data_5AJM # _entry.id 5AJM # _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 5AJM PDBE EBI-63142 WWPDB D_1290063142 # _pdbx_database_PDB_obs_spr.id SPRSDE _pdbx_database_PDB_obs_spr.date 2015-03-25 _pdbx_database_PDB_obs_spr.pdb_id 5AJM _pdbx_database_PDB_obs_spr.replace_pdb_id 4CQT _pdbx_database_PDB_obs_spr.details ? # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 5AJM _pdbx_database_status.deposit_site PDBE _pdbx_database_status.process_site PDBE _pdbx_database_status.SG_entry . _pdbx_database_status.recvd_initial_deposition_date 2015-02-25 _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 5AJM _cell.length_a 101.580 _cell.length_b 101.580 _cell.length_c 452.980 _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 5AJM _symmetry.space_group_name_H-M 'H 3 2' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 155 # loop_ _entity.id _entity.type _entity.src_method _entity.pdbx_description _entity.formula_weight _entity.pdbx_number_of_molecules _entity.pdbx_ec _entity.pdbx_mutation _entity.pdbx_fragment _entity.details 1 polymer nat 'HAEMAGGLUTININ HA1' 36965.844 1 ? ? '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 9 ? ? ? ? 4 non-polymer man BETA-D-MANNOSE 180.156 2 ? ? ? ? 5 non-polymer man ALPHA-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 18.015 163 ? ? ? ? # loop_ _entity_poly.entity_id _entity_poly.type _entity_poly.nstd_linkage _entity_poly.nstd_monomer _entity_poly.pdbx_seq_one_letter_code _entity_poly.pdbx_seq_one_letter_code_can _entity_poly.pdbx_strand_id _entity_poly.pdbx_target_identifier 1 'polypeptide(L)' no no ;DQICIGYHANNSTEQVDTIMEKNVTVTHAQDILEKTHNGKLCDLDGVKPLILRDCSVAGWLLGNPMCDEFINVPEWSYIV EKANPVNDLCYPGDFNDYEELKHLLSRINHFEKIQIIPKSSWSSHEASLGVSSACPYQGKSSFFRNVVWLIKKNSTYPTI KRSYNNTNQEDLLVLWGIHHPKDAAEQTKLYQNPTTYISVGTSTLNQRLVPRIATRSKVNGQSGRMEFFWTILKPNDAIN FESNGNFIAPEYAYKIVKKGDSTIMKSELEYGNCNTKCQTPMGAINSSMPFHNIHPLTIGECPKYVKSNRLVLATGLRNS PQRETR ; ;DQICIGYHANNSTEQVDTIMEKNVTVTHAQDILEKTHNGKLCDLDGVKPLILRDCSVAGWLLGNPMCDEFINVPEWSYIV EKANPVNDLCYPGDFNDYEELKHLLSRINHFEKIQIIPKSSWSSHEASLGVSSACPYQGKSSFFRNVVWLIKKNSTYPTI KRSYNNTNQEDLLVLWGIHHPKDAAEQTKLYQNPTTYISVGTSTLNQRLVPRIATRSKVNGQSGRMEFFWTILKPNDAIN FESNGNFIAPEYAYKIVKKGDSTIMKSELEYGNCNTKCQTPMGAINSSMPFHNIHPLTIGECPKYVKSNRLVLATGLRNS PQRETR ; A ? 2 'polypeptide(L)' no no ;GLFGAIAGFIEGGWQGMVDGWYGYHHSNEQGSGYAADKESTQKAIDGVTNKVNSIIDKMNTQFEAVGREFNNLERRIENL NKKMEDGFLDVWTYNAELLVLMENERTLDFHDSNVKNLYDKVRLQLRDNAKELGNGCFEFYHKCDNECMESVRNGTYDYP QYSEEA ; ;GLFGAIAGFIEGGWQGMVDGWYGYHHSNEQGSGYAADKESTQKAIDGVTNKVNSIIDKMNTQFEAVGREFNNLERRIENL NKKMEDGFLDVWTYNAELLVLMENERTLDFHDSNVKNLYDKVRLQLRDNAKELGNGCFEFYHKCDNECMESVRNGTYDYP QYSEEA ; B ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 ASP n 1 2 GLN n 1 3 ILE n 1 4 CYS n 1 5 ILE n 1 6 GLY n 1 7 TYR n 1 8 HIS n 1 9 ALA n 1 10 ASN n 1 11 ASN n 1 12 SER n 1 13 THR n 1 14 GLU n 1 15 GLN n 1 16 VAL n 1 17 ASP n 1 18 THR n 1 19 ILE n 1 20 MET n 1 21 GLU n 1 22 LYS n 1 23 ASN n 1 24 VAL n 1 25 THR n 1 26 VAL n 1 27 THR n 1 28 HIS n 1 29 ALA n 1 30 GLN n 1 31 ASP n 1 32 ILE n 1 33 LEU n 1 34 GLU n 1 35 LYS n 1 36 THR n 1 37 HIS n 1 38 ASN n 1 39 GLY n 1 40 LYS n 1 41 LEU n 1 42 CYS n 1 43 ASP n 1 44 LEU n 1 45 ASP n 1 46 GLY n 1 47 VAL n 1 48 LYS n 1 49 PRO n 1 50 LEU n 1 51 ILE n 1 52 LEU n 1 53 ARG n 1 54 ASP n 1 55 CYS n 1 56 SER n 1 57 VAL n 1 58 ALA n 1 59 GLY n 1 60 TRP n 1 61 LEU n 1 62 LEU n 1 63 GLY n 1 64 ASN n 1 65 PRO n 1 66 MET n 1 67 CYS n 1 68 ASP n 1 69 GLU n 1 70 PHE n 1 71 ILE n 1 72 ASN n 1 73 VAL n 1 74 PRO n 1 75 GLU n 1 76 TRP n 1 77 SER n 1 78 TYR n 1 79 ILE n 1 80 VAL n 1 81 GLU n 1 82 LYS n 1 83 ALA n 1 84 ASN n 1 85 PRO n 1 86 VAL n 1 87 ASN n 1 88 ASP n 1 89 LEU n 1 90 CYS n 1 91 TYR n 1 92 PRO n 1 93 GLY n 1 94 ASP n 1 95 PHE n 1 96 ASN n 1 97 ASP n 1 98 TYR n 1 99 GLU n 1 100 GLU n 1 101 LEU n 1 102 LYS n 1 103 HIS n 1 104 LEU n 1 105 LEU n 1 106 SER n 1 107 ARG n 1 108 ILE n 1 109 ASN n 1 110 HIS n 1 111 PHE n 1 112 GLU n 1 113 LYS n 1 114 ILE n 1 115 GLN n 1 116 ILE n 1 117 ILE n 1 118 PRO n 1 119 LYS n 1 120 SER n 1 121 SER n 1 122 TRP n 1 123 SER n 1 124 SER n 1 125 HIS n 1 126 GLU n 1 127 ALA n 1 128 SER n 1 129 LEU n 1 130 GLY n 1 131 VAL n 1 132 SER n 1 133 SER n 1 134 ALA n 1 135 CYS n 1 136 PRO n 1 137 TYR n 1 138 GLN n 1 139 GLY n 1 140 LYS n 1 141 SER n 1 142 SER n 1 143 PHE n 1 144 PHE n 1 145 ARG n 1 146 ASN n 1 147 VAL n 1 148 VAL n 1 149 TRP n 1 150 LEU n 1 151 ILE n 1 152 LYS n 1 153 LYS n 1 154 ASN n 1 155 SER n 1 156 THR n 1 157 TYR n 1 158 PRO n 1 159 THR n 1 160 ILE n 1 161 LYS n 1 162 ARG n 1 163 SER n 1 164 TYR n 1 165 ASN n 1 166 ASN n 1 167 THR n 1 168 ASN n 1 169 GLN n 1 170 GLU n 1 171 ASP n 1 172 LEU n 1 173 LEU n 1 174 VAL n 1 175 LEU n 1 176 TRP n 1 177 GLY n 1 178 ILE n 1 179 HIS n 1 180 HIS n 1 181 PRO n 1 182 LYS n 1 183 ASP n 1 184 ALA n 1 185 ALA n 1 186 GLU n 1 187 GLN n 1 188 THR n 1 189 LYS n 1 190 LEU n 1 191 TYR n 1 192 GLN n 1 193 ASN n 1 194 PRO n 1 195 THR n 1 196 THR n 1 197 TYR n 1 198 ILE n 1 199 SER n 1 200 VAL n 1 201 GLY n 1 202 THR n 1 203 SER n 1 204 THR n 1 205 LEU n 1 206 ASN n 1 207 GLN n 1 208 ARG n 1 209 LEU n 1 210 VAL n 1 211 PRO n 1 212 ARG n 1 213 ILE n 1 214 ALA n 1 215 THR n 1 216 ARG n 1 217 SER n 1 218 LYS n 1 219 VAL n 1 220 ASN n 1 221 GLY n 1 222 GLN n 1 223 SER n 1 224 GLY n 1 225 ARG n 1 226 MET n 1 227 GLU n 1 228 PHE n 1 229 PHE n 1 230 TRP n 1 231 THR n 1 232 ILE n 1 233 LEU n 1 234 LYS n 1 235 PRO n 1 236 ASN n 1 237 ASP n 1 238 ALA n 1 239 ILE n 1 240 ASN n 1 241 PHE n 1 242 GLU n 1 243 SER n 1 244 ASN n 1 245 GLY n 1 246 ASN n 1 247 PHE n 1 248 ILE n 1 249 ALA n 1 250 PRO n 1 251 GLU n 1 252 TYR n 1 253 ALA n 1 254 TYR n 1 255 LYS n 1 256 ILE n 1 257 VAL n 1 258 LYS n 1 259 LYS n 1 260 GLY n 1 261 ASP n 1 262 SER n 1 263 THR n 1 264 ILE n 1 265 MET n 1 266 LYS n 1 267 SER n 1 268 GLU n 1 269 LEU n 1 270 GLU n 1 271 TYR n 1 272 GLY n 1 273 ASN n 1 274 CYS n 1 275 ASN n 1 276 THR n 1 277 LYS n 1 278 CYS n 1 279 GLN n 1 280 THR n 1 281 PRO n 1 282 MET n 1 283 GLY n 1 284 ALA n 1 285 ILE n 1 286 ASN n 1 287 SER n 1 288 SER n 1 289 MET n 1 290 PRO n 1 291 PHE n 1 292 HIS n 1 293 ASN n 1 294 ILE n 1 295 HIS n 1 296 PRO n 1 297 LEU n 1 298 THR n 1 299 ILE n 1 300 GLY n 1 301 GLU n 1 302 CYS n 1 303 PRO n 1 304 LYS n 1 305 TYR n 1 306 VAL n 1 307 LYS n 1 308 SER n 1 309 ASN n 1 310 ARG n 1 311 LEU n 1 312 VAL n 1 313 LEU n 1 314 ALA n 1 315 THR n 1 316 GLY n 1 317 LEU n 1 318 ARG n 1 319 ASN n 1 320 SER n 1 321 PRO n 1 322 GLN n 1 323 ARG n 1 324 GLU n 1 325 THR n 1 326 ARG n 2 1 GLY n 2 2 LEU n 2 3 PHE n 2 4 GLY n 2 5 ALA n 2 6 ILE n 2 7 ALA n 2 8 GLY n 2 9 PHE n 2 10 ILE n 2 11 GLU n 2 12 GLY n 2 13 GLY n 2 14 TRP n 2 15 GLN n 2 16 GLY n 2 17 MET n 2 18 VAL n 2 19 ASP n 2 20 GLY n 2 21 TRP n 2 22 TYR n 2 23 GLY n 2 24 TYR n 2 25 HIS n 2 26 HIS n 2 27 SER n 2 28 ASN n 2 29 GLU n 2 30 GLN n 2 31 GLY n 2 32 SER n 2 33 GLY n 2 34 TYR n 2 35 ALA n 2 36 ALA n 2 37 ASP n 2 38 LYS n 2 39 GLU n 2 40 SER n 2 41 THR n 2 42 GLN n 2 43 LYS n 2 44 ALA n 2 45 ILE n 2 46 ASP n 2 47 GLY n 2 48 VAL n 2 49 THR n 2 50 ASN n 2 51 LYS n 2 52 VAL n 2 53 ASN n 2 54 SER n 2 55 ILE n 2 56 ILE n 2 57 ASP n 2 58 LYS n 2 59 MET n 2 60 ASN n 2 61 THR n 2 62 GLN n 2 63 PHE n 2 64 GLU n 2 65 ALA n 2 66 VAL n 2 67 GLY n 2 68 ARG n 2 69 GLU n 2 70 PHE n 2 71 ASN n 2 72 ASN n 2 73 LEU n 2 74 GLU n 2 75 ARG n 2 76 ARG n 2 77 ILE n 2 78 GLU n 2 79 ASN n 2 80 LEU n 2 81 ASN n 2 82 LYS n 2 83 LYS n 2 84 MET n 2 85 GLU n 2 86 ASP n 2 87 GLY n 2 88 PHE n 2 89 LEU n 2 90 ASP n 2 91 VAL n 2 92 TRP n 2 93 THR n 2 94 TYR n 2 95 ASN n 2 96 ALA n 2 97 GLU n 2 98 LEU n 2 99 LEU n 2 100 VAL n 2 101 LEU n 2 102 MET n 2 103 GLU n 2 104 ASN n 2 105 GLU n 2 106 ARG n 2 107 THR n 2 108 LEU n 2 109 ASP n 2 110 PHE n 2 111 HIS n 2 112 ASP n 2 113 SER n 2 114 ASN n 2 115 VAL n 2 116 LYS n 2 117 ASN n 2 118 LEU n 2 119 TYR n 2 120 ASP n 2 121 LYS n 2 122 VAL n 2 123 ARG n 2 124 LEU n 2 125 GLN n 2 126 LEU n 2 127 ARG n 2 128 ASP n 2 129 ASN n 2 130 ALA n 2 131 LYS n 2 132 GLU n 2 133 LEU n 2 134 GLY n 2 135 ASN n 2 136 GLY n 2 137 CYS n 2 138 PHE n 2 139 GLU n 2 140 PHE n 2 141 TYR n 2 142 HIS n 2 143 LYS n 2 144 CYS n 2 145 ASP n 2 146 ASN n 2 147 GLU n 2 148 CYS n 2 149 MET n 2 150 GLU n 2 151 SER n 2 152 VAL n 2 153 ARG n 2 154 ASN n 2 155 GLY n 2 156 THR n 2 157 TYR n 2 158 ASP n 2 159 TYR n 2 160 PRO n 2 161 GLN n 2 162 TYR n 2 163 SER n 2 164 GLU n 2 165 GLU n 2 166 ALA n # loop_ _entity_src_nat.entity_id _entity_src_nat.pdbx_src_id _entity_src_nat.pdbx_alt_source_flag _entity_src_nat.pdbx_beg_seq_num _entity_src_nat.pdbx_end_seq_num _entity_src_nat.common_name _entity_src_nat.pdbx_organism_scientific _entity_src_nat.pdbx_ncbi_taxonomy_id _entity_src_nat.genus _entity_src_nat.species _entity_src_nat.strain _entity_src_nat.tissue _entity_src_nat.tissue_fraction _entity_src_nat.pdbx_secretion _entity_src_nat.pdbx_fragment _entity_src_nat.pdbx_variant _entity_src_nat.pdbx_cell_line _entity_src_nat.pdbx_atcc _entity_src_nat.pdbx_cellular_location _entity_src_nat.pdbx_organ _entity_src_nat.pdbx_organelle _entity_src_nat.pdbx_cell _entity_src_nat.pdbx_plasmid_name _entity_src_nat.pdbx_plasmid_details _entity_src_nat.details 1 1 sample ? ? ? 'INFLUENZA A VIRUS (A/VIETNAM/1194/2004(H5N1))' 644788 ? ? ? ? ? ? ? 'ASN186LYS MUTANT' ? ? ? ? ? ? ? ? ? 2 1 sample ? ? ? 'INFLUENZA A VIRUS (A/VIETNAM/1194/2004(H5N1))' 644788 ? ? ? ? ? ? ? 'ASN186LYS MUTANT' ? ? ? ? ? ? ? ? ? # loop_ _struct_ref.id _struct_ref.db_name _struct_ref.db_code _struct_ref.entity_id _struct_ref.pdbx_seq_one_letter_code _struct_ref.pdbx_align_begin _struct_ref.pdbx_db_accession _struct_ref.pdbx_db_isoform 1 UNP Q6DQ34_9INFA 1 ? ? Q6DQ34 ? 2 UNP Q6DQ34_9INFA 2 ? ? Q6DQ34 ? # loop_ _struct_ref_seq.align_id _struct_ref_seq.ref_id _struct_ref_seq.pdbx_PDB_id_code _struct_ref_seq.pdbx_strand_id _struct_ref_seq.seq_align_beg _struct_ref_seq.pdbx_seq_align_beg_ins_code _struct_ref_seq.seq_align_end _struct_ref_seq.pdbx_seq_align_end_ins_code _struct_ref_seq.pdbx_db_accession _struct_ref_seq.db_align_beg _struct_ref_seq.pdbx_db_align_beg_ins_code _struct_ref_seq.db_align_end _struct_ref_seq.pdbx_db_align_end_ins_code _struct_ref_seq.pdbx_auth_seq_align_beg _struct_ref_seq.pdbx_auth_seq_align_end 1 1 5AJM A 1 ? 324 ? Q6DQ34 17 ? 340 ? 1 324 2 2 5AJM 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 5AJM THR A 325 ? UNP Q6DQ34 ? ? 'expression tag' 325 1 1 5AJM ARG A 326 ? UNP Q6DQ34 ? ? 'expression tag' 326 2 1 5AJM LYS A 182 ? UNP Q6DQ34 ASN 198 conflict 182 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 5AJM _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 3.74 _exptl_crystal.density_percent_sol 67 _exptl_crystal.description NONE # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method ? _exptl_crystal_grow.temp ? _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH ? _exptl_crystal_grow.pdbx_pH_range ? _exptl_crystal_grow.pdbx_details '0.1 M HEPES/MOPS PH 7.0, 0.05 M MGCL2, 28-30% PEG 550 MME, SEEDED WITH CRUSHED WILD-TYPE VN1194 HA CRYSTALS.' # _diffrn.id 1 _diffrn.ambient_temp 100 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector PIXEL _diffrn_detector.type 'DECTRIS PILATUS' _diffrn_detector.pdbx_collection_date ? _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator ? _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 0.92 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'DIAMOND BEAMLINE I04-1' _diffrn_source.pdbx_synchrotron_site Diamond _diffrn_source.pdbx_synchrotron_beamline I04-1 _diffrn_source.pdbx_wavelength 0.92 _diffrn_source.pdbx_wavelength_list ? # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 5AJM _reflns.observed_criterion_sigma_I 2.7 _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 50.79 _reflns.d_resolution_high 2.45 _reflns.number_obs 33498 _reflns.number_all ? _reflns.percent_possible_obs 99.2 _reflns.pdbx_Rmerge_I_obs 0.08 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 13.10 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 7.8 # _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_ordinal 1 _reflns_shell.d_res_high 2.45 _reflns_shell.d_res_low 2.58 _reflns_shell.percent_possible_all 98.1 _reflns_shell.Rmerge_I_obs 0.68 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs 2.70 _reflns_shell.pdbx_redundancy 7.6 # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 5AJM _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 31800 _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 150.99 _refine.ls_d_res_high 2.45 _refine.ls_percent_reflns_obs 99.12 _refine.ls_R_factor_obs 0.20171 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.20038 _refine.ls_R_factor_R_free 0.22665 _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 1697 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.955 _refine.correlation_coeff_Fo_to_Fc_free 0.947 _refine.B_iso_mean 78.353 _refine.aniso_B[1][1] 1.90 _refine.aniso_B[2][2] 1.90 _refine.aniso_B[3][3] -6.17 _refine.aniso_B[1][2] 0.95 _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. U VALUES 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 0.268 _refine.pdbx_overall_ESU_R_Free 0.207 _refine.overall_SU_ML 0.184 _refine.pdbx_overall_phase_error ? _refine.overall_SU_B 16.592 _refine.overall_SU_R_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 3860 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 215 _refine_hist.number_atoms_solvent 163 _refine_hist.number_atoms_total 4238 _refine_hist.d_res_high 2.45 _refine_hist.d_res_low 150.99 # 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 ? 4188 'X-RAY DIFFRACTION' ? r_bond_other_d 0.001 0.020 ? 3821 'X-RAY DIFFRACTION' ? r_angle_refined_deg 1.052 1.999 ? 5697 'X-RAY DIFFRACTION' ? r_angle_other_deg 0.672 3.003 ? 8782 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 5.559 5.000 ? 483 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg 36.266 25.150 ? 200 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg 14.726 15.000 ? 681 'X-RAY DIFFRACTION' ? r_dihedral_angle_4_deg 14.659 15.000 ? 17 'X-RAY DIFFRACTION' ? r_chiral_restr 0.057 0.200 ? 643 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.003 0.020 ? 4625 'X-RAY DIFFRACTION' ? r_gen_planes_other 0.001 0.020 ? 944 'X-RAY DIFFRACTION' ? r_nbd_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbd_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbtor_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbtor_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_metal_ion_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_metal_ion_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_vdw_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_vdw_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_hbond_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_hbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_metal_ion_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_metal_ion_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcbond_it 1.368 4.390 ? 1932 'X-RAY DIFFRACTION' ? r_mcbond_other 1.367 4.390 ? 1931 'X-RAY DIFFRACTION' ? r_mcangle_it 2.264 6.583 ? 2412 'X-RAY DIFFRACTION' ? r_mcangle_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scbond_it 2.456 5.365 ? 2256 'X-RAY DIFFRACTION' ? r_scbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scangle_it ? ? ? ? 'X-RAY DIFFRACTION' ? r_scangle_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_long_range_B_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_long_range_B_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_rigid_bond_restr ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_free ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_bonded ? ? ? ? 'X-RAY DIFFRACTION' ? # _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_ls_shell.pdbx_total_number_of_bins_used 20 _refine_ls_shell.d_res_high 2.450 _refine_ls_shell.d_res_low 2.514 _refine_ls_shell.number_reflns_R_work 2270 _refine_ls_shell.R_factor_R_work 0.329 _refine_ls_shell.percent_reflns_obs 96.31 _refine_ls_shell.R_factor_R_free 0.372 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 104 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? # _struct.entry_id 5AJM _struct.title ;H5 (VN1194) Asn186Lys Mutant Haemagglutinin in Complex with Avian Receptor Analogue 3'SLN ; _struct.pdbx_descriptor 'HAEMAGGLUTININ HA1, HAEMAGGLUTININ HA2' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 5AJM _struct_keywords.pdbx_keywords 'VIRAL PROTEIN' _struct_keywords.text ;VIRAL PROTEIN, HAEMAGGLUTININ, HAEMAGGLUTININ MUTANT, H5N1, INFLUENZA, SIALIC ACID, GLYCOPROTEIN, VIRUS RECEPTOR, AVIAN FLU, SIALYLLACTOSAMINE, 3SLN, 3'SLN, 6SLN, 6'SLN, LSTA ; # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 3 ? D N N 3 ? E N N 3 ? F N N 3 ? G N N 3 ? H N N 4 ? I N N 5 ? J N N 5 ? K N N 3 ? L N N 6 ? M N N 7 ? N N N 3 ? O N N 3 ? P N N 3 ? Q N N 4 ? R N N 8 ? S N N 9 ? T 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 CYS A 67 ? ILE A 71 ? CYS A 67 ILE A 71 5 ? 5 HELX_P HELX_P3 3 ASP A 97 ? SER A 106 ? ASP A 97 SER A 106 1 ? 10 HELX_P HELX_P4 4 PRO A 118 ? TRP A 122 ? PRO A 118 TRP A 122 5 ? 5 HELX_P HELX_P5 5 ASP A 183 ? GLN A 192 ? ASP A 183 GLN A 192 1 ? 10 HELX_P HELX_P6 6 ASP B 37 ? MET B 59 ? ASP B 37 MET B 59 1 ? 23 HELX_P HELX_P7 7 GLU B 74 ? ARG B 127 ? GLU B 74 ARG B 127 1 ? 54 HELX_P HELX_P8 8 ASP B 145 ? GLY B 155 ? ASP B 145 GLY B 155 1 ? 11 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 ? ? ? ? ? ? ? 2.092 ? disulf2 disulf ? ? A CYS 42 SG ? ? ? 1_555 A CYS 274 SG ? ? A CYS 42 A CYS 274 1_555 ? ? ? ? ? ? ? 2.040 ? disulf3 disulf ? ? A CYS 55 SG ? ? ? 1_555 A CYS 67 SG ? ? A CYS 55 A CYS 67 1_555 ? ? ? ? ? ? ? 2.049 ? disulf4 disulf ? ? A CYS 90 SG ? ? ? 1_555 A CYS 135 SG ? ? A CYS 90 A CYS 135 1_555 ? ? ? ? ? ? ? 2.057 ? disulf5 disulf ? ? A CYS 278 SG ? ? ? 1_555 A CYS 302 SG ? ? A CYS 278 A CYS 302 1_555 ? ? ? ? ? ? ? 2.058 ? disulf6 disulf ? ? B CYS 144 SG ? ? ? 1_555 B CYS 148 SG ? ? B CYS 144 B CYS 148 1_555 ? ? ? ? ? ? ? 2.050 ? covale1 covale ? ? A ASN 11 ND2 ? ? ? 1_555 C NAG . C1 ? ? A ASN 11 A NAG 1322 1_555 ? ? ? ? ? ? ? 1.460 ? covale2 covale ? ? A ASN 23 ND2 ? ? ? 1_555 D NAG . C1 ? ? A ASN 23 A NAG 1323 1_555 ? ? ? ? ? ? ? 1.441 ? covale3 covale ? ? A ASN 165 ND2 ? ? ? 1_555 F NAG . C1 ? ? A ASN 165 A NAG 1325 1_555 ? ? ? ? ? ? ? 1.440 ? covale4 covale ? ? A ASN 286 ND2 ? ? ? 1_555 K NAG . C1 ? ? A ASN 286 A NAG 1330 1_555 ? ? ? ? ? ? ? 1.445 ? covale5 covale ? ? D NAG . O4 ? ? ? 1_555 E NAG . C1 ? ? A NAG 1323 A NAG 1324 1_555 ? ? ? ? ? ? ? 1.445 ? covale6 covale ? ? F NAG . O4 ? ? ? 1_555 G NAG . C1 ? ? A NAG 1325 A NAG 1326 1_555 ? ? ? ? ? ? ? 1.445 ? covale7 covale ? ? G NAG . O4 ? ? ? 1_555 H BMA . C1 ? ? A NAG 1326 A BMA 1327 1_555 ? ? ? ? ? ? ? 1.458 ? covale8 covale ? ? H BMA . O3 ? ? ? 1_555 I MAN . C1 ? ? A BMA 1327 A MAN 1328 1_555 ? ? ? ? ? ? ? 1.444 ? covale9 covale ? ? H BMA . O6 ? ? ? 1_555 J MAN . C1 ? ? A BMA 1327 A MAN 1329 1_555 ? ? ? ? ? ? ? 1.450 ? covale10 covale ? ? L SIA . C2 ? ? ? 1_555 M GAL . O3 ? ? A SIA 1331 A GAL 1332 1_555 ? ? ? ? ? ? ? 1.433 ? covale11 covale ? ? M GAL . C1 ? ? ? 1_555 N NAG . O4 ? ? A GAL 1332 A NAG 1333 1_555 ? ? ? ? ? ? ? 1.432 ? covale12 covale ? ? B ASN 154 ND2 ? ? ? 1_555 O NAG . C1 ? ? B ASN 154 B NAG 1163 1_555 ? ? ? ? ? ? ? 1.443 ? covale13 covale ? ? O NAG . O4 ? ? ? 1_555 P NAG . C1 ? ? B NAG 1163 B NAG 1164 1_555 ? ? ? ? ? ? ? 1.446 ? covale14 covale ? ? P NAG . O4 ? ? ? 1_555 Q BMA . C1 ? ? B NAG 1164 B BMA 1165 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 SER B 32 ? ALA B 36 ? SER B 32 ALA B 36 BA 2 TYR B 22 ? SER B 27 ? TYR B 22 SER B 27 BA 3 GLN A 2 ? TYR A 7 ? GLN A 2 TYR A 7 BA 4 CYS B 137 ? PHE B 140 ? CYS B 137 PHE B 140 BA 5 ALA B 130 ? GLU B 132 ? ALA B 130 GLU B 132 AA 1 GLN A 15 ? VAL A 16 ? GLN A 15 VAL A 16 AA 2 VAL A 24 ? THR A 25 ? VAL A 24 THR A 25 AB 1 ALA A 29 ? ASP A 31 ? ALA A 29 ASP A 31 AB 2 VAL A 312 ? ALA A 314 ? VAL A 312 ALA A 314 AC 1 LEU A 33 ? GLU A 34 ? LEU A 33 GLU A 34 AC 2 PHE A 291 ? HIS A 292 ? PHE A 291 HIS A 292 AC 3 LYS A 304 ? TYR A 305 ? LYS A 304 TYR A 305 AD 1 LEU A 41 ? LEU A 44 ? LEU A 41 LEU A 44 AD 2 TYR A 271 ? THR A 276 ? TYR A 271 THR A 276 AE 1 LEU A 50 ? ILE A 51 ? LEU A 50 ILE A 51 AE 2 ILE A 79 ? GLU A 81 ? ILE A 79 GLU A 81 AE 3 ILE A 264 ? LYS A 266 ? ILE A 264 LYS A 266 AF 1 GLY A 93 ? PHE A 95 ? GLY A 93 PHE A 95 AF 2 ARG A 225 ? LEU A 233 ? ARG A 225 LEU A 233 AF 3 LEU A 172 ? HIS A 180 ? LEU A 172 HIS A 180 AF 4 PHE A 247 ? PRO A 250 ? PHE A 247 PRO A 250 AF 5 VAL A 147 ? TRP A 149 ? VAL A 147 TRP A 149 AG 1 GLY A 93 ? PHE A 95 ? GLY A 93 PHE A 95 AG 2 ARG A 225 ? LEU A 233 ? ARG A 225 LEU A 233 AG 3 LEU A 172 ? HIS A 180 ? LEU A 172 HIS A 180 AG 4 TYR A 252 ? LYS A 259 ? TYR A 252 LYS A 259 AG 5 ILE A 108 ? GLN A 115 ? ILE A 108 GLN A 115 AH 1 SER A 132 ? TYR A 137 ? SER A 132 TYR A 137 AH 2 LYS A 140 ? SER A 142 ? LYS A 140 SER A 142 AI 1 ILE A 160 ? ASN A 165 ? ILE A 160 ASN A 165 AI 2 ALA A 238 ? SER A 243 ? ALA A 238 SER A 243 AI 3 ILE A 198 ? GLY A 201 ? ILE A 198 GLY A 201 AI 4 ASN A 206 ? LEU A 209 ? ASN A 206 LEU A 209 AJ 1 GLY A 283 ? ALA A 284 ? GLY A 283 ALA A 284 AJ 2 CYS A 278 ? THR A 280 ? CYS A 278 THR A 280 AJ 3 ILE A 299 ? GLY A 300 ? ILE A 299 GLY A 300 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id BA 1 2 N ALA B 35 ? N ALA B 35 O TYR B 24 ? O TYR B 24 BA 2 3 N SER B 27 ? N SER B 27 O GLN A 2 ? O GLN A 2 BA 3 4 N ILE A 3 ? N ILE A 3 O PHE B 138 ? O PHE B 138 BA 4 5 N GLU B 139 ? N GLU B 139 O LYS B 131 ? O LYS B 131 AA 1 2 N VAL A 16 ? N VAL A 16 O VAL A 24 ? O VAL A 24 AB 1 2 N GLN A 30 ? N GLN A 30 O LEU A 313 ? O LEU A 313 AC 1 2 N GLU A 34 ? N GLU A 34 O PHE A 291 ? O PHE A 291 AC 2 3 N HIS A 292 ? N HIS A 292 O LYS A 304 ? O LYS A 304 AD 1 2 O LEU A 41 ? O LEU A 41 N GLY A 272 ? N GLY A 272 AE 1 2 O LEU A 50 ? O LEU A 50 N VAL A 80 ? N VAL A 80 AE 2 3 N GLU A 81 ? N GLU A 81 O MET A 265 ? O MET A 265 AF 1 2 N ASP A 94 ? N ASP A 94 O MET A 226 ? O MET A 226 AF 2 3 N LEU A 233 ? N LEU A 233 O LEU A 172 ? O LEU A 172 AF 3 4 N GLY A 177 ? N GLY A 177 O ILE A 248 ? O ILE A 248 AF 4 5 N ALA A 249 ? N ALA A 249 O VAL A 148 ? O VAL A 148 AG 1 2 N ASP A 94 ? N ASP A 94 O MET A 226 ? O MET A 226 AG 2 3 N LEU A 233 ? N LEU A 233 O LEU A 172 ? O LEU A 172 AG 3 4 N LEU A 173 ? N LEU A 173 O TYR A 254 ? O TYR A 254 AG 4 5 O LYS A 258 ? O LYS A 258 N ASN A 109 ? N ASN A 109 AH 1 2 N TYR A 137 ? N TYR A 137 O LYS A 140 ? O LYS A 140 AI 1 2 N TYR A 164 ? N TYR A 164 O ILE A 239 ? O ILE A 239 AI 2 3 N GLU A 242 ? N GLU A 242 O SER A 199 ? O SER A 199 AI 3 4 N VAL A 200 ? N VAL A 200 O GLN A 207 ? O GLN A 207 AJ 1 2 N GLY A 283 ? N GLY A 283 O THR A 280 ? O THR A 280 AJ 2 3 N GLN A 279 ? N GLN A 279 O ILE A 299 ? O ILE A 299 # loop_ _struct_site.id _struct_site.pdbx_evidence_code _struct_site.pdbx_auth_asym_id _struct_site.pdbx_auth_comp_id _struct_site.pdbx_auth_seq_id _struct_site.pdbx_auth_ins_code _struct_site.pdbx_num_residues _struct_site.details AC1 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE MPO B 1166' AC2 Software ? ? ? ? 1 'Binding site for Mono-Saccharide NAG A1322 bound to ASN A 11' AC3 Software ? ? ? ? 2 'Binding site for Poly-Saccharide residues NAG A1323 through NAG A1324 bound to ASN A 23' AC4 Software ? ? ? ? 6 'Binding site for Poly-Saccharide residues NAG A1325 through MAN A1329 bound to ASN A 165' AC5 Software ? ? ? ? 1 'Binding site for Mono-Saccharide NAG A1330 bound to ASN A 286' AC6 Software ? ? ? ? 3 'Binding site for Poly-Saccharide residues NAG B1163 through BMA B1165 bound to ASN B 154' AC7 Software ? ? ? ? 12 'Binding site for Poly-Saccharide residues SIA A1331 through NAG A1333' # loop_ _struct_site_gen.id _struct_site_gen.site_id _struct_site_gen.pdbx_num_res _struct_site_gen.label_comp_id _struct_site_gen.label_asym_id _struct_site_gen.label_seq_id _struct_site_gen.pdbx_auth_ins_code _struct_site_gen.auth_comp_id _struct_site_gen.auth_asym_id _struct_site_gen.auth_seq_id _struct_site_gen.label_atom_id _struct_site_gen.label_alt_id _struct_site_gen.symmetry _struct_site_gen.details 1 AC1 4 TRP B 14 ? TRP B 14 . ? 1_555 ? 2 AC1 4 HIS B 25 ? HIS B 25 . ? 1_555 ? 3 AC1 4 TYR B 34 ? TYR B 34 . ? 1_555 ? 4 AC1 4 ASN B 135 ? ASN B 135 . ? 1_555 ? 5 AC2 1 ASN A 11 ? ASN A 11 . ? 1_555 ? 6 AC3 2 LYS A 22 ? LYS A 22 . ? 1_555 ? 7 AC3 2 ASN A 23 ? ASN A 23 . ? 1_555 ? 8 AC4 6 ARG A 107 ? ARG A 107 . ? 6_555 ? 9 AC4 6 ASN A 165 ? ASN A 165 . ? 1_555 ? 10 AC4 6 SER A 217 ? SER A 217 . ? 2_545 ? 11 AC4 6 ASN A 236 ? ASN A 236 . ? 1_555 ? 12 AC4 6 HIS A 295 ? HIS A 295 . ? 4_545 ? 13 AC4 6 ARG B 75 ? ARG B 75 . ? 4_545 ? 14 AC5 1 ASN A 286 ? ASN A 286 . ? 1_555 ? 15 AC6 3 GLU B 147 ? GLU B 147 . ? 1_555 ? 16 AC6 3 GLU B 150 ? GLU B 150 . ? 1_555 ? 17 AC6 3 ASN B 154 ? ASN B 154 . ? 1_555 ? 18 AC7 12 TYR A 91 ? TYR A 91 . ? 1_555 ? 19 AC7 12 LEU A 129 ? LEU A 129 . ? 1_555 ? 20 AC7 12 VAL A 131 ? VAL A 131 . ? 1_555 ? 21 AC7 12 SER A 132 ? SER A 132 . ? 1_555 ? 22 AC7 12 SER A 133 ? SER A 133 . ? 1_555 ? 23 AC7 12 HIS A 179 ? HIS A 179 . ? 1_555 ? 24 AC7 12 GLU A 186 ? GLU A 186 . ? 1_555 ? 25 AC7 12 LEU A 190 ? LEU A 190 . ? 1_555 ? 26 AC7 12 LYS A 218 ? LYS A 218 . ? 1_555 ? 27 AC7 12 GLY A 221 ? GLY A 221 . ? 1_555 ? 28 AC7 12 GLN A 222 ? GLN A 222 . ? 1_555 ? 29 AC7 12 HOH S . ? HOH A 2050 . ? 1_555 ? # _database_PDB_matrix.entry_id 5AJM _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 5AJM _atom_sites.fract_transf_matrix[1][1] 0.009844 _atom_sites.fract_transf_matrix[1][2] 0.005684 _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] 0.011367 _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] 0.002208 _atom_sites.fract_transf_vector[1] 0.00000 _atom_sites.fract_transf_vector[2] 0.00000 _atom_sites.fract_transf_vector[3] 0.00000 # loop_ _atom_type.symbol C N O S # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 N N . ASP A 1 1 ? 36.927 -15.870 -83.838 1.00 65.36 ? 1 ASP A N 1 ATOM 2 C CA . ASP A 1 1 ? 36.102 -16.349 -82.692 1.00 64.43 ? 1 ASP A CA 1 ATOM 3 C C . ASP A 1 1 ? 36.978 -17.047 -81.680 1.00 62.25 ? 1 ASP A C 1 ATOM 4 O O . ASP A 1 1 ? 37.885 -17.788 -82.052 1.00 60.89 ? 1 ASP A O 1 ATOM 5 C CB . ASP A 1 1 ? 35.023 -17.316 -83.175 1.00 65.67 ? 1 ASP A CB 1 ATOM 6 C CG . ASP A 1 1 ? 34.105 -16.695 -84.204 1.00 68.23 ? 1 ASP A CG 1 ATOM 7 O OD1 . ASP A 1 1 ? 34.288 -15.500 -84.519 1.00 68.21 ? 1 ASP A OD1 1 ATOM 8 O OD2 . ASP A 1 1 ? 33.202 -17.403 -84.696 1.00 72.10 ? 1 ASP A OD2 1 ATOM 9 N N . GLN A 1 2 ? 36.710 -16.807 -80.399 1.00 62.76 ? 2 GLN A N 1 ATOM 10 C CA . GLN A 1 2 ? 37.493 -17.423 -79.337 1.00 60.66 ? 2 GLN A CA 1 ATOM 11 C C . GLN A 1 2 ? 36.684 -17.749 -78.099 1.00 59.71 ? 2 GLN A C 1 ATOM 12 O O . GLN A 1 2 ? 35.631 -17.149 -77.841 1.00 59.48 ? 2 GLN A O 1 ATOM 13 C CB . GLN A 1 2 ? 38.686 -16.539 -78.945 1.00 61.39 ? 2 GLN A CB 1 ATOM 14 C CG . GLN A 1 2 ? 38.342 -15.123 -78.534 1.00 64.26 ? 2 GLN A CG 1 ATOM 15 C CD . GLN A 1 2 ? 39.460 -14.448 -77.756 1.00 65.16 ? 2 GLN A CD 1 ATOM 16 O OE1 . GLN A 1 2 ? 39.219 -13.827 -76.722 1.00 67.93 ? 2 GLN A OE1 1 ATOM 17 N NE2 . GLN A 1 2 ? 40.684 -14.563 -78.249 1.00 64.67 ? 2 GLN A NE2 1 ATOM 18 N N . ILE A 1 3 ? 37.202 -18.717 -77.345 1.00 57.37 ? 3 ILE A N 1 ATOM 19 C CA . ILE A 1 3 ? 36.692 -19.057 -76.030 1.00 57.14 ? 3 ILE A CA 1 ATOM 20 C C . ILE A 1 3 ? 37.861 -19.003 -75.048 1.00 56.39 ? 3 ILE A C 1 ATOM 21 O O . ILE A 1 3 ? 38.973 -19.430 -75.368 1.00 54.65 ? 3 ILE A O 1 ATOM 22 C CB . ILE A 1 3 ? 35.983 -20.431 -76.029 1.00 57.74 ? 3 ILE A CB 1 ATOM 23 C CG1 . ILE A 1 3 ? 35.226 -20.649 -74.719 1.00 58.34 ? 3 ILE A CG1 1 ATOM 24 C CG2 . ILE A 1 3 ? 36.956 -21.575 -76.261 1.00 56.25 ? 3 ILE A CG2 1 ATOM 25 C CD1 . ILE A 1 3 ? 34.176 -21.736 -74.821 1.00 59.39 ? 3 ILE A CD1 1 ATOM 26 N N . CYS A 1 4 ? 37.615 -18.439 -73.869 1.00 57.42 ? 4 CYS A N 1 ATOM 27 C CA . CYS A 1 4 ? 38.663 -18.198 -72.888 1.00 55.78 ? 4 CYS A CA 1 ATOM 28 C C . CYS A 1 4 ? 38.281 -18.867 -71.588 1.00 54.07 ? 4 CYS A C 1 ATOM 29 O O . CYS A 1 4 ? 37.101 -18.975 -71.269 1.00 54.58 ? 4 CYS A O 1 ATOM 30 C CB . CYS A 1 4 ? 38.842 -16.692 -72.647 1.00 58.57 ? 4 CYS A CB 1 ATOM 31 S SG . CYS A 1 4 ? 39.286 -15.714 -74.107 1.00 64.56 ? 4 CYS A SG 1 ATOM 32 N N . ILE A 1 5 ? 39.277 -19.311 -70.832 1.00 50.50 ? 5 ILE A N 1 ATOM 33 C CA . ILE A 1 5 ? 39.036 -19.814 -69.494 1.00 48.98 ? 5 ILE A CA 1 ATOM 34 C C . ILE A 1 5 ? 39.512 -18.763 -68.520 1.00 48.34 ? 5 ILE A C 1 ATOM 35 O O . ILE A 1 5 ? 40.524 -18.117 -68.758 1.00 47.18 ? 5 ILE A O 1 ATOM 36 C CB . ILE A 1 5 ? 39.772 -21.133 -69.245 1.00 48.39 ? 5 ILE A CB 1 ATOM 37 C CG1 . ILE A 1 5 ? 39.338 -22.172 -70.275 1.00 50.90 ? 5 ILE A CG1 1 ATOM 38 C CG2 . ILE A 1 5 ? 39.521 -21.635 -67.834 1.00 48.34 ? 5 ILE A CG2 1 ATOM 39 C CD1 . ILE A 1 5 ? 37.917 -22.640 -70.103 1.00 53.53 ? 5 ILE A CD1 1 ATOM 40 N N . GLY A 1 6 ? 38.771 -18.585 -67.429 1.00 48.39 ? 6 GLY A N 1 ATOM 41 C CA . GLY A 1 6 ? 39.079 -17.540 -66.464 1.00 47.72 ? 6 GLY A CA 1 ATOM 42 C C . GLY A 1 6 ? 38.414 -17.773 -65.131 1.00 47.32 ? 6 GLY A C 1 ATOM 43 O O . GLY A 1 6 ? 37.771 -18.801 -64.911 1.00 48.02 ? 6 GLY A O 1 ATOM 44 N N . TYR A 1 7 ? 38.561 -16.800 -64.245 1.00 46.57 ? 7 TYR A N 1 ATOM 45 C CA . TYR A 1 7 ? 38.120 -16.953 -62.880 1.00 46.68 ? 7 TYR A CA 1 ATOM 46 C C . TYR A 1 7 ? 37.573 -15.646 -62.317 1.00 48.75 ? 7 TYR A C 1 ATOM 47 O O . TYR A 1 7 ? 37.818 -14.569 -62.847 1.00 49.33 ? 7 TYR A O 1 ATOM 48 C CB . TYR A 1 7 ? 39.274 -17.486 -62.018 1.00 45.34 ? 7 TYR A CB 1 ATOM 49 C CG . TYR A 1 7 ? 40.537 -16.653 -62.077 1.00 44.90 ? 7 TYR A CG 1 ATOM 50 C CD1 . TYR A 1 7 ? 41.480 -16.852 -63.067 1.00 44.79 ? 7 TYR A CD1 1 ATOM 51 C CD2 . TYR A 1 7 ? 40.786 -15.670 -61.134 1.00 46.55 ? 7 TYR A CD2 1 ATOM 52 C CE1 . TYR A 1 7 ? 42.631 -16.083 -63.122 1.00 45.91 ? 7 TYR A CE1 1 ATOM 53 C CE2 . TYR A 1 7 ? 41.937 -14.901 -61.181 1.00 46.47 ? 7 TYR A CE2 1 ATOM 54 C CZ . TYR A 1 7 ? 42.853 -15.109 -62.171 1.00 46.24 ? 7 TYR A CZ 1 ATOM 55 O OH . TYR A 1 7 ? 43.988 -14.328 -62.220 1.00 48.46 ? 7 TYR A OH 1 ATOM 56 N N . HIS A 1 8 ? 36.830 -15.781 -61.229 1.00 49.59 ? 8 HIS A N 1 ATOM 57 C CA . HIS A 1 8 ? 36.084 -14.699 -60.602 1.00 52.55 ? 8 HIS A CA 1 ATOM 58 C C . HIS A 1 8 ? 36.986 -13.616 -60.018 1.00 53.35 ? 8 HIS A C 1 ATOM 59 O O . HIS A 1 8 ? 38.058 -13.898 -59.491 1.00 53.73 ? 8 HIS A O 1 ATOM 60 C CB . HIS A 1 8 ? 35.239 -15.316 -59.481 1.00 53.39 ? 8 HIS A CB 1 ATOM 61 C CG . HIS A 1 8 ? 34.360 -14.351 -58.758 1.00 55.27 ? 8 HIS A CG 1 ATOM 62 N ND1 . HIS A 1 8 ? 33.300 -13.711 -59.363 1.00 57.75 ? 8 HIS A ND1 1 ATOM 63 C CD2 . HIS A 1 8 ? 34.348 -13.957 -57.462 1.00 54.98 ? 8 HIS A CD2 1 ATOM 64 C CE1 . HIS A 1 8 ? 32.691 -12.942 -58.478 1.00 58.43 ? 8 HIS A CE1 1 ATOM 65 N NE2 . HIS A 1 8 ? 33.306 -13.075 -57.316 1.00 56.86 ? 8 HIS A NE2 1 ATOM 66 N N . ALA A 1 9 ? 36.538 -12.372 -60.113 1.00 55.30 ? 9 ALA A N 1 ATOM 67 C CA . ALA A 1 9 ? 37.126 -11.271 -59.356 1.00 55.71 ? 9 ALA A CA 1 ATOM 68 C C . ALA A 1 9 ? 35.988 -10.431 -58.808 1.00 57.77 ? 9 ALA A C 1 ATOM 69 O O . ALA A 1 9 ? 34.856 -10.558 -59.255 1.00 62.41 ? 9 ALA A O 1 ATOM 70 C CB . ALA A 1 9 ? 38.039 -10.439 -60.232 1.00 55.24 ? 9 ALA A CB 1 ATOM 71 N N . ASN A 1 10 ? 36.276 -9.595 -57.824 1.00 58.21 ? 10 ASN A N 1 ATOM 72 C CA . ASN A 1 10 ? 35.262 -8.715 -57.260 1.00 61.45 ? 10 ASN A CA 1 ATOM 73 C C . ASN A 1 10 ? 35.918 -7.528 -56.559 1.00 65.45 ? 10 ASN A C 1 ATOM 74 O O . ASN A 1 10 ? 37.118 -7.310 -56.716 1.00 63.54 ? 10 ASN A O 1 ATOM 75 C CB . ASN A 1 10 ? 34.323 -9.495 -56.326 1.00 60.27 ? 10 ASN A CB 1 ATOM 76 C CG . ASN A 1 10 ? 35.004 -9.966 -55.049 1.00 59.08 ? 10 ASN A CG 1 ATOM 77 O OD1 . ASN A 1 10 ? 36.158 -9.639 -54.772 1.00 57.76 ? 10 ASN A OD1 1 ATOM 78 N ND2 . ASN A 1 10 ? 34.279 -10.746 -54.262 1.00 58.60 ? 10 ASN A ND2 1 ATOM 79 N N . ASN A 1 11 ? 35.138 -6.763 -55.799 1.00 72.78 ? 11 ASN A N 1 ATOM 80 C CA . ASN A 1 11 ? 35.649 -5.554 -55.153 1.00 79.77 ? 11 ASN A CA 1 ATOM 81 C C . ASN A 1 11 ? 36.147 -5.781 -53.720 1.00 75.68 ? 11 ASN A C 1 ATOM 82 O O . ASN A 1 11 ? 36.319 -4.828 -52.959 1.00 76.11 ? 11 ASN A O 1 ATOM 83 C CB . ASN A 1 11 ? 34.598 -4.425 -55.210 1.00 90.70 ? 11 ASN A CB 1 ATOM 84 C CG . ASN A 1 11 ? 33.286 -4.781 -54.518 1.00 103.06 ? 11 ASN A CG 1 ATOM 85 O OD1 . ASN A 1 11 ? 33.168 -5.812 -53.852 1.00 101.93 ? 11 ASN A OD1 1 ATOM 86 N ND2 . ASN A 1 11 ? 32.278 -3.901 -54.687 1.00 121.48 ? 11 ASN A ND2 1 ATOM 87 N N . SER A 1 12 ? 36.401 -7.040 -53.367 1.00 70.72 ? 12 SER A N 1 ATOM 88 C CA . SER A 1 12 ? 36.794 -7.398 -52.009 1.00 66.56 ? 12 SER A CA 1 ATOM 89 C C . SER A 1 12 ? 38.167 -6.849 -51.667 1.00 64.98 ? 12 SER A C 1 ATOM 90 O O . SER A 1 12 ? 39.066 -6.840 -52.510 1.00 62.04 ? 12 SER A O 1 ATOM 91 C CB . SER A 1 12 ? 36.811 -8.917 -51.825 1.00 64.02 ? 12 SER A CB 1 ATOM 92 O OG . SER A 1 12 ? 37.070 -9.264 -50.477 1.00 61.40 ? 12 SER A OG 1 ATOM 93 N N . THR A 1 13 ? 38.300 -6.384 -50.424 1.00 65.01 ? 13 THR A N 1 ATOM 94 C CA . THR A 1 13 ? 39.568 -5.948 -49.857 1.00 64.30 ? 13 THR A CA 1 ATOM 95 C C . THR A 1 13 ? 39.987 -6.845 -48.693 1.00 63.52 ? 13 THR A C 1 ATOM 96 O O . THR A 1 13 ? 41.007 -6.588 -48.065 1.00 64.24 ? 13 THR A O 1 ATOM 97 C CB . THR A 1 13 ? 39.475 -4.499 -49.348 1.00 67.70 ? 13 THR A CB 1 ATOM 98 O OG1 . THR A 1 13 ? 38.387 -4.384 -48.418 1.00 69.61 ? 13 THR A OG1 1 ATOM 99 C CG2 . THR A 1 13 ? 39.254 -3.533 -50.507 1.00 68.59 ? 13 THR A CG2 1 ATOM 100 N N . GLU A 1 14 ? 39.206 -7.891 -48.410 1.00 62.55 ? 14 GLU A N 1 ATOM 101 C CA . GLU A 1 14 ? 39.558 -8.883 -47.388 1.00 61.42 ? 14 GLU A CA 1 ATOM 102 C C . GLU A 1 14 ? 40.919 -9.502 -47.694 1.00 58.48 ? 14 GLU A C 1 ATOM 103 O O . GLU A 1 14 ? 41.212 -9.813 -48.851 1.00 59.05 ? 14 GLU A O 1 ATOM 104 C CB . GLU A 1 14 ? 38.528 -10.015 -47.343 1.00 64.39 ? 14 GLU A CB 1 ATOM 105 C CG . GLU A 1 14 ? 37.099 -9.608 -47.011 1.00 69.07 ? 14 GLU A CG 1 ATOM 106 C CD . GLU A 1 14 ? 36.925 -9.178 -45.572 1.00 73.12 ? 14 GLU A CD 1 ATOM 107 O OE1 . GLU A 1 14 ? 37.557 -9.793 -44.685 1.00 73.85 ? 14 GLU A OE1 1 ATOM 108 O OE2 . GLU A 1 14 ? 36.156 -8.218 -45.334 1.00 80.50 ? 14 GLU A OE2 1 ATOM 109 N N . GLN A 1 15 ? 41.729 -9.701 -46.654 1.00 55.70 ? 15 GLN A N 1 ATOM 110 C CA . GLN A 1 15 ? 43.087 -10.222 -46.794 1.00 52.90 ? 15 GLN A CA 1 ATOM 111 C C . GLN A 1 15 ? 43.306 -11.406 -45.871 1.00 51.35 ? 15 GLN A C 1 ATOM 112 O O . GLN A 1 15 ? 42.747 -11.458 -44.784 1.00 51.17 ? 15 GLN A O 1 ATOM 113 C CB . GLN A 1 15 ? 44.109 -9.149 -46.434 1.00 54.92 ? 15 GLN A CB 1 ATOM 114 C CG . GLN A 1 15 ? 43.963 -7.846 -47.193 1.00 59.16 ? 15 GLN A CG 1 ATOM 115 C CD . GLN A 1 15 ? 45.096 -6.878 -46.917 1.00 62.36 ? 15 GLN A CD 1 ATOM 116 O OE1 . GLN A 1 15 ? 45.552 -6.172 -47.813 1.00 67.64 ? 15 GLN A OE1 1 ATOM 117 N NE2 . GLN A 1 15 ? 45.559 -6.844 -45.678 1.00 63.63 ? 15 GLN A NE2 1 ATOM 118 N N . VAL A 1 16 ? 44.139 -12.348 -46.300 1.00 49.37 ? 16 VAL A N 1 ATOM 119 C CA . VAL A 1 16 ? 44.512 -13.484 -45.465 1.00 46.52 ? 16 VAL A CA 1 ATOM 120 C C . VAL A 1 16 ? 46.013 -13.648 -45.498 1.00 46.26 ? 16 VAL A C 1 ATOM 121 O O . VAL A 1 16 ? 46.665 -13.154 -46.412 1.00 45.19 ? 16 VAL A O 1 ATOM 122 C CB . VAL A 1 16 ? 43.855 -14.789 -45.946 1.00 45.72 ? 16 VAL A CB 1 ATOM 123 C CG1 . VAL A 1 16 ? 42.347 -14.622 -45.991 1.00 47.24 ? 16 VAL A CG1 1 ATOM 124 C CG2 . VAL A 1 16 ? 44.391 -15.216 -47.310 1.00 45.37 ? 16 VAL A CG2 1 ATOM 125 N N . ASP A 1 17 ? 46.552 -14.344 -44.500 1.00 47.48 ? 17 ASP A N 1 ATOM 126 C CA . ASP A 1 17 ? 47.978 -14.656 -44.452 1.00 47.38 ? 17 ASP A CA 1 ATOM 127 C C . ASP A 1 17 ? 48.218 -16.114 -44.817 1.00 46.22 ? 17 ASP A C 1 ATOM 128 O O . ASP A 1 17 ? 47.389 -16.979 -44.542 1.00 42.93 ? 17 ASP A O 1 ATOM 129 C CB . ASP A 1 17 ? 48.546 -14.388 -43.062 1.00 48.46 ? 17 ASP A CB 1 ATOM 130 C CG . ASP A 1 17 ? 48.660 -12.902 -42.742 1.00 52.54 ? 17 ASP A CG 1 ATOM 131 O OD1 . ASP A 1 17 ? 48.711 -12.072 -43.675 1.00 55.51 ? 17 ASP A OD1 1 ATOM 132 O OD2 . ASP A 1 17 ? 48.715 -12.561 -41.537 1.00 55.74 ? 17 ASP A OD2 1 ATOM 133 N N . THR A 1 18 ? 49.358 -16.358 -45.455 1.00 47.82 ? 18 THR A N 1 ATOM 134 C CA . THR A 1 18 ? 49.867 -17.701 -45.721 1.00 47.40 ? 18 THR A CA 1 ATOM 135 C C . THR A 1 18 ? 51.307 -17.761 -45.216 1.00 49.80 ? 18 THR A C 1 ATOM 136 O O . THR A 1 18 ? 51.840 -16.763 -44.736 1.00 51.09 ? 18 THR A O 1 ATOM 137 C CB . THR A 1 18 ? 49.849 -18.004 -47.227 1.00 46.24 ? 18 THR A CB 1 ATOM 138 O OG1 . THR A 1 18 ? 50.795 -17.162 -47.894 1.00 48.16 ? 18 THR A OG1 1 ATOM 139 C CG2 . THR A 1 18 ? 48.478 -17.746 -47.803 1.00 45.81 ? 18 THR A CG2 1 ATOM 140 N N . ILE A 1 19 ? 51.945 -18.917 -45.341 1.00 52.31 ? 19 ILE A N 1 ATOM 141 C CA . ILE A 1 19 ? 53.326 -19.083 -44.879 1.00 53.56 ? 19 ILE A CA 1 ATOM 142 C C . ILE A 1 19 ? 54.299 -18.208 -45.681 1.00 54.51 ? 19 ILE A C 1 ATOM 143 O O . ILE A 1 19 ? 55.202 -17.587 -45.115 1.00 55.03 ? 19 ILE A O 1 ATOM 144 C CB . ILE A 1 19 ? 53.770 -20.556 -45.006 1.00 58.48 ? 19 ILE A CB 1 ATOM 145 C CG1 . ILE A 1 19 ? 52.925 -21.472 -44.110 1.00 60.33 ? 19 ILE A CG1 1 ATOM 146 C CG2 . ILE A 1 19 ? 55.240 -20.717 -44.655 1.00 61.47 ? 19 ILE A CG2 1 ATOM 147 C CD1 . ILE A 1 19 ? 53.273 -21.411 -42.640 1.00 59.29 ? 19 ILE A CD1 1 ATOM 148 N N . MET A 1 20 ? 54.114 -18.171 -46.998 1.00 54.30 ? 20 MET A N 1 ATOM 149 C CA . MET A 1 20 ? 55.039 -17.482 -47.900 1.00 54.39 ? 20 MET A CA 1 ATOM 150 C C . MET A 1 20 ? 54.670 -16.037 -48.191 1.00 54.00 ? 20 MET A C 1 ATOM 151 O O . MET A 1 20 ? 55.490 -15.282 -48.715 1.00 54.50 ? 20 MET A O 1 ATOM 152 C CB . MET A 1 20 ? 55.103 -18.204 -49.237 1.00 55.71 ? 20 MET A CB 1 ATOM 153 C CG . MET A 1 20 ? 55.800 -19.541 -49.190 1.00 57.80 ? 20 MET A CG 1 ATOM 154 S SD . MET A 1 20 ? 56.161 -20.097 -50.856 1.00 61.43 ? 20 MET A SD 1 ATOM 155 C CE . MET A 1 20 ? 57.656 -21.021 -50.550 1.00 64.85 ? 20 MET A CE 1 ATOM 156 N N . GLU A 1 21 ? 53.436 -15.656 -47.897 1.00 53.17 ? 21 GLU A N 1 ATOM 157 C CA . GLU A 1 21 ? 52.970 -14.325 -48.250 1.00 54.23 ? 21 GLU A CA 1 ATOM 158 C C . GLU A 1 21 ? 51.923 -13.839 -47.264 1.00 52.26 ? 21 GLU A C 1 ATOM 159 O O . GLU A 1 21 ? 51.009 -14.574 -46.889 1.00 50.37 ? 21 GLU A O 1 ATOM 160 C CB . GLU A 1 21 ? 52.401 -14.332 -49.666 1.00 55.49 ? 21 GLU A CB 1 ATOM 161 C CG . GLU A 1 21 ? 52.311 -12.951 -50.296 1.00 60.08 ? 21 GLU A CG 1 ATOM 162 C CD . GLU A 1 21 ? 51.743 -12.967 -51.712 1.00 63.19 ? 21 GLU A CD 1 ATOM 163 O OE1 . GLU A 1 21 ? 51.574 -14.077 -52.295 1.00 59.95 ? 21 GLU A OE1 1 ATOM 164 O OE2 . GLU A 1 21 ? 51.477 -11.857 -52.243 1.00 61.50 ? 21 GLU A OE2 1 ATOM 165 N N . LYS A 1 22 ? 52.069 -12.591 -46.848 1.00 53.57 ? 22 LYS A N 1 ATOM 166 C CA . LYS A 1 22 ? 51.144 -11.988 -45.911 1.00 55.81 ? 22 LYS A CA 1 ATOM 167 C C . LYS A 1 22 ? 50.286 -10.994 -46.655 1.00 54.16 ? 22 LYS A C 1 ATOM 168 O O . LYS A 1 22 ? 50.704 -10.452 -47.676 1.00 53.07 ? 22 LYS A O 1 ATOM 169 C CB . LYS A 1 22 ? 51.917 -11.307 -44.791 1.00 60.60 ? 22 LYS A CB 1 ATOM 170 C CG . LYS A 1 22 ? 52.662 -12.279 -43.890 1.00 64.57 ? 22 LYS A CG 1 ATOM 171 C CD . LYS A 1 22 ? 53.515 -11.520 -42.887 1.00 73.75 ? 22 LYS A CD 1 ATOM 172 C CE . LYS A 1 22 ? 53.860 -12.358 -41.663 1.00 77.44 ? 22 LYS A CE 1 ATOM 173 N NZ . LYS A 1 22 ? 54.304 -11.514 -40.518 1.00 79.47 ? 22 LYS A NZ 1 ATOM 174 N N . ASN A 1 23 ? 49.076 -10.775 -46.159 1.00 54.10 ? 23 ASN A N 1 ATOM 175 C CA . ASN A 1 23 ? 48.177 -9.771 -46.725 1.00 56.91 ? 23 ASN A CA 1 ATOM 176 C C . ASN A 1 23 ? 47.827 -10.005 -48.194 1.00 54.55 ? 23 ASN A C 1 ATOM 177 O O . ASN A 1 23 ? 47.875 -9.088 -49.004 1.00 54.89 ? 23 ASN A O 1 ATOM 178 C CB . ASN A 1 23 ? 48.769 -8.365 -46.526 1.00 62.96 ? 23 ASN A CB 1 ATOM 179 C CG . ASN A 1 23 ? 48.883 -7.983 -45.065 1.00 68.62 ? 23 ASN A CG 1 ATOM 180 O OD1 . ASN A 1 23 ? 48.345 -8.668 -44.189 1.00 68.09 ? 23 ASN A OD1 1 ATOM 181 N ND2 . ASN A 1 23 ? 49.580 -6.883 -44.790 1.00 78.87 ? 23 ASN A ND2 1 ATOM 182 N N . VAL A 1 24 ? 47.465 -11.244 -48.516 1.00 53.07 ? 24 VAL A N 1 ATOM 183 C CA . VAL A 1 24 ? 46.957 -11.609 -49.835 1.00 50.59 ? 24 VAL A CA 1 ATOM 184 C C . VAL A 1 24 ? 45.482 -11.242 -49.917 1.00 50.36 ? 24 VAL A C 1 ATOM 185 O O . VAL A 1 24 ? 44.692 -11.727 -49.118 1.00 50.38 ? 24 VAL A O 1 ATOM 186 C CB . VAL A 1 24 ? 47.070 -13.129 -50.052 1.00 49.90 ? 24 VAL A CB 1 ATOM 187 C CG1 . VAL A 1 24 ? 46.428 -13.541 -51.370 1.00 50.36 ? 24 VAL A CG1 1 ATOM 188 C CG2 . VAL A 1 24 ? 48.526 -13.569 -49.991 1.00 49.80 ? 24 VAL A CG2 1 ATOM 189 N N . THR A 1 25 ? 45.107 -10.385 -50.866 1.00 50.11 ? 25 THR A N 1 ATOM 190 C CA . THR A 1 25 ? 43.700 -10.019 -51.045 1.00 50.40 ? 25 THR A CA 1 ATOM 191 C C . THR A 1 25 ? 42.934 -11.153 -51.708 1.00 49.60 ? 25 THR A C 1 ATOM 192 O O . THR A 1 25 ? 43.355 -11.663 -52.753 1.00 50.29 ? 25 THR A O 1 ATOM 193 C CB . THR A 1 25 ? 43.523 -8.782 -51.941 1.00 52.79 ? 25 THR A CB 1 ATOM 194 O OG1 . THR A 1 25 ? 44.410 -7.749 -51.522 1.00 56.08 ? 25 THR A OG1 1 ATOM 195 C CG2 . THR A 1 25 ? 42.103 -8.257 -51.854 1.00 55.47 ? 25 THR A CG2 1 ATOM 196 N N . VAL A 1 26 ? 41.800 -11.524 -51.123 1.00 48.77 ? 26 VAL A N 1 ATOM 197 C CA . VAL A 1 26 ? 40.989 -12.613 -51.652 1.00 47.50 ? 26 VAL A CA 1 ATOM 198 C C . VAL A 1 26 ? 39.555 -12.189 -51.894 1.00 48.81 ? 26 VAL A C 1 ATOM 199 O O . VAL A 1 26 ? 39.077 -11.247 -51.290 1.00 52.69 ? 26 VAL A O 1 ATOM 200 C CB . VAL A 1 26 ? 40.986 -13.832 -50.719 1.00 45.81 ? 26 VAL A CB 1 ATOM 201 C CG1 . VAL A 1 26 ? 42.387 -14.409 -50.614 1.00 44.83 ? 26 VAL A CG1 1 ATOM 202 C CG2 . VAL A 1 26 ? 40.433 -13.475 -49.344 1.00 46.75 ? 26 VAL A CG2 1 ATOM 203 N N . THR A 1 27 ? 38.875 -12.922 -52.769 1.00 50.02 ? 27 THR A N 1 ATOM 204 C CA . THR A 1 27 ? 37.507 -12.613 -53.159 1.00 51.26 ? 27 THR A CA 1 ATOM 205 C C . THR A 1 27 ? 36.543 -12.864 -52.019 1.00 52.29 ? 27 THR A C 1 ATOM 206 O O . THR A 1 27 ? 35.562 -12.141 -51.865 1.00 55.39 ? 27 THR A O 1 ATOM 207 C CB . THR A 1 27 ? 37.062 -13.453 -54.372 1.00 51.73 ? 27 THR A CB 1 ATOM 208 O OG1 . THR A 1 27 ? 37.156 -14.851 -54.068 1.00 50.30 ? 27 THR A OG1 1 ATOM 209 C CG2 . THR A 1 27 ? 37.928 -13.143 -55.577 1.00 51.74 ? 27 THR A CG2 1 ATOM 210 N N . HIS A 1 28 ? 36.818 -13.903 -51.234 1.00 51.13 ? 28 HIS A N 1 ATOM 211 C CA . HIS A 1 28 ? 36.005 -14.236 -50.066 1.00 50.91 ? 28 HIS A CA 1 ATOM 212 C C . HIS A 1 28 ? 36.851 -14.841 -48.961 1.00 49.71 ? 28 HIS A C 1 ATOM 213 O O . HIS A 1 28 ? 37.836 -15.546 -49.223 1.00 46.37 ? 28 HIS A O 1 ATOM 214 C CB . HIS A 1 28 ? 34.907 -15.230 -50.439 1.00 52.27 ? 28 HIS A CB 1 ATOM 215 C CG . HIS A 1 28 ? 34.138 -14.843 -51.657 1.00 53.98 ? 28 HIS A CG 1 ATOM 216 N ND1 . HIS A 1 28 ? 34.617 -15.053 -52.933 1.00 52.91 ? 28 HIS A ND1 1 ATOM 217 C CD2 . HIS A 1 28 ? 32.935 -14.241 -51.797 1.00 55.08 ? 28 HIS A CD2 1 ATOM 218 C CE1 . HIS A 1 28 ? 33.735 -14.604 -53.806 1.00 54.40 ? 28 HIS A CE1 1 ATOM 219 N NE2 . HIS A 1 28 ? 32.706 -14.108 -53.144 1.00 55.23 ? 28 HIS A NE2 1 ATOM 220 N N . ALA A 1 29 ? 36.426 -14.584 -47.729 1.00 50.78 ? 29 ALA A N 1 ATOM 221 C CA . ALA A 1 29 ? 37.122 -15.048 -46.533 1.00 50.65 ? 29 ALA A CA 1 ATOM 222 C C . ALA A 1 29 ? 36.130 -15.216 -45.394 1.00 51.76 ? 29 ALA A C 1 ATOM 223 O O . ALA A 1 29 ? 35.005 -14.707 -45.455 1.00 54.98 ? 29 ALA A O 1 ATOM 224 C CB . ALA A 1 29 ? 38.203 -14.059 -46.139 1.00 51.03 ? 29 ALA A CB 1 ATOM 225 N N . GLN A 1 30 ? 36.547 -15.935 -44.361 1.00 50.82 ? 30 GLN A N 1 ATOM 226 C CA . GLN A 1 30 ? 35.700 -16.180 -43.199 1.00 53.72 ? 30 GLN A CA 1 ATOM 227 C C . GLN A 1 30 ? 36.483 -15.972 -41.898 1.00 52.91 ? 30 GLN A C 1 ATOM 228 O O . GLN A 1 30 ? 37.417 -16.714 -41.588 1.00 48.42 ? 30 GLN A O 1 ATOM 229 C CB . GLN A 1 30 ? 35.116 -17.594 -43.251 1.00 55.03 ? 30 GLN A CB 1 ATOM 230 C CG . GLN A 1 30 ? 34.166 -17.913 -42.102 1.00 58.00 ? 30 GLN A CG 1 ATOM 231 C CD . GLN A 1 30 ? 33.457 -19.244 -42.271 1.00 60.25 ? 30 GLN A CD 1 ATOM 232 O OE1 . GLN A 1 30 ? 33.296 -19.739 -43.382 1.00 64.11 ? 30 GLN A OE1 1 ATOM 233 N NE2 . GLN A 1 30 ? 33.035 -19.833 -41.165 1.00 62.22 ? 30 GLN A NE2 1 ATOM 234 N N . ASP A 1 31 ? 36.096 -14.943 -41.154 1.00 55.82 ? 31 ASP A N 1 ATOM 235 C CA . ASP A 1 31 ? 36.649 -14.684 -39.833 1.00 56.54 ? 31 ASP A CA 1 ATOM 236 C C . ASP A 1 31 ? 36.130 -15.766 -38.883 1.00 55.93 ? 31 ASP A C 1 ATOM 237 O O . ASP A 1 31 ? 34.945 -16.096 -38.912 1.00 55.77 ? 31 ASP A O 1 ATOM 238 C CB . ASP A 1 31 ? 36.211 -13.293 -39.365 1.00 58.36 ? 31 ASP A CB 1 ATOM 239 C CG . ASP A 1 31 ? 36.900 -12.849 -38.093 1.00 59.35 ? 31 ASP A CG 1 ATOM 240 O OD1 . ASP A 1 31 ? 37.725 -13.600 -37.536 1.00 57.68 ? 31 ASP A OD1 1 ATOM 241 O OD2 . ASP A 1 31 ? 36.608 -11.726 -37.643 1.00 65.21 ? 31 ASP A OD2 1 ATOM 242 N N . ILE A 1 32 ? 37.017 -16.320 -38.057 1.00 53.63 ? 32 ILE A N 1 ATOM 243 C CA . ILE A 1 32 ? 36.630 -17.363 -37.099 1.00 53.13 ? 32 ILE A CA 1 ATOM 244 C C . ILE A 1 32 ? 36.990 -17.037 -35.643 1.00 53.35 ? 32 ILE A C 1 ATOM 245 O O . ILE A 1 32 ? 36.936 -17.918 -34.780 1.00 51.29 ? 32 ILE A O 1 ATOM 246 C CB . ILE A 1 32 ? 37.258 -18.721 -37.468 1.00 51.12 ? 32 ILE A CB 1 ATOM 247 C CG1 . ILE A 1 32 ? 38.781 -18.624 -37.493 1.00 49.55 ? 32 ILE A CG1 1 ATOM 248 C CG2 . ILE A 1 32 ? 36.730 -19.203 -38.806 1.00 51.89 ? 32 ILE A CG2 1 ATOM 249 C CD1 . ILE A 1 32 ? 39.455 -19.965 -37.649 1.00 49.92 ? 32 ILE A CD1 1 ATOM 250 N N . LEU A 1 33 ? 37.344 -15.781 -35.377 1.00 53.37 ? 33 LEU A N 1 ATOM 251 C CA . LEU A 1 33 ? 37.727 -15.339 -34.044 1.00 54.08 ? 33 LEU A CA 1 ATOM 252 C C . LEU A 1 33 ? 36.790 -14.248 -33.553 1.00 57.62 ? 33 LEU A C 1 ATOM 253 O O . LEU A 1 33 ? 36.703 -13.178 -34.160 1.00 59.21 ? 33 LEU A O 1 ATOM 254 C CB . LEU A 1 33 ? 39.155 -14.804 -34.064 1.00 52.94 ? 33 LEU A CB 1 ATOM 255 C CG . LEU A 1 33 ? 39.748 -14.352 -32.727 1.00 52.72 ? 33 LEU A CG 1 ATOM 256 C CD1 . LEU A 1 33 ? 39.948 -15.531 -31.793 1.00 50.22 ? 33 LEU A CD1 1 ATOM 257 C CD2 . LEU A 1 33 ? 41.069 -13.633 -32.952 1.00 54.12 ? 33 LEU A CD2 1 ATOM 258 N N . GLU A 1 34 ? 36.091 -14.517 -32.453 1.00 60.44 ? 34 GLU A N 1 ATOM 259 C CA . GLU A 1 34 ? 35.263 -13.501 -31.816 1.00 62.17 ? 34 GLU A CA 1 ATOM 260 C C . GLU A 1 34 ? 36.129 -12.545 -30.997 1.00 61.49 ? 34 GLU A C 1 ATOM 261 O O . GLU A 1 34 ? 36.875 -12.972 -30.121 1.00 59.21 ? 34 GLU A O 1 ATOM 262 C CB . GLU A 1 34 ? 34.201 -14.142 -30.926 1.00 63.72 ? 34 GLU A CB 1 ATOM 263 C CG . GLU A 1 34 ? 33.224 -13.135 -30.339 1.00 66.27 ? 34 GLU A CG 1 ATOM 264 C CD . GLU A 1 34 ? 32.684 -12.184 -31.386 1.00 69.11 ? 34 GLU A CD 1 ATOM 265 O OE1 . GLU A 1 34 ? 31.962 -12.649 -32.295 1.00 72.31 ? 34 GLU A OE1 1 ATOM 266 O OE2 . GLU A 1 34 ? 33.006 -10.979 -31.321 1.00 71.57 ? 34 GLU A OE2 1 ATOM 267 N N . LYS A 1 35 ? 36.019 -11.252 -31.291 1.00 64.30 ? 35 LYS A N 1 ATOM 268 C CA . LYS A 1 35 ? 36.865 -10.228 -30.670 1.00 64.82 ? 35 LYS A CA 1 ATOM 269 C C . LYS A 1 35 ? 36.113 -9.294 -29.725 1.00 65.85 ? 35 LYS A C 1 ATOM 270 O O . LYS A 1 35 ? 36.746 -8.545 -28.982 1.00 66.43 ? 35 LYS A O 1 ATOM 271 C CB . LYS A 1 35 ? 37.564 -9.398 -31.754 1.00 66.05 ? 35 LYS A CB 1 ATOM 272 C CG . LYS A 1 35 ? 38.853 -10.009 -32.273 1.00 65.31 ? 35 LYS A CG 1 ATOM 273 C CD . LYS A 1 35 ? 39.398 -9.241 -33.472 1.00 67.09 ? 35 LYS A CD 1 ATOM 274 C CE . LYS A 1 35 ? 39.153 -9.963 -34.792 1.00 67.51 ? 35 LYS A CE 1 ATOM 275 N NZ . LYS A 1 35 ? 37.723 -10.287 -35.074 1.00 68.61 ? 35 LYS A NZ 1 ATOM 276 N N . THR A 1 36 ? 34.782 -9.344 -29.742 1.00 66.92 ? 36 THR A N 1 ATOM 277 C CA . THR A 1 36 ? 33.969 -8.416 -28.965 1.00 71.89 ? 36 THR A CA 1 ATOM 278 C C . THR A 1 36 ? 33.233 -9.095 -27.818 1.00 72.63 ? 36 THR A C 1 ATOM 279 O O . THR A 1 36 ? 32.905 -10.279 -27.894 1.00 69.11 ? 36 THR A O 1 ATOM 280 C CB . THR A 1 36 ? 32.913 -7.717 -29.845 1.00 75.83 ? 36 THR A CB 1 ATOM 281 O OG1 . THR A 1 36 ? 31.981 -8.684 -30.345 1.00 77.84 ? 36 THR A OG1 1 ATOM 282 C CG2 . THR A 1 36 ? 33.572 -6.990 -31.011 1.00 75.95 ? 36 THR A CG2 1 ATOM 283 N N . HIS A 1 37 ? 32.978 -8.309 -26.769 1.00 74.24 ? 37 HIS A N 1 ATOM 284 C CA . HIS A 1 37 ? 32.141 -8.696 -25.630 1.00 75.20 ? 37 HIS A CA 1 ATOM 285 C C . HIS A 1 37 ? 31.285 -7.482 -25.250 1.00 78.84 ? 37 HIS A C 1 ATOM 286 O O . HIS A 1 37 ? 31.559 -6.373 -25.710 1.00 79.79 ? 37 HIS A O 1 ATOM 287 C CB . HIS A 1 37 ? 33.008 -9.133 -24.443 1.00 74.41 ? 37 HIS A CB 1 ATOM 288 C CG . HIS A 1 37 ? 33.996 -8.095 -23.995 1.00 76.26 ? 37 HIS A CG 1 ATOM 289 N ND1 . HIS A 1 37 ? 33.785 -7.288 -22.899 1.00 77.82 ? 37 HIS A ND1 1 ATOM 290 C CD2 . HIS A 1 37 ? 35.198 -7.728 -24.502 1.00 76.72 ? 37 HIS A CD2 1 ATOM 291 C CE1 . HIS A 1 37 ? 34.812 -6.473 -22.744 1.00 77.78 ? 37 HIS A CE1 1 ATOM 292 N NE2 . HIS A 1 37 ? 35.685 -6.718 -23.704 1.00 78.03 ? 37 HIS A NE2 1 ATOM 293 N N . ASN A 1 38 ? 30.262 -7.683 -24.419 1.00 80.06 ? 38 ASN A N 1 ATOM 294 C CA . ASN A 1 38 ? 29.346 -6.586 -24.045 1.00 81.59 ? 38 ASN A CA 1 ATOM 295 C C . ASN A 1 38 ? 29.783 -5.786 -22.806 1.00 82.44 ? 38 ASN A C 1 ATOM 296 O O . ASN A 1 38 ? 29.155 -4.795 -22.449 1.00 85.13 ? 38 ASN A O 1 ATOM 297 C CB . ASN A 1 38 ? 27.903 -7.098 -23.882 1.00 81.85 ? 38 ASN A CB 1 ATOM 298 C CG . ASN A 1 38 ? 27.702 -7.942 -22.637 1.00 80.39 ? 38 ASN A CG 1 ATOM 299 O OD1 . ASN A 1 38 ? 28.655 -8.304 -21.949 1.00 80.74 ? 38 ASN A OD1 1 ATOM 300 N ND2 . ASN A 1 38 ? 26.452 -8.273 -22.350 1.00 80.45 ? 38 ASN A ND2 1 ATOM 301 N N . GLY A 1 39 ? 30.843 -6.237 -22.146 1.00 81.38 ? 39 GLY A N 1 ATOM 302 C CA . GLY A 1 39 ? 31.479 -5.472 -21.069 1.00 82.12 ? 39 GLY A CA 1 ATOM 303 C C . GLY A 1 39 ? 30.777 -5.570 -19.726 1.00 83.41 ? 39 GLY A C 1 ATOM 304 O O . GLY A 1 39 ? 31.050 -4.772 -18.820 1.00 80.16 ? 39 GLY A O 1 ATOM 305 N N . LYS A 1 40 ? 29.889 -6.558 -19.593 1.00 84.83 ? 40 LYS A N 1 ATOM 306 C CA . LYS A 1 40 ? 28.999 -6.663 -18.440 1.00 86.26 ? 40 LYS A CA 1 ATOM 307 C C . LYS A 1 40 ? 28.958 -8.066 -17.832 1.00 85.27 ? 40 LYS A C 1 ATOM 308 O O . LYS A 1 40 ? 29.193 -9.063 -18.516 1.00 84.18 ? 40 LYS A O 1 ATOM 309 C CB . LYS A 1 40 ? 27.589 -6.246 -18.857 1.00 89.15 ? 40 LYS A CB 1 ATOM 310 C CG . LYS A 1 40 ? 27.499 -4.792 -19.287 1.00 92.48 ? 40 LYS A CG 1 ATOM 311 C CD . LYS A 1 40 ? 26.152 -4.429 -19.882 1.00 95.26 ? 40 LYS A CD 1 ATOM 312 C CE . LYS A 1 40 ? 26.147 -2.970 -20.309 1.00 98.87 ? 40 LYS A CE 1 ATOM 313 N NZ . LYS A 1 40 ? 24.775 -2.462 -20.578 1.00 104.35 ? 40 LYS A NZ 1 ATOM 314 N N . LEU A 1 41 ? 28.666 -8.128 -16.536 1.00 87.24 ? 41 LEU A N 1 ATOM 315 C CA . LEU A 1 41 ? 28.354 -9.389 -15.869 1.00 87.08 ? 41 LEU A CA 1 ATOM 316 C C . LEU A 1 41 ? 26.861 -9.643 -16.019 1.00 86.98 ? 41 LEU A C 1 ATOM 317 O O . LEU A 1 41 ? 26.049 -8.757 -15.753 1.00 89.18 ? 41 LEU A O 1 ATOM 318 C CB . LEU A 1 41 ? 28.738 -9.328 -14.393 1.00 88.18 ? 41 LEU A CB 1 ATOM 319 C CG . LEU A 1 41 ? 30.216 -9.039 -14.128 1.00 88.70 ? 41 LEU A CG 1 ATOM 320 C CD1 . LEU A 1 41 ? 30.465 -8.976 -12.633 1.00 90.15 ? 41 LEU A CD1 1 ATOM 321 C CD2 . LEU A 1 41 ? 31.119 -10.082 -14.780 1.00 86.71 ? 41 LEU A CD2 1 ATOM 322 N N . CYS A 1 42 ? 26.505 -10.850 -16.445 1.00 85.22 ? 42 CYS A N 1 ATOM 323 C CA . CYS A 1 42 ? 25.138 -11.148 -16.853 1.00 88.79 ? 42 CYS A CA 1 ATOM 324 C C . CYS A 1 42 ? 24.644 -12.450 -16.274 1.00 85.03 ? 42 CYS A C 1 ATOM 325 O O . CYS A 1 42 ? 25.432 -13.286 -15.839 1.00 79.99 ? 42 CYS A O 1 ATOM 326 C CB . CYS A 1 42 ? 25.057 -11.243 -18.381 1.00 92.46 ? 42 CYS A CB 1 ATOM 327 S SG . CYS A 1 42 ? 25.693 -9.792 -19.245 1.00 95.46 ? 42 CYS A SG 1 ATOM 328 N N . ASP A 1 43 ? 23.326 -12.622 -16.298 1.00 86.95 ? 43 ASP A N 1 ATOM 329 C CA . ASP A 1 43 ? 22.723 -13.903 -15.964 1.00 87.64 ? 43 ASP A CA 1 ATOM 330 C C . ASP A 1 43 ? 23.241 -14.943 -16.944 1.00 85.21 ? 43 ASP A C 1 ATOM 331 O O . ASP A 1 43 ? 23.354 -14.671 -18.139 1.00 85.10 ? 43 ASP A O 1 ATOM 332 C CB . ASP A 1 43 ? 21.192 -13.848 -16.053 1.00 91.72 ? 43 ASP A CB 1 ATOM 333 C CG . ASP A 1 43 ? 20.570 -12.856 -15.081 1.00 94.37 ? 43 ASP A CG 1 ATOM 334 O OD1 . ASP A 1 43 ? 21.170 -12.565 -14.029 1.00 92.82 ? 43 ASP A OD1 1 ATOM 335 O OD2 . ASP A 1 43 ? 19.463 -12.362 -15.376 1.00 98.87 ? 43 ASP A OD2 1 ATOM 336 N N . LEU A 1 44 ? 23.579 -16.119 -16.432 1.00 85.73 ? 44 LEU A N 1 ATOM 337 C CA . LEU A 1 44 ? 23.914 -17.255 -17.275 1.00 86.33 ? 44 LEU A CA 1 ATOM 338 C C . LEU A 1 44 ? 22.647 -18.072 -17.503 1.00 90.71 ? 44 LEU A C 1 ATOM 339 O O . LEU A 1 44 ? 22.078 -18.614 -16.558 1.00 91.74 ? 44 LEU A O 1 ATOM 340 C CB . LEU A 1 44 ? 24.987 -18.121 -16.613 1.00 84.17 ? 44 LEU A CB 1 ATOM 341 C CG . LEU A 1 44 ? 25.492 -19.323 -17.418 1.00 84.97 ? 44 LEU A CG 1 ATOM 342 C CD1 . LEU A 1 44 ? 26.157 -18.873 -18.714 1.00 85.01 ? 44 LEU A CD1 1 ATOM 343 C CD2 . LEU A 1 44 ? 26.455 -20.160 -16.592 1.00 83.24 ? 44 LEU A CD2 1 ATOM 344 N N . ASP A 1 45 ? 22.190 -18.129 -18.753 1.00 95.25 ? 45 ASP A N 1 ATOM 345 C CA . ASP A 1 45 ? 21.052 -18.971 -19.124 1.00 98.76 ? 45 ASP A CA 1 ATOM 346 C C . ASP A 1 45 ? 19.839 -18.693 -18.221 1.00 98.64 ? 45 ASP A C 1 ATOM 347 O O . ASP A 1 45 ? 19.136 -19.615 -17.800 1.00 97.33 ? 45 ASP A O 1 ATOM 348 C CB . ASP A 1 45 ? 21.474 -20.445 -19.041 1.00 101.64 ? 45 ASP A CB 1 ATOM 349 C CG . ASP A 1 45 ? 20.514 -21.376 -19.747 1.00 107.39 ? 45 ASP A CG 1 ATOM 350 O OD1 . ASP A 1 45 ? 20.349 -21.242 -20.977 1.00 113.72 ? 45 ASP A OD1 1 ATOM 351 O OD2 . ASP A 1 45 ? 19.935 -22.252 -19.068 1.00 110.70 ? 45 ASP A OD2 1 ATOM 352 N N . GLY A 1 46 ? 19.624 -17.414 -17.911 1.00 97.52 ? 46 GLY A N 1 ATOM 353 C CA . GLY A 1 46 ? 18.535 -16.982 -17.035 1.00 98.09 ? 46 GLY A CA 1 ATOM 354 C C . GLY A 1 46 ? 18.882 -16.944 -15.554 1.00 96.80 ? 46 GLY A C 1 ATOM 355 O O . GLY A 1 46 ? 18.310 -16.146 -14.808 1.00 97.07 ? 46 GLY A O 1 ATOM 356 N N . VAL A 1 47 ? 19.820 -17.794 -15.128 1.00 91.98 ? 47 VAL A N 1 ATOM 357 C CA . VAL A 1 47 ? 20.151 -17.962 -13.710 1.00 89.34 ? 47 VAL A CA 1 ATOM 358 C C . VAL A 1 47 ? 21.196 -16.937 -13.260 1.00 87.54 ? 47 VAL A C 1 ATOM 359 O O . VAL A 1 47 ? 22.351 -16.994 -13.680 1.00 85.13 ? 47 VAL A O 1 ATOM 360 C CB . VAL A 1 47 ? 20.687 -19.382 -13.431 1.00 86.87 ? 47 VAL A CB 1 ATOM 361 C CG1 . VAL A 1 47 ? 20.977 -19.561 -11.947 1.00 87.78 ? 47 VAL A CG1 1 ATOM 362 C CG2 . VAL A 1 47 ? 19.701 -20.434 -13.918 1.00 87.96 ? 47 VAL A CG2 1 ATOM 363 N N . LYS A 1 48 ? 20.793 -16.021 -12.386 1.00 89.75 ? 48 LYS A N 1 ATOM 364 C CA . LYS A 1 48 ? 21.656 -14.918 -11.949 1.00 89.51 ? 48 LYS A CA 1 ATOM 365 C C . LYS A 1 48 ? 22.865 -15.385 -11.120 1.00 86.27 ? 48 LYS A C 1 ATOM 366 O O . LYS A 1 48 ? 22.752 -16.327 -10.335 1.00 86.42 ? 48 LYS A O 1 ATOM 367 C CB . LYS A 1 48 ? 20.830 -13.899 -11.145 1.00 92.91 ? 48 LYS A CB 1 ATOM 368 C CG . LYS A 1 48 ? 21.560 -12.600 -10.836 1.00 94.29 ? 48 LYS A CG 1 ATOM 369 C CD . LYS A 1 48 ? 20.800 -11.693 -9.881 1.00 98.04 ? 48 LYS A CD 1 ATOM 370 C CE . LYS A 1 48 ? 21.705 -10.568 -9.398 1.00 98.26 ? 48 LYS A CE 1 ATOM 371 N NZ . LYS A 1 48 ? 20.960 -9.462 -8.743 1.00 104.10 ? 48 LYS A NZ 1 ATOM 372 N N . PRO A 1 49 ? 24.030 -14.727 -11.297 1.00 83.58 ? 49 PRO A N 1 ATOM 373 C CA . PRO A 1 49 ? 25.185 -15.056 -10.458 1.00 80.29 ? 49 PRO A CA 1 ATOM 374 C C . PRO A 1 49 ? 25.100 -14.442 -9.072 1.00 79.60 ? 49 PRO A C 1 ATOM 375 O O . PRO A 1 49 ? 24.388 -13.457 -8.875 1.00 81.13 ? 49 PRO A O 1 ATOM 376 C CB . PRO A 1 49 ? 26.354 -14.418 -11.210 1.00 77.40 ? 49 PRO A CB 1 ATOM 377 C CG . PRO A 1 49 ? 25.741 -13.240 -11.881 1.00 80.20 ? 49 PRO A CG 1 ATOM 378 C CD . PRO A 1 49 ? 24.378 -13.715 -12.314 1.00 82.50 ? 49 PRO A CD 1 ATOM 379 N N . LEU A 1 50 ? 25.842 -15.022 -8.132 1.00 77.13 ? 50 LEU A N 1 ATOM 380 C CA . LEU A 1 50 ? 26.017 -14.443 -6.808 1.00 77.52 ? 50 LEU A CA 1 ATOM 381 C C . LEU A 1 50 ? 27.117 -13.398 -6.892 1.00 77.10 ? 50 LEU A C 1 ATOM 382 O O . LEU A 1 50 ? 28.280 -13.742 -7.096 1.00 76.40 ? 50 LEU A O 1 ATOM 383 C CB . LEU A 1 50 ? 26.393 -15.527 -5.791 1.00 75.77 ? 50 LEU A CB 1 ATOM 384 C CG . LEU A 1 50 ? 26.754 -15.083 -4.368 1.00 75.99 ? 50 LEU A CG 1 ATOM 385 C CD1 . LEU A 1 50 ? 25.673 -14.200 -3.763 1.00 78.25 ? 50 LEU A CD1 1 ATOM 386 C CD2 . LEU A 1 50 ? 27.011 -16.288 -3.476 1.00 75.35 ? 50 LEU A CD2 1 ATOM 387 N N . ILE A 1 51 ? 26.750 -12.126 -6.755 1.00 79.94 ? 51 ILE A N 1 ATOM 388 C CA . ILE A 1 51 ? 27.725 -11.036 -6.808 1.00 80.55 ? 51 ILE A CA 1 ATOM 389 C C . ILE A 1 51 ? 28.005 -10.544 -5.395 1.00 80.82 ? 51 ILE A C 1 ATOM 390 O O . ILE A 1 51 ? 27.254 -9.736 -4.844 1.00 81.12 ? 51 ILE A O 1 ATOM 391 C CB . ILE A 1 51 ? 27.250 -9.878 -7.718 1.00 83.26 ? 51 ILE A CB 1 ATOM 392 C CG1 . ILE A 1 51 ? 26.930 -10.433 -9.110 1.00 84.31 ? 51 ILE A CG1 1 ATOM 393 C CG2 . ILE A 1 51 ? 28.305 -8.774 -7.790 1.00 82.57 ? 51 ILE A CG2 1 ATOM 394 C CD1 . ILE A 1 51 ? 26.961 -9.416 -10.233 1.00 86.84 ? 51 ILE A CD1 1 ATOM 395 N N . LEU A 1 52 ? 29.114 -11.021 -4.832 1.00 78.72 ? 52 LEU A N 1 ATOM 396 C CA . LEU A 1 52 ? 29.465 -10.753 -3.437 1.00 79.57 ? 52 LEU A CA 1 ATOM 397 C C . LEU A 1 52 ? 29.804 -9.285 -3.142 1.00 82.58 ? 52 LEU A C 1 ATOM 398 O O . LEU A 1 52 ? 29.895 -8.892 -1.971 1.00 82.18 ? 52 LEU A O 1 ATOM 399 C CB . LEU A 1 52 ? 30.616 -11.666 -2.998 1.00 76.20 ? 52 LEU A CB 1 ATOM 400 C CG . LEU A 1 52 ? 30.307 -13.170 -3.021 1.00 74.97 ? 52 LEU A CG 1 ATOM 401 C CD1 . LEU A 1 52 ? 31.553 -14.000 -2.746 1.00 72.07 ? 52 LEU A CD1 1 ATOM 402 C CD2 . LEU A 1 52 ? 29.210 -13.517 -2.027 1.00 77.33 ? 52 LEU A CD2 1 ATOM 403 N N . ARG A 1 53 ? 29.990 -8.486 -4.193 1.00 83.49 ? 53 ARG A N 1 ATOM 404 C CA . ARG A 1 53 ? 30.164 -7.041 -4.063 1.00 88.73 ? 53 ARG A CA 1 ATOM 405 C C . ARG A 1 53 ? 31.453 -6.725 -3.283 1.00 89.83 ? 53 ARG A C 1 ATOM 406 O O . ARG A 1 53 ? 32.541 -7.076 -3.743 1.00 93.35 ? 53 ARG A O 1 ATOM 407 C CB . ARG A 1 53 ? 28.904 -6.413 -3.447 1.00 93.59 ? 53 ARG A CB 1 ATOM 408 C CG . ARG A 1 53 ? 28.692 -4.951 -3.809 1.00 98.40 ? 53 ARG A CG 1 ATOM 409 C CD . ARG A 1 53 ? 27.540 -4.338 -3.023 1.00 103.61 ? 53 ARG A CD 1 ATOM 410 N NE . ARG A 1 53 ? 26.642 -3.561 -3.878 1.00 107.58 ? 53 ARG A NE 1 ATOM 411 C CZ . ARG A 1 53 ? 25.665 -4.073 -4.629 1.00 108.91 ? 53 ARG A CZ 1 ATOM 412 N NH1 . ARG A 1 53 ? 25.433 -5.385 -4.656 1.00 107.54 ? 53 ARG A NH1 1 ATOM 413 N NH2 . ARG A 1 53 ? 24.909 -3.266 -5.366 1.00 110.70 ? 53 ARG A NH2 1 ATOM 414 N N . ASP A 1 54 ? 31.349 -6.084 -2.120 1.00 92.00 ? 54 ASP A N 1 ATOM 415 C CA . ASP A 1 54 ? 32.519 -5.809 -1.286 1.00 91.74 ? 54 ASP A CA 1 ATOM 416 C C . ASP A 1 54 ? 32.841 -6.939 -0.303 1.00 90.38 ? 54 ASP A C 1 ATOM 417 O O . ASP A 1 54 ? 33.848 -6.863 0.401 1.00 91.88 ? 54 ASP A O 1 ATOM 418 C CB . ASP A 1 54 ? 32.320 -4.507 -0.503 1.00 95.38 ? 54 ASP A CB 1 ATOM 419 C CG . ASP A 1 54 ? 32.299 -3.279 -1.396 1.00 97.64 ? 54 ASP A CG 1 ATOM 420 O OD1 . ASP A 1 54 ? 33.008 -3.272 -2.427 1.00 93.18 ? 54 ASP A OD1 1 ATOM 421 O OD2 . ASP A 1 54 ? 31.580 -2.311 -1.049 1.00 102.13 ? 54 ASP A OD2 1 ATOM 422 N N . CYS A 1 55 ? 32.001 -7.972 -0.238 1.00 88.74 ? 55 CYS A N 1 ATOM 423 C CA . CYS A 1 55 ? 32.250 -9.101 0.667 1.00 87.59 ? 55 CYS A CA 1 ATOM 424 C C . CYS A 1 55 ? 33.110 -10.179 -0.001 1.00 81.67 ? 55 CYS A C 1 ATOM 425 O O . CYS A 1 55 ? 33.110 -10.322 -1.219 1.00 81.06 ? 55 CYS A O 1 ATOM 426 C CB . CYS A 1 55 ? 30.932 -9.711 1.176 1.00 89.16 ? 55 CYS A CB 1 ATOM 427 S SG . CYS A 1 55 ? 29.900 -8.575 2.140 1.00 97.19 ? 55 CYS A SG 1 ATOM 428 N N . SER A 1 56 ? 33.853 -10.916 0.820 1.00 78.50 ? 56 SER A N 1 ATOM 429 C CA . SER A 1 56 ? 34.583 -12.099 0.384 1.00 74.58 ? 56 SER A CA 1 ATOM 430 C C . SER A 1 56 ? 33.731 -13.337 0.645 1.00 73.58 ? 56 SER A C 1 ATOM 431 O O . SER A 1 56 ? 32.641 -13.248 1.210 1.00 75.00 ? 56 SER A O 1 ATOM 432 C CB . SER A 1 56 ? 35.896 -12.229 1.154 1.00 72.98 ? 56 SER A CB 1 ATOM 433 O OG . SER A 1 56 ? 35.655 -12.686 2.476 1.00 73.36 ? 56 SER A OG 1 ATOM 434 N N . VAL A 1 57 ? 34.245 -14.494 0.247 1.00 71.10 ? 57 VAL A N 1 ATOM 435 C CA . VAL A 1 57 ? 33.553 -15.762 0.477 1.00 70.21 ? 57 VAL A CA 1 ATOM 436 C C . VAL A 1 57 ? 33.515 -16.069 1.978 1.00 70.39 ? 57 VAL A C 1 ATOM 437 O O . VAL A 1 57 ? 32.530 -16.609 2.481 1.00 70.49 ? 57 VAL A O 1 ATOM 438 C CB . VAL A 1 57 ? 34.219 -16.911 -0.315 1.00 67.33 ? 57 VAL A CB 1 ATOM 439 C CG1 . VAL A 1 57 ? 33.632 -18.259 0.066 1.00 67.01 ? 57 VAL A CG1 1 ATOM 440 C CG2 . VAL A 1 57 ? 34.066 -16.673 -1.813 1.00 67.57 ? 57 VAL A CG2 1 ATOM 441 N N . ALA A 1 58 ? 34.587 -15.710 2.683 1.00 69.36 ? 58 ALA A N 1 ATOM 442 C CA . ALA A 1 58 ? 34.660 -15.887 4.133 1.00 69.64 ? 58 ALA A CA 1 ATOM 443 C C . ALA A 1 58 ? 33.641 -14.996 4.847 1.00 71.39 ? 58 ALA A C 1 ATOM 444 O O . ALA A 1 58 ? 32.860 -15.473 5.678 1.00 71.08 ? 58 ALA A O 1 ATOM 445 C CB . ALA A 1 58 ? 36.062 -15.586 4.630 1.00 68.39 ? 58 ALA A CB 1 ATOM 446 N N . GLY A 1 59 ? 33.648 -13.707 4.506 1.00 71.93 ? 59 GLY A N 1 ATOM 447 C CA . GLY A 1 59 ? 32.701 -12.745 5.066 1.00 72.32 ? 59 GLY A CA 1 ATOM 448 C C . GLY A 1 59 ? 31.270 -13.194 4.852 1.00 74.22 ? 59 GLY A C 1 ATOM 449 O O . GLY A 1 59 ? 30.435 -13.082 5.751 1.00 76.64 ? 59 GLY A O 1 ATOM 450 N N . TRP A 1 60 ? 30.988 -13.714 3.659 1.00 71.99 ? 60 TRP A N 1 ATOM 451 C CA . TRP A 1 60 ? 29.676 -14.264 3.354 1.00 72.71 ? 60 TRP A CA 1 ATOM 452 C C . TRP A 1 60 ? 29.346 -15.457 4.254 1.00 73.39 ? 60 TRP A C 1 ATOM 453 O O . TRP A 1 60 ? 28.341 -15.442 4.967 1.00 75.23 ? 60 TRP A O 1 ATOM 454 C CB . TRP A 1 60 ? 29.608 -14.666 1.879 1.00 71.96 ? 60 TRP A CB 1 ATOM 455 C CG . TRP A 1 60 ? 28.458 -15.554 1.520 1.00 72.54 ? 60 TRP A CG 1 ATOM 456 C CD1 . TRP A 1 60 ? 27.181 -15.482 1.995 1.00 75.62 ? 60 TRP A CD1 1 ATOM 457 C CD2 . TRP A 1 60 ? 28.477 -16.634 0.584 1.00 70.92 ? 60 TRP A CD2 1 ATOM 458 N NE1 . TRP A 1 60 ? 26.407 -16.462 1.420 1.00 75.84 ? 60 TRP A NE1 1 ATOM 459 C CE2 . TRP A 1 60 ? 27.180 -17.183 0.552 1.00 72.82 ? 60 TRP A CE2 1 ATOM 460 C CE3 . TRP A 1 60 ? 29.468 -17.195 -0.227 1.00 68.26 ? 60 TRP A CE3 1 ATOM 461 C CZ2 . TRP A 1 60 ? 26.848 -18.265 -0.258 1.00 73.29 ? 60 TRP A CZ2 1 ATOM 462 C CZ3 . TRP A 1 60 ? 29.138 -18.271 -1.030 1.00 67.54 ? 60 TRP A CZ3 1 ATOM 463 C CH2 . TRP A 1 60 ? 27.840 -18.793 -1.043 1.00 69.96 ? 60 TRP A CH2 1 ATOM 464 N N . LEU A 1 61 ? 30.199 -16.477 4.232 1.00 72.11 ? 61 LEU A N 1 ATOM 465 C CA . LEU A 1 61 ? 29.875 -17.755 4.876 1.00 72.67 ? 61 LEU A CA 1 ATOM 466 C C . LEU A 1 61 ? 29.822 -17.672 6.399 1.00 73.65 ? 61 LEU A C 1 ATOM 467 O O . LEU A 1 61 ? 28.927 -18.243 7.023 1.00 74.49 ? 61 LEU A O 1 ATOM 468 C CB . LEU A 1 61 ? 30.850 -18.849 4.436 1.00 70.50 ? 61 LEU A CB 1 ATOM 469 C CG . LEU A 1 61 ? 30.692 -19.313 2.984 1.00 70.31 ? 61 LEU A CG 1 ATOM 470 C CD1 . LEU A 1 61 ? 31.728 -20.378 2.662 1.00 69.20 ? 61 LEU A CD1 1 ATOM 471 C CD2 . LEU A 1 61 ? 29.290 -19.835 2.705 1.00 71.90 ? 61 LEU A CD2 1 ATOM 472 N N . LEU A 1 62 ? 30.778 -16.960 6.986 1.00 72.99 ? 62 LEU A N 1 ATOM 473 C CA . LEU A 1 62 ? 30.779 -16.711 8.430 1.00 73.88 ? 62 LEU A CA 1 ATOM 474 C C . LEU A 1 62 ? 29.665 -15.755 8.866 1.00 76.41 ? 62 LEU A C 1 ATOM 475 O O . LEU A 1 62 ? 29.246 -15.774 10.023 1.00 78.69 ? 62 LEU A O 1 ATOM 476 C CB . LEU A 1 62 ? 32.133 -16.157 8.866 1.00 71.88 ? 62 LEU A CB 1 ATOM 477 C CG . LEU A 1 62 ? 33.278 -17.159 8.757 1.00 69.28 ? 62 LEU A CG 1 ATOM 478 C CD1 . LEU A 1 62 ? 34.608 -16.438 8.859 1.00 68.99 ? 62 LEU A CD1 1 ATOM 479 C CD2 . LEU A 1 62 ? 33.169 -18.233 9.830 1.00 70.34 ? 62 LEU A CD2 1 ATOM 480 N N . GLY A 1 63 ? 29.190 -14.927 7.940 1.00 77.74 ? 63 GLY A N 1 ATOM 481 C CA . GLY A 1 63 ? 28.123 -13.976 8.221 1.00 80.57 ? 63 GLY A CA 1 ATOM 482 C C . GLY A 1 63 ? 28.651 -12.683 8.813 1.00 81.66 ? 63 GLY A C 1 ATOM 483 O O . GLY A 1 63 ? 28.126 -12.200 9.815 1.00 82.04 ? 63 GLY A O 1 ATOM 484 N N . ASN A 1 64 ? 29.699 -12.133 8.198 1.00 80.80 ? 64 ASN A N 1 ATOM 485 C CA . ASN A 1 64 ? 30.195 -10.800 8.531 1.00 82.62 ? 64 ASN A CA 1 ATOM 486 C C . ASN A 1 64 ? 29.013 -9.838 8.557 1.00 85.87 ? 64 ASN A C 1 ATOM 487 O O . ASN A 1 64 ? 28.231 -9.810 7.605 1.00 85.31 ? 64 ASN A O 1 ATOM 488 C CB . ASN A 1 64 ? 31.235 -10.346 7.492 1.00 81.40 ? 64 ASN A CB 1 ATOM 489 C CG . ASN A 1 64 ? 31.801 -8.956 7.771 1.00 82.69 ? 64 ASN A CG 1 ATOM 490 O OD1 . ASN A 1 64 ? 31.063 -7.991 7.970 1.00 84.52 ? 64 ASN A OD1 1 ATOM 491 N ND2 . ASN A 1 64 ? 33.125 -8.847 7.753 1.00 81.18 ? 64 ASN A ND2 1 ATOM 492 N N . PRO A 1 65 ? 28.874 -9.049 9.642 1.00 88.73 ? 65 PRO A N 1 ATOM 493 C CA . PRO A 1 65 ? 27.685 -8.196 9.812 1.00 93.20 ? 65 PRO A CA 1 ATOM 494 C C . PRO A 1 65 ? 27.476 -7.143 8.712 1.00 95.26 ? 65 PRO A C 1 ATOM 495 O O . PRO A 1 65 ? 26.363 -6.649 8.550 1.00 98.30 ? 65 PRO A O 1 ATOM 496 C CB . PRO A 1 65 ? 27.910 -7.534 11.181 1.00 94.46 ? 65 PRO A CB 1 ATOM 497 C CG . PRO A 1 65 ? 29.370 -7.648 11.445 1.00 91.73 ? 65 PRO A CG 1 ATOM 498 C CD . PRO A 1 65 ? 29.827 -8.898 10.757 1.00 88.65 ? 65 PRO A CD 1 ATOM 499 N N . MET A 1 66 ? 28.529 -6.819 7.963 1.00 96.33 ? 66 MET A N 1 ATOM 500 C CA . MET A 1 66 ? 28.429 -5.936 6.796 1.00 99.07 ? 66 MET A CA 1 ATOM 501 C C . MET A 1 66 ? 27.981 -6.677 5.519 1.00 97.14 ? 66 MET A C 1 ATOM 502 O O . MET A 1 66 ? 27.949 -6.084 4.440 1.00 95.49 ? 66 MET A O 1 ATOM 503 C CB . MET A 1 66 ? 29.785 -5.265 6.538 1.00 99.75 ? 66 MET A CB 1 ATOM 504 C CG . MET A 1 66 ? 30.326 -4.440 7.702 1.00 101.91 ? 66 MET A CG 1 ATOM 505 S SD . MET A 1 66 ? 29.694 -2.750 7.744 1.00 108.41 ? 66 MET A SD 1 ATOM 506 C CE . MET A 1 66 ? 30.478 -2.029 6.300 1.00 107.50 ? 66 MET A CE 1 ATOM 507 N N . CYS A 1 67 ? 27.639 -7.961 5.642 1.00 96.54 ? 67 CYS A N 1 ATOM 508 C CA . CYS A 1 67 ? 27.257 -8.794 4.495 1.00 95.63 ? 67 CYS A CA 1 ATOM 509 C C . CYS A 1 67 ? 25.858 -9.385 4.668 1.00 97.43 ? 67 CYS A C 1 ATOM 510 O O . CYS A 1 67 ? 25.603 -10.534 4.305 1.00 95.65 ? 67 CYS A O 1 ATOM 511 C CB . CYS A 1 67 ? 28.279 -9.917 4.309 1.00 91.98 ? 67 CYS A CB 1 ATOM 512 S SG . CYS A 1 67 ? 29.956 -9.305 4.054 1.00 91.12 ? 67 CYS A SG 1 ATOM 513 N N . ASP A 1 68 ? 24.952 -8.582 5.217 1.00 101.16 ? 68 ASP A N 1 ATOM 514 C CA . ASP A 1 68 ? 23.570 -9.006 5.442 1.00 103.33 ? 68 ASP A CA 1 ATOM 515 C C . ASP A 1 68 ? 22.792 -9.160 4.135 1.00 103.81 ? 68 ASP A C 1 ATOM 516 O O . ASP A 1 68 ? 21.808 -9.897 4.084 1.00 106.14 ? 68 ASP A O 1 ATOM 517 C CB . ASP A 1 68 ? 22.856 -8.015 6.364 1.00 106.62 ? 68 ASP A CB 1 ATOM 518 C CG . ASP A 1 68 ? 23.444 -7.993 7.761 1.00 106.37 ? 68 ASP A CG 1 ATOM 519 O OD1 . ASP A 1 68 ? 24.340 -8.812 8.048 1.00 104.83 ? 68 ASP A OD1 1 ATOM 520 O OD2 . ASP A 1 68 ? 23.009 -7.158 8.580 1.00 110.18 ? 68 ASP A OD2 1 ATOM 521 N N . GLU A 1 69 ? 23.235 -8.465 3.088 1.00 101.58 ? 69 GLU A N 1 ATOM 522 C CA . GLU A 1 69 ? 22.692 -8.648 1.743 1.00 101.81 ? 69 GLU A CA 1 ATOM 523 C C . GLU A 1 69 ? 22.673 -10.130 1.349 1.00 98.49 ? 69 GLU A C 1 ATOM 524 O O . GLU A 1 69 ? 21.732 -10.590 0.701 1.00 99.02 ? 69 GLU A O 1 ATOM 525 C CB . GLU A 1 69 ? 23.521 -7.844 0.730 1.00 102.04 ? 69 GLU A CB 1 ATOM 526 C CG . GLU A 1 69 ? 23.035 -7.919 -0.715 1.00 103.57 ? 69 GLU A CG 1 ATOM 527 C CD . GLU A 1 69 ? 23.941 -7.179 -1.692 1.00 103.03 ? 69 GLU A CD 1 ATOM 528 O OE1 . GLU A 1 69 ? 24.938 -6.565 -1.250 1.00 103.50 ? 69 GLU A OE1 1 ATOM 529 O OE2 . GLU A 1 69 ? 23.656 -7.211 -2.910 1.00 102.87 ? 69 GLU A OE2 1 ATOM 530 N N . PHE A 1 70 ? 23.706 -10.867 1.759 1.00 94.30 ? 70 PHE A N 1 ATOM 531 C CA . PHE A 1 70 ? 23.860 -12.279 1.406 1.00 91.50 ? 70 PHE A CA 1 ATOM 532 C C . PHE A 1 70 ? 23.529 -13.222 2.561 1.00 91.67 ? 70 PHE A C 1 ATOM 533 O O . PHE A 1 70 ? 24.080 -14.323 2.649 1.00 87.57 ? 70 PHE A O 1 ATOM 534 C CB . PHE A 1 70 ? 25.291 -12.534 0.924 1.00 87.96 ? 70 PHE A CB 1 ATOM 535 C CG . PHE A 1 70 ? 25.807 -11.472 0.001 1.00 86.65 ? 70 PHE A CG 1 ATOM 536 C CD1 . PHE A 1 70 ? 25.339 -11.385 -1.300 1.00 86.19 ? 70 PHE A CD1 1 ATOM 537 C CD2 . PHE A 1 70 ? 26.735 -10.538 0.442 1.00 85.55 ? 70 PHE A CD2 1 ATOM 538 C CE1 . PHE A 1 70 ? 25.804 -10.403 -2.153 1.00 85.99 ? 70 PHE A CE1 1 ATOM 539 C CE2 . PHE A 1 70 ? 27.199 -9.550 -0.405 1.00 85.74 ? 70 PHE A CE2 1 ATOM 540 C CZ . PHE A 1 70 ? 26.734 -9.483 -1.706 1.00 85.44 ? 70 PHE A CZ 1 ATOM 541 N N . ILE A 1 71 ? 22.622 -12.795 3.436 1.00 96.39 ? 71 ILE A N 1 ATOM 542 C CA . ILE A 1 71 ? 22.225 -13.608 4.582 1.00 98.63 ? 71 ILE A CA 1 ATOM 543 C C . ILE A 1 71 ? 21.444 -14.845 4.139 1.00 99.33 ? 71 ILE A C 1 ATOM 544 O O . ILE A 1 71 ? 21.525 -15.881 4.786 1.00 98.52 ? 71 ILE A O 1 ATOM 545 C CB . ILE A 1 71 ? 21.418 -12.790 5.626 1.00 103.66 ? 71 ILE A CB 1 ATOM 546 C CG1 . ILE A 1 71 ? 21.307 -13.567 6.945 1.00 103.94 ? 71 ILE A CG1 1 ATOM 547 C CG2 . ILE A 1 71 ? 20.033 -12.411 5.101 1.00 106.73 ? 71 ILE A CG2 1 ATOM 548 C CD1 . ILE A 1 71 ? 20.976 -12.696 8.136 1.00 106.18 ? 71 ILE A CD1 1 ATOM 549 N N . ASN A 1 72 ? 20.690 -14.731 3.046 1.00 101.55 ? 72 ASN A N 1 ATOM 550 C CA . ASN A 1 72 ? 20.045 -15.889 2.417 1.00 102.80 ? 72 ASN A CA 1 ATOM 551 C C . ASN A 1 72 ? 19.955 -15.721 0.902 1.00 101.19 ? 72 ASN A C 1 ATOM 552 O O . ASN A 1 72 ? 19.049 -15.065 0.389 1.00 104.44 ? 72 ASN A O 1 ATOM 553 C CB . ASN A 1 72 ? 18.662 -16.146 3.024 1.00 107.25 ? 72 ASN A CB 1 ATOM 554 C CG . ASN A 1 72 ? 18.726 -17.021 4.265 1.00 109.87 ? 72 ASN A CG 1 ATOM 555 O OD1 . ASN A 1 72 ? 19.441 -18.024 4.294 1.00 109.31 ? 72 ASN A OD1 1 ATOM 556 N ND2 . ASN A 1 72 ? 17.982 -16.645 5.300 1.00 114.16 ? 72 ASN A ND2 1 ATOM 557 N N . VAL A 1 73 ? 20.908 -16.323 0.199 1.00 96.91 ? 73 VAL A N 1 ATOM 558 C CA . VAL A 1 73 ? 21.048 -16.133 -1.243 1.00 94.82 ? 73 VAL A CA 1 ATOM 559 C C . VAL A 1 73 ? 20.436 -17.293 -2.022 1.00 93.83 ? 73 VAL A C 1 ATOM 560 O O . VAL A 1 73 ? 20.679 -18.458 -1.694 1.00 91.54 ? 73 VAL A O 1 ATOM 561 C CB . VAL A 1 73 ? 22.528 -15.970 -1.658 1.00 91.71 ? 73 VAL A CB 1 ATOM 562 C CG1 . VAL A 1 73 ? 23.173 -14.823 -0.894 1.00 91.21 ? 73 VAL A CG1 1 ATOM 563 C CG2 . VAL A 1 73 ? 23.317 -17.261 -1.451 1.00 90.23 ? 73 VAL A CG2 1 ATOM 564 N N . PRO A 1 74 ? 19.650 -16.981 -3.070 1.00 94.26 ? 74 PRO A N 1 ATOM 565 C CA . PRO A 1 74 ? 19.081 -18.043 -3.891 1.00 95.16 ? 74 PRO A CA 1 ATOM 566 C C . PRO A 1 74 ? 20.170 -18.733 -4.703 1.00 91.93 ? 74 PRO A C 1 ATOM 567 O O . PRO A 1 74 ? 21.330 -18.299 -4.682 1.00 86.31 ? 74 PRO A O 1 ATOM 568 C CB . PRO A 1 74 ? 18.115 -17.295 -4.811 1.00 97.25 ? 74 PRO A CB 1 ATOM 569 C CG . PRO A 1 74 ? 18.728 -15.947 -4.961 1.00 96.36 ? 74 PRO A CG 1 ATOM 570 C CD . PRO A 1 74 ? 19.403 -15.647 -3.650 1.00 95.18 ? 74 PRO A CD 1 ATOM 571 N N . GLU A 1 75 ? 19.800 -19.792 -5.417 1.00 92.93 ? 75 GLU A N 1 ATOM 572 C CA . GLU A 1 75 ? 20.783 -20.546 -6.183 1.00 91.66 ? 75 GLU A CA 1 ATOM 573 C C . GLU A 1 75 ? 21.426 -19.681 -7.269 1.00 87.66 ? 75 GLU A C 1 ATOM 574 O O . GLU A 1 75 ? 20.791 -18.779 -7.821 1.00 86.00 ? 75 GLU A O 1 ATOM 575 C CB . GLU A 1 75 ? 20.183 -21.830 -6.768 1.00 95.13 ? 75 GLU A CB 1 ATOM 576 C CG . GLU A 1 75 ? 19.210 -21.667 -7.920 1.00 98.76 ? 75 GLU A CG 1 ATOM 577 C CD . GLU A 1 75 ? 18.980 -22.982 -8.641 1.00 100.57 ? 75 GLU A CD 1 ATOM 578 O OE1 . GLU A 1 75 ? 19.966 -23.534 -9.183 1.00 95.42 ? 75 GLU A OE1 1 ATOM 579 O OE2 . GLU A 1 75 ? 17.825 -23.472 -8.647 1.00 104.75 ? 75 GLU A OE2 1 ATOM 580 N N . TRP A 1 76 ? 22.697 -19.958 -7.547 1.00 84.38 ? 76 TRP A N 1 ATOM 581 C CA . TRP A 1 76 ? 23.477 -19.153 -8.480 1.00 83.09 ? 76 TRP A CA 1 ATOM 582 C C . TRP A 1 76 ? 24.026 -20.005 -9.619 1.00 82.09 ? 76 TRP A C 1 ATOM 583 O O . TRP A 1 76 ? 24.058 -21.237 -9.546 1.00 83.08 ? 76 TRP A O 1 ATOM 584 C CB . TRP A 1 76 ? 24.625 -18.444 -7.751 1.00 80.85 ? 76 TRP A CB 1 ATOM 585 C CG . TRP A 1 76 ? 25.602 -19.389 -7.115 1.00 79.07 ? 76 TRP A CG 1 ATOM 586 C CD1 . TRP A 1 76 ? 26.680 -19.978 -7.711 1.00 76.47 ? 76 TRP A CD1 1 ATOM 587 C CD2 . TRP A 1 76 ? 25.578 -19.866 -5.765 1.00 78.62 ? 76 TRP A CD2 1 ATOM 588 N NE1 . TRP A 1 76 ? 27.330 -20.791 -6.814 1.00 75.93 ? 76 TRP A NE1 1 ATOM 589 C CE2 . TRP A 1 76 ? 26.675 -20.740 -5.612 1.00 76.40 ? 76 TRP A CE2 1 ATOM 590 C CE3 . TRP A 1 76 ? 24.735 -19.640 -4.669 1.00 82.03 ? 76 TRP A CE3 1 ATOM 591 C CZ2 . TRP A 1 76 ? 26.954 -21.387 -4.410 1.00 76.47 ? 76 TRP A CZ2 1 ATOM 592 C CZ3 . TRP A 1 76 ? 25.013 -20.284 -3.469 1.00 80.74 ? 76 TRP A CZ3 1 ATOM 593 C CH2 . TRP A 1 76 ? 26.113 -21.147 -3.351 1.00 78.94 ? 76 TRP A CH2 1 ATOM 594 N N . SER A 1 77 ? 24.447 -19.322 -10.676 1.00 81.86 ? 77 SER A N 1 ATOM 595 C CA . SER A 1 77 ? 25.092 -19.952 -11.819 1.00 78.43 ? 77 SER A CA 1 ATOM 596 C C . SER A 1 77 ? 26.598 -19.930 -11.609 1.00 75.72 ? 77 SER A C 1 ATOM 597 O O . SER A 1 77 ? 27.283 -20.929 -11.819 1.00 76.23 ? 77 SER A O 1 ATOM 598 C CB . SER A 1 77 ? 24.734 -19.186 -13.089 1.00 78.92 ? 77 SER A CB 1 ATOM 599 O OG . SER A 1 77 ? 24.802 -17.785 -12.872 1.00 78.77 ? 77 SER A OG 1 ATOM 600 N N . TYR A 1 78 ? 27.101 -18.770 -11.201 1.00 73.82 ? 78 TYR A N 1 ATOM 601 C CA . TYR A 1 78 ? 28.510 -18.594 -10.878 1.00 69.73 ? 78 TYR A CA 1 ATOM 602 C C . TYR A 1 78 ? 28.643 -17.515 -9.809 1.00 68.46 ? 78 TYR A C 1 ATOM 603 O O . TYR A 1 78 ? 27.680 -16.816 -9.508 1.00 70.25 ? 78 TYR A O 1 ATOM 604 C CB . TYR A 1 78 ? 29.316 -18.236 -12.139 1.00 67.97 ? 78 TYR A CB 1 ATOM 605 C CG . TYR A 1 78 ? 28.888 -16.962 -12.851 1.00 68.11 ? 78 TYR A CG 1 ATOM 606 C CD1 . TYR A 1 78 ? 27.787 -16.942 -13.707 1.00 68.92 ? 78 TYR A CD1 1 ATOM 607 C CD2 . TYR A 1 78 ? 29.602 -15.781 -12.679 1.00 67.99 ? 78 TYR A CD2 1 ATOM 608 C CE1 . TYR A 1 78 ? 27.405 -15.775 -14.357 1.00 70.39 ? 78 TYR A CE1 1 ATOM 609 C CE2 . TYR A 1 78 ? 29.229 -14.614 -13.322 1.00 68.94 ? 78 TYR A CE2 1 ATOM 610 C CZ . TYR A 1 78 ? 28.132 -14.611 -14.157 1.00 70.32 ? 78 TYR A CZ 1 ATOM 611 O OH . TYR A 1 78 ? 27.778 -13.432 -14.780 1.00 71.37 ? 78 TYR A OH 1 ATOM 612 N N . ILE A 1 79 ? 29.831 -17.387 -9.233 1.00 65.15 ? 79 ILE A N 1 ATOM 613 C CA . ILE A 1 79 ? 30.051 -16.438 -8.148 1.00 66.32 ? 79 ILE A CA 1 ATOM 614 C C . ILE A 1 79 ? 31.059 -15.387 -8.583 1.00 65.66 ? 79 ILE A C 1 ATOM 615 O O . ILE A 1 79 ? 32.001 -15.695 -9.318 1.00 64.40 ? 79 ILE A O 1 ATOM 616 C CB . ILE A 1 79 ? 30.546 -17.161 -6.884 1.00 65.80 ? 79 ILE A CB 1 ATOM 617 C CG1 . ILE A 1 79 ? 29.480 -18.147 -6.401 1.00 67.71 ? 79 ILE A CG1 1 ATOM 618 C CG2 . ILE A 1 79 ? 30.882 -16.164 -5.785 1.00 66.53 ? 79 ILE A CG2 1 ATOM 619 C CD1 . ILE A 1 79 ? 29.964 -19.087 -5.321 1.00 68.53 ? 79 ILE A CD1 1 ATOM 620 N N . VAL A 1 80 ? 30.862 -14.148 -8.136 1.00 66.28 ? 80 VAL A N 1 ATOM 621 C CA . VAL A 1 80 ? 31.766 -13.062 -8.510 1.00 67.12 ? 80 VAL A CA 1 ATOM 622 C C . VAL A 1 80 ? 32.336 -12.350 -7.292 1.00 68.00 ? 80 VAL A C 1 ATOM 623 O O . VAL A 1 80 ? 31.610 -11.700 -6.548 1.00 71.39 ? 80 VAL A O 1 ATOM 624 C CB . VAL A 1 80 ? 31.082 -12.028 -9.423 1.00 68.42 ? 80 VAL A CB 1 ATOM 625 C CG1 . VAL A 1 80 ? 32.072 -10.931 -9.806 1.00 67.38 ? 80 VAL A CG1 1 ATOM 626 C CG2 . VAL A 1 80 ? 30.521 -12.711 -10.661 1.00 68.96 ? 80 VAL A CG2 1 ATOM 627 N N . GLU A 1 81 ? 33.650 -12.459 -7.131 1.00 68.00 ? 81 GLU A N 1 ATOM 628 C CA . GLU A 1 81 ? 34.373 -11.887 -6.010 1.00 70.42 ? 81 GLU A CA 1 ATOM 629 C C . GLU A 1 81 ? 35.391 -10.879 -6.532 1.00 71.15 ? 81 GLU A C 1 ATOM 630 O O . GLU A 1 81 ? 36.040 -11.121 -7.545 1.00 72.72 ? 81 GLU A O 1 ATOM 631 C CB . GLU A 1 81 ? 35.093 -13.009 -5.262 1.00 70.50 ? 81 GLU A CB 1 ATOM 632 C CG . GLU A 1 81 ? 35.760 -12.585 -3.968 1.00 72.77 ? 81 GLU A CG 1 ATOM 633 C CD . GLU A 1 81 ? 36.450 -13.737 -3.263 1.00 72.44 ? 81 GLU A CD 1 ATOM 634 O OE1 . GLU A 1 81 ? 37.198 -14.491 -3.929 1.00 70.46 ? 81 GLU A OE1 1 ATOM 635 O OE2 . GLU A 1 81 ? 36.234 -13.889 -2.040 1.00 74.28 ? 81 GLU A OE2 1 ATOM 636 N N . LYS A 1 82 ? 35.537 -9.753 -5.847 1.00 74.71 ? 82 LYS A N 1 ATOM 637 C CA . LYS A 1 82 ? 36.568 -8.779 -6.204 1.00 76.61 ? 82 LYS A CA 1 ATOM 638 C C . LYS A 1 82 ? 37.961 -9.302 -5.847 1.00 75.01 ? 82 LYS A C 1 ATOM 639 O O . LYS A 1 82 ? 38.104 -10.247 -5.070 1.00 72.73 ? 82 LYS A O 1 ATOM 640 C CB . LYS A 1 82 ? 36.313 -7.433 -5.515 1.00 80.75 ? 82 LYS A CB 1 ATOM 641 C CG . LYS A 1 82 ? 35.152 -6.646 -6.101 1.00 84.45 ? 82 LYS A CG 1 ATOM 642 C CD . LYS A 1 82 ? 35.014 -5.279 -5.444 1.00 89.32 ? 82 LYS A CD 1 ATOM 643 C CE . LYS A 1 82 ? 34.203 -4.313 -6.298 1.00 94.12 ? 82 LYS A CE 1 ATOM 644 N NZ . LYS A 1 82 ? 32.822 -4.798 -6.579 1.00 96.06 ? 82 LYS A NZ 1 ATOM 645 N N . ALA A 1 83 ? 38.985 -8.686 -6.429 1.00 76.87 ? 83 ALA A N 1 ATOM 646 C CA . ALA A 1 83 ? 40.372 -9.078 -6.168 1.00 77.62 ? 83 ALA A CA 1 ATOM 647 C C . ALA A 1 83 ? 40.773 -8.847 -4.709 1.00 82.04 ? 83 ALA A C 1 ATOM 648 O O . ALA A 1 83 ? 41.511 -9.651 -4.133 1.00 84.19 ? 83 ALA A O 1 ATOM 649 C CB . ALA A 1 83 ? 41.320 -8.336 -7.099 1.00 76.58 ? 83 ALA A CB 1 ATOM 650 N N . ASN A 1 84 ? 40.286 -7.755 -4.118 1.00 84.60 ? 84 ASN A N 1 ATOM 651 C CA . ASN A 1 84 ? 40.600 -7.424 -2.731 1.00 86.41 ? 84 ASN A CA 1 ATOM 652 C C . ASN A 1 84 ? 39.385 -6.883 -1.969 1.00 86.72 ? 84 ASN A C 1 ATOM 653 O O . ASN A 1 84 ? 39.335 -5.693 -1.645 1.00 86.72 ? 84 ASN A O 1 ATOM 654 C CB . ASN A 1 84 ? 41.754 -6.416 -2.691 1.00 90.47 ? 84 ASN A CB 1 ATOM 655 C CG . ASN A 1 84 ? 43.045 -6.986 -3.262 1.00 91.78 ? 84 ASN A CG 1 ATOM 656 O OD1 . ASN A 1 84 ? 43.612 -7.933 -2.714 1.00 92.29 ? 84 ASN A OD1 1 ATOM 657 N ND2 . ASN A 1 84 ? 43.513 -6.415 -4.370 1.00 93.23 ? 84 ASN A ND2 1 ATOM 658 N N . PRO A 1 85 ? 38.404 -7.761 -1.667 1.00 84.84 ? 85 PRO A N 1 ATOM 659 C CA . PRO A 1 85 ? 37.184 -7.316 -0.977 1.00 85.97 ? 85 PRO A CA 1 ATOM 660 C C . PRO A 1 85 ? 37.494 -6.742 0.401 1.00 86.65 ? 85 PRO A C 1 ATOM 661 O O . PRO A 1 85 ? 38.318 -7.307 1.119 1.00 88.21 ? 85 PRO A O 1 ATOM 662 C CB . PRO A 1 85 ? 36.345 -8.602 -0.854 1.00 83.90 ? 85 PRO A CB 1 ATOM 663 C CG . PRO A 1 85 ? 36.967 -9.587 -1.791 1.00 81.48 ? 85 PRO A CG 1 ATOM 664 C CD . PRO A 1 85 ? 38.417 -9.221 -1.864 1.00 80.91 ? 85 PRO A CD 1 ATOM 665 N N . VAL A 1 86 ? 36.850 -5.633 0.763 1.00 86.84 ? 86 VAL A N 1 ATOM 666 C CA . VAL A 1 86 ? 37.119 -4.984 2.053 1.00 88.75 ? 86 VAL A CA 1 ATOM 667 C C . VAL A 1 86 ? 36.475 -5.703 3.247 1.00 87.96 ? 86 VAL A C 1 ATOM 668 O O . VAL A 1 86 ? 37.029 -5.684 4.347 1.00 87.52 ? 86 VAL A O 1 ATOM 669 C CB . VAL A 1 86 ? 36.704 -3.488 2.064 1.00 92.56 ? 86 VAL A CB 1 ATOM 670 C CG1 . VAL A 1 86 ? 37.371 -2.744 0.915 1.00 92.78 ? 86 VAL A CG1 1 ATOM 671 C CG2 . VAL A 1 86 ? 35.188 -3.322 2.018 1.00 93.83 ? 86 VAL A CG2 1 ATOM 672 N N . ASN A 1 87 ? 35.317 -6.329 3.029 1.00 86.24 ? 87 ASN A N 1 ATOM 673 C CA . ASN A 1 87 ? 34.603 -7.053 4.082 1.00 85.43 ? 87 ASN A CA 1 ATOM 674 C C . ASN A 1 87 ? 34.957 -8.537 4.093 1.00 84.93 ? 87 ASN A C 1 ATOM 675 O O . ASN A 1 87 ? 34.176 -9.383 3.643 1.00 85.81 ? 87 ASN A O 1 ATOM 676 C CB . ASN A 1 87 ? 33.092 -6.896 3.915 1.00 87.19 ? 87 ASN A CB 1 ATOM 677 C CG . ASN A 1 87 ? 32.632 -5.461 4.042 1.00 90.43 ? 87 ASN A CG 1 ATOM 678 O OD1 . ASN A 1 87 ? 33.154 -4.695 4.852 1.00 93.80 ? 87 ASN A OD1 1 ATOM 679 N ND2 . ASN A 1 87 ? 31.635 -5.091 3.249 1.00 92.40 ? 87 ASN A ND2 1 ATOM 680 N N . ASP A 1 88 ? 36.142 -8.844 4.609 1.00 83.99 ? 88 ASP A N 1 ATOM 681 C CA . ASP A 1 88 ? 36.605 -10.219 4.743 1.00 81.12 ? 88 ASP A CA 1 ATOM 682 C C . ASP A 1 88 ? 36.422 -10.613 6.219 1.00 81.62 ? 88 ASP A C 1 ATOM 683 O O . ASP A 1 88 ? 35.294 -10.604 6.723 1.00 81.49 ? 88 ASP A O 1 ATOM 684 C CB . ASP A 1 88 ? 38.061 -10.328 4.243 1.00 80.13 ? 88 ASP A CB 1 ATOM 685 C CG . ASP A 1 88 ? 38.537 -11.775 4.074 1.00 80.11 ? 88 ASP A CG 1 ATOM 686 O OD1 . ASP A 1 88 ? 37.704 -12.706 4.060 1.00 79.88 ? 88 ASP A OD1 1 ATOM 687 O OD2 . ASP A 1 88 ? 39.762 -11.984 3.947 1.00 81.89 ? 88 ASP A OD2 1 ATOM 688 N N . LEU A 1 89 ? 37.508 -10.939 6.914 1.00 79.84 ? 89 LEU A N 1 ATOM 689 C CA . LEU A 1 89 ? 37.447 -11.205 8.339 1.00 79.81 ? 89 LEU A CA 1 ATOM 690 C C . LEU A 1 89 ? 37.528 -9.873 9.087 1.00 80.75 ? 89 LEU A C 1 ATOM 691 O O . LEU A 1 89 ? 38.604 -9.278 9.191 1.00 79.53 ? 89 LEU A O 1 ATOM 692 C CB . LEU A 1 89 ? 38.591 -12.134 8.751 1.00 78.81 ? 89 LEU A CB 1 ATOM 693 C CG . LEU A 1 89 ? 38.651 -13.483 8.024 1.00 76.70 ? 89 LEU A CG 1 ATOM 694 C CD1 . LEU A 1 89 ? 39.901 -14.246 8.434 1.00 76.39 ? 89 LEU A CD1 1 ATOM 695 C CD2 . LEU A 1 89 ? 37.403 -14.318 8.279 1.00 75.87 ? 89 LEU A CD2 1 ATOM 696 N N . CYS A 1 90 ? 36.383 -9.408 9.591 1.00 82.21 ? 90 CYS A N 1 ATOM 697 C CA . CYS A 1 90 ? 36.309 -8.132 10.300 1.00 83.99 ? 90 CYS A CA 1 ATOM 698 C C . CYS A 1 90 ? 37.162 -8.172 11.569 1.00 83.31 ? 90 CYS A C 1 ATOM 699 O O . CYS A 1 90 ? 37.974 -7.278 11.802 1.00 85.27 ? 90 CYS A O 1 ATOM 700 C CB . CYS A 1 90 ? 34.853 -7.747 10.611 1.00 87.81 ? 90 CYS A CB 1 ATOM 701 S SG . CYS A 1 90 ? 33.830 -8.998 11.438 1.00 90.05 ? 90 CYS A SG 1 ATOM 702 N N . TYR A 1 91 ? 36.976 -9.214 12.374 1.00 81.01 ? 91 TYR A N 1 ATOM 703 C CA . TYR A 1 91 ? 37.897 -9.528 13.455 1.00 80.13 ? 91 TYR A CA 1 ATOM 704 C C . TYR A 1 91 ? 39.062 -10.297 12.837 1.00 77.74 ? 91 TYR A C 1 ATOM 705 O O . TYR A 1 91 ? 38.838 -11.305 12.165 1.00 76.38 ? 91 TYR A O 1 ATOM 706 C CB . TYR A 1 91 ? 37.205 -10.384 14.521 1.00 81.19 ? 91 TYR A CB 1 ATOM 707 C CG . TYR A 1 91 ? 37.914 -10.382 15.856 1.00 82.46 ? 91 TYR A CG 1 ATOM 708 C CD1 . TYR A 1 91 ? 39.083 -11.112 16.046 1.00 81.13 ? 91 TYR A CD1 1 ATOM 709 C CD2 . TYR A 1 91 ? 37.424 -9.637 16.930 1.00 83.99 ? 91 TYR A CD2 1 ATOM 710 C CE1 . TYR A 1 91 ? 39.741 -11.105 17.265 1.00 81.90 ? 91 TYR A CE1 1 ATOM 711 C CE2 . TYR A 1 91 ? 38.074 -9.630 18.154 1.00 83.52 ? 91 TYR A CE2 1 ATOM 712 C CZ . TYR A 1 91 ? 39.233 -10.362 18.316 1.00 82.29 ? 91 TYR A CZ 1 ATOM 713 O OH . TYR A 1 91 ? 39.887 -10.360 19.527 1.00 82.43 ? 91 TYR A OH 1 ATOM 714 N N . PRO A 1 92 ? 40.310 -9.839 13.060 1.00 77.91 ? 92 PRO A N 1 ATOM 715 C CA . PRO A 1 92 ? 41.454 -10.440 12.364 1.00 75.63 ? 92 PRO A CA 1 ATOM 716 C C . PRO A 1 92 ? 41.694 -11.897 12.731 1.00 76.22 ? 92 PRO A C 1 ATOM 717 O O . PRO A 1 92 ? 41.357 -12.328 13.839 1.00 77.64 ? 92 PRO A O 1 ATOM 718 C CB . PRO A 1 92 ? 42.636 -9.592 12.836 1.00 76.14 ? 92 PRO A CB 1 ATOM 719 C CG . PRO A 1 92 ? 42.224 -9.125 14.189 1.00 78.79 ? 92 PRO A CG 1 ATOM 720 C CD . PRO A 1 92 ? 40.749 -8.853 14.064 1.00 79.84 ? 92 PRO A CD 1 ATOM 721 N N . GLY A 1 93 ? 42.275 -12.643 11.797 1.00 76.45 ? 93 GLY A N 1 ATOM 722 C CA . GLY A 1 93 ? 42.623 -14.035 12.033 1.00 75.34 ? 93 GLY A CA 1 ATOM 723 C C . GLY A 1 93 ? 42.877 -14.810 10.756 1.00 75.14 ? 93 GLY A C 1 ATOM 724 O O . GLY A 1 93 ? 43.491 -14.302 9.817 1.00 72.00 ? 93 GLY A O 1 ATOM 725 N N . ASP A 1 94 ? 42.405 -16.052 10.739 1.00 76.43 ? 94 ASP A N 1 ATOM 726 C CA . ASP A 1 94 ? 42.608 -16.951 9.618 1.00 76.31 ? 94 ASP A CA 1 ATOM 727 C C . ASP A 1 94 ? 41.375 -17.784 9.384 1.00 74.73 ? 94 ASP A C 1 ATOM 728 O O . ASP A 1 94 ? 40.576 -18.011 10.297 1.00 74.76 ? 94 ASP A O 1 ATOM 729 C CB . ASP A 1 94 ? 43.787 -17.885 9.884 1.00 78.22 ? 94 ASP A CB 1 ATOM 730 C CG . ASP A 1 94 ? 45.117 -17.209 9.672 1.00 81.16 ? 94 ASP A CG 1 ATOM 731 O OD1 . ASP A 1 94 ? 45.557 -17.122 8.506 1.00 83.00 ? 94 ASP A OD1 1 ATOM 732 O OD2 . ASP A 1 94 ? 45.721 -16.763 10.669 1.00 84.02 ? 94 ASP A OD2 1 ATOM 733 N N . PHE A 1 95 ? 41.236 -18.226 8.139 1.00 72.07 ? 95 PHE A N 1 ATOM 734 C CA . PHE A 1 95 ? 40.234 -19.192 7.757 1.00 69.06 ? 95 PHE A CA 1 ATOM 735 C C . PHE A 1 95 ? 41.015 -20.411 7.288 1.00 68.06 ? 95 PHE A C 1 ATOM 736 O O . PHE A 1 95 ? 41.672 -20.379 6.250 1.00 66.88 ? 95 PHE A O 1 ATOM 737 C CB . PHE A 1 95 ? 39.369 -18.621 6.647 1.00 68.60 ? 95 PHE A CB 1 ATOM 738 C CG . PHE A 1 95 ? 38.052 -19.309 6.489 1.00 68.91 ? 95 PHE A CG 1 ATOM 739 C CD1 . PHE A 1 95 ? 37.988 -20.622 6.058 1.00 69.58 ? 95 PHE A CD1 1 ATOM 740 C CD2 . PHE A 1 95 ? 36.871 -18.637 6.760 1.00 70.02 ? 95 PHE A CD2 1 ATOM 741 C CE1 . PHE A 1 95 ? 36.767 -21.255 5.902 1.00 71.68 ? 95 PHE A CE1 1 ATOM 742 C CE2 . PHE A 1 95 ? 35.650 -19.263 6.606 1.00 71.36 ? 95 PHE A CE2 1 ATOM 743 C CZ . PHE A 1 95 ? 35.597 -20.575 6.179 1.00 71.74 ? 95 PHE A CZ 1 ATOM 744 N N . ASN A 1 96 ? 40.967 -21.473 8.078 1.00 68.24 ? 96 ASN A N 1 ATOM 745 C CA . ASN A 1 96 ? 41.736 -22.680 7.799 1.00 67.49 ? 96 ASN A CA 1 ATOM 746 C C . ASN A 1 96 ? 41.237 -23.421 6.555 1.00 65.38 ? 96 ASN A C 1 ATOM 747 O O . ASN A 1 96 ? 40.026 -23.564 6.349 1.00 64.44 ? 96 ASN A O 1 ATOM 748 C CB . ASN A 1 96 ? 41.684 -23.606 9.015 1.00 70.92 ? 96 ASN A CB 1 ATOM 749 C CG . ASN A 1 96 ? 42.745 -24.679 8.973 1.00 72.22 ? 96 ASN A CG 1 ATOM 750 O OD1 . ASN A 1 96 ? 43.935 -24.399 9.150 1.00 73.48 ? 96 ASN A OD1 1 ATOM 751 N ND2 . ASN A 1 96 ? 42.323 -25.918 8.741 1.00 72.52 ? 96 ASN A ND2 1 ATOM 752 N N . ASP A 1 97 ? 42.184 -23.899 5.745 1.00 64.60 ? 97 ASP A N 1 ATOM 753 C CA . ASP A 1 97 ? 41.907 -24.569 4.464 1.00 63.35 ? 97 ASP A CA 1 ATOM 754 C C . ASP A 1 97 ? 40.891 -23.798 3.613 1.00 60.35 ? 97 ASP A C 1 ATOM 755 O O . ASP A 1 97 ? 39.967 -24.376 3.028 1.00 57.93 ? 97 ASP A O 1 ATOM 756 C CB . ASP A 1 97 ? 41.456 -26.022 4.691 1.00 67.58 ? 97 ASP A CB 1 ATOM 757 C CG . ASP A 1 97 ? 42.615 -26.956 5.008 1.00 70.10 ? 97 ASP A CG 1 ATOM 758 O OD1 . ASP A 1 97 ? 43.734 -26.707 4.521 1.00 71.30 ? 97 ASP A OD1 1 ATOM 759 O OD2 . ASP A 1 97 ? 42.403 -27.951 5.735 1.00 75.42 ? 97 ASP A OD2 1 ATOM 760 N N . TYR A 1 98 ? 41.089 -22.487 3.542 1.00 58.07 ? 98 TYR A N 1 ATOM 761 C CA . TYR A 1 98 ? 40.166 -21.594 2.846 1.00 59.07 ? 98 TYR A CA 1 ATOM 762 C C . TYR A 1 98 ? 40.105 -21.889 1.351 1.00 58.52 ? 98 TYR A C 1 ATOM 763 O O . TYR A 1 98 ? 39.025 -21.923 0.754 1.00 58.49 ? 98 TYR A O 1 ATOM 764 C CB . TYR A 1 98 ? 40.613 -20.149 3.067 1.00 58.67 ? 98 TYR A CB 1 ATOM 765 C CG . TYR A 1 98 ? 39.674 -19.076 2.563 1.00 58.75 ? 98 TYR A CG 1 ATOM 766 C CD1 . TYR A 1 98 ? 38.314 -19.122 2.841 1.00 60.27 ? 98 TYR A CD1 1 ATOM 767 C CD2 . TYR A 1 98 ? 40.162 -17.980 1.852 1.00 57.99 ? 98 TYR A CD2 1 ATOM 768 C CE1 . TYR A 1 98 ? 37.461 -18.125 2.402 1.00 61.48 ? 98 TYR A CE1 1 ATOM 769 C CE2 . TYR A 1 98 ? 39.321 -16.976 1.414 1.00 58.48 ? 98 TYR A CE2 1 ATOM 770 C CZ . TYR A 1 98 ? 37.971 -17.052 1.690 1.00 61.50 ? 98 TYR A CZ 1 ATOM 771 O OH . TYR A 1 98 ? 37.120 -16.059 1.263 1.00 64.60 ? 98 TYR A OH 1 ATOM 772 N N . GLU A 1 99 ? 41.273 -22.109 0.755 1.00 57.33 ? 99 GLU A N 1 ATOM 773 C CA . GLU A 1 99 ? 41.362 -22.317 -0.684 1.00 57.88 ? 99 GLU A CA 1 ATOM 774 C C . GLU A 1 99 ? 40.688 -23.633 -1.072 1.00 57.00 ? 99 GLU A C 1 ATOM 775 O O . GLU A 1 99 ? 39.983 -23.694 -2.078 1.00 56.06 ? 99 GLU A O 1 ATOM 776 C CB . GLU A 1 99 ? 42.818 -22.273 -1.166 1.00 58.07 ? 99 GLU A CB 1 ATOM 777 C CG . GLU A 1 99 ? 43.461 -20.884 -1.113 1.00 59.41 ? 99 GLU A CG 1 ATOM 778 C CD . GLU A 1 99 ? 43.732 -20.384 0.308 1.00 64.06 ? 99 GLU A CD 1 ATOM 779 O OE1 . GLU A 1 99 ? 44.101 -21.198 1.191 1.00 64.86 ? 99 GLU A OE1 1 ATOM 780 O OE2 . GLU A 1 99 ? 43.570 -19.168 0.547 1.00 66.04 ? 99 GLU A OE2 1 ATOM 781 N N . GLU A 1 100 ? 40.880 -24.672 -0.259 1.00 56.41 ? 100 GLU A N 1 ATOM 782 C CA . GLU A 1 100 ? 40.213 -25.952 -0.496 1.00 56.93 ? 100 GLU A CA 1 ATOM 783 C C . GLU A 1 100 ? 38.691 -25.825 -0.374 1.00 57.81 ? 100 GLU A C 1 ATOM 784 O O . GLU A 1 100 ? 37.958 -26.556 -1.036 1.00 60.65 ? 100 GLU A O 1 ATOM 785 C CB . GLU A 1 100 ? 40.745 -27.044 0.439 1.00 56.69 ? 100 GLU A CB 1 ATOM 786 C CG . GLU A 1 100 ? 42.095 -27.617 0.018 1.00 56.65 ? 100 GLU A CG 1 ATOM 787 C CD . GLU A 1 100 ? 41.993 -28.600 -1.140 1.00 58.74 ? 100 GLU A CD 1 ATOM 788 O OE1 . GLU A 1 100 ? 41.118 -29.499 -1.100 1.00 60.25 ? 100 GLU A OE1 1 ATOM 789 O OE2 . GLU A 1 100 ? 42.786 -28.479 -2.100 1.00 57.25 ? 100 GLU A OE2 1 ATOM 790 N N . LEU A 1 101 ? 38.215 -24.896 0.447 1.00 57.60 ? 101 LEU A N 1 ATOM 791 C CA . LEU A 1 101 ? 36.774 -24.674 0.574 1.00 59.24 ? 101 LEU A CA 1 ATOM 792 C C . LEU A 1 101 ? 36.219 -23.957 -0.652 1.00 58.34 ? 101 LEU A C 1 ATOM 793 O O . LEU A 1 101 ? 35.182 -24.352 -1.194 1.00 56.32 ? 101 LEU A O 1 ATOM 794 C CB . LEU A 1 101 ? 36.442 -23.875 1.837 1.00 60.22 ? 101 LEU A CB 1 ATOM 795 C CG . LEU A 1 101 ? 34.965 -23.519 2.009 1.00 61.67 ? 101 LEU A CG 1 ATOM 796 C CD1 . LEU A 1 101 ? 34.110 -24.774 2.108 1.00 62.52 ? 101 LEU A CD1 1 ATOM 797 C CD2 . LEU A 1 101 ? 34.794 -22.636 3.228 1.00 63.93 ? 101 LEU A CD2 1 ATOM 798 N N . LYS A 1 102 ? 36.902 -22.899 -1.078 1.00 58.89 ? 