.44 ? 258 LYS A O 1 ATOM 2069 C CB . LYS A 1 258 ? 21.794 -27.235 -6.067 1.00 108.08 ? 258 LYS A CB 1 ATOM 2070 C CG . LYS A 1 258 ? 20.359 -27.462 -6.515 1.00 112.53 ? 258 LYS A CG 1 ATOM 2071 C CD . LYS A 1 258 ? 20.285 -28.065 -7.909 1.00 115.01 ? 258 LYS A CD 1 ATOM 2072 C CE . LYS A 1 258 ? 20.899 -27.145 -8.954 1.00 114.83 ? 258 LYS A CE 1 ATOM 2073 N NZ . LYS A 1 258 ? 20.208 -27.240 -10.270 1.00 116.65 ? 258 LYS A NZ 1 ATOM 2074 N N . LYS A 1 259 ? 24.326 -29.475 -6.347 1.00 101.63 ? 259 LYS A N 1 ATOM 2075 C CA . LYS A 1 259 ? 25.699 -29.568 -6.834 1.00 100.28 ? 259 LYS A CA 1 ATOM 2076 C C . LYS A 1 259 ? 25.725 -29.387 -8.348 1.00 100.57 ? 259 LYS A C 1 ATOM 2077 O O . LYS A 1 259 ? 24.684 -29.420 -8.998 1.00 102.66 ? 259 LYS A O 1 ATOM 2078 C CB . LYS A 1 259 ? 26.311 -30.908 -6.431 1.00 100.37 ? 259 LYS A CB 1 ATOM 2079 C CG . LYS A 1 259 ? 26.519 -31.026 -4.929 1.00 101.19 ? 259 LYS A CG 1 ATOM 2080 C CD . LYS A 1 259 ? 27.025 -32.393 -4.502 1.00 101.53 ? 259 LYS A CD 1 ATOM 2081 C CE . LYS A 1 259 ? 27.138 -32.467 -2.985 1.00 101.52 ? 259 LYS A CE 1 ATOM 2082 N NZ . LYS A 1 259 ? 27.472 -33.830 -2.486 1.00 101.96 ? 259 LYS A NZ 1 ATOM 2083 N N . GLY A 1 260 ? 26.912 -29.171 -8.904 1.00 101.10 ? 260 GLY A N 1 ATOM 2084 C CA . GLY A 1 260 ? 27.063 -29.003 -10.350 1.00 102.24 ? 260 GLY A CA 1 ATOM 2085 C C . GLY A 1 260 ? 28.090 -27.960 -10.733 1.00 101.21 ? 260 GLY A C 1 ATOM 2086 O O . GLY A 1 260 ? 28.850 -27.480 -9.895 1.00 101.21 ? 260 GLY A O 1 ATOM 2087 N N . ASP A 1 261 ? 28.101 -27.602 -12.011 1.00 102.24 ? 261 ASP A N 1 ATOM 2088 C CA . ASP A 1 261 ? 29.112 -26.699 -12.544 1.00 101.99 ? 261 ASP A CA 1 ATOM 2089 C C . ASP A 1 261 ? 28.912 -25.273 -12.058 1.00 96.88 ? 261 ASP A C 1 ATOM 2090 O O . ASP A 1 261 ? 27.811 -24.732 -12.121 1.00 96.89 ? 261 ASP A O 1 ATOM 2091 C CB . ASP A 1 261 ? 29.123 -26.736 -14.078 1.00 106.11 ? 261 ASP A CB 1 ATOM 2092 C CG . ASP A 1 261 ? 29.734 -28.013 -14.628 1.00 110.53 ? 261 ASP A CG 1 ATOM 2093 O OD1 . ASP A 1 261 ? 30.307 -28.790 -13.830 1.00 112.19 ? 261 ASP A OD1 1 ATOM 2094 O OD2 . ASP A 1 261 ? 29.647 -28.240 -15.858 1.00 115.17 ? 261 ASP A OD2 1 ATOM 2095 N N . SER A 1 262 ? 29.996 -24.682 -11.573 1.00 91.61 ? 262 SER A N 1 ATOM 2096 C CA . SER A 1 262 ? 30.007 -23.301 -11.116 1.00 91.37 ? 262 SER A CA 1 ATOM 2097 C C . SER A 1 262 ? 31.459 -22.837 -11.064 1.00 89.83 ? 262 SER A C 1 ATOM 2098 O O . SER A 1 262 ? 32.368 -23.599 -11.400 1.00 91.69 ? 262 SER A O 1 ATOM 2099 C CB . SER A 1 262 ? 29.349 -23.185 -9.736 1.00 92.12 ? 262 SER A CB 1 ATOM 2100 O OG . SER A 1 262 ? 29.430 -21.864 -9.221 1.00 92.91 ? 262 SER A OG 1 ATOM 2101 N N . THR A 1 263 ? 31.680 -21.594 -10.649 1.00 90.03 ? 263 THR A N 1 ATOM 2102 C CA . THR A 1 263 ? 33.028 -21.048 -10.591 1.00 84.54 ? 263 THR A CA 1 ATOM 2103 C C . THR A 1 263 ? 33.073 -19.749 -9.803 1.00 81.30 ? 263 THR A C 1 ATOM 2104 O O . THR A 1 263 ? 32.102 -18.995 -9.772 1.00 80.76 ? 263 THR A O 1 ATOM 2105 C CB . THR A 1 263 ? 33.592 -20.799 -12.009 1.00 81.98 ? 263 THR A CB 1 ATOM 2106 O OG1 . THR A 1 263 ? 34.993 -20.537 -11.931 1.00 80.34 ? 263 THR A OG1 1 ATOM 2107 C CG2 . THR A 1 263 ? 32.908 -19.625 -12.686 1.00 80.77 ? 263 THR A CG2 1 ATOM 2108 N N . ILE A 1 264 ? 34.210 -19.500 -9.166 1.00 79.65 ? 264 ILE A N 1 ATOM 2109 C CA . ILE A 1 264 ? 34.456 -18.230 -8.504 1.00 77.47 ? 264 ILE A CA 1 ATOM 2110 C C . ILE A 1 264 ? 35.280 -17.373 -9.452 1.00 76.26 ? 264 ILE A C 1 ATOM 2111 O O . ILE A 1 264 ? 36.433 -17.678 -9.747 1.00 76.54 ? 264 ILE A O 1 ATOM 2112 C CB . ILE A 1 264 ? 35.178 -18.406 -7.160 1.00 76.93 ? 264 ILE A CB 1 ATOM 2113 C CG1 . ILE A 1 264 ? 34.379 -19.356 -6.270 1.00 79.27 ? 264 ILE A CG1 1 ATOM 2114 C CG2 . ILE A 1 264 ? 35.345 -17.061 -6.472 1.00 75.49 ? 264 ILE A CG2 1 ATOM 2115 C CD1 . ILE A 1 264 ? 35.096 -19.772 -5.009 1.00 81.19 ? 264 ILE A CD1 1 ATOM 2116 N N . MET A 1 265 ? 34.659 -16.302 -9.928 1.00 76.48 ? 265 MET A N 1 ATOM 2117 C CA . MET A 1 265 ? 35.233 -15.415 -10.919 1.00 74.85 ? 265 MET A CA 1 ATOM 2118 C C . MET A 1 265 ? 35.792 -14.189 -10.210 1.00 75.05 ? 265 MET A C 1 ATOM 2119 O O . MET A 1 265 ? 35.186 -13.683 -9.267 1.00 75.93 ? 265 MET A O 1 ATOM 2120 C CB . MET A 1 265 ? 34.127 -15.015 -11.887 1.00 76.40 ? 265 MET A CB 1 ATOM 2121 C CG . MET A 1 265 ? 34.572 -14.453 -13.218 1.00 76.25 ? 265 MET A CG 1 ATOM 2122 S SD . MET A 1 265 ? 33.135 -14.269 -14.296 1.00 78.57 ? 265 MET A SD 1 ATOM 2123 C CE . MET A 1 265 ? 32.961 -15.942 -14.918 1.00 78.55 ? 265 MET A CE 1 ATOM 2124 N N . LYS A 1 266 ? 36.956 -13.731 -10.654 1.00 75.79 ? 266 LYS A N 1 ATOM 2125 C CA . LYS A 1 266 ? 37.618 -12.574 -10.076 1.00 77.93 ? 266 LYS A CA 1 ATOM 2126 C C . LYS A 1 266 ? 37.371 -11.380 -10.969 1.00 77.61 ? 266 LYS A C 1 ATOM 2127 O O . LYS A 1 266 ? 37.803 -11.370 -12.122 1.00 78.99 ? 266 LYS A O 1 ATOM 2128 C CB . LYS A 1 266 ? 39.117 -12.827 -9.962 1.00 82.18 ? 266 LYS A CB 1 ATOM 2129 C CG . LYS A 1 266 ? 39.475 -13.779 -8.838 1.00 87.09 ? 266 LYS A CG 1 ATOM 2130 C CD . LYS A 1 266 ? 39.628 -13.044 -7.512 1.00 90.95 ? 266 LYS A CD 1 ATOM 2131 C CE . LYS A 1 266 ? 38.881 -13.736 -6.386 1.00 93.99 ? 266 LYS A CE 1 ATOM 2132 N NZ . LYS A 1 266 ? 39.149 -15.199 -6.327 1.00 96.20 ? 266 LYS A NZ 1 ATOM 2133 N N . SER A 1 267 ? 36.682 -10.375 -10.442 1.00 78.60 ? 267 SER A N 1 ATOM 2134 C CA . SER A 1 267 ? 36.275 -9.221 -11.237 1.00 79.17 ? 267 SER A CA 1 ATOM 2135 C C . SER A 1 267 ? 35.887 -8.043 -10.349 1.00 80.79 ? 267 SER A C 1 ATOM 2136 O O . SER A 1 267 ? 35.308 -8.224 -9.278 1.00 82.49 ? 267 SER A O 1 ATOM 2137 C CB . SER A 1 267 ? 35.096 -9.607 -12.135 1.00 79.53 ? 267 SER A CB 1 ATOM 2138 O OG . SER A 1 267 ? 34.699 -8.526 -12.959 1.00 81.60 ? 267 SER A OG 1 ATOM 2139 N N . GLU A 1 268 ? 36.218 -6.838 -10.796 1.00 81.84 ? 268 GLU A N 1 ATOM 2140 C CA . GLU A 1 268 ? 35.801 -5.624 -10.110 1.00 84.12 ? 268 GLU A CA 1 ATOM 2141 C C . GLU A 1 268 ? 34.446 -5.141 -10.620 1.00 85.07 ? 268 GLU A C 1 ATOM 2142 O O . GLU A 1 268 ? 33.858 -4.232 -10.045 1.00 89.44 ? 268 GLU A O 1 ATOM 2143 C CB . GLU A 1 268 ? 36.844 -4.520 -10.296 1.00 85.67 ? 268 GLU A CB 1 ATOM 2144 C CG . GLU A 1 268 ? 38.253 -4.908 -9.877 1.00 86.21 ? 268 GLU A CG 1 ATOM 2145 C CD . GLU A 1 268 ? 38.316 -5.484 -8.473 1.00 88.06 ? 268 GLU A CD 1 ATOM 2146 O OE1 . GLU A 1 268 ? 37.945 -4.769 -7.510 1.00 87.75 ? 268 GLU A OE1 1 ATOM 2147 O OE2 . GLU A 1 268 ? 38.737 -6.657 -8.338 1.00 88.46 ? 268 GLU A OE2 1 ATOM 2148 N N . LEU A 1 269 ? 33.949 -5.753 -11.690 1.00 84.68 ? 269 LEU A N 1 ATOM 2149 C CA . LEU A 1 269 ? 32.699 -5.327 -12.309 1.00 87.11 ? 269 LEU A CA 1 ATOM 2150 C C . LEU A 1 269 ? 31.500 -5.670 -11.455 1.00 88.34 ? 269 LEU A C 1 ATOM 2151 O O . LEU A 1 269 ? 31.568 -6.538 -10.589 1.00 85.54 ? 269 LEU A O 1 ATOM 2152 C CB . LEU A 1 269 ? 32.523 -5.969 -13.686 1.00 87.09 ? 269 LEU A CB 1 ATOM 2153 C CG . LEU A 1 269 ? 33.494 -5.496 -14.765 1.00 88.41 ? 269 LEU A CG 1 ATOM 2154 C CD1 . LEU A 1 269 ? 33.437 -6.427 -15.967 1.00 88.73 ? 269 LEU A CD1 1 ATOM 2155 C CD2 . LEU A 1 269 ? 33.194 -4.059 -15.171 1.00 91.05 ? 269 LEU A CD2 1 ATOM 2156 N N . GLU A 1 270 ? 30.402 -4.979 -11.741 1.00 92.64 ? 270 GLU A N 1 ATOM 2157 C CA . GLU A 1 270 ? 29.138 -5.131 -11.035 1.00 96.39 ? 270 GLU A CA 1 ATOM 2158 C C . GLU A 1 270 ? 28.075 -5.660 -12.007 1.00 94.04 ? 270 GLU A C 1 ATOM 2159 O O . GLU A 1 270 ? 28.329 -5.779 -13.208 1.00 94.43 ? 270 GLU A O 1 ATOM 2160 C CB . GLU A 1 270 ? 28.720 -3.785 -10.414 1.00 103.67 ? 270 GLU A CB 1 ATOM 2161 C CG . GLU A 1 270 ? 28.586 -2.634 -11.413 1.00 109.32 ? 270 GLU A CG 1 ATOM 2162 C CD . GLU A 1 270 ? 28.484 -1.259 -10.766 1.00 114.69 ? 270 GLU A CD 1 ATOM 2163 O OE1 . GLU A 1 270 ? 28.360 -1.165 -9.522 1.00 118.53 ? 270 GLU A OE1 1 ATOM 2164 O OE2 . GLU A 1 270 ? 28.528 -0.260 -11.518 1.00 116.49 ? 270 GLU A OE2 1 ATOM 2165 N N . TYR A 1 271 ? 26.894 -5.973 -11.482 1.00 93.52 ? 271 TYR A N 1 ATOM 2166 C CA . TYR A 1 271 ? 25.818 -6.596 -12.261 1.00 92.44 ? 271 TYR A CA 1 ATOM 2167 C C . TYR A 1 271 ? 25.399 -5.761 -13.470 1.00 93.71 ? 271 TYR A C 1 ATOM 2168 O O . TYR A 1 271 ? 25.074 -4.582 -13.344 1.00 92.98 ? 271 TYR A O 1 ATOM 2169 C CB . TYR A 1 271 ? 24.600 -6.843 -11.369 1.00 95.03 ? 271 TYR A CB 1 ATOM 2170 C CG . TYR A 1 271 ? 23.507 -7.670 -12.009 1.00 96.57 ? 271 TYR A CG 1 ATOM 2171 C CD1 . TYR A 1 271 ? 23.783 -8.910 -12.576 1.00 94.11 ? 271 TYR A CD1 1 ATOM 2172 C CD2 . TYR A 1 271 ? 22.189 -7.222 -12.025 1.00 100.21 ? 271 TYR A CD2 1 ATOM 2173 C CE1 . TYR A 1 271 ? 22.783 -9.673 -13.154 1.00 95.23 ? 271 TYR A CE1 1 ATOM 2174 C CE2 . TYR A 1 271 ? 21.182 -7.982 -12.593 1.00 101.97 ? 271 TYR A CE2 1 ATOM 2175 C CZ . TYR A 1 271 ? 21.484 -9.206 -13.158 1.00 99.65 ? 271 TYR A CZ 1 ATOM 2176 O OH . TYR A 1 271 ? 20.484 -9.959 -13.728 1.00 101.46 ? 271 TYR A OH 1 ATOM 2177 N N . GLY A 1 272 ? 25.411 -6.391 -14.642 1.00 94.23 ? 272 GLY A N 1 ATOM 2178 C CA . GLY A 1 272 ? 25.071 -5.719 -15.890 1.00 96.38 ? 272 GLY A CA 1 ATOM 2179 C C . GLY A 1 272 ? 23.581 -5.651 -16.162 1.00 100.86 ? 272 GLY A C 1 ATOM 2180 O O . GLY A 1 272 ? 23.139 -4.871 -17.011 1.00 101.30 ? 272 GLY A O 1 ATOM 2181 N N . ASN A 1 273 ? 22.809 -6.471 -15.449 1.00 103.35 ? 273 ASN A N 1 ATOM 2182 C CA . ASN A 1 273 ? 21.360 -6.553 -15.639 1.00 108.04 ? 273 ASN A CA 1 ATOM 2183 C C . ASN A 1 273 ? 21.058 -6.999 -17.066 1.00 107.43 ? 273 ASN A C 1 ATOM 2184 O O . ASN A 1 273 ? 20.626 -6.220 -17.916 1.00 108.27 ? 273 ASN A O 1 ATOM 2185 C CB . ASN A 1 273 ? 20.692 -5.223 -15.279 1.00 111.48 ? 273 ASN A CB 1 ATOM 2186 C CG . ASN A 1 273 ? 19.332 -5.422 -14.649 1.00 116.28 ? 273 ASN A CG 1 ATOM 2187 O OD1 . ASN A 1 273 ? 18.473 -6.101 -15.214 1.00 118.32 ? 273 ASN A OD1 1 ATOM 2188 N ND2 . ASN A 1 273 ? 19.135 -4.852 -13.462 1.00 118.16 ? 273 ASN A ND2 1 ATOM 2189 N N . CYS A 1 274 ? 21.283 -8.285 -17.300 1.00 105.47 ? 274 CYS A N 1 ATOM 2190 C CA . CYS A 1 274 ? 21.651 -8.760 -18.620 1.00 103.95 ? 274 CYS A CA 1 ATOM 2191 C C . CYS A 1 274 ? 21.660 -10.292 -18.665 1.00 98.54 ? 274 CYS A C 1 ATOM 2192 O O . CYS A 1 274 ? 21.773 -10.934 -17.623 1.00 98.13 ? 274 CYS A O 1 ATOM 2193 C CB . CYS A 1 274 ? 23.048 -8.202 -18.915 1.00 104.73 ? 274 CYS A CB 1 ATOM 2194 S SG . CYS A 1 274 ? 24.014 -9.132 -20.108 1.00 111.48 ? 274 CYS A SG 1 ATOM 2195 N N . ASN A 1 275 ? 21.552 -10.873 -19.860 1.00 95.00 ? 275 ASN A N 1 ATOM 2196 C CA . ASN A 1 275 ? 21.599 -12.337 -20.022 1.00 93.49 ? 275 ASN A CA 1 ATOM 2197 C C . ASN A 1 275 ? 22.585 -12.796 -21.106 1.00 91.20 ? 275 ASN A C 1 ATOM 2198 O O . ASN A 1 275 ? 22.787 -12.107 -22.104 1.00 92.46 ? 275 ASN A O 1 ATOM 2199 C CB . ASN A 1 275 ? 20.202 -12.877 -20.336 1.00 96.43 ? 275 ASN A CB 1 ATOM 2200 C CG . ASN A 1 275 ? 20.126 -14.392 -20.256 1.00 95.54 ? 275 ASN A CG 1 ATOM 2201 O OD1 . ASN A 1 275 ? 20.329 -14.980 -19.202 1.00 94.75 ? 275 ASN A OD1 1 ATOM 2202 N ND2 . ASN A 1 275 ? 19.831 -15.026 -21.375 1.00 97.53 ? 275 ASN A ND2 1 ATOM 2203 N N . THR A 1 276 ? 23.189 -13.967 -20.907 1.00 89.45 ? 276 THR A N 1 ATOM 2204 C CA . THR A 1 276 ? 24.157 -14.516 -21.861 1.00 86.02 ? 276 THR A CA 1 ATOM 2205 C C . THR A 1 276 ? 24.253 -16.030 -21.739 1.00 86.39 ? 276 THR A C 1 ATOM 2206 O O . THR A 1 276 ? 23.737 -16.610 -20.791 1.00 89.49 ? 276 THR A O 1 ATOM 2207 C CB . THR A 1 276 ? 25.561 -13.914 -21.641 1.00 83.76 ? 276 THR A CB 1 ATOM 2208 O OG1 . THR A 1 276 ? 26.456 -14.373 -22.660 1.00 83.73 ? 276 THR A OG1 1 ATOM 2209 C CG2 . THR A 1 276 ? 26.130 -14.303 -20.269 1.00 83.95 ? 276 THR A CG2 1 ATOM 2210 N N . LYS A 1 277 ? 24.918 -16.660 -22.703 1.00 86.31 ? 277 LYS A N 1 ATOM 2211 C CA . LYS A 1 277 ? 25.169 -18.104 -22.677 1.00 88.92 ? 277 LYS A CA 1 ATOM 2212 C C . LYS A 1 277 ? 26.653 -18.419 -22.471 1.00 84.02 ? 277 LYS A C 1 ATOM 2213 O O . LYS A 1 277 ? 27.043 -19.583 -22.416 1.00 82.37 ? 277 LYS A O 1 ATOM 2214 C CB . LYS A 1 277 ? 24.676 -18.751 -23.979 1.00 94.62 ? 277 LYS A CB 1 ATOM 2215 C CG . LYS A 1 277 ? 23.231 -18.408 -24.345 1.00 101.68 ? 277 LYS A CG 1 ATOM 2216 C CD . LYS A 1 277 ? 22.214 -19.081 -23.423 1.00 107.96 ? 277 LYS A CD 1 ATOM 2217 C CE . LYS A 1 277 ? 21.350 -20.095 -24.167 1.00 113.67 ? 277 LYS A CE 1 ATOM 2218 N NZ . LYS A 1 277 ? 22.140 -21.163 -24.845 1.00 114.10 ? 277 LYS A NZ 1 ATOM 2219 N N . CYS A 1 278 ? 27.473 -17.379 -22.365 1.00 80.91 ? 278 CYS A N 1 ATOM 2220 C CA . CYS A 1 278 ? 28.903 -17.531 -22.160 1.00 79.68 ? 278 CYS A CA 1 ATOM 2221 C C . CYS A 1 278 ? 29.438 -16.267 -21.497 1.00 76.47 ? 278 CYS A C 1 ATOM 2222 O O . CYS A 1 278 ? 29.275 -15.167 -22.034 1.00 75.31 ? 278 CYS A O 1 ATOM 2223 C CB . CYS A 1 278 ? 29.602 -17.772 -23.499 1.00 81.03 ? 278 CYS A CB 1 ATOM 2224 S SG . CYS A 1 278 ? 31.414 -17.662 -23.454 1.00 82.90 ? 278 CYS A SG 1 ATOM 2225 N N . GLN A 1 279 ? 30.070 -16.420 -20.335 1.00 74.25 ? 279 GLN A N 1 ATOM 2226 C CA . GLN A 1 279 ? 30.490 -15.271 -19.535 1.00 73.12 ? 279 GLN A CA 1 ATOM 2227 C C . GLN A 1 279 ? 31.982 -15.294 -19.252 1.00 70.82 ? 279 GLN A C 1 ATOM 2228 O O . GLN A 1 279 ? 32.546 -16.351 -18.981 1.00 69.97 ? 279 GLN A O 1 ATOM 2229 C CB . GLN A 1 279 ? 29.723 -15.242 -18.210 1.00 74.53 ? 279 GLN A CB 1 ATOM 2230 C CG . GLN A 1 279 ? 30.015 -14.031 -17.331 1.00 74.29 ? 279 GLN A CG 1 ATOM 2231 C CD . GLN A 1 279 ? 29.341 -12.762 -17.820 1.00 75.70 ? 279 GLN A CD 1 ATOM 2232 O OE1 . GLN A 1 279 ? 28.116 -12.701 -17.933 1.00 77.43 ? 279 GLN A OE1 1 ATOM 2233 N NE2 . GLN A 1 279 ? 30.136 -11.732 -18.094 1.00 74.85 ? 279 GLN A NE2 1 ATOM 2234 N N . THR A 1 280 ? 32.602 -14.115 -19.307 1.00 69.71 ? 280 THR A N 1 ATOM 2235 C CA . THR A 1 280 ? 33.987 -13.931 -18.881 1.00 69.54 ? 280 THR A CA 1 ATOM 2236 C C . THR A 1 280 ? 34.080 -12.857 -17.793 1.00 70.81 ? 280 THR A C 1 ATOM 2237 O O . THR A 1 280 ? 33.156 -12.054 -17.634 1.00 72.16 ? 280 THR A O 1 ATOM 2238 C CB . THR A 1 280 ? 34.892 -13.501 -20.052 1.00 68.40 ? 280 THR A CB 1 ATOM 2239 O OG1 . THR A 1 280 ? 34.849 -12.073 -20.212 1.00 66.47 ? 280 THR A OG1 1 ATOM 2240 C CG2 . THR A 1 280 ? 34.465 -14.194 -21.343 1.00 67.82 ? 280 THR A CG2 1 ATOM 2241 N N . PRO A 1 281 ? 35.210 -12.822 -17.056 1.00 71.29 ? 281 PRO A N 1 ATOM 2242 C CA . PRO A 1 281 ? 35.456 -11.783 -16.046 1.00 71.69 ? 281 PRO A CA 1 ATOM 2243 C C . PRO A 1 281 ? 35.455 -10.351 -16.576 1.00 72.58 ? 281 PRO A C 1 ATOM 2244 O O . PRO A 1 281 ? 35.384 -9.416 -15.779 1.00 72.49 ? 281 PRO A O 1 ATOM 2245 C CB . PRO A 1 281 ? 36.851 -12.125 -15.520 1.00 71.03 ? 281 PRO A CB 1 ATOM 2246 C CG . PRO A 1 281 ? 37.022 -13.574 -15.779 1.00 70.98 ? 281 PRO A CG 1 ATOM 2247 C CD . PRO A 1 281 ? 36.221 -13.895 -16.998 1.00 70.19 ? 281 PRO A CD 1 ATOM 2248 N N . MET A 1 282 ? 35.553 -10.183 -17.895 1.00 74.23 ? 282 MET A N 1 ATOM 2249 C CA . MET A 1 282 ? 35.562 -8.857 -18.514 1.00 76.86 ? 282 MET A CA 1 ATOM 2250 C C . MET A 1 282 ? 34.253 -8.504 -19.200 1.00 74.95 ? 282 MET A C 1 ATOM 2251 O O . MET A 1 282 ? 34.045 -7.349 -19.566 1.00 75.25 ? 282 MET A O 1 ATOM 2252 C CB . MET A 1 282 ? 36.683 -8.771 -19.542 1.00 81.42 ? 282 MET A CB 1 ATOM 2253 C CG . MET A 1 282 ? 38.024 -9.255 -19.020 1.00 86.90 ? 282 MET A CG 1 ATOM 2254 S SD . MET A 1 282 ? 39.416 -8.450 -19.830 1.00 99.23 ? 282 MET A SD 1 ATOM 2255 C CE . MET A 1 282 ? 38.902 -8.487 -21.549 1.00 94.29 ? 282 MET A CE 1 ATOM 2256 N N . GLY A 1 283 ? 33.379 -9.491 -19.379 1.00 73.02 ? 283 GLY A N 1 ATOM 2257 C CA . GLY A 1 283 ? 32.139 -9.292 -20.119 1.00 74.10 ? 283 GLY A CA 1 ATOM 2258 C C . GLY A 1 283 ? 31.613 -10.579 -20.725 1.00 74.24 ? 283 GLY A C 1 ATOM 2259 O O . GLY A 1 283 ? 32.288 -11.613 -20.688 1.00 72.49 ? 283 GLY A O 1 ATOM 2260 N N . ALA A 1 284 ? 30.408 -10.511 -21.286 1.00 76.12 ? 284 ALA A N 1 ATOM 2261 C CA . ALA A 1 284 ? 29.732 -11.684 -21.848 1.00 77.19 ? 284 ALA A CA 1 ATOM 2262 C C . ALA A 1 284 ? 29.978 -11.813 -23.351 1.00 78.28 ? 284 ALA A C 1 ATOM 2263 O O . ALA A 1 284 ? 30.381 -10.850 -24.015 1.00 76.17 ? 284 ALA A O 1 ATOM 2264 C CB . ALA A 1 284 ? 28.243 -11.613 -21.569 1.00 79.56 ? 284 ALA A CB 1 ATOM 2265 N N . ILE A 1 285 ? 29.719 -13.009 -23.876 1.00 79.72 ? 285 ILE A N 1 ATOM 2266 C CA . ILE A 1 285 ? 29.988 -13.329 -25.279 1.00 81.10 ? 285 ILE A CA 1 ATOM 2267 C C . ILE A 1 285 ? 28.749 -13.907 -25.953 1.00 85.05 ? 285 ILE A C 1 ATOM 2268 O O . ILE A 1 285 ? 28.104 -14.818 -25.433 1.00 86.51 ? 285 ILE A O 1 ATOM 2269 C CB . ILE A 1 285 ? 31.161 -14.328 -25.420 1.00 78.45 ? 285 ILE A CB 1 ATOM 2270 C CG1 . ILE A 1 285 ? 32.491 -13.620 -25.178 1.00 77.07 ? 285 ILE A CG1 1 ATOM 2271 C CG2 . ILE A 1 285 ? 31.193 -14.954 -26.805 1.00 78.58 ? 285 ILE A CG2 1 ATOM 2272 C CD1 . ILE A 1 285 ? 33.661 -14.565 -24.995 1.00 75.92 ? 285 ILE A CD1 1 ATOM 2273 N N . ASN A 1 286 ? 28.439 -13.363 -27.123 1.00 88.47 ? 286 ASN A N 1 ATOM 2274 C CA . ASN A 1 286 ? 27.369 -13.864 -27.962 1.00 94.71 ? 286 ASN A CA 1 ATOM 2275 C C . ASN A 1 286 ? 27.868 -13.913 -29.403 1.00 89.58 ? 286 ASN A C 1 ATOM 2276 O O . ASN A 1 286 ? 27.820 -12.919 -30.120 1.00 87.03 ? 286 ASN A O 1 ATOM 2277 C CB . ASN A 1 286 ? 26.140 -12.962 -27.831 1.00 103.10 ? 286 ASN A CB 1 ATOM 2278 C CG . ASN A 1 286 ? 25.079 -13.275 -28.861 1.00 116.19 ? 286 ASN A CG 1 ATOM 2279 O OD1 . ASN A 1 286 ? 24.655 -14.423 -28.993 1.00 116.24 ? 286 ASN A OD1 1 ATOM 2280 N ND2 . ASN A 1 286 ? 24.647 -12.248 -29.602 1.00 132.69 ? 286 ASN A ND2 1 ATOM 2281 N N . SER A 1 287 ? 28.388 -15.066 -29.809 1.00 86.89 ? 287 SER A N 1 ATOM 2282 C CA . SER A 1 287 ? 28.824 -15.254 -31.188 1.00 86.72 ? 287 SER A CA 1 ATOM 2283 C C . SER A 1 287 ? 28.895 -16.727 -31.557 1.00 85.06 ? 287 SER A C 1 ATOM 2284 O O . SER A 1 287 ? 28.966 -17.590 -30.692 1.00 84.05 ? 287 SER A O 1 ATOM 2285 C CB . SER A 1 287 ? 30.184 -14.580 -31.431 1.00 86.10 ? 287 SER A CB 1 ATOM 2286 O OG . SER A 1 287 ? 31.265 -15.412 -31.062 1.00 83.35 ? 287 SER A OG 1 ATOM 2287 N N . SER A 1 288 ? 28.883 -16.993 -32.859 1.00 85.72 ? 288 SER A N 1 ATOM 2288 C CA . SER A 1 288 ? 28.956 -18.354 -33.386 1.00 86.60 ? 288 SER A CA 1 ATOM 2289 C C . SER A 1 288 ? 30.370 -18.733 -33.850 1.00 81.18 ? 288 SER A C 1 ATOM 2290 O O . SER A 1 288 ? 30.566 -19.795 -34.442 1.00 81.27 ? 288 SER A O 1 ATOM 2291 C CB . SER A 1 288 ? 27.950 -18.504 -34.534 1.00 91.36 ? 288 SER A CB 1 ATOM 2292 O OG . SER A 1 288 ? 27.898 -17.323 -35.324 1.00 92.81 ? 288 SER A OG 1 ATOM 2293 N N . MET A 1 289 ? 31.349 -17.877 -33.563 1.00 76.42 ? 289 MET A N 1 ATOM 2294 C CA . MET A 1 289 ? 32.735 -18.118 -33.957 1.00 74.88 ? 289 MET A CA 1 ATOM 2295 C C . MET A 1 289 ? 33.312 -19.276 -33.158 1.00 73.42 ? 289 MET A C 1 ATOM 2296 O O . MET A 1 289 ? 32.986 -19.431 -31.990 1.00 75.11 ? 289 MET A O 1 ATOM 2297 C CB . MET A 1 289 ? 33.610 -16.899 -33.664 1.00 78.30 ? 289 MET A CB 1 ATOM 2298 C CG . MET A 1 289 ? 33.189 -15.597 -34.313 1.00 80.76 ? 289 MET A CG 1 ATOM 2299 S SD . MET A 1 289 ? 33.493 -15.592 -36.078 1.00 82.51 ? 289 MET A SD 1 ATOM 2300 C CE . MET A 1 289 ? 33.912 -13.858 -36.270 1.00 81.28 ? 289 MET A CE 1 ATOM 2301 N N . PRO A 1 290 ? 34.194 -20.078 -33.773 1.00 70.87 ? 290 PRO A N 1 ATOM 2302 C CA . PRO A 1 290 ? 34.846 -21.159 -33.027 1.00 69.87 ? 290 PRO A CA 1 ATOM 2303 C C . PRO A 1 290 ? 35.907 -20.713 -32.020 1.00 67.38 ? 290 PRO A C 1 ATOM 2304 O O . PRO A 1 290 ? 36.284 -21.502 -31.167 1.00 69.22 ? 290 PRO A O 1 ATOM 2305 C CB . PRO A 1 290 ? 35.504 -21.989 -34.131 1.00 69.57 ? 290 PRO A CB 1 ATOM 2306 C CG . PRO A 1 290 ? 35.730 -21.016 -35.231 1.00 68.74 ? 290 PRO A CG 1 ATOM 2307 C CD . PRO A 1 290 ? 34.525 -20.133 -35.206 1.00 68.33 ? 290 PRO A CD 1 ATOM 2308 N N . PHE A 1 291 ? 36.388 -19.478 -32.121 1.00 65.39 ? 291 PHE A N 1 ATOM 2309 C CA . PHE A 1 291 ? 37.441 -18.985 -31.233 1.00 64.90 ? 291 PHE A CA 1 ATOM 2310 C C . PHE A 1 291 ? 37.116 -17.607 -30.692 1.00 62.45 ? 291 PHE A C 1 ATOM 2311 O O . PHE A 1 291 ? 36.345 -16.869 -31.294 1.00 62.54 ? 291 PHE A O 1 ATOM 2312 C CB . PHE A 1 291 ? 38.761 -18.848 -31.988 1.00 66.39 ? 291 PHE A CB 1 ATOM 2313 C CG . PHE A 1 291 ? 39.346 -20.139 -32.455 1.00 68.07 ? 291 PHE A CG 1 ATOM 2314 C CD1 . PHE A 1 291 ? 40.106 -20.918 -31.595 1.00 71.74 ? 291 PHE A CD1 1 ATOM 2315 C CD2 . PHE A 1 291 ? 39.179 -20.558 -33.766 1.00 70.15 ? 291 PHE A CD2 1 ATOM 2316 C CE1 . PHE A 1 291 ? 40.666 -22.109 -32.027 1.00 73.79 ? 291 PHE A CE1 1 ATOM 2317 C CE2 . PHE A 1 291 ? 39.737 -21.748 -34.209 1.00 72.19 ? 291 PHE A CE2 1 ATOM 2318 C CZ . PHE A 1 291 ? 40.483 -22.521 -33.339 1.00 73.61 ? 291 PHE A CZ 1 ATOM 2319 N N . HIS A 1 292 ? 37.739 -17.251 -29.574 1.00 61.63 ? 292 HIS A N 1 ATOM 2320 C CA . HIS A 1 292 ? 37.725 -15.868 -29.089 1.00 61.16 ? 292 HIS A CA 1 ATOM 2321 C C . HIS A 1 292 ? 39.045 -15.536 -28.416 1.00 59.89 ? 292 HIS A C 1 ATOM 2322 O O . HIS A 1 292 ? 39.849 -16.433 -28.168 1.00 60.88 ? 292 HIS A O 1 ATOM 2323 C CB . HIS A 1 292 ? 36.553 -15.625 -28.129 1.00 63.25 ? 292 HIS A CB 1 ATOM 2324 C CG . HIS A 1 292 ? 36.666 -16.344 -26.818 1.00 63.74 ? 292 HIS A CG 1 ATOM 2325 N ND1 . HIS A 1 292 ? 37.333 -15.820 -25.733 1.00 63.64 ? 292 HIS A ND1 1 ATOM 2326 C CD2 . HIS A 1 292 ? 36.169 -17.535 -26.409 1.00 64.72 ? 292 HIS A CD2 1 ATOM 2327 C CE1 . HIS A 1 292 ? 37.259 -16.663 -24.721 1.00 64.95 ? 292 HIS A CE1 1 ATOM 2328 N NE2 . HIS A 1 292 ? 36.557 -17.713 -25.105 1.00 65.70 ? 292 HIS A NE2 1 ATOM 2329 N N . ASN A 1 293 ? 39.268 -14.256 -28.128 1.00 59.11 ? 293 ASN A N 1 ATOM 2330 C CA . ASN A 1 293 ? 40.501 -13.814 -27.451 1.00 59.75 ? 293 ASN A CA 1 ATOM 2331 C C . ASN A 1 293 ? 40.246 -12.855 -26.279 1.00 61.19 ? 293 ASN A C 1 ATOM 2332 O O . ASN A 1 293 ? 41.118 -12.062 -25.908 1.00 61.59 ? 293 ASN A O 1 ATOM 2333 C CB . ASN A 1 293 ? 41.442 -13.160 -28.461 1.00 59.83 ? 293 ASN A CB 1 ATOM 2334 C CG . ASN A 1 293 ? 40.923 -11.835 -28.981 1.00 59.99 ? 293 ASN A CG 1 ATOM 2335 O OD1 . ASN A 1 293 ? 39.801 -11.434 -28.692 1.00 61.10 ? 293 ASN A OD1 1 ATOM 2336 N ND2 . ASN A 1 293 ? 41.743 -11.149 -29.759 1.00 61.44 ? 293 ASN A ND2 1 ATOM 2337 N N . ILE A 1 294 ? 39.051 -12.942 -25.706 1.00 60.77 ? 294 ILE A N 1 ATOM 2338 C CA . ILE A 1 294 ? 38.621 -12.058 -24.626 1.00 63.54 ? 294 ILE A CA 1 ATOM 2339 C C . ILE A 1 294 ? 39.370 -12.347 -23.325 1.00 64.19 ? 294 ILE A C 1 ATOM 2340 O O . ILE A 1 294 ? 40.046 -11.474 -22.786 1.00 64.42 ? 294 ILE A O 1 ATOM 2341 C CB . ILE A 1 294 ? 37.094 -12.194 -24.363 1.00 63.84 ? 294 ILE A CB 1 ATOM 2342 C CG1 . ILE A 1 294 ? 36.274 -11.955 -25.643 1.00 63.09 ? 294 ILE A CG1 1 ATOM 2343 C CG2 . ILE A 1 294 ? 36.654 -11.241 -23.265 1.00 66.42 ? 294 ILE A CG2 1 ATOM 2344 C CD1 . ILE A 1 294 ? 36.661 -10.713 -26.415 1.00 63.67 ? 294 ILE A CD1 1 ATOM 2345 N N . HIS A 1 295 ? 39.243 -13.579 -22.838 1.00 65.32 ? 295 HIS A N 1 ATOM 2346 C CA . HIS A 1 295 ? 39.782 -13.977 -21.544 1.00 66.90 ? 295 HIS A CA 1 ATOM 2347 C C . HIS A 1 295 ? 39.744 -15.517 -21.401 1.00 65.68 ? 295 HIS A C 1 ATOM 2348 O O . HIS A 1 295 ? 38.776 -16.142 -21.821 1.00 63.13 ? 295 HIS A O 1 ATOM 2349 C CB . HIS A 1 295 ? 38.946 -13.318 -20.445 1.00 70.08 ? 295 HIS A CB 1 ATOM 2350 C CG . HIS A 1 295 ? 39.586 -13.343 -19.097 1.00 72.97 ? 295 HIS A CG 1 ATOM 2351 N ND1 . HIS A 1 295 ? 39.603 -14.468 -18.307 1.00 74.82 ? 295 HIS A ND1 1 ATOM 2352 C CD2 . HIS A 1 295 ? 40.222 -12.380 -18.391 1.00 75.43 ? 295 HIS A CD2 1 ATOM 2353 C CE1 . HIS A 1 295 ? 40.230 -14.204 -17.176 1.00 75.64 ? 295 HIS A CE1 1 ATOM 2354 N NE2 . HIS A 1 295 ? 40.614 -12.943 -17.201 1.00 75.78 ? 295 HIS A NE2 1 ATOM 2355 N N . PRO A 1 296 ? 40.791 -16.129 -20.807 1.00 66.36 ? 296 PRO A N 1 ATOM 2356 C CA . PRO A 1 296 ? 40.836 -17.600 -20.709 1.00 67.25 ? 296 PRO A CA 1 ATOM 2357 C C . PRO A 1 296 ? 39.784 -18.247 -19.795 1.00 67.95 ? 296 PRO A C 1 ATOM 2358 O O . PRO A 1 296 ? 39.271 -19.314 -20.112 1.00 68.05 ? 296 PRO A O 1 ATOM 2359 C CB . PRO A 1 296 ? 42.252 -17.884 -20.175 1.00 67.70 ? 296 PRO A CB 1 ATOM 2360 C CG . PRO A 1 296 ? 42.693 -16.614 -19.542 1.00 68.90 ? 296 PRO A CG 1 ATOM 2361 C CD . PRO A 1 296 ? 42.040 -15.512 -20.323 1.00 67.43 ? 296 PRO A CD 1 ATOM 2362 N N . LEU A 1 297 ? 39.489 -17.624 -18.664 1.00 69.34 ? 297 LEU A N 1 ATOM 2363 C CA . LEU A 1 297 ? 38.520 -18.175 -17.712 1.00 72.31 ? 297 LEU A CA 1 ATOM 2364 C C . LEU A 1 297 ? 37.084 -17.840 -18.115 1.00 72.81 ? 297 LEU A C 1 ATOM 2365 O O . LEU A 1 297 ? 36.628 -16.722 -17.919 1.00 75.17 ? 297 LEU A O 1 ATOM 2366 C CB . LEU A 1 297 ? 38.815 -17.653 -16.298 1.00 73.79 ? 297 LEU A CB 1 ATOM 2367 C CG . LEU A 1 297 ? 40.264 -17.832 -15.813 1.00 76.05 ? 297 LEU A CG 1 ATOM 2368 C CD1 . LEU A 1 297 ? 40.531 -17.063 -14.525 1.00 76.69 ? 297 LEU A CD1 1 ATOM 2369 C CD2 . LEU A 1 297 ? 40.590 -19.309 -15.635 1.00 78.32 ? 297 LEU A CD2 1 ATOM 2370 N N . THR A 1 298 ? 36.371 -18.804 -18.688 1.00 73.54 ? 298 THR A N 1 ATOM 2371 C CA . THR A 1 298 ? 34.971 -18.592 -19.058 1.00 72.19 ? 298 THR A CA 1 ATOM 2372 C C . THR A 1 298 ? 34.075 -19.648 -18.426 1.00 73.72 ? 298 THR A C 1 ATOM 2373 O O . THR A 1 298 ? 34.555 -20.643 -17.891 1.00 73.88 ? 298 THR A O 1 ATOM 2374 C CB . THR A 1 298 ? 34.771 -18.602 -20.587 1.00 70.96 ? 298 THR A CB 1 ATOM 2375 O OG1 . THR A 1 298 ? 34.800 -19.946 -21.083 1.00 71.67 ? 298 THR A OG1 1 ATOM 2376 C CG2 . THR A 1 298 ? 35.854 -17.803 -21.271 1.00 71.03 ? 298 THR A CG2 1 ATOM 2377 N N . ILE A 1 299 ? 32.771 -19.416 -18.498 1.00 74.39 ? 299 ILE A N 1 ATOM 2378 C CA . ILE A 1 299 ? 31.779 -20.344 -17.976 1.00 78.15 ? 299 ILE A CA 1 ATOM 2379 C C . ILE A 1 299 ? 30.628 -20.346 -18.970 1.00 79.05 ? 299 ILE A C 1 ATOM 2380 O O . ILE A 1 299 ? 30.253 -19.289 -19.479 1.00 77.10 ? 299 ILE A O 1 ATOM 2381 C CB . ILE A 1 299 ? 31.320 -19.939 -16.546 1.00 81.93 ? 299 ILE A CB 1 ATOM 2382 C CG1 . ILE A 1 299 ? 30.155 -20.805 -16.038 1.00 85.84 ? 299 ILE A CG1 1 ATOM 2383 C CG2 . ILE A 1 299 ? 30.919 -18.470 -16.485 1.00 81.87 ? 299 ILE A CG2 1 ATOM 2384 C CD1 . ILE A 1 299 ? 30.533 -22.230 -15.688 1.00 88.99 ? 299 ILE A CD1 1 ATOM 2385 N N . GLY A 1 300 ? 30.096 -21.533 -19.262 1.00 82.20 ? 300 GLY A N 1 ATOM 2386 C CA . GLY A 1 300 ? 29.008 -21.688 -20.227 1.00 86.10 ? 300 GLY A CA 1 ATOM 2387 C C . GLY A 1 300 ? 29.455 -22.323 -21.534 1.00 88.59 ? 300 GLY A C 1 ATOM 2388 O O . GLY A 1 300 ? 30.537 -22.905 -21.613 1.00 89.73 ? 300 GLY A O 1 ATOM 2389 N N . GLU A 1 301 ? 28.614 -22.211 -22.562 1.00 91.92 ? 301 GLU A N 1 ATOM 2390 C CA . GLU A 1 301 ? 28.925 -22.760 -23.882 1.00 93.25 ? 301 GLU A CA 1 ATOM 2391 C C . GLU A 1 301 ? 29.678 -21.691 -24.657 1.00 88.00 ? 301 GLU A C 1 ATOM 2392 O O . GLU A 1 301 ? 29.070 -20.780 -25.213 1.00 86.44 ? 301 GLU A O 1 ATOM 2393 C CB . GLU A 1 301 ? 27.649 -23.184 -24.626 1.00 99.52 ? 301 GLU A CB 1 ATOM 2394 C CG . GLU A 1 301 ? 27.746 -24.556 -25.281 1.00 105.08 ? 301 GLU A CG 1 ATOM 2395 C CD . GLU A 1 301 ? 27.756 -25.685 -24.257 1.00 112.12 ? 301 GLU A CD 1 ATOM 2396 O OE1 . GLU A 1 301 ? 26.701 -25.946 -23.632 1.00 115.98 ? 301 GLU A OE1 1 ATOM 2397 O OE2 . GLU A 1 301 ? 28.827 -26.302 -24.061 1.00 115.10 ? 301 GLU A OE2 1 ATOM 2398 N N . CYS A 1 302 ? 31.004 -21.808 -24.676 1.00 84.75 ? 302 CYS A N 1 ATOM 2399 C CA . CYS A 1 302 ? 31.870 -20.764 -25.211 1.00 81.56 ? 302 CYS A CA 1 ATOM 2400 C C . CYS A 1 302 ? 32.695 -21.225 -26.406 1.00 77.77 ? 302 CYS A C 1 ATOM 2401 O O . CYS A 1 302 ? 32.872 -22.422 -26.620 1.00 76.63 ? 302 CYS A O 1 ATOM 2402 C CB . CYS A 1 302 ? 32.829 -20.290 -24.119 1.00 83.72 ? 302 CYS A CB 1 ATOM 2403 S SG . CYS A 1 302 ? 32.027 -19.477 -22.717 1.00 88.83 ? 302 CYS A SG 1 ATOM 2404 N N . PRO A 1 303 ? 33.216 -20.266 -27.186 1.00 74.28 ? 303 PRO A N 1 ATOM 2405 C CA . PRO A 1 303 ? 34.259 -20.607 -28.144 1.00 73.60 ? 303 PRO A CA 1 ATOM 2406 C C . PRO A 1 303 ? 35.566 -20.890 -27.415 1.00 72.90 ? 303 PRO A C 1 ATOM 2407 O O . PRO A 1 303 ? 35.658 -20.648 -26.212 1.00 72.05 ? 303 PRO A O 1 ATOM 2408 C CB . PRO A 1 303 ? 34.386 -19.348 -29.014 1.00 71.84 ? 303 PRO A CB 1 ATOM 2409 C CG . PRO A 1 303 ? 33.255 -18.455 -28.632 1.00 71.66 ? 303 PRO A CG 1 ATOM 2410 C CD . PRO A 1 303 ? 32.855 -18.842 -27.249 1.00 73.15 ? 303 PRO A CD 1 ATOM 2411 N N . LYS A 1 304 ? 36.565 -21.393 -28.134 1.00 72.85 ? 304 LYS A N 1 ATOM 2412 C CA . LYS A 1 304 ? 37.855 -21.700 -27.524 1.00 73.47 ? 304 LYS A CA 1 ATOM 2413 C C . LYS A 1 304 ? 38.747 -20.475 -27.487 1.00 69.59 ? 304 LYS A C 1 ATOM 2414 O O . LYS A 1 304 ? 38.791 -19.689 -28.433 1.00 68.62 ? 304 LYS A O 1 ATOM 2415 C CB . LYS A 1 304 ? 38.546 -22.857 -28.246 1.00 77.92 ? 304 LYS A CB 1 ATOM 2416 C CG . LYS A 1 304 ? 37.877 -24.207 -28.003 1.00 85.44 ? 304 LYS A CG 1 ATOM 2417 C CD . LYS A 1 304 ? 37.878 -24.590 -26.519 1.00 91.66 ? 304 LYS A CD 1 ATOM 2418 C CE . LYS A 1 304 ? 37.271 -25.965 -26.258 1.00 97.37 ? 304 LYS A CE 1 ATOM 2419 N NZ . LYS A 1 304 ? 35.842 -26.047 -26.677 1.00 98.07 ? 304 LYS A NZ 1 ATOM 2420 N N . TYR A 1 305 ? 39.445 -20.307 -26.372 1.00 66.89 ? 305 TYR A N 1 ATOM 2421 C CA . TYR A 1 305 ? 40.240 -19.121 -26.171 1.00 65.13 ? 305 TYR A CA 1 ATOM 2422 C C . TYR A 1 305 ? 41.595 -19.310 -26.814 1.00 64.29 ? 305 TYR A C 1 ATOM 2423 O O . TYR A 1 305 ? 42.236 -20.336 -26.606 1.00 66.67 ? 305 TYR A O 1 ATOM 2424 C CB . TYR A 1 305 ? 40.417 -18.821 -24.680 1.00 65.54 ? 305 TYR A CB 1 ATOM 2425 C CG . TYR A 1 305 ? 41.368 -17.678 -24.430 1.00 64.01 ? 305 TYR A CG 1 ATOM 2426 C CD1 . TYR A 1 305 ? 40.959 -16.364 -24.600 1.00 63.29 ? 305 TYR A CD1 1 ATOM 2427 C CD2 . TYR A 1 305 ? 42.683 -17.910 -24.062 1.00 64.90 ? 305 TYR A CD2 1 ATOM 2428 C CE1 . TYR A 1 305 ? 41.828 -15.313 -24.390 1.00 63.85 ? 305 TYR A CE1 1 ATOM 2429 C CE2 . TYR A 1 305 ? 43.561 -16.862 -23.847 1.00 66.05 ? 305 TYR A CE2 1 ATOM 2430 C CZ . TYR A 1 305 ? 43.127 -15.565 -24.014 1.00 65.29 ? 305 TYR A CZ 1 ATOM 2431 O OH . TYR A 1 305 ? 43.990 -14.513 -23.809 1.00 66.64 ? 305 TYR A OH 1 ATOM 2432 N N . VAL A 1 306 ? 42.027 -18.313 -27.585 1.00 61.91 ? 306 VAL A N 1 ATOM 2433 C CA . VAL A 1 306 ? 43.405 -18.246 -28.079 1.00 61.06 ? 306 VAL A CA 1 ATOM 2434 C C . VAL A 1 306 ? 43.949 -16.841 -27.880 1.00 61.73 ? 306 VAL A C 1 ATOM 2435 O O . VAL A 1 306 ? 43.192 -15.884 -27.858 1.00 60.91 ? 306 VAL A O 1 ATOM 2436 C CB . VAL A 1 306 ? 43.514 -18.638 -29.571 1.00 60.10 ? 306 VAL A CB 1 ATOM 2437 C CG1 . VAL A 1 306 ? 43.108 -20.088 -29.775 1.00 60.80 ? 306 VAL A CG1 1 ATOM 2438 C CG2 . VAL A 1 306 ? 42.667 -17.734 -30.453 1.00 58.32 ? 306 VAL A CG2 1 ATOM 2439 N N . LYS A 1 307 ? 45.266 -16.722 -27.761 1.00 65.57 ? 307 LYS A N 1 ATOM 2440 C CA . LYS A 1 307 ? 45.931 -15.421 -27.638 1.00 68.84 ? 307 LYS A CA 1 ATOM 2441 C C . LYS A 1 307 ? 46.119 -14.651 -28.964 1.00 69.07 ? 307 LYS A C 1 ATOM 2442 O O . LYS A 1 307 ? 46.913 -13.715 -29.015 1.00 74.79 ? 307 LYS A O 1 ATOM 2443 C CB . LYS A 1 307 ? 47.316 -15.605 -27.010 1.00 71.16 ? 307 LYS A CB 1 ATOM 2444 C CG . LYS A 1 307 ? 47.334 -15.884 -25.529 1.00 73.16 ? 307 LYS A CG 1 ATOM 2445 C CD . LYS A 1 307 ? 48.775 -16.101 -25.105 1.00 78.61 ? 307 LYS A CD 1 ATOM 2446 C CE . LYS A 1 307 ? 48.920 -16.338 -23.615 1.00 82.61 ? 307 LYS A CE 1 ATOM 2447 N NZ . LYS A 1 307 ? 50.345 -16.626 -23.281 1.00 88.11 ? 307 LYS A NZ 1 ATOM 2448 N N . SER A 1 308 ? 45.420 -15.027 -30.029 1.00 67.08 ? 308 SER A N 1 ATOM 2449 C CA . SER A 1 308 ? 45.608 -14.384 -31.330 1.00 65.69 ? 308 SER A CA 1 ATOM 2450 C C . SER A 1 308 ? 44.926 -13.030 -31.386 1.00 66.55 ? 308 SER A C 1 ATOM 2451 O O . SER A 1 308 ? 43.899 -12.813 -30.741 1.00 66.65 ? 308 SER A O 1 ATOM 2452 C CB . SER A 1 308 ? 45.036 -15.251 -32.452 1.00 63.82 ? 308 SER A CB 1 ATOM 2453 O OG . SER A 1 308 ? 45.508 -16.580 -32.375 1.00 64.71 ? 308 SER A OG 1 ATOM 2454 N N . ASN A 1 309 ? 45.498 -12.129 -32.178 1.00 69.48 ? 309 ASN A N 1 ATOM 2455 C CA . ASN A 1 309 ? 44.833 -10.881 -32.543 1.00 71.79 ? 309 ASN A CA 1 ATOM 2456 C C . ASN A 1 309 ? 43.954 -11.046 -33.777 1.00 69.25 ? 309 ASN A C 1 ATOM 2457 O O . ASN A 1 309 ? 43.030 -10.263 -33.986 1.00 68.71 ? 309 ASN A O 1 ATOM 2458 C CB . ASN A 1 309 ? 45.868 -9.782 -32.795 1.00 76.27 ? 309 ASN A CB 1 ATOM 2459 C CG . ASN A 1 309 ? 46.463 -9.238 -31.506 1.00 81.20 ? 309 ASN A CG 1 ATOM 2460 O OD1 . ASN A 1 309 ? 45.775 -9.133 -30.484 1.00 80.58 ? 309 ASN A OD1 1 ATOM 2461 N ND2 . ASN A 1 309 ? 47.747 -8.883 -31.548 1.00 84.94 ? 309 ASN A ND2 1 ATOM 2462 N N . ARG A 1 310 ? 44.240 -12.076 -34.575 1.00 67.98 ? 310 ARG A N 1 ATOM 2463 C CA . ARG A 1 310 ? 43.626 -12.245 -35.891 1.00 66.76 ? 310 ARG A CA 1 ATOM 2464 C C . ARG A 1 310 ? 43.672 -13.703 -36.385 1.00 63.05 ? 310 ARG A C 1 ATOM 2465 O O . ARG A 1 310 ? 44.737 -14.307 -36.458 1.00 62.80 ? 310 ARG A O 1 ATOM 2466 C CB . ARG A 1 310 ? 44.360 -11.339 -36.886 1.00 70.49 ? 310 ARG A CB 1 ATOM 2467 C CG . ARG A 1 310 ? 43.672 -11.164 -38.227 1.00 72.74 ? 310 ARG A CG 1 ATOM 2468 C CD . ARG A 1 310 ? 44.474 -10.264 -39.149 1.00 75.54 ? 310 ARG A CD 1 ATOM 2469 N NE . ARG A 1 310 ? 44.165 -10.539 -40.553 1.00 78.82 ? 310 ARG A NE 1 ATOM 2470 C CZ . ARG A 1 310 ? 43.138 -10.023 -41.228 1.00 80.48 ? 310 ARG A CZ 1 ATOM 2471 N NH1 . ARG A 1 310 ? 42.286 -9.180 -40.651 1.00 82.86 ? 310 ARG A NH1 1 ATOM 2472 N NH2 . ARG A 1 310 ? 42.963 -10.350 -42.500 1.00 81.72 ? 310 ARG A NH2 1 ATOM 2473 N N . LEU A 1 311 ? 42.510 -14.263 -36.711 1.00 60.59 ? 311 LEU A N 1 ATOM 2474 C CA . LEU A 1 311 ? 42.427 -15.548 -37.427 1.00 60.25 ? 311 LEU A CA 1 ATOM 2475 C C . LEU A 1 311 ? 41.389 -15.438 -38.551 1.00 58.01 ? 311 LEU A C 1 ATOM 2476 O O . LEU A 1 311 ? 40.187 -15.381 -38.290 1.00 58.54 ? 311 LEU A O 1 ATOM 2477 C CB . LEU A 1 311 ? 42.048 -16.707 -36.494 1.00 59.54 ? 311 LEU A CB 1 ATOM 2478 C CG . LEU A 1 311 ? 42.988 -17.081 -35.347 1.00 60.42 ? 311 LEU A CG 1 ATOM 2479 C CD1 . LEU A 1 311 ? 42.352 -18.174 -34.509 1.00 60.64 ? 311 LEU A CD1 1 ATOM 2480 C CD2 . LEU A 1 311 ? 44.352 -17.538 -35.829 1.00 62.28 ? 311 LEU A CD2 1 ATOM 2481 N N . VAL A 1 312 ? 41.868 -15.403 -39.792 1.00 55.94 ? 312 VAL A N 1 ATOM 2482 C CA . VAL A 1 312 ? 41.007 -15.266 -40.961 1.00 54.95 ? 312 VAL A CA 1 ATOM 2483 C C . VAL A 1 312 ? 41.403 -16.301 -42.012 1.00 53.66 ? 312 VAL A C 1 ATOM 2484 O O . VAL A 1 312 ? 42.558 -16.341 -42.428 1.00 53.10 ? 312 VAL A O 1 ATOM 2485 C CB . VAL A 1 312 ? 41.127 -13.860 -41.574 1.00 55.37 ? 312 VAL A CB 1 ATOM 2486 C CG1 . VAL A 1 312 ? 40.211 -13.723 -42.782 1.00 55.79 ? 312 VAL A CG1 1 ATOM 2487 C CG2 . VAL A 1 312 ? 40.815 -12.801 -40.526 1.00 55.56 ? 312 VAL A CG2 1 ATOM 2488 N N . LEU A 1 313 ? 40.439 -17.135 -42.409 1.00 52.72 ? 313 LEU A N 1 ATOM 2489 C CA . LEU A 1 313 ? 40.631 -18.201 -43.400 1.00 51.92 ? 313 LEU A CA 1 ATOM 2490 C C . LEU A 1 313 ? 40.233 -17.732 -44.787 1.00 50.99 ? 313 LEU A C 1 ATOM 2491 O O . LEU A 1 313 ? 39.180 -17.117 -44.965 1.00 51.10 ? 313 LEU A O 1 ATOM 2492 C CB . LEU A 1 313 ? 39.753 -19.413 -43.082 1.00 52.12 ? 313 LEU A CB 1 ATOM 2493 C CG . LEU A 1 313 ? 40.169 -20.358 -41.961 1.00 54.45 ? 313 LEU A CG 1 ATOM 2494 C CD1 . LEU A 1 313 ? 39.013 -21.285 -41.616 1.00 54.89 ? 313 LEU A CD1 1 ATOM 2495 C CD2 . LEU A 1 313 ? 41.399 -21.170 -42.353 1.00 56.08 ? 313 LEU A CD2 1 ATOM 2496 N N . ALA A 1 314 ? 41.057 -18.052 -45.775 1.00 50.01 ? 314 ALA A N 1 ATOM 2497 C CA . ALA A 1 314 ? 40.677 -17.867 -47.168 1.00 49.36 ? 314 ALA A CA 1 ATOM 2498 C C . ALA A 1 314 ? 39.622 -18.907 -47.528 1.00 49.39 ? 314 ALA A C 1 ATOM 2499 O O . ALA A 1 314 ? 39.729 -20.079 -47.140 1.00 47.40 ? 314 ALA A O 1 ATOM 2500 C CB . ALA A 1 314 ? 41.888 -18.021 -48.074 1.00 49.87 ? 314 ALA A CB 1 ATOM 2501 N N . THR A 1 315 ? 38.596 -18.454 -48.240 1.00 49.48 ? 315 THR A N 1 ATOM 2502 C CA . THR A 1 315 ? 37.618 -19.329 -48.882 1.00 51.00 ? 315 THR A CA 1 ATOM 2503 C C . THR A 1 315 ? 37.665 -19.116 -50.397 1.00 51.00 ? 315 THR A C 1 ATOM 2504 O O . THR A 1 315 ? 37.776 -20.067 -51.171 1.00 52.28 ? 315 THR A O 1 ATOM 2505 C CB . THR A 1 315 ? 36.198 -19.042 -48.375 1.00 52.91 ? 315 THR A CB 1 ATOM 2506 O OG1 . THR A 1 315 ? 35.965 -17.625 -48.358 1.00 53.28 ? 315 THR A OG1 1 ATOM 2507 C CG2 . THR A 1 315 ? 36.031 -19.585 -46.976 1.00 53.83 ? 315 THR A CG2 1 ATOM 2508 N N . GLY A 1 316 ? 37.598 -17.859 -50.814 1.00 49.31 ? 316 GLY A N 1 ATOM 2509 C CA . GLY A 1 316 ? 37.755 -17.517 -52.212 1.00 49.42 ? 316 GLY A CA 1 ATOM 2510 C C . GLY A 1 316 ? 39.195 -17.531 -52.667 1.00 48.77 ? 316 GLY A C 1 ATOM 2511 O O . GLY A 1 316 ? 40.061 -18.116 -52.025 1.00 48.57 ? 316 GLY A O 1 ATOM 2512 N N . LEU A 1 317 ? 39.456 -16.849 -53.771 1.00 49.77 ? 317 LEU A N 1 ATOM 2513 C CA . LEU A 1 317 ? 40.759 -16.923 -54.415 1.00 51.73 ? 317 LEU A CA 1 ATOM 2514 C C . LEU A 1 317 ? 41.441 -15.558 -54.486 1.00 51.45 ? 317 LEU A C 1 ATOM 2515 O O . LEU A 1 317 ? 40.857 -14.542 -54.144 1.00 51.06 ? 317 LEU A O 1 ATOM 2516 C CB . LEU A 1 317 ? 40.634 -17.576 -55.803 1.00 53.03 ? 317 LEU A CB 1 ATOM 2517 C CG . LEU A 1 317 ? 39.497 -17.132 -56.718 1.00 53.65 ? 317 LEU A CG 1 ATOM 2518 C CD1 . LEU A 1 317 ? 39.811 -15.754 -57.255 1.00 56.63 ? 317 LEU A CD1 1 ATOM 2519 C CD2 . LEU A 1 317 ? 39.296 -18.099 -57.865 1.00 53.85 ? 317 LEU A CD2 1 ATOM 2520 N N . ARG A 1 318 ? 42.697 -15.571 -54.905 1.00 52.19 ? 318 ARG A N 1 ATOM 2521 C CA . ARG A 1 318 ? 43.519 -14.375 -54.991 1.00 54.32 ? 318 ARG A CA 1 ATOM 2522 C C . ARG A 1 318 ? 42.871 -13.341 -55.899 1.00 54.85 ? 318 ARG A C 1 ATOM 2523 O O . ARG A 1 318 ? 42.697 -13.577 -57.096 1.00 53.18 ? 318 ARG A O 1 ATOM 2524 C CB . ARG A 1 318 ? 44.909 -14.753 -55.516 1.00 55.90 ? 318 ARG A CB 1 ATOM 2525 C CG . ARG A 1 318 ? 45.889 -13.601 -55.599 1.00 59.95 ? 318 ARG A CG 1 ATOM 2526 C CD . ARG A 1 318 ? 47.196 -14.038 -56.236 1.00 63.50 ? 318 ARG A CD 1 ATOM 2527 N NE . ARG A 1 318 ? 48.019 -14.834 -55.325 1.00 64.60 ? 318 ARG A NE 1 ATOM 2528 C CZ . ARG A 1 318 ? 48.871 -14.329 -54.438 1.00 66.40 ? 318 ARG A CZ 1 ATOM 2529 N NH1 . ARG A 1 318 ? 49.020 -13.012 -54.308 1.00 68.50 ? 318 ARG A NH1 1 ATOM 2530 N NH2 . ARG A 1 318 ? 49.575 -15.149 -53.667 1.00 67.77 ? 318 ARG A NH2 1 ATOM 2531 N N . ASN A 1 319 ? 42.529 -12.197 -55.315 1.00 58.52 ? 319 ASN A N 1 ATOM 2532 C CA . ASN A 1 319 ? 41.780 -11.145 -56.003 1.00 60.99 ? 319 ASN A CA 1 ATOM 2533 C C . ASN A 1 319 ? 42.689 -10.230 -56.799 1.00 68.25 ? 319 ASN A C 1 ATOM 2534 O O . ASN A 1 319 ? 43.801 -9.928 -56.382 1.00 71.99 ? 319 ASN A O 1 ATOM 2535 C CB . ASN A 1 319 ? 40.981 -10.321 -55.004 1.00 59.21 ? 319 ASN A CB 1 ATOM 2536 C CG . ASN A 1 319 ? 39.902 -9.493 -55.665 1.00 59.69 ? 319 ASN A CG 1 ATOM 2537 O OD1 . ASN A 1 319 ? 39.600 -9.667 -56.839 1.00 58.61 ? 319 ASN A OD1 1 ATOM 2538 N ND2 . ASN A 1 319 ? 39.312 -8.583 -54.908 1.00 60.87 ? 319 ASN A ND2 1 ATOM 2539 N N . SER A 1 320 ? 42.193 -9.782 -57.946 1.00 77.44 ? 320 SER A N 1 ATOM 2540 C CA . SER A 1 320 ? 42.995 -9.039 -58.915 1.00 85.45 ? 320 SER A CA 1 ATOM 2541 C C . SER A 1 320 ? 42.892 -7.530 -58.698 1.00 92.17 ? 320 SER A C 1 ATOM 2542 O O . SER A 1 320 ? 41.816 -7.031 -58.364 1.00 91.13 ? 320 SER A O 1 ATOM 2543 C CB . SER A 1 320 ? 42.544 -9.378 -60.343 1.00 84.84 ? 320 SER A CB 1 ATOM 2544 O OG . SER A 1 320 ? 42.464 -10.782 -60.523 1.00 83.40 ? 320 SER A OG 1 ATOM 2545 N N . PRO A 1 321 ? 44.012 -6.803 -58.893 1.00 100.35 ? 321 PRO A N 1 ATOM 2546 C CA . PRO A 1 321 ? 43.979 -5.341 -58.894 1.00 105.91 ? 321 PRO A CA 1 ATOM 2547 C C . PRO A 1 321 ? 43.438 -4.786 -60.212 1.00 107.83 ? 321 PRO A C 1 ATOM 2548 O O . PRO A 1 321 ? 42.750 -3.763 -60.213 1.00 114.10 ? 321 PRO A O 1 ATOM 2549 C CB . PRO A 1 321 ? 45.451 -4.957 -58.707 1.00 108.40 ? 321 PRO A CB 1 ATOM 2550 C CG . PRO A 1 321 ? 46.213 -6.092 -59.294 1.00 106.37 ? 321 PRO A CG 1 ATOM 2551 C CD . PRO A 1 321 ? 45.387 -7.322 -59.042 1.00 101.86 ? 321 PRO A CD 1 ATOM 2552 N N . GLY B 2 1 ? 51.148 -18.794 -58.294 1.00 51.28 ? 1 GLY B N 1 ATOM 2553 C CA . GLY B 2 1 ? 50.829 -19.998 -57.472 1.00 49.04 ? 1 GLY B CA 1 ATOM 2554 C C . GLY B 2 1 ? 51.442 -21.248 -58.051 1.00 48.79 ? 1 GLY B C 1 ATOM 2555 O O . GLY B 2 1 ? 52.003 -21.222 -59.140 1.00 50.37 ? 1 GLY B O 1 ATOM 2556 N N . LEU B 2 2 ? 51.305 -22.358 -57.337 1.00 47.48 ? 2 LEU B N 1 ATOM 2557 C CA . LEU B 2 2 ? 51.969 -23.590 -57.740 1.00 47.62 ? 2 LEU B CA 1 ATOM 2558 C C . LEU B 2 2 ? 51.565 -24.092 -59.121 1.00 47.50 ? 2 LEU B C 1 ATOM 2559 O O . LEU B 2 2 ? 52.370 -24.718 -59.790 1.00 48.65 ? 2 LEU B O 1 ATOM 2560 C CB . LEU B 2 2 ? 51.724 -24.691 -56.719 1.00 46.51 ? 2 LEU B CB 1 ATOM 2561 C CG . LEU B 2 2 ? 52.427 -24.540 -55.383 1.00 46.12 ? 2 LEU B CG 1 ATOM 2562 C CD1 . LEU B 2 2 ? 51.952 -25.636 -54.446 1.00 44.70 ? 2 LEU B CD1 1 ATOM 2563 C CD2 . LEU B 2 2 ? 53.937 -24.564 -55.546 1.00 48.42 ? 2 LEU B CD2 1 ATOM 2564 N N . PHE B 2 3 ? 50.341 -23.805 -59.552 1.00 45.92 ? 3 PHE B N 1 ATOM 2565 C CA . PHE B 2 3 ? 49.810 -24.410 -60.777 1.00 46.58 ? 3 PHE B CA 1 ATOM 2566 C C . PHE B 2 3 ? 49.904 -23.529 -62.008 1.00 47.83 ? 3 PHE B C 1 ATOM 2567 O O . PHE B 2 3 ? 49.580 -23.968 -63.106 1.00 49.12 ? 3 PHE B O 1 ATOM 2568 C CB . PHE B 2 3 ? 48.396 -24.969 -60.519 1.00 45.04 ? 3 PHE B CB 1 ATOM 2569 C CG . PHE B 2 3 ? 48.419 -26.115 -59.546 1.00 44.87 ? 3 PHE B CG 1 ATOM 2570 C CD1 . PHE B 2 3 ? 48.686 -27.398 -59.982 1.00 45.43 ? 3 PHE B CD1 1 ATOM 2571 C CD2 . PHE B 2 3 ? 48.301 -25.887 -58.180 1.00 44.14 ? 3 PHE B CD2 1 ATOM 2572 C CE1 . PHE B 2 3 ? 48.784 -28.440 -59.082 1.00 46.05 ? 3 PHE B CE1 1 ATOM 2573 C CE2 . PHE B 2 3 ? 48.406 -26.927 -57.275 1.00 43.84 ? 3 PHE B CE2 1 ATOM 2574 C CZ . PHE B 2 3 ? 48.647 -28.203 -57.724 1.00 44.65 ? 3 PHE B CZ 1 ATOM 2575 N N . GLY B 2 4 ? 50.388 -22.303 -61.824 1.00 48.97 ? 4 GLY B N 1 ATOM 2576 C CA . GLY B 2 4 ? 50.761 -21.430 -62.930 1.00 49.98 ? 4 GLY B CA 1 ATOM 2577 C C . GLY B 2 4 ? 49.640 -20.697 -63.640 1.00 49.76 ? 4 GLY B C 1 ATOM 2578 O O . GLY B 2 4 ? 49.913 -19.902 -64.546 1.00 51.67 ? 4 GLY B O 1 ATOM 2579 N N . ALA B 2 5 ? 48.385 -20.943 -63.257 1.00 47.82 ? 5 ALA B N 1 ATOM 2580 C CA . ALA B 2 5 ? 47.240 -20.333 -63.961 1.00 46.84 ? 5 ALA B CA 1 ATOM 2581 C C . ALA B 2 5 ? 46.881 -18.975 -63.397 1.00 46.79 ? 5 ALA B C 1 ATOM 2582 O O . ALA B 2 5 ? 47.078 -17.967 -64.060 1.00 48.44 ? 5 ALA B O 1 ATOM 2583 C CB . ALA B 2 5 ? 46.025 -21.252 -63.924 1.00 45.52 ? 5 ALA B CB 1 ATOM 2584 N N . ILE B 2 6 ? 46.353 -18.954 -62.175 1.00 46.37 ? 6 ILE B N 1 ATOM 2585 C CA . ILE B 2 6 ? 45.915 -17.716 -61.529 1.00 47.52 ? 6 ILE B CA 1 ATOM 2586 C C . ILE B 2 6 ? 47.085 -16.744 -61.342 1.00 49.83 ? 6 ILE B C 1 ATOM 2587 O O . ILE B 2 6 ? 48.116 -17.093 -60.764 1.00 50.26 ? 6 ILE B O 1 ATOM 2588 C CB . ILE B 2 6 ? 45.267 -18.000 -60.158 1.00 46.97 ? 6 ILE B CB 1 ATOM 2589 C CG1 . ILE B 2 6 ? 43.896 -18.639 -60.353 1.00 46.04 ? 6 ILE B CG1 1 ATOM 2590 C CG2 . ILE B 2 6 ? 45.122 -16.712 -59.351 1.00 48.28 ? 6 ILE B CG2 1 ATOM 2591 C CD1 . ILE B 2 6 ? 43.242 -19.092 -59.069 1.00 45.47 ? 6 ILE B CD1 1 ATOM 2592 N N . ALA B 2 7 ? 46.922 -15.524 -61.835 1.00 51.70 ? 7 ALA B N 1 ATOM 2593 C CA . ALA B 2 7 ? 48.015 -14.548 -61.836 1.00 54.76 ? 7 ALA B CA 1 ATOM 2594 C C . ALA B 2 7 ? 49.284 -15.147 -62.445 1.00 56.46 ? 7 ALA B C 1 ATOM 2595 O O . ALA B 2 7 ? 50.390 -14.834 -62.023 1.00 58.01 ? 7 ALA B O 1 ATOM 2596 C CB . ALA B 2 7 ? 48.284 -14.046 -60.424 1.00 54.79 ? 7 ALA B CB 1 ATOM 2597 N N . GLY B 2 8 ? 49.103 -16.014 -63.434 1.00 57.23 ? 8 GLY B N 1 ATOM 2598 C CA . GLY B 2 8 ? 50.206 -16.692 -64.111 1.00 59.22 ? 8 GLY B CA 1 ATOM 2599 C C . GLY B 2 8 ? 50.052 -16.431 -65.594 1.00 61.10 ? 8 GLY B C 1 ATOM 2600 O O . GLY B 2 8 ? 50.214 -15.298 -66.026 1.00 64.65 ? 8 GLY B O 1 ATOM 2601 N N . PHE B 2 9 ? 49.720 -17.461 -66.370 1.00 59.82 ? 9 PHE B N 1 ATOM 2602 C CA . PHE B 2 9 ? 49.461 -17.275 -67.793 1.00 60.82 ? 9 PHE B CA 1 ATOM 2603 C C . PHE B 2 9 ? 48.068 -16.685 -68.006 1.00 60.84 ? 9 PHE B C 1 ATOM 2604 O O . PHE B 2 9 ? 47.785 -16.147 -69.074 1.00 64.12 ? 9 PHE B O 1 ATOM 2605 C CB . PHE B 2 9 ? 49.691 -18.566 -68.607 1.00 60.89 ? 9 PHE B CB 1 ATOM 2606 C CG . PHE B 2 9 ? 48.682 -19.646 -68.357 1.00 58.21 ? 9 PHE B CG 1 ATOM 2607 C CD1 . PHE B 2 9 ? 47.467 -19.649 -69.030 1.00 57.51 ? 9 PHE B CD1 1 ATOM 2608 C CD2 . PHE B 2 9 ? 48.950 -20.666 -67.467 1.00 56.89 ? 9 PHE B CD2 1 ATOM 2609 C CE1 . PHE B 2 9 ? 46.525 -20.640 -68.796 1.00 55.83 ? 9 PHE B CE1 1 ATOM 2610 C CE2 . PHE B 2 9 ? 48.020 -21.662 -67.231 1.00 55.60 ? 9 PHE B CE2 1 ATOM 2611 C CZ . PHE B 2 9 ? 46.802 -21.646 -67.891 1.00 55.08 ? 9 PHE B CZ 1 ATOM 2612 N N . ILE B 2 10 ? 47.200 -16.779 -67.001 1.00 59.24 ? 10 ILE B N 1 ATOM 2613 C CA . ILE B 2 10 ? 45.976 -15.981 -66.980 1.00 59.73 ? 10 ILE B CA 1 ATOM 2614 C C . ILE B 2 10 ? 46.229 -14.810 -66.045 1.00 62.83 ? 10 ILE B C 1 ATOM 2615 O O . ILE B 2 10 ? 46.259 -14.965 -64.825 1.00 63.28 ? 10 ILE B O 1 ATOM 2616 C CB . ILE B 2 10 ? 44.752 -16.780 -66.521 1.00 56.74 ? 10 ILE B CB 1 ATOM 2617 C CG1 . ILE B 2 10 ? 44.611 -18.044 -67.366 1.00 56.43 ? 10 ILE B CG1 1 ATOM 2618 C CG2 . ILE B 2 10 ? 43.504 -15.924 -66.654 1.00 56.12 ? 10 ILE B CG2 1 ATOM 2619 C CD1 . ILE B 2 10 ? 43.562 -19.011 -66.867 1.00 55.31 ? 10 ILE B CD1 1 ATOM 2620 N N . GLU B 2 11 ? 46.426 -13.636 -66.627 1.00 67.34 ? 11 GLU B N 1 ATOM 2621 C CA . GLU B 2 11 ? 46.995 -12.510 -65.894 1.00 71.30 ? 11 GLU B CA 1 ATOM 2622 C C . GLU B 2 11 ? 46.117 -11.955 -64.782 1.00 68.52 ? 11 GLU B C 1 ATOM 2623 O O . GLU B 2 11 ? 46.628 -11.494 -63.760 1.00 69.41 ? 11 GLU B O 1 ATOM 2624 C CB . GLU B 2 11 ? 47.372 -11.392 -66.864 1.00 78.29 ? 11 GLU B CB 1 ATOM 2625 C CG . GLU B 2 11 ? 48.577 -11.735 -67.729 1.00 83.63 ? 11 GLU B CG 1 ATOM 2626 C CD . GLU B 2 11 ? 49.327 -10.499 -68.195 1.00 91.38 ? 11 GLU B CD 1 ATOM 2627 O OE1 . GLU B 2 11 ? 48.666 -9.539 -68.666 1.00 94.55 ? 11 GLU B OE1 1 ATOM 2628 O OE2 . GLU B 2 11 ? 50.576 -10.492 -68.080 1.00 94.68 ? 11 GLU B OE2 1 ATOM 2629 N N . GLY B 2 12 ? 44.805 -11.989 -64.979 1.00 65.77 ? 12 GLY B N 1 ATOM 2630 C CA . GLY B 2 12 ? 43.883 -11.446 -63.986 1.00 64.53 ? 12 GLY B CA 1 ATOM 2631 C C . GLY B 2 12 ? 42.516 -12.073 -64.031 1.00 61.12 ? 12 GLY B C 1 ATOM 2632 O O . GLY B 2 12 ? 42.156 -12.714 -65.012 1.00 61.98 ? 12 GLY B O 1 ATOM 2633 N N . GLY B 2 13 ? 41.761 -11.895 -62.957 1.00 59.53 ? 13 GLY B N 1 ATOM 2634 C CA . GLY B 2 13 ? 40.384 -12.366 -62.891 1.00 58.27 ? 13 GLY B CA 1 ATOM 2635 C C . GLY B 2 13 ? 39.420 -11.442 -63.625 1.00 59.31 ? 13 GLY B C 1 ATOM 2636 O O . GLY B 2 13 ? 39.829 -10.451 -64.223 1.00 61.42 ? 13 GLY B O 1 ATOM 2637 N N . TRP B 2 14 ? 38.135 -11.773 -63.566 1.00 58.12 ? 14 TRP B N 1 ATOM 2638 C CA . TRP B 2 14 ? 37.106 -11.070 -64.310 1.00 58.87 ? 14 TRP B CA 1 ATOM 2639 C C . TRP B 2 14 ? 36.055 -10.505 -63.370 1.00 61.98 ? 14 TRP B C 1 ATOM 2640 O O . TRP B 2 14 ? 35.275 -11.254 -62.788 1.00 61.05 ? 14 TRP B O 1 ATOM 2641 C CB . TRP B 2 14 ? 36.421 -12.029 -65.291 1.00 56.57 ? 14 TRP B CB 1 ATOM 2642 C CG . TRP B 2 14 ? 37.285 -12.503 -66.428 1.00 54.52 ? 14 TRP B CG 1 ATOM 2643 C CD1 . TRP B 2 14 ? 38.315 -11.833 -67.002 1.00 54.99 ? 14 TRP B CD1 1 ATOM 2644 C CD2 . TRP B 2 14 ? 37.151 -13.733 -67.159 1.00 52.38 ? 14 TRP B CD2 1 ATOM 2645 N NE1 . TRP B 2 14 ? 38.844 -12.571 -68.036 1.00 53.89 ? 14 TRP B NE1 1 ATOM 2646 C CE2 . TRP B 2 14 ? 38.144 -13.739 -68.155 1.00 52.36 ? 14 TRP B CE2 1 ATOM 2647 C CE3 . TRP B 2 14 ? 36.283 -14.824 -67.071 1.00 51.67 ? 14 TRP B CE3 1 ATOM 2648 C CZ2 . TRP B 2 14 ? 38.310 -14.806 -69.047 1.00 52.04 ? 14 TRP B CZ2 1 ATOM 2649 C CZ3 . TRP B 2 14 ? 36.443 -15.882 -67.959 1.00 50.86 ? 14 TRP B CZ3 1 ATOM 2650 C CH2 . TRP B 2 14 ? 37.454 -15.865 -68.933 1.00 51.10 ? 14 TRP B CH2 1 ATOM 2651 N N . GLN B 2 15 ? 36.014 -9.179 -63.244 1.00 67.09 ? 15 GLN B N 1 ATOM 2652 C CA . GLN B 2 15 ? 34.917 -8.502 -62.534 1.00 70.87 ? 15 GLN B CA 1 ATOM 2653 C C . GLN B 2 15 ? 33.562 -8.917 -63.109 1.00 70.13 ? 15 GLN B C 1 ATOM 2654 O O . GLN B 2 15 ? 32.572 -8.968 -62.387 1.00 70.71 ? 15 GLN B O 1 ATOM 2655 C CB . GLN B 2 15 ? 35.044 -6.973 -62.629 1.00 75.40 ? 15 GLN B CB 1 ATOM 2656 C CG . GLN B 2 15 ? 36.292 -6.369 -62.000 1.00 78.04 ? 15 GLN B CG 1 ATOM 2657 C CD . GLN B 2 15 ? 36.228 -6.305 -60.485 1.00 80.52 ? 15 GLN B CD 1 ATOM 2658 O OE1 . GLN B 2 15 ? 37.021 -6.948 -59.792 1.00 81.41 ? 15 GLN B OE1 1 ATOM 2659 N NE2 . GLN B 2 15 ? 35.286 -5.528 -59.961 1.00 84.34 ? 15 GLN B NE2 1 ATOM 2660 N N . GLY B 2 16 ? 33.532 -9.209 -64.409 1.00 69.98 ? 16 GLY B N 1 ATOM 2661 C CA . GLY B 2 16 ? 32.292 -9.507 -65.133 1.00 71.26 ? 16 GLY B CA 1 ATOM 2662 C C . GLY B 2 16 ? 31.685 -10.897 -64.982 1.00 70.32 ? 16 GLY B C 1 ATOM 2663 O O . GLY B 2 16 ? 30.575 -11.129 -65.456 1.00 72.15 ? 16 GLY B O 1 ATOM 2664 N N . MET B 2 17 ? 32.392 -11.829 -64.343 1.00 67.87 ? 17 MET B N 1 ATOM 2665 C CA . MET B 2 17 ? 31.818 -13.142 -64.049 1.00 67.25 ? 17 MET B CA 1 ATOM 2666 C C . MET B 2 17 ? 31.388 -13.230 -62.582 1.00 67.55 ? 17 MET B C 1 ATOM 2667 O O . MET B 2 17 ? 32.204 -13.469 -61.698 1.00 66.31 ? 17 MET B O 1 ATOM 2668 C CB . MET B 2 17 ? 32.815 -14.246 -64.365 1.00 65.90 ? 17 MET B CB 1 ATOM 2669 C CG . MET B 2 17 ? 32.225 -15.631 -64.208 1.00 66.07 ? 17 MET B CG 1 ATOM 2670 S SD . MET B 2 17 ? 33.301 -16.872 -64.917 1.00 65.20 ? 17 MET B SD 1 ATOM 2671 C CE . MET B 2 17 ? 34.765 -16.573 -63.937 1.00 64.50 ? 17 MET B CE 1 ATOM 2672 N N . VAL B 2 18 ? 30.097 -13.046 -62.334 1.00 69.94 ? 18 VAL B N 1 ATOM 2673 C CA . VAL B 2 18 ? 29.575 -12.944 -60.971 1.00 71.53 ? 18 VAL B CA 1 ATOM 2674 C C . VAL B 2 18 ? 28.913 -14.228 -60.477 1.00 71.98 ? 18 VAL B C 1 ATOM 2675 O O . VAL B 2 18 ? 28.721 -14.409 -59.279 1.00 72.15 ? 18 VAL B O 1 ATOM 2676 C CB . VAL B 2 18 ? 28.564 -11.791 -60.862 1.00 75.10 ? 18 VAL B CB 1 ATOM 2677 C CG1 . VAL B 2 18 ? 29.162 -10.516 -61.445 1.00 76.02 ? 18 VAL B CG1 1 ATOM 2678 C CG2 . VAL B 2 18 ? 27.250 -12.143 -61.555 1.00 76.75 ? 18 VAL B CG2 1 ATOM 2679 N N . ASP B 2 19 ? 28.582 -15.123 -61.400 1.00 72.72 ? 19 ASP B N 1 ATOM 2680 C CA . ASP B 2 19 ? 27.814 -16.327 -61.072 1.00 74.28 ? 19 ASP B CA 1 ATOM 2681 C C . ASP B 2 19 ? 28.693 -17.568 -60.802 1.00 70.22 ? 19 ASP B C 1 ATOM 2682 O O . ASP B 2 19 ? 28.188 -18.687 -60.757 1.00 71.74 ? 19 ASP B O 1 ATOM 2683 C CB . ASP B 2 19 ? 26.762 -16.603 -62.175 1.00 77.16 ? 19 ASP B CB 1 ATOM 2684 C CG . ASP B 2 19 ? 27.359 -16.634 -63.596 1.00 77.52 ? 19 ASP B CG 1 ATOM 2685 O OD1 . ASP B 2 19 ? 28.558 -16.310 -63.789 1.00 75.20 ? 19 ASP B OD1 1 ATOM 2686 O OD2 . ASP B 2 19 ? 26.611 -16.982 -64.536 1.00 80.78 ? 19 ASP B OD2 1 ATOM 2687 N N . GLY B 2 20 ? 29.993 -17.382 -60.599 1.00 65.28 ? 20 GLY B N 1 ATOM 2688 C CA . GLY B 2 20 ? 30.859 -18.521 -60.321 1.00 63.08 ? 20 GLY B CA 1 ATOM 2689 C C . GLY B 2 20 ? 32.311 -18.165 -60.073 1.00 61.34 ? 20 GLY B C 1 ATOM 2690 O O . GLY B 2 20 ? 32.729 -17.023 -60.288 1.00 62.39 ? 20 GLY B O 1 ATOM 2691 N N . TRP B 2 21 ? 33.091 -19.145 -59.625 1.00 58.54 ? 21 TRP B N 1 ATOM 2692 C CA . TRP B 2 21 ? 34.507 -18.905 -59.357 1.00 56.25 ? 21 TRP B CA 1 ATOM 2693 C C . TRP B 2 21 ? 35.353 -19.071 -60.611 1.00 53.13 ? 21 TRP B C 1 ATOM 2694 O O . TRP B 2 21 ? 36.343 -18.368 -60.788 1.00 51.38 ? 21 TRP B O 1 ATOM 2695 C CB . TRP B 2 21 ? 35.024 -19.815 -58.232 1.00 56.69 ? 21 TRP B CB 1 ATOM 2696 C CG . TRP B 2 21 ? 34.920 -19.229 -56.837 1.00 58.74 ? 21 TRP B CG 1 ATOM 2697 C CD1 . TRP B 2 21 ? 35.020 -17.911 -56.473 1.00 60.30 ? 21 TRP B CD1 1 ATOM 2698 C CD2 . TRP B 2 21 ? 34.741 -19.956 -55.630 1.00 60.57 ? 21 TRP B CD2 1 ATOM 2699 N NE1 . TRP B 2 21 ? 34.895 -17.777 -55.114 1.00 61.53 ? 21 TRP B NE1 1 ATOM 2700 C CE2 . TRP B 2 21 ? 34.724 -19.020 -54.572 1.00 61.62 ? 21 TRP B CE2 1 ATOM 2701 C CE3 . TRP B 2 21 ? 34.598 -21.312 -55.337 1.00 62.08 ? 21 TRP B CE3 1 ATOM 2702 C CZ2 . TRP B 2 21 ? 34.564 -19.397 -53.252 1.00 63.92 ? 21 TRP B CZ2 1 ATOM 2703 C CZ3 . TRP B 2 21 ? 34.443 -21.691 -54.020 1.00 64.51 ? 21 TRP B CZ3 1 ATOM 2704 C CH2 . TRP B 2 21 ? 34.424 -20.735 -52.990 1.00 65.49 ? 21 TRP B CH2 1 ATOM 2705 N N . TYR B 2 22 ? 34.966 -20.017 -61.463 1.00 52.01 ? 22 TYR B N 1 ATOM 2706 C CA . TYR B 2 22 ? 35.684 -20.306 -62.697 1.00 50.41 ? 22 TYR B CA 1 ATOM 2707 C C . TYR B 2 22 ? 34.696 -20.428 -63.830 1.00 50.27 ? 22 TYR B C 1 ATOM 2708 O O . TYR B 2 22 ? 33.556 -20.843 -63.616 1.00 50.73 ? 22 TYR B O 1 ATOM 2709 C CB . TYR B 2 22 ? 36.450 -21.628 -62.599 1.00 49.38 ? 22 TYR B CB 1 ATOM 2710 C CG . TYR B 2 22 ? 36.901 -22.005 -61.213 1.00 49.33 ? 22 TYR B CG 1 ATOM 2711 C CD1 . TYR B 2 22 ? 37.865 -21.266 -60.554 1.00 48.96 ? 22 TYR B CD1 1 ATOM 2712 C CD2 . TYR B 2 22 ? 36.373 -23.120 -60.564 1.00 50.59 ? 22 TYR B CD2 1 ATOM 2713 C CE1 . TYR B 2 22 ? 38.297 -21.623 -59.286 1.00 49.00 ? 22 TYR B CE1 1 ATOM 2714 C CE2 . TYR B 2 22 ? 36.793 -23.478 -59.295 1.00 50.02 ? 22 TYR B CE2 1 ATOM 2715 C CZ . TYR B 2 22 ? 37.754 -22.727 -58.665 1.00 49.26 ? 22 TYR B CZ 1 ATOM 2716 O OH . TYR B 2 22 ? 38.182 -23.067 -57.405 1.00 49.67 ? 22 TYR B OH 1 ATOM 2717 N N . GLY B 2 23 ? 35.138 -20.094 -65.038 1.00 49.68 ? 23 GLY B N 1 ATOM 2718 C CA . GLY B 2 23 ? 34.270 -20.205 -66.198 1.00 51.31 ? 23 GLY B CA 1 ATOM 2719 C C . GLY B 2 23 ? 34.893 -19.762 -67.502 1.00 52.13 ? 23 GLY B C 1 ATOM 2720 O O . GLY B 2 23 ? 36.126 -19.702 -67.633 1.00 50.38 ? 23 GLY B O 1 ATOM 2721 N N . TYR B 2 24 ? 34.019 -19.443 -68.460 1.00 54.40 ? 24 TYR B N 1 ATOM 2722 C CA . TYR B 2 24 ? 34.419 -19.144 -69.836 1.00 55.29 ? 24 TYR B CA 1 ATOM 2723 C C . TYR B 2 24 ? 34.009 -17.745 -70.252 1.00 55.11 ? 24 TYR B C 1 ATOM 2724 O O . TYR B 2 24 ? 32.996 -17.242 -69.790 1.00 56.07 ? 24 TYR B O 1 ATOM 2725 C CB . TYR B 2 24 ? 33.757 -20.124 -70.805 1.00 56.99 ? 24 TYR B CB 1 ATOM 2726 C CG . TYR B 2 24 ? 33.831 -21.556 -70.367 1.00 58.05 ? 24 TYR B CG 1 ATOM 2727 C CD1 . TYR B 2 24 ? 32.886 -22.082 -69.501 1.00 59.45 ? 24 TYR B CD1 1 ATOM 2728 C CD2 . TYR B 2 24 ? 34.846 -22.388 -70.814 1.00 58.79 ? 24 TYR B CD2 1 ATOM 2729 C CE1 . TYR B 2 24 ? 32.945 -23.396 -69.091 1.00 61.04 ? 24 TYR B CE1 1 ATOM 2730 C CE2 . TYR B 2 24 ? 34.918 -23.707 -70.408 1.00 59.71 ? 24 TYR B CE2 1 ATOM 2731 C CZ . TYR B 2 24 ? 33.966 -24.204 -69.546 1.00 61.24 ? 24 TYR B CZ 1 ATOM 2732 O OH . TYR B 2 24 ? 34.025 -25.509 -69.138 1.00 64.03 ? 24 TYR B OH 1 ATOM 2733 N N . HIS B 2 25 ? 34.799 -17.137 -71.137 1.00 54.96 ? 25 HIS B N 1 ATOM 2734 C CA . HIS B 2 25 ? 34.390 -15.935 -71.862 1.00 56.09 ? 25 HIS B CA 1 ATOM 2735 C C . HIS B 2 25 ? 34.514 -16.181 -73.354 1.00 56.87 ? 25 HIS B C 1 ATOM 2736 O O . HIS B 2 25 ? 35.550 -16.621 -73.813 1.00 56.40 ? 25 HIS B O 1 ATOM 2737 C CB . HIS B 2 25 ? 35.253 -14.739 -71.496 1.00 55.76 ? 25 HIS B CB 1 ATOM 2738 C CG . HIS B 2 25 ? 34.870 -13.490 -72.219 1.00 57.61 ? 25 HIS B CG 1 ATOM 2739 N ND1 . HIS B 2 25 ? 35.510 -13.068 -73.365 1.00 58.32 ? 25 HIS B ND1 1 ATOM 2740 C CD2 . HIS B 2 25 ? 33.885 -12.589 -71.984 1.00 58.83 ? 25 HIS B CD2 1 ATOM 2741 C CE1 . HIS B 2 25 ? 34.952 -11.949 -73.790 1.00 59.80 ? 25 HIS B CE1 1 ATOM 2742 N NE2 . HIS B 2 25 ? 33.965 -11.637 -72.969 1.00 60.05 ? 25 HIS B NE2 1 ATOM 2743 N N . HIS B 2 26 ? 33.462 -15.885 -74.110 1.00 59.08 ? 26 HIS B N 1 ATOM 2744 C CA . HIS B 2 26 ? 33.462 -16.141 -75.557 1.00 60.14 ? 26 HIS B CA 1 ATOM 2745 C C . HIS B 2 26 ? 33.260 -14.852 -76.319 1.00 61.03 ? 26 HIS B C 1 ATOM 2746 O O . HIS B 2 26 ? 32.636 -13.942 -75.810 1.00 61.64 ? 26 HIS B O 1 ATOM 2747 C CB . HIS B 2 26 ? 32.347 -17.128 -75.924 1.00 60.84 ? 26 HIS B CB 1 ATOM 2748 C CG . HIS B 2 26 ? 30.982 -16.533 -75.892 1.00 62.23 ? 26 HIS B CG 1 ATOM 2749 N ND1 . HIS B 2 26 ? 30.251 -16.414 -74.731 1.00 64.18 ? 26 HIS B ND1 1 ATOM 2750 C CD2 . HIS B 2 26 ? 30.217 -16.004 -76.874 1.00 64.39 ? 26 HIS B CD2 1 ATOM 2751 C CE1 . HIS B 2 26 ? 29.092 -15.835 -74.997 1.00 64.75 ? 26 HIS B CE1 1 ATOM 2752 N NE2 . HIS B 2 26 ? 29.045 -15.580 -76.292 1.00 65.82 ? 26 HIS B NE2 1 ATOM 2753 N N . SER B 2 27 ? 33.802 -14.768 -77.529 1.00 61.82 ? 27 SER B N 1 ATOM 2754 C CA . SER B 2 27 ? 33.426 -13.689 -78.444 1.00 63.90 ? 27 SER B CA 1 ATOM 2755 C C . SER B 2 27 ? 33.479 -14.113 -79.917 1.00 64.69 ? 27 SER B C 1 ATOM 2756 O O . SER B 2 27 ? 34.421 -14.767 -80.363 1.00 64.39 ? 27 SER B O 1 ATOM 2757 C CB . SER B 2 27 ? 34.256 -12.433 -78.200 1.00 64.46 ? 27 SER B CB 1 ATOM 2758 O OG . SER B 2 27 ? 35.613 -12.679 -78.413 1.00 64.37 ? 27 SER B OG 1 ATOM 2759 N N . ASN B 2 28 ? 32.433 -13.739 -80.647 1.00 66.27 ? 28 ASN B N 1 ATOM 2760 C CA . ASN B 2 28 ? 32.248 -14.119 -82.043 1.00 67.25 ? 28 ASN B CA 1 ATOM 2761 C C . ASN B 2 28 ? 31.385 -13.047 -82.709 1.00 69.93 ? 28 ASN B C 1 ATOM 2762 O O . ASN B 2 28 ? 31.218 -11.973 -82.137 1.00 70.66 ? 28 ASN B O 1 ATOM 2763 C CB . ASN B 2 28 ? 31.617 -15.518 -82.131 1.00 65.87 ? 28 ASN B CB 1 ATOM 2764 C CG . ASN B 2 28 ? 30.261 -15.597 -81.456 1.00 64.82 ? 28 ASN B CG 1 ATOM 2765 O OD1 . ASN B 2 28 ? 29.602 -14.588 -81.256 1.00 65.73 ? 28 ASN B OD1 1 ATOM 2766 N ND2 . ASN B 2 28 ? 29.843 -16.801 -81.101 1.00 63.59 ? 28 ASN B ND2 1 ATOM 2767 N N . GLU B 2 29 ? 30.845 -13.310 -83.896 1.00 72.79 ? 29 GLU B N 1 ATOM 2768 C CA . GLU B 2 29 ? 30.090 -12.276 -84.619 1.00 76.87 ? 29 GLU B CA 1 ATOM 2769 C C . GLU B 2 29 ? 28.777 -11.899 -83.947 1.00 78.26 ? 29 GLU B C 1 ATOM 2770 O O . GLU B 2 29 ? 28.318 -10.773 -84.089 1.00 80.42 ? 29 GLU B O 1 ATOM 2771 C CB . GLU B 2 29 ? 29.797 -12.709 -86.053 1.00 79.92 ? 29 GLU B CB 1 ATOM 2772 C CG . GLU B 2 29 ? 31.042 -12.911 -86.902 1.00 81.20 ? 29 GLU B CG 1 ATOM 2773 C CD . GLU B 2 29 ? 30.721 -13.241 -88.351 1.00 83.80 ? 29 GLU B CD 1 ATOM 2774 O OE1 . GLU B 2 29 ? 29.748 -12.689 -88.912 1.00 84.66 ? 29 GLU B OE1 1 ATOM 2775 O OE2 . GLU B 2 29 ? 31.457 -14.063 -88.931 1.00 85.72 ? 29 GLU B OE2 1 ATOM 2776 N N . GLN B 2 30 ? 28.175 -12.843 -83.231 1.00 78.88 ? 30 GLN B N 1 ATOM 2777 C CA . GLN B 2 30 ? 26.901 -12.613 -82.540 1.00 81.23 ? 30 GLN B CA 1 ATOM 2778 C C . GLN B 2 30 ? 27.060 -11.807 -81.249 1.00 79.08 ? 30 GLN B C 1 ATOM 2779 O O . GLN B 2 30 ? 26.089 -11.239 -80.752 1.00 79.35 ? 30 GLN B O 1 ATOM 2780 C CB . GLN B 2 30 ? 26.217 -13.946 -82.225 1.00 83.90 ? 30 GLN B CB 1 ATOM 2781 C CG . GLN B 2 30 ? 25.798 -14.743 -83.454 1.00 88.28 ? 30 GLN B CG 1 ATOM 2782 C CD . GLN B 2 30 ? 26.108 -16.229 -83.313 1.00 91.15 ? 30 GLN B CD 1 ATOM 2783 O OE1 . GLN B 2 30 ? 27.262 -16.659 -83.465 1.00 90.77 ? 30 GLN B OE1 1 ATOM 2784 N NE2 . GLN B 2 30 ? 25.078 -17.022 -83.024 1.00 94.03 ? 30 GLN B NE2 1 ATOM 2785 N N . GLY B 2 31 ? 28.273 -11.770 -80.699 1.00 75.77 ? 31 GLY B N 1 ATOM 2786 C CA . GLY B 2 31 ? 28.533 -11.022 -79.466 1.00 74.62 ? 31 GLY B CA 1 ATOM 2787 C C . GLY B 2 31 ? 29.516 -11.700 -78.537 1.00 70.44 ? 31 GLY B C 1 ATOM 2788 O O . GLY B 2 31 ? 30.374 -12.448 -78.981 1.00 68.32 ? 31 GLY B O 1 ATOM 2789 N N . SER B 2 32 ? 29.388 -11.432 -77.241 1.00 69.44 ? 32 SER B N 1 ATOM 2790 C CA . SER B 2 32 ? 30.334 -11.958 -76.261 1.00 66.78 ? 32 SER B CA 1 ATOM 2791 C C . SER B 2 32 ? 29.776 -11.953 -74.850 1.00 66.30 ? 32 SER B C 1 ATOM 2792 O O . SER B 2 32 ? 28.812 -11.257 -74.564 1.00 68.30 ? 32 SER B O 1 ATOM 2793 C CB . SER B 2 32 ? 31.611 -11.124 -76.279 1.00 66.51 ? 32 SER B CB 1 ATOM 2794 O OG . SER B 2 32 ? 31.364 -9.842 -75.746 1.00 68.60 ? 32 SER B OG 1 ATOM 2795 N N . GLY B 2 33 ? 30.396 -12.730 -73.968 1.00 64.39 ? 33 GLY B N 1 ATOM 2796 C CA . GLY B 2 33 ? 30.002 -12.740 -72.562 1.00 64.62 ? 33 GLY B CA 1 ATOM 2797 C C . GLY B 2 33 ? 30.649 -13.801 -71.696 1.00 61.54 ? 33 GLY B C 1 ATOM 2798 O O . GLY B 2 33 ? 31.489 -14.563 -72.152 1.00 60.82 ? 33 GLY B O 1 ATOM 2799 N N . TYR B 2 34 ? 30.235 -13.838 -70.434 1.00 61.94 ? 34 TYR B N 1 ATOM 2800 C CA . TYR B 2 34 ? 30.802 -14.740 -69.436 1.00 60.28 ? 34 TYR B CA 1 ATOM 2801 C C . TYR B 2 34 ? 29.836 -15.852 -69.078 1.00 60.79 ? 34 TYR B C 1 ATOM 2802 O O . TYR B 2 34 ? 28.641 -15.627 -68.973 1.00 62.58 ? 34 TYR B O 1 ATOM 2803 C CB . TYR B 2 34 ? 31.143 -13.970 -68.160 1.00 59.95 ? 34 TYR B CB 1 ATOM 2804 C CG . TYR B 2 34 ? 32.102 -12.823 -68.364 1.00 60.02 ? 34 TYR B CG 1 ATOM 2805 C CD1 . TYR B 2 34 ? 33.478 -13.013 -68.324 1.00 58.08 ? 34 TYR B CD1 1 ATOM 2806 C CD2 . TYR B 2 34 ? 31.629 -11.542 -68.592 1.00 62.75 ? 34 TYR B CD2 1 ATOM 2807 C CE1 . TYR B 2 34 ? 34.349 -11.946 -68.510 1.00 59.16 ? 34 TYR B CE1 1 ATOM 2808 C CE2 . TYR B 2 34 ? 32.489 -10.477 -68.781 1.00 63.36 ? 34 TYR B CE2 1 ATOM 2809 C CZ . TYR B 2 34 ? 33.840 -10.682 -68.739 1.00 62.14 ? 34 TYR B CZ 1 ATOM 2810 O OH . TYR B 2 34 ? 34.668 -9.602 -68.923 1.00 64.96 ? 34 TYR B OH 1 ATOM 2811 N N . ALA B 2 35 ? 30.365 -17.049 -68.867 1.00 60.14 ? 35 ALA B N 1 ATOM 2812 C CA . ALA B 2 35 ? 29.564 -18.174 -68.402 1.00 61.73 ? 35 ALA B CA 1 ATOM 2813 C C . ALA B 2 35 ? 30.353 -19.033 -67.407 1.00 61.33 ? 35 ALA B C 1 ATOM 2814 O O . ALA B 2 35 ? 31.397 -19.594 -67.735 1.00 60.53 ? 35 ALA B O 1 ATOM 2815 C CB . ALA B 2 35 ? 29.114 -19.011 -69.578 1.00 62.47 ? 35 ALA B CB 1 ATOM 2816 N N . ALA B 2 36 ? 29.834 -19.129 -66.191 1.00 63.12 ? 36 ALA B N 1 ATOM 2817 C CA . ALA B 2 36 ? 30.459 -19.902 -65.135 1.00 62.85 ? 36 ALA B CA 1 ATOM 2818 C C . ALA B 2 36 ? 30.384 -21.392 -65.433 1.00 64.04 ? 36 ALA B C 1 ATOM 2819 O O . ALA B 2 36 ? 29.383 -21.865 -65.947 1.00 67.38 ? 36 ALA B O 1 ATOM 2820 C CB . ALA B 2 36 ? 29.770 -19.604 -63.811 1.00 64.33 ? 36 ALA B CB 1 ATOM 2821 N N . ASP B 2 37 ? 31.453 -22.119 -65.112 1.00 64.10 ? 37 ASP B N 1 ATOM 2822 C CA . ASP B 2 37 ? 31.459 -23.579 -65.139 1.00 65.20 ? 37 ASP B CA 1 ATOM 2823 C C . ASP B 2 37 ? 30.975 -24.088 -63.773 1.00 69.22 ? 37 ASP B C 1 ATOM 2824 O O . ASP B 2 37 ? 31.685 -23.981 -62.761 1.00 67.35 ? 37 ASP B O 1 ATOM 2825 C CB . ASP B 2 37 ? 32.864 -24.080 -65.437 1.00 64.30 ? 37 ASP B CB 1 ATOM 2826 C CG . ASP B 2 37 ? 32.929 -25.578 -65.605 1.00 65.56 ? 37 ASP B CG 1 ATOM 2827 O OD1 . ASP B 2 37 ? 33.083 -26.278 -64.581 1.00 66.19 ? 37 ASP B OD1 1 ATOM 2828 O OD2 . ASP B 2 37 ? 32.837 -26.050 -66.761 1.00 64.68 ? 37 ASP B OD2 1 ATOM 2829 N N . LYS B 2 38 ? 29.758 -24.632 -63.755 1.00 74.48 ? 38 LYS B N 1 ATOM 2830 C CA . LYS B 2 38 ? 29.072 -24.993 -62.515 1.00 77.19 ? 38 LYS B CA 1 ATOM 2831 C C . LYS B 2 38 ? 29.696 -26.173 -61.792 1.00 75.35 ? 38 LYS B C 1 ATOM 2832 O O . LYS B 2 38 ? 29.768 -26.167 -60.570 1.00 74.69 ? 38 LYS B O 1 ATOM 2833 C CB . LYS B 2 38 ? 27.595 -25.278 -62.791 1.00 84.19 ? 38 LYS B CB 1 ATOM 2834 C CG . LYS B 2 38 ? 26.747 -24.016 -62.911 1.00 89.11 ? 38 LYS B CG 1 ATOM 2835 C CD . LYS B 2 38 ? 25.619 -24.177 -63.923 1.00 94.47 ? 38 LYS B CD 1 ATOM 2836 C CE . LYS B 2 38 ? 24.540 -23.123 -63.738 1.00 98.42 ? 38 LYS B CE 1 ATOM 2837 N NZ . LYS B 2 38 ? 23.553 -23.513 -62.691 1.00 103.24 ? 38 LYS B NZ 1 ATOM 2838 N N . GLU B 2 39 ? 30.141 -27.177 -62.541 1.00 74.92 ? 39 GLU B N 1 ATOM 2839 C CA . GLU B 2 39 ? 30.725 -28.378 -61.944 1.00 75.71 ? 39 GLU B CA 1 ATOM 2840 C C . GLU B 2 39 ? 31.987 -28.085 -61.133 1.00 70.62 ? 39 GLU B C 1 ATOM 2841 O O . GLU B 2 39 ? 32.093 -28.493 -59.975 1.00 70.58 ? 39 GLU B O 1 ATOM 2842 C CB . GLU B 2 39 ? 31.038 -29.431 -63.015 1.00 79.95 ? 39 GLU B CB 1 ATOM 2843 C CG . GLU B 2 39 ? 31.947 -30.558 -62.524 1.00 83.02 ? 39 GLU B CG 1 ATOM 2844 C CD . GLU B 2 39 ? 31.980 -31.762 -63.450 1.00 87.28 ? 39 GLU B CD 1 ATOM 2845 O OE1 . GLU B 2 39 ? 30.899 -32.250 -63.850 1.00 91.17 ? 39 GLU B OE1 1 ATOM 2846 O OE2 . GLU B 2 39 ? 33.097 -32.226 -63.771 1.00 87.85 ? 39 GLU B OE2 1 ATOM 2847 N N . SER B 2 40 ? 32.951 -27.403 -61.743 1.00 65.79 ? 