data_3MJ7 # _entry.id 3MJ7 # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.281 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 3MJ7 RCSB RCSB058611 WWPDB D_1000058611 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.details _pdbx_database_related.content_type PDB 3MJ6 . unspecified PDB 3MJ8 . unspecified PDB 3MJ9 . unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 3MJ7 _pdbx_database_status.recvd_initial_deposition_date 2010-04-12 _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site RCSB _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.SG_entry ? _pdbx_database_status.pdb_format_compatible Y _pdbx_database_status.status_code_cs ? # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Verdino, P.' 1 'Wilson, I.A.' 2 # loop_ _citation.id _citation.title _citation.journal_abbrev _citation.journal_volume _citation.page_first _citation.page_last _citation.year _citation.journal_id_ASTM _citation.country _citation.journal_id_ISSN _citation.journal_id_CSD _citation.book_publisher _citation.pdbx_database_id_PubMed _citation.pdbx_database_id_DOI primary 'The molecular interaction of CAR and JAML recruits the central cell signal transducer PI3K.' Science 329 1210 1214 2010 SCIEAS US 0036-8075 0038 ? 20813955 10.1126/science.1187996 1 'The junctional adhesion molecule JAML is a costimulatory receptor for epithelial gammadelta T cell activation.' Science 329 1205 1210 2010 SCIEAS US 0036-8075 0038 ? 20813954 10.1126/science.1192698 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Verdino, P.' 1 primary 'Witherden, D.A.' 2 primary 'Havran, W.L.' 3 primary 'Wilson, I.A.' 4 1 'Witherden, D.A.' 5 1 'Verdino, P.' 6 1 'Rieder, S.E.' 7 1 'Garijo, O.' 8 1 'Mills, R.E.' 9 1 'Teyton, L.' 10 1 'Fischer, W.H.' 11 1 'Wilson, I.A.' 12 1 'Havran, W.L.' 13 # _cell.entry_id 3MJ7 _cell.length_a 89.865 _cell.length_b 89.865 _cell.length_c 127.170 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 120.00 _cell.Z_PDB 6 _cell.pdbx_unique_axis ? _cell.length_a_esd ? _cell.length_b_esd ? _cell.length_c_esd ? _cell.angle_alpha_esd ? _cell.angle_beta_esd ? _cell.angle_gamma_esd ? # _symmetry.entry_id 3MJ7 _symmetry.space_group_name_H-M 'P 31 1 2' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 151 _symmetry.space_group_name_Hall ? # 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 man 'Junctional adhesion molecule-like' 30647.387 1 ? 'K124R, R211Q' 'EXTRACELLULAR DOMAIN (UNP RESIDUES 21-280)' ? 2 polymer man 'Coxsackievirus and adenovirus receptor homolog' 25046.229 1 ? ? 'EXTRACELLULAR DOMAIN (UNP RESIDUES 18-236)' ? 3 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 5 ? ? ? ? 4 non-polymer man BETA-D-MANNOSE 180.156 1 ? ? ? ? 5 non-polymer man ALPHA-D-MANNOSE 180.156 1 ? ? ? ? 6 non-polymer man ALPHA-L-FUCOSE 164.156 1 ? ? ? ? # loop_ _entity_name_com.entity_id _entity_name_com.name 1 'Dendritic cell-specific protein CREA7, mCrea7' 2 'CAR, mCAR' # 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 ;RSQGLPGLTVSSPQLRVHVGESVLMGCVVQRTEEKHVDRVDWLFSKDKDDASEYVLFYYSNLSVPTGRFQNRSHLVGDTF HNDGSLLLQDVQKADEGIYTCEIRLKNESMVMKKPVELWVLPEEPRDLRVRVGDTTQMRCSIQSTEEKRVTKVNWMFSSG SHTEEETVLSYDSNMRSGKFQSLGRFRNRVDLTGDISRNDGSIKLQTVKESDQGIYTCSIYVGKLESRKTIVLHVVQDEF QRTISPTPPTDKGQQGILNGNQHHHHHH ; ;RSQGLPGLTVSSPQLRVHVGESVLMGCVVQRTEEKHVDRVDWLFSKDKDDASEYVLFYYSNLSVPTGRFQNRSHLVGDTF HNDGSLLLQDVQKADEGIYTCEIRLKNESMVMKKPVELWVLPEEPRDLRVRVGDTTQMRCSIQSTEEKRVTKVNWMFSSG SHTEEETVLSYDSNMRSGKFQSLGRFRNRVDLTGDISRNDGSIKLQTVKESDQGIYTCSIYVGKLESRKTIVLHVVQDEF QRTISPTPPTDKGQQGILNGNQHHHHHH ; A ? 2 'polypeptide(L)' no no ;SGLSITTPEQRIEKAKGETAYLPCKFTLSPEDQGPLDIEWLISPSDNQIVDQVIILYSGDKIYDNYYPDLKGRVHFTSND VKSGDASINVTNLQLSDIGTYQCKVKKAPGVANKKFLLTVLVKPSGTRCFVDGSEEIGNDFKLKCEPKEGSLPLQFEWQK LSDSQTMPTPWLAEMTSPVISVKNASSEYSGTYSCTVQNRVGSDQCMLRLDVVPPSNRAHHHHHH ; ;SGLSITTPEQRIEKAKGETAYLPCKFTLSPEDQGPLDIEWLISPSDNQIVDQVIILYSGDKIYDNYYPDLKGRVHFTSND VKSGDASINVTNLQLSDIGTYQCKVKKAPGVANKKFLLTVLVKPSGTRCFVDGSEEIGNDFKLKCEPKEGSLPLQFEWQK LSDSQTMPTPWLAEMTSPVISVKNASSEYSGTYSCTVQNRVGSDQCMLRLDVVPPSNRAHHHHHH ; B ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 ARG n 1 2 SER n 1 3 GLN n 1 4 GLY n 1 5 LEU n 1 6 PRO n 1 7 GLY n 1 8 LEU n 1 9 THR n 1 10 VAL n 1 11 SER n 1 12 SER n 1 13 PRO n 1 14 GLN n 1 15 LEU n 1 16 ARG n 1 17 VAL n 1 18 HIS n 1 19 VAL n 1 20 GLY n 1 21 GLU n 1 22 SER n 1 23 VAL n 1 24 LEU n 1 25 MET n 1 26 GLY n 1 27 CYS n 1 28 VAL n 1 29 VAL n 1 30 GLN n 1 31 ARG n 1 32 THR n 1 33 GLU n 1 34 GLU n 1 35 LYS n 1 36 HIS n 1 37 VAL n 1 38 ASP n 1 39 ARG n 1 40 VAL n 1 41 ASP n 1 42 TRP n 1 43 LEU n 1 44 PHE n 1 45 SER n 1 46 LYS n 1 47 ASP n 1 48 LYS n 1 49 ASP n 1 50 ASP n 1 51 ALA n 1 52 SER n 1 53 GLU n 1 54 TYR n 1 55 VAL n 1 56 LEU n 1 57 PHE n 1 58 TYR n 1 59 TYR n 1 60 SER n 1 61 ASN n 1 62 LEU n 1 63 SER n 1 64 VAL n 1 65 PRO n 1 66 THR n 1 67 GLY n 1 68 ARG n 1 69 PHE n 1 70 GLN n 1 71 ASN n 1 72 ARG n 1 73 SER n 1 74 HIS n 1 75 LEU n 1 76 VAL n 1 77 GLY n 1 78 ASP n 1 79 THR n 1 80 PHE n 1 81 HIS n 1 82 ASN n 1 83 ASP n 1 84 GLY n 1 85 SER n 1 86 LEU n 1 87 LEU n 1 88 LEU n 1 89 GLN n 1 90 ASP n 1 91 VAL n 1 92 GLN n 1 93 LYS n 1 94 ALA n 1 95 ASP n 1 96 GLU n 1 97 GLY n 1 98 ILE n 1 99 TYR n 1 100 THR n 1 101 CYS n 1 102 GLU n 1 103 ILE n 1 104 ARG n 1 105 LEU n 1 106 LYS n 1 107 ASN n 1 108 GLU n 1 109 SER n 1 110 MET n 1 111 VAL n 1 112 MET n 1 113 LYS n 1 114 LYS n 1 115 PRO n 1 116 VAL n 1 117 GLU n 1 118 LEU n 1 119 TRP n 1 120 VAL n 1 121 LEU n 1 122 PRO n 1 123 GLU n 1 124 GLU n 1 125 PRO n 1 126 ARG n 1 127 ASP n 1 128 LEU n 1 129 ARG n 1 130 VAL n 1 131 ARG n 1 132 VAL n 1 133 GLY n 1 134 ASP n 1 135 THR n 1 136 THR n 1 137 GLN n 1 138 MET n 1 139 ARG n 1 140 CYS n 1 141 SER n 1 142 ILE n 1 143 GLN n 1 144 SER n 1 145 THR n 1 146 GLU n 1 147 GLU n 1 148 LYS n 1 149 ARG n 1 150 VAL n 1 151 THR n 1 152 LYS n 1 153 VAL n 1 154 ASN n 1 155 TRP n 1 156 MET n 1 157 PHE n 1 158 SER n 1 159 SER n 1 160 GLY n 1 161 SER n 1 162 HIS n 1 163 THR n 1 164 GLU n 1 165 GLU n 1 166 GLU n 1 167 THR n 1 168 VAL n 1 169 LEU n 1 170 SER n 1 171 TYR n 1 172 ASP n 1 173 SER n 1 174 ASN n 1 175 MET n 1 176 ARG n 1 177 SER n 1 178 GLY n 1 179 LYS n 1 180 PHE n 1 181 GLN n 1 182 SER n 1 183 LEU n 1 184 GLY n 1 185 ARG n 1 186 PHE n 1 187 ARG n 1 188 ASN n 1 189 ARG n 1 190 VAL n 1 191 ASP n 1 192 LEU n 1 193 THR n 1 194 GLY n 1 195 ASP n 1 196 ILE n 1 197 SER n 1 198 ARG n 1 199 ASN n 1 200 ASP n 1 201 GLY n 1 202 SER n 1 203 ILE n 1 204 LYS n 1 205 LEU n 1 206 GLN n 1 207 THR n 1 208 VAL n 1 209 LYS n 1 210 GLU n 1 211 SER n 1 212 ASP n 1 213 GLN n 1 214 GLY n 1 215 ILE n 1 216 TYR n 1 217 THR n 1 218 CYS n 1 219 SER n 1 220 ILE n 1 221 TYR n 1 222 VAL n 1 223 GLY n 1 224 LYS n 1 225 LEU n 1 226 GLU n 1 227 SER n 1 228 ARG n 1 229 LYS n 1 230 THR n 1 231 ILE n 1 232 VAL n 1 233 LEU n 1 234 HIS n 1 235 VAL n 1 236 VAL n 1 237 GLN n 1 238 ASP n 1 239 GLU n 1 240 PHE n 1 241 GLN n 1 242 ARG n 1 243 THR n 1 244 ILE n 1 245 SER n 1 246 PRO n 1 247 THR n 1 248 PRO n 1 249 PRO n 1 250 THR n 1 251 ASP n 1 252 LYS n 1 253 GLY n 1 254 GLN n 1 255 GLN n 1 256 GLY n 1 257 ILE n 1 258 LEU n 1 259 ASN n 1 260 GLY n 1 261 ASN n 1 262 GLN n 1 263 HIS n 1 264 HIS n 1 265 HIS n 1 266 HIS n 1 267 HIS n 1 268 HIS n 2 1 SER n 2 2 GLY n 2 3 LEU n 2 4 SER n 2 5 ILE n 2 6 THR n 2 7 THR n 2 8 PRO n 2 9 GLU n 2 10 GLN n 2 11 ARG n 2 12 ILE n 2 13 GLU n 2 14 LYS n 2 15 ALA n 2 16 LYS n 2 17 GLY n 2 18 GLU n 2 19 THR n 2 20 ALA n 2 21 TYR n 2 22 LEU n 2 23 PRO n 2 24 CYS n 2 25 LYS n 2 26 PHE n 2 27 THR n 2 28 LEU n 2 29 SER n 2 30 PRO n 2 31 GLU n 2 32 ASP n 2 33 GLN n 2 34 GLY n 2 35 PRO n 2 36 LEU n 2 37 ASP n 2 38 ILE n 2 39 GLU n 2 40 TRP n 2 41 LEU n 2 42 ILE n 2 43 SER n 2 44 PRO n 2 45 SER n 2 46 ASP n 2 47 ASN n 2 48 GLN n 2 49 ILE n 2 50 VAL n 2 51 ASP n 2 52 GLN n 2 53 VAL n 2 54 ILE n 2 55 ILE n 2 56 LEU n 2 57 TYR n 2 58 SER n 2 59 GLY n 2 60 ASP n 2 61 LYS n 2 62 ILE n 2 63 TYR n 2 64 ASP n 2 65 ASN n 2 66 TYR n 2 67 TYR n 2 68 PRO n 2 69 ASP n 2 70 LEU n 2 71 LYS n 2 72 GLY n 2 73 ARG n 2 74 VAL n 2 75 HIS n 2 76 PHE n 2 77 THR n 2 78 SER n 2 79 ASN n 2 80 ASP n 2 81 VAL n 2 82 LYS n 2 83 SER n 2 84 GLY n 2 85 ASP n 2 86 ALA n 2 87 SER n 2 88 ILE n 2 89 ASN n 2 90 VAL n 2 91 THR n 2 92 ASN n 2 93 LEU n 2 94 GLN n 2 95 LEU n 2 96 SER n 2 97 ASP n 2 98 ILE n 2 99 GLY n 2 100 THR n 2 101 TYR n 2 102 GLN n 2 103 CYS n 2 104 LYS n 2 105 VAL n 2 106 LYS n 2 107 LYS n 2 108 ALA n 2 109 PRO n 2 110 GLY n 2 111 VAL n 2 112 ALA n 2 113 ASN n 2 114 LYS n 2 115 LYS n 2 116 PHE n 2 117 LEU n 2 118 LEU n 2 119 THR n 2 120 VAL n 2 121 LEU n 2 122 VAL n 2 123 LYS n 2 124 PRO n 2 125 SER n 2 126 GLY n 2 127 THR n 2 128 ARG n 2 129 CYS n 2 130 PHE n 2 131 VAL n 2 132 ASP n 2 133 GLY n 2 134 SER n 2 135 GLU n 2 136 GLU n 2 137 ILE n 2 138 GLY n 2 139 ASN n 2 140 ASP n 2 141 PHE n 2 142 LYS n 2 143 LEU n 2 144 LYS n 2 145 CYS n 2 146 GLU n 2 147 PRO n 2 148 LYS n 2 149 GLU n 2 150 GLY n 2 151 SER n 2 152 LEU n 2 153 PRO n 2 154 LEU n 2 155 GLN n 2 156 PHE n 2 157 GLU n 2 158 TRP n 2 159 GLN n 2 160 LYS n 2 161 LEU n 2 162 SER n 2 163 ASP n 2 164 SER n 2 165 GLN n 2 166 THR n 2 167 MET n 2 168 PRO n 2 169 THR n 2 170 PRO n 2 171 TRP n 2 172 LEU n 2 173 ALA n 2 174 GLU n 2 175 MET n 2 176 THR n 2 177 SER n 2 178 PRO n 2 179 VAL n 2 180 ILE n 2 181 SER n 2 182 VAL n 2 183 LYS n 2 184 ASN n 2 185 ALA n 2 186 SER n 2 187 SER n 2 188 GLU n 2 189 TYR n 2 190 SER n 2 191 GLY n 2 192 THR n 2 193 TYR n 2 194 SER n 2 195 CYS n 2 196 THR n 2 197 VAL n 2 198 GLN n 2 199 ASN n 2 200 ARG n 2 201 VAL n 2 202 GLY n 2 203 SER n 2 204 ASP n 2 205 GLN n 2 206 CYS n 2 207 MET n 2 208 LEU n 2 209 ARG n 2 210 LEU n 2 211 ASP n 2 212 VAL n 2 213 VAL n 2 214 PRO n 2 215 PRO n 2 216 SER n 2 217 ASN n 2 218 ARG n 2 219 ALA n 2 220 HIS n 2 221 HIS n 2 222 HIS n 2 223 HIS n 2 224 HIS n 2 225 HIS n # loop_ _entity_src_gen.entity_id _entity_src_gen.pdbx_src_id _entity_src_gen.pdbx_alt_source_flag _entity_src_gen.pdbx_seq_type _entity_src_gen.pdbx_beg_seq_num _entity_src_gen.pdbx_end_seq_num _entity_src_gen.gene_src_common_name _entity_src_gen.gene_src_genus _entity_src_gen.pdbx_gene_src_gene _entity_src_gen.gene_src_species _entity_src_gen.gene_src_strain _entity_src_gen.gene_src_tissue _entity_src_gen.gene_src_tissue_fraction _entity_src_gen.gene_src_details _entity_src_gen.pdbx_gene_src_fragment _entity_src_gen.pdbx_gene_src_scientific_name _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id _entity_src_gen.pdbx_gene_src_variant _entity_src_gen.pdbx_gene_src_cell_line _entity_src_gen.pdbx_gene_src_atcc _entity_src_gen.pdbx_gene_src_organ _entity_src_gen.pdbx_gene_src_organelle _entity_src_gen.pdbx_gene_src_cell _entity_src_gen.pdbx_gene_src_cellular_location _entity_src_gen.host_org_common_name _entity_src_gen.pdbx_host_org_scientific_name _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id _entity_src_gen.host_org_genus _entity_src_gen.pdbx_host_org_gene _entity_src_gen.pdbx_host_org_organ _entity_src_gen.host_org_species _entity_src_gen.pdbx_host_org_tissue _entity_src_gen.pdbx_host_org_tissue_fraction _entity_src_gen.pdbx_host_org_strain _entity_src_gen.pdbx_host_org_variant _entity_src_gen.pdbx_host_org_cell_line _entity_src_gen.pdbx_host_org_atcc _entity_src_gen.pdbx_host_org_culture_collection _entity_src_gen.pdbx_host_org_cell _entity_src_gen.pdbx_host_org_organelle _entity_src_gen.pdbx_host_org_cellular_location _entity_src_gen.pdbx_host_org_vector_type _entity_src_gen.pdbx_host_org_vector _entity_src_gen.host_org_details _entity_src_gen.expression_system_id _entity_src_gen.plasmid_name _entity_src_gen.plasmid_details _entity_src_gen.pdbx_description 1 1 sample ? ? ? mouse ? 'Amica1, Gm638, Jaml' ? ? ? ? ? ? 'Mus musculus' 10090 ? ? ? ? ? ? ? 'FRUIT FLY' 'DROSOPHILA MELANOGASTER' 7227 ? ? ? ? ? ? ? ? ? ? ? ? ? ? plasmid ? ? ? 'PMT/BIP/V5-HIS A' ? ? 2 1 sample ? ? ? mouse ? 'Car, Cxadr' ? ? ? ? ? ? 'Mus musculus' 10090 ? ? ? ? ? ? ? 'fall armyworm' 'Spodoptera frugiperda' 7108 ? ? ? ? ? ? ? ? ? ? ? ? ? ? plasmid ? ? ? PBAC6 ? ? # loop_ _struct_ref.id _struct_ref.db_name _struct_ref.db_code _struct_ref.pdbx_db_accession _struct_ref.entity_id _struct_ref.pdbx_seq_one_letter_code _struct_ref.pdbx_align_begin _struct_ref.pdbx_db_isoform 1 UNP JAML1_MOUSE Q80UL9 1 ;QGLPGLTVSSPQLRVHVGESVLMGCVVQRTEEKHVDRVDWLFSKDKDDASEYVLFYYSNLSVPTGRFQNRSHLVGDTFHN DGSLLLQDVQKADEGIYTCEIRLKNESMVMKKPVELWVLPEEPKDLRVRVGDTTQMRCSIQSTEEKRVTKVNWMFSSGSH TEEETVLSYDSNMRSGKFQSLGRFRNRVDLTGDISRNDGSIKLQTVKESDRGIYTCSIYVGKLESRKTIVLHVVQDEFQR TISPTPPTDKGQQGILNGNQ ; 21 ? 2 UNP CXAR_MOUSE P97792 2 ;SGLSITTPEQRIEKAKGETAYLPCKFTLSPEDQGPLDIEWLISPSDNQIVDQVIILYSGDKIYDNYYPDLKGRVHFTSND VKSGDASINVTNLQLSDIGTYQCKVKKAPGVANKKFLLTVLVKPSGTRCFVDGSEEIGNDFKLKCEPKEGSLPLQFEWQK LSDSQTMPTPWLAEMTSPVISVKNASSEYSGTYSCTVQNRVGSDQCMLRLDVVPPSNRA ; 18 ? # 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 3MJ7 A 3 ? 262 ? Q80UL9 21 ? 280 ? 1 260 2 2 3MJ7 B 1 ? 219 ? P97792 18 ? 236 ? -1 217 # 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 3MJ7 ARG A 1 ? UNP Q80UL9 ? ? 'EXPRESSION TAG' -1 1 1 3MJ7 SER A 2 ? UNP Q80UL9 ? ? 'EXPRESSION TAG' 0 2 1 3MJ7 ARG A 126 ? UNP Q80UL9 LYS 144 'ENGINEERED MUTATION' 124 3 1 3MJ7 GLN A 213 ? UNP Q80UL9 ARG 231 'ENGINEERED MUTATION' 211 4 1 3MJ7 HIS A 263 ? UNP Q80UL9 ? ? 'EXPRESSION TAG' 261 5 1 3MJ7 HIS A 264 ? UNP Q80UL9 ? ? 'EXPRESSION TAG' 262 6 1 3MJ7 HIS A 265 ? UNP Q80UL9 ? ? 'EXPRESSION TAG' 263 7 1 3MJ7 HIS A 266 ? UNP Q80UL9 ? ? 'EXPRESSION TAG' 264 8 1 3MJ7 HIS A 267 ? UNP Q80UL9 ? ? 'EXPRESSION TAG' 265 9 1 3MJ7 HIS A 268 ? UNP Q80UL9 ? ? 'EXPRESSION TAG' 266 10 2 3MJ7 HIS B 220 ? UNP P97792 ? ? 'EXPRESSION TAG' 218 11 2 3MJ7 HIS B 221 ? UNP P97792 ? ? 'EXPRESSION TAG' 219 12 2 3MJ7 HIS B 222 ? UNP P97792 ? ? 'EXPRESSION TAG' 220 13 2 3MJ7 HIS B 223 ? UNP P97792 ? ? 'EXPRESSION TAG' 221 14 2 3MJ7 HIS B 224 ? UNP P97792 ? ? 'EXPRESSION TAG' 222 15 2 3MJ7 HIS B 225 ? UNP P97792 ? ? 'EXPRESSION TAG' 223 16 # 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 FUC saccharide . ALPHA-L-FUCOSE ? 'C6 H12 O5' 164.156 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 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 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 # _exptl.entry_id 3MJ7 _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.66 _exptl_crystal.density_percent_sol 53.79 _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.preparation ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method 'VAPOR DIFFUSION, SITTING DROP' _exptl_crystal_grow.temp 295 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 6.00 _exptl_crystal_grow.pdbx_details '0.25 M LI-SULFATE, 0.1 M MES, 24% PEG 3350, pH 6.00, VAPOR DIFFUSION, SITTING DROP, temperature 295K' _exptl_crystal_grow.pdbx_pH_range ? # _diffrn.id 1 _diffrn.ambient_temp 100.0 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector CCD _diffrn_detector.type 'MARMOSAIC 300 mm CCD' _diffrn_detector.pdbx_collection_date 2007-12-01 _diffrn_detector.details 'SI(111) DOUBLE CRYSTAL MONOCHROMETER. ADJUSTABLE FOCUSING MIRRORS IN K-B GEOMETRY' # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator 'DOUBLE CRYSTAL CRYO-COOLED SI(111)' _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 1.03317 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'APS BEAMLINE 23-ID-D' _diffrn_source.pdbx_synchrotron_site APS _diffrn_source.pdbx_synchrotron_beamline 23-ID-D _diffrn_source.pdbx_wavelength 1.03317 _diffrn_source.pdbx_wavelength_list ? # _reflns.entry_id 3MJ7 _reflns.observed_criterion_sigma_I 0.000 _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 40.000 _reflns.d_resolution_high 2.800 _reflns.number_obs 14679 _reflns.number_all ? _reflns.percent_possible_obs 99.7 _reflns.pdbx_Rmerge_I_obs 0.09100 _reflns.pdbx_Rsym_value 0.09100 _reflns.pdbx_netI_over_sigmaI 12.7000 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 4.600 _reflns.R_free_details ? _reflns.limit_h_max ? _reflns.limit_h_min ? _reflns.limit_k_max ? _reflns.limit_k_min ? _reflns.limit_l_max ? _reflns.limit_l_min ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 # _reflns_shell.d_res_high 2.80 _reflns_shell.d_res_low 2.90 _reflns_shell.percent_possible_all 99.8 _reflns_shell.Rmerge_I_obs 0.52900 _reflns_shell.pdbx_Rsym_value 0.52900 _reflns_shell.meanI_over_sigI_obs 2.900 _reflns_shell.pdbx_redundancy 4.60 _reflns_shell.percent_possible_obs ? _reflns_shell.number_unique_all ? _reflns_shell.number_measured_all ? _reflns_shell.number_measured_obs ? _reflns_shell.number_unique_obs ? _reflns_shell.pdbx_chi_squared ? _reflns_shell.pdbx_diffrn_id ? _reflns_shell.pdbx_ordinal 1 # _refine.entry_id 3MJ7 _refine.ls_number_reflns_obs 13927 _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 38.92 _refine.ls_d_res_high 2.80 _refine.ls_percent_reflns_obs 99.8 _refine.ls_R_factor_obs 0.229 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.227 _refine.ls_R_factor_R_free 0.276 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.000 _refine.ls_number_reflns_R_free 729 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.925 _refine.correlation_coeff_Fo_to_Fc_free 0.888 _refine.B_iso_mean 68.212 _refine.aniso_B[1][1] 0.89000 _refine.aniso_B[2][2] 0.89000 _refine.aniso_B[3][3] -1.33000 _refine.aniso_B[1][2] 0.44000 _refine.aniso_B[1][3] 0.00000 _refine.aniso_B[2][3] 0.00000 _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' _refine.pdbx_starting_model ? _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 2.932 _refine.pdbx_overall_ESU_R_Free 0.391 _refine.overall_SU_ML 0.359 _refine.overall_SU_B 40.735 _refine.ls_redundancy_reflns_obs ? _refine.B_iso_min ? _refine.B_iso_max ? _refine.overall_SU_R_Cruickshank_DPI ? _refine.overall_SU_R_free ? _refine.ls_wR_factor_R_free ? _refine.ls_wR_factor_R_work ? _refine.overall_FOM_free_R_set ? _refine.overall_FOM_work_R_set ? _refine.pdbx_overall_phase_error ? _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _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 3338 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 102 _refine_hist.number_atoms_solvent 0 _refine_hist.number_atoms_total 3440 _refine_hist.d_res_high 2.80 _refine_hist.d_res_low 38.92 # 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 0.008 0.022 ? 3513 'X-RAY DIFFRACTION' ? r_bond_other_d 0.002 0.020 ? 2421 'X-RAY DIFFRACTION' ? r_angle_refined_deg 1.261 1.997 ? 4758 'X-RAY DIFFRACTION' ? r_angle_other_deg 1.000 3.003 ? 5877 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 6.498 5.000 ? 413 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg 36.710 24.688 ? 160 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg 17.209 15.000 ? 626 'X-RAY DIFFRACTION' ? r_dihedral_angle_4_deg 14.946 15.000 ? 22 'X-RAY DIFFRACTION' ? r_chiral_restr 0.060 0.200 ? 551 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.004 0.021 ? 3758 'X-RAY DIFFRACTION' ? r_gen_planes_other 0.001 0.020 ? 660 '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 0.148 0.200 ? 89 '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 0.132 0.200 ? 14 'X-RAY DIFFRACTION' ? r_symmetry_vdw_other 0.165 0.200 ? 45 'X-RAY DIFFRACTION' ? r_symmetry_hbond_refined 0.245 0.200 ? 2 '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 0.980 3.000 ? 2078 'X-RAY DIFFRACTION' ? r_mcbond_other 0.149 3.000 ? 844 'X-RAY DIFFRACTION' ? r_mcangle_it 1.976 5.000 ? 3384 'X-RAY DIFFRACTION' ? r_scbond_it 3.471 8.000 ? 1435 'X-RAY DIFFRACTION' ? r_scangle_it 5.724 11.000 ? 1374 '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_total_number_of_bins_used 20 _refine_ls_shell.d_res_high 2.80 _refine_ls_shell.d_res_low 2.87 _refine_ls_shell.number_reflns_R_work 1000 _refine_ls_shell.R_factor_R_work 0.3390 _refine_ls_shell.percent_reflns_obs 99.06 _refine_ls_shell.R_factor_R_free 0.4400 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 54 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? _refine_ls_shell.number_reflns_obs ? _refine_ls_shell.redundancy_reflns_obs ? _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' # _struct.entry_id 3MJ7 _struct.title 'Crystal structure of the complex of JAML and Coxsackie and Adenovirus receptor, CAR' _struct.pdbx_descriptor 'Junctional adhesion molecule-like, Coxsackievirus and adenovirus receptor homolog' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 3MJ7 _struct_keywords.pdbx_keywords 'IMMUNE SYSTEM' _struct_keywords.text ;IMMUNOGLOBULIN TANDEM DOMAIN, IMMUNE RECEPTOR COMPLEX, CELL ADHESION, CELL JUNCTION, GLYCOPROTEIN, IMMUNOGLOBULIN DOMAIN, MEMBRANE, TRANSMEMBRANE, COSTIMULATION, PHOSPHOPROTEIN, RECEPTOR, SECRETED, TIGHT JUNCTION, IMMUNE SYSTEM ; # 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 4 ? F N N 5 ? G N N 6 ? H N N 3 ? I N N 3 ? J N N 3 ? # _struct_biol.id 1 _struct_biol.details ? # 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 GLY A 67 ? GLN A 70 ? GLY A 65 GLN A 68 5 ? 4 HELX_P HELX_P2 2 GLN A 92 ? GLU A 96 ? GLN A 90 GLU A 94 5 ? 5 HELX_P HELX_P3 3 ASP A 195 ? ASN A 199 ? ASP A 193 ASN A 197 5 ? 5 HELX_P HELX_P4 4 LYS A 209 ? GLN A 213 ? LYS A 207 GLN A 211 5 ? 5 HELX_P HELX_P5 5 TYR B 67 ? LYS B 71 ? TYR B 65 LYS B 69 5 ? 5 HELX_P HELX_P6 6 ASP B 80 ? GLY B 84 ? ASP B 78 GLY B 82 5 ? 5 HELX_P HELX_P7 7 GLN B 94 ? ASP B 97 ? GLN B 92 ASP B 95 5 ? 4 HELX_P HELX_P8 8 PRO B 168 ? MET B 175 ? PRO B 166 MET B 173 5 ? 8 # _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 27 SG ? ? ? 1_555 A CYS 101 SG ? ? A CYS 25 A CYS 99 1_555 ? ? ? ? ? ? ? 2.038 ? disulf2 disulf ? ? A CYS 140 SG ? ? ? 1_555 A CYS 218 SG ? ? A CYS 138 A CYS 216 1_555 ? ? ? ? ? ? ? 2.091 ? disulf3 disulf ? ? B CYS 24 SG ? ? ? 1_555 B CYS 103 SG ? ? B CYS 22 B CYS 101 1_555 ? ? ? ? ? ? ? 2.054 ? disulf4 disulf ? ? B CYS 129 SG ? ? ? 1_555 B CYS 206 SG ? ? B CYS 127 B CYS 204 1_555 ? ? ? ? ? ? ? 2.047 ? disulf5 disulf ? ? B CYS 145 SG ? ? ? 1_555 B CYS 195 SG ? ? B CYS 143 B CYS 193 1_555 ? ? ? ? ? ? ? 2.039 ? covale1 covale ? ? A ASN 71 ND2 ? ? ? 1_555 C NAG . C1 ? ? A ASN 69 A NAG 401 1_555 ? ? ? ? ? ? ? 1.430 ? covale2 covale ? ? D NAG . O4 ? ? ? 1_555 E BMA . C1 ? ? A NAG 402 A BMA 403 1_555 ? ? ? ? ? ? ? 1.431 ? covale3 covale ? ? I NAG . O4 ? ? ? 1_555 J NAG . C1 ? ? B NAG 301 B NAG 302 1_555 ? ? ? ? ? ? ? 1.433 ? covale4 covale ? ? B ASN 89 ND2 ? ? ? 1_555 I NAG . C1 ? ? B ASN 87 B NAG 301 1_555 ? ? ? ? ? ? ? 1.435 ? covale5 covale ? ? C NAG . O4 ? ? ? 1_555 D NAG . C1 ? ? A NAG 401 A NAG 402 1_555 ? ? ? ? ? ? ? 1.436 ? covale6 covale ? ? A ASN 107 ND2 ? ? ? 1_555 H NAG . C1 ? ? A ASN 105 A NAG 501 1_555 ? ? ? ? ? ? ? 1.444 ? covale7 covale ? ? C NAG . O6 ? ? ? 1_555 G FUC . C1 ? ? A NAG 401 A FUC 406 1_555 ? ? ? ? ? ? ? 1.450 ? covale8 covale ? ? E BMA . O3 ? ? ? 1_555 F MAN . C1 ? ? A BMA 403 A MAN 405 1_555 ? ? ? ? ? ? ? 1.454 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? # loop_ _struct_mon_prot_cis.pdbx_id _struct_mon_prot_cis.label_comp_id _struct_mon_prot_cis.label_seq_id _struct_mon_prot_cis.label_asym_id _struct_mon_prot_cis.label_alt_id _struct_mon_prot_cis.pdbx_PDB_ins_code _struct_mon_prot_cis.auth_comp_id _struct_mon_prot_cis.auth_seq_id _struct_mon_prot_cis.auth_asym_id _struct_mon_prot_cis.pdbx_label_comp_id_2 _struct_mon_prot_cis.pdbx_label_seq_id_2 _struct_mon_prot_cis.pdbx_label_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_ins_code_2 _struct_mon_prot_cis.pdbx_auth_comp_id_2 _struct_mon_prot_cis.pdbx_auth_seq_id_2 _struct_mon_prot_cis.pdbx_auth_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_model_num _struct_mon_prot_cis.pdbx_omega_angle 1 ALA 108 B . ? ALA 106 B PRO 109 B ? PRO 107 B 1 4.23 2 LYS 148 B . ? LYS 146 B GLU 149 B ? GLU 147 B 1 3.84 3 LEU 152 B . ? LEU 150 B PRO 153 B ? PRO 151 B 1 -0.61 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 7 ? B ? 7 ? C ? 4 ? D ? 6 ? E ? 3 ? F ? 3 ? G ? 3 ? H ? 2 ? # 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 A 1 2 ? parallel A 2 3 ? anti-parallel A 3 4 ? anti-parallel A 4 5 ? anti-parallel A 5 6 ? anti-parallel A 6 7 ? parallel B 1 2 ? anti-parallel B 2 3 ? anti-parallel B 3 4 ? anti-parallel B 4 5 ? anti-parallel B 5 6 ? anti-parallel B 6 7 ? anti-parallel C 1 2 ? anti-parallel C 2 3 ? anti-parallel C 3 4 ? parallel D 1 2 ? parallel D 2 3 ? anti-parallel D 3 4 ? anti-parallel D 4 5 ? anti-parallel D 5 6 ? anti-parallel E 1 2 ? anti-parallel E 2 3 ? anti-parallel F 1 2 ? anti-parallel F 2 3 ? anti-parallel G 1 2 ? anti-parallel G 2 3 ? anti-parallel H 1 2 ? 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 A 1 GLN A 14 ? HIS A 18 ? GLN A 12 HIS A 16 A 2 MET A 110 ? LEU A 121 ? MET A 108 LEU A 119 A 3 VAL B 50 ? SER B 58 ? VAL B 48 SER B 56 A 4 ASP B 37 ? PRO B 44 ? ASP B 35 PRO B 42 A 5 GLY B 99 ? LYS B 107 ? GLY B 97 LYS B 105 A 6 GLY B 110 ? LEU B 121 ? GLY B 108 LEU B 119 A 7 GLN B 10 ? ALA B 15 ? GLN B 8 ALA B 13 B 1 LEU A 62 ? PRO A 65 ? LEU A 60 PRO A 63 B 2 GLU A 53 ? TYR A 59 ? GLU A 51 TYR A 57 B 3 VAL A 37 ? SER A 45 ? VAL A 35 SER A 43 B 4 GLY A 97 ? LEU A 105 ? GLY A 95 LEU A 103 B 5 MET A 110 ? LEU A 121 ? MET A 108 LEU A 119 B 6 VAL B 50 ? SER B 58 ? VAL B 48 SER B 56 B 7 LYS B 61 ? TYR B 63 ? LYS B 59 TYR B 61 C 1 SER A 73 ? LEU A 75 ? SER A 71 LEU A 73 C 2 LEU A 86 ? LEU A 88 ? LEU A 84 LEU A 86 C 3 VAL A 23 ? MET A 25 ? VAL A 21 MET A 23 C 4 GLN A 143 ? SER A 144 ? GLN A 141 SER A 142 D 1 ASP A 127 ? ARG A 131 ? ASP A 125 ARG A 129 D 2 LEU A 225 ? VAL A 236 ? LEU A 223 VAL A 234 D 3 GLY A 214 ? VAL A 222 ? GLY A 212 VAL A 220 D 4 LYS A 152 ? SER A 158 ? LYS A 150 SER A 156 D 5 GLU A 166 ? ASP A 172 ? GLU A 164 ASP A 170 D 6 PHE A 180 ? GLN A 181 ? PHE A 178 GLN A 179 E 1 THR A 136 ? MET A 138 ? THR A 134 MET A 136 E 2 ILE A 203 ? LEU A 205 ? ILE A 201 LEU A 203 E 3 VAL A 190 ? LEU A 192 ? VAL A 188 LEU A 190 F 1 ALA B 20 ? LEU B 22 ? ALA B 18 LEU B 20 F 2 ILE B 88 ? VAL B 90 ? ILE B 86 VAL B 88 F 3 VAL B 74 ? PHE B 76 ? VAL B 72 PHE B 74 G 1 ARG B 128 ? VAL B 131 ? ARG B 126 VAL B 129 G 2 LEU B 143 ? GLU B 146 ? LEU B 141 GLU B 144 G 3 VAL B 179 ? ILE B 180 ? VAL B 177 ILE B 178 H 1 GLN B 155 ? GLN B 159 ? GLN B 153 GLN B 157 H 2 SER B 194 ? GLN B 198 ? SER B 192 GLN B 196 # 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 A 1 2 N VAL A 17 ? N VAL A 15 O LEU A 121 ? O LEU A 119 A 2 3 N VAL A 111 ? N VAL A 109 O ASP B 51 ? O ASP B 49 A 3 4 O GLN B 52 ? O GLN B 50 N ILE B 42 ? N ILE B 40 A 4 5 N ASP B 37 ? N ASP B 35 O LYS B 106 ? O LYS B 104 A 5 6 N TYR B 101 ? N TYR B 99 O PHE B 116 ? O PHE B 114 A 6 7 O LEU B 117 ? O LEU B 115 N GLN B 10 ? N GLN B 8 B 1 2 O VAL A 64 ? O VAL A 62 N PHE A 57 ? N PHE A 55 B 2 3 O VAL A 55 ? O VAL A 53 N TRP A 42 ? N TRP A 40 B 3 4 N SER A 45 ? N SER A 43 O ILE A 98 ? O ILE A 96 B 4 5 N ILE A 103 ? N ILE A 101 O MET A 112 ? O MET A 110 B 5 6 N VAL A 111 ? N VAL A 109 O ASP B 51 ? O ASP B 49 B 6 7 N SER B 58 ? N SER B 56 O LYS B 61 ? O LYS B 59 C 1 2 N HIS A 74 ? N HIS A 72 O LEU A 87 ? O LEU A 85 C 2 3 O LEU A 88 ? O LEU A 86 N VAL A 23 ? N VAL A 21 C 3 4 N LEU A 24 ? N LEU A 22 O GLN A 143 ? O GLN A 141 D 1 2 N LEU A 128 ? N LEU A 126 O HIS A 234 ? O HIS A 232 D 2 3 O ILE A 231 ? O ILE A 229 N TYR A 216 ? N TYR A 214 D 3 4 O TYR A 221 ? O TYR A 219 N LYS A 152 ? N LYS A 150 D 4 5 N TRP A 155 ? N TRP A 153 O LEU A 169 ? O LEU A 167 D 5 6 N SER A 170 ? N SER A 168 O PHE A 180 ? O PHE A 178 E 1 2 N MET A 138 ? N MET A 136 O ILE A 203 ? O ILE A 201 E 2 3 O LYS A 204 ? O LYS A 202 N ASP A 191 ? N ASP A 189 F 1 2 N ALA B 20 ? N ALA B 18 O VAL B 90 ? O VAL B 88 F 2 3 O ASN B 89 ? O ASN B 87 N HIS B 75 ? N HIS B 73 G 1 2 N ARG B 128 ? N ARG B 126 O GLU B 146 ? O GLU B 144 G 2 3 N LEU B 143 ? N LEU B 141 O ILE B 180 ? O ILE B 178 H 1 2 N GLN B 155 ? N GLN B 153 O GLN B 198 ? O GLN B 196 # 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 NAG A 401' AC2 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG A 402' AC3 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE BMA A 403' AC4 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE MAN A 405' AC5 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE FUC A 406' AC6 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG A 501' AC7 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE NAG B 301' AC8 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG B 302' # 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 GLY A 67 ? GLY A 65 . ? 1_555 ? 2 AC1 4 ASN A 71 ? ASN A 69 . ? 1_555 ? 3 AC1 4 NAG D . ? NAG A 402 . ? 1_555 ? 4 AC1 4 FUC G . ? FUC A 406 . ? 1_555 ? 5 AC2 3 NAG C . ? NAG A 401 . ? 1_555 ? 6 AC2 3 BMA E . ? BMA A 403 . ? 1_555 ? 7 AC2 3 FUC G . ? FUC A 406 . ? 1_555 ? 8 AC3 3 GLU A 123 ? GLU A 121 . ? 6_545 ? 9 AC3 3 NAG D . ? NAG A 402 . ? 1_555 ? 10 AC3 3 MAN F . ? MAN A 405 . ? 1_555 ? 11 AC4 2 GLY A 20 ? GLY A 18 . ? 6_545 ? 12 AC4 2 BMA E . ? BMA A 403 . ? 1_555 ? 13 AC5 2 NAG C . ? NAG A 401 . ? 1_555 ? 14 AC5 2 NAG D . ? NAG A 402 . ? 1_555 ? 15 AC6 1 ASN A 107 ? ASN A 105 . ? 1_555 ? 16 AC7 4 ARG A 187 ? ARG A 185 . ? 6_445 ? 17 AC7 4 THR B 77 ? THR B 75 . ? 1_555 ? 18 AC7 4 ASN B 89 ? ASN B 87 . ? 1_555 ? 19 AC7 4 NAG J . ? NAG B 302 . ? 1_555 ? 20 AC8 1 NAG I . ? NAG B 301 . ? 1_555 ? # _database_PDB_matrix.entry_id 3MJ7 _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 3MJ7 _atom_sites.fract_transf_matrix[1][1] 0.011128 _atom_sites.fract_transf_matrix[1][2] 0.006425 _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] 0.012849 _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] 0.007863 _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 . PRO A 1 13 ? 12.029 -21.152 -17.332 1.00 50.80 ? 11 PRO A N 1 ATOM 2 C CA . PRO A 1 13 ? 13.079 -20.213 -16.935 1.00 50.07 ? 11 PRO A CA 1 ATOM 3 C C . PRO A 1 13 ? 14.462 -20.858 -16.863 1.00 49.02 ? 11 PRO A C 1 ATOM 4 O O . PRO A 1 13 ? 14.667 -21.870 -16.178 1.00 49.04 ? 11 PRO A O 1 ATOM 5 C CB . PRO A 1 13 ? 12.613 -19.725 -15.557 1.00 48.44 ? 11 PRO A CB 1 ATOM 6 C CG . PRO A 1 13 ? 11.145 -19.924 -15.566 1.00 48.44 ? 11 PRO A CG 1 ATOM 7 C CD . PRO A 1 13 ? 10.892 -21.137 -16.398 1.00 50.42 ? 11 PRO A CD 1 ATOM 8 N N . GLN A 1 14 ? 15.395 -20.257 -17.588 1.00 49.40 ? 12 GLN A N 1 ATOM 9 C CA . GLN A 1 14 ? 16.755 -20.771 -17.693 1.00 47.34 ? 12 GLN A CA 1 ATOM 10 C C . GLN A 1 14 ? 17.729 -19.856 -16.975 1.00 44.90 ? 12 GLN A C 1 ATOM 11 O O . GLN A 1 14 ? 17.531 -18.645 -16.891 1.00 47.45 ? 12 GLN A O 1 ATOM 12 C CB . GLN A 1 14 ? 17.182 -20.859 -19.162 1.00 50.22 ? 12 GLN A CB 1 ATOM 13 C CG . GLN A 1 14 ? 16.144 -21.418 -20.097 1.00 56.00 ? 12 GLN A CG 1 ATOM 14 C CD . GLN A 1 14 ? 16.064 -22.918 -20.018 1.00 62.60 ? 12 GLN A CD 1 ATOM 15 O OE1 . GLN A 1 14 ? 16.894 -23.621 -20.593 1.00 66.68 ? 12 GLN A OE1 1 ATOM 16 N NE2 . GLN A 1 14 ? 