102 LYS A N 1 ATOM 799 C CA . LYS A 1 102 ? 36.510 -22.183 -2.295 1.00 60.39 ? 102 LYS A CA 1 ATOM 800 C C . LYS A 1 102 ? 36.477 -23.120 -3.500 1.00 59.08 ? 102 LYS A C 1 ATOM 801 O O . LYS A 1 102 ? 35.615 -22.990 -4.366 1.00 59.26 ? 102 LYS A O 1 ATOM 802 C CB . LYS A 1 102 ? 37.442 -21.007 -2.570 1.00 61.26 ? 102 LYS A CB 1 ATOM 803 C CG . LYS A 1 102 ? 37.351 -19.907 -1.530 1.00 65.18 ? 102 LYS A CG 1 ATOM 804 C CD . LYS A 1 102 ? 38.444 -18.865 -1.710 1.00 67.23 ? 102 LYS A CD 1 ATOM 805 C CE . LYS A 1 102 ? 38.029 -17.760 -2.667 1.00 70.25 ? 102 LYS A CE 1 ATOM 806 N NZ . LYS A 1 102 ? 38.889 -16.556 -2.494 1.00 72.38 ? 102 LYS A NZ 1 ATOM 807 N N . HIS A 1 103 ? 37.408 -24.069 -3.551 1.00 58.90 ? 103 HIS A N 1 ATOM 808 C CA . HIS A 1 103 ? 37.384 -25.085 -4.596 1.00 59.24 ? 103 HIS A CA 1 ATOM 809 C C . HIS A 1 103 ? 36.120 -25.935 -4.501 1.00 60.96 ? 103 HIS A C 1 ATOM 810 O O . HIS A 1 103 ? 35.530 -26.294 -5.515 1.00 61.99 ? 103 HIS A O 1 ATOM 811 C CB . HIS A 1 103 ? 38.612 -25.992 -4.520 1.00 58.87 ? 103 HIS A CB 1 ATOM 812 C CG . HIS A 1 103 ? 38.650 -27.027 -5.600 1.00 58.60 ? 103 HIS A CG 1 ATOM 813 N ND1 . HIS A 1 103 ? 39.202 -26.786 -6.839 1.00 57.19 ? 103 HIS A ND1 1 ATOM 814 C CD2 . HIS A 1 103 ? 38.170 -28.291 -5.641 1.00 59.71 ? 103 HIS A CD2 1 ATOM 815 C CE1 . HIS A 1 103 ? 39.078 -27.864 -7.591 1.00 56.61 ? 103 HIS A CE1 1 ATOM 816 N NE2 . HIS A 1 103 ? 38.453 -28.790 -6.890 1.00 58.24 ? 103 HIS A NE2 1 ATOM 817 N N . LEU A 1 104 ? 35.720 -26.257 -3.277 1.00 63.40 ? 104 LEU A N 1 ATOM 818 C CA . LEU A 1 104 ? 34.503 -27.024 -3.032 1.00 66.79 ? 104 LEU A CA 1 ATOM 819 C C . LEU A 1 104 ? 33.280 -26.296 -3.590 1.00 69.37 ? 104 LEU A C 1 ATOM 820 O O . LEU A 1 104 ? 32.360 -26.928 -4.108 1.00 69.79 ? 104 LEU A O 1 ATOM 821 C CB . LEU A 1 104 ? 34.327 -27.264 -1.529 1.00 69.62 ? 104 LEU A CB 1 ATOM 822 C CG . LEU A 1 104 ? 33.836 -28.647 -1.108 1.00 71.89 ? 104 LEU A CG 1 ATOM 823 C CD1 . LEU A 1 104 ? 34.823 -29.727 -1.531 1.00 71.81 ? 104 LEU A CD1 1 ATOM 824 C CD2 . LEU A 1 104 ? 33.625 -28.677 0.393 1.00 72.88 ? 104 LEU A CD2 1 ATOM 825 N N . LEU A 1 105 ? 33.296 -24.966 -3.485 1.00 71.81 ? 105 LEU A N 1 ATOM 826 C CA . LEU A 1 105 ? 32.208 -24.100 -3.974 1.00 73.49 ? 105 LEU A CA 1 ATOM 827 C C . LEU A 1 105 ? 32.044 -24.068 -5.484 1.00 73.39 ? 105 LEU A C 1 ATOM 828 O O . LEU A 1 105 ? 30.999 -23.648 -5.982 1.00 78.57 ? 105 LEU A O 1 ATOM 829 C CB . LEU A 1 105 ? 32.421 -22.655 -3.519 1.00 72.69 ? 105 LEU A CB 1 ATOM 830 C CG . LEU A 1 105 ? 31.938 -22.257 -2.141 1.00 73.27 ? 105 LEU A CG 1 ATOM 831 C CD1 . LEU A 1 105 ? 32.231 -20.779 -1.945 1.00 74.36 ? 105 LEU A CD1 1 ATOM 832 C CD2 . LEU A 1 105 ? 30.454 -22.541 -1.989 1.00 76.69 ? 105 LEU A CD2 1 ATOM 833 N N . SER A 1 106 ? 33.075 -24.470 -6.214 1.00 77.93 ? 106 SER A N 1 ATOM 834 C CA A SER A 1 106 ? 33.013 -24.532 -7.674 0.50 79.15 ? 106 SER A CA 1 ATOM 835 C CA B SER A 1 106 ? 32.991 -24.510 -7.665 0.50 79.10 ? 106 SER A CA 1 ATOM 836 C C . SER A 1 106 ? 32.096 -25.662 -8.132 1.00 80.45 ? 106 SER A C 1 ATOM 837 O O . SER A 1 106 ? 31.708 -25.717 -9.297 1.00 83.77 ? 106 SER A O 1 ATOM 838 C CB A SER A 1 106 ? 34.411 -24.727 -8.276 0.50 78.14 ? 106 SER A CB 1 ATOM 839 C CB B SER A 1 106 ? 34.392 -24.615 -8.260 0.50 78.01 ? 106 SER A CB 1 ATOM 840 O OG A SER A 1 106 ? 34.843 -26.077 -8.178 0.50 77.39 ? 106 SER A OG 1 ATOM 841 O OG B SER A 1 106 ? 35.221 -23.601 -7.711 0.50 76.09 ? 106 SER A OG 1 ATOM 842 N N . ARG A 1 107 ? 31.770 -26.570 -7.212 1.00 82.37 ? 107 ARG A N 1 ATOM 843 C CA . ARG A 1 107 ? 30.856 -27.680 -7.473 1.00 87.23 ? 107 ARG A CA 1 ATOM 844 C C . ARG A 1 107 ? 29.521 -27.491 -6.737 1.00 84.51 ? 107 ARG A C 1 ATOM 845 O O . ARG A 1 107 ? 28.784 -28.458 -6.533 1.00 84.31 ? 107 ARG A O 1 ATOM 846 C CB . ARG A 1 107 ? 31.493 -29.003 -7.031 1.00 94.07 ? 107 ARG A CB 1 ATOM 847 C CG . ARG A 1 107 ? 32.812 -29.343 -7.713 1.00 101.51 ? 107 ARG A CG 1 ATOM 848 C CD . ARG A 1 107 ? 33.694 -30.189 -6.800 1.00 108.99 ? 107 ARG A CD 1 ATOM 849 N NE . ARG A 1 107 ? 34.893 -30.703 -7.472 1.00 116.19 ? 107 ARG A NE 1 ATOM 850 C CZ . ARG A 1 107 ? 35.868 -31.389 -6.868 1.00 118.96 ? 107 ARG A CZ 1 ATOM 851 N NH1 . ARG A 1 107 ? 35.809 -31.652 -5.561 1.00 120.47 ? 107 ARG A NH1 1 ATOM 852 N NH2 . ARG A 1 107 ? 36.914 -31.814 -7.572 1.00 114.71 ? 107 ARG A NH2 1 ATOM 853 N N . ILE A 1 108 ? 29.218 -26.257 -6.333 1.00 80.67 ? 108 ILE A N 1 ATOM 854 C CA . ILE A 1 108 ? 27.986 -25.961 -5.595 1.00 80.84 ? 108 ILE A CA 1 ATOM 855 C C . ILE A 1 108 ? 27.243 -24.766 -6.203 1.00 80.72 ? 108 ILE A C 1 ATOM 856 O O . ILE A 1 108 ? 27.847 -23.730 -6.489 1.00 79.50 ? 108 ILE A O 1 ATOM 857 C CB . ILE A 1 108 ? 28.269 -25.677 -4.098 1.00 79.56 ? 108 ILE A CB 1 ATOM 858 C CG1 . ILE A 1 108 ? 28.957 -26.877 -3.437 1.00 78.12 ? 108 ILE A CG1 1 ATOM 859 C CG2 . ILE A 1 108 ? 26.975 -25.358 -3.363 1.00 79.86 ? 108 ILE A CG2 1 ATOM 860 C CD1 . ILE A 1 108 ? 29.475 -26.603 -2.041 1.00 76.49 ? 108 ILE A CD1 1 ATOM 861 N N . ASN A 1 109 ? 25.931 -24.922 -6.385 1.00 81.74 ? 109 ASN A N 1 ATOM 862 C CA . ASN A 1 109 ? 25.065 -23.864 -6.913 1.00 83.01 ? 109 ASN A CA 1 ATOM 863 C C . ASN A 1 109 ? 24.087 -23.285 -5.893 1.00 83.82 ? 109 ASN A C 1 ATOM 864 O O . ASN A 1 109 ? 23.535 -22.206 -6.122 1.00 82.75 ? 109 ASN A O 1 ATOM 865 C CB . ASN A 1 109 ? 24.251 -24.391 -8.095 1.00 85.44 ? 109 ASN A CB 1 ATOM 866 C CG . ASN A 1 109 ? 25.116 -24.765 -9.278 1.00 85.40 ? 109 ASN A CG 1 ATOM 867 O OD1 . ASN A 1 109 ? 25.964 -23.984 -9.714 1.00 83.51 ? 109 ASN A OD1 1 ATOM 868 N ND2 . ASN A 1 109 ? 24.902 -25.963 -9.813 1.00 87.65 ? 109 ASN A ND2 1 ATOM 869 N N . HIS A 1 110 ? 23.846 -23.999 -4.792 1.00 83.54 ? 110 HIS A N 1 ATOM 870 C CA . HIS A 1 110 ? 22.866 -23.549 -3.809 1.00 84.16 ? 110 HIS A CA 1 ATOM 871 C C . HIS A 1 110 ? 23.094 -24.094 -2.401 1.00 83.33 ? 110 HIS A C 1 ATOM 872 O O . HIS A 1 110 ? 23.231 -25.304 -2.202 1.00 82.71 ? 110 HIS A O 1 ATOM 873 C CB . HIS A 1 110 ? 21.461 -23.924 -4.277 1.00 87.45 ? 110 HIS A CB 1 ATOM 874 C CG . HIS A 1 110 ? 20.365 -23.231 -3.527 1.00 89.96 ? 110 HIS A CG 1 ATOM 875 N ND1 . HIS A 1 110 ? 19.091 -23.748 -3.429 1.00 92.23 ? 110 HIS A ND1 1 ATOM 876 C CD2 . HIS A 1 110 ? 20.354 -22.066 -2.836 1.00 89.14 ? 110 HIS A CD2 1 ATOM 877 C CE1 . HIS A 1 110 ? 18.342 -22.930 -2.712 1.00 93.90 ? 110 HIS A CE1 1 ATOM 878 N NE2 . HIS A 1 110 ? 19.085 -21.902 -2.340 1.00 91.78 ? 110 HIS A NE2 1 ATOM 879 N N . PHE A 1 111 ? 23.120 -23.177 -1.436 1.00 83.00 ? 111 PHE A N 1 ATOM 880 C CA . PHE A 1 111 ? 23.123 -23.517 -0.017 1.00 83.36 ? 111 PHE A CA 1 ATOM 881 C C . PHE A 1 111 ? 21.748 -23.226 0.583 1.00 87.02 ? 111 PHE A C 1 ATOM 882 O O . PHE A 1 111 ? 21.056 -22.314 0.136 1.00 88.59 ? 111 PHE A O 1 ATOM 883 C CB . PHE A 1 111 ? 24.142 -22.669 0.754 1.00 80.25 ? 111 PHE A CB 1 ATOM 884 C CG . PHE A 1 111 ? 25.578 -23.103 0.604 1.00 77.75 ? 111 PHE A CG 1 ATOM 885 C CD1 . PHE A 1 111 ? 25.953 -24.442 0.695 1.00 77.48 ? 111 PHE A CD1 1 ATOM 886 C CD2 . PHE A 1 111 ? 26.573 -22.152 0.439 1.00 75.13 ? 111 PHE A CD2 1 ATOM 887 C CE1 . PHE A 1 111 ? 27.284 -24.817 0.584 1.00 73.76 ? 111 PHE A CE1 1 ATOM 888 C CE2 . PHE A 1 111 ? 27.898 -22.524 0.332 1.00 72.49 ? 111 PHE A CE2 1 ATOM 889 C CZ . PHE A 1 111 ? 28.255 -23.856 0.405 1.00 71.87 ? 111 PHE A CZ 1 ATOM 890 N N . GLU A 1 112 ? 21.369 -23.989 1.607 1.00 89.05 ? 112 GLU A N 1 ATOM 891 C CA . GLU A 1 112 ? 20.202 -23.664 2.439 1.00 93.20 ? 112 GLU A CA 1 ATOM 892 C C . GLU A 1 112 ? 20.655 -23.540 3.887 1.00 90.86 ? 112 GLU A C 1 ATOM 893 O O . GLU A 1 112 ? 21.034 -24.531 4.510 1.00 89.36 ? 112 GLU A O 1 ATOM 894 C CB . GLU A 1 112 ? 19.118 -24.741 2.318 1.00 96.93 ? 112 GLU A CB 1 ATOM 895 C CG . GLU A 1 112 ? 18.264 -24.641 1.058 1.00 100.27 ? 112 GLU A CG 1 ATOM 896 C CD . GLU A 1 112 ? 17.055 -23.730 1.203 1.00 103.26 ? 112 GLU A CD 1 ATOM 897 O OE1 . GLU A 1 112 ? 16.604 -23.505 2.350 1.00 102.87 ? 112 GLU A OE1 1 ATOM 898 O OE2 . GLU A 1 112 ? 16.548 -23.254 0.157 1.00 104.18 ? 112 GLU A OE2 1 ATOM 899 N N . LYS A 1 113 ? 20.623 -22.322 4.415 1.00 90.24 ? 113 LYS A N 1 ATOM 900 C CA . LYS A 1 113 ? 21.067 -22.073 5.781 1.00 90.56 ? 113 LYS A CA 1 ATOM 901 C C . LYS A 1 113 ? 20.067 -22.619 6.789 1.00 92.47 ? 113 LYS A C 1 ATOM 902 O O . LYS A 1 113 ? 18.871 -22.353 6.681 1.00 96.00 ? 113 LYS A O 1 ATOM 903 C CB . LYS A 1 113 ? 21.266 -20.576 6.010 1.00 91.41 ? 113 LYS A CB 1 ATOM 904 C CG . LYS A 1 113 ? 21.764 -20.225 7.402 1.00 92.20 ? 113 LYS A CG 1 ATOM 905 C CD . LYS A 1 113 ? 22.852 -19.161 7.366 1.00 91.92 ? 113 LYS A CD 1 ATOM 906 C CE . LYS A 1 113 ? 22.340 -17.824 6.859 1.00 92.85 ? 113 LYS A CE 1 ATOM 907 N NZ . LYS A 1 113 ? 23.464 -16.912 6.499 1.00 90.93 ? 113 LYS A NZ 1 ATOM 908 N N . ILE A 1 114 ? 20.559 -23.389 7.757 1.00 91.26 ? 114 ILE A N 1 ATOM 909 C CA . ILE A 1 114 ? 19.723 -23.881 8.850 1.00 93.56 ? 114 ILE A CA 1 ATOM 910 C C . ILE A 1 114 ? 20.427 -23.749 10.191 1.00 93.45 ? 114 ILE A C 1 ATOM 911 O O . ILE A 1 114 ? 21.656 -23.676 10.255 1.00 92.95 ? 114 ILE A O 1 ATOM 912 C CB . ILE A 1 114 ? 19.309 -25.351 8.658 1.00 94.46 ? 114 ILE A CB 1 ATOM 913 C CG1 . ILE A 1 114 ? 20.537 -26.247 8.478 1.00 92.83 ? 114 ILE A CG1 1 ATOM 914 C CG2 . ILE A 1 114 ? 18.367 -25.481 7.470 1.00 96.24 ? 114 ILE A CG2 1 ATOM 915 C CD1 . ILE A 1 114 ? 20.253 -27.701 8.775 1.00 94.48 ? 114 ILE A CD1 1 ATOM 916 N N . GLN A 1 115 ? 19.630 -23.733 11.254 1.00 94.69 ? 115 GLN A N 1 ATOM 917 C CA . GLN A 1 115 ? 20.130 -23.601 12.615 1.00 94.24 ? 115 GLN A CA 1 ATOM 918 C C . GLN A 1 115 ? 20.368 -24.980 13.224 1.00 93.86 ? 115 GLN A C 1 ATOM 919 O O . GLN A 1 115 ? 19.479 -25.834 13.199 1.00 94.06 ? 115 GLN A O 1 ATOM 920 C CB . GLN A 1 115 ? 19.117 -22.834 13.462 1.00 96.54 ? 115 GLN A CB 1 ATOM 921 C CG . GLN A 1 115 ? 19.578 -22.547 14.879 1.00 96.55 ? 115 GLN A CG 1 ATOM 922 C CD . GLN A 1 115 ? 18.516 -21.851 15.700 1.00 98.72 ? 115 GLN A CD 1 ATOM 923 O OE1 . GLN A 1 115 ? 18.693 -20.710 16.124 1.00 98.73 ? 115 GLN A OE1 1 ATOM 924 N NE2 . GLN A 1 115 ? 17.399 -22.535 15.924 1.00 100.12 ? 115 GLN A NE2 1 ATOM 925 N N . ILE A 1 116 ? 21.559 -25.184 13.783 1.00 92.01 ? 116 ILE A N 1 ATOM 926 C CA . ILE A 1 116 ? 21.909 -26.467 14.405 1.00 92.49 ? 116 ILE A CA 1 ATOM 927 C C . ILE A 1 116 ? 22.076 -26.364 15.925 1.00 94.55 ? 116 ILE A C 1 ATOM 928 O O . ILE A 1 116 ? 21.654 -27.264 16.651 1.00 98.04 ? 116 ILE A O 1 ATOM 929 C CB . ILE A 1 116 ? 23.155 -27.116 13.754 1.00 88.85 ? 116 ILE A CB 1 ATOM 930 C CG1 . ILE A 1 116 ? 24.315 -26.120 13.649 1.00 86.61 ? 116 ILE A CG1 1 ATOM 931 C CG2 . ILE A 1 116 ? 22.801 -27.654 12.375 1.00 87.63 ? 116 ILE A CG2 1 ATOM 932 C CD1 . ILE A 1 116 ? 25.640 -26.760 13.299 1.00 84.20 ? 116 ILE A CD1 1 ATOM 933 N N . ILE A 1 117 ? 22.672 -25.274 16.407 1.00 94.99 ? 117 ILE A N 1 ATOM 934 C CA . ILE A 1 117 ? 22.764 -25.013 17.849 1.00 96.49 ? 117 ILE A CA 1 ATOM 935 C C . ILE A 1 117 ? 22.210 -23.619 18.154 1.00 97.21 ? 117 ILE A C 1 ATOM 936 O O . ILE A 1 117 ? 22.918 -22.621 17.976 1.00 93.91 ? 117 ILE A O 1 ATOM 937 C CB . ILE A 1 117 ? 24.211 -25.131 18.375 1.00 95.68 ? 117 ILE A CB 1 ATOM 938 C CG1 . ILE A 1 117 ? 24.846 -26.443 17.890 1.00 94.37 ? 117 ILE A CG1 1 ATOM 939 C CG2 . ILE A 1 117 ? 24.226 -25.042 19.898 1.00 97.45 ? 117 ILE A CG2 1 ATOM 940 C CD1 . ILE A 1 117 ? 26.227 -26.716 18.446 1.00 93.46 ? 117 ILE A CD1 1 ATOM 941 N N . PRO A 1 118 ? 20.941 -23.550 18.615 1.00 100.29 ? 118 PRO A N 1 ATOM 942 C CA . PRO A 1 118 ? 20.272 -22.281 18.923 1.00 102.14 ? 118 PRO A CA 1 ATOM 943 C C . PRO A 1 118 ? 21.068 -21.399 19.876 1.00 102.07 ? 118 PRO A C 1 ATOM 944 O O . PRO A 1 118 ? 21.627 -21.892 20.854 1.00 100.28 ? 118 PRO A O 1 ATOM 945 C CB . PRO A 1 118 ? 18.962 -22.719 19.588 1.00 105.61 ? 118 PRO A CB 1 ATOM 946 C CG . PRO A 1 118 ? 18.704 -24.087 19.070 1.00 105.26 ? 118 PRO A CG 1 ATOM 947 C CD . PRO A 1 118 ? 20.054 -24.706 18.851 1.00 102.56 ? 118 PRO A CD 1 ATOM 948 N N . LYS A 1 119 ? 21.107 -20.103 19.579 1.00 103.35 ? 119 LYS A N 1 ATOM 949 C CA . LYS A 1 119 ? 21.862 -19.140 20.375 1.00 104.98 ? 119 LYS A CA 1 ATOM 950 C C . LYS A 1 119 ? 21.330 -19.056 21.802 1.00 108.68 ? 119 LYS A C 1 ATOM 951 O O . LYS A 1 119 ? 22.089 -18.817 22.743 1.00 109.79 ? 119 LYS A O 1 ATOM 952 C CB . LYS A 1 119 ? 21.798 -17.762 19.718 1.00 105.65 ? 119 LYS A CB 1 ATOM 953 C CG . LYS A 1 119 ? 22.656 -16.699 20.377 1.00 107.18 ? 119 LYS A CG 1 ATOM 954 C CD . LYS A 1 119 ? 22.564 -15.399 19.600 1.00 109.63 ? 119 LYS A CD 1 ATOM 955 C CE . LYS A 1 119 ? 23.519 -14.352 20.144 1.00 111.23 ? 119 LYS A CE 1 ATOM 956 N NZ . LYS A 1 119 ? 23.566 -13.143 19.275 1.00 112.37 ? 119 LYS A NZ 1 ATOM 957 N N . SER A 1 120 ? 20.026 -19.264 21.954 1.00 111.48 ? 120 SER A N 1 ATOM 958 C CA . SER A 1 120 ? 19.365 -19.149 23.247 1.00 115.01 ? 120 SER A CA 1 ATOM 959 C C . SER A 1 120 ? 19.210 -20.509 23.935 1.00 115.02 ? 120 SER A C 1 ATOM 960 O O . SER A 1 120 ? 18.275 -20.710 24.706 1.00 118.18 ? 120 SER A O 1 ATOM 961 C CB . SER A 1 120 ? 17.997 -18.490 23.057 1.00 118.34 ? 120 SER A CB 1 ATOM 962 O OG . SER A 1 120 ? 18.082 -17.421 22.128 1.00 117.67 ? 120 SER A OG 1 ATOM 963 N N . SER A 1 121 ? 20.115 -21.441 23.644 1.00 112.35 ? 121 SER A N 1 ATOM 964 C CA . SER A 1 121 ? 20.148 -22.732 24.333 1.00 112.24 ? 121 SER A CA 1 ATOM 965 C C . SER A 1 121 ? 21.431 -22.898 25.155 1.00 110.43 ? 121 SER A C 1 ATOM 966 O O . SER A 1 121 ? 21.699 -23.984 25.672 1.00 109.65 ? 121 SER A O 1 ATOM 967 C CB . SER A 1 121 ? 20.006 -23.876 23.325 1.00 109.86 ? 121 SER A CB 1 ATOM 968 O OG . SER A 1 121 ? 21.119 -23.932 22.455 1.00 106.17 ? 121 SER A OG 1 ATOM 969 N N . TRP A 1 122 ? 22.210 -21.822 25.278 1.00 108.80 ? 122 TRP A N 1 ATOM 970 C CA . TRP A 1 122 ? 23.438 -21.829 26.069 1.00 107.61 ? 122 TRP A CA 1 ATOM 971 C C . TRP A 1 122 ? 23.147 -21.289 27.466 1.00 111.78 ? 122 TRP A C 1 ATOM 972 O O . TRP A 1 122 ? 23.518 -20.163 27.800 1.00 113.67 ? 122 TRP A O 1 ATOM 973 C CB . TRP A 1 122 ? 24.513 -20.980 25.392 1.00 104.40 ? 122 TRP A CB 1 ATOM 974 C CG . TRP A 1 122 ? 24.996 -21.530 24.084 1.00 101.12 ? 122 TRP A CG 1 ATOM 975 C CD1 . TRP A 1 122 ? 24.733 -21.037 22.837 1.00 99.13 ? 122 TRP A CD1 1 ATOM 976 C CD2 . TRP A 1 122 ? 25.840 -22.670 23.893 1.00 98.63 ? 122 TRP A CD2 1 ATOM 977 N NE1 . TRP A 1 122 ? 25.359 -21.800 21.884 1.00 95.84 ? 122 TRP A NE1 1 ATOM 978 C CE2 . TRP A 1 122 ? 26.046 -22.810 22.503 1.00 95.59 ? 122 TRP A CE2 1 ATOM 979 C CE3 . TRP A 1 122 ? 26.441 -23.589 24.761 1.00 98.55 ? 122 TRP A CE3 1 ATOM 980 C CZ2 . TRP A 1 122 ? 26.827 -23.833 21.961 1.00 93.08 ? 122 TRP A CZ2 1 ATOM 981 C CZ3 . TRP A 1 122 ? 27.219 -24.606 24.222 1.00 96.31 ? 122 TRP A CZ3 1 ATOM 982 C CH2 . TRP A 1 122 ? 27.407 -24.718 22.832 1.00 93.48 ? 122 TRP A CH2 1 ATOM 983 N N . SER A 1 123 ? 22.476 -22.100 28.278 1.00 113.49 ? 123 SER A N 1 ATOM 984 C CA . SER A 1 123 ? 22.014 -21.670 29.597 1.00 116.24 ? 123 SER A CA 1 ATOM 985 C C . SER A 1 123 ? 23.144 -21.543 30.630 1.00 117.63 ? 123 SER A C 1 ATOM 986 O O . SER A 1 123 ? 23.037 -20.749 31.564 1.00 120.59 ? 123 SER A O 1 ATOM 987 C CB . SER A 1 123 ? 20.926 -22.621 30.108 1.00 117.79 ? 123 SER A CB 1 ATOM 988 O OG . SER A 1 123 ? 21.255 -23.972 29.841 1.00 114.74 ? 123 SER A OG 1 ATOM 989 N N . SER A 1 124 ? 24.219 -22.313 30.455 1.00 115.52 ? 124 SER A N 1 ATOM 990 C CA . SER A 1 124 ? 25.359 -22.302 31.388 1.00 115.11 ? 124 SER A CA 1 ATOM 991 C C . SER A 1 124 ? 26.465 -21.306 31.011 1.00 112.37 ? 124 SER A C 1 ATOM 992 O O . SER A 1 124 ? 27.462 -21.190 31.724 1.00 110.98 ? 124 SER A O 1 ATOM 993 C CB . SER A 1 124 ? 25.968 -23.704 31.483 1.00 114.10 ? 124 SER A CB 1 ATOM 994 O OG . SER A 1 124 ? 24.994 -24.659 31.858 1.00 116.08 ? 124 SER A OG 1 ATOM 995 N N . HIS A 1 125 ? 26.298 -20.605 29.891 1.00 111.13 ? 125 HIS A N 1 ATOM 996 C CA . HIS A 1 125 ? 27.303 -19.662 29.401 1.00 109.81 ? 125 HIS A CA 1 ATOM 997 C C . HIS A 1 125 ? 26.636 -18.411 28.863 1.00 112.03 ? 125 HIS A C 1 ATOM 998 O O . HIS A 1 125 ? 25.495 -18.456 28.405 1.00 113.68 ? 125 HIS A O 1 ATOM 999 C CB . HIS A 1 125 ? 28.132 -20.286 28.276 1.00 104.76 ? 125 HIS A CB 1 ATOM 1000 C CG . HIS A 1 125 ? 28.828 -21.553 28.660 1.00 103.20 ? 125 HIS A CG 1 ATOM 1001 N ND1 . HIS A 1 125 ? 28.194 -22.777 28.667 1.00 103.31 ? 125 HIS A ND1 1 ATOM 1002 C CD2 . HIS A 1 125 ? 30.108 -21.789 29.034 1.00 101.80 ? 125 HIS A CD2 1 ATOM 1003 C CE1 . HIS A 1 125 ? 29.051 -23.711 29.039 1.00 102.74 ? 125 HIS A CE1 1 ATOM 1004 N NE2 . HIS A 1 125 ? 30.220 -23.139 29.264 1.00 102.08 ? 125 HIS A NE2 1 ATOM 1005 N N . GLU A 1 126 ? 27.359 -17.296 28.902 1.00 112.99 ? 126 GLU A N 1 ATOM 1006 C CA . GLU A 1 126 ? 26.874 -16.058 28.312 1.00 113.61 ? 126 GLU A CA 1 ATOM 1007 C C . GLU A 1 126 ? 27.063 -16.135 26.801 1.00 110.13 ? 126 GLU A C 1 ATOM 1008 O O . GLU A 1 126 ? 28.174 -16.372 26.320 1.00 108.52 ? 126 GLU A O 1 ATOM 1009 C CB . GLU A 1 126 ? 27.619 -14.857 28.894 1.00 115.94 ? 126 GLU A CB 1 ATOM 1010 C CG . GLU A 1 126 ? 27.096 -13.506 28.430 1.00 118.45 ? 126 GLU A CG 1 ATOM 1011 C CD . GLU A 1 126 ? 25.605 -13.331 28.670 1.00 122.01 ? 126 GLU A CD 1 ATOM 1012 O OE1 . GLU A 1 126 ? 25.178 -13.371 29.850 1.00 122.44 ? 126 GLU A OE1 1 ATOM 1013 O OE2 . GLU A 1 126 ? 24.866 -13.154 27.671 1.00 121.98 ? 126 GLU A OE2 1 ATOM 1014 N N . ALA A 1 127 ? 25.975 -15.943 26.059 1.00 108.78 ? 127 ALA A N 1 ATOM 1015 C CA . ALA A 1 127 ? 25.986 -16.112 24.608 1.00 104.00 ? 127 ALA A CA 1 ATOM 1016 C C . ALA A 1 127 ? 25.487 -14.884 23.848 1.00 103.84 ? 127 ALA A C 1 ATOM 1017 O O . ALA A 1 127 ? 25.209 -14.975 22.654 1.00 102.45 ? 127 ALA A O 1 ATOM 1018 C CB . ALA A 1 127 ? 25.154 -17.329 24.230 1.00 103.16 ? 127 ALA A CB 1 ATOM 1019 N N . SER A 1 128 ? 25.383 -13.743 24.528 1.00 105.78 ? 128 SER A N 1 ATOM 1020 C CA . SER A 1 128 ? 24.914 -12.506 23.896 1.00 105.89 ? 128 SER A CA 1 ATOM 1021 C C . SER A 1 128 ? 25.845 -11.308 24.122 1.00 104.60 ? 128 SER A C 1 ATOM 1022 O O . SER A 1 128 ? 25.475 -10.170 23.829 1.00 105.61 ? 128 SER A O 1 ATOM 1023 C CB . SER A 1 128 ? 23.490 -12.191 24.364 1.00 109.90 ? 128 SER A CB 1 ATOM 1024 O OG . SER A 1 128 ? 22.555 -12.956 23.620 1.00 110.09 ? 128 SER A OG 1 ATOM 1025 N N . LEU A 1 129 ? 27.055 -11.572 24.612 1.00 101.83 ? 129 LEU A N 1 ATOM 1026 C CA . LEU A 1 129 ? 28.073 -10.539 24.787 1.00 101.49 ? 129 LEU A CA 1 ATOM 1027 C C . LEU A 1 129 ? 29.307 -10.812 23.933 1.00 97.89 ? 129 LEU A C 1 ATOM 1028 O O . LEU A 1 129 ? 30.349 -10.184 24.126 1.00 98.21 ? 129 LEU A O 1 ATOM 1029 C CB . LEU A 1 129 ? 28.476 -10.450 26.259 1.00 103.83 ? 129 LEU A CB 1 ATOM 1030 C CG . LEU A 1 129 ? 27.348 -10.135 27.244 1.00 107.37 ? 129 LEU A CG 1 ATOM 1031 C CD1 . LEU A 1 129 ? 27.903 -10.006 28.654 1.00 109.27 ? 129 LEU A CD1 1 ATOM 1032 C CD2 . LEU A 1 129 ? 26.605 -8.868 26.842 1.00 109.48 ? 129 LEU A CD2 1 ATOM 1033 N N . GLY A 1 130 ? 29.179 -11.733 22.976 1.00 95.49 ? 130 GLY A N 1 ATOM 1034 C CA . GLY A 1 130 ? 30.287 -12.136 22.111 1.00 91.48 ? 130 GLY A CA 1 ATOM 1035 C C . GLY A 1 130 ? 30.469 -11.238 20.901 1.00 89.87 ? 130 GLY A C 1 ATOM 1036 O O . GLY A 1 130 ? 30.339 -11.689 19.754 1.00 86.23 ? 130 GLY A O 1 ATOM 1037 N N . VAL A 1 131 ? 30.808 -9.977 21.170 1.00 90.75 ? 131 VAL A N 1 ATOM 1038 C CA . VAL A 1 131 ? 30.887 -8.932 20.148 1.00 89.96 ? 131 VAL A CA 1 ATOM 1039 C C . VAL A 1 131 ? 32.209 -8.159 20.223 1.00 89.68 ? 131 VAL A C 1 ATOM 1040 O O . VAL A 1 131 ? 32.970 -8.306 21.178 1.00 90.25 ? 131 VAL A O 1 ATOM 1041 C CB . VAL A 1 131 ? 29.702 -7.946 20.276 1.00 92.74 ? 131 VAL A CB 1 ATOM 1042 C CG1 . VAL A 1 131 ? 28.379 -8.686 20.123 1.00 92.58 ? 131 VAL A CG1 1 ATOM 1043 C CG2 . VAL A 1 131 ? 29.743 -7.192 21.605 1.00 95.60 ? 131 VAL A CG2 1 ATOM 1044 N N . SER A 1 132 ? 32.466 -7.336 19.207 1.00 89.20 ? 132 SER A N 1 ATOM 1045 C CA . SER A 1 132 ? 33.694 -6.536 19.125 1.00 88.48 ? 132 SER A CA 1 ATOM 1046 C C . SER A 1 132 ? 33.497 -5.302 18.253 1.00 90.10 ? 132 SER A C 1 ATOM 1047 O O . SER A 1 132 ? 32.661 -5.299 17.343 1.00 89.63 ? 132 SER A O 1 ATOM 1048 C CB . SER A 1 132 ? 34.846 -7.371 18.557 1.00 84.37 ? 132 SER A CB 1 ATOM 1049 O OG . SER A 1 132 ? 35.938 -6.550 18.162 1.00 82.59 ? 132 SER A OG 1 ATOM 1050 N N . SER A 1 133 ? 34.288 -4.267 18.526 1.00 92.22 ? 133 SER A N 1 ATOM 1051 C CA . SER A 1 133 ? 34.245 -3.023 17.759 1.00 93.86 ? 133 SER A CA 1 ATOM 1052 C C . SER A 1 133 ? 34.825 -3.177 16.348 1.00 91.86 ? 133 SER A C 1 ATOM 1053 O O . SER A 1 133 ? 34.564 -2.344 15.480 1.00 92.36 ? 133 SER A O 1 ATOM 1054 C CB . SER A 1 133 ? 34.984 -1.912 18.509 1.00 96.52 ? 133 SER A CB 1 ATOM 1055 O OG . SER A 1 133 ? 36.318 -2.295 18.796 1.00 95.89 ? 133 SER A OG 1 ATOM 1056 N N . ALA A 1 134 ? 35.609 -4.233 16.123 1.00 90.57 ? 134 ALA A N 1 ATOM 1057 C CA . ALA A 1 134 ? 36.145 -4.539 14.788 1.00 89.11 ? 134 ALA A CA 1 ATOM 1058 C C . ALA A 1 134 ? 35.068 -5.023 13.808 1.00 88.86 ? 134 ALA A C 1 ATOM 1059 O O . ALA A 1 134 ? 35.248 -4.924 12.595 1.00 86.90 ? 134 ALA A O 1 ATOM 1060 C CB . ALA A 1 134 ? 37.260 -5.570 14.884 1.00 87.05 ? 134 ALA A CB 1 ATOM 1061 N N . CYS A 1 135 ? 33.960 -5.546 14.335 1.00 90.99 ? 135 CYS A N 1 ATOM 1062 C CA . CYS A 1 135 ? 32.819 -5.958 13.519 1.00 91.66 ? 135 CYS A CA 1 ATOM 1063 C C . CYS A 1 135 ? 31.584 -5.106 13.853 1.00 92.63 ? 135 CYS A C 1 ATOM 1064 O O . CYS A 1 135 ? 30.667 -5.571 14.538 1.00 92.06 ? 135 CYS A O 1 ATOM 1065 C CB . CYS A 1 135 ? 32.526 -7.443 13.743 1.00 93.26 ? 135 CYS A CB 1 ATOM 1066 S SG . CYS A 1 135 ? 33.945 -8.523 13.436 1.00 94.87 ? 135 CYS A SG 1 ATOM 1067 N N . PRO A 1 136 ? 31.561 -3.848 13.370 1.00 92.27 ? 136 PRO A N 1 ATOM 1068 C CA . PRO A 1 136 ? 30.458 -2.944 13.684 1.00 94.74 ? 136 PRO A CA 1 ATOM 1069 C C . PRO A 1 136 ? 29.202 -3.200 12.854 1.00 93.97 ? 136 PRO A C 1 ATOM 1070 O O . PRO A 1 136 ? 29.285 -3.743 11.755 1.00 91.14 ? 136 PRO A O 1 ATOM 1071 C CB . PRO A 1 136 ? 31.037 -1.569 13.343 1.00 96.18 ? 136 PRO A CB 1 ATOM 1072 C CG . PRO A 1 136 ? 31.988 -1.846 12.235 1.00 93.23 ? 136 PRO A CG 1 ATOM 1073 C CD . PRO A 1 136 ? 32.598 -3.177 12.563 1.00 90.77 ? 136 PRO A CD 1 ATOM 1074 N N . TYR A 1 137 ? 28.054 -2.798 13.393 1.00 96.62 ? 137 TYR A N 1 ATOM 1075 C CA . TYR A 1 137 ? 26.780 -2.847 12.680 1.00 97.56 ? 137 TYR A CA 1 ATOM 1076 C C . TYR A 1 137 ? 25.857 -1.743 13.194 1.00 100.97 ? 137 TYR A C 1 ATOM 1077 O O . TYR A 1 137 ? 25.490 -1.735 14.373 1.00 103.63 ? 137 TYR A O 1 ATOM 1078 C CB . TYR A 1 137 ? 26.116 -4.212 12.861 1.00 96.90 ? 137 TYR A CB 1 ATOM 1079 C CG . TYR A 1 137 ? 24.749 -4.319 12.213 1.00 98.54 ? 137 TYR A CG 1 ATOM 1080 C CD1 . TYR A 1 137 ? 24.615 -4.377 10.824 1.00 97.10 ? 137 TYR A CD1 1 ATOM 1081 C CD2 . TYR A 1 137 ? 23.589 -4.366 12.987 1.00 100.46 ? 137 TYR A CD2 1 ATOM 1082 C CE1 . TYR A 1 137 ? 23.367 -4.475 10.229 1.00 98.08 ? 137 TYR A CE1 1 ATOM 1083 C CE2 . TYR A 1 137 ? 22.338 -4.465 12.399 1.00 101.65 ? 137 TYR A CE2 1 ATOM 1084 C CZ . TYR A 1 137 ? 22.233 -4.520 11.022 1.00 100.40 ? 137 TYR A CZ 1 ATOM 1085 O OH . TYR A 1 137 ? 20.994 -4.618 10.439 1.00 101.44 ? 137 TYR A OH 1 ATOM 1086 N N . GLN A 1 138 ? 25.494 -0.816 12.308 1.00 101.76 ? 138 GLN A N 1 ATOM 1087 C CA . GLN A 1 138 ? 24.648 0.328 12.660 1.00 105.81 ? 138 GLN A CA 1 ATOM 1088 C C . GLN A 1 138 ? 25.164 1.077 13.896 1.00 107.89 ? 138 GLN A C 1 ATOM 1089 O O . GLN A 1 138 ? 24.383 1.474 14.762 1.00 110.54 ? 138 GLN A O 1 ATOM 1090 C CB . GLN A 1 138 ? 23.197 -0.118 12.877 1.00 107.70 ? 138 GLN A CB 1 ATOM 1091 C CG . GLN A 1 138 ? 22.615 -0.899 11.710 1.00 106.49 ? 138 GLN A CG 1 ATOM 1092 C CD . GLN A 1 138 ? 21.104 -1.055 11.780 1.00 109.00 ? 138 GLN A CD 1 ATOM 1093 O OE1 . GLN A 1 138 ? 20.468 -0.706 12.775 1.00 110.44 ? 138 GLN A OE1 1 ATOM 1094 N NE2 . GLN A 1 138 ? 20.522 -1.585 10.711 1.00 109.23 ? 138 GLN A NE2 1 ATOM 1095 N N . GLY A 1 139 ? 26.482 1.256 13.968 1.00 106.05 ? 139 GLY A N 1 ATOM 1096 C CA . GLY A 1 139 ? 27.113 2.031 15.036 1.00 107.19 ? 139 GLY A CA 1 ATOM 1097 C C . GLY A 1 139 ? 27.480 1.244 16.279 1.00 106.06 ? 139 GLY A C 1 ATOM 1098 O O . GLY A 1 139 ? 28.215 1.746 17.131 1.00 106.27 ? 139 GLY A O 1 ATOM 1099 N N . LYS A 1 140 ? 26.973 0.017 16.383 1.00 104.28 ? 140 LYS A N 1 ATOM 1100 C CA . LYS A 1 140 ? 27.174 -0.811 17.568 1.00 105.50 ? 140 LYS A CA 1 ATOM 1101 C C . LYS A 1 140 ? 28.104 -1.969 17.261 1.00 100.82 ? 140 LYS A C 1 ATOM 1102 O O . LYS A 1 140 ? 28.266 -2.349 16.108 1.00 97.90 ? 140 LYS A O 1 ATOM 1103 C CB . LYS A 1 140 ? 25.832 -1.346 18.083 1.00 108.65 ? 140 LYS A CB 1 ATOM 1104 C CG . LYS A 1 140 ? 25.005 -0.314 18.837 1.00 114.75 ? 140 LYS A CG 1 ATOM 1105 C CD . LYS A 1 140 ? 23.554 -0.748 19.033 1.00 118.21 ? 140 LYS A CD 1 ATOM 1106 C CE . LYS A 1 140 ? 22.627 -0.225 17.937 1.00 119.84 ? 140 LYS A CE 1 ATOM 1107 N NZ . LYS A 1 140 ? 22.917 -0.804 16.593 1.00 117.15 ? 140 LYS A NZ 1 ATOM 1108 N N . SER A 1 141 ? 28.708 -2.525 18.308 1.00 100.90 ? 141 SER A N 1 ATOM 1109 C CA . SER A 1 141 ? 29.606 -3.673 18.182 1.00 97.36 ? 141 SER A CA 1 ATOM 1110 C C . SER A 1 141 ? 28.805 -4.940 17.892 1.00 95.64 ? 141 SER A C 1 ATOM 1111 O O . SER A 1 141 ? 27.795 -5.206 18.537 1.00 98.08 ? 141 SER A O 1 ATOM 1112 C CB . SER A 1 141 ? 30.421 -3.854 19.466 1.00 97.87 ? 141 SER A CB 1 ATOM 1113 O OG . SER A 1 141 ? 31.202 -2.704 19.745 1.00 99.56 ? 141 SER A OG 1 ATOM 1114 N N . SER A 1 142 ? 29.257 -5.717 16.917 1.00 92.78 ? 142 SER A N 1 ATOM 1115 C CA . SER A 1 142 ? 28.545 -6.918 16.502 1.00 91.54 ? 142 SER A CA 1 ATOM 1116 C C . SER A 1 142 ? 29.551 -8.052 16.295 1.00 88.53 ? 142 SER A C 1 ATOM 1117 O O . SER A 1 142 ? 30.661 -7.996 16.826 1.00 87.96 ? 142 SER A O 1 ATOM 1118 C CB . SER A 1 142 ? 27.743 -6.627 15.228 1.00 91.50 ? 142 SER A CB 1 ATOM 1119 O OG . SER A 1 142 ? 26.850 -7.683 14.926 1.00 91.26 ? 142 SER A OG 1 ATOM 1120 N N . PHE A 1 143 ? 29.160 -9.085 15.551 1.00 86.70 ? 143 PHE A N 1 ATOM 1121 C CA . PHE A 1 143 ? 30.041 -10.226 15.288 1.00 84.34 ? 143 PHE A CA 1 ATOM 1122 C C . PHE A 1 143 ? 29.504 -11.070 14.140 1.00 83.63 ? 143 PHE A C 1 ATOM 1123 O O . PHE A 1 143 ? 28.337 -10.940 13.760 1.00 86.65 ? 143 PHE A O 1 ATOM 1124 C CB . PHE A 1 143 ? 30.178 -11.101 16.541 1.00 84.03 ? 143 PHE A CB 1 ATOM 1125 C CG . PHE A 1 143 ? 31.387 -12.001 16.533 1.00 80.42 ? 143 PHE A CG 1 ATOM 1126 C CD1 . PHE A 1 143 ? 32.669 -11.463 16.565 1.00 79.01 ? 143 PHE A CD1 1 ATOM 1127 C CD2 . PHE A 1 143 ? 31.245 -13.384 16.513 1.00 78.69 ? 143 PHE A CD2 1 ATOM 1128 C CE1 . PHE A 1 143 ? 33.783 -12.284 16.568 1.00 77.46 ? 143 PHE A CE1 1 ATOM 1129 C CE2 . PHE A 1 143 ? 32.356 -14.211 16.518 1.00 77.09 ? 143 PHE A CE2 1 ATOM 1130 C CZ . PHE A 1 143 ? 33.629 -13.661 16.544 1.00 76.63 ? 143 PHE A CZ 1 ATOM 1131 N N . PHE A 1 144 ? 30.366 -11.924 13.591 1.00 80.80 ? 144 PHE A N 1 ATOM 1132 C CA . PHE A 1 144 ? 29.963 -12.907 12.586 1.00 79.19 ? 144 PHE A CA 1 ATOM 1133 C C . PHE A 1 144 ? 28.649 -13.573 13.014 1.00 80.14 ? 144 PHE A C 1 ATOM 1134 O O . PHE A 1 144 ? 28.603 -14.274 14.023 1.00 80.82 ? 144 PHE A O 1 ATOM 1135 C CB . PHE A 1 144 ? 31.038 -13.987 12.415 1.00 77.10 ? 144 PHE A CB 1 ATOM 1136 C CG . PHE A 1 144 ? 32.390 -13.466 11.984 1.00 75.85 ? 144 PHE A CG 1 ATOM 1137 C CD1 . PHE A 1 144 ? 32.597 -13.011 10.694 1.00 74.88 ? 144 PHE A CD1 1 ATOM 1138 C CD2 . PHE A 1 144 ? 33.465 -13.462 12.871 1.00 76.42 ? 144 PHE A CD2 1 ATOM 1139 C CE1 . PHE A 1 144 ? 33.845 -12.553 10.296 1.00 74.35 ? 144 PHE A CE1 1 ATOM 1140 C CE2 . PHE A 1 144 ? 34.713 -13.004 12.479 1.00 75.26 ? 144 PHE A CE2 1 ATOM 1141 C CZ . PHE A 1 144 ? 34.904 -12.549 11.189 1.00 74.17 ? 144 PHE A CZ 1 ATOM 1142 N N . ARG A 1 145 ? 27.589 -13.350 12.244 1.00 80.52 ? 145 ARG A N 1 ATOM 1143 C CA . ARG A 1 145 ? 26.241 -13.772 12.630 1.00 81.37 ? 145 ARG A CA 1 ATOM 1144 C C . ARG A 1 145 ? 26.031 -15.281 12.743 1.00 82.60 ? 145 ARG A C 1 ATOM 1145 O O . ARG A 1 145 ? 25.128 -15.720 13.450 1.00 86.36 ? 145 ARG A O 1 ATOM 1146 C CB . ARG A 1 145 ? 25.211 -13.225 11.643 1.00 80.58 ? 145 ARG A CB 1 ATOM 1147 C CG . ARG A 1 145 ? 25.211 -11.716 11.513 1.00 80.94 ? 145 ARG A CG 1 ATOM 1148 C CD . ARG A 1 145 ? 23.862 -11.228 11.034 1.00 83.00 ? 145 ARG A CD 1 ATOM 1149 N NE . ARG A 1 145 ? 23.871 -9.793 10.772 1.00 85.02 ? 145 ARG A NE 1 ATOM 1150 C CZ . ARG A 1 145 ? 23.807 -8.848 11.709 1.00 88.16 ? 145 ARG A CZ 1 ATOM 1151 N NH1 . ARG A 1 145 ? 23.744 -9.160 13.002 1.00 89.33 ? 145 ARG A NH1 1 ATOM 1152 N NH2 . ARG A 1 145 ? 23.817 -7.572 11.348 1.00 90.42 ? 145 ARG A NH2 1 ATOM 1153 N N . ASN A 1 146 ? 26.838 -16.076 12.046 1.00 82.97 ? 146 ASN A N 1 ATOM 1154 C CA . ASN A 1 146 ? 26.585 -17.518 11.958 1.00 82.73 ? 146 ASN A CA 1 ATOM 1155 C C . ASN A 1 146 ? 27.247 -18.345 13.053 1.00 81.01 ? 146 ASN A C 1 ATOM 1156 O O . ASN A 1 146 ? 26.958 -19.537 13.191 1.00 79.26 ? 146 ASN A O 1 ATOM 1157 C CB . ASN A 1 146 ? 26.975 -18.042 10.573 1.00 81.50 ? 146 ASN A CB 1 ATOM 1158 C CG . ASN A 1 146 ? 26.116 -17.453 9.475 1.00 83.32 ? 146 ASN A CG 1 ATOM 1159 O OD1 . ASN A 1 146 ? 24.972 -17.061 9.714 1.00 86.88 ? 146 ASN A OD1 1 ATOM 1160 N ND2 . ASN A 1 146 ? 26.658 -17.389 8.263 1.00 83.92 ? 146 ASN A ND2 1 ATOM 1161 N N . VAL A 1 147 ? 28.111 -17.712 13.840 1.00 80.88 ? 147 VAL A N 1 ATOM 1162 C CA . VAL A 1 147 ? 28.747 -18.386 14.968 1.00 81.13 ? 147 VAL A CA 1 ATOM 1163 C C . VAL A 1 147 ? 28.637 -17.563 16.251 1.00 82.66 ? 147 VAL A C 1 ATOM 1164 O O . VAL A 1 147 ? 28.563 -16.336 16.208 1.00 84.23 ? 147 VAL A O 1 ATOM 1165 C CB . VAL A 1 147 ? 30.216 -18.726 14.658 1.00 79.58 ? 147 VAL A CB 1 ATOM 1166 C CG1 . VAL A 1 147 ? 30.290 -19.718 13.507 1.00 77.85 ? 147 VAL A CG1 1 ATOM 1167 C CG2 . VAL A 1 147 ? 31.013 -17.469 14.327 1.00 79.41 ? 147 VAL A CG2 1 ATOM 1168 N N . VAL A 1 148 ? 28.630 -18.254 17.387 1.00 83.05 ? 148 VAL A N 1 ATOM 1169 C CA . VAL A 1 148 ? 28.400 -17.632 18.691 1.00 84.66 ? 148 VAL A CA 1 ATOM 1170 C C . VAL A 1 148 ? 29.696 -17.580 19.492 1.00 83.83 ? 148 VAL A C 1 ATOM 1171 O O . VAL A 1 148 ? 30.270 -18.621 19.813 1.00 84.29 ? 148 VAL A O 1 ATOM 1172 C CB . VAL A 1 148 ? 27.359 -18.433 19.503 1.00 86.24 ? 148 VAL A CB 1 ATOM 1173 C CG1 . VAL A 1 148 ? 26.999 -17.697 20.786 1.00 89.91 ? 148 VAL A CG1 1 ATOM 1174 C CG2 . VAL A 1 148 ? 26.114 -18.701 18.668 1.00 86.52 ? 148 VAL A CG2 1 ATOM 1175 N N . TRP A 1 149 ? 30.154 -16.371 19.813 1.00 83.48 ? 149 TRP A N 1 ATOM 1176 C CA . TRP A 1 149 ? 31.340 -16.190 20.651 1.00 83.46 ? 149 TRP A CA 1 ATOM 1177 C C . TRP A 1 149 ? 30.939 -16.246 22.137 1.00 86.42 ? 149 TRP A C 1 ATOM 1178 O O . TRP A 1 149 ? 30.502 -15.253 22.714 1.00 87.58 ? 149 TRP A O 1 ATOM 1179 C CB . TRP A 1 149 ? 32.036 -14.870 20.296 1.00 82.92 ? 149 TRP A CB 1 ATOM 1180 C CG . TRP A 1 149 ? 33.302 -14.571 21.067 1.00 82.98 ? 149 TRP A CG 1 ATOM 1181 C CD1 . TRP A 1 149 ? 33.941 -15.382 21.964 1.00 82.82 ? 149 TRP A CD1 1 ATOM 1182 C CD2 . TRP A 1 149 ? 34.099 -13.385 20.964 1.00 82.94 ? 149 TRP A CD2 1 ATOM 1183 N NE1 . TRP A 1 149 ? 35.073 -14.763 22.437 1.00 83.34 ? 149 TRP A NE1 1 ATOM 1184 C CE2 . TRP A 1 149 ? 35.197 -13.540 21.835 1.00 83.09 ? 149 TRP A CE2 1 ATOM 1185 C CE3 . TRP A 1 149 ? 33.991 -12.206 20.218 1.00 83.02 ? 149 TRP A CE3 1 ATOM 1186 C CZ2 . TRP A 1 149 ? 36.177 -12.559 21.985 1.00 83.53 ? 149 TRP A CZ2 1 ATOM 1187 C CZ3 . TRP A 1 149 ? 34.967 -11.230 20.368 1.00 83.68 ? 149 TRP A CZ3 1 ATOM 1188 C CH2 . TRP A 1 149 ? 36.045 -11.414 21.244 1.00 83.87 ? 149 TRP A CH2 1 ATOM 1189 N N . LEU A 1 150 ? 31.101 -17.422 22.741 1.00 86.79 ? 150 LEU A N 1 ATOM 1190 C CA . LEU A 1 150 ? 30.652 -17.675 24.107 1.00 89.39 ? 150 LEU A CA 1 ATOM 1191 C C . LEU A 1 150 ? 31.694 -17.227 25.121 1.00 90.86 ? 150 LEU A C 1 ATOM 1192 O O . LEU A 1 150 ? 32.890 -17.428 24.904 1.00 89.43 ? 150 LEU A O 1 ATOM 1193 C CB . LEU A 1 150 ? 30.377 -19.167 24.305 1.00 89.34 ? 150 LEU A CB 1 ATOM 1194 C CG . LEU A 1 150 ? 29.315 -19.789 23.394 1.00 88.93 ? 150 LEU A CG 1 ATOM 1195 C CD1 . LEU A 1 150 ? 29.411 -21.308 23.408 1.00 88.42 ? 150 LEU A CD1 1 ATOM 1196 C CD2 . LEU A 1 150 ? 27.921 -19.335 23.799 1.00 91.33 ? 150 LEU A CD2 1 ATOM 1197 N N . ILE A 1 151 ? 31.230 -16.624 26.219 1.00 93.86 ? 151 ILE A N 1 ATOM 1198 C CA . ILE A 1 151 ? 32.093 -16.271 27.355 1.00 95.37 ? 151 ILE A CA 1 ATOM 1199 C C . ILE A 1 151 ? 31.519 -16.806 28.676 1.00 97.82 ? 151 ILE A C 1 ATOM 1200 O O . ILE A 1 151 ? 30.421 -17.368 28.713 1.00 96.92 ? 151 ILE A O 1 ATOM 1201 C CB . ILE A 1 151 ? 32.335 -14.742 27.449 1.00 96.46 ? 151 ILE A CB 1 ATOM 1202 C CG1 . ILE A 1 151 ? 31.072 -14.002 27.904 1.00 99.48 ? 151 ILE A CG1 1 ATOM 1203 C CG2 . ILE A 1 151 ? 32.822 -14.195 26.113 1.00 93.47 ? 151 ILE A CG2 1 ATOM 1204 C CD1 . ILE A 1 151 ? 31.262 -12.509 28.066 1.00 101.06 ? 151 ILE A CD1 1 ATOM 1205 N N . LYS A 1 152 ? 32.283 -16.632 29.750 1.00 101.18 ? 152 LYS A N 1 ATOM 1206 C CA . LYS A 1 152 ? 31.892 -17.088 31.090 1.00 105.08 ? 152 LYS A CA 1 ATOM 1207 C C . LYS A 1 152 ? 30.642 -16.381 31.626 1.00 109.12 ? 152 LYS A C 1 ATOM 1208 O O . LYS A 1 152 ? 30.387 -15.222 31.299 1.00 109.47 ? 152 LYS A O 1 ATOM 1209 C CB . LYS A 1 152 ? 33.050 -16.873 32.069 1.00 106.18 ? 152 LYS A CB 1 ATOM 1210 C CG . LYS A 1 152 ? 33.328 -15.411 32.396 1.00 108.52 ? 152 LYS A CG 1 ATOM 1211 C CD . LYS A 1 152 ? 34.549 -15.261 33.286 1.00 109.79 ? 152 LYS A CD 1 ATOM 1212 C CE . LYS A 1 152 ? 34.588 -13.897 33.954 1.00 112.06 ? 152 LYS A CE 1 ATOM 1213 N NZ . LYS A 1 152 ? 35.836 -13.721 34.744 1.00 113.65 ? 152 LYS A NZ 1 ATOM 1214 N N . LYS A 1 153 ? 29.880 -17.086 32.462 1.00 113.26 ? 153 LYS A N 1 ATOM 1215 C CA . LYS A 1 153 ? 28.696 -16.521 33.115 1.00 118.08 ? 153 LYS A CA 1 ATOM 1216 C C . LYS A 1 153 ? 28.828 -16.647 34.629 1.00 120.49 ? 153 LYS A C 1 ATOM 1217 O O . LYS A 1 153 ? 28.992 -17.750 35.147 1.00 119.65 ? 153 LYS A O 1 ATOM 1218 C CB . LYS A 1 153 ? 27.425 -17.228 32.635 1.00 119.42 ? 153 LYS A CB 1 ATOM 1219 C CG . LYS A 1 153 ? 26.172 -16.374 32.762 1.00 123.19 ? 153 LYS A CG 1 ATOM 1220 C CD . LYS A 1 153 ? 24.913 -17.141 32.387 1.00 124.31 ? 153 LYS A CD 1 ATOM 1221 C CE . LYS A 1 153 ? 24.490 -18.094 33.494 1.00 127.03 ? 153 LYS A CE 1 ATOM 1222 N NZ . LYS A 1 153 ? 23.105 -18.606 33.299 1.00 128.82 ? 153 LYS A NZ 1 ATOM 1223 N N . ASN A 1 154 ? 28.742 -15.510 35.321 1.00 124.27 ? 154 ASN A N 1 ATOM 1224 C CA . ASN A 1 154 ? 28.986 -15.415 36.773 1.00 127.95 ? 154 ASN A CA 1 ATOM 1225 C C . ASN A 1 154 ? 30.336 -16.034 37.183 1.00 126.48 ? 154 ASN A C 1 ATOM 1226 O O . ASN A 1 154 ? 30.418 -16.824 38.127 1.00 127.67 ? 154 ASN A O 1 ATOM 1227 C CB . ASN A 1 154 ? 27.814 -16.006 37.583 1.00 130.96 ? 154 ASN A CB 1 ATOM 1228 C CG . ASN A 1 154 ? 27.783 -15.512 39.029 1.00 136.67 ? 154 ASN A CG 1 ATOM 1229 O OD1 . ASN A 1 154 ? 28.637 -14.732 39.452 1.00 138.20 ? 154 ASN A OD1 1 ATOM 1230 N ND2 . ASN A 1 154 ? 26.790 -15.967 39.794 1.00 140.47 ? 154 ASN A ND2 1 ATOM 1231 N N . SER A 1 155 ? 31.383 -15.662 36.446 1.00 123.77 ? 155 SER A N 1 ATOM 1232 C CA . SER A 1 155 ? 32.770 -16.057 36.738 1.00 122.33 ? 155 SER A CA 1 ATOM 1233 C C . SER A 1 155 ? 33.044 -17.567 36.680 1.00 120.39 ? 155 SER A C 1 ATOM 1234 O O . SER A 1 155 ? 33.888 -18.074 37.421 1.00 121.57 ? 155 SER A O 1 ATOM 1235 C CB . SER A 1 155 ? 33.219 -15.493 38.095 1.00 125.36 ? 155 SER A CB 1 ATOM 1236 O OG . SER A 1 155 ? 33.032 -14.091 38.149 1.00 127.03 ? 155 SER A OG 1 ATOM 1237 N N . THR A 1 156 ? 32.340 -18.277 35.802 1.00 117.80 ? 156 THR A N 1 ATOM 1238 C CA . THR A 1 156 ? 32.623 -19.692 35.545 1.00 116.15 ? 156 THR A CA 1 ATOM 1239 C C . THR A 1 156 ? 32.393 -20.021 34.078 1.00 113.75 ? 156 THR A C 1 ATOM 1240 O O . THR A 1 156 ? 31.444 -19.527 33.466 1.00 116.38 ? 156 THR A O 1 ATOM 1241 C CB . THR A 1 156 ? 31.737 -20.641 36.381 1.00 118.06 ? 156 THR A CB 1 ATOM 1242 O OG1 . THR A 1 156 ? 30.354 -20.380 36.112 1.00 119.33 ? 156 THR A OG1 1 ATOM 1243 C CG2 . THR A 1 156 ? 32.002 -20.481 37.865 1.00 121.52 ? 156 THR A CG2 1 ATOM 1244 N N . TYR A 1 157 ? 33.275 -20.845 33.519 1.00 110.43 ? 157 TYR A N 1 ATOM 1245 C CA . TYR A 1 157 ? 33.088 -21.413 32.190 1.00 104.84 ? 157 TYR A CA 1 ATOM 1246 C C . TYR A 1 157 ? 33.129 -22.930 32.363 1.00 102.94 ? 157 TYR A C 1 ATOM 1247 O O . TYR A 1 157 ? 34.206 -23.529 32.376 1.00 100.28 ? 157 TYR A O 1 ATOM 1248 C CB . TYR A 1 157 ? 34.184 -20.927 31.235 1.00 102.86 ? 157 TYR A CB 1 ATOM 1249 C CG . TYR A 1 157 ? 33.902 -21.164 29.758 1.00 100.05 ? 157 TYR A CG 1 ATOM 1250 C CD1 . TYR A 1 157 ? 34.010 -22.436 29.199 1.00 98.48 ? 157 TYR A CD1 1 ATOM 1251 C CD2 . TYR A 1 157 ? 33.541 -20.112 28.918 1.00 99.22 ? 157 TYR A CD2 1 ATOM 1252 C CE1 . TYR A 1 157 ? 33.761 -22.654 27.852 1.00 97.17 ? 157 TYR A CE1 1 ATOM 1253 C CE2 . TYR A 1 157 ? 33.293 -20.319 27.570 1.00 96.74 ? 157 TYR A CE2 1 ATOM 1254 C CZ . TYR A 1 157 ? 33.401 -21.594 27.040 1.00 95.78 ? 157 TYR A CZ 1 ATOM 1255 O OH . TYR A 1 157 ? 33.158 -21.812 25.701 1.00 93.02 ? 157 TYR A OH 1 ATOM 1256 N N . PRO A 1 158 ? 31.953 -23.554 32.548 1.00 103.87 ? 158 PRO A N 1 ATOM 1257 C CA . PRO A 1 158 ? 31.937 -25.005 32.700 1.00 103.44 ? 158 PRO A CA 1 ATOM 1258 C C . PRO A 1 158 ? 32.122 -25.686 31.356 1.00 99.13 ? 158 PRO A C 1 ATOM 1259 O O . PRO A 1 158 ? 31.892 -25.068 30.316 1.00 97.26 ? 158 PRO A O 1 ATOM 1260 C CB . PRO A 1 158 ? 30.550 -25.291 33.291 1.00 106.14 ? 158 PRO A CB 1 ATOM 1261 C CG . PRO A 1 158 ? 29.702 -24.138 32.887 1.00 106.72 ? 158 PRO A CG 1 ATOM 1262 C CD . PRO A 1 158 ? 30.610 -22.957 32.682 1.00 106.14 ? 158 PRO A CD 1 ATOM 1263 N N . THR A 1 159 ? 32.549 -26.944 31.380 1.00 98.62 ? 159 THR A N 1 ATOM 1264 C CA . THR A 1 159 ? 32.820 -27.679 30.147 1.00 95.58 ? 159 THR A CA 1 ATOM 1265 C C . THR A 1 159 ? 31.548 -27.791 29.311 1.00 95.24 ? 159 THR A C 1 ATOM 1266 O O . THR A 1 159 ? 30.462 -28.038 29.841 1.00 96.45 ? 159 THR A O 1 ATOM 1267 C CB . THR A 1 159 ? 33.376 -29.095 30.420 1.00 95.22 ? 159 THR A CB 1 ATOM 1268 O OG1 . THR A 1 159 ? 34.408 -29.032 31.411 1.00 95.95 ? 159 THR A OG1 1 ATOM 1269 C CG2 . THR A 1 159 ? 33.947 -29.709 29.148 1.00 92.29 ? 159 THR A CG2 1 ATOM 1270 N N . ILE A 1 160 ? 31.705 -27.583 28.006 1.00 93.72 ? 160 ILE A N 1 ATOM 1271 C CA . ILE A 1 160 ? 30.626 -27.719 27.032 1.00 93.33 ? 160 ILE A CA 1 ATOM 1272 C C . ILE A 1 160 ? 30.718 -29.106 26.408 1.00 93.18 ? 160 ILE A C 1 ATOM 1273 O O . ILE A 1 160 ? 31.798 -29.533 26.014 1.00 91.18 ? 160 ILE A O 1 ATOM 1274 C CB . ILE A 1 160 ? 30.751 -26.644 25.925 1.00 91.14 ? 160 ILE A CB 1 ATOM 1275 C CG1 . ILE A 1 160 ? 30.459 -25.256 26.507 1.00 92.92 ? 160 ILE A CG1 1 ATOM 1276 C CG2 . ILE A 1 160 ? 29.813 -26.940 24.760 1.00 90.05 ? 160 ILE A CG2 1 ATOM 1277 C CD1 . ILE A 1 160 ? 30.933 -24.101 25.650 1.00 90.98 ? 160 ILE A CD1 1 ATOM 1278 N N . LYS A 1 161 ? 29.595 -29.813 26.341 1.00 96.08 ? 161 LYS A N 1 ATOM 1279 C CA . LYS A 1 161 ? 29.518 -31.078 25.614 1.00 97.01 ? 161 LYS A CA 1 ATOM 1280 C C . LYS A 1 161 ? 28.273 -31.046 24.742 1.00 97.41 ? 161 LYS A C 1 ATOM 1281 O O . LYS A 1 161 ? 27.180 -31.367 25.210 1.00 99.79 ? 161 LYS A O 1 ATOM 1282 C CB . LYS A 1 161 ? 29.442 -32.272 26.572 1.00 101.52 ? 161 LYS A CB 1 ATOM 1283 C CG . LYS A 1 161 ? 30.672 -32.509 27.439 1.00 104.47 ? 161 LYS A CG 1 ATOM 1284 C CD . LYS A 1 161 ? 30.394 -33.614 28.456 1.00 109.64 ? 161 LYS A CD 1 ATOM 1285 C CE . LYS A 1 161 ? 31.487 -33.753 29.510 1.00 112.43 ? 161 LYS A CE 1 ATOM 1286 N NZ . LYS A 1 161 ? 32.661 -34.522 29.009 1.00 111.99 ? 161 LYS A NZ 1 ATOM 1287 N N . ARG A 1 162 ? 28.433 -30.647 23.483 1.00 96.03 ? 162 ARG A N 1 ATOM 1288 C CA . ARG A 1 162 ? 27.301 -30.523 22.567 1.00 96.52 ? 162 ARG A CA 1 ATOM 1289 C C . ARG A 1 162 ? 27.516 -31.322 21.288 1.00 95.53 ? 162 ARG A C 1 ATOM 1290 O O . ARG A 1 162 ? 28.612 -31.344 20.722 1.00 93.22 ? 162 ARG A O 1 ATOM 1291 C CB . ARG A 1 162 ? 27.030 -29.053 22.240 1.00 97.06 ? 162 ARG A CB 1 ATOM 1292 C CG . ARG A 1 162 ? 26.552 -28.243 23.437 1.00 101.34 ? 162 ARG A CG 1 ATOM 1293 C CD . ARG A 1 162 ? 25.121 -28.586 23.838 1.00 105.22 ? 162 ARG A CD 1 ATOM 1294 N NE . ARG A 1 162 ? 24.137 -27.681 23.242 1.00 106.70 ? 162 ARG A NE 1 ATOM 1295 C CZ . ARG A 1 162 ? 23.792 -26.492 23.737 1.00 108.61 ? 162 ARG A CZ 1 ATOM 1296 N NH1 . ARG A 1 162 ? 24.351 -26.021 24.849 1.00 109.88 ? 162 ARG A NH1 1 ATOM 1297 N NH2 . ARG A 1 162 ? 22.881 -25.757 23.111 1.00 110.07 ? 162 ARG A NH2 1 ATOM 1298 N N . SER A 1 163 ? 26.442 -31.965 20.839 1.00 95.68 ? 163 SER A N 1 ATOM 1299 C CA . SER A 1 163 ? 26.479 -32.872 19.711 1.00 92.79 ? 163 SER A CA 1 ATOM 1300 C C . SER A 1 163 ? 25.351 -32.530 18.744 1.00 93.68 ? 163 SER A C 1 ATOM 1301 O O . SER A 1 163 ? 24.224 -32.290 19.172 1.00 94.31 ? 163 SER A O 1 ATOM 1302 C CB . SER A 1 163 ? 26.319 -34.307 20.214 1.00 93.57 ? 163 SER A CB 1 ATOM 1303 O OG . SER A 1 163 ? 26.245 -35.235 19.146 1.00 94.30 ? 163 SER A OG 1 ATOM 1304 N N . TYR A 1 164 ? 25.655 -32.486 17.448 1.00 92.74 ? 164 TYR A N 1 ATOM 1305 C CA . TYR A 1 164 ? 24.614 -32.352 16.432 1.00 93.94 ? 164 TYR A CA 1 ATOM 1306 C C . TYR A 1 164 ? 24.648 -33.527 15.459 1.00 95.52 ? 164 TYR A C 1 ATOM 1307 O O . TYR A 1 164 ? 25.707 -33.890 14.950 1.00 93.86 ? 164 TYR A O 1 ATOM 1308 C CB . TYR A 1 164 ? 24.731 -31.037 15.665 1.00 91.39 ? 164 TYR A CB 1 ATOM 1309 C CG . TYR A 1 164 ? 23.765 -30.982 14.509 1.00 91.83 ? 164 TYR A CG 1 ATOM 1310 C CD1 . TYR A 1 164 ? 22.400 -30.821 14.723 1.00 94.61 ? 164 TYR A CD1 1 ATOM 1311 C CD2 . TYR A 1 164 ? 24.208 -31.134 13.203 1.00 91.49 ? 164 TYR A CD2 1 ATOM 1312 C CE1 . TYR A 1 164 ? 21.508 -30.788 13.662 1.00 95.42 ? 164 TYR A CE1 1 ATOM 1313 C CE2 . TYR A 1 164 ? 23.325 -31.106 12.136 1.00 92.20 ? 164 TYR A CE2 1 ATOM 1314 C CZ . TYR A 1 164 ? 21.980 -30.935 12.370 1.00 93.67 ? 164 TYR A CZ 1 ATOM 1315 O OH . TYR A 1 164 ? 21.120 -30.906 11.303 1.00 94.24 ? 164 TYR A OH 1 ATOM 1316 N N . ASN A 1 165 ? 23.472 -34.099 15.208 1.00 99.58 ? 165 ASN A N 1 ATOM 1317 C CA . ASN A 1 165 ? 23.308 -35.253 14.332 1.00 102.99 ? 165 ASN A CA 1 ATOM 1318 C C . ASN A 1 165 ? 22.672 -34.790 13.027 1.00 101.83 ? 165 ASN A C 1 ATOM 1319 O O . ASN A 1 165 ? 21.592 -34.203 13.035 1.00 104.54 ? 165 ASN A O 1 ATOM 1320 C CB . ASN A 1 165 ? 22.435 -36.297 15.041 1.00 108.74 ? 165 ASN A CB 1 ATOM 1321 C CG . ASN A 1 165 ? 22.135 -37.524 14.187 1.00 113.80 ? 165 ASN A CG 1 ATOM 1322 O OD1 . ASN A 1 165 ? 21.603 -37.413 13.084 1.00 112.42 ? 165 ASN A OD1 1 ATOM 1323 N ND2 . ASN A 1 165 ? 22.461 -38.706 14.712 1.00 120.72 ? 165 ASN A ND2 1 ATOM 1324 N N . ASN A 1 166 ? 23.349 -35.044 11.911 1.00 98.83 ? 166 ASN A N 1 ATOM 1325 C CA . ASN A 1 166 ? 22.842 -34.644 10.602 1.00 97.60 ? 166 ASN A CA 1 ATOM 1326 C C . ASN A 1 166 ? 21.731 -35.578 10.130 1.00 99.26 ? 166 ASN A C 1 ATOM 1327 O O . ASN A 1 166 ? 21.993 -36.581 9.455 1.00 97.65 ? 166 ASN A O 1 ATOM 1328 C CB . ASN A 1 166 ? 23.977 -34.607 9.573 1.00 94.88 ? 166 ASN A CB 1 ATOM 1329 C CG . ASN A 1 166 ? 23.553 -33.989 8.254 1.00 94.76 ? 166 ASN A CG 1 ATOM 1330 O OD1 . ASN A 1 166 ? 22.489 -33.374 8.153 1.00 96.17 ? 166 ASN A OD1 1 ATOM 1331 N ND2 . ASN A 1 166 ? 24.392 -34.143 7.233 1.00 93.11 ? 166 ASN A ND2 1 ATOM 1332 N N . THR A 1 167 ? 20.494 -35.237 10.492 1.00 100.84 ? 167 THR A N 1 ATOM 1333 C CA . THR A 1 167 ? 19.313 -35.989 10.055 1.00 104.47 ? 167 THR A CA 1 ATOM 1334 C C . THR A 1 167 ? 18.813 -35.549 8.673 1.00 105.43 ? 167 THR A C 1 ATOM 1335 O O . THR A 1 167 ? 17.860 -36.125 8.142 1.00 109.94 ? 167 THR A O 1 ATOM 1336 C CB . THR A 1 167 ? 18.149 -35.874 11.067 1.00 106.56 ? 167 THR A CB 1 ATOM 1337 O OG1 . THR A 1 167 ? 17.883 -34.494 11.354 1.00 105.78 ? 167 THR A OG1 1 ATOM 1338 C CG2 . THR A 1 167 ? 18.488 -36.604 12.351 1.00 106.39 ? 167 THR A CG2 1 ATOM 1339 N N . ASN A 1 168 ? 19.454 -34.539 8.089 1.00 102.01 ? 168 ASN A N 1 ATOM 1340 C CA . ASN A 1 168 ? 19.110 -34.095 6.745 1.00 100.20 ? 168 ASN A CA 1 ATOM 1341 C C . ASN A 1 168 ? 19.618 -35.098 5.729 1.00 100.00 ? 168 ASN A C 1 ATOM 1342 O O . ASN A 1 168 ? 20.562 -35.840 6.001 1.00 100.88 ? 168 ASN A O 1 ATOM 1343 C CB . ASN A 1 168 ? 19.731 -32.733 6.442 1.00 97.11 ? 168 ASN A CB 1 ATOM 1344 C CG . ASN A 1 168 ? 19.433 -31.702 7.507 1.00 96.20 ? 168 ASN A CG 1 ATOM 1345 O OD1 . ASN A 1 168 ? 18.371 -31.082 7.503 1.00 96.92 ? 168 ASN A OD1 1 ATOM 1346 N ND2 . ASN A 1 168 ? 20.381 -31.501 8.419 1.00 93.91 ? 168 ASN A ND2 1 ATOM 1347 N N . GLN A 1 169 ? 18.998 -35.115 4.556 1.00 100.53 ? 169 GLN A N 1 ATOM 1348 C CA . GLN A 1 169 ? 19.476 -35.952 3.457 1.00 100.26 ? 169 GLN A CA 1 ATOM 1349 C C . GLN A 1 169 ? 20.755 -35.395 2.803 1.00 96.28 ? 169 GLN A C 1 ATOM 1350 O O . GLN A 1 169 ? 21.508 -36.149 2.188 1.00 95.08 ? 169 GLN A O 1 ATOM 1351 C CB . GLN A 1 169 ? 18.383 -36.136 2.392 1.00 103.06 ? 169 GLN A CB 1 ATOM 1352 C CG . GLN A 1 169 ? 17.751 -37.520 2.346 1.00 105.09 ? 169 GLN A CG 1 ATOM 1353 C CD . GLN A 1 169 ? 17.142 -37.826 0.981 1.00 107.75 ? 169 GLN A CD 1 ATOM 1354 O OE1 . GLN A 1 169 ? 17.776 -38.456 0.129 1.00 105.39 ? 169 GLN A OE1 1 ATOM 1355 N NE2 . GLN A 1 169 ? 15.918 -37.360 0.758 1.00 109.83 ? 169 GLN A NE2 1 ATOM 1356 N N . GLU A 1 170 ? 21.002 -34.091 2.953 1.00 93.36 ? 170 GLU A N 1 ATOM 1357 C CA . GLU A 1 170 ? 22.077 -33.397 2.232 1.00 89.16 ? 170 GLU A CA 1 ATOM 1358 C C . GLU A 1 170 ? 23.314 -33.127 3.087 1.00 86.82 ? 170 GLU A C 1 ATOM 1359 O O . GLU A 1 170 ? 23.183 -32.709 4.240 1.00 87.91 ? 170 GLU A O 1 ATOM 1360 C CB . GLU A 1 170 ? 21.567 -32.054 1.710 1.00 89.10 ? 170 GLU A CB 1 ATOM 1361 C CG . GLU A 1 170 ? 20.249 -32.122 0.952 1.00 92.64 ? 170 GLU A CG 1 ATOM 1362 C CD . GLU A 1 170 ? 19.038 -31.872 1.829 1.00 95.00 ? 170 GLU A CD 1 ATOM 1363 O OE1 . GLU A 1 170 ? 19.107 -32.155 3.044 1.00 97.12 ? 170 GLU A OE1 1 ATOM 1364 O OE2 . GLU A 1 170 ? 18.014 -31.387 1.305 1.00 96.41 ? 170 GLU A OE2 1 ATOM 1365 N N . ASP A 1 171 ? 24.503 -33.368 2.516 1.00 84.80 ? 171 ASP A N 1 ATOM 1366 C CA . ASP A 1 171 ? 25.795 -32.963 3.106 1.00 81.20 ? 171 ASP A CA 1 ATOM 1367 C C . ASP A 1 171 ? 25.665 -31.593 3.758 1.00 79.17 ? 171 ASP A C 1 ATOM 1368 O O . ASP A 1 171 ? 24.952 -30.729 3.244 1.00 78.48 ? 171 ASP A O 1 ATOM 1369 C CB . ASP A 1 171 ? 26.892 -32.841 2.024 1.00 81.47 ? 171 ASP A CB 1 ATOM 1370 C CG . ASP A 1 171 ? 27.475 -34.186 1.566 1.00 82.79 ? 171 ASP A CG 1 ATOM 1371 O OD1 . ASP A 1 171 ? 27.299 -35.222 2.236 1.00 84.48 ? 171 ASP A OD1 1 ATOM 1372 O OD2 . ASP A 1 171 ? 28.147 -34.191 0.509 1.00 83.27 ? 171 ASP A OD2 1 ATOM 1373 N N . LEU A 1 172 ? 26.381 -31.381 4.860 1.00 78.43 ? 172 LEU A N 1 ATOM 1374 C CA . LEU A 1 172 ? 26.282 -30.132 5.611 1.00 78.88 ? 172 LEU A CA 1 ATOM 1375 C C . LEU A 1 172 ? 27.646 -29.479 5.873 1.00 77.06 ? 172 LEU A C 1 ATOM 1376 O O . LEU A 1 172 ? 28.554 -30.105 6.430 1.00 76.17 ? 172 LEU A O 1 ATOM 1377 C CB . LEU A 1 172 ? 25.575 -30.388 6.941 1.00 81.27 ? 172 LEU A CB 1 ATOM 1378 C CG . LEU A 1 172 ? 25.054 -29.125 7.630 1.00 84.06 ? 172 LEU A CG 1 ATOM 1379 C CD1 . LEU A 1 172 ? 23.714 -28.713 7.043 1.00 86.46 ? 172 LEU A CD1 1 ATOM 1380 C CD2 . LEU A 1 172 ? 24.920 -29.328 9.131 1.00 86.66 ? 172 LEU A CD2 1 ATOM 1381 N N . LEU A 1 173 ? 27.773 -28.211 5.487 1.00 75.61 ? 173 LEU A N 1 ATOM 1382 C CA . LEU A 1 173 ? 28.970 -27.429 5.779 1.00 74.49 ? 173 LEU A CA 1 ATOM 1383 C C . LEU A 1 173 ? 28.861 -26.805 7.157 1.00 74.87 ? 173 LEU A C 1 ATOM 1384 O O . LEU A 1 173 ? 28.034 -25.919 7.369 1.00 77.30 ? 173 LEU A O 1 ATOM 1385 C CB . LEU A 1 173 ? 29.156 -26.318 4.747 1.00 74.70 ? 173 LEU A CB 1 ATOM 1386 C CG . LEU A 1 173 ? 30.291 -25.325 5.021 1.00 73.50 ? 173 LEU A CG 1 ATOM 1387 C CD1 . LEU A 1 173 ? 31.628 -26.046 5.096 1.00 72.13 ? 173 LEU A CD1 1 ATOM 1388 C CD2 . LEU A 1 173 ? 30.320 -24.251 3.944 1.00 73.39 ? 173 LEU A CD2 1 ATOM 1389 N N . VAL A 1 174 ? 29.707 -27.254 8.081 1.00 73.92 ? 174 VAL A N 1 ATOM 1390 C CA . VAL A 1 174 ? 29.710 -26.745 9.453 1.00 72.77 ? 174 VAL A CA 1 ATOM 1391 C C . VAL A 1 174 ? 30.953 -25.889 9.684 1.00 70.64 ? 174 VAL A C 1 ATOM 1392 O O . VAL A 1 174 ? 32.070 -26.318 9.386 1.00 69.02 ? 174 VAL A O 1 ATOM 1393 C CB . VAL A 1 174 ? 29.693 -27.892 10.485 1.00 73.80 ? 174 VAL A CB 1 ATOM 1394 C CG1 . VAL A 1 174 ? 29.628 -27.338 11.903 1.00 75.40 ? 174 VAL A CG1 1 ATOM 1395 C CG2 . VAL A 1 174 ? 28.526 -28.832 10.225 1.00 75.02 ? 174 VAL A CG2 1 ATOM 1396 N N . LEU A 1 175 ? 30.740 -24.686 10.216 1.00 69.91 ? 175 LEU A N 1 ATOM 1397 C CA . LEU A 1 175 ? 31.808 -23.749 10.546 1.00 68.86 ? 175 LEU A CA 1 ATOM 1398 C C . LEU A 1 175 ? 31.886 -23.525 12.054 1.00 70.22 ? 175 LEU A C 1 ATOM 1399 O O . LEU A 1 175 ? 30.862 -23.440 12.729 1.00 70.86 ? 175 LEU A O 1 ATOM 1400 C CB . LEU A 1 175 ? 31.537 -22.402 9.884 1.00 68.91 ? 175 LEU A CB 1 ATOM 1401 C CG . LEU A 1 175 ? 31.551 -22.339 8.358 1.00 68.95 ? 175 LEU A CG 1 ATOM 1402 C CD1 . LEU A 1 175 ? 30.764 -21.126 7.886 1.00 70.19 ? 175 LEU A CD1 1 ATOM 1403 C CD2 . LEU A 1 175 ? 32.974 -22.289 7.828 1.00 66.85 ? 175 LEU A CD2 1 ATOM 1404 N N . TRP A 1 176 ? 33.104 -23.417 12.573 1.00 69.92 ? 176 TRP A N 1 ATOM 1405 C CA . TRP A 1 176 ? 33.324 -23.015 13.959 1.00 71.72 ? 176 TRP A CA 1 ATOM 1406 C C . TRP A 1 176 ? 34.663 -22.302 14.087 1.00 70.92 ? 176 TRP A C 1 ATOM 1407 O O . TRP A 1 176 ? 35.383 -22.155 13.109 1.00 69.76 ? 176 TRP A O 1 ATOM 1408 C CB . TRP A 1 176 ? 33.264 -24.230 14.892 1.00 73.61 ? 176 TRP A CB 1 ATOM 1409 C CG . TRP A 1 176 ? 34.382 -25.222 14.709 1.00 72.75 ? 176 TRP A CG 1 ATOM 1410 C CD1 . TRP A 1 176 ? 35.530 -25.315 15.447 1.00 72.73 ? 176 TRP A CD1 1 ATOM 1411 C CD2 . TRP A 1 176 ? 34.446 -26.269 13.737 1.00 70.70 ? 176 TRP A CD2 1 ATOM 1412 N NE1 . TRP A 1 176 ? 36.304 -26.353 14.989 1.00 71.27 ? 176 TRP A NE1 1 ATOM 1413 C CE2 . TRP A 1 176 ? 35.660 -26.954 13.939 1.00 70.55 ? 176 TRP A CE2 1 ATOM 1414 C CE3 . TRP A 1 176 ? 33.592 -26.696 12.716 1.00 70.32 ? 176 TRP A CE3 1 ATOM 1415 C CZ2 . TRP A 1 176 ? 36.043 -28.038 13.153 1.00 69.72 ? 176 TRP A CZ2 1 ATOM 1416 C CZ3 . TRP A 1 176 ? 33.975 -27.772 11.938 1.00 69.42 ? 176 TRP A CZ3 1 ATOM 1417 C CH2 . TRP A 1 176 ? 35.187 -28.430 12.158 1.00 68.81 ? 176 TRP A CH2 1 ATOM 1418 N N . GLY A 1 177 ? 35.000 -21.859 15.293 1.00 73.71 ? 177 GLY A N 1 ATOM 1419 C CA . GLY A 1 177 ? 36.262 -21.152 15.499 1.00 73.30 ? 177 GLY A CA 1 ATOM 1420 C C . GLY A 1 177 ? 36.827 -21.227 16.900 1.00 73.72 ? 177 GLY A C 1 ATOM 1421 O O . GLY A 1 177 ? 36.156 -21.653 17.838 1.00 73.53 ? 177 GLY A O 1 ATOM 1422 N N . ILE A 1 178 ? 38.082 -20.806 17.015 1.00 73.78 ? 178 ILE A N 1 ATOM 1423 C CA . ILE A 1 178 ? 38.770 -20.692 18.290 1.00 75.99 ? 178 ILE A CA 1 ATOM 1424 C C . ILE A 1 178 ? 39.303 -19.267 18.419 1.00 76.59 ? 178 ILE A C 1 ATOM 1425 O O . ILE A 1 178 ? 39.772 -18.685 17.441 1.00 74.78 ? 178 ILE A O 1 ATOM 1426 C CB . ILE A 1 178 ? 39.923 -21.719 18.422 1.00 76.97 ? 178 ILE A CB 1 ATOM 1427 C CG1 . ILE A 1 178 ? 40.547 -21.637 19.818 1.00 80.07 ? 178 ILE A CG1 1 ATOM 1428 C CG2 . ILE A 1 178 ? 40.993 -21.506 17.355 1.00 75.62 ? 178 ILE A CG2 1 ATOM 1429 C CD1 . ILE A 1 178 ? 41.387 -22.836 20.206 1.00 81.43 ? 178 ILE A CD1 1 ATOM 1430 N N . HIS A 1 179 ? 39.227 -18.708 19.623 1.00 78.16 ? 179 HIS A N 1 ATOM 1431 C CA . HIS A 1 179 ? 39.716 -17.359 19.872 1.00 79.81 ? 179 HIS A CA 1 ATOM 1432 C C . HIS A 1 179 ? 41.093 -17.390 20.532 1.00 81.19 ? 179 HIS A C 1 ATOM 1433 O O . HIS A 1 179 ? 41.304 -18.097 21.519 1.00 84.16 ? 179 HIS A O 1 ATOM 1434 C CB . HIS A 1 179 ? 38.728 -16.584 20.746 1.00 81.50 ? 179 HIS A CB 1 ATOM 1435 C CG . HIS A 1 179 ? 39.232 -15.243 21.179 1.00 82.78 ? 179 HIS A CG 1 ATOM 1436 N ND1 . HIS A 1 179 ? 39.434 -14.917 22.501 1.00 85.44 ? 179 HIS A ND1 1 ATOM 1437 C CD2 . HIS A 1 179 ? 39.589 -14.152 20.464 1.00 83.23 ? 179 HIS A CD2 1 ATOM 1438 C CE1 . HIS A 1 179 ? 39.882 -13.677 22.583 1.00 86.99 ? 179 HIS A CE1 1 ATOM 1439 N NE2 . HIS A 1 179 ? 39.985 -13.190 21.361 1.00 85.72 ? 179 HIS A NE2 1 ATOM 1440 N N . HIS A 1 180 ? 42.021 -16.617 19.976 1.00 81.27 ? 180 HIS A N 1 ATOM 1441 C CA . HIS A 1 180 ? 43.355 -16.458 20.534 1.00 83.01 ? 180 HIS A CA 1 ATOM 1442 C C . HIS A 1 180 ? 43.412 -15.109 21.246 1.00 86.28 ? 180 HIS A C 1 ATOM 1443 O O . HIS A 1 180 ? 43.298 -14.068 20.600 1.00 86.56 ? 180 HIS A O 1 ATOM 1444 C CB . HIS A 1 180 ? 44.406 -16.504 19.427 1.00 82.00 ? 180 HIS A CB 1 ATOM 1445 C CG . HIS A 1 180 ? 44.396 -17.778 18.641 1.00 80.88 ? 180 HIS A CG 1 ATOM 1446 N ND1 . HIS A 1 180 ? 44.537 -19.012 19.233 1.00 81.89 ? 180 HIS A ND1 1 ATOM 1447 C CD2 . HIS A 1 180 ? 44.260 -18.012 17.315 1.00 79.52 ? 180 HIS A CD2 1 ATOM 1448 C CE1 . HIS A 1 180 ? 44.491 -19.953 18.307 1.00 79.51 ? 180 HIS A CE1 1 ATOM 1449 N NE2 . HIS A 1 180 ? 44.322 -19.373 17.135 1.00 78.73 ? 180 HIS A NE2 1 ATOM 1450 N N . PRO A 1 181 ? 43.570 -15.115 22.580 1.00 88.27 ? 181 PRO A N 1 ATOM 1451 C CA . PRO A 1 181 ? 43.632 -13.840 23.297 1.00 91.18 ? 181 PRO A CA 1 ATOM 1452 C C . PRO A 1 181 ? 45.022 -13.191 23.310 1.00 91.18 ? 181 PRO A C 1 ATOM 1453 O O . PRO A 1 181 ? 46.028 -13.848 23.035 1.00 88.16 ? 181 PRO A O 1 ATOM 1454 C CB . PRO A 1 181 ? 43.198 -14.207 24.730 1.00 94.14 ? 181 PRO A CB 1 ATOM 1455 C CG . PRO A 1 181 ? 42.947 -15.683 24.740 1.00 92.90 ? 181 PRO A CG 1 ATOM 1456 C CD . PRO A 1 181 ? 43.557 -16.260 23.502 1.00 89.45 ? 181 PRO A CD 1 ATOM 1457 N N . LYS A 1 182 ? 45.044 -11.903 23.649 1.00 93.19 ? 182 LYS A N 1 ATOM 1458 C CA . LYS A 1 182 ? 46.267 -11.100 23.733 1.00 94.64 ? 182 LYS A CA 1 ATOM 1459 C C . LYS A 1 182 ? 47.266 -11.624 24.775 1.00 96.00 ? 182 LYS A C 1 ATOM 1460 O O . LYS A 1 182 ? 48.455 -11.762 24.476 1.00 95.27 ? 182 LYS A O 1 ATOM 1461 C CB . LYS A 1 182 ? 45.884 -9.649 24.050 1.00 97.77 ? 182 LYS A CB 1 ATOM 1462 C CG . LYS A 1 182 ? 47.034 -8.712 24.389 1.00 101.21 ? 182 LYS A CG 1 ATOM 1463 C CD . LYS A 1 182 ? 46.503 -7.433 25.015 1.00 104.83 ? 182 LYS A CD 1 ATOM 1464 C CE . LYS A 1 182 ? 47.608 -6.585 25.626 1.00 108.87 ? 182 LYS A CE 1 ATOM 1465 N NZ . LYS A 1 182 ? 48.329 -5.781 24.602 1.00 109.30 ? 182 LYS A NZ 1 ATOM 1466 N N . ASP A 1 183 ? 46.782 -11.900 25.989 1.00 97.76 ? 183 ASP A N 1 ATOM 1467 C CA . ASP A 1 183 ? 47.645 -12.346 27.099 1.00 100.21 ? 183 ASP A CA 1 ATOM 1468 C C . ASP A 1 183 ? 46.883 -13.138 28.184 1.00 100.41 ? 183 ASP A C 1 ATOM 1469 O O . ASP A 1 183 ? 45.672 -13.348 28.079 1.00 99.18 ? 183 ASP A O 1 ATOM 1470 C CB . ASP A 1 183 ? 48.394 -11.143 27.716 1.00 103.04 ? 183 ASP A CB 1 ATOM 1471 C CG . ASP A 1 183 ? 47.457 -10.072 28.263 1.00 104.90 ? 183 ASP A CG 1 ATOM 1472 O OD1 . ASP A 1 183 ? 46.327 -10.408 28.674 1.00 105.08 ? 183 ASP A OD1 1 ATOM 1473 O OD2 . ASP A 1 183 ? 47.860 -8.887 28.290 1.00 106.08 ? 183 ASP A OD2 1 ATOM 1474 N N . ALA A 1 184 ? 47.604 -13.571 29.218 1.00 101.35 ? 184 ALA A N 1 ATOM 1475 C CA . ALA A 1 184 ? 47.027 -14.388 30.295 1.00 102.69 ? 184 ALA A CA 1 ATOM 1476 C C . ALA A 1 184 ? 45.844 -13.731 31.020 1.00 104.44 ? 184 ALA A C 1 ATOM 1477 O O . ALA A 1 184 ? 44.926 -14.423 31.471 1.00 104.14 ? 184 ALA A O 1 ATOM 1478 C CB . ALA A 1 184 ? 48.108 -14.765 31.301 1.00 104.40 ? 184 ALA A CB 1 ATOM 1479 N N . ALA A 1 185 ? 45.874 -12.405 31.139 1.00 105.68 ? 185 ALA A N 1 ATOM 1480 C CA . ALA A 1 185 ? 44.816 -11.662 31.827 1.00 107.23 ? 185 ALA A CA 1 ATOM 1481 C C . ALA A 1 185 ? 43.508 -11.684 31.037 1.00 104.20 ? 185 ALA A C 1 ATOM 1482 O O . ALA A 1 185 ? 42.429 -11.851 31.606 1.00 103.73 ? 185 ALA A O 1 ATOM 1483 C CB . ALA A 1 185 ? 45.256 -10.227 32.082 1.00 109.76 ? 185 ALA A CB 1 ATOM 1484 N N . GLU A 1 186 ? 43.610 -11.522 29.724 1.00 101.84 ? 186 GLU A N 1 ATOM 1485 C CA . GLU A 1 186 ? 42.434 -11.546 28.857 1.00 100.20 ? 186 GLU A CA 1 ATOM 1486 C C . GLU A 1 186 ? 41.767 -12.924 28.864 1.00 97.35 ? 186 GLU A C 1 ATOM 1487 O O . GLU A 1 186 ? 40.540 -13.027 28.859 1.00 96.00 ? 186 GLU A O 1 ATOM 1488 C CB . GLU A 1 186 ? 42.821 -11.151 27.435 1.00 99.11 ? 186 GLU A CB 1 ATOM 1489 C CG . GLU A 1 186 ? 41.648 -10.735 26.564 1.00 99.19 ? 186 GLU A CG 1 ATOM 1490 C CD . GLU A 1 186 ? 42.099 -10.162 25.236 1.00 97.98 ? 186 GLU A CD 1 ATOM 1491 O OE1 . GLU A 1 186 ? 42.426 -10.950 24.317 1.00 96.89 ? 186 GLU A OE1 1 ATOM 1492 O OE2 . GLU A 1 186 ? 42.122 -8.920 25.112 1.00 99.25 ? 186 GLU A OE2 1 ATOM 1493 N N . GLN A 1 187 ? 42.586 -13.972 28.885 1.00 96.03 ? 187 GLN A N 1 ATOM 1494 C CA . GLN A 1 187 ? 42.102 -15.352 28.944 1.00 95.41 ? 187 GLN A CA 1 ATOM 1495 C C . GLN A 1 187 ? 41.163 -15.571 30.138 1.00 98.31 ? 187 GLN A C 1 ATOM 1496 O O . GLN A 1 187 ? 40.012 -15.980 29.968 1.00 97.81 ? 187 GLN A O 1 ATOM 1497 C CB . GLN A 1 187 ? 43.298 -16.316 29.009 1.00 94.43 ? 187 GLN A CB 1 ATOM 1498 C CG . GLN A 1 187 ? 42.955 -17.786 29.215 1.00 93.26 ? 187 GLN A CG 1 ATOM 1499 C CD . GLN A 1 187 ? 42.162 -18.380 28.067 1.00 90.27 ? 187 GLN A CD 1 ATOM 1500 O OE1 . GLN A 1 187 ? 42.447 -18.119 26.896 1.00 87.44 ? 187 GLN A OE1 1 ATOM 1501 N NE2 . GLN A 1 187 ? 41.171 -19.202 28.400 1.00 89.92 ? 187 GLN A NE2 1 ATOM 1502 N N . THR A 1 188 ? 41.656 -15.288 31.340 1.00 101.76 ? 188 THR A N 1 ATOM 1503 C CA . THR A 1 188 ? 40.850 -15.451 32.550 1.00 104.57 ? 188 THR A CA 1 ATOM 1504 C C . THR A 1 188 ? 39.677 -14.463 32.574 1.00 105.70 ? 188 THR A C 1 ATOM 1505 O O . THR A 1 188 ? 38.583 -14.806 33.025 1.00 106.76 ? 188 THR A O 1 ATOM 1506 C CB . THR A 1 188 ? 41.692 -15.284 33.833 1.00 107.93 ? 188 THR A CB 1 ATOM 1507 O OG1 . THR A 1 188 ? 42.228 -13.958 33.892 1.00 110.71 ? 188 THR A OG1 1 ATOM 1508 C CG2 . THR A 1 188 ? 42.834 -16.297 33.871 1.00 107.15 ? 188 THR A CG2 1 ATOM 1509 N N . LYS A 1 189 ? 39.904 -13.249 32.075 1.00 105.12 ? 189 LYS A N 1 ATOM 1510 C CA . LYS A 1 189 ? 38.858 -12.228 32.016 1.00 106.61 ? 189 LYS A CA 1 ATOM 1511 C C . LYS A 1 189 ? 37.625 -12.690 31.219 1.00 105.93 ? 189 LYS A C 1 ATOM 1512 O O . LYS A 1 189 ? 36.494 -12.376 31.594 1.00 107.78 ? 189 LYS A O 1 ATOM 1513 C CB . LYS A 1 189 ? 39.420 -10.933 31.422 1.00 106.58 ? 189 LYS A CB 1 ATOM 1514 C CG . LYS A 1 189 ? 38.441 -9.770 31.391 1.00 109.18 ? 189 LYS A CG 1 ATOM 1515 C CD . LYS A 1 189 ? 38.946 -8.645 30.502 1.00 109.43 ? 189 LYS A CD 1 ATOM 1516 C CE . LYS A 1 189 ? 37.851 -7.630 30.218 1.00 111.31 ? 189 LYS A CE 1 ATOM 1517 N NZ . LYS A 1 189 ? 38.201 -6.735 29.081 1.00 109.98 ? 189 LYS A NZ 1 ATOM 1518 N N . LEU A 1 190 ? 37.841 -13.434 30.135 1.00 102.56 ? 190 LEU A N 1 ATOM 1519 C CA . LEU A 1 190 ? 36.739 -13.905 29.290 1.00 102.16 ? 190 LEU A CA 1 ATOM 1520 C C . LEU A 1 190 ? 36.264 -15.311 29.646 1.00 101.61 ? 190 LEU A C 1 ATOM 1521 O O . LEU A 1 190 ? 35.063 -15.585 29.628 1.00 102.36 ? 190 LEU A O 1 ATOM 1522 C CB . LEU A 1 190 ? 37.146 -13.890 27.810 1.00 99.74 ? 190 LEU A CB 1 ATOM 1523 C CG . LEU A 1 190 ? 37.710 -12.589 27.235 1.00 100.55 ? 190 LEU A CG 1 ATOM 1524 C CD1 . LEU A 1 190 ? 37.802 -12.694 25.722 1.00 98.03 ? 190 LEU A CD1 1 ATOM 1525 C CD2 . LEU A 1 190 ? 36.884 -11.378 27.642 1.00 103.60 ? 190 LEU A CD2 1 ATOM 1526 N N . TYR A 1 191 ? 37.206 -16.201 29.949 1.00 100.61 ? 191 TYR A N 1 ATOM 1527 C CA . TYR A 1 191 ? 36.907 -17.630 30.062 1.00 99.30 ? 191 TYR A CA 1 ATOM 1528 C C . TYR A 1 191 ? 37.218 -18.253 31.429 1.00 101.69 ? 191 TYR A C 1 ATOM 1529 O O . TYR A 1 191 ? 36.912 -19.425 31.650 1.00 101.95 ? 191 TYR A O 1 ATOM 1530 C CB . TYR A 1 191 ? 37.664 -18.390 28.968 1.00 96.17 ? 191 TYR A CB 1 ATOM 1531 C CG . TYR A 1 191 ? 37.575 -17.743 27.596 1.00 93.28 ? 191 TYR A CG 1 ATOM 1532 C CD1 . TYR A 1 191 ? 36.369 -17.707 26.898 1.00 92.17 ? 191 TYR A CD1 1 ATOM 1533 C CD2 . TYR A 1 191 ? 38.693 -17.154 27.005 1.00 91.38 ? 191 TYR A CD2 1 ATOM 1534 C CE1 . TYR A 1 191 ? 36.281 -17.116 25.648 1.00 89.77 ? 191 TYR A CE1 1 ATOM 1535 C CE2 . TYR A 1 191 ? 38.611 -16.557 25.760 1.00 89.32 ? 191 TYR A CE2 1 ATOM 1536 C CZ . TYR A 1 191 ? 37.402 -16.543 25.087 1.00 88.28 ? 191 TYR A CZ 1 ATOM 1537 O OH . TYR A 1 191 ? 37.311 -15.953 23.855 1.00 85.90 ? 191 TYR A OH 1 ATOM 1538 N N . GLN A 1 192 ? 37.821 -17.483 32.336 1.00 103.88 ? 192 GLN A N 1 ATOM 1539 C CA . GLN A 1 192 ? 38.185 -17.959 33.680 1.00 106.23 ? 192 GLN A CA 1 ATOM 1540 C C . GLN A 1 192 ? 39.320 -18.992 33.657 1.00 104.41 ? 192 GLN A C 1 ATOM 1541 O O . GLN A 1 192 ? 40.412 -18.729 34.167 1.00 105.57 ? 192 GLN A O 1 ATOM 1542 C CB . GLN A 1 192 ? 36.959 -18.518 34.426 1.00 108.29 ? 192 GLN A CB 1 ATOM 1543 C CG . GLN A 1 192 ? 37.077 -18.469 35.944 1.00 111.88 ? 192 GLN A CG 1 ATOM 1544 C CD . GLN A 1 192 ? 36.835 -17.081 36.514 1.00 114.80 ? 192 GLN A CD 1 ATOM 1545 O OE1 . GLN A 1 192 ? 35.922 -16.375 36.091 1.00 115.33 ? 192 GLN A OE1 1 ATOM 1546 N NE2 . GLN A 1 192 ? 37.650 -16.687 37.485 1.00 117.48 ? 192 GLN A NE2 1 ATOM 1547 N N . ASN A 1 193 ? 39.055 -20.158 33.069 1.00 101.57 ? 193 ASN A N 1 ATOM 1548 C CA . ASN A 1 193 ? 40.030 -21.246 33.003 1.00 100.22 ? 193 ASN A CA 1 ATOM 1549 C C . ASN A 1 193 ? 41.281 -20.810 32.238 1.00 99.13 ? 193 ASN A C 1 ATOM 1550 O O . ASN A 1 193 ? 41.169 -20.298 31.126 1.00 98.00 ? 193 ASN A O 1 ATOM 1551 C CB . ASN A 1 193 ? 39.404 -22.474 32.333 1.00 98.02 ? 193 ASN A CB 1 ATOM 1552 C CG . ASN A 1 193 ? 38.170 -22.975 33.066 1.00 99.23 ? 193 ASN A CG 1 ATOM 1553 O OD1 . ASN A 1 193 ? 38.148 -23.029 34.296 1.00 103.70 ? 193 ASN A OD1 1 ATOM 1554 N ND2 . ASN A 1 193 ? 37.136 -23.336 32.317 1.00 96.27 ? 193 ASN A ND2 1 ATOM 1555 N N . PRO A 1 194 ? 42.474 -20.999 32.832 1.00 100.61 ? 194 PRO A N 1 ATOM 1556 C CA . PRO A 1 194 ? 43.700 -20.493 32.217 1.00 99.90 ? 194 PRO A CA 1 ATOM 1557 C C . PRO A 1 194 ? 44.208 -21.349 31.055 1.00 97.49 ? 194 PRO A C 1 ATOM 1558 O O . PRO A 1 194 ? 44.767 -20.809 30.102 1.00 95.34 ? 194 PRO A O 1 ATOM 1559 C CB . PRO A 1 194 ? 44.698 -20.510 33.375 1.00 102.30 ? 194 PRO A CB 1 ATOM 1560 C CG . PRO A 1 194 ? 44.251 -21.647 34.221 1.00 103.54 ? 194 PRO A CG 1 ATOM 1561 C CD . PRO A 1 194 ? 42.751 -21.698 34.101 1.00 103.43 ? 194 PRO A CD 1 ATOM 1562 N N . THR A 1 195 ? 44.022 -22.665 31.142 1.00 97.44 ? 195 THR A N 1 ATOM 1563 C CA . THR A 1 195 ? 44.455 -23.589 30.096 1.00 94.73 ? 195 THR A CA 1 ATOM 1564 C C . THR A 1 195 ? 43.229 -24.295 29.522 1.00 93.17 ? 195 THR A C 1 ATOM 1565 O O . THR A 1 195 ? 42.541 -25.030 30.231 1.00 94.07 ? 195 THR A O 1 ATOM 1566 C CB . THR A 1 195 ? 45.443 -24.635 30.653 1.00 95.66 ? 195 THR A CB 1 ATOM 1567 O OG1 . THR A 1 195 ? 46.377 -23.997 31.527 1.00 96.63 ? 195 THR A OG1 1 ATOM 1568 C CG2 . THR A 1 195 ? 46.205 -25.317 29.526 1.00 94.08 ? 195 THR A CG2 1 ATOM 1569 N N . THR A 1 196 ? 42.963 -24.072 28.238 1.00 91.64 ? 196 THR A N 1 ATOM 1570 C CA . THR A 1 196 ? 41.716 -24.518 27.616 1.00 90.39 ? 196 THR A CA 1 ATOM 1571 C C . THR A 1 196 ? 41.953 -25.290 26.320 1.00 87.60 ? 196 THR A C 1 ATOM 1572 O O . THR A 1 196 ? 43.092 -25.463 25.885 1.00 85.25 ? 196 THR A O 1 ATOM 1573 C CB . THR A 1 196 ? 40.798 -23.315 27.322 1.00 90.48 ? 196 THR A CB 1 ATOM 1574 O OG1 . THR A 1 196 ? 41.511 -22.358 26.532 1.00 89.47 ? 196 THR A OG1 1 ATOM 1575 C CG2 . THR A 1 196 ? 40.349 -22.663 28.614 1.00 93.66 ? 196 THR A CG2 1 ATOM 1576 N N . TYR A 1 197 ? 40.861 -25.761 25.722 1.00 86.81 ? 197 TYR A N 1 ATOM 1577 C CA . TYR A 1 197 ? 40.907 -26.515 24.481 1.00 83.82 ? 197 TYR A CA 1 ATOM 1578 C C . TYR A 1 197 ? 39.537 -26.557 23.825 1.00 83.83 ? 197 TYR A C 1 ATOM 1579 O O . TYR A 1 197 ? 38.529 -26.218 24.440 1.00 83.54 ? 197 TYR A O 1 ATOM 1580 C CB . TYR A 1 197 ? 41.361 -27.952 24.748 1.00 84.10 ? 197 TYR A CB 1 ATOM 1581 C CG . TYR A 1 197 ? 40.371 -28.763 25.562 1.00 85.38 ? 197 TYR A CG 1 ATOM 1582 C CD1 . TYR A 1 197 ? 40.337 -28.665 26.952 1.00 88.37 ? 197 TYR A CD1 1 ATOM 1583 C CD2 . TYR A 1 197 ? 39.468 -29.623 24.942 1.00 84.21 ? 197 TYR A CD2 1 ATOM 1584 C CE1 . TYR A 1 197 ? 39.435 -29.404 27.699 1.00 89.96 ? 197 TYR A CE1 1 ATOM 1585 C CE2 . TYR A 1 197 ? 38.561 -30.366 25.679 1.00 85.93 ? 197 TYR A CE2 1 ATOM 1586 C CZ . TYR A 1 197 ? 38.547 -30.253 27.059 1.00 89.59 ? 197 TYR A CZ 1 ATOM 1587 O OH . TYR A 1 197 ? 37.645 -30.989 27.804 1.00 91.62 ? 197 TYR A OH 1 ATOM 1588 N N . ILE A 1 198 ? 39.519 -26.973 22.564 1.00 83.68 ? 198 ILE A N 1 ATOM 1589 C CA . ILE A 1 198 ? 38.284 -27.304 21.865 1.00 83.78 ? 198 ILE A CA 1 ATOM 1590 C C . ILE A 1 198 ? 38.526 -28.613 21.137 1.00 82.86 ? 198 ILE A C 1 ATOM 1591 O O . ILE A 1 198 ? 39.438 -28.703 20.316 1.00 82.59 ? 198 ILE A O 1 ATOM 1592 C CB . ILE A 1 198 ? 37.898 -26.230 20.833 1.00 83.28 ? 198 ILE A CB 1 ATOM 1593 C CG1 . ILE A 1 198 ? 37.654 -24.882 21.512 1.00 84.82 ? 198 ILE A CG1 1 ATOM 1594 C CG2 . ILE A 1 198 ? 36.653 -26.652 20.063 1.00 83.34 ? 198 ILE A CG2 1 ATOM 1595 C CD1 . ILE A 1 198 ? 37.852 -23.710 20.580 1.00 84.63 ? 198 ILE A CD1 1 ATOM 1596 N N . SER A 1 199 ? 37.722 -29.626 21.446 1.00 83.35 ? 199 SER A N 1 ATOM 1597 C CA . SER A 1 199 ? 37.827 -30.916 20.778 1.00 82.42 ? 199 SER A CA 1 ATOM 1598 C C . SER A 1 199 ? 36.604 -31.136 19.893 1.00 80.87 ? 199 SER A C 1 ATOM 1599 O O . SER A 1 199 ? 35.472 -30.978 20.345 1.00 80.54 ? 199 SER A O 1 ATOM 1600 C CB . SER A 1 199 ? 37.976 -32.047 21.801 1.00 84.56 ? 199 SER A CB 1 ATOM 1601 O OG . SER A 1 199 ? 36.740 -32.364 22.411 1.00 87.09 ? 199 SER A OG 1 ATOM 1602 N N . VAL A 1 200 ? 36.847 -31.492 18.632 1.00 80.09 ? 200 VAL A N 1 ATOM 1603 C CA . VAL A 1 200 ? 35.784 -31.687 17.647 1.00 79.28 ? 200 VAL A CA 1 ATOM 1604 C C . VAL A 1 200 ? 35.940 -33.054 17.001 1.00 79.36 ? 200 VAL A C 1 ATOM 1605 O O . VAL A 1 200 ? 37.027 -33.403 16.535 1.00 79.56 ? 200 VAL A O 1 ATOM 1606 C CB . VAL A 1 200 ? 35.824 -30.616 16.535 1.00 78.32 ? 200 VAL A CB 1 ATOM 1607 C CG1 . VAL A 1 200 ? 34.559 -30.677 15.689 1.00 78.96 ? 200 VAL A CG1 1 ATOM 1608 C CG2 . VAL A 1 200 ? 35.993 -29.224 17.127 1.00 78.73 ? 200 VAL A CG2 1 ATOM 1609 N N . GLY A 1 201 ? 34.851 -33.815 16.955 1.00 80.14 ? 201 GLY A N 1 ATOM 1610 C CA . GLY A 1 201 ? 34.876 -35.156 16.387 1.00 80.27 ? 201 GLY A CA 1 ATOM 1611 C C . GLY A 1 201 ? 33.691 -35.449 15.489 1.00 80.62 ? 201 GLY A C 1 ATOM 1612 O O . GLY A 1 201 ? 32.567 -35.058 15.785 1.00 82.86 ? 201 GLY A O 1 ATOM 1613 N N . THR A 1 202 ? 33.964 -36.121 14.375 1.00 80.46 ? 202 THR A N 1 ATOM 1614 C CA . THR A 1 202 ? 32.939 -36.743 13.541 1.00 80.70 ? 202 THR A CA 1 ATOM 1615 C C . THR A 1 202 ? 33.403 -38.178 13.345 1.00 82.45 ? 202 THR A C 1 ATOM 1616 O O . THR A 1 202 ? 34.243 -38.666 14.106 1.00 83.65 ? 202 THR A O 1 ATOM 1617 C CB . THR A 1 202 ? 32.787 -36.039 12.171 1.00 79.13 ? 202 THR A CB 1 ATOM 1618 O OG1 . THR A 1 202 ? 33.928 -36.318 11.343 1.00 76.65 ? 202 THR A OG1 1 ATOM 1619 C CG2 . THR A 1 202 ? 32.634 -34.539 12.343 1.00 77.93 ? 202 THR A CG2 1 ATOM 1620 N N . SER A 1 203 ? 32.875 -38.855 12.333 1.00 83.71 ? 203 SER A N 1 ATOM 1621 C CA . SER A 1 203 ? 33.373 -40.180 11.973 1.00 85.09 ? 203 SER A CA 1 ATOM 1622 C C . SER A 1 203 ? 34.773 -40.097 11.363 1.00 84.37 ? 203 SER A C 1 ATOM 1623 O O . SER A 1 203 ? 35.558 -41.036 11.483 1.00 85.68 ? 203 SER A O 1 ATOM 1624 C CB . SER A 1 203 ? 32.419 -40.860 10.994 1.00 85.91 ? 203 SER A CB 1 ATOM 1625 O OG . SER A 1 203 ? 32.187 -40.033 9.873 1.00 84.65 ? 203 SER A OG 1 ATOM 1626 N N . THR A 1 204 ? 35.078 -38.979 10.706 1.00 82.95 ? 204 THR A N 1 ATOM 1627 C CA . THR A 1 204 ? 36.379 -38.784 10.060 1.00 82.17 ? 204 THR A CA 1 ATOM 1628 C C . THR A 1 204 ? 37.274 -37.831 10.845 1.00 81.28 ? 204 THR A C 1 ATOM 1629 O O . THR A 1 204 ? 38.484 -38.036 10.917 1.00 84.05 ? 204 THR A O 1 ATOM 1630 C CB . THR A 1 204 ? 36.227 -38.241 8.622 1.00 80.32 ? 204 THR A CB 1 ATOM 1631 O OG1 . THR A 1 204 ? 35.669 -36.920 8.650 1.00 79.13 ? 204 THR A OG1 1 ATOM 1632 C CG2 . THR A 1 204 ? 35.332 -39.152 7.797 1.00 80.71 ? 204 THR A CG2 1 ATOM 1633 N N . LEU A 1 205 ? 36.679 -36.797 11.431 1.00 79.69 ? 205 LEU A N 1 ATOM 1634 C CA . LEU A 1 205 ? 37.439 -35.751 12.104 1.00 78.33 ? 205 LEU A CA 1 ATOM 1635 C C . LEU A 1 205 ? 37.882 -36.140 13.528 1.00 78.86 ? 205 LEU A C 1 ATOM 1636 O O . LEU A 1 205 ? 37.104 -36.723 14.297 1.00 78.53 ? 205 LEU A O 1 ATOM 1637 C CB . LEU A 1 205 ? 36.604 -34.468 12.144 1.00 79.13 ? 205 LEU A CB 1 ATOM 1638 C CG . LEU A 1 205 ? 37.340 -33.162 12.452 1.00 79.78 ? 205 LEU A CG 1 ATOM 1639 C CD1 . LEU A 1 205 ? 38.429 -32.895 11.423 1.00 78.30 ? 205 LEU A CD1 1 ATOM 1640 C CD2 . LEU A 1 205 ? 36.356 -32.002 12.503 1.00 79.77 ? 205 LEU A CD2 1 ATOM 1641 N N . ASN A 1 206 ? 39.135 -35.815 13.861 1.00 76.70 ? 206 ASN A N 1 ATOM 1642 C CA . ASN A 1 206 ? 39.665 -35.985 15.217 1.00 76.95 ? 206 ASN A CA 1 ATOM 1643 C C . ASN A 1 206 ? 40.544 -34.806 15.631 1.00 75.63 ? 206 ASN A C 1 ATOM 1644 O O . ASN A 1 206 ? 41.769 -34.917 15.701 1.00 74.20 ? 206 ASN A O 1 ATOM 1645 C CB . ASN A 1 206 ? 40.455 -37.290 15.339 1.00 78.28 ? 206 ASN A CB 1 ATOM 1646 C CG . ASN A 1 206 ? 40.893 -37.573 16.767 1.00 79.44 ? 206 ASN A CG 1 ATOM 1647 O OD1 . ASN A 1 206 ? 40.208 -37.209 17.722 1.00 79.22 ? 206 ASN A OD1 1 ATOM 1648 N ND2 . ASN A 1 206 ? 42.044 -38.216 16.918 1.00 80.98 ? 206 ASN A ND2 1 ATOM 1649 N N . GLN A 1 207 ? 39.896 -33.688 15.936 1.00 75.24 ? 207 GLN A N 1 ATOM 1650 C CA . GLN A 1 207 ? 40.580 -32.424 16.171 1.00 75.29 ? 207 GLN A CA 1 ATOM 1651 C C . GLN A 1 207 ? 40.642 -32.067 17.658 1.00 78.79 ? 207 GLN A C 1 ATOM 1652 O O . GLN A 1 207 ? 39.741 -32.398 18.431 1.00 79.95 ? 207 GLN A O 1 ATOM 1653 C CB . GLN A 1 207 ? 39.852 -31.328 15.395 1.00 73.71 ? 207 GLN A CB 1 ATOM 1654 C CG . GLN A 1 207 ? 40.398 -29.925 15.569 1.00 73.64 ? 207 GLN A CG 1 ATOM 1655 C CD . GLN A 1 207 ? 39.643 -28.919 14.720 1.00 74.11 ? 207 GLN A CD 1 ATOM 1656 O OE1 . GLN A 1 207 ? 38.886 -28.097 15.237 1.00 75.34 ? 207 GLN A OE1 1 ATOM 1657 N NE2 . GLN A 1 207 ? 39.835 -28.990 13.406 1.00 73.46 ? 207 GLN A NE2 1 ATOM 1658 N N . ARG A 1 208 ? 41.726 -31.405 18.052 1.00 80.39 ? 208 ARG A N 1 ATOM 1659 C CA . ARG A 1 208 ? 41.809 -30.762 19.357 1.00 83.08 ? 208 ARG A CA 1 ATOM 1660 C C . ARG A 1 208 ? 42.620 -29.479 19.222 1.00 82.91 ? 208 ARG A C 1 ATOM 1661 O O . ARG A 1 208 ? 43.829 -29.522 19.007 1.00 83.73 ? 208 ARG A O 1 ATOM 1662 C CB . ARG A 1 208 ? 42.448 -31.678 20.399 1.00 86.63 ? 208 ARG A CB 1 ATOM 1663 C CG . ARG A 1 208 ? 42.231 -31.214 21.834 1.00 89.76 ? 208 ARG A CG 1 ATOM 1664 C CD . ARG A 1 208 ? 43.191 -31.895 22.797 1.00 92.89 ? 208 ARG A CD 1 ATOM 1665 N NE . ARG A 1 208 ? 42.795 -31.712 24.194 1.00 95.87 ? 208 ARG A NE 1 ATOM 1666 C CZ . ARG A 1 208 ? 41.854 -32.419 24.822 1.00 98.81 ? 208 ARG A CZ 1 ATOM 1667 N NH1 . ARG A 1 208 ? 41.179 -33.378 24.191 1.00 99.21 ? 208 ARG A NH1 1 ATOM 1668 N NH2 . ARG A 1 208 ? 41.578 -32.164 26.098 1.00 101.72 ? 208 ARG A NH2 1 ATOM 1669 N N . LEU A 1 209 ? 41.944 -28.342 19.340 1.00 82.72 ? 209 LEU A N 1 ATOM 1670 C CA . LEU A 1 209 ? 42.592 -27.048 19.216 1.00 82.29 ? 209 LEU A CA 1 ATOM 1671 C C . LEU A 1 209 ? 42.960 -26.534 20.601 1.00 84.19 ? 209 LEU A C 1 ATOM 1672 O O . LEU A 1 209 ? 42.267 -26.812 21.576 1.00 84.72 ? 209 LEU A O 1 ATOM 1673 C CB . LEU A 1 209 ? 41.660 -26.051 18.518 1.00 82.06 ? 209 LEU A CB 1 ATOM 1674 C CG . LEU A 1 209 ? 41.030 -26.491 17.188 1.00 81.54 ? 209 LEU A CG 1 ATOM 1675 C CD1 . LEU A 1 209 ? 39.955 -25.503 16.756 1.00 81.41 ? 209 LEU A CD1 1 ATOM 1676 C CD2 . LEU A 1 209 ? 42.082 -26.655 16.099 1.00 80.02 ? 209 LEU A CD2 1 ATOM 1677 N N . VAL A 1 210 ? 44.067 -25.802 20.679 1.00 85.80 ? 210 VAL A N 1 ATOM 1678 C CA . VAL A 1 210 ? 44.451 -25.088 21.893 1.00 88.95 ? 210 VAL A CA 1 ATOM 1679 C C . VAL A 1 210 ? 44.787 -23.646 21.520 1.00 88.54 ? 210 VAL A C 1 ATOM 1680 O O . VAL A 1 210 ? 45.403 -23.407 20.479 1.00 86.97 ? 210 VAL A O 1 ATOM 1681 C CB . VAL A 1 210 ? 45.649 -25.746 22.629 1.00 91.11 ? 210 VAL A CB 1 ATOM 1682 C CG1 . VAL A 1 210 ? 45.221 -27.053 23.274 1.00 91.84 ? 210 VAL A CG1 1 ATOM 1683 C CG2 . VAL A 1 210 ? 46.833 -25.976 21.697 1.00 90.76 ? 210 VAL A CG2 1 ATOM 1684 N N . PRO A 1 211 ? 44.374 -22.677 22.355 1.00 90.79 ? 211 PRO A N 1 ATOM 1685 C CA . PRO A 1 211 ? 44.673 -21.292 22.001 1.00 91.74 ? 211 PRO A CA 1 ATOM 1686 C C . PRO A 1 211 ? 46.155 -20.967 22.146 1.00 91.67 ? 211 PRO A C 1 ATOM 1687 O O . PRO A 1 211 ? 46.777 -21.312 23.150 1.00 92.38 ? 211 PRO A O 1 ATOM 1688 C CB . PRO A 1 211 ? 43.840 -20.465 22.996 1.00 93.99 ? 211 PRO A CB 1 ATOM 1689 C CG . PRO A 1 211 ? 42.975 -21.433 23.727 1.00 94.25 ? 211 PRO A CG 1 ATOM 1690 C CD . PRO A 1 211 ? 43.633 -22.771 23.623 1.00 93.01 ? 211 PRO A CD 1 ATOM 1691 N N . ARG A 1 212 ? 46.709 -20.340 21.120 1.00 91.48 ? 212 ARG A N 1 ATOM 1692 C CA . ARG A 1 212 ? 48.061 -19.822 21.149 1.00 94.33 ? 212 ARG A CA 1 ATOM 1693 C C . ARG A 1 212 ? 48.036 -18.361 21.591 1.00 96.12 ? 212 ARG A C 1 ATOM 1694 O O . ARG A 1 212 ? 47.453 -17.509 20.918 1.00 93.48 ? 212 ARG A O 1 ATOM 1695 C CB . ARG A 1 212 ? 48.704 -19.974 19.762 1.00 94.00 ? 212 ARG A CB 1 ATOM 1696 C CG . ARG A 1 212 ? 49.361 -21.333 19.546 1.00 94.71 ? 212 ARG A CG 1 ATOM 1697 C CD . ARG A 1 212 ? 48.898 -22.055 18.290 1.00 94.03 ? 212 ARG A CD 1 ATOM 1698 N NE . ARG A 1 212 ? 49.083 -21.273 17.066 1.00 92.75 ? 212 ARG A NE 1 ATOM 1699 C CZ . ARG A 1 212 ? 48.145 -21.061 16.141 1.00 93.33 ? 212 ARG A CZ 1 ATOM 1700 N NH1 . ARG A 1 212 ? 46.922 -21.574 16.260 1.00 91.99 ? 212 ARG A NH1 1 ATOM 1701 N NH2 . ARG A 1 212 ? 48.435 -20.332 15.069 1.00 95.35 ? 212 ARG A NH2 1 ATOM 1702 N N . ILE A 1 213 ? 48.646 -18.088 22.742 1.00 100.52 ? 213 ILE A N 1 ATOM 1703 C CA . ILE A 1 213 ? 48.840 -16.718 23.204 1.00 104.02 ? 213 ILE A CA 1 ATOM 1704 C C . ILE A 1 213 ? 50.142 -16.184 22.610 1.00 105.57 ? 213 ILE A C 1 ATOM 1705 O O . ILE A 1 213 ? 51.134 -16.915 22.502 1.00 104.80 ? 213 ILE A O 1 ATOM 1706 C CB . ILE A 1 213 ? 48.893 -16.612 24.748 1.00 105.84 ? 213 ILE A CB 1 ATOM 1707 C CG1 . ILE A 1 213 ? 47.543 -17.003 25.370 1.00 107.03 ? 213 ILE A CG1 1 ATOM 1708 C CG2 . ILE A 1 213 ? 49.272 -15.199 25.175 1.00 107.14 ? 213 ILE A CG2 1 ATOM 1709 C CD1 . ILE A 1 213 ? 47.439 -18.461 25.763 1.00 107.71 ? 213 ILE A CD1 1 ATOM 1710 N N . ALA A 1 214 ? 50.116 -14.911 22.216 1.00 106.36 ? 214 ALA A N 1 ATOM 1711 C CA . ALA A 1 214 ? 51.302 -14.197 21.746 1.00 106.06 ? 214 ALA A CA 1 ATOM 1712 C C . ALA A 1 214 ? 50.994 -12.709 21.625 1.00 106.23 ? 214 ALA A C 1 ATOM 1713 O O . ALA A 1 214 ? 49.849 -12.320 21.378 1.00 104.17 ? 214 ALA A O 1 ATOM 1714 C CB . ALA A 1 214 ? 51.772 -14.747 20.406 1.00 104.71 ? 214 ALA A CB 1 ATOM 1715 N N . THR A 1 215 ? 52.018 -11.882 21.811 1.00 108.04 ? 215 THR A N 1 ATOM 1716 C CA . THR A 1 215 ? 51.885 -10.443 21.618 1.00 107.44 ? 215 THR A CA 1 ATOM 1717 C C . THR A 1 215 ? 51.825 -10.186 20.120 1.00 103.49 ? 215 THR A C 1 ATOM 1718 O O . THR A 1 215 ? 52.771 -10.490 19.394 1.00 103.25 ? 215 THR A O 1 ATOM 1719 C CB . THR A 1 215 ? 53.067 -9.671 22.231 1.00 109.81 ? 215 THR A CB 1 ATOM 1720 O OG1 . THR A 1 215 ? 53.314 -10.154 23.554 1.00 111.33 ? 215 THR A OG1 1 ATOM 1721 C CG2 . THR A 1 215 ? 52.772 -8.172 22.283 1.00 111.65 ? 215 THR A CG2 1 ATOM 1722 N N . ARG A 1 216 ? 50.706 -9.645 19.660 1.00 99.93 ? 216 ARG A N 1 ATOM 1723 C CA . ARG A 1 216 ? 50.490 -9.446 18.240 1.00 96.09 ? 216 ARG A CA 1 ATOM 1724 C C . ARG A 1 216 ? 50.222 -7.988 17.931 1.00 96.43 ? 216 ARG A C 1 ATOM 1725 O O . ARG A 1 216 ? 49.662 -7.262 18.753 1.00 95.88 ? 216 ARG A O 1 ATOM 1726 C CB . ARG A 1 216 ? 49.310 -10.290 17.775 1.00 93.99 ? 216 ARG A CB 1 ATOM 1727 C CG . ARG A 1 216 ? 49.574 -11.784 17.798 1.00 92.52 ? 216 ARG A CG 1 ATOM 1728 C CD . ARG A 1 216 ? 48.326 -12.564 17.420 1.00 90.50 ? 216 ARG A CD 1 ATOM 1729 N NE . ARG A 1 216 ? 47.402 -12.707 18.544 1.00 90.95 ? 216 ARG A NE 1 ATOM 1730 C CZ . ARG A 1 216 ? 47.461 -13.664 19.472 1.00 89.77 ? 216 ARG A CZ 1 ATOM 1731 N NH1 . ARG A 1 216 ? 48.411 -14.592 19.443 1.00 88.60 ? 216 ARG A NH1 1 ATOM 1732 N NH2 . ARG A 1 216 ? 46.558 -13.693 20.443 1.00 90.67 ? 216 ARG A NH2 1 ATOM 1733 N N . SER A 1 217 ? 50.625 -7.573 16.733 1.00 95.46 ? 217 SER A N 1 ATOM 1734 C CA . SER A 1 217 ? 50.304 -6.250 16.218 1.00 96.56 ? 217 SER A CA 1 ATOM 1735 C C . SER A 1 217 ? 48.792 -6.089 16.128 1.00 95.53 ? 217 SER A C 1 ATOM 1736 O O . SER A 1 217 ? 48.070 -7.060 15.909 1.00 91.98 ? 217 SER A O 1 ATOM 1737 C CB . SER A 1 217 ? 50.922 -6.056 14.833 1.00 95.80 ? 217 SER A CB 1 ATOM 1738 O OG . SER A 1 217 ? 52.314 -6.312 14.859 1.00 97.17 ? 217 SER A OG 1 ATOM 1739 N N . LYS A 1 218 ? 48.316 -4.863 16.310 1.00 98.28 ? 218 LYS A N 1 ATOM 1740 C CA . LYS A 1 218 ? 46.892 -4.580 16.180 1.00 99.60 ? 218 LYS A CA 1 ATOM 1741 C C . LYS A 1 218 ? 46.462 -4.607 14.715 1.00 96.28 ? 218 LYS A C 1 ATOM 1742 O O . LYS A 1 218 ? 47.164 -4.102 13.841 1.00 96.32 ? 218 LYS A O 1 ATOM 1743 C CB . LYS A 1 218 ? 46.544 -3.225 16.794 1.00 104.60 ? 218 LYS A CB 1 ATOM 1744 C CG . LYS A 1 218 ? 46.509 -3.234 18.308 1.00 108.64 ? 218 LYS A CG 1 ATOM 1745 C CD . LYS A 1 218 ? 46.141 -1.863 18.849 1.00 113.75 ? 218 LYS A CD 1 ATOM 1746 C CE . LYS A 1 218 ? 45.821 -1.917 20.332 1.00 117.67 ? 218 LYS A CE 1 ATOM 1747 N NZ . LYS A 1 218 ? 47.001 -2.309 21.155 1.00 119.85 ? 218 LYS A NZ 1 ATOM 1748 N N . VAL A 1 219 ? 45.310 -5.218 14.461 1.00 92.86 ? 219 VAL A N 1 ATOM 1749 C CA . VAL A 1 219 ? 44.696 -5.225 13.144 1.00 89.89 ? 219 VAL A CA 1 ATOM 1750 C C . VAL A 1 219 ? 43.210 -4.979 13.358 1.00 89.63 ? 219 VAL A C 1 ATOM 1751 O O . VAL A 1 219 ? 42.542 -5.767 14.024 1.00 88.70 ? 219 VAL A O 1 ATOM 1752 C CB . VAL A 1 219 ? 44.918 -6.573 12.440 1.00 88.42 ? 219 VAL A CB 1 ATOM 1753 C CG1 . VAL A 1 219 ? 44.229 -6.595 11.081 1.00 86.18 ? 219 VAL A CG1 1 ATOM 1754 C CG2 . VAL A 1 219 ? 46.410 -6.854 12.302 1.00 88.63 ? 219 VAL A CG2 1 ATOM 1755 N N . ASN A 1 220 ? 42.704 -3.878 12.808 1.00 89.92 ? 220 ASN A N 1 ATOM 1756 C CA . ASN A 1 220 ? 41.364 -3.381 13.139 1.00 91.29 ? 220 ASN A CA 1 ATOM 1757 C C . ASN A 1 220 ? 41.148 -3.235 14.656 1.00 91.09 ? 220 ASN A C 1 ATOM 1758 O O . ASN A 1 220 ? 40.085 -3.567 15.184 1.00 91.06 ? 220 ASN A O 1 ATOM 1759 C CB . ASN A 1 220 ? 40.279 -4.267 12.512 1.00 91.06 ? 220 ASN A CB 1 ATOM 1760 C CG . ASN A 1 220 ? 40.299 -4.228 10.997 1.00 91.00 ? 220 ASN A CG 1 ATOM 1761 O OD1 . ASN A 1 220 ? 40.247 -3.157 10.392 1.00 93.41 ? 220 ASN A OD1 1 ATOM 1762 N ND2 . ASN A 1 220 ? 40.365 -5.400 10.375 1.00 89.06 ? 220 ASN A ND2 1 ATOM 1763 N N . GLY A 1 221 ? 42.172 -2.736 15.345 1.00 90.48 ? 221 GLY A N 1 ATOM 1764 C CA . GLY A 1 221 ? 42.086 -2.445 16.771 1.00 91.41 ? 221 GLY A CA 1 ATOM 1765 C C . GLY A 1 221 ? 42.123 -3.643 17.705 1.00 89.85 ? 221 GLY A C 1 ATOM 1766 O O . GLY A 1 221 ? 41.802 -3.509 18.883 1.00 91.11 ? 221 GLY A O 1 ATOM 1767 N N . GLN A 1 222 ? 42.524 -4.809 17.205 1.00 87.24 ? 222 GLN A N 1 ATOM 1768 C CA . GLN A 1 222 ? 42.545 -6.018 18.031 1.00 86.97 ? 222 GLN A CA 1 ATOM 1769 C C . GLN A 1 222 ? 43.905 -6.717 18.009 1.00 86.23 ? 222 GLN A C 1 ATOM 1770 O O . GLN A 1 222 ? 44.504 -6.901 16.946 1.00 84.69 ? 222 GLN A O 1 ATOM 1771 C CB . GLN A 1 222 ? 41.456 -7.001 17.588 1.00 84.98 ? 222 GLN A CB 1 ATOM 1772 C CG . GLN A 1 222 ? 40.061 -6.405 17.424 1.00 86.42 ? 222 GLN A CG 1 ATOM 1773 C CD . GLN A 1 222 ? 39.505 -5.749 18.684 1.00 90.43 ? 222 GLN A CD 1 ATOM 1774 O OE1 . GLN A 1 222 ? 39.897 -6.069 19.814 1.00 89.05 ? 222 GLN A OE1 1 ATOM 1775 N NE2 . GLN A 1 222 ? 38.568 -4.824 18.487 1.00 93.00 ? 222 GLN A NE2 1 ATOM 1776 N N . SER A 1 223 ? 44.377 -7.097 19.196 1.00 87.24 ? 223 SER A N 1 ATOM 1777 C CA . SER A 1 223 ? 45.592 -7.896 19.353 1.00 87.22 ? 223 SER A CA 1 ATOM 1778 C C . SER A 1 223 ? 45.255 -9.384 19.319 1.00 84.82 ? 223 SER A C 1 ATOM 1779 O O . SER A 1 223 ? 46.108 -10.213 19.013 1.00 84.33 ? 223 SER A O 1 ATOM 1780 C CB . SER A 1 223 ? 46.281 -7.566 20.680 1.00 91.14 ? 223 SER A CB 1 ATOM 1781 O OG . SER A 1 223 ? 46.349 -6.165 20.897 1.00 95.54 ? 223 SER A OG 1 ATOM 1782 N N . GLY A 1 224 ? 44.010 -9.718 19.650 1.00 84.46 ? 224 GLY A N 1 ATOM 1783 C CA . GLY A 1 224 ? 43.543 -11.098 19.616 1.00 82.44 ? 224 GLY A CA 1 ATOM 1784 C C . GLY A 1 224 ? 43.231 -11.555 18.206 1.00 79.87 ? 224 GLY A C 1 ATOM 1785 O O . GLY A 1 224 ? 43.087 -10.732 17.300 1.00 78.34 ? 224 GLY A O 1 ATOM 1786 N N . ARG A 1 225 ? 43.115 -12.871 18.029 1.00 78.50 ? 225 ARG A N 1 ATOM 1787 C CA . ARG A 1 225 ? 42.851 -13.471 16.719 1.00 77.63 ? 225 ARG A CA 1 ATOM 1788 C C . ARG A 1 225 ? 41.739 -14.514 16.789 1.00 77.45 ? 225 ARG A C 1 ATOM 1789 O O . ARG A 1 225 ? 41.499 -15.106 17.838 1.00 78.37 ? 225 ARG A O 1 ATOM 1790 C CB . ARG A 1 225 ? 44.122 -14.130 16.162 1.00 75.86 ? 225 ARG A CB 1 ATOM 1791 C CG . ARG A 1 225 ? 45.281 -13.177 15.895 1.00 76.64 ? 225 ARG A CG 1 ATOM 1792 C CD . ARG A 1 225 ? 45.037 -12.318 14.663 1.00 75.96 ? 225 ARG A CD 1 ATOM 1793 N NE . ARG A 1 225 ? 46.185 -11.459 14.366 1.00 77.23 ? 225 ARG A NE 1 ATOM 1794 C CZ . ARG A 1 225 ? 46.338 -10.199 14.779 1.00 78.89 ? 225 ARG A CZ 1 ATOM 1795 N NH1 . ARG A 1 225 ? 45.414 -9.598 15.528 1.00 80.31 ? 225 ARG A NH1 1 ATOM 1796 N NH2 . ARG A 1 225 ? 47.436 -9.530 14.438 1.00 79.17 ? 225 ARG A NH2 1 ATOM 1797 N N . MET A 1 226 ? 41.066 -14.723 15.661 1.00 76.47 ? 226 MET A N 1 ATOM 1798 C CA . MET A 1 226 ? 40.067 -15.774 15.522 1.00 77.71 ? 226 MET A CA 1 ATOM 1799 C C . MET A 1 226 ? 40.488 -16.688 14.387 1.00 75.81 ? 226 MET A C 1 ATOM 1800 O O . MET A 1 226 ? 40.661 -16.228 13.264 1.00 76.50 ? 226 MET A O 1 ATOM 1801 C CB . MET A 1 226 ? 38.705 -15.175 15.183 1.00 80.47 ? 226 MET A CB 1 ATOM 1802 C CG . MET A 1 226 ? 38.101 -14.312 16.276 1.00 84.74 ? 226 MET A CG 1 ATOM 1803 S SD . MET A 1 226 ? 37.216 -15.262 17.525 1.00 88.93 ? 226 MET A SD 1 ATOM 1804 C CE . MET A 1 226 ? 36.509 -13.922 18.477 1.00 91.49 ? 226 MET A CE 1 ATOM 1805 N N . GLU A 1 227 ? 40.648 -17.975 14.676 1.00 75.42 ? 227 GLU A N 1 ATOM 1806 C CA . GLU A 1 227 ? 41.002 -18.965 13.661 1.00 73.96 ? 227 GLU A CA 1 ATOM 1807 C C . GLU A 1 227 ? 39.772 -19.815 13.370 1.00 72.52 ? 227 GLU A C 1 ATOM 1808 O O . GLU A 1 227 ? 39.218 -20.432 14.273 1.00 74.27 ? 227 GLU A O 1 ATOM 1809 C CB . GLU A 1 227 ? 42.161 -19.830 14.155 1.00 75.38 ? 227 GLU A CB 1 ATOM 1810 C CG . GLU A 1 227 ? 42.837 -20.662 13.077 1.00 76.47 ? 227 GLU A CG 1 ATOM 1811 C CD . GLU A 1 227 ? 44.185 -21.221 13.517 1.00 78.22 ? 227 GLU A CD 1 ATOM 1812 O OE1 . GLU A 1 227 ? 44.470 -21.237 14.740 1.00 77.65 ? 227 GLU A OE1 1 ATOM 1813 O OE2 . GLU A 1 227 ? 44.964 -21.643 12.630 1.00 77.93 ? 227 GLU A OE2 1 ATOM 1814 N N . PHE A 1 228 ? 39.329 -19.825 12.117 1.00 70.79 ? 228 PHE A N 1 ATOM 1815 C CA . PHE A 1 228 ? 38.086 -20.501 11.759 1.00 69.49 ? 228 PHE A CA 1 ATOM 1816 C C . PHE A 1 228 ? 38.340 -21.795 11.004 1.00 67.45 ? 228 PHE A C 1 ATOM 1817 O O . PHE A 1 228 ? 39.203 -21.852 10.127 1.00 66.95 ? 228 PHE A O 1 ATOM 1818 C CB . PHE A 1 228 ? 37.191 -19.567 10.952 1.00 70.18 ? 228 PHE A CB 1 ATOM 1819 C CG . PHE A 1 228 ? 36.649 -18.420 11.757 1.00 72.21 ? 228 PHE A CG 1 ATOM 1820 C CD1 . PHE A 1 228 ? 35.591 -18.614 12.633 1.00 72.95 ? 228 PHE A CD1 1 ATOM 1821 C CD2 . PHE A 1 228 ? 37.213 -17.154 11.657 1.00 73.23 ? 228 PHE A CD2 1 ATOM 1822 C CE1 . PHE A 1 228 ? 35.098 -17.564 13.388 1.00 75.94 ? 228 PHE A CE1 1 ATOM 1823 C CE2 . PHE A 1 228 ? 36.725 -16.099 12.408 1.00 75.64 ? 228 PHE A CE2 1 ATOM 1824 C CZ . PHE A 1 228 ? 35.667 -16.305 13.279 1.00 77.01 ? 228 PHE A CZ 1 ATOM 1825 N N . PHE A 1 229 ? 37.576 -22.825 11.365 1.00 66.15 ? 229 PHE A N 1 ATOM 1826 C CA . PHE A 1 229 ? 37.708 -24.163 10.796 1.00 65.11 ? 229 PHE A CA 1 ATOM 1827 C C . PHE A 1 229 ? 36.375 -24.630 10.226 1.00 65.76 ? 229 PHE A C 1 ATOM 1828 O O . PHE A 1 229 ? 35.315 -24.076 10.550 1.00 64.44 ? 229 PHE A O 1 ATOM 1829 C CB . PHE A 1 229 ? 38.154 -25.158 11.870 1.00 66.10 ? 229 PHE A CB 1 ATOM 1830 C CG . PHE A 1 229 ? 39.529 -24.897 12.407 1.00 66.15 ? 229 PHE A CG 1 ATOM 1831 C CD1 . PHE A 1 229 ? 39.729 -23.958 13.408 1.00 67.21 ? 229 PHE A CD1 1 ATOM 1832 C CD2 . PHE A 1 229 ? 40.625 -25.596 11.916 1.00 65.85 ? 229 PHE A CD2 1 ATOM 1833 C CE1 . PHE A 1 229 ? 40.998 -23.717 13.909 1.00 67.78 ? 229 PHE A CE1 1 ATOM 1834 C CE2 . PHE A 1 229 ? 41.896 -25.356 12.409 1.00 66.41 ? 229 PHE A CE2 1 ATOM 1835 C CZ . PHE A 1 229 ? 42.083 -24.417 13.409 1.00 67.30 ? 229 PHE A CZ 1 ATOM 1836 N N . TRP A 1 230 ? 36.433 -25.658 9.383 1.00 65.39 ? 230 TRP A N 1 ATOM 1837 C CA . TRP A 1 230 ? 35.226 -26.211 8.789 1.00 66.08 ? 230 TRP A CA 1 ATOM 1838 C C . TRP A 1 230 ? 35.332 -27.707 8.543 1.00 65.75 ? 230 TRP A C 1 ATOM 1839 O O . TRP A 1 230 ? 36.423 -28.272 8.561 1.00 65.13 ? 230 TRP A O 1 ATOM 1840 C CB . TRP A 1 230 ? 34.918 -25.493 7.476 1.00 65.67 ? 230 TRP A CB 1 ATOM 1841 C CG . TRP A 1 230 ? 35.997 -25.618 6.449 1.00 64.62 ? 230 TRP A CG 1 ATOM 1842 C CD1 . TRP A 1 230 ? 37.101 -24.822 6.315 1.00 64.66 ? 230 TRP A CD1 1 ATOM 1843 C CD2 . TRP A 1 230 ? 36.075 -26.591 5.406 1.00 64.02 ? 230 TRP A CD2 1 ATOM 1844 N NE1 . TRP A 1 230 ? 37.862 -25.241 5.254 1.00 63.65 ? 230 TRP A NE1 1 ATOM 1845 C CE2 . TRP A 1 230 ? 37.256 -26.327 4.678 1.00 64.11 ? 230 TRP A CE2 1 ATOM 1846 C CE3 . TRP A 1 230 ? 35.264 -27.663 5.016 1.00 65.31 ? 230 TRP A CE3 1 ATOM 1847 C CZ2 . TRP A 1 230 ? 37.645 -27.097 3.575 1.00 64.28 ? 230 TRP A CZ2 1 ATOM 1848 C CZ3 . TRP A 1 230 ? 35.651 -28.431 3.919 1.00 66.08 ? 230 TRP A CZ3 1 ATOM 1849 C CH2 . TRP A 1 230 ? 36.832 -28.143 3.213 1.00 64.74 ? 230 TRP A CH2 1 ATOM 1850 N N . THR A 1 231 ? 34.181 -28.336 8.328 1.00 66.05 ? 231 THR A N 1 ATOM 1851 C CA . THR A 1 231 ? 34.115 -29.712 7.849 1.00 66.94 ? 231 THR A CA 1 ATOM 1852 C C . THR A 1 231 ? 32.825 -29.929 7.063 1.00 68.44 ? 231 THR A C 1 ATOM 1853 O O . THR A 1 231 ? 31.900 -29.122 7.140 1.00 70.55 ? 231 THR A O 1 ATOM 1854 C CB . THR A 1 231 ? 34.185 -30.727 9.011 1.00 67.96 ? 231 THR A CB 1 ATOM 1855 O OG1 . THR A 1 231 ? 34.366 -32.049 8.491 1.00 67.75 ? 231 THR A OG1 1 ATOM 1856 C CG2 . THR A 1 231 ? 32.917 -30.696 9.855 1.00 68.53 ? 231 THR A CG2 1 ATOM 1857 N N . ILE A 1 232 ? 32.778 -31.014 6.300 1.00 69.98 ? 232 ILE A N 1 ATOM 1858 C CA . ILE A 1 232 ? 31.548 -31.454 5.651 1.00 72.01 ? 232 ILE A CA 1 ATOM 1859 C C . ILE A 1 232 ? 31.030 -32.613 6.477 1.00 73.91 ? 232 ILE A C 1 ATOM 1860 O O . ILE A 1 232 ? 31.693 -33.638 6.590 1.00 75.45 ? 232 ILE A O 1 ATOM 1861 C CB . ILE A 1 232 ? 31.785 -31.865 4.172 1.00 72.76 ? 232 ILE A CB 1 ATOM 1862 C CG1 . ILE A 1 232 ? 31.415 -30.716 3.231 1.00 72.09 ? 232 ILE A CG1 1 ATOM 1863 C CG2 . ILE A 1 232 ? 30.945 -33.076 3.772 1.00 74.51 ? 232 ILE A CG2 1 ATOM 1864 C CD1 . ILE A 1 232 ? 32.040 -29.391 3.590 1.00 71.59 ? 232 ILE A CD1 1 ATOM 1865 N N . LEU A 1 233 ? 29.857 -32.433 7.075 1.00 77.05 ? 233 LEU A N 1 ATOM 1866 C CA . LEU A 1 233 ? 29.244 -33.467 7.900 1.00 78.63 ? 233 LEU A CA 1 ATOM 1867 C C . LEU A 1 233 ? 28.318 -34.289 7.023 1.00 79.54 ? 233 LEU A C 1 ATOM 1868 O O . LEU A 1 233 ? 27.343 -33.765 6.487 1.00 79.28 ? 233 LEU A O 1 ATOM 1869 C CB . LEU A 1 233 ? 28.464 -32.826 9.050 1.00 80.26 ? 233 LEU A CB 1 ATOM 1870 C CG . LEU A 1 233 ? 27.863 -33.748 10.114 1.00 82.19 ? 233 LEU A CG 1 ATOM 1871 C CD1 . LEU A 1 233 ? 28.948 -34.513 10.862 1.00 81.96 ? 233 LEU A CD1 1 ATOM 1872 C CD2 . LEU A 1 233 ? 27.015 -32.931 11.077 1.00 83.39 ? 233 LEU A CD2 1 ATOM 1873 N N . LYS A 1 234 ? 28.624 -35.572 6.869 1.00 82.13 ? 234 LYS A N 1 ATOM 1874 C CA . LYS A 1 234 ? 27.868 -36.430 5.953 1.00 87.47 ? 234 LYS A CA 1 ATOM 1875 C C . LYS A 1 234 ? 26.539 -36.860 6.571 1.00 89.81 ? 234 LYS A C 1 ATOM 1876 O O . LYS A 1 234 ? 26.354 -36.726 7.784 1.00 89.54 ? 234 LYS A O 1 ATOM 1877 C CB . LYS A 1 234 ? 28.717 -37.633 5.520 1.00 92.17 ? 234 LYS A CB 1 ATOM 1878 C CG . LYS A 1 234 ? 29.432 -37.394 4.192 1.00 95.94 ? 234 LYS A CG 1 ATOM 1879 C CD . LYS A 1 234 ? 30.353 -38.540 3.805 1.00 101.14 ? 234 LYS A CD 1 ATOM 1880 C CE . LYS A 1 234 ? 31.658 -38.490 4.585 1.00 103.77 ? 234 LYS A CE 1 ATOM 1881 N NZ . LYS A 1 234 ? 32.499 -39.696 4.352 1.00 107.26 ? 234 LYS A NZ 1 ATOM 1882 N N . PRO A 1 235 ? 25.600 -37.367 5.740 1.00 91.04 ? 235 PRO A N 1 ATOM 1883 C CA . PRO A 1 235 ? 24.281 -37.700 6.295 1.00 91.95 ? 235 PRO A CA 1 ATOM 1884 C C . PRO A 1 235 ? 24.375 -38.813 7.330 1.00 93.57 ? 235 PRO A C 1 ATOM 1885 O O . PRO A 1 235 ? 25.171 -39.739 7.164 1.00 93.19 ? 