40 SER B N 1 ATOM 2848 C CA . SER B 2 40 ? 34.197 -27.108 -61.046 1.00 62.92 ? 40 SER B CA 1 ATOM 2849 C C . SER B 2 40 ? 33.973 -26.096 -59.922 1.00 60.48 ? 40 SER B C 1 ATOM 2850 O O . SER B 2 40 ? 34.592 -26.210 -58.864 1.00 58.83 ? 40 SER B O 1 ATOM 2851 C CB . SER B 2 40 ? 35.289 -26.635 -62.008 1.00 61.06 ? 40 SER B CB 1 ATOM 2852 O OG . SER B 2 40 ? 34.879 -25.494 -62.726 1.00 63.23 ? 40 SER B OG 1 ATOM 2853 N N . THR B 2 41 ? 33.083 -25.128 -60.146 1.00 58.88 ? 41 THR B N 1 ATOM 2854 C CA . THR B 2 41 ? 32.689 -24.192 -59.096 1.00 57.80 ? 41 THR B CA 1 ATOM 2855 C C . THR B 2 41 ? 32.119 -24.920 -57.881 1.00 58.66 ? 41 THR B C 1 ATOM 2856 O O . THR B 2 41 ? 32.511 -24.644 -56.756 1.00 57.89 ? 41 THR B O 1 ATOM 2857 C CB . THR B 2 41 ? 31.637 -23.168 -59.587 1.00 58.98 ? 41 THR B CB 1 ATOM 2858 O OG1 . THR B 2 41 ? 32.186 -22.369 -60.640 1.00 58.10 ? 41 THR B OG1 1 ATOM 2859 C CG2 . THR B 2 41 ? 31.208 -22.250 -58.454 1.00 59.42 ? 41 THR B CG2 1 ATOM 2860 N N . GLN B 2 42 ? 31.196 -25.847 -58.107 1.00 61.17 ? 42 GLN B N 1 ATOM 2861 C CA . GLN B 2 42 ? 30.547 -26.558 -57.005 1.00 64.32 ? 42 GLN B CA 1 ATOM 2862 C C . GLN B 2 42 ? 31.512 -27.493 -56.276 1.00 63.98 ? 42 GLN B C 1 ATOM 2863 O O . GLN B 2 42 ? 31.426 -27.632 -55.059 1.00 64.99 ? 42 GLN B O 1 ATOM 2864 C CB . GLN B 2 42 ? 29.332 -27.345 -57.504 1.00 68.05 ? 42 GLN B CB 1 ATOM 2865 C CG . GLN B 2 42 ? 28.490 -27.976 -56.402 1.00 71.83 ? 42 GLN B CG 1 ATOM 2866 C CD . GLN B 2 42 ? 27.886 -26.957 -55.445 1.00 73.76 ? 42 GLN B CD 1 ATOM 2867 O OE1 . GLN B 2 42 ? 28.044 -27.063 -54.227 1.00 74.25 ? 42 GLN B OE1 1 ATOM 2868 N NE2 . GLN B 2 42 ? 27.185 -25.968 -55.992 1.00 74.70 ? 42 GLN B NE2 1 ATOM 2869 N N . LYS B 2 43 ? 32.409 -28.147 -57.010 1.00 63.56 ? 43 LYS B N 1 ATOM 2870 C CA . LYS B 2 43 ? 33.480 -28.917 -56.373 1.00 64.26 ? 43 LYS B CA 1 ATOM 2871 C C . LYS B 2 43 ? 34.295 -28.032 -55.448 1.00 60.09 ? 43 LYS B C 1 ATOM 2872 O O . LYS B 2 43 ? 34.694 -28.461 -54.367 1.00 60.42 ? 43 LYS B O 1 ATOM 2873 C CB . LYS B 2 43 ? 34.429 -29.547 -57.396 1.00 66.69 ? 43 LYS B CB 1 ATOM 2874 C CG . LYS B 2 43 ? 33.909 -30.817 -58.056 1.00 74.04 ? 43 LYS B CG 1 ATOM 2875 C CD . LYS B 2 43 ? 35.051 -31.789 -58.348 1.00 77.83 ? 43 LYS B CD 1 ATOM 2876 C CE . LYS B 2 43 ? 34.555 -33.095 -58.952 1.00 82.94 ? 43 LYS B CE 1 ATOM 2877 N NZ . LYS B 2 43 ? 34.256 -32.944 -60.406 1.00 85.21 ? 43 LYS B NZ 1 ATOM 2878 N N . ALA B 2 44 ? 34.551 -26.799 -55.873 1.00 55.66 ? 44 ALA B N 1 ATOM 2879 C CA . ALA B 2 44 ? 35.346 -25.895 -55.069 1.00 53.25 ? 44 ALA B CA 1 ATOM 2880 C C . ALA B 2 44 ? 34.602 -25.498 -53.807 1.00 54.15 ? 44 ALA B C 1 ATOM 2881 O O . ALA B 2 44 ? 35.179 -25.488 -52.730 1.00 54.08 ? 44 ALA B O 1 ATOM 2882 C CB . ALA B 2 44 ? 35.741 -24.668 -55.869 1.00 51.75 ? 44 ALA B CB 1 ATOM 2883 N N . ILE B 2 45 ? 33.318 -25.187 -53.934 1.00 55.97 ? 45 ILE B N 1 ATOM 2884 C CA . ILE B 2 45 ? 32.520 -24.819 -52.770 1.00 57.96 ? 45 ILE B CA 1 ATOM 2885 C C . ILE B 2 45 ? 32.480 -25.950 -51.744 1.00 58.94 ? 45 ILE B C 1 ATOM 2886 O O . ILE B 2 45 ? 32.562 -25.696 -50.545 1.00 59.83 ? 45 ILE B O 1 ATOM 2887 C CB . ILE B 2 45 ? 31.086 -24.403 -53.164 1.00 61.01 ? 45 ILE B CB 1 ATOM 2888 C CG1 . ILE B 2 45 ? 31.104 -23.058 -53.902 1.00 60.21 ? 45 ILE B CG1 1 ATOM 2889 C CG2 . ILE B 2 45 ? 30.184 -24.302 -51.940 1.00 63.05 ? 45 ILE B CG2 1 ATOM 2890 C CD1 . ILE B 2 45 ? 29.831 -22.791 -54.684 1.00 62.92 ? 45 ILE B CD1 1 ATOM 2891 N N . ASP B 2 46 ? 32.368 -27.190 -52.208 1.00 59.58 ? 46 ASP B N 1 ATOM 2892 C CA . ASP B 2 46 ? 32.324 -28.344 -51.298 1.00 61.70 ? 46 ASP B CA 1 ATOM 2893 C C . ASP B 2 46 ? 33.656 -28.576 -50.579 1.00 59.00 ? 46 ASP B C 1 ATOM 2894 O O . ASP B 2 46 ? 33.685 -28.842 -49.376 1.00 60.41 ? 46 ASP B O 1 ATOM 2895 C CB . ASP B 2 46 ? 31.913 -29.614 -52.045 1.00 64.46 ? 46 ASP B CB 1 ATOM 2896 C CG . ASP B 2 46 ? 30.518 -29.515 -52.659 1.00 68.19 ? 46 ASP B CG 1 ATOM 2897 O OD1 . ASP B 2 46 ? 29.816 -28.509 -52.405 1.00 69.20 ? 46 ASP B OD1 1 ATOM 2898 O OD2 . ASP B 2 46 ? 30.131 -30.444 -53.408 1.00 70.35 ? 46 ASP B OD2 1 ATOM 2899 N N . GLY B 2 47 ? 34.758 -28.473 -51.307 1.00 55.82 ? 47 GLY B N 1 ATOM 2900 C CA . GLY B 2 47 ? 36.076 -28.664 -50.711 1.00 54.29 ? 47 GLY B CA 1 ATOM 2901 C C . GLY B 2 47 ? 36.361 -27.660 -49.608 1.00 54.06 ? 47 GLY B C 1 ATOM 2902 O O . GLY B 2 47 ? 36.758 -28.030 -48.496 1.00 54.07 ? 47 GLY B O 1 ATOM 2903 N N . VAL B 2 48 ? 36.134 -26.385 -49.913 1.00 53.31 ? 48 VAL B N 1 ATOM 2904 C CA . VAL B 2 48 ? 36.403 -25.305 -48.974 1.00 52.63 ? 48 VAL B CA 1 ATOM 2905 C C . VAL B 2 48 ? 35.470 -25.350 -47.762 1.00 54.35 ? 48 VAL B C 1 ATOM 2906 O O . VAL B 2 48 ? 35.898 -25.090 -46.644 1.00 55.39 ? 48 VAL B O 1 ATOM 2907 C CB . VAL B 2 48 ? 36.301 -23.943 -49.683 1.00 52.88 ? 48 VAL B CB 1 ATOM 2908 C CG1 . VAL B 2 48 ? 36.345 -22.799 -48.685 1.00 53.35 ? 48 VAL B CG1 1 ATOM 2909 C CG2 . VAL B 2 48 ? 37.428 -23.810 -50.711 1.00 51.28 ? 48 VAL B CG2 1 ATOM 2910 N N . THR B 2 49 ? 34.205 -25.685 -47.979 1.00 55.42 ? 49 THR B N 1 ATOM 2911 C CA . THR B 2 49 ? 33.240 -25.789 -46.889 1.00 57.68 ? 49 THR B CA 1 ATOM 2912 C C . THR B 2 49 ? 33.607 -26.908 -45.930 1.00 59.51 ? 49 THR B C 1 ATOM 2913 O O . THR B 2 49 ? 33.587 -26.727 -44.712 1.00 60.51 ? 49 THR B O 1 ATOM 2914 C CB . THR B 2 49 ? 31.836 -26.050 -47.438 1.00 59.79 ? 49 THR B CB 1 ATOM 2915 O OG1 . THR B 2 49 ? 31.499 -25.009 -48.357 1.00 58.10 ? 49 THR B OG1 1 ATOM 2916 C CG2 . THR B 2 49 ? 30.811 -26.110 -46.324 1.00 62.83 ? 49 THR B CG2 1 ATOM 2917 N N . ASN B 2 50 ? 33.944 -28.071 -46.477 1.00 60.92 ? 50 ASN B N 1 ATOM 2918 C CA . ASN B 2 50 ? 34.420 -29.179 -45.650 1.00 62.69 ? 50 ASN B CA 1 ATOM 2919 C C . ASN B 2 50 ? 35.667 -28.809 -44.865 1.00 60.68 ? 50 ASN B C 1 ATOM 2920 O O . ASN B 2 50 ? 35.794 -29.150 -43.693 1.00 61.41 ? 50 ASN B O 1 ATOM 2921 C CB . ASN B 2 50 ? 34.704 -30.407 -46.510 1.00 63.47 ? 50 ASN B CB 1 ATOM 2922 C CG . ASN B 2 50 ? 33.439 -31.070 -47.002 1.00 67.42 ? 50 ASN B CG 1 ATOM 2923 O OD1 . ASN B 2 50 ? 32.439 -31.097 -46.303 1.00 71.75 ? 50 ASN B OD1 1 ATOM 2924 N ND2 . ASN B 2 50 ? 33.478 -31.603 -48.211 1.00 68.14 ? 50 ASN B ND2 1 ATOM 2925 N N . LYS B 2 51 ? 36.585 -28.109 -45.523 1.00 58.91 ? 51 LYS B N 1 ATOM 2926 C CA . LYS B 2 51 ? 37.825 -27.680 -44.891 1.00 57.56 ? 51 LYS B CA 1 ATOM 2927 C C . LYS B 2 51 ? 37.536 -26.828 -43.659 1.00 58.60 ? 51 LYS B C 1 ATOM 2928 O O . LYS B 2 51 ? 38.060 -27.087 -42.579 1.00 58.89 ? 51 LYS B O 1 ATOM 2929 C CB . LYS B 2 51 ? 38.680 -26.892 -45.883 1.00 55.57 ? 51 LYS B CB 1 ATOM 2930 C CG . LYS B 2 51 ? 39.863 -26.185 -45.249 1.00 55.03 ? 51 LYS B CG 1 ATOM 2931 C CD . LYS B 2 51 ? 40.683 -25.455 -46.288 1.00 54.82 ? 51 LYS B CD 1 ATOM 2932 C CE . LYS B 2 51 ? 41.350 -26.427 -47.238 1.00 55.01 ? 51 LYS B CE 1 ATOM 2933 N NZ . LYS B 2 51 ? 42.556 -25.816 -47.858 1.00 55.11 ? 51 LYS B NZ 1 ATOM 2934 N N . VAL B 2 52 ? 36.699 -25.814 -43.827 1.00 58.63 ? 52 VAL B N 1 ATOM 2935 C CA . VAL B 2 52 ? 36.389 -24.926 -42.726 1.00 60.34 ? 52 VAL B CA 1 ATOM 2936 C C . VAL B 2 52 ? 35.796 -25.728 -41.561 1.00 63.16 ? 52 VAL B C 1 ATOM 2937 O O . VAL B 2 52 ? 36.236 -25.579 -40.412 1.00 63.85 ? 52 VAL B O 1 ATOM 2938 C CB . VAL B 2 52 ? 35.419 -23.805 -43.150 1.00 61.52 ? 52 VAL B CB 1 ATOM 2939 C CG1 . VAL B 2 52 ? 34.969 -23.002 -41.937 1.00 63.87 ? 52 VAL B CG1 1 ATOM 2940 C CG2 . VAL B 2 52 ? 36.076 -22.890 -44.169 1.00 59.66 ? 52 VAL B CG2 1 ATOM 2941 N N . ASN B 2 53 ? 34.817 -26.582 -41.856 1.00 64.69 ? 53 ASN B N 1 ATOM 2942 C CA . ASN B 2 53 ? 34.187 -27.391 -40.812 1.00 68.37 ? 53 ASN B CA 1 ATOM 2943 C C . ASN B 2 53 ? 35.176 -28.368 -40.178 1.00 67.89 ? 53 ASN B C 1 ATOM 2944 O O . ASN B 2 53 ? 35.083 -28.658 -38.991 1.00 69.47 ? 53 ASN B O 1 ATOM 2945 C CB . ASN B 2 53 ? 32.973 -28.148 -41.355 1.00 71.46 ? 53 ASN B CB 1 ATOM 2946 C CG . ASN B 2 53 ? 31.890 -27.224 -41.881 1.00 73.45 ? 53 ASN B CG 1 ATOM 2947 O OD1 . ASN B 2 53 ? 31.789 -26.073 -41.467 1.00 74.76 ? 53 ASN B OD1 1 ATOM 2948 N ND2 . ASN B 2 53 ? 31.076 -27.725 -42.805 1.00 74.95 ? 53 ASN B ND2 1 ATOM 2949 N N . SER B 2 54 ? 36.125 -28.870 -40.965 1.00 66.29 ? 54 SER B N 1 ATOM 2950 C CA . SER B 2 54 ? 37.160 -29.753 -40.430 1.00 67.03 ? 54 SER B CA 1 ATOM 2951 C C . SER B 2 54 ? 38.049 -28.999 -39.457 1.00 67.26 ? 54 SER B C 1 ATOM 2952 O O . SER B 2 54 ? 38.355 -29.502 -38.382 1.00 68.69 ? 54 SER B O 1 ATOM 2953 C CB . SER B 2 54 ? 38.014 -30.373 -41.543 1.00 65.02 ? 54 SER B CB 1 ATOM 2954 O OG . SER B 2 54 ? 37.377 -31.508 -42.090 1.00 66.82 ? 54 SER B OG 1 ATOM 2955 N N . ILE B 2 55 ? 38.454 -27.791 -39.847 1.00 67.59 ? 55 ILE B N 1 ATOM 2956 C CA . ILE B 2 55 ? 39.269 -26.923 -39.001 1.00 68.71 ? 55 ILE B CA 1 ATOM 2957 C C . ILE B 2 55 ? 38.542 -26.581 -37.696 1.00 72.20 ? 55 ILE B C 1 ATOM 2958 O O . ILE B 2 55 ? 39.114 -26.705 -36.614 1.00 72.98 ? 55 ILE B O 1 ATOM 2959 C CB . ILE B 2 55 ? 39.681 -25.642 -39.764 1.00 69.02 ? 55 ILE B CB 1 ATOM 2960 C CG1 . ILE B 2 55 ? 40.734 -26.001 -40.821 1.00 67.25 ? 55 ILE B CG1 1 ATOM 2961 C CG2 . ILE B 2 55 ? 40.223 -24.575 -38.814 1.00 69.79 ? 55 ILE B CG2 1 ATOM 2962 C CD1 . ILE B 2 55 ? 41.103 -24.871 -41.754 1.00 65.85 ? 55 ILE B CD1 1 ATOM 2963 N N . ILE B 2 56 ? 37.284 -26.167 -37.799 1.00 74.77 ? 56 ILE B N 1 ATOM 2964 C CA . ILE B 2 56 ? 36.484 -25.867 -36.617 1.00 78.14 ? 56 ILE B CA 1 ATOM 2965 C C . ILE B 2 56 ? 36.417 -27.073 -35.668 1.00 82.66 ? 56 ILE B C 1 ATOM 2966 O O . ILE B 2 56 ? 36.676 -26.940 -34.471 1.00 84.38 ? 56 ILE B O 1 ATOM 2967 C CB . ILE B 2 56 ? 35.058 -25.432 -37.011 1.00 79.88 ? 56 ILE B CB 1 ATOM 2968 C CG1 . ILE B 2 56 ? 35.098 -24.057 -37.684 1.00 78.95 ? 56 ILE B CG1 1 ATOM 2969 C CG2 . ILE B 2 56 ? 34.137 -25.393 -35.795 1.00 83.50 ? 56 ILE B CG2 1 ATOM 2970 C CD1 . ILE B 2 56 ? 33.809 -23.665 -38.377 1.00 80.75 ? 56 ILE B CD1 1 ATOM 2971 N N . ASP B 2 57 ? 36.083 -28.245 -36.206 1.00 85.83 ? 57 ASP B N 1 ATOM 2972 C CA . ASP B 2 57 ? 35.807 -29.424 -35.374 1.00 90.42 ? 57 ASP B CA 1 ATOM 2973 C C . ASP B 2 57 ? 37.052 -30.062 -34.763 1.00 88.52 ? 57 ASP B C 1 ATOM 2974 O O . ASP B 2 57 ? 36.969 -30.685 -33.714 1.00 90.22 ? 57 ASP B O 1 ATOM 2975 C CB . ASP B 2 57 ? 35.000 -30.470 -36.156 1.00 94.62 ? 57 ASP B CB 1 ATOM 2976 C CG . ASP B 2 57 ? 33.511 -30.131 -36.215 1.00 101.03 ? 57 ASP B CG 1 ATOM 2977 O OD1 . ASP B 2 57 ? 32.867 -30.095 -35.137 1.00 105.14 ? 57 ASP B OD1 1 ATOM 2978 O OD2 . ASP B 2 57 ? 32.986 -29.900 -37.333 1.00 101.81 ? 57 ASP B OD2 1 ATOM 2979 N N . LYS B 2 58 ? 38.201 -29.915 -35.411 1.00 86.03 ? 58 LYS B N 1 ATOM 2980 C CA . LYS B 2 58 ? 39.452 -30.409 -34.837 1.00 85.28 ? 58 LYS B CA 1 ATOM 2981 C C . LYS B 2 58 ? 39.877 -29.594 -33.623 1.00 87.62 ? 58 LYS B C 1 ATOM 2982 O O . LYS B 2 58 ? 40.463 -30.139 -32.693 1.00 87.77 ? 58 LYS B O 1 ATOM 2983 C CB . LYS B 2 58 ? 40.570 -30.458 -35.893 1.00 81.87 ? 58 LYS B CB 1 ATOM 2984 C CG . LYS B 2 58 ? 41.005 -31.863 -36.307 1.00 81.94 ? 58 LYS B CG 1 ATOM 2985 C CD . LYS B 2 58 ? 39.937 -32.925 -36.070 1.00 84.75 ? 58 LYS B CD 1 ATOM 2986 C CE . LYS B 2 58 ? 40.239 -34.201 -36.823 1.00 85.26 ? 58 LYS B CE 1 ATOM 2987 N NZ . LYS B 2 58 ? 39.420 -35.333 -36.316 1.00 89.04 ? 58 LYS B NZ 1 ATOM 2988 N N . MET B 2 59 ? 39.549 -28.304 -33.621 1.00 90.25 ? 59 MET B N 1 ATOM 2989 C CA . MET B 2 59 ? 39.832 -27.423 -32.487 1.00 93.14 ? 59 MET B CA 1 ATOM 2990 C C . MET B 2 59 ? 38.678 -27.432 -31.474 1.00 100.26 ? 59 MET B C 1 ATOM 2991 O O . MET B 2 59 ? 38.630 -26.592 -30.576 1.00 102.14 ? 59 MET B O 1 ATOM 2992 C CB . MET B 2 59 ? 40.076 -25.995 -32.981 1.00 91.53 ? 59 MET B CB 1 ATOM 2993 C CG . MET B 2 59 ? 41.103 -25.866 -34.100 1.00 88.81 ? 59 MET B CG 1 ATOM 2994 S SD . MET B 2 59 ? 42.839 -25.998 -33.624 1.00 87.95 ? 59 MET B SD 1 ATOM 2995 C CE . MET B 2 59 ? 43.009 -24.854 -32.258 1.00 90.66 ? 59 MET B CE 1 ATOM 2996 N N . ASN B 2 60 ? 37.756 -28.383 -31.623 1.00 106.30 ? 60 ASN B N 1 ATOM 2997 C CA . ASN B 2 60 ? 36.587 -28.510 -30.751 1.00 112.41 ? 60 ASN B CA 1 ATOM 2998 C C . ASN B 2 60 ? 36.981 -28.942 -29.340 1.00 114.86 ? 60 ASN B C 1 ATOM 2999 O O . ASN B 2 60 ? 36.649 -28.272 -28.364 1.00 114.40 ? 60 ASN B O 1 ATOM 3000 C CB . ASN B 2 60 ? 35.607 -29.523 -31.355 1.00 115.19 ? 60 ASN B CB 1 ATOM 3001 C CG . ASN B 2 60 ? 34.255 -29.509 -30.682 1.00 120.38 ? 60 ASN B CG 1 ATOM 3002 O OD1 . ASN B 2 60 ? 33.951 -30.373 -29.859 1.00 122.45 ? 60 ASN B OD1 1 ATOM 3003 N ND2 . ASN B 2 60 ? 33.428 -28.532 -31.037 1.00 122.28 ? 60 ASN B ND2 1 ATOM 3004 N N . THR B 2 61 ? 37.679 -30.069 -29.241 1.00 113.94 ? 61 THR B N 1 ATOM 3005 C CA . THR B 2 61 ? 38.251 -30.507 -27.979 1.00 111.72 ? 61 THR B CA 1 ATOM 3006 C C . THR B 2 61 ? 39.574 -29.779 -27.845 1.00 108.98 ? 61 THR B C 1 ATOM 3007 O O . THR B 2 61 ? 40.468 -29.950 -28.672 1.00 111.07 ? 61 THR B O 1 ATOM 3008 C CB . THR B 2 61 ? 38.493 -32.028 -27.929 1.00 115.30 ? 61 THR B CB 1 ATOM 3009 O OG1 . THR B 2 61 ? 37.317 -32.727 -28.355 1.00 121.77 ? 61 THR B OG1 1 ATOM 3010 C CG2 . THR B 2 61 ? 38.849 -32.465 -26.511 1.00 114.25 ? 61 THR B CG2 1 ATOM 3011 N N . GLN B 2 62 ? 39.681 -28.959 -26.806 1.00 106.69 ? 62 GLN B N 1 ATOM 3012 C CA . GLN B 2 62 ? 40.855 -28.127 -26.576 1.00 103.51 ? 62 GLN B CA 1 ATOM 3013 C C . GLN B 2 62 ? 40.856 -27.639 -25.123 1.00 101.98 ? 62 GLN B C 1 ATOM 3014 O O . GLN B 2 62 ? 39.795 -27.521 -24.499 1.00 107.62 ? 62 GLN B O 1 ATOM 3015 C CB . GLN B 2 62 ? 40.863 -26.951 -27.561 1.00 104.29 ? 62 GLN B CB 1 ATOM 3016 C CG . GLN B 2 62 ? 41.644 -25.725 -27.105 1.00 102.63 ? 62 GLN B CG 1 ATOM 3017 C CD . GLN B 2 62 ? 41.651 -24.614 -28.134 1.00 106.51 ? 62 GLN B CD 1 ATOM 3018 O OE1 . GLN B 2 62 ? 41.222 -24.799 -29.274 1.00 110.29 ? 62 GLN B OE1 1 ATOM 3019 N NE2 . GLN B 2 62 ? 42.132 -23.443 -27.733 1.00 106.23 ? 62 GLN B NE2 1 ATOM 3020 N N . PHE B 2 63 ? 42.046 -27.349 -24.604 1.00 95.36 ? 63 PHE B N 1 ATOM 3021 C CA . PHE B 2 63 ? 42.232 -27.011 -23.192 1.00 94.03 ? 63 PHE B CA 1 ATOM 3022 C C . PHE B 2 63 ? 41.302 -25.901 -22.678 1.00 94.94 ? 63 PHE B C 1 ATOM 3023 O O . PHE B 2 63 ? 41.017 -24.934 -23.389 1.00 100.01 ? 63 PHE B O 1 ATOM 3024 C CB . PHE B 2 63 ? 43.692 -26.623 -22.933 1.00 89.65 ? 63 PHE B CB 1 ATOM 3025 C CG . PHE B 2 63 ? 44.004 -26.412 -21.485 1.00 86.79 ? 63 PHE B CG 1 ATOM 3026 C CD1 . PHE B 2 63 ? 44.113 -27.499 -20.623 1.00 83.66 ? 63 PHE B CD1 1 ATOM 3027 C CD2 . PHE B 2 63 ? 44.171 -25.127 -20.973 1.00 88.64 ? 63 PHE B CD2 1 ATOM 3028 C CE1 . PHE B 2 63 ? 44.389 -27.310 -19.281 1.00 82.33 ? 63 PHE B CE1 1 ATOM 3029 C CE2 . PHE B 2 63 ? 44.449 -24.931 -19.626 1.00 84.57 ? 63 PHE B CE2 1 ATOM 3030 C CZ . PHE B 2 63 ? 44.556 -26.025 -18.782 1.00 82.00 ? 63 PHE B CZ 1 ATOM 3031 N N . GLU B 2 64 ? 40.828 -26.068 -21.442 1.00 91.26 ? 64 GLU B N 1 ATOM 3032 C CA . GLU B 2 64 ? 40.001 -25.070 -20.768 1.00 92.80 ? 64 GLU B CA 1 ATOM 3033 C C . GLU B 2 64 ? 40.586 -24.743 -19.398 1.00 90.27 ? 64 GLU B C 1 ATOM 3034 O O . GLU B 2 64 ? 40.850 -25.640 -18.597 1.00 89.93 ? 64 GLU B O 1 ATOM 3035 C CB . GLU B 2 64 ? 38.575 -25.585 -20.588 1.00 96.22 ? 64 GLU B CB 1 ATOM 3036 C CG . GLU B 2 64 ? 37.824 -25.828 -21.888 1.00 99.99 ? 64 GLU B CG 1 ATOM 3037 C CD . GLU B 2 64 ? 36.366 -26.188 -21.663 1.00 104.11 ? 64 GLU B CD 1 ATOM 3038 O OE1 . GLU B 2 64 ? 35.870 -26.018 -20.528 1.00 102.57 ? 64 GLU B OE1 1 ATOM 3039 O OE2 . GLU B 2 64 ? 35.713 -26.641 -22.625 1.00 107.93 ? 64 GLU B OE2 1 ATOM 3040 N N . ALA B 2 65 ? 40.777 -23.456 -19.128 1.00 91.91 ? 65 ALA B N 1 ATOM 3041 C CA . ALA B 2 65 ? 41.334 -23.007 -17.851 1.00 90.47 ? 65 ALA B CA 1 ATOM 3042 C C . ALA B 2 65 ? 40.273 -23.012 -16.749 1.00 93.16 ? 65 ALA B C 1 ATOM 3043 O O . ALA B 2 65 ? 39.092 -22.775 -17.013 1.00 92.98 ? 65 ALA B O 1 ATOM 3044 C CB . ALA B 2 65 ? 41.937 -21.618 -18.001 1.00 90.70 ? 65 ALA B CB 1 ATOM 3045 N N . VAL B 2 66 ? 40.705 -23.290 -15.518 1.00 93.12 ? 66 VAL B N 1 ATOM 3046 C CA . VAL B 2 66 ? 39.826 -23.237 -14.347 1.00 96.74 ? 66 VAL B CA 1 ATOM 3047 C C . VAL B 2 66 ? 40.482 -22.393 -13.258 1.00 95.99 ? 66 VAL B C 1 ATOM 3048 O O . VAL B 2 66 ? 41.702 -22.408 -13.108 1.00 95.54 ? 66 VAL B O 1 ATOM 3049 C CB . VAL B 2 66 ? 39.524 -24.648 -13.795 1.00 97.17 ? 66 VAL B CB 1 ATOM 3050 C CG1 . VAL B 2 66 ? 38.580 -24.576 -12.596 1.00 101.39 ? 66 VAL B CG1 1 ATOM 3051 C CG2 . VAL B 2 66 ? 38.942 -25.533 -14.889 1.00 100.71 ? 66 VAL B CG2 1 ATOM 3052 N N . GLY B 2 67 ? 39.664 -21.661 -12.505 1.00 100.20 ? 67 GLY B N 1 ATOM 3053 C CA . GLY B 2 67 ? 40.148 -20.852 -11.388 1.00 98.21 ? 67 GLY B CA 1 ATOM 3054 C C . GLY B 2 67 ? 40.580 -21.709 -10.209 1.00 93.89 ? 67 GLY B C 1 ATOM 3055 O O . GLY B 2 67 ? 39.835 -22.583 -9.760 1.00 94.49 ? 67 GLY B O 1 ATOM 3056 N N . ARG B 2 68 ? 41.795 -21.468 -9.724 1.00 88.01 ? 68 ARG B N 1 ATOM 3057 C CA . ARG B 2 68 ? 42.330 -22.174 -8.563 1.00 84.15 ? 68 ARG B CA 1 ATOM 3058 C C . ARG B 2 68 ? 43.159 -21.196 -7.744 1.00 82.59 ? 68 ARG B C 1 ATOM 3059 O O . ARG B 2 68 ? 43.986 -20.466 -8.290 1.00 81.58 ? 68 ARG B O 1 ATOM 3060 C CB . ARG B 2 68 ? 43.175 -23.376 -8.998 1.00 81.85 ? 68 ARG B CB 1 ATOM 3061 C CG . ARG B 2 68 ? 42.341 -24.527 -9.548 1.00 84.97 ? 68 ARG B CG 1 ATOM 3062 C CD . ARG B 2 68 ? 43.128 -25.822 -9.713 1.00 80.89 ? 68 ARG B CD 1 ATOM 3063 N NE . ARG B 2 68 ? 44.049 -25.754 -10.837 1.00 79.17 ? 68 ARG B NE 1 ATOM 3064 C CZ . ARG B 2 68 ? 43.706 -25.848 -12.123 1.00 78.85 ? 68 ARG B CZ 1 ATOM 3065 N NH1 . ARG B 2 68 ? 42.451 -26.028 -12.498 1.00 80.72 ? 68 ARG B NH1 1 ATOM 3066 N NH2 . ARG B 2 68 ? 44.641 -25.753 -13.056 1.00 79.12 ? 68 ARG B NH2 1 ATOM 3067 N N . GLU B 2 69 ? 42.924 -21.176 -6.434 1.00 84.00 ? 69 GLU B N 1 ATOM 3068 C CA . GLU B 2 69 ? 43.567 -20.211 -5.546 1.00 80.09 ? 69 GLU B CA 1 ATOM 3069 C C . GLU B 2 69 ? 44.490 -20.891 -4.567 1.00 72.77 ? 69 GLU B C 1 ATOM 3070 O O . GLU B 2 69 ? 44.268 -22.036 -4.189 1.00 68.17 ? 69 GLU B O 1 ATOM 3071 C CB . GLU B 2 69 ? 42.518 -19.399 -4.801 1.00 86.56 ? 69 GLU B CB 1 ATOM 3072 C CG . GLU B 2 69 ? 41.940 -18.284 -5.647 1.00 91.65 ? 69 GLU B CG 1 ATOM 3073 C CD . GLU B 2 69 ? 40.548 -17.895 -5.216 1.00 99.24 ? 69 GLU B CD 1 ATOM 3074 O OE1 . GLU B 2 69 ? 39.586 -18.606 -5.589 1.00 101.67 ? 69 GLU B OE1 1 ATOM 3075 O OE2 . GLU B 2 69 ? 40.419 -16.883 -4.495 1.00 104.78 ? 69 GLU B OE2 1 ATOM 3076 N N . PHE B 2 70 ? 45.529 -20.160 -4.170 1.00 72.20 ? 70 PHE B N 1 ATOM 3077 C CA . PHE B 2 70 ? 46.593 -20.676 -3.312 1.00 70.42 ? 70 PHE B CA 1 ATOM 3078 C C . PHE B 2 70 ? 47.033 -19.618 -2.309 1.00 71.36 ? 70 PHE B C 1 ATOM 3079 O O . PHE B 2 70 ? 47.041 -18.431 -2.619 1.00 69.39 ? 70 PHE B O 1 ATOM 3080 C CB . PHE B 2 70 ? 47.786 -21.088 -4.167 1.00 67.07 ? 70 PHE B CB 1 ATOM 3081 C CG . PHE B 2 70 ? 47.432 -22.023 -5.283 1.00 65.65 ? 70 PHE B CG 1 ATOM 3082 C CD1 . PHE B 2 70 ? 47.029 -21.529 -6.521 1.00 66.23 ? 70 PHE B CD1 1 ATOM 3083 C CD2 . PHE B 2 70 ? 47.491 -23.397 -5.097 1.00 64.55 ? 70 PHE B CD2 1 ATOM 3084 C CE1 . PHE B 2 70 ? 46.693 -22.390 -7.550 1.00 65.12 ? 70 PHE B CE1 1 ATOM 3085 C CE2 . PHE B 2 70 ? 47.162 -24.264 -6.125 1.00 64.40 ? 70 PHE B CE2 1 ATOM 3086 C CZ . PHE B 2 70 ? 46.763 -23.762 -7.351 1.00 64.63 ? 70 PHE B CZ 1 ATOM 3087 N N . ASN B 2 71 ? 47.399 -20.045 -1.105 1.00 73.06 ? 71 ASN B N 1 ATOM 3088 C CA . ASN B 2 71 ? 47.789 -19.092 -0.068 1.00 76.90 ? 71 ASN B CA 1 ATOM 3089 C C . ASN B 2 71 ? 49.252 -18.668 -0.224 1.00 76.08 ? 71 ASN B C 1 ATOM 3090 O O . ASN B 2 71 ? 49.924 -19.063 -1.185 1.00 72.43 ? 71 ASN B O 1 ATOM 3091 C CB . ASN B 2 71 ? 47.462 -19.618 1.344 1.00 79.94 ? 71 ASN B CB 1 ATOM 3092 C CG . ASN B 2 71 ? 48.387 -20.730 1.800 1.00 78.87 ? 71 ASN B CG 1 ATOM 3093 O OD1 . ASN B 2 71 ? 49.608 -20.575 1.809 1.00 77.44 ? 71 ASN B OD1 1 ATOM 3094 N ND2 . ASN B 2 71 ? 47.804 -21.857 2.201 1.00 81.47 ? 71 ASN B ND2 1 ATOM 3095 N N . ASN B 2 72 ? 49.732 -17.862 0.720 1.00 79.01 ? 72 ASN B N 1 ATOM 3096 C CA . ASN B 2 72 ? 51.038 -17.223 0.605 1.00 79.78 ? 72 ASN B CA 1 ATOM 3097 C C . ASN B 2 72 ? 52.241 -18.170 0.731 1.00 76.06 ? 72 ASN B C 1 ATOM 3098 O O . ASN B 2 72 ? 53.348 -17.808 0.331 1.00 75.88 ? 72 ASN B O 1 ATOM 3099 C CB . ASN B 2 72 ? 51.152 -16.091 1.633 1.00 85.71 ? 72 ASN B CB 1 ATOM 3100 C CG . ASN B 2 72 ? 52.347 -15.194 1.381 1.00 88.71 ? 72 ASN B CG 1 ATOM 3101 O OD1 . ASN B 2 72 ? 52.684 -14.901 0.236 1.00 92.08 ? 72 ASN B OD1 1 ATOM 3102 N ND2 . ASN B 2 72 ? 52.999 -14.758 2.452 1.00 93.12 ? 72 ASN B ND2 1 ATOM 3103 N N . LEU B 2 73 ? 52.033 -19.359 1.296 1.00 73.45 ? 73 LEU B N 1 ATOM 3104 C CA . LEU B 2 73 ? 53.084 -20.378 1.375 1.00 72.30 ? 73 LEU B CA 1 ATOM 3105 C C . LEU B 2 73 ? 52.769 -21.589 0.479 1.00 71.05 ? 73 LEU B C 1 ATOM 3106 O O . LEU B 2 73 ? 53.154 -22.724 0.779 1.00 71.21 ? 73 LEU B O 1 ATOM 3107 C CB . LEU B 2 73 ? 53.291 -20.814 2.824 1.00 76.00 ? 73 LEU B CB 1 ATOM 3108 C CG . LEU B 2 73 ? 53.900 -19.772 3.776 1.00 79.73 ? 73 LEU B CG 1 ATOM 3109 C CD1 . LEU B 2 73 ? 53.820 -20.252 5.219 1.00 80.37 ? 73 LEU B CD1 1 ATOM 3110 C CD2 . LEU B 2 73 ? 55.342 -19.452 3.393 1.00 78.65 ? 73 LEU B CD2 1 ATOM 3111 N N . GLU B 2 74 ? 52.064 -21.331 -0.621 1.00 68.50 ? 74 GLU B N 1 ATOM 3112 C CA . GLU B 2 74 ? 51.866 -22.314 -1.679 1.00 65.59 ? 74 GLU B CA 1 ATOM 3113 C C . GLU B 2 74 ? 52.300 -21.685 -3.001 1.00 64.84 ? 74 GLU B C 1 ATOM 3114 O O . GLU B 2 74 ? 51.672 -21.897 -4.038 1.00 60.02 ? 74 GLU B O 1 ATOM 3115 C CB . GLU B 2 74 ? 50.403 -22.736 -1.740 1.00 65.38 ? 74 GLU B CB 1 ATOM 3116 C CG . GLU B 2 74 ? 49.937 -23.516 -0.523 1.00 66.47 ? 74 GLU B CG 1 ATOM 3117 C CD . GLU B 2 74 ? 48.446 -23.792 -0.553 1.00 69.35 ? 74 GLU B CD 1 ATOM 3118 O OE1 . GLU B 2 74 ? 47.677 -22.869 -0.895 1.00 71.71 ? 74 GLU B OE1 1 ATOM 3119 O OE2 . GLU B 2 74 ? 48.037 -24.928 -0.237 1.00 70.71 ? 74 GLU B OE2 1 ATOM 3120 N N . ARG B 2 75 ? 53.373 -20.895 -2.941 1.00 67.22 ? 75 ARG B N 1 ATOM 3121 C CA . ARG B 2 75 ? 53.845 -20.119 -4.083 1.00 66.38 ? 75 ARG B CA 1 ATOM 3122 C C . ARG B 2 75 ? 54.351 -21.019 -5.201 1.00 64.34 ? 75 ARG B C 1 ATOM 3123 O O . ARG B 2 75 ? 54.158 -20.719 -6.374 1.00 65.69 ? 75 ARG B O 1 ATOM 3124 C CB . ARG B 2 75 ? 54.948 -19.130 -3.654 1.00 73.81 ? 75 ARG B CB 1 ATOM 3125 C CG . ARG B 2 75 ? 54.576 -17.646 -3.561 1.00 80.34 ? 75 ARG B CG 1 ATOM 3126 C CD . ARG B 2 75 ? 53.086 -17.379 -3.403 1.00 86.93 ? 75 ARG B CD 1 ATOM 3127 N NE . ARG B 2 75 ? 52.797 -15.977 -3.096 1.00 99.15 ? 75 ARG B NE 1 ATOM 3128 C CZ . ARG B 2 75 ? 51.582 -15.422 -3.130 1.00 106.72 ? 75 ARG B CZ 1 ATOM 3129 N NH1 . ARG B 2 75 ? 50.510 -16.141 -3.470 1.00 107.52 ? 75 ARG B NH1 1 ATOM 3130 N NH2 . ARG B 2 75 ? 51.436 -14.135 -2.822 1.00 109.86 ? 75 ARG B NH2 1 ATOM 3131 N N . ARG B 2 76 ? 54.991 -22.125 -4.846 1.00 64.67 ? 76 ARG B N 1 ATOM 3132 C CA . ARG B 2 76 ? 55.512 -23.048 -5.853 1.00 61.83 ? 76 ARG B CA 1 ATOM 3133 C C . ARG B 2 76 ? 54.399 -23.663 -6.704 1.00 60.70 ? 76 ARG B C 1 ATOM 3134 O O . ARG B 2 76 ? 54.443 -23.575 -7.930 1.00 59.11 ? 76 ARG B O 1 ATOM 3135 C CB . ARG B 2 76 ? 56.332 -24.147 -5.194 1.00 62.44 ? 76 ARG B CB 1 ATOM 3136 C CG . ARG B 2 76 ? 57.640 -23.663 -4.600 1.00 63.95 ? 76 ARG B CG 1 ATOM 3137 C CD . ARG B 2 76 ? 58.276 -24.770 -3.776 1.00 66.71 ? 76 ARG B CD 1 ATOM 3138 N NE . ARG B 2 76 ? 57.413 -25.135 -2.649 1.00 66.23 ? 76 ARG B NE 1 ATOM 3139 C CZ . ARG B 2 76 ? 57.421 -26.307 -2.019 1.00 66.07 ? 76 ARG B CZ 1 ATOM 3140 N NH1 . ARG B 2 76 ? 58.248 -27.278 -2.390 1.00 69.02 ? 76 ARG B NH1 1 ATOM 3141 N NH2 . ARG B 2 76 ? 56.580 -26.511 -1.015 1.00 65.11 ? 76 ARG B NH2 1 ATOM 3142 N N . ILE B 2 77 ? 53.404 -24.276 -6.061 1.00 61.01 ? 77 ILE B N 1 ATOM 3143 C CA . ILE B 2 77 ? 52.301 -24.884 -6.804 1.00 62.77 ? 77 ILE B CA 1 ATOM 3144 C C . ILE B 2 77 ? 51.424 -23.852 -7.518 1.00 63.18 ? 77 ILE B C 1 ATOM 3145 O O . ILE B 2 77 ? 50.881 -24.132 -8.584 1.00 61.75 ? 77 ILE B O 1 ATOM 3146 C CB . ILE B 2 77 ? 51.423 -25.809 -5.944 1.00 65.90 ? 77 ILE B CB 1 ATOM 3147 C CG1 . ILE B 2 77 ? 50.704 -25.034 -4.843 1.00 72.35 ? 77 ILE B CG1 1 ATOM 3148 C CG2 . ILE B 2 77 ? 52.256 -26.942 -5.367 1.00 68.17 ? 77 ILE B CG2 1 ATOM 3149 C CD1 . ILE B 2 77 ? 49.779 -25.907 -4.015 1.00 77.96 ? 77 ILE B CD1 1 ATOM 3150 N N . GLU B 2 78 ? 51.287 -22.664 -6.947 1.00 62.62 ? 78 GLU B N 1 ATOM 3151 C CA . GLU B 2 78 ? 50.591 -21.598 -7.644 1.00 62.56 ? 78 GLU B CA 1 ATOM 3152 C C . GLU B 2 78 ? 51.294 -21.333 -8.975 1.00 60.44 ? 78 GLU B C 1 ATOM 3153 O O . GLU B 2 78 ? 50.644 -21.177 -10.010 1.00 59.26 ? 78 GLU B O 1 ATOM 3154 C CB . GLU B 2 78 ? 50.551 -20.324 -6.802 1.00 67.03 ? 78 GLU B CB 1 ATOM 3155 C CG . GLU B 2 78 ? 49.899 -19.132 -7.488 1.00 72.61 ? 78 GLU B CG 1 ATOM 3156 C CD . GLU B 2 78 ? 49.901 -17.885 -6.621 1.00 83.46 ? 78 GLU B CD 1 ATOM 3157 O OE1 . GLU B 2 78 ? 50.947 -17.575 -6.010 1.00 88.44 ? 78 GLU B OE1 1 ATOM 3158 O OE2 . GLU B 2 78 ? 48.854 -17.206 -6.551 1.00 93.19 ? 78 GLU B OE2 1 ATOM 3159 N N . ASN B 2 79 ? 52.619 -21.297 -8.940 1.00 57.43 ? 79 ASN B N 1 ATOM 3160 C CA . ASN B 2 79 ? 53.406 -20.983 -10.115 1.00 60.66 ? 79 ASN B CA 1 ATOM 3161 C C . ASN B 2 79 ? 53.342 -22.134 -11.111 1.00 59.81 ? 79 ASN B C 1 ATOM 3162 O O . ASN B 2 79 ? 53.265 -21.919 -12.316 1.00 59.09 ? 79 ASN B O 1 ATOM 3163 C CB . ASN B 2 79 ? 54.848 -20.691 -9.704 1.00 66.04 ? 79 ASN B CB 1 ATOM 3164 C CG . ASN B 2 79 ? 55.749 -20.405 -10.885 1.00 70.77 ? 79 ASN B CG 1 ATOM 3165 O OD1 . ASN B 2 79 ? 55.710 -19.329 -11.470 1.00 77.25 ? 79 ASN B OD1 1 ATOM 3166 N ND2 . ASN B 2 79 ? 56.573 -21.369 -11.231 1.00 73.84 ? 79 ASN B ND2 1 ATOM 3167 N N . LEU B 2 80 ? 53.356 -23.356 -10.591 1.00 60.13 ? 80 LEU B N 1 ATOM 3168 C CA . LEU B 2 80 ? 53.224 -24.553 -11.412 1.00 59.92 ? 80 LEU B CA 1 ATOM 3169 C C . LEU B 2 80 ? 51.916 -24.474 -12.174 1.00 58.15 ? 80 LEU B C 1 ATOM 3170 O O . LEU B 2 80 ? 51.881 -24.665 -13.381 1.00 60.16 ? 80 LEU B O 1 ATOM 3171 C CB . LEU B 2 80 ? 53.262 -25.801 -10.523 1.00 61.85 ? 80 LEU B CB 1 ATOM 3172 C CG . LEU B 2 80 ? 53.430 -27.181 -11.159 1.00 64.63 ? 80 LEU B CG 1 ATOM 3173 C CD1 . LEU B 2 80 ? 53.708 -28.227 -10.091 1.00 66.22 ? 80 LEU B CD1 1 ATOM 3174 C CD2 . LEU B 2 80 ? 52.203 -27.580 -11.960 1.00 68.85 ? 80 LEU B CD2 1 ATOM 3175 N N . ASN B 2 81 ? 50.846 -24.162 -11.450 1.00 59.99 ? 81 ASN B N 1 ATOM 3176 C CA . ASN B 2 81 ? 49.510 -23.998 -12.022 1.00 57.85 ? 81 ASN B CA 1 ATOM 3177 C C . ASN B 2 81 ? 49.473 -22.947 -13.118 1.00 60.40 ? 81 ASN B C 1 ATOM 3178 O O . ASN B 2 81 ? 48.802 -23.121 -14.125 1.00 59.08 ? 81 ASN B O 1 ATOM 3179 C CB . ASN B 2 81 ? 48.527 -23.600 -10.928 1.00 57.80 ? 81 ASN B CB 1 ATOM 3180 C CG . ASN B 2 81 ? 47.112 -23.473 -11.437 1.00 59.61 ? 81 ASN B CG 1 ATOM 3181 O OD1 . ASN B 2 81 ? 46.525 -24.450 -11.872 1.00 61.87 ? 81 ASN B OD1 1 ATOM 3182 N ND2 . ASN B 2 81 ? 46.553 -22.271 -11.370 1.00 60.23 ? 81 ASN B ND2 1 ATOM 3183 N N . LYS B 2 82 ? 50.197 -21.853 -12.908 1.00 62.97 ? 82 LYS B N 1 ATOM 3184 C CA . LYS B 2 82 ? 50.222 -20.765 -13.863 1.00 67.27 ? 82 LYS B CA 1 ATOM 3185 C C . LYS B 2 82 ? 50.961 -21.190 -15.122 1.00 67.34 ? 82 LYS B C 1 ATOM 3186 O O . LYS B 2 82 ? 50.475 -20.959 -16.223 1.00 64.67 ? 82 LYS B O 1 ATOM 3187 C CB . LYS B 2 82 ? 50.879 -19.529 -13.255 1.00 72.72 ? 82 LYS B CB 1 ATOM 3188 C CG . LYS B 2 82 ? 50.843 -18.298 -14.148 1.00 81.81 ? 82 LYS B CG 1 ATOM 3189 C CD . LYS B 2 82 ? 51.663 -17.172 -13.536 1.00 91.25 ? 82 LYS B CD 1 ATOM 3190 C CE . LYS B 2 82 ? 52.276 -16.260 -14.591 1.00 98.98 ? 82 LYS B CE 1 ATOM 3191 N NZ . LYS B 2 82 ? 53.354 -15.421 -13.994 1.00 103.05 ? 82 LYS B NZ 1 ATOM 3192 N N . LYS B 2 83 ? 52.130 -21.808 -14.954 1.00 66.37 ? 83 LYS B N 1 ATOM 3193 C CA . LYS B 2 83 ? 52.917 -22.287 -16.093 1.00 68.11 ? 83 LYS B CA 1 ATOM 3194 C C . LYS B 2 83 ? 52.185 -23.359 -16.890 1.00 64.30 ? 83 LYS B C 1 ATOM 3195 O O . LYS B 2 83 ? 52.287 -23.401 -18.112 1.00 64.72 ? 83 LYS B O 1 ATOM 3196 C CB . LYS B 2 83 ? 54.294 -22.793 -15.647 1.00 72.90 ? 83 LYS B CB 1 ATOM 3197 C CG . LYS B 2 83 ? 55.406 -21.766 -15.808 1.00 81.84 ? 83 LYS B CG 1 ATOM 3198 C CD . LYS B 2 83 ? 55.072 -20.437 -15.131 1.00 87.81 ? 83 LYS B CD 1 ATOM 3199 C CE . LYS B 2 83 ? 56.160 -19.389 -15.347 1.00 94.13 ? 83 LYS B CE 1 ATOM 3200 N NZ . LYS B 2 83 ? 56.264 -18.962 -16.774 1.00 97.28 ? 83 LYS B NZ 1 ATOM 3201 N N . MET B 2 84 ? 51.439 -24.211 -16.198 1.00 62.17 ? 84 MET B N 1 ATOM 3202 C CA . MET B 2 84 ? 50.623 -25.216 -16.861 1.00 60.22 ? 84 MET B CA 1 ATOM 3203 C C . MET B 2 84 ? 49.505 -24.575 -17.684 1.00 57.42 ? 84 MET B C 1 ATOM 3204 O O . MET B 2 84 ? 49.355 -24.890 -18.867 1.00 60.95 ? 84 MET B O 1 ATOM 3205 C CB . MET B 2 84 ? 50.028 -26.184 -15.841 1.00 62.10 ? 84 MET B CB 1 ATOM 3206 C CG . MET B 2 84 ? 49.500 -27.471 -16.454 1.00 65.93 ? 84 MET B CG 1 ATOM 3207 S SD . MET B 2 84 ? 47.902 -27.959 -15.796 1.00 72.63 ? 84 MET B SD 1 ATOM 3208 C CE . MET B 2 84 ? 46.879 -26.643 -16.436 1.00 74.15 ? 84 MET B CE 1 ATOM 3209 N N . GLU B 2 85 ? 48.734 -23.674 -17.080 1.00 77.59 ? 85 GLU B N 1 ATOM 3210 C CA . GLU B 2 85 ? 47.616 -23.051 -17.792 1.00 75.63 ? 85 GLU B CA 1 ATOM 3211 C C . GLU B 2 85 ? 48.144 -22.281 -19.001 1.00 72.21 ? 85 GLU B C 1 ATOM 3212 O O . GLU B 2 85 ? 47.640 -22.435 -20.113 1.00 70.24 ? 85 GLU B O 1 ATOM 3213 C CB . GLU B 2 85 ? 46.800 -22.138 -16.871 1.00 79.92 ? 85 GLU B CB 1 ATOM 3214 C CG . GLU B 2 85 ? 46.188 -22.839 -15.652 1.00 84.77 ? 85 GLU B CG 1 ATOM 3215 C CD . GLU B 2 85 ? 44.672 -23.027 -15.709 1.00 89.07 ? 85 GLU B CD 1 ATOM 3216 O OE1 . GLU B 2 85 ? 43.939 -22.092 -15.313 1.00 92.08 ? 85 GLU B OE1 1 ATOM 3217 O OE2 . GLU B 2 85 ? 44.205 -24.123 -16.097 1.00 90.18 ? 85 GLU B OE2 1 ATOM 3218 N N . ASP B 2 86 ? 49.189 -21.489 -18.785 1.00 70.86 ? 86 ASP B N 1 ATOM 3219 C CA . ASP B 2 86 ? 49.827 -20.719 -19.858 1.00 69.44 ? 86 ASP B CA 1 ATOM 3220 C C . ASP B 2 86 ? 50.438 -21.572 -20.953 1.00 65.49 ? 86 ASP B C 1 ATOM 3221 O O . ASP B 2 86 ? 50.324 -21.244 -22.128 1.00 64.13 ? 86 ASP B O 1 ATOM 3222 C CB . ASP B 2 86 ? 50.930 -19.815 -19.299 1.00 72.86 ? 86 ASP B CB 1 ATOM 3223 C CG . ASP B 2 86 ? 50.481 -18.397 -19.135 1.00 77.05 ? 86 ASP B CG 1 ATOM 3224 O OD1 . ASP B 2 86 ? 49.947 -17.837 -20.125 1.00 80.75 ? 86 ASP B OD1 1 ATOM 3225 O OD2 . ASP B 2 86 ? 50.670 -17.841 -18.030 1.00 80.58 ? 86 ASP B OD2 1 ATOM 3226 N N . GLY B 2 87 ? 51.118 -22.639 -20.558 1.00 63.50 ? 87 GLY B N 1 ATOM 3227 C CA . GLY B 2 87 ? 51.732 -23.550 -21.502 1.00 62.20 ? 87 GLY B CA 1 ATOM 3228 C C . GLY B 2 87 ? 50.748 -24.084 -22.526 1.00 61.18 ? 87 GLY B C 1 ATOM 3229 O O . GLY B 2 87 ? 51.036 -24.082 -23.730 1.00 60.08 ? 87 GLY B O 1 ATOM 3230 N N . PHE B 2 88 ? 49.584 -24.530 -22.054 1.00 60.19 ? 88 PHE B N 1 ATOM 3231 C CA . PHE B 2 88 ? 48.577 -25.088 -22.946 1.00 59.34 ? 88 PHE B CA 1 ATOM 3232 C C . PHE B 2 88 ? 47.988 -24.017 -23.871 1.00 59.86 ? 88 PHE B C 1 ATOM 3233 O O . PHE B 2 88 ? 47.802 -24.269 -25.061 1.00 58.24 ? 88 PHE B O 1 ATOM 3234 C CB . PHE B 2 88 ? 47.473 -25.800 -22.159 1.00 60.51 ? 88 PHE B CB 1 ATOM 3235 C CG . PHE B 2 88 ? 47.856 -27.179 -21.674 1.00 61.32 ? 88 PHE B CG 1 ATOM 3236 C CD1 . PHE B 2 88 ? 48.140 -28.196 -22.576 1.00 60.97 ? 88 PHE B CD1 1 ATOM 3237 C CD2 . PHE B 2 88 ? 47.920 -27.465 -20.319 1.00 63.15 ? 88 PHE B CD2 1 ATOM 3238 C CE1 . PHE B 2 88 ? 48.480 -29.466 -22.140 1.00 61.57 ? 88 PHE B CE1 1 ATOM 3239 C CE2 . PHE B 2 88 ? 48.260 -28.735 -19.875 1.00 64.36 ? 88 PHE B CE2 1 ATOM 3240 C CZ . PHE B 2 88 ? 48.541 -29.735 -20.788 1.00 64.26 ? 88 PHE B CZ 1 ATOM 3241 N N . LEU B 2 89 ? 47.719 -22.823 -23.343 1.00 62.37 ? 89 LEU B N 1 ATOM 3242 C CA . LEU B 2 89 ? 47.248 -21.713 -24.182 1.00 63.96 ? 89 LEU B CA 1 ATOM 3243 C C . LEU B 2 89 ? 48.200 -21.440 -25.346 1.00 61.74 ? 89 LEU B C 1 ATOM 3244 O O . LEU B 2 89 ? 47.763 -21.260 -26.472 1.00 59.45 ? 89 LEU B O 1 ATOM 3245 C CB . LEU B 2 89 ? 47.085 -20.423 -23.383 1.00 68.69 ? 89 LEU B CB 1 ATOM 3246 C CG . LEU B 2 89 ? 46.064 -20.384 -22.237 1.00 75.02 ? 89 LEU B CG 1 ATOM 3247 C CD1 . LEU B 2 89 ? 46.126 -19.002 -21.594 1.00 77.88 ? 89 LEU B CD1 1 ATOM 3248 C CD2 . LEU B 2 89 ? 44.637 -20.741 -22.674 1.00 76.01 ? 89 LEU B CD2 1 ATOM 3249 N N . ASP B 2 90 ? 49.497 -21.402 -25.066 1.00 61.37 ? 90 ASP B N 1 ATOM 3250 C CA . ASP B 2 90 ? 50.493 -21.160 -26.104 1.00 61.80 ? 90 ASP B CA 1 ATOM 3251 C C . ASP B 2 90 ? 50.508 -22.278 -27.141 1.00 60.01 ? 90 ASP B C 1 ATOM 3252 O O . ASP B 2 90 ? 50.688 -22.029 -28.328 1.00 60.87 ? 90 ASP B O 1 ATOM 3253 C CB . ASP B 2 90 ? 51.893 -21.013 -25.498 1.00 63.21 ? 90 ASP B CB 1 ATOM 3254 C CG . ASP B 2 90 ? 52.061 -19.730 -24.715 1.00 67.41 ? 90 ASP B CG 1 ATOM 3255 O OD1 . ASP B 2 90 ? 51.205 -18.821 -24.846 1.00 68.18 ? 90 ASP B OD1 1 ATOM 3256 O OD2 . ASP B 2 90 ? 53.064 -19.629 -23.969 1.00 71.27 ? 90 ASP B OD2 1 ATOM 3257 N N . VAL B 2 91 ? 50.339 -23.510 -26.683 1.00 59.60 ? 91 VAL B N 1 ATOM 3258 C CA . VAL B 2 91 ? 50.281 -24.655 -27.579 1.00 58.46 ? 91 VAL B CA 1 ATOM 3259 C C . VAL B 2 91 ? 49.082 -24.543 -28.523 1.00 57.08 ? 91 VAL B C 1 ATOM 3260 O O . VAL B 2 91 ? 49.223 -24.719 -29.731 1.00 58.05 ? 91 VAL B O 1 ATOM 3261 C CB . VAL B 2 91 ? 50.208 -25.984 -26.793 1.00 58.38 ? 91 VAL B CB 1 ATOM 3262 C CG1 . VAL B 2 91 ? 49.821 -27.136 -27.707 1.00 58.09 ? 91 VAL B CG1 1 ATOM 3263 C CG2 . VAL B 2 91 ? 51.541 -26.267 -26.112 1.00 59.05 ? 91 VAL B CG2 1 ATOM 3264 N N . TRP B 2 92 ? 47.912 -24.244 -27.979 1.00 55.78 ? 92 TRP B N 1 ATOM 3265 C CA . TRP B 2 92 ? 46.719 -24.149 -28.802 1.00 56.01 ? 92 TRP B CA 1 ATOM 3266 C C . TRP B 2 92 ? 46.691 -22.902 -29.682 1.00 55.87 ? 92 TRP B C 1 ATOM 3267 O O . TRP B 2 92 ? 46.136 -22.933 -30.776 1.00 56.77 ? 92 TRP B O 1 ATOM 3268 C CB . TRP B 2 92 ? 45.464 -24.245 -27.940 1.00 56.84 ? 92 TRP B CB 1 ATOM 3269 C CG . TRP B 2 92 ? 45.259 -25.635 -27.459 1.00 58.32 ? 92 TRP B CG 1 ATOM 3270 C CD1 . TRP B 2 92 ? 45.421 -26.097 -26.188 1.00 59.93 ? 92 TRP B CD1 1 ATOM 3271 C CD2 . TRP B 2 92 ? 44.899 -26.766 -28.253 1.00 58.42 ? 92 TRP B CD2 1 ATOM 3272 N NE1 . TRP B 2 92 ? 45.161 -27.442 -26.136 1.00 60.40 ? 92 TRP B NE1 1 ATOM 3273 C CE2 . TRP B 2 92 ? 44.837 -27.878 -27.391 1.00 59.80 ? 92 TRP B CE2 1 ATOM 3274 C CE3 . TRP B 2 92 ? 44.610 -26.945 -29.607 1.00 57.97 ? 92 TRP B CE3 1 ATOM 3275 C CZ2 . TRP B 2 92 ? 44.497 -29.153 -27.838 1.00 61.60 ? 92 TRP B CZ2 1 ATOM 3276 C CZ3 . TRP B 2 92 ? 44.267 -28.208 -30.049 1.00 59.25 ? 92 TRP B CZ3 1 ATOM 3277 C CH2 . TRP B 2 92 ? 44.210 -29.298 -29.166 1.00 60.86 ? 92 TRP B CH2 1 ATOM 3278 N N . THR B 2 93 ? 47.287 -21.814 -29.215 1.00 56.65 ? 93 THR B N 1 ATOM 3279 C CA . THR B 2 93 ? 47.415 -20.622 -30.031 1.00 56.72 ? 93 THR B CA 1 ATOM 3280 C C . THR B 2 93 ? 48.281 -20.956 -31.244 1.00 55.81 ? 93 THR B C 1 ATOM 3281 O O . THR B 2 93 ? 47.939 -20.591 -32.368 1.00 56.77 ? 93 THR B O 1 ATOM 3282 C CB . THR B 2 93 ? 48.025 -19.447 -29.239 1.00 58.49 ? 93 THR B CB 1 ATOM 3283 O OG1 . THR B 2 93 ? 47.113 -19.042 -28.216 1.00 59.86 ? 93 THR B OG1 1 ATOM 3284 C CG2 . THR B 2 93 ? 48.282 -18.255 -30.139 1.00 59.81 ? 93 THR B CG2 1 ATOM 3285 N N . TYR B 2 94 ? 49.381 -21.667 -31.007 1.00 54.57 ? 94 TYR B N 1 ATOM 3286 C CA . TYR B 2 94 ? 50.306 -22.060 -32.070 1.00 53.72 ? 94 TYR B CA 1 ATOM 3287 C C . TYR B 2 94 ? 49.594 -22.943 -33.075 1.00 52.82 ? 94 TYR B C 1 ATOM 3288 O O . TYR B 2 94 ? 49.623 -22.674 -34.270 1.00 52.43 ? 94 TYR B O 1 ATOM 3289 C CB . TYR B 2 94 ? 51.534 -22.782 -31.491 1.00 53.85 ? 94 TYR B CB 1 ATOM 3290 C CG . TYR B 2 94 ? 52.418 -23.460 -32.517 1.00 52.79 ? 94 TYR B CG 1 ATOM 3291 C CD1 . TYR B 2 94 ? 52.138 -24.754 -32.963 1.00 52.25 ? 94 TYR B CD1 1 ATOM 3292 C CD2 . TYR B 2 94 ? 53.534 -22.819 -33.038 1.00 52.94 ? 94 TYR B CD2 1 ATOM 3293 C CE1 . TYR B 2 94 ? 52.938 -25.377 -33.907 1.00 51.69 ? 94 TYR B CE1 1 ATOM 3294 C CE2 . TYR B 2 94 ? 54.341 -23.437 -33.980 1.00 53.02 ? 94 TYR B CE2 1 ATOM 3295 C CZ . TYR B 2 94 ? 54.035 -24.715 -34.407 1.00 52.69 ? 94 TYR B CZ 1 ATOM 3296 O OH . TYR B 2 94 ? 54.825 -25.343 -35.335 1.00 54.04 ? 94 TYR B OH 1 ATOM 3297 N N . ASN B 2 95 ? 48.950 -23.991 -32.581 1.00 54.75 ? 95 ASN B N 1 ATOM 3298 C CA . ASN B 2 95 ? 48.181 -24.894 -33.433 1.00 54.72 ? 95 ASN B CA 1 ATOM 3299 C C . ASN B 2 95 ? 47.202 -24.141 -34.320 1.00 54.84 ? 95 ASN B C 1 ATOM 3300 O O . ASN B 2 95 ? 47.168 -24.362 -35.530 1.00 55.98 ? 95 ASN B O 1 ATOM 3301 C CB . ASN B 2 95 ? 47.434 -25.937 -32.598 1.00 56.00 ? 95 ASN B CB 1 ATOM 3302 C CG . ASN B 2 95 ? 48.370 -26.940 -31.940 1.00 59.08 ? 95 ASN B CG 1 ATOM 3303 O OD1 . ASN B 2 95 ? 49.555 -26.992 -32.245 1.00 60.20 ? 95 ASN B OD1 1 ATOM 3304 N ND2 . ASN B 2 95 ? 47.833 -27.746 -31.030 1.00 62.06 ? 95 ASN B ND2 1 ATOM 3305 N N . ALA B 2 96 ? 46.426 -23.237 -33.731 1.00 55.47 ? 96 ALA B N 1 ATOM 3306 C CA . ALA B 2 96 ? 45.407 -22.493 -34.489 1.00 55.36 ? 96 ALA B CA 1 ATOM 3307 C C . ALA B 2 96 ? 46.014 -21.602 -35.580 1.00 53.26 ? 96 ALA B C 1 ATOM 3308 O O . ALA B 2 96 ? 45.560 -21.614 -36.715 1.00 51.40 ? 96 ALA B O 1 ATOM 3309 C CB . ALA B 2 96 ? 44.548 -21.658 -33.553 1.00 56.91 ? 96 ALA B CB 1 ATOM 3310 N N . GLU B 2 97 ? 47.043 -20.840 -35.235 1.00 53.06 ? 97 GLU B N 1 ATOM 3311 C CA . GLU B 2 97 ? 47.623 -19.893 -36.186 1.00 54.57 ? 97 GLU B CA 1 ATOM 3312 C C . GLU B 2 97 ? 48.334 -20.604 -37.333 1.00 52.83 ? 97 GLU B C 1 ATOM 3313 O O . GLU B 2 97 ? 48.214 -20.206 -38.489 1.00 53.07 ? 97 GLU B O 1 ATOM 3314 C CB . GLU B 2 97 ? 48.556 -18.910 -35.472 1.00 57.13 ? 97 GLU B CB 1 ATOM 3315 C CG . GLU B 2 97 ? 47.790 -17.926 -34.592 1.00 60.34 ? 97 GLU B CG 1 ATOM 3316 C CD . GLU B 2 97 ? 48.668 -17.001 -33.776 1.00 64.40 ? 97 GLU B CD 1 ATOM 3317 O OE1 . GLU B 2 97 ? 49.905 -17.180 -33.770 1.00 68.56 ? 97 GLU B OE1 1 ATOM 3318 O OE2 . GLU B 2 97 ? 48.113 -16.087 -33.125 1.00 67.77 ? 97 GLU B OE2 1 ATOM 3319 N N . LEU B 2 98 ? 49.051 -21.671 -37.010 1.00 52.84 ? 98 LEU B N 1 ATOM 3320 C CA . LEU B 2 98 ? 49.772 -22.434 -38.008 1.00 51.83 ? 98 LEU B CA 1 ATOM 3321 C C . LEU B 2 98 ? 48.807 -23.132 -38.953 1.00 50.38 ? 98 LEU B C 1 ATOM 3322 O O . LEU B 2 98 ? 49.014 -23.147 -40.152 1.00 49.49 ? 98 LEU B O 1 ATOM 3323 C CB . LEU B 2 98 ? 50.654 -23.471 -37.335 1.00 53.64 ? 98 LEU B CB 1 ATOM 3324 C CG . LEU B 2 98 ? 51.598 -24.229 -38.265 1.00 55.12 ? 98 LEU B CG 1 ATOM 3325 C CD1 . LEU B 2 98 ? 52.688 -23.281 -38.747 1.00 56.67 ? 98 LEU B CD1 1 ATOM 3326 C CD2 . LEU B 2 98 ? 52.196 -25.444 -37.563 1.00 55.64 ? 98 LEU B CD2 1 ATOM 3327 N N . LEU B 2 99 ? 47.747 -23.706 -38.411 1.00 51.34 ? 99 LEU B N 1 ATOM 3328 C CA . LEU B 2 99 ? 46.760 -24.384 -39.229 1.00 52.47 ? 99 LEU B CA 1 ATOM 3329 C C . LEU B 2 99 ? 46.184 -23.426 -40.269 1.00 52.29 ? 99 LEU B C 1 ATOM 3330 O O . LEU B 2 99 ? 46.054 -23.768 -41.449 1.00 52.85 ? 99 LEU B O 1 ATOM 3331 C CB . LEU B 2 99 ? 45.642 -24.941 -38.348 1.00 55.08 ? 99 LEU B CB 1 ATOM 3332 C CG . LEU B 2 99 ? 44.565 -25.771 -39.053 1.00 58.43 ? 99 LEU B CG 1 ATOM 3333 C CD1 . LEU B 2 99 ? 45.163 -26.978 -39.745 1.00 59.35 ? 99 LEU B CD1 1 ATOM 3334 C CD2 . LEU B 2 99 ? 43.503 -26.212 -38.058 1.00 62.43 ? 99 LEU B CD2 1 ATOM 3335 N N . VAL B 2 100 ? 45.842 -22.223 -39.826 1.00 52.17 ? 100 VAL B N 1 ATOM 3336 C CA . VAL B 2 100 ? 45.281 -21.209 -40.714 1.00 50.42 ? 100 VAL B CA 1 ATOM 3337 C C . VAL B 2 100 ? 46.264 -20.790 -41.814 1.00 48.42 ? 100 VAL B C 1 ATOM 3338 O O . VAL B 2 100 ? 45.887 -20.717 -42.980 1.00 45.90 ? 100 VAL B O 1 ATOM 3339 C CB . VAL B 2 100 ? 44.771 -20.001 -39.908 1.00 50.84 ? 100 VAL B CB 1 ATOM 3340 C CG1 . VAL B 2 100 ? 44.526 -18.795 -40.809 1.00 51.79 ? 100 VAL B CG1 1 ATOM 3341 C CG2 . VAL B 2 100 ? 43.491 -20.400 -39.180 1.00 51.60 ? 100 VAL B CG2 1 ATOM 3342 N N . LEU B 2 101 ? 47.504 -20.500 -41.431 1.00 47.83 ? 101 LEU B N 1 ATOM 3343 C CA . LEU B 2 101 ? 48.578 -20.244 -42.392 1.00 48.00 ? 101 LEU B CA 1 ATOM 3344 C C . LEU B 2 101 ? 48.716 -21.372 -43.427 1.00 48.81 ? 101 LEU B C 1 ATOM 3345 O O . LEU B 2 101 ? 48.673 -21.137 -44.632 1.00 52.66 ? 101 LEU B O 1 ATOM 3346 C CB . LEU B 2 101 ? 49.902 -20.086 -41.648 1.00 48.94 ? 101 LEU B CB 1 ATOM 3347 C CG . LEU B 2 101 ? 50.476 -18.687 -41.442 1.00 51.68 ? 101 LEU B CG 1 ATOM 3348 C CD1 . LEU B 2 101 ? 49.416 -17.616 -41.245 1.00 53.35 ? 101 LEU B CD1 1 ATOM 3349 C CD2 . LEU B 2 101 ? 51.436 -18.709 -40.269 1.00 52.17 ? 101 LEU B CD2 1 ATOM 3350 N N . MET B 2 102 ? 48.884 -22.596 -42.956 1.00 47.79 ? 102 MET B N 1 ATOM 3351 C CA . MET B 2 102 ? 49.094 -23.720 -43.844 1.00 48.40 ? 102 MET B CA 1 ATOM 3352 C C . MET B 2 102 ? 47.894 -23.954 -44.756 1.00 48.04 ? 102 MET B C 1 ATOM 3353 O O . MET B 2 102 ? 48.061 -24.119 -45.968 1.00 49.12 ? 102 MET B O 1 ATOM 3354 C CB . MET B 2 102 ? 49.427 -24.986 -43.044 1.00 51.07 ? 102 MET B CB 1 ATOM 3355 C CG . MET B 2 102 ? 50.767 -24.912 -42.324 1.00 55.24 ? 102 MET B CG 1 ATOM 3356 S SD . MET B 2 102 ? 51.384 -26.496 -41.697 1.00 62.84 ? 102 MET B SD 1 ATOM 3357 C CE . MET B 2 102 ? 49.903 -27.156 -40.936 1.00 62.57 ? 102 MET B CE 1 ATOM 3358 N N . GLU B 2 103 ? 46.687 -23.965 -44.199 1.00 47.49 ? 103 GLU B N 1 ATOM 3359 C CA . GLU B 2 103 ? 45.511 -24.261 -45.014 1.00 48.91 ? 103 GLU B CA 1 ATOM 3360 C C . GLU B 2 103 ? 45.119 -23.110 -45.951 1.00 49.07 ? 103 GLU B C 1 ATOM 3361 O O . GLU B 2 103 ? 44.595 -23.351 -47.039 1.00 49.57 ? 103 GLU B O 1 ATOM 3362 C CB . GLU B 2 103 ? 44.336 -24.704 -44.147 1.00 50.69 ? 103 GLU B CB 1 ATOM 3363 C CG . GLU B 2 103 ? 44.536 -26.091 -43.536 1.00 53.01 ? 103 GLU B CG 1 ATOM 3364 C CD . GLU B 2 103 ? 44.603 -27.209 -44.571 1.00 54.84 ? 103 GLU B CD 1 ATOM 3365 O OE1 . GLU B 2 103 ? 43.936 -27.099 -45.624 1.00 56.13 ? 103 GLU B OE1 1 ATOM 3366 O OE2 . GLU B 2 103 ? 45.325 -28.208 -44.337 1.00 58.47 ? 103 GLU B OE2 1 ATOM 3367 N N . ASN B 2 104 ? 45.387 -21.871 -45.553 1.00 48.31 ? 104 ASN B N 1 ATOM 3368 C CA . ASN B 2 104 ? 45.230 -20.746 -46.473 1.00 48.76 ? 104 ASN B CA 1 ATOM 3369 C C . ASN B 2 104 ? 46.093 -20.920 -47.721 1.00 48.64 ? 104 ASN B C 1 ATOM 3370 O O . ASN B 2 104 ? 45.621 -20.746 -48.833 1.00 47.41 ? 104 ASN B O 1 ATOM 3371 C CB . ASN B 2 104 ? 45.577 -19.409 -45.799 1.00 48.68 ? 104 ASN B CB 1 ATOM 3372 C CG . ASN B 2 104 ? 44.471 -18.908 -44.891 1.00 48.48 ? 104 ASN B CG 1 ATOM 3373 O OD1 . ASN B 2 104 ? 43.359 -19.422 -44.921 1.00 47.13 ? 104 ASN B OD1 1 ATOM 3374 N ND2 . ASN B 2 104 ? 44.776 -17.901 -44.076 1.00 49.50 ? 104 ASN B ND2 1 ATOM 3375 N N . GLU B 2 105 ? 47.359 -21.258 -47.536 1.00 49.88 ? 105 GLU B N 1 ATOM 3376 C CA . GLU B 2 105 ? 48.216 -21.499 -48.674 1.00 50.99 ? 105 GLU B CA 1 ATOM 3377 C C . GLU B 2 105 ? 47.630 -22.605 -49.536 1.00 49.08 ? 105 GLU B C 1 ATOM 3378 O O . GLU B 2 105 ? 47.597 -22.502 -50.756 1.00 47.02 ? 105 GLU B O 1 ATOM 3379 C CB . GLU B 2 105 ? 49.617 -21.887 -48.235 1.00 55.65 ? 105 GLU B CB 1 ATOM 3380 C CG . GLU B 2 105 ? 50.654 -21.670 -49.318 1.00 63.41 ? 105 GLU B CG 1 ATOM 3381 C CD . GLU B 2 105 ? 52.040 -21.561 -48.737 1.00 72.67 ? 105 GLU B CD 1 ATOM 3382 O OE1 . GLU B 2 105 ? 52.484 -22.563 -48.135 1.00 82.13 ? 105 GLU B OE1 1 ATOM 3383 O OE2 . GLU B 2 105 ? 52.667 -20.475 -48.855 1.00 75.52 ? 105 GLU B OE2 1 ATOM 3384 N N . ARG B 2 106 ? 47.153 -23.666 -48.906 1.00 49.28 ? 106 ARG B N 1 ATOM 3385 C CA . ARG B 2 106 ? 46.589 -24.761 -49.684 1.00 51.39 ? 106 ARG B CA 1 ATOM 3386 C C . ARG B 2 106 ? 45.301 -24.359 -50.408 1.00 47.84 ? 106 ARG B C 1 ATOM 3387 O O . ARG B 2 106 ? 45.063 -24.803 -51.523 1.00 49.03 ? 106 ARG B O 1 ATOM 3388 C CB . ARG B 2 106 ? 46.389 -26.006 -48.822 1.00 54.15 ? 106 ARG B CB 1 ATOM 3389 C CG . ARG B 2 106 ? 47.700 -26.613 -48.314 1.00 57.51 ? 106 ARG B CG 1 ATOM 3390 C CD . ARG B 2 106 ? 47.569 -28.123 -48.140 1.00 63.82 ? 106 ARG B CD 1 ATOM 3391 N NE . ARG B 2 106 ? 47.931 -28.867 -49.360 1.00 67.31 ? 106 ARG B NE 1 ATOM 3392 C CZ . ARG B 2 106 ? 47.421 -30.042 -49.724 1.00 70.67 ? 106 ARG B CZ 1 ATOM 3393 N NH1 . ARG B 2 106 ? 46.490 -30.641 -48.995 1.00 74.04 ? 106 ARG B NH1 1 ATOM 3394 N NH2 . ARG B 2 106 ? 47.836 -30.630 -50.841 1.00 76.83 ? 106 ARG B NH2 1 ATOM 3395 N N . THR B 2 107 ? 44.494 -23.498 -49.798 1.00 46.36 ? 107 THR B N 1 ATOM 3396 C CA . THR B 2 107 ? 43.229 -23.083 -50.400 1.00 43.82 ? 107 THR B CA 1 ATOM 3397 C C . THR B 2 107 ? 43.486 -22.259 -51.664 1.00 43.48 ? 107 THR B C 1 ATOM 3398 O O . THR B 2 107 ? 42.830 -22.460 -52.678 1.00 42.06 ? 107 THR B O 1 ATOM 3399 C CB . THR B 2 107 ? 42.348 -22.308 -49.396 1.00 44.66 ? 107 THR B CB 1 ATOM 3400 O OG1 . THR B 2 107 ? 41.902 -23.189 -48.354 1.00 44.17 ? 107 THR B OG1 1 ATOM 3401 C CG2 . THR B 2 107 ? 41.119 -21.711 -50.085 1.00 46.27 ? 107 THR B CG2 1 ATOM 3402 N N . LEU B 2 108 ? 44.447 -21.344 -51.616 1.00 43.09 ? 108 LEU B N 1 ATOM 3403 C CA . LEU B 2 108 ? 44.770 -20.551 -52.795 1.00 43.54 ? 108 LEU B CA 1 ATOM 3404 C C . LEU B 2 108 ? 45.293 -21.428 -53.951 1.00 44.03 ? 108 LEU B C 1 ATOM 3405 O O . LEU B 2 108 ? 44.866 -21.284 -55.104 1.00 43.48 ? 108 LEU B O 1 ATOM 3406 C CB . LEU B 2 108 ? 45.770 -19.452 -52.447 1.00 44.28 ? 108 LEU B CB 1 ATOM 3407 C CG . LEU B 2 108 ? 45.327 -18.395 -51.422 1.00 46.29 ? 108 LEU B CG 1 ATOM 3408 C CD1 . LEU B 2 108 ? 46.397 -17.328 -51.285 1.00 48.04 ? 108 LEU B CD1 1 ATOM 3409 C CD2 . LEU B 2 108 ? 44.000 -17.737 -51.768 1.00 47.48 ? 108 LEU B CD2 1 ATOM 3410 N N . ASP B 2 109 ? 46.208 -22.337 -53.637 1.00 43.74 ? 109 ASP B N 1 ATOM 3411 C CA . ASP B 2 109 ? 46.688 -23.306 -54.608 1.00 44.05 ? 109 ASP B CA 1 ATOM 3412 C C . ASP B 2 109 ? 45.567 -24.189 -55.204 1.00 43.31 ? 109 ASP B C 1 ATOM 3413 O O . ASP B 2 109 ? 45.612 -24.526 -56.379 1.00 45.50 ? 109 ASP B O 1 ATOM 3414 C CB . ASP B 2 109 ? 47.741 -24.200 -53.959 1.00 47.03 ? 109 ASP B CB 1 ATOM 3415 C CG . ASP B 2 109 ? 49.036 -23.448 -53.619 1.00 51.28 ? 109 ASP B CG 1 ATOM 3416 O OD1 . ASP B 2 109 ? 49.419 -22.526 -54.379 1.00 51.74 ? 109 ASP B OD1 1 ATOM 3417 O OD2 . ASP B 2 109 ? 49.680 -23.813 -52.594 1.00 55.53 ? 109 ASP B OD2 1 ATOM 3418 N N . PHE B 2 110 ? 44.591 -24.585 -54.387 1.00 40.94 ? 110 PHE B N 1 ATOM 3419 C CA . PHE B 2 110 ? 43.461 -25.412 -54.820 1.00 39.73 ? 110 PHE B CA 1 ATOM 3420 C C . PHE B 2 110 ? 42.705 -24.708 -55.945 1.00 40.88 ? 110 PHE B C 1 ATOM 3421 O O . PHE B 2 110 ? 42.410 -25.319 -56.980 1.00 42.69 ? 110 PHE B O 1 ATOM 3422 C CB . PHE B 2 110 ? 42.552 -25.682 -53.604 1.00 39.74 ? 110 PHE B CB 1 ATOM 3423 C CG . PHE B 2 110 ? 41.285 -26.444 -53.904 1.00 40.74 ? 110 PHE B CG 1 ATOM 3424 C CD1 . PHE B 2 110 ? 41.316 -27.688 -54.521 1.00 42.52 ? 110 PHE B CD1 1 ATOM 3425 C CD2 . PHE B 2 110 ? 40.058 -25.945 -53.505 1.00 41.44 ? 110 PHE B CD2 1 ATOM 3426 C CE1 . PHE B 2 110 ? 40.146 -28.395 -54.766 1.00 44.15 ? 110 PHE B CE1 1 ATOM 3427 C CE2 . PHE B 2 110 ? 38.877 -26.649 -53.747 1.00 43.62 ? 110 PHE B CE2 1 ATOM 3428 C CZ . PHE B 2 110 ? 38.919 -27.876 -54.380 1.00 44.71 ? 110 PHE B CZ 1 ATOM 3429 N N . HIS B 2 111 ? 42.410 -23.422 -55.747 1.00 40.50 ? 111 HIS B N 1 ATOM 3430 C CA . HIS B 2 111 ? 41.760 -22.600 -56.771 1.00 41.39 ? 111 HIS B CA 1 ATOM 3431 C C . HIS B 2 111 ? 42.605 -22.522 -58.065 1.00 41.67 ? 111 HIS B C 1 ATOM 3432 O O . HIS B 2 111 ? 42.070 -22.643 -59.169 1.00 44.79 ? 111 HIS B O 1 ATOM 3433 C CB . HIS B 2 111 ? 41.478 -21.178 -56.243 1.00 41.08 ? 111 HIS B CB 1 ATOM 3434 C CG . HIS B 2 111 ? 40.394 -21.113 -55.208 1.00 41.31 ? 111 HIS B CG 1 ATOM 3435 N ND1 . HIS B 2 111 ? 39.094 -21.493 -55.466 1.00 42.36 ? 111 HIS B ND1 1 ATOM 3436 C CD2 . HIS B 2 111 ? 40.415 -20.693 -53.919 1.00 40.69 ? 111 HIS B CD2 1 ATOM 3437 C CE1 . HIS B 2 111 ? 38.364 -21.320 -54.379 1.00 43.14 ? 111 HIS B CE1 1 ATOM 3438 N NE2 . HIS B 2 111 ? 39.141 -20.833 -53.427 1.00 41.91 ? 111 HIS B NE2 1 ATOM 3439 N N . ASP B 2 112 ? 43.911 -22.336 -57.918 1.00 39.45 ? 112 ASP B N 1 ATOM 3440 C CA . ASP B 2 112 ? 44.833 -22.292 -59.043 1.00 39.90 ? 112 ASP B CA 1 ATOM 3441 C C . ASP B 2 112 ? 44.750 -23.625 -59.809 1.00 41.37 ? 112 ASP B C 1 ATOM 3442 O O . ASP B 2 112 ? 44.623 -23.656 -61.038 1.00 43.77 ? 112 ASP B O 1 ATOM 3443 C CB . ASP B 2 112 ? 46.253 -22.045 -58.506 1.00 40.59 ? 112 ASP B CB 1 ATOM 3444 C CG . ASP B 2 112 ? 47.250 -21.652 -59.586 1.00 42.97 ? 112 ASP B CG 1 ATOM 3445 O OD1 . ASP B 2 112 ? 46.844 -21.404 -60.743 1.00 43.53 ? 112 ASP B OD1 1 ATOM 3446 O OD2 . ASP B 2 112 ? 48.463 -21.584 -59.265 1.00 44.96 ? 112 ASP B OD2 1 ATOM 3447 N N . SER B 2 113 ? 44.780 -24.727 -59.071 1.00 40.96 ? 113 SER B N 1 ATOM 3448 C CA . SER B 2 113 ? 44.649 -26.062 -59.650 1.00 41.79 ? 113 SER B CA 1 ATOM 3449 C C . SER B 2 113 ? 43.347 -26.240 -60.434 1.00 42.50 ? 113 SER B C 1 ATOM 3450 O O . SER B 2 113 ? 43.348 -26.775 -61.550 1.00 41.60 ? 113 SER B O 1 ATOM 3451 C CB . SER B 2 113 ? 44.729 -27.122 -58.548 1.00 42.17 ? 113 SER B CB 1 ATOM 3452 O OG . SER B 2 113 ? 44.352 -28.393 -59.028 1.00 44.25 ? 113 SER B OG 1 ATOM 3453 N N . ASN B 2 114 ? 42.233 -25.810 -59.849 1.00 42.22 ? 114 ASN B N 1 ATOM 3454 C CA . ASN B 2 114 ? 40.956 -25.963 -60.528 1.00 42.83 ? 114 ASN B CA 1 ATOM 3455 C C . ASN B 2 114 ? 40.929 -25.164 -61.828 1.00 42.40 ? 114 ASN B C 1 ATOM 3456 O O . ASN B 2 114 ? 40.348 -25.617 -62.808 1.00 41.34 ? 114 ASN B O 1 ATOM 3457 C CB . ASN B 2 114 ? 39.795 -25.546 -59.634 1.00 43.93 ? 114 ASN B CB 1 ATOM 3458 C CG . ASN B 2 114 ? 39.648 -26.421 -58.413 1.00 44.89 ? 114 ASN B CG 1 ATOM 3459 O OD1 . ASN B 2 114 ? 39.868 -27.638 -58.453 1.00 46.28 ? 114 ASN B OD1 1 ATOM 3460 N ND2 . ASN B 2 114 ? 39.260 -25.807 -57.315 1.00 45.04 ? 114 ASN B ND2 1 ATOM 3461 N N . VAL B 2 115 ? 41.580 -23.994 -61.849 1.00 41.61 ? 115 VAL B N 1 ATOM 3462 C CA . VAL B 2 115 ? 41.595 -23.168 -63.065 1.00 41.25 ? 115 VAL B CA 1 ATOM 3463 C C . VAL B 2 115 ? 42.443 -23.836 -64.152 1.00 42.17 ? 115 VAL B C 1 ATOM 3464 O O . VAL B 2 115 ? 42.024 -23.919 -65.305 1.00 41.91 ? 115 VAL B O 1 ATOM 3465 C CB . VAL B 2 115 ? 42.103 -21.739 -62.789 1.00 41.02 ? 115 VAL B CB 1 ATOM 3466 C CG1 . VAL B 2 115 ? 42.318 -20.973 -64.090 1.00 41.87 ? 115 VAL B CG1 1 ATOM 3467 C CG2 . VAL B 2 115 ? 41.119 -20.987 -61.917 1.00 41.73 ? 115 VAL B CG2 1 ATOM 3468 N N . LYS B 2 116 ? 43.627 -24.317 -63.781 1.00 43.40 ? 116 LYS B N 1 ATOM 3469 C CA . LYS B 2 116 ? 44.480 -25.020 -64.731 1.00 46.02 ? 116 LYS B CA 1 ATOM 3470 C C . LYS B 2 116 ? 43.807 -26.253 -65.310 1.00 46.80 ? 116 LYS B C 1 ATOM 3471 O O . LYS B 2 116 ? 43.915 -26.526 -66.512 1.00 47.48 ? 116 LYS B O 1 ATOM 3472 C CB . LYS B 2 116 ? 45.802 -25.447 -64.098 1.00 49.02 ? 116 LYS B CB 1 ATOM 3473 C CG . LYS B 2 116 ? 46.839 -25.778 -65.150 1.00 54.64 ? 116 LYS B CG 1 ATOM 3474 C CD . LYS B 2 116 ? 47.957 -26.638 -64.589 1.00 62.71 ? 116 LYS B CD 1 ATOM 3475 C CE . LYS B 2 116 ? 49.047 -26.867 -65.630 1.00 67.27 ? 116 LYS B CE 1 ATOM 3476 N NZ . LYS B 2 116 ? 49.521 -25.571 -66.203 1.00 68.01 ? 116 LYS B NZ 1 ATOM 3477 N N . ASN B 2 117 ? 43.127 -27.010 -64.459 1.00 47.14 ? 117 ASN B N 1 ATOM 3478 C CA . ASN B 2 117 ? 42.476 -28.232 -64.909 1.00 49.86 ? 117 ASN B CA 1 ATOM 3479 C C . ASN B 2 117 ? 41.344 -27.945 -65.878 1.00 50.60 ? 117 ASN B C 1 ATOM 3480 O O . ASN B 2 117 ? 41.148 -28.680 -66.841 1.00 52.24 ? 117 ASN B O 1 ATOM 3481 C CB . ASN B 2 117 ? 41.979 -29.050 -63.718 1.00 50.57 ? 117 ASN B CB 1 ATOM 3482 C CG . ASN B 2 117 ? 43.116 -29.653 -62.918 1.00 50.51 ? 117 ASN B CG 1 ATOM 3483 O OD1 . ASN B 2 117 ? 44.221 -29.813 -63.418 1.00 50.52 ? 117 ASN B OD1 1 ATOM 3484 N ND2 . ASN B 2 117 ? 42.847 -29.991 -61.669 1.00 51.33 ? 117 ASN B ND2 1 ATOM 3485 N N . LEU B 2 118 ? 40.615 -26.866 -65.631 1.00 50.40 ? 118 LEU B N 1 ATOM 3486 C CA . LEU B 2 118 ? 39.554 -26.450 -66.537 1.00 51.97 ? 118 LEU B CA 1 ATOM 3487 C C . LEU B 2 118 ? 40.154 -26.022 -67.871 1.00 52.09 ? 118 LEU B C 1 ATOM 3488 O O . LEU B 2 118 ? 39.657 -26.405 -68.933 1.00 53.92 ? 118 LEU B O 1 ATOM 3489 C CB . LEU B 2 118 ? 38.743 -25.320 -65.910 1.00 53.14 ? 118 LEU B CB 1 ATOM 3490 C CG . LEU B 2 118 ? 37.561 -24.759 -66.683 1.00 55.82 ? 118 LEU B CG 1 ATOM 3491 C CD1 . LEU B 2 118 ? 36.624 -25.858 -67.165 1.00 59.26 ? 118 LEU B CD1 1 ATOM 3492 C CD2 . LEU B 2 118 ? 36.826 -23.778 -65.791 1.00 56.69 ? 118 LEU B CD2 1 ATOM 3493 N N . TYR B 2 119 ? 41.240 -25.254 -67.819 1.00 49.87 ? 119 TYR B N 1 ATOM 3494 C CA . TYR B 2 119 ? 41.946 -24.865 -69.038 1.00 49.30 ? 119 TYR B CA 1 ATOM 3495 C C . TYR B 2 119 ? 42.436 -26.081 -69.824 1.00 51.43 ? 119 TYR B C 1 ATOM 3496 O O . TYR B 2 119 ? 42.322 -26.107 -71.046 1.00 55.90 ? 119 TYR B O 1 ATOM 3497 C CB . TYR B 2 119 ? 43.115 -23.930 -68.720 1.00 47.62 ? 119 TYR B CB 1 ATOM 3498 C CG . TYR B 2 119 ? 43.942 -23.523 -69.928 1.00 48.51 ? 119 TYR B CG 1 ATOM 3499 C CD1 . TYR B 2 119 ? 43.514 -22.515 -70.787 1.00 49.07 ? 119 TYR B CD1 1 ATOM 3500 C CD2 . TYR B 2 119 ? 45.163 -24.134 -70.199 1.00 50.24 ? 119 TYR B CD2 1 ATOM 3501 C CE1 . TYR B 2 119 ? 44.274 -22.129 -71.883 1.00 51.13 ? 119 TYR B CE1 1 ATOM 3502 C CE2 . TYR B 2 119 ? 45.930 -23.759 -71.293 1.00 51.57 ? 119 TYR B CE2 1 ATOM 3503 C CZ . TYR B 2 119 ? 45.483 -22.760 -72.131 1.00 53.25 ? 119 TYR B CZ 1 ATOM 3504 O OH . TYR B 2 119 ? 46.245 -22.391 -73.214 1.00 55.31 ? 119 TYR B OH 1 ATOM 3505 N N . ASP B 2 120 ? 42.976 -27.086 -69.146 1.00 51.54 ? 120 ASP B N 1 ATOM 3506 C CA . ASP B 2 120 ? 43.459 -28.279 -69.852 1.00 54.00 ? 120 ASP B CA 1 ATOM 3507 C C . ASP B 2 120 ? 42.312 -29.098 -70.447 1.00 53.45 ? 120 ASP B C 1 ATOM 3508 O O . ASP B 2 120 ? 42.420 -29.614 -71.551 1.00 53.60 ? 120 ASP B O 1 ATOM 3509 C CB . ASP B 2 120 ? 44.321 -29.150 -68.929 1.00 56.37 ? 120 ASP B CB 1 ATOM 3510 C CG . ASP B 2 120 ? 45.654 -28.503 -68.594 1.00 57.27 ? 120 ASP B CG 1 ATOM 3511 O OD1 . ASP B 2 120 ? 46.248 -27.857 -69.483 1.00 58.79 ? 120 ASP B OD1 1 ATOM 3512 O OD2 . ASP B 2 120 ? 46.119 -28.647 -67.439 1.00 59.90 ? 120 ASP B OD2 1 ATOM 3513 N N . LYS B 2 121 ? 41.218 -29.208 -69.713 1.00 53.99 ? 121 LYS B N 1 ATOM 3514 C CA . LYS B 2 121 ? 40.008 -29.879 -70.204 1.00 58.30 ? 121 LYS B CA 1 ATOM 3515 C C . LYS B 2 121 ? 39.575 -29.337 -71.564 1.00 58.59 ? 121 LYS B C 1 ATOM 3516 O O . LYS B 2 121 ? 39.264 -30.099 -72.469 1.00 61.56 ? 121 LYS B O 1 ATOM 3517 C CB . LYS B 2 121 ? 38.884 -29.678 -69.191 1.00 60.34 ? 121 LYS B CB 1 ATOM 3518 C CG . LYS B 2 121 ? 37.600 -30.446 -69.424 1.00 64.68 ? 121 LYS B CG 1 ATOM 3519 C CD . LYS B 2 121 ? 36.590 -30.048 -68.346 1.00 67.14 ? 121 LYS B CD 1 ATOM 3520 C CE . LYS B 2 121 ? 35.430 -31.024 -68.221 1.00 72.43 ? 121 LYS B CE 1 ATOM 3521 N NZ . LYS B 2 121 ? 34.564 -31.019 -69.435 1.00 76.62 ? 121 LYS B NZ 1 ATOM 3522 N N . VAL B 2 122 ? 39.564 -28.015 -71.703 1.00 56.26 ? 122 VAL B N 1 ATOM 3523 C CA . VAL B 2 122 ? 39.202 -27.378 -72.960 1.00 55.92 ? 122 VAL B CA 1 ATOM 3524 C C . VAL B 2 122 ? 40.292 -27.571 -74.012 1.00 58.60 ? 122 VAL B C 1 ATOM 3525 O O . VAL B 2 122 ? 39.995 -27.880 -75.173 1.00 59.78 ? 122 VAL B O 1 ATOM 3526 C CB . VAL B 2 122 ? 38.909 -25.881 -72.755 1.00 53.77 ? 122 VAL B CB 1 ATOM 3527 C CG1 . VAL B 2 122 ? 38.793 -25.147 -74.090 1.00 53.73 ? 122 VAL B CG1 1 ATOM 3528 C CG2 . VAL B 2 122 ? 37.640 -25.724 -71.927 1.00 53.23 ? 122 VAL B CG2 1 ATOM 3529 N N . ARG B 2 123 ? 41.546 -27.391 -73.614 1.00 58.02 ? 123 ARG B N 1 ATOM 3530 C CA . ARG B 2 123 ? 42.666 -27.608 -74.527 1.00 61.33 ? 123 ARG B CA 1 ATOM 3531 C C . ARG B 2 123 ? 42.610 -29.000 -75.173 1.00 65.09 ? 123 ARG B C 1 ATOM 3532 O O . ARG B 2 123 ? 42.799 -29.130 -76.388 1.00 66.83 ? 123 ARG B O 1 ATOM 3533 C CB . ARG B 2 123 ? 43.992 -27.436 -73.788 1.00 62.77 ? 123 ARG B CB 1 ATOM 3534 C CG . ARG B 2 123 ? 45.203 -27.377 -74.701 1.00 66.31 ? 123 ARG B CG 1 ATOM 3535 C CD . ARG B 2 123 ? 46.498 -27.209 -73.914 1.00 68.68 ? 123 ARG B CD 1 ATOM 3536 N NE . ARG B 2 123 ? 46.601 -28.154 -72.802 1.00 70.22 ? 123 ARG B NE 1 ATOM 3537 C CZ . ARG B 2 123 ? 46.873 -29.455 -72.926 1.00 72.45 ? 123 ARG B CZ 1 ATOM 3538 N NH1 . ARG B 2 123 ? 47.077 -30.014 -74.120 1.00 74.39 ? 123 ARG B NH1 1 ATOM 3539 N NH2 . ARG B 2 123 ? 46.935 -30.210 -71.839 1.00 71.84 ? 123 ARG B NH2 1 ATOM 3540 N N . LEU B 2 124 ? 42.340 -30.026 -74.363 1.00 66.91 ? 124 LEU B N 1 ATOM 3541 C CA . LEU B 2 124 ? 42.322 -31.424 -74.838 1.00 72.82 ? 124 LEU B CA 1 ATOM 3542 C C . LEU B 2 124 ? 41.137 -31.748 -75.755 1.00 74.84 ? 124 LEU B C 1 ATOM 3543 O O . LEU B 2 124 ? 41.176 -32.738 -76.481 1.00 79.30 ? 124 LEU B O 1 ATOM 3544 C CB . LEU B 2 124 ? 42.346 -32.409 -73.657 1.00 74.52 ? 124 LEU B CB 1 ATOM 3545 C CG . LEU B 2 124 ? 43.644 -32.391 -72.833 1.00 75.57 ? 124 LEU B CG 1 ATOM 3546 C CD1 . LEU B 2 124 ? 43.445 -32.913 -71.410 1.00 77.01 ? 124 LEU B CD1 1 ATOM 3547 C CD2 . LEU B 2 124 ? 44.745 -33.163 -73.545 1.00 78.42 ? 124 LEU B CD2 1 ATOM 3548 N N . GLN B 2 125 ? 40.090 -30.926 -75.706 1.00 73.55 ? 125 GLN B N 1 ATOM 3549 C CA . GLN B 2 125 ? 38.970 -31.031 -76.640 1.00 74.78 ? 125 GLN B CA 1 ATOM 3550 C C . GLN B 2 125 ? 39.298 -30.364 -77.950 1.00 73.96 ? 125 GLN B C 1 ATOM 3551 O O . GLN B 2 125 ? 39.184 -30.967 -79.010 1.00 78.11 ? 125 GLN B O 1 ATOM 3552 C CB . GLN B 2 125 ? 37.727 -30.360 -76.077 1.00 75.00 ? 125 GLN B CB 1 ATOM 3553 C CG . GLN B 2 125 ? 37.085 -31.124 -74.944 1.00 78.91 ? 125 GLN B CG 1 ATOM 3554 C CD . GLN B 2 125 ? 35.715 -30.589 -74.628 1.00 80.55 ? 125 GLN B CD 1 ATOM 3555 O OE1 . GLN B 2 125 ? 34.723 -31.071 -75.168 1.00 86.35 ? 125 GLN B OE1 1 ATOM 3556 N NE2 . GLN B 2 125 ? 35.650 -29.564 -73.782 1.00 77.86 ? 125 GLN B NE2 1 ATOM 3557 N N . LEU B 2 126 ? 39.695 -29.103 -77.875 1.00 71.47 ? 126 LEU B N 1 ATOM 3558 C CA . LEU B 2 126 ? 39.976 -28.346 -79.077 1.00 73.06 ? 126 LEU B CA 1 ATOM 3559 C C . LEU B 2 126 ? 41.129 -28.955 -79.860 1.00 77.54 ? 126 LEU B C 1 ATOM 3560 O O . LEU B 2 126 ? 41.049 -29.064 -81.073 1.00 82.74 ? 126 LEU B O 1 ATOM 3561 C CB . LEU B 2 126 ? 40.250 -26.878 -78.750 1.00 68.89 ? 126 LEU B CB 1 ATOM 3562 C CG . LEU B 2 126 ? 39.073 -26.151 -78.095 1.00 66.60 ? 126 LEU B CG 1 ATOM 3563 C CD1 . LEU B 2 126 ? 39.386 -24.677 -77.939 1.00 64.71 ? 126 LEU B CD1 1 ATOM 3564 C CD2 . LEU B 2 126 ? 37.791 -26.337 -78.889 1.00 69.37 ? 126 LEU B CD2 1 ATOM 3565 N N . ARG B 2 127 ? 42.187 -29.369 -79.172 1.00 83.21 ? 127 ARG B N 1 ATOM 3566 C CA . ARG B 2 127 ? 43.356 -29.951 -79.844 1.00 89.34 ? 127 ARG B CA 1 ATOM 3567 C C . ARG B 2 127 ? 43.862 -28.988 -80.937 1.00 88.37 ? 127 ARG B C 1 ATOM 3568 O O . ARG B 2 127 ? 44.058 -27.808 -80.656 1.00 88.20 ? 127 ARG B O 1 ATOM 3569 C CB . ARG B 2 127 ? 43.034 -31.359 -80.383 1.00 95.59 ? 127 ARG B CB 1 ATOM 3570 C CG . ARG B 2 127 ? 42.709 -32.381 -79.294 1.00 97.71 ? 127 ARG B CG 1 ATOM 3571 C CD . ARG B 2 127 ? 41.794 -33.496 -79.788 1.00 101.68 ? 127 ARG B CD 1 ATOM 3572 N NE . ARG B 2 127 ? 42.396 -34.294 -80.856 1.00 107.60 ? 127 ARG B NE 1 ATOM 3573 C CZ . ARG B 2 127 ? 41.804 -35.331 -81.454 1.00 115.54 ? 127 ARG B CZ 1 ATOM 3574 N NH1 . ARG B 2 127 ? 40.580 -35.711 -81.095 1.00 118.22 ? 127 ARG B NH1 1 ATOM 3575 N NH2 . ARG B 2 127 ? 42.440 -36.001 -82.417 1.00 119.10 ? 127 ARG B NH2 1 ATOM 3576 N N . ASP B 2 128 ? 44.038 -29.455 -82.172 1.00 90.74 ? 128 ASP B N 1 ATOM 3577 C CA . ASP B 2 128 ? 44.598 -28.599 -83.225 1.00 92.16 ? 128 ASP B CA 1 ATOM 3578 C C . ASP B 2 128 ? 43.544 -27.850 -84.071 1.00 88.17 ? 128 ASP B C 1 ATOM 3579 O O . ASP B 2 128 ? 43.878 -27.294 -85.113 1.00 88.79 ? 128 ASP B O 1 ATOM 3580 C CB . ASP B 2 128 ? 45.549 -29.408 -84.121 1.00 98.47 ? 128 ASP B CB 1 ATOM 3581 C CG . ASP B 2 128 ? 44.820 -30.401 -85.012 1.00 104.08 ? 128 ASP B CG 1 ATOM 3582 O OD1 . ASP B 2 128 ? 43.675 -30.775 -84.681 1.00 104.74 ? 128 ASP B OD1 1 ATOM 3583 O OD2 . ASP B 2 128 ? 45.392 -30.803 -86.050 1.00 111.69 ? 128 ASP B OD2 1 ATOM 3584 N N . ASN B 2 129 ? 42.287 -27.826 -83.618 1.00 86.05 ? 129 ASN B N 1 ATOM 3585 C CA . ASN B 2 129 ? 41.233 -27.016 -84.255 1.00 83.65 ? 129 ASN B CA 1 ATOM 3586 C C . ASN B 2 129 ? 41.199 -25.548 -83.799 1.00 80.40 ? 129 ASN B C 1 ATOM 3587 O O . ASN B 2 129 ? 40.298 -24.800 -84.201 1.00 80.31 ? 129 ASN B O 1 ATOM 3588 C CB . ASN B 2 129 ? 39.849 -27.629 -83.996 1.00 87.02 ? 129 ASN B CB 1 ATOM 3589 C CG . ASN B 2 129 ? 39.594 -28.887 -84.806 1.00 93.61 ? 129 ASN B CG 1 ATOM 3590 O OD1 . ASN B 2 129 ? 40.504 -29.456 -85.412 1.00 102.95 ? 129 ASN B OD1 1 ATOM 3591 N ND2 . ASN B 2 129 ? 38.342 -29.335 -84.812 1.00 93.68 ? 129 ASN B ND2 1 ATOM 3592 N N . ALA B 2 130 ? 42.166 -25.139 -82.971 1.00 77.51 ? 130 ALA B N 1 ATOM 3593 C CA . ALA B 2 130 ? 42.233 -23.771 -82.444 1.00 73.90 ? 130 ALA B CA 1 ATOM 3594 C C . ALA B 2 130 ? 43.669 -23.391 -82.121 1.00 73.65 ? 130 ALA B C 1 ATOM 3595 O O . ALA B 2 130 ? 44.478 -24.262 -81.831 1.00 77.81 ? 130 ALA B O 1 ATOM 3596 C CB . ALA B 2 130 ? 41.382 -23.655 -81.190 1.00 71.79 ? 130 ALA B CB 1 ATOM 3597 N N . LYS B 2 131 ? 43.981 -22.098 -82.157 1.00 73.00 ? 131 LYS B N 1 ATOM 3598 C CA . LYS B 2 131 ? 45.299 -21.612 -81.739 1.00 74.97 ? 131 LYS B CA 1 ATOM 3599 C C . LYS B 2 131 ? 45.333 -21.321 -80.242 1.00 71.64 ? 131 LYS B C 1 ATOM 3600 O O . LYS B 2 131 ? 44.492 -20.592 -79.719 1.00 69.06 ? 131 LYS B O 1 ATOM 3601 C CB . LYS B 2 131 ? 45.692 -20.355 -82.511 1.00 81.35 ? 131 LYS B CB 1 ATOM 3602 C CG . LYS B 2 131 ? 46.006 -20.634 -83.967 1.00 88.30 ? 131 LYS B CG 1 ATOM 3603 C CD . LYS B 2 131 ? 46.390 -19.385 -84.748 1.00 96.28 ? 131 LYS B CD 1 ATOM 3604 C CE . LYS B 2 131 ? 45.172 -18.676 -85.330 1.00 97.91 ? 131 LYS B CE 1 ATOM 3605 N NZ . LYS B 2 131 ? 45.559 -17.557 -86.237 1.00 101.29 ? 131 LYS B NZ 1 ATOM 3606 N N . GLU B 2 132 ? 46.311 -21.899 -79.556 1.00 70.34 ? 132 GLU B N 1 ATOM 3607 C CA . GLU B 2 132 ? 46.529 -21.630 -78.149 1.00 66.58 ? 132 GLU B CA 1 ATOM 3608 C C . GLU B 2 132 ? 47.286 -20.306 -78.016 1.00 66.99 ? 132 GLU B C 1 ATOM 3609 O O . GLU B 2 132 ? 48.494 -20.245 -78.236 1.00 69.90 ? 132 GLU B O 1 ATOM 3610 C CB . GLU B 2 132 ? 47.314 -22.776 -77.532 1.00 67.27 ? 132 GLU B CB 1 ATOM 3611 C CG . GLU B 2 132 ? 47.324 -22.774 -76.017 1.00 66.16 ? 132 GLU B CG 1 ATOM 3612 C CD . GLU B 2 132 ? 48.018 -23.988 -75.425 1.00 68.91 ? 132 GLU B CD 1 ATOM 3613 O OE1 . GLU B 2 132 ? 48.567 -24.820 -76.191 1.00 70.84 ? 132 GLU B OE1 1 ATOM 3614 O OE2 . GLU B 2 132 ? 48.008 -24.106 -74.180 1.00 69.34 ? 132 GLU B OE2 1 ATOM 3615 N N . LEU B 2 133 ? 46.571 -19.245 -77.661 1.00 64.91 ? 133 LEU B N 1 ATOM 3616 C CA . LEU B 2 133 ? 47.152 -17.897 -77.661 1.00 65.79 ? 133 LEU B CA 1 ATOM 3617 C C . LEU B 2 133 ? 48.203 -17.657 -76.585 1.00 66.06 ? 133 LEU B C 1 ATOM 3618 O O . LEU B 2 133 ? 49.059 -16.796 -76.757 1.00 68.37 ? 133 LEU B O 1 ATOM 3619 C CB . LEU B 2 133 ? 46.050 -16.836 -77.552 1.00 64.97 ? 133 LEU B CB 1 ATOM 3620 C CG . LEU B 2 133 ? 45.456 -16.297 -78.859 1.00 66.73 ? 133 LEU B CG 1 ATOM 3621 C CD1 . LEU B 2 133 ? 45.705 -17.191 -80.069 1.00 67.72 ? 133 LEU B CD1 1 ATOM 3622 C CD2 . LEU B 2 133 ? 43.965 -16.042 -78.690 1.00 66.08 ? 133 LEU B CD2 1 ATOM 3623 N N . GLY B 2 134 ? 48.126 -18.400 -75.482 1.00 63.99 ? 134 GLY B N 1 ATOM 3624 C CA . GLY B 2 134 ? 49.110 -18.295 -74.398 1.00 64.89 ? 134 GLY B CA 1 ATOM 3625 C C . GLY B 2 134 ? 48.679 -17.455 -73.203 1.00 63.91 ? 134 GLY B C 1 ATOM 3626 O O . GLY B 2 134 ? 49.471 -17.229 -72.283 1.00 64.90 ? 134 GLY B O 1 ATOM 3627 N N . ASN B 2 135 ? 47.426 -17.007 -73.204 1.00 61.57 ? 135 ASN B N 1 ATOM 3628 C CA . ASN B 2 135 ? 46.908 -16.130 -72.152 1.00 61.51 ? 135 ASN B CA 1 ATOM 3629 C C . ASN B 2 135 ? 