15.058 -23.426 -19.305 1.00 65.79 ? 12 GLN A NE2 1 ATOM 17 N N . LEU A 1 15 ? 18.791 -20.457 -16.470 1.00 40.14 ? 13 LEU A N 1 ATOM 18 C CA . LEU A 1 15 ? 19.943 -19.712 -15.977 1.00 37.05 ? 13 LEU A CA 1 ATOM 19 C C . LEU A 1 15 ? 21.223 -20.458 -16.318 1.00 35.79 ? 13 LEU A C 1 ATOM 20 O O . LEU A 1 15 ? 21.276 -21.684 -16.343 1.00 34.74 ? 13 LEU A O 1 ATOM 21 C CB . LEU A 1 15 ? 19.856 -19.468 -14.466 1.00 35.00 ? 13 LEU A CB 1 ATOM 22 C CG . LEU A 1 15 ? 18.622 -18.730 -13.923 1.00 37.03 ? 13 LEU A CG 1 ATOM 23 C CD1 . LEU A 1 15 ? 18.487 -18.960 -12.414 1.00 36.77 ? 13 LEU A CD1 1 ATOM 24 C CD2 . LEU A 1 15 ? 18.635 -17.233 -14.234 1.00 30.67 ? 13 LEU A CD2 1 ATOM 25 N N . ARG A 1 16 ? 22.242 -19.676 -16.617 1.00 36.78 ? 14 ARG A N 1 ATOM 26 C CA . ARG A 1 16 ? 23.556 -20.180 -16.953 1.00 36.66 ? 14 ARG A CA 1 ATOM 27 C C . ARG A 1 16 ? 24.544 -19.614 -15.959 1.00 33.89 ? 14 ARG A C 1 ATOM 28 O O . ARG A 1 16 ? 24.663 -18.394 -15.816 1.00 34.59 ? 14 ARG A O 1 ATOM 29 C CB . ARG A 1 16 ? 23.953 -19.700 -18.352 1.00 41.29 ? 14 ARG A CB 1 ATOM 30 C CG . ARG A 1 16 ? 23.619 -20.636 -19.494 1.00 52.59 ? 14 ARG A CG 1 ATOM 31 C CD . ARG A 1 16 ? 24.003 -20.027 -20.839 1.00 62.71 ? 14 ARG A CD 1 ATOM 32 N NE . ARG A 1 16 ? 22.835 -19.502 -21.545 1.00 75.85 ? 14 ARG A NE 1 ATOM 33 C CZ . ARG A 1 16 ? 22.404 -18.242 -21.479 1.00 84.95 ? 14 ARG A CZ 1 ATOM 34 N NH1 . ARG A 1 16 ? 23.036 -17.339 -20.734 1.00 85.53 ? 14 ARG A NH1 1 ATOM 35 N NH2 . ARG A 1 16 ? 21.326 -17.884 -22.169 1.00 90.14 ? 14 ARG A NH2 1 ATOM 36 N N . VAL A 1 17 ? 25.267 -20.488 -15.283 1.00 30.19 ? 15 VAL A N 1 ATOM 37 C CA . VAL A 1 17 ? 26.317 -20.034 -14.385 1.00 28.82 ? 15 VAL A CA 1 ATOM 38 C C . VAL A 1 17 ? 27.586 -20.804 -14.609 1.00 28.63 ? 15 VAL A C 1 ATOM 39 O O . VAL A 1 17 ? 27.577 -21.947 -15.043 1.00 28.65 ? 15 VAL A O 1 ATOM 40 C CB . VAL A 1 17 ? 25.929 -20.105 -12.885 1.00 27.74 ? 15 VAL A CB 1 ATOM 41 C CG1 . VAL A 1 17 ? 24.984 -18.971 -12.542 1.00 29.23 ? 15 VAL A CG1 1 ATOM 42 C CG2 . VAL A 1 17 ? 25.318 -21.436 -12.533 1.00 24.13 ? 15 VAL A CG2 1 ATOM 43 N N . HIS A 1 18 ? 28.695 -20.138 -14.325 1.00 30.37 ? 16 HIS A N 1 ATOM 44 C CA . HIS A 1 18 ? 29.996 -20.773 -14.424 1.00 29.31 ? 16 HIS A CA 1 ATOM 45 C C . HIS A 1 18 ? 30.306 -21.446 -13.112 1.00 27.89 ? 16 HIS A C 1 ATOM 46 O O . HIS A 1 18 ? 29.911 -20.979 -12.047 1.00 25.98 ? 16 HIS A O 1 ATOM 47 C CB . HIS A 1 18 ? 31.075 -19.761 -14.728 1.00 29.64 ? 16 HIS A CB 1 ATOM 48 C CG . HIS A 1 18 ? 30.938 -19.111 -16.061 1.00 33.90 ? 16 HIS A CG 1 ATOM 49 N ND1 . HIS A 1 18 ? 31.544 -19.610 -17.193 1.00 42.15 ? 16 HIS A ND1 1 ATOM 50 C CD2 . HIS A 1 18 ? 30.303 -17.979 -16.440 1.00 36.41 ? 16 HIS A CD2 1 ATOM 51 C CE1 . HIS A 1 18 ? 31.274 -18.821 -18.216 1.00 43.38 ? 16 HIS A CE1 1 ATOM 52 N NE2 . HIS A 1 18 ? 30.529 -17.819 -17.785 1.00 38.71 ? 16 HIS A NE2 1 ATOM 53 N N . VAL A 1 19 ? 31.016 -22.555 -13.195 1.00 28.71 ? 17 VAL A N 1 ATOM 54 C CA . VAL A 1 19 ? 31.386 -23.259 -11.995 1.00 28.62 ? 17 VAL A CA 1 ATOM 55 C C . VAL A 1 19 ? 32.115 -22.322 -11.056 1.00 31.17 ? 17 VAL A C 1 ATOM 56 O O . VAL A 1 19 ? 33.012 -21.581 -11.458 1.00 32.92 ? 17 VAL A O 1 ATOM 57 C CB . VAL A 1 19 ? 32.298 -24.452 -12.266 1.00 30.86 ? 17 VAL A CB 1 ATOM 58 C CG1 . VAL A 1 19 ? 32.917 -24.897 -10.964 1.00 30.07 ? 17 VAL A CG1 1 ATOM 59 C CG2 . VAL A 1 19 ? 31.533 -25.594 -12.932 1.00 25.91 ? 17 VAL A CG2 1 ATOM 60 N N . GLY A 1 20 ? 31.702 -22.374 -9.795 1.00 31.80 ? 18 GLY A N 1 ATOM 61 C CA . GLY A 1 20 ? 32.311 -21.602 -8.724 1.00 33.03 ? 18 GLY A CA 1 ATOM 62 C C . GLY A 1 20 ? 31.431 -20.453 -8.297 1.00 32.80 ? 18 GLY A C 1 ATOM 63 O O . GLY A 1 20 ? 31.436 -20.049 -7.137 1.00 36.15 ? 18 GLY A O 1 ATOM 64 N N . GLU A 1 21 ? 30.658 -19.931 -9.236 1.00 31.36 ? 19 GLU A N 1 ATOM 65 C CA . GLU A 1 21 ? 29.872 -18.728 -8.974 1.00 31.76 ? 19 GLU A CA 1 ATOM 66 C C . GLU A 1 21 ? 28.547 -19.038 -8.305 1.00 28.33 ? 19 GLU A C 1 ATOM 67 O O . GLU A 1 21 ? 28.253 -20.183 -7.970 1.00 27.86 ? 19 GLU A O 1 ATOM 68 C CB . GLU A 1 21 ? 29.644 -17.927 -10.259 1.00 33.11 ? 19 GLU A CB 1 ATOM 69 C CG . GLU A 1 21 ? 30.942 -17.411 -10.892 1.00 43.94 ? 19 GLU A CG 1 ATOM 70 C CD . GLU A 1 21 ? 30.706 -16.521 -12.116 1.00 55.18 ? 19 GLU A CD 1 ATOM 71 O OE1 . GLU A 1 21 ? 29.783 -16.829 -12.910 1.00 62.90 ? 19 GLU A OE1 1 ATOM 72 O OE2 . GLU A 1 21 ? 31.449 -15.524 -12.286 1.00 61.82 ? 19 GLU A OE2 1 ATOM 73 N N . SER A 1 22 ? 27.748 -17.995 -8.145 1.00 28.32 ? 20 SER A N 1 ATOM 74 C CA . SER A 1 22 ? 26.480 -18.074 -7.411 1.00 28.34 ? 20 SER A CA 1 ATOM 75 C C . SER A 1 22 ? 25.272 -17.764 -8.271 1.00 28.31 ? 20 SER A C 1 ATOM 76 O O . SER A 1 22 ? 25.352 -17.134 -9.325 1.00 30.61 ? 20 SER A O 1 ATOM 77 C CB . SER A 1 22 ? 26.500 -17.114 -6.215 1.00 29.98 ? 20 SER A CB 1 ATOM 78 O OG . SER A 1 22 ? 27.488 -17.489 -5.262 1.00 32.81 ? 20 SER A OG 1 ATOM 79 N N . VAL A 1 23 ? 24.130 -18.204 -7.792 1.00 28.26 ? 21 VAL A N 1 ATOM 80 C CA . VAL A 1 23 ? 22.890 -18.007 -8.533 1.00 29.01 ? 21 VAL A CA 1 ATOM 81 C C . VAL A 1 23 ? 21.712 -17.872 -7.599 1.00 29.53 ? 21 VAL A C 1 ATOM 82 O O . VAL A 1 23 ? 21.621 -18.572 -6.594 1.00 29.80 ? 21 VAL A O 1 ATOM 83 C CB . VAL A 1 23 ? 22.630 -19.172 -9.482 1.00 26.61 ? 21 VAL A CB 1 ATOM 84 C CG1 . VAL A 1 23 ? 22.728 -20.463 -8.738 1.00 23.55 ? 21 VAL A CG1 1 ATOM 85 C CG2 . VAL A 1 23 ? 21.289 -19.028 -10.097 1.00 28.94 ? 21 VAL A CG2 1 ATOM 86 N N . LEU A 1 24 ? 20.824 -16.951 -7.946 1.00 30.45 ? 22 LEU A N 1 ATOM 87 C CA . LEU A 1 24 ? 19.652 -16.663 -7.135 1.00 31.09 ? 22 LEU A CA 1 ATOM 88 C C . LEU A 1 24 ? 18.393 -17.058 -7.876 1.00 32.68 ? 22 LEU A C 1 ATOM 89 O O . LEU A 1 24 ? 17.951 -16.370 -8.802 1.00 35.96 ? 22 LEU A O 1 ATOM 90 C CB . LEU A 1 24 ? 19.602 -15.182 -6.768 1.00 32.48 ? 22 LEU A CB 1 ATOM 91 C CG . LEU A 1 24 ? 18.517 -14.801 -5.761 1.00 32.84 ? 22 LEU A CG 1 ATOM 92 C CD1 . LEU A 1 24 ? 18.811 -13.443 -5.159 1.00 33.28 ? 22 LEU A CD1 1 ATOM 93 C CD2 . LEU A 1 24 ? 17.132 -14.810 -6.408 1.00 31.63 ? 22 LEU A CD2 1 ATOM 94 N N . MET A 1 25 ? 17.814 -18.166 -7.440 1.00 31.34 ? 23 MET A N 1 ATOM 95 C CA . MET A 1 25 ? 16.595 -18.687 -8.039 1.00 32.29 ? 23 MET A CA 1 ATOM 96 C C . MET A 1 25 ? 15.361 -18.125 -7.356 1.00 34.34 ? 23 MET A C 1 ATOM 97 O O . MET A 1 25 ? 14.992 -18.522 -6.254 1.00 34.49 ? 23 MET A O 1 ATOM 98 C CB . MET A 1 25 ? 16.611 -20.208 -7.988 1.00 31.22 ? 23 MET A CB 1 ATOM 99 C CG . MET A 1 25 ? 17.782 -20.780 -8.766 1.00 33.62 ? 23 MET A CG 1 ATOM 100 S SD . MET A 1 25 ? 17.967 -22.552 -8.608 1.00 42.01 ? 23 MET A SD 1 ATOM 101 C CE . MET A 1 25 ? 18.824 -22.688 -7.049 1.00 45.49 ? 23 MET A CE 1 ATOM 102 N N . GLY A 1 26 ? 14.730 -17.185 -8.042 1.00 37.58 ? 24 GLY A N 1 ATOM 103 C CA . GLY A 1 26 ? 13.562 -16.484 -7.522 1.00 40.84 ? 24 GLY A CA 1 ATOM 104 C C . GLY A 1 26 ? 12.388 -17.388 -7.246 1.00 42.25 ? 24 GLY A C 1 ATOM 105 O O . GLY A 1 26 ? 12.210 -18.421 -7.889 1.00 41.06 ? 24 GLY A O 1 ATOM 106 N N . CYS A 1 27 ? 11.599 -16.990 -6.256 1.00 45.19 ? 25 CYS A N 1 ATOM 107 C CA . CYS A 1 27 ? 10.329 -17.658 -5.949 1.00 46.94 ? 25 CYS A CA 1 ATOM 108 C C . CYS A 1 27 ? 9.379 -16.690 -5.260 1.00 48.95 ? 25 CYS A C 1 ATOM 109 O O . CYS A 1 27 ? 9.286 -16.644 -4.043 1.00 49.31 ? 25 CYS A O 1 ATOM 110 C CB . CYS A 1 27 ? 10.558 -18.908 -5.083 1.00 45.32 ? 25 CYS A CB 1 ATOM 111 S SG . CYS A 1 27 ? 9.138 -20.052 -5.039 1.00 52.30 ? 25 CYS A SG 1 ATOM 112 N N . VAL A 1 28 ? 8.675 -15.917 -6.068 1.00 52.31 ? 26 VAL A N 1 ATOM 113 C CA . VAL A 1 28 ? 7.819 -14.847 -5.563 1.00 55.95 ? 26 VAL A CA 1 ATOM 114 C C . VAL A 1 28 ? 6.362 -15.001 -5.971 1.00 59.60 ? 26 VAL A C 1 ATOM 115 O O . VAL A 1 28 ? 5.975 -14.701 -7.098 1.00 60.74 ? 26 VAL A O 1 ATOM 116 C CB . VAL A 1 28 ? 8.307 -13.487 -6.046 1.00 56.99 ? 26 VAL A CB 1 ATOM 117 C CG1 . VAL A 1 28 ? 7.462 -12.378 -5.443 1.00 60.82 ? 26 VAL A CG1 1 ATOM 118 C CG2 . VAL A 1 28 ? 9.763 -13.317 -5.692 1.00 55.64 ? 26 VAL A CG2 1 ATOM 119 N N . VAL A 1 29 ? 5.566 -15.455 -5.013 1.00 60.94 ? 27 VAL A N 1 ATOM 120 C CA . VAL A 1 29 ? 4.136 -15.640 -5.205 1.00 64.76 ? 27 VAL A CA 1 ATOM 121 C C . VAL A 1 29 ? 3.481 -14.271 -5.215 1.00 70.91 ? 27 VAL A C 1 ATOM 122 O O . VAL A 1 29 ? 3.259 -13.665 -4.171 1.00 73.30 ? 27 VAL A O 1 ATOM 123 C CB . VAL A 1 29 ? 3.529 -16.496 -4.078 1.00 64.68 ? 27 VAL A CB 1 ATOM 124 C CG1 . VAL A 1 29 ? 2.027 -16.624 -4.264 1.00 67.93 ? 27 VAL A CG1 1 ATOM 125 C CG2 . VAL A 1 29 ? 4.206 -17.883 -4.016 1.00 57.62 ? 27 VAL A CG2 1 ATOM 126 N N . GLN A 1 30 ? 3.175 -13.783 -6.407 1.00 74.36 ? 28 GLN A N 1 ATOM 127 C CA . GLN A 1 30 ? 2.689 -12.415 -6.550 1.00 80.59 ? 28 GLN A CA 1 ATOM 128 C C . GLN A 1 30 ? 1.184 -12.304 -6.360 1.00 86.71 ? 28 GLN A C 1 ATOM 129 O O . GLN A 1 30 ? 0.398 -12.537 -7.282 1.00 90.45 ? 28 GLN A O 1 ATOM 130 C CB . GLN A 1 30 ? 3.080 -11.821 -7.908 1.00 82.05 ? 28 GLN A CB 1 ATOM 131 C CG . GLN A 1 30 ? 3.030 -10.293 -7.920 1.00 87.68 ? 28 GLN A CG 1 ATOM 132 C CD . GLN A 1 30 ? 2.146 -9.739 -9.023 1.00 97.56 ? 28 GLN A CD 1 ATOM 133 O OE1 . GLN A 1 30 ? 1.361 -10.470 -9.625 1.00 103.59 ? 28 GLN A OE1 1 ATOM 134 N NE2 . GLN A 1 30 ? 2.259 -8.439 -9.283 1.00 103.57 ? 28 GLN A NE2 1 ATOM 135 N N . ARG A 1 31 ? 0.796 -11.921 -5.150 1.00 88.33 ? 29 ARG A N 1 ATOM 136 C CA . ARG A 1 31 ? -0.598 -11.605 -4.847 1.00 93.82 ? 29 ARG A CA 1 ATOM 137 C C . ARG A 1 31 ? -0.742 -10.095 -4.876 1.00 98.70 ? 29 ARG A C 1 ATOM 138 O O . ARG A 1 31 ? 0.125 -9.396 -5.397 1.00 98.13 ? 29 ARG A O 1 ATOM 139 C CB . ARG A 1 31 ? -1.008 -12.156 -3.479 1.00 93.54 ? 29 ARG A CB 1 ATOM 140 C CG . ARG A 1 31 ? -0.968 -13.675 -3.383 1.00 88.28 ? 29 ARG A CG 1 ATOM 141 C CD . ARG A 1 31 ? -2.056 -14.320 -4.230 1.00 91.94 ? 29 ARG A CD 1 ATOM 142 N NE . ARG A 1 31 ? -2.085 -15.771 -4.065 1.00 88.08 ? 29 ARG A NE 1 ATOM 143 C CZ . ARG A 1 31 ? -1.365 -16.624 -4.787 1.00 87.92 ? 29 ARG A CZ 1 ATOM 144 N NH1 . ARG A 1 31 ? -0.545 -16.185 -5.736 1.00 88.64 ? 29 ARG A NH1 1 ATOM 145 N NH2 . ARG A 1 31 ? -1.457 -17.924 -4.558 1.00 85.59 ? 29 ARG A NH2 1 ATOM 146 N N . THR A 1 32 ? -1.834 -9.596 -4.311 1.00 104.25 ? 30 THR A N 1 ATOM 147 C CA . THR A 1 32 ? -2.089 -8.163 -4.278 1.00 109.75 ? 30 THR A CA 1 ATOM 148 C C . THR A 1 32 ? -1.826 -7.615 -2.886 1.00 109.97 ? 30 THR A C 1 ATOM 149 O O . THR A 1 32 ? -2.405 -6.609 -2.486 1.00 115.51 ? 30 THR A O 1 ATOM 150 C CB . THR A 1 32 ? -3.530 -7.838 -4.698 1.00 117.42 ? 30 THR A CB 1 ATOM 151 O OG1 . THR A 1 32 ? -4.452 -8.536 -3.851 1.00 119.94 ? 30 THR A OG1 1 ATOM 152 C CG2 . THR A 1 32 ? -3.763 -8.245 -6.145 1.00 117.36 ? 30 THR A CG2 1 ATOM 153 N N . GLU A 1 33 ? -0.936 -8.282 -2.156 1.00 104.36 ? 31 GLU A N 1 ATOM 154 C CA . GLU A 1 33 ? -0.609 -7.870 -0.783 1.00 104.46 ? 31 GLU A CA 1 ATOM 155 C C . GLU A 1 33 ? 0.572 -8.584 -0.128 1.00 97.48 ? 31 GLU A C 1 ATOM 156 O O . GLU A 1 33 ? 1.083 -9.594 -0.611 1.00 92.00 ? 31 GLU A O 1 ATOM 157 C CB . GLU A 1 33 ? -1.840 -8.030 0.110 1.00 108.92 ? 31 GLU A CB 1 ATOM 158 C CG . GLU A 1 33 ? -2.432 -9.429 0.084 1.00 106.80 ? 31 GLU A CG 1 ATOM 159 C CD . GLU A 1 33 ? -3.822 -9.495 0.694 1.00 114.90 ? 31 GLU A CD 1 ATOM 160 O OE1 . GLU A 1 33 ? -4.312 -8.468 1.215 1.00 119.52 ? 31 GLU A OE1 1 ATOM 161 O OE2 . GLU A 1 33 ? -4.433 -10.582 0.651 1.00 116.18 ? 31 GLU A OE2 1 ATOM 162 N N . GLU A 1 34 ? 0.984 -8.007 0.992 1.00 98.38 ? 32 GLU A N 1 ATOM 163 C CA . GLU A 1 34 ? 2.023 -8.579 1.853 1.00 93.71 ? 32 GLU A CA 1 ATOM 164 C C . GLU A 1 34 ? 1.499 -9.819 2.548 1.00 91.23 ? 32 GLU A C 1 ATOM 165 O O . GLU A 1 34 ? 0.515 -9.766 3.284 1.00 94.69 ? 32 GLU A O 1 ATOM 166 C CB . GLU A 1 34 ? 2.480 -7.575 2.925 1.00 96.89 ? 32 GLU A CB 1 ATOM 167 C CG . GLU A 1 34 ? 3.264 -6.390 2.390 1.00 99.57 ? 32 GLU A CG 1 ATOM 168 C CD . GLU A 1 34 ? 4.602 -6.788 1.796 1.00 96.92 ? 32 GLU A CD 1 ATOM 169 O OE1 . GLU A 1 34 ? 5.256 -7.723 2.317 1.00 91.30 ? 32 GLU A OE1 1 ATOM 170 O OE2 . GLU A 1 34 ? 5.003 -6.154 0.799 1.00 100.61 ? 32 GLU A OE2 1 ATOM 171 N N . LYS A 1 35 ? 2.177 -10.935 2.319 1.00 84.43 ? 33 LYS A N 1 ATOM 172 C CA . LYS A 1 35 ? 1.800 -12.198 2.949 1.00 82.19 ? 33 LYS A CA 1 ATOM 173 C C . LYS A 1 35 ? 3.015 -12.974 3.427 1.00 75.80 ? 33 LYS A C 1 ATOM 174 O O . LYS A 1 35 ? 3.976 -13.175 2.687 1.00 72.76 ? 33 LYS A O 1 ATOM 175 C CB . LYS A 1 35 ? 0.979 -13.052 1.981 1.00 82.11 ? 33 LYS A CB 1 ATOM 176 C CG . LYS A 1 35 ? -0.438 -12.551 1.747 1.00 89.85 ? 33 LYS A CG 1 ATOM 177 C CD . LYS A 1 35 ? -1.200 -13.502 0.844 1.00 92.05 ? 33 LYS A CD 1 ATOM 178 C CE . LYS A 1 35 ? -2.538 -12.927 0.424 1.00 99.35 ? 33 LYS A CE 1 ATOM 179 N NZ . LYS A 1 35 ? -3.296 -13.866 -0.450 1.00 100.89 ? 33 LYS A NZ 1 ATOM 180 N N . HIS A 1 36 ? 2.955 -13.417 4.674 1.00 74.71 ? 34 HIS A N 1 ATOM 181 C CA . HIS A 1 36 ? 4.074 -14.132 5.275 1.00 69.59 ? 34 HIS A CA 1 ATOM 182 C C . HIS A 1 36 ? 4.114 -15.535 4.726 1.00 64.71 ? 34 HIS A C 1 ATOM 183 O O . HIS A 1 36 ? 3.112 -16.243 4.730 1.00 66.89 ? 34 HIS A O 1 ATOM 184 C CB . HIS A 1 36 ? 3.981 -14.157 6.804 1.00 71.70 ? 34 HIS A CB 1 ATOM 185 C CG . HIS A 1 36 ? 3.975 -12.797 7.423 1.00 76.10 ? 34 HIS A CG 1 ATOM 186 N ND1 . HIS A 1 36 ? 4.375 -11.672 6.737 1.00 79.31 ? 34 HIS A ND1 1 ATOM 187 C CD2 . HIS A 1 36 ? 3.621 -12.378 8.660 1.00 83.58 ? 34 HIS A CD2 1 ATOM 188 C CE1 . HIS A 1 36 ? 4.261 -10.616 7.523 1.00 84.35 ? 34 HIS A CE1 1 ATOM 189 N NE2 . HIS A 1 36 ? 3.803 -11.017 8.695 1.00 87.54 ? 34 HIS A NE2 1 ATOM 190 N N . VAL A 1 37 ? 5.283 -15.913 4.232 1.00 59.27 ? 35 VAL A N 1 ATOM 191 C CA . VAL A 1 37 ? 5.500 -17.260 3.728 1.00 55.42 ? 35 VAL A CA 1 ATOM 192 C C . VAL A 1 37 ? 5.429 -18.242 4.882 1.00 57.18 ? 35 VAL A C 1 ATOM 193 O O . VAL A 1 37 ? 6.091 -18.070 5.907 1.00 58.40 ? 35 VAL A O 1 ATOM 194 C CB . VAL A 1 37 ? 6.874 -17.411 3.032 1.00 50.20 ? 35 VAL A CB 1 ATOM 195 C CG1 . VAL A 1 37 ? 7.185 -18.873 2.797 1.00 45.04 ? 35 VAL A CG1 1 ATOM 196 C CG2 . VAL A 1 37 ? 6.907 -16.635 1.730 1.00 47.16 ? 35 VAL A CG2 1 ATOM 197 N N . ASP A 1 38 ? 4.621 -19.275 4.701 1.00 58.25 ? 36 ASP A N 1 ATOM 198 C CA . ASP A 1 38 ? 4.459 -20.314 5.712 1.00 58.53 ? 36 ASP A CA 1 ATOM 199 C C . ASP A 1 38 ? 5.453 -21.453 5.460 1.00 54.97 ? 36 ASP A C 1 ATOM 200 O O . ASP A 1 38 ? 5.893 -22.129 6.393 1.00 54.44 ? 36 ASP A O 1 ATOM 201 C CB . ASP A 1 38 ? 3.018 -20.833 5.704 1.00 61.45 ? 36 ASP A CB 1 ATOM 202 C CG . ASP A 1 38 ? 2.777 -21.913 6.739 1.00 62.84 ? 36 ASP A CG 1 ATOM 203 O OD1 . ASP A 1 38 ? 3.256 -23.046 6.535 1.00 61.08 ? 36 ASP A OD1 1 ATOM 204 O OD2 . ASP A 1 38 ? 2.094 -21.637 7.748 1.00 66.55 ? 36 ASP A OD2 1 ATOM 205 N N . ARG A 1 39 ? 5.824 -21.641 4.198 1.00 52.63 ? 37 ARG A N 1 ATOM 206 C CA . ARG A 1 39 ? 6.654 -22.787 3.814 1.00 50.65 ? 37 ARG A CA 1 ATOM 207 C C . ARG A 1 39 ? 7.298 -22.676 2.456 1.00 47.03 ? 37 ARG A C 1 ATOM 208 O O . ARG A 1 39 ? 6.692 -22.151 1.535 1.00 50.25 ? 37 ARG A O 1 ATOM 209 C CB . ARG A 1 39 ? 5.791 -24.041 3.752 1.00 52.29 ? 37 ARG A CB 1 ATOM 210 C CG . ARG A 1 39 ? 5.629 -24.763 5.033 1.00 54.37 ? 37 ARG A CG 1 ATOM 211 C CD . ARG A 1 39 ? 4.513 -25.757 4.888 1.00 55.10 ? 37 ARG A CD 1 ATOM 212 N NE . ARG A 1 39 ? 3.869 -26.010 6.165 1.00 58.98 ? 37 ARG A NE 1 ATOM 213 C CZ . ARG A 1 39 ? 3.779 -27.200 6.735 1.00 63.32 ? 37 ARG A CZ 1 ATOM 214 N NH1 . ARG A 1 39 ? 4.278 -28.276 6.137 1.00 63.74 ? 37 ARG A NH1 1 ATOM 215 N NH2 . ARG A 1 39 ? 3.162 -27.308 7.897 1.00 70.51 ? 37 ARG A NH2 1 ATOM 216 N N . VAL A 1 40 ? 8.499 -23.231 2.333 1.00 41.72 ? 38 VAL A N 1 ATOM 217 C CA . VAL A 1 40 ? 9.089 -23.502 1.024 1.00 40.38 ? 38 VAL A CA 1 ATOM 218 C C . VAL A 1 40 ? 9.886 -24.802 0.991 1.00 38.24 ? 38 VAL A C 1 ATOM 219 O O . VAL A 1 40 ? 10.697 -25.071 1.875 1.00 36.79 ? 38 VAL A O 1 ATOM 220 C CB . VAL A 1 40 ? 10.056 -22.396 0.576 1.00 40.58 ? 38 VAL A CB 1 ATOM 221 C CG1 . VAL A 1 40 ? 10.451 -22.628 -0.873 1.00 42.86 ? 38 VAL A CG1 1 ATOM 222 C CG2 . VAL A 1 40 ? 9.446 -21.008 0.755 1.00 40.69 ? 38 VAL A CG2 1 ATOM 223 N N . ASP A 1 41 ? 9.647 -25.601 -0.043 1.00 37.27 ? 39 ASP A N 1 ATOM 224 C CA . ASP A 1 41 ? 10.512 -26.733 -0.351 1.00 36.32 ? 39 ASP A CA 1 ATOM 225 C C . ASP A 1 41 ? 11.236 -26.464 -1.656 1.00 35.15 ? 39 ASP A C 1 ATOM 226 O O . ASP A 1 41 ? 10.616 -26.176 -2.680 1.00 36.73 ? 39 ASP A O 1 ATOM 227 C CB . ASP A 1 41 ? 9.724 -28.032 -0.510 1.00 37.85 ? 39 ASP A CB 1 ATOM 228 C CG . ASP A 1 41 ? 9.019 -28.458 0.760 1.00 44.32 ? 39 ASP A CG 1 ATOM 229 O OD1 . ASP A 1 41 ? 9.128 -27.712 1.759 1.00 45.20 ? 39 ASP A OD1 1 ATOM 230 O OD2 . ASP A 1 41 ? 8.338 -29.524 0.744 1.00 43.42 ? 39 ASP A OD2 1 ATOM 231 N N . TRP A 1 42 ? 12.554 -26.564 -1.620 1.00 32.12 ? 40 TRP A N 1 ATOM 232 C CA . TRP A 1 42 ? 13.322 -26.541 -2.845 1.00 30.55 ? 40 TRP A CA 1 ATOM 233 C C . TRP A 1 42 ? 13.850 -27.933 -3.147 1.00 31.02 ? 40 TRP A C 1 ATOM 234 O O . TRP A 1 42 ? 14.700 -28.453 -2.427 1.00 29.50 ? 40 TRP A O 1 ATOM 235 C CB . TRP A 1 42 ? 14.483 -25.564 -2.731 1.00 29.79 ? 40 TRP A CB 1 ATOM 236 C CG . TRP A 1 42 ? 14.115 -24.140 -2.952 1.00 28.20 ? 40 TRP A CG 1 ATOM 237 C CD1 . TRP A 1 42 ? 13.832 -23.201 -2.000 1.00 29.22 ? 40 TRP A CD1 1 ATOM 238 C CD2 . TRP A 1 42 ? 14.025 -23.476 -4.207 1.00 20.46 ? 40 TRP A CD2 1 ATOM 239 N NE1 . TRP A 1 42 ? 13.562 -21.993 -2.593 1.00 24.72 ? 40 TRP A NE1 1 ATOM 240 C CE2 . TRP A 1 42 ? 13.665 -22.143 -3.950 1.00 22.84 ? 40 TRP A CE2 1 ATOM 241 C CE3 . TRP A 1 42 ? 14.196 -23.885 -5.524 1.00 22.96 ? 40 TRP A CE3 1 ATOM 242 C CZ2 . TRP A 1 42 ? 13.472 -21.220 -4.963 1.00 28.63 ? 40 TRP A CZ2 1 ATOM 243 C CZ3 . TRP A 1 42 ? 14.010 -22.962 -6.532 1.00 26.69 ? 40 TRP A CZ3 1 ATOM 244 C CH2 . TRP A 1 42 ? 13.655 -21.647 -6.246 1.00 27.79 ? 40 TRP A CH2 1 ATOM 245 N N . LEU A 1 43 ? 13.334 -28.531 -4.217 1.00 33.25 ? 41 LEU A N 1 ATOM 246 C CA . LEU A 1 43 ? 13.799 -29.850 -4.664 1.00 34.47 ? 41 LEU A CA 1 ATOM 247 C C . LEU A 1 43 ? 14.646 -29.730 -5.902 1.00 34.32 ? 41 LEU A C 1 ATOM 248 O O . LEU A 1 43 ? 14.484 -28.798 -6.687 1.00 36.77 ? 41 LEU A O 1 ATOM 249 C CB . LEU A 1 43 ? 12.631 -30.793 -4.965 1.00 35.56 ? 41 LEU A CB 1 ATOM 250 C CG . LEU A 1 43 ? 11.630 -31.031 -3.842 1.00 35.86 ? 41 LEU A CG 1 ATOM 251 C CD1 . LEU A 1 43 ? 10.313 -30.377 -4.214 1.00 38.57 ? 41 LEU A CD1 1 ATOM 252 C CD2 . LEU A 1 43 ? 11.446 -32.530 -3.593 1.00 36.42 ? 41 LEU A CD2 1 ATOM 253 N N . PHE A 1 44 ? 15.544 -30.691 -6.074 1.00 33.91 ? 42 PHE A N 1 ATOM 254 C CA . PHE A 1 44 ? 16.425 -30.724 -7.233 1.00 32.90 ? 42 PHE A CA 1 ATOM 255 C C . PHE A 1 44 ? 16.295 -32.033 -7.971 1.00 36.39 ? 42 PHE A C 1 ATOM 256 O O . PHE A 1 44 ? 16.314 -33.126 -7.379 1.00 37.25 ? 42 PHE A O 1 ATOM 257 C CB . PHE A 1 44 ? 17.890 -30.543 -6.823 1.00 31.83 ? 42 PHE A CB 1 ATOM 258 C CG . PHE A 1 44 ? 18.854 -30.861 -7.927 1.00 28.72 ? 42 PHE A CG 1 ATOM 259 C CD1 . PHE A 1 44 ? 19.122 -29.936 -8.913 1.00 28.07 ? 42 PHE A CD1 1 ATOM 260 C CD2 . PHE A 1 44 ? 19.452 -32.106 -8.005 1.00 26.93 ? 42 PHE A CD2 1 ATOM 261 C CE1 . PHE A 1 44 ? 19.980 -30.241 -9.949 1.00 30.40 ? 42 PHE A CE1 1 ATOM 262 C CE2 . PHE A 1 44 ? 20.307 -32.417 -9.034 1.00 25.54 ? 42 PHE A CE2 1 ATOM 263 C CZ . PHE A 1 44 ? 20.572 -31.488 -10.009 1.00 28.35 ? 42 PHE A CZ 1 ATOM 264 N N . SER A 1 45 ? 16.171 -31.915 -9.282 1.00 37.51 ? 43 SER A N 1 ATOM 265 C CA . SER A 1 45 ? 16.082 -33.098 -10.115 1.00 39.83 ? 43 SER A CA 1 ATOM 266 C C . SER A 1 45 ? 16.820 -32.912 -11.427 1.00 40.26 ? 43 SER A C 1 ATOM 267 O O . SER A 1 45 ? 16.710 -31.879 -12.103 1.00 38.95 ? 43 SER A O 1 ATOM 268 C CB . SER A 1 45 ? 14.629 -33.460 -10.368 1.00 41.44 ? 43 SER A CB 1 ATOM 269 O OG . SER A 1 45 ? 14.434 -34.844 -10.156 1.00 48.32 ? 43 SER A OG 1 ATOM 270 N N . LYS A 1 46 ? 17.611 -33.929 -11.732 1.00 40.31 ? 44 LYS A N 1 ATOM 271 C CA . LYS A 1 46 ? 18.343 -34.007 -12.980 1.00 39.47 ? 44 LYS A CA 1 ATOM 272 C C . LYS A 1 46 ? 17.346 -34.236 -14.095 1.00 41.49 ? 44 LYS A C 1 ATOM 273 O O . LYS A 1 46 ? 16.350 -34.934 -13.938 1.00 44.36 ? 44 LYS A O 1 ATOM 274 C CB . LYS A 1 46 ? 19.397 -35.124 -12.941 1.00 40.84 ? 44 LYS A CB 1 ATOM 275 C CG . LYS A 1 46 ? 20.585 -34.828 -12.021 1.00 35.10 ? 44 LYS A CG 1 ATOM 276 C CD . LYS A 1 46 ? 21.791 -35.670 -12.397 1.00 41.67 ? 44 LYS A CD 1 ATOM 277 C CE . LYS A 1 46 ? 21.757 -37.038 -11.699 1.00 56.79 ? 44 LYS A CE 1 ATOM 278 N NZ . LYS A 1 46 ? 22.497 -38.127 -12.435 1.00 63.20 ? 44 LYS A NZ 1 ATOM 279 N N . ASP A 1 47 ? 17.624 -33.604 -15.217 1.00 42.09 ? 45 ASP A N 1 ATOM 280 C CA . ASP A 1 47 ? 16.786 -33.694 -16.394 1.00 45.62 ? 45 ASP A CA 1 ATOM 281 C C . ASP A 1 47 ? 16.461 -35.145 -16.716 1.00 49.66 ? 45 ASP A C 1 ATOM 282 O O . ASP A 1 47 ? 17.347 -36.007 -16.783 1.00 50.45 ? 45 ASP A O 1 ATOM 283 C CB . ASP A 1 47 ? 17.492 -33.016 -17.569 1.00 46.90 ? 45 ASP A CB 1 ATOM 284 C CG . ASP A 1 47 ? 16.658 -32.996 -18.827 1.00 53.10 ? 45 ASP A CG 1 ATOM 285 O OD1 . ASP A 1 47 ? 16.624 -34.018 -19.541 1.00 60.96 ? 45 ASP A OD1 1 ATOM 286 O OD2 . ASP A 1 47 ? 16.067 -31.938 -19.127 1.00 63.30 ? 45 ASP A OD2 1 ATOM 287 N N . LYS A 1 48 ? 15.165 -35.387 -16.891 1.00 52.03 ? 46 LYS A N 1 ATOM 288 C CA . LYS A 1 48 ? 14.629 -36.648 -17.388 1.00 56.22 ? 46 LYS A CA 1 ATOM 289 C C . LYS A 1 48 ? 14.786 -37.789 -16.382 1.00 57.36 ? 46 LYS A C 1 ATOM 290 O O . LYS A 1 48 ? 14.629 -38.966 -16.711 1.00 60.21 ? 46 LYS A O 1 ATOM 291 C CB . LYS A 1 48 ? 15.282 -37.006 -18.720 1.00 58.95 ? 46 LYS A CB 1 ATOM 292 C CG . LYS A 1 48 ? 14.310 -37.480 -19.768 1.00 64.98 ? 46 LYS A CG 1 ATOM 293 C CD . LYS A 1 48 ? 15.065 -37.967 -20.970 1.00 71.14 ? 46 LYS A CD 1 ATOM 294 C CE . LYS A 1 48 ? 14.126 -38.377 -22.099 1.00 76.40 ? 46 LYS A CE 1 ATOM 295 N NZ . LYS A 1 48 ? 14.848 -38.500 -23.398 1.00 72.92 ? 46 LYS A NZ 1 ATOM 296 N N . ASP A 1 49 ? 15.065 -37.416 -15.143 1.00 55.02 ? 47 ASP A N 1 ATOM 297 C CA . ASP A 1 49 ? 15.255 -38.383 -14.060 1.00 54.95 ? 47 ASP A CA 1 ATOM 298 C C . ASP A 1 49 ? 14.280 -38.054 -12.940 1.00 54.13 ? 47 ASP A C 1 ATOM 299 O O . ASP A 1 49 ? 14.189 -36.910 -12.498 1.00 52.28 ? 47 ASP A O 1 ATOM 300 C CB . ASP A 1 49 ? 16.728 -38.335 -13.614 1.00 52.83 ? 47 ASP A CB 1 ATOM 301 C CG . ASP A 1 49 ? 16.950 -38.739 -12.164 1.00 51.33 ? 47 ASP A CG 1 ATOM 302 O OD1 . ASP A 1 49 ? 16.556 -39.857 -11.779 1.00 45.12 ? 47 ASP A OD1 1 ATOM 303 O OD2 . ASP A 1 49 ? 17.585 -37.935 -11.427 1.00 51.96 ? 47 ASP A OD2 1 ATOM 304 N N . ASP A 1 50 ? 13.542 -39.068 -12.508 1.00 57.06 ? 48 ASP A N 1 ATOM 305 C CA . ASP A 1 50 ? 12.458 -38.896 -11.519 1.00 57.41 ? 48 ASP A CA 1 ATOM 306 C C . ASP A 1 50 ? 12.980 -38.858 -10.095 1.00 54.60 ? 48 ASP A C 1 ATOM 307 O O . ASP A 1 50 ? 12.321 -38.347 -9.186 1.00 54.93 ? 48 ASP A O 1 ATOM 308 C CB . ASP A 1 50 ? 11.383 -39.977 -11.656 1.00 62.03 ? 48 ASP A CB 1 ATOM 309 C CG . ASP A 1 50 ? 10.411 -39.678 -12.785 1.00 69.39 ? 48 ASP A CG 1 ATOM 310 O OD1 . ASP A 1 50 ? 10.407 -38.507 -13.245 1.00 71.84 ? 48 ASP A OD1 1 ATOM 311 O OD2 . ASP A 1 50 ? 9.666 -40.598 -13.212 1.00 71.27 ? 48 ASP A OD2 1 ATOM 312 N N . ALA A 1 51 ? 14.175 -39.396 -9.907 1.00 52.80 ? 49 ALA A N 1 ATOM 313 C CA . ALA A 1 51 ? 14.889 -39.193 -8.653 1.00 48.74 ? 49 ALA A CA 1 ATOM 314 C C . ALA A 1 51 ? 14.953 -37.699 -8.388 1.00 44.46 ? 49 ALA A C 1 ATOM 315 O O . ALA A 1 51 ? 14.959 -36.893 -9.301 1.00 43.13 ? 49 ALA A O 1 ATOM 316 C CB . ALA A 1 51 ? 16.290 -39.784 -8.720 1.00 46.84 ? 49 ALA A CB 1 ATOM 317 N N . SER A 1 52 ? 14.996 -37.345 -7.118 1.00 43.86 ? 50 SER A N 1 ATOM 318 C CA . SER A 1 52 ? 15.102 -35.949 -6.714 1.00 41.84 ? 50 SER A CA 1 ATOM 319 C C . SER A 1 52 ? 15.528 -35.804 -5.249 1.00 40.94 ? 50 SER A C 1 ATOM 320 O O . SER A 1 52 ? 15.277 -36.675 -4.420 1.00 40.24 ? 50 SER A O 1 ATOM 321 C CB . SER A 1 52 ? 13.769 -35.236 -6.928 1.00 42.47 ? 50 SER A CB 1 ATOM 322 O OG . SER A 1 52 ? 12.880 -35.579 -5.880 1.00 43.13 ? 50 SER A OG 1 ATOM 323 N N . GLU A 1 53 ? 16.177 -34.683 -4.947 1.00 39.05 ? 51 GLU A N 1 ATOM 324 C CA . GLU A 1 53 ? 16.696 -34.449 -3.607 1.00 37.48 ? 51 GLU A CA 1 ATOM 325 C C . GLU A 1 53 ? 16.410 -33.049 -3.070 1.00 34.35 ? 51 GLU A C 1 ATOM 326 O O . GLU A 1 53 ? 16.431 -32.073 -3.800 1.00 35.20 ? 51 GLU A O 1 ATOM 327 C CB . GLU A 1 53 ? 18.192 -34.788 -3.565 1.00 38.17 ? 51 GLU A CB 1 ATOM 328 C CG . GLU A 1 53 ? 19.100 -34.009 -4.511 1.00 43.72 ? 51 GLU A CG 1 ATOM 329 C CD . GLU A 1 53 ? 20.502 -34.637 -4.654 1.00 49.49 ? 51 GLU A CD 1 ATOM 330 O OE1 . GLU A 1 53 ? 21.104 -35.019 -3.631 1.00 53.56 ? 51 GLU A OE1 1 ATOM 331 O OE2 . GLU A 1 53 ? 21.006 -34.747 -5.796 1.00 52.89 ? 51 GLU A OE2 1 ATOM 332 N N . TYR A 1 54 ? 16.095 -32.986 -1.782 1.00 34.16 ? 52 TYR A N 1 ATOM 333 C CA . TYR A 1 54 ? 15.893 -31.708 -1.069 1.00 32.79 ? 52 TYR A CA 1 ATOM 334 C C . TYR A 1 54 ? 17.170 -30.888 -1.018 1.00 30.30 ? 52 TYR A C 1 ATOM 335 O O . TYR A 1 54 ? 18.234 -31.383 -0.671 1.00 29.84 ? 52 TYR A O 1 ATOM 336 C CB . TYR A 1 54 ? 15.355 -31.905 0.369 1.00 32.80 ? 52 TYR A CB 1 ATOM 337 C CG . TYR A 1 54 ? 13.858 -32.083 0.415 1.00 38.95 ? 52 TYR A CG 1 ATOM 338 C CD1 . TYR A 1 54 ? 13.289 -33.331 0.231 1.00 36.63 ? 52 TYR A CD1 1 ATOM 339 C CD2 . TYR A 1 54 ? 13.005 -30.995 0.615 1.00 41.98 ? 52 TYR A CD2 1 ATOM 340 C CE1 . TYR A 1 54 ? 11.936 -33.496 0.239 1.00 42.54 ? 52 TYR A CE1 1 ATOM 341 C CE2 . TYR A 1 54 ? 11.634 -31.156 0.631 1.00 39.97 ? 52 TYR A CE2 1 ATOM 342 C CZ . TYR A 1 54 ? 11.103 -32.418 0.438 1.00 45.12 ? 52 TYR A CZ 1 ATOM 343 O OH . TYR A 1 54 ? 9.730 -32.635 0.440 1.00 52.21 ? 52 TYR A OH 1 ATOM 344 N N . VAL A 1 55 ? 17.008 -29.620 -1.360 1.00 29.18 ? 53 VAL A N 1 ATOM 345 C CA . VAL A 1 55 ? 18.078 -28.646 -1.362 1.00 28.83 ? 53 VAL A CA 1 ATOM 346 C C . VAL A 1 55 ? 18.011 -27.805 -0.101 1.00 30.83 ? 53 VAL A C 1 ATOM 347 O O . VAL A 1 55 ? 18.987 -27.681 0.656 1.00 33.80 ? 53 VAL A O 1 ATOM 348 C CB . VAL A 1 55 ? 17.956 -27.710 -2.562 1.00 28.12 ? 53 VAL A CB 1 ATOM 349 C CG1 . VAL A 1 55 ? 18.931 -26.540 -2.437 1.00 23.76 ? 53 VAL A CG1 1 ATOM 350 C CG2 . VAL A 1 55 ? 18.186 -28.504 -3.843 1.00 30.99 ? 53 VAL A CG2 1 ATOM 351 N N . LEU A 1 56 ? 16.840 -27.228 0.112 1.00 29.77 ? 54 LEU A N 1 ATOM 352 C CA . LEU A 1 56 ? 16.574 -26.436 1.302 1.00 30.42 ? 54 LEU A CA 1 ATOM 353 C C . LEU A 1 56 ? 15.082 -26.438 1.597 1.00 32.56 ? 54 LEU A C 1 ATOM 354 O O . LEU A 1 56 ? 14.252 -26.328 0.685 1.00 34.34 ? 54 LEU A O 1 ATOM 355 C CB . LEU A 1 56 ? 17.066 -25.011 1.080 1.00 29.38 ? 54 LEU A CB 1 ATOM 356 C CG . LEU A 1 56 ? 16.723 -23.973 2.155 1.00 33.73 ? 54 LEU A CG 1 ATOM 357 C CD1 . LEU A 1 56 ? 17.701 -22.791 2.125 1.00 24.06 ? 54 LEU A CD1 1 ATOM 358 C CD2 . LEU A 1 56 ? 15.282 -23.492 1.990 1.00 28.61 ? 54 LEU A CD2 1 ATOM 359 N N . PHE A 1 57 ? 14.726 -26.594 2.860 1.00 31.98 ? 55 PHE A N 1 ATOM 360 C CA . PHE A 1 57 ? 13.330 -26.466 3.216 1.00 32.55 ? 55 PHE A CA 1 ATOM 361 C C . PHE A 1 57 ? 13.137 -25.665 4.472 1.00 34.24 ? 55 PHE A C 1 ATOM 362 O O . PHE A 1 57 ? 13.941 -25.710 5.395 1.00 34.93 ? 55 PHE A O 1 ATOM 363 C CB . PHE A 1 57 ? 12.637 -27.827 3.300 1.00 33.52 ? 55 PHE A CB 1 ATOM 364 C CG . PHE A 1 57 ? 12.966 -28.609 4.517 1.00 33.42 ? 55 PHE A CG 1 ATOM 365 C CD1 . PHE A 1 57 ? 12.268 -28.415 5.689 1.00 38.10 ? 55 PHE A CD1 1 ATOM 366 C CD2 . PHE A 1 57 ? 13.953 -29.572 4.481 1.00 36.80 ? 55 PHE A CD2 1 ATOM 367 C CE1 . PHE A 1 57 ? 12.565 -29.150 6.819 1.00 40.47 ? 55 PHE A CE1 1 ATOM 368 C CE2 . PHE A 1 57 ? 14.258 -30.320 5.601 1.00 40.94 ? 55 PHE A CE2 1 ATOM 369 C CZ . PHE A 1 57 ? 13.557 -30.109 6.777 1.00 44.14 ? 55 PHE A CZ 1 ATOM 370 N N . TYR A 1 58 ? 12.047 -24.914 4.460 1.00 35.41 ? 56 TYR A N 1 ATOM 371 C CA . TYR A 1 58 ? 11.766 -23.912 5.470 1.00 37.00 ? 56 TYR A CA 1 ATOM 372 C C . TYR A 1 58 ? 10.339 -24.044 5.958 1.00 41.12 ? 56 TYR A C 1 ATOM 373 O O . TYR A 1 58 ? 9.416 -24.176 5.156 1.00 43.87 ? 56 TYR A O 1 ATOM 374 C CB . TYR A 1 58 ? 12.002 -22.524 4.891 1.00 34.83 ? 56 TYR A CB 1 ATOM 375 C CG . TYR A 1 58 ? 11.393 -21.416 5.700 1.00 39.65 ? 56 TYR A CG 1 ATOM 376 C CD1 . TYR A 1 58 ? 12.019 -20.938 6.840 1.00 49.53 ? 56 TYR A CD1 1 ATOM 377 C CD2 . TYR A 1 58 ? 10.194 -20.844 5.328 1.00 42.52 ? 56 TYR A CD2 1 ATOM 378 C CE1 . TYR A 1 58 ? 11.456 -19.915 7.588 1.00 56.36 ? 56 TYR A CE1 1 ATOM 379 C CE2 . TYR A 1 58 ? 9.627 -19.824 6.055 1.00 49.19 ? 56 TYR A CE2 1 ATOM 380 C CZ . TYR A 1 58 ? 10.254 -19.359 7.186 1.00 57.27 ? 56 TYR A CZ 1 ATOM 381 O OH . TYR A 1 58 ? 9.668 -18.342 7.916 1.00 63.80 ? 56 TYR A OH 1 ATOM 382 N N . TYR A 1 59 ? 10.173 -24.056 7.277 1.00 42.86 ? 57 TYR A N 1 ATOM 383 C CA . TYR A 1 59 ? 8.848 -24.175 7.886 1.00 46.45 ? 57 TYR A CA 1 ATOM 384 C C . TYR A 1 59 ? 8.817 -23.712 9.328 1.00 49.42 ? 57 TYR A C 1 ATOM 385 O O . TYR A 1 59 ? 9.709 -24.000 10.105 1.00 50.45 ? 57 TYR A O 1 ATOM 386 C CB . TYR A 1 59 ? 8.332 -25.612 7.803 1.00 45.96 ? 57 TYR A CB 1 ATOM 387 C CG . TYR A 1 59 ? 8.868 -26.539 8.867 1.00 49.35 ? 57 TYR A CG 1 ATOM 388 C CD1 . TYR A 1 59 ? 10.233 -26.755 9.012 1.00 47.14 ? 57 TYR A CD1 1 ATOM 389 C CD2 . TYR A 1 59 ? 8.010 -27.232 9.703 1.00 53.10 ? 57 TYR A CD2 1 ATOM 390 C CE1 . TYR A 1 59 ? 10.723 -27.616 9.972 1.00 42.13 ? 57 TYR A CE1 1 ATOM 391 C CE2 . TYR A 1 59 ? 8.499 -28.097 10.663 1.00 55.41 ? 57 TYR A CE2 1 ATOM 392 C CZ . TYR A 1 59 ? 9.856 -28.281 10.787 1.00 48.48 ? 57 TYR A CZ 1 ATOM 393 O OH . TYR A 1 59 ? 10.337 -29.135 11.742 1.00 56.31 ? 57 TYR A OH 1 ATOM 394 N N . SER A 1 60 ? 7.768 -22.983 9.666 1.00 52.77 ? 58 SER A N 1 ATOM 395 C CA . SER A 1 60 ? 7.639 -22.421 10.987 1.00 57.43 ? 58 SER A CA 1 ATOM 396 C C . SER A 1 60 ? 8.966 -21.847 11.428 1.00 56.91 ? 58 SER A C 1 ATOM 397 O O . SER A 1 60 ? 9.564 -22.308 12.394 1.00 58.42 ? 58 SER A O 1 ATOM 398 C CB . SER A 1 60 ? 7.160 -23.481 11.982 1.00 60.23 ? 58 SER A CB 1 ATOM 399 O OG . SER A 1 60 ? 8.037 -24.588 12.025 1.00 60.97 ? 58 SER A OG 1 ATOM 400 N N . ASN A 1 61 ? 9.427 -20.850 10.685 1.00 57.02 ? 59 ASN A N 1 ATOM 401 C CA . ASN A 1 61 ? 10.602 -20.049 11.066 1.00 57.89 ? 59 ASN A CA 1 ATOM 402 C C . ASN A 1 61 ? 11.873 -20.883 11.219 1.00 54.95 ? 59 ASN A C 1 ATOM 403 O O . ASN A 1 61 ? 12.802 -20.495 11.911 1.00 56.18 ? 59 ASN A O 1 ATOM 404 C CB . ASN A 1 61 ? 10.330 -19.269 12.365 1.00 62.42 ? 59 ASN A CB 1 ATOM 405 C CG . ASN A 1 61 ? 9.224 -18.225 12.212 1.00 67.09 ? 59 ASN A CG 1 ATOM 406 O OD1 . ASN A 1 61 ? 9.038 -17.653 11.138 1.00 71.42 ? 59 ASN A OD1 1 ATOM 407 N ND2 . ASN A 1 61 ? 8.497 -17.967 13.294 1.00 73.02 ? 59 ASN A ND2 1 ATOM 408 N N . LEU A 1 62 ? 11.900 -22.032 10.557 1.00 51.65 ? 60 LEU A N 1 ATOM 409 C CA . LEU A 1 62 ? 13.048 -22.929 10.615 1.00 48.55 ? 60 LEU A CA 1 ATOM 410 C C . LEU A 1 62 ? 13.605 -23.259 9.246 1.00 45.95 ? 