235 PRO A O 1 ATOM 1886 C CB . PRO A 1 235 ? 23.472 -38.156 5.076 1.00 93.01 ? 235 PRO A CB 1 ATOM 1887 C CG . PRO A 1 235 ? 24.475 -38.521 4.041 1.00 92.14 ? 235 PRO A CG 1 ATOM 1888 C CD . PRO A 1 235 ? 25.716 -37.730 4.314 1.00 89.62 ? 235 PRO A CD 1 ATOM 1889 N N . ASN A 1 236 ? 23.584 -38.699 8.396 1.00 94.58 ? 236 ASN A N 1 ATOM 1890 C CA . ASN A 1 236 ? 23.593 -39.659 9.497 1.00 96.70 ? 236 ASN A CA 1 ATOM 1891 C C . ASN A 1 236 ? 24.842 -39.646 10.378 1.00 95.32 ? 236 ASN A C 1 ATOM 1892 O O . ASN A 1 236 ? 24.944 -40.458 11.296 1.00 98.09 ? 236 ASN A O 1 ATOM 1893 C CB . ASN A 1 236 ? 23.338 -41.089 8.991 1.00 99.45 ? 236 ASN A CB 1 ATOM 1894 C CG . ASN A 1 236 ? 21.875 -41.448 8.994 1.00 103.99 ? 236 ASN A CG 1 ATOM 1895 O OD1 . ASN A 1 236 ? 21.152 -41.140 9.942 1.00 106.89 ? 236 ASN A OD1 1 ATOM 1896 N ND2 . ASN A 1 236 ? 21.429 -42.115 7.940 1.00 106.10 ? 236 ASN A ND2 1 ATOM 1897 N N . ASP A 1 237 ? 25.781 -38.738 10.123 1.00 91.36 ? 237 ASP A N 1 ATOM 1898 C CA . ASP A 1 237 ? 26.925 -38.584 11.011 1.00 90.29 ? 237 ASP A CA 1 ATOM 1899 C C . ASP A 1 237 ? 26.632 -37.463 12.002 1.00 89.75 ? 237 ASP A C 1 ATOM 1900 O O . ASP A 1 237 ? 25.773 -36.611 11.760 1.00 89.86 ? 237 ASP A O 1 ATOM 1901 C CB . ASP A 1 237 ? 28.206 -38.292 10.222 1.00 88.86 ? 237 ASP A CB 1 ATOM 1902 C CG . ASP A 1 237 ? 29.477 -38.653 10.995 1.00 88.46 ? 237 ASP A CG 1 ATOM 1903 O OD1 . ASP A 1 237 ? 29.422 -39.508 11.909 1.00 90.11 ? 237 ASP A OD1 1 ATOM 1904 O OD2 . ASP A 1 237 ? 30.543 -38.085 10.680 1.00 85.51 ? 237 ASP A OD2 1 ATOM 1905 N N . ALA A 1 238 ? 27.339 -37.481 13.124 1.00 88.96 ? 238 ALA A N 1 ATOM 1906 C CA . ALA A 1 238 ? 27.165 -36.475 14.161 1.00 89.66 ? 238 ALA A CA 1 ATOM 1907 C C . ALA A 1 238 ? 28.479 -35.759 14.411 1.00 87.39 ? 238 ALA A C 1 ATOM 1908 O O . ALA A 1 238 ? 29.540 -36.385 14.384 1.00 88.07 ? 238 ALA A O 1 ATOM 1909 C CB . ALA A 1 238 ? 26.675 -37.125 15.446 1.00 90.92 ? 238 ALA A CB 1 ATOM 1910 N N . ILE A 1 239 ? 28.405 -34.450 14.645 1.00 85.13 ? 239 ILE A N 1 ATOM 1911 C CA . ILE A 1 239 ? 29.573 -33.682 15.071 1.00 82.73 ? 239 ILE A CA 1 ATOM 1912 C C . ILE A 1 239 ? 29.513 -33.456 16.585 1.00 85.15 ? 239 ILE A C 1 ATOM 1913 O O . ILE A 1 239 ? 28.455 -33.134 17.134 1.00 85.62 ? 239 ILE A O 1 ATOM 1914 C CB . ILE A 1 239 ? 29.712 -32.349 14.302 1.00 80.71 ? 239 ILE A CB 1 ATOM 1915 C CG1 . ILE A 1 239 ? 31.104 -31.751 14.532 1.00 79.87 ? 239 ILE A CG1 1 ATOM 1916 C CG2 . ILE A 1 239 ? 28.624 -31.354 14.688 1.00 80.95 ? 239 ILE A CG2 1 ATOM 1917 C CD1 . ILE A 1 239 ? 31.489 -30.694 13.520 1.00 78.43 ? 239 ILE A CD1 1 ATOM 1918 N N . ASN A 1 240 ? 30.650 -33.646 17.250 1.00 85.06 ? 240 ASN A N 1 ATOM 1919 C CA . ASN A 1 240 ? 30.734 -33.579 18.704 1.00 86.82 ? 240 ASN A CA 1 ATOM 1920 C C . ASN A 1 240 ? 31.738 -32.533 19.156 1.00 84.93 ? 240 ASN A C 1 ATOM 1921 O O . ASN A 1 240 ? 32.924 -32.644 18.858 1.00 83.09 ? 240 ASN A O 1 ATOM 1922 C CB . ASN A 1 240 ? 31.158 -34.931 19.258 1.00 89.22 ? 240 ASN A CB 1 ATOM 1923 C CG . ASN A 1 240 ? 30.095 -35.993 19.080 1.00 92.67 ? 240 ASN A CG 1 ATOM 1924 O OD1 . ASN A 1 240 ? 28.947 -35.813 19.486 1.00 93.28 ? 240 ASN A OD1 1 ATOM 1925 N ND2 . ASN A 1 240 ? 30.474 -37.116 18.476 1.00 95.08 ? 240 ASN A ND2 1 ATOM 1926 N N . PHE A 1 241 ? 31.256 -31.532 19.887 1.00 84.83 ? 241 PHE A N 1 ATOM 1927 C CA . PHE A 1 241 ? 32.110 -30.494 20.447 1.00 83.93 ? 241 PHE A CA 1 ATOM 1928 C C . PHE A 1 241 ? 32.278 -30.683 21.955 1.00 85.68 ? 241 PHE A C 1 ATOM 1929 O O . PHE A 1 241 ? 31.313 -30.968 22.666 1.00 87.47 ? 241 PHE A O 1 ATOM 1930 C CB . PHE A 1 241 ? 31.514 -29.116 20.166 1.00 83.63 ? 241 PHE A CB 1 ATOM 1931 C CG . PHE A 1 241 ? 31.450 -28.774 18.709 1.00 82.73 ? 241 PHE A CG 1 ATOM 1932 C CD1 . PHE A 1 241 ? 32.560 -28.261 18.056 1.00 81.25 ? 241 PHE A CD1 1 ATOM 1933 C CD2 . PHE A 1 241 ? 30.281 -28.967 17.987 1.00 83.67 ? 241 PHE A CD2 1 ATOM 1934 C CE1 . PHE A 1 241 ? 32.508 -27.944 16.710 1.00 81.04 ? 241 PHE A CE1 1 ATOM 1935 C CE2 . PHE A 1 241 ? 30.218 -28.649 16.641 1.00 82.60 ? 241 PHE A CE2 1 ATOM 1936 C CZ . PHE A 1 241 ? 31.335 -28.138 15.999 1.00 81.22 ? 241 PHE A CZ 1 ATOM 1937 N N . GLU A 1 242 ? 33.514 -30.546 22.426 1.00 84.82 ? 242 GLU A N 1 ATOM 1938 C CA . GLU A 1 242 ? 33.798 -30.414 23.851 1.00 86.95 ? 242 GLU A CA 1 ATOM 1939 C C . GLU A 1 242 ? 34.790 -29.264 24.019 1.00 85.83 ? 242 GLU A C 1 ATOM 1940 O O . GLU A 1 242 ? 35.811 -29.219 23.325 1.00 83.36 ? 242 GLU A O 1 ATOM 1941 C CB . GLU A 1 242 ? 34.350 -31.724 24.443 1.00 88.43 ? 242 GLU A CB 1 ATOM 1942 C CG . GLU A 1 242 ? 34.711 -31.644 25.927 1.00 91.27 ? 242 GLU A CG 1 ATOM 1943 C CD . GLU A 1 242 ? 35.138 -32.980 26.520 1.00 92.64 ? 242 GLU A CD 1 ATOM 1944 O OE1 . GLU A 1 242 ? 34.355 -33.950 26.451 1.00 93.51 ? 242 GLU A OE1 1 ATOM 1945 O OE2 . GLU A 1 242 ? 36.255 -33.060 27.073 1.00 92.89 ? 242 GLU A OE2 1 ATOM 1946 N N . SER A 1 243 ? 34.494 -28.327 24.920 1.00 86.27 ? 243 SER A N 1 ATOM 1947 C CA . SER A 1 243 ? 35.400 -27.201 25.131 1.00 85.67 ? 243 SER A CA 1 ATOM 1948 C C . SER A 1 243 ? 35.461 -26.660 26.551 1.00 88.33 ? 243 SER A C 1 ATOM 1949 O O . SER A 1 243 ? 34.524 -26.779 27.332 1.00 90.85 ? 243 SER A O 1 ATOM 1950 C CB . SER A 1 243 ? 35.077 -26.051 24.182 1.00 83.91 ? 243 SER A CB 1 ATOM 1951 O OG . SER A 1 243 ? 36.018 -25.002 24.344 1.00 82.49 ? 243 SER A OG 1 ATOM 1952 N N . ASN A 1 244 ? 36.594 -26.024 26.824 1.00 89.22 ? 244 ASN A N 1 ATOM 1953 C CA . ASN A 1 244 ? 36.962 -25.501 28.125 1.00 91.51 ? 244 ASN A CA 1 ATOM 1954 C C . ASN A 1 244 ? 36.949 -23.964 28.163 1.00 91.00 ? 244 ASN A C 1 ATOM 1955 O O . ASN A 1 244 ? 37.097 -23.358 29.220 1.00 91.33 ? 244 ASN A O 1 ATOM 1956 C CB . ASN A 1 244 ? 38.375 -25.997 28.421 1.00 91.89 ? 244 ASN A CB 1 ATOM 1957 C CG . ASN A 1 244 ? 38.674 -26.063 29.889 1.00 95.49 ? 244 ASN A CG 1 ATOM 1958 O OD1 . ASN A 1 244 ? 37.830 -25.735 30.711 1.00 100.49 ? 244 ASN A OD1 1 ATOM 1959 N ND2 . ASN A 1 244 ? 39.885 -26.489 30.232 1.00 96.69 ? 244 ASN A ND2 1 ATOM 1960 N N . GLY A 1 245 ? 36.755 -23.352 26.998 1.00 89.99 ? 245 GLY A N 1 ATOM 1961 C CA . GLY A 1 245 ? 36.943 -21.919 26.799 1.00 90.10 ? 245 GLY A CA 1 ATOM 1962 C C . GLY A 1 245 ? 37.384 -21.661 25.367 1.00 88.50 ? 245 GLY A C 1 ATOM 1963 O O . GLY A 1 245 ? 37.779 -22.592 24.654 1.00 86.48 ? 245 GLY A O 1 ATOM 1964 N N . ASN A 1 246 ? 37.300 -20.399 24.946 1.00 88.77 ? 246 ASN A N 1 ATOM 1965 C CA . ASN A 1 246 ? 37.797 -19.940 23.636 1.00 86.41 ? 246 ASN A CA 1 ATOM 1966 C C . ASN A 1 246 ? 37.013 -20.473 22.429 1.00 83.09 ? 246 ASN A C 1 ATOM 1967 O O . ASN A 1 246 ? 37.425 -20.287 21.289 1.00 81.04 ? 246 ASN A O 1 ATOM 1968 C CB . ASN A 1 246 ? 39.300 -20.249 23.477 1.00 86.57 ? 246 ASN A CB 1 ATOM 1969 C CG . ASN A 1 246 ? 40.153 -19.601 24.561 1.00 90.00 ? 246 ASN A CG 1 ATOM 1970 O OD1 . ASN A 1 246 ? 40.540 -18.437 24.451 1.00 93.46 ? 246 ASN A OD1 1 ATOM 1971 N ND2 . ASN A 1 246 ? 40.469 -20.360 25.602 1.00 90.18 ? 246 ASN A ND2 1 ATOM 1972 N N . PHE A 1 247 ? 35.864 -21.092 22.684 1.00 82.97 ? 247 PHE A N 1 ATOM 1973 C CA . PHE A 1 247 ? 35.075 -21.752 21.648 1.00 79.41 ? 247 PHE A CA 1 ATOM 1974 C C . PHE A 1 247 ? 34.168 -20.756 20.935 1.00 78.25 ? 247 PHE A C 1 ATOM 1975 O O . PHE A 1 247 ? 33.432 -20.010 21.567 1.00 80.19 ? 247 PHE A O 1 ATOM 1976 C CB . PHE A 1 247 ? 34.254 -22.879 22.293 1.00 80.65 ? 247 PHE A CB 1 ATOM 1977 C CG . PHE A 1 247 ? 33.450 -23.712 21.328 1.00 79.99 ? 247 PHE A CG 1 ATOM 1978 C CD1 . PHE A 1 247 ? 33.993 -24.160 20.133 1.00 77.82 ? 247 PHE A CD1 1 ATOM 1979 C CD2 . PHE A 1 247 ? 32.154 -24.093 21.648 1.00 81.51 ? 247 PHE A CD2 1 ATOM 1980 C CE1 . PHE A 1 247 ? 33.249 -24.938 19.264 1.00 77.08 ? 247 PHE A CE1 1 ATOM 1981 C CE2 . PHE A 1 247 ? 31.409 -24.876 20.785 1.00 80.41 ? 247 PHE A CE2 1 ATOM 1982 C CZ . PHE A 1 247 ? 31.957 -25.298 19.590 1.00 78.72 ? 247 PHE A CZ 1 ATOM 1983 N N . ILE A 1 248 ? 34.250 -20.729 19.610 1.00 77.72 ? 248 ILE A N 1 ATOM 1984 C CA . ILE A 1 248 ? 33.311 -19.970 18.799 1.00 77.31 ? 248 ILE A CA 1 ATOM 1985 C C . ILE A 1 248 ? 32.363 -21.006 18.215 1.00 77.23 ? 248 ILE A C 1 ATOM 1986 O O . ILE A 1 248 ? 32.719 -21.742 17.299 1.00 76.41 ? 248 ILE A O 1 ATOM 1987 C CB . ILE A 1 248 ? 34.018 -19.167 17.691 1.00 75.93 ? 248 ILE A CB 1 ATOM 1988 C CG1 . ILE A 1 248 ? 35.249 -18.431 18.237 1.00 76.13 ? 248 ILE A CG1 1 ATOM 1989 C CG2 . ILE A 1 248 ? 33.053 -18.176 17.061 1.00 76.89 ? 248 ILE A CG2 1 ATOM 1990 C CD1 . ILE A 1 248 ? 34.961 -17.481 19.377 1.00 78.81 ? 248 ILE A CD1 1 ATOM 1991 N N . ALA A 1 249 ? 31.162 -21.083 18.773 1.00 79.49 ? 249 ALA A N 1 ATOM 1992 C CA . ALA A 1 249 ? 30.257 -22.193 18.482 1.00 81.04 ? 249 ALA A CA 1 ATOM 1993 C C . ALA A 1 249 ? 29.426 -21.965 17.218 1.00 80.86 ? 249 ALA A C 1 ATOM 1994 O O . ALA A 1 249 ? 29.033 -20.836 16.928 1.00 81.06 ? 249 ALA A O 1 ATOM 1995 C CB . ALA A 1 249 ? 29.339 -22.440 19.669 1.00 83.41 ? 249 ALA A CB 1 ATOM 1996 N N . PRO A 1 250 ? 29.153 -23.042 16.460 1.00 80.95 ? 250 PRO A N 1 ATOM 1997 C CA . PRO A 1 250 ? 28.228 -22.896 15.340 1.00 81.11 ? 250 PRO A CA 1 ATOM 1998 C C . PRO A 1 250 ? 26.838 -22.489 15.812 1.00 85.27 ? 250 PRO A C 1 ATOM 1999 O O . PRO A 1 250 ? 26.359 -23.009 16.819 1.00 86.61 ? 250 PRO A O 1 ATOM 2000 C CB . PRO A 1 250 ? 28.180 -24.297 14.717 1.00 79.31 ? 250 PRO A CB 1 ATOM 2001 C CG . PRO A 1 250 ? 28.815 -25.215 15.697 1.00 79.68 ? 250 PRO A CG 1 ATOM 2002 C CD . PRO A 1 250 ? 29.754 -24.386 16.513 1.00 80.17 ? 250 PRO A CD 1 ATOM 2003 N N . GLU A 1 251 ? 26.224 -21.547 15.101 1.00 86.99 ? 251 GLU A N 1 ATOM 2004 C CA . GLU A 1 251 ? 24.817 -21.204 15.290 1.00 89.85 ? 251 GLU A CA 1 ATOM 2005 C C . GLU A 1 251 ? 24.068 -21.728 14.060 1.00 89.86 ? 251 GLU A C 1 ATOM 2006 O O . GLU A 1 251 ? 23.159 -22.556 14.181 1.00 89.60 ? 251 GLU A O 1 ATOM 2007 C CB . GLU A 1 251 ? 24.654 -19.683 15.451 1.00 92.13 ? 251 GLU A CB 1 ATOM 2008 C CG . GLU A 1 251 ? 23.710 -19.239 16.563 1.00 96.87 ? 251 GLU A CG 1 ATOM 2009 C CD . GLU A 1 251 ? 22.255 -19.165 16.136 1.00 99.94 ? 251 GLU A CD 1 ATOM 2010 O OE1 . GLU A 1 251 ? 21.766 -20.131 15.523 1.00 102.60 ? 251 GLU A OE1 1 ATOM 2011 O OE2 . GLU A 1 251 ? 21.592 -18.144 16.424 1.00 101.40 ? 251 GLU A OE2 1 ATOM 2012 N N . TYR A 1 252 ? 24.486 -21.257 12.880 1.00 87.16 ? 252 TYR A N 1 ATOM 2013 C CA . TYR A 1 252 ? 23.915 -21.682 11.599 1.00 86.78 ? 252 TYR A CA 1 ATOM 2014 C C . TYR A 1 252 ? 24.931 -22.469 10.767 1.00 84.29 ? 252 TYR A C 1 ATOM 2015 O O . TYR A 1 252 ? 26.135 -22.214 10.822 1.00 82.62 ? 252 TYR A O 1 ATOM 2016 C CB . TYR A 1 252 ? 23.441 -20.466 10.791 1.00 87.27 ? 252 TYR A CB 1 ATOM 2017 C CG . TYR A 1 252 ? 22.336 -19.670 11.450 1.00 90.51 ? 252 TYR A CG 1 ATOM 2018 C CD1 . TYR A 1 252 ? 22.628 -18.620 12.318 1.00 91.17 ? 252 TYR A CD1 1 ATOM 2019 C CD2 . TYR A 1 252 ? 20.999 -19.966 11.207 1.00 92.77 ? 252 TYR A CD2 1 ATOM 2020 C CE1 . TYR A 1 252 ? 21.621 -17.887 12.925 1.00 93.39 ? 252 TYR A CE1 1 ATOM 2021 C CE2 . TYR A 1 252 ? 19.984 -19.241 11.813 1.00 95.52 ? 252 TYR A CE2 1 ATOM 2022 C CZ . TYR A 1 252 ? 20.299 -18.202 12.669 1.00 95.90 ? 252 TYR A CZ 1 ATOM 2023 O OH . TYR A 1 252 ? 19.292 -17.478 13.272 1.00 98.64 ? 252 TYR A OH 1 ATOM 2024 N N . ALA A 1 253 ? 24.432 -23.426 9.993 1.00 83.73 ? 253 ALA A N 1 ATOM 2025 C CA . ALA A 1 253 ? 25.256 -24.195 9.066 1.00 80.81 ? 253 ALA A CA 1 ATOM 2026 C C . ALA A 1 253 ? 24.501 -24.363 7.746 1.00 81.46 ? 253 ALA A C 1 ATOM 2027 O O . ALA A 1 253 ? 23.268 -24.282 7.716 1.00 83.15 ? 253 ALA A O 1 ATOM 2028 C CB . ALA A 1 253 ? 25.602 -25.546 9.671 1.00 80.44 ? 253 ALA A CB 1 ATOM 2029 N N . TYR A 1 254 ? 25.240 -24.600 6.664 1.00 79.13 ? 254 TYR A N 1 ATOM 2030 C CA . TYR A 1 254 ? 24.667 -24.588 5.320 1.00 79.46 ? 254 TYR A CA 1 ATOM 2031 C C . TYR A 1 254 ? 24.403 -25.991 4.780 1.00 81.05 ? 254 TYR A C 1 ATOM 2032 O O . TYR A 1 254 ? 25.323 -26.807 4.684 1.00 79.66 ? 254 TYR A O 1 ATOM 2033 C CB . TYR A 1 254 ? 25.603 -23.858 4.356 1.00 77.52 ? 254 TYR A CB 1 ATOM 2034 C CG . TYR A 1 254 ? 25.775 -22.381 4.634 1.00 77.25 ? 254 TYR A CG 1 ATOM 2035 C CD1 . TYR A 1 254 ? 24.932 -21.439 4.048 1.00 78.52 ? 254 TYR A CD1 1 ATOM 2036 C CD2 . TYR A 1 254 ? 26.793 -21.923 5.461 1.00 76.66 ? 254 TYR A CD2 1 ATOM 2037 C CE1 . TYR A 1 254 ? 25.088 -20.084 4.287 1.00 79.11 ? 254 TYR A CE1 1 ATOM 2038 C CE2 . TYR A 1 254 ? 26.959 -20.569 5.709 1.00 77.70 ? 254 TYR A CE2 1 ATOM 2039 C CZ . TYR A 1 254 ? 26.102 -19.652 5.118 1.00 79.18 ? 254 TYR A CZ 1 ATOM 2040 O OH . TYR A 1 254 ? 26.256 -18.303 5.356 1.00 81.19 ? 254 TYR A OH 1 ATOM 2041 N N . LYS A 1 255 ? 23.149 -26.266 4.422 1.00 83.55 ? 255 LYS A N 1 ATOM 2042 C CA . LYS A 1 255 ? 22.817 -27.470 3.661 1.00 85.00 ? 255 LYS A CA 1 ATOM 2043 C C . LYS A 1 255 ? 23.277 -27.286 2.222 1.00 83.52 ? 255 LYS A C 1 ATOM 2044 O O . LYS A 1 255 ? 23.088 -26.218 1.646 1.00 82.46 ? 255 LYS A O 1 ATOM 2045 C CB . LYS A 1 255 ? 21.311 -27.735 3.654 1.00 88.39 ? 255 LYS A CB 1 ATOM 2046 C CG . LYS A 1 255 ? 20.722 -28.256 4.952 1.00 90.92 ? 255 LYS A CG 1 ATOM 2047 C CD . LYS A 1 255 ? 19.349 -28.887 4.730 1.00 94.50 ? 255 LYS A CD 1 ATOM 2048 C CE . LYS A 1 255 ? 18.319 -27.891 4.213 1.00 96.95 ? 255 LYS A CE 1 ATOM 2049 N NZ . LYS A 1 255 ? 17.056 -28.558 3.789 1.00 100.50 ? 255 LYS A NZ 1 ATOM 2050 N N . ILE A 1 256 ? 23.869 -28.333 1.651 1.00 82.74 ? 256 ILE A N 1 ATOM 2051 C CA . ILE A 1 256 ? 24.279 -28.332 0.253 1.00 82.71 ? 256 ILE A CA 1 ATOM 2052 C C . ILE A 1 256 ? 23.192 -29.020 -0.569 1.00 84.89 ? 256 ILE A C 1 ATOM 2053 O O . ILE A 1 256 ? 23.192 -30.241 -0.719 1.00 84.42 ? 256 ILE A O 1 ATOM 2054 C CB . ILE A 1 256 ? 25.619 -29.068 0.060 1.00 81.81 ? 256 ILE A CB 1 ATOM 2055 C CG1 . ILE A 1 256 ? 26.657 -28.557 1.066 1.00 80.95 ? 256 ILE A CG1 1 ATOM 2056 C CG2 . ILE A 1 256 ? 26.111 -28.898 -1.370 1.00 81.43 ? 256 ILE A CG2 1 ATOM 2057 C CD1 . ILE A 1 256 ? 28.086 -28.982 0.778 1.00 79.24 ? 256 ILE A CD1 1 ATOM 2058 N N . VAL A 1 257 ? 22.268 -28.235 -1.110 1.00 86.97 ? 257 VAL A N 1 ATOM 2059 C CA . VAL A 1 257 ? 21.090 -28.814 -1.762 1.00 91.04 ? 257 VAL A CA 1 ATOM 2060 C C . VAL A 1 257 ? 21.327 -29.167 -3.232 1.00 93.00 ? 257 VAL A C 1 ATOM 2061 O O . VAL A 1 257 ? 20.885 -30.228 -3.696 1.00 93.37 ? 257 VAL A O 1 ATOM 2062 C CB . VAL A 1 257 ? 19.827 -27.933 -1.597 1.00 93.43 ? 257 VAL A CB 1 ATOM 2063 C CG1 . VAL A 1 257 ? 19.300 -28.048 -0.177 1.00 94.76 ? 257 VAL A CG1 1 ATOM 2064 C CG2 . VAL A 1 257 ? 20.093 -26.475 -1.945 1.00 92.68 ? 257 VAL A CG2 1 ATOM 2065 N N . LYS A 1 258 ? 22.034 -28.298 -3.955 1.00 92.77 ? 258 LYS A N 1 ATOM 2066 C CA . LYS A 1 258 ? 22.324 -28.542 -5.364 1.00 94.01 ? 258 LYS A CA 1 ATOM 2067 C C . LYS A 1 258 ? 23.823 -28.508 -5.637 1.00 90.96 ? 258 LYS A C 1 ATOM 2068 O O . LYS A 1 258 ? 24.493 -27.523 -5.331 1.00 88.36 ? 258 LYS A O 1 ATOM 2069 C CB . LYS A 1 258 ? 21.609 -27.522 -6.254 1.00 96.53 ? 258 LYS A CB 1 ATOM 2070 C CG . LYS A 1 258 ? 21.614 -27.917 -7.723 1.00 99.66 ? 258 LYS A CG 1 ATOM 2071 C CD . LYS A 1 258 ? 21.247 -26.771 -8.658 1.00 102.24 ? 258 LYS A CD 1 ATOM 2072 C CE . LYS A 1 258 ? 19.774 -26.780 -9.038 1.00 105.93 ? 258 LYS A CE 1 ATOM 2073 N NZ . LYS A 1 258 ? 19.531 -25.974 -10.265 1.00 106.45 ? 258 LYS A NZ 1 ATOM 2074 N N . LYS A 1 259 ? 24.332 -29.593 -6.218 1.00 91.68 ? 259 LYS A N 1 ATOM 2075 C CA . LYS A 1 259 ? 25.708 -29.667 -6.704 1.00 90.54 ? 259 LYS A CA 1 ATOM 2076 C C . LYS A 1 259 ? 25.723 -29.618 -8.230 1.00 91.11 ? 259 LYS A C 1 ATOM 2077 O O . LYS A 1 259 ? 24.857 -30.201 -8.884 1.00 92.32 ? 259 LYS A O 1 ATOM 2078 C CB . LYS A 1 259 ? 26.366 -30.962 -6.232 1.00 91.43 ? 259 LYS A CB 1 ATOM 2079 C CG . LYS A 1 259 ? 26.652 -30.999 -4.745 1.00 93.07 ? 259 LYS A CG 1 ATOM 2080 C CD . LYS A 1 259 ? 27.128 -32.372 -4.298 1.00 95.09 ? 259 LYS A CD 1 ATOM 2081 C CE . LYS A 1 259 ? 27.424 -32.382 -2.806 1.00 96.81 ? 259 LYS A CE 1 ATOM 2082 N NZ . LYS A 1 259 ? 27.609 -33.755 -2.259 1.00 98.36 ? 259 LYS A NZ 1 ATOM 2083 N N . GLY A 1 260 ? 26.707 -28.930 -8.799 1.00 90.28 ? 260 GLY A N 1 ATOM 2084 C CA . GLY A 1 260 ? 26.820 -28.849 -10.256 1.00 91.62 ? 260 GLY A CA 1 ATOM 2085 C C . GLY A 1 260 ? 27.896 -27.900 -10.734 1.00 89.73 ? 260 GLY A C 1 ATOM 2086 O O . GLY A 1 260 ? 28.841 -27.610 -10.009 1.00 90.13 ? 260 GLY A O 1 ATOM 2087 N N . ASP A 1 261 ? 27.742 -27.411 -11.960 1.00 90.77 ? 261 ASP A N 1 ATOM 2088 C CA . ASP A 1 261 ? 28.749 -26.556 -12.592 1.00 89.72 ? 261 ASP A CA 1 ATOM 2089 C C . ASP A 1 261 ? 28.685 -25.131 -12.074 1.00 85.13 ? 261 ASP A C 1 ATOM 2090 O O . ASP A 1 261 ? 27.658 -24.462 -12.185 1.00 85.33 ? 261 ASP A O 1 ATOM 2091 C CB . ASP A 1 261 ? 28.576 -26.542 -14.117 1.00 94.37 ? 261 ASP A CB 1 ATOM 2092 C CG . ASP A 1 261 ? 29.256 -27.713 -14.796 1.00 99.36 ? 261 ASP A CG 1 ATOM 2093 O OD1 . ASP A 1 261 ? 30.140 -28.338 -14.167 1.00 101.81 ? 261 ASP A OD1 1 ATOM 2094 O OD2 . ASP A 1 261 ? 28.916 -27.999 -15.967 1.00 104.37 ? 261 ASP A OD2 1 ATOM 2095 N N . SER A 1 262 ? 29.801 -24.671 -11.527 1.00 80.75 ? 262 SER A N 1 ATOM 2096 C CA . SER A 1 262 ? 29.913 -23.310 -11.027 1.00 80.25 ? 262 SER A CA 1 ATOM 2097 C C . SER A 1 262 ? 31.375 -22.873 -11.104 1.00 78.87 ? 262 SER A C 1 ATOM 2098 O O . SER A 1 262 ? 32.238 -23.636 -11.543 1.00 78.60 ? 262 SER A O 1 ATOM 2099 C CB . SER A 1 262 ? 29.393 -23.227 -9.585 1.00 79.17 ? 262 SER A CB 1 ATOM 2100 O OG . SER A 1 262 ? 29.335 -21.887 -9.125 1.00 78.52 ? 262 SER A OG 1 ATOM 2101 N N . THR A 1 263 ? 31.641 -21.638 -10.688 1.00 75.20 ? 263 THR A N 1 ATOM 2102 C CA . THR A 1 263 ? 32.990 -21.102 -10.689 1.00 71.57 ? 263 THR A CA 1 ATOM 2103 C C . THR A 1 263 ? 33.015 -19.809 -9.901 1.00 69.73 ? 263 THR A C 1 ATOM 2104 O O . THR A 1 263 ? 32.023 -19.081 -9.862 1.00 70.54 ? 263 THR A O 1 ATOM 2105 C CB . THR A 1 263 ? 33.508 -20.841 -12.126 1.00 69.66 ? 263 THR A CB 1 ATOM 2106 O OG1 . THR A 1 263 ? 34.902 -20.528 -12.088 1.00 69.63 ? 263 THR A OG1 1 ATOM 2107 C CG2 . THR A 1 263 ? 32.774 -19.691 -12.789 1.00 68.40 ? 263 THR A CG2 1 ATOM 2108 N N . ILE A 1 264 ? 34.149 -19.537 -9.267 1.00 69.23 ? 264 ILE A N 1 ATOM 2109 C CA . ILE A 1 264 ? 34.374 -18.256 -8.615 1.00 67.62 ? 264 ILE A CA 1 ATOM 2110 C C . ILE A 1 264 ? 35.195 -17.396 -9.569 1.00 67.13 ? 264 ILE A C 1 ATOM 2111 O O . ILE A 1 264 ? 36.359 -17.680 -9.847 1.00 66.34 ? 264 ILE A O 1 ATOM 2112 C CB . ILE A 1 264 ? 35.077 -18.410 -7.258 1.00 66.74 ? 264 ILE A CB 1 ATOM 2113 C CG1 . ILE A 1 264 ? 34.261 -19.347 -6.358 1.00 68.82 ? 264 ILE A CG1 1 ATOM 2114 C CG2 . ILE A 1 264 ? 35.240 -17.050 -6.594 1.00 65.29 ? 264 ILE A CG2 1 ATOM 2115 C CD1 . ILE A 1 264 ? 34.979 -19.793 -5.102 1.00 70.29 ? 264 ILE A CD1 1 ATOM 2116 N N . MET A 1 265 ? 34.555 -16.348 -10.071 1.00 67.03 ? 265 MET A N 1 ATOM 2117 C CA . MET A 1 265 ? 35.108 -15.484 -11.094 1.00 66.67 ? 265 MET A CA 1 ATOM 2118 C C . MET A 1 265 ? 35.621 -14.219 -10.422 1.00 68.07 ? 265 MET A C 1 ATOM 2119 O O . MET A 1 265 ? 34.884 -13.569 -9.697 1.00 70.18 ? 265 MET A O 1 ATOM 2120 C CB . MET A 1 265 ? 33.981 -15.155 -12.063 1.00 67.69 ? 265 MET A CB 1 ATOM 2121 C CG . MET A 1 265 ? 34.359 -14.411 -13.321 1.00 68.02 ? 265 MET A CG 1 ATOM 2122 S SD . MET A 1 265 ? 32.899 -14.271 -14.373 1.00 69.95 ? 265 MET A SD 1 ATOM 2123 C CE . MET A 1 265 ? 32.758 -15.948 -14.995 1.00 68.80 ? 265 MET A CE 1 ATOM 2124 N N . LYS A 1 266 ? 36.889 -13.885 -10.634 1.00 69.80 ? 266 LYS A N 1 ATOM 2125 C CA . LYS A 1 266 ? 37.472 -12.694 -10.025 1.00 72.46 ? 266 LYS A CA 1 ATOM 2126 C C . LYS A 1 266 ? 37.275 -11.510 -10.967 1.00 72.77 ? 266 LYS A C 1 ATOM 2127 O O . LYS A 1 266 ? 37.747 -11.531 -12.104 1.00 73.56 ? 266 LYS A O 1 ATOM 2128 C CB . LYS A 1 266 ? 38.960 -12.904 -9.716 1.00 75.63 ? 266 LYS A CB 1 ATOM 2129 C CG . LYS A 1 266 ? 39.273 -14.157 -8.898 1.00 79.14 ? 266 LYS A CG 1 ATOM 2130 C CD . LYS A 1 266 ? 38.806 -14.065 -7.448 1.00 82.02 ? 266 LYS A CD 1 ATOM 2131 C CE . LYS A 1 266 ? 39.775 -13.260 -6.595 1.00 86.50 ? 266 LYS A CE 1 ATOM 2132 N NZ . LYS A 1 266 ? 39.185 -12.846 -5.285 1.00 90.15 ? 266 LYS A NZ 1 ATOM 2133 N N . SER A 1 267 ? 36.571 -10.486 -10.491 1.00 75.01 ? 267 SER A N 1 ATOM 2134 C CA . SER A 1 267 ? 36.209 -9.332 -11.316 1.00 75.71 ? 267 SER A CA 1 ATOM 2135 C C . SER A 1 267 ? 35.799 -8.135 -10.455 1.00 78.17 ? 267 SER A C 1 ATOM 2136 O O . SER A 1 267 ? 35.214 -8.302 -9.382 1.00 79.42 ? 267 SER A O 1 ATOM 2137 C CB . SER A 1 267 ? 35.057 -9.712 -12.250 1.00 75.92 ? 267 SER A CB 1 ATOM 2138 O OG . SER A 1 267 ? 34.582 -8.591 -12.976 1.00 78.58 ? 267 SER A OG 1 ATOM 2139 N N . GLU A 1 268 ? 36.108 -6.932 -10.934 1.00 79.72 ? 268 GLU A N 1 ATOM 2140 C CA . GLU A 1 268 ? 35.718 -5.695 -10.254 1.00 80.15 ? 268 GLU A CA 1 ATOM 2141 C C . GLU A 1 268 ? 34.389 -5.149 -10.779 1.00 80.78 ? 268 GLU A C 1 ATOM 2142 O O . GLU A 1 268 ? 33.881 -4.157 -10.260 1.00 85.57 ? 268 GLU A O 1 ATOM 2143 C CB . GLU A 1 268 ? 36.797 -4.621 -10.415 1.00 82.30 ? 268 GLU A CB 1 ATOM 2144 C CG . GLU A 1 268 ? 38.209 -5.060 -10.055 1.00 82.98 ? 268 GLU A CG 1 ATOM 2145 C CD . GLU A 1 268 ? 38.334 -5.582 -8.634 1.00 84.69 ? 268 GLU A CD 1 ATOM 2146 O OE1 . GLU A 1 268 ? 37.829 -4.917 -7.697 1.00 84.86 ? 268 GLU A OE1 1 ATOM 2147 O OE2 . GLU A 1 268 ? 38.952 -6.659 -8.460 1.00 83.36 ? 268 GLU A OE2 1 ATOM 2148 N N . LEU A 1 269 ? 33.825 -5.795 -11.796 1.00 79.52 ? 269 LEU A N 1 ATOM 2149 C CA . LEU A 1 269 ? 32.574 -5.335 -12.400 1.00 81.73 ? 269 LEU A CA 1 ATOM 2150 C C . LEU A 1 269 ? 31.377 -5.711 -11.541 1.00 82.27 ? 269 LEU A C 1 ATOM 2151 O O . LEU A 1 269 ? 31.426 -6.678 -10.786 1.00 78.94 ? 269 LEU A O 1 ATOM 2152 C CB . LEU A 1 269 ? 32.395 -5.929 -13.802 1.00 81.00 ? 269 LEU A CB 1 ATOM 2153 C CG . LEU A 1 269 ? 33.513 -5.686 -14.820 1.00 80.04 ? 269 LEU A CG 1 ATOM 2154 C CD1 . LEU A 1 269 ? 33.233 -6.471 -16.089 1.00 79.88 ? 269 LEU A CD1 1 ATOM 2155 C CD2 . LEU A 1 269 ? 33.673 -4.206 -15.135 1.00 83.32 ? 269 LEU A CD2 1 ATOM 2156 N N . GLU A 1 270 ? 30.305 -4.931 -11.672 1.00 88.87 ? 270 GLU A N 1 ATOM 2157 C CA . GLU A 1 270 ? 29.046 -5.179 -10.968 1.00 92.47 ? 270 GLU A CA 1 ATOM 2158 C C . GLU A 1 270 ? 28.029 -5.807 -11.934 1.00 90.30 ? 270 GLU A C 1 ATOM 2159 O O . GLU A 1 270 ? 28.337 -6.026 -13.105 1.00 88.20 ? 270 GLU A O 1 ATOM 2160 C CB . GLU A 1 270 ? 28.491 -3.869 -10.383 1.00 98.63 ? 270 GLU A CB 1 ATOM 2161 C CG . GLU A 1 270 ? 29.467 -3.068 -9.521 1.00 101.97 ? 270 GLU A CG 1 ATOM 2162 C CD . GLU A 1 270 ? 29.576 -3.570 -8.084 1.00 103.13 ? 270 GLU A CD 1 ATOM 2163 O OE1 . GLU A 1 270 ? 29.728 -4.795 -7.872 1.00 103.52 ? 270 GLU A OE1 1 ATOM 2164 O OE2 . GLU A 1 270 ? 29.513 -2.733 -7.157 1.00 104.62 ? 270 GLU A OE2 1 ATOM 2165 N N . TYR A 1 271 ? 26.824 -6.086 -11.438 1.00 90.22 ? 271 TYR A N 1 ATOM 2166 C CA . TYR A 1 271 ? 25.765 -6.716 -12.234 1.00 90.14 ? 271 TYR A CA 1 ATOM 2167 C C . TYR A 1 271 ? 25.336 -5.838 -13.410 1.00 93.51 ? 271 TYR A C 1 ATOM 2168 O O . TYR A 1 271 ? 25.282 -4.613 -13.291 1.00 95.08 ? 271 TYR A O 1 ATOM 2169 C CB . TYR A 1 271 ? 24.552 -7.011 -11.348 1.00 91.86 ? 271 TYR A CB 1 ATOM 2170 C CG . TYR A 1 271 ? 23.451 -7.811 -12.014 1.00 91.47 ? 271 TYR A CG 1 ATOM 2171 C CD1 . TYR A 1 271 ? 23.714 -9.041 -12.609 1.00 87.28 ? 271 TYR A CD1 1 ATOM 2172 C CD2 . TYR A 1 271 ? 22.140 -7.350 -12.019 1.00 94.33 ? 271 TYR A CD2 1 ATOM 2173 C CE1 . TYR A 1 271 ? 22.705 -9.779 -13.203 1.00 87.98 ? 271 TYR A CE1 1 ATOM 2174 C CE2 . TYR A 1 271 ? 21.126 -8.081 -12.610 1.00 95.24 ? 271 TYR A CE2 1 ATOM 2175 C CZ . TYR A 1 271 ? 21.412 -9.294 -13.198 1.00 92.40 ? 271 TYR A CZ 1 ATOM 2176 O OH . TYR A 1 271 ? 20.397 -10.012 -13.779 1.00 93.98 ? 271 TYR A OH 1 ATOM 2177 N N . GLY A 1 272 ? 25.017 -6.477 -14.534 1.00 93.75 ? 272 GLY A N 1 ATOM 2178 C CA . GLY A 1 272 ? 24.727 -5.766 -15.778 1.00 96.29 ? 272 GLY A CA 1 ATOM 2179 C C . GLY A 1 272 ? 23.268 -5.713 -16.200 1.00 101.40 ? 272 GLY A C 1 ATOM 2180 O O . GLY A 1 272 ? 22.956 -5.083 -17.212 1.00 102.11 ? 272 GLY A O 1 ATOM 2181 N N . ASN A 1 273 ? 22.378 -6.355 -15.439 1.00 104.86 ? 273 ASN A N 1 ATOM 2182 C CA . ASN A 1 273 ? 20.955 -6.471 -15.810 1.00 110.53 ? 273 ASN A CA 1 ATOM 2183 C C . ASN A 1 273 ? 20.846 -6.983 -17.237 1.00 108.20 ? 273 ASN A C 1 ATOM 2184 O O . ASN A 1 273 ? 20.494 -6.247 -18.157 1.00 109.96 ? 273 ASN A O 1 ATOM 2185 C CB . ASN A 1 273 ? 20.229 -5.130 -15.644 1.00 116.16 ? 273 ASN A CB 1 ATOM 2186 C CG . ASN A 1 273 ? 19.970 -4.787 -14.190 1.00 121.35 ? 273 ASN A CG 1 ATOM 2187 O OD1 . ASN A 1 273 ? 20.718 -4.024 -13.574 1.00 123.04 ? 273 ASN A OD1 1 ATOM 2188 N ND2 . ASN A 1 273 ? 18.910 -5.360 -13.627 1.00 124.61 ? 273 ASN A ND2 1 ATOM 2189 N N . CYS A 1 274 ? 21.152 -8.262 -17.405 1.00 105.06 ? 274 CYS A N 1 ATOM 2190 C CA . CYS A 1 274 ? 21.651 -8.755 -18.678 1.00 102.96 ? 274 CYS A CA 1 ATOM 2191 C C . CYS A 1 274 ? 21.618 -10.283 -18.735 1.00 96.93 ? 274 CYS A C 1 ATOM 2192 O O . CYS A 1 274 ? 21.672 -10.941 -17.697 1.00 95.57 ? 274 CYS A O 1 ATOM 2193 C CB . CYS A 1 274 ? 23.090 -8.244 -18.824 1.00 102.72 ? 274 CYS A CB 1 ATOM 2194 S SG . CYS A 1 274 ? 24.054 -8.979 -20.147 1.00 108.46 ? 274 CYS A SG 1 ATOM 2195 N N . ASN A 1 275 ? 21.541 -10.846 -19.941 1.00 94.14 ? 275 ASN A N 1 ATOM 2196 C CA . ASN A 1 275 ? 21.539 -12.309 -20.115 1.00 92.48 ? 275 ASN A CA 1 ATOM 2197 C C . ASN A 1 275 ? 22.484 -12.790 -21.231 1.00 89.93 ? 275 ASN A C 1 ATOM 2198 O O . ASN A 1 275 ? 22.623 -12.136 -22.269 1.00 91.21 ? 275 ASN A O 1 ATOM 2199 C CB . ASN A 1 275 ? 20.110 -12.807 -20.377 1.00 94.97 ? 275 ASN A CB 1 ATOM 2200 C CG . ASN A 1 275 ? 19.969 -14.314 -20.216 1.00 93.42 ? 275 ASN A CG 1 ATOM 2201 O OD1 . ASN A 1 275 ? 20.532 -14.910 -19.304 1.00 90.73 ? 275 ASN A OD1 1 ATOM 2202 N ND2 . ASN A 1 275 ? 19.202 -14.932 -21.101 1.00 96.00 ? 275 ASN A ND2 1 ATOM 2203 N N . THR A 1 276 ? 23.125 -13.938 -21.012 1.00 85.94 ? 276 THR A N 1 ATOM 2204 C CA . THR A 1 276 ? 24.093 -14.482 -21.964 1.00 81.44 ? 276 THR A CA 1 ATOM 2205 C C . THR A 1 276 ? 24.157 -16.001 -21.870 1.00 80.47 ? 276 THR A C 1 ATOM 2206 O O . THR A 1 276 ? 23.574 -16.593 -20.970 1.00 83.82 ? 276 THR A O 1 ATOM 2207 C CB . THR A 1 276 ? 25.499 -13.891 -21.713 1.00 78.81 ? 276 THR A CB 1 ATOM 2208 O OG1 . THR A 1 276 ? 26.380 -14.239 -22.787 1.00 77.92 ? 276 THR A OG1 1 ATOM 2209 C CG2 . THR A 1 276 ? 26.088 -14.394 -20.391 1.00 78.41 ? 276 THR A CG2 1 ATOM 2210 N N . LYS A 1 277 ? 24.861 -16.616 -22.813 1.00 79.83 ? 277 LYS A N 1 ATOM 2211 C CA . LYS A 1 277 ? 25.110 -18.062 -22.817 1.00 82.69 ? 277 LYS A CA 1 ATOM 2212 C C . LYS A 1 277 ? 26.566 -18.391 -22.472 1.00 76.60 ? 277 LYS A C 1 ATOM 2213 O O . LYS A 1 277 ? 26.927 -19.554 -22.309 1.00 74.67 ? 277 LYS A O 1 ATOM 2214 C CB . LYS A 1 277 ? 24.792 -18.643 -24.200 1.00 89.10 ? 277 LYS A CB 1 ATOM 2215 C CG . LYS A 1 277 ? 23.309 -18.736 -24.527 1.00 98.40 ? 277 LYS A CG 1 ATOM 2216 C CD . LYS A 1 277 ? 22.684 -19.990 -23.931 1.00 105.95 ? 277 LYS A CD 1 ATOM 2217 C CE . LYS A 1 277 ? 21.241 -20.163 -24.380 1.00 112.97 ? 277 LYS A CE 1 ATOM 2218 N NZ . LYS A 1 277 ? 20.629 -21.401 -23.821 1.00 117.98 ? 277 LYS A NZ 1 ATOM 2219 N N . CYS A 1 278 ? 27.402 -17.365 -22.383 1.00 72.81 ? 278 CYS A N 1 ATOM 2220 C CA . CYS A 1 278 ? 28.828 -17.550 -22.203 1.00 71.83 ? 278 CYS A CA 1 ATOM 2221 C C . CYS A 1 278 ? 29.371 -16.309 -21.530 1.00 69.27 ? 278 CYS A C 1 ATOM 2222 O O . CYS A 1 278 ? 29.257 -15.211 -22.077 1.00 70.63 ? 278 CYS A O 1 ATOM 2223 C CB . CYS A 1 278 ? 29.507 -17.750 -23.559 1.00 73.29 ? 278 CYS A CB 1 ATOM 2224 S SG . CYS A 1 278 ? 31.319 -17.728 -23.512 1.00 75.48 ? 278 CYS A SG 1 ATOM 2225 N N . GLN A 1 279 ? 29.955 -16.476 -20.348 1.00 66.51 ? 279 GLN A N 1 ATOM 2226 C CA . GLN A 1 279 ? 30.367 -15.333 -19.542 1.00 66.12 ? 279 GLN A CA 1 ATOM 2227 C C . GLN A 1 279 ? 31.864 -15.336 -19.278 1.00 62.59 ? 279 GLN A C 1 ATOM 2228 O O . GLN A 1 279 ? 32.453 -16.393 -19.054 1.00 61.86 ? 279 GLN A O 1 ATOM 2229 C CB . GLN A 1 279 ? 29.608 -15.334 -18.211 1.00 67.92 ? 279 GLN A CB 1 ATOM 2230 C CG . GLN A 1 279 ? 29.863 -14.108 -17.347 1.00 67.45 ? 279 GLN A CG 1 ATOM 2231 C CD . GLN A 1 279 ? 29.218 -12.858 -17.907 1.00 68.64 ? 279 GLN A CD 1 ATOM 2232 O OE1 . GLN A 1 279 ? 27.996 -12.786 -18.033 1.00 70.65 ? 279 GLN A OE1 1 ATOM 2233 N NE2 . GLN A 1 279 ? 30.033 -11.863 -18.239 1.00 68.06 ? 279 GLN A NE2 1 ATOM 2234 N N . THR A 1 280 ? 32.461 -14.145 -19.300 1.00 60.53 ? 280 THR A N 1 ATOM 2235 C CA . THR A 1 280 ? 33.857 -13.956 -18.926 1.00 60.13 ? 280 THR A CA 1 ATOM 2236 C C . THR A 1 280 ? 33.990 -12.857 -17.867 1.00 61.85 ? 280 THR A C 1 ATOM 2237 O O . THR A 1 280 ? 33.098 -12.016 -17.721 1.00 61.43 ? 280 THR A O 1 ATOM 2238 C CB . THR A 1 280 ? 34.722 -13.554 -20.135 1.00 59.85 ? 280 THR A CB 1 ATOM 2239 O OG1 . THR A 1 280 ? 34.675 -12.133 -20.312 1.00 59.67 ? 280 THR A OG1 1 ATOM 2240 C CG2 . THR A 1 280 ? 34.253 -14.260 -21.411 1.00 59.68 ? 280 THR A CG2 1 ATOM 2241 N N . PRO A 1 281 ? 35.118 -12.843 -17.138 1.00 64.12 ? 281 PRO A N 1 ATOM 2242 C CA . PRO A 1 281 ? 35.393 -11.821 -16.115 1.00 66.17 ? 281 PRO A CA 1 ATOM 2243 C C . PRO A 1 281 ? 35.381 -10.368 -16.596 1.00 68.83 ? 281 PRO A C 1 ATOM 2244 O O . PRO A 1 281 ? 35.373 -9.460 -15.761 1.00 69.63 ? 281 PRO A O 1 ATOM 2245 C CB . PRO A 1 281 ? 36.798 -12.176 -15.628 1.00 65.77 ? 281 PRO A CB 1 ATOM 2246 C CG . PRO A 1 281 ? 36.957 -13.624 -15.911 1.00 65.04 ? 281 PRO A CG 1 ATOM 2247 C CD . PRO A 1 281 ? 36.078 -13.960 -17.076 1.00 63.45 ? 281 PRO A CD 1 ATOM 2248 N N . MET A 1 282 ? 35.400 -10.136 -17.908 1.00 71.85 ? 282 MET A N 1 ATOM 2249 C CA . MET A 1 282 ? 35.316 -8.765 -18.425 1.00 76.01 ? 282 MET A CA 1 ATOM 2250 C C . MET A 1 282 ? 34.123 -8.513 -19.341 1.00 73.01 ? 282 MET A C 1 ATOM 2251 O O . MET A 1 282 ? 33.994 -7.422 -19.899 1.00 74.20 ? 282 MET A O 1 ATOM 2252 C CB . MET A 1 282 ? 36.623 -8.352 -19.104 1.00 81.47 ? 282 MET A CB 1 ATOM 2253 C CG . MET A 1 282 ? 37.148 -9.310 -20.153 1.00 85.94 ? 282 MET A CG 1 ATOM 2254 S SD . MET A 1 282 ? 38.793 -8.813 -20.704 1.00 98.58 ? 282 MET A SD 1 ATOM 2255 C CE . MET A 1 282 ? 39.674 -8.696 -19.141 1.00 97.60 ? 282 MET A CE 1 ATOM 2256 N N . GLY A 1 283 ? 33.235 -9.495 -19.463 1.00 68.71 ? 283 GLY A N 1 ATOM 2257 C CA . GLY A 1 283 ? 32.009 -9.319 -20.235 1.00 68.51 ? 283 GLY A CA 1 ATOM 2258 C C . GLY A 1 283 ? 31.509 -10.610 -20.842 1.00 67.17 ? 283 GLY A C 1 ATOM 2259 O O . GLY A 1 283 ? 32.231 -11.607 -20.892 1.00 65.41 ? 283 GLY A O 1 ATOM 2260 N N . ALA A 1 284 ? 30.269 -10.580 -21.317 1.00 67.69 ? 284 ALA A N 1 ATOM 2261 C CA . ALA A 1 284 ? 29.630 -11.753 -21.900 1.00 68.36 ? 284 ALA A CA 1 ATOM 2262 C C . ALA A 1 284 ? 29.896 -11.849 -23.407 1.00 69.46 ? 284 ALA A C 1 ATOM 2263 O O . ALA A 1 284 ? 30.192 -10.844 -24.069 1.00 68.24 ? 284 ALA A O 1 ATOM 2264 C CB . ALA A 1 284 ? 28.136 -11.713 -21.635 1.00 71.25 ? 284 ALA A CB 1 ATOM 2265 N N . ILE A 1 285 ? 29.767 -13.066 -23.931 1.00 69.12 ? 285 ILE A N 1 ATOM 2266 C CA . ILE A 1 285 ? 30.014 -13.363 -25.343 1.00 70.06 ? 285 ILE A CA 1 ATOM 2267 C C . ILE A 1 285 ? 28.744 -13.896 -25.994 1.00 73.93 ? 285 ILE A C 1 ATOM 2268 O O . ILE A 1 285 ? 28.045 -14.743 -25.433 1.00 76.69 ? 285 ILE A O 1 ATOM 2269 C CB . ILE A 1 285 ? 31.157 -14.396 -25.510 1.00 66.44 ? 285 ILE A CB 1 ATOM 2270 C CG1 . ILE A 1 285 ? 32.512 -13.702 -25.413 1.00 64.46 ? 285 ILE A CG1 1 ATOM 2271 C CG2 . ILE A 1 285 ? 31.078 -15.107 -26.850 1.00 67.13 ? 285 ILE A CG2 1 ATOM 2272 C CD1 . ILE A 1 285 ? 33.657 -14.646 -25.125 1.00 63.33 ? 285 ILE A CD1 1 ATOM 2273 N N . ASN A 1 286 ? 28.464 -13.388 -27.189 1.00 78.36 ? 286 ASN A N 1 ATOM 2274 C CA . ASN A 1 286 ? 27.333 -13.831 -27.985 1.00 84.40 ? 286 ASN A CA 1 ATOM 2275 C C . ASN A 1 286 ? 27.762 -13.927 -29.441 1.00 81.26 ? 286 ASN A C 1 ATOM 2276 O O . ASN A 1 286 ? 27.639 -12.969 -30.200 1.00 80.75 ? 286 ASN A O 1 ATOM 2277 C CB . ASN A 1 286 ? 26.169 -12.851 -27.824 1.00 92.66 ? 286 ASN A CB 1 ATOM 2278 C CG . ASN A 1 286 ? 24.997 -13.179 -28.725 1.00 105.01 ? 286 ASN A CG 1 ATOM 2279 O OD1 . ASN A 1 286 ? 24.626 -14.346 -28.877 1.00 103.98 ? 286 ASN A OD1 1 ATOM 2280 N ND2 . ASN A 1 286 ? 24.406 -12.142 -29.330 1.00 120.64 ? 286 ASN A ND2 1 ATOM 2281 N N . SER A 1 287 ? 28.296 -15.081 -29.823 1.00 78.38 ? 287 SER A N 1 ATOM 2282 C CA . SER A 1 287 ? 28.656 -15.312 -31.215 1.00 77.99 ? 287 SER A CA 1 ATOM 2283 C C . SER A 1 287 ? 28.683 -16.789 -31.567 1.00 76.43 ? 287 SER A C 1 ATOM 2284 O O . SER A 1 287 ? 28.704 -17.650 -30.692 1.00 74.24 ? 287 SER A O 1 ATOM 2285 C CB . SER A 1 287 ? 30.010 -14.669 -31.539 1.00 76.28 ? 287 SER A CB 1 ATOM 2286 O OG . SER A 1 287 ? 31.090 -15.512 -31.195 1.00 73.13 ? 287 SER A OG 1 ATOM 2287 N N . SER A 1 288 ? 28.681 -17.063 -32.866 1.00 77.78 ? 288 SER A N 1 ATOM 2288 C CA . SER A 1 288 ? 28.741 -18.427 -33.372 1.00 78.66 ? 288 SER A CA 1 ATOM 2289 C C . SER A 1 288 ? 30.156 -18.800 -33.827 1.00 73.01 ? 288 SER A C 1 ATOM 2290 O O . SER A 1 288 ? 30.361 -19.871 -34.386 1.00 73.85 ? 288 SER A O 1 ATOM 2291 C CB . SER A 1 288 ? 27.748 -18.589 -34.524 1.00 84.21 ? 288 SER A CB 1 ATOM 2292 O OG . SER A 1 288 ? 27.975 -17.608 -35.523 1.00 86.98 ? 288 SER A OG 1 ATOM 2293 N N . MET A 1 289 ? 31.130 -17.930 -33.569 1.00 69.50 ? 289 MET A N 1 ATOM 2294 C CA . MET A 1 289 ? 32.516 -18.188 -33.961 1.00 68.30 ? 289 MET A CA 1 ATOM 2295 C C . MET A 1 289 ? 33.075 -19.354 -33.152 1.00 67.95 ? 289 MET A C 1 ATOM 2296 O O . MET A 1 289 ? 32.693 -19.536 -32.004 1.00 71.09 ? 289 MET A O 1 ATOM 2297 C CB . MET A 1 289 ? 33.395 -16.969 -33.695 1.00 69.47 ? 289 MET A CB 1 ATOM 2298 C CG . MET A 1 289 ? 32.964 -15.677 -34.366 1.00 70.66 ? 289 MET A CG 1 ATOM 2299 S SD . MET A 1 289 ? 33.358 -15.639 -36.115 1.00 72.35 ? 289 MET A SD 1 ATOM 2300 C CE . MET A 1 289 ? 33.758 -13.899 -36.292 1.00 70.69 ? 289 MET A CE 1 ATOM 2301 N N . PRO A 1 290 ? 33.989 -20.143 -33.741 1.00 66.41 ? 290 PRO A N 1 ATOM 2302 C CA . PRO A 1 290 ? 34.613 -21.244 -33.002 1.00 65.04 ? 290 PRO A CA 1 ATOM 2303 C C . PRO A 1 290 ? 35.701 -20.812 -32.018 1.00 62.28 ? 290 PRO A C 1 ATOM 2304 O O . PRO A 1 290 ? 36.112 -21.612 -31.186 1.00 64.17 ? 290 PRO A O 1 ATOM 2305 C CB . PRO A 1 290 ? 35.232 -22.089 -34.114 1.00 64.98 ? 290 PRO A CB 1 ATOM 2306 C CG . PRO A 1 290 ? 35.561 -21.094 -35.172 1.00 64.49 ? 290 PRO A CG 1 ATOM 2307 C CD . PRO A 1 290 ? 34.418 -20.126 -35.152 1.00 64.91 ? 290 PRO A CD 1 ATOM 2308 N N . PHE A 1 291 ? 36.166 -19.570 -32.121 1.00 59.83 ? 291 PHE A N 1 ATOM 2309 C CA . PHE A 1 291 ? 37.262 -19.074 -31.297 1.00 57.89 ? 291 PHE A CA 1 ATOM 2310 C C . PHE A 1 291 ? 36.948 -17.699 -30.761 1.00 56.09 ? 291 PHE A C 1 ATOM 2311 O O . PHE A 1 291 ? 36.157 -16.970 -31.352 1.00 56.50 ? 291 PHE A O 1 ATOM 2312 C CB . PHE A 1 291 ? 38.534 -18.915 -32.126 1.00 59.88 ? 291 PHE A CB 1 ATOM 2313 C CG . PHE A 1 291 ? 39.149 -20.202 -32.578 1.00 61.73 ? 291 PHE A CG 1 ATOM 2314 C CD1 . PHE A 1 291 ? 39.886 -20.977 -31.698 1.00 64.26 ? 291 PHE A CD1 1 ATOM 2315 C CD2 . PHE A 1 291 ? 39.035 -20.613 -33.897 1.00 64.06 ? 291 PHE A CD2 1 ATOM 2316 C CE1 . PHE A 1 291 ? 40.478 -22.155 -32.118 1.00 65.90 ? 291 PHE A CE1 1 ATOM 2317 C CE2 . PHE A 1 291 ? 39.623 -21.788 -34.326 1.00 65.07 ? 291 PHE A CE2 1 ATOM 2318 C CZ . PHE A 1 291 ? 40.344 -22.558 -33.434 1.00 66.74 ? 291 PHE A CZ 1 ATOM 2319 N N . HIS A 1 292 ? 37.605 -17.334 -29.662 1.00 55.37 ? 292 HIS A N 1 ATOM 2320 C CA . HIS A 1 292 ? 37.590 -15.952 -29.175 1.00 53.71 ? 292 HIS A CA 1 ATOM 2321 C C . HIS A 1 292 ? 38.896 -15.618 -28.468 1.00 52.65 ? 292 HIS A C 1 ATOM 2322 O O . HIS A 1 292 ? 39.686 -16.517 -28.171 1.00 51.97 ? 292 HIS A O 1 ATOM 2323 C CB . HIS A 1 292 ? 36.406 -15.717 -28.242 1.00 55.42 ? 292 HIS A CB 1 ATOM 2324 C CG . HIS A 1 292 ? 36.539 -16.379 -26.907 1.00 55.89 ? 292 HIS A CG 1 ATOM 2325 N ND1 . HIS A 1 292 ? 37.174 -15.786 -25.839 1.00 54.69 ? 292 HIS A ND1 1 ATOM 2326 C CD2 . HIS A 1 292 ? 36.097 -17.576 -26.462 1.00 56.86 ? 292 HIS A CD2 1 ATOM 2327 C CE1 . HIS A 1 292 ? 37.131 -16.595 -24.799 1.00 55.87 ? 292 HIS A CE1 1 ATOM 2328 N NE2 . HIS A 1 292 ? 36.484 -17.690 -25.150 1.00 57.36 ? 292 HIS A NE2 1 ATOM 2329 N N . ASN A 1 293 ? 39.123 -14.331 -28.204 1.00 51.74 ? 293 ASN A N 1 ATOM 2330 C CA . ASN A 1 293 ? 40.344 -13.884 -27.520 1.00 52.32 ? 293 ASN A CA 1 ATOM 2331 C C . ASN A 1 293 ? 40.076 -12.916 -26.358 1.00 53.98 ? 293 ASN A C 1 ATOM 2332 O O . ASN A 1 293 ? 40.935 -12.110 -25.991 1.00 56.26 ? 293 ASN A O 1 ATOM 2333 C CB . ASN A 1 293 ? 41.301 -13.256 -28.534 1.00 53.17 ? 293 ASN A CB 1 ATOM 2334 C CG . ASN A 1 293 ? 40.786 -11.945 -29.102 1.00 54.57 ? 293 ASN A CG 1 ATOM 2335 O OD1 . ASN A 1 293 ? 39.674 -11.514 -28.812 1.00 54.33 ? 293 ASN A OD1 1 ATOM 2336 N ND2 . ASN A 1 293 ? 41.601 -11.304 -29.919 1.00 56.95 ? 293 ASN A ND2 1 ATOM 2337 N N . ILE A 1 294 ? 38.881 -13.002 -25.788 1.00 54.69 ? 294 ILE A N 1 ATOM 2338 C CA . ILE A 1 294 ? 38.464 -12.129 -24.686 1.00 56.91 ? 294 ILE A CA 1 ATOM 2339 C C . ILE A 1 294 ? 39.203 -12.449 -23.393 1.00 57.41 ? 294 ILE A C 1 ATOM 2340 O O . ILE A 1 294 ? 39.878 -11.587 -22.836 1.00 58.95 ? 294 ILE A O 1 ATOM 2341 C CB . ILE A 1 294 ? 36.942 -12.238 -24.416 1.00 57.12 ? 294 ILE A CB 1 ATOM 2342 C CG1 . ILE A 1 294 ? 36.132 -12.003 -25.699 1.00 57.94 ? 294 ILE A CG1 1 ATOM 2343 C CG2 . ILE A 1 294 ? 36.520 -11.252 -23.341 1.00 59.35 ? 294 ILE A CG2 1 ATOM 2344 C CD1 . ILE A 1 294 ? 36.583 -10.807 -26.514 1.00 59.78 ? 294 ILE A CD1 1 ATOM 2345 N N . HIS A 1 295 ? 39.068 -13.690 -22.925 1.00 58.29 ? 295 HIS A N 1 ATOM 2346 C CA . HIS A 1 295 ? 39.610 -14.102 -21.631 1.00 59.05 ? 295 HIS A CA 1 ATOM 2347 C C . HIS A 1 295 ? 39.594 -15.642 -21.474 1.00 57.10 ? 295 HIS A C 1 ATOM 2348 O O . HIS A 1 295 ? 38.611 -16.276 -21.849 1.00 54.64 ? 295 HIS A O 1 ATOM 2349 C CB . HIS A 1 295 ? 38.767 -13.457 -20.534 1.00 60.77 ? 295 HIS A CB 1 ATOM 2350 C CG . HIS A 1 295 ? 39.432 -13.425 -19.202 1.00 63.47 ? 295 HIS A CG 1 ATOM 2351 N ND1 . HIS A 1 295 ? 39.507 -14.531 -18.390 1.00 64.24 ? 295 HIS A ND1 1 ATOM 2352 C CD2 . HIS A 1 295 ? 40.042 -12.421 -18.531 1.00 66.55 ? 295 HIS A CD2 1 ATOM 2353 C CE1 . HIS A 1 295 ? 40.145 -14.217 -17.277 1.00 66.54 ? 295 HIS A CE1 1 ATOM 2354 N NE2 . HIS A 1 295 ? 40.477 -12.940 -17.337 1.00 67.30 ? 295 HIS A NE2 1 ATOM 2355 N N . PRO A 1 296 ? 40.666 -16.243 -20.904 1.00 57.97 ? 296 PRO A N 1 ATOM 2356 C CA . PRO A 1 296 ? 40.735 -17.716 -20.779 1.00 58.93 ? 296 PRO A CA 1 ATOM 2357 C C . PRO A 1 296 ? 39.710 -18.354 -19.839 1.00 59.03 ? 296 PRO A C 1 ATOM 2358 O O . PRO A 1 296 ? 39.257 -19.465 -20.085 1.00 59.32 ? 296 PRO A O 1 ATOM 2359 C CB . PRO A 1 296 ? 42.154 -17.963 -20.243 1.00 60.18 ? 296 PRO A CB 1 ATOM 2360 C CG . PRO A 1 296 ? 42.550 -16.687 -19.592 1.00 60.73 ? 296 PRO A CG 1 ATOM 2361 C CD . PRO A 1 296 ? 41.904 -15.607 -20.414 1.00 59.91 ? 296 PRO A CD 1 ATOM 2362 N N . LEU A 1 297 ? 39.378 -17.673 -18.753 1.00 61.15 ? 297 LEU A N 1 ATOM 2363 C CA . LEU A 1 297 ? 38.420 -18.192 -17.774 1.00 63.63 ? 297 LEU A CA 1 ATOM 2364 C C . LEU A 1 297 ? 36.991 -17.819 -18.158 1.00 63.27 ? 297 LEU A C 1 ATOM 2365 O O . LEU A 1 297 ? 36.556 -16.698 -17.921 1.00 66.48 ? 297 LEU A O 1 ATOM 2366 C CB . LEU A 1 297 ? 38.759 -17.668 -16.371 1.00 64.14 ? 297 LEU A CB 1 ATOM 2367 C CG . LEU A 1 297 ? 40.234 -17.822 -15.970 1.00 66.35 ? 297 LEU A CG 1 ATOM 2368 C CD1 . LEU A 1 297 ? 40.512 -17.224 -14.594 1.00 67.34 ? 297 LEU A CD1 1 ATOM 2369 C CD2 . LEU A 1 297 ? 40.646 -19.286 -16.024 1.00 67.72 ? 297 LEU A CD2 1 ATOM 2370 N N . THR A 1 298 ? 36.269 -18.754 -18.767 1.00 62.34 ? 298 THR A N 1 ATOM 2371 C CA . THR A 1 298 ? 34.874 -18.527 -19.137 1.00 60.70 ? 298 THR A CA 1 ATOM 2372 C C . THR A 1 298 ? 33.985 -19.594 -18.520 1.00 61.90 ? 298 THR A C 1 ATOM 2373 O O . THR A 1 298 ? 34.469 -20.623 -18.048 1.00 60.87 ? 298 THR A O 1 ATOM 2374 C CB . THR A 1 298 ? 34.679 -18.531 -20.667 1.00 60.43 ? 298 THR A CB 1 ATOM 2375 O OG1 . THR A 1 298 ? 34.744 -19.871 -21.172 1.00 60.97 ? 298 THR A OG1 1 ATOM 2376 C CG2 . THR A 1 298 ? 35.747 -17.686 -21.343 1.00 60.53 ? 298 THR A CG2 1 ATOM 2377 N N . ILE A 1 299 ? 32.682 -19.337 -18.519 1.00 63.16 ? 299 ILE A N 1 ATOM 2378 C CA . ILE A 1 299 ? 31.705 -20.330 -18.082 1.00 65.58 ? 299 ILE A CA 1 ATOM 2379 C C . ILE A 1 299 ? 30.516 -20.291 -19.029 1.00 67.33 ? 299 ILE A C 1 ATOM 2380 O O . ILE A 1 299 ? 30.117 -19.215 -19.481 1.00 66.84 ? 299 ILE A O 1 ATOM 2381 C CB . ILE A 1 299 ? 31.259 -20.105 -16.615 1.00 66.88 ? 299 ILE A CB 1 ATOM 2382 C CG1 . ILE A 1 299 ? 30.264 -21.187 -16.181 1.00 68.71 ? 299 ILE A CG1 1 ATOM 2383 C CG2 . ILE A 1 299 ? 30.651 -18.721 -16.416 1.00 66.39 ? 299 ILE A CG2 1 ATOM 2384 C CD1 . ILE A 1 299 ? 29.992 -21.200 -14.694 1.00 70.02 ? 299 ILE A CD1 1 ATOM 2385 N N . GLY A 1 300 ? 29.965 -21.468 -19.322 1.00 70.89 ? 300 GLY A N 1 ATOM 2386 C CA . GLY A 1 300 ? 28.854 -21.609 -20.261 1.00 75.88 ? 300 GLY A CA 1 ATOM 2387 C C . GLY A 1 300 ? 29.266 -22.367 -21.513 1.00 79.44 ? 300 GLY A C 1 ATOM 2388 O O . GLY A 1 300 ? 30.268 -23.087 -21.512 1.00 79.94 ? 300 GLY A O 1 ATOM 2389 N N . GLU A 1 301 ? 28.489 -22.208 -22.580 1.00 83.14 ? 301 GLU A N 1 ATOM 2390 C CA . GLU A 1 301 ? 28.808 -22.827 -23.862 1.00 87.02 ? 301 GLU A CA 1 ATOM 2391 C C . GLU A 1 301 ? 29.570 -21.797 -24.677 1.00 80.49 ? 301 GLU A C 1 ATOM 2392 O O . GLU A 1 301 ? 28.973 -20.876 -25.237 1.00 79.14 ? 301 GLU A O 1 ATOM 2393 C CB . GLU A 1 301 ? 27.536 -23.279 -24.590 1.00 95.53 ? 301 GLU A CB 1 ATOM 2394 C CG . GLU A 1 301 ? 27.686 -24.613 -25.309 1.00 103.42 ? 301 GLU A CG 1 ATOM 2395 C CD . GLU A 1 301 ? 27.816 -25.782 -24.341 1.00 109.90 ? 301 GLU A CD 1 ATOM 2396 O OE1 . GLU A 1 301 ? 26.870 -26.018 -23.556 1.00 113.43 ? 301 GLU A OE1 1 ATOM 2397 O OE2 . GLU A 1 301 ? 28.871 -26.455 -24.352 1.00 113.81 ? 301 GLU A OE2 1 ATOM 2398 N N . CYS A 1 302 ? 30.891 -21.949 -24.726 1.00 75.87 ? 302 CYS A N 1 ATOM 2399 C CA . CYS A 1 302 ? 31.762 -20.907 -25.256 1.00 72.74 ? 302 CYS A CA 1 ATOM 2400 C C . CYS A 1 302 ? 32.614 -21.360 -26.440 1.00 70.34 ? 302 CYS A C 1 ATOM 2401 O O . CYS A 1 302 ? 32.850 -22.556 -26.633 1.00 68.13 ? 302 CYS A O 1 ATOM 2402 C CB . CYS A 1 302 ? 32.689 -20.397 -24.150 1.00 73.29 ? 302 CYS A CB 1 ATOM 2403 S SG . CYS A 1 302 ? 31.838 -19.579 -22.778 1.00 77.88 ? 302 CYS A SG 1 ATOM 2404 N N . PRO A 1 303 ? 33.089 -20.390 -27.239 1.00 68.03 ? 303 PRO A N 1 ATOM 2405 C CA . PRO A 1 303 ? 34.140 -20.691 -28.197 1.00 67.02 ? 303 PRO A CA 1 ATOM 2406 C C . PRO A 1 303 ? 35.451 -20.920 -27.462 1.00 66.20 ? 303 PRO A C 1 ATOM 2407 O O . PRO A 1 303 ? 35.573 -20.531 -26.301 1.00 67.29 ? 303 PRO A O 1 ATOM 2408 C CB . PRO A 1 303 ? 34.220 -19.426 -29.065 1.00 65.67 ? 303 PRO A CB 1 ATOM 2409 C CG . PRO A 1 303 ? 33.085 -18.550 -28.653 1.00 66.31 ? 303 PRO A CG 1 ATOM 2410 C CD . PRO A 1 303 ? 32.699 -18.971 -27.274 1.00 67.60 ? 303 PRO A CD 1 ATOM 2411 N N . LYS A 1 304 ? 36.423 -21.535 -28.129 1.00 66.06 ? 304 LYS A N 1 ATOM 2412 C CA . LYS A 1 304 ? 37.709 -21.822 -27.504 1.00 66.55 ? 304 LYS A CA 1 ATOM 2413 C C . LYS A 1 304 ? 38.567 -20.574 -27.492 1.00 62.92 ? 304 LYS A C 1 ATOM 2414 O O . LYS A 1 304 ? 38.673 -19.863 -28.490 1.00 62.98 ? 304 LYS A O 1 ATOM 2415 C CB . LYS A 1 304 ? 38.441 -22.952 -28.229 1.00 71.14 ? 304 LYS A CB 1 ATOM 2416 C CG . LYS A 1 304 ? 37.624 -24.234 -28.378 1.00 77.86 ? 304 LYS A CG 1 ATOM 2417 C CD . LYS A 1 304 ? 37.291 -24.886 -27.039 1.00 83.16 ? 304 LYS A CD 1 ATOM 2418 C CE . LYS A 1 304 ? 35.871 -25.432 -27.012 1.00 86.79 ? 304 LYS A CE 1 ATOM 2419 N NZ . LYS A 1 304 ? 35.610 -26.191 -25.758 1.00 90.81 ? 304 LYS A NZ 1 ATOM 2420 N N . TYR A 1 305 ? 39.173 -20.306 -26.348 1.00 60.51 ? 305 TYR A N 1 ATOM 2421 C CA . TYR A 1 305 ? 40.016 -19.144 -26.195 1.00 58.98 ? 305 TYR A CA 1 ATOM 2422 C C . TYR A 1 305 ? 41.360 -19.382 -26.871 1.00 58.47 ? 305 TYR A C 1 ATOM 2423 O O . TYR A 1 305 ? 41.974 -20.432 -26.696 1.00 59.26 ? 305 TYR A O 1 ATOM 2424 C CB . TYR A 1 305 ? 40.233 -18.829 -24.712 1.00 59.43 ? 305 TYR A CB 1 ATOM 2425 C CG . TYR A 1 305 ? 41.196 -17.693 -24.478 1.00 57.85 ? 305 TYR A CG 1 ATOM 2426 C CD1 . TYR A 1 305 ? 40.785 -16.373 -24.598 1.00 56.56 ? 305 TYR A CD1 1 ATOM 2427 C CD2 . TYR A 1 305 ? 42.517 -17.937 -24.154 1.00 59.31 ? 305 TYR A CD2 1 ATOM 2428 C CE1 . TYR A 1 305 ? 41.665 -15.328 -24.393 1.00 57.59 ? 305 TYR A CE1 1 ATOM 2429 C CE2 . TYR A 1 305 ? 43.404 -16.895 -23.944 1.00 61.28 ? 305 TYR A CE2 1 ATOM 2430 C CZ . TYR A 1 305 ? 42.971 -15.593 -24.066 1.00 59.12 ? 305 TYR A CZ 1 ATOM 2431 O OH . TYR A 1 305 ? 43.845 -14.554 -23.862 1.00 60.19 ? 305 TYR A OH 1 ATOM 2432 N N . VAL A 1 306 ? 41.811 -18.390 -27.633 1.00 57.06 ? 306 VAL A N 1 ATOM 2433 C CA . VAL A 1 306 ? 43.170 -18.364 -28.164 1.00 56.41 ? 306 VAL A CA 1 ATOM 2434 C C . VAL A 1 306 ? 43.736 -16.970 -27.946 1.00 56.63 ? 306 VAL A C 1 ATOM 2435 O O . VAL A 1 306 ? 42.988 -16.015 -27.856 1.00 56.62 ? 306 VAL A O 1 ATOM 2436 C CB . VAL A 1 306 ? 43.205 -18.707 -29.667 1.00 56.36 ? 306 VAL A CB 1 ATOM 2437 C CG1 . VAL A 1 306 ? 42.790 -20.149 -29.897 1.00 56.42 ? 306 VAL A CG1 1 ATOM 2438 C CG2 . VAL A 1 306 ? 42.312 -17.766 -30.466 1.00 55.53 ? 306 VAL A CG2 1 ATOM 2439 N N . LYS A 1 307 ? 45.055 -16.857 -27.888 1.00 60.81 ? 307 LYS A N 1 ATOM 2440 C CA . LYS A 1 307 ? 45.722 -15.563 -27.737 1.00 65.03 ? 307 LYS A CA 1 ATOM 2441 C C . LYS A 1 307 ? 45.857 -14.728 -29.033 1.00 66.06 ? 307 LYS A C 1 ATOM 2442 O O . LYS A 1 307 ? 46.487 -13.671 -29.014 1.00 73.24 ? 307 LYS A O 1 ATOM 2443 C CB . LYS A 1 307 ? 47.123 -15.769 -27.148 1.00 68.67 ? 307 LYS A CB 1 ATOM 2444 C CG . LYS A 1 307 ? 47.181 -15.844 -25.642 1.00 70.53 ? 307 LYS A CG 1 ATOM 2445 C CD . LYS A 1 307 ? 48.628 -16.015 -25.214 1.00 76.25 ? 307 LYS A CD 1 ATOM 2446 C CE . LYS A 1 307 ? 48.781 -16.110 -23.708 1.00 80.29 ? 307 LYS A CE 1 ATOM 2447 N NZ . LYS A 1 307 ? 50.185 -16.457 -23.332 1.00 85.96 ? 307 LYS A NZ 1 ATOM 2448 N N . SER A 1 308 ? 45.284 -15.175 -30.145 1.00 63.48 ? 308 SER A N 1 ATOM 2449 C CA . SER A 1 308 ? 45.465 -14.478 -31.423 1.00 61.78 ? 308 SER A CA 1 ATOM 2450 C C . SER A 1 308 ? 44.736 -13.146 -31.480 1.00 61.58 ? 308 SER A C 1 ATOM 2451 O O . SER A 1 308 ? 43.672 -12.982 -30.882 1.00 60.63 ? 308 SER A O 1 ATOM 2452 C CB . SER A 1 308 ? 44.970 -15.340 -32.588 1.00 59.22 ? 308 SER A CB 1 ATOM 2453 O OG . SER A 1 308 ? 45.445 -16.663 -32.482 1.00 59.66 ? 308 SER A OG 1 ATOM 2454 N N . ASN A 1 309 ? 45.311 -12.208 -32.226 1.00 64.96 ? 309 ASN A N 1 ATOM 2455 C CA . ASN A 1 309 ? 44.623 -10.975 -32.601 1.00 67.20 ? 309 ASN A CA 1 ATOM 2456 C C . ASN A 1 309 ? 43.785 -11.149 -33.867 1.00 64.20 ? 309 ASN A C 1 ATOM 2457 O O . ASN A 1 309 ? 42.885 -10.352 -34.125 1.00 65.43 ? 309 ASN A O 1 ATOM 2458 C CB . ASN A 1 309 ? 45.629 -9.833 -32.793 1.00 72.83 ? 309 ASN A CB 1 ATOM 2459 C CG . ASN A 1 309 ? 46.222 -9.350 -31.476 1.00 79.50 ? 309 ASN A CG 1 ATOM 2460 O OD1 . ASN A 1 309 ? 45.498 -9.118 -30.501 1.00 81.75 ? 309 ASN A OD1 1 ATOM 2461 N ND2 . ASN A 1 309 ? 47.544 -9.195 -31.439 1.00 83.55 ? 309 ASN A ND2 1 ATOM 2462 N N . ARG A 1 310 ? 44.068 -12.193 -34.645 1.00 61.16 ? 310 ARG A N 1 ATOM 2463 C CA . ARG A 1 310 ? 43.440 -12.363 -35.955 1.00 60.23 ? 310 ARG A CA 1 ATOM 2464 C C . ARG A 1 310 ? 43.468 -13.821 -36.439 1.00 56.19 ? 310 ARG A C 1 ATOM 2465 O O . ARG A 1 310 ? 44.534 -14.428 -36.514 1.00 54.23 ? 310 ARG A O 1 ATOM 2466 C CB . ARG A 1 310 ? 44.168 -11.472 -36.965 1.00 64.06 ? 310 ARG A CB 1 ATOM 2467 C CG . ARG A 1 310 ? 43.450 -11.266 -38.286 1.00 65.95 ? 310 ARG A CG 1 ATOM 2468 C CD . ARG A 1 310 ? 44.233 -10.331 -39.194 1.00 69.78 ? 310 ARG A CD 1 ATOM 2469 N NE . ARG A 1 310 ? 43.953 -10.607 -40.606 1.00 73.92 ? 310 ARG A NE 1 ATOM 2470 C CZ . ARG A 1 310 ? 42.860 -10.214 -41.260 1.00 74.27 ? 310 ARG A CZ 1 ATOM 2471 N NH1 . ARG A 1 310 ? 41.912 -9.508 -40.653 1.00 76.64 ? 310 ARG A NH1 1 ATOM 2472 N NH2 . ARG A 1 310 ? 42.715 -10.528 -42.538 1.00 74.26 ? 310 ARG A NH2 1 ATOM 2473 N N . LEU A 1 311 ? 42.296 -14.376 -36.749 1.00 53.07 ? 311 LEU A N 1 ATOM 2474 C CA . LEU A 1 311 ? 42.196 -15.667 -37.450 1.00 51.42 ? 311 LEU A CA 1 ATOM 2475 C C . LEU A 1 311 ? 41.170 -15.560 -38.584 1.00 50.29 ? 311 LEU A C 1 ATOM 2476 O O . LEU A 1 311 ? 39.963 -15.482 -38.342 1.00 51.43 ? 311 LEU A O 1 ATOM 2477 C CB . LEU A 1 311 ? 41.820 -16.811 -36.500 1.00 50.23 ? 311 LEU A CB 1 ATOM 2478 C CG . LEU A 1 311 ? 42.813 -17.192 -35.394 1.00 52.32 ? 311 LEU A CG 1 ATOM 2479 C CD1 . LEU A 1 311 ? 42.228 -18.250 -34.470 1.00 53.21 ? 311 LEU A CD1 1 ATOM 2480 C CD2 . LEU A 1 311 ? 44.129 -17.697 -35.954 1.00 53.86 ? 311 LEU A CD2 1 ATOM 2481 N N . VAL A 1 312 ? 41.661 -15.546 -39.818 1.00 48.64 ? 312 VAL A N 1 ATOM 2482 C CA . VAL A 1 312 ? 40.811 -15.418 -40.998 1.00 48.12 ? 312 VAL A CA 1 ATOM 2483 C C . VAL A 1 312 ? 41.198 -16.469 -42.025 1.00 47.08 ? 312 VAL A C 1 ATOM 2484 O O . VAL A 1 312 ? 42.358 -16.524 -42.449 1.00 46.14 ? 312 VAL A O 1 ATOM 2485 C CB . VAL A 1 312 ? 40.963 -14.032 -41.635 1.00 49.16 ? 312 VAL A CB 1 ATOM 2486 C CG1 . VAL A 1 312 ? 40.044 -13.896 -42.841 1.00 49.55 ? 312 VAL A CG1 1 ATOM 2487 C CG2 . VAL A 1 312 ? 40.688 -12.951 -40.596 1.00 49.86 ? 312 VAL A CG2 1 ATOM 2488 N N . LEU A 1 313 ? 40.227 -17.304 -42.399 1.00 45.65 ? 313 LEU A N 1 ATOM 2489 C CA . LEU A 1 313 ? 40.423 -18.370 -43.382 1.00 45.99 ? 313 LEU A CA 1 ATOM 2490 C C . LEU A 1 313 ? 40.055 -17.875 -44.765 1.00 46.32 ? 313 LEU A C 1 ATOM 2491 O O . LEU A 1 313 ? 39.066 -17.165 -44.926 1.00 47.15 ? 313 LEU A O 1 ATOM 2492 C CB . LEU A 1 313 ? 39.542 -19.581 -43.069 1.00 45.81 ? 313 LEU A CB 1 ATOM 2493 C CG . LEU A 1 313 ? 40.012 -20.511 -41.955 1.00 47.27 ? 313 LEU A CG 1 ATOM 2494 C CD1 . LEU A 1 313 ? 38.895 -21.455 -41.546 1.00 48.56 ? 313 LEU A CD1 1 ATOM 2495 C CD2 . LEU A 1 313 ? 41.237 -21.300 -42.382 1.00 48.71 ? 313 LEU A CD2 1 ATOM 2496 N N . ALA A 1 314 ? 40.848 -18.254 -45.760 1.00 46.33 ? 314 ALA A N 1 ATOM 2497 C CA . ALA A 1 314 ? 40.492 -18.002 -47.151 1.00 45.96 ? 314 ALA A CA 1 ATOM 2498 C C . ALA A 1 314 ? 39.440 -19.014 -47.540 1.00 46.21 ? 314 ALA A C 1 ATOM 2499 O O . ALA A 1 314 ? 39.548 -20.194 -47.204 1.00 46.86 ? 314 ALA A O 1 ATOM 2500 C CB . ALA A 1 314 ? 41.705 -18.133 -48.063 1.00 46.04 ? 314 ALA A CB 1 ATOM 2501 N N . THR A 1 315 ? 38.405 -18.535 -48.217 1.00 46.93 ? 315 THR A N 1 ATOM 2502 C CA . THR A 1 315 ? 37.406 -19.398 -48.839 1.00 47.52 ? 315 THR A CA 1 ATOM 2503 C C . THR A 1 315 ? 37.488 -19.239 -50.350 1.00 46.56 ? 315 THR A C 1 ATOM 2504 O O . THR A 1 315 ? 37.550 -20.220 -51.084 1.00 48.26 ? 315 THR A O 1 ATOM 2505 C CB . THR A 1 315 ? 35.993 -19.041 -48.351 1.00 49.09 ? 315 THR A CB 1 ATOM 2506 O OG1 . THR A 1 315 ? 35.843 -17.617 -48.323 1.00 49.10 ? 315 THR A OG1 1 ATOM 2507 C CG2 . THR A 1 315 ? 35.774 -19.573 -46.953 1.00 49.73 ? 315 THR A CG2 1 ATOM 2508 N N . GLY A 1 316 ? 37.502 -17.996 -50.809 1.00 45.30 ? 316 GLY A N 1 ATOM 2509 C CA . GLY A 1 316 ? 37.598 -17.705 -52.228 1.00 45.50 ? 316 GLY A CA 1 ATOM 2510 C C . GLY A 1 316 ? 39.029 -17.706 -52.695 1.00 45.34 ? 316 GLY A C 1 ATOM 2511 O O . GLY A 1 316 ? 39.894 -18.302 -52.057 1.00 45.42 ? 316 GLY A O 1 ATOM 2512 N N . LEU A 1 317 ? 39.287 -17.018 -53.802 1.00 46.28 ? 317 LEU A N 1 ATOM 2513 C CA . LEU A 1 317 ? 40.599 -17.083 -54.442 1.00 46.79 ? 317 LEU A CA 1 ATOM 2514 C C . LEU A 1 317 ? 41.257 -15.714 -54.499 1.00 46.03 ? 317 LEU A C 1 ATOM 2515 O O . LEU A 1 317 ? 40.672 -14.715 -54.093 1.00 45.28 ? 317 LEU A O 1 ATOM 2516 C CB . LEU A 1 317 ? 40.502 -17.741 -55.833 1.00 48.66 ? 317 LEU A CB 1 ATOM 2517 C CG . LEU A 1 317 ? 39.303 -17.411 -56.713 1.00 49.71 ? 317 LEU A CG 1 ATOM 2518 C CD1 . LEU A 1 317 ? 39.328 -15.941 -57.051 1.00 51.27 ? 317 LEU A CD1 1 ATOM 2519 C CD2 . LEU A 1 317 ? 39.322 -18.230 -57.986 1.00 51.07 ? 317 LEU A CD2 1 ATOM 2520 N N . ARG A 1 318 ? 42.492 -15.692 -54.975 1.00 46.45 ? 318 ARG A N 1 ATOM 2521 C CA . ARG A 1 318 ? 43.284 -14.477 -55.015 1.00 49.77 ? 318 ARG A CA 1 ATOM 2522 C C . ARG A 1 318 ? 42.603 -13.452 -55.904 1.00 51.93 ? 318 ARG A C 1 ATOM 2523 O O . ARG A 1 318 ? 42.273 -13.746 -57.050 1.00 51.58 ? 318 ARG A O 1 ATOM 2524 C CB . ARG A 1 318 ? 44.686 -14.791 -55.535 1.00 51.59 ? 318 ARG A CB 1 ATOM 2525 C CG . ARG A 1 318 ? 45.658 -13.629 -55.474 1.00 55.54 ? 318 ARG A CG 1 ATOM 2526 C CD . ARG A 1 318 ? 46.988 -14.005 -56.098 1.00 58.52 ? 318 ARG A CD 1 ATOM 2527 N NE . ARG A 1 318 ? 47.801 -14.826 -55.202 1.00 59.86 ? 318 ARG A NE 1 ATOM 2528 C CZ . ARG A 1 318 ? 48.765 -14.360 -54.412 1.00 61.64 ? 318 ARG A CZ 1 ATOM 2529 N NH1 . ARG A 1 318 ? 49.058 -13.061 -54.377 1.00 63.45 ? 318 ARG A NH1 1 ATOM 2530 N NH2 . ARG A 1 318 ? 49.443 -15.204 -53.644 1.00 63.36 ? 318 ARG A NH2 1 ATOM 2531 N N . ASN A 1 319 ? 42.396 -12.253 -55.364 1.00 56.25 ? 319 ASN A N 1 ATOM 2532 C CA . ASN A 1 319 ? 41.658 -11.198 -56.050 1.00 59.42 ? 319 ASN A CA 1 ATOM 2533 C C . ASN A 1 319 ? 42.580 -10.274 -56.828 1.00 66.87 ? 319 ASN A C 1 ATOM 2534 O O . ASN A 1 319 ? 43.695 -9.992 -56.406 1.00 71.84 ? 319 ASN A O 1 ATOM 2535 C CB . ASN A 1 319 ? 40.831 -10.399 -55.051 1.00 58.20 ? 319 ASN A CB 1 ATOM 2536 C CG . ASN A 1 319 ? 39.724 -9.610 -55.712 1.00 59.20 ? 319 ASN A CG 1 ATOM 2537 O OD1 . ASN A 1 319 ? 39.361 -9.866 -56.853 1.00 58.38 ? 319 ASN A OD1 1 ATOM 2538 N ND2 . ASN A 1 319 ? 39.178 -8.642 -54.991 1.00 61.24 ? 319 ASN A ND2 1 ATOM 2539 N N . SER A 1 320 ? 42.093 -9.795 -57.966 1.00 76.99 ? 320 SER A N 1 ATOM 2540 C CA . SER A 1 320 ? 42.925 -9.101 -58.951 1.00 82.81 ? 320 SER A CA 1 ATOM 2541 C C . SER A 1 320 ? 42.872 -7.579 -58.786 1.00 88.39 ? 320 SER A C 1 ATOM 2542 O O . SER A 1 320 ? 41.815 -7.032 -58.493 1.00 86.42 ? 320 SER A O 1 ATOM 2543 C CB . SER A 1 320 ? 42.462 -9.483 -60.362 1.00 82.95 ? 320 SER A CB 1 ATOM 2544 O OG . SER A 1 320 ? 42.192 -10.874 -60.438 1.00 80.84 ? 320 SER A OG 1 ATOM 2545 N N . PRO A 1 321 ? 44.015 -6.891 -58.980 1.00 96.40 ? 321 PRO A N 1 ATOM 2546 C CA . PRO A 1 321 ? 44.022 -5.431 -58.951 1.00 101.61 ? 321 PRO A CA 1 ATOM 2547 C C . PRO A 1 321 ? 43.537 -4.845 -60.273 1.00 103.34 ? 321 PRO A C 1 ATOM 2548 O O . PRO A 1 321 ? 42.430 -4.315 -60.336 1.00 107.15 ? 321 PRO A O 1 ATOM 2549 C CB . PRO A 1 321 ? 45.497 -5.099 -58.726 1.00 104.14 ? 321 PRO A CB 1 ATOM 2550 C CG . PRO A 1 321 ? 46.225 -6.211 -59.398 1.00 102.94 ? 321 PRO A CG 1 ATOM 2551 C CD . PRO A 1 321 ? 45.368 -7.436 -59.214 1.00 98.60 ? 321 PRO A CD 1 ATOM 2552 N N . GLY B 2 1 ? 50.953 -18.724 -58.115 1.00 51.51 ? 1 GLY B N 1 ATOM 2553 C CA . GLY B 2 1 ? 50.527 -20.005 -57.494 1.00 48.84 ? 1 GLY B CA 1 ATOM 2554 C C . GLY B 2 1 ? 51.246 -21.201 -58.071 1.00 47.83 ? 1 GLY B C 1 ATOM 2555 O O . GLY B 2 1 ? 51.822 -21.131 -59.153 1.00 50.06 ? 1 GLY B O 1 ATOM 2556 N N . LEU B 2 2 ? 51.184 -22.311 -57.350 1.00 45.66 ? 2 LEU B N 1 ATOM 2557 C CA . LEU B 2 2 ? 51.876 -23.526 -57.751 1.00 45.96 ? 2 LEU B CA 1 ATOM 2558 C C . LEU B 2 2 ? 51.462 -24.063 -59.126 1.00 45.75 ? 2 LEU B C 1 ATOM 2559 O O . LEU B 2 2 ? 52.270 -24.690 -59.803 1.00 46.76 ? 2 LEU B O 1 ATOM 2560 C CB . LEU B 2 2 ? 51.646 -24.621 -56.715 1.00 44.12 ? 2 LEU B CB 1 ATOM 2561 C CG . LEU B 2 2 ? 52.308 -24.416 -55.372 1.00 43.69 ? 2 LEU B CG 1 ATOM 2562 C CD1 . LEU B 2 2 ? 51.897 -25.533 -54.431 1.00 43.12 ? 2 LEU B CD1 1 ATOM 2563 C CD2 . LEU B 2 2 ? 53.814 -24.356 -55.522 1.00 45.66 ? 2 LEU B CD2 1 ATOM 2564 N N . PHE B 2 3 ? 50.219 -23.819 -59.534 1.00 43.38 ? 3 PHE B N 1 ATOM 2565 C CA . PHE B 2 3 ? 49.686 -24.443 -60.743 1.00 44.02 ? 3 PHE B CA 1 ATOM 2566 C C . PHE B 2 3 ? 49.730 -23.547 -61.965 1.00 45.21 ? 3 PHE B C 1 ATOM 2567 O O . PHE B 2 3 ? 49.358 -23.976 -63.051 1.00 47.05 ? 3 PHE B O 1 ATOM 2568 C CB . PHE B 2 3 ? 48.289 -25.027 -60.468 1.00 42.24 ? 3 PHE B CB 1 ATOM 2569 C CG . PHE B 2 3 ? 48.337 -26.137 -59.466 1.00 42.04 ? 3 PHE B CG 1 ATOM 2570 C CD1 . PHE B 2 3 ? 48.611 -27.431 -59.868 1.00 42.46 ? 3 PHE B CD1 1 ATOM 2571 C CD2 . PHE B 2 3 ? 48.232 -25.866 -58.109 1.00 41.75 ? 3 PHE B CD2 1 ATOM 2572 C CE1 . PHE B 2 3 ? 48.730 -28.449 -58.940 1.00 43.95 ? 3 PHE B CE1 1 ATOM 2573 C CE2 . PHE B 2 3 ? 48.355 -26.878 -57.170 1.00 42.25 ? 3 PHE B CE2 1 ATOM 2574 C CZ . PHE B 2 3 ? 48.607 -28.174 -57.582 1.00 43.00 ? 3 PHE B CZ 1 ATOM 2575 N N . GLY B 2 4 ? 50.214 -22.320 -61.788 1.00 45.60 ? 4 GLY B N 1 ATOM 2576 C CA . GLY B 2 4 ? 50.562 -21.450 -62.906 1.00 46.38 ? 4 GLY B CA 1 ATOM 2577 C C . GLY B 2 4 ? 49.424 -20.706 -63.591 1.00 45.44 ? 4 GLY B C 1 ATOM 2578 O O . GLY B 2 4 ? 49.683 -19.865 -64.446 1.00 47.43 ? 4 GLY B O 1 ATOM 2579 N N . ALA B 2 5 ? 48.173 -20.986 -63.232 1.00 42.88 ? 5 ALA B N 1 ATOM 2580 C CA . ALA B 2 5 ? 47.042 -20.391 -63.947 1.00 42.34 ? 5 ALA B CA 1 ATOM 2581 C C . ALA B 2 5 ? 46.648 -19.048 -63.377 1.00 42.85 ? 5 ALA B C 1 ATOM 2582 O O . ALA B 2 5 ? 46.813 -18.023 -64.043 1.00 43.67 ? 5 ALA B O 1 ATOM 2583 C CB . ALA B 2 5 ? 45.846 -21.327 -63.946 1.00 41.67 ? 5 ALA B CB 1 ATOM 2584 N N . ILE B 2 6 ? 46.122 -19.056 -62.152 1.00 42.64 ? 6 ILE B N 1 ATOM 2585 C CA . ILE B 2 6 ? 45.678 -17.829 -61.489 1.00 43.94 ? 6 ILE B CA 1 ATOM 2586 C C . ILE B 2 6 ? 46.849 -16.865 -61.327 1.00 46.61 ? 6 ILE B C 1 ATOM 2587 O O . ILE B 2 6 ? 47.890 -17.230 -60.780 1.00 47.26 ? 6 ILE B O 1 ATOM 2588 C CB . ILE B 2 6 ? 45.039 -18.114 -60.116 1.00 43.17 ? 6 ILE B CB 1 ATOM 2589 C CG1 . ILE B 2 6 ? 43.662 -18.745 -60.310 1.00 42.54 ? 6 ILE B CG1 1 ATOM 2590 C CG2 . ILE B 2 6 ? 44.903 -16.828 -59.307 1.00 44.32 ? 6 ILE B CG2 1 ATOM 2591 C CD1 . ILE B 2 6 ? 43.037 -19.287 -59.047 1.00 42.33 ? 6 ILE B CD1 1 ATOM 2592 N N . ALA B 2 7 ? 46.672 -15.645 -61.829 1.00 48.81 ? 7 ALA B N 1 ATOM 2593 C CA . ALA B 2 7 ? 47.721 -14.633 -61.834 1.00 52.37 ? 7 ALA B CA 1 ATOM 2594 C C . ALA B 2 7 ? 49.021 -15.177 -62.417 1.00 54.49 ? 7 ALA B C 1 ATOM 2595 O O . ALA B 2 7 ? 50.107 -14.817 -61.971 1.00 57.60 ? 7 ALA B O 1 ATOM 2596 C CB . ALA B 2 7 ? 47.943 -14.110 -60.423 1.00 53.30 ? 7 ALA B CB 1 ATOM 2597 N N . GLY B 2 8 ? 48.894 -16.061 -63.401 1.00 54.64 ? 8 GLY B N 1 ATOM 2598 C CA . GLY B 2 8 ? 50.034 -16.667 -64.082 1.00 55.81 ? 8 GLY B CA 1 ATOM 2599 C C . GLY B 2 8 ? 49.836 -16.455 -65.570 1.00 57.63 ? 8 GLY B C 1 ATOM 2600 O O . GLY B 2 8 ? 49.943 -15.330 -66.038 1.00 59.63 ? 8 GLY B O 1 ATOM 2601 N N . PHE B 2 9 ? 49.512 -17.516 -66.312 1.00 56.35 ? 9 PHE B N 1 ATOM 2602 C CA . PHE B 2 9 ? 49.240 -17.366 -67.740 1.00 56.53 ? 9 PHE B CA 1 ATOM 2603 C C . PHE B 2 9 ? 47.856 -16.759 -67.969 1.00 55.81 ? 9 PHE B C 1 ATOM 2604 O O . PHE B 2 9 ? 47.609 -16.189 -69.027 1.00 57.53 ? 9 PHE B O 1 ATOM 2605 C CB . PHE B 2 9 ? 49.469 -18.666 -68.537 1.00 56.03 ? 9 PHE B CB 1 ATOM 2606 C CG . PHE B 2 9 ? 48.449 -19.735 -68.296 1.00 53.35 ? 9 PHE B CG 1 ATOM 2607 C CD1 . PHE B 2 9 ? 47.254 -19.741 -68.995 1.00 52.91 ? 9 PHE B CD1 1 ATOM 2608 C CD2 . PHE B 2 9 ? 48.699 -20.755 -67.397 1.00 51.64 ? 9 PHE B CD2 1 ATOM 2609 C CE1 . PHE B 2 9 ? 46.310 -20.730 -68.775 1.00 51.32 ? 9 PHE B CE1 1 ATOM 2610 C CE2 . PHE B 2 9 ? 47.767 -21.747 -67.178 1.00 50.12 ? 9 PHE B CE2 1 ATOM 2611 C CZ . PHE B 2 9 ? 46.568 -21.732 -67.863 1.00 50.37 ? 9 PHE B CZ 1 ATOM 2612 N N . ILE B 2 10 ? 46.967 -16.868 -66.979 1.00 54.51 ? 10 ILE B N 1 ATOM 2613 C CA . ILE B 2 10 ? 45.732 -16.076 -66.964 1.00 54.70 ? 10 ILE B CA 1 ATOM 2614 C C . ILE B 2 10 ? 45.970 -14.886 -66.048 1.00 57.60 ? 10 ILE B C 1 ATOM 2615 O O . ILE B 2 10 ? 45.925 -15.006 -64.830 1.00 59.02 ? 10 ILE B O 1 ATOM 2616 C CB . ILE B 2 10 ? 44.513 -16.877 -66.486 1.00 52.49 ? 10 ILE B CB 1 ATOM 2617 C CG1 . ILE B 2 10 ? 44.384 -18.179 -67.280 1.00 52.27 ? 10 ILE B CG1 1 ATOM 2618 C CG2 . ILE B 2 10 ? 43.247 -16.046 -66.646 1.00 52.13 ? 10 ILE B CG2 1 ATOM 2619 C CD1 . ILE B 2 10 ? 43.242 -19.061 -66.816 1.00 51.10 ? 10 ILE B CD1 1 ATOM 2620 N N . GLU B 2 11 ? 46.231 -13.735 -66.652 1.00 62.59 ? 11 GLU B N 1 ATOM 2621 C CA . GLU B 2 11 ? 46.742 -12.566 -65.934 1.00 66.40 ? 11 GLU B CA 1 ATOM 2622 C C . GLU B 2 11 ? 45.875 -12.089 -64.780 1.00 63.82 ? 11 GLU B C 1 ATOM 2623 O O . GLU B 2 11 ? 46.400 -11.713 -63.732 1.00 64.80 ? 11 GLU B O 1 ATOM 2624 C CB . GLU B 2 11 ? 46.930 -11.398 -66.901 1.00 73.21 ? 11 GLU B CB 1 ATOM 2625 C CG . GLU B 2 11 ? 48.281 -11.354 -67.588 1.00 78.77 ? 11 GLU B CG 1 ATOM 2626 C CD . GLU B 2 11 ? 48.526 -10.001 -68.227 1.00 85.94 ? 11 GLU B CD 1 ATOM 2627 O OE1 . GLU B 2 11 ? 47.674 -9.569 -69.045 1.00 88.46 ? 11 GLU B OE1 1 ATOM 2628 O OE2 . GLU B 2 11 ? 49.555 -9.369 -67.894 1.00 90.61 ? 11 GLU B OE2 1 ATOM 2629 N N . GLY B 2 12 ? 44.560 -12.077 -64.984 1.00 60.76 ? 12 GLY B N 1 ATOM 2630 C CA . GLY B 2 12 ? 43.631 -11.542 -63.988 1.00 59.36 ? 12 GLY B CA 1 ATOM 2631 C C . GLY B 2 12 ? 42.252 -12.164 -64.022 1.00 56.54 ? 12 GLY B C 1 ATOM 2632 O O . GLY B 2 12 ? 41.883 -12.848 -64.981 1.00 56.29 ? 12 GLY B O 1 ATOM 2633 N N . GLY B 2 13 ? 41.492 -11.929 -62.959 1.00 55.04 ? 13 GLY B N 1 ATOM 2634 C CA . GLY B 2 13 ? 40.125 -12.421 -62.852 1.00 53.78 ? 13 GLY B CA 1 ATOM 2635 C C . GLY B 2 13 ? 39.134 -11.563 -63.627 1.00 55.29 ? 13 GLY B C 1 ATOM 2636 O O . GLY B 2 13 ? 39.504 -10.548 -64.209 1.00 57.28 ? 13 GLY B O 1 ATOM 2637 N N . TRP B 2 14 ? 37.871 -11.986 -63.626 1.00 54.32 ? 14 TRP B N 1 ATOM 2638 C CA . TRP B 2 14 ? 36.806 -11.319 -64.350 1.00 55.39 ? 14 TRP B CA 1 ATOM 2639 C C . TRP B 2 14 ? 35.742 -10.783 -63.392 1.00 59.73 ? 14 TRP B C 1 ATOM 2640 O O . TRP B 2 14 ? 35.010 -11.555 -62.769 1.00 58.73 ? 14 TRP B O 1 ATOM 2641 C CB . TRP B 2 14 ? 36.146 -12.296 -65.324 1.00 53.13 ? 14 TRP B CB 1 ATOM 2642 C CG . TRP B 2 14 ? 37.018 -12.772 -66.452 1.00 50.71 ? 14 TRP B CG 1 ATOM 2643 C CD1 . TRP B 2 14 ? 38.058 -12.104 -67.025 1.00 51.16 ? 14 TRP B CD1 1 ATOM 2644 C CD2 . TRP B 2 14 ? 36.884 -13.998 -67.180 1.00 48.52 ? 14 TRP B CD2 1 ATOM 2645 N NE1 . TRP B 2 14 ? 38.591 -12.845 -68.054 1.00 49.59 ? 14 TRP B NE1 1 ATOM 2646 C CE2 . TRP B 2 14 ? 37.885 -14.010 -68.172 1.00 48.38 ? 14 TRP B CE2 1 ATOM 2647 C CE3 . TRP B 2 14 ? 36.015 -15.085 -67.091 1.00 47.72 ? 14 TRP B CE3 1 ATOM 2648 C CZ2 . TRP B 2 14 ? 38.048 -15.072 -69.059 1.00 47.68 ? 14 TRP B CZ2 1 ATOM 2649 C CZ3 . TRP B 2 14 ? 36.178 -16.139 -67.973 1.00 47.10 ? 14 TRP B CZ3 1 ATOM 2650 C CH2 . TRP B 2 14 ? 37.187 -16.125 -68.944 1.00 46.92 ? 14 TRP B CH2 1 ATOM 2651 N N . GLN B 2 15 ? 35.649 -9.458 -63.288 1.00 65.31 ? 15 GLN B N 1 ATOM 2652 C CA . GLN B 2 15 ? 34.558 -8.814 -62.553 1.00 69.38 ? 15 GLN B CA 1 ATOM 2653 C C . GLN B 2 15 ? 33.217 -9.233 -63.152 1.00 69.23 ? 15 GLN B C 1 ATOM 2654 O O . GLN B 2 15 ? 32.214 -9.305 -62.453 1.00 70.84 ? 15 GLN B O 1 ATOM 2655 C CB . GLN B 2 15 ? 34.671 -7.283 -62.618 1.00 74.03 ? 15 GLN B CB 1 ATOM 2656 C CG . GLN B 2 15 ? 35.896 -6.674 -61.940 1.00 76.01 ? 15 GLN B CG 1 ATOM 2657 C CD . GLN B 2 15 ? 35.770 -6.572 -60.430 1.00 78.87 ? 15 GLN B CD 1 ATOM 2658 O OE1 . GLN B 2 15 ? 36.690 -6.942 -59.697 1.00 80.25 ? 15 GLN B OE1 1 ATOM 2659 N NE2 . GLN B 2 15 ? 34.636 -6.060 -59.954 1.00 82.13 ? 15 GLN B NE2 1 ATOM 2660 N N . GLY B 2 16 ? 33.213 -9.501 -64.454 1.00 68.78 ? 16 GLY B N 1 ATOM 2661 C CA . GLY B 2 16 ? 31.992 -9.815 -65.187 1.00 70.04 ? 16 GLY B CA 1 ATOM 2662 C C . GLY B 2 16 ? 31.404 -11.196 -64.962 1.00 68.93 ? 16 GLY B C 1 ATOM 2663 O O . GLY B 2 16 ? 30.248 -11.432 -65.321 1.00 70.43 ? 16 GLY B O 1 ATOM 2664 N N . MET B 2 17 ? 32.178 -12.116 -64.388 1.00 66.18 ? 17 MET B N 1 ATOM 2665 C CA . MET B 2 17 ? 31.655 -13.448 -64.085 1.00 66.26 ? 17 MET B CA 1 ATOM 2666 C C . MET B 2 17 ? 31.176 -13.552 -62.639 1.00 66.92 ? 17 MET B C 1 ATOM 2667 O O . MET B 2 17 ? 31.959 -13.806 -61.720 1.00 66.72 ? 17 MET B O 1 ATOM 2668 C CB . MET B 2 17 ? 32.688 -14.529 -64.358 1.00 65.09 ? 17 MET B CB 1 ATOM 2669 C CG . MET B 2 17 ? 32.080 -15.917 -64.287 1.00 65.50 ? 17 MET B CG 1 ATOM 2670 S SD . MET B 2 17 ? 33.229 -17.137 -64.887 1.00 64.08 ? 17 MET B SD 1 ATOM 2671 C CE . MET B 2 17 ? 34.518 -16.906 -63.666 1.00 64.81 ? 17 MET B CE 1 ATOM 2672 N N . VAL B 2 18 ? 29.869 -13.407 -62.472 1.00 68.55 ? 18 VAL B N 1 ATOM 2673 C CA . VAL B 2 18 ? 29.229 -13.226 -61.174 1.00 70.96 ? 18 VAL B CA 1 ATOM 2674 C C . VAL B 2 18 ? 28.700 -14.542 -60.590 1.00 70.60 ? 18 VAL B C 1 ATOM 2675 O O . VAL B 2 18 ? 28.573 -14.687 -59.378 1.00 70.30 ? 18 VAL B O 1 ATOM 2676 C CB . VAL B 2 18 ? 28.065 -12.218 -61.339 1.00 75.02 ? 18 VAL B CB 1 ATOM 2677 C CG1 . VAL B 2 18 ? 27.050 -12.324 -60.213 1.00 79.59 ? 18 VAL B CG1 1 ATOM 2678 C CG2 . VAL B 2 18 ? 28.612 -10.803 -61.451 1.00 75.79 ? 18 VAL B CG2 1 ATOM 2679 N N . ASP B 2 19 ? 28.394 -15.496 -61.459 1.00 70.90 ? 19 ASP B N 1 ATOM 2680 C CA . ASP B 2 19 ? 27.607 -16.673 -61.083 1.00 71.80 ? 19 ASP B CA 1 ATOM 2681 C C . ASP B 2 19 ? 28.452 -17.906 -60.721 1.00 67.29 ? 19 ASP B C 1 ATOM 2682 O O . ASP B 2 19 ? 27.901 -18.975 -60.467 1.00 68.79 ? 19 ASP B O 1 ATOM 2683 C CB . ASP B 2 19 ? 26.622 -17.011 -62.218 1.00 75.11 ? 19 ASP B CB 1 ATOM 2684 C CG . ASP B 2 19 ? 27.304 -17.115 -63.590 1.00 76.80 ? 19 ASP B CG 1 ATOM 2685 O OD1 . ASP B 2 19 ? 28.545 -16.938 -63.670 1.00 72.93 ? 19 ASP B OD1 1 ATOM 2686 O OD2 . ASP B 2 19 ? 26.596 -17.364 -64.599 1.00 82.63 ? 19 ASP B OD2 1 ATOM 2687 N N . GLY B 2 20 ? 29.775 -17.772 -60.697 1.00 61.26 ? 20 GLY B N 1 ATOM 2688 C CA . GLY B 2 20 ? 30.639 -18.899 -60.351 1.00 58.85 ? 20 GLY B CA 1 ATOM 2689 C C . GLY B 2 20 ? 32.084 -18.513 -60.090 1.00 56.53 ? 20 GLY B C 1 ATOM 2690 O O . GLY B 2 20 ? 32.480 -17.376 -60.322 1.00 56.95 ? 20 GLY B O 1 ATOM 2691 N N . TRP B 2 21 ? 32.881 -19.463 -59.610 1.00 55.02 ? 21 TRP B N 1 ATOM 2692 C CA . TRP B 2 21 ? 34.290 -19.193 -59.335 1.00 52.80 ? 21 TRP B CA 1 ATOM 2693 C C . TRP B 2 21 ? 35.150 -19.305 -60.580 1.00 50.59 ? 21 TRP B C 1 ATOM 2694 O O . TRP B 2 21 ? 36.092 -18.531 -60.762 1.00 48.60 ? 21 TRP B O 1 ATOM 2695 C CB . TRP B 2 21 ? 34.824 -20.106 -58.233 1.00 53.62 ? 21 TRP B CB 1 ATOM 2696 C CG . TRP B 2 21 ? 34.777 -19.474 -56.857 1.00 57.64 ? 21 TRP B CG 1 ATOM 2697 C CD1 . TRP B 2 21 ? 34.975 -18.152 -56.535 1.00 58.78 ? 21 TRP B CD1 1 ATOM 2698 C CD2 . TRP B 2 21 ? 34.550 -20.149 -55.628 1.00 60.66 ? 21 TRP B CD2 1 ATOM 2699 N NE1 . TRP B 2 21 ? 34.866 -17.969 -55.182 1.00 60.39 ? 21 TRP B NE1 1 ATOM 2700 C CE2 . TRP B 2 21 ? 34.602 -19.180 -54.600 1.00 61.50 ? 21 TRP B CE2 1 ATOM 2701 C CE3 . TRP B 2 21 ? 34.303 -21.482 -55.291 1.00 64.18 ? 21 TRP B CE3 1 ATOM 2702 C CZ2 . TRP B 2 21 ? 34.419 -19.503 -53.263 1.00 64.85 ? 21 TRP B CZ2 1 ATOM 2703 C CZ3 . TRP B 2 21 ? 34.124 -21.808 -53.957 1.00 67.09 ? 21 TRP B CZ3 1 ATOM 2704 C CH2 . TRP B 2 21 ? 34.182 -20.820 -52.956 1.00 67.30 ? 21 TRP B CH2 1 ATOM 2705 N N . TYR B 2 22 ? 34.820 -20.273 -61.431 1.00 49.16 ? 22 TYR B N 1 ATOM 2706 C CA . TYR B 2 22 ? 35.541 -20.500 -62.665 1.00 47.01 ? 22 TYR B CA 1 ATOM 2707 C C . TYR B 2 22 ? 34.564 -20.638 -63.810 1.00 47.07 ? 22 TYR B C 1 ATOM 2708 O O . TYR B 2 22 ? 33.429 -21.085 -63.616 1.00 47.42 ? 22 TYR B O 1 ATOM 2709 C CB . TYR B 2 22 ? 36.349 -21.789 -62.580 1.00 45.85 ? 22 TYR B CB 1 ATOM 2710 C CG . TYR B 2 22 ? 36.799 -22.174 -61.197 1.00 44.71 ? 22 TYR B CG 1 ATOM 2711 C CD1 . TYR B 2 22 ? 37.788 -21.460 -60.549 1.00 44.22 ? 22 TYR B CD1 1 ATOM 2712 C CD2 . TYR B 2 22 ? 36.258 -23.277 -60.551 1.00 45.41 ? 22 TYR B CD2 1 ATOM 2713 C CE1 . TYR B 2 22 ? 38.226 -21.827 -59.288 1.00 43.21 ? 22 TYR B CE1 1 ATOM 2714 C CE2 . TYR B 2 22 ? 36.680 -23.643 -59.286 1.00 44.45 ? 22 TYR B CE2 1 ATOM 2715 C CZ . TYR B 2 22 ? 37.669 -22.919 -58.666 1.00 43.00 ? 22 TYR B CZ 1 ATOM 2716 O OH . TYR B 2 22 ? 38.108 -23.277 -57.418 1.00 41.89 ? 22 TYR B OH 1 ATOM 2717 N N . GLY B 2 23 ? 35.012 -20.287 -65.011 1.00 46.00 ? 23 GLY B N 1 ATOM 2718 C CA . GLY B 2 23 ? 34.149 -20.405 -66.171 1.00 47.61 ? 23 GLY B CA 1 ATOM 2719 C C . GLY B 2 23 ? 34.775 -19.978 -67.474 1.00 47.65 ? 23 GLY B C 1 ATOM 2720 O O . GLY B 2 23 ? 36.003 -19.944 -67.604 1.00 46.40 ? 23 GLY B O 1 ATOM 2721 N N . TYR B 2 24 ? 33.908 -19.646 -68.428 1.00 49.49 ? 24 TYR B N 1 ATOM 2722 C CA . TYR B 2 24 ? 34.298 -19.389 -69.809 1.00 50.33 ? 24 TYR B CA 1 ATOM 2723 C C . TYR B 2 24 ? 33.855 -18.015 -70.265 1.00 50.82 ? 24 TYR B C 1 ATOM 2724 O O . TYR B 2 24 ? 32.819 -17.519 -69.833 1.00 53.08 ? 24 TYR B O 1 ATOM 2725 C CB . TYR B 2 24 ? 33.629 -20.396 -70.740 1.00 52.34 ? 24 TYR B CB 1 ATOM 2726 C CG . TYR B 2 24 ? 33.699 -21.827 -70.286 1.00 53.80 ? 24 TYR B CG 1 ATOM 2727 C CD1 . TYR B 2 24 ? 32.728 -22.353 -69.452 1.00 55.36 ? 24 TYR B CD1 1 ATOM 2728 C CD2 . TYR B 2 24 ? 34.727 -22.660 -70.705 1.00 55.10 ? 24 TYR B CD2 1 ATOM 2729 C CE1 . TYR B 2 24 ? 32.775 -23.671 -69.040 1.00 57.38 ? 24 TYR B CE1 1 ATOM 2730 C CE2 . TYR B 2 24 ? 34.789 -23.982 -70.296 1.00 56.63 ? 24 TYR B CE2 1 ATOM 2731 C CZ . TYR B 2 24 ? 33.811 -24.485 -69.461 1.00 57.84 ? 24 TYR B CZ 1 ATOM 2732 O OH . TYR B 2 24 ? 33.860 -25.796 -69.041 1.00 59.68 ? 24 TYR B OH 1 ATOM 2733 N N . HIS B 2 25 ? 34.628 -17.418 -71.162 1.00 50.39 ? 25 HIS B N 1 ATOM 2734 C CA . HIS B 2 25 ? 34.188 -16.235 -71.884 1.00 52.26 ? 25 HIS B CA 1 ATOM 2735 C C . HIS B 2 25 ? 34.309 -16.490 -73.369 1.00 52.85 ? 25 HIS B C 1 ATOM 2736 O O . HIS B 2 25 ? 35.376 -16.856 -73.839 1.00 51.92 ? 25 HIS B O 1 ATOM 2737 C CB . HIS B 2 25 ? 35.021 -15.018 -71.530 1.00 52.00 ? 25 HIS B CB 1 ATOM 2738 C CG . HIS B 2 25 ? 34.583 -13.776 -72.237 1.00 54.12 ? 25 HIS B CG 1 ATOM 2739 N ND1 . HIS B 2 25 ? 35.185 -13.327 -73.391 1.00 54.90 ? 25 HIS B ND1 1 ATOM 2740 C CD2 . HIS B 2 25 ? 33.588 -12.899 -71.964 1.00 55.72 ? 25 HIS B CD2 1 ATOM 2741 C CE1 . HIS B 2 25 ? 34.593 -12.216 -73.790 1.00 56.61 ? 25 HIS B CE1 1 ATOM 2742 N NE2 . HIS B 2 25 ? 33.619 -11.937 -72.944 1.00 57.66 ? 25 HIS B NE2 1 ATOM 2743 N N . HIS B 2 26 ? 33.214 -16.278 -74.094 1.00 55.21 ? 26 HIS B N 1 ATOM 2744 C CA . HIS B 2 26 ? 33.158 -16.548 -75.528 1.00 56.58 ? 26 HIS B CA 1 ATOM 2745 C C . HIS B 2 26 ? 32.972 -15.258 -76.307 1.00 58.43 ? 26 HIS B C 1 ATOM 2746 O O . HIS B 2 26 ? 32.482 -14.263 -75.781 1.00 59.33 ? 26 HIS B O 1 ATOM 2747 C CB . HIS B 2 26 ? 32.028 -17.532 -75.852 1.00 57.31 ? 26 HIS B CB 1 ATOM 2748 C CG . HIS B 2 26 ? 30.673 -16.908 -75.897 1.00 59.44 ? 26 HIS B CG 1 ATOM 2749 N ND1 . HIS B 2 26 ? 29.903 -16.718 -74.771 1.00 60.96 ? 26 HIS B ND1 1 ATOM 2750 C CD2 . HIS B 2 26 ? 29.947 -16.428 -76.934 1.00 61.71 ? 26 HIS B CD2 1 ATOM 2751 C CE1 . HIS B 2 26 ? 28.762 -16.143 -75.110 1.00 62.97 ? 26 HIS B CE1 1 ATOM 2752 N NE2 . HIS B 2 26 ? 28.762 -15.961 -76.418 1.00 63.93 ? 26 HIS B NE2 1 ATOM 2753 N N . SER B 2 27 ? 33.365 -15.291 -77.570 1.00 59.64 ? 27 SER B N 1 ATOM 2754 C CA . SER B 2 27 ? 33.356 -14.106 -78.405 1.00 61.88 ? 27 SER B CA 1 ATOM 2755 C C . SER B 2 27 ? 33.313 -14.509 -79.880 1.00 62.85 ? 27 SER B C 1 ATOM 2756 O O . SER B 2 27 ? 34.250 -15.132 -80.378 1.00 61.85 ? 27 SER B O 1 ATOM 2757 C CB . SER B 2 27 ? 34.602 -13.279 -78.108 1.00 61.85 ? 27 SER B CB 1 ATOM 2758 O OG . SER B 2 27 ? 34.702 -12.182 -78.984 1.00 65.62 ? 27 SER B OG 1 ATOM 2759 N N . ASN B 2 28 ? 32.217 -14.169 -80.559 1.00 64.75 ? 28 ASN B N 1 ATOM 2760 C CA . ASN B 2 28 ? 32.018 -14.504 -81.976 1.00 65.65 ? 28 ASN B CA 1 ATOM 2761 C C . ASN B 2 28 ? 31.203 -13.394 -82.661 1.00 68.87 ? 28 ASN B C 1 ATOM 2762 O O . ASN B 2 28 ? 31.089 -12.301 -82.107 1.00 69.74 ? 28 ASN B O 1 ATOM 2763 C CB . ASN B 2 28 ? 31.364 -15.895 -82.103 1.00 64.67 ? 28 ASN B CB 1 ATOM 2764 C CG . ASN B 2 28 ? 30.017 -15.981 -81.403 1.00 64.60 ? 28 ASN B CG 1 ATOM 2765 O OD1 . ASN B 2 28 ? 29.338 -14.978 -81.236 1.00 66.25 ? 28 ASN B OD1 1 ATOM 2766 N ND2 . ASN B 2 28 ? 29.625 -17.182 -80.998 1.00 63.21 ? 28 ASN B ND2 1 ATOM 2767 N N . GLU B 2 29 ? 30.654 -13.649 -83.849 1.00 71.73 ? 29 GLU B N 1 ATOM 2768 C CA . GLU B 2 29 ? 29.879 -12.626 -84.565 1.00 76.18 ? 29 GLU B CA 1 ATOM 2769 C C . GLU B 2 29 ? 28.531 -12.319 -83.906 1.00 78.15 ? 29 GLU B C 1 ATOM 2770 O O . GLU B 2 29 ? 28.001 -11.219 -84.057 1.00 79.01 ? 29 GLU B O 1 ATOM 2771 C CB . GLU B 2 29 ? 29.640 -13.033 -86.026 1.00 79.92 ? 29 GLU B CB 1 ATOM 2772 C CG . GLU B 2 29 ? 30.880 -12.948 -86.909 1.00 81.38 ? 29 GLU B CG 1 ATOM 2773 C CD . GLU B 2 29 ? 30.579 -13.118 -88.393 1.00 84.00 ? 29 GLU B CD 1 ATOM 2774 O OE1 . GLU B 2 29 ? 29.718 -12.389 -88.947 1.00 86.72 ? 29 GLU B OE1 1 ATOM 2775 O OE2 . GLU B 2 29 ? 31.219 -13.988 -89.012 1.00 84.39 ? 29 GLU B OE2 1 ATOM 2776 N N . GLN B 2 30 ? 27.980 -13.295 -83.189 1.00 79.19 ? 30 GLN B N 1 ATOM 2777 C CA . GLN B 2 30 ? 26.687 -13.138 -82.511 1.00 80.99 ? 30 GLN B CA 1 ATOM 2778 C C . GLN B 2 30 ? 26.789 -12.300 -81.236 1.00 78.96 ? 30 GLN B C 1 ATOM 2779 O O . GLN B 2 30 ? 25.800 -11.719 -80.798 1.00 80.53 ? 30 GLN B O 1 ATOM 2780 C CB . GLN B 2 30 ? 26.093 -14.512 -82.176 1.00 83.05 ? 30 GLN B CB 1 ATOM 2781 C CG . GLN B 2 30 ? 25.775 -15.367 -83.399 1.00 86.58 ? 30 GLN B CG 1 ATOM 2782 C CD . GLN B 2 30 ? 25.664 -16.850 -83.073 1.00 87.65 ? 30 GLN B CD 1 ATOM 2783 O OE1 . GLN B 2 30 ? 26.629 -17.478 -82.640 1.00 87.53 ? 30 GLN B OE1 1 ATOM 2784 N NE2 . GLN B 2 30 ? 24.483 -17.417 -83.286 1.00 91.12 ? 30 GLN B NE2 1 ATOM 2785 N N . GLY B 2 31 ? 27.977 -12.242 -80.636 1.00 74.99 ? 31 GLY B N 1 ATOM 2786 C CA . GLY B 2 31 ? 28.173 -11.477 -79.403 1.00 73.57 ? 31 GLY B CA 1 ATOM 2787 C C . GLY B 2 31 ? 29.252 -12.049 -78.511 1.00 69.13 ? 31 GLY B C 1 ATOM 2788 O O . GLY B 2 31 ? 30.134 -12.767 -78.971 1.00 68.21 ? 31 GLY B O 1 ATOM 2789 N N . SER B 2 32 ? 29.183 -11.726 -77.226 1.00 67.31 ? 32 SER B N 1 ATOM 2790 C CA . SER B 2 32 ? 30.157 -12.226 -76.260 1.00 63.04 ? 32 SER B CA 1 ATOM 2791 C C . SER B 2 32 ? 29.562 -12.280 -74.864 1.00 62.51 ? 32 SER B C 1 ATOM 2792 O O . SER B 2 32 ? 28.603 -11.579 -74.569 1.00 64.15 ? 32 SER B O 1 ATOM 2793 C CB . SER B 2 32 ? 31.397 -11.335 -76.253 1.00 62.11 ? 32 SER B CB 1 ATOM 2794 O OG . SER B 2 32 ? 31.093 -10.038 -75.772 1.00 63.29 ? 32 SER B OG 1 ATOM 2795 N N . GLY B 2 33 ? 30.134 -13.118 -74.008 1.00 60.64 ? 33 GLY B N 1 ATOM 2796 C CA . GLY B 2 33 ? 29.698 -13.179 -72.619 1.00 61.06 ? 33 GLY B CA 1 ATOM 2797 C C . GLY B 2 33 ? 30.368 -14.226 -71.753 1.00 58.53 ? 33 GLY B C 1 ATOM 2798 O O . GLY B 2 33 ? 31.205 -15.002 -72.212 1.00 57.85 ? 33 GLY B O 1 ATOM 2799 N N . TYR B 2 34 ? 29.971 -14.245 -70.488 1.00 58.83 ? 34 TYR B N 1 ATOM 2800 C CA . TYR B 2 34 ? 30.540 -15.140 -69.497 1.00 57.08 ? 34 TYR B CA 1 ATOM 2801 C C . TYR B 2 34 ? 29.581 -16.272 -69.183 1.00 57.86 ? 34 TYR B C 1 ATOM 2802 O O . TYR B 2 34 ? 28.380 -16.095 -69.216 1.00 59.93 ? 34 TYR B O 1 ATOM 2803 C CB . TYR B 2 34 ? 30.824 -14.373 -68.216 1.00 56.93 ? 34 TYR B CB 1 ATOM 2804 C CG . TYR B 2 34 ? 31.772 -13.215 -68.394 1.00 57.27 ? 34 TYR B CG 1 ATOM 2805 C CD1 . TYR B 2 34 ? 33.148 -13.400 -68.339 1.00 55.24 ? 34 TYR B CD1 1 ATOM 2806 C CD2 . TYR B 2 34 ? 31.292 -11.929 -68.616 1.00 60.19 ? 34 TYR B CD2 1 ATOM 2807 C CE1 . TYR B 2 34 ? 34.018 -12.333 -68.498 1.00 56.26 ? 34 TYR B CE1 1 ATOM 2808 C CE2 . TYR B 2 34 ? 32.155 -10.858 -68.778 1.00 60.80 ? 34 TYR B CE2 1 ATOM 2809 C CZ . TYR B 2 34 ? 33.513 -11.064 -68.711 1.00 59.44 ? 34 TYR B CZ 1 ATOM 2810 O OH . TYR B 2 34 ? 34.369 -9.999 -68.868 1.00 61.91 ? 34 TYR B OH 1 ATOM 2811 N N . ALA B 2 35 ? 30.123 -17.438 -68.873 1.00 57.45 ? 35 ALA B N 1 ATOM 2812 C CA . ALA B 2 35 ? 29.317 -18.534 -68.351 1.00 58.67 ? 35 ALA B CA 1 ATOM 2813 C C . ALA B 2 35 ? 30.142 -19.362 -67.356 1.00 57.55 ? 35 ALA B C 1 ATOM 2814 O O . ALA B 2 35 ? 31.253 -19.805 -67.658 1.00 54.57 ? 35 ALA B O 1 ATOM 2815 C CB . ALA B 2 35 ? 28.800 -19.399 -69.481 1.00 59.38 ? 35 ALA B CB 1 ATOM 2816 N N . ALA B 2 36 ? 29.584 -19.549 -66.167 1.00 59.44 ? 36 ALA B N 1 ATOM 2817 C CA . ALA B 2 36 ? 30.245 -20.281 -65.108 1.00 59.39 ? 36 ALA B CA 1 ATOM 2818 C C . ALA B 2 36 ? 30.229 -21.772 -65.398 1.00 61.15 ? 36 ALA B C 1 ATOM 2819 O O . ALA B 2 36 ? 29.223 -22.301 -65.847 1.00 64.62 ? 36 ALA B O 1 ATOM 2820 C CB . ALA B 2 36 ? 29.555 -20.006 -63.783 1.00 60.98 ? 36 ALA B CB 1 ATOM 2821 N N . ASP B 2 37 ? 31.351 -22.439 -65.140 1.00 61.30 ? 37 ASP B N 1 ATOM 2822 C CA . ASP B 2 37 ? 31.399 -23.892 -65.129 1.00 63.07 ? 37 ASP B CA 1 ATOM 2823 C C . ASP B 2 37 ? 30.851 -24.396 -63.781 1.00 66.44 ? 37 ASP B C 1 ATOM 2824 O O . ASP B 2 37 ? 31.509 -24.280 -62.739 1.00 62.58 ? 37 ASP B O 1 ATOM 2825 C CB . ASP B 2 37 ? 32.827 -24.372 -65.340 1.00 62.15 ? 37 ASP B CB 1 ATOM 2826 C CG . ASP B 2 37 ? 32.902 -25.855 -65.600 1.00 64.31 ? 37 ASP B CG 1 ATOM 2827 O OD1 . ASP B 2 37 ? 32.520 -26.273 -66.716 1.00 66.16 ? 37 ASP B OD1 1 ATOM 2828 O OD2 . ASP B 2 37 ? 33.342 -26.595 -64.692 1.00 63.64 ? 37 ASP B OD2 1 ATOM 2829 N N . LYS B 2 38 ? 29.638 -24.947 -63.820 1.00 72.13 ? 38 LYS B N 1 ATOM 2830 C CA . LYS B 2 38 ? 28.888 -25.331 -62.621 1.00 75.92 ? 38 LYS B CA 1 ATOM 2831 C C . LYS B 2 38 ? 29.580 -26.442 -61.839 1.00 74.31 ? 38 LYS B C 1 ATOM 2832 O O . LYS B 2 38 ? 29.755 -26.332 -60.631 1.00 74.26 ? 38 LYS B O 1 ATOM 2833 C CB . LYS B 2 38 ? 27.479 -25.788 -63.016 1.00 83.16 ? 38 LYS B CB 1 ATOM 2834 C CG . LYS B 2 38 ? 26.489 -25.908 -61.862 1.00 90.16 ? 38 LYS B CG 1 ATOM 2835 C CD . LYS B 2 38 ? 25.597 -27.144 -61.980 1.00 96.10 ? 38 LYS B CD 1 ATOM 2836 C CE . LYS B 2 38 ? 24.700 -27.124 -63.215 1.00 100.28 ? 38 LYS B CE 1 ATOM 2837 N NZ . LYS B 2 38 ? 23.499 -26.258 -63.040 1.00 104.70 ? 38 LYS B NZ 1 ATOM 2838 N N . GLU B 2 39 ? 29.974 -27.500 -62.541 1.00 74.54 ? 39 GLU B N 1 ATOM 2839 C CA . GLU B 2 39 ? 30.571 -28.685 -61.928 1.00 75.40 ? 39 GLU B CA 1 ATOM 2840 C C . GLU B 2 39 ? 31.827 -28.379 -61.113 1.00 69.37 ? 39 GLU B C 1 ATOM 2841 O O . GLU B 2 39 ? 31.921 -28.770 -59.950 1.00 69.50 ? 39 GLU B O 1 ATOM 2842 C CB . GLU B 2 39 ? 30.918 -29.710 -63.009 1.00 80.66 ? 39 GLU B CB 1 ATOM 2843 C CG . GLU B 2 39 ? 31.533 -31.003 -62.483 1.00 86.72 ? 39 GLU B CG 1 ATOM 2844 C CD . GLU B 2 39 ? 32.097 -31.888 -63.583 1.00 91.61 ? 39 GLU B CD 1 ATOM 2845 O OE1 . GLU B 2 39 ? 31.642 -31.778 -64.746 1.00 94.84 ? 39 GLU B OE1 1 ATOM 2846 O OE2 . GLU B 2 39 ? 33.002 -32.699 -63.280 1.00 94.22 ? 39 GLU B OE2 1 ATOM 2847 N N . SER B 2 40 ? 32.795 -27.707 -61.732 1.00 62.30 ? 40 SER B N 1 ATOM 2848 C CA . SER B 2 40 ? 34.052 -27.413 -61.064 1.00 57.45 ? 40 SER B CA 1 ATOM 2849 C C . SER B 2 40 ? 33.877 -26.356 -59.967 1.00 56.21 ? 40 SER B C 1 ATOM 2850 O O . SER B 2 40 ? 34.568 -26.408 -58.947 1.00 53.99 ? 40 SER B O 1 ATOM 2851 C CB . SER B 2 40 ? 35.131 -26.996 -62.067 1.00 54.53 ? 40 SER B CB 1 ATOM 2852 O OG . SER B 2 40 ? 34.876 -25.717 -62.600 1.00 54.59 ? 40 SER B OG 1 ATOM 2853 N N . THR B 2 41 ? 32.953 -25.414 -60.172 1.00 55.06 ? 41 THR B N 1 ATOM 2854 C CA . THR B 2 41 ? 32.604 -24.433 -59.144 1.00 54.04 ? 41 THR B CA 1 ATOM 2855 C C . THR B 2 41 ? 32.040 -25.110 -57.893 1.00 55.50 ? 41 THR B C 1 ATOM 2856 O O . THR B 2 41 ? 32.436 -24.775 -56.779 1.00 53.81 ? 41 THR B O 1 ATOM 2857 C CB . THR B 2 41 ? 31.573 -23.401 -59.663 1.00 55.64 ? 41 THR B CB 1 ATOM 2858 O OG1 . THR B 2 41 ? 32.187 -22.550 -60.633 1.00 54.46 ? 41 THR B OG1 1 ATOM 2859 C CG2 . THR B 2 41 ? 31.036 -22.525 -58.536 1.00 56.61 ? 41 THR B CG2 1 ATOM 2860 N N . GLN B 2 42 ? 31.108 -26.045 -58.082 1.00 58.41 ? 42 GLN B N 1 ATOM 2861 C CA . GLN B 2 42 ? 30.465 -26.748 -56.965 1.00 61.59 ? 42 GLN B CA 1 ATOM 2862 C C . GLN B 2 42 ? 31.438 -27.676 -56.250 1.00 61.19 ? 42 GLN B C 1 ATOM 2863 O O . GLN B 2 42 ? 31.338 -27.868 -55.040 1.00 60.14 ? 42 GLN B O 1 ATOM 2864 C CB . GLN B 2 42 ? 29.256 -27.553 -57.451 1.00 65.74 ? 42 GLN B CB 1 ATOM 2865 C CG . GLN B 2 42 ? 28.404 -28.150 -56.335 1.00 69.75 ? 42 GLN B CG 1 ATOM 2866 C CD . GLN B 2 42 ? 27.894 -27.103 -55.355 1.00 71.76 ? 42 GLN B CD 1 ATOM 2867 O OE1 . GLN B 2 42 ? 28.154 -27.181 -54.152 1.00 71.75 ? 42 GLN B OE1 1 ATOM 2868 N NE2 . GLN B 2 42 ? 27.177 -26.106 -55.869 1.00 72.88 ? 42 GLN B NE2 1 ATOM 2869 N N . LYS B 2 43 ? 32.360 -28.260 -57.014 1.00 61.06 ? 43 LYS B N 1 ATOM 2870 C CA . LYS B 2 43 ? 33.472 -29.031 -56.456 1.00 62.42 ? 43 LYS B CA 1 ATOM 2871 C C . LYS B 2 43 ? 34.271 -28.169 -55.476 1.00 57.74 ? 43 LYS B C 1 ATOM 2872 O O . LYS B 2 43 ? 34.643 -28.623 -54.393 1.00 57.53 ? 43 LYS B O 1 ATOM 2873 C CB . LYS B 2 43 ? 34.413 -29.500 -57.573 1.00 65.94 ? 43 LYS B CB 1 ATOM 2874 C CG . LYS B 2 43 ? 34.798 -30.968 -57.518 1.00 71.92 ? 43 LYS B CG 1 ATOM 2875 C CD . LYS B 2 43 ? 33.656 -31.864 -57.994 1.00 79.28 ? 43 LYS B CD 1 ATOM 2876 C CE . LYS B 2 43 ? 34.164 -33.068 -58.781 1.00 83.77 ? 43 LYS B CE 1 ATOM 2877 N NZ . LYS B 2 43 ? 34.543 -32.717 -60.183 1.00 84.22 ? 43 LYS B NZ 1 ATOM 2878 N N . ALA B 2 44 ? 34.539 -26.927 -55.869 1.00 52.93 ? 44 ALA B N 1 ATOM 2879 C CA . ALA B 2 44 ? 35.325 -26.031 -55.048 1.00 51.33 ? 44 ALA B CA 1 ATOM 2880 C C . ALA B 2 44 ? 34.566 -25.647 -53.779 1.00 52.75 ? 44 ALA B C 1 ATOM 2881 O O . ALA B 2 44 ? 35.138 -25.641 -52.690 1.00 52.65 ? 44 ALA B O 1 ATOM 2882 C CB . ALA B 2 44 ? 35.720 -24.793 -55.834 1.00 50.03 ? 44 ALA B CB 1 ATOM 2883 N N . ILE B 2 45 ? 33.280 -25.344 -53.921 1.00 53.81 ? 45 ILE B N 1 ATOM 2884 C CA . ILE B 2 45 ? 32.446 -25.030 -52.772 1.00 55.61 ? 45 ILE B CA 1 ATOM 2885 C C . ILE B 2 45 ? 32.440 -26.164 -51.753 1.00 56.70 ? 45 ILE B C 1 ATOM 2886 O O . ILE B 2 45 ? 32.578 -25.915 -50.560 1.00 59.69 ? 45 ILE B O 1 ATOM 2887 C CB . ILE B 2 45 ? 31.000 -24.684 -53.198 1.00 58.56 ? 45 ILE B CB 1 ATOM 2888 C CG1 . ILE B 2 45 ? 30.975 -23.305 -53.870 1.00 57.70 ? 45 ILE B CG1 1 ATOM 2889 C CG2 . ILE B 2 45 ? 30.054 -24.692 -51.998 1.00 60.48 ? 45 ILE B CG2 1 ATOM 2890 C CD1 . ILE B 2 45 ? 29.718 -23.037 -54.672 1.00 60.69 ? 45 ILE B CD1 1 ATOM 2891 N N . ASP B 2 46 ? 32.288 -27.401 -52.213 1.00 57.18 ? 46 ASP B N 1 ATOM 2892 C CA . ASP B 2 46 ? 32.244 -28.558 -51.304 1.00 58.73 ? 46 ASP B CA 1 ATOM 2893 C C . ASP B 2 46 ? 33.569 -28.784 -50.574 1.00 56.01 ? 46 ASP B C 1 ATOM 2894 O O . ASP B 2 46 ? 33.585 -29.081 -49.383 1.00 57.53 ? 46 ASP B O 1 ATOM 2895 C CB . ASP B 2 46 ? 31.854 -29.836 -52.058 1.00 60.92 ? 46 ASP B CB 1 ATOM 2896 C CG . ASP B 2 46 ? 30.466 -29.751 -52.689 1.00 64.78 ? 46 ASP B CG 1 ATOM 2897 O OD1 . ASP B 2 46 ? 29.722 -28.792 -52.381 1.00 65.72 ? 46 ASP B OD1 1 ATOM 2898 O OD2 . ASP B 2 46 ? 30.125 -30.642 -53.503 1.00 66.76 ? 46 ASP B OD2 1 ATOM 2899 N N . GLY B 2 47 ? 34.675 -28.643 -51.287 1.00 52.87 ? 47 GLY B N 1 ATOM 2900 C CA . GLY B 2 47 ? 35.992 -28.869 -50.701 1.00 51.48 ? 47 GLY B CA 1 ATOM 2901 C C . GLY B 2 47 ? 36.339 -27.844 -49.645 1.00 50.65 ? 47 GLY B C 1 ATOM 2902 O O . GLY B 2 47 ? 36.855 -28.184 -48.578 1.00 50.91 ? 47 GLY B O 1 ATOM 2903 N N . VAL B 2 48 ? 36.036 -26.585 -49.939 1.00 50.43 ? 48 VAL B N 1 ATOM 2904 C CA . VAL B 2 48 ? 36.343 -25.486 -49.035 1.00 49.49 ? 48 VAL B CA 1 ATOM 2905 C C . VAL B 2 48 ? 35.404 -25.522 -47.829 1.00 51.65 ? 48 VAL B C 1 ATOM 2906 O O . VAL B 2 48 ? 35.830 -25.274 -46.714 1.00 52.80 ? 48 VAL B O 1 ATOM 2907 C CB . VAL B 2 48 ? 36.252 -24.132 -49.760 1.00 49.40 ? 48 VAL B CB 1 ATOM 2908 C CG1 . VAL B 2 48 ? 36.428 -22.980 -48.786 1.00 50.47 ? 48 VAL B CG1 1 ATOM 2909 C CG2 . VAL B 2 48 ? 37.305 -24.045 -50.858 1.00 47.66 ? 48 VAL B CG2 1 ATOM 2910 N N . THR B 2 49 ? 34.136 -25.849 -48.049 1.00 53.53 ? 49 THR B N 1 ATOM 2911 C CA . THR B 2 49 ? 33.176 -25.955 -46.948 1.00 56.18 ? 49 THR B CA 1 ATOM 2912 C C . THR B 2 49 ? 33.537 -27.078 -45.979 1.00 57.32 ? 49 THR B C 1 ATOM 2913 O O . THR B 2 49 ? 33.515 -26.884 -44.766 1.00 58.80 ? 49 THR B O 1 ATOM 2914 C CB . THR B 2 49 ? 31.750 -26.176 -47.474 1.00 58.63 ? 49 THR B CB 1 ATOM 2915 O OG1 . THR B 2 49 ? 31.385 -25.071 -48.303 1.00 57.55 ? 49 THR B OG1 1 ATOM 2916 C CG2 . THR B 2 49 ? 30.754 -26.300 -46.326 1.00 61.59 ? 49 THR B CG2 1 ATOM 2917 N N . ASN B 2 50 ? 33.870 -28.249 -46.511 1.00 58.21 ? 50 ASN B N 1 ATOM 2918 C CA . ASN B 2 50 ? 34.316 -29.369 -45.678 1.00 59.39 ? 50 ASN B CA 1 ATOM 2919 C C . ASN B 2 50 ? 35.557 -29.012 -44.874 1.00 57.68 ? 50 ASN B C 1 ATOM 2920 O O . ASN B 2 50 ? 35.683 -29.379 -43.715 1.00 57.65 ? 50 ASN B O 1 ATOM 2921 C CB . ASN B 2 50 ? 34.609 -30.600 -46.539 1.00 59.64 ? 50 ASN B CB 1 ATOM 2922 C CG . ASN B 2 50 ? 33.347 -31.245 -47.087 1.00 63.23 ? 50 ASN B CG 1 ATOM 2923 O OD1 . ASN B 2 50 ? 32.247 -30.961 -46.629 1.00 66.33 ? 50 ASN B OD1 1 ATOM 2924 N ND2 . ASN B 2 50 ? 33.504 -32.116 -48.077 1.00 63.65 ? 50 ASN B ND2 1 ATOM 2925 N N . LYS B 2 51 ? 36.472 -28.299 -45.521 1.00 56.99 ? 51 LYS B N 1 ATOM 2926 C CA . LYS B 2 51 ? 37.719 -27.864 -44.912 1.00 55.39 ? 51 LYS B CA 1 ATOM 2927 C C . LYS B 2 51 ? 37.465 -26.973 -43.700 1.00 55.81 ? 51 LYS B C 1 ATOM 2928 O O . LYS B 2 51 ? 38.030 -27.173 -42.629 1.00 56.05 ? 51 LYS B O 1 ATOM 2929 C CB . LYS B 2 51 ? 38.512 -27.084 -45.950 1.00 54.79 ? 51 LYS B CB 1 ATOM 2930 C CG . LYS B 2 51 ? 39.839 -26.537 -45.474 1.00 55.04 ? 51 LYS B CG 1 ATOM 2931 C CD . LYS B 2 51 ? 40.304 -25.449 -46.417 1.00 56.44 ? 51 LYS B CD 1 ATOM 2932 C CE . LYS B 2 51 ? 41.800 -25.510 -46.618 1.00 56.81 ? 51 LYS B CE 1 ATOM 2933 N NZ . LYS B 2 51 ? 42.175 -26.411 -47.731 1.00 56.19 ? 51 LYS B NZ 1 ATOM 2934 N N . VAL B 2 52 ? 36.611 -25.979 -43.881 1.00 55.15 ? 52 VAL B N 1 ATOM 2935 C CA . VAL B 2 52 ? 36.308 -25.055 -42.812 1.00 55.75 ? 52 VAL B CA 1 ATOM 2936 C C . VAL B 2 52 ? 35.713 -25.826 -41.623 1.00 57.21 ? 52 VAL B C 1 ATOM 2937 O O . VAL B 2 52 ? 36.131 -25.625 -40.481 1.00 57.19 ? 52 VAL B O 1 ATOM 2938 C CB . VAL B 2 52 ? 35.376 -23.928 -43.307 1.00 56.73 ? 52 VAL B CB 1 ATOM 2939 C CG1 . VAL B 2 52 ? 34.916 -23.051 -42.149 1.00 59.58 ? 52 VAL B CG1 1 ATOM 2940 C CG2 . VAL B 2 52 ? 36.089 -23.081 -44.355 1.00 54.58 ? 52 VAL B CG2 1 ATOM 2941 N N . ASN B 2 53 ? 34.778 -26.731 -41.898 1.00 58.48 ? 53 ASN B N 1 ATOM 2942 C CA . ASN B 2 53 ? 34.170 -27.548 -40.840 1.00 62.16 ? 53 ASN B CA 1 ATOM 2943 C C . ASN B 2 53 ? 35.181 -28.498 -40.201 1.00 61.51 ? 53 ASN B C 1 ATOM 2944 O O . ASN B 2 53 ? 35.145 -28.721 -39.000 1.00 62.56 ? 53 ASN B O 1 ATOM 2945 C CB . ASN B 2 53 ? 32.969 -28.344 -41.365 1.00 64.99 ? 53 ASN B CB 1 ATOM 2946 C CG . ASN B 2 53 ? 31.886 -27.459 -41.959 1.00 66.98 ? 53 ASN B CG 1 ATOM 2947 O OD1 . ASN B 2 53 ? 31.713 -26.312 -41.554 1.00 68.61 ? 53 ASN B OD1 1 ATOM 2948 N ND2 . ASN B 2 53 ? 31.152 -27.992 -42.930 1.00 68.76 ? 53 ASN B ND2 1 ATOM 2949 N N . SER B 2 54 ? 36.086 -29.046 -41.007 1.00 61.27 ? 54 SER B N 1 ATOM 2950 C CA . SER B 2 54 ? 37.153 -29.905 -40.489 1.00 61.83 ? 54 SER B CA 1 ATOM 2951 C C . SER B 2 54 ? 38.055 -29.132 -39.541 1.00 62.61 ? 54 SER B C 1 ATOM 2952 O O . SER B 2 54 ? 38.456 -29.648 -38.500 1.00 62.23 ? 54 SER B O 1 ATOM 2953 C CB . SER B 2 54 ? 37.992 -30.503 -41.626 1.00 60.15 ? 54 SER B CB 1 ATOM 2954 O OG . SER B 2 54 ? 37.339 -31.621 -42.205 1.00 61.49 ? 54 SER B OG 1 ATOM 2955 N N . ILE B 2 55 ? 38.373 -27.894 -39.914 1.00 64.55 ? 55 ILE B N 1 ATOM 2956 C CA . ILE B 2 55 ? 39.214 -27.032 -39.087 1.00 66.43 ? 55 ILE B CA 1 ATOM 2957 C C . ILE B 2 55 ? 38.509 -26.732 -37.773 1.00 70.61 ? 55 ILE B C 1 ATOM 2958 O O . ILE B 2 55 ? 39.072 -26.952 -36.704 1.00 73.76 ? 55 ILE B O 1 ATOM 2959 C CB . ILE B 2 55 ? 39.581 -25.721 -39.818 1.00 66.76 ? 55 ILE B CB 1 ATOM 2960 C CG1 . ILE B 2 55 ? 40.616 -26.011 -40.906 1.00 65.73 ? 55 ILE B CG1 1 ATOM 2961 C CG2 . ILE B 2 55 ? 40.135 -24.683 -38.849 1.00 68.61 ? 55 ILE B CG2 1 ATOM 2962 C CD1 . ILE B 2 55 ? 40.961 -24.814 -41.766 1.00 65.29 ? 55 ILE B CD1 1 ATOM 2963 N N . ILE B 2 56 ? 37.275 -26.245 -37.856 1.00 72.71 ? 56 ILE B N 1 ATOM 2964 C CA . ILE B 2 56 ? 36.502 -25.931 -36.662 1.00 75.04 ? 56 ILE B CA 1 ATOM 2965 C C . ILE B 2 56 ? 36.396 -27.168 -35.771 1.00 78.81 ? 56 ILE B C 1 ATOM 2966 O O . ILE B 2 56 ? 36.616 -27.089 -34.562 1.00 80.23 ? 56 ILE B O 1 ATOM 2967 C CB . ILE B 2 56 ? 35.084 -25.437 -37.018 1.00 77.03 ? 56 ILE B CB 1 ATOM 2968 C CG1 . ILE B 2 56 ? 35.150 -24.089 -37.743 1.00 75.84 ? 56 ILE B CG1 1 ATOM 2969 C CG2 . ILE B 2 56 ? 34.219 -25.322 -35.764 1.00 79.96 ? 56 ILE B CG2 1 ATOM 2970 C CD1 . ILE B 2 56 ? 33.873 -23.718 -38.467 1.00 77.48 ? 56 ILE B CD1 1 ATOM 2971 N N . ASP B 2 57 ? 36.073 -28.307 -36.379 1.00 81.37 ? 57 ASP B N 1 ATOM 2972 C CA . ASP B 2 57 ? 35.808 -29.536 -35.634 1.00 85.66 ? 57 ASP B CA 1 ATOM 2973 C C . ASP B 2 57 ? 