45.588 -16.632 -71.557 1.00 58.91 ? 135 ASN B C 1 ATOM 3630 O O . ASN B 2 135 ? 44.894 -15.893 -70.857 1.00 56.68 ? 135 ASN B O 1 ATOM 3631 C CB . ASN B 2 135 ? 46.696 -14.739 -72.728 1.00 64.15 ? 135 ASN B CB 1 ATOM 3632 C CG . ASN B 2 135 ? 45.712 -14.740 -73.875 1.00 64.21 ? 135 ASN B CG 1 ATOM 3633 O OD1 . ASN B 2 135 ? 45.290 -15.798 -74.348 1.00 63.22 ? 135 ASN B OD1 1 ATOM 3634 N ND2 . ASN B 2 135 ? 45.345 -13.562 -74.333 1.00 67.40 ? 135 ASN B ND2 1 ATOM 3635 N N . GLY B 2 136 ? 45.247 -17.886 -71.843 1.00 57.45 ? 136 GLY B N 1 ATOM 3636 C CA . GLY B 2 136 ? 43.988 -18.460 -71.404 1.00 55.25 ? 136 GLY B CA 1 ATOM 3637 C C . GLY B 2 136 ? 42.964 -18.589 -72.511 1.00 53.61 ? 136 GLY B C 1 ATOM 3638 O O . GLY B 2 136 ? 41.917 -19.198 -72.310 1.00 51.82 ? 136 GLY B O 1 ATOM 3639 N N . CYS B 2 137 ? 43.270 -18.037 -73.681 1.00 55.87 ? 137 CYS B N 1 ATOM 3640 C CA . CYS B 2 137 ? 42.326 -18.026 -74.790 1.00 57.33 ? 137 CYS B CA 1 ATOM 3641 C C . CYS B 2 137 ? 42.737 -18.929 -75.938 1.00 57.47 ? 137 CYS B C 1 ATOM 3642 O O . CYS B 2 137 ? 43.920 -19.180 -76.172 1.00 58.57 ? 137 CYS B O 1 ATOM 3643 C CB . CYS B 2 137 ? 42.145 -16.613 -75.313 1.00 60.02 ? 137 CYS B CB 1 ATOM 3644 S SG . CYS B 2 137 ? 41.582 -15.458 -74.056 1.00 64.23 ? 137 CYS B SG 1 ATOM 3645 N N . PHE B 2 138 ? 41.720 -19.401 -76.646 1.00 57.68 ? 138 PHE B N 1 ATOM 3646 C CA . PHE B 2 138 ? 41.874 -20.220 -77.822 1.00 58.56 ? 138 PHE B CA 1 ATOM 3647 C C . PHE B 2 138 ? 41.154 -19.519 -78.959 1.00 60.69 ? 138 PHE B C 1 ATOM 3648 O O . PHE B 2 138 ? 39.968 -19.259 -78.864 1.00 60.97 ? 138 PHE B O 1 ATOM 3649 C CB . PHE B 2 138 ? 41.238 -21.593 -77.601 1.00 57.79 ? 138 PHE B CB 1 ATOM 3650 C CG . PHE B 2 138 ? 41.898 -22.400 -76.522 1.00 58.19 ? 138 PHE B CG 1 ATOM 3651 C CD1 . PHE B 2 138 ? 42.983 -23.223 -76.813 1.00 58.20 ? 138 PHE B CD1 1 ATOM 3652 C CD2 . PHE B 2 138 ? 41.432 -22.345 -75.212 1.00 58.62 ? 138 PHE B CD2 1 ATOM 3653 C CE1 . PHE B 2 138 ? 43.590 -23.970 -75.819 1.00 58.76 ? 138 PHE B CE1 1 ATOM 3654 C CE2 . PHE B 2 138 ? 42.038 -23.092 -74.212 1.00 57.86 ? 138 PHE B CE2 1 ATOM 3655 C CZ . PHE B 2 138 ? 43.120 -23.900 -74.516 1.00 58.53 ? 138 PHE B CZ 1 ATOM 3656 N N . GLU B 2 139 ? 41.874 -19.224 -80.032 1.00 63.78 ? 139 GLU B N 1 ATOM 3657 C CA . GLU B 2 139 ? 41.295 -18.620 -81.210 1.00 65.48 ? 139 GLU B CA 1 ATOM 3658 C C . GLU B 2 139 ? 41.005 -19.716 -82.232 1.00 66.70 ? 139 GLU B C 1 ATOM 3659 O O . GLU B 2 139 ? 41.904 -20.463 -82.617 1.00 66.29 ? 139 GLU B O 1 ATOM 3660 C CB . GLU B 2 139 ? 42.264 -17.600 -81.777 1.00 69.67 ? 139 GLU B CB 1 ATOM 3661 C CG . GLU B 2 139 ? 41.781 -16.909 -83.033 1.00 75.05 ? 139 GLU B CG 1 ATOM 3662 C CD . GLU B 2 139 ? 42.884 -16.108 -83.681 1.00 83.20 ? 139 GLU B CD 1 ATOM 3663 O OE1 . GLU B 2 139 ? 43.538 -15.314 -82.964 1.00 88.85 ? 139 GLU B OE1 1 ATOM 3664 O OE2 . GLU B 2 139 ? 43.104 -16.280 -84.902 1.00 89.87 ? 139 GLU B OE2 1 ATOM 3665 N N . PHE B 2 140 ? 39.750 -19.795 -82.676 1.00 68.52 ? 140 PHE B N 1 ATOM 3666 C CA . PHE B 2 140 ? 39.289 -20.872 -83.556 1.00 69.52 ? 140 PHE B CA 1 ATOM 3667 C C . PHE B 2 140 ? 39.705 -20.683 -85.011 1.00 72.58 ? 140 PHE B C 1 ATOM 3668 O O . PHE B 2 140 ? 39.802 -19.556 -85.494 1.00 71.63 ? 140 PHE B O 1 ATOM 3669 C CB . PHE B 2 140 ? 37.766 -20.982 -83.501 1.00 67.75 ? 140 PHE B CB 1 ATOM 3670 C CG . PHE B 2 140 ? 37.247 -21.513 -82.207 1.00 66.01 ? 140 PHE B CG 1 ATOM 3671 C CD1 . PHE B 2 140 ? 37.021 -20.665 -81.136 1.00 65.14 ? 140 PHE B CD1 1 ATOM 3672 C CD2 . PHE B 2 140 ? 36.979 -22.863 -82.057 1.00 66.77 ? 140 PHE B CD2 1 ATOM 3673 C CE1 . PHE B 2 140 ? 36.530 -21.154 -79.941 1.00 64.73 ? 140 PHE B CE1 1 ATOM 3674 C CE2 . PHE B 2 140 ? 36.492 -23.364 -80.860 1.00 66.39 ? 140 PHE B CE2 1 ATOM 3675 C CZ . PHE B 2 140 ? 36.269 -22.508 -79.801 1.00 65.40 ? 140 PHE B CZ 1 ATOM 3676 N N . TYR B 2 141 ? 39.931 -21.794 -85.710 1.00 76.34 ? 141 TYR B N 1 ATOM 3677 C CA . TYR B 2 141 ? 40.203 -21.742 -87.155 1.00 80.77 ? 141 TYR B CA 1 ATOM 3678 C C . TYR B 2 141 ? 38.929 -21.592 -87.970 1.00 81.02 ? 141 TYR B C 1 ATOM 3679 O O . TYR B 2 141 ? 38.964 -21.090 -89.089 1.00 86.73 ? 141 TYR B O 1 ATOM 3680 C CB . TYR B 2 141 ? 40.964 -22.980 -87.621 1.00 80.89 ? 141 TYR B CB 1 ATOM 3681 C CG . TYR B 2 141 ? 42.343 -23.052 -87.039 1.00 82.00 ? 141 TYR B CG 1 ATOM 3682 C CD1 . TYR B 2 141 ? 43.253 -22.016 -87.234 1.00 83.13 ? 141 TYR B CD1 1 ATOM 3683 C CD2 . TYR B 2 141 ? 42.735 -24.138 -86.268 1.00 82.95 ? 141 TYR B CD2 1 ATOM 3684 C CE1 . TYR B 2 141 ? 44.520 -22.073 -86.693 1.00 85.65 ? 141 TYR B CE1 1 ATOM 3685 C CE2 . TYR B 2 141 ? 44.000 -24.203 -85.720 1.00 84.29 ? 141 TYR B CE2 1 ATOM 3686 C CZ . TYR B 2 141 ? 44.886 -23.171 -85.937 1.00 86.50 ? 141 TYR B CZ 1 ATOM 3687 O OH . TYR B 2 141 ? 46.144 -23.243 -85.393 1.00 91.03 ? 141 TYR B OH 1 ATOM 3688 N N . HIS B 2 142 ? 37.816 -22.029 -87.398 1.00 98.87 ? 142 HIS B N 1 ATOM 3689 C CA . HIS B 2 142 ? 36.516 -21.953 -88.044 1.00 100.94 ? 142 HIS B CA 1 ATOM 3690 C C . HIS B 2 142 ? 35.650 -20.968 -87.276 1.00 97.59 ? 142 HIS B C 1 ATOM 3691 O O . HIS B 2 142 ? 35.937 -20.653 -86.120 1.00 92.82 ? 142 HIS B O 1 ATOM 3692 C CB . HIS B 2 142 ? 35.858 -23.334 -88.045 1.00 103.11 ? 142 HIS B CB 1 ATOM 3693 C CG . HIS B 2 142 ? 35.733 -23.946 -86.683 1.00 100.28 ? 142 HIS B CG 1 ATOM 3694 N ND1 . HIS B 2 142 ? 34.610 -23.792 -85.897 1.00 98.43 ? 142 HIS B ND1 1 ATOM 3695 C CD2 . HIS B 2 142 ? 36.599 -24.694 -85.958 1.00 98.91 ? 142 HIS B CD2 1 ATOM 3696 C CE1 . HIS B 2 142 ? 34.785 -24.432 -84.754 1.00 95.79 ? 142 HIS B CE1 1 ATOM 3697 N NE2 . HIS B 2 142 ? 35.984 -24.985 -84.764 1.00 95.82 ? 142 HIS B NE2 1 ATOM 3698 N N . LYS B 2 143 ? 34.594 -20.473 -87.906 1.00 99.89 ? 143 LYS B N 1 ATOM 3699 C CA . LYS B 2 143 ? 33.638 -19.653 -87.175 1.00 99.29 ? 143 LYS B CA 1 ATOM 3700 C C . LYS B 2 143 ? 32.960 -20.545 -86.141 1.00 95.52 ? 143 LYS B C 1 ATOM 3701 O O . LYS B 2 143 ? 32.575 -21.676 -86.451 1.00 98.48 ? 143 LYS B O 1 ATOM 3702 C CB . LYS B 2 143 ? 32.598 -19.021 -88.096 1.00 104.78 ? 143 LYS B CB 1 ATOM 3703 C CG . LYS B 2 143 ? 33.189 -18.194 -89.228 1.00 111.07 ? 143 LYS B CG 1 ATOM 3704 C CD . LYS B 2 143 ? 32.232 -17.120 -89.731 1.00 114.90 ? 143 LYS B CD 1 ATOM 3705 C CE . LYS B 2 143 ? 30.842 -17.658 -90.062 1.00 118.96 ? 143 LYS B CE 1 ATOM 3706 N NZ . LYS B 2 143 ? 29.917 -17.705 -88.887 1.00 116.18 ? 143 LYS B NZ 1 ATOM 3707 N N . CYS B 2 144 ? 32.846 -20.040 -84.915 1.00 88.09 ? 144 CYS B N 1 ATOM 3708 C CA . CYS B 2 144 ? 32.260 -20.789 -83.811 1.00 83.64 ? 144 CYS B CA 1 ATOM 3709 C C . CYS B 2 144 ? 31.109 -19.961 -83.240 1.00 81.15 ? 144 CYS B C 1 ATOM 3710 O O . CYS B 2 144 ? 31.335 -18.999 -82.504 1.00 78.60 ? 144 CYS B O 1 ATOM 3711 C CB . CYS B 2 144 ? 33.340 -21.077 -82.758 1.00 80.27 ? 144 CYS B CB 1 ATOM 3712 S SG . CYS B 2 144 ? 32.902 -22.217 -81.420 1.00 79.79 ? 144 CYS B SG 1 ATOM 3713 N N . ASP B 2 145 ? 29.878 -20.320 -83.608 1.00 82.95 ? 145 ASP B N 1 ATOM 3714 C CA . ASP B 2 145 ? 28.682 -19.601 -83.144 1.00 83.90 ? 145 ASP B CA 1 ATOM 3715 C C . ASP B 2 145 ? 28.331 -20.017 -81.710 1.00 81.87 ? 145 ASP B C 1 ATOM 3716 O O . ASP B 2 145 ? 29.067 -20.786 -81.091 1.00 81.18 ? 145 ASP B O 1 ATOM 3717 C CB . ASP B 2 145 ? 27.496 -19.797 -84.109 1.00 88.80 ? 145 ASP B CB 1 ATOM 3718 C CG . ASP B 2 145 ? 27.016 -21.244 -84.193 1.00 92.35 ? 145 ASP B CG 1 ATOM 3719 O OD1 . ASP B 2 145 ? 27.557 -22.116 -83.483 1.00 91.30 ? 145 ASP B OD1 1 ATOM 3720 O OD2 . ASP B 2 145 ? 26.090 -21.510 -84.987 1.00 97.44 ? 145 ASP B OD2 1 ATOM 3721 N N . ASN B 2 146 ? 27.225 -19.509 -81.174 1.00 81.41 ? 146 ASN B N 1 ATOM 3722 C CA . ASN B 2 146 ? 26.887 -19.770 -79.772 1.00 79.76 ? 146 ASN B CA 1 ATOM 3723 C C . ASN B 2 146 ? 26.639 -21.250 -79.478 1.00 82.07 ? 146 ASN B C 1 ATOM 3724 O O . ASN B 2 146 ? 27.026 -21.747 -78.425 1.00 81.39 ? 146 ASN B O 1 ATOM 3725 C CB . ASN B 2 146 ? 25.696 -18.914 -79.329 1.00 80.11 ? 146 ASN B CB 1 ATOM 3726 C CG . ASN B 2 146 ? 25.973 -17.419 -79.427 1.00 77.46 ? 146 ASN B CG 1 ATOM 3727 O OD1 . ASN B 2 146 ? 27.120 -16.969 -79.454 1.00 74.15 ? 146 ASN B OD1 1 ATOM 3728 N ND2 . ASN B 2 146 ? 24.914 -16.645 -79.487 1.00 80.67 ? 146 ASN B ND2 1 ATOM 3729 N N . GLU B 2 147 ? 26.019 -21.957 -80.414 1.00 88.69 ? 147 GLU B N 1 ATOM 3730 C CA . GLU B 2 147 ? 25.870 -23.415 -80.309 1.00 93.77 ? 147 GLU B CA 1 ATOM 3731 C C . GLU B 2 147 ? 27.230 -24.122 -80.238 1.00 89.48 ? 147 GLU B C 1 ATOM 3732 O O . GLU B 2 147 ? 27.420 -25.062 -79.464 1.00 89.41 ? 147 GLU B O 1 ATOM 3733 C CB . GLU B 2 147 ? 25.083 -23.959 -81.506 1.00 101.99 ? 147 GLU B CB 1 ATOM 3734 C CG . GLU B 2 147 ? 23.604 -23.601 -81.519 1.00 108.67 ? 147 GLU B CG 1 ATOM 3735 C CD . GLU B 2 147 ? 22.782 -24.468 -80.579 1.00 114.04 ? 147 GLU B CD 1 ATOM 3736 O OE1 . GLU B 2 147 ? 22.965 -24.344 -79.347 1.00 112.28 ? 147 GLU B OE1 1 ATOM 3737 O OE2 . GLU B 2 147 ? 21.953 -25.270 -81.071 1.00 120.19 ? 147 GLU B OE2 1 ATOM 3738 N N . CYS B 2 148 ? 28.162 -23.669 -81.068 1.00 86.44 ? 148 CYS B N 1 ATOM 3739 C CA . CYS B 2 148 ? 29.522 -24.188 -81.080 1.00 84.26 ? 148 CYS B CA 1 ATOM 3740 C C . CYS B 2 148 ? 30.192 -23.906 -79.727 1.00 79.50 ? 148 CYS B C 1 ATOM 3741 O O . CYS B 2 148 ? 30.759 -24.803 -79.100 1.00 80.08 ? 148 CYS B O 1 ATOM 3742 C CB . CYS B 2 148 ? 30.286 -23.548 -82.247 1.00 85.46 ? 148 CYS B CB 1 ATOM 3743 S SG . CYS B 2 148 ? 32.063 -23.849 -82.340 1.00 88.06 ? 148 CYS B SG 1 ATOM 3744 N N . MET B 2 149 ? 30.091 -22.665 -79.263 1.00 75.28 ? 149 MET B N 1 ATOM 3745 C CA . MET B 2 149 ? 30.641 -22.292 -77.963 1.00 71.39 ? 149 MET B CA 1 ATOM 3746 C C . MET B 2 149 ? 30.066 -23.150 -76.844 1.00 72.75 ? 149 MET B C 1 ATOM 3747 O O . MET B 2 149 ? 30.808 -23.659 -76.004 1.00 70.33 ? 149 MET B O 1 ATOM 3748 C CB . MET B 2 149 ? 30.376 -20.815 -77.665 1.00 69.44 ? 149 MET B CB 1 ATOM 3749 C CG . MET B 2 149 ? 31.121 -19.846 -78.572 1.00 68.39 ? 149 MET B CG 1 ATOM 3750 S SD . MET B 2 149 ? 32.912 -20.028 -78.500 1.00 66.72 ? 149 MET B SD 1 ATOM 3751 C CE . MET B 2 149 ? 33.428 -18.704 -79.591 1.00 66.61 ? 149 MET B CE 1 ATOM 3752 N N . GLU B 2 150 ? 28.747 -23.316 -76.840 1.00 77.34 ? 150 GLU B N 1 ATOM 3753 C CA . GLU B 2 150 ? 28.082 -24.122 -75.817 1.00 80.74 ? 150 GLU B CA 1 ATOM 3754 C C . GLU B 2 150 ? 28.632 -25.547 -75.771 1.00 81.06 ? 150 GLU B C 1 ATOM 3755 O O . GLU B 2 150 ? 28.780 -26.110 -74.691 1.00 80.14 ? 150 GLU B O 1 ATOM 3756 C CB . GLU B 2 150 ? 26.564 -24.121 -76.036 1.00 87.20 ? 150 GLU B CB 1 ATOM 3757 C CG . GLU B 2 150 ? 25.756 -25.040 -75.121 1.00 93.37 ? 150 GLU B CG 1 ATOM 3758 C CD . GLU B 2 150 ? 25.854 -24.693 -73.642 1.00 93.95 ? 150 GLU B CD 1 ATOM 3759 O OE1 . GLU B 2 150 ? 26.312 -23.585 -73.293 1.00 92.23 ? 150 GLU B OE1 1 ATOM 3760 O OE2 . GLU B 2 150 ? 25.452 -25.539 -72.815 1.00 99.33 ? 150 GLU B OE2 1 ATOM 3761 N N . SER B 2 151 ? 28.953 -26.114 -76.933 1.00 82.10 ? 151 SER B N 1 ATOM 3762 C CA . SER B 2 151 ? 29.480 -27.479 -77.002 1.00 85.51 ? 151 SER B CA 1 ATOM 3763 C C . SER B 2 151 ? 30.888 -27.594 -76.414 1.00 83.41 ? 151 SER B C 1 ATOM 3764 O O . SER B 2 151 ? 31.283 -28.664 -75.941 1.00 85.74 ? 151 SER B O 1 ATOM 3765 C CB . SER B 2 151 ? 29.485 -27.992 -78.443 1.00 88.88 ? 151 SER B CB 1 ATOM 3766 O OG . SER B 2 151 ? 30.519 -27.392 -79.197 1.00 86.02 ? 151 SER B OG 1 ATOM 3767 N N . VAL B 2 152 ? 31.651 -26.503 -76.462 1.00 79.89 ? 152 VAL B N 1 ATOM 3768 C CA . VAL B 2 152 ? 32.953 -26.457 -75.803 1.00 75.46 ? 152 VAL B CA 1 ATOM 3769 C C . VAL B 2 152 ? 32.745 -26.493 -74.290 1.00 75.74 ? 152 VAL B C 1 ATOM 3770 O O . VAL B 2 152 ? 33.444 -27.213 -73.582 1.00 75.54 ? 152 VAL B O 1 ATOM 3771 C CB . VAL B 2 152 ? 33.761 -25.212 -76.211 1.00 71.91 ? 152 VAL B CB 1 ATOM 3772 C CG1 . VAL B 2 152 ? 35.079 -25.148 -75.451 1.00 70.21 ? 152 VAL B CG1 1 ATOM 3773 C CG2 . VAL B 2 152 ? 34.018 -25.231 -77.710 1.00 73.79 ? 152 VAL B CG2 1 ATOM 3774 N N . ARG B 2 153 ? 31.766 -25.740 -73.802 1.00 76.87 ? 153 ARG B N 1 ATOM 3775 C CA . ARG B 2 153 ? 31.421 -25.774 -72.381 1.00 79.60 ? 153 ARG B CA 1 ATOM 3776 C C . ARG B 2 153 ? 30.770 -27.098 -71.972 1.00 86.52 ? 153 ARG B C 1 ATOM 3777 O O . ARG B 2 153 ? 30.920 -27.528 -70.831 1.00 88.01 ? 153 ARG B O 1 ATOM 3778 C CB . ARG B 2 153 ? 30.484 -24.622 -72.024 1.00 78.56 ? 153 ARG B CB 1 ATOM 3779 C CG . ARG B 2 153 ? 31.016 -23.246 -72.370 1.00 73.94 ? 153 ARG B CG 1 ATOM 3780 C CD . ARG B 2 153 ? 30.112 -22.164 -71.808 1.00 75.11 ? 153 ARG B CD 1 ATOM 3781 N NE . ARG B 2 153 ? 30.031 -21.035 -72.728 1.00 75.04 ? 153 ARG B NE 1 ATOM 3782 C CZ . ARG B 2 153 ? 29.028 -20.799 -73.572 1.00 76.59 ? 153 ARG B CZ 1 ATOM 3783 N NH1 . ARG B 2 153 ? 27.967 -21.596 -73.623 1.00 79.08 ? 153 ARG B NH1 1 ATOM 3784 N NH2 . ARG B 2 153 ? 29.084 -19.739 -74.370 1.00 77.06 ? 153 ARG B NH2 1 ATOM 3785 N N . ASN B 2 154 ? 30.033 -27.718 -72.896 1.00 94.30 ? 154 ASN B N 1 ATOM 3786 C CA . ASN B 2 154 ? 29.410 -29.035 -72.679 1.00 102.71 ? 154 ASN B CA 1 ATOM 3787 C C . ASN B 2 154 ? 30.391 -30.134 -72.312 1.00 101.41 ? 154 ASN B C 1 ATOM 3788 O O . ASN B 2 154 ? 30.124 -30.944 -71.426 1.00 106.04 ? 154 ASN B O 1 ATOM 3789 C CB . ASN B 2 154 ? 28.713 -29.521 -73.955 1.00 111.28 ? 154 ASN B CB 1 ATOM 3790 C CG . ASN B 2 154 ? 27.315 -28.981 -74.116 1.00 122.00 ? 154 ASN B CG 1 ATOM 3791 O OD1 . ASN B 2 154 ? 26.918 -28.029 -73.449 1.00 123.72 ? 154 ASN B OD1 1 ATOM 3792 N ND2 . ASN B 2 154 ? 26.554 -29.598 -75.018 1.00 136.18 ? 154 ASN B ND2 1 ATOM 3793 N N . GLY B 2 155 ? 31.516 -30.156 -73.021 1.00 95.17 ? 155 GLY B N 1 ATOM 3794 C CA . GLY B 2 155 ? 32.359 -31.339 -73.122 1.00 93.95 ? 155 GLY B CA 1 ATOM 3795 C C . GLY B 2 155 ? 32.082 -32.064 -74.429 1.00 95.38 ? 155 GLY B C 1 ATOM 3796 O O . GLY B 2 155 ? 32.624 -33.136 -74.671 1.00 98.44 ? 155 GLY B O 1 ATOM 3797 N N . THR B 2 156 ? 31.273 -31.448 -75.288 1.00 94.22 ? 156 THR B N 1 ATOM 3798 C CA . THR B 2 156 ? 30.713 -32.094 -76.472 1.00 98.41 ? 156 THR B CA 1 ATOM 3799 C C . THR B 2 156 ? 31.364 -31.644 -77.773 1.00 96.68 ? 156 THR B C 1 ATOM 3800 O O . THR B 2 156 ? 31.060 -32.188 -78.824 1.00 101.95 ? 156 THR B O 1 ATOM 3801 C CB . THR B 2 156 ? 29.200 -31.797 -76.553 1.00 102.06 ? 156 THR B CB 1 ATOM 3802 O OG1 . THR B 2 156 ? 28.552 -32.339 -75.398 1.00 105.47 ? 156 THR B OG1 1 ATOM 3803 C CG2 . THR B 2 156 ? 28.554 -32.401 -77.801 1.00 109.09 ? 156 THR B CG2 1 ATOM 3804 N N . TYR B 2 157 ? 32.257 -30.661 -77.719 1.00 93.36 ? 157 TYR B N 1 ATOM 3805 C CA . TYR B 2 157 ? 32.831 -30.093 -78.943 1.00 93.32 ? 157 TYR B CA 1 ATOM 3806 C C . TYR B 2 157 ? 33.292 -31.179 -79.904 1.00 99.90 ? 157 TYR B C 1 ATOM 3807 O O . TYR B 2 157 ? 34.311 -31.835 -79.675 1.00 99.50 ? 157 TYR B O 1 ATOM 3808 C CB . TYR B 2 157 ? 34.004 -29.171 -78.631 1.00 87.62 ? 157 TYR B CB 1 ATOM 3809 C CG . TYR B 2 157 ? 34.665 -28.618 -79.874 1.00 85.98 ? 157 TYR B CG 1 ATOM 3810 C CD1 . TYR B 2 157 ? 34.069 -27.596 -80.607 1.00 84.64 ? 157 TYR B CD1 1 ATOM 3811 C CD2 . TYR B 2 157 ? 35.881 -29.121 -80.320 1.00 86.10 ? 157 TYR B CD2 1 ATOM 3812 C CE1 . TYR B 2 157 ? 34.673 -27.085 -81.743 1.00 84.29 ? 157 TYR B CE1 1 ATOM 3813 C CE2 . TYR B 2 157 ? 36.491 -28.616 -81.456 1.00 85.84 ? 157 TYR B CE2 1 ATOM 3814 C CZ . TYR B 2 157 ? 35.886 -27.600 -82.162 1.00 84.64 ? 157 TYR B CZ 1 ATOM 3815 O OH . TYR B 2 157 ? 36.498 -27.103 -83.287 1.00 84.70 ? 157 TYR B OH 1 ATOM 3816 N N . ASP B 2 158 ? 32.535 -31.346 -80.983 1.00 107.62 ? 158 ASP B N 1 ATOM 3817 C CA . ASP B 2 158 ? 32.756 -32.427 -81.933 1.00 116.83 ? 158 ASP B CA 1 ATOM 3818 C C . ASP B 2 158 ? 33.966 -32.112 -82.811 1.00 118.32 ? 158 ASP B C 1 ATOM 3819 O O . ASP B 2 158 ? 33.858 -31.418 -83.829 1.00 118.80 ? 158 ASP B O 1 ATOM 3820 C CB . ASP B 2 158 ? 31.496 -32.657 -82.781 1.00 122.64 ? 158 ASP B CB 1 ATOM 3821 C CG . ASP B 2 158 ? 31.493 -34.001 -83.470 1.00 130.05 ? 158 ASP B CG 1 ATOM 3822 O OD1 . ASP B 2 158 ? 32.280 -34.884 -83.073 1.00 130.99 ? 158 ASP B OD1 1 ATOM 3823 O OD2 . ASP B 2 158 ? 30.695 -34.179 -84.411 1.00 138.08 ? 158 ASP B OD2 1 ATOM 3824 N N . TYR B 2 159 ? 35.119 -32.632 -82.397 1.00 120.56 ? 159 TYR B N 1 ATOM 3825 C CA . TYR B 2 159 ? 36.394 -32.312 -83.033 1.00 121.45 ? 159 TYR B CA 1 ATOM 3826 C C . TYR B 2 159 ? 36.432 -32.682 -84.527 1.00 129.29 ? 159 TYR B C 1 ATOM 3827 O O . TYR B 2 159 ? 36.767 -31.831 -85.355 1.00 129.57 ? 159 TYR B O 1 ATOM 3828 C CB . TYR B 2 159 ? 37.558 -32.947 -82.251 1.00 120.16 ? 159 TYR B CB 1 ATOM 3829 C CG . TYR B 2 159 ? 38.867 -32.975 -83.000 1.00 121.41 ? 159 TYR B CG 1 ATOM 3830 C CD1 . TYR B 2 159 ? 39.190 -34.041 -83.843 1.00 127.36 ? 159 TYR B CD1 1 ATOM 3831 C CD2 . TYR B 2 159 ? 39.782 -31.937 -82.870 1.00 116.21 ? 159 TYR B CD2 1 ATOM 3832 C CE1 . TYR B 2 159 ? 40.386 -34.067 -84.536 1.00 128.79 ? 159 TYR B CE1 1 ATOM 3833 C CE2 . TYR B 2 159 ? 40.982 -31.954 -83.556 1.00 118.80 ? 159 TYR B CE2 1 ATOM 3834 C CZ . TYR B 2 159 ? 41.280 -33.022 -84.388 1.00 124.96 ? 159 TYR B CZ 1 ATOM 3835 O OH . TYR B 2 159 ? 42.472 -33.051 -85.073 1.00 126.92 ? 159 TYR B OH 1 ATOM 3836 N N . PRO B 2 160 ? 36.080 -33.937 -84.882 1.00 138.61 ? 160 PRO B N 1 ATOM 3837 C CA . PRO B 2 160 ? 36.063 -34.310 -86.311 1.00 146.28 ? 160 PRO B CA 1 ATOM 3838 C C . PRO B 2 160 ? 35.113 -33.485 -87.204 1.00 146.72 ? 160 PRO B C 1 ATOM 3839 O O . PRO B 2 160 ? 35.302 -33.450 -88.421 1.00 150.65 ? 160 PRO B O 1 ATOM 3840 C CB . PRO B 2 160 ? 35.632 -35.785 -86.288 1.00 153.05 ? 160 PRO B CB 1 ATOM 3841 C CG . PRO B 2 160 ? 36.003 -36.271 -84.928 1.00 149.82 ? 160 PRO B CG 1 ATOM 3842 C CD . PRO B 2 160 ? 35.781 -35.097 -84.019 1.00 141.72 ? 160 PRO B CD 1 ATOM 3843 N N . GLN B 2 161 ? 34.108 -32.839 -86.611 1.00 143.30 ? 161 GLN B N 1 ATOM 3844 C CA . GLN B 2 161 ? 33.187 -31.980 -87.365 1.00 143.32 ? 161 GLN B CA 1 ATOM 3845 C C . GLN B 2 161 ? 33.886 -30.730 -87.908 1.00 136.45 ? 161 GLN B C 1 ATOM 3846 O O . GLN B 2 161 ? 33.495 -30.203 -88.951 1.00 139.63 ? 161 GLN B O 1 ATOM 3847 C CB . GLN B 2 161 ? 31.995 -31.568 -86.492 1.00 141.86 ? 161 GLN B CB 1 ATOM 3848 C CG . GLN B 2 161 ? 30.806 -31.018 -87.269 1.00 144.59 ? 161 GLN B CG 1 ATOM 3849 C CD . GLN B 2 161 ? 29.674 -30.561 -86.366 1.00 143.04 ? 161 GLN B CD 1 ATOM 3850 O OE1 . GLN B 2 161 ? 29.682 -30.810 -85.159 1.00 139.68 ? 161 GLN B OE1 1 ATOM 3851 N NE2 . GLN B 2 161 ? 28.691 -29.886 -86.949 1.00 145.89 ? 161 GLN B NE2 1 ATOM 3852 N N . TYR B 2 162 ? 34.908 -30.261 -87.195 1.00 126.20 ? 162 TYR B N 1 ATOM 3853 C CA . TYR B 2 162 ? 35.693 -29.112 -87.626 1.00 121.02 ? 162 TYR B CA 1 ATOM 3854 C C . TYR B 2 162 ? 37.161 -29.499 -87.770 1.00 118.11 ? 162 TYR B C 1 ATOM 3855 O O . TYR B 2 162 ? 37.622 -29.865 -88.847 1.00 119.33 ? 162 TYR B O 1 ATOM 3856 C CB . TYR B 2 162 ? 35.575 -27.971 -86.613 1.00 115.53 ? 162 TYR B CB 1 ATOM 3857 C CG . TYR B 2 162 ? 34.168 -27.651 -86.136 1.00 115.90 ? 162 TYR B CG 1 ATOM 3858 C CD1 . TYR B 2 162 ? 33.329 -26.812 -86.871 1.00 117.69 ? 162 TYR B CD1 1 ATOM 3859 C CD2 . TYR B 2 162 ? 33.690 -28.158 -84.928 1.00 114.72 ? 162 TYR B CD2 1 ATOM 3860 C CE1 . TYR B 2 162 ? 32.050 -26.503 -86.424 1.00 117.69 ? 162 TYR B CE1 1 ATOM 3861 C CE2 . TYR B 2 162 ? 32.413 -27.855 -84.473 1.00 114.63 ? 162 TYR B CE2 1 ATOM 3862 C CZ . TYR B 2 162 ? 31.596 -27.028 -85.220 1.00 115.98 ? 162 TYR B CZ 1 ATOM 3863 O OH . TYR B 2 162 ? 30.329 -26.729 -84.763 1.00 114.78 ? 162 TYR B OH 1 HETATM 3864 C C1 . NAG C 3 . ? 31.295 -3.755 -53.989 1.00 111.48 ? 1011 NAG A C1 1 HETATM 3865 C C2 . NAG C 3 . ? 30.668 -2.474 -53.425 1.00 122.79 ? 1011 NAG A C2 1 HETATM 3866 C C3 . NAG C 3 . ? 29.273 -2.735 -52.851 1.00 127.58 ? 1011 NAG A C3 1 HETATM 3867 C C4 . NAG C 3 . ? 28.392 -3.515 -53.821 1.00 129.54 ? 1011 NAG A C4 1 HETATM 3868 C C5 . NAG C 3 . ? 29.145 -4.712 -54.409 1.00 127.32 ? 1011 NAG A C5 1 HETATM 3869 C C6 . NAG C 3 . ? 28.330 -5.388 -55.514 1.00 125.31 ? 1011 NAG A C6 1 HETATM 3870 C C7 . NAG C 3 . ? 32.475 -0.983 -52.700 1.00 124.28 ? 1011 NAG A C7 1 HETATM 3871 C C8 . NAG C 3 . ? 33.270 -0.429 -51.552 1.00 122.91 ? 1011 NAG A C8 1 HETATM 3872 N N2 . NAG C 3 . ? 31.513 -1.864 -52.408 1.00 122.34 ? 1011 NAG A N2 1 HETATM 3873 O O3 . NAG C 3 . ? 28.633 -1.512 -52.565 1.00 131.68 ? 1011 NAG A O3 1 HETATM 3874 O O4 . NAG C 3 . ? 27.219 -3.935 -53.151 1.00 127.76 ? 1011 NAG A O4 1 HETATM 3875 O O5 . NAG C 3 . ? 30.397 -4.300 -54.939 1.00 119.98 ? 1011 NAG A O5 1 HETATM 3876 O O6 . NAG C 3 . ? 28.080 -6.731 -55.167 1.00 123.52 ? 1011 NAG A O6 1 HETATM 3877 O O7 . NAG C 3 . ? 32.735 -0.615 -53.847 1.00 126.58 ? 1011 NAG A O7 1 HETATM 3878 C C1 . NAG D 3 . ? 50.028 -6.345 -43.366 1.00 80.47 ? 1023 NAG A C1 1 HETATM 3879 C C2 . NAG D 3 . ? 51.361 -5.739 -42.936 1.00 89.84 ? 1023 NAG A C2 1 HETATM 3880 C C3 . NAG D 3 . ? 51.286 -5.126 -41.533 1.00 95.06 ? 1023 NAG A C3 1 HETATM 3881 C C4 . NAG D 3 . ? 50.023 -4.305 -41.307 1.00 100.03 ? 1023 NAG A C4 1 HETATM 3882 C C5 . NAG D 3 . ? 48.813 -5.124 -41.727 1.00 96.47 ? 1023 NAG A C5 1 HETATM 3883 C C6 . NAG D 3 . ? 47.491 -4.387 -41.512 1.00 96.04 ? 1023 NAG A C6 1 HETATM 3884 C C7 . NAG D 3 . ? 53.302 -6.926 -43.915 1.00 86.26 ? 1023 NAG A C7 1 HETATM 3885 C C8 . NAG D 3 . ? 54.313 -8.026 -43.749 1.00 84.08 ? 1023 NAG A C8 1 HETATM 3886 N N2 . NAG D 3 . ? 52.403 -6.763 -42.934 1.00 91.00 ? 1023 NAG A N2 1 HETATM 3887 O O3 . NAG D 3 . ? 52.416 -4.314 -41.318 1.00 95.52 ? 1023 NAG A O3 1 HETATM 3888 O O4 . NAG D 3 . ? 49.919 -3.946 -39.939 1.00 116.80 ? 1023 NAG A O4 1 HETATM 3889 O O5 . NAG D 3 . ? 48.974 -5.440 -43.094 1.00 89.05 ? 1023 NAG A O5 1 HETATM 3890 O O6 . NAG D 3 . ? 47.484 -3.165 -42.218 1.00 96.96 ? 1023 NAG A O6 1 HETATM 3891 O O7 . NAG D 3 . ? 53.337 -6.235 -44.930 1.00 83.88 ? 1023 NAG A O7 1 HETATM 3892 C C1 . NAG E 3 . ? 50.202 -2.544 -39.744 1.00 132.25 ? 1024 NAG A C1 1 HETATM 3893 C C2 . NAG E 3 . ? 49.747 -2.110 -38.349 1.00 135.85 ? 1024 NAG A C2 1 HETATM 3894 C C3 . NAG E 3 . ? 50.328 -0.768 -37.885 1.00 140.97 ? 1024 NAG A C3 1 HETATM 3895 C C4 . NAG E 3 . ? 51.736 -0.483 -38.403 1.00 144.45 ? 1024 NAG A C4 1 HETATM 3896 C C5 . NAG E 3 . ? 51.864 -0.900 -39.863 1.00 144.37 ? 1024 NAG A C5 1 HETATM 3897 C C6 . NAG E 3 . ? 53.267 -0.667 -40.411 1.00 146.66 ? 1024 NAG A C6 1 HETATM 3898 C C7 . NAG E 3 . ? 47.501 -2.984 -37.879 1.00 133.14 ? 1024 NAG A C7 1 HETATM 3899 C C8 . NAG E 3 . ? 46.018 -2.743 -37.955 1.00 128.17 ? 1024 NAG A C8 1 HETATM 3900 N N2 . NAG E 3 . ? 48.294 -2.018 -38.349 1.00 136.49 ? 1024 NAG A N2 1 HETATM 3901 O O3 . NAG E 3 . ? 50.341 -0.722 -36.474 1.00 139.34 ? 1024 NAG A O3 1 HETATM 3902 O O4 . NAG E 3 . ? 52.008 0.895 -38.266 1.00 147.63 ? 1024 NAG A O4 1 HETATM 3903 O O5 . NAG E 3 . ? 51.573 -2.276 -39.931 1.00 137.51 ? 1024 NAG A O5 1 HETATM 3904 O O6 . NAG E 3 . ? 53.325 -1.127 -41.745 1.00 149.80 ? 1024 NAG A O6 1 HETATM 3905 O O7 . NAG E 3 . ? 47.931 -4.033 -37.399 1.00 129.15 ? 1024 NAG A O7 1 HETATM 3906 C C1 . NAG F 3 . ? 21.946 -39.880 14.169 1.00 93.67 ? 1165 NAG A C1 1 HETATM 3907 C C2 . NAG F 3 . ? 22.661 -41.191 14.471 1.00 100.57 ? 1165 NAG A C2 1 HETATM 3908 C C3 . NAG F 3 . ? 22.154 -42.303 13.566 1.00 104.62 ? 1165 NAG A C3 1 HETATM 3909 C C4 . NAG F 3 . ? 20.634 -42.384 13.611 1.00 109.93 ? 1165 NAG A C4 1 HETATM 3910 C C5 . NAG F 3 . ? 20.022 -41.014 13.326 1.00 107.63 ? 1165 NAG A C5 1 HETATM 3911 C C6 . NAG F 3 . ? 18.483 -41.010 13.331 1.00 109.67 ? 1165 NAG A C6 1 HETATM 3912 C C7 . NAG F 3 . ? 24.973 -41.294 15.303 1.00 106.35 ? 1165 NAG A C7 1 HETATM 3913 C C8 . NAG F 3 . ? 26.429 -41.100 14.987 1.00 107.36 ? 1165 NAG A C8 1 HETATM 3914 N N2 . NAG F 3 . ? 24.099 -41.042 14.321 1.00 102.65 ? 1165 NAG A N2 1 HETATM 3915 O O3 . NAG F 3 . ? 22.700 -43.538 13.969 1.00 106.19 ? 1165 NAG A O3 1 HETATM 3916 O O4 . NAG F 3 . ? 20.230 -43.315 12.633 1.00 125.45 ? 1165 NAG A O4 1 HETATM 3917 O O5 . NAG F 3 . ? 20.547 -40.090 14.256 1.00 100.33 ? 1165 NAG A O5 1 HETATM 3918 O O6 . NAG F 3 . ? 17.916 -40.531 14.536 1.00 108.35 ? 1165 NAG A O6 1 HETATM 3919 O O7 . NAG F 3 . ? 24.652 -41.669 16.431 1.00 107.33 ? 1165 NAG A O7 1 HETATM 3920 C C1 . NAG G 3 . ? 19.620 -44.476 13.227 1.00 141.35 ? 1166 NAG A C1 1 HETATM 3921 C C2 . NAG G 3 . ? 19.034 -45.322 12.111 1.00 149.49 ? 1166 NAG A C2 1 HETATM 3922 C C3 . NAG G 3 . ? 18.242 -46.474 12.713 1.00 155.75 ? 1166 NAG A C3 1 HETATM 3923 C C4 . NAG G 3 . ? 19.071 -47.256 13.739 1.00 157.88 ? 1166 NAG A C4 1 HETATM 3924 C C5 . NAG G 3 . ? 19.898 -46.344 14.658 1.00 149.92 ? 1166 NAG A C5 1 HETATM 3925 C C6 . NAG G 3 . ? 20.975 -47.148 15.385 1.00 146.58 ? 1166 NAG A C6 1 HETATM 3926 C C7 . NAG G 3 . ? 18.213 -44.569 9.922 1.00 153.88 ? 1166 NAG A C7 1 HETATM 3927 C C8 . NAG G 3 . ? 17.269 -43.669 9.176 1.00 152.58 ? 1166 NAG A C8 1 HETATM 3928 N N2 . NAG G 3 . ? 18.180 -44.509 11.257 1.00 153.83 ? 1166 NAG A N2 1 HETATM 3929 O O3 . NAG G 3 . ? 17.796 -47.310 11.666 1.00 158.57 ? 1166 NAG A O3 1 HETATM 3930 O O4 . NAG G 3 . ? 18.219 -48.049 14.554 1.00 167.45 ? 1166 NAG A O4 1 HETATM 3931 O O5 . NAG G 3 . ? 20.522 -45.279 13.959 1.00 143.14 ? 1166 NAG A O5 1 HETATM 3932 O O6 . NAG G 3 . ? 21.519 -46.370 16.426 1.00 142.50 ? 1166 NAG A O6 1 HETATM 3933 O O7 . NAG G 3 . ? 18.964 -45.313 9.289 1.00 153.49 ? 1166 NAG A O7 1 HETATM 3934 C C1 . MAN H 4 . ? 17.785 -49.312 13.988 1.00 173.63 ? 1167 MAN A C1 1 HETATM 3935 C C2 . MAN H 4 . ? 18.241 -50.419 14.947 1.00 172.65 ? 1167 MAN A C2 1 HETATM 3936 C C3 . MAN H 4 . ? 18.349 -51.780 14.255 1.00 176.65 ? 1167 MAN A C3 1 HETATM 3937 C C4 . MAN H 4 . ? 17.391 -51.816 13.068 1.00 181.17 ? 1167 MAN A C4 1 HETATM 3938 C C5 . MAN H 4 . ? 17.923 -50.829 12.036 1.00 180.41 ? 1167 MAN A C5 1 HETATM 3939 C C6 . MAN H 4 . ? 16.949 -50.715 10.869 1.00 179.51 ? 1167 MAN A C6 1 HETATM 3940 O O2 . MAN H 4 . ? 17.321 -50.483 16.046 1.00 163.30 ? 1167 MAN A O2 1 HETATM 3941 O O3 . MAN H 4 . ? 18.088 -52.863 15.165 1.00 172.61 ? 1167 MAN A O3 1 HETATM 3942 O O4 . MAN H 4 . ? 17.280 -53.117 12.475 1.00 180.19 ? 1167 MAN A O4 1 HETATM 3943 O O5 . MAN H 4 . ? 18.207 -49.550 12.630 1.00 180.37 ? 1167 MAN A O5 1 HETATM 3944 O O6 . MAN H 4 . ? 17.067 -51.920 10.095 1.00 177.81 ? 1167 MAN A O6 1 HETATM 3945 C C1 . BMA I 5 . ? 18.824 -54.040 14.765 1.00 163.24 ? 1168 BMA A C1 1 HETATM 3946 C C2 . BMA I 5 . ? 20.139 -54.118 15.531 1.00 159.28 ? 1168 BMA A C2 1 HETATM 3947 C C3 . BMA I 5 . ? 20.911 -55.353 15.077 1.00 153.72 ? 1168 BMA A C3 1 HETATM 3948 C C4 . BMA I 5 . ? 20.020 -56.592 15.146 1.00 152.11 ? 1168 BMA A C4 1 HETATM 3949 C C5 . BMA I 5 . ? 18.709 -56.358 14.387 1.00 151.75 ? 1168 BMA A C5 1 HETATM 3950 C C6 . BMA I 5 . ? 17.760 -57.561 14.394 1.00 145.30 ? 1168 BMA A C6 1 HETATM 3951 O O2 . BMA I 5 . ? 19.890 -54.170 16.920 1.00 159.41 ? 1168 BMA A O2 1 HETATM 3952 O O3 . BMA I 5 . ? 22.056 -55.531 15.880 1.00 152.59 ? 1168 BMA A O3 1 HETATM 3953 O O4 . BMA I 5 . ? 20.715 -57.706 14.627 1.00 146.29 ? 1168 BMA A O4 1 HETATM 3954 O O5 . BMA I 5 . ? 18.073 -55.224 14.951 1.00 158.64 ? 1168 BMA A O5 1 HETATM 3955 O O6 . BMA I 5 . ? 16.652 -57.337 15.240 1.00 135.77 ? 1168 BMA A O6 1 HETATM 3956 C C1 . MAN J 4 . ? 16.255 -51.971 8.896 1.00 180.43 ? 1169 MAN A C1 1 HETATM 3957 C C2 . MAN J 4 . ? 17.014 -51.292 7.744 1.00 180.68 ? 1169 MAN A C2 1 HETATM 3958 C C3 . MAN J 4 . ? 16.565 -49.861 7.441 1.00 179.03 ? 1169 MAN A C3 1 HETATM 3959 C C4 . MAN J 4 . ? 15.048 -49.786 7.420 1.00 178.92 ? 1169 MAN A C4 1 HETATM 3960 C C5 . MAN J 4 . ? 14.520 -50.215 8.784 1.00 176.24 ? 1169 MAN A C5 1 HETATM 3961 C C6 . MAN J 4 . ? 12.995 -50.133 8.872 1.00 168.86 ? 1169 MAN A C6 1 HETATM 3962 O O2 . MAN J 4 . ? 16.894 -52.089 6.583 1.00 177.78 ? 1169 MAN A O2 1 HETATM 3963 O O3 . MAN J 4 . ? 17.089 -49.433 6.201 1.00 173.68 ? 1169 MAN A O3 1 HETATM 3964 O O4 . MAN J 4 . ? 14.644 -48.461 7.160 1.00 178.17 ? 1169 MAN A O4 1 HETATM 3965 O O5 . MAN J 4 . ? 14.902 -51.549 9.076 1.00 181.45 ? 1169 MAN A O5 1 HETATM 3966 O O6 . MAN J 4 . ? 12.407 -50.318 7.603 1.00 159.92 ? 1169 MAN A O6 1 HETATM 3967 C C1 . NAG K 3 . ? 23.659 -12.302 -30.660 1.00 126.55 ? 1286 NAG A C1 1 HETATM 3968 C C2 . NAG K 3 . ? 22.282 -11.733 -30.282 1.00 136.22 ? 1286 NAG A C2 1 HETATM 3969 C C3 . NAG K 3 . ? 21.431 -11.203 -31.458 1.00 136.49 ? 1286 NAG A C3 1 HETATM 3970 C C4 . NAG K 3 . ? 22.123 -11.073 -32.829 1.00 139.90 ? 1286 NAG A C4 1 HETATM 3971 C C5 . NAG K 3 . ? 23.436 -11.842 -32.966 1.00 136.99 ? 1286 NAG A C5 1 HETATM 3972 C C6 . NAG K 3 . ? 24.251 -11.353 -34.164 1.00 133.91 ? 1286 NAG A C6 1 HETATM 3973 C C7 . NAG K 3 . ? 21.284 -12.720 -28.242 1.00 133.83 ? 1286 NAG A C7 1 HETATM 3974 C C8 . NAG K 3 . ? 20.493 -13.857 -27.659 1.00 129.49 ? 1286 NAG A C8 1 HETATM 3975 N N2 . NAG K 3 . ? 21.527 -12.757 -29.560 1.00 135.46 ? 1286 NAG A N2 1 HETATM 3976 O O3 . NAG K 3 . ? 20.891 -9.944 -31.107 1.00 129.96 ? 1286 NAG A O3 1 HETATM 3977 O O4 . NAG K 3 . ? 21.228 -11.484 -33.844 1.00 146.18 ? 1286 NAG A O4 1 HETATM 3978 O O5 . NAG K 3 . ? 24.188 -11.638 -31.794 1.00 134.50 ? 1286 NAG A O5 1 HETATM 3979 O O6 . NAG K 3 . ? 25.132 -12.366 -34.596 1.00 129.66 ? 1286 NAG A O6 1 HETATM 3980 O O7 . NAG K 3 . ? 21.664 -11.817 -27.496 1.00 134.02 ? 1286 NAG A O7 1 HETATM 3981 C C1 . SIA L 6 . ? 36.318 -4.902 21.732 1.00 107.75 ? 1322 SIA A C1 1 HETATM 3982 C C2 . SIA L 6 . ? 36.653 -5.126 23.198 1.00 103.39 ? 1322 SIA A C2 1 HETATM 3983 C C3 . SIA L 6 . ? 35.345 -5.050 23.983 1.00 99.23 ? 1322 SIA A C3 1 HETATM 3984 C C4 . SIA L 6 . ? 34.508 -6.299 23.780 1.00 97.68 ? 1322 SIA A C4 1 HETATM 3985 C C5 . SIA L 6 . ? 35.327 -7.500 24.220 1.00 96.16 ? 1322 SIA A C5 1 HETATM 3986 C C6 . SIA L 6 . ? 36.577 -7.588 23.342 1.00 92.57 ? 1322 SIA A C6 1 HETATM 3987 C C7 . SIA L 6 . ? 37.490 -8.766 23.691 1.00 90.41 ? 1322 SIA A C7 1 HETATM 3988 C C8 . SIA L 6 . ? 38.853 -8.706 23.000 1.00 90.97 ? 1322 SIA A C8 1 HETATM 3989 C C9 . SIA L 6 . ? 39.510 -10.084 23.012 1.00 90.77 ? 1322 SIA A C9 1 HETATM 3990 C C10 . SIA L 6 . ? 34.552 -9.798 24.660 1.00 101.57 ? 1322 SIA A C10 1 HETATM 3991 C C11 . SIA L 6 . ? 33.555 -10.853 24.275 1.00 102.37 ? 1322 SIA A C11 1 HETATM 3992 N N5 . SIA L 6 . ? 34.458 -8.650 23.987 1.00 98.48 ? 1322 SIA A N5 1 HETATM 3993 O O1A . SIA L 6 . ? 35.783 -3.817 21.399 1.00 112.54 ? 1322 SIA A O1A 1 HETATM 3994 O O1B . SIA L 6 . ? 36.566 -5.799 20.896 1.00 105.85 ? 1322 SIA A O1B 1 HETATM 3995 O O4 . SIA L 6 . ? 33.294 -6.202 24.528 1.00 98.42 ? 1322 SIA A O4 1 HETATM 3996 O O6 . SIA L 6 . ? 37.330 -6.373 23.441 1.00 95.72 ? 1322 SIA A O6 1 HETATM 3997 O O7 . SIA L 6 . ? 37.703 -8.830 25.101 1.00 89.41 ? 1322 SIA A O7 1 HETATM 3998 O O8 . SIA L 6 . ? 38.722 -8.260 21.645 1.00 92.29 ? 1322 SIA A O8 1 HETATM 3999 O O9 . SIA L 6 . ? 40.796 -10.028 22.386 1.00 91.66 ? 1322 SIA A O9 1 HETATM 4000 O O10 . SIA L 6 . ? 35.396 -9.998 25.523 1.00 101.52 ? 1322 SIA A O10 1 HETATM 4001 C C1 . GAL M 7 . ? 41.220 -3.502 23.678 1.00 120.48 ? 1323 GAL A C1 1 HETATM 4002 C C2 . GAL M 7 . ? 39.850 -3.951 24.194 1.00 118.79 ? 1323 GAL A C2 1 HETATM 4003 C C3 . GAL M 7 . ? 38.776 -3.892 23.112 1.00 116.93 ? 1323 GAL A C3 1 HETATM 4004 C C4 . GAL M 7 . ? 38.799 -2.537 22.419 1.00 121.52 ? 1323 GAL A C4 1 HETATM 4005 C C5 . GAL M 7 . ? 40.213 -2.200 21.942 1.00 124.34 ? 1323 GAL A C5 1 HETATM 4006 C C6 . GAL M 7 . ? 40.260 -0.834 21.257 1.00 120.64 ? 1323 GAL A C6 1 HETATM 4007 O O1 . GAL M 7 . ? 42.154 -3.415 24.756 1.00 114.19 ? 1323 GAL A O1 1 HETATM 4008 O O2 . GAL M 7 . ? 39.939 -5.295 24.668 1.00 120.30 ? 1323 GAL A O2 1 HETATM 4009 O O3 . GAL M 7 . ? 37.485 -4.072 23.703 1.00 111.17 ? 1323 GAL A O3 1 HETATM 4010 O O4 . GAL M 7 . ? 38.324 -1.538 23.334 1.00 121.40 ? 1323 GAL A O4 1 HETATM 4011 O O5 . GAL M 7 . ? 41.120 -2.221 23.052 1.00 125.15 ? 1323 GAL A O5 1 HETATM 4012 O O6 . GAL M 7 . ? 41.003 -0.920 20.036 1.00 112.81 ? 1323 GAL A O6 1 HETATM 4013 C C1 . NAG N 3 . ? 25.193 -29.221 -75.296 1.00 95.60 ? 1154 NAG B C1 1 HETATM 4014 C C2 . NAG N 3 . ? 24.173 -30.369 -75.371 1.00 104.19 ? 1154 NAG B C2 1 HETATM 4015 C C3 . NAG N 3 . ? 23.728 -30.755 -76.782 1.00 112.51 ? 1154 NAG B C3 1 HETATM 4016 C C4 . NAG N 3 . ? 23.656 -29.542 -77.696 1.00 118.22 ? 1154 NAG B C4 1 HETATM 4017 C C5 . NAG N 3 . ? 25.004 -28.826 -77.649 1.00 110.93 ? 1154 NAG B C5 1 HETATM 4018 C C6 . NAG N 3 . ? 25.137 -27.699 -78.675 1.00 110.35 ? 1154 NAG B C6 1 HETATM 4019 C C7 . NAG N 3 . ? 24.811 -31.612 -73.365 1.00 101.39 ? 1154 NAG B C7 1 HETATM 4020 C C8 . NAG N 3 . ? 25.354 -32.888 -72.784 1.00 98.56 ? 1154 NAG B C8 1 HETATM 4021 N N2 . NAG N 3 . ? 24.686 -31.551 -74.692 1.00 102.20 ? 1154 NAG B N2 1 HETATM 4022 O O3 . NAG N 3 . ? 22.464 -31.379 -76.712 1.00 113.90 ? 1154 NAG B O3 1 HETATM 4023 O O4 . NAG N 3 . ? 23.270 -29.943 -79.003 1.00 128.24 ? 1154 NAG B O4 1 HETATM 4024 O O5 . NAG N 3 . ? 25.121 -28.283 -76.355 1.00 100.56 ? 1154 NAG B O5 1 HETATM 4025 O O6 . NAG N 3 . ? 24.437 -26.553 -78.239 1.00 106.59 ? 1154 NAG B O6 1 HETATM 4026 O O7 . NAG N 3 . ? 24.508 -30.681 -72.619 1.00 100.48 ? 1154 NAG B O7 1 HETATM 4027 C C1 . NAG O 3 . ? 22.044 -29.290 -79.396 1.00 136.06 ? 1155 NAG B C1 1 HETATM 4028 C C2 . NAG O 3 . ? 21.725 -29.685 -80.839 1.00 137.80 ? 1155 NAG B C2 1 HETATM 4029 C C3 . NAG O 3 . ? 20.270 -29.419 -81.258 1.00 146.45 ? 1155 NAG B C3 1 HETATM 4030 C C4 . NAG O 3 . ? 19.246 -29.549 -80.125 1.00 151.83 ? 1155 NAG B C4 1 HETATM 4031 C C5 . NAG O 3 . ? 19.786 -28.916 -78.846 1.00 147.34 ? 1155 NAG B C5 1 HETATM 4032 C C6 . NAG O 3 . ? 18.812 -29.000 -77.672 1.00 143.85 ? 1155 NAG B C6 1 HETATM 4033 C C7 . NAG O 3 . ? 23.825 -29.427 -82.103 1.00 130.43 ? 1155 NAG B C7 1 HETATM 4034 C C8 . NAG O 3 . ? 24.637 -28.559 -83.021 1.00 128.47 ? 1155 NAG B C8 1 HETATM 4035 N N2 . NAG O 3 . ? 22.629 -28.964 -81.727 1.00 134.89 ? 1155 NAG B N2 1 HETATM 4036 O O3 . NAG O 3 . ? 19.926 -30.296 -82.309 1.00 144.49 ? 1155 NAG B O3 1 HETATM 4037 O O4 . NAG O 3 . ? 18.012 -28.951 -80.498 1.00 161.06 ? 1155 NAG B O4 1 HETATM 4038 O O5 . NAG O 3 . ? 20.974 -29.605 -78.526 1.00 141.96 ? 1155 NAG B O5 1 HETATM 4039 O O6 . NAG O 3 . ? 18.578 -30.347 -77.330 1.00 139.40 ? 1155 NAG B O6 1 HETATM 4040 O O7 . NAG O 3 . ? 24.282 -30.509 -81.742 1.00 129.82 ? 1155 NAG B O7 1 HETATM 4041 C C1 . BMA P 5 . ? 17.082 -29.896 -81.077 1.00 167.91 ? 1156 BMA B C1 1 HETATM 4042 C C2 . BMA P 5 . ? 15.688 -29.649 -80.507 1.00 166.99 ? 1156 BMA B C2 1 HETATM 4043 C C3 . BMA P 5 . ? 14.698 -30.667 -81.072 1.00 167.82 ? 1156 BMA B C3 1 HETATM 4044 C C4 . BMA P 5 . ? 14.785 -30.747 -82.597 1.00 168.29 ? 1156 BMA B C4 1 HETATM 4045 C C5 . BMA P 5 . ? 16.230 -30.874 -83.082 1.00 167.15 ? 1156 BMA B C5 1 HETATM 4046 C C6 . BMA P 5 . ? 16.299 -30.846 -84.611 1.00 163.08 ? 1156 BMA B C6 1 HETATM 4047 O O2 . BMA P 5 . ? 15.264 -28.315 -80.817 1.00 160.67 ? 1156 BMA B O2 1 HETATM 4048 O O3 . BMA P 5 . ? 13.366 -30.314 -80.679 1.00 166.28 ? 1156 BMA B O3 1 HETATM 4049 O O4 . BMA P 5 . ? 14.036 -31.877 -83.057 1.00 163.16 ? 1156 BMA B O4 1 HETATM 4050 O O5 . BMA P 5 . ? 17.026 -29.829 -82.506 1.00 170.73 ? 1156 BMA B O5 1 HETATM 4051 O O6 . BMA P 5 . ? 17.365 -30.006 -85.070 1.00 161.16 ? 1156 BMA B O6 1 HETATM 4052 S S1 . MPO Q 8 . ? 38.363 -11.030 -71.450 1.00 117.29 ? 1163 MPO B S1 1 HETATM 4053 O O1 . MPO Q 8 . ? 39.363 -10.326 -70.689 1.00 128.52 ? 1163 MPO B O1 1 HETATM 4054 O O2 . MPO Q 8 . ? 37.983 -10.237 -72.588 1.00 122.85 ? 1163 MPO B O2 1 HETATM 4055 O O4 . MPO Q 8 . ? 44.869 -9.952 -72.350 1.00 102.84 ? 1163 MPO B O4 1 HETATM 4056 N N1 . MPO Q 8 . ? 42.365 -11.190 -71.937 1.00 98.13 ? 1163 MPO B N1 1 HETATM 4057 C C1 . MPO Q 8 . ? 38.979 -12.492 -71.942 1.00 102.66 ? 1163 MPO B C1 1 HETATM 4058 O O3 . MPO Q 8 . ? 37.038 -11.267 -70.521 1.00 118.23 ? 1163 MPO B O3 1 HETATM 4059 C C2 . MPO Q 8 . ? 40.326 -12.293 -72.615 1.00 95.62 ? 1163 MPO B C2 1 HETATM 4060 C C3 . MPO Q 8 . ? 41.486 -12.328 -71.628 1.00 93.63 ? 1163 MPO B C3 1 HETATM 4061 C C4 . MPO Q 8 . ? 43.203 -11.497 -73.106 1.00 101.06 ? 1163 MPO B C4 1 HETATM 4062 C C5 . MPO Q 8 . ? 44.047 -10.280 -73.468 1.00 100.79 ? 1163 MPO B C5 1 HETATM 4063 C C6 . MPO Q 8 . ? 44.119 -9.675 -71.163 1.00 102.29 ? 1163 MPO B C6 1 HETATM 4064 C C7 . MPO Q 8 . ? 43.234 -10.865 -70.798 1.00 100.69 ? 1163 MPO B C7 1 HETATM 4065 O O . HOH R 9 . ? 38.710 -13.863 -82.548 1.00 68.92 ? 2001 HOH A O 1 HETATM 4066 O O . HOH R 9 . ? 37.800 -17.608 -85.350 1.00 69.93 ? 2002 HOH A O 1 HETATM 4067 O O . HOH R 9 . ? 36.426 -14.103 -75.745 1.00 66.74 ? 2003 HOH A O 1 HETATM 4068 O O . HOH R 9 . ? 41.724 -15.938 -70.192 1.00 52.37 ? 2004 HOH A O 1 HETATM 4069 O O . HOH R 9 . ? 40.222 -14.518 -65.698 1.00 52.97 ? 2005 HOH A O 1 HETATM 4070 O O . HOH R 9 . ? 40.605 -12.522 -58.926 1.00 50.66 ? 2006 HOH A O 1 HETATM 4071 O O . HOH R 9 . ? 31.591 -11.499 -54.998 1.00 66.22 ? 2007 HOH A O 1 HETATM 4072 O O . HOH R 9 . ? 32.395 -6.745 -56.471 1.00 59.69 ? 2008 HOH A O 1 HETATM 4073 O O . HOH R 9 . ? 32.804 -2.353 -57.319 1.00 82.00 ? 2009 HOH A O 1 HETATM 4074 O O . HOH R 9 . ? 40.849 -5.067 -54.184 1.00 77.73 ? 2010 HOH A O 1 HETATM 4075 O O . HOH R 9 . ? 34.541 -10.419 -49.920 1.00 71.38 ? 2011 HOH A O 1 HETATM 4076 O O . HOH R 9 . ? 35.963 -6.500 -48.827 1.00 70.84 ? 2012 HOH A O 1 HETATM 4077 O O . HOH R 9 . ? 43.278 -5.355 -49.601 1.00 70.78 ? 2013 HOH A O 1 HETATM 4078 O O . HOH R 9 . ? 46.437 -10.690 -43.889 1.00 61.65 ? 2014 HOH A O 1 HETATM 4079 O O . HOH R 9 . ? 45.889 -7.916 -43.012 1.00 74.70 ? 2015 HOH A O 1 HETATM 4080 O O . HOH R 9 . ? 45.060 -15.049 -42.437 1.00 41.95 ? 2016 HOH A O 1 HETATM 4081 O O . HOH R 9 . ? 50.115 -9.821 -41.374 1.00 65.60 ? 2017 HOH A O 1 HETATM 4082 O O . HOH R 9 . ? 46.753 -12.603 -39.622 1.00 59.17 ? 2018 HOH A O 1 HETATM 4083 O O . HOH R 9 . ? 51.889 -18.473 -50.544 1.00 56.12 ? 2019 HOH A O 1 HETATM 4084 O O . HOH R 9 . ? 56.558 -14.324 -51.132 1.00 62.86 ? 2020 HOH A O 1 HETATM 4085 O O . HOH R 9 . ? 52.612 -16.585 -52.208 1.00 62.34 ? 2021 HOH A O 1 HETATM 4086 O O . HOH R 9 . ? 45.835 -10.278 -54.058 1.00 75.85 ? 2022 HOH A O 1 HETATM 4087 O O . HOH R 9 . ? 31.910 -17.715 -50.702 1.00 73.47 ? 2023 HOH A O 1 HETATM 4088 O O . HOH R 9 . ? 34.075 -13.195 -41.828 1.00 69.08 ? 2024 HOH A O 1 HETATM 4089 O O . HOH R 9 . ? 40.471 -12.311 -37.006 1.00 59.57 ? 2025 HOH A O 1 HETATM 4090 O O . HOH R 9 . ? 48.036 -29.029 -1.317 1.00 65.34 ? 2026 HOH A O 1 HETATM 4091 O O . HOH R 9 . ? 34.733 -9.951 -33.675 1.00 72.11 ? 2027 HOH A O 1 HETATM 4092 O O . HOH R 9 . ? 30.765 -11.321 -28.048 1.00 61.08 ? 2028 HOH A O 1 HETATM 4093 O O . HOH R 9 . ? 22.637 -14.002 -5.016 1.00 73.47 ? 2029 HOH A O 1 HETATM 4094 O O . HOH R 9 . ? 33.798 -9.514 -3.661 1.00 71.79 ? 2030 HOH A O 1 HETATM 4095 O O . HOH R 9 . ? 25.809 -13.912 5.554 1.00 69.81 ? 2031 HOH A O 1 HETATM 4096 O O . HOH R 9 . ? 18.055 -15.291 9.171 1.00 76.64 ? 2032 HOH A O 1 HETATM 4097 O O . HOH R 9 . ? 18.340 -17.881 8.777 1.00 68.04 ? 2033 HOH A O 1 HETATM 4098 O O . HOH R 9 . ? 38.164 -14.727 -0.407 1.00 61.15 ? 2034 HOH A O 1 HETATM 4099 O O . HOH R 9 . ? 41.554 -7.745 21.158 1.00 70.39 ? 2035 HOH A O 1 HETATM 4100 O O . HOH R 9 . ? 43.266 -24.829 1.593 1.00 64.84 ? 2036 HOH A O 1 HETATM 4101 O O . HOH R 9 . ? 45.507 -29.293 -2.856 1.00 62.77 ? 2037 HOH A O 1 HETATM 4102 O O . HOH R 9 . ? 23.656 -35.451 4.282 1.00 74.91 ? 2038 HOH A O 1 HETATM 4103 O O . HOH R 9 . ? 28.912 -14.808 -34.490 1.00 80.09 ? 2039 HOH A O 1 HETATM 4104 O O . HOH R 9 . ? 40.701 -8.951 -24.146 1.00 68.48 ? 2040 HOH A O 1 HETATM 4105 O O . HOH R 9 . ? 42.786 -8.971 -26.152 1.00 73.07 ? 2041 HOH A O 1 HETATM 4106 O O . HOH R 9 . ? 42.162 -8.465 -31.164 1.00 75.96 ? 2042 HOH A O 1 HETATM 4107 O O . HOH R 9 . ? 47.995 -12.488 -33.610 1.00 67.66 ? 2043 HOH A O 1 HETATM 4108 O O . HOH R 9 . ? 45.298 -15.319 -39.606 1.00 56.69 ? 2044 HOH A O 1 HETATM 4109 O O . HOH R 9 . ? 41.733 -21.686 -46.101 1.00 46.60 ? 2045 HOH A O 1 HETATM 4110 O O . HOH R 9 . ? 32.585 -20.008 -49.816 1.00 68.80 ? 2046 HOH A O 1 HETATM 4111 O O . HOH R 9 . ? 44.280 -18.271 -55.697 1.00 46.13 ? 2047 HOH A O 1 HETATM 4112 O O . HOH R 9 . ? 47.003 -18.099 -56.306 1.00 51.44 ? 2048 HOH A O 1 HETATM 4113 O O . HOH R 9 . ? 48.633 -17.021 -57.983 1.00 61.87 ? 2049 HOH A O 1 HETATM 4114 O O . HOH R 9 . ? 45.982 -10.326 -58.445 1.00 74.77 ? 2050 HOH A O 1 HETATM 4115 O O . HOH S 9 . ? 49.718 -19.548 -60.590 1.00 49.25 ? 2001 HOH B O 1 HETATM 4116 O O . HOH S 9 . ? 51.110 -15.454 -57.317 1.00 69.94 ? 2002 HOH B O 1 HETATM 4117 O O . HOH S 9 . ? 53.111 -20.632 -54.810 1.00 62.04 ? 2003 HOH B O 1 HETATM 4118 O O . HOH S 9 . ? 52.910 -25.983 -62.240 1.00 63.73 ? 2004 HOH B O 1 HETATM 4119 O O . HOH S 9 . ? 52.709 -19.262 -64.878 1.00 55.54 ? 2005 HOH B O 1 HETATM 4120 O O . HOH S 9 . ? 50.437 -12.838 -64.562 1.00 68.58 ? 2006 HOH B O 1 HETATM 4121 O O . HOH S 9 . ? 45.654 -13.363 -69.647 1.00 65.32 ? 2007 HOH B O 1 HETATM 4122 O O . HOH S 9 . ? 49.933 -14.408 -70.267 1.00 69.42 ? 2008 HOH B O 1 HETATM 4123 O O . HOH S 9 . ? 43.658 -12.298 -67.944 1.00 64.33 ? 2009 HOH B O 1 HETATM 4124 O O . HOH S 9 . ? 41.836 -8.957 -65.411 1.00 66.76 ? 2010 HOH B O 1 HETATM 4125 O O . HOH S 9 . ? 41.447 -13.731 -68.545 1.00 61.14 ? 2011 HOH B O 1 HETATM 4126 O O . HOH S 9 . ? 35.309 -8.832 -66.435 1.00 64.01 ? 2012 HOH B O 1 HETATM 4127 O O . HOH S 9 . ? 28.312 -19.485 -56.407 1.00 72.04 ? 2013 HOH B O 1 HETATM 4128 O O . HOH S 9 . ? 31.105 -17.498 -56.252 1.00 63.41 ? 2014 HOH B O 1 HETATM 4129 O O . HOH S 9 . ? 30.747 -17.799 -72.303 1.00 70.37 ? 2015 HOH B O 1 HETATM 4130 O O . HOH S 9 . ? 27.734 -17.641 -72.543 1.00 59.20 ? 2016 HOH B O 1 HETATM 4131 O O . HOH S 9 . ? 32.547 -21.539 -47.820 1.00 66.67 ? 2017 HOH B O 1 HETATM 4132 O O . HOH S 9 . ? 28.275 -24.189 -44.750 1.00 71.70 ? 2018 HOH B O 1 HETATM 4133 O O . HOH S 9 . ? 34.439 -31.420 -41.820 1.00 78.07 ? 2019 HOH B O 1 HETATM 4134 O O . HOH S 9 . ? 37.053 -34.076 -42.772 1.00 63.35 ? 2020 HOH B O 1 HETATM 4135 O O . HOH S 9 . ? 39.725 -37.448 -37.953 1.00 60.22 ? 2021 HOH B O 1 HETATM 4136 O O . HOH S 9 . ? 43.935 -21.080 -12.479 1.00 70.69 ? 2022 HOH B O 1 HETATM 4137 O O . HOH S 9 . ? 47.873 -19.851 -10.333 1.00 63.13 ? 2023 HOH B O 1 HETATM 4138 O O . HOH S 9 . ? 52.506 -19.998 -29.131 1.00 63.27 ? 2024 HOH B O 1 HETATM 4139 O O . HOH S 9 . ? 47.685 -27.011 -36.063 1.00 52.66 ? 2025 HOH B O 1 HETATM 4140 O O . HOH S 9 . ? 50.834 -29.348 -30.864 0.33 50.96 ? 2026 HOH B O 1 HETATM 4141 O O . HOH S 9 . ? 47.384 -17.374 -38.787 1.00 52.01 ? 2027 HOH B O 1 HETATM 4142 O O . HOH S 9 . ? 52.335 -19.010 -32.030 1.00 74.24 ? 2028 HOH B O 1 HETATM 4143 O O . HOH S 9 . ? 50.195 -27.620 -46.346 1.00 73.88 ? 2029 HOH B O 1 HETATM 4144 O O . HOH S 9 . ? 46.289 -27.275 -52.375 1.00 51.54 ? 2030 HOH B O 1 HETATM 4145 O O . HOH S 9 . ? 44.765 -29.286 -51.260 1.00 59.88 ? 2031 HOH B O 1 HETATM 4146 O O . HOH S 9 . ? 49.750 -32.008 -52.579 1.00 50.56 ? 2032 HOH B O 1 HETATM 4147 O O . HOH S 9 . ? 52.001 -22.593 -52.651 1.00 48.06 ? 2033 HOH B O 1 HETATM 4148 O O . HOH S 9 . ? 42.130 -29.143 -57.896 1.00 53.05 ? 2034 HOH B O 1 HETATM 4149 O O . HOH S 9 . ? 38.627 -27.670 -62.483 1.00 53.44 ? 2035 HOH B O 1 HETATM 4150 O O . HOH S 9 . ? 37.720 -29.421 -57.548 1.00 73.38 ? 2036 HOH B O 1 HETATM 4151 O O . HOH S 9 . ? 41.874 -31.390 -67.003 1.00 57.00 ? 2037 HOH B O 1 HETATM 4152 O O . HOH S 9 . ? 45.169 -30.358 -65.738 1.00 56.89 ? 2038 HOH B O 1 HETATM 4153 O O . HOH S 9 . ? 37.915 -29.045 -64.717 1.00 74.15 ? 2039 HOH B O 1 HETATM 4154 O O . HOH S 9 . ? 46.028 -19.648 -74.050 1.00 51.25 ? 2040 HOH B O 1 HETATM 4155 O O . HOH S 9 . ? 38.512 -32.756 -72.326 1.00 66.99 ? 2041 HOH B O 1 HETATM 4156 O O . HOH S 9 . ? 37.904 -33.614 -78.824 1.00 71.78 ? 2042 HOH B O 1 HETATM 4157 O O . HOH S 9 . ? 47.961 -24.015 -81.043 1.00 70.94 ? 2043 HOH B O 1 HETATM 4158 O O . HOH S 9 . ? 49.646 -27.608 -75.664 1.00 63.47 ? 2044 HOH B O 1 HETATM 4159 O O . HOH S 9 . ? 49.028 -25.295 -71.964 1.00 65.54 ? 2045 HOH B O 1 HETATM 4160 O O . HOH S 9 . ? 47.116 -11.244 -73.658 1.00 71.81 ? 2046 HOH B O 1 HETATM 4161 O O . HOH S 9 . ? 24.272 -19.336 -85.802 1.00 77.05 ? 2047 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 ? 0.9113 0.9689 0.7142 0.3020 -0.0951 0.0101 1 ASP A N 2 C CA . ASP A 1 ? 0.8826 0.9973 0.7189 0.2960 -0.0975 -0.0004 1 ASP A CA 3 C C . ASP A 1 ? 0.8547 0.9502 0.7183 0.2616 -0.0888 -0.0004 1 ASP A C 4 O O . ASP A 1 ? 0.8200 0.8944 0.6920 0.2356 -0.0828 0.0020 1 ASP A O 5 C CB . ASP A 1 ? 0.8559 1.0500 0.7153 0.2889 -0.1036 -0.0124 1 ASP A CB 6 C CG . ASP A 1 ? 0.8795 1.1074 0.7154 0.3246 -0.1133 -0.0139 1 ASP A CG 7 O OD1 . ASP A 1 ? 0.9136 1.0969 0.7111 0.3573 -0.1151 -0.0049 1 ASP A OD1 8 O OD2 . ASP A 1 ? 0.8989 1.1981 0.7518 0.3193 -0.1189 -0.0246 1 ASP A OD2 9 N N . GLN A 2 ? 0.8453 0.9499 0.7210 0.2637 -0.0882 -0.0033 2 GLN A N 10 C CA . GLN A 2 ? 0.8118 0.9019 0.7123 0.2341 -0.0806 -0.0036 2 GLN A CA 11 C C . GLN A 2 ? 0.7648 0.8978 0.6891 0.2317 -0.0820 -0.0120 2 GLN A C 12 O O . GLN A 2 ? 0.7863 0.9512 0.7041 0.2579 -0.0883 -0.0160 2 GLN A O 13 C CB . GLN A 2 ? 0.8650 0.8838 0.7460 0.2323 -0.0739 0.0073 2 GLN A CB 14 C CG . GLN A 2 ? 0.9251 0.9133 0.7780 0.2596 -0.0756 0.0115 2 GLN A CG 15 C CD . GLN A 2 ? 0.9727 0.8894 0.8036 0.2496 -0.0678 0.0214 2 GLN A CD 16 O OE1 . GLN A 2 ? 0.9837 0.8811 0.8166 0.2448 -0.0644 0.0222 2 GLN A OE1 17 N NE2 . GLN A 2 ? 1.0085 0.8883 0.8180 0.2440 -0.0647 0.0285 2 GLN A NE2 18 N N . ILE A 3 ? 0.7028 0.8363 0.6525 0.2012 -0.0757 -0.0146 3 ILE A N 19 C CA . ILE A 3 ? 0.6857 0.8486 0.6568 0.1935 -0.0750 -0.0212 3 ILE A CA 20 C C . ILE A 3 ? 0.6819 0.7957 0.6573 0.1791 -0.0672 -0.0147 3 ILE A C 21 O O . ILE A 3 ? 0.6822 0.7603 0.6566 0.1623 -0.0615 -0.0091 3 ILE A O 22 C CB . ILE A 3 ? 0.6724 0.8918 0.6675 0.1687 -0.0751 -0.0326 3 ILE A CB 23 C CG1 . ILE A 3 ? 0.6649 0.9217 0.6786 0.1636 -0.0750 -0.0402 3 ILE A CG1 24 C CG2 . ILE A 3 ? 0.6606 0.8527 0.6626 0.1372 -0.0677 -0.0313 3 ILE A CG2 25 C CD1 . ILE A 3 ? 0.6512 0.9762 0.6805 0.1450 -0.0770 -0.0532 3 ILE A CD1 26 N N . CYS A 4 ? 0.6799 0.7952 0.6591 0.1872 -0.0673 -0.0157 4 CYS A N 27 C CA . CYS A 4 ? 0.6748 0.7461 0.6551 0.1770 -0.0609 -0.0098 4 CYS A CA 28 C C . CYS A 4 ? 0.6501 0.7515 0.6550 0.1639 -0.0591 -0.0165 4 CYS A C 29 O O . CYS A 4 ? 0.6369 0.7865 0.6499 0.1734 -0.0638 -0.0245 4 CYS A O 30 C CB . CYS A 4 ? 0.7401 0.7698 0.6911 0.2017 -0.0620 -0.0032 4 CYS A CB 31 S SG . CYS A 4 ? 0.8567 0.8383 0.7677 0.2183 -0.0631 0.0060 4 CYS A SG 32 N N . ILE A 5 ? 0.6049 0.6806 0.6205 0.1432 -0.0524 -0.0134 5 ILE A N 33 C CA . ILE A 5 ? 0.5688 0.6622 0.6034 0.1313 -0.0498 -0.0181 5 ILE A CA 34 C C . ILE A 5 ? 0.5791 0.6402 0.6057 0.1408 -0.0482 -0.0132 5 ILE A C 35 O O . ILE A 5 ? 0.5858 0.6021 0.5977 0.1408 -0.0452 -0.0053 5 ILE A O 36 C CB . ILE A 5 ? 0.5477 0.6337 0.5957 0.1034 -0.0433 -0.0183 5 ILE A CB 37 C CG1 . ILE A 5 ? 0.5707 0.6807 0.6201 0.0920 -0.0441 -0.0236 5 ILE A CG1 38 C CG2 . ILE A 5 ? 0.5259 0.6256 0.5893 0.0913 -0.0402 -0.0226 5 ILE A CG2 39 C CD1 . ILE A 5 ? 0.5854 0.7516 0.6431 0.0909 -0.0485 -0.0344 5 ILE A CD1 40 N N . GLY A 6 ? 0.5712 0.6567 0.6062 0.1470 -0.0498 -0.0184 6 GLY A N 41 C CA . GLY A 6 ? 0.5851 0.6408 0.6092 0.1578 -0.0487 -0.0149 6 GLY A CA 42 C C . GLY A 6 ? 0.5607 0.6467 0.6015 0.1555 -0.0484 -0.0214 6 GLY A C 43 O O . GLY A 6 ? 0.5587 0.6880 0.6196 0.1424 -0.0484 -0.0284 6 GLY A O 44 N N . TYR A 7 ? 0.5708 0.6320 0.5999 0.1671 -0.0479 -0.0192 7 TYR A N 45 C CA . TYR A 7 ? 0.5717 0.6549 0.6154 0.1640 -0.0467 -0.0243 7 TYR A CA 46 C C . TYR A 7 ? 0.6113 0.6828 0.6334 0.1922 -0.0497 -0.0250 7 TYR A C 47 O O . TYR A 7 ? 0.6454 0.6785 0.6366 0.2116 -0.0514 -0.0202 7 TYR A O 48 C CB . TYR A 7 ? 0.5702 0.6279 0.6255 0.1393 -0.0403 -0.0205 7 TYR A CB 49 C CG . TYR A 7 ? 0.5995 0.6012 0.6351 0.1380 -0.0372 -0.0121 7 TYR A CG 50 C CD1 . TYR A 7 ? 0.6052 0.5838 0.6353 0.1278 -0.0350 -0.0062 7 TYR A CD1 51 C CD2 . TYR A 7 ? 0.6463 0.6197 0.6668 0.1451 -0.0362 -0.0106 7 TYR A CD2 52 C CE1 . TYR A 7 ? 0.6469 0.5802 0.6579 0.1233 -0.0317 0.0006 7 TYR A CE1 53 C CE2 . TYR A 7 ? 0.6583 0.5821 0.6575 0.1393 -0.0328 -0.0040 7 TYR A CE2 54 C CZ . TYR A 7 ? 0.6618 0.5679 0.6569 0.1274 -0.0305 0.0015 7 TYR A CZ 55 O OH . TYR A 7 ? 0.6800 0.5419 0.6526 0.1184 -0.0265 0.0072 7 TYR A OH 56 N N . HIS A 8 ? 0.6101 0.7121 0.6452 0.1941 -0.0497 -0.0311 8 HIS A N 57 C CA . HIS A 8 ? 0.6628 0.7663 0.6794 0.2237 -0.0527 -0.0340 8 HIS A CA 58 C C . HIS A 8 ? 0.7010 0.7376 0.6899 0.2286 -0.0495 -0.0277 8 HIS A C 59 O O . HIS A 8 ? 0.7164 0.7252 0.7133 0.2040 -0.0444 -0.0239 8 HIS A O 60 C CB . HIS A 8 ? 0.6356 0.7953 0.6780 0.2184 -0.0524 -0.0428 8 HIS A CB 61 C CG . HIS A 8 ? 0.6591 0.8333 0.6860 0.2504 -0.0556 -0.0474 8 HIS A CG 62 N ND1 . HIS A 8 ? 0.6983 0.9013 0.7086 0.2847 -0.0617 -0.0511 8 HIS A ND1 63 C CD2 . HIS A 8 ? 0.6605 0.8276 0.6851 0.2551 -0.0535 -0.0494 8 HIS A CD2 64 C CE1 . HIS A 8 ? 0.7000 0.9114 0.6967 0.3111 -0.0631 -0.0550 8 HIS A CE1 65 N NE2 . HIS A 8 ? 0.6747 0.8637 0.6801 0.2928 -0.0580 -0.0542 8 HIS A NE2 66 N N . ALA A 9 ? 0.7393 0.7502 0.6920 0.2610 -0.0524 -0.0272 9 ALA A N 67 C CA . ALA A 9 ? 0.7646 0.7143 0.6847 0.2677 -0.0493 -0.0237 9 ALA A CA 68 C C . ALA A 9 ? 0.8009 0.7610 0.6979 0.3056 -0.0529 -0.0291 9 ALA A C 69 O O . ALA A 9 ? 0.8338 0.8388 0.7309 0.3315 -0.0584 -0.0335 9 ALA A O 70 C CB . ALA A 9 ? 0.7929 0.6716 0.6739 0.2667 -0.0471 -0.0152 9 ALA A CB 71 N N . ASN A 10 ? 0.8196 0.7418 0.6961 0.3097 -0.0499 -0.0292 10 ASN A N 72 C CA . ASN A 10 ? 0.8821 0.8046 0.7293 0.3488 -0.0526 -0.0338 10 ASN A CA 73 C C . ASN A 10 ? 0.9733 0.8146 0.7739 0.3530 -0.0481 -0.0305 10 ASN A C 74 O O . ASN A 10 ? 0.9794 0.7673 0.7696 0.3249 -0.0432 -0.0246 10 ASN A O 75 C CB . ASN A 10 ? 0.8380 0.8422 0.7260 0.3506 -0.0545 -0.0431 10 ASN A CB 76 C CG . ASN A 10 ? 0.8107 0.8157 0.7262 0.3181 -0.0494 -0.0441 10 ASN A CG 77 O OD1 . ASN A 10 ? 0.8260 0.7743 0.7313 0.2955 -0.0447 -0.0383 10 ASN A OD1 78 N ND2 . ASN A 10 ? 0.7781 0.8509 0.7280 0.3147 -0.0500 -0.0518 10 ASN A ND2 79 N N . ASN A 11 ? 1.1025 0.9360 0.8729 0.3877 -0.0495 -0.0349 11 ASN A N 80 C CA . ASN A 11 ? 1.2376 0.9858 0.9531 0.3947 -0.0450 -0.0325 11 ASN A CA 81 C C . ASN A 11 ? 1.1766 0.9257 0.9135 0.3680 -0.0405 -0.0355 11 ASN A C 82 O O . ASN A 11 ? 1.2268 0.9197 0.9216 0.3774 -0.0373 -0.0362 11 ASN A O 83 C CB . ASN A 11 ? 1.3928 1.1180 1.0530 0.4497 -0.0481 -0.0352 11 ASN A CB 84 C CG . ASN A 11 ? 1.5150 1.3242 1.2045 0.4767 -0.0524 -0.0447 11 ASN A CG 85 O OD1 . ASN A 11 ? 1.4642 1.3422 1.2124 0.4510 -0.0523 -0.0493 11 ASN A OD1 86 N ND2 . ASN A 11 ? 1.7533 1.5567 1.3981 0.5299 -0.0560 -0.0477 11 ASN A ND2 87 N N . SER A 12 ? 1.0595 0.8680 0.8573 0.3349 -0.0400 -0.0370 12 SER A N 88 C CA . SER A 12 ? 0.9994 0.8199 0.8225 0.3112 -0.0363 -0.0400 12 SER A CA 89 C C . SER A 12 ? 1.0299 0.7794 0.8287 0.2826 -0.0305 -0.0348 12 SER A C 90 O O . SER A 12 ? 1.0123 0.7297 0.8029 0.2632 -0.0287 -0.0286 12 SER A O 91 C CB . SER A 12 ? 0.9199 0.8153 0.8075 0.2835 -0.0368 -0.0421 12 SER A CB 92 O OG . SER A 12 ? 0.8757 0.7873 0.7858 0.2657 -0.0337 -0.0453 12 SER A OG 93 N N . THR A 13 ? 1.0490 0.7783 0.8360 0.2796 -0.0276 -0.0380 13 THR A N 94 C CA . THR A 13 ? 1.0615 0.7334 0.8276 0.2497 -0.0220 -0.0351 13 THR A CA 95 C C . THR A 13 ? 1.0176 0.7317 0.8303 0.2215 -0.0201 -0.0375 13 THR A C 96 O O . THR A 13 ? 1.0171 0.6987 0.8206 0.1949 -0.0158 -0.0361 13 THR A O 97 C CB . THR A 13 ? 1.1626 0.7593 0.8613 0.2699 -0.0193 -0.0370 13 THR A CB 98 O OG1 . THR A 13 ? 1.1734 0.8005 0.8775 0.2954 -0.0211 -0.0440 13 THR A OG1 99 C CG2 . THR A 13 ? 1.2050 0.7473 0.8468 0.2996 -0.0205 -0.0337 13 THR A CG2 100 N N . GLU A 14 ? 0.9847 0.7715 0.8446 0.2262 -0.0229 -0.0414 14 GLU A N 101 C CA . GLU A 14 ? 0.9446 0.7716 0.8475 0.2003 -0.0210 -0.0431 14 GLU A CA 102 C C . GLU A 14 ? 0.8656 0.6889 0.7892 0.1650 -0.0184 -0.0371 14 GLU A C 103 O O . GLU A 14 ? 0.8602 0.6860 0.7898 0.1604 -0.0195 -0.0329 14 GLU A O 104 C CB . GLU A 14 ? 0.9802 0.8829 0.9252 0.2082 -0.0238 -0.0478 14 GLU A CB 105 C CG . GLU A 14 ? 1.0936 1.0170 1.0258 0.2413 -0.0259 -0.0551 14 GLU A CG 106 C CD . GLU A 14 ? 1.1800 1.1549 1.1459 0.2320 -0.0245 -0.0606 14 GLU A CD 107 O OE1 . GLU A 14 ? 1.2312 1.1851 1.1985 0.2125 -0.0210 -0.0597 14 GLU A OE1 108 O OE2 . GLU A 14 ? 1.2693 1.3074 1.2590 0.2426 -0.0266 -0.0660 14 GLU A OE2 109 N N . GLN A 15 ? 0.8243 0.6444 0.7577 0.1419 -0.0152 -0.0371 15 GLN A N 110 C CA . GLN A 15 ? 0.7814 0.5990 0.7297 0.1110 -0.0126 -0.0321 15 GLN A CA 111 C C . GLN A 15 ? 0.7117 0.5762 0.7016 0.0950 -0.0116 -0.0328 15 GLN A C 112 O O . GLN A 15 ? 0.6717 0.5523 0.6685 0.1002 -0.0115 -0.0373 15 GLN A O 113 C CB . GLN A 15 ? 0.8509 0.6141 0.7620 0.0959 -0.0090 -0.0312 15 GLN A CB 114 C CG . GLN A 15 ? 0.9465 0.6480 0.8046 0.1080 -0.0083 -0.0300 15 GLN A CG 115 C CD . GLN A 15 ? 1.0023 0.6484 0.8203 0.0849 -0.0035 -0.0296 15 GLN A CD 116 O OE1 . GLN A 15 ? 1.0603 0.6579 0.8398 0.0789 -0.0012 -0.0266 15 GLN A OE1 117 N NE2 . GLN A 15 ? 1.0158 0.6689 0.8405 0.0698 -0.0016 -0.0329 15 GLN A NE2 118 N N . VAL A 16 ? 0.6715 0.5549 0.6852 0.0768 -0.0106 -0.0282 16 VAL A N 119 C CA . VAL A 16 ? 0.6358 0.5540 0.6808 0.0622 -0.0091 -0.0278 16 VAL A CA 120 C C . VAL A 16 ? 0.6544 0.5645 0.7002 0.0407 -0.0066 -0.0232 16 VAL A C 121 O O . VAL A 16 ? 0.6679 0.5547 0.6974 0.0349 -0.0060 -0.0201 16 VAL A O 122 C CB . VAL A 16 ? 0.5947 0.5520 0.6680 0.0646 -0.0100 -0.0274 16 VAL A CB 123 C CG1 . VAL A 16 ? 0.5959 0.5724 0.6697 0.0841 -0.0125 -0.0331 16 VAL A CG1 124 C CG2 . VAL A 16 ? 0.5927 0.5463 0.6682 0.0601 -0.0103 -0.0225 16 VAL A CG2 125 N N . ASP A 17 ? 0.6606 0.5923 0.7237 0.0293 -0.0050 -0.0230 17 ASP A N 126 C CA . ASP A 17 ? 0.6612 0.5989 0.7290 0.0113 -0.0030 -0.0191 17 ASP A CA 127 C C . ASP A 17 ? 0.6378 0.6060 0.7308 0.0102 -0.0024 -0.0151 17 ASP A C 128 O O . ASP A 17 ? 0.5803 0.5654 0.6874 0.0177 -0.0027 -0.0163 17 ASP A O 129 C CB . ASP A 17 ? 0.7013 0.6429 0.7671 0.0014 -0.0017 -0.0215 17 ASP A CB 130 C CG . ASP A 17 ? 0.7818 0.6859 0.8151 -0.0033 -0.0010 -0.0253 17 ASP A CG 131 O OD1 . ASP A 17 ? 0.8405 0.7138 0.8499 -0.0063 -0.0004 -0.0243 17 ASP A OD1 132 O OD2 . ASP A 17 ? 0.8064 0.7083 0.8343 -0.0050 -0.0006 -0.0292 17 ASP A OD2 133 N N . THR A 18 ? 0.6552 0.6288 0.7498 0.0005 -0.0011 -0.0109 18 THR A N 134 C CA . THR A 18 ? 0.6140 0.6121 0.7258 0.0008 0.0001 -0.0067 18 THR A CA 135 C C . THR A 18 ? 0.6154 0.6312 0.7289 -0.0101 0.0018 -0.0045 18 THR A C 136 O O . THR A 18 ? 0.6737 0.6840 0.7761 -0.0213 0.0020 -0.0067 18 THR A O 137 C CB . THR A 18 ? 0.6222 0.6159 0.7343 0.0046 -0.0001 -0.0037 18 THR A CB 138 O OG1 . THR A 18 ? 0.6490 0.6363 0.7508 -0.0050 0.0008 -0.0014 18 THR A OG1 139 C CG2 . THR A 18 ? 0.6171 0.5959 0.7237 0.0147 -0.0024 -0.0066 18 THR A CG2 140 N N . ILE A 19 ? 0.6351 0.6725 0.7591 -0.0067 0.0031 -0.0006 19 ILE A N 141 C CA . ILE A 19 ? 0.6378 0.7021 0.7642 -0.0128 0.0043 0.0014 19 ILE A CA 142 C C . ILE A 19 ? 0.6481 0.7160 0.7665 -0.0261 0.0051 0.0017 19 ILE A C 143 O O . ILE A 19 ? 0.6637 0.7491 0.7782 -0.0395 0.0058 0.0001 19 ILE A O 144 C CB . ILE A 19 ? 0.6869 0.7697 0.8205 -0.0005 0.0058 0.0059 19 ILE A CB 145 C CG1 . ILE A 19 ? 0.7406 0.8176 0.8760 0.0087 0.0062 0.0057 19 ILE A CG1 146 C CG2 . ILE A 19 ? 0.7022 0.8199 0.8375 -0.0022 0.0067 0.0080 19 ILE A CG2 147 C CD1 . ILE A 19 ? 0.7456 0.8364 0.8818 0.0061 0.0059 0.0040 19 ILE A CD1 148 N N . MET A 20 ? 0.6460 0.6987 0.7605 -0.0243 0.0052 0.0035 20 MET A N 149 C CA . MET A 20 ? 0.6617 0.7178 0.7671 -0.0373 0.0068 0.0045 20 MET A CA 150 C C . MET A 20 ? 0.6793 0.6992 0.7626 -0.0498 0.0069 0.0016 20 MET A C 151 O O . MET A 20 ? 0.6553 0.6738 0.7246 -0.0666 0.0091 0.0016 20 MET A O 152 C CB . MET A 20 ? 0.6883 0.7472 0.7984 -0.0282 0.0074 0.0086 20 MET A CB 153 C CG . MET A 20 ? 0.6979 0.7891 0.8205 -0.0163 0.0086 0.0119 20 MET A CG 154 S SD . MET A 20 ? 0.7518 0.8490 0.8738 -0.0103 0.0103 0.0160 20 MET A SD 155 C CE . MET A 20 ? 0.8341 0.9457 0.9620 0.0121 0.0114 0.0193 20 MET A CE 156 N N . GLU A 21 ? 0.6754 0.6650 0.7518 -0.0412 0.0049 -0.0009 21 GLU A N 157 C CA . GLU A 21 ? 0.7110 0.6583 0.7597 -0.0464 0.0050 -0.0032 21 GLU A CA 158 C C . GLU A 21 ? 0.7290 0.6553 0.7700 -0.0376 0.0033 -0.0075 21 GLU A C 159 O O . GLU A 21 ? 0.7091 0.6485 0.7681 -0.0225 0.0013 -0.0082 21 GLU A O 160 C CB . GLU A 21 ? 0.7330 0.6613 0.7759 -0.0364 0.0042 -0.0005 21 GLU A CB 161 C CG . GLU A 21 ? 0.8114 0.6928 0.8181 -0.0424 0.0052 -0.0015 21 GLU A CG 162 C CD . GLU A 21 ? 0.8721 0.7370 0.8722 -0.0312 0.0041 0.0016 21 GLU A CD 163 O OE1 . GLU A 21 ? 0.8212 0.7136 0.8461 -0.0221 0.0028 0.0042 21 GLU A OE1 164 O OE2 . GLU A 21 ? 0.8966 0.7177 0.8626 -0.0314 0.0048 0.0015 21 GLU A OE2 165 N N . LYS A 22 ? 0.7651 0.6573 0.7758 -0.0480 0.0046 -0.0108 22 LYS A N 166 C CA . LYS A 22 ? 0.8028 0.6718 0.8006 -0.0387 0.0034 -0.0154 22 LYS A CA 167 C C . LYS A 22 ? 0.7983 0.6185 0.7636 -0.0261 0.0028 -0.0163 22 LYS A C 168 O O . LYS A 22 ? 0.7955 0.5909 0.7396 -0.0323 0.0043 -0.0138 22 LYS A O 169 C CB . LYS A 22 ? 0.8798 0.7455 0.8635 -0.0585 0.0057 -0.0192 22 LYS A CB 170 C CG . LYS A 22 ? 0.9072 0.8256 0.9217 -0.0672 0.0057 -0.0181 22 LYS A CG 171 C CD . LYS A 22 ? 1.0152 0.9376 1.0184 -0.0856 0.0072 -0.0226 22 LYS A CD 172 C CE . LYS A 22 ? 1.0586 0.9854 1.0716 -0.0725 0.0054 -0.0257 22 LYS A CE 173 N NZ . LYS A 22 ? 1.0798 1.0124 1.0819 -0.0907 0.0066 -0.0304 22 LYS A NZ 174 N N . ASN A 23 ? 0.8067 0.6153 0.7671 -0.0065 0.0007 -0.0198 23 ASN A N 175 C CA . ASN A 23 ? 0.8631 0.6257 0.7879 0.0113 -0.0002 -0.0212 23 ASN A CA 176 C C . ASN A 23 ? 0.8308 0.5914 0.7567 0.0224 -0.0018 -0.0171 23 ASN A C 177 O O . ASN A 23 ? 0.8716 0.5877 0.7602 0.0233 -0.0006 -0.0156 23 ASN A O 178 C CB . ASN A 23 ? 0.9622 0.6676 0.8362 -0.0034 0.0036 -0.0232 23 ASN A CB 179 C CG . ASN A 23 ? 1.0395 0.7411 0.9064 -0.0116 0.0050 -0.0284 23 ASN A CG 180 O OD1 . ASN A 23 ? 1.0245 0.7627 0.9222 -0.0012 0.0027 -0.0305 23 ASN A OD1 181 N ND2 . ASN A 23 ? 1.2035 0.8593 1.0270 -0.0320 0.0091 -0.0308 23 ASN A ND2 182 N N . VAL A 24 ? 0.7914 0.5974 0.7564 0.0300 -0.0043 -0.0155 24 VAL A N 183 C CA . VAL A 24 ? 0.7564 0.5684 0.7271 0.0422 -0.0065 -0.0126 24 VAL A CA 184 C C . VAL A 24 ? 0.7652 0.5734 0.7269 0.0704 -0.0101 -0.0162 24 VAL A C 185 O O . VAL A 24 ? 0.7662 0.6045 0.7481 0.0796 -0.0117 -0.0201 24 VAL A O 186 C CB . VAL A 24 ? 0.7156 0.5760 0.7278 0.0374 -0.0070 -0.0105 24 VAL A CB 187 C CG1 . VAL A 24 ? 0.7249 0.5923 0.7422 0.0489 -0.0093 -0.0084 24 VAL A CG1 188 C CG2 . VAL A 24 ? 0.6984 0.5701 0.7199 0.0148 -0.0038 -0.0071 24 VAL A CG2 189 N N . THR A 25 ? 0.7766 0.5501 0.7062 0.0849 -0.0112 -0.0150 25 THR A N 190 C CA . THR A 25 ? 0.7821 0.5568 0.7002 0.1160 -0.0151 -0.0186 25 THR A CA 191 C C . THR A 25 ? 0.7482 0.5751 0.7018 0.1250 -0.0187 -0.0191 25 THR A C 192 O O . THR A 25 ? 0.7545 0.5870 0.7169 0.1172 -0.0188 -0.0151 25 THR A O 193 C CB . THR A 25 ? 0.8385 0.5565 0.7051 0.1326 -0.0153 -0.0167 25 THR A CB 194 O OG1 . THR A 25 ? 0.9203 0.5808 0.7460 0.1182 -0.0107 -0.0161 25 THR A OG1 195 C CG2 . THR A 25 ? 0.8641 0.5857 0.7151 0.1693 -0.0194 -0.0211 25 THR A CG2 196 N N . VAL A 26 ? 0.7207 0.5860 0.6923 0.1400 -0.0212 -0.0246 26 VAL A N 197 C CA . VAL A 26 ? 0.6762 0.5940 0.6784 0.1449 -0.0240 -0.0268 26 VAL A CA 198 C C . VAL A 26 ? 0.6935 0.6313 0.6853 0.1758 -0.0284 -0.0320 26 VAL A C 199 O O . VAL A 26 ? 0.7593 0.6779 0.7256 0.1956 -0.0290 -0.0350 26 VAL A O 200 C CB . VAL A 26 ? 0.6314 0.5917 0.6705 0.1277 -0.0222 -0.0293 26 VAL A CB 201 C CG1 . VAL A 26 ? 0.6223 0.5704 0.6723 0.1017 -0.0185 -0.0238 26 VAL A CG1 202 C CG2 . VAL A 26 ? 0.6359 0.6048 0.6740 0.1349 -0.0217 -0.0345 26 VAL A CG2 203 N N . THR A 27 ? 0.6672 0.6463 0.6775 0.1802 -0.0313 -0.0337 27 THR A N 204 C CA . THR A 27 ? 0.6636 0.6747 0.6670 0.2098 -0.0361 -0.0391 27 THR A CA 205 C C . THR A 27 ? 0.6527 0.7132 0.6740 0.2164 -0.0365 -0.0470 27 THR A C 206 O O . THR A 27 ? 0.7036 0.7806 0.7095 0.2464 -0.0396 -0.0520 27 THR A O 207 C CB . THR A 27 ? 0.6478 0.6966 0.6682 0.2080 -0.0390 -0.0395 27 THR A CB 208 O OG1 . THR A 27 ? 0.5902 0.6820 0.6475 0.1814 -0.0368 -0.0421 27 THR A OG1 209 C CG2 . THR A 27 ? 0.6615 0.6650 0.6644 0.2025 -0.0386 -0.0318 27 THR A CG2 210 N N . HIS A 28 ? 0.6188 0.7042 0.6706 0.1895 -0.0331 -0.0483 28 HIS A N 211 C CA . HIS A 28 ? 0.5862 0.7158 0.6551 0.1895 -0.0321 -0.0555 28 HIS A CA 212 C C . HIS A 28 ? 0.5888 0.7053 0.6720 0.1628 -0.0271 -0.0533 28 HIS A C 213 O O . HIS A 28 ? 0.5751 0.6725 0.6671 0.1401 -0.0246 -0.0477 28 HIS A O 214 C CB . HIS A 28 ? 0.5488 0.7472 0.6429 0.1842 -0.0334 -0.0620 28 HIS A CB 215 C CG . HIS A 28 ? 0.5640 0.7853 0.6484 0.2077 -0.0387 -0.0643 28 HIS A CG 216 N ND1 . HIS A 28 ? 0.5605 0.7644 0.6413 0.2027 -0.0402 -0.0593 28 HIS A ND1 217 C CD2 . HIS A 28 ? 0.5636 0.8257 0.6395 0.2386 -0.0430 -0.0710 28 HIS A CD2 218 C CE1 . HIS A 28 ? 0.5666 0.7986 0.6374 0.2285 -0.0454 -0.0628 28 HIS A CE1 219 N NE2 . HIS A 28 ? 0.5719 0.8409 0.6393 0.2517 -0.0473 -0.0699 28 HIS A NE2 220 N N . ALA A 29 ? 0.6147 0.7454 0.6998 0.1675 -0.0258 -0.0580 29 ALA A N 221 C CA . ALA A 29 ? 0.6162 0.7360 0.7117 0.1461 -0.0214 -0.0565 29 ALA A CA 222 C C . ALA A 29 ? 0.6109 0.7748 0.7184 0.1491 -0.0202 -0.0641 29 ALA A C 223 O O . ALA A 29 ? 0.6455 0.8468 0.7510 0.1699 -0.0228 -0.0707 29 ALA A O 224 C CB . ALA A 29 ? 0.6463 0.7075 0.7174 0.1482 -0.0204 -0.0520 29 ALA A CB 225 N N . GLN A 30 ? 0.6090 0.7719 0.7282 0.1290 -0.0162 -0.0634 30 GLN A N 226 C CA . GLN A 30 ? 0.6370 0.8387 0.7663 0.1288 -0.0141 -0.0702 30 GLN A CA 227 C C . GLN A 30 ? 0.6316 0.8037 0.7564 0.1204 -0.0112 -0.0680 30 GLN A C 228 O O . GLN A 30 ? 0.6182 0.7736 0.7509 0.0984 -0.0083 -0.0628 30 GLN A O 229 C CB . GLN A 30 ? 0.6331 0.8816 0.7846 0.1064 -0.0112 -0.0733 30 GLN A CB 230 C CG . GLN A 30 ? 0.6501 0.9468 0.8111 0.1044 -0.0086 -0.0814 30 GLN A CG 231 C CD . GLN A 30 ? 0.6562 0.9996 0.8326 0.0798 -0.0052 -0.0859 30 GLN A CD 232 O OE1 . GLN A 30 ? 0.6766 1.0306 0.8561 0.0725 -0.0062 -0.0857 30 GLN A OE1 233 N NE2 . GLN A 30 ? 0.6613 1.0306 0.8442 0.0652 -0.0005 -0.0902 30 GLN A NE2 234 N N . ASP A 31 ? 0.6548 0.8205 0.7642 0.1400 -0.0120 -0.0721 31 ASP A N 235 C CA . ASP A 31 ? 0.6843 0.8300 0.7891 0.1333 -0.0092 -0.0719 31 ASP A CA 236 C C . ASP A 31 ? 0.6556 0.8462 0.7831 0.1166 -0.0055 -0.0755 31 ASP A C 237 O O . ASP A 31 ? 0.6470 0.8880 0.7851 0.1213 -0.0054 -0.0819 31 ASP A O 238 C CB . ASP A 31 ? 0.7253 0.8536 0.8036 0.1610 -0.0108 -0.0766 31 ASP A CB 239 C CG . ASP A 31 ? 0.7699 0.8666 0.8367 0.1540 -0.0083 -0.0763 31 ASP A CG 240 O OD1 . ASP A 31 ? 0.7409 0.8339 0.8222 0.1290 -0.0057 -0.0725 31 ASP A OD1 241 O OD2 . ASP A 31 ? 0.8602 0.9345 0.9000 0.1755 -0.0088 -0.0803 31 ASP A OD2 242 N N . ILE A 32 ? 0.6168 0.7908 0.7495 0.0965 -0.0023 -0.0716 32 ILE A N 243 C CA . ILE A 32 ? 0.6002 0.8069 0.7478 0.0796 0.0021 -0.0741 32 ILE A CA 244 C C . ILE A 32 ? 0.6147 0.8101 0.7571 0.0780 0.0042 -0.0750 32 ILE A C 245 O O . ILE A 32 ? 0.6068 0.8204 0.7578 0.0627 0.0083 -0.0757 32 ILE A O 246 C CB . ILE A 32 ? 0.5732 0.7754 0.7305 0.0550 0.0049 -0.0682 32 ILE A CB 247 C CG1 . ILE A 32 ? 0.5757 0.7324 0.7267 0.0490 0.0043 -0.0598 32 ILE A CG1 248 C CG2 . ILE A 32 ? 0.5640 0.7861 0.7270 0.0537 0.0036 -0.0693 32 ILE A CG2 249 C CD1 . ILE A 32 ? 