60 LEU A C 1 ATOM 411 O O . LEU A 1 62 ? 12.936 -23.887 8.434 1.00 44.13 ? 60 LEU A O 1 ATOM 412 C CB . LEU A 1 62 ? 12.646 -24.221 11.303 1.00 47.77 ? 60 LEU A CB 1 ATOM 413 C CG . LEU A 1 62 ? 12.254 -24.012 12.756 1.00 48.34 ? 60 LEU A CG 1 ATOM 414 C CD1 . LEU A 1 62 ? 11.554 -25.242 13.272 1.00 49.33 ? 60 LEU A CD1 1 ATOM 415 C CD2 . LEU A 1 62 ? 13.475 -23.689 13.600 1.00 43.31 ? 60 LEU A CD2 1 ATOM 416 N N . SER A 1 63 ? 14.849 -22.852 9.013 1.00 45.54 ? 61 SER A N 1 ATOM 417 C CA . SER A 1 63 ? 15.507 -23.083 7.727 1.00 42.61 ? 61 SER A CA 1 ATOM 418 C C . SER A 1 63 ? 16.501 -24.218 7.786 1.00 40.87 ? 61 SER A C 1 ATOM 419 O O . SER A 1 63 ? 17.459 -24.188 8.547 1.00 42.08 ? 61 SER A O 1 ATOM 420 C CB . SER A 1 63 ? 16.220 -21.835 7.247 1.00 42.12 ? 61 SER A CB 1 ATOM 421 O OG . SER A 1 63 ? 16.572 -22.004 5.884 1.00 45.51 ? 61 SER A OG 1 ATOM 422 N N . VAL A 1 64 ? 16.266 -25.207 6.938 1.00 38.62 ? 62 VAL A N 1 ATOM 423 C CA . VAL A 1 64 ? 17.041 -26.436 6.946 1.00 37.21 ? 62 VAL A CA 1 ATOM 424 C C . VAL A 1 64 ? 17.658 -26.715 5.584 1.00 35.68 ? 62 VAL A C 1 ATOM 425 O O . VAL A 1 64 ? 17.096 -27.456 4.782 1.00 36.51 ? 62 VAL A O 1 ATOM 426 C CB . VAL A 1 64 ? 16.161 -27.612 7.369 1.00 37.91 ? 62 VAL A CB 1 ATOM 427 C CG1 . VAL A 1 64 ? 16.952 -28.912 7.386 1.00 34.66 ? 62 VAL A CG1 1 ATOM 428 C CG2 . VAL A 1 64 ? 15.566 -27.332 8.736 1.00 40.15 ? 62 VAL A CG2 1 ATOM 429 N N . PRO A 1 65 ? 18.816 -26.104 5.302 1.00 35.26 ? 63 PRO A N 1 ATOM 430 C CA . PRO A 1 65 ? 19.513 -26.510 4.078 1.00 33.48 ? 63 PRO A CA 1 ATOM 431 C C . PRO A 1 65 ? 19.988 -27.918 4.257 1.00 34.04 ? 63 PRO A C 1 ATOM 432 O O . PRO A 1 65 ? 20.493 -28.269 5.318 1.00 36.11 ? 63 PRO A O 1 ATOM 433 C CB . PRO A 1 65 ? 20.706 -25.550 3.996 1.00 34.53 ? 63 PRO A CB 1 ATOM 434 C CG . PRO A 1 65 ? 20.838 -24.946 5.385 1.00 34.82 ? 63 PRO A CG 1 ATOM 435 C CD . PRO A 1 65 ? 19.479 -24.990 6.002 1.00 35.67 ? 63 PRO A CD 1 ATOM 436 N N . THR A 1 66 ? 19.804 -28.734 3.237 1.00 33.74 ? 64 THR A N 1 ATOM 437 C CA . THR A 1 66 ? 20.074 -30.162 3.386 1.00 35.11 ? 64 THR A CA 1 ATOM 438 C C . THR A 1 66 ? 20.989 -30.741 2.325 1.00 34.08 ? 64 THR A C 1 ATOM 439 O O . THR A 1 66 ? 21.310 -30.116 1.306 1.00 32.26 ? 64 THR A O 1 ATOM 440 C CB . THR A 1 66 ? 18.753 -31.002 3.366 1.00 35.70 ? 64 THR A CB 1 ATOM 441 O OG1 . THR A 1 66 ? 18.313 -31.180 2.013 1.00 35.25 ? 64 THR A OG1 1 ATOM 442 C CG2 . THR A 1 66 ? 17.654 -30.324 4.166 1.00 33.73 ? 64 THR A CG2 1 ATOM 443 N N . GLY A 1 67 ? 21.370 -31.976 2.608 1.00 35.30 ? 65 GLY A N 1 ATOM 444 C CA . GLY A 1 67 ? 22.089 -32.834 1.694 1.00 36.10 ? 65 GLY A CA 1 ATOM 445 C C . GLY A 1 67 ? 23.437 -32.290 1.320 1.00 38.49 ? 65 GLY A C 1 ATOM 446 O O . GLY A 1 67 ? 24.184 -31.778 2.148 1.00 41.01 ? 65 GLY A O 1 ATOM 447 N N . ARG A 1 68 ? 23.733 -32.400 0.039 1.00 38.82 ? 66 ARG A N 1 ATOM 448 C CA . ARG A 1 68 ? 25.000 -31.931 -0.488 1.00 38.54 ? 66 ARG A CA 1 ATOM 449 C C . ARG A 1 68 ? 24.930 -30.433 -0.758 1.00 36.15 ? 66 ARG A C 1 ATOM 450 O O . ARG A 1 68 ? 25.900 -29.846 -1.206 1.00 38.65 ? 66 ARG A O 1 ATOM 451 C CB . ARG A 1 68 ? 25.400 -32.722 -1.743 1.00 38.98 ? 66 ARG A CB 1 ATOM 452 C CG . ARG A 1 68 ? 24.525 -32.506 -2.979 1.00 36.59 ? 66 ARG A CG 1 ATOM 453 C CD . ARG A 1 68 ? 24.922 -33.479 -4.092 1.00 37.01 ? 66 ARG A CD 1 ATOM 454 N NE . ARG A 1 68 ? 23.928 -33.521 -5.160 1.00 37.62 ? 66 ARG A NE 1 ATOM 455 C CZ . ARG A 1 68 ? 23.752 -32.550 -6.051 1.00 42.83 ? 66 ARG A CZ 1 ATOM 456 N NH1 . ARG A 1 68 ? 24.502 -31.455 -6.006 1.00 46.55 ? 66 ARG A NH1 1 ATOM 457 N NH2 . ARG A 1 68 ? 22.822 -32.662 -6.992 1.00 44.20 ? 66 ARG A NH2 1 ATOM 458 N N . PHE A 1 69 ? 23.782 -29.825 -0.480 1.00 33.71 ? 67 PHE A N 1 ATOM 459 C CA . PHE A 1 69 ? 23.624 -28.364 -0.611 1.00 31.37 ? 67 PHE A CA 1 ATOM 460 C C . PHE A 1 69 ? 23.684 -27.725 0.757 1.00 32.47 ? 67 PHE A C 1 ATOM 461 O O . PHE A 1 69 ? 23.562 -26.510 0.913 1.00 31.09 ? 67 PHE A O 1 ATOM 462 C CB . PHE A 1 69 ? 22.297 -27.990 -1.249 1.00 27.76 ? 67 PHE A CB 1 ATOM 463 C CG . PHE A 1 69 ? 22.051 -28.650 -2.556 1.00 27.99 ? 67 PHE A CG 1 ATOM 464 C CD1 . PHE A 1 69 ? 21.608 -29.964 -2.607 1.00 30.42 ? 67 PHE A CD1 1 ATOM 465 C CD2 . PHE A 1 69 ? 22.232 -27.959 -3.735 1.00 19.66 ? 67 PHE A CD2 1 ATOM 466 C CE1 . PHE A 1 69 ? 21.362 -30.578 -3.820 1.00 27.80 ? 67 PHE A CE1 1 ATOM 467 C CE2 . PHE A 1 69 ? 21.984 -28.566 -4.940 1.00 23.36 ? 67 PHE A CE2 1 ATOM 468 C CZ . PHE A 1 69 ? 21.557 -29.877 -4.984 1.00 26.76 ? 67 PHE A CZ 1 ATOM 469 N N . GLN A 1 70 ? 23.875 -28.587 1.734 1.00 34.54 ? 68 GLN A N 1 ATOM 470 C CA . GLN A 1 70 ? 23.908 -28.202 3.144 1.00 39.50 ? 68 GLN A CA 1 ATOM 471 C C . GLN A 1 70 ? 24.718 -26.950 3.444 1.00 41.91 ? 68 GLN A C 1 ATOM 472 O O . GLN A 1 70 ? 24.356 -26.177 4.321 1.00 44.51 ? 68 GLN A O 1 ATOM 473 C CB . GLN A 1 70 ? 24.508 -29.335 3.958 1.00 43.36 ? 68 GLN A CB 1 ATOM 474 C CG . GLN A 1 70 ? 24.193 -29.311 5.407 1.00 46.83 ? 68 GLN A CG 1 ATOM 475 C CD . GLN A 1 70 ? 24.587 -30.618 6.042 1.00 54.55 ? 68 GLN A CD 1 ATOM 476 O OE1 . GLN A 1 70 ? 24.982 -30.667 7.211 1.00 63.82 ? 68 GLN A OE1 1 ATOM 477 N NE2 . GLN A 1 70 ? 24.511 -31.698 5.258 1.00 46.19 ? 68 GLN A NE2 1 ATOM 478 N N . ASN A 1 71 ? 25.819 -26.762 2.734 1.00 42.45 ? 69 ASN A N 1 ATOM 479 C CA . ASN A 1 71 ? 26.725 -25.656 3.027 1.00 45.38 ? 69 ASN A CA 1 ATOM 480 C C . ASN A 1 71 ? 26.605 -24.519 2.045 1.00 42.20 ? 69 ASN A C 1 ATOM 481 O O . ASN A 1 71 ? 27.279 -23.500 2.185 1.00 42.77 ? 69 ASN A O 1 ATOM 482 C CB . ASN A 1 71 ? 28.171 -26.135 3.007 1.00 48.44 ? 69 ASN A CB 1 ATOM 483 C CG . ASN A 1 71 ? 28.552 -26.862 4.260 1.00 60.05 ? 69 ASN A CG 1 ATOM 484 O OD1 . ASN A 1 71 ? 28.211 -26.443 5.362 1.00 71.38 ? 69 ASN A OD1 1 ATOM 485 N ND2 . ASN A 1 71 ? 29.263 -27.960 4.114 1.00 70.41 ? 69 ASN A ND2 1 ATOM 486 N N . ARG A 1 72 ? 25.746 -24.700 1.055 1.00 38.42 ? 70 ARG A N 1 ATOM 487 C CA . ARG A 1 72 ? 25.761 -23.835 -0.128 1.00 36.79 ? 70 ARG A CA 1 ATOM 488 C C . ARG A 1 72 ? 24.484 -23.050 -0.375 1.00 35.10 ? 70 ARG A C 1 ATOM 489 O O . ARG A 1 72 ? 24.507 -22.065 -1.117 1.00 33.61 ? 70 ARG A O 1 ATOM 490 C CB . ARG A 1 72 ? 26.041 -24.674 -1.369 1.00 35.60 ? 70 ARG A CB 1 ATOM 491 C CG . ARG A 1 72 ? 27.393 -25.330 -1.343 1.00 38.17 ? 70 ARG A CG 1 ATOM 492 C CD . ARG A 1 72 ? 27.743 -25.913 -2.692 1.00 37.29 ? 70 ARG A CD 1 ATOM 493 N NE . ARG A 1 72 ? 27.021 -27.150 -2.962 1.00 32.43 ? 70 ARG A NE 1 ATOM 494 C CZ . ARG A 1 72 ? 26.789 -27.610 -4.183 1.00 30.75 ? 70 ARG A CZ 1 ATOM 495 N NH1 . ARG A 1 72 ? 27.202 -26.927 -5.223 1.00 34.29 ? 70 ARG A NH1 1 ATOM 496 N NH2 . ARG A 1 72 ? 26.135 -28.740 -4.369 1.00 35.97 ? 70 ARG A NH2 1 ATOM 497 N N . SER A 1 73 ? 23.385 -23.512 0.227 1.00 33.40 ? 71 SER A N 1 ATOM 498 C CA . SER A 1 73 ? 22.043 -22.984 -0.040 1.00 32.21 ? 71 SER A CA 1 ATOM 499 C C . SER A 1 73 ? 21.479 -22.143 1.084 1.00 34.16 ? 71 SER A C 1 ATOM 500 O O . SER A 1 73 ? 21.454 -22.547 2.246 1.00 35.42 ? 71 SER A O 1 ATOM 501 C CB . SER A 1 73 ? 21.086 -24.131 -0.303 1.00 31.16 ? 71 SER A CB 1 ATOM 502 O OG . SER A 1 73 ? 21.254 -25.124 0.681 1.00 34.05 ? 71 SER A OG 1 ATOM 503 N N . HIS A 1 74 ? 20.999 -20.967 0.710 1.00 34.32 ? 72 HIS A N 1 ATOM 504 C CA . HIS A 1 74 ? 20.427 -20.041 1.669 1.00 36.90 ? 72 HIS A CA 1 ATOM 505 C C . HIS A 1 74 ? 19.078 -19.540 1.209 1.00 37.13 ? 72 HIS A C 1 ATOM 506 O O . HIS A 1 74 ? 18.770 -19.535 0.022 1.00 38.97 ? 72 HIS A O 1 ATOM 507 C CB . HIS A 1 74 ? 21.354 -18.854 1.867 1.00 40.03 ? 72 HIS A CB 1 ATOM 508 C CG . HIS A 1 74 ? 22.741 -19.227 2.287 1.00 44.16 ? 72 HIS A CG 1 ATOM 509 N ND1 . HIS A 1 74 ? 23.215 -19.008 3.564 1.00 49.51 ? 72 HIS A ND1 1 ATOM 510 C CD2 . HIS A 1 74 ? 23.765 -19.780 1.594 1.00 42.42 ? 72 HIS A CD2 1 ATOM 511 C CE1 . HIS A 1 74 ? 24.470 -19.414 3.640 1.00 49.46 ? 72 HIS A CE1 1 ATOM 512 N NE2 . HIS A 1 74 ? 24.826 -19.890 2.459 1.00 48.50 ? 72 HIS A NE2 1 ATOM 513 N N . LEU A 1 75 ? 18.267 -19.124 2.166 1.00 38.19 ? 73 LEU A N 1 ATOM 514 C CA . LEU A 1 75 ? 16.931 -18.634 1.868 1.00 38.98 ? 73 LEU A CA 1 ATOM 515 C C . LEU A 1 75 ? 16.962 -17.125 1.992 1.00 41.37 ? 73 LEU A C 1 ATOM 516 O O . LEU A 1 75 ? 16.882 -16.566 3.073 1.00 42.32 ? 73 LEU A O 1 ATOM 517 C CB . LEU A 1 75 ? 15.905 -19.271 2.806 1.00 40.25 ? 73 LEU A CB 1 ATOM 518 C CG . LEU A 1 75 ? 14.419 -19.093 2.489 1.00 44.87 ? 73 LEU A CG 1 ATOM 519 C CD1 . LEU A 1 75 ? 14.145 -19.143 0.992 1.00 46.94 ? 73 LEU A CD1 1 ATOM 520 C CD2 . LEU A 1 75 ? 13.601 -20.156 3.214 1.00 44.91 ? 73 LEU A CD2 1 ATOM 521 N N . VAL A 1 76 ? 17.107 -16.485 0.846 1.00 42.86 ? 74 VAL A N 1 ATOM 522 C CA . VAL A 1 76 ? 17.384 -15.056 0.769 1.00 45.42 ? 74 VAL A CA 1 ATOM 523 C C . VAL A 1 76 ? 16.118 -14.290 0.459 1.00 48.62 ? 74 VAL A C 1 ATOM 524 O O . VAL A 1 76 ? 16.114 -13.055 0.399 1.00 50.54 ? 74 VAL A O 1 ATOM 525 C CB . VAL A 1 76 ? 18.424 -14.761 -0.317 1.00 44.58 ? 74 VAL A CB 1 ATOM 526 C CG1 . VAL A 1 76 ? 19.782 -15.320 0.093 1.00 42.15 ? 74 VAL A CG1 1 ATOM 527 C CG2 . VAL A 1 76 ? 17.971 -15.343 -1.661 1.00 42.28 ? 74 VAL A CG2 1 ATOM 528 N N . GLY A 1 77 ? 15.038 -15.037 0.272 1.00 49.03 ? 75 GLY A N 1 ATOM 529 C CA . GLY A 1 77 ? 13.736 -14.429 0.028 1.00 52.61 ? 75 GLY A CA 1 ATOM 530 C C . GLY A 1 77 ? 13.197 -13.762 1.277 1.00 56.32 ? 75 GLY A C 1 ATOM 531 O O . GLY A 1 77 ? 13.371 -14.262 2.386 1.00 56.13 ? 75 GLY A O 1 ATOM 532 N N . ASP A 1 78 ? 12.546 -12.619 1.095 1.00 60.32 ? 76 ASP A N 1 ATOM 533 C CA . ASP A 1 78 ? 11.853 -11.951 2.207 1.00 65.10 ? 76 ASP A CA 1 ATOM 534 C C . ASP A 1 78 ? 10.559 -12.664 2.602 1.00 66.03 ? 76 ASP A C 1 ATOM 535 O O . ASP A 1 78 ? 9.559 -12.643 1.886 1.00 67.28 ? 76 ASP A O 1 ATOM 536 C CB . ASP A 1 78 ? 11.545 -10.492 1.891 1.00 68.95 ? 76 ASP A CB 1 ATOM 537 C CG . ASP A 1 78 ? 11.038 -9.750 3.101 1.00 76.33 ? 76 ASP A CG 1 ATOM 538 O OD1 . ASP A 1 78 ? 11.817 -9.611 4.069 1.00 80.21 ? 76 ASP A OD1 1 ATOM 539 O OD2 . ASP A 1 78 ? 9.864 -9.322 3.101 1.00 84.58 ? 76 ASP A OD2 1 ATOM 540 N N . THR A 1 79 ? 10.589 -13.273 3.772 1.00 66.10 ? 77 THR A N 1 ATOM 541 C CA . THR A 1 79 ? 9.506 -14.137 4.217 1.00 68.49 ? 77 THR A CA 1 ATOM 542 C C . THR A 1 79 ? 8.211 -13.383 4.508 1.00 73.80 ? 77 THR A C 1 ATOM 543 O O . THR A 1 79 ? 7.191 -13.997 4.828 1.00 74.75 ? 77 THR A O 1 ATOM 544 C CB . THR A 1 79 ? 9.922 -14.899 5.477 1.00 68.53 ? 77 THR A CB 1 ATOM 545 O OG1 . THR A 1 79 ? 11.288 -15.297 5.345 1.00 68.85 ? 77 THR A OG1 1 ATOM 546 C CG2 . THR A 1 79 ? 9.061 -16.130 5.685 1.00 69.36 ? 77 THR A CG2 1 ATOM 547 N N . PHE A 1 80 ? 8.248 -12.058 4.386 1.00 77.59 ? 78 PHE A N 1 ATOM 548 C CA . PHE A 1 80 ? 7.059 -11.231 4.625 1.00 83.09 ? 78 PHE A CA 1 ATOM 549 C C . PHE A 1 80 ? 6.406 -10.744 3.330 1.00 84.04 ? 78 PHE A C 1 ATOM 550 O O . PHE A 1 80 ? 5.199 -10.511 3.286 1.00 88.25 ? 78 PHE A O 1 ATOM 551 C CB . PHE A 1 80 ? 7.400 -10.033 5.512 1.00 87.58 ? 78 PHE A CB 1 ATOM 552 C CG . PHE A 1 80 ? 8.067 -10.404 6.807 1.00 92.13 ? 78 PHE A CG 1 ATOM 553 C CD1 . PHE A 1 80 ? 7.593 -11.462 7.576 1.00 94.91 ? 78 PHE A CD1 1 ATOM 554 C CD2 . PHE A 1 80 ? 9.161 -9.685 7.266 1.00 96.93 ? 78 PHE A CD2 1 ATOM 555 C CE1 . PHE A 1 80 ? 8.207 -11.803 8.769 1.00 95.07 ? 78 PHE A CE1 1 ATOM 556 C CE2 . PHE A 1 80 ? 9.779 -10.020 8.460 1.00 97.55 ? 78 PHE A CE2 1 ATOM 557 C CZ . PHE A 1 80 ? 9.301 -11.082 9.211 1.00 97.16 ? 78 PHE A CZ 1 ATOM 558 N N . HIS A 1 81 ? 7.206 -10.580 2.284 1.00 80.59 ? 79 HIS A N 1 ATOM 559 C CA . HIS A 1 81 ? 6.695 -10.114 1.000 1.00 81.66 ? 79 HIS A CA 1 ATOM 560 C C . HIS A 1 81 ? 6.687 -11.271 0.009 1.00 75.87 ? 79 HIS A C 1 ATOM 561 O O . HIS A 1 81 ? 7.270 -11.203 -1.077 1.00 74.11 ? 79 HIS A O 1 ATOM 562 C CB . HIS A 1 81 ? 7.508 -8.925 0.477 1.00 83.71 ? 79 HIS A CB 1 ATOM 563 C CG . HIS A 1 81 ? 6.961 -8.323 -0.784 1.00 90.18 ? 79 HIS A CG 1 ATOM 564 N ND1 . HIS A 1 81 ? 5.628 -8.007 -0.941 1.00 98.07 ? 79 HIS A ND1 1 ATOM 565 C CD2 . HIS A 1 81 ? 7.569 -7.968 -1.943 1.00 91.79 ? 79 HIS A CD2 1 ATOM 566 C CE1 . HIS A 1 81 ? 5.437 -7.489 -2.143 1.00 100.13 ? 79 HIS A CE1 1 ATOM 567 N NE2 . HIS A 1 81 ? 6.599 -7.454 -2.771 1.00 96.77 ? 79 HIS A NE2 1 ATOM 568 N N . ASN A 1 82 ? 6.035 -12.346 0.429 1.00 72.58 ? 80 ASN A N 1 ATOM 569 C CA . ASN A 1 82 ? 5.668 -13.443 -0.466 1.00 69.49 ? 80 ASN A CA 1 ATOM 570 C C . ASN A 1 82 ? 6.846 -14.137 -1.141 1.00 63.55 ? 80 ASN A C 1 ATOM 571 O O . ASN A 1 82 ? 6.681 -14.739 -2.197 1.00 61.18 ? 80 ASN A O 1 ATOM 572 C CB . ASN A 1 82 ? 4.752 -12.929 -1.579 1.00 72.80 ? 80 ASN A CB 1 ATOM 573 C CG . ASN A 1 82 ? 3.654 -12.028 -1.073 1.00 79.92 ? 80 ASN A CG 1 ATOM 574 O OD1 . ASN A 1 82 ? 3.779 -11.394 -0.026 1.00 85.96 ? 80 ASN A OD1 1 ATOM 575 N ND2 . ASN A 1 82 ? 2.569 -11.949 -1.830 1.00 84.49 ? 80 ASN A ND2 1 ATOM 576 N N . ASP A 1 83 ? 8.021 -14.068 -0.529 1.00 60.79 ? 81 ASP A N 1 ATOM 577 C CA . ASP A 1 83 ? 9.258 -14.425 -1.224 1.00 57.36 ? 81 ASP A CA 1 ATOM 578 C C . ASP A 1 83 ? 10.086 -15.537 -0.586 1.00 52.48 ? 81 ASP A C 1 ATOM 579 O O . ASP A 1 83 ? 10.607 -15.387 0.512 1.00 52.59 ? 81 ASP A O 1 ATOM 580 C CB . ASP A 1 83 ? 10.104 -13.161 -1.349 1.00 59.41 ? 81 ASP A CB 1 ATOM 581 C CG . ASP A 1 83 ? 11.280 -13.329 -2.288 1.00 59.53 ? 81 ASP A CG 1 ATOM 582 O OD1 . ASP A 1 83 ? 11.439 -14.420 -2.875 1.00 58.51 ? 81 ASP A OD1 1 ATOM 583 O OD2 . ASP A 1 83 ? 12.048 -12.353 -2.438 1.00 63.19 ? 81 ASP A OD2 1 ATOM 584 N N . GLY A 1 84 ? 10.226 -16.640 -1.313 1.00 48.53 ? 82 GLY A N 1 ATOM 585 C CA . GLY A 1 84 ? 11.003 -17.790 -0.845 1.00 45.89 ? 82 GLY A CA 1 ATOM 586 C C . GLY A 1 84 ? 12.221 -18.076 -1.711 1.00 43.16 ? 82 GLY A C 1 ATOM 587 O O . GLY A 1 84 ? 12.747 -19.196 -1.752 1.00 40.50 ? 82 GLY A O 1 ATOM 588 N N . SER A 1 85 ? 12.667 -17.043 -2.409 1.00 43.51 ? 83 SER A N 1 ATOM 589 C CA . SER A 1 85 ? 13.792 -17.169 -3.332 1.00 40.96 ? 83 SER A CA 1 ATOM 590 C C . SER A 1 85 ? 14.985 -17.816 -2.662 1.00 38.40 ? 83 SER A C 1 ATOM 591 O O . SER A 1 85 ? 15.263 -17.602 -1.477 1.00 38.03 ? 83 SER A O 1 ATOM 592 C CB . SER A 1 85 ? 14.198 -15.805 -3.895 1.00 42.49 ? 83 SER A CB 1 ATOM 593 O OG . SER A 1 85 ? 13.100 -15.149 -4.504 1.00 46.76 ? 83 SER A OG 1 ATOM 594 N N . LEU A 1 86 ? 15.694 -18.596 -3.467 1.00 36.30 ? 84 LEU A N 1 ATOM 595 C CA . LEU A 1 86 ? 16.880 -19.322 -3.031 1.00 35.38 ? 84 LEU A CA 1 ATOM 596 C C . LEU A 1 86 ? 18.177 -18.746 -3.581 1.00 34.89 ? 84 LEU A C 1 ATOM 597 O O . LEU A 1 86 ? 18.234 -18.282 -4.719 1.00 36.51 ? 84 LEU A O 1 ATOM 598 C CB . LEU A 1 86 ? 16.778 -20.765 -3.491 1.00 33.87 ? 84 LEU A CB 1 ATOM 599 C CG . LEU A 1 86 ? 17.934 -21.643 -3.037 1.00 32.08 ? 84 LEU A CG 1 ATOM 600 C CD1 . LEU A 1 86 ? 17.754 -22.018 -1.573 1.00 32.92 ? 84 LEU A CD1 1 ATOM 601 C CD2 . LEU A 1 86 ? 18.025 -22.880 -3.907 1.00 29.04 ? 84 LEU A CD2 1 ATOM 602 N N . LEU A 1 87 ? 19.223 -18.786 -2.766 1.00 33.42 ? 85 LEU A N 1 ATOM 603 C CA . LEU A 1 87 ? 20.561 -18.465 -3.243 1.00 32.34 ? 85 LEU A CA 1 ATOM 604 C C . LEU A 1 87 ? 21.429 -19.683 -3.117 1.00 32.30 ? 85 LEU A C 1 ATOM 605 O O . LEU A 1 87 ? 21.601 -20.222 -2.020 1.00 33.36 ? 85 LEU A O 1 ATOM 606 C CB . LEU A 1 87 ? 21.200 -17.319 -2.459 1.00 34.00 ? 85 LEU A CB 1 ATOM 607 C CG . LEU A 1 87 ? 22.583 -16.889 -2.981 1.00 30.47 ? 85 LEU A CG 1 ATOM 608 C CD1 . LEU A 1 87 ? 22.450 -15.865 -4.080 1.00 31.01 ? 85 LEU A CD1 1 ATOM 609 C CD2 . LEU A 1 87 ? 23.446 -16.328 -1.886 1.00 25.92 ? 85 LEU A CD2 1 ATOM 610 N N . LEU A 1 88 ? 21.980 -20.102 -4.248 1.00 31.30 ? 86 LEU A N 1 ATOM 611 C CA . LEU A 1 88 ? 22.901 -21.226 -4.287 1.00 31.11 ? 86 LEU A CA 1 ATOM 612 C C . LEU A 1 88 ? 24.310 -20.733 -4.584 1.00 32.48 ? 86 LEU A C 1 ATOM 613 O O . LEU A 1 88 ? 24.538 -19.973 -5.525 1.00 34.82 ? 86 LEU A O 1 ATOM 614 C CB . LEU A 1 88 ? 22.437 -22.240 -5.330 1.00 29.54 ? 86 LEU A CB 1 ATOM 615 C CG . LEU A 1 88 ? 23.174 -23.577 -5.350 1.00 31.65 ? 86 LEU A CG 1 ATOM 616 C CD1 . LEU A 1 88 ? 23.135 -24.244 -3.976 1.00 30.97 ? 86 LEU A CD1 1 ATOM 617 C CD2 . LEU A 1 88 ? 22.595 -24.501 -6.422 1.00 25.30 ? 86 LEU A CD2 1 ATOM 618 N N . GLN A 1 89 ? 25.252 -21.162 -3.760 1.00 33.25 ? 87 GLN A N 1 ATOM 619 C CA . GLN A 1 89 ? 26.630 -20.693 -3.861 1.00 34.84 ? 87 GLN A CA 1 ATOM 620 C C . GLN A 1 89 ? 27.607 -21.777 -4.227 1.00 35.96 ? 87 GLN A C 1 ATOM 621 O O . GLN A 1 89 ? 27.371 -22.956 -3.977 1.00 37.66 ? 87 GLN A O 1 ATOM 622 C CB . GLN A 1 89 ? 27.058 -20.092 -2.539 1.00 36.73 ? 87 GLN A CB 1 ATOM 623 C CG . GLN A 1 89 ? 26.484 -18.738 -2.326 1.00 39.31 ? 87 GLN A CG 1 ATOM 624 C CD . GLN A 1 89 ? 27.080 -18.074 -1.138 1.00 41.46 ? 87 GLN A CD 1 ATOM 625 O OE1 . GLN A 1 89 ? 26.926 -18.549 -0.021 1.00 40.98 ? 87 GLN A OE1 1 ATOM 626 N NE2 . GLN A 1 89 ? 27.778 -16.967 -1.363 1.00 47.60 ? 87 GLN A NE2 1 ATOM 627 N N . ASP A 1 90 ? 28.713 -21.356 -4.821 1.00 37.55 ? 88 ASP A N 1 ATOM 628 C CA . ASP A 1 90 ? 29.776 -22.257 -5.228 1.00 39.38 ? 88 ASP A CA 1 ATOM 629 C C . ASP A 1 90 ? 29.178 -23.389 -6.079 1.00 37.10 ? 88 ASP A C 1 ATOM 630 O O . ASP A 1 90 ? 29.260 -24.573 -5.754 1.00 38.20 ? 88 ASP A O 1 ATOM 631 C CB . ASP A 1 90 ? 30.536 -22.767 -3.996 1.00 41.70 ? 88 ASP A CB 1 ATOM 632 C CG . ASP A 1 90 ? 31.412 -21.668 -3.341 1.00 55.31 ? 88 ASP A CG 1 ATOM 633 O OD1 . ASP A 1 90 ? 32.173 -20.971 -4.068 1.00 70.08 ? 88 ASP A OD1 1 ATOM 634 O OD2 . ASP A 1 90 ? 31.359 -21.498 -2.097 1.00 60.43 ? 88 ASP A OD2 1 ATOM 635 N N . VAL A 1 91 ? 28.548 -22.993 -7.174 1.00 34.36 ? 89 VAL A N 1 ATOM 636 C CA . VAL A 1 91 ? 27.902 -23.946 -8.089 1.00 32.30 ? 89 VAL A CA 1 ATOM 637 C C . VAL A 1 91 ? 28.871 -24.891 -8.796 1.00 33.29 ? 89 VAL A C 1 ATOM 638 O O . VAL A 1 91 ? 29.912 -24.491 -9.299 1.00 33.00 ? 89 VAL A O 1 ATOM 639 C CB . VAL A 1 91 ? 27.061 -23.215 -9.171 1.00 31.22 ? 89 VAL A CB 1 ATOM 640 C CG1 . VAL A 1 91 ? 26.431 -24.220 -10.129 1.00 24.80 ? 89 VAL A CG1 1 ATOM 641 C CG2 . VAL A 1 91 ? 26.003 -22.338 -8.512 1.00 28.37 ? 89 VAL A CG2 1 ATOM 642 N N . GLN A 1 92 ? 28.472 -26.152 -8.851 1.00 34.56 ? 90 GLN A N 1 ATOM 643 C CA . GLN A 1 92 ? 29.253 -27.220 -9.481 1.00 37.48 ? 90 GLN A CA 1 ATOM 644 C C . GLN A 1 92 ? 28.522 -27.846 -10.659 1.00 37.13 ? 90 GLN A C 1 ATOM 645 O O . GLN A 1 92 ? 27.343 -27.608 -10.865 1.00 36.82 ? 90 GLN A O 1 ATOM 646 C CB . GLN A 1 92 ? 29.496 -28.314 -8.457 1.00 39.91 ? 90 GLN A CB 1 ATOM 647 C CG . GLN A 1 92 ? 30.003 -27.785 -7.130 1.00 44.51 ? 90 GLN A CG 1 ATOM 648 C CD . GLN A 1 92 ? 29.631 -28.670 -5.968 1.00 51.80 ? 90 GLN A CD 1 ATOM 649 O OE1 . GLN A 1 92 ? 29.954 -28.361 -4.812 1.00 62.69 ? 90 GLN A OE1 1 ATOM 650 N NE2 . GLN A 1 92 ? 28.947 -29.775 -6.256 1.00 43.23 ? 90 GLN A NE2 1 ATOM 651 N N . LYS A 1 93 ? 29.210 -28.699 -11.401 1.00 38.84 ? 91 LYS A N 1 ATOM 652 C CA . LYS A 1 93 ? 28.625 -29.281 -12.614 1.00 38.69 ? 91 LYS A CA 1 ATOM 653 C C . LYS A 1 93 ? 27.512 -30.235 -12.240 1.00 36.70 ? 91 LYS A C 1 ATOM 654 O O . LYS A 1 93 ? 26.541 -30.400 -12.974 1.00 36.32 ? 91 LYS A O 1 ATOM 655 C CB . LYS A 1 93 ? 29.676 -30.008 -13.448 1.00 41.28 ? 91 LYS A CB 1 ATOM 656 C CG . LYS A 1 93 ? 29.141 -30.553 -14.770 1.00 45.60 ? 91 LYS A CG 1 ATOM 657 C CD . LYS A 1 93 ? 28.602 -29.453 -15.697 1.00 46.57 ? 91 LYS A CD 1 ATOM 658 C CE . LYS A 1 93 ? 27.951 -30.058 -16.947 1.00 45.81 ? 91 LYS A CE 1 ATOM 659 N NZ . LYS A 1 93 ? 27.679 -29.064 -18.027 1.00 44.61 ? 91 LYS A NZ 1 ATOM 660 N N . ALA A 1 94 ? 27.662 -30.820 -11.059 1.00 36.17 ? 92 ALA A N 1 ATOM 661 C CA . ALA A 1 94 ? 26.695 -31.767 -10.497 1.00 32.70 ? 92 ALA A CA 1 ATOM 662 C C . ALA A 1 94 ? 25.433 -31.057 -10.037 1.00 32.46 ? 92 ALA A C 1 ATOM 663 O O . ALA A 1 94 ? 24.492 -31.705 -9.575 1.00 34.29 ? 92 ALA A O 1 ATOM 664 C CB . ALA A 1 94 ? 27.310 -32.505 -9.334 1.00 31.39 ? 92 ALA A CB 1 ATOM 665 N N . ASP A 1 95 ? 25.405 -29.731 -10.171 1.00 32.39 ? 93 ASP A N 1 ATOM 666 C CA . ASP A 1 95 ? 24.212 -28.942 -9.828 1.00 31.43 ? 93 ASP A CA 1 ATOM 667 C C . ASP A 1 95 ? 23.343 -28.708 -11.038 1.00 31.59 ? 93 ASP A C 1 ATOM 668 O O . ASP A 1 95 ? 22.316 -28.027 -10.957 1.00 31.87 ? 93 ASP A O 1 ATOM 669 C CB . ASP A 1 95 ? 24.580 -27.575 -9.277 1.00 31.63 ? 93 ASP A CB 1 ATOM 670 C CG . ASP A 1 95 ? 25.381 -27.651 -8.017 1.00 36.20 ? 93 ASP A CG 1 ATOM 671 O OD1 . ASP A 1 95 ? 25.445 -28.736 -7.397 1.00 40.75 ? 93 ASP A OD1 1 ATOM 672 O OD2 . ASP A 1 95 ? 25.944 -26.602 -7.650 1.00 38.98 ? 93 ASP A OD2 1 ATOM 673 N N . GLU A 1 96 ? 23.769 -29.254 -12.167 1.00 32.45 ? 94 GLU A N 1 ATOM 674 C CA . GLU A 1 96 ? 23.013 -29.108 -13.411 1.00 33.58 ? 94 GLU A CA 1 ATOM 675 C C . GLU A 1 96 ? 21.697 -29.888 -13.400 1.00 33.51 ? 94 GLU A C 1 ATOM 676 O O . GLU A 1 96 ? 21.662 -31.118 -13.379 1.00 32.81 ? 94 GLU A O 1 ATOM 677 C CB . GLU A 1 96 ? 23.858 -29.536 -14.611 1.00 35.83 ? 94 GLU A CB 1 ATOM 678 C CG . GLU A 1 96 ? 23.349 -28.980 -15.917 1.00 39.37 ? 94 GLU A CG 1 ATOM 679 C CD . GLU A 1 96 ? 24.359 -29.085 -17.030 1.00 47.64 ? 94 GLU A CD 1 ATOM 680 O OE1 . GLU A 1 96 ? 24.451 -30.158 -17.671 1.00 58.60 ? 94 GLU A OE1 1 ATOM 681 O OE2 . GLU A 1 96 ? 25.057 -28.081 -17.264 1.00 50.54 ? 94 GLU A OE2 1 ATOM 682 N N . GLY A 1 97 ? 20.607 -29.143 -13.425 1.00 33.63 ? 95 GLY A N 1 ATOM 683 C CA . GLY A 1 97 ? 19.284 -29.744 -13.579 1.00 34.15 ? 95 GLY A CA 1 ATOM 684 C C . GLY A 1 97 ? 18.156 -28.768 -13.344 1.00 33.50 ? 95 GLY A C 1 ATOM 685 O O . GLY A 1 97 ? 18.335 -27.548 -13.438 1.00 32.84 ? 95 GLY A O 1 ATOM 686 N N . ILE A 1 98 ? 16.989 -29.323 -13.033 1.00 34.29 ? 96 ILE A N 1 ATOM 687 C CA . ILE A 1 98 ? 15.809 -28.525 -12.710 1.00 33.65 ? 96 ILE A CA 1 ATOM 688 C C . ILE A 1 98 ? 15.688 -28.404 -11.207 1.00 31.95 ? 96 ILE A C 1 ATOM 689 O O . ILE A 1 98 ? 15.912 -29.368 -10.473 1.00 33.49 ? 96 ILE A O 1 ATOM 690 C CB . ILE A 1 98 ? 14.503 -29.125 -13.292 1.00 35.91 ? 96 ILE A CB 1 ATOM 691 C CG1 . ILE A 1 98 ? 14.693 -29.482 -14.767 1.00 39.69 ? 96 ILE A CG1 1 ATOM 692 C CG2 . ILE A 1 98 ? 13.336 -28.138 -13.131 1.00 33.03 ? 96 ILE A CG2 1 ATOM 693 C CD1 . ILE A 1 98 ? 13.402 -29.433 -15.596 1.00 47.83 ? 96 ILE A CD1 1 ATOM 694 N N . TYR A 1 99 ? 15.361 -27.191 -10.783 1.00 30.99 ? 97 TYR A N 1 ATOM 695 C CA . TYR A 1 99 ? 15.106 -26.849 -9.393 1.00 31.17 ? 97 TYR A CA 1 ATOM 696 C C . TYR A 1 99 ? 13.652 -26.433 -9.281 1.00 34.04 ? 97 TYR A C 1 ATOM 697 O O . TYR A 1 99 ? 13.163 -25.617 -10.061 1.00 36.42 ? 97 TYR A O 1 ATOM 698 C CB . TYR A 1 99 ? 16.017 -25.692 -8.951 1.00 30.23 ? 97 TYR A CB 1 ATOM 699 C CG . TYR A 1 99 ? 17.471 -26.092 -8.803 1.00 31.10 ? 97 TYR A CG 1 ATOM 700 C CD1 . TYR A 1 99 ? 18.271 -26.287 -9.919 1.00 26.57 ? 97 TYR A CD1 1 ATOM 701 C CD2 . TYR A 1 99 ? 18.041 -26.291 -7.547 1.00 30.20 ? 97 TYR A CD2 1 ATOM 702 C CE1 . TYR A 1 99 ? 19.588 -26.669 -9.796 1.00 27.20 ? 97 TYR A CE1 1 ATOM 703 C CE2 . TYR A 1 99 ? 19.361 -26.667 -7.418 1.00 26.89 ? 97 TYR A CE2 1 ATOM 704 C CZ . TYR A 1 99 ? 20.131 -26.855 -8.551 1.00 28.41 ? 97 TYR A CZ 1 ATOM 705 O OH . TYR A 1 99 ? 21.454 -27.240 -8.454 1.00 29.41 ? 97 TYR A OH 1 ATOM 706 N N . THR A 1 100 ? 12.950 -26.991 -8.309 1.00 35.03 ? 98 THR A N 1 ATOM 707 C CA . THR A 1 100 ? 11.538 -26.672 -8.155 1.00 37.48 ? 98 THR A CA 1 ATOM 708 C C . THR A 1 100 ? 11.194 -26.146 -6.779 1.00 38.77 ? 98 THR A C 1 ATOM 709 O O . THR A 1 100 ? 11.344 -26.832 -5.765 1.00 37.80 ? 98 THR A O 1 ATOM 710 C CB . THR A 1 100 ? 10.673 -27.886 -8.433 1.00 38.73 ? 98 THR A CB 1 ATOM 711 O OG1 . THR A 1 100 ? 11.201 -28.588 -9.562 1.00 37.94 ? 98 THR A OG1 1 ATOM 712 C CG2 . THR A 1 100 ? 9.264 -27.452 -8.703 1.00 37.91 ? 98 THR A CG2 1 ATOM 713 N N . CYS A 1 101 ? 10.723 -24.910 -6.780 1.00 40.89 ? 99 CYS A N 1 ATOM 714 C CA . CYS A 1 101 ? 10.224 -24.260 -5.581 1.00 43.02 ? 99 CYS A CA 1 ATOM 715 C C . CYS A 1 101 ? 8.778 -24.686 -5.353 1.00 45.12 ? 99 CYS A C 1 ATOM 716 O O . CYS A 1 101 ? 7.938 -24.542 -6.233 1.00 48.29 ? 99 CYS A O 1 ATOM 717 C CB . CYS A 1 101 ? 10.299 -22.746 -5.758 1.00 43.69 ? 99 CYS A CB 1 ATOM 718 S SG . CYS A 1 101 ? 9.899 -21.790 -4.296 1.00 53.45 ? 99 CYS A SG 1 ATOM 719 N N . GLU A 1 102 ? 8.500 -25.230 -4.178 1.00 43.58 ? 100 GLU A N 1 ATOM 720 C CA . GLU A 1 102 ? 7.128 -25.493 -3.753 1.00 45.62 ? 100 GLU A CA 1 ATOM 721 C C . GLU A 1 102 ? 6.835 -24.634 -2.545 1.00 45.85 ? 100 GLU A C 1 ATOM 722 O O . GLU A 1 102 ? 7.456 -24.813 -1.501 1.00 45.60 ? 100 GLU A O 1 ATOM 723 C CB . GLU A 1 102 ? 6.948 -26.952 -3.369 1.00 46.00 ? 100 GLU A CB 1 ATOM 724 C CG . GLU A 1 102 ? 7.279 -27.943 -4.467 1.00 50.76 ? 100 GLU A CG 1 ATOM 725 C CD . GLU A 1 102 ? 6.934 -29.375 -4.068 1.00 59.80 ? 100 GLU A CD 1 ATOM 726 O OE1 . GLU A 1 102 ? 6.406 -29.568 -2.950 1.00 61.56 ? 100 GLU A OE1 1 ATOM 727 O OE2 . GLU A 1 102 ? 7.191 -30.310 -4.868 1.00 66.47 ? 100 GLU A OE2 1 ATOM 728 N N . ILE A 1 103 ? 5.897 -23.703 -2.688 1.00 46.78 ? 101 ILE A N 1 ATOM 729 C CA . ILE A 1 103 ? 5.706 -22.651 -1.694 1.00 47.39 ? 101 ILE A CA 1 ATOM 730 C C . ILE A 1 103 ? 4.258 -22.429 -1.315 1.00 53.02 ? 101 ILE A C 1 ATOM 731 O O . ILE A 1 103 ? 3.363 -22.488 -2.162 1.00 56.29 ? 101 ILE A O 1 ATOM 732 C CB . ILE A 1 103 ? 6.289 -21.329 -2.198 1.00 47.09 ? 101 ILE A CB 1 ATOM 733 C CG1 . ILE A 1 103 ? 6.158 -20.239 -1.138 1.00 50.97 ? 101 ILE A CG1 1 ATOM 734 C CG2 . ILE A 1 103 ? 5.591 -20.881 -3.460 1.00 48.08 ? 101 ILE A CG2 1 ATOM 735 C CD1 . ILE A 1 103 ? 6.852 -18.943 -1.526 1.00 52.07 ? 101 ILE A CD1 1 ATOM 736 N N . ARG A 1 104 ? 4.039 -22.188 -0.024 1.00 54.64 ? 102 ARG A N 1 ATOM 737 C CA . ARG A 1 104 ? 2.703 -21.900 0.504 1.00 59.32 ? 102 ARG A CA 1 ATOM 738 C C . ARG A 1 104 ? 2.708 -20.723 1.454 1.00 61.85 ? 102 ARG A C 1 ATOM 739 O O . ARG A 1 104 ? 3.574 -20.599 2.308 1.00 61.20 ? 102 ARG A O 1 ATOM 740 C CB . ARG A 1 104 ? 2.105 -23.112 1.224 1.00 60.44 ? 102 ARG A CB 1 ATOM 741 C CG . ARG A 1 104 ? 0.683 -22.845 1.759 1.00 67.06 ? 102 ARG A CG 1 ATOM 742 C CD . ARG A 1 104 ? -0.022 -24.104 2.259 1.00 68.74 ? 102 ARG A CD 1 ATOM 743 N NE . ARG A 1 104 ? 0.512 -24.552 3.542 1.00 68.36 ? 102 ARG A NE 1 ATOM 744 C CZ . ARG A 1 104 ? 0.267 -23.957 4.705 1.00 69.38 ? 102 ARG A CZ 1 ATOM 745 N NH1 . ARG A 1 104 ? -0.496 -22.873 4.769 1.00 74.15 ? 102 ARG A NH1 1 ATOM 746 N NH2 . ARG A 1 104 ? 0.806 -24.442 5.811 1.00 68.64 ? 102 ARG A NH2 1 ATOM 747 N N . LEU A 1 105 ? 1.704 -19.873 1.304 1.00 66.90 ? 103 LEU A N 1 ATOM 748 C CA . LEU A 1 105 ? 1.572 -18.672 2.120 1.00 69.92 ? 103 LEU A CA 1 ATOM 749 C C . LEU A 1 105 ? 0.646 -18.926 3.301 1.00 73.79 ? 103 LEU A C 1 ATOM 750 O O . LEU A 1 105 ? -0.220 -19.804 3.257 1.00 74.86 ? 103 LEU A O 1 ATOM 751 C CB . LEU A 1 105 ? 1.063 -17.510 1.266 1.00 72.71 ? 103 LEU A CB 1 ATOM 752 C CG . LEU A 1 105 ? 1.895 -17.261 0.005 1.00 70.16 ? 103 LEU A CG 1 ATOM 753 C CD1 . LEU A 1 105 ? 1.528 -15.943 -0.659 1.00 72.78 ? 103 LEU A CD1 1 ATOM 754 C CD2 . LEU A 1 105 ? 3.380 -17.288 0.333 1.00 64.69 ? 103 LEU A CD2 1 ATOM 755 N N . LYS A 1 106 ? 0.852 -18.157 4.362 1.00 75.85 ? 104 LYS A N 1 ATOM 756 C CA . LYS A 1 106 ? 0.079 -18.331 5.597 1.00 81.41 ? 104 LYS A CA 1 ATOM 757 C C . LYS A 1 106 ? -1.392 -17.996 5.389 1.00 86.92 ? 104 LYS A C 1 ATOM 758 O O . LYS A 1 106 ? -1.758 -17.241 4.487 1.00 88.93 ? 104 LYS A O 1 ATOM 759 C CB . LYS A 1 106 ? 0.658 -17.494 6.749 1.00 83.13 ? 104 LYS A CB 1 ATOM 760 C CG . LYS A 1 106 ? 0.294 -16.010 6.716 1.00 89.88 ? 104 LYS A CG 1 ATOM 761 C CD . LYS A 1 106 ? 0.537 -15.354 8.071 1.00 94.93 ? 104 LYS A CD 1 ATOM 762 C CE . LYS A 1 106 ? 0.032 -13.912 8.114 1.00 101.70 ? 104 LYS A CE 1 ATOM 763 N NZ . LYS A 1 106 ? 0.858 -12.972 7.300 1.00 99.59 ? 104 LYS A NZ 1 ATOM 764 N N . ASN A 1 107 ? -2.232 -18.580 6.232 1.00 89.95 ? 105 ASN A N 1 ATOM 765 C CA . ASN A 1 107 ? -3.668 -18.343 6.157 1.00 95.88 ? 105 ASN A CA 1 ATOM 766 C C . ASN A 1 107 ? -4.145 -18.646 4.734 1.00 95.69 ? 105 ASN A C 1 ATOM 767 O O . ASN A 1 107 ? -5.054 -18.002 4.219 1.00 100.39 ? 105 ASN A O 1 ATOM 768 C CB . ASN A 1 107 ? -3.980 -16.893 6.548 1.00 100.40 ? 105 ASN A CB 1 ATOM 769 C CG . ASN A 1 107 ? -4.629 -16.769 7.918 1.00 105.56 ? 105 ASN A CG 1 ATOM 770 O OD1 . ASN A 1 107 ? -4.154 -16.031 8.781 1.00 104.82 ? 105 ASN A OD1 1 ATOM 771 N ND2 . ASN A 1 107 ? -5.722 -17.492 8.120 1.00 112.06 ? 105 ASN A ND2 1 ATOM 772 N N . GLU A 1 108 ? -3.508 -19.635 4.110 1.00 90.90 ? 106 GLU A N 1 ATOM 773 C CA . GLU A 1 108 ? -3.773 -19.988 2.707 1.00 90.29 ? 106 GLU A CA 1 ATOM 774 C C . GLU A 1 108 ? -3.368 -21.435 2.400 1.00 85.54 ? 106 GLU A C 1 ATOM 775 O O . GLU A 1 108 ? -2.262 -21.861 2.734 1.00 81.65 ? 106 GLU A O 1 ATOM 776 C CB . GLU A 1 108 ? -3.035 -18.998 1.800 1.00 88.63 ? 106 GLU A CB 1 ATOM 777 C CG . GLU A 1 108 ? -3.099 -19.297 0.310 1.00 91.60 ? 106 GLU A CG 1 ATOM 778 C CD . GLU A 1 108 ? -2.643 -18.121 -0.553 1.00 95.99 ? 106 GLU A CD 1 ATOM 779 O OE1 . GLU A 1 108 ? -3.057 -16.970 -0.276 1.00 103.47 ? 106 GLU A OE1 1 ATOM 780 O OE2 . GLU A 1 108 ? -1.882 -18.349 -1.519 1.00 89.81 ? 106 GLU A OE2 1 ATOM 781 N N . SER A 1 109 ? -4.277 -22.181 1.777 1.00 86.73 ? 107 SER A N 1 ATOM 782 C CA . SER A 1 109 ? -4.125 -23.638 1.625 1.00 84.02 ? 107 SER A CA 1 ATOM 783 C C . SER A 1 109 ? -3.626 -24.043 0.248 1.00 81.32 ? 107 SER A C 1 ATOM 784 O O . SER A 1 109 ? -3.634 -25.226 -0.107 1.00 80.76 ? 107 SER A O 1 ATOM 785 C CB . SER A 1 109 ? -5.455 -24.348 1.874 1.00 89.31 ? 107 SER A CB 1 ATOM 786 O OG . SER A 1 109 ? -6.210 -24.434 0.677 1.00 91.63 ? 107 SER A OG 1 ATOM 787 N N . MET A 1 110 ? -3.194 -23.049 -0.517 1.00 79.73 ? 108 MET A N 1 ATOM 788 C CA . MET A 1 110 ? -2.714 -23.258 -1.890 1.00 76.95 ? 108 MET A CA 1 ATOM 789 C C . MET A 1 110 ? -1.192 -23.310 -1.902 1.00 68.61 ? 108 MET A C 1 ATOM 790 O O . MET A 1 110 ? -0.529 -22.437 -1.345 1.00 63.46 ? 108 MET A O 1 ATOM 791 C CB . MET A 1 110 ? -3.206 -22.128 -2.803 1.00 80.68 ? 108 MET A CB 1 ATOM 792 C CG . MET A 1 110 ? -3.807 -22.587 -4.134 1.00 87.36 ? 108 MET A CG 1 ATOM 793 S SD . MET A 1 110 ? -5.475 -23.315 -4.035 1.00 103.54 ? 108 MET A SD 1 ATOM 794 C CE . MET A 1 110 ? -6.308 -22.215 -2.889 1.00 105.83 ? 108 MET A CE 1 ATOM 795 N N . VAL A 1 111 ? -0.661 -24.352 -2.533 1.00 65.76 ? 109 VAL A N 1 ATOM 796 C CA . VAL A 1 111 ? 0.789 -24.527 -2.684 1.00 61.58 ? 109 VAL A CA 1 ATOM 797 C C . VAL A 1 111 ? 1.214 -24.326 -4.123 1.00 61.33 ? 109 VAL A C 1 ATOM 798 O O . VAL A 1 111 ? 0.641 -24.921 -5.023 1.00 65.67 ? 109 VAL A O 1 ATOM 799 C CB . VAL A 1 111 ? 1.242 -25.936 -2.277 1.00 59.70 ? 109 VAL A CB 1 ATOM 800 C CG1 . VAL A 1 111 ? 2.753 -25.985 -2.180 1.00 50.41 ? 109 VAL A CG1 1 ATOM 801 C CG2 . VAL A 1 111 ? 0.603 -26.353 -0.965 1.00 61.15 ? 109 VAL A CG2 1 ATOM 802 N N . MET A 1 112 ? 2.235 -23.504 -4.327 1.00 58.67 ? 