37.036 -30.067 -34.891 1.00 83.73 ? 57 ASP B C 1 ATOM 2974 O O . ASP B 2 57 ? 36.922 -30.528 -33.764 1.00 84.50 ? 57 ASP B O 1 ATOM 2975 C CB . ASP B 2 57 ? 35.260 -30.619 -36.570 1.00 88.00 ? 57 ASP B CB 1 ATOM 2976 C CG . ASP B 2 57 ? 34.861 -31.879 -35.830 1.00 94.15 ? 57 ASP B CG 1 ATOM 2977 O OD1 . ASP B 2 57 ? 34.092 -31.776 -34.844 1.00 100.55 ? 57 ASP B OD1 1 ATOM 2978 O OD2 . ASP B 2 57 ? 35.317 -32.973 -36.229 1.00 94.66 ? 57 ASP B OD2 1 ATOM 2979 N N . LYS B 2 58 ? 38.202 -30.011 -35.528 1.00 81.80 ? 58 LYS B N 1 ATOM 2980 C CA . LYS B 2 58 ? 39.443 -30.469 -34.902 1.00 81.45 ? 58 LYS B CA 1 ATOM 2981 C C . LYS B 2 58 ? 39.807 -29.641 -33.674 1.00 84.67 ? 58 LYS B C 1 ATOM 2982 O O . LYS B 2 58 ? 40.342 -30.172 -32.701 1.00 83.43 ? 58 LYS B O 1 ATOM 2983 C CB . LYS B 2 58 ? 40.600 -30.465 -35.917 1.00 79.73 ? 58 LYS B CB 1 ATOM 2984 C CG . LYS B 2 58 ? 41.062 -31.838 -36.399 1.00 80.77 ? 58 LYS B CG 1 ATOM 2985 C CD . LYS B 2 58 ? 40.030 -32.938 -36.187 1.00 83.90 ? 58 LYS B CD 1 ATOM 2986 C CE . LYS B 2 58 ? 40.441 -34.225 -36.862 1.00 84.16 ? 58 LYS B CE 1 ATOM 2987 N NZ . LYS B 2 58 ? 39.596 -35.358 -36.402 1.00 87.52 ? 58 LYS B NZ 1 ATOM 2988 N N . MET B 2 59 ? 39.490 -28.351 -33.716 1.00 86.98 ? 59 MET B N 1 ATOM 2989 C CA . MET B 2 59 ? 39.742 -27.453 -32.594 1.00 90.42 ? 59 MET B CA 1 ATOM 2990 C C . MET B 2 59 ? 38.593 -27.478 -31.569 1.00 96.31 ? 59 MET B C 1 ATOM 2991 O O . MET B 2 59 ? 38.540 -26.630 -30.682 1.00 97.29 ? 59 MET B O 1 ATOM 2992 C CB . MET B 2 59 ? 39.953 -26.027 -33.113 1.00 90.18 ? 59 MET B CB 1 ATOM 2993 C CG . MET B 2 59 ? 41.030 -25.889 -34.183 1.00 88.09 ? 59 MET B CG 1 ATOM 2994 S SD . MET B 2 59 ? 42.730 -26.032 -33.597 1.00 90.58 ? 59 MET B SD 1 ATOM 2995 C CE . MET B 2 59 ? 42.882 -24.710 -32.399 1.00 93.36 ? 59 MET B CE 1 ATOM 2996 N N . ASN B 2 60 ? 37.682 -28.448 -31.694 1.00 102.23 ? 60 ASN B N 1 ATOM 2997 C CA . ASN B 2 60 ? 36.545 -28.604 -30.776 1.00 107.75 ? 60 ASN B CA 1 ATOM 2998 C C . ASN B 2 60 ? 37.001 -28.999 -29.373 1.00 108.22 ? 60 ASN B C 1 ATOM 2999 O O . ASN B 2 60 ? 36.742 -28.287 -28.405 1.00 107.83 ? 60 ASN B O 1 ATOM 3000 C CB . ASN B 2 60 ? 35.564 -29.653 -31.323 1.00 110.64 ? 60 ASN B CB 1 ATOM 3001 C CG . ASN B 2 60 ? 34.429 -29.962 -30.364 1.00 115.65 ? 60 ASN B CG 1 ATOM 3002 O OD1 . ASN B 2 60 ? 34.216 -31.117 -29.990 1.00 116.90 ? 60 ASN B OD1 1 ATOM 3003 N ND2 . ASN B 2 60 ? 33.695 -28.933 -29.963 1.00 118.23 ? 60 ASN B ND2 1 ATOM 3004 N N . THR B 2 61 ? 37.669 -30.144 -29.270 1.00 116.61 ? 61 THR B N 1 ATOM 3005 C CA . THR B 2 61 ? 38.269 -30.562 -28.013 1.00 113.61 ? 61 THR B CA 1 ATOM 3006 C C . THR B 2 61 ? 39.561 -29.773 -27.857 1.00 109.30 ? 61 THR B C 1 ATOM 3007 O O . THR B 2 61 ? 40.438 -29.831 -28.721 1.00 110.45 ? 61 THR B O 1 ATOM 3008 C CB . THR B 2 61 ? 38.565 -32.073 -27.980 1.00 117.13 ? 61 THR B CB 1 ATOM 3009 O OG1 . THR B 2 61 ? 37.415 -32.802 -28.424 1.00 121.09 ? 61 THR B OG1 1 ATOM 3010 C CG2 . THR B 2 61 ? 38.925 -32.516 -26.566 1.00 116.05 ? 61 THR B CG2 1 ATOM 3011 N N . GLN B 2 62 ? 39.660 -29.028 -26.762 1.00 103.70 ? 62 GLN B N 1 ATOM 3012 C CA . GLN B 2 62 ? 40.791 -28.137 -26.523 1.00 101.91 ? 62 GLN B CA 1 ATOM 3013 C C . GLN B 2 62 ? 40.821 -27.697 -25.052 1.00 97.73 ? 62 GLN B C 1 ATOM 3014 O O . GLN B 2 62 ? 39.786 -27.676 -24.380 1.00 99.02 ? 62 GLN B O 1 ATOM 3015 C CB . GLN B 2 62 ? 40.711 -26.932 -27.474 1.00 102.95 ? 62 GLN B CB 1 ATOM 3016 C CG . GLN B 2 62 ? 41.548 -25.720 -27.079 1.00 100.85 ? 62 GLN B CG 1 ATOM 3017 C CD . GLN B 2 62 ? 41.585 -24.649 -28.154 1.00 104.55 ? 62 GLN B CD 1 ATOM 3018 O OE1 . GLN B 2 62 ? 41.229 -24.894 -29.308 1.00 109.77 ? 62 GLN B OE1 1 ATOM 3019 N NE2 . GLN B 2 62 ? 42.016 -23.450 -27.779 1.00 103.53 ? 62 GLN B NE2 1 ATOM 3020 N N . PHE B 2 63 ? 42.011 -27.352 -24.566 1.00 92.54 ? 63 PHE B N 1 ATOM 3021 C CA . PHE B 2 63 ? 42.212 -27.002 -23.159 1.00 90.39 ? 63 PHE B CA 1 ATOM 3022 C C . PHE B 2 63 ? 41.286 -25.892 -22.655 1.00 91.04 ? 63 PHE B C 1 ATOM 3023 O O . PHE B 2 63 ? 41.191 -24.826 -23.263 1.00 94.83 ? 63 PHE B O 1 ATOM 3024 C CB . PHE B 2 63 ? 43.657 -26.574 -22.921 1.00 86.45 ? 63 PHE B CB 1 ATOM 3025 C CG . PHE B 2 63 ? 43.981 -26.348 -21.478 1.00 83.10 ? 63 PHE B CG 1 ATOM 3026 C CD1 . PHE B 2 63 ? 44.140 -27.426 -20.617 1.00 80.59 ? 63 PHE B CD1 1 ATOM 3027 C CD2 . PHE B 2 63 ? 44.117 -25.058 -20.974 1.00 83.49 ? 63 PHE B CD2 1 ATOM 3028 C CE1 . PHE B 2 63 ? 44.433 -27.226 -19.283 1.00 78.72 ? 63 PHE B CE1 1 ATOM 3029 C CE2 . PHE B 2 63 ? 44.410 -24.850 -19.637 1.00 80.06 ? 63 PHE B CE2 1 ATOM 3030 C CZ . PHE B 2 63 ? 44.568 -25.936 -18.792 1.00 77.77 ? 63 PHE B CZ 1 ATOM 3031 N N . GLU B 2 64 ? 40.612 -26.155 -21.539 1.00 89.15 ? 64 GLU B N 1 ATOM 3032 C CA . GLU B 2 64 ? 39.799 -25.153 -20.864 1.00 90.52 ? 64 GLU B CA 1 ATOM 3033 C C . GLU B 2 64 ? 40.425 -24.840 -19.515 1.00 88.36 ? 64 GLU B C 1 ATOM 3034 O O . GLU B 2 64 ? 40.724 -25.747 -18.737 1.00 86.32 ? 64 GLU B O 1 ATOM 3035 C CB . GLU B 2 64 ? 38.376 -25.664 -20.664 1.00 94.75 ? 64 GLU B CB 1 ATOM 3036 C CG . GLU B 2 64 ? 37.616 -25.898 -21.959 1.00 99.84 ? 64 GLU B CG 1 ATOM 3037 C CD . GLU B 2 64 ? 36.184 -26.348 -21.728 1.00 105.08 ? 64 GLU B CD 1 ATOM 3038 O OE1 . GLU B 2 64 ? 35.734 -26.346 -20.560 1.00 106.70 ? 64 GLU B OE1 1 ATOM 3039 O OE2 . GLU B 2 64 ? 35.509 -26.706 -22.717 1.00 105.15 ? 64 GLU B OE2 1 ATOM 3040 N N . ALA B 2 65 ? 40.626 -23.555 -19.241 1.00 89.65 ? 65 ALA B N 1 ATOM 3041 C CA . ALA B 2 65 ? 41.230 -23.130 -17.979 1.00 88.27 ? 65 ALA B CA 1 ATOM 3042 C C . ALA B 2 65 ? 40.194 -23.109 -16.853 1.00 89.48 ? 65 ALA B C 1 ATOM 3043 O O . ALA B 2 65 ? 39.008 -22.867 -17.093 1.00 90.48 ? 65 ALA B O 1 ATOM 3044 C CB . ALA B 2 65 ? 41.885 -21.763 -18.137 1.00 88.41 ? 65 ALA B CB 1 ATOM 3045 N N . VAL B 2 66 ? 40.654 -23.381 -15.631 1.00 87.79 ? 66 VAL B N 1 ATOM 3046 C CA . VAL B 2 66 ? 39.800 -23.363 -14.441 1.00 90.32 ? 66 VAL B CA 1 ATOM 3047 C C . VAL B 2 66 ? 40.483 -22.563 -13.340 1.00 87.43 ? 66 VAL B C 1 ATOM 3048 O O . VAL B 2 66 ? 41.705 -22.633 -13.193 1.00 84.81 ? 66 VAL B O 1 ATOM 3049 C CB . VAL B 2 66 ? 39.510 -24.790 -13.922 1.00 92.01 ? 66 VAL B CB 1 ATOM 3050 C CG1 . VAL B 2 66 ? 38.567 -24.748 -12.719 1.00 95.61 ? 66 VAL B CG1 1 ATOM 3051 C CG2 . VAL B 2 66 ? 38.930 -25.655 -15.036 1.00 94.11 ? 66 VAL B CG2 1 ATOM 3052 N N . GLY B 2 67 ? 39.689 -21.818 -12.569 1.00 88.09 ? 67 GLY B N 1 ATOM 3053 C CA . GLY B 2 67 ? 40.203 -21.008 -11.464 1.00 85.59 ? 67 GLY B CA 1 ATOM 3054 C C . GLY B 2 67 ? 40.630 -21.843 -10.264 1.00 81.25 ? 67 GLY B C 1 ATOM 3055 O O . GLY B 2 67 ? 39.839 -22.615 -9.725 1.00 82.70 ? 67 GLY B O 1 ATOM 3056 N N . ARG B 2 68 ? 41.890 -21.698 -9.860 1.00 75.64 ? 68 ARG B N 1 ATOM 3057 C CA . ARG B 2 68 ? 42.410 -22.338 -8.650 1.00 72.58 ? 68 ARG B CA 1 ATOM 3058 C C . ARG B 2 68 ? 43.133 -21.296 -7.830 1.00 70.74 ? 68 ARG B C 1 ATOM 3059 O O . ARG B 2 68 ? 43.978 -20.572 -8.350 1.00 71.35 ? 68 ARG B O 1 ATOM 3060 C CB . ARG B 2 68 ? 43.382 -23.463 -8.991 1.00 68.32 ? 68 ARG B CB 1 ATOM 3061 C CG . ARG B 2 68 ? 42.710 -24.694 -9.563 1.00 68.38 ? 68 ARG B CG 1 ATOM 3062 C CD . ARG B 2 68 ? 43.711 -25.783 -9.916 1.00 65.28 ? 68 ARG B CD 1 ATOM 3063 N NE . ARG B 2 68 ? 43.188 -26.595 -11.007 1.00 66.74 ? 68 ARG B NE 1 ATOM 3064 C CZ . ARG B 2 68 ? 43.307 -26.294 -12.300 1.00 67.08 ? 68 ARG B CZ 1 ATOM 3065 N NH1 . ARG B 2 68 ? 43.972 -25.216 -12.709 1.00 63.46 ? 68 ARG B NH1 1 ATOM 3066 N NH2 . ARG B 2 68 ? 42.760 -27.094 -13.203 1.00 73.36 ? 68 ARG B NH2 1 ATOM 3067 N N . GLU B 2 69 ? 42.814 -21.233 -6.545 1.00 71.65 ? 69 GLU B N 1 ATOM 3068 C CA . GLU B 2 69 ? 43.385 -20.222 -5.671 1.00 69.93 ? 69 GLU B CA 1 ATOM 3069 C C . GLU B 2 69 ? 44.373 -20.878 -4.715 1.00 63.85 ? 69 GLU B C 1 ATOM 3070 O O . GLU B 2 69 ? 44.186 -22.018 -4.312 1.00 60.55 ? 69 GLU B O 1 ATOM 3071 C CB . GLU B 2 69 ? 42.267 -19.508 -4.914 1.00 78.33 ? 69 GLU B CB 1 ATOM 3072 C CG . GLU B 2 69 ? 42.300 -17.992 -5.052 1.00 84.09 ? 69 GLU B CG 1 ATOM 3073 C CD . GLU B 2 69 ? 40.927 -17.363 -4.927 1.00 92.32 ? 69 GLU B CD 1 ATOM 3074 O OE1 . GLU B 2 69 ? 39.975 -17.870 -5.560 1.00 93.68 ? 69 GLU B OE1 1 ATOM 3075 O OE2 . GLU B 2 69 ? 40.800 -16.360 -4.192 1.00 98.95 ? 69 GLU B OE2 1 ATOM 3076 N N . PHE B 2 70 ? 45.431 -20.151 -4.373 1.00 62.33 ? 70 PHE B N 1 ATOM 3077 C CA . PHE B 2 70 ? 46.487 -20.661 -3.500 1.00 60.41 ? 70 PHE B CA 1 ATOM 3078 C C . PHE B 2 70 ? 46.876 -19.601 -2.477 1.00 60.92 ? 70 PHE B C 1 ATOM 3079 O O . PHE B 2 70 ? 46.712 -18.410 -2.731 1.00 62.33 ? 70 PHE B O 1 ATOM 3080 C CB . PHE B 2 70 ? 47.712 -21.046 -4.330 1.00 57.62 ? 70 PHE B CB 1 ATOM 3081 C CG . PHE B 2 70 ? 47.419 -22.027 -5.426 1.00 56.01 ? 70 PHE B CG 1 ATOM 3082 C CD1 . PHE B 2 70 ? 47.010 -21.587 -6.680 1.00 55.81 ? 70 PHE B CD1 1 ATOM 3083 C CD2 . PHE B 2 70 ? 47.546 -23.391 -5.204 1.00 55.61 ? 70 PHE B CD2 1 ATOM 3084 C CE1 . PHE B 2 70 ? 46.730 -22.494 -7.686 1.00 54.79 ? 70 PHE B CE1 1 ATOM 3085 C CE2 . PHE B 2 70 ? 47.273 -24.304 -6.210 1.00 54.40 ? 70 PHE B CE2 1 ATOM 3086 C CZ . PHE B 2 70 ? 46.865 -23.856 -7.452 1.00 53.91 ? 70 PHE B CZ 1 ATOM 3087 N N . ASN B 2 71 ? 47.384 -20.029 -1.322 1.00 60.62 ? 71 ASN B N 1 ATOM 3088 C CA . ASN B 2 71 ? 47.762 -19.078 -0.263 1.00 62.22 ? 71 ASN B CA 1 ATOM 3089 C C . ASN B 2 71 ? 49.227 -18.651 -0.383 1.00 59.63 ? 71 ASN B C 1 ATOM 3090 O O . ASN B 2 71 ? 49.928 -19.075 -1.306 1.00 55.15 ? 71 ASN B O 1 ATOM 3091 C CB . ASN B 2 71 ? 47.399 -19.605 1.145 1.00 64.04 ? 71 ASN B CB 1 ATOM 3092 C CG . ASN B 2 71 ? 48.344 -20.685 1.659 1.00 62.28 ? 71 ASN B CG 1 ATOM 3093 O OD1 . ASN B 2 71 ? 49.563 -20.587 1.535 1.00 60.16 ? 71 ASN B OD1 1 ATOM 3094 N ND2 . ASN B 2 71 ? 47.774 -21.715 2.273 1.00 65.50 ? 71 ASN B ND2 1 ATOM 3095 N N . ASN B 2 72 ? 49.675 -17.820 0.556 1.00 63.06 ? 72 ASN B N 1 ATOM 3096 C CA . ASN B 2 72 ? 50.989 -17.174 0.489 1.00 64.68 ? 72 ASN B CA 1 ATOM 3097 C C . ASN B 2 72 ? 52.198 -18.110 0.642 1.00 61.46 ? 72 ASN B C 1 ATOM 3098 O O . ASN B 2 72 ? 53.307 -17.751 0.245 1.00 60.11 ? 72 ASN B O 1 ATOM 3099 C CB . ASN B 2 72 ? 51.074 -16.063 1.541 1.00 70.47 ? 72 ASN B CB 1 ATOM 3100 C CG . ASN B 2 72 ? 52.213 -15.099 1.279 1.00 73.84 ? 72 ASN B CG 1 ATOM 3101 O OD1 . ASN B 2 72 ? 52.378 -14.610 0.162 1.00 77.38 ? 72 ASN B OD1 1 ATOM 3102 N ND2 . ASN B 2 72 ? 53.006 -14.819 2.306 1.00 76.10 ? 72 ASN B ND2 1 ATOM 3103 N N . LEU B 2 73 ? 51.989 -19.288 1.229 1.00 59.07 ? 73 LEU B N 1 ATOM 3104 C CA . LEU B 2 73 ? 53.038 -20.302 1.320 1.00 58.79 ? 73 LEU B CA 1 ATOM 3105 C C . LEU B 2 73 ? 52.748 -21.504 0.405 1.00 57.05 ? 73 LEU B C 1 ATOM 3106 O O . LEU B 2 73 ? 53.181 -22.628 0.680 1.00 55.63 ? 73 LEU B O 1 ATOM 3107 C CB . LEU B 2 73 ? 53.217 -20.750 2.771 1.00 61.72 ? 73 LEU B CB 1 ATOM 3108 C CG . LEU B 2 73 ? 53.863 -19.721 3.708 1.00 66.08 ? 73 LEU B CG 1 ATOM 3109 C CD1 . LEU B 2 73 ? 53.751 -20.170 5.160 1.00 67.86 ? 73 LEU B CD1 1 ATOM 3110 C CD2 . LEU B 2 73 ? 55.319 -19.468 3.331 1.00 65.90 ? 73 LEU B CD2 1 ATOM 3111 N N . GLU B 2 74 ? 52.015 -21.254 -0.680 1.00 54.23 ? 74 GLU B N 1 ATOM 3112 C CA . GLU B 2 74 ? 51.839 -22.230 -1.753 1.00 52.31 ? 74 GLU B CA 1 ATOM 3113 C C . GLU B 2 74 ? 52.271 -21.612 -3.085 1.00 49.43 ? 74 GLU B C 1 ATOM 3114 O O . GLU B 2 74 ? 51.645 -21.837 -4.113 1.00 47.50 ? 74 GLU B O 1 ATOM 3115 C CB . GLU B 2 74 ? 50.381 -22.683 -1.826 1.00 52.11 ? 74 GLU B CB 1 ATOM 3116 C CG . GLU B 2 74 ? 49.911 -23.452 -0.613 1.00 53.93 ? 74 GLU B CG 1 ATOM 3117 C CD . GLU B 2 74 ? 48.434 -23.784 -0.690 1.00 57.53 ? 74 GLU B CD 1 ATOM 3118 O OE1 . GLU B 2 74 ? 47.638 -22.915 -1.117 1.00 59.34 ? 74 GLU B OE1 1 ATOM 3119 O OE2 . GLU B 2 74 ? 48.061 -24.915 -0.326 1.00 58.41 ? 74 GLU B OE2 1 ATOM 3120 N N . ARG B 2 75 ? 53.340 -20.826 -3.053 1.00 50.47 ? 75 ARG B N 1 ATOM 3121 C CA . ARG B 2 75 ? 53.816 -20.142 -4.235 1.00 51.30 ? 75 ARG B CA 1 ATOM 3122 C C . ARG B 2 75 ? 54.323 -21.099 -5.308 1.00 50.14 ? 75 ARG B C 1 ATOM 3123 O O . ARG B 2 75 ? 54.144 -20.839 -6.489 1.00 47.64 ? 75 ARG B O 1 ATOM 3124 C CB . ARG B 2 75 ? 54.918 -19.139 -3.880 1.00 56.70 ? 75 ARG B CB 1 ATOM 3125 C CG . ARG B 2 75 ? 54.462 -17.937 -3.061 1.00 62.33 ? 75 ARG B CG 1 ATOM 3126 C CD . ARG B 2 75 ? 53.348 -17.165 -3.753 1.00 67.70 ? 75 ARG B CD 1 ATOM 3127 N NE . ARG B 2 75 ? 52.919 -16.000 -2.982 1.00 78.30 ? 75 ARG B NE 1 ATOM 3128 C CZ . ARG B 2 75 ? 51.868 -15.235 -3.284 1.00 85.76 ? 75 ARG B CZ 1 ATOM 3129 N NH1 . ARG B 2 75 ? 51.118 -15.499 -4.357 1.00 85.90 ? 75 ARG B NH1 1 ATOM 3130 N NH2 . ARG B 2 75 ? 51.562 -14.195 -2.508 1.00 89.39 ? 75 ARG B NH2 1 ATOM 3131 N N . ARG B 2 76 ? 54.961 -22.197 -4.921 1.00 50.50 ? 76 ARG B N 1 ATOM 3132 C CA . ARG B 2 76 ? 55.508 -23.101 -5.928 1.00 49.82 ? 76 ARG B CA 1 ATOM 3133 C C . ARG B 2 76 ? 54.396 -23.696 -6.780 1.00 49.68 ? 76 ARG B C 1 ATOM 3134 O O . ARG B 2 76 ? 54.451 -23.624 -8.004 1.00 48.44 ? 76 ARG B O 1 ATOM 3135 C CB . ARG B 2 76 ? 56.340 -24.195 -5.292 1.00 50.40 ? 76 ARG B CB 1 ATOM 3136 C CG . ARG B 2 76 ? 57.648 -23.696 -4.705 1.00 51.74 ? 76 ARG B CG 1 ATOM 3137 C CD . ARG B 2 76 ? 58.245 -24.757 -3.803 1.00 54.01 ? 76 ARG B CD 1 ATOM 3138 N NE . ARG B 2 76 ? 57.306 -25.131 -2.740 1.00 52.21 ? 76 ARG B NE 1 ATOM 3139 C CZ . ARG B 2 76 ? 57.303 -26.293 -2.091 1.00 53.09 ? 76 ARG B CZ 1 ATOM 3140 N NH1 . ARG B 2 76 ? 58.194 -27.238 -2.374 1.00 56.25 ? 76 ARG B NH1 1 ATOM 3141 N NH2 . ARG B 2 76 ? 56.389 -26.513 -1.152 1.00 51.67 ? 76 ARG B NH2 1 ATOM 3142 N N . ILE B 2 77 ? 53.377 -24.259 -6.136 1.00 50.65 ? 77 ILE B N 1 ATOM 3143 C CA . ILE B 2 77 ? 52.262 -24.856 -6.869 1.00 50.89 ? 77 ILE B CA 1 ATOM 3144 C C . ILE B 2 77 ? 51.401 -23.812 -7.576 1.00 51.07 ? 77 ILE B C 1 ATOM 3145 O O . ILE B 2 77 ? 50.777 -24.108 -8.591 1.00 52.08 ? 77 ILE B O 1 ATOM 3146 C CB . ILE B 2 77 ? 51.379 -25.761 -5.992 1.00 52.03 ? 77 ILE B CB 1 ATOM 3147 C CG1 . ILE B 2 77 ? 50.730 -24.980 -4.859 1.00 55.78 ? 77 ILE B CG1 1 ATOM 3148 C CG2 . ILE B 2 77 ? 52.199 -26.919 -5.438 1.00 54.52 ? 77 ILE B CG2 1 ATOM 3149 C CD1 . ILE B 2 77 ? 49.760 -25.821 -4.044 1.00 61.26 ? 77 ILE B CD1 1 ATOM 3150 N N . GLU B 2 78 ? 51.361 -22.596 -7.055 1.00 50.33 ? 78 GLU B N 1 ATOM 3151 C CA . GLU B 2 78 ? 50.660 -21.539 -7.755 1.00 52.12 ? 78 GLU B CA 1 ATOM 3152 C C . GLU B 2 78 ? 51.363 -21.279 -9.084 1.00 49.73 ? 78 GLU B C 1 ATOM 3153 O O . GLU B 2 78 ? 50.712 -21.108 -10.108 1.00 47.81 ? 78 GLU B O 1 ATOM 3154 C CB . GLU B 2 78 ? 50.609 -20.264 -6.925 1.00 56.98 ? 78 GLU B CB 1 ATOM 3155 C CG . GLU B 2 78 ? 49.845 -19.133 -7.588 1.00 63.24 ? 78 GLU B CG 1 ATOM 3156 C CD . GLU B 2 78 ? 49.694 -17.936 -6.672 1.00 74.52 ? 78 GLU B CD 1 ATOM 3157 O OE1 . GLU B 2 78 ? 50.726 -17.445 -6.151 1.00 79.78 ? 78 GLU B OE1 1 ATOM 3158 O OE2 . GLU B 2 78 ? 48.543 -17.491 -6.463 1.00 81.13 ? 78 GLU B OE2 1 ATOM 3159 N N . ASN B 2 79 ? 52.690 -21.261 -9.050 1.00 47.94 ? 79 ASN B N 1 ATOM 3160 C CA . ASN B 2 79 ? 53.494 -20.990 -10.223 1.00 51.73 ? 79 ASN B CA 1 ATOM 3161 C C . ASN B 2 79 ? 53.383 -22.129 -11.230 1.00 51.01 ? 79 ASN B C 1 ATOM 3162 O O . ASN B 2 79 ? 53.341 -21.902 -12.434 1.00 50.63 ? 79 ASN B O 1 ATOM 3163 C CB . ASN B 2 79 ? 54.953 -20.785 -9.823 1.00 55.06 ? 79 ASN B CB 1 ATOM 3164 C CG . ASN B 2 79 ? 55.829 -20.403 -10.995 1.00 59.77 ? 79 ASN B CG 1 ATOM 3165 O OD1 . ASN B 2 79 ? 55.483 -19.523 -11.775 1.00 64.22 ? 79 ASN B OD1 1 ATOM 3166 N ND2 . ASN B 2 79 ? 56.978 -21.050 -11.115 1.00 63.27 ? 79 ASN B ND2 1 ATOM 3167 N N . LEU B 2 80 ? 53.321 -23.350 -10.714 1.00 50.28 ? 80 LEU B N 1 ATOM 3168 C CA . LEU B 2 80 ? 53.148 -24.534 -11.534 1.00 50.72 ? 80 LEU B CA 1 ATOM 3169 C C . LEU B 2 80 ? 51.804 -24.442 -12.230 1.00 49.71 ? 80 LEU B C 1 ATOM 3170 O O . LEU B 2 80 ? 51.706 -24.676 -13.424 1.00 50.14 ? 80 LEU B O 1 ATOM 3171 C CB . LEU B 2 80 ? 53.217 -25.788 -10.661 1.00 51.20 ? 80 LEU B CB 1 ATOM 3172 C CG . LEU B 2 80 ? 53.335 -27.159 -11.321 1.00 53.78 ? 80 LEU B CG 1 ATOM 3173 C CD1 . LEU B 2 80 ? 53.646 -28.229 -10.283 1.00 56.22 ? 80 LEU B CD1 1 ATOM 3174 C CD2 . LEU B 2 80 ? 52.065 -27.513 -12.067 1.00 56.36 ? 80 LEU B CD2 1 ATOM 3175 N N . ASN B 2 81 ? 50.772 -24.080 -11.479 1.00 49.39 ? 81 ASN B N 1 ATOM 3176 C CA . ASN B 2 81 ? 49.434 -23.916 -12.047 1.00 49.88 ? 81 ASN B CA 1 ATOM 3177 C C . ASN B 2 81 ? 49.417 -22.884 -13.168 1.00 51.62 ? 81 ASN B C 1 ATOM 3178 O O . ASN B 2 81 ? 48.775 -23.082 -14.191 1.00 50.60 ? 81 ASN B O 1 ATOM 3179 C CB . ASN B 2 81 ? 48.442 -23.498 -10.974 1.00 48.20 ? 81 ASN B CB 1 ATOM 3180 C CG . ASN B 2 81 ? 47.026 -23.449 -11.490 1.00 50.53 ? 81 ASN B CG 1 ATOM 3181 O OD1 . ASN B 2 81 ? 46.459 -24.474 -11.861 1.00 52.70 ? 81 ASN B OD1 1 ATOM 3182 N ND2 . ASN B 2 81 ? 46.440 -22.259 -11.508 1.00 50.96 ? 81 ASN B ND2 1 ATOM 3183 N N . LYS B 2 82 ? 50.147 -21.795 -12.959 1.00 52.75 ? 82 LYS B N 1 ATOM 3184 C CA . LYS B 2 82 ? 50.174 -20.684 -13.884 1.00 57.55 ? 82 LYS B CA 1 ATOM 3185 C C . LYS B 2 82 ? 50.887 -21.113 -15.159 1.00 58.81 ? 82 LYS B C 1 ATOM 3186 O O . LYS B 2 82 ? 50.386 -20.890 -16.251 1.00 56.24 ? 82 LYS B O 1 ATOM 3187 C CB . LYS B 2 82 ? 50.892 -19.489 -13.249 1.00 63.73 ? 82 LYS B CB 1 ATOM 3188 C CG . LYS B 2 82 ? 50.173 -18.162 -13.421 1.00 71.10 ? 82 LYS B CG 1 ATOM 3189 C CD . LYS B 2 82 ? 50.475 -17.525 -14.760 1.00 77.01 ? 82 LYS B CD 1 ATOM 3190 C CE . LYS B 2 82 ? 51.784 -16.747 -14.729 1.00 82.81 ? 82 LYS B CE 1 ATOM 3191 N NZ . LYS B 2 82 ? 52.005 -16.052 -16.031 1.00 88.16 ? 82 LYS B NZ 1 ATOM 3192 N N . LYS B 2 83 ? 52.045 -21.750 -15.004 1.00 58.68 ? 83 LYS B N 1 ATOM 3193 C CA . LYS B 2 83 ? 52.834 -22.216 -16.140 1.00 62.05 ? 83 LYS B CA 1 ATOM 3194 C C . LYS B 2 83 ? 52.097 -23.271 -16.964 1.00 59.66 ? 83 LYS B C 1 ATOM 3195 O O . LYS B 2 83 ? 52.246 -23.330 -18.179 1.00 60.83 ? 83 LYS B O 1 ATOM 3196 C CB . LYS B 2 83 ? 54.197 -22.754 -15.682 1.00 66.24 ? 83 LYS B CB 1 ATOM 3197 C CG . LYS B 2 83 ? 55.358 -21.781 -15.850 1.00 74.33 ? 83 LYS B CG 1 ATOM 3198 C CD . LYS B 2 83 ? 55.128 -20.427 -15.186 1.00 79.10 ? 83 LYS B CD 1 ATOM 3199 C CE . LYS B 2 83 ? 54.815 -19.328 -16.199 1.00 86.37 ? 83 LYS B CE 1 ATOM 3200 N NZ . LYS B 2 83 ? 55.952 -19.018 -17.120 1.00 91.81 ? 83 LYS B NZ 1 ATOM 3201 N N . MET B 2 84 ? 51.298 -24.089 -16.295 1.00 56.79 ? 84 MET B N 1 ATOM 3202 C CA . MET B 2 84 ? 50.523 -25.116 -16.964 1.00 56.00 ? 84 MET B CA 1 ATOM 3203 C C . MET B 2 84 ? 49.394 -24.518 -17.808 1.00 53.70 ? 84 MET B C 1 ATOM 3204 O O . MET B 2 84 ? 49.219 -24.903 -18.966 1.00 53.42 ? 84 MET B O 1 ATOM 3205 C CB . MET B 2 84 ? 49.945 -26.089 -15.940 1.00 56.55 ? 84 MET B CB 1 ATOM 3206 C CG . MET B 2 84 ? 49.480 -27.402 -16.540 1.00 60.30 ? 84 MET B CG 1 ATOM 3207 S SD . MET B 2 84 ? 47.913 -27.953 -15.871 1.00 66.00 ? 84 MET B SD 1 ATOM 3208 C CE . MET B 2 84 ? 46.859 -26.579 -16.305 1.00 66.14 ? 84 MET B CE 1 ATOM 3209 N N . GLU B 2 85 ? 48.636 -23.586 -17.238 1.00 67.57 ? 85 GLU B N 1 ATOM 3210 C CA . GLU B 2 85 ? 47.527 -22.968 -17.964 1.00 67.38 ? 85 GLU B CA 1 ATOM 3211 C C . GLU B 2 85 ? 48.069 -22.231 -19.191 1.00 64.39 ? 85 GLU B C 1 ATOM 3212 O O . GLU B 2 85 ? 47.614 -22.459 -20.316 1.00 62.32 ? 85 GLU B O 1 ATOM 3213 C CB . GLU B 2 85 ? 46.738 -22.003 -17.074 1.00 71.66 ? 85 GLU B CB 1 ATOM 3214 C CG . GLU B 2 85 ? 46.166 -22.618 -15.792 1.00 77.11 ? 85 GLU B CG 1 ATOM 3215 C CD . GLU B 2 85 ? 44.653 -22.826 -15.807 1.00 80.53 ? 85 GLU B CD 1 ATOM 3216 O OE1 . GLU B 2 85 ? 44.185 -23.795 -16.433 1.00 81.32 ? 85 GLU B OE1 1 ATOM 3217 O OE2 . GLU B 2 85 ? 43.928 -22.025 -15.175 1.00 84.23 ? 85 GLU B OE2 1 ATOM 3218 N N . ASP B 2 86 ? 49.054 -21.367 -18.959 1.00 62.99 ? 86 ASP B N 1 ATOM 3219 C CA . ASP B 2 86 ? 49.729 -20.618 -20.018 1.00 62.28 ? 86 ASP B CA 1 ATOM 3220 C C . ASP B 2 86 ? 50.350 -21.497 -21.093 1.00 58.91 ? 86 ASP B C 1 ATOM 3221 O O . ASP B 2 86 ? 50.274 -21.179 -22.277 1.00 57.46 ? 86 ASP B O 1 ATOM 3222 C CB . ASP B 2 86 ? 50.832 -19.732 -19.429 1.00 65.22 ? 86 ASP B CB 1 ATOM 3223 C CG . ASP B 2 86 ? 50.349 -18.345 -19.105 1.00 70.01 ? 86 ASP B CG 1 ATOM 3224 O OD1 . ASP B 2 86 ? 49.652 -17.753 -19.968 1.00 76.17 ? 86 ASP B OD1 1 ATOM 3225 O OD2 . ASP B 2 86 ? 50.675 -17.836 -18.010 1.00 71.24 ? 86 ASP B OD2 1 ATOM 3226 N N . GLY B 2 87 ? 50.988 -22.580 -20.670 1.00 56.95 ? 87 GLY B N 1 ATOM 3227 C CA . GLY B 2 87 ? 51.629 -23.498 -21.584 1.00 55.31 ? 87 GLY B CA 1 ATOM 3228 C C . GLY B 2 87 ? 50.647 -24.040 -22.602 1.00 54.79 ? 87 GLY B C 1 ATOM 3229 O O . GLY B 2 87 ? 50.921 -24.023 -23.814 1.00 53.13 ? 87 GLY B O 1 ATOM 3230 N N . PHE B 2 88 ? 49.500 -24.510 -22.118 1.00 53.13 ? 88 PHE B N 1 ATOM 3231 C CA . PHE B 2 88 ? 48.485 -25.056 -23.003 1.00 52.90 ? 88 PHE B CA 1 ATOM 3232 C C . PHE B 2 88 ? 47.899 -23.983 -23.925 1.00 54.20 ? 88 PHE B C 1 ATOM 3233 O O . PHE B 2 88 ? 47.670 -24.253 -25.102 1.00 54.70 ? 88 PHE B O 1 ATOM 3234 C CB . PHE B 2 88 ? 47.382 -25.761 -22.213 1.00 53.46 ? 88 PHE B CB 1 ATOM 3235 C CG . PHE B 2 88 ? 47.772 -27.123 -21.715 1.00 53.75 ? 88 PHE B CG 1 ATOM 3236 C CD1 . PHE B 2 88 ? 48.094 -28.134 -22.601 1.00 53.22 ? 88 PHE B CD1 1 ATOM 3237 C CD2 . PHE B 2 88 ? 47.817 -27.398 -20.362 1.00 55.46 ? 88 PHE B CD2 1 ATOM 3238 C CE1 . PHE B 2 88 ? 48.453 -29.392 -22.152 1.00 53.97 ? 88 PHE B CE1 1 ATOM 3239 C CE2 . PHE B 2 88 ? 48.174 -28.653 -19.904 1.00 56.14 ? 88 PHE B CE2 1 ATOM 3240 C CZ . PHE B 2 88 ? 48.494 -29.650 -20.800 1.00 56.19 ? 88 PHE B CZ 1 ATOM 3241 N N . LEU B 2 89 ? 47.674 -22.772 -23.411 1.00 56.18 ? 89 LEU B N 1 ATOM 3242 C CA . LEU B 2 89 ? 47.196 -21.671 -24.251 1.00 57.26 ? 89 LEU B CA 1 ATOM 3243 C C . LEU B 2 89 ? 48.137 -21.420 -25.422 1.00 55.11 ? 89 LEU B C 1 ATOM 3244 O O . LEU B 2 89 ? 47.695 -21.249 -26.546 1.00 52.75 ? 89 LEU B O 1 ATOM 3245 C CB . LEU B 2 89 ? 47.067 -20.375 -23.463 1.00 60.76 ? 89 LEU B CB 1 ATOM 3246 C CG . LEU B 2 89 ? 45.987 -20.298 -22.384 1.00 66.71 ? 89 LEU B CG 1 ATOM 3247 C CD1 . LEU B 2 89 ? 46.014 -18.898 -21.768 1.00 68.94 ? 89 LEU B CD1 1 ATOM 3248 C CD2 . LEU B 2 89 ? 44.595 -20.656 -22.921 1.00 67.66 ? 89 LEU B CD2 1 ATOM 3249 N N . ASP B 2 90 ? 49.434 -21.396 -25.145 1.00 55.06 ? 90 ASP B N 1 ATOM 3250 C CA . ASP B 2 90 ? 50.427 -21.149 -26.179 1.00 55.08 ? 90 ASP B CA 1 ATOM 3251 C C . ASP B 2 90 ? 50.437 -22.265 -27.216 1.00 52.29 ? 90 ASP B C 1 ATOM 3252 O O . ASP B 2 90 ? 50.565 -22.000 -28.405 1.00 53.26 ? 90 ASP B O 1 ATOM 3253 C CB . ASP B 2 90 ? 51.821 -20.985 -25.569 1.00 57.01 ? 90 ASP B CB 1 ATOM 3254 C CG . ASP B 2 90 ? 51.963 -19.704 -24.783 1.00 61.03 ? 90 ASP B CG 1 ATOM 3255 O OD1 . ASP B 2 90 ? 51.077 -18.830 -24.888 1.00 63.40 ? 90 ASP B OD1 1 ATOM 3256 O OD2 . ASP B 2 90 ? 52.969 -19.567 -24.054 1.00 66.87 ? 90 ASP B OD2 1 ATOM 3257 N N . VAL B 2 91 ? 50.298 -23.502 -26.762 1.00 50.62 ? 91 VAL B N 1 ATOM 3258 C CA . VAL B 2 91 ? 50.238 -24.645 -27.658 1.00 49.54 ? 91 VAL B CA 1 ATOM 3259 C C . VAL B 2 91 ? 49.031 -24.552 -28.589 1.00 49.87 ? 91 VAL B C 1 ATOM 3260 O O . VAL B 2 91 ? 49.154 -24.793 -29.792 1.00 50.47 ? 91 VAL B O 1 ATOM 3261 C CB . VAL B 2 91 ? 50.173 -25.969 -26.884 1.00 49.38 ? 91 VAL B CB 1 ATOM 3262 C CG1 . VAL B 2 91 ? 49.825 -27.119 -27.816 1.00 49.15 ? 91 VAL B CG1 1 ATOM 3263 C CG2 . VAL B 2 91 ? 51.501 -26.235 -26.178 1.00 50.41 ? 91 VAL B CG2 1 ATOM 3264 N N . TRP B 2 92 ? 47.873 -24.204 -28.041 1.00 49.79 ? 92 TRP B N 1 ATOM 3265 C CA . TRP B 2 92 ? 46.662 -24.136 -28.848 1.00 50.19 ? 92 TRP B CA 1 ATOM 3266 C C . TRP B 2 92 ? 46.612 -22.894 -29.731 1.00 49.66 ? 92 TRP B C 1 ATOM 3267 O O . TRP B 2 92 ? 46.056 -22.937 -30.825 1.00 49.48 ? 92 TRP B O 1 ATOM 3268 C CB . TRP B 2 92 ? 45.419 -24.245 -27.973 1.00 51.46 ? 92 TRP B CB 1 ATOM 3269 C CG . TRP B 2 92 ? 45.199 -25.643 -27.518 1.00 53.46 ? 92 TRP B CG 1 ATOM 3270 C CD1 . TRP B 2 92 ? 45.321 -26.124 -26.246 1.00 55.58 ? 92 TRP B CD1 1 ATOM 3271 C CD2 . TRP B 2 92 ? 44.845 -26.761 -28.336 1.00 53.51 ? 92 TRP B CD2 1 ATOM 3272 N NE1 . TRP B 2 92 ? 45.051 -27.471 -26.222 1.00 57.05 ? 92 TRP B NE1 1 ATOM 3273 C CE2 . TRP B 2 92 ? 44.754 -27.885 -27.493 1.00 55.28 ? 92 TRP B CE2 1 ATOM 3274 C CE3 . TRP B 2 92 ? 44.590 -26.919 -29.702 1.00 54.09 ? 92 TRP B CE3 1 ATOM 3275 C CZ2 . TRP B 2 92 ? 44.415 -29.146 -27.966 1.00 57.18 ? 92 TRP B CZ2 1 ATOM 3276 C CZ3 . TRP B 2 92 ? 44.248 -28.174 -30.173 1.00 54.78 ? 92 TRP B CZ3 1 ATOM 3277 C CH2 . TRP B 2 92 ? 44.163 -29.272 -29.305 1.00 56.80 ? 92 TRP B CH2 1 ATOM 3278 N N . THR B 2 93 ? 47.207 -21.800 -29.270 1.00 49.39 ? 93 THR B N 1 ATOM 3279 C CA . THR B 2 93 ? 47.329 -20.616 -30.091 1.00 49.34 ? 93 THR B CA 1 ATOM 3280 C C . THR B 2 93 ? 48.181 -20.953 -31.306 1.00 49.64 ? 93 THR B C 1 ATOM 3281 O O . THR B 2 93 ? 47.805 -20.634 -32.435 1.00 50.63 ? 93 THR B O 1 ATOM 3282 C CB . THR B 2 93 ? 47.945 -19.453 -29.313 1.00 50.30 ? 93 THR B CB 1 ATOM 3283 O OG1 . THR B 2 93 ? 47.042 -19.062 -28.281 1.00 51.90 ? 93 THR B OG1 1 ATOM 3284 C CG2 . THR B 2 93 ? 48.177 -18.266 -30.208 1.00 51.61 ? 93 THR B CG2 1 ATOM 3285 N N . TYR B 2 94 ? 49.309 -21.618 -31.064 1.00 49.38 ? 94 TYR B N 1 ATOM 3286 C CA . TYR B 2 94 ? 50.214 -22.035 -32.127 1.00 48.92 ? 94 TYR B CA 1 ATOM 3287 C C . TYR B 2 94 ? 49.486 -22.934 -33.122 1.00 48.70 ? 94 TYR B C 1 ATOM 3288 O O . TYR B 2 94 ? 49.485 -22.660 -34.317 1.00 47.12 ? 94 TYR B O 1 ATOM 3289 C CB . TYR B 2 94 ? 51.443 -22.743 -31.544 1.00 49.47 ? 94 TYR B CB 1 ATOM 3290 C CG . TYR B 2 94 ? 52.307 -23.450 -32.562 1.00 49.19 ? 94 TYR B CG 1 ATOM 3291 C CD1 . TYR B 2 94 ? 52.029 -24.757 -32.949 1.00 48.58 ? 94 TYR B CD1 1 ATOM 3292 C CD2 . TYR B 2 94 ? 53.405 -22.821 -33.131 1.00 49.86 ? 94 TYR B CD2 1 ATOM 3293 C CE1 . TYR B 2 94 ? 52.813 -25.408 -33.885 1.00 49.32 ? 94 TYR B CE1 1 ATOM 3294 C CE2 . TYR B 2 94 ? 54.193 -23.465 -34.073 1.00 50.00 ? 94 TYR B CE2 1 ATOM 3295 C CZ . TYR B 2 94 ? 53.892 -24.758 -34.444 1.00 50.10 ? 94 TYR B CZ 1 ATOM 3296 O OH . TYR B 2 94 ? 54.672 -25.413 -35.370 1.00 52.48 ? 94 TYR B OH 1 ATOM 3297 N N . ASN B 2 95 ? 48.849 -23.990 -32.627 1.00 50.12 ? 95 ASN B N 1 ATOM 3298 C CA . ASN B 2 95 ? 48.100 -24.898 -33.491 1.00 48.98 ? 95 ASN B CA 1 ATOM 3299 C C . ASN B 2 95 ? 47.114 -24.138 -34.377 1.00 50.19 ? 95 ASN B C 1 ATOM 3300 O O . ASN B 2 95 ? 47.074 -24.358 -35.591 1.00 50.74 ? 95 ASN B O 1 ATOM 3301 C CB . ASN B 2 95 ? 47.368 -25.966 -32.677 1.00 49.65 ? 95 ASN B CB 1 ATOM 3302 C CG . ASN B 2 95 ? 48.314 -27.001 -32.076 1.00 52.56 ? 95 ASN B CG 1 ATOM 3303 O OD1 . ASN B 2 95 ? 49.501 -27.015 -32.371 1.00 53.19 ? 95 ASN B OD1 1 ATOM 3304 N ND2 . ASN B 2 95 ? 47.784 -27.873 -31.225 1.00 54.70 ? 95 ASN B ND2 1 ATOM 3305 N N . ALA B 2 96 ? 46.347 -23.232 -33.777 1.00 49.64 ? 96 ALA B N 1 ATOM 3306 C CA . ALA B 2 96 ? 45.324 -22.484 -34.508 1.00 49.67 ? 96 ALA B CA 1 ATOM 3307 C C . ALA B 2 96 ? 45.923 -21.587 -35.598 1.00 48.59 ? 96 ALA B C 1 ATOM 3308 O O . ALA B 2 96 ? 45.458 -21.588 -36.721 1.00 47.80 ? 96 ALA B O 1 ATOM 3309 C CB . ALA B 2 96 ? 44.493 -21.643 -33.548 1.00 51.15 ? 96 ALA B CB 1 ATOM 3310 N N . GLU B 2 97 ? 46.949 -20.821 -35.262 1.00 49.19 ? 97 GLU B N 1 ATOM 3311 C CA . GLU B 2 97 ? 47.527 -19.886 -36.225 1.00 50.60 ? 97 GLU B CA 1 ATOM 3312 C C . GLU B 2 97 ? 48.252 -20.609 -37.354 1.00 50.05 ? 97 GLU B C 1 ATOM 3313 O O . GLU B 2 97 ? 48.190 -20.177 -38.502 1.00 50.36 ? 97 GLU B O 1 ATOM 3314 C CB . GLU B 2 97 ? 48.447 -18.885 -35.526 1.00 52.25 ? 97 GLU B CB 1 ATOM 3315 C CG . GLU B 2 97 ? 47.664 -17.950 -34.612 1.00 54.90 ? 97 GLU B CG 1 ATOM 3316 C CD . GLU B 2 97 ? 48.523 -17.001 -33.813 1.00 57.73 ? 97 GLU B CD 1 ATOM 3317 O OE1 . GLU B 2 97 ? 49.763 -17.066 -33.915 1.00 60.37 ? 97 GLU B OE1 1 ATOM 3318 O OE2 . GLU B 2 97 ? 47.947 -16.184 -33.066 1.00 61.43 ? 97 GLU B OE2 1 ATOM 3319 N N . LEU B 2 98 ? 48.913 -21.719 -37.036 1.00 48.86 ? 98 LEU B N 1 ATOM 3320 C CA . LEU B 2 98 ? 49.633 -22.484 -38.039 1.00 47.83 ? 98 LEU B CA 1 ATOM 3321 C C . LEU B 2 98 ? 48.664 -23.184 -38.979 1.00 46.80 ? 98 LEU B C 1 ATOM 3322 O O . LEU B 2 98 ? 48.892 -23.238 -40.174 1.00 47.13 ? 98 LEU B O 1 ATOM 3323 C CB . LEU B 2 98 ? 50.549 -23.515 -37.389 1.00 48.14 ? 98 LEU B CB 1 ATOM 3324 C CG . LEU B 2 98 ? 51.536 -24.203 -38.334 1.00 49.26 ? 98 LEU B CG 1 ATOM 3325 C CD1 . LEU B 2 98 ? 52.627 -23.234 -38.769 1.00 49.86 ? 98 LEU B CD1 1 ATOM 3326 C CD2 . LEU B 2 98 ? 52.143 -25.435 -37.676 1.00 50.28 ? 98 LEU B CD2 1 ATOM 3327 N N . LEU B 2 99 ? 47.584 -23.724 -38.439 1.00 46.66 ? 99 LEU B N 1 ATOM 3328 C CA . LEU B 2 99 ? 46.614 -24.419 -39.261 1.00 46.61 ? 99 LEU B CA 1 ATOM 3329 C C . LEU B 2 99 ? 46.015 -23.453 -40.284 1.00 46.56 ? 99 LEU B C 1 ATOM 3330 O O . LEU B 2 99 ? 45.814 -23.806 -41.453 1.00 45.70 ? 99 LEU B O 1 ATOM 3331 C CB . LEU B 2 99 ? 45.512 -25.018 -38.391 1.00 48.76 ? 99 LEU B CB 1 ATOM 3332 C CG . LEU B 2 99 ? 44.463 -25.864 -39.118 1.00 50.92 ? 99 LEU B CG 1 ATOM 3333 C CD1 . LEU B 2 99 ? 45.118 -27.045 -39.806 1.00 51.54 ? 99 LEU B CD1 1 ATOM 3334 C CD2 . LEU B 2 99 ? 43.393 -26.339 -38.148 1.00 53.52 ? 99 LEU B CD2 1 ATOM 3335 N N . VAL B 2 100 ? 45.735 -22.232 -39.838 1.00 45.68 ? 100 VAL B N 1 ATOM 3336 C CA . VAL B 2 100 ? 45.152 -21.224 -40.714 1.00 44.71 ? 100 VAL B CA 1 ATOM 3337 C C . VAL B 2 100 ? 46.120 -20.832 -41.835 1.00 43.33 ? 100 VAL B C 1 ATOM 3338 O O . VAL B 2 100 ? 45.721 -20.806 -42.997 1.00 41.83 ? 100 VAL B O 1 ATOM 3339 C CB . VAL B 2 100 ? 44.669 -19.995 -39.922 1.00 44.93 ? 100 VAL B CB 1 ATOM 3340 C CG1 . VAL B 2 100 ? 44.378 -18.823 -40.851 1.00 45.56 ? 100 VAL B CG1 1 ATOM 3341 C CG2 . VAL B 2 100 ? 43.422 -20.368 -39.138 1.00 45.77 ? 100 VAL B CG2 1 ATOM 3342 N N . LEU B 2 101 ? 47.372 -20.534 -41.488 1.00 42.29 ? 101 LEU B N 1 ATOM 3343 C CA . LEU B 2 101 ? 48.389 -20.214 -42.490 1.00 42.17 ? 101 LEU B CA 1 ATOM 3344 C C . LEU B 2 101 ? 48.567 -21.356 -43.501 1.00 41.98 ? 101 LEU B C 1 ATOM 3345 O O . LEU B 2 101 ? 48.547 -21.133 -44.708 1.00 42.46 ? 101 LEU B O 1 ATOM 3346 C CB . LEU B 2 101 ? 49.740 -19.927 -41.834 1.00 42.54 ? 101 LEU B CB 1 ATOM 3347 C CG . LEU B 2 101 ? 49.876 -18.676 -40.973 1.00 45.04 ? 101 LEU B CG 1 ATOM 3348 C CD1 . LEU B 2 101 ? 51.312 -18.554 -40.490 1.00 46.91 ? 101 LEU B CD1 1 ATOM 3349 C CD2 . LEU B 2 101 ? 49.464 -17.415 -41.713 1.00 46.69 ? 101 LEU B CD2 1 ATOM 3350 N N . MET B 2 102 ? 48.753 -22.572 -43.005 1.00 41.71 ? 102 MET B N 1 ATOM 3351 C CA . MET B 2 102 ? 48.981 -23.714 -43.875 1.00 43.27 ? 102 MET B CA 1 ATOM 3352 C C . MET B 2 102 ? 47.796 -23.976 -44.794 1.00 43.90 ? 102 MET B C 1 ATOM 3353 O O . MET B 2 102 ? 47.981 -24.215 -45.994 1.00 45.31 ? 102 MET B O 1 ATOM 3354 C CB . MET B 2 102 ? 49.273 -24.972 -43.068 1.00 44.49 ? 102 MET B CB 1 ATOM 3355 C CG . MET B 2 102 ? 50.668 -25.016 -42.486 1.00 48.05 ? 102 MET B CG 1 ATOM 3356 S SD . MET B 2 102 ? 50.916 -26.552 -41.574 1.00 53.09 ? 102 MET B SD 1 ATOM 3357 C CE . MET B 2 102 ? 52.679 -26.458 -41.264 1.00 55.86 ? 102 MET B CE 1 ATOM 3358 N N . GLU B 2 103 ? 46.588 -23.949 -44.242 1.00 43.12 ? 103 GLU B N 1 ATOM 3359 C CA . GLU B 2 103 ? 45.414 -24.281 -45.039 1.00 44.59 ? 103 GLU B CA 1 ATOM 3360 C C . GLU B 2 103 ? 45.011 -23.138 -45.974 1.00 44.03 ? 103 GLU B C 1 ATOM 3361 O O . GLU B 2 103 ? 44.459 -23.377 -47.039 1.00 44.94 ? 103 GLU B O 1 ATOM 3362 C CB . GLU B 2 103 ? 44.252 -24.723 -44.148 1.00 46.03 ? 103 GLU B CB 1 ATOM 3363 C CG . GLU B 2 103 ? 44.448 -26.115 -43.540 1.00 48.37 ? 103 GLU B CG 1 ATOM 3364 C CD . GLU B 2 103 ? 44.594 -27.235 -44.574 1.00 50.02 ? 103 GLU B CD 1 ATOM 3365 O OE1 . GLU B 2 103 ? 43.935 -27.180 -45.627 1.00 49.34 ? 103 GLU B OE1 1 ATOM 3366 O OE2 . GLU B 2 103 ? 45.370 -28.191 -44.336 1.00 53.67 ? 103 GLU B OE2 1 ATOM 3367 N N . ASN B 2 104 ? 45.301 -21.903 -45.590 1.00 44.34 ? 104 ASN B N 1 ATOM 3368 C CA . ASN B 2 104 ? 45.096 -20.782 -46.492 1.00 43.79 ? 104 ASN B CA 1 ATOM 3369 C C . ASN B 2 104 ? 45.969 -20.939 -47.735 1.00 43.75 ? 104 ASN B C 1 ATOM 3370 O O . ASN B 2 104 ? 45.524 -20.676 -48.842 1.00 40.54 ? 104 ASN B O 1 ATOM 3371 C CB . ASN B 2 104 ? 45.387 -19.446 -45.802 1.00 43.54 ? 104 ASN B CB 1 ATOM 3372 C CG . ASN B 2 104 ? 44.248 -18.986 -44.904 1.00 45.10 ? 104 ASN B CG 1 ATOM 3373 O OD1 . ASN B 2 104 ? 43.163 -19.577 -44.890 1.00 44.61 ? 104 ASN B OD1 1 ATOM 3374 N ND2 . ASN B 2 104 ? 44.491 -17.923 -44.145 1.00 46.57 ? 104 ASN B ND2 1 ATOM 3375 N N . GLU B 2 105 ? 47.208 -21.378 -47.554 1.00 45.68 ? 105 GLU B N 1 ATOM 3376 C CA . GLU B 2 105 ? 48.078 -21.596 -48.696 1.00 48.57 ? 105 GLU B CA 1 ATOM 3377 C C . GLU B 2 105 ? 47.497 -22.680 -49.589 1.00 46.25 ? 105 GLU B C 1 ATOM 3378 O O . GLU B 2 105 ? 47.464 -22.535 -50.801 1.00 43.16 ? 105 GLU B O 1 ATOM 3379 C CB . GLU B 2 105 ? 49.480 -21.982 -48.257 1.00 54.48 ? 105 GLU B CB 1 ATOM 3380 C CG . GLU B 2 105 ? 50.537 -21.750 -49.318 1.00 61.53 ? 105 GLU B CG 1 ATOM 3381 C CD . GLU B 2 105 ? 51.902 -21.552 -48.707 1.00 70.98 ? 105 GLU B CD 1 ATOM 3382 O OE1 . GLU B 2 105 ? 52.337 -22.460 -47.957 1.00 79.98 ? 105 GLU B OE1 1 ATOM 3383 O OE2 . GLU B 2 105 ? 52.529 -20.492 -48.957 1.00 74.23 ? 105 GLU B OE2 1 ATOM 3384 N N . ARG B 2 106 ? 47.003 -23.752 -48.985 1.00 46.79 ? 106 ARG B N 1 ATOM 3385 C CA . ARG B 2 106 ? 46.425 -24.837 -49.768 1.00 48.13 ? 106 ARG B CA 1 ATOM 3386 C C . ARG B 2 106 ? 45.113 -24.450 -50.454 1.00 45.32 ? 106 ARG B C 1 ATOM 3387 O O . ARG B 2 106 ? 44.821 -24.945 -51.537 1.00 45.33 ? 106 ARG B O 1 ATOM 3388 C CB . ARG B 2 106 ? 46.275 -26.100 -48.921 1.00 51.92 ? 106 ARG B CB 1 ATOM 3389 C CG . ARG B 2 106 ? 47.624 -26.626 -48.436 1.00 57.01 ? 106 ARG B CG 1 ATOM 3390 C CD . ARG B 2 106 ? 47.579 -28.081 -47.988 1.00 63.27 ? 106 ARG B CD 1 ATOM 3391 N NE . ARG B 2 106 ? 48.085 -29.003 -49.019 1.00 68.89 ? 106 ARG B NE 1 ATOM 3392 C CZ . ARG B 2 106 ? 47.363 -29.907 -49.687 1.00 71.58 ? 106 ARG B CZ 1 ATOM 3393 N NH1 . ARG B 2 106 ? 46.059 -30.060 -49.466 1.00 74.23 ? 106 ARG B NH1 1 ATOM 3394 N NH2 . ARG B 2 106 ? 47.957 -30.683 -50.587 1.00 76.61 ? 106 ARG B NH2 1 ATOM 3395 N N . THR B 2 107 ? 44.340 -23.550 -49.854 1.00 43.49 ? 107 THR B N 1 ATOM 3396 C CA . THR B 2 107 ? 43.079 -23.118 -50.454 1.00 41.47 ? 107 THR B CA 1 ATOM 3397 C C . THR B 2 107 ? 43.326 -22.285 -51.710 1.00 40.72 ? 107 THR B C 1 ATOM 3398 O O . THR B 2 107 ? 42.687 -22.492 -52.725 1.00 39.64 ? 107 THR B O 1 ATOM 3399 C CB . THR B 2 107 ? 42.202 -22.342 -49.455 1.00 41.71 ? 107 THR B CB 1 ATOM 3400 O OG1 . THR B 2 107 ? 41.693 -23.252 -48.477 1.00 42.59 ? 107 THR B OG1 1 ATOM 3401 C CG2 . THR B 2 107 ? 41.005 -21.701 -50.152 1.00 43.29 ? 107 THR B CG2 1 ATOM 3402 N N . LEU B 2 108 ? 44.259 -21.348 -51.637 1.00 40.09 ? 108 LEU B N 1 ATOM 3403 C CA . LEU B 2 108 ? 44.607 -20.565 -52.798 1.00 41.29 ? 108 LEU B CA 1 ATOM 3404 C C . LEU B 2 108 ? 45.148 -21.460 -53.928 1.00 41.09 ? 108 LEU B C 1 ATOM 3405 O O . LEU B 2 108 ? 44.757 -21.312 -55.094 1.00 40.05 ? 108 LEU B O 1 ATOM 3406 C CB . LEU B 2 108 ? 45.618 -19.485 -52.426 1.00 41.86 ? 108 LEU B CB 1 ATOM 3407 C CG . LEU B 2 108 ? 45.157 -18.491 -51.360 1.00 43.44 ? 108 LEU B CG 1 ATOM 3408 C CD1 . LEU B 2 108 ? 46.185 -17.383 -51.229 1.00 45.59 ? 108 LEU B CD1 1 ATOM 3409 C CD2 . LEU B 2 108 ? 43.792 -17.896 -51.665 1.00 44.62 ? 108 LEU B CD2 1 ATOM 3410 N N . ASP B 2 109 ? 46.036 -22.385 -53.576 1.00 39.94 ? 109 ASP B N 1 ATOM 3411 C CA . ASP B 2 109 ? 46.577 -23.329 -54.545 1.00 40.35 ? 109 ASP B CA 1 ATOM 3412 C C . ASP B 2 109 ? 45.498 -24.249 -55.136 1.00 39.45 ? 109 ASP B C 1 ATOM 3413 O O . ASP B 2 109 ? 45.576 -24.618 -56.300 1.00 40.74 ? 109 ASP B O 1 ATOM 3414 C CB . ASP B 2 109 ? 47.694 -24.160 -53.915 1.00 41.71 ? 109 ASP B CB 1 ATOM 3415 C CG . ASP B 2 109 ? 48.983 -23.348 -53.678 1.00 45.71 ? 109 ASP B CG 1 ATOM 3416 O OD1 . ASP B 2 109 ? 49.282 -22.432 -54.482 1.00 46.80 ? 109 ASP B OD1 1 ATOM 3417 O OD2 . ASP B 2 109 ? 49.711 -23.647 -52.688 1.00 49.56 ? 109 ASP B OD2 1 ATOM 3418 N N . PHE B 2 110 ? 44.505 -24.619 -54.331 1.00 37.94 ? 110 PHE B N 1 ATOM 3419 C CA . PHE B 2 110 ? 43.402 -25.484 -54.761 1.00 36.23 ? 110 PHE B CA 1 ATOM 3420 C C . PHE B 2 110 ? 42.628 -24.818 -55.894 1.00 36.73 ? 110 PHE B C 1 ATOM 3421 O O . PHE B 2 110 ? 42.386 -25.429 -56.932 1.00 39.11 ? 110 PHE B O 1 ATOM 3422 C CB . PHE B 2 110 ? 42.498 -25.762 -53.555 1.00 36.30 ? 110 PHE B CB 1 ATOM 3423 C CG . PHE B 2 110 ? 41.256 -26.555 -53.859 1.00 37.03 ? 110 PHE B CG 1 ATOM 3424 C CD1 . PHE B 2 110 ? 41.328 -27.790 -54.470 1.00 38.19 ? 110 PHE B CD1 1 ATOM 3425 C CD2 . PHE B 2 110 ? 40.014 -26.076 -53.486 1.00 37.57 ? 110 PHE B CD2 1 ATOM 3426 C CE1 . PHE B 2 110 ? 40.181 -28.513 -54.736 1.00 39.97 ? 110 PHE B CE1 1 ATOM 3427 C CE2 . PHE B 2 110 ? 38.861 -26.793 -53.748 1.00 39.39 ? 110 PHE B CE2 1 ATOM 3428 C CZ . PHE B 2 110 ? 38.943 -28.015 -54.374 1.00 40.54 ? 110 PHE B CZ 1 ATOM 3429 N N . HIS B 2 111 ? 42.258 -23.557 -55.695 1.00 36.02 ? 111 HIS B N 1 ATOM 3430 C CA . HIS B 2 111 ? 41.603 -22.765 -56.727 1.00 35.99 ? 111 HIS B CA 1 ATOM 3431 C C . HIS B 2 111 ? 42.443 -22.657 -58.007 1.00 36.54 ? 111 HIS B C 1 ATOM 3432 O O . HIS B 2 111 ? 41.915 -22.745 -59.117 1.00 37.79 ? 111 HIS B O 1 ATOM 3433 C CB . HIS B 2 111 ? 41.318 -21.358 -56.213 1.00 36.33 ? 111 HIS B CB 1 ATOM 3434 C CG . HIS B 2 111 ? 40.208 -21.290 -55.215 1.00 37.33 ? 111 HIS B CG 1 ATOM 3435 N ND1 . HIS B 2 111 ? 38.910 -21.636 -55.525 1.00 38.02 ? 111 HIS B ND1 1 ATOM 3436 C CD2 . HIS B 2 111 ? 40.191 -20.873 -53.926 1.00 37.20 ? 111 HIS B CD2 1 ATOM 3437 C CE1 . HIS B 2 111 ? 38.148 -21.462 -54.461 1.00 39.72 ? 111 HIS B CE1 1 ATOM 3438 N NE2 . HIS B 2 111 ? 38.900 -20.996 -53.479 1.00 38.97 ? 111 HIS B NE2 1 ATOM 3439 N N . ASP B 2 112 ? 43.744 -22.449 -57.846 1.00 35.18 ? 112 ASP B N 1 ATOM 3440 C CA . ASP B 2 112 ? 44.644 -22.350 -58.971 1.00 35.74 ? 112 ASP B CA 1 ATOM 3441 C C . ASP B 2 112 ? 44.610 -23.660 -59.760 1.00 37.14 ? 112 ASP B C 1 ATOM 3442 O O . ASP B 2 112 ? 44.484 -23.659 -60.982 1.00 39.58 ? 112 ASP B O 1 ATOM 3443 C CB . ASP B 2 112 ? 46.062 -22.056 -58.469 1.00 36.59 ? 112 ASP B CB 1 ATOM 3444 C CG . ASP B 2 112 ? 47.010 -21.658 -59.583 1.00 37.41 ? 112 ASP B CG 1 ATOM 3445 O OD1 . ASP B 2 112 ? 46.531 -21.352 -60.693 1.00 37.61 ? 112 ASP B OD1 1 ATOM 3446 O OD2 . ASP B 2 112 ? 48.238 -21.653 -59.341 1.00 39.07 ? 112 ASP B OD2 1 ATOM 3447 N N . SER B 2 113 ? 44.705 -24.774 -59.049 1.00 36.75 ? 113 SER B N 1 ATOM 3448 C CA . SER B 2 113 ? 44.588 -26.096 -59.648 1.00 37.82 ? 113 SER B CA 1 ATOM 3449 C C . SER B 2 113 ? 43.263 -26.314 -60.401 1.00 39.20 ? 113 SER B C 1 ATOM 3450 O O . SER B 2 113 ? 43.240 -26.947 -61.463 1.00 39.57 ? 113 SER B O 1 ATOM 3451 C CB . SER B 2 113 ? 44.743 -27.156 -58.560 1.00 38.15 ? 113 SER B CB 1 ATOM 3452 O OG . SER B 2 113 ? 44.364 -28.433 -59.022 1.00 40.23 ? 113 SER B OG 1 ATOM 3453 N N . ASN B 2 114 ? 42.157 -25.816 -59.858 1.00 38.97 ? 114 ASN B N 1 ATOM 3454 C CA . ASN B 2 114 ? 40.868 -26.026 -60.521 1.00 40.03 ? 114 ASN B CA 1 ATOM 3455 C C . ASN B 2 114 ? 40.765 -25.246 -61.822 1.00 38.45 ? 114 ASN B C 1 ATOM 3456 O O . ASN B 2 114 ? 40.137 -25.711 -62.764 1.00 38.79 ? 114 ASN B O 1 ATOM 3457 C CB . ASN B 2 114 ? 39.702 -25.669 -59.608 1.00 41.00 ? 114 ASN B CB 1 ATOM 3458 C CG . ASN B 2 114 ? 39.575 -26.608 -58.437 1.00 42.65 ? 114 ASN B CG 1 ATOM 3459 O OD1 . ASN B 2 114 ? 39.897 -27.798 -58.525 1.00 43.85 ? 114 ASN B OD1 1 ATOM 3460 N ND2 . ASN B 2 114 ? 39.101 -26.080 -57.328 1.00 44.17 ? 114 ASN B ND2 1 ATOM 3461 N N . VAL B 2 115 ? 41.394 -24.075 -61.874 1.00 37.74 ? 115 VAL B N 1 ATOM 3462 C CA . VAL B 2 115 ? 41.428 -23.278 -63.096 1.00 38.37 ? 115 VAL B CA 1 ATOM 3463 C C . VAL B 2 115 ? 42.303 -23.966 -64.130 1.00 38.64 ? 115 VAL B C 1 ATOM 3464 O O . VAL B 2 115 ? 41.942 -24.042 -65.289 1.00 38.25 ? 115 VAL B O 1 ATOM 3465 C CB . VAL B 2 115 ? 41.968 -21.863 -62.842 1.00 39.56 ? 115 VAL B CB 1 ATOM 3466 C CG1 . VAL B 2 115 ? 42.219 -21.137 -64.156 1.00 41.50 ? 115 VAL B CG1 1 ATOM 3467 C CG2 . VAL B 2 115 ? 40.988 -21.069 -62.000 1.00 40.66 ? 115 VAL B CG2 1 ATOM 3468 N N . LYS B 2 116 ? 43.452 -24.466 -63.694 1.00 39.81 ? 116 LYS B N 1 ATOM 3469 C CA . LYS B 2 116 ? 44.369 -25.168 -64.573 1.00 41.85 ? 116 LYS B CA 1 ATOM 3470 C C . LYS B 2 116 ? 43.724 -26.404 -65.190 1.00 42.85 ? 116 LYS B C 1 ATOM 3471 O O . LYS B 2 116 ? 43.876 -26.655 -66.387 1.00 42.68 ? 116 LYS B O 1 ATOM 3472 C CB . LYS B 2 116 ? 45.639 -25.546 -63.801 1.00 43.80 ? 116 LYS B CB 1 ATOM 3473 C CG . LYS B 2 116 ? 46.713 -26.269 -64.595 1.00 46.36 ? 116 LYS B CG 1 ATOM 3474 C CD . LYS B 2 116 ? 47.046 -25.512 -65.867 1.00 51.14 ? 116 LYS B CD 1 ATOM 3475 C CE . LYS B 2 116 ? 48.318 -26.034 -66.521 1.00 55.97 ? 116 LYS B CE 1 ATOM 3476 N NZ . LYS B 2 116 ? 49.519 -25.706 -65.707 1.00 57.50 ? 116 LYS B NZ 1 ATOM 3477 N N . ASN B 2 117 ? 43.001 -27.170 -64.380 1.00 43.65 ? 117 ASN B N 1 ATOM 3478 C CA . ASN B 2 117 ? 42.359 -28.392 -64.868 1.00 46.42 ? 117 ASN B CA 1 ATOM 3479 C C . ASN B 2 117 ? 41.214 -28.107 -65.835 1.00 47.29 ? 117 ASN B C 1 ATOM 3480 O O . ASN B 2 117 ? 40.991 -28.860 -66.785 1.00 48.51 ? 117 ASN B O 1 ATOM 3481 C CB . ASN B 2 117 ? 41.869 -29.250 -63.704 1.00 46.94 ? 117 ASN B CB 1 ATOM 3482 C CG . ASN B 2 117 ? 43.009 -29.791 -62.866 1.00 48.74 ? 117 ASN B CG 1 ATOM 3483 O OD1 . ASN B 2 117 ? 44.139 -29.911 -63.337 1.00 49.80 ? 117 ASN B OD1 1 ATOM 3484 N ND2 . ASN B 2 117 ? 42.721 -30.112 -61.612 1.00 49.34 ? 117 ASN B ND2 1 ATOM 3485 N N . LEU B 2 118 ? 40.493 -27.020 -65.591 1.00 46.57 ? 118 LEU B N 1 ATOM 3486 C CA . LEU B 2 118 ? 39.428 -26.595 -66.493 1.00 47.59 ? 118 LEU B CA 1 ATOM 3487 C C . LEU B 2 118 ? 40.028 -26.185 -67.837 1.00 47.55 ? 118 LEU B C 1 ATOM 3488 O O . LEU B 2 118 ? 39.533 -26.574 -68.896 1.00 48.92 ? 118 LEU B O 1 ATOM 3489 C CB . LEU B 2 118 ? 38.647 -25.434 -65.876 1.00 48.10 ? 118 LEU B CB 1 ATOM 3490 C CG . LEU B 2 118 ? 37.402 -24.950 -66.604 1.00 49.48 ? 118 LEU B CG 1 ATOM 3491 C CD1 . LEU B 2 118 ? 36.455 -26.104 -66.870 1.00 52.69 ? 118 LEU B CD1 1 ATOM 3492 C CD2 . LEU B 2 118 ? 36.715 -23.874 -65.784 1.00 50.06 ? 118 LEU B CD2 1 ATOM 3493 N N . TYR B 2 119 ? 41.114 -25.421 -67.785 1.00 45.67 ? 119 TYR B N 1 ATOM 3494 C CA . TYR B 2 119 ? 41.821 -25.008 -68.986 1.00 45.02 ? 119 TYR B CA 1 ATOM 3495 C C . TYR B 2 119 ? 42.320 -26.208 -69.787 1.00 47.36 ? 119 TYR B C 1 ATOM 3496 O O . TYR B 2 119 ? 42.115 -26.279 -70.993 1.00 49.12 ? 119 TYR B O 1 ATOM 3497 C CB . TYR B 2 119 ? 42.989 -24.093 -68.624 1.00 43.28 ? 119 TYR B CB 1 ATOM 3498 C CG . TYR B 2 119 ? 43.795 -23.638 -69.814 1.00 44.13 ? 119 TYR B CG 1 ATOM 3499 C CD1 . TYR B 2 119 ? 43.362 -22.578 -70.612 1.00 44.79 ? 119 TYR B CD1 1 ATOM 3500 C CD2 . TYR B 2 119 ? 44.987 -24.262 -70.147 1.00 44.69 ? 119 TYR B CD2 1 ATOM 3501 C CE1 . TYR B 2 119 ? 44.102 -22.155 -71.702 1.00 45.49 ? 119 TYR B CE1 1 ATOM 3502 C CE2 . TYR B 2 119 ? 45.728 -23.849 -71.236 1.00 46.81 ? 119 TYR B CE2 1 ATOM 3503 C CZ . TYR B 2 119 ? 45.280 -22.798 -72.007 1.00 47.23 ? 119 TYR B CZ 1 ATOM 3504 O OH . TYR B 2 119 ? 46.017 -22.396 -73.081 1.00 49.23 ? 119 TYR B OH 1 ATOM 3505 N N . ASP B 2 120 ? 42.977 -27.150 -69.125 1.00 48.73 ? 120 ASP B N 1 ATOM 3506 C CA . ASP B 2 120 ? 43.484 -28.324 -69.822 1.00 51.35 ? 120 ASP B CA 1 ATOM 3507 C C . ASP B 2 120 ? 42.338 -29.123 -70.428 1.00 52.48 ? 120 ASP B C 1 ATOM 3508 O O . ASP B 2 120 ? 42.427 -29.573 -71.565 1.00 54.13 ? 120 ASP B O 1 ATOM 3509 C CB . ASP B 2 120 ? 44.349 -29.194 -68.896 1.00 53.04 ? 120 ASP B CB 1 ATOM 3510 C CG . ASP B 2 120 ? 45.690 -28.539 -68.565 1.00 54.71 ? 120 ASP B CG 1 ATOM 3511 O OD1 . ASP B 2 120 ? 46.238 -27.822 -69.431 1.00 57.87 ? 120 ASP B OD1 1 ATOM 3512 O OD2 . ASP B 2 120 ? 46.207 -28.732 -67.443 1.00 55.02 ? 120 ASP B OD2 1 ATOM 3513 N N . LYS B 2 121 ? 41.258 -29.276 -69.676 1.00 53.80 ? 121 LYS B N 1 ATOM 3514 C CA . LYS B 2 121 ? 40.075 -30.007 -70.141 1.00 58.32 ? 121 LYS B CA 1 ATOM 3515 C C . LYS B 2 121 ? 39.598 -29.477 -71.492 1.00 58.03 ? 121 LYS B C 1 ATOM 3516 O O . LYS B 2 121 ? 39.323 -30.250 -72.404 1.00 61.37 ? 121 LYS B O 1 ATOM 3517 C CB . LYS B 2 121 ? 38.970 -29.893 -69.087 1.00 61.66 ? 121 LYS B CB 1 ATOM 3518 C CG . LYS B 2 121 ? 37.624 -30.501 -69.431 1.00 67.22 ? 121 LYS B CG 1 ATOM 3519 C CD . LYS B 2 121 ? 36.756 -30.535 -68.175 1.00 72.05 ? 121 LYS B CD 1 ATOM 3520 C CE . LYS B 2 121 ? 35.299 -30.869 -68.468 1.00 79.25 ? 121 LYS B CE 1 ATOM 3521 N NZ . LYS B 2 121 ? 34.534 -29.695 -68.986 1.00 82.27 ? 121 LYS B NZ 1 ATOM 3522 N N . VAL B 2 122 ? 39.521 -28.156 -71.617 1.00 54.12 ? 122 VAL B N 1 ATOM 3523 C CA . VAL B 2 122 ? 39.158 -27.521 -72.872 1.00 53.45 ? 122 VAL B CA 1 ATOM 3524 C C . VAL B 2 122 ? 40.246 -27.736 -73.920 1.00 55.00 ? 122 VAL B C 1 ATOM 3525 O O . VAL B 2 122 ? 39.948 -28.073 -75.067 1.00 57.26 ? 122 VAL B O 1 ATOM 3526 C CB . VAL B 2 122 ? 38.862 -26.019 -72.671 1.00 51.19 ? 122 VAL B CB 1 ATOM 3527 C CG1 . VAL B 2 122 ? 38.803 -25.271 -73.999 1.00 50.78 ? 122 VAL B CG1 1 ATOM 3528 C CG2 . VAL B 2 122 ? 37.555 -25.859 -71.907 1.00 51.42 ? 122 VAL B CG2 1 ATOM 3529 N N . ARG B 2 123 ? 41.499 -27.564 -73.531 1.00 53.65 ? 123 ARG B N 1 ATOM 3530 C CA . ARG B 2 123 ? 42.611 -27.758 -74.458 1.00 56.49 ? 123 ARG B CA 1 ATOM 3531 C C . ARG B 2 123 ? 42.575 -29.148 -75.107 1.00 59.35 ? 123 ARG B C 1 ATOM 3532 O O . ARG B 2 123 ? 42.726 -29.277 -76.322 1.00 60.87 ? 123 ARG B O 1 ATOM 3533 C CB . ARG B 2 123 ? 43.934 -27.562 -73.724 1.00 58.07 ? 123 ARG B CB 1 ATOM 3534 C CG . ARG B 2 123 ? 45.139 -27.453 -74.638 1.00 61.48 ? 123 ARG B CG 1 ATOM 3535 C CD . ARG B 2 123 ? 46.418 -27.256 -73.834 1.00 63.98 ? 123 ARG B CD 1 ATOM 3536 N NE . ARG B 2 123 ? 46.513 -28.170 -72.694 1.00 64.67 ? 123 ARG B NE 1 ATOM 3537 C CZ . ARG B 2 123 ? 46.823 -29.465 -72.777 1.00 67.80 ? 123 ARG B CZ 1 ATOM 3538 N NH1 . ARG B 2 123 ? 47.075 -30.050 -73.953 1.00 70.05 ? 123 ARG B NH1 1 ATOM 3539 N NH2 . ARG B 2 123 ? 46.881 -30.187 -71.669 1.00 67.55 ? 123 ARG B NH2 1 ATOM 3540 N N . LEU B 2 124 ? 42.350 -30.176 -74.291 1.00 60.64 ? 124 LEU B N 1 ATOM 3541 C CA . LEU B 2 124 ? 42.324 -31.565 -74.757 1.00 64.12 ? 124 LEU B CA 1 ATOM 3542 C C . LEU B 2 124 ? 41.142 -31.880 -75.685 1.00 66.25 ? 124 LEU B C 1 ATOM 3543 O O . LEU B 2 124 ? 41.207 -32.830 -76.461 1.00 70.06 ? 124 LEU B O 1 ATOM 3544 C CB . LEU B 2 124 ? 42.317 -32.528 -73.566 1.00 65.04 ? 124 LEU B CB 1 ATOM 3545 C CG . LEU B 2 124 ? 43.588 -32.505 -72.707 1.00 66.49 ? 124 LEU B CG 1 ATOM 3546 C CD1 . LEU B 2 124 ? 43.362 -33.128 -71.329 1.00 67.96 ? 124 LEU B CD1 1 ATOM 3547 C CD2 . LEU B 2 124 ? 44.747 -33.186 -73.422 1.00 69.38 ? 124 LEU B CD2 1 ATOM 3548 N N . GLN B 2 125 ? 40.066 -31.103 -75.600 1.00 65.06 ? 125 GLN B N 1 ATOM 3549 C CA . GLN B 2 125 ? 38.944 -31.255 -76.526 1.00 66.82 ? 125 GLN B CA 1 ATOM 3550 C C . GLN B 2 125 ? 39.281 -30.639 -77.866 1.00 65.77 ? 125 GLN B C 1 ATOM 3551 O O . GLN B 2 125 ? 39.214 -31.302 -78.898 1.00 69.25 ? 125 GLN B O 1 ATOM 3552 C CB . GLN B 2 125 ? 37.691 -30.574 -75.996 1.00 66.81 ? 125 GLN B CB 1 ATOM 3553 C CG . GLN B 2 125 ? 37.127 -31.188 -74.735 1.00 68.97 ? 125 GLN B CG 1 ATOM 3554 C CD . GLN B 2 125 ? 35.732 -30.681 -74.460 1.00 70.67 ? 125 GLN B CD 1 ATOM 3555 O OE1 . GLN B 2 125 ? 34.790 -31.062 -75.151 1.00 75.73 ? 125 GLN B OE1 1 ATOM 3556 N NE2 . GLN B 2 125 ? 35.591 -29.805 -73.467 1.00 68.49 ? 125 GLN B NE2 1 ATOM 3557 N N . LEU B 2 126 ? 39.653 -29.367 -77.836 1.00 62.24 ? 126 LEU B N 1 ATOM 3558 C CA . LEU B 2 126 ? 39.913 -28.617 -79.048 1.00 63.70 ? 126 LEU B CA 1 ATOM 3559 C C . LEU B 2 126 ? 41.077 -29.200 -79.844 1.00 68.13 ? 126 LEU B C 1 ATOM 3560 O O . LEU B 2 126 ? 41.009 -29.275 -81.061 1.00 71.43 ? 126 LEU B O 1 ATOM 3561 C CB . LEU B 2 126 ? 40.156 -27.134 -78.728 1.00 60.55 ? 126 LEU B CB 1 ATOM 3562 C CG . LEU B 2 126 ? 39.017 -26.422 -77.982 1.00 57.73 ? 126 LEU B CG 1 ATOM 3563 C CD1 . LEU B 2 126 ? 39.239 -24.922 -77.928 1.00 56.40 ? 126 LEU B CD1 1 ATOM 3564 C CD2 . LEU B 2 126 ? 37.675 -26.726 -78.614 1.00 59.42 ? 126 LEU B CD2 1 ATOM 3565 N N . ARG B 2 127 ? 42.127 -29.638 -79.160 1.00 74.89 ? 127 ARG B N 1 ATOM 3566 C CA . ARG B 2 127 ? 43.311 -30.189 -79.831 1.00 80.15 ? 127 ARG B CA 1 ATOM 3567 C C . ARG B 2 127 ? 43.818 -29.171 -80.870 1.00 80.38 ? 127 ARG B C 1 ATOM 3568 O O . ARG B 2 127 ? 43.952 -27.993 -80.542 1.00 79.44 ? 127 ARG B O 1 ATOM 3569 C CB . ARG B 2 127 ? 43.008 -31.580 -80.426 1.00 84.61 ? 127 ARG B CB 1 ATOM 3570 C CG . ARG B 2 127 ? 42.699 -32.642 -79.372 1.00 87.12 ? 127 ARG B CG 1 ATOM 3571 C CD . ARG B 2 127 ? 41.809 -33.769 -79.885 1.00 90.89 ? 127 ARG B CD 1 ATOM 3572 N NE . ARG B 2 127 ? 42.422 -34.531 -80.972 1.00 97.03 ? 127 ARG B NE 1 ATOM 3573 C CZ . ARG B 2 127 ? 41.920 -35.652 -81.495 1.00 103.32 ? 127 ARG B CZ 1 ATOM 3574 N NH1 . ARG B 2 127 ? 40.781 -36.167 -81.036 1.00 105.95 ? 127 ARG B NH1 1 ATOM 3575 N NH2 . ARG B 2 127 ? 42.563 -36.270 -82.482 1.00 105.60 ? 127 ARG B NH2 1 ATOM 3576 N N . ASP B 2 128 ? 44.060 -29.588 -82.112 1.00 83.55 ? 128 ASP B N 1 ATOM 3577 C CA . ASP B 2 128 ? 44.618 -28.677 -83.117 1.00 84.43 ? 128 ASP B CA 1 ATOM 3578 C C . ASP B 2 128 ? 43.570 -27.968 -84.004 1.00 80.75 ? 128 ASP B C 1 ATOM 3579 O O . ASP B 2 128 ? 43.916 -27.432 -85.051 1.00 83.68 ? 128 ASP B O 1 ATOM 3580 C CB . ASP B 2 128 ? 45.663 -29.407 -83.975 1.00 90.44 ? 128 ASP B CB 1 ATOM 3581 C CG . ASP B 2 128 ? 45.059 -30.499 -84.843 1.00 95.92 ? 128 ASP B CG 1 ATOM 3582 O OD1 . ASP B 2 128 ? 43.822 -30.696 -84.806 1.00 94.46 ? 128 ASP B OD1 1 ATOM 3583 O OD2 . ASP B 2 128 ? 45.833 -31.165 -85.568 1.00 104.20 ? 128 ASP B OD2 1 ATOM 3584 N N . ASN B 2 129 ? 42.305 -27.961 -83.586 1.00 76.65 ? 129 ASN B N 1 ATOM 3585 C CA . ASN B 2 129 ? 41.267 -27.154 -84.246 1.00 74.39 ? 129 ASN B CA 1 ATOM 3586 C C . ASN B 2 129 ? 41.195 -25.691 -83.766 1.00 71.48 ? 129 ASN B C 1 ATOM 3587 O O . ASN B 2 129 ? 40.271 -24.964 -84.152 1.00 71.06 ? 129 ASN B O 1 ATOM 3588 C CB . ASN B 2 129 ? 39.888 -27.798 -84.052 1.00 76.13 ? 129 ASN B CB 1 ATOM 3589 C CG . ASN B 2 129 ? 39.697 -29.054 -84.880 1.00 81.31 ? 129 ASN B CG 1 ATOM 3590 O OD1 . ASN B 2 129 ? 40.636 -29.574 -85.489 1.00 87.33 ? 129 ASN B OD1 1 ATOM 3591 N ND2 . ASN B 2 129 ? 38.467 -29.553 -84.902 1.00 81.92 ? 129 ASN B ND2 1 ATOM 3592 N N . ALA B 2 130 ? 42.157 -25.265 -82.940 1.00 69.43 ? 130 ALA B N 1 ATOM 3593 C CA . ALA B 2 130 ? 42.193 -23.905 -82.381 1.00 65.76 ? 130 ALA B CA 1 ATOM 3594 C C . ALA B 2 130 ? 43.627 -23.497 -82.049 1.00 66.55 ? 130 ALA B C 1 ATOM 3595 O O . ALA B 2 130 ? 44.459 -24.359 -81.779 1.00 68.06 ? 130 ALA B O 1 ATOM 3596 C CB . ALA B 2 130 ? 41.339 -23.842 -81.127 1.00 63.43 ? 130 ALA B CB 1 ATOM 3597 N N . LYS B 2 131 ? 43.916 -22.195 -82.057 1.00 66.15 ? 131 LYS B N 1 ATOM 3598 C CA . LYS B 2 131 ? 45.249 -21.702 -81.681 1.00 67.17 ? 131 LYS B CA 1 ATOM 3599 C C . LYS B 2 131 ? 45.289 -21.387 -80.192 1.00 63.98 ? 131 LYS B C 1 ATOM 3600 O O . LYS B 2 131 ? 44.497 -20.587 -79.696 1.00 61.51 ? 131 LYS B O 1 ATOM 3601 C CB . LYS B 2 131 ? 45.639 -20.452 -82.475 1.00 72.27 ? 131 LYS B CB 1 ATOM 3602 C CG . LYS B 2 131 ? 45.409 -20.585 -83.972 1.00 79.91 ? 131 LYS B CG 1 ATOM 3603 C CD . LYS B 2 131 ? 46.248 -19.627 -84.815 1.00 86.90 ? 131 LYS B CD 1 ATOM 3604 C CE . LYS B 2 131 ? 47.544 -20.280 -85.297 1.00 91.80 ? 131 LYS B CE 1 ATOM 3605 N NZ . LYS B 2 131 ? 48.472 -19.336 -85.991 1.00 95.59 ? 131 LYS B NZ 1 ATOM 3606 N N . GLU B 2 132 ? 46.211 -22.020 -79.478 1.00 61.57 ? 132 GLU B N 1 ATOM 3607 C CA . GLU B 2 132 ? 46.421 -21.703 -78.082 1.00 58.83 ? 132 GLU B CA 1 ATOM 3608 C C . GLU B 2 132 ? 47.160 -20.367 -78.004 1.00 59.12 ? 132 GLU B C 1 ATOM 3609 O O . GLU B 2 132 ? 48.344 -20.290 -78.306 1.00 61.53 ? 132 GLU B O 1 ATOM 3610 C CB . GLU B 2 132 ? 47.207 -22.814 -77.402 1.00 59.41 ? 132 GLU B CB 1 ATOM 3611 C CG . GLU B 2 132 ? 47.193 -22.725 -75.889 1.00 59.10 ? 132 GLU B CG 1 ATOM 3612 C CD . GLU B 2 132 ? 47.853 -23.911 -75.202 1.00 61.06 ? 132 GLU B CD 1 ATOM 3613 O OE1 . GLU B 2 132 ? 48.469 -24.765 -75.884 1.00 63.94 ? 132 GLU B OE1 1 ATOM 3614 O OE2 . GLU B 2 132 ? 47.749 -23.985 -73.961 1.00 61.21 ? 132 GLU B OE2 1 ATOM 3615 N N . LEU B 2 133 ? 46.449 -19.312 -77.621 1.00 57.39 ? 133 LEU B N 1 ATOM 3616 C CA . LEU B 2 133 ? 47.015 -17.964 -77.638 1.00 58.94 ? 133 LEU B CA 1 ATOM 3617 C C . LEU B 2 133 ? 48.020 -17.705 -76.533 1.00 61.28 ? 133 LEU B C 1 ATOM 3618 O O . LEU B 2 133 ? 48.865 -16.825 -76.674 1.00 64.78 ? 133 LEU B O 1 ATOM 3619 C CB . LEU B 2 133 ? 45.912 -16.916 -77.561 1.00 57.88 ? 133 LEU B CB 1 ATOM 3620 C CG . LEU B 2 133 ? 44.995 -16.857 -78.779 1.00 57.51 ? 133 LEU B CG 1 ATOM 3621 C CD1 . LEU B 2 133 ? 43.944 -15.776 -78.569 1.00 57.51 ? 133 LEU B CD1 1 ATOM 3622 C CD2 . LEU B 2 133 ? 45.794 -16.603 -80.051 1.00 59.91 ? 133 LEU B CD2 1 ATOM 3623 N N . GLY B 2 134 ? 47.916 -18.449 -75.432 1.00 60.92 ? 134 GLY B N 1 ATOM 3624 C CA . GLY B 2 134 ? 48.874 -18.351 -74.328 1.00 62.70 ? 134 GLY B CA 1 ATOM 3625 C C . GLY B 2 134 ? 48.428 -17.489 -73.159 1.00 61.54 ? 134 GLY B C 1 ATOM 3626 O O . GLY B 2 134 ? 49.208 -17.243 -72.237 1.00 62.88 ? 134 GLY B O 1 ATOM 3627 N N . ASN B 2 135 ? 47.177 -17.039 -73.185 1.00 59.26 ? 135 ASN B N 1 ATOM 3628 C CA . ASN B 2 135 ? 46.654 -16.144 -72.152 1.00 58.90 ? 135 ASN B CA 1 ATOM 3629 C C . ASN B 2 135 ? 45.357 -16.665 -71.531 1.00 55.17 ? 135 ASN B C 1 ATOM 3630 O O . ASN B 2 135 ? 44.640 -15.928 -70.849 1.00 54.17 ? 135 ASN B O 1 ATOM 3631 C CB . ASN B 2 135 ? 46.423 -14.760 -72.748 1.00 61.75 ? 135 ASN B CB 1 ATOM 3632 C CG . ASN B 2 135 ? 45.383 -14.769 -73.849 1.00 63.09 ? 135 ASN B CG 1 ATOM 3633 O OD1 . ASN B 2 135 ? 45.000 -15.827 -74.355 1.00 61.45 ? 135 ASN B OD1 1 ATOM 3634 N ND2 . ASN B 2 135 ? 44.923 -13.587 -74.232 1.00 67.44 ? 135 ASN B ND2 1 ATOM 3635 N N . GLY B 2 136 ? 45.070 -17.941 -71.767 1.00 53.19 ? 136 GLY B N 1 ATOM 3636 C CA . GLY B 2 136 ? 43.816 -18.546 -71.347 1.00 51.66 ? 136 GLY B CA 1 ATOM 3637 C C . GLY B 2 136 ? 42.821 -18.720 -72.481 1.00 50.50 ? 136 GLY B C 1 ATOM 3638 O O . GLY B 2 136 ? 41.789 -19.362 -72.300 1.00 48.40 ? 136 GLY B O 1 ATOM 3639 N N . CYS B 2 137 ? 43.128 -18.165 -73.650 1.00 52.66 ? 137 CYS B N 1 ATOM 3640 C CA . CYS B 2 137 ? 42.171 -18.153 -74.752 1.00 55.84 ? 137 CYS B CA 1 ATOM 3641 C C . CYS B 2 137 ? 42.566 -19.078 -75.888 1.00 55.79 ? 137 CYS B C 1 ATOM 3642 O O . CYS B 2 137 ? 43.743 -19.347 -76.121 1.00 55.80 ? 137 CYS B O 1 ATOM 3643 C CB . CYS B 2 137 ? 41.974 -16.741 -75.294 1.00 58.16 ? 137 CYS B CB 1 ATOM 3644 S SG . CYS B 2 137 ? 41.373 -15.570 -74.063 1.00 62.65 ? 137 CYS B SG 1 ATOM 3645 N N . PHE B 2 138 ? 41.540 -19.547 -76.586 1.00 55.72 ? 138 PHE B N 1 ATOM 3646 C CA . PHE B 2 138 ? 41.684 -20.404 -77.738 1.00 55.70 ? 138 PHE B CA 1 ATOM 3647 C C . PHE B 2 138 ? 40.995 -19.729 -78.901 1.00 58.00 ? 138 PHE B C 1 ATOM 3648 O O . PHE B 2 138 ? 39.804 -19.443 -78.826 1.00 57.57 ? 138 PHE B O 1 ATOM 3649 C CB . PHE B 2 138 ? 41.028 -21.754 -77.472 1.00 53.94 ? 138 PHE B CB 1 ATOM 3650 C CG . PHE B 2 138 ? 41.741 -22.575 -76.441 1.00 53.31 ? 138 PHE B CG 1 ATOM 3651 C CD1 . PHE B 2 138 ? 42.837 -23.352 -76.793 1.00 52.75 ? 138 PHE B CD1 1 ATOM 3652 C CD2 . PHE B 2 138 ? 41.325 -22.566 -75.116 1.00 53.01 ? 138 PHE B CD2 1 ATOM 3653 C CE1 . PHE B 2 138 ? 43.496 -24.112 -75.849 1.00 52.57 ? 138 PHE B CE1 1 ATOM 3654 C CE2 . PHE B 2 138 ? 41.987 -23.326 -74.165 1.00 51.77 ? 138 PHE B CE2 1 ATOM 3655 C CZ . PHE B 2 138 ? 43.078 -24.091 -74.532 1.00 52.12 ? 138 PHE B CZ 1 ATOM 3656 N N . GLU B 2 139 ? 41.746 -19.477 -79.968 1.00 61.21 ? 139 GLU B N 1 ATOM 3657 C CA . GLU B 2 139 ? 41.207 -18.868 -81.172 1.00 63.14 ? 139 GLU B CA 1 ATOM 3658 C C . GLU B 2 139 ? 40.912 -19.957 -82.196 1.00 63.04 ? 139 GLU B C 1 ATOM 3659 O O . GLU B 2 139 ? 41.811 -20.692 -82.616 1.00 64.08 ? 139 GLU B O 1 ATOM 3660 C CB . GLU B 2 139 ? 42.203 -17.863 -81.731 1.00 67.78 ? 139 GLU B CB 1 ATOM 3661 C CG . GLU B 2 139 ? 41.675 -17.029 -82.885 1.00 72.55 ? 139 GLU B CG 1 ATOM 3662 C CD . GLU B 2 139 ? 42.742 -16.107 -83.432 1.00 79.69 ? 139 GLU B CD 1 ATOM 3663 O OE1 . GLU B 2 139 ? 43.206 -15.215 -82.683 1.00 84.04 ? 139 GLU B OE1 1 ATOM 3664 O OE2 . GLU B 2 139 ? 43.131 -16.287 -84.605 1.00 86.33 ? 139 GLU B OE2 1 ATOM 3665 N N . PHE B 2 140 ? 39.649 -20.054 -82.598 1.00 63.10 ? 140 PHE B N 1 ATOM 3666 C CA . PHE B 2 140 ? 39.196 -21.110 -83.498 1.00 63.66 ? 140 PHE B CA 1 ATOM 3667 C C . PHE B 2 140 ? 39.615 -20.887 -84.951 1.00 66.04 ? 140 PHE B C 1 ATOM 3668 O O . PHE B 2 140 ? 39.701 -19.749 -85.414 1.00 64.34 ? 140 PHE B O 1 ATOM 3669 C CB . PHE B 2 140 ? 37.677 -21.221 -83.441 1.00 62.17 ? 140 PHE B CB 1 ATOM 3670 C CG . PHE B 2 140 ? 37.163 -21.761 -82.152 1.00 60.92 ? 140 PHE B CG 1 ATOM 3671 C CD1 . PHE B 2 140 ? 36.999 -23.128 -81.978 1.00 61.46 ? 140 PHE B CD1 1 ATOM 3672 C CD2 . PHE B 2 140 ? 36.837 -20.911 -81.111 1.00 60.14 ? 140 PHE B CD2 1 ATOM 3673 C CE1 . PHE B 2 140 ? 36.514 -23.638 -80.789 1.00 61.33 ? 140 PHE B CE1 1 ATOM 3674 C CE2 . PHE B 2 140 ? 36.346 -21.411 -79.921 1.00 59.78 ? 140 PHE B CE2 1 ATOM 3675 C CZ . PHE B 2 140 ? 36.188 -22.778 -79.759 1.00 60.84 ? 140 PHE B CZ 1 ATOM 3676 N N . TYR B 2 141 ? 39.864 -21.985 -85.664 1.00 68.48 ? 141 TYR B N 1 ATOM 3677 C CA . TYR B 2 141 ? 40.136 -21.923 -87.106 1.00 72.14 ? 141 TYR B CA 1 ATOM 3678 C C . TYR B 2 141 ? 38.847 -21.829 -87.893 1.00 70.67 ? 141 TYR B C 1 ATOM 3679 O O . TYR B 2 141 ? 38.788 -21.148 -88.907 1.00 75.77 ? 141 TYR B O 1 ATOM 3680 C CB . TYR B 2 141 ? 40.924 -23.143 -87.575 1.00 74.39 ? 141 TYR B CB 1 ATOM 3681 C CG . TYR B 2 141 ? 42.310 -23.202 -87.005 1.00 75.60 ? 141 TYR B CG 1 ATOM 3682 C CD1 . TYR B 2 141 ? 43.182 -22.124 -87.139 1.00 78.15 ? 141 TYR B CD1 1 ATOM 3683 C CD2 . TYR B 2 141 ? 42.748 -24.321 -86.319 1.00 77.05 ? 141 TYR B CD2 1 ATOM 3684 C CE1 . TYR B 2 141 ? 44.455 -22.167 -86.612 1.00 81.04 ? 141 TYR B CE1 1 ATOM 3685 C CE2 . TYR B 2 141 ? 44.022 -24.373 -85.786 1.00 80.56 ? 141 TYR B CE2 1 ATOM 3686 C CZ . TYR B 2 141 ? 44.870 -23.298 -85.940 1.00 82.03 ? 141 TYR B CZ 1 ATOM 3687 O OH . TYR B 2 141 ? 46.134 -23.360 -85.410 1.00 86.96 ? 141 TYR B OH 1 ATOM 3688 N N . HIS B 2 142 ? 37.826 -22.532 -87.418 1.00 93.55 ? 142 HIS B N 1 ATOM 3689 C CA . HIS B 2 142 ? 36.492 -22.452 -87.987 1.00 94.07 ? 142 HIS B CA 1 ATOM 3690 C C . HIS B 2 142 ? 35.669 -21.405 -87.248 1.00 89.57 ? 142 HIS B C 1 ATOM 3691 O O . HIS B 2 142 ? 36.075 -20.900 -86.205 1.00 86.31 ? 142 HIS B O 1 ATOM 3692 C CB . HIS B 2 142 ? 35.803 -23.820 -87.923 1.00 96.42 ? 142 HIS B CB 1 ATOM 3693 C CG . HIS B 2 142 ? 35.662 -24.367 -86.537 1.00 93.15 ? 142 HIS B CG 1 ATOM 3694 N ND1 . HIS B 2 142 ? 34.504 -24.236 -85.800 1.00 92.10 ? 142 HIS B ND1 1 ATOM 3695 C CD2 . HIS B 2 142 ? 36.534 -25.042 -85.751 1.00 91.74 ? 142 HIS B CD2 1 ATOM 3696 C CE1 . HIS B 2 142 ? 34.670 -24.810 -84.622 1.00 89.35 ? 142 HIS B CE1 1 ATOM 3697 N NE2 . HIS B 2 142 ? 35.893 -25.306 -84.567 1.00 89.07 ? 142 HIS B NE2 1 ATOM 3698 N N . LYS B 2 143 ? 34.510 -21.076 -87.797 1.00 91.49 ? 143 LYS B N 1 ATOM 3699 C CA . LYS B 2 143 ? 33.605 -20.141 -87.147 1.00 89.24 ? 143 LYS B CA 1 ATOM 3700 C C . LYS B 2 143 ? 32.840 -20.925 -86.083 1.00 85.87 ? 143 LYS B C 1 ATOM 3701 O O . LYS B 2 143 ? 32.348 -22.020 -86.356 1.00 87.12 ? 143 LYS B O 1 ATOM 3702 C CB . LYS B 2 143 ? 32.653 -19.510 -88.166 1.00 94.27 ? 143 LYS B CB 1 ATOM 3703 C CG . LYS B 2 143 ? 32.504 -18.004 -88.017 1.00 95.15 ? 143 LYS B CG 1 ATOM 3704 C CD . LYS B 2 143 ? 31.772 -17.392 -89.202 1.00 101.21 ? 143 LYS B CD 1 ATOM 3705 C CE . LYS B 2 143 ? 30.265 -17.604 -89.116 1.00 104.51 ? 143 LYS B CE 1 ATOM 3706 N NZ . LYS B 2 143 ? 29.615 -16.790 -88.047 1.00 102.01 ? 143 LYS B NZ 1 ATOM 3707 N N . CYS B 2 144 ? 32.760 -20.373 -84.873 1.00 81.27 ? 144 CYS B N 1 ATOM 3708 C CA . CYS B 2 144 ? 32.176 -21.084 -83.738 1.00 78.77 ? 144 CYS B CA 1 ATOM 3709 C C . CYS B 2 144 ? 31.006 -20.294 -83.162 1.00 77.91 ? 144 CYS B C 1 ATOM 3710 O O . CYS B 2 144 ? 31.192 -19.394 -82.343 1.00 76.27 ? 144 CYS B O 1 ATOM 3711 C CB . CYS B 2 144 ? 33.250 -21.347 -82.669 1.00 75.67 ? 144 CYS B CB 1 ATOM 3712 S SG . CYS B 2 144 ? 32.788 -22.522 -81.365 1.00 74.97 ? 144 CYS B SG 1 ATOM 3713 N N . ASP B 2 145 ? 29.799 -20.638 -83.606 1.00 81.25 ? 145 ASP B N 1 ATOM 3714 C CA . ASP B 2 145 ? 28.567 -19.985 -83.141 1.00 82.37 ? 145 ASP B CA 1 ATOM 3715 C C . ASP B 2 145 ? 28.226 -20.432 -81.710 1.00 79.68 ? 145 ASP B C 1 ATOM 3716 O O . ASP B 2 145 ? 28.981 -21.191 -81.104 1.00 76.96 ? 145 ASP B O 1 ATOM 3717 C CB . ASP B 2 145 ? 27.402 -20.257 -84.115 1.00 86.83 ? 145 ASP B CB 1 ATOM 3718 C CG . ASP B 2 145 ? 27.034 -21.732 -84.211 1.00 89.71 ? 145 ASP B CG 1 ATOM 3719 O OD1 . ASP B 2 145 ? 27.726 -22.573 -83.611 1.00 87.97 ? 145 ASP B OD1 1 ATOM 3720 O OD2 . ASP B 2 145 ? 26.049 -22.059 -84.901 1.00 96.58 ? 145 ASP B OD2 1 ATOM 3721 N N . ASN B 2 146 ? 27.095 -19.972 -81.176 1.00 80.87 ? 146 ASN B N 1 ATOM 3722 C CA . ASN B 2 146 ? 26.751 -20.230 -79.773 1.00 79.47 ? 146 ASN B CA 1 ATOM 3723 C C . ASN B 2 146 ? 26.516 -21.705 -79.443 1.00 82.37 ? 146 ASN B C 1 ATOM 3724 O O . ASN B 2 146 ? 26.897 -22.168 -78.363 1.00 80.95 ? 146 ASN B O 1 ATOM 3725 C CB . ASN B 2 146 ? 25.560 -19.371 -79.340 1.00 80.73 ? 146 ASN B CB 1 ATOM 3726 C CG . ASN B 2 146 ? 25.861 -17.879 -79.398 1.00 79.51 ? 146 ASN B CG 1 ATOM 3727 O OD1 . ASN B 2 146 ? 27.016 -17.457 -79.413 1.00 76.49 ? 146 ASN B OD1 1 ATOM 3728 N ND2 . ASN B 2 146 ? 24.817 -17.074 -79.437 1.00 83.65 ? 146 ASN B ND2 1 ATOM 3729 N N . GLU B 2 147 ? 25.924 -22.449 -80.372 1.00 88.48 ? 147 GLU B N 1 ATOM 3730 C CA . GLU B 2 147 ? 25.802 -23.908 -80.220 1.00 92.69 ? 147 GLU B CA 1 ATOM 3731 C C . GLU B 2 147 ? 27.184 -24.572 -80.196 1.00 87.68 ? 147 GLU B C 1 ATOM 3732 O O . GLU B 2 147 ? 27.429 -25.485 -79.407 1.00 87.89 ? 147 GLU B O 1 ATOM 3733 C CB . GLU B 2 147 ? 24.961 -24.528 -81.345 1.00 100.67 ? 147 GLU B CB 1 ATOM 3734 C CG . GLU B 2 147 ? 23.499 -24.101 -81.361 1.00 107.46 ? 147 GLU B CG 1 ATOM 3735 C CD . GLU B 2 147 ? 23.249 -22.877 -82.228 1.00 109.52 ? 147 GLU B CD 1 ATOM 3736 O OE1 . GLU B 2 147 ? 23.995 -21.880 -82.090 1.00 104.69 ? 147 GLU B OE1 1 ATOM 3737 O OE2 . GLU B 2 147 ? 22.304 -22.913 -83.049 1.00 116.57 ? 147 GLU B OE2 1 ATOM 3738 N N . CYS B 2 148 ? 28.071 -24.114 -81.076 1.00 84.83 ? 148 CYS B N 1 ATOM 3739 C CA . CYS B 2 148 ? 29.459 -24.577 -81.110 1.00 81.53 ? 148 CYS B CA 1 ATOM 3740 C C . CYS B 2 148 ? 30.120 -24.313 -79.744 1.00 75.13 ? 148 CYS B C 1 ATOM 3741 O O . CYS B 2 148 ? 30.619 -25.236 -79.092 1.00 72.46 ? 148 CYS B O 1 ATOM 3742 C CB . CYS B 2 148 ? 30.199 -23.873 -82.260 1.00 82.29 ? 148 CYS B CB 1 ATOM 3743 S SG . CYS B 2 148 ? 31.986 -24.119 -82.369 1.00 83.38 ? 148 CYS B SG 1 ATOM 3744 N N . MET B 2 149 ? 30.067 -23.057 -79.301 1.00 71.63 ? 149 MET B N 1 ATOM 3745 C CA . MET B 2 149 ? 30.576 -22.663 -77.984 1.00 67.41 ? 149 MET B CA 1 ATOM 3746 C C . MET B 2 149 ? 30.006 -23.520 -76.866 1.00 68.30 ? 149 MET B C 1 ATOM 3747 O O . MET B 2 149 ? 30.736 -23.932 -75.967 1.00 65.99 ? 149 MET B O 1 ATOM 3748 C CB . MET B 2 149 ? 30.239 -21.200 -77.692 1.00 66.57 ? 149 MET B CB 1 ATOM 3749 C CG . MET B 2 149 ? 30.945 -20.190 -78.579 1.00 65.55 ? 149 MET B CG 1 ATOM 3750 S SD . MET B 2 149 ? 32.732 -20.344 -78.498 1.00 62.84 ? 149 MET B SD 1 ATOM 3751 C CE . MET B 2 149 ? 33.225 -18.972 -79.543 1.00 63.82 ? 149 MET B CE 1 ATOM 3752 N N . GLU B 2 150 ? 28.702 -23.781 -76.920 1.00 72.93 ? 150 GLU B N 1 ATOM 3753 C CA . GLU B 2 150 ? 28.042 -24.588 -75.899 1.00 76.09 ? 150 GLU B CA 1 ATOM 3754 C C . GLU B 2 150 ? 28.611 -26.004 -75.825 1.00 77.19 ? 150 GLU B C 1 ATOM 3755 O O . GLU B 2 150 ? 28.720 -26.564 -74.736 1.00 77.15 ? 150 GLU B O 1 ATOM 3756 C CB . GLU B 2 150 ? 26.527 -24.633 -76.137 1.00 82.92 ? 150 GLU B CB 1 ATOM 3757 C CG . GLU B 2 150 ? 25.724 -25.310 -75.030 1.00 87.90 ? 150 GLU B CG 1 ATOM 3758 C CD . GLU B 2 150 ? 25.916 -24.654 -73.670 1.00 87.37 ? 150 GLU B CD 1 ATOM 3759 O OE1 . GLU B 2 150 ? 25.775 -23.418 -73.583 1.00 88.25 ? 150 GLU B OE1 1 ATOM 3760 O OE2 . GLU B 2 150 ? 26.220 -25.364 -72.687 1.00 87.95 ? 150 GLU B OE2 1 ATOM 3761 N N . SER B 2 151 ? 28.979 -26.578 -76.968 1.00 78.76 ? 151 SER B N 1 ATOM 3762 C CA . SER B 2 151 ? 29.514 -27.941 -76.990 1.00 81.70 ? 151 SER B CA 1 ATOM 3763 C C . SER B 2 151 ? 30.915 -28.008 -76.372 1.00 78.50 ? 151 SER B C 1 ATOM 3764 O O . SER B 2 151 ? 31.328 -29.061 -75.872 1.00 80.33 ? 151 SER B O 1 ATOM 3765 C CB . SER B 2 151 ? 29.528 -28.507 -78.414 1.00 85.79 ? 151 SER B CB 1 ATOM 3766 O OG . SER B 2 151 ? 30.539 -27.909 -79.203 1.00 83.90 ? 151 SER B OG 1 ATOM 3767 N N . VAL B 2 152 ? 31.642 -26.890 -76.407 1.00 74.42 ? 152 VAL B N 1 ATOM 3768 C CA . VAL B 2 152 ? 32.938 -26.798 -75.730 1.00 70.80 ? 152 VAL B CA 1 ATOM 3769 C C . VAL B 2 152 ? 32.731 -26.826 -74.216 1.00 70.74 ? 152 VAL B C 1 ATOM 3770 O O . VAL B 2 152 ? 33.463 -27.504 -73.505 1.00 69.01 ? 152 VAL B O 1 ATOM 3771 C CB . VAL B 2 152 ? 33.719 -25.526 -76.113 1.00 67.05 ? 152 VAL B CB 1 ATOM 3772 C CG1 . VAL B 2 152 ? 35.057 -25.489 -75.385 1.00 64.91 ? 152 VAL B CG1 1 ATOM 3773 C CG2 . VAL B 2 152 ? 33.933 -25.465 -77.616 1.00 68.60 ? 152 VAL B CG2 1 ATOM 3774 N N . ARG B 2 153 ? 31.726 -26.099 -73.734 1.00 72.75 ? 153 ARG B N 1 ATOM 3775 C CA . ARG B 2 153 ? 31.387 -26.112 -72.312 1.00 75.58 ? 153 ARG B CA 1 ATOM 3776 C C . ARG B 2 153 ? 30.782 -27.446 -71.896 1.00 82.47 ? 153 ARG B C 1 ATOM 3777 O O . ARG B 2 153 ? 31.022 -27.908 -70.785 1.00 83.06 ? 153 ARG B O 1 ATOM 3778 C CB . ARG B 2 153 ? 30.414 -24.986 -71.970 1.00 75.58 ? 153 ARG B CB 1 ATOM 3779 C CG . ARG B 2 153 ? 30.929 -23.597 -72.293 1.00 71.84 ? 153 ARG B CG 1 ATOM 3780 C CD . ARG B 2 153 ? 30.025 -22.525 -71.713 1.00 73.57 ? 153 ARG B CD 1 ATOM 3781 N NE . ARG B 2 153 ? 30.003 -21.363 -72.595 1.00 73.72 ? 153 ARG B NE 1 ATOM 3782 C CZ . ARG B 2 153 ? 29.107 -21.152 -73.557 1.00 75.10 ? 153 ARG B CZ 1 ATOM 3783 N NH1 . ARG B 2 153 ? 28.111 -22.007 -73.764 1.00 77.35 ? 153 ARG B NH1 1 ATOM 3784 N NH2 . ARG B 2 153 ? 29.203 -20.063 -74.314 1.00 75.56 ? 153 ARG B NH2 1 ATOM 3785 N N . ASN B 2 154 ? 29.985 -28.041 -72.786 1.00 91.55 ? 154 ASN B N 1 ATOM 3786 C CA . ASN B 2 154 ? 29.426 -29.386 -72.587 1.00 100.46 ? 154 ASN B CA 1 ATOM 3787 C C . ASN B 2 154 ? 30.475 -30.433 -72.257 1.00 98.72 ? 154 ASN B C 1 ATOM 3788 O O . ASN B 2 154 ? 30.313 -31.216 -71.324 1.00 103.80 ? 154 ASN B O 1 ATOM 3789 C CB . ASN B 2 154 ? 28.725 -29.873 -73.859 1.00 110.05 ? 154 ASN B CB 1 ATOM 3790 C CG . ASN B 2 154 ? 27.333 -29.319 -74.017 1.00 121.45 ? 154 ASN B CG 1 ATOM 3791 O OD1 . ASN B 2 154 ? 26.928 -28.405 -73.299 1.00 123.68 ? 154 ASN B OD1 1 ATOM 3792 N ND2 . ASN B 2 154 ? 26.585 -29.877 -74.971 1.00 136.14 ? 154 ASN B ND2 1 ATOM 3793 N N . GLY B 2 155 ? 31.544 -30.441 -73.044 1.00 92.62 ? 155 GLY B N 1 ATOM 3794 C CA . GLY B 2 155 ? 32.464 -31.564 -73.087 1.00 91.17 ? 155 GLY B CA 1 ATOM 3795 C C . GLY B 2 155 ? 32.247 -32.376 -74.351 1.00 93.04 ? 155 GLY B C 1 ATOM 3796 O O . GLY B 2 155 ? 32.922 -33.380 -74.567 1.00 95.32 ? 155 GLY B O 1 ATOM 3797 N N . THR B 2 156 ? 31.321 -31.923 -75.196 1.00 92.37 ? 156 THR B N 1 ATOM 3798 C CA . THR B 2 156 ? 30.890 -32.673 -76.372 1.00 96.46 ? 156 THR B CA 1 ATOM 3799 C C . THR B 2 156 ? 31.275 -31.976 -77.673 1.00 93.96 ? 156 THR B C 1 ATOM 3800 O O . THR B 2 156 ? 30.586 -32.119 -78.680 1.00 97.87 ? 156 THR B O 1 ATOM 3801 C CB . THR B 2 156 ? 29.359 -32.863 -76.368 1.00 101.62 ? 156 THR B CB 1 ATOM 3802 O OG1 . THR B 2 156 ? 28.714 -31.588 -76.479 1.00 99.05 ? 156 THR B OG1 1 ATOM 3803 C CG2 . THR B 2 156 ? 28.897 -33.560 -75.091 1.00 104.56 ? 156 THR B CG2 1 ATOM 3804 N N . TYR B 2 157 ? 32.372 -31.224 -77.657 1.00 89.25 ? 157 TYR B N 1 ATOM 3805 C CA . TYR B 2 157 ? 32.856 -30.560 -78.868 1.00 88.74 ? 157 TYR B CA 1 ATOM 3806 C C . TYR B 2 157 ? 33.327 -31.609 -79.867 1.00 93.95 ? 157 TYR B C 1 ATOM 3807 O O . TYR B 2 157 ? 34.319 -32.301 -79.633 1.00 93.34 ? 157 TYR B O 1 ATOM 3808 C CB . TYR B 2 157 ? 33.993 -29.583 -78.552 1.00 82.64 ? 157 TYR B CB 1 ATOM 3809 C CG . TYR B 2 157 ? 34.655 -28.999 -79.784 1.00 81.54 ? 157 TYR B CG 1 ATOM 3810 C CD1 . TYR B 2 157 ? 34.041 -27.986 -80.518 1.00 81.84 ? 157 TYR B CD1 1 ATOM 3811 C CD2 . TYR B 2 157 ? 35.889 -29.463 -80.218 1.00 81.60 ? 157 TYR B CD2 1 ATOM 3812 C CE1 . TYR B 2 157 ? 34.643 -27.452 -81.649 1.00 81.68 ? 157 TYR B CE1 1 ATOM 3813 C CE2 . TYR B 2 157 ? 36.497 -28.935 -81.345 1.00 82.20 ? 157 TYR B CE2 1 ATOM 3814 C CZ . TYR B 2 157 ? 35.873 -27.932 -82.056 1.00 81.29 ? 157 TYR B CZ 1 ATOM 3815 O OH . TYR B 2 157 ? 36.488 -27.414 -83.170 1.00 80.98 ? 157 TYR B OH 1 ATOM 3816 N N . ASP B 2 158 ? 32.607 -31.720 -80.978 1.00 101.01 ? 158 ASP B N 1 ATOM 3817 C CA . ASP B 2 158 ? 32.863 -32.771 -81.957 1.00 108.82 ? 158 ASP B CA 1 ATOM 3818 C C . ASP B 2 158 ? 34.045 -32.385 -82.850 1.00 108.81 ? 158 ASP B C 1 ATOM 3819 O O . ASP B 2 158 ? 33.882 -31.728 -83.882 1.00 109.90 ? 158 ASP B O 1 ATOM 3820 C CB . ASP B 2 158 ? 31.599 -33.052 -82.781 1.00 115.57 ? 158 ASP B CB 1 ATOM 3821 C CG . ASP B 2 158 ? 31.612 -34.423 -83.431 1.00 123.85 ? 158 ASP B CG 1 ATOM 3822 O OD1 . ASP B 2 158 ? 32.429 -35.281 -83.035 1.00 124.77 ? 158 ASP B OD1 1 ATOM 3823 O OD2 . ASP B 2 158 ? 30.792 -34.649 -84.340 1.00 131.50 ? 158 ASP B OD2 1 ATOM 3824 N N . TYR B 2 159 ? 35.239 -32.792 -82.424 1.00 108.61 ? 159 TYR B N 1 ATOM 3825 C CA . TYR B 2 159 ? 36.482 -32.495 -83.138 1.00 109.01 ? 159 TYR B CA 1 ATOM 3826 C C . TYR B 2 159 ? 36.487 -33.030 -84.586 1.00 117.85 ? 159 TYR B C 1 ATOM 3827 O O . TYR B 2 159 ? 36.909 -32.319 -85.504 1.00 118.90 ? 159 TYR B O 1 ATOM 3828 C CB . TYR B 2 159 ? 37.683 -33.018 -82.333 1.00 106.77 ? 159 TYR B CB 1 ATOM 3829 C CG . TYR B 2 159 ? 38.998 -33.024 -83.077 1.00 108.28 ? 159 TYR B CG 1 ATOM 3830 C CD1 . TYR B 2 159 ? 39.349 -34.093 -83.901 1.00 114.41 ? 159 TYR B CD1 1 ATOM 3831 C CD2 . TYR B 2 159 ? 39.899 -31.972 -82.943 1.00 104.04 ? 159 TYR B CD2 1 ATOM 3832 C CE1 . TYR B 2 159 ? 40.553 -34.106 -84.581 1.00 116.26 ? 159 TYR B CE1 1 ATOM 3833 C CE2 . TYR B 2 159 ? 41.106 -31.976 -83.619 1.00 106.35 ? 159 TYR B CE2 1 ATOM 3834 C CZ . TYR B 2 159 ? 41.428 -33.046 -84.437 1.00 112.33 ? 159 TYR B CZ 1 ATOM 3835 O OH . TYR B 2 159 ? 42.625 -33.064 -85.111 1.00 115.64 ? 159 TYR B OH 1 ATOM 3836 N N . PRO B 2 160 ? 36.020 -34.278 -84.798 1.00 125.77 ? 160 PRO B N 1 ATOM 3837 C CA . PRO B 2 160 ? 35.890 -34.761 -86.183 1.00 134.54 ? 160 PRO B CA 1 ATOM 3838 C C . PRO B 2 160 ? 34.954 -33.924 -87.073 1.00 135.61 ? 160 PRO B C 1 ATOM 3839 O O . PRO B 2 160 ? 35.107 -33.939 -88.296 1.00 140.14 ? 160 PRO B O 1 ATOM 3840 C CB . PRO B 2 160 ? 35.339 -36.183 -86.011 1.00 141.41 ? 160 PRO B CB 1 ATOM 3841 C CG . PRO B 2 160 ? 35.796 -36.605 -84.658 1.00 137.40 ? 160 PRO B CG 1 ATOM 3842 C CD . PRO B 2 160 ? 35.794 -35.359 -83.819 1.00 127.83 ? 160 PRO B CD 1 ATOM 3843 N N . GLN B 2 161 ? 34.002 -33.211 -86.470 1.00 131.85 ? 161 GLN B N 1 ATOM 3844 C CA . GLN B 2 161 ? 33.077 -32.357 -87.225 1.00 133.20 ? 161 GLN B CA 1 ATOM 3845 C C . GLN B 2 161 ? 33.775 -31.125 -87.801 1.00 128.03 ? 161 GLN B C 1 ATOM 3846 O O . GLN B 2 161 ? 33.375 -30.616 -88.849 1.00 132.29 ? 161 GLN B O 1 ATOM 3847 C CB . GLN B 2 161 ? 31.900 -31.918 -86.348 1.00 130.94 ? 161 GLN B CB 1 ATOM 3848 C CG . GLN B 2 161 ? 30.725 -31.341 -87.127 1.00 134.46 ? 161 GLN B CG 1 ATOM 3849 C CD . GLN B 2 161 ? 29.531 -31.020 -86.245 1.00 133.13 ? 161 GLN B CD 1 ATOM 3850 O OE1 . GLN B 2 161 ? 29.608 -31.097 -85.018 1.00 128.22 ? 161 GLN B OE1 1 ATOM 3851 N NE2 . GLN B 2 161 ? 28.416 -30.658 -86.869 1.00 137.92 ? 161 GLN B NE2 1 ATOM 3852 N N . TYR B 2 162 ? 34.807 -30.649 -87.110 1.00 119.56 ? 162 TYR B N 1 ATOM 3853 C CA . TYR B 2 162 ? 35.584 -29.510 -87.572 1.00 115.24 ? 162 TYR B CA 1 ATOM 3854 C C . TYR B 2 162 ? 37.023 -29.946 -87.816 1.00 113.80 ? 162 TYR B C 1 ATOM 3855 O O . TYR B 2 162 ? 37.704 -29.413 -88.688 1.00 112.81 ? 162 TYR B O 1 ATOM 3856 C CB . TYR B 2 162 ? 35.537 -28.381 -86.539 1.00 109.16 ? 162 TYR B CB 1 ATOM 3857 C CG . TYR B 2 162 ? 34.135 -27.936 -86.146 1.00 109.11 ? 162 TYR B CG 1 ATOM 3858 C CD1 . TYR B 2 162 ? 33.360 -27.150 -87.000 1.00 112.01 ? 162 TYR B CD1 1 ATOM 3859 C CD2 . TYR B 2 162 ? 33.590 -28.293 -84.914 1.00 106.28 ? 162 TYR B CD2 1 ATOM 3860 C CE1 . TYR B 2 162 ? 32.083 -26.738 -86.638 1.00 111.62 ? 162 TYR B CE1 1 ATOM 3861 C CE2 . TYR B 2 162 ? 32.315 -27.887 -84.544 1.00 105.82 ? 162 TYR B CE2 1 ATOM 3862 C CZ . TYR B 2 162 ? 31.565 -27.109 -85.404 1.00 108.40 ? 162 TYR B CZ 1 ATOM 3863 O OH . TYR B 2 162 ? 30.301 -26.706 -85.029 1.00 107.83 ? 162 TYR B OH 1 HETATM 3864 C C1 . NAG C 3 . ? 30.944 -4.054 -54.113 1.00 110.34 ? 1322 NAG A C1 1 HETATM 3865 C C2 . NAG C 3 . ? 30.168 -2.828 -53.620 1.00 120.04 ? 1322 NAG A C2 1 HETATM 3866 C C3 . NAG C 3 . ? 28.799 -3.164 -53.026 1.00 124.77 ? 1322 NAG A C3 1 HETATM 3867 C C4 . NAG C 3 . ? 28.029 -4.149 -53.897 1.00 127.93 ? 1322 NAG A C4 1 HETATM 3868 C C5 . NAG C 3 . ? 28.921 -5.329 -54.279 1.00 125.94 ? 1322 NAG A C5 1 HETATM 3869 C C6 . NAG C 3 . ? 28.200 -6.303 -55.213 1.00 124.88 ? 1322 NAG A C6 1 HETATM 3870 C C7 . NAG C 3 . ? 31.575 -0.935 -52.965 1.00 120.00 ? 1322 NAG A C7 1 HETATM 3871 C C8 . NAG C 3 . ? 32.356 -0.258 -51.876 1.00 118.51 ? 1322 NAG A C8 1 HETATM 3872 N N2 . NAG C 3 . ? 30.958 -2.079 -52.654 1.00 119.15 ? 1322 NAG A N2 1 HETATM 3873 O O3 . NAG C 3 . ? 28.036 -1.984 -52.902 1.00 125.85 ? 1322 NAG A O3 1 HETATM 3874 O O4 . NAG C 3 . ? 26.880 -4.586 -53.198 1.00 130.56 ? 1322 NAG A O4 1 HETATM 3875 O O5 . NAG C 3 . ? 30.095 -4.855 -54.918 1.00 120.76 ? 1322 NAG A O5 1 HETATM 3876 O O6 . NAG C 3 . ? 28.327 -7.619 -54.723 1.00 127.18 ? 1322 NAG A O6 1 HETATM 3877 O O7 . NAG C 3 . ? 31.530 -0.424 -54.084 1.00 121.48 ? 1322 NAG A O7 1 HETATM 3878 C C1 . NAG D 3 . ? 49.718 -6.414 -43.434 1.00 76.35 ? 1323 NAG A C1 1 HETATM 3879 C C2 . NAG D 3 . ? 51.018 -5.751 -42.998 1.00 84.37 ? 1323 NAG A C2 1 HETATM 3880 C C3 . NAG D 3 . ? 50.917 -5.019 -41.654 1.00 88.37 ? 1323 NAG A C3 1 HETATM 3881 C C4 . NAG D 3 . ? 49.580 -4.322 -41.422 1.00 90.42 ? 1323 NAG A C4 1 HETATM 3882 C C5 . NAG D 3 . ? 48.453 -5.262 -41.819 1.00 89.24 ? 1323 NAG A C5 1 HETATM 3883 C C6 . NAG D 3 . ? 47.051 -4.696 -41.583 1.00 88.82 ? 1323 NAG A C6 1 HETATM 3884 C C7 . NAG D 3 . ? 53.013 -6.955 -43.801 1.00 88.84 ? 1323 NAG A C7 1 HETATM 3885 C C8 . NAG D 3 . ? 53.989 -8.072 -43.543 1.00 86.53 ? 1323 NAG A C8 1 HETATM 3886 N N2 . NAG D 3 . ? 52.039 -6.783 -42.899 1.00 88.36 ? 1323 NAG A N2 1 HETATM 3887 O O3 . NAG D 3 . ? 51.947 -4.063 -41.587 1.00 91.73 ? 1323 NAG A O3 1 HETATM 3888 O O4 . NAG D 3 . ? 49.439 -3.993 -40.055 1.00 102.95 ? 1323 NAG A O4 1 HETATM 3889 O O5 . NAG D 3 . ? 48.629 -5.552 -43.185 1.00 80.34 ? 1323 NAG A O5 1 HETATM 3890 O O6 . NAG D 3 . ? 46.996 -3.334 -41.936 1.00 91.53 ? 1323 NAG A O6 1 HETATM 3891 O O7 . NAG D 3 . ? 53.142 -6.255 -44.808 1.00 88.19 ? 1323 NAG A O7 1 HETATM 3892 C C1 . NAG E 3 . ? 49.791 -2.622 -39.766 1.00 116.70 ? 1324 NAG A C1 1 HETATM 3893 C C2 . NAG E 3 . ? 49.062 -2.181 -38.493 1.00 119.22 ? 1324 NAG A C2 1 HETATM 3894 C C3 . NAG E 3 . ? 49.562 -0.838 -37.960 1.00 121.77 ? 1324 NAG A C3 1 HETATM 3895 C C4 . NAG E 3 . ? 51.084 -0.737 -37.999 1.00 123.46 ? 1324 NAG A C4 1 HETATM 3896 C C5 . NAG E 3 . ? 51.591 -1.139 -39.382 1.00 124.00 ? 1324 NAG A C5 1 HETATM 3897 C C6 . NAG E 3 . ? 53.111 -1.049 -39.499 1.00 124.66 ? 1324 NAG A C6 1 HETATM 3898 C C7 . NAG E 3 . ? 46.771 -3.060 -38.419 1.00 117.34 ? 1324 NAG A C7 1 HETATM 3899 C C8 . NAG E 3 . ? 45.324 -2.842 -38.770 1.00 113.42 ? 1324 NAG A C8 1 HETATM 3900 N N2 . NAG E 3 . ? 47.632 -2.099 -38.762 1.00 119.65 ? 1324 NAG A N2 1 HETATM 3901 O O3 . NAG E 3 . ? 49.114 -0.655 -36.635 1.00 119.74 ? 1324 NAG A O3 1 HETATM 3902 O O4 . NAG E 3 . ? 51.465 0.584 -37.686 1.00 125.09 ? 1324 NAG A O4 1 HETATM 3903 O O5 . NAG E 3 . ? 51.188 -2.471 -39.629 1.00 120.37 ? 1324 NAG A O5 1 HETATM 3904 O O6 . NAG E 3 . ? 53.716 -2.053 -38.714 1.00 124.67 ? 1324 NAG A O6 1 HETATM 3905 O O7 . NAG E 3 . ? 47.112 -4.094 -37.841 1.00 114.51 ? 1324 NAG A O7 1 HETATM 3906 C C1 . NAG F 3 . ? 22.198 -39.957 14.049 1.00 85.34 ? 1325 NAG A C1 1 HETATM 3907 C C2 . NAG F 3 . ? 23.006 -41.196 14.422 1.00 91.38 ? 1325 NAG A C2 1 HETATM 3908 C C3 . NAG F 3 . ? 22.539 -42.382 13.581 1.00 97.74 ? 1325 NAG A C3 1 HETATM 3909 C C4 . NAG F 3 . ? 21.040 -42.601 13.765 1.00 103.70 ? 1325 NAG A C4 1 HETATM 3910 C C5 . NAG F 3 . ? 20.279 -41.298 13.529 1.00 100.11 ? 1325 NAG A C5 1 HETATM 3911 C C6 . NAG F 3 . ? 18.782 -41.488 13.821 1.00 102.80 ? 1325 NAG A C6 1 HETATM 3912 C C7 . NAG F 3 . ? 25.361 -41.218 15.153 1.00 97.11 ? 1325 NAG A C7 1 HETATM 3913 C C8 . NAG F 3 . ? 26.795 -40.953 14.772 1.00 96.34 ? 1325 NAG A C8 1 HETATM 3914 N N2 . NAG F 3 . ? 24.429 -40.983 14.218 1.00 94.96 ? 1325 NAG A N2 1 HETATM 3915 O O3 . NAG F 3 . ? 23.256 -43.552 13.917 1.00 97.99 ? 1325 NAG A O3 1 HETATM 3916 O O4 . NAG F 3 . ? 20.560 -43.524 12.812 1.00 116.43 ? 1325 NAG A O4 1 HETATM 3917 O O5 . NAG F 3 . ? 20.836 -40.254 14.305 1.00 91.37 ? 1325 NAG A O5 1 HETATM 3918 O O6 . NAG F 3 . ? 18.161 -40.321 14.322 1.00 104.66 ? 1325 NAG A O6 1 HETATM 3919 O O7 . NAG F 3 . ? 25.107 -41.625 16.286 1.00 94.37 ? 1325 NAG A O7 1 HETATM 3920 C C1 . NAG G 3 . ? 20.460 -44.903 13.231 1.00 128.95 ? 1326 NAG A C1 1 HETATM 3921 C C2 . NAG G 3 . ? 19.616 -45.590 12.161 1.00 135.98 ? 1326 NAG A C2 1 HETATM 3922 C C3 . NAG G 3 . ? 18.529 -46.478 12.748 1.00 143.09 ? 1326 NAG A C3 1 HETATM 3923 C C4 . NAG G 3 . ? 19.120 -47.371 13.836 1.00 147.04 ? 1326 NAG A C4 1 HETATM 3924 C C5 . NAG G 3 . ? 19.796 -46.487 14.903 1.00 141.00 ? 1326 NAG A C5 1 HETATM 3925 C C6 . NAG G 3 . ? 21.179 -46.998 15.314 1.00 140.55 ? 1326 NAG A C6 1 HETATM 3926 C C7 . NAG G 3 . ? 19.053 -44.562 9.977 1.00 137.37 ? 1326 NAG A C7 1 HETATM 3927 C C8 . NAG G 3 . ? 19.801 -45.633 9.233 1.00 136.05 ? 1326 NAG A C8 1 HETATM 3928 N N2 . NAG G 3 . ? 18.995 -44.586 11.311 1.00 136.52 ? 1326 NAG A N2 1 HETATM 3929 O O3 . NAG G 3 . ? 17.976 -47.233 11.695 1.00 146.18 ? 1326 NAG A O3 1 HETATM 3930 O O4 . NAG G 3 . ? 18.113 -48.175 14.447 1.00 158.34 ? 1326 NAG A O4 1 HETATM 3931 O O5 . NAG G 3 . ? 19.887 -45.121 14.509 1.00 132.08 ? 1326 NAG A O5 1 HETATM 3932 O O6 . NAG G 3 . ? 21.056 -48.082 16.205 1.00 142.83 ? 1326 NAG A O6 1 HETATM 3933 O O7 . NAG G 3 . ? 18.497 -43.673 9.340 1.00 137.67 ? 1326 NAG A O7 1 HETATM 3934 C C1 . BMA H 4 . ? 17.827 -49.468 13.836 1.00 167.91 ? 1327 BMA A C1 1 HETATM 3935 C C2 . BMA H 4 . ? 18.967 -50.461 14.083 1.00 167.59 ? 1327 BMA A C2 1 HETATM 3936 C C3 . BMA H 4 . ? 18.642 -51.866 13.567 1.00 168.70 ? 1327 BMA A C3 1 HETATM 3937 C C4 . BMA H 4 . ? 17.600 -51.843 12.455 1.00 171.65 ? 1327 BMA A C4 1 HETATM 3938 C C5 . BMA H 4 . ? 17.694 -50.560 11.638 1.00 173.72 ? 1327 BMA A C5 1 HETATM 3939 C C6 . BMA H 4 . ? 16.676 -50.600 10.500 1.00 172.60 ? 1327 BMA A C6 1 HETATM 3940 O O2 . BMA H 4 . ? 19.245 -50.511 15.489 1.00 166.30 ? 1327 BMA A O2 1 HETATM 3941 O O3 . BMA H 4 . ? 18.160 -52.703 14.637 1.00 162.91 ? 1327 BMA A O3 1 HETATM 3942 O O4 . BMA H 4 . ? 17.794 -52.965 11.582 1.00 167.42 ? 1327 BMA A O4 1 HETATM 3943 O O5 . BMA H 4 . ? 17.485 -49.387 12.443 1.00 174.77 ? 1327 BMA A O5 1 HETATM 3944 O O6 . BMA H 4 . ? 17.311 -51.153 9.335 1.00 171.99 ? 1327 BMA A O6 1 HETATM 3945 C C1 . MAN I 5 . ? 18.743 -54.022 14.567 1.00 158.07 ? 1328 MAN A C1 1 HETATM 3946 C C2 . MAN I 5 . ? 20.096 -54.021 15.271 1.00 155.78 ? 1328 MAN A C2 1 HETATM 3947 C C3 . MAN I 5 . ? 20.768 -55.377 15.084 1.00 150.56 ? 1328 MAN A C3 1 HETATM 3948 C C4 . MAN I 5 . ? 19.825 -56.515 15.467 1.00 147.07 ? 1328 MAN A C4 1 HETATM 3949 C C5 . MAN I 5 . ? 18.404 -56.332 14.920 1.00 146.67 ? 1328 MAN A C5 1 HETATM 3950 C C6 . MAN I 5 . ? 17.454 -57.344 15.557 1.00 140.80 ? 1328 MAN A C6 1 HETATM 3951 O O2 . MAN I 5 . ? 19.923 -53.733 16.642 1.00 155.19 ? 1328 MAN A O2 1 HETATM 3952 O O3 . MAN I 5 . ? 21.938 -55.454 15.867 1.00 150.07 ? 1328 MAN A O3 1 HETATM 3953 O O4 . MAN I 5 . ? 20.357 -57.729 14.981 1.00 139.39 ? 1328 MAN A O4 1 HETATM 3954 O O5 . MAN I 5 . ? 17.928 -55.016 15.156 1.00 153.49 ? 1328 MAN A O5 1 HETATM 3955 O O6 . MAN I 5 . ? 16.119 -57.057 15.212 1.00 132.29 ? 1328 MAN A O6 1 HETATM 3956 C C1 . MAN J 5 . ? 16.863 -50.625 8.061 1.00 174.01 ? 1329 MAN A C1 1 HETATM 3957 C C2 . MAN J 5 . ? 17.269 -49.152 7.899 1.00 173.80 ? 1329 MAN A C2 1 HETATM 3958 C C3 . MAN J 5 . ? 16.170 -48.120 8.169 1.00 172.87 ? 1329 MAN A C3 1 HETATM 3959 C C4 . MAN J 5 . ? 14.809 -48.581 7.667 1.00 172.71 ? 1329 MAN A C4 1 HETATM 3960 C C5 . MAN J 5 . ? 14.484 -49.990 8.147 1.00 171.61 ? 1329 MAN A C5 1 HETATM 3961 C C6 . MAN J 5 . ? 13.197 -50.490 7.499 1.00 165.95 ? 1329 MAN A C6 1 HETATM 3962 O O2 . MAN J 5 . ? 17.775 -48.969 6.593 1.00 173.72 ? 1329 MAN A O2 1 HETATM 3963 O O3 . MAN J 5 . ? 16.505 -46.901 7.543 1.00 170.62 ? 1329 MAN A O3 1 HETATM 3964 O O4 . MAN J 5 . ? 13.826 -47.688 8.140 1.00 172.59 ? 1329 MAN A O4 1 HETATM 3965 O O5 . MAN J 5 . ? 15.497 -50.905 7.777 1.00 175.67 ? 1329 MAN A O5 1 HETATM 3966 O O6 . MAN J 5 . ? 12.129 -49.614 7.777 1.00 161.08 ? 1329 MAN A O6 1 HETATM 3967 C C1 . NAG K 3 . ? 23.284 -12.202 -30.239 1.00 117.07 ? 1330 NAG A C1 1 HETATM 3968 C C2 . NAG K 3 . ? 21.806 -12.088 -29.864 1.00 128.79 ? 1330 NAG A C2 1 HETATM 3969 C C3 . NAG K 3 . ? 20.945 -12.482 -31.064 1.00 134.74 ? 1330 NAG A C3 1 HETATM 3970 C C4 . NAG K 3 . ? 21.342 -11.691 -32.313 1.00 136.29 ? 1330 NAG A C4 1 HETATM 3971 C C5 . NAG K 3 . ? 22.860 -11.635 -32.509 1.00 133.01 ? 1330 NAG A C5 1 HETATM 3972 C C6 . NAG K 3 . ? 23.247 -10.625 -33.589 1.00 131.15 ? 1330 NAG A C6 1 HETATM 3973 C C7 . NAG K 3 . ? 21.407 -12.363 -27.455 1.00 122.04 ? 1330 NAG A C7 1 HETATM 3974 C C8 . NAG K 3 . ? 21.037 -13.287 -26.329 1.00 117.76 ? 1330 NAG A C8 1 HETATM 3975 N N2 . NAG K 3 . ? 21.461 -12.881 -28.688 1.00 125.78 ? 1330 NAG A N2 1 HETATM 3976 O O3 . NAG K 3 . ? 19.586 -12.244 -30.768 1.00 136.39 ? 1330 NAG A O3 1 HETATM 3977 O O4 . NAG K 3 . ? 20.752 -12.279 -33.452 1.00 141.65 ? 1330 NAG A O4 1 HETATM 3978 O O5 . NAG K 3 . ? 23.503 -11.285 -31.296 1.00 126.60 ? 1330 NAG A O5 1 HETATM 3979 O O6 . NAG K 3 . ? 24.093 -11.238 -34.535 1.00 131.25 ? 1330 NAG A O6 1 HETATM 3980 O O7 . NAG K 3 . ? 21.649 -11.181 -27.206 1.00 122.39 ? 1330 NAG A O7 1 HETATM 3981 C C1 . SIA L 6 . ? 36.167 -5.091 21.614 1.00 92.75 ? 1331 SIA A C1 1 HETATM 3982 C C2 . SIA L 6 . ? 36.506 -5.200 23.094 1.00 88.84 ? 1331 SIA A C2 1 HETATM 3983 C C3 . SIA L 6 . ? 35.207 -5.121 23.899 1.00 85.05 ? 1331 SIA A C3 1 HETATM 3984 C C4 . SIA L 6 . ? 34.381 -6.386 23.745 1.00 83.30 ? 1331 SIA A C4 1 HETATM 3985 C C5 . SIA L 6 . ? 35.232 -7.590 24.126 1.00 81.99 ? 1331 SIA A C5 1 HETATM 3986 C C6 . SIA L 6 . ? 36.497 -7.638 23.263 1.00 78.85 ? 1331 SIA A C6 1 HETATM 3987 C C7 . SIA L 6 . ? 37.431 -8.813 23.573 1.00 76.43 ? 1331 SIA A C7 1 HETATM 3988 C C8 . SIA L 6 . ? 38.791 -8.710 22.867 1.00 75.36 ? 1331 SIA A C8 1 HETATM 3989 C C9 . SIA L 6 . ? 39.532 -10.046 22.919 1.00 74.84 ? 1331 SIA A C9 1 HETATM 3990 C C10 . SIA L 6 . ? 34.486 -9.895 24.463 1.00 86.69 ? 1331 SIA A C10 1 HETATM 3991 C C11 . SIA L 6 . ? 33.531 -10.968 24.032 1.00 86.58 ? 1331 SIA A C11 1 HETATM 3992 N N5 . SIA L 6 . ? 34.382 -8.736 23.821 1.00 84.44 ? 1331 SIA A N5 1 HETATM 3993 O O1A . SIA L 6 . ? 35.379 -4.188 21.237 1.00 95.37 ? 1331 SIA A O1A 1 HETATM 3994 O O1B . SIA L 6 . ? 36.686 -5.896 20.807 1.00 92.92 ? 1331 SIA A O1B 1 HETATM 3995 O O4 . SIA L 6 . ? 33.213 -6.311 24.567 1.00 80.98 ? 1331 SIA A O4 1 HETATM 3996 O O6 . SIA L 6 . ? 37.225 -6.410 23.399 1.00 79.10 ? 1331 SIA A O6 1 HETATM 3997 O O7 . SIA L 6 . ? 37.621 -8.922 24.984 1.00 74.97 ? 1331 SIA A O7 1 HETATM 3998 O O8 . SIA L 6 . ? 38.623 -8.348 21.488 1.00 77.11 ? 1331 SIA A O8 1 HETATM 3999 O O9 . SIA L 6 . ? 40.841 -9.939 22.338 1.00 70.66 ? 1331 SIA A O9 1 HETATM 4000 O O10 . SIA L 6 . ? 35.315 -10.081 25.340 1.00 86.71 ? 1331 SIA A O10 1 HETATM 4001 C C1 . GAL M 7 . ? 40.887 -3.015 23.449 1.00 116.74 ? 1332 GAL A C1 1 HETATM 4002 C C2 . GAL M 7 . ? 39.551 -3.488 24.020 1.00 109.35 ? 1332 GAL A C2 1 HETATM 4003 C C3 . GAL M 7 . ? 38.580 -3.905 22.923 1.00 104.13 ? 1332 GAL A C3 1 HETATM 4004 C C4 . GAL M 7 . ? 38.498 -2.839 21.834 1.00 106.76 ? 1332 GAL A C4 1 HETATM 4005 C C5 . GAL M 7 . ? 39.896 -2.458 21.362 1.00 108.98 ? 1332 GAL A C5 1 HETATM 4006 C C6 . GAL M 7 . ? 39.852 -1.384 20.279 1.00 106.83 ? 1332 GAL A C6 1 HETATM 4007 O O2 . GAL M 7 . ? 39.762 -4.606 24.884 1.00 108.60 ? 1332 GAL A O2 1 HETATM 4008 O O3 . GAL M 7 . ? 37.295 -4.083 23.523 1.00 97.06 ? 1332 GAL A O3 1 HETATM 4009 O O4 . GAL M 7 . ? 37.803 -1.688 22.333 1.00 104.50 ? 1332 GAL A O4 1 HETATM 4010 O O5 . GAL M 7 . ? 40.659 -1.994 22.475 1.00 115.57 ? 1332 GAL A O5 1 HETATM 4011 O O6 . GAL M 7 . ? 41.181 -1.104 19.829 1.00 103.72 ? 1332 GAL A O6 1 HETATM 4012 C C1 . NAG N 3 . ? 45.698 -1.363 24.906 1.00 142.56 ? 1333 NAG A C1 1 HETATM 4013 C C2 . NAG N 3 . ? 44.877 -0.544 23.911 1.00 142.48 ? 1333 NAG A C2 1 HETATM 4014 C C3 . NAG N 3 . ? 43.396 -0.751 24.217 1.00 139.99 ? 1333 NAG A C3 1 HETATM 4015 C C4 . NAG N 3 . ? 43.069 -2.241 24.083 1.00 134.18 ? 1333 NAG A C4 1 HETATM 4016 C C5 . NAG N 3 . ? 44.020 -3.107 24.918 1.00 132.94 ? 1333 NAG A C5 1 HETATM 4017 C C6 . NAG N 3 . ? 43.878 -4.587 24.569 1.00 127.19 ? 1333 NAG A C6 1 HETATM 4018 C C7 . NAG N 3 . ? 46.060 1.611 23.417 1.00 143.98 ? 1333 NAG A C7 1 HETATM 4019 C C8 . NAG N 3 . ? 46.844 0.991 22.291 1.00 142.44 ? 1333 NAG A C8 1 HETATM 4020 N N2 . NAG N 3 . ? 45.184 0.872 24.116 1.00 144.73 ? 1333 NAG A N2 1 HETATM 4021 O O1 . NAG N 3 . ? 47.105 -1.157 24.716 1.00 140.15 ? 1333 NAG A O1 1 HETATM 4022 O O3 . NAG N 3 . ? 42.584 0.035 23.334 1.00 139.23 ? 1333 NAG A O3 1 HETATM 4023 O O4 . NAG N 3 . ? 41.718 -2.492 24.492 1.00 126.41 ? 1333 NAG A O4 1 HETATM 4024 O O5 . NAG N 3 . ? 45.394 -2.748 24.716 1.00 141.28 ? 1333 NAG A O5 1 HETATM 4025 O O6 . NAG N 3 . ? 43.084 -5.252 25.553 1.00 121.08 ? 1333 NAG A O6 1 HETATM 4026 O O7 . NAG N 3 . ? 46.221 2.788 23.693 1.00 146.50 ? 1333 NAG A O7 1 HETATM 4027 C C1 . NAG O 3 . ? 25.228 -29.488 -75.268 1.00 96.57 ? 1163 NAG B C1 1 HETATM 4028 C C2 . NAG O 3 . ? 24.221 -30.648 -75.297 1.00 104.46 ? 1163 NAG B C2 1 HETATM 4029 C C3 . NAG O 3 . ? 23.806 -31.109 -76.694 1.00 108.86 ? 1163 NAG B C3 1 HETATM 4030 C C4 . NAG O 3 . ? 23.703 -29.925 -77.642 1.00 112.55 ? 1163 NAG B C4 1 HETATM 4031 C C5 . NAG O 3 . ? 25.048 -29.210 -77.640 1.00 106.34 ? 1163 NAG B C5 1 HETATM 4032 C C6 . NAG O 3 . ? 25.182 -28.130 -78.713 1.00 106.08 ? 1163 NAG B C6 1 HETATM 4033 C C7 . NAG O 3 . ? 24.806 -31.752 -73.198 1.00 104.95 ? 1163 NAG B C7 1 HETATM 4034 C C8 . NAG O 3 . ? 25.364 -32.969 -72.515 1.00 102.60 ? 1163 NAG B C8 1 HETATM 4035 N N2 . NAG O 3 . ? 24.741 -31.774 -74.531 1.00 104.90 ? 1163 NAG B N2 1 HETATM 4036 O O3 . NAG O 3 . ? 22.559 -31.763 -76.622 1.00 108.33 ? 1163 NAG B O3 1 HETATM 4037 O O4 . NAG O 3 . ? 23.292 -30.360 -78.929 1.00 123.03 ? 1163 NAG B O4 1 HETATM 4038 O O5 . NAG O 3 . ? 25.163 -28.607 -76.375 1.00 100.41 ? 1163 NAG B O5 1 HETATM 4039 O O6 . NAG O 3 . ? 24.417 -26.994 -78.375 1.00 103.67 ? 1163 NAG B O6 1 HETATM 4040 O O7 . NAG O 3 . ? 24.436 -30.791 -72.524 1.00 105.22 ? 1163 NAG B O7 1 HETATM 4041 C C1 . NAG P 3 . ? 22.126 -29.628 -79.370 1.00 128.75 ? 1164 NAG B C1 1 HETATM 4042 C C2 . NAG P 3 . ? 21.776 -30.027 -80.805 1.00 128.59 ? 1164 NAG B C2 1 HETATM 4043 C C3 . NAG P 3 . ? 20.415 -29.482 -81.253 1.00 135.93 ? 1164 NAG B C3 1 HETATM 4044 C C4 . NAG P 3 . ? 19.335 -29.573 -80.170 1.00 142.60 ? 1164 NAG B C4 1 HETATM 4045 C C5 . NAG P 3 . ? 19.893 -29.054 -78.845 1.00 137.60 ? 1164 NAG B C5 1 HETATM 4046 C C6 . NAG P 3 . ? 18.882 -29.083 -77.696 1.00 132.63 ? 1164 NAG B C6 1 HETATM 4047 C C7 . NAG P 3 . ? 23.962 -30.201 -81.916 1.00 119.73 ? 1164 NAG B C7 1 HETATM 4048 C C8 . NAG P 3 . ? 24.926 -29.608 -82.904 1.00 115.95 ? 1164 NAG B C8 1 HETATM 4049 N N2 . NAG P 3 . ? 22.803 -29.564 -81.731 1.00 124.16 ? 1164 NAG B N2 1 HETATM 4050 O O3 . NAG P 3 . ? 20.011 -30.163 -82.421 1.00 135.69 ? 1164 NAG B O3 1 HETATM 4051 O O4 . NAG P 3 . ? 