0.5536 0.7032 0.7092 0.0294 0.0077 -0.0540 32 ILE A CD1 250 N N . LEU A 33 ? 0.6330 0.7959 0.7576 0.0930 0.0019 -0.0753 33 LEU A N 251 C CA . LEU A 33 ? 0.6552 0.8031 0.7715 0.0915 0.0036 -0.0765 33 LEU A CA 252 C C . LEU A 33 ? 0.7062 0.8615 0.8075 0.1161 0.0028 -0.0844 33 LEU A C 253 O O . LEU A 33 ? 0.7360 0.8666 0.8162 0.1365 -0.0001 -0.0857 33 LEU A O 254 C CB . LEU A 33 ? 0.6616 0.7605 0.7639 0.0845 0.0025 -0.0708 33 LEU A CB 255 C CG . LEU A 33 ? 0.6752 0.7561 0.7665 0.0803 0.0039 -0.0722 33 LEU A CG 256 C CD1 . LEU A 33 ? 0.6631 0.7674 0.7722 0.0627 0.0070 -0.0702 33 LEU A CD1 257 C CD2 . LEU A 33 ? 0.7009 0.7368 0.7738 0.0732 0.0025 -0.0683 33 LEU A CD2 258 N N . GLU A 34 ? 0.7379 0.9245 0.8462 0.1153 0.0056 -0.0896 34 GLU A N 259 C CA . GLU A 34 ? 0.7699 0.9655 0.8626 0.1404 0.0053 -0.0974 34 GLU A CA 260 C C . GLU A 34 ? 0.7702 0.9147 0.8382 0.1431 0.0054 -0.0969 34 GLU A C 261 O O . GLU A 34 ? 0.7548 0.8922 0.8287 0.1240 0.0076 -0.0945 34 GLU A O 262 C CB . GLU A 34 ? 0.7621 1.0162 0.8717 0.1376 0.0089 -0.1040 34 GLU A CB 263 C CG . GLU A 34 ? 0.7853 1.0555 0.8791 0.1664 0.0088 -0.1127 34 GLU A CG 264 C CD . GLU A 34 ? 0.8314 1.0950 0.9056 0.1996 0.0046 -0.1156 34 GLU A CD 265 O OE1 . GLU A 34 ? 0.8380 1.1442 0.9259 0.2046 0.0031 -0.1175 34 GLU A OE1 266 O OE2 . GLU A 34 ? 0.8869 1.1000 0.9286 0.2200 0.0031 -0.1161 34 GLU A OE2 267 N N . LYS A 35 ? 0.8042 0.9120 0.8409 0.1668 0.0032 -0.0992 35 LYS A N 268 C CA . LYS A 35 ? 0.8503 0.9003 0.8551 0.1668 0.0036 -0.0993 35 LYS A CA 269 C C . LYS A 35 ? 0.8932 0.9389 0.8731 0.1912 0.0049 -0.1075 35 LYS A C 270 O O . LYS A 35 ? 0.9281 0.9307 0.8825 0.1871 0.0063 -0.1088 35 LYS A O 271 C CB . LYS A 35 ? 0.8963 0.8899 0.8725 0.1708 0.0014 -0.0952 35 LYS A CB 272 C CG . LYS A 35 ? 0.8931 0.8736 0.8847 0.1413 0.0011 -0.0870 35 LYS A CG 273 C CD . LYS A 35 ? 0.9484 0.8789 0.9120 0.1443 -0.0006 -0.0834 35 LYS A CD 274 C CE . LYS A 35 ? 0.9570 0.9107 0.9420 0.1444 -0.0028 -0.0788 35 LYS A CE 275 N NZ . LYS A 35 ? 0.9411 0.9432 0.9411 0.1666 -0.0042 -0.0831 35 LYS A NZ 276 N N . THR A 36 ? 0.8745 0.9673 0.8605 0.2159 0.0047 -0.1137 36 THR A N 277 C CA . THR A 36 ? 0.9257 1.0175 0.8853 0.2452 0.0059 -0.1220 36 THR A CA 278 C C . THR A 36 ? 0.9066 1.0604 0.8924 0.2407 0.0090 -0.1274 36 THR A C 279 O O . THR A 36 ? 0.8394 1.0471 0.8627 0.2209 0.0102 -0.1260 36 THR A O 280 C CB . THR A 36 ? 0.9600 1.0599 0.8975 0.2861 0.0033 -0.1264 36 THR A CB 281 O OG1 . THR A 36 ? 0.9414 1.1237 0.9156 0.2897 0.0027 -0.1294 36 THR A OG1 282 C CG2 . THR A 36 ? 0.9897 1.0314 0.9009 0.2908 0.0005 -0.1206 36 THR A CG2 283 N N . HIS A 37 ? 0.9386 1.0795 0.8995 0.2586 0.0109 -0.1338 37 HIS A N 284 C CA . HIS A 37 ? 0.9205 1.1185 0.8982 0.2615 0.0142 -0.1406 37 HIS A CA 285 C C . HIS A 37 ? 0.9855 1.1761 0.9260 0.3046 0.0145 -0.1495 37 HIS A C 286 O O . HIS A 37 ? 1.0447 1.1732 0.9423 0.3274 0.0126 -0.1494 37 HIS A O 287 C CB . HIS A 37 ? 0.8906 1.0745 0.8777 0.2303 0.0172 -0.1380 37 HIS A CB 288 C CG . HIS A 37 ? 0.9334 1.0426 0.8823 0.2305 0.0171 -0.1376 37 HIS A CG 289 N ND1 . HIS A 37 ? 0.9705 1.0626 0.8906 0.2482 0.0192 -0.1448 37 HIS A ND1 290 C CD2 . HIS A 37 ? 0.9546 1.0034 0.8876 0.2127 0.0155 -0.1315 37 HIS A CD2 291 C CE1 . HIS A 37 ? 1.0016 1.0227 0.8877 0.2398 0.0191 -0.1433 37 HIS A CE1 292 N NE2 . HIS A 37 ? 0.9992 0.9955 0.8932 0.2172 0.0169 -0.1355 37 HIS A NE2 293 N N . ASN A 38 ? 0.9884 1.2396 0.9409 0.3162 0.0173 -0.1572 38 ASN A N 294 C CA . ASN A 38 ? 1.0407 1.2938 0.9580 0.3617 0.0178 -0.1664 38 ASN A CA 295 C C . ASN A 38 ? 1.0902 1.2899 0.9736 0.3653 0.0207 -0.1696 38 ASN A C 296 O O . ASN A 38 ? 1.1399 1.3191 0.9825 0.4044 0.0213 -0.1765 38 ASN A O 297 C CB . ASN A 38 ? 1.0006 1.3563 0.9457 0.3778 0.0194 -0.1746 38 ASN A CB 298 C CG . ASN A 38 ? 0.9631 1.3685 0.9377 0.3510 0.0244 -0.1776 38 ASN A CG 299 O OD1 . ASN A 38 ? 0.9722 1.3369 0.9480 0.3220 0.0263 -0.1731 38 ASN A OD1 300 N ND2 . ASN A 38 ? 0.9213 1.4179 0.9185 0.3603 0.0267 -0.1855 38 ASN A ND2 301 N N . GLY A 39 ? 1.0752 1.2550 0.9738 0.3262 0.0225 -0.1650 39 GLY A N 302 C CA . GLY A 39 ? 1.1128 1.2338 0.9781 0.3228 0.0247 -0.1672 39 GLY A CA 303 C C . GLY A 39 ? 1.1146 1.2787 0.9837 0.3325 0.0287 -0.1753 39 GLY A C 304 O O . GLY A 39 ? 1.1290 1.2471 0.9616 0.3420 0.0306 -0.1797 39 GLY A O 305 N N . LYS A 40 ? 1.0799 1.3317 0.9913 0.3275 0.0304 -0.1775 40 LYS A N 306 C CA . LYS A 40 ? 1.0701 1.3773 0.9881 0.3382 0.0347 -0.1859 40 LYS A CA 307 C C . LYS A 40 ? 1.0233 1.3877 0.9871 0.2983 0.0382 -0.1831 40 LYS A C 308 O O . LYS A 40 ? 1.0153 1.3962 1.0092 0.2702 0.0373 -0.1761 40 LYS A O 309 C CB . LYS A 40 ? 1.0921 1.4610 1.0073 0.3802 0.0345 -0.1943 40 LYS A CB 310 C CG . LYS A 40 ? 1.1729 1.4831 1.0335 0.4274 0.0319 -0.1978 40 LYS A CG 311 C CD . LYS A 40 ? 1.1790 1.5563 1.0366 0.4734 0.0309 -0.2057 40 LYS A CD 312 C CE . LYS A 40 ? 1.2583 1.5652 1.0585 0.5186 0.0275 -0.2062 40 LYS A CE 313 N NZ . LYS A 40 ? 1.3185 1.6786 1.0985 0.5762 0.0272 -0.2159 40 LYS A NZ 314 N N . LEU A 41 ? 1.0454 1.4355 1.0098 0.2967 0.0426 -0.1886 41 LEU A N 315 C CA . LEU A 41 ? 1.0143 1.4669 1.0158 0.2647 0.0473 -0.1878 41 LEU A CA 316 C C . LEU A 41 ? 0.9649 1.5097 0.9838 0.2821 0.0500 -0.1965 41 LEU A C 317 O O . LEU A 41 ? 0.9798 1.5444 0.9782 0.3217 0.0503 -0.2057 41 LEU A O 318 C CB . LEU A 41 ? 1.0504 1.4857 1.0423 0.2533 0.0509 -0.1894 41 LEU A CB 319 C CG . LEU A 41 ? 1.1019 1.4529 1.0741 0.2371 0.0480 -0.1825 41 LEU A CG 320 C CD1 . LEU A 41 ? 1.1254 1.4628 1.0830 0.2323 0.0513 -0.1862 41 LEU A CD1 321 C CD2 . LEU A 41 ? 1.0591 1.3989 1.0570 0.1995 0.0464 -0.1713 41 LEU A CD2 322 N N . CYS A 42 ? 0.9002 1.5016 0.9537 0.2530 0.0523 -0.1942 42 CYS A N 323 C CA . CYS A 42 ? 0.8962 1.5902 0.9679 0.2647 0.0544 -0.2025 42 CYS A CA 324 C C . CYS A 42 ? 0.8299 1.5904 0.9304 0.2254 0.0614 -0.2038 42 CYS A C 325 O O . CYS A 42 ? 0.7912 1.5199 0.8991 0.1876 0.0639 -0.1959 42 CYS A O 326 C CB . CYS A 42 ? 0.9266 1.6240 1.0056 0.2714 0.0492 -0.1995 42 CYS A CB 327 S SG . CYS A 42 ? 0.9772 1.5927 1.0169 0.3157 0.0416 -0.1973 42 CYS A SG 328 N N . ASP A 43 ? 0.8223 1.6761 0.9359 0.2348 0.0648 -0.2140 43 ASP A N 329 C CA . ASP A 43 ? 0.7917 1.7160 0.9300 0.1942 0.0722 -0.2165 43 ASP A CA 330 C C . ASP A 43 ? 0.7595 1.6652 0.9127 0.1576 0.0714 -0.2077 43 ASP A C 331 O O . ASP A 43 ? 0.7470 1.6443 0.9022 0.1718 0.0655 -0.2059 43 ASP A O 332 C CB . ASP A 43 ? 0.7946 1.8314 0.9446 0.2117 0.0752 -0.2302 43 ASP A CB 333 C CG . ASP A 43 ? 0.8110 1.8761 0.9454 0.2509 0.0769 -0.2400 43 ASP A CG 334 O OD1 . ASP A 43 ? 0.8235 1.8263 0.9397 0.2551 0.0774 -0.2368 43 ASP A OD1 335 O OD2 . ASP A 43 ? 0.8215 1.9741 0.9605 0.2788 0.0775 -0.2515 43 ASP A OD2 336 N N . LEU A 44 ? 0.7689 1.6638 0.9283 0.1122 0.0774 -0.2022 44 LEU A N 337 C CA . LEU A 44 ? 0.7805 1.6585 0.9493 0.0754 0.0782 -0.1945 44 LEU A CA 338 C C . LEU A 44 ? 0.8064 1.7745 0.9896 0.0481 0.0853 -0.2028 44 LEU A C 339 O O . LEU A 44 ? 0.8062 1.8047 0.9886 0.0177 0.0940 -0.2055 44 LEU A O 340 C CB . LEU A 44 ? 0.7794 1.5860 0.9391 0.0435 0.0811 -0.1831 44 LEU A CB 341 C CG . LEU A 44 ? 0.7950 1.5744 0.9570 0.0049 0.0832 -0.1743 44 LEU A CG 342 C CD1 . LEU A 44 ? 0.8091 1.5548 0.9752 0.0193 0.0751 -0.1692 44 LEU A CD1 343 C CD2 . LEU A 44 ? 0.7912 1.5051 0.9394 -0.0196 0.0864 -0.1638 44 LEU A CD2 344 N N . ASP A 45 ? 0.8607 1.8727 1.0550 0.0577 0.0817 -0.2072 45 ASP A N 345 C CA . ASP A 45 ? 0.8980 1.9958 1.1054 0.0271 0.0878 -0.2153 45 ASP A CA 346 C C . ASP A 45 ? 0.8661 2.0611 1.0792 0.0338 0.0938 -0.2291 45 ASP A C 347 O O . ASP A 45 ? 0.8296 2.0820 1.0468 -0.0067 0.1031 -0.2348 45 ASP A O 348 C CB . ASP A 45 ? 0.9556 2.0159 1.1567 -0.0294 0.0952 -0.2076 45 ASP A CB 349 C CG . ASP A 45 ? 1.0096 2.1186 1.2182 -0.0615 0.0983 -0.2116 45 ASP A CG 350 O OD1 . ASP A 45 ? 1.0862 2.1614 1.2974 -0.0560 0.0921 -0.2061 45 ASP A OD1 351 O OD2 . ASP A 45 ? 1.0521 2.2325 1.2622 -0.0943 0.1075 -0.2206 45 ASP A OD2 352 N N . GLY A 46 ? 0.8615 2.0716 1.0711 0.0849 0.0890 -0.2347 46 GLY A N 353 C CA . GLY A 46 ? 0.8320 2.1309 1.0447 0.1007 0.0939 -0.2478 46 GLY A CA 354 C C . GLY A 46 ? 0.8353 2.0971 1.0352 0.0976 0.0987 -0.2458 46 GLY A C 355 O O . GLY A 46 ? 0.8284 2.1243 1.0227 0.1335 0.0988 -0.2538 46 GLY A O 356 N N . VAL A 47 ? 0.8177 2.0089 1.0107 0.0571 0.1026 -0.2350 47 VAL A N 357 C CA . VAL A 47 ? 0.7959 1.9546 0.9767 0.0458 0.1080 -0.2324 47 VAL A CA 358 C C . VAL A 47 ? 0.8048 1.8753 0.9699 0.0815 0.1007 -0.2256 47 VAL A C 359 O O . VAL A 47 ? 0.8307 1.8173 0.9896 0.0766 0.0955 -0.2142 47 VAL A O 360 C CB . VAL A 47 ? 0.7819 1.8990 0.9564 -0.0110 0.1154 -0.2233 47 VAL A CB 361 C CG1 . VAL A 47 ? 0.8113 1.8943 0.9713 -0.0208 0.1207 -0.2201 47 VAL A CG1 362 C CG2 . VAL A 47 ? 0.7653 1.9617 0.9480 -0.0528 0.1240 -0.2304 47 VAL A CG2 363 N N . LYS A 48 ? 0.8133 1.9046 0.9699 0.1154 0.1008 -0.2333 48 LYS A N 364 C CA . LYS A 48 ? 0.8438 1.8562 0.9801 0.1500 0.0947 -0.2293 48 LYS A CA 365 C C . LYS A 48 ? 0.8338 1.7682 0.9598 0.1216 0.0965 -0.2187 48 LYS A C 366 O O . LYS A 48 ? 0.8242 1.7789 0.9534 0.0860 0.1044 -0.2179 48 LYS A O 367 C CB . LYS A 48 ? 0.8839 1.9432 1.0095 0.1920 0.0959 -0.2415 48 LYS A CB 368 C CG . LYS A 48 ? 0.9310 1.9103 1.0284 0.2310 0.0901 -0.2397 48 LYS A CG 369 C CD . LYS A 48 ? 0.9728 1.9941 1.0547 0.2704 0.0927 -0.2518 48 LYS A CD 370 C CE . LYS A 48 ? 1.0156 1.9438 1.0633 0.2985 0.0885 -0.2493 48 LYS A CE 371 N NZ . LYS A 48 ? 1.0796 2.0376 1.1043 0.3464 0.0900 -0.2614 48 LYS A NZ 372 N N . PRO A 49 ? 0.8388 1.6847 0.9497 0.1370 0.0894 -0.2109 49 PRO A N 373 C CA . PRO A 49 ? 0.8245 1.6029 0.9251 0.1143 0.0902 -0.2017 49 PRO A CA 374 C C . PRO A 49 ? 0.8113 1.5893 0.8968 0.1277 0.0933 -0.2072 49 PRO A C 375 O O . PRO A 49 ? 0.8100 1.6196 0.8873 0.1633 0.0929 -0.2174 49 PRO A O 376 C CB . PRO A 49 ? 0.8170 1.5133 0.9069 0.1281 0.0813 -0.1936 49 PRO A CB 377 C CG . PRO A 49 ? 0.8426 1.5524 0.9241 0.1719 0.0766 -0.2015 49 PRO A CG 378 C CD . PRO A 49 ? 0.8391 1.6424 0.9400 0.1721 0.0805 -0.2096 49 PRO A CD 379 N N . LEU A 50 ? 0.7927 1.5334 0.8721 0.1014 0.0961 -0.2004 50 LEU A N 380 C CA . LEU A 50 ? 0.8009 1.5250 0.8633 0.1123 0.0978 -0.2039 50 LEU A CA 381 C C . LEU A 50 ? 0.8272 1.4724 0.8699 0.1344 0.0897 -0.2005 50 LEU A C 382 O O . LEU A 50 ? 0.8277 1.4153 0.8687 0.1167 0.0858 -0.1903 50 LEU A O 383 C CB . LEU A 50 ? 0.7895 1.5050 0.8508 0.0749 0.1040 -0.1975 50 LEU A CB 384 C CG . LEU A 50 ? 0.8030 1.4995 0.8470 0.0807 0.1060 -0.1998 50 LEU A CG 385 C CD1 . LEU A 50 ? 0.8160 1.5717 0.8562 0.1075 0.1100 -0.2136 50 LEU A CD1 386 C CD2 . LEU A 50 ? 0.8085 1.4985 0.8503 0.0428 0.1123 -0.1923 50 LEU A CD2 387 N N . ILE A 51 ? 0.8607 1.5035 0.8853 0.1728 0.0875 -0.2096 51 ILE A N 388 C CA . ILE A 51 ? 0.9025 1.4670 0.9004 0.1926 0.0809 -0.2081 51 ILE A CA 389 C C . ILE A 51 ? 0.9248 1.4653 0.9009 0.1962 0.0831 -0.2119 51 ILE A C 390 O O . ILE A 51 ? 0.9330 1.4950 0.8925 0.2250 0.0857 -0.2223 51 ILE A O 391 C CB . ILE A 51 ? 0.9341 1.4939 0.9163 0.2342 0.0768 -0.2146 51 ILE A CB 392 C CG1 . ILE A 51 ? 0.9392 1.5202 0.9442 0.2267 0.0741 -0.2097 51 ILE A CG1 393 C CG2 . ILE A 51 ? 0.9690 1.4407 0.9143 0.2519 0.0715 -0.2140 51 ILE A CG2 394 C CD1 . ILE A 51 ? 0.9901 1.5558 0.9781 0.2653 0.0690 -0.2135 51 ILE A CD1 395 N N . LEU A 52 ? 0.9182 1.4151 0.8929 0.1683 0.0820 -0.2036 52 LEU A N 396 C CA . LEU A 52 ? 0.9351 1.4127 0.8920 0.1648 0.0841 -0.2061 52 LEU A CA 397 C C . LEU A 52 ? 0.9905 1.4133 0.9107 0.1930 0.0806 -0.2130 52 LEU A C 398 O O . LEU A 52 ? 1.0144 1.4273 0.9156 0.1970 0.0830 -0.2182 52 LEU A O 399 C CB . LEU A 52 ? 0.8996 1.3469 0.8635 0.1294 0.0830 -0.1950 52 LEU A CB 400 C CG . LEU A 52 ? 0.8671 1.3555 0.8561 0.0992 0.0880 -0.1877 52 LEU A CG 401 C CD1 . LEU A 52 ? 0.8590 1.3077 0.8475 0.0718 0.0858 -0.1761 52 LEU A CD1 402 C CD2 . LEU A 52 ? 0.8746 1.4233 0.8670 0.0964 0.0967 -0.1946 52 LEU A CD2 403 N N . ARG A 53 ? 1.0222 1.4054 0.9283 0.2111 0.0754 -0.2130 53 ARG A N 404 C CA . ARG A 53 ? 1.1183 1.4418 0.9807 0.2390 0.0730 -0.2201 53 ARG A CA 405 C C . ARG A 53 ? 1.1607 1.4243 1.0022 0.2178 0.0709 -0.2176 53 ARG A C 406 O O . ARG A 53 ? 1.1727 1.4070 1.0238 0.1914 0.0668 -0.2087 53 ARG A O 407 C CB . ARG A 53 ? 1.1806 1.5390 1.0248 0.2762 0.0776 -0.2325 53 ARG A CB 408 C CG . ARG A 53 ? 1.2734 1.5737 1.0678 0.3159 0.0756 -0.2402 53 ARG A CG 409 C CD . ARG A 53 ? 1.3439 1.6723 1.1142 0.3528 0.0807 -0.2526 53 ARG A CD 410 N NE . ARG A 53 ? 1.3846 1.7276 1.1368 0.3991 0.0804 -0.2592 53 ARG A NE 411 C CZ . ARG A 53 ? 1.3678 1.7922 1.1535 0.4099 0.0813 -0.2600 53 ARG A CZ 412 N NH1 . ARG A 53 ? 1.3143 1.8085 1.1512 0.3749 0.0835 -0.2549 53 ARG A NH1 413 N NH2 . ARG A 53 ? 1.4164 1.8516 1.1806 0.4561 0.0804 -0.2664 53 ARG A NH2 414 N N . ASP A 54 ? 1.2005 1.4501 1.0139 0.2289 0.0737 -0.2258 54 ASP A N 415 C CA . ASP A 54 ? 1.2198 1.4198 1.0128 0.2075 0.0720 -0.2248 54 ASP A CA 416 C C . ASP A 54 ? 1.1775 1.4161 0.9981 0.1780 0.0742 -0.2194 54 ASP A C 417 O O . ASP A 54 ? 1.2002 1.4074 1.0092 0.1581 0.0721 -0.2175 54 ASP A O 418 C CB . ASP A 54 ? 1.2906 1.4479 1.0331 0.2328 0.0740 -0.2367 54 ASP A CB 419 C CG . ASP A 54 ? 1.3367 1.4334 1.0373 0.2602 0.0719 -0.2414 54 ASP A CG 420 O OD1 . ASP A 54 ? 1.3093 1.3712 1.0112 0.2472 0.0674 -0.2348 54 ASP A OD1 421 O OD2 . ASP A 54 ? 1.3789 1.4608 1.0418 0.2959 0.0751 -0.2518 54 ASP A OD2 422 N N . CYS A 55 ? 1.1415 1.4474 0.9950 0.1743 0.0787 -0.2172 55 CYS A N 423 C CA . CYS A 55 ? 1.1276 1.4656 1.0017 0.1465 0.0818 -0.2114 55 CYS A CA 424 C C . CYS A 55 ? 1.0614 1.3951 0.9606 0.1173 0.0785 -0.1981 55 CYS A C 425 O O . CYS A 55 ? 1.0514 1.3760 0.9610 0.1185 0.0751 -0.1939 55 CYS A O 426 C CB . CYS A 55 ? 1.1154 1.5248 1.0063 0.1520 0.0896 -0.2158 55 CYS A CB 427 S SG . CYS A 55 ? 1.2152 1.6400 1.0770 0.1870 0.0946 -0.2314 55 CYS A SG 428 N N . SER A 56 ? 1.0280 1.3669 0.9337 0.0933 0.0796 -0.1916 56 SER A N 429 C CA . SER A 56 ? 0.9908 1.3284 0.9161 0.0685 0.0775 -0.1789 56 SER A CA 430 C C . SER A 56 ? 0.9638 1.3489 0.9062 0.0543 0.0849 -0.1748 56 SER A C 431 O O . SER A 56 ? 0.9525 1.3738 0.8927 0.0606 0.0913 -0.1819 56 SER A O 432 C CB . SER A 56 ? 1.0066 1.3102 0.9204 0.0530 0.0729 -0.1737 56 SER A CB 433 O OG . SER A 56 ? 1.0218 1.3428 0.9289 0.0457 0.0772 -0.1744 56 SER A OG 434 N N . VAL A 57 ? 0.9441 1.3268 0.8996 0.0343 0.0845 -0.1635 57 VAL A N 435 C CA . VAL A 57 ? 0.9197 1.3365 0.8838 0.0163 0.0922 -0.1587 57 VAL A CA 436 C C . VAL A 57 ? 0.9289 1.3540 0.8788 0.0083 0.0971 -0.1594 57 VAL A C 437 O O . VAL A 57 ? 0.9063 1.3691 0.8570 0.0000 0.1056 -0.1620 57 VAL A O 438 C CB . VAL A 57 ? 0.8831 1.2816 0.8548 -0.0023 0.0907 -0.1458 57 VAL A CB 439 C CG1 . VAL A 57 ? 0.8766 1.2976 0.8465 -0.0240 0.0997 -0.1406 57 VAL A CG1 440 C CG2 . VAL A 57 ? 0.8806 1.2766 0.8671 0.0051 0.0868 -0.1458 57 VAL A CG2 441 N N . ALA A 58 ? 0.9451 1.3375 0.8811 0.0096 0.0919 -0.1578 58 ALA A N 442 C CA . ALA A 58 ? 0.9667 1.3637 0.8872 0.0045 0.0953 -0.1590 58 ALA A CA 443 C C . ALA A 58 ? 0.9762 1.3992 0.8897 0.0206 0.0997 -0.1725 58 ALA A C 444 O O . ALA A 58 ? 0.9800 1.4369 0.8912 0.0144 0.1078 -0.1749 58 ALA A O 445 C CB . ALA A 58 ? 0.9698 1.3299 0.8775 0.0026 0.0877 -0.1551 58 ALA A CB 446 N N . GLY A 59 ? 0.9646 1.3699 0.8710 0.0414 0.0949 -0.1814 59 GLY A N 447 C CA . GLY A 59 ? 0.9629 1.3878 0.8580 0.0628 0.0987 -0.1947 59 GLY A CA 448 C C . GLY A 59 ? 0.9658 1.4496 0.8762 0.0663 0.1068 -0.1989 59 GLY A C 449 O O . GLY A 59 ? 1.0070 1.5259 0.9113 0.0734 0.1133 -0.2069 59 GLY A O 450 N N . TRP A 60 ? 0.9269 1.4250 0.8568 0.0600 0.1067 -0.1940 60 TRP A N 451 C CA . TRP A 60 ? 0.8990 1.4584 0.8446 0.0583 0.1143 -0.1980 60 TRP A CA 452 C C . TRP A 60 ? 0.9008 1.4903 0.8469 0.0305 0.1232 -0.1938 60 TRP A C 453 O O . TRP A 60 ? 0.9126 1.5512 0.8573 0.0326 0.1309 -0.2020 60 TRP A O 454 C CB . TRP A 60 ? 0.8849 1.4469 0.8489 0.0549 0.1114 -0.1933 60 TRP A CB 455 C CG . TRP A 60 ? 0.8644 1.4874 0.8451 0.0404 0.1193 -0.1946 60 TRP A CG 456 C CD1 . TRP A 60 ? 0.8725 1.5610 0.8566 0.0453 0.1272 -0.2048 60 TRP A CD1 457 C CD2 . TRP A 60 ? 0.8344 1.4604 0.8285 0.0171 0.1204 -0.1862 60 TRP A CD2 458 N NE1 . TRP A 60 ? 0.8583 1.5931 0.8575 0.0233 0.1333 -0.2036 60 TRP A NE1 459 C CE2 . TRP A 60 ? 0.8330 1.5267 0.8370 0.0056 0.1293 -0.1922 60 TRP A CE2 460 C CE3 . TRP A 60 ? 0.8260 1.4052 0.8230 0.0047 0.1150 -0.1747 60 TRP A CE3 461 C CZ2 . TRP A 60 ? 0.8316 1.5426 0.8456 -0.0204 0.1332 -0.1873 60 TRP A CZ2 462 C CZ3 . TRP A 60 ? 0.8088 1.4030 0.8157 -0.0175 0.1187 -0.1694 60 TRP A CZ3 463 C CH2 . TRP A 60 ? 0.8141 1.4712 0.8281 -0.0310 0.1277 -0.1757 60 TRP A CH2 464 N N . LEU A 61 ? 0.8967 1.4555 0.8413 0.0055 0.1225 -0.1811 61 LEU A N 465 C CA . LEU A 61 ? 0.8992 1.4764 0.8379 -0.0232 0.1317 -0.1754 61 LEU A CA 466 C C . LEU A 61 ? 0.9245 1.5069 0.8456 -0.0250 0.1362 -0.1783 61 LEU A C 467 O O . LEU A 61 ? 0.9236 1.5481 0.8411 -0.0383 0.1462 -0.1819 61 LEU A O 468 C CB . LEU A 61 ? 0.8847 1.4184 0.8187 -0.0443 0.1295 -0.1605 61 LEU A CB 469 C CG . LEU A 61 ? 0.8649 1.4006 0.8142 -0.0509 0.1284 -0.1568 61 LEU A CG 470 C CD1 . LEU A 61 ? 0.8770 1.3653 0.8157 -0.0689 0.1267 -0.1421 61 LEU A CD1 471 C CD2 . LEU A 61 ? 0.8547 1.4491 0.8124 -0.0646 0.1382 -0.1633 61 LEU A CD2 472 N N . LEU A 62 ? 0.9386 1.4803 0.8478 -0.0135 0.1290 -0.1772 62 LEU A N 473 C CA . LEU A 62 ? 0.9467 1.4914 0.8383 -0.0119 0.1321 -0.1811 62 LEU A CA 474 C C . LEU A 62 ? 0.9659 1.5538 0.8580 0.0089 0.1364 -0.1962 62 LEU A C 475 O O . LEU A 62 ? 0.9940 1.6043 0.8746 0.0062 0.1428 -0.2007 62 LEU A O 476 C CB . LEU A 62 ? 0.9392 1.4333 0.8178 -0.0047 0.1227 -0.1778 62 LEU A CB 477 C CG . LEU A 62 ? 0.9227 1.3804 0.7968 -0.0221 0.1188 -0.1629 62 LEU A CG 478 C CD1 . LEU A 62 ? 0.9302 1.3480 0.7981 -0.0129 0.1079 -0.1617 62 LEU A CD1 479 C CD2 . LEU A 62 ? 0.9391 1.4007 0.7958 -0.0408 0.1262 -0.1559 62 LEU A CD2 480 N N . GLY A 63 ? 0.9596 1.5587 0.8624 0.0314 0.1330 -0.2040 63 GLY A N 481 C CA . GLY A 63 ? 0.9804 1.6204 0.8807 0.0578 0.1365 -0.2186 63 GLY A CA 482 C C . GLY A 63 ? 1.0005 1.6020 0.8783 0.0831 0.1311 -0.2260 63 GLY A C 483 O O . GLY A 63 ? 1.0116 1.6344 0.8760 0.0944 0.1359 -0.2349 63 GLY A O 484 N N . ASN A 64 ? 0.9986 1.5426 0.8698 0.0900 0.1217 -0.2228 64 ASN A N 485 C CA . ASN A 64 ? 1.0206 1.5213 0.8655 0.1131 0.1166 -0.2311 64 ASN A CA 486 C C . ASN A 64 ? 1.0650 1.5977 0.9008 0.1471 0.1208 -0.2450 64 ASN A C 487 O O . ASN A 64 ? 1.0548 1.6191 0.9058 0.1592 0.1218 -0.2469 64 ASN A O 488 C CB . ASN A 64 ? 1.0163 1.4598 0.8577 0.1141 0.1071 -0.2263 64 ASN A CB 489 C CG . ASN A 64 ? 1.0383 1.4270 0.8455 0.1319 0.1024 -0.2347 64 ASN A CG 490 O OD1 . ASN A 64 ? 1.0571 1.4480 0.8429 0.1590 0.1053 -0.2465 64 ASN A OD1 491 N ND2 . ASN A 64 ? 1.0328 1.3713 0.8316 0.1166 0.0952 -0.2291 64 ASN A ND2 492 N N . PRO A 65 ? 1.1278 1.6547 0.9374 0.1642 0.1233 -0.2550 65 PRO A N 493 C CA . PRO A 65 ? 1.1757 1.7373 0.9730 0.2007 0.1281 -0.2687 65 PRO A CA 494 C C . PRO A 65 ? 1.2227 1.7524 1.0044 0.2340 0.1231 -0.2741 65 PRO A C 495 O O . PRO A 65 ? 1.2360 1.8040 1.0121 0.2671 0.1267 -0.2839 65 PRO A O 496 C CB . PRO A 65 ? 1.2077 1.7509 0.9740 0.2096 0.1306 -0.2767 65 PRO A CB 497 C CG . PRO A 65 ? 1.2032 1.6846 0.9593 0.1836 0.1243 -0.2688 65 PRO A CG 498 C CD . PRO A 65 ? 1.1512 1.6425 0.9401 0.1515 0.1221 -0.2543 65 PRO A CD 499 N N . MET A 66 ? 1.2660 1.7284 1.0388 0.2258 0.1151 -0.2679 66 MET A N 500 C CA . MET A 66 ? 1.3143 1.7405 1.0724 0.2515 0.1104 -0.2705 66 MET A CA 501 C C . MET A 66 ? 1.2712 1.7430 1.0652 0.2494 0.1099 -0.2648 66 MET A C 502 O O . MET A 66 ? 1.2775 1.7297 1.0621 0.2728 0.1065 -0.2668 66 MET A O 503 C CB . MET A 66 ? 1.3437 1.6849 1.0799 0.2372 0.1027 -0.2656 66 MET A CB 504 C CG . MET A 66 ? 1.3980 1.6848 1.0920 0.2387 0.1022 -0.2726 66 MET A CG 505 S SD . MET A 66 ? 1.4898 1.7268 1.1243 0.2878 0.1039 -0.2878 66 MET A SD 506 C CE . MET A 66 ? 1.5462 1.6983 1.1321 0.2700 0.1011 -0.2920 66 MET A CE 507 N N . CYS A 67 ? 1.2289 1.7570 1.0595 0.2205 0.1137 -0.2578 67 CYS A N 508 C CA . CYS A 67 ? 1.1889 1.7572 1.0527 0.2104 0.1136 -0.2518 67 CYS A CA 509 C C . CYS A 67 ? 1.1656 1.8265 1.0504 0.2134 0.1221 -0.2577 67 CYS A C 510 O O . CYS A 67 ? 1.1309 1.8343 1.0445 0.1863 0.1251 -0.2514 67 CYS A O 511 C CB . CYS A 67 ? 1.1436 1.6904 1.0274 0.1693 0.1109 -0.2375 67 CYS A CB 512 S SG . CYS A 67 ? 1.1759 1.6281 1.0385 0.1624 0.1011 -0.2312 67 CYS A SG 513 N N . ASP A 68 ? 1.1797 1.8715 1.0470 0.2460 0.1263 -0.2703 68 ASP A N 514 C CA . ASP A 68 ? 1.1581 1.9471 1.0433 0.2522 0.1346 -0.2782 68 ASP A CA 515 C C . ASP A 68 ? 1.1315 1.9696 1.0392 0.2619 0.1335 -0.2791 68 ASP A C 516 O O . ASP A 68 ? 1.1146 2.0363 1.0474 0.2476 0.1401 -0.2816 68 ASP A O 517 C CB . ASP A 68 ? 1.1803 1.9903 1.0384 0.2921 0.1386 -0.2923 68 ASP A CB 518 C CG . ASP A 68 ? 1.1982 1.9839 1.0394 0.2778 0.1419 -0.2928 68 ASP A CG 519 O OD1 . ASP A 68 ? 1.1795 1.9401 1.0317 0.2374 0.1415 -0.2821 68 ASP A OD1 520 O OD2 . ASP A 68 ? 1.2481 2.0394 1.0628 0.3090 0.1450 -0.3039 68 ASP A OD2 521 N N . GLU A 69 ? 1.1302 1.9168 1.0267 0.2840 0.1256 -0.2773 69 GLU A N 522 C CA . GLU A 69 ? 1.1112 1.9358 1.0279 0.2925 0.1234 -0.2768 69 GLU A CA 523 C C . GLU A 69 ? 1.0577 1.9261 1.0120 0.2452 0.1266 -0.2683 69 GLU A C 524 O O . GLU A 69 ? 1.0288 1.9723 1.0052 0.2446 0.1296 -0.2720 69 GLU A O 525 C CB . GLU A 69 ? 1.1301 1.8725 1.0286 0.3098 0.1141 -0.2720 69 GLU A CB 526 C CG . GLU A 69 ? 1.1151 1.8902 1.0306 0.3228 0.1109 -0.2715 69 GLU A CG 527 C CD . GLU A 69 ? 1.1278 1.8179 1.0219 0.3385 0.1023 -0.2664 69 GLU A CD 528 O OE1 . GLU A 69 ? 1.1633 1.7691 1.0268 0.3399 0.0990 -0.2643 69 GLU A OE1 529 O OE2 . GLU A 69 ? 1.1041 1.8132 1.0108 0.3480 0.0990 -0.2649 69 GLU A OE2 530 N N . PHE A 70 ? 1.0374 1.8585 0.9950 0.2064 0.1262 -0.2573 70 PHE A N 531 C CA . PHE A 70 ? 1.0037 1.8431 0.9866 0.1619 0.1290 -0.2475 70 PHE A CA 532 C C . PHE A 70 ? 0.9975 1.8770 0.9846 0.1295 0.1386 -0.2471 70 PHE A C 533 O O . PHE A 70 ? 0.9783 1.8323 0.9696 0.0914 0.1404 -0.2363 70 PHE A O 534 C CB . PHE A 70 ? 0.9900 1.7448 0.9701 0.1437 0.1215 -0.2342 70 PHE A CB 535 C CG . PHE A 70 ? 0.9835 1.6859 0.9516 0.1738 0.1124 -0.2346 70 PHE A CG 536 C CD1 . PHE A 70 ? 0.9482 1.6761 0.9286 0.1885 0.1098 -0.2363 70 PHE A CD1 537 C CD2 . PHE A 70 ? 0.9994 1.6279 0.9406 0.1865 0.1070 -0.2340 70 PHE A CD2 538 C CE1 . PHE A 70 ? 0.9663 1.6420 0.9311 0.2162 0.1021 -0.2364 70 PHE A CE1 539 C CE2 . PHE A 70 ? 1.0102 1.5859 0.9344 0.2110 0.0998 -0.2346 70 PHE A CE2 540 C CZ . PHE A 70 ? 0.9948 1.5920 0.9300 0.2266 0.0975 -0.2354 70 PHE A CZ 541 N N . ILE A 71 ? 1.0244 1.9661 1.0075 0.1459 0.1452 -0.2589 71 ILE A N 542 C CA . ILE A 71 ? 1.0428 2.0237 1.0259 0.1170 0.1552 -0.2598 71 ILE A CA 543 C C . ILE A 71 ? 1.0294 2.0789 1.0330 0.0797 0.1635 -0.2589 71 ILE A C 544 O O . ILE A 71 ? 1.0279 2.0819 1.0282 0.0414 0.1712 -0.2538 71 ILE A O 545 C CB . ILE A 71 ? 1.0927 2.1170 1.0622 0.1478 0.1599 -0.2733 71 ILE A CB 546 C CG1 . ILE A 71 ? 1.0951 2.1304 1.0569 0.1181 0.1685 -0.2718 71 ILE A CG1 547 C CG2 . ILE A 71 ? 1.0818 2.2044 1.0645 0.1721 0.1640 -0.2865 71 ILE A CG2 548 C CD1 . ILE A 71 ? 1.1069 2.1526 1.0487 0.1485 0.1709 -0.2824 71 ILE A CD1 549 N N . ASN A 72 ? 1.0402 2.1409 1.0613 0.0901 0.1623 -0.2639 72 ASN A N 550 C CA . ASN A 72 ? 1.0312 2.1919 1.0702 0.0512 0.1695 -0.2632 72 ASN A CA 551 C C . ASN A 72 ? 0.9895 2.1555 1.0445 0.0604 0.1628 -0.2621 72 ASN A C 552 O O . ASN A 72 ? 0.9963 2.2404 1.0647 0.0803 0.1636 -0.2728 72 ASN A O 553 C CB . ASN A 72 ? 1.0525 2.3227 1.0981 0.0457 0.1806 -0.2766 72 ASN A CB 554 C CG . ASN A 72 ? 1.0967 2.3670 1.1291 0.0081 0.1909 -0.2738 72 ASN A CG 555 O OD1 . ASN A 72 ? 1.1196 2.3328 1.1428 -0.0311 0.1930 -0.2614 72 ASN A OD1 556 N ND2 . ASN A 72 ? 1.1307 2.4639 1.1591 0.0218 0.1976 -0.2852 72 ASN A ND2 557 N N . VAL A 73 ? 0.9641 2.0491 1.0172 0.0466 0.1563 -0.2490 73 VAL A N 558 C CA . VAL A 73 ? 0.9296 2.0022 0.9949 0.0579 0.1486 -0.2464 73 VAL A CA 559 C C . VAL A 73 ? 0.8972 2.0240 0.9785 0.0203 0.1546 -0.2461 73 VAL A C 560 O O . VAL A 73 ? 0.9028 2.0190 0.9784 -0.0249 0.1619 -0.2396 73 VAL A O 561 C CB . VAL A 73 ? 0.9182 1.8849 0.9746 0.0580 0.1393 -0.2329 73 VAL A CB 562 C CG1 . VAL A 73 ? 0.9309 1.8426 0.9680 0.0900 0.1338 -0.2340 73 VAL A CG1 563 C CG2 . VAL A 73 ? 0.9156 1.8396 0.9675 0.0110 0.1432 -0.2202 73 VAL A CG2 564 N N . PRO A 74 ? 0.8726 2.0539 0.9699 0.0387 0.1515 -0.2532 74 PRO A N 565 C CA . PRO A 74 ? 0.8567 2.0885 0.9678 0.0016 0.1566 -0.2537 74 PRO A CA 566 C C . PRO A 74 ? 0.8278 1.9788 0.9368 -0.0225 0.1520 -0.2395 74 PRO A C 567 O O . PRO A 74 ? 0.7906 1.8533 0.8897 -0.0095 0.1446 -0.2296 74 PRO A O 568 C CB . PRO A 74 ? 0.8549 2.1670 0.9826 0.0380 0.1527 -0.2658 74 PRO A CB 569 C CG . PRO A 74 ? 0.8664 2.1186 0.9844 0.0920 0.1418 -0.2644 74 PRO A CG 570 C CD . PRO A 74 ? 0.8803 2.0700 0.9788 0.0943 0.1428 -0.2602 74 PRO A CD 571 N N . GLU A 75 ? 0.8253 2.0106 0.9420 -0.0583 0.1567 -0.2394 75 GLU A N 572 C CA . GLU A 75 ? 0.8204 1.9390 0.9341 -0.0820 0.1534 -0.2272 75 GLU A CA 573 C C . GLU A 75 ? 0.8164 1.8840 0.9373 -0.0420 0.1402 -0.2227 75 GLU A C 574 O O . GLU A 75 ? 0.7963 1.9088 0.9290 -0.0049 0.1350 -0.2314 75 GLU A O 575 C CB . GLU A 75 ? 0.8316 2.0132 0.9528 -0.1195 0.1603 -0.2321 75 GLU A CB 576 C CG . GLU A 75 ? 0.8486 1.9650 0.9615 -0.1504 0.1594 -0.2205 75 GLU A CG 577 C CD . GLU A 75 ? 0.8636 2.0433 0.9793 -0.1910 0.1673 -0.2269 75 GLU A CD 578 O OE1 . GLU A 75 ? 0.8920 2.1678 1.0143 -0.2038 0.1752 -0.2399 75 GLU A OE1 579 O OE2 . GLU A 75 ? 0.8936 2.0290 1.0037 -0.2113 0.1658 -0.2194 75 GLU A OE2 580 N N . TRP A 76 ? 0.8227 1.7971 0.9336 -0.0490 0.1352 -0.2091 76 TRP A N 581 C CA . TRP A 76 ? 0.8336 1.7544 0.9487 -0.0179 0.1235 -0.2039 76 TRP A CA 582 C C . TRP A 76 ? 0.8237 1.7083 0.9416 -0.0419 0.1215 -0.1946 76 TRP A C 583 O O . TRP A 76 ? 0.8525 1.7359 0.9634 -0.0831 0.1290 -0.1905 76 TRP A O 584 C CB . TRP A 76 ? 0.8365 1.6807 0.9374 0.0018 0.1178 -0.1973 76 TRP A CB 585 C CG . TRP A 76 ? 0.8511 1.6348 0.9378 -0.0298 0.1207 -0.1854 76 TRP A CG 586 C CD1 . TRP A 76 ? 0.8601 1.5787 0.9421 -0.0433 0.1167 -0.1731 76 TRP A CD1 587 C CD2 . TRP A 76 ? 0.8497 1.6335 0.9223 -0.0491 0.1284 -0.1846 76 TRP A CD2 588 N NE1 . TRP A 76 ? 0.8654 1.5438 0.9299 -0.0674 0.1212 -0.1647 76 TRP A NE1 589 C CE2 . TRP A 76 ? 0.8530 1.5685 0.9110 -0.0721 0.1284 -0.1712 76 TRP A CE2 590 C CE3 . TRP A 76 ? 0.8640 1.7002 0.9335 -0.0478 0.1354 -0.1939 76 TRP A CE3 591 C CZ2 . TRP A 76 ? 0.8771 1.5720 0.9156 -0.0928 0.1349 -0.1665 76 TRP A CZ2 592 C CZ3 . TRP A 76 ? 0.8708 1.6868 0.9228 -0.0713 0.1421 -0.1893 76 TRP A CZ3 593 C CH2 . TRP A 76 ? 0.8877 1.6322 0.9235 -0.0932 0.1417 -0.1755 76 TRP A CH2 594 N N . SER A 77 ? 0.8035 1.6560 0.9278 -0.0157 0.1118 -0.1917 77 SER A N 595 C CA . SER A 77 ? 0.7816 1.5941 0.9085 -0.0320 0.1084 -0.1827 77 SER A CA 596 C C . SER A 77 ? 0.7880 1.5087 0.9026 -0.0312 0.1033 -0.1699 77 SER A C 597 O O . SER A 77 ? 0.7973 1.4769 0.9032 -0.0592 0.1057 -0.1602 77 SER A O 598 C CB . SER A 77 ? 0.7615 1.5979 0.9023 -0.0035 0.1010 -0.1873 77 SER A CB 599 O OG . SER A 77 ? 0.7588 1.5864 0.8962 0.0410 0.0945 -0.1918 77 SER A OG 600 N N . TYR A 78 ? 0.7757 1.4657 0.8866 0.0016 0.0964 -0.1704 78 TYR A N 601 C CA . TYR A 78 ? 0.7674 1.3816 0.8663 0.0030 0.0916 -0.1605 78 TYR A CA 602 C C . TYR A 78 ? 0.7665 1.3737 0.8551 0.0264 0.0903 -0.1658 78 TYR A C 603 O O . TYR A 78 ? 0.7715 1.4276 0.8618 0.0456 0.0923 -0.1766 78 TYR A O 604 C CB . TYR A 78 ? 0.7434 1.3115 0.8455 0.0156 0.0829 -0.1543 78 TYR A CB 605 C CG . TYR A 78 ? 0.7201 1.3007 0.8252 0.0514 0.0768 -0.1617 78 TYR A CG 606 C CD1 . TYR A 78 ? 0.6910 1.3268 0.8087 0.0594 0.0773 -0.1685 78 TYR A CD1 607 C CD2 . TYR A 78 ? 0.7263 1.2615 0.8174 0.0771 0.0708 -0.1621 78 TYR A CD2 608 C CE1 . TYR A 78 ? 0.6946 1.3386 0.8100 0.0963 0.0717 -0.1747 78 TYR A CE1 609 C CE2 . TYR A 78 ? 0.7315 1.2675 0.8164 0.1110 0.0661 -0.1684 78 TYR A CE2 610 C CZ . TYR A 78 ? 0.7254 1.3150 0.8220 0.1228 0.0663 -0.1743 78 TYR A CZ 611 O OH . TYR A 78 ? 0.7260 1.3123 0.8112 0.1608 0.0614 -0.1800 78 TYR A OH 612 N N . ILE A 79 ? 0.7656 1.3144 0.8419 0.0250 0.0869 -0.1587 79 ILE A N 613 C CA . ILE A 79 ? 0.7981 1.3320 0.8608 0.0435 0.0855 -0.1634 79 ILE A CA 614 C C . ILE A 79 ? 0.8085 1.2844 0.8613 0.0628 0.0767 -0.1609 79 ILE A C 615 O O . ILE A 79 ? 0.7844 1.2216 0.8395 0.0522 0.0724 -0.1518 79 ILE A O 616 C CB . ILE A 79 ? 0.8253 1.3441 0.8778 0.0219 0.0900 -0.1583 79 ILE A CB 617 C CG1 . ILE A 79 ? 0.8386 1.4110 0.8946 -0.0002 0.1002 -0.1613 79 ILE A CG1 618 C CG2 . ILE A 79 ? 0.8562 1.3555 0.8935 0.0398 0.0879 -0.1630 79 ILE A CG2 619 C CD1 . ILE A 79 ? 0.8550 1.4041 0.8971 -0.0265 0.1053 -0.1533 79 ILE A CD1 620 N N . VAL A 80 ? 0.8418 1.3106 0.8804 0.0905 0.0745 -0.1692 80 VAL A N 621 C CA . VAL A 80 ? 0.8723 1.2813 0.8935 0.1059 0.0674 -0.1681 80 VAL A CA 622 C C . VAL A 80 ? 0.8825 1.2618 0.8821 0.1093 0.0673 -0.1712 80 VAL A C 623 O O . VAL A 80 ? 0.9244 1.3249 0.9129 0.1260 0.0706 -0.1803 80 VAL A O 624 C CB . VAL A 80 ? 0.8940 1.3038 0.9063 0.1386 0.0643 -0.1754 80 VAL A CB 625 C CG1 . VAL A 80 ? 0.9157 1.2550 0.9019 0.1506 0.0582 -0.1745 80 VAL A CG1 626 C CG2 . VAL A 80 ? 0.8730 1.3144 0.9068 0.1352 0.0638 -0.1727 80 VAL A CG2 627 N N . GLU A 81 ? 0.8910 1.2241 0.8840 0.0938 0.0633 -0.1640 81 GLU A N 628 C CA . GLU A 81 ? 0.9222 1.2260 0.8946 0.0920 0.0625 -0.1662 81 GLU A CA 629 C C . GLU A 81 ? 0.9300 1.1760 0.8831 0.0952 0.0561 -0.1655 81 GLU A C 630 O O . GLU A 81 ? 0.9548 1.1840 0.9174 0.0853 0.0523 -0.1582 81 GLU A O 631 C CB . GLU A 81 ? 0.9394 1.2500 0.9210 0.0657 0.0644 -0.1580 81 GLU A CB 632 C CG . GLU A 81 ? 1.0020 1.2919 0.9644 0.0623 0.0638 -0.1604 81 GLU A CG 633 C CD . GLU A 81 ? 1.0165 1.3061 0.9845 0.0391 0.0639 -0.1508 81 GLU A CD 634 O OE1 . GLU A 81 ? 0.9816 1.2570 0.9586 0.0276 0.0604 -0.1416 81 GLU A OE1 635 O OE2 . GLU A 81 ? 1.0352 1.3384 0.9962 0.0344 0.0677 -0.1524 81 GLU A OE2 636 N N . LYS A 82 ? 0.9636 1.1781 0.8869 0.1070 0.0554 -0.1733 82 LYS A N 637 C CA . LYS A 82 ? 1.0062 1.1622 0.9045 0.1040 0.0504 -0.1735 82 LYS A CA 638 C C . LYS A 82 ? 1.0020 1.1463 0.9070 0.0754 0.0471 -0.1657 82 LYS A C 639 O O . LYS A 82 ? 0.9508 1.1257 0.8744 0.0613 0.0488 -0.1604 82 LYS A O 640 C CB . LYS A 82 ? 1.0563 1.1763 0.9134 0.1223 0.0515 -0.1848 82 LYS A CB 641 C CG . LYS A 82 ? 1.0766 1.1983 0.9180 0.1569 0.0538 -0.1926 82 LYS A CG 642 C CD . LYS A 82 ? 1.1419 1.2117 0.9325 0.1761 0.0548 -0.2031 82 LYS A CD 643 C CE . LYS A 82 ? 1.1738 1.2524 0.9456 0.2172 0.0577 -0.2116 82 LYS A CE 644 N NZ . LYS A 82 ? 1.1937 1.2690 0.9709 0.2311 0.0551 -0.2082 82 LYS A NZ 645 N N . ALA A 83 ? 1.0424 1.1426 0.9292 0.0673 0.0427 -0.1654 83 ALA A N 646 C CA . ALA A 83 ? 1.0613 1.1544 0.9515 0.0419 0.0389 -0.1596 83 ALA A CA 647 C C . ALA A 83 ? 1.1238 1.2143 0.9961 0.0343 0.0397 -0.1648 83 ALA A C 648 O O . ALA A 83 ? 1.1133 1.2266 0.9993 0.0187 0.0386 -0.1591 83 ALA A O 649 C CB . ALA A 83 ? 1.0588 1.1107 0.9328 0.0333 0.0347 -0.1592 83 ALA A CB 650 N N . ASN A 84 ? 1.1831 1.2447 1.0221 0.0472 0.0418 -0.1756 84 ASN A N 651 C CA . ASN A 84 ? 1.2364 1.2914 1.0539 0.0407 0.0428 -0.1821 84 ASN A CA 652 C C . ASN A 84 ? 1.2332 1.2913 1.0339 0.0647 0.0481 -0.1915 84 ASN A C 653 O O . ASN A 84 ? 1.2581 1.2738 1.0183 0.0739 0.0492 -0.2014 84 ASN A O 654 C CB . ASN A 84 ? 1.3288 1.3332 1.1098 0.0251 0.0397 -0.1876 84 ASN A CB 655 C CG . ASN A 84 ? 1.3541 1.3637 1.1513 0.0004 0.0345 -0.1795 84 ASN A CG 656 O OD1 . ASN A 84 ? 1.3393 1.3894 1.1658 -0.0109 0.0326 -0.1713 84 ASN A OD1 657 N ND2 . ASN A 84 ? 1.4063 1.3741 1.1811 -0.0070 0.0327 -0.1817 84 ASN A ND2 658 N N . PRO A 85 ? 1.1928 1.3008 1.0211 0.0741 0.0520 -0.1888 85 PRO A N 659 C CA . PRO A 85 ? 1.2019 1.3233 1.0169 0.0979 0.0574 -0.1981 85 PRO A CA 660 C C . PRO A 85 ? 1.2162 1.3189 1.0018 0.0947 0.0587 -0.2058 85 PRO A C 661 O O . PRO A 85 ? 1.2264 1.3377 1.0193 0.0724 0.0569 -0.2016 85 PRO A O 662 C CB . PRO A 85 ? 1.1514 1.3359 1.0041 0.0964 0.0615 -0.1924 85 PRO A CB 663 C CG . PRO A 85 ? 1.0975 1.2909 0.9787 0.0793 0.0582 -0.1807 85 PRO A CG 664 C CD . PRO A 85 ? 1.1195 1.2725 0.9878 0.0619 0.0523 -0.1777 85 PRO A CD 665 N N . VAL A 86 ? 1.2502 1.3268 1.0002 0.1182 0.0617 -0.2171 86 VAL A N 666 C CA . VAL A 86 ? 1.2960 1.3482 1.0122 0.1157 0.0631 -0.2257 86 VAL A CA 667 C C . VAL A 86 ? 1.2678 1.3724 1.0021 0.1165 0.0676 -0.2263 86 VAL A C 668 O O . VAL A 86 ? 1.2661 1.3663 0.9895 0.1015 0.0673 -0.2280 86 VAL A O 669 C CB . VAL A 86 ? 1.3721 1.3676 1.0342 0.1420 0.0654 -0.2381 86 VAL A CB 670 C CG1 . VAL A 86 ? 1.4035 1.3406 1.0414 0.1397 0.0618 -0.2373 86 VAL A CG1 671 C CG2 . VAL A 86 ? 1.3772 1.4045 1.0399 0.1795 0.0707 -0.2440 86 VAL A CG2 672 N N . ASN A 87 ? 1.2131 1.3690 0.9736 0.1322 0.0719 -0.2251 87 ASN A N 673 C CA . ASN A 87 ? 1.1755 1.3840 0.9520 0.1316 0.0774 -0.2258 87 ASN A CA 674 C C . ASN A 87 ? 1.1432 1.3915 0.9584 0.1056 0.0773 -0.2133 87 ASN A C 675 O O . ASN A 87 ? 1.1279 1.4206 0.9701 0.1068 0.0809 -0.2093 87 ASN A O 676 C CB . ASN A 87 ? 1.1805 1.4272 0.9588 0.1620 0.0833 -0.2333 87 ASN A CB 677 C CG . ASN A 87 ? 1.2542 1.4612 0.9869 0.1931 0.0846 -0.2462 87 ASN A CG 678 O OD1 . ASN A 87 ? 1.2947 1.4693 0.9962 0.1913 0.0851 -0.2524 87 ASN A OD1 679 N ND2 . ASN A 87 ? 1.2725 1.4801 0.9973 0.2232 0.0853 -0.2506 87 ASN A ND2 680 N N . ASP A 88 ? 1.1602 1.3912 0.9739 0.0822 0.0734 -0.2074 88 ASP A N 681 C CA . ASP A 88 ? 1.1194 1.3790 0.9596 0.0601 0.0733 -0.1954 88 ASP A CA 682 C C . ASP A 88 ? 1.1323 1.4156 0.9662 0.0552 0.0780 -0.1972 88 ASP A C 683 O O . ASP A 88 ? 1.1279 1.4394 0.9602 0.0685 0.0846 -0.2040 88 ASP A O 684 C CB . ASP A 88 ? 1.1042 1.3350 0.9454 0.0417 0.0657 -0.1878 88 ASP A CB 685 C CG . ASP A 88 ? 1.0794 1.3338 0.9455 0.0250 0.0651 -0.1741 88 ASP A CG 686 O OD1 . ASP A 88 ? 1.0414 1.3268 0.9241 0.0254 0.0707 -0.1700 88 ASP A OD1 687 O OD2 . ASP A 88 ? 1.1106 1.3520 0.9764 0.0113 0.0594 -0.1679 88 ASP A OD2 688 N N . LEU A 89 ? 1.1229 1.3985 0.9526 0.0375 0.0747 -0.1916 89 LEU A N 689 C CA . LEU A 89 ? 1.1315 1.4241 0.9512 0.0327 0.0784 -0.1932 89 LEU A CA 690 C C . LEU A 89 ? 1.1571 1.4235 0.9453 0.0414 0.0773 -0.2060 89 LEU A C 691 O O . LEU A 89 ? 1.1592 1.3961 0.9313 0.0312 0.0713 -0.2072 89 LEU A O 692 C CB . LEU A 89 ? 1.1073 1.4025 0.9320 0.0131 0.0748 -0.1816 89 LEU A CB 693 C CG . LEU A 89 ? 1.0557 1.3653 0.9028 0.0038 0.0756 -0.1680 89 LEU A CG 694 C CD1 . LEU A 89 ? 1.0518 1.3582 0.8950 -0.0093 0.0713 -0.1577 89 LEU A CD1 695 C CD2 . LEU A 89 ? 1.0270 1.3689 0.8834 0.0044 0.0851 -0.1668 89 LEU A CD2 696 N N . CYS A 90 ? 1.1716 1.4504 0.9489 0.0598 0.0836 -0.2160 90 CYS A N 697 C CA . CYS A 90 ? 1.2071 1.4563 0.9488 0.0719 0.0838 -0.2291 90 CYS A CA 698 C C . CYS A 90 ? 1.1857 1.4293 0.9121 0.0556 0.0819 -0.2293 90 CYS A C 699 O O . CYS A 90 ? 1.2194 1.4240 0.9179 0.0507 0.0776 -0.2359 90 CYS A O 700 C CB . CYS A 90 ? 1.2403 1.5132 0.9747 0.0979 0.0916 -0.2391 90 CYS A CB 701 S SG . CYS A 90 ? 1.2507 1.5937 1.0110 0.0930 0.1005 -0.2347 90 CYS A SG 702 N N . TYR A 91 ? 1.1423 1.4237 0.8842 0.0459 0.0854 -0.2223 91 TYR A N 703 C CA . TYR A 91 ? 1.1551 1.4364 0.8869 0.0295 0.0826 -0.2194 91 TYR A CA 704 C C . TYR A 91 ? 1.1281 1.4069 0.8764 0.0118 0.0756 -0.2066 91 TYR A C 705 O O . TYR A 91 ? 1.1076 1.4061 0.8797 0.0085 0.0772 -0.1959 91 TYR A O 706 C CB . TYR A 91 ? 1.1745 1.4941 0.9109 0.0284 0.0900 -0.2167 91 TYR A CB 707 C CG . TYR A 91 ? 1.2284 1.5463 0.9454 0.0186 0.0883 -0.2179 91 TYR A CG 708 C CD1 . TYR A 91 ? 1.2322 1.5506 0.9528 0.0020 0.0824 -0.2075 91 TYR A CD1 709 C CD2 . TYR A 91 ? 1.2623 1.5800 0.9557 0.0281 0.0926 -0.2298 91 TYR A CD2 710 C CE1 . TYR A 91 ? 1.2660 1.5871 0.9683 -0.0056 0.0804 -0.2087 91 TYR A CE1 711 C CE2 . TYR A 91 ? 1.2897 1.6070 0.9648 0.0187 0.0910 -0.2312 91 TYR A CE2 712 C CZ . TYR A 91 ? 1.2802 1.6002 0.9603 0.0015 0.0847 -0.2206 91 TYR A CZ 713 O OH . TYR A 91 ? 1.2978 1.6214 0.9592 -0.0065 0.0826 -0.2221 91 TYR A OH 714 N N . PRO A 92 ? 1.1515 1.4081 0.8853 -0.0001 0.0680 -0.2083 92 PRO A N 715 C CA . PRO A 92 ? 1.1257 1.3829 0.8744 -0.0137 0.0609 -0.1976 92 PRO A CA 716 C C . PRO A 92 ? 1.1193 1.4064 0.8841 -0.0198 0.0614 -0.1835 92 PRO A C 717 O O . PRO A 92 ? 1.1389 1.4430 0.8968 -0.0189 0.0659 -0.1825 92 PRO A O 718 C CB . PRO A 92 ? 1.1498 1.3882 0.8750 -0.0268 0.0540 -0.2048 92 PRO A CB 719 C CG . PRO A 92 ? 1.1809 1.4193 0.8823 -0.0233 0.0579 -0.2143 92 PRO A CG 720 C CD . PRO A 92 ? 1.1928 1.4292 0.8944 -0.0035 0.0662 -0.2198 92 PRO A CD 721 N N . GLY A 93 ? 1.1368 1.4266 0.9188 -0.0249 0.0571 -0.1726 93 GLY A N 722 C CA . GLY A 93 ? 1.1281 1.4369 0.9180 -0.0282 0.0575 -0.1585 93 GLY A CA 723 C C . GLY A 93 ? 1.1156 1.4227 0.9247 -0.0286 0.0555 -0.1474 93 GLY A C 724 O O . GLY A 93 ? 1.0979 1.3939 0.9144 -0.0308 0.0498 -0.1491 93 GLY A O 725 N N . ASP A 94 ? 1.1198 1.4351 0.9330 -0.0278 0.0607 -0.1362 94 ASP A N 726 C CA . ASP A 94 ? 1.1049 1.4153 0.9320 -0.0278 0.0602 -0.1252 94 ASP A CA 727 C C . ASP A 94 ? 1.0882 1.4012 0.9199 -0.0286 0.0702 -0.1215 94 ASP A C 728 O O . ASP A 94 ? 1.0832 1.4065 0.9054 -0.0301 0.0776 -0.1246 94 ASP A O 729 C CB . ASP A 94 ? 1.1304 1.4433 0.9486 -0.0276 0.0558 -0.1126 94 ASP A CB 730 C CG . ASP A 94 ? 1.1679 1.4883 0.9842 -0.0290 0.0455 -0.1158 94 ASP A CG 731 O OD1 . ASP A 94 ? 1.1893 1.5051 1.0185 -0.0315 0.0404 -0.1192 94 ASP A OD1 732 O OD2 . ASP A 94 ? 1.2204 1.5533 1.0211 -0.0287 0.0426 -0.1152 94 ASP A OD2 733 N N . PHE A 95 ? 1.0246 1.3307 0.8701 -0.0292 0.0705 -0.1153 95 PHE A N 734 C CA . PHE A 95 ? 0.9774 1.2857 0.8250 -0.0343 0.0795 -0.1101 95 PHE A CA 735 C C . PHE A 95 ? 0.9707 1.2623 0.8106 -0.0364 0.0782 -0.0955 95 PHE A C 736 O O . PHE A 95 ? 0.9472 1.2302 0.7983 -0.0329 0.0720 -0.0919 95 PHE A O 737 C CB . PHE A 95 ? 0.9460 1.2605 0.8144 -0.0321 0.0812 -0.1172 95 PHE A CB 738 C CG . PHE A 95 ? 0.9424 1.2727 0.8130 -0.0395 0.0917 -0.1173 95 PHE A CG 739 C CD1 . PHE A 95 ? 0.9536 1.2744 0.8173 -0.0504 0.0967 -0.1063 95 PHE A CD1 740 C CD2 . PHE A 95 ? 0.9502 1.3058 0.8270 -0.0357 0.0969 -0.1291 95 PHE A CD2 741 C CE1 . PHE A 95 ? 0.9670 1.3043 0.8303 -0.0623 0.1070 -0.1074 95 PHE A CE1 742 C CE2 . PHE A 95 ? 0.9492 1.3292 0.8292 -0.0446 0.1067 -0.1303 95 PHE A CE2 743 C CZ . PHE A 95 ? 0.9546 1.3260 0.8280 -0.0604 0.1119 -0.1197 95 PHE A CZ 744 N N . ASN A 96 ? 1.0003 1.2847 0.8169 -0.0411 0.0845 -0.0871 96 ASN A N 745 C CA . ASN A 96 ? 1.0229 1.2844 0.8213 -0.0392 0.0839 -0.0727 96 ASN A CA 746 C C . ASN A 96 ? 0.9909 1.2374 0.7943 -0.0455 0.0886 -0.0673 96 ASN A C 747 O O . ASN A 96 ? 0.9547 1.2072 0.7606 -0.0575 0.0975 -0.0711 96 ASN A O 748 C CB . ASN A 96 ? 1.0889 1.3394 0.8525 -0.0417 0.0902 -0.0654 96 ASN A CB 749 C CG . ASN A 96 ? 1.1413 1.3674 0.8788 -0.0313 0.0868 -0.0511 96 ASN A CG 750 O OD1 . ASN A 96 ? 1.1491 1.3848 0.8898 -0.0183 0.0767 -0.0499 96 ASN A OD1 751 N ND2 . ASN A 96 ? 1.1827 1.3774 0.8906 -0.0367 0.0955 -0.0406 96 ASN A ND2 752 N N . ASP A 97 ? 1.0001 1.2307 0.8041 -0.0378 0.0826 -0.0591 97 ASP A N 753 C CA . ASP A 97 ? 0.9901 1.2036 0.7980 -0.0424 0.0858 -0.0538 97 ASP A CA 754 C C . ASP A 97 ? 0.9261 1.1586 0.7645 -0.0497 0.0875 -0.0644 97 ASP A C 755 O O . ASP A 97 ? 0.9189 1.1474 0.7564 -0.0613 0.0952 -0.0638 97 ASP A O 756 C CB . ASP A 97 ? 1.0718 1.2550 0.8431 -0.0520 0.0965 -0.0437 97 ASP A CB 757 C CG . ASP A 97 ? 1.1461 1.3002 0.8826 -0.0386 0.0940 -0.0304 97 ASP A CG 758 O OD1 . ASP A 97 ? 1.1680 1.3230 0.9131 -0.0230 0.0846 -0.0265 97 ASP A OD1 759 O OD2 . ASP A 97 ? 1.2354 1.3661 0.9333 -0.0428 0.1018 -0.0238 97 ASP A OD2 760 N N . TYR A 98 ? 0.8786 1.1304 0.7402 -0.0427 0.0803 -0.0744 98 TYR A N 761 C CA . TYR A 98 ? 0.8698 1.1392 0.7559 -0.0440 0.0812 -0.0854 98 TYR A CA 762 C C . TYR A 98 ? 0.8745 1.1357 0.7746 -0.0455 0.0806 -0.0820 98 TYR A C 763 O O . TYR A 98 ? 0.8754 1.1495 0.7865 -0.0513 0.0858 -0.0870 98 TYR A O 764 C CB . TYR A 98 ? 0.8534 1.1315 0.7511 -0.0346 0.0732 -0.0953 98 TYR A CB 765 C CG . TYR A 98 ? 0.8485 1.1403 0.7625 -0.0305 0.0742 -0.1076 98 TYR A CG 766 C CD1 . TYR A 98 ? 0.8513 1.1643 0.7669 -0.0335 0.0828 -0.1135 98 TYR A CD1 767 C CD2 . TYR A 98 ? 0.8327 1.1168 0.7571 -0.0227 0.0668 -0.1136 98 TYR A CD2 768 C CE1 . TYR A 98 ? 0.8553 1.1843 0.7832 -0.0245 0.0834 -0.1248 98 TYR A CE1 769 C CE2 . TYR A 98 ? 0.8330 1.1236 0.7654 -0.0147 0.0678 -0.1244 98 TYR A CE2 770 C CZ . TYR A 98 ? 0.8657 1.1802 0.8002 -0.0134 0.0758 -0.1299 98 TYR A CZ 771 O OH . TYR A 98 ? 0.9019 1.2269 0.8420 -0.0005 0.0767 -0.1407 98 TYR A OH 772 N N . GLU A 99 ? 0.8859 1.1295 0.7852 -0.0399 0.0741 -0.0739 99 GLU A N 773 C CA . GLU A 99 ? 0.8977 1.1320 0.8100 -0.0399 0.0724 -0.0705 99 GLU A CA 774 C C . GLU A 99 ? 0.9063 1.1266 0.8038 -0.0512 0.0814 -0.0635 99 GLU A C 775 O O . GLU A 99 ? 0.9015 1.1266 0.8116 -0.0575 0.0844 -0.0662 99 GLU A O 776 C CB . GLU A 99 ? 0.9122 1.1354 0.8258 -0.0305 0.0635 -0.0639 99 GLU A CB 777 C CG . GLU A 99 ? 0.9165 1.1522 0.8450 -0.0250 0.0547 -0.0720 99 GLU A CG 778 C CD . GLU A 99 ? 0.9476 1.1934 0.8641 -0.0235 0.0527 -0.0757 99 GLU A CD 779 O OE1 . GLU A 99 ? 0.9681 1.2109 0.8653 -0.0211 0.0535 -0.0678 99 GLU A OE1 780 O OE2 . GLU A 99 ? 0.9304 1.1845 0.8533 -0.0239 0.0504 -0.0865 99 GLU A OE2 781 N N . GLU A 100 ? 0.9225 1.1234 0.7892 -0.0543 0.0861 -0.0548 100 GLU A N 782 C CA . GLU A 100 ? 0.9247 1.1033 0.7667 -0.0687 0.0963 -0.0483 100 GLU A CA 783 C C . GLU A 100 ? 0.9216 1.1257 0.7712 -0.0861 0.1053 -0.0577 100 GLU A C 784 O O . GLU A 100 ? 0.9329 1.1313 0.7759 -0.1017 0.1126 -0.0568 100 GLU A O 785 C CB . GLU A 100 ? 0.9433 1.0904 0.7427 -0.0673 0.1003 -0.0374 100 GLU A CB 786 C CG . GLU A 100 ? 0.9489 1.0676 0.7326 -0.0502 0.0940 -0.0259 100 GLU A CG 787 C CD . GLU A 100 ? 0.9750 1.0617 0.7451 -0.0551 0.0980 -0.0191 100 GLU A CD 788 O OE1 . GLU A 100 ? 1.0089 1.0731 0.7529 -0.0738 0.1091 -0.0172 100 GLU A OE1 789 O OE2 . GLU A 100 ? 0.9356 1.0192 0.7188 -0.0420 0.0906 -0.0158 100 GLU A OE2 790 N N . LEU A 101 ? 0.8969 1.1320 0.7595 -0.0835 0.1049 -0.0674 101 LEU A N 791 C CA . LEU A 101 ? 0.8974 1.1672 0.7703 -0.0958 0.1126 -0.0778 101 LEU A CA 792 C C . LEU A 101 ? 0.8461 1.1393 0.7507 -0.0916 0.1093 -0.0855 101 LEU A C 793 O O . LEU A 101 ? 0.7987 1.1082 0.7065 -0.1058 0.1160 -0.0883 101 LEU A O 794 C CB . LEU A 101 ? 0.9060 1.2017 0.7814 -0.0903 0.1130 -0.0863 101 LEU A CB 795 C CG . LEU A 101 ? 0.9074 1.2461 0.7913 -0.1006 0.1216 -0.0974 101 LEU A CG 796 C CD1 . LEU A 101 ? 0.9248 1.2620 0.7869 -0.1272 0.1340 -0.0935 101 LEU A CD1 797 C CD2 . LEU A 101 ? 0.9421 1.2996 0.8225 -0.0933 0.1221 -0.1044 101 LEU A CD2 798 N N . LYS A 102 ? 0.8316 1.1263 0.7567 -0.0731 0.0991 -0.0891 102 LYS A N 799 C CA . LYS A 102 ? 0.8190 1.1274 0.7695 -0.0660 0.0950 -0.0950 102 LYS A CA 800 C C . LYS A 102 ? 0.8110 1.1058 0.7609 -0.0768 0.0974 -0.0882 102 LYS A C 801 O O . LYS A 102 ? 0.8074 1.1255 0.7718 -0.0812 0.1000 -0.0938 102 LYS A O 802 C CB . LYS A 102 ? 0.8259 1.1211 0.7880 -0.0484 0.0840 -0.0963 102 LYS A CB 803 C CG . LYS A 102 ? 0.8532 1.1634 0.8196 -0.0361 0.0813 -0.1073 102 LYS A CG 804 C CD . LYS A 102 ? 0.8800 1.1686 0.8491 -0.0253 0.0713 -0.1074 102 LYS A CD 805 C CE . LYS A 102 ? 0.9064 1.2003 0.8800 -0.0117 0.0684 -0.1195 102 LYS A CE 806 N NZ . LYS A 102 ? 0.9313 1.2002 0.8999 -0.0070 0.0600 -0.1203 102 LYS A NZ 807 N N . HIS A 103 ? 0.8167 1.0748 0.7481 -0.0796 0.0965 -0.0764 103 HIS A N 808 C CA . HIS A 103 ? 0.8271 1.0650 0.7515 -0.0895 0.0993 -0.0697 103 HIS A CA 809 C C . HIS A 103 ? 0.8503 1.0994 0.7602 -0.1135 0.1113 -0.0718 103 HIS A C 810 O O . HIS A 103 ? 0.8466 1.1004 0.7616 -0.1243 0.1142 -0.0730 103 HIS A O 811 C CB . HIS A 103 ? 0.8414 1.0356 0.7412 -0.0847 0.0969 -0.0565 103 HIS A CB 812 C CG . HIS A 103 ? 0.8583 1.0242 0.7430 -0.0942 0.1009 -0.0493 103 HIS A CG 813 N ND1 . HIS A 103 ? 0.8403 1.0008 0.7425 -0.0864 0.0948 -0.0477 103 HIS A ND1 814 C CD2 . HIS A 103 ? 0.8863 1.0247 0.7363 -0.1125 0.1111 -0.0436 103 HIS A CD2 815 C CE1 . HIS A 103 ? 0.8425 0.9745 0.7229 -0.0980 0.1006 -0.0415 103 HIS A CE1 816 N NE2 . HIS A 103 ? 0.8797 0.9954 0.7263 -0.1146 0.1107 -0.0390 103 HIS A NE2 817 N N . LEU A 104 ? 0.8863 1.1409 0.7767 -0.1236 0.1185 -0.0728 104 LEU A N 818 C CA . LEU A 104 ? 0.9458 1.2149 0.8191 -0.1506 0.1310 -0.0759 104 LEU A CA 819 C C . LEU A 104 ? 0.9503 1.2784 0.8550 -0.1543 0.1325 -0.0894 104 LEU A C 820 O O . LEU A 104 ? 0.9704 1.3168 0.8690 -0.1778 0.1411 -0.0927 104 LEU A O 821 C CB . LEU A 104 ? 0.9910 1.2579 0.8387 -0.1581 0.1377 -0.0751 104 LEU A CB 822 C CG . LEU A 104 ? 1.0393 1.2786 0.8416 -0.1867 0.1510 -0.0692 104 LEU A CG 823 C CD1 . LEU A 104 ? 1.0790 1.2521 0.8454 -0.1883 0.1516 -0.0554 104 LEU A CD1 824 C CD2 . LEU A 104 ? 1.0604 1.3010 0.8435 -0.1873 0.1550 -0.0690 104 LEU A CD2 825 N N . LEU A 105 ? 0.9666 1.3234 0.9013 -0.1308 0.1243 -0.0973 105 LEU A N 826 C CA . LEU A 105 ? 0.9583 1.3709 0.9207 -0.1253 0.1243 -0.1101 105 LEU A CA 827 C C . LEU A 105 ? 0.9680 1.3866 0.9483 -0.1236 0.1207 -0.1109 105 LEU A C 828 O O . LEU A 105 ? 1.0149 1.4830 1.0134 -0.1229 0.1224 -0.1209 105 LEU A O 829 C CB . LEU A 105 ? 0.9325 1.3610 0.9126 -0.0971 0.1165 -0.1177 105 LEU A CB 830 C CG . LEU A 105 ? 0.9277 1.3736 0.8989 -0.0942 0.1201 -0.1229 105 LEU A CG 831 C CD1 . LEU A 105 ? 0.9198 1.3772 0.9062 -0.0652 0.1122 -0.1317 105 LEU A CD1 832 C CD2 . LEU A 105 ? 0.9419 1.4372 0.9095 -0.1138 0.1316 -0.1301 105 LEU A CD2 833 N N . SER A 106 ? 1.0469 1.6525 0.8859 -0.0553 0.1585 -0.1141 106 SER A N 834 C CA . SER A 106 ? 1.0895 1.7075 0.9213 -0.0583 0.1595 -0.1150 106 SER A CA 835 C C . SER A 106 ? 1.1076 1.7246 0.9197 -0.0746 0.1626 -0.1260 106 SER A C 836 O O . SER A 106 ? 1.1678 1.7985 0.9710 -0.0804 0.1606 -0.1286 106 SER A O 837 C CB . SER A 106 ? 1.0994 1.7011 0.9285 -0.0499 0.1649 -0.1101 106 SER A CB 838 O OG . SER A 106 ? 1.1262 1.6983 0.9447 -0.0516 0.1721 -0.1143 106 SER A OG 839 N N . ARG A 107 ? 1.1432 1.7425 0.9473 -0.0825 0.1665 -0.1320 107 ARG A N 840 C CA . ARG A 107 ? 1.1982 1.7955 0.9867 -0.0999 0.1687 -0.1419 107 ARG A CA 841 C C . ARG A 107 ? 1.1237 1.7468 0.9245 -0.1086 0.1650 -0.1433 107 ARG A C 842 O O . ARG A 107 ? 1.1129 1.7355 0.9053 -0.1243 0.1667 -0.1504 107 ARG A O 843 C CB . ARG A 107 ? 1.3107 1.8715 1.0833 -0.1048 0.1762 -0.1466 107 ARG A CB 844 C CG . ARG A 107 ? 1.4062 1.9409 1.1623 -0.1020 0.1824 -0.1498 107 ARG A CG 845 C CD . ARG A 107 ? 1.5148 2.0136 1.2566 -0.1080 0.1888 -0.1546 107 ARG A CD 846 N NE . ARG A 107 ? 1.6151 2.0889 1.3372 -0.1096 0.1960 -0.1618 107 ARG A NE 847 C CZ . ARG A 107 ? 1.6770 2.1174 1.3829 -0.1167 0.2019 -0.1681 107 ARG A CZ 848 N NH1 . ARG A 107 ? 1.6684 2.0965 1.3747 -0.1239 0.2011 -0.1670 107 ARG A NH1 849 N NH2 . ARG A 107 ? 1.6954 2.1128 1.3831 -0.1162 0.2093 -0.1756 107 ARG A NH2 850 N N . ILE A 108 ? 1.0494 1.6943 0.8712 -0.0984 0.1606 -0.1366 108 ILE A N 851 C CA . ILE A 108 ? 1.0242 1.6924 0.8607 -0.1033 0.1601 -0.1374 108 ILE A CA 852 C C . ILE A 108 ? 0.9937 1.6993 0.8524 -0.0974 0.1522 -0.1326 108 ILE A C 853 O O . ILE A 108 ? 0.9887 1.6980 0.8564 -0.0832 0.1477 -0.1256 108 ILE A O 854 C CB . ILE A 108 ? 1.0073 1.6602 0.8463 -0.0960 0.1647 -0.1350 108 ILE A CB 855 C CG1 . ILE A 108 ? 1.0175 1.6355 0.8352 -0.1041 0.1715 -0.1388 108 ILE A CG1 856 C CG2 . ILE A 108 ? 0.9904 1.6690 0.8456 -0.0978 0.1667 -0.1354 108 ILE A CG2 857 C CD1 . ILE A 108 ? 1.0135 1.6098 0.8269 -0.0963 0.1739 -0.1354 108 ILE A CD1 858 N N . ASN A 109 ? 0.9816 1.7149 0.8511 -0.1086 0.1500 -0.1354 109 ASN A N 859 C CA . ASN A 109 ? 0.9568 1.7284 0.8510 -0.1037 0.1417 -0.1304 109 ASN A CA 860 C C . ASN A 109 ? 0.9385 1.7323 0.8575 -0.1003 0.1457 -0.1292 109 ASN A C 861 O O . ASN A 109 ? 0.9067 1.7279 0.8495 -0.0905 0.1400 -0.1237 109 ASN A O 862 C CB . ASN A 109 ? 0.9753 1.7672 0.8673 -0.1185 0.1335 -0.1332 109 ASN A CB 863 C CG . ASN A 109 ? 1.0048 1.7789 0.8715 -0.1194 0.1294 -0.1341 109 ASN A CG 864 O OD1 . ASN A 109 ? 1.0020 1.7817 0.8708 -0.1075 0.1239 -0.1270 109 ASN A OD1 865 N ND2 . ASN A 109 ? 1.0420 1.7933 0.8837 -0.1335 0.1330 -0.1428 109 ASN A ND2 866 N N . HIS A 110 ? 0.9326 1.7142 0.8458 -0.1080 0.1562 -0.1339 110 HIS A N 867 C CA . HIS A 110 ? 0.9250 1.7275 0.8595 -0.1055 0.1634 -0.1335 110 HIS A CA 868 C C . HIS A 110 ? 0.9291 1.7047 0.8476 -0.1078 0.1765 -0.1367 110 HIS A C 869 O O . HIS A 110 ? 0.9357 1.6910 0.8349 -0.1220 0.1812 -0.1406 110 HIS A O 870 C CB . HIS A 110 ? 0.9334 1.7735 0.8894 -0.1200 0.1614 -0.1345 110 HIS A CB 871 C CG . HIS A 110 ? 0.9290 1.8003 0.9160 -0.1143 0.1683 -0.1323 110 HIS A CG 872 N ND1 . HIS A 110 ? 0.9340 1.8333 0.9409 -0.1288 0.1737 -0.1335 110 HIS A ND1 873 C CD2 . HIS A 110 ? 0.9125 1.7908 0.9148 -0.0953 0.1718 -0.1291 110 HIS A CD2 874 C CE1 . HIS A 110 ? 0.9245 1.8487 0.9590 -0.1179 0.1816 -0.1309 110 HIS A CE1 875 N NE2 . HIS A 110 ? 0.9193 1.8297 0.9498 -0.0972 0.1806 -0.1289 110 HIS A NE2 876 N N . PHE A 111 ? 0.9354 1.7091 0.8600 -0.0936 0.1818 -0.1351 111 PHE A N 877 C CA . PHE A 111 ? 0.9637 1.7163 0.8729 -0.0951 0.1946 -0.1377 111 PHE A CA 878 C C . PHE A 111 ? 0.9831 1.7681 0.9154 -0.0966 0.2054 -0.1384 111 PHE A C 879 O O . PHE A 111 ? 0.9691 1.7883 0.9312 -0.0889 0.2014 -0.1360 111 PHE A O 880 C CB . PHE A 111 ? 0.9521 1.6760 0.8474 -0.0781 0.1935 -0.1363 111 PHE A CB 881 C CG . PHE A 111 ? 0.9436 1.6304 0.8151 -0.0773 0.1867 -0.1350 111 PHE A CG 882 C CD1 . PHE A 111 ? 0.9568 1.6186 0.8058 -0.0905 0.1907 -0.1370 111 PHE A CD1 883 C CD2 . PHE A 111 ? 0.9138 1.5901 0.7876 -0.0629 0.1767 -0.1311 111 PHE A CD2 884 C CE1 . PHE A 111 ? 0.9359 1.5647 0.7671 -0.0880 0.1850 -0.1351 111 PHE A CE1 885 C CE2 . PHE A 111 ? 0.8977 1.5430 0.7550 -0.0616 0.1713 -0.1288 111 PHE A CE2 886 C CZ . PHE A 111 ? 0.9131 1.5352 0.7498 -0.0734 0.1756 -0.1309 111 PHE A CZ 887 N N . GLU A 112 ? 1.0227 1.7971 0.9425 -0.1059 0.2195 -0.1406 112 GLU A N 888 C CA . GLU A 112 ? 1.0625 1.8619 1.0007 -0.1041 0.2343 -0.1410 112 GLU A CA 889 C C . GLU A 112 ? 1.0542 1.8195 0.9623 -0.0983 0.2470 -0.1430 112 GLU A C 890 O O . GLU A 112 ? 1.0469 1.7839 0.9271 -0.1104 0.2524 -0.1433 112 GLU A O 891 C CB . GLU A 112 ? 1.0996 1.9277 1.0560 -0.1247 0.2415 -0.1407 112 GLU A CB 892 C CG . GLU A 112 ? 1.1283 1.9929 1.1150 -0.1218 0.2570 -0.1397 112 GLU A CG 893 C CD . GLU A 112 ? 1.1809 2.0691 1.1837 -0.1445 0.2665 -0.1384 112 GLU A CD 894 O OE1 . GLU A 112 ? 1.1942 2.0928 1.2050 -0.1605 0.2542 -0.1380 112 GLU A OE1 895 O OE2 . GLU A 112 ? 1.1767 2.0722 1.1833 -0.1467 0.2866 -0.1378 112 GLU A OE2 896 N N . LYS A 113 ? 1.0405 1.8064 0.9524 -0.0799 0.2509 -0.1442 113 LYS A N 897 C CA . LYS A 113 ? 1.0851 1.8160 0.9641 -0.0729 0.2609 -0.1469 113 LYS A CA 898 C C . LYS A 113 ? 1.1117 1.8512 0.9866 -0.0825 0.2832 -0.1479 113 LYS A C 899 O O . LYS A 113 ? 1.1124 1.8925 1.0208 -0.0831 0.2940 -0.1476 113 LYS A O 900 C CB . LYS A 113 ? 1.0946 1.8221 0.9782 -0.0505 0.2579 -0.1491 113 LYS A CB 901 C CG . LYS A 113 ? 1.1440 1.8308 0.9886 -0.0426 0.2650 -0.1530 113 LYS A CG 902 C CD . LYS A 113 ? 1.1665 1.8302 1.0040 -0.0250 0.2501 -0.1543 113 LYS A CD 903 C CE . LYS A 113 ? 1.1590 1.8510 1.0298 -0.0083 0.2510 -0.1560 113 LYS A CE 904 N NZ . LYS A 113 ? 1.1512 1.8273 1.0249 0.0048 0.2318 -0.1544 113 LYS A NZ 905 N N . ILE A 114 ? 1.1367 1.8386 0.9718 -0.0903 0.2902 -0.1479 114 ILE A N 906 C CA . ILE A 114 ? 1.1827 1.8863 1.0065 -0.0987 0.3132 -0.1479 114 ILE A CA 907 C C . ILE A 114 ? 1.2310 1.8879 1.0057 -0.0917 0.3192 -0.1499 114 ILE A C 908 O O . ILE A 114 ? 1.2528 1.8724 1.0003 -0.0869 0.3033 -0.1497 114 ILE A O 909 C CB . ILE A 114 ? 1.1944 1.9028 1.0189 -0.1234 0.3181 -0.1437 114 ILE A CB 910 C CG1 . ILE A 114 ? 1.2115 1.8750 1.0008 -0.1316 0.3047 -0.1418 114 ILE A CG1 911 C CG2 . ILE A 114 ? 1.1670 1.9228 1.0389 -0.1321 0.3123 -0.1424 114 ILE A CG2 912 C CD1 . ILE A 114 ? 1.2446 1.8949 1.0175 -0.1537 0.3150 -0.1378 114 ILE A CD1 913 N N . GLN A 115 ? 1.2432 1.9032 1.0071 -0.0917 0.3423 -0.1512 115 GLN A N 914 C CA . GLN A 115 ? 1.2749 1.8907 0.9875 -0.0857 0.3499 -0.1535 115 GLN A CA 915 C C . GLN A 115 ? 1.2974 1.8835 0.9740 -0.1047 0.3550 -0.1475 115 GLN A C 916 O O . GLN A 115 ? 1.2921 1.8992 0.9816 -0.1209 0.3707 -0.1434 115 GLN A O 917 C CB . GLN A 115 ? 1.2877 1.9193 1.0023 -0.0748 0.3749 -0.1583 115 GLN A CB 918 C CG . GLN A 115 ? 1.3261 1.9100 0.9841 -0.0651 0.3809 -0.1630 115 GLN A CG 919 C CD . GLN A 115 ? 1.3433 1.9406 0.9992 -0.0547 0.4096 -0.1686 115 GLN A CD 920 O OE1 . GLN A 115 ? 1.3578 1.9399 0.9999 -0.0356 0.4101 -0.1769 115 GLN A OE1 921 N NE2 . GLN A 115 ? 1.3434 1.9683 1.0134 -0.0673 0.4345 -0.1642 115 GLN A NE2 922 N N . ILE A 116 ? 1.3054 1.8425 0.9386 -0.1031 0.3410 -0.1463 116 ILE A N 923 C CA . ILE A 116 ? 1.3350 1.8381 0.9311 -0.1196 0.3432 -0.1394 116 ILE A CA 924 C C . ILE A 116 ? 1.3951 1.8582 0.9355 -0.1163 0.3541 -0.1394 116 ILE A C 925 O O . ILE A 116 ? 1.4515 1.8996 0.9656 -0.1307 0.3681 -0.1333 116 ILE A O 926 C CB . ILE A 116 ? 1.3031 1.7801 0.8934 -0.1238 0.3180 -0.1353 116 ILE A CB 927 C CG1 . ILE A 116 ? 1.2767 1.7345 0.8609 -0.1056 0.2966 -0.1388 116 ILE A CG1 928 C CG2 . ILE A 116 ? 1.2657 1.7762 0.8995 -0.1343 0.3129 -0.1341 116 ILE A CG2 929 C CD1 . ILE A 116 ? 1.2669 1.6912 0.8369 -0.1082 0.2748 -0.1335 116 ILE A CD1 930 N N . ILE A 117 ? 1.4141 1.8582 0.9346 -0.0983 0.3473 -0.1459 117 ILE A N 931 C CA . ILE A 117 ? 1.4718 1.8770 0.9354 -0.0939 0.3574 -0.1478 117 ILE A CA 932 C C . ILE A 117 ? 1.4749 1.8932 0.9427 -0.0753 0.3698 -0.1586 117 ILE A C 933 O O . ILE A 117 ? 1.4641 1.8698 0.9314 -0.0600 0.3522 -0.1648 117 ILE A O 934 C CB . ILE A 117 ? 1.5033 1.8551 0.9229 -0.0915 0.3318 -0.1450 117 ILE A CB 935 C CG1 . ILE A 117 ? 1.4972 1.8354 0.9158 -0.1080 0.3201 -0.1341 117 ILE A CG1 936 C CG2 . ILE A 117 ? 1.5763 1.8860 0.9319 -0.0881 0.3408 -0.1471 117 ILE A CG2 937 C CD1 . ILE A 117 ? 1.5173 1.8054 0.8975 -0.1063 0.2950 -0.1290 117 ILE A CD1 938 N N . PRO A 118 ? 1.4954 1.9385 0.9687 -0.0764 0.4009 -0.1606 118 PRO A N 939 C CA . PRO A 118 ? 1.5014 1.9607 0.9852 -0.0573 0.4155 -0.1712 118 PRO A CA 940 C C . PRO A 118 ? 1.5527 1.9614 0.9799 -0.0429 0.4087 -0.1797 118 PRO A C 941 O O . PRO A 118 ? 1.5952 1.9588 0.9636 -0.0498 0.4072 -0.1768 118 PRO A O 942 C CB . PRO A 118 ? 1.5236 2.0113 1.0146 -0.0641 0.4526 -0.1695 118 PRO A CB 943 C CG . PRO A 118 ? 1.5101 2.0090 1.0119 -0.0881 0.4543 -0.1575 118 PRO A CG 944 C CD . PRO A 118 ? 1.5149 1.9706 0.9854 -0.0952 0.4247 -0.1526 118 PRO A CD 945 N N . LYS A 119 ? 1.5585 1.9739 1.0033 -0.0234 0.4035 -0.1896 119 LYS A N 946 C CA . LYS A 119 ? 1.6108 1.9782 1.0066 -0.0091 0.3934 -0.1993 119 LYS A CA 947 C C . LYS A 119 ? 1.6729 2.0121 1.0103 -0.0070 0.4209 -0.2052 119 LYS A C 948 O O . LYS A 119 ? 1.7385 2.0241 1.0130 -0.0048 0.4109 -0.2092 119 LYS A O 949 C CB . LYS A 119 ? 1.6002 1.9853 1.0339 0.0110 0.3860 -0.2086 119 LYS A CB 950 C CG . LYS A 119 ? 1.6427 1.9779 1.0362 0.0237 0.3647 -0.2176 119 LYS A CG 951 C CD . LYS A 119 ? 1.6232 1.9783 1.0635 0.0404 0.3520 -0.2232 119 LYS A CD 952 C CE . LYS A 119 ? 1.6742 1.9790 1.0752 0.0532 0.3335 -0.2334 119 LYS A CE 953 N NZ . LYS A 119 ? 1.6485 1.9705 1.0955 0.0691 0.3214 -0.2378 119 LYS A NZ 954 N N . SER A 120 ? 1.6693 2.0449 1.0275 -0.0081 0.4555 -0.2051 120 SER A N 955 C CA . SER A 120 ? 1.7062 2.0613 1.0129 -0.0065 0.4879 -0.2096 120 SER A CA 956 C C . SER A 120 ? 1.7469 2.0649 0.9949 -0.0259 0.4891 -0.1996 120 SER A C 957 O O . SER A 120 ? 1.8250 2.1059 1.0089 -0.0243 0.5061 -0.2035 120 SER A O 958 C CB . SER A 120 ? 1.6816 2.0929 1.0368 -0.0045 0.5251 -0.2092 120 SER A CB 959 O OG . SER A 120 ? 1.6376 2.0883 1.0363 -0.0245 0.5268 -0.1955 120 SER A OG 960 N N . SER A 121 ? 1.7270 2.0528 0.9948 -0.0436 0.4712 -0.1867 121 SER A N 961 C CA . SER A 121 ? 1.7624 2.0572 0.9831 -0.0630 0.4725 -0.1748 121 SER A CA 962 C C . SER A 121 ? 1.8019 2.0292 0.9463 -0.0620 0.4507 -0.1755 121 SER A C 963 O O . SER A 121 ? 1.8308 2.0271 0.9278 -0.0764 0.4533 -0.1656 121 SER A O 964 C CB . SER A 121 ? 1.7245 2.0416 0.9882 -0.0803 0.4557 -0.1621 121 SER A CB 965 O OG . SER A 121 ? 1.7013 2.0796 1.0354 -0.0830 0.4705 -0.1611 121 SER A OG 966 N N . TRP A 122 ? 1.7935 1.9975 0.9269 -0.0461 0.4279 -0.1861 122 TRP A N 967 C CA . TRP A 122 ? 1.8396 1.9808 0.9049 -0.0456 0.4025 -0.1868 122 TRP A CA 968 C C . TRP A 122 ? 1.9226 2.0259 0.9166 -0.0376 0.4235 -0.1971 122 TRP A C 969 O O . TRP A 122 ? 1.9661 2.0513 0.9441 -0.0210 0.4182 -0.2116 122 TRP A O 970 C CB . TRP A 122 ? 1.8021 1.9349 0.8904 -0.0345 0.3659 -0.1923 122 TRP A CB 971 C CG . TRP A 122 ? 1.7399 1.9036 0.8894 -0.0421 0.3452 -0.1822 122 TRP A CG 972 C CD1 . TRP A 122 ? 1.6796 1.8897 0.8992 -0.0354 0.3418 -0.1847 122 TRP A CD1 973 C CD2 . TRP A 122 ? 1.7310 1.8798 0.8751 -0.0575 0.3259 -0.1678 122 TRP A CD2 974 N NE1 . TRP A 122 ? 1.6384 1.8625 0.8935 -0.0458 0.3223 -0.1737 122 TRP A NE1 975 C CE2 . TRP A 122 ? 1.6689 1.8562 0.8806 -0.0589 0.3127 -0.1636 122 TRP A CE2 976 C CE3 . TRP A 122 ? 1.7723 1.8776 0.8602 -0.0696 0.3182 -0.1578 122 TRP A CE3 977 C CZ2 . TRP A 122 ? 1.6435 1.8265 0.8684 -0.0711 0.2941 -0.1511 122 TRP A CZ2 978 C CZ3 . TRP A 122 ? 1.7492 1.8512 0.8536 -0.0815 0.2983 -0.1442 122 TRP A CZ3 979 C CH2 . TRP A 122 ? 1.6951 1.8356 0.8678 -0.0818 0.2873 -0.1417 122 TRP A CH2 980 N N . SER A 123 ? 1.9642 2.0536 0.9137 -0.0499 0.4475 -0.1893 123 SER A N 981 C CA . SER A 123 ? 2.0432 2.0994 0.9220 -0.0439 0.4747 -0.1980 123 SER A CA 982 C C . SER A 123 ? 2.1174 2.1015 0.9086 -0.0446 0.4494 -0.1996 123 SER A C 983 O O . SER A 123 ? 2.1874 2.1362 0.9173 -0.0345 0.4625 -0.2121 123 SER A O 984 C CB . SER A 123 ? 2.0642 2.1394 0.9346 -0.0576 0.5145 -0.1876 123 SER A CB 985 O OG . SER A 123 ? 2.0347 2.1119 0.9155 -0.0784 0.5016 -0.1690 123 SER A OG 986 N N . SER A 124 ? 2.1062 2.0679 0.8910 -0.0562 0.4134 -0.1869 124 SER A N 987 C CA . SER A 124 ? 2.1555 2.0510 0.8632 -0.0584 0.3837 -0.1858 124 SER A CA 988 C C . SER A 124 ? 2.1356 2.0140 0.8559 -0.0467 0.3438 -0.1953 124 SER A C 989 O O . SER A 124 ? 2.1788 2.0032 0.8388 -0.0470 0.3162 -0.1966 124 SER A O 990 C CB . SER A 124 ? 2.1542 2.0323 0.8468 -0.0776 0.3662 -0.1647 124 SER A CB 991 O OG . SER A 124 ? 2.1558 2.0542 0.8479 -0.0904 0.4015 -0.1540 124 SER A OG 992 N N . HIS A 125 ? 2.0639 1.9880 0.8625 -0.0374 0.3398 -0.2009 125 HIS A N 993 C CA . HIS A 125 ? 2.0355 1.9500 0.8571 -0.0272 0.3034 -0.2080 125 HIS A CA 994 C C . HIS A 125 ? 2.0101 1.9561 0.8755 -0.0094 0.3187 -0.2244 125 HIS A C 995 O O . HIS A 125 ? 1.9828 1.9738 0.8868 -0.0062 0.3526 -0.2263 125 HIS A O 996 C CB . HIS A 125 ? 1.9592 1.8973 0.8407 -0.0355 0.2744 -0.1936 125 HIS A CB 997 C CG . HIS A 125 ? 1.9703 1.8815 0.8197 -0.0519 0.2589 -0.1762 125 HIS A CG 998 N ND1 . HIS A 125 ? 1.9666 1.8954 0.8199 -0.0653 0.2814 -0.1638 125 HIS A ND1 999 C CD2 . HIS A 125 ? 1.9863 1.8548 0.8027 -0.0569 0.2219 -0.1683 125 HIS A CD2 1000 C CE1 . HIS A 125 ? 1.9895 1.8852 0.8112 -0.0772 0.2597 -0.1492 125 HIS A CE1 1001 N NE2 . HIS A 125 ? 1.9983 1.8583 0.7983 -0.0719 0.2233 -0.1513 125 HIS A NE2 1002 N N . GLU A 126 ? 2.0092 1.9318 0.8715 0.0020 0.2924 -0.2351 126 GLU A N 1003 C CA . GLU A 126 ? 1.9816 1.9277 0.8841 0.0199 0.3025 -0.2502 126 GLU A CA 1004 C C . GLU A 126 ? 1.8947 1.8914 0.8874 0.0215 0.2875 -0.2434 126 GLU A C 1005 O O . GLU A 126 ? 1.8825 1.8686 0.8929 0.0193 0.2512 -0.2383 126 GLU A O 1006 C CB . GLU A 126 ? 2.0376 1.9294 0.8890 0.0309 0.2824 -0.2659 126 GLU A CB 1007 C CG . GLU A 126 ? 2.0269 1.9342 0.9135 0.0505 0.2915 -0.2822 126 GLU A CG 1008 C CD . GLU A 126 ? 2.0351 1.9762 0.9353 0.0607 0.3397 -0.2901 126 GLU A CD 1009 O OE1 . GLU A 126 ? 2.0648 1.9745 0.8991 0.0641 0.3648 -0.2997 126 GLU A OE1 1010 O OE2 . GLU A 126 ? 1.9673 1.9666 0.9444 0.0654 0.3522 -0.2861 126 GLU A OE2 1011 N N . ALA A 127 ? 1.8393 1.8913 0.8888 0.0254 0.3155 -0.2430 127 ALA A N 1012 C CA . ALA A 127 ? 1.7392 1.8420 0.8707 0.0247 0.3049 -0.2349 127 ALA A CA 1013 C C . ALA A 127 ? 1.7192 1.8444 0.8973 0.0427 0.3043 -0.2456 127 ALA A C 1014 O O . ALA A 127 ? 1.6836 1.8471 0.9261 0.0434 0.2927 -0.2393 127 ALA A O 1015 C CB . ALA A 127 ? 1.6897 1.8410 0.8578 0.0140 0.3312 -0.2248 127 ALA A CB 1016 N N . SER A 128 ? 1.7736 1.8729 0.9176 0.0575 0.3166 -0.2615 128 SER A N 1017 C CA . SER A 128 ? 1.7421 1.8616 0.9288 0.0763 0.3211 -0.2721 128 SER A CA 1018 C C . SER A 128 ? 1.7422 1.8148 0.9044 0.0861 0.2922 -0.2826 128 SER A C 1019 O O . SER A 128 ? 1.7230 1.8006 0.9090 0.1029 0.2961 -0.2932 128 SER A O 1020 C CB . SER A 128 ? 1.7923 1.9272 0.9726 0.0884 0.3637 -0.2830 128 SER A CB 1021 O OG . SER A 128 ? 1.7800 1.9674 0.9995 0.0794 0.3886 -0.2722 128 SER A OG 1022 N N . LEU A 129 ? 1.7481 1.7751 0.8650 0.0755 0.2624 -0.2790 129 LEU A N 1023 C CA . LEU A 129 ? 1.7600 1.7429 0.8575 0.0812 0.2298 -0.2868 129 LEU A CA 1024 C C . LEU A 129 ? 1.7134 1.7033 0.8486 0.0708 0.1917 -0.2721 129 LEU A C 1025 O O . LEU A 129 ? 1.7302 1.6833 0.8502 0.0710 0.1600 -0.2746 129 LEU A O 1026 C CB . LEU A 129 ? 1.8518 1.7683 0.8577 0.0790 0.2248 -0.2972 129 LEU A CB 1027 C CG . LEU A 129 ? 1.9083 1.8087 0.8649 0.0900 0.2635 -0.3134 129 LEU A CG 1028 C CD1 . LEU A 129 ? 1.9939 1.8228 0.8542 0.0864 0.2527 -0.3232 129 LEU A CD1 1029 C CD2 . LEU A 129 ? 1.8975 1.8123 0.8888 0.1113 0.2793 -0.3280 129 LEU A CD2 1030 N N . GLY A 130 ? 1.6533 1.6903 0.8389 0.0618 0.1954 -0.2569 130 GLY A N 1031 C CA . GLY A 130 ? 1.6041 1.6528 0.8297 0.0529 0.1645 -0.2425 130 GLY A CA 1032 C C . GLY A 130 ? 1.5606 1.6406 0.8524 0.0624 0.1548 -0.2415 130 GLY A C 1033 O O . GLY A 130 ? 1.4902 1.6183 0.8384 0.0597 0.1600 -0.2313 130 GLY A O 1034 N N . VAL A 131 ? 1.5832 1.6331 0.8654 0.0726 0.1395 -0.2517 131 VAL A N 1035 C CA . VAL A 131 ? 1.5322 1.6050 0.8718 0.0828 0.1304 -0.2513 131 VAL A CA 1036 C C . VAL A 131 ? 1.5343 1.5690 0.8686 0.0821 0.0937 -0.2512 131 VAL A C 1037 O O . VAL A 131 ? 1.6096 1.5965 0.8910 0.0759 0.0760 -0.2549 131 VAL A O 1038 C CB . VAL A 131 ? 1.5536 1.6365 0.9005 0.1005 0.1567 -0.2655 131 VAL A CB 1039 C CG1 . VAL A 131 ? 1.5338 1.6613 0.8967 0.1008 0.1926 -0.2638 131 VAL A CG1 1040 C CG2 . VAL A 131 ? 1.6271 1.6524 0.9086 0.1087 0.1578 -0.2837 131 VAL A CG2 1041 N N . SER A 132 ? 1.4862 1.5425 0.8758 0.0879 0.0819 -0.2463 132 SER A N 1042 C CA . SER A 132 ? 1.4808 1.5075 0.8773 0.0865 0.0474 -0.2441 132 SER A CA 1043 C C . SER A 132 ? 1.4608 1.5032 0.9048 0.0992 0.0461 -0.2459 132 SER A C 1044 O O . SER A 132 ? 1.4207 1.5098 0.9099 0.1058 0.0652 -0.2415 132 SER A O 1045 C CB . SER A 132 ? 1.4236 1.4629 0.8465 0.0722 0.0240 -0.2257 132 SER A CB 1046 O OG . SER A 132 ? 1.4019 1.4273 0.8509 0.0713 -0.0061 -0.2203 132 SER A OG 1047 N N . SER A 133 ? 1.4903 1.4925 0.9241 0.1019 0.0219 -0.2515 133 SER A N 1048 C CA . SER A 133 ? 1.4784 1.4877 0.9544 0.1133 0.0172 -0.2523 133 SER A CA 1049 C C . SER A 133 ? 1.4136 1.4635 0.9558 0.1077 0.0038 -0.2322 133 SER A C 1050 O O . SER A 133 ? 1.3803 1.4477 0.9648 0.1167 0.0042 -0.2291 133 SER A O 1051 C CB . SER A 133 ? 1.5402 1.4898 0.9829 0.1157 -0.0064 -0.2643 133 SER A CB 1052 O OG . SER A 133 ? 1.5633 1.4866 0.9909 0.1001 -0.0385 -0.2564 133 SER A OG 1053 N N . ALA A 134 ? 1.3963 1.4597 0.9465 0.0934 -0.0074 -0.2184 134 ALA A N 1054 C CA . ALA A 134 ? 1.3474 1.4519 0.9572 0.0881 -0.0151 -0.1994 134 ALA A CA 1055 C C . ALA A 134 ? 1.3093 1.4686 0.9548 0.0933 0.0119 -0.1944 134 ALA A C 1056 O O . ALA A 134 ? 