110 MET A N 1 ATOM 803 C CA . MET A 1 112 ? 2.657 -23.089 -5.675 1.00 58.97 ? 110 MET A CA 1 ATOM 804 C C . MET A 1 112 ? 3.917 -23.794 -6.157 1.00 53.94 ? 110 MET A C 1 ATOM 805 O O . MET A 1 112 ? 4.900 -23.887 -5.448 1.00 50.89 ? 110 MET A O 1 ATOM 806 C CB . MET A 1 112 ? 2.891 -21.580 -5.707 1.00 60.44 ? 110 MET A CB 1 ATOM 807 C CG . MET A 1 112 ? 1.681 -20.748 -5.300 1.00 71.86 ? 110 MET A CG 1 ATOM 808 S SD . MET A 1 112 ? 0.565 -20.385 -6.673 1.00 85.97 ? 110 MET A SD 1 ATOM 809 C CE . MET A 1 112 ? 1.623 -19.349 -7.702 1.00 84.83 ? 110 MET A CE 1 ATOM 810 N N . LYS A 1 113 ? 3.878 -24.244 -7.400 1.00 54.99 ? 111 LYS A N 1 ATOM 811 C CA . LYS A 1 113 ? 4.951 -25.043 -8.006 1.00 52.68 ? 111 LYS A CA 1 ATOM 812 C C . LYS A 1 113 ? 5.641 -24.302 -9.166 1.00 51.91 ? 111 LYS A C 1 ATOM 813 O O . LYS A 1 113 ? 5.146 -24.265 -10.301 1.00 53.00 ? 111 LYS A O 1 ATOM 814 C CB . LYS A 1 113 ? 4.363 -26.363 -8.518 1.00 55.99 ? 111 LYS A CB 1 ATOM 815 C CG . LYS A 1 113 ? 4.859 -27.626 -7.861 1.00 58.43 ? 111 LYS A CG 1 ATOM 816 C CD . LYS A 1 113 ? 3.655 -28.538 -7.598 1.00 67.93 ? 111 LYS A CD 1 ATOM 817 C CE . LYS A 1 113 ? 3.976 -30.025 -7.737 1.00 71.15 ? 111 LYS A CE 1 ATOM 818 N NZ . LYS A 1 113 ? 2.740 -30.871 -7.593 1.00 73.93 ? 111 LYS A NZ 1 ATOM 819 N N . LYS A 1 114 ? 6.805 -23.740 -8.870 1.00 48.82 ? 112 LYS A N 1 ATOM 820 C CA . LYS A 1 114 ? 7.570 -22.960 -9.836 1.00 47.45 ? 112 LYS A CA 1 ATOM 821 C C . LYS A 1 114 ? 8.926 -23.602 -10.097 1.00 43.88 ? 112 LYS A C 1 ATOM 822 O O . LYS A 1 114 ? 9.742 -23.738 -9.182 1.00 41.23 ? 112 LYS A O 1 ATOM 823 C CB . LYS A 1 114 ? 7.784 -21.553 -9.303 1.00 47.02 ? 112 LYS A CB 1 ATOM 824 C CG . LYS A 1 114 ? 6.523 -20.914 -8.757 1.00 53.47 ? 112 LYS A CG 1 ATOM 825 C CD . LYS A 1 114 ? 6.837 -19.579 -8.116 1.00 59.91 ? 112 LYS A CD 1 ATOM 826 C CE . LYS A 1 114 ? 5.592 -18.758 -7.881 1.00 68.85 ? 112 LYS A CE 1 ATOM 827 N NZ . LYS A 1 114 ? 5.933 -17.465 -7.221 1.00 71.97 ? 112 LYS A NZ 1 ATOM 828 N N . PRO A 1 115 ? 9.169 -24.016 -11.346 1.00 43.62 ? 113 PRO A N 1 ATOM 829 C CA . PRO A 1 115 ? 10.447 -24.617 -11.692 1.00 40.58 ? 113 PRO A CA 1 ATOM 830 C C . PRO A 1 115 ? 11.408 -23.652 -12.352 1.00 39.73 ? 113 PRO A C 1 ATOM 831 O O . PRO A 1 115 ? 10.993 -22.676 -12.979 1.00 40.80 ? 113 PRO A O 1 ATOM 832 C CB . PRO A 1 115 ? 10.047 -25.687 -12.695 1.00 41.70 ? 113 PRO A CB 1 ATOM 833 C CG . PRO A 1 115 ? 8.881 -25.094 -13.401 1.00 45.10 ? 113 PRO A CG 1 ATOM 834 C CD . PRO A 1 115 ? 8.197 -24.155 -12.440 1.00 46.35 ? 113 PRO A CD 1 ATOM 835 N N . VAL A 1 116 ? 12.691 -23.949 -12.195 1.00 37.63 ? 114 VAL A N 1 ATOM 836 C CA . VAL A 1 116 ? 13.760 -23.191 -12.850 1.00 37.81 ? 114 VAL A CA 1 ATOM 837 C C . VAL A 1 116 ? 14.892 -24.110 -13.297 1.00 36.40 ? 114 VAL A C 1 ATOM 838 O O . VAL A 1 116 ? 15.355 -24.953 -12.539 1.00 35.87 ? 114 VAL A O 1 ATOM 839 C CB . VAL A 1 116 ? 14.333 -22.122 -11.932 1.00 35.88 ? 114 VAL A CB 1 ATOM 840 C CG1 . VAL A 1 116 ? 14.896 -22.755 -10.692 1.00 34.48 ? 114 VAL A CG1 1 ATOM 841 C CG2 . VAL A 1 116 ? 15.411 -21.334 -12.665 1.00 40.90 ? 114 VAL A CG2 1 ATOM 842 N N . GLU A 1 117 ? 15.321 -23.952 -14.543 1.00 36.52 ? 115 GLU A N 1 ATOM 843 C CA . GLU A 1 117 ? 16.354 -24.824 -15.100 1.00 35.86 ? 115 GLU A CA 1 ATOM 844 C C . GLU A 1 117 ? 17.719 -24.179 -14.962 1.00 33.21 ? 115 GLU A C 1 ATOM 845 O O . GLU A 1 117 ? 17.886 -22.991 -15.214 1.00 32.86 ? 115 GLU A O 1 ATOM 846 C CB . GLU A 1 117 ? 16.061 -25.151 -16.560 1.00 39.12 ? 115 GLU A CB 1 ATOM 847 C CG . GLU A 1 117 ? 16.873 -26.311 -17.114 1.00 43.04 ? 115 GLU A CG 1 ATOM 848 C CD . GLU A 1 117 ? 16.304 -26.850 -18.425 1.00 55.87 ? 115 GLU A CD 1 ATOM 849 O OE1 . GLU A 1 117 ? 15.744 -26.056 -19.220 1.00 57.57 ? 115 GLU A OE1 1 ATOM 850 O OE2 . GLU A 1 117 ? 16.413 -28.076 -18.659 1.00 63.43 ? 115 GLU A OE2 1 ATOM 851 N N . LEU A 1 118 ? 18.690 -24.974 -14.536 1.00 31.41 ? 116 LEU A N 1 ATOM 852 C CA . LEU A 1 118 ? 20.036 -24.471 -14.297 1.00 31.09 ? 116 LEU A CA 1 ATOM 853 C C . LEU A 1 118 ? 21.061 -25.208 -15.129 1.00 31.66 ? 116 LEU A C 1 ATOM 854 O O . LEU A 1 118 ? 21.238 -26.417 -15.001 1.00 32.59 ? 116 LEU A O 1 ATOM 855 C CB . LEU A 1 118 ? 20.400 -24.593 -12.813 1.00 29.92 ? 116 LEU A CB 1 ATOM 856 C CG . LEU A 1 118 ? 21.729 -23.955 -12.392 1.00 26.70 ? 116 LEU A CG 1 ATOM 857 C CD1 . LEU A 1 118 ? 21.605 -22.473 -12.451 1.00 35.25 ? 116 LEU A CD1 1 ATOM 858 C CD2 . LEU A 1 118 ? 22.142 -24.383 -10.998 1.00 19.06 ? 116 LEU A CD2 1 ATOM 859 N N . TRP A 1 119 ? 21.735 -24.438 -15.970 1.00 31.20 ? 117 TRP A N 1 ATOM 860 C CA . TRP A 1 119 ? 22.835 -24.919 -16.787 1.00 32.15 ? 117 TRP A CA 1 ATOM 861 C C . TRP A 1 119 ? 24.158 -24.448 -16.226 1.00 31.52 ? 117 TRP A C 1 ATOM 862 O O . TRP A 1 119 ? 24.313 -23.301 -15.833 1.00 32.10 ? 117 TRP A O 1 ATOM 863 C CB . TRP A 1 119 ? 22.690 -24.379 -18.203 1.00 35.65 ? 117 TRP A CB 1 ATOM 864 C CG . TRP A 1 119 ? 21.460 -24.849 -18.860 1.00 37.07 ? 117 TRP A CG 1 ATOM 865 C CD1 . TRP A 1 119 ? 20.322 -24.132 -19.103 1.00 37.23 ? 117 TRP A CD1 1 ATOM 866 C CD2 . TRP A 1 119 ? 21.226 -26.161 -19.354 1.00 35.54 ? 117 TRP A CD2 1 ATOM 867 N NE1 . TRP A 1 119 ? 19.396 -24.923 -19.729 1.00 38.24 ? 117 TRP A NE1 1 ATOM 868 C CE2 . TRP A 1 119 ? 19.925 -26.176 -19.896 1.00 38.30 ? 117 TRP A CE2 1 ATOM 869 C CE3 . TRP A 1 119 ? 21.995 -27.327 -19.400 1.00 30.21 ? 117 TRP A CE3 1 ATOM 870 C CZ2 . TRP A 1 119 ? 19.381 -27.306 -20.483 1.00 38.02 ? 117 TRP A CZ2 1 ATOM 871 C CZ3 . TRP A 1 119 ? 21.457 -28.437 -19.973 1.00 39.08 ? 117 TRP A CZ3 1 ATOM 872 C CH2 . TRP A 1 119 ? 20.155 -28.425 -20.511 1.00 40.69 ? 117 TRP A CH2 1 ATOM 873 N N . VAL A 1 120 ? 25.128 -25.338 -16.213 1.00 31.53 ? 118 VAL A N 1 ATOM 874 C CA . VAL A 1 120 ? 26.413 -25.008 -15.643 1.00 31.01 ? 118 VAL A CA 1 ATOM 875 C C . VAL A 1 120 ? 27.491 -25.048 -16.689 1.00 33.37 ? 118 VAL A C 1 ATOM 876 O O . VAL A 1 120 ? 27.712 -26.081 -17.331 1.00 33.69 ? 118 VAL A O 1 ATOM 877 C CB . VAL A 1 120 ? 26.747 -25.960 -14.518 1.00 30.78 ? 118 VAL A CB 1 ATOM 878 C CG1 . VAL A 1 120 ? 28.206 -25.776 -14.073 1.00 32.32 ? 118 VAL A CG1 1 ATOM 879 C CG2 . VAL A 1 120 ? 25.769 -25.720 -13.374 1.00 26.60 ? 118 VAL A CG2 1 ATOM 880 N N . LEU A 1 121 ? 28.141 -23.899 -16.851 1.00 34.65 ? 119 LEU A N 1 ATOM 881 C CA . LEU A 1 121 ? 29.209 -23.723 -17.824 1.00 39.31 ? 119 LEU A CA 1 ATOM 882 C C . LEU A 1 121 ? 30.562 -23.963 -17.168 1.00 40.88 ? 119 LEU A C 1 ATOM 883 O O . LEU A 1 121 ? 30.696 -23.822 -15.966 1.00 40.07 ? 119 LEU A O 1 ATOM 884 C CB . LEU A 1 121 ? 29.171 -22.302 -18.401 1.00 41.83 ? 119 LEU A CB 1 ATOM 885 C CG . LEU A 1 121 ? 27.827 -21.779 -18.925 1.00 43.55 ? 119 LEU A CG 1 ATOM 886 C CD1 . LEU A 1 121 ? 28.031 -20.501 -19.750 1.00 34.59 ? 119 LEU A CD1 1 ATOM 887 C CD2 . LEU A 1 121 ? 27.123 -22.845 -19.741 1.00 36.69 ? 119 LEU A CD2 1 ATOM 888 N N . PRO A 1 122 ? 31.582 -24.305 -17.961 1.00 44.82 ? 120 PRO A N 1 ATOM 889 C CA . PRO A 1 122 ? 32.907 -24.498 -17.382 1.00 48.18 ? 120 PRO A CA 1 ATOM 890 C C . PRO A 1 122 ? 33.432 -23.260 -16.695 1.00 51.03 ? 120 PRO A C 1 ATOM 891 O O . PRO A 1 122 ? 33.033 -22.146 -17.023 1.00 52.08 ? 120 PRO A O 1 ATOM 892 C CB . PRO A 1 122 ? 33.781 -24.807 -18.592 1.00 51.08 ? 120 PRO A CB 1 ATOM 893 C CG . PRO A 1 122 ? 32.837 -25.154 -19.695 1.00 50.57 ? 120 PRO A CG 1 ATOM 894 C CD . PRO A 1 122 ? 31.602 -24.386 -19.428 1.00 46.31 ? 120 PRO A CD 1 ATOM 895 N N . GLU A 1 123 ? 34.335 -23.480 -15.751 1.00 54.72 ? 121 GLU A N 1 ATOM 896 C CA . GLU A 1 123 ? 34.942 -22.390 -14.966 1.00 57.77 ? 121 GLU A CA 1 ATOM 897 C C . GLU A 1 123 ? 35.591 -21.346 -15.851 1.00 60.17 ? 121 GLU A C 1 ATOM 898 O O . GLU A 1 123 ? 36.195 -21.670 -16.863 1.00 63.09 ? 121 GLU A O 1 ATOM 899 C CB . GLU A 1 123 ? 36.003 -22.941 -13.998 1.00 60.35 ? 121 GLU A CB 1 ATOM 900 C CG . GLU A 1 123 ? 36.407 -21.988 -12.873 1.00 64.87 ? 121 GLU A CG 1 ATOM 901 C CD . GLU A 1 123 ? 37.596 -22.491 -12.058 1.00 72.45 ? 121 GLU A CD 1 ATOM 902 O OE1 . GLU A 1 123 ? 38.036 -23.641 -12.277 1.00 73.09 ? 121 GLU A OE1 1 ATOM 903 O OE2 . GLU A 1 123 ? 38.092 -21.729 -11.196 1.00 77.11 ? 121 GLU A OE2 1 ATOM 904 N N . GLU A 1 124 ? 35.459 -20.087 -15.453 1.00 55.71 ? 122 GLU A N 1 ATOM 905 C CA . GLU A 1 124 ? 36.233 -18.992 -16.072 1.00 55.86 ? 122 GLU A CA 1 ATOM 906 C C . GLU A 1 124 ? 37.710 -19.077 -15.661 1.00 54.95 ? 122 GLU A C 1 ATOM 907 O O . GLU A 1 124 ? 38.012 -19.359 -14.506 1.00 55.39 ? 122 GLU A O 1 ATOM 908 C CB . GLU A 1 124 ? 35.677 -17.609 -15.687 1.00 54.23 ? 122 GLU A CB 1 ATOM 909 C CG . GLU A 1 124 ? 34.368 -17.253 -16.378 1.00 58.11 ? 122 GLU A CG 1 ATOM 910 C CD . GLU A 1 124 ? 34.187 -15.750 -16.554 1.00 63.75 ? 122 GLU A CD 1 ATOM 911 O OE1 . GLU A 1 124 ? 34.481 -14.998 -15.593 1.00 65.02 ? 122 GLU A OE1 1 ATOM 912 O OE2 . GLU A 1 124 ? 33.751 -15.322 -17.653 1.00 64.15 ? 122 GLU A OE2 1 ATOM 913 N N . PRO A 1 125 ? 38.635 -18.824 -16.602 1.00 54.26 ? 123 PRO A N 1 ATOM 914 C CA . PRO A 1 125 ? 40.052 -18.907 -16.246 1.00 54.27 ? 123 PRO A CA 1 ATOM 915 C C . PRO A 1 125 ? 40.443 -17.812 -15.277 1.00 51.46 ? 123 PRO A C 1 ATOM 916 O O . PRO A 1 125 ? 39.868 -16.730 -15.290 1.00 50.01 ? 123 PRO A O 1 ATOM 917 C CB . PRO A 1 125 ? 40.764 -18.716 -17.586 1.00 54.81 ? 123 PRO A CB 1 ATOM 918 C CG . PRO A 1 125 ? 39.826 -17.885 -18.384 1.00 52.99 ? 123 PRO A CG 1 ATOM 919 C CD . PRO A 1 125 ? 38.439 -18.281 -17.961 1.00 54.07 ? 123 PRO A CD 1 ATOM 920 N N . ARG A 1 126 ? 41.414 -18.104 -14.430 1.00 52.19 ? 124 ARG A N 1 ATOM 921 C CA . ARG A 1 126 ? 41.786 -17.165 -13.379 1.00 51.21 ? 124 ARG A CA 1 ATOM 922 C C . ARG A 1 126 ? 42.774 -16.167 -13.951 1.00 49.67 ? 124 ARG A C 1 ATOM 923 O O . ARG A 1 126 ? 42.856 -15.024 -13.510 1.00 47.03 ? 124 ARG A O 1 ATOM 924 C CB . ARG A 1 126 ? 42.358 -17.880 -12.153 1.00 54.60 ? 124 ARG A CB 1 ATOM 925 C CG . ARG A 1 126 ? 41.604 -17.489 -10.891 1.00 58.99 ? 124 ARG A CG 1 ATOM 926 C CD . ARG A 1 126 ? 42.149 -18.143 -9.630 1.00 66.96 ? 124 ARG A CD 1 ATOM 927 N NE . ARG A 1 126 ? 43.290 -17.411 -9.077 1.00 70.82 ? 124 ARG A NE 1 ATOM 928 C CZ . ARG A 1 126 ? 44.562 -17.769 -9.234 1.00 77.07 ? 124 ARG A CZ 1 ATOM 929 N NH1 . ARG A 1 126 ? 44.878 -18.856 -9.932 1.00 80.85 ? 124 ARG A NH1 1 ATOM 930 N NH2 . ARG A 1 126 ? 45.523 -17.042 -8.683 1.00 79.21 ? 124 ARG A NH2 1 ATOM 931 N N . ASP A 1 127 ? 43.491 -16.618 -14.970 1.00 50.44 ? 125 ASP A N 1 ATOM 932 C CA . ASP A 1 127 ? 44.506 -15.813 -15.626 1.00 51.21 ? 125 ASP A CA 1 ATOM 933 C C . ASP A 1 127 ? 43.895 -15.042 -16.779 1.00 48.44 ? 125 ASP A C 1 ATOM 934 O O . ASP A 1 127 ? 43.097 -15.558 -17.552 1.00 48.50 ? 125 ASP A O 1 ATOM 935 C CB . ASP A 1 127 ? 45.663 -16.687 -16.123 1.00 55.28 ? 125 ASP A CB 1 ATOM 936 C CG . ASP A 1 127 ? 46.481 -17.272 -14.982 1.00 62.18 ? 125 ASP A CG 1 ATOM 937 O OD1 . ASP A 1 127 ? 47.103 -16.481 -14.237 1.00 65.37 ? 125 ASP A OD1 1 ATOM 938 O OD2 . ASP A 1 127 ? 46.508 -18.518 -14.830 1.00 65.49 ? 125 ASP A OD2 1 ATOM 939 N N . LEU A 1 128 ? 44.295 -13.786 -16.865 1.00 46.68 ? 126 LEU A N 1 ATOM 940 C CA . LEU A 1 128 ? 43.845 -12.876 -17.899 1.00 43.26 ? 126 LEU A CA 1 ATOM 941 C C . LEU A 1 128 ? 45.070 -12.149 -18.463 1.00 43.73 ? 126 LEU A C 1 ATOM 942 O O . LEU A 1 128 ? 45.903 -11.652 -17.717 1.00 45.16 ? 126 LEU A O 1 ATOM 943 C CB . LEU A 1 128 ? 42.850 -11.905 -17.271 1.00 40.89 ? 126 LEU A CB 1 ATOM 944 C CG . LEU A 1 128 ? 42.132 -10.908 -18.167 1.00 40.98 ? 126 LEU A CG 1 ATOM 945 C CD1 . LEU A 1 128 ? 41.187 -11.611 -19.115 1.00 39.30 ? 126 LEU A CD1 1 ATOM 946 C CD2 . LEU A 1 128 ? 41.369 -9.928 -17.299 1.00 40.07 ? 126 LEU A CD2 1 ATOM 947 N N . ARG A 1 129 ? 45.209 -12.138 -19.779 1.00 43.78 ? 127 ARG A N 1 ATOM 948 C CA . ARG A 1 129 ? 46.378 -11.528 -20.411 1.00 46.08 ? 127 ARG A CA 1 ATOM 949 C C . ARG A 1 129 ? 45.967 -10.374 -21.292 1.00 45.62 ? 127 ARG A C 1 ATOM 950 O O . ARG A 1 129 ? 45.198 -10.535 -22.231 1.00 45.42 ? 127 ARG A O 1 ATOM 951 C CB . ARG A 1 129 ? 47.147 -12.538 -21.259 1.00 48.09 ? 127 ARG A CB 1 ATOM 952 C CG . ARG A 1 129 ? 47.188 -13.938 -20.699 1.00 54.83 ? 127 ARG A CG 1 ATOM 953 C CD . ARG A 1 129 ? 48.328 -14.179 -19.729 1.00 62.08 ? 127 ARG A CD 1 ATOM 954 N NE . ARG A 1 129 ? 48.210 -15.514 -19.128 1.00 69.65 ? 127 ARG A NE 1 ATOM 955 C CZ . ARG A 1 129 ? 49.172 -16.143 -18.455 1.00 71.02 ? 127 ARG A CZ 1 ATOM 956 N NH1 . ARG A 1 129 ? 50.364 -15.581 -18.282 1.00 72.12 ? 127 ARG A NH1 1 ATOM 957 N NH2 . ARG A 1 129 ? 48.936 -17.349 -17.957 1.00 74.25 ? 127 ARG A NH2 1 ATOM 958 N N . VAL A 1 130 ? 46.493 -9.201 -20.978 1.00 46.16 ? 128 VAL A N 1 ATOM 959 C CA . VAL A 1 130 ? 46.179 -8.010 -21.745 1.00 46.16 ? 128 VAL A CA 1 ATOM 960 C C . VAL A 1 130 ? 47.437 -7.209 -22.055 1.00 48.61 ? 128 VAL A C 1 ATOM 961 O O . VAL A 1 130 ? 48.440 -7.282 -21.352 1.00 48.91 ? 128 VAL A O 1 ATOM 962 C CB . VAL A 1 130 ? 45.182 -7.101 -20.990 1.00 44.80 ? 128 VAL A CB 1 ATOM 963 C CG1 . VAL A 1 130 ? 44.190 -7.940 -20.203 1.00 39.78 ? 128 VAL A CG1 1 ATOM 964 C CG2 . VAL A 1 130 ? 45.932 -6.135 -20.055 1.00 49.06 ? 128 VAL A CG2 1 ATOM 965 N N . ARG A 1 131 ? 47.345 -6.433 -23.120 1.00 49.82 ? 129 ARG A N 1 ATOM 966 C CA . ARG A 1 131 ? 48.443 -5.591 -23.579 1.00 52.70 ? 129 ARG A CA 1 ATOM 967 C C . ARG A 1 131 ? 48.287 -4.181 -23.053 1.00 51.21 ? 129 ARG A C 1 ATOM 968 O O . ARG A 1 131 ? 47.179 -3.650 -23.004 1.00 49.28 ? 129 ARG A O 1 ATOM 969 C CB . ARG A 1 131 ? 48.479 -5.560 -25.110 1.00 55.85 ? 129 ARG A CB 1 ATOM 970 C CG . ARG A 1 131 ? 49.130 -6.772 -25.732 1.00 63.73 ? 129 ARG A CG 1 ATOM 971 C CD . ARG A 1 131 ? 50.642 -6.582 -25.796 1.00 79.44 ? 129 ARG A CD 1 ATOM 972 N NE . ARG A 1 131 ? 51.346 -7.845 -25.999 1.00 89.63 ? 129 ARG A NE 1 ATOM 973 C CZ . ARG A 1 131 ? 51.490 -8.448 -27.175 1.00 98.21 ? 129 ARG A CZ 1 ATOM 974 N NH1 . ARG A 1 131 ? 50.979 -7.910 -28.278 1.00 101.22 ? 129 ARG A NH1 1 ATOM 975 N NH2 . ARG A 1 131 ? 52.148 -9.598 -27.248 1.00 103.64 ? 129 ARG A NH2 1 ATOM 976 N N . VAL A 1 132 ? 49.403 -3.576 -22.662 1.00 51.78 ? 130 VAL A N 1 ATOM 977 C CA . VAL A 1 132 ? 49.383 -2.175 -22.235 1.00 52.61 ? 130 VAL A CA 1 ATOM 978 C C . VAL A 1 132 ? 48.557 -1.347 -23.204 1.00 52.11 ? 130 VAL A C 1 ATOM 979 O O . VAL A 1 132 ? 48.680 -1.483 -24.419 1.00 52.60 ? 130 VAL A O 1 ATOM 980 C CB . VAL A 1 132 ? 50.793 -1.530 -22.161 1.00 55.87 ? 130 VAL A CB 1 ATOM 981 C CG1 . VAL A 1 132 ? 50.665 -0.061 -21.864 1.00 54.22 ? 130 VAL A CG1 1 ATOM 982 C CG2 . VAL A 1 132 ? 51.658 -2.195 -21.104 1.00 57.17 ? 130 VAL A CG2 1 ATOM 983 N N . GLY A 1 133 ? 47.712 -0.494 -22.641 1.00 51.24 ? 131 GLY A N 1 ATOM 984 C CA . GLY A 1 133 ? 46.880 0.405 -23.422 1.00 52.28 ? 131 GLY A CA 1 ATOM 985 C C . GLY A 1 133 ? 45.483 -0.143 -23.610 1.00 50.58 ? 131 GLY A C 1 ATOM 986 O O . GLY A 1 133 ? 44.564 0.588 -23.960 1.00 51.98 ? 131 GLY A O 1 ATOM 987 N N . ASP A 1 134 ? 45.329 -1.438 -23.371 1.00 48.12 ? 132 ASP A N 1 ATOM 988 C CA . ASP A 1 134 ? 44.032 -2.101 -23.522 1.00 46.66 ? 132 ASP A CA 1 ATOM 989 C C . ASP A 1 134 ? 42.991 -1.694 -22.499 1.00 44.58 ? 132 ASP A C 1 ATOM 990 O O . ASP A 1 134 ? 43.297 -1.340 -21.364 1.00 45.53 ? 132 ASP A O 1 ATOM 991 C CB . ASP A 1 134 ? 44.177 -3.623 -23.413 1.00 46.31 ? 132 ASP A CB 1 ATOM 992 C CG . ASP A 1 134 ? 44.879 -4.228 -24.603 1.00 53.52 ? 132 ASP A CG 1 ATOM 993 O OD1 . ASP A 1 134 ? 45.222 -3.460 -25.529 1.00 66.41 ? 132 ASP A OD1 1 ATOM 994 O OD2 . ASP A 1 134 ? 45.071 -5.467 -24.619 1.00 54.75 ? 132 ASP A OD2 1 ATOM 995 N N . THR A 1 135 ? 41.744 -1.783 -22.933 1.00 42.41 ? 133 THR A N 1 ATOM 996 C CA . THR A 1 135 ? 40.612 -1.797 -22.033 1.00 40.25 ? 133 THR A CA 1 ATOM 997 C C . THR A 1 135 ? 40.167 -3.248 -21.871 1.00 39.98 ? 133 THR A C 1 ATOM 998 O O . THR A 1 135 ? 39.982 -3.971 -22.844 1.00 41.08 ? 133 THR A O 1 ATOM 999 C CB . THR A 1 135 ? 39.450 -0.973 -22.560 1.00 40.16 ? 133 THR A CB 1 ATOM 1000 O OG1 . THR A 1 135 ? 39.807 0.406 -22.541 1.00 43.65 ? 133 THR A OG1 1 ATOM 1001 C CG2 . THR A 1 135 ? 38.208 -1.171 -21.700 1.00 40.30 ? 133 THR A CG2 1 ATOM 1002 N N . THR A 1 136 ? 39.990 -3.655 -20.625 1.00 39.07 ? 134 THR A N 1 ATOM 1003 C CA . THR A 1 136 ? 39.656 -5.028 -20.310 1.00 37.60 ? 134 THR A CA 1 ATOM 1004 C C . THR A 1 136 ? 38.523 -5.143 -19.315 1.00 36.92 ? 134 THR A C 1 ATOM 1005 O O . THR A 1 136 ? 38.575 -4.595 -18.215 1.00 36.00 ? 134 THR A O 1 ATOM 1006 C CB . THR A 1 136 ? 40.841 -5.787 -19.712 1.00 37.82 ? 134 THR A CB 1 ATOM 1007 O OG1 . THR A 1 136 ? 40.349 -6.970 -19.076 1.00 39.49 ? 134 THR A OG1 1 ATOM 1008 C CG2 . THR A 1 136 ? 41.550 -4.962 -18.669 1.00 39.73 ? 134 THR A CG2 1 ATOM 1009 N N . GLN A 1 137 ? 37.502 -5.882 -19.729 1.00 37.05 ? 135 GLN A N 1 ATOM 1010 C CA . GLN A 1 137 ? 36.358 -6.173 -18.877 1.00 36.70 ? 135 GLN A CA 1 ATOM 1011 C C . GLN A 1 137 ? 36.718 -7.253 -17.889 1.00 34.62 ? 135 GLN A C 1 ATOM 1012 O O . GLN A 1 137 ? 37.452 -8.175 -18.206 1.00 35.29 ? 135 GLN A O 1 ATOM 1013 C CB . GLN A 1 137 ? 35.135 -6.616 -19.688 1.00 36.93 ? 135 GLN A CB 1 ATOM 1014 C CG . GLN A 1 137 ? 34.026 -7.162 -18.805 1.00 37.78 ? 135 GLN A CG 1 ATOM 1015 C CD . GLN A 1 137 ? 32.761 -7.449 -19.563 1.00 42.91 ? 135 GLN A CD 1 ATOM 1016 O OE1 . GLN A 1 137 ? 31.713 -6.890 -19.258 1.00 51.05 ? 135 GLN A OE1 1 ATOM 1017 N NE2 . GLN A 1 137 ? 32.845 -8.324 -20.561 1.00 48.56 ? 135 GLN A NE2 1 ATOM 1018 N N . MET A 1 138 ? 36.195 -7.099 -16.683 1.00 34.16 ? 136 MET A N 1 ATOM 1019 C CA . MET A 1 138 ? 36.343 -8.087 -15.631 1.00 34.10 ? 136 MET A CA 1 ATOM 1020 C C . MET A 1 138 ? 34.975 -8.504 -15.085 1.00 34.50 ? 136 MET A C 1 ATOM 1021 O O . MET A 1 138 ? 34.239 -7.727 -14.459 1.00 32.29 ? 136 MET A O 1 ATOM 1022 C CB . MET A 1 138 ? 37.223 -7.538 -14.531 1.00 35.04 ? 136 MET A CB 1 ATOM 1023 C CG . MET A 1 138 ? 38.607 -7.184 -14.984 1.00 36.89 ? 136 MET A CG 1 ATOM 1024 S SD . MET A 1 138 ? 39.638 -6.723 -13.565 1.00 45.24 ? 136 MET A SD 1 ATOM 1025 C CE . MET A 1 138 ? 38.501 -5.658 -12.681 1.00 46.56 ? 136 MET A CE 1 ATOM 1026 N N . ARG A 1 139 ? 34.647 -9.758 -15.347 1.00 35.56 ? 137 ARG A N 1 ATOM 1027 C CA . ARG A 1 139 ? 33.291 -10.234 -15.146 1.00 36.61 ? 137 ARG A CA 1 ATOM 1028 C C . ARG A 1 139 ? 33.046 -10.542 -13.687 1.00 35.80 ? 137 ARG A C 1 ATOM 1029 O O . ARG A 1 139 ? 33.905 -11.095 -12.993 1.00 34.71 ? 137 ARG A O 1 ATOM 1030 C CB . ARG A 1 139 ? 33.028 -11.476 -15.998 1.00 37.78 ? 137 ARG A CB 1 ATOM 1031 C CG . ARG A 1 139 ? 33.178 -11.250 -17.496 1.00 47.45 ? 137 ARG A CG 1 ATOM 1032 C CD . ARG A 1 139 ? 32.045 -10.406 -18.023 1.00 60.57 ? 137 ARG A CD 1 ATOM 1033 N NE . ARG A 1 139 ? 30.782 -11.147 -18.008 1.00 71.36 ? 137 ARG A NE 1 ATOM 1034 C CZ . ARG A 1 139 ? 29.572 -10.594 -17.943 1.00 78.17 ? 137 ARG A CZ 1 ATOM 1035 N NH1 . ARG A 1 139 ? 29.425 -9.276 -17.865 1.00 78.96 ? 137 ARG A NH1 1 ATOM 1036 N NH2 . ARG A 1 139 ? 28.499 -11.373 -17.947 1.00 84.44 ? 137 ARG A NH2 1 ATOM 1037 N N . CYS A 1 140 ? 31.858 -10.158 -13.242 1.00 35.45 ? 138 CYS A N 1 ATOM 1038 C CA . CYS A 1 140 ? 31.375 -10.502 -11.913 1.00 36.28 ? 138 CYS A CA 1 ATOM 1039 C C . CYS A 1 140 ? 29.884 -10.231 -11.779 1.00 36.64 ? 138 CYS A C 1 ATOM 1040 O O . CYS A 1 140 ? 29.433 -9.100 -11.962 1.00 38.05 ? 138 CYS A O 1 ATOM 1041 C CB . CYS A 1 140 ? 32.125 -9.701 -10.878 1.00 37.25 ? 138 CYS A CB 1 ATOM 1042 S SG . CYS A 1 140 ? 31.941 -10.347 -9.252 1.00 48.12 ? 138 CYS A SG 1 ATOM 1043 N N . SER A 1 141 ? 29.135 -11.286 -11.468 1.00 35.48 ? 139 SER A N 1 ATOM 1044 C CA . SER A 1 141 ? 27.682 -11.207 -11.336 1.00 35.30 ? 139 SER A CA 1 ATOM 1045 C C . SER A 1 141 ? 27.085 -12.331 -10.517 1.00 36.67 ? 139 SER A C 1 ATOM 1046 O O . SER A 1 141 ? 27.732 -13.331 -10.212 1.00 39.00 ? 139 SER A O 1 ATOM 1047 C CB . SER A 1 141 ? 27.032 -11.264 -12.704 1.00 36.24 ? 139 SER A CB 1 ATOM 1048 O OG . SER A 1 141 ? 27.064 -12.587 -13.218 1.00 34.48 ? 139 SER A OG 1 ATOM 1049 N N . ILE A 1 142 ? 25.829 -12.128 -10.151 1.00 36.64 ? 140 ILE A N 1 ATOM 1050 C CA . ILE A 1 142 ? 24.986 -13.192 -9.663 1.00 35.70 ? 140 ILE A CA 1 ATOM 1051 C C . ILE A 1 142 ? 23.839 -13.323 -10.628 1.00 36.93 ? 140 ILE A C 1 ATOM 1052 O O . ILE A 1 142 ? 23.053 -12.397 -10.815 1.00 39.62 ? 140 ILE A O 1 ATOM 1053 C CB . ILE A 1 142 ? 24.399 -12.891 -8.290 1.00 37.50 ? 140 ILE A CB 1 ATOM 1054 C CG1 . ILE A 1 142 ? 25.502 -12.718 -7.247 1.00 38.05 ? 140 ILE A CG1 1 ATOM 1055 C CG2 . ILE A 1 142 ? 23.456 -14.016 -7.881 1.00 39.06 ? 140 ILE A CG2 1 ATOM 1056 C CD1 . ILE A 1 142 ? 25.013 -12.936 -5.829 1.00 36.41 ? 140 ILE A CD1 1 ATOM 1057 N N . GLN A 1 143 ? 23.760 -14.475 -11.265 1.00 36.37 ? 141 GLN A N 1 ATOM 1058 C CA . GLN A 1 143 ? 22.670 -14.745 -12.186 1.00 36.46 ? 141 GLN A CA 1 ATOM 1059 C C . GLN A 1 143 ? 21.415 -14.925 -11.372 1.00 38.75 ? 141 GLN A C 1 ATOM 1060 O O . GLN A 1 143 ? 21.431 -15.575 -10.320 1.00 39.40 ? 141 GLN A O 1 ATOM 1061 C CB . GLN A 1 143 ? 22.960 -15.988 -13.009 1.00 36.72 ? 141 GLN A CB 1 ATOM 1062 C CG . GLN A 1 143 ? 24.159 -15.825 -13.915 1.00 35.93 ? 141 GLN A CG 1 ATOM 1063 C CD . GLN A 1 143 ? 23.968 -14.718 -14.928 1.00 37.46 ? 141 GLN A CD 1 ATOM 1064 O OE1 . GLN A 1 143 ? 22.946 -14.661 -15.621 1.00 39.35 ? 141 GLN A OE1 1 ATOM 1065 N NE2 . GLN A 1 143 ? 24.948 -13.826 -15.017 1.00 31.47 ? 141 GLN A NE2 1 ATOM 1066 N N . SER A 1 144 ? 20.334 -14.331 -11.862 1.00 40.02 ? 142 SER A N 1 ATOM 1067 C CA . SER A 1 144 ? 19.090 -14.251 -11.105 1.00 41.88 ? 142 SER A CA 1 ATOM 1068 C C . SER A 1 144 ? 17.867 -14.102 -11.976 1.00 43.91 ? 142 SER A C 1 ATOM 1069 O O . SER A 1 144 ? 17.940 -13.649 -13.103 1.00 45.30 ? 142 SER A O 1 ATOM 1070 C CB . SER A 1 144 ? 19.158 -13.061 -10.150 1.00 43.21 ? 142 SER A CB 1 ATOM 1071 O OG . SER A 1 144 ? 17.887 -12.783 -9.587 1.00 47.63 ? 142 SER A OG 1 ATOM 1072 N N . THR A 1 145 ? 16.729 -14.487 -11.428 1.00 46.45 ? 143 THR A N 1 ATOM 1073 C CA . THR A 1 145 ? 15.459 -14.343 -12.129 1.00 48.72 ? 143 THR A CA 1 ATOM 1074 C C . THR A 1 145 ? 14.708 -13.157 -11.558 1.00 51.87 ? 143 THR A C 1 ATOM 1075 O O . THR A 1 145 ? 13.601 -12.842 -11.975 1.00 54.47 ? 143 THR A O 1 ATOM 1076 C CB . THR A 1 145 ? 14.597 -15.589 -11.971 1.00 49.65 ? 143 THR A CB 1 ATOM 1077 O OG1 . THR A 1 145 ? 14.373 -15.831 -10.581 1.00 47.31 ? 143 THR A OG1 1 ATOM 1078 C CG2 . THR A 1 145 ? 15.285 -16.786 -12.583 1.00 47.50 ? 143 THR A CG2 1 ATOM 1079 N N . GLU A 1 146 ? 15.342 -12.504 -10.596 1.00 52.60 ? 144 GLU A N 1 ATOM 1080 C CA . GLU A 1 146 ? 14.756 -11.360 -9.899 1.00 56.40 ? 144 GLU A CA 1 ATOM 1081 C C . GLU A 1 146 ? 15.714 -10.163 -9.859 1.00 56.34 ? 144 GLU A C 1 ATOM 1082 O O . GLU A 1 146 ? 16.907 -10.308 -9.562 1.00 52.70 ? 144 GLU A O 1 ATOM 1083 C CB . GLU A 1 146 ? 14.361 -11.765 -8.474 1.00 56.92 ? 144 GLU A CB 1 ATOM 1084 C CG . GLU A 1 146 ? 13.593 -13.082 -8.385 1.00 59.42 ? 144 GLU A CG 1 ATOM 1085 C CD . GLU A 1 146 ? 12.261 -13.062 -9.137 1.00 67.06 ? 144 GLU A CD 1 ATOM 1086 O OE1 . GLU A 1 146 ? 11.518 -12.059 -9.039 1.00 70.86 ? 144 GLU A OE1 1 ATOM 1087 O OE2 . GLU A 1 146 ? 11.953 -14.060 -9.825 1.00 69.62 ? 144 GLU A OE2 1 ATOM 1088 N N . GLU A 1 147 ? 15.175 -8.983 -10.163 1.00 59.88 ? 145 GLU A N 1 ATOM 1089 C CA . GLU A 1 147 ? 15.985 -7.753 -10.217 1.00 60.64 ? 145 GLU A CA 1 ATOM 1090 C C . GLU A 1 147 ? 16.317 -7.209 -8.848 1.00 59.53 ? 145 GLU A C 1 ATOM 1091 O O . GLU A 1 147 ? 15.774 -7.636 -7.832 1.00 59.29 ? 145 GLU A O 1 ATOM 1092 C CB . GLU A 1 147 ? 15.309 -6.642 -11.030 1.00 65.32 ? 145 GLU A CB 1 ATOM 1093 C CG . GLU A 1 147 ? 15.604 -6.701 -12.520 1.00 71.07 ? 145 GLU A CG 1 ATOM 1094 C CD . GLU A 1 147 ? 15.178 -5.433 -13.269 1.00 82.20 ? 145 GLU A CD 1 ATOM 1095 O OE1 . GLU A 1 147 ? 15.183 -4.336 -12.658 1.00 85.36 ? 145 GLU A OE1 1 ATOM 1096 O OE2 . GLU A 1 147 ? 14.845 -5.537 -14.475 1.00 86.99 ? 145 GLU A OE2 1 ATOM 1097 N N . LYS A 1 148 ? 17.249 -6.266 -8.867 1.00 58.09 ? 146 LYS A N 1 ATOM 1098 C CA . LYS A 1 148 ? 17.609 -5.463 -7.706 1.00 58.75 ? 146 LYS A CA 1 ATOM 1099 C C . LYS A 1 148 ? 17.934 -6.283 -6.463 1.00 56.18 ? 146 LYS A C 1 ATOM 1100 O O . LYS A 1 148 ? 17.605 -5.862 -5.355 1.00 58.81 ? 146 LYS A O 1 ATOM 1101 C CB . LYS A 1 148 ? 16.457 -4.515 -7.360 1.00 64.10 ? 146 LYS A CB 1 ATOM 1102 C CG . LYS A 1 148 ? 16.013 -3.606 -8.490 1.00 68.85 ? 146 LYS A CG 1 ATOM 1103 C CD . LYS A 1 148 ? 16.972 -2.452 -8.679 1.00 73.06 ? 146 LYS A CD 1 ATOM 1104 C CE . LYS A 1 148 ? 16.444 -1.440 -9.693 1.00 78.76 ? 146 LYS A CE 1 ATOM 1105 N NZ . LYS A 1 148 ? 15.408 -0.531 -9.116 1.00 87.06 ? 146 LYS A NZ 1 ATOM 1106 N N . ARG A 1 149 ? 18.584 -7.431 -6.635 1.00 51.27 ? 147 ARG A N 1 ATOM 1107 C CA . ARG A 1 149 ? 18.839 -8.331 -5.496 1.00 49.60 ? 147 ARG A CA 1 ATOM 1108 C C . ARG A 1 149 ? 20.212 -8.164 -4.864 1.00 47.55 ? 147 ARG A C 1 ATOM 1109 O O . ARG A 1 149 ? 20.406 -8.451 -3.678 1.00 47.44 ? 147 ARG A O 1 ATOM 1110 C CB . ARG A 1 149 ? 18.640 -9.791 -5.890 1.00 47.61 ? 147 ARG A CB 1 ATOM 1111 C CG . ARG A 1 149 ? 17.205 -10.160 -6.170 1.00 48.81 ? 147 ARG A CG 1 ATOM 1112 C CD . ARG A 1 149 ? 16.246 -9.544 -5.180 1.00 52.37 ? 147 ARG A CD 1 ATOM 1113 N NE . ARG A 1 149 ? 15.031 -10.344 -5.112 1.00 56.45 ? 147 ARG A NE 1 ATOM 1114 C CZ . ARG A 1 149 ? 14.770 -11.228 -4.158 1.00 59.25 ? 147 ARG A CZ 1 ATOM 1115 N NH1 . ARG A 1 149 ? 15.631 -11.415 -3.163 1.00 60.52 ? 147 ARG A NH1 1 ATOM 1116 N NH2 . ARG A 1 149 ? 13.642 -11.922 -4.195 1.00 61.25 ? 147 ARG A NH2 1 ATOM 1117 N N . VAL A 1 150 ? 21.160 -7.702 -5.663 1.00 46.17 ? 148 VAL A N 1 ATOM 1118 C CA . VAL A 1 150 ? 22.498 -7.393 -5.159 1.00 45.50 ? 148 VAL A CA 1 ATOM 1119 C C . VAL A 1 150 ? 22.462 -6.156 -4.284 1.00 48.31 ? 148 VAL A C 1 ATOM 1120 O O . VAL A 1 150 ? 21.849 -5.150 -4.618 1.00 50.44 ? 148 VAL A O 1 ATOM 1121 C CB . VAL A 1 150 ? 23.513 -7.177 -6.298 1.00 43.46 ? 148 VAL A CB 1 ATOM 1122 C CG1 . VAL A 1 150 ? 24.826 -6.660 -5.746 1.00 42.89 ? 148 VAL A CG1 1 ATOM 1123 C CG2 . VAL A 1 150 ? 23.728 -8.476 -7.066 1.00 41.62 ? 148 VAL A CG2 1 ATOM 1124 N N . THR A 1 151 ? 23.136 -6.258 -3.152 1.00 49.14 ? 149 THR A N 1 ATOM 1125 C CA . THR A 1 151 ? 23.142 -5.204 -2.149 1.00 52.35 ? 149 THR A CA 1 ATOM 1126 C C . THR A 1 151 ? 24.433 -4.423 -2.228 1.00 54.61 ? 149 THR A C 1 ATOM 1127 O O . THR A 1 151 ? 24.462 -3.205 -2.068 1.00 58.07 ? 149 THR A O 1 ATOM 1128 C CB . THR A 1 151 ? 23.009 -5.795 -0.742 1.00 52.63 ? 149 THR A CB 1 ATOM 1129 O OG1 . THR A 1 151 ? 21.625 -6.034 -0.469 1.00 50.51 ? 149 THR A OG1 1 ATOM 1130 C CG2 . THR A 1 151 ? 23.586 -4.855 0.304 1.00 55.96 ? 149 THR A CG2 1 ATOM 1131 N N . LYS A 1 152 ? 25.506 -5.143 -2.504 1.00 53.46 ? 150 LYS A N 1 ATOM 1132 C CA . LYS A 1 152 ? 26.837 -4.568 -2.413 1.00 55.30 ? 150 LYS A CA 1 ATOM 1133 C C . LYS A 1 152 ? 27.832 -5.287 -3.326 1.00 53.25 ? 150 LYS A C 1 ATOM 1134 O O . LYS A 1 152 ? 27.824 -6.516 -3.441 1.00 51.10 ? 150 LYS A O 1 ATOM 1135 C CB . LYS A 1 152 ? 27.278 -4.619 -0.945 1.00 57.35 ? 150 LYS A CB 1 ATOM 1136 C CG . LYS A 1 152 ? 28.727 -4.336 -0.677 1.00 59.36 ? 150 LYS A CG 1 ATOM 1137 C CD . LYS A 1 152 ? 29.004 -4.443 0.820 1.00 65.12 ? 150 LYS A CD 1 ATOM 1138 C CE . LYS A 1 152 ? 30.479 -4.214 1.139 1.00 69.43 ? 150 LYS A CE 1 ATOM 1139 N NZ . LYS A 1 152 ? 30.773 -4.350 2.594 1.00 74.49 ? 150 LYS A NZ 1 ATOM 1140 N N . VAL A 1 153 ? 28.656 -4.491 -3.996 1.00 54.24 ? 151 VAL A N 1 ATOM 1141 C CA . VAL A 1 153 ? 29.754 -5.007 -4.812 1.00 52.44 ? 151 VAL A CA 1 ATOM 1142 C C . VAL A 1 153 ? 31.037 -4.301 -4.437 1.00 54.54 ? 151 VAL A C 1 ATOM 1143 O O . VAL A 1 153 ? 31.080 -3.076 -4.371 1.00 55.59 ? 151 VAL A O 1 ATOM 1144 C CB . VAL A 1 153 ? 29.529 -4.755 -6.308 1.00 51.52 ? 151 VAL A CB 1 ATOM 1145 C CG1 . VAL A 1 153 ? 30.743 -5.226 -7.111 1.00 48.12 ? 151 VAL A CG1 1 ATOM 1146 C CG2 . VAL A 1 153 ? 28.262 -5.444 -6.776 1.00 52.25 ? 151 VAL A CG2 1 ATOM 1147 N N . ASN A 1 154 ? 32.083 -5.088 -4.220 1.00 53.95 ? 152 ASN A N 1 ATOM 1148 C CA . ASN A 1 154 ? 33.376 -4.543 -3.823 1.00 55.59 ? 152 ASN A CA 1 ATOM 1149 C C . ASN A 1 154 ? 34.545 -5.152 -4.572 1.00 53.07 ? 152 ASN A C 1 ATOM 1150 O O . ASN A 1 154 ? 34.836 -6.340 -4.437 1.00 51.60 ? 152 ASN A O 1 ATOM 1151 C CB . ASN A 1 154 ? 33.589 -4.742 -2.330 1.00 58.44 ? 152 ASN A CB 1 ATOM 1152 C CG . ASN A 1 154 ? 34.990 -4.367 -1.890 1.00 65.63 ? 152 ASN A CG 1 ATOM 1153 O OD1 . ASN A 1 154 ? 35.494 -3.288 -2.218 1.00 73.81 ? 152 ASN A OD1 1 ATOM 1154 N ND2 . ASN A 1 154 ? 35.630 -5.258 -1.139 1.00 70.29 ? 152 ASN A ND2 1 ATOM 1155 N N . TRP A 1 155 ? 35.219 -4.308 -5.347 1.00 52.05 ? 153 TRP A N 1 ATOM 1156 C CA . TRP A 1 155 ? 36.419 -4.714 -6.075 1.00 48.76 ? 153 TRP A CA 1 ATOM 1157 C C . TRP A 1 155 ? 37.620 -4.228 -5.311 1.00 51.26 ? 153 TRP A C 1 ATOM 1158 O O . TRP A 1 155 ? 37.715 -3.047 -4.994 1.00 53.56 ? 153 TRP A O 1 ATOM 1159 C CB . TRP A 1 155 ? 36.452 -4.130 -7.495 1.00 46.15 ? 153 TRP A CB 1 ATOM 1160 C CG . TRP A 1 155 ? 35.524 -4.804 -8.464 1.00 40.23 ? 153 TRP A CG 1 ATOM 1161 C CD1 . TRP A 1 155 ? 34.251 -4.430 -8.773 1.00 38.78 ? 153 TRP A CD1 1 ATOM 1162 C CD2 . TRP A 1 155 ? 35.805 -5.957 -9.265 1.00 32.61 ? 153 TRP A CD2 1 ATOM 1163 N NE1 . TRP A 1 155 ? 33.720 -5.277 -9.708 1.00 34.07 ? 153 TRP A NE1 1 ATOM 1164 C CE2 . TRP A 1 155 ? 34.652 -6.226 -10.026 1.00 31.87 ? 153 TRP A CE2 1 ATOM 1165 C CE3 . TRP A 1 155 ? 36.912 -6.795 -9.401 1.00 33.95 ? 153 TRP A CE3 1 ATOM 1166 C CZ2 . TRP A 1 155 ? 34.572 -7.295 -10.907 1.00 33.86 ? 153 TRP A CZ2 1 ATOM 1167 C CZ3 . TRP A 1 155 ? 36.838 -7.854 -10.285 1.00 35.42 ? 153 TRP A CZ3 1 ATOM 1168 C CH2 . TRP A 1 155 ? 35.678 -8.095 -11.028 1.00 35.30 ? 153 TRP A CH2 1 ATOM 1169 N N . MET A 1 156 ? 38.525 -5.154 -5.012 1.00 51.14 ? 154 MET A N 1 ATOM 1170 C CA . MET A 1 156 ? 39.811 -4.815 -4.407 1.00 54.43 ? 154 MET A CA 1 ATOM 1171 C C . MET A 1 156 ? 40.936 -5.194 -5.351 1.00 53.10 ? 154 MET A C 1 ATOM 1172 O O . MET A 1 156 ? 40.788 -6.068 -6.196 1.00 51.02 ? 154 MET A O 1 ATOM 1173 C CB . MET A 1 156 ? 40.001 -5.529 -3.069 1.00 56.33 ? 154 MET A CB 1 ATOM 1174 C CG . MET A 1 156 ? 39.016 -5.109 -1.978 1.00 60.44 ? 154 MET A CG 1 ATOM 1175 S SD . MET A 1 156 ? 39.132 -3.377 -1.462 1.00 71.49 ? 154 MET A SD 1 ATOM 1176 C CE . MET A 1 156 ? 40.773 -3.314 -0.733 1.00 69.91 ? 154 MET A CE 1 ATOM 1177 N N . PHE A 1 157 ? 42.059 -4.513 -5.203 1.00 55.48 ? 155 PHE A N 1 ATOM 1178 C CA . PHE A 1 157 ? 43.251 -4.816 -5.977 1.00 55.25 ? 155 PHE A CA 1 ATOM 1179 C C . PHE A 1 157 ? 44.462 -5.038 -5.096 1.00 58.17 ? 155 PHE A C 1 ATOM 1180 O O . PHE A 1 157 ? 44.561 -4.481 -4.006 1.00 59.25 ? 155 PHE A O 1 ATOM 1181 C CB . PHE A 1 157 ? 43.560 -3.670 -6.942 1.00 56.23 ? 155 PHE A CB 1 ATOM 1182 C CG . PHE A 1 157 ? 