18.187 -28.827 -80.550 1.00 155.03 ? 1164 NAG B O4 1 HETATM 4052 O O5 . NAG P 3 . ? 21.017 -29.845 -78.516 1.00 134.34 ? 1164 NAG B O5 1 HETATM 4053 O O6 . NAG P 3 . ? 18.656 -30.406 -77.266 1.00 126.36 ? 1164 NAG B O6 1 HETATM 4054 O O7 . NAG P 3 . ? 24.264 -31.232 -81.315 1.00 121.31 ? 1164 NAG B O7 1 HETATM 4055 C C1 . BMA Q 4 . ? 17.232 -29.588 -81.327 1.00 162.70 ? 1165 BMA B C1 1 HETATM 4056 C C2 . BMA Q 4 . ? 15.907 -29.673 -80.574 1.00 162.79 ? 1165 BMA B C2 1 HETATM 4057 C C3 . BMA Q 4 . ? 14.878 -30.470 -81.375 1.00 163.90 ? 1165 BMA B C3 1 HETATM 4058 C C4 . BMA Q 4 . ? 14.785 -29.984 -82.820 1.00 164.44 ? 1165 BMA B C4 1 HETATM 4059 C C5 . BMA Q 4 . ? 16.166 -29.827 -83.457 1.00 163.22 ? 1165 BMA B C5 1 HETATM 4060 C C6 . BMA Q 4 . ? 16.068 -29.186 -84.839 1.00 159.25 ? 1165 BMA B C6 1 HETATM 4061 O O2 . BMA Q 4 . ? 15.414 -28.352 -80.315 1.00 160.50 ? 1165 BMA B O2 1 HETATM 4062 O O3 . BMA Q 4 . ? 13.589 -30.368 -80.756 1.00 162.89 ? 1165 BMA B O3 1 HETATM 4063 O O4 . BMA Q 4 . ? 14.007 -30.921 -83.574 1.00 161.51 ? 1165 BMA B O4 1 HETATM 4064 O O5 . BMA Q 4 . ? 17.005 -29.021 -82.621 1.00 165.48 ? 1165 BMA B O5 1 HETATM 4065 O O6 . BMA Q 4 . ? 17.365 -29.133 -85.444 1.00 155.69 ? 1165 BMA B O6 1 HETATM 4066 S S1 . MPO R 8 . ? 38.133 -11.112 -71.379 1.00 115.49 ? 1166 MPO B S1 1 HETATM 4067 O O1 . MPO R 8 . ? 38.945 -10.406 -70.422 1.00 123.35 ? 1166 MPO B O1 1 HETATM 4068 O O2 . MPO R 8 . ? 38.012 -10.317 -72.570 1.00 123.13 ? 1166 MPO B O2 1 HETATM 4069 O O4 . MPO R 8 . ? 44.259 -9.917 -73.073 1.00 106.31 ? 1166 MPO B O4 1 HETATM 4070 N N1 . MPO R 8 . ? 42.358 -11.417 -72.157 1.00 101.39 ? 1166 MPO B N1 1 HETATM 4071 C C1 . MPO R 8 . ? 38.830 -12.584 -71.730 1.00 102.77 ? 1166 MPO B C1 1 HETATM 4072 O O3 . MPO R 8 . ? 36.638 -11.334 -70.754 1.00 112.12 ? 1166 MPO B O3 1 HETATM 4073 C C2 . MPO R 8 . ? 40.146 -12.423 -72.479 1.00 95.48 ? 1166 MPO B C2 1 HETATM 4074 C C3 . MPO R 8 . ? 41.321 -12.250 -71.527 1.00 94.48 ? 1166 MPO B C3 1 HETATM 4075 C C4 . MPO R 8 . ? 43.659 -11.680 -71.524 1.00 104.87 ? 1166 MPO B C4 1 HETATM 4076 C C5 . MPO R 8 . ? 44.665 -10.587 -71.878 1.00 105.83 ? 1166 MPO B C5 1 HETATM 4077 C C6 . MPO R 8 . ? 43.056 -9.171 -72.866 1.00 108.94 ? 1166 MPO B C6 1 HETATM 4078 C C7 . MPO R 8 . ? 42.060 -9.978 -72.027 1.00 108.09 ? 1166 MPO B C7 1 HETATM 4079 O O . HOH S 9 . ? 38.423 -14.158 -82.474 1.00 64.61 ? 2001 HOH A O 1 HETATM 4080 O O . HOH S 9 . ? 37.383 -18.191 -85.697 1.00 73.99 ? 2002 HOH A O 1 HETATM 4081 O O . HOH S 9 . ? 34.439 -12.611 -83.521 1.00 72.85 ? 2003 HOH A O 1 HETATM 4082 O O . HOH S 9 . ? 36.329 -14.221 -75.696 1.00 52.16 ? 2004 HOH A O 1 HETATM 4083 O O . HOH S 9 . ? 42.948 -13.053 -76.503 1.00 67.98 ? 2005 HOH A O 1 HETATM 4084 O O . HOH S 9 . ? 41.441 -15.994 -70.210 1.00 51.30 ? 2006 HOH A O 1 HETATM 4085 O O . HOH S 9 . ? 39.931 -14.662 -65.601 1.00 52.01 ? 2007 HOH A O 1 HETATM 4086 O O . HOH S 9 . ? 40.448 -12.763 -58.929 1.00 47.19 ? 2008 HOH A O 1 HETATM 4087 O O . HOH S 9 . ? 31.417 -11.657 -54.859 1.00 55.56 ? 2009 HOH A O 1 HETATM 4088 O O . HOH S 9 . ? 39.409 -7.533 -58.634 1.00 64.48 ? 2010 HOH A O 1 HETATM 4089 O O . HOH S 9 . ? 40.195 -5.336 -54.405 1.00 69.24 ? 2011 HOH A O 1 HETATM 4090 O O . HOH S 9 . ? 34.465 -10.411 -49.798 1.00 73.81 ? 2012 HOH A O 1 HETATM 4091 O O . HOH S 9 . ? 35.635 -6.812 -48.877 1.00 66.43 ? 2013 HOH A O 1 HETATM 4092 O O . HOH S 9 . ? 42.929 -5.860 -49.866 1.00 79.62 ? 2014 HOH A O 1 HETATM 4093 O O . HOH S 9 . ? 45.711 -7.806 -42.812 1.00 75.74 ? 2015 HOH A O 1 HETATM 4094 O O . HOH S 9 . ? 46.247 -10.653 -43.834 1.00 58.35 ? 2016 HOH A O 1 HETATM 4095 O O . HOH S 9 . ? 44.876 -15.114 -42.460 1.00 41.59 ? 2017 HOH A O 1 HETATM 4096 O O . HOH S 9 . ? 49.813 -9.691 -41.598 1.00 63.75 ? 2018 HOH A O 1 HETATM 4097 O O . HOH S 9 . ? 46.597 -13.009 -39.698 1.00 59.85 ? 2019 HOH A O 1 HETATM 4098 O O . HOH S 9 . ? 50.168 -14.111 -39.977 1.00 63.17 ? 2020 HOH A O 1 HETATM 4099 O O . HOH S 9 . ? 51.409 -18.553 -50.627 1.00 63.03 ? 2021 HOH A O 1 HETATM 4100 O O . HOH S 9 . ? 56.470 -14.130 -51.151 1.00 58.99 ? 2022 HOH A O 1 HETATM 4101 O O . HOH S 9 . ? 52.511 -16.547 -52.152 1.00 59.32 ? 2023 HOH A O 1 HETATM 4102 O O . HOH S 9 . ? 52.708 -14.030 -55.087 1.00 67.28 ? 2024 HOH A O 1 HETATM 4103 O O . HOH S 9 . ? 54.270 -11.138 -47.445 1.00 66.39 ? 2025 HOH A O 1 HETATM 4104 O O . HOH S 9 . ? 47.074 -9.227 -52.845 1.00 71.57 ? 2026 HOH A O 1 HETATM 4105 O O . HOH S 9 . ? 31.987 -18.022 -50.648 1.00 66.26 ? 2027 HOH A O 1 HETATM 4106 O O . HOH S 9 . ? 32.971 -13.824 -47.575 1.00 67.01 ? 2028 HOH A O 1 HETATM 4107 O O . HOH S 9 . ? 32.117 -18.491 -45.461 1.00 63.67 ? 2029 HOH A O 1 HETATM 4108 O O . HOH S 9 . ? 30.980 -21.955 -40.701 1.00 69.82 ? 2030 HOH A O 1 HETATM 4109 O O . HOH S 9 . ? 33.737 -13.812 -41.865 1.00 69.97 ? 2031 HOH A O 1 HETATM 4110 O O . HOH S 9 . ? 40.134 -12.420 -36.852 1.00 58.46 ? 2032 HOH A O 1 HETATM 4111 O O . HOH S 9 . ? 47.852 -29.020 -1.380 1.00 45.63 ? 2033 HOH A O 1 HETATM 4112 O O . HOH S 9 . ? 34.525 -10.090 -33.725 1.00 68.86 ? 2034 HOH A O 1 HETATM 4113 O O . HOH S 9 . ? 39.879 -8.787 -27.961 1.00 77.86 ? 2035 HOH A O 1 HETATM 4114 O O . HOH S 9 . ? 30.533 -11.364 -28.203 1.00 61.89 ? 2036 HOH A O 1 HETATM 4115 O O . HOH S 9 . ? 27.891 -5.197 -15.834 1.00 63.50 ? 2037 HOH A O 1 HETATM 4116 O O . HOH S 9 . ? 26.919 -27.499 27.421 1.00 76.83 ? 2038 HOH A O 1 HETATM 4117 O O . HOH S 9 . ? 22.789 -21.143 -16.244 1.00 69.93 ? 2039 HOH A O 1 HETATM 4118 O O . HOH S 9 . ? 31.869 -8.371 -6.776 1.00 74.80 ? 2040 HOH A O 1 HETATM 4119 O O . HOH S 9 . ? 25.511 -14.814 5.715 1.00 75.37 ? 2041 HOH A O 1 HETATM 4120 O O . HOH S 9 . ? 25.299 -6.840 2.998 1.00 72.71 ? 2042 HOH A O 1 HETATM 4121 O O . HOH S 9 . ? 22.093 -9.710 -3.189 1.00 74.02 ? 2043 HOH A O 1 HETATM 4122 O O . HOH S 9 . ? 16.832 -15.640 -1.089 1.00 75.98 ? 2044 HOH A O 1 HETATM 4123 O O . HOH S 9 . ? 18.113 -18.500 8.865 1.00 61.05 ? 2045 HOH A O 1 HETATM 4124 O O . HOH S 9 . ? 18.641 -16.043 9.052 1.00 63.57 ? 2046 HOH A O 1 HETATM 4125 O O . HOH S 9 . ? 22.575 -14.493 -5.161 1.00 71.68 ? 2047 HOH A O 1 HETATM 4126 O O . HOH S 9 . ? 38.277 -14.621 -0.430 1.00 60.99 ? 2048 HOH A O 1 HETATM 4127 O O . HOH S 9 . ? 40.085 -15.012 4.254 1.00 82.64 ? 2049 HOH A O 1 HETATM 4128 O O . HOH S 9 . ? 41.299 -8.070 21.044 1.00 57.87 ? 2050 HOH A O 1 HETATM 4129 O O . HOH S 9 . ? 46.314 -14.693 12.630 1.00 63.67 ? 2051 HOH A O 1 HETATM 4130 O O . HOH S 9 . ? 41.782 -16.419 5.691 1.00 72.18 ? 2052 HOH A O 1 HETATM 4131 O O . HOH S 9 . ? 43.631 -18.677 5.414 1.00 69.16 ? 2053 HOH A O 1 HETATM 4132 O O . HOH S 9 . ? 39.416 -26.419 8.681 1.00 63.37 ? 2054 HOH A O 1 HETATM 4133 O O . HOH S 9 . ? 43.181 -24.606 1.479 1.00 54.97 ? 2055 HOH A O 1 HETATM 4134 O O . HOH S 9 . ? 39.665 -28.416 6.857 1.00 66.21 ? 2056 HOH A O 1 HETATM 4135 O O . HOH S 9 . ? 40.772 -22.723 -4.809 1.00 65.30 ? 2057 HOH A O 1 HETATM 4136 O O . HOH S 9 . ? 45.407 -29.065 -2.975 1.00 47.13 ? 2058 HOH A O 1 HETATM 4137 O O . HOH S 9 . ? 46.726 -18.208 -56.251 1.00 49.24 ? 2059 HOH A O 1 HETATM 4138 O O . HOH S 9 . ? 16.867 -21.708 22.130 1.00 77.00 ? 2060 HOH A O 1 HETATM 4139 O O . HOH S 9 . ? 25.714 -24.879 27.716 1.00 74.05 ? 2061 HOH A O 1 HETATM 4140 O O . HOH S 9 . ? 28.311 -13.933 24.855 1.00 76.87 ? 2062 HOH A O 1 HETATM 4141 O O . HOH S 9 . ? 27.154 -13.076 21.501 1.00 76.06 ? 2063 HOH A O 1 HETATM 4142 O O . HOH S 9 . ? 28.445 0.676 11.608 1.00 65.71 ? 2064 HOH A O 1 HETATM 4143 O O . HOH S 9 . ? 28.176 -1.076 20.791 1.00 74.73 ? 2065 HOH A O 1 HETATM 4144 O O . HOH S 9 . ? 25.190 -11.152 14.868 1.00 77.17 ? 2066 HOH A O 1 HETATM 4145 O O . HOH S 9 . ? 24.130 -15.965 16.227 1.00 72.67 ? 2067 HOH A O 1 HETATM 4146 O O . HOH S 9 . ? 24.065 -37.170 18.178 1.00 69.98 ? 2068 HOH A O 1 HETATM 4147 O O . HOH S 9 . ? 24.027 -35.253 4.485 1.00 78.44 ? 2069 HOH A O 1 HETATM 4148 O O . HOH S 9 . ? 45.101 -8.015 29.036 1.00 74.82 ? 2070 HOH A O 1 HETATM 4149 O O . HOH S 9 . ? 33.426 -34.793 9.172 1.00 62.64 ? 2071 HOH A O 1 HETATM 4150 O O . HOH S 9 . ? 36.561 -43.270 9.627 1.00 69.47 ? 2072 HOH A O 1 HETATM 4151 O O . HOH S 9 . ? 41.927 -35.511 12.317 1.00 73.79 ? 2073 HOH A O 1 HETATM 4152 O O . HOH S 9 . ? 43.853 -31.305 15.832 1.00 66.84 ? 2074 HOH A O 1 HETATM 4153 O O . HOH S 9 . ? 44.393 -1.871 14.218 1.00 69.38 ? 2075 HOH A O 1 HETATM 4154 O O . HOH S 9 . ? 48.555 -12.673 13.832 1.00 80.99 ? 2076 HOH A O 1 HETATM 4155 O O . HOH S 9 . ? 35.541 -32.116 5.302 1.00 62.47 ? 2077 HOH A O 1 HETATM 4156 O O . HOH S 9 . ? 36.879 -32.653 8.161 1.00 72.18 ? 2078 HOH A O 1 HETATM 4157 O O . HOH S 9 . ? 25.993 -29.965 -13.138 1.00 70.95 ? 2079 HOH A O 1 HETATM 4158 O O . HOH S 9 . ? 39.706 -13.622 -13.554 1.00 67.87 ? 2080 HOH A O 1 HETATM 4159 O O . HOH S 9 . ? 30.761 -1.810 -13.083 1.00 75.06 ? 2081 HOH A O 1 HETATM 4160 O O . HOH S 9 . ? 18.130 -9.474 -18.015 1.00 79.02 ? 2082 HOH A O 1 HETATM 4161 O O . HOH S 9 . ? 24.888 -15.535 -32.071 1.00 79.80 ? 2083 HOH A O 1 HETATM 4162 O O . HOH S 9 . ? 36.448 -19.838 -23.286 1.00 66.80 ? 2084 HOH A O 1 HETATM 4163 O O . HOH S 9 . ? 42.299 -9.321 -26.201 1.00 76.68 ? 2085 HOH A O 1 HETATM 4164 O O . HOH S 9 . ? 41.660 -8.511 -31.075 1.00 68.52 ? 2086 HOH A O 1 HETATM 4165 O O . HOH S 9 . ? 39.993 -8.738 -24.682 1.00 74.16 ? 2087 HOH A O 1 HETATM 4166 O O . HOH S 9 . ? 40.883 -21.508 -21.584 1.00 64.61 ? 2088 HOH A O 1 HETATM 4167 O O . HOH S 9 . ? 45.191 -11.430 -27.625 1.00 74.55 ? 2089 HOH A O 1 HETATM 4168 O O . HOH S 9 . ? 45.216 -15.412 -39.643 1.00 47.21 ? 2090 HOH A O 1 HETATM 4169 O O . HOH S 9 . ? 40.048 -9.885 -38.049 1.00 68.98 ? 2091 HOH A O 1 HETATM 4170 O O . HOH S 9 . ? 41.618 -21.848 -46.157 1.00 45.50 ? 2092 HOH A O 1 HETATM 4171 O O . HOH S 9 . ? 44.036 -18.314 -55.706 1.00 39.28 ? 2093 HOH A O 1 HETATM 4172 O O . HOH S 9 . ? 48.369 -17.142 -57.920 1.00 52.31 ? 2094 HOH A O 1 HETATM 4173 O O . HOH S 9 . ? 46.072 -10.482 -58.469 1.00 77.28 ? 2095 HOH A O 1 HETATM 4174 O O . HOH S 9 . ? 23.890 -44.432 16.916 1.00 71.07 ? 2096 HOH A O 1 HETATM 4175 O O . HOH T 9 . ? 49.465 -19.537 -60.595 1.00 51.57 ? 2001 HOH B O 1 HETATM 4176 O O . HOH T 9 . ? 52.774 -26.100 -62.146 1.00 57.38 ? 2002 HOH B O 1 HETATM 4177 O O . HOH T 9 . ? 52.441 -19.370 -64.985 1.00 49.35 ? 2003 HOH B O 1 HETATM 4178 O O . HOH T 9 . ? 32.962 -2.344 -58.070 1.00 69.67 ? 2004 HOH B O 1 HETATM 4179 O O . HOH T 9 . ? 50.352 -12.894 -64.719 1.00 65.14 ? 2005 HOH B O 1 HETATM 4180 O O . HOH T 9 . ? 45.747 -13.365 -69.816 1.00 70.72 ? 2006 HOH B O 1 HETATM 4181 O O . HOH T 9 . ? 49.540 -14.348 -70.333 1.00 62.76 ? 2007 HOH B O 1 HETATM 4182 O O . HOH T 9 . ? 43.592 -12.690 -68.026 1.00 57.82 ? 2008 HOH B O 1 HETATM 4183 O O . HOH T 9 . ? 49.219 -11.212 -62.965 1.00 70.07 ? 2009 HOH B O 1 HETATM 4184 O O . HOH T 9 . ? 41.505 -9.469 -65.761 1.00 66.25 ? 2010 HOH B O 1 HETATM 4185 O O . HOH T 9 . ? 41.244 -13.787 -68.587 1.00 58.25 ? 2011 HOH B O 1 HETATM 4186 O O . HOH T 9 . ? 35.180 -9.094 -66.390 1.00 57.15 ? 2012 HOH B O 1 HETATM 4187 O O . HOH T 9 . ? 36.044 -3.821 -57.901 1.00 77.32 ? 2013 HOH B O 1 HETATM 4188 O O . HOH T 9 . ? 32.473 -20.517 -49.945 1.00 58.46 ? 2014 HOH B O 1 HETATM 4189 O O . HOH T 9 . ? 28.347 -15.416 -65.929 1.00 66.02 ? 2015 HOH B O 1 HETATM 4190 O O . HOH T 9 . ? 29.707 -19.334 -56.157 1.00 67.73 ? 2016 HOH B O 1 HETATM 4191 O O . HOH T 9 . ? 31.111 -17.372 -56.281 1.00 52.20 ? 2017 HOH B O 1 HETATM 4192 O O . HOH T 9 . ? 30.738 -18.162 -72.524 1.00 63.53 ? 2018 HOH B O 1 HETATM 4193 O O . HOH T 9 . ? 27.758 -14.721 -78.846 1.00 59.73 ? 2019 HOH B O 1 HETATM 4194 O O . HOH T 9 . ? 25.208 -14.990 -75.483 0.50 65.15 ? 2020 HOH B O 1 HETATM 4195 O O . HOH T 9 . ? 31.379 -9.760 -79.439 1.00 73.05 ? 2021 HOH B O 1 HETATM 4196 O O . HOH T 9 . ? 30.001 -28.230 -65.606 1.00 72.74 ? 2022 HOH B O 1 HETATM 4197 O O . HOH T 9 . ? 28.463 -25.917 -66.124 1.00 63.10 ? 2023 HOH B O 1 HETATM 4198 O O . HOH T 9 . ? 29.098 -28.380 -49.568 1.00 73.28 ? 2024 HOH B O 1 HETATM 4199 O O . HOH T 9 . ? 32.389 -21.812 -47.711 1.00 63.84 ? 2025 HOH B O 1 HETATM 4200 O O . HOH T 9 . ? 43.123 -27.836 -49.730 1.00 60.39 ? 2026 HOH B O 1 HETATM 4201 O O . HOH T 9 . ? 37.290 -34.224 -42.699 1.00 57.42 ? 2027 HOH B O 1 HETATM 4202 O O . HOH T 9 . ? 41.150 -33.185 -32.021 1.00 65.84 ? 2028 HOH B O 1 HETATM 4203 O O . HOH T 9 . ? 42.538 -26.071 -16.092 1.00 62.08 ? 2029 HOH B O 1 HETATM 4204 O O . HOH T 9 . ? 43.784 -21.161 -12.485 1.00 78.72 ? 2030 HOH B O 1 HETATM 4205 O O . HOH T 9 . ? 45.676 -17.717 -5.968 1.00 57.46 ? 2031 HOH B O 1 HETATM 4206 O O . HOH T 9 . ? 49.979 -23.326 3.834 1.00 65.98 ? 2032 HOH B O 1 HETATM 4207 O O . HOH T 9 . ? 56.139 -14.656 2.367 1.00 61.61 ? 2033 HOH B O 1 HETATM 4208 O O . HOH T 9 . ? 52.129 -24.331 2.851 1.00 64.18 ? 2034 HOH B O 1 HETATM 4209 O O . HOH T 9 . ? 54.084 -24.914 0.089 1.00 51.83 ? 2035 HOH B O 1 HETATM 4210 O O . HOH T 9 . ? 49.717 -27.161 -0.780 1.00 57.15 ? 2036 HOH B O 1 HETATM 4211 O O . HOH T 9 . ? 53.890 -18.025 -7.222 1.00 63.78 ? 2037 HOH B O 1 HETATM 4212 O O . HOH T 9 . ? 48.004 -19.866 -10.494 1.00 54.05 ? 2038 HOH B O 1 HETATM 4213 O O . HOH T 9 . ? 53.714 -24.137 -24.054 1.00 60.12 ? 2039 HOH B O 1 HETATM 4214 O O . HOH T 9 . ? 52.253 -19.802 -29.171 1.00 68.54 ? 2040 HOH B O 1 HETATM 4215 O O . HOH T 9 . ? 47.701 -26.962 -36.259 1.00 48.51 ? 2041 HOH B O 1 HETATM 4216 O O . HOH T 9 . ? 50.794 -29.325 -31.134 0.33 53.83 ? 2042 HOH B O 1 HETATM 4217 O O . HOH T 9 . ? 47.284 -17.442 -38.752 1.00 47.23 ? 2043 HOH B O 1 HETATM 4218 O O . HOH T 9 . ? 45.784 -30.171 -45.936 1.00 67.02 ? 2044 HOH B O 1 HETATM 4219 O O . HOH T 9 . ? 46.140 -27.286 -52.429 1.00 46.23 ? 2045 HOH B O 1 HETATM 4220 O O . HOH T 9 . ? 44.790 -29.409 -51.503 1.00 53.47 ? 2046 HOH B O 1 HETATM 4221 O O . HOH T 9 . ? 49.645 -32.046 -52.442 1.00 52.60 ? 2047 HOH B O 1 HETATM 4222 O O . HOH T 9 . ? 51.920 -22.421 -52.642 1.00 47.58 ? 2048 HOH B O 1 HETATM 4223 O O . HOH T 9 . ? 42.113 -29.424 -57.866 1.00 49.96 ? 2049 HOH B O 1 HETATM 4224 O O . HOH T 9 . ? 38.516 -27.851 -62.483 1.00 49.38 ? 2050 HOH B O 1 HETATM 4225 O O . HOH T 9 . ? 37.810 -29.809 -57.587 1.00 64.32 ? 2051 HOH B O 1 HETATM 4226 O O . HOH T 9 . ? 39.762 -29.802 -60.776 1.00 59.35 ? 2052 HOH B O 1 HETATM 4227 O O . HOH T 9 . ? 41.994 -31.419 -67.171 1.00 55.89 ? 2053 HOH B O 1 HETATM 4228 O O . HOH T 9 . ? 45.097 -30.578 -65.779 1.00 50.10 ? 2054 HOH B O 1 HETATM 4229 O O . HOH T 9 . ? 45.795 -19.888 -74.073 1.00 51.06 ? 2055 HOH B O 1 HETATM 4230 O O . HOH T 9 . ? 38.384 -32.769 -72.264 1.00 58.78 ? 2056 HOH B O 1 HETATM 4231 O O . HOH T 9 . ? 44.400 -27.455 -77.765 1.00 63.63 ? 2057 HOH B O 1 HETATM 4232 O O . HOH T 9 . ? 48.964 -25.666 -72.335 1.00 54.92 ? 2058 HOH B O 1 HETATM 4233 O O . HOH T 9 . ? 37.840 -33.872 -78.842 1.00 69.35 ? 2059 HOH B O 1 HETATM 4234 O O . HOH T 9 . ? 46.813 -27.162 -81.110 1.00 72.94 ? 2060 HOH B O 1 HETATM 4235 O O . HOH T 9 . ? 47.634 -24.404 -80.809 1.00 65.70 ? 2061 HOH B O 1 HETATM 4236 O O . HOH T 9 . ? 49.632 -27.711 -75.605 1.00 63.43 ? 2062 HOH B O 1 HETATM 4237 O O . HOH T 9 . ? 49.926 -14.024 -73.082 1.00 66.82 ? 2063 HOH B O 1 HETATM 4238 O O . HOH T 9 . ? 47.010 -11.590 -73.863 1.00 74.33 ? 2064 HOH B O 1 HETATM 4239 O O . HOH T 9 . ? 26.925 -32.004 -79.501 1.00 73.25 ? 2065 HOH B O 1 HETATM 4240 O O . HOH T 9 . ? 38.787 -31.647 -89.844 1.00 74.42 ? 2066 HOH B O 1 HETATM 4241 O O . HOH T 9 . ? 17.625 -12.673 9.035 1.00 81.19 ? 2067 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 ? 0.9184 0.9944 0.5706 0.3064 -0.1239 -0.0342 1 ASP A N 2 C CA . ASP A 1 ? 0.8810 1.0040 0.5629 0.3009 -0.1263 -0.0433 1 ASP A CA 3 C C . ASP A 1 ? 0.8515 0.9565 0.5570 0.2720 -0.1175 -0.0429 1 ASP A C 4 O O . ASP A 1 ? 0.8393 0.9247 0.5497 0.2509 -0.1115 -0.0411 1 ASP A O 5 C CB . ASP A 1 ? 0.8681 1.0587 0.5683 0.2942 -0.1335 -0.0553 1 ASP A CB 6 C CG . ASP A 1 ? 0.8984 1.1172 0.5771 0.3240 -0.1430 -0.0566 1 ASP A CG 7 O OD1 . ASP A 1 ? 0.9216 1.1019 0.5681 0.3522 -0.1439 -0.0478 1 ASP A OD1 8 O OD2 . ASP A 1 ? 0.9235 1.2020 0.6142 0.3185 -0.1496 -0.0663 1 ASP A OD2 9 N N . GLN A 2 ? 0.8513 0.9637 0.5695 0.2732 -0.1167 -0.0444 2 GLN A N 10 C CA . GLN A 2 ? 0.8226 0.9197 0.5623 0.2481 -0.1088 -0.0439 2 GLN A CA 11 C C . GLN A 2 ? 0.7895 0.9256 0.5534 0.2438 -0.1105 -0.0516 2 GLN A C 12 O O . GLN A 2 ? 0.7770 0.9449 0.5380 0.2653 -0.1170 -0.0552 2 GLN A O 13 C CB . GLN A 2 ? 0.8576 0.8949 0.5801 0.2489 -0.1018 -0.0324 2 GLN A CB 14 C CG . GLN A 2 ? 0.9104 0.9243 0.6069 0.2749 -0.1047 -0.0276 2 GLN A CG 15 C CD . GLN A 2 ? 0.9438 0.9041 0.6280 0.2660 -0.0973 -0.0187 2 GLN A CD 16 O OE1 . GLN A 2 ? 0.9834 0.9341 0.6634 0.2742 -0.0975 -0.0184 2 GLN A OE1 17 N NE2 . GLN A 2 ? 0.9507 0.8787 0.6279 0.2488 -0.0907 -0.0115 2 GLN A NE2 18 N N . ILE A 3 ? 0.7534 0.8874 0.5389 0.2172 -0.1043 -0.0540 3 ILE A N 19 C CA . ILE A 3 ? 0.7343 0.8948 0.5418 0.2085 -0.1038 -0.0598 3 ILE A CA 20 C C . ILE A 3 ? 0.7374 0.8552 0.5499 0.1967 -0.0952 -0.0530 3 ILE A C 21 O O . ILE A 3 ? 0.7269 0.8130 0.5366 0.1833 -0.0891 -0.0481 3 ILE A O 22 C CB . ILE A 3 ? 0.7207 0.9265 0.5467 0.1852 -0.1053 -0.0709 3 ILE A CB 23 C CG1 . ILE A 3 ? 0.7096 0.9513 0.5556 0.1784 -0.1058 -0.0773 3 ILE A CG1 24 C CG2 . ILE A 3 ? 0.7114 0.8874 0.5385 0.1595 -0.0984 -0.0704 3 ILE A CG2 25 C CD1 . ILE A 3 ? 0.7005 0.9979 0.5582 0.1580 -0.1096 -0.0892 3 ILE A CD1 26 N N . CYS A 4 ? 0.7479 0.8675 0.5663 0.2034 -0.0949 -0.0528 4 CYS A N 27 C CA . CYS A 4 ? 0.7391 0.8205 0.5598 0.1944 -0.0878 -0.0462 4 CYS A CA 28 C C . CYS A 4 ? 0.7010 0.8075 0.5460 0.1809 -0.0860 -0.0524 4 CYS A C 29 O O . CYS A 4 ? 0.6896 0.8399 0.5443 0.1863 -0.0910 -0.0601 4 CYS A O 30 C CB . CYS A 4 ? 0.7943 0.8409 0.5902 0.2157 -0.0886 -0.0388 4 CYS A CB 31 S SG . CYS A 4 ? 0.8960 0.9031 0.6538 0.2321 -0.0903 -0.0303 4 CYS A SG 32 N N . ILE A 5 ? 0.6608 0.7432 0.5149 0.1637 -0.0788 -0.0489 5 ILE A N 33 C CA . ILE A 5 ? 0.6299 0.7278 0.5033 0.1520 -0.0765 -0.0533 5 ILE A CA 34 C C . ILE A 5 ? 0.6325 0.7037 0.5006 0.1606 -0.0743 -0.0471 5 ILE A C 35 O O . ILE A 5 ? 0.6357 0.6684 0.4886 0.1623 -0.0712 -0.0387 5 ILE A O 36 C CB . ILE A 5 ? 0.6219 0.7111 0.5058 0.1281 -0.0701 -0.0542 5 ILE A CB 37 C CG1 . ILE A 5 ? 0.6490 0.7551 0.5299 0.1184 -0.0720 -0.0604 5 ILE A CG1 38 C CG2 . ILE A 5 ? 0.6116 0.7132 0.5119 0.1163 -0.0674 -0.0582 5 ILE A CG2 39 C CD1 . ILE A 5 ? 0.6636 0.8170 0.5534 0.1124 -0.0773 -0.0710 5 ILE A CD1 40 N N . GLY A 6 ? 0.6226 0.7152 0.5009 0.1646 -0.0758 -0.0516 6 GLY A N 41 C CA . GLY A 6 ? 0.6258 0.6923 0.4951 0.1741 -0.0744 -0.0469 6 GLY A CA 42 C C . GLY A 6 ? 0.6058 0.6994 0.4928 0.1714 -0.0742 -0.0527 6 GLY A C 43 O O . GLY A 6 ? 0.5953 0.7274 0.5019 0.1587 -0.0745 -0.0601 6 GLY A O 44 N N . TYR A 7 ? 0.6074 0.6784 0.4837 0.1820 -0.0735 -0.0495 7 TYR A N 45 C CA . TYR A 7 ? 0.5972 0.6876 0.4888 0.1788 -0.0723 -0.0538 7 TYR A CA 46 C C . TYR A 7 ? 0.6337 0.7136 0.5048 0.2050 -0.0754 -0.0534 7 TYR A C 47 O O . TYR A 7 ? 0.6640 0.7061 0.5040 0.2223 -0.0772 -0.0481 7 TYR A O 48 C CB . TYR A 7 ? 0.5844 0.6508 0.4875 0.1559 -0.0653 -0.0498 7 TYR A CB 49 C CG . TYR A 7 ? 0.6025 0.6179 0.4856 0.1546 -0.0622 -0.0404 7 TYR A CG 50 C CD1 . TYR A 7 ? 0.6099 0.6057 0.4863 0.1460 -0.0599 -0.0348 7 TYR A CD1 51 C CD2 . TYR A 7 ? 0.6373 0.6254 0.5059 0.1602 -0.0613 -0.0374 7 TYR A CD2 52 C CE1 . TYR A 7 ? 0.6439 0.5994 0.5012 0.1411 -0.0568 -0.0263 7 TYR A CE1 53 C CE2 . TYR A 7 ? 0.6588 0.6013 0.5055 0.1539 -0.0584 -0.0292 7 TYR A CE2 54 C CZ . TYR A 7 ? 0.6620 0.5910 0.5040 0.1434 -0.0561 -0.0236 7 TYR A CZ 55 O OH . TYR A 7 ? 0.7109 0.6003 0.5302 0.1338 -0.0529 -0.0156 7 TYR A OH 56 N N . HIS A 8 ? 0.6292 0.7404 0.5145 0.2075 -0.0756 -0.0591 8 HIS A N 57 C CA . HIS A 8 ? 0.6723 0.7846 0.5397 0.2354 -0.0787 -0.0608 8 HIS A CA 58 C C . HIS A 8 ? 0.7140 0.7608 0.5523 0.2403 -0.0759 -0.0535 8 HIS A C 59 O O . HIS A 8 ? 0.7256 0.7448 0.5711 0.2168 -0.0707 -0.0493 8 HIS A O 60 C CB . HIS A 8 ? 0.6566 0.8210 0.5508 0.2299 -0.0780 -0.0685 8 HIS A CB 61 C CG . HIS A 8 ? 0.6814 0.8582 0.5605 0.2601 -0.0808 -0.0715 8 HIS A CG 62 N ND1 . HIS A 8 ? 0.7083 0.9147 0.5711 0.2933 -0.0869 -0.0748 8 HIS A ND1 63 C CD2 . HIS A 8 ? 0.6817 0.8487 0.5585 0.2642 -0.0783 -0.0721 8 HIS A CD2 64 C CE1 . HIS A 8 ? 0.7195 0.9318 0.5686 0.3186 -0.0878 -0.0771 8 HIS A CE1 65 N NE2 . HIS A 8 ? 0.7052 0.8928 0.5626 0.3005 -0.0826 -0.0756 8 HIS A NE2 66 N N . ALA A 9 ? 0.7593 0.7809 0.5608 0.2712 -0.0794 -0.0522 9 ALA A N 67 C CA . ALA A 9 ? 0.7966 0.7566 0.5635 0.2775 -0.0772 -0.0473 9 ALA A CA 68 C C . ALA A 9 ? 0.8270 0.7967 0.5714 0.3141 -0.0810 -0.0519 9 ALA A C 69 O O . ALA A 9 ? 0.8664 0.8875 0.6175 0.3368 -0.0857 -0.0574 9 ALA A O 70 C CB . ALA A 9 ? 0.8263 0.7199 0.5528 0.2768 -0.0766 -0.0387 9 ALA A CB 71 N N . ASN A 10 ? 0.8571 0.7809 0.5738 0.3202 -0.0789 -0.0500 10 ASN A N 72 C CA . ASN A 10 ? 0.9075 0.8323 0.5952 0.3588 -0.0820 -0.0540 10 ASN A CA 73 C C . ASN A 10 ? 1.0033 0.8441 0.6392 0.3638 -0.0795 -0.0492 10 ASN A C 74 O O . ASN A 10 ? 1.0033 0.7876 0.6232 0.3376 -0.0762 -0.0424 10 ASN A O 75 C CB . ASN A 10 ? 0.8523 0.8546 0.5831 0.3598 -0.0819 -0.0626 10 ASN A CB 76 C CG . ASN A 10 ? 0.8318 0.8268 0.5861 0.3296 -0.0764 -0.0625 10 ASN A CG 77 O OD1 . ASN A 10 ? 0.8407 0.7753 0.5785 0.3099 -0.0729 -0.0564 10 ASN A OD1 78 N ND2 . ASN A 10 ? 0.7915 0.8515 0.5834 0.3248 -0.0756 -0.0694 10 ASN A ND2 79 N N . ASN A 11 ? 1.1082 0.9417 0.7154 0.3967 -0.0811 -0.0529 11 ASN A N 80 C CA . ASN A 11 ? 1.2457 0.9920 0.7930 0.4046 -0.0791 -0.0491 11 ASN A CA 81 C C . ASN A 11 ? 1.1893 0.9312 0.7549 0.3802 -0.0746 -0.0506 11 ASN A C 82 O O . ASN A 11 ? 1.2308 0.9119 0.7491 0.3902 -0.0734 -0.0497 11 ASN A O 83 C CB . ASN A 11 ? 1.4111 1.1343 0.9010 0.4597 -0.0832 -0.0514 11 ASN A CB 84 C CG . ASN A 11 ? 1.5301 1.3358 1.0499 0.4885 -0.0853 -0.0603 11 ASN A CG 85 O OD1 . ASN A 11 ? 1.4737 1.3460 1.0532 0.4644 -0.0833 -0.0648 11 ASN A OD1 86 N ND2 . ASN A 11 ? 1.7803 1.5815 1.2541 0.5419 -0.0893 -0.0628 11 ASN A ND2 87 N N . SER A 12 ? 1.0853 0.8870 0.7149 0.3480 -0.0721 -0.0527 12 SER A N 88 C CA . SER A 12 ? 1.0230 0.8308 0.6752 0.3260 -0.0681 -0.0545 12 SER A CA 89 C C . SER A 12 ? 1.0376 0.7710 0.6604 0.2981 -0.0645 -0.0478 12 SER A C 90 O O . SER A 12 ? 1.0127 0.7170 0.6276 0.2775 -0.0636 -0.0416 12 SER A O 91 C CB . SER A 12 ? 0.9433 0.8250 0.6642 0.2975 -0.0660 -0.0575 12 SER A CB 92 O OG . SER A 12 ? 0.9006 0.7909 0.6415 0.2805 -0.0623 -0.0595 12 SER A OG 93 N N . THR A 13 ? 1.0529 0.7591 0.6583 0.2971 -0.0625 -0.0493 13 THR A N 94 C CA . THR A 13 ? 1.0716 0.7182 0.6535 0.2662 -0.0591 -0.0443 13 THR A CA 95 C C . THR A 13 ? 1.0321 0.7188 0.6624 0.2390 -0.0556 -0.0463 13 THR A C 96 O O . THR A 13 ? 1.0577 0.7079 0.6752 0.2126 -0.0529 -0.0430 13 THR A O 97 C CB . THR A 13 ? 1.1665 0.7320 0.6739 0.2865 -0.0596 -0.0441 13 THR A CB 98 O OG1 . THR A 13 ? 1.1817 0.7731 0.6901 0.3178 -0.0606 -0.0512 13 THR A OG1 99 C CG2 . THR A 13 ? 1.2165 0.7256 0.6641 0.3110 -0.0625 -0.0406 13 THR A CG2 100 N N . GLU A 14 ? 0.9774 0.7389 0.6602 0.2442 -0.0557 -0.0518 14 GLU A N 101 C CA . GLU A 14 ? 0.9346 0.7357 0.6634 0.2188 -0.0522 -0.0534 14 GLU A CA 102 C C . GLU A 14 ? 0.8924 0.6880 0.6415 0.1815 -0.0494 -0.0472 14 GLU A C 103 O O . GLU A 14 ? 0.8956 0.6964 0.6517 0.1756 -0.0500 -0.0438 14 GLU A O 104 C CB . GLU A 14 ? 0.9293 0.8097 0.7075 0.2256 -0.0526 -0.0595 14 GLU A CB 105 C CG . GLU A 14 ? 0.9821 0.8914 0.7508 0.2619 -0.0551 -0.0665 14 GLU A CG 106 C CD . GLU A 14 ? 1.0411 0.9392 0.7979 0.2684 -0.0531 -0.0696 14 GLU A CD 107 O OE1 . GLU A 14 ? 1.0398 0.9448 0.8216 0.2412 -0.0496 -0.0689 14 GLU A OE1 108 O OE2 . GLU A 14 ? 1.1527 1.0339 0.8722 0.3029 -0.0552 -0.0728 14 GLU A OE2 109 N N . GLN A 15 ? 0.8561 0.6456 0.6147 0.1583 -0.0463 -0.0458 15 GLN A N 110 C CA . GLN A 15 ? 0.8156 0.6039 0.5905 0.1253 -0.0434 -0.0398 15 GLN A CA 111 C C . GLN A 15 ? 0.7656 0.5997 0.5857 0.1095 -0.0403 -0.0414 15 GLN A C 112 O O . GLN A 15 ? 0.7571 0.6035 0.5835 0.1164 -0.0398 -0.0460 15 GLN A O 113 C CB . GLN A 15 ? 0.8754 0.6042 0.6072 0.1089 -0.0426 -0.0353 15 GLN A CB 114 C CG . GLN A 15 ? 0.9691 0.6361 0.6425 0.1225 -0.0450 -0.0333 15 GLN A CG 115 C CD . GLN A 15 ? 1.0452 0.6517 0.6727 0.0975 -0.0436 -0.0284 15 GLN A CD 116 O OE1 . GLN A 15 ? 1.1394 0.7022 0.7283 0.0909 -0.0440 -0.0238 15 GLN A OE1 117 N NE2 . GLN A 15 ? 1.0613 0.6655 0.6908 0.0814 -0.0420 -0.0296 15 GLN A NE2 118 N N . VAL A 16 ? 0.7237 0.5806 0.5715 0.0897 -0.0381 -0.0374 16 VAL A N 119 C CA . VAL A 16 ? 0.6641 0.5562 0.5474 0.0750 -0.0348 -0.0378 16 VAL A CA 120 C C . VAL A 16 ? 0.6623 0.5480 0.5472 0.0513 -0.0324 -0.0310 16 VAL A C 121 O O . VAL A 16 ? 0.6614 0.5269 0.5286 0.0447 -0.0329 -0.0263 16 VAL A O 122 C CB . VAL A 16 ? 0.6279 0.5642 0.5449 0.0786 -0.0340 -0.0408 16 VAL A CB 123 C CG1 . VAL A 16 ? 0.6414 0.5953 0.5581 0.1004 -0.0366 -0.0478 16 VAL A CG1 124 C CG2 . VAL A 16 ? 0.6211 0.5600 0.5427 0.0730 -0.0339 -0.0367 16 VAL A CG2 125 N N . ASP A 17 ? 0.6643 0.5703 0.5693 0.0392 -0.0296 -0.0305 17 ASP A N 126 C CA . ASP A 17 ? 0.6587 0.5721 0.5696 0.0191 -0.0272 -0.0243 17 ASP A CA 127 C C . ASP A 17 ? 0.6218 0.5710 0.5634 0.0184 -0.0244 -0.0229 17 ASP A C 128 O O . ASP A 17 ? 0.5682 0.5355 0.5275 0.0267 -0.0236 -0.0272 17 ASP A O 129 C CB . ASP A 17 ? 0.6746 0.5850 0.5816 0.0073 -0.0262 -0.0240 17 ASP A CB 130 C CG . ASP A 17 ? 0.7541 0.6204 0.6216 0.0021 -0.0285 -0.0241 17 ASP A CG 131 O OD1 . ASP A 17 ? 0.8110 0.6469 0.6510 0.0021 -0.0301 -0.0222 17 ASP A OD1 132 O OD2 . ASP A 17 ? 0.8000 0.6581 0.6598 -0.0027 -0.0284 -0.0262 17 ASP A OD2 133 N N . THR A 18 ? 0.6386 0.5963 0.5821 0.0079 -0.0227 -0.0170 18 THR A N 134 C CA . THR A 18 ? 0.6165 0.6031 0.5814 0.0081 -0.0195 -0.0146 18 THR A CA 135 C C . THR A 18 ? 0.6409 0.6439 0.6072 -0.0053 -0.0173 -0.0088 18 THR A C 136 O O . THR A 18 ? 0.6658 0.6583 0.6172 -0.0180 -0.0185 -0.0071 18 THR A O 137 C CB . THR A 18 ? 0.6013 0.5894 0.5661 0.0132 -0.0195 -0.0130 18 THR A CB 138 O OG1 . THR A 18 ? 0.6337 0.6134 0.5828 0.0028 -0.0198 -0.0075 18 THR A OG1 139 C CG2 . THR A 18 ? 0.6014 0.5771 0.5620 0.0256 -0.0226 -0.0185 18 THR A CG2 140 N N . ILE A 19 ? 0.6594 0.6881 0.6400 -0.0022 -0.0141 -0.0059 19 ILE A N 141 C CA . ILE A 19 ? 0.6655 0.7205 0.6489 -0.0109 -0.0119 -0.0003 19 ILE A CA 142 C C . ILE A 19 ? 0.6799 0.7401 0.6512 -0.0249 -0.0124 0.0049 19 ILE A C 143 O O . ILE A 19 ? 0.6846 0.7572 0.6492 -0.0410 -0.0125 0.0080 19 ILE A O 144 C CB . ILE A 19 ? 0.7160 0.7946 0.7113 0.0015 -0.0082 0.0020 19 ILE A CB 145 C CG1 . ILE A 19 ? 0.7400 0.8107 0.7416 0.0110 -0.0070 -0.0026 19 ILE A CG1 146 C CG2 . ILE A 19 ? 0.7413 0.8554 0.7389 -0.0031 -0.0061 0.0082 19 ILE A CG2 147 C CD1 . ILE A 19 ? 0.7228 0.8031 0.7270 0.0065 -0.0067 -0.0022 19 ILE A CD1 148 N N . MET A 20 ? 0.6814 0.7333 0.6483 -0.0206 -0.0125 0.0058 20 MET A N 149 C CA . MET A 20 ? 0.6844 0.7430 0.6390 -0.0341 -0.0120 0.0112 20 MET A CA 150 C C . MET A 20 ? 0.7014 0.7208 0.6294 -0.0465 -0.0150 0.0104 20 MET A C 151 O O . MET A 20 ? 0.7135 0.7328 0.6244 -0.0641 -0.0145 0.0149 20 MET A O 152 C CB . MET A 20 ? 0.6961 0.7645 0.6562 -0.0225 -0.0101 0.0131 20 MET A CB 153 C CG . MET A 20 ? 0.7053 0.8098 0.6811 -0.0105 -0.0063 0.0156 20 MET A CG 154 S SD . MET A 20 ? 0.7482 0.8633 0.7224 -0.0008 -0.0038 0.0189 20 MET A SD 155 C CE . MET A 20 ? 0.7710 0.9394 0.7536 0.0061 0.0009 0.0248 20 MET A CE 156 N N . GLU A 21 ? 0.7047 0.6902 0.6253 -0.0367 -0.0179 0.0048 21 GLU A N 157 C CA . GLU A 21 ? 0.7436 0.6847 0.6323 -0.0417 -0.0208 0.0038 21 GLU A CA 158 C C . GLU A 21 ? 0.7309 0.6442 0.6105 -0.0329 -0.0234 -0.0022 21 GLU A C 159 O O . GLU A 21 ? 0.6967 0.6207 0.5963 -0.0162 -0.0238 -0.0070 21 GLU A O 160 C CB . GLU A 21 ? 0.7657 0.6936 0.6490 -0.0295 -0.0217 0.0038 21 GLU A CB 161 C CG . GLU A 21 ? 0.8525 0.7346 0.6956 -0.0367 -0.0238 0.0055 21 GLU A CG 162 C CD . GLU A 21 ? 0.8977 0.7683 0.7349 -0.0229 -0.0250 0.0057 21 GLU A CD 163 O OE1 . GLU A 21 ? 0.8371 0.7387 0.7022 -0.0115 -0.0239 0.0050 21 GLU A OE1 164 O OE2 . GLU A 21 ? 0.9032 0.7302 0.7034 -0.0235 -0.0270 0.0067 21 GLU A OE2 165 N N . LYS A 22 ? 0.7711 0.6475 0.6167 -0.0453 -0.0250 -0.0020 22 LYS A N 166 C CA . LYS A 22 ? 0.8149 0.6608 0.6448 -0.0356 -0.0273 -0.0076 22 LYS A CA 167 C C . LYS A 22 ? 0.8219 0.6196 0.6163 -0.0224 -0.0300 -0.0094 22 LYS A C 168 O O . LYS A 22 ? 0.8228 0.5997 0.5939 -0.0303 -0.0300 -0.0053 22 LYS A O 169 C CB . LYS A 22 ? 0.8859 0.7197 0.6968 -0.0575 -0.0270 -0.0067 22 LYS A CB 170 C CG . LYS A 22 ? 0.9084 0.7918 0.7533 -0.0660 -0.0248 -0.0055 22 LYS A CG 171 C CD . LYS A 22 ? 1.0347 0.9092 0.8582 -0.0910 -0.0250 -0.0044 22 LYS A CD 172 C CE . LYS A 22 ? 1.0581 0.9734 0.9110 -0.0918 -0.0239 -0.0052 22 LYS A CE 173 N NZ . LYS A 22 ? 1.0977 0.9957 0.9261 -0.1117 -0.0251 -0.0064 22 LYS A NZ 174 N N . ASN A 23 ? 0.8282 0.6104 0.6170 -0.0006 -0.0322 -0.0154 23 ASN A N 175 C CA . ASN A 23 ? 0.8921 0.6280 0.6421 0.0182 -0.0351 -0.0176 23 ASN A CA 176 C C . ASN A 23 ? 0.8589 0.6008 0.6129 0.0304 -0.0361 -0.0160 23 ASN A C 177 O O . ASN A 23 ? 0.8907 0.5900 0.6050 0.0317 -0.0374 -0.0133 23 ASN A O 178 C CB . ASN A 23 ? 1.0086 0.6825 0.7012 0.0021 -0.0355 -0.0150 23 ASN A CB 179 C CG . ASN A 23 ? 1.0889 0.7488 0.7697 -0.0059 -0.0353 -0.0180 23 ASN A CG 180 O OD1 . ASN A 23 ? 1.0602 0.7533 0.7734 0.0055 -0.0351 -0.0224 23 ASN A OD1 181 N ND2 . ASN A 23 ? 1.2524 0.8609 0.8834 -0.0275 -0.0352 -0.0157 23 ASN A ND2 182 N N . VAL A 24 ? 0.8089 0.6004 0.6072 0.0387 -0.0355 -0.0177 24 VAL A N 183 C CA . VAL A 24 ? 0.7710 0.5740 0.5770 0.0521 -0.0368 -0.0177 24 VAL A CA 184 C C . VAL A 24 ? 0.7741 0.5702 0.5693 0.0814 -0.0405 -0.0238 24 VAL A C 185 O O . VAL A 24 ? 0.7582 0.5813 0.5747 0.0917 -0.0408 -0.0293 24 VAL A O 186 C CB . VAL A 24 ? 0.7294 0.5848 0.5819 0.0490 -0.0346 -0.0182 24 VAL A CB 187 C CG1 . VAL A 24 ? 0.7288 0.5964 0.5881 0.0627 -0.0364 -0.0193 24 VAL A CG1 188 C CG2 . VAL A 24 ? 0.7196 0.5894 0.5831 0.0258 -0.0309 -0.0121 24 VAL A CG2 189 N N . THR A 25 ? 0.7935 0.5562 0.5542 0.0955 -0.0432 -0.0226 25 THR A N 190 C CA . THR A 25 ? 0.8013 0.5637 0.5499 0.1277 -0.0470 -0.0282 25 THR A CA 191 C C . THR A 25 ? 0.7589 0.5775 0.5480 0.1373 -0.0482 -0.0320 25 THR A C 192 O O . THR A 25 ? 0.7603 0.5898 0.5608 0.1290 -0.0477 -0.0288 25 THR A O 193 C CB . THR A 25 ? 0.8680 0.5754 0.5624 0.1433 -0.0497 -0.0255 25 THR A CB 194 O OG1 . THR A 25 ? 0.9447 0.5919 0.5942 0.1268 -0.0481 -0.0211 25 THR A OG1 195 C CG2 . THR A 25 ? 0.9088 0.6146 0.5842 0.1811 -0.0537 -0.0314 25 THR A CG2 196 N N . VAL A 26 ? 0.7304 0.5845 0.5380 0.1539 -0.0496 -0.0389 26 VAL A N 197 C CA . VAL A 26 ? 0.6841 0.5935 0.5271 0.1589 -0.0507 -0.0435 26 VAL A CA 198 C C . VAL A 26 ? 0.6975 0.6269 0.5303 0.1900 -0.0551 -0.0494 26 VAL A C 199 O O . VAL A 26 ? 0.7626 0.6712 0.5681 0.2099 -0.0566 -0.0513 26 VAL A O 200 C CB . VAL A 26 ? 0.6359 0.5862 0.5186 0.1423 -0.0474 -0.0467 26 VAL A CB 201 C CG1 . VAL A 26 ? 0.6232 0.5627 0.5176 0.1157 -0.0432 -0.0408 26 VAL A CG1 202 C CG2 . VAL A 26 ? 0.6473 0.6015 0.5276 0.1505 -0.0470 -0.0510 26 VAL A CG2 203 N N . THR A 27 ? 0.6914 0.6639 0.5453 0.1944 -0.0572 -0.0527 27 THR A N 204 C CA . THR A 27 ? 0.6984 0.7031 0.5460 0.2238 -0.0619 -0.0584 27 THR A CA 205 C C . THR A 27 ? 0.6911 0.7398 0.5560 0.2317 -0.0615 -0.0655 27 THR A C 206 O O . THR A 27 ? 0.7320 0.7936 0.5791 0.2621 -0.0647 -0.0694 27 THR A O 207 C CB . THR A 27 ? 0.6836 0.7299 0.5519 0.2209 -0.0642 -0.0606 27 THR A CB 208 O OG1 . THR A 27 ? 0.6399 0.7244 0.5468 0.1938 -0.0609 -0.0634 27 THR A OG1 209 C CG2 . THR A 27 ? 0.7039 0.7091 0.5529 0.2166 -0.0646 -0.0537 27 THR A CG2 210 N N . HIS A 28 ? 0.6575 0.7301 0.5550 0.2058 -0.0574 -0.0670 28 HIS A N 211 C CA . HIS A 28 ? 0.6351 0.7490 0.5502 0.2076 -0.0561 -0.0733 28 HIS A CA 212 C C . HIS A 28 ? 0.6190 0.7197 0.5502 0.1811 -0.0508 -0.0712 28 HIS A C 213 O O . HIS A 28 ? 0.5781 0.6632 0.5206 0.1573 -0.0481 -0.0668 28 HIS A O 214 C CB . HIS A 28 ? 0.6193 0.8042 0.5627 0.2039 -0.0573 -0.0802 28 HIS A CB 215 C CG . HIS A 28 ? 0.6372 0.8441 0.5697 0.2265 -0.0628 -0.0822 28 HIS A CG 216 N ND1 . HIS A 28 ? 0.6303 0.8207 0.5594 0.2198 -0.0644 -0.0786 28 HIS A ND1 217 C CD2 . HIS A 28 ? 0.6413 0.8875 0.5640 0.2578 -0.0671 -0.0873 28 HIS A CD2 218 C CE1 . HIS A 28 ? 0.6440 0.8610 0.5620 0.2449 -0.0697 -0.0814 28 HIS A CE1 219 N NE2 . HIS A 28 ? 0.6440 0.8966 0.5578 0.2692 -0.0715 -0.0867 28 HIS A NE2 220 N N . ALA A 29 ? 0.6294 0.7396 0.5605 0.1876 -0.0494 -0.0745 29 ALA A N 221 C CA . ALA A 29 ? 0.6272 0.7265 0.5707 0.1664 -0.0448 -0.0730 29 ALA A CA 222 C C . ALA A 29 ? 0.6237 0.7640 0.5788 0.1727 -0.0434 -0.0795 29 ALA A C 223 O O . ALA A 29 ? 0.6566 0.8277 0.6046 0.1976 -0.0462 -0.0847 29 ALA A O 224 C CB . ALA A 29 ? 0.6621 0.6992 0.5776 0.1663 -0.0442 -0.0671 29 ALA A CB 225 N N . GLN A 30 ? 0.6053 0.7486 0.5771 0.1514 -0.0390 -0.0792 30 GLN A N 226 C CA . GLN A 30 ? 0.6255 0.8068 0.6088 0.1531 -0.0368 -0.0849 30 GLN A CA 227 C C . GLN A 30 ? 0.6280 0.7764 0.6061 0.1446 -0.0335 -0.0822 30 GLN A C 228 O O . GLN A 30 ? 0.5727 0.7053 0.5617 0.1210 -0.0303 -0.0782 30 GLN A O 229 C CB . GLN A 30 ? 0.6156 0.8481 0.6272 0.1311 -0.0342 -0.0889 30 GLN A CB 230 C CG . GLN A 30 ? 0.6339 0.9124 0.6574 0.1294 -0.0314 -0.0950 30 GLN A CG 231 C CD . GLN A 30 ? 0.6386 0.9677 0.6829 0.1051 -0.0289 -0.0995 30 GLN A CD 232 O OE1 . GLN A 30 ? 0.6820 1.0238 0.7302 0.0976 -0.0308 -0.1002 30 GLN A OE1 233 N NE2 . GLN A 30 ? 0.6514 1.0069 0.7057 0.0909 -0.0245 -0.1027 30 GLN A NE2 234 N N . ASP A 31 ? 0.6749 0.8129 0.6332 0.1661 -0.0345 -0.0845 31 ASP A N 235 C CA . ASP A 31 ? 0.6948 0.8071 0.6463 0.1599 -0.0317 -0.0833 31 ASP A CA 236 C C . ASP A 31 ? 0.6622 0.8211 0.6418 0.1444 -0.0275 -0.0871 31 ASP A C 237 O O . ASP A 31 ? 0.6383 0.8505 0.6302 0.1516 -0.0273 -0.0930 31 ASP A O 238 C CB . ASP A 31 ? 0.7375 0.8254 0.6547 0.1899 -0.0339 -0.0858 31 ASP A CB 239 C CG . ASP A 31 ? 0.7673 0.8177 0.6698 0.1832 -0.0318 -0.0843 31 ASP A CG 240 O OD1 . ASP A 31 ? 0.7409 0.7885 0.6621 0.1565 -0.0288 -0.0812 31 ASP A OD1 241 O OD2 . ASP A 31 ? 0.8623 0.8843 0.7310 0.2065 -0.0332 -0.0864 31 ASP A OD2 242 N N . ILE A 32 ? 0.6365 0.7771 0.6240 0.1227 -0.0239 -0.0837 32 ILE A N 243 C CA . ILE A 32 ? 0.6117 0.7869 0.6200 0.1063 -0.0193 -0.0864 32 ILE A CA 244 C C . ILE A 32 ? 0.6225 0.7804 0.6241 0.1052 -0.0169 -0.0860 32 ILE A C 245 O O . ILE A 32 ? 0.5858 0.7615 0.6014 0.0889 -0.0127 -0.0867 32 ILE A O 246 C CB . ILE A 32 ? 0.5808 0.7559 0.6054 0.0792 -0.0164 -0.0828 32 ILE A CB 247 C CG1 . ILE A 32 ? 0.5794 0.7069 0.5964 0.0703 -0.0164 -0.0753 32 ILE A CG1 248 C CG2 . ILE A 32 ? 0.5805 0.7788 0.6122 0.0775 -0.0183 -0.0845 32 ILE A CG2 249 C CD1 . ILE A 32 ? 0.5812 0.7062 0.6094 0.0487 -0.0130 -0.0715 32 ILE A CD1 250 N N . LEU A 33 ? 0.6439 0.7639 0.6201 0.1215 -0.0195 -0.0851 33 LEU A N 251 C CA . LEU A 33 ? 0.6638 0.7622 0.6287 0.1209 -0.0178 -0.0850 33 LEU A CA 252 C C . LEU A 33 ? 0.7154 0.8160 0.6581 0.1498 -0.0192 -0.0907 33 LEU A C 253 O O . LEU A 33 ? 0.7548 0.8260 0.6691 0.1708 -0.0229 -0.0908 33 LEU A O 254 C CB . LEU A 33 ? 0.6734 0.7174 0.6206 0.1105 -0.0194 -0.0787 33 LEU A CB 255 C CG . LEU A 33 ? 0.6839 0.7021 0.6173 0.1053 -0.0182 -0.0782 33 LEU A CG 256 C CD1 . LEU A 33 ? 0.6348 0.6795 0.5939 0.0867 -0.0139 -0.0774 33 LEU A CD1 257 C CD2 . LEU A 33 ? 0.7258 0.6940 0.6365 0.0947 -0.0206 -0.0727 33 LEU A CD2 258 N N . GLU A 34 ? 0.7372 0.8704 0.6889 0.1522 -0.0160 -0.0951 34 GLU A N 259 C CA . GLU A 34 ? 0.7661 0.9016 0.6946 0.1816 -0.0166 -0.1006 34 GLU A CA 260 C C . GLU A 34 ? 0.7891 0.8623 0.6850 0.1838 -0.0173 -0.0986 34 GLU A C 261 O O . GLU A 34 ? 0.7611 0.8232 0.6655 0.1622 -0.0149 -0.0961 34 GLU A O 262 C CB . GLU A 34 ? 0.7579 0.9556 0.7077 0.1822 -0.0123 -0.1062 34 GLU A CB 263 C CG . GLU A 34 ? 0.7936 1.0041 0.7202 0.2174 -0.0127 -0.1123 34 GLU A CG 264 C CD . GLU A 34 ? 0.8401 1.0437 0.7419 0.2508 -0.0173 -0.1141 34 GLU A CD 265 O OE1 . GLU A 34 ? 0.8575 1.1116 0.7784 0.2540 -0.0184 -0.1159 34 GLU A OE1 266 O OE2 . GLU A 34 ? 0.9050 1.0496 0.7646 0.2728 -0.0199 -0.1135 34 GLU A OE2 267 N N . LYS A 35 ? 0.8524 0.8834 0.7072 0.2097 -0.0207 -0.0997 35 LYS A N 268 C CA . LYS A 35 ? 0.8957 0.8575 0.7097 0.2094 -0.0219 -0.0980 35 LYS A CA 269 C C . LYS A 35 ? 0.9244 0.8734 0.7042 0.2393 -0.0213 -0.1040 35 LYS A C 270 O O . LYS A 35 ? 0.9616 0.8554 0.7069 0.2361 -0.0216 -0.1036 35 LYS A O 271 C CB . LYS A 35 ? 0.9422 0.8451 0.7224 0.2106 -0.0258 -0.0938 35 LYS A CB 272 C CG . LYS A 35 ? 0.9303 0.8212 0.7299 0.1754 -0.0261 -0.0867 35 LYS A CG 273 C CD . LYS A 35 ? 0.9796 0.8216 0.7479 0.1767 -0.0295 -0.0827 35 LYS A CD 274 C CE . LYS A 35 ? 0.9632 0.8411 0.7608 0.1760 -0.0305 -0.0806 35 LYS A CE 275 N NZ . LYS A 35 ? 0.9534 0.8855 0.7682 0.2018 -0.0305 -0.0862 35 LYS A NZ 276 N N . THR A 36 ? 0.9178 0.9194 0.7054 0.2676 -0.0204 -0.1097 36 THR A N 277 C CA . THR A 36 ? 0.9954 0.9890 0.7472 0.3033 -0.0198 -0.1156 36 THR A CA 278 C C . THR A 36 ? 0.9734 1.0310 0.7553 0.3025 -0.0151 -0.1203 36 THR A C 279 O O . THR A 36 ? 0.8910 1.0140 0.7210 0.2827 -0.0126 -0.1203 36 THR A O 280 C CB . THR A 36 ? 1.0492 1.0557 0.7765 0.3464 -0.0225 -0.1191 36 THR A CB 281 O OG1 . THR A 36 ? 1.0287 1.1255 0.8036 0.3468 -0.0215 -0.1215 36 THR A OG1 282 C CG2 . THR A 36 ? 1.0849 1.0242 0.7766 0.3493 -0.0269 -0.1144 36 THR A CG2 283 N N . HIS A 37 ? 1.0130 1.0466 0.7611 0.3237 -0.0138 -0.1244 37 HIS A N 284 C CA . HIS A 37 ? 0.9998 1.0912 0.7662 0.3313 -0.0092 -0.1296 37 HIS A CA 285 C C . HIS A 37 ? 1.0676 1.1436 0.7843 0.3810 -0.0096 -0.1358 37 HIS A C 286 O O . HIS A 37 ? 1.1210 1.1259 0.7849 0.4031 -0.0132 -0.1351 37 HIS A O 287 C CB . HIS A 37 ? 0.9931 1.0641 0.7700 0.2990 -0.0063 -0.1275 37 HIS A CB 288 C CG . HIS A 37 ? 1.0633 1.0437 0.7905 0.2979 -0.0088 -0.1259 37 HIS A CG 289 N ND1 . HIS A 37 ? 1.1059 1.0563 0.7947 0.3178 -0.0074 -0.1304 37 HIS A ND1 290 C CD2 . HIS A 37 ? 1.0980 1.0121 0.8049 0.2774 -0.0123 -0.1205 37 HIS A CD2 291 C CE1 . HIS A 37 ? 1.1479 1.0144 0.7931 0.3076 -0.0102 -0.1281 37 HIS A CE1 292 N NE2 . HIS A 37 ? 1.1544 1.0000 0.8104 0.2822 -0.0131 -0.1220 37 HIS A NE2 293 N N . ASN A 38 ? 1.0575 1.1976 0.7870 0.3990 -0.0055 -0.1415 38 ASN A N 294 C CA . ASN A 38 ? 1.0941 1.2295 0.7766 0.4520 -0.0054 -0.1478 38 ASN A CA 295 C C . ASN A 38 ? 1.1426 1.2105 0.7793 0.4599 -0.0039 -0.1498 38 ASN A C 296 O O . ASN A 38 ? 1.2000 1.2473 0.7874 0.5049 -0.0037 -0.1548 38 ASN A O 297 C CB . ASN A 38 ? 1.0489 1.2968 0.7642 0.4737 -0.0019 -0.1537 38 ASN A CB 298 C CG . ASN A 38 ? 1.0004 1.3024 0.7517 0.4495 0.0042 -0.1558 38 ASN A CG 299 O OD1 . ASN A 38 ? 1.0159 1.2770 0.7748 0.4143 0.0056 -0.1523 38 ASN A OD1 300 N ND2 . ASN A 38 ? 0.9618 1.3601 0.7350 0.4679 0.0079 -0.1614 38 ASN A ND2 301 N N . GLY A 39 ? 1.1351 1.1706 0.7864 0.4174 -0.0029 -0.1461 39 GLY A N 302 C CA . GLY A 39 ? 1.1844 1.1458 0.7900 0.4170 -0.0025 -0.1472 39 GLY A CA 303 C C . GLY A 39 ? 1.1855 1.1886 0.7950 0.4312 0.0026 -0.1529 39 GLY A C 304 O O . GLY A 39 ? 1.1798 1.1235 0.7424 0.4420 0.0030 -0.1556 39 GLY A O 305 N N . LYS A 40 ? 1.1520 1.2560 0.8151 0.4285 0.0066 -0.1548 40 LYS A N 306 C CA . LYS A 40 ? 1.1498 1.3094 0.8183 0.4464 0.0121 -0.1607 40 LYS A CA 307 C C . LYS A 40 ? 1.0926 1.3243 0.8229 0.4056 0.0171 -0.1590 40 LYS A C 308 O O . LYS A 40 ? 1.0535 1.3175 0.8275 0.3729 0.0168 -0.1546 40 LYS A O 309 C CB . LYS A 40 ? 1.1687 1.3911 0.8275 0.4969 0.0129 -0.1666 40 LYS A CB 310 C CG . LYS A 40 ? 1.2602 1.4071 0.8464 0.5459 0.0088 -0.1690 40 LYS A CG 311 C CD . LYS A 40 ? 1.2762 1.4893 0.8537 0.5987 0.0088 -0.1739 40 LYS A CD 312 C CE . LYS A 40 ? 1.3791 1.5025 0.8749 0.6489 0.0048 -0.1755 40 LYS A CE 313 N NZ . LYS A 40 ? 1.4345 1.6203 0.9100 0.7118 0.0055 -0.1814 40 LYS A NZ 314 N N . LEU A 41 ? 1.1115 1.3629 0.8402 0.4082 0.0219 -0.1626 41 LEU A N 315 C CA . LEU A 41 ? 1.0675 1.3940 0.8472 0.3768 0.0278 -0.1620 41 LEU A CA 316 C C . LEU A 41 ? 1.0249 1.4549 0.8251 0.4010 0.0318 -0.1677 41 LEU A C 317 O O . LEU A 41 ? 1.0583 1.5029 0.8270 0.4473 0.0326 -0.1737 41 LEU A O 318 C CB . LEU A 41 ? 1.0942 1.3951 0.8612 0.3678 0.0313 -0.1631 41 LEU A CB 319 C CG . LEU A 41 ? 1.1397 1.3457 0.8847 0.3432 0.0272 -0.1581 41 LEU A CG 320 C CD1 . LEU A 41 ? 1.1677 1.3576 0.9000 0.3369 0.0306 -0.1600 41 LEU A CD1 321 C CD2 . LEU A 41 ? 1.1024 1.3058 0.8865 0.2981 0.0254 -0.1504 41 LEU A CD2 322 N N . CYS A 42 ? 0.9621 1.4640 0.8119 0.3697 0.0344 -0.1658 42 CYS A N 323 C CA . CYS A 42 ? 0.9652 1.5714 0.8371 0.3861 0.0372 -0.1708 42 CYS A CA 324 C C . CYS A 42 ? 0.8764 1.5630 0.7915 0.3476 0.0443 -0.1710 42 CYS A C 325 O O . CYS A 42 ? 0.8169 1.4741 0.7484 0.3049 0.0463 -0.1660 42 CYS A O 326 C CB . CYS A 42 ? 1.0044 1.6210 0.8875 0.3871 0.0320 -0.1689 42 CYS A CB 327 S SG . CYS A 42 ? 1.0941 1.6097 0.9233 0.4268 0.0237 -0.1675 42 CYS A SG 328 N N . ASP A 43 ? 0.8611 1.6508 0.7919 0.3628 0.0482 -0.1768 43 ASP A N 329 C CA . ASP A 43 ? 0.8284 1.7030 0.7985 0.3221 0.0550 -0.1774 43 ASP A CA 330 C C . ASP A 43 ? 0.7925 1.6559 0.7893 0.2767 0.0530 -0.1719 43 ASP A C 331 O O . ASP A 43 ? 0.7963 1.6454 0.7917 0.2877 0.0470 -0.1708 43 ASP A O 332 C CB . ASP A 43 ? 0.8355 1.8318 0.8174 0.3461 0.0586 -0.1848 43 ASP A CB 333 C CG . ASP A 43 ? 0.8713 1.8888 0.8255 0.3954 0.0614 -0.1908 43 ASP A CG 334 O OD1 . ASP A 43 ? 0.8787 1.8351 0.8129 0.3962 0.0633 -0.1896 43 ASP A OD1 335 O OD2 . ASP A 43 ? 0.9027 2.0006 0.8533 0.4353 0.0616 -0.1969 43 ASP A OD2 336 N N . LEU A 44 ? 0.7921 1.6563 0.8088 0.2274 0.0581 -0.1682 44 LEU A N 337 C CA . LEU A 44 ? 0.7932 1.6550 0.8320 0.1831 0.0577 -0.1637 44 LEU A CA 338 C C . LEU A 44 ? 0.8040 1.7759 0.8667 0.1624 0.0629 -0.1684 44 LEU A C 339 O O . LEU A 44 ? 0.7976 1.8208 0.8673 0.1434 0.0704 -0.1706 44 LEU A O 340 C CB . LEU A 44 ? 0.7870 1.5842 0.8268 0.1422 0.0605 -0.1569 44 LEU A CB 341 C CG . LEU A 44 ? 0.7987 1.5766 0.8530 0.0982 0.0604 -0.1515 44 LEU A CG 342 C CD1 . LEU A 44 ? 0.8167 1.5455 0.8676 0.1115 0.0521 -0.1486 44 LEU A CD1 343 C CD2 . LEU A 44 ? 0.7978 1.5175 0.8475 0.0644 0.0640 -0.1451 44 LEU A CD2 344 N N . ASP A 45 ? 0.8449 1.8556 0.9186 0.1654 0.0589 -0.1702 45 ASP A N 345 C CA . ASP A 45 ? 0.8470 1.9626 0.9430 0.1390 0.0630 -0.1746 45 ASP A CA 346 C C . ASP A 45 ? 0.8112 2.0259 0.9106 0.1569 0.0691 -0.1817 45 ASP A C 347 O O . ASP A 45 ? 0.7658 2.0525 0.8797 0.1193 0.0763 -0.1840 45 ASP A O 348 C CB . ASP A 45 ? 0.8875 1.9817 0.9928 0.0757 0.0679 -0.1700 45 ASP A CB 349 C CG . ASP A 45 ? 0.9255 2.1067 1.0480 0.0403 0.0706 -0.1738 45 ASP A CG 350 O OD1 . ASP A 45 ? 0.9983 2.1952 1.1273 0.0483 0.0648 -0.1750 45 ASP A OD1 351 O OD2 . ASP A 45 ? 0.9488 2.1811 1.0760 0.0021 0.0787 -0.1756 45 ASP A OD2 352 N N . GLY A 46 ? 0.8032 2.0174 0.8849 0.2143 0.0664 -0.1851 46 GLY A N 353 C CA . GLY A 46 ? 0.7811 2.0843 0.8614 0.2418 0.0717 -0.1919 46 GLY A CA 354 C C . GLY A 46 ? 0.7805 2.0487 0.8488 0.2380 0.0777 -0.1907 46 GLY A C 355 O O . GLY A 46 ? 0.7767 2.0803 0.8313 0.2789 0.0800 -0.1956 46 GLY A O 356 N N . VAL A 47 ? 0.7419 1.9403 0.8126 0.1916 0.0801 -0.1844 47 VAL A N 357 C CA . VAL A 47 ? 0.7210 1.8908 0.7826 0.1798 0.0862 -0.1828 47 VAL A CA 358 C C . VAL A 47 ? 0.7429 1.8068 0.7763 0.2138 0.0812 -0.1800 47 VAL A C 359 O O . VAL A 47 ? 0.7450 1.7173 0.7721 0.2016 0.0760 -0.1739 47 VAL A O 360 C CB . VAL A 47 ? 0.6957 1.8371 0.7678 0.1156 0.0912 -0.1768 47 VAL A CB 361 C CG1 . VAL A 47 ? 0.7191 1.8354 0.7806 0.1048 0.0977 -0.1751 47 VAL A CG1 362 C CG2 . VAL A 47 ? 0.6710 1.9071 0.7641 0.0751 0.0963 -0.1796 47 VAL A CG2 363 N N . LYS A 48 ? 0.7725 1.8507 0.7869 0.2547 0.0831 -0.1847 48 LYS A N 364 C CA . LYS A 48 ? 0.8132 1.7942 0.7934 0.2897 0.0783 -0.1836 48 LYS A CA 365 C C . LYS A 48 ? 0.8023 1.6979 0.7774 0.2556 0.0794 -0.1772 48 LYS A C 366 O O . LYS A 48 ? 0.7901 1.7137 0.7797 0.2195 0.0863 -0.1756 48 LYS A O 367 C CB . LYS A 48 ? 0.8507 1.8717 0.8076 0.3413 0.0811 -0.1908 48 LYS A CB 368 C CG . LYS A 48 ? 0.9165 1.8378 0.8284 0.3834 0.0757 -0.1911 48 LYS A CG 369 C CD . LYS A 48 ? 0.9632 1.9152 0.8465 0.4322 0.0795 -0.1982 48 LYS A CD 370 C CE . LYS A 48 ? 1.0215 1.8570 0.8550 0.4609 0.0749 -0.1979 48 LYS A CE 371 N NZ . LYS A 48 ? 1.1038 1.9545 0.8971 0.5202 0.0771 -0.2053 48 LYS A NZ 372 N N . PRO A 49 ? 0.8104 1.6028 0.7624 0.2664 0.0725 -0.1733 49 PRO A N 373 C CA . PRO A 49 ? 0.7961 1.5134 0.7410 0.2394 0.0729 -0.1677 49 PRO A CA 374 C C . PRO A 49 ? 0.7989 1.5052 0.7202 0.2601 0.0763 -0.1712 49 PRO A C 375 O O . PRO A 49 ? 0.8179 1.5469 0.7178 0.3044 0.0764 -0.1777 49 PRO A O 376 C CB . PRO A 49 ? 0.7970 1.4202 0.7235 0.2471 0.0640 -0.1636 49 PRO A CB 377 C CG . PRO A 49 ? 0.8372 1.4685 0.7417 0.2958 0.0598 -0.1690 49 PRO A CG 378 C CD . PRO A 49 ? 0.8210 1.5620 0.7516 0.2999 0.0641 -0.1735 49 PRO A CD 379 N N . LEU A 50 ? 0.7796 1.4490 0.7020 0.2299 0.0791 -0.1669 50 LEU A N 380 C CA . LEU A 50 ? 0.8021 1.4439 0.6993 0.2456 0.0812 -0.1693 50 LEU A CA 381 C C . LEU A 50 ? 0.8413 1.3834 0.7046 0.2640 0.0731 -0.1680 50 LEU A C 382 O O . LEU A 50 ? 0.8516 1.3333 0.7179 0.2370 0.0690 -0.1616 50 LEU A O 383 C CB . LEU A 50 ? 0.7753 1.4178 0.6859 0.2045 0.0872 -0.1647 50 LEU A CB 384 C CG . LEU A 50 ? 0.7978 1.4053 0.6842 0.2134 0.0892 -0.1660 50 LEU A CG 385 C CD1 . LEU A 50 ? 0.8166 1.4717 0.6850 0.2553 0.0930 -0.1746 50 LEU A CD1 386 C CD2 . LEU A 50 ? 0.7818 1.3985 0.6828 0.1719 0.0956 -0.1609 50 LEU A CD2 387 N N . ILE A 51 ? 0.8948 1.4200 0.7226 0.3099 0.0710 -0.1742 51 ILE A N 388 C CA . ILE A 51 ? 0.9496 1.3756 0.7356 0.3266 0.0637 -0.1739 51 ILE A CA 389 C C . ILE A 51 ? 0.9752 1.3648 0.7309 0.3344 0.0658 -0.1767 51 ILE A C 390 O O . ILE A 51 ? 0.9844 1.3870 0.7107 0.3733 0.0683 -0.1836 51 ILE A O 391 C CB . ILE A 51 ? 0.9995 1.4100 0.7539 0.3725 0.0591 -0.1786 51 ILE A CB 392 C CG1 . ILE A 51 ? 0.9875 1.4413 0.7747 0.3634 0.0572 -0.1759 51 ILE A CG1 393 C CG2 . ILE A 51 ? 1.0444 1.3439 0.7489 0.3834 0.0519 -0.1780 51 ILE A CG2 394 C CD1 . ILE A 51 ? 1.0441 1.4550 0.8005 0.3966 0.0504 -0.1772 51 ILE A CD1 395 N N . LEU A 52 ? 0.9622 1.3057 0.7229 0.2990 0.0644 -0.1712 52 LEU A N 396 C CA . LEU A 52 ? 0.9909 1.3042 0.7282 0.2985 0.0664 -0.1730 52 LEU A CA 397 C C . LEU A 52 ? 1.0745 1.3103 0.7529 0.3309 0.0615 -0.1783 52 LEU A C 398 O O . LEU A 52 ? 1.0857 1.2992 0.7376 0.3382 0.0635 -0.1816 52 LEU A O 399 C CB . LEU A 52 ? 0.9507 1.2366 0.7079 0.2531 0.0654 -0.1654 52 LEU A CB 400 C CG . LEU A 52 ? 0.8981 1.2485 0.7020 0.2196 0.0715 -0.1602 52 LEU A CG 401 C CD1 . LEU A 52 ? 0.8701 1.1823 0.6859 0.1810 0.0694 -0.1520 52 LEU A CD1 402 C CD2 . LEU A 52 ? 0.9029 1.3215 0.7139 0.2257 0.0807 -0.1644 52 LEU A CD2 403 N N . ARG A 53 ? 1.1091 1.3002 0.7631 0.3492 0.0554 -0.1789 53 ARG A N 404 C CA . ARG A 53 ? 1.2233 1.3363 0.8119 0.3829 0.0513 -0.1844 53 ARG A CA 405 C C . ARG A 53 ? 1.2736 1.3058 0.8338 0.3573 0.0472 -0.1826 53 ARG A C 406 O O . ARG A 53 ? 1.3242 1.3238 0.8989 0.3222 0.0423 -0.1762 53 ARG A O 407 C CB . ARG A 53 ? 1.2819 1.4310 0.8431 0.4314 0.0568 -0.1929 53 ARG A CB 408 C CG . ARG A 53 ? 1.3883 1.4698 0.8805 0.4790 0.0531 -0.1988 53 ARG A CG 409 C CD . ARG A 53 ? 1.4543 1.5680 0.9143 0.5294 0.0589 -0.2073 53 ARG A CD 410 N NE . ARG A 53 ? 1.5115 1.6347 0.9413 0.5818 0.0582 -0.2117 53 ARG A NE 411 C CZ . ARG A 53 ? 1.4828 1.7014 0.9539 0.5958 0.0608 -0.2116 53 ARG A CZ 412 N NH1 . ARG A 53 ? 1.4111 1.7210 0.9539 0.5583 0.0648 -0.2075 53 ARG A NH1 413 N NH2 . ARG A 53 ? 1.5161 1.7374 0.9526 0.6476 0.0595 -0.2157 53 ARG A NH2 414 N N . ASP A 54 ? 1.3240 1.3277 0.8440 0.3741 0.0492 -0.1882 54 ASP A N 415 C CA . ASP A 54 ? 1.3526 1.2875 0.8456 0.3483 0.0454 -0.1872 54 ASP A CA 416 C C . ASP A 54 ? 1.3060 1.2857 0.8422 0.3143 0.0492 -0.1831 54 ASP A C 417 O O . ASP A 54 ? 1.3451 1.2794 0.8664 0.2899 0.0459 -0.1815 54 ASP A O 418 C CB . ASP A 54 ? 1.4444 1.3152 0.8644 0.3820 0.0452 -0.1957 54 ASP A CB 419 C CG . ASP A 54 ? 1.5172 1.3150 0.8776 0.4113 0.0404 -0.1992 54 ASP A CG 420 O OD1 . ASP A 54 ? 1.4696 1.2356 0.8353 0.3906 0.0348 -0.1942 54 ASP A OD1 421 O OD2 . ASP A 54 ? 1.6024 1.3716 0.9066 0.4561 0.0424 -0.2069 54 ASP A OD2 422 N N . CYS A 55 ? 1.2395 1.3067 0.8253 0.3116 0.0560 -0.1813 55 CYS A N 423 C CA . CYS A 55 ? 1.1997 1.3063 0.8220 0.2797 0.0603 -0.1768 55 CYS A CA 424 C C . CYS A 55 ? 1.1081 1.2219 0.7732 0.2389 0.0576 -0.1674 55 CYS A C 425 O O . CYS A 55 ? 1.0928 1.2124 0.7746 0.2367 0.0549 -0.1646 55 CYS A O 426 C CB . CYS A 55 ? 1.1818 1.3759 0.8298 0.2927 0.0700 -0.1796 55 CYS A CB 427 S SG . CYS A 55 ? 1.2987 1.4961 0.8981 0.3430 0.0746 -0.1905 55 CYS A SG 428 N N . SER A 56 ? 1.0639 1.1755 0.7431 0.2090 0.0582 -0.1625 56 SER A N 429 C CA . SER A 56 ? 0.9969 1.1221 0.7148 0.1736 0.0571 -0.1534 56 SER A CA 430 C C . SER A 56 ? 0.9481 1.1449 0.7028 0.1629 0.0660 -0.1509 56 SER A C 431 O O . SER A 56 ? 0.9526 1.1922 0.7050 0.1805 0.0726 -0.1561 56 SER A O 432 C CB . SER A 56 ? 0.9938 1.0771 0.7020 0.1493 0.0528 -0.1492 56 SER A CB 433 O OG . SER A 56 ? 0.9908 1.0968 0.6998 0.1450 0.0584 -0.1497 56 SER A OG 434 N N . VAL A 57 ? 0.9027 1.1111 0.6876 0.1333 0.0663 -0.1428 57 VAL A N 435 C CA . VAL A 57 ? 0.8631 1.1284 0.6761 0.1162 0.0748 -0.1396 57 VAL A CA 436 C C . VAL A 57 ? 0.8660 1.1387 0.6696 0.1099 0.0800 -0.1397 57 VAL A C 437 O O . VAL A 57 ? 0.8470 1.1715 0.6600 0.1079 0.0886 -0.1413 57 VAL A O 438 C CB . VAL A 57 ? 0.8196 1.0813 0.6573 0.0872 0.0735 -0.1307 57 VAL A CB 439 C CG1 . VAL A 57 ? 0.7951 1.1005 0.6507 0.0650 0.0825 -0.1269 57 VAL A CG1 440 C CG2 . VAL A 57 ? 0.8182 1.0819 0.6672 0.0937 0.0695 -0.1311 57 VAL A CG2 441 N N . ALA A 58 ? 0.8760 1.0994 0.6599 0.1056 0.0748 -0.1381 58 ALA A N 442 C CA . ALA A 58 ? 0.8837 1.1076 0.6547 0.1014 0.0787 -0.1384 58 ALA A CA 443 C C . ALA A 58 ? 0.9064 1.1493 0.6568 0.1296 0.0829 -0.1478 58 ALA A C 444 O O . ALA A 58 ? 0.8868 1.1723 0.6417 0.1287 0.0913 -0.1490 58 ALA A O 445 C CB . ALA A 58 ? 0.8920 1.0613 0.6451 0.0916 0.0709 -0.1354 58 ALA A CB 446 N N . GLY A 59 ? 0.9331 1.1427 0.6572 0.1553 0.0775 -0.1543 59 GLY A N 447 C CA . GLY A 59 ? 0.9435 1.1638 0.6405 0.1891 0.0809 -0.1637 59 GLY A CA 448 C C . GLY A 59 ? 0.9338 1.2327 0.6536 0.2006 0.0899 -0.1663 59 GLY A C 449 O O . GLY A 59 ? 0.9549 1.2907 0.6663 0.2155 0.0968 -0.1711 59 GLY A O 450 N N . TRP A 60 ? 0.8864 1.2145 0.6345 0.1925 0.0898 -0.1632 60 TRP A N 451 C CA . TRP A 60 ? 0.8599 1.2698 0.6329 0.1963 0.0979 -0.1651 60 TRP A CA 452 C C . TRP A 60 ? 0.8471 1.3026 0.6386 0.1680 0.1069 -0.1613 60 TRP A C 453 O O . TRP A 60 ? 0.8528 1.3632 0.6426 0.1794 0.1148 -0.1661 60 TRP A O 454 C CB . TRP A 60 ? 0.8370 1.2619 0.6354 0.1870 0.0951 -0.1619 60 TRP A CB 455 C CG . TRP A 60 ? 0.8060 1.3157 0.6347 0.1760 0.1031 -0.1620 60 TRP A CG 456 C CD1 . TRP A 60 ? 0.8196 1.4029 0.6506 0.1920 0.1111 -0.1680 60 TRP A CD1 457 C CD2 . TRP A 60 ? 0.7684 1.2997 0.6266 0.1453 0.1039 -0.1561 60 TRP A CD2 458 N NE1 . TRP A 60 ? 0.7893 1.4419 0.6504 0.1695 0.1168 -0.1663 60 TRP A NE1 459 C CE2 . TRP A 60 ? 0.7574 1.3754 0.6338 0.1404 0.1125 -0.1591 60 TRP A CE2 460 C CE3 . TRP A 60 ? 0.7460 1.2327 0.6148 0.1213 0.0984 -0.1488 60 TRP A CE3 461 C CZ2 . TRP A 60 ? 0.7424 1.3981 0.6442 0.1096 0.1155 -0.1553 60 TRP A CZ2 462 C CZ3 . TRP A 60 ? 0.7171 1.2387 0.6106 0.0946 0.1015 -0.1449 60 TRP A CZ3 463 C CH2 . TRP A 60 ? 0.7157 1.3183 0.6242 0.0877 0.1099 -0.1483 60 TRP A CH2 464 N N . LEU A 61 ? 0.8342 1.2658 0.6397 0.1325 0.1060 -0.1527 61 LEU A N 465 C CA . LEU A 61 ? 0.8241 1.2931 0.6438 0.1021 0.1149 -0.1478 61 LEU A CA 466 C C . LEU A 61 ? 0.8427 1.3118 0.6440 0.1046 0.1197 -0.1495 61 LEU A C 467 O O . LEU A 61 ? 0.8330 1.3573 0.6399 0.0955 0.1294 -0.1504 61 LEU A O 468 C CB . LEU A 61 ? 0.8044 1.2385 0.6358 0.0681 0.1124 -0.1379 61 LEU A CB 469 C CG . LEU A 61 ? 0.7902 1.2382 0.6430 0.0575 0.1106 -0.1355 61 LEU A CG 470 C CD1 . LEU A 61 ? 0.7883 1.1952 0.6458 0.0278 0.1084 -0.1257 61 LEU A CD1 471 C CD2 . LEU A 61 ? 0.7789 1.3048 0.6480 0.0501 0.1196 -0.1387 61 LEU A CD2 472 N N . LEU A 62 ? 0.8622 1.2709 0.6402 0.1150 0.1130 -0.1500 62 LEU A N 473 C CA . LEU A 62 ? 0.8825 1.2856 0.6390 0.1212 0.1164 -0.1525 62 LEU A CA 474 C C . LEU A 62 ? 0.9072 1.3478 0.6484 0.1562 0.1209 -0.1626 62 LEU A C 475 O O . LEU A 62 ? 0.9328 1.3948 0.6624 0.1602 0.1273 -0.1652 62 LEU A O 476 C CB . LEU A 62 ? 0.8894 1.2187 0.6232 0.1215 0.1071 -0.1509 62 LEU A CB 477 C CG . LEU A 62 ? 0.8628 1.1615 0.6079 0.0899 0.1037 -0.1407 62 LEU A CG 478 C CD1 . LEU A 62 ? 0.8870 1.1218 0.6125 0.0921 0.0928 -0.1401 62 LEU A CD1 479 C CD2 . LEU A 62 ? 0.8695 1.1875 0.6156 0.0691 0.1116 -0.1355 62 LEU A CD2 480 N N . GLY A 63 ? 0.9223 1.3706 0.6609 0.1836 0.1177 -0.1683 63 GLY A N 481 C CA . GLY A 63 ? 0.9525 1.4361 0.6727 0.2236 0.1215 -0.1780 63 GLY A CA 482 C C . GLY A 63 ? 1.0039 1.4197 0.6791 0.2525 0.1155 -0.1839 63 GLY A C 483 O O . GLY A 63 ? 1.0119 1.4412 0.6641 0.2744 0.1202 -0.1899 63 GLY A O 484 N N . ASN A 64 ? 1.0227 1.3648 0.6827 0.2508 0.1052 -0.1823 64 ASN A N 485 C CA . ASN A 64 ? 1.0865 1.3561 0.6967 0.2764 0.0987 -0.1885 64 ASN A CA 486 C C . ASN A 64 ? 1.1283 1.4230 0.7113 0.3247 0.1027 -0.1982 64 ASN A C 487 O O . ASN A 64 ? 1.1017 1.4397 0.6998 0.3416 0.1043 -0.1997 64 ASN A O 488 C CB . ASN A 64 ? 1.0966 1.2986 0.6975 0.2682 0.0880 -0.1858 64 ASN A CB 489 C CG . ASN A 64 ? 1.1602 1.2788 0.7027 0.2888 0.0811 -0.1922 64 ASN A CG 490 O OD1 . ASN A 64 ? 1.1990 1.3088 0.7035 0.3278 0.0831 -0.2005 64 ASN A OD1 491 N ND2 . ASN A 64 ? 1.1655 1.2219 0.6970 0.2625 0.0730 -0.1883 64 ASN A ND2 492 N N . PRO A 65 ? 1.1874 1.4560 0.7278 0.3488 0.1044 -0.2051 65 PRO A N 493 C CA . PRO A 65 ? 1.2439 1.5424 0.7551 0.3993 0.1095 -0.2144 65 PRO A CA 494 C C . PRO A 65 ? 1.2926 1.5545 0.7726 0.4359 0.1040 -0.2190 65 PRO A C 495 O O . PRO A 65 ? 1.3209 1.6267 0.7874 0.4790 0.1087 -0.2253 65 PRO A O 496 C CB . PRO A 65 ? 1.2904 1.5438 0.7547 0.4129 0.1105 -0.2200 65 PRO A CB 497 C CG . PRO A 65 ? 1.2837 1.4611 0.7406 0.3750 0.1024 -0.2149 65 PRO A CG 498 C CD . PRO A 65 ? 1.2143 1.4249 0.7292 0.3321 0.1014 -0.2046 65 PRO A CD 499 N N . MET A 66 ? 1.3358 1.5211 0.8032 0.4196 0.0945 -0.2157 66 MET A N 500 C CA . MET A 66 ? 1.3929 1.5390 0.8324 0.4478 0.0890 -0.2184 66 MET A CA 501 C C . MET A 66 ? 1.3292 1.5404 0.8212 0.4390 0.0896 -0.2134 66 MET A C 502 O O . MET A 66 ? 1.3232 1.5062 0.7988 0.4579 0.0848 -0.2143 66 MET A O 503 C CB . MET A 66 ? 1.4511 1.4870 0.8521 0.4295 0.0788 -0.2169 66 MET A CB 504 C CG . MET A 66 ? 1.5231 1.4840 0.8649 0.4346 0.0768 -0.2224 66 MET A CG 505 S SD . MET A 66 ? 1.6593 1.5501 0.9098 0.4972 0.0763 -0.2339 66 MET A SD 506 C CE . MET A 66 ? 1.6869 1.4911 0.9065 0.4915 0.0663 -0.2316 66 MET A CE 507 N N . CYS A 67 ? 1.2747 1.5684 0.8250 0.4094 0.0956 -0.2082 67 CYS A N 508 C CA . CYS A 67 ? 1.2260 1.5813 0.8262 0.3937 0.0965 -0.2033 67 CYS A CA 509 C C . CYS A 67 ? 1.2007 1.6694 0.8319 0.4050 0.1065 -0.2059 67 CYS A C 510 O O . CYS A 67 ? 1.1409 1.6729 0.8204 0.3725 0.1103 -0.2007 67 CYS A O 511 C CB . CYS A 67 ? 1.1712 1.5134 0.8102 0.3391 0.0938 -0.1936 67 CYS A CB 512 S SG . CYS A 67 ? 1.2095 1.4348 0.8178 0.3214 0.0821 -0.1901 67 CYS A SG 513 N N . ASP A 68 ? 1.2500 1.7440 0.8496 0.4511 0.1109 -0.2143 68 ASP A N 514 C CA . ASP A 68 ? 1.2305 1.8403 0.8551 0.4663 0.1208 -0.2179 68 ASP A CA 515 C C . ASP A 68 ? 1.2058 1.8816 0.8569 0.4782 0.1204 -0.2181 68 ASP A C 516 O O . ASP A 68 ? 1.1876 1.9699 0.8755 0.4703 0.1279 -0.2185 68 ASP A O 517 C CB . ASP A 68 ? 1.2851 1.9021 0.8638 0.5182 0.1252 -0.2270 68 ASP A CB 518 C CG . ASP A 68 ? 1.3046 1.8753 0.8617 0.5045 0.1271 -0.2273 68 ASP A CG 519 O OD1 . ASP A 68 ? 1.2863 1.8295 0.8674 0.4549 0.1256 -0.2201 68 ASP A OD1 520 O OD2 . ASP A 68 ? 1.3702 1.9320 0.8841 0.5451 0.1302 -0.2348 68 ASP A OD2 521 N N . GLU A 69 ? 1.2052 1.8187 0.8356 0.4954 0.1118 -0.2179 69 GLU A N 522 C CA . GLU A 69 ? 1.1827 1.8469 0.8388 0.5019 0.1099 -0.2171 69 GLU A CA 523 C C . GLU A 69 ? 1.0985 1.8270 0.8166 0.4462 0.1131 -0.2101 69 GLU A C 524 O O . GLU A 69 ? 1.0644 1.8849 0.8132 0.4472 0.1167 -0.2111 69 GLU A O 525 C CB . GLU A 69 ? 1.2283 1.7948 0.8538 0.5139 0.0995 -0.2156 69 GLU A CB 526 C CG . GLU A 69 ? 1.2271 1.8349 0.8733 0.5241 0.0965 -0.2147 69 GLU A CG 527 C CD . GLU A 69 ? 1.2644 1.7707 0.8796 0.5307 0.0865 -0.2123 69 GLU A CD 528 O OE1 . GLU A 69 ? 1.3176 1.7220 0.8929 0.5267 0.0819 -0.2118 69 GLU A OE1 529 O OE2 . GLU A 69 ? 1.2497 1.7796 0.8793 0.5381 0.0833 -0.2111 69 GLU A OE2 530 N N . PHE A 70 ? 1.0572 1.7366 0.7893 0.3985 0.1119 -0.2032 70 PHE A N 531 C CA . PHE A 70 ? 0.9927 1.7108 0.7730 0.3449 0.1145 -0.1958 70 PHE A CA 532 C C . PHE A 70 ? 0.9716 1.7416 0.7698 0.3150 0.1241 -0.1943 70 PHE A C 533 O O . PHE A 70 ? 0.9152 1.6757 0.7365 0.2675 0.1255 -0.1870 70 PHE A O 534 C CB . PHE A 70 ? 0.9777 1.6045 0.7597 0.3133 0.1064 -0.1882 70 PHE A CB 535 C CG . PHE A 70 ? 0.9934 1.5510 0.7477 0.3408 0.0969 -0.1896 70 PHE A CG 536 C CD1 . PHE A 70 ? 0.9735 1.5607 0.7407 0.3531 0.0941 -0.1901 70 PHE A CD1 537 C CD2 . PHE A 70 ? 1.0253 1.4882 0.7370 0.3535 0.0909 -0.1906 70 PHE A CD2 538 C CE1 . PHE A 70 ? 1.0031 1.5232 0.7408 0.3782 0.0858 -0.1911 70 PHE A CE1 539 C CE2 . PHE A 70 ? 1.0608 1.4559 0.7410 0.3757 0.0828 -0.1918 70 PHE A CE2 540 C CZ . PHE A 70 ? 1.0438 1.4660 0.7366 0.3887 0.0804 -0.1918 70 PHE A CZ 541 N N . ILE A 71 ? 1.0183 1.8418 0.8025 0.3441 0.1309 -0.2010 71 ILE A N 542 C CA . ILE A 71 ? 1.0247 1.9008 0.8219 0.3181 0.1407 -0.2000 71 ILE A CA 543 C C . ILE A 71 ? 0.9882 1.9587 0.8272 0.2800 0.1479 -0.1972 71 ILE A C 544 O O . ILE A 71 ? 0.9681 1.9543 0.8210 0.2375 0.1543 -0.1924 71 ILE A O 545 C CB . ILE A 71 ? 1.0851 1.9987 0.8549 0.3616 0.1466 -0.2084 71 ILE A CB 546 C CG1 . ILE A 71 ? 1.0764 2.0195 0.8533 0.3316 0.1558 -0.2063 71 ILE A CG1 547 C CG2 . ILE A 71 ? 1.0874 2.1037 0.8640 0.3992 0.1508 -0.2155 71 ILE A CG2 548 C CD1 . ILE A 71 ? 1.1169 2.0588 0.8585 0.3711 0.1596 -0.2133 71 ILE A CD1 549 N N . ASN A 72 ? 0.9908 2.0218 0.8457 0.2944 0.1468 -0.2002 72 ASN A N 550 C CA . ASN A 72 ? 0.9672 2.0795 0.8592 0.2536 0.1520 -0.1976 72 ASN A CA 551 C C . ASN A 72 ? 0.9401 2.0594 0.8453 0.2626 0.1449 -0.1978 72 ASN A C 552 O O . ASN A 72 ? 0.9598 2.1439 0.8646 0.3016 0.1446 -0.2043 72 ASN A O 553 C CB . ASN A 72 ? 0.9785 2.2150 0.8817 0.2562 0.1632 -0.2031 72 ASN A CB 554 C CG . ASN A 72 ? 1.0086 2.2529 0.9130 0.2161 0.1724 -0.1995 72 ASN A CG 555 O OD1 . ASN A 72 ? 1.0148 2.2118 0.9268 0.1667 0.1727 -0.1917 72 ASN A OD1 556 N ND2 . ASN A 72 ? 1.0472 2.3495 0.9407 0.2392 0.1799 -0.2051 72 ASN A ND2 557 N N . VAL A 73 ? 0.9044 1.9578 0.8199 0.2282 0.1393 -0.1905 73 VAL A N 558 C CA . VAL A 73 ? 0.8791 1.9198 0.8039 0.2356 0.1316 -0.1898 73 VAL A CA 559 C C . VAL A 73 ? 0.8311 1.9451 0.7888 0.1937 0.1356 -0.1878 73 VAL A C 560 O O . VAL A 73 ? 0.7998 1.9099 0.7683 0.1431 0.1406 -0.1823 73 VAL A O 561 C CB . VAL A 73 ? 0.8837 1.8043 0.7966 0.2272 0.1221 -0.1834 73 VAL A CB 562 C CG1 . VAL A 73 ? 0.9150 1.7595 0.7911 0.2629 0.1179 -0.1857 73 VAL A CG1 563 C CG2 . VAL A 73 ? 0.8722 1.7568 0.7992 0.1708 0.1242 -0.1748 73 VAL A CG2 564 N N . PRO A 74 ? 0.8113 1.9891 0.7809 0.2145 0.1332 -0.1922 74 PRO A N 565 C CA . PRO A 74 ? 0.7904 2.0364 0.7887 0.1732 0.1362 -0.1909 74 PRO A CA 566 C C . PRO A 74 ? 0.7756 1.9377 0.7796 0.1368 0.1304 -0.1830 74 PRO A C 567 O O . PRO A 74 ? 0.7437 1.8038 0.7318 0.1476 0.1237 -0.1789 74 PRO A O 568 C CB . PRO A 74 ? 0.7890 2.1125 0.7936 0.2151 0.1331 -0.1979 74 PRO A CB 569 C CG . PRO A 74 ? 0.8141 2.0570 0.7901 0.2707 0.1245 -0.1993 74 PRO A CG 570 C CD . PRO A 74 ? 0.8301 2.0042 0.7823 0.2755 0.1265 -0.1978 74 PRO A CD 571 N N . GLU A 75 ? 0.7670 1.9730 0.7911 0.0939 0.1331 -0.1812 75 GLU A N 572 C CA . GLU A 75 ? 0.7755 1.9050 0.8023 0.0590 0.1286 -0.1737 75 GLU A CA 573 C C . GLU A 75 ? 0.7449 1.8172 0.7687 0.0931 0.1174 -0.1732 75 GLU A C 574 O O . GLU A 75 ? 0.7089 1.8250 0.7337 0.1340 0.1138 -0.1791 75 GLU A O 575 C CB . GLU A 75 ? 0.7953 1.9816 0.8378 0.0066 0.1339 -0.1727 75 GLU A CB 576 C CG . GLU A 75 ? 0.8062 2.0791 0.8670 0.0156 0.1317 -0.1785 75 GLU A CG 577 C CD . GLU A 75 ? 0.8187 2.1140 0.8886 -0.0422 0.1350 -0.1761 75 GLU A CD 578 O OE1 . GLU A 75 ? 0.7845 1.9930 0.8481 -0.0647 0.1310 -0.1695 75 GLU A OE1 579 O OE2 . GLU A 75 ? 0.8334 2.2328 0.9139 -0.0661 0.1417 -0.1809 75 GLU A OE2 580 N N . TRP A 76 ? 0.7382 1.7127 0.7554 0.0770 0.1122 -0.1660 76 TRP A N 581 C CA . TRP A 76 ? 0.7457 1.6549 0.7565 0.1047 0.1020 -0.1645 76 TRP A CA 582 C C . TRP A 76 ? 0.7394 1.6177 0.7619 0.0717 0.0986 -0.1590 76 TRP A C 583 O O . TRP A 76 ? 0.7482 1.6314 0.7769 0.0266 0.1038 -0.1552 76 TRP A O 584 C CB . TRP A 76 ? 0.7559 1.5722 0.7438 0.1230 0.0977 -0.1615 76 TRP A CB 585 C CG . TRP A 76 ? 0.7535 1.5121 0.7388 0.0842 0.1000 -0.1540 76 TRP A CG 586 C CD1 . TRP A 76 ? 0.7417 1.4353 0.7285 0.0605 0.0957 -0.1467 76 TRP A CD1 587 C CD2 . TRP A 76 ? 0.7488 1.5115 0.7270 0.0673 0.1072 -0.1528 76 TRP A CD2 588 N NE1 . TRP A 76 ? 0.7494 1.4064 0.7292 0.0321 0.0996 -0.1410 76 TRP A NE1 589 C CE2 . TRP A 76 ? 0.7440 1.4404 0.7182 0.0347 0.1066 -0.1445 76 TRP A CE2 590 C CE3 . TRP A 76 ? 0.7753 1.5925 0.7488 0.0779 0.1142 -0.1578 76 TRP A CE3 591 C CZ2 . TRP A 76 ? 0.7538 1.4338 0.7180 0.0130 0.1126 -0.1409 76 TRP A CZ2 592 C CZ3 . TRP A 76 ? 0.7671 1.5683 0.7324 0.0537 0.1204 -0.1544 76 TRP A CZ3 593 C CH2 . TRP A 76 ? 0.7693 1.5009 0.7293 0.0217 0.1194 -0.1458 76 TRP A CH2 594 N N . SER A 77 ? 0.7488 1.5919 0.7697 0.0955 0.0901 -0.1587 77 SER A N 595 C CA . SER A 77 ? 0.7153 1.5201 0.7445 0.0715 0.0858 -0.1535 77 SER A CA 596 C C . SER A 77 ? 0.7193 1.4224 0.7353 0.0657 0.0813 -0.1462 77 SER A C 597 O O . SER A 77 ? 0.7371 1.4035 0.7558 0.0318 0.0821 -0.1400 77 SER A O 598 C CB . SER A 77 ? 0.7135 1.5379 0.7471 0.1015 0.0790 -0.1570 77 SER A CB 599 O OG . SER A 77 ? 0.7259 1.5268 0.7403 0.1505 0.0744 -0.1603 77 SER A OG 600 N N . TYR A 78 ? 0.7159 1.3746 0.7145 0.0999 0.0767 -0.1473 78 TYR A N 601 C CA . TYR A 78 ? 0.6982 1.2687 0.6826 0.0962 0.0722 -0.1414 78 TYR A CA 602 C C . TYR A 78 ? 0.6978 1.2442 0.6593 0.1256 0.0715 -0.1448 78 TYR A C 603 O O . TYR A 78 ? 0.7078 1.2991 0.6625 0.1544 0.0735 -0.1516 78 TYR A O 604 C CB . TYR A 78 ? 0.6929 1.2136 0.6761 0.1024 0.0639 -0.1381 78 TYR A CB 605 C CG . TYR A 78 ? 0.6970 1.2221 0.6689 0.1427 0.0585 -0.1433 78 TYR A CG 606 C CD1 . TYR A 78 ? 0.6812 1.2719 0.6657 0.1543 0.0590 -0.1479 78 TYR A CD1 607 C CD2 . TYR A 78 ? 0.7259 1.1870 0.6704 0.1686 0.0528 -0.1436 78 TYR A CD2 608 C CE1 . TYR A 78 ? 0.7046 1.2959 0.6739 0.1951 0.0540 -0.1522 78 TYR A CE1 609 C CE2 . TYR A 78 ? 0.7465 1.2010 0.6718 0.2064 0.0482 -0.1480 78 TYR A CE2 610 C CZ . TYR A 78 ? 0.7386 1.2573 0.6760 0.2217 0.0487 -0.1521 78 TYR A CZ 611 O OH . TYR A 78 ? 0.7635 1.2714 0.6767 0.2633 0.0441 -0.1561 78 TYR A OH 612 N N . ILE A 79 ? 0.6835 1.1609 0.6310 0.1190 0.0685 -0.1402 79 ILE A N 613 C CA . ILE A 79 ? 0.7166 1.1644 0.6389 0.1414 0.0678 -0.1434 79 ILE A CA 614 C C . ILE A 79 ? 0.7406 1.1144 0.6396 0.1582 0.0591 -0.1423 79 ILE A C 615 O O . ILE A 79 ? 0.7353 1.0708 0.6406 0.1408 0.0545 -0.1365 79 ILE A O 616 C CB . ILE A 79 ? 0.7147 1.1491 0.6361 0.1169 0.0723 -0.1396 79 ILE A CB 617 C CG1 . ILE A 79 ? 0.7095 1.2154 0.6477 0.0987 0.0818 -0.1409 79 ILE A CG1 618 C CG2 . ILE A 79 ? 0.7456 1.1436 0.6388 0.1383 0.0708 -0.1428 79 ILE A CG2 619 C CD1 . ILE A 79 ? 0.7256 1.2161 0.6622 0.0697 0.0869 -0.1357 79 ILE A CD1 620 N N . VAL A 80 ? 0.7659 1.1183 0.6343 0.1913 0.0571 -0.1480 80 VAL A N 621 C CA . VAL A 80 ? 0.8120 1.0890 0.6493 0.2052 0.0492 -0.1477 80 VAL A CA 622 C C . VAL A 80 ? 0.8507 1.0782 0.6550 0.2115 0.0483 -0.1497 80 VAL A C 623 O O . VAL A 80 ? 0.8970 1.1362 0.6793 0.2382 0.0512 -0.1561 80 VAL A O 624 C CB . VAL A 80 ? 0.8351 1.1122 0.6523 0.2425 0.0460 -0.1529 80 VAL A CB 625 C CG1 . VAL A 80 ? 0.8639 1.0539 0.6423 0.2517 0.0384 -0.1520 80 VAL A CG1 626 C CG2 . VAL A 80 ? 0.8140 1.1426 0.6637 0.2359 0.0464 -0.1512 80 VAL A CG2 627 N N . GLU A 81 ? 0.8700 1.0441 0.6694 0.1875 0.0439 -0.1443 81 GLU A N 628 C CA . GLU A 81 ? 0.9266 1.0526 0.6962 0.1858 0.0422 -0.1454 81 GLU A CA 629 C C . GLU A 81 ? 0.9718 1.0237 0.7078 0.1867 0.0340 -0.1448 81 GLU A C 630 O O . GLU A 81 ? 0.9918 1.0301 0.7410 0.1714 0.0300 -0.1397 81 GLU A O 631 C CB . GLU A 81 ? 0.9167 1.0522 0.7099 0.1524 0.0443 -0.1391 81 GLU A CB 632 C CG . GLU A 81 ? 0.9662 1.0652 0.7334 0.1485 0.0432 -0.1403 81 GLU A CG 633 C CD . GLU A 81 ? 0.9508 1.0617 0.7400 0.1187 0.0452 -0.1335 81 GLU A CD 634 O OE1 . GLU A 81 ? 0.9195 1.0279 0.7298 0.0976 0.0429 -0.1265 81 GLU A OE1 635 O OE2 . GLU A 81 ? 0.9723 1.0946 0.7553 0.1186 0.0494 -0.1353 81 GLU A OE2 636 N N . LYS A 82 ? 1.0489 1.0514 0.7384 0.2029 0.0319 -0.1500 82 LYS A N 637 C CA . LYS A 82 ? 1.1115 1.0378 0.7615 0.1974 0.0246 -0.1497 82 LYS A CA 638 C C . LYS A 82 ? 1.0930 1.0016 0.7556 0.1590 0.0211 -0.1433 82 LYS A C 639 O O . LYS A 82 ? 1.0428 0.9869 0.7339 0.1427 0.0244 -0.1402 82 LYS A O 640 C CB . LYS A 82 ? 1.2026 1.0745 0.7909 0.2241 0.0237 -0.1576 82 LYS A CB 641 C CG . LYS A 82 ? 1.2584 1.1304 0.8201 0.2674 0.0252 -0.1637 82 LYS A CG 642 C CD . LYS A 82 ? 1.3665 1.1704 0.8567 0.2952 0.0241 -0.1713 82 LYS A CD 643 C CE . LYS A 82 ? 1.4493 1.2281 0.8987 0.3379 0.0233 -0.1759 82 LYS A CE 644 N NZ . LYS A 82 ? 1.4338 1.2983 0.9177 0.3685 0.0289 -0.1781 82 LYS A NZ 645 N N . ALA A 83 ? 1.1422 0.9974 0.7813 0.1449 0.0145 -0.1412 83 ALA A N 646 C CA . ALA A 83 ? 1.1526 0.9956 0.8010 0.1098 0.0105 -0.1353 83 ALA A CA 647 C C . ALA A 83 ? 1.2213 1.0481 0.8476 0.1019 0.0104 -0.1381 83 ALA A C 648 O O . ALA A 83 ? 1.2328 1.0825 0.8834 0.0790 0.0101 -0.1331 83 ALA A O 649 C CB . ALA A 83 ? 1.1648 0.9570 0.7877 0.0961 0.0037 -0.1334 83 ALA A CB 650 N N . ASN A 84 ? 1.2837 1.0698 0.8610 0.1226 0.0106 -0.1460 84 ASN A N 651 C CA . ASN A 84 ? 1.3225 1.0881 0.8726 0.1169 0.0105 -0.1497 84 ASN A CA 652 C C . ASN A 84 ? 1.3362 1.0998 0.8588 0.1519 0.0157 -0.1579 84 ASN A C 653 O O . ASN A 84 ? 1.3764 1.0790 0.8396 0.1660 0.0137 -0.1646 84 ASN A O 654 C CB . ASN A 84 ? 1.4135 1.1096 0.9142 0.0959 0.0032 -0.1511 84 ASN A CB 655 C CG . ASN A 84 ? 1.4164 1.1253 0.9455 0.0599 -0.0017 -0.1430 84 ASN A CG 656 O OD1 . ASN A 84 ? 1.3971 1.1476 0.9619 0.0414 -0.0015 -0.1379 84 ASN A OD1 657 N ND2 . ASN A 84 ? 1.4525 1.1264 0.9636 0.0516 -0.0061 -0.1416 84 ASN A ND2 658 N N . PRO A 85 ? 1.2771 1.1070 0.8393 0.1654 0.0227 -0.1575 85 PRO A N 659 C CA . PRO A 85 ? 1.2947 1.1364 0.8354 0.2003 0.0284 -0.1652 85 PRO A CA 660 C C . PRO A 85 ? 1.3290 1.1339 0.8295 0.1996 0.0281 -0.1701 85 PRO A C 661 O O . PRO A 85 ? 1.3412 1.1530 0.8575 0.1711 0.0268 -0.1662 85 PRO A O 662 C CB . PRO A 85 ? 1.2208 1.1484 0.8186 0.2004 0.0359 -0.1620 85 PRO A CB 663 C CG . PRO A 85 ? 1.1676 1.1183 0.8102 0.1725 0.0338 -0.1533 85 PRO A CG 664 C CD . PRO A 85 ? 1.1850 1.0805 0.8089 0.1469 0.0261 -0.1500 85 PRO A CD 665 N N . VAL A 86 ? 1.3626 1.1279 0.8089 0.2323 0.0292 -0.1786 86 VAL A N 666 C CA . VAL A 86 ? 1.4166 1.1388 0.8165 0.2333 0.0288 -0.1843 86 VAL A CA 667 C C . VAL A 86 ? 1.3780 1.1597 0.8044 0.2396 0.0360 -0.1854 86 VAL A C 668 O O . VAL A 86 ? 1.3829 1.1475 0.7948 0.2242 0.0351 -0.1864 86 VAL A O 669 C CB . VAL A 86 ? 1.5166 1.1628 0.8375 0.2676 0.0275 -0.1934 86 VAL A CB 670 C CG1 . VAL A 86 ? 1.5529 1.1323 0.8401 0.2587 0.0207 -0.1921 86 VAL A CG1 671 C CG2 . VAL A 86 ? 1.5205 1.2061 0.8384 0.3171 0.0346 -0.1988 86 VAL A CG2 672 N N . ASN A 87 ? 1.3201 1.1728 0.7837 0.2602 0.0431 -0.1852 87 ASN A N 673 C CA . ASN A 87 ? 1.2805 1.1957 0.7698 0.2647 0.0510 -0.1860 87 ASN A CA 674 C C . ASN A 87 ? 1.2344 1.2068 0.7858 0.2295 0.0532 -0.1769 87 ASN A C 675 O O . ASN A 87 ? 1.2097 1.2478 0.8030 0.2310 0.0587 -0.1741 87 ASN A O 676 C CB . ASN A 87 ? 1.2850 1.2519 0.7760 0.3056 0.0582 -0.1914 87 ASN A CB 677 C CG . ASN A 87 ? 1.3673 1.2783 0.7902 0.3481 0.0572 -0.2008 87 ASN A CG 678 O OD1 . ASN A 87 ? 1.4485 1.2945 0.8210 0.3491 0.0544 -0.2051 87 ASN A OD1 679 N ND2 . ASN A 87 ? 1.3860 1.3214 0.8034 0.3847 0.0594 -0.2041 87 ASN A ND2 680 N N . ASP A 88 ? 1.2307 1.1768 0.7839 0.1978 0.0487 -0.1723 88 ASP A N 681 C CA . ASP A 88 ? 1.1639 1.1528 0.7656 0.1669 0.0505 -0.1634 88 ASP A CA 682 C C . ASP A 88 ? 1.1639 1.1737 0.7636 0.1640 0.0557 -0.1644 88 ASP A C 683 O O . ASP A 88 ? 1.1506 1.1967 0.7491 0.1854 0.0633 -0.1691 88 ASP A O 684 C CB . ASP A 88 ? 1.1623 1.1147 0.7677 0.1371 0.0419 -0.1571 88 ASP A CB 685 C CG . ASP A 88 ? 1.1324 1.1259 0.7857 0.1105 0.0434 -0.1472 88 ASP A CG 686 O OD1 . ASP A 88 ? 1.1020 1.1470 0.7860 0.1123 0.0508 -0.1448 88 ASP A OD1 687 O OD2 . ASP A 88 ? 1.1603 1.1339 0.8171 0.0875 0.0372 -0.1417 88 ASP A OD2 688 N N . LEU A 89 ? 1.1482 1.1389 0.7465 0.1389 0.0519 -0.1602 89 LEU A N 689 C CA . LEU A 89 ? 1.1465 1.1488 0.7370 0.1363 0.0559 -0.1613 89 LEU A CA 690 C C . LEU A 89 ? 1.1944 1.1440 0.7297 0.1526 0.0527 -0.1705 89 LEU A C 691 O O . LEU A 89 ? 1.2052 1.1035 0.7131 0.1379 0.0445 -0.1711 89 LEU A O 692 C CB . LEU A 89 ? 1.1264 1.1318 0.7363 0.1050 0.0527 -0.1526 89 LEU A CB 693 C CG . LEU A 89 ? 1.0712 1.1164 0.7269 0.0883 0.0555 -0.1430 89 LEU A CG 694 C CD1 . LEU A 89 ? 1.0660 1.1056 0.7308 0.0634 0.0513 -0.1347 89 LEU A CD1 695 C CD2 . LEU A 89 ? 1.0353 1.1344 0.7129 0.0947 0.0665 -0.1424 89 LEU A CD2 696 N N . CYS A 90 ? 1.2146 1.1780 0.7310 0.1826 0.0592 -0.1779 90 CYS A N 697 C CA . CYS A 90 ? 1.2747 1.1847 0.7320 0.2036 0.0573 -0.1875 90 CYS A CA 698 C C . CYS A 90 ? 1.2795 1.1667 0.7191 0.1835 0.0546 -0.1874 90 CYS A C 699 O O . CYS A 90 ? 1.3403 1.1641 0.7357 0.1761 0.0472 -0.1913 90 CYS A O 700 C CB . CYS A 90 ? 1.3178 1.2578 0.7610 0.2437 0.0659 -0.1951 90 CYS A CB 701 S SG . CYS A 90 ? 1.2996 1.3335 0.7884 0.2435 0.0781 -0.1921 90 CYS A SG 702 N N . TYR A 91 ? 1.2228 1.1610 0.6942 0.1730 0.0605 -0.1827 91 TYR A N 703 C CA . TYR A 91 ? 1.2175 1.1443 0.6829 0.1498 0.0574 -0.1800 91 TYR A CA 704 C C . TYR A 91 ? 1.1753 1.1057 0.6725 0.1176 0.0510 -0.1702 91 TYR A C 705 O O . TYR A 91 ? 1.1298 1.1021 0.6702 0.1107 0.0545 -0.1629 91 TYR A O 706 C CB . TYR A 91 ? 1.2072 1.1862 0.6915 0.1526 0.0669 -0.1782 91 TYR A CB 707 C CG . TYR A 91 ? 1.2365 1.1971 0.6995 0.1395 0.0645 -0.1786 91 TYR A CG 708 C CD1 . TYR A 91 ? 1.2138 1.1747 0.6942 0.1097 0.0590 -0.1703 91 TYR A CD1 709 C CD2 . TYR A 91 ? 1.2748 1.2185 0.6978 0.1591 0.0675 -0.1873 91 TYR A CD2 710 C CE1 . TYR A 91 ? 1.2344 1.1824 0.6949 0.0986 0.0563 -0.1706 91 TYR A CE1 711 C CE2 . TYR A 91 ? 1.2812 1.2085 0.6837 0.1465 0.0651 -0.1879 91 TYR A CE2 712 C CZ . TYR A 91 ? 1.2580 1.1886 0.6801 0.1158 0.0592 -0.1795 91 TYR A CZ 713 O OH . TYR A 91 ? 1.2706 1.1889 0.6724 0.1040 0.0563 -0.1800 91 TYR A OH 714 N N . PRO A 92 ? 1.1992 1.0877 0.6732 0.0975 0.0416 -0.1701 92 PRO A N 715 C CA . PRO A 92 ? 1.1594 1.0535 0.6605 0.0704 0.0349 -0.1614 92 PRO A CA 716 C C . PRO A 92 ? 1.1369 1.0801 0.6792 0.0567 0.0385 -0.1513 92 PRO A C 717 O O . PRO A 92 ? 1.1489 1.1111 0.6898 0.0598 0.0438 -0.1512 92 PRO A O 718 C CB . PRO A 92 ? 1.1947 1.0419 0.6564 0.0521 0.0252 -0.1649 92 PRO A CB 719 C CG . PRO A 92 ? 1.2445 1.0775 0.6717 0.0634 0.0281 -0.1721 92 PRO A CG 720 C CD . PRO A 92 ? 1.2569 1.0976 0.6791 0.0967 0.0372 -0.1778 92 PRO A CD 721 N N . GLY A 93 ? 1.1235 1.0834 0.6980 0.0426 0.0359 -0.1429 93 GLY A N 722 C CA . GLY A 93 ? 1.0867 1.0830 0.6927 0.0306 0.0386 -0.1328 93 GLY A CA 723 C C . GLY A 93 ? 1.0677 1.0804 0.7069 0.0232 0.0380 -0.1249 93 GLY A C 724 O O . GLY A 93 ? 1.0342 1.0289 0.6727 0.0172 0.0312 -0.1250 93 GLY A O 725 N N . ASP A 94 ? 1.0650 1.1095 0.7296 0.0222 0.0455 -0.1180 94 ASP A N 726 C CA . ASP A 94 ? 1.0494 1.1079 0.7422 0.0152 0.0460 -0.1101 94 ASP A CA 727 C C . ASP A 94 ? 1.0140 1.1004 0.7248 0.0196 0.0566 -0.1086 94 ASP A C 728 O O . ASP A 94 ? 1.0114 1.1134 0.7159 0.0239 0.0641 -0.1106 94 ASP A O 729 C CB . ASP A 94 ? 1.0699 1.1334 0.7686 0.0024 0.0424 -0.1004 94 ASP A CB 730 C CG . ASP A 94 ? 1.1153 1.1633 0.8050 -0.0063 0.0311 -0.1005 94 ASP A CG 731 O OD1 . ASP A 94 ? 1.1354 1.1806 0.8376 -0.0105 0.0268 -0.0983 94 ASP A OD1 732 O OD2 . ASP A 94 ? 1.1608 1.2015 0.8301 -0.0106 0.0266 -0.1028 94 ASP A OD2 733 N N . PHE A 95 ? 0.9708 1.0649 0.7028 0.0168 0.0572 -0.1050 95 PHE A N 734 C CA . PHE A 95 ? 0.9177 1.0391 0.6671 0.0144 0.0665 -0.1022 95 PHE A CA 735 C C . PHE A 95 ? 0.9028 1.0205 0.6629 0.0009 0.0658 -0.0916 95 PHE A C 736 O O . PHE A 95 ? 0.8876 0.9955 0.6580 -0.0013 0.0600 -0.0888 95 PHE A O 737 C CB . PHE A 95 ? 0.9046 1.0366 0.6653 0.0242 0.0674 -0.1079 95 PHE A CB 738 C CG . PHE A 95 ? 0.8915 1.0613 0.6657 0.0231 0.0777 -0.1085 95 PHE A CG 739 C CD1 . PHE A 95 ? 0.8917 1.0728 0.6793 0.0065 0.0826 -0.1008 95 PHE A CD1 740 C CD2 . PHE A 95 ? 0.8985 1.0933 0.6684 0.0385 0.0827 -0.1170 95 PHE A CD2 741 C CE1 . PHE A 95 ? 0.9030 1.1204 0.6999 0.0002 0.0921 -0.1018 95 PHE A CE1 742 C CE2 . PHE A 95 ? 0.8962 1.1358 0.6795 0.0352 0.0921 -0.1179 95 PHE A CE2 743 C CZ . PHE A 95 ? 0.8925 1.1438 0.6896 0.0135 0.0969 -0.1103 95 PHE A CZ 744 N N . ASN A 96 ? 0.9055 1.0282 0.6591 -0.0068 0.0720 -0.0856 96 ASN A N 745 C CA . ASN A 96 ? 0.8995 1.0115 0.6533 -0.0157 0.0719 -0.0752 96 ASN A CA 746 C C . ASN A 96 ? 0.8663 0.9832 0.6346 -0.0225 0.0760 -0.0721 96 ASN A C 747 O O . ASN A 96 ? 0.8456 0.9824 0.6203 -0.0264 0.0836 -0.0758 96 ASN A O 748 C CB . ASN A 96 ? 0.9499 1.0597 0.6850 -0.0210 0.0784 -0.0698 96 ASN A CB 749 C CG . ASN A 96 ? 0.9762 1.0669 0.7010 -0.0237 0.0763 -0.0590 96 ASN A CG 750 O OD1 . ASN A 96 ? 0.9957 1.0794 0.7169 -0.0178 0.0677 -0.0565 96 ASN A OD1 751 N ND2 . ASN A 96 ? 0.9856 1.0679 0.7019 -0.0325 0.0845 -0.0526 96 ASN A ND2 752 N N . ASP A 97 ? 0.8601 0.9620 0.6324 -0.0239 0.0711 -0.0654 97 ASP A N 753 C CA . ASP A 97 ? 0.8408 0.9416 0.6245 -0.0298 0.0735 -0.0623 97 ASP A CA 754 C C . ASP A 97 ? 0.7900 0.9106 0.5923 -0.0279 0.0744 -0.0706 97 ASP A C 755 O O . ASP A 97 ? 0.7528 0.8865 0.5616 -0.0361 0.0811 -0.0709 97 ASP A O 756 C CB . ASP A 97 ? 0.9024 0.9948 0.6704 -0.0418 0.0832 -0.0556 97 ASP A CB 757 C CG . ASP A 97 ? 0.9504 1.0152 0.6978 -0.0393 0.0813 -0.0455 97 ASP A CG 758 O OD1 . ASP A 97 ? 0.9657 1.0245 0.7189 -0.0301 0.0727 -0.0427 97 ASP A OD1 759 O OD2 . ASP A 97 ? 1.0309 1.0809 0.7537 -0.0459 0.0886 -0.0402 97 ASP A OD2 760 N N . TYR A 98 ? 0.7593 0.8807 0.5663 -0.0171 0.0675 -0.0772 98 TYR A N 761 C CA . TYR A 98 ? 0.7632 0.8998 0.5814 -0.0093 0.0677 -0.0855 98 TYR A CA 762 C C . TYR A 98 ? 0.7502 0.8884 0.5850 -0.0125 0.0664 -0.0835 98 TYR A C 763 O O . TYR A 98 ? 0.7386 0.8996 0.5840 -0.0123 0.0711 -0.0873 98 TYR A O 764 C CB . TYR A 98 ? 0.7660 0.8881 0.5752 0.0028 0.0598 -0.0919 98 TYR A CB 765 C CG . TYR A 98 ? 0.7638 0.8943 0.5742 0.0168 0.0598 -0.1010 98 TYR A CG 766 C CD1 . TYR A 98 ? 0.7717 0.9335 0.5848 0.0233 0.0679 -0.1061 98 TYR A CD1 767 C CD2 . TYR A 98 ? 0.7637 0.8712 0.5684 0.0246 0.0518 -0.1046 98 TYR A CD2 768 C CE1 . TYR A 98 ? 0.7842 0.9566 0.5953 0.0415 0.0677 -0.1143 98 TYR A CE1 769 C CE2 . TYR A 98 ? 0.7716 0.8803 0.5701 0.0414 0.0517 -0.1126 98 TYR A CE2 770 C CZ . TYR A 98 ? 0.7975 0.9398 0.5995 0.0520 0.0596 -0.1174 98 TYR A CZ 771 O OH . TYR A 98 ? 0.8379 0.9851 0.6315 0.0737 0.0595 -0.1253 98 TYR A OH 772 N N . GLU A 99 ? 0.7410 0.8592 0.5779 -0.0151 0.0601 -0.0775 99 GLU A N 773 C CA . GLU A 99 ? 0.7438 0.8604 0.5951 -0.0169 0.0580 -0.0755 99 GLU A CA 774 C C . GLU A 99 ? 0.7290 0.8537 0.5829 -0.0286 0.0661 -0.0714 99 GLU A C 775 O O . GLU A 99 ? 0.7087 0.8463 0.5750 -0.0308 0.0680 -0.0738 99 GLU A O 776 C CB . GLU A 99 ? 0.7524 0.8501 0.6038 -0.0168 0.0497 -0.0699 99 GLU A CB 777 C CG . GLU A 99 ? 0.7740 0.8622 0.6211 -0.0109 0.0412 -0.0747 99 GLU A CG 778 C CD . GLU A 99 ? 0.8399 0.9240 0.6700 -0.0095 0.0398 -0.0773 99 GLU A CD 779 O OE1 . GLU A 99 ? 0.8518 0.9379 0.6746 -0.0129 0.0422 -0.0721 99 GLU A OE1 780 O OE2 . GLU A 99 ? 0.8712 0.9467 0.6912 -0.0041 0.0364 -0.0846 99 GLU A OE2 781 N N . GLU A 100 ? 0.7299 0.8451 0.5683 -0.0367 0.0711 -0.0654 100 GLU A N 782 C CA . GLU A 100 ? 0.7392 0.8537 0.5700 -0.0515 0.0798 -0.0616 100 GLU A CA 783 C C . GLU A 100 ? 0.7368 0.8855 0.5742 -0.0591 0.0874 -0.0686 100 GLU A C 784 O O . GLU A 100 ? 0.7692 0.9273 0.6077 -0.0731 0.0930 -0.0683 100 GLU A O 785 C CB . GLU A 100 ? 0.7532 0.8430 0.5576 -0.0573 0.0839 -0.0536 100 GLU A CB 786 C CG . GLU A 100 ? 0.7660 0.8260 0.5606 -0.0507 0.0786 -0.0451 100 GLU A CG 787 C CD . GLU A 100 ? 0.8001 0.8428 0.5891 -0.0587 0.0817 -0.0408 100 GLU A CD 788 O OE1 . GLU A 100 ? 0.8268 0.8626 0.5998 -0.0749 0.0906 -0.0400 100 GLU A OE1 789 O OE2 . GLU A 100 ? 0.7804 0.8161 0.5787 -0.0504 0.0755 -0.0384 100 GLU A OE2 790 N N . LEU A 101 ? 0.7263 0.8958 0.5664 -0.0497 0.0875 -0.0753 101 LEU A N 791 C CA . LEU A 101 ? 0.7307 0.9421 0.5781 -0.0525 0.0943 -0.0825 101 LEU A CA 792 C C . LEU A 101 ? 0.7051 0.9390 0.5726 -0.0434 0.0910 -0.0884 101 LEU A C 793 O O . LEU A 101 ? 0.6656 0.9326 0.5416 -0.0533 0.0966 -0.0910 101 LEU A O 794 C CB . LEU A 101 ? 0.7404 0.9666 0.5811 -0.0410 0.0956 -0.0879 101 LEU A CB 795 C CG . LEU A 101 ? 0.7393 1.0166 0.5874 -0.0385 0.1025 -0.0960 101 LEU A CG 796 C CD1 . LEU A 101 ? 0.7433 1.0446 0.5874 -0.0645 0.1132 -0.0932 101 LEU A CD1 797 C CD2 . LEU A 101 ? 0.7686 1.0536 0.6067 -0.0225 0.1028 -0.1014 101 LEU A CD2 798 N N . LYS A 102 ? 0.7160 0.9329 0.5886 -0.0258 0.0820 -0.0906 102 LYS A N 799 C CA . LYS A 102 ? 0.7258 0.9556 0.6130 -0.0150 0.0780 -0.0954 102 LYS A CA 800 C C . LYS A 102 ? 0.7056 0.9359 0.6031 -0.0296 0.0791 -0.0910 102 LYS A C 801 O O . LYS A 102 ? 0.6941 0.9534 0.6041 -0.0284 0.0804 -0.0952 102 LYS A O 802 C CB . LYS A 102 ? 0.7483 0.9476 0.6318 0.0015 0.0681 -0.0969 102 LYS A CB 803 C CG . LYS A 102 ? 0.8044 0.9994 0.6727 0.0172 0.0666 -0.1030 102 LYS A CG 804 C CD . LYS A 102 ? 0.8472 1.0030 0.7041 0.0260 0.0569 -0.1036 102 LYS A CD 805 C CE . LYS A 102 ? 0.8875 1.0394 0.7424 0.0431 0.0529 -0.1097 102 LYS A CE 806 N NZ . LYS A 102 ? 0.9361 1.0461 0.7679 0.0508 0.0450 -0.1122 102 LYS A NZ 807 N N . HIS A 103 ? 0.7166 0.9150 0.6061 -0.0420 0.0787 -0.0827 103 HIS A N 808 C CA . HIS A 103 ? 0.7224 0.9144 0.6142 -0.0566 0.0808 -0.0783 103 HIS A CA 809 C C . HIS A 103 ? 0.7352 0.9573 0.6239 -0.0762 0.0906 -0.0802 103 HIS A C 810 O O . HIS A 103 ? 0.7401 0.9784 0.6369 -0.0859 0.0922 -0.0816 103 HIS A O 811 C CB . HIS A 103 ? 0.7369 0.8867 0.6133 -0.0624 0.0793 -0.0689 103 HIS A CB 812 C CG . HIS A 103 ? 0.7396 0.8747 0.6121 -0.0750 0.0814 -0.0644 103 HIS A CG 813 N ND1 . HIS A 103 ? 0.7211 0.8467 0.6053 -0.0681 0.0752 -0.0633 103 HIS A ND1 814 C CD2 . HIS A 103 ? 0.7630 0.8885 0.6172 -0.0953 0.0893 -0.0611 103 HIS A CD2 815 C CE1 . HIS A 103 ? 0.7216 0.8330 0.5962 -0.0816 0.0789 -0.0596 103 HIS A CE1 816 N NE2 . HIS A 103 ? 0.7500 0.8585 0.6043 -0.0990 0.0875 -0.0583 103 HIS A NE2 817 N N . LEU A 104 ? 0.7675 0.9984 0.6431 -0.0840 0.0971 -0.0802 104 LEU A N 818 C CA . LEU A 104 ? 0.8015 1.0652 0.6711 -0.1063 0.1072 -0.0822 104 LEU A CA 819 C C . LEU A 104 ? 0.8069 1.1303 0.6986 -0.1005 0.1080 -0.0913 104 LEU A C 820 O O . LEU A 104 ? 0.8008 1.1560 0.6948 -0.1206 0.1137 -0.0931 104 LEU A O 821 C CB . LEU A 104 ? 0.8425 1.1080 0.6947 -0.1121 0.1134 -0.0813 104 LEU A CB 822 C CG . LEU A 104 ? 0.8819 1.1407 0.7087 -0.1436 0.1239 -0.0769 104 LEU A CG 823 C CD1 . LEU A 104 ? 0.9096 1.1067 0.7123 -0.1533 0.1230 -0.0676 104 LEU A CD1 824 C CD2 . LEU A 104 ? 0.8974 1.1626 0.7092 -0.1458 0.1296 -0.0767 104 LEU A CD2 825 N N . LEU A 105 ? 0.8291 1.1661 0.7334 -0.0724 0.1021 -0.0969 105 LEU A N 826 C CA . LEU A 105 ? 0.8266 1.2178 0.7478 -0.0573 0.1019 -0.1056 105 LEU A CA 827 C C . LEU A 105 ? 0.8174 1.2176 0.7534 -0.0567 0.0978 -0.1067 105 LEU A C 828 O O . LEU A 105 ? 0.8611 1.3140 0.8101 -0.0490 0.0990 -0.1132 105 LEU A O 829 C CB . LEU A 105 ? 0.8184 1.2044 0.7389 -0.0244 0.0960 -0.1108 105 LEU A CB 830 C CG . LEU A 105 ? 0.8220 1.2292 0.7326 -0.0157 0.1007 -0.1148 105 LEU A CG 831 C CD1 . LEU A 105 ? 0.8440 1.2337 0.7477 0.0178 0.0937 -0.1201 105 LEU A CD1 832 C CD2 . LEU A 105 ? 0.8388 1.3179 0.7572 -0.0228 0.1096 -0.1202 105 LEU A CD2 833 N N . SER A 106 ? 0.8647 1.3790 0.7174 -0.0228 0.0914 -0.0938 106 SER A N 834 C CA A SER A 106 ? 0.8786 1.4046 0.7243 -0.0268 0.0908 -0.0945 106 SER A CA 835 C CA B SER A 106 ? 0.8776 1.4044 0.7236 -0.0266 0.0906 -0.0945 106 SER A CA 836 C C . SER A 106 ? 0.8924 1.4372 0.7272 -0.0482 0.0949 -0.1058 106 SER A C 837 O O . SER A 106 ? 0.9313 1.4940 0.7577 -0.0540 0.0923 -0.1084 106 SER A O 838 C CB A SER A 106 ? 0.8790 1.3706 0.7192 -0.0246 0.0962 -0.0890 106 SER A CB 839 C CB B SER A 106 ? 0.8767 1.3696 0.7179 -0.0232 0.0954 -0.0884 106 SER A CB 840 O OG A SER A 106 ? 0.8814 1.3481 0.7108 -0.0390 0.1071 -0.0956 106 SER A OG 841 O OG B SER A 106 ? 0.8538 1.3301 0.7070 -0.0068 0.0902 -0.0773 106 SER A OG 842 N N . ARG A 107 ? 0.9193 1.4581 0.7522 -0.0614 0.1007 -0.1119 107 ARG A N 843 C CA . ARG A 107 ? 0.9789 1.5332 0.8021 -0.0849 0.1041 -0.1222 107 ARG A CA 844 C C . ARG A 107 ? 0.9261 1.5229 0.7621 -0.0888 0.1004 -0.1239 107 ARG A C 845 O O . ARG A 107 ? 0.9213 1.5293 0.7529 -0.1101 0.1040 -0.1307 107 ARG A O 846 C CB . ARG A 107 ? 1.0839 1.5966 0.8939 -0.0997 0.1148 -0.1270 107 ARG A CB 847 C CG . ARG A 107 ? 1.1956 1.6671 0.9941 -0.0953 0.1212 -0.1256 107 ARG A CG 848 C CD . ARG A 107 ? 1.3056 1.7343 1.1012 -0.0975 0.1302 -0.1239 107 ARG A CD 849 N NE . ARG A 107 ? 1.4125 1.8039 1.1982 -0.0939 0.1387 -0.1232 107 ARG A NE 850 C CZ . ARG A 107 ? 1.4608 1.8135 1.2458 -0.0917 0.1467 -0.1196 107 ARG A CZ 851 N NH1 . ARG A 107 ? 1.4808 1.8246 1.2720 -0.0940 0.1461 -0.1160 107 ARG A NH1 852 N NH2 . ARG A 107 ? 1.4190 1.7426 1.1970 -0.0861 0.1557 -0.1186 107 ARG A NH2 853 N N . ILE A 108 ? 0.8647 1.4842 0.7163 -0.0682 0.0941 -0.1175 108 ILE A N 854 C CA . ILE A 108 ? 0.8479 1.5100 0.7137 -0.0669 0.0926 -0.1182 108 ILE A CA 855 C C . ILE A 108 ? 0.8276 1.5321 0.7074 -0.0497 0.0827 -0.1135 108 ILE A C 856 O O . ILE A 108 ? 0.8160 1.5069 0.6976 -0.0290 0.0772 -0.1068 108 ILE A O 857 C CB . ILE A 108 ? 0.8365 1.4807 0.7059 -0.0558 0.0972 -0.1156 108 ILE A CB 858 C CG1 . ILE A 108 ? 0.8360 1.4400 0.6923 -0.0724 0.1060 -0.1182 108 ILE A CG1 859 C CG2 . ILE A 108 ? 0.8202 1.5106 0.7033 -0.0527 0.0982 -0.1165 108 ILE A CG2 860 C CD1 . ILE A 108 ? 0.8239 1.4031 0.6792 -0.0616 0.1088 -0.1144 108 ILE A CD1 861 N N . ASN A 109 ? 0.8197 1.5759 0.7103 -0.0587 0.0800 -0.1159 109 ASN A N 862 C CA . ASN A 109 ? 0.8145 1.6180 0.7215 -0.0421 0.0704 -0.1104 109 ASN A CA 863 C C . ASN A 109 ? 0.8054 1.6469 0.7326 -0.0281 0.0727 -0.1085 109 ASN A C 864 O O . ASN A 109 ? 0.7767 1.6490 0.7185 -0.0063 0.0660 -0.1026 109 ASN A O 865 C CB . ASN A 109 ? 0.8325 1.6749 0.7391 -0.0615 0.0633 -0.1129 109 ASN A CB 866 C CG . ASN A 109 ? 0.8504 1.6599 0.7345 -0.0709 0.0607 -0.1148 109 ASN A CG 867 O OD1 . ASN A 109 ? 0.8366 1.6209 0.7155 -0.0529 0.0578 -0.1087 109 ASN A OD1 868 N ND2 . ASN A 109 ? 0.8841 1.6928 0.7536 -0.0996 0.0621 -0.1233 109 ASN A ND2 869 N N . HIS A 110 ? 0.8022 1.6423 0.7295 -0.0399 0.0829 -0.1128 110 HIS A N 870 C CA . HIS A 110 ? 0.7911 1.6706 0.7360 -0.0279 0.0878 -0.1115 110 HIS A CA 871 C C . HIS A 110 ? 0.7913 1.6468 0.7280 -0.0339 0.1001 -0.1148 110 HIS A C 872 O O . HIS A 110 ? 0.7917 1.6326 0.7184 -0.0604 0.1059 -0.1185 110 HIS A O 873 C CB . HIS A 110 ? 0.8034 1.7515 0.7679 -0.0423 0.0853 -0.1111 110 HIS A CB 874 C CG . HIS A 110 ? 0.8099 1.8099 0.7983 -0.0238 0.0896 -0.1075 110 HIS A CG 875 N ND1 . HIS A 110 ? 0.8105 1.8740 0.8198 -0.0393 0.0925 -0.1066 110 HIS A ND1 876 C CD2 . HIS A 110 ? 0.7983 1.7960 0.7926 0.0093 0.0923 -0.1048 110 HIS A CD2 877 C CE1 . HIS A 110 ? 0.8126 1.9137 0.8416 -0.0147 0.0982 -0.1029 110 HIS A CE1 878 N NE2 . HIS A 110 ? 0.8031 1.8627 0.8214 0.0156 0.0983 -0.1026 110 HIS A NE2 879 N N . PHE A 111 ? 0.7884 1.6380 0.7272 -0.0088 0.1037 -0.1132 111 PHE A N 880 C CA . PHE A 111 ? 0.7999 1.6364 0.7308 -0.0109 0.1153 -0.1156 111 PHE A CA 881 C C . PHE A 111 ? 0.8198 1.7167 0.7698 -0.0029 0.1229 -0.1150 111 PHE A C 882 O O . PHE A 111 ? 0.8208 1.7565 0.7889 0.0174 0.1184 -0.1122 111 PHE A O 883 C CB . PHE A 111 ? 0.7831 1.5677 0.6984 0.0118 0.1144 -0.1153 111 PHE A CB 884 C CG . PHE A 111 ? 0.7778 1.5017 0.6748 0.0025 0.1105 -0.1146 111 PHE A CG 885 C CD1 . PHE A 111 ? 0.7842 1.4886 0.6713 -0.0245 0.1156 -0.1161 111 PHE A CD1 886 C CD2 . PHE A 111 ? 0.7596 1.4449 0.6501 0.0216 0.1022 -0.1116 111 PHE A CD2 887 C CE1 . PHE A 111 ? 0.7596 1.4105 0.6326 -0.0296 0.1131 -0.1145 111 PHE A CE1 888 C CE2 . PHE A 111 ? 0.7471 1.3822 0.6250 0.0140 0.0992 -0.1094 111 PHE A CE2 889 C CZ . PHE A 111 ? 0.7471 1.3663 0.6172 -0.0103 0.1050 -0.1108 111 PHE A CZ 890 N N . GLU A 112 ? 0.8441 1.7491 0.7904 -0.0176 0.1352 -0.1165 112 GLU A N 891 C CA . GLU A 112 ? 0.8742 1.8312 0.8358 -0.0069 0.1462 -0.1156 112 GLU A CA 892 C C . GLU A 112 ? 0.8639 1.7846 0.8039 0.0027 0.1568 -0.1180 112 GLU A C 893 O O . GLU A 112 ? 0.8589 1.7537 0.7828 -0.0196 0.1630 -0.1183 112 GLU A O 894 C CB . GLU A 112 ? 0.8971 1.9097 0.8762 -0.0369 0.1522 -0.1136 112 GLU A CB 895 C CG . GLU A 112 ? 0.9116 1.9811 0.9173 -0.0418 0.1421 -0.1105 112 GLU A CG 896 C CD . GLU A 112 ? 0.9163 2.0550 0.9520 -0.0173 0.1457 -0.1061 112 GLU A CD 897 O OE1 . GLU A 112 ? 0.9052 2.0602 0.9433 -0.0050 0.1602 -0.1059 112 GLU A OE1 898 O OE2 . GLU A 112 ? 0.9081 2.0858 0.9643 -0.0098 0.1343 -0.1022 112 GLU A OE2 899 N N . LYS A 113 ? 0.8585 1.7744 0.7956 0.0358 0.1584 -0.1196 113 LYS A N 900 C CA . LYS A 113 ? 0.8835 1.7621 0.7954 0.0469 0.1670 -0.1231 113 LYS A CA 901 C C . LYS A 113 ? 0.8925 1.8132 0.8077 0.0385 0.1848 -0.1227 113 LYS A C 902 O O . LYS A 113 ? 0.9076 1.8920 0.8480 0.0470 0.1920 -0.1209 113 LYS A O 903 C CB . LYS A 113 ? 0.9031 1.7619 0.8081 0.0847 0.1631 -0.1263 113 LYS A CB 904 C CG . LYS A 113 ? 0.9380 1.7534 0.8119 0.0968 0.1700 -0.1314 113 LYS A CG 905 C CD . LYS A 113 ? 0.9611 1.7155 0.8158 0.1175 0.1569 -0.1341 113 LYS A CD 906 C CE . LYS A 113 ? 0.9630 1.7341 0.8309 0.1502 0.1528 -0.1352 113 LYS A CE 907 N NZ . LYS A 113 ? 0.9631 1.6751 0.8169 0.1634 0.1368 -0.1352 113 LYS A NZ 908 N N . ILE A 114 ? 0.8964 1.7835 0.7874 0.0218 0.1918 -0.1229 114 ILE A N 909 C CA . ILE A 114 ? 0.9154 1.8356 0.8038 0.0139 0.2100 -0.1215 114 ILE A CA 910 C C . ILE A 114 ? 0.9435 1.8125 0.7946 0.0215 0.2159 -0.1244 114 ILE A C 911 O O . ILE A 114 ? 0.9657 1.7718 0.7942 0.0218 0.2046 -0.1258 114 ILE A O 912 C CB . ILE A 114 ? 0.9153 1.8600 0.8135 -0.0258 0.2147 -0.1158 114 ILE A CB 913 C CG1 . ILE A 114 ? 0.9234 1.8038 0.7999 -0.0488 0.2054 -0.1149 114 ILE A CG1 914 C CG2 . ILE A 114 ? 0.9050 1.9117 0.8399 -0.0348 0.2101 -0.1131 114 ILE A CG2 915 C CD1 . ILE A 114 ? 0.9432 1.8300 0.8167 -0.0858 0.2134 -0.1097 114 ILE A CD1 916 N N . GLN A 115 ? 0.9512 1.8504 0.7964 0.0268 0.2336 -0.1246 115 GLN A N 917 C CA . GLN A 115 ? 0.9723 1.8295 0.7789 0.0340 0.2409 -0.1275 115 GLN A CA 918 C C . GLN A 115 ? 0.9776 1.8201 0.7685 -0.0003 0.2467 -0.1206 115 GLN A C 919 O O . GLN A 115 ? 0.9580 1.8488 0.7669 -0.0222 0.2580 -0.1145 115 GLN A O 920 C CB . GLN A 115 ? 0.9886 1.8859 0.7935 0.0600 0.2592 -0.1317 115 GLN A CB 921 C CG . GLN A 115 ? 1.0185 1.8718 0.7782 0.0709 0.2669 -0.1367 115 GLN A CG 922 C CD . GLN A 115 ? 1.0332 1.9281 0.7897 0.0969 0.2880 -0.1415 115 GLN A CD 923 O OE1 . GLN A 115 ? 1.0495 1.9174 0.7846 0.1290 0.2881 -0.1512 115 GLN A OE1 924 N NE2 . GLN A 115 ? 1.0220 1.9828 0.7995 0.0832 0.3067 -0.1347 115 GLN A NE2 925 N N . ILE A 116 ? 0.9873 1.7636 0.7452 -0.0051 0.2386 -0.1204 116 ILE A N 926 C CA . ILE A 116 ? 1.0069 1.7608 0.7466 -0.0353 0.2426 -0.1124 116 ILE A CA 927 C C . ILE A 116 ? 1.0542 1.7838 0.7544 -0.0291 0.2523 -0.1124 116 ILE A C 928 O O . ILE A 116 ? 1.0973 1.8404 0.7874 -0.0496 0.2655 -0.1052 116 ILE A O 929 C CB . ILE A 116 ? 0.9798 1.6800 0.7159 -0.0520 0.2253 -0.1088 116 ILE A CB 930 C CG1 . ILE A 116 ? 0.9734 1.6221 0.6955 -0.0291 0.2090 -0.1139 116 ILE A CG1 931 C CG2 . ILE A 116 ? 0.9436 1.6725 0.7134 -0.0684 0.2206 -0.1073 116 ILE A CG2 932 C CD1 . ILE A 116 ? 0.9633 1.5577 0.6780 -0.0434 0.1945 -0.1086 116 ILE A CD1 933 N N . ILE A 117 ? 