1.2444 1.4369 0.9395 0.0936 0.0089 -0.1817 134 ALA A O 1057 C CB . ALA A 134 ? 1.3349 1.4367 0.9419 0.0730 -0.0326 -0.1870 134 ALA A CB 1058 N N . CYS A 135 ? 1.3482 1.5165 0.9681 0.0966 0.0376 -0.2039 135 CYS A N 1059 C CA . CYS A 135 ? 1.3295 1.5486 0.9811 0.1010 0.0630 -0.2008 135 CYS A CA 1060 C C . CYS A 135 ? 1.3184 1.5389 0.9653 0.1171 0.0842 -0.2146 135 CYS A C 1061 O O . CYS A 135 ? 1.3010 1.5280 0.9246 0.1190 0.1078 -0.2230 135 CYS A O 1062 C CB . CYS A 135 ? 1.3650 1.6010 0.9995 0.0900 0.0775 -0.1979 135 CYS A CB 1063 S SG . CYS A 135 ? 1.4294 1.6640 1.0690 0.0730 0.0564 -0.1823 135 CYS A SG 1064 N N . PRO A 136 ? 1.2898 1.5047 0.9613 0.1289 0.0766 -0.2162 136 PRO A N 1065 C CA . PRO A 136 ? 1.3140 1.5254 0.9819 0.1463 0.0953 -0.2297 136 PRO A CA 1066 C C . PRO A 136 ? 1.2730 1.5403 0.9810 0.1532 0.1198 -0.2254 136 PRO A C 1067 O O . PRO A 136 ? 1.2075 1.5150 0.9558 0.1468 0.1161 -0.2107 136 PRO A O 1068 C CB . PRO A 136 ? 1.3247 1.5130 1.0123 0.1549 0.0754 -0.2292 136 PRO A CB 1069 C CG . PRO A 136 ? 1.2635 1.4754 0.9915 0.1440 0.0559 -0.2097 136 PRO A CG 1070 C CD . PRO A 136 ? 1.2550 1.4661 0.9600 0.1271 0.0511 -0.2047 136 PRO A CD 1071 N N . TYR A 137 ? 1.3114 1.5804 1.0077 0.1662 0.1444 -0.2383 137 TYR A N 1072 C CA . TYR A 137 ? 1.2889 1.6099 1.0282 0.1754 0.1663 -0.2350 137 TYR A CA 1073 C C . TYR A 137 ? 1.3192 1.6277 1.0570 0.1971 0.1831 -0.2492 137 TYR A C 1074 O O . TYR A 137 ? 1.3841 1.6653 1.0785 0.2021 0.2001 -0.2644 137 TYR A O 1075 C CB . TYR A 137 ? 1.2860 1.6395 1.0190 0.1646 0.1871 -0.2330 137 TYR A CB 1076 C CG . TYR A 137 ? 1.2632 1.6722 1.0419 0.1723 0.2088 -0.2294 137 TYR A CG 1077 C CD1 . TYR A 137 ? 1.2154 1.6686 1.0465 0.1696 0.1999 -0.2145 137 TYR A CD1 1078 C CD2 . TYR A 137 ? 1.2764 1.6939 1.0461 0.1821 0.2381 -0.2403 137 TYR A CD2 1079 C CE1 . TYR A 137 ? 1.1873 1.6917 1.0610 0.1759 0.2166 -0.2104 137 TYR A CE1 1080 C CE2 . TYR A 137 ? 1.2525 1.7236 1.0693 0.1889 0.2566 -0.2358 137 TYR A CE2 1081 C CZ . TYR A 137 ? 1.2077 1.7220 1.0767 0.1853 0.2442 -0.2208 137 TYR A CZ 1082 O OH . TYR A 137 ? 1.1863 1.7541 1.1026 0.1911 0.2595 -0.2157 137 TYR A OH 1083 N N . GLN A 138 ? 1.2869 1.6142 1.0712 0.2104 0.1790 -0.2439 138 GLN A N 1084 C CA . GLN A 138 ? 1.3236 1.6390 1.1141 0.2333 0.1931 -0.2560 138 GLN A CA 1085 C C . GLN A 138 ? 1.3921 1.6387 1.1261 0.2394 0.1885 -0.2744 138 GLN A C 1086 O O . GLN A 138 ? 1.4217 1.6500 1.1281 0.2526 0.2113 -0.2909 138 GLN A O 1087 C CB . GLN A 138 ? 1.3330 1.6896 1.1392 0.2420 0.2266 -0.2603 138 GLN A CB 1088 C CG . GLN A 138 ? 1.2757 1.6997 1.1393 0.2365 0.2294 -0.2430 138 GLN A CG 1089 C CD . GLN A 138 ? 1.2707 1.7380 1.1584 0.2459 0.2609 -0.2462 138 GLN A CD 1090 O OE1 . GLN A 138 ? 1.3003 1.7490 1.1627 0.2577 0.2841 -0.2613 138 GLN A OE1 1091 N NE2 . GLN A 138 ? 1.2304 1.7562 1.1676 0.2402 0.2620 -0.2317 138 GLN A NE2 1092 N N . GLY A 139 ? 1.3998 1.6085 1.1164 0.2291 0.1588 -0.2713 139 GLY A N 1093 C CA . GLY A 139 ? 1.4565 1.5974 1.1227 0.2330 0.1471 -0.2873 139 GLY A CA 1094 C C . GLY A 139 ? 1.4912 1.5958 1.0906 0.2207 0.1484 -0.2979 139 GLY A C 1095 O O . GLY A 139 ? 1.5266 1.5727 1.0803 0.2193 0.1322 -0.3093 139 GLY A O 1096 N N . LYS A 140 ? 1.4742 1.6115 1.0669 0.2112 0.1663 -0.2936 140 LYS A N 1097 C CA . LYS A 140 ? 1.5361 1.6418 1.0643 0.2004 0.1713 -0.3025 140 LYS A CA 1098 C C . LYS A 140 ? 1.4831 1.6023 1.0115 0.1779 0.1535 -0.2869 140 LYS A C 1099 O O . LYS A 140 ? 1.4234 1.5871 1.0030 0.1716 0.1471 -0.2704 140 LYS A O 1100 C CB . LYS A 140 ? 1.5775 1.7043 1.0910 0.2078 0.2102 -0.3112 140 LYS A CB 1101 C CG . LYS A 140 ? 1.6326 1.7564 1.1555 0.2325 0.2337 -0.3254 140 LYS A CG 1102 C CD . LYS A 140 ? 1.6982 1.8268 1.1894 0.2394 0.2723 -0.3374 140 LYS A CD 1103 C CE . LYS A 140 ? 1.6630 1.8518 1.1829 0.2274 0.2906 -0.3237 140 LYS A CE 1104 N NZ . LYS A 140 ? 1.6059 1.8566 1.2049 0.2288 0.2867 -0.3073 140 LYS A NZ 1105 N N . SER A 141 ? 1.5210 1.6001 0.9904 0.1665 0.1458 -0.2924 141 SER A N 1106 C CA . SER A 141 ? 1.4850 1.5712 0.9491 0.1462 0.1296 -0.2786 141 SER A CA 1107 C C . SER A 141 ? 1.4503 1.5845 0.9284 0.1395 0.1547 -0.2708 141 SER A C 1108 O O . SER A 141 ? 1.4983 1.6343 0.9500 0.1444 0.1829 -0.2802 141 SER A O 1109 C CB . SER A 141 ? 1.5362 1.5629 0.9304 0.1371 0.1135 -0.2867 141 SER A CB 1110 O OG . SER A 141 ? 1.5581 1.5404 0.9421 0.1400 0.0857 -0.2925 141 SER A OG 1111 N N . SER A 142 ? 1.3957 1.5676 0.9152 0.1281 0.1450 -0.2538 142 SER A N 1112 C CA . SER A 142 ? 1.3676 1.5857 0.9056 0.1200 0.1655 -0.2455 142 SER A CA 1113 C C . SER A 142 ? 1.3388 1.5578 0.8737 0.1014 0.1478 -0.2320 142 SER A C 1114 O O . SER A 142 ? 1.3511 1.5308 0.8584 0.0952 0.1236 -0.2311 142 SER A O 1115 C CB . SER A 142 ? 1.3256 1.5987 0.9286 0.1280 0.1760 -0.2386 142 SER A CB 1116 O OG . SER A 142 ? 1.3170 1.6318 0.9338 0.1234 0.2010 -0.2355 142 SER A OG 1117 N N . PHE A 143 ? 1.2963 1.5587 0.8599 0.0928 0.1591 -0.2218 143 PHE A N 1118 C CA . PHE A 143 ? 1.2741 1.5389 0.8378 0.0765 0.1450 -0.2092 143 PHE A CA 1119 C C . PHE A 143 ? 1.2223 1.5399 0.8309 0.0699 0.1560 -0.1987 143 PHE A C 1120 O O . PHE A 143 ? 1.2309 1.5833 0.8636 0.0756 0.1767 -0.2013 143 PHE A O 1121 C CB . PHE A 143 ? 1.3181 1.5493 0.8232 0.0668 0.1493 -0.2125 143 PHE A CB 1122 C CG . PHE A 143 ? 1.3082 1.5236 0.8044 0.0530 0.1270 -0.2011 143 PHE A CG 1123 C CD1 . PHE A 143 ? 1.3030 1.4916 0.8008 0.0527 0.0969 -0.1973 143 PHE A CD1 1124 C CD2 . PHE A 143 ? 1.2944 1.5212 0.7823 0.0403 0.1362 -0.1936 143 PHE A CD2 1125 C CE1 . PHE A 143 ? 1.2953 1.4716 0.7894 0.0412 0.0768 -0.1860 143 PHE A CE1 1126 C CE2 . PHE A 143 ? 1.2891 1.5005 0.7707 0.0293 0.1162 -0.1829 143 PHE A CE2 1127 C CZ . PHE A 143 ? 1.2869 1.4742 0.7728 0.0303 0.0867 -0.1789 143 PHE A CZ 1128 N N . PHE A 144 ? 1.1873 1.5099 0.8074 0.0581 0.1413 -0.1870 144 PHE A N 1129 C CA . PHE A 144 ? 1.1320 1.4967 0.7843 0.0494 0.1505 -0.1781 144 PHE A CA 1130 C C . PHE A 144 ? 1.1402 1.5240 0.7816 0.0460 0.1784 -0.1831 144 PHE A C 1131 O O . PHE A 144 ? 1.2023 1.5622 0.8018 0.0394 0.1863 -0.1862 144 PHE A O 1132 C CB . PHE A 144 ? 1.1291 1.4824 0.7750 0.0362 0.1359 -0.1679 144 PHE A CB 1133 C CG . PHE A 144 ? 1.1281 1.4663 0.7896 0.0380 0.1095 -0.1608 144 PHE A CG 1134 C CD1 . PHE A 144 ? 1.0956 1.4624 0.8031 0.0420 0.1032 -0.1539 144 PHE A CD1 1135 C CD2 . PHE A 144 ? 1.1609 1.4571 0.7916 0.0348 0.0905 -0.1598 144 PHE A CD2 1136 C CE1 . PHE A 144 ? 1.0843 1.4389 0.8084 0.0429 0.0809 -0.1460 144 PHE A CE1 1137 C CE2 . PHE A 144 ? 1.1443 1.4295 0.7945 0.0355 0.0663 -0.1521 144 PHE A CE2 1138 C CZ . PHE A 144 ? 1.1062 1.4212 0.8040 0.0395 0.0626 -0.1450 144 PHE A CZ 1139 N N . ARG A 145 ? 1.0997 1.5272 0.7798 0.0500 0.1926 -0.1828 145 ARG A N 1140 C CA . ARG A 145 ? 1.0923 1.5433 0.7715 0.0490 0.2200 -0.1876 145 ARG A CA 1141 C C . ARG A 145 ? 1.1085 1.5693 0.7768 0.0316 0.2309 -0.1825 145 ARG A C 1142 O O . ARG A 145 ? 1.1501 1.6223 0.8090 0.0286 0.2539 -0.1861 145 ARG A O 1143 C CB . ARG A 145 ? 1.0423 1.5410 0.7731 0.0576 0.2284 -0.1867 145 ARG A CB 1144 C CG . ARG A 145 ? 1.0441 1.5356 0.7879 0.0764 0.2227 -0.1922 145 ARG A CG 1145 C CD . ARG A 145 ? 1.0323 1.5692 0.8191 0.0861 0.2389 -0.1930 145 ARG A CD 1146 N NE . ARG A 145 ? 1.0375 1.5707 0.8438 0.1048 0.2325 -0.1964 145 ARG A NE 1147 C CZ . ARG A 145 ? 1.0842 1.5895 0.8685 0.1193 0.2409 -0.2081 145 ARG A CZ 1148 N NH1 . ARG A 145 ? 1.1296 1.6069 0.8675 0.1174 0.2562 -0.2176 145 ARG A NH1 1149 N NH2 . ARG A 145 ? 1.0966 1.5991 0.9029 0.1360 0.2339 -0.2102 145 ARG A NH2 1150 N N . ASN A 146 ? 1.1193 1.5760 0.7906 0.0202 0.2157 -0.1738 146 ASN A N 1151 C CA . ASN A 146 ? 1.1242 1.5914 0.7909 0.0035 0.2248 -0.1685 146 ASN A CA 1152 C C . ASN A 146 ? 1.1544 1.5788 0.7716 -0.0055 0.2220 -0.1671 146 ASN A C 1153 O O . ASN A 146 ? 1.1549 1.5813 0.7614 -0.0192 0.2317 -0.1631 146 ASN A O 1154 C CB . ASN A 146 ? 1.0792 1.5711 0.7815 -0.0035 0.2131 -0.1602 146 ASN A CB 1155 C CG . ASN A 146 ? 1.0646 1.6017 0.8134 0.0027 0.2168 -0.1601 146 ASN A CG 1156 O OD1 . ASN A 146 ? 1.1007 1.6621 0.8618 0.0064 0.2341 -0.1645 146 ASN A OD1 1157 N ND2 . ASN A 146 ? 1.0500 1.5993 0.8256 0.0041 0.2011 -0.1543 146 ASN A ND2 1158 N N . VAL A 147 ? 1.1870 1.5714 0.7737 0.0016 0.2076 -0.1700 147 VAL A N 1159 C CA . VAL A 147 ? 1.2346 1.5754 0.7713 -0.0058 0.2015 -0.1681 147 VAL A CA 1160 C C . VAL A 147 ? 1.2796 1.5872 0.7719 0.0028 0.2066 -0.1779 147 VAL A C 1161 O O . VAL A 147 ? 1.2822 1.5917 0.7843 0.0163 0.2057 -0.1858 147 VAL A O 1162 C CB . VAL A 147 ? 1.2355 1.5547 0.7748 -0.0084 0.1736 -0.1598 147 VAL A CB 1163 C CG1 . VAL A 147 ? 1.2026 1.5483 0.7754 -0.0180 0.1727 -0.1510 147 VAL A CG1 1164 C CG2 . VAL A 147 ? 1.2180 1.5325 0.7765 0.0041 0.1548 -0.1620 147 VAL A CG2 1165 N N . VAL A 148 ? 1.3391 1.6144 0.7806 -0.0050 0.2120 -0.1775 148 VAL A N 1166 C CA . VAL A 148 ? 1.4024 1.6438 0.7926 0.0017 0.2207 -0.1875 148 VAL A CA 1167 C C . VAL A 148 ? 1.4448 1.6331 0.7890 -0.0001 0.1942 -0.1859 148 VAL A C 1168 O O . VAL A 148 ? 1.4818 1.6506 0.8028 -0.0119 0.1859 -0.1766 148 VAL A O 1169 C CB . VAL A 148 ? 1.4501 1.6949 0.8113 -0.0064 0.2510 -0.1881 148 VAL A CB 1170 C CG1 . VAL A 148 ? 1.5294 1.7419 0.8373 0.0023 0.2648 -0.1999 148 VAL A CG1 1171 C CG2 . VAL A 148 ? 1.4087 1.7095 0.8214 -0.0080 0.2743 -0.1871 148 VAL A CG2 1172 N N . TRP A 149 ? 1.4556 1.6199 0.7882 0.0113 0.1797 -0.1943 149 TRP A N 1173 C CA . TRP A 149 ? 1.5028 1.6153 0.7906 0.0096 0.1524 -0.1940 149 TRP A CA 1174 C C . TRP A 149 ? 1.5867 1.6593 0.8016 0.0081 0.1658 -0.2016 149 TRP A C 1175 O O . TRP A 149 ? 1.6297 1.6875 0.8197 0.0188 0.1768 -0.2155 149 TRP A O 1176 C CB . TRP A 149 ? 1.4901 1.5917 0.7952 0.0210 0.1307 -0.2002 149 TRP A CB 1177 C CG . TRP A 149 ? 1.5277 1.5798 0.7968 0.0182 0.0976 -0.1988 149 TRP A CG 1178 C CD1 . TRP A 149 ? 1.5683 1.5845 0.7899 0.0077 0.0846 -0.1925 149 TRP A CD1 1179 C CD2 . TRP A 149 ? 1.5233 1.5560 0.8019 0.0253 0.0719 -0.2031 149 TRP A CD2 1180 N NE1 . TRP A 149 ? 1.5933 1.5712 0.7963 0.0078 0.0512 -0.1925 149 TRP A NE1 1181 C CE2 . TRP A 149 ? 1.5593 1.5463 0.7970 0.0179 0.0431 -0.1993 149 TRP A CE2 1182 C CE3 . TRP A 149 ? 1.4986 1.5477 0.8175 0.0366 0.0695 -0.2089 149 TRP A CE3 1183 C CZ2 . TRP A 149 ? 1.5645 1.5231 0.8020 0.0205 0.0118 -0.2015 149 TRP A CZ2 1184 C CZ3 . TRP A 149 ? 1.5134 1.5323 0.8306 0.0393 0.0397 -0.2110 149 TRP A CZ3 1185 C CH2 . TRP A 149 ? 1.5441 1.5189 0.8219 0.0308 0.0111 -0.2075 149 TRP A CH2 1186 N N . LEU A 150 ? 1.6183 1.6718 0.7976 -0.0047 0.1651 -0.1924 150 LEU A N 1187 C CA . LEU A 150 ? 1.6938 1.7114 0.8014 -0.0081 0.1808 -0.1972 150 LEU A CA 1188 C C . LEU A 150 ? 1.7519 1.7104 0.8000 -0.0075 0.1526 -0.2006 150 LEU A C 1189 O O . LEU A 150 ? 1.7425 1.6857 0.7987 -0.0126 0.1195 -0.1911 150 LEU A O 1190 C CB . LEU A 150 ? 1.7084 1.7310 0.8032 -0.0231 0.1934 -0.1841 150 LEU A CB 1191 C CG . LEU A 150 ? 1.6735 1.7506 0.8188 -0.0270 0.2225 -0.1807 150 LEU A CG 1192 C CD1 . LEU A 150 ? 1.6789 1.7556 0.8163 -0.0436 0.2264 -0.1660 150 LEU A CD1 1193 C CD2 . LEU A 150 ? 1.6925 1.7854 0.8277 -0.0198 0.2586 -0.1924 150 LEU A CD2 1194 N N . ILE A 151 ? 1.8095 1.7354 0.7987 -0.0014 0.1660 -0.2143 151 ILE A N 1195 C CA . ILE A 151 ? 1.8746 1.7383 0.7928 -0.0025 0.1416 -0.2192 151 ILE A CA 1196 C C . ILE A 151 ? 1.9529 1.7826 0.7910 -0.0073 0.1642 -0.2224 151 ILE A C 1197 O O . ILE A 151 ? 1.9431 1.7990 0.7835 -0.0078 0.2018 -0.2229 151 ILE A O 1198 C CB . ILE A 151 ? 1.8825 1.7261 0.7972 0.0112 0.1290 -0.2359 151 ILE A CB 1199 C CG1 . ILE A 151 ? 1.9110 1.7578 0.8050 0.0240 0.1667 -0.2537 151 ILE A CG1 1200 C CG2 . ILE A 151 ? 1.8057 1.6852 0.8008 0.0160 0.1105 -0.2318 151 ILE A CG2 1201 C CD1 . ILE A 151 ? 1.9320 1.7545 0.8192 0.0383 0.1563 -0.2713 151 ILE A CD1 1202 N N . LYS A 152 ? 2.0426 1.8141 0.8099 -0.0113 0.1406 -0.2240 152 LYS A N 1203 C CA . LYS A 152 ? 2.1365 1.8678 0.8176 -0.0173 0.1573 -0.2252 152 LYS A CA 1204 C C . LYS A 152 ? 2.2007 1.9291 0.8476 -0.0060 0.1982 -0.2436 152 LYS A C 1205 O O . LYS A 152 ? 2.1926 1.9280 0.8609 0.0084 0.2027 -0.2595 152 LYS A O 1206 C CB . LYS A 152 ? 2.1966 1.8633 0.8077 -0.0232 0.1184 -0.2241 152 LYS A CB 1207 C CG . LYS A 152 ? 2.2345 1.8655 0.8192 -0.0124 0.1000 -0.2432 152 LYS A CG 1208 C CD . LYS A 152 ? 2.2901 1.8654 0.8246 -0.0208 0.0521 -0.2386 152 LYS A CD 1209 C CE . LYS A 152 ? 2.3148 1.8552 0.8303 -0.0119 0.0296 -0.2573 152 LYS A CE 1210 N NZ . LYS A 152 ? 2.4011 1.8982 0.8330 -0.0045 0.0534 -0.2783 152 LYS A NZ 1211 N N . LYS A 153 ? 2.2752 1.9924 0.8692 -0.0123 0.2282 -0.2406 153 LYS A N 1212 C CA . LYS A 153 ? 2.3310 2.0444 0.8868 -0.0024 0.2715 -0.2562 153 LYS A CA 1213 C C . LYS A 153 ? 2.4221 2.0694 0.8677 -0.0075 0.2724 -0.2598 153 LYS A C 1214 O O . LYS A 153 ? 2.4305 2.0604 0.8393 -0.0226 0.2671 -0.2435 153 LYS A O 1215 C CB . LYS A 153 ? 2.3112 2.0809 0.9120 -0.0058 0.3144 -0.2481 153 LYS A CB 1216 C CG . LYS A 153 ? 2.3650 2.1471 0.9524 0.0072 0.3621 -0.2636 153 LYS A CG 1217 C CD . LYS A 153 ? 2.3685 2.1933 0.9780 -0.0017 0.4031 -0.2519 153 LYS A CD 1218 C CE . LYS A 153 ? 2.3881 2.2441 1.0153 0.0131 0.4505 -0.2656 153 LYS A CE 1219 N NZ . LYS A 153 ? 2.3206 2.2347 1.0445 0.0246 0.4510 -0.2698 153 LYS A NZ 1220 N N . ASN A 154 ? 2.4849 2.0939 0.8765 0.0052 0.2794 -0.2811 154 ASN A N 1221 C CA . ASN A 154 ? 2.6011 2.1398 0.8797 0.0018 0.2767 -0.2880 154 ASN A CA 1222 C C . ASN A 154 ? 2.6218 2.1164 0.8612 -0.0132 0.2252 -0.2740 154 ASN A C 1223 O O . ASN A 154 ? 2.6787 2.1344 0.8427 -0.0247 0.2244 -0.2649 154 ASN A O 1224 C CB . ASN A 154 ? 2.6481 2.1887 0.8789 -0.0023 0.3259 -0.2843 154 ASN A CB 1225 C CG . ASN A 154 ? 2.7901 2.2621 0.9040 0.0010 0.3370 -0.2990 154 ASN A CG 1226 O OD1 . ASN A 154 ? 2.8532 2.2768 0.9228 0.0081 0.3107 -0.3154 154 ASN A OD1 1227 N ND2 . ASN A 154 ? 2.8442 2.3102 0.9059 -0.0048 0.3764 -0.2933 154 ASN A ND2 1228 N N . SER A 155 ? 2.5599 2.0622 0.8536 -0.0128 0.1827 -0.2714 155 SER A N 1229 C CA . SER A 155 ? 2.5674 2.0354 0.8415 -0.0255 0.1304 -0.2576 155 SER A CA 1230 C C . SER A 155 ? 2.5439 2.0263 0.8258 -0.0412 0.1282 -0.2317 155 SER A C 1231 O O . SER A 155 ? 2.6350 2.0717 0.8531 -0.0524 0.1034 -0.2209 155 SER A O 1232 C CB . SER A 155 ? 2.6784 2.0686 0.8449 -0.0271 0.1086 -0.2692 155 SER A CB 1233 O OG . SER A 155 ? 2.7092 2.0800 0.8589 -0.0123 0.1154 -0.2951 155 SER A OG 1234 N N . THR A 156 ? 2.4555 1.9989 0.8132 -0.0422 0.1533 -0.2216 156 THR A N 1235 C CA . THR A 156 ? 2.4310 1.9896 0.8036 -0.0567 0.1522 -0.1977 156 THR A CA 1236 C C . THR A 156 ? 2.3400 1.9659 0.8192 -0.0561 0.1589 -0.1892 156 THR A C 1237 O O . THR A 156 ? 2.3298 1.9998 0.8550 -0.0478 0.1924 -0.1985 156 THR A O 1238 C CB . THR A 156 ? 2.4701 2.0194 0.7840 -0.0637 0.1937 -0.1930 156 THR A CB 1239 O OG1 . THR A 156 ? 2.5754 2.0659 0.7882 -0.0609 0.1981 -0.2059 156 THR A OG1 1240 C CG2 . THR A 156 ? 2.4573 2.0011 0.7642 -0.0805 0.1826 -0.1673 156 THR A CG2 1241 N N . TYR A 157 ? 2.3072 1.9401 0.8249 -0.0643 0.1265 -0.1717 157 TYR A N 1242 C CA . TYR A 157 ? 2.2033 1.8942 0.8122 -0.0661 0.1326 -0.1614 157 TYR A CA 1243 C C . TYR A 157 ? 2.2092 1.8943 0.8059 -0.0810 0.1326 -0.1399 157 TYR A C 1244 O O . TYR A 157 ? 2.2017 1.8695 0.8037 -0.0869 0.0972 -0.1255 157 TYR A O 1245 C CB . TYR A 157 ? 2.1475 1.8535 0.8203 -0.0607 0.0955 -0.1606 157 TYR A CB 1246 C CG . TYR A 157 ? 2.0621 1.8311 0.8299 -0.0578 0.1073 -0.1573 157 TYR A CG 1247 C CD1 . TYR A 157 ? 2.0222 1.8160 0.8271 -0.0675 0.1105 -0.1405 157 TYR A CD1 1248 C CD2 . TYR A 157 ? 2.0159 1.8172 0.8339 -0.0455 0.1143 -0.1712 157 TYR A CD2 1249 C CE1 . TYR A 157 ? 1.9522 1.8002 0.8381 -0.0654 0.1203 -0.1385 157 TYR A CE1 1250 C CE2 . TYR A 157 ? 1.9300 1.7868 0.8299 -0.0433 0.1236 -0.1678 157 TYR A CE2 1251 C CZ . TYR A 157 ? 1.9009 1.7808 0.8331 -0.0535 0.1265 -0.1520 157 TYR A CZ 1252 O OH . TYR A 157 ? 1.8189 1.7509 0.8273 -0.0518 0.1350 -0.1496 157 TYR A OH 1253 N N . PRO A 158 ? 2.2259 1.9242 0.8059 -0.0871 0.1725 -0.1368 158 PRO A N 1254 C CA . PRO A 158 ? 2.2262 1.9188 0.7968 -0.1019 0.1744 -0.1160 158 PRO A CA 1255 C C . PRO A 158 ? 2.1182 1.8598 0.7783 -0.1048 0.1718 -0.1065 158 PRO A C 1256 O O . PRO A 158 ? 2.0482 1.8346 0.7734 -0.0964 0.1804 -0.1167 158 PRO A O 1257 C CB . PRO A 158 ? 2.2756 1.9698 0.8038 -0.1070 0.2210 -0.1179 158 PRO A CB 1258 C CG . PRO A 158 ? 2.2485 1.9805 0.8114 -0.0940 0.2493 -0.1378 158 PRO A CG 1259 C CD . PRO A 158 ? 2.2382 1.9596 0.8134 -0.0807 0.2179 -0.1514 158 PRO A CD 1260 N N . THR A 159 ? 2.1175 1.8484 0.7785 -0.1164 0.1598 -0.0871 159 THR A N 1261 C CA . THR A 159 ? 2.0417 1.8111 0.7808 -0.1194 0.1547 -0.0779 159 THR A CA 1262 C C . THR A 159 ? 1.9991 1.8223 0.7887 -0.1205 0.1937 -0.0846 159 THR A C 1263 O O . THR A 159 ? 2.0213 1.8467 0.7808 -0.1269 0.2274 -0.0853 159 THR A O 1264 C CB . THR A 159 ? 2.0555 1.7992 0.7785 -0.1321 0.1411 -0.0560 159 THR A CB 1265 O OG1 . THR A 159 ? 2.0984 1.7921 0.7729 -0.1313 0.1036 -0.0484 159 THR A OG1 1266 C CG2 . THR A 159 ? 1.9761 1.7544 0.7778 -0.1334 0.1331 -0.0482 159 THR A CG2 1267 N N . ILE A 160 ? 1.9417 1.8079 0.8076 -0.1145 0.1885 -0.0891 160 ILE A N 1268 C CA . ILE A 160 ? 1.8920 1.8122 0.8147 -0.1160 0.2189 -0.0943 160 ILE A CA 1269 C C . ILE A 160 ? 1.8725 1.8054 0.8292 -0.1285 0.2191 -0.0797 160 ILE A C 1270 O O . ILE A 160 ? 1.8538 1.7756 0.8299 -0.1283 0.1908 -0.0710 160 ILE A O 1271 C CB . ILE A 160 ? 1.8192 1.7780 0.8044 -0.1024 0.2117 -0.1071 160 ILE A CB 1272 C CG1 . ILE A 160 ? 1.8541 1.8007 0.8092 -0.0895 0.2138 -0.1229 160 ILE A CG1 1273 C CG2 . ILE A 160 ? 1.7690 1.7836 0.8153 -0.1051 0.2382 -0.1102 160 ILE A CG2 1274 C CD1 . ILE A 160 ? 1.8016 1.7701 0.8066 -0.0759 0.1960 -0.1328 160 ILE A CD1 1275 N N . LYS A 161 ? 1.8861 1.8416 0.8507 -0.1393 0.2511 -0.0771 161 LYS A N 1276 C CA . LYS A 161 ? 1.8699 1.8408 0.8715 -0.1519 0.2542 -0.0658 161 LYS A CA 1277 C C . LYS A 161 ? 1.8305 1.8546 0.8811 -0.1563 0.2849 -0.0728 161 LYS A C 1278 O O . LYS A 161 ? 1.8667 1.8971 0.8990 -0.1665 0.3143 -0.0704 161 LYS A O 1279 C CB . LYS A 161 ? 1.9563 1.8868 0.9057 -0.1668 0.2579 -0.0493 161 LYS A CB 1280 C CG . LYS A 161 ? 2.0159 1.8953 0.9262 -0.1648 0.2232 -0.0381 161 LYS A CG 1281 C CD . LYS A 161 ? 2.0904 1.9294 0.9462 -0.1796 0.2286 -0.0207 161 LYS A CD 1282 C CE . LYS A 161 ? 2.1527 1.9381 0.9593 -0.1766 0.1940 -0.0096 161 LYS A CE 1283 N NZ . LYS A 161 ? 2.2427 1.9848 0.9851 -0.1903 0.2002 0.0074 161 LYS A NZ 1284 N N . ARG A 162 ? 1.7765 1.8391 0.8894 -0.1488 0.2775 -0.0807 162 ARG A N 1285 C CA . ARG A 162 ? 1.7393 1.8550 0.9035 -0.1520 0.3015 -0.0874 162 ARG A CA 1286 C C . ARG A 162 ? 1.6919 1.8278 0.9074 -0.1590 0.2916 -0.0829 162 ARG A C 1287 O O . ARG A 162 ? 1.6759 1.7963 0.9021 -0.1539 0.2651 -0.0797 162 ARG A O 1288 C CB . ARG A 162 ? 1.7231 1.8683 0.9128 -0.1353 0.3039 -0.1025 162 ARG A CB 1289 C CG . ARG A 162 ? 1.8031 1.9254 0.9407 -0.1262 0.3136 -0.1097 162 ARG A CG 1290 C CD . ARG A 162 ? 1.8543 1.9877 0.9714 -0.1345 0.3510 -0.1094 162 ARG A CD 1291 N NE . ARG A 162 ? 1.8218 2.0127 0.9972 -0.1322 0.3730 -0.1170 162 ARG A NE 1292 C CZ . ARG A 162 ? 1.8114 2.0249 1.0003 -0.1172 0.3852 -0.1299 162 ARG A CZ 1293 N NH1 . ARG A 162 ? 1.8420 2.0237 0.9880 -0.1031 0.3786 -0.1386 162 ARG A NH1 1294 N NH2 . ARG A 162 ? 1.7718 2.0393 1.0182 -0.1165 0.4031 -0.1341 162 ARG A NH2 1295 N N . SER A 163 ? 1.6575 1.8283 0.9053 -0.1709 0.3134 -0.0828 163 SER A N 1296 C CA . SER A 163 ? 1.6017 1.7871 0.8905 -0.1808 0.3069 -0.0788 163 SER A CA 1297 C C . SER A 163 ? 1.5560 1.7968 0.8979 -0.1854 0.3244 -0.0862 163 SER A C 1298 O O . SER A 163 ? 1.5596 1.8199 0.9008 -0.1945 0.3499 -0.0859 163 SER A O 1299 C CB . SER A 163 ? 1.6334 1.7858 0.8924 -0.1986 0.3115 -0.0651 163 SER A CB 1300 O OG . SER A 163 ? 1.6445 1.8026 0.9377 -0.2074 0.3032 -0.0619 163 SER A OG 1301 N N . TYR A 164 ? 1.5033 1.7700 0.8913 -0.1793 0.3106 -0.0921 164 TYR A N 1302 C CA . TYR A 164 ? 1.4657 1.7834 0.9043 -0.1849 0.3226 -0.0980 164 TYR A CA 1303 C C . TYR A 164 ? 1.4781 1.7978 0.9399 -0.1999 0.3168 -0.0941 164 TYR A C 1304 O O . TYR A 164 ? 1.4798 1.7728 0.9373 -0.1974 0.2977 -0.0913 164 TYR A O 1305 C CB . TYR A 164 ? 1.4007 1.7507 0.8747 -0.1676 0.3136 -0.1082 164 TYR A CB 1306 C CG . TYR A 164 ? 1.3743 1.7749 0.9005 -0.1738 0.3212 -0.1128 164 TYR A CG 1307 C CD1 . TYR A 164 ? 1.3888 1.8251 0.9323 -0.1801 0.3445 -0.1144 164 TYR A CD1 1308 C CD2 . TYR A 164 ? 1.3706 1.7833 0.9285 -0.1742 0.3050 -0.1147 164 TYR A CD2 1309 C CE1 . TYR A 164 ? 1.3683 1.8519 0.9614 -0.1868 0.3487 -0.1175 164 TYR A CE1 1310 C CE2 . TYR A 164 ? 1.3525 1.8092 0.9540 -0.1811 0.3095 -0.1186 164 TYR A CE2 1311 C CZ . TYR A 164 ? 1.3563 1.8489 0.9764 -0.1877 0.3299 -0.1197 164 TYR A CZ 1312 O OH . TYR A 164 ? 1.3475 1.8848 1.0128 -0.1951 0.3314 -0.1226 164 TYR A OH 1313 N N . ASN A 165 ? 1.5000 1.8519 0.9882 -0.2152 0.3337 -0.0945 165 ASN A N 1314 C CA . ASN A 165 ? 1.5269 1.8810 1.0355 -0.2322 0.3306 -0.0921 165 ASN A CA 1315 C C . ASN A 165 ? 1.4805 1.8847 1.0407 -0.2325 0.3292 -0.1008 165 ASN A C 1316 O O . ASN A 165 ? 1.4870 1.9315 1.0708 -0.2340 0.3442 -0.1037 165 ASN A O 1317 C CB . ASN A 165 ? 1.6092 1.9548 1.1019 -0.2539 0.3505 -0.0834 165 ASN A CB 1318 C CG . ASN A 165 ? 1.6594 2.0069 1.1734 -0.2743 0.3487 -0.0816 165 ASN A CG 1319 O OD1 . ASN A 165 ? 1.5907 1.9715 1.1446 -0.2768 0.3434 -0.0890 165 ASN A OD1 1320 N ND2 . ASN A 165 ? 1.7964 2.1056 1.2814 -0.2895 0.3528 -0.0714 165 ASN A ND2 1321 N N . ASN A 166 ? 1.4394 1.8409 1.0167 -0.2307 0.3116 -0.1044 166 ASN A N 1322 C CA . ASN A 166 ? 1.3892 1.8343 1.0105 -0.2312 0.3074 -0.1121 166 ASN A CA 1323 C C . ASN A 166 ? 1.3923 1.8565 1.0336 -0.2551 0.3168 -0.1113 166 ASN A C 1324 O O . ASN A 166 ? 1.3712 1.8165 1.0113 -0.2670 0.3087 -0.1115 166 ASN A O 1325 C CB . ASN A 166 ? 1.3567 1.7910 0.9856 -0.2205 0.2866 -0.1163 166 ASN A CB 1326 C CG . ASN A 166 ? 1.3230 1.8011 0.9918 -0.2186 0.2812 -0.1239 166 ASN A CG 1327 O OD1 . ASN A 166 ? 1.3031 1.8220 0.9964 -0.2190 0.2900 -0.1260 166 ASN A OD1 1328 N ND2 . ASN A 166 ? 1.2945 1.7643 0.9699 -0.2161 0.2668 -0.1274 166 ASN A ND2 1329 N N . THR A 167 ? 1.3899 1.8911 1.0506 -0.2620 0.3340 -0.1105 167 THR A N 1330 C CA . THR A 167 ? 1.3994 1.9275 1.0874 -0.2855 0.3426 -0.1093 167 THR A CA 1331 C C . THR A 167 ? 1.3738 1.9470 1.1065 -0.2857 0.3319 -0.1169 167 THR A C 1332 O O . THR A 167 ? 1.3867 1.9836 1.1452 -0.3057 0.3340 -0.1169 167 THR A O 1333 C CB . THR A 167 ? 1.4125 1.9628 1.1052 -0.2942 0.3678 -0.1032 167 THR A CB 1334 O OG1 . THR A 167 ? 1.3822 1.9683 1.0937 -0.2757 0.3746 -0.1072 167 THR A OG1 1335 C CG2 . THR A 167 ? 1.4429 1.9461 1.0866 -0.2974 0.3786 -0.0944 167 THR A CG2 1336 N N . ASN A 168 ? 1.3274 1.9113 1.0685 -0.2645 0.3194 -0.1227 168 ASN A N 1337 C CA . ASN A 168 ? 1.2704 1.8923 1.0482 -0.2631 0.3070 -0.1289 168 ASN A CA 1338 C C . ASN A 168 ? 1.2608 1.8612 1.0326 -0.2743 0.2918 -0.1326 168 ASN A C 1339 O O . ASN A 168 ? 1.3224 1.8762 1.0623 -0.2737 0.2874 -0.1316 168 ASN A O 1340 C CB . ASN A 168 ? 1.2365 1.8698 1.0208 -0.2373 0.2977 -0.1326 168 ASN A CB 1341 C CG . ASN A 168 ? 1.2225 1.8758 1.0129 -0.2238 0.3121 -0.1310 168 ASN A CG 1342 O OD1 . ASN A 168 ? 1.2156 1.9140 1.0408 -0.2260 0.3209 -0.1309 168 ASN A OD1 1343 N ND2 . ASN A 168 ? 1.2101 1.8297 0.9670 -0.2094 0.3140 -0.1298 168 ASN A ND2 1344 N N . GLN A 169 ? 1.2126 1.8460 1.0144 -0.2839 0.2833 -0.1372 169 GLN A N 1345 C CA . GLN A 169 ? 1.2101 1.8240 1.0044 -0.2929 0.2684 -0.1430 169 GLN A CA 1346 C C . GLN A 169 ? 1.1796 1.7734 0.9591 -0.2714 0.2552 -0.1470 169 GLN A C 1347 O O . GLN A 169 ? 1.1681 1.7287 0.9285 -0.2742 0.2471 -0.1508 169 GLN A O 1348 C CB . GLN A 169 ? 1.1987 1.8541 1.0266 -0.3084 0.2606 -0.1471 169 GLN A CB 1349 C CG . GLN A 169 ? 1.2105 1.8638 1.0438 -0.3382 0.2647 -0.1463 169 GLN A CG 1350 C CD . GLN A 169 ? 1.2156 1.8751 1.0571 -0.3530 0.2475 -0.1544 169 GLN A CD 1351 O OE1 . GLN A 169 ? 1.1915 1.8938 1.0663 -0.3661 0.2425 -0.1548 169 GLN A OE1 1352 N NE2 . GLN A 169 ? 1.2127 1.8292 1.0234 -0.3502 0.2380 -0.1610 169 GLN A NE2 1353 N N . GLU A 170 ? 1.1455 1.7586 0.9347 -0.2501 0.2541 -0.1459 170 GLU A N 1354 C CA . GLU A 170 ? 1.1105 1.7150 0.8948 -0.2305 0.2414 -0.1486 170 GLU A CA 1355 C C . GLU A 170 ? 1.1147 1.6814 0.8727 -0.2139 0.2419 -0.1450 170 GLU A C 1356 O O . GLU A 170 ? 1.1457 1.7085 0.8959 -0.2088 0.2512 -0.1407 170 GLU A O 1357 C CB . GLU A 170 ? 1.0722 1.7217 0.8865 -0.2176 0.2370 -0.1490 170 GLU A CB 1358 C CG . GLU A 170 ? 1.0707 1.7637 0.9161 -0.2320 0.2339 -0.1510 170 GLU A CG 1359 C CD . GLU A 170 ? 1.0714 1.7970 0.9404 -0.2393 0.2478 -0.1471 170 GLU A CD 1360 O OE1 . GLU A 170 ? 1.1263 1.8321 0.9792 -0.2432 0.2620 -0.1437 170 GLU A OE1 1361 O OE2 . GLU A 170 ? 1.0269 1.7983 0.9309 -0.2409 0.2447 -0.1467 170 GLU A OE2 1362 N N . ASP A 171 ? 1.1157 1.6550 0.8603 -0.2057 0.2319 -0.1466 171 ASP A N 1363 C CA . ASP A 171 ? 1.1114 1.6197 0.8381 -0.1883 0.2283 -0.1426 171 ASP A CA 1364 C C . ASP A 171 ? 1.0849 1.6129 0.8206 -0.1728 0.2295 -0.1401 171 ASP A C 1365 O O . ASP A 171 ? 1.0575 1.6233 0.8180 -0.1680 0.2280 -0.1423 171 ASP A O 1366 C CB . ASP A 171 ? 1.1303 1.6268 0.8574 -0.1773 0.2170 -0.1448 171 ASP A CB 1367 C CG . ASP A 171 ? 1.1608 1.6249 0.8721 -0.1876 0.2161 -0.1477 171 ASP A CG 1368 O OD1 . ASP A 171 ? 1.2259 1.6623 0.9199 -0.1989 0.2218 -0.1455 171 ASP A OD1 1369 O OD2 . ASP A 171 ? 1.1645 1.6289 0.8795 -0.1836 0.2101 -0.1520 171 ASP A OD2 1370 N N . LEU A 172 ? 1.1059 1.6063 0.8205 -0.1645 0.2311 -0.1356 172 LEU A N 1371 C CA . LEU A 172 ? 1.1070 1.6184 0.8238 -0.1502 0.2327 -0.1345 172 LEU A CA 1372 C C . LEU A 172 ? 1.0888 1.5753 0.7956 -0.1329 0.2202 -0.1318 172 LEU A C 1373 O O . LEU A 172 ? 1.0990 1.5487 0.7844 -0.1330 0.2155 -0.1278 172 LEU A O 1374 C CB . LEU A 172 ? 1.1556 1.6569 0.8524 -0.1571 0.2467 -0.1319 172 LEU A CB 1375 C CG . LEU A 172 ? 1.1810 1.6966 0.8788 -0.1443 0.2529 -0.1329 172 LEU A CG 1376 C CD1 . LEU A 172 ? 1.1640 1.7293 0.8968 -0.1455 0.2611 -0.1365 172 LEU A CD1 1377 C CD2 . LEU A 172 ? 1.2342 1.7235 0.8982 -0.1485 0.2649 -0.1295 172 LEU A CD2 1378 N N . LEU A 173 ? 1.0581 1.5650 0.7827 -0.1182 0.2141 -0.1330 173 LEU A N 1379 C CA . LEU A 173 ? 1.0517 1.5382 0.7705 -0.1024 0.2020 -0.1300 173 LEU A CA 1380 C C . LEU A 173 ? 1.0729 1.5458 0.7722 -0.0959 0.2052 -0.1296 173 LEU A C 1381 O O . LEU A 173 ? 1.0878 1.5841 0.7970 -0.0911 0.2120 -0.1331 173 LEU A O 1382 C CB . LEU A 173 ? 1.0335 1.5458 0.7800 -0.0904 0.1935 -0.1308 173 LEU A CB 1383 C CG . LEU A 173 ? 1.0330 1.5290 0.7792 -0.0745 0.1808 -0.1272 173 LEU A CG 1384 C CD1 . LEU A 173 ? 1.0538 1.5140 0.7852 -0.0743 0.1726 -0.1221 173 LEU A CD1 1385 C CD2 . LEU A 173 ? 1.0013 1.5234 0.7759 -0.0647 0.1737 -0.1266 173 LEU A CD2 1386 N N . VAL A 174 ? 1.1031 1.5371 0.7741 -0.0951 0.1998 -0.1253 174 VAL A N 1387 C CA . VAL A 174 ? 1.1028 1.5165 0.7468 -0.0896 0.2010 -0.1252 174 VAL A CA 1388 C C . VAL A 174 ? 1.0859 1.4799 0.7276 -0.0753 0.1828 -0.1227 174 VAL A C 1389 O O . VAL A 174 ? 1.0717 1.4497 0.7179 -0.0736 0.1701 -0.1174 174 VAL A O 1390 C CB . VAL A 174 ? 1.1383 1.5192 0.7461 -0.1010 0.2071 -0.1209 174 VAL A CB 1391 C CG1 . VAL A 174 ? 1.1818 1.5447 0.7571 -0.0966 0.2118 -0.1220 174 VAL A CG1 1392 C CG2 . VAL A 174 ? 1.1388 1.5362 0.7523 -0.1177 0.2230 -0.1216 174 VAL A CG2 1393 N N . LEU A 175 ? 1.0811 1.4760 0.7170 -0.0653 0.1819 -0.1265 175 LEU A N 1394 C CA . LEU A 175 ? 1.0839 1.4588 0.7164 -0.0530 0.1639 -0.1248 175 LEU A CA 1395 C C . LEU A 175 ? 1.1213 1.4623 0.7114 -0.0516 0.1628 -0.1262 175 LEU A C 1396 O O . LEU A 175 ? 1.1346 1.4801 0.7073 -0.0534 0.1789 -0.1317 175 LEU A O 1397 C CB . LEU A 175 ? 1.0644 1.4665 0.7261 -0.0413 0.1615 -0.1291 175 LEU A CB 1398 C CG . LEU A 175 ? 1.0529 1.4897 0.7542 -0.0413 0.1616 -0.1278 175 LEU A CG 1399 C CD1 . LEU A 175 ? 1.0432 1.5072 0.7692 -0.0304 0.1621 -0.1316 175 LEU A CD1 1400 C CD2 . LEU A 175 ? 1.0332 1.4582 0.7463 -0.0396 0.1467 -0.1205 175 LEU A CD2 1401 N N . TRP A 176 ? 1.1338 1.4413 0.7073 -0.0485 0.1438 -0.1208 176 TRP A N 1402 C CA . TRP A 176 ? 1.1863 1.4585 0.7174 -0.0457 0.1374 -0.1224 176 TRP A CA 1403 C C . TRP A 176 ? 1.1845 1.4363 0.7205 -0.0372 0.1112 -0.1187 176 TRP A C 1404 O O . TRP A 176 ? 1.1425 1.4105 0.7168 -0.0331 0.1012 -0.1145 176 TRP A O 1405 C CB . TRP A 176 ? 1.2345 1.4773 0.7249 -0.0569 0.1423 -0.1173 176 TRP A CB 1406 C CG . TRP A 176 ? 1.2420 1.4649 0.7353 -0.0611 0.1265 -0.1064 176 TRP A CG 1407 C CD1 . TRP A 176 ? 1.2690 1.4553 0.7403 -0.0592 0.1050 -0.0993 176 TRP A CD1 1408 C CD2 . TRP A 176 ? 1.2165 1.4541 0.7370 -0.0674 0.1308 -0.1016 176 TRP A CD2 1409 N NE1 . TRP A 176 ? 1.2574 1.4368 0.7443 -0.0628 0.0964 -0.0894 176 TRP A NE1 1410 C CE2 . TRP A 176 ? 1.2287 1.4375 0.7440 -0.0675 0.1129 -0.0914 176 TRP A CE2 1411 C CE3 . TRP A 176 ? 1.1826 1.4539 0.7308 -0.0729 0.1472 -0.1051 176 TRP A CE3 1412 C CZ2 . TRP A 176 ? 1.2137 1.4251 0.7502 -0.0716 0.1133 -0.0855 176 TRP A CZ2 1413 C CZ3 . TRP A 176 ? 1.1769 1.4488 0.7421 -0.0784 0.1463 -0.1000 176 TRP A CZ3 1414 C CH2 . TRP A 176 ? 1.1935 1.4350 0.7527 -0.0771 0.1305 -0.0906 176 TRP A CH2 1415 N N . GLY A 177 ? 1.2525 1.4686 0.7493 -0.0351 0.1001 -0.1199 177 GLY A N 1416 C CA . GLY A 177 ? 1.2642 1.4592 0.7650 -0.0286 0.0729 -0.1162 177 GLY A CA 1417 C C . GLY A 177 ? 1.3074 1.4561 0.7571 -0.0307 0.0575 -0.1149 177 GLY A C 1418 O O . GLY A 177 ? 1.3495 1.4800 0.7542 -0.0358 0.0701 -0.1183 177 GLY A O 1419 N N . ILE A 178 ? 1.3095 1.4394 0.7667 -0.0273 0.0297 -0.1093 178 ILE A N 1420 C CA . ILE A 178 ? 1.3738 1.4585 0.7847 -0.0292 0.0087 -0.1076 178 ILE A CA 1421 C C . ILE A 178 ? 1.3892 1.4635 0.8054 -0.0216 -0.0105 -0.1134 178 ILE A C 1422 O O . ILE A 178 ? 1.3379 1.4370 0.8037 -0.0163 -0.0165 -0.1116 178 ILE A O 1423 C CB . ILE A 178 ? 1.3874 1.4539 0.8015 -0.0345 -0.0120 -0.0922 178 ILE A CB 1424 C CG1 . ILE A 178 ? 1.4594 1.4773 0.8178 -0.0382 -0.0336 -0.0897 178 ILE A CG1 1425 C CG2 . ILE A 178 ? 1.3432 1.4282 0.8155 -0.0297 -0.0303 -0.0836 178 ILE A CG2 1426 C CD1 . ILE A 178 ? 1.4850 1.4831 0.8405 -0.0437 -0.0518 -0.0736 178 ILE A CD1 1427 N N . HIS A 179 ? 1.4468 1.4828 0.8098 -0.0217 -0.0196 -0.1206 179 HIS A N 1428 C CA . HIS A 179 ? 1.4774 1.4950 0.8379 -0.0160 -0.0405 -0.1270 179 HIS A CA 1429 C C . HIS A 179 ? 1.5222 1.5037 0.8671 -0.0209 -0.0770 -0.1174 179 HIS A C 1430 O O . HIS A 179 ? 1.5753 1.5240 0.8703 -0.0273 -0.0841 -0.1141 179 HIS A O 1431 C CB . HIS A 179 ? 1.5210 1.5179 0.8314 -0.0116 -0.0261 -0.1440 179 HIS A CB 1432 C CG . HIS A 179 ? 1.5429 1.5094 0.8381 -0.0070 -0.0495 -0.1520 179 HIS A CG 1433 N ND1 . HIS A 179 ? 1.6251 1.5421 0.8530 -0.0090 -0.0609 -0.1602 179 HIS A ND1 1434 C CD2 . HIS A 179 ? 1.5170 1.4933 0.8542 -0.0014 -0.0647 -0.1529 179 HIS A CD2 1435 C CE1 . HIS A 179 ? 1.6420 1.5388 0.8710 -0.0049 -0.0826 -0.1669 179 HIS A CE1 1436 N NE2 . HIS A 179 ? 1.5855 1.5180 0.8820 -0.0004 -0.0852 -0.1622 179 HIS A NE2 1437 N N . HIS A 180 ? 1.4984 1.4868 0.8871 -0.0183 -0.1004 -0.1120 180 HIS A N 1438 C CA . HIS A 180 ? 1.5443 1.5012 0.9253 -0.0228 -0.1380 -0.1031 180 HIS A CA 1439 C C . HIS A 180 ? 1.5925 1.5157 0.9387 -0.0209 -0.1537 -0.1162 180 HIS A C 1440 O O . HIS A 180 ? 1.5679 1.5054 0.9446 -0.0149 -0.1523 -0.1228 180 HIS A O 1441 C CB . HIS A 180 ? 1.5062 1.4905 0.9585 -0.0219 -0.1545 -0.0884 180 HIS A CB 1442 C CG . HIS A 180 ? 1.4870 1.5033 0.9750 -0.0224 -0.1378 -0.0772 180 HIS A CG 1443 N ND1 . HIS A 180 ? 1.5292 1.5332 0.9859 -0.0275 -0.1303 -0.0722 180 HIS A ND1 1444 C CD2 . HIS A 180 ? 1.4403 1.4974 0.9898 -0.0187 -0.1271 -0.0704 180 HIS A CD2 1445 C CE1 . HIS A 180 ? 1.4724 1.5073 0.9707 -0.0267 -0.1160 -0.0638 180 HIS A CE1 1446 N NE2 . HIS A 180 ? 1.4285 1.4959 0.9820 -0.0212 -0.1135 -0.0630 180 HIS A NE2 1447 N N . PRO A 181 ? 1.6617 1.5376 0.9410 -0.0260 -0.1689 -0.1201 181 PRO A N 1448 C CA . PRO A 181 ? 1.7098 1.5476 0.9486 -0.0246 -0.1845 -0.1343 181 PRO A CA 1449 C C . PRO A 181 ? 1.6986 1.5247 0.9693 -0.0282 -0.2255 -0.1264 181 PRO A C 1450 O O . PRO A 181 ? 1.6488 1.4938 0.9680 -0.0319 -0.2424 -0.1086 181 PRO A O 1451 C CB . PRO A 181 ? 1.7998 1.5911 0.9542 -0.0304 -0.1872 -0.1387 181 PRO A CB 1452 C CG . PRO A 181 ? 1.7959 1.5927 0.9607 -0.0376 -0.1971 -0.1193 181 PRO A CG 1453 C CD . PRO A 181 ? 1.7103 1.5627 0.9476 -0.0337 -0.1750 -0.1107 181 PRO A CD 1454 N N . ASN A 182 ? 1.7422 1.5362 0.9862 -0.0270 -0.2408 -0.1396 182 ASN A N 1455 C CA . ASN A 182 ? 1.7528 1.5343 1.0274 -0.0316 -0.2801 -0.1333 182 ASN A CA 1456 C C . ASN A 182 ? 1.8026 1.5465 1.0451 -0.0426 -0.3194 -0.1232 182 ASN A C 1457 O O . ASN A 182 ? 1.7777 1.5351 1.0716 -0.0477 -0.3467 -0.1056 182 ASN A O 1458 C CB . ASN A 182 ? 1.7916 1.5474 1.0467 -0.0274 -0.2843 -0.1518 182 ASN A CB 1459 C CG . ASN A 182 ? 1.7613 1.5369 1.0866 -0.0274 -0.3032 -0.1445 182 ASN A CG 1460 O OD1 . ASN A 182 ? 1.6935 1.5154 1.0788 -0.0212 -0.2823 -0.1390 182 ASN A OD1 1461 N ND2 . ASN A 182 ? 1.8064 1.5475 1.1254 -0.0355 -0.3436 -0.1433 182 ASN A ND2 1462 N N . ASP A 183 ? 1.8649 1.5620 1.0226 -0.0458 -0.3219 -0.1338 183 ASP A N 1463 C CA . ASP A 183 ? 1.9282 1.5819 1.0420 -0.0565 -0.3613 -0.1260 183 ASP A CA 1464 C C . ASP A 183 ? 1.9604 1.5857 0.9947 -0.0589 -0.3469 -0.1285 183 ASP A C 1465 O O . ASP A 183 ? 1.9292 1.5682 0.9432 -0.0527 -0.3057 -0.1375 183 ASP A O 1466 C CB . ASP A 183 ? 1.9950 1.6027 1.0775 -0.0611 -0.3956 -0.1380 183 ASP A CB 1467 C CG . ASP A 183 ? 2.0391 1.6182 1.0620 -0.0539 -0.3718 -0.1647 183 ASP A CG 1468 O OD1 . ASP A 183 ? 2.0690 1.6418 1.0395 -0.0492 -0.3384 -0.1741 183 ASP A OD1 1469 O OD2 . ASP A 183 ? 2.0521 1.6139 1.0815 -0.0529 -0.3864 -0.1761 183 ASP A OD2 1470 N N . ALA A 184 ? 2.0108 1.5971 1.0016 -0.0686 -0.3817 -0.1196 184 ALA A N 1471 C CA . ALA A 184 ? 2.0721 1.6250 0.9813 -0.0725 -0.3730 -0.1197 184 ALA A CA 1472 C C . ALA A 184 ? 2.1311 1.6498 0.9580 -0.0684 -0.3460 -0.1443 184 ALA A C 1473 O O . ALA A 184 ? 2.1426 1.6543 0.9192 -0.0678 -0.3167 -0.1465 184 ALA A O 1474 C CB . ALA A 184 ? 2.1146 1.6269 0.9895 -0.0839 -0.4214 -0.1060 184 ALA A CB 1475 N N . ALA A 185 ? 2.1588 1.6565 0.9742 -0.0655 -0.3549 -0.1622 185 ALA A N 1476 C CA . ALA A 185 ? 2.2142 1.6769 0.9541 -0.0597 -0.3302 -0.1873 185 ALA A CA 1477 C C . ALA A 185 ? 2.1562 1.6612 0.9231 -0.0472 -0.2764 -0.1973 185 ALA A C 1478 O O . ALA A 185 ? 2.1891 1.6779 0.8951 -0.0428 -0.2438 -0.2104 185 ALA A O 1479 C CB . ALA A 185 ? 2.2591 1.6835 0.9815 -0.0602 -0.3587 -0.2033 185 ALA A CB 1480 N N . GLU A 186 ? 2.0735 1.6328 0.9314 -0.0417 -0.2673 -0.1905 186 GLU A N 1481 C CA . GLU A 186 ? 2.0227 1.6258 0.9139 -0.0304 -0.2201 -0.1984 186 GLU A CA 1482 C C . GLU A 186 ? 1.9908 1.6203 0.8774 -0.0318 -0.1886 -0.1885 186 GLU A C 1483 O O . GLU A 186 ? 1.9667 1.6143 0.8437 -0.0247 -0.1476 -0.1985 186 GLU A O 1484 C CB . GLU A 186 ? 1.9501 1.6018 0.9367 -0.0252 -0.2218 -0.1924 186 GLU A CB 1485 C CG . GLU A 186 ? 1.9193 1.6073 0.9347 -0.0126 -0.1800 -0.2042 186 GLU A CG 1486 C CD . GLU A 186 ? 1.8611 1.5884 0.9611 -0.0076 -0.1853 -0.1995 186 GLU A CD 1487 O OE1 . GLU A 186 ? 1.8022 1.5722 0.9655 -0.0101 -0.1862 -0.1820 186 GLU A OE1 1488 O OE2 . GLU A 186 ? 1.8703 1.5840 0.9714 -0.0007 -0.1875 -0.2132 186 GLU A OE2 1489 N N . GLN A 187 ? 1.9796 1.6114 0.8759 -0.0411 -0.2082 -0.1685 187 GLN A N 1490 C CA . GLN A 187 ? 1.9680 1.6151 0.8524 -0.0446 -0.1837 -0.1578 187 GLN A CA 1491 C C . GLN A 187 ? 2.0518 1.6603 0.8435 -0.0457 -0.1618 -0.1697 187 GLN A C 1492 O O . GLN A 187 ? 2.0344 1.6649 0.8203 -0.0424 -0.1209 -0.1737 187 GLN A O 1493 C CB . GLN A 187 ? 1.9571 1.5999 0.8568 -0.0540 -0.2154 -0.1349 187 GLN A CB 1494 C CG . GLN A 187 ? 1.9512 1.6007 0.8325 -0.0590 -0.1951 -0.1224 187 GLN A CG 1495 C CD . GLN A 187 ? 1.8609 1.5668 0.8037 -0.0543 -0.1578 -0.1199 187 GLN A CD 1496 O OE1 . GLN A 187 ? 1.7801 1.5254 0.7985 -0.0499 -0.1605 -0.1158 187 GLN A OE1 1497 N NE2 . GLN A 187 ? 1.8675 1.5769 0.7768 -0.0561 -0.1232 -0.1218 187 GLN A NE2 1498 N N . THR A 188 ? 2.1439 1.6946 0.8629 -0.0507 -0.1892 -0.1750 188 THR A N 1499 C CA . THR A 188 ? 2.2242 1.7320 0.8467 -0.0519 -0.1699 -0.1865 188 THR A CA 1500 C C . THR A 188 ? 2.2225 1.7346 0.8312 -0.0398 -0.1332 -0.2105 188 THR A C 1501 O O . THR A 188 ? 2.2490 1.7623 0.8188 -0.0368 -0.0937 -0.2173 188 THR A O 1502 C CB . THR A 188 ? 2.3287 1.7696 0.8715 -0.0604 -0.2108 -0.1876 188 THR A CB 1503 O OG1 . THR A 188 ? 2.3554 1.7761 0.9051 -0.0573 -0.2381 -0.2011 188 THR A OG1 1504 C CG2 . THR A 188 ? 2.3290 1.7653 0.8848 -0.0717 -0.2473 -0.1623 188 THR A CG2 1505 N N . LYS A 189 ? 2.1884 1.7045 0.8332 -0.0325 -0.1458 -0.2221 189 LYS A N 1506 C CA . LYS A 189 ? 2.1968 1.7145 0.8337 -0.0193 -0.1151 -0.2448 189 LYS A CA 1507 C C . LYS A 189 ? 2.1457 1.7216 0.8315 -0.0110 -0.0665 -0.2447 189 LYS A C 1508 O O . LYS A 189 ? 2.1670 1.7412 0.8260 -0.0011 -0.0314 -0.2614 189 LYS A O 1509 C CB . LYS A 189 ? 2.1827 1.6967 0.8610 -0.0143 -0.1421 -0.2532 189 LYS A CB 1510 C CG . LYS A 189 ? 2.1857 1.7077 0.8749 0.0010 -0.1136 -0.2744 189 LYS A CG 1511 C CD . LYS A 189 ? 2.1935 1.6973 0.9090 0.0033 -0.1468 -0.2820 189 LYS A CD 1512 C CE . LYS A 189 ? 2.1135 1.6705 0.9184 0.0140 -0.1314 -0.2817 189 LYS A CE 1513 N NZ . LYS A 189 ? 2.1189 1.6932 0.9191 0.0293 -0.0842 -0.2975 189 LYS A NZ 1514 N N . LEU A 190 ? 2.0664 1.6924 0.8230 -0.0150 -0.0648 -0.2263 190 LEU A N 1515 C CA . LEU A 190 ? 2.0111 1.6941 0.8186 -0.0095 -0.0233 -0.2244 190 LEU A CA 1516 C C . LEU A 190 ? 2.0259 1.7175 0.8088 -0.0180 -0.0004 -0.2128 190 LEU A C 1517 O O . LEU A 190 ? 2.0158 1.7287 0.7930 -0.0141 0.0401 -0.2186 190 LEU A O 1518 C CB . LEU A 190 ? 1.9111 1.6461 0.8156 -0.0077 -0.0330 -0.2134 190 LEU A CB 1519 C CG . LEU A 190 ? 1.8736 1.6270 0.8248 0.0044 -0.0314 -0.2253 190 LEU A CG 1520 C CD1 . LEU A 190 ? 1.9474 1.6471 0.8512 0.0077 -0.0551 -0.2404 190 LEU A CD1 1521 C CD2 . LEU A 190 ? 1.7857 1.5811 0.8225 0.0031 -0.0486 -0.2109 190 LEU A CD2 1522 N N . TYR A 191 ? 2.0504 1.7264 0.8226 -0.0297 -0.0268 -0.1954 191 TYR A N 1523 C CA . TYR A 191 ? 2.0551 1.7409 0.8151 -0.0390 -0.0098 -0.1807 191 TYR A CA 1524 C C . TYR A 191 ? 2.1566 1.7862 0.8283 -0.0487 -0.0236 -0.1750 191 TYR A C 1525 O O . TYR A 191 ? 2.1860 1.8160 0.8340 -0.0565 -0.0060 -0.1641 191 TYR A O 1526 C CB . TYR A 191 ? 1.9840 1.7079 0.8196 -0.0436 -0.0248 -0.1619 191 TYR A CB 1527 C CG . TYR A 191 ? 1.8951 1.6680 0.8144 -0.0348 -0.0201 -0.1659 191 TYR A CG 1528 C CD1 . TYR A 191 ? 1.8574 1.6734 0.8101 -0.0287 0.0182 -0.1732 191 TYR A CD1 1529 C CD2 . TYR A 191 ? 1.8538 1.6303 0.8187 -0.0329 -0.0543 -0.1615 191 TYR A CD2 1530 C CE1 . TYR A 191 ? 1.7770 1.6364 0.8027 -0.0209 0.0214 -0.1758 191 TYR A CE1 1531 C CE2 . TYR A 191 ? 1.7848 1.6047 0.8228 -0.0252 -0.0491 -0.1639 191 TYR A CE2 1532 C CZ . TYR A 191 ? 1.7392 1.5993 0.8051 -0.0191 -0.0116 -0.1712 191 TYR A CZ 1533 O OH . TYR A 191 ? 1.6667 1.5684 0.8012 -0.0117 -0.0073 -0.1727 191 TYR A OH 1534 N N . ARG A 192 ? 2.2147 1.7950 0.8371 -0.0491 -0.0561 -0.1818 192 ARG A N 1535 C CA . ARG A 192 ? 2.2905 1.8116 0.8234 -0.0584 -0.0760 -0.1771 192 ARG A CA 1536 C C . ARG A 192 ? 2.2624 1.7796 0.8094 -0.0695 -0.1072 -0.1521 192 ARG A C 1537 O O . ARG A 192 ? 2.2898 1.7738 0.8199 -0.0743 -0.1515 -0.1460 192 ARG A O 1538 C CB . ARG A 192 ? 2.3695 1.8708 0.8269 -0.0590 -0.0358 -0.1848 192 ARG A CB 1539 C CG . ARG A 192 ? 2.4977 1.9305 0.8517 -0.0604 -0.0497 -0.1972 192 ARG A CG 1540 C CD . ARG A 192 ? 2.5670 1.9811 0.8456 -0.0606 -0.0066 -0.2042 192 ARG A CD 1541 N NE . ARG A 192 ? 2.6080 2.0086 0.8504 -0.0737 -0.0070 -0.1829 192 ARG A NE 1542 C CZ . ARG A 192 ? 2.7042 2.0465 0.8613 -0.0831 -0.0325 -0.1757 192 ARG A CZ 1543 N NH1 . ARG A 192 ? 2.7778 2.0668 0.8715 -0.0819 -0.0610 -0.1891 192 ARG A NH1 1544 N NH2 . ARG A 192 ? 2.7210 2.0561 0.8541 -0.0945 -0.0303 -0.1545 192 ARG A NH2 1545 N N . ASN A 193 ? 2.2038 1.7538 0.7826 -0.0736 -0.0851 -0.1377 193 ASN A N 1546 C CA . ASN A 193 ? 2.1821 1.7325 0.7838 -0.0821 -0.1110 -0.1138 193 ASN A CA 1547 C C . ASN A 193 ? 2.1387 1.7014 0.8053 -0.0798 -0.1523 -0.1073 193 ASN A C 1548 O O . ASN A 193 ? 2.0710 1.6748 0.8079 -0.0722 -0.1453 -0.1138 193 ASN A O 1549 C CB . ASN A 193 ? 2.1219 1.7168 0.7718 -0.0844 -0.0788 -0.1029 193 ASN A CB 1550 C CG . ASN A 193 ? 2.1629 1.7482 0.7544 -0.0889 -0.0385 -0.1056 193 ASN A CG 1551 O OD1 . ASN A 193 ? 2.1043 1.7275 0.7243 -0.0854 0.0009 -0.1136 193 ASN A OD1 1552 N ND2 . ASN A 193 ? 2.2553 1.7900 0.7647 -0.0971 -0.0485 -0.0980 193 ASN A ND2 1553 N N . PRO A 194 ? 2.1840 1.7116 0.8280 -0.0865 -0.1957 -0.0935 194 PRO A N 1554 C CA . PRO A 194 ? 2.1440 1.6830 0.8505 -0.0850 -0.2358 -0.0863 194 PRO A CA 1555 C C . PRO A 194 ? 2.0623 1.6504 0.8592 -0.0833 -0.2336 -0.0694 194 PRO A C 1556 O O . PRO A 194 ? 1.9805 1.6034 0.8509 -0.0775 -0.2404 -0.0707 194 PRO A O 1557 C CB . PRO A 194 ? 2.2288 1.7134 0.8762 -0.0936 -0.2811 -0.0759 194 PRO A CB 1558 C CG . PRO A 194 ? 2.2856 1.7430 0.8632 -0.1003 -0.2645 -0.0674 194 PRO A CG 1559 C CD . PRO A 194 ? 2.2730 1.7499 0.8345 -0.0961 -0.2100 -0.0825 194 PRO A CD 1560 N N . THR A 195 ? 2.0721 1.6607 0.8613 -0.0883 -0.2235 -0.0538 195 THR A N 1561 C CA . THR A 195 ? 1.9994 1.6298 0.8665 -0.0865 -0.2173 -0.0390 195 THR A CA 1562 C C . THR A 195 ? 1.9707 1.6333 0.8489 -0.0855 -0.1682 -0.0454 195 THR A C 1563 O O . THR A 195 ? 2.0265 1.6691 0.8468 -0.0913 -0.1469 -0.0449 195 THR A O 1564 C CB . THR A 195 ? 2.0228 1.6296 0.8789 -0.0928 -0.2428 -0.0154 195 THR A CB 1565 O OG1 . THR A 195 ? 2.0604 1.6343 0.8991 -0.0951 -0.2907 -0.0086 195 THR A OG1 1566 C CG2 . THR A 195 ? 1.9465 1.5942 0.8863 -0.0891 -0.2381 -0.0012 195 THR A CG2 1567 N N . THR A 196 ? 1.8969 1.6091 0.8490 -0.0788 -0.1508 -0.0506 196 THR A N 1568 C CA . THR A 196 ? 1.8531 1.5999 0.8231 -0.0783 -0.1068 -0.0571 196 THR A CA 1569 C C . THR A 196 ? 1.7820 1.5701 0.8292 -0.0764 -0.1006 -0.0468 196 THR A C 1570 O O . THR A 196 ? 1.7453 1.5389 0.8373 -0.0737 -0.1277 -0.0358 196 THR A O 1571 C CB . THR A 196 ? 1.8350 1.6033 0.8108 -0.0713 -0.0832 -0.0783 196 THR A CB 1572 O OG1 . THR A 196 ? 1.7745 1.5670 0.8113 -0.0637 -0.1006 -0.0816 196 THR A OG1 1573 C CG2 . THR A 196 ? 1.9212 1.6470 0.8162 -0.0720 -0.0834 -0.0908 196 THR A CG2 1574 N N . TYR A 197 ? 1.7552 1.5716 0.8166 -0.0782 -0.0643 -0.0507 197 TYR A N 1575 C CA . TYR A 197 ? 1.6823 1.5357 0.8089 -0.0773 -0.0537 -0.0437 197 TYR A CA 1576 C C . TYR A 197 ? 1.6653 1.5544 0.8073 -0.0782 -0.0140 -0.0550 197 TYR A C 1577 O O . TYR A 197 ? 1.6886 1.5718 0.7885 -0.0802 0.0068 -0.0655 197 TYR A O 1578 C CB . TYR A 197 ? 1.6964 1.5285 0.8122 -0.0841 -0.0612 -0.0255 197 TYR A CB 1579 C CG . TYR A 197 ? 1.7265 1.5377 0.7838 -0.0942 -0.0375 -0.0240 197 TYR A CG 1580 C CD1 . TYR A 197 ? 1.7961 1.5644 0.7772 -0.0989 -0.0445 -0.0237 197 TYR A CD1 1581 C CD2 . TYR A 197 ? 1.6890 1.5226 0.7660 -0.0997 -0.0080 -0.0225 197 TYR A CD2 1582 C CE1 . TYR A 197 ? 1.8331 1.5826 0.7601 -0.1085 -0.0208 -0.0210 197 TYR A CE1 1583 C CE2 . TYR A 197 ? 1.7284 1.5441 0.7552 -0.1102 0.0143 -0.0198 197 TYR A CE2 1584 C CZ . TYR A 197 ? 1.8037 1.5781 0.7561 -0.1144 0.0088 -0.0184 197 TYR A CZ 1585 O OH . TYR A 197 ? 1.8352 1.5922 0.7371 -0.1251 0.0330 -0.0145 197 TYR A OH 1586 N N . ILE A 198 ? 1.6311 1.5573 0.8339 -0.0764 -0.0038 -0.0529 198 ILE A N 1587 C CA . ILE A 198 ? 1.6076 1.5675 0.8284 -0.0798 0.0310 -0.0603 198 ILE A CA 1588 C C . ILE A 198 ? 1.5810 1.5510 0.8347 -0.0846 0.0351 -0.0494 198 ILE A C 1589 O O . ILE A 198 ? 1.5550 1.5380 0.8562 -0.0788 0.0205 -0.0441 198 ILE A O 1590 C CB . ILE A 198 ? 1.5635 1.5651 0.8304 -0.0714 0.0412 -0.0734 198 ILE A CB 1591 C CG1 . ILE A 198 ? 1.5869 1.5765 0.8259 -0.0649 0.0354 -0.0850 198 ILE A CG1 1592 C CG2 . ILE A 198 ? 1.5378 1.5742 0.8223 -0.0759 0.0749 -0.0800 198 ILE A CG2 1593 C CD1 . ILE A 198 ? 1.5430 1.5640 0.8322 -0.0548 0.0313 -0.0932 198 ILE A CD1 1594 N N . SER A 199 ? 1.5970 1.5595 0.8252 -0.0950 0.0556 -0.0459 199 SER A N 1595 C CA . SER A 199 ? 1.5755 1.5439 0.8307 -0.1007 0.0619 -0.0371 199 SER A CA 1596 C C . SER A 199 ? 1.5292 1.5357 0.8106 -0.1061 0.0926 -0.0464 199 SER A C 1597 O O . SER A 199 ? 1.5346 1.5468 0.7897 -0.1125 0.1146 -0.0528 199 SER A O 1598 C CB . SER A 199 ? 1.6295 1.5559 0.8379 -0.1102 0.0580 -0.0232 199 SER A CB 1599 O OG . SER A 199 ? 1.6790 1.5928 0.8343 -0.1186 0.0771 -0.0267 199 SER A OG 1600 N N . VAL A 200 ? 1.4987 1.5312 0.8321 -0.1034 0.0937 -0.0470 200 VAL A N 1601 C CA . VAL A 200 ? 1.4706 1.5403 0.8332 -0.1086 0.1183 -0.0557 200 VAL A CA 1602 C C . VAL A 200 ? 1.4681 1.5322 0.8477 -0.1159 0.1222 -0.0486 200 VAL A C 1603 O O . VAL A 200 ? 1.4621 1.5152 0.8629 -0.1095 0.1054 -0.0415 200 VAL A O 1604 C CB . VAL A 200 ? 1.4221 1.5309 0.8315 -0.0982 0.1170 -0.0656 200 VAL A CB 1605 C CG1 . VAL A 200 ? 1.4048 1.5520 0.8342 -0.1040 0.1421 -0.0756 200 VAL A CG1 1606 C CG2 . VAL A 200 ? 1.4230 1.5278 0.8207 -0.0880 0.1038 -0.0701 200 VAL A CG2 1607 N N . GLY A 201 ? 1.4691 1.5407 0.8413 -0.1290 0.1444 -0.0506 201 GLY A N 1608 C CA . GLY A 201 ? 1.4684 1.5310 0.8528 -0.1377 0.1494 -0.0453 201 GLY A CA 1609 C C . GLY A 201 ? 1.4458 1.5410 0.8519 -0.1485 0.1721 -0.0543 201 GLY A C 1610 O O . GLY A 201 ? 1.4571 1.5704 0.8520 -0.1555 0.1890 -0.0597 201 GLY A O 1611 N N . THR A 202 ? 1.4227 1.5256 0.8606 -0.1493 0.1720 -0.0561 202 THR A N 1612 C CA . THR A 202 ? 1.4128 1.5376 0.8672 -0.1627 0.1901 -0.0630 202 THR A CA 1613 C C . THR A 202 ? 1.4562 1.5494 0.9078 -0.1703 0.1886 -0.0563 202 THR A C 1614 O O . THR A 202 ? 1.4808 1.5357 0.9116 -0.1670 0.1768 -0.0449 202 THR A O 1615 C CB . THR A 202 ? 1.3468 1.5141 0.8429 -0.1562 0.1919 -0.0747 202 THR A CB 1616 O OG1 . THR A 202 ? 1.3088 1.4684 0.8276 -0.1459 0.1793 -0.0737 202 THR A OG1 1617 C CG2 . THR A 202 ? 1.3232 1.5171 0.8246 -0.1457 0.1903 -0.0802 202 THR A CG2 1618 N N . SER A 203 ? 1.4627 1.5700 0.9342 -0.1804 0.1993 -0.0631 203 SER A N 1619 C CA . SER A 203 ? 1.4897 1.5666 0.9624 -0.1858 0.1977 -0.0594 203 SER A CA 1620 C C . SER A 203 ? 1.4726 1.5366 0.9639 -0.1676 0.1816 -0.0572 203 SER A C 1621 O O . SER A 203 ? 1.5114 1.5377 0.9938 -0.1651 0.1738 -0.0478 203 SER A O 1622 C CB . SER A 203 ? 1.4799 1.5763 0.9709 -0.2000 0.2108 -0.0698 203 SER A CB 1623 O OG . SER A 203 ? 1.4351 1.5727 0.9559 -0.1926 0.2110 -0.0813 203 SER A OG 1624 N N . THR A 204 ? 1.4348 1.5306 0.9535 -0.1548 0.1771 -0.0647 204 THR A N 1625 C CA . THR A 204 ? 1.4245 1.5139 0.9657 -0.1373 0.1638 -0.0621 204 THR A CA 1626 C C . THR A 204 ? 1.4389 1.5225 0.9747 -0.1242 0.1472 -0.0535 204 THR A C 1627 O O . THR A 204 ? 1.5179 1.5736 1.0535 -0.1156 0.1335 -0.0429 204 THR A O 1628 C CB . THR A 204 ? 1.3632 1.4885 0.9379 -0.1309 0.1679 -0.0738 204 THR A CB 1629 O OG1 . THR A 204 ? 1.3225 1.4834 0.9042 -0.1274 0.1678 -0.0786 204 THR A OG1 1630 C CG2 . THR A 204 ? 1.3522 1.4830 0.9294 -0.1451 0.1821 -0.0836 204 THR A CG2 1631 N N . LEU A 205 ? 1.4026 1.5116 0.9346 -0.1230 0.1479 -0.0579 205 LEU A N 1632 C CA . LEU A 205 ? 1.3772 1.4836 0.9065 -0.1106 0.1311 -0.0525 205 LEU A CA 1633 C C . LEU A 205 ? 1.4150 1.4816 0.9067 -0.1127 0.1197 -0.0401 205 LEU A C 1634 O O . LEU A 205 ? 1.4213 1.4706 0.8802 -0.1257 0.1295 -0.0374 205 LEU A O 1635 C CB . LEU A 205 ? 1.3537 1.4939 0.8854 -0.1091 0.1362 -0.0617 205 LEU A CB 1636 C CG . LEU A 205 ? 1.3494 1.4939 0.8876 -0.0954 0.1191 -0.0598 205 LEU A CG 1637 C CD1 . LEU A 205 ? 1.3051 1.4611 0.8840 -0.0827 0.1086 -0.0581 205 LEU A CD1 1638 C CD2 . LEU A 205 ? 1.3270 1.4999 0.8627 -0.0952 0.1271 -0.0694 205 LEU A CD2 1639 N N . ASN A 206 ? 1.4038 1.4564 0.9010 -0.1004 0.0985 -0.0317 206 ASN A N 1640 C CA . ASN A 206 ? 1.4372 1.4521 0.8991 -0.1007 0.0824 -0.0190 206 ASN A CA 1641 C C . ASN A 206 ? 1.4138 1.4309 0.8831 -0.0884 0.0600 -0.0160 206 ASN A C 1642 O O . ASN A 206 ? 1.3982 1.4052 0.8903 -0.0784 0.0413 -0.0067 206 ASN A O 1643 C CB . ASN A 206 ? 1.4689 1.4502 0.9318 -0.1006 0.0754 -0.0067 206 ASN A CB 1644 C CG . ASN A 206 ? 1.5343 1.4759 0.9626 -0.1000 0.0550 0.0086 206 ASN A CG 1645 O OD1 . ASN A 206 ? 1.5758 1.5013 0.9583 -0.1094 0.0578 0.0105 206 ASN A OD1 1646 N ND2 . ASN A 206 ? 1.5523 1.4784 1.0026 -0.0888 0.0344 0.0200 206 ASN A ND2 1647 N N . GLN A 207 ? 1.4027 1.4322 0.8535 -0.0893 0.0620 -0.0237 207 GLN A N 1648 C CA . GLN A 207 ? 1.3973 1.4335 0.8580 -0.0788 0.0431 -0.0244 207 GLN A CA 1649 C C . GLN A 207 ? 1.4586 1.4623 0.8694 -0.0810 0.0279 -0.0194 207 GLN A C 1650 O O . GLN A 207 ? 1.4782 1.4650 0.8440 -0.0908 0.0397 -0.0201 207 GLN A O 1651 C CB . GLN A 207 ? 1.3569 1.4328 0.8381 -0.0763 0.0567 -0.0388 207 GLN A CB 1652 C CG . GLN A 207 ? 1.3452 1.4306 0.8405 -0.0661 0.0397 -0.0412 207 GLN A CG 1653 C CD . GLN A 207 ? 1.3188 1.4411 0.8321 -0.0639 0.0546 -0.0546 207 GLN A CD 1654 O OE1 . GLN A 207 ? 1.3544 1.4770 0.8421 -0.0647 0.0590 -0.0621 207 GLN A OE1 1655 N NE2 . GLN A 207 ? 1.2786 1.4312 0.8347 -0.0606 0.0632 -0.0575 207 GLN A NE2 1656 N N . ARG A 208 ? 1.4804 1.4750 0.8990 -0.0725 0.0016 -0.0141 208 ARG A N 1657 C CA . ARG A 208 ? 1.5507 1.5162 0.9216 -0.0739 -0.0155 -0.0122 208 ARG A CA 1658 C C . ARG A 208 ? 1.5416 1.5172 0.9356 -0.0645 -0.0368 -0.0151 208 ARG A C 1659 O O . ARG A 208 ? 1.5294 1.5025 0.9560 -0.0581 -0.0597 -0.0049 208 ARG A O 1660 C CB . ARG A 208 ? 1.6186 1.5414 0.9578 -0.0774 -0.0345 0.0042 208 ARG A CB 1661 C CG . ARG A 208 ? 1.6930 1.5807 0.9672 -0.0822 -0.0470 0.0052 208 ARG A CG 1662 C CD . ARG A 208 ? 1.7536 1.6003 1.0044 -0.0831 -0.0759 0.0235 208 ARG A CD 1663 N NE . ARG A 208 ? 1.8229 1.6316 1.0004 -0.0900 -0.0842 0.0247 208 ARG A NE 1664 C CZ . ARG A 208 ? 1.8660 1.6546 0.9902 -0.1002 -0.0643 0.0253 208 ARG A CZ 1665 N NH1 . ARG A 208 ? 1.8471 1.6502 0.9846 -0.1060 -0.0361 0.0248 208 ARG A NH1 1666 N NH2 . ARG A 208 ? 1.9396 1.6922 0.9948 -0.1054 -0.0726 0.0265 208 ARG A NH2 1667 N N . LEU A 209 ? 1.5495 1.5364 0.9287 -0.0638 -0.0288 -0.0285 209 LEU A N 1668 C CA . LEU A 209 ? 1.5466 1.5426 0.9467 -0.0560 -0.0468 -0.0328 209 LEU A CA 1669 C C . LEU A 209 ? 1.6067 1.5636 0.9567 -0.0576 -0.0709 -0.0312 209 LEU A C 1670 O O . LEU A 209 ? 1.6405 1.5721 0.9321 -0.0640 -0.0626 -0.0345 209 LEU A O 1671 C CB . LEU A 209 ? 1.5265 1.5551 0.9402 -0.0531 -0.0252 -0.0487 209 LEU A CB 1672 C CG . LEU A 209 ? 1.4811 1.5491 0.9370 -0.0528 -0.0001 -0.0526 209 LEU A CG 1673 C CD1 . LEU A 209 ? 1.4608 1.5566 0.9208 -0.0507 0.0193 -0.0674 209 LEU A CD1 1674 C CD2 . LEU A 209 ? 1.4383 1.5254 0.9521 -0.0461 -0.0109 -0.0448 209 LEU A CD2 1675 N N . VAL A 210 ? 1.6198 1.5713 0.9922 -0.0525 -0.1008 -0.0258 210 VAL A N 1676 C CA . VAL A 210 ? 1.6882 1.6032 1.0157 -0.0543 -0.1275 -0.0262 210 VAL A CA 1677 C C . VAL A 210 ? 1.6739 1.6033 1.0278 -0.0484 -0.1385 -0.0353 210 VAL A C 1678 O O . VAL A 210 ? 1.6146 1.5736 1.0313 -0.0429 -0.1434 -0.0311 210 VAL A O 1679 C CB . VAL A 210 ? 1.7109 1.5959 1.0331 -0.0563 -0.1616 -0.0080 210 VAL A CB 1680 C CG1 . VAL A 210 ? 1.7404 1.6010 1.0216 -0.0630 -0.1527 0.0008 210 VAL A CG1 1681 C CG2 . VAL A 210 ? 1.6655 1.5761 1.0631 -0.0496 -0.1762 0.0041 210 VAL A CG2 1682 N N . PRO A 211 ? 1.7113 1.6186 1.0167 -0.0494 -0.1409 -0.0480 211 PRO A N 1683 C CA . PRO A 211 ? 1.6937 1.6096 1.0225 -0.0441 -0.1530 -0.0566 211 PRO A CA 1684 C C . PRO A 211 ? 1.6915 1.5935 1.0446 -0.0445 -0.1938 -0.0445 211 PRO A C 1685 O O . PRO A 211 ? 1.7177 1.5881 1.0418 -0.0495 -0.2174 -0.0336 211 PRO A O 1686 C CB . PRO A 211 ? 1.7504 1.6372 1.0120 -0.0453 -0.1462 -0.0729 211 PRO A CB 1687 C CG . PRO A 211 ? 1.7771 1.6522 0.9894 -0.0504 -0.1214 -0.0739 211 PRO A CG 1688 C CD . PRO A 211 ? 1.7665 1.6401 0.9945 -0.0549 -0.1303 -0.0555 211 PRO A CD 1689 N N . ARG A 212 ? 1.6389 1.5651 1.0461 -0.0397 -0.2022 -0.0453 212 ARG A N 1690 C CA . ARG A 212 ? 1.6466 1.5672 1.0894 -0.0404 -0.2393 -0.0330 212 ARG A CA 1691 C C . ARG A 212 ? 1.6716 1.5758 1.1029 -0.0407 -0.2580 -0.0436 212 ARG A C 1692 O O . ARG A 212 ? 1.6189 1.5457 1.0752 -0.0358 -0.2427 -0.0536 212 ARG A O 1693 C CB . ARG A 212 ? 1.5742 1.5389 1.0989 -0.0351 -0.2337 -0.0213 212 ARG A CB 1694 C CG . ARG A 212 ? 1.5584 1.5323 1.0974 -0.0346 -0.2230 -0.0089 212 ARG A CG 1695 C CD . ARG A 212 ? 1.4891 1.5064 1.1040 -0.0282 -0.2114 -0.0008 212 ARG A CD 1696 N NE . ARG A 212 ? 1.4598 1.5074 1.0859 -0.0247 -0.1780 -0.0137 212 ARG A NE 1697 C CZ . ARG A 212 ? 1.4182 1.5035 1.1024 -0.0191 -0.1664 -0.0117 212 ARG A CZ 1698 N NH1 . ARG A 212 ? 1.4152 1.5144 1.1548 -0.0160 -0.1830 0.0027 212 ARG A NH1 1699 N NH2 . ARG A 212 ? 1.3780 1.4879 1.0653 -0.0167 -0.1380 -0.0234 212 ARG A NH2 1700 N N . ILE A 213 ? 1.7440 1.6065 1.1354 -0.0468 -0.2922 -0.0412 213 ILE A N 1701 C CA . ILE A 213 ? 1.7846 1.6233 1.1596 -0.0488 -0.3152 -0.0514 213 ILE A CA 1702 C C . ILE A 213 ? 1.7582 1.6172 1.2070 -0.0492 -0.3428 -0.0383 213 ILE A C 1703 O O . ILE A 213 ? 1.7468 1.6126 1.2308 -0.0516 -0.3635 -0.0197 213 ILE A O 1704 C CB . ILE A 213 ? 1.8616 1.6428 1.1560 -0.0564 -0.3420 -0.0554 213 ILE A CB 1705 C CG1 . ILE A 213 ? 1.9007 1.6602 1.1183 -0.0556 -0.3113 -0.0710 213 ILE A CG1 1706 C CG2 . ILE A 213 ? 1.8895 1.6437 1.1749 -0.0599 -0.3737 -0.0634 213 ILE A CG2 1707 C CD1 . ILE A 213 ? 1.8954 1.6645 1.1011 -0.0564 -0.2887 -0.0617 213 ILE A CD1 1708 N N . ALA A 214 ? 1.7391 1.6084 1.2131 -0.0467 -0.3418 -0.0475 214 ALA A N 1709 C CA . ALA A 214 ? 1.7093 1.5959 1.2511 -0.0484 -0.3673 -0.0360 214 ALA A CA 1710 C C . ALA A 214 ? 1.7114 1.5902 1.2528 -0.0475 -0.3695 -0.0504 214 ALA A C 1711 O O . ALA A 214 ? 1.6896 1.5681 1.2017 -0.0416 -0.3411 -0.0674 214 ALA A O 1712 C CB . ALA A 214 ? 1.6423 1.5818 1.2624 -0.0426 -0.3485 -0.0215 214 ALA A CB 1713 N N . THR A 215 ? 1.7143 1.5866 1.2908 -0.0533 -0.4038 -0.0428 215 THR A N 1714 C CA . THR A 215 ? 1.7213 1.5835 1.3034 -0.0536 -0.4104 -0.0542 215 THR A CA 1715 C C . THR A 215 ? 1.6457 1.5581 1.2987 -0.0463 -0.3848 -0.0491 215 THR A C 1716 O O . THR A 215 ? 1.6061 1.5510 1.3290 -0.0477 -0.3930 -0.0307 215 THR A O 1717 C CB . THR A 215 ? 1.7593 1.5945 1.3539 -0.0647 -0.4592 -0.0469 215 THR A CB 1718 O OG1 . THR A 215 ? 1.8113 1.6020 1.3413 -0.0720 -0.4852 -0.0484 215 THR A OG1 1719 C CG2 . THR A 215 ? 1.7765 1.5900 1.3639 -0.0660 -0.4676 -0.0615 215 THR A CG2 1720 N N . ARG A 216 ? 1.6310 1.5498 1.2652 -0.0382 -0.3533 -0.0650 216 ARG A N 1721 C CA . ARG A 216 ? 1.5663 1.5311 1.2586 -0.0308 -0.3268 -0.0612 216 ARG A CA 1722 C C . ARG A 216 ? 1.5710 1.5260 1.2758 -0.0299 -0.3340 -0.0693 216 ARG A C 1723 O O . ARG A 216 ? 1.6060 1.5176 1.2600 -0.0318 -0.3474 -0.0847 216 ARG A O 1724 C CB . ARG A 216 ? 1.5433 1.5287 1.2129 -0.0220 -0.2847 -0.0710 216 ARG A CB 1725 C CG . ARG A 216 ? 1.5027 1.5229 1.1996 -0.0204 -0.2667 -0.0581 216 ARG A CG 1726 C CD . ARG A 216 ? 1.5362 1.5327 1.1821 -0.0241 -0.2695 -0.0584 216 ARG A CD 1727 N NE . ARG A 216 ? 1.5872 1.5582 1.1630 -0.0221 -0.2520 -0.0772 216 ARG A NE 1728 C CZ . ARG A 216 ? 1.6151 1.5692 1.1406 -0.0242 -0.2435 -0.0797 216 ARG A CZ 1729 N NH1 . ARG A 216 ? 1.6074 1.5657 1.1435 -0.0281 -0.2513 -0.0649 216 ARG A NH1 1730 N NH2 . ARG A 216 ? 1.6474 1.5800 1.1123 -0.0221 -0.2257 -0.0967 216 ARG A NH2 1731 N N . SER A 217 ? 1.5300 1.5235 1.3006 -0.0269 -0.3245 -0.0587 217 SER A N 1732 C CA . SER A 217 ? 1.5377 1.5282 1.3231 -0.0238 -0.3225 -0.0657 217 SER A CA 1733 C C . SER A 217 ? 1.5252 1.5178 1.2728 -0.0127 -0.2883 -0.0839 217 SER A C 1734 O O . SER A 217 ? 1.5019 1.5166 1.2379 -0.0078 -0.2615 -0.0852 217 SER A O 1735 C CB . SER A 217 ? 1.4910 1.5251 1.3562 -0.0235 -0.3183 -0.0472 217 SER A CB 1736 O OG . SER A 217 ? 1.5002 1.5419 1.4083 -0.0325 -0.3444 -0.0281 217 SER A OG 1737 N N . LYS A 218 ? 1.5471 1.5159 1.2770 -0.0089 -0.2896 -0.0976 218 LYS A N 1738 C CA . LYS A 218 ? 1.5380 1.5113 1.2400 0.0030 -0.2575 -0.1139 218 LYS A CA 1739 C C . LYS A 218 ? 1.4755 1.5017 1.2325 0.0100 -0.2311 -0.1039 218 LYS A C 1740 O O . LYS A 218 ? 1.4612 1.5067 1.2729 0.0078 -0.2399 -0.0899 218 LYS A O 1741 C CB . LYS A 218 ? 1.5800 1.5116 1.2508 0.0067 -0.2664 -0.1312 218 LYS A CB 1742 C CG . LYS A 218 ? 1.6478 1.5237 1.2440 0.0031 -0.2819 -0.1480 218 LYS A CG 1743 C CD . LYS A 218 ? 1.6921 1.5275 1.2524 0.0101 -0.2822 -0.1685 218 LYS A CD 1744 C CE . LYS A 218 ? 1.7676 1.5486 1.2436 0.0089 -0.2890 -0.1879 218 LYS A CE 1745 N NZ . LYS A 218 ? 1.8217 1.5613 1.2772 -0.0057 -0.3320 -0.1847 218 LYS A NZ 1746 N N . VAL A 219 ? 1.4416 1.4909 1.1829 0.0176 -0.1992 -0.1103 219 VAL A N 1747 C CA . VAL A 219 ? 1.3773 1.4730 1.1600 0.0249 -0.1733 -0.1042 219 VAL A CA 1748 C C . VAL A 219 ? 1.3772 1.4714 1.1269 0.0356 -0.1479 -0.1217 219 VAL A C 1749 O O . VAL A 219 ? 1.3985 1.4838 1.1041 0.0365 -0.1346 -0.1322 219 VAL A O 1750 C CB . VAL A 219 ? 1.3544 1.4879 1.1597 0.0220 -0.1593 -0.0915 219 VAL A CB 1751 C CG1 . VAL A 219 ? 1.3028 1.4814 1.1429 0.0290 -0.1327 -0.0870 219 VAL A CG1 1752 C CG2 . VAL A 219 ? 1.3533 1.4899 1.1952 0.0131 -0.1828 -0.0737 219 VAL A CG2 1753 N N . ASN A 220 ? 1.3609 1.4640 1.1334 0.0438 -0.1410 -0.1238 220 ASN A N 1754 C CA . ASN A 220 ? 1.3800 1.4762 1.1245 0.0555 -0.1208 -0.1410 220 ASN A CA 1755 C C . ASN A 220 ? 1.4148 1.4587 1.0967 0.0562 -0.1290 -0.1597 220 ASN A C 1756 O O . ASN A 220 ? 1.4347 1.4736 1.0789 0.0634 -0.1075 -0.1742 220 ASN A O 1757 C CB . ASN A 220 ? 1.3706 1.5067 1.1157 0.0603 -0.0892 -0.1421 220 ASN A CB 1758 C CG . ASN A 220 ? 1.3340 1.5188 1.1341 0.0615 -0.0790 -0.1267 220 ASN A CG 1759 O OD1 . ASN A 220 ? 1.3068 1.5011 1.1439 0.0556 -0.0937 -0.1114 220 ASN A OD1 1760 N ND2 . ASN A 220 ? 1.3298 1.5458 1.1349 0.0688 -0.0535 -0.1304 220 ASN A ND2 1761 N N . GLY A 221 ? 1.4177 1.4227 1.0885 0.0481 -0.1600 -0.1591 221 GLY A N 1762 C CA . GLY A 221 ? 1.4688 1.4184 1.0770 0.0478 -0.1719 -0.1771 221 GLY A CA 1763 C C . GLY A 221 ? 1.4850 1.4189 1.0404 0.0419 -0.1694 -0.1821 221 GLY A C 1764 O O . GLY A 221 ? 1.5372 1.4269 1.0317 0.0431 -0.1723 -0.1988 221 GLY A O 1765 N N . GLN A 222 ? 1.4424 1.4095 1.0181 0.0356 -0.1640 -0.1679 222 GLN A N 1766 C CA . GLN A 222 ? 1.4820 1.4354 1.0106 0.0296 -0.1616 -0.1700 222 GLN A CA 1767 C C . GLN A 222 ? 1.4723 1.4299 1.0228 0.0174 -0.1864 -0.1520 222 GLN A C 1768 O O . GLN A 222 ? 1.4316 1.4267 1.0415 0.0157 -0.1874 -0.1358 222 GLN A O 1769 C CB . GLN A 222 ? 1.4627 1.4514 0.9873 0.0350 -0.1248 -0.1721 222 GLN A CB 1770 C CG . GLN A 222 ? 1.4820 1.4752 0.9938 0.0481 -0.0973 -0.1880 222 GLN A CG 1771 C CD . GLN A 222 ? 1.5720 1.5126 1.0192 0.0523 -0.0999 -0.2078 222 GLN A CD 1772 O OE1 . GLN A 222 ? 1.5963 1.4997 0.9915 0.0448 -0.1130 -0.2117 222 GLN A OE1 1773 N NE2 . GLN A 222 ? 1.6046 1.5402 1.0533 0.0648 -0.0873 -0.2205 222 GLN A NE2 1774 N N . ASN A 223 ? 1.5255 1.4440 1.0270 0.0096 -0.2061 -0.1546 223 ASN A N 1775 C CA . ASN A 223 ? 1.5296 1.4488 1.0475 -0.0012 -0.2309 -0.1376 223 ASN A CA 1776 C C . ASN A 223 ? 1.5135 1.4532 1.0209 -0.0028 -0.2120 -0.1310 223 ASN A C 1777 O O . ASN A 223 ? 1.4797 1.4393 1.0225 -0.0081 -0.2214 -0.1139 223 ASN A O 1778 C CB . ASN A 223 ? 1.6108 1.4751 1.0809 -0.0097 -0.2662 -0.1424 223 ASN A CB 1779 C CG . ASN A 223 ? 1.6365 1.4785 1.1239 -0.0116 -0.2924 -0.1455 223 ASN A CG 1780 O OD1 . ASN A 223 ? 1.6288 1.4957 1.1810 -0.0146 -0.3055 -0.1308 223 ASN A OD1 1781 N ND2 . ASN A 223 ? 1.6883 1.4810 1.1165 -0.0103 -0.3002 -0.1648 223 ASN A ND2 1782 N N . GLY A 224 ? 1.5406 1.4744 1.0002 0.0018 -0.1849 -0.1442 224 GLY A N 1783 C CA . GLY A 224 ? 1.5193 1.4719 0.9674 0.0000 -0.1634 -0.1391 224 GLY A CA 1784 C C . GLY A 224 ? 1.4369 1.4441 0.9472 0.0030 -0.1429 -0.1284 224 GLY A C 1785 O O . GLY A 224 ? 1.4013 1.4335 0.9554 0.0087 -0.1375 -0.1281 224 GLY A O 1786 N N . ARG A 225 ? 1.4202 1.4435 0.9318 -0.0009 -0.1318 -0.1197 225 ARG A N 1787 C CA . ARG A 225 ? 1.3713 1.4426 0.9353 0.0010 -0.1123 -0.1104 225 ARG A CA 1788 C C . ARG A 225 ? 1.3655 1.4500 0.9056 0.0000 -0.0828 -0.1142 225 ARG A C 1789 O O . ARG A 225 ? 1.4239 1.4815 0.9148 -0.0049 -0.0827 -0.1164 225 ARG A O 1790 C CB . ARG A 225 ? 1.3407 1.4223 0.9470 -0.0037 -0.1316 -0.0920 225 ARG A CB 1791 C CG . ARG A 225 ? 1.3341 1.4128 0.9791 -0.0038 -0.1589 -0.0847 225 ARG A CG 1792 C CD . ARG A 225 ? 1.2819 1.3979 0.9797 0.0022 -0.1459 -0.0826 225 ARG A CD 1793 N NE . ARG A 225 ? 1.2796 1.3928 1.0168 0.0006 -0.1717 -0.0734 225 ARG A NE 1794 C CZ . ARG A 225 ? 1.3034 1.3914 1.0300 0.0008 -0.1886 -0.0807 225 ARG A CZ 1795 N NH1 . ARG A 225 ? 1.3321 1.3942 1.0080 0.0042 -0.1814 -0.0985 225 ARG A NH1 1796 N NH2 . ARG A 225 ? 1.3015 1.3895 1.0694 -0.0025 -0.2124 -0.0700 225 ARG A NH2 1797 N N . MET A 226 ? 1.3129 1.4382 0.8877 0.0039 -0.0587 -0.1143 226 MET A N 1798 C CA . MET A 226 ? 1.3094 1.4529 0.8724 0.0014 -0.0316 -0.1163 226 MET A CA 1799 C C . MET A 226 ? 1.2618 1.4363 0.8701 -0.0011 -0.0276 -0.1036 226 MET A C 1800 O O . MET A 226 ? 1.2393 1.4393 0.8942 0.0029 -0.0299 -0.0985 226 MET A O 1801 C CB . MET A 226 ? 1.3159 1.4814 0.8794 0.0078 -0.0060 -0.1285 226 MET A CB 1802 C CG . MET A 226 ? 1.3752 1.5107 0.8920 0.0121 -0.0037 -0.1430 226 MET A CG 1803 S SD . MET A 226 ? 1.4396 1.5524 0.8917 0.0062 0.0148 -0.1496 226 MET A SD 1804 C CE . MET A 226 ? 1.4892 1.5757 0.9001 0.0156 0.0219 -0.1683 226 MET A CE 1805 N N . GLU A 227 ? 1.2590 1.4293 0.8516 -0.0075 -0.0210 -0.0986 227 GLU A N 1806 C CA . GLU A 227 ? 1.2224 1.4168 0.8519 -0.0097 -0.0155 -0.0882 227 GLU A CA 1807 C C . GLU A 227 ? 1.2050 1.4169 0.8231 -0.0138 0.0122 -0.0932 227 GLU A C 1808 O O . GLU A 227 ? 1.2318 1.4236 0.8097 -0.0198 0.0185 -0.0950 227 GLU A O 1809 C CB . GLU A 227 ? 1.2532 1.4235 0.8793 -0.0136 -0.0363 -0.0759 227 GLU A CB 1810 C CG . GLU A 227 ? 1.2418 1.4337 0.9116 -0.0133 -0.0337 -0.0645 227 GLU A CG 1811 C CD . GLU A 227 ? 1.2700 1.4399 0.9462 -0.0147 -0.0575 -0.0509 227 GLU A CD 1812 O OE1 . GLU A 227 ? 1.2904 1.4267 0.9316 -0.0176 -0.0767 -0.0501 227 GLU A OE1 1813 O OE2 . GLU A 227 ? 1.2649 1.4508 0.9812 -0.0124 -0.0572 -0.0409 227 GLU A OE2 1814 N N . PHE A 228 ? 1.1490 1.3978 0.8015 -0.0115 0.0281 -0.0948 228 PHE A N 1815 C CA . PHE A 228 ? 1.1224 1.3913 0.7678 -0.0162 0.0534 -0.1006 228 PHE A CA 1816 C C . PHE A 228 ? 1.0907 1.3698 0.7527 -0.0218 0.0600 -0.0936 228 PHE A C 1817 O O . PHE A 228 ? 1.0586 1.3491 0.7550 -0.0187 0.0529 -0.0863 228 PHE A O 1818 C CB . PHE A 228 ? 1.0909 1.3929 0.7590 -0.0108 0.0665 -0.1080 228 PHE A CB 1819 C CG . PHE A 228 ? 1.1128 1.4036 0.7624 -0.0044 0.0643 -0.1169 228 PHE A CG 1820 C CD1 . PHE A 228 ? 1.1405 1.4250 0.7559 -0.0060 0.0803 -0.1263 228 PHE A CD1 1821 C CD2 . PHE A 228 ? 1.1158 1.4007 0.7820 0.0033 0.0472 -0.1158 228 PHE A CD2 1822 C CE1 . PHE A 228 ? 1.1641 1.4356 0.7604 0.0014 0.0802 -0.1356 228 PHE A CE1 1823 C CE2 . PHE A 228 ? 1.1426 1.4127 0.7897 0.0096 0.0451 -0.1252 228 PHE A CE2 1824 C CZ . PHE A 228 ? 1.1665 1.4292 0.7776 0.0094 0.0621 -0.1357 228 PHE A CZ 1825 N N . PHE A 229 ? 1.0926 1.3662 0.7291 -0.0302 0.0744 -0.0958 229 PHE A N 1826 C CA . PHE A 229 ? 1.0835 1.3604 0.7288 -0.0367 0.0816 -0.0906 229 PHE A CA 1827 C C . PHE A 229 ? 1.0749 1.3774 0.7217 -0.0436 0.1046 -0.0978 229 PHE A C 1828 O O . PHE A 229 ? 1.0686 1.3842 0.7065 -0.0436 0.1153 -0.1056 229 PHE A O 1829 C CB . PHE A 229 ? 1.1201 1.3600 0.7325 -0.0425 0.0742 -0.0841 229 PHE A CB 1830 C CG . PHE A 229 ? 1.1422 1.3579 0.7575 -0.0369 0.0489 -0.0751 229 PHE A CG 1831 C CD1 . PHE A 229 ? 1.1772 1.3733 0.7701 -0.0337 0.0341 -0.0770 229 PHE A CD1 1832 C CD2 . PHE A 229 ? 1.1361 1.3486 0.7779 -0.0348 0.0395 -0.0648 229 PHE A CD2 1833 C CE1 . PHE A 229 ? 