44.871 -3.822 -7.653 1.00 56.30 ? 155 PHE A CG 1 ATOM 1183 C CD1 . PHE A 1 157 ? 45.074 -4.862 -8.541 1.00 58.88 ? 155 PHE A CD1 1 ATOM 1184 C CD2 . PHE A 1 157 ? 45.897 -2.938 -7.429 1.00 60.61 ? 155 PHE A CD2 1 ATOM 1185 C CE1 . PHE A 1 157 ? 46.276 -5.011 -9.199 1.00 64.12 ? 155 PHE A CE1 1 ATOM 1186 C CE2 . PHE A 1 157 ? 47.098 -3.079 -8.083 1.00 66.78 ? 155 PHE A CE2 1 ATOM 1187 C CZ . PHE A 1 157 ? 47.289 -4.118 -8.971 1.00 66.29 ? 155 PHE A CZ 1 ATOM 1188 N N . SER A 1 158 ? 45.373 -5.864 -5.599 1.00 59.17 ? 156 SER A N 1 ATOM 1189 C CA . SER A 1 158 ? 46.722 -5.989 -5.046 1.00 65.39 ? 156 SER A CA 1 ATOM 1190 C C . SER A 1 158 ? 47.564 -7.038 -5.746 1.00 68.38 ? 156 SER A C 1 ATOM 1191 O O . SER A 1 158 ? 47.086 -8.124 -6.065 1.00 67.12 ? 156 SER A O 1 ATOM 1192 C CB . SER A 1 158 ? 46.675 -6.363 -3.571 1.00 67.41 ? 156 SER A CB 1 ATOM 1193 O OG . SER A 1 158 ? 46.385 -7.730 -3.417 1.00 64.03 ? 156 SER A OG 1 ATOM 1194 N N . SER A 1 159 ? 48.826 -6.713 -5.983 1.00 74.13 ? 157 SER A N 1 ATOM 1195 C CA . SER A 1 159 ? 49.810 -7.764 -6.213 1.00 77.60 ? 157 SER A CA 1 ATOM 1196 C C . SER A 1 159 ? 50.007 -8.371 -4.833 1.00 84.02 ? 157 SER A C 1 ATOM 1197 O O . SER A 1 159 ? 50.983 -8.066 -4.129 1.00 89.06 ? 157 SER A O 1 ATOM 1198 C CB . SER A 1 159 ? 51.115 -7.215 -6.788 1.00 79.58 ? 157 SER A CB 1 ATOM 1199 O OG . SER A 1 159 ? 51.646 -6.211 -5.954 1.00 80.08 ? 157 SER A OG 1 ATOM 1200 N N . GLY A 1 160 ? 49.054 -9.233 -4.469 1.00 83.91 ? 158 GLY A N 1 ATOM 1201 C CA . GLY A 1 160 ? 48.750 -9.552 -3.064 1.00 88.49 ? 158 GLY A CA 1 ATOM 1202 C C . GLY A 1 160 ? 49.293 -10.794 -2.375 1.00 93.50 ? 158 GLY A C 1 ATOM 1203 O O . GLY A 1 160 ? 48.536 -11.713 -2.044 1.00 93.79 ? 158 GLY A O 1 ATOM 1204 N N . SER A 1 161 ? 50.597 -10.805 -2.135 1.00 99.02 ? 159 SER A N 1 ATOM 1205 C CA . SER A 1 161 ? 51.218 -11.753 -1.211 1.00 104.64 ? 159 SER A CA 1 ATOM 1206 C C . SER A 1 161 ? 52.119 -10.955 -0.286 1.00 111.48 ? 159 SER A C 1 ATOM 1207 O O . SER A 1 161 ? 53.092 -10.337 -0.734 1.00 113.61 ? 159 SER A O 1 ATOM 1208 C CB . SER A 1 161 ? 52.042 -12.801 -1.958 1.00 105.60 ? 159 SER A CB 1 ATOM 1209 O OG . SER A 1 161 ? 51.321 -13.336 -3.050 1.00 102.09 ? 159 SER A OG 1 ATOM 1210 N N . HIS A 1 162 ? 51.775 -10.959 1.000 1.00 115.16 ? 160 HIS A N 1 ATOM 1211 C CA . HIS A 1 162 ? 52.468 -10.141 2.002 1.00 121.29 ? 160 HIS A CA 1 ATOM 1212 C C . HIS A 1 162 ? 52.456 -8.659 1.604 1.00 120.07 ? 160 HIS A C 1 ATOM 1213 O O . HIS A 1 162 ? 53.417 -7.916 1.850 1.00 124.20 ? 160 HIS A O 1 ATOM 1214 C CB . HIS A 1 162 ? 53.903 -10.639 2.217 1.00 127.58 ? 160 HIS A CB 1 ATOM 1215 C CG . HIS A 1 162 ? 53.986 -11.909 3.007 1.00 131.45 ? 160 HIS A CG 1 ATOM 1216 N ND1 . HIS A 1 162 ? 54.938 -12.120 3.981 1.00 138.33 ? 160 HIS A ND1 1 ATOM 1217 C CD2 . HIS A 1 162 ? 53.221 -13.026 2.980 1.00 127.98 ? 160 HIS A CD2 1 ATOM 1218 C CE1 . HIS A 1 162 ? 54.764 -13.317 4.513 1.00 140.41 ? 160 HIS A CE1 1 ATOM 1219 N NE2 . HIS A 1 162 ? 53.727 -13.887 3.924 1.00 134.30 ? 160 HIS A NE2 1 ATOM 1220 N N . THR A 1 163 ? 51.350 -8.253 0.986 1.00 113.90 ? 161 THR A N 1 ATOM 1221 C CA . THR A 1 163 ? 51.161 -6.871 0.542 1.00 112.06 ? 161 THR A CA 1 ATOM 1222 C C . THR A 1 163 ? 49.716 -6.391 0.682 1.00 107.80 ? 161 THR A C 1 ATOM 1223 O O . THR A 1 163 ? 48.756 -7.143 0.476 1.00 103.98 ? 161 THR A O 1 ATOM 1224 C CB . THR A 1 163 ? 51.630 -6.672 -0.919 1.00 109.49 ? 161 THR A CB 1 ATOM 1225 O OG1 . THR A 1 163 ? 51.245 -7.801 -1.712 1.00 101.85 ? 161 THR A OG1 1 ATOM 1226 C CG2 . THR A 1 163 ? 53.153 -6.499 -0.971 1.00 114.19 ? 161 THR A CG2 1 ATOM 1227 N N . GLU A 1 164 ? 49.600 -5.117 1.033 1.00 108.40 ? 162 GLU A N 1 ATOM 1228 C CA . GLU A 1 164 ? 48.310 -4.481 1.309 1.00 105.02 ? 162 GLU A CA 1 ATOM 1229 C C . GLU A 1 164 ? 47.447 -4.385 0.059 1.00 97.99 ? 162 GLU A C 1 ATOM 1230 O O . GLU A 1 164 ? 47.845 -4.805 -1.023 1.00 95.15 ? 162 GLU A O 1 ATOM 1231 C CB . GLU A 1 164 ? 48.514 -3.083 1.907 1.00 108.83 ? 162 GLU A CB 1 ATOM 1232 C CG . GLU A 1 164 ? 49.219 -3.099 3.266 1.00 114.65 ? 162 GLU A CG 1 ATOM 1233 C CD . GLU A 1 164 ? 50.340 -2.066 3.391 1.00 119.01 ? 162 GLU A CD 1 ATOM 1234 O OE1 . GLU A 1 164 ? 50.456 -1.169 2.524 1.00 111.78 ? 162 GLU A OE1 1 ATOM 1235 O OE2 . GLU A 1 164 ? 51.115 -2.158 4.368 1.00 123.94 ? 162 GLU A OE2 1 ATOM 1236 N N . GLU A 1 165 ? 46.270 -3.796 0.232 1.00 94.99 ? 163 GLU A N 1 ATOM 1237 C CA . GLU A 1 165 ? 45.268 -3.729 -0.821 1.00 88.03 ? 163 GLU A CA 1 ATOM 1238 C C . GLU A 1 165 ? 44.736 -2.331 -1.058 1.00 86.73 ? 163 GLU A C 1 ATOM 1239 O O . GLU A 1 165 ? 44.860 -1.433 -0.222 1.00 91.25 ? 163 GLU A O 1 ATOM 1240 C CB . GLU A 1 165 ? 44.096 -4.632 -0.473 1.00 85.66 ? 163 GLU A CB 1 ATOM 1241 C CG . GLU A 1 165 ? 44.486 -6.063 -0.190 1.00 87.84 ? 163 GLU A CG 1 ATOM 1242 C CD . GLU A 1 165 ? 43.276 -6.968 -0.029 1.00 87.34 ? 163 GLU A CD 1 ATOM 1243 O OE1 . GLU A 1 165 ? 42.505 -7.119 -1.007 1.00 81.75 ? 163 GLU A OE1 1 ATOM 1244 O OE2 . GLU A 1 165 ? 43.097 -7.525 1.077 1.00 90.33 ? 163 GLU A OE2 1 ATOM 1245 N N . GLU A 1 166 ? 44.139 -2.179 -2.230 1.00 80.51 ? 164 GLU A N 1 ATOM 1246 C CA . GLU A 1 166 ? 43.449 -0.955 -2.615 1.00 78.92 ? 164 GLU A CA 1 ATOM 1247 C C . GLU A 1 166 ? 42.053 -1.265 -3.106 1.00 71.95 ? 164 GLU A C 1 ATOM 1248 O O . GLU A 1 166 ? 41.791 -2.347 -3.620 1.00 66.94 ? 164 GLU A O 1 ATOM 1249 C CB . GLU A 1 166 ? 44.180 -0.254 -3.758 1.00 79.69 ? 164 GLU A CB 1 ATOM 1250 C CG . GLU A 1 166 ? 45.648 0.031 -3.538 1.00 84.35 ? 164 GLU A CG 1 ATOM 1251 C CD . GLU A 1 166 ? 46.257 0.759 -4.720 1.00 86.51 ? 164 GLU A CD 1 ATOM 1252 O OE1 . GLU A 1 166 ? 46.083 0.282 -5.863 1.00 83.54 ? 164 GLU A OE1 1 ATOM 1253 O OE2 . GLU A 1 166 ? 46.909 1.806 -4.507 1.00 92.15 ? 164 GLU A OE2 1 ATOM 1254 N N . THR A 1 167 ? 41.179 -0.278 -2.966 1.00 70.93 ? 165 THR A N 1 ATOM 1255 C CA . THR A 1 167 ? 39.823 -0.334 -3.517 1.00 65.72 ? 165 THR A CA 1 ATOM 1256 C C . THR A 1 167 ? 39.790 0.129 -4.959 1.00 63.03 ? 165 THR A C 1 ATOM 1257 O O . THR A 1 167 ? 40.045 1.305 -5.264 1.00 65.21 ? 165 THR A O 1 ATOM 1258 C CB . THR A 1 167 ? 38.856 0.570 -2.748 1.00 67.93 ? 165 THR A CB 1 ATOM 1259 O OG1 . THR A 1 167 ? 38.565 -0.015 -1.480 1.00 68.71 ? 165 THR A OG1 1 ATOM 1260 C CG2 . THR A 1 167 ? 37.568 0.755 -3.532 1.00 64.94 ? 165 THR A CG2 1 ATOM 1261 N N . VAL A 1 168 ? 39.454 -0.800 -5.845 1.00 57.10 ? 166 VAL A N 1 ATOM 1262 C CA . VAL A 1 168 ? 39.287 -0.462 -7.244 1.00 54.41 ? 166 VAL A CA 1 ATOM 1263 C C . VAL A 1 168 ? 37.984 0.297 -7.380 1.00 55.85 ? 166 VAL A C 1 ATOM 1264 O O . VAL A 1 168 ? 37.951 1.488 -7.695 1.00 59.04 ? 166 VAL A O 1 ATOM 1265 C CB . VAL A 1 168 ? 39.253 -1.712 -8.135 1.00 49.83 ? 166 VAL A CB 1 ATOM 1266 C CG1 . VAL A 1 168 ? 38.889 -1.341 -9.566 1.00 42.04 ? 166 VAL A CG1 1 ATOM 1267 C CG2 . VAL A 1 168 ? 40.597 -2.418 -8.097 1.00 48.67 ? 166 VAL A CG2 1 ATOM 1268 N N . LEU A 1 169 ? 36.907 -0.415 -7.110 1.00 54.30 ? 167 LEU A N 1 ATOM 1269 C CA . LEU A 1 169 ? 35.569 0.155 -7.212 1.00 55.05 ? 167 LEU A CA 1 ATOM 1270 C C . LEU A 1 169 ? 34.656 -0.476 -6.184 1.00 54.08 ? 167 LEU A C 1 ATOM 1271 O O . LEU A 1 169 ? 34.840 -1.624 -5.785 1.00 51.37 ? 167 LEU A O 1 ATOM 1272 C CB . LEU A 1 169 ? 35.008 -0.052 -8.629 1.00 52.87 ? 167 LEU A CB 1 ATOM 1273 C CG . LEU A 1 169 ? 33.565 0.385 -8.922 1.00 53.09 ? 167 LEU A CG 1 ATOM 1274 C CD1 . LEU A 1 169 ? 33.408 0.756 -10.386 1.00 48.05 ? 167 LEU A CD1 1 ATOM 1275 C CD2 . LEU A 1 169 ? 32.554 -0.694 -8.549 1.00 45.47 ? 167 LEU A CD2 1 ATOM 1276 N N . SER A 1 170 ? 33.671 0.300 -5.765 1.00 56.77 ? 168 SER A N 1 ATOM 1277 C CA . SER A 1 170 ? 32.688 -0.180 -4.811 1.00 58.75 ? 168 SER A CA 1 ATOM 1278 C C . SER A 1 170 ? 31.335 0.488 -4.974 1.00 61.99 ? 168 SER A C 1 ATOM 1279 O O . SER A 1 170 ? 31.236 1.667 -5.295 1.00 64.66 ? 168 SER A O 1 ATOM 1280 C CB . SER A 1 170 ? 33.193 0.005 -3.383 1.00 61.41 ? 168 SER A CB 1 ATOM 1281 O OG . SER A 1 170 ? 33.140 1.365 -3.008 1.00 68.58 ? 168 SER A OG 1 ATOM 1282 N N . TYR A 1 171 ? 30.299 -0.308 -4.753 1.00 63.01 ? 169 TYR A N 1 ATOM 1283 C CA . TYR A 1 171 ? 28.915 0.151 -4.810 1.00 66.99 ? 169 TYR A CA 1 ATOM 1284 C C . TYR A 1 171 ? 28.105 -0.467 -3.689 1.00 68.98 ? 169 TYR A C 1 ATOM 1285 O O . TYR A 1 171 ? 28.358 -1.599 -3.280 1.00 66.56 ? 169 TYR A O 1 ATOM 1286 C CB . TYR A 1 171 ? 28.294 -0.213 -6.157 1.00 65.43 ? 169 TYR A CB 1 ATOM 1287 C CG . TYR A 1 171 ? 26.803 0.020 -6.221 1.00 70.11 ? 169 TYR A CG 1 ATOM 1288 C CD1 . TYR A 1 171 ? 26.289 1.249 -6.618 1.00 78.15 ? 169 TYR A CD1 1 ATOM 1289 C CD2 . TYR A 1 171 ? 25.909 -0.988 -5.886 1.00 70.12 ? 169 TYR A CD2 1 ATOM 1290 C CE1 . TYR A 1 171 ? 24.925 1.468 -6.676 1.00 81.04 ? 169 TYR A CE1 1 ATOM 1291 C CE2 . TYR A 1 171 ? 24.547 -0.781 -5.938 1.00 75.48 ? 169 TYR A CE2 1 ATOM 1292 C CZ . TYR A 1 171 ? 24.060 0.451 -6.333 1.00 80.59 ? 169 TYR A CZ 1 ATOM 1293 O OH . TYR A 1 171 ? 22.702 0.662 -6.385 1.00 86.97 ? 169 TYR A OH 1 ATOM 1294 N N . ASP A 1 172 ? 27.120 0.286 -3.216 1.00 75.08 ? 170 ASP A N 1 ATOM 1295 C CA . ASP A 1 172 ? 26.303 -0.124 -2.067 1.00 79.20 ? 170 ASP A CA 1 ATOM 1296 C C . ASP A 1 172 ? 24.915 0.519 -2.061 1.00 84.75 ? 170 ASP A C 1 ATOM 1297 O O . ASP A 1 172 ? 24.732 1.638 -1.568 1.00 90.15 ? 170 ASP A O 1 ATOM 1298 C CB . ASP A 1 172 ? 27.045 0.197 -0.765 1.00 82.07 ? 170 ASP A CB 1 ATOM 1299 C CG . ASP A 1 172 ? 26.281 -0.240 0.475 1.00 87.31 ? 170 ASP A CG 1 ATOM 1300 O OD1 . ASP A 1 172 ? 25.711 -1.355 0.477 1.00 87.61 ? 170 ASP A OD1 1 ATOM 1301 O OD2 . ASP A 1 172 ? 26.262 0.530 1.464 1.00 95.23 ? 170 ASP A OD2 1 ATOM 1302 N N . SER A 1 173 ? 23.947 -0.224 -2.597 1.00 84.90 ? 171 SER A N 1 ATOM 1303 C CA . SER A 1 173 ? 22.549 0.224 -2.718 1.00 89.32 ? 171 SER A CA 1 ATOM 1304 C C . SER A 1 173 ? 22.051 0.805 -1.419 1.00 95.41 ? 171 SER A C 1 ATOM 1305 O O . SER A 1 173 ? 21.424 1.861 -1.388 1.00 100.39 ? 171 SER A O 1 ATOM 1306 C CB . SER A 1 173 ? 21.634 -0.940 -3.098 1.00 86.60 ? 171 SER A CB 1 ATOM 1307 O OG . SER A 1 173 ? 21.807 -1.307 -4.456 1.00 82.95 ? 171 SER A OG 1 ATOM 1308 N N . ASN A 1 174 ? 22.334 0.076 -0.351 1.00 96.18 ? 172 ASN A N 1 ATOM 1309 C CA . ASN A 1 174 ? 22.054 0.519 1.013 1.00 101.91 ? 172 ASN A CA 1 ATOM 1310 C C . ASN A 1 174 ? 22.309 2.022 1.167 1.00 108.29 ? 172 ASN A C 1 ATOM 1311 O O . ASN A 1 174 ? 21.516 2.738 1.782 1.00 113.29 ? 172 ASN A O 1 ATOM 1312 C CB . ASN A 1 174 ? 22.907 -0.295 1.998 1.00 100.46 ? 172 ASN A CB 1 ATOM 1313 C CG . ASN A 1 174 ? 23.075 0.381 3.341 1.00 107.40 ? 172 ASN A CG 1 ATOM 1314 O OD1 . ASN A 1 174 ? 22.175 0.357 4.179 1.00 112.80 ? 172 ASN A OD1 1 ATOM 1315 N ND2 . ASN A 1 174 ? 24.250 0.962 3.567 1.00 109.57 ? 172 ASN A ND2 1 ATOM 1316 N N . MET A 1 175 ? 23.399 2.492 0.561 1.00 108.52 ? 173 MET A N 1 ATOM 1317 C CA . MET A 1 175 ? 23.813 3.907 0.639 1.00 114.36 ? 173 MET A CA 1 ATOM 1318 C C . MET A 1 175 ? 23.366 4.751 -0.549 1.00 115.91 ? 173 MET A C 1 ATOM 1319 O O . MET A 1 175 ? 22.920 4.241 -1.580 1.00 112.11 ? 173 MET A O 1 ATOM 1320 C CB . MET A 1 175 ? 25.332 4.021 0.798 1.00 113.74 ? 173 MET A CB 1 ATOM 1321 C CG . MET A 1 175 ? 25.806 3.653 2.194 1.00 115.71 ? 173 MET A CG 1 ATOM 1322 S SD . MET A 1 175 ? 27.538 4.042 2.508 1.00 118.03 ? 173 MET A SD 1 ATOM 1323 C CE . MET A 1 175 ? 27.446 5.805 2.854 1.00 124.48 ? 173 MET A CE 1 ATOM 1324 N N . ARG A 1 176 ? 23.516 6.059 -0.370 1.00 121.79 ? 174 ARG A N 1 ATOM 1325 C CA . ARG A 1 176 ? 23.056 7.062 -1.343 1.00 124.74 ? 174 ARG A CA 1 ATOM 1326 C C . ARG A 1 176 ? 23.891 7.030 -2.616 1.00 121.39 ? 174 ARG A C 1 ATOM 1327 O O . ARG A 1 176 ? 23.610 6.261 -3.540 1.00 116.74 ? 174 ARG A O 1 ATOM 1328 C CB . ARG A 1 176 ? 23.090 8.471 -0.737 1.00 131.82 ? 174 ARG A CB 1 ATOM 1329 C CG . ARG A 1 176 ? 22.180 8.650 0.461 1.00 135.99 ? 174 ARG A CG 1 ATOM 1330 C CD . ARG A 1 176 ? 22.144 10.095 0.911 1.00 143.76 ? 174 ARG A CD 1 ATOM 1331 N NE . ARG A 1 176 ? 21.399 10.253 2.156 1.00 148.95 ? 174 ARG A NE 1 ATOM 1332 C CZ . ARG A 1 176 ? 21.080 11.423 2.704 1.00 156.10 ? 174 ARG A CZ 1 ATOM 1333 N NH1 . ARG A 1 176 ? 21.433 12.563 2.122 1.00 160.47 ? 174 ARG A NH1 1 ATOM 1334 N NH2 . ARG A 1 176 ? 20.398 11.451 3.840 1.00 159.54 ? 174 ARG A NH2 1 ATOM 1335 N N . SER A 1 177 ? 24.923 7.869 -2.650 1.00 124.09 ? 175 SER A N 1 ATOM 1336 C CA . SER A 1 177 ? 25.833 7.951 -3.801 1.00 121.51 ? 175 SER A CA 1 ATOM 1337 C C . SER A 1 177 ? 26.838 6.797 -3.779 1.00 115.64 ? 175 SER A C 1 ATOM 1338 O O . SER A 1 177 ? 28.052 7.004 -3.685 1.00 115.69 ? 175 SER A O 1 ATOM 1339 C CB . SER A 1 177 ? 26.569 9.298 -3.818 1.00 126.66 ? 175 SER A CB 1 ATOM 1340 O OG . SER A 1 177 ? 25.656 10.382 -3.888 1.00 133.22 ? 175 SER A OG 1 ATOM 1341 N N . GLY A 1 178 ? 26.299 5.586 -3.895 1.00 110.81 ? 176 GLY A N 1 ATOM 1342 C CA . GLY A 1 178 ? 27.030 4.345 -3.638 1.00 105.06 ? 176 GLY A CA 1 ATOM 1343 C C . GLY A 1 178 ? 28.254 4.074 -4.490 1.00 101.07 ? 176 GLY A C 1 ATOM 1344 O O . GLY A 1 178 ? 29.121 3.296 -4.096 1.00 98.52 ? 176 GLY A O 1 ATOM 1345 N N . LYS A 1 179 ? 28.328 4.716 -5.651 1.00 100.62 ? 177 LYS A N 1 ATOM 1346 C CA . LYS A 1 179 ? 29.424 4.473 -6.602 1.00 96.35 ? 177 LYS A CA 1 ATOM 1347 C C . LYS A 1 179 ? 30.725 5.059 -6.093 1.00 95.43 ? 177 LYS A C 1 ATOM 1348 O O . LYS A 1 179 ? 30.772 6.222 -5.716 1.00 100.30 ? 177 LYS A O 1 ATOM 1349 C CB . LYS A 1 179 ? 29.101 5.071 -7.975 1.00 98.24 ? 177 LYS A CB 1 ATOM 1350 C CG . LYS A 1 179 ? 27.978 4.367 -8.723 1.00 99.29 ? 177 LYS A CG 1 ATOM 1351 C CD . LYS A 1 179 ? 27.787 4.982 -10.107 1.00 104.82 ? 177 LYS A CD 1 ATOM 1352 C CE . LYS A 1 179 ? 27.092 4.017 -11.057 1.00 103.34 ? 177 LYS A CE 1 ATOM 1353 N NZ . LYS A 1 179 ? 27.279 4.409 -12.481 1.00 104.49 ? 177 LYS A NZ 1 ATOM 1354 N N . PHE A 1 180 ? 31.775 4.244 -6.083 1.00 89.44 ? 178 PHE A N 1 ATOM 1355 C CA . PHE A 1 180 ? 33.105 4.708 -5.678 1.00 90.20 ? 178 PHE A CA 1 ATOM 1356 C C . PHE A 1 180 ? 34.232 4.198 -6.548 1.00 86.13 ? 178 PHE A C 1 ATOM 1357 O O . PHE A 1 180 ? 34.557 3.013 -6.551 1.00 82.20 ? 178 PHE A O 1 ATOM 1358 C CB . PHE A 1 180 ? 33.426 4.323 -4.237 1.00 91.16 ? 178 PHE A CB 1 ATOM 1359 C CG . PHE A 1 180 ? 34.824 4.695 -3.821 1.00 94.77 ? 178 PHE A CG 1 ATOM 1360 C CD1 . PHE A 1 180 ? 35.128 6.003 -3.461 1.00 100.27 ? 178 PHE A CD1 1 ATOM 1361 C CD2 . PHE A 1 180 ? 35.845 3.753 -3.817 1.00 92.20 ? 178 PHE A CD2 1 ATOM 1362 C CE1 . PHE A 1 180 ? 36.417 6.362 -3.088 1.00 102.73 ? 178 PHE A CE1 1 ATOM 1363 C CE2 . PHE A 1 180 ? 37.140 4.113 -3.440 1.00 96.11 ? 178 PHE A CE2 1 ATOM 1364 C CZ . PHE A 1 180 ? 37.422 5.418 -3.078 1.00 97.73 ? 178 PHE A CZ 1 ATOM 1365 N N . GLN A 1 181 ? 34.859 5.131 -7.246 1.00 88.41 ? 179 GLN A N 1 ATOM 1366 C CA . GLN A 1 181 ? 35.971 4.817 -8.128 1.00 86.20 ? 179 GLN A CA 1 ATOM 1367 C C . GLN A 1 181 ? 37.284 5.199 -7.481 1.00 88.35 ? 179 GLN A C 1 ATOM 1368 O O . GLN A 1 181 ? 37.460 6.306 -6.974 1.00 92.22 ? 179 GLN A O 1 ATOM 1369 C CB . GLN A 1 181 ? 35.780 5.498 -9.477 1.00 87.20 ? 179 GLN A CB 1 ATOM 1370 C CG . GLN A 1 181 ? 34.396 5.236 -10.043 1.00 87.02 ? 179 GLN A CG 1 ATOM 1371 C CD . GLN A 1 181 ? 34.336 5.376 -11.540 1.00 88.53 ? 179 GLN A CD 1 ATOM 1372 O OE1 . GLN A 1 181 ? 35.062 6.175 -12.134 1.00 93.25 ? 179 GLN A OE1 1 ATOM 1373 N NE2 . GLN A 1 181 ? 33.467 4.592 -12.167 1.00 87.01 ? 179 GLN A NE2 1 ATOM 1374 N N . SER A 1 182 ? 38.191 4.234 -7.511 1.00 86.00 ? 180 SER A N 1 ATOM 1375 C CA . SER A 1 182 ? 39.422 4.249 -6.727 1.00 88.99 ? 180 SER A CA 1 ATOM 1376 C C . SER A 1 182 ? 39.933 5.644 -6.432 1.00 94.17 ? 180 SER A C 1 ATOM 1377 O O . SER A 1 182 ? 40.070 6.042 -5.275 1.00 98.45 ? 180 SER A O 1 ATOM 1378 C CB . SER A 1 182 ? 40.513 3.470 -7.460 1.00 86.51 ? 180 SER A CB 1 ATOM 1379 O OG . SER A 1 182 ? 41.714 3.434 -6.710 1.00 91.05 ? 180 SER A OG 1 ATOM 1380 N N . LEU A 1 183 ? 40.220 6.369 -7.502 1.00 94.68 ? 181 LEU A N 1 ATOM 1381 C CA . LEU A 1 183 ? 40.862 7.689 -7.424 1.00 99.65 ? 181 LEU A CA 1 ATOM 1382 C C . LEU A 1 183 ? 42.318 7.539 -7.001 1.00 100.48 ? 181 LEU A C 1 ATOM 1383 O O . LEU A 1 183 ? 43.039 8.517 -6.827 1.00 104.62 ? 181 LEU A O 1 ATOM 1384 C CB . LEU A 1 183 ? 40.130 8.628 -6.462 1.00 103.91 ? 181 LEU A CB 1 ATOM 1385 C CG . LEU A 1 183 ? 40.059 10.051 -7.031 1.00 109.61 ? 181 LEU A CG 1 ATOM 1386 C CD1 . LEU A 1 183 ? 38.853 10.174 -7.959 1.00 106.81 ? 181 LEU A CD1 1 ATOM 1387 C CD2 . LEU A 1 183 ? 40.021 11.135 -5.949 1.00 115.93 ? 181 LEU A CD2 1 ATOM 1388 N N . GLY A 1 184 ? 42.730 6.292 -6.836 1.00 96.96 ? 182 GLY A N 1 ATOM 1389 C CA . GLY A 1 184 ? 44.121 5.972 -6.558 1.00 98.20 ? 182 GLY A CA 1 ATOM 1390 C C . GLY A 1 184 ? 44.852 5.640 -7.838 1.00 95.69 ? 182 GLY A C 1 ATOM 1391 O O . GLY A 1 184 ? 45.162 6.520 -8.632 1.00 97.89 ? 182 GLY A O 1 ATOM 1392 N N . ARG A 1 185 ? 45.120 4.355 -8.039 1.00 91.37 ? 183 ARG A N 1 ATOM 1393 C CA . ARG A 1 185 ? 45.816 3.908 -9.238 1.00 88.60 ? 183 ARG A CA 1 ATOM 1394 C C . ARG A 1 185 ? 44.787 3.719 -10.326 1.00 84.31 ? 183 ARG A C 1 ATOM 1395 O O . ARG A 1 185 ? 45.118 3.421 -11.472 1.00 83.76 ? 183 ARG A O 1 ATOM 1396 C CB . ARG A 1 185 ? 46.565 2.601 -8.999 1.00 86.67 ? 183 ARG A CB 1 ATOM 1397 C CG . ARG A 1 185 ? 47.648 2.332 -10.033 1.00 88.01 ? 183 ARG A CG 1 ATOM 1398 C CD . ARG A 1 185 ? 48.419 1.081 -9.686 1.00 90.02 ? 183 ARG A CD 1 ATOM 1399 N NE . ARG A 1 185 ? 49.016 1.172 -8.354 1.00 96.30 ? 183 ARG A NE 1 ATOM 1400 C CZ . ARG A 1 185 ? 49.606 0.162 -7.719 1.00 97.46 ? 183 ARG A CZ 1 ATOM 1401 N NH1 . ARG A 1 185 ? 49.688 -1.035 -8.284 1.00 93.87 ? 183 ARG A NH1 1 ATOM 1402 N NH2 . ARG A 1 185 ? 50.116 0.350 -6.507 1.00 101.89 ? 183 ARG A NH2 1 ATOM 1403 N N . PHE A 1 186 ? 43.529 3.889 -9.950 1.00 82.30 ? 184 PHE A N 1 ATOM 1404 C CA . PHE A 1 186 ? 42.435 3.737 -10.898 1.00 78.57 ? 184 PHE A CA 1 ATOM 1405 C C . PHE A 1 186 ? 41.629 5.016 -10.923 1.00 82.32 ? 184 PHE A C 1 ATOM 1406 O O . PHE A 1 186 ? 40.409 5.024 -10.737 1.00 82.55 ? 184 PHE A O 1 ATOM 1407 C CB . PHE A 1 186 ? 41.592 2.508 -10.557 1.00 74.53 ? 184 PHE A CB 1 ATOM 1408 C CG . PHE A 1 186 ? 42.419 1.316 -10.177 1.00 67.08 ? 184 PHE A CG 1 ATOM 1409 C CD1 . PHE A 1 186 ? 43.052 0.565 -11.146 1.00 59.85 ? 184 PHE A CD1 1 ATOM 1410 C CD2 . PHE A 1 186 ? 42.592 0.965 -8.853 1.00 62.11 ? 184 PHE A CD2 1 ATOM 1411 C CE1 . PHE A 1 186 ? 43.832 -0.517 -10.804 1.00 57.35 ? 184 PHE A CE1 1 ATOM 1412 C CE2 . PHE A 1 186 ? 43.369 -0.120 -8.510 1.00 60.60 ? 184 PHE A CE2 1 ATOM 1413 C CZ . PHE A 1 186 ? 43.991 -0.860 -9.489 1.00 57.07 ? 184 PHE A CZ 1 ATOM 1414 N N . ARG A 1 187 ? 42.376 6.095 -11.148 1.00 85.75 ? 185 ARG A N 1 ATOM 1415 C CA . ARG A 1 187 ? 41.834 7.439 -11.371 1.00 88.42 ? 185 ARG A CA 1 ATOM 1416 C C . ARG A 1 187 ? 41.026 7.492 -12.652 1.00 85.56 ? 185 ARG A C 1 ATOM 1417 O O . ARG A 1 187 ? 41.582 7.457 -13.744 1.00 85.21 ? 185 ARG A O 1 ATOM 1418 C CB . ARG A 1 187 ? 42.966 8.471 -11.494 1.00 92.93 ? 185 ARG A CB 1 ATOM 1419 C CG . ARG A 1 187 ? 43.792 8.711 -10.235 1.00 96.45 ? 185 ARG A CG 1 ATOM 1420 C CD . ARG A 1 187 ? 45.099 9.439 -10.559 1.00 100.07 ? 185 ARG A CD 1 ATOM 1421 N NE . ARG A 1 187 ? 45.806 9.897 -9.365 1.00 106.97 ? 185 ARG A NE 1 ATOM 1422 C CZ . ARG A 1 187 ? 46.862 10.707 -9.385 1.00 116.87 ? 185 ARG A CZ 1 ATOM 1423 N NH1 . ARG A 1 187 ? 47.342 11.159 -10.537 1.00 120.15 ? 185 ARG A NH1 1 ATOM 1424 N NH2 . ARG A 1 187 ? 47.437 11.082 -8.251 1.00 122.44 ? 185 ARG A NH2 1 ATOM 1425 N N . ASN A 1 188 ? 39.711 7.576 -12.501 1.00 84.08 ? 186 ASN A N 1 ATOM 1426 C CA . ASN A 1 188 ? 38.809 7.817 -13.629 1.00 83.20 ? 186 ASN A CA 1 ATOM 1427 C C . ASN A 1 188 ? 39.032 6.875 -14.809 1.00 78.09 ? 186 ASN A C 1 ATOM 1428 O O . ASN A 1 188 ? 38.815 7.252 -15.967 1.00 77.98 ? 186 ASN A O 1 ATOM 1429 C CB . ASN A 1 188 ? 38.960 9.255 -14.119 1.00 87.85 ? 186 ASN A CB 1 ATOM 1430 C CG . ASN A 1 188 ? 39.024 10.247 -12.985 1.00 97.11 ? 186 ASN A CG 1 ATOM 1431 O OD1 . ASN A 1 188 ? 39.764 10.059 -12.018 1.00 103.66 ? 186 ASN A OD1 1 ATOM 1432 N ND2 . ASN A 1 188 ? 38.250 11.317 -13.095 1.00 107.44 ? 186 ASN A ND2 1 ATOM 1433 N N . ARG A 1 189 ? 39.485 5.660 -14.519 1.00 72.61 ? 187 ARG A N 1 ATOM 1434 C CA . ARG A 1 189 ? 39.665 4.670 -15.577 1.00 67.72 ? 187 ARG A CA 1 ATOM 1435 C C . ARG A 1 189 ? 39.184 3.299 -15.157 1.00 61.81 ? 187 ARG A C 1 ATOM 1436 O O . ARG A 1 189 ? 39.817 2.277 -15.411 1.00 57.85 ? 187 ARG A O 1 ATOM 1437 C CB . ARG A 1 189 ? 41.106 4.655 -16.086 1.00 68.38 ? 187 ARG A CB 1 ATOM 1438 C CG . ARG A 1 189 ? 42.176 4.389 -15.085 1.00 67.70 ? 187 ARG A CG 1 ATOM 1439 C CD . ARG A 1 189 ? 43.515 4.514 -15.815 1.00 66.82 ? 187 ARG A CD 1 ATOM 1440 N NE . ARG A 1 189 ? 44.636 4.031 -15.026 1.00 69.54 ? 187 ARG A NE 1 ATOM 1441 C CZ . ARG A 1 189 ? 44.906 2.747 -14.825 1.00 68.58 ? 187 ARG A CZ 1 ATOM 1442 N NH1 . ARG A 1 189 ? 44.133 1.814 -15.355 1.00 67.70 ? 187 ARG A NH1 1 ATOM 1443 N NH2 . ARG A 1 189 ? 45.946 2.400 -14.088 1.00 70.28 ? 187 ARG A NH2 1 ATOM 1444 N N . VAL A 1 190 ? 38.023 3.318 -14.523 1.00 60.38 ? 188 VAL A N 1 ATOM 1445 C CA . VAL A 1 190 ? 37.367 2.112 -14.059 1.00 55.89 ? 188 VAL A CA 1 ATOM 1446 C C . VAL A 1 190 ? 35.898 2.379 -13.783 1.00 56.92 ? 188 VAL A C 1 ATOM 1447 O O . VAL A 1 190 ? 35.556 3.291 -13.043 1.00 59.71 ? 188 VAL A O 1 ATOM 1448 C CB . VAL A 1 190 ? 38.017 1.606 -12.782 1.00 54.03 ? 188 VAL A CB 1 ATOM 1449 C CG1 . VAL A 1 190 ? 37.806 2.606 -11.654 1.00 60.91 ? 188 VAL A CG1 1 ATOM 1450 C CG2 . VAL A 1 190 ? 37.439 0.299 -12.405 1.00 52.33 ? 188 VAL A CG2 1 ATOM 1451 N N . ASP A 1 191 ? 35.034 1.579 -14.391 1.00 56.19 ? 189 ASP A N 1 ATOM 1452 C CA . ASP A 1 191 ? 33.587 1.766 -14.254 1.00 58.38 ? 189 ASP A CA 1 ATOM 1453 C C . ASP A 1 191 ? 32.761 0.540 -14.637 1.00 55.68 ? 189 ASP A C 1 ATOM 1454 O O . ASP A 1 191 ? 33.207 -0.324 -15.383 1.00 55.87 ? 189 ASP A O 1 ATOM 1455 C CB . ASP A 1 191 ? 33.134 2.963 -15.086 1.00 61.57 ? 189 ASP A CB 1 ATOM 1456 C CG . ASP A 1 191 ? 31.770 3.473 -14.666 1.00 68.21 ? 189 ASP A CG 1 ATOM 1457 O OD1 . ASP A 1 191 ? 31.673 4.657 -14.281 1.00 78.29 ? 189 ASP A OD1 1 ATOM 1458 O OD2 . ASP A 1 191 ? 30.794 2.692 -14.699 1.00 72.72 ? 189 ASP A OD2 1 ATOM 1459 N N . LEU A 1 192 ? 31.542 0.499 -14.115 1.00 55.90 ? 190 LEU A N 1 ATOM 1460 C CA . LEU A 1 192 ? 30.612 -0.609 -14.353 1.00 53.49 ? 190 LEU A CA 1 ATOM 1461 C C . LEU A 1 192 ? 30.103 -0.623 -15.781 1.00 54.72 ? 190 LEU A C 1 ATOM 1462 O O . LEU A 1 192 ? 29.499 0.341 -16.254 1.00 55.27 ? 190 LEU A O 1 ATOM 1463 C CB . LEU A 1 192 ? 29.409 -0.526 -13.418 1.00 54.65 ? 190 LEU A CB 1 ATOM 1464 C CG . LEU A 1 192 ? 29.699 -0.651 -11.930 1.00 52.01 ? 190 LEU A CG 1 ATOM 1465 C CD1 . LEU A 1 192 ? 28.434 -0.422 -11.143 1.00 51.53 ? 190 LEU A CD1 1 ATOM 1466 C CD2 . LEU A 1 192 ? 30.271 -2.015 -11.640 1.00 51.91 ? 190 LEU A CD2 1 ATOM 1467 N N . THR A 1 193 ? 30.333 -1.757 -16.436 1.00 53.12 ? 191 THR A N 1 ATOM 1468 C CA . THR A 1 193 ? 29.959 -1.954 -17.830 1.00 53.82 ? 191 THR A CA 1 ATOM 1469 C C . THR A 1 193 ? 28.484 -2.267 -17.904 1.00 54.51 ? 191 THR A C 1 ATOM 1470 O O . THR A 1 193 ? 27.841 -2.067 -18.930 1.00 55.95 ? 191 THR A O 1 ATOM 1471 C CB . THR A 1 193 ? 30.736 -3.114 -18.452 1.00 51.06 ? 191 THR A CB 1 ATOM 1472 O OG1 . THR A 1 193 ? 30.564 -4.296 -17.659 1.00 52.90 ? 191 THR A OG1 1 ATOM 1473 C CG2 . THR A 1 193 ? 32.195 -2.792 -18.503 1.00 55.25 ? 191 THR A CG2 1 ATOM 1474 N N . GLY A 1 194 ? 27.954 -2.763 -16.796 1.00 54.61 ? 192 GLY A N 1 ATOM 1475 C CA . GLY A 1 194 ? 26.551 -3.140 -16.723 1.00 56.85 ? 192 GLY A CA 1 ATOM 1476 C C . GLY A 1 194 ? 25.862 -2.391 -15.617 1.00 60.62 ? 192 GLY A C 1 ATOM 1477 O O . GLY A 1 194 ? 26.359 -1.373 -15.132 1.00 63.47 ? 192 GLY A O 1 ATOM 1478 N N . ASP A 1 195 ? 24.710 -2.899 -15.211 1.00 62.03 ? 193 ASP A N 1 ATOM 1479 C CA . ASP A 1 195 ? 23.972 -2.285 -14.112 1.00 65.49 ? 193 ASP A CA 1 ATOM 1480 C C . ASP A 1 195 ? 23.635 -3.298 -13.043 1.00 63.62 ? 193 ASP A C 1 ATOM 1481 O O . ASP A 1 195 ? 23.409 -4.478 -13.318 1.00 61.92 ? 193 ASP A O 1 ATOM 1482 C CB . ASP A 1 195 ? 22.714 -1.546 -14.602 1.00 70.40 ? 193 ASP A CB 1 ATOM 1483 C CG . ASP A 1 195 ? 21.871 -2.374 -15.544 1.00 72.18 ? 193 ASP A CG 1 ATOM 1484 O OD1 . ASP A 1 195 ? 22.111 -3.593 -15.619 1.00 71.23 ? 193 ASP A OD1 1 ATOM 1485 O OD2 . ASP A 1 195 ? 20.973 -1.805 -16.210 1.00 79.60 ? 193 ASP A OD2 1 ATOM 1486 N N . ILE A 1 196 ? 23.619 -2.814 -11.811 1.00 64.72 ? 194 ILE A N 1 ATOM 1487 C CA . ILE A 1 196 ? 23.432 -3.673 -10.654 1.00 63.00 ? 194 ILE A CA 1 ATOM 1488 C C . ILE A 1 196 ? 21.975 -4.041 -10.542 1.00 62.94 ? 194 ILE A C 1 ATOM 1489 O O . ILE A 1 196 ? 21.624 -5.030 -9.913 1.00 61.35 ? 194 ILE A O 1 ATOM 1490 C CB . ILE A 1 196 ? 23.838 -2.989 -9.346 1.00 65.29 ? 194 ILE A CB 1 ATOM 1491 C CG1 . ILE A 1 196 ? 25.324 -2.625 -9.351 1.00 66.16 ? 194 ILE A CG1 1 ATOM 1492 C CG2 . ILE A 1 196 ? 23.532 -3.918 -8.174 1.00 67.13 ? 194 ILE A CG2 1 ATOM 1493 C CD1 . ILE A 1 196 ? 26.234 -3.762 -8.890 1.00 65.78 ? 194 ILE A CD1 1 ATOM 1494 N N . SER A 1 197 ? 21.127 -3.236 -11.164 1.00 65.07 ? 195 SER A N 1 ATOM 1495 C CA . SER A 1 197 ? 19.694 -3.504 -11.145 1.00 66.56 ? 195 SER A CA 1 ATOM 1496 C C . SER A 1 197 ? 19.444 -4.850 -11.807 1.00 63.41 ? 195 SER A C 1 ATOM 1497 O O . SER A 1 197 ? 18.411 -5.484 -11.581 1.00 63.76 ? 195 SER A O 1 ATOM 1498 C CB . SER A 1 197 ? 18.896 -2.386 -11.830 1.00 70.80 ? 195 SER A CB 1 ATOM 1499 O OG . SER A 1 197 ? 19.436 -2.042 -13.095 1.00 72.82 ? 195 SER A OG 1 ATOM 1500 N N . ARG A 1 198 ? 20.405 -5.277 -12.621 1.00 60.75 ? 196 ARG A N 1 ATOM 1501 C CA . ARG A 1 198 ? 20.357 -6.590 -13.267 1.00 59.06 ? 196 ARG A CA 1 ATOM 1502 C C . ARG A 1 198 ? 21.380 -7.499 -12.612 1.00 54.36 ? 196 ARG A C 1 ATOM 1503 O O . ARG A 1 198 ? 21.856 -8.469 -13.201 1.00 53.12 ? 196 ARG A O 1 ATOM 1504 C CB . ARG A 1 198 ? 20.597 -6.488 -14.772 1.00 59.44 ? 196 ARG A CB 1 ATOM 1505 C CG . ARG A 1 198 ? 19.381 -5.997 -15.559 1.00 67.54 ? 196 ARG A CG 1 ATOM 1506 C CD . ARG A 1 198 ? 19.733 -5.728 -17.027 1.00 75.95 ? 196 ARG A CD 1 ATOM 1507 N NE . ARG A 1 198 ? 20.732 -6.665 -17.550 1.00 77.77 ? 196 ARG A NE 1 ATOM 1508 C CZ . ARG A 1 198 ? 21.010 -6.829 -18.841 1.00 77.43 ? 196 ARG A CZ 1 ATOM 1509 N NH1 . ARG A 1 198 ? 20.364 -6.129 -19.765 1.00 78.44 ? 196 ARG A NH1 1 ATOM 1510 N NH2 . ARG A 1 198 ? 21.940 -7.705 -19.203 1.00 75.88 ? 196 ARG A NH2 1 ATOM 1511 N N . ASN A 1 199 ? 21.688 -7.157 -11.369 1.00 52.69 ? 197 ASN A N 1 ATOM 1512 C CA . ASN A 1 199 ? 22.519 -7.975 -10.492 1.00 49.36 ? 197 ASN A CA 1 ATOM 1513 C C . ASN A 1 199 ? 23.883 -8.289 -11.080 1.00 44.98 ? 197 ASN A C 1 ATOM 1514 O O . ASN A 1 199 ? 24.449 -9.346 -10.842 1.00 42.00 ? 197 ASN A O 1 ATOM 1515 C CB . ASN A 1 199 ? 21.780 -9.260 -10.152 1.00 49.75 ? 197 ASN A CB 1 ATOM 1516 C CG . ASN A 1 199 ? 20.335 -9.008 -9.776 1.00 55.13 ? 197 ASN A CG 1 ATOM 1517 O OD1 . ASN A 1 199 ? 20.042 -8.472 -8.705 1.00 59.21 ? 197 ASN A OD1 1 ATOM 1518 N ND2 . ASN A 1 199 ? 19.422 -9.387 -10.661 1.00 62.64 ? 197 ASN A ND2 1 ATOM 1519 N N . ASP A 1 200 ? 24.398 -7.345 -11.853 1.00 44.79 ? 198 ASP A N 1 ATOM 1520 C CA . ASP A 1 200 ? 25.724 -7.468 -12.448 1.00 42.89 ? 198 ASP A CA 1 ATOM 1521 C C . ASP A 1 200 ? 26.682 -6.421 -11.927 1.00 42.99 ? 198 ASP A C 1 ATOM 1522 O O . ASP A 1 200 ? 26.369 -5.228 -11.895 1.00 46.21 ? 198 ASP A O 1 ATOM 1523 C CB . ASP A 1 200 ? 25.632 -7.340 -13.963 1.00 44.32 ? 198 ASP A CB 1 ATOM 1524 C CG . ASP A 1 200 ? 26.919 -7.717 -14.654 1.00 44.17 ? 198 ASP A CG 1 ATOM 1525 O OD1 . ASP A 1 200 ? 27.890 -8.070 -13.951 1.00 46.43 ? 198 ASP A OD1 1 ATOM 1526 O OD2 . ASP A 1 200 ? 26.958 -7.658 -15.899 1.00 48.60 ? 198 ASP A OD2 1 ATOM 1527 N N . GLY A 1 201 ? 27.861 -6.889 -11.542 1.00 40.57 ? 199 GLY A N 1 ATOM 1528 C CA . GLY A 1 201 ? 28.886 -6.034 -10.966 1.00 41.72 ? 199 GLY A CA 1 ATOM 1529 C C . GLY A 1 201 ? 30.178 -6.040 -11.760 1.00 41.49 ? 199 GLY A C 1 ATOM 1530 O O . GLY A 1 201 ? 31.256 -5.802 -11.220 1.00 42.92 ? 199 GLY A O 1 ATOM 1531 N N . SER A 1 202 ? 30.075 -6.314 -13.051 1.00 40.54 ? 200 SER A N 1 ATOM 1532 C CA . SER A 1 202 ? 31.261 -6.307 -13.909 1.00 38.83 ? 200 SER A CA 1 ATOM 1533 C C . SER A 1 202 ? 31.776 -4.892 -14.085 1.00 39.92 ? 200 SER A C 1 ATOM 1534 O O . SER A 1 202 ? 30.995 -3.938 -14.189 1.00 42.84 ? 200 SER A O 1 ATOM 1535 C CB . SER A 1 202 ? 30.962 -6.941 -15.270 1.00 37.40 ? 200 SER A CB 1 ATOM 1536 O OG . SER A 1 202 ? 30.709 -8.326 -15.121 1.00 35.27 ? 200 SER A OG 1 ATOM 1537 N N . ILE A 1 203 ? 33.097 -4.771 -14.107 1.00 38.73 ? 201 ILE A N 1 ATOM 1538 C CA . ILE A 1 203 ? 33.758 -3.494 -14.395 1.00 39.66 ? 201 ILE A CA 1 ATOM 1539 C C . ILE A 1 203 ? 34.778 -3.621 -15.514 1.00 39.47 ? 201 ILE A C 1 ATOM 1540 O O . ILE A 1 203 ? 35.243 -4.708 -15.835 1.00 37.72 ? 201 ILE A O 1 ATOM 1541 C CB . ILE A 1 203 ? 34.476 -2.921 -13.161 1.00 40.72 ? 201 ILE A CB 1 ATOM 1542 C CG1 . ILE A 1 203 ? 35.652 -3.813 -12.745 1.00 37.04 ? 201 ILE A CG1 1 ATOM 1543 C CG2 . ILE A 1 203 ? 33.505 -2.759 -12.007 1.00 39.99 ? 201 ILE A CG2 1 ATOM 1544 C CD1 . ILE A 1 203 ? 36.609 -3.130 -11.767 1.00 33.96 ? 201 ILE A CD1 1 ATOM 1545 N N . LYS A 1 204 ? 35.107 -2.487 -16.110 1.00 42.08 ? 202 LYS A N 1 ATOM 1546 C CA . LYS A 1 204 ? 36.208 -2.415 -17.073 1.00 42.87 ? 202 LYS A CA 1 ATOM 1547 C C . LYS A 1 204 ? 37.291 -1.500 -16.561 1.00 42.77 ? 202 LYS A C 1 ATOM 1548 O O . LYS A 1 204 ? 37.014 -0.510 -15.912 1.00 43.36 ? 202 LYS A O 1 ATOM 1549 C CB . LYS A 1 204 ? 35.741 -1.874 -18.418 1.00 45.49 ? 202 LYS A CB 1 ATOM 1550 C CG . LYS A 1 204 ? 35.417 -0.396 -18.392 1.00 49.24 ? 202 LYS A CG 1 ATOM 1551 C CD . LYS A 1 204 ? 35.270 0.153 -19.789 1.00 59.46 ? 202 LYS A CD 1 ATOM 1552 C CE . LYS A 1 204 ? 34.275 1.301 -19.822 1.00 66.17 ? 202 LYS A CE 1 ATOM 1553 N NZ . LYS A 1 204 ? 32.907 0.828 -19.458 1.00 69.20 ? 202 LYS A NZ 1 ATOM 1554 N N . LEU A 1 205 ? 38.524 -1.864 -16.879 1.00 41.94 ? 203 LEU A N 1 ATOM 1555 C CA . LEU A 1 205 ? 39.696 -1.062 -16.585 1.00 43.51 ? 203 LEU A CA 1 ATOM 1556 C C . LEU A 1 205 ? 40.239 -0.543 -17.907 1.00 45.49 ? 203 LEU A C 1 ATOM 1557 O O . LEU A 1 205 ? 40.593 -1.330 -18.791 1.00 42.90 ? 203 LEU A O 1 ATOM 1558 C CB . LEU A 1 205 ? 40.743 -1.900 -15.859 1.00 41.13 ? 203 LEU A CB 1 ATOM 1559 C CG . LEU A 1 205 ? 41.852 -1.081 -15.204 1.00 49.08 ? 203 LEU A CG 1 ATOM 1560 C CD1 . LEU A 1 205 ? 41.299 -0.074 -14.175 1.00 56.35 ? 203 LEU A CD1 1 ATOM 1561 C CD2 . LEU A 1 205 ? 42.868 -2.000 -14.542 1.00 52.83 ? 203 LEU A CD2 1 ATOM 1562 N N . GLN A 1 206 ? 40.320 0.785 -18.022 1.00 49.31 ? 204 GLN A N 1 ATOM 1563 C CA . GLN A 1 206 ? 40.397 1.433 -19.328 1.00 51.23 ? 