1.0801 1.7731 0.7560 -0.0023 0.2457 -0.1202 117 ILE A N 934 C CA . ILE A 117 ? 1.1205 1.7911 0.7545 0.0067 0.2546 -0.1225 117 ILE A CA 935 C C . ILE A 117 ? 1.1269 1.8124 0.7542 0.0426 0.2616 -0.1346 117 ILE A C 936 O O . ILE A 117 ? 1.1020 1.7477 0.7183 0.0635 0.2472 -0.1424 117 ILE A O 937 C CB . ILE A 117 ? 1.1462 1.7438 0.7455 0.0016 0.2377 -0.1203 117 ILE A CB 938 C CG1 . ILE A 117 ? 1.1320 1.7113 0.7422 -0.0294 0.2294 -0.1086 117 ILE A CG1 939 C CG2 . ILE A 117 ? 1.1907 1.7685 0.7434 0.0057 0.2471 -0.1213 117 ILE A CG2 940 C CD1 . ILE A 117 ? 1.1522 1.6665 0.7325 -0.0359 0.2140 -0.1032 117 ILE A CD1 941 N N . PRO A 118 ? 1.1446 1.8872 0.7789 0.0501 0.2843 -0.1356 118 PRO A N 942 C CA . PRO A 118 ? 1.1631 1.9251 0.7927 0.0867 0.2949 -0.1469 118 PRO A CA 943 C C . PRO A 118 ? 1.2006 1.8984 0.7791 0.1074 0.2889 -0.1574 118 PRO A C 944 O O . PRO A 118 ? 1.2029 1.8645 0.7426 0.0937 0.2889 -0.1548 118 PRO A O 945 C CB . PRO A 118 ? 1.1828 2.0103 0.8195 0.0832 0.3228 -0.1428 118 PRO A CB 946 C CG . PRO A 118 ? 1.1580 2.0176 0.8236 0.0451 0.3236 -0.1291 118 PRO A CG 947 C CD . PRO A 118 ? 1.1516 1.9449 0.8004 0.0236 0.3019 -0.1250 118 PRO A CD 948 N N . LYS A 119 ? 1.2221 1.9050 0.7996 0.1394 0.2828 -0.1688 119 LYS A N 949 C CA . LYS A 119 ? 1.2806 1.8987 0.8095 0.1596 0.2745 -0.1805 119 LYS A CA 950 C C . LYS A 119 ? 1.3409 1.9616 0.8267 0.1692 0.2961 -0.1866 119 LYS A C 951 O O . LYS A 119 ? 1.3911 1.9545 0.8261 0.1702 0.2892 -0.1924 119 LYS A O 952 C CB . LYS A 119 ? 1.2891 1.8966 0.8287 0.1929 0.2666 -0.1910 119 LYS A CB 953 C CG . LYS A 119 ? 1.3493 1.8828 0.8401 0.2118 0.2540 -0.2037 119 LYS A CG 954 C CD . LYS A 119 ? 1.3790 1.9020 0.8846 0.2426 0.2457 -0.2120 119 LYS A CD 955 C CE . LYS A 119 ? 1.4417 1.8846 0.8997 0.2570 0.2293 -0.2240 119 LYS A CE 956 N NZ . LYS A 119 ? 1.4567 1.8821 0.9305 0.2829 0.2179 -0.2295 119 LYS A NZ 957 N N . SER A 120 ? 1.3467 2.0362 0.8529 0.1754 0.3220 -0.1847 120 SER A N 958 C CA . SER A 120 ? 1.3995 2.1019 0.8685 0.1874 0.3471 -0.1902 120 SER A CA 959 C C . SER A 120 ? 1.3959 2.1189 0.8552 0.1534 0.3591 -0.1766 120 SER A C 960 O O . SER A 120 ? 1.4247 2.1908 0.8750 0.1572 0.3858 -0.1754 120 SER A O 961 C CB . SER A 120 ? 1.4097 2.1788 0.9078 0.2179 0.3707 -0.1953 120 SER A CB 962 O OG . SER A 120 ? 1.3973 2.1558 0.9178 0.2446 0.3574 -0.2031 120 SER A OG 963 N N . SER A 121 ? 1.3713 2.0641 0.8332 0.1209 0.3402 -0.1656 121 SER A N 964 C CA . SER A 121 ? 1.3735 2.0712 0.8200 0.0880 0.3481 -0.1519 121 SER A CA 965 C C . SER A 121 ? 1.3938 2.0151 0.7870 0.0773 0.3308 -0.1513 121 SER A C 966 O O . SER A 121 ? 1.3918 2.0045 0.7700 0.0492 0.3318 -0.1382 121 SER A O 967 C CB . SER A 121 ? 1.3154 2.0472 0.8116 0.0563 0.3431 -0.1371 121 SER A CB 968 O OG . SER A 121 ? 1.2800 1.9662 0.7878 0.0480 0.3154 -0.1360 121 SER A OG 969 N N . TRP A 122 ? 1.4008 1.9671 0.7659 0.0992 0.3142 -0.1645 122 TRP A N 970 C CA . TRP A 122 ? 1.4264 1.9215 0.7408 0.0911 0.2952 -0.1647 122 TRP A CA 971 C C . TRP A 122 ? 1.5051 1.9834 0.7586 0.1075 0.3103 -0.1752 122 TRP A C 972 O O . TRP A 122 ? 1.5546 1.9901 0.7741 0.1312 0.3020 -0.1910 122 TRP A O 973 C CB . TRP A 122 ? 1.4017 1.8450 0.7199 0.1019 0.2664 -0.1721 122 TRP A CB 974 C CG . TRP A 122 ? 1.3406 1.7910 0.7105 0.0850 0.2501 -0.1616 122 TRP A CG 975 C CD1 . TRP A 122 ? 1.2922 1.7663 0.7078 0.0966 0.2458 -0.1649 122 TRP A CD1 976 C CD2 . TRP A 122 ? 1.3126 1.7442 0.6909 0.0546 0.2363 -0.1460 122 TRP A CD2 977 N NE1 . TRP A 122 ? 1.2402 1.7115 0.6900 0.0747 0.2309 -0.1534 122 TRP A NE1 978 C CE2 . TRP A 122 ? 1.2529 1.6976 0.6814 0.0496 0.2253 -0.1421 122 TRP A CE2 979 C CE3 . TRP A 122 ? 1.3311 1.7351 0.6783 0.0322 0.2322 -0.1345 122 TRP A CE3 980 C CZ2 . TRP A 122 ? 1.2196 1.6497 0.6674 0.0242 0.2122 -0.1286 122 TRP A CZ2 981 C CZ3 . TRP A 122 ? 1.3002 1.6900 0.6691 0.0075 0.2182 -0.1198 122 TRP A CZ3 982 C CH2 . TRP A 122 ? 1.2436 1.6459 0.6622 0.0043 0.2091 -0.1177 122 TRP A CH2 983 N N . SER A 123 ? 1.5213 2.0319 0.7589 0.0940 0.3329 -0.1665 123 SER A N 984 C CA . SER A 123 ? 1.5769 2.0822 0.7574 0.1096 0.3530 -0.1758 123 SER A CA 985 C C . SER A 123 ? 1.6419 2.0726 0.7549 0.1037 0.3343 -0.1786 123 SER A C 986 O O . SER A 123 ? 1.7060 2.1112 0.7646 0.1243 0.3422 -0.1934 123 SER A O 987 C CB . SER A 123 ? 1.5737 2.1413 0.7607 0.0947 0.3839 -0.1631 123 SER A CB 988 O OG . SER A 123 ? 1.5256 2.0995 0.7346 0.0573 0.3760 -0.1423 123 SER A OG 989 N N . SER A 124 ? 1.6256 2.0218 0.7418 0.0766 0.3094 -0.1646 124 SER A N 990 C CA . SER A 124 ? 1.6622 1.9916 0.7197 0.0675 0.2882 -0.1636 124 SER A CA 991 C C . SER A 124 ? 1.6496 1.9206 0.6995 0.0793 0.2568 -0.1751 124 SER A C 992 O O . SER A 124 ? 1.6658 1.8814 0.6697 0.0721 0.2356 -0.1748 124 SER A O 993 C CB . SER A 124 ? 1.6493 1.9723 0.7137 0.0324 0.2778 -0.1399 124 SER A CB 994 O OG . SER A 124 ? 1.6562 2.0287 0.7255 0.0179 0.3054 -0.1276 124 SER A OG 995 N N . HIS A 125 ? 1.6143 1.8986 0.7094 0.0959 0.2528 -0.1837 125 HIS A N 996 C CA . HIS A 125 ? 1.6149 1.8478 0.7096 0.1056 0.2237 -0.1927 125 HIS A CA 997 C C . HIS A 125 ? 1.6352 1.8783 0.7433 0.1384 0.2325 -0.2113 125 HIS A C 998 O O . HIS A 125 ? 1.6252 1.9261 0.7680 0.1501 0.2566 -0.2125 125 HIS A O 999 C CB . HIS A 125 ? 1.5337 1.7655 0.6813 0.0857 0.2019 -0.1775 125 HIS A CB 1000 C CG . HIS A 125 ? 1.5194 1.7405 0.6611 0.0552 0.1924 -0.1576 125 HIS A CG 1001 N ND1 . HIS A 125 ? 1.5000 1.7641 0.6614 0.0368 0.2109 -0.1431 125 HIS A ND1 1002 C CD2 . HIS A 125 ? 1.5252 1.6975 0.6452 0.0400 0.1657 -0.1488 125 HIS A CD2 1003 C CE1 . HIS A 125 ? 1.5052 1.7436 0.6549 0.0130 0.1966 -0.1265 125 HIS A CE1 1004 N NE2 . HIS A 125 ? 1.5225 1.7075 0.6485 0.0152 0.1691 -0.1292 125 HIS A NE2 1005 N N . GLU A 126 ? 1.6747 1.8615 0.7567 0.1527 0.2119 -0.2248 126 GLU A N 1006 C CA . GLU A 126 ? 1.6784 1.8648 0.7733 0.1841 0.2161 -0.2413 126 GLU A CA 1007 C C . GLU A 126 ? 1.6036 1.8133 0.7676 0.1800 0.2042 -0.2321 126 GLU A C 1008 O O . GLU A 126 ? 1.5879 1.7686 0.7667 0.1614 0.1780 -0.2224 126 GLU A O 1009 C CB . GLU A 126 ? 1.7514 1.8632 0.7907 0.1980 0.1967 -0.2586 126 GLU A CB 1010 C CG . GLU A 126 ? 1.7853 1.8872 0.8282 0.2329 0.2021 -0.2769 126 GLU A CG 1011 C CD . GLU A 126 ? 1.8122 1.9663 0.8572 0.2599 0.2394 -0.2859 126 GLU A CD 1012 O OE1 . GLU A 126 ? 1.8369 1.9862 0.8291 0.2662 0.2577 -0.2944 126 GLU A OE1 1013 O OE2 . GLU A 126 ? 1.7777 1.9794 0.8776 0.2749 0.2503 -0.2838 126 GLU A OE2 1014 N N . ALA A 127 ? 1.5544 1.8184 0.7605 0.1975 0.2239 -0.2344 127 ALA A N 1015 C CA . ALA A 127 ? 1.4618 1.7565 0.7331 0.1930 0.2158 -0.2249 127 ALA A CA 1016 C C . ALA A 127 ? 1.4515 1.7509 0.7432 0.2250 0.2175 -0.2365 127 ALA A C 1017 O O . ALA A 127 ? 1.4037 1.7398 0.7491 0.2254 0.2161 -0.2294 127 ALA A O 1018 C CB . ALA A 127 ? 1.4135 1.7790 0.7272 0.1761 0.2350 -0.2108 127 ALA A CB 1019 N N . SER A 128 ? 1.5043 1.7640 0.7509 0.2517 0.2200 -0.2543 128 SER A N 1020 C CA . SER A 128 ? 1.5021 1.7586 0.7626 0.2852 0.2218 -0.2657 128 SER A CA 1021 C C . SER A 128 ? 1.5273 1.7010 0.7459 0.2967 0.1986 -0.2789 128 SER A C 1022 O O . SER A 128 ? 1.5463 1.7038 0.7626 0.3271 0.2007 -0.2907 128 SER A O 1023 C CB . SER A 128 ? 1.5393 1.8416 0.7947 0.3148 0.2552 -0.2756 128 SER A CB 1024 O OG . SER A 128 ? 1.4944 1.8793 0.8091 0.3096 0.2718 -0.2626 128 SER A OG 1025 N N . LEU A 129 ? 1.5199 1.6417 0.7074 0.2719 0.1755 -0.2756 129 LEU A N 1026 C CA . LEU A 129 ? 1.5539 1.5972 0.7049 0.2754 0.1491 -0.2853 129 LEU A CA 1027 C C . LEU A 129 ? 1.5037 1.5283 0.6874 0.2492 0.1190 -0.2699 129 LEU A C 1028 O O . LEU A 129 ? 1.5376 1.4998 0.6939 0.2426 0.0935 -0.2734 129 LEU A O 1029 C CB . LEU A 129 ? 1.6251 1.6178 0.7023 0.2702 0.1461 -0.2965 129 LEU A CB 1030 C CG . LEU A 129 ? 1.6805 1.6842 0.7148 0.2966 0.1767 -0.3134 129 LEU A CG 1031 C CD1 . LEU A 129 ? 1.7503 1.6955 0.7060 0.2889 0.1694 -0.3246 129 LEU A CD1 1032 C CD2 . LEU A 129 ? 1.7092 1.7047 0.7458 0.3362 0.1877 -0.3295 129 LEU A CD2 1033 N N . GLY A 130 ? 1.4357 1.5149 0.6778 0.2345 0.1224 -0.2530 130 GLY A N 1034 C CA . GLY A 130 ? 1.3764 1.4462 0.6533 0.2104 0.0982 -0.2371 130 GLY A CA 1035 C C . GLY A 130 ? 1.3479 1.4086 0.6583 0.2230 0.0862 -0.2365 130 GLY A C 1036 O O . GLY A 130 ? 1.2704 1.3725 0.6334 0.2172 0.0876 -0.2244 130 GLY A O 1037 N N . VAL A 131 ? 1.3895 1.3924 0.6660 0.2388 0.0736 -0.2491 131 VAL A N 1038 C CA . VAL A 131 ? 1.3774 1.3639 0.6769 0.2550 0.0634 -0.2501 131 VAL A CA 1039 C C . VAL A 131 ? 1.4054 1.3204 0.6816 0.2438 0.0325 -0.2503 131 VAL A C 1040 O O . VAL A 131 ? 1.4386 1.3149 0.6755 0.2273 0.0194 -0.2526 131 VAL A O 1041 C CB . VAL A 131 ? 1.4166 1.4057 0.7014 0.2931 0.0825 -0.2665 131 VAL A CB 1042 C CG1 . VAL A 131 ? 1.3783 1.4458 0.6933 0.3033 0.1124 -0.2641 131 VAL A CG1 1043 C CG2 . VAL A 131 ? 1.4960 1.4255 0.7108 0.3061 0.0827 -0.2864 131 VAL A CG2 1044 N N . SER A 132 ? 1.3962 1.2956 0.6974 0.2520 0.0204 -0.2466 132 SER A N 1045 C CA . SER A 132 ? 1.4136 1.2486 0.6996 0.2404 -0.0092 -0.2447 132 SER A CA 1046 C C . SER A 132 ? 1.4379 1.2498 0.7357 0.2621 -0.0143 -0.2474 132 SER A C 1047 O O . SER A 132 ? 1.4042 1.2612 0.7400 0.2791 0.0005 -0.2433 132 SER A O 1048 C CB . SER A 132 ? 1.3452 1.1933 0.6672 0.2078 -0.0268 -0.2238 132 SER A CB 1049 O OG . SER A 132 ? 1.3389 1.1378 0.6613 0.1980 -0.0536 -0.2182 132 SER A OG 1050 N N . SER A 133 ? 1.4995 1.2402 0.7643 0.2600 -0.0366 -0.2533 133 SER A N 1051 C CA . SER A 133 ? 1.5298 1.2362 0.8003 0.2781 -0.0449 -0.2549 133 SER A CA 1052 C C . SER A 133 ? 1.4769 1.2087 0.8047 0.2640 -0.0563 -0.2328 133 SER A C 1053 O O . SER A 133 ? 1.4806 1.2037 0.8250 0.2808 -0.0578 -0.2300 133 SER A O 1054 C CB . SER A 133 ? 1.6114 1.2293 0.8266 0.2756 -0.0672 -0.2674 133 SER A CB 1055 O OG . SER A 133 ? 1.6121 1.2078 0.8235 0.2397 -0.0922 -0.2570 133 SER A OG 1056 N N . ALA A 134 ? 1.4410 1.2029 0.7973 0.2343 -0.0636 -0.2168 134 ALA A N 1057 C CA . ALA A 134 ? 1.3942 1.1867 0.8048 0.2206 -0.0708 -0.1959 134 ALA A CA 1058 C C . ALA A 134 ? 1.3545 1.2144 0.8073 0.2362 -0.0486 -0.1908 134 ALA A C 1059 O O . ALA A 134 ? 1.3107 1.1894 0.8017 0.2343 -0.0526 -0.1770 134 ALA A O 1060 C CB . ALA A 134 ? 1.3582 1.1638 0.7856 0.1872 -0.0826 -0.1812 134 ALA A CB 1061 N N . CYS A 135 ? 1.3715 1.2688 0.8168 0.2504 -0.0258 -0.2012 135 CYS A N 1062 C CA . CYS A 135 ? 1.3457 1.3086 0.8283 0.2657 -0.0051 -0.1978 135 CYS A CA 1063 C C . CYS A 135 ? 1.3651 1.3264 0.8281 0.3020 0.0107 -0.2134 135 CYS A C 1064 O O . CYS A 135 ? 1.3504 1.3441 0.8032 0.3125 0.0312 -0.2229 135 CYS A O 1065 C CB . CYS A 135 ? 1.3414 1.3609 0.8410 0.2490 0.0096 -0.1934 135 CYS A CB 1066 S SG . CYS A 135 ? 1.3541 1.3750 0.8755 0.2100 -0.0064 -0.1756 135 CYS A SG 1067 N N . PRO A 136 ? 1.3748 1.2981 0.8328 0.3220 0.0019 -0.2152 136 PRO A N 1068 C CA . PRO A 136 ? 1.4155 1.3303 0.8537 0.3599 0.0162 -0.2298 136 PRO A CA 1069 C C . PRO A 136 ? 1.3671 1.3553 0.8479 0.3806 0.0358 -0.2243 136 PRO A C 1070 O O . PRO A 136 ? 1.3020 1.3340 0.8269 0.3676 0.0328 -0.2081 136 PRO A O 1071 C CB . PRO A 136 ? 1.4632 1.3072 0.8840 0.3697 -0.0036 -0.2303 136 PRO A CB 1072 C CG . PRO A 136 ? 1.4105 1.2629 0.8688 0.3434 -0.0212 -0.2095 136 PRO A CG 1073 C CD . PRO A 136 ? 1.3660 1.2486 0.8343 0.3106 -0.0217 -0.2033 136 PRO A CD 1074 N N . TYR A 137 ? 1.4012 1.4026 0.8676 0.4129 0.0555 -0.2376 137 TYR A N 1075 C CA . TYR A 137 ? 1.3772 1.4469 0.8828 0.4374 0.0734 -0.2329 137 TYR A CA 1076 C C . TYR A 137 ? 1.4360 1.4842 0.9163 0.4810 0.0867 -0.2479 137 TYR A C 1077 O O . TYR A 137 ? 1.4862 1.5218 0.9296 0.4921 0.1012 -0.2643 137 TYR A O 1078 C CB . TYR A 137 ? 1.3343 1.4825 0.8648 0.4234 0.0923 -0.2296 137 TYR A CB 1079 C CG . TYR A 137 ? 1.3157 1.5407 0.8875 0.4463 0.1106 -0.2246 137 TYR A CG 1080 C CD1 . TYR A 137 ? 1.2695 1.5326 0.8873 0.4437 0.1027 -0.2084 137 TYR A CD1 1081 C CD2 . TYR A 137 ? 1.3299 1.5919 0.8951 0.4701 0.1355 -0.2352 137 TYR A CD2 1082 C CE1 . TYR A 137 ? 1.2449 1.5808 0.9011 0.4633 0.1170 -0.2027 137 TYR A CE1 1083 C CE2 . TYR A 137 ? 1.3059 1.6435 0.9129 0.4903 0.1513 -0.2289 137 TYR A CE2 1084 C CZ . TYR A 137 ? 1.2626 1.6370 0.9153 0.4864 0.1409 -0.2126 137 TYR A CZ 1085 O OH . TYR A 137 ? 1.2359 1.6876 0.9306 0.5051 0.1542 -0.2055 137 TYR A OH 1086 N N . GLN A 138 ? 1.4415 1.4845 0.9404 0.5065 0.0823 -0.2420 138 GLN A N 1087 C CA . GLN A 138 ? 1.5082 1.5262 0.9859 0.5519 0.0939 -0.2547 138 GLN A CA 1088 C C . GLN A 138 ? 1.5867 1.5152 0.9975 0.5590 0.0902 -0.2757 138 GLN A C 1089 O O . GLN A 138 ? 1.6325 1.5535 1.0142 0.5896 0.1096 -0.2926 138 GLN A O 1090 C CB . GLN A 138 ? 1.4968 1.5966 0.9988 0.5767 0.1231 -0.2577 138 GLN A CB 1091 C CG . GLN A 138 ? 1.4297 1.6205 0.9958 0.5678 0.1262 -0.2380 138 GLN A CG 1092 C CD . GLN A 138 ? 1.4255 1.6957 1.0203 0.5980 0.1525 -0.2388 138 GLN A CD 1093 O OE1 . GLN A 138 ? 1.4549 1.7185 1.0228 0.6251 0.1720 -0.2542 138 GLN A OE1 1094 N NE2 . GLN A 138 ? 1.3842 1.7319 1.0341 0.5931 0.1531 -0.2217 138 GLN A NE2 1095 N N . GLY A 139 ? 1.5936 1.4560 0.9800 0.5302 0.0653 -0.2743 139 GLY A N 1096 C CA . GLY A 139 ? 1.6604 1.4306 0.9817 0.5319 0.0558 -0.2930 139 GLY A CA 1097 C C . GLY A 139 ? 1.6604 1.4244 0.9452 0.5092 0.0600 -0.3046 139 GLY A C 1098 O O . GLY A 139 ? 1.7066 1.3940 0.9370 0.5011 0.0469 -0.3181 139 GLY A O 1099 N N . LYS A 140 ? 1.6021 1.4450 0.9151 0.4977 0.0773 -0.2990 140 LYS A N 1100 C CA . LYS A 140 ? 1.6276 1.4729 0.9079 0.4783 0.0845 -0.3082 140 LYS A CA 1101 C C . LYS A 140 ? 1.5510 1.4221 0.8575 0.4334 0.0700 -0.2916 140 LYS A C 1102 O O . LYS A 140 ? 1.4841 1.3941 0.8415 0.4210 0.0630 -0.2735 140 LYS A O 1103 C CB . LYS A 140 ? 1.6426 1.5558 0.9298 0.5002 0.1180 -0.3150 140 LYS A CB 1104 C CG . LYS A 140 ? 1.7452 1.6249 0.9900 0.5440 0.1360 -0.3363 140 LYS A CG 1105 C CD . LYS A 140 ? 1.7537 1.7154 1.0222 0.5704 0.1706 -0.3382 140 LYS A CD 1106 C CE . LYS A 140 ? 1.7421 1.7494 1.0618 0.6028 0.1787 -0.3288 140 LYS A CE 1107 N NZ . LYS A 140 ? 1.6717 1.7266 1.0530 0.5782 0.1633 -0.3052 140 LYS A NZ 1108 N N . SER A 141 ? 1.5720 1.4202 0.8414 0.4104 0.0659 -0.2978 141 SER A N 1109 C CA . SER A 141 ? 1.5133 1.3829 0.8031 0.3695 0.0534 -0.2826 141 SER A CA 1110 C C . SER A 141 ? 1.4475 1.4062 0.7802 0.3632 0.0749 -0.2726 141 SER A C 1111 O O . SER A 141 ? 1.4706 1.4635 0.7924 0.3795 0.0994 -0.2816 141 SER A O 1112 C CB . SER A 141 ? 1.5551 1.3736 0.7897 0.3494 0.0425 -0.2919 141 SER A CB 1113 O OG . SER A 141 ? 1.6184 1.3526 0.8120 0.3512 0.0201 -0.3013 141 SER A OG 1114 N N . SER A 142 ? 1.3832 1.3785 0.7634 0.3391 0.0661 -0.2539 142 SER A N 1115 C CA . SER A 142 ? 1.3266 1.4025 0.7489 0.3301 0.0838 -0.2437 142 SER A CA 1116 C C . SER A 142 ? 1.2801 1.3641 0.7197 0.2915 0.0709 -0.2292 142 SER A C 1117 O O . SER A 142 ? 1.2992 1.3317 0.7111 0.2736 0.0525 -0.2291 142 SER A O 1118 C CB . SER A 142 ? 1.2942 1.4174 0.7649 0.3486 0.0904 -0.2359 142 SER A CB 1119 O OG . SER A 142 ? 1.2528 1.4548 0.7597 0.3431 0.1092 -0.2289 142 SER A OG 1120 N N . PHE A 143 ? 1.2209 1.3685 0.7050 0.2788 0.0802 -0.2169 143 PHE A N 1121 C CA . PHE A 143 ? 1.1817 1.3388 0.6841 0.2448 0.0706 -0.2031 143 PHE A CA 1122 C C . PHE A 143 ? 1.1338 1.3562 0.6877 0.2368 0.0796 -0.1912 143 PHE A C 1123 O O . PHE A 143 ? 1.1500 1.4185 0.7236 0.2549 0.0953 -0.1937 143 PHE A O 1124 C CB . PHE A 143 ? 1.1892 1.3428 0.6608 0.2285 0.0772 -0.2062 143 PHE A CB 1125 C CG . PHE A 143 ? 1.1465 1.2855 0.6237 0.1966 0.0616 -0.1934 143 PHE A CG 1126 C CD1 . PHE A 143 ? 1.1515 1.2352 0.6153 0.1870 0.0369 -0.1902 143 PHE A CD1 1127 C CD2 . PHE A 143 ? 1.1045 1.2846 0.6008 0.1761 0.0716 -0.1840 143 PHE A CD2 1128 C CE1 . PHE A 143 ? 1.1322 1.2064 0.6045 0.1598 0.0231 -0.1771 143 PHE A CE1 1129 C CE2 . PHE A 143 ? 1.0874 1.2524 0.5891 0.1497 0.0581 -0.1718 143 PHE A CE2 1130 C CZ . PHE A 143 ? 1.1021 1.2163 0.5933 0.1426 0.0341 -0.1681 143 PHE A CZ 1131 N N . PHE A 144 ? 1.0897 1.3155 0.6648 0.2099 0.0693 -0.1783 144 PHE A N 1132 C CA . PHE A 144 ? 1.0364 1.3184 0.6539 0.1972 0.0773 -0.1679 144 PHE A CA 1133 C C . PHE A 144 ? 1.0287 1.3655 0.6508 0.2010 0.1007 -0.1725 144 PHE A C 1134 O O . PHE A 144 ? 1.0445 1.3812 0.6452 0.1898 0.1090 -0.1748 144 PHE A O 1135 C CB . PHE A 144 ? 1.0098 1.2831 0.6366 0.1668 0.0680 -0.1564 144 PHE A CB 1136 C CG . PHE A 144 ? 1.0091 1.2361 0.6367 0.1599 0.0459 -0.1492 144 PHE A CG 1137 C CD1 . PHE A 144 ? 0.9853 1.2183 0.6414 0.1638 0.0383 -0.1419 144 PHE A CD1 1138 C CD2 . PHE A 144 ? 1.0409 1.2210 0.6415 0.1481 0.0323 -0.1482 144 PHE A CD2 1139 C CE1 . PHE A 144 ? 0.9906 1.1847 0.6495 0.1560 0.0193 -0.1336 144 PHE A CE1 1140 C CE2 . PHE A 144 ? 1.0371 1.1800 0.6425 0.1399 0.0117 -0.1399 144 PHE A CE2 1141 C CZ . PHE A 144 ? 1.0109 1.1611 0.6462 0.1438 0.0060 -0.1324 144 PHE A CZ 1142 N N . ARG A 145 ? 1.0079 1.3930 0.6586 0.2161 0.1108 -0.1723 145 ARG A N 1143 C CA . ARG A 145 ? 0.9971 1.4389 0.6556 0.2234 0.1332 -0.1764 145 ARG A CA 1144 C C . ARG A 145 ? 0.9957 1.4757 0.6671 0.1946 0.1431 -0.1695 145 ARG A C 1145 O O . ARG A 145 ? 1.0331 1.5484 0.6999 0.1954 0.1615 -0.1727 145 ARG A O 1146 C CB . ARG A 145 ? 0.9598 1.4495 0.6524 0.2443 0.1387 -0.1748 145 ARG A CB 1147 C CG . ARG A 145 ? 0.9793 1.4353 0.6608 0.2764 0.1315 -0.1810 145 ARG A CG 1148 C CD . ARG A 145 ? 0.9779 1.4895 0.6862 0.3032 0.1443 -0.1815 145 ARG A CD 1149 N NE . ARG A 145 ? 1.0178 1.4949 0.7179 0.3349 0.1364 -0.1856 145 ARG A NE 1150 C CZ . ARG A 145 ? 1.0836 1.5183 0.7476 0.3600 0.1406 -0.1984 145 ARG A CZ 1151 N NH1 . ARG A 145 ? 1.1138 1.5359 0.7443 0.3575 0.1527 -0.2086 145 ARG A NH1 1152 N NH2 . ARG A 145 ? 1.1253 1.5263 0.7837 0.3878 0.1324 -0.2009 145 ARG A NH2 1153 N N . ASN A 146 ? 0.9975 1.4703 0.6846 0.1696 0.1322 -0.1598 146 ASN A N 1154 C CA . ASN A 146 ? 0.9778 1.4856 0.6799 0.1424 0.1411 -0.1530 146 ASN A CA 1155 C C . ASN A 146 ? 0.9758 1.4529 0.6491 0.1229 0.1419 -0.1514 146 ASN A C 1156 O O . ASN A 146 ? 0.9432 1.4453 0.6232 0.1014 0.1513 -0.1460 146 ASN A O 1157 C CB . ASN A 146 ? 0.9477 1.4674 0.6815 0.1266 0.1317 -0.1441 146 ASN A CB 1158 C CG . ASN A 146 ? 0.9467 1.5088 0.7104 0.1421 0.1327 -0.1438 146 ASN A CG 1159 O OD1 . ASN A 146 ? 0.9765 1.5780 0.7467 0.1590 0.1448 -0.1483 146 ASN A OD1 1160 N ND2 . ASN A 146 ? 0.9499 1.5063 0.7323 0.1370 0.1202 -0.1376 146 ASN A ND2 1161 N N . VAL A 147 ? 1.0033 1.4259 0.6437 0.1298 0.1313 -0.1553 147 VAL A N 1162 C CA . VAL A 147 ? 1.0271 1.4190 0.6363 0.1136 0.1302 -0.1532 147 VAL A CA 1163 C C . VAL A 147 ? 1.0707 1.4336 0.6364 0.1308 0.1330 -0.1642 147 VAL A C 1164 O O . VAL A 147 ? 1.1001 1.4440 0.6562 0.1542 0.1283 -0.1731 147 VAL A O 1165 C CB . VAL A 147 ? 1.0212 1.3707 0.6320 0.0966 0.1104 -0.1440 147 VAL A CB 1166 C CG1 . VAL A 147 ? 0.9779 1.3546 0.6256 0.0786 0.1112 -0.1342 147 VAL A CG1 1167 C CG2 . VAL A 147 ? 1.0342 1.3430 0.6401 0.1114 0.0920 -0.1468 147 VAL A CG2 1168 N N . VAL A 148 ? 1.0873 1.4441 0.6242 0.1188 0.1407 -0.1634 148 VAL A N 1169 C CA . VAL A 148 ? 1.1309 1.4644 0.6213 0.1333 0.1468 -0.1745 148 VAL A CA 1170 C C . VAL A 148 ? 1.1533 1.4253 0.6064 0.1225 0.1274 -0.1728 148 VAL A C 1171 O O . VAL A 148 ? 1.1625 1.4280 0.6121 0.0992 0.1234 -0.1619 148 VAL A O 1172 C CB . VAL A 148 ? 1.1406 1.5154 0.6207 0.1276 0.1714 -0.1742 148 VAL A CB 1173 C CG1 . VAL A 148 ? 1.2103 1.5649 0.6409 0.1466 0.1811 -0.1872 148 VAL A CG1 1174 C CG2 . VAL A 148 ? 1.1069 1.5502 0.6304 0.1319 0.1890 -0.1724 148 VAL A CG2 1175 N N . TRP A 149 ? 1.1735 1.3998 0.5987 0.1391 0.1146 -0.1830 149 TRP A N 1176 C CA . TRP A 149 ? 1.2056 1.3734 0.5920 0.1292 0.0943 -0.1825 149 TRP A CA 1177 C C . TRP A 149 ? 1.2651 1.4207 0.5978 0.1322 0.1057 -0.1911 149 TRP A C 1178 O O . TRP A 149 ? 1.2977 1.4339 0.5961 0.1539 0.1110 -0.2067 149 TRP A O 1179 C CB . TRP A 149 ? 1.2164 1.3381 0.5961 0.1423 0.0738 -0.1892 149 TRP A CB 1180 C CG . TRP A 149 ? 1.2494 1.3112 0.5923 0.1307 0.0493 -0.1884 149 TRP A CG 1181 C CD1 . TRP A 149 ? 1.2605 1.3073 0.5792 0.1104 0.0422 -0.1807 149 TRP A CD1 1182 C CD2 . TRP A 149 ? 1.2708 1.2812 0.5993 0.1371 0.0269 -0.1939 149 TRP A CD2 1183 N NE1 . TRP A 149 ? 1.2946 1.2867 0.5853 0.1040 0.0162 -0.1812 149 TRP A NE1 1184 C CE2 . TRP A 149 ? 1.2975 1.2658 0.5937 0.1190 0.0063 -0.1895 149 TRP A CE2 1185 C CE3 . TRP A 149 ? 1.2733 1.2683 0.6128 0.1556 0.0214 -0.2010 149 TRP A CE3 1186 C CZ2 . TRP A 149 ? 1.3283 1.2416 0.6039 0.1170 -0.0198 -0.1926 149 TRP A CZ2 1187 C CZ3 . TRP A 149 ? 1.3084 1.2450 0.6259 0.1539 -0.0036 -0.2040 149 TRP A CZ3 1188 C CH2 . TRP A 149 ? 1.3343 1.2315 0.6207 0.1338 -0.0241 -0.2000 149 TRP A CH2 1189 N N . LEU A 150 ? 1.2696 1.4347 0.5934 0.1106 0.1097 -0.1804 150 LEU A N 1190 C CA . LEU A 150 ? 1.3201 1.4814 0.5948 0.1103 0.1232 -0.1854 150 LEU A CA 1191 C C . LEU A 150 ? 1.3773 1.4761 0.5989 0.1055 0.1016 -0.1889 150 LEU A C 1192 O O . LEU A 150 ? 1.3659 1.4361 0.5960 0.0893 0.0771 -0.1782 150 LEU A O 1193 C CB . LEU A 150 ? 1.3035 1.5003 0.5908 0.0874 0.1361 -0.1702 150 LEU A CB 1194 C CG . LEU A 150 ? 1.2604 1.5210 0.5974 0.0862 0.1570 -0.1655 150 LEU A CG 1195 C CD1 . LEU A 150 ? 1.2423 1.5228 0.5945 0.0580 0.1616 -0.1482 150 LEU A CD1 1196 C CD2 . LEU A 150 ? 1.2818 1.5801 0.6084 0.1069 0.1840 -0.1776 150 LEU A CD2 1197 N N . ILE A 151 ? 1.4399 1.5193 0.6070 0.1197 0.1110 -0.2037 151 ILE A N 1198 C CA . ILE A 151 ? 1.4985 1.5197 0.6056 0.1134 0.0921 -0.2083 151 ILE A CA 1199 C C . ILE A 151 ? 1.5443 1.5719 0.6006 0.1103 0.1105 -0.2104 151 ILE A C 1200 O O . ILE A 151 ? 1.5119 1.5896 0.5809 0.1144 0.1391 -0.2089 151 ILE A O 1201 C CB . ILE A 151 ? 1.5393 1.5101 0.6156 0.1339 0.0790 -0.2276 151 ILE A CB 1202 C CG1 . ILE A 151 ? 1.5841 1.5648 0.6309 0.1636 0.1062 -0.2478 151 ILE A CG1 1203 C CG2 . ILE A 151 ? 1.4856 1.4530 0.6126 0.1372 0.0630 -0.2240 151 ILE A CG2 1204 C CD1 . ILE A 151 ? 1.6350 1.5595 0.6454 0.1853 0.0947 -0.2681 151 ILE A CD1 1205 N N . LYS A 152 ? 1.6225 1.6003 0.6215 0.1017 0.0932 -0.2128 152 LYS A N 1206 C CA . LYS A 152 ? 1.6918 1.6674 0.6334 0.0974 0.1073 -0.2142 152 LYS A CA 1207 C C . LYS A 152 ? 1.7504 1.7380 0.6576 0.1250 0.1372 -0.2351 152 LYS A C 1208 O O . LYS A 152 ? 1.7618 1.7319 0.6657 0.1491 0.1379 -0.2530 152 LYS A O 1209 C CB . LYS A 152 ? 1.7452 1.6596 0.6296 0.0836 0.0780 -0.2139 152 LYS A CB 1210 C CG . LYS A 152 ? 1.8087 1.6668 0.6476 0.1008 0.0637 -0.2368 152 LYS A CG 1211 C CD . LYS A 152 ? 1.8615 1.6615 0.6484 0.0824 0.0306 -0.2345 152 LYS A CD 1212 C CE . LYS A 152 ? 1.9318 1.6727 0.6532 0.0988 0.0223 -0.2605 152 LYS A CE 1213 N NZ . LYS A 152 ? 1.9867 1.6712 0.6602 0.0779 -0.0142 -0.2577 152 LYS A NZ 1214 N N . LYS A 153 ? 1.8020 1.8186 0.6829 0.1218 0.1623 -0.2318 153 LYS A N 1215 C CA . LYS A 153 ? 1.8701 1.9018 0.7144 0.1476 0.1938 -0.2499 153 LYS A CA 1216 C C . LYS A 153 ? 1.9385 1.9378 0.7017 0.1416 0.1965 -0.2541 153 LYS A C 1217 O O . LYS A 153 ? 1.9261 1.9393 0.6806 0.1178 0.1979 -0.2361 153 LYS A O 1218 C CB . LYS A 153 ? 1.8444 1.9547 0.7381 0.1515 0.2278 -0.2417 153 LYS A CB 1219 C CG . LYS A 153 ? 1.8866 2.0229 0.7712 0.1862 0.2588 -0.2609 153 LYS A CG 1220 C CD . LYS A 153 ? 1.8568 2.0765 0.7901 0.1867 0.2919 -0.2504 153 LYS A CD 1221 C CE . LYS A 153 ? 1.8958 2.1379 0.7929 0.1707 0.3128 -0.2404 153 LYS A CE 1222 N NZ . LYS A 153 ? 1.8785 2.2019 0.8144 0.1758 0.3492 -0.2340 153 LYS A NZ 1223 N N . ASN A 154 ? 2.0218 1.9760 0.7240 0.1636 0.1975 -0.2779 154 ASN A N 1224 C CA . ASN A 154 ? 2.1122 2.0229 0.7264 0.1595 0.1957 -0.2860 154 ASN A CA 1225 C C . ASN A 154 ? 2.1132 1.9852 0.7074 0.1262 0.1596 -0.2691 154 ASN A C 1226 O O . ASN A 154 ? 2.1412 2.0142 0.6956 0.1092 0.1629 -0.2579 154 ASN A O 1227 C CB . ASN A 154 ? 2.1434 2.1006 0.7319 0.1655 0.2360 -0.2847 154 ASN A CB 1228 C CG . ASN A 154 ? 2.2640 2.1750 0.7540 0.1738 0.2419 -0.3019 154 ASN A CG 1229 O OD1 . ASN A 154 ? 2.3236 2.1652 0.7619 0.1741 0.2145 -0.3157 154 ASN A OD1 1230 N ND2 . ASN A 154 ? 2.3084 2.2581 0.7708 0.1798 0.2780 -0.3011 154 ASN A ND2 1231 N N . SER A 155 ? 2.0793 1.9197 0.7036 0.1178 0.1254 -0.2660 155 SER A N 1232 C CA . SER A 155 ? 2.0784 1.8803 0.6893 0.0892 0.0871 -0.2507 155 SER A CA 1233 C C . SER A 155 ? 2.0300 1.8691 0.6752 0.0622 0.0860 -0.2206 155 SER A C 1234 O O . SER A 155 ? 2.0650 1.8778 0.6764 0.0410 0.0644 -0.2076 155 SER A O 1235 C CB . SER A 155 ? 2.1687 1.9093 0.6853 0.0871 0.0726 -0.2646 155 SER A CB 1236 O OG . SER A 155 ? 2.2159 1.9135 0.6972 0.1114 0.0717 -0.2933 155 SER A OG 1237 N N . THR A 156 ? 1.9555 1.8538 0.6665 0.0630 0.1082 -0.2094 156 THR A N 1238 C CA . THR A 156 ? 1.9108 1.8405 0.6619 0.0380 0.1063 -0.1814 156 THR A CA 1239 C C . THR A 156 ? 1.8376 1.8102 0.6743 0.0389 0.1122 -0.1734 156 THR A C 1240 O O . THR A 156 ? 1.8516 1.8552 0.7151 0.0588 0.1340 -0.1862 156 THR A O 1241 C CB . THR A 156 ? 1.9325 1.8962 0.6570 0.0310 0.1360 -0.1722 156 THR A CB 1242 O OG1 . THR A 156 ? 1.9279 1.9377 0.6686 0.0515 0.1728 -0.1847 156 THR A OG1 1243 C CG2 . THR A 156 ? 2.0193 1.9421 0.6559 0.0269 0.1302 -0.1767 156 THR A CG2 1244 N N . TYR A 157 ? 1.7814 1.7550 0.6596 0.0182 0.0923 -0.1522 157 TYR A N 1245 C CA . TYR A 157 ? 1.6715 1.6857 0.6262 0.0147 0.0988 -0.1418 157 TYR A CA 1246 C C . TYR A 157 ? 1.6354 1.6718 0.6041 -0.0088 0.1049 -0.1175 157 TYR A C 1247 O O . TYR A 157 ? 1.6067 1.6209 0.5827 -0.0258 0.0813 -0.1002 157 TYR A O 1248 C CB . TYR A 157 ? 1.6414 1.6318 0.6349 0.0137 0.0692 -0.1399 157 TYR A CB 1249 C CG . TYR A 157 ? 1.5685 1.5972 0.6357 0.0164 0.0769 -0.1357 157 TYR A CG 1250 C CD1 . TYR A 157 ? 1.5251 1.5813 0.6353 -0.0013 0.0807 -0.1158 157 TYR A CD1 1251 C CD2 . TYR A 157 ? 1.5482 1.5824 0.6393 0.0366 0.0797 -0.1516 157 TYR A CD2 1252 C CE1 . TYR A 157 ? 1.4771 1.5655 0.6495 0.0003 0.0871 -0.1132 157 TYR A CE1 1253 C CE2 . TYR A 157 ? 1.4839 1.5529 0.6389 0.0384 0.0855 -0.1473 157 TYR A CE2 1254 C CZ . TYR A 157 ? 1.4495 1.5459 0.6440 0.0198 0.0893 -0.1287 157 TYR A CZ 1255 O OH . TYR A 157 ? 1.3842 1.5128 0.6374 0.0207 0.0947 -0.1255 157 TYR A OH 1256 N N . PRO A 158 ? 1.6322 1.7115 0.6029 -0.0097 0.1366 -0.1153 158 PRO A N 1257 C CA . PRO A 158 ? 1.6167 1.7141 0.5996 -0.0332 0.1432 -0.0919 158 PRO A CA 1258 C C . PRO A 158 ? 1.5306 1.6508 0.5850 -0.0423 0.1400 -0.0806 158 PRO A C 1259 O O . PRO A 158 ? 1.4878 1.6246 0.5831 -0.0292 0.1414 -0.0919 158 PRO A O 1260 C CB . PRO A 158 ? 1.6441 1.7819 0.6067 -0.0306 0.1791 -0.0952 158 PRO A CB 1261 C CG . PRO A 158 ? 1.6414 1.8005 0.6130 -0.0039 0.1947 -0.1187 158 PRO A CG 1262 C CD . PRO A 158 ? 1.6532 1.7658 0.6139 0.0104 0.1675 -0.1330 158 PRO A CD 1263 N N . THR A 159 ? 1.5207 1.6389 0.5875 -0.0641 0.1354 -0.0583 159 THR A N 1264 C CA . THR A 159 ? 1.4566 1.5894 0.5857 -0.0736 0.1317 -0.0474 159 THR A CA 1265 C C . THR A 159 ? 1.4216 1.6067 0.5902 -0.0700 0.1587 -0.0550 159 THR A C 1266 O O . THR A 159 ? 1.4322 1.6480 0.5843 -0.0720 0.1837 -0.0564 159 THR A O 1267 C CB . THR A 159 ? 1.4559 1.5756 0.5862 -0.0968 0.1259 -0.0221 159 THR A CB 1268 O OG1 . THR A 159 ? 1.4941 1.5708 0.5808 -0.1006 0.1027 -0.0132 159 THR A OG1 1269 C CG2 . THR A 159 ? 1.3986 1.5202 0.5878 -0.1035 0.1167 -0.0128 159 THR A CG2 1270 N N . ILE A 160 ? 1.3813 1.5779 0.6018 -0.0649 0.1528 -0.0593 160 ILE A N 1271 C CA . ILE A 160 ? 1.3453 1.5913 0.6096 -0.0631 0.1733 -0.0649 160 ILE A CA 1272 C C . ILE A 160 ? 1.3291 1.5841 0.6271 -0.0861 0.1757 -0.0478 160 ILE A C 1273 O O . ILE A 160 ? 1.3092 1.5339 0.6214 -0.0932 0.1566 -0.0376 160 ILE A O 1274 C CB . ILE A 160 ? 1.3047 1.5554 0.6029 -0.0439 0.1644 -0.0796 160 ILE A CB 1275 C CG1 . ILE A 160 ? 1.3412 1.5837 0.6057 -0.0197 0.1658 -0.0983 160 ILE A CG1 1276 C CG2 . ILE A 160 ? 1.2576 1.5577 0.6061 -0.0454 0.1805 -0.0819 160 ILE A CG2 1277 C CD1 . ILE A 160 ? 1.3145 1.5423 0.6000 -0.0015 0.1498 -0.1104 160 ILE A CD1 1278 N N . LYS A 161 ? 1.3483 1.6441 0.6583 -0.0978 0.1993 -0.0443 161 LYS A N 1279 C CA . LYS A 161 ? 1.3455 1.6511 0.6892 -0.1199 0.2032 -0.0310 161 LYS A CA 1280 C C . LYS A 161 ? 1.3194 1.6807 0.7010 -0.1203 0.2223 -0.0394 161 LYS A C 1281 O O . LYS A 161 ? 1.3395 1.7378 0.7144 -0.1284 0.2441 -0.0375 161 LYS A O 1282 C CB . LYS A 161 ? 1.4160 1.7104 0.7310 -0.1425 0.2111 -0.0125 161 LYS A CB 1283 C CG . LYS A 161 ? 1.4832 1.7242 0.7621 -0.1453 0.1911 0.0000 161 LYS A CG 1284 C CD . LYS A 161 ? 1.5614 1.7962 0.8081 -0.1665 0.2021 0.0184 161 LYS A CD 1285 C CE . LYS A 161 ? 1.6275 1.8138 0.8307 -0.1677 0.1829 0.0314 161 LYS A CE 1286 N NZ . LYS A 161 ? 1.6268 1.7766 0.8516 -0.1754 0.1626 0.0466 161 LYS A NZ 1287 N N . ARG A 162 ? 1.2858 1.6554 0.7073 -0.1120 0.2141 -0.0476 162 ARG A N 1288 C CA . ARG A 162 ? 1.2615 1.6851 0.7208 -0.1111 0.2287 -0.0556 162 ARG A CA 1289 C C . ARG A 162 ? 1.2353 1.6600 0.7343 -0.1266 0.2227 -0.0508 162 ARG A C 1290 O O . ARG A 162 ? 1.2154 1.6033 0.7233 -0.1242 0.2047 -0.0490 162 ARG A O 1291 C CB . ARG A 162 ? 1.2603 1.7007 0.7269 -0.0819 0.2271 -0.0729 162 ARG A CB 1292 C CG . ARG A 162 ? 1.3257 1.7715 0.7532 -0.0649 0.2380 -0.0807 162 ARG A CG 1293 C CD . ARG A 162 ? 1.3550 1.8576 0.7853 -0.0710 0.2656 -0.0794 162 ARG A CD 1294 N NE . ARG A 162 ? 1.3480 1.8999 0.8061 -0.0502 0.2768 -0.0924 162 ARG A NE 1295 C CZ . ARG A 162 ? 1.3770 1.9342 0.8155 -0.0218 0.2832 -0.1059 162 ARG A CZ 1296 N NH1 . ARG A 162 ? 1.4243 1.9389 0.8118 -0.0116 0.2792 -0.1100 162 ARG A NH1 1297 N NH2 . ARG A 162 ? 1.3698 1.9738 0.8386 -0.0027 0.2933 -0.1154 162 ARG A NH2 1298 N N . SER A 163 ? 1.2149 1.6835 0.7371 -0.1428 0.2385 -0.0490 163 SER A N 1299 C CA . SER A 163 ? 1.1672 1.6373 0.7210 -0.1620 0.2354 -0.0449 163 SER A CA 1300 C C . SER A 163 ? 1.1467 1.6755 0.7371 -0.1603 0.2445 -0.0543 163 SER A C 1301 O O . SER A 163 ? 1.1382 1.7151 0.7302 -0.1592 0.2610 -0.0563 163 SER A O 1302 C CB . SER A 163 ? 1.1852 1.6437 0.7264 -0.1922 0.2438 -0.0295 163 SER A CB 1303 O OG . SER A 163 ? 1.1855 1.6437 0.7536 -0.2125 0.2425 -0.0269 163 SER A OG 1304 N N . TYR A 164 ? 1.1258 1.6525 0.7452 -0.1593 0.2339 -0.0594 164 TYR A N 1305 C CA . TYR A 164 ? 1.1111 1.6924 0.7657 -0.1625 0.2401 -0.0660 164 TYR A CA 1306 C C . TYR A 164 ? 1.1274 1.7017 0.8000 -0.1898 0.2372 -0.0617 164 TYR A C 1307 O O . TYR A 164 ? 1.1228 1.6501 0.7933 -0.1917 0.2247 -0.0602 164 TYR A O 1308 C CB . TYR A 164 ? 1.0689 1.6624 0.7412 -0.1341 0.2308 -0.0781 164 TYR A CB 1309 C CG . TYR A 164 ? 1.0444 1.6912 0.7535 -0.1386 0.2340 -0.0830 164 TYR A CG 1310 C CD1 . TYR A 164 ? 1.0535 1.7640 0.7772 -0.1397 0.2495 -0.0838 164 TYR A CD1 1311 C CD2 . TYR A 164 ? 1.0371 1.6728 0.7663 -0.1426 0.2218 -0.0859 164 TYR A CD2 1312 C CE1 . TYR A 164 ? 1.0344 1.7974 0.7936 -0.1449 0.2504 -0.0869 164 TYR A CE1 1313 C CE2 . TYR A 164 ? 1.0196 1.7040 0.7797 -0.1483 0.2230 -0.0900 164 TYR A CE2 1314 C CZ . TYR A 164 ? 1.0116 1.7600 0.7875 -0.1499 0.2362 -0.0901 164 TYR A CZ 1315 O OH . TYR A 164 ? 0.9912 1.7903 0.7992 -0.1562 0.2351 -0.0928 164 TYR A OH 1316 N N . ASN A 165 ? 1.1572 1.7791 0.8474 -0.2106 0.2491 -0.0599 165 ASN A N 1317 C CA . ASN A 165 ? 1.1969 1.8151 0.9012 -0.2403 0.2475 -0.0570 165 ASN A CA 1318 C C . ASN A 165 ? 1.1561 1.8189 0.8942 -0.2371 0.2433 -0.0667 165 ASN A C 1319 O O . ASN A 165 ? 1.1637 1.8879 0.9205 -0.2310 0.2514 -0.0695 165 ASN A O 1320 C CB . ASN A 165 ? 1.2653 1.9036 0.9629 -0.2709 0.2625 -0.0462 165 ASN A CB 1321 C CG . ASN A 165 ? 1.3267 1.9608 1.0364 -0.3052 0.2613 -0.0435 165 ASN A CG 1322 O OD1 . ASN A 165 ? 1.2894 1.9566 1.0255 -0.3104 0.2573 -0.0512 165 ASN A OD1 1323 N ND2 . ASN A 165 ? 1.4359 2.0271 1.1239 -0.3293 0.2643 -0.0324 165 ASN A ND2 1324 N N . ASN A 166 ? 1.1255 1.7585 0.8709 -0.2400 0.2310 -0.0712 166 ASN A N 1325 C CA . ASN A 166 ? 1.0882 1.7584 0.8617 -0.2380 0.2249 -0.0799 166 ASN A CA 1326 C C . ASN A 166 ? 1.0910 1.8005 0.8801 -0.2716 0.2308 -0.0781 166 ASN A C 1327 O O . ASN A 166 ? 1.0818 1.7615 0.8669 -0.2954 0.2263 -0.0784 166 ASN A O 1328 C CB . ASN A 166 ? 1.0697 1.6934 0.8420 -0.2299 0.2108 -0.0852 166 ASN A CB 1329 C CG . ASN A 166 ? 1.0477 1.7079 0.8450 -0.2227 0.2034 -0.0939 166 ASN A CG 1330 O OD1 . ASN A 166 ? 1.0388 1.7592 0.8560 -0.2172 0.2069 -0.0960 166 ASN A OD1 1331 N ND2 . ASN A 166 ? 1.0389 1.6636 0.8351 -0.2215 0.1933 -0.0982 166 ASN A ND2 1332 N N . THR A 167 ? 1.0828 1.8592 0.8895 -0.2732 0.2410 -0.0761 167 THR A N 1333 C CA . THR A 167 ? 1.1052 1.9315 0.9324 -0.3054 0.2458 -0.0733 167 THR A CA 1334 C C . THR A 167 ? 1.0941 1.9616 0.9501 -0.3033 0.2351 -0.0814 167 THR A C 1335 O O . THR A 167 ? 1.1306 2.0412 1.0054 -0.3309 0.2354 -0.0800 167 THR A O 1336 C CB . THR A 167 ? 1.1078 1.9957 0.9451 -0.3098 0.2628 -0.0654 167 THR A CB 1337 O OG1 . THR A 167 ? 1.0818 2.0072 0.9302 -0.2724 0.2662 -0.0697 167 THR A OG1 1338 C CG2 . THR A 167 ? 1.1287 1.9783 0.9355 -0.3223 0.2737 -0.0552 167 THR A CG2 1339 N N . ASN A 168 ? 1.0544 1.9087 0.9130 -0.2724 0.2249 -0.0890 168 ASN A N 1340 C CA . ASN A 168 ? 1.0130 1.8995 0.8945 -0.2686 0.2134 -0.0958 168 ASN A CA 1341 C C . ASN A 168 ? 1.0281 1.8725 0.8989 -0.2945 0.2037 -0.1000 168 ASN A C 1342 O O . ASN A 168 ? 1.0695 1.8486 0.9148 -0.3029 0.2042 -0.0990 168 ASN A O 1343 C CB . ASN A 168 ? 0.9761 1.8537 0.8600 -0.2284 0.2055 -0.1012 168 ASN A CB 1344 C CG . ASN A 168 ? 0.9556 1.8579 0.8416 -0.1992 0.2149 -0.0992 168 ASN A CG 1345 O OD1 . ASN A 168 ? 0.9348 1.9024 0.8453 -0.1891 0.2198 -0.0984 168 ASN A OD1 1346 N ND2 . ASN A 168 ? 0.9530 1.8027 0.8125 -0.1846 0.2172 -0.0985 168 ASN A ND2 1347 N N . GLN A 169 ? 1.0164 1.8976 0.9055 -0.3060 0.1948 -0.1045 169 GLN A N 1348 C CA . GLN A 169 ? 1.0309 1.8717 0.9068 -0.3276 0.1850 -0.1111 169 GLN A CA 1349 C C . GLN A 169 ? 1.0023 1.7913 0.8645 -0.3014 0.1764 -0.1174 169 GLN A C 1350 O O . GLN A 169 ? 1.0114 1.7471 0.8540 -0.3138 0.1724 -0.1222 169 GLN A O 1351 C CB . GLN A 169 ? 1.0403 1.9382 0.9373 -0.3499 0.1767 -0.1142 169 GLN A CB 1352 C CG . GLN A 169 ? 1.0676 1.9659 0.9593 -0.3964 0.1786 -0.1127 169 GLN A CG 1353 C CD . GLN A 169 ? 1.0894 2.0154 0.9893 -0.4198 0.1649 -0.1195 169 GLN A CD 1354 O OE1 . GLN A 169 ? 1.0851 1.9580 0.9611 -0.4327 0.1575 -0.1284 169 GLN A OE1 1355 N NE2 . GLN A 169 ? 1.0767 2.0866 1.0099 -0.4241 0.1614 -0.1154 169 GLN A NE2 1356 N N . GLU A 170 ? 0.9573 1.7607 0.8291 -0.2654 0.1743 -0.1171 170 GLU A N 1357 C CA . GLU A 170 ? 0.9187 1.6855 0.7834 -0.2407 0.1652 -0.1216 170 GLU A CA 1358 C C . GLU A 170 ? 0.9140 1.6241 0.7608 -0.2199 0.1681 -0.1186 170 GLU A C 1359 O O . GLU A 170 ? 0.9252 1.6434 0.7714 -0.2078 0.1750 -0.1139 170 GLU A O 1360 C CB . GLU A 170 ? 0.8934 1.7111 0.7808 -0.2146 0.1584 -0.1223 170 GLU A CB 1361 C CG . GLU A 170 ? 0.9078 1.7938 0.8183 -0.2306 0.1540 -0.1230 170 GLU A CG 1362 C CD . GLU A 170 ? 0.9090 1.8589 0.8418 -0.2304 0.1631 -0.1170 170 GLU A CD 1363 O OE1 . GLU A 170 ? 0.9434 1.8796 0.8673 -0.2320 0.1751 -0.1130 170 GLU A OE1 1364 O OE2 . GLU A 170 ? 0.8959 1.9118 0.8554 -0.2279 0.1586 -0.1154 170 GLU A OE2 1365 N N . ASP A 171 ? 0.9118 1.5666 0.7437 -0.2162 0.1630 -0.1211 171 ASP A N 1366 C CA . ASP A 171 ? 0.8871 1.4917 0.7065 -0.1942 0.1622 -0.1176 171 ASP A CA 1367 C C . ASP A 171 ? 0.8501 1.4792 0.6789 -0.1651 0.1609 -0.1153 171 ASP A C 1368 O O . ASP A 171 ? 0.8204 1.4949 0.6666 -0.1532 0.1572 -0.1178 171 ASP A O 1369 C CB . ASP A 171 ? 0.9045 1.4718 0.7190 -0.1846 0.1547 -0.1208 171 ASP A CB 1370 C CG . ASP A 171 ? 0.9425 1.4629 0.7401 -0.2061 0.1576 -0.1230 171 ASP A CG 1371 O OD1 . ASP A 171 ? 0.9735 1.4762 0.7601 -0.2265 0.1645 -0.1205 171 ASP A OD1 1372 O OD2 . ASP A 171 ? 0.9571 1.4558 0.7509 -0.2015 0.1535 -0.1271 171 ASP A OD2 1373 N N . LEU A 172 ? 0.8559 1.4524 0.6716 -0.1529 0.1631 -0.1106 172 LEU A N 1374 C CA . LEU A 172 ? 0.8558 1.4674 0.6740 -0.1265 0.1623 -0.1099 172 LEU A CA 1375 C C . LEU A 172 ? 0.8526 1.4154 0.6597 -0.1058 0.1543 -0.1075 172 LEU A C 1376 O O . LEU A 172 ? 0.8613 1.3798 0.6532 -0.1119 0.1543 -0.1027 172 LEU A O 1377 C CB . LEU A 172 ? 0.8828 1.5119 0.6932 -0.1327 0.1735 -0.1066 172 LEU A CB 1378 C CG . LEU A 172 ? 0.9072 1.5657 0.7210 -0.1067 0.1760 -0.1084 172 LEU A CG 1379 C CD1 . LEU A 172 ? 0.9068 1.6324 0.7459 -0.1046 0.1793 -0.1114 172 LEU A CD1 1380 C CD2 . LEU A 172 ? 0.9491 1.6002 0.7433 -0.1082 0.1862 -0.1046 172 LEU A CD2 1381 N N . LEU A 173 ? 0.8283 1.4004 0.6442 -0.0818 0.1468 -0.1097 173 LEU A N 1382 C CA . LEU A 173 ? 0.8306 1.3616 0.6379 -0.0627 0.1379 -0.1070 173 LEU A CA 1383 C C . LEU A 173 ? 0.8418 1.3682 0.6348 -0.0496 0.1401 -0.1067 173 LEU A C 1384 O O . LEU A 173 ? 0.8604 1.4185 0.6582 -0.0344 0.1425 -0.1109 173 LEU A O 1385 C CB . LEU A 173 ? 0.8260 1.3653 0.6467 -0.0440 0.1285 -0.1088 173 LEU A CB 1386 C CG . LEU A 173 ? 0.8257 1.3272 0.6399 -0.0243 0.1182 -0.1055 173 LEU A CG 1387 C CD1 . LEU A 173 ? 0.8262 1.2815 0.6328 -0.0335 0.1149 -0.0993 173 LEU A CD1 1388 C CD2 . LEU A 173 ? 0.8159 1.3290 0.6437 -0.0079 0.1099 -0.1061 173 LEU A CD2 1389 N N . VAL A 174 ? 0.8494 1.3356 0.6238 -0.0544 0.1392 -0.1017 174 VAL A N 1390 C CA . VAL A 174 ? 0.8451 1.3205 0.5994 -0.0441 0.1404 -0.1015 174 VAL A CA 1391 C C . VAL A 174 ? 0.8353 1.2685 0.5804 -0.0281 0.1264 -0.0992 174 VAL A C 1392 O O . VAL A 174 ? 0.8251 1.2254 0.5717 -0.0340 0.1189 -0.0928 174 VAL A O 1393 C CB . VAL A 174 ? 0.8687 1.3307 0.6048 -0.0631 0.1486 -0.0959 174 VAL A CB 1394 C CG1 . VAL A 174 ? 0.9003 1.3532 0.6112 -0.0524 0.1505 -0.0963 174 VAL A CG1 1395 C CG2 . VAL A 174 ? 0.8678 1.3688 0.6137 -0.0834 0.1617 -0.0966 174 VAL A CG2 1396 N N . LEU A 175 ? 0.8285 1.2634 0.5644 -0.0081 0.1233 -0.1043 175 LEU A N 1397 C CA . LEU A 175 ? 0.8322 1.2274 0.5566 0.0060 0.1090 -0.1031 175 LEU A CA 1398 C C . LEU A 175 ? 0.8670 1.2412 0.5598 0.0098 0.1091 -0.1044 175 LEU A C 1399 O O . LEU A 175 ? 0.8709 1.2694 0.5522 0.0137 0.1211 -0.1102 175 LEU A O 1400 C CB . LEU A 175 ? 0.8258 1.2319 0.5607 0.0273 0.1033 -0.1089 175 LEU A CB 1401 C CG . LEU A 175 ? 0.8113 1.2348 0.5738 0.0272 0.1002 -0.1071 175 LEU A CG 1402 C CD1 . LEU A 175 ? 0.8159 1.2639 0.5872 0.0483 0.0994 -0.1131 175 LEU A CD1 1403 C CD2 . LEU A 175 ? 0.7951 1.1818 0.5629 0.0246 0.0873 -0.0994 175 LEU A CD2 1404 N N . TRP A 176 ? 0.8823 1.2135 0.5610 0.0088 0.0958 -0.0987 176 TRP A N 1405 C CA . TRP A 176 ? 0.9250 1.2304 0.5695 0.0136 0.0917 -0.1005 176 TRP A CA 1406 C C . TRP A 176 ? 0.9314 1.1938 0.5692 0.0188 0.0711 -0.0962 176 TRP A C 1407 O O . TRP A 176 ? 0.9109 1.1669 0.5726 0.0187 0.0621 -0.0910 176 TRP A O 1408 C CB . TRP A 176 ? 0.9561 1.2578 0.5830 -0.0039 0.0996 -0.0939 176 TRP A CB 1409 C CG . TRP A 176 ? 0.9508 1.2273 0.5859 -0.0194 0.0914 -0.0808 176 TRP A CG 1410 C CD1 . TRP A 176 ? 0.9686 1.2072 0.5876 -0.0228 0.0773 -0.0719 176 TRP A CD1 1411 C CD2 . TRP A 176 ? 0.9127 1.2000 0.5735 -0.0326 0.0971 -0.0750 176 TRP A CD2 1412 N NE1 . TRP A 176 ? 0.9482 1.1754 0.5843 -0.0353 0.0747 -0.0600 176 TRP A NE1 1413 C CE2 . TRP A 176 ? 0.9223 1.1762 0.5821 -0.0412 0.0874 -0.0626 176 TRP A CE2 1414 C CE3 . TRP A 176 ? 0.8891 1.2103 0.5723 -0.0381 0.1088 -0.0792 176 TRP A CE3 1415 C CZ2 . TRP A 176 ? 0.9064 1.1569 0.5857 -0.0528 0.0910 -0.0554 176 TRP A CZ2 1416 C CZ3 . TRP A 176 ? 0.8741 1.1901 0.5736 -0.0522 0.1111 -0.0729 176 TRP A CZ3 1417 C CH2 . TRP A 176 ? 0.8794 1.1588 0.5763 -0.0584 0.1032 -0.0616 176 TRP A CH2 1418 N N . GLY A 177 ? 0.9875 1.2212 0.5919 0.0222 0.0635 -0.0981 177 GLY A N 1419 C CA . GLY A 177 ? 0.9984 1.1917 0.5951 0.0245 0.0418 -0.0938 177 GLY A CA 1420 C C . GLY A 177 ? 1.0269 1.1879 0.5863 0.0187 0.0321 -0.0911 177 GLY A C 1421 O O . GLY A 177 ? 1.0312 1.1985 0.5639 0.0160 0.0433 -0.0946 177 GLY A O 1422 N N . ILE A 178 ? 1.0391 1.1670 0.5972 0.0159 0.0106 -0.0839 178 ILE A N 1423 C CA . ILE A 178 ? 1.0903 1.1843 0.6125 0.0102 -0.0043 -0.0808 178 ILE A CA 1424 C C . ILE A 178 ? 1.1134 1.1756 0.6211 0.0193 -0.0233 -0.0876 178 ILE A C 1425 O O . ILE A 178 ? 1.0814 1.1423 0.6176 0.0231 -0.0316 -0.0850 178 ILE A O 1426 C CB . ILE A 178 ? 1.1021 1.1854 0.6371 -0.0060 -0.0155 -0.0618 178 ILE A CB 1427 C CG1 . ILE A 178 ? 1.1655 1.2167 0.6603 -0.0126 -0.0318 -0.0579 178 ILE A CG1 1428 C CG2 . ILE A 178 ? 1.0729 1.1528 0.6476 -0.0072 -0.0288 -0.0515 178 ILE A CG2 1429 C CD1 . ILE A 178 ? 1.1825 1.2281 0.6832 -0.0273 -0.0385 -0.0388 178 ILE A CD1 1430 N N . HIS A 179 ? 1.1578 1.1927 0.6191 0.0221 -0.0300 -0.0963 179 HIS A N 1431 C CA . HIS A 179 ? 1.1983 1.1958 0.6384 0.0290 -0.0491 -0.1042 179 HIS A CA 1432 C C . HIS A 179 ? 1.2309 1.1953 0.6587 0.0135 -0.0760 -0.0922 179 HIS A C 1433 O O . HIS A 179 ? 1.2792 1.2367 0.6818 0.0032 -0.0789 -0.0864 179 HIS A O 1434 C CB . HIS A 179 ? 1.2401 1.2242 0.6325 0.0440 -0.0396 -0.1242 179 HIS A CB 1435 C CG . HIS A 179 ? 1.2827 1.2191 0.6434 0.0498 -0.0599 -0.1340 179 HIS A CG 1436 N ND1 . HIS A 179 ? 1.3472 1.2466 0.6525 0.0468 -0.0703 -0.1417 179 HIS A ND1 1437 C CD2 . HIS A 179 ? 1.2906 1.2072 0.6647 0.0569 -0.0724 -0.1372 179 HIS A CD2 1438 C CE1 . HIS A 179 ? 1.3875 1.2447 0.6728 0.0516 -0.0888 -0.1505 179 HIS A CE1 1439 N NE2 . HIS A 179 ? 1.3544 1.2209 0.6817 0.0576 -0.0903 -0.1473 179 HIS A NE2 1440 N N . HIS A 180 ? 1.2319 1.1776 0.6784 0.0112 -0.0961 -0.0870 180 HIS A N 1441 C CA . HIS A 180 ? 1.2664 1.1826 0.7051 -0.0039 -0.1246 -0.0753 180 HIS A CA 1442 C C . HIS A 180 ? 1.3378 1.2092 0.7311 0.0002 -0.1411 -0.0902 180 HIS A C 1443 O O . HIS A 180 ? 1.3430 1.2022 0.7438 0.0095 -0.1440 -0.0982 180 HIS A O 1444 C CB . HIS A 180 ? 1.2321 1.1593 0.7243 -0.0111 -0.1362 -0.0579 180 HIS A CB 1445 C CG . HIS A 180 ? 1.1908 1.1566 0.7257 -0.0137 -0.1198 -0.0448 180 HIS A CG 1446 N ND1 . HIS A 180 ? 1.2015 1.1772 0.7329 -0.0225 -0.1156 -0.0345 180 HIS A ND1 1447 C CD2 . HIS A 180 ? 1.1496 1.1434 0.7284 -0.0088 -0.1068 -0.0407 180 HIS A CD2 1448 C CE1 . HIS A 180 ? 1.1482 1.1535 0.7193 -0.0227 -0.1005 -0.0255 180 HIS A CE1 1449 N NE2 . HIS A 180 ? 1.1248 1.1422 0.7243 -0.0147 -0.0949 -0.0295 180 HIS A NE2 1450 N N . PRO A 181 ? 1.3889 1.2330 0.7319 -0.0067 -0.1521 -0.0944 181 PRO A N 1451 C CA . PRO A 181 ? 1.4585 1.2541 0.7520 -0.0037 -0.1682 -0.1106 181 PRO A CA 1452 C C . PRO A 181 ? 1.4669 1.2311 0.7663 -0.0204 -0.2030 -0.1000 181 PRO A C 1453 O O . PRO A 181 ? 1.4105 1.1920 0.7473 -0.0356 -0.2162 -0.0783 181 PRO A O 1454 C CB . PRO A 181 ? 1.5207 1.3018 0.7544 -0.0052 -0.1643 -0.1193 181 PRO A CB 1455 C CG . PRO A 181 ? 1.4838 1.3066 0.7393 -0.0104 -0.1470 -0.1054 181 PRO A CG 1456 C CD . PRO A 181 ? 1.4071 1.2612 0.7306 -0.0162 -0.1478 -0.0865 181 PRO A CD 1457 N N . LYS A 182 ? 1.5202 1.2384 0.7821 -0.0170 -0.2172 -0.1156 182 LYS A N 1458 C CA . LYS A 182 ? 1.5511 1.2334 0.8115 -0.0343 -0.2517 -0.1084 182 LYS A CA 1459 C C . LYS A 182 ? 1.5786 1.2501 0.8188 -0.0568 -0.2771 -0.0953 182 LYS A C 1460 O O . LYS A 182 ? 1.5546 1.2338 0.8315 -0.0746 -0.2998 -0.0745 182 LYS A O 1461 C CB . LYS A 182 ? 1.6251 1.2529 0.8368 -0.0248 -0.2589 -0.1318 182 LYS A CB 1462 C CG . LYS A 182 ? 1.6907 1.2702 0.8846 -0.0449 -0.2963 -0.1288 182 LYS A CG 1463 C CD . LYS A 182 ? 1.7791 1.2965 0.9073 -0.0344 -0.3009 -0.1560 182 LYS A CD 1464 C CE . LYS A 182 ? 1.8591 1.3219 0.9556 -0.0582 -0.3404 -0.1555 182 LYS A CE 1465 N NZ . LYS A 182 ? 1.8538 1.3063 0.9927 -0.0673 -0.3572 -0.1445 182 LYS A NZ 1466 N N . ASP A 183 ? 1.6254 1.2811 0.8079 -0.0555 -0.2734 -0.1066 183 ASP A N 1467 C CA . ASP A 183 ? 1.6707 1.3126 0.8243 -0.0761 -0.2986 -0.0954 183 ASP A CA 1468 C C . ASP A 183 ? 1.6880 1.3343 0.7930 -0.0713 -0.2820 -0.1024 183 ASP A C 1469 O O . ASP A 183 ? 1.6701 1.3325 0.7659 -0.0524 -0.2500 -0.1159 183 ASP A O 1470 C CB . ASP A 183 ? 1.7393 1.3248 0.8508 -0.0904 -0.3335 -0.1036 183 ASP A CB 1471 C CG . ASP A 183 ? 1.8015 1.3384 0.8458 -0.0750 -0.3251 -0.1354 183 ASP A CG 1472 O OD1 . ASP A 183 ? 1.8114 1.3564 0.8246 -0.0570 -0.2967 -0.1500 183 ASP A OD1 1473 O OD2 . ASP A 183 ? 1.8396 1.3292 0.8619 -0.0808 -0.3467 -0.1454 183 ASP A OD2 1474 N N . ALA A 184 ? 1.7139 1.3479 0.7889 -0.0891 -0.3045 -0.0916 184 ALA A N 1475 C CA . ALA A 184 ? 1.7453 1.3831 0.7733 -0.0879 -0.2916 -0.0939 184 ALA A CA 1476 C C . ALA A 184 ? 1.8005 1.4087 0.7589 -0.0715 -0.2726 -0.1239 184 ALA A C 1477 O O . ALA A 184 ? 1.7978 1.4248 0.7342 -0.0621 -0.2460 -0.1283 184 ALA A O 1478 C CB . ALA A 184 ? 1.7802 1.4034 0.7830 -0.1108 -0.3247 -0.0771 184 ALA A CB 1479 N N . ALA A 185 ? 1.8436 1.4048 0.7670 -0.0681 -0.2856 -0.1439 185 ALA A N 1480 C CA . ALA A 185 ? 1.8974 1.4247 0.7522 -0.0501 -0.2684 -0.1740 185 ALA A CA 1481 C C . ALA A 185 ? 1.8393 1.3989 0.7210 -0.0229 -0.2281 -0.1856 185 ALA A C 1482 O O . ALA A 185 ? 1.8442 1.4095 0.6876 -0.0072 -0.2009 -0.2001 185 ALA A O 1483 C CB . ALA A 185 ? 1.9647 1.4284 0.7773 -0.0536 -0.2943 -0.1919 185 ALA A CB 1484 N N . GLU A 186 ? 1.7794 1.3626 0.7275 -0.0178 -0.2245 -0.1780 186 GLU A N 1485 C CA . GLU A 186 ? 1.7363 1.3542 0.7165 0.0063 -0.1897 -0.1864 186 GLU A CA 1486 C C . GLU A 186 ? 1.6746 1.3475 0.6768 0.0081 -0.1623 -0.1753 186 GLU A C 1487 O O . GLU A 186 ? 1.6528 1.3477 0.6470 0.0271 -0.1311 -0.1877 186 GLU A O 1488 C CB . GLU A 186 ? 1.6959 1.3276 0.7421 0.0078 -0.1952 -0.1775 186 GLU A CB 1489 C CG . GLU A 186 ? 1.6827 1.3351 0.7509 0.0343 -0.1660 -0.1905 186 GLU A CG 1490 C CD . GLU A 186 ? 1.6478 1.3040 0.7709 0.0351 -0.1751 -0.1826 186 GLU A CD 1491 O OE1 . GLU A 186 ? 1.5994 1.2990 0.7831 0.0276 -0.1717 -0.1630 186 GLU A OE1 1492 O OE2 . GLU A 186 ? 1.6848 1.2983 0.7879 0.0433 -0.1852 -0.1959 186 GLU A OE2 1493 N N . GLN A 187 ? 1.6414 1.3357 0.6717 -0.0118 -0.1746 -0.1513 187 GLN A N 1494 C CA . GLN A 187 ? 1.6122 1.3518 0.6613 -0.0140 -0.1525 -0.1382 187 GLN A CA 1495 C C . GLN A 187 ? 1.6718 1.4062 0.6575 -0.0072 -0.1333 -0.1513 187 GLN A C 1496 O O . GLN A 187 ? 1.6519 1.4199 0.6446 0.0060 -0.1011 -0.1572 187 GLN A O 1497 C CB . GLN A 187 ? 1.5872 1.3367 0.6640 -0.0364 -0.1743 -0.1108 187 GLN A CB 1498 C CG . GLN A 187 ? 1.5561 1.3421 0.6453 -0.0416 -0.1559 -0.0952 187 GLN A CG 1499 C CD . GLN A 187 ? 1.4847 1.3164 0.6288 -0.0314 -0.1267 -0.0930 187 GLN A CD 1500 O OE1 . GLN A 187 ? 1.4275 1.2719 0.6230 -0.0280 -0.1288 -0.0897 187 GLN A OE1 1501 N NE2 . GLN A 187 ? 1.4757 1.3328 0.6080 -0.0281 -0.0996 -0.0940 187 GLN A NE2 1502 N N . THR A 188 ? 1.7498 1.4433 0.6732 -0.0172 -0.1533 -0.1553 188 THR A N 1503 C CA . THR A 188 ? 1.8109 1.4955 0.6669 -0.0117 -0.1364 -0.1675 188 THR A CA 1504 C C . THR A 188 ? 1.8389 1.5129 0.6644 0.0146 -0.1118 -0.1962 188 THR A C 1505 O O . THR A 188 ? 1.8530 1.5487 0.6548 0.0267 -0.0813 -0.2043 188 THR A O 1506 C CB . THR A 188 ? 1.8905 1.5295 0.6810 -0.0287 -0.1660 -0.1665 188 THR A CB 1507 O OG1 . THR A 188 ? 1.9517 1.5396 0.7151 -0.0282 -0.1909 -0.1824 188 THR A OG1 1508 C CG2 . THR A 188 ? 1.8656 1.5185 0.6871 -0.0527 -0.1901 -0.1361 188 THR A CG2 1509 N N . LYS A 189 ? 1.8415 1.4832 0.6694 0.0237 -0.1246 -0.2102 189 LYS A N 1510 C CA . LYS A 189 ? 1.8736 1.5010 0.6759 0.0513 -0.1031 -0.2368 189 LYS A CA 1511 C C . LYS A 189 ? 1.8294 1.5164 0.6791 0.0705 -0.0653 -0.2368 189 LYS A C 1512 O O . LYS A 189 ? 1.8607 1.5542 0.6804 0.0923 -0.0376 -0.2545 189 LYS A O 1513 C CB . LYS A 189 ? 1.8858 1.4695 0.6943 0.0555 -0.1256 -0.2470 189 LYS A CB 1514 C CG . LYS A 189 ? 1.9371 1.4960 0.7152 0.0857 -0.1069 -0.2747 189 LYS A CG 1515 C CD . LYS A 189 ? 1.9434 1.4689 0.7456 0.0896 -0.1263 -0.2793 189 LYS A CD 1516 C CE . LYS A 189 ? 1.9762 1.4885 0.7647 0.1236 -0.1031 -0.3027 189 LYS A CE 1517 N NZ . LYS A 189 ? 1.9515 1.4465 0.7806 0.1287 -0.1167 -0.3015 189 LYS A NZ 1518 N N . LEU A 190 ? 1.7479 1.4787 0.6703 0.0623 -0.0640 -0.2170 190 LEU A N 1519 C CA . LEU A 190 ? 1.7076 1.4959 0.6783 0.0767 -0.0318 -0.2155 190 LEU A CA 1520 C C . LEU A 190 ? 1.6828 1.5165 0.6614 0.0662 -0.0119 -0.2014 190 LEU A C 1521 O O . LEU A 190 ? 1.6781 1.5501 0.6611 0.0796 0.0194 -0.2074 190 LEU A O 1522 C CB . LEU A 190 ? 1.6454 1.4553 0.6891 0.0747 -0.0397 -0.2037 190 LEU A CB 1523 C CG . LEU A 190 ? 1.6674 1.4370 0.7159 0.0817 -0.0606 -0.2123 190 LEU A CG 1524 C CD1 . LEU A 190 ? 1.6000 1.4033 0.7214 0.0831 -0.0592 -0.2006 190 LEU A CD1 1525 C CD2 . LEU A 190 ? 1.7319 1.4706 0.7341 0.1077 -0.0493 -0.2385 190 LEU A CD2 1526 N N . TYR A 191 ? 1.6700 1.5002 0.6527 0.0419 -0.0302 -0.1816 191 TYR A N 1527 C CA . TYR A 191 ? 1.6334 1.5047 0.6347 0.0292 -0.0143 -0.1639 191 TYR A CA 1528 C C . TYR A 191 ? 1.6886 1.5412 0.6341 0.0142 -0.0207 -0.1563 191 TYR A C 1529 O O . TYR A 191 ? 1.6793 1.5616 0.6328 0.0037 -0.0065 -0.1416 191 TYR A O 1530 C CB . TYR A 191 ? 1.5638 1.4572 0.6332 0.0152 -0.0257 -0.1424 191 TYR A CB 1531 C CG . TYR A 191 ? 1.5053 1.4118 0.6272 0.0272 -0.0248 -0.1476 191 TYR A CG 1532 C CD1 . TYR A 191 ? 1.4690 1.4152 0.6177 0.0431 0.0033 -0.1562 191 TYR A CD1 1533 C CD2 . TYR A 191 ? 1.4821 1.3632 0.6267 0.0220 -0.0524 -0.1426 191 TYR A CD2 1534 C CE1 . TYR A 191 ? 1.4194 1.3777 0.6136 0.0541 0.0031 -0.1597 191 TYR A CE1 1535 C CE2 . TYR A 191 ? 1.4372 1.3295 0.6269 0.0325 -0.0512 -0.1460 191 TYR A CE2 1536 C CZ . TYR A 191 ? 1.4038 1.3337 0.6168 0.0489 -0.0237 -0.1546 191 TYR A CZ 1537 O OH . TYR A 191 ? 1.3557 1.2969 0.6111 0.0594 -0.0233 -0.1569 191 TYR A OH 1538 N N . GLN A 192 ? 1.7523 1.5546 0.6401 0.0122 -0.0426 -0.1658 192 GLN A N 1539 C CA . GLN A 192 ? 1.8096 1.5893 0.6372 -0.0024 -0.0525 -0.1592 192 GLN A CA 1540 C C . GLN A 192 ? 1.7763 1.5595 0.6312 -0.0266 -0.0762 -0.1306 192 GLN A C 1541 O O . GLN A 192 ? 1.8110 1.5582 0.6418 -0.0396 -0.1089 -0.1247 192 GLN A O 1542 C CB . GLN A 192 ? 1.8386 1.6444 0.6315 0.0044 -0.0178 -0.1638 192 GLN A CB 1543 C CG . GLN A 192 ? 1.9238 1.6949 0.6324 -0.0019 -0.0240 -0.1683 192 GLN A CG 1544 C CD . GLN A 192 ? 1.9961 1.7229 0.6430 0.0154 -0.0259 -0.1976 192 GLN A CD 1545 O OE1 . GLN A 192 ? 1.9969 1.7342 0.6510 0.0389 -0.0029 -0.2169 192 GLN A OE1 1546 N NE2 . GLN A 192 ? 2.0678 1.7435 0.6524 0.0043 -0.0537 -0.2010 192 GLN A NE2 1547 N N . ASN A 193 ? 1.7095 1.5355 0.6142 -0.0323 -0.0600 -0.1128 193 ASN A N 1548 C CA . ASN A 193 ? 1.6810 1.5125 0.6145 -0.0520 -0.0778 -0.0849 193 ASN A CA 1549 C C . ASN A 193 ? 1.6581 1.4748 0.6337 -0.0574 -0.1089 -0.0770 193 ASN A C 1550 O O . ASN A 193 ? 1.6245 1.4534 0.6455 -0.0476 -0.1044 -0.0842 193 ASN A O 1551 C CB . ASN A 193 ? 1.6217 1.4988 0.6036 -0.0547 -0.0518 -0.0710 193 ASN A CB 1552 C CG . ASN A 193 ? 1.6427 1.5396 0.5881 -0.0522 -0.0205 -0.0757 193 ASN A CG 1553 O OD1 . ASN A 193 ? 1.7265 1.6032 0.6102 -0.0573 -0.0230 -0.0757 193 ASN A OD1 1554 N ND2 . ASN A 193 ? 1.5790 1.5170 0.5617 -0.0453 0.0089 -0.0792 193 ASN A ND2 1555 N N . PRO A 194 ? 1.6897 1.4822 0.6509 -0.0733 -0.1407 -0.0610 194 PRO A N 1556 C CA . PRO A 194 ? 1.6728 1.4520 0.6709 -0.0795 -0.1716 -0.0531 194 PRO A CA 1557 C C . PRO A 194 ? 1.6054 1.4174 0.6814 -0.0830 -0.1700 -0.0320 194 PRO A C 1558 O O . PRO A 194 ? 1.5626 1.3769 0.6831 -0.0807 -0.1810 -0.0315 194 PRO A O 1559 C CB . PRO A 194 ? 1.7289 1.4765 0.6816 -0.0960 -0.2047 -0.0418 194 PRO A CB 1560 C CG . PRO A 194 ? 1.7508 1.5095 0.6735 -0.1016 -0.1902 -0.0299 194 PRO A CG 1561 C CD . PRO A 194 ? 1.7466 1.5255 0.6576 -0.0868 -0.1500 -0.0478 194 PRO A CD 1562 N N . THR A 195 ? 1.5926 1.4274 0.6824 -0.0884 -0.1562 -0.0146 195 THR A N 1563 C CA . THR A 195 ? 1.5264 1.3885 0.6843 -0.0907 -0.1521 0.0046 195 THR A CA 1564 C C . THR A 195 ? 1.4898 1.3832 0.6669 -0.0837 -0.1154 -0.0007 195 THR A C 1565 O O . THR A 195 ? 1.5096 1.4085 0.6562 -0.0875 -0.0990 0.0021 195 THR A O 1566 C CB . THR A 195 ? 1.5385 1.3964 0.6999 -0.1045 -0.1707 0.0330 195 THR A CB 1567 O OG1 . THR A 195 ? 1.5719 1.4008 0.6987 -0.1132 -0.2046 0.0367 195 THR A OG1 1568 C CG2 . THR A 195 ? 1.4876 1.3661 0.7209 -0.1048 -0.1734 0.0519 195 THR A CG2 1569 N N . THR A 196 ? 1.4467 1.3613 0.6738 -0.0749 -0.1033 -0.0075 196 THR A N 1570 C CA . THR A 196 ? 1.4147 1.3604 0.6595 -0.0681 -0.0702 -0.0162 196 THR A CA 1571 C C . THR A 196 ? 1.3500 1.3196 0.6588 -0.0692 -0.0626 -0.0047 196 THR A C 1572 O O . THR A 196 ? 1.3117 1.2748 0.6526 -0.0732 -0.0813 0.0100 196 THR A O 1573 C CB . THR A 196 ? 1.4180 1.3681 0.6518 -0.0526 -0.0578 -0.0420 196 THR A CB 1574 O OG1 . THR A 196 ? 1.3995 1.3389 0.6612 -0.0470 -0.0756 -0.0461 196 THR A OG1 1575 C CG2 . THR A 196 ? 1.4886 1.4158 0.6543 -0.0492 -0.0582 -0.0560 196 THR A CG2 1576 N N . TYR A 197 ? 1.3249 1.3229 0.6507 -0.0660 -0.0349 -0.0114 197 TYR A N 1577 C CA . TYR A 197 ? 1.2618 1.2813 0.6415 -0.0674 -0.0247 -0.0038 197 TYR A CA 1578 C C . TYR A 197 ? 1.2472 1.2987 0.6391 -0.0620 0.0031 -0.0182 197 TYR A C 1579 O O . TYR A 197 ? 1.2514 1.3116 0.6112 -0.0580 0.0170 -0.0306 197 TYR A O 1580 C CB . TYR A 197 ? 1.2647 1.2797 0.6510 -0.0801 -0.0245 0.0181 197 TYR A CB 1581 C CG . TYR A 197 ? 1.2897 1.3115 0.6427 -0.0883 -0.0050 0.0194 197 TYR A CG 1582 C CD1 . TYR A 197 ? 1.3513 1.3555 0.6508 -0.0926 -0.0113 0.0217 197 TYR A CD1 1583 C CD2 . TYR A 197 ? 1.2600 1.3059 0.6337 -0.0931 0.0195 0.0188 197 TYR A CD2 1584 C CE1 . TYR A 197 ? 1.3791 1.3910 0.6478 -0.1008 0.0077 0.0245 197 TYR A CE1 1585 C CE2 . TYR A 197 ? 1.2887 1.3425 0.6340 -0.1028 0.0375 0.0216 197 TYR A CE2 1586 C CZ . TYR A 197 ? 1.3578 1.3953 0.6510 -0.1063 0.0324 0.0250 197 TYR A CZ 1587 O OH . TYR A 197 ? 1.3900 1.4369 0.6541 -0.1166 0.0515 0.0293 197 TYR A OH 1588 N N . ILE A 198 ? 1.2235 1.2937 0.6622 -0.0617 0.0111 -0.0159 198 ILE A N 1589 C CA . ILE A 198 ? 1.2081 1.3116 0.6636 -0.0609 0.0361 -0.0253 198 ILE A CA 1590 C C . ILE A 198 ? 1.1838 1.2929 0.6714 -0.0720 0.0428 -0.0119 198 ILE A C 1591 O O . ILE A 198 ? 1.1722 1.2738 0.6918 -0.0704 0.0325 -0.0049 198 ILE A O 1592 C CB . ILE A 198 ? 1.1878 1.3088 0.6675 -0.0468 0.0387 -0.0408 198 ILE A CB 1593 C CG1 . ILE A 198 ? 1.2221 1.3320 0.6687 -0.0337 0.0324 -0.0553 198 ILE A CG1 1594 C CG2 . ILE A 198 ? 1.1690 1.3282 0.6693 -0.0476 0.0625 -0.0483 198 ILE A CG2 1595 C CD1 . ILE A 198 ? 1.2121 1.3220 0.6814 -0.0200 0.0241 -0.0650 198 ILE A CD1 1596 N N . SER A 199 ? 1.1894 1.3101 0.6673 -0.0835 0.0605 -0.0082 199 SER A N 1597 C CA . SER A 199 ? 1.1688 1.2904 0.6722 -0.0951 0.0685 0.0028 199 SER A CA 1598 C C . SER A 199 ? 1.1312 1.2873 0.6542 -0.0985 0.0896 -0.0086 199 SER A C 1599 O O . SER A 199 ? 1.1249 1.3045 0.6307 -0.1005 0.1039 -0.0168 199 SER A O 1600 C CB . SER A 199 ? 1.2111 1.3132 0.6886 -0.1091 0.0699 0.0193 199 SER A CB 1601 O OG . SER A 199 ? 1.2450 1.3658 0.6981 -0.1179 0.0888 0.0151 199 SER A OG 1602 N N . VAL A 200 ? 1.1078 1.2685 0.6667 -0.0992 0.0912 -0.0087 200 VAL A N 1603 C CA . VAL A 200 ? 1.0797 1.2731 0.6596 -0.1034 0.1078 -0.0192 200 VAL A CA 1604 C C . VAL A 200 ? 1.0788 1.2617 0.6748 -0.1181 0.1146 -0.0107 200 VAL A C 1605 O O . VAL A 200 ? 1.0846 1.2426 0.6957 -0.1154 0.1053 -0.0024 200 VAL A O 1606 C CB . VAL A 200 ? 1.0532 1.2634 0.6592 -0.0886 0.1031 -0.0313 200 VAL A CB 1607 C CG1 . VAL A 200 ? 1.0427 1.2922 0.6653 -0.0924 0.1191 -0.0425 200 VAL A CG1 1608 C CG2 . VAL A 200 ? 1.0647 1.2718 0.6547 -0.0724 0.0921 -0.0383 200 VAL A CG2 1609 N N . GLY A 201 ? 1.0834 1.2852 0.6764 -0.1336 0.1312 -0.0128 201 GLY A N 1610 C CA . GLY A 201 ? 1.0864 1.2741 0.6895 -0.1500 0.1386 -0.0062 201 GLY A CA 1611 C C . GLY A 201 ? 1.0745 1.2956 0.6931 -0.1618 0.1529 -0.0170 201 GLY A C 1612 O O . GLY A 201 ? 1.0924 1.3500 0.7060 -0.1649 0.1623 -0.0242 201 GLY A O 1613 N N . THR A 202 ? 1.0702 1.2796 0.7075 -0.1677 0.1543 -0.0183 202 THR A N 1614 C CA . THR A 202 ? 1.0622 1.2940 0.7101 -0.1852 0.1664 -0.0260 202 THR A CA 1615 C C . THR A 202 ? 1.0999 1.2901 0.7428 -0.2009 0.1696 -0.0170 202 THR A C 1616 O O . THR A 202 ? 1.1321 1.2851 0.7612 -0.1992 0.1647 -0.0035 202 THR A O 1617 C CB . THR A 202 ? 1.0255 1.2822 0.6988 -0.1756 0.1642 -0.0396 202 THR A CB 1618 O OG1 . THR A 202 ? 1.0015 1.2250 0.6857 -0.1684 0.1576 -0.0375 202 THR A OG1 1619 C CG2 . THR A 202 ? 0.9991 1.2848 0.6772 -0.1549 0.1582 -0.0466 202 THR A CG2 1620 N N . SER A 203 ? 1.1112 1.3056 0.7639 -0.2160 0.1769 -0.0243 203 SER A N 1621 C CA . SER A 203 ? 1.1457 1.2943 0.7929 -0.2287 0.1799 -0.0183 203 SER A CA 1622 C C . SER A 203 ? 1.1442 1.2592 0.8023 -0.2088 0.1716 -0.0161 203 SER A C 1623 O O . SER A 203 ? 1.1782 1.2478 0.8293 -0.2100 0.1717 -0.0060 203 SER A O 1624 C CB . SER A 203 ? 1.1504 1.3113 0.8025 -0.2509 0.1888 -0.0289 203 SER A CB 1625 O OG . SER A 203 ? 1.1171 1.3105 0.7888 -0.2414 0.1861 -0.0431 203 SER A OG 1626 N N . THR A 204 ? 1.1127 1.2505 0.7887 -0.1901 0.1650 -0.0244 204 THR A N 1627 C CA . THR A 204 ? 1.1061 1.2199 0.7960 -0.1711 0.1580 -0.0218 204 THR A CA 1628 C C . THR A 204 ? 1.0940 1.2073 0.7871 -0.1512 0.1452 -0.0128 204 THR A C 1629 O O . THR A 204 ? 1.1367 1.2209 0.8357 -0.1398 0.1388 -0.0020 204 THR A O 1630 C CB . THR A 204 ? 1.0694 1.2051 0.7774 -0.1652 0.1591 -0.0361 204 THR A CB 1631 O OG1 . THR A 204 ? 1.0371 1.2163 0.7533 -0.1562 0.1541 -0.0432 204 THR A OG1 1632 C CG2 . THR A 204 ? 1.0758 1.2123 0.7786 -0.1867 0.1696 -0.0463 204 THR A CG2 1633 N N . LEU A 205 ? 1.0645 1.2100 0.7534 -0.1472 0.1413 -0.0170 205 LEU A N 1634 C CA . LEU A 205 ? 1.0472 1.1926 0.7364 -0.1296 0.1278 -0.0115 205 LEU A CA 1635 C C . LEU A 205 ? 1.0693 1.1902 0.7368 -0.1322 0.1221 0.0034 205 LEU A C 1636 O O . LEU A 205 ? 1.0715 1.1936 0.7186 -0.1468 0.1299 0.0060 205 LEU A O 1637 C CB . LEU A 205 ? 1.0440 1.2287 0.7338 -0.1228 0.1265 -0.0234 205 LEU A CB 1638 C CG . LEU A 205 ? 1.0509 1.2362 0.7440 -0.1037 0.1118 -0.0224 205 LEU A CG 1639 C CD1 . LEU A 205 ? 1.0277 1.2021 0.7452 -0.0922 0.1045 -0.0201 205 LEU A CD1 1640 C CD2 . LEU A 205 ? 1.0400 1.2606 0.7304 -0.0970 0.1131 -0.0352 205 LEU A CD2 1641 N N . ASN A 206 ? 1.0470 1.1476 0.7195 -0.1188 0.1082 0.0143 206 ASN A N 1642 C CA . ASN A 206 ? 1.0641 1.1439 0.7158 -0.1191 0.0986 0.0291 206 ASN A CA 1643 C C . ASN A 206 ? 1.0459 1.1269 0.7009 -0.1038 0.0802 0.0324 206 ASN A C 1644 O O . ASN A 206 ? 1.0305 1.0916 0.6971 -0.0959 0.0681 0.0457 206 ASN A O 1645 C CB . ASN A 206 ? 1.0930 1.1358 0.7454 -0.1231 0.0991 0.0455 206 ASN A CB 1646 C CG . ASN A 206 ? 1.1227 1.1449 0.7510 -0.1253 0.0892 0.0626 206 ASN A CG 1647 O OD1 . ASN A 206 ? 1.1248 1.1583 0.7269 -0.1316 0.0891 0.0606 206 ASN A OD1 1648 N ND2 . ASN A 206 ? 1.1491 1.1420 0.7856 -0.1192 0.0810 0.0799 206 ASN A ND2 1649 N N . GLN A 207 ? 1.0369 1.1408 0.6811 -0.0999 0.0780 0.0208 207 GLN A N 1650 C CA . GLN A 207 ? 1.0366 1.1414 0.6828 -0.0866 0.0609 0.0199 207 GLN A CA 1651 C C . GLN A 207 ? 1.0960 1.1897 0.7079 -0.0879 0.0504 0.0250 207 GLN A C 1652 O O . GLN A 207 ? 1.1181 1.2167 0.7028 -0.0966 0.0603 0.0227 207 GLN A O 1653 C CB . GLN A 207 ? 1.0037 1.1369 0.6602 -0.0790 0.0651 0.0023 207 GLN A CB 1654 C CG . GLN A 207 ? 1.0031 1.1355 0.6595 -0.0661 0.0485 -0.0009 207 GLN A CG 1655 C CD . GLN A 207 ? 0.9967 1.1549 0.6642 -0.0576 0.0538 -0.0170 207 GLN A CD 1656 O OE1 . GLN A 207 ? 1.0151 1.1841 0.6635 -0.0527 0.0548 -0.0275 207 GLN A OE1 1657 N NE2 . GLN A 207 ? 0.9754 1.1431 0.6725 -0.0548 0.0577 -0.0186 207 GLN A NE2 1658 N N . ARG A 208 ? 1.1209 1.2002 0.7335 -0.0802 0.0302 0.0327 208 ARG A N 1659 C CA . ARG A 208 ? 1.1701 1.2390 0.7477 -0.0800 0.0172 0.0337 208 ARG A CA 1660 C C . ARG A 208 ? 1.1662 1.2314 0.7528 -0.0697 -0.0025 0.0311 208 ARG A C 1661 O O . ARG A 208 ? 1.1729 1.2271 0.7814 -0.0674 -0.0176 0.0444 208 ARG A O 1662 C CB . ARG A 208 ? 1.2294 1.2742 0.7881 -0.0878 0.0087 0.0531 208 ARG A CB 1663 C CG . ARG A 208 ? 1.2877 1.3228 0.8000 -0.0909 -0.0001 0.0527 208 ARG A CG 1664 C CD . ARG A 208 ? 1.3407 1.3506 0.8380 -0.0965 -0.0161 0.0747 208 ARG A CD 1665 N NE . ARG A 208 ? 1.3988 1.3991 0.8448 -0.1024 -0.0201 0.0747 208 ARG A NE 1666 C CZ . ARG A 208 ? 1.4450 1.4472 0.8619 -0.1117 -0.0032 0.0753 208 ARG A CZ 1667 N NH1 . ARG A 208 ? 1.4409 1.4534 0.8752 -0.1181 0.0179 0.0758 208 ARG A NH1 1668 N NH2 . ARG A 208 ? 1.5012 1.4945 0.8692 -0.1158 -0.0073 0.0755 208 ARG A NH2 1669 N N . LEU A 209 ? 1.1661 1.2404 0.7365 -0.0636 -0.0020 0.0145 209 LEU A N 1670 C CA . LEU A 209 ? 1.1615 1.2286 0.7365 -0.0551 -0.0203 0.0103 209 LEU A CA 1671 C C . LEU A 209 ? 1.2069 1.2508 0.7412 -0.0576 -0.0382 0.0124 209 LEU A C 1672 O O . LEU A 209 ? 1.2272 1.2678 0.7240 -0.0618 -0.0308 0.0090 209 LEU A O 1673 C CB . LEU A 209 ? 1.1512 1.2366 0.7302 -0.0453 -0.0103 -0.0092 209 LEU A CB 1674 C CG . LEU A 209 ? 1.1248 1.2367 0.7368 -0.0437 0.0085 -0.0143 209 LEU A CG 1675 C CD1 . LEU A 209 ? 1.1174 1.2492 0.7265 -0.0336 0.0177 -0.0326 209 LEU A CD1 1676 C CD2 . LEU A 209 ? 1.0926 1.2033 0.7447 -0.0422 0.0017 -0.0040 209 LEU A CD2 1677 N N . VAL A 210 ? 1.2301 1.2585 0.7712 -0.0562 -0.0619 0.0187 210 VAL A N 1678 C CA . VAL A 210 ? 1.2916 1.2958 0.7925 -0.0591 -0.0823 0.0180 210 VAL A CA 1679 C C . VAL A 210 ? 1.2877 1.2832 0.7932 -0.0526 -0.0971 0.0079 210 VAL A C 1680 O O . VAL A 210 ? 1.2510 1.2551 0.7984 -0.0500 -0.1016 0.0132 210 VAL A O 1681 C CB . VAL A 210 ? 1.3246 1.3131 0.8241 -0.0686 -0.1030 0.0406 210 VAL A CB 1682 C CG1 . VAL A 210 ? 1.3398 1.3287 0.8211 -0.0752 -0.0900 0.0499 210 VAL A CG1 1683 C CG2 . VAL A 210 ? 1.3000 1.2960 0.8526 -0.0679 -0.1133 0.0571 210 VAL A CG2 1684 N N . PRO A 211 ? 1.3374 1.3140 0.7983 -0.0499 -0.1037 -0.0069 211 PRO A N 1685 C CA . PRO A 211 ? 1.3535 1.3161 0.8162 -0.0442 -0.1179 -0.0168 211 PRO A CA 1686 C C . PRO A 211 ? 1.3539 1.2991 0.8299 -0.0539 -0.1486 -0.0011 211 PRO A C 1687 O O . PRO A 211 ? 1.3755 1.3057 0.8288 -0.0640 -0.1654 0.0098 211 PRO A O 1688 C CB . PRO A 211 ? 1.4080 1.3499 0.8131 -0.0385 -0.1160 -0.0369 211 PRO A CB 1689 C CG . PRO A 211 ? 1.4164 1.3699 0.7947 -0.0403 -0.0964 -0.0378 211 PRO A CG 1690 C CD . PRO A 211 ? 1.3878 1.3529 0.7934 -0.0515 -0.0978 -0.0154 211 PRO A CD 1691 N N . ARG A 212 ? 1.3370 1.2872 0.8516 -0.0516 -0.1557 0.0017 212 ARG A N 1692 C CA . ARG A 212 ? 1.3720 1.3092 0.9032 -0.0611 -0.1847 0.0157 212 ARG A CA 1693 C C . ARG A 212 ? 1.4172 1.3218 0.9131 -0.0614 -0.2020 0.0005 212 ARG A C 1694 O O . ARG A 212 ? 1.3837 1.2857 0.8824 -0.0513 -0.1932 -0.0139 212 ARG A O 1695 C CB . ARG A 212 ? 1.3389 1.3006 0.9321 -0.0592 -0.1813 0.0286 212 ARG A CB 1696 C CG . ARG A 212 ? 1.3290 1.3121 0.9573 -0.0627 -0.1770 0.0501 212 ARG A CG 1697 C CD . ARG A 212 ? 1.2987 1.3094 0.9646 -0.0539 -0.1501 0.0499 212 ARG A CD 1698 N NE . ARG A 212 ? 1.2680 1.2891 0.9671 -0.0487 -0.1482 0.0476 212 ARG A NE 1699 C CZ . ARG A 212 ? 1.2688 1.3027 0.9746 -0.0392 -0.1278 0.0337 212 ARG A CZ 1700 N NH1 . ARG A 212 ? 1.2564 1.2975 0.9413 -0.0342 -0.1068 0.0202 212 ARG A NH1 1701 N NH2 . ARG A 212 ? 1.2821 1.3238 1.0168 -0.0355 -0.1287 0.0345 212 ARG A NH2 1702 N N . ILE A 213 ? 1.4940 1.3714 0.9539 -0.0728 -0.2268 0.0037 213 ILE A N 1703 C CA . ILE A 213 ? 1.5626 1.4023 0.9875 -0.0765 -0.2482 -0.0090 213 ILE A CA 1704 C C . ILE A 213 ? 1.5685 1.4078 1.0348 -0.0881 -0.2734 0.0075 213 ILE A C 1705 O O . ILE A 213 ? 1.5396 1.3996 1.0428 -0.0978 -0.2843 0.0309 213 ILE A O 1706 C CB . ILE A 213 ? 1.6178 1.4251 0.9785 -0.0854 -0.2651 -0.0147 213 ILE A CB 1707 C CG1 . ILE A 213 ? 1.6478 1.4551 0.9637 -0.0735 -0.2384 -0.0321 213 ILE A CG1 1708 C CG2 . ILE A 213 ? 1.6606 1.4241 0.9862 -0.0921 -0.2909 -0.0267 213 ILE A CG2 1709 C CD1 . ILE A 213 ? 1.6466 1.4786 0.9672 -0.0771 -0.2264 -0.0175 213 ILE A CD1 1710 N N . ALA A 214 ? 1.5880 1.4044 1.0489 -0.0865 -0.2816 -0.0041 214 ALA A N 1711 C CA . ALA A 214 ? 1.5754 1.3859 1.0685 -0.1000 -0.3074 0.0100 214 ALA A CA 1712 C C . ALA A 214 ? 1.5999 1.3710 1.0654 -0.0975 -0.3156 -0.0086 214 ALA A C 1713 O O . ALA A 214 ? 1.5835 1.3462 1.0281 -0.0799 -0.2941 -0.0289 214 ALA A O 1714 C CB . ALA A 214 ? 1.5204 1.3735 1.0845 -0.0971 -0.2955 0.0288 214 ALA A CB 1715 N N . THR A 215 ? 1.6309 1.3776 1.0967 -0.1153 -0.3472 -0.0008 215 THR A N 1716 C CA . THR A 215 ? 1.6447 1.3495 1.0881 -0.1155 -0.3579 -0.0155 215 THR A CA 1717 C C . THR A 215 ? 1.5685 1.2978 1.0660 -0.1066 -0.3426 -0.0086 215 THR A C 1718 O O . THR A 215 ? 1.5365 1.2967 1.0897 -0.1169 -0.3492 0.0148 215 THR A O 1719 C CB . THR A 215 ? 1.6902 1.3618 1.1201 -0.1413 -0.3983 -0.0071 215 THR A CB 1720 O OG1 . THR A 215 ? 1.7273 1.3868 1.1158 -0.1521 -0.4143 -0.0071 215 THR A OG1 1721 C CG2 . THR A 215 ? 1.7461 1.3606 1.1354 -0.1411 -0.4094 -0.0273 215 THR A CG2 1722 N N . ARG A 216 ? 1.5326 1.2503 1.0139 -0.0867 -0.3215 -0.0281 216 ARG A N 1723 C CA . ARG A 216 ? 1.4605 1.2025 0.9879 -0.0761 -0.3048 -0.0228 216 ARG A CA 1724 C C . ARG A 216 ? 1.4863 1.1849 0.9927 -0.0716 -0.3124 -0.0356 216 ARG A C 1725 O O . ARG A 216 ? 1.5135 1.1662 0.9633 -0.0658 -0.3175 -0.0568 216 ARG A O 1726 C CB . ARG A 216 ? 1.4192 1.1968 0.9551 -0.0545 -0.2696 -0.0313 216 ARG A CB 1727 C CG . ARG A 216 ? 1.3762 1.1979 0.9413 -0.0582 -0.2590 -0.0163 216 ARG A CG 1728 C CD . ARG A 216 ? 1.3400 1.1915 0.9072 -0.0394 -0.2256 -0.0268 216 ARG A CD 1729 N NE . ARG A 216 ? 1.3690 1.2040 0.8826 -0.0320 -0.2177 -0.0453 216 ARG A NE 1730 C CZ . ARG A 216 ? 1.3578 1.1994 0.8537 -0.0384 -0.2174 -0.0418 216 ARG A CZ 1731 N NH1 . ARG A 216 ? 1.3251 1.1883 0.8530 -0.0513 -0.2254 -0.0202 216 ARG A NH1 1732 N NH2 . ARG A 216 ? 1.3910 1.2178 0.8363 -0.0309 -0.2082 -0.0591 216 ARG A NH2 1733 N N . SER A 217 ? 1.4547 1.1666 1.0058 -0.0734 -0.3122 -0.0223 217 SER A N 1734 C CA . SER A 217 ? 1.4853 1.1600 1.0235 -0.0667 -0.3157 -0.0316 217 SER A CA 1735 C C . SER A 217 ? 1.4834 1.1530 0.9932 -0.0378 -0.2892 -0.0549 217 SER A C 1736 O O . SER A 217 ? 1.4201 1.1315 0.9433 -0.0242 -0.2641 -0.0572 217 SER A O 1737 C CB . SER A 217 ? 1.4476 1.1487 1.0437 -0.0721 -0.3147 -0.0103 217 SER A CB 1738 O OG . SER A 217 ? 1.4485 1.1648 1.0788 -0.0974 -0.3361 0.0135 217 SER A OG 1739 N N . LYS A 218 ? 1.5484 1.1665 1.0191 -0.0286 -0.2950 -0.0717 218 LYS A N 1740 C CA . LYS A 218 ? 1.5747 1.1884 1.0215 0.0010 -0.2705 -0.0926 218 LYS A CA 1741 C C . LYS A 218 ? 1.5043 1.1557 0.9982 0.0147 -0.2515 -0.0832 218 LYS A C 1742 O O . LYS A 218 ? 1.4952 1.1441 1.0203 0.0047 -0.2623 -0.0673 218 LYS A O 1743 C CB . LYS A 218 ? 1.6801 1.2236 1.0705 0.0091 -0.2823 -0.1131 218 LYS A CB 1744 C CG . LYS A 218 ? 1.7639 1.2702 1.0939 0.0043 -0.2925 -0.1303 218 LYS A CG 1745 C CD . LYS A 218 ? 1.8729 1.3049 1.1442 0.0142 -0.3025 -0.1524 218 LYS A CD 1746 C CE . LYS A 218 ? 1.9562 1.3540 1.1605 0.0161 -0.3052 -0.1739 218 LYS A CE 1747 N NZ . LYS A 218 ? 1.9904 1.3791 1.1843 -0.0162 -0.3334 -0.1635 218 LYS A NZ 1748 N N . VAL A 219 ? 1.4474 1.1353 0.9456 0.0363 -0.2236 -0.0924 219 VAL A N 1749 C CA . VAL A 219 ? 1.3859 1.1088 0.9206 0.0518 -0.2048 -0.0869 219 VAL A CA 1750 C C . VAL A 219 ? 1.3922 1.1145 0.8987 0.0807 -0.1839 -0.1083 219 VAL A C 1751 O O . VAL A 219 ? 1.3780 1.1225 0.8696 0.0874 -0.1688 -0.1185 219 VAL A O 1752 C CB . VAL A 219 ? 1.3302 1.1161 0.9132 0.0446 -0.1908 -0.0709 219 VAL A CB 1753 C CG1 . VAL A 219 ? 1.2790 1.1007 0.8948 0.0600 -0.1718 -0.0666 219 VAL A CG1 1754 C CG2 . VAL A 219 ? 1.3218 1.1114 0.9342 0.0183 -0.2101 -0.0490 219 VAL A CG2 1755 N N . ASN A 220 ? 1.4064 1.1038 0.9062 0.0979 -0.1831 -0.1139 220 ASN A N 1756 C CA . ASN A 220 ? 1.4380 1.1244 0.9061 0.1276 -0.1668 -0.1349 220 ASN A CA 1757 C C . ASN A 220 ? 1.4675 1.1150 0.8786 0.1303 -0.1700 -0.1552 220 ASN A C 1758 O O . ASN A 220 ? 1.4678 1.1329 0.8592 0.1492 -0.1497 -0.1703 220 ASN A O 1759 C CB . ASN A 220 ? 1.4033 1.1560 0.9007 0.1439 -0.1388 -0.1350 220 ASN A CB 1760 C CG . ASN A 220 ? 1.3761 1.1613 0.9204 0.1459 -0.1347 -0.1186 220 ASN A CG 1761 O OD1 . ASN A 220 ? 1.4158 1.1735 0.9599 0.1561 -0.1415 -0.1164 220 ASN A OD1 1762 N ND2 . ASN A 220 ? 1.3201 1.1617 0.9022 0.1363 -0.1234 -0.1069 220 ASN A ND2 1763 N N . GLY A 221 ? 1.4860 1.0816 0.8702 0.1103 -0.1959 -0.1548 221 GLY A N 1764 C CA . GLY A 221 ? 1.5338 1.0825 0.8570 0.1108 -0.2030 -0.1744 221 GLY A CA 1765 C C . GLY A 221 ? 1.5080 1.0859 0.8201 0.1000 -0.1970 -0.1758 221 GLY A C 1766 O O . GLY A 221 ? 1.5519 1.0992 0.8107 0.1049 -0.1967 -0.1936 221 GLY A O 1767 N N . GLN A 222 ? 1.4407 1.0745 0.7997 0.0857 -0.1921 -0.1571 222 GLN A N 1768 C CA . GLN A 222 ? 1.4303 1.0926 0.7815 0.0757 -0.1857 -0.1561 222 GLN A CA 1769 C C . GLN A 222 ? 1.4072 1.0821 0.7871 0.0460 -0.2055 -0.1342 222 GLN A C 1770 O O . GLN A 222 ? 1.3622 1.0629 0.7927 0.0373 -0.2088 -0.1156 222 GLN A O 1771 C CB . GLN A 222 ? 1.3759 1.0999 0.7531 0.0912 -0.1543 -0.1566 222 GLN A CB 1772 C CG . GLN A 222 ? 1.3983 1.1249 0.7605 0.1222 -0.1324 -0.1744 222 GLN A CG 1773 C CD . GLN A 222 ? 1.4856 1.1671 0.7831 0.1361 -0.1306 -0.1976 222 GLN A CD 1774 O OE1 . GLN A 222 ? 1.4874 1.1484 0.7477 0.1231 -0.1391 -0.2021 222 GLN A OE1 1775 N NE2 . GLN A 222 ? 1.5283 1.1942 0.8108 0.1640 -0.1187 -0.2123 222 GLN A NE2 1776 N N . SER A 223 ? 1.4370 1.0945 0.7833 0.0314 -0.2182 -0.1361 223 SER A N 1777 C CA . SER A 223 ? 1.4228 1.0969 0.7941 0.0054 -0.2359 -0.1151 223 SER A CA 1778 C C . SER A 223 ? 1.3660 1.0951 0.7619 0.0062 -0.2151 -0.1067 223 SER A C 1779 O O . SER A 223 ? 1.3375 1.0949 0.7720 -0.0093 -0.2215 -0.0863 223 SER A O 1780 C CB . SER A 223 ? 1.5049 1.1321 0.8257 -0.0116 -0.2625 -0.1201 223 SER A CB 1781 O OG . SER A 223 ? 1.5932 1.1603 0.8766 -0.0100 -0.2791 -0.1340 223 SER A OG 1782 N N . GLY A 224 ? 1.3641 1.1076 0.7374 0.0244 -0.1899 -0.1222 224 GLY A N 1783 C CA . GLY A 224 ? 1.3154 1.1082 0.7086 0.0251 -0.1685 -0.1157 224 GLY A CA 1784 C C . GLY A 224 ? 1.2487 1.0876 0.6983 0.0319 -0.1508 -0.1062 224 GLY A C 1785 O O . GLY A 224 ? 1.2248 1.0596 0.6921 0.0413 -0.1505 -0.1080 224 GLY A O 1786 N N . ARG A 225 ? 1.2092 1.0896 0.6840 0.0269 -0.1364 -0.0962 225 ARG A N 1787 C CA . ARG A 225 ? 1.1668 1.0909 0.6920 0.0308 -0.1196 -0.0873 225 ARG A CA 1788 C C . ARG A 225 ? 1.1519 1.1134 0.6774 0.0374 -0.0929 -0.0928 225 ARG A C 1789 O O . ARG A 225 ? 1.1742 1.1331 0.6703 0.0333 -0.0889 -0.0961 225 ARG A O 1790 C CB . ARG A 225 ? 1.1260 1.0634 0.6929 0.0139 -0.1312 -0.0649 225 ARG A CB 1791 C CG . ARG A 225 ? 1.1412 1.0514 0.7194 0.0046 -0.1567 -0.0553 225 ARG A CG 1792 C CD . ARG A 225 ? 1.1235 1.0374 0.7254 0.0149 -0.1524 -0.0565 225 ARG A CD 1793 N NE . ARG A 225 ? 1.1430 1.0327 0.7586 0.0034 -0.1762 -0.0448 225 ARG A NE 1794 C CZ . ARG A 225 ? 1.1888 1.0336 0.7751 0.0030 -0.1941 -0.0528 225 ARG A CZ 1795 N NH1 . ARG A 225 ? 1.2320 1.0484 0.7709 0.0163 -0.1901 -0.0741 225 ARG A NH1 1796 N NH2 . ARG A 225 ? 1.1922 1.0195 0.7964 -0.0110 -0.2157 -0.0392 225 ARG A NH2 1797 N N . MET A 226 ? 1.1171 1.1133 0.6752 0.0463 -0.0754 -0.0928 226 MET A N 1798 C CA . MET A 226 ? 1.1167 1.1528 0.6832 0.0490 -0.0512 -0.0955 226 MET A CA 1799 C C . MET A 226 ? 1.0673 1.1333 0.6800 0.0401 -0.0459 -0.0810 226 MET A C 1800 O O . MET A 226 ? 1.0641 1.1380 0.7047 0.0444 -0.0475 -0.0773 226 MET A O 1801 C CB . MET A 226 ? 1.1474 1.2012 0.7089 0.0688 -0.0341 -0.1107 226 MET A CB 1802 C CG . MET A 226 ? 1.2261 1.2531 0.7404 0.0820 -0.0338 -0.1274 226 MET A CG 1803 S SD . MET A 226 ? 1.2844 1.3287 0.7661 0.0801 -0.0151 -0.1346 226 MET A SD 1804 C CE . MET A 226 ? 1.3451 1.3562 0.7749 0.1020 -0.0135 -0.1561 226 MET A CE 1805 N N . GLU A 227 ? 1.0558 1.1360 0.6739 0.0282 -0.0393 -0.0729 227 GLU A N 1806 C CA . GLU A 227 ? 1.0160 1.1211 0.6731 0.0206 -0.0319 -0.0607 227 GLU A CA 1807 C C . GLU A 227 ? 0.9850 1.1243 0.6460 0.0221 -0.0083 -0.0676 227 GLU A C 1808 O O . GLU A 227 ? 1.0136 1.1563 0.6520 0.0182 0.0002 -0.0712 227 GLU A O 1809 C CB . GLU A 227 ? 1.0363 1.1291 0.6986 0.0062 -0.0425 -0.0450 227 GLU A CB 1810 C CG . GLU A 227 ? 1.0309 1.1407 0.7341 0.0005 -0.0383 -0.0312 227 GLU A CG 1811 C CD . GLU A 227 ? 1.0547 1.1499 0.7676 -0.0100 -0.0528 -0.0136 227 GLU A CD 1812 O OE1 . GLU A 227 ? 1.0630 1.1383 0.7488 -0.0154 -0.0646 -0.0115 227 GLU A OE1 1813 O OE2 . GLU A 227 ? 1.0360 1.1410 0.7838 -0.0122 -0.0523 -0.0013 227 GLU A OE2 1814 N N . PHE A 228 ? 0.9453 1.1106 0.6339 0.0267 0.0016 -0.0689 228 PHE A N 1815 C CA . PHE A 228 ? 0.9154 1.1158 0.6090 0.0273 0.0220 -0.0760 228 PHE A CA 1816 C C . PHE A 228 ? 0.8763 1.0923 0.5942 0.0146 0.0305 -0.0673 228 PHE A C 1817 O O . PHE A 228 ? 0.8635 1.0753 0.6049 0.0125 0.0248 -0.0585 228 PHE A O 1818 C CB . PHE A 228 ? 0.9145 1.1351 0.6168 0.0423 0.0272 -0.0855 228 PHE A CB 1819 C CG . PHE A 228 ? 0.9539 1.1610 0.6286 0.0573 0.0241 -0.0969 228 PHE A CG 1820 C CD1 . PHE A 228 ? 0.9661 1.1873 0.6184 0.0614 0.0372 -0.1066 228 PHE A CD1 1821 C CD2 . PHE A 228 ? 0.9783 1.1564 0.6479 0.0672 0.0085 -0.0977 228 PHE A CD2 1822 C CE1 . PHE A 228 ? 1.0181 1.2248 0.6424 0.0775 0.0363 -0.1182 228 PHE A CE1 1823 C CE2 . PHE A 228 ? 1.0248 1.1840 0.6652 0.0820 0.0060 -0.1095 228 PHE A CE2 1824 C CZ . PHE A 228 ? 1.0453 1.2186 0.6623 0.0884 0.0205 -0.1204 228 PHE A CZ 1825 N N . PHE A 229 ? 0.8567 1.0894 0.5672 0.0062 0.0448 -0.0697 229 PHE A N 1826 C CA . PHE A 229 ? 0.8351 1.0769 0.5619 -0.0071 0.0541 -0.0631 229 PHE A CA 1827 C C . PHE A 229 ? 0.8292 1.1070 0.5622 -0.0104 0.0711 -0.0717 229 PHE A C 1828 O O . PHE A 229 ? 0.8090 1.1073 0.5321 -0.0032 0.0771 -0.0812 229 PHE A O 1829 C CB . PHE A 229 ? 0.8597 1.0819 0.5701 -0.0189 0.0536 -0.0548 229 PHE A CB 1830 C CG . PHE A 229 ? 0.8718 1.0620 0.5794 -0.0184 0.0357 -0.0436 229 PHE A CG 1831 C CD1 . PHE A 229 ? 0.8994 1.0713 0.5829 -0.0126 0.0228 -0.0461 229 PHE A CD1 1832 C CD2 . PHE A 229 ? 0.8647 1.0436 0.5935 -0.0236 0.0315 -0.0306 229 PHE A CD2 1833 C CE1 . PHE A 229 ? 0.9164 1.0610 0.5980 -0.0147 0.0040 -0.0351 229 PHE A CE1 1834 C CE2 . PHE A 229 ? 0.8790 1.0343 0.6098 -0.0235 0.0141 -0.0184 229 PHE A CE2 1835 C CZ . PHE A 229 ? 0.9036 1.0425 0.6110 -0.0203 -0.0007 -0.0204 229 PHE A CZ 1836 N N . TRP A 230 ? 0.8165 1.1022 0.5658 -0.0214 0.0787 -0.0683 230 TRP A N 1837 C CA . TRP A 230 ? 0.8119 1.1312 0.5676 -0.0287 0.0929 -0.0756 230 TRP A CA 1838 C C . TRP A 230 ? 0.8089 1.1222 0.5673 -0.0468 0.1016 -0.0711 230 TRP A C 1839 O O . TRP A 230 ? 0.8100 1.0942 0.5706 -0.0503 0.0973 -0.0620 230 TRP A O 1840 C CB . TRP A 230 ? 0.7928 1.1345 0.5679 -0.0198 0.0918 -0.0805 230 TRP A CB 1841 C CG . TRP A 230 ? 0.7795 1.1050 0.5709 -0.0199 0.0864 -0.0739 230 TRP A CG 1842 C CD1 . TRP A 230 ? 0.7851 1.0890 0.5827 -0.0099 0.0741 -0.0672 230 TRP A CD1 1843 C CD2 . TRP A 230 ? 0.7667 1.0966 0.5692 -0.0307 0.0940 -0.0733 230 TRP A CD2 1844 N NE1 . TRP A 230 ? 0.7687 1.0669 0.5827 -0.0128 0.0750 -0.0616 230 TRP A NE1 1845 C CE2 . TRP A 230 ? 0.7695 1.0815 0.5849 -0.0246 0.0874 -0.0661 230 TRP A CE2 1846 C CE3 . TRP A 230 ? 0.7780 1.1240 0.5794 -0.0458 0.1056 -0.0784 230 TRP A CE3 1847 C CZ2 . TRP A 230 ? 0.7694 1.0785 0.5946 -0.0308 0.0938 -0.0647 230 TRP A CZ2 1848 C CZ3 . TRP A 230 ? 0.7873 1.1267 0.5966 -0.0534 0.1102 -0.0779 230 TRP A CZ3 1849 C CH2 . TRP A 230 ? 0.7730 1.0938 0.5931 -0.0448 0.1051 -0.0715 230 TRP A CH2 1850 N N . THR A 231 ? 0.8033 1.1442 0.5620 -0.0582 0.1137 -0.0771 231 THR A N 1851 C CA . THR A 231 ? 0.8155 1.1512 0.5767 -0.0768 0.1223 -0.0753 231 THR A CA 1852 C C . THR A 231 ? 0.8183 1.1938 0.5882 -0.0862 0.1313 -0.0842 231 THR A C 1853 O O . THR A 231 ? 0.8324 1.2425 0.6058 -0.0784 0.1324 -0.0902 231 THR A O 1854 C CB . THR A 231 ? 0.8415 1.1563 0.5842 -0.0902 0.1271 -0.0683 231 THR A CB 1855 O OG1 . THR A 231 ? 0.8438 1.1420 0.5882 -0.1064 0.1338 -0.0655 231 THR A OG1 1856 C CG2 . THR A 231 ? 0.8431 1.1871 0.5737 -0.0963 0.1358 -0.0726 231 THR A CG2 1857 N N . ILE A 232 ? 0.8387 1.2087 0.6117 -0.1024 0.1371 -0.0851 232 ILE A N 1858 C CA . ILE A 232 ? 0.8507 1.2563 0.6292 -0.1175 0.1446 -0.0927 232 ILE A CA 1859 C C . ILE A 232 ? 0.8809 1.2812 0.6462 -0.1389 0.1538 -0.0897 232 ILE A C 1860 O O . ILE A 232 ? 0.9163 1.2785 0.6722 -0.1497 0.1560 -0.0847 232 ILE A O 1861 C CB . ILE A 232 ? 0.8589 1.2601 0.6455 -0.1234 0.1442 -0.0972 232 ILE A CB 1862 C CG1 . ILE A 232 ? 0.8344 1.2691 0.6355 -0.1092 0.1382 -0.1024 232 ILE A CG1 1863 C CG2 . ILE A 232 ? 0.8798 1.2897 0.6616 -0.1497 0.1523 -0.1020 232 ILE A CG2 1864 C CD1 . ILE A 232 ? 0.8284 1.2578 0.6339 -0.0846 0.1295 -0.0985 232 ILE A CD1 1865 N N . LEU A 233 ? 0.9080 1.3465 0.6731 -0.1441 0.1597 -0.0919 233 LEU A N 1866 C CA . LEU A 233 ? 0.9318 1.3710 0.6849 -0.1660 0.1694 -0.0878 233 LEU A CA 1867 C C . LEU A 233 ? 0.9325 1.3959 0.6939 -0.1899 0.1748 -0.0929 233 LEU A C 1868 O O . LEU A 233 ? 0.9076 1.4200 0.6846 -0.1894 0.1751 -0.0989 233 LEU A O 1869 C CB . LEU A 233 ? 0.9436 1.4141 0.6918 -0.1590 0.1746 -0.0866 233 LEU A CB 1870 C CG . LEU A 233 ? 0.9722 1.4453 0.7055 -0.1794 0.1857 -0.0800 233 LEU A CG 1871 C CD1 . LEU A 233 ? 0.9953 1.4116 0.7072 -0.1843 0.1835 -0.0701 233 LEU A CD1 1872 C CD2 . LEU A 233 ? 0.9754 1.4873 0.7056 -0.1684 0.1925 -0.0809 233 LEU A CD2 1873 N N . LYS A 234 ? 0.9806 1.4088 0.7311 -0.2108 0.1781 -0.0904 234 LYS A N 1874 C CA . LYS A 234 ? 1.0426 1.4841 0.7968 -0.2362 0.1814 -0.0964 234 LYS A CA 1875 C C . LYS A 234 ? 1.0583 1.5399 0.8143 -0.2586 0.1897 -0.0941 234 LYS A C 1876 O O . LYS A 234 ? 1.0550 1.5429 0.8042 -0.2557 0.1953 -0.0868 234 LYS A O 1877 C CB . LYS A 234 ? 1.1266 1.5095 0.8659 -0.2491 0.1822 -0.0956 234 LYS A CB 1878 C CG . LYS A 234 ? 1.1780 1.5450 0.9221 -0.2377 0.1763 -0.1032 234 LYS A CG 1879 C CD . LYS A 234 ? 1.2693 1.5757 0.9977 -0.2456 0.1792 -0.1028 234 LYS A CD 1880 C CE . LYS A 234 ? 1.3184 1.5826 1.0420 -0.2264 0.1779 -0.0919 234 LYS A CE 1881 N NZ . LYS A 234 ? 1.3868 1.5923 1.0962 -0.2329 0.1824 -0.0896 234 LYS A NZ 1882 N N . PRO A 235 ? 1.0613 1.5721 0.8259 -0.2818 0.1906 -0.1000 235 PRO A N 1883 C CA . PRO A 235 ? 1.0546 1.6127 0.8263 -0.3037 0.1984 -0.0965 235 PRO A CA 1884 C C . PRO A 235 ? 1.0934 1.6166 0.8451 -0.3247 0.2070 -0.0867 235 PRO A C 1885 O O . PRO A 235 ? 1.1143 1.5783 0.8481 -0.3346 0.2060 -0.0854 235 PRO A O 1886 C CB . PRO A 235 ? 1.0551 1.6410 0.8378 -0.3275 0.1945 -0.1044 235 PRO A CB 1887 C CG . PRO A 235 ? 1.0659 1.5990 0.8359 -0.3251 0.1876 -0.1115 235 PRO A CG 1888 C CD . PRO A 235 ? 1.0462 1.5466 0.8122 -0.2911 0.1846 -0.1093 235 PRO A CD 1889 N N . ASN A 236 ? 1.0936 1.6527 0.8475 -0.3298 0.2160 -0.0792 236 ASN A N 1890 C CA . ASN A 236 ? 1.1363 1.6676 0.8702 -0.3491 0.2250 -0.0676 236 ASN A CA 1891 C C . ASN A 236 ? 1.1458 1.6194 0.8567 -0.3307 0.2236 -0.0601 236 ASN A C 1892 O O . ASN A 236 ? 1.1966 1.6421 0.8883 -0.3454 0.2299 -0.0490 236 ASN A O 1893 C CB . ASN A 236 ? 1.1830 1.6871 0.9084 -0.3867 0.2261 -0.0668 236 ASN A CB 1894 C CG . ASN A 236 ? 1.2158 1.7789 0.9563 -0.4169 0.2327 -0.0648 236 ASN A CG 1895 O OD1 . ASN A 236 ? 1.2359 1.8427 0.9827 -0.4173 0.2423 -0.0568 236 ASN A OD1 1896 N ND2 . ASN A 236 ? 1.2400 1.8054 0.9859 -0.4431 0.2277 -0.0717 236 ASN A ND2 1897 N N . ASP A 237 ? 1.1003 1.5574 0.8134 -0.2999 0.2149 -0.0648 237 ASP A N 1898 C CA . ASP A 237 ? 1.1083 1.5194 0.8028 -0.2818 0.2116 -0.0569 237 ASP A CA 1899 C C . ASP A 237 ? 1.0909 1.5351 0.7838 -0.2613 0.2141 -0.0555 237 ASP A C 1900 O O . ASP A 237 ? 1.0688 1.5668 0.7788 -0.2529 0.2165 -0.0626 237 ASP A O 1901 C CB . ASP A 237 ? 1.1026 1.4738 0.7999 -0.2619 0.2005 -0.0611 237 ASP A CB 1902 C CG . ASP A 237 ? 1.1229 1.4366 0.8015 -0.2528 0.1965 -0.0501 237 ASP A CG 1903 O OD1 . ASP A 237 ? 1.1572 1.4489 0.8175 -0.2682 0.2020 -0.0391 237 ASP A OD1 1904 O OD2 . ASP A 237 ? 1.0914 1.3830 0.7745 -0.2308 0.1872 -0.0510 237 ASP A OD2 1905 N N . ALA A 238 ? 1.0995 1.5103 0.7702 -0.2532 0.2133 -0.0461 238 ALA A N 1906 C CA . ALA A 238 ? 1.1046 1.5366 0.7656 -0.2341 0.2155 -0.0455 238 ALA A CA 1907 C C . ALA A 238 ? 1.0923 1.4849 0.7433 -0.2087 0.2022 -0.0448 238 ALA A C 1908 O O . ALA A 238 ? 1.1200 1.4633 0.7629 -0.2109 0.1949 -0.0376 238 ALA A O 1909 C CB . ALA A 238 ? 1.1278 1.5608 0.7660 -0.2505 0.2270 -0.0339 238 ALA A CB 1910 N N . ILE A 239 ? 1.0560 1.4701 0.7085 -0.1847 0.1990 -0.0519 239 ILE A N 1911 C CA . ILE A 239 ? 1.0414 1.4205 0.6815 -0.1627 0.1858 -0.0507 239 ILE A CA 1912 C C . ILE A 239 ? 1.0846 1.4574 0.6934 -0.1589 0.1892 -0.0451 239 ILE A C 1913 O O . ILE A 239 ? 1.0798 1.4906 0.6827 -0.1587 0.2016 -0.0486 239 ILE A O 1914 C CB . ILE A 239 ? 1.0043 1.3997 0.6624 -0.1387 0.1773 -0.0621 239 ILE A CB 1915 C CG1 . ILE A 239 ? 1.0109 1.3635 0.6602 -0.1216 0.1611 -0.0590 239 ILE A CG1 1916 C CG2 . ILE A 239 ? 0.9922 1.4333 0.6503 -0.1258 0.1855 -0.0706 239 ILE A CG2 1917 C CD1 . ILE A 239 ? 0.9841 1.3418 0.6540 -0.1028 0.1510 -0.0672 239 ILE A CD1 1918 N N . ASN A 240 ? 1.1056 1.4320 0.6944 -0.1558 0.1785 -0.0357 240 ASN A N 1919 C CA . ASN A 240 ? 1.1441 1.4569 0.6976 -0.1548 0.1796 -0.0287 240 ASN A CA 1920 C C . ASN A 240 ? 1.1338 1.4200 0.6731 -0.1333 0.1629 -0.0307 240 ASN A C 1921 O O . ASN A 240 ? 1.1199 1.3715 0.6656 -0.1297 0.1478 -0.0247 240 ASN A O 1922 C CB . ASN A 240 ? 1.1913 1.4702 0.7286 -0.1750 0.1805 -0.0121 240 ASN A CB 1923 C CG . ASN A 240 ? 1.2255 1.5269 0.7688 -0.2001 0.1975 -0.0085 240 ASN A CG 1924 O OD1 . ASN A 240 ? 1.2210 1.5632 0.7599 -0.2052 0.2119 -0.0120 240 ASN A OD1 1925 N ND2 . ASN A 240 ? 1.2616 1.5361 0.8148 -0.2160 0.1961 -0.0013 240 ASN A ND2 1926 N N . PHE A 241 ? 1.1337 1.4360 0.6535 -0.1195 0.1660 -0.0391 241 PHE A N 1927 C CA . PHE A 241 ? 1.1381 1.4130 0.6379 -0.1013 0.1500 -0.0423 241 PHE A CA 1928 C C . PHE A 241 ? 1.1824 1.4358 0.6372 -0.1056 0.1496 -0.0344 241 PHE A C 1929 O O . PHE A 241 ? 1.2041 1.4797 0.6396 -0.1126 0.1667 -0.0341 241 PHE A O 1930 C CB . PHE A 241 ? 1.1240 1.4245 0.6292 -0.0802 0.1523 -0.0592 241 PHE A CB 1931 C CG . PHE A 241 ? 1.0929 1.4117 0.6387 -0.0738 0.1497 -0.0660 241 PHE A CG 1932 C CD1 . PHE A 241 ? 1.0784 1.3705 0.6383 -0.0645 0.1314 -0.0658 241 PHE A CD1 1933 C CD2 . PHE A 241 ? 1.0814 1.4462 0.6515 -0.0780 0.1650 -0.0716 241 PHE A CD2 1934 C CE1 . PHE A 241 ? 1.0587 1.3673 0.6530 -0.0589 0.1296 -0.0712 241 PHE A CE1 1935 C CE2 . PHE A 241 ? 1.0508 1.4324 0.6552 -0.0725 0.1615 -0.0774 241 PHE A CE2 1936 C CZ . PHE A 241 ? 1.0396 1.3919 0.6547 -0.0626 0.1443 -0.0773 241 PHE A CZ 1937 N N . GLU A 242 ? 1.1906 1.4028 0.6294 -0.1021 0.1298 -0.0268 242 GLU A N 1938 C CA . GLU A 242 ? 1.2410 1.4299 0.6328 -0.1023 0.1243 -0.0216 242 GLU A CA 1939 C C . GLU A 242 ? 1.2397 1.4006 0.6208 -0.0864 0.1016 -0.0273 242 GLU A C 1940 O O . GLU A 242 ? 1.2057 1.3488 0.6126 -0.0844 0.0848 -0.0222 242 GLU A O 1941 C CB . GLU A 242 ? 1.2728 1.4360 0.6510 -0.1208 0.1209 -0.0007 242 GLU A CB 1942 C CG . GLU A 242 ? 1.3345 1.4722 0.6613 -0.1222 0.1130 0.0069 242 GLU A CG 1943 C CD . GLU A 242 ? 1.3642 1.4787 0.6770 -0.1404 0.1112 0.0295 242 GLU A CD 1944 O OE1 . GLU A 242 ? 1.3685 1.4985 0.6860 -0.1555 0.1297 0.0359 242 GLU A OE1 1945 O OE2 . GLU A 242 ? 1.3840 1.4644 0.6809 -0.1400 0.0904 0.0417 242 GLU A OE2 1946 N N . SER A 243 ? 1.2594 1.4161 0.6024 -0.0756 0.1015 -0.0380 243 SER A N 1947 C CA . SER A 243 ? 1.2666 1.3931 0.5953 -0.0628 0.0789 -0.0444 243 SER A CA 1948 C C . SER A 243 ? 1.3278 1.4306 0.5978 -0.0594 0.0732 -0.0484 243 SER A C 1949 O O . SER A 243 ? 1.3653 1.4827 0.6038 -0.0599 0.0918 -0.0528 243 SER A O 1950 C CB . SER A 243 ? 1.2309 1.3724 0.5847 -0.0452 0.0797 -0.0615 243 SER A CB 1951 O OG . SER A 243 ? 1.2283 1.3365 0.5694 -0.0357 0.0564 -0.0662 243 SER A OG 1952 N N . ASN A 244 ? 1.3554 1.4224 0.6121 -0.0563 0.0469 -0.0472 244 ASN A N 1953 C CA . ASN A 244 ? 1.4141 1.4493 0.6136 -0.0555 0.0338 -0.0497 244 ASN A CA 1954 C C . ASN A 244 ? 1.4194 1.4382 0.6000 -0.0380 0.0253 -0.0707 244 ASN A C 1955 O O . ASN A 244 ? 1.4506 1.4414 0.5781 -0.0353 0.0164 -0.0780 244 ASN A O 1956 C CB . ASN A 244 ? 1.4289 1.4338 0.6286 -0.0679 0.0062 -0.0300 244 ASN A CB 1957 C CG . ASN A 244 ? 1.5039 1.4814 0.6430 -0.0751 -0.0045 -0.0245 244 ASN A CG 1958 O OD1 . ASN A 244 ? 1.5819 1.5611 0.6753 -0.0706 0.0100 -0.0363 244 ASN A OD1 1959 N ND2 . ASN A 244 ? 1.5275 1.4810 0.6653 -0.0856 -0.0299 -0.0058 244 ASN A ND2 1960 N N . GLY A 245 ? 1.3878 1.4219 0.6097 -0.0266 0.0281 -0.0802 245 GLY A N 1961 C CA . GLY A 245 ? 1.3988 1.4122 0.6124 -0.0109 0.0162 -0.0969 245 GLY A CA 1962 C C . GLY A 245 ? 1.3559 1.3793 0.6272 -0.0074 0.0084 -0.0945 245 GLY A C 1963 O O . GLY A 245 ? 1.3116 1.3506 0.6237 -0.0182 0.0080 -0.0792 245 GLY A O 1964 N N . ASN A 246 ? 1.3627 1.3752 0.6351 0.0081 0.0032 -0.1095 246 ASN A N 1965 C CA . ASN A 246 ? 1.3153 1.3316 0.6362 0.0122 -0.0067 -0.1075 246 ASN A CA 1966 C C . ASN A 246 ? 1.2418 1.3035 0.6116 0.0156 0.0141 -0.1061 246 ASN A C 1967 O O . ASN A 246 ? 1.2000 1.2684 0.6108 0.0170 0.0077 -0.1022 246 ASN A O 1968 C CB . ASN A 246 ? 1.3184 1.3129 0.6579 -0.0028 -0.0333 -0.0897 246 ASN A CB 1969 C CG . ASN A 246 ? 1.3917 1.3417 0.6864 -0.0077 -0.0586 -0.0908 246 ASN A CG 1970 O OD1 . ASN A 246 ? 1.4470 1.3706 0.7333 -0.0014 -0.0743 -0.0998 246 ASN A OD1 1971 N ND2 . ASN A 246 ? 1.4071 1.3472 0.6719 -0.0202 -0.0639 -0.0807 246 ASN A ND2 1972 N N . PHE A 247 ? 1.2318 1.3253 0.5955 0.0162 0.0388 -0.1095 247 PHE A N 1973 C CA . PHE A 247 ? 1.1575 1.2958 0.5640 0.0151 0.0578 -0.1071 247 PHE A CA 1974 C C . PHE A 247 ? 1.1305 1.2909 0.5518 0.0353 0.0683 -0.1221 247 PHE A C 1975 O O . PHE A 247 ? 1.1651 1.3251 0.5567 0.0504 0.0775 -0.1358 247 PHE A O 1976 C CB . PHE A 247 ? 1.1691 1.3326 0.5627 0.0039 0.0784 -0.1022 247 PHE A CB 1977 C CG . PHE A 247 ? 1.1322 1.3403 0.5667 -0.0026 0.0967 -0.0985 247 PHE A CG 1978 C CD1 . PHE A 247 ? 1.0889 1.3018 0.5659 -0.0096 0.0899 -0.0904 247 PHE A CD1 1979 C CD2 . PHE A 247 ? 1.1409 1.3864 0.5695 -0.0031 0.1208 -0.1027 247 PHE A CD2 1980 C CE1 . PHE A 247 ? 1.0562 1.3067 0.5657 -0.0172 0.1055 -0.0883 247 PHE A CE1 1981 C CE2 . PHE A 247 ? 1.1012 1.3877 0.5662 -0.0121 0.1357 -0.0990 247 PHE A CE2 1982 C CZ . PHE A 247 ? 1.0667 1.3537 0.5706 -0.0196 0.1273 -0.0925 247 PHE A CZ 1983 N N . ILE A 248 ? 1.1029 1.2812 0.5690 0.0367 0.0668 -0.1192 248 ILE A N 1984 C CA . ILE A 248 ? 1.0815 1.2881 0.5678 0.0546 0.0777 -0.1301 248 ILE A CA 1985 C C . ILE A 248 ? 1.0539 1.3109 0.5694 0.0458 0.0977 -0.1259 248 ILE A C 1986 O O . ILE A 248 ? 1.0291 1.2968 0.5773 0.0332 0.0952 -0.1164 248 ILE A O 1987 C CB . ILE A 248 ? 1.0597 1.2519 0.5733 0.0616 0.0613 -0.1291 248 ILE A CB 1988 C CG1 . ILE A 248 ? 1.0879 1.2273 0.5773 0.0610 0.0372 -0.1280 248 ILE A CG1 1989 C CG2 . ILE A 248 ? 1.0608 1.2748 0.5859 0.0836 0.0703 -0.1409 248 ILE A CG2 1990 C CD1 . ILE A 248 ? 1.1477 1.2586 0.5884 0.0743 0.0357 -0.1421 248 ILE A CD1 1991 N N . ALA A 249 ? 1.0767 1.3644 0.5793 0.0516 0.1179 -0.1329 249 ALA A N 1992 C CA . ALA A 249 ? 1.0734 1.4079 0.5978 0.0380 0.1367 -0.1274 249 ALA A CA 1993 C C . ALA A 249 ? 1.0426 1.4215 0.6082 0.0459 0.1445 -0.1310 249 ALA A C 1994 O O . ALA A 249 ? 1.0420 1.4271 0.6109 0.0682 0.1443 -0.1406 249 ALA A O 1995 C CB . ALA A 249 ? 1.1075 1.4600 0.6015 0.0384 0.1557 -0.1309 249 ALA A CB 1996 N N . PRO A 250 ? 1.0242 1.4323 0.6194 0.0274 0.1507 -0.1230 250 PRO A N 1997 C CA . PRO A 250 ? 0.9982 1.4539 0.6296 0.0327 0.1585 -0.1262 250 PRO A CA 1998 C C . PRO A 250 ? 1.0368 1.5376 0.6657 0.0463 0.1775 -0.1337 250 PRO A C 1999 O O . PRO A 250 ? 1.0570 1.5683 0.6656 0.0388 0.1911 -0.1324 250 PRO A O 2000 C CB . PRO A 250 ? 0.9623 1.4354 0.6157 0.0058 0.1626 -0.1167 250 PRO A CB 2001 C CG . PRO A 250 ? 0.9863 1.4274 0.6136 -0.0118 0.1620 -0.1086 250 PRO A CG 2002 C CD . PRO A 250 ? 1.0183 1.4126 0.6152 0.0016 0.1486 -0.1108 250 PRO A CD 2003 N N . GLU A 251 ? 1.0429 1.5701 0.6923 0.0673 0.1786 -0.1404 251 GLU A N 2004 C CA . GLU A 251 ? 1.0579 1.6392 0.7166 0.0817 0.1974 -0.1459 251 GLU A CA 2005 C C . GLU A 251 ? 1.0251 1.6609 0.7284 0.0711 0.2008 -0.1408 251 GLU A C 2006 O O . GLU A 251 ? 1.0019 1.6844 0.7183 0.0558 0.2156 -0.1367 251 GLU A O 2007 C CB . GLU A 251 ? 1.0949 1.6637 0.7420 0.1165 0.1955 -0.1569 251 GLU A CB 2008 C CG . GLU A 251 ? 1.1557 1.7448 0.7803 0.1351 0.2152 -0.1650 251 GLU A CG 2009 C CD . GLU A 251 ? 1.1584 1.8217 0.8173 0.1463 0.2333 -0.1651 251 GLU A CD 2010 O OE1 . GLU A 251 ? 1.1663 1.8750 0.8571 0.1242 0.2378 -0.1562 251 GLU A OE1 2011 O OE2 . GLU A 251 ? 1.1743 1.8503 0.8280 0.1772 0.2428 -0.1738 251 GLU A OE2 2012 N N . TYR A 252 ? 0.9863 1.6146 0.7109 0.0773 0.1863 -0.1406 252 TYR A N 2013 C CA . TYR A 252 ? 0.9536 1.6271 0.7166 0.0670 0.1857 -0.1362 252 TYR A CA 2014 C C . TYR A 252 ? 0.9299 1.5733 0.6994 0.0444 0.1723 -0.1301 252 TYR A C 2015 O O . TYR A 252 ? 0.9317 1.5220 0.6856 0.0465 0.1594 -0.1293 252 TYR A O 2016 C CB . TYR A 252 ? 0.9457 1.6412 0.7288 0.0947 0.1811 -0.1402 252 TYR A CB 2017 C CG . TYR A 252 ? 0.9752 1.7063 0.7576 0.1208 0.1958 -0.1461 252 TYR A CG 2018 C CD1 . TYR A 252 ? 1.0065 1.6992 0.7586 0.1467 0.1961 -0.1543 252 TYR A CD1 2019 C CD2 . TYR A 252 ? 0.9699 1.7734 0.7816 0.1197 0.2097 -0.1435 252 TYR A CD2 2020 C CE1 . TYR A 252 ? 1.0255 1.7482 0.7747 0.1734 0.2115 -0.1608 252 TYR A CE1 2021 C CE2 . TYR A 252 ? 