1.1921 1.3665 0.7896 -0.0301 0.0080 -0.0681 229 PHE A CE1 1834 C CE2 . PHE A 229 ? 1.1529 1.3466 0.8034 -0.0299 0.0152 -0.0551 229 PHE A CE2 1835 C CZ . PHE A 229 ? 1.1773 1.3524 0.8060 -0.0283 -0.0018 -0.0565 229 PHE A CZ 1836 N N . TRP A 230 ? 1.0765 1.3858 0.7357 -0.0493 0.1118 -0.0952 230 TRP A N 1837 C CA . TRP A 230 ? 1.0608 1.3945 0.7243 -0.0576 0.1309 -0.1015 230 TRP A CA 1838 C C . TRP A 230 ? 1.0677 1.3905 0.7266 -0.0673 0.1373 -0.0988 230 TRP A C 1839 O O . TRP A 230 ? 1.0725 1.3736 0.7331 -0.0651 0.1278 -0.0916 230 TRP A O 1840 C CB . TRP A 230 ? 1.0236 1.3939 0.7218 -0.0522 0.1336 -0.1051 230 TRP A CB 1841 C CG . TRP A 230 ? 1.0059 1.3800 0.7308 -0.0468 0.1259 -0.0996 230 TRP A CG 1842 C CD1 . TRP A 230 ? 0.9971 1.3686 0.7407 -0.0363 0.1117 -0.0937 230 TRP A CD1 1843 C CD2 . TRP A 230 ? 0.9962 1.3773 0.7324 -0.0516 0.1333 -0.0995 230 TRP A CD2 1844 N NE1 . TRP A 230 ? 0.9622 1.3406 0.7292 -0.0338 0.1116 -0.0892 230 TRP A NE1 1845 C CE2 . TRP A 230 ? 0.9813 1.3643 0.7422 -0.0425 0.1249 -0.0935 230 TRP A CE2 1846 C CE3 . TRP A 230 ? 1.0058 1.3905 0.7332 -0.0633 0.1463 -0.1043 230 TRP A CE3 1847 C CZ2 . TRP A 230 ? 0.9949 1.3823 0.7689 -0.0434 0.1310 -0.0929 230 TRP A CZ2 1848 C CZ3 . TRP A 230 ? 1.0011 1.3880 0.7405 -0.0650 0.1500 -0.1044 230 TRP A CZ3 1849 C CH2 . TRP A 230 ? 0.9909 1.3786 0.7518 -0.0544 0.1432 -0.0991 230 TRP A CH2 1850 N N . THR A 231 ? 1.0744 1.4122 0.7289 -0.0782 0.1534 -0.1043 231 THR A N 1851 C CA . THR A 231 ? 1.0771 1.4072 0.7300 -0.0888 0.1607 -0.1036 231 THR A CA 1852 C C . THR A 231 ? 1.0666 1.4275 0.7296 -0.0991 0.1754 -0.1113 231 THR A C 1853 O O . THR A 231 ? 1.0477 1.4334 0.7153 -0.0989 0.1817 -0.1158 231 THR A O 1854 C CB . THR A 231 ? 1.1093 1.4028 0.7291 -0.0970 0.1615 -0.0981 231 THR A CB 1855 O OG1 . THR A 231 ? 1.1070 1.3877 0.7280 -0.1052 0.1658 -0.0966 231 THR A OG1 1856 C CG2 . THR A 231 ? 1.1222 1.4197 0.7187 -0.1064 0.1745 -0.1013 231 THR A CG2 1857 N N . ILE A 232 ? 1.0796 1.4383 0.7474 -0.1077 0.1802 -0.1127 232 ILE A N 1858 C CA . ILE A 232 ? 1.0744 1.4563 0.7478 -0.1213 0.1922 -0.1193 232 ILE A CA 1859 C C . ILE A 232 ? 1.1086 1.4668 0.7573 -0.1361 0.2006 -0.1171 232 ILE A C 1860 O O . ILE A 232 ? 1.1282 1.4550 0.7651 -0.1397 0.1983 -0.1135 232 ILE A O 1861 C CB . ILE A 232 ? 1.0557 1.4484 0.7465 -0.1231 0.1917 -0.1236 232 ILE A CB 1862 C CG1 . ILE A 232 ? 1.0179 1.4484 0.7332 -0.1150 0.1890 -0.1271 232 ILE A CG1 1863 C CG2 . ILE A 232 ? 1.0785 1.4726 0.7635 -0.1417 0.2013 -0.1287 232 ILE A CG2 1864 C CD1 . ILE A 232 ? 1.0126 1.4433 0.7373 -0.0977 0.1790 -0.1223 232 ILE A CD1 1865 N N . LEU A 233 ? 1.1506 1.5236 0.7927 -0.1442 0.2111 -0.1186 233 LEU A N 1866 C CA . LEU A 233 ? 1.1888 1.5434 0.8086 -0.1600 0.2216 -0.1156 233 LEU A CA 1867 C C . LEU A 233 ? 1.1866 1.5597 0.8208 -0.1767 0.2297 -0.1208 233 LEU A C 1868 O O . LEU A 233 ? 1.1546 1.5665 0.8101 -0.1802 0.2350 -0.1260 233 LEU A O 1869 C CB . LEU A 233 ? 1.2114 1.5739 0.8173 -0.1604 0.2312 -0.1144 233 LEU A CB 1870 C CG . LEU A 233 ? 1.2616 1.6029 0.8394 -0.1757 0.2437 -0.1091 233 LEU A CG 1871 C CD1 . LEU A 233 ? 1.2943 1.5859 0.8408 -0.1744 0.2348 -0.1004 233 LEU A CD1 1872 C CD2 . LEU A 233 ? 1.2696 1.6270 0.8382 -0.1740 0.2564 -0.1098 233 LEU A CD2 1873 N N . LYS A 234 ? 1.2192 1.5633 0.8423 -0.1868 0.2294 -0.1193 234 LYS A N 1874 C CA . LYS A 234 ? 1.2582 1.6127 0.8918 -0.2038 0.2345 -0.1250 234 LYS A CA 1875 C C . LYS A 234 ? 1.2775 1.6497 0.9113 -0.2223 0.2481 -0.1243 234 LYS A C 1876 O O . LYS A 234 ? 1.2846 1.6548 0.9052 -0.2216 0.2557 -0.1187 234 LYS A O 1877 C CB . LYS A 234 ? 1.3257 1.6379 0.9448 -0.2085 0.2308 -0.1238 234 LYS A CB 1878 C CG . LYS A 234 ? 1.3419 1.6467 0.9703 -0.1924 0.2204 -0.1267 234 LYS A CG 1879 C CD . LYS A 234 ? 1.4104 1.6775 1.0288 -0.1971 0.2194 -0.1280 234 LYS A CD 1880 C CE . LYS A 234 ? 1.4674 1.7417 1.0886 -0.2165 0.2249 -0.1371 234 LYS A CE 1881 N NZ . LYS A 234 ? 1.5068 1.7502 1.1221 -0.2163 0.2231 -0.1427 234 LYS A NZ 1882 N N . PRO A 235 ? 1.2921 1.6826 0.9412 -0.2392 0.2513 -0.1299 235 PRO A N 1883 C CA . PRO A 235 ? 1.2879 1.6954 0.9413 -0.2587 0.2645 -0.1276 235 PRO A CA 1884 C C . PRO A 235 ? 1.3342 1.7000 0.9580 -0.2698 0.2719 -0.1191 235 PRO A C 1885 O O . PRO A 235 ? 1.3593 1.6837 0.9649 -0.2691 0.2653 -0.1174 235 PRO A O 1886 C CB . PRO A 235 ? 1.2920 1.7183 0.9653 -0.2756 0.2617 -0.1352 235 PRO A CB 1887 C CG . PRO A 235 ? 1.2826 1.6870 0.9504 -0.2668 0.2491 -0.1412 235 PRO A CG 1888 C CD . PRO A 235 ? 1.2653 1.6633 0.9282 -0.2417 0.2432 -0.1384 235 PRO A CD 1889 N N . ASN A 236 ? 1.3564 1.7327 0.9756 -0.2789 0.2863 -0.1131 236 ASN A N 1890 C CA . ASN A 236 ? 1.3901 1.7287 0.9795 -0.2915 0.2952 -0.1032 236 ASN A CA 1891 C C . ASN A 236 ? 1.4070 1.7012 0.9614 -0.2766 0.2888 -0.0958 236 ASN A C 1892 O O . ASN A 236 ? 1.4510 1.7091 0.9770 -0.2858 0.2938 -0.0863 236 ASN A O 1893 C CB . ASN A 236 ? 1.4217 1.7380 1.0107 -0.3128 0.2940 -0.1038 236 ASN A CB 1894 C CG . ASN A 236 ? 1.4524 1.7878 1.0522 -0.3380 0.3091 -0.1001 236 ASN A CG 1895 O OD1 . ASN A 236 ? 1.4863 1.8231 1.0740 -0.3424 0.3237 -0.0913 236 ASN A OD1 1896 N ND2 . ASN A 236 ? 1.4539 1.8031 1.0759 -0.3553 0.3058 -0.1066 236 ASN A ND2 1897 N N . ASP A 237 ? 1.3799 1.6761 0.9368 -0.2546 0.2767 -0.0991 237 ASP A N 1898 C CA . ASP A 237 ? 1.3990 1.6571 0.9265 -0.2403 0.2679 -0.0918 237 ASP A CA 1899 C C . ASP A 237 ? 1.3868 1.6583 0.9020 -0.2308 0.2742 -0.0900 237 ASP A C 1900 O O . ASP A 237 ? 1.3437 1.6567 0.8798 -0.2299 0.2833 -0.0959 237 ASP A O 1901 C CB . ASP A 237 ? 1.3830 1.6325 0.9217 -0.2226 0.2503 -0.0956 237 ASP A CB 1902 C CG . ASP A 237 ? 1.4119 1.6154 0.9243 -0.2122 0.2386 -0.0862 237 ASP A CG 1903 O OD1 . ASP A 237 ? 1.4493 1.6202 0.9323 -0.2213 0.2425 -0.0767 237 ASP A OD1 1904 O OD2 . ASP A 237 ? 1.3962 1.5964 0.9185 -0.1951 0.2248 -0.0873 237 ASP A OD2 1905 N N . ALA A 238 ? 1.4154 1.6502 0.8957 -0.2235 0.2690 -0.0818 238 ALA A N 1906 C CA . ALA A 238 ? 1.4278 1.6659 0.8870 -0.2147 0.2744 -0.0806 238 ALA A CA 1907 C C . ALA A 238 ? 1.4191 1.6328 0.8632 -0.1954 0.2547 -0.0788 238 ALA A C 1908 O O . ALA A 238 ? 1.4576 1.6357 0.8895 -0.1933 0.2407 -0.0719 238 ALA A O 1909 C CB . ALA A 238 ? 1.4662 1.6813 0.8885 -0.2288 0.2898 -0.0711 238 ALA A CB 1910 N N . ILE A 239 ? 1.3870 1.6199 0.8346 -0.1815 0.2532 -0.0847 239 ILE A N 1911 C CA . ILE A 239 ? 1.3885 1.5985 0.8203 -0.1648 0.2343 -0.0829 239 ILE A CA 1912 C C . ILE A 239 ? 1.4447 1.6252 0.8267 -0.1649 0.2381 -0.0776 239 ILE A C 1913 O O . ILE A 239 ? 1.4402 1.6341 0.8093 -0.1708 0.2583 -0.0800 239 ILE A O 1914 C CB . ILE A 239 ? 1.3347 1.5774 0.7985 -0.1492 0.2271 -0.0924 239 ILE A CB 1915 C CG1 . ILE A 239 ? 1.3414 1.5601 0.7994 -0.1341 0.2034 -0.0893 239 ILE A CG1 1916 C CG2 . ILE A 239 ? 1.3311 1.5991 0.7920 -0.1459 0.2423 -0.0993 239 ILE A CG2 1917 C CD1 . ILE A 239 ? 1.2955 1.5432 0.7903 -0.1204 0.1942 -0.0963 239 ILE A CD1 1918 N N . ASN A 240 ? 1.4768 1.6173 0.8310 -0.1583 0.2189 -0.0700 240 ASN A N 1919 C CA . ASN A 240 ? 1.5342 1.6390 0.8339 -0.1593 0.2188 -0.0636 240 ASN A CA 1920 C C . ASN A 240 ? 1.5410 1.6300 0.8261 -0.1434 0.1977 -0.0656 240 ASN A C 1921 O O . ASN A 240 ? 1.5340 1.6074 0.8304 -0.1360 0.1742 -0.0607 240 ASN A O 1922 C CB . ASN A 240 ? 1.5750 1.6377 0.8461 -0.1696 0.2126 -0.0493 240 ASN A CB 1923 C CG . ASN A 240 ? 1.5986 1.6695 0.8790 -0.1875 0.2324 -0.0463 240 ASN A CG 1924 O OD1 . ASN A 240 ? 1.6034 1.6861 0.8697 -0.1981 0.2553 -0.0472 240 ASN A OD1 1925 N ND2 . ASN A 240 ? 1.5962 1.6603 0.9010 -0.1913 0.2243 -0.0426 240 ASN A ND2 1926 N N . PHE A 241 ? 1.5684 1.6601 0.8286 -0.1385 0.2063 -0.0726 241 PHE A N 1927 C CA . PHE A 241 ? 1.5868 1.6603 0.8282 -0.1248 0.1865 -0.0759 241 PHE A CA 1928 C C . PHE A 241 ? 1.6609 1.6885 0.8349 -0.1281 0.1834 -0.0697 241 PHE A C 1929 O O . PHE A 241 ? 1.7005 1.7255 0.8412 -0.1348 0.2067 -0.0714 241 PHE A O 1930 C CB . PHE A 241 ? 1.5643 1.6714 0.8266 -0.1144 0.1962 -0.0902 241 PHE A CB 1931 C CG . PHE A 241 ? 1.5229 1.6708 0.8475 -0.1086 0.1927 -0.0954 241 PHE A CG 1932 C CD1 . PHE A 241 ? 1.5038 1.6490 0.8525 -0.0980 0.1676 -0.0946 241 PHE A CD1 1933 C CD2 . PHE A 241 ? 1.4955 1.6844 0.8544 -0.1144 0.2141 -0.1003 241 PHE A CD2 1934 C CE1 . PHE A 241 ? 1.4616 1.6427 0.8638 -0.0929 0.1656 -0.0986 241 PHE A CE1 1935 C CE2 . PHE A 241 ? 1.4569 1.6811 0.8682 -0.1095 0.2097 -0.1047 241 PHE A CE2 1936 C CZ . PHE A 241 ? 1.4389 1.6584 0.8700 -0.0985 0.1863 -0.1038 241 PHE A CZ 1937 N N . GLU A 242 ? 1.6887 1.6805 0.8432 -0.1235 0.1544 -0.0618 242 GLU A N 1938 C CA . GLU A 242 ? 1.7604 1.7064 0.8484 -0.1243 0.1445 -0.0570 242 GLU A CA 1939 C C . GLU A 242 ? 1.7553 1.6871 0.8415 -0.1115 0.1146 -0.0611 242 GLU A C 1940 O O . GLU A 242 ? 1.7104 1.6478 0.8367 -0.1058 0.0916 -0.0567 242 GLU A O 1941 C CB . GLU A 242 ? 1.8176 1.7257 0.8748 -0.1350 0.1357 -0.0394 242 GLU A CB 1942 C CG . GLU A 242 ? 1.9066 1.7639 0.8902 -0.1368 0.1227 -0.0324 242 GLU A CG 1943 C CD . GLU A 242 ? 1.9478 1.7673 0.9013 -0.1474 0.1138 -0.0132 242 GLU A CD 1944 O OE1 . GLU A 242 ? 1.9499 1.7764 0.9085 -0.1589 0.1360 -0.0075 242 GLU A OE1 1945 O OE2 . GLU A 242 ? 1.9654 1.7471 0.8902 -0.1445 0.0836 -0.0032 242 GLU A OE2 1946 N N . SER A 243 ? 1.7928 1.7060 0.8328 -0.1073 0.1158 -0.0696 243 SER A N 1947 C CA . SER A 243 ? 1.8002 1.6955 0.8324 -0.0968 0.0869 -0.0745 243 SER A CA 1948 C C . SER A 243 ? 1.8834 1.7397 0.8409 -0.0964 0.0875 -0.0806 243 SER A C 1949 O O . SER A 243 ? 1.9521 1.8072 0.8739 -0.1009 0.1171 -0.0853 243 SER A O 1950 C CB . SER A 243 ? 1.7342 1.6701 0.8226 -0.0858 0.0893 -0.0875 243 SER A CB 1951 O OG . SER A 243 ? 1.7315 1.6488 0.8122 -0.0768 0.0622 -0.0924 243 SER A OG 1952 N N . ASN A 244 ? 1.9101 1.7347 0.8448 -0.0912 0.0547 -0.0807 244 ASN A N 1953 C CA . ASN A 244 ? 1.9831 1.7655 0.8431 -0.0900 0.0503 -0.0885 244 ASN A CA 1954 C C . ASN A 244 ? 1.9669 1.7478 0.8367 -0.0786 0.0323 -0.1029 244 ASN A C 1955 O O . ASN A 244 ? 2.0064 1.7450 0.8182 -0.0774 0.0152 -0.1082 244 ASN A O 1956 C CB . ASN A 244 ? 2.0398 1.7704 0.8418 -0.0981 0.0239 -0.0732 244 ASN A CB 1957 C CG . ASN A 244 ? 2.0210 1.7447 0.8592 -0.0959 -0.0185 -0.0616 244 ASN A CG 1958 O OD1 . ASN A 244 ? 1.9474 1.7084 0.8590 -0.0904 -0.0236 -0.0615 244 ASN A OD1 1959 N ND2 . ASN A 244 ? 2.0561 1.7327 0.8434 -0.1003 -0.0490 -0.0508 244 ASN A ND2 1960 N N . GLY A 245 ? 1.8823 1.7073 0.8232 -0.0709 0.0361 -0.1091 245 GLY A N 1961 C CA . GLY A 245 ? 1.8696 1.6973 0.8281 -0.0603 0.0216 -0.1221 245 GLY A CA 1962 C C . GLY A 245 ? 1.8018 1.6713 0.8440 -0.0548 0.0116 -0.1193 245 GLY A C 1963 O O . GLY A 245 ? 1.7828 1.6701 0.8649 -0.0590 0.0060 -0.1059 245 GLY A O 1964 N N . ASN A 246 ? 1.7743 1.6575 0.8409 -0.0450 0.0100 -0.1320 246 ASN A N 1965 C CA . ASN A 246 ? 1.6968 1.6165 0.8384 -0.0389 -0.0006 -0.1301 246 ASN A CA 1966 C C . ASN A 246 ? 1.6217 1.5932 0.8183 -0.0386 0.0268 -0.1283 246 ASN A C 1967 O O . ASN A 246 ? 1.5598 1.5614 0.8163 -0.0356 0.0192 -0.1233 246 ASN A O 1968 C CB . ASN A 246 ? 1.6846 1.5917 0.8488 -0.0420 -0.0379 -0.1152 246 ASN A CB 1969 C CG . ASN A 246 ? 1.7469 1.6031 0.8593 -0.0439 -0.0698 -0.1159 246 ASN A CG 1970 O OD1 . ASN A 246 ? 1.7877 1.6067 0.8347 -0.0498 -0.0708 -0.1148 246 ASN A OD1 1971 N ND2 . ASN A 246 ? 1.7359 1.5897 0.8768 -0.0397 -0.0970 -0.1170 246 ASN A ND2 1972 N N . PHE A 247 ? 1.6365 1.6182 0.8119 -0.0420 0.0589 -0.1327 247 PHE A N 1973 C CA . PHE A 247 ? 1.5605 1.5875 0.7812 -0.0447 0.0838 -0.1302 247 PHE A CA 1974 C C . PHE A 247 ? 1.5199 1.5846 0.7764 -0.0353 0.1028 -0.1426 247 PHE A C 1975 O O . PHE A 247 ? 1.5540 1.6116 0.7818 -0.0298 0.1179 -0.1546 247 PHE A O 1976 C CB . PHE A 247 ? 1.5987 1.6176 0.7809 -0.0552 0.1074 -0.1264 247 PHE A CB 1977 C CG . PHE A 247 ? 1.5523 1.6129 0.7767 -0.0611 0.1307 -0.1229 247 PHE A CG 1978 C CD1 . PHE A 247 ? 1.4941 1.5796 0.7729 -0.0620 0.1207 -0.1156 247 PHE A CD1 1979 C CD2 . PHE A 247 ? 1.5683 1.6420 0.7762 -0.0667 0.1629 -0.1267 247 PHE A CD2 1980 C CE1 . PHE A 247 ? 1.4560 1.5759 0.7685 -0.0685 0.1406 -0.1136 247 PHE A CE1 1981 C CE2 . PHE A 247 ? 1.5226 1.6335 0.7691 -0.0741 0.1820 -0.1234 247 PHE A CE2 1982 C CZ . PHE A 247 ? 1.4723 1.6048 0.7692 -0.0752 0.1700 -0.1174 247 PHE A CZ 1983 N N . ILE A 248 ? 1.4736 1.5772 0.7920 -0.0329 0.1017 -0.1394 248 ILE A N 1984 C CA . ILE A 248 ? 1.4281 1.5725 0.7856 -0.0254 0.1203 -0.1481 248 ILE A CA 1985 C C . ILE A 248 ? 1.3974 1.5748 0.7751 -0.0341 0.1445 -0.1444 248 ILE A C 1986 O O . ILE A 248 ? 1.3547 1.5482 0.7645 -0.0396 0.1391 -0.1356 248 ILE A O 1987 C CB . ILE A 248 ? 1.3852 1.5503 0.7959 -0.0176 0.1023 -0.1465 248 ILE A CB 1988 C CG1 . ILE A 248 ? 1.4126 1.5413 0.8076 -0.0135 0.0715 -0.1454 248 ILE A CG1 1989 C CG2 . ILE A 248 ? 1.3617 1.5606 0.8031 -0.0080 0.1185 -0.1561 248 ILE A CG2 1990 C CD1 . ILE A 248 ? 1.4707 1.5671 0.8187 -0.0075 0.0712 -0.1579 248 ILE A CD1 1991 N N . ALA A 249 ? 1.4170 1.6032 0.7752 -0.0355 0.1716 -0.1511 249 ALA A N 1992 C CA . ALA A 249 ? 1.4187 1.6295 0.7869 -0.0468 0.1945 -0.1468 249 ALA A CA 1993 C C . ALA A 249 ? 1.3621 1.6261 0.7871 -0.0444 0.2089 -0.1501 249 ALA A C 1994 O O . ALA A 249 ? 1.3488 1.6306 0.7940 -0.0325 0.2116 -0.1582 249 ALA A O 1995 C CB . ALA A 249 ? 1.4740 1.6676 0.7924 -0.0515 0.2175 -0.1501 249 ALA A CB 1996 N N . PRO A 250 ? 1.3317 1.6193 0.7813 -0.0559 0.2171 -0.1436 250 PRO A N 1997 C CA . PRO A 250 ? 1.2924 1.6300 0.7910 -0.0562 0.2310 -0.1464 250 PRO A CA 1998 C C . PRO A 250 ? 1.3267 1.6858 0.8236 -0.0533 0.2574 -0.1539 250 PRO A C 1999 O O . PRO A 250 ? 1.3863 1.7289 0.8464 -0.0598 0.2737 -0.1537 250 PRO A O 2000 C CB . PRO A 250 ? 1.2633 1.6095 0.7725 -0.0723 0.2351 -0.1385 250 PRO A CB 2001 C CG . PRO A 250 ? 1.2847 1.5891 0.7652 -0.0762 0.2167 -0.1307 250 PRO A CG 2002 C CD . PRO A 250 ? 1.3370 1.6039 0.7719 -0.0689 0.2103 -0.1332 250 PRO A CD 2003 N N . GLU A 251 ? 1.3164 1.7116 0.8533 -0.0431 0.2619 -0.1596 251 GLU A N 2004 C CA . GLU A 251 ? 1.3368 1.7633 0.8873 -0.0400 0.2881 -0.1653 251 GLU A CA 2005 C C . GLU A 251 ? 1.2772 1.7522 0.8783 -0.0492 0.2942 -0.1612 251 GLU A C 2006 O O . GLU A 251 ? 1.2430 1.7346 0.8468 -0.0623 0.3126 -0.1583 251 GLU A O 2007 C CB . GLU A 251 ? 1.3646 1.7948 0.9240 -0.0203 0.2874 -0.1746 251 GLU A CB 2008 C CG . GLU A 251 ? 1.4500 1.8725 0.9815 -0.0127 0.3118 -0.1831 251 GLU A CG 2009 C CD . GLU A 251 ? 1.4611 1.9335 1.0315 -0.0122 0.3386 -0.1846 251 GLU A CD 2010 O OE1 . GLU A 251 ? 1.4732 1.9706 1.0610 -0.0278 0.3485 -0.1776 251 GLU A OE1 2011 O OE2 . GLU A 251 ? 1.4691 1.9551 1.0538 0.0038 0.3496 -0.1926 251 GLU A OE2 2012 N N . TYR A 252 ? 1.2200 1.7156 0.8593 -0.0434 0.2777 -0.1603 252 TYR A N 2013 C CA . TYR A 252 ? 1.1729 1.7113 0.8574 -0.0516 0.2784 -0.1567 252 TYR A CA 2014 C C . TYR A 252 ? 1.1518 1.6782 0.8389 -0.0601 0.2593 -0.1507 252 TYR A C 2015 O O . TYR A 252 ? 1.1334 1.6279 0.8027 -0.0545 0.2421 -0.1491 252 TYR A O 2016 C CB . TYR A 252 ? 1.1474 1.7215 0.8742 -0.0376 0.2759 -0.1600 252 TYR A CB 2017 C CG . TYR A 252 ? 1.1959 1.7856 0.9277 -0.0265 0.2958 -0.1663 252 TYR A CG 2018 C CD1 . TYR A 252 ? 1.2108 1.8388 0.9671 -0.0334 0.3171 -0.1657 252 TYR A CD1 2019 C CD2 . TYR A 252 ? 1.2232 1.7888 0.9363 -0.0092 0.2937 -0.1729 252 TYR A CD2 2020 C CE1 . TYR A 252 ? 1.2264 1.8704 0.9904 -0.0218 0.3377 -0.1712 252 TYR A CE1 2021 C CE2 . TYR A 252 ? 1.2447 1.8221 0.9612 0.0026 0.3139 -0.1798 252 TYR A CE2 2022 C CZ . TYR A 252 ? 1.2435 1.8613 0.9866 -0.0031 0.3369 -0.1787 252 TYR A CZ 2023 O OH . TYR A 252 ? 1.2566 1.8881 1.0065 0.0100 0.3592 -0.1852 252 TYR A OH 2024 N N . ALA A 253 ? 1.1428 1.6948 0.8532 -0.0736 0.2625 -0.1476 253 ALA A N 2025 C CA . ALA A 253 ? 1.1215 1.6662 0.8381 -0.0809 0.2470 -0.1433 253 ALA A CA 2026 C C . ALA A 253 ? 1.0957 1.6830 0.8521 -0.0877 0.2473 -0.1432 253 ALA A C 2027 O O . ALA A 253 ? 1.1144 1.7330 0.8890 -0.0943 0.2612 -0.1444 253 ALA A O 2028 C CB . ALA A 253 ? 1.1514 1.6634 0.8360 -0.0951 0.2493 -0.1392 253 ALA A CB 2029 N N . TYR A 254 ? 1.0728 1.6611 0.8420 -0.0863 0.2318 -0.1413 254 TYR A N 2030 C CA . TYR A 254 ? 1.0450 1.6705 0.8475 -0.0910 0.2285 -0.1414 254 TYR A CA 2031 C C . TYR A 254 ? 1.0536 1.6784 0.8532 -0.1106 0.2303 -0.1408 254 TYR A C 2032 O O . TYR A 254 ? 1.0644 1.6571 0.8430 -0.1152 0.2248 -0.1392 254 TYR A O 2033 C CB . TYR A 254 ? 1.0240 1.6504 0.8394 -0.0791 0.2120 -0.1395 254 TYR A CB 2034 C CG . TYR A 254 ? 1.0116 1.6395 0.8346 -0.0604 0.2074 -0.1398 254 TYR A CG 2035 C CD1 . TYR A 254 ? 1.0198 1.6119 0.8201 -0.0510 0.2009 -0.1391 254 TYR A CD1 2036 C CD2 . TYR A 254 ? 0.9930 1.6570 0.8467 -0.0523 0.2080 -0.1403 254 TYR A CD2 2037 C CE1 . TYR A 254 ? 1.0181 1.6083 0.8244 -0.0350 0.1956 -0.1401 254 TYR A CE1 2038 C CE2 . TYR A 254 ? 0.9928 1.6551 0.8536 -0.0349 0.2036 -0.1407 254 TYR A CE2 2039 C CZ . TYR A 254 ? 1.0139 1.6382 0.8501 -0.0267 0.1976 -0.1412 254 TYR A CZ 2040 O OH . TYR A 254 ? 1.0348 1.6544 0.8770 -0.0105 0.1924 -0.1423 254 TYR A OH 2041 N N . LYS A 255 ? 1.0579 1.7177 0.8804 -0.1219 0.2373 -0.1420 255 LYS A N 2042 C CA . LYS A 255 ? 1.0692 1.7313 0.8927 -0.1412 0.2364 -0.1426 255 LYS A CA 2043 C C . LYS A 255 ? 1.0380 1.7116 0.8752 -0.1393 0.2216 -0.1435 255 LYS A C 2044 O O . LYS A 255 ? 0.9926 1.6957 0.8538 -0.1294 0.2157 -0.1429 255 LYS A O 2045 C CB . LYS A 255 ? 1.0962 1.7931 0.9413 -0.1559 0.2480 -0.1429 255 LYS A CB 2046 C CG . LYS A 255 ? 1.1233 1.8138 0.9566 -0.1593 0.2664 -0.1414 255 LYS A CG 2047 C CD . LYS A 255 ? 1.1489 1.8604 0.9961 -0.1813 0.2779 -0.1401 255 LYS A CD 2048 C CE . LYS A 255 ? 1.1391 1.9059 1.0322 -0.1831 0.2785 -0.1403 255 LYS A CE 2049 N NZ . LYS A 255 ? 1.1692 1.9575 1.0787 -0.2056 0.2905 -0.1379 255 LYS A NZ 2050 N N . ILE A 256 ? 1.0569 1.7058 0.8773 -0.1484 0.2164 -0.1446 256 ILE A N 2051 C CA . ILE A 256 ? 1.0505 1.7065 0.8775 -0.1488 0.2048 -0.1464 256 ILE A CA 2052 C C . ILE A 256 ? 1.0578 1.7394 0.8980 -0.1678 0.2045 -0.1498 256 ILE A C 2053 O O . ILE A 256 ? 1.0557 1.7182 0.8810 -0.1840 0.2065 -0.1528 256 ILE A O 2054 C CB . ILE A 256 ? 1.0725 1.6874 0.8747 -0.1483 0.2008 -0.1469 256 ILE A CB 2055 C CG1 . ILE A 256 ? 1.0822 1.6727 0.8746 -0.1307 0.1984 -0.1425 256 ILE A CG1 2056 C CG2 . ILE A 256 ? 1.0690 1.6905 0.8745 -0.1489 0.1918 -0.1495 256 ILE A CG2 2057 C CD1 . ILE A 256 ? 1.1040 1.6524 0.8739 -0.1306 0.1968 -0.1413 256 ILE A CD1 2058 N N . VAL A 257 ? 1.0559 1.7798 0.9248 -0.1660 0.2007 -0.1489 257 VAL A N 2059 C CA . VAL A 257 ? 1.0933 1.8469 0.9798 -0.1847 0.1984 -0.1510 257 VAL A CA 2060 C C . VAL A 257 ? 1.1182 1.8736 0.9999 -0.1905 0.1843 -0.1544 257 VAL A C 2061 O O . VAL A 257 ? 1.1379 1.8935 1.0156 -0.2103 0.1812 -0.1587 257 VAL A O 2062 C CB . VAL A 257 ? 1.0862 1.8880 1.0102 -0.1816 0.2014 -0.1475 257 VAL A CB 2063 C CG1 . VAL A 257 ? 1.0949 1.8953 1.0206 -0.1834 0.2191 -0.1459 257 VAL A CG1 2064 C CG2 . VAL A 257 ? 1.0651 1.8841 1.0046 -0.1594 0.1941 -0.1440 257 VAL A CG2 2065 N N . LYS A 258 ? 1.1057 1.8601 0.9855 -0.1740 0.1759 -0.1524 258 LYS A N 2066 C CA . LYS A 258 ? 1.1286 1.8848 1.0005 -0.1771 0.1636 -0.1548 258 LYS A CA 2067 C C . LYS A 258 ? 1.1053 1.8252 0.9518 -0.1653 0.1633 -0.1552 258 LYS A C 2068 O O . LYS A 258 ? 1.0967 1.8108 0.9467 -0.1474 0.1647 -0.1500 258 LYS A O 2069 C CB . LYS A 258 ? 1.1368 1.9344 1.0353 -0.1688 0.1530 -0.1497 258 LYS A CB 2070 C CG . LYS A 258 ? 1.1725 2.0086 1.0946 -0.1852 0.1464 -0.1503 258 LYS A CG 2071 C CD . LYS A 258 ? 1.2094 2.0447 1.1158 -0.1988 0.1327 -0.1548 258 LYS A CD 2072 C CE . LYS A 258 ? 1.2076 2.0471 1.1081 -0.1840 0.1220 -0.1506 258 LYS A CE 2073 N NZ . LYS A 258 ? 1.2231 2.0851 1.1238 -0.1960 0.1052 -0.1513 258 LYS A NZ 2074 N N . LYS A 259 ? 1.1146 1.8101 0.9369 -0.1755 0.1617 -0.1614 259 LYS A N 2075 C CA . LYS A 259 ? 1.1149 1.7795 0.9159 -0.1646 0.1623 -0.1619 259 LYS A CA 2076 C C . LYS A 259 ? 1.1176 1.7928 0.9107 -0.1656 0.1532 -0.1639 259 LYS A C 2077 O O . LYS A 259 ? 1.1333 1.8344 0.9331 -0.1778 0.1447 -0.1661 259 LYS A O 2078 C CB . LYS A 259 ? 1.1383 1.7606 0.9148 -0.1727 0.1703 -0.1676 259 LYS A CB 2079 C CG . LYS A 259 ? 1.1533 1.7595 0.9320 -0.1692 0.1786 -0.1637 259 LYS A CG 2080 C CD . LYS A 259 ? 1.1793 1.7435 0.9349 -0.1781 0.1853 -0.1679 259 LYS A CD 2081 C CE . LYS A 259 ? 1.1841 1.7336 0.9394 -0.1756 0.1922 -0.1626 259 LYS A CE 2082 N NZ . LYS A 259 ? 1.2102 1.7197 0.9441 -0.1859 0.1981 -0.1650 259 LYS A NZ 2083 N N . GLY A 260 ? 1.1353 1.7915 0.9147 -0.1529 0.1547 -0.1622 260 GLY A N 2084 C CA . GLY A 260 ? 1.1524 1.8142 0.9181 -0.1527 0.1482 -0.1635 260 GLY A CA 2085 C C . GLY A 260 ? 1.1378 1.8003 0.9074 -0.1330 0.1487 -0.1547 260 GLY A C 2086 O O . GLY A 260 ? 1.1368 1.7903 0.9183 -0.1196 0.1539 -0.1485 260 GLY A O 2087 N N . ASP A 261 ? 1.1509 1.8239 0.9098 -0.1321 0.1427 -0.1534 261 ASP A N 2088 C CA . ASP A 261 ? 1.1478 1.8199 0.9075 -0.1153 0.1445 -0.1444 261 ASP A CA 2089 C C . ASP A 261 ? 1.0635 1.7627 0.8549 -0.1027 0.1384 -0.1324 261 ASP A C 2090 O O . ASP A 261 ? 1.0481 1.7777 0.8556 -0.1067 0.1286 -0.1300 261 ASP A O 2091 C CB . ASP A 261 ? 1.2076 1.8819 0.9420 -0.1189 0.1404 -0.1459 261 ASP A CB 2092 C CG . ASP A 261 ? 1.2872 1.9260 0.9863 -0.1255 0.1500 -0.1574 261 ASP A CG 2093 O OD1 . ASP A 261 ? 1.3176 1.9297 1.0156 -0.1247 0.1602 -0.1622 261 ASP A OD1 2094 O OD2 . ASP A 261 ? 1.3564 1.9921 1.0273 -0.1312 0.1474 -0.1618 261 ASP A OD2 2095 N N . SER A 262 ? 0.9973 1.6846 0.7989 -0.0875 0.1439 -0.1250 262 SER A N 2096 C CA . SER A 262 ? 0.9789 1.6847 0.8079 -0.0744 0.1386 -0.1141 262 SER A CA 2097 C C . SER A 262 ? 0.9644 1.6519 0.7968 -0.0602 0.1441 -0.1061 262 SER A C 2098 O O . SER A 262 ? 1.0013 1.6655 0.8170 -0.0603 0.1528 -0.1089 262 SER A O 2099 C CB . SER A 262 ? 0.9805 1.6919 0.8278 -0.0752 0.1384 -0.1162 262 SER A CB 2100 O OG . SER A 262 ? 0.9785 1.7020 0.8497 -0.0615 0.1341 -0.1073 262 SER A OG 2101 N N . THR A 263 ? 1.2172 1.2869 0.9167 -0.1470 0.0663 -0.0768 263 THR A N 2102 C CA . THR A 263 ? 1.1381 1.2043 0.8696 -0.0951 0.0589 -0.0778 263 THR A CA 2103 C C . THR A 263 ? 1.0435 1.1952 0.8502 -0.0800 0.0606 -0.0932 263 THR A C 2104 O O . THR A 263 ? 0.9983 1.2178 0.8525 -0.0958 0.0655 -0.1042 263 THR A O 2105 C CB . THR A 263 ? 1.1002 1.1537 0.8609 -0.0706 0.0535 -0.0761 263 THR A CB 2106 O OG1 . THR A 263 ? 1.0785 1.1235 0.8506 -0.0266 0.0469 -0.0768 263 THR A OG1 2107 C CG2 . THR A 263 ? 1.0327 1.1622 0.8738 -0.0734 0.0564 -0.0881 263 THR A CG2 2108 N N . ILE A 264 ? 1.0215 1.1713 0.8334 -0.0476 0.0565 -0.0954 264 ILE A N 2109 C CA . ILE A 264 ? 0.9485 1.1691 0.8261 -0.0327 0.0586 -0.1113 264 ILE A CA 2110 C C . ILE A 264 ? 0.9126 1.1464 0.8385 -0.0062 0.0560 -0.1181 264 ILE A C 2111 O O . ILE A 264 ? 0.9301 1.1383 0.8400 0.0178 0.0505 -0.1145 264 ILE A O 2112 C CB . ILE A 264 ? 0.9484 1.1715 0.8029 -0.0195 0.0573 -0.1128 264 ILE A CB 2113 C CG1 . ILE A 264 ? 1.0080 1.2035 0.8005 -0.0490 0.0606 -0.1041 264 ILE A CG1 2114 C CG2 . ILE A 264 ? 0.8846 1.1799 0.8037 -0.0107 0.0611 -0.1313 264 ILE A CG2 2115 C CD1 . ILE A 264 ? 1.0511 1.2318 0.8020 -0.0331 0.0584 -0.1015 264 ILE A CD1 2116 N N . MET A 265 ? 0.8841 1.1589 0.8628 -0.0099 0.0604 -0.1285 265 MET A N 2117 C CA . MET A 265 ? 0.8496 1.1281 0.8661 0.0080 0.0603 -0.1348 265 MET A CA 2118 C C . MET A 265 ? 0.8282 1.1438 0.8796 0.0185 0.0649 -0.1518 265 MET A C 2119 O O . MET A 265 ? 0.8241 1.1732 0.8878 0.0119 0.0695 -0.1608 265 MET A O 2120 C CB . MET A 265 ? 0.8584 1.1481 0.8962 -0.0001 0.0628 -0.1354 265 MET A CB 2121 C CG . MET A 265 ? 0.8554 1.1277 0.9140 0.0147 0.0619 -0.1358 265 MET A CG 2122 S SD . MET A 265 ? 0.8749 1.1639 0.9465 0.0079 0.0634 -0.1342 265 MET A SD 2123 C CE . MET A 265 ? 0.9041 1.1516 0.9289 -0.0137 0.0581 -0.1166 265 MET A CE 2124 N N . LYS A 266 ? 0.8353 1.1464 0.8980 0.0318 0.0644 -0.1574 266 LYS A N 2125 C CA . LYS A 266 ? 0.8447 1.1850 0.9311 0.0342 0.0705 -0.1753 266 LYS A CA 2126 C C . LYS A 266 ? 0.8375 1.1659 0.9455 0.0340 0.0770 -0.1838 266 LYS A C 2127 O O . LYS A 266 ? 0.8628 1.1677 0.9710 0.0376 0.0756 -0.1797 266 LYS A O 2128 C CB . LYS A 266 ? 0.8975 1.2501 0.9750 0.0438 0.0672 -0.1792 266 LYS A CB 2129 C CG . LYS A 266 ? 0.9645 1.3309 1.0137 0.0520 0.0616 -0.1744 266 LYS A CG 2130 C CD . LYS A 266 ? 0.9934 1.4046 1.0576 0.0457 0.0675 -0.1905 266 LYS A CD 2131 C CE . LYS A 266 ? 1.0391 1.4507 1.0812 0.0424 0.0656 -0.1828 266 LYS A CE 2132 N NZ . LYS A 266 ? 1.0955 1.4736 1.0859 0.0562 0.0566 -0.1651 266 LYS A NZ 2133 N N . SER A 267 ? 0.8424 1.1822 0.9617 0.0326 0.0842 -0.1958 267 SER A N 2134 C CA . SER A 267 ? 0.8565 1.1710 0.9807 0.0391 0.0907 -0.2031 267 SER A CA 2135 C C . SER A 267 ? 0.8752 1.1961 0.9984 0.0419 0.0995 -0.2204 267 SER A C 2136 O O . SER A 267 ? 0.8837 1.2391 1.0113 0.0413 0.0989 -0.2234 267 SER A O 2137 C CB . SER A 267 ? 0.8624 1.1712 0.9882 0.0473 0.0865 -0.1913 267 SER A CB 2138 O OG . SER A 267 ? 0.8986 1.1800 1.0217 0.0616 0.0918 -0.1972 267 SER A OG 2139 N N . GLU A 268 ? 0.9062 1.1873 1.0161 0.0440 0.1082 -0.2321 268 GLU A N 2140 C CA . GLU A 268 ? 0.9453 1.2116 1.0393 0.0509 0.1176 -0.2489 268 GLU A CA 2141 C C . GLU A 268 ? 0.9652 1.2173 1.0499 0.0799 0.1174 -0.2474 268 GLU A C 2142 O O . GLU A 268 ? 1.0295 1.2725 1.0962 0.0962 0.1233 -0.2603 268 GLU A O 2143 C CB . GLU A 268 ? 0.9909 1.2073 1.0571 0.0352 0.1294 -0.2641 268 GLU A CB 2144 C CG . GLU A 268 ? 0.9840 1.2322 1.0593 0.0069 0.1300 -0.2697 268 GLU A CG 2145 C CD . GLU A 268 ? 0.9809 1.2902 1.0746 0.0032 0.1261 -0.2730 268 GLU A CD 2146 O OE1 . GLU A 268 ? 0.9796 1.2902 1.0643 0.0032 0.1326 -0.2866 268 GLU A OE1 2147 O OE2 . GLU A 268 ? 0.9665 1.3173 1.0774 0.0028 0.1164 -0.2618 268 GLU A OE2 2148 N N . LEU A 269 ? 0.9564 1.2109 1.0501 0.0891 0.1105 -0.2328 269 LEU A N 2149 C CA . LEU A 269 ? 0.9905 1.2442 1.0751 0.1200 0.1094 -0.2321 269 LEU A CA 2150 C C . LEU A 269 ? 0.9773 1.3023 1.0771 0.1301 0.1055 -0.2351 269 LEU A C 2151 O O . LEU A 269 ? 0.9203 1.2908 1.0389 0.1080 0.1021 -0.2319 269 LEU A O 2152 C CB . LEU A 269 ? 0.9896 1.2374 1.0819 0.1229 0.1029 -0.2166 269 LEU A CB 2153 C CG . LEU A 269 ? 1.0357 1.2144 1.1091 0.1185 0.1071 -0.2140 269 LEU A CG 2154 C CD1 . LEU A 269 ? 1.0325 1.2178 1.1209 0.1155 0.0991 -0.1974 269 LEU A CD1 2155 C CD2 . LEU A 269 ? 1.1050 1.2193 1.1350 0.1456 0.1160 -0.2243 269 LEU A CD2 2156 N N . GLU A 270 ? 1.0329 1.3682 1.1189 0.1654 0.1062 -0.2418 270 GLU A N 2157 C CA . GLU A 270 ? 1.0493 1.4660 1.1469 0.1801 0.1032 -0.2486 270 GLU A CA 2158 C C . GLU A 270 ? 0.9986 1.4678 1.1068 0.1932 0.0964 -0.2414 270 GLU A C 2159 O O . GLU A 270 ? 1.0175 1.4491 1.1214 0.1959 0.0944 -0.2313 270 GLU A O 2160 C CB . GLU A 270 ? 1.1579 1.5566 1.2244 0.2178 0.1097 -0.2674 270 GLU A CB 2161 C CG . GLU A 270 ? 1.2698 1.5932 1.2905 0.2603 0.1138 -0.2715 270 GLU A CG 2162 C CD . GLU A 270 ? 1.3733 1.6416 1.3429 0.2941 0.1225 -0.2899 270 GLU A CD 2163 O OE1 . GLU A 270 ? 1.4074 1.7121 1.3843 0.2888 0.1246 -0.3012 270 GLU A OE1 2164 O OE2 . GLU A 270 ? 1.4440 1.6241 1.3581 0.3267 0.1279 -0.2931 270 GLU A OE2 2165 N N . TYR A 271 ? 0.9564 1.5194 1.0777 0.1987 0.0935 -0.2481 271 TYR A N 2166 C CA . TYR A 271 ? 0.9137 1.5516 1.0470 0.2013 0.0878 -0.2446 271 TYR A CA 2167 C C . TYR A 271 ? 0.9437 1.5597 1.0571 0.2504 0.0867 -0.2468 271 TYR A C 2168 O O . TYR A 271 ? 0.9502 1.5474 1.0354 0.2998 0.0895 -0.2595 271 TYR A O 2169 C CB . TYR A 271 ? 0.9036 1.6581 1.0491 0.2001 0.0868 -0.2573 271 TYR A CB 2170 C CG . TYR A 271 ? 0.8865 1.7379 1.0447 0.1860 0.0824 -0.2562 271 TYR A CG 2171 C CD1 . TYR A 271 ? 0.8571 1.6973 1.0215 0.1368 0.0804 -0.2404 271 TYR A CD1 2172 C CD2 . TYR A 271 ? 0.8964 1.8554 1.0556 0.2217 0.0807 -0.2731 271 TYR A CD2 2173 C CE1 . TYR A 271 ? 0.8405 1.7678 1.0101 0.1157 0.0781 -0.2414 271 TYR A CE1 2174 C CE2 . TYR A 271 ? 0.8801 1.9437 1.0507 0.2027 0.0777 -0.2754 271 TYR A CE2 2175 C CZ . TYR A 271 ? 0.8554 1.9001 1.0307 0.1456 0.0771 -0.2596 271 TYR A CZ 2176 O OH . TYR A 271 ? 0.8428 1.9892 1.0231 0.1194 0.0758 -0.2637 271 TYR A OH 2177 N N . GLY A 272 ? 0.9490 1.5613 1.0700 0.2385 0.0826 -0.2342 272 GLY A N 2178 C CA . GLY A 272 ? 0.9905 1.5800 1.0915 0.2828 0.0810 -0.2339 272 GLY A CA 2179 C C . GLY A 272 ? 1.0080 1.7119 1.1121 0.3171 0.0764 -0.2451 272 GLY A C 2180 O O . GLY A 272 ? 1.0253 1.7194 1.1041 0.3704 0.0748 -0.2488 272 GLY A O 2181 N N . ASN A 273 ? 0.9937 1.8092 1.1238 0.2863 0.0747 -0.2514 273 ASN A N 2182 C CA . ASN A 273 ? 1.0044 1.9583 1.1421 0.3083 0.0708 -0.2653 273 ASN A CA 2183 C C . ASN A 273 ? 0.9887 1.9631 1.1302 0.3077 0.0665 -0.2574 273 ASN A C 2184 O O . ASN A 273 ? 1.0041 1.9831 1.1266 0.3663 0.0636 -0.2620 273 ASN A O 2185 C CB . ASN A 273 ? 1.0480 2.0286 1.1592 0.3843 0.0708 -0.2841 273 ASN A CB 2186 C CG . ASN A 273 ? 1.0477 2.1959 1.1745 0.3922 0.0684 -0.3040 273 ASN A CG 2187 O OD1 . ASN A 273 ? 1.0295 2.2920 1.1742 0.3763 0.0649 -0.3080 273 ASN A OD1 2188 N ND2 . ASN A 273 ? 1.0666 2.2370 1.1860 0.4126 0.0708 -0.3182 273 ASN A ND2 2189 N N . CYS A 274 ? 0.9551 1.9377 1.1147 0.2415 0.0663 -0.2455 274 CYS A N 2190 C CA . CYS A 274 ? 0.9513 1.8879 1.1104 0.2289 0.0637 -0.2311 274 CYS A CA 2191 C C . CYS A 274 ? 0.8716 1.8324 1.0403 0.1527 0.0643 -0.2220 274 CYS A C 2192 O O . CYS A 274 ? 0.8635 1.8325 1.0326 0.1087 0.0676 -0.2220 274 CYS A O 2193 C CB . CYS A 274 ? 1.0164 1.8018 1.1610 0.2425 0.0655 -0.2173 274 CYS A CB 2194 S SG . CYS A 274 ? 1.1282 1.8318 1.2758 0.2030 0.0635 -0.1957 274 CYS A SG 2195 N N . ASN A 275 ? 0.8260 1.7893 0.9944 0.1376 0.0618 -0.2143 275 ASN A N 2196 C CA . ASN A 275 ? 0.8087 1.7728 0.9707 0.0653 0.0634 -0.2052 275 ASN A CA 2197 C C . ASN A 275 ? 0.8184 1.6749 0.9719 0.0546 0.0611 -0.1862 275 ASN A C 2198 O O . ASN A 275 ? 0.8430 1.6696 1.0007 0.0976 0.0579 -0.1830 275 ASN A O 2199 C CB . ASN A 275 ? 0.7972 1.9050 0.9616 0.0397 0.0641 -0.2198 275 ASN A CB 2200 C CG . ASN A 275 ? 0.7942 1.8999 0.9360 -0.0448 0.0687 -0.2139 275 ASN A CG 2201 O OD1 . ASN A 275 ? 0.7974 1.8802 0.9224 -0.0873 0.0733 -0.2117 275 ASN A OD1 2202 N ND2 . ASN A 275 ? 0.8167 1.9391 0.9498 -0.0695 0.0682 -0.2113 275 ASN A ND2 2203 N N . THR A 276 ? 0.8225 1.6186 0.9574 -0.0005 0.0629 -0.1739 276 THR A N 2204 C CA . THR A 276 ? 0.8164 1.5132 0.9387 -0.0107 0.0604 -0.1567 276 THR A CA 2205 C C . THR A 276 ? 0.8436 1.5087 0.9301 -0.0756 0.0628 -0.1482 276 THR A C 2206 O O . THR A 276 ? 0.8765 1.5790 0.9445 -0.1152 0.0674 -0.1538 276 THR A O 2207 C CB . THR A 276 ? 0.8221 1.4126 0.9479 0.0185 0.0591 -0.1471 276 THR A CB 2208 O OG1 . THR A 276 ? 0.8515 1.3623 0.9676 0.0141 0.0561 -0.1328 276 THR A OG1 2209 C CG2 . THR A 276 ? 0.8394 1.3971 0.9532 -0.0050 0.0617 -0.1451 276 THR A CG2 2210 N N . LYS A 277 ? 0.8736 1.4631 0.9425 -0.0858 0.0603 -0.1349 277 LYS A N 2211 C CA . LYS A 277 ? 0.9441 1.4723 0.9622 -0.1405 0.0625 -0.1249 277 LYS A CA 2212 C C . LYS A 277 ? 0.9291 1.3365 0.9268 -0.1286 0.0593 -0.1095 277 LYS A C 2213 O O . LYS A 277 ? 0.9499 1.2853 0.8944 -0.1615 0.0602 -0.0997 277 LYS A O 2214 C CB . LYS A 277 ? 1.0173 1.5582 1.0198 -0.1646 0.0624 -0.1237 277 LYS A CB 2215 C CG . LYS A 277 ? 1.0531 1.7316 1.0785 -0.1713 0.0646 -0.1412 277 LYS A CG 2216 C CD . LYS A 277 ? 1.1167 1.8706 1.1146 -0.2303 0.0726 -0.1537 277 LYS A CD 2217 C CE . LYS A 277 ? 1.1863 1.9848 1.1479 -0.2924 0.0780 -0.1601 277 LYS A CE 2218 N NZ . LYS A 277 ? 1.2530 1.9207 1.1615 -0.3218 0.0783 -0.1434 277 LYS A NZ 2219 N N . CYS A 278 ? 0.8853 1.2711 0.9177 -0.0810 0.0561 -0.1087 278 CYS A N 2220 C CA . CYS A 278 ? 0.9037 1.2000 0.9237 -0.0660 0.0530 -0.0981 278 CYS A CA 2221 C C . CYS A 278 ? 0.8478 1.1537 0.9039 -0.0290 0.0535 -0.1049 278 CYS A C 2222 O O . CYS A 278 ? 0.8146 1.1451 0.9017 0.0021 0.0537 -0.1109 278 CYS A O 2223 C CB . CYS A 278 ? 0.9404 1.1826 0.9559 -0.0537 0.0485 -0.0885 278 CYS A CB 2224 S SG . CYS A 278 ? 0.9920 1.1536 1.0042 -0.0243 0.0441 -0.0802 278 CYS A SG 2225 N N . GLN A 279 ? 0.8318 1.1132 0.8760 -0.0325 0.0543 -0.1043 279 GLN A N 2226 C CA . GLN A 279 ? 0.8036 1.0986 0.8760 -0.0060 0.0564 -0.1133 279 GLN A CA 2227 C C . GLN A 279 ? 0.7958 1.0336 0.8613 0.0058 0.0544 -0.1087 279 GLN A C 2228 O O . GLN A 279 ? 0.8095 1.0080 0.8409 -0.0070 0.0514 -0.0999 279 GLN A O 2229 C CB . GLN A 279 ? 0.8046 1.1511 0.8760 -0.0207 0.0603 -0.1220 279 GLN A CB 2230 C CG . GLN A 279 ? 0.7877 1.1506 0.8843 0.0052 0.0632 -0.1333 279 GLN A CG 2231 C CD . GLN A 279 ? 0.7848 1.1851 0.9064 0.0368 0.0653 -0.1441 279 GLN A CD 2232 O OE1 . GLN A 279 ? 0.7827 1.2493 0.9099 0.0368 0.0659 -0.1509 279 GLN A OE1 2233 N NE2 . GLN A 279 ? 0.7854 1.1438 0.9148 0.0643 0.0670 -0.1472 279 GLN A NE2 2234 N N . THR A 280 ? 0.7747 1.0089 0.8652 0.0305 0.0565 -0.1160 280 THR A N 2235 C CA . THR A 280 ? 0.7829 0.9875 0.8718 0.0385 0.0563 -0.1174 280 THR A CA 2236 C C . THR A 280 ? 0.7863 1.0136 0.8908 0.0459 0.0622 -0.1311 280 THR A C 2237 O O . THR A 280 ? 0.7902 1.0447 0.9068 0.0538 0.0662 -0.1392 280 THR A O 2238 C CB . THR A 280 ? 0.7766 0.9499 0.8723 0.0518 0.0556 -0.1158 280 THR A CB 2239 O OG1 . THR A 280 ? 0.7462 0.9210 0.8584 0.0650 0.0622 -0.1264 280 THR A OG1 2240 C CG2 . THR A 280 ? 0.7771 0.9350 0.8647 0.0489 0.0512 -0.1049 280 THR A CG2 2241 N N . PRO A 281 ? 0.7962 1.0154 0.8970 0.0460 0.0627 -0.1351 281 PRO A N 2242 C CA . PRO A 281 ? 0.7919 1.0283 0.9038 0.0492 0.0692 -0.1497 281 PRO A CA 2243 C C . PRO A 281 ? 0.8062 1.0257 0.9257 0.0603 0.0766 -0.1603 281 PRO A C 2244 O O . PRO A 281 ? 0.8032 1.0282 0.9230 0.0630 0.0833 -0.1732 281 PRO A O 2245 C CB . PRO A 281 ? 0.7865 1.0214 0.8908 0.0469 0.0674 -0.1518 281 PRO A CB 2246 C CG . PRO A 281 ? 0.7989 1.0185 0.8797 0.0462 0.0588 -0.1368 281 PRO A CG 2247 C CD . PRO A 281 ? 0.7962 0.9957 0.8752 0.0444 0.0566 -0.1268 281 PRO A CD 2248 N N . MET A 282 ? 0.8372 1.0283 0.9549 0.0665 0.0760 -0.1549 282 MET A N 2249 C CA . MET A 282 ? 0.8846 1.0417 0.9940 0.0775 0.0838 -0.1630 282 MET A CA 2250 C C . MET A 282 ? 0.8610 1.0187 0.9679 0.0986 0.0832 -0.1601 282 MET A C 2251 O O . MET A 282 ? 0.8827 1.0057 0.9708 0.1162 0.0897 -0.1670 282 MET A O 2252 C CB . MET A 282 ? 0.9555 1.0796 1.0584 0.0704 0.0849 -0.1606 282 MET A CB 2253 C CG . MET A 282 ? 1.0177 1.1602 1.1236 0.0541 0.0837 -0.1643 282 MET A CG 2254 S SD . MET A 282 ? 1.1867 1.3041 1.2795 0.0387 0.0917 -0.1739 282 MET A SD 2255 C CE . MET A 282 ? 1.1390 1.2166 1.2270 0.0508 0.0889 -0.1603 282 MET A CE 2256 N N . GLY A 283 ? 0.8203 1.0159 0.9383 0.0969 0.0760 -0.1510 283 GLY A N 2257 C CA . GLY A 283 ? 0.8268 1.0436 0.9450 0.1161 0.0743 -0.1495 283 GLY A CA 2258 C C . GLY A 283 ? 0.8163 1.0629 0.9417 0.1006 0.0671 -0.1379 283 GLY A C 2259 O O . GLY A 283 ? 0.8000 1.0320 0.9222 0.0786 0.0633 -0.1293 283 GLY A O 2260 N N . ALA A 284 ? 0.8253 1.1132 0.9537 0.1135 0.0654 -0.1390 284 ALA A N 2261 C CA . ALA A 284 ? 0.8262 1.1503 0.9562 0.0925 0.0604 -0.1313 284 ALA A CA 2262 C C . ALA A 284 ? 0.8512 1.1443 0.9789 0.0992 0.0574 -0.1223 284 ALA A C 2263 O O . ALA A 284 ? 0.8382 1.0930 0.9630 0.1252 0.0595 -0.1231 284 ALA A O 2264 C CB . ALA A 284 ? 0.8258 1.2354 0.9618 0.0972 0.0606 -0.1408 284 ALA A CB 2265 N N . ILE A 285 ? 0.8676 1.1719 0.9896 0.0731 0.0534 -0.1141 285 ILE A N 2266 C CA . ILE A 285 ? 0.8958 1.1712 1.0145 0.0747 0.0500 -0.1050 285 ILE A CA 2267 C C . ILE A 285 ? 0.9262 1.2614 1.0440 0.0626 0.0481 -0.1058 285 ILE A C 2268 O O . ILE A 285 ? 0.9359 1.3085 1.0425 0.0291 0.0486 -0.1075 285 ILE A O 2269 C CB . ILE A 285 ? 0.8875 1.1031 0.9902 0.0544 0.0469 -0.0940 285 ILE A CB 2270 C CG1 . ILE A 285 ? 0.8839 1.0535 0.9909 0.0697 0.0487 -0.0952 285 ILE A CG1 2271 C CG2 . ILE A 285 ? 0.8980 1.0946 0.9930 0.0494 0.0430 -0.0852 285 ILE A CG2 2272 C CD1 . ILE A 285 ? 0.8881 1.0184 0.9783 0.0574 0.0450 -0.0882 285 ILE A CD1 2273 N N . ASN A 286 ? 0.9642 1.3083 1.0890 0.0876 0.0466 -0.1054 286 ASN A N 2274 C CA . ASN A 286 ? 1.0224 1.4285 1.1476 0.0781 0.0445 -0.1071 286 ASN A CA 2275 C C . ASN A 286 ? 0.9727 1.3350 1.0958 0.0884 0.0414 -0.0976 286 ASN A C 2276 O O . ASN A 286 ? 0.9406 1.2974 1.0686 0.1270 0.0412 -0.0984 286 ASN A O 2277 C CB . ASN A 286 ? 1.0956 1.5896 1.2321 0.1103 0.0454 -0.1209 286 ASN A CB 2278 C CG . ASN A 286 ? 1.2346 1.8063 1.3740 0.1096 0.0429 -0.1251 286 ASN A CG 2279 O OD1 . ASN A 286 ? 1.2260 1.8324 1.3581 0.0625 0.0431 -0.1252 286 ASN A OD1 2280 N ND2 . ASN A 286 ? 1.4346 2.0303 1.5769 0.1616 0.0410 -0.1292 286 ASN A ND2 2281 N N . SER A 287 ? 0.9569 1.2793 1.0653 0.0556 0.0392 -0.0883 287 SER A N 2282 C CA . SER A 287 ? 0.9675 1.2543 1.0734 0.0617 0.0360 -0.0797 287 SER A CA 2283 C C . SER A 287 ? 0.9626 1.2270 1.0424 0.0206 0.0341 -0.0732 287 SER A C 2284 O O . SER A 287 ? 0.9638 1.2108 1.0191 -0.0105 0.0355 -0.0725 287 SER A O 2285 C CB . SER A 287 ? 0.9834 1.1956 1.0923 0.0853 0.0360 -0.0734 287 SER A CB 2286 O OG . SER A 287 ? 0.9715 1.1297 1.0657 0.0656 0.0344 -0.0670 287 SER A OG 2287 N N . SER A 288 ? 0.9744 1.2310 1.0518 0.0217 0.0313 -0.0685 288 SER A N 2288 C CA . SER A 288 ? 1.0076 1.2315 1.0514 -0.0150 0.0299 -0.0628 288 SER A CA 2289 C C . SER A 288 ? 0.9737 1.1085 1.0023 -0.0049 0.0260 -0.0517 288 SER A C 2290 O O . SER A 288 ? 0.9999 1.0935 0.9946 -0.0257 0.0241 -0.0462 288 SER A O 2291 C CB . SER A 288 ? 1.0465 1.3301 1.0947 -0.0237 0.0295 -0.0669 288 SER A CB 2292 O OG . SER A 288 ? 1.0453 1.3551 1.1261 0.0216 0.0275 -0.0674 288 SER A OG 2293 N N . MET A 289 ? 0.9158 1.0237 0.9643 0.0255 0.0254 -0.0500 289 MET A N 2294 C CA . MET A 289 ? 0.9207 0.9655 0.9591 0.0376 0.0219 -0.0428 289 MET A CA 2295 C C . MET A 289 ? 0.9320 0.9287 0.9287 0.0211 0.0200 -0.0393 289 MET A C 2296 O O . MET A 289 ? 0.9539 0.9595 0.9402 0.0082 0.0226 -0.0426 289 MET A O 2297 C CB . MET A 289 ? 0.9574 0.9959 1.0217 0.0648 0.0239 -0.0455 289 MET A CB 2298 C CG . MET A 289 ? 0.9724 1.0346 1.0615 0.0872 0.0271 -0.0485 289 MET A CG 2299 S SD . MET A 289 ? 1.0007 1.0439 1.0904 0.0974 0.0242 -0.0415 289 MET A SD 2300 C CE . MET A 289 ? 0.9876 1.0138 1.0869 0.1255 0.0306 -0.0448 289 MET A CE 2301 N N . PRO A 290 ? 0.9274 0.8704 0.8947 0.0258 0.0153 -0.0328 290 PRO A N 2302 C CA . PRO A 290 ? 0.9513 0.8375 0.8659 0.0219 0.0127 -0.0291 290 PRO A CA 2303 C C . PRO A 290 ? 0.9167 0.8022 0.8414 0.0450 0.0116 -0.0318 290 PRO A C 2304 O O . PRO A 290 ? 0.9673 0.8152 0.8477 0.0451 0.0098 -0.0297 290 PRO A O 2305 C CB . PRO A 290 ? 0.9759 0.8108 0.8566 0.0310 0.0072 -0.0229 290 PRO A CB 2306 C CG . PRO A 290 ? 0.9359 0.8075 0.8684 0.0482 0.0066 -0.0241 290 PRO A CG 2307 C CD . PRO A 290 ? 0.8980 0.8284 0.8699 0.0362 0.0119 -0.0287 290 PRO A CD 2308 N N . PHE A 291 ? 0.8624 0.7854 0.8368 0.0630 0.0133 -0.0371 291 PHE A N 2309 C CA . PHE A 291 ? 0.8495 0.7818 0.8345 0.0795 0.0136 -0.0427 291 PHE A CA 2310 C C . PHE A 291 ? 0.7906 0.7643 0.8181 0.0786 0.0205 -0.0508 291 PHE A C 2311 O O . PHE A 291 ? 0.7779 0.7699 0.8285 0.0769 0.0240 -0.0517 291 PHE A O 2312 C CB . PHE A 291 ? 0.8677 0.7972 0.8577 0.1005 0.0100 -0.0440 291 PHE A CB 2313 C CG . PHE A 291 ? 0.9186 0.8063 0.8613 0.1130 0.0022 -0.0379 291 PHE A CG 2314 C CD1 . PHE A 291 ? 0.9858 0.8527 0.8872 0.1301 -0.0025 -0.0383 291 PHE A CD1 2315 C CD2 . PHE A 291 ? 0.9551 0.8217 0.8886 0.1126 -0.0006 -0.0324 291 PHE A CD2 2316 C CE1 . PHE A 291 ? 1.0471 0.8652 0.8915 0.1503 -0.0101 -0.0331 291 PHE A CE1 2317 C CE2 . PHE A 291 ? 1.0140 0.8337 0.8953 0.1277 -0.0077 -0.0276 291 PHE A CE2 2318 C CZ . PHE A 291 ? 1.0572 0.8491 0.8906 0.1487 -0.0125 -0.0279 291 PHE A CZ 2319 N N . HIS A 292 ? 0.7748 0.7605 0.8065 0.0834 0.0223 -0.0574 292 HIS A N 2320 C CA . HIS A 292 ? 0.7492 0.7623 0.8123 0.0844 0.0297 -0.0670 292 HIS A CA 2321 C C . HIS A 292 ? 0.7285 0.7534 0.7936 0.0905 0.0309 -0.0756 292 HIS A C 2322 O O . HIS A 292 ? 0.7496 0.7705 0.7930 0.0992 0.0249 -0.0741 292 HIS A O 2323 C CB . HIS A 292 ? 0.7670 0.8002 0.8358 0.0751 0.0334 -0.0698 292 HIS A CB 2324 C CG . HIS A 292 ? 0.7797 0.8135 0.8288 0.0682 0.0318 -0.0703 292 HIS A CG 2325 N ND1 . HIS A 292 ? 0.7708 0.8198 0.8276 0.0724 0.0346 -0.0788 292 HIS A ND1 2326 C CD2 . HIS A 292 ? 0.8092 0.8258 0.8241 0.0552 0.0285 -0.0637 292 HIS A CD2 2327 C CE1 . HIS A 292 ? 0.7974 0.8414 0.8291 0.0671 0.0321 -0.0764 292 HIS A CE1 2328 N NE2 . HIS A 292 ? 0.8251 0.8439 0.8272 0.0558 0.0288 -0.0669 292 HIS A NE2 2329 N N . ASN A 293 ? 0.7077 0.7466 0.7917 0.0869 0.0391 -0.0857 293 ASN A N 2330 C CA . ASN A 293 ? 0.7075 0.7692 0.7935 0.0847 0.0424 -0.0977 293 ASN A CA 2331 C C . ASN A 293 ? 0.7191 0.7925 0.8132 0.0759 0.0506 -0.1083 293 ASN A C 2332 O O . ASN A 293 ? 0.7185 0.8073 0.8144 0.0662 0.0575 -0.1213 293 ASN A O 2333 C CB . ASN A 293 ? 0.7066 0.7703 0.7963 0.0800 0.0465 -0.1034 293 ASN A CB 2334 C CG . ASN A 293 ? 0.7172 0.7531 0.8092 0.0708 0.0568 -0.1062 293 ASN A CG 2335 O OD1 . ASN A 293 ? 0.7362 0.7560 0.8293 0.0751 0.0592 -0.1036 293 ASN A OD1 2336 N ND2 . ASN A 293 ? 0.7398 0.7693 0.8255 0.0595 0.0630 -0.1123 293 ASN A ND2 2337 N N . ILE A 294 ? 0.7143 0.7844 0.8103 0.0768 0.0504 -0.1044 294 ILE A N 2338 C CA . ILE A 294 ? 0.7443 0.8241 0.8459 0.0726 0.0576 -0.1141 294 ILE A CA 2339 C C . ILE A 294 ? 0.7442 0.8510 0.8436 0.0682 0.0571 -0.1217 294 ILE A C 2340 O O . ILE A 294 ? 0.7425 0.8608 0.8444 0.0598 0.0644 -0.1350 294 ILE A O 2341 C CB . ILE A 294 ? 0.7451 0.8307 0.8498 0.0765 0.0565 -0.1092 294 ILE A CB 2342 C CG1 . ILE A 294 ? 0.7396 0.8117 0.8458 0.0853 0.0561 -0.1027 294 ILE A CG1 2343 C CG2 . ILE A 294 ? 0.7725 0.8701 0.8809 0.0773 0.0636 -0.1204 294 ILE A CG2 2344 C CD1 . ILE A 294 ? 0.7592 0.8003 0.8599 0.0922 0.0634 -0.1077 294 ILE A CD1 2345 N N . HIS A 295 ? 0.7605 0.8733 0.8482 0.0726 0.0490 -0.1135 295 HIS A N 2346 C CA . HIS A 295 ? 0.7759 0.9116 0.8546 0.0740 0.0473 -0.1185 295 HIS A CA 2347 C C . HIS A 295 ? 0.7777 0.8947 0.8232 0.0832 0.0376 -0.1056 295 HIS A C 2348 O O . HIS A 295 ? 0.7589 0.8489 0.7910 0.0772 0.0352 -0.0948 295 HIS A O 2349 C CB . HIS A 295 ? 0.8083 0.9572 0.8973 0.0656 0.0534 -0.1251 295 HIS A CB 2350 C CG . HIS A 295 ? 0.8365 1.0142 0.9220 0.0650 0.0541 -0.1340 295 HIS A CG 2351 N ND1 . HIS A 295 ? 0.8672 1.0464 0.9293 0.0709 0.0475 -0.1269 295 HIS A ND1 2352 C CD2 . HIS A 295 ? 0.8554 1.0588 0.9519 0.0580 0.0614 -0.1499 295 HIS A CD2 2353 C CE1 . HIS A 295 ? 0.8663 1.0777 0.9301 0.0718 0.0495 -0.1375 295 HIS A CE1 2354 N NE2 . HIS A 295 ? 0.8538 1.0845 0.9409 0.0621 0.0580 -0.1524 295 HIS A NE2 2355 N N . PRO A 296 ? 0.7892 0.9187 0.8134 0.0980 0.0325 -0.1079 296 PRO A N 2356 C CA . PRO A 296 ? 0.8300 0.9217 0.8035 0.1129 0.0236 -0.0952 296 PRO A CA 2357 C C . PRO A 296 ? 0.8581 0.9215 0.8022 0.0997 0.0242 -0.0872 296 PRO A C 2358 O O . PRO A 296 ? 0.8919 0.9030 0.7906 0.0959 0.0207 -0.0747 296 PRO A O 2359 C CB . PRO A 296 ? 0.8307 0.9542 0.7874 0.1397 0.0184 -0.1029 296 PRO A CB 2360 C CG . PRO A 296 ? 0.8112 0.9956 0.8111 0.1275 0.0262 -0.1204 296 PRO A CG 2361 C CD . PRO A 296 ? 0.7819 0.9605 0.8197 0.1036 0.0348 -0.1233 296 PRO A CD 2362 N N . LEU A 297 ? 0.8583 0.9541 0.8222 0.0896 0.0294 -0.0952 297 LEU A N 2363 C CA . LEU A 297 ? 0.9105 0.9895 0.8474 0.0735 0.0310 -0.0895 297 LEU A CA 2364 C C . LEU A 297 ? 0.9082 0.9924 0.8659 0.0472 0.0363 -0.0881 297 LEU A C 2365 O O . LEU A 297 ? 0.9100 1.0349 0.9113 0.0417 0.0421 -0.0981 297 LEU A O 2366 C CB . LEU A 297 ? 0.9115 1.0308 0.8614 0.0754 0.0340 -0.0999 297 LEU A CB 2367 C CG . LEU A 297 ? 0.9382 1.0771 0.8740 0.1033 0.0290 -0.1057 297 LEU A CG 2368 C CD1 . LEU A 297 ? 0.9207 1.1121 0.8809 0.1004 0.0337 -0.1195 297 LEU A CD1 2369 C CD2 . LEU A 297 ? 1.0100 1.0942 0.8718 0.1244 0.0207 -0.0923 297 LEU A CD2 2370 N N . THR A 298 ? 0.9432 0.9873 0.8636 0.0321 0.0347 -0.0770 298 THR A N 2371 C CA . THR A 298 ? 0.9134 0.9793 0.8503 0.0059 0.0395 -0.0777 298 THR A CA 2372 C C . THR A 298 ? 0.9580 1.0012 0.8419 -0.0256 0.0417 -0.0716 298 THR A C 2373 O O . THR A 298 ? 0.9986 0.9866 0.8219 -0.0252 0.0392 -0.0636 298 THR A O 2374 C CB . THR A 298 ? 0.8983 0.9526 0.8454 0.0067 0.0377 -0.0735 298 THR A CB 2375 O OG1 . THR A 298 ? 0.9477 0.9406 0.8347 -0.0036 0.0341 -0.0618 298 THR A OG1 2376 C CG2 . THR A 298 ? 0.8861 0.9458 0.8671 0.0340 0.0357 -0.0775 298 THR A CG2 2377 N N . ILE A 299 ? 0.9462 1.0334 0.8469 -0.0525 0.0469 -0.0763 299 ILE A N 2378 C CA . ILE A 299 ? 1.0131 1.0923 0.8639 -0.0940 0.0515 -0.0736 299 ILE A CA 2379 C C . ILE A 299 ? 1.0073 1.1254 0.8709 -0.1192 0.0545 -0.0769 299 ILE A C 2380 O O . ILE A 299 ? 0.9414 1.1230 0.8652 -0.1017 0.0546 -0.0855 299 ILE A O 2381 C CB . ILE A 299 ? 1.0407 1.1689 0.9035 -0.1044 0.0561 -0.0820 299 ILE A CB 2382 C CG1 . ILE A 299 ? 1.1048 1.2393 0.9175 -0.1561 0.0628 -0.0818 299 ILE A CG1 2383 C CG2 . ILE A 299 ? 0.9866 1.1989 0.9253 -0.0847 0.0580 -0.0962 299 ILE A CG2 2384 C CD1 . ILE A 299 ? 1.2110 1.2438 0.9264 -0.1776 0.0634 -0.0683 299 ILE A CD1 2385 N N . GLY A 300 ? 1.0826 1.1588 0.8819 -0.1593 0.0573 -0.0706 300 GLY A N 2386 C CA . GLY A 300 ? 1.1166 1.2348 0.9202 -0.1898 0.0608 -0.0752 300 GLY A CA 2387 C C . GLY A 300 ? 1.1796 1.2319 0.9544 -0.1867 0.0570 -0.0658 300 GLY A C 2388 O O . GLY A 300 ? 1.2378 1.2007 0.9710 -0.1667 0.0522 -0.0549 300 GLY A O 2389 N N . GLU A 301 ? 1.1980 1.3008 0.9936 -0.2033 0.0586 -0.0712 301 GLU A N 2390 C CA . GLU A 301 ? 1.2402 1.2900 1.0129 -0.2024 0.0554 -0.0638 301 GLU A CA 2391 C C . GLU A 301 ? 1.1444 1.2134 0.9857 -0.1476 0.0483 -0.0632 301 GLU A C 2392 O O . GLU A 301 ? 1.0800 1.2266 0.9777 -0.1352 0.0484 -0.0713 301 GLU A O 2393 C CB . GLU A 301 ? 1.3073 1.4078 1.0660 -0.2506 0.0613 -0.0713 301 GLU A CB 2394 C CG . GLU A 301 ? 1.4396 1.4425 1.1105 -0.2879 0.0637 -0.0629 301 GLU A CG 2395 C CD . GLU A 301 ? 1.5908 1.5062 1.1632 -0.3295 0.0703 -0.0577 301 GLU A CD 2396 O OE1 . GLU A 301 ? 1.6315 1.5952 1.1798 -0.3841 0.0798 -0.0670 301 GLU A OE1 2397 O OE2 . GLU A 301 ? 1.6862 1.4862 1.2007 -0.3057 0.0661 -0.0449 301 GLU A OE2 2398 N N . CYS A 302 ? 1.1306 1.1296 0.9599 -0.1145 0.0425 -0.0545 302 CYS A N 2399 C CA . CYS A 302 ? 1.0656 1.0803 0.9529 -0.0686 0.0375 -0.0554 302 CYS A CA 2400 C C . CYS A 302 ? 1.0422 1.0007 0.9120 -0.0521 0.0319 -0.0472 302 CYS A C 2401 O O . CYS A 302 ? 1.0729 0.9619 0.8767 -0.0666 0.0306 -0.0395 302 CYS A O 2402 C CB . CYS A 302 ? 1.0914 1.0990 0.9908 -0.0426 0.0360 -0.0569 302 CYS A CB 2403 S SG . CYS A 302 ? 1.1219 1.2003 1.0531 -0.0520 0.0420 -0.0682 302 CYS A SG 2404 N N . PRO A 303 ? 0.9728 0.9554 0.8941 -0.0216 0.0293 -0.0491 303 PRO A N 2405 C CA . PRO A 303 ? 0.9842 0.9195 0.8927 -0.0005 0.0236 -0.0427 303 PRO A CA 2406 C C . PRO A 303 ? 0.9953 0.8940 0.8804 0.0236 0.0195 -0.0408 303 PRO A C 2407 O O . PRO A 303 ? 0.9786 0.8925 0.8665 0.0244 0.0215 -0.0447 303 PRO A O 2408 C CB . PRO A 303 ? 0.9278 0.9056 0.8963 0.0206 0.0239 -0.0470 303 PRO A CB 2409 C CG . PRO A 303 ? 0.8932 0.9328 0.8966 0.0134 0.0293 -0.0549 303 PRO A CG 2410 C CD . PRO A 303 ? 0.9161 0.9636 0.8996 -0.0053 0.0321 -0.0577 303 PRO A CD 2411 N N . LYS A 304 ? 1.0158 0.8746 0.8777 0.0455 0.0135 -0.0361 304 LYS A N 2412 C CA . LYS A 304 ? 1.0388 0.8771 0.8757 0.0754 0.0084 -0.0364 304 LYS A CA 2413 C C . LYS A 304 ? 0.9501 0.8469 0.8471 0.0958 0.0089 -0.0460 304 LYS A C 2414 O O . LYS A 304 ? 0.9153 0.8381 0.8538 0.0965 0.0107 -0.0488 304 LYS A O 2415 C CB . LYS A 304 ? 1.1377 0.9106 0.9125 0.0950 0.0012 -0.0290 304 LYS A CB 2416 C CG . LYS A 304 ? 1.2896 0.9797 0.9769 0.0741 0.0020 -0.0201 304 LYS A CG 2417 C CD . LYS A 304 ? 1.3906 1.0573 1.0347 0.0727 0.0035 -0.0192 304 LYS A CD 2418 C CE . LYS A 304 ? 1.5316 1.0982 1.0700 0.0477 0.0060 -0.0101 304 LYS A CE 2419 N NZ . LYS A 304 ? 1.5369 1.1108 1.0786 -0.0087 0.0145 -0.0105 304 LYS A NZ 2420 N N . TYR A 305 ? 0.9103 0.8257 0.8056 0.1093 0.0085 -0.0517 305 TYR A N 2421 C CA . TYR A 305 ? 0.8522 0.8249 0.7975 0.1183 0.0115 -0.0637 305 TYR A CA 2422 C C . TYR A 305 ? 0.8400 0.8244 0.7784 0.1447 0.0057 -0.0672 305 TYR A C 2423 O O . TYR A 305 ? 0.8943 0.8548 0.7839 0.1698 -0.0018 -0.0639 305 TYR A O 2424 C CB . TYR A 305 ? 0.8474 0.8468 0.7958 0.1184 0.0141 -0.0708 305 TYR A CB 2425 C CG . TYR A 305 ? 0.7957 0.8518 0.7845 0.1230 0.0181 -0.0855 305 TYR A CG 2426 C CD1 . TYR A 305 ? 0.7651 0.8431 0.7965 0.1049 0.0271 -0.0930 305 TYR A CD1 2427 C CD2 . TYR A 305 ? 0.8009 0.8880 0.7771 0.1455 0.0137 -0.0932 305 TYR A CD2 2428 C CE1 . TYR A 305 ? 0.7512 0.8686 0.8063 0.1009 0.0331 -0.1075 305 TYR A CE1 2429 C CE2 . TYR A 305 ? 0.7843 0.9313 0.7938 0.1405 0.0192 -0.1095 305 TYR A CE2 2430 C CZ . TYR A 305 ? 0.7595 0.9153 0.8058 0.1140 0.0298 -0.1164 305 TYR A CZ 2431 O OH . TYR A 305 ? 0.7542 0.9569 0.8208 0.1009 0.0376 -0.1337 305 TYR A OH 2432 N N . VAL A 306 ? 0.7838 0.8042 0.7644 0.1404 0.0097 -0.0747 306 VAL A N 2433 C CA . VAL A 306 ? 0.7601 0.8169 0.7431 0.1593 0.0064 -0.0832 306 VAL A CA 2434 C C . VAL A 306 ? 0.7363 0.8481 0.7611 0.1418 0.0158 -0.0985 306 VAL A C 2435 O O . VAL A 306 ? 0.7207 0.8235 0.7699 0.1192 0.0244 -0.0995 306 VAL A O 2436 C CB . VAL A 306 ? 0.7573 0.7925 0.7335 0.1664 0.0022 -0.0767 306 VAL A CB 2437 C CG1 . VAL A 306 ? 0.8060 0.7775 0.7267 0.1821 -0.0062 -0.0634 306 VAL A CG1 2438 C CG2 . VAL A 306 ? 0.7264 0.7522 0.7373 0.1414 0.0096 -0.0738 306 VAL A CG2 2439 N N . LYS A 307 ? 0.7655 0.9342 0.7915 0.1525 0.0146 -0.1118 307 LYS A N 2440 C CA . LYS A 307 ? 0.7799 1.0011 0.8347 0.1274 0.0254 -0.1292 307 LYS A CA 2441 C C . LYS A 307 ? 0.7788 0.9971 0.8483 0.1077 0.0320 -0.1317 307 LYS A C 2442 O O . LYS A 307 ? 0.8339 1.0946 0.9132 0.0842 0.0413 -0.1477 307 LYS A O 2443 C CB . LYS A 307 ? 0.7845 1.0861 0.8331 0.1418 0.0224 -0.1460 307 LYS A CB 2444 C CG . LYS A 307 ? 0.8070 1.1273 0.8454 0.1532 0.0201 -0.1497 307 LYS A CG 2445 C CD . LYS A 307 ? 0.8474 1.2612 0.8781 0.1735 0.0159 -0.1677 307 LYS A CD 2446 C CE . LYS A 307 ? 0.8924 1.3350 0.9115 0.1877 0.0135 -0.1732 307 LYS A CE 2447 N NZ . LYS A 307 ? 0.9309 1.4775 0.9396 0.2152 0.0078 -0.1919 307 LYS A NZ 2448 N N . SER A 308 ? 0.7713 0.9402 0.8373 0.1134 0.0283 -0.1170 308 SER A N 2449 C CA . SER A 308 ? 0.7527 0.9156 0.8276 0.0983 0.0337 -0.1179 308 SER A CA 2450 C C . SER A 308 ? 0.7721 0.9006 0.8557 0.0703 0.0469 -0.1196 308 SER A C 2451 O O . SER A 308 ? 0.7831 0.8803 0.8689 0.0701 0.0488 -0.1143 308 SER A O 2452 C CB . SER A 308 ? 0.7457 0.8673 0.8117 0.1154 0.0251 -0.1017 308 SER A CB 2453 O OG . SER A 308 ? 0.7622 0.8919 0.8044 0.1460 0.0129 -0.0983 308 SER A OG 2454 N N . ASN A 309 ? 0.8090 0.9407 0.8901 0.0480 0.0563 -0.1275 309 ASN A N 2455 C CA . ASN A 309 ? 0.8602 0.9360 0.9316 0.0278 0.0686 -0.1264 309 ASN A CA 2456 C C . ASN A 309 ? 0.8442 0.8726 0.9142 0.0414 0.0648 -0.1101 309 ASN A C 2457 O O . ASN A 309 ? 0.8580 0.8354 0.9174 0.0411 0.0710 -0.1048 309 ASN A O 2458 C CB . ASN A 309 ? 0.9187 1.0067 0.9725 -0.0090 0.0830 -0.1432 309 ASN A CB 2459 C CG . ASN A 309 ? 0.9710 1.0941 1.0203 -0.0313 0.0913 -0.1616 309 ASN A CG 2460 O OD1 . ASN A 309 ? 0.9679 1.0733 1.0204 -0.0232 0.0912 -0.1602 309 ASN A OD1 2461 N ND2 . ASN A 309 ? 1.0017 1.1825 1.0431 -0.0618 0.0990 -0.1805 309 ASN A ND2 2462 N N . ARG A 310 ? 0.8197 0.8669 0.8963 0.0571 0.0542 -0.1029 310 ARG A N 2463 C CA . ARG A 310 ? 0.8162 0.8291 0.8914 0.0660 0.0510 -0.0898 310 ARG A CA 2464 C C . ARG A 310 ? 0.7635 0.7903 0.8420 0.0886 0.0369 -0.0809 310 ARG A C 2465 O O . ARG A 310 ? 0.7481 0.8144 0.8237 0.0956 0.0317 -0.0872 310 ARG A O 2466 C CB . ARG A 310 ? 0.8700 0.8761 0.9323 0.0446 0.0608 -0.0959 310 ARG A CB 2467 C CG . ARG A 310 ? 0.9153 0.8776 0.9707 0.0517 0.0606 -0.0831 310 ARG A CG 2468 C CD . ARG A 310 ? 0.9619 0.9122 0.9959 0.0264 0.0716 -0.0893 310 ARG A CD 2469 N NE . ARG A 310 ? 1.0104 0.9414 1.0432 0.0378 0.0671 -0.0774 310 ARG A NE 2470 C CZ . ARG A 310 ? 1.0547 0.9302 1.0732 0.0489 0.0695 -0.0660 310 ARG A CZ 2471 N NH1 . ARG A 310 ? 1.1057 0.9364 1.1061 0.0543 0.0762 -0.0649 310 ARG A NH1 2472 N NH2 . ARG A 310 ? 1.0723 0.9407 1.0919 0.0586 0.0648 -0.0565 310 ARG A NH2 2473 N N . LEU A 311 ? 0.7426 0.7382 0.8212 0.1004 0.0312 -0.0677 311 LEU A N 2474 C CA . LEU A 311 ? 0.7434 0.7326 0.8131 0.1160 0.0202 -0.0587 311 LEU A CA 2475 C C . LEU A 311 ? 0.7234 0.6845 0.7962 0.1156 0.0203 -0.0480 311 LEU A C 2476 O O . LEU A 311 ? 0.7335 0.6820 0.8089 0.1144 0.0210 -0.0429 311 LEU A O 2477 C CB . LEU A 311 ? 0.7430 0.7234 0.7961 0.1265 0.0125 -0.0547 311 LEU A CB 2478 C CG . LEU A 311 ? 0.7491 0.7555 0.7910 0.1361 0.0098 -0.0633 311 LEU A CG 2479 C CD1 . LEU A 311 ? 0.7711 0.7478 0.7849 0.1440 0.0037 -0.0563 311 LEU A CD1 2480 C CD2 . LEU A 311 ? 0.7656 0.8041 0.7967 0.1536 0.0042 -0.0701 311 LEU A CD2 2481 N N . VAL A 312 ? 0.6976 0.6582 0.7698 0.1171 0.0195 -0.0462 312 VAL A N 2482 C CA . VAL A 312 ? 0.6912 0.6311 0.7655 0.1188 0.0193 -0.0369 312 VAL A CA 2483 C C . VAL A 312 ? 0.6778 0.6175 0.7435 0.1275 0.0109 -0.0324 312 VAL A C 2484 O O . VAL A 312 ? 0.6652 0.6235 0.7287 0.1298 0.0100 -0.0379 312 VAL A O 2485 C CB . VAL A 312 ? 0.7009 0.6275 0.7753 0.1108 0.0297 -0.0388 312 VAL A CB 2486 C CG1 . VAL A 312 ? 0.7130 0.6208 0.7858 0.1192 0.0287 -0.0288 312 VAL A CG1 2487 C CG2 . VAL A 312 ? 0.7084 0.6234 0.7794 0.1043 0.0388 -0.0446 312 VAL A CG2 2488 N N . LEU A 313 ? 0.6741 0.5972 0.7319 0.1304 0.0052 -0.0242 313 LEU A N 2489 C CA . LEU A 313 ? 0.6733 0.5847 0.7146 0.1377 -0.0025 -0.0197 313 LEU A CA 2490 C C . LEU A 313 ? 0.6579 0.5691 0.7103 0.1363 -0.0008 -0.0144 313 LEU A C 2491 O O . LEU A 313 ? 0.6553 0.5679 0.7184 0.1324 0.0032 -0.0108 313 LEU A O 2492 C CB . LEU A 313 ? 0.6933 0.5789 0.7081 0.1334 -0.0077 -0.0149 313 LEU A CB 2493 C CG . LEU A 313 ? 0.7409 0.6056 0.7224 0.1391 -0.0119 -0.0172 313 LEU A CG 2494 C CD1 . LEU A 313 ? 0.7679 0.6001 0.7175 0.1220 -0.0127 -0.0126 313 LEU A CD1 2495 C CD2 . LEU A 313 ? 0.7753 0.6281 0.7276 0.1625 -0.0194 -0.0194 313 LEU A CD2 2496 N N . ALA A 314 ? 0.6465 0.5602 0.6936 0.1432 -0.0044 -0.0145 314 ALA A N 2497 C CA . ALA A 314 ? 0.6374 0.5483 0.6898 0.1431 -0.0043 -0.0086 314 ALA A CA 2498 C C . ALA A 314 ? 0.6476 0.5432 0.6858 0.1406 -0.0100 -0.0030 314 ALA A C 2499 O O . ALA A 314 ? 0.6385 0.5134 0.6490 0.1415 -0.0157 -0.0037 314 ALA A O 2500 C CB . ALA A 314 ? 0.6411 0.5640 0.6899 0.1499 -0.0068 -0.0117 314 ALA A CB 2501 N N . THR A 315 ? 0.6420 0.5464 0.6917 0.1370 -0.0076 0.0017 315 THR A N 2502 C CA . THR A 315 ? 0.6654 0.5694 0.7031 0.1289 -0.0116 0.0048 315 THR A CA 2503 C C . THR A 315 ? 0.6608 0.5719 0.7053 0.1355 -0.0127 0.0089 315 THR A C 2504 O O . THR A 315 ? 0.6867 0.5857 0.7138 0.1328 -0.0179 0.0098 315 THR A O 2505 C CB . THR A 315 ? 0.6780 0.6081 0.7242 0.1195 -0.0083 0.0041 315 THR A CB 2506 O OG1 . THR A 315 ? 0.6695 0.6175 0.7373 0.1337 -0.0027 0.0048 315 THR A OG1 2507 C CG2 . THR A 315 ? 0.6975 0.6183 0.7294 0.1070 -0.0079 0.0003 315 THR A CG2 2508 N N . GLY A 316 ? 0.6296 0.5525 0.6916 0.1448 -0.0074 0.0114 316 GLY A N 2509 C CA . GLY A 316 ? 0.6293 0.5544 0.6939 0.1522 -0.0075 0.0160 316 GLY A CA 2510 C C . GLY A 316 ? 0.6260 0.5402 0.6869 0.1536 -0.0080 0.0143 316 GLY A C 2511 O O . GLY A 316 ? 0.6269 0.5376 0.6811 0.1524 -0.0107 0.0089 316 GLY A O 2512 N N . LEU A 317 ? 0.6385 0.5520 0.7005 0.1577 -0.0050 0.0182 317 LEU A N 2513 C CA . LEU A 317 ? 0.6635 0.5802 0.7220 0.1558 -0.0053 0.0153 317 LEU A CA 2514 C C . LEU A 317 ? 0.6646 0.5725 0.7178 0.1476 0.0053 0.0141 317 LEU A C 2515 O O . LEU A 317 ? 0.6695 0.5553 0.7153 0.1479 0.0127 0.0172 317 LEU A O 2516 C CB . LEU A 317 ? 0.6788 0.6013 0.7347 0.1609 -0.0112 0.0193 317 LEU A CB 2517 C CG . LEU A 317 ? 0.6857 0.6090 0.7437 0.1663 -0.0099 0.0275 317 LEU A CG 2518 C CD1 . LEU A 317 ? 0.7310 0.6393 0.7813 0.1682 -0.0010 0.0318 317 LEU A CD1 2519 C CD2 . LEU A 317 ? 0.6858 0.6192 0.7411 0.1681 -0.0172 0.0291 317 LEU A CD2 2520 N N . ARG A 318 ? 0.6694 0.5941 0.7195 0.1393 0.0065 0.0081 318 ARG A N 2521 C CA . ARG A 318 ? 0.7031 0.6216 0.7394 0.1201 0.0184 0.0039 318 ARG A CA 2522 C C . ARG A 318 ? 0.7305 0.6075 0.7459 0.1199 0.0261 0.0142 318 ARG A C 2523 O O . ARG A 318 ? 0.7090 0.5881 0.7235 0.1272 0.0226 0.0205 318 ARG A O 2524 C CB . ARG A 318 ? 0.7079 0.6705 0.7454 0.1108 0.0170 -0.0058 318 ARG A CB 2525 C CG . ARG A 318 ? 0.7639 0.7316 0.7824 0.0795 0.0309 -0.0139 318 ARG A CG 2526 C CD . ARG A 318 ? 0.7865 0.8173 0.8088 0.0711 0.0288 -0.0254 318 ARG A CD 2527 N NE . ARG A 318 ? 0.7758 0.8666 0.8123 0.0810 0.0216 -0.0395 318 ARG A NE 2528 C CZ . ARG A 318 ? 0.7870 0.9157 0.8201 0.0594 0.0293 -0.0541 318 ARG A CZ 2529 N NH1 . ARG A 318 ? 0.8293 0.9325 0.8408 0.0203 0.0459 -0.0570 318 ARG A NH1 2530 N NH2 . ARG A 318 ? 0.7807 0.9694 0.8248 0.0776 0.0207 -0.0666 318 ARG A NH2 2531 N N . ASN A 319 ? 0.7989 0.6337 0.7911 0.1146 0.0366 0.0156 319 ASN A N 2532 C CA . ASN A 319 ? 0.8599 0.6402 0.8172 0.1245 0.0440 0.0259 319 ASN A CA 2533 C C . ASN A 319 ? 0.9766 0.7230 0.8936 0.0995 0.0564 0.0254 319 ASN A C 2534 O O . ASN A 319 ? 1.0242 0.7794 0.9314 0.0670 0.0646 0.0143 319 ASN A O 2535 C CB . ASN A 319 ? 0.8575 0.5974 0.7948 0.1358 0.0498 0.0270 319 ASN A CB 2536 C CG . ASN A 319 ? 0.8918 0.5835 0.7926 0.1648 0.0528 0.0383 319 ASN A CG 2537 O OD1 . ASN A 319 ? 0.8773 0.5740 0.7756 0.1781 0.0488 0.0461 319 ASN A OD1 2538 N ND2 . ASN A 319 ? 0.9328 0.5788 0.8011 0.1789 0.0595 0.0386 319 ASN A ND2 2539 N N . SER A 320 ? 1.1141 0.8248 1.0035 0.1128 0.0583 0.0365 320 SER A N 2540 C CA . SER A 320 ? 1.2418 0.9177 1.0875 0.0876 0.0697 0.0377 320 SER A CA 2541 C C . SER A 320 ? 1.3847 0.9629 1.1543 0.0774 0.0869 0.0408 320 SER A C 2542 O O . SER A 320 ? 1.3953 0.9260 1.1412 0.1106 0.0868 0.0484 320 SER A O 2543 C CB . SER A 320 ? 1.2307 0.9135 1.0792 0.1084 0.0628 0.0488 320 SER A CB 2544 O OG . SER A 320 ? 1.1676 0.9257 1.0756 0.1208 0.0472 0.0462 320 SER A OG 2545 N N . PRO A 321 ? 1.5138 1.0613 1.2376 0.0306 0.1024 0.0337 321 PRO A N 2546 C CA . PRO A 321 ? 1.6542 1.0862 1.2836 0.0147 0.1214 0.0372 321 PRO A CA 2547 C C . PRO A 321 ? 1.7213 1.0825 1.2934 0.0367 0.1246 0.0534 321 PRO A C 2548 O O . PRO A 321 ? 1.8614 1.1175 1.3563 0.0592 0.1333 0.0626 321 PRO A O 2549 C CB . PRO A 321 ? 1.6905 1.1335 1.2948 -0.0532 0.1369 0.0209 321 PRO A CB 2550 C CG . PRO A 321 ? 1.6038 1.1609 1.2768 -0.0631 0.1256 0.0140 321 PRO A CG 2551 C CD . PRO A 321 ? 1.4987 1.1210 1.2504 -0.0114 0.1036 0.0194 321 PRO A CD 2552 N N . GLY B 1 ? 0.5075 0.5972 0.8439 -0.0149 -0.0884 0.1155 1 GLY B N 2553 C CA . GLY B 1 ? 0.4897 0.5570 0.8166 0.0077 -0.0781 0.0893 1 GLY B CA 2554 C C . GLY B 1 ? 0.4648 0.5885 0.8006 0.0321 -0.0653 0.0857 1 GLY B C 2555 O O . GLY B 1 ? 0.4587 0.6456 0.8097 0.0368 -0.0614 0.1011 1 GLY B O 2556 N N . LEU B 2 ? 0.4621 0.5597 0.7822 0.0506 -0.0598 0.0654 2 LEU B N 2557 C CA . LEU B 2 ? 0.4527 0.5888 0.7677 0.0797 -0.0525 0.0598 2 LEU B CA 2558 C C . LEU B 2 ? 0.4440 0.6055 0.7555 0.1006 -0.0425 0.0538 2 LEU B C 2559 O O . LEU B 2 ? 0.4412 0.6559 0.7512 0.1260 -0.0392 0.0578 2 LEU B O 2560 C CB . LEU B 2 ? 0.4658 0.5485 0.7529 0.0943 -0.0513 0.0380 2 LEU B CB 2561 C CG . LEU B 2 ? 0.4658 0.5350 0.7514 0.0853 -0.0608 0.0425 2 LEU B CG 2562 C CD1 . LEU B 2 ? 0.4797 0.4867 0.7320 0.0987 -0.0582 0.0208 2 LEU B CD1 2563 C CD2 . LEU B 2 ? 0.4644 0.6089 0.7663 0.0938 -0.0664 0.0611 2 LEU B CD2 2564 N N . PHE B 3 ? 0.4362 0.5643 0.7443 0.0933 -0.0385 0.0440 3 PHE B N 2565 C CA . PHE B 3 ? 0.4433 0.5840 0.7423 0.1135 -0.0310 0.0336 3 PHE B CA 2566 C C . PHE B 3 ? 0.4354 0.6276 0.7542 0.1097 -0.0287 0.0517 3 PHE B C 2567 O O . PHE B 3 ? 0.4483 0.6584 0.7596 0.1289 -0.0232 0.0448 3 PHE B O 2568 C CB . PHE B 3 ? 0.4512 0.5296 0.7302 0.1109 -0.0286 0.0096 3 PHE B CB 2569 C CG . PHE B 3 ? 0.4736 0.5058 0.7253 0.1180 -0.0309 -0.0060 3 PHE B CG 2570 C CD1 . PHE B 3 ? 0.4945 0.5163 0.7154 0.1445 -0.0326 -0.0187 3 PHE B CD1 2571 C CD2 . PHE B 3 ? 0.4768 0.4730 0.7271 0.1014 -0.0335 -0.0066 3 PHE B CD2 2572 C CE1 . PHE B 3 ? 0.5305 0.5009 0.7182 0.1512 -0.0376 -0.0310 3 PHE B CE1 2573 C CE2 . PHE B 3 ? 0.4964 0.4503 0.7188 0.1077 -0.0359 -0.0180 3 PHE B CE2 2574 C CZ . PHE B 3 ? 0.5225 0.4610 0.7129 0.1312 -0.0383 -0.0296 3 PHE B CZ 2575 N N . GLY B 4 ? 0.4364 0.6485 0.7755 0.0840 -0.0352 0.0758 4 GLY B N 2576 C CA . GLY B 4 ? 0.4256 0.6921 0.7814 0.0757 -0.0353 0.1007 4 GLY B CA 2577 C C . GLY B 4 ? 0.4328 0.6729 0.7849 0.0687 -0.0344 0.0981 4 GLY B C 2578 O O . GLY B 4 ? 0.4414 0.7191 0.8029 0.0597 -0.0356 0.1206 4 GLY B O 2579 N N . ALA B 5 ? 0.4325 0.6143 0.7703 0.0727 -0.0325 0.0731 5 ALA B N 2580 C CA . ALA B 5 ? 0.4274 0.5919 0.7604 0.0725 -0.0314 0.0680 5 ALA B CA 2581 C C . ALA B 5 ? 0.4426 0.5653 0.7697 0.0513 -0.0430 0.0780 5 ALA B C 2582 O O . ALA B 5 ? 0.4604 0.5927 0.7874 0.0405 -0.0495 0.0986 5 ALA B O 2583 C CB . ALA B 5 ? 0.4242 0.5604 0.7450 0.0868 -0.0249 0.0385 5 ALA B CB 2584 N N . ILE B 6 ? 0.4578 0.5304 0.7738 0.0471 -0.0470 0.0638 6 ILE B N 2585 C CA . ILE B 6 ? 0.4952 0.5167 0.7936 0.0357 -0.0605 0.0681 6 ILE B CA 2586 C C . ILE B 6 ? 0.5266 0.5431 0.8237 0.0103 -0.0776 0.0966 6 ILE B C 2587 O O . ILE B 6 ? 0.5226 0.5564 0.8308 -0.0009 -0.0807 0.1053 6 ILE B O 2588 C CB . ILE B 6 ? 0.5073 0.4851 0.7923 0.0402 -0.0607 0.0482 6 ILE B CB 2589 C CG1 . ILE B 6 ? 0.4944 0.4772 0.7776 0.0575 -0.0480 0.0254 6 ILE B CG1 2590 C CG2 . ILE B 6 ? 0.5517 0.4725 0.8103 0.0329 -0.0789 0.0538 6 ILE B CG2 2591 C CD1 . ILE B 6 ? 0.4993 0.4561 0.7722 0.0606 -0.0448 0.0088 6 ILE B CD1 2592 N N . ALA B 7 ? 0.5641 0.5559 0.8444 -0.0003 -0.0909 0.1122 7 ALA B N 2593 C CA . ALA B 7 ? 0.6063 0.5926 0.8818 -0.0329 -0.1109 0.1445 7 ALA B CA 2594 C C . ALA B 7 ? 0.5876 0.6602 0.8976 -0.0441 -0.1026 0.1662 7 ALA B C 2595 O O . ALA B 7 ? 0.5990 0.6882 0.9168 -0.0717 -0.1156 0.1892 7 ALA B O 2596 C CB . ALA B 7 ? 0.6347 0.5585 0.8885 -0.0482 -0.1309 0.1433 7 ALA B CB 2597 N N . GLY B 8 ? 0.5722 0.7024 0.9001 -0.0203 -0.0821 0.1585 8 GLY B N 2598 C CA . GLY B 8 ? 0.5585 0.7781 0.9133 -0.0173 -0.0718 0.1751 8 GLY B CA 2599 C C . GLY B 8 ? 0.5671 0.8297 0.9246 -0.0102 -0.0642 0.1887 8 GLY B C 2600 O O . GLY B 8 ? 0.6175 0.8721 0.9669 -0.0357 -0.0767 0.2156 8 GLY B O 2601 N N . PHE B 9 ? 0.5364 0.8369 0.8994 0.0240 -0.0465 0.1706 9 PHE B N 2602 C CA . PHE B 9 ? 0.5369 0.8751 0.8988 0.0363 -0.0390 0.1795 9 PHE B CA 2603 C C . PHE B 9 ? 0.5657 0.8390 0.9068 0.0406 -0.0425 0.1632 9 PHE B C 2604 O O . PHE B 9 ? 0.6048 0.8924 0.9393 0.0437 -0.0416 0.1748 9 PHE B O 2605 C CB . PHE B 9 ? 0.5150 0.9159 0.8828 0.0743 -0.0224 0.1663 9 PHE B CB 2606 C CG . PHE B 9 ? 0.5006 0.8567 0.8546 0.1013 -0.0166 0.1258 9 PHE B CG 2607 C CD1 . PHE B 9 ? 0.5046 0.8341 0.8465 0.1141 -0.0140 0.1076 9 PHE B CD1 2608 C CD2 . PHE B 9 ? 0.4895 0.8316 0.8405 0.1116 -0.0154 0.1077 9 PHE B CD2 2609 C CE1 . PHE B 9 ? 0.4995 0.7924 0.8292 0.1308 -0.0114 0.0739 9 PHE B CE1 2610 C CE2 . PHE B 9 ? 0.4939 0.7905 0.8280 0.1291 -0.0129 0.0744 9 PHE B CE2 2611 C CZ . PHE B 9 ? 0.4980 0.7719 0.8228 0.1358 -0.0114 0.0584 9 PHE B CZ 2612 N N . ILE B 10 ? 0.5708 0.7794 0.9006 0.0433 -0.0464 0.1375 10 ILE B N 2613 C CA . ILE B 10 ? 0.6038 0.7543 0.9113 0.0464 -0.0534 0.1265 10 ILE B CA 2614 C C . ILE B 10 ? 0.6696 0.7601 0.9575 0.0205 -0.0737 0.1414 10 ILE B C 2615 O O . ILE B 10 ? 0.6880 0.7438 0.9724 0.0155 -0.0788 0.1304 10 ILE B O 2616 C CB . ILE B 10 ? 0.5747 0.7021 0.8790 0.0680 -0.0452 0.0904 10 ILE B CB 2617 C CG1 . ILE B 10 ? 0.5510 0.7258 0.8674 0.0892 -0.0307 0.0754 10 ILE B CG1 2618 C CG2 . ILE B 10 ? 0.5872 0.6753 0.8696 0.0776 -0.0512 0.0812 10 ILE B CG2 2619 C CD1 . ILE B 10 ? 0.5440 0.6997 0.8577 0.1007 -0.0252 0.0441 10 ILE B CD1 2620 N N . GLU B 11 ? 