204 GLN A CA 1 ATOM 1564 C C . GLN A 1 206 ? 41.769 1.407 -19.941 1.00 52.67 ? 204 GLN A C 1 ATOM 1565 O O . GLN A 1 206 ? 41.938 0.994 -21.082 1.00 55.70 ? 204 GLN A O 1 ATOM 1566 C CB . GLN A 1 206 ? 39.843 2.848 -19.286 1.00 54.12 ? 204 GLN A CB 1 ATOM 1567 C CG . GLN A 1 206 ? 38.369 2.840 -18.993 1.00 54.37 ? 204 GLN A CG 1 ATOM 1568 C CD . GLN A 1 206 ? 37.602 3.874 -19.758 1.00 61.49 ? 204 GLN A CD 1 ATOM 1569 O OE1 . GLN A 1 206 ? 37.904 5.064 -19.694 1.00 68.87 ? 204 GLN A OE1 1 ATOM 1570 N NE2 . GLN A 1 206 ? 36.579 3.430 -20.481 1.00 62.87 ? 204 GLN A NE2 1 ATOM 1571 N N . THR A 1 207 ? 42.761 1.854 -19.211 1.00 53.02 ? 205 THR A N 1 ATOM 1572 C CA . THR A 1 207 ? 44.078 1.913 -19.811 1.00 54.79 ? 205 THR A CA 1 ATOM 1573 C C . THR A 1 207 ? 45.008 1.096 -18.989 1.00 54.46 ? 205 THR A C 1 ATOM 1574 O O . THR A 1 207 ? 45.575 1.556 -17.994 1.00 57.13 ? 205 THR A O 1 ATOM 1575 C CB . THR A 1 207 ? 44.600 3.347 -19.924 1.00 59.75 ? 205 THR A CB 1 ATOM 1576 O OG1 . THR A 1 207 ? 43.834 4.048 -20.910 1.00 58.72 ? 205 THR A OG1 1 ATOM 1577 C CG2 . THR A 1 207 ? 46.079 3.353 -20.316 1.00 60.47 ? 205 THR A CG2 1 ATOM 1578 N N . VAL A 1 208 ? 45.145 -0.143 -19.407 1.00 52.81 ? 206 VAL A N 1 ATOM 1579 C CA . VAL A 1 208 ? 45.955 -1.083 -18.659 1.00 52.47 ? 206 VAL A CA 1 ATOM 1580 C C . VAL A 1 208 ? 47.421 -0.653 -18.729 1.00 55.37 ? 206 VAL A C 1 ATOM 1581 O O . VAL A 1 208 ? 47.969 -0.403 -19.800 1.00 55.13 ? 206 VAL A O 1 ATOM 1582 C CB . VAL A 1 208 ? 45.721 -2.527 -19.122 1.00 49.22 ? 206 VAL A CB 1 ATOM 1583 C CG1 . VAL A 1 208 ? 46.844 -3.426 -18.669 1.00 51.04 ? 206 VAL A CG1 1 ATOM 1584 C CG2 . VAL A 1 208 ? 44.393 -3.001 -18.577 1.00 43.89 ? 206 VAL A CG2 1 ATOM 1585 N N . LYS A 1 209 ? 48.000 -0.501 -17.545 1.00 57.70 ? 207 LYS A N 1 ATOM 1586 C CA . LYS A 1 209 ? 49.406 -0.169 -17.362 1.00 61.97 ? 207 LYS A CA 1 ATOM 1587 C C . LYS A 1 209 ? 50.065 -1.378 -16.735 1.00 63.07 ? 207 LYS A C 1 ATOM 1588 O O . LYS A 1 209 ? 49.373 -2.258 -16.226 1.00 62.72 ? 207 LYS A O 1 ATOM 1589 C CB . LYS A 1 209 ? 49.556 1.022 -16.410 1.00 64.94 ? 207 LYS A CB 1 ATOM 1590 C CG . LYS A 1 209 ? 48.508 2.111 -16.581 1.00 66.04 ? 207 LYS A CG 1 ATOM 1591 C CD . LYS A 1 209 ? 48.780 3.283 -15.657 1.00 71.01 ? 207 LYS A CD 1 ATOM 1592 C CE . LYS A 1 209 ? 47.883 4.462 -15.969 1.00 72.59 ? 207 LYS A CE 1 ATOM 1593 N NZ . LYS A 1 209 ? 47.697 5.343 -14.784 1.00 79.47 ? 207 LYS A NZ 1 ATOM 1594 N N . GLU A 1 210 ? 51.391 -1.427 -16.761 1.00 66.62 ? 208 GLU A N 1 ATOM 1595 C CA . GLU A 1 210 ? 52.119 -2.485 -16.050 1.00 69.41 ? 208 GLU A CA 1 ATOM 1596 C C . GLU A 1 210 ? 51.815 -2.427 -14.558 1.00 70.26 ? 208 GLU A C 1 ATOM 1597 O O . GLU A 1 210 ? 51.745 -3.459 -13.884 1.00 70.18 ? 208 GLU A O 1 ATOM 1598 C CB . GLU A 1 210 ? 53.631 -2.376 -16.241 1.00 74.24 ? 208 GLU A CB 1 ATOM 1599 C CG . GLU A 1 210 ? 54.161 -3.023 -17.504 1.00 77.93 ? 208 GLU A CG 1 ATOM 1600 C CD . GLU A 1 210 ? 55.676 -3.191 -17.460 1.00 88.69 ? 208 GLU A CD 1 ATOM 1601 O OE1 . GLU A 1 210 ? 56.199 -3.586 -16.391 1.00 93.37 ? 208 GLU A OE1 1 ATOM 1602 O OE2 . GLU A 1 210 ? 56.346 -2.920 -18.483 1.00 95.23 ? 208 GLU A OE2 1 ATOM 1603 N N . SER A 1 211 ? 51.633 -1.212 -14.054 1.00 71.80 ? 209 SER A N 1 ATOM 1604 C CA . SER A 1 211 ? 51.402 -0.997 -12.623 1.00 73.38 ? 209 SER A CA 1 ATOM 1605 C C . SER A 1 211 ? 50.107 -1.662 -12.153 1.00 70.11 ? 209 SER A C 1 ATOM 1606 O O . SER A 1 211 ? 49.863 -1.767 -10.957 1.00 71.82 ? 209 SER A O 1 ATOM 1607 C CB . SER A 1 211 ? 51.346 0.496 -12.291 1.00 75.91 ? 209 SER A CB 1 ATOM 1608 O OG . SER A 1 211 ? 50.231 1.113 -12.915 1.00 75.57 ? 209 SER A OG 1 ATOM 1609 N N . ASP A 1 212 ? 49.288 -2.114 -13.097 1.00 65.72 ? 210 ASP A N 1 ATOM 1610 C CA . ASP A 1 212 ? 47.967 -2.675 -12.771 1.00 62.42 ? 210 ASP A CA 1 ATOM 1611 C C . ASP A 1 212 ? 48.008 -4.191 -12.608 1.00 59.95 ? 210 ASP A C 1 ATOM 1612 O O . ASP A 1 212 ? 47.002 -4.837 -12.327 1.00 57.34 ? 210 ASP A O 1 ATOM 1613 C CB . ASP A 1 212 ? 46.955 -2.295 -13.849 1.00 60.32 ? 210 ASP A CB 1 ATOM 1614 C CG . ASP A 1 212 ? 46.772 -0.803 -13.957 1.00 63.76 ? 210 ASP A CG 1 ATOM 1615 O OD1 . ASP A 1 212 ? 47.278 -0.084 -13.068 1.00 70.16 ? 210 ASP A OD1 1 ATOM 1616 O OD2 . ASP A 1 212 ? 46.129 -0.345 -14.924 1.00 64.15 ? 210 ASP A OD2 1 ATOM 1617 N N . GLN A 1 213 ? 49.197 -4.742 -12.772 1.00 60.48 ? 211 GLN A N 1 ATOM 1618 C CA . GLN A 1 213 ? 49.391 -6.184 -12.741 1.00 58.12 ? 211 GLN A CA 1 ATOM 1619 C C . GLN A 1 213 ? 49.273 -6.738 -11.329 1.00 59.06 ? 211 GLN A C 1 ATOM 1620 O O . GLN A 1 213 ? 50.135 -6.516 -10.483 1.00 62.91 ? 211 GLN A O 1 ATOM 1621 C CB . GLN A 1 213 ? 50.756 -6.515 -13.321 1.00 60.34 ? 211 GLN A CB 1 ATOM 1622 C CG . GLN A 1 213 ? 51.123 -7.963 -13.290 1.00 61.06 ? 211 GLN A CG 1 ATOM 1623 C CD . GLN A 1 213 ? 52.270 -8.245 -14.228 1.00 64.84 ? 211 GLN A CD 1 ATOM 1624 O OE1 . GLN A 1 213 ? 52.065 -8.396 -15.433 1.00 55.33 ? 211 GLN A OE1 1 ATOM 1625 N NE2 . GLN A 1 213 ? 53.491 -8.290 -13.688 1.00 71.24 ? 211 GLN A NE2 1 ATOM 1626 N N . GLY A 1 214 ? 48.196 -7.465 -11.077 1.00 56.11 ? 212 GLY A N 1 ATOM 1627 C CA . GLY A 1 214 ? 47.997 -8.069 -9.765 1.00 56.44 ? 212 GLY A CA 1 ATOM 1628 C C . GLY A 1 214 ? 46.778 -8.950 -9.641 1.00 53.21 ? 212 GLY A C 1 ATOM 1629 O O . GLY A 1 214 ? 46.395 -9.655 -10.574 1.00 51.36 ? 212 GLY A O 1 ATOM 1630 N N . ILE A 1 215 ? 46.175 -8.901 -8.464 1.00 52.82 ? 213 ILE A N 1 ATOM 1631 C CA . ILE A 1 215 ? 44.980 -9.679 -8.196 1.00 50.38 ? 213 ILE A CA 1 ATOM 1632 C C . ILE A 1 215 ? 43.798 -8.790 -7.951 1.00 48.98 ? 213 ILE A C 1 ATOM 1633 O O . ILE A 1 215 ? 43.756 -8.021 -7.004 1.00 52.09 ? 213 ILE A O 1 ATOM 1634 C CB . ILE A 1 215 ? 45.112 -10.548 -6.950 1.00 52.22 ? 213 ILE A CB 1 ATOM 1635 C CG1 . ILE A 1 215 ? 46.201 -11.607 -7.134 1.00 54.47 ? 213 ILE A CG1 1 ATOM 1636 C CG2 . ILE A 1 215 ? 43.767 -11.192 -6.655 1.00 48.23 ? 213 ILE A CG2 1 ATOM 1637 C CD1 . ILE A 1 215 ? 46.682 -12.207 -5.824 1.00 58.34 ? 213 ILE A CD1 1 ATOM 1638 N N . TYR A 1 216 ? 42.814 -8.926 -8.809 1.00 46.15 ? 214 TYR A N 1 ATOM 1639 C CA . TYR A 1 216 ? 41.567 -8.244 -8.596 1.00 44.91 ? 214 TYR A CA 1 ATOM 1640 C C . TYR A 1 216 ? 40.619 -9.263 -8.008 1.00 44.09 ? 214 TYR A C 1 ATOM 1641 O O . TYR A 1 216 ? 40.631 -10.431 -8.373 1.00 42.62 ? 214 TYR A O 1 ATOM 1642 C CB . TYR A 1 216 ? 41.062 -7.644 -9.904 1.00 43.36 ? 214 TYR A CB 1 ATOM 1643 C CG . TYR A 1 216 ? 42.042 -6.646 -10.468 1.00 41.46 ? 214 TYR A CG 1 ATOM 1644 C CD1 . TYR A 1 216 ? 43.252 -7.061 -10.994 1.00 41.05 ? 214 TYR A CD1 1 ATOM 1645 C CD2 . TYR A 1 216 ? 41.770 -5.289 -10.435 1.00 41.08 ? 214 TYR A CD2 1 ATOM 1646 C CE1 . TYR A 1 216 ? 44.154 -6.155 -11.487 1.00 47.86 ? 214 TYR A CE1 1 ATOM 1647 C CE2 . TYR A 1 216 ? 42.664 -4.371 -10.921 1.00 42.62 ? 214 TYR A CE2 1 ATOM 1648 C CZ . TYR A 1 216 ? 43.853 -4.806 -11.451 1.00 45.73 ? 214 TYR A CZ 1 ATOM 1649 O OH . TYR A 1 216 ? 44.744 -3.886 -11.938 1.00 46.29 ? 214 TYR A OH 1 ATOM 1650 N N . THR A 1 217 ? 39.831 -8.800 -7.056 1.00 45.51 ? 215 THR A N 1 ATOM 1651 C CA . THR A 1 217 ? 38.999 -9.665 -6.255 1.00 46.02 ? 215 THR A CA 1 ATOM 1652 C C . THR A 1 217 ? 37.647 -9.032 -6.062 1.00 45.88 ? 215 THR A C 1 ATOM 1653 O O . THR A 1 217 ? 37.492 -8.041 -5.348 1.00 49.43 ? 215 THR A O 1 ATOM 1654 C CB . THR A 1 217 ? 39.649 -9.911 -4.890 1.00 49.40 ? 215 THR A CB 1 ATOM 1655 O OG1 . THR A 1 217 ? 40.978 -10.401 -5.087 1.00 53.84 ? 215 THR A OG1 1 ATOM 1656 C CG2 . THR A 1 217 ? 38.864 -10.916 -4.088 1.00 48.15 ? 215 THR A CG2 1 ATOM 1657 N N . CYS A 1 218 ? 36.675 -9.623 -6.730 1.00 44.17 ? 216 CYS A N 1 ATOM 1658 C CA . CYS A 1 218 ? 35.299 -9.166 -6.664 1.00 43.72 ? 216 CYS A CA 1 ATOM 1659 C C . CYS A 1 218 ? 34.595 -9.837 -5.510 1.00 44.54 ? 216 CYS A C 1 ATOM 1660 O O . CYS A 1 218 ? 34.935 -10.940 -5.085 1.00 45.76 ? 216 CYS A O 1 ATOM 1661 C CB . CYS A 1 218 ? 34.568 -9.460 -7.964 1.00 41.89 ? 216 CYS A CB 1 ATOM 1662 S SG . CYS A 1 218 ? 32.854 -8.945 -7.998 1.00 42.51 ? 216 CYS A SG 1 ATOM 1663 N N . SER A 1 219 ? 33.620 -9.119 -4.993 1.00 44.27 ? 217 SER A N 1 ATOM 1664 C CA . SER A 1 219 ? 32.924 -9.518 -3.798 1.00 43.99 ? 217 SER A CA 1 ATOM 1665 C C . SER A 1 219 ? 31.553 -8.962 -3.920 1.00 42.80 ? 217 SER A C 1 ATOM 1666 O O . SER A 1 219 ? 31.319 -7.762 -3.766 1.00 44.38 ? 217 SER A O 1 ATOM 1667 C CB . SER A 1 219 ? 33.605 -8.980 -2.539 1.00 47.26 ? 217 SER A CB 1 ATOM 1668 O OG . SER A 1 219 ? 34.592 -9.883 -2.087 1.00 49.75 ? 217 SER A OG 1 ATOM 1669 N N . ILE A 1 220 ? 30.646 -9.864 -4.215 1.00 40.38 ? 218 ILE A N 1 ATOM 1670 C CA . ILE A 1 220 ? 29.301 -9.488 -4.528 1.00 40.09 ? 218 ILE A CA 1 ATOM 1671 C C . ILE A 1 220 ? 28.413 -10.035 -3.422 1.00 42.11 ? 218 ILE A C 1 ATOM 1672 O O . ILE A 1 220 ? 28.642 -11.135 -2.908 1.00 43.69 ? 218 ILE A O 1 ATOM 1673 C CB . ILE A 1 220 ? 28.974 -10.004 -5.918 1.00 37.20 ? 218 ILE A CB 1 ATOM 1674 C CG1 . ILE A 1 220 ? 27.698 -9.363 -6.455 1.00 40.13 ? 218 ILE A CG1 1 ATOM 1675 C CG2 . ILE A 1 220 ? 28.929 -11.506 -5.909 1.00 36.67 ? 218 ILE A CG2 1 ATOM 1676 C CD1 . ILE A 1 220 ? 27.668 -9.328 -7.980 1.00 38.32 ? 218 ILE A CD1 1 ATOM 1677 N N . TYR A 1 221 ? 27.453 -9.231 -2.991 1.00 43.25 ? 219 TYR A N 1 ATOM 1678 C CA . TYR A 1 221 ? 26.635 -9.606 -1.843 1.00 44.91 ? 219 TYR A CA 1 ATOM 1679 C C . TYR A 1 221 ? 25.180 -9.481 -2.126 1.00 46.19 ? 219 TYR A C 1 ATOM 1680 O O . TYR A 1 221 ? 24.722 -8.588 -2.838 1.00 47.40 ? 219 TYR A O 1 ATOM 1681 C CB . TYR A 1 221 ? 26.863 -8.698 -0.642 1.00 48.40 ? 219 TYR A CB 1 ATOM 1682 C CG . TYR A 1 221 ? 28.273 -8.549 -0.144 1.00 50.15 ? 219 TYR A CG 1 ATOM 1683 C CD1 . TYR A 1 221 ? 29.201 -7.797 -0.848 1.00 48.06 ? 219 TYR A CD1 1 ATOM 1684 C CD2 . TYR A 1 221 ? 28.658 -9.100 1.072 1.00 48.79 ? 219 TYR A CD2 1 ATOM 1685 C CE1 . TYR A 1 221 ? 30.480 -7.633 -0.384 1.00 51.90 ? 219 TYR A CE1 1 ATOM 1686 C CE2 . TYR A 1 221 ? 29.943 -8.937 1.548 1.00 52.83 ? 219 TYR A CE2 1 ATOM 1687 C CZ . TYR A 1 221 ? 30.848 -8.198 0.813 1.00 52.60 ? 219 TYR A CZ 1 ATOM 1688 O OH . TYR A 1 221 ? 32.132 -8.018 1.260 1.00 57.62 ? 219 TYR A OH 1 ATOM 1689 N N . VAL A 1 222 ? 24.459 -10.396 -1.513 1.00 47.24 ? 220 VAL A N 1 ATOM 1690 C CA . VAL A 1 222 ? 23.040 -10.248 -1.279 1.00 48.22 ? 220 VAL A CA 1 ATOM 1691 C C . VAL A 1 222 ? 22.928 -10.316 0.228 1.00 51.65 ? 220 VAL A C 1 ATOM 1692 O O . VAL A 1 222 ? 23.025 -11.393 0.829 1.00 52.29 ? 220 VAL A O 1 ATOM 1693 C CB . VAL A 1 222 ? 22.248 -11.371 -1.944 1.00 46.64 ? 220 VAL A CB 1 ATOM 1694 C CG1 . VAL A 1 222 ? 20.749 -11.091 -1.873 1.00 46.26 ? 220 VAL A CG1 1 ATOM 1695 C CG2 . VAL A 1 222 ? 22.707 -11.513 -3.386 1.00 43.33 ? 220 VAL A CG2 1 ATOM 1696 N N . GLY A 1 223 ? 22.777 -9.150 0.841 1.00 53.59 ? 221 GLY A N 1 ATOM 1697 C CA . GLY A 1 223 ? 22.877 -9.047 2.284 1.00 56.34 ? 221 GLY A CA 1 ATOM 1698 C C . GLY A 1 223 ? 24.244 -9.505 2.746 1.00 56.26 ? 221 GLY A C 1 ATOM 1699 O O . GLY A 1 223 ? 25.263 -9.157 2.161 1.00 56.63 ? 221 GLY A O 1 ATOM 1700 N N . LYS A 1 224 ? 24.257 -10.316 3.791 1.00 58.23 ? 222 LYS A N 1 ATOM 1701 C CA . LYS A 1 224 ? 25.497 -10.722 4.446 1.00 59.07 ? 222 LYS A CA 1 ATOM 1702 C C . LYS A 1 224 ? 26.224 -11.826 3.679 1.00 55.15 ? 222 LYS A C 1 ATOM 1703 O O . LYS A 1 224 ? 27.380 -12.133 3.950 1.00 57.09 ? 222 LYS A O 1 ATOM 1704 C CB . LYS A 1 224 ? 25.213 -11.185 5.884 1.00 62.18 ? 222 LYS A CB 1 ATOM 1705 C CG . LYS A 1 224 ? 24.570 -10.113 6.782 1.00 68.87 ? 222 LYS A CG 1 ATOM 1706 C CD . LYS A 1 224 ? 25.434 -8.852 6.953 1.00 69.00 ? 222 LYS A CD 1 ATOM 1707 C CE . LYS A 1 224 ? 26.533 -9.043 7.990 1.00 69.67 ? 222 LYS A CE 1 ATOM 1708 N NZ . LYS A 1 224 ? 27.341 -7.794 8.194 1.00 71.11 ? 222 LYS A NZ 1 ATOM 1709 N N . LEU A 1 225 ? 25.544 -12.424 2.720 1.00 51.00 ? 223 LEU A N 1 ATOM 1710 C CA . LEU A 1 225 ? 26.126 -13.553 2.001 1.00 48.56 ? 223 LEU A CA 1 ATOM 1711 C C . LEU A 1 225 ? 27.136 -13.078 0.963 1.00 46.41 ? 223 LEU A C 1 ATOM 1712 O O . LEU A 1 225 ? 26.838 -12.246 0.103 1.00 45.19 ? 223 LEU A O 1 ATOM 1713 C CB . LEU A 1 225 ? 25.034 -14.403 1.352 1.00 46.77 ? 223 LEU A CB 1 ATOM 1714 C CG . LEU A 1 225 ? 24.107 -15.075 2.362 1.00 48.13 ? 223 LEU A CG 1 ATOM 1715 C CD1 . LEU A 1 225 ? 22.913 -15.707 1.645 1.00 43.89 ? 223 LEU A CD1 1 ATOM 1716 C CD2 . LEU A 1 225 ? 24.871 -16.105 3.203 1.00 43.69 ? 223 LEU A CD2 1 ATOM 1717 N N . GLU A 1 226 ? 28.345 -13.610 1.056 1.00 46.97 ? 224 GLU A N 1 ATOM 1718 C CA . GLU A 1 226 ? 29.407 -13.198 0.156 1.00 45.94 ? 224 GLU A CA 1 ATOM 1719 C C . GLU A 1 226 ? 29.714 -14.235 -0.894 1.00 44.26 ? 224 GLU A C 1 ATOM 1720 O O . GLU A 1 226 ? 29.812 -15.427 -0.614 1.00 44.76 ? 224 GLU A O 1 ATOM 1721 C CB . GLU A 1 226 ? 30.690 -12.869 0.920 1.00 47.72 ? 224 GLU A CB 1 ATOM 1722 C CG . GLU A 1 226 ? 31.737 -12.203 0.035 1.00 48.53 ? 224 GLU A CG 1 ATOM 1723 C CD . GLU A 1 226 ? 33.005 -11.800 0.771 1.00 56.11 ? 224 GLU A CD 1 ATOM 1724 O OE1 . GLU A 1 226 ? 33.235 -12.247 1.933 1.00 47.88 ? 224 GLU A OE1 1 ATOM 1725 O OE2 . GLU A 1 226 ? 33.778 -11.028 0.154 1.00 55.47 ? 224 GLU A OE2 1 ATOM 1726 N N . SER A 1 227 ? 29.859 -13.739 -2.114 1.00 42.33 ? 225 SER A N 1 ATOM 1727 C CA . SER A 1 227 ? 30.456 -14.495 -3.189 1.00 41.17 ? 225 SER A CA 1 ATOM 1728 C C . SER A 1 227 ? 31.685 -13.738 -3.610 1.00 41.97 ? 225 SER A C 1 ATOM 1729 O O . SER A 1 227 ? 31.613 -12.576 -3.985 1.00 41.52 ? 225 SER A O 1 ATOM 1730 C CB . SER A 1 227 ? 29.489 -14.640 -4.356 1.00 38.88 ? 225 SER A CB 1 ATOM 1731 O OG . SER A 1 227 ? 28.300 -15.277 -3.925 1.00 42.58 ? 225 SER A OG 1 ATOM 1732 N N . ARG A 1 228 ? 32.815 -14.418 -3.503 1.00 44.32 ? 226 ARG A N 1 ATOM 1733 C CA . ARG A 1 228 ? 34.109 -13.877 -3.893 1.00 45.04 ? 226 ARG A CA 1 ATOM 1734 C C . ARG A 1 228 ? 34.550 -14.450 -5.219 1.00 43.11 ? 226 ARG A C 1 ATOM 1735 O O . ARG A 1 228 ? 34.436 -15.648 -5.468 1.00 43.63 ? 226 ARG A O 1 ATOM 1736 C CB . ARG A 1 228 ? 35.189 -14.216 -2.854 1.00 48.23 ? 226 ARG A CB 1 ATOM 1737 C CG . ARG A 1 228 ? 35.209 -13.335 -1.630 1.00 54.59 ? 226 ARG A CG 1 ATOM 1738 C CD . ARG A 1 228 ? 36.383 -13.705 -0.734 1.00 62.56 ? 226 ARG A CD 1 ATOM 1739 N NE . ARG A 1 228 ? 36.300 -13.075 0.583 1.00 72.10 ? 226 ARG A NE 1 ATOM 1740 C CZ . ARG A 1 228 ? 37.048 -13.415 1.632 1.00 80.54 ? 226 ARG A CZ 1 ATOM 1741 N NH1 . ARG A 1 228 ? 37.940 -14.394 1.534 1.00 82.93 ? 226 ARG A NH1 1 ATOM 1742 N NH2 . ARG A 1 228 ? 36.900 -12.774 2.786 1.00 84.47 ? 226 ARG A NH2 1 ATOM 1743 N N . LYS A 1 229 ? 35.079 -13.578 -6.057 1.00 41.96 ? 227 LYS A N 1 ATOM 1744 C CA . LYS A 1 229 ? 35.764 -13.986 -7.272 1.00 41.41 ? 227 LYS A CA 1 ATOM 1745 C C . LYS A 1 229 ? 37.131 -13.303 -7.323 1.00 42.95 ? 227 LYS A C 1 ATOM 1746 O O . LYS A 1 229 ? 37.278 -12.156 -6.895 1.00 42.75 ? 227 LYS A O 1 ATOM 1747 C CB . LYS A 1 229 ? 34.930 -13.578 -8.472 1.00 39.97 ? 227 LYS A CB 1 ATOM 1748 C CG . LYS A 1 229 ? 35.256 -14.285 -9.752 1.00 40.35 ? 227 LYS A CG 1 ATOM 1749 C CD . LYS A 1 229 ? 34.364 -13.754 -10.861 1.00 39.69 ? 227 LYS A CD 1 ATOM 1750 C CE . LYS A 1 229 ? 34.669 -14.426 -12.172 1.00 43.26 ? 227 LYS A CE 1 ATOM 1751 N NZ . LYS A 1 229 ? 34.426 -13.516 -13.326 1.00 50.71 ? 227 LYS A NZ 1 ATOM 1752 N N . THR A 1 230 ? 38.130 -14.017 -7.832 1.00 43.25 ? 228 THR A N 1 ATOM 1753 C CA . THR A 1 230 ? 39.463 -13.438 -8.002 1.00 44.22 ? 228 THR A CA 1 ATOM 1754 C C . THR A 1 230 ? 40.000 -13.659 -9.402 1.00 43.21 ? 228 THR A C 1 ATOM 1755 O O . THR A 1 230 ? 39.981 -14.770 -9.916 1.00 44.42 ? 228 THR A O 1 ATOM 1756 C CB . THR A 1 230 ? 40.473 -14.016 -6.997 1.00 47.33 ? 228 THR A CB 1 ATOM 1757 O OG1 . THR A 1 230 ? 41.150 -15.140 -7.575 1.00 48.58 ? 228 THR A OG1 1 ATOM 1758 C CG2 . THR A 1 230 ? 39.772 -14.433 -5.720 1.00 49.55 ? 228 THR A CG2 1 ATOM 1759 N N . ILE A 1 231 ? 40.465 -12.576 -10.010 1.00 42.15 ? 229 ILE A N 1 ATOM 1760 C CA . ILE A 1 231 ? 41.081 -12.621 -11.330 1.00 41.11 ? 229 ILE A CA 1 ATOM 1761 C C . ILE A 1 231 ? 42.511 -12.135 -11.231 1.00 42.38 ? 229 ILE A C 1 ATOM 1762 O O . ILE A 1 231 ? 42.784 -11.104 -10.609 1.00 42.65 ? 229 ILE A O 1 ATOM 1763 C CB . ILE A 1 231 ? 40.373 -11.689 -12.330 1.00 39.20 ? 229 ILE A CB 1 ATOM 1764 C CG1 . ILE A 1 231 ? 38.905 -12.067 -12.498 1.00 38.00 ? 229 ILE A CG1 1 ATOM 1765 C CG2 . ILE A 1 231 ? 41.070 -11.741 -13.675 1.00 42.37 ? 229 ILE A CG2 1 ATOM 1766 C CD1 . ILE A 1 231 ? 38.110 -11.060 -13.330 1.00 35.49 ? 229 ILE A CD1 1 ATOM 1767 N N . VAL A 1 232 ? 43.414 -12.888 -11.850 1.00 41.92 ? 230 VAL A N 1 ATOM 1768 C CA . VAL A 1 232 ? 44.806 -12.477 -11.967 1.00 43.24 ? 230 VAL A CA 1 ATOM 1769 C C . VAL A 1 232 ? 45.085 -11.861 -13.331 1.00 43.03 ? 230 VAL A C 1 ATOM 1770 O O . VAL A 1 232 ? 45.130 -12.543 -14.368 1.00 41.45 ? 230 VAL A O 1 ATOM 1771 C CB . VAL A 1 232 ? 45.778 -13.635 -11.749 1.00 45.80 ? 230 VAL A CB 1 ATOM 1772 C CG1 . VAL A 1 232 ? 47.193 -13.188 -12.106 1.00 48.31 ? 230 VAL A CG1 1 ATOM 1773 C CG2 . VAL A 1 232 ? 45.709 -14.113 -10.311 1.00 46.71 ? 230 VAL A CG2 1 ATOM 1774 N N . LEU A 1 233 ? 45.303 -10.553 -13.292 1.00 44.12 ? 231 LEU A N 1 ATOM 1775 C CA . LEU A 1 233 ? 45.557 -9.753 -14.485 1.00 44.05 ? 231 LEU A CA 1 ATOM 1776 C C . LEU A 1 233 ? 47.038 -9.628 -14.773 1.00 46.75 ? 231 LEU A C 1 ATOM 1777 O O . LEU A 1 233 ? 47.769 -8.986 -14.033 1.00 48.36 ? 231 LEU A O 1 ATOM 1778 C CB . LEU A 1 233 ? 44.960 -8.357 -14.322 1.00 43.23 ? 231 LEU A CB 1 ATOM 1779 C CG . LEU A 1 233 ? 45.280 -7.423 -15.485 1.00 44.15 ? 231 LEU A CG 1 ATOM 1780 C CD1 . LEU A 1 233 ? 44.442 -7.799 -16.702 1.00 41.97 ? 231 LEU A CD1 1 ATOM 1781 C CD2 . LEU A 1 233 ? 45.058 -5.970 -15.078 1.00 43.43 ? 231 LEU A CD2 1 ATOM 1782 N N . HIS A 1 234 ? 47.457 -10.248 -15.868 1.00 48.37 ? 232 HIS A N 1 ATOM 1783 C CA . HIS A 1 234 ? 48.801 -10.060 -16.419 1.00 51.48 ? 232 HIS A CA 1 ATOM 1784 C C . HIS A 1 234 ? 48.763 -8.949 -17.452 1.00 51.31 ? 232 HIS A C 1 ATOM 1785 O O . HIS A 1 234 ? 47.795 -8.811 -18.209 1.00 49.90 ? 232 HIS A O 1 ATOM 1786 C CB . HIS A 1 234 ? 49.324 -11.337 -17.090 1.00 52.83 ? 232 HIS A CB 1 ATOM 1787 C CG . HIS A 1 234 ? 49.393 -12.526 -16.181 1.00 57.35 ? 232 HIS A CG 1 ATOM 1788 N ND1 . HIS A 1 234 ? 50.322 -12.638 -15.168 1.00 62.00 ? 232 HIS A ND1 1 ATOM 1789 C CD2 . HIS A 1 234 ? 48.661 -13.666 -16.147 1.00 59.42 ? 232 HIS A CD2 1 ATOM 1790 C CE1 . HIS A 1 234 ? 50.151 -13.790 -14.542 1.00 62.93 ? 232 HIS A CE1 1 ATOM 1791 N NE2 . HIS A 1 234 ? 49.151 -14.433 -15.118 1.00 61.13 ? 232 HIS A NE2 1 ATOM 1792 N N . VAL A 1 235 ? 49.834 -8.170 -17.483 1.00 53.77 ? 233 VAL A N 1 ATOM 1793 C CA . VAL A 1 235 ? 49.978 -7.070 -18.436 1.00 54.48 ? 233 VAL A CA 1 ATOM 1794 C C . VAL A 1 235 ? 51.331 -7.104 -19.126 1.00 58.41 ? 233 VAL A C 1 ATOM 1795 O O . VAL A 1 235 ? 52.369 -7.213 -18.478 1.00 61.19 ? 233 VAL A O 1 ATOM 1796 C CB . VAL A 1 235 ? 49.824 -5.718 -17.731 1.00 55.00 ? 233 VAL A CB 1 ATOM 1797 C CG1 . VAL A 1 235 ? 50.190 -4.580 -18.676 1.00 55.90 ? 233 VAL A CG1 1 ATOM 1798 C CG2 . VAL A 1 235 ? 48.406 -5.567 -17.196 1.00 52.42 ? 233 VAL A CG2 1 ATOM 1799 N N . VAL A 1 236 ? 51.309 -7.013 -20.448 1.00 60.27 ? 234 VAL A N 1 ATOM 1800 C CA . VAL A 1 236 ? 52.538 -7.073 -21.244 1.00 65.12 ? 234 VAL A CA 1 ATOM 1801 C C . VAL A 1 236 ? 52.700 -5.891 -22.200 1.00 66.95 ? 234 VAL A C 1 ATOM 1802 O O . VAL A 1 236 ? 51.761 -5.470 -22.877 1.00 66.35 ? 234 VAL A O 1 ATOM 1803 C CB . VAL A 1 236 ? 52.626 -8.391 -22.057 1.00 65.79 ? 234 VAL A CB 1 ATOM 1804 C CG1 . VAL A 1 236 ? 53.924 -8.433 -22.871 1.00 69.20 ? 234 VAL A CG1 1 ATOM 1805 C CG2 . VAL A 1 236 ? 52.534 -9.607 -21.132 1.00 66.06 ? 234 VAL A CG2 1 ATOM 1806 N N . GLN A 1 237 ? 53.907 -5.349 -22.228 1.00 70.27 ? 235 GLN A N 1 ATOM 1807 C CA . GLN A 1 237 ? 54.271 -4.388 -23.252 1.00 72.61 ? 235 GLN A CA 1 ATOM 1808 C C . GLN A 1 237 ? 55.393 -4.949 -24.092 1.00 75.39 ? 235 GLN A C 1 ATOM 1809 O O . GLN A 1 237 ? 56.437 -5.356 -23.575 1.00 77.15 ? 235 GLN A O 1 ATOM 1810 C CB . GLN A 1 237 ? 54.708 -3.065 -22.646 1.00 74.99 ? 235 GLN A CB 1 ATOM 1811 C CG . GLN A 1 237 ? 54.972 -2.004 -23.697 1.00 76.83 ? 235 GLN A CG 1 ATOM 1812 C CD . GLN A 1 237 ? 55.030 -0.631 -23.100 1.00 82.21 ? 235 GLN A CD 1 ATOM 1813 O OE1 . GLN A 1 237 ? 54.414 -0.369 -22.068 1.00 83.82 ? 235 GLN A OE1 1 ATOM 1814 N NE2 . GLN A 1 237 ? 55.784 0.260 -23.731 1.00 92.72 ? 235 GLN A NE2 1 ATOM 1815 N N . ASP A 1 238 ? 55.169 -4.961 -25.397 1.00 75.30 ? 236 ASP A N 1 ATOM 1816 C CA . ASP A 1 238 ? 56.148 -5.532 -26.301 1.00 78.62 ? 236 ASP A CA 1 ATOM 1817 C C . ASP A 1 238 ? 57.300 -4.583 -26.449 1.00 81.57 ? 236 ASP A C 1 ATOM 1818 O O . ASP A 1 238 ? 57.145 -3.461 -26.919 1.00 83.14 ? 236 ASP A O 1 ATOM 1819 C CB . ASP A 1 238 ? 55.544 -5.918 -27.655 1.00 78.52 ? 236 ASP A CB 1 ATOM 1820 C CG . ASP A 1 238 ? 54.839 -7.275 -27.598 1.00 80.21 ? 236 ASP A CG 1 ATOM 1821 O OD1 . ASP A 1 238 ? 54.410 -7.678 -26.487 1.00 71.43 ? 236 ASP A OD1 1 ATOM 1822 O OD2 . ASP A 1 238 ? 54.730 -7.945 -28.652 1.00 86.12 ? 236 ASP A OD2 1 ATOM 1823 N N . GLU A 1 239 ? 58.451 -5.036 -25.976 1.00 83.85 ? 237 GLU A N 1 ATOM 1824 C CA . GLU A 1 239 ? 59.701 -4.365 -26.259 1.00 88.11 ? 237 GLU A CA 1 ATOM 1825 C C . GLU A 1 239 ? 59.904 -4.612 -27.736 1.00 89.33 ? 237 GLU A C 1 ATOM 1826 O O . GLU A 1 239 ? 59.566 -5.684 -28.237 1.00 90.12 ? 237 GLU A O 1 ATOM 1827 C CB . GLU A 1 239 ? 60.856 -4.939 -25.430 1.00 91.61 ? 237 GLU A CB 1 ATOM 1828 C CG . GLU A 1 239 ? 60.699 -4.774 -23.908 1.00 89.90 ? 237 GLU A CG 1 ATOM 1829 C CD . GLU A 1 239 ? 61.992 -4.333 -23.198 1.00 97.18 ? 237 GLU A CD 1 ATOM 1830 O OE1 . GLU A 1 239 ? 63.061 -4.209 -23.845 1.00 96.66 ? 237 GLU A OE1 1 ATOM 1831 O OE2 . GLU A 1 239 ? 61.931 -4.100 -21.971 1.00 97.77 ? 237 GLU A OE2 1 ATOM 1832 N N . PHE A 1 240 ? 60.412 -3.614 -28.439 1.00 89.98 ? 238 PHE A N 1 ATOM 1833 C CA . PHE A 1 240 ? 60.468 -3.688 -29.894 1.00 90.39 ? 238 PHE A CA 1 ATOM 1834 C C . PHE A 1 240 ? 61.841 -4.061 -30.403 1.00 94.97 ? 238 PHE A C 1 ATOM 1835 O O . PHE A 1 240 ? 62.705 -3.203 -30.580 1.00 97.62 ? 238 PHE A O 1 ATOM 1836 C CB . PHE A 1 240 ? 60.025 -2.366 -30.504 1.00 90.26 ? 238 PHE A CB 1 ATOM 1837 C CG . PHE A 1 240 ? 58.558 -2.103 -30.361 1.00 84.20 ? 238 PHE A CG 1 ATOM 1838 C CD1 . PHE A 1 240 ? 57.661 -2.617 -31.281 1.00 79.90 ? 238 PHE A CD1 1 ATOM 1839 C CD2 . PHE A 1 240 ? 58.072 -1.349 -29.304 1.00 79.32 ? 238 PHE A CD2 1 ATOM 1840 C CE1 . PHE A 1 240 ? 56.308 -2.377 -31.155 1.00 73.46 ? 238 PHE A CE1 1 ATOM 1841 C CE2 . PHE A 1 240 ? 56.717 -1.104 -29.175 1.00 72.46 ? 238 PHE A CE2 1 ATOM 1842 C CZ . PHE A 1 240 ? 55.837 -1.618 -30.099 1.00 70.48 ? 238 PHE A CZ 1 ATOM 1843 N N . GLN A 1 241 ? 62.018 -5.354 -30.653 1.00 95.53 ? 239 GLN A N 1 ATOM 1844 C CA . GLN A 1 241 ? 63.269 -5.875 -31.207 1.00 100.64 ? 239 GLN A CA 1 ATOM 1845 C C . GLN A 1 241 ? 63.026 -6.772 -32.415 1.00 102.42 ? 239 GLN A C 1 ATOM 1846 O O . GLN A 1 241 ? 63.978 -7.193 -33.077 1.00 107.12 ? 239 GLN A O 1 ATOM 1847 C CB . GLN A 1 241 ? 64.041 -6.664 -30.154 1.00 101.94 ? 239 GLN A CB 1 ATOM 1848 C CG . GLN A 1 241 ? 64.338 -5.886 -28.890 1.00 99.45 ? 239 GLN A CG 1 ATOM 1849 C CD . GLN A 1 241 ? 65.067 -4.596 -29.166 1.00 98.29 ? 239 GLN A CD 1 ATOM 1850 O OE1 . GLN A 1 241 ? 65.896 -4.518 -30.073 1.00 101.09 ? 239 GLN A OE1 1 ATOM 1851 N NE2 . GLN A 1 241 ? 64.759 -3.569 -28.386 1.00 93.77 ? 239 GLN A NE2 1 ATOM 1852 N N . ILE B 2 5 ? 18.415 -45.636 -8.852 1.00 57.49 ? 3 ILE B N 1 ATOM 1853 C CA . ILE B 2 5 ? 17.139 -46.382 -8.752 1.00 56.93 ? 3 ILE B CA 1 ATOM 1854 C C . ILE B 2 5 ? 16.251 -45.708 -7.751 1.00 54.62 ? 3 ILE B C 1 ATOM 1855 O O . ILE B 2 5 ? 16.679 -45.387 -6.663 1.00 53.76 ? 3 ILE B O 1 ATOM 1856 C CB . ILE B 2 5 ? 17.369 -47.832 -8.309 1.00 58.60 ? 3 ILE B CB 1 ATOM 1857 C CG1 . ILE B 2 5 ? 18.382 -48.508 -9.228 1.00 61.48 ? 3 ILE B CG1 1 ATOM 1858 C CG2 . ILE B 2 5 ? 16.065 -48.605 -8.337 1.00 58.79 ? 3 ILE B CG2 1 ATOM 1859 C CD1 . ILE B 2 5 ? 18.428 -50.005 -9.081 1.00 65.50 ? 3 ILE B CD1 1 ATOM 1860 N N . THR B 2 6 ? 15.007 -45.492 -8.138 1.00 56.32 ? 4 THR B N 1 ATOM 1861 C CA . THR B 2 6 ? 14.010 -44.912 -7.238 1.00 55.94 ? 4 THR B CA 1 ATOM 1862 C C . THR B 2 6 ? 12.728 -45.736 -7.285 1.00 57.04 ? 4 THR B C 1 ATOM 1863 O O . THR B 2 6 ? 12.657 -46.743 -7.981 1.00 58.64 ? 4 THR B O 1 ATOM 1864 C CB . THR B 2 6 ? 13.681 -43.432 -7.583 1.00 54.59 ? 4 THR B CB 1 ATOM 1865 O OG1 . THR B 2 6 ? 12.581 -42.988 -6.783 1.00 57.48 ? 4 THR B OG1 1 ATOM 1866 C CG2 . THR B 2 6 ? 13.296 -43.269 -9.055 1.00 58.98 ? 4 THR B CG2 1 ATOM 1867 N N . THR B 2 7 ? 11.722 -45.285 -6.546 1.00 56.23 ? 5 THR B N 1 ATOM 1868 C CA . THR B 2 7 ? 10.440 -45.978 -6.478 1.00 59.30 ? 5 THR B CA 1 ATOM 1869 C C . THR B 2 7 ? 9.307 -45.043 -6.903 1.00 59.68 ? 5 THR B C 1 ATOM 1870 O O . THR B 2 7 ? 9.262 -43.882 -6.491 1.00 57.78 ? 5 THR B O 1 ATOM 1871 C CB . THR B 2 7 ? 10.163 -46.536 -5.058 1.00 59.10 ? 5 THR B CB 1 ATOM 1872 O OG1 . THR B 2 7 ? 10.185 -45.466 -4.104 1.00 54.51 ? 5 THR B OG1 1 ATOM 1873 C CG2 . THR B 2 7 ? 11.221 -47.582 -4.670 1.00 59.82 ? 5 THR B CG2 1 ATOM 1874 N N . PRO B 2 8 ? 8.394 -45.543 -7.746 1.00 62.15 ? 6 PRO B N 1 ATOM 1875 C CA . PRO B 2 8 ? 7.308 -44.706 -8.270 1.00 62.81 ? 6 PRO B CA 1 ATOM 1876 C C . PRO B 2 8 ? 6.254 -44.286 -7.254 1.00 62.68 ? 6 PRO B C 1 ATOM 1877 O O . PRO B 2 8 ? 6.386 -44.533 -6.054 1.00 62.57 ? 6 PRO B O 1 ATOM 1878 C CB . PRO B 2 8 ? 6.654 -45.584 -9.338 1.00 65.45 ? 6 PRO B CB 1 ATOM 1879 C CG . PRO B 2 8 ? 7.623 -46.672 -9.626 1.00 68.29 ? 6 PRO B CG 1 ATOM 1880 C CD . PRO B 2 8 ? 8.498 -46.839 -8.433 1.00 64.79 ? 6 PRO B CD 1 ATOM 1881 N N . GLU B 2 9 ? 5.198 -43.669 -7.770 1.00 64.36 ? 7 GLU B N 1 ATOM 1882 C CA . GLU B 2 9 ? 4.081 -43.202 -6.944 1.00 65.56 ? 7 GLU B CA 1 ATOM 1883 C C . GLU B 2 9 ? 3.051 -44.316 -6.849 1.00 67.92 ? 7 GLU B C 1 ATOM 1884 O O . GLU B 2 9 ? 2.407 -44.652 -7.831 1.00 69.54 ? 7 GLU B O 1 ATOM 1885 C CB . GLU B 2 9 ? 3.412 -41.952 -7.545 1.00 66.02 ? 7 GLU B CB 1 ATOM 1886 C CG . GLU B 2 9 ? 4.334 -41.006 -8.336 1.00 66.94 ? 7 GLU B CG 1 ATOM 1887 C CD . GLU B 2 9 ? 4.347 -41.296 -9.841 1.00 74.63 ? 7 GLU B CD 1 ATOM 1888 O OE1 . GLU B 2 9 ? 3.256 -41.495 -10.433 1.00 80.92 ? 7 GLU B OE1 1 ATOM 1889 O OE2 . GLU B 2 9 ? 5.449 -41.320 -10.436 1.00 71.62 ? 7 GLU B OE2 1 ATOM 1890 N N . GLN B 2 10 ? 2.892 -44.892 -5.669 1.00 68.80 ? 8 GLN B N 1 ATOM 1891 C CA . GLN B 2 10 ? 1.951 -46.006 -5.516 1.00 71.49 ? 8 GLN B CA 1 ATOM 1892 C C . GLN B 2 10 ? 0.603 -45.685 -6.147 1.00 71.86 ? 8 GLN B C 1 ATOM 1893 O O . GLN B 2 10 ? 0.052 -44.598 -5.964 1.00 70.75 ? 8 GLN B O 1 ATOM 1894 C CB . GLN B 2 10 ? 1.782 -46.401 -4.046 1.00 71.29 ? 8 GLN B CB 1 ATOM 1895 C CG . GLN B 2 10 ? 3.012 -47.102 -3.469 1.00 74.84 ? 8 GLN B CG 1 ATOM 1896 C CD . GLN B 2 10 ? 2.850 -47.501 -2.003 1.00 79.32 ? 8 GLN B CD 1 ATOM 1897 O OE1 . GLN B 2 10 ? 3.773 -47.333 -1.194 1.00 78.55 ? 8 GLN B OE1 1 ATOM 1898 N NE2 . GLN B 2 10 ? 1.675 -48.026 -1.654 1.00 77.97 ? 8 GLN B NE2 1 ATOM 1899 N N . ARG B 2 11 ? 0.098 -46.659 -6.898 1.00 73.61 ? 9 ARG B N 1 ATOM 1900 C CA . ARG B 2 11 ? -1.173 -46.541 -7.619 1.00 75.28 ? 9 ARG B CA 1 ATOM 1901 C C . ARG B 2 11 ? -2.279 -47.228 -6.851 1.00 75.97 ? 9 ARG B C 1 ATOM 1902 O O . ARG B 2 11 ? -2.239 -48.438 -6.634 1.00 77.34 ? 9 ARG B O 1 ATOM 1903 C CB . ARG B 2 11 ? -1.062 -47.173 -9.010 1.00 77.70 ? 9 ARG B CB 1 ATOM 1904 C CG . ARG B 2 11 ? 0.032 -46.551 -9.875 1.00 81.86 ? 9 ARG B CG 1 ATOM 1905 C CD . ARG B 2 11 ? 0.009 -47.034 -11.325 1.00 89.27 ? 9 ARG B CD 1 ATOM 1906 N NE . ARG B 2 11 ? 0.880 -48.189 -11.550 1.00 92.93 ? 9 ARG B NE 1 ATOM 1907 C CZ . ARG B 2 11 ? 1.210 -48.666 -12.748 1.00 96.42 ? 9 ARG B CZ 1 ATOM 1908 N NH1 . ARG B 2 11 ? 0.746 -48.093 -13.849 1.00 99.46 ? 9 ARG B NH1 1 ATOM 1909 N NH2 . ARG B 2 11 ? 2.009 -49.720 -12.847 1.00 98.07 ? 9 ARG B NH2 1 ATOM 1910 N N . ILE B 2 12 ? -3.269 -46.440 -6.445 1.00 74.87 ? 10 ILE B N 1 ATOM 1911 C CA . ILE B 2 12 ? -4.440 -46.960 -5.725 1.00 75.39 ? 10 ILE B CA 1 ATOM 1912 C C . ILE B 2 12 ? -5.730 -46.798 -6.506 1.00 76.15 ? 10 ILE B C 1 ATOM 1913 O O . ILE B 2 12 ? -6.156 -45.681 -6.808 1.00 75.35 ? 10 ILE B O 1 ATOM 1914 C CB . ILE B 2 12 ? -4.634 -46.275 -4.363 1.00 73.71 ? 10 ILE B CB 1 ATOM 1915 C CG1 . ILE B 2 12 ? -3.389 -46.465 -3.494 1.00 71.51 ? 10 ILE B CG1 1 ATOM 1916 C CG2 . ILE B 2 12 ? -5.888 -46.820 -3.678 1.00 76.83 ? 10 ILE B CG2 1 ATOM 1917 C CD1 . ILE B 2 12 ? -2.781 -47.853 -3.585 1.00 71.13 ? 10 ILE B CD1 1 ATOM 1918 N N . GLU B 2 13 ? -6.350 -47.938 -6.799 1.00 77.80 ? 11 GLU B N 1 ATOM 1919 C CA . GLU B 2 13 ? -7.627 -48.000 -7.527 1.00 78.97 ? 11 GLU B CA 1 ATOM 1920 C C . GLU B 2 13 ? -8.774 -48.401 -6.609 1.00 80.44 ? 11 GLU B C 1 ATOM 1921 O O . GLU B 2 13 ? -8.762 -49.466 -5.983 1.00 81.28 ? 11 GLU B O 1 ATOM 1922 C CB . GLU B 2 13 ? -7.524 -48.988 -8.678 1.00 80.13 ? 11 GLU B CB 1 ATOM 1923 C CG . GLU B 2 13 ? -8.628 -48.844 -9.684 1.00 81.69 ? 11 GLU B CG 1 ATOM 1924 C CD . GLU B 2 13 ? -8.394 -49.670 -10.948 1.00 84.35 ? 11 GLU B CD 1 ATOM 1925 O OE1 . GLU B 2 13 ? -7.874 -50.812 -10.848 1.00 88.96 ? 11 GLU B OE1 1 ATOM 1926 O OE2 . GLU B 2 13 ? -8.734 -49.175 -12.046 1.00 80.25 ? 11 GLU B OE2 1 ATOM 1927 N N . LYS B 2 14 ? -9.771 -47.528 -6.546 1.00 80.54 ? 12 LYS B N 1 ATOM 1928 C CA . LYS B 2 14 ? -10.942 -47.744 -5.699 1.00 82.32 ? 12 LYS B CA 1 ATOM 1929 C C . LYS B 2 14 ? -12.260 -47.516 -6.426 1.00 85.12 ? 12 LYS B C 1 ATOM 1930 O O . LYS B 2 14 ? -12.315 -46.922 -7.502 1.00 83.65 ? 12 LYS B O 1 ATOM 1931 C CB . LYS B 2 14 ? -10.873 -46.839 -4.465 1.00 79.70 ? 12 LYS B CB 1 ATOM 1932 C CG . LYS B 2 14 ? -9.869 -47.292 -3.422 1.00 77.41 ? 12 LYS B CG 1 ATOM 1933 C CD . LYS B 2 14 ? -10.113 -48.746 -2.983 1.00 77.83 ? 12 LYS B CD 1 ATOM 1934 C CE . LYS B 2 14 ? -9.465 -49.057 -1.652 1.00 76.32 ? 12 LYS B CE 1 ATOM 1935 N NZ . LYS B 2 14 ? -10.139 -48.305 -0.562 1.00 76.27 ? 12 LYS B NZ 1 ATOM 1936 N N . ALA B 2 15 ? -13.323 -48.017 -5.809 1.00 88.67 ? 13 ALA B N 1 ATOM 1937 C CA . ALA B 2 15 ? -14.685 -47.788 -6.294 1.00 92.02 ? 13 ALA B CA 1 ATOM 1938 C C . ALA B 2 15 ? -15.254 -46.540 -5.656 1.00 91.75 ? 13 ALA B C 1 ATOM 1939 O O . ALA B 2 15 ? -14.701 -45.985 -4.701 1.00 90.35 ? 13 ALA B O 1 ATOM 1940 C CB . ALA B 2 15 ? -15.573 -48.967 -5.993 1.00 95.01 ? 13 ALA B CB 1 ATOM 1941 N N . LYS B 2 16 ? -16.379 -46.115 -6.202 1.00 93.41 ? 14 LYS B N 1 ATOM 1942 C CA . LYS B 2 16 ? -17.065 -44.917 -5.731 1.00 93.60 ? 14 LYS B CA 1 ATOM 1943 C C . LYS B 2 16 ? -17.584 -45.142 -4.329 1.00 94.80 ? 14 LYS B C 1 ATOM 1944 O O . LYS B 2 16 ? -17.702 -46.275 -3.865 1.00 96.75 ? 14 LYS B O 1 ATOM 1945 C CB . LYS B 2 16 ? -18.225 -44.557 -6.675 1.00 97.56 ? 