0.9920 1.8318 0.8056 0.1460 0.2251 -0.1482 252 TYR A CE2 2022 C CZ . TYR A 252 ? 1.0214 1.8195 0.8029 0.1741 0.2269 -0.1573 252 TYR A CZ 2023 O OH . TYR A 252 ? 1.0449 1.8767 0.8263 0.2029 0.2440 -0.1628 252 TYR A OH 2024 N N . ALA A 253 ? 0.9036 1.5818 0.6961 0.0227 0.1757 -0.1258 253 ALA A N 2025 C CA . ALA A 253 ? 0.8723 1.5264 0.6718 0.0028 0.1654 -0.1213 253 ALA A CA 2026 C C . ALA A 253 ? 0.8548 1.5555 0.6849 -0.0038 0.1641 -0.1209 253 ALA A C 2027 O O . ALA A 253 ? 0.8518 1.6085 0.6990 -0.0019 0.1730 -0.1218 253 ALA A O 2028 C CB . ALA A 253 ? 0.8793 1.5129 0.6644 -0.0246 0.1708 -0.1163 253 ALA A CB 2029 N N . TYR A 254 ? 0.8302 1.5095 0.6667 -0.0117 0.1530 -0.1192 254 TYR A N 2030 C CA . TYR A 254 ? 0.8139 1.5308 0.6745 -0.0154 0.1486 -0.1193 254 TYR A CA 2031 C C . TYR A 254 ? 0.8279 1.5574 0.6940 -0.0481 0.1518 -0.1179 254 TYR A C 2032 O O . TYR A 254 ? 0.8291 1.5156 0.6821 -0.0638 0.1495 -0.1165 254 TYR A O 2033 C CB . TYR A 254 ? 0.7988 1.4857 0.6610 -0.0021 0.1347 -0.1184 254 TYR A CB 2034 C CG . TYR A 254 ? 0.8001 1.4757 0.6593 0.0294 0.1292 -0.1196 254 TYR A CG 2035 C CD1 . TYR A 254 ? 0.7973 1.5120 0.6740 0.0489 0.1270 -0.1202 254 TYR A CD1 2036 C CD2 . TYR A 254 ? 0.8169 1.4409 0.6549 0.0393 0.1251 -0.1197 254 TYR A CD2 2037 C CE1 . TYR A 254 ? 0.8117 1.5104 0.6837 0.0783 0.1220 -0.1214 254 TYR A CE1 2038 C CE2 . TYR A 254 ? 0.8374 1.4455 0.6695 0.0664 0.1191 -0.1217 254 TYR A CE2 2039 C CZ . TYR A 254 ? 0.8389 1.4823 0.6873 0.0862 0.1181 -0.1228 254 TYR A CZ 2040 O OH . TYR A 254 ? 0.8739 1.4963 0.7146 0.1138 0.1123 -0.1249 254 TYR A OH 2041 N N . LYS A 255 ? 0.8337 1.6216 0.7191 -0.0583 0.1567 -0.1182 255 LYS A N 2042 C CA . LYS A 255 ? 0.8454 1.6473 0.7370 -0.0900 0.1565 -0.1180 255 LYS A CA 2043 C C . LYS A 255 ? 0.8282 1.6206 0.7246 -0.0889 0.1440 -0.1197 255 LYS A C 2044 O O . LYS A 255 ? 0.8039 1.6169 0.7125 -0.0671 0.1369 -0.1194 255 LYS A O 2045 C CB . LYS A 255 ? 0.8574 1.7299 0.7710 -0.1022 0.1633 -0.1168 255 LYS A CB 2046 C CG . LYS A 255 ? 0.8855 1.7740 0.7949 -0.1126 0.1782 -0.1139 255 LYS A CG 2047 C CD . LYS A 255 ? 0.9007 1.8565 0.8334 -0.1360 0.1838 -0.1111 255 LYS A CD 2048 C CE . LYS A 255 ? 0.8988 1.9225 0.8623 -0.1158 0.1813 -0.1103 255 LYS A CE 2049 N NZ . LYS A 255 ? 0.9123 2.0041 0.9022 -0.1420 0.1831 -0.1065 255 LYS A NZ 2050 N N . ILE A 256 ? 0.8329 1.5929 0.7179 -0.1120 0.1420 -0.1211 256 ILE A N 2051 C CA . ILE A 256 ? 0.8354 1.5862 0.7209 -0.1146 0.1323 -0.1234 256 ILE A CA 2052 C C . ILE A 256 ? 0.8442 1.6407 0.7404 -0.1394 0.1305 -0.1260 256 ILE A C 2053 O O . ILE A 256 ? 0.8471 1.6278 0.7326 -0.1680 0.1336 -0.1289 256 ILE A O 2054 C CB . ILE A 256 ? 0.8525 1.5387 0.7173 -0.1232 0.1321 -0.1242 256 ILE A CB 2055 C CG1 . ILE A 256 ? 0.8590 1.5026 0.7140 -0.1040 0.1333 -0.1201 256 ILE A CG1 2056 C CG2 . ILE A 256 ? 0.8515 1.5278 0.7148 -0.1211 0.1237 -0.1264 256 ILE A CG2 2057 C CD1 . ILE A 256 ? 0.8613 1.4470 0.7026 -0.1048 0.1313 -0.1186 256 ILE A CD1 2058 N N . VAL A 257 ? 0.8450 1.6972 0.7621 -0.1287 0.1247 -0.1247 257 VAL A N 2059 C CA . VAL A 257 ? 0.8739 1.7801 0.8052 -0.1527 0.1217 -0.1257 257 VAL A CA 2060 C C . VAL A 257 ? 0.9046 1.8018 0.8272 -0.1665 0.1107 -0.1298 257 VAL A C 2061 O O . VAL A 257 ? 0.9085 1.8135 0.8258 -0.1983 0.1094 -0.1339 257 VAL A O 2062 C CB . VAL A 257 ? 0.8696 1.8495 0.8309 -0.1371 0.1211 -0.1208 257 VAL A CB 2063 C CG1 . VAL A 257 ? 0.8783 1.8762 0.8461 -0.1361 0.1352 -0.1180 257 VAL A CG1 2064 C CG2 . VAL A 257 ? 0.8566 1.8393 0.8254 -0.0998 0.1138 -0.1179 257 VAL A CG2 2065 N N . LYS A 258 ? 0.9094 1.7878 0.8278 -0.1439 0.1030 -0.1289 258 LYS A N 2066 C CA . LYS A 258 ? 0.9324 1.8006 0.8388 -0.1541 0.0936 -0.1326 258 LYS A CA 2067 C C . LYS A 258 ? 0.9234 1.7247 0.8079 -0.1438 0.0951 -0.1340 258 LYS A C 2068 O O . LYS A 258 ? 0.8954 1.6789 0.7829 -0.1165 0.0946 -0.1290 258 LYS A O 2069 C CB . LYS A 258 ? 0.9409 1.8615 0.8652 -0.1387 0.0814 -0.1279 258 LYS A CB 2070 C CG . LYS A 258 ? 0.9848 1.9067 0.8953 -0.1556 0.0709 -0.1318 258 LYS A CG 2071 C CD . LYS A 258 ? 1.0008 1.9605 0.9234 -0.1350 0.0579 -0.1250 258 LYS A CD 2072 C CE . LYS A 258 ? 1.0147 2.0501 0.9602 -0.1468 0.0485 -0.1220 258 LYS A CE 2073 N NZ . LYS A 258 ? 1.0107 2.0747 0.9592 -0.1346 0.0332 -0.1161 258 LYS A NZ 2074 N N . LYS A 259 ? 0.9520 1.7168 0.8145 -0.1662 0.0970 -0.1408 259 LYS A N 2075 C CA . LYS A 259 ? 0.9633 1.6706 0.8061 -0.1581 0.0991 -0.1421 259 LYS A CA 2076 C C . LYS A 259 ? 0.9724 1.6859 0.8035 -0.1629 0.0910 -0.1456 259 LYS A C 2077 O O . LYS A 259 ? 0.9800 1.7211 0.8067 -0.1857 0.0858 -0.1513 259 LYS A O 2078 C CB . LYS A 259 ? 0.9982 1.6538 0.8218 -0.1767 0.1094 -0.1472 259 LYS A CB 2079 C CG . LYS A 259 ? 1.0228 1.6610 0.8523 -0.1697 0.1173 -0.1422 259 LYS A CG 2080 C CD . LYS A 259 ? 1.0702 1.6615 0.8813 -0.1904 0.1265 -0.1459 259 LYS A CD 2081 C CE . LYS A 259 ? 1.0962 1.6709 0.9110 -0.1833 0.1331 -0.1394 259 LYS A CE 2082 N NZ . LYS A 259 ? 1.1337 1.6709 0.9325 -0.2059 0.1415 -0.1410 259 LYS A NZ 2083 N N . GLY A 260 ? 0.9724 1.6606 0.7973 -0.1429 0.0895 -0.1417 260 GLY A N 2084 C CA . GLY A 260 ? 0.9935 1.6843 0.8034 -0.1459 0.0831 -0.1441 260 GLY A CA 2085 C C . GLY A 260 ? 0.9780 1.6457 0.7856 -0.1209 0.0824 -0.1364 260 GLY A C 2086 O O . GLY A 260 ? 0.9923 1.6274 0.8048 -0.1058 0.0885 -0.1313 260 GLY A O 2087 N N . ASP A 261 ? 0.9875 1.6738 0.7878 -0.1177 0.0741 -0.1344 261 ASP A N 2088 C CA . ASP A 261 ? 0.9825 1.6481 0.7782 -0.0971 0.0736 -0.1261 261 ASP A CA 2089 C C . ASP A 261 ? 0.9104 1.5942 0.7300 -0.0705 0.0669 -0.1135 261 ASP A C 2090 O O . ASP A 261 ? 0.8932 1.6222 0.7268 -0.0645 0.0568 -0.1095 261 ASP A O 2091 C CB . ASP A 261 ? 1.0439 1.7224 0.8192 -0.1040 0.0671 -0.1277 261 ASP A CB 2092 C CG . ASP A 261 ? 1.1310 1.7692 0.8748 -0.1213 0.0771 -0.1388 261 ASP A CG 2093 O OD1 . ASP A 261 ? 1.1776 1.7729 0.9180 -0.1215 0.0898 -0.1419 261 ASP A OD1 2094 O OD2 . ASP A 261 ? 1.1987 1.8471 0.9197 -0.1339 0.0722 -0.1444 261 ASP A OD2 2095 N N . SER A 262 ? 0.8656 1.5132 0.6894 -0.0545 0.0722 -0.1070 262 SER A N 2096 C CA . SER A 262 ? 0.8514 1.5046 0.6933 -0.0297 0.0659 -0.0959 262 SER A CA 2097 C C . SER A 262 ? 0.8493 1.4597 0.6878 -0.0176 0.0698 -0.0877 262 SER A C 2098 O O . SER A 262 ? 0.8600 1.4418 0.6846 -0.0268 0.0783 -0.0904 262 SER A O 2099 C CB . SER A 262 ? 0.8297 1.4910 0.6874 -0.0254 0.0674 -0.0978 262 SER A CB 2100 O OG . SER A 262 ? 0.8147 1.4821 0.6867 -0.0011 0.0608 -0.0891 262 SER A OG 2101 N N . THR A 263 ? 1.0629 1.0881 0.7064 -0.0552 0.0597 -0.1033 263 THR A N 2102 C CA . THR A 263 ? 1.0063 1.0336 0.6793 -0.0104 0.0521 -0.1001 263 THR A CA 2103 C C . THR A 263 ? 0.9357 1.0401 0.6738 0.0003 0.0465 -0.1138 263 THR A C 2104 O O . THR A 263 ? 0.9165 1.0728 0.6908 -0.0148 0.0463 -0.1260 263 THR A O 2105 C CB . THR A 263 ? 0.9787 0.9936 0.6744 0.0057 0.0480 -0.0984 263 THR A CB 2106 O OG1 . THR A 263 ? 0.9722 0.9911 0.6824 0.0433 0.0425 -0.0953 263 THR A OG1 2107 C CG2 . THR A 263 ? 0.9215 0.9964 0.6810 -0.0019 0.0443 -0.1116 263 THR A CG2 2108 N N . ILE A 264 ? 0.9232 1.0376 0.6695 0.0277 0.0429 -0.1128 264 ILE A N 2109 C CA . ILE A 264 ? 0.8639 1.0410 0.6643 0.0355 0.0393 -0.1275 264 ILE A CA 2110 C C . ILE A 264 ? 0.8427 1.0291 0.6786 0.0509 0.0355 -0.1328 264 ILE A C 2111 O O . ILE A 264 ? 0.8392 1.0170 0.6644 0.0697 0.0333 -0.1268 264 ILE A O 2112 C CB . ILE A 264 ? 0.8510 1.0472 0.6376 0.0476 0.0390 -0.1267 264 ILE A CB 2113 C CG1 . ILE A 264 ? 0.9002 1.0747 0.6401 0.0296 0.0443 -0.1195 264 ILE A CG1 2114 C CG2 . ILE A 264 ? 0.7958 1.0526 0.6324 0.0478 0.0373 -0.1449 264 ILE A CG2 2115 C CD1 . ILE A 264 ? 0.9280 1.1060 0.6368 0.0468 0.0447 -0.1134 264 ILE A CD1 2116 N N . MET A 265 ? 0.8233 1.0287 0.6948 0.0444 0.0356 -0.1443 265 MET A N 2117 C CA . MET A 265 ? 0.8126 1.0129 0.7075 0.0529 0.0345 -0.1494 265 MET A CA 2118 C C . MET A 265 ? 0.8145 1.0418 0.7301 0.0536 0.0364 -0.1653 265 MET A C 2119 O O . MET A 265 ? 0.8327 1.0775 0.7563 0.0499 0.0390 -0.1758 265 MET A O 2120 C CB . MET A 265 ? 0.8242 1.0183 0.7295 0.0487 0.0353 -0.1511 265 MET A CB 2121 C CG . MET A 265 ? 0.8301 1.0052 0.7491 0.0576 0.0350 -0.1529 265 MET A CG 2122 S SD . MET A 265 ? 0.8509 1.0317 0.7752 0.0587 0.0355 -0.1525 265 MET A SD 2123 C CE . MET A 265 ? 0.8526 1.0114 0.7501 0.0419 0.0342 -0.1374 265 MET A CE 2124 N N . LYS A 266 ? 0.8332 1.0669 0.7519 0.0560 0.0363 -0.1686 266 LYS A N 2125 C CA . LYS A 266 ? 0.8568 1.1122 0.7841 0.0459 0.0409 -0.1864 266 LYS A CA 2126 C C . LYS A 266 ? 0.8726 1.0914 0.8009 0.0405 0.0463 -0.1956 266 LYS A C 2127 O O . LYS A 266 ? 0.8894 1.0888 0.8168 0.0410 0.0457 -0.1906 266 LYS A O 2128 C CB . LYS A 266 ? 0.8841 1.1810 0.8086 0.0447 0.0397 -0.1885 266 LYS A CB 2129 C CG . LYS A 266 ? 0.9241 1.2487 0.8340 0.0620 0.0347 -0.1761 266 LYS A CG 2130 C CD . LYS A 266 ? 0.9527 1.3018 0.8621 0.0571 0.0361 -0.1822 266 LYS A CD 2131 C CE . LYS A 266 ? 0.9870 1.3949 0.9047 0.0448 0.0392 -0.2001 266 LYS A CE 2132 N NZ . LYS A 266 ? 1.0263 1.4518 0.9473 0.0351 0.0421 -0.2104 266 LYS A NZ 2133 N N . SER A 267 ? 0.9077 1.1119 0.8305 0.0387 0.0525 -0.2085 267 SER A N 2134 C CA . SER A 267 ? 0.9396 1.0915 0.8456 0.0424 0.0596 -0.2159 267 SER A CA 2135 C C . SER A 267 ? 0.9855 1.1160 0.8687 0.0419 0.0691 -0.2336 267 SER A C 2136 O O . SER A 267 ? 0.9882 1.1506 0.8788 0.0469 0.0676 -0.2372 267 SER A O 2137 C CB . SER A 267 ? 0.9443 1.0839 0.8564 0.0639 0.0554 -0.2039 267 SER A CB 2138 O OG . SER A 267 ? 1.0022 1.0925 0.8911 0.0783 0.0624 -0.2096 267 SER A OG 2139 N N . GLU A 268 ? 1.0378 1.1065 0.8846 0.0351 0.0802 -0.2449 268 GLU A N 2140 C CA . GLU A 268 ? 1.0730 1.0945 0.8778 0.0378 0.0925 -0.2623 268 GLU A CA 2141 C C . GLU A 268 ? 1.1035 1.0816 0.8844 0.0802 0.0951 -0.2592 268 GLU A C 2142 O O . GLU A 268 ? 1.1937 1.1266 0.9311 0.0962 0.1053 -0.2720 268 GLU A O 2143 C CB . GLU A 268 ? 1.1365 1.0978 0.8926 0.0028 0.1074 -0.2785 268 GLU A CB 2144 C CG . GLU A 268 ? 1.1179 1.1403 0.8945 -0.0394 0.1057 -0.2841 268 GLU A CG 2145 C CD . GLU A 268 ? 1.1048 1.2035 0.9096 -0.0456 0.1003 -0.2893 268 GLU A CD 2146 O OE1 . GLU A 268 ? 1.1213 1.1998 0.9033 -0.0444 0.1075 -0.3025 268 GLU A OE1 2147 O OE2 . GLU A 268 ? 1.0492 1.2248 0.8931 -0.0480 0.0893 -0.2797 268 GLU A OE2 2148 N N . LEU A 269 ? 1.0739 1.0692 0.8781 0.1012 0.0864 -0.2431 269 LEU A N 2149 C CA . LEU A 269 ? 1.1155 1.0909 0.8990 0.1457 0.0878 -0.2398 269 LEU A CA 2150 C C . LEU A 269 ? 1.0915 1.1377 0.8966 0.1686 0.0819 -0.2413 269 LEU A C 2151 O O . LEU A 269 ? 1.0144 1.1262 0.8590 0.1475 0.0740 -0.2385 269 LEU A O 2152 C CB . LEU A 269 ? 1.0972 1.0806 0.8997 0.1554 0.0806 -0.2238 269 LEU A CB 2153 C CG . LEU A 269 ? 1.1099 1.0353 0.8960 0.1336 0.0849 -0.2203 269 LEU A CG 2154 C CD1 . LEU A 269 ? 1.0909 1.0399 0.9041 0.1438 0.0759 -0.2040 269 LEU A CD1 2155 C CD2 . LEU A 269 ? 1.2107 1.0316 0.9235 0.1432 0.1013 -0.2304 269 LEU A CD2 2156 N N . GLU A 270 ? 1.1907 1.2233 0.9627 0.2143 0.0867 -0.2459 270 GLU A N 2157 C CA . GLU A 270 ? 1.2036 1.3176 0.9921 0.2411 0.0818 -0.2493 270 GLU A CA 2158 C C . GLU A 270 ? 1.1454 1.3277 0.9578 0.2640 0.0733 -0.2382 270 GLU A C 2159 O O . GLU A 270 ? 1.1260 1.2835 0.9416 0.2605 0.0713 -0.2277 270 GLU A O 2160 C CB . GLU A 270 ? 1.3167 1.3848 1.0461 0.2841 0.0933 -0.2642 270 GLU A CB 2161 C CG . GLU A 270 ? 1.3996 1.3857 1.0891 0.2584 0.1054 -0.2785 270 GLU A CG 2162 C CD . GLU A 270 ? 1.3805 1.4323 1.1057 0.2301 0.1013 -0.2865 270 GLU A CD 2163 O OE1 . GLU A 270 ? 1.3391 1.4696 1.1245 0.1998 0.0894 -0.2769 270 GLU A OE1 2164 O OE2 . GLU A 270 ? 1.4244 1.4412 1.1094 0.2391 0.1111 -0.3023 270 GLU A OE2 2165 N N . TYR A 271 ? 1.1081 1.3840 0.9358 0.2841 0.0690 -0.2423 271 TYR A N 2166 C CA . TYR A 271 ? 1.0698 1.4355 0.9195 0.2982 0.0618 -0.2359 271 TYR A CA 2167 C C . TYR A 271 ? 1.1360 1.4692 0.9477 0.3533 0.0657 -0.2333 271 TYR A C 2168 O O . TYR A 271 ? 1.1972 1.4615 0.9538 0.3995 0.0751 -0.2403 271 TYR A O 2169 C CB . TYR A 271 ? 1.0473 1.5303 0.9126 0.3077 0.0587 -0.2452 271 TYR A CB 2170 C CG . TYR A 271 ? 0.9951 1.5956 0.8849 0.3055 0.0521 -0.2423 271 TYR A CG 2171 C CD1 . TYR A 271 ? 0.9272 1.5439 0.8450 0.2533 0.0471 -0.2316 271 TYR A CD1 2172 C CD2 . TYR A 271 ? 1.0014 1.7023 0.8803 0.3549 0.0521 -0.2519 271 TYR A CD2 2173 C CE1 . TYR A 271 ? 0.8956 1.6192 0.8281 0.2411 0.0434 -0.2318 271 TYR A CE1 2174 C CE2 . TYR A 271 ? 0.9635 1.7912 0.8640 0.3460 0.0470 -0.2524 271 TYR A CE2 2175 C CZ . TYR A 271 ? 0.9159 1.7522 0.8426 0.2841 0.0432 -0.2430 271 TYR A CZ 2176 O OH . TYR A 271 ? 0.8896 1.8511 0.8301 0.2663 0.0403 -0.2462 271 TYR A OH 2177 N N . GLY A 272 ? 1.1171 1.4947 0.9501 0.3492 0.0597 -0.2234 272 GLY A N 2178 C CA . GLY A 272 ? 1.1713 1.5174 0.9701 0.3986 0.0626 -0.2181 272 GLY A CA 2179 C C . GLY A 272 ? 1.1967 1.6619 0.9940 0.4487 0.0590 -0.2212 272 GLY A C 2180 O O . GLY A 272 ? 1.2237 1.6693 0.9869 0.4996 0.0615 -0.2164 272 GLY A O 2181 N N . ASN A 273 ? 1.1868 1.7807 1.0166 0.4349 0.0539 -0.2298 273 ASN A N 2182 C CA . ASN A 273 ? 1.2065 1.9508 1.0423 0.4716 0.0498 -0.2356 273 ASN A CA 2183 C C . ASN A 273 ? 1.1626 1.9361 1.0123 0.4628 0.0456 -0.2257 273 ASN A C 2184 O O . ASN A 273 ? 1.1974 1.9658 1.0146 0.5246 0.0473 -0.2222 273 ASN A O 2185 C CB . ASN A 273 ? 1.2953 2.0433 1.0749 0.5655 0.0557 -0.2436 273 ASN A CB 2186 C CG . ASN A 273 ? 1.3573 2.1249 1.1285 0.5749 0.0587 -0.2571 273 ASN A CG 2187 O OD1 . ASN A 273 ? 1.4341 2.0731 1.1679 0.5843 0.0667 -0.2591 273 ASN A OD1 2188 N ND2 . ASN A 273 ? 1.3326 2.2658 1.1361 0.5671 0.0533 -0.2679 273 ASN A ND2 2189 N N . CYS A 274 ? 1.1009 1.8993 0.9918 0.3872 0.0410 -0.2212 274 CYS A N 2190 C CA . CYS A 274 ? 1.0845 1.8431 0.9843 0.3639 0.0388 -0.2091 274 CYS A CA 2191 C C . CYS A 274 ? 0.9788 1.7920 0.9121 0.2835 0.0353 -0.2080 274 CYS A C 2192 O O . CYS A 274 ? 0.9529 1.7807 0.8975 0.2381 0.0358 -0.2125 274 CYS A O 2193 C CB . CYS A 274 ? 1.1434 1.7342 1.0251 0.3618 0.0426 -0.1990 274 CYS A CB 2194 S SG . CYS A 274 ? 1.2338 1.7569 1.1302 0.3207 0.0399 -0.1841 274 CYS A SG 2195 N N . ASN A 275 ? 0.9343 1.7679 0.8747 0.2656 0.0332 -0.2020 275 ASN A N 2196 C CA . ASN A 275 ? 0.8989 1.7613 0.8535 0.1877 0.0327 -0.2011 275 ASN A CA 2197 C C . ASN A 275 ? 0.8983 1.6663 0.8522 0.1654 0.0319 -0.1875 275 ASN A C 2198 O O . ASN A 275 ? 0.9241 1.6680 0.8735 0.2067 0.0306 -0.1815 275 ASN A O 2199 C CB . ASN A 275 ? 0.8722 1.9041 0.8320 0.1706 0.0327 -0.2142 275 ASN A CB 2200 C CG . ASN A 275 ? 0.8455 1.9023 0.8016 0.0793 0.0364 -0.2176 275 ASN A CG 2201 O OD1 . ASN A 275 ? 0.8375 1.8245 0.7854 0.0376 0.0392 -0.2148 275 ASN A OD1 2202 N ND2 . ASN A 275 ? 0.8470 2.0003 0.8003 0.0476 0.0378 -0.2242 275 ASN A ND2 2203 N N . THR A 276 ? 0.8674 1.5794 0.8187 0.1035 0.0335 -0.1825 276 THR A N 2204 C CA . THR A 276 ? 0.8424 1.4629 0.7890 0.0835 0.0330 -0.1701 276 THR A CA 2205 C C . THR A 276 ? 0.8413 1.4474 0.7688 0.0133 0.0369 -0.1691 276 THR A C 2206 O O . THR A 276 ? 0.8725 1.5242 0.7880 -0.0236 0.0408 -0.1769 276 THR A O 2207 C CB . THR A 276 ? 0.8501 1.3474 0.7969 0.1062 0.0321 -0.1605 276 THR A CB 2208 O OG1 . THR A 276 ? 0.8634 1.2900 0.8073 0.0978 0.0310 -0.1496 276 THR A OG1 2209 C CG2 . THR A 276 ? 0.8607 1.3161 0.8024 0.0774 0.0337 -0.1605 276 THR A CG2 2210 N N . LYS A 277 ? 0.8602 1.3963 0.7766 -0.0042 0.0373 -0.1595 277 LYS A N 2211 C CA . LYS A 277 ? 0.9257 1.4111 0.8052 -0.0643 0.0432 -0.1564 277 LYS A CA 2212 C C . LYS A 277 ? 0.8954 1.2547 0.7604 -0.0595 0.0427 -0.1433 277 LYS A C 2213 O O . LYS A 277 ? 0.9068 1.2019 0.7285 -0.0970 0.0484 -0.1385 277 LYS A O 2214 C CB . LYS A 277 ? 1.0058 1.5072 0.8726 -0.0877 0.0453 -0.1565 277 LYS A CB 2215 C CG . LYS A 277 ? 1.0764 1.7175 0.9448 -0.1119 0.0481 -0.1719 277 LYS A CG 2216 C CD . LYS A 277 ? 1.1818 1.8408 1.0029 -0.1896 0.0588 -0.1815 277 LYS A CD 2217 C CE . LYS A 277 ? 1.2196 2.0336 1.0391 -0.2251 0.0629 -0.1997 277 LYS A CE 2218 N NZ . LYS A 277 ? 1.2986 2.1245 1.0598 -0.3139 0.0765 -0.2112 277 LYS A NZ 2219 N N . CYS A 278 ? 0.8498 1.1742 0.7424 -0.0130 0.0372 -0.1384 278 CYS A N 2220 C CA . CYS A 278 ? 0.8715 1.1019 0.7559 -0.0043 0.0360 -0.1281 278 CYS A CA 2221 C C . CYS A 278 ? 0.8322 1.0568 0.7428 0.0326 0.0328 -0.1303 278 CYS A C 2222 O O . CYS A 278 ? 0.8387 1.0773 0.7678 0.0642 0.0310 -0.1326 278 CYS A O 2223 C CB . CYS A 278 ? 0.9062 1.0908 0.7878 0.0024 0.0343 -0.1198 278 CYS A CB 2224 S SG . CYS A 278 ? 0.9636 1.0619 0.8424 0.0232 0.0316 -0.1095 278 CYS A SG 2225 N N . GLN A 279 ? 0.8084 1.0070 0.7118 0.0281 0.0336 -0.1299 279 GLN A N 2226 C CA . GLN A 279 ? 0.7973 0.9957 0.7191 0.0538 0.0326 -0.1354 279 GLN A CA 2227 C C . GLN A 279 ? 0.7722 0.9148 0.6910 0.0588 0.0316 -0.1302 279 GLN A C 2228 O O . GLN A 279 ? 0.7796 0.8934 0.6775 0.0452 0.0316 -0.1228 279 GLN A O 2229 C CB . GLN A 279 ? 0.8052 1.0493 0.7262 0.0450 0.0344 -0.1436 279 GLN A CB 2230 C CG . GLN A 279 ? 0.7944 1.0399 0.7285 0.0706 0.0348 -0.1518 279 GLN A CG 2231 C CD . GLN A 279 ? 0.8004 1.0664 0.7412 0.1051 0.0358 -0.1585 279 GLN A CD 2232 O OE1 . GLN A 279 ? 0.8031 1.1352 0.7461 0.1135 0.0357 -0.1638 279 GLN A OE1 2233 N NE2 . GLN A 279 ? 0.8130 1.0239 0.7492 0.1259 0.0378 -0.1589 279 GLN A NE2 2234 N N . THR A 280 ? 0.7467 0.8751 0.6780 0.0785 0.0321 -0.1350 280 THR A N 2235 C CA . THR A 280 ? 0.7517 0.8512 0.6818 0.0785 0.0322 -0.1349 280 THR A CA 2236 C C . THR A 280 ? 0.7704 0.8760 0.7037 0.0837 0.0358 -0.1469 280 THR A C 2237 O O . THR A 280 ? 0.7621 0.8773 0.6946 0.0966 0.0387 -0.1543 280 THR A O 2238 C CB . THR A 280 ? 0.7578 0.8268 0.6893 0.0844 0.0321 -0.1316 280 THR A CB 2239 O OG1 . THR A 280 ? 0.7619 0.8141 0.6913 0.0950 0.0369 -0.1401 280 THR A OG1 2240 C CG2 . THR A 280 ? 0.7582 0.8219 0.6876 0.0840 0.0296 -0.1225 280 THR A CG2 2241 N N . PRO A 281 ? 0.8005 0.9036 0.7323 0.0762 0.0363 -0.1499 281 PRO A N 2242 C CA . PRO A 281 ? 0.8260 0.9327 0.7554 0.0737 0.0412 -0.1634 281 PRO A CA 2243 C C . PRO A 281 ? 0.8776 0.9457 0.7920 0.0794 0.0488 -0.1732 281 PRO A C 2244 O O . PRO A 281 ? 0.8959 0.9536 0.7962 0.0775 0.0553 -0.1858 281 PRO A O 2245 C CB . PRO A 281 ? 0.8160 0.9378 0.7452 0.0625 0.0402 -0.1641 281 PRO A CB 2246 C CG . PRO A 281 ? 0.8058 0.9336 0.7319 0.0675 0.0340 -0.1493 281 PRO A CG 2247 C CD . PRO A 281 ? 0.7933 0.8986 0.7191 0.0716 0.0326 -0.1409 281 PRO A CD 2248 N N . MET A 282 ? 0.9278 0.9659 0.8362 0.0861 0.0495 -0.1676 282 MET A N 2249 C CA . MET A 282 ? 1.0092 0.9923 0.8866 0.0949 0.0587 -0.1749 282 MET A CA 2250 C C . MET A 282 ? 0.9777 0.9494 0.8470 0.1257 0.0583 -0.1688 282 MET A C 2251 O O . MET A 282 ? 1.0239 0.9390 0.8562 0.1419 0.0666 -0.1719 282 MET A O 2252 C CB . MET A 282 ? 1.0944 1.0442 0.9568 0.0726 0.0637 -0.1773 282 MET A CB 2253 C CG . MET A 282 ? 1.1372 1.1067 1.0216 0.0690 0.0561 -0.1648 282 MET A CG 2254 S SD . MET A 282 ? 1.3069 1.2633 1.1753 0.0376 0.0623 -0.1717 282 MET A SD 2255 C CE . MET A 282 ? 1.2793 1.2807 1.1484 0.0122 0.0654 -0.1870 282 MET A CE 2256 N N . GLY A 283 ? 0.8969 0.9218 0.7920 0.1334 0.0502 -0.1610 283 GLY A N 2257 C CA . GLY A 283 ? 0.8899 0.9326 0.7807 0.1623 0.0492 -0.1574 283 GLY A CA 2258 C C . GLY A 283 ? 0.8473 0.9412 0.7635 0.1513 0.0413 -0.1481 283 GLY A C 2259 O O . GLY A 283 ? 0.8217 0.9136 0.7499 0.1257 0.0375 -0.1420 283 GLY A O 2260 N N . ALA A 284 ? 0.8382 0.9786 0.7550 0.1720 0.0399 -0.1479 284 ALA A N 2261 C CA . ALA A 284 ? 0.8234 1.0182 0.7560 0.1543 0.0348 -0.1426 284 ALA A CA 2262 C C . ALA A 284 ? 0.8451 1.0174 0.7766 0.1584 0.0334 -0.1339 284 ALA A C 2263 O O . ALA A 284 ? 0.8493 0.9779 0.7656 0.1846 0.0365 -0.1324 284 ALA A O 2264 C CB . ALA A 284 ? 0.8302 1.1116 0.7653 0.1685 0.0344 -0.1498 284 ALA A CB 2265 N N . ILE A 285 ? 0.8306 1.0257 0.7698 0.1307 0.0302 -0.1288 285 ILE A N 2266 C CA . ILE A 285 ? 0.8481 1.0268 0.7872 0.1292 0.0286 -0.1211 285 ILE A CA 2267 C C . ILE A 285 ? 0.8710 1.1254 0.8125 0.1229 0.0275 -0.1233 285 ILE A C 2268 O O . ILE A 285 ? 0.8903 1.1941 0.8296 0.0937 0.0282 -0.1284 285 ILE A O 2269 C CB . ILE A 285 ? 0.8197 0.9491 0.7555 0.1010 0.0272 -0.1138 285 ILE A CB 2270 C CG1 . ILE A 285 ? 0.8138 0.8863 0.7491 0.1106 0.0281 -0.1120 285 ILE A CG1 2271 C CG2 . ILE A 285 ? 0.8299 0.9587 0.7622 0.0907 0.0258 -0.1076 285 ILE A CG2 2272 C CD1 . ILE A 285 ? 0.8107 0.8547 0.7409 0.0926 0.0265 -0.1073 285 ILE A CD1 2273 N N . ASN A 286 ? 0.9234 1.1892 0.8648 0.1473 0.0267 -0.1201 286 ASN A N 2274 C CA . ASN A 286 ? 0.9710 1.3206 0.9152 0.1423 0.0256 -0.1231 286 ASN A CA 2275 C C . ASN A 286 ? 0.9412 1.2619 0.8845 0.1457 0.0242 -0.1148 286 ASN A C 2276 O O . ASN A 286 ? 0.9368 1.2555 0.8757 0.1866 0.0241 -0.1113 286 ASN A O 2277 C CB . ASN A 286 ? 1.0497 1.4787 0.9925 0.1871 0.0259 -0.1303 286 ASN A CB 2278 C CG . ASN A 286 ? 1.1682 1.7070 1.1148 0.1879 0.0245 -0.1350 286 ASN A CG 2279 O OD1 . ASN A 286 ? 1.1384 1.7242 1.0880 0.1361 0.0251 -0.1397 286 ASN A OD1 2280 N ND2 . ASN A 286 ? 1.3559 1.9341 1.2937 0.2470 0.0239 -0.1342 286 ASN A ND2 2281 N N . SER A 287 ? 0.9164 1.2057 0.8561 0.1053 0.0242 -0.1112 287 SER A N 2282 C CA . SER A 287 ? 0.9187 1.1872 0.8572 0.1043 0.0230 -0.1045 287 SER A CA 2283 C C . SER A 287 ? 0.9069 1.1676 0.8294 0.0555 0.0250 -0.1051 287 SER A C 2284 O O . SER A 287 ? 0.8908 1.1346 0.7954 0.0229 0.0283 -0.1083 287 SER A O 2285 C CB . SER A 287 ? 0.9260 1.1073 0.8649 0.1245 0.0221 -0.0955 287 SER A CB 2286 O OG . SER A 287 ? 0.9074 1.0310 0.8401 0.0987 0.0222 -0.0922 287 SER A OG 2287 N N . SER A 288 ? 0.9235 1.1880 0.8439 0.0516 0.0245 -0.1021 288 SER A N 2288 C CA . SER A 288 ? 0.9512 1.1930 0.8444 0.0064 0.0284 -0.1032 288 SER A CA 2289 C C . SER A 288 ? 0.9158 1.0605 0.7979 0.0112 0.0274 -0.0930 288 SER A C 2290 O O . SER A 288 ? 0.9491 1.0567 0.8004 -0.0165 0.0311 -0.0925 288 SER A O 2291 C CB . SER A 288 ? 0.9947 1.3158 0.8891 -0.0058 0.0292 -0.1091 288 SER A CB 2292 O OG . SER A 288 ? 1.0195 1.3486 0.9369 0.0384 0.0242 -0.1019 288 SER A OG 2293 N N . MET A 289 ? 0.8780 0.9839 0.7789 0.0447 0.0236 -0.0865 289 MET A N 2294 C CA . MET A 289 ? 0.8883 0.9249 0.7820 0.0519 0.0222 -0.0787 289 MET A CA 2295 C C . MET A 289 ? 0.9129 0.8972 0.7718 0.0331 0.0254 -0.0779 289 MET A C 2296 O O . MET A 289 ? 0.9536 0.9442 0.8034 0.0223 0.0277 -0.0817 289 MET A O 2297 C CB . MET A 289 ? 0.9021 0.9204 0.8172 0.0817 0.0195 -0.0755 289 MET A CB 2298 C CG . MET A 289 ? 0.9038 0.9461 0.8347 0.1074 0.0189 -0.0746 289 MET A CG 2299 S SD . MET A 289 ? 0.9290 0.9593 0.8606 0.1140 0.0174 -0.0676 289 MET A SD 2300 C CE . MET A 289 ? 0.9178 0.9199 0.8482 0.1459 0.0198 -0.0644 289 MET A CE 2301 N N . PRO A 290 ? 0.9199 0.8501 0.7531 0.0337 0.0261 -0.0724 290 PRO A N 2302 C CA . PRO A 290 ? 0.9390 0.8076 0.7246 0.0287 0.0300 -0.0697 290 PRO A CA 2303 C C . PRO A 290 ? 0.9030 0.7628 0.7007 0.0555 0.0264 -0.0667 290 PRO A C 2304 O O . PRO A 290 ? 0.9537 0.7729 0.7115 0.0580 0.0295 -0.0642 290 PRO A O 2305 C CB . PRO A 290 ? 0.9659 0.7853 0.7175 0.0314 0.0318 -0.0651 290 PRO A CB 2306 C CG . PRO A 290 ? 0.9306 0.7887 0.7309 0.0495 0.0255 -0.0635 290 PRO A CG 2307 C CD . PRO A 290 ? 0.9019 0.8241 0.7404 0.0420 0.0241 -0.0685 290 PRO A CD 2308 N N . PHE A 291 ? 0.8449 0.7398 0.6886 0.0737 0.0215 -0.0675 291 PHE A N 2309 C CA . PHE A 291 ? 0.8152 0.7142 0.6703 0.0916 0.0191 -0.0677 291 PHE A CA 2310 C C . PHE A 291 ? 0.7692 0.7023 0.6596 0.0925 0.0185 -0.0736 291 PHE A C 2311 O O . PHE A 291 ? 0.7632 0.7134 0.6702 0.0916 0.0188 -0.0751 291 PHE A O 2312 C CB . PHE A 291 ? 0.8387 0.7369 0.6996 0.1082 0.0163 -0.0649 291 PHE A CB 2313 C CG . PHE A 291 ? 0.8882 0.7497 0.7075 0.1199 0.0170 -0.0593 291 PHE A CG 2314 C CD1 . PHE A 291 ? 0.9385 0.7809 0.7222 0.1385 0.0177 -0.0567 291 PHE A CD1 2315 C CD2 . PHE A 291 ? 0.9270 0.7707 0.7363 0.1175 0.0173 -0.0563 291 PHE A CD2 2316 C CE1 . PHE A 291 ? 0.9920 0.7893 0.7227 0.1593 0.0196 -0.0508 291 PHE A CE1 2317 C CE2 . PHE A 291 ? 0.9708 0.7703 0.7315 0.1323 0.0192 -0.0517 291 PHE A CE2 2318 C CZ . PHE A 291 ? 1.0153 0.7874 0.7330 0.1558 0.0208 -0.0487 291 PHE A CZ 2319 N N . HIS A 292 ? 0.7560 0.6971 0.6509 0.0978 0.0184 -0.0770 292 HIS A N 2320 C CA . HIS A 292 ? 0.7218 0.6804 0.6386 0.0983 0.0199 -0.0839 292 HIS A CA 2321 C C . HIS A 292 ? 0.7039 0.6743 0.6221 0.0998 0.0202 -0.0885 292 HIS A C 2322 O O . HIS A 292 ? 0.6981 0.6740 0.6027 0.1076 0.0180 -0.0857 292 HIS A O 2323 C CB . HIS A 292 ? 0.7379 0.7103 0.6577 0.0942 0.0216 -0.0884 292 HIS A CB 2324 C CG . HIS A 292 ? 0.7465 0.7221 0.6549 0.0896 0.0217 -0.0897 292 HIS A CG 2325 N ND1 . HIS A 292 ? 0.7254 0.7123 0.6402 0.0918 0.0225 -0.0957 292 HIS A ND1 2326 C CD2 . HIS A 292 ? 0.7708 0.7354 0.6544 0.0808 0.0224 -0.0862 292 HIS A CD2 2327 C CE1 . HIS A 292 ? 0.7448 0.7333 0.6446 0.0897 0.0223 -0.0946 292 HIS A CE1 2328 N NE2 . HIS A 292 ? 0.7781 0.7466 0.6547 0.0829 0.0228 -0.0883 292 HIS A NE2 2329 N N . ASN A 293 ? 0.6885 0.6626 0.6148 0.0932 0.0241 -0.0965 293 ASN A N 2330 C CA . ASN A 293 ? 0.6883 0.6858 0.6139 0.0845 0.0262 -0.1048 293 ASN A CA 2331 C C . ASN A 293 ? 0.7103 0.7067 0.6341 0.0743 0.0315 -0.1152 293 ASN A C 2332 O O . ASN A 293 ? 0.7377 0.7450 0.6550 0.0571 0.0368 -0.1257 293 ASN A O 2333 C CB . ASN A 293 ? 0.6991 0.6990 0.6222 0.0737 0.0290 -0.1076 293 ASN A CB 2334 C CG . ASN A 293 ? 0.7352 0.6915 0.6466 0.0639 0.0365 -0.1106 293 ASN A CG 2335 O OD1 . ASN A 293 ? 0.7428 0.6722 0.6494 0.0730 0.0386 -0.1100 293 ASN A OD1 2336 N ND2 . ASN A 293 ? 0.7720 0.7207 0.6713 0.0475 0.0414 -0.1138 293 ASN A ND2 2337 N N . ILE A 294 ? 0.7218 0.7087 0.6475 0.0820 0.0310 -0.1139 294 ILE A N 2338 C CA . ILE A 294 ? 0.7527 0.7360 0.6738 0.0779 0.0360 -0.1236 294 ILE A CA 2339 C C . ILE A 294 ? 0.7468 0.7639 0.6707 0.0699 0.0352 -0.1297 294 ILE A C 2340 O O . ILE A 294 ? 0.7670 0.7897 0.6834 0.0541 0.0410 -0.1413 294 ILE A O 2341 C CB . ILE A 294 ? 0.7544 0.7374 0.6785 0.0912 0.0348 -0.1211 294 ILE A CB 2342 C CG1 . ILE A 294 ? 0.7708 0.7384 0.6923 0.1043 0.0348 -0.1151 294 ILE A CG1 2343 C CG2 . ILE A 294 ? 0.7876 0.7649 0.7026 0.0928 0.0404 -0.1318 294 ILE A CG2 2344 C CD1 . ILE A 294 ? 0.8148 0.7398 0.7167 0.1065 0.0413 -0.1172 294 ILE A CD1 2345 N N . HIS A 295 ? 0.7508 0.7866 0.6775 0.0793 0.0294 -0.1222 295 HIS A N 2346 C CA . HIS A 295 ? 0.7508 0.8181 0.6748 0.0795 0.0282 -0.1256 295 HIS A CA 2347 C C . HIS A 295 ? 0.7325 0.7971 0.6399 0.0952 0.0234 -0.1133 295 HIS A C 2348 O O . HIS A 295 ? 0.7141 0.7498 0.6121 0.0955 0.0229 -0.1058 295 HIS A O 2349 C CB . HIS A 295 ? 0.7717 0.8388 0.6987 0.0736 0.0316 -0.1337 295 HIS A CB 2350 C CG . HIS A 295 ? 0.7944 0.8969 0.7204 0.0686 0.0324 -0.1414 295 HIS A CG 2351 N ND1 . HIS A 295 ? 0.8008 0.9213 0.7186 0.0797 0.0283 -0.1345 295 HIS A ND1 2352 C CD2 . HIS A 295 ? 0.8273 0.9484 0.7529 0.0523 0.0379 -0.1560 295 HIS A CD2 2353 C CE1 . HIS A 295 ? 0.8167 0.9758 0.7359 0.0749 0.0297 -0.1436 295 HIS A CE1 2354 N NE2 . HIS A 295 ? 0.8226 0.9862 0.7484 0.0553 0.0356 -0.1579 295 HIS A NE2 2355 N N . PRO A 296 ? 0.7382 0.8315 0.6327 0.1084 0.0213 -0.1119 296 PRO A N 2356 C CA . PRO A 296 ? 0.7706 0.8400 0.6284 0.1307 0.0190 -0.0988 296 PRO A CA 2357 C C . PRO A 296 ? 0.7893 0.8287 0.6248 0.1259 0.0211 -0.0943 296 PRO A C 2358 O O . PRO A 296 ? 0.8232 0.8122 0.6184 0.1299 0.0229 -0.0838 296 PRO A O 2359 C CB . PRO A 296 ? 0.7726 0.8942 0.6198 0.1535 0.0168 -0.1004 296 PRO A CB 2360 C CG . PRO A 296 ? 0.7498 0.9279 0.6299 0.1317 0.0186 -0.1166 296 PRO A CG 2361 C CD . PRO A 296 ? 0.7405 0.8913 0.6444 0.1047 0.0220 -0.1230 296 PRO A CD 2362 N N . LEU A 297 ? 0.8007 0.8678 0.6548 0.1142 0.0223 -0.1031 297 LEU A N 2363 C CA . LEU A 297 ? 0.8443 0.8941 0.6792 0.1060 0.0246 -0.1004 297 LEU A CA 2364 C C . LEU A 297 ? 0.8378 0.8778 0.6882 0.0838 0.0267 -0.1040 297 LEU A C 2365 O O . LEU A 297 ? 0.8589 0.9262 0.7408 0.0766 0.0273 -0.1146 297 LEU A O 2366 C CB . LEU A 297 ? 0.8323 0.9254 0.6792 0.1064 0.0247 -0.1089 297 LEU A CB 2367 C CG . LEU A 297 ? 0.8497 0.9828 0.6884 0.1289 0.0223 -0.1092 297 LEU A CG 2368 C CD1 . LEU A 297 ? 0.8403 1.0252 0.6932 0.1238 0.0230 -0.1201 297 LEU A CD1 2369 C CD2 . LEU A 297 ? 0.8980 0.9941 0.6808 0.1594 0.0218 -0.0931 297 LEU A CD2 2370 N N . THR A 298 ? 0.8482 0.8507 0.6695 0.0743 0.0289 -0.0961 298 THR A N 2371 C CA . THR A 298 ? 0.8197 0.8338 0.6527 0.0526 0.0309 -0.1007 298 THR A CA 2372 C C . THR A 298 ? 0.8556 0.8506 0.6456 0.0289 0.0362 -0.0976 298 THR A C 2373 O O . THR A 298 ? 0.8754 0.8228 0.6147 0.0314 0.0394 -0.0889 298 THR A O 2374 C CB . THR A 298 ? 0.8184 0.8203 0.6574 0.0511 0.0301 -0.0980 298 THR A CB 2375 O OG1 . THR A 298 ? 0.8591 0.8091 0.6484 0.0431 0.0334 -0.0886 298 THR A OG1 2376 C CG2 . THR A 298 ? 0.8088 0.8159 0.6753 0.0707 0.0265 -0.0991 298 THR A CG2 2377 N N . ILE A 299 ? 0.8546 0.8879 0.6575 0.0065 0.0383 -0.1052 299 ILE A N 2378 C CA . ILE A 299 ? 0.9030 0.9276 0.6614 -0.0290 0.0453 -0.1052 299 ILE A CA 2379 C C . ILE A 299 ? 0.9083 0.9743 0.6756 -0.0536 0.0473 -0.1120 299 ILE A C 2380 O O . ILE A 299 ? 0.8661 0.9909 0.6828 -0.0368 0.0426 -0.1191 299 ILE A O 2381 C CB . ILE A 299 ? 0.9062 0.9665 0.6685 -0.0370 0.0467 -0.1113 299 ILE A CB 2382 C CG1 . ILE A 299 ? 0.9517 1.0005 0.6584 -0.0824 0.0560 -0.1120 299 ILE A CG1 2383 C CG2 . ILE A 299 ? 0.8539 0.9930 0.6758 -0.0237 0.0422 -0.1240 299 ILE A CG2 2384 C CD1 . ILE A 299 ? 0.9644 1.0338 0.6620 -0.0916 0.0583 -0.1153 299 ILE A CD1 2385 N N . GLY A 300 ? 0.9835 1.0161 0.6941 -0.0929 0.0557 -0.1102 300 GLY A N 2386 C CA . GLY A 300 ? 1.0307 1.1110 0.7414 -0.1245 0.0590 -0.1182 300 GLY A CA 2387 C C . GLY A 300 ? 1.1096 1.1245 0.7845 -0.1325 0.0622 -0.1113 300 GLY A C 2388 O O . GLY A 300 ? 1.1623 1.0833 0.7916 -0.1206 0.0646 -0.1000 300 GLY A O 2389 N N . GLU A 301 ? 1.1324 1.2017 0.8247 -0.1485 0.0623 -0.1183 301 GLU A N 2390 C CA . GLU A 301 ? 1.2086 1.2255 0.8724 -0.1565 0.0650 -0.1136 301 GLU A CA 2391 C C . GLU A 301 ? 1.1005 1.1322 0.8255 -0.1049 0.0538 -0.1085 301 GLU A C 2392 O O . GLU A 301 ? 1.0405 1.1514 0.8150 -0.0917 0.0486 -0.1147 301 GLU A O 2393 C CB . GLU A 301 ? 1.3037 1.3784 0.9476 -0.2089 0.0724 -0.1256 301 GLU A CB 2394 C CG . GLU A 301 ? 1.4631 1.4423 1.0239 -0.2497 0.0843 -0.1229 301 GLU A CG 2395 C CD . GLU A 301 ? 1.6111 1.4872 1.0773 -0.2851 0.0979 -0.1193 301 GLU A CD 2396 O OE1 . GLU A 301 ? 1.6493 1.5682 1.0923 -0.3319 0.1057 -0.1295 301 GLU A OE1 2397 O OE2 . GLU A 301 ? 1.7203 1.4736 1.1304 -0.2629 0.1012 -0.1063 301 GLU A OE2 2398 N N . CYS A 302 ? 1.0703 1.0275 0.7849 -0.0745 0.0510 -0.0976 302 CYS A N 2399 C CA . CYS A 302 ? 1.0086 0.9788 0.7765 -0.0308 0.0418 -0.0939 302 CYS A CA 2400 C C . CYS A 302 ? 1.0015 0.9186 0.7524 -0.0189 0.0411 -0.0862 302 CYS A C 2401 O O . CYS A 302 ? 1.0171 0.8651 0.7062 -0.0333 0.0476 -0.0812 302 CYS A O 2402 C CB . CYS A 302 ? 1.0134 0.9741 0.7973 -0.0028 0.0379 -0.0914 302 CYS A CB 2403 S SG . CYS A 302 ? 1.0399 1.0662 0.8532 -0.0069 0.0374 -0.1013 302 CYS A SG 2404 N N . PRO A 303 ? 0.9481 0.8906 0.7460 0.0081 0.0343 -0.0853 303 PRO A N 2405 C CA . PRO A 303 ? 0.9532 0.8524 0.7410 0.0253 0.0325 -0.0780 303 PRO A CA 2406 C C . PRO A 303 ? 0.9597 0.8238 0.7318 0.0503 0.0309 -0.0724 303 PRO A C 2407 O O . PRO A 303 ? 0.9635 0.8460 0.7471 0.0558 0.0299 -0.0749 303 PRO A O 2408 C CB . PRO A 303 ? 0.9045 0.8461 0.7448 0.0436 0.0269 -0.0797 303 PRO A CB 2409 C CG . PRO A 303 ? 0.8836 0.8839 0.7520 0.0402 0.0267 -0.0873 303 PRO A CG 2410 C CD . PRO A 303 ? 0.9044 0.9082 0.7558 0.0254 0.0297 -0.0909 303 PRO A CD 2411 N N . LYS A 304 ? 0.9806 0.8036 0.7259 0.0680 0.0306 -0.0658 304 LYS A N 2412 C CA . LYS A 304 ? 0.9988 0.8050 0.7247 0.0991 0.0288 -0.0609 304 LYS A CA 2413 C C . LYS A 304 ? 0.9139 0.7797 0.6970 0.1158 0.0222 -0.0654 304 LYS A C 2414 O O . LYS A 304 ? 0.8965 0.7838 0.7125 0.1143 0.0197 -0.0674 304 LYS A O 2415 C CB . LYS A 304 ? 1.0965 0.8421 0.7643 0.1191 0.0314 -0.0530 304 LYS A CB 2416 C CG . LYS A 304 ? 1.2345 0.8986 0.8255 0.0952 0.0416 -0.0498 304 LYS A CG 2417 C CD . LYS A 304 ? 1.3336 0.9555 0.8707 0.0870 0.0484 -0.0476 304 LYS A CD 2418 C CE . LYS A 304 ? 1.4023 0.9934 0.9018 0.0328 0.0584 -0.0526 304 LYS A CE 2419 N NZ . LYS A 304 ? 1.4948 1.0296 0.9258 0.0213 0.0673 -0.0496 304 LYS A NZ 2420 N N . TYR A 305 ? 0.8734 0.7636 0.6619 0.1279 0.0209 -0.0676 305 TYR A N 2421 C CA . TYR A 305 ? 0.8213 0.7669 0.6528 0.1336 0.0174 -0.0749 305 TYR A CA 2422 C C . TYR A 305 ? 0.8114 0.7746 0.6357 0.1567 0.0147 -0.0728 305 TYR A C 2423 O O . TYR A 305 ? 0.8413 0.7872 0.6230 0.1841 0.0145 -0.0661 305 TYR A O 2424 C CB . TYR A 305 ? 0.8156 0.7903 0.6522 0.1351 0.0177 -0.0801 305 TYR A CB 2425 C CG . TYR A 305 ? 0.7658 0.7972 0.6350 0.1330 0.0165 -0.0903 305 TYR A CG 2426 C CD1 . TYR A 305 ? 0.7364 0.7768 0.6358 0.1113 0.0191 -0.0994 305 TYR A CD1 2427 C CD2 . TYR A 305 ? 0.7726 0.8480 0.6328 0.1524 0.0144 -0.0919 305 TYR A CD2 2428 C CE1 . TYR A 305 ? 0.7322 0.8100 0.6461 0.0994 0.0214 -0.1107 305 TYR A CE1 2429 C CE2 . TYR A 305 ? 0.7686 0.9056 0.6539 0.1394 0.0153 -0.1046 305 TYR A CE2 2430 C CZ . TYR A 305 ? 0.7355 0.8662 0.6445 0.1081 0.0197 -0.1143 305 TYR A CZ 2431 O OH . TYR A 305 ? 0.7302 0.9076 0.6492 0.0856 0.0239 -0.1286 305 TYR A OH 2432 N N . VAL A 306 ? 0.7709 0.7676 0.6295 0.1475 0.0135 -0.0786 306 VAL A N 2433 C CA . VAL A 306 ? 0.7480 0.7874 0.6078 0.1627 0.0112 -0.0806 306 VAL A CA 2434 C C . VAL A 306 ? 0.7224 0.8146 0.6147 0.1390 0.0132 -0.0935 306 VAL A C 2435 O O . VAL A 306 ? 0.7234 0.7957 0.6321 0.1154 0.0167 -0.0981 306 VAL A O 2436 C CB . VAL A 306 ? 0.7570 0.7730 0.6114 0.1673 0.0102 -0.0750 306 VAL A CB 2437 C CG1 . VAL A 306 ? 0.7942 0.7488 0.6007 0.1873 0.0109 -0.0644 306 VAL A CG1 2438 C CG2 . VAL A 306 ? 0.7435 0.7408 0.6257 0.1401 0.0121 -0.0768 306 VAL A CG2 2439 N N . LYS A 307 ? 0.7526 0.9118 0.6461 0.1453 0.0122 -0.1002 307 LYS A N 2440 C CA . LYS A 307 ? 0.7828 0.9929 0.6950 0.1119 0.0168 -0.1153 307 LYS A CA 2441 C C . LYS A 307 ? 0.7976 0.9950 0.7174 0.0862 0.0208 -0.1184 307 LYS A C 2442 O O . LYS A 307 ? 0.8778 1.1065 0.7986 0.0519 0.0274 -0.1316 307 LYS A O 2443 C CB . LYS A 307 ? 0.7972 1.1064 0.7055 0.1227 0.0151 -0.1243 307 LYS A CB 2444 C CG . LYS A 307 ? 0.8113 1.1521 0.7165 0.1282 0.0151 -0.1292 307 LYS A CG 2445 C CD . LYS A 307 ? 0.8455 1.3049 0.7469 0.1416 0.0132 -0.1393 307 LYS A CD 2446 C CE . LYS A 307 ? 0.8832 1.3869 0.7804 0.1501 0.0128 -0.1444 307 LYS A CE 2447 N NZ . LYS A 307 ? 0.9139 1.5487 0.8034 0.1753 0.0097 -0.1529 307 LYS A NZ 2448 N N . SER A 308 ? 0.7815 0.9309 0.6996 0.0984 0.0182 -0.1071 308 SER A N 2449 C CA . SER A 308 ? 0.7625 0.9010 0.6839 0.0787 0.0216 -0.1083 308 SER A CA 2450 C C . SER A 308 ? 0.7787 0.8643 0.6967 0.0492 0.0298 -0.1126 308 SER A C 2451 O O . SER A 308 ? 0.7807 0.8245 0.6986 0.0540 0.0307 -0.1100 308 SER A O 2452 C CB . SER A 308 ? 0.7433 0.8448 0.6621 0.1010 0.0168 -0.0953 308 SER A CB 2453 O OG . SER A 308 ? 0.7468 0.8686 0.6515 0.1353 0.0110 -0.0897 308 SER A OG 2454 N N . ASN A 309 ? 0.8255 0.9102 0.7326 0.0206 0.0369 -0.1191 309 ASN A N 2455 C CA . ASN A 309 ? 0.8858 0.8968 0.7707 0.0007 0.0466 -0.1200 309 ASN A CA 2456 C C . ASN A 309 ? 0.8631 0.8269 0.7492 0.0203 0.0437 -0.1063 309 ASN A C 2457 O O . ASN A 309 ? 0.9063 0.8069 0.7729 0.0228 0.0494 -0.1028 309 ASN A O 2458 C CB . ASN A 309 ? 0.9656 0.9812 0.8204 -0.0458 0.0591 -0.1341 309 ASN A CB 2459 C CG . ASN A 309 ? 1.0417 1.0927 0.8861 -0.0744 0.0656 -0.1508 309 ASN A CG 2460 O OD1 . ASN A 309 ? 1.0826 1.1002 0.9234 -0.0669 0.0670 -0.1521 309 ASN A OD1 2461 N ND2 . ASN A 309 ? 1.0688 1.1977 0.9080 -0.1087 0.0697 -0.1651 309 ASN A ND2 2462 N N . ARG A 310 ? 0.8082 0.8039 0.7118 0.0380 0.0354 -0.0988 310 ARG A N 2463 C CA . ARG A 310 ? 0.8072 0.7698 0.7115 0.0509 0.0331 -0.0878 310 ARG A CA 2464 C C . ARG A 310 ? 0.7424 0.7306 0.6618 0.0759 0.0235 -0.0799 310 ARG A C 2465 O O . ARG A 310 ? 0.7012 0.7366 0.6225 0.0807 0.0203 -0.0828 310 ARG A O 2466 C CB . ARG A 310 ? 0.8651 0.8184 0.7504 0.0259 0.0405 -0.0908 310 ARG A CB 2467 C CG . ARG A 310 ? 0.9065 0.8150 0.7842 0.0368 0.0409 -0.0798 310 ARG A CG 2468 C CD . ARG A 310 ? 0.9703 0.8615 0.8194 0.0077 0.0503 -0.0829 310 ARG A CD 2469 N NE . ARG A 310 ? 1.0251 0.9057 0.8779 0.0216 0.0468 -0.0721 310 ARG A NE 2470 C CZ . ARG A 310 ? 1.0519 0.8793 0.8908 0.0409 0.0483 -0.0618 310 ARG A CZ 2471 N NH1 . ARG A 310 ? 1.1055 0.8836 0.9229 0.0535 0.0534 -0.0605 310 ARG A NH1 2472 N NH2 . ARG A 310 ? 1.0489 0.8791 0.8935 0.0514 0.0448 -0.0532 310 ARG A NH2 2473 N N . LEU A 311 ? 0.7117 0.6702 0.6344 0.0919 0.0201 -0.0714 311 LEU A N 2474 C CA . LEU A 311 ? 0.6905 0.6510 0.6122 0.1084 0.0144 -0.0646 311 LEU A CA 2475 C C . LEU A 311 ? 0.6840 0.6194 0.6074 0.1095 0.0144 -0.0580 311 LEU A C 2476 O O . LEU A 311 ? 0.7022 0.6250 0.6270 0.1112 0.0150 -0.0563 311 LEU A O 2477 C CB . LEU A 311 ? 0.6811 0.6350 0.5923 0.1209 0.0116 -0.0633 311 LEU A CB 2478 C CG . LEU A 311 ? 0.7008 0.6833 0.6039 0.1306 0.0105 -0.0678 311 LEU A CG 2479 C CD1 . LEU A 311 ? 0.7283 0.6843 0.6093 0.1423 0.0099 -0.0644 311 LEU A CD1 2480 C CD2 . LEU A 311 ? 0.7112 0.7296 0.6056 0.1466 0.0080 -0.0685 311 LEU A CD2 2481 N N . VAL A 312 ? 0.6617 0.6013 0.5850 0.1092 0.0139 -0.0550 312 VAL A N 2482 C CA . VAL A 312 ? 0.6597 0.5846 0.5842 0.1116 0.0138 -0.0488 312 VAL A CA 2483 C C . VAL A 312 ? 0.6455 0.5772 0.5661 0.1175 0.0102 -0.0458 312 VAL A C 2484 O O . VAL A 312 ? 0.6279 0.5778 0.5473 0.1183 0.0095 -0.0473 312 VAL A O 2485 C CB . VAL A 312 ? 0.6800 0.5894 0.5985 0.1044 0.0192 -0.0474 312 VAL A CB 2486 C CG1 . VAL A 312 ? 0.6887 0.5885 0.6054 0.1144 0.0188 -0.0398 312 VAL A CG1 2487 C CG2 . VAL A 312 ? 0.7000 0.5870 0.6074 0.0998 0.0252 -0.0516 312 VAL A CG2 2488 N N . LEU A 313 ? 0.6330 0.5543 0.5472 0.1194 0.0089 -0.0432 313 LEU A N 2489 C CA . LEU A 313 ? 0.6445 0.5587 0.5443 0.1229 0.0074 -0.0414 313 LEU A CA 2490 C C . LEU A 313 ? 0.6420 0.5658 0.5523 0.1201 0.0072 -0.0374 313 LEU A C 2491 O O . LEU A 313 ? 0.6467 0.5784 0.5664 0.1181 0.0083 -0.0354 313 LEU A O 2492 C CB . LEU A 313 ? 0.6590 0.5488 0.5327 0.1163 0.0091 -0.0430 313 LEU A CB 2493 C CG . LEU A 313 ? 0.6974 0.5587 0.5399 0.1239 0.0104 -0.0449 313 LEU A CG 2494 C CD1 . LEU A 313 ? 0.7360 0.5644 0.5447 0.1056 0.0153 -0.0473 313 LEU A CD1 2495 C CD2 . LEU A 313 ? 0.7297 0.5762 0.5450 0.1462 0.0096 -0.0438 313 LEU A CD2 2496 N N . ALA A 314 ? 0.6426 0.5696 0.5480 0.1245 0.0058 -0.0362 314 ALA A N 2497 C CA . ALA A 314 ? 0.6332 0.5685 0.5446 0.1222 0.0055 -0.0321 314 ALA A CA 2498 C C . ALA A 314 ? 0.6433 0.5721 0.5405 0.1149 0.0061 -0.0337 314 ALA A C 2499 O O . ALA A 314 ? 0.6697 0.5721 0.5388 0.1127 0.0075 -0.0375 314 ALA A O 2500 C CB . ALA A 314 ? 0.6311 0.5773 0.5409 0.1273 0.0041 -0.0316 314 ALA A CB 2501 N N . THR A 315 ? 0.6413 0.5928 0.5491 0.1108 0.0064 -0.0315 315 THR A N 2502 C CA . THR A 315 ? 0.6489 0.6131 0.5437 0.0961 0.0079 -0.0353 315 THR A CA 2503 C C . THR A 315 ? 0.6286 0.6110 0.5295 0.0993 0.0065 -0.0317 315 THR A C 2504 O O . THR A 315 ? 0.6598 0.6324 0.5414 0.0886 0.0079 -0.0355 315 THR A O 2505 C CB . THR A 315 ? 0.6533 0.6559 0.5559 0.0894 0.0090 -0.0381 315 THR A CB 2506 O OG1 . THR A 315 ? 0.6407 0.6616 0.5635 0.1119 0.0076 -0.0314 315 THR A OG1 2507 C CG2 . THR A 315 ? 0.6721 0.6563 0.5609 0.0776 0.0114 -0.0438 315 THR A CG2 2508 N N . GLY A 316 ? 0.6005 0.6006 0.5199 0.1143 0.0052 -0.0242 316 GLY A N 2509 C CA . GLY A 316 ? 0.5966 0.6126 0.5197 0.1198 0.0042 -0.0190 316 GLY A CA 2510 C C . GLY A 316 ? 0.6023 0.5962 0.5240 0.1218 0.0034 -0.0169 316 GLY A C 2511 O O . GLY A 316 ? 0.6122 0.5869 0.5268 0.1201 0.0031 -0.0213 316 GLY A O 2512 N N . LEU A 317 ? 0.6104 0.6128 0.5354 0.1276 0.0035 -0.0101 317 LEU A N 2513 C CA . LEU A 317 ? 0.6189 0.6164 0.5424 0.1254 0.0029 -0.0097 317 LEU A CA 2514 C C . LEU A 317 ? 0.6149 0.5996 0.5344 0.1243 0.0066 -0.0036 317 LEU A C 2515 O O . LEU A 317 ? 0.6149 0.5799 0.5255 0.1297 0.0102 0.0014 317 LEU A O 2516 C CB . LEU A 317 ? 0.6372 0.6527 0.5590 0.1243 0.0013 -0.0096 317 LEU A CB 2517 C CG . LEU A 317 ? 0.6412 0.6819 0.5658 0.1277 0.0014 -0.0046 317 LEU A CG 2518 C CD1 . LEU A 317 ? 0.6649 0.6975 0.5858 0.1402 0.0038 0.0067 317 LEU A CD1 2519 C CD2 . LEU A 317 ? 0.6531 0.7127 0.5745 0.1217 0.0001 -0.0074 317 LEU A CD2 2520 N N . ARG A 318 ? 0.6178 0.6115 0.5357 0.1160 0.0070 -0.0052 318 ARG A N 2521 C CA . ARG A 318 ? 0.6691 0.6494 0.5727 0.1019 0.0131 -0.0027 318 ARG A CA 2522 C C . ARG A 318 ? 0.7129 0.6642 0.5961 0.1066 0.0179 0.0087 318 ARG A C 2523 O O . ARG A 318 ? 0.7017 0.6691 0.5887 0.1146 0.0153 0.0135 318 ARG A O 2524 C CB . ARG A 318 ? 0.6789 0.6960 0.5852 0.0898 0.0123 -0.0085 318 ARG A CB 2525 C CG . ARG A 318 ? 0.7368 0.7507 0.6229 0.0616 0.0206 -0.0103 318 ARG A CG 2526 C CD . ARG A 318 ? 0.7526 0.8267 0.6441 0.0496 0.0193 -0.0178 318 ARG A CD 2527 N NE . ARG A 318 ? 0.7476 0.8736 0.6533 0.0580 0.0146 -0.0293 318 ARG A NE 2528 C CZ . ARG A 318 ? 0.7596 0.9227 0.6597 0.0362 0.0187 -0.0392 318 ARG A CZ 2529 N NH1 . ARG A 318 ? 0.7977 0.9405 0.6727 -0.0039 0.0295 -0.0404 318 ARG A NH1 2530 N NH2 . ARG A 318 ? 0.7592 0.9777 0.6705 0.0545 0.0134 -0.0486 318 ARG A NH2 2531 N N . ASN A 319 ? 0.7932 0.6970 0.6471 0.1044 0.0259 0.0130 319 ASN A N 2532 C CA . ASN A 319 ? 0.8604 0.7198 0.6774 0.1201 0.0323 0.0256 319 ASN A CA 2533 C C . ASN A 319 ? 0.9813 0.8023 0.7572 0.0972 0.0421 0.0300 319 ASN A C 2534 O O . ASN A 319 ? 1.0496 0.8655 0.8145 0.0632 0.0477 0.0218 319 ASN A O 2535 C CB . ASN A 319 ? 0.8690 0.6827 0.6598 0.1377 0.0375 0.0283 319 ASN A CB 2536 C CG . ASN A 319 ? 0.9041 0.6874 0.6579 0.1746 0.0415 0.0418 319 ASN A CG 2537 O OD1 . ASN A 319 ? 0.8817 0.6944 0.6419 0.1887 0.0378 0.0484 319 ASN A OD1 2538 N ND2 . ASN A 319 ? 0.9636 0.6894 0.6739 0.1947 0.0493 0.0457 319 ASN A ND2 2539 N N . SER A 320 ? 1.1259 0.9247 0.8748 0.1140 0.0450 0.0423 320 SER A N 2540 C CA . SER A 320 ? 1.2237 0.9904 0.9323 0.0903 0.0540 0.0473 320 SER A CA 2541 C C . SER A 320 ? 1.3590 1.0175 0.9820 0.0858 0.0712 0.0559 320 SER A C 2542 O O . SER A 320 ? 1.3606 0.9712 0.9516 0.1242 0.0742 0.0649 320 SER A O 2543 C CB . SER A 320 ? 1.2107 1.0097 0.9312 0.1116 0.0483 0.0566 320 SER A CB 2544 O OG . SER A 320 ? 1.1357 1.0155 0.9204 0.1209 0.0346 0.0488 320 SER A OG 2545 N N . PRO A 321 ? 1.4890 1.1077 1.0661 0.0381 0.0839 0.0521 321 PRO A N 2546 C CA . PRO A 321 ? 1.6312 1.1243 1.1050 0.0263 0.1042 0.0600 321 PRO A CA 2547 C C . PRO A 321 ? 1.6911 1.1273 1.1082 0.0526 0.1106 0.0786 321 PRO A C 2548 O O . PRO A 321 ? 1.7736 1.1505 1.1472 0.1057 0.1136 0.0926 321 PRO A O 2549 C CB . PRO A 321 ? 1.6714 1.1644 1.1212 -0.0465 0.1155 0.0453 321 PRO A CB 2550 C CG . PRO A 321 ? 1.5901 1.2047 1.1166 -0.0601 0.1016 0.0378 321 PRO A CG 2551 C CD . PRO A 321 ? 1.4821 1.1720 1.0922 -0.0088 0.0815 0.0389 321 PRO A CD 2552 N N . GLY B 1 ? 0.5679 0.6725 0.7169 -0.0393 -0.1095 0.1231 1 GLY B N 2553 C CA . GLY B 1 ? 0.5388 0.6346 0.6823 -0.0152 -0.0970 0.0995 1 GLY B CA 2554 C C . GLY B 1 ? 0.5022 0.6552 0.6601 0.0054 -0.0834 0.1032 1 GLY B C 2555 O O . GLY B 1 ? 0.5077 0.7132 0.6813 0.0087 -0.0781 0.1204 1 GLY B O 2556 N N . LEU B 2 ? 0.4836 0.6222 0.6292 0.0224 -0.0778 0.0870 2 LEU B N 2557 C CA . LEU B 2 ? 0.4746 0.6524 0.6190 0.0490 -0.0676 0.0876 2 LEU B CA 2558 C C . LEU B 2 ? 0.4689 0.6626 0.6068 0.0704 -0.0542 0.0834 2 LEU B C 2559 O O . LEU B 2 ? 0.4658 0.7066 0.6042 0.0936 -0.0476 0.0925 2 LEU B O 2560 C CB . LEU B 2 ? 0.4739 0.6103 0.5920 0.0629 -0.0657 0.0679 2 LEU B CB 2561 C CG . LEU B 2 ? 0.4705 0.5991 0.5903 0.0516 -0.0780 0.0719 2 LEU B CG 2562 C CD1 . LEU B 2 ? 0.4910 0.5696 0.5777 0.0663 -0.0742 0.0513 2 LEU B CD1 2563 C CD2 . LEU B 2 ? 0.4637 0.6646 0.6067 0.0550 -0.0837 0.0952 2 LEU B CD2 2564 N N . PHE B 3 ? 0.4541 0.6113 0.5830 0.0658 -0.0511 0.0698 3 PHE B N 2565 C CA . PHE B 3 ? 0.4649 0.6265 0.5811 0.0857 -0.0411 0.0617 3 PHE B CA 2566 C C . PHE B 3 ? 0.4629 0.6592 0.5957 0.0822 -0.0392 0.0773 3 PHE B C 2567 O O . PHE B 3 ? 0.4876 0.6908 0.6094 0.0998 -0.0320 0.0722 3 PHE B O 2568 C CB . PHE B 3 ? 0.4681 0.5754 0.5612 0.0846 -0.0389 0.0364 3 PHE B CB 2569 C CG . PHE B 3 ? 0.4854 0.5584 0.5536 0.0903 -0.0392 0.0235 3 PHE B CG 2570 C CD1 . PHE B 3 ? 0.5051 0.5668 0.5413 0.1142 -0.0359 0.0162 3 PHE B CD1 2571 C CD2 . PHE B 3 ? 0.4897 0.5373 0.5594 0.0747 -0.0443 0.0201 3 PHE B CD2 2572 C CE1 . PHE B 3 ? 0.5479 0.5693 0.5525 0.1203 -0.0380 0.0058 3 PHE B CE1 2573 C CE2 . PHE B 3 ? 0.5158 0.5305 0.5593 0.0803 -0.0446 0.0103 3 PHE B CE2 2574 C CZ . PHE B 3 ? 0.5411 0.5412 0.5515 0.1021 -0.0416 0.0035 3 PHE B CZ 2575 N N . GLY B 4 ? 0.4553 0.6684 0.6089 0.0584 -0.0477 0.0971 4 GLY B N 2576 C CA . GLY B 4 ? 0.4480 0.6990 0.6152 0.0516 -0.0470 0.1190 4 GLY B CA 2577 C C . GLY B 4 ? 0.4500 0.6687 0.6077 0.0473 -0.0478 0.1119 4 GLY B C 2578 O O . GLY B 4 ? 0.4661 0.7063 0.6297 0.0387 -0.0492 0.1312 4 GLY B O 2579 N N . ALA B 5 ? 0.4383 0.6102 0.5806 0.0529 -0.0474 0.0864 5 ALA B N 2580 C CA . ALA B 5 ? 0.4412 0.5930 0.5743 0.0556 -0.0476 0.0782 5 ALA B CA 2581 C C . ALA B 5 ? 0.4627 0.5769 0.5885 0.0381 -0.0604 0.0820 5 ALA B C 2582 O O . ALA B 5 ? 0.4749 0.5879 0.5964 0.0299 -0.0664 0.0983 5 ALA B O 2583 C CB . ALA B 5 ? 0.4433 0.5757 0.5641 0.0695 -0.0419 0.0515 5 ALA B CB 2584 N N . ILE B 6 ? 0.4749 0.5532 0.5922 0.0342 -0.0654 0.0673 6 ILE B N 2585 C CA . ILE B 6 ? 0.5131 0.5450 0.6113 0.0252 -0.0792 0.0673 6 ILE B CA 2586 C C . ILE B 6 ? 0.5505 0.5740 0.6465 0.0006 -0.0942 0.0930 6 ILE B C 2587 O O . ILE B 6 ? 0.5471 0.5910 0.6577 -0.0124 -0.0967 0.1035 6 ILE B O 2588 C CB . ILE B 6 ? 0.5171 0.5184 0.6047 0.0286 -0.0805 0.0485 6 ILE B CB 2589 C CG1 . ILE B 6 ? 0.5067 0.5167 0.5930 0.0462 -0.0691 0.0268 6 ILE B CG1 2590 C CG2 . ILE B 6 ? 0.5591 0.5067 0.6182 0.0222 -0.0978 0.0512 6 ILE B CG2 2591 C CD1 . ILE B 6 ? 0.5108 0.5067 0.5907 0.0483 -0.0658 0.0108 6 ILE B CD1 2592 N N . ALA B 7 ? 0.5956 0.5889 0.6701 -0.0067 -0.1058 0.1040 7 ALA B N 2593 C CA . ALA B 7 ? 0.6481 0.6278 0.7139 -0.0377 -0.1234 0.1321 7 ALA B CA 2594 C C . ALA B 7 ? 0.6382 0.6918 0.7402 -0.0518 -0.1156 0.1560 7 ALA B C 2595 O O . ALA B 7 ? 0.6710 0.7368 0.7806 -0.0809 -0.1282 0.1778 7 ALA B O 2596 C CB . ALA B 7 ? 0.6854 0.6109 0.7289 -0.0536 -0.1429 0.1301 7 ALA B CB 2597 N N . GLY B 8 ? 0.6163 0.7218 0.7379 -0.0294 -0.0957 0.1517 8 GLY B N 2598 C CA . GLY B 8 ? 0.5958 0.7784 0.7463 -0.0303 -0.0849 0.1725 8 GLY B CA 2599 C C . GLY B 8 ? 0.6115 0.8187 0.7593 -0.0194 -0.0753 0.1825 8 GLY B C 2600 O O . GLY B 8 ? 0.6473 0.8370 0.7813 -0.0400 -0.0855 0.2022 8 GLY B O 2601 N N . PHE B 9 ? 0.5828 0.8217 0.7365 0.0127 -0.0579 0.1685 9 PHE B N 2602 C CA . PHE B 9 ? 0.5809 0.8393 0.7275 0.0273 -0.0491 0.1750 9 PHE B CA 2603 C C . PHE B 9 ? 0.6000 0.7992 0.7215 0.0344 -0.0550 0.1561 9 PHE B C 2604 O O . PHE B 9 ? 0.6258 0.8253 0.7348 0.0390 -0.0539 0.1653 9 PHE B O 2605 C CB . PHE B 9 ? 0.5557 0.8647 0.7083 0.0610 -0.0316 0.1684 9 PHE B CB 2606 C CG . PHE B 9 ? 0.5370 0.8133 0.6768 0.0849 -0.0277 0.1334 9 PHE B CG 2607 C CD1 . PHE B 9 ? 0.5459 0.7952 0.6690 0.0988 -0.0269 0.1152 9 PHE B CD1 2608 C CD2 . PHE B 9 ? 0.5153 0.7896 0.6572 0.0918 -0.0260 0.1203 9 PHE B CD2 2609 C CE1 . PHE B 9 ? 0.5379 0.7622 0.6498 0.1132 -0.0257 0.0861 9 PHE B CE1 2610 C CE2 . PHE B 9 ? 0.5130 0.7532 0.6383 0.1070 -0.0242 0.0913 9 PHE B CE2 2611 C CZ . PHE B 9 ? 0.5282 0.7455 0.6399 0.1149 -0.0245 0.0750 9 PHE B CZ 2612 N N . ILE B 10 ? 0.6015 0.7552 0.7146 0.0375 -0.0608 0.1312 10 ILE B N 2613 C CA . ILE B 10 ? 0.6294 0.7316 0.7173 0.0441 -0.0691 0.1167 10 ILE B CA 2614 C C . ILE B 10 ? 0.6903 0.7403 0.7579 0.0208 -0.0877 0.1272 10 ILE B C 2615 O O . ILE B 10 ? 0.7166 0.7428 0.7831 0.0152 -0.0936 0.1169 10 ILE B O 2616 C CB . ILE B 10 ? 0.6046 0.6971 0.6926 0.0637 -0.0639 0.0846 10 ILE B CB 2617 C CG1 . ILE B 10 ? 0.5845 0.7170 0.6846 0.0813 -0.0502 0.0742 10 ILE B CG1 2618 C CG2 . ILE B 10 ? 0.6193 0.6780 0.6834 0.0772 -0.0709 0.0721 10 ILE B CG2 2619 C CD1 . ILE B 10 ? 0.5722 0.6977 0.6717 0.0912 -0.0473 0.0463 10 ILE B CD1 2620 N N . GLU B 11 ? 0.7692 0.7949 0.8139 0.0071 -0.0986 0.1484 11 GLU B N 2621 C CA . GLU B 11 ? 0.8454 0.8152 0.8622 -0.0227 -0.1209 0.1655 11 GLU B CA 2622 C C . GLU B 11 ? 0.8476 0.7464 0.8307 -0.0126 -0.1347 0.1435 11 GLU B C 2623 O O . GLU B 11 ? 0.8760 0.7394 0.8468 -0.0338 -0.1502 0.1491 11 GLU B O 2624 C CB . GLU B 11 ? 0.9521 0.8929 0.9366 -0.0371 -0.1319 0.1900 11 GLU B CB 2625 C CG . GLU B 11 ? 0.9956 0.9938 1.0035 -0.0687 -0.1287 0.2270 11 GLU B CG 2626 C CD . GLU B 11 ? 1.1168 1.0665 1.0819 -0.0954 -0.1462 0.2554 11 GLU B CD 2627 O OE1 . GLU B 11 ? 1.1704 1.0866 1.1040 -0.0724 -0.1451 0.2480 11 GLU B OE1 2628 O OE2 . GLU B 11 ? 1.1803 1.1228 1.1398 -0.1409 -0.1627 0.2857 11 GLU B OE2 2629 N N . GLY B 12 ? 0.8203 0.7020 0.7864 0.0212 -0.1299 0.1197 12 GLY B N 2630 C CA . GLY B 12 ? 0.8349 0.6567 0.7637 0.0396 -0.1414 0.0996 12 GLY B CA 2631 C C . GLY B 12 ? 0.7867 0.6366 0.7249 0.0768 -0.1272 0.0711 12 GLY B C 2632 O O . GLY B 12 ? 0.7572 0.6595 0.7220 0.0883 -0.1123 0.0660 12 GLY B O 2633 N N . GLY B 13 ? 0.7864 0.6039 0.7008 0.0949 -0.1328 0.0534 13 GLY B N 2634 C CA . GLY B 13 ? 0.7563 0.6085 0.6788 0.1278 -0.1207 0.0290 13 GLY B CA 2635 C C . GLY B 13 ? 0.7927 0.6283 0.6797 0.1600 -0.1266 0.0234 13 GLY B C 2636 O O . GLY B 13 ? 0.8481 0.6318 0.6966 0.1574 -0.1410 0.0379 13 GLY B O 2637 N N . TRP B 14 ? 0.7610 0.6432 0.6597 0.1893 -0.1162 0.0036 14 TRP B N 2638 C CA . TRP B 14 ? 0.7833 0.6675 0.6539 0.2259 -0.1201 -0.0043 14 TRP B CA 2639 C C . TRP B 14 ? 0.8540 0.7262 0.6894 0.2647 -0.1247 -0.0205 14 TRP B C 2640 O O . TRP B 14 ? 0.8109 0.7439 0.6769 0.2725 -0.1117 -0.0340 14 TRP B O 2641 C CB . TRP B 14 ? 0.7117 0.6787 0.6284 0.2298 -0.1048 -0.0127 14 TRP B CB 2642 C CG . TRP B 14 ? 0.6681 0.6492 0.6093 0.2049 -0.1000 0.0011 14 TRP B CG 2643 C CD1 . TRP B 14 ? 0.6956 0.6318 0.6163 0.1888 -0.1081 0.0221 14 TRP B CD1 2644 C CD2 . TRP B 14 ? 0.6046 0.6497 0.5892 0.1956 -0.0869 -0.0041 14 TRP B CD2 2645 N NE1 . TRP B 14 ? 0.6518 0.6286 0.6037 0.1745 -0.0980 0.0305 14 TRP B NE1 2646 C CE2 . TRP B 14 ? 0.6047 0.6418 0.5918 0.1805 -0.0861 0.0131 14 TRP B CE2 2647 C CE3 . TRP B 14 ? 0.5637 0.6694 0.5802 0.1971 -0.0775 -0.0206 14 TRP B CE3 2648 C CZ2 . TRP B 14 ? 0.5713 0.6535 0.5868 0.1740 -0.0760 0.0119 14 TRP B CZ2 2649 C CZ3 . TRP B 14 ? 0.5352 0.6768 0.5774 0.1845 -0.0706 -0.0216 14 TRP B CZ3 2650 C CH2 . TRP B 14 ? 0.5389 0.6660 0.5779 0.1767 -0.0699 -0.0067 14 TRP B CH2 2651 N N . GLN B 15 ? 0.9746 0.7669 0.7399 0.2901 -0.1439 -0.0181 15 GLN B N 2652 C CA . GLN B 15 ? 1.0464 0.8252 0.7647 0.3407 -0.1495 -0.0340 15 GLN B CA 2653 C C . GLN B 15 ? 1.0031 0.8769 0.7505 0.3746 -0.1358 -0.0480 15 GLN B C 2654 O O . GLN B 15 ? 1.0092 0.9286 0.7541 0.4087 -0.1294 -0.0617 15 GLN B O 2655 C CB . GLN B 15 ? 1.1747 0.8390 0.7989 0.3671 -0.1761 -0.0289 15 GLN B CB 2656 C CG . GLN B 15 ? 1.2493 0.8088 0.8302 0.3337 -0.1967 -0.0143 15 GLN B CG 2657 C CD . GLN B 15 ? 1.3059 0.8332 0.8576 0.3490 -0.2020 -0.0252 15 GLN B CD 2658 O OE1 . GLN B 15 ? 1.3225 0.8331 0.8935 0.3099 -0.2039 -0.0178 15 GLN B OE1 2659 N NE2 . GLN B 15 ? 1.3658 0.8868 0.8680 0.4095 -0.2046 -0.0425 15 GLN B NE2 2660 N N . GLY B 16 ? 0.9773 0.8849 0.7513 0.3648 -0.1318 -0.0432 16 GLY B N 2661 C CA . GLY B 16 ? 0.9566 0.9503 0.7544 0.3939 -0.1235 -0.0549 16 GLY B CA 2662 C C . GLY B 16 ? 0.8822 0.9848 0.7522 0.3755 -0.1046 -0.0636 16 GLY B C 2663 O O . GLY B 16 ? 0.8680 1.0511 0.7568 0.3995 -0.0996 -0.0736 16 GLY B O 2664 N N . MET B 17 ? 0.8338 0.9395 0.7412 0.3321 -0.0958 -0.0591 17 MET B N 2665 C CA . MET B 17 ? 0.7864 0.9797 0.7513 0.3102 -0.0805 -0.0660 17 MET B CA 2666 C C . MET B 17 ? 0.7888 1.0022 0.7514 0.3202 -0.0741 -0.0722 17 MET B C 2667 O O . MET B 17 ? 0.7999 0.9733 0.7617 0.2979 -0.0723 -0.0683 17 MET B O 2668 C CB . MET B 17 ? 0.7613 0.9488 0.7630 0.2615 -0.0744 -0.0585 17 MET B CB 2669 C CG . MET B 17 ? 0.7247 0.9902 0.7740 0.2378 -0.0631 -0.0655 17 MET B CG 2670 S SD . MET B 17 ? 0.7036 0.9521 0.7790 0.1935 -0.0594 -0.0587 17 MET B SD 2671 C CE . MET B 17 ? 0.7409 0.9204 0.8014 0.1792 -0.0592 -0.0497 17 MET B CE 2672 N N . VAL B 18 ? 0.7852 1.0705 0.7490 0.3544 -0.0701 -0.0812 18 VAL B N 2673 C CA . VAL B 18 ? 0.8117 1.1231 0.7615 0.3799 -0.0641 -0.0865 18 VAL B CA 2674 C C . VAL B 18 ? 0.7578 1.1614 0.7634 0.3475 -0.0475 -0.0870 18 VAL B C 2675 O O . VAL B 18 ? 0.7525 1.1652 0.7535 0.3503 -0.0397 -0.0874 18 VAL B O 2676 C CB . VAL B 18 ? 0.8638 1.2097 0.7768 0.4443 -0.0692 -0.0942 18 VAL B CB 2677 C CG1 . VAL B 18 ? 0.8945 1.3191 0.8105 0.4732 -0.0575 -0.0993 18 VAL B CG1 2678 C CG2 . VAL B 18 ? 0.9391 1.1667 0.7738 0.4803 -0.0882 -0.0937 18 VAL B CG2 2679 N N . ASP B 19 ? 0.7251 1.1913 0.7775 0.3156 -0.0438 -0.0863 19 ASP B N 2680 C CA . ASP B 19 ? 0.6887 1.2515 0.7878 0.2854 -0.0320 -0.0857 19 ASP B CA 2681 C C . ASP B 19 ? 0.6345 1.1661 0.7563 0.2284 -0.0270 -0.0808 19 ASP B C 2682 O O . ASP B 19 ? 0.6216 1.2169 0.7752 0.1947 -0.0200 -0.0786 19 ASP B O 2683 C CB . ASP B 19 ? 0.6908 1.3424 0.8206 0.2832 -0.0353 -0.0880 19 ASP B CB 2684 C CG . ASP B 19 ? 0.7294 1.3302 0.8585 0.2680 -0.0459 -0.0883 19 ASP B CG 2685 O OD1 . ASP B 19 ? 0.7188 1.2247 0.8275 0.2581 -0.0491 -0.0848 19 ASP B OD1 2686 O OD2 . ASP B 19 ? 0.7768 1.4376 0.9253 0.2666 -0.0513 -0.0911 19 ASP B OD2 2687 N N . GLY B 20 ? 0.5965 1.0319 0.6991 0.2171 -0.0317 -0.0778 20 GLY B N 2688 C CA . GLY B 20 ? 0.5719 0.9747 0.6893 0.1716 -0.0278 -0.0738 20 GLY B CA 2689 C C . GLY B 20 ? 0.5821 0.8900 0.6759 0.1687 -0.0329 -0.0690 20 GLY B C 2690 O O . GLY B 20 ? 0.6126 0.8730 0.6782 0.1947 -0.0415 -0.0673 20 GLY B O 2691 N N . TRP B 21 ? 0.5694 0.8493 0.6716 0.1357 -0.0291 -0.0658 21 TRP B N 2692 C CA . TRP B 21 ? 0.5722 0.7763 0.6578 0.1300 -0.0343 -0.0595 21 TRP B CA 2693 C C . TRP B 21 ? 0.5505 0.7308 0.6410 0.1204 -0.0400 -0.0540 21 TRP B C 2694 O O . TRP B 21 ? 0.5464 0.6788 0.6213 0.1261 -0.0474 -0.0460 21 TRP B O 2695 C CB . TRP B 21 ? 0.5878 0.7734 0.6760 0.1055 -0.0284 -0.0581 21 TRP B CB 2696 C CG . TRP B 21 ? 0.6533 0.8172 0.7194 0.1217 -0.0275 -0.0589 21 TRP B CG 2697 C CD1 . TRP B 21 ? 0.6923 0.8141 0.7268 0.1504 -0.0370 -0.0584 21 TRP B CD1 2698 C CD2 . TRP B 21 ? 0.6884 0.8625 0.7539 0.1105 -0.0185 -0.0601 21 TRP B CD2 2699 N NE1 . TRP B 21 ? 0.7250 0.8309 0.7386 0.1607 -0.0348 -0.0607 21 TRP B NE1 2700 C CE2 . TRP B 21 ? 0.7199 0.8620 0.7548 0.1370 -0.0220 -0.0613 21 TRP B CE2 2701 C CE3 . TRP B 21 ? 0.7189 0.9196 0.8001 0.0801 -0.0094 -0.0597 21 TRP B CE3 2702 C CZ2 . TRP B 21 ? 0.7656 0.9088 0.7895 0.1366 -0.0144 -0.0622 21 TRP B CZ2 2703 C CZ3 . TRP B 21 ? 0.7591 0.9602 0.8299 0.0760 -0.0015 -0.0591 21 TRP B CZ3 2704 C CH2 . TRP B 21 ? 0.7787 0.9550 0.8232 0.1055 -0.0029 -0.0604 21 TRP B CH2 2705 N N . TYR B 22 ? 0.5149 0.7291 0.6238 0.1047 -0.0376 -0.0571 22 TYR B N 2706 C CA . TYR B 22 ? 0.4925 0.6908 0.6027 0.1001 -0.0416 -0.0528 22 TYR B CA 2707 C C . TYR B 22 ? 0.4754 0.7187 0.5942 0.1061 -0.0442 -0.0588 22 TYR B C 2708 O O . TYR B 22 ? 0.4593 0.7523 0.5900 0.0998 -0.0426 -0.0660 22 TYR B O 2709 C CB . TYR B 22 ? 0.4837 0.6624 0.5961 0.0758 -0.0389 -0.0515 22 TYR B CB 2710 C CG . TYR B 22 ? 0.4786 0.6333 0.5867 0.0636 -0.0349 -0.0504 22 TYR B CG 2711 C CD1 . TYR B 22 ? 0.4875 0.6051 0.5874 0.0695 -0.0371 -0.0425 22 TYR B CD1 2712 C CD2 . TYR B 22 ? 0.4833 0.6499 0.5923 0.0431 -0.0306 -0.0561 22 TYR B CD2 2713 C CE1 . TYR B 22 ? 0.4843 0.5790 0.5782 0.0598 -0.0347 -0.0420 22 TYR B CE1 2714 C CE2 . TYR B 22 ? 0.4822 0.6236 0.5831 0.0334 -0.0268 -0.0547 22 TYR B CE2 2715 C CZ . TYR B 22 ? 0.4778 0.5840 0.5718 0.0439 -0.0286 -0.0486 22 TYR B CZ 2716 O OH . TYR B 22 ? 0.4757 0.5562 0.5599 0.0360 -0.0261 -0.0478 22 TYR B OH 2717 N N . GLY B 23 ? 0.4681 0.6987 0.5809 0.1162 -0.0488 -0.0545 23 GLY B N 2718 C CA . GLY B 23 ? 0.4741 0.7432 0.5916 0.1236 -0.0532 -0.0606 23 GLY B CA 2719 C C . GLY B 23 ? 0.4852 0.7341 0.5913 0.1368 -0.0571 -0.0541 23 GLY B C 2720 O O . GLY B 23 ? 0.4841 0.6960 0.5829 0.1331 -0.0551 -0.0434 23 GLY B O 2721 N N . TYR B 24 ? 0.4983 0.7788 0.6033 0.1530 -0.0625 -0.0593 24 TYR B N 2722 C CA . TYR B 24 ? 0.5170 0.7859 0.6094 0.1658 -0.0662 -0.0543 24 TYR B CA 2723 C C . TYR B 24 ? 0.5288 0.7967 0.6052 0.1957 -0.0712 -0.0514 24 TYR B C 2724 O O . TYR B 24 ? 0.5475 0.8446 0.6247 0.2114 -0.0739 -0.0591 24 TYR B O 2725 C CB . TYR B 24 ? 0.5304 0.8313 0.6270 0.1586 -0.0719 -0.0647 24 TYR B CB 2726 C CG . TYR B 24 ? 0.5480 0.8465 0.6497 0.1287 -0.0718 -0.0708 24 TYR B CG 2727 C CD1 . TYR B 24 ? 0.5508 0.8848 0.6680 0.1089 -0.0732 -0.0786 24 TYR B CD1 2728 C CD2 . TYR B 24 ? 0.5825 0.8429 0.6681 0.1219 -0.0710 -0.0677 24 TYR B CD2 2729 C CE1 . TYR B 24 ? 0.5818 0.9034 0.6950 0.0778 -0.0754 -0.0827 24 TYR B CE1 2730 C CE2 . TYR B 24 ? 0.6101 0.8542 0.6875 0.0978 -0.0737 -0.0740 24 TYR B CE2 2731 C CZ . TYR B 24 ? 0.6129 0.8823 0.7024 0.0731 -0.0767 -0.0813 24 TYR B CZ 2732 O OH . TYR B 24 ? 0.6504 0.8936 0.7237 0.0453 -0.0815 -0.0860 24 TYR B OH 2733 N N . HIS B 25 ? 0.5403 0.7762 0.5981 0.2056 -0.0725 -0.0394 25 HIS B N 2734 C CA . HIS B 25 ? 0.5749 0.8025 0.6082 0.2342 -0.0794 -0.0366 25 HIS B CA 2735 C C . HIS B 25 ? 0.5820 0.8179 0.6083 0.2413 -0.0811 -0.0342 25 HIS B C 2736 O O . HIS B 25 ? 0.5771 0.7943 0.6015 0.2300 -0.0759 -0.0226 25 HIS B O 2737 C CB . HIS B 25 ? 0.6010 0.7687 0.6060 0.2383 -0.0821 -0.0203 25 HIS B CB 2738 C CG . HIS B 25 ? 0.6486 0.7920 0.6158 0.2681 -0.0916 -0.0166 25 HIS B CG 2739 N ND1 . HIS B 25 ? 0.6738 0.7923 0.6198 0.2712 -0.0934 -0.0019 25 HIS B ND1 2740 C CD2 . HIS B 25 ? 0.6787 0.8182 0.6203 0.2995 -0.0998 -0.0255 25 HIS B CD2 2741 C CE1 . HIS B 25 ? 0.7175 0.8096 0.6239 0.3005 -0.1036 -0.0017 25 HIS B CE1 2742 N NE2 . HIS B 25 ? 0.7286 0.8320 0.6301 0.3207 -0.1081 -0.0168 25 HIS B NE2 2743 N N . HIS B 26 ? 0.6031 0.8711 0.6237 0.2632 -0.0884 -0.0447 26 HIS B N 2744 C CA . HIS B 26 ? 0.6203 0.8985 0.6311 0.2731 -0.0920 -0.0452 26 HIS B CA 2745 C C . HIS B 26 ? 0.6623 0.9185 0.6394 0.3042 -0.0979 -0.0379 26 HIS B C 2746 O O . HIS B 26 ? 0.6834 0.9270 0.6438 0.3231 -0.1027 -0.0387 26 HIS B O 2747 C CB . HIS B 26 ? 0.6044 0.9393 0.6340 0.2688 -0.0992 -0.0638 26 HIS B CB 2748 C CG . HIS B 26 ? 0.6156 0.9964 0.6463 0.2931 -0.1079 -0.0742 26 HIS B CG 2749 N ND1 . HIS B 26 ? 0.6175 1.0336 0.6650 0.2943 -0.1071 -0.0806 26 HIS B ND1 2750 C CD2 . HIS B 26 ? 0.6422 1.0450 0.6575 0.3211 -0.1174 -0.0790 26 HIS B CD2 2751 C CE1 . HIS B 26 ? 0.6287 1.0919 0.6721 0.3241 -0.1153 -0.0885 26 HIS B CE1 2752 N NE2 . HIS B 26 ? 0.6501 1.1048 0.6742 0.3402 -0.1225 -0.0882 26 HIS B NE2 2753 N N . SER B 27 ? 0.6864 0.9332 0.6466 0.3121 -0.0982 -0.0308 27 SER B N 2754 C CA . SER B 27 ? 0.7378 0.9541 0.6594 0.3386 -0.1033 -0.0202 27 SER B CA 2755 C C . SER B 27 ? 0.7491 0.9801 0.6589 0.3512 -0.1051 -0.0209 27 SER B C 2756 O O . SER B 27 ? 0.7380 0.9626 0.6495 0.3384 -0.0971 -0.0111 27 SER B O 2757 C CB . SER B 27 ? 0.7641 0.9214 0.6645 0.3258 -0.0983 0.0046 27 SER B CB 2758 O OG . SER B 27 ? 0.8395 0.9582 0.6956 0.3454 -0.1039 0.0185 27 SER B OG 2759 N N . ASN B 28 ? 0.7702 1.0241 0.6660 0.3796 -0.1161 -0.0330 28 ASN B N 2760 C CA . ASN B 28 ? 0.7822 1.0498 0.6622 0.3955 -0.1210 -0.0362 28 ASN B CA 2761 C C . ASN B 28 ? 0.8367 1.0987 0.6814 0.4342 -0.1319 -0.0380 28 ASN B C 2762 O O . ASN B 28 ? 0.8655 1.0959 0.6883 0.4481 -0.1342 -0.0320 28 ASN B O 2763 C CB . ASN B 28 ? 0.7433 1.0620 0.6520 0.3818 -0.1274 -0.0568 28 ASN B CB 2764 C CG . ASN B 28 ? 0.7152 1.0893 0.6499 0.3827 -0.1375 -0.0750 28 ASN B CG 2765 O OD1 . ASN B 28 ? 0.7367 1.1203 0.6603 0.4095 -0.1423 -0.0765 28 ASN B OD1 2766 N ND2 . ASN B 28 ? 0.6751 1.0866 0.6399 0.3545 -0.1415 -0.0877 28 ASN B ND2 2767 N N . GLU B 29 ? 0.8694 1.1548 0.7012 0.4540 -0.1405 -0.0465 29 GLU B N 2768 C CA . GLU B 29 ? 0.9400 1.2204 0.7342 0.4948 -0.1518 -0.0487 29 GLU B CA 2769 C C . GLU B 29 ? 0.9438 1.2742 0.7515 0.5155 -0.1631 -0.0670 29 GLU B C 2770 O O . GLU B 29 ? 0.9727 1.2862 0.7431 0.5535 -0.1710 -0.0666 29 GLU B O 2771 C CB . GLU B 29 ? 0.9883 1.2840 0.7645 0.5118 -0.1592 -0.0538 29 GLU B CB 2772 C CG . GLU B 29 ? 1.0335 1.2796 0.7791 0.5087 -0.1478 -0.0318 29 GLU B CG 2773 C CD . GLU B 29 ? 1.0744 1.3276 0.7896 0.5352 -0.1559 -0.0361 29 GLU B CD 2774 O OE1 . GLU B 29 ? 1.1168 1.3737 0.8044 0.5691 -0.1686 -0.0426 29 GLU B OE1 2775 O OE2 . GLU B 29 ? 1.0798 1.3329 0.7939 0.5258 -0.1501 -0.0334 29 GLU B OE2 2776 N N . GLN B 30 ? 0.9199 1.3125 0.7765 0.4920 -0.1642 -0.0817 30 GLN B N 2777 C CA . GLN B 30 ? 0.9126 1.3741 0.7905 0.5083 -0.1727 -0.0968 30 GLN B CA 2778 C C . GLN B 30 ? 0.8984 1.3332 0.7684 0.5173 -0.1660 -0.0915 30 GLN B C 2779 O O . GLN B 30 ? 0.9064 1.3817 0.7718 0.5500 -0.1724 -0.1003 30 GLN B O 2780 C CB . GLN B 30 ? 0.8954 1.4335 0.8266 0.4724 -0.1767 -0.1105 30 GLN B CB 2781 C CG . GLN B 30 ? 0.9307 1.4960 0.8630 0.4650 -0.1899 -0.1194 30 GLN B CG 2782 C CD . GLN B 30 ? 0.9205 1.5200 0.8897 0.4161 -0.1940 -0.1278 30 GLN B CD 2783 O OE1 . GLN B 30 ? 0.9330 1.4866 0.9062 0.3861 -0.1833 -0.1216 30 GLN B OE1 2784 N NE2 . GLN B 30 ? 0.9299 1.6095 0.9226 0.4071 -0.2116 -0.1410 30 GLN B NE2 2785 N N . GLY B 31 ? 0.8714 1.2408 0.7370 0.4908 -0.1541 -0.0771 31 GLY B N 2786 C CA . GLY B 31 ? 0.8704 1.2027 0.7225 0.4959 -0.1501 -0.0719 31 GLY B CA 2787 C C . GLY B 31 ? 0.8157 1.1182 0.6928 0.4514 -0.1376 -0.0625 31 GLY B C 2788 O O . GLY B 31 ? 0.8042 1.0927 0.6948 0.4220 -0.1309 -0.0546 31 GLY B O 2789 N N . SER B 32 ? 0.7948 1.0884 0.6743 0.4507 -0.1350 -0.0637 32 SER B N 2790 C CA . SER B 32 ? 0.7421 1.0090 0.6440 0.4110 -0.1246 -0.0557 32 SER B CA 2791 C C . SER B 32 ? 0.7194 1.0167 0.6390 0.4128 -0.1223 -0.0653 32 SER B C 2792 O O . SER B 32 ? 0.7397 1.0582 0.6397 0.4511 -0.1287 -0.0738 32 SER B O 2793 C CB . SER B 32 ? 0.7750 0.9489 0.6361 0.4036 -0.1243 -0.0346 32 SER B CB 2794 O OG . SER B 32 ? 0.8245 0.9460 0.6341 0.4350 -0.1344 -0.0330 32 SER B OG 2795 N N . GLY B 33 ? 0.6832 0.9844 0.6363 0.3751 -0.1129 -0.0636 33 GLY B N 2796 C CA . GLY B 33 ? 0.6763 1.0005 0.6433 0.3744 -0.1090 -0.0703 33 GLY B CA 2797 C C . GLY B 33 ? 0.6316 0.9580 0.6342 0.3306 -0.0988 -0.0681 33 GLY B C 2798 O O . GLY B 33 ? 0.6231 0.9344 0.6405 0.3007 -0.0947 -0.0622 33 GLY B O 2799 N N . TYR B 34 ? 0.6260 0.9717 0.6376 0.3314 -0.0948 -0.0731 34 TYR B N 2800 C CA . TYR B 34 ? 0.5958 0.9387 0.6343 0.2941 -0.0857 -0.0713 34 TYR B CA 2801 C C . TYR B 34 ? 0.5636 0.9915 0.6432 0.2753 -0.0814 -0.0813 34 TYR B C 2802 O O . TYR B 34 ? 0.5643 1.0609 0.6518 0.2966 -0.0840 -0.0888 34 TYR B O 2803 C CB . TYR B 34 ? 0.6170 0.9150 0.6312 0.3055 -0.0848 -0.0682 34 TYR B CB 2804 C CG . TYR B 34 ? 0.6677 0.8735 0.6346 0.3166 -0.0932 -0.0562 34 TYR B CG 2805 C CD1 . TYR B 34 ? 0.6595 0.8116 0.6279 0.2838 -0.0917 -0.0425 34 TYR B CD1 2806 C CD2 . TYR B 34 ? 0.7326 0.9052 0.6493 0.3593 -0.1043 -0.0571 34 TYR B CD2 2807 C CE1 . TYR B 34 ? 0.7128 0.7859 0.6388 0.2858 -0.1013 -0.0278 34 TYR B CE1 2808 C CE2 . TYR B 34 ? 0.7890 0.8670 0.6542 0.3631 -0.1154 -0.0439 34 TYR B CE2 2809 C CZ . TYR B 34 ? 0.7848 0.8161 0.6573 0.3226 -0.1141 -0.0282 34 TYR B CZ 2810 O OH . TYR B 34 ? 0.8624 0.8053 0.6847 0.3186 -0.1269 -0.0117 34 TYR B OH 2811 N N . ALA B 35 ? 0.5521 0.9760 0.6547 0.2346 -0.0759 -0.0799 35 ALA B N 2812 C CA . ALA B 35 ? 0.5349 1.0249 0.6693 0.2076 -0.0731 -0.0861 35 ALA B CA 2813 C C . ALA B 35 ? 0.5308 0.9841 0.6718 0.1734 -0.0653 -0.0821 35 ALA B C 2814 O O . ALA B 35 ? 0.5143 0.9118 0.6473 0.1571 -0.0648 -0.0774 35 ALA B O 2815 C CB . ALA B 35 ? 0.5259 1.0560 0.6744 0.1901 -0.0816 -0.0914 35 ALA B CB 2816 N N . ALA B 36 ? 0.5387 1.0276 0.6920 0.1664 -0.0588 -0.0833 36 ALA B N 2817 C CA . ALA B 36 ? 0.5479 1.0044 0.7041 0.1374 -0.0515 -0.0798 36 ALA B CA 2818 C C . ALA B 36 ? 0.5636 1.0281 0.7317 0.0944 -0.0543 -0.0814 36 ALA B C 2819 O O . ALA B 36 ? 0.5824 1.1074 0.7655 0.0798 -0.0602 -0.0851 36 ALA B O 2820 C CB . ALA B 36 ? 0.5532 1.0492 0.7145 0.1459 -0.0434 -0.0799 36 ALA B CB 2821 N N . ASP B 37 ? 0.5907 0.9915 0.7470 0.0748 -0.0523 -0.0783 37 ASP B N 2822 C CA . ASP B 37 ? 0.6178 1.0074 0.7711 0.0359 -0.0560 -0.0801 37 ASP B CA 2823 C C . ASP B 37 ? 0.6485 1.0649 0.8109 0.0119 -0.0492 -0.0779 37 ASP B C 2824 O O . ASP B 37 ? 0.6137 0.9949 0.7692 0.0139 -0.0409 -0.0743 37 ASP B O 2825 C CB . ASP B 37 ? 0.6390 0.9522 0.7701 0.0331 -0.0562 -0.0774 37 ASP B CB 2826 C CG . ASP B 37 ? 0.6820 0.9677 0.7937 0.0018 -0.0642 -0.0813 37 ASP B CG 2827 O OD1 . ASP B 37 ? 0.7063 0.9985 0.8091 -0.0025 -0.0755 -0.0863 37 ASP B OD1 2828 O OD2 . ASP B 37 ? 0.6893 0.9402 0.7884 -0.0171 -0.0612 -0.0795 37 ASP B OD2 2829 N N . LYS B 38 ? 0.6932 1.1765 0.8710 -0.0124 -0.0535 -0.0787 38 LYS B N 2830 C CA . LYS B 38 ? 0.7207 1.2525 0.9114 -0.0357 -0.0459 -0.0735 38 LYS B CA 2831 C C . LYS B 38 ? 0.7287 1.1969 0.8976 -0.0703 -0.0445 -0.0702 38 LYS B C 2832 O O . LYS B 38 ? 0.7304 1.1928 0.8982 -0.0692 -0.0332 -0.0657 38 LYS B O 2833 C CB . LYS B 38 ? 0.7741 1.3985 0.9871 -0.0623 -0.0537 -0.0718 38 LYS B CB 2834 C CG . LYS B 38 ? 0.8277 1.5355 1.0623 -0.0794 -0.0434 -0.0627 38 LYS B CG 2835 C CD . LYS B 38 ? 0.8840 1.6407 1.1266 -0.1403 -0.0544 -0.0557 38 LYS B CD 2836 C CE . LYS B 38 ? 0.9083 1.7327 1.1690 -0.1461 -0.0704 -0.0586 38 LYS B CE 2837 N NZ . LYS B 38 ? 0.9072 1.8641 1.2069 -0.1199 -0.0627 -0.0540 38 LYS B NZ 2838 N N . GLU B 39 ? 0.7572 1.1727 0.9021 -0.0969 -0.0572 -0.0731 39 GLU B N 2839 C CA . GLU B 39 ? 0.8019 1.1485 0.9145 -0.1287 -0.0597 -0.0710 39 GLU B CA 2840 C C . GLU B 39 ? 0.7504 1.0352 0.8500 -0.1052 -0.0487 -0.0699 39 GLU B C 2841 O O . GLU B 39 ? 0.7599 1.0298 0.8510 -0.1208 -0.0418 -0.0652 39 GLU B O 2842 C CB . GLU B 39 ? 0.9011 1.1867 0.9770 -0.1463 -0.0780 -0.0768 39 GLU B CB 2843 C CG . GLU B 39 ? 1.0221 1.2227 1.0500 -0.1748 -0.0844 -0.0760 39 GLU B CG 2844 C CD . GLU B 39 ? 1.1264 1.2498 1.1045 -0.1759 -0.1027 -0.0838 39 GLU B CD 2845 O OE1 . GLU B 39 ? 1.1589 1.3045 1.1401 -0.1728 -0.1144 -0.0889 39 GLU B OE1 2846 O OE2 . GLU B 39 ? 1.2033 1.2421 1.1344 -0.1760 -0.1062 -0.0854 39 GLU B OE2 2847 N N . SER B 40 ? 0.6730 0.9242 0.7700 -0.0703 -0.0482 -0.0727 40 SER B N 2848 C CA . SER B 40 ? 0.6325 0.8314 0.7191 -0.0512 -0.0409 -0.0700 40 SER B CA 2849 C C . SER B 40 ? 0.6008 0.8281 0.7067 -0.0343 -0.0296 -0.0662 40 SER B C 2850 O O . SER B 40 ? 0.5881 0.7798 0.6835 -0.0332 -0.0244 -0.0634 40 SER B O 2851 C CB . SER B 40 ? 0.6087 0.7746 0.6886 -0.0236 -0.0440 -0.0702 40 SER B CB 2852 O OG . SER B 40 ? 0.5898 0.7925 0.6919 0.0019 -0.0422 -0.0690 40 SER B OG 2853 N N . THR B 41 ? 0.5585 0.8467 0.6866 -0.0177 -0.0274 -0.0670 41 THR B N 2854 C CA . THR B 41 ? 0.5342 0.8489 0.6702 0.0035 -0.0186 -0.0649 41 THR B CA 2855 C C . THR B 41 ? 0.5455 0.8827 0.6808 -0.0201 -0.0104 -0.0613 41 THR B C 2856 O O . THR B 41 ? 0.5351 0.8491 0.6604 -0.0093 -0.0037 -0.0593 41 THR B O 2857 C CB . THR B 41 ? 0.5272 0.9073 0.6794 0.0307 -0.0190 -0.0672 41 THR B CB 2858 O OG1 . THR B 41 ? 0.5248 0.8736 0.6707 0.0568 -0.0256 -0.0686 41 THR B OG1 2859 C CG2 . THR B 41 ? 0.5300 0.9404 0.6805 0.0567 -0.0103 -0.0661 41 THR B CG2 2860 N N . GLN B 42 ? 0.5647 0.9468 0.7080 -0.0542 -0.0122 -0.0594 42 GLN B N 2861 C CA . GLN B 42 ? 0.5951 1.0075 0.7376 -0.0838 -0.0044 -0.0523 42 GLN B CA 2862 C C . GLN B 42 ? 0.6278 0.9578 0.7394 -0.1052 -0.0046 -0.0504 42 GLN B C 2863 O O . GLN B 42 ? 0.6166 0.9480 0.7204 -0.1133 0.0048 -0.0448 42 GLN B O 2864 C CB . GLN B 42 ? 0.6202 1.1007 0.7770 -0.1239 -0.0102 -0.0476 42 GLN B CB 2865 C CG . GLN B 42 ? 0.6515 1.1860 0.8128 -0.1575 -0.0009 -0.0357 42 GLN B CG 2866 C CD . GLN B 42 ? 0.6489 1.2503 0.8273 -0.1203 0.0162 -0.0321 42 GLN B CD 2867 O OE1 . GLN B 42 ? 0.6603 1.2417 0.8242 -0.1192 0.0271 -0.0273 42 GLN B OE1 2868 N NE2 . GLN B 42 ? 0.6300 1.3064 0.8327 -0.0850 0.0175 -0.0352 42 GLN B NE2 2869 N N . LYS B 43 ? 0.6564 0.9168 0.7468 -0.1105 -0.0154 -0.0551 43 LYS B N 2870 C CA . LYS B 43 ? 0.7129 0.8898 0.7691 -0.1181 -0.0170 -0.0549 43 LYS B CA 2871 C C . LYS B 43 ? 0.6601 0.8161 0.7179 -0.0875 -0.0082 -0.0541 43 LYS B C 2872 O O . LYS B 43 ? 0.6754 0.7973 0.7133 -0.0960 -0.0038 -0.0511 43 LYS B O 2873 C CB . LYS B 43 ? 0.7845 0.9019 0.8189 -0.1113 -0.0289 -0.0606 43 LYS B CB 2874 C CG . LYS B 43 ? 0.8997 0.9463 0.8864 -0.1384 -0.0385 -0.0613 43 LYS B CG 2875 C CD . LYS B 43 ? 0.9915 1.0547 0.9660 -0.1813 -0.0496 -0.0602 43 LYS B CD 2876 C CE . LYS B 43 ? 1.0948 1.0745 1.0135 -0.1932 -0.0677 -0.0659 43 LYS B CE 2877 N NZ . LYS B 43 ? 1.0998 1.0780 1.0221 -0.1648 -0.0750 -0.0735 43 LYS B NZ 2878 N N . ALA B 44 ? 0.5881 0.7588 0.6643 -0.0535 -0.0078 -0.0563 44 ALA B N 2879 C CA . ALA B 44 ? 0.5783 0.7215 0.6505 -0.0274 -0.0047 -0.0553 44 ALA B CA 2880 C C . ALA B 44 ? 0.5855 0.7609 0.6578 -0.0225 0.0053 -0.0531 44 ALA B C 2881 O O . ALA B 44 ? 0.6020 0.7410 0.6573 -0.0184 0.0080 -0.0516 44 ALA B O 2882 C CB . ALA B 44 ? 0.5578 0.7019 0.6413 0.0023 -0.0099 -0.0563 44 ALA B CB 2883 N N . ILE B 45 ? 0.5688 0.8169 0.6588 -0.0205 0.0106 -0.0526 45 ILE B N 2884 C CA . ILE B 45 ? 0.5765 0.8705 0.6660 -0.0119 0.0222 -0.0491 45 ILE B CA 2885 C C . ILE B 45 ? 0.6004 0.8797 0.6744 -0.0448 0.0290 -0.0427 45 ILE B C 2886 O O . ILE B 45 ? 0.6477 0.9143 0.7059 -0.0322 0.0363 -0.0407 45 ILE B O 2887 C CB . ILE B 45 ? 0.5726 0.9656 0.6868 -0.0057 0.0272 -0.0475 45 ILE B CB 2888 C CG1 . ILE B 45 ? 0.5586 0.9581 0.6755 0.0396 0.0216 -0.0540 45 ILE B CG1 2889 C CG2 . ILE B 45 ? 0.5754 1.0327 0.6899 -0.0035 0.0419 -0.0403 45 ILE B CG2 2890 C CD1 . ILE B 45 ? 0.5577 1.0491 0.6992 0.0477 0.0223 -0.0542 45 ILE B CD1 2891 N N . ASP B 46 ? 0.6094 0.8825 0.6807 -0.0864 0.0248 -0.0394 46 ASP B N 2892 C CA . ASP B 46 ? 0.6449 0.8943 0.6925 -0.1225 0.0290 -0.0318 46 ASP B CA 2893 C C . ASP B 46 ? 0.6511 0.8099 0.6670 -0.1128 0.0267 -0.0347 46 ASP B C 2894 O O . ASP B 46 ? 0.6815 0.8263 0.6780 -0.1189 0.0345 -0.0295 46 ASP B O 2895 C CB . ASP B 46 ? 0.6778 0.9207 0.7162 -0.1706 0.0192 -0.0283 46 ASP B CB 2896 C CG . ASP B 46 ? 0.6829 1.0249 0.7537 -0.1890 0.0196 -0.0230 46 ASP B CG 2897 O OD1 . ASP B 46 ? 0.6580 1.0820 0.7573 -0.1630 0.0308 -0.0208 46 ASP B OD1 2898 O OD2 . ASP B 46 ? 0.7120 1.0489 0.7758 -0.2273 0.0070 -0.0214 46 ASP B OD2 2899 N N . GLY B 47 ? 0.6313 0.7352 0.6421 -0.0969 0.0161 -0.0417 47 GLY B N 2900 C CA . GLY B 47 ? 0.6476 0.6765 0.6319 -0.0864 0.0121 -0.0436 47 GLY B CA 2901 C C . GLY B 47 ? 0.6381 0.6637 0.6227 -0.0573 0.0168 -0.0439 47 GLY B C 2902 O O . GLY B 47 ? 0.6630 0.6485 0.6229 -0.0579 0.0186 -0.0422 47 GLY B O 2903 N N . VAL B 48 ? 0.6163 0.6777 0.6220 -0.0308 0.0168 -0.0464 48 VAL B N 2904 C CA . VAL B 48 ? 0.6124 0.6595 0.6086 -0.0005 0.0166 -0.0479 48 VAL B CA 2905 C C . VAL B 48 ? 0.6323 0.7130 0.6170 0.0016 0.0298 -0.0446 48 VAL B C 2906 O O . VAL B 48 ? 0.6663 0.7129 0.6272 0.0152 0.0303 -0.0449 48 VAL B O 2907 C CB . VAL B 48 ? 0.6014 0.6646 0.6108 0.0282 0.0098 -0.0513 48 VAL B CB 2908 C CG1 . VAL B 48 ? 0.6310 0.6692 0.6174 0.0594 0.0060 -0.0534 48 VAL B CG1 2909 C CG2 . VAL B 48 ? 0.5870 0.6179 0.6058 0.0259 -0.0022 -0.0514 48 VAL B CG2 2910 N N . THR B 49 ? 0.6268 0.7791 0.6278 -0.0125 0.0402 -0.0402 49 THR B N 2911 C CA . THR B 49 ? 0.6464 0.8484 0.6397 -0.0125 0.0554 -0.0334 49 THR B CA 2912 C C . THR B 49 ? 0.6836 0.8439 0.6505 -0.0413 0.0601 -0.0270 49 THR B C 2913 O O . THR B 49 ? 0.7121 0.8653 0.6568 -0.0266 0.0680 -0.0245 49 THR B O 2914 C CB . THR B 49 ? 0.6344 0.9366 0.6564 -0.0287 0.0647 -0.0265 49 THR B CB 2915 O OG1 . THR B 49 ? 0.6020 0.9419 0.6429 0.0050 0.0604 -0.0331 49 THR B OG1 2916 C CG2 . THR B 49 ? 0.6513 1.0207 0.6680 -0.0292 0.0826 -0.0157 49 THR B CG2 2917 N N . ASN B 50 ? 0.7079 0.8341 0.6697 -0.0791 0.0540 -0.0247 50 ASN B N 2918 C CA . ASN B 50 ? 0.7535 0.8232 0.6797 -0.1050 0.0551 -0.0193 50 ASN B CA 2919 C C . ASN B 50 ? 0.7642 0.7620 0.6653 -0.0769 0.0495 -0.0255 50 ASN B C 2920 O O . ASN B 50 ? 0.7823 0.7538 0.6542 -0.0793 0.0554 -0.0212 50 ASN B O 2921 C CB . ASN B 50 ? 0.7759 0.8018 0.6884 -0.1417 0.0441 -0.0187 50 ASN B CB 2922 C CG . ASN B 50 ? 0.7970 0.8833 0.7223 -0.1832 0.0468 -0.0094 50 ASN B CG 2923 O OD1 . ASN B 50 ? 0.8027 0.9706 0.7469 -0.1899 0.0598 -0.0001 50 ASN B OD1 2924 N ND2 . ASN B 50 ? 0.8191 0.8680 0.7314 -0.2106 0.0331 -0.0114 50 ASN B ND2 2925 N N . LYS B 51 ? 0.7612 0.7306 0.6737 -0.0527 0.0372 -0.0342 51 LYS B N 2926 C CA . LYS B 51 ? 0.7668 0.6764 0.6615 -0.0293 0.0277 -0.0389 51 LYS B CA 2927 C C . LYS B 51 ? 0.7749 0.6904 0.6551 -0.0031 0.0328 -0.0395 51 LYS B C 2928 O O . LYS B 51 ? 0.8024 0.6741 0.6532 0.0024 0.0314 -0.0392 51 LYS B O 2929 C CB . LYS B 51 ? 0.7550 0.6555 0.6715 -0.0128 0.0143 -0.0441 51 LYS B CB 2930 C CG . LYS B 51 ? 0.7788 0.6290 0.6834 0.0060 0.0011 -0.0463 51 LYS B CG 2931 C CD . LYS B 51 ? 0.7864 0.6441 0.7141 0.0203 -0.0105 -0.0476 51 LYS B CD 2932 C CE . LYS B 51 ? 0.8029 0.6250 0.7306 0.0215 -0.0246 -0.0452 51 LYS B CE 2933 N NZ . LYS B 51 ? 0.7889 0.6177 0.7283 0.0102 -0.0242 -0.0437 51 LYS B NZ 2934 N N . VAL B 52 ? 0.7443 0.7114 0.6398 0.0174 0.0374 -0.0409 52 VAL B N 2935 C CA . VAL B 52 ? 0.7586 0.7281 0.6314 0.0504 0.0407 -0.0428 52 VAL B CA 2936 C C . VAL B 52 ? 0.7792 0.7651 0.6296 0.0396 0.0573 -0.0350 52 VAL B C 2937 O O . VAL B 52 ? 0.8037 0.7488 0.6205 0.0572 0.0560 -0.0365 52 VAL B O 2938 C CB . VAL B 52 ? 0.7482 0.7730 0.6342 0.0794 0.0431 -0.0458 52 VAL B CB 2939 C CG1 . VAL B 52 ? 0.7949 0.8227 0.6460 0.1200 0.0476 -0.0481 52 VAL B CG1 2940 C CG2 . VAL B 52 ? 0.7277 0.7209 0.6254 0.0905 0.0248 -0.0521 52 VAL B CG2 2941 N N . ASN B 53 ? 0.7710 0.8136 0.6374 0.0074 0.0712 -0.0254 53 ASN B N 2942 C CA . ASN B 53 ? 0.8177 0.8809 0.6630 -0.0116 0.0875 -0.0136 53 ASN B CA 2943 C C . ASN B 53 ? 0.8494 0.8277 0.6600 -0.0303 0.0814 -0.0128 53 ASN B C 2944 O O . ASN B 53 ? 0.8786 0.8413 0.6570 -0.0259 0.0898 -0.0077 53 ASN B O 2945 C CB . ASN B 53 ? 0.8188 0.9619 0.6888 -0.0520 0.0999 -0.0005 53 ASN B CB 2946 C CG . ASN B 53 ? 0.7998 1.0405 0.7047 -0.0311 0.1068 -0.0002 53 ASN B CG 2947 O OD1 . ASN B 53 ? 0.8165 1.0757 0.7148 0.0175 0.1094 -0.0063 53 ASN B OD1 2948 N ND2 . ASN B 53 ? 0.7922 1.0915 0.7287 -0.0658 0.1077 0.0064 53 ASN B ND2 2949 N N . SER B 54 ? 0.8633 0.7880 0.6768 -0.0467 0.0668 -0.0179 54 SER B N 2950 C CA . SER B 54 ? 0.9099 0.7523 0.6871 -0.0558 0.0585 -0.0188 54 SER B CA 2951 C C . SER B 54 ? 0.9414 0.7394 0.6981 -0.0197 0.0506 -0.0260 54 SER B C 2952 O O . SER B 54 ? 0.9641 0.7172 0.6833 -0.0197 0.0515 -0.0236 54 SER B O 2953 C CB . SER B 54 ? 0.9005 0.7017 0.6834 -0.0687 0.0436 -0.0239 54 SER B CB 2954 O OG . SER B 54 ? 0.9173 0.7252 0.6937 -0.1084 0.0468 -0.0167 54 SER B OG 2955 N N . ILE B 55 ? 0.9566 0.7625 0.7336 0.0092 0.0405 -0.0342 55 ILE B N 2956 C CA . ILE B 55 ? 1.0028 0.7634 0.7579 0.0400 0.0278 -0.0408 55 ILE B CA 2957 C C . ILE B 55 ? 1.0629 0.8337 0.7861 0.0589 0.0400 -0.0385 55 ILE B C 2958 O O . ILE B 55 ? 1.1309 0.8535 0.8181 0.0668 0.0364 -0.0391 55 ILE B O 2959 C CB . ILE B 55 ? 0.9991 0.7618 0.7755 0.0614 0.0122 -0.0478 55 ILE B CB 2960 C CG1 . ILE B 55 ? 0.9841 0.7284 0.7849 0.0467 -0.0016 -0.0485 55 ILE B CG1 2961 C CG2 . ILE B 55 ? 1.0483 0.7658 0.7927 0.0915 -0.0024 -0.0535 55 ILE B CG2 2962 C CD1 . ILE B 55 ? 0.9694 0.7190 0.7924 0.0595 -0.0161 -0.0515 55 ILE B CD1 2963 N N . ILE B 56 ? 1.0634 0.9010 0.7981 0.0692 0.0546 -0.0354 56 ILE B N 2964 C CA . ILE B 56 ? 1.0952 0.9570 0.7991 0.0932 0.0691 -0.0317 56 ILE B CA 2965 C C . ILE B 56 ? 1.1547 1.0062 0.8336 0.0670 0.0829 -0.0207 56 ILE B C 2966 O O . ILE B 56 ? 1.1977 1.0152 0.8354 0.0863 0.0846 -0.0208 56 ILE B O 2967 C CB . ILE B 56 ? 1.0815 1.0384 0.8070 0.1059 0.0861 -0.0269 56 ILE B CB 2968 C CG1 . ILE B 56 ? 1.0638 1.0190 0.7988 0.1406 0.0714 -0.0384 56 ILE B CG1 2969 C CG2 . ILE B 56 ? 1.1157 1.1133 0.8092 0.1299 0.1057 -0.0194 56 ILE B CG2 2970 C CD1 . ILE B 56 ? 1.0429 1.0934 0.8076 0.1500 0.0847 -0.0347 56 ILE B CD1 2971 N N . ASP B 57 ? 1.1739 1.0467 0.8710 0.0225 0.0906 -0.0110 57 ASP B N 2972 C CA . ASP B 57 ? 1.2414 1.1039 0.9094 -0.0096 0.1034 0.0026 57 ASP B CA 2973 C C . ASP B 57 ? 1.2634 1.0291 0.8887 -0.0067 0.0909 -0.0021 57 ASP B C 2974 O O . ASP B 57 ? 1.2930 1.0393 0.8784 -0.0079 0.1005 0.0056 57 ASP B O 2975 C CB . ASP B 57 ? 1.2549 1.1452 0.9434 -0.0614 0.1077 0.0132 57 ASP B CB 2976 C CG . ASP B 57 ? 1.3495 1.2266 1.0012 -0.1013 0.1194 0.0304 57 ASP B CG 2977 O OD1 . ASP B 57 ? 1.4195 1.3440 1.0570 -0.0968 0.1381 0.0427 57 ASP B OD1 2978 O OD2 . ASP B 57 ? 1.3830 1.1993 1.0142 -0.1358 0.1094 0.0325 57 ASP B OD2 2979 N N . LYS B 58 ? 1.2545 0.9656 0.8877 -0.0017 0.0699 -0.0136 58 LYS B N 2980 C CA . LYS B 58 ? 1.2899 0.9187 0.8863 0.0056 0.0557 -0.0185 58 LYS B CA 2981 C C . LYS B 58 ? 1.3489 0.9521 0.9161 0.0426 0.0511 -0.0242 58 LYS B C 2982 O O . LYS B 58 ? 1.3651 0.9154 0.8896 0.0465 0.0485 -0.0231 58 LYS B O 2983 C CB . LYS B 58 ? 1.2716 0.8682 0.8894 0.0074 0.0348 -0.0278 58 LYS B CB 2984 C CG . LYS B 58 ? 1.3056 0.8591 0.9043 -0.0181 0.0307 -0.0248 58 LYS B CG 2985 C CD . LYS B 58 ? 1.3527 0.9101 0.9250 -0.0546 0.0469 -0.0118 58 LYS B CD 2986 C CE . LYS B 58 ? 1.3832 0.8861 0.9282 -0.0788 0.0380 -0.0105 58 LYS B CE 2987 N NZ . LYS B 58 ? 1.4470 0.9300 0.9483 -0.1183 0.0489 0.0040 58 LYS B NZ 2988 N N . MET B 59 ? 1.3624 0.9970 0.9453 0.0711 0.0485 -0.0304 59 MET B N 2989 C CA . MET B 59 ? 1.4282 1.0324 0.9750 0.1089 0.0410 -0.0370 59 MET B CA 2990 C C . MET B 59 ? 1.5000 1.1423 1.0171 0.1217 0.0651 -0.0283 59 MET B C 2991 O O . MET B 59 ? 1.5291 1.1556 1.0119 0.1599 0.0617 -0.0340 59 MET B O 2992 C CB . MET B 59 ? 1.4192 1.0247 0.9826 0.1356 0.0233 -0.0478 59 MET B CB 2993 C CG . MET B 59 ? 1.3891 0.9719 0.9861 0.1218 0.0012 -0.0529 59 MET B CG 2994 S SD . MET B 59 ? 1.4535 0.9604 1.0275 0.1242 -0.0265 -0.0580 59 MET B SD 2995 C CE . MET B 59 ? 1.5205 0.9813 1.0455 0.1621 -0.0446 -0.0665 59 MET B CE 2996 N N . ASN B 60 ? 1.5551 1.2477 1.0817 0.0894 0.0882 -0.0134 60 ASN B N 2997 C CA . ASN B 60 ? 1.6146 1.3613 1.1183 0.0943 0.1143 0.0003 60 ASN B CA 2998 C C . ASN B 60 ? 1.6600 1.3470 1.1048 0.1062 0.1156 0.0027 60 ASN B C 2999 O O . ASN B 60 ? 1.6652 1.3556 1.0762 0.1463 0.1205 0.0004 60 ASN B O 3000 C CB . ASN B 60 ? 1.6206 1.4332 1.1499 0.0442 0.1346 0.0191 60 ASN B CB 3001 C CG . ASN B 60 ? 1.6693 1.5478 1.1772 0.0400 0.1627 0.0387 60 ASN B CG 3002 O OD1 . ASN B 60 ? 1.6949 1.5651 1.1817 -0.0013 0.1734 0.0555 60 ASN B OD1 3003 N ND2 . ASN B 60 ? 1.6802 1.6236 1.1884 0.0840 0.1744 0.0379 60 ASN B ND2 3004 N N . THR B 61 ? 1.2880 1.9299 1.2128 -0.0937 -0.2525 -0.2813 61 THR B N 3005 C CA . THR B 61 ? 1.2748 1.8270 1.2148 -0.0975 -0.2328 -0.2799 61 THR B CA 3006 C C . THR B 61 ? 1.2426 1.7457 1.1646 -0.0571 -0.2125 -0.2604 61 THR B C 3007 O O . THR B 61 ? 1.2709 1.7709 1.1546 -0.0484 -0.2097 -0.2772 61 THR B O 3008 C CB . THR B 61 ? 1.3553 1.8244 1.2707 -0.1349 -0.2416 -0.3229 61 THR B CB 3009 O OG1 . THR B 61 ? 1.3907 1.9058 1.3043 -0.1867 -0.2666 -0.3428 61 THR B OG1 3010 C CG2 . THR B 61 ? 1.3684 1.7449 1.2961 -0.1456 -0.2314 -0.3120 61 THR B CG2 3011 N N . GLN B 62 ? 1.1709 1.6509 1.1182 -0.0376 -0.1986 -0.2278 62 GLN B N 3012 C CA . GLN B 62 ? 1.1692 1.6063 1.0967 -0.0093 -0.1827 -0.2031 62 GLN B CA 3013 C C . GLN B 62 ? 1.1196 1.5157 1.0779 0.0031 -0.1683 -0.1801 62 GLN B C 3014 O O . GLN B 62 ? 1.1120 1.5438 1.1066 -0.0002 -0.1723 -0.1763 62 GLN B O 3015 C CB . GLN B 62 ? 1.1816 1.6566 1.0734 0.0077 -0.1982 -0.1737 62 GLN B CB 3016 C CG . GLN B 62 ? 1.1819 1.6050 1.0449 0.0251 -0.1923 -0.1340 62 GLN B CG 3017 C CD . GLN B 62 ? 1.2459 1.6797 1.0469 0.0261 -0.2175 -0.0999 62 GLN B CD 3018 O OE1 . GLN B 62 ? 1.3006 1.7923 1.0779 0.0134 -0.2333 -0.1091 62 GLN B OE1 3019 N NE2 . GLN B 62 ? 1.2674 1.6352 1.0311 0.0358 -0.2266 -0.0580 62 GLN B NE2 3020 N N . PHE B 63 ? 1.0776 1.4177 1.0208 0.0144 -0.1512 -0.1684 63 PHE B N 3021 C CA . PHE B 63 ? 1.0576 1.3541 1.0228 0.0234 -0.1368 -0.1505 63 PHE B CA 3022 C C . PHE B 63 ? 1.0522 1.3733 1.0335 0.0481 -0.1457 -0.1277 63 PHE B C 3023 O O . PHE B 63 ? 1.1100 1.4310 1.0622 0.0715 -0.1633 -0.1079 63 PHE B O 3024 C CB . PHE B 63 ? 1.0314 1.2821 0.9712 0.0307 -0.1215 -0.1390 63 PHE B CB 3025 C CG . PHE B 63 ? 0.9983 1.2027 0.9565 0.0362 -0.1073 -0.1251 63 PHE B CG 3026 C CD1 . PHE B 63 ? 0.9699 1.1432 0.9491 0.0242 -0.1002 -0.1407 63 PHE B CD1 3027 C CD2 . PHE B 63 ? 1.0164 1.1957 0.9602 0.0513 -0.1072 -0.0961 63 PHE B CD2 3028 C CE1 . PHE B 63 ? 0.9540 1.0920 0.9450 0.0253 -0.0884 -0.1258 63 PHE B CE1 3029 C CE2 . PHE B 63 ? 0.9807 1.1230 0.9382 0.0554 -0.0943 -0.0879 63 PHE B CE2 3030 C CZ . PHE B 63 ? 0.9465 1.0782 0.9304 0.0414 -0.0824 -0.1019 63 PHE B CZ 3031 N N . GLU B 64 ? 1.0084 1.3499 1.0290 0.0439 -0.1380 -0.1326 64 GLU B N 3032 C CA . GLU B 64 ? 1.0060 1.3860 1.0476 0.0793 -0.1443 -0.1250 64 GLU B CA 3033 C C . GLU B 64 ? 0.9954 1.3224 1.0396 0.0848 -0.1247 -0.1162 64 GLU B C 3034 O O . GLU B 64 ? 0.9699 1.2826 1.0272 0.0503 -0.1068 -0.1204 64 GLU B O 3035 C CB . GLU B 64 ? 1.0050 1.5016 1.0936 0.0662 -0.1494 -0.1449 64 GLU B CB 3036 C CG . GLU B 64 ? 1.0461 1.6123 1.1351 0.0616 -0.1727 -0.1555 64 GLU B CG 3037 C CD . GLU B 64 ? 1.0482 1.7575 1.1868 0.0418 -0.1784 -0.1761 64 GLU B CD 3038 O OE1 . GLU B 64 ? 1.0380 1.8057 1.2102 0.0358 -0.1635 -0.1821 64 GLU B OE1 3039 O OE2 . GLU B 64 ? 1.0246 1.8037 1.1669 0.0266 -0.1973 -0.1875 64 GLU B OE2 3040 N N . ALA B 65 ? 1.0329 1.3183 1.0549 0.1264 -0.1342 -0.1030 65 ALA B N 3041 C CA . ALA B 65 ? 1.0341 1.2678 1.0519 0.1327 -0.1185 -0.0973 65 ALA B CA 3042 C C . ALA B 65 ? 1.0071 1.3237 1.0689 0.1482 -0.1109 -0.1182 65 ALA B C 3043 O O . ALA B 65 ? 0.9795 1.3897 1.0686 0.1776 -0.1263 -0.1369 65 ALA B O 3044 C CB . ALA B 65 ? 1.0856 1.2258 1.0478 0.1621 -0.1377 -0.0767 65 ALA B CB 3045 N N . VAL B 66 ? 0.9892 1.2890 1.0573 0.1274 -0.0878 -0.1171 66 VAL B N 3046 C CA . VAL B 66 ? 0.9786 1.3721 1.0812 0.1322 -0.0755 -0.1372 66 VAL B CA 3047 C C . VAL B 66 ? 0.9703 1.3013 1.0504 0.1541 -0.0672 -0.1361 66 VAL B C 3048 O O . VAL B 66 ? 0.9808 1.2118 1.0298 0.1324 -0.0600 -0.1142 66 VAL B O 3049 C CB . VAL B 66 ? 0.9727 1.4254 1.0980 0.0601 -0.0566 -0.1344 66 VAL B CB 3050 C CG1 . VAL B 66 ? 0.9646 1.5476 1.1207 0.0514 -0.0417 -0.1535 66 VAL B CG1 3051 C CG2 . VAL B 66 ? 0.9822 1.4753 1.1183 0.0283 -0.0689 -0.1369 66 VAL B CG2 3052 N N . GLY B 67 ? 0.9491 1.3525 1.0454 0.1992 -0.0696 -0.1655 67 GLY B N 3053 C CA . GLY B 67 ? 0.9433 1.2941 1.0146 0.2241 -0.0648 -0.1743 67 GLY B CA 3054 C C . GLY B 67 ? 0.8770 1.2542 0.9559 0.1644 -0.0323 -0.1644 67 GLY B C 3055 O O . GLY B 67 ? 0.8423 1.3451 0.9548 0.1283 -0.0152 -0.1739 67 GLY B O 3056 N N . ARG B 68 ? 0.8563 1.1196 0.8982 0.1470 -0.0273 -0.1422 68 ARG B N 3057 C CA . ARG B 68 ? 0.8162 1.0873 0.8544 0.0993 -0.0044 -0.1304 68 ARG B CA 3058 C C . ARG B 68 ? 0.8277 1.0302 0.8300 0.1256 -0.0059 -0.1380 68 ARG B C 3059 O O . ARG B 68 ? 0.8843 0.9763 0.8503 0.1417 -0.0224 -0.1264 68 ARG B O 3060 C CB . ARG B 68 ? 0.7884 0.9906 0.8169 0.0471 -0.0017 -0.0951 68 ARG B CB 3061 C CG . ARG B 68 ? 0.7655 1.0165 0.8162 0.0074 -0.0036 -0.0889 68 ARG B CG 3062 C CD . ARG B 68 ? 0.7619 0.9241 0.7943 -0.0265 -0.0110 -0.0649 68 ARG B CD 3063 N NE . ARG B 68 ? 0.7737 0.9460 0.8162 -0.0430 -0.0235 -0.0681 68 ARG B NE 3064 C CZ . ARG B 68 ? 0.7829 0.9384 0.8276 -0.0141 -0.0333 -0.0763 68 ARG B CZ 3065 N NH1 . ARG B 68 ? 0.7536 0.8729 0.7847 0.0253 -0.0345 -0.0757 68 ARG B NH1 3066 N NH2 . ARG B 68 ? 0.8546 1.0269 0.9058 -0.0338 -0.0451 -0.0829 68 ARG B NH2 3067 N N . GLU B 69 ? 0.8145 1.0876 0.8202 0.1206 0.0101 -0.1571 69 GLU B N 3068 C CA . GLU B 69 ? 0.8244 1.0401 0.7925 0.1465 0.0070 -0.1734 69 GLU B CA 3069 C C . GLU B 69 ? 0.7608 0.9533 0.7119 0.0882 0.0243 -0.1445 69 GLU B C 3070 O O . GLU B 69 ? 0.6923 0.9479 0.6604 0.0370 0.0390 -0.1248 69 GLU B O 3071 C CB . GLU B 69 ? 0.8904 1.2153 0.8704 0.1995 0.0084 -0.2295 69 GLU B CB 3072 C CG . GLU B 69 ? 1.0101 1.2365 0.9483 0.2794 -0.0252 -0.2656 69 GLU B CG 3073 C CD . GLU B 69 ? 1.0670 1.4102 1.0306 0.3618 -0.0381 -0.3305 69 GLU B CD 3074 O OE1 . GLU B 69 ? 1.0280 1.4895 1.0421 0.3693 -0.0354 -0.3366 69 GLU B OE1 3075 O OE2 . GLU B 69 ? 1.1680 1.4912 1.1002 0.4227 -0.0537 -0.3808 69 GLU B OE2 3076 N N . PHE B 70 ? 0.7878 0.8828 0.6977 0.0925 0.0162 -0.1395 70 PHE B N 3077 C CA . PHE B 70 ? 0.7769 0.8495 0.6689 0.0451 0.0265 -0.1130 70 PHE B CA 3078 C C . PHE B 70 ? 0.8074 0.8493 0.6581 0.0599 0.0239 -0.1374 70 PHE B C 3079 O O . PHE B 70 ? 0.8549 0.8361 0.6771 0.1051 0.0047 -0.1663 70 PHE B O 3080 C CB . PHE B 70 ? 0.7709 0.7625 0.6561 0.0229 0.0168 -0.0771 70 PHE B CB 3081 C CG . PHE B 70 ? 0.7350 0.7412 0.6521 0.0153 0.0147 -0.0616 70 PHE B CG 3082 C CD1 . PHE B 70 ? 0.7367 0.7242 0.6597 0.0431 0.0032 -0.0690 70 PHE B CD1 3083 C CD2 . PHE B 70 ? 0.7187 0.7446 0.6497 -0.0202 0.0176 -0.0398 70 PHE B CD2 3084 C CE1 . PHE B 70 ? 0.7092 0.7147 0.6580 0.0346 0.0007 -0.0596 70 PHE B CE1 3085 C CE2 . PHE B 70 ? 0.6976 0.7210 0.6485 -0.0266 0.0100 -0.0319 70 PHE B CE2 3086 C CZ . PHE B 70 ? 0.6878 0.7095 0.6509 0.0003 0.0045 -0.0442 70 PHE B CZ 3087 N N . ASN B 71 ? 0.7979 0.8695 0.6361 0.0218 0.0368 -0.1260 71 ASN B N 3088 C CA . ASN B 71 ? 0.8396 0.8897 0.6346 0.0303 0.0346 -0.1527 71 ASN B CA 3089 C C . ASN B 71 ? 0.8547 0.7983 0.6126 0.0071 0.0192 -0.1286 71 ASN B C 3090 O O . ASN B 71 ? 0.8068 0.7117 0.5771 -0.0103 0.0127 -0.0950 71 ASN B O 3091 C CB . ASN B 71 ? 0.8264 0.9874 0.6196 0.0003 0.0562 -0.1600 71 ASN B CB 3092 C CG . ASN B 71 ? 0.8083 0.9636 0.5945 -0.0609 0.0588 -0.1076 71 ASN B CG 3093 O OD1 . ASN B 71 ? 0.8130 0.8904 0.5823 -0.0724 0.0459 -0.0849 71 ASN B OD1 3094 N ND2 . ASN B 71 ? 0.8174 1.0606 0.6108 -0.1025 0.0710 -0.0885 71 ASN B ND2 3095 N N . ASN B 72 ? 0.9240 0.8366 0.6355 0.0044 0.0135 -0.1502 72 ASN B N 3096 C CA . ASN B 72 ? 0.9906 0.8097 0.6571 -0.0243 -0.0048 -0.1343 72 ASN B CA 3097 C C . ASN B 72 ? 0.9331 0.7853 0.6169 -0.0741 0.0015 -0.0892 72 ASN B C 3098 O O . ASN B 72 ? 0.9379 0.7457 0.6005 -0.1017 -0.0119 -0.0715 72 ASN B O 3099 C CB . ASN B 72 ? 1.0986 0.8748 0.7042 -0.0166 -0.0162 -0.1753 72 ASN B CB 3100 C CG . ASN B 72 ? 1.2026 0.8579 0.7450 -0.0494 -0.0447 -0.1650 72 ASN B CG 3101 O OD1 . ASN B 72 ? 1.2832 0.8517 0.8053 -0.0504 -0.0662 -0.1506 72 ASN B OD1 3102 N ND2 . ASN B 72 ? 1.2444 0.8984 0.7487 -0.0858 -0.0470 -0.1697 72 ASN B ND2 3103 N N . LEU B 73 ? 0.8654 0.7977 0.5811 -0.0869 0.0166 -0.0716 73 LEU B N 3104 C CA . LEU B 73 ? 0.8492 0.8035 0.5809 -0.1160 0.0120 -0.0322 73 LEU B CA 3105 C C . LEU B 73 ? 0.8084 0.7750 0.5842 -0.1067 0.0112 -0.0092 73 LEU B C 3106 O O . LEU B 73 ? 0.7817 0.7645 0.5674 -0.1190 0.0022 0.0179 73 LEU B O 3107 C CB . LEU B 73 ? 0.8767 0.8801 0.5882 -0.1423 0.0149 -0.0232 73 LEU B CB 3108 C CG . LEU B 73 ? 0.9513 0.9441 0.6155 -0.1590 0.0109 -0.0430 73 LEU B CG 3109 C CD1 . LEU B 73 ? 0.9604 1.0168 0.6010 -0.1843 0.0166 -0.0377 73 LEU B CD1 3110 C CD2 . LEU B 73 ? 0.9589 0.9279 0.6170 -0.1793 -0.0059 -0.0259 73 LEU B CD2 3111 N N . GLU B 74 ? 0.7729 0.7206 0.5671 -0.0826 0.0140 -0.0218 74 GLU B N 3112 C CA . GLU B 74 ? 0.7362 0.6851 0.5662 -0.0738 0.0102 -0.0066 74 GLU B CA 3113 C C . GLU B 74 ? 0.7102 0.6251 0.5429 -0.0604 0.0037 -0.0108 74 GLU B C 3114 O O . GLU B 74 ? 0.6799 0.5916 0.5331 -0.0439 0.0035 -0.0140 74 GLU B O 3115 C CB . GLU B 74 ? 0.7160 0.6992 0.5647 -0.0683 0.0197 -0.0149 74 GLU B CB 3116 C CG . GLU B 74 ? 0.7266 0.7579 0.5645 -0.1005 0.0251 -0.0026 74 GLU B CG 3117 C CD . GLU B 74 ? 0.7448 0.8416 0.5996 -0.1082 0.0368 -0.0135 74 GLU B CD 3118 O OE1 . GLU B 74 ? 0.7523 0.8801 0.6222 -0.0742 0.0457 -0.0479 74 GLU B OE1 3119 O OE2 . GLU B 74 ? 0.7512 0.8690 0.5991 -0.1503 0.0323 0.0126 74 GLU B OE2 3120 N N . ARG B 75 ? 0.7386 0.6349 0.5442 -0.0768 -0.0031 -0.0086 75 ARG B N 3121 C CA . ARG B 75 ? 0.7627 0.6327 0.5540 -0.0837 -0.0112 -0.0060 75 ARG B CA 3122 C C . ARG B 75 ? 0.7198 0.6371 0.5480 -0.0779 -0.0116 0.0032 75 ARG B C 3123 O O . ARG B 75 ? 0.6921 0.6002 0.5180 -0.0754 -0.0142 0.0031 75 ARG B O 3124 C CB . ARG B 75 ? 0.8531 0.7035 0.5976 -0.1226 -0.0208 -0.0017 75 ARG B CB 3125 C CG . ARG B 75 ? 0.9684 0.7420 0.6578 -0.1255 -0.0295 -0.0197 75 ARG B CG 3126 C CD . ARG B 75 ? 1.0707 0.7656 0.7361 -0.0934 -0.0418 -0.0350 75 ARG B CD 3127 N NE . ARG B 75 ? 1.2525 0.8632 0.8594 -0.0799 -0.0590 -0.0636 75 ARG B NE 3128 C CZ . ARG B 75 ? 1.3803 0.9177 0.9603 -0.0330 -0.0783 -0.0895 75 ARG B CZ 3129 N NH1 . ARG B 75 ? 