0.7388 0.8116 1.0082 0.0036 -0.0876 0.1673 11 GLU B N 2621 C CA . GLU B 11 ? 0.8161 0.8315 1.0613 -0.0288 -0.1129 0.1894 11 GLU B CA 2622 C C . GLU B 11 ? 0.8233 0.7482 1.0318 -0.0191 -0.1276 0.1678 11 GLU B C 2623 O O . GLU B 11 ? 0.8557 0.7335 1.0481 -0.0398 -0.1463 0.1747 11 GLU B O 2624 C CB . GLU B 11 ? 0.9131 0.9228 1.1388 -0.0522 -0.1273 0.2248 11 GLU B CB 2625 C CG . GLU B 11 ? 0.9369 1.0433 1.1972 -0.0715 -0.1174 0.2569 11 GLU B CG 2626 C CD . GLU B 11 ? 1.0457 1.1404 1.2860 -0.1156 -0.1397 0.3028 11 GLU B CD 2627 O OE1 . GLU B 11 ? 1.1210 1.1510 1.3203 -0.1161 -0.1536 0.3086 11 GLU B OE1 2628 O OE2 . GLU B 11 ? 1.0609 1.2123 1.3242 -0.1506 -0.1446 0.3344 11 GLU B OE2 2629 N N . GLY B 12 ? 0.8000 0.7054 0.9935 0.0141 -0.1204 0.1422 12 GLY B N 2630 C CA . GLY B 12 ? 0.8215 0.6534 0.9768 0.0323 -0.1327 0.1214 12 GLY B CA 2631 C C . GLY B 12 ? 0.7689 0.6230 0.9304 0.0699 -0.1147 0.0894 12 GLY B C 2632 O O . GLY B 12 ? 0.7525 0.6636 0.9390 0.0810 -0.0976 0.0839 12 GLY B O 2633 N N . GLY B 13 ? 0.7704 0.5836 0.9079 0.0888 -0.1198 0.0693 13 GLY B N 2634 C CA . GLY B 13 ? 0.7440 0.5851 0.8850 0.1222 -0.1051 0.0420 13 GLY B CA 2635 C C . GLY B 13 ? 0.7751 0.5971 0.8814 0.1505 -0.1133 0.0386 13 GLY B C 2636 O O . GLY B 13 ? 0.8267 0.6047 0.9022 0.1435 -0.1310 0.0577 13 GLY B O 2637 N N . TRP B 14 ? 0.7472 0.6047 0.8564 0.1816 -0.1017 0.0158 14 TRP B N 2638 C CA . TRP B 14 ? 0.7658 0.6237 0.8472 0.2149 -0.1064 0.0092 14 TRP B CA 2639 C C . TRP B 14 ? 0.8265 0.6608 0.8677 0.2544 -0.1138 -0.0094 14 TRP B C 2640 O O . TRP B 14 ? 0.7881 0.6787 0.8529 0.2664 -0.0980 -0.0267 14 TRP B O 2641 C CB . TRP B 14 ? 0.6936 0.6376 0.8181 0.2200 -0.0855 -0.0011 14 TRP B CB 2642 C CG . TRP B 14 ? 0.6489 0.6200 0.8027 0.1948 -0.0789 0.0146 14 TRP B CG 2643 C CD1 . TRP B 14 ? 0.6711 0.6076 0.8107 0.1765 -0.0902 0.0398 14 TRP B CD1 2644 C CD2 . TRP B 14 ? 0.5843 0.6249 0.7810 0.1878 -0.0611 0.0068 14 TRP B CD2 2645 N NE1 . TRP B 14 ? 0.6279 0.6179 0.8016 0.1628 -0.0776 0.0483 14 TRP B NE1 2646 C CE2 . TRP B 14 ? 0.5789 0.6264 0.7842 0.1720 -0.0610 0.0264 14 TRP B CE2 2647 C CE3 . TRP B 14 ? 0.5477 0.6436 0.7719 0.1921 -0.0477 -0.0136 14 TRP B CE3 2648 C CZ2 . TRP B 14 ? 0.5462 0.6491 0.7819 0.1679 -0.0479 0.0229 14 TRP B CZ2 2649 C CZ3 . TRP B 14 ? 0.5133 0.6537 0.7655 0.1818 -0.0380 -0.0166 14 TRP B CZ3 2650 C CH2 . TRP B 14 ? 0.5149 0.6561 0.7705 0.1737 -0.0382 -0.0001 14 TRP B CH2 2651 N N . GLN B 15 ? 0.9408 0.6922 0.9163 0.2760 -0.1394 -0.0048 15 GLN B N 2652 C CA . GLN B 15 ? 1.0133 0.7420 0.9373 0.3279 -0.1489 -0.0240 15 GLN B CA 2653 C C . GLN B 15 ? 0.9655 0.7868 0.9121 0.3620 -0.1305 -0.0410 15 GLN B C 2654 O O . GLN B 15 ? 0.9638 0.8226 0.9004 0.3983 -0.1248 -0.0587 15 GLN B O 2655 C CB . GLN B 15 ? 1.1375 0.7520 0.9752 0.3505 -0.1837 -0.0163 15 GLN B CB 2656 C CG . GLN B 15 ? 1.2172 0.7290 1.0191 0.3163 -0.2100 0.0016 15 GLN B CG 2657 C CD . GLN B 15 ? 1.2703 0.7451 1.0440 0.3328 -0.2182 -0.0128 15 GLN B CD 2658 O OE1 . GLN B 15 ? 1.2659 0.7515 1.0758 0.2971 -0.2114 -0.0077 15 GLN B OE1 2659 N NE2 . GLN B 15 ? 1.3558 0.7881 1.0607 0.3916 -0.2333 -0.0314 15 GLN B NE2 2660 N N . GLY B 16 ? 0.9396 0.8033 0.9162 0.3502 -0.1219 -0.0344 16 GLY B N 2661 C CA . GLY B 16 ? 0.9214 0.8697 0.9165 0.3796 -0.1090 -0.0485 16 GLY B CA 2662 C C . GLY B 16 ? 0.8514 0.9080 0.9124 0.3645 -0.0836 -0.0604 16 GLY B C 2663 O O . GLY B 16 ? 0.8444 0.9772 0.9199 0.3870 -0.0754 -0.0718 16 GLY B O 2664 N N . MET B 17 ? 0.8060 0.8690 0.9038 0.3253 -0.0732 -0.0567 17 MET B N 2665 C CA . MET B 17 ? 0.7522 0.9016 0.9012 0.3076 -0.0534 -0.0664 17 MET B CA 2666 C C . MET B 17 ? 0.7555 0.9156 0.8955 0.3191 -0.0496 -0.0743 17 MET B C 2667 O O . MET B 17 ? 0.7542 0.8715 0.8939 0.2980 -0.0501 -0.0694 17 MET B O 2668 C CB . MET B 17 ? 0.7210 0.8719 0.9111 0.2603 -0.0448 -0.0582 17 MET B CB 2669 C CG . MET B 17 ? 0.6844 0.9088 0.9172 0.2384 -0.0296 -0.0671 17 MET B CG 2670 S SD . MET B 17 ? 0.6647 0.8828 0.9299 0.1964 -0.0244 -0.0609 17 MET B SD 2671 C CE . MET B 17 ? 0.6860 0.8279 0.9367 0.1821 -0.0295 -0.0483 17 MET B CE 2672 N N . VAL B 18 ? 0.7666 0.9916 0.8992 0.3546 -0.0454 -0.0857 18 VAL B N 2673 C CA . VAL B 18 ? 0.7864 1.0298 0.9017 0.3770 -0.0421 -0.0925 18 VAL B CA 2674 C C . VAL B 18 ? 0.7423 1.0849 0.9078 0.3501 -0.0221 -0.0941 18 VAL B C 2675 O O . VAL B 18 ? 0.7410 1.0993 0.9009 0.3546 -0.0161 -0.0952 18 VAL B O 2676 C CB . VAL B 18 ? 0.8448 1.1001 0.9086 0.4432 -0.0519 -0.1028 18 VAL B CB 2677 C CG1 . VAL B 18 ? 0.9125 1.0583 0.9174 0.4670 -0.0759 -0.0996 18 VAL B CG1 2678 C CG2 . VAL B 18 ? 0.8154 1.1915 0.9092 0.4593 -0.0406 -0.1095 18 VAL B CG2 2679 N N . ASP B 19 ? 0.7160 1.1207 0.9261 0.3200 -0.0139 -0.0930 19 ASP B N 2680 C CA . ASP B 19 ? 0.6900 1.1895 0.9427 0.2895 0.0003 -0.0924 19 ASP B CA 2681 C C . ASP B 19 ? 0.6405 1.1073 0.9201 0.2329 0.0053 -0.0855 19 ASP B C 2682 O O . ASP B 19 ? 0.6294 1.1560 0.9403 0.1973 0.0125 -0.0831 19 ASP B O 2683 C CB . ASP B 19 ? 0.6875 1.2780 0.9664 0.2901 0.0018 -0.0962 19 ASP B CB 2684 C CG . ASP B 19 ? 0.7045 1.2517 0.9890 0.2778 -0.0061 -0.0964 19 ASP B CG 2685 O OD1 . ASP B 19 ? 0.7121 1.1659 0.9792 0.2728 -0.0124 -0.0918 19 ASP B OD1 2686 O OD2 . ASP B 19 ? 0.7166 1.3301 1.0228 0.2730 -0.0066 -0.0999 19 ASP B OD2 2687 N N . GLY B 20 ? 0.6147 0.9872 0.8786 0.2243 -0.0005 -0.0815 20 GLY B N 2688 C CA . GLY B 20 ? 0.5910 0.9318 0.8739 0.1794 0.0032 -0.0762 20 GLY B CA 2689 C C . GLY B 20 ? 0.6057 0.8540 0.8708 0.1757 -0.0041 -0.0707 20 GLY B C 2690 O O . GLY B 20 ? 0.6436 0.8445 0.8823 0.2006 -0.0144 -0.0687 20 GLY B O 2691 N N . TRP B 21 ? 0.5753 0.7971 0.8519 0.1433 -0.0009 -0.0668 21 TRP B N 2692 C CA . TRP B 21 ? 0.5749 0.7230 0.8394 0.1374 -0.0077 -0.0601 21 TRP B CA 2693 C C . TRP B 21 ? 0.5379 0.6681 0.8127 0.1269 -0.0119 -0.0552 21 TRP B C 2694 O O . TRP B 21 ? 0.5344 0.6200 0.7977 0.1306 -0.0201 -0.0464 21 TRP B O 2695 C CB . TRP B 21 ? 0.5863 0.7145 0.8532 0.1145 -0.0030 -0.0583 21 TRP B CB 2696 C CG . TRP B 21 ? 0.6260 0.7356 0.8701 0.1308 -0.0037 -0.0586 21 TRP B CG 2697 C CD1 . TRP B 21 ? 0.6682 0.7416 0.8815 0.1612 -0.0141 -0.0591 21 TRP B CD1 2698 C CD2 . TRP B 21 ? 0.6467 0.7651 0.8896 0.1185 0.0041 -0.0584 21 TRP B CD2 2699 N NE1 . TRP B 21 ? 0.6946 0.7560 0.8874 0.1722 -0.0133 -0.0613 21 TRP B NE1 2700 C CE2 . TRP B 21 ? 0.6782 0.7716 0.8915 0.1461 -0.0005 -0.0600 21 TRP B CE2 2701 C CE3 . TRP B 21 ? 0.6542 0.7924 0.9120 0.0867 0.0123 -0.0564 21 TRP B CE3 2702 C CZ2 . TRP B 21 ? 0.7093 0.8070 0.9123 0.1448 0.0058 -0.0595 21 TRP B CZ2 2703 C CZ3 . TRP B 21 ? 0.6881 0.8276 0.9355 0.0812 0.0182 -0.0538 21 TRP B CZ3 2704 C CH2 . TRP B 21 ? 0.7138 0.8381 0.9364 0.1112 0.0165 -0.0553 21 TRP B CH2 2705 N N . TYR B 22 ? 0.5051 0.6721 0.7990 0.1126 -0.0077 -0.0597 22 TYR B N 2706 C CA . TYR B 22 ? 0.4855 0.6439 0.7860 0.1076 -0.0108 -0.0568 22 TYR B CA 2707 C C . TYR B 22 ? 0.4647 0.6709 0.7743 0.1135 -0.0108 -0.0639 22 TYR B C 2708 O O . TYR B 22 ? 0.4528 0.7039 0.7708 0.1076 -0.0079 -0.0712 22 TYR B O 2709 C CB . TYR B 22 ? 0.4772 0.6168 0.7820 0.0851 -0.0098 -0.0576 22 TYR B CB 2710 C CG . TYR B 22 ? 0.4889 0.5984 0.7871 0.0734 -0.0078 -0.0557 22 TYR B CG 2711 C CD1 . TYR B 22 ? 0.4991 0.5723 0.7890 0.0798 -0.0110 -0.0470 22 TYR B CD1 2712 C CD2 . TYR B 22 ? 0.5032 0.6185 0.8006 0.0530 -0.0049 -0.0610 22 TYR B CD2 2713 C CE1 . TYR B 22 ? 0.5113 0.5570 0.7935 0.0709 -0.0101 -0.0460 22 TYR B CE1 2714 C CE2 . TYR B 22 ? 0.5087 0.5949 0.7969 0.0435 -0.0030 -0.0584 22 TYR B CE2 2715 C CZ . TYR B 22 ? 0.5126 0.5652 0.7938 0.0549 -0.0050 -0.0520 22 TYR B CZ 2716 O OH . TYR B 22 ? 0.5309 0.5548 0.8015 0.0475 -0.0040 -0.0502 22 TYR B OH 2717 N N . GLY B 23 ? 0.4587 0.6616 0.7673 0.1233 -0.0145 -0.0602 23 GLY B N 2718 C CA . GLY B 23 ? 0.4629 0.7089 0.7779 0.1309 -0.0159 -0.0674 23 GLY B CA 2719 C C . GLY B 23 ? 0.4774 0.7161 0.7872 0.1443 -0.0193 -0.0609 23 GLY B C 2720 O O . GLY B 23 ? 0.4668 0.6749 0.7726 0.1414 -0.0196 -0.0497 23 GLY B O 2721 N N . TYR B 24 ? 0.4939 0.7687 0.8042 0.1594 -0.0216 -0.0664 24 TYR B N 2722 C CA . TYR B 24 ? 0.5063 0.7838 0.8108 0.1729 -0.0243 -0.0611 24 TYR B CA 2723 C C . TYR B 24 ? 0.5092 0.7866 0.7979 0.1988 -0.0281 -0.0546 24 TYR B C 2724 O O . TYR B 24 ? 0.5170 0.8125 0.8010 0.2126 -0.0294 -0.0618 24 TYR B O 2725 C CB . TYR B 24 ? 0.5129 0.8275 0.8247 0.1695 -0.0272 -0.0748 24 TYR B CB 2726 C CG . TYR B 24 ? 0.5274 0.8344 0.8438 0.1436 -0.0289 -0.0843 24 TYR B CG 2727 C CD1 . TYR B 24 ? 0.5352 0.8627 0.8610 0.1238 -0.0296 -0.0921 24 TYR B CD1 2728 C CD2 . TYR B 24 ? 0.5493 0.8287 0.8556 0.1405 -0.0312 -0.0841 24 TYR B CD2 2729 C CE1 . TYR B 24 ? 0.5623 0.8721 0.8848 0.0958 -0.0343 -0.0983 24 TYR B CE1 2730 C CE2 . TYR B 24 ? 0.5708 0.8283 0.8694 0.1199 -0.0366 -0.0936 24 TYR B CE2 2731 C CZ . TYR B 24 ? 0.5847 0.8519 0.8902 0.0948 -0.0391 -0.1001 24 TYR B CZ 2732 O OH . TYR B 24 ? 0.6355 0.8712 0.9263 0.0703 -0.0474 -0.1071 24 TYR B OH 2733 N N . HIS B 25 ? 0.5176 0.7764 0.7943 0.2070 -0.0305 -0.0401 25 HIS B N 2734 C CA . HIS B 25 ? 0.5406 0.7952 0.7952 0.2316 -0.0367 -0.0335 25 HIS B CA 2735 C C . HIS B 25 ? 0.5412 0.8227 0.7969 0.2397 -0.0360 -0.0312 25 HIS B C 2736 O O . HIS B 25 ? 0.5344 0.8132 0.7952 0.2293 -0.0325 -0.0207 25 HIS B O 2737 C CB . HIS B 25 ? 0.5647 0.7606 0.7932 0.2310 -0.0440 -0.0121 25 HIS B CB 2738 C CG . HIS B 25 ? 0.6062 0.7817 0.8008 0.2553 -0.0540 -0.0037 25 HIS B CG 2739 N ND1 . HIS B 25 ? 0.6210 0.7906 0.8042 0.2550 -0.0565 0.0153 25 HIS B ND1 2740 C CD2 . HIS B 25 ? 0.6367 0.7971 0.8014 0.2843 -0.0628 -0.0115 25 HIS B CD2 2741 C CE1 . HIS B 25 ? 0.6613 0.8039 0.8072 0.2791 -0.0675 0.0196 25 HIS B CE1 2742 N NE2 . HIS B 25 ? 0.6715 0.8062 0.8037 0.2999 -0.0722 0.0022 25 HIS B NE2 2743 N N . HIS B 26 ? 0.5612 0.8733 0.8102 0.2618 -0.0395 -0.0410 26 HIS B N 2744 C CA . HIS B 26 ? 0.5660 0.9059 0.8133 0.2728 -0.0398 -0.0412 26 HIS B CA 2745 C C . HIS B 26 ? 0.5915 0.9178 0.8095 0.2984 -0.0459 -0.0291 26 HIS B C 2746 O O . HIS B 26 ? 0.6119 0.9196 0.8105 0.3144 -0.0520 -0.0302 26 HIS B O 2747 C CB . HIS B 26 ? 0.5519 0.9440 0.8159 0.2737 -0.0416 -0.0651 26 HIS B CB 2748 C CG . HIS B 26 ? 0.5593 0.9856 0.8197 0.2944 -0.0464 -0.0760 26 HIS B CG 2749 N ND1 . HIS B 26 ? 0.5769 1.0170 0.8447 0.2925 -0.0456 -0.0833 26 HIS B ND1 2750 C CD2 . HIS B 26 ? 0.5810 1.0365 0.8290 0.3218 -0.0519 -0.0803 26 HIS B CD2 2751 C CE1 . HIS B 26 ? 0.5724 1.0544 0.8332 0.3199 -0.0502 -0.0917 26 HIS B CE1 2752 N NE2 . HIS B 26 ? 0.5875 1.0774 0.8362 0.3377 -0.0546 -0.0906 26 HIS B NE2 2753 N N . SER B 27 ? 0.6023 0.9353 0.8113 0.3051 -0.0451 -0.0171 27 SER B N 2754 C CA . SER B 27 ? 0.6414 0.9669 0.8197 0.3311 -0.0518 -0.0077 27 SER B CA 2755 C C . SER B 27 ? 0.6388 1.0025 0.8165 0.3439 -0.0494 -0.0079 27 SER B C 2756 O O . SER B 27 ? 0.6279 1.0036 0.8152 0.3330 -0.0428 0.0007 27 SER B O 2757 C CB . SER B 27 ? 0.6799 0.9429 0.8263 0.3252 -0.0581 0.0215 27 SER B CB 2758 O OG . SER B 27 ? 0.6765 0.9369 0.8323 0.3008 -0.0521 0.0444 27 SER B OG 2759 N N . ASN B 28 ? 0.6564 1.0420 0.8197 0.3717 -0.0556 -0.0188 28 ASN B N 2760 C CA . ASN B 28 ? 0.6575 1.0812 0.8167 0.3891 -0.0558 -0.0236 28 ASN B CA 2761 C C . ASN B 28 ? 0.7024 1.1247 0.8301 0.4223 -0.0645 -0.0226 28 ASN B C 2762 O O . ASN B 28 ? 0.7341 1.1140 0.8365 0.4309 -0.0704 -0.0133 28 ASN B O 2763 C CB . ASN B 28 ? 0.6152 1.0856 0.8020 0.3825 -0.0568 -0.0524 28 ASN B CB 2764 C CG . ASN B 28 ? 0.5875 1.0869 0.7884 0.3846 -0.0629 -0.0742 28 ASN B CG 2765 O OD1 . ASN B 28 ? 0.6053 1.1018 0.7903 0.4058 -0.0668 -0.0725 28 ASN B OD1 2766 N ND2 . ASN B 28 ? 0.5538 1.0821 0.7803 0.3634 -0.0651 -0.0935 28 ASN B ND2 2767 N N . GLU B 29 ? 0.7270 1.1892 0.8494 0.4441 -0.0674 -0.0329 29 GLU B N 2768 C CA . GLU B 29 ? 0.7910 1.2511 0.8786 0.4796 -0.0761 -0.0307 29 GLU B CA 2769 C C . GLU B 29 ? 0.8031 1.2807 0.8897 0.4997 -0.0841 -0.0507 29 GLU B C 2770 O O . GLU B 29 ? 0.8523 1.3038 0.8996 0.5307 -0.0926 -0.0451 29 GLU B O 2771 C CB . GLU B 29 ? 0.8166 1.3205 0.8993 0.4999 -0.0780 -0.0387 29 GLU B CB 2772 C CG . GLU B 29 ? 0.8384 1.3344 0.9123 0.4927 -0.0698 -0.0164 29 GLU B CG 2773 C CD . GLU B 29 ? 0.8626 1.3984 0.9231 0.5197 -0.0729 -0.0245 29 GLU B CD 2774 O OE1 . GLU B 29 ? 0.8756 1.4246 0.9164 0.5489 -0.0820 -0.0333 29 GLU B OE1 2775 O OE2 . GLU B 29 ? 0.8789 1.4333 0.9449 0.5155 -0.0671 -0.0228 29 GLU B OE2 2776 N N . GLN B 30 ? 0.7828 1.3060 0.9081 0.4835 -0.0824 -0.0728 30 GLN B N 2777 C CA . GLN B 30 ? 0.7974 1.3603 0.9286 0.5011 -0.0879 -0.0907 30 GLN B CA 2778 C C . GLN B 30 ? 0.7922 1.3056 0.9066 0.5035 -0.0875 -0.0824 30 GLN B C 2779 O O . GLN B 30 ? 0.7929 1.3279 0.8941 0.5331 -0.0931 -0.0927 30 GLN B O 2780 C CB . GLN B 30 ? 0.7917 1.4259 0.9701 0.4753 -0.0874 -0.1127 30 GLN B CB 2781 C CG . GLN B 30 ? 0.8272 1.5112 1.0157 0.4760 -0.0943 -0.1261 30 GLN B CG 2782 C CD . GLN B 30 ? 0.8499 1.5447 1.0688 0.4337 -0.0946 -0.1361 30 GLN B CD 2783 O OE1 . GLN B 30 ? 0.8623 1.5103 1.0763 0.4183 -0.0891 -0.1268 30 GLN B OE1 2784 N NE2 . GLN B 30 ? 0.8562 1.6137 1.1027 0.4152 -0.1029 -0.1539 30 GLN B NE2 2785 N N . GLY B 31 ? 0.7718 1.2229 0.8844 0.4752 -0.0821 -0.0645 31 GLY B N 2786 C CA . GLY B 31 ? 0.7832 1.1769 0.8752 0.4748 -0.0847 -0.0563 31 GLY B CA 2787 C C . GLY B 31 ? 0.7286 1.0988 0.8489 0.4322 -0.0760 -0.0494 31 GLY B C 2788 O O . GLY B 31 ? 0.6934 1.0673 0.8351 0.4054 -0.0689 -0.0420 31 GLY B O 2789 N N . SER B 32 ? 0.7250 1.0722 0.8412 0.4306 -0.0772 -0.0526 32 SER B N 2790 C CA . SER B 32 ? 0.6939 1.0122 0.8313 0.3931 -0.0705 -0.0454 32 SER B CA 2791 C C . SER B 32 ? 0.6848 1.0078 0.8263 0.3964 -0.0700 -0.0572 32 SER B C 2792 O O . SER B 32 ? 0.7149 1.0486 0.8314 0.4327 -0.0767 -0.0668 32 SER B O 2793 C CB . SER B 32 ? 0.7281 0.9648 0.8342 0.3801 -0.0763 -0.0178 32 SER B CB 2794 O OG . SER B 32 ? 0.7932 0.9660 0.8474 0.4045 -0.0910 -0.0126 32 SER B OG 2795 N N . GLY B 33 ? 0.6532 0.9703 0.8228 0.3622 -0.0622 -0.0563 33 GLY B N 2796 C CA . GLY B 33 ? 0.6551 0.9733 0.8268 0.3631 -0.0608 -0.0646 33 GLY B CA 2797 C C . GLY B 33 ? 0.6046 0.9234 0.8104 0.3232 -0.0513 -0.0644 33 GLY B C 2798 O O . GLY B 33 ? 0.5901 0.9044 0.8163 0.2956 -0.0465 -0.0584 33 GLY B O 2799 N N . TYR B 34 ? 0.6069 0.9325 0.8141 0.3249 -0.0491 -0.0714 34 TYR B N 2800 C CA . TYR B 34 ? 0.5800 0.8986 0.8119 0.2904 -0.0413 -0.0708 34 TYR B CA 2801 C C . TYR B 34 ? 0.5490 0.9452 0.8155 0.2755 -0.0332 -0.0844 34 TYR B C 2802 O O . TYR B 34 ? 0.5515 1.0077 0.8184 0.2977 -0.0332 -0.0935 34 TYR B O 2803 C CB . TYR B 34 ? 0.6040 0.8663 0.8075 0.2997 -0.0461 -0.0662 34 TYR B CB 2804 C CG . TYR B 34 ? 0.6471 0.8233 0.8102 0.3066 -0.0593 -0.0500 34 TYR B CG 2805 C CD1 . TYR B 34 ? 0.6355 0.7658 0.8055 0.2739 -0.0600 -0.0338 34 TYR B CD1 2806 C CD2 . TYR B 34 ? 0.7098 0.8508 0.8237 0.3454 -0.0733 -0.0493 34 TYR B CD2 2807 C CE1 . TYR B 34 ? 0.6855 0.7431 0.8191 0.2724 -0.0746 -0.0146 34 TYR B CE1 2808 C CE2 . TYR B 34 ? 0.7618 0.8144 0.8314 0.3455 -0.0899 -0.0316 34 TYR B CE2 2809 C CZ . TYR B 34 ? 0.7550 0.7692 0.8370 0.3053 -0.0905 -0.0129 34 TYR B CZ 2810 O OH . TYR B 34 ? 0.8328 0.7647 0.8708 0.2986 -0.1093 0.0085 34 TYR B OH 2811 N N . ALA B 35 ? 0.5327 0.9280 0.8246 0.2376 -0.0278 -0.0842 35 ALA B N 2812 C CA . ALA B 35 ? 0.5240 0.9784 0.8430 0.2128 -0.0233 -0.0929 35 ALA B CA 2813 C C . ALA B 35 ? 0.5289 0.9460 0.8555 0.1798 -0.0188 -0.0890 35 ALA B C 2814 O O . ALA B 35 ? 0.5335 0.9062 0.8600 0.1625 -0.0199 -0.0852 35 ALA B O 2815 C CB . ALA B 35 ? 0.5141 1.0100 0.8496 0.1987 -0.0277 -0.1002 35 ALA B CB 2816 N N . ALA B 36 ? 0.5425 0.9827 0.8730 0.1750 -0.0137 -0.0896 36 ALA B N 2817 C CA . ALA B 36 ? 0.5489 0.9561 0.8830 0.1463 -0.0095 -0.0857 36 ALA B CA 2818 C C . ALA B 36 ? 0.5547 0.9739 0.9045 0.1062 -0.0118 -0.0888 36 ALA B C 2819 O O . ALA B 36 ? 0.5729 1.0512 0.9361 0.0946 -0.0154 -0.0938 36 ALA B O 2820 C CB . ALA B 36 ? 0.5578 0.9969 0.8894 0.1547 -0.0033 -0.0850 36 ALA B CB 2821 N N . ASP B 37 ? 0.5774 0.9373 0.9208 0.0859 -0.0125 -0.0859 37 ASP B N 2822 C CA . ASP B 37 ? 0.5945 0.9442 0.9385 0.0491 -0.0182 -0.0891 37 ASP B CA 2823 C C . ASP B 37 ? 0.6392 1.0042 0.9865 0.0242 -0.0134 -0.0844 37 ASP B C 2824 O O . ASP B 37 ? 0.6318 0.9565 0.9705 0.0257 -0.0079 -0.0793 37 ASP B O 2825 C CB . ASP B 37 ? 0.6119 0.8912 0.9400 0.0480 -0.0218 -0.0886 37 ASP B CB 2826 C CG . ASP B 37 ? 0.6419 0.8933 0.9559 0.0181 -0.0325 -0.0944 37 ASP B CG 2827 O OD1 . ASP B 37 ? 0.6620 0.8859 0.9672 -0.0044 -0.0325 -0.0914 37 ASP B OD1 2828 O OD2 . ASP B 37 ? 0.6339 0.8841 0.9396 0.0187 -0.0428 -0.1021 37 ASP B OD2 2829 N N . LYS B 38 ? 0.6804 1.1090 1.0404 -0.0002 -0.0162 -0.0843 38 LYS B N 2830 C CA . LYS B 38 ? 0.6994 1.1674 1.0659 -0.0238 -0.0101 -0.0758 38 LYS B CA 2831 C C . LYS B 38 ? 0.7028 1.1083 1.0521 -0.0605 -0.0143 -0.0711 38 LYS B C 2832 O O . LYS B 38 ? 0.6963 1.0993 1.0424 -0.0654 -0.0057 -0.0634 38 LYS B O 2833 C CB . LYS B 38 ? 0.7483 1.3151 1.1356 -0.0451 -0.0134 -0.0732 38 LYS B CB 2834 C CG . LYS B 38 ? 0.7781 1.4276 1.1801 -0.0026 -0.0047 -0.0749 38 LYS B CG 2835 C CD . LYS B 38 ? 0.8117 1.5450 1.2330 -0.0120 -0.0132 -0.0779 38 LYS B CD 2836 C CE . LYS B 38 ? 0.8223 1.6599 1.2574 0.0270 -0.0041 -0.0771 38 LYS B CE 2837 N NZ . LYS B 38 ? 0.8454 1.7791 1.2980 0.0027 0.0034 -0.0638 38 LYS B NZ 2838 N N . GLU B 39 ? 0.7210 1.0725 1.0532 -0.0822 -0.0290 -0.0765 39 GLU B N 2839 C CA . GLU B 39 ? 0.7637 1.0443 1.0685 -0.1140 -0.0373 -0.0735 39 GLU B CA 2840 C C . GLU B 39 ? 0.7242 0.9428 1.0160 -0.0913 -0.0284 -0.0722 39 GLU B C 2841 O O . GLU B 39 ? 0.7334 0.9329 1.0153 -0.1086 -0.0246 -0.0644 39 GLU B O 2842 C CB . GLU B 39 ? 0.8461 1.0687 1.1227 -0.1297 -0.0583 -0.0830 39 GLU B CB 2843 C CG . GLU B 39 ? 0.9311 1.0575 1.1656 -0.1459 -0.0692 -0.0835 39 GLU B CG 2844 C CD . GLU B 39 ? 1.0190 1.0845 1.2128 -0.1658 -0.0957 -0.0931 39 GLU B CD 2845 O OE1 . GLU B 39 ? 1.0580 1.1539 1.2521 -0.2026 -0.1103 -0.0916 39 GLU B OE1 2846 O OE2 . GLU B 39 ? 1.0643 1.0518 1.2220 -0.1432 -0.1038 -0.1022 39 GLU B OE2 2847 N N . SER B 40 ? 0.6727 0.8630 0.9640 -0.0551 -0.0260 -0.0779 40 SER B N 2848 C CA . SER B 40 ? 0.6568 0.7957 0.9381 -0.0365 -0.0201 -0.0752 40 SER B CA 2849 C C . SER B 40 ? 0.6122 0.7792 0.9066 -0.0234 -0.0073 -0.0682 40 SER B C 2850 O O . SER B 40 ? 0.6068 0.7383 0.8901 -0.0249 -0.0039 -0.0639 40 SER B O 2851 C CB . SER B 40 ? 0.6425 0.7559 0.9214 -0.0063 -0.0219 -0.0787 40 SER B CB 2852 O OG . SER B 40 ? 0.6487 0.8068 0.9469 0.0154 -0.0176 -0.0786 40 SER B OG 2853 N N . THR B 41 ? 0.5657 0.7935 0.8780 -0.0070 -0.0018 -0.0683 41 THR B N 2854 C CA . THR B 41 ? 0.5417 0.7975 0.8569 0.0114 0.0077 -0.0640 41 THR B CA 2855 C C . THR B 41 ? 0.5467 0.8231 0.8591 -0.0149 0.0131 -0.0570 41 THR B C 2856 O O . THR B 41 ? 0.5480 0.8021 0.8495 -0.0060 0.0185 -0.0533 41 THR B O 2857 C CB . THR B 41 ? 0.5299 0.8538 0.8572 0.0374 0.0106 -0.0667 41 THR B CB 2858 O OG1 . THR B 41 ? 0.5277 0.8272 0.8526 0.0627 0.0055 -0.0706 41 THR B OG1 2859 C CG2 . THR B 41 ? 0.5299 0.8785 0.8493 0.0638 0.0183 -0.0643 41 THR B CG2 2860 N N . GLN B 42 ? 0.5617 0.8806 0.8817 -0.0496 0.0100 -0.0537 42 GLN B N 2861 C CA . GLN B 42 ? 0.5923 0.9414 0.9100 -0.0814 0.0147 -0.0422 42 GLN B CA 2862 C C . GLN B 42 ? 0.6248 0.8900 0.9163 -0.1030 0.0105 -0.0387 42 GLN B C 2863 O O . GLN B 42 ? 0.6388 0.9082 0.9222 -0.1108 0.0181 -0.0296 42 GLN B O 2864 C CB . GLN B 42 ? 0.6128 1.0288 0.9440 -0.1220 0.0084 -0.0360 42 GLN B CB 2865 C CG . GLN B 42 ? 0.6421 1.1121 0.9749 -0.1595 0.0139 -0.0185 42 GLN B CG 2866 C CD . GLN B 42 ? 0.6355 1.1861 0.9809 -0.1258 0.0322 -0.0128 42 GLN B CD 2867 O OE1 . GLN B 42 ? 0.6481 1.1916 0.9812 -0.1279 0.0409 -0.0037 42 GLN B OE1 2868 N NE2 . GLN B 42 ? 0.6159 1.2418 0.9805 -0.0903 0.0369 -0.0189 42 GLN B NE2 2869 N N . LYS B 43 ? 0.6495 0.8416 0.9240 -0.1089 -0.0019 -0.0460 43 LYS B N 2870 C CA . LYS B 43 ? 0.6964 0.8045 0.9408 -0.1168 -0.0068 -0.0451 43 LYS B CA 2871 C C . LYS B 43 ? 0.6495 0.7394 0.8942 -0.0847 0.0035 -0.0446 43 LYS B C 2872 O O . LYS B 43 ? 0.6716 0.7264 0.8978 -0.0931 0.0053 -0.0390 43 LYS B O 2873 C CB . LYS B 43 ? 0.7569 0.7969 0.9803 -0.1115 -0.0211 -0.0554 43 LYS B CB 2874 C CG . LYS B 43 ? 0.8659 0.8817 1.0657 -0.1482 -0.0391 -0.0571 43 LYS B CG 2875 C CD . LYS B 43 ? 0.9611 0.8802 1.1160 -0.1421 -0.0546 -0.0653 43 LYS B CD 2876 C CE . LYS B 43 ? 1.0539 0.9275 1.1700 -0.1778 -0.0785 -0.0683 43 LYS B CE 2877 N NZ . LYS B 43 ? 1.0725 0.9684 1.1969 -0.1675 -0.0875 -0.0794 43 LYS B NZ 2878 N N . ALA B 44 ? 0.5820 0.6898 0.8431 -0.0495 0.0077 -0.0496 44 ALA B N 2879 C CA . ALA B 44 ? 0.5615 0.6439 0.8179 -0.0221 0.0120 -0.0489 44 ALA B CA 2880 C C . ALA B 44 ? 0.5615 0.6802 0.8157 -0.0182 0.0217 -0.0432 44 ALA B C 2881 O O . ALA B 44 ? 0.5775 0.6616 0.8159 -0.0136 0.0234 -0.0404 44 ALA B O 2882 C CB . ALA B 44 ? 0.5379 0.6235 0.8050 0.0089 0.0099 -0.0531 44 ALA B CB 2883 N N . ILE B 45 ? 0.5547 0.7488 0.8232 -0.0173 0.0279 -0.0413 45 ILE B N 2884 C CA . ILE B 45 ? 0.5641 0.8090 0.8289 -0.0079 0.0385 -0.0351 45 ILE B CA 2885 C C . ILE B 45 ? 0.5843 0.8187 0.8365 -0.0426 0.0421 -0.0239 45 ILE B C 2886 O O . ILE B 45 ? 0.6011 0.8333 0.8387 -0.0298 0.0488 -0.0197 45 ILE B O 2887 C CB . ILE B 45 ? 0.5628 0.9086 0.8467 -0.0002 0.0447 -0.0334 45 ILE B CB 2888 C CG1 . ILE B 45 ? 0.5513 0.9003 0.8360 0.0451 0.0411 -0.0443 45 ILE B CG1 2889 C CG2 . ILE B 45 ? 0.5667 0.9824 0.8465 0.0054 0.0572 -0.0237 45 ILE B CG2 2890 C CD1 . ILE B 45 ? 0.5483 0.9898 0.8527 0.0523 0.0438 -0.0452 45 ILE B CD1 2891 N N . ASP B 46 ? 0.5973 0.8179 0.8486 -0.0856 0.0354 -0.0190 46 ASP B N 2892 C CA . ASP B 46 ? 0.6383 0.8366 0.8694 -0.1239 0.0351 -0.0062 46 ASP B CA 2893 C C . ASP B 46 ? 0.6440 0.7504 0.8475 -0.1133 0.0315 -0.0096 46 ASP B C 2894 O O . ASP B 46 ? 0.6704 0.7686 0.8565 -0.1196 0.0373 -0.0004 46 ASP B O 2895 C CB . ASP B 46 ? 0.6789 0.8662 0.9041 -0.1736 0.0223 -0.0009 46 ASP B CB 2896 C CG . ASP B 46 ? 0.6829 0.9714 0.9366 -0.1926 0.0241 0.0055 46 ASP B CG 2897 O OD1 . ASP B 46 ? 0.6594 1.0337 0.9361 -0.1642 0.0377 0.0067 46 ASP B OD1 2898 O OD2 . ASP B 46 ? 0.7145 0.9950 0.9635 -0.2338 0.0097 0.0086 46 ASP B OD2 2899 N N . GLY B 47 ? 0.6256 0.6703 0.8250 -0.0962 0.0222 -0.0214 47 GLY B N 2900 C CA . GLY B 47 ? 0.6391 0.6080 0.8156 -0.0836 0.0176 -0.0245 47 GLY B CA 2901 C C . GLY B 47 ? 0.6347 0.6093 0.8100 -0.0543 0.0253 -0.0241 47 GLY B C 2902 O O . GLY B 47 ? 0.6531 0.5951 0.8062 -0.0571 0.0267 -0.0193 47 GLY B O 2903 N N . VAL B 48 ? 0.6076 0.6176 0.8004 -0.0250 0.0281 -0.0295 48 VAL B N 2904 C CA . VAL B 48 ? 0.6043 0.6081 0.7871 0.0070 0.0299 -0.0315 48 VAL B CA 2905 C C . VAL B 48 ? 0.6153 0.6632 0.7866 0.0077 0.0414 -0.0239 48 VAL B C 2906 O O . VAL B 48 ? 0.6447 0.6653 0.7947 0.0231 0.0417 -0.0235 48 VAL B O 2907 C CB . VAL B 48 ? 0.5985 0.6189 0.7919 0.0379 0.0258 -0.0389 48 VAL B CB 2908 C CG1 . VAL B 48 ? 0.6154 0.6248 0.7869 0.0723 0.0236 -0.0419 48 VAL B CG1 2909 C CG2 . VAL B 48 ? 0.5900 0.5665 0.7919 0.0380 0.0147 -0.0425 48 VAL B CG2 2910 N N . THR B 49 ? 0.5994 0.7215 0.7847 -0.0091 0.0504 -0.0166 49 THR B N 2911 C CA . THR B 49 ? 0.6097 0.7946 0.7874 -0.0107 0.0633 -0.0052 49 THR B CA 2912 C C . THR B 49 ? 0.6530 0.7991 0.8091 -0.0415 0.0648 0.0064 49 THR B C 2913 O O . THR B 49 ? 0.6707 0.8217 0.8069 -0.0267 0.0718 0.0114 49 THR B O 2914 C CB . THR B 49 ? 0.5950 0.8796 0.7971 -0.0311 0.0712 0.0041 49 THR B CB 2915 O OG1 . THR B 49 ? 0.5572 0.8748 0.7754 0.0015 0.0690 -0.0076 49 THR B OG1 2916 C CG2 . THR B 49 ? 0.6067 0.9766 0.8039 -0.0313 0.0863 0.0194 49 THR B CG2 2917 N N . ASN B 50 ? 0.6865 0.7885 0.8398 -0.0815 0.0566 0.0102 50 ASN B N 2918 C CA . ASN B 50 ? 0.7380 0.7829 0.8609 -0.1089 0.0537 0.0201 50 ASN B CA 2919 C C . ASN B 50 ? 0.7431 0.7181 0.8444 -0.0779 0.0499 0.0114 50 ASN B C 2920 O O . ASN B 50 ? 0.7663 0.7244 0.8427 -0.0805 0.0541 0.0198 50 ASN B O 2921 C CB . ASN B 50 ? 0.7701 0.7594 0.8820 -0.1476 0.0396 0.0211 50 ASN B CB 2922 C CG . ASN B 50 ? 0.7968 0.8455 0.9194 -0.1928 0.0394 0.0349 50 ASN B CG 2923 O OD1 . ASN B 50 ? 0.8249 0.9479 0.9533 -0.2102 0.0509 0.0519 50 ASN B OD1 2924 N ND2 . ASN B 50 ? 0.8145 0.8358 0.9388 -0.2120 0.0254 0.0286 50 ASN B ND2 2925 N N . LYS B 51 ? 0.7297 0.6682 0.8406 -0.0507 0.0411 -0.0037 51 LYS B N 2926 C CA . LYS B 51 ? 0.7378 0.6168 0.8325 -0.0245 0.0341 -0.0111 51 LYS B CA 2927 C C . LYS B 51 ? 0.7482 0.6488 0.8296 0.0028 0.0408 -0.0102 51 LYS B C 2928 O O . LYS B 51 ? 0.7725 0.6368 0.8283 0.0072 0.0399 -0.0076 51 LYS B O 2929 C CB . LYS B 51 ? 0.7137 0.5717 0.8261 -0.0040 0.0236 -0.0229 51 LYS B CB 2930 C CG . LYS B 51 ? 0.7259 0.5386 0.8265 0.0210 0.0141 -0.0283 51 LYS B CG 2931 C CD . LYS B 51 ? 0.7209 0.5216 0.8403 0.0324 0.0031 -0.0344 51 LYS B CD 2932 C CE . LYS B 51 ? 0.7274 0.5095 0.8534 0.0174 -0.0012 -0.0347 51 LYS B CE 2933 N NZ . LYS B 51 ? 0.7291 0.4974 0.8675 0.0301 -0.0124 -0.0365 51 LYS B NZ 2934 N N . VAL B 52 ? 0.7255 0.6832 0.8191 0.0253 0.0462 -0.0133 52 VAL B N 2935 C CA . VAL B 52 ? 0.7482 0.7237 0.8206 0.0605 0.0500 -0.0151 52 VAL B CA 2936 C C . VAL B 52 ? 0.7797 0.7859 0.8340 0.0457 0.0635 -0.0005 52 VAL B C 2937 O O . VAL B 52 ? 0.8085 0.7837 0.8339 0.0640 0.0624 -0.0010 52 VAL B O 2938 C CB . VAL B 52 ? 0.7398 0.7771 0.8206 0.0916 0.0533 -0.0208 52 VAL B CB 2939 C CG1 . VAL B 52 ? 0.7732 0.8319 0.8215 0.1338 0.0570 -0.0231 52 VAL B CG1 2940 C CG2 . VAL B 52 ? 0.7271 0.7231 0.8166 0.1078 0.0378 -0.0334 52 VAL B CG2 2941 N N . ASN B 53 ? 0.7741 0.8403 0.8435 0.0101 0.0745 0.0141 53 ASN B N 2942 C CA . ASN B 53 ? 0.8140 0.9171 0.8668 -0.0126 0.0871 0.0337 53 ASN B CA 2943 C C . ASN B 53 ? 0.8464 0.8628 0.8705 -0.0341 0.0802 0.0382 53 ASN B C 2944 O O . ASN B 53 ? 0.8742 0.8935 0.8719 -0.0335 0.0875 0.0493 53 ASN B O 2945 C CB . ASN B 53 ? 0.8186 1.0027 0.8939 -0.0568 0.0960 0.0518 53 ASN B CB 2946 C CG . ASN B 53 ? 0.8009 1.0868 0.9032 -0.0322 0.1044 0.0490 53 ASN B CG 2947 O OD1 . ASN B 53 ? 0.8130 1.1212 0.9062 0.0211 0.1075 0.0380 53 ASN B OD1 2948 N ND2 . ASN B 53 ? 0.7913 1.1349 0.9217 -0.0690 0.1054 0.0581 53 ASN B ND2 2949 N N . SER B 54 ? 0.8502 0.7922 0.8762 -0.0488 0.0659 0.0297 54 SER B N 2950 C CA . SER B 54 ? 0.8987 0.7550 0.8930 -0.0601 0.0569 0.0311 54 SER B CA 2951 C C . SER B 54 ? 0.9201 0.7395 0.8958 -0.0197 0.0531 0.0210 54 SER B C 2952 O O . SER B 54 ? 0.9594 0.7473 0.9033 -0.0212 0.0543 0.0281 54 SER B O 2953 C CB . SER B 54 ? 0.8936 0.6863 0.8906 -0.0736 0.0417 0.0220 54 SER B CB 2954 O OG . SER B 54 ? 0.9189 0.7109 0.9092 -0.1182 0.0395 0.0338 54 SER B OG 2955 N N . ILE B 55 ? 0.9186 0.7386 0.9108 0.0141 0.0464 0.0053 55 ILE B N 2956 C CA . ILE B 55 ? 0.9515 0.7344 0.9246 0.0504 0.0375 -0.0050 55 ILE B CA 2957 C C . ILE B 55 ? 0.9927 0.8108 0.9396 0.0712 0.0484 0.0009 55 ILE B C 2958 O O . ILE B 55 ? 1.0258 0.8050 0.9422 0.0830 0.0449 0.0010 55 ILE B O 2959 C CB . ILE B 55 ? 0.9515 0.7279 0.9428 0.0758 0.0250 -0.0195 55 ILE B CB 2960 C CG1 . ILE B 55 ? 0.9358 0.6727 0.9467 0.0601 0.0131 -0.0237 55 ILE B CG1 2961 C CG2 . ILE B 55 ? 0.9815 0.7245 0.9457 0.1121 0.0128 -0.0288 55 ILE B CG2 2962 C CD1 . ILE B 55 ? 0.9113 0.6477 0.9430 0.0747 0.0015 -0.0325 55 ILE B CD1 2963 N N . ILE B 56 ? 0.9955 0.8927 0.9528 0.0786 0.0617 0.0059 56 ILE B N 2964 C CA . ILE B 56 ? 1.0294 0.9782 0.9613 0.1030 0.0745 0.0131 56 ILE B CA 2965 C C . ILE B 56 ? 1.0949 1.0407 1.0052 0.0736 0.0848 0.0325 56 ILE B C 2966 O O . ILE B 56 ? 1.1343 1.0617 1.0102 0.0968 0.0856 0.0330 56 ILE B O 2967 C CB . ILE B 56 ? 1.0100 1.0641 0.9609 0.1119 0.0892 0.0190 56 ILE B CB 2968 C CG1 . ILE B 56 ? 0.9988 1.0467 0.9544 0.1540 0.0773 -0.0012 56 ILE B CG1 2969 C CG2 . ILE B 56 ? 1.0392 1.1680 0.9655 0.1321 0.1066 0.0323 56 ILE B CG2 2970 C CD1 . ILE B 56 ? 0.9812 1.1274 0.9597 0.1630 0.0887 0.0020 56 ILE B CD1 2971 N N . ASP B 57 ? 1.1268 1.0831 1.0513 0.0223 0.0899 0.0485 57 ASP B N 2972 C CA . ASP B 57 ? 1.1930 1.1503 1.0923 -0.0131 0.0988 0.0718 57 ASP B CA 2973 C C . ASP B 57 ? 1.2149 1.0690 1.0794 -0.0151 0.0865 0.0683 57 ASP B C 2974 O O . ASP B 57 ? 1.2502 1.0962 1.0814 -0.0250 0.0928 0.0841 57 ASP B O 2975 C CB . ASP B 57 ? 1.2285 1.2211 1.1456 -0.0719 0.1029 0.0915 57 ASP B CB 2976 C CG . ASP B 57 ? 1.2581 1.3809 1.1999 -0.0776 0.1207 0.1070 57 ASP B CG 2977 O OD1 . ASP B 57 ? 1.2940 1.4816 1.2193 -0.0699 0.1362 0.1242 57 ASP B OD1 2978 O OD2 . ASP B 57 ? 1.2414 1.4083 1.2186 -0.0873 0.1195 0.1028 57 ASP B OD2 2979 N N . LYS B 58 ? 1.2053 0.9869 1.0765 -0.0047 0.0691 0.0493 58 LYS B N 2980 C CA . LYS B 58 ? 1.2357 0.9292 1.0752 0.0018 0.0562 0.0439 58 LYS B CA 2981 C C . LYS B 58 ? 1.2766 0.9603 1.0924 0.0443 0.0546 0.0359 58 LYS B C 2982 O O . LYS B 58 ? 1.3064 0.9421 1.0864 0.0470 0.0511 0.0399 58 LYS B O 2983 C CB . LYS B 58 ? 1.2061 0.8428 1.0618 0.0037 0.0386 0.0276 58 LYS B CB 2984 C CG . LYS B 58 ? 1.2344 0.8103 1.0686 -0.0275 0.0304 0.0339 58 LYS B CG 2985 C CD . LYS B 58 ? 1.2725 0.8624 1.0852 -0.0713 0.0397 0.0572 58 LYS B CD 2986 C CE . LYS B 58 ? 1.3096 0.8316 1.0984 -0.1030 0.0258 0.0604 58 LYS B CE 2987 N NZ . LYS B 58 ? 1.3744 0.8839 1.1249 -0.1495 0.0285 0.0861 58 LYS B NZ 2988 N N . MET B 59 ? 1.2921 1.0160 1.1209 0.0789 0.0552 0.0244 59 MET B N 2989 C CA . MET B 59 ? 1.3430 1.0545 1.1415 0.1228 0.0501 0.0149 59 MET B CA 2990 C C . MET B 59 ? 1.4180 1.1980 1.1933 0.1343 0.0702 0.0299 59 MET B C 2991 O O . MET B 59 ? 1.4498 1.2346 1.1963 0.1781 0.0680 0.0216 59 MET B O 2992 C CB . MET B 59 ? 1.3201 1.0264 1.1311 0.1569 0.0354 -0.0054 59 MET B CB 2993 C CG . MET B 59 ? 1.2916 0.9514 1.1315 0.1436 0.0175 -0.0162 59 MET B CG 2994 S SD . MET B 59 ? 1.3143 0.8900 1.1373 0.1485 -0.0059 -0.0251 59 MET B SD 2995 C CE . MET B 59 ? 1.3719 0.9227 1.1503 0.1936 -0.0194 -0.0363 59 MET B CE 2996 N N . ASN B 60 ? 1.4732 1.3077 1.2581 0.0947 0.0881 0.0531 60 ASN B N 2997 C CA . ASN B 60 ? 1.5271 1.4478 1.2961 0.0973 0.1098 0.0740 60 ASN B CA 2998 C C . ASN B 60 ? 1.5855 1.4720 1.3064 0.1075 0.1121 0.0829 60 ASN B C 2999 O O . ASN B 60 ? 1.5768 1.4994 1.2706 0.1506 0.1189 0.0811 60 ASN B O 3000 C CB . ASN B 60 ? 1.5337 1.5164 1.3266 0.0390 0.1239 0.1004 60 ASN B CB 3001 C CG . ASN B 60 ? 1.5603 1.6636 1.3499 0.0389 0.1476 0.1250 60 ASN B CG 3002 O OD1 . ASN B 60 ? 1.5893 1.7093 1.3540 0.0104 0.1583 0.1514 60 ASN B OD1 3003 N ND2 . ASN B 60 ? 1.5472 1.7394 1.3594 0.0717 0.1556 0.1180 60 ASN B ND2 3004 N N . THR B 61 ? 1.1592 1.9955 1.1745 -0.1553 -0.2429 -0.2112 61 THR B N 3005 C CA . THR B 61 ? 1.1574 1.9000 1.1874 -0.1619 -0.2172 -0.2132 61 THR B CA 3006 C C . THR B 61 ? 1.1593 1.8178 1.1637 -0.1209 -0.2017 -0.1926 61 THR B C 3007 O O . THR B 61 ? 1.2099 1.8375 1.1729 -0.1218 -0.1990 -0.2061 61 THR B O 3008 C CB . THR B 61 ? 1.2325 1.9069 1.2416 -0.2167 -0.2121 -0.2541 61 THR B CB 3009 O OG1 . THR B 61 ? 1.2853 2.0396 1.3019 -0.2697 -0.2306 -0.2766 61 THR B OG1 3010 C CG2 . THR B 61 ? 1.2444 1.8293 1.2673 -0.2254 -0.1931 -0.2479 61 THR B CG2 3011 N N . GLN B 62 ? 1.1311 1.7638 1.1588 -0.0885 -0.1910 -0.1632 62 GLN B N 3012 C CA . GLN B 62 ? 1.1233 1.6831 1.1266 -0.0564 -0.1783 -0.1398 62 GLN B CA 3013 C C . GLN B 62 ? 1.1066 1.6284 1.1399 -0.0357 -0.1640 -0.1209 62 GLN B C 3014 O O . GLN B 62 ? 1.1468 1.7239 1.2184 -0.0311 -0.1679 -0.1185 62 GLN B O 3015 C CB . GLN B 62 ? 1.1358 1.7232 1.1035 -0.0292 -0.1973 -0.1111 62 GLN B CB 3016 C CG . GLN B 62 ? 1.1459 1.6642 1.0893 0.0020 -0.1917 -0.0748 62 GLN B CG 3017 C CD . GLN B 62 ? 1.2117 1.7345 1.1007 0.0189 -0.2164 -0.0410 62 GLN B CD 3018 O OE1 . GLN B 62 ? 1.2465 1.8303 1.1138 0.0076 -0.2356 -0.0452 62 GLN B OE1 3019 N NE2 . GLN B 62 ? 1.2428 1.6928 1.1006 0.0420 -0.2191 -0.0057 62 GLN B NE2 3020 N N . PHE B 63 ? 1.0550 1.4976 1.0708 -0.0248 -0.1473 -0.1109 63 PHE B N 3021 C CA . PHE B 63 ? 1.0463 1.4442 1.0824 -0.0113 -0.1322 -0.0978 63 PHE B CA 3022 C C . PHE B 63 ? 1.0394 1.4728 1.0950 0.0240 -0.1407 -0.0777 63 PHE B C 3023 O O . PHE B 63 ? 1.1047 1.5547 1.1405 0.0535 -0.1601 -0.0601 63 PHE B O 3024 C CB . PHE B 63 ? 1.0246 1.3488 1.0329 -0.0035 -0.1184 -0.0875 63 PHE B CB 3025 C CG . PHE B 63 ? 0.9990 1.2758 1.0227 0.0044 -0.1036 -0.0781 63 PHE B CG 3026 C CD1 . PHE B 63 ? 0.9618 1.2137 1.0034 -0.0159 -0.0934 -0.0933 63 PHE B CD1 3027 C CD2 . PHE B 63 ? 1.0368 1.2837 1.0475 0.0300 -0.1032 -0.0536 63 PHE B CD2 3028 C CE1 . PHE B 63 ? 0.9548 1.1690 1.0045 -0.0117 -0.0813 -0.0826 63 PHE B CE1 3029 C CE2 . PHE B 63 ? 0.9948 1.2027 1.0157 0.0350 -0.0896 -0.0491 63 PHE B CE2 3030 C CZ . PHE B 63 ? 0.9579 1.1577 1.0001 0.0137 -0.0778 -0.0628 63 PHE B CZ 3031 N N . GLU B 64 ? 0.9779 1.4220 1.0674 0.0227 -0.1282 -0.0820 64 GLU B N 3032 C CA . GLU B 64 ? 0.9770 1.4604 1.0887 0.0638 -0.1322 -0.0737 64 GLU B CA 3033 C C . GLU B 64 ? 0.9665 1.3866 1.0765 0.0713 -0.1117 -0.0683 64 GLU B C 3034 O O . GLU B 64 ? 0.9643 1.3685 1.0842 0.0354 -0.0941 -0.0762 64 GLU B O 3035 C CB . GLU B 64 ? 0.9625 1.5696 1.1237 0.0516 -0.1356 -0.0921 64 GLU B CB 3036 C CG . GLU B 64 ? 0.9804 1.6714 1.1474 0.0453 -0.1598 -0.0994 64 GLU B CG 3037 C CD . GLU B 64 ? 0.9652 1.8041 1.1864 0.0328 -0.1644 -0.1183 64 GLU B CD 3038 O OE1 . GLU B 64 ? 0.9187 1.8050 1.1733 0.0409 -0.1491 -0.1246 64 GLU B OE1 3039 O OE2 . GLU B 64 ? 0.9835 1.9040 1.2132 0.0113 -0.1829 -0.1290 64 GLU B OE2 3040 N N . ALA B 65 ? 1.0093 1.3845 1.0983 0.1164 -0.1177 -0.0543 65 ALA B N 3041 C CA . ALA B 65 ? 1.0143 1.3284 1.0945 0.1244 -0.1007 -0.0518 65 ALA B CA 3042 C C . ALA B 65 ? 1.0088 1.4006 1.1304 0.1384 -0.0896 -0.0699 65 ALA B C 3043 O O . ALA B 65 ? 0.9642 1.4517 1.1170 0.1673 -0.1014 -0.0818 65 ALA B O 3044 C CB . ALA B 65 ? 1.0643 1.2875 1.0945 0.1601 -0.1140 -0.0330 65 ALA B CB 3045 N N . VAL B 66 ? 1.0175 1.3817 1.1389 0.1174 -0.0676 -0.0731 66 VAL B N 3046 C CA . VAL B 66 ? 1.0275 1.4690 1.1791 0.1248 -0.0522 -0.0910 66 VAL B CA 3047 C C . VAL B 66 ? 1.0527 1.4195 1.1750 0.1471 -0.0416 -0.0911 66 VAL B C 3048 O O . VAL B 66 ? 1.0915 1.3599 1.1786 0.1272 -0.0386 -0.0756 66 VAL B O 3049 C CB . VAL B 66 ? 1.0075 1.5043 1.1802 0.0582 -0.0351 -0.0949 66 VAL B CB 3050 C CG1 . VAL B 66 ? 1.0177 1.6170 1.2176 0.0559 -0.0162 -0.1127 66 VAL B CG1 3051 C CG2 . VAL B 66 ? 1.0265 1.5816 1.2183 0.0265 -0.0477 -0.0979 66 VAL B CG2 3052 N N . GLY B 67 ? 1.0819 1.5061 1.2193 0.1894 -0.0366 -0.1131 67 GLY B N 3053 C CA . GLY B 67 ? 1.0882 1.4488 1.1947 0.2108 -0.0263 -0.1217 67 GLY B CA 3054 C C . GLY B 67 ? 1.0315 1.4004 1.1355 0.1537 -0.0002 -0.1191 67 GLY B C 3055 O O . GLY B 67 ? 0.9942 1.4663 1.1296 0.1179 0.0151 -0.1264 67 GLY B O 3056 N N . ARG B 68 ? 1.0070 1.2685 1.0684 0.1396 0.0022 -0.1061 68 ARG B N 3057 C CA . ARG B 68 ? 0.9644 1.2198 1.0131 0.0919 0.0206 -0.0997 68 ARG B CA 3058 C C . ARG B 68 ? 0.9865 1.1602 0.9912 0.1086 0.0225 -0.1050 68 ARG B C 3059 O O . ARG B 68 ? 1.0151 1.0959 0.9888 0.1231 0.0075 -0.0956 68 ARG B O 3060 C CB . ARG B 68 ? 0.9512 1.1634 0.9955 0.0420 0.0155 -0.0732 68 ARG B CB 3061 C CG . ARG B 68 ? 0.9567 1.2392 1.0326 0.0100 0.0147 -0.0712 68 ARG B CG 3062 C CD . ARG B 68 ? 0.9295 1.1537 0.9903 -0.0363 0.0079 -0.0515 68 ARG B CD 3063 N NE . ARG B 68 ? 0.9311 1.0922 0.9847 -0.0200 -0.0072 -0.0456 68 ARG B NE 3064 C CZ . ARG B 68 ? 0.9153 1.0966 0.9841 -0.0112 -0.0183 -0.0504 68 ARG B CZ 3065 N NH1 . ARG B 68 ? 0.9023 1.1656 0.9989 -0.0155 -0.0191 -0.0608 68 ARG B NH1 3066 N NH2 . ARG B 68 ? 0.9394 1.0719 0.9950 -0.0008 -0.0287 -0.0460 68 ARG B NH2 3067 N N . GLU B 69 ? 0.9941 1.2070 0.9904 0.0993 0.0410 -0.1204 69 GLU B N 3068 C CA . GLU B 69 ? 0.9823 1.1276 0.9333 0.1143 0.0433 -0.1334 69 GLU B CA 3069 C C . GLU B 69 ? 0.9049 1.0290 0.8308 0.0613 0.0519 -0.1155 69 GLU B C 3070 O O . GLU B 69 ? 0.8238 1.0026 0.7636 0.0196 0.0609 -0.1007 69 GLU B O 3071 C CB . GLU B 69 ? 1.0415 1.2519 0.9953 0.1610 0.0551 -0.1762 69 GLU B CB 3072 C CG . GLU B 69 ? 1.1153 1.2963 1.0707 0.2342 0.0351 -0.1968 69 GLU B CG 3073 C CD . GLU B 69 ? 1.1601 1.4628 1.1479 0.2895 0.0455 -0.2425 69 GLU B CD 3074 O OE1 . GLU B 69 ? 1.1279 1.5630 1.1722 0.2840 0.0525 -0.2444 69 GLU B OE1 3075 O OE2 . GLU B 69 ? 1.2508 1.5235 1.2068 0.3380 0.0463 -0.2804 69 GLU B OE2 3076 N N . PHE B 70 ? 0.9406 0.9796 0.8230 0.0610 0.0453 -0.1155 70 PHE B N 3077 C CA . PHE B 70 ? 0.9351 0.9500 0.7907 0.0167 0.0464 -0.0972 70 PHE B CA 3078 C C . PHE B 70 ? 0.9775 0.9500 0.7838 0.0226 0.0492 -0.1198 70 PHE B C 3079 O O . PHE B 70 ? 0.9820 0.8911 0.7635 0.0553 0.0408 -0.1400 70 PHE B O 3080 C CB . PHE B 70 ? 0.9101 0.8703 0.7679 -0.0017 0.0288 -0.0684 70 PHE B CB 3081 C CG . PHE B 70 ? 0.8701 0.8562 0.7681 -0.0029 0.0234 -0.0533 70 PHE B CG 3082 C CD1 . PHE B 70 ? 0.8753 0.8519 0.7891 0.0251 0.0157 -0.0579 70 PHE B CD1 3083 C CD2 . PHE B 70 ? 0.8439 0.8538 0.7549 -0.0332 0.0222 -0.0345 70 PHE B CD2 3084 C CE1 . PHE B 70 ? 0.8408 0.8458 0.7875 0.0210 0.0103 -0.0480 70 PHE B CE1 3085 C CE2 . PHE B 70 ? 0.8284 0.8502 0.7683 -0.0367 0.0152 -0.0261 70 PHE B CE2 3086 C CZ . PHE B 70 ? 0.8229 0.8496 0.7832 -0.0106 0.0109 -0.0348 70 PHE B CZ 3087 N N . ASN B 71 ? 0.9985 0.9959 0.7814 -0.0112 0.0575 -0.1159 71 ASN B N 3088 C CA . ASN B 71 ? 1.0753 1.0401 0.8065 -0.0110 0.0607 -0.1418 71 ASN B CA 3089 C C . ASN B 71 ? 1.1031 0.9854 0.8023 -0.0339 0.0412 -0.1269 71 ASN B C 3090 O O . ASN B 71 ? 1.0564 0.9175 0.7779 -0.0438 0.0275 -0.0995 71 ASN B O 3091 C CB . ASN B 71 ? 1.0952 1.1352 0.8069 -0.0394 0.0787 -0.1475 71 ASN B CB 3092 C CG . ASN B 71 ? 1.0843 1.1269 0.7857 -0.0896 0.0681 -0.1049 71 ASN B CG 3093 O OD1 . ASN B 71 ? 1.0902 1.0798 0.7722 -0.1035 0.0503 -0.0912 71 ASN B OD1 3094 N ND2 . ASN B 71 ? 1.0933 1.1991 0.8033 -0.1182 0.0764 -0.0837 71 ASN B ND2 3095 N N . ASN B 72 ? 1.1694 1.0170 0.8156 -0.0451 0.0407 -0.1488 72 ASN B N 3096 C CA . ASN B 72 ? 1.2156 0.9910 0.8247 -0.0729 0.0223 -0.1423 72 ASN B CA 3097 C C . ASN B 72 ? 1.1508 0.9645 0.7748 -0.1144 0.0108 -0.1060 72 ASN B C 3098 O O . ASN B 72 ? 1.1626 0.9461 0.7744 -0.1388 -0.0045 -0.0964 72 ASN B O 3099 C CB . ASN B 72 ? 1.3301 1.0550 0.8713 -0.0770 0.0232 -0.1814 72 ASN B CB 3100 C CG . ASN B 72 ? 1.4141 1.0496 0.9069 -0.1114 0.0025 -0.1798 72 ASN B CG 3101 O OD1 . ASN B 72 ? 1.4719 1.0562 0.9706 -0.1140 -0.0104 -0.1623 72 ASN B OD1 3102 N ND2 . ASN B 72 ? 1.4918 1.1148 0.9314 -0.1458 -0.0011 -0.1973 72 ASN B ND2 3103 N N . LEU B 73 ? 1.0882 0.9690 0.7337 -0.1230 0.0157 -0.0865 73 LEU B N 3104 C CA . LEU B 73 ? 1.0586 0.9693 0.7190 -0.1462 -0.0018 -0.0522 73 LEU B CA 3105 C C . LEU B 73 ? 1.0196 0.9492 0.7306 -0.1312 -0.0056 -0.0262 73 LEU B C 3106 O O . LEU B 73 ? 1.0126 0.9628 0.7301 -0.1399 -0.0190 0.0004 73 LEU B O 3107 C CB . LEU B 73 ? 1.1055 1.0526 0.7294 -0.1717 -0.0039 -0.0452 73 LEU B CB 3108 C CG . LEU B 73 ? 1.1755 1.1098 0.7442 -0.1950 -0.0061 -0.0700 73 LEU B CG 3109 C CD1 . LEU B 73 ? 1.1818 1.1620 0.7100 -0.2188 -0.0049 -0.0639 73 LEU B CD1 3110 C CD2 . LEU B 73 ? 1.1643 1.0903 0.7338 -0.2154 -0.0286 -0.0618 73 LEU B CD2 3111 N N . GLU B 74 ? 0.9833 0.8967 0.7228 -0.1073 0.0023 -0.0349 74 GLU B N 3112 C CA . GLU B 74 ? 0.9283 0.8518 0.7120 -0.0951 -0.0031 -0.0168 74 GLU B CA 3113 C C . GLU B 74 ? 0.9220 0.8199 0.7218 -0.0827 -0.0086 -0.0215 74 GLU B C 3114 O O . GLU B 74 ? 0.8513 0.7497 0.6793 -0.0649 -0.0062 -0.0211 74 GLU B O 3115 C CB . GLU B 74 ? 0.9113 0.8609 0.7121 -0.0862 0.0123 -0.0213 74 GLU B CB 3116 C CG . GLU B 74 ? 0.9209 0.9045 0.7000 -0.1123 0.0184 -0.0103 74 GLU B CG 3117 C CD . GLU B 74 ? 0.9350 0.9694 0.7307 -0.1138 0.0375 -0.0193 74 GLU B CD 3118 O OE1 . GLU B 74 ? 0.9528 1.0085 0.7632 -0.0852 0.0513 -0.0490 74 GLU B OE1 3119 O OE2 . GLU B 74 ? 0.9474 1.0012 0.7380 -0.1445 0.0360 0.0032 74 GLU B OE2 3120 N N . ARG B 75 ? 0.9659 0.8464 0.7417 -0.0996 -0.0167 -0.0251 75 ARG B N 3121 C CA . ARG B 75 ? 0.9653 0.8188 0.7382 -0.1035 -0.0216 -0.0267 75 ARG B CA 3122 C C . ARG B 75 ? 0.9115 0.8058 0.7272 -0.0973 -0.0284 -0.0132 75 ARG B C 3123 O O . ARG B 75 ? 0.9303 0.8123 0.7531 -0.0912 -0.0277 -0.0126 75 ARG B O 3124 C CB . ARG B 75 ? 1.0806 0.9138 0.8101 -0.1400 -0.0294 -0.0321 75 ARG B CB 3125 C CG . ARG B 75 ? 1.2125 0.9567 0.8834 -0.1469 -0.0288 -0.0500 75 ARG B CG 3126 C CD . ARG B 75 ? 1.3089 1.0173 0.9766 -0.1031 -0.0185 -0.0676 75 ARG B CD 3127 N NE . ARG B 75 ? 1.5169 1.1296 1.1207 -0.0983 -0.0232 -0.0920 75 ARG B NE 3128 C CZ . ARG B 75 ? 1.6302 1.2012 1.2233 -0.0502 -0.0200 -0.1145 75 ARG B CZ 3129 N NH1 . ARG B 75 ? 1.6014 1.2353 1.2484 -0.0110 -0.0094 -0.1139 75 ARG B NH1 3130 N NH2 . ARG B 75 ? 1.7274 1.1937 1.2529 -0.0400 -0.0300 -0.1406 75 ARG B NH2 3131 N N . ARG B 76 ? 0.8929 0.8326 0.7319 -0.0950 -0.0376 -0.0040 76 ARG B N 3132 C CA . ARG B 76 ? 0.8311 0.8093 0.7088 -0.0792 -0.0461 -0.0002 76 ARG B CA 3133 C C . ARG B 76 ? 0.8155 0.7756 0.7154 -0.0572 -0.0404 -0.0006 76 ARG B C 3134 O O . ARG B 76 ? 0.7866 0.7579 0.7013 -0.0515 -0.0391 -0.0052 76 ARG B O 3135 C CB . ARG B 76 ? 0.8224 0.8363 0.7138 -0.0679 -0.0638 0.0069 76 ARG B CB 3136 C CG . ARG B 76 ? 0.8280 0.8920 0.7097 -0.0875 -0.0739 0.0050 76 ARG B CG 3137 C CD . ARG B 76 ? 0.8509 0.9430 0.7407 -0.0662 -0.0975 0.0148 76 ARG B CD 3138 N NE . ARG B 76 ? 0.8736 0.9117 0.7312 -0.0708 -0.0983 0.0301 76 ARG B NE 3139 C CZ . ARG B 76 ? 0.8808 0.8998 0.7297 -0.0527 -0.1197 0.0482 76 ARG B CZ 3140 N NH1 . ARG B 76 ? 0.9034 0.9426 0.7763 -0.0155 -0.1461 0.0495 76 ARG B NH1 3141 N NH2 . ARG B 76 ? 0.8954 0.8729 0.7058 -0.0714 -0.1161 0.0642 76 ARG B NH2 3142 N N . ILE B 77 ? 0.8263 0.7670 0.7247 -0.0522 -0.0373 0.0043 77 ILE B N 3143 C CA . ILE B 77 ? 0.8442 0.7784 0.7624 -0.0410 -0.0330 0.0029 77 ILE B CA 3144 C C . ILE B 77 ? 0.8510 0.7803 0.7693 -0.0345 -0.0212 -0.0067 77 ILE B C 3145 O O . ILE B 77 ? 0.8235 0.7612 0.7616 -0.0243 -0.0218 -0.0098 77 ILE B O 3146 C CB . ILE B 77 ? 0.8894 0.8142 0.8004 -0.0511 -0.0325 0.0126 77 ILE B CB 3147 C CG1 . ILE B 77 ? 0.9754 0.9099 0.8636 -0.0638 -0.0167 0.0089 77 ILE B CG1 3148 C CG2 . ILE B 77 ? 0.9279 0.8339 0.8282 -0.0519 -0.0534 0.0276 77 ILE B CG2 3149 C CD1 . ILE B 77 ? 1.0468 0.9922 0.9232 -0.0862 -0.0123 0.0197 77 ILE B CD1 3150 N N . GLU B 78 ? 0.8593 0.7693 0.7506 -0.0371 -0.0145 -0.0131 78 GLU B N 3151 C CA . GLU B 78 ? 0.8697 0.7562 0.7512 -0.0211 -0.0119 -0.0216 78 GLU B CA 3152 C C . GLU B 78 ? 0.8461 0.7243 0.7260 -0.0260 -0.0207 -0.0144 78 GLU B C 3153 O O . GLU B 78 ? 0.8292 0.7062 0.7162 -0.0112 -0.0237 -0.0138 78 GLU B O 3154 C CB . GLU B 78 ? 0.9550 0.7977 0.7941 -0.0200 -0.0092 -0.0335 78 GLU B CB 3155 C CG . GLU B 78 ? 1.0507 0.8422 0.8659 0.0054 -0.0151 -0.0420 78 GLU B CG 3156 C CD . GLU B 78 ? 1.2279 0.9531 0.9902 0.0111 -0.0169 -0.0598 78 GLU B CD 3157 O OE1 . GLU B 78 ? 1.3107 1.0092 1.0405 -0.0228 -0.0192 -0.0581 78 GLU B OE1 3158 O OE2 . GLU B 78 ? 1.3621 1.0645 1.1140 0.0521 -0.0180 -0.0795 78 GLU B OE2 3159 N N . ASN B 79 ? 0.8083 0.6953 0.6785 -0.0493 -0.0252 -0.0093 79 ASN B N 3160 C CA . ASN B 79 ? 0.8475 0.7466 0.7108 -0.0649 -0.0302 -0.0037 79 ASN B CA 3161 C C . ASN B 79 ? 0.8068 0.7558 0.7100 -0.0497 -0.0309 -0.0069 79 ASN B C 3162 O O . ASN B 79 ? 0.7963 0.7538 0.6952 -0.0516 -0.0325 -0.0048 79 ASN B O 3163 C CB . ASN B 79 ? 0.9120 0.8369 0.7602 -0.0982 -0.0331 -0.0022 79 ASN B CB 3164 C CG . ASN B 79 ? 0.9611 0.9258 0.8020 -0.1250 -0.0347 0.0022 79 ASN B CG 3165 O OD1 . ASN B 79 ? 1.0742 0.9917 0.8691 -0.1507 -0.0376 0.0126 79 ASN B OD1 3166 N ND2 . ASN B 79 ? 0.9579 1.0091 0.8386 -0.1189 -0.0346 -0.0065 79 ASN B ND2 3167 N N . LEU B 80 ? 0.7933 0.7652 0.7263 -0.0360 -0.0326 -0.0119 80 LEU B N 3168 C CA . LEU B 80 ? 0.7723 0.7697 0.7348 -0.0189 -0.0370 -0.0203 80 LEU B CA 3169 C C . LEU B 80 ? 0.7530 0.7374 0.7190 -0.0116 -0.0341 -0.0211 80 LEU B C 3170 O O . LEU B 80 ? 0.7690 0.7754 0.7415 -0.0080 -0.0362 -0.0274 80 LEU B O 3171 C CB . LEU B 80 ? 0.7962 0.7829 0.7711 -0.0078 -0.0455 -0.0207 80 LEU B CB 3172 C CG . LEU B 80 ? 0.8244 0.8135 0.8178 0.0127 -0.0577 -0.0334 80 LEU B CG 3173 C CD1 . LEU B 80 ? 0.8586 0.8124 0.8451 0.0221 -0.0741 -0.0265 80 LEU B CD1 3174 C CD2 . LEU B 80 ? 0.8814 0.8545 0.8801 0.0109 -0.0553 -0.0386 80 LEU B CD2 3175 N N . ASN B 81 ? 0.7851 0.7476 0.7468 -0.0090 -0.0295 -0.0172 81 ASN B N 3176 C CA . ASN B 81 ? 0.7524 0.7227 0.7229 0.0021 -0.0284 -0.0201 81 ASN B CA 3177 C C . ASN B 81 ? 0.7942 0.7554 0.7454 0.0089 -0.0338 -0.0158 81 ASN B C 3178 O O . ASN B 81 ? 0.7670 0.7498 0.7280 0.0174 -0.0392 -0.0179 81 ASN B O 3179 C CB . ASN B 81 ? 0.7527 0.7221 0.7215 0.0078 -0.0206 -0.0222 81 ASN B CB 3180 C CG . ASN B 81 ? 0.7576 0.7626 0.7449 0.0244 -0.0206 -0.0296 81 ASN B CG 3181 O OD1 . ASN B 81 ? 0.7666 0.8066 0.7775 0.0148 -0.0221 -0.0328 81 ASN B OD1 3182 N ND2 . ASN B 81 ? 0.7732 0.7683 0.7470 0.0509 -0.0220 -0.0346 81 ASN B ND2 3183 N N . LYS B 82 ? 0.8511 0.7748 0.7668 -0.0001 -0.0352 -0.0077 82 LYS B N 3184 C CA . LYS B 82 ? 0.9293 0.8197 0.8069 -0.0022 -0.0451 0.0038 82 LYS B CA 3185 C C . LYS B 82 ? 0.9164 0.8476 0.7945 -0.0213 -0.0467 0.0072 82 LYS B C 3186 O O . LYS B 82 ? 0.8858 0.8202 0.7511 -0.0165 -0.0554 0.0140 82 LYS B O 3187 C CB . LYS B 82 ? 1.0377 0.8615 0.8638 -0.0197 -0.0486 0.0120 82 LYS B CB 3188 C CG . LYS B 82 ? 1.1955 0.9515 0.9615 -0.0269 -0.0652 0.0300 82 LYS B CG 3189 C CD . LYS B 82 ? 1.3621 1.0390 1.0661 -0.0593 -0.0708 0.0376 82 LYS B CD 3190 C CE . LYS B 82 ? 1.5008 1.1244 1.1355 -0.1007 -0.0859 0.0638 82 LYS B CE 3191 N NZ . LYS B 82 ? 1.5897 1.1584 1.1674 -0.1548 -0.0883 0.0703 82 LYS B NZ 3192 N N . LYS B 83 ? 0.8857 0.8577 0.7782 -0.0394 -0.0397 0.0001 83 LYS B N 3193 C CA . LYS B 83 ? 0.8855 0.9190 0.7834 -0.0527 -0.0380 -0.0066 83 LYS B CA 3194 C C . LYS B 83 ? 0.8167 0.8816 0.7448 -0.0306 -0.0399 -0.0222 83 LYS B C 3195 O O . LYS B 83 ? 0.8137 0.9146 0.7310 -0.0381 -0.0414 -0.0254 83 LYS B O 3196 C CB . LYS B 83 ? 0.9218 1.0102 0.8380 -0.0634 -0.0321 -0.0190 83 LYS B CB 3197 C CG . LYS B 83 ? 1.0402 1.1499 0.9195 -0.1076 -0.0295 -0.0072 83 LYS B CG 3198 C CD . LYS B 83 ? 1.1637 1.1803 0.9925 -0.1285 -0.0353 0.0149 83 LYS B CD 3199 C CE . LYS B 83 ? 1.2592 1.2809 1.0363 -0.1880 -0.0361 0.0296 83 LYS B CE 3200 N NZ . LYS B 83 ? 1.3065 1.3447 1.0450 -0.2186 -0.0381 0.0444 83 LYS B NZ 3201 N N . MET B 84 ? 0.7844 0.8354 0.7425 -0.0109 -0.0406 -0.0315 84 MET B N 3202 C CA . MET B 84 ? 0.7468 0.8153 0.7260 0.0002 -0.0450 -0.0464 84 MET B CA 3203 C C . MET B 84 ? 0.7141 0.7860 0.6815 0.0032 -0.0516 -0.0371 84 MET B C 3204 O O . MET B 84 ? 0.7491 0.8538 0.7130 0.0008 -0.0565 -0.0456 84 MET B O 3205 C CB . MET B 84 ? 0.7711 0.8160 0.7723 0.0058 -0.0461 -0.0521 84 MET B CB 3206 C CG . MET B 84 ? 0.8136 0.8635 0.8280 0.0062 -0.0535 -0.0713 84 MET B CG 3207 S SD . MET B 84 ? 0.8974 0.9383 0.9238 -0.0086 -0.0552 -0.0665 84 MET B SD 3208 C CE . MET B 84 ? 0.9007 0.9869 0.9298 0.0008 -0.0540 -0.0571 84 MET B CE 3209 N N . GLU B 85 ? 1.0011 1.1281 0.8189 0.0718 -0.0072 -0.0690 85 GLU B N 3210 C CA . GLU B 85 ? 0.9699 1.1072 0.7963 0.0795 -0.0052 -0.0815 85 GLU B CA 3211 C C . GLU B 85 ? 0.9344 1.0354 0.7737 0.0733 -0.0210 -0.0858 85 GLU B C 3212 O O . GLU B 85 ? 0.9005 1.0063 0.7621 0.0672 -0.0141 -0.0837 85 GLU B O 3213 C CB . GLU B 85 ? 1.0286 1.1828 0.8254 0.1094 -0.0103 -0.1013 85 GLU B CB 3214 C CG . GLU B 85 ? 1.0770 1.2830 0.8611 0.1145 0.0060 -0.0961 85 GLU B CG 3215 C CD . GLU B 85 ? 1.1048 1.3852 0.8941 0.1222 0.0233 -0.0980 85 GLU B CD 3216 O OE1 . GLU B 85 ? 1.1404 1.4501 0.9082 0.1606 0.0180 -0.1175 85 GLU B OE1 3217 O OE2 . GLU B 85 ? 1.1024 1.4152 0.9089 0.0906 0.0408 -0.0795 85 GLU B OE2 3218 N N . ASP B 86 ? 0.9344 1.0016 0.7565 0.0690 -0.0430 -0.0898 86 ASP B N 3219 C CA . ASP B 86 ? 0.9263 0.9599 0.7521 0.0528 -0.0612 -0.0901 86 ASP B CA 3220 C C . ASP B 86 ? 0.8565 0.9102 0.7218 0.0342 -0.0518 -0.0715 86 ASP B C 3221 O O . ASP B 86 ? 0.8384 0.8799 0.7182 0.0262 -0.0552 -0.0715 86 ASP B O 3222 C CB . ASP B 86 ? 0.9918 0.9933 0.7833 0.0377 -0.0887 -0.0929 86 ASP B CB 3223 C CG . ASP B 86 ? 1.0863 1.0207 0.8205 0.0486 -0.1128 -0.1139 86 ASP B CG 3224 O OD1 . ASP B 86 ? 1.1458 1.0482 0.8740 0.0530 -0.1179 -0.1206 86 ASP B OD1 3225 O OD2 . ASP B 86 ? 1.1564 1.0623 0.8431 0.0557 -0.1283 -0.1242 86 ASP B OD2 3226 N N . GLY B 87 ? 0.8194 0.8999 0.6936 0.0325 -0.0418 -0.0564 87 GLY B N 3227 C CA . GLY B 87 ? 0.7902 0.8861 0.6870 0.0275 -0.0336 -0.0399 87 GLY B CA 3228 C C . GLY B 87 ? 0.7753 0.8613 0.6879 0.0275 -0.0183 -0.0391 87 GLY B C 3229 O O . GLY B 87 ? 0.7553 0.8406 0.6868 0.0210 -0.0200 -0.0340 87 GLY B O 3230 N N . PHE B 88 ? 0.7657 0.8523 0.6690 0.0314 -0.0040 -0.0430 88 PHE B N 3231 C CA . PHE B 88 ? 0.7515 0.8380 0.6651 0.0234 0.0096 -0.0407 88 PHE B CA 3232 C C . PHE B 88 ? 0.7508 0.8396 0.6840 0.0247 0.0025 -0.0538 88 PHE B C 3233 O O . PHE B 88 ? 0.7262 0.8102 0.6766 0.0167 0.0063 -0.0497 88 PHE B O 3234 C CB . PHE B 88 ? 0.7665 0.8710 0.6616 0.0173 0.0249 -0.0383 88 PHE B CB 3235 C CG . PHE B 88 ? 0.7962 0.8750 0.6585 0.0091 0.0332 -0.0207 88 PHE B CG 3236 C CD1 . PHE B 88 ? 0.8105 0.8488 0.6571 0.0013 0.0366 -0.0078 88 PHE B CD1 3237 C CD2 . PHE B 88 ? 0.8264 0.9111 0.6620 0.0129 0.0358 -0.0177 88 PHE B CD2 3238 C CE1 . PHE B 88 ? 0.8511 0.8427 0.6454 0.0000 0.0405 0.0075 88 PHE B CE1 3239 C CE2 . PHE B 88 ? 0.8694 0.9156 0.6606 0.0077 0.0412 -0.0010 88 PHE B CE2 3240 C CZ . PHE B 88 ? 0.8944 0.8876 0.6596 0.0025 0.0426 0.0114 88 PHE B CZ 3241 N N . LEU B 89 ? 0.7875 0.8741 0.7081 0.0384 -0.0097 -0.0699 89 LEU B N 3242 C CA . LEU B 89 ? 0.8131 0.8832 0.7338 0.0469 -0.0210 -0.0832 89 LEU B CA 3243 C C . LEU B 89 ? 0.7889 0.8325 0.7243 0.0296 -0.0325 -0.0755 89 LEU B C 3244 O O . LEU B 89 ? 0.7566 0.7960 0.7064 0.0282 -0.0314 -0.0770 89 LEU B O 3245 C CB . LEU B 89 ? 0.8959 0.9385 0.7756 0.0693 -0.0394 -0.1020 89 LEU B CB 3246 C CG . LEU B 89 ? 0.9716 1.0491 0.8296 0.0975 -0.0311 -0.1138 89 LEU B CG 3247 C CD1 . LEU B 89 ? 1.0447 1.0693 0.8452 0.1254 -0.0557 -0.1341 89 LEU B CD1 3248 C CD2 . LEU B 89 ? 0.9575 1.0974 0.8333 0.1101 -0.0128 -0.1166 89 LEU B CD2 3249 N N . ASP B 90 ? 0.7878 0.8249 0.7191 0.0160 -0.0437 -0.0662 90 ASP B N 3250 C CA . ASP B 90 ? 0.7894 0.8243 0.7345 -0.0038 -0.0547 -0.0555 90 ASP B CA 3251 C C . ASP B 90 ? 0.7485 0.8067 0.7248 -0.0037 -0.0375 -0.0429 90 ASP B C 3252 O O . ASP B 90 ? 0.7549 0.8116 0.7464 -0.0126 -0.0415 -0.0390 90 ASP B O 3253 C CB . ASP B 90 ? 0.8045 0.8570 0.7400 -0.0199 -0.0689 -0.0453 90 ASP B CB 3254 C CG . ASP B 90 ? 0.8857 0.8980 0.7777 -0.0309 -0.0937 -0.0566 90 ASP B CG 3255 O OD1 . ASP B 90 ? 0.9232 0.8819 0.7855 -0.0219 -0.1032 -0.0727 90 ASP B OD1 3256 O OD2 . ASP B 90 ? 0.9325 0.9638 0.8116 -0.0464 -0.1055 -0.0496 90 ASP B OD2 3257 N N . VAL B 91 ? 0.7397 0.8098 0.7150 0.0060 -0.0205 -0.0362 91 VAL B N 3258 C CA . VAL B 91 ? 0.7232 0.7920 0.7060 0.0085 -0.0071 -0.0256 91 VAL B CA 3259 C C . VAL B 91 ? 0.7044 0.7639 0.7004 0.0026 -0.0004 -0.0327 91 VAL B C 3260 O O . VAL B 91 ? 0.7134 0.7693 0.7230 -0.0003 0.0004 -0.0280 91 VAL B O 3261 C CB . VAL B 91 ? 0.7354 0.7925 0.6902 0.0168 0.0057 -0.0173 91 VAL B CB 3262 C CG1 . VAL B 91 ? 0.7465 0.7742 0.6866 0.0157 0.0164 -0.0092 91 VAL B CG1 3263 C CG2 . VAL B 91 ? 0.7434 0.8161 0.6840 0.0311 -0.0005 -0.0081 91 VAL B CG2 3264 N N . TRP B 92 ? 0.6872 0.7536 0.6784 0.0036 0.0044 -0.0437 92 TRP B N 3265 C CA . TRP B 92 ? 0.6824 0.7600 0.6858 0.0003 0.0110 -0.0500 92 TRP B CA 3266 C C . TRP B 92 ? 0.6799 0.7479 0.6949 0.0071 -0.0024 -0.0601 92 TRP B C 3267 O O . TRP B 92 ? 0.6849 0.7575 0.7147 0.0042 0.0012 -0.0609 92 TRP B O 3268 C CB . TRP B 92 ? 0.6844 0.7976 0.6778 0.0024 0.0208 -0.0569 92 TRP B CB 3269 C CG . TRP B 92 ? 0.7089 0.8232 0.6838 -0.0174 0.0342 -0.0429 92 TRP B CG 3270 C CD1 . TRP B 92 ? 0.7369 0.8523 0.6878 -0.0186 0.0379 -0.0380 92 TRP B CD1 3271 C CD2 . TRP B 92 ? 0.7189 0.8172 0.6835 -0.0417 0.0427 -0.0309 92 TRP B CD2 3272 N NE1 . TRP B 92 ? 0.7591 0.8551 0.6807 -0.0436 0.0477 -0.0227 92 TRP B NE1 3273 C CE2 . TRP B 92 ? 0.7557 0.8357 0.6807 -0.0594 0.0496 -0.0184 92 TRP B CE2 3274 C CE3 . TRP B 92 ? 0.7122 0.8018 0.6888 -0.0517 0.0433 -0.0295 92 TRP B CE3 3275 C CZ2 . TRP B 92 ? 0.8048 0.8450 0.6908 -0.0898 0.0545 -0.0042 92 TRP B CZ2 3276 C CZ3 . TRP B 92 ? 0.7491 0.8079 0.6941 -0.0799 0.0493 -0.0168 92 TRP B CZ3 3277 C CH2 . TRP B 92 ? 0.7966 0.8246 0.6914 -0.1003 0.0536 -0.0041 92 TRP B CH2 3278 N N . THR B 93 ? 0.7023 0.7487 0.7014 0.0131 -0.0198 -0.0669 93 THR B N 3279 C CA . THR B 93 ? 0.7165 0.7313 0.7073 0.0134 -0.0373 -0.0735 93 THR B CA 3280 C C . THR B 93 ? 0.6962 0.7132 0.7111 -0.0057 -0.0382 -0.0587 93 THR B C 3281 O O . THR B 93 ? 0.7089 0.7162 0.7319 -0.0068 -0.0407 -0.0605 93 THR B O 3282 C CB . THR B 93 ? 0.7668 0.7391 0.7164 0.0131 -0.0609 -0.0808 93 THR B CB 3283 O OG1 . THR B 93 ? 0.7958 0.7635 0.7153 0.0413 -0.0612 -0.0976 93 THR B OG1 3284 C CG2 . THR B 93 ? 0.8099 0.7292 0.7332 0.0035 -0.0834 -0.0836 93 THR B CG2 3285 N N . TYR B 94 ? 0.6714 0.7077 0.6944 -0.0152 -0.0357 -0.0444 94 TYR B N 3286 C CA . TYR B 94 ? 0.6477 0.7037 0.6897 -0.0246 -0.0359 -0.0296 94 TYR B CA 3287 C C . TYR B 94 ? 0.6309 0.6873 0.6886 -0.0172 -0.0201 -0.0284 94 TYR B C 3288 O O . TYR B 94 ? 0.6215 0.6778 0.6926 -0.0222 -0.0230 -0.0260 94 TYR B O 3289 C CB . TYR B 94 ? 0.6385 0.7288 0.6787 -0.0222 -0.0347 -0.0159 94 TYR B CB 3290 C CG . TYR B 94 ? 0.6086 0.7346 0.6625 -0.0166 -0.0310 -0.0010 94 TYR B CG 3291 C CD1 . TYR B 94 ? 0.6076 0.7221 0.6554 0.0051 -0.0153 0.0022 94 TYR B CD1 3292 C CD2 . TYR B 94 ? 0.5924 0.7634 0.6556 -0.0335 -0.0449 0.0106 94 TYR B CD2 3293 C CE1 . TYR B 94 ? 0.5910 0.7331 0.6398 0.0213 -0.0132 0.0137 94 TYR B CE1 3294 C CE2 . TYR B 94 ? 0.5727 0.7942 0.6476 -0.0212 -0.0407 0.0243 94 TYR B CE2 3295 C CZ . TYR B 94 ? 0.5770 0.7813 0.6435 0.0121 -0.0246 0.0243 94 TYR B CZ 3296 O OH . TYR B 94 ? 0.5794 0.8279 0.6459 0.0352 -0.0215 0.0357 94 TYR B OH 3297 N N . ASN B 95 ? 0.6595 0.7122 0.7087 -0.0100 -0.0052 -0.0289 95 ASN B N 3298 C CA . ASN B 95 ? 0.6620 0.7052 0.7121 -0.0119 0.0071 -0.0272 95 ASN B CA 3299 C C . ASN B 95 ? 0.6559 0.7040 0.7239 -0.0160 0.0055 -0.0371 95 ASN B C 3300 O O . ASN B 95 ? 0.6681 0.7123 0.7465 -0.0187 0.0070 -0.0337 95 ASN B O 3301 C CB . ASN B 95 ? 0.6899 0.7229 0.7148 -0.0170 0.0191 -0.0258 95 ASN B CB 3302 C CG . ASN B 95 ? 0.7468 0.7581 0.7400 -0.0074 0.0209 -0.0144 95 ASN B CG 3303 O OD1 . ASN B 95 ? 0.7592 0.7755 0.7527 0.0083 0.0152 -0.0074 95 ASN B OD1 3304 N ND2 . ASN B 95 ? 0.8014 0.7944 0.7621 -0.0156 0.0283 -0.0115 95 ASN B ND2 3305 N N . ALA B 96 ? 0.6616 0.7185 0.7274 -0.0104 0.0014 -0.0500 96 ALA B N 3306 C CA . ALA B 96 ? 0.6548 0.7203 0.7283 -0.0033 -0.0010 -0.0611 96 ALA B CA 3307 C C . ALA B 96 ? 0.6351 0.6750 0.7134 -0.0039 -0.0150 -0.0602 96 ALA B C 3308 O O . ALA B 96 ? 0.6059 0.6500 0.6973 -0.0044 -0.0126 -0.0607 96 ALA B O 3309 C CB . ALA B 96 ? 0.6756 0.7553 0.7316 0.0168 -0.0048 -0.0765 96 ALA B CB 3310 N N . GLU B 97 ? 0.6457 0.6611 0.7093 -0.0092 -0.0308 -0.0572 97 GLU B N 3311 C CA . GLU B 97 ? 0.6759 0.6649 0.7327 -0.0200 -0.0474 -0.0534 97 GLU B CA 3312 C C . GLU B 97 ? 0.6361 0.6502 0.7210 -0.0324 -0.0409 -0.0380 97 GLU B C 3313 O O . GLU B 97 ? 0.6399 0.6462 0.7304 -0.0363 -0.0452 -0.0366 97 GLU B O 3314 C CB . GLU B 97 ? 0.7302 0.6872 0.7531 -0.0351 -0.0693 -0.0512 97 GLU B CB 3315 C CG . GLU B 97 ? 0.8026 0.7115 0.7787 -0.0153 -0.0820 -0.0698 97 GLU B CG 3316 C CD . GLU B 97 ? 0.8860 0.7472 0.8135 -0.0342 -0.1067 -0.0687 97 GLU B CD 3317 O OE1 . GLU B 97 ? 0.9271 0.8122 0.8656 -0.0675 -0.1123 -0.0516 97 GLU B OE1 3318 O OE2 . GLU B 97 ? 0.9671 0.7693 0.8385 -0.0140 -0.1221 -0.0852 97 GLU B OE2 3319 N N . LEU B 98 ? 0.6233 0.6657 0.7188 -0.0325 -0.0309 -0.0273 98 LEU B N 3320 C CA . LEU B 98 ? 0.5970 0.6647 0.7075 -0.0318 -0.0250 -0.0140 98 LEU B CA 3321 C C . LEU B 98 ? 0.5797 0.6365 0.6981 -0.0238 -0.0126 -0.0186 98 LEU B C 3322 O O . LEU B 98 ? 0.5625 0.6265 0.6915 -0.0243 -0.0132 -0.0134 98 LEU B O 3323 C CB . LEU B 98 ? 0.6147 0.7058 0.7176 -0.0202 -0.0183 -0.0043 98 LEU B CB 3324 C CG . LEU B 98 ? 0.6215 0.7456 0.7273 -0.0061 -0.0147 0.0092 98 LEU B CG 3325 C CD1 . LEU B 98 ? 0.6189 0.7953 0.7390 -0.0242 -0.0288 0.0214 98 LEU B CD1 3326 C CD2 . LEU B 98 ? 0.6348 0.7642 0.7151 0.0205 -0.0073 0.0151 98 LEU B CD2 3327 N N . LEU B 99 ? 0.5983 0.6434 0.7091 -0.0207 -0.0024 -0.0271 99 LEU B N 3328 C CA . LEU B 99 ? 0.6140 0.6535 0.7262 -0.0233 0.0071 -0.0302 99 LEU B CA 3329 C C . LEU B 99 ? 0.6038 0.6493 0.7335 -0.0235 0.0012 -0.0371 99 LEU B C 3330 O O . LEU B 99 ? 0.6090 0.6533 0.7459 -0.0249 0.0039 -0.0344 99 LEU B O 3331 C CB . LEU B 99 ? 0.6501 0.6935 0.7491 -0.0310 0.0163 -0.0361 99 LEU B CB 3332 C CG . LEU B 99 ? 0.6946 0.7392 0.7863 -0.0469 0.0246 -0.0365 99 LEU B CG 3333 C CD1 . LEU B 99 ? 0.7306 0.7307 0.7939 -0.0493 0.0264 -0.0262 99 LEU B CD1 3334 C CD2 . LEU B 99 ? 0.7422 0.8106 0.8194 -0.0641 0.0320 -0.0386 99 LEU B CD2 3335 N N . VAL B 100 ? 0.6039 0.6473 0.7308 -0.0181 -0.0084 -0.0466 100 VAL B N 3336 C CA . VAL B 100 ? 0.5843 0.6196 0.7120 -0.0110 -0.0172 -0.0541 100 VAL B CA 3337 C C . VAL B 100 ? 0.5621 0.5833 0.6945 -0.0211 -0.0269 -0.0431 100 VAL B C 3338 O O . VAL B 100 ? 0.5264 0.5493 0.6683 -0.0194 -0.0262 -0.0434 100 VAL B O 3339 C CB . VAL B 100 ? 0.6049 0.6214 0.7054 0.0061 -0.0294 -0.0679 100 VAL B CB 3340 C CG1 . VAL B 100 ? 0.6357 0.6168 0.7154 0.0173 -0.0452 -0.0738 100 VAL B CG1 3341 C CG2 . VAL B 100 ? 0.6000 0.6586 0.7019 0.0211 -0.0173 -0.0791 100 VAL B CG2 3342 N N . LEU B 101 ? 0.5583 0.5756 0.6833 -0.0339 -0.0364 -0.0323 101 LEU B N 3343 C CA . LEU B 101 ? 0.5544 0.5839 0.6853 -0.0498 -0.0444 -0.0169 101 LEU B CA 3344 C C . LEU B 101 ? 0.5471 0.6069 0.7004 -0.0412 -0.0302 -0.0099 101 LEU B C 3345 O O . LEU B 101 ? 0.5924 0.6551 0.7533 -0.0437 -0.0323 -0.0064 101 LEU B O 3346 C CB . LEU B 101 ? 0.5617 0.6129 0.6849 -0.0671 -0.0534 -0.0039 101 LEU B CB 3347 C CG . LEU B 101 ? 0.6169 0.6392 0.7076 -0.0970 -0.0780 0.0014 101 LEU B CG 3348 C CD1 . LEU B 101 ? 0.6766 0.6222 0.7282 -0.0889 -0.0909 -0.0158 101 LEU B CD1 3349 C CD2 . LEU B 101 ? 0.6180 0.6646 0.6994 -0.1119 -0.0844 0.0091 101 LEU B CD2 3350 N N . MET B 102 ? 0.5302 0.6022 0.6834 -0.0292 -0.0177 -0.0080 102 MET B N 3351 C CA . MET B 102 ? 0.5353 0.6158 0.6880 -0.0153 -0.0079 -0.0024 102 MET B CA 3352 C C . MET B 102 ? 0.5368 0.5957 0.6929 -0.0155 -0.0024 -0.0117 102 MET B C 3353 O O . MET B 102 ? 0.5467 0.6120 0.7074 -0.0108 -0.0019 -0.0075 102 MET B O 3354 C CB . MET B 102 ? 0.5802 0.6515 0.7087 0.0010 0.0005 0.0000 102 MET B CB 3355 C CG . MET B 102 ? 0.6210 0.7314 0.7466 0.0084 -0.0043 0.0112 102 MET B CG 3356 S SD . MET B 102 ? 0.7362 0.8328 0.8185 0.0435 0.0037 0.0159 102 MET B SD 3357 C CE . MET B 102 ? 0.7658 0.7890 0.8224 0.0295 0.0112 0.0035 102 MET B CE 3358 N N . GLU B 103 ? 0.5354 0.5802 0.6888 -0.0212 0.0016 -0.0235 103 GLU B N 3359 C CA . GLU B 103 ? 0.5533 0.5956 0.7094 -0.0256 0.0067 -0.0310 103 GLU B CA 3360 C C . GLU B 103 ? 0.5463 0.5982 0.7198 -0.0230 -0.0010 -0.0356 103 GLU B C 3361 O O . GLU B 103 ? 0.5497 0.6053 0.7285 -0.0236 0.0014 -0.0374 103 GLU B O 3362 C CB . GLU B 103 ? 0.5770 0.6256 0.7236 -0.0362 0.0135 -0.0390 103 GLU B CB 3363 C CG . GLU B 103 ? 0.6271 0.6469 0.7402 -0.0453 0.0201 -0.0326 103 GLU B CG 3364 C CD . GLU B 103 ? 0.6729 0.6547 0.7563 -0.0489 0.0214 -0.0276 103 GLU B CD 3365 O OE1 . GLU B 103 ? 0.6825 0.6742 0.7761 -0.0565 0.0209 -0.0314 103 GLU B OE1 3366 O OE2 . GLU B 103 ? 0.7480 0.6843 0.7892 -0.0401 0.0215 -0.0207 103 GLU B OE2 3367 N N . ASN B 104 ? 0.5393 0.5851 0.7112 -0.0206 -0.0124 -0.0373 104 ASN B N 3368 C CA . ASN B 104 ? 0.5498 0.5832 0.7198 -0.0176 -0.0239 -0.0390 104 ASN B CA 3369 C C . ASN B 104 ? 0.5423 0.5834 0.7223 -0.0251 -0.0251 -0.0256 104 ASN B C 3370 O O . ASN B 104 ? 0.5249 0.5661 0.7102 -0.0214 -0.0256 -0.0274 104 ASN B O 3371 C CB . ASN B 104 ? 0.5694 0.5683 0.7120 -0.0188 -0.0414 -0.0406 104 ASN B CB 3372 C CG . ASN B 104 ? 0.5767 0.5657 0.6996 0.0027 -0.0436 -0.0581 104 ASN B CG 3373 O OD1 . ASN B 104 ? 0.5433 0.5680 0.6796 0.0159 -0.0319 -0.0677 104 ASN B OD1 3374 N ND2 . ASN B 104 ? 0.6170 0.5619 0.7018 0.0056 -0.0599 -0.0616 104 ASN B ND2 3375 N N . GLU B 105 ? 0.5520 0.6098 0.7335 -0.0324 -0.0255 -0.0117 105 GLU B N 3376 C CA . GLU B 105 ? 0.5541 0.6392 0.7439 -0.0337 -0.0252 0.0020 105 GLU B CA 3377 C C . GLU B 105 ? 0.5291 0.6130 0.7225 -0.0181 -0.0131 -0.0032 105 GLU B C 3378 O O . GLU B 105 ? 0.4985 0.5901 0.6979 -0.0160 -0.0140 -0.0002 105 GLU B O 3379 C CB . GLU B 105 ? 0.5996 0.7261 0.7888 -0.0348 -0.0254 0.0170 105 GLU B CB 3380 C CG . GLU B 105 ? 0.6784 0.8563 0.8748 -0.0407 -0.0298 0.0347 105 GLU B CG 3381 C CD . GLU B 105 ? 0.7750 1.0155 0.9707 -0.0512 -0.0354 0.0519 105 GLU B CD 3382 O OE1 . GLU B 105 ? 0.8885 1.1523 1.0799 -0.0253 -0.0264 0.0520 105 GLU B OE1 3383 O OE2 . GLU B 105 ? 0.8046 1.0684 0.9965 -0.0875 -0.0504 0.0660 105 GLU B OE2 3384 N N . ARG B 106 ? 0.5411 0.6087 0.7227 -0.0111 -0.0037 -0.0103 106 ARG B N 3385 C CA . ARG B 106 ? 0.5788 0.6278 0.7459 -0.0046 0.0036 -0.0145 106 ARG B CA 3386 C C . ARG B 106 ? 0.5299 0.5786 0.7092 -0.0140 0.0031 -0.0247 106 ARG B C 3387 O O . ARG B 106 ? 0.5484 0.5918 0.7227 -0.0114 0.0045 -0.0251 106 ARG B O 3388 C CB . ARG B 106 ? 0.6360 0.6518 0.7695 -0.0038 0.0098 -0.0171 106 ARG B CB 3389 C CG . ARG B 106 ? 0.6867 0.7014 0.7972 0.0179 0.0101 -0.0073 106 ARG B CG 3390 C CD . ARG B 106 ? 0.8071 0.7601 0.8575 0.0285 0.0131 -0.0088 106 ARG B CD 3391 N NE . ARG B 106 ? 0.8713 0.7992 0.8870 0.0528 0.0115 -0.0070 106 ARG B NE 3392 C CZ . ARG B 106 ? 0.9609 0.8120 0.9124 0.0533 0.0095 -0.0114 106 ARG B CZ 3393 N NH1 . ARG B 106 ? 1.0327 0.8308 0.9497 0.0220 0.0091 -0.0154 106 ARG B NH1 3394 N NH2 . ARG B 106 ? 1.0604 0.8851 0.9737 0.0825 0.0062 -0.0110 106 ARG B NH2 3395 N N . THR B 107 ? 0.5043 0.5624 0.6949 -0.0195 0.0002 -0.0332 107 THR B N 3396 C CA . THR B 107 ? 0.4639 0.5379 0.6632 -0.0197 -0.0005 -0.0435 107 THR B CA 3397 C C . THR B 107 ? 0.4571 0.5299 0.6649 -0.0119 -0.0080 -0.0402 107 THR B C 3398 O O . THR B 107 ? 0.4344 0.5173 0.6465 -0.0109 -0.0063 -0.0439 107 THR B O 3399 C CB . THR B 107 ? 0.4683 0.5604 0.6683 -0.0137 -0.0027 -0.0545 107 THR B CB 3400 O OG1 . THR B 107 ? 0.4599 0.5655 0.6527 -0.0263 0.0058 -0.0565 107 THR B OG1 3401 C CG2 . THR B 107 ? 0.4765 0.5995 0.6821 -0.0016 -0.0051 -0.0651 107 THR B CG2 3402 N N . LEU B 108 ? 0.4573 0.5177 0.6624 -0.0115 -0.0175 -0.0315 108 LEU B N 3403 C CA . LEU B 108 ? 0.4648 0.5200 0.6694 -0.0117 -0.0264 -0.0246 108 LEU B CA 3404 C C . LEU B 108 ? 0.4617 0.5359 0.6755 -0.0106 -0.0195 -0.0159 108 LEU B C 3405 O O . LEU B 108 ? 0.4524 0.5296 0.6700 -0.0064 -0.0205 -0.0173 108 LEU B O 3406 C CB . LEU B 108 ? 0.4862 0.5220 0.6741 -0.0252 -0.0410 -0.0129 108 LEU B CB 3407 C CG . LEU B 108 ? 0.5352 0.5295 0.6940 -0.0221 -0.0535 -0.0222 108 LEU B CG 3408 C CD1 . LEU B 108 ? 0.5794 0.5399 0.7061 -0.0473 -0.0727 -0.0076 108 LEU B CD1 3409 C CD2 . LEU B 108 ? 0.5629 0.5364 0.7046 0.0028 -0.0584 -0.0382 108 LEU B CD2 3410 N N . ASP B 109 ? 0.4550 0.5409 0.6660 -0.0084 -0.0133 -0.0079 109 ASP B N 3411 C CA . ASP B 109 ? 0.4573 0.5545 0.6620 0.0048 -0.0074 -0.0025 109 ASP B CA 3412 C C . ASP B 109 ? 0.4600 0.5324 0.6530 0.0078 -0.0020 -0.0150 109 ASP B C 3413 O O . ASP B 109 ? 0.4894 0.5631 0.6764 0.0167 -0.0016 -0.0137 109 ASP B O 3414 C CB . ASP B 109 ? 0.4972 0.6040 0.6856 0.0187 -0.0030 0.0049 109 ASP B CB 3415 C CG . ASP B 109 ? 0.5309 0.6868 0.7309 0.0124 -0.0090 0.0214 109 ASP B CG 3416 O OD1 . ASP B 109 ? 0.5231 0.7076 0.7352 -0.0016 -0.0163 0.0321 109 ASP B OD1 3417 O OD2 . ASP B 109 ? 