14 LYS B CB 1 ATOM 1946 C CG . LYS B 2 16 ? -19.003 -43.276 -6.338 1.00 97.70 ? 14 LYS B CG 1 ATOM 1947 C CD . LYS B 2 16 ? -20.141 -43.059 -7.329 1.00 101.49 ? 14 LYS B CD 1 ATOM 1948 C CE . LYS B 2 16 ? -21.171 -42.054 -6.822 1.00 105.35 ? 14 LYS B CE 1 ATOM 1949 N NZ . LYS B 2 16 ? -22.381 -41.961 -7.717 1.00 109.07 ? 14 LYS B NZ 1 ATOM 1950 N N . GLY B 2 17 ? -17.848 -44.026 -3.663 1.00 94.30 ? 15 GLY B N 1 ATOM 1951 C CA . GLY B 2 17 ? -18.615 -43.984 -2.423 1.00 96.01 ? 15 GLY B CA 1 ATOM 1952 C C . GLY B 2 17 ? -17.963 -44.591 -1.202 1.00 94.25 ? 15 GLY B C 1 ATOM 1953 O O . GLY B 2 17 ? -18.569 -44.637 -0.139 1.00 96.42 ? 15 GLY B O 1 ATOM 1954 N N . GLU B 2 18 ? -16.733 -45.060 -1.352 1.00 91.36 ? 16 GLU B N 1 ATOM 1955 C CA . GLU B 2 18 ? -16.033 -45.748 -0.261 1.00 90.56 ? 16 GLU B CA 1 ATOM 1956 C C . GLU B 2 18 ? -14.762 -45.027 0.200 1.00 85.09 ? 16 GLU B C 1 ATOM 1957 O O . GLU B 2 18 ? -14.571 -43.848 -0.095 1.00 83.04 ? 16 GLU B O 1 ATOM 1958 C CB . GLU B 2 18 ? -15.737 -47.192 -0.662 1.00 92.20 ? 16 GLU B CB 1 ATOM 1959 C CG . GLU B 2 18 ? -14.615 -47.360 -1.676 1.00 89.57 ? 16 GLU B CG 1 ATOM 1960 C CD . GLU B 2 18 ? -14.913 -48.476 -2.656 1.00 92.57 ? 16 GLU B CD 1 ATOM 1961 O OE1 . GLU B 2 18 ? -16.102 -48.639 -3.010 1.00 88.09 ? 16 GLU B OE1 1 ATOM 1962 O OE2 . GLU B 2 18 ? -13.963 -49.176 -3.069 1.00 92.39 ? 16 GLU B OE2 1 ATOM 1963 N N . THR B 2 19 ? -13.906 -45.737 0.934 1.00 83.33 ? 17 THR B N 1 ATOM 1964 C CA . THR B 2 19 ? -12.809 -45.095 1.675 1.00 79.98 ? 17 THR B CA 1 ATOM 1965 C C . THR B 2 19 ? -11.436 -45.577 1.257 1.00 78.13 ? 17 THR B C 1 ATOM 1966 O O . THR B 2 19 ? -11.171 -46.782 1.268 1.00 79.26 ? 17 THR B O 1 ATOM 1967 C CB . THR B 2 19 ? -12.977 -45.276 3.195 1.00 80.59 ? 17 THR B CB 1 ATOM 1968 O OG1 . THR B 2 19 ? -14.109 -44.519 3.643 1.00 84.29 ? 17 THR B OG1 1 ATOM 1969 C CG2 . THR B 2 19 ? -11.759 -44.795 3.922 1.00 73.32 ? 17 THR B CG2 1 ATOM 1970 N N . ALA B 2 20 ? -10.566 -44.616 0.928 1.00 76.36 ? 18 ALA B N 1 ATOM 1971 C CA . ALA B 2 20 ? -9.226 -44.928 0.431 1.00 74.26 ? 18 ALA B CA 1 ATOM 1972 C C . ALA B 2 20 ? -8.290 -44.869 1.608 1.00 73.24 ? 18 ALA B C 1 ATOM 1973 O O . ALA B 2 20 ? -8.345 -43.889 2.359 1.00 75.16 ? 18 ALA B O 1 ATOM 1974 C CB . ALA B 2 20 ? -8.799 -43.930 -0.651 1.00 72.98 ? 18 ALA B CB 1 ATOM 1975 N N . TYR B 2 21 ? -7.452 -45.910 1.727 1.00 73.09 ? 19 TYR B N 1 ATOM 1976 C CA . TYR B 2 21 ? -6.375 -46.001 2.746 1.00 71.72 ? 19 TYR B CA 1 ATOM 1977 C C . TYR B 2 21 ? -4.973 -45.776 2.185 1.00 66.94 ? 19 TYR B C 1 ATOM 1978 O O . TYR B 2 21 ? -4.443 -46.604 1.435 1.00 63.81 ? 19 TYR B O 1 ATOM 1979 C CB . TYR B 2 21 ? -6.399 -47.352 3.437 1.00 74.73 ? 19 TYR B CB 1 ATOM 1980 C CG . TYR B 2 21 ? -5.276 -47.528 4.426 1.00 73.25 ? 19 TYR B CG 1 ATOM 1981 C CD1 . TYR B 2 21 ? -5.215 -46.744 5.571 1.00 77.13 ? 19 TYR B CD1 1 ATOM 1982 C CD2 . TYR B 2 21 ? -4.276 -48.470 4.216 1.00 72.83 ? 19 TYR B CD2 1 ATOM 1983 C CE1 . TYR B 2 21 ? -4.187 -46.900 6.495 1.00 75.41 ? 19 TYR B CE1 1 ATOM 1984 C CE2 . TYR B 2 21 ? -3.251 -48.642 5.137 1.00 72.69 ? 19 TYR B CE2 1 ATOM 1985 C CZ . TYR B 2 21 ? -3.213 -47.848 6.272 1.00 74.17 ? 19 TYR B CZ 1 ATOM 1986 O OH . TYR B 2 21 ? -2.201 -47.990 7.191 1.00 79.25 ? 19 TYR B OH 1 ATOM 1987 N N . LEU B 2 22 ? -4.378 -44.658 2.598 1.00 65.95 ? 20 LEU B N 1 ATOM 1988 C CA . LEU B 2 22 ? -3.075 -44.259 2.085 1.00 64.12 ? 20 LEU B CA 1 ATOM 1989 C C . LEU B 2 22 ? -2.070 -44.359 3.228 1.00 61.23 ? 20 LEU B C 1 ATOM 1990 O O . LEU B 2 22 ? -2.124 -43.554 4.148 1.00 60.39 ? 20 LEU B O 1 ATOM 1991 C CB . LEU B 2 22 ? -3.134 -42.815 1.519 1.00 63.74 ? 20 LEU B CB 1 ATOM 1992 C CG . LEU B 2 22 ? -4.065 -42.582 0.281 1.00 69.63 ? 20 LEU B CG 1 ATOM 1993 C CD1 . LEU B 2 22 ? -4.247 -41.079 0.045 1.00 66.68 ? 20 LEU B CD1 1 ATOM 1994 C CD2 . LEU B 2 22 ? -3.447 -43.204 -0.962 1.00 67.37 ? 20 LEU B CD2 1 ATOM 1995 N N . PRO B 2 23 ? -1.182 -45.368 3.182 1.00 61.43 ? 21 PRO B N 1 ATOM 1996 C CA . PRO B 2 23 ? -0.142 -45.590 4.200 1.00 61.65 ? 21 PRO B CA 1 ATOM 1997 C C . PRO B 2 23 ? 1.072 -44.681 4.123 1.00 58.62 ? 21 PRO B C 1 ATOM 1998 O O . PRO B 2 23 ? 1.695 -44.519 3.076 1.00 55.55 ? 21 PRO B O 1 ATOM 1999 C CB . PRO B 2 23 ? 0.301 -47.026 3.925 1.00 63.48 ? 21 PRO B CB 1 ATOM 2000 C CG . PRO B 2 23 ? 0.103 -47.193 2.483 1.00 63.67 ? 21 PRO B CG 1 ATOM 2001 C CD . PRO B 2 23 ? -1.111 -46.386 2.115 1.00 61.52 ? 21 PRO B CD 1 ATOM 2002 N N . CYS B 2 24 ? 1.394 -44.109 5.272 1.00 59.10 ? 22 CYS B N 1 ATOM 2003 C CA . CYS B 2 24 ? 2.550 -43.225 5.399 1.00 57.96 ? 22 CYS B CA 1 ATOM 2004 C C . CYS B 2 24 ? 3.153 -43.325 6.793 1.00 57.35 ? 22 CYS B C 1 ATOM 2005 O O . CYS B 2 24 ? 2.979 -42.453 7.652 1.00 56.59 ? 22 CYS B O 1 ATOM 2006 C CB . CYS B 2 24 ? 2.129 -41.793 5.063 1.00 58.08 ? 22 CYS B CB 1 ATOM 2007 S SG . CYS B 2 24 ? 3.436 -40.608 4.883 1.00 53.66 ? 22 CYS B SG 1 ATOM 2008 N N . LYS B 2 25 ? 3.862 -44.425 6.990 1.00 58.05 ? 23 LYS B N 1 ATOM 2009 C CA . LYS B 2 25 ? 4.522 -44.721 8.257 1.00 59.38 ? 23 LYS B CA 1 ATOM 2010 C C . LYS B 2 25 ? 5.996 -44.329 8.223 1.00 57.81 ? 23 LYS B C 1 ATOM 2011 O O . LYS B 2 25 ? 6.714 -44.564 7.236 1.00 56.27 ? 23 LYS B O 1 ATOM 2012 C CB . LYS B 2 25 ? 4.371 -46.203 8.594 1.00 62.03 ? 23 LYS B CB 1 ATOM 2013 C CG . LYS B 2 25 ? 2.922 -46.644 8.840 1.00 66.29 ? 23 LYS B CG 1 ATOM 2014 C CD . LYS B 2 25 ? 2.867 -48.134 9.113 1.00 70.07 ? 23 LYS B CD 1 ATOM 2015 C CE . LYS B 2 25 ? 1.469 -48.607 9.431 1.00 75.43 ? 23 LYS B CE 1 ATOM 2016 N NZ . LYS B 2 25 ? 1.423 -50.090 9.598 1.00 79.97 ? 23 LYS B NZ 1 ATOM 2017 N N . PHE B 2 26 ? 6.435 -43.722 9.320 1.00 57.07 ? 24 PHE B N 1 ATOM 2018 C CA . PHE B 2 26 ? 7.792 -43.192 9.410 1.00 54.72 ? 24 PHE B CA 1 ATOM 2019 C C . PHE B 2 26 ? 8.503 -43.519 10.715 1.00 55.17 ? 24 PHE B C 1 ATOM 2020 O O . PHE B 2 26 ? 7.888 -43.702 11.766 1.00 56.82 ? 24 PHE B O 1 ATOM 2021 C CB . PHE B 2 26 ? 7.772 -41.681 9.201 1.00 53.04 ? 24 PHE B CB 1 ATOM 2022 C CG . PHE B 2 26 ? 7.057 -40.934 10.280 1.00 54.45 ? 24 PHE B CG 1 ATOM 2023 C CD1 . PHE B 2 26 ? 7.718 -40.562 11.437 1.00 57.39 ? 24 PHE B CD1 1 ATOM 2024 C CD2 . PHE B 2 26 ? 5.731 -40.599 10.138 1.00 60.00 ? 24 PHE B CD2 1 ATOM 2025 C CE1 . PHE B 2 26 ? 7.066 -39.875 12.435 1.00 62.97 ? 24 PHE B CE1 1 ATOM 2026 C CE2 . PHE B 2 26 ? 5.065 -39.910 11.136 1.00 67.04 ? 24 PHE B CE2 1 ATOM 2027 C CZ . PHE B 2 26 ? 5.736 -39.549 12.290 1.00 67.16 ? 24 PHE B CZ 1 ATOM 2028 N N . THR B 2 27 ? 9.821 -43.600 10.602 1.00 54.22 ? 25 THR B N 1 ATOM 2029 C CA . THR B 2 27 ? 10.714 -43.855 11.722 1.00 54.57 ? 25 THR B CA 1 ATOM 2030 C C . THR B 2 27 ? 11.680 -42.703 11.867 1.00 53.52 ? 25 THR B C 1 ATOM 2031 O O . THR B 2 27 ? 12.502 -42.456 10.981 1.00 53.09 ? 25 THR B O 1 ATOM 2032 C CB . THR B 2 27 ? 11.541 -45.125 11.484 1.00 55.51 ? 25 THR B CB 1 ATOM 2033 O OG1 . THR B 2 27 ? 10.679 -46.188 11.068 1.00 59.57 ? 25 THR B OG1 1 ATOM 2034 C CG2 . THR B 2 27 ? 12.269 -45.531 12.740 1.00 54.70 ? 25 THR B CG2 1 ATOM 2035 N N . LEU B 2 28 ? 11.575 -42.001 12.986 1.00 53.40 ? 26 LEU B N 1 ATOM 2036 C CA . LEU B 2 28 ? 12.449 -40.854 13.252 1.00 52.07 ? 26 LEU B CA 1 ATOM 2037 C C . LEU B 2 28 ? 13.858 -41.297 13.596 1.00 51.95 ? 26 LEU B C 1 ATOM 2038 O O . LEU B 2 28 ? 14.077 -42.358 14.172 1.00 53.82 ? 26 LEU B O 1 ATOM 2039 C CB . LEU B 2 28 ? 11.885 -39.969 14.371 1.00 52.61 ? 26 LEU B CB 1 ATOM 2040 C CG . LEU B 2 28 ? 10.621 -39.208 13.968 1.00 54.26 ? 26 LEU B CG 1 ATOM 2041 C CD1 . LEU B 2 28 ? 9.967 -38.513 15.154 1.00 47.54 ? 26 LEU B CD1 1 ATOM 2042 C CD2 . LEU B 2 28 ? 10.966 -38.195 12.869 1.00 54.95 ? 26 LEU B CD2 1 ATOM 2043 N N . SER B 2 29 ? 14.816 -40.465 13.217 1.00 50.36 ? 27 SER B N 1 ATOM 2044 C CA . SER B 2 29 ? 16.210 -40.687 13.568 1.00 50.91 ? 27 SER B CA 1 ATOM 2045 C C . SER B 2 29 ? 16.631 -39.716 14.673 1.00 49.22 ? 27 SER B C 1 ATOM 2046 O O . SER B 2 29 ? 16.040 -38.654 14.832 1.00 47.83 ? 27 SER B O 1 ATOM 2047 C CB . SER B 2 29 ? 17.102 -40.550 12.328 1.00 50.71 ? 27 SER B CB 1 ATOM 2048 O OG . SER B 2 29 ? 16.864 -41.624 11.430 1.00 54.71 ? 27 SER B OG 1 ATOM 2049 N N . PRO B 2 30 ? 17.646 -40.094 15.455 1.00 48.68 ? 28 PRO B N 1 ATOM 2050 C CA . PRO B 2 30 ? 18.074 -39.330 16.620 1.00 49.75 ? 28 PRO B CA 1 ATOM 2051 C C . PRO B 2 30 ? 18.311 -37.844 16.343 1.00 48.77 ? 28 PRO B C 1 ATOM 2052 O O . PRO B 2 30 ? 18.085 -37.011 17.208 1.00 49.29 ? 28 PRO B O 1 ATOM 2053 C CB . PRO B 2 30 ? 19.390 -40.014 17.013 1.00 51.79 ? 28 PRO B CB 1 ATOM 2054 C CG . PRO B 2 30 ? 19.252 -41.421 16.520 1.00 49.91 ? 28 PRO B CG 1 ATOM 2055 C CD . PRO B 2 30 ? 18.431 -41.330 15.275 1.00 48.96 ? 28 PRO B CD 1 ATOM 2056 N N . GLU B 2 31 ? 18.770 -37.523 15.145 1.00 48.11 ? 29 GLU B N 1 ATOM 2057 C CA . GLU B 2 31 ? 19.045 -36.131 14.776 1.00 48.55 ? 29 GLU B CA 1 ATOM 2058 C C . GLU B 2 31 ? 17.749 -35.349 14.829 1.00 49.50 ? 29 GLU B C 1 ATOM 2059 O O . GLU B 2 31 ? 17.713 -34.169 15.167 1.00 50.93 ? 29 GLU B O 1 ATOM 2060 C CB . GLU B 2 31 ? 19.568 -36.020 13.339 1.00 47.61 ? 29 GLU B CB 1 ATOM 2061 C CG . GLU B 2 31 ? 20.675 -36.983 12.953 1.00 54.29 ? 29 GLU B CG 1 ATOM 2062 C CD . GLU B 2 31 ? 20.160 -38.291 12.386 1.00 60.94 ? 29 GLU B CD 1 ATOM 2063 O OE1 . GLU B 2 31 ? 19.803 -38.325 11.184 1.00 60.98 ? 29 GLU B OE1 1 ATOM 2064 O OE2 . GLU B 2 31 ? 20.140 -39.289 13.145 1.00 66.39 ? 29 GLU B OE2 1 ATOM 2065 N N . ASP B 2 32 ? 16.680 -36.049 14.483 1.00 49.66 ? 30 ASP B N 1 ATOM 2066 C CA . ASP B 2 32 ? 15.427 -35.422 14.091 1.00 49.74 ? 30 ASP B CA 1 ATOM 2067 C C . ASP B 2 32 ? 14.731 -34.866 15.313 1.00 51.28 ? 30 ASP B C 1 ATOM 2068 O O . ASP B 2 32 ? 13.913 -35.532 15.951 1.00 52.41 ? 30 ASP B O 1 ATOM 2069 C CB . ASP B 2 32 ? 14.525 -36.422 13.343 1.00 49.72 ? 30 ASP B CB 1 ATOM 2070 C CG . ASP B 2 32 ? 15.168 -36.946 12.055 1.00 49.42 ? 30 ASP B CG 1 ATOM 2071 O OD1 . ASP B 2 32 ? 16.023 -36.229 11.492 1.00 59.65 ? 30 ASP B OD1 1 ATOM 2072 O OD2 . ASP B 2 32 ? 14.830 -38.067 11.605 1.00 40.65 ? 30 ASP B OD2 1 ATOM 2073 N N . GLN B 2 33 ? 15.053 -33.615 15.606 1.00 51.08 ? 31 GLN B N 1 ATOM 2074 C CA . GLN B 2 33 ? 14.682 -33.003 16.871 1.00 51.82 ? 31 GLN B CA 1 ATOM 2075 C C . GLN B 2 33 ? 13.710 -31.845 16.727 1.00 50.96 ? 31 GLN B C 1 ATOM 2076 O O . GLN B 2 33 ? 13.112 -31.422 17.701 1.00 53.43 ? 31 GLN B O 1 ATOM 2077 C CB . GLN B 2 33 ? 15.941 -32.503 17.569 1.00 52.42 ? 31 GLN B CB 1 ATOM 2078 C CG . GLN B 2 33 ? 16.060 -32.974 19.004 1.00 57.86 ? 31 GLN B CG 1 ATOM 2079 C CD . GLN B 2 33 ? 16.255 -34.478 19.104 1.00 57.43 ? 31 GLN B CD 1 ATOM 2080 O OE1 . GLN B 2 33 ? 15.638 -35.149 19.935 1.00 53.25 ? 31 GLN B OE1 1 ATOM 2081 N NE2 . GLN B 2 33 ? 17.113 -35.014 18.244 1.00 55.55 ? 31 GLN B NE2 1 ATOM 2082 N N . GLY B 2 34 ? 13.557 -31.333 15.514 1.00 48.74 ? 32 GLY B N 1 ATOM 2083 C CA . GLY B 2 34 ? 12.684 -30.183 15.262 1.00 48.32 ? 32 GLY B CA 1 ATOM 2084 C C . GLY B 2 34 ? 11.206 -30.450 15.503 1.00 48.15 ? 32 GLY B C 1 ATOM 2085 O O . GLY B 2 34 ? 10.810 -31.546 15.901 1.00 48.30 ? 32 GLY B O 1 ATOM 2086 N N . PRO B 2 35 ? 10.366 -29.440 15.277 1.00 47.37 ? 33 PRO B N 1 ATOM 2087 C CA . PRO B 2 35 ? 8.950 -29.718 15.467 1.00 48.11 ? 33 PRO B CA 1 ATOM 2088 C C . PRO B 2 35 ? 8.469 -30.721 14.443 1.00 46.78 ? 33 PRO B C 1 ATOM 2089 O O . PRO B 2 35 ? 8.801 -30.602 13.257 1.00 46.62 ? 33 PRO B O 1 ATOM 2090 C CB . PRO B 2 35 ? 8.286 -28.355 15.251 1.00 48.67 ? 33 PRO B CB 1 ATOM 2091 C CG . PRO B 2 35 ? 9.390 -27.347 15.431 1.00 48.55 ? 33 PRO B CG 1 ATOM 2092 C CD . PRO B 2 35 ? 10.626 -28.029 14.955 1.00 47.07 ? 33 PRO B CD 1 ATOM 2093 N N . LEU B 2 36 ? 7.718 -31.714 14.905 1.00 46.39 ? 34 LEU B N 1 ATOM 2094 C CA . LEU B 2 36 ? 7.066 -32.655 13.998 1.00 45.38 ? 34 LEU B CA 1 ATOM 2095 C C . LEU B 2 36 ? 5.977 -31.930 13.259 1.00 47.14 ? 34 LEU B C 1 ATOM 2096 O O . LEU B 2 36 ? 5.231 -31.127 13.833 1.00 48.15 ? 34 LEU B O 1 ATOM 2097 C CB . LEU B 2 36 ? 6.439 -33.838 14.724 1.00 47.05 ? 34 LEU B CB 1 ATOM 2098 C CG . LEU B 2 36 ? 5.650 -34.771 13.799 1.00 46.36 ? 34 LEU B CG 1 ATOM 2099 C CD1 . LEU B 2 36 ? 6.595 -35.679 13.008 1.00 40.73 ? 34 LEU B CD1 1 ATOM 2100 C CD2 . LEU B 2 36 ? 4.673 -35.591 14.600 1.00 49.83 ? 34 LEU B CD2 1 ATOM 2101 N N . ASP B 2 37 ? 5.881 -32.240 11.974 1.00 46.71 ? 35 ASP B N 1 ATOM 2102 C CA . ASP B 2 37 ? 4.922 -31.572 11.119 1.00 47.56 ? 35 ASP B CA 1 ATOM 2103 C C . ASP B 2 37 ? 4.544 -32.378 9.898 1.00 45.77 ? 35 ASP B C 1 ATOM 2104 O O . ASP B 2 37 ? 5.382 -32.711 9.080 1.00 43.92 ? 35 ASP B O 1 ATOM 2105 C CB . ASP B 2 37 ? 5.492 -30.242 10.684 1.00 47.94 ? 35 ASP B CB 1 ATOM 2106 C CG . ASP B 2 37 ? 4.510 -29.450 9.880 1.00 54.07 ? 35 ASP B CG 1 ATOM 2107 O OD1 . ASP B 2 37 ? 3.958 -30.029 8.919 1.00 58.45 ? 35 ASP B OD1 1 ATOM 2108 O OD2 . ASP B 2 37 ? 4.275 -28.265 10.214 1.00 58.80 ? 35 ASP B OD2 1 ATOM 2109 N N . ILE B 2 38 ? 3.257 -32.668 9.783 1.00 47.96 ? 36 ILE B N 1 ATOM 2110 C CA . ILE B 2 38 ? 2.737 -33.439 8.662 1.00 48.01 ? 36 ILE B CA 1 ATOM 2111 C C . ILE B 2 38 ? 1.757 -32.634 7.845 1.00 50.06 ? 36 ILE B C 1 ATOM 2112 O O . ILE B 2 38 ? 0.961 -31.861 8.375 1.00 51.77 ? 36 ILE B O 1 ATOM 2113 C CB . ILE B 2 38 ? 2.021 -34.716 9.116 1.00 48.55 ? 36 ILE B CB 1 ATOM 2114 C CG1 . ILE B 2 38 ? 2.951 -35.578 9.976 1.00 48.64 ? 36 ILE B CG1 1 ATOM 2115 C CG2 . ILE B 2 38 ? 1.539 -35.482 7.893 1.00 46.67 ? 36 ILE B CG2 1 ATOM 2116 C CD1 . ILE B 2 38 ? 2.236 -36.287 11.130 1.00 45.81 ? 36 ILE B CD1 1 ATOM 2117 N N . GLU B 2 39 ? 1.821 -32.841 6.540 1.00 49.81 ? 37 GLU B N 1 ATOM 2118 C CA . GLU B 2 39 ? 1.003 -32.079 5.609 1.00 51.34 ? 37 GLU B CA 1 ATOM 2119 C C . GLU B 2 39 ? 0.640 -32.910 4.385 1.00 49.60 ? 37 GLU B C 1 ATOM 2120 O O . GLU B 2 39 ? 1.499 -33.265 3.585 1.00 50.23 ? 37 GLU B O 1 ATOM 2121 C CB . GLU B 2 39 ? 1.746 -30.798 5.196 1.00 51.77 ? 37 GLU B CB 1 ATOM 2122 C CG . GLU B 2 39 ? 0.830 -29.684 4.692 1.00 57.32 ? 37 GLU B CG 1 ATOM 2123 C CD . GLU B 2 39 ? 1.574 -28.464 4.129 1.00 62.89 ? 37 GLU B CD 1 ATOM 2124 O OE1 . GLU B 2 39 ? 2.705 -28.613 3.609 1.00 65.15 ? 37 GLU B OE1 1 ATOM 2125 O OE2 . GLU B 2 39 ? 1.009 -27.347 4.197 1.00 66.85 ? 37 GLU B OE2 1 ATOM 2126 N N . TRP B 2 40 ? -0.641 -33.234 4.259 1.00 49.90 ? 38 TRP B N 1 ATOM 2127 C CA . TRP B 2 40 ? -1.147 -33.957 3.079 1.00 48.26 ? 38 TRP B CA 1 ATOM 2128 C C . TRP B 2 40 ? -1.625 -32.977 2.026 1.00 51.49 ? 38 TRP B C 1 ATOM 2129 O O . TRP B 2 40 ? -2.377 -32.037 2.324 1.00 55.09 ? 38 TRP B O 1 ATOM 2130 C CB . TRP B 2 40 ? -2.292 -34.930 3.422 1.00 46.10 ? 38 TRP B CB 1 ATOM 2131 C CG . TRP B 2 40 ? -1.852 -36.198 4.062 1.00 29.39 ? 38 TRP B CG 1 ATOM 2132 C CD1 . TRP B 2 40 ? -1.649 -36.401 5.383 1.00 36.03 ? 38 TRP B CD1 1 ATOM 2133 C CD2 . TRP B 2 40 ? -1.611 -37.459 3.424 1.00 24.06 ? 38 TRP B CD2 1 ATOM 2134 N NE1 . TRP B 2 40 ? -1.268 -37.688 5.614 1.00 27.57 ? 38 TRP B NE1 1 ATOM 2135 C CE2 . TRP B 2 40 ? -1.231 -38.365 4.429 1.00 34.15 ? 38 TRP B CE2 1 ATOM 2136 C CE3 . TRP B 2 40 ? -1.642 -37.898 2.101 1.00 26.81 ? 38 TRP B CE3 1 ATOM 2137 C CZ2 . TRP B 2 40 ? -0.861 -39.681 4.156 1.00 34.73 ? 38 TRP B CZ2 1 ATOM 2138 C CZ3 . TRP B 2 40 ? -1.304 -39.217 1.827 1.00 30.58 ? 38 TRP B CZ3 1 ATOM 2139 C CH2 . TRP B 2 40 ? -0.919 -40.092 2.852 1.00 35.82 ? 38 TRP B CH2 1 ATOM 2140 N N . LEU B 2 41 ? -1.180 -33.213 0.795 1.00 50.82 ? 39 LEU B N 1 ATOM 2141 C CA . LEU B 2 41 ? -1.580 -32.390 -0.337 1.00 51.96 ? 39 LEU B CA 1 ATOM 2142 C C . LEU B 2 41 ? -2.285 -33.185 -1.416 1.00 52.89 ? 39 LEU B C 1 ATOM 2143 O O . LEU B 2 41 ? -1.844 -34.269 -1.794 1.00 50.86 ? 39 LEU B O 1 ATOM 2144 C CB . LEU B 2 41 ? -0.358 -31.720 -0.938 1.00 50.81 ? 39 LEU B CB 1 ATOM 2145 C CG . LEU B 2 41 ? 0.449 -30.835 -0.006 1.00 48.07 ? 39 LEU B CG 1 ATOM 2146 C CD1 . LEU B 2 41 ? 1.745 -30.513 -0.704 1.00 49.65 ? 39 LEU B CD1 1 ATOM 2147 C CD2 . LEU B 2 41 ? -0.304 -29.566 0.345 1.00 48.12 ? 39 LEU B CD2 1 ATOM 2148 N N . ILE B 2 42 ? -3.392 -32.625 -1.893 1.00 55.84 ? 40 ILE B N 1 ATOM 2149 C CA . ILE B 2 42 ? -4.097 -33.160 -3.068 1.00 57.90 ? 40 ILE B CA 1 ATOM 2150 C C . ILE B 2 42 ? -3.749 -32.346 -4.290 1.00 58.45 ? 40 ILE B C 1 ATOM 2151 O O . ILE B 2 42 ? -3.656 -31.118 -4.234 1.00 58.56 ? 40 ILE B O 1 ATOM 2152 C CB . ILE B 2 42 ? -5.642 -33.162 -2.919 1.00 60.83 ? 40 ILE B CB 1 ATOM 2153 C CG1 . ILE B 2 42 ? -6.287 -33.971 -4.066 1.00 60.92 ? 40 ILE B CG1 1 ATOM 2154 C CG2 . ILE B 2 42 ? -6.193 -31.730 -2.883 1.00 63.36 ? 40 ILE B CG2 1 ATOM 2155 C CD1 . ILE B 2 42 ? -7.796 -33.863 -4.142 1.00 56.16 ? 40 ILE B CD1 1 ATOM 2156 N N . SER B 2 43 ? -3.556 -33.065 -5.390 1.00 59.52 ? 41 SER B N 1 ATOM 2157 C CA . SER B 2 43 ? -3.215 -32.465 -6.673 1.00 61.86 ? 41 SER B CA 1 ATOM 2158 C C . SER B 2 43 ? -4.280 -32.829 -7.706 1.00 65.91 ? 41 SER B C 1 ATOM 2159 O O . SER B 2 43 ? -4.130 -33.795 -8.459 1.00 64.16 ? 41 SER B O 1 ATOM 2160 C CB . SER B 2 43 ? -1.834 -32.945 -7.125 1.00 59.35 ? 41 SER B CB 1 ATOM 2161 O OG . SER B 2 43 ? -1.265 -32.051 -8.061 1.00 62.35 ? 41 SER B OG 1 ATOM 2162 N N . PRO B 2 44 ? -5.375 -32.054 -7.738 1.00 71.95 ? 42 PRO B N 1 ATOM 2163 C CA . PRO B 2 44 ? -6.497 -32.350 -8.625 1.00 76.69 ? 42 PRO B CA 1 ATOM 2164 C C . PRO B 2 44 ? -6.073 -32.480 -10.073 1.00 78.64 ? 42 PRO B C 1 ATOM 2165 O O . PRO B 2 44 ? -5.346 -31.632 -10.590 1.00 77.11 ? 42 PRO B O 1 ATOM 2166 C CB . PRO B 2 44 ? -7.414 -31.136 -8.448 1.00 79.22 ? 42 PRO B CB 1 ATOM 2167 C CG . PRO B 2 44 ? -7.072 -30.583 -7.122 1.00 76.89 ? 42 PRO B CG 1 ATOM 2168 C CD . PRO B 2 44 ? -5.613 -30.839 -6.939 1.00 72.96 ? 42 PRO B CD 1 ATOM 2169 N N . SER B 2 45 ? -6.543 -33.558 -10.695 1.00 81.72 ? 43 SER B N 1 ATOM 2170 C CA . SER B 2 45 ? -6.230 -33.894 -12.083 1.00 84.28 ? 43 SER B CA 1 ATOM 2171 C C . SER B 2 45 ? -4.733 -33.777 -12.350 1.00 83.57 ? 43 SER B C 1 ATOM 2172 O O . SER B 2 45 ? -4.289 -33.684 -13.495 1.00 85.07 ? 43 SER B O 1 ATOM 2173 C CB . SER B 2 45 ? -7.025 -33.007 -13.043 1.00 87.65 ? 43 SER B CB 1 ATOM 2174 O OG . SER B 2 45 ? -8.423 -33.193 -12.870 1.00 90.56 ? 43 SER B OG 1 ATOM 2175 N N . ASP B 2 46 ? -3.975 -33.765 -11.262 1.00 82.58 ? 44 ASP B N 1 ATOM 2176 C CA . ASP B 2 46 ? -2.516 -33.805 -11.291 1.00 83.42 ? 44 ASP B CA 1 ATOM 2177 C C . ASP B 2 46 ? -1.825 -32.573 -11.846 1.00 84.38 ? 44 ASP B C 1 ATOM 2178 O O . ASP B 2 46 ? -0.609 -32.612 -12.057 1.00 85.31 ? 44 ASP B O 1 ATOM 2179 C CB . ASP B 2 46 ? -2.025 -35.018 -12.086 1.00 84.54 ? 44 ASP B CB 1 ATOM 2180 C CG . ASP B 2 46 ? -2.578 -36.318 -11.558 1.00 89.77 ? 44 ASP B CG 1 ATOM 2181 O OD1 . ASP B 2 46 ? -3.447 -36.275 -10.659 1.00 93.16 ? 44 ASP B OD1 1 ATOM 2182 O OD2 . ASP B 2 46 ? -2.141 -37.381 -12.046 1.00 98.64 ? 44 ASP B OD2 1 ATOM 2183 N N . ASN B 2 47 ? -2.563 -31.488 -12.082 1.00 85.59 ? 45 ASN B N 1 ATOM 2184 C CA . ASN B 2 47 ? -1.936 -30.262 -12.621 1.00 84.14 ? 45 ASN B CA 1 ATOM 2185 C C . ASN B 2 47 ? -0.723 -29.880 -11.777 1.00 81.39 ? 45 ASN B C 1 ATOM 2186 O O . ASN B 2 47 ? -0.781 -29.801 -10.542 1.00 80.12 ? 45 ASN B O 1 ATOM 2187 C CB . ASN B 2 47 ? -2.922 -29.092 -12.752 1.00 85.67 ? 45 ASN B CB 1 ATOM 2188 C CG . ASN B 2 47 ? -3.230 -28.417 -11.428 1.00 82.15 ? 45 ASN B CG 1 ATOM 2189 O OD1 . ASN B 2 47 ? -3.128 -27.199 -11.303 1.00 77.76 ? 45 ASN B OD1 1 ATOM 2190 N ND2 . ASN B 2 47 ? -3.629 -29.202 -10.439 1.00 81.94 ? 45 ASN B ND2 1 ATOM 2191 N N . GLN B 2 48 ? 0.383 -29.672 -12.469 1.00 79.56 ? 46 GLN B N 1 ATOM 2192 C CA . GLN B 2 48 ? 1.687 -29.640 -11.825 1.00 76.95 ? 46 GLN B CA 1 ATOM 2193 C C . GLN B 2 48 ? 2.075 -28.232 -11.407 1.00 74.94 ? 46 GLN B C 1 ATOM 2194 O O . GLN B 2 48 ? 3.217 -27.977 -11.032 1.00 74.99 ? 46 GLN B O 1 ATOM 2195 C CB . GLN B 2 48 ? 2.748 -30.235 -12.753 1.00 77.73 ? 46 GLN B CB 1 ATOM 2196 C CG . GLN B 2 48 ? 2.624 -31.751 -12.940 1.00 81.35 ? 46 GLN B CG 1 ATOM 2197 C CD . GLN B 2 48 ? 3.198 -32.230 -14.267 1.00 86.77 ? 46 GLN B CD 1 ATOM 2198 O OE1 . GLN B 2 48 ? 2.826 -31.730 -15.331 1.00 90.77 ? 46 GLN B OE1 1 ATOM 2199 N NE2 . GLN B 2 48 ? 4.106 -33.205 -14.209 1.00 88.55 ? 46 GLN B NE2 1 ATOM 2200 N N . ILE B 2 49 ? 1.116 -27.321 -11.454 1.00 73.13 ? 47 ILE B N 1 ATOM 2201 C CA . ILE B 2 49 ? 1.374 -25.947 -11.039 1.00 70.78 ? 47 ILE B CA 1 ATOM 2202 C C . ILE B 2 49 ? 0.927 -25.725 -9.602 1.00 68.40 ? 47 ILE B C 1 ATOM 2203 O O . ILE B 2 49 ? 1.472 -24.882 -8.895 1.00 66.23 ? 47 ILE B O 1 ATOM 2204 C CB . ILE B 2 49 ? 0.662 -24.942 -11.948 1.00 73.32 ? 47 ILE B CB 1 ATOM 2205 C CG1 . ILE B 2 49 ? 1.198 -25.049 -13.381 1.00 74.75 ? 47 ILE B CG1 1 ATOM 2206 C CG2 . ILE B 2 49 ? 0.856 -23.543 -11.417 1.00 72.34 ? 47 ILE B CG2 1 ATOM 2207 C CD1 . ILE B 2 49 ? 0.232 -24.557 -14.446 1.00 75.30 ? 47 ILE B CD1 1 ATOM 2208 N N . VAL B 2 50 ? -0.069 -26.489 -9.170 1.00 67.64 ? 48 VAL B N 1 ATOM 2209 C CA . VAL B 2 50 ? -0.657 -26.271 -7.850 1.00 66.35 ? 48 VAL B CA 1 ATOM 2210 C C . VAL B 2 50 ? -1.127 -27.531 -7.166 1.00 65.60 ? 48 VAL B C 1 ATOM 2211 O O . VAL B 2 50 ? -1.721 -28.417 -7.781 1.00 66.68 ? 48 VAL B O 1 ATOM 2212 C CB . VAL B 2 50 ? -1.868 -25.320 -7.910 1.00 68.80 ? 48 VAL B CB 1 ATOM 2213 C CG1 . VAL B 2 50 ? -2.363 -25.041 -6.515 1.00 66.14 ? 48 VAL B CG1 1 ATOM 2214 C CG2 . VAL B 2 50 ? -1.511 -24.019 -8.611 1.00 70.68 ? 48 VAL B CG2 1 ATOM 2215 N N . ASP B 2 51 ? -0.848 -27.586 -5.872 1.00 64.36 ? 49 ASP B N 1 ATOM 2216 C CA . ASP B 2 51 ? -1.421 -28.589 -4.979 1.00 63.73 ? 49 ASP B CA 1 ATOM 2217 C C . ASP B 2 51 ? -2.216 -27.880 -3.889 1.00 63.65 ? 49 ASP B C 1 ATOM 2218 O O . ASP B 2 51 ? -2.060 -26.673 -3.663 1.00 64.72 ? 49 ASP B O 1 ATOM 2219 C CB . ASP B 2 51 ? -0.323 -29.437 -4.336 1.00 62.21 ? 49 ASP B CB 1 ATOM 2220 C CG . ASP B 2 51 ? 0.584 -30.114 -5.355 1.00 65.04 ? 49 ASP B CG 1 ATOM 2221 O OD1 . ASP B 2 51 ? 0.105 -30.461 -6.461 1.00 69.90 ? 49 ASP B OD1 1 ATOM 2222 O OD2 . ASP B 2 51 ? 1.780 -30.318 -5.030 1.00 66.33 ? 49 ASP B OD2 1 ATOM 2223 N N . GLN B 2 52 ? -3.078 -28.632 -3.218 1.00 62.45 ? 50 GLN B N 1 ATOM 2224 C CA . GLN B 2 52 ? -3.830 -28.091 -2.087 1.00 63.73 ? 50 GLN B CA 1 ATOM 2225 C C . GLN B 2 52 ? -3.691 -28.938 -0.851 1.00 61.00 ? 50 GLN B C 1 ATOM 2226 O O . GLN B 2 52 ? -3.623 -30.167 -0.917 1.00 59.23 ? 50 GLN B O 1 ATOM 2227 C CB . GLN B 2 52 ? -5.309 -27.918 -2.429 1.00 67.55 ? 50 GLN B CB 1 ATOM 2228 C CG . GLN B 2 52 ? -5.619 -26.518 -2.902 1.00 73.22 ? 50 GLN B CG 1 ATOM 2229 C CD . GLN B 2 52 ? -7.079 -26.302 -3.215 1.00 80.12 ? 50 GLN B CD 1 ATOM 2230 O OE1 . GLN B 2 52 ? -7.695 -25.364 -2.713 1.00 86.44 ? 50 GLN B OE1 1 ATOM 2231 N NE2 . GLN B 2 52 ? -7.642 -27.161 -4.056 1.00 80.96 ? 50 GLN B NE2 1 ATOM 2232 N N . VAL B 2 53 ? -3.637 -28.252 0.281 1.00 60.21 ? 51 VAL B N 1 ATOM 2233 C CA . VAL B 2 53 ? -3.581 -28.924 1.568 1.00 58.94 ? 51 VAL B CA 1 ATOM 2234 C C . VAL B 2 53 ? -4.969 -29.413 1.924 1.00 61.50 ? 51 VAL B C 1 ATOM 2235 O O . VAL B 2 53 ? -5.948 -28.671 1.859 1.00 63.64 ? 51 VAL B O 1 ATOM 2236 C CB . VAL B 2 53 ? -3.060 -28.018 2.707 1.00 59.50 ? 51 VAL B CB 1 ATOM 2237 C CG1 . VAL B 2 53 ? -3.075 -28.783 4.026 1.00 55.58 ? 51 VAL B CG1 1 ATOM 2238 C CG2 . VAL B 2 53 ? -1.656 -27.487 2.395 1.00 53.08 ? 51 VAL B CG2 1 ATOM 2239 N N . ILE B 2 54 ? -5.038 -30.679 2.298 1.00 60.97 ? 52 ILE B N 1 ATOM 2240 C CA . ILE B 2 54 ? -6.280 -31.261 2.759 1.00 63.57 ? 52 ILE B CA 1 ATOM 2241 C C . ILE B 2 54 ? -6.224 -31.394 4.284 1.00 65.20 ? 52 ILE B C 1 ATOM 2242 O O . ILE B 2 54 ? -7.042 -30.811 4.991 1.00 69.06 ? 52 ILE B O 1 ATOM 2243 C CB . ILE B 2 54 ? -6.596 -32.580 2.017 1.00 62.86 ? 52 ILE B CB 1 ATOM 2244 C CG1 . ILE B 2 54 ? -5.681 -33.740 2.423 1.00 57.11 ? 52 ILE B CG1 1 ATOM 2245 C CG2 . ILE B 2 54 ? -6.462 -32.357 0.527 1.00 64.03 ? 52 ILE B CG2 1 ATOM 2246 C CD1 . ILE B 2 54 ? -5.803 -34.955 1.507 1.00 50.07 ? 52 ILE B CD1 1 ATOM 2247 N N . ILE B 2 55 ? -5.221 -32.102 4.782 1.00 63.07 ? 53 ILE B N 1 ATOM 2248 C CA . ILE B 2 55 ? -5.017 -32.229 6.224 1.00 62.89 ? 53 ILE B CA 1 ATOM 2249 C C . ILE B 2 55 ? -3.577 -31.926 6.639 1.00 61.24 ? 53 ILE B C 1 ATOM 2250 O O . ILE B 2 55 ? -2.622 -32.234 5.930 1.00 58.66 ? 53 ILE B O 1 ATOM 2251 C CB . ILE B 2 55 ? -5.424 -33.619 6.747 1.00 62.64 ? 53 ILE B CB 1 ATOM 2252 C CG1 . ILE B 2 55 ? -5.736 -33.529 8.249 1.00 66.63 ? 53 ILE B CG1 1 ATOM 2253 C CG2 . ILE B 2 55 ? -4.340 -34.628 6.480 1.00 58.80 ? 53 ILE B CG2 1 ATOM 2254 C CD1 . ILE B 2 55 ? -6.208 -34.819 8.890 1.00 69.98 ? 53 ILE B CD1 1 ATOM 2255 N N . LEU B 2 56 ? -3.469 -31.333 7.821 1.00 62.95 ? 54 LEU B N 1 ATOM 2256 C CA . LEU B 2 56 ? -2.210 -30.856 8.383 1.00 61.70 ? 54 LEU B CA 1 ATOM 2257 C C . LEU B 2 56 ? -2.109 -31.189 9.877 1.00 64.05 ? 54 LEU B C 1 ATOM 2258 O O . LEU B 2 56 ? -3.100 -31.170 10.609 1.00 67.28 ? 54 LEU B O 1 ATOM 2259 C CB . LEU B 2 56 ? -2.102 -29.343 8.156 1.00 62.05 ? 54 LEU B CB 1 ATOM 2260 C CG . LEU B 2 56 ? -1.040 -28.534 8.904 1.00 62.15 ? 54 LEU B CG 1 ATOM 2261 C CD1 . LEU B 2 56 ? 0.362 -29.064 8.635 1.00 60.14 ? 54 LEU B CD1 1 ATOM 2262 C CD2 . LEU B 2 56 ? -1.132 -27.066 8.516 1.00 62.22 ? 54 LEU B CD2 1 ATOM 2263 N N . TYR B 2 57 ? -0.894 -31.500 10.309 1.00 63.05 ? 55 TYR B N 1 ATOM 2264 C CA . TYR B 2 57 ? -0.604 -31.811 11.708 1.00 64.28 ? 55 TYR B CA 1 ATOM 2265 C C . TYR B 2 57 ? 0.491 -30.881 12.210 1.00 63.27 ? 55 TYR B C 1 ATOM 2266 O O . TYR B 2 57 ? 1.601 -30.892 11.684 1.00 59.48 ? 55 TYR B O 1 ATOM 2267 C CB . TYR B 2 57 ? -0.144 -33.263 11.833 1.00 64.12 ? 55 TYR B CB 1 ATOM 2268 C CG . TYR B 2 57 ? 0.029 -33.771 13.254 1.00 66.04 ? 55 TYR B CG 1 ATOM 2269 C CD1 . TYR B 2 57 ? 1.177 -33.502 13.977 1.00 60.22 ? 55 TYR B CD1 1 ATOM 2270 C CD2 . TYR B 2 57 ? -0.959 -34.535 13.859 1.00 71.97 ? 55 TYR B CD2 1 ATOM 2271 C CE1 . TYR B 2 57 ? 1.333 -33.967 15.265 1.00 64.28 ? 55 TYR B CE1 1 ATOM 2272 C CE2 . TYR B 2 57 ? -0.811 -35.010 15.147 1.00 71.42 ? 55 TYR B CE2 1 ATOM 2273 C CZ . TYR B 2 57 ? 0.339 -34.724 15.845 1.00 69.95 ? 55 TYR B CZ 1 ATOM 2274 O OH . TYR B 2 57 ? 0.492 -35.196 17.132 1.00 71.88 ? 55 TYR B OH 1 ATOM 2275 N N . SER B 2 58 ? 0.166 -30.096 13.235 1.00 65.89 ? 56 SER B N 1 ATOM 2276 C CA . SER B 2 58 ? 1.078 -29.063 13.752 1.00 65.86 ? 56 SER B CA 1 ATOM 2277 C C . SER B 2 58 ? 0.704 -28.503 15.117 1.00 69.55 ? 56 SER B C 1 ATOM 2278 O O . SER B 2 58 ? -0.472 -28.243 15.409 1.00 72.27 ? 56 SER B O 1 ATOM 2279 C CB . SER B 2 58 ? 1.178 -27.895 12.768 1.00 65.85 ? 56 SER B CB 1 ATOM 2280 O OG . SER B 2 58 ? 1.681 -26.733 13.416 1.00 66.11 ? 56 SER B OG 1 ATOM 2281 N N . GLY B 2 59 ? 1.738 -28.286 15.926 1.00 69.91 ? 57 GLY B N 1 ATOM 2282 C CA . GLY B 2 59 ? 1.576 -27.836 17.308 1.00 74.16 ? 57 GLY B CA 1 ATOM 2283 C C . GLY B 2 59 ? 0.864 -28.941 18.048 1.00 76.62 ? 57 GLY B C 1 ATOM 2284 O O . GLY B 2 59 ? 0.155 -28.718 19.030 1.00 80.07 ? 57 GLY B O 1 ATOM 2285 N N . ASP B 2 60 ? 1.055 -30.145 17.523 1.00 75.54 ? 58 ASP B N 1 ATOM 2286 C CA . ASP B 2 60 ? 0.348 -31.332 17.977 1.00 77.44 ? 58 ASP B CA 1 ATOM 2287 C C . ASP B 2 60 ? -1.145 -31.063 18.039 1.00 78.62 ? 58 ASP B C 1 ATOM 2288 O O . ASP B 2 60 ? -1.813 -31.376 19.017 1.00 80.52 ? 58 ASP B O 1 ATOM 2289 C CB . ASP B 2 60 ? 0.882 -31.802 19.325 1.00 80.89 ? 58 ASP B CB 1 ATOM 2290 C CG . ASP B 2 60 ? 0.598 -33.269 19.577 1.00 86.95 ? 58 ASP B CG 1 ATOM 2291 O OD1 . ASP B 2 60 ? -0.429 -33.769 19.052 1.00 92.89 ? 58 ASP B OD1 1 ATOM 2292 O OD2 . ASP B 2 60 ? 1.397 -33.913 20.299 1.00 93.20 ? 58 ASP B OD2 1 ATOM 2293 N N . LYS B 2 61 ? -1.639 -30.448 16.973 1.00 77.51 ? 59 LYS B N 1 ATOM 2294 C CA . LYS B 2 61 ? -3.069 -30.273 16.745 1.00 79.77 ? 59 LYS B CA 1 ATOM 2295 C C . LYS B 2 61 ? -3.384 -30.495 15.275 1.00 77.12 ? 59 LYS B C 1 ATOM 2296 O O . LYS B 2 61 ? -2.696 -29.988 14.387 1.00 75.21 ? 59 LYS B O 1 ATOM 2297 C CB . LYS B 2 61 ? -3.541 -28.881 17.188 1.00 82.98 ? 59 LYS B CB 1 ATOM 2298 C CG . LYS B 2 61 ? -3.244 -28.564 18.649 1.00 84.82 ? 59 LYS B CG 1 ATOM 2299 C CD . LYS B 2 61 ? -4.213 -27.539 19.217 1.00 88.28 ? 59 LYS B CD 1 ATOM 2300 C CE . LYS B 2 61 ? -4.125 -27.479 20.742 1.00 91.59 ? 59 LYS B CE 1 ATOM 2301 N NZ . LYS B 2 61 ? -5.429 -27.130 21.386 1.00 89.01 ? 59 LYS B NZ 1 ATOM 2302 N N . ILE B 2 62 ? -4.430 -31.274 15.041 1.00 77.72 ? 60 ILE B N 1 ATOM 2303 C CA . ILE B 2 62 ? -4.872 -31.613 13.687 1.00 75.68 ? 60 ILE B CA 1 ATOM 2304 C C . ILE B 2 62 ? -5.688 -30.486 13.073 1.00 78.14 ? 60 ILE B C 1 ATOM 2305 O O . ILE B 2 62 ? -6.322 -29.692 13.772 1.00 82.23 ? 60 ILE B O 1 ATOM 2306 C CB . ILE B 2 62 ? -5.683 -32.931 13.670 1.00 76.16 ? 60 ILE B CB 1 ATOM 2307 C CG1 . ILE B 2 62 ? -4.740 -34.111 13.921 1.00 71.42 ? 60 ILE B CG1 1 ATOM 2308 C CG2 . ILE B 2 62 ? -6.411 -33.097 12.344 1.00 75.19 ? 60 ILE B CG2 1 ATOM 2309 C CD1 . ILE B 2 62 ? -5.413 -35.451 13.963 1.00 68.57 ? 60 ILE B CD1 1 ATOM 2310 N N . TYR B 2 63 ? -5.645 -30.417 11.749 1.00 76.13 ? 61 TYR B N 1 ATOM 2311 C CA . TYR B 2 63 ? -6.463 -29.470 11.003 1.00 77.06 ? 61 TYR B CA 1 ATOM 2312 C C . TYR B 2 63 ? -7.091 -30.110 9.778 1.00 77.39 ? 61 TYR B C 1 ATOM 2313 O O . TYR B 2 63 ? -6.409 -30.602 8.887 1.00 73.67 ? 61 TYR B O 1 ATOM 2314 C CB . TYR B 2 63 ? -5.638 -28.269 10.569 1.00 75.40 ? 61 TYR B CB 1 ATOM 2315 C CG . TYR B 2 63 ? -5.046 -27.449 11.687 1.00 74.22 ? 61 TYR B CG 1 ATOM 2316 C CD1 . TYR B 2 63 ? -5.726 -26.358 12.200 1.00 76.63 ? 61 TYR B CD1 1 ATOM 2317 C CD2 . TYR B 2 63 ? -3.788 -27.741 12.204 1.00 74.54 ? 61 TYR B CD2 1 ATOM 2318 C CE1 . TYR B 2 63 ? -5.183 -25.585 13.211 1.00 78.26 ? 61 TYR B CE1 1 ATOM 2319 C CE2 . TYR B 2 63 ? -3.231 -26.969 13.215 1.00 74.40 ? 61 TYR B CE2 1 ATOM 2320 C CZ . TYR B 2 63 ? -3.940 -25.893 13.714 1.00 76.39 ? 61 TYR B CZ 1 ATOM 2321 O OH . TYR B 2 63 ? -3.416 -25.117 14.717 1.00 79.06 ? 61 TYR B OH 1 ATOM 2322 N N . ASP B 2 64 ? -8.415 -30.074 9.763 1.00 82.60 ? 62 ASP B N 1 ATOM 2323 C CA . ASP B 2 64 ? -9.234 -30.568 8.651 1.00 84.39 ? 62 ASP B CA 1 ATOM 2324 C C . ASP B 2 64 ? -9.890 -29.358 8.001 1.00 88.48 ? 62 ASP B C 1 ATOM 2325 O O . ASP B 2 64 ? -10.849 -29.466 7.242 1.00 89.14 ? 62 ASP B O 1 ATOM 2326 C CB . ASP B 2 64 ? -10.305 -31.534 9.165 1.00 86.55 ? 62 ASP B CB 1 ATOM 2327 C CG . ASP B 2 64 ? -11.080 -30.973 10.357 1.00 91.33 ? 62 ASP B CG 1 ATOM 2328 O OD1 . ASP B 2 64 ? -10.404 -30.541 11.318 1.00 80.29 ? 62 ASP B OD1 1 ATOM 2329 O OD2 . ASP B 2 64 ? -12.345 -30.953 10.327 1.00 97.70 ? 62 ASP B OD2 1 ATOM 2330 N N . ASN B 2 65 ? -9.303 -28.208 8.310 1.00 91.52 ? 63 ASN B N 1 ATOM 2331 C CA . ASN B 2 65 ? -9.926 -26.885 8.160 1.00 96.42 ? 63 ASN B CA 1 ATOM 2332 C C . ASN B 2 65 ? -10.132 -26.430 6.713 1.00 96.86 ? 63 ASN B C 1 ATOM 2333 O O . ASN B 2 65 ? -10.875 -25.480 6.462 1.00 100.54 ? 63 ASN B O 1 ATOM 2334 C CB . ASN B 2 65 ? -9.083 -25.836 8.925 1.00 96.90 ? 