1.3702 0.9151 0.9786 -0.0022 -0.0808 -0.0846 75 ARG B NH1 3130 N NH2 . ARG B 75 ? 1.4726 0.9294 0.9944 -0.0104 -0.0997 -0.1255 75 ARG B NH2 3131 N N . ARG B 76 ? 0.6993 0.6639 0.5554 -0.0712 -0.0140 0.0082 76 ARG B N 3132 C CA . ARG B 76 ? 0.6651 0.6751 0.5527 -0.0522 -0.0200 0.0041 76 ARG B CA 3133 C C . ARG B 76 ? 0.6663 0.6491 0.5721 -0.0300 -0.0189 -0.0022 76 ARG B C 3134 O O . ARG B 76 ? 0.6421 0.6442 0.5541 -0.0247 -0.0182 -0.0098 76 ARG B O 3135 C CB . ARG B 76 ? 0.6540 0.7000 0.5608 -0.0332 -0.0348 0.0049 76 ARG B CB 3136 C CG . ARG B 76 ? 0.6527 0.7620 0.5511 -0.0525 -0.0384 0.0069 76 ARG B CG 3137 C CD . ARG B 76 ? 0.6714 0.7988 0.5819 -0.0254 -0.0607 0.0105 76 ARG B CD 3138 N NE . ARG B 76 ? 0.6812 0.7323 0.5703 -0.0325 -0.0641 0.0289 76 ARG B NE 3139 C CZ . ARG B 76 ? 0.7056 0.7227 0.5889 -0.0131 -0.0907 0.0420 76 ARG B CZ 3140 N NH1 . ARG B 76 ? 0.7333 0.7705 0.6332 0.0323 -0.1220 0.0327 76 ARG B NH1 3141 N NH2 . ARG B 76 ? 0.7153 0.6788 0.5692 -0.0391 -0.0901 0.0632 76 ARG B NH2 3142 N N . ILE B 77 ? 0.6884 0.6381 0.5982 -0.0256 -0.0189 0.0017 77 ILE B N 3143 C CA . ILE B 77 ? 0.6913 0.6257 0.6167 -0.0151 -0.0196 -0.0040 77 ILE B CA 3144 C C . ILE B 77 ? 0.6968 0.6269 0.6168 -0.0127 -0.0102 -0.0118 77 ILE B C 3145 O O . ILE B 77 ? 0.7037 0.6378 0.6373 -0.0024 -0.0126 -0.0187 77 ILE B O 3146 C CB . ILE B 77 ? 0.7124 0.6285 0.6360 -0.0285 -0.0242 0.0061 77 ILE B CB 3147 C CG1 . ILE B 77 ? 0.7589 0.6929 0.6676 -0.0466 -0.0089 0.0080 77 ILE B CG1 3148 C CG2 . ILE B 77 ? 0.7561 0.6446 0.6708 -0.0260 -0.0481 0.0185 77 ILE B CG2 3149 C CD1 . ILE B 77 ? 0.8262 0.7734 0.7281 -0.0760 -0.0096 0.0199 77 ILE B CD1 3150 N N . GLU B 78 ? 0.7018 0.6149 0.5959 -0.0186 -0.0059 -0.0128 78 GLU B N 3151 C CA . GLU B 78 ? 0.7398 0.6247 0.6158 -0.0061 -0.0103 -0.0207 78 GLU B CA 3152 C C . GLU B 78 ? 0.7156 0.5960 0.5780 -0.0155 -0.0183 -0.0120 78 GLU B C 3153 O O . GLU B 78 ? 0.6943 0.5671 0.5552 -0.0034 -0.0253 -0.0139 78 GLU B O 3154 C CB . GLU B 78 ? 0.8299 0.6700 0.6653 -0.0052 -0.0152 -0.0285 78 GLU B CB 3155 C CG . GLU B 78 ? 0.9386 0.7218 0.7424 0.0205 -0.0336 -0.0393 78 GLU B CG 3156 C CD . GLU B 78 ? 1.1183 0.8386 0.8746 0.0343 -0.0469 -0.0582 78 GLU B CD 3157 O OE1 . GLU B 78 ? 1.2116 0.8911 0.9284 0.0008 -0.0515 -0.0491 78 GLU B OE1 3158 O OE2 . GLU B 78 ? 1.2019 0.9213 0.9596 0.0812 -0.0549 -0.0876 78 GLU B OE2 3159 N N . ASN B 79 ? 0.6889 0.5920 0.5406 -0.0403 -0.0178 -0.0033 79 ASN B N 3160 C CA . ASN B 79 ? 0.7327 0.6657 0.5672 -0.0624 -0.0219 0.0040 79 ASN B CA 3161 C C . ASN B 79 ? 0.6919 0.6808 0.5652 -0.0404 -0.0185 -0.0091 79 ASN B C 3162 O O . ASN B 79 ? 0.6859 0.6927 0.5450 -0.0486 -0.0219 -0.0075 79 ASN B O 3163 C CB . ASN B 79 ? 0.7622 0.7456 0.5841 -0.0969 -0.0201 0.0102 79 ASN B CB 3164 C CG . ASN B 79 ? 0.8092 0.8549 0.6069 -0.1353 -0.0219 0.0180 79 ASN B CG 3165 O OD1 . ASN B 79 ? 0.8989 0.8940 0.6474 -0.1617 -0.0330 0.0345 79 ASN B OD1 3166 N ND2 . ASN B 79 ? 0.8042 0.9680 0.6316 -0.1390 -0.0147 0.0056 79 ASN B ND2 3167 N N . LEU B 80 ? 0.6646 0.6696 0.5764 -0.0150 -0.0169 -0.0216 80 LEU B N 3168 C CA . LEU B 80 ? 0.6526 0.6826 0.5921 0.0103 -0.0219 -0.0403 80 LEU B CA 3169 C C . LEU B 80 ? 0.6496 0.6500 0.5890 0.0145 -0.0231 -0.0408 80 LEU B C 3170 O O . LEU B 80 ? 0.6455 0.6730 0.5865 0.0201 -0.0260 -0.0519 80 LEU B O 3171 C CB . LEU B 80 ? 0.6592 0.6675 0.6185 0.0310 -0.0327 -0.0469 80 LEU B CB 3172 C CG . LEU B 80 ? 0.6871 0.6944 0.6618 0.0631 -0.0509 -0.0721 80 LEU B CG 3173 C CD1 . LEU B 80 ? 0.7354 0.6927 0.7078 0.0801 -0.0744 -0.0701 80 LEU B CD1 3174 C CD2 . LEU B 80 ? 0.7304 0.7048 0.7061 0.0591 -0.0533 -0.0770 80 LEU B CD2 3175 N N . ASN B 81 ? 0.6587 0.6210 0.5968 0.0133 -0.0211 -0.0328 81 ASN B N 3176 C CA . ASN B 81 ? 0.6645 0.6226 0.6082 0.0222 -0.0242 -0.0370 81 ASN B CA 3177 C C . ASN B 81 ? 0.6983 0.6500 0.6130 0.0224 -0.0323 -0.0308 81 ASN B C 3178 O O . ASN B 81 ? 0.6782 0.6467 0.5978 0.0302 -0.0391 -0.0365 81 ASN B O 3179 C CB . ASN B 81 ? 0.6442 0.5954 0.5918 0.0264 -0.0201 -0.0373 81 ASN B CB 3180 C CG . ASN B 81 ? 0.6585 0.6389 0.6226 0.0410 -0.0246 -0.0483 81 ASN B CG 3181 O OD1 . ASN B 81 ? 0.6688 0.6781 0.6555 0.0312 -0.0259 -0.0539 81 ASN B OD1 3182 N ND2 . ASN B 81 ? 0.6725 0.6428 0.6208 0.0663 -0.0328 -0.0541 81 ASN B ND2 3183 N N . LYS B 82 ? 0.7362 0.6570 0.6112 0.0064 -0.0359 -0.0161 82 LYS B N 3184 C CA . LYS B 82 ? 0.8261 0.7111 0.6496 -0.0064 -0.0532 0.0001 82 LYS B CA 3185 C C . LYS B 82 ? 0.8233 0.7698 0.6415 -0.0285 -0.0504 0.0023 82 LYS B C 3186 O O . LYS B 82 ? 0.7974 0.7440 0.5956 -0.0286 -0.0628 0.0080 82 LYS B O 3187 C CB . LYS B 82 ? 0.9442 0.7653 0.7120 -0.0336 -0.0633 0.0176 82 LYS B CB 3188 C CG . LYS B 82 ? 1.0929 0.8092 0.7993 -0.0218 -0.0958 0.0280 82 LYS B CG 3189 C CD . LYS B 82 ? 1.1996 0.8845 0.8421 -0.0567 -0.1197 0.0567 82 LYS B CD 3190 C CE . LYS B 82 ? 1.3072 0.9598 0.8795 -0.1278 -0.1284 0.0852 82 LYS B CE 3191 N NZ . LYS B 82 ? 1.4133 1.0310 0.9055 -0.1770 -0.1566 0.1211 82 LYS B NZ 3192 N N . LYS B 83 ? 0.7936 0.8055 0.6305 -0.0421 -0.0359 -0.0069 83 LYS B N 3193 C CA . LYS B 83 ? 0.8056 0.9094 0.6426 -0.0559 -0.0306 -0.0180 83 LYS B CA 3194 C C . LYS B 83 ? 0.7558 0.8858 0.6253 -0.0231 -0.0315 -0.0443 83 LYS B C 3195 O O . LYS B 83 ? 0.7569 0.9441 0.6104 -0.0338 -0.0329 -0.0511 83 LYS B O 3196 C CB . LYS B 83 ? 0.8228 1.0108 0.6831 -0.0593 -0.0187 -0.0347 83 LYS B CB 3197 C CG . LYS B 83 ? 0.9211 1.1663 0.7368 -0.1183 -0.0164 -0.0143 83 LYS B CG 3198 C CD . LYS B 83 ? 1.0380 1.1714 0.7959 -0.1576 -0.0296 0.0236 83 LYS B CD 3199 C CE . LYS B 83 ? 1.1739 1.2534 0.8545 -0.2041 -0.0496 0.0569 83 LYS B CE 3200 N NZ . LYS B 83 ? 1.2192 1.4108 0.8581 -0.2743 -0.0459 0.0705 83 LYS B NZ 3201 N N . MET B 84 ? 0.7201 0.8105 0.6273 0.0076 -0.0326 -0.0578 84 MET B N 3202 C CA . MET B 84 ? 0.6997 0.7982 0.6298 0.0282 -0.0387 -0.0816 84 MET B CA 3203 C C . MET B 84 ? 0.6797 0.7677 0.5930 0.0237 -0.0480 -0.0701 84 MET B C 3204 O O . MET B 84 ? 0.6646 0.7921 0.5730 0.0245 -0.0532 -0.0850 84 MET B O 3205 C CB . MET B 84 ? 0.7125 0.7643 0.6719 0.0423 -0.0425 -0.0898 84 MET B CB 3206 C CG . MET B 84 ? 0.7579 0.8035 0.7297 0.0544 -0.0558 -0.1182 84 MET B CG 3207 S SD . MET B 84 ? 0.8409 0.8415 0.8254 0.0365 -0.0639 -0.1093 84 MET B SD 3208 C CE . MET B 84 ? 0.8293 0.8696 0.8142 0.0336 -0.0568 -0.0923 84 MET B CE 3209 N N . GLU B 85 ? 0.9266 1.0078 0.6328 0.0827 -0.0547 -0.0552 85 GLU B N 3210 C CA . GLU B 85 ? 0.9186 1.0128 0.6288 0.0920 -0.0510 -0.0631 85 GLU B CA 3211 C C . GLU B 85 ? 0.8905 0.9450 0.6109 0.0859 -0.0621 -0.0695 85 GLU B C 3212 O O . GLU B 85 ? 0.8554 0.9158 0.5966 0.0779 -0.0552 -0.0652 85 GLU B O 3213 C CB . GLU B 85 ? 0.9776 1.0888 0.6564 0.1243 -0.0551 -0.0790 85 GLU B CB 3214 C CG . GLU B 85 ? 1.0330 1.1967 0.7001 0.1313 -0.0442 -0.0725 85 GLU B CG 3215 C CD . GLU B 85 ? 1.0494 1.2912 0.7192 0.1402 -0.0290 -0.0686 85 GLU B CD 3216 O OE1 . GLU B 85 ? 1.0420 1.3136 0.7341 0.1099 -0.0165 -0.0513 85 GLU B OE1 3217 O OE2 . GLU B 85 ? 1.0931 1.3705 0.7368 0.1782 -0.0310 -0.0826 85 GLU B OE2 3218 N N . ASP B 86 ? 0.8919 0.9076 0.5937 0.0846 -0.0805 -0.0781 86 ASP B N 3219 C CA . ASP B 86 ? 0.8952 0.8731 0.5983 0.0693 -0.0944 -0.0810 86 ASP B CA 3220 C C . ASP B 86 ? 0.8335 0.8287 0.5763 0.0479 -0.0867 -0.0661 86 ASP B C 3221 O O . ASP B 86 ? 0.8152 0.7981 0.5699 0.0398 -0.0882 -0.0659 86 ASP B O 3222 C CB . ASP B 86 ? 0.9553 0.8969 0.6259 0.0574 -0.1175 -0.0872 86 ASP B CB 3223 C CG . ASP B 86 ? 1.0557 0.9372 0.6670 0.0746 -0.1364 -0.1058 86 ASP B CG 3224 O OD1 . ASP B 86 ? 1.1478 1.0006 0.7458 0.0856 -0.1387 -0.1126 86 ASP B OD1 3225 O OD2 . ASP B 86 ? 1.0936 0.9497 0.6634 0.0802 -0.1508 -0.1143 86 ASP B OD2 3226 N N . GLY B 87 ? 0.7963 0.8158 0.5518 0.0438 -0.0799 -0.0545 87 GLY B N 3227 C CA . GLY B 87 ? 0.7633 0.7955 0.5427 0.0352 -0.0743 -0.0419 87 GLY B CA 3228 C C . GLY B 87 ? 0.7531 0.7819 0.5468 0.0342 -0.0613 -0.0378 87 GLY B C 3229 O O . GLY B 87 ? 0.7273 0.7531 0.5383 0.0269 -0.0621 -0.0350 87 GLY B O 3230 N N . PHE B 88 ? 0.7324 0.7690 0.5175 0.0382 -0.0501 -0.0363 88 PHE B N 3231 C CA . PHE B 88 ? 0.7244 0.7666 0.5191 0.0301 -0.0390 -0.0308 88 PHE B CA 3232 C C . PHE B 88 ? 0.7361 0.7797 0.5437 0.0340 -0.0417 -0.0415 88 PHE B C 3233 O O . PHE B 88 ? 0.7381 0.7786 0.5616 0.0255 -0.0377 -0.0376 88 PHE B O 3234 C CB . PHE B 88 ? 0.7286 0.7952 0.5074 0.0245 -0.0281 -0.0237 88 PHE B CB 3235 C CG . PHE B 88 ? 0.7476 0.7926 0.5020 0.0136 -0.0255 -0.0085 88 PHE B CG 3236 C CD1 . PHE B 88 ? 0.7569 0.7644 0.5007 0.0037 -0.0255 0.0020 88 PHE B CD1 3237 C CD2 . PHE B 88 ? 0.7741 0.8272 0.5058 0.0170 -0.0249 -0.0050 88 PHE B CD2 3238 C CE1 . PHE B 88 ? 0.7942 0.7610 0.4956 -0.0003 -0.0270 0.0151 88 PHE B CE1 3239 C CE2 . PHE B 88 ? 0.8057 0.8253 0.5021 0.0089 -0.0248 0.0095 88 PHE B CE2 3240 C CZ . PHE B 88 ? 0.8292 0.7999 0.5058 0.0015 -0.0269 0.0194 88 PHE B CZ 3241 N N . LEU B 89 ? 0.7677 0.8073 0.5597 0.0499 -0.0503 -0.0555 89 LEU B N 3242 C CA . LEU B 89 ? 0.7884 0.8116 0.5756 0.0600 -0.0571 -0.0668 89 LEU B CA 3243 C C . LEU B 89 ? 0.7665 0.7599 0.5677 0.0426 -0.0655 -0.0635 89 LEU B C 3244 O O . LEU B 89 ? 0.7336 0.7240 0.5465 0.0412 -0.0631 -0.0639 89 LEU B O 3245 C CB . LEU B 89 ? 0.8559 0.8514 0.6014 0.0838 -0.0718 -0.0835 89 LEU B CB 3246 C CG . LEU B 89 ? 0.9256 0.9592 0.6499 0.1132 -0.0652 -0.0910 89 LEU B CG 3247 C CD1 . LEU B 89 ? 0.9901 0.9725 0.6569 0.1436 -0.0853 -0.1105 89 LEU B CD1 3248 C CD2 . LEU B 89 ? 0.9116 1.0069 0.6524 0.1238 -0.0495 -0.0885 89 LEU B CD2 3249 N N . ASP B 90 ? 0.7699 0.7524 0.5697 0.0288 -0.0754 -0.0592 90 ASP B N 3250 C CA . ASP B 90 ? 0.7684 0.7434 0.5810 0.0092 -0.0839 -0.0535 90 ASP B CA 3251 C C . ASP B 90 ? 0.7147 0.7129 0.5590 0.0063 -0.0704 -0.0425 90 ASP B C 3252 O O . ASP B 90 ? 0.7241 0.7185 0.5810 -0.0021 -0.0723 -0.0405 90 ASP B O 3253 C CB . ASP B 90 ? 0.7922 0.7767 0.5974 -0.0062 -0.0968 -0.0489 90 ASP B CB 3254 C CG . ASP B 90 ? 0.8711 0.8149 0.6330 -0.0124 -0.1167 -0.0596 90 ASP B CG 3255 O OD1 . ASP B 90 ? 0.9266 0.8244 0.6579 -0.0001 -0.1228 -0.0716 90 ASP B OD1 3256 O OD2 . ASP B 90 ? 0.9448 0.9001 0.6956 -0.0273 -0.1281 -0.0566 90 ASP B OD2 3257 N N . VAL B 91 ? 0.6876 0.7005 0.5351 0.0131 -0.0590 -0.0353 91 VAL B N 3258 C CA . VAL B 91 ? 0.6701 0.6844 0.5279 0.0127 -0.0496 -0.0259 91 VAL B CA 3259 C C . VAL B 91 ? 0.6726 0.6822 0.5399 0.0084 -0.0424 -0.0283 91 VAL B C 3260 O O . VAL B 91 ? 0.6774 0.6830 0.5572 0.0047 -0.0410 -0.0249 91 VAL B O 3261 C CB . VAL B 91 ? 0.6775 0.6845 0.5143 0.0183 -0.0429 -0.0175 91 VAL B CB 3262 C CG1 . VAL B 91 ? 0.6856 0.6695 0.5125 0.0155 -0.0368 -0.0091 91 VAL B CG1 3263 C CG2 . VAL B 91 ? 0.6905 0.7076 0.5172 0.0295 -0.0500 -0.0140 91 VAL B CG2 3264 N N . TRP B 92 ? 0.6705 0.6903 0.5310 0.0117 -0.0380 -0.0342 92 TRP B N 3265 C CA . TRP B 92 ? 0.6680 0.7021 0.5371 0.0097 -0.0309 -0.0361 92 TRP B CA 3266 C C . TRP B 92 ? 0.6632 0.6854 0.5383 0.0179 -0.0386 -0.0460 92 TRP B C 3267 O O . TRP B 92 ? 0.6548 0.6827 0.5426 0.0151 -0.0346 -0.0454 92 TRP B O 3268 C CB . TRP B 92 ? 0.6749 0.7472 0.5332 0.0132 -0.0231 -0.0372 92 TRP B CB 3269 C CG . TRP B 92 ? 0.7024 0.7803 0.5486 -0.0076 -0.0155 -0.0226 92 TRP B CG 3270 C CD1 . TRP B 92 ? 0.7345 0.8163 0.5608 -0.0099 -0.0142 -0.0174 92 TRP B CD1 3271 C CD2 . TRP B 92 ? 0.7089 0.7747 0.5495 -0.0317 -0.0111 -0.0105 92 TRP B CD2 3272 N NE1 . TRP B 92 ? 0.7654 0.8332 0.5691 -0.0359 -0.0101 -0.0017 92 TRP B NE1 3273 C CE2 . TRP B 92 ? 0.7463 0.7996 0.5546 -0.0505 -0.0093 0.0025 92 TRP B CE2 3274 C CE3 . TRP B 92 ? 0.7153 0.7725 0.5674 -0.0405 -0.0104 -0.0093 92 TRP B CE3 3275 C CZ2 . TRP B 92 ? 0.7916 0.8119 0.5689 -0.0804 -0.0094 0.0169 92 TRP B CZ2 3276 C CZ3 . TRP B 92 ? 0.7403 0.7729 0.5682 -0.0679 -0.0093 0.0037 92 TRP B CZ3 3277 C CH2 . TRP B 92 ? 0.7879 0.7964 0.5739 -0.0890 -0.0100 0.0168 92 TRP B CH2 3278 N N . THR B 93 ? 0.6737 0.6716 0.5315 0.0251 -0.0518 -0.0543 93 THR B N 3279 C CA . THR B 93 ? 0.6877 0.6529 0.5341 0.0269 -0.0640 -0.0615 93 THR B CA 3280 C C . THR B 93 ? 0.6838 0.6480 0.5543 0.0070 -0.0644 -0.0514 93 THR B C 3281 O O . THR B 93 ? 0.6967 0.6533 0.5736 0.0067 -0.0642 -0.0523 93 THR B O 3282 C CB . THR B 93 ? 0.7275 0.6497 0.5340 0.0285 -0.0831 -0.0698 93 THR B CB 3283 O OG1 . THR B 93 ? 0.7577 0.6796 0.5348 0.0568 -0.0834 -0.0818 93 THR B OG1 3284 C CG2 . THR B 93 ? 0.7708 0.6405 0.5497 0.0214 -0.1000 -0.0740 93 THR B CG2 3285 N N . TYR B 94 ? 0.6719 0.6510 0.5535 -0.0045 -0.0648 -0.0420 94 TYR B N 3286 C CA . TYR B 94 ? 0.6540 0.6491 0.5557 -0.0154 -0.0647 -0.0321 94 TYR B CA 3287 C C . TYR B 94 ? 0.6442 0.6441 0.5622 -0.0095 -0.0520 -0.0290 94 TYR B C 3288 O O . TYR B 94 ? 0.6209 0.6196 0.5499 -0.0141 -0.0528 -0.0277 94 TYR B O 3289 C CB . TYR B 94 ? 0.6504 0.6744 0.5548 -0.0158 -0.0662 -0.0237 94 TYR B CB 3290 C CG . TYR B 94 ? 0.6311 0.6864 0.5514 -0.0130 -0.0638 -0.0139 94 TYR B CG 3291 C CD1 . TYR B 94 ? 0.6262 0.6751 0.5443 0.0050 -0.0534 -0.0105 94 TYR B CD1 3292 C CD2 . TYR B 94 ? 0.6249 0.7161 0.5534 -0.0289 -0.0738 -0.0074 94 TYR B CD2 3293 C CE1 . TYR B 94 ? 0.6267 0.6992 0.5482 0.0180 -0.0528 -0.0038 94 TYR B CE1 3294 C CE2 . TYR B 94 ? 0.6073 0.7434 0.5492 -0.0195 -0.0709 0.0014 94 TYR B CE2 3295 C CZ . TYR B 94 ? 0.6140 0.7383 0.5513 0.0095 -0.0602 0.0017 94 TYR B CZ 3296 O OH . TYR B 94 ? 0.6303 0.7938 0.5700 0.0291 -0.0589 0.0082 94 TYR B OH 3297 N N . ASN B 95 ? 0.6633 0.6648 0.5763 -0.0037 -0.0420 -0.0269 95 ASN B N 3298 C CA . ASN B 95 ? 0.6493 0.6465 0.5653 -0.0063 -0.0332 -0.0229 95 ASN B CA 3299 C C . ASN B 95 ? 0.6587 0.6615 0.5869 -0.0080 -0.0317 -0.0292 95 ASN B C 3300 O O . ASN B 95 ? 0.6632 0.6629 0.6017 -0.0110 -0.0301 -0.0267 95 ASN B O 3301 C CB . ASN B 95 ? 0.6663 0.6586 0.5617 -0.0116 -0.0264 -0.0181 95 ASN B CB 3302 C CG . ASN B 95 ? 0.7185 0.6892 0.5893 -0.0052 -0.0288 -0.0105 95 ASN B CG 3303 O OD1 . ASN B 95 ? 0.7249 0.6976 0.5985 0.0078 -0.0341 -0.0091 95 ASN B OD1 3304 N ND2 . ASN B 95 ? 0.7606 0.7156 0.6023 -0.0137 -0.0258 -0.0046 95 ASN B ND2 3305 N N . ALA B 96 ? 0.6511 0.6623 0.5727 -0.0002 -0.0331 -0.0381 96 ALA B N 3306 C CA . ALA B 96 ? 0.6477 0.6678 0.5717 0.0085 -0.0325 -0.0456 96 ALA B CA 3307 C C . ALA B 96 ? 0.6428 0.6347 0.5687 0.0082 -0.0420 -0.0476 96 ALA B C 3308 O O . ALA B 96 ? 0.6276 0.6242 0.5644 0.0081 -0.0390 -0.0473 96 ALA B O 3309 C CB . ALA B 96 ? 0.6689 0.7024 0.5722 0.0297 -0.0348 -0.0565 96 ALA B CB 3310 N N . GLU B 97 ? 0.6644 0.6289 0.5757 0.0032 -0.0546 -0.0481 97 GLU B N 3311 C CA . GLU B 97 ? 0.6946 0.6307 0.5974 -0.0067 -0.0664 -0.0469 97 GLU B CA 3312 C C . GLU B 97 ? 0.6701 0.6294 0.6022 -0.0206 -0.0613 -0.0355 97 GLU B C 3313 O O . GLU B 97 ? 0.6759 0.6267 0.6107 -0.0250 -0.0639 -0.0340 97 GLU B O 3314 C CB . GLU B 97 ? 0.7382 0.6392 0.6077 -0.0197 -0.0847 -0.0476 97 GLU B CB 3315 C CG . GLU B 97 ? 0.8011 0.6602 0.6245 0.0023 -0.0942 -0.0620 97 GLU B CG 3316 C CD . GLU B 97 ? 0.8691 0.6784 0.6458 -0.0135 -0.1156 -0.0635 97 GLU B CD 3317 O OE1 . GLU B 97 ? 0.8954 0.7171 0.6814 -0.0474 -0.1225 -0.0515 97 GLU B OE1 3318 O OE2 . GLU B 97 ? 0.9493 0.7104 0.6745 0.0093 -0.1268 -0.0769 97 GLU B OE2 3319 N N . LEU B 98 ? 0.6411 0.6273 0.5881 -0.0222 -0.0546 -0.0281 98 LEU B N 3320 C CA . LEU B 98 ? 0.6146 0.6238 0.5789 -0.0238 -0.0508 -0.0190 98 LEU B CA 3321 C C . LEU B 98 ? 0.6007 0.6044 0.5732 -0.0165 -0.0411 -0.0205 98 LEU B C 3322 O O . LEU B 98 ? 0.5993 0.6097 0.5818 -0.0172 -0.0407 -0.0170 98 LEU B O 3323 C CB . LEU B 98 ? 0.6118 0.6429 0.5742 -0.0155 -0.0486 -0.0128 98 LEU B CB 3324 C CG . LEU B 98 ? 0.6131 0.6760 0.5825 -0.0058 -0.0478 -0.0044 98 LEU B CG 3325 C CD1 . LEU B 98 ? 0.6028 0.7088 0.5829 -0.0235 -0.0575 0.0030 98 LEU B CD1 3326 C CD2 . LEU B 98 ? 0.6298 0.6993 0.5813 0.0170 -0.0455 -0.0013 98 LEU B CD2 3327 N N . LEU B 99 ? 0.6033 0.6003 0.5693 -0.0132 -0.0340 -0.0246 99 LEU B N 3328 C CA . LEU B 99 ? 0.6022 0.5983 0.5704 -0.0155 -0.0270 -0.0243 99 LEU B CA 3329 C C . LEU B 99 ? 0.5961 0.5970 0.5760 -0.0138 -0.0284 -0.0295 99 LEU B C 3330 O O . LEU B 99 ? 0.5825 0.5840 0.5701 -0.0156 -0.0259 -0.0275 99 LEU B O 3331 C CB . LEU B 99 ? 0.6310 0.6347 0.5872 -0.0223 -0.0210 -0.0249 99 LEU B CB 3332 C CG . LEU B 99 ? 0.6587 0.6667 0.6094 -0.0368 -0.0161 -0.0216 99 LEU B CG 3333 C CD1 . LEU B 99 ? 0.6869 0.6545 0.6170 -0.0398 -0.0186 -0.0148 99 LEU B CD1 3334 C CD2 . LEU B 99 ? 0.6879 0.7210 0.6247 -0.0529 -0.0115 -0.0187 99 LEU B CD2 3335 N N . VAL B 100 ? 0.5890 0.5853 0.5613 -0.0069 -0.0342 -0.0367 100 VAL B N 3336 C CA . VAL B 100 ? 0.5809 0.5686 0.5492 0.0014 -0.0384 -0.0426 100 VAL B CA 3337 C C . VAL B 100 ? 0.5671 0.5390 0.5403 -0.0089 -0.0450 -0.0361 100 VAL B C 3338 O O . VAL B 100 ? 0.5441 0.5193 0.5258 -0.0070 -0.0427 -0.0359 100 VAL B O 3339 C CB . VAL B 100 ? 0.6005 0.5683 0.5383 0.0193 -0.0473 -0.0533 100 VAL B CB 3340 C CG1 . VAL B 100 ? 0.6273 0.5616 0.5422 0.0312 -0.0574 -0.0587 100 VAL B CG1 3341 C CG2 . VAL B 100 ? 0.5974 0.6069 0.5348 0.0348 -0.0383 -0.0594 100 VAL B CG2 3342 N N . LEU B 101 ? 0.5581 0.5229 0.5257 -0.0219 -0.0532 -0.0297 101 LEU B N 3343 C CA . LEU B 101 ? 0.5528 0.5240 0.5254 -0.0378 -0.0593 -0.0199 101 LEU B CA 3344 C C . LEU B 101 ? 0.5313 0.5345 0.5292 -0.0319 -0.0488 -0.0143 101 LEU B C 3345 O O . LEU B 101 ? 0.5341 0.5408 0.5383 -0.0342 -0.0491 -0.0113 101 LEU B O 3346 C CB . LEU B 101 ? 0.5554 0.5402 0.5206 -0.0571 -0.0690 -0.0112 101 LEU B CB 3347 C CG . LEU B 101 ? 0.6149 0.5553 0.5412 -0.0718 -0.0857 -0.0144 101 LEU B CG 3348 C CD1 . LEU B 101 ? 0.6287 0.6012 0.5525 -0.0996 -0.0953 -0.0024 101 LEU B CD1 3349 C CD2 . LEU B 101 ? 0.6669 0.5505 0.5565 -0.0798 -0.0992 -0.0164 101 LEU B CD2 3350 N N . MET B 102 ? 0.5216 0.5391 0.5243 -0.0223 -0.0415 -0.0132 102 MET B N 3351 C CA . MET B 102 ? 0.5360 0.5651 0.5430 -0.0108 -0.0356 -0.0095 102 MET B CA 3352 C C . MET B 102 ? 0.5487 0.5612 0.5579 -0.0093 -0.0305 -0.0144 102 MET B C 3353 O O . MET B 102 ? 0.5628 0.5820 0.5766 -0.0045 -0.0296 -0.0118 102 MET B O 3354 C CB . MET B 102 ? 0.5594 0.5816 0.5496 0.0022 -0.0327 -0.0085 102 MET B CB 3355 C CG . MET B 102 ? 0.5939 0.6496 0.5820 0.0096 -0.0372 -0.0022 102 MET B CG 3356 S SD . MET B 102 ? 0.6777 0.7087 0.6308 0.0338 -0.0356 -0.0023 102 MET B SD 3357 C CE . MET B 102 ? 0.6889 0.7882 0.6453 0.0510 -0.0411 0.0056 102 MET B CE 3358 N N . GLU B 103 ? 0.5440 0.5452 0.5492 -0.0130 -0.0273 -0.0209 103 GLU B N 3359 C CA . GLU B 103 ? 0.5619 0.5634 0.5688 -0.0156 -0.0229 -0.0243 103 GLU B CA 3360 C C . GLU B 103 ? 0.5490 0.5571 0.5669 -0.0119 -0.0252 -0.0279 103 GLU B C 3361 O O . GLU B 103 ? 0.5571 0.5703 0.5801 -0.0117 -0.0229 -0.0287 103 GLU B O 3362 C CB . GLU B 103 ? 0.5804 0.5903 0.5783 -0.0241 -0.0187 -0.0272 103 GLU B CB 3363 C CG . GLU B 103 ? 0.6261 0.6128 0.5989 -0.0340 -0.0182 -0.0215 103 GLU B CG 3364 C CD . GLU B 103 ? 0.6654 0.6192 0.6157 -0.0368 -0.0206 -0.0178 103 GLU B CD 3365 O OE1 . GLU B 103 ? 0.6520 0.6136 0.6090 -0.0427 -0.0199 -0.0195 103 GLU B OE1 3366 O OE2 . GLU B 103 ? 0.7354 0.6506 0.6534 -0.0290 -0.0247 -0.0139 103 GLU B OE2 3367 N N . ASN B 104 ? 0.5579 0.5566 0.5701 -0.0093 -0.0322 -0.0299 104 ASN B N 3368 C CA . ASN B 104 ? 0.5576 0.5427 0.5635 -0.0053 -0.0384 -0.0317 104 ASN B CA 3369 C C . ASN B 104 ? 0.5513 0.5428 0.5683 -0.0137 -0.0392 -0.0226 104 ASN B C 3370 O O . ASN B 104 ? 0.5101 0.5006 0.5296 -0.0099 -0.0390 -0.0234 104 ASN B O 3371 C CB . ASN B 104 ? 0.5762 0.5256 0.5523 -0.0049 -0.0512 -0.0343 104 ASN B CB 3372 C CG . ASN B 104 ? 0.6049 0.5481 0.5604 0.0173 -0.0520 -0.0467 104 ASN B CG 3373 O OD1 . ASN B 104 ? 0.5814 0.5629 0.5507 0.0289 -0.0420 -0.0518 104 ASN B OD1 3374 N ND2 . ASN B 104 ? 0.6515 0.5501 0.5677 0.0226 -0.0654 -0.0510 104 ASN B ND2 3375 N N . GLU B 105 ? 0.5686 0.5758 0.5911 -0.0215 -0.0401 -0.0140 105 GLU B N 3376 C CA . GLU B 105 ? 0.5934 0.6261 0.6257 -0.0240 -0.0400 -0.0047 105 GLU B CA 3377 C C . GLU B 105 ? 0.5610 0.5966 0.5998 -0.0096 -0.0320 -0.0084 105 GLU B C 3378 O O . GLU B 105 ? 0.5175 0.5608 0.5616 -0.0078 -0.0317 -0.0061 105 GLU B O 3379 C CB . GLU B 105 ? 0.6552 0.7247 0.6902 -0.0268 -0.0418 0.0047 105 GLU B CB 3380 C CG . GLU B 105 ? 0.7262 0.8431 0.7685 -0.0338 -0.0447 0.0172 105 GLU B CG 3381 C CD . GLU B 105 ? 0.8283 0.9978 0.8708 -0.0472 -0.0506 0.0288 105 GLU B CD 3382 O OE1 . GLU B 105 ? 0.9356 1.1253 0.9779 -0.0275 -0.0468 0.0269 105 GLU B OE1 3383 O OE2 . GLU B 105 ? 0.8647 1.0543 0.9014 -0.0799 -0.0606 0.0408 105 GLU B OE2 3384 N N . ARG B 106 ? 0.5747 0.5976 0.6057 -0.0031 -0.0273 -0.0134 106 ARG B N 3385 C CA . ARG B 106 ? 0.5993 0.6088 0.6205 0.0031 -0.0240 -0.0162 106 ARG B CA 3386 C C . ARG B 106 ? 0.5611 0.5708 0.5900 -0.0038 -0.0222 -0.0218 106 ARG B C 3387 O O . ARG B 106 ? 0.5638 0.5697 0.5889 -0.0014 -0.0217 -0.0225 106 ARG B O 3388 C CB . ARG B 106 ? 0.6657 0.6473 0.6598 0.0037 -0.0238 -0.0174 106 ARG B CB 3389 C CG . ARG B 106 ? 0.7347 0.7179 0.7137 0.0217 -0.0264 -0.0127 106 ARG B CG 3390 C CD . ARG B 106 ? 0.8465 0.7798 0.7778 0.0307 -0.0297 -0.0136 106 ARG B CD 3391 N NE . ARG B 106 ? 0.9377 0.8461 0.8336 0.0567 -0.0343 -0.0141 106 ARG B NE 3392 C CZ . ARG B 106 ? 1.0041 0.8564 0.8593 0.0527 -0.0394 -0.0174 106 ARG B CZ 3393 N NH1 . ARG B 106 ? 1.0477 0.8758 0.8971 0.0170 -0.0396 -0.0183 106 ARG B NH1 3394 N NH2 . ARG B 106 ? 1.0910 0.9150 0.9048 0.0848 -0.0457 -0.0193 106 ARG B NH2 3395 N N . THR B 107 ? 0.5335 0.5505 0.5685 -0.0074 -0.0223 -0.0263 107 THR B N 3396 C CA . THR B 107 ? 0.5014 0.5332 0.5410 -0.0054 -0.0209 -0.0323 107 THR B CA 3397 C C . THR B 107 ? 0.4913 0.5199 0.5360 0.0021 -0.0241 -0.0308 107 THR B C 3398 O O . THR B 107 ? 0.4727 0.5119 0.5216 0.0041 -0.0224 -0.0329 107 THR B O 3399 C CB . THR B 107 ? 0.5008 0.5478 0.5363 0.0014 -0.0212 -0.0390 107 THR B CB 3400 O OG1 . THR B 107 ? 0.5075 0.5714 0.5394 -0.0106 -0.0168 -0.0388 107 THR B OG1 3401 C CG2 . THR B 107 ? 0.5118 0.5852 0.5479 0.0151 -0.0211 -0.0457 107 THR B CG2 3402 N N . LEU B 108 ? 0.4900 0.5037 0.5297 0.0015 -0.0303 -0.0259 108 LEU B N 3403 C CA . LEU B 108 ? 0.5084 0.5152 0.5452 0.0011 -0.0351 -0.0209 108 LEU B CA 3404 C C . LEU B 108 ? 0.4944 0.5221 0.5447 0.0011 -0.0305 -0.0152 108 LEU B C 3405 O O . LEU B 108 ? 0.4793 0.5105 0.5320 0.0057 -0.0301 -0.0156 108 LEU B O 3406 C CB . LEU B 108 ? 0.5288 0.5141 0.5476 -0.0125 -0.0456 -0.0126 108 LEU B CB 3407 C CG . LEU B 108 ? 0.5721 0.5178 0.5606 -0.0081 -0.0544 -0.0195 108 LEU B CG 3408 C CD1 . LEU B 108 ? 0.6225 0.5314 0.5783 -0.0314 -0.0698 -0.0092 108 LEU B CD1 3409 C CD2 . LEU B 108 ? 0.5988 0.5278 0.5689 0.0171 -0.0561 -0.0311 108 LEU B CD2 3410 N N . ASP B 109 ? 0.4749 0.5149 0.5275 0.0016 -0.0281 -0.0110 109 ASP B N 3411 C CA . ASP B 109 ? 0.4754 0.5304 0.5274 0.0130 -0.0255 -0.0079 109 ASP B CA 3412 C C . ASP B 109 ? 0.4734 0.5090 0.5165 0.0181 -0.0230 -0.0164 109 ASP B C 3413 O O . ASP B 109 ? 0.4900 0.5289 0.5291 0.0273 -0.0230 -0.0161 109 ASP B O 3414 C CB . ASP B 109 ? 0.4912 0.5593 0.5342 0.0235 -0.0255 -0.0038 109 ASP B CB 3415 C CG . ASP B 109 ? 0.5241 0.6358 0.5768 0.0146 -0.0290 0.0082 109 ASP B CG 3416 O OD1 . ASP B 109 ? 0.5283 0.6615 0.5884 0.0013 -0.0320 0.0165 109 ASP B OD1 3417 O OD2 . ASP B 109 ? 0.5694 0.6958 0.6179 0.0174 -0.0300 0.0108 109 ASP B OD2 3418 N N . PHE B 110 ? 0.4616 0.4816 0.4982 0.0087 -0.0220 -0.0227 110 PHE B N 3419 C CA . PHE B 110 ? 0.4487 0.4565 0.4712 0.0003 -0.0221 -0.0281 110 PHE B CA 3420 C C . PHE B 110 ? 0.4431 0.4720 0.4804 0.0015 -0.0214 -0.0309 110 PHE B C 3421 O O . PHE B 110 ? 0.4793 0.5007 0.5060 0.0018 -0.0231 -0.0323 110 PHE B O 3422 C CB . PHE B 110 ? 0.4512 0.4607 0.4674 -0.0174 -0.0212 -0.0306 110 PHE B CB 3423 C CG . PHE B 110 ? 0.4650 0.4772 0.4647 -0.0396 -0.0231 -0.0327 110 PHE B CG 3424 C CD1 . PHE B 110 ? 0.5076 0.4747 0.4687 -0.0488 -0.0297 -0.0317 110 PHE B CD1 3425 C CD2 . PHE B 110 ? 0.4504 0.5123 0.4648 -0.0515 -0.0202 -0.0352 110 PHE B CD2 3426 C CE1 . PHE B 110 ? 0.5384 0.5046 0.4756 -0.0805 -0.0347 -0.0315 110 PHE B CE1 3427 C CE2 . PHE B 110 ? 0.4707 0.5551 0.4708 -0.0801 -0.0227 -0.0343 110 PHE B CE2 3428 C CZ . PHE B 110 ? 0.5153 0.5487 0.4762 -0.1005 -0.0307 -0.0316 110 PHE B CZ 3429 N N . HIS B 111 ? 0.4226 0.4703 0.4755 0.0056 -0.0208 -0.0322 111 HIS B N 3430 C CA . HIS B 111 ? 0.4151 0.4778 0.4747 0.0141 -0.0217 -0.0348 111 HIS B CA 3431 C C . HIS B 111 ? 0.4236 0.4797 0.4849 0.0204 -0.0229 -0.0290 111 HIS B C 3432 O O . HIS B 111 ? 0.4361 0.5011 0.4987 0.0244 -0.0229 -0.0312 111 HIS B O 3433 C CB . HIS B 111 ? 0.4213 0.4822 0.4769 0.0259 -0.0249 -0.0372 111 HIS B CB 3434 C CG . HIS B 111 ? 0.4262 0.5131 0.4793 0.0305 -0.0232 -0.0449 111 HIS B CG 3435 N ND1 . HIS B 111 ? 0.4174 0.5517 0.4755 0.0311 -0.0204 -0.0504 111 HIS B ND1 3436 C CD2 . HIS B 111 ? 0.4286 0.5116 0.4731 0.0354 -0.0244 -0.0475 111 HIS B CD2 3437 C CE1 . HIS B 111 ? 0.4284 0.5973 0.4833 0.0368 -0.0189 -0.0550 111 HIS B CE1 3438 N NE2 . HIS B 111 ? 0.4339 0.5673 0.4795 0.0420 -0.0212 -0.0542 111 HIS B NE2 3439 N N . ASP B 112 ? 0.4081 0.4591 0.4693 0.0202 -0.0243 -0.0206 112 ASP B N 3440 C CA . ASP B 112 ? 0.4103 0.4743 0.4734 0.0248 -0.0250 -0.0124 112 ASP B CA 3441 C C . ASP B 112 ? 0.4308 0.4947 0.4855 0.0361 -0.0230 -0.0163 112 ASP B C 3442 O O . ASP B 112 ? 0.4591 0.5311 0.5137 0.0433 -0.0230 -0.0161 112 ASP B O 3443 C CB . ASP B 112 ? 0.4153 0.4960 0.4792 0.0187 -0.0269 -0.0010 112 ASP B CB 3444 C CG . ASP B 112 ? 0.4135 0.5282 0.4799 0.0172 -0.0283 0.0115 112 ASP B CG 3445 O OD1 . ASP B 112 ? 0.4167 0.5293 0.4830 0.0202 -0.0285 0.0113 112 ASP B OD1 3446 O OD2 . ASP B 112 ? 0.4210 0.5743 0.4894 0.0122 -0.0293 0.0227 112 ASP B OD2 3447 N N . SER B 113 ? 0.4380 0.4824 0.4758 0.0383 -0.0233 -0.0202 113 SER B N 3448 C CA . SER B 113 ? 0.4713 0.4877 0.4780 0.0485 -0.0264 -0.0254 113 SER B CA 3449 C C . SER B 113 ? 0.4942 0.4999 0.4955 0.0357 -0.0285 -0.0323 113 SER B C 3450 O O . SER B 113 ? 0.5114 0.5012 0.4909 0.0452 -0.0323 -0.0352 113 SER B O 3451 C CB . SER B 113 ? 0.4992 0.4766 0.4737 0.0477 -0.0299 -0.0279 113 SER B CB 3452 O OG . SER B 113 ? 0.5601 0.4838 0.4847 0.0500 -0.0378 -0.0338 113 SER B OG 3453 N N . ASN B 114 ? 0.4808 0.5019 0.4981 0.0166 -0.0267 -0.0350 114 ASN B N 3454 C CA . ASN B 114 ? 0.4915 0.5238 0.5055 0.0025 -0.0289 -0.0403 114 ASN B CA 3455 C C . ASN B 114 ? 0.4578 0.5139 0.4891 0.0168 -0.0275 -0.0404 114 ASN B C 3456 O O . ASN B 114 ? 0.4656 0.5225 0.4858 0.0121 -0.0309 -0.0442 114 ASN B O 3457 C CB . ASN B 114 ? 0.4881 0.5550 0.5147 -0.0155 -0.0270 -0.0426 114 ASN B CB 3458 C CG . ASN B 114 ? 0.5239 0.5695 0.5273 -0.0382 -0.0295 -0.0411 114 ASN B CG 3459 O OD1 . ASN B 114 ? 0.5701 0.5631 0.5330 -0.0486 -0.0365 -0.0402 114 ASN B OD1 3460 N ND2 . ASN B 114 ? 0.5265 0.6060 0.5460 -0.0436 -0.0254 -0.0410 114 ASN B ND2 3461 N N . VAL B 115 ? 0.4377 0.5074 0.4888 0.0305 -0.0245 -0.0353 115 VAL B N 3462 C CA . VAL B 115 ? 0.4383 0.5218 0.4977 0.0423 -0.0246 -0.0327 115 VAL B CA 3463 C C . VAL B 115 ? 0.4472 0.5250 0.4959 0.0529 -0.0252 -0.0294 115 VAL B C 3464 O O . VAL B 115 ? 0.4411 0.5254 0.4869 0.0590 -0.0263 -0.0316 115 VAL B O 3465 C CB . VAL B 115 ? 0.4516 0.5343 0.5171 0.0461 -0.0254 -0.0251 115 VAL B CB 3466 C CG1 . VAL B 115 ? 0.4752 0.5626 0.5388 0.0534 -0.0273 -0.0188 115 VAL B CG1 3467 C CG2 . VAL B 115 ? 0.4665 0.5487 0.5297 0.0486 -0.0271 -0.0312 115 VAL B CG2 3468 N N . LYS B 116 ? 0.4670 0.5385 0.5071 0.0598 -0.0248 -0.0248 116 LYS B N 3469 C CA . LYS B 116 ? 0.4973 0.5730 0.5200 0.0811 -0.0259 -0.0226 116 LYS B CA 3470 C C . LYS B 116 ? 0.5350 0.5712 0.5219 0.0867 -0.0319 -0.0333 116 LYS B C 3471 O O . LYS B 116 ? 0.5360 0.5755 0.5101 0.1035 -0.0338 -0.0348 116 LYS B O 3472 C CB . LYS B 116 ? 0.5215 0.6067 0.5358 0.0938 -0.0253 -0.0170 116 LYS B CB 3473 C CG . LYS B 116 ? 0.5552 0.6605 0.5458 0.1281 -0.0265 -0.0150 116 LYS B CG 3474 C CD . LYS B 116 ? 0.5923 0.7488 0.6019 0.1323 -0.0234 -0.0064 116 LYS B CD 3475 C CE . LYS B 116 ? 0.6422 0.8498 0.6344 0.1695 -0.0229 -0.0011 116 LYS B CE 3476 N NZ . LYS B 116 ? 0.6367 0.9055 0.6426 0.1695 -0.0202 0.0115 116 LYS B NZ 3477 N N . ASN B 117 ? 0.5661 0.5623 0.5303 0.0690 -0.0366 -0.0399 117 ASN B N 3478 C CA . ASN B 117 ? 0.6357 0.5786 0.5495 0.0623 -0.0472 -0.0482 117 ASN B CA 3479 C C . ASN B 117 ? 0.6360 0.5990 0.5616 0.0459 -0.0486 -0.0519 117 ASN B C 3480 O O . ASN B 117 ? 0.6754 0.6053 0.5625 0.0488 -0.0573 -0.0574 117 ASN B O 3481 C CB . ASN B 117 ? 0.6699 0.5646 0.5488 0.0362 -0.0540 -0.0504 117 ASN B CB 3482 C CG . ASN B 117 ? 0.7134 0.5744 0.5640 0.0589 -0.0557 -0.0486 117 ASN B CG 3483 O OD1 . ASN B 117 ? 0.7292 0.5947 0.5683 0.0983 -0.0552 -0.0479 117 ASN B OD1 3484 N ND2 . ASN B 117 ? 0.7329 0.5702 0.5716 0.0362 -0.0575 -0.0472 117 ASN B ND2 3485 N N . LEU B 118 ? 0.5944 0.6093 0.5659 0.0327 -0.0415 -0.0496 118 LEU B N 3486 C CA . LEU B 118 ? 0.5911 0.6401 0.5770 0.0250 -0.0420 -0.0529 118 LEU B CA 3487 C C . LEU B 118 ? 0.5857 0.6436 0.5775 0.0515 -0.0402 -0.0511 118 LEU B C 3488 O O . LEU B 118 ? 0.6093 0.6640 0.5853 0.0512 -0.0454 -0.0559 118 LEU B O 3489 C CB . LEU B 118 ? 0.5676 0.6689 0.5911 0.0202 -0.0358 -0.0518 118 LEU B CB 3490 C CG . LEU B 118 ? 0.5645 0.7151 0.6006 0.0179 -0.0366 -0.0560 118 LEU B CG 3491 C CD1 . LEU B 118 ? 0.6125 0.7666 0.6227 -0.0145 -0.0451 -0.0602 118 LEU B CD1 3492 C CD2 . LEU B 118 ? 0.5489 0.7457 0.6075 0.0257 -0.0322 -0.0566 118 LEU B CD2 3493 N N . TYR B 119 ? 0.5507 0.6229 0.5618 0.0704 -0.0340 -0.0429 119 TYR B N 3494 C CA . TYR B 119 ? 0.5346 0.6257 0.5501 0.0912 -0.0320 -0.0373 119 TYR B CA 3495 C C . TYR B 119 ? 0.5857 0.6511 0.5627 0.1107 -0.0375 -0.0424 119 TYR B C 3496 O O . TYR B 119 ? 0.6087 0.6800 0.5775 0.1212 -0.0396 -0.0449 119 TYR B O 3497 C CB . TYR B 119 ? 0.4979 0.6141 0.5326 0.0964 -0.0267 -0.0241 119 TYR B CB 3498 C CG . TYR B 119 ? 0.4966 0.6460 0.5343 0.1104 -0.0248 -0.0141 119 TYR B CG 3499 C CD1 . TYR B 119 ? 0.4973 0.6591 0.5454 0.1054 -0.0247 -0.0087 119 TYR B CD1 3500 C CD2 . TYR B 119 ? 0.5002 0.6730 0.5249 0.1316 -0.0238 -0.0093 119 TYR B CD2 3501 C CE1 . TYR B 119 ? 0.4955 0.6899 0.5432 0.1127 -0.0234 0.0031 119 TYR B CE1 3502 C CE2 . TYR B 119 ? 0.5098 0.7307 0.5382 0.1429 -0.0214 0.0018 119 TYR B CE2 3503 C CZ . TYR B 119 ? 0.5078 0.7380 0.5487 0.1292 -0.0211 0.0089 119 TYR B CZ 3504 O OH . TYR B 119 ? 0.5165 0.7961 0.5578 0.1353 -0.0192 0.0223 119 TYR B OH 3505 N N . ASP B 120 ? 0.6250 0.6563 0.5702 0.1205 -0.0412 -0.0448 120 ASP B N 3506 C CA . ASP B 120 ? 0.6901 0.6815 0.5796 0.1497 -0.0498 -0.0518 120 ASP B CA 3507 C C . ASP B 120 ? 0.7360 0.6736 0.5845 0.1325 -0.0618 -0.0630 120 ASP B C 3508 O O . ASP B 120 ? 0.7733 0.6941 0.5892 0.1535 -0.0681 -0.0684 120 ASP B O 3509 C CB . ASP B 120 ? 0.7375 0.6912 0.5867 0.1694 -0.0543 -0.0534 120 ASP B CB 3510 C CG . ASP B 120 ? 0.7245 0.7476 0.6067 0.1921 -0.0442 -0.0415 120 ASP B CG 3511 O OD1 . ASP B 120 ? 0.7332 0.8217 0.6437 0.2043 -0.0376 -0.0329 120 ASP B OD1 3512 O OD2 . ASP B 120 ? 0.7317 0.7491 0.6097 0.1940 -0.0436 -0.0393 120 ASP B OD2 3513 N N . LYS B 121 ? 0.7589 0.6776 0.6076 0.0918 -0.0657 -0.0654 121 LYS B N 3514 C CA . LYS B 121 ? 0.8418 0.7227 0.6513 0.0607 -0.0788 -0.0730 121 LYS B CA 3515 C C . LYS B 121 ? 0.8168 0.7394 0.6486 0.0667 -0.0769 -0.0748 121 LYS B C 3516 O O . LYS B 121 ? 0.8902 0.7697 0.6720 0.0669 -0.0895 -0.0821 121 LYS B O 3517 C CB . LYS B 121 ? 0.8716 0.7718 0.6993 0.0127 -0.0788 -0.0706 121 LYS B CB 3518 C CG . LYS B 121 ? 0.9551 0.8471 0.7518 -0.0334 -0.0919 -0.0742 121 LYS B CG 3519 C CD . LYS B 121 ? 1.0032 0.9235 0.8108 -0.0792 -0.0918 -0.0692 121 LYS B CD 3520 C CE . LYS B 121 ? 1.0864 1.0439 0.8806 -0.1322 -0.1020 -0.0688 121 LYS B CE 3521 N NZ . LYS B 121 ? 1.0646 1.1340 0.9273 -0.1214 -0.0901 -0.0690 121 LYS B NZ 3522 N N . VAL B 122 ? 0.7205 0.7173 0.6183 0.0728 -0.0632 -0.0682 122 VAL B N 3523 C CA . VAL B 122 ? 0.6919 0.7285 0.6106 0.0832 -0.0606 -0.0684 122 VAL B CA 3524 C C . VAL B 122 ? 0.7218 0.7477 0.6202 0.1217 -0.0606 -0.0677 122 VAL B C 3525 O O . VAL B 122 ? 0.7609 0.7783 0.6363 0.1297 -0.0670 -0.0734 122 VAL B O 3526 C CB . VAL B 122 ? 0.6231 0.7224 0.5994 0.0842 -0.0492 -0.0610 122 VAL B CB 3527 C CG1 . VAL B 122 ? 0.6027 0.7335 0.5932 0.1029 -0.0465 -0.0585 122 VAL B CG1 3528 C CG2 . VAL B 122 ? 0.6123 0.7393 0.6022 0.0556 -0.0505 -0.0644 122 VAL B CG2 3529 N N . ARG B 123 ? 0.6993 0.7347 0.6043 0.1458 -0.0541 -0.0604 123 ARG B N 3530 C CA . ARG B 123 ? 0.7367 0.7863 0.6236 0.1862 -0.0530 -0.0579 123 ARG B CA 3531 C C . ARG B 123 ? 0.8209 0.8016 0.6326 0.2076 -0.0680 -0.0719 123 ARG B C 3532 O O . ARG B 123 ? 0.8434 0.8324 0.6371 0.2325 -0.0705 -0.0750 123 ARG B O 3533 C CB . ARG B 123 ? 0.7426 0.8229 0.6409 0.2050 -0.0458 -0.0479 123 ARG B CB 3534 C CG . ARG B 123 ? 0.7681 0.9049 0.6630 0.2443 -0.0413 -0.0401 123 ARG B CG 3535 C CD . ARG B 123 ? 0.7786 0.9656 0.6865 0.2574 -0.0348 -0.0284 123 ARG B CD 3536 N NE . ARG B 123 ? 0.8179 0.9479 0.6915 0.2640 -0.0411 -0.0374 123 ARG B NE 3537 C CZ . ARG B 123 ? 0.8997 0.9732 0.7031 0.3041 -0.0520 -0.0502 123 ARG B CZ 3538 N NH1 . ARG B 123 ? 0.9453 1.0127 0.7037 0.3458 -0.0581 -0.0575 123 ARG B NH1 3539 N NH2 . ARG B 123 ? 0.9280 0.9422 0.6962 0.3054 -0.0587 -0.0563 123 ARG B NH2 3540 N N . LEU B 124 ? 0.8803 0.7843 0.6393 0.1965 -0.0799 -0.0801 124 LEU B N 3541 C CA . LEU B 124 ? 0.9890 0.7961 0.6513 0.2144 -0.1000 -0.0938 124 LEU B CA 3542 C C . LEU B 124 ? 1.0357 0.8104 0.6711 0.1854 -0.1124 -0.1019 124 LEU B C 3543 O O . LEU B 124 ? 1.1358 0.8362 0.6898 0.2065 -0.1295 -0.1130 124 LEU B O 3544 C CB . LEU B 124 ? 1.0501 0.7693 0.6519 0.2010 -0.1125 -0.0981 124 LEU B CB 3545 C CG . LEU B 124 ? 1.0606 0.7985 0.6671 0.2395 -0.1046 -0.0929 124 LEU B CG 3546 C CD1 . LEU B 124 ? 1.1146 0.7828 0.6850 0.2125 -0.1129 -0.0936 124 LEU B CD1 3547 C CD2 . LEU B 124 ? 1.1256 0.8436 0.6668 0.3122 -0.1114 -0.0998 124 LEU B CD2 3548 N N . GLN B 125 ? 0.9820 0.8119 0.6781 0.1404 -0.1055 -0.0971 125 GLN B N 3549 C CA . GLN B 125 ? 1.0099 0.8371 0.6920 0.1131 -0.1154 -0.1031 125 GLN B CA 3550 C C . GLN B 125 ? 0.9707 0.8490 0.6792 0.1495 -0.1076 -0.1025 125 GLN B C 3551 O O . GLN B 125 ? 1.0477 0.8827 0.7006 0.1641 -0.1206 -0.1117 125 GLN B O 3552 C CB . GLN B 125 ? 0.9697 0.8605 0.7084 0.0627 -0.1098 -0.0980 125 GLN B CB 3553 C CG . GLN B 125 ? 1.0172 0.8728 0.7306 0.0161 -0.1182 -0.0968 125 GLN B CG 3554 C CD . GLN B 125 ? 0.9981 0.9318 0.7551 -0.0315 -0.1160 -0.0932 125 GLN B CD 3555 O OE1 . GLN B 125 ? 1.0683 1.0089 0.8004 -0.0627 -0.1283 -0.0969 125 GLN B OE1 3556 N NE2 . GLN B 125 ? 0.9283 0.9274 0.7467 -0.0344 -0.1011 -0.0864 125 GLN B NE2 3557 N N . LEU B 126 ? 0.8721 0.8355 0.6573 0.1623 -0.0883 -0.0911 126 LEU B N 3558 C CA . LEU B 126 ? 0.8626 0.8811 0.6765 0.1884 -0.0802 -0.0866 126 LEU B CA 3559 C C . LEU B 126 ? 0.9390 0.9410 0.7088 0.2388 -0.0830 -0.0892 126 LEU B C 3560 O O . LEU B 126 ? 0.9838 0.9933 0.7368 0.2580 -0.0864 -0.0932 126 LEU B O 3561 C CB . LEU B 126 ? 0.7736 0.8667 0.6603 0.1862 -0.0629 -0.0713 126 LEU B CB 3562 C CG . LEU B 126 ? 0.7174 0.8338 0.6422 0.1511 -0.0602 -0.0700 126 LEU B CG 3563 C CD1 . LEU B 126 ? 0.6681 0.8343 0.6406 0.1569 -0.0483 -0.0567 126 LEU B CD1 3564 C CD2 . LEU B 126 ? 0.7415 0.8619 0.6543 0.1307 -0.0695 -0.0797 126 LEU B CD2 3565 N N . ARG B 127 ? 1.0376 1.0229 0.7850 0.2645 -0.0820 -0.0877 127 ARG B N 3566 C CA . ARG B 127 ? 1.1184 1.1063 0.8207 0.3236 -0.0842 -0.0902 127 ARG B CA 3567 C C . ARG B 127 ? 1.0712 1.1587 0.8241 0.3416 -0.0699 -0.0770 127 ARG B C 3568 O O . ARG B 127 ? 1.0141 1.1696 0.8345 0.3178 -0.0559 -0.0605 127 ARG B O 3569 C CB . ARG B 127 ? 1.2445 1.1262 0.8441 0.3448 -0.1071 -0.1098 127 ARG B CB 3570 C CG . ARG B 127 ? 1.3365 1.1071 0.8667 0.3261 -0.1244 -0.1196 127 ARG B CG 3571 C CD . ARG B 127 ? 1.4568 1.1075 0.8891 0.3080 -0.1514 -0.1359 127 ARG B CD 3572 N NE . ARG B 127 ? 1.5806 1.1798 0.9262 0.3706 -0.1653 -0.1486 127 ARG B NE 3573 C CZ . ARG B 127 ? 1.7415 1.2121 0.9721 0.3689 -0.1940 -0.1647 127 ARG B CZ 3574 N NH1 . ARG B 127 ? 1.8162 1.2028 1.0065 0.2981 -0.2124 -0.1676 127 ARG B NH1 3575 N NH2 . ARG B 127 ? 1.8124 1.2390 0.9608 0.4369 -0.2062 -0.1774 127 ARG B NH2 3576 N N . ASP B 128 ? 1.1238 1.2134 0.8374 0.3802 -0.0753 -0.0835 128 ASP B N 3577 C CA . ASP B 128 ? 1.0881 1.2764 0.8435 0.3965 -0.0623 -0.0688 128 ASP B CA 3578 C C . ASP B 128 ? 1.0276 1.2268 0.8138 0.3674 -0.0611 -0.0673 128 ASP B C 3579 O O . ASP B 128 ? 1.0393 1.3000 0.8402 0.3842 -0.0545 -0.0581 128 ASP B O 3580 C CB . ASP B 128 ? 1.1746 1.3869 0.8747 0.4643 -0.0658 -0.0737 128 ASP B CB 3581 C CG . ASP B 128 ? 1.3022 1.4217 0.9205 0.4902 -0.0850 -0.0965 128 ASP B CG 3582 O OD1 . ASP B 128 ? 1.3120 1.3569 0.9202 0.4476 -0.0958 -0.1066 128 ASP B OD1 3583 O OD2 . ASP B 128 ? 1.4251 1.5505 0.9836 0.5541 -0.0908 -0.1041 128 ASP B OD2 3584 N N . ASN B 129 ? 0.9897 1.1387 0.7838 0.3254 -0.0675 -0.0753 129 ASN B N 3585 C CA . ASN B 129 ? 0.9414 1.1147 0.7702 0.2996 -0.0655 -0.0729 129 ASN B CA 3586 C C . ASN B 129 ? 0.8650 1.0924 0.7585 0.2743 -0.0521 -0.0548 129 ASN B C 3587 O O . ASN B 129 ? 0.8477 1.0889 0.7634 0.2578 -0.0516 -0.0536 129 ASN B O 3588 C CB . ASN B 129 ? 0.9912 1.1057 0.7956 0.2666 -0.0797 -0.0888 129 ASN B CB 3589 C CG . ASN B 129 ? 1.1044 1.1529 0.8321 0.2828 -0.0980 -0.1060 129 ASN B CG 3590 O OD1 . ASN B 129 ? 1.1989 1.2351 0.8841 0.3290 -0.1006 -0.1094 129 ASN B OD1 3591 N ND2 . ASN B 129 ? 1.1340 1.1420 0.8367 0.2446 -0.1125 -0.1168 129 ASN B ND2 3592 N N . ALA B 130 ? 0.8236 1.0767 0.7378 0.2732 -0.0435 -0.0413 130 ALA B N 3593 C CA . ALA B 130 ? 0.7527 1.0359 0.7099 0.2472 -0.0352 -0.0240 130 ALA B CA 3594 C C . ALA B 130 ? 0.7429 1.0748 0.7108 0.2510 -0.0273 -0.0049 130 ALA B C 3595 O O . ALA B 130 ? 0.7653 1.1063 0.7145 0.2739 -0.0274 -0.0083 130 ALA B O 3596 C CB . ALA B 130 ? 0.7313 0.9775 0.7013 0.2199 -0.0376 -0.0313 130 ALA B CB 3597 N N . LYS B 131 ? 0.7209 1.0826 0.7101 0.2281 -0.0228 0.0157 131 LYS B N 3598 C CA . LYS B 131 ? 0.7125 1.1293 0.7104 0.2171 -0.0174 0.0378 131 LYS B CA 3599 C C . LYS B 131 ? 0.6774 1.0657 0.6878 0.1911 -0.0180 0.0398 131 LYS B C 3600 O O . LYS B 131 ? 0.6597 1.0023 0.6751 0.1682 -0.0213 0.0395 131 LYS B O 3601 C CB . LYS B 131 ? 0.7638 1.2191 0.7629 0.1951 -0.0162 0.0630 131 LYS B CB 3602 C CG . LYS B 131 ? 0.8568 1.3351 0.8445 0.2179 -0.0158 0.0615 131 LYS B CG 3603 C CD . LYS B 131 ? 0.9257 1.4678 0.9082 0.1985 -0.0135 0.0912 131 LYS B CD 3604 C CE . LYS B 131 ? 0.9533 1.5995 0.9353 0.2225 -0.0067 0.1010 131 LYS B CE 3605 N NZ . LYS B 131 ? 0.9746 1.7047 0.9528 0.1923 -0.0044 0.1353 131 LYS B NZ 3606 N N . GLU B 132 ? 0.6372 1.0540 0.6481 0.2002 -0.0154 0.0409 132 GLU B N 3607 C CA . GLU B 132 ? 0.6043 1.0039 0.6269 0.1754 -0.0156 0.0450 132 GLU B CA 3608 C C . GLU B 132 ? 0.5936 1.0304 0.6223 0.1367 -0.0157 0.0728 132 GLU B C 3609 O O . GLU B 132 ? 0.5966 1.1149 0.6264 0.1335 -0.0125 0.0914 132 GLU B O 3610 C CB . GLU B 132 ? 0.6075 1.0275 0.6224 0.2009 -0.0139 0.0379 132 GLU B CB 3611 C CG . GLU B 132 ? 0.6107 0.9990 0.6357 0.1797 -0.0148 0.0362 132 GLU B CG 3612 C CD . GLU B 132 ? 0.6390 1.0334 0.6475 0.2101 -0.0148 0.0268 132 GLU B CD 3613 O OE1 . GLU B 132 ? 0.6726 1.1007 0.6562 0.2528 -0.0148 0.0225 132 GLU B OE1 3614 O OE2 . GLU B 132 ? 0.6501 1.0117 0.6638 0.1957 -0.0159 0.0231 132 GLU B OE2 3615 N N . LEU B 133 ? 0.5932 0.9703 0.6170 0.1074 -0.0215 0.0763 133 LEU B N 3616 C CA . LEU B 133 ? 0.6170 0.9980 0.6245 0.0651 -0.0274 0.1030 133 LEU B CA 3617 C C . LEU B 133 ? 0.6371 1.0444 0.6469 0.0342 -0.0290 0.1177 133 LEU B C 3618 O O . LEU B 133 ? 0.6764 1.1157 0.6692 -0.0071 -0.0344 0.1449 133 LEU B O 3619 C CB . LEU B 133 ? 0.6423 0.9326 0.6244 0.0532 -0.0368 0.0997 133 LEU B CB 3620 C CG . LEU B 133 ? 0.6459 0.9196 0.6198 0.0770 -0.0372 0.0914 133 LEU B CG 3621 C CD1 . LEU B 133 ? 0.6857 0.8735 0.6260 0.0743 -0.0480 0.0875 133 LEU B CD1 3622 C CD2 . LEU B 133 ? 0.6601 0.9917 0.6246 0.0679 -0.0358 0.1128 133 LEU B CD2 3623 N N . GLY B 134 ? 0.6319 1.0250 0.6578 0.0488 -0.0260 0.1014 134 GLY B N 3624 C CA . GLY B 134 ? 0.6422 1.0670 0.6731 0.0250 -0.0270 0.1128 134 GLY B CA 3625 C C . GLY B 134 ? 0.6595 1.0038 0.6750 -0.0054 -0.0361 0.1124 134 GLY B C 3626 O O . GLY B 134 ? 0.6705 1.0338 0.6848 -0.0325 -0.0393 0.1236 134 GLY B O 3627 N N . ASN B 135 ? 0.6639 0.9238 0.6641 0.0028 -0.0410 0.0988 135 ASN B N 3628 C CA . ASN B 135 ? 0.6955 0.8733 0.6690 -0.0151 -0.0514 0.0963 135 ASN B CA 3629 C C . ASN B 135 ? 0.6584 0.7928 0.6449 0.0182 -0.0480 0.0687 135 ASN B C 3630 O O . ASN B 135 ? 0.6762 0.7451 0.6369 0.0182 -0.0562 0.0622 135 ASN B O 3631 C CB . ASN B 135 ? 0.7703 0.8849 0.6909 -0.0379 -0.0656 0.1108 135 ASN B CB 3632 C CG . ASN B 135 ? 0.7952 0.8903 0.7116 -0.0054 -0.0638 0.0994 135 ASN B CG 3633 O OD1 . ASN B 135 ? 0.7461 0.8878 0.7010 0.0262 -0.0520 0.0844 135 ASN B OD1 3634 N ND2 . ASN B 135 ? 0.8942 0.9135 0.7547 -0.0126 -0.0778 0.1066 135 ASN B ND2 3635 N N . GLY B 136 ? 0.6104 0.7821 0.6286 0.0460 -0.0376 0.0533 136 GLY B N 3636 C CA . GLY B 136 ? 0.5962 0.7421 0.6246 0.0682 -0.0352 0.0304 136 GLY B CA 3637 C C . GLY B 136 ? 0.5812 0.7284 0.6092 0.0888 -0.0345 0.0204 136 GLY B C 3638 O O . GLY B 136 ? 0.5525 0.6971 0.5895 0.1018 -0.0329 0.0033 136 GLY B O 3639 N N . CYS B 137 ? 0.6094 0.7664 0.6249 0.0877 -0.0365 0.0325 137 CYS B N 3640 C CA . CYS B 137 ? 0.6514 0.8076 0.6626 0.1074 -0.0372 0.0241 137 CYS B CA 3641 C C . CYS B 137 ? 0.6322 0.8326 0.6549 0.1196 -0.0317 0.0235 137 CYS B C 3642 O O . CYS B 137 ? 0.6188 0.8564 0.6448 0.1151 -0.0283 0.0357 137 CYS B O 3643 C CB . CYS B 137 ? 0.7055 0.8236 0.6809 0.1035 -0.0462 0.0358 137 CYS B CB 3644 S SG . CYS B 137 ? 0.7992 0.8444 0.7370 0.1028 -0.0574 0.0328 137 CYS B SG 3645 N N . PHE B 138 ? 0.6305 0.8318 0.6550 0.1374 -0.0320 0.0088 138 PHE B N 3646 C CA . PHE B 138 ? 0.6211 0.8498 0.6456 0.1532 -0.0298 0.0046 138 PHE B CA 3647 C C . PHE B 138 ? 0.6529 0.8828 0.6679 0.1625 -0.0327 0.0059 138 PHE B C 3648 O O . PHE B 138 ? 0.6526 0.8689 0.6659 0.1681 -0.0363 -0.0048 138 PHE B O 3649 C CB . PHE B 138 ? 0.6023 0.8209 0.6265 0.1599 -0.0311 -0.0153 138 PHE B CB 3650 C CG . PHE B 138 ? 0.5980 0.8068 0.6205 0.1564 -0.0298 -0.0173 138 PHE B CG 3651 C CD1 . PHE B 138 ? 0.5903 0.8148 0.5991 0.1745 -0.0284 -0.0147 138 PHE B CD1 3652 C CD2 . PHE B 138 ? 0.5988 0.7866 0.6289 0.1406 -0.0303 -0.0220 138 PHE B CD2 3653 C CE1 . PHE B 138 ? 0.5949 0.8083 0.5942 0.1788 -0.0283 -0.0172 138 PHE B CE1 3654 C CE2 . PHE B 138 ? 0.5890 0.7643 0.6137 0.1387 -0.0296 -0.0234 138 PHE B CE2 3655 C CZ . PHE B 138 ? 0.5956 0.7812 0.6035 0.1587 -0.0290 -0.0211 138 PHE B CZ 3656 N N . GLU B 139 ? 0.6876 0.9429 0.6951 0.1661 -0.0312 0.0196 139 GLU B N 3657 C CA . GLU B 139 ? 0.7162 0.9723 0.7107 0.1760 -0.0341 0.0225 139 GLU B CA 3658 C C . GLU B 139 ? 0.7056 0.9869 0.7026 0.1974 -0.0327 0.0090 139 GLU B C 3659 O O . GLU B 139 ? 0.7099 1.0201 0.7049 0.2073 -0.0293 0.0116 139 GLU B O 3660 C CB . GLU B 139 ? 0.7772 1.0439 0.7543 0.1601 -0.0349 0.0488 139 GLU B CB 3661 C CG . GLU B 139 ? 0.8502 1.1030 0.8032 0.1674 -0.0398 0.0552 139 GLU B CG 3662 C CD . GLU B 139 ? 0.9458 1.2085 0.8735 0.1414 -0.0424 0.0850 139 GLU B CD 3663 O OE1 . GLU B 139 ? 1.0212 1.2472 0.9249 0.1107 -0.0491 0.1011 139 GLU B OE1 3664 O OE2 . GLU B 139 ? 1.0148 1.3234 0.9419 0.1480 -0.0389 0.0934 139 GLU B OE2 3665 N N . PHE B 140 ? 0.7099 0.9827 0.7051 0.2070 -0.0370 -0.0057 140 PHE B N 3666 C CA . PHE B 140 ? 0.7147 1.0001 0.7039 0.2209 -0.0395 -0.0204 140 PHE B CA 3667 C C . PHE B 140 ? 0.7404 1.0503 0.7185 0.2374 -0.0383 -0.0119 140 PHE B C 3668 O O . PHE B 140 ? 0.7191 1.0329 0.6927 0.2362 -0.0377 0.0032 140 PHE B O 3669 C CB . PHE B 140 ? 0.6951 0.9804 0.6866 0.2188 -0.0454 -0.0365 140 PHE B CB 3670 C CG . PHE B 140 ? 0.6803 0.9548 0.6797 0.2007 -0.0472 -0.0466 140 PHE B CG 3671 C CD1 . PHE B 140 ? 0.6965 0.9563 0.6822 0.1889 -0.0526 -0.0593 140 PHE B CD1 3672 C CD2 . PHE B 140 ? 0.6677 0.9394 0.6781 0.1955 -0.0457 -0.0432 140 PHE B CD2 3673 C CE1 . PHE B 140 ? 0.6976 0.9471 0.6854 0.1660 -0.0554 -0.0662 140 PHE B CE1 3674 C CE2 . PHE B 140 ? 0.6606 0.9319 0.6790 0.1788 -0.0467 -0.0516 140 PHE B CE2 3675 C CZ . PHE B 140 ? 0.6795 0.9432 0.6891 0.1610 -0.0510 -0.0619 140 PHE B CZ 3676 N N . TYR B 141 ? 0.7732 1.0915 0.7373 0.2538 -0.0399 -0.0215 141 TYR B N 3677 C CA . TYR B 141 ? 0.8145 1.1608 0.7658 0.2740 -0.0394 -0.0167 141 TYR B CA 3678 C C . TYR B 141 ? 0.7988 1.1408 0.7454 0.2781 -0.0458 -0.0285 141 TYR B C 3679 O O . TYR B 141 ? 0.8581 1.2200 0.8009 0.2883 -0.0448 -0.0197 141 TYR B O 3680 C CB . TYR B 141 ? 0.8488 1.2025 0.7754 0.2995 -0.0406 -0.0245 141 TYR B CB 3681 C CG . TYR B 141 ? 0.8532 1.2365 0.7829 0.3051 -0.0336 -0.0111 141 TYR B CG 3682 C CD1 . TYR B 141 ? 0.8623 1.2981 0.8090 0.2932 -0.0256 0.0151 141 TYR B CD1 3683 C CD2 . TYR B 141 ? 0.8864 1.2460 0.7953 0.3197 -0.0369 -0.0232 141 TYR B CD2 3684 C CE1 . TYR B 141 ? 0.8818 1.3642 0.8330 0.2936 -0.0198 0.0293 141 TYR B CE1 3685 C CE2 . TYR B 141 ? 0.9162 1.3168 0.8281 0.3299 -0.0305 -0.0111 141 TYR B CE2 3686 C CZ . TYR B 141 ? 0.9028 1.3740 0.8401 0.3158 -0.0213 0.0153 141 TYR B CZ 3687 O OH . TYR B 141 ? 0.9442 1.4742 0.8856 0.3218 -0.0156 0.0288 141 TYR B OH 3688 N N . HIS B 142 ? 1.0508 1.7131 0.7904 0.3318 -0.1681 -0.1494 142 HIS B N 3689 C CA . HIS B 142 ? 1.0563 1.7382 0.7796 0.3410 -0.1999 -0.1792 142 HIS B CA 3690 C C . HIS B 142 ? 0.9859 1.6589 0.7586 0.3070 -0.1947 -0.1476 142 HIS B C 3691 O O . HIS B 142 ? 0.9454 1.5767 0.7572 0.2721 -0.1731 -0.1160 142 HIS B O 3692 C CB . HIS B 142 ? 1.0986 1.7452 0.8196 0.3267 -0.2428 -0.2534 142 HIS B CB 3693 C CG . HIS B 142 ? 1.0582 1.6383 0.8427 0.2705 -0.2427 -0.2648 142 HIS B CG 3694 N ND1 . HIS B 142 ? 1.0284 1.5985 0.8726 0.2291 -0.2572 -0.2697 142 HIS B ND1 3695 C CD2 . HIS B 142 ? 1.0546 1.5817 0.8493 0.2570 -0.2262 -0.2666 142 HIS B CD2 3696 C CE1 . HIS B 142 ? 1.0007 1.5090 0.8852 0.1930 -0.2475 -0.2734 142 HIS B CE1 3697 N NE2 . HIS B 142 ? 1.0171 1.4965 0.8705 0.2092 -0.2304 -0.2732 142 HIS B NE2 3698 N N . LYS B 143 ? 0.9997 1.7130 0.7636 0.3232 -0.2165 -0.1573 143 LYS B N 3699 C CA . LYS B 143 ? 0.9604 1.6685 0.7618 0.3043 -0.2103 -0.1279 143 LYS B CA 3700 C C . LYS B 143 ? 0.9085 1.5835 0.7706 0.2574 -0.2313 -0.1627 143 LYS B C 3701 O O . LYS B 143 ? 0.9157 1.6049 0.7896 0.2477 -0.2666 -0.2149 143 LYS B O 3702 C CB . LYS B 143 ? 1.0104 1.7909 0.7806 0.3492 -0.2235 -0.1188 143 LYS B CB 3703 C CG . LYS B 143 ? 1.0278 1.7985 0.7887 0.3659 -0.1878 -0.0529 143 LYS B CG 3704 C CD . LYS B 143 ? 1.0945 1.9430 0.8080 0.4272 -0.1945 -0.0366 143 LYS B CD 3705 C CE . LYS B 143 ? 1.1049 2.0126 0.8534 0.4278 -0.2323 -0.0639 143 LYS B CE 3706 N NZ . LYS B 143 ? 1.0731 1.9435 0.8591 0.4120 -0.2094 -0.0266 143 LYS B NZ 3707 N N . CYS B 144 ? 0.8555 1.4803 0.7522 0.2294 -0.2092 -0.1330 144 CYS B N 3708 C CA . CYS B 144 ? 0.8171 1.4068 0.7689 0.1909 -0.2168 -0.1532 144 CYS B CA 3709 C C . CYS B 144 ? 0.7922 1.3955 0.7726 0.1930 -0.2091 -0.1247 144 CYS B C 3710 O O . CYS B 144 ? 0.7935 1.3436 0.7609 0.1944 -0.1816 -0.0879 144 CYS B O 3711 C CB . CYS B 144 ? 0.8018 1.3158 0.7575 0.1662 -0.1959 -0.1464 144 CYS B CB 3712 S SG . CYS B 144 ? 0.7915 1.2556 0.8015 0.1289 -0.1994 -0.1712 144 CYS B SG 3713 N N . ASP B 145 ? 0.7979 1.4742 0.8150 0.1957 -0.2360 -0.1425 145 ASP B N 3714 C CA . ASP B 145 ? 0.7871 1.5026 0.8401 0.2064 -0.2281 -0.1117 145 ASP B CA 3715 C C . ASP B 145 ? 0.7503 1.4198 0.8574 0.1749 -0.2111 -0.1042 145 ASP B C 3716 O O . ASP B 145 ? 0.7366 1.3399 0.8475 0.1462 -0.2061 -0.1226 145 ASP B O 3717 C CB . ASP B 145 ? 0.7926 1.6258 0.8809 0.2180 -0.2675 -0.1311 145 ASP B CB 3718 C CG . ASP B 145 ? 0.7995 1.6571 0.9520 0.1708 -0.3087 -0.1854 145 ASP B CG 3719 O OD1 . ASP B 145 ? 0.8017 1.5796 0.9612 0.1368 -0.3019 -0.2065 145 ASP B OD1 3720 O OD2 . ASP B 145 ? 0.8399 1.7945 1.0352 0.1674 -0.3506 -0.2075 145 ASP B OD2 3721 N N . ASN B 146 ? 0.7395 1.4490 0.8843 0.1887 -0.1985 -0.0724 146 ASN B N 3722 C CA . ASN B 146 ? 0.7229 1.3901 0.9065 0.1743 -0.1718 -0.0525 146 ASN B CA 3723 C C . ASN B 146 ? 0.7292 1.4073 0.9931 0.1243 -0.1872 -0.0820 146 ASN B C 3724 O O . ASN B 146 ? 0.7340 1.3389 1.0028 0.1090 -0.1638 -0.0761 146 ASN B O 3725 C CB . ASN B 146 ? 0.7164 1.4340 0.9170 0.2134 -0.1489 -0.0047 146 ASN B CB 3726 C CG . ASN B 146 ? 0.7512 1.4135 0.8563 0.2653 -0.1247 0.0283 146 ASN B CG 3727 O OD1 . ASN B 146 ? 0.7668 1.3369 0.8026 0.2622 -0.1190 0.0217 146 ASN B OD1 3728 N ND2 . ASN B 146 ? 0.7849 1.5040 0.8895 0.3131 -0.1097 0.0670 146 ASN B ND2 3729 N N . GLU B 147 ? 0.7604 1.5208 1.0808 0.0997 -0.2284 -0.1147 147 GLU B N 3730 C CA . GLU B 147 ? 0.7947 1.5429 1.1843 0.0448 -0.2491 -0.1502 147 GLU B CA 3731 C C . GLU B 147 ? 0.7880 1.4281 1.1153 0.0338 -0.2479 -0.1849 147 GLU B C 3732 O O . GLU B 147 ? 0.8037 1.3782 1.1575 0.0055 -0.2341 -0.1905 147 GLU B O 3733 C CB . GLU B 147 ? 0.8426 1.6897 1.2928 0.0178 -0.3060 -0.1892 147 GLU B CB 3734 C CG . GLU B 147 ? 0.8538 1.8356 1.3936 0.0213 -0.3135 -0.1546 147 GLU B CG 3735 C CD . GLU B 147 ? 0.8722 1.9328 1.3563 0.0805 -0.3217 -0.1377 147 GLU B CD 3736 O OE1 . GLU B 147 ? 0.8647 1.8601 1.2532 0.1276 -0.2864 -0.1126 147 GLU B OE1 3737 O OE2 . GLU B 147 ? 0.9015 2.0890 1.4387 0.0793 -0.3649 -0.1485 147 GLU B OE2 3738 N N . CYS B 148 ? 0.7827 1.4116 1.0287 0.0616 -0.2585 -0.2019 148 CYS B N 3739 C CA . CYS B 148 ? 0.7889 1.3355 0.9733 0.0634 -0.2523 -0.2244 148 CYS B CA 3740 C C . CYS B 148 ? 0.7386 1.2078 0.9083 0.0655 -0.2104 -0.1909 148 CYS B C 3741 O O . CYS B 148 ? 0.7236 1.1298 0.8999 0.0482 -0.2011 -0.2029 148 CYS B O 3742 C CB . CYS B 148 ? 0.8157 1.3869 0.9242 0.1011 -0.2608 -0.2290 148 CYS B CB 3743 S SG . CYS B 148 ? 0.8758 1.3791 0.9131 0.1162 -0.2443 -0.2367 148 CYS B SG 3744 N N . MET B 149 ? 0.7029 1.1719 0.8467 0.0904 -0.1874 -0.1500 149 MET B N 3745 C CA . MET B 149 ? 0.6824 1.0776 0.8013 0.0967 -0.1559 -0.1221 149 MET B CA 3746 C C . MET B 149 ? 0.6851 1.0551 0.8550 0.0803 -0.1391 -0.1149 149 MET B C 3747 O O . MET B 149 ? 0.6853 0.9878 0.8342 0.0792 -0.1230 -0.1132 149 MET B O 3748 C CB . MET B 149 ? 0.6855 1.0759 0.7679 0.1271 -0.1385 -0.0834 149 MET B CB 3749 C CG . MET B 149 ? 0.6911 1.0822 0.7173 0.1439 -0.1438 -0.0767 149 MET B CG 3750 S SD . MET B 149 ? 0.6883 1.0229 0.6762 0.1285 -0.1446 -0.0877 149 MET B SD 3751 C CE . MET B 149 ? 0.7117 1.0602 0.6532 0.1472 -0.1416 -0.0610 149 MET B CE 3752 N N . GLU B 150 ? 0.6991 1.1318 0.9399 0.0698 -0.1416 -0.1054 150 GLU B N 3753 C CA . GLU B 150 ? 0.7218 1.1429 1.0265 0.0529 -0.1191 -0.0867 150 GLU B CA 3754 C C . GLU B 150 ? 0.7482 1.1134 1.0714 0.0195 -0.1256 -0.1184 150 GLU B C 3755 O O . GLU B 150 ? 0.7630 1.0726 1.0957 0.0190 -0.0954 -0.0989 150 GLU B O 3756 C CB . GLU B 150 ? 0.7426 1.2664 1.1414 0.0406 -0.1243 -0.0669 150 GLU B CB 3757 C CG . GLU B 150 ? 0.7775 1.3061 1.2562 0.0264 -0.0907 -0.0295 150 GLU B CG 3758 C CD . GLU B 150 ? 0.8104 1.2792 1.2302 0.0752 -0.0412 0.0158 150 GLU B CD 3759 O OE1 . GLU B 150 ? 0.8378 1.3155 1.2000 0.1209 -0.0312 0.0375 150 GLU B OE1 3760 O OE2 . GLU B 150 ? 0.8392 1.2431 1.2593 0.0731 -0.0129 0.0287 150 GLU B OE2 3761 N N . SER B 151 ? 0.7678 1.1401 1.0845 0.0001 -0.1623 -0.1655 151 SER B N 3762 C CA . SER B 151 ? 0.8270 1.1306 1.1467 -0.0245 -0.1691 -0.1992 151 SER B CA 3763 C C . SER B 151 ? 0.8383 1.0624 1.0819 0.0030 -0.1462 -0.1963 151 SER B C 3764 O O . SER B 151 ? 0.8853 1.0392 1.1277 -0.0039 -0.1330 -0.2039 151 SER B O 3765 C CB . SER B 151 ? 0.8744 1.1978 1.1874 -0.0417 -0.2172 -0.2552 151 SER B CB 3766 O OG . SER B 151 ? 0.8771 1.2056 1.1052 -0.0060 -0.2273 -0.2709 151 SER B OG 3767 N N . VAL B 152 ? 0.8025 1.0389 0.9864 0.0334 -0.1425 -0.1829 152 VAL B N 3768 C CA . VAL B 152 ? 0.7942 0.9766 0.9195 0.0558 -0.1259 -0.1745 152 VAL B CA 3769 C C . VAL B 152 ? 0.8068 0.9445 0.9365 0.0660 -0.0936 -0.1405 152 VAL B C 3770 O O . VAL B 152 ? 0.8105 0.8945 0.9171 0.0770 -0.0789 -0.1393 152 VAL B O 3771 C CB . VAL B 152 ? 0.7550 0.9630 0.8296 0.0748 -0.1330 -0.1646 152 VAL B CB 3772 C CG1 . VAL B 152 ? 0.7556 0.9237 0.7871 0.0893 -0.1235 -0.1563 152 VAL B CG1 3773 C CG2 . VAL B 152 ? 0.7622 1.0198 0.8246 0.0762 -0.1575 -0.1894 152 VAL B CG2 3774 N N . ARG B 153 ? 0.8165 0.9790 0.9687 0.0717 -0.0803 -0.1105 153 ARG B N 3775 C CA . ARG B 153 ? 0.8664 0.9904 1.0149 0.0925 -0.0454 -0.0743 153 ARG B CA 3776 C C . ARG B 153 ? 0.9379 1.0442 1.1515 0.0731 -0.0241 -0.0653 153 ARG B C 3777 O O . ARG B 153 ? 0.9695 1.0222 1.1642 0.0940 0.0065 -0.0425 153 ARG B O 3778 C CB . ARG B 153 ? 0.8556 1.0120 1.0040 0.1145 -0.0322 -0.0411 153 ARG B CB 3779 C CG . ARG B 153 ? 0.8331 0.9841 0.9124 0.1334 -0.0489 -0.0448 153 ARG B CG 3780 C CD . ARG B 153 ? 0.8625 1.0148 0.9179 0.1695 -0.0286 -0.0097 153 ARG B CD 3781 N NE . ARG B 153 ? 0.8673 1.0407 0.8929 0.1755 -0.0467 -0.0129 153 ARG B NE 3782 C CZ . ARG B 153 ? 0.8426 1.0957 0.9151 0.1717 -0.0542 -0.0079 153 ARG B CZ 3783 N NH1 . ARG B 153 ? 0.8165 1.1435 0.9789 0.1538 -0.0511 -0.0023 153 ARG B NH1 3784 N NH2 . ARG B 153 ? 0.8596 1.1201 0.8910 0.1855 -0.0659 -0.0061 153 ARG B NH2 3785 N N . ASN B 154 ? 1.0132 1.1630 1.3023 0.0332 -0.0419 -0.0821 154 ASN B N 3786 C CA . ASN B 154 ? 1.1101 1.2339 1.4731 -0.0013 -0.0293 -0.0792 154 ASN B CA 3787 C C . ASN B 154 ? 1.1347 1.1629 1.4531 0.0053 -0.0188 -0.0958 154 ASN B C 3788 O O . ASN B 154 ? 1.2098 1.1850 1.5493 0.0081 0.0180 -0.0662 154 ASN B O 3789 C CB . ASN B 154 ? 1.1919 1.3650 1.6244 -0.0518 -0.0710 -0.1163 154 ASN B CB 3790 C CG . ASN B 154 ? 1.2723 1.5509 1.7914 -0.0684 -0.0748 -0.0886 154 ASN B CG 3791 O OD1 . ASN B 154 ? 1.2904 1.6056 1.8033 -0.0332 -0.0450 -0.0424 154 ASN B OD1 3792 N ND2 . ASN B 154 ? 1.4155 1.7449 2.0121 -0.1186 -0.1145 -0.1182 154 ASN B ND2 3793 N N . GLY B 155 ? 1.0841 1.0952 1.3400 0.0141 -0.0470 -0.1376 155 GLY B N 3794 C CA . GLY B 155 ? 1.1052 1.0359 1.3228 0.0210 -0.0438 -0.1613 155 GLY B CA 3795 C C . GLY B 155 ? 1.1274 1.0433 1.3646 -0.0140 -0.0794 -0.2122 155 GLY B C 3796 O O . GLY B 155 ? 1.1954 1.0328 1.3934 -0.0061 -0.0797 -0.2385 155 GLY B O 3797 N N . THR B 156 ? 1.0776 1.0670 1.3651 -0.0455 -0.1117 -0.2277 156 THR B N 3798 C CA . THR B 156 ? 1.1248 1.1053 1.4351 -0.0829 -0.1550 -0.2804 156 THR B CA 3799 C C . THR B 156 ? 1.0911 1.1326 1.3462 -0.0632 -0.1954 -0.3180 156 THR B C 3800 O O . THR B 156 ? 1.1195 1.1986 1.4003 -0.0899 -0.2388 -0.3552 156 THR B O 3801 C CB . THR B 156 ? 1.1337 1.1654 1.5618 -0.1401 -0.1674 -0.2691 156 THR B CB 3802 O OG1 . THR B 156 ? 1.0521 1.2022 1.5093 -0.1305 -0.1726 -0.2423 156 THR B OG1 3803 C CG2 . THR B 156 ? 1.1667 1.1456 1.6604 -0.1593 -0.1195 -0.2204 156 THR B CG2 3804 N N . TYR B 157 ? 1.0511 1.1070 1.2331 -0.0166 -0.1822 -0.3060 157 TYR B N 3805 C CA . TYR B 157 ? 1.0440 1.1562 1.1713 0.0086 -0.2099 -0.3301 157 TYR B CA 3806 C C . TYR B 157 ? 1.1466 1.2039 1.2193 0.0181 -0.2363 -0.3861 157 TYR B C 3807 O O . TYR B 157 ? 1.1802 1.1664 1.1998 0.0454 -0.2178 -0.3922 157 TYR B O 3808 C CB . TYR B 157 ? 0.9762 1.1123 1.0515 0.0483 -0.1866 -0.2976 157 TYR B CB 3809 C CG . TYR B 157 ? 0.9628 1.1520 0.9832 0.0778 -0.2045 -0.3118 157 TYR B CG 3810 C CD1 . TYR B 157 ? 0.9381 1.2040 0.9673 0.0780 -0.2215 -0.3054 157 TYR B CD1 3811 C CD2 . TYR B 157 ? 0.9917 1.1591 0.9497 0.1132 -0.1993 -0.3250 157 TYR B CD2 3812 C CE1 . TYR B 157 ? 0.9378 1.2519 0.9140 0.1109 -0.2311 -0.3102 157 TYR B CE1 3813 C CE2 . TYR B 157 ? 0.9964 1.2204 0.9064 0.1463 -0.2079 -0.3284 157 TYR B CE2 3814 C CZ . TYR B 157 ? 0.9585 1.2529 0.8773 0.1441 -0.2229 -0.3203 157 TYR B CZ 3815 O OH . TYR B 157 ? 0.9530 1.3026 0.8213 0.1827 -0.2247 -0.3158 157 TYR B OH 3816 N N . ASP B 158 ? 1.2231 1.3135 1.3014 0.0020 -0.2812 -0.4278 158 ASP B N 3817 C CA . ASP B 158 ? 1.3650 1.3882 1.3814 0.0109 -0.3149 -0.4912 158 ASP B CA 3818 C C . ASP B 158 ? 1.3917 1.4387 1.3040 0.0778 -0.3123 -0.4998 158 ASP B C 3819 O O . ASP B 158 ? 1.3899 1.5128 1.2731 0.0986 -0.3380 -0.5123 158 ASP B O 3820 C CB . ASP B 158 ? 1.4258 1.4786 1.4869 -0.0333 -0.3729 -0.5372 158 ASP B CB 3821 C CG . ASP B 158 ? 1.5845 1.5239 1.5973 -0.0451 -0.4117 -0.6088 158 ASP B CG 3822 O OD1 . ASP B 158 ? 1.6527 1.4757 1.6123 -0.0251 -0.3850 -0.6156 158 ASP B OD1 3823 O OD2 . ASP B 158 ? 1.6703 1.6327 1.6932 -0.0721 -0.4719 -0.6603 158 ASP B OD2 3824 N N . TYR B 159 ? 1.4253 1.4162 1.2850 0.1159 -0.2773 -0.4861 159 TYR B N 3825 C CA . TYR B 159 ? 1.4483 1.4716 1.2220 0.1824 -0.2643 -0.4809 159 TYR B CA 3826 C C . TYR B 159 ? 1.5964 1.5997 1.2817 0.2188 -0.3018 -0.5411 159 TYR B C 3827 O O . TYR B 159 ? 1.5996 1.6817 1.2362 0.2639 -0.3034 -0.5328 159 TYR B O 3828 C CB . TYR B 159 ? 1.4470 1.4184 1.1913 0.2159 -0.2224 -0.4552 159 TYR B CB 3829 C CG . TYR B 159 ? 1.4844 1.4854 1.1441 0.2888 -0.2065 -0.4501 159 TYR B CG 3830 C CD1 . TYR B 159 ? 1.6196 1.5431 1.1842 0.3366 -0.2170 -0.4990 159 TYR B CD1 3831 C CD2 . TYR B 159 ? 1.3915 1.4953 1.0662 0.3110 -0.1799 -0.3940 159 TYR B CD2 3832 C CE1 . TYR B 159 ? 1.6572 1.6180 1.1421 0.4146 -0.1955 -0.4867 159 TYR B CE1 3833 C CE2 . TYR B 159 ? 1.4257 1.5758 1.0393 0.3771 -0.1602 -0.3784 159 TYR B CE2 3834 C CZ . TYR B 159 ? 1.5553 1.6398 1.0730 0.4338 -0.1649 -0.4221 159 TYR B CZ 3835 O OH . TYR B 159 ? 1.6002 1.7396 1.0541 0.5106 -0.1388 -0.3999 159 TYR B OH 3836 N N . PRO B 160 ? 1.7430 1.6339 1.4017 0.2016 -0.3319 -0.6015 160 PRO B N 3837 C CA . PRO B 160 ? 1.8954 1.7575 1.4591 0.2352 -0.3789 -0.6694 160 PRO B CA 3838 C C . PRO B 160 ? 1.8662 1.8352 1.4511 0.2204 -0.4242 -0.6846 160 PRO B C 3839 O O . PRO B 160 ? 1.9504 1.9351 1.4393 0.2728 -0.4538 -0.7240 160 PRO B O 3840 C CB . PRO B 160 ? 2.0358 1.7442 1.5930 0.1947 -0.4090 -0.7301 160 PRO B CB 3841 C CG . PRO B 160 ? 1.9920 1.6350 1.5935 0.1808 -0.3558 -0.6850 160 PRO B CG 3842 C CD . PRO B 160 ? 1.7980 1.5675 1.4914 0.1629 -0.3204 -0.6095 160 PRO B CD 3843 N N . GLN B 161 ? 1.7555 1.7984 1.4559 0.1598 -0.4275 -0.6515 161 GLN B N 3844 C CA . GLN B 161 ? 1.7262 1.8819 1.4530 0.1510 -0.4660 -0.6565 161 GLN B CA 3845 C C . GLN B 161 ? 1.6435 1.9011 1.3200 0.2152 -0.4373 -0.6100 161 GLN B C 3846 O O . GLN B 161 ? 1.6855 2.0173 1.3237 0.2442 -0.4685 -0.6255 161 GLN B O 3847 C CB . GLN B 161 ? 1.6336 1.8443 1.4971 0.0789 -0.4681 -0.6237 161 GLN B CB 3848 C CG . GLN B 161 ? 1.6294 1.9498 1.5298 0.0639 -0.5191 -0.6399 161 GLN B CG 3849 C CD . GLN B 161 ? 1.5461 1.9266 1.5858 -0.0017 -0.5179 -0.6039 161 GLN B CD 3850 O OE1 . GLN B 161 ? 1.4762 1.8176 1.5781 -0.0303 -0.4729 -0.5610 161 GLN B OE1 3851 N NE2 . GLN B 161 ? 1.5566 2.0409 1.6429 -0.0184 -0.5663 -0.6182 161 GLN B NE2 3852 N N . TYR B 162 ? 1.5334 1.7960 1.2133 0.2358 -0.3791 -0.5510 162 TYR B N 3853 C CA . TYR B 162 ? 1.4612 1.8108 1.1067 0.2872 -0.3464 -0.4988 162 TYR B CA 3854 C C . TYR B 162 ? 1.4792 1.7992 1.0454 0.3480 -0.3131 -0.4904 162 TYR B C 3855 O O . TYR B 162 ? 1.4660 1.8487 0.9718 0.4081 -0.2962 -0.4670 162 TYR B O 3856 C CB . TYR B 162 ? 1.3400 1.7367 1.0709 0.2530 -0.3105 -0.4300 162 TYR B CB 3857 C CG . TYR B 162 ? 1.3017 1.7310 1.1129 0.2022 -0.3329 -0.4275 162 TYR B CG 3858 C CD1 . TYR B 162 ? 1.3122 1.8253 1.1185 0.2170 -0.3566 -0.4254 162 TYR B CD1 3859 C CD2 . TYR B 162 ? 1.2544 1.6390 1.1448 0.1478 -0.3258 -0.4203 162 TYR B CD2 3860 C CE1 . TYR B 162 ? 1.2666 1.8247 1.1496 0.1787 -0.3740 -0.4167 162 TYR B CE1 3861 C CE2 . TYR B 162 ? 1.2082 1.6364 1.1762 0.1090 -0.3397 -0.4092 162 TYR B CE2 3862 C CZ . TYR B 162 ? 1.2113 1.7295 1.1780 0.1243 -0.3644 -0.4074 162 TYR B CZ 3863 O OH . TYR B 162 ? 1.1582 1.7335 1.2052 0.0933 -0.3755 -0.3906 162 TYR B OH # _database_PDB_caveat.id 1 _database_PDB_caveat.text ;BMA A 1327 HAS WRONG CHIRALITY AT ATOM C1 MAN A 1328 HAS WRONG CHIRALITY AT ATOM C1 NAG A 1326 HAS WRONG CHIRALITY AT ATOM C1 NAG B 1163 HAS WRONG CHIRALITY AT ATOM C1 ; # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 ASP 1 1 1 ASP ASP A . n A 1 2 GLN 2 2 2 GLN GLN A . n A 1 3 ILE 3 3 3 ILE ILE A . n A 1 4 CYS 4 4 4 CYS CYS A . n A 1 5 ILE 5 5 5 ILE ILE A . n A 1 6 GLY 6 6 6 GLY GLY A . n A 1 7 TYR 7 7 7 TYR TYR A . n A 1 8 HIS 8 8 8 HIS HIS A . n A 1 9 ALA 9 9 9 ALA ALA A . n A 1 10 ASN 10 10 10 ASN ASN A . n A 1 11 ASN 11 11 11 ASN ASN A . n A 1 12 SER 12 12 12 SER SER A . n A 1 13 THR 13 13 13 THR THR A . n A 1 14 GLU 14 14 14 GLU GLU A . n A 1 15 GLN 15 15 15 GLN GLN A . n A 1 16 VAL 16 16 16 VAL VAL A . n A 1 17 ASP 17 17 17 ASP ASP A . n A 1 18 THR 18 18 18 THR THR A . n A 1 19 ILE 19 19 19 ILE ILE A . n A 1 20 MET 20 20 20 MET MET A . n A 1 21 GLU 21 21 21 GLU GLU A . n A 1 22 LYS 22 22 22 LYS LYS A . n A 1 23 ASN 23 23 23 ASN ASN A . n A 1 24 VAL 24 24 24 VAL VAL A . n A 1 25 THR 25 25 25 THR THR A . n A 1 26 VAL 26 26 26 VAL VAL A . n A 1 27 THR 27 27 27 THR THR A . n A 1 28 HIS 28 28 28 HIS HIS A . n A 1 29 ALA 29 29 29 ALA ALA A . n A 1 30 GLN 30 30 30 GLN GLN A . n A 1 31 ASP 31 31 31 ASP ASP A . n A 1 32 ILE 32 32 32 ILE ILE A . n A 1 33 LEU 33 33 33 LEU LEU A . n A 1 34 GLU 34 34 34 GLU GLU A . n A 1 35 LYS 35 35 35 LYS LYS A . n A 1 36 THR 36 36 36 THR THR A . n A 1 37 HIS 37 37 37 HIS HIS A . n A 1 38 ASN 38 38 38 ASN ASN A . n A 1 39 GLY 39 39 39 GLY GLY A . n A 1 40 LYS 40 40 40 LYS LYS A . n A 1 41 LEU 41 41 41 LEU LEU A . n A 1 42 CYS 42 42 42 CYS CYS A . n A 1 43 ASP 43 43 43 ASP ASP A . n A 1 44 LEU 44 44 44 LEU LEU A . n A 1 45 ASP 45 45 45 ASP ASP A . n A 1 46 GLY 46 46 46 GLY GLY A . n A 1 47 VAL 47 47 47 VAL VAL A . n A 1 48 LYS 48 48 48 LYS LYS A . n A 1 49 PRO 49 49 49 PRO PRO A . n A 1 50 LEU 50 50 50 LEU LEU A . n A 1 51 ILE 51 51 51 ILE ILE A . n A 1 52 LEU 52 52 52 LEU LEU A . n A 1 53 ARG 53 53 53 ARG ARG A . n A 1 54 ASP 54 54 54 ASP ASP A . n A 1 55 CYS 55 55 55 CYS CYS A . n A 1 56 SER 56 56 56 SER SER A . n A 1 57 VAL 57 57 57 VAL VAL A . n A 1 58 ALA 58 58 58 ALA ALA A . n A 1 59 GLY 59 59 59 GLY GLY A . n A 1 60 TRP 60 60 60 TRP TRP A . n A 1 61 LEU 61 61 61 LEU LEU A . n A 1 62 LEU 62 62 62 LEU LEU A . n A 1 63 GLY 63 63 63 GLY GLY A . n A 1 64 ASN 64 64 64 ASN ASN A . n A 1 65 PRO 65 65 65 PRO PRO A . n A 1 66 MET 66 66 66 MET MET A . n A 1 67 CYS 67 67 67 CYS CYS A . n A 1 68 ASP 68 68 68 ASP ASP A . n A 1 69 GLU 69 69 69 GLU GLU A . n A 1 70 PHE 70 70 70 PHE PHE A . n A 1 71 ILE 71 71 71 ILE ILE A . n A 1 72 ASN 72 72 72 ASN ASN A . n A 1 73 VAL 73 73 73 VAL VAL A . n A 1 74 PRO 74 74 74 PRO PRO A . n A 1 75 GLU 75 75 75 GLU GLU A . n A 1 76 TRP 76 76 76 TRP TRP A . n A 1 77 SER 77 77 77 SER SER A . n A 1 78 TYR 78 78 78 TYR TYR A . n A 1 79 ILE 79 79 79 ILE ILE A . n A 1 80 VAL 80 80 80 VAL VAL A . n A 1 81 GLU 81 81 81 GLU GLU A . n A 1 82 LYS 82 82 82 LYS LYS A . n A 1 83 ALA 83 83 83 ALA ALA A . n A 1 84 ASN 84 84 84 ASN ASN A . n A 1 85 PRO 85 85 85 PRO PRO A . n A 1 86 VAL 86 86 86 VAL VAL A . n A 1 87 ASN 87 87 87 ASN ASN A . n A 1 88 ASP 88 88 88 ASP ASP A . n A 1 89 LEU 89 89 89 LEU LEU A . n A 1 90 CYS 90 90 90 CYS CYS A . n A 1 91 TYR 91 91 91 TYR TYR A . n A 1 92 PRO 92 92 92 PRO PRO A . n A 1 93 GLY 93 93 93 GLY GLY A . n A 1 94 ASP 94 94 94 ASP ASP A . n A 1 95 PHE 95 95 95 PHE PHE A . n A 1 96 ASN 96 96 96 ASN ASN A . n A 1 97 ASP 97 97 97 ASP ASP A . n A 1 98 TYR 98 98 98 TYR TYR A . n A 1 99 GLU 99 99 99 GLU GLU A . n A 1 100 GLU 100 100 100 GLU GLU A . n A 1 101 LEU 101 101 101 LEU LEU A . n A 1 102 LYS 102 102 102 LYS LYS A . n A 1 103 HIS 103 103 103 HIS HIS A . n A 1 104 LEU 104 104 104 LEU LEU A . n A 1 105 LEU 105 105 105 LEU LEU A . n A 1 106 SER 106 106 106 SER SER A . n A 1 107 ARG 107 107 107 ARG ARG A . n A 1 108 ILE 108 108 108 ILE ILE A . n A 1 109 ASN 109 109 109 ASN ASN A . n A 1 110 HIS 110 110 110 HIS HIS A . n A 1 111 PHE 111 111 111 PHE PHE A . n A 1 112 GLU 112 112 112 GLU GLU A . n A 1 113 LYS 113 113 113 LYS LYS A . n A 1 114 ILE 114 114 114 ILE ILE A . n A 1 115 GLN 115 115 115 GLN GLN A . n A 1 116 ILE 116 116 116 ILE ILE A . n A 1 117 ILE 117 117 117 ILE ILE A . n A 1 118 PRO 118 118 118 PRO PRO A . n A 1 119 LYS 119 119 119 LYS LYS A . n A 1 120 SER 120 120 120 SER SER A . n A 1 121 SER 121 121 121 SER SER A . n A 1 122 TRP 122 122 122 TRP TRP A . n A 1 123 SER 123 123 123 SER SER A . n A 1 124 SER 124 124 124 SER SER A . n A 1 125 HIS 125 125 125 HIS HIS A . n A 1 126 GLU 126 126 126 GLU GLU A . n A 1 127 ALA 127 127 127 ALA ALA A . n A 1 128 SER 128 128 128 SER SER A . n A 1 129 LEU 129 129 129 LEU LEU A . n A 1 130 GLY 130 130 130 GLY GLY A . n A 1 131 VAL 131 131 131 VAL VAL A . n A 1 132 SER 132 132 132 SER SER A . n A 1 133 SER 133 133 133 SER SER A . n A 1 134 ALA 134 134 134 ALA ALA A . n A 1 135 CYS 135 135 135 CYS CYS A . n A 1 136 PRO 136 136 136 PRO PRO A . n A 1 137 TYR 137 137 137 TYR TYR A . n A 1 138 GLN 138 138 138 GLN GLN A . n A 1 139 GLY 139 139 139 GLY GLY A . n A 1 140 LYS 140 140 140 LYS LYS A . n A 1 141 SER 141 141 141 SER SER A . n A 1 142 SER 142 142 142 SER SER A . n A 1 143 PHE 143 143 143 PHE PHE A . n A 1 144 PHE 144 144 144 PHE PHE A . n A 1 145 ARG 145 145 145 ARG ARG A . n A 1 146 ASN 146 146 146 ASN ASN A . n A 1 147 VAL 147 147 147 VAL VAL A . n A 1 148 VAL 148 148 148 VAL VAL A . n A 1 149 TRP 149 149 149 TRP TRP A . n A 1 150 LEU 150 150 150 LEU LEU A . n A 1 151 ILE 151 151 151 ILE ILE A . n A 1 152 LYS 152 152 152 LYS LYS A . n A 1 153 LYS 153 153 153 LYS LYS A . n A 1 154 ASN 154 154 154 ASN ASN A . n A 1 155 SER 155 155 155 SER SER A . n A 1 156 THR 156 156 156 THR THR A . n A 1 157 TYR 157 157 157 TYR TYR A . n A 1 158 PRO 158 158 158 PRO PRO A . n A 1 159 THR 159 159 159 THR THR A . n A 1 160 ILE 160 160 160 ILE ILE A . n A 1 161 LYS 161 161 161 LYS LYS A . n A 1 162 ARG 162 162 162 ARG ARG A . n A 1 163 SER 163 163 163 SER SER A . n A 1 164 TYR 164 164 164 TYR TYR A . n A 1 165 ASN 165 165 165 ASN ASN A . n A 1 166 ASN 166 166 166 ASN ASN A . n A 1 167 THR 167 167 167 THR THR A . n A 1 168 ASN 168 168 168 ASN ASN A . n A 1 169 GLN 169 169 169 GLN GLN A . n A 1 170 GLU 170 170 170 GLU GLU A . n A 1 171 ASP 171 171 171 ASP ASP A . n A 1 172 LEU 172 172 172 LEU LEU A . n A 1 173 LEU 173 173 173 LEU LEU A . n A 1 174 VAL 174 174 174 VAL VAL A . n A 1 175 LEU 175 175 175 LEU LEU A . n A 1 176 TRP 176 176 176 TRP TRP A . n A 1 177 GLY 177 177 177 GLY GLY A . n A 1 178 ILE 178 178 178 ILE ILE A . n A 1 179 HIS 179 179 179 HIS HIS A . n A 1 180 HIS 180 180 180 HIS HIS A . n A 1 181 PRO 181 181 181 PRO PRO A . n A 1 182 LYS 182 182 182 LYS LYS A . n A 1 183 ASP 183 183 183 ASP ASP A . n A 1 184 ALA 184 184 184 ALA ALA A . n A 1 185 ALA 185 185 185 ALA ALA A . n A 1 186 GLU 186 186 186 GLU GLU A . n A 1 187 GLN 187 187 187 GLN GLN A . n A 1 188 THR 188 188 188 THR THR A . n A 1 189 LYS 189 189 189 LYS LYS A . n A 1 190 LEU 190 190 190 LEU LEU A . n A 1 191 TYR 191 191 191 TYR TYR A . n A 1 192 GLN 192 192 192 GLN GLN A . n A 1 193 ASN 193 193 193 ASN ASN A . n A 1 194 PRO 194 194 194 PRO PRO A . n A 1 195 THR 195 195 195 THR THR A . n A 1 196 THR 196 196 196 THR THR A . n A 1 197 TYR 197 197 197 TYR TYR A . n A 1 198 ILE 198 198 198 ILE ILE A . n A 1 199 SER 199 199 199 SER SER A . n A 1 200 VAL 200 200 200 VAL VAL A . n A 1 201 GLY 201 201 201 GLY GLY A . n A 1 202 THR 202 202 202 THR THR A . n A 1 203 SER 203 203 203 SER SER A . n A 1 204 THR 204 204 204 THR THR A . n A 1 205 LEU 205 205 205 LEU LEU A . n A 1 206 ASN 206 206 206 ASN ASN A . n A 1 207 GLN 207 207 207 GLN GLN A . n A 1 208 ARG 208 208 208 ARG ARG A . n A 1 209 LEU 209 209 209 LEU LEU A . n A 1 210 VAL 210 210 210 VAL VAL A . n A 1 211 PRO 211 211 211 PRO PRO A . n A 1 212 ARG 212 212 212 ARG ARG A . n A 1 213 ILE 213 213 213 ILE ILE A . n A 1 214 ALA 214 214 214 ALA ALA A . n A 1 215 THR 215 215 215 THR THR A . n A 1 216 ARG 216 216 216 ARG ARG A . n A 1 217 SER 217 217 217 SER SER A . n A 1 218 LYS 218 218 218 LYS LYS A . n A 1 219 VAL 219 219 219 VAL VAL A . n A 1 220 ASN 220 220 220 ASN ASN A . n A 1 221 GLY 221 221 221 GLY GLY A . n A 1 222 GLN 222 222 222 GLN GLN A . n A 1 223 SER 223 223 223 SER SER A . n A 1 224 GLY 224 224 224 GLY GLY A . n A 1 225 ARG 225 225 225 ARG ARG A . n A 1 226 MET 226 226 226 MET MET A . n A 1 227 GLU 227 227 227 GLU GLU A . n A 1 228 PHE 228 228 228 PHE PHE A . n A 1 229 PHE 229 229 229 PHE PHE A . n A 1 230 TRP 230 230 230 TRP TRP A . n A 1 231 THR 231 231 231 THR THR A . n A 1 232 ILE 232 232 232 ILE ILE A . n A 1 233 LEU 233 233 233 LEU LEU A . n A 1 234 LYS 234 234 234 LYS LYS A . n A 1 235 PRO 235 235 235 PRO PRO A . n A 1 236 ASN 236 236 236 ASN ASN A . n A 1 237 ASP 237 237 237 ASP ASP A . n A 1 238 ALA 238 238 238 ALA ALA A . n A 1 239 ILE 239 239 239 ILE ILE A . n A 1 240 ASN 240 240 240 ASN ASN A . n A 1 241 PHE 241 241 241 PHE PHE A . n A 1 242 GLU 242 242 242 GLU GLU A . n A 1 243 SER 243 243 243 SER SER A . n A 1 244 ASN 244 244 244 ASN ASN A . n A 1 245 GLY 245 245 245 GLY GLY A . n A 1 246 ASN 246 246 246 ASN ASN A . n A 1 247 PHE 247 247 247 PHE PHE A . n A 1 248 ILE 248 248 248 ILE ILE A . n A 1 249 ALA 249 249 249 ALA ALA A . n A 1 250 PRO 250 250 250 PRO PRO A . n A 1 251 GLU 251 251 251 GLU GLU A . n A 1 252 TYR 252 252 252 TYR TYR A . n A 1 253 ALA 253 253 253 ALA ALA A . n A 1 254 TYR 254 254 254 TYR TYR A . n A 1 255 LYS 255 255 255 LYS LYS A . n A 1 256 ILE 256 256 256 ILE ILE A . n A 1 257 VAL 257 257 257 VAL VAL A . n A 1 258 LYS 258 258 258 LYS LYS A . n A 1 259 LYS 259 259 259 LYS LYS A . n A 1 260 GLY 260 260 260 GLY GLY A . n A 1 261 ASP 261 261 261 ASP ASP A . n A 1 262 SER 262 262 262 SER SER A . n A 1 263 THR 263 263 263 THR THR A . n A 1 264 ILE 264 264 264 ILE ILE A . n A 1 265 MET 265 265 265 MET MET A . n A 1 266 LYS 266 266 266 LYS LYS A . n A 1 267 SER 267 267 267 SER SER A . n A 1 268 GLU 268 268 268 GLU GLU A . n A 1 269 LEU 269 269 269 LEU LEU A . n A 1 270 GLU 270 270 270 GLU GLU A . n A 1 271 TYR 271 271 271 TYR TYR A . n A 1 272 GLY 272 272 272 GLY GLY A . n A 1 273 ASN 273 273 273 ASN ASN A . n A 1 274 CYS 274 274 274 CYS CYS A . n A 1 275 ASN 275 275 275 ASN ASN A . n A 1 276 THR 276 276 276 THR THR A . n A 1 277 LYS 277 277 277 LYS LYS A . n A 1 278 CYS 278 278 278 CYS CYS A . n A 1 279 GLN 279 279 279 GLN GLN A . n A 1 280 THR 280 280 280 THR THR A . n A 1 281 PRO 281 281 281 PRO PRO A . n A 1 282 MET 282 282 282 MET MET A . n A 1 283 GLY 283 283 283 GLY GLY A . n A 1 284 ALA 284 284 284 ALA ALA A . n A 1 285 ILE 285 285 285 ILE ILE A . n A 1 286 ASN 286 286 286 ASN ASN A . n A 1 287 SER 287 287 287 SER SER A . n A 1 288 SER 288 288 288 SER SER A . n A 1 289 MET 289 289 289 MET MET A . n A 1 290 PRO 290 290 290 PRO PRO A . n A 1 291 PHE 291 291 291 PHE PHE A . n A 1 292 HIS 292 292 292 HIS HIS A . n A 1 293 ASN 293 293 293 ASN ASN A . n A 1 294 ILE 294 294 294 ILE ILE A . n A 1 295 HIS 295 295 295 HIS HIS A . n A 1 296 PRO 296 296 296 PRO PRO A . n A 1 297 LEU 297 297 297 LEU LEU A . n A 1 298 THR 298 298 298 THR THR A . n A 1 299 ILE 299 299 299 ILE ILE A . n A 1 300 GLY 300 300 300 GLY GLY A . n A 1 301 GLU 301 301 301 GLU GLU A . n A 1 302 CYS 302 302 302 CYS CYS A . n A 1 303 PRO 303 303 303 PRO PRO A . n A 1 304 LYS 304 304 304 LYS LYS A . n A 1 305 TYR 305 305 305 TYR TYR A . n A 1 306 VAL 306 306 306 VAL VAL A . n A 1 307 LYS 307 307 307 LYS LYS A . n A 1 308 SER 308 308 308 SER SER A . n A 1 309 ASN 309 309 309 ASN ASN A . n A 1 310 ARG 310 310 310 ARG ARG A . n A 1 311 LEU 311 311 311 LEU LEU A . n A 1 312 VAL 312 312 312 VAL VAL A . n A 1 313 LEU 313 313 313 LEU LEU A . n A 1 314 ALA 314 314 314 ALA ALA A . n A 1 315 THR 315 315 315 THR THR A . n A 1 316 GLY 316 316 316 GLY GLY A . n A 1 317 LEU 317 317 317 LEU LEU A . n A 1 318 ARG 318 318 318 ARG ARG A . n A 1 319 ASN 319 319 319 ASN ASN A . n A 1 320 SER 320 320 320 SER SER A . n A 1 321 PRO 321 321 321 PRO PRO A . n A 1 322 GLN 322 322 ? ? ? A . n A 1 323 ARG 323 323 ? ? ? A . n A 1 324 GLU 324 324 ? ? ? A . n A 1 325 THR 325 325 ? ? ? A . n A 1 326 ARG 326 326 ? ? ? A . n B 2 1 GLY 1 1 1 GLY GLY B . n B 2 2 LEU 2 2 2 LEU LEU B . n B 2 3 PHE 3 3 3 PHE PHE B . n B 2 4 GLY 4 4 4 GLY GLY B . n B 2 5 ALA 5 5 5 ALA ALA B . n B 2 6 ILE 6 6 6 ILE ILE B . n B 2 7 ALA 7 7 7 ALA ALA B . n B 2 8 GLY 8 8 8 GLY GLY B . n B 2 9 PHE 9 9 9 PHE PHE B . n B 2 10 ILE 10 10 10 ILE ILE B . n B 2 11 GLU 11 11 11 GLU GLU B . n B 2 12 GLY 12 12 12 GLY GLY B . n B 2 13 GLY 13 13 13 GLY GLY B . n B 2 14 TRP 14 14 14 TRP TRP B . n B 2 15 GLN 15 15 15 GLN GLN B . n B 2 16 GLY 16 16 16 GLY GLY B . n B 2 17 MET 17 17 17 MET MET B . n B 2 18 VAL 18 18 18 VAL VAL B . n B 2 19 ASP 19 19 19 ASP ASP B . n B 2 20 GLY 20 20 20 GLY GLY B . n B 2 21 TRP 21 21 21 TRP TRP B . n B 2 22 TYR 22 22 22 TYR TYR B . n B 2 23 GLY 23 23 23 GLY GLY B . n B 2 24 TYR 24 24 24 TYR TYR B . n B 2 25 HIS 25 25 25 HIS HIS B . n B 2 26 HIS 26 26 26 HIS HIS B . n B 2 27 SER 27 27 27 SER SER B . n B 2 28 ASN 28 28 28 ASN ASN B . n B 2 29 GLU 29 29 29 GLU GLU B . n B 2 30 GLN 30 30 30 GLN GLN B . n B 2 31 GLY 31 31 31 GLY GLY B . n B 2 32 SER 32 32 32 SER SER B . n B 2 33 GLY 33 33 33 GLY GLY B . n B 2 34 TYR 34 34 34 TYR TYR B . n B 2 35 ALA 35 35 35 ALA ALA B . n B 2 36 ALA 36 36 36 ALA ALA B . n B 2 37 ASP 37 37 37 ASP ASP B . n B 2 38 LYS 38 38 38 LYS LYS B . n B 2 39 GLU 39 39 39 GLU GLU B . n B 2 40 SER 40 40 40 SER SER B . n B 2 41 THR 41 41 41 THR THR B . n B 2 42 GLN 42 42 42 GLN GLN B . n B 2 43 LYS 43 43 43 LYS LYS B . n B 2 44 ALA 44 44 44 ALA ALA B . n B 2 45 ILE 45 45 45 ILE ILE B . n B 2 46 ASP 46 46 46 ASP ASP B . n B 2 47 GLY 47 47 47 GLY GLY B . n B 2 48 VAL 48 48 48 VAL VAL B . n B 2 49 THR 49 49 49 THR THR B . n B 2 50 ASN 50 50 50 ASN ASN B . n B 2 51 LYS 51 51 51 LYS LYS B . n B 2 52 VAL 52 52 52 VAL VAL B . n B 2 53 ASN 53 53 53 ASN ASN B . n B 2 54 SER 54 54 54 SER SER B . n B 2 55 ILE 55 55 55 ILE ILE B . n B 2 56 ILE 56 56 56 ILE ILE B . n B 2 57 ASP 57 57 57 ASP ASP B . n B 2 58 LYS 58 58 58 LYS LYS B . n B 2 59 MET 59 59 59 MET MET B . n B 2 60 ASN 60 60 60 ASN ASN B . n B 2 61 THR 61 61 61 THR THR B . n B 2 62 GLN 62 62 62 GLN GLN B . n B 2 63 PHE 63 63 63 PHE PHE B . n B 2 64 GLU 64 64 64 GLU GLU B . n B 2 65 ALA 65 65 65 ALA ALA B . n B 2 66 VAL 66 66 66 VAL VAL B . n B 2 67 GLY 67 67 67 GLY GLY B . n B 2 68 ARG 68 68 68 ARG ARG B . n B 2 69 GLU 69 69 69 GLU GLU B . n B 2 70 PHE 70 70 70 PHE PHE B . n B 2 71 ASN 71 71 71 ASN ASN B . n B 2 72 ASN 72 72 72 ASN ASN B . n B 2 73 LEU 73 73 73 LEU LEU B . n B 2 74 GLU 74 74 74 GLU GLU B . n B 2 75 ARG 75 75 75 ARG ARG B . n B 2 76 ARG 76 76 76 ARG ARG B . n B 2 77 ILE 77 77 77 ILE ILE B . n B 2 78 GLU 78 78 78 GLU GLU B . n B 2 79 ASN 79 79 79 ASN ASN B . n B 2 80 LEU 80 80 80 LEU LEU B . n B 2 81 ASN 81 81 81 ASN ASN B . n B 2 82 LYS 82 82 82 LYS LYS B . n B 2 83 LYS 83 83 83 LYS LYS B . n B 2 84 MET 84 84 84 MET MET B . n B 2 85 GLU 85 85 85 GLU GLU B . n B 2 86 ASP 86 86 86 ASP ASP B . n B 2 87 GLY 87 87 87 GLY GLY B . n B 2 88 PHE 88 88 88 PHE PHE B . n B 2 89 LEU 89 89 89 LEU LEU B . n B 2 90 ASP 90 90 90 ASP ASP B . n B 2 91 VAL 91 91 91 VAL VAL B . n B 2 92 TRP 92 92 92 TRP TRP B . n B 2 93 THR 93 93 93 THR THR B . n B 2 94 TYR 94 94 94 TYR TYR B . n B 2 95 ASN 95 95 95 ASN ASN B . n B 2 96 ALA 96 96 96 ALA ALA B . n B 2 97 GLU 97 97 97 GLU GLU B . n B 2 98 LEU 98 98 98 LEU LEU B . n B 2 99 LEU 99 99 99 LEU LEU B . n B 2 100 VAL 100 100 100 VAL VAL B . n B 2 101 LEU 101 101 101 LEU LEU B . n B 2 102 MET 102 102 102 MET MET B . n B 2 103 GLU 103 103 103 GLU GLU B . n B 2 104 ASN 104 104 104 ASN ASN B . n B 2 105 GLU 105 105 105 GLU GLU B . n B 2 106 ARG 106 106 106 ARG ARG B . n B 2 107 THR 107 107 107 THR THR B . n B 2 108 LEU 108 108 108 LEU LEU B . n B 2 109 ASP 109 109 109 ASP ASP B . n B 2 110 PHE 110 110 110 PHE PHE B . n B 2 111 HIS 111 111 111 HIS HIS B . n B 2 112 ASP 112 112 112 ASP ASP B . n B 2 113 SER 113 113 113 SER SER B . n B 2 114 ASN 114 114 114 ASN ASN B . n B 2 115 VAL 115 115 115 VAL VAL B . n B 2 116 LYS 116 116 116 LYS LYS B . n B 2 117 ASN 117 117 117 ASN ASN B . n B 2 118 LEU 118 118 118 LEU LEU B . n B 2 119 TYR 119 119 119 TYR TYR B . n B 2 120 ASP 120 120 120 ASP ASP B . n B 2 121 LYS 121 121 121 LYS LYS B . n B 2 122 VAL 122 122 122 VAL VAL B . n B 2 123 ARG 123 123 123 ARG ARG B . n B 2 124 LEU 124 124 124 LEU LEU B . n B 2 125 GLN 125 125 125 GLN GLN B . n B 2 126 LEU 126 126 126 LEU LEU B . n B 2 127 ARG 127 127 127 ARG ARG B . n B 2 128 ASP 128 128 128 ASP ASP B . n B 2 129 ASN 129 129 129 ASN ASN B . n B 2 130 ALA 130 130 130 ALA ALA B . n B 2 131 LYS 131 131 131 LYS LYS B . n B 2 132 GLU 132 132 132 GLU GLU B . n B 2 133 LEU 133 133 133 LEU LEU B . n B 2 134 GLY 134 134 134 GLY GLY B . n B 2 135 ASN 135 135 135 ASN ASN B . n B 2 136 GLY 136 136 136 GLY GLY B . n B 2 137 CYS 137 137 137 CYS CYS B . n B 2 138 PHE 138 138 138 PHE PHE B . n B 2 139 GLU 139 139 139 GLU GLU B . n B 2 140 PHE 140 140 140 PHE PHE B . n B 2 141 TYR 141 141 141 TYR TYR B . n B 2 142 HIS 142 142 142 HIS HIS B . n B 2 143 LYS 143 143 143 LYS LYS B . n B 2 144 CYS 144 144 144 CYS CYS B . n B 2 145 ASP 145 145 145 ASP ASP B . n B 2 146 ASN 146 146 146 ASN ASN B . n B 2 147 GLU 147 147 147 GLU GLU B . n B 2 148 CYS 148 148 148 CYS CYS B . n B 2 149 MET 149 149 149 MET MET B . n B 2 150 GLU 150 150 150 GLU GLU B . n B 2 151 SER 151 151 151 SER SER B . n B 2 152 VAL 152 152 152 VAL VAL B . n B 2 153 ARG 153 153 153 ARG ARG B . n B 2 154 ASN 154 154 154 ASN ASN B . n B 2 155 GLY 155 155 155 GLY GLY B . n B 2 156 THR 156 156 156 THR THR B . n B 2 157 TYR 157 157 157 TYR TYR B . n B 2 158 ASP 158 158 158 ASP ASP B . n B 2 159 TYR 159 159 159 TYR TYR B . n B 2 160 PRO 160 160 160 PRO PRO B . n B 2 161 GLN 161 161 161 GLN GLN B . n B 2 162 TYR 162 162 162 TYR TYR B . n B 2 163 SER 163 163 ? ? ? B . n B 2 164 GLU 164 164 ? ? ? B . n B 2 165 GLU 165 165 ? ? ? B . n B 2 166 ALA 166 166 ? ? ? B . n # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code C 3 NAG 1 1322 1322 NAG NAG A . D 3 NAG 1 1323 1323 NAG NAG A . E 3 NAG 2 1324 1324 NAG NAG A . F 3 NAG 1 1325 1325 NAG NAG A . G 3 NAG 2 1326 1326 NAG NAG A . H 4 BMA 3 1327 1327 BMA BMA A . I 5 MAN 4 1328 1328 MAN MAN A . J 5 MAN 5 1329 1329 MAN MAN A . K 3 NAG 1 1330 1330 NAG NAG A . L 6 SIA 1 1331 1331 SIA SIA A . M 7 GAL 2 1332 1332 GAL GAL A . N 3 NAG 3 1333 1333 NAG NAG A . O 3 NAG 1 1163 1163 NAG NAG B . P 3 NAG 2 1164 1164 NAG NAG B . Q 4 BMA 3 1165 1165 BMA BMA B . R 8 MPO 1 1166 1166 MPO MPO B . S 9 HOH 1 2001 2001 HOH HOH A . S 9 HOH 2 2002 2002 HOH HOH A . S 9 HOH 3 2003 2003 HOH HOH A . S 9 HOH 4 2004 2004 HOH HOH A . S 9 HOH 5 2005 2005 HOH HOH A . S 9 HOH 6 2006 2006 HOH HOH A . S 9 HOH 7 2007 2007 HOH HOH A . S 9 HOH 8 2008 2008 HOH HOH A . S 9 HOH 9 2009 2009 HOH HOH A . S 9 HOH 10 2010 2010 HOH HOH A . S 9 HOH 11 2011 2011 HOH HOH A . S 9 HOH 12 2012 2012 HOH HOH A . S 9 HOH 13 2013 2013 HOH HOH A . S 9 HOH 14 2014 2014 HOH HOH A . S 9 HOH 15 2015 2015 HOH HOH A . S 9 HOH 16 2016 2016 HOH HOH A . S 9 HOH 17 2017 2017 HOH HOH A . S 9 HOH 18 2018 2018 HOH HOH A . S 9 HOH 19 2019 2019 HOH HOH A . S 9 HOH 20 2020 2020 HOH HOH A . S 9 HOH 21 2021 2021 HOH HOH A . S 9 HOH 22 2022 2022 HOH HOH A . S 9 HOH 23 2023 2023 HOH HOH A . S 9 HOH 24 2024 2024 HOH HOH A . S 9 HOH 25 2025 2025 HOH HOH A . S 9 HOH 26 2026 2026 HOH HOH A . S 9 HOH 27 2027 2027 HOH HOH A . S 9 HOH 28 2028 2028 HOH HOH A . S 9 HOH 29 2029 2029 HOH HOH A . S 9 HOH 30 2030 2030 HOH HOH A . S 9 HOH 31 2031 2031 HOH HOH A . S 9 HOH 32 2032 2032 HOH HOH A . S 9 HOH 33 2033 2033 HOH HOH A . S 9 HOH 34 2034 2034 HOH HOH A . S 9 HOH 35 2035 2035 HOH HOH A . S 9 HOH 36 2036 2036 HOH HOH A . S 9 HOH 37 2037 2037 HOH HOH A . S 9 HOH 38 2038 2038 HOH HOH A . S 9 HOH 39 2039 2039 HOH HOH A . S 9 HOH 40 2040 2040 HOH HOH A . S 9 HOH 41 2041 2041 HOH HOH A . S 9 HOH 42 2042 2042 HOH HOH A . S 9 HOH 43 2043 2043 HOH HOH A . S 9 HOH 44 2044 2044 HOH HOH A . S 9 HOH 45 2045 2045 HOH HOH A . S 9 HOH 46 2046 2046 HOH HOH A . S 9 HOH 47 2047 2047 HOH HOH A . S 9 HOH 48 2048 2048 HOH HOH A . S 9 HOH 49 2049 2049 HOH HOH A . S 9 HOH 50 2050 2050 HOH HOH A . S 9 HOH 51 2051 2051 HOH HOH A . S 9 HOH 52 2052 2052 HOH HOH A . S 9 HOH 53 2053 2053 HOH HOH A . S 9 HOH 54 2054 2054 HOH HOH A . S 9 HOH 55 2055 2055 HOH HOH A . S 9 HOH 56 2056 2056 HOH HOH A . S 9 HOH 57 2057 2057 HOH HOH A . S 9 HOH 58 2058 2058 HOH HOH A . S 9 HOH 59 2059 2059 HOH HOH A . S 9 HOH 60 2060 2060 HOH HOH A . S 9 HOH 61 2061 2061 HOH HOH A . S 9 HOH 62 2062 2062 HOH HOH A . S 9 HOH 63 2063 2063 HOH HOH A . S 9 HOH 64 2064 2064 HOH HOH A . S 9 HOH 65 2065 2065 HOH HOH A . S 9 HOH 66 2066 2066 HOH HOH A . S 9 HOH 67 2067 2067 HOH HOH A . S 9 HOH 68 2068 2068 HOH HOH A . S 9 HOH 69 2069 2069 HOH HOH A . S 9 HOH 70 2070 2070 HOH HOH A . S 9 HOH 71 2071 2071 HOH HOH A . S 9 HOH 72 2072 2072 HOH HOH A . S 9 HOH 73 2073 2073 HOH HOH A . S 9 HOH 74 2074 2074 HOH HOH A . S 9 HOH 75 2075 2075 HOH HOH A . S 9 HOH 76 2076 2076 HOH HOH A . S 9 HOH 77 2077 2077 HOH HOH A . S 9 HOH 78 2078 2078 HOH HOH A . S 9 HOH 79 2079 2079 HOH HOH A . S 9 HOH 80 2080 2080 HOH HOH A . S 9 HOH 81 2081 2081 HOH HOH A . S 9 HOH 82 2082 2082 HOH HOH A . S 9 HOH 83 2083 2083 HOH HOH A . S 9 HOH 84 2084 2084 HOH HOH A . S 9 HOH 85 2085 2085 HOH HOH A . S 9 HOH 86 2086 2086 HOH HOH A . S 9 HOH 87 2087 2087 HOH HOH A . S 9 HOH 88 2088 2088 HOH HOH A . S 9 HOH 89 2089 2089 HOH HOH A . S 9 HOH 90 2090 2090 HOH HOH A . S 9 HOH 91 2091 2091 HOH HOH A . S 9 HOH 92 2092 2092 HOH HOH A . S 9 HOH 93 2093 2093 HOH HOH A . S 9 HOH 94 2094 2094 HOH HOH A . S 9 HOH 95 2095 2095 HOH HOH A . S 9 HOH 96 2096 2096 HOH HOH A . T 9 HOH 1 2001 2001 HOH HOH B . T 9 HOH 2 2002 2002 HOH HOH B . T 9 HOH 3 2003 2003 HOH HOH B . T 9 HOH 4 2004 2004 HOH HOH B . T 9 HOH 5 2005 2005 HOH HOH B . T 9 HOH 6 2006 2006 HOH HOH B . T 9 HOH 7 2007 2007 HOH HOH B . T 9 HOH 8 2008 2008 HOH HOH B . T 9 HOH 9 2009 2009 HOH HOH B . T 9 HOH 10 2010 2010 HOH HOH B . T 9 HOH 11 2011 2011 HOH HOH B . T 9 HOH 12 2012 2012 HOH HOH B . T 9 HOH 13 2013 2013 HOH HOH B . T 9 HOH 14 2014 2014 HOH HOH B . T 9 HOH 15 2015 2015 HOH HOH B . T 9 HOH 16 2016 2016 HOH HOH B . T 9 HOH 17 2017 2017 HOH HOH B . T 9 HOH 18 2018 2018 HOH HOH B . T 9 HOH 19 2019 2019 HOH HOH B . T 9 HOH 20 2020 2020 HOH HOH B . T 9 HOH 21 2021 2021 HOH HOH B . T 9 HOH 22 2022 2022 HOH HOH B . T 9 HOH 23 2023 2023 HOH HOH B . T 9 HOH 24 2024 2024 HOH HOH B . T 9 HOH 25 2025 2025 HOH HOH B . T 9 HOH 26 2026 2026 HOH HOH B . T 9 HOH 27 2027 2027 HOH HOH B . T 9 HOH 28 2028 2028 HOH HOH B . T 9 HOH 29 2029 2029 HOH HOH B . T 9 HOH 30 2030 2030 HOH HOH B . T 9 HOH 31 2031 2031 HOH HOH B . T 9 HOH 32 2032 2032 HOH HOH B . T 9 HOH 33 2033 2033 HOH HOH B . T 9 HOH 34 2034 2034 HOH HOH B . T 9 HOH 35 2035 2035 HOH HOH B . T 9 HOH 36 2036 2036 HOH HOH B . T 9 HOH 37 2037 2037 HOH HOH B . T 9 HOH 38 2038 2038 HOH HOH B . T 9 HOH 39 2039 2039 HOH HOH B . T 9 HOH 40 2040 2040 HOH HOH B . T 9 HOH 41 2041 2041 HOH HOH B . T 9 HOH 42 2042 2042 HOH HOH B . T 9 HOH 43 2043 2043 HOH HOH B . T 9 HOH 44 2044 2044 HOH HOH B . T 9 HOH 45 2045 2045 HOH HOH B . T 9 HOH 46 2046 2046 HOH HOH B . T 9 HOH 47 2047 2047 HOH HOH B . T 9 HOH 48 2048 2048 HOH HOH B . T 9 HOH 49 2049 2049 HOH HOH B . T 9 HOH 50 2050 2050 HOH HOH B . T 9 HOH 51 2051 2051 HOH HOH B . T 9 HOH 52 2052 2052 HOH HOH B . T 9 HOH 53 2053 2053 HOH HOH B . T 9 HOH 54 2054 2054 HOH HOH B . T 9 HOH 55 2055 2055 HOH HOH B . T 9 HOH 56 2056 2056 HOH HOH B . T 9 HOH 57 2057 2057 HOH HOH B . T 9 HOH 58 2058 2058 HOH HOH B . T 9 HOH 59 2059 2059 HOH HOH B . T 9 HOH 60 2060 2060 HOH HOH B . T 9 HOH 61 2061 2061 HOH HOH B . T 9 HOH 62 2062 2062 HOH HOH B . T 9 HOH 63 2063 2063 HOH HOH B . T 9 HOH 64 2064 2064 HOH HOH B . T 9 HOH 65 2065 2065 HOH HOH B . T 9 HOH 66 2066 2066 HOH HOH B . T 9 HOH 67 2067 2067 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,T # 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)' 38680 ? 1 MORE -14.2 ? 1 'SSA (A^2)' 64320 ? # 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 50.7900000000 0.8660254038 -0.5000000000 0.0000000000 -87.9708605164 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 101.5800000000 -0.8660254038 -0.5000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 # loop_ _pdbx_struct_special_symmetry.id _pdbx_struct_special_symmetry.PDB_model_num _pdbx_struct_special_symmetry.auth_asym_id _pdbx_struct_special_symmetry.auth_comp_id _pdbx_struct_special_symmetry.auth_seq_id _pdbx_struct_special_symmetry.PDB_ins_code _pdbx_struct_special_symmetry.label_asym_id _pdbx_struct_special_symmetry.label_comp_id _pdbx_struct_special_symmetry.label_seq_id 1 1 B HOH 2020 ? T HOH . 2 1 B HOH 2042 ? T HOH . # _pdbx_audit_revision_history.ordinal 1 _pdbx_audit_revision_history.data_content_type 'Structure model' _pdbx_audit_revision_history.major_revision 1 _pdbx_audit_revision_history.minor_revision 0 _pdbx_audit_revision_history.revision_date 2015-03-25 # _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 ? # 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 34.4277 -14.0946 -18.9323 0.1779 0.3687 0.0910 0.1573 0.0169 -0.1201 0.4260 0.4597 5.3683 -0.0957 -0.1859 0.0833 -0.0239 -0.1360 0.0715 0.1301 -0.1121 0.1408 -0.7953 -1.1467 0.1360 'X-RAY DIFFRACTION' 2 ? refined 32.4162 -21.5083 16.4655 0.4939 0.7801 0.0652 0.0386 0.0975 -0.1186 1.8270 2.2021 2.9674 0.1827 0.0982 -0.8741 -0.0952 -0.4129 0.0956 0.8162 -0.1146 0.0670 -0.2903 -0.8672 0.2098 'X-RAY DIFFRACTION' 3 ? refined 35.5854 -14.8127 -27.0905 0.1934 0.1849 0.1212 0.0960 0.0242 -0.0966 1.4151 0.1260 11.8955 -0.0461 -1.6287 1.1427 0.0894 -0.2280 0.2134 0.0189 -0.0674 0.0381 -0.0322 -0.4008 -0.0220 'X-RAY DIFFRACTION' 4 ? refined 36.2120 -21.1929 -58.9553 0.1303 0.2795 0.2273 0.0759 -0.0306 -0.0524 1.3073 2.1094 8.3105 -1.2710 1.8925 -1.2297 -0.0490 0.0940 0.0304 0.1777 -0.1216 0.1494 -0.2471 -1.0378 0.1706 'X-RAY DIFFRACTION' 5 ? refined 48.2333 -22.7839 -10.5215 0.1170 0.0572 0.0531 0.0321 -0.0196 -0.0377 8.7203 3.2354 18.0073 2.4129 6.3924 2.6139 -0.0023 0.0239 0.0249 -0.0373 -0.2437 0.3686 -0.6534 -0.5202 0.2460 'X-RAY DIFFRACTION' 6 ? refined 44.6276 -24.0527 -56.9676 0.0705 0.1115 0.1187 0.0218 -0.0226 -0.0196 1.5192 0.6234 12.6505 -0.5987 2.4841 -0.7952 0.0978 0.1399 0.0398 0.0298 -0.2143 0.0063 0.3263 0.2028 0.1165 'X-RAY DIFFRACTION' 7 ? refined 31.6320 -26.3787 -80.9056 0.3427 0.7430 0.4580 0.0548 -0.2454 -0.2761 7.5579 7.6324 11.6030 -5.7121 -0.6421 -3.4846 0.4077 1.6262 -1.3055 -0.6724 -0.2128 1.3272 0.9746 -0.9500 -0.1949 # 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 5AJM _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 ? ? 63.93 -117.34 2 1 ASP A 88 ? ? -102.08 -118.42 3 1 CYS A 135 ? ? -116.13 75.57 4 1 ASP A 171 ? ? -38.53 145.42 5 1 GLN A 192 ? ? 69.09 -65.43 6 1 THR A 202 ? ? -128.69 -161.20 7 1 ASN A 273 ? ? 50.73 72.48 8 1 ARG B 127 ? ? 53.64 -130.05 # loop_ _pdbx_validate_chiral.id _pdbx_validate_chiral.PDB_model_num _pdbx_validate_chiral.auth_atom_id _pdbx_validate_chiral.label_alt_id _pdbx_validate_chiral.auth_asym_id _pdbx_validate_chiral.auth_comp_id _pdbx_validate_chiral.auth_seq_id _pdbx_validate_chiral.PDB_ins_code _pdbx_validate_chiral.details _pdbx_validate_chiral.omega 1 1 C1 ? A NAG 1326 ? 'WRONG HAND' . 2 1 C1 ? A BMA 1327 ? 'WRONG HAND' . 3 1 C1 ? A MAN 1328 ? 'WRONG HAND' . 4 1 C1 ? B NAG 1163 ? 'WRONG HAND' . # loop_ _pdbx_unobs_or_zero_occ_residues.id _pdbx_unobs_or_zero_occ_residues.PDB_model_num _pdbx_unobs_or_zero_occ_residues.polymer_flag _pdbx_unobs_or_zero_occ_residues.occupancy_flag _pdbx_unobs_or_zero_occ_residues.auth_asym_id _pdbx_unobs_or_zero_occ_residues.auth_comp_id _pdbx_unobs_or_zero_occ_residues.auth_seq_id _pdbx_unobs_or_zero_occ_residues.PDB_ins_code _pdbx_unobs_or_zero_occ_residues.label_asym_id _pdbx_unobs_or_zero_occ_residues.label_comp_id _pdbx_unobs_or_zero_occ_residues.label_seq_id 1 1 Y 1 A GLN 322 ? A GLN 322 2 1 Y 1 A ARG 323 ? A ARG 323 3 1 Y 1 A GLU 324 ? A GLU 324 4 1 Y 1 A THR 325 ? A THR 325 5 1 Y 1 A ARG 326 ? A ARG 326 6 1 Y 1 B SER 163 ? B SER 163 7 1 Y 1 B GLU 164 ? B GLU 164 8 1 Y 1 B GLU 165 ? B GLU 165 9 1 Y 1 B ALA 166 ? B ALA 166 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 3 N-ACETYL-D-GLUCOSAMINE NAG 4 BETA-D-MANNOSE BMA 5 ALPHA-D-MANNOSE MAN 6 'O-SIALIC ACID' SIA 7 BETA-D-GALACTOSE GAL 8 '3[N-MORPHOLINO]PROPANE SULFONIC ACID' MPO 9 water HOH #