0.5835 0.7510 0.7755 0.0180 -0.0074 0.0250 109 ASP B OD2 3418 N N . PHE B 110 ? 0.4382 0.4933 0.6239 -0.0034 0.0011 -0.0257 110 PHE B N 3419 C CA . PHE B 110 ? 0.4335 0.4735 0.6024 -0.0149 0.0037 -0.0350 110 PHE B CA 3420 C C . PHE B 110 ? 0.4330 0.4980 0.6224 -0.0150 0.0004 -0.0398 110 PHE B C 3421 O O . PHE B 110 ? 0.4638 0.5191 0.6392 -0.0166 0.0002 -0.0417 110 PHE B O 3422 C CB . PHE B 110 ? 0.4347 0.4773 0.5978 -0.0348 0.0066 -0.0419 110 PHE B CB 3423 C CG . PHE B 110 ? 0.4526 0.4979 0.5973 -0.0610 0.0074 -0.0485 110 PHE B CG 3424 C CD1 . PHE B 110 ? 0.5085 0.5018 0.6052 -0.0729 0.0052 -0.0468 110 PHE B CD1 3425 C CD2 . PHE B 110 ? 0.4358 0.5374 0.6013 -0.0746 0.0085 -0.0558 110 PHE B CD2 3426 C CE1 . PHE B 110 ? 0.5381 0.5313 0.6082 -0.1101 0.0025 -0.0505 110 PHE B CE1 3427 C CE2 . PHE B 110 ? 0.4605 0.5872 0.6099 -0.1078 0.0084 -0.0589 110 PHE B CE2 3428 C CZ . PHE B 110 ? 0.5092 0.5791 0.6104 -0.1320 0.0047 -0.0553 110 PHE B CZ 3429 N N . HIS B 111 ? 0.4126 0.5009 0.6252 -0.0099 -0.0040 -0.0422 111 HIS B N 3430 C CA . HIS B 111 ? 0.4142 0.5202 0.6382 -0.0018 -0.0092 -0.0463 111 HIS B CA 3431 C C . HIS B 111 ? 0.4204 0.5185 0.6444 0.0051 -0.0117 -0.0362 111 HIS B C 3432 O O . HIS B 111 ? 0.4565 0.5635 0.6817 0.0079 -0.0122 -0.0396 111 HIS B O 3433 C CB . HIS B 111 ? 0.4093 0.5166 0.6349 0.0110 -0.0176 -0.0502 111 HIS B CB 3434 C CG . HIS B 111 ? 0.4033 0.5380 0.6285 0.0151 -0.0153 -0.0627 111 HIS B CG 3435 N ND1 . HIS B 111 ? 0.3975 0.5831 0.6291 0.0136 -0.0111 -0.0724 111 HIS B ND1 3436 C CD2 . HIS B 111 ? 0.3996 0.5294 0.6172 0.0206 -0.0170 -0.0661 111 HIS B CD2 3437 C CE1 . HIS B 111 ? 0.3958 0.6172 0.6261 0.0192 -0.0092 -0.0804 111 HIS B CE1 3438 N NE2 . HIS B 111 ? 0.3963 0.5789 0.6170 0.0262 -0.0126 -0.0777 111 HIS B NE2 3439 N N . ASP B 112 ? 0.3944 0.4876 0.6170 0.0067 -0.0134 -0.0229 112 ASP B N 3440 C CA . ASP B 112 ? 0.3957 0.5021 0.6183 0.0127 -0.0149 -0.0102 112 ASP B CA 3441 C C . ASP B 112 ? 0.4218 0.5217 0.6283 0.0241 -0.0082 -0.0142 112 ASP B C 3442 O O . ASP B 112 ? 0.4503 0.5571 0.6556 0.0311 -0.0092 -0.0137 112 ASP B O 3443 C CB . ASP B 112 ? 0.3980 0.5237 0.6204 0.0089 -0.0170 0.0062 112 ASP B CB 3444 C CG . ASP B 112 ? 0.4148 0.5783 0.6397 0.0084 -0.0205 0.0238 112 ASP B CG 3445 O OD1 . ASP B 112 ? 0.4214 0.5849 0.6476 0.0114 -0.0224 0.0233 112 ASP B OD1 3446 O OD2 . ASP B 112 ? 0.4263 0.6305 0.6516 0.0036 -0.0217 0.0397 112 ASP B OD2 3447 N N . SER B 113 ? 0.4325 0.5078 0.6160 0.0257 -0.0035 -0.0188 113 SER B N 3448 C CA . SER B 113 ? 0.4687 0.5077 0.6115 0.0351 -0.0018 -0.0241 113 SER B CA 3449 C C . SER B 113 ? 0.4824 0.5114 0.6211 0.0187 -0.0042 -0.0351 113 SER B C 3450 O O . SER B 113 ? 0.4844 0.4969 0.5994 0.0282 -0.0063 -0.0368 113 SER B O 3451 C CB . SER B 113 ? 0.5018 0.4955 0.6050 0.0331 0.0000 -0.0272 113 SER B CB 3452 O OG . SER B 113 ? 0.5690 0.5003 0.6121 0.0334 -0.0033 -0.0339 113 SER B OG 3453 N N . ASN B 114 ? 0.4661 0.5133 0.6247 -0.0038 -0.0044 -0.0427 114 ASN B N 3454 C CA . ASN B 114 ? 0.4696 0.5309 0.6269 -0.0214 -0.0069 -0.0520 114 ASN B CA 3455 C C . ASN B 114 ? 0.4479 0.5357 0.6274 -0.0054 -0.0098 -0.0508 114 ASN B C 3456 O O . ASN B 114 ? 0.4396 0.5260 0.6052 -0.0116 -0.0125 -0.0558 114 ASN B O 3457 C CB . ASN B 114 ? 0.4626 0.5666 0.6399 -0.0406 -0.0059 -0.0591 114 ASN B CB 3458 C CG . ASN B 114 ? 0.4908 0.5730 0.6420 -0.0644 -0.0034 -0.0591 114 ASN B CG 3459 O OD1 . ASN B 114 ? 0.5444 0.5685 0.6456 -0.0793 -0.0055 -0.0573 114 ASN B OD1 3460 N ND2 . ASN B 114 ? 0.4721 0.5926 0.6465 -0.0662 -0.0006 -0.0614 114 ASN B ND2 3461 N N . VAL B 115 ? 0.4234 0.5287 0.6290 0.0110 -0.0111 -0.0431 115 VAL B N 3462 C CA . VAL B 115 ? 0.4092 0.5312 0.6271 0.0231 -0.0155 -0.0395 115 VAL B CA 3463 C C . VAL B 115 ? 0.4295 0.5417 0.6310 0.0347 -0.0141 -0.0323 115 VAL B C 3464 O O . VAL B 115 ? 0.4255 0.5435 0.6233 0.0391 -0.0162 -0.0354 115 VAL B O 3465 C CB . VAL B 115 ? 0.4011 0.5260 0.6314 0.0290 -0.0216 -0.0304 115 VAL B CB 3466 C CG1 . VAL B 115 ? 0.4103 0.5402 0.6404 0.0369 -0.0277 -0.0224 115 VAL B CG1 3467 C CG2 . VAL B 115 ? 0.4077 0.5367 0.6411 0.0311 -0.0255 -0.0410 115 VAL B CG2 3468 N N . LYS B 116 ? 0.4522 0.5561 0.6406 0.0447 -0.0110 -0.0231 116 LYS B N 3469 C CA . LYS B 116 ? 0.4936 0.5973 0.6579 0.0675 -0.0095 -0.0172 116 LYS B CA 3470 C C . LYS B 116 ? 0.5335 0.5904 0.6542 0.0702 -0.0113 -0.0303 116 LYS B C 3471 O O . LYS B 116 ? 0.5482 0.6039 0.6517 0.0862 -0.0132 -0.0307 116 LYS B O 3472 C CB . LYS B 116 ? 0.5330 0.6467 0.6830 0.0863 -0.0061 -0.0068 116 LYS B CB 3473 C CG . LYS B 116 ? 0.5990 0.7455 0.7315 0.1191 -0.0047 0.0031 116 LYS B CG 3474 C CD . LYS B 116 ? 0.7105 0.8631 0.8089 0.1524 -0.0016 0.0079 116 LYS B CD 3475 C CE . LYS B 116 ? 0.7541 0.9659 0.8361 0.1936 0.0002 0.0190 116 LYS B CE 3476 N NZ . LYS B 116 ? 0.7173 1.0163 0.8504 0.1716 0.0001 0.0383 116 LYS B NZ 3477 N N . ASN B 117 ? 0.5606 0.5751 0.6555 0.0506 -0.0123 -0.0399 117 ASN B N 3478 C CA . ASN B 117 ? 0.6353 0.5887 0.6705 0.0402 -0.0184 -0.0505 117 ASN B CA 3479 C C . ASN B 117 ? 0.6318 0.6086 0.6822 0.0202 -0.0225 -0.0576 117 ASN B C 3480 O O . ASN B 117 ? 0.6803 0.6191 0.6856 0.0220 -0.0290 -0.0631 117 ASN B O 3481 C CB . ASN B 117 ? 0.6733 0.5772 0.6711 0.0117 -0.0206 -0.0554 117 ASN B CB 3482 C CG . ASN B 117 ? 0.6993 0.5607 0.6590 0.0388 -0.0189 -0.0501 117 ASN B CG 3483 O OD1 . ASN B 117 ? 0.7057 0.5662 0.6475 0.0822 -0.0179 -0.0449 117 ASN B OD1 3484 N ND2 . ASN B 117 ? 0.7229 0.5589 0.6685 0.0160 -0.0185 -0.0507 117 ASN B ND2 3485 N N . LEU B 118 ? 0.5904 0.6279 0.6967 0.0060 -0.0203 -0.0582 118 LEU B N 3486 C CA . LEU B 118 ? 0.5913 0.6676 0.7157 -0.0046 -0.0241 -0.0646 118 LEU B CA 3487 C C . LEU B 118 ? 0.5876 0.6725 0.7190 0.0238 -0.0248 -0.0594 118 LEU B C 3488 O O . LEU B 118 ? 0.6186 0.6990 0.7311 0.0208 -0.0297 -0.0651 118 LEU B O 3489 C CB . LEU B 118 ? 0.5696 0.7081 0.7414 -0.0100 -0.0224 -0.0668 118 LEU B CB 3490 C CG . LEU B 118 ? 0.5781 0.7736 0.7692 -0.0120 -0.0264 -0.0740 118 LEU B CG 3491 C CD1 . LEU B 118 ? 0.6309 0.8298 0.7909 -0.0466 -0.0317 -0.0816 118 LEU B CD1 3492 C CD2 . LEU B 118 ? 0.5609 0.8113 0.7817 -0.0056 -0.0255 -0.0779 118 LEU B CD2 3493 N N . TYR B 119 ? 0.5469 0.6471 0.7010 0.0467 -0.0210 -0.0471 119 TYR B N 3494 C CA . TYR B 119 ? 0.5327 0.6503 0.6904 0.0694 -0.0214 -0.0380 119 TYR B CA 3495 C C . TYR B 119 ? 0.5878 0.6704 0.6960 0.0885 -0.0223 -0.0409 119 TYR B C 3496 O O . TYR B 119 ? 0.6449 0.7346 0.7444 0.0998 -0.0250 -0.0421 119 TYR B O 3497 C CB . TYR B 119 ? 0.4938 0.6401 0.6753 0.0786 -0.0189 -0.0204 119 TYR B CB 3498 C CG . TYR B 119 ? 0.4937 0.6727 0.6769 0.0950 -0.0193 -0.0064 119 TYR B CG 3499 C CD1 . TYR B 119 ? 0.4901 0.6857 0.6886 0.0904 -0.0242 -0.0021 119 TYR B CD1 3500 C CD2 . TYR B 119 ? 0.5151 0.7144 0.6795 0.1184 -0.0151 0.0036 119 TYR B CD2 3501 C CE1 . TYR B 119 ? 0.5055 0.7343 0.7028 0.0999 -0.0248 0.0134 119 TYR B CE1 3502 C CE2 . TYR B 119 ? 0.5145 0.7632 0.6817 0.1323 -0.0146 0.0187 119 TYR B CE2 3503 C CZ . TYR B 119 ? 0.5255 0.7876 0.7103 0.1186 -0.0194 0.0243 119 TYR B CZ 3504 O OH . TYR B 119 ? 0.5345 0.8483 0.7189 0.1271 -0.0192 0.0416 119 TYR B OH 3505 N N . ASP B 120 ? 0.6181 0.6559 0.6843 0.0972 -0.0216 -0.0428 120 ASP B N 3506 C CA . ASP B 120 ? 0.6899 0.6751 0.6866 0.1263 -0.0258 -0.0477 120 ASP B CA 3507 C C . ASP B 120 ? 0.7191 0.6446 0.6669 0.1028 -0.0361 -0.0629 120 ASP B C 3508 O O . ASP B 120 ? 0.7451 0.6425 0.6491 0.1235 -0.0418 -0.0675 120 ASP B O 3509 C CB . ASP B 120 ? 0.7514 0.6913 0.6992 0.1490 -0.0251 -0.0466 120 ASP B CB 3510 C CG . ASP B 120 ? 0.7260 0.7390 0.7112 0.1778 -0.0165 -0.0300 120 ASP B CG 3511 O OD1 . ASP B 120 ? 0.7132 0.7936 0.7271 0.1952 -0.0133 -0.0188 120 ASP B OD1 3512 O OD2 . ASP B 120 ? 0.7615 0.7698 0.7447 0.1792 -0.0138 -0.0265 120 ASP B OD2 3513 N N . LYS B 121 ? 0.7286 0.6418 0.6809 0.0571 -0.0394 -0.0696 121 LYS B N 3514 C CA . LYS B 121 ? 0.8087 0.6867 0.7198 0.0187 -0.0507 -0.0809 121 LYS B CA 3515 C C . LYS B 121 ? 0.7879 0.7125 0.7257 0.0249 -0.0525 -0.0832 121 LYS B C 3516 O O . LYS B 121 ? 0.8611 0.7372 0.7408 0.0200 -0.0631 -0.0909 121 LYS B O 3517 C CB . LYS B 121 ? 0.8133 0.7259 0.7534 -0.0323 -0.0506 -0.0831 121 LYS B CB 3518 C CG . LYS B 121 ? 0.8899 0.7832 0.7845 -0.0878 -0.0634 -0.0911 121 LYS B CG 3519 C CD . LYS B 121 ? 0.8819 0.8486 0.8204 -0.1306 -0.0598 -0.0900 121 LYS B CD 3520 C CE . LYS B 121 ? 0.9741 0.9238 0.8543 -0.2007 -0.0736 -0.0931 121 LYS B CE 3521 N NZ . LYS B 121 ? 1.0142 1.0052 0.8918 -0.2212 -0.0826 -0.0984 121 LYS B NZ 3522 N N . VAL B 122 ? 0.7045 0.7131 0.7202 0.0360 -0.0442 -0.0762 122 VAL B N 3523 C CA . VAL B 122 ? 0.6770 0.7300 0.7179 0.0460 -0.0458 -0.0766 122 VAL B CA 3524 C C . VAL B 122 ? 0.7249 0.7606 0.7408 0.0875 -0.0449 -0.0711 122 VAL B C 3525 O O . VAL B 122 ? 0.7519 0.7777 0.7417 0.0934 -0.0510 -0.0768 122 VAL B O 3526 C CB . VAL B 122 ? 0.6014 0.7285 0.7129 0.0496 -0.0404 -0.0701 122 VAL B CB 3527 C CG1 . VAL B 122 ? 0.5834 0.7455 0.7126 0.0684 -0.0424 -0.0672 122 VAL B CG1 3528 C CG2 . VAL B 122 ? 0.5766 0.7389 0.7069 0.0180 -0.0423 -0.0783 122 VAL B CG2 3529 N N . ARG B 123 ? 0.7129 0.7557 0.7358 0.1164 -0.0375 -0.0594 123 ARG B N 3530 C CA . ARG B 123 ? 0.7608 0.8105 0.7591 0.1602 -0.0354 -0.0521 123 ARG B CA 3531 C C . ARG B 123 ? 0.8652 0.8337 0.7741 0.1787 -0.0452 -0.0660 123 ARG B C 3532 O O . ARG B 123 ? 0.8930 0.8666 0.7795 0.2049 -0.0479 -0.0673 123 ARG B O 3533 C CB . ARG B 123 ? 0.7655 0.8447 0.7747 0.1847 -0.0273 -0.0377 123 ARG B CB 3534 C CG . ARG B 123 ? 0.7961 0.9272 0.7964 0.2292 -0.0231 -0.0249 123 ARG B CG 3535 C CD . ARG B 123 ? 0.8043 0.9878 0.8173 0.2487 -0.0157 -0.0089 123 ARG B CD 3536 N NE . ARG B 123 ? 0.8594 0.9794 0.8291 0.2575 -0.0173 -0.0186 123 ARG B NE 3537 C CZ . ARG B 123 ? 0.9393 0.9895 0.8239 0.2989 -0.0227 -0.0306 123 ARG B CZ 3538 N NH1 . ARG B 123 ? 0.9861 1.0220 0.8183 0.3397 -0.0270 -0.0362 123 ARG B NH1 3539 N NH2 . ARG B 123 ? 0.9683 0.9522 0.8091 0.3022 -0.0256 -0.0375 123 ARG B NH2 3540 N N . LEU B 124 ? 0.9366 0.8212 0.7846 0.1641 -0.0524 -0.0761 124 LEU B N 3541 C CA . LEU B 124 ? 1.0866 0.8596 0.8208 0.1799 -0.0669 -0.0897 124 LEU B CA 3542 C C . LEU B 124 ? 1.1339 0.8727 0.8370 0.1435 -0.0802 -0.1017 124 LEU B C 3543 O O . LEU B 124 ? 1.2533 0.9013 0.8586 0.1605 -0.0944 -0.1124 124 LEU B O 3544 C CB . LEU B 124 ? 1.1643 0.8403 0.8270 0.1674 -0.0743 -0.0950 124 LEU B CB 3545 C CG . LEU B 124 ? 1.1703 0.8643 0.8366 0.2152 -0.0644 -0.0855 124 LEU B CG 3546 C CD1 . LEU B 124 ? 1.2199 0.8508 0.8555 0.1868 -0.0675 -0.0870 124 LEU B CD1 3547 C CD2 . LEU B 124 ? 1.2488 0.9014 0.8294 0.2920 -0.0688 -0.0884 124 LEU B CD2 3548 N N . GLN B 125 ? 1.0687 0.8792 0.8467 0.0968 -0.0772 -0.1004 125 GLN B N 3549 C CA . GLN B 125 ? 1.0871 0.9011 0.8531 0.0636 -0.0882 -0.1094 125 GLN B CA 3550 C C . GLN B 125 ? 1.0465 0.9173 0.8463 0.1015 -0.0834 -0.1060 125 GLN B C 3551 O O . GLN B 125 ? 1.1341 0.9597 0.8739 0.1119 -0.0943 -0.1146 125 GLN B O 3552 C CB . GLN B 125 ? 1.0419 0.9327 0.8751 0.0095 -0.0862 -0.1090 125 GLN B CB 3553 C CG . GLN B 125 ? 1.1202 0.9653 0.9127 -0.0442 -0.0940 -0.1124 125 GLN B CG 3554 C CD . GLN B 125 ? 1.0906 1.0310 0.9387 -0.0959 -0.0944 -0.1131 125 GLN B CD 3555 O OE1 . GLN B 125 ? 1.1742 1.1186 0.9880 -0.1406 -0.1078 -0.1193 125 GLN B OE1 3556 N NE2 . GLN B 125 ? 1.0017 1.0254 0.9312 -0.0874 -0.0808 -0.1069 125 GLN B NE2 3557 N N . LEU B 126 ? 0.9548 0.9180 0.8427 0.1191 -0.0690 -0.0928 126 LEU B N 3558 C CA . LEU B 126 ? 0.9448 0.9657 0.8656 0.1477 -0.0649 -0.0860 126 LEU B CA 3559 C C . LEU B 126 ? 1.0293 1.0213 0.8954 0.2003 -0.0648 -0.0840 126 LEU B C 3560 O O . LEU B 126 ? 1.1019 1.0960 0.9457 0.2180 -0.0694 -0.0877 126 LEU B O 3561 C CB . LEU B 126 ? 0.8359 0.9402 0.8415 0.1505 -0.0534 -0.0697 126 LEU B CB 3562 C CG . LEU B 126 ? 0.7793 0.9190 0.8322 0.1144 -0.0544 -0.0733 126 LEU B CG 3563 C CD1 . LEU B 126 ? 0.7181 0.9121 0.8284 0.1246 -0.0480 -0.0582 126 LEU B CD1 3564 C CD2 . LEU B 126 ? 0.8130 0.9665 0.8563 0.0935 -0.0640 -0.0860 126 LEU B CD2 3565 N N . ARG B 127 ? 1.1165 1.0878 0.9572 0.2299 -0.0599 -0.0788 127 ARG B N 3566 C CA . ARG B 127 ? 1.2161 1.1780 1.0004 0.2926 -0.0592 -0.0767 127 ARG B CA 3567 C C . ARG B 127 ? 1.1523 1.2158 0.9897 0.3151 -0.0504 -0.0614 127 ARG B C 3568 O O . ARG B 127 ? 1.0968 1.2413 1.0131 0.2958 -0.0408 -0.0438 127 ARG B O 3569 C CB . ARG B 127 ? 1.3757 1.2155 1.0409 0.3086 -0.0768 -0.0974 127 ARG B CB 3570 C CG . ARG B 127 ? 1.4657 1.1903 1.0566 0.2856 -0.0882 -0.1089 127 ARG B CG 3571 C CD . ARG B 127 ? 1.5955 1.1910 1.0769 0.2587 -0.1114 -0.1282 127 ARG B CD 3572 N NE . ARG B 127 ? 1.7282 1.2541 1.1058 0.3216 -0.1224 -0.1381 127 ARG B NE 3573 C CZ . ARG B 127 ? 1.9134 1.3071 1.1695 0.3094 -0.1466 -0.1556 127 ARG B CZ 3574 N NH1 . ARG B 127 ? 1.9789 1.3067 1.2060 0.2271 -0.1622 -0.1625 127 ARG B NH1 3575 N NH2 . ARG B 127 ? 2.0134 1.3427 1.1690 0.3786 -0.1567 -0.1655 127 ARG B NH2 3576 N N . ASP B 128 ? 1.2027 1.2551 0.9899 0.3521 -0.0555 -0.0673 128 ASP B N 3577 C CA . ASP B 128 ? 1.1726 1.3255 1.0035 0.3737 -0.0470 -0.0504 128 ASP B CA 3578 C C . ASP B 128 ? 1.1019 1.2743 0.9737 0.3387 -0.0506 -0.0516 128 ASP B C 3579 O O . ASP B 128 ? 1.0826 1.3184 0.9726 0.3564 -0.0468 -0.0401 128 ASP B O 3580 C CB . ASP B 128 ? 1.2761 1.4317 1.0336 0.4449 -0.0482 -0.0529 128 ASP B CB 3581 C CG . ASP B 128 ? 1.4109 1.4634 1.0801 0.4585 -0.0644 -0.0773 128 ASP B CG 3582 O OD1 . ASP B 128 ? 1.4555 1.4204 1.1039 0.4105 -0.0765 -0.0933 128 ASP B OD1 3583 O OD2 . ASP B 128 ? 1.5208 1.5852 1.1376 0.5153 -0.0662 -0.0796 128 ASP B OD2 3584 N N . ASN B 129 ? 1.0855 1.2138 0.9701 0.2909 -0.0580 -0.0644 129 ASN B N 3585 C CA . ASN B 129 ? 1.0297 1.1912 0.9576 0.2613 -0.0612 -0.0652 129 ASN B CA 3586 C C . ASN B 129 ? 0.9398 1.1686 0.9464 0.2406 -0.0533 -0.0471 129 ASN B C 3587 O O . ASN B 129 ? 0.9210 1.1731 0.9572 0.2232 -0.0570 -0.0482 129 ASN B O 3588 C CB . ASN B 129 ? 1.0990 1.2053 1.0022 0.2200 -0.0739 -0.0859 129 ASN B CB 3589 C CG . ASN B 129 ? 1.2385 1.2668 1.0513 0.2286 -0.0884 -0.1038 129 ASN B CG 3590 O OD1 . ASN B 129 ? 1.3845 1.3844 1.1425 0.2761 -0.0889 -0.1043 129 ASN B OD1 3591 N ND2 . ASN B 129 ? 1.2582 1.2539 1.0474 0.1821 -0.1019 -0.1184 129 ASN B ND2 3592 N N . ALA B 130 ? 0.8868 1.1413 0.9170 0.2443 -0.0447 -0.0309 130 ALA B N 3593 C CA . ALA B 130 ? 0.8094 1.1045 0.8939 0.2217 -0.0412 -0.0132 130 ALA B CA 3594 C C . ALA B 130 ? 0.7869 1.1291 0.8822 0.2307 -0.0333 0.0107 130 ALA B C 3595 O O . ALA B 130 ? 0.8478 1.1914 0.9172 0.2548 -0.0289 0.0096 130 ALA B O 3596 C CB . ALA B 130 ? 0.7865 1.0514 0.8898 0.1925 -0.0435 -0.0240 130 ALA B CB 3597 N N . LYS B 131 ? 0.7568 1.1359 0.8810 0.2106 -0.0336 0.0328 131 LYS B N 3598 C CA . LYS B 131 ? 0.7601 1.1937 0.8948 0.2026 -0.0287 0.0592 131 LYS B CA 3599 C C . LYS B 131 ? 0.7208 1.1289 0.8722 0.1775 -0.0291 0.0597 131 LYS B C 3600 O O . LYS B 131 ? 0.6988 1.0637 0.8615 0.1548 -0.0357 0.0543 131 LYS B O 3601 C CB . LYS B 131 ? 0.8250 1.3001 0.9659 0.1813 -0.0327 0.0868 131 LYS B CB 3602 C CG . LYS B 131 ? 0.9018 1.4260 1.0274 0.2074 -0.0299 0.0928 131 LYS B CG 3603 C CD . LYS B 131 ? 0.9904 1.5528 1.1149 0.1796 -0.0352 0.1231 131 LYS B CD 3604 C CE . LYS B 131 ? 1.0345 1.5339 1.1518 0.1726 -0.0454 0.1140 131 LYS B CE 3605 N NZ . LYS B 131 ? 1.0754 1.5982 1.1751 0.1491 -0.0524 0.1438 131 LYS B NZ 3606 N N . GLU B 132 ? 0.6952 1.1338 0.8436 0.1877 -0.0226 0.0655 132 GLU B N 3607 C CA . GLU B 132 ? 0.6473 1.0718 0.8106 0.1646 -0.0226 0.0688 132 GLU B CA 3608 C C . GLU B 132 ? 0.6341 1.1013 0.8100 0.1266 -0.0274 0.0995 132 GLU B C 3609 O O . GLU B 132 ? 0.6434 1.1935 0.8191 0.1248 -0.0237 0.1230 132 GLU B O 3610 C CB . GLU B 132 ? 0.6554 1.0976 0.8029 0.1941 -0.0152 0.0638 132 GLU B CB 3611 C CG . GLU B 132 ? 0.6474 1.0603 0.8062 0.1755 -0.0149 0.0602 132 GLU B CG 3612 C CD . GLU B 132 ? 0.6898 1.1070 0.8216 0.2114 -0.0090 0.0532 132 GLU B CD 3613 O OE1 . GLU B 132 ? 0.7170 1.1601 0.8146 0.2567 -0.0058 0.0512 132 GLU B OE1 3614 O OE2 . GLU B 132 ? 0.7025 1.0924 0.8399 0.1991 -0.0085 0.0489 132 GLU B OE2 3615 N N . LEU B 133 ? 0.6260 1.0369 0.8033 0.0960 -0.0376 0.1001 133 LEU B N 3616 C CA . LEU B 133 ? 0.6387 1.0572 0.8039 0.0534 -0.0483 0.1293 133 LEU B CA 3617 C C . LEU B 133 ? 0.6298 1.0818 0.7983 0.0233 -0.0492 0.1478 133 LEU B C 3618 O O . LEU B 133 ? 0.6518 1.1410 0.8048 -0.0177 -0.0574 0.1787 133 LEU B O 3619 C CB . LEU B 133 ? 0.6655 0.9930 0.8102 0.0400 -0.0626 0.1218 133 LEU B CB 3620 C CG . LEU B 133 ? 0.7005 1.0096 0.8253 0.0479 -0.0694 0.1240 133 LEU B CG 3621 C CD1 . LEU B 133 ? 0.6859 1.0625 0.8248 0.0750 -0.0581 0.1229 133 LEU B CD1 3622 C CD2 . LEU B 133 ? 0.7184 0.9564 0.8357 0.0698 -0.0760 0.0976 133 LEU B CD2 3623 N N . GLY B 134 ? 0.6028 1.0419 0.7864 0.0382 -0.0425 0.1306 134 GLY B N 3624 C CA . GLY B 134 ? 0.6001 1.0768 0.7888 0.0146 -0.0426 0.1457 134 GLY B CA 3625 C C . GLY B 134 ? 0.6173 1.0153 0.7956 -0.0174 -0.0542 0.1424 134 GLY B C 3626 O O . GLY B 134 ? 0.6218 1.0442 0.7998 -0.0441 -0.0571 0.1560 134 GLY B O 3627 N N . ASN B 135 ? 0.6211 0.9312 0.7873 -0.0105 -0.0614 0.1236 135 ASN B N 3628 C CA . ASN B 135 ? 0.6548 0.8835 0.7986 -0.0294 -0.0745 0.1180 135 ASN B CA 3629 C C . ASN B 135 ? 0.6329 0.8151 0.7903 0.0041 -0.0694 0.0848 135 ASN B C 3630 O O . ASN B 135 ? 0.6339 0.7509 0.7686 0.0030 -0.0800 0.0755 135 ASN B O 3631 C CB . ASN B 135 ? 0.7267 0.8913 0.8195 -0.0542 -0.0944 0.1327 135 ASN B CB 3632 C CG . ASN B 135 ? 0.7349 0.8807 0.8241 -0.0227 -0.0939 0.1198 135 ASN B CG 3633 O OD1 . ASN B 135 ? 0.6954 0.8850 0.8216 0.0105 -0.0788 0.1027 135 ASN B OD1 3634 N ND2 . ASN B 135 ? 0.8174 0.8908 0.8525 -0.0330 -0.1124 0.1282 135 ASN B ND2 3635 N N . GLY B 136 ? 0.5937 0.8101 0.7792 0.0330 -0.0549 0.0679 136 GLY B N 3636 C CA . GLY B 136 ? 0.5715 0.7605 0.7674 0.0539 -0.0507 0.0400 136 GLY B CA 3637 C C . GLY B 136 ? 0.5512 0.7394 0.7461 0.0733 -0.0512 0.0272 136 GLY B C 3638 O O . GLY B 136 ? 0.5264 0.7124 0.7302 0.0849 -0.0478 0.0061 136 GLY B O 3639 N N . CYS B 137 ? 0.5809 0.7784 0.7634 0.0726 -0.0562 0.0414 137 CYS B N 3640 C CA . CYS B 137 ? 0.6006 0.7985 0.7794 0.0916 -0.0583 0.0307 137 CYS B CA 3641 C C . CYS B 137 ? 0.5864 0.8256 0.7715 0.1028 -0.0503 0.0330 137 CYS B C 3642 O O . CYS B 137 ? 0.5887 0.8630 0.7738 0.0987 -0.0454 0.0500 137 CYS B O 3643 C CB . CYS B 137 ? 0.6580 0.8184 0.8041 0.0886 -0.0732 0.0427 137 CYS B CB 3644 S SG . CYS B 137 ? 0.7460 0.8355 0.8590 0.0886 -0.0876 0.0371 137 CYS B SG 3645 N N . PHE B 138 ? 0.5881 0.8292 0.7743 0.1190 -0.0500 0.0153 138 PHE B N 3646 C CA . PHE B 138 ? 0.5930 0.8584 0.7737 0.1337 -0.0456 0.0130 138 PHE B CA 3647 C C . PHE B 138 ? 0.6215 0.8892 0.7952 0.1425 -0.0529 0.0127 138 PHE B C 3648 O O . PHE B 138 ? 0.6275 0.8861 0.8030 0.1474 -0.0582 -0.0024 138 PHE B O 3649 C CB . PHE B 138 ? 0.5889 0.8427 0.7641 0.1386 -0.0417 -0.0098 138 PHE B CB 3650 C CG . PHE B 138 ? 0.6005 0.8400 0.7706 0.1350 -0.0357 -0.0109 138 PHE B CG 3651 C CD1 . PHE B 138 ? 0.6051 0.8526 0.7538 0.1542 -0.0305 -0.0048 138 PHE B CD1 3652 C CD2 . PHE B 138 ? 0.6083 0.8296 0.7895 0.1187 -0.0357 -0.0185 138 PHE B CD2 3653 C CE1 . PHE B 138 ? 0.6219 0.8534 0.7575 0.1585 -0.0262 -0.0063 138 PHE B CE1 3654 C CE2 . PHE B 138 ? 0.6071 0.8117 0.7797 0.1162 -0.0308 -0.0191 138 PHE B CE2 3655 C CZ . PHE B 138 ? 0.6230 0.8296 0.7713 0.1368 -0.0264 -0.0130 138 PHE B CZ 3656 N N . GLU B 139 ? 0.6566 0.9462 0.8205 0.1465 -0.0532 0.0302 139 GLU B N 3657 C CA . GLU B 139 ? 0.6816 0.9722 0.8340 0.1567 -0.0601 0.0316 139 GLU B CA 3658 C C . GLU B 139 ? 0.6900 1.0042 0.8402 0.1755 -0.0555 0.0178 139 GLU B C 3659 O O . GLU B 139 ? 0.6794 1.0169 0.8226 0.1847 -0.0487 0.0236 139 GLU B O 3660 C CB . GLU B 139 ? 0.7383 1.0358 0.8730 0.1427 -0.0649 0.0619 139 GLU B CB 3661 C CG . GLU B 139 ? 0.8156 1.1066 0.9294 0.1527 -0.0731 0.0672 139 GLU B CG 3662 C CD . GLU B 139 ? 0.9216 1.2276 1.0122 0.1301 -0.0773 0.1010 139 GLU B CD 3663 O OE1 . GLU B 139 ? 1.0073 1.2889 1.0799 0.0983 -0.0843 0.1210 139 GLU B OE1 3664 O OE2 . GLU B 139 ? 0.9947 1.3391 1.0808 0.1401 -0.0746 0.1088 139 GLU B OE2 3665 N N . PHE B 140 ? 0.7144 1.0252 0.8638 0.1838 -0.0609 -0.0005 140 PHE B N 3666 C CA . PHE B 140 ? 0.7271 1.0488 0.8655 0.1941 -0.0604 -0.0167 140 PHE B CA 3667 C C . PHE B 140 ? 0.7634 1.1063 0.8880 0.2111 -0.0611 -0.0057 140 PHE B C 3668 O O . PHE B 140 ? 0.7494 1.0988 0.8734 0.2126 -0.0652 0.0104 140 PHE B O 3669 C CB . PHE B 140 ? 0.7004 1.0300 0.8438 0.1895 -0.0672 -0.0380 140 PHE B CB 3670 C CG . PHE B 140 ? 0.6780 0.9999 0.8301 0.1699 -0.0661 -0.0512 140 PHE B CG 3671 C CD1 . PHE B 140 ? 0.6611 0.9833 0.8305 0.1673 -0.0665 -0.0483 140 PHE B CD1 3672 C CD2 . PHE B 140 ? 0.6993 1.0057 0.8318 0.1529 -0.0666 -0.0659 140 PHE B CD2 3673 C CE1 . PHE B 140 ? 0.6523 0.9767 0.8305 0.1494 -0.0648 -0.0596 140 PHE B CE1 3674 C CE2 . PHE B 140 ? 0.6960 0.9955 0.8312 0.1281 -0.0665 -0.0755 140 PHE B CE2 3675 C CZ . PHE B 140 ? 0.6679 0.9852 0.8318 0.1269 -0.0642 -0.0720 140 PHE B CZ 3676 N N . TYR B 141 ? 0.8176 1.1624 0.9205 0.2247 -0.0589 -0.0147 141 TYR B N 3677 C CA . TYR B 141 ? 0.8709 1.2404 0.9577 0.2450 -0.0597 -0.0078 141 TYR B CA 3678 C C . TYR B 141 ? 0.8741 1.2462 0.9582 0.2466 -0.0686 -0.0223 141 TYR B C 3679 O O . TYR B 141 ? 0.9413 1.3350 1.0193 0.2602 -0.0708 -0.0134 141 TYR B O 3680 C CB . TYR B 141 ? 0.8853 1.2514 0.9369 0.2692 -0.0558 -0.0134 141 TYR B CB 3681 C CG . TYR B 141 ? 0.8908 1.2811 0.9436 0.2786 -0.0465 0.0042 141 TYR B CG 3682 C CD1 . TYR B 141 ? 0.8794 1.3264 0.9527 0.2724 -0.0418 0.0339 141 TYR B CD1 3683 C CD2 . TYR B 141 ? 0.9222 1.2804 0.9491 0.2901 -0.0442 -0.0073 141 TYR B CD2 3684 C CE1 . TYR B 141 ? 0.8956 1.3865 0.9720 0.2761 -0.0340 0.0521 141 TYR B CE1 3685 C CE2 . TYR B 141 ? 0.9266 1.3213 0.9548 0.3040 -0.0358 0.0087 141 TYR B CE2 3686 C CZ . TYR B 141 ? 0.9195 1.3904 0.9768 0.2961 -0.0302 0.0385 141 TYR B CZ 3687 O OH . TYR B 141 ? 0.9570 1.4847 1.0170 0.3056 -0.0225 0.0562 141 TYR B OH 3688 N N . HIS B 142 ? 1.0475 1.7548 0.9544 0.4001 -0.1233 -0.1484 142 HIS B N 3689 C CA . HIS B 142 ? 1.0725 1.8073 0.9556 0.4151 -0.1505 -0.1777 142 HIS B CA 3690 C C . HIS B 142 ? 1.0186 1.7409 0.9486 0.3750 -0.1447 -0.1504 142 HIS B C 3691 O O . HIS B 142 ? 0.9604 1.6321 0.9344 0.3308 -0.1304 -0.1277 142 HIS B O 3692 C CB . HIS B 142 ? 1.1153 1.8161 0.9865 0.4040 -0.1979 -0.2542 142 HIS B CB 3693 C CG . HIS B 142 ? 1.0871 1.7113 1.0118 0.3406 -0.2047 -0.2700 142 HIS B CG 3694 N ND1 . HIS B 142 ? 1.0517 1.6596 1.0287 0.2925 -0.2162 -0.2753 142 HIS B ND1 3695 C CD2 . HIS B 142 ? 1.0881 1.6521 1.0178 0.3250 -0.1977 -0.2761 142 HIS B CD2 3696 C CE1 . HIS B 142 ? 1.0314 1.5683 1.0400 0.2501 -0.2138 -0.2825 142 HIS B CE1 3697 N NE2 . HIS B 142 ? 1.0520 1.5581 1.0306 0.2690 -0.2044 -0.2846 142 HIS B NE2 3698 N N . LYS B 143 ? 1.0376 1.8064 0.9514 0.3978 -0.1575 -0.1539 143 LYS B N 3699 C CA . LYS B 143 ? 1.0205 1.7796 0.9725 0.3687 -0.1546 -0.1341 143 LYS B CA 3700 C C . LYS B 143 ? 0.9696 1.6884 0.9712 0.3154 -0.1798 -0.1759 143 LYS B C 3701 O O . LYS B 143 ? 1.0046 1.7302 1.0071 0.3098 -0.2142 -0.2304 143 LYS B O 3702 C CB . LYS B 143 ? 1.0762 1.9052 0.9998 0.4123 -0.1656 -0.1312 143 LYS B CB 3703 C CG . LYS B 143 ? 1.1621 2.0319 1.0261 0.4747 -0.1371 -0.0855 143 LYS B CG 3704 C CD . LYS B 143 ? 1.2039 2.1183 1.0434 0.5140 -0.1326 -0.0571 143 LYS B CD 3705 C CE . LYS B 143 ? 1.2326 2.2097 1.0775 0.5248 -0.1826 -0.1142 143 LYS B CE 3706 N NZ . LYS B 143 ? 1.1801 2.1381 1.0960 0.4697 -0.1952 -0.1272 143 LYS B NZ 3707 N N . CYS B 144 ? 0.8792 1.5497 0.9181 0.2785 -0.1621 -0.1490 144 CYS B N 3708 C CA . CYS B 144 ? 0.8210 1.4513 0.9055 0.2322 -0.1739 -0.1738 144 CYS B CA 3709 C C . CYS B 144 ? 0.7744 1.4231 0.8856 0.2264 -0.1667 -0.1515 144 CYS B C 3710 O O . CYS B 144 ? 0.7581 1.3656 0.8626 0.2262 -0.1421 -0.1121 144 CYS B O 3711 C CB . CYS B 144 ? 0.8025 1.3544 0.8931 0.2058 -0.1570 -0.1625 144 CYS B CB 3712 S SG . CYS B 144 ? 0.8044 1.2927 0.9346 0.1584 -0.1641 -0.1880 144 CYS B SG 3713 N N . ASP B 145 ? 0.7659 1.4791 0.9067 0.2252 -0.1912 -0.1780 145 ASP B N 3714 C CA . ASP B 145 ? 0.7545 1.5078 0.9256 0.2284 -0.1840 -0.1563 145 ASP B CA 3715 C C . ASP B 145 ? 0.7285 1.4354 0.9467 0.1867 -0.1701 -0.1501 145 ASP B C 3716 O O . ASP B 145 ? 0.7422 1.3794 0.9629 0.1575 -0.1661 -0.1607 145 ASP B O 3717 C CB . ASP B 145 ? 0.7721 1.6337 0.9681 0.2454 -0.2178 -0.1844 145 ASP B CB 3718 C CG . ASP B 145 ? 0.7912 1.6729 1.0450 0.2017 -0.2556 -0.2388 145 ASP B CG 3719 O OD1 . ASP B 145 ? 0.7979 1.6033 1.0677 0.1612 -0.2505 -0.2507 145 ASP B OD1 3720 O OD2 . ASP B 145 ? 0.8161 1.7874 1.0989 0.2086 -0.2937 -0.2705 145 ASP B OD2 3721 N N . ASN B 146 ? 0.6985 1.4464 0.9483 0.1918 -0.1596 -0.1292 146 ASN B N 3722 C CA . ASN B 146 ? 0.6800 1.3871 0.9633 0.1653 -0.1371 -0.1125 146 ASN B CA 3723 C C . ASN B 146 ? 0.6888 1.3939 1.0356 0.1137 -0.1503 -0.1422 146 ASN B C 3724 O O . ASN B 146 ? 0.7043 1.3352 1.0530 0.0912 -0.1309 -0.1329 146 ASN B O 3725 C CB . ASN B 146 ? 0.6591 1.4243 0.9605 0.1926 -0.1194 -0.0802 146 ASN B CB 3726 C CG . ASN B 146 ? 0.6611 1.3942 0.8880 0.2449 -0.1030 -0.0475 146 ASN B CG 3727 O OD1 . ASN B 146 ? 0.6653 1.3156 0.8362 0.2502 -0.0978 -0.0403 146 ASN B OD1 3728 N ND2 . ASN B 146 ? 0.6783 1.4778 0.9089 0.2835 -0.0950 -0.0257 146 ASN B ND2 3729 N N . GLU B 147 ? 0.7323 1.5112 1.1263 0.0969 -0.1858 -0.1790 147 GLU B N 3730 C CA . GLU B 147 ? 0.7843 1.5430 1.2355 0.0432 -0.2061 -0.2136 147 GLU B CA 3731 C C . GLU B 147 ? 0.7853 1.4337 1.1810 0.0356 -0.2067 -0.2332 147 GLU B C 3732 O O . GLU B 147 ? 0.8004 1.3793 1.2173 0.0003 -0.1975 -0.2361 147 GLU B O 3733 C CB . GLU B 147 ? 0.8421 1.6918 1.3412 0.0309 -0.2575 -0.2605 147 GLU B CB 3734 C CG . GLU B 147 ? 0.8558 1.8330 1.4401 0.0261 -0.2641 -0.2470 147 GLU B CG 3735 C CD . GLU B 147 ? 0.8837 1.8728 1.5765 -0.0357 -0.2525 -0.2350 147 GLU B CD 3736 O OE1 . GLU B 147 ? 0.8829 1.8126 1.5706 -0.0395 -0.2031 -0.1904 147 GLU B OE1 3737 O OE2 . GLU B 147 ? 0.9082 1.9662 1.6922 -0.0798 -0.2936 -0.2690 147 GLU B OE2 3738 N N . CYS B 148 ? 0.7735 1.4118 1.0988 0.0733 -0.2149 -0.2421 148 CYS B N 3739 C CA . CYS B 148 ? 0.7917 1.3464 1.0633 0.0782 -0.2126 -0.2547 148 CYS B CA 3740 C C . CYS B 148 ? 0.7626 1.2396 1.0184 0.0730 -0.1757 -0.2173 148 CYS B C 3741 O O . CYS B 148 ? 0.7962 1.1995 1.0472 0.0544 -0.1708 -0.2260 148 CYS B O 3742 C CB . CYS B 148 ? 0.8176 1.4027 1.0267 0.1258 -0.2198 -0.2572 148 CYS B CB 3743 S SG . CYS B 148 ? 0.8944 1.4100 1.0416 0.1459 -0.2079 -0.2567 148 CYS B SG 3744 N N . MET B 149 ? 0.7102 1.1982 0.9518 0.0938 -0.1528 -0.1779 149 MET B N 3745 C CA . MET B 149 ? 0.6929 1.1075 0.9122 0.0946 -0.1259 -0.1479 149 MET B CA 3746 C C . MET B 149 ? 0.7100 1.0896 0.9645 0.0668 -0.1118 -0.1437 149 MET B C 3747 O O . MET B 149 ? 0.7124 1.0157 0.9440 0.0617 -0.1012 -0.1406 149 MET B O 3748 C CB . MET B 149 ? 0.6726 1.0974 0.8683 0.1231 -0.1097 -0.1121 149 MET B CB 3749 C CG . MET B 149 ? 0.6685 1.1046 0.8256 0.1492 -0.1141 -0.1022 149 MET B CG 3750 S SD . MET B 149 ? 0.6776 1.0519 0.8057 0.1445 -0.1151 -0.1036 149 MET B SD 3751 C CE . MET B 149 ? 0.6739 1.0807 0.7763 0.1726 -0.1103 -0.0752 149 MET B CE 3752 N N . GLU B 150 ? 0.7278 1.1696 1.0410 0.0511 -0.1102 -0.1397 150 GLU B N 3753 C CA . GLU B 150 ? 0.7619 1.1834 1.1223 0.0225 -0.0893 -0.1250 150 GLU B CA 3754 C C . GLU B 150 ? 0.7871 1.1383 1.1546 -0.0104 -0.0991 -0.1515 150 GLU B C 3755 O O . GLU B 150 ? 0.7993 1.0831 1.1624 -0.0191 -0.0736 -0.1318 150 GLU B O 3756 C CB . GLU B 150 ? 0.7812 1.3068 1.2254 0.0053 -0.0897 -0.1163 150 GLU B CB 3757 C CG . GLU B 150 ? 0.8355 1.3597 1.3526 -0.0329 -0.0650 -0.0944 150 GLU B CG 3758 C CD . GLU B 150 ? 0.8741 1.3429 1.3527 -0.0060 -0.0167 -0.0463 150 GLU B CD 3759 O OE1 . GLU B 150 ? 0.8858 1.3296 1.2891 0.0422 -0.0069 -0.0317 150 GLU B OE1 3760 O OE2 . GLU B 150 ? 0.9356 1.3814 1.4572 -0.0316 0.0111 -0.0223 150 GLU B OE2 3761 N N . SER B 151 ? 0.7979 1.1576 1.1641 -0.0201 -0.1352 -0.1954 151 SER B N 3762 C CA . SER B 151 ? 0.8690 1.1502 1.2297 -0.0440 -0.1488 -0.2262 151 SER B CA 3763 C C . SER B 151 ? 0.8971 1.0886 1.1836 -0.0169 -0.1339 -0.2191 151 SER B C 3764 O O . SER B 151 ? 0.9582 1.0664 1.2332 -0.0292 -0.1290 -0.2266 151 SER B O 3765 C CB . SER B 151 ? 0.9024 1.2118 1.2629 -0.0480 -0.1955 -0.2803 151 SER B CB 3766 O OG . SER B 151 ? 0.8867 1.2054 1.1764 -0.0023 -0.2042 -0.2903 151 SER B OG 3767 N N . VAL B 152 ? 0.8624 1.0712 1.1021 0.0195 -0.1284 -0.2042 152 VAL B N 3768 C CA . VAL B 152 ? 0.8464 0.9901 1.0307 0.0433 -0.1172 -0.1937 152 VAL B CA 3769 C C . VAL B 152 ? 0.8696 0.9591 1.0491 0.0424 -0.0878 -0.1610 152 VAL B C 3770 O O . VAL B 152 ? 0.9019 0.9183 1.0501 0.0497 -0.0795 -0.1597 152 VAL B O 3771 C CB . VAL B 152 ? 0.7996 0.9800 0.9526 0.0728 -0.1207 -0.1821 152 VAL B CB 3772 C CG1 . VAL B 152 ? 0.8092 0.9359 0.9226 0.0912 -0.1149 -0.1716 152 VAL B CG1 3773 C CG2 . VAL B 152 ? 0.8070 1.0421 0.9547 0.0841 -0.1426 -0.2075 152 VAL B CG2 3774 N N . ARG B 153 ? 0.8636 0.9903 1.0669 0.0420 -0.0705 -0.1333 153 ARG B N 3775 C CA . ARG B 153 ? 0.9166 0.9991 1.1087 0.0507 -0.0383 -0.0989 153 ARG B CA 3776 C C . ARG B 153 ? 1.0006 1.0510 1.2356 0.0189 -0.0203 -0.0922 153 ARG B C 3777 O O . ARG B 153 ? 1.0504 1.0358 1.2577 0.0313 0.0073 -0.0667 153 ARG B O 3778 C CB . ARG B 153 ? 0.8830 1.0182 1.0839 0.0680 -0.0218 -0.0697 153 ARG B CB 3779 C CG . ARG B 153 ? 0.8338 0.9835 0.9922 0.0969 -0.0373 -0.0713 153 ARG B CG 3780 C CD . ARG B 153 ? 0.8437 1.0187 0.9913 0.1249 -0.0183 -0.0414 153 ARG B CD 3781 N NE . ARG B 153 ? 0.8293 1.0507 0.9713 0.1379 -0.0346 -0.0450 153 ARG B NE 3782 C CZ . ARG B 153 ? 0.8049 1.1134 0.9920 0.1343 -0.0368 -0.0436 153 ARG B CZ 3783 N NH1 . ARG B 153 ? 0.7932 1.1627 1.0489 0.1107 -0.0275 -0.0409 153 ARG B NH1 3784 N NH2 . ARG B 153 ? 0.8082 1.1449 0.9747 0.1547 -0.0491 -0.0428 153 ARG B NH2 3785 N N . ASN B 154 ? 1.0625 1.1563 1.3643 -0.0211 -0.0374 -0.1140 154 ASN B N 3786 C CA . ASN B 154 ? 1.1624 1.2197 1.5203 -0.0647 -0.0276 -0.1117 154 ASN B CA 3787 C C . ASN B 154 ? 1.2021 1.1423 1.5089 -0.0608 -0.0254 -0.1228 154 ASN B C 3788 O O . ASN B 154 ? 1.2783 1.1544 1.5964 -0.0742 0.0055 -0.0941 154 ASN B O 3789 C CB . ASN B 154 ? 1.2288 1.3422 1.6573 -0.1083 -0.0659 -0.1517 154 ASN B CB 3790 C CG . ASN B 154 ? 1.2964 1.5260 1.8129 -0.1299 -0.0619 -0.1329 154 ASN B CG 3791 O OD1 . ASN B 154 ? 1.3038 1.5806 1.8162 -0.1019 -0.0315 -0.0922 154 ASN B OD1 3792 N ND2 . ASN B 154 ? 1.4339 1.7116 2.0288 -0.1764 -0.0967 -0.1655 154 ASN B ND2 3793 N N . GLY B 155 ? 1.1495 1.0664 1.4001 -0.0378 -0.0551 -0.1601 155 GLY B N 3794 C CA . GLY B 155 ? 1.1803 1.0001 1.3893 -0.0341 -0.0649 -0.1848 155 GLY B CA 3795 C C . GLY B 155 ? 1.1877 1.0112 1.4251 -0.0635 -0.1048 -0.2357 155 GLY B C 3796 O O . GLY B 155 ? 1.2675 1.0028 1.4702 -0.0616 -0.1181 -0.2635 155 GLY B O 3797 N N . THR B 156 ? 1.1225 1.0453 1.4122 -0.0824 -0.1270 -0.2507 156 THR B N 3798 C CA . THR B 156 ? 1.1578 1.0963 1.4849 -0.1141 -0.1708 -0.3009 156 THR B CA 3799 C C . THR B 156 ? 1.1372 1.1243 1.4121 -0.0752 -0.2070 -0.3425 156 THR B C 3800 O O . THR B 156 ? 1.1998 1.1923 1.4814 -0.0865 -0.2493 -0.3921 156 THR B O 3801 C CB . THR B 156 ? 1.1378 1.1700 1.5699 -0.1611 -0.1741 -0.2885 156 THR B CB 3802 O OG1 . THR B 156 ? 1.1756 1.1673 1.6646 -0.1985 -0.1356 -0.2445 156 THR B OG1 3803 C CG2 . THR B 156 ? 1.2021 1.2632 1.6796 -0.1954 -0.2306 -0.3469 156 THR B CG2 3804 N N . TYR B 157 ? 1.1010 1.1225 1.3239 -0.0284 -0.1916 -0.3220 157 TYR B N 3805 C CA . TYR B 157 ? 1.0941 1.1768 1.2749 0.0107 -0.2154 -0.3468 157 TYR B CA 3806 C C . TYR B 157 ? 1.2098 1.2412 1.3448 0.0258 -0.2500 -0.4018 157 TYR B C 3807 O O . TYR B 157 ? 1.2489 1.2036 1.3280 0.0520 -0.2431 -0.4080 157 TYR B O 3808 C CB . TYR B 157 ? 1.0322 1.1308 1.1664 0.0528 -0.1915 -0.3146 157 TYR B CB 3809 C CG . TYR B 157 ? 1.0027 1.1655 1.0984 0.0939 -0.2062 -0.3282 157 TYR B CG 3810 C CD1 . TYR B 157 ? 0.9498 1.2032 1.0629 0.1004 -0.2123 -0.3203 157 TYR B CD1 3811 C CD2 . TYR B 157 ? 1.0321 1.1685 1.0709 0.1331 -0.2098 -0.3440 157 TYR B CD2 3812 C CE1 . TYR B 157 ? 0.9394 1.2503 1.0129 0.1431 -0.2189 -0.3242 157 TYR B CE1 3813 C CE2 . TYR B 157 ? 1.0178 1.2216 1.0223 0.1761 -0.2153 -0.3476 157 TYR B CE2 3814 C CZ . TYR B 157 ? 0.9687 1.2570 0.9900 0.1801 -0.2185 -0.3360 157 TYR B CZ 3815 O OH . TYR B 157 ? 0.9607 1.3139 0.9434 0.2277 -0.2173 -0.3315 157 TYR B OH 3816 N N . ASP B 158 ? 1.2870 1.3624 1.4396 0.0161 -0.2901 -0.4436 158 ASP B N 3817 C CA . ASP B 158 ? 1.4389 1.4563 1.5437 0.0303 -0.3328 -0.5062 158 ASP B CA 3818 C C . ASP B 158 ? 1.4798 1.5228 1.4932 0.1048 -0.3334 -0.5161 158 ASP B C 3819 O O . ASP B 158 ? 1.4620 1.5948 1.4569 0.1371 -0.3486 -0.5255 158 ASP B O 3820 C CB . ASP B 158 ? 1.4800 1.5441 1.6358 -0.0036 -0.3834 -0.5518 158 ASP B CB 3821 C CG . ASP B 158 ? 1.6183 1.5859 1.7371 -0.0080 -0.4350 -0.6229 158 ASP B CG 3822 O OD1 . ASP B 158 ? 1.6879 1.5352 1.7539 0.0038 -0.4248 -0.6304 158 ASP B OD1 3823 O OD2 . ASP B 158 ? 1.7001 1.7081 1.8382 -0.0199 -0.4895 -0.6741 158 ASP B OD2 3824 N N . TYR B 159 ? 1.5513 1.5207 1.5088 0.1362 -0.3135 -0.5091 159 TYR B N 3825 C CA . TYR B 159 ? 1.5745 1.5807 1.4592 0.2075 -0.3021 -0.5033 159 TYR B CA 3826 C C . TYR B 159 ? 1.6902 1.7148 1.5075 0.2569 -0.3410 -0.5579 159 TYR B C 3827 O O . TYR B 159 ? 1.6696 1.7916 1.4618 0.3020 -0.3337 -0.5430 159 TYR B O 3828 C CB . TYR B 159 ? 1.5981 1.5255 1.4419 0.2330 -0.2773 -0.4884 159 TYR B CB 3829 C CG . TYR B 159 ? 1.6281 1.5874 1.3976 0.3105 -0.2704 -0.4911 159 TYR B CG 3830 C CD1 . TYR B 159 ? 1.7520 1.6481 1.4388 0.3592 -0.2977 -0.5448 159 TYR B CD1 3831 C CD2 . TYR B 159 ? 1.5264 1.5794 1.3098 0.3365 -0.2368 -0.4391 159 TYR B CD2 3832 C CE1 . TYR B 159 ? 1.7800 1.7172 1.3963 0.4402 -0.2855 -0.5421 159 TYR B CE1 3833 C CE2 . TYR B 159 ? 1.5609 1.6617 1.2914 0.4063 -0.2248 -0.4327 159 TYR B CE2 3834 C CZ . TYR B 159 ? 1.6849 1.7332 1.3299 0.4623 -0.2462 -0.4821 159 TYR B CZ 3835 O OH . TYR B 159 ? 1.7091 1.8150 1.2985 0.5416 -0.2288 -0.4710 159 TYR B OH 3836 N N . PRO B 160 ? 1.8526 1.7781 1.6357 0.2512 -0.3831 -0.6206 160 PRO B N 3837 C CA . PRO B 160 ? 1.9728 1.9072 1.6779 0.3054 -0.4286 -0.6818 160 PRO B CA 3838 C C . PRO B 160 ? 1.9314 1.9793 1.6640 0.3018 -0.4562 -0.6937 160 PRO B C 3839 O O . PRO B 160 ? 1.9939 2.0813 1.6488 0.3675 -0.4820 -0.7281 160 PRO B O 3840 C CB . PRO B 160 ? 2.1153 1.9015 1.7983 0.2778 -0.4753 -0.7484 160 PRO B CB 3841 C CG . PRO B 160 ? 2.0958 1.7885 1.8082 0.2426 -0.4372 -0.7111 160 PRO B CG 3842 C CD . PRO B 160 ? 1.9311 1.7205 1.7330 0.2030 -0.3908 -0.6382 160 PRO B CD 3843 N N . GLN B 161 ? 1.8363 1.9380 1.6705 0.2353 -0.4496 -0.6644 161 GLN B N 3844 C CA . GLN B 161 ? 1.7879 2.0058 1.6518 0.2362 -0.4720 -0.6685 161 GLN B CA 3845 C C . GLN B 161 ? 1.6804 2.0024 1.5016 0.3011 -0.4338 -0.6189 161 GLN B C 3846 O O . GLN B 161 ? 1.7029 2.1079 1.4945 0.3408 -0.4553 -0.6326 161 GLN B O 3847 C CB . GLN B 161 ? 1.7171 1.9720 1.7009 0.1564 -0.4659 -0.6402 161 GLN B CB 3848 C CG . GLN B 161 ? 1.7019 2.0658 1.7259 0.1503 -0.5048 -0.6608 161 GLN B CG 3849 C CD . GLN B 161 ? 1.6250 2.0405 1.7693 0.0809 -0.4907 -0.6241 161 GLN B CD 3850 O OE1 . GLN B 161 ? 1.5843 1.9416 1.7812 0.0327 -0.4562 -0.5897 161 GLN B OE1 3851 N NE2 . GLN B 161 ? 1.6100 2.1403 1.7930 0.0841 -0.5155 -0.6289 161 GLN B NE2 3852 N N . TYR B 162 ? 1.5522 1.8696 1.3733 0.3110 -0.3787 -0.5602 162 TYR B N 3853 C CA . TYR B 162 ? 1.4663 1.8716 1.2602 0.3628 -0.3384 -0.5058 162 TYR B CA 3854 C C . TYR B 162 ? 1.4590 1.8402 1.1885 0.4186 -0.3126 -0.4946 162 TYR B C 3855 O O . TYR B 162 ? 1.4972 1.8934 1.1435 0.4883 -0.3251 -0.5221 162 TYR B O 3856 C CB . TYR B 162 ? 1.3601 1.7997 1.2297 0.3193 -0.2971 -0.4386 162 TYR B CB 3857 C CG . TYR B 162 ? 1.3345 1.7917 1.2774 0.2622 -0.3125 -0.4401 162 TYR B CG 3858 C CD1 . TYR B 162 ? 1.3251 1.8710 1.2755 0.2773 -0.3245 -0.4354 162 TYR B CD1 3859 C CD2 . TYR B 162 ? 1.3209 1.7134 1.3247 0.1998 -0.3101 -0.4396 162 TYR B CD2 3860 C CE1 . TYR B 162 ? 1.2908 1.8681 1.3128 0.2317 -0.3362 -0.4329 162 TYR B CE1 3861 C CE2 . TYR B 162 ? 1.2849 1.7086 1.3620 0.1526 -0.3173 -0.4331 162 TYR B CE2 3862 C CZ . TYR B 162 ? 1.2659 1.7860 1.3550 0.1684 -0.3312 -0.4306 162 TYR B CZ 3863 O OH . TYR B 162 ? 1.2102 1.7750 1.3760 0.1277 -0.3368 -0.4213 162 TYR B OH # _database_PDB_caveat.id 1 _database_PDB_caveat.text 'NAG B1154 HAS WRONG CHIRALITY AT ATOM C1' # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 ASP 1 1 1 ASP ASP A . n A 1 2 GLN 2 2 2 GLN GLN A . n A 1 3 ILE 3 3 3 ILE ILE A . n A 1 4 CYS 4 4 4 CYS CYS A . n A 1 5 ILE 5 5 5 ILE ILE A . n A 1 6 GLY 6 6 6 GLY GLY A . n A 1 7 TYR 7 7 7 TYR TYR A . n A 1 8 HIS 8 8 8 HIS HIS A . n A 1 9 ALA 9 9 9 ALA ALA A . n A 1 10 ASN 10 10 10 ASN ASN A . n A 1 11 ASN 11 11 11 ASN ASN A . n A 1 12 SER 12 12 12 SER SER A . n A 1 13 THR 13 13 13 THR THR A . n A 1 14 GLU 14 14 14 GLU GLU A . n A 1 15 GLN 15 15 15 GLN GLN A . n A 1 16 VAL 16 16 16 VAL VAL A . n A 1 17 ASP 17 17 17 ASP ASP A . n A 1 18 THR 18 18 18 THR THR A . n A 1 19 ILE 19 19 19 ILE ILE A . n A 1 20 MET 20 20 20 MET MET A . n A 1 21 GLU 21 21 21 GLU GLU A . n A 1 22 LYS 22 22 22 LYS LYS A . n A 1 23 ASN 23 23 23 ASN ASN A . n A 1 24 VAL 24 24 24 VAL VAL A . n A 1 25 THR 25 25 25 THR THR A . n A 1 26 VAL 26 26 26 VAL VAL A . n A 1 27 THR 27 27 27 THR THR A . n A 1 28 HIS 28 28 28 HIS HIS A . n A 1 29 ALA 29 29 29 ALA ALA A . n A 1 30 GLN 30 30 30 GLN GLN A . n A 1 31 ASP 31 31 31 ASP ASP A . n A 1 32 ILE 32 32 32 ILE ILE A . n A 1 33 LEU 33 33 33 LEU LEU A . n A 1 34 GLU 34 34 34 GLU GLU A . n A 1 35 LYS 35 35 35 LYS LYS A . n A 1 36 THR 36 36 36 THR THR A . n A 1 37 HIS 37 37 37 HIS HIS A . n A 1 38 ASN 38 38 38 ASN ASN A . n A 1 39 GLY 39 39 39 GLY GLY A . n A 1 40 LYS 40 40 40 LYS LYS A . n A 1 41 LEU 41 41 41 LEU LEU A . n A 1 42 CYS 42 42 42 CYS CYS A . n A 1 43 ASP 43 43 43 ASP ASP A . n A 1 44 LEU 44 44 44 LEU LEU A . n A 1 45 ASP 45 45 45 ASP ASP A . n A 1 46 GLY 46 46 46 GLY GLY A . n A 1 47 VAL 47 47 47 VAL VAL A . n A 1 48 LYS 48 48 48 LYS LYS A . n A 1 49 PRO 49 49 49 PRO PRO A . n A 1 50 LEU 50 50 50 LEU LEU A . n A 1 51 ILE 51 51 51 ILE ILE A . n A 1 52 LEU 52 52 52 LEU LEU A . n A 1 53 ARG 53 53 53 ARG ARG A . n A 1 54 ASP 54 54 54 ASP ASP A . n A 1 55 CYS 55 55 55 CYS CYS A . n A 1 56 SER 56 56 56 SER SER A . n A 1 57 VAL 57 57 57 VAL VAL A . n A 1 58 ALA 58 58 58 ALA ALA A . n A 1 59 GLY 59 59 59 GLY GLY A . n A 1 60 TRP 60 60 60 TRP TRP A . n A 1 61 LEU 61 61 61 LEU LEU A . n A 1 62 LEU 62 62 62 LEU LEU A . n A 1 63 GLY 63 63 63 GLY GLY A . n A 1 64 ASN 64 64 64 ASN ASN A . n A 1 65 PRO 65 65 65 PRO PRO A . n A 1 66 MET 66 66 66 MET MET A . n A 1 67 CYS 67 67 67 CYS CYS A . n A 1 68 ASP 68 68 68 ASP ASP A . n A 1 69 GLU 69 69 69 GLU GLU A . n A 1 70 PHE 70 70 70 PHE PHE A . n A 1 71 ILE 71 71 71 ILE ILE A . n A 1 72 ASN 72 72 72 ASN ASN A . n A 1 73 VAL 73 73 73 VAL VAL A . n A 1 74 PRO 74 74 74 PRO PRO A . n A 1 75 GLU 75 75 75 GLU GLU A . n A 1 76 TRP 76 76 76 TRP TRP A . n A 1 77 SER 77 77 77 SER SER A . n A 1 78 TYR 78 78 78 TYR TYR A . n A 1 79 ILE 79 79 79 ILE ILE A . n A 1 80 VAL 80 80 80 VAL VAL A . n A 1 81 GLU 81 81 81 GLU GLU A . n A 1 82 LYS 82 82 82 LYS LYS A . n A 1 83 ALA 83 83 83 ALA ALA A . n A 1 84 ASN 84 84 84 ASN ASN A . n A 1 85 PRO 85 85 85 PRO PRO A . n A 1 86 VAL 86 86 86 VAL VAL A . n A 1 87 ASN 87 87 87 ASN ASN A . n A 1 88 ASP 88 88 88 ASP ASP A . n A 1 89 LEU 89 89 89 LEU LEU A . n A 1 90 CYS 90 90 90 CYS CYS A . n A 1 91 TYR 91 91 91 TYR TYR A . n A 1 92 PRO 92 92 92 PRO PRO A . n A 1 93 GLY 93 93 93 GLY GLY A . n A 1 94 ASP 94 94 94 ASP ASP A . n A 1 95 PHE 95 95 95 PHE PHE A . n A 1 96 ASN 96 96 96 ASN ASN A . n A 1 97 ASP 97 97 97 ASP ASP A . n A 1 98 TYR 98 98 98 TYR TYR A . n A 1 99 GLU 99 99 99 GLU GLU A . n A 1 100 GLU 100 100 100 GLU GLU A . n A 1 101 LEU 101 101 101 LEU LEU A . n A 1 102 LYS 102 102 102 LYS LYS A . n A 1 103 HIS 103 103 103 HIS HIS A . n A 1 104 LEU 104 104 104 LEU LEU A . n A 1 105 LEU 105 105 105 LEU LEU A . n A 1 106 SER 106 106 106 SER SER A . n A 1 107 ARG 107 107 107 ARG ARG A . n A 1 108 ILE 108 108 108 ILE ILE A . n A 1 109 ASN 109 109 109 ASN ASN A . n A 1 110 HIS 110 110 110 HIS HIS A . n A 1 111 PHE 111 111 111 PHE PHE A . n A 1 112 GLU 112 112 112 GLU GLU A . n A 1 113 LYS 113 113 113 LYS LYS A . n A 1 114 ILE 114 114 114 ILE ILE A . n A 1 115 GLN 115 115 115 GLN GLN A . n A 1 116 ILE 116 116 116 ILE ILE A . n A 1 117 ILE 117 117 117 ILE ILE A . n A 1 118 PRO 118 118 118 PRO PRO A . n A 1 119 LYS 119 119 119 LYS LYS A . n A 1 120 SER 120 120 120 SER SER A . n A 1 121 SER 121 121 121 SER SER A . n A 1 122 TRP 122 122 122 TRP TRP A . n A 1 123 SER 123 123 123 SER SER A . n A 1 124 SER 124 124 124 SER SER A . n A 1 125 HIS 125 125 125 HIS HIS A . n A 1 126 GLU 126 126 126 GLU GLU A . n A 1 127 ALA 127 127 127 ALA ALA A . n A 1 128 SER 128 128 128 SER SER A . n A 1 129 LEU 129 129 129 LEU LEU A . n A 1 130 GLY 130 130 130 GLY GLY A . n A 1 131 VAL 131 131 131 VAL VAL A . n A 1 132 SER 132 132 132 SER SER A . n A 1 133 SER 133 133 133 SER SER A . n A 1 134 ALA 134 134 134 ALA ALA A . n A 1 135 CYS 135 135 135 CYS CYS A . n A 1 136 PRO 136 136 136 PRO PRO A . n A 1 137 TYR 137 137 137 TYR TYR A . n A 1 138 GLN 138 138 138 GLN GLN A . n A 1 139 GLY 139 139 139 GLY GLY A . n A 1 140 LYS 140 140 140 LYS LYS A . n A 1 141 SER 141 141 141 SER SER A . n A 1 142 SER 142 142 142 SER SER A . n A 1 143 PHE 143 143 143 PHE PHE A . n A 1 144 PHE 144 144 144 PHE PHE A . n A 1 145 ARG 145 145 145 ARG ARG A . n A 1 146 ASN 146 146 146 ASN ASN A . n A 1 147 VAL 147 147 147 VAL VAL A . n A 1 148 VAL 148 148 148 VAL VAL A . n A 1 149 TRP 149 149 149 TRP TRP A . n A 1 150 LEU 150 150 150 LEU LEU A . n A 1 151 ILE 151 151 151 ILE ILE A . n A 1 152 LYS 152 152 152 LYS LYS A . n A 1 153 LYS 153 153 153 LYS LYS A . n A 1 154 ASN 154 154 154 ASN ASN A . n A 1 155 SER 155 155 155 SER SER A . n A 1 156 THR 156 156 156 THR THR A . n A 1 157 TYR 157 157 157 TYR TYR A . n A 1 158 PRO 158 158 158 PRO PRO A . n A 1 159 THR 159 159 159 THR THR A . n A 1 160 ILE 160 160 160 ILE ILE A . n A 1 161 LYS 161 161 161 LYS LYS A . n A 1 162 ARG 162 162 162 ARG ARG A . n A 1 163 SER 163 163 163 SER SER A . n A 1 164 TYR 164 164 164 TYR TYR A . n A 1 165 ASN 165 165 165 ASN ASN A . n A 1 166 ASN 166 166 166 ASN ASN A . n A 1 167 THR 167 167 167 THR THR A . n A 1 168 ASN 168 168 168 ASN ASN A . n A 1 169 GLN 169 169 169 GLN GLN A . n A 1 170 GLU 170 170 170 GLU GLU A . n A 1 171 ASP 171 171 171 ASP ASP A . n A 1 172 LEU 172 172 172 LEU LEU A . n A 1 173 LEU 173 173 173 LEU LEU A . n A 1 174 VAL 174 174 174 VAL VAL A . n A 1 175 LEU 175 175 175 LEU LEU A . n A 1 176 TRP 176 176 176 TRP TRP A . n A 1 177 GLY 177 177 177 GLY GLY A . n A 1 178 ILE 178 178 178 ILE ILE A . n A 1 179 HIS 179 179 179 HIS HIS A . n A 1 180 HIS 180 180 180 HIS HIS A . n A 1 181 PRO 181 181 181 PRO PRO A . n A 1 182 ASN 182 182 182 ASN ASN A . n A 1 183 ASP 183 183 183 ASP ASP A . n A 1 184 ALA 184 184 184 ALA ALA A . n A 1 185 ALA 185 185 185 ALA ALA A . n A 1 186 GLU 186 186 186 GLU GLU A . n A 1 187 GLN 187 187 187 GLN GLN A . n A 1 188 THR 188 188 188 THR THR A . n A 1 189 LYS 189 189 189 LYS LYS A . n A 1 190 LEU 190 190 190 LEU LEU A . n A 1 191 TYR 191 191 191 TYR TYR A . n A 1 192 ARG 192 192 192 ARG ARG A . n A 1 193 ASN 193 193 193 ASN ASN A . n A 1 194 PRO 194 194 194 PRO PRO A . n A 1 195 THR 195 195 195 THR THR A . n A 1 196 THR 196 196 196 THR THR A . n A 1 197 TYR 197 197 197 TYR TYR A . n A 1 198 ILE 198 198 198 ILE ILE A . n A 1 199 SER 199 199 199 SER SER A . n A 1 200 VAL 200 200 200 VAL VAL A . n A 1 201 GLY 201 201 201 GLY GLY A . n A 1 202 THR 202 202 202 THR THR A . n A 1 203 SER 203 203 203 SER SER A . n A 1 204 THR 204 204 204 THR THR A . n A 1 205 LEU 205 205 205 LEU LEU A . n A 1 206 ASN 206 206 206 ASN ASN A . n A 1 207 GLN 207 207 207 GLN GLN A . n A 1 208 ARG 208 208 208 ARG ARG A . n A 1 209 LEU 209 209 209 LEU LEU A . n A 1 210 VAL 210 210 210 VAL VAL A . n A 1 211 PRO 211 211 211 PRO PRO A . n A 1 212 ARG 212 212 212 ARG ARG A . n A 1 213 ILE 213 213 213 ILE ILE A . n A 1 214 ALA 214 214 214 ALA ALA A . n A 1 215 THR 215 215 215 THR THR A . n A 1 216 ARG 216 216 216 ARG ARG A . n A 1 217 SER 217 217 217 SER SER A . n A 1 218 LYS 218 218 218 LYS LYS A . n A 1 219 VAL 219 219 219 VAL VAL A . n A 1 220 ASN 220 220 220 ASN ASN A . n A 1 221 GLY 221 221 221 GLY GLY A . n A 1 222 GLN 222 222 222 GLN GLN A . n A 1 223 ASN 223 223 223 ASN ASN A . n A 1 224 GLY 224 224 224 GLY GLY A . n A 1 225 ARG 225 225 225 ARG ARG A . n A 1 226 MET 226 226 226 MET MET A . n A 1 227 GLU 227 227 227 GLU GLU A . n A 1 228 PHE 228 228 228 PHE PHE A . n A 1 229 PHE 229 229 229 PHE PHE A . n A 1 230 TRP 230 230 230 TRP TRP A . n A 1 231 THR 231 231 231 THR THR A . n A 1 232 ILE 232 232 232 ILE ILE A . n A 1 233 LEU 233 233 233 LEU LEU A . n A 1 234 LYS 234 234 234 LYS LYS A . n A 1 235 PRO 235 235 235 PRO PRO A . n A 1 236 ASN 236 236 236 ASN ASN A . n A 1 237 ASP 237 237 237 ASP ASP A . n A 1 238 ALA 238 238 238 ALA ALA A . n A 1 239 ILE 239 239 239 ILE ILE A . n A 1 240 ASN 240 240 240 ASN ASN A . n A 1 241 PHE 241 241 241 PHE PHE A . n A 1 242 GLU 242 242 242 GLU GLU A . n A 1 243 SER 243 243 243 SER SER A . n A 1 244 ASN 244 244 244 ASN ASN A . n A 1 245 GLY 245 245 245 GLY GLY A . n A 1 246 ASN 246 246 246 ASN ASN A . n A 1 247 PHE 247 247 247 PHE PHE A . n A 1 248 ILE 248 248 248 ILE ILE A . n A 1 249 ALA 249 249 249 ALA ALA A . n A 1 250 PRO 250 250 250 PRO PRO A . n A 1 251 GLU 251 251 251 GLU GLU A . n A 1 252 TYR 252 252 252 TYR TYR A . n A 1 253 ALA 253 253 253 ALA ALA A . n A 1 254 TYR 254 254 254 TYR TYR A . n A 1 255 LYS 255 255 255 LYS LYS A . n A 1 256 ILE 256 256 256 ILE ILE A . n A 1 257 VAL 257 257 257 VAL VAL A . n A 1 258 LYS 258 258 258 LYS LYS A . n A 1 259 LYS 259 259 259 LYS LYS A . n A 1 260 GLY 260 260 260 GLY GLY A . n A 1 261 ASP 261 261 261 ASP ASP A . n A 1 262 SER 262 262 262 SER SER A . n A 1 263 THR 263 263 263 THR THR A . n A 1 264 ILE 264 264 264 ILE ILE A . n A 1 265 MET 265 265 265 MET MET A . n A 1 266 LYS 266 266 266 LYS LYS A . n A 1 267 SER 267 267 267 SER SER A . n A 1 268 GLU 268 268 268 GLU GLU A . n A 1 269 LEU 269 269 269 LEU LEU A . n A 1 270 GLU 270 270 270 GLU GLU A . n A 1 271 TYR 271 271 271 TYR TYR A . n A 1 272 GLY 272 272 272 GLY GLY A . n A 1 273 ASN 273 273 273 ASN ASN A . n A 1 274 CYS 274 274 274 CYS CYS A . n A 1 275 ASN 275 275 275 ASN ASN A . n A 1 276 THR 276 276 276 THR THR A . n A 1 277 LYS 277 277 277 LYS LYS A . n A 1 278 CYS 278 278 278 CYS CYS A . n A 1 279 GLN 279 279 279 GLN GLN A . n A 1 280 THR 280 280 280 THR THR A . n A 1 281 PRO 281 281 281 PRO PRO A . n A 1 282 MET 282 282 282 MET MET A . n A 1 283 GLY 283 283 283 GLY GLY A . n A 1 284 ALA 284 284 284 ALA ALA A . n A 1 285 ILE 285 285 285 ILE ILE A . n A 1 286 ASN 286 286 286 ASN ASN A . n A 1 287 SER 287 287 287 SER SER A . n A 1 288 SER 288 288 288 SER SER A . n A 1 289 MET 289 289 289 MET MET A . n A 1 290 PRO 290 290 290 PRO PRO A . n A 1 291 PHE 291 291 291 PHE PHE A . n A 1 292 HIS 292 292 292 HIS HIS A . n A 1 293 ASN 293 293 293 ASN ASN A . n A 1 294 ILE 294 294 294 ILE ILE A . n A 1 295 HIS 295 295 295 HIS HIS A . n A 1 296 PRO 296 296 296 PRO PRO A . n A 1 297 LEU 297 297 297 LEU LEU A . n A 1 298 THR 298 298 298 THR THR A . n A 1 299 ILE 299 299 299 ILE ILE A . n A 1 300 GLY 300 300 300 GLY GLY A . n A 1 301 GLU 301 301 301 GLU GLU A . n A 1 302 CYS 302 302 302 CYS CYS A . n A 1 303 PRO 303 303 303 PRO PRO A . n A 1 304 LYS 304 304 304 LYS LYS A . n A 1 305 TYR 305 305 305 TYR TYR A . n A 1 306 VAL 306 306 306 VAL VAL A . n A 1 307 LYS 307 307 307 LYS LYS A . n A 1 308 SER 308 308 308 SER SER A . n A 1 309 ASN 309 309 309 ASN ASN A . n A 1 310 ARG 310 310 310 ARG ARG A . n A 1 311 LEU 311 311 311 LEU LEU A . n A 1 312 VAL 312 312 312 VAL VAL A . n A 1 313 LEU 313 313 313 LEU LEU A . n A 1 314 ALA 314 314 314 ALA ALA A . n A 1 315 THR 315 315 315 THR THR A . n A 1 316 GLY 316 316 316 GLY GLY A . n A 1 317 LEU 317 317 317 LEU LEU A . n A 1 318 ARG 318 318 318 ARG ARG A . n A 1 319 ASN 319 319 319 ASN ASN A . n A 1 320 SER 320 320 320 SER SER A . n A 1 321 PRO 321 321 321 PRO PRO A . n A 1 322 GLN 322 322 ? ? ? A . n A 1 323 ARG 323 323 ? ? ? A . n A 1 324 GLU 324 324 ? ? ? A . n A 1 325 THR 325 325 ? ? ? A . n A 1 326 ARG 326 326 ? ? ? A . n B 2 1 GLY 1 1 1 GLY GLY B . n B 2 2 LEU 2 2 2 LEU LEU B . n B 2 3 PHE 3 3 3 PHE PHE B . n B 2 4 GLY 4 4 4 GLY GLY B . n B 2 5 ALA 5 5 5 ALA ALA B . n B 2 6 ILE 6 6 6 ILE ILE B . n B 2 7 ALA 7 7 7 ALA ALA B . n B 2 8 GLY 8 8 8 GLY GLY B . n B 2 9 PHE 9 9 9 PHE PHE B . n B 2 10 ILE 10 10 10 ILE ILE B . n B 2 11 GLU 11 11 11 GLU GLU B . n B 2 12 GLY 12 12 12 GLY GLY B . n B 2 13 GLY 13 13 13 GLY GLY B . n B 2 14 TRP 14 14 14 TRP TRP B . n B 2 15 GLN 15 15 15 GLN GLN B . n B 2 16 GLY 16 16 16 GLY GLY B . n B 2 17 MET 17 17 17 MET MET B . n B 2 18 VAL 18 18 18 VAL VAL B . n B 2 19 ASP 19 19 19 ASP ASP B . n B 2 20 GLY 20 20 20 GLY GLY B . n B 2 21 TRP 21 21 21 TRP TRP B . n B 2 22 TYR 22 22 22 TYR TYR B . n B 2 23 GLY 23 23 23 GLY GLY B . n B 2 24 TYR 24 24 24 TYR TYR B . n B 2 25 HIS 25 25 25 HIS HIS B . n B 2 26 HIS 26 26 26 HIS HIS B . n B 2 27 SER 27 27 27 SER SER B . n B 2 28 ASN 28 28 28 ASN ASN B . n B 2 29 GLU 29 29 29 GLU GLU B . n B 2 30 GLN 30 30 30 GLN GLN B . n B 2 31 GLY 31 31 31 GLY GLY B . n B 2 32 SER 32 32 32 SER SER B . n B 2 33 GLY 33 33 33 GLY GLY B . n B 2 34 TYR 34 34 34 TYR TYR B . n B 2 35 ALA 35 35 35 ALA ALA B . n B 2 36 ALA 36 36 36 ALA ALA B . n B 2 37 ASP 37 37 37 ASP ASP B . n B 2 38 LYS 38 38 38 LYS LYS B . n B 2 39 GLU 39 39 39 GLU GLU B . n B 2 40 SER 40 40 40 SER SER B . n B 2 41 THR 41 41 41 THR THR B . n B 2 42 GLN 42 42 42 GLN GLN B . n B 2 43 LYS 43 43 43 LYS LYS B . n B 2 44 ALA 44 44 44 ALA ALA B . n B 2 45 ILE 45 45 45 ILE ILE B . n B 2 46 ASP 46 46 46 ASP ASP B . n B 2 47 GLY 47 47 47 GLY GLY B . n B 2 48 VAL 48 48 48 VAL VAL B . n B 2 49 THR 49 49 49 THR THR B . n B 2 50 ASN 50 50 50 ASN ASN B . n B 2 51 LYS 51 51 51 LYS LYS B . n B 2 52 VAL 52 52 52 VAL VAL B . n B 2 53 ASN 53 53 53 ASN ASN B . n B 2 54 SER 54 54 54 SER SER B . n B 2 55 ILE 55 55 55 ILE ILE B . n B 2 56 ILE 56 56 56 ILE ILE B . n B 2 57 ASP 57 57 57 ASP ASP B . n B 2 58 LYS 58 58 58 LYS LYS B . n B 2 59 MET 59 59 59 MET MET B . n B 2 60 ASN 60 60 60 ASN ASN B . n B 2 61 THR 61 61 61 THR THR B . n B 2 62 GLN 62 62 62 GLN GLN B . n B 2 63 PHE 63 63 63 PHE PHE B . n B 2 64 GLU 64 64 64 GLU GLU B . n B 2 65 ALA 65 65 65 ALA ALA B . n B 2 66 VAL 66 66 66 VAL VAL B . n B 2 67 GLY 67 67 67 GLY GLY B . n B 2 68 ARG 68 68 68 ARG ARG B . n B 2 69 GLU 69 69 69 GLU GLU B . n B 2 70 PHE 70 70 70 PHE PHE B . n B 2 71 ASN 71 71 71 ASN ASN B . n B 2 72 ASN 72 72 72 ASN ASN B . n B 2 73 LEU 73 73 73 LEU LEU B . n B 2 74 GLU 74 74 74 GLU GLU B . n B 2 75 ARG 75 75 75 ARG ARG B . n B 2 76 ARG 76 76 76 ARG ARG B . n B 2 77 ILE 77 77 77 ILE ILE B . n B 2 78 GLU 78 78 78 GLU GLU B . n B 2 79 ASN 79 79 79 ASN ASN B . n B 2 80 LEU 80 80 80 LEU LEU B . n B 2 81 ASN 81 81 81 ASN ASN B . n B 2 82 LYS 82 82 82 LYS LYS B . n B 2 83 LYS 83 83 83 LYS LYS B . n B 2 84 MET 84 84 84 MET MET B . n B 2 85 GLU 85 85 85 GLU GLU B . n B 2 86 ASP 86 86 86 ASP ASP B . n B 2 87 GLY 87 87 87 GLY GLY B . n B 2 88 PHE 88 88 88 PHE PHE B . n B 2 89 LEU 89 89 89 LEU LEU B . n B 2 90 ASP 90 90 90 ASP ASP B . n B 2 91 VAL 91 91 91 VAL VAL B . n B 2 92 TRP 92 92 92 TRP TRP B . n B 2 93 THR 93 93 93 THR THR B . n B 2 94 TYR 94 94 94 TYR TYR B . n B 2 95 ASN 95 95 95 ASN ASN B . n B 2 96 ALA 96 96 96 ALA ALA B . n B 2 97 GLU 97 97 97 GLU GLU B . n B 2 98 LEU 98 98 98 LEU LEU B . n B 2 99 LEU 99 99 99 LEU LEU B . n B 2 100 VAL 100 100 100 VAL VAL B . n B 2 101 LEU 101 101 101 LEU LEU B . n B 2 102 MET 102 102 102 MET MET B . n B 2 103 GLU 103 103 103 GLU GLU B . n B 2 104 ASN 104 104 104 ASN ASN B . n B 2 105 GLU 105 105 105 GLU GLU B . n B 2 106 ARG 106 106 106 ARG ARG B . n B 2 107 THR 107 107 107 THR THR B . n B 2 108 LEU 108 108 108 LEU LEU B . n B 2 109 ASP 109 109 109 ASP ASP B . n B 2 110 PHE 110 110 110 PHE PHE B . n B 2 111 HIS 111 111 111 HIS HIS B . n B 2 112 ASP 112 112 112 ASP ASP B . n B 2 113 SER 113 113 113 SER SER B . n B 2 114 ASN 114 114 114 ASN ASN B . n B 2 115 VAL 115 115 115 VAL VAL B . n B 2 116 LYS 116 116 116 LYS LYS B . n B 2 117 ASN 117 117 117 ASN ASN B . n B 2 118 LEU 118 118 118 LEU LEU B . n B 2 119 TYR 119 119 119 TYR TYR B . n B 2 120 ASP 120 120 120 ASP ASP B . n B 2 121 LYS 121 121 121 LYS LYS B . n B 2 122 VAL 122 122 122 VAL VAL B . n B 2 123 ARG 123 123 123 ARG ARG B . n B 2 124 LEU 124 124 124 LEU LEU B . n B 2 125 GLN 125 125 125 GLN GLN B . n B 2 126 LEU 126 126 126 LEU LEU B . n B 2 127 ARG 127 127 127 ARG ARG B . n B 2 128 ASP 128 128 128 ASP ASP B . n B 2 129 ASN 129 129 129 ASN ASN B . n B 2 130 ALA 130 130 130 ALA ALA B . n B 2 131 LYS 131 131 131 LYS LYS B . n B 2 132 GLU 132 132 132 GLU GLU B . n B 2 133 LEU 133 133 133 LEU LEU B . n B 2 134 GLY 134 134 134 GLY GLY B . n B 2 135 ASN 135 135 135 ASN ASN B . n B 2 136 GLY 136 136 136 GLY GLY B . n B 2 137 CYS 137 137 137 CYS CYS B . n B 2 138 PHE 138 138 138 PHE PHE B . n B 2 139 GLU 139 139 139 GLU GLU B . n B 2 140 PHE 140 140 140 PHE PHE B . n B 2 141 TYR 141 141 141 TYR TYR B . n B 2 142 HIS 142 142 142 HIS HIS B . n B 2 143 LYS 143 143 143 LYS LYS B . n B 2 144 CYS 144 144 144 CYS CYS B . n B 2 145 ASP 145 145 145 ASP ASP B . n B 2 146 ASN 146 146 146 ASN ASN B . n B 2 147 GLU 147 147 147 GLU GLU B . n B 2 148 CYS 148 148 148 CYS CYS B . n B 2 149 MET 149 149 149 MET MET B . n B 2 150 GLU 150 150 150 GLU GLU B . n B 2 151 SER 151 151 151 SER SER B . n B 2 152 VAL 152 152 152 VAL VAL B . n B 2 153 ARG 153 153 153 ARG ARG B . n B 2 154 ASN 154 154 154 ASN ASN B . n B 2 155 GLY 155 155 155 GLY GLY B . n B 2 156 THR 156 156 156 THR THR B . n B 2 157 TYR 157 157 157 TYR TYR B . n B 2 158 ASP 158 158 158 ASP ASP B . n B 2 159 TYR 159 159 159 TYR TYR B . n B 2 160 PRO 160 160 160 PRO PRO B . n B 2 161 GLN 161 161 161 GLN GLN B . n B 2 162 TYR 162 162 162 TYR TYR B . n B 2 163 SER 163 163 ? ? ? B . n B 2 164 GLU 164 164 ? ? ? B . n B 2 165 GLU 165 165 ? ? ? B . n B 2 166 ALA 166 166 ? ? ? B . n # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code C 3 NAG 1 1011 1011 NAG NAG A . D 3 NAG 1 1023 1023 NAG NAG A . E 3 NAG 2 1024 1024 NAG NAG A . F 3 NAG 1 1165 1165 NAG NAG A . G 3 NAG 2 1166 1166 NAG NAG A . H 4 MAN 3 1167 1167 MAN MAN A . I 5 BMA 4 1168 1168 BMA BMA A . J 4 MAN 5 1169 1169 MAN MAN A . K 3 NAG 1 1286 1286 NAG NAG A . L 6 SIA 1 1322 1322 SIA SIA A . M 7 GAL 2 1323 1323 GAL GAL A . N 3 NAG 1 1154 1154 NAG NAG B . O 3 NAG 2 1155 1155 NAG NAG B . P 5 BMA 3 1156 1156 BMA BMA B . Q 8 MPO 1 1163 1163 MPO MPO B . R 9 HOH 1 2001 2001 HOH HOH A . R 9 HOH 2 2002 2002 HOH HOH A . R 9 HOH 3 2003 2003 HOH HOH A . R 9 HOH 4 2004 2004 HOH HOH A . R 9 HOH 5 2005 2005 HOH HOH A . R 9 HOH 6 2006 2006 HOH HOH A . R 9 HOH 7 2007 2007 HOH HOH A . R 9 HOH 8 2008 2008 HOH HOH A . R 9 HOH 9 2009 2009 HOH HOH A . R 9 HOH 10 2010 2010 HOH HOH A . R 9 HOH 11 2011 2011 HOH HOH A . R 9 HOH 12 2012 2012 HOH HOH A . R 9 HOH 13 2013 2013 HOH HOH A . R 9 HOH 14 2014 2014 HOH HOH A . R 9 HOH 15 2015 2015 HOH HOH A . R 9 HOH 16 2016 2016 HOH HOH A . R 9 HOH 17 2017 2017 HOH HOH A . R 9 HOH 18 2018 2018 HOH HOH A . R 9 HOH 19 2019 2019 HOH HOH A . R 9 HOH 20 2020 2020 HOH HOH A . R 9 HOH 21 2021 2021 HOH HOH A . R 9 HOH 22 2022 2022 HOH HOH A . R 9 HOH 23 2023 2023 HOH HOH A . R 9 HOH 24 2024 2024 HOH HOH A . R 9 HOH 25 2025 2025 HOH HOH A . R 9 HOH 26 2026 2026 HOH HOH A . R 9 HOH 27 2027 2027 HOH HOH A . R 9 HOH 28 2028 2028 HOH HOH A . R 9 HOH 29 2029 2029 HOH HOH A . R 9 HOH 30 2030 2030 HOH HOH A . R 9 HOH 31 2031 2031 HOH HOH A . R 9 HOH 32 2032 2032 HOH HOH A . R 9 HOH 33 2033 2033 HOH HOH A . R 9 HOH 34 2034 2034 HOH HOH A . R 9 HOH 35 2035 2035 HOH HOH A . R 9 HOH 36 2036 2036 HOH HOH A . R 9 HOH 37 2037 2037 HOH HOH A . R 9 HOH 38 2038 2038 HOH HOH A . R 9 HOH 39 2039 2039 HOH HOH A . R 9 HOH 40 2040 2040 HOH HOH A . R 9 HOH 41 2041 2041 HOH HOH A . R 9 HOH 42 2042 2042 HOH HOH A . R 9 HOH 43 2043 2043 HOH HOH A . R 9 HOH 44 2044 2044 HOH HOH A . R 9 HOH 45 2045 2045 HOH HOH A . R 9 HOH 46 2046 2046 HOH HOH A . R 9 HOH 47 2047 2047 HOH HOH A . R 9 HOH 48 2048 2048 HOH HOH A . R 9 HOH 49 2049 2049 HOH HOH A . R 9 HOH 50 2050 2050 HOH HOH A . S 9 HOH 1 2001 2001 HOH HOH B . S 9 HOH 2 2002 2002 HOH HOH B . S 9 HOH 3 2003 2003 HOH HOH B . S 9 HOH 4 2004 2004 HOH HOH B . S 9 HOH 5 2005 2005 HOH HOH B . S 9 HOH 6 2006 2006 HOH HOH B . S 9 HOH 7 2007 2007 HOH HOH B . S 9 HOH 8 2008 2008 HOH HOH B . S 9 HOH 9 2009 2009 HOH HOH B . S 9 HOH 10 2010 2010 HOH HOH B . S 9 HOH 11 2011 2011 HOH HOH B . S 9 HOH 12 2012 2012 HOH HOH B . S 9 HOH 13 2013 2013 HOH HOH B . S 9 HOH 14 2014 2014 HOH HOH B . S 9 HOH 15 2015 2015 HOH HOH B . S 9 HOH 16 2016 2016 HOH HOH B . S 9 HOH 17 2017 2017 HOH HOH B . S 9 HOH 18 2018 2018 HOH HOH B . S 9 HOH 19 2019 2019 HOH HOH B . S 9 HOH 20 2020 2020 HOH HOH B . S 9 HOH 21 2021 2021 HOH HOH B . S 9 HOH 22 2022 2022 HOH HOH B . S 9 HOH 23 2023 2023 HOH HOH B . S 9 HOH 24 2024 2024 HOH HOH B . S 9 HOH 25 2025 2025 HOH HOH B . S 9 HOH 26 2026 2026 HOH HOH B . S 9 HOH 27 2027 2027 HOH HOH B . S 9 HOH 28 2028 2028 HOH HOH B . S 9 HOH 29 2029 2029 HOH HOH B . S 9 HOH 30 2030 2030 HOH HOH B . S 9 HOH 31 2031 2031 HOH HOH B . S 9 HOH 32 2032 2032 HOH HOH B . S 9 HOH 33 2033 2033 HOH HOH B . S 9 HOH 34 2034 2034 HOH HOH B . S 9 HOH 35 2035 2035 HOH HOH B . S 9 HOH 36 2036 2036 HOH HOH B . S 9 HOH 37 2037 2037 HOH HOH B . S 9 HOH 38 2038 2038 HOH HOH B . S 9 HOH 39 2039 2039 HOH HOH B . S 9 HOH 40 2040 2040 HOH HOH B . S 9 HOH 41 2041 2041 HOH HOH B . S 9 HOH 42 2042 2042 HOH HOH B . S 9 HOH 43 2043 2043 HOH HOH B . S 9 HOH 44 2044 2044 HOH HOH B . S 9 HOH 45 2045 2045 HOH HOH B . S 9 HOH 46 2046 2046 HOH HOH B . S 9 HOH 47 2047 2047 HOH HOH B . # 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)' 37370 ? 1 MORE -44.2 ? 1 'SSA (A^2)' 65260 ? # 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 50.8340000000 0.8660254038 -0.5000000000 0.0000000000 -88.0470707520 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 101.6680000000 -0.8660254038 -0.5000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 # _pdbx_struct_special_symmetry.id 1 _pdbx_struct_special_symmetry.PDB_model_num 1 _pdbx_struct_special_symmetry.auth_asym_id B _pdbx_struct_special_symmetry.auth_comp_id HOH _pdbx_struct_special_symmetry.auth_seq_id 2026 _pdbx_struct_special_symmetry.PDB_ins_code ? _pdbx_struct_special_symmetry.label_asym_id S _pdbx_struct_special_symmetry.label_comp_id HOH _pdbx_struct_special_symmetry.label_seq_id . # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 2014-05-28 2 'Structure model' 1 1 2014-06-11 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # _pdbx_audit_revision_group.ordinal 1 _pdbx_audit_revision_group.revision_ordinal 2 _pdbx_audit_revision_group.data_content_type 'Structure model' _pdbx_audit_revision_group.group 'Database references' # loop_ _pdbx_refine_tls.pdbx_refine_id _pdbx_refine_tls.id _pdbx_refine_tls.details _pdbx_refine_tls.method _pdbx_refine_tls.origin_x _pdbx_refine_tls.origin_y _pdbx_refine_tls.origin_z _pdbx_refine_tls.T[1][1] _pdbx_refine_tls.T[2][2] _pdbx_refine_tls.T[3][3] _pdbx_refine_tls.T[1][2] _pdbx_refine_tls.T[1][3] _pdbx_refine_tls.T[2][3] _pdbx_refine_tls.L[1][1] _pdbx_refine_tls.L[2][2] _pdbx_refine_tls.L[3][3] _pdbx_refine_tls.L[1][2] _pdbx_refine_tls.L[1][3] _pdbx_refine_tls.L[2][3] _pdbx_refine_tls.S[1][1] _pdbx_refine_tls.S[1][2] _pdbx_refine_tls.S[1][3] _pdbx_refine_tls.S[2][1] _pdbx_refine_tls.S[2][2] _pdbx_refine_tls.S[2][3] _pdbx_refine_tls.S[3][1] _pdbx_refine_tls.S[3][2] _pdbx_refine_tls.S[3][3] 'X-RAY DIFFRACTION' 1 ? refined 34.5203 -14.0691 -18.8573 0.1377 0.4271 0.2169 0.0944 0.0368 -0.1270 0.5124 0.4495 5.2282 -0.0622 -0.4669 0.4571 0.0170 -0.2216 0.1138 0.1184 -0.1666 0.1331 -0.5394 -1.0119 0.1496 'X-RAY DIFFRACTION' 2 ? refined 32.3607 -21.6122 16.6069 0.6887 0.9157 0.1349 -0.0369 0.1479 -0.1383 1.6607 2.9296 1.7163 0.1593 0.1589 -0.6186 -0.0552 -0.3411 0.0935 1.1262 -0.1159 0.0112 0.0579 -0.5116 0.1711 'X-RAY DIFFRACTION' 3 ? refined 35.7265 -14.7544 -27.0627 0.2359 0.2989 0.3203 0.0727 0.0396 -0.0782 1.0236 0.2904 10.3099 -0.0915 -0.6816 1.6279 0.1609 -0.3434 0.2282 0.0427 -0.0604 0.0783 0.2198 -0.4330 -0.1005 'X-RAY DIFFRACTION' 4 ? refined 36.3635 -20.9580 -58.9358 0.1825 0.2778 0.4633 0.0853 -0.0048 -0.0539 2.0984 1.6088 8.4774 -1.4103 2.5911 -1.1402 -0.0478 0.1150 -0.0203 0.2204 -0.1090 0.0907 -0.2049 -1.0059 0.1568 'X-RAY DIFFRACTION' 5 ? refined 48.3076 -22.7774 -10.4117 0.1101 0.0655 0.0639 0.0160 -0.0172 -0.0245 7.1562 3.6383 14.7586 2.0036 3.2226 1.9973 0.0746 -0.0802 0.1138 0.1569 -0.2111 0.3641 -0.6704 -0.6386 0.1365 'X-RAY DIFFRACTION' 6 ? refined 44.6940 -23.9932 -56.9374 0.0561 0.1328 0.2559 0.0090 -0.0040 -0.0204 1.5522 0.7273 13.7668 -0.5903 2.4072 -0.9316 0.0186 0.1302 0.0846 0.0178 -0.2851 0.0544 0.4429 0.1942 0.2665 'X-RAY DIFFRACTION' 7 ? refined 31.6735 -26.0638 -80.9426 0.3215 0.7195 0.5229 0.0740 -0.2192 -0.2972 7.2881 7.3623 10.2383 -5.9521 0.5344 -1.8412 0.6244 1.6093 -1.2900 -0.4989 -0.4328 1.1954 1.1380 -0.9759 -0.1916 # 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 4CQQ _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 ? ? 62.47 -116.88 2 1 ASP A 88 ? ? -97.86 -122.36 3 1 CYS A 135 ? ? -114.55 71.95 4 1 ARG A 192 ? ? 69.28 -63.74 5 1 THR A 202 ? ? -127.47 -162.37 6 1 GLU A 251 ? ? -107.61 -61.83 7 1 ASN A 273 ? ? 60.96 74.50 8 1 ARG B 127 ? ? 53.64 -127.80 9 1 TYR B 157 ? ? -47.27 107.15 # _pdbx_validate_chiral.id 1 _pdbx_validate_chiral.PDB_model_num 1 _pdbx_validate_chiral.auth_atom_id C1 _pdbx_validate_chiral.label_alt_id ? _pdbx_validate_chiral.auth_asym_id B _pdbx_validate_chiral.auth_comp_id NAG _pdbx_validate_chiral.auth_seq_id 1154 _pdbx_validate_chiral.PDB_ins_code ? _pdbx_validate_chiral.details 'WRONG HAND' _pdbx_validate_chiral.omega . # loop_ _pdbx_unobs_or_zero_occ_residues.id _pdbx_unobs_or_zero_occ_residues.PDB_model_num _pdbx_unobs_or_zero_occ_residues.polymer_flag _pdbx_unobs_or_zero_occ_residues.occupancy_flag _pdbx_unobs_or_zero_occ_residues.auth_asym_id _pdbx_unobs_or_zero_occ_residues.auth_comp_id _pdbx_unobs_or_zero_occ_residues.auth_seq_id _pdbx_unobs_or_zero_occ_residues.PDB_ins_code _pdbx_unobs_or_zero_occ_residues.label_asym_id _pdbx_unobs_or_zero_occ_residues.label_comp_id _pdbx_unobs_or_zero_occ_residues.label_seq_id 1 1 Y 1 A GLN 322 ? A GLN 322 2 1 Y 1 A ARG 323 ? A ARG 323 3 1 Y 1 A GLU 324 ? A GLU 324 4 1 Y 1 A THR 325 ? A THR 325 5 1 Y 1 A ARG 326 ? A ARG 326 6 1 Y 1 B SER 163 ? B SER 163 7 1 Y 1 B GLU 164 ? B GLU 164 8 1 Y 1 B GLU 165 ? B GLU 165 9 1 Y 1 B ALA 166 ? B ALA 166 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 3 N-ACETYL-D-GLUCOSAMINE NAG 4 ALPHA-D-MANNOSE MAN 5 BETA-D-MANNOSE BMA 6 'O-SIALIC ACID' SIA 7 BETA-D-GALACTOSE GAL 8 '3[N-MORPHOLINO]PROPANE SULFONIC ACID' MPO 9 water HOH #