63 ASN B CB 1 ATOM 2335 C CG . ASN B 2 65 ? -9.861 -24.570 9.261 1.00 102.84 ? 63 ASN B CG 1 ATOM 2336 O OD1 . ASN B 2 65 ? -11.098 -24.559 9.277 1.00 106.07 ? 63 ASN B OD1 1 ATOM 2337 N ND2 . ASN B 2 65 ? -9.129 -23.495 9.557 1.00 102.28 ? 63 ASN B ND2 1 ATOM 2338 N N . TYR B 2 66 ? -9.493 -27.117 5.769 1.00 94.10 ? 64 TYR B N 1 ATOM 2339 C CA . TYR B 2 66 ? -9.480 -26.665 4.362 1.00 94.27 ? 64 TYR B CA 1 ATOM 2340 C C . TYR B 2 66 ? -9.886 -27.714 3.332 1.00 93.12 ? 64 TYR B C 1 ATOM 2341 O O . TYR B 2 66 ? -10.131 -28.882 3.656 1.00 92.08 ? 64 TYR B O 1 ATOM 2342 C CB . TYR B 2 66 ? -8.114 -26.068 3.974 1.00 91.65 ? 64 TYR B CB 1 ATOM 2343 C CG . TYR B 2 66 ? -7.014 -26.244 5.006 1.00 90.38 ? 64 TYR B CG 1 ATOM 2344 C CD1 . TYR B 2 66 ? -6.363 -27.462 5.167 1.00 89.06 ? 64 TYR B CD1 1 ATOM 2345 C CD2 . TYR B 2 66 ? -6.609 -25.176 5.803 1.00 92.33 ? 64 TYR B CD2 1 ATOM 2346 C CE1 . TYR B 2 66 ? -5.357 -27.615 6.112 1.00 89.22 ? 64 TYR B CE1 1 ATOM 2347 C CE2 . TYR B 2 66 ? -5.603 -25.319 6.744 1.00 90.67 ? 64 TYR B CE2 1 ATOM 2348 C CZ . TYR B 2 66 ? -4.981 -26.538 6.894 1.00 88.80 ? 64 TYR B CZ 1 ATOM 2349 O OH . TYR B 2 66 ? -3.977 -26.679 7.824 1.00 86.79 ? 64 TYR B OH 1 ATOM 2350 N N . TYR B 2 67 ? -9.916 -27.259 2.081 1.00 92.89 ? 65 TYR B N 1 ATOM 2351 C CA . TYR B 2 67 ? -10.461 -28.019 0.959 1.00 92.85 ? 65 TYR B CA 1 ATOM 2352 C C . TYR B 2 67 ? -11.914 -28.379 1.266 1.00 96.55 ? 65 TYR B C 1 ATOM 2353 O O . TYR B 2 67 ? -12.222 -29.530 1.581 1.00 96.33 ? 65 TYR B O 1 ATOM 2354 C CB . TYR B 2 67 ? -9.626 -29.273 0.701 1.00 89.57 ? 65 TYR B CB 1 ATOM 2355 C CG . TYR B 2 67 ? -9.714 -29.804 -0.716 1.00 89.35 ? 65 TYR B CG 1 ATOM 2356 C CD1 . TYR B 2 67 ? -10.659 -30.753 -1.060 1.00 91.65 ? 65 TYR B CD1 1 ATOM 2357 C CD2 . TYR B 2 67 ? -8.835 -29.372 -1.702 1.00 88.98 ? 65 TYR B CD2 1 ATOM 2358 C CE1 . TYR B 2 67 ? -10.743 -31.250 -2.344 1.00 93.60 ? 65 TYR B CE1 1 ATOM 2359 C CE2 . TYR B 2 67 ? -8.912 -29.865 -2.993 1.00 89.95 ? 65 TYR B CE2 1 ATOM 2360 C CZ . TYR B 2 67 ? -9.872 -30.804 -3.307 1.00 93.48 ? 65 TYR B CZ 1 ATOM 2361 O OH . TYR B 2 67 ? -9.971 -31.308 -4.587 1.00 97.51 ? 65 TYR B OH 1 ATOM 2362 N N . PRO B 2 68 ? -12.810 -27.380 1.190 1.00 99.86 ? 66 PRO B N 1 ATOM 2363 C CA . PRO B 2 68 ? -14.218 -27.512 1.541 1.00 103.59 ? 66 PRO B CA 1 ATOM 2364 C C . PRO B 2 68 ? -14.891 -28.716 0.900 1.00 103.87 ? 66 PRO B C 1 ATOM 2365 O O . PRO B 2 68 ? -15.911 -29.198 1.398 1.00 106.81 ? 66 PRO B O 1 ATOM 2366 C CB . PRO B 2 68 ? -14.826 -26.221 0.997 1.00 107.12 ? 66 PRO B CB 1 ATOM 2367 C CG . PRO B 2 68 ? -13.737 -25.238 1.088 1.00 105.20 ? 66 PRO B CG 1 ATOM 2368 C CD . PRO B 2 68 ? -12.476 -25.996 0.807 1.00 100.57 ? 66 PRO B CD 1 ATOM 2369 N N . ASP B 2 69 ? -14.330 -29.185 -0.205 1.00 100.90 ? 67 ASP B N 1 ATOM 2370 C CA . ASP B 2 69 ? -14.868 -30.367 -0.877 1.00 101.25 ? 67 ASP B CA 1 ATOM 2371 C C . ASP B 2 69 ? -14.710 -31.581 0.033 1.00 99.48 ? 67 ASP B C 1 ATOM 2372 O O . ASP B 2 69 ? -15.575 -32.452 0.082 1.00 102.13 ? 67 ASP B O 1 ATOM 2373 C CB . ASP B 2 69 ? -14.184 -30.602 -2.232 1.00 99.29 ? 67 ASP B CB 1 ATOM 2374 C CG . ASP B 2 69 ? -14.455 -31.988 -2.798 1.00 100.32 ? 67 ASP B CG 1 ATOM 2375 O OD1 . ASP B 2 69 ? -13.863 -32.972 -2.301 1.00 99.80 ? 67 ASP B OD1 1 ATOM 2376 O OD2 . ASP B 2 69 ? -15.249 -32.095 -3.755 1.00 105.20 ? 67 ASP B OD2 1 ATOM 2377 N N . LEU B 2 70 ? -13.617 -31.607 0.783 1.00 95.75 ? 68 LEU B N 1 ATOM 2378 C CA . LEU B 2 70 ? -13.273 -32.766 1.607 1.00 94.23 ? 68 LEU B CA 1 ATOM 2379 C C . LEU B 2 70 ? -13.673 -32.563 3.059 1.00 96.04 ? 68 LEU B C 1 ATOM 2380 O O . LEU B 2 70 ? -13.285 -33.332 3.938 1.00 95.41 ? 68 LEU B O 1 ATOM 2381 C CB . LEU B 2 70 ? -11.773 -33.073 1.529 1.00 89.81 ? 68 LEU B CB 1 ATOM 2382 C CG . LEU B 2 70 ? -11.362 -33.862 0.286 1.00 88.49 ? 68 LEU B CG 1 ATOM 2383 C CD1 . LEU B 2 70 ? -9.851 -33.917 0.159 1.00 81.04 ? 68 LEU B CD1 1 ATOM 2384 C CD2 . LEU B 2 70 ? -11.969 -35.268 0.330 1.00 92.69 ? 68 LEU B CD2 1 ATOM 2385 N N . LYS B 2 71 ? -14.448 -31.517 3.303 1.00 98.77 ? 69 LYS B N 1 ATOM 2386 C CA . LYS B 2 71 ? -14.912 -31.214 4.660 1.00 100.72 ? 69 LYS B CA 1 ATOM 2387 C C . LYS B 2 71 ? -15.608 -32.415 5.272 1.00 101.44 ? 69 LYS B C 1 ATOM 2388 O O . LYS B 2 71 ? -16.720 -32.774 4.883 1.00 104.74 ? 69 LYS B O 1 ATOM 2389 C CB . LYS B 2 71 ? -15.874 -30.017 4.669 1.00 105.44 ? 69 LYS B CB 1 ATOM 2390 C CG . LYS B 2 71 ? -16.410 -29.656 6.056 1.00 108.68 ? 69 LYS B CG 1 ATOM 2391 C CD . LYS B 2 71 ? -17.305 -28.422 6.019 1.00 112.59 ? 69 LYS B CD 1 ATOM 2392 C CE . LYS B 2 71 ? -17.652 -27.952 7.431 1.00 116.41 ? 69 LYS B CE 1 ATOM 2393 N NZ . LYS B 2 71 ? -18.618 -26.812 7.446 1.00 120.24 ? 69 LYS B NZ 1 ATOM 2394 N N . GLY B 2 72 ? -14.940 -33.025 6.239 1.00 98.18 ? 70 GLY B N 1 ATOM 2395 C CA . GLY B 2 72 ? -15.538 -34.093 7.027 1.00 99.17 ? 70 GLY B CA 1 ATOM 2396 C C . GLY B 2 72 ? -15.302 -35.463 6.432 1.00 96.54 ? 70 GLY B C 1 ATOM 2397 O O . GLY B 2 72 ? -15.806 -36.464 6.945 1.00 98.86 ? 70 GLY B O 1 ATOM 2398 N N . ARG B 2 73 ? -14.516 -35.510 5.363 1.00 92.24 ? 71 ARG B N 1 ATOM 2399 C CA . ARG B 2 73 ? -14.319 -36.756 4.626 1.00 89.66 ? 71 ARG B CA 1 ATOM 2400 C C . ARG B 2 73 ? -12.903 -37.352 4.684 1.00 85.47 ? 71 ARG B C 1 ATOM 2401 O O . ARG B 2 73 ? -12.682 -38.451 4.164 1.00 85.37 ? 71 ARG B O 1 ATOM 2402 C CB . ARG B 2 73 ? -14.749 -36.552 3.175 1.00 89.92 ? 71 ARG B CB 1 ATOM 2403 C CG . ARG B 2 73 ? -16.237 -36.271 3.050 1.00 92.18 ? 71 ARG B CG 1 ATOM 2404 C CD . ARG B 2 73 ? -16.772 -36.581 1.653 1.00 90.76 ? 71 ARG B CD 1 ATOM 2405 N NE . ARG B 2 73 ? -16.199 -35.722 0.615 1.00 91.02 ? 71 ARG B NE 1 ATOM 2406 C CZ . ARG B 2 73 ? -15.293 -36.116 -0.278 1.00 90.59 ? 71 ARG B CZ 1 ATOM 2407 N NH1 . ARG B 2 73 ? -14.849 -37.369 -0.284 1.00 89.29 ? 71 ARG B NH1 1 ATOM 2408 N NH2 . ARG B 2 73 ? -14.836 -35.251 -1.172 1.00 87.51 ? 71 ARG B NH2 1 ATOM 2409 N N . VAL B 2 74 ? -11.958 -36.654 5.315 1.00 82.28 ? 72 VAL B N 1 ATOM 2410 C CA . VAL B 2 74 ? -10.584 -37.173 5.435 1.00 79.20 ? 72 VAL B CA 1 ATOM 2411 C C . VAL B 2 74 ? -10.032 -37.165 6.868 1.00 79.85 ? 72 VAL B C 1 ATOM 2412 O O . VAL B 2 74 ? -10.155 -36.174 7.596 1.00 81.43 ? 72 VAL B O 1 ATOM 2413 C CB . VAL B 2 74 ? -9.592 -36.427 4.503 1.00 77.10 ? 72 VAL B CB 1 ATOM 2414 C CG1 . VAL B 2 74 ? -9.476 -34.956 4.880 1.00 78.84 ? 72 VAL B CG1 1 ATOM 2415 C CG2 . VAL B 2 74 ? -8.227 -37.092 4.552 1.00 67.88 ? 72 VAL B CG2 1 ATOM 2416 N N . HIS B 2 75 ? -9.413 -38.280 7.260 1.00 78.62 ? 73 HIS B N 1 ATOM 2417 C CA . HIS B 2 75 ? -8.895 -38.447 8.640 1.00 77.98 ? 73 HIS B CA 1 ATOM 2418 C C . HIS B 2 75 ? -7.620 -39.309 8.741 1.00 72.47 ? 73 HIS B C 1 ATOM 2419 O O . HIS B 2 75 ? -7.472 -40.291 8.014 1.00 71.19 ? 73 HIS B O 1 ATOM 2420 C CB . HIS B 2 75 ? -9.987 -39.085 9.513 1.00 81.72 ? 73 HIS B CB 1 ATOM 2421 C CG . HIS B 2 75 ? -11.158 -38.190 9.813 1.00 91.73 ? 73 HIS B CG 1 ATOM 2422 N ND1 . HIS B 2 75 ? -11.274 -37.489 10.996 1.00 100.54 ? 73 HIS B ND1 1 ATOM 2423 C CD2 . HIS B 2 75 ? -12.293 -37.928 9.112 1.00 101.27 ? 73 HIS B CD2 1 ATOM 2424 C CE1 . HIS B 2 75 ? -12.414 -36.817 11.003 1.00 103.07 ? 73 HIS B CE1 1 ATOM 2425 N NE2 . HIS B 2 75 ? -13.049 -37.061 9.868 1.00 103.38 ? 73 HIS B NE2 1 ATOM 2426 N N . PHE B 2 76 ? -6.724 -38.932 9.652 1.00 68.14 ? 74 PHE B N 1 ATOM 2427 C CA . PHE B 2 76 ? -5.570 -39.792 10.013 1.00 63.58 ? 74 PHE B CA 1 ATOM 2428 C C . PHE B 2 76 ? -6.103 -41.071 10.625 1.00 64.35 ? 74 PHE B C 1 ATOM 2429 O O . PHE B 2 76 ? -6.844 -41.033 11.605 1.00 64.73 ? 74 PHE B O 1 ATOM 2430 C CB . PHE B 2 76 ? -4.658 -39.139 11.051 1.00 62.04 ? 74 PHE B CB 1 ATOM 2431 C CG . PHE B 2 76 ? -3.828 -38.005 10.532 1.00 58.34 ? 74 PHE B CG 1 ATOM 2432 C CD1 . PHE B 2 76 ? -2.730 -38.237 9.710 1.00 58.44 ? 74 PHE B CD1 1 ATOM 2433 C CD2 . PHE B 2 76 ? -4.110 -36.705 10.912 1.00 55.76 ? 74 PHE B CD2 1 ATOM 2434 C CE1 . PHE B 2 76 ? -1.947 -37.180 9.258 1.00 54.37 ? 74 PHE B CE1 1 ATOM 2435 C CE2 . PHE B 2 76 ? -3.342 -35.654 10.460 1.00 58.32 ? 74 PHE B CE2 1 ATOM 2436 C CZ . PHE B 2 76 ? -2.252 -35.890 9.636 1.00 54.71 ? 74 PHE B CZ 1 ATOM 2437 N N . THR B 2 77 ? -5.709 -42.202 10.060 1.00 63.01 ? 75 THR B N 1 ATOM 2438 C CA . THR B 2 77 ? -6.149 -43.491 10.574 1.00 65.63 ? 75 THR B CA 1 ATOM 2439 C C . THR B 2 77 ? -5.697 -43.642 12.001 1.00 67.12 ? 75 THR B C 1 ATOM 2440 O O . THR B 2 77 ? -6.489 -43.817 12.912 1.00 71.27 ? 75 THR B O 1 ATOM 2441 C CB . THR B 2 77 ? -5.579 -44.647 9.752 1.00 65.06 ? 75 THR B CB 1 ATOM 2442 O OG1 . THR B 2 77 ? -4.178 -44.439 9.523 1.00 54.59 ? 75 THR B OG1 1 ATOM 2443 C CG2 . THR B 2 77 ? -6.312 -44.736 8.415 1.00 68.01 ? 75 THR B CG2 1 ATOM 2444 N N . SER B 2 78 ? -4.395 -43.573 12.175 1.00 67.29 ? 76 SER B N 1 ATOM 2445 C CA . SER B 2 78 ? -3.763 -43.714 13.490 1.00 68.95 ? 76 SER B CA 1 ATOM 2446 C C . SER B 2 78 ? -4.359 -42.843 14.573 1.00 74.03 ? 76 SER B C 1 ATOM 2447 O O . SER B 2 78 ? -4.951 -41.786 14.335 1.00 72.76 ? 76 SER B O 1 ATOM 2448 C CB . SER B 2 78 ? -2.256 -43.419 13.417 1.00 65.79 ? 76 SER B CB 1 ATOM 2449 O OG . SER B 2 78 ? -1.725 -43.150 14.707 1.00 59.68 ? 76 SER B OG 1 ATOM 2450 N N . ASN B 2 79 ? -4.140 -43.326 15.785 1.00 79.88 ? 77 ASN B N 1 ATOM 2451 C CA . ASN B 2 79 ? -4.435 -42.598 17.003 1.00 84.61 ? 77 ASN B CA 1 ATOM 2452 C C . ASN B 2 79 ? -3.229 -41.693 17.277 1.00 84.79 ? 77 ASN B C 1 ATOM 2453 O O . ASN B 2 79 ? -3.314 -40.459 17.232 1.00 87.27 ? 77 ASN B O 1 ATOM 2454 C CB . ASN B 2 79 ? -4.639 -43.579 18.159 1.00 88.03 ? 77 ASN B CB 1 ATOM 2455 C CG . ASN B 2 79 ? -5.483 -44.792 17.761 1.00 93.41 ? 77 ASN B CG 1 ATOM 2456 O OD1 . ASN B 2 79 ? -6.719 -44.763 17.819 1.00 91.84 ? 77 ASN B OD1 1 ATOM 2457 N ND2 . ASN B 2 79 ? -4.809 -45.873 17.370 1.00 95.98 ? 77 ASN B ND2 1 ATOM 2458 N N . ASP B 2 80 ? -2.089 -42.338 17.501 1.00 82.74 ? 78 ASP B N 1 ATOM 2459 C CA . ASP B 2 80 ? -0.855 -41.642 17.865 1.00 79.81 ? 78 ASP B CA 1 ATOM 2460 C C . ASP B 2 80 ? 0.044 -41.437 16.666 1.00 75.29 ? 78 ASP B C 1 ATOM 2461 O O . ASP B 2 80 ? 0.950 -42.225 16.394 1.00 72.65 ? 78 ASP B O 1 ATOM 2462 C CB . ASP B 2 80 ? -0.107 -42.420 18.944 1.00 81.65 ? 78 ASP B CB 1 ATOM 2463 C CG . ASP B 2 80 ? 0.907 -41.570 19.673 1.00 82.06 ? 78 ASP B CG 1 ATOM 2464 O OD1 . ASP B 2 80 ? 0.901 -40.333 19.483 1.00 87.94 ? 78 ASP B OD1 1 ATOM 2465 O OD2 . ASP B 2 80 ? 1.710 -42.142 20.438 1.00 83.06 ? 78 ASP B OD2 1 ATOM 2466 N N . VAL B 2 81 ? -0.208 -40.345 15.965 1.00 73.55 ? 79 VAL B N 1 ATOM 2467 C CA . VAL B 2 81 ? 0.456 -40.087 14.681 1.00 69.44 ? 79 VAL B CA 1 ATOM 2468 C C . VAL B 2 81 ? 1.970 -39.912 14.868 1.00 66.92 ? 79 VAL B C 1 ATOM 2469 O O . VAL B 2 81 ? 2.770 -40.335 14.030 1.00 65.85 ? 79 VAL B O 1 ATOM 2470 C CB . VAL B 2 81 ? -0.189 -38.880 13.940 1.00 67.82 ? 79 VAL B CB 1 ATOM 2471 C CG1 . VAL B 2 81 ? 0.769 -38.264 12.970 1.00 69.93 ? 79 VAL B CG1 1 ATOM 2472 C CG2 . VAL B 2 81 ? -1.429 -39.336 13.214 1.00 68.59 ? 79 VAL B CG2 1 ATOM 2473 N N . LYS B 2 82 ? 2.352 -39.321 15.992 1.00 67.03 ? 80 LYS B N 1 ATOM 2474 C CA . LYS B 2 82 ? 3.764 -39.053 16.288 1.00 64.21 ? 80 LYS B CA 1 ATOM 2475 C C . LYS B 2 82 ? 4.539 -40.347 16.427 1.00 63.91 ? 80 LYS B C 1 ATOM 2476 O O . LYS B 2 82 ? 5.734 -40.404 16.156 1.00 63.91 ? 80 LYS B O 1 ATOM 2477 C CB . LYS B 2 82 ? 3.919 -38.290 17.596 1.00 65.70 ? 80 LYS B CB 1 ATOM 2478 C CG . LYS B 2 82 ? 3.287 -36.916 17.622 1.00 66.52 ? 80 LYS B CG 1 ATOM 2479 C CD . LYS B 2 82 ? 3.505 -36.252 18.971 1.00 67.30 ? 80 LYS B CD 1 ATOM 2480 C CE . LYS B 2 82 ? 3.215 -37.193 20.131 1.00 66.48 ? 80 LYS B CE 1 ATOM 2481 N NZ . LYS B 2 82 ? 3.137 -36.444 21.405 1.00 71.82 ? 80 LYS B NZ 1 ATOM 2482 N N . SER B 2 83 ? 3.854 -41.383 16.880 1.00 65.98 ? 81 SER B N 1 ATOM 2483 C CA . SER B 2 83 ? 4.507 -42.659 17.150 1.00 66.81 ? 81 SER B CA 1 ATOM 2484 C C . SER B 2 83 ? 5.190 -43.174 15.900 1.00 64.37 ? 81 SER B C 1 ATOM 2485 O O . SER B 2 83 ? 5.858 -44.201 15.938 1.00 65.75 ? 81 SER B O 1 ATOM 2486 C CB . SER B 2 83 ? 3.505 -43.710 17.641 1.00 70.65 ? 81 SER B CB 1 ATOM 2487 O OG . SER B 2 83 ? 2.562 -44.052 16.626 1.00 72.04 ? 81 SER B OG 1 ATOM 2488 N N . GLY B 2 84 ? 5.009 -42.457 14.794 1.00 61.74 ? 82 GLY B N 1 ATOM 2489 C CA . GLY B 2 84 ? 5.586 -42.862 13.514 1.00 59.66 ? 82 GLY B CA 1 ATOM 2490 C C . GLY B 2 84 ? 4.557 -43.292 12.479 1.00 59.12 ? 82 GLY B C 1 ATOM 2491 O O . GLY B 2 84 ? 4.854 -44.096 11.584 1.00 57.97 ? 82 GLY B O 1 ATOM 2492 N N . ASP B 2 85 ? 3.350 -42.749 12.591 1.00 58.60 ? 83 ASP B N 1 ATOM 2493 C CA . ASP B 2 85 ? 2.288 -43.076 11.641 1.00 59.37 ? 83 ASP B CA 1 ATOM 2494 C C . ASP B 2 85 ? 1.454 -41.901 11.184 1.00 57.63 ? 83 ASP B C 1 ATOM 2495 O O . ASP B 2 85 ? 0.692 -41.316 11.960 1.00 58.76 ? 83 ASP B O 1 ATOM 2496 C CB . ASP B 2 85 ? 1.346 -44.116 12.208 1.00 62.17 ? 83 ASP B CB 1 ATOM 2497 C CG . ASP B 2 85 ? 0.387 -44.618 11.174 1.00 67.76 ? 83 ASP B CG 1 ATOM 2498 O OD1 . ASP B 2 85 ? -0.232 -43.781 10.471 1.00 70.71 ? 83 ASP B OD1 1 ATOM 2499 O OD2 . ASP B 2 85 ? 0.273 -45.853 11.048 1.00 77.21 ? 83 ASP B OD2 1 ATOM 2500 N N . ALA B 2 86 ? 1.569 -41.624 9.889 1.00 53.97 ? 84 ALA B N 1 ATOM 2501 C CA . ALA B 2 86 ? 0.943 -40.469 9.275 1.00 52.51 ? 84 ALA B CA 1 ATOM 2502 C C . ALA B 2 86 ? -0.149 -40.876 8.295 1.00 52.86 ? 84 ALA B C 1 ATOM 2503 O O . ALA B 2 86 ? -0.720 -40.036 7.619 1.00 52.89 ? 84 ALA B O 1 ATOM 2504 C CB . ALA B 2 86 ? 1.998 -39.638 8.560 1.00 49.95 ? 84 ALA B CB 1 ATOM 2505 N N . SER B 2 87 ? -0.440 -42.168 8.231 1.00 53.62 ? 85 SER B N 1 ATOM 2506 C CA . SER B 2 87 ? -1.430 -42.680 7.272 1.00 53.24 ? 85 SER B CA 1 ATOM 2507 C C . SER B 2 87 ? -2.775 -42.004 7.441 1.00 54.51 ? 85 SER B C 1 ATOM 2508 O O . SER B 2 87 ? -3.153 -41.574 8.536 1.00 56.95 ? 85 SER B O 1 ATOM 2509 C CB . SER B 2 87 ? -1.587 -44.200 7.408 1.00 54.50 ? 85 SER B CB 1 ATOM 2510 O OG . SER B 2 87 ? -0.339 -44.832 7.589 1.00 52.01 ? 85 SER B OG 1 ATOM 2511 N N . ILE B 2 88 ? -3.502 -41.927 6.335 1.00 54.30 ? 86 ILE B N 1 ATOM 2512 C CA . ILE B 2 88 ? -4.843 -41.358 6.341 1.00 56.67 ? 86 ILE B CA 1 ATOM 2513 C C . ILE B 2 88 ? -5.873 -42.218 5.635 1.00 60.31 ? 86 ILE B C 1 ATOM 2514 O O . ILE B 2 88 ? -5.558 -43.072 4.808 1.00 59.80 ? 86 ILE B O 1 ATOM 2515 C CB . ILE B 2 88 ? -4.890 -39.951 5.698 1.00 53.39 ? 86 ILE B CB 1 ATOM 2516 C CG1 . ILE B 2 88 ? -4.529 -40.000 4.221 1.00 46.48 ? 86 ILE B CG1 1 ATOM 2517 C CG2 . ILE B 2 88 ? -4.006 -39.038 6.421 1.00 47.55 ? 86 ILE B CG2 1 ATOM 2518 C CD1 . ILE B 2 88 ? -4.646 -38.664 3.509 1.00 51.76 ? 86 ILE B CD1 1 ATOM 2519 N N . ASN B 2 89 ? -7.117 -41.959 5.998 1.00 65.02 ? 87 ASN B N 1 ATOM 2520 C CA . ASN B 2 89 ? -8.299 -42.456 5.277 1.00 71.29 ? 87 ASN B CA 1 ATOM 2521 C C . ASN B 2 89 ? -9.058 -41.331 4.591 1.00 73.02 ? 87 ASN B C 1 ATOM 2522 O O . ASN B 2 89 ? -9.224 -40.259 5.171 1.00 76.11 ? 87 ASN B O 1 ATOM 2523 C CB . ASN B 2 89 ? -9.249 -43.193 6.222 1.00 73.91 ? 87 ASN B CB 1 ATOM 2524 C CG . ASN B 2 89 ? -8.928 -44.669 6.335 1.00 77.84 ? 87 ASN B CG 1 ATOM 2525 O OD1 . ASN B 2 89 ? -8.013 -45.176 5.678 1.00 76.30 ? 87 ASN B OD1 1 ATOM 2526 N ND2 . ASN B 2 89 ? -9.687 -45.370 7.167 1.00 88.40 ? 87 ASN B ND2 1 ATOM 2527 N N . VAL B 2 90 ? -9.495 -41.603 3.362 1.00 72.93 ? 88 VAL B N 1 ATOM 2528 C CA . VAL B 2 90 ? -10.348 -40.696 2.569 1.00 73.70 ? 88 VAL B CA 1 ATOM 2529 C C . VAL B 2 90 ? -11.695 -41.368 2.412 1.00 78.73 ? 88 VAL B C 1 ATOM 2530 O O . VAL B 2 90 ? -11.792 -42.448 1.827 1.00 79.57 ? 88 VAL B O 1 ATOM 2531 C CB . VAL B 2 90 ? -9.754 -40.423 1.183 1.00 72.12 ? 88 VAL B CB 1 ATOM 2532 C CG1 . VAL B 2 90 ? -10.638 -39.458 0.381 1.00 70.89 ? 88 VAL B CG1 1 ATOM 2533 C CG2 . VAL B 2 90 ? -8.302 -39.883 1.321 1.00 66.67 ? 88 VAL B CG2 1 ATOM 2534 N N . THR B 2 91 ? -12.731 -40.725 2.952 1.00 81.82 ? 89 THR B N 1 ATOM 2535 C CA . THR B 2 91 ? -14.049 -41.332 3.049 1.00 86.66 ? 89 THR B CA 1 ATOM 2536 C C . THR B 2 91 ? -15.030 -40.818 2.015 1.00 89.01 ? 89 THR B C 1 ATOM 2537 O O . THR B 2 91 ? -14.938 -39.681 1.538 1.00 87.85 ? 89 THR B O 1 ATOM 2538 C CB . THR B 2 91 ? -14.644 -41.152 4.461 1.00 90.22 ? 89 THR B CB 1 ATOM 2539 O OG1 . THR B 2 91 ? -14.684 -39.762 4.806 1.00 92.34 ? 89 THR B OG1 1 ATOM 2540 C CG2 . THR B 2 91 ? -13.794 -41.896 5.484 1.00 86.83 ? 89 THR B CG2 1 ATOM 2541 N N . ASN B 2 92 ? -15.962 -41.706 1.680 1.00 91.61 ? 90 ASN B N 1 ATOM 2542 C CA . ASN B 2 92 ? -17.016 -41.442 0.705 1.00 93.73 ? 90 ASN B CA 1 ATOM 2543 C C . ASN B 2 92 ? -16.425 -40.945 -0.610 1.00 91.75 ? 90 ASN B C 1 ATOM 2544 O O . ASN B 2 92 ? -16.601 -39.791 -1.002 1.00 92.20 ? 90 ASN B O 1 ATOM 2545 C CB . ASN B 2 92 ? -18.016 -40.435 1.285 1.00 96.42 ? 90 ASN B CB 1 ATOM 2546 C CG . ASN B 2 92 ? -19.380 -40.508 0.634 1.00 98.14 ? 90 ASN B CG 1 ATOM 2547 O OD1 . ASN B 2 92 ? -20.140 -39.545 0.681 1.00 96.48 ? 90 ASN B OD1 1 ATOM 2548 N ND2 . ASN B 2 92 ? -19.694 -41.642 0.016 1.00 99.15 ? 90 ASN B ND2 1 ATOM 2549 N N . LEU B 2 93 ? -15.716 -41.843 -1.282 1.00 89.89 ? 91 LEU B N 1 ATOM 2550 C CA . LEU B 2 93 ? -14.966 -41.491 -2.494 1.00 87.36 ? 91 LEU B CA 1 ATOM 2551 C C . LEU B 2 93 ? -15.879 -41.113 -3.657 1.00 89.97 ? 91 LEU B C 1 ATOM 2552 O O . LEU B 2 93 ? -16.853 -41.802 -3.958 1.00 92.13 ? 91 LEU B O 1 ATOM 2553 C CB . LEU B 2 93 ? -13.985 -42.604 -2.910 1.00 85.21 ? 91 LEU B CB 1 ATOM 2554 C CG . LEU B 2 93 ? -12.643 -42.606 -2.169 1.00 78.34 ? 91 LEU B CG 1 ATOM 2555 C CD1 . LEU B 2 93 ? -11.697 -43.632 -2.773 1.00 72.15 ? 91 LEU B CD1 1 ATOM 2556 C CD2 . LEU B 2 93 ? -12.019 -41.226 -2.176 1.00 76.78 ? 91 LEU B CD2 1 ATOM 2557 N N . GLN B 2 94 ? -15.534 -39.990 -4.286 1.00 89.33 ? 92 GLN B N 1 ATOM 2558 C CA . GLN B 2 94 ? -16.205 -39.488 -5.487 1.00 91.16 ? 92 GLN B CA 1 ATOM 2559 C C . GLN B 2 94 ? -15.201 -39.213 -6.598 1.00 88.22 ? 92 GLN B C 1 ATOM 2560 O O . GLN B 2 94 ? -13.995 -39.286 -6.393 1.00 86.45 ? 92 GLN B O 1 ATOM 2561 C CB . GLN B 2 94 ? -16.953 -38.187 -5.188 1.00 93.26 ? 92 GLN B CB 1 ATOM 2562 C CG . GLN B 2 94 ? -17.577 -38.104 -3.801 1.00 95.37 ? 92 GLN B CG 1 ATOM 2563 C CD . GLN B 2 94 ? -18.538 -39.234 -3.510 1.00 97.88 ? 92 GLN B CD 1 ATOM 2564 O OE1 . GLN B 2 94 ? -19.000 -39.925 -4.416 1.00 102.35 ? 92 GLN B OE1 1 ATOM 2565 N NE2 . GLN B 2 94 ? -18.847 -39.427 -2.237 1.00 99.44 ? 92 GLN B NE2 1 ATOM 2566 N N . LEU B 2 95 ? -15.714 -38.859 -7.766 1.00 90.28 ? 93 LEU B N 1 ATOM 2567 C CA . LEU B 2 95 ? -14.879 -38.699 -8.959 1.00 88.63 ? 93 LEU B CA 1 ATOM 2568 C C . LEU B 2 95 ? -14.027 -37.453 -8.885 1.00 86.16 ? 93 LEU B C 1 ATOM 2569 O O . LEU B 2 95 ? -13.020 -37.353 -9.573 1.00 84.87 ? 93 LEU B O 1 ATOM 2570 C CB . LEU B 2 95 ? -15.718 -38.677 -10.243 1.00 92.17 ? 93 LEU B CB 1 ATOM 2571 C CG . LEU B 2 95 ? -16.078 -40.073 -10.750 1.00 93.40 ? 93 LEU B CG 1 ATOM 2572 C CD1 . LEU B 2 95 ? -16.763 -39.984 -12.099 1.00 92.70 ? 93 LEU B CD1 1 ATOM 2573 C CD2 . LEU B 2 95 ? -14.827 -40.954 -10.837 1.00 89.88 ? 93 LEU B CD2 1 ATOM 2574 N N . SER B 2 96 ? -14.433 -36.514 -8.039 1.00 86.93 ? 94 SER B N 1 ATOM 2575 C CA . SER B 2 96 ? -13.700 -35.249 -7.873 1.00 85.20 ? 94 SER B CA 1 ATOM 2576 C C . SER B 2 96 ? -12.459 -35.447 -7.007 1.00 81.04 ? 94 SER B C 1 ATOM 2577 O O . SER B 2 96 ? -11.589 -34.578 -6.920 1.00 79.89 ? 94 SER B O 1 ATOM 2578 C CB . SER B 2 96 ? -14.602 -34.184 -7.249 1.00 87.73 ? 94 SER B CB 1 ATOM 2579 O OG . SER B 2 96 ? -15.125 -34.621 -6.004 1.00 91.51 ? 94 SER B OG 1 ATOM 2580 N N . ASP B 2 97 ? -12.382 -36.611 -6.381 1.00 79.96 ? 95 ASP B N 1 ATOM 2581 C CA . ASP B 2 97 ? -11.301 -36.905 -5.446 1.00 77.16 ? 95 ASP B CA 1 ATOM 2582 C C . ASP B 2 97 ? -10.131 -37.498 -6.197 1.00 75.11 ? 95 ASP B C 1 ATOM 2583 O O . ASP B 2 97 ? -9.103 -37.846 -5.605 1.00 71.10 ? 95 ASP B O 1 ATOM 2584 C CB . ASP B 2 97 ? -11.770 -37.877 -4.370 1.00 78.04 ? 95 ASP B CB 1 ATOM 2585 C CG . ASP B 2 97 ? -12.951 -37.354 -3.600 1.00 81.32 ? 95 ASP B CG 1 ATOM 2586 O OD1 . ASP B 2 97 ? -13.151 -36.121 -3.586 1.00 83.81 ? 95 ASP B OD1 1 ATOM 2587 O OD2 . ASP B 2 97 ? -13.679 -38.175 -3.007 1.00 84.54 ? 95 ASP B OD2 1 ATOM 2588 N N . ILE B 2 98 ? -10.308 -37.617 -7.509 1.00 75.96 ? 96 ILE B N 1 ATOM 2589 C CA . ILE B 2 98 ? -9.254 -38.120 -8.367 1.00 74.38 ? 96 ILE B CA 1 ATOM 2590 C C . ILE B 2 98 ? -8.118 -37.113 -8.365 1.00 72.94 ? 96 ILE B C 1 ATOM 2591 O O . ILE B 2 98 ? -8.324 -35.899 -8.385 1.00 74.38 ? 96 ILE B O 1 ATOM 2592 C CB . ILE B 2 98 ? -9.739 -38.362 -9.800 1.00 76.02 ? 96 ILE B CB 1 ATOM 2593 C CG1 . ILE B 2 98 ? -10.722 -39.529 -9.827 1.00 82.00 ? 96 ILE B CG1 1 ATOM 2594 C CG2 . ILE B 2 98 ? -8.577 -38.686 -10.699 1.00 72.74 ? 96 ILE B CG2 1 ATOM 2595 C CD1 . ILE B 2 98 ? -11.440 -39.715 -11.166 1.00 83.20 ? 96 ILE B CD1 1 ATOM 2596 N N . GLY B 2 99 ? -6.907 -37.632 -8.313 1.00 70.17 ? 97 GLY B N 1 ATOM 2597 C CA . GLY B 2 99 ? -5.750 -36.784 -8.274 1.00 67.85 ? 97 GLY B CA 1 ATOM 2598 C C . GLY B 2 99 ? -4.532 -37.489 -7.747 1.00 65.81 ? 97 GLY B C 1 ATOM 2599 O O . GLY B 2 99 ? -4.447 -38.719 -7.729 1.00 66.45 ? 97 GLY B O 1 ATOM 2600 N N . THR B 2 100 ? -3.581 -36.676 -7.320 1.00 63.74 ? 98 THR B N 1 ATOM 2601 C CA . THR B 2 100 ? -2.331 -37.168 -6.785 1.00 60.98 ? 98 THR B CA 1 ATOM 2602 C C . THR B 2 100 ? -2.180 -36.702 -5.363 1.00 59.60 ? 98 THR B C 1 ATOM 2603 O O . THR B 2 100 ? -2.350 -35.522 -5.044 1.00 59.04 ? 98 THR B O 1 ATOM 2604 C CB . THR B 2 100 ? -1.142 -36.714 -7.632 1.00 59.86 ? 98 THR B CB 1 ATOM 2605 O OG1 . THR B 2 100 ? -1.232 -37.335 -8.921 1.00 62.92 ? 98 THR B OG1 1 ATOM 2606 C CG2 . THR B 2 100 ? 0.161 -37.106 -6.968 1.00 54.63 ? 98 THR B CG2 1 ATOM 2607 N N . TYR B 2 101 ? -1.883 -37.677 -4.518 1.00 59.51 ? 99 TYR B N 1 ATOM 2608 C CA . TYR B 2 101 ? -1.876 -37.498 -3.078 1.00 59.14 ? 99 TYR B CA 1 ATOM 2609 C C . TYR B 2 101 ? -0.471 -37.684 -2.561 1.00 56.60 ? 99 TYR B C 1 ATOM 2610 O O . TYR B 2 101 ? 0.223 -38.652 -2.892 1.00 57.40 ? 99 TYR B O 1 ATOM 2611 C CB . TYR B 2 101 ? -2.859 -38.472 -2.412 1.00 60.85 ? 99 TYR B CB 1 ATOM 2612 C CG . TYR B 2 101 ? -4.315 -38.128 -2.688 1.00 64.51 ? 99 TYR B CG 1 ATOM 2613 C CD1 . TYR B 2 101 ? -4.932 -38.519 -3.873 1.00 66.02 ? 99 TYR B CD1 1 ATOM 2614 C CD2 . TYR B 2 101 ? -5.070 -37.405 -1.766 1.00 68.35 ? 99 TYR B CD2 1 ATOM 2615 C CE1 . TYR B 2 101 ? -6.261 -38.203 -4.135 1.00 70.48 ? 99 TYR B CE1 1 ATOM 2616 C CE2 . TYR B 2 101 ? -6.410 -37.084 -2.023 1.00 71.15 ? 99 TYR B CE2 1 ATOM 2617 C CZ . TYR B 2 101 ? -6.998 -37.488 -3.206 1.00 70.57 ? 99 TYR B CZ 1 ATOM 2618 O OH . TYR B 2 101 ? -8.318 -37.167 -3.465 1.00 68.58 ? 99 TYR B OH 1 ATOM 2619 N N . GLN B 2 102 ? -0.059 -36.720 -1.754 1.00 54.61 ? 100 GLN B N 1 ATOM 2620 C CA . GLN B 2 102 ? 1.313 -36.629 -1.312 1.00 50.82 ? 100 GLN B CA 1 ATOM 2621 C C . GLN B 2 102 ? 1.410 -36.501 0.196 1.00 49.41 ? 100 GLN B C 1 ATOM 2622 O O . GLN B 2 102 ? 0.680 -35.726 0.813 1.00 48.58 ? 100 GLN B O 1 ATOM 2623 C CB . GLN B 2 102 ? 1.946 -35.420 -1.972 1.00 49.67 ? 100 GLN B CB 1 ATOM 2624 C CG . GLN B 2 102 ? 3.419 -35.292 -1.718 1.00 49.45 ? 100 GLN B CG 1 ATOM 2625 C CD . GLN B 2 102 ? 4.053 -34.190 -2.536 1.00 48.23 ? 100 GLN B CD 1 ATOM 2626 O OE1 . GLN B 2 102 ? 5.268 -34.179 -2.739 1.00 52.11 ? 100 GLN B OE1 1 ATOM 2627 N NE2 . GLN B 2 102 ? 3.236 -33.256 -3.016 1.00 43.31 ? 100 GLN B NE2 1 ATOM 2628 N N . CYS B 2 103 ? 2.332 -37.264 0.772 1.00 49.18 ? 101 CYS B N 1 ATOM 2629 C CA . CYS B 2 103 ? 2.568 -37.265 2.214 1.00 49.20 ? 101 CYS B CA 1 ATOM 2630 C C . CYS B 2 103 ? 3.928 -36.655 2.596 1.00 45.45 ? 101 CYS B C 1 ATOM 2631 O O . CYS B 2 103 ? 4.968 -37.215 2.306 1.00 42.89 ? 101 CYS B O 1 ATOM 2632 C CB . CYS B 2 103 ? 2.448 -38.699 2.738 1.00 49.78 ? 101 CYS B CB 1 ATOM 2633 S SG . CYS B 2 103 ? 2.452 -38.842 4.522 1.00 50.53 ? 101 CYS B SG 1 ATOM 2634 N N . LYS B 2 104 ? 3.869 -35.501 3.259 1.00 45.03 ? 102 LYS B N 1 ATOM 2635 C CA . LYS B 2 104 ? 5.038 -34.723 3.634 1.00 45.38 ? 102 LYS B CA 1 ATOM 2636 C C . LYS B 2 104 ? 5.280 -34.647 5.135 1.00 45.16 ? 102 LYS B C 1 ATOM 2637 O O . LYS B 2 104 ? 4.600 -33.916 5.842 1.00 44.53 ? 102 LYS B O 1 ATOM 2638 C CB . LYS B 2 104 ? 4.914 -33.288 3.109 1.00 46.41 ? 102 LYS B CB 1 ATOM 2639 C CG . LYS B 2 104 ? 5.203 -33.115 1.632 1.00 48.62 ? 102 LYS B CG 1 ATOM 2640 C CD . LYS B 2 104 ? 4.961 -31.668 1.248 1.00 53.29 ? 102 LYS B CD 1 ATOM 2641 C CE . LYS B 2 104 ? 5.371 -31.368 -0.179 1.00 54.28 ? 102 LYS B CE 1 ATOM 2642 N NZ . LYS B 2 104 ? 5.520 -29.895 -0.367 1.00 60.31 ? 102 LYS B NZ 1 ATOM 2643 N N . VAL B 2 105 ? 6.317 -35.358 5.575 1.00 44.22 ? 103 VAL B N 1 ATOM 2644 C CA . VAL B 2 105 ? 6.745 -35.379 6.975 1.00 43.45 ? 103 VAL B CA 1 ATOM 2645 C C . VAL B 2 105 ? 8.033 -34.572 7.189 1.00 43.07 ? 103 VAL B C 1 ATOM 2646 O O . VAL B 2 105 ? 9.048 -34.786 6.513 1.00 42.64 ? 103 VAL B O 1 ATOM 2647 C CB . VAL B 2 105 ? 6.993 -36.830 7.478 1.00 43.13 ? 103 VAL B CB 1 ATOM 2648 C CG1 . VAL B 2 105 ? 6.874 -36.880 8.972 1.00 45.12 ? 103 VAL B CG1 1 ATOM 2649 C CG2 . VAL B 2 105 ? 6.008 -37.827 6.850 1.00 37.22 ? 103 VAL B CG2 1 ATOM 2650 N N . LYS B 2 106 ? 7.989 -33.655 8.149 1.00 42.91 ? 104 LYS B N 1 ATOM 2651 C CA . LYS B 2 106 ? 9.148 -32.817 8.471 1.00 42.08 ? 104 LYS B CA 1 ATOM 2652 C C . LYS B 2 106 ? 9.416 -32.718 9.969 1.00 43.12 ? 104 LYS B C 1 ATOM 2653 O O . LYS B 2 106 ? 8.572 -32.283 10.761 1.00 45.21 ? 104 LYS B O 1 ATOM 2654 C CB . LYS B 2 106 ? 8.978 -31.410 7.896 1.00 42.01 ? 104 LYS B CB 1 ATOM 2655 C CG . LYS B 2 106 ? 9.039 -31.349 6.391 1.00 43.12 ? 104 LYS B CG 1 ATOM 2656 C CD . LYS B 2 106 ? 8.652 -29.973 5.849 1.00 42.44 ? 104 LYS B CD 1 ATOM 2657 C CE . LYS B 2 106 ? 8.520 -30.029 4.332 1.00 40.48 ? 104 LYS B CE 1 ATOM 2658 N NZ . LYS B 2 106 ? 7.952 -28.770 3.789 1.00 44.16 ? 104 LYS B NZ 1 ATOM 2659 N N . LYS B 2 107 ? 10.614 -33.131 10.342 1.00 41.94 ? 105 LYS B N 1 ATOM 2660 C CA . LYS B 2 107 ? 11.077 -32.958 11.700 1.00 42.47 ? 105 LYS B CA 1 ATOM 2661 C C . LYS B 2 107 ? 12.564 -32.646 11.693 1.00 42.17 ? 105 LYS B C 1 ATOM 2662 O O . LYS B 2 107 ? 13.420 -33.535 11.686 1.00 41.19 ? 105 LYS B O 1 ATOM 2663 C CB . LYS B 2 107 ? 10.771 -34.198 12.532 1.00 43.04 ? 105 LYS B CB 1 ATOM 2664 C CG . LYS B 2 107 ? 10.859 -33.920 14.015 1.00 47.97 ? 105 LYS B CG 1 ATOM 2665 C CD . LYS B 2 107 ? 10.024 -34.859 14.869 1.00 48.52 ? 105 LYS B CD 1 ATOM 2666 C CE . LYS B 2 107 ? 10.599 -34.969 16.273 1.00 47.37 ? 105 LYS B CE 1 ATOM 2667 N NZ . LYS B 2 107 ? 11.485 -33.819 16.602 1.00 47.39 ? 105 LYS B NZ 1 ATOM 2668 N N . ALA B 2 108 ? 12.850 -31.353 11.679 1.00 42.61 ? 106 ALA B N 1 ATOM 2669 C CA . ALA B 2 108 ? 14.188 -30.864 11.407 1.00 42.47 ? 106 ALA B CA 1 ATOM 2670 C C . ALA B 2 108 ? 15.256 -31.732 12.081 1.00 43.45 ? 106 ALA B C 1 ATOM 2671 O O . ALA B 2 108 ? 15.185 -32.002 13.289 1.00 43.93 ? 106 ALA B O 1 ATOM 2672 C CB . ALA B 2 108 ? 14.315 -29.424 11.840 1.00 43.51 ? 106 ALA B CB 1 ATOM 2673 N N . PRO B 2 109 ? 16.275 -32.146 11.306 1.00 43.31 ? 107 PRO B N 1 ATOM 2674 C CA . PRO B 2 109 ? 16.494 -31.771 9.914 1.00 41.77 ? 107 PRO B CA 1 ATOM 2675 C C . PRO B 2 109 ? 15.919 -32.778 8.942 1.00 40.56 ? 107 PRO B C 1 ATOM 2676 O O . PRO B 2 109 ? 16.046 -32.616 7.727 1.00 42.50 ? 107 PRO B O 1 ATOM 2677 C CB . PRO B 2 109 ? 18.016 -31.788 9.804 1.00 40.62 ? 107 PRO B CB 1 ATOM 2678 C CG . PRO B 2 109 ? 18.425 -32.907 10.705 1.00 39.83 ? 107 PRO B CG 1 ATOM 2679 C CD . PRO B 2 109 ? 17.397 -32.957 11.821 1.00 44.61 ? 107 PRO B CD 1 ATOM 2680 N N . GLY B 2 110 ? 15.314 -33.824 9.478 1.00 39.98 ? 108 GLY B N 1 ATOM 2681 C CA . GLY B 2 110 ? 14.826 -34.931 8.652 1.00 39.33 ? 108 GLY B CA 1 ATOM 2682 C C . GLY B 2 110 ? 13.591 -34.581 7.849 1.00 39.11 ? 108 GLY B C 1 ATOM 2683 O O . GLY B 2 110 ? 12.753 -33.782 8.272 1.00 37.69 ? 108 GLY B O 1 ATOM 2684 N N . VAL B 2 111 ? 13.475 -35.206 6.686 1.00 39.61 ? 109 VAL B N 1 ATOM 2685 C CA . VAL B 2 111 ? 12.318 -34.988 5.823 1.00 41.28 ? 109 VAL B CA 1 ATOM 2686 C C . VAL B 2 111 ? 12.029 -36.148 4.906 1.00 41.66 ? 109 VAL B C 1 ATOM 2687 O O . VAL B 2 111 ? 12.931 -36.726 4.324 1.00 43.31 ? 109 VAL B O 1 ATOM 2688 C CB . VAL B 2 111 ? 12.526 -33.748 4.942 1.00 42.53 ? 109 VAL B CB 1 ATOM 2689 C CG1 . VAL B 2 111 ? 13.940 -33.721 4.400 1.00 38.44 ? 109 VAL B CG1 1 ATOM 2690 C CG2 . VAL B 2 111 ? 11.495 -33.729 3.807 1.00 43.43 ? 109 VAL B CG2 1 ATOM 2691 N N . ALA B 2 112 ? 10.756 -36.471 4.763 1.00 43.31 ? 110 ALA B N 1 ATOM 2692 C CA . ALA B 2 112 ? 10.344 -37.548 3.851 1.00 43.95 ? 110 ALA B CA 1 ATOM 2693 C C . ALA B 2 112 ? 9.084 -37.225 3.055 1.00 43.80 ? 110 ALA B C 1 ATOM 2694 O O . ALA B 2 112 ? 8.291 -36.340 3.406 1.00 42.65 ? 110 ALA B O 1 ATOM 2695 C CB . ALA B 2 112 ? 10.140 -38.843 4.607 1.00 44.07 ? 110 ALA B CB 1 ATOM 2696 N N . ASN B 2 113 ? 8.936 -37.999 1.991 1.00 44.05 ? 111 ASN B N 1 ATOM 2697 C CA . ASN B 2 113 ? 7.922 -37.770 0.963 1.00 43.96 ? 111 ASN B CA 1 ATOM 2698 C C . ASN B 2 113 ? 7.461 -39.059 0.290 1.00 45.78 ? 111 ASN B C 1 ATOM 2699 O O . ASN B 2 113 ? 8.264 -39.934 -0.055 1.00 45.42 ? 111 ASN B O 1 ATOM 2700 C CB . ASN B 2 113 ? 8.465 -36.825 -0.104 1.00 44.75 ? 111 ASN B CB 1 ATOM 2701 C CG . ASN B 2 113 ? 7.436 -36.493 -1.168 1.00 49.99 ? 111 ASN B CG 1 ATOM 2702 O OD1 . ASN B 2 113 ? 7.291 -37.217 -2.161 1.00 54.13 ? 111 ASN B OD1 1 ATOM 2703 N ND2 . ASN B 2 113 ? 6.725 -35.384 -0.976 1.00 52.12 ? 111 ASN B ND2 1 ATOM 2704 N N . LYS B 2 114 ? 6.143 -39.154 0.122 1.00 47.26 ? 112 LYS B N 1 ATOM 2705 C CA . LYS B 2 114 ? 5.504 -40.286 -0.536 1.00 48.78 ? 112 LYS B CA 1 ATOM 2706 C C . LYS B 2 114 ? 4.420 -39.819 -1.488 1.00 50.27 ? 112 LYS B C 1 ATOM 2707 O O . LYS B 2 114 ? 3.571 -38.994 -1.128 1.00 51.87 ? 112 LYS B O 1 ATOM 2708 C CB . LYS B 2 114 ? 4.878 -41.223 0.497 1.00 50.93 ? 112 LYS B CB 1 ATOM 2709 C CG . LYS B 2 114 ? 5.545 -42.591 0.619 1.00 54.75 ? 112 LYS B CG 1 ATOM 2710 C CD . LYS B 2 114 ? 4.501 -43.694 0.901 1.00 60.19 ? 112 LYS B CD 1 ATOM 2711 C CE . LYS B 2 114 ? 5.081 -44.847 1.727 1.00 65.74 ? 112 LYS B CE 1 ATOM 2712 N NZ . LYS B 2 114 ? 4.014 -45.737 2.291 1.00 69.77 ? 112 LYS B NZ 1 ATOM 2713 N N . LYS B 2 115 ? 4.443 -40.366 -2.695 1.00 50.35 ? 113 LYS B N 1 ATOM 2714 C CA . LYS B 2 115 ? 3.444 -40.028 -3.704 1.00 50.51 ? 113 LYS B CA 1 ATOM 2715 C C . LYS B 2 115 ? 2.460 -41.145 -3.898 1.00 50.22 ? 113 LYS B C 1 ATOM 2716 O O . LYS B 2 115 ? 2.830 -42.309 -4.050 1.00 48.69 ? 113 LYS B O 1 ATOM 2717 C CB . LYS B 2 115 ? 4.103 -39.731 -5.049 1.00 51.32 ? 113 LYS B CB 1 ATOM 2718 C CG . LYS B 2 115 ? 5.165 -38.661 -5.006 1.00 54.68 ? 113 LYS B CG 1 ATOM 2719 C CD . LYS B 2 115 ? 4.584 -37.251 -4.941 1.00 57.84 ? 113 LYS B CD 1 ATOM 2720 C CE . LYS B 2 115 ? 5.643 -36.213 -5.344 1.00 59.03 ? 113 LYS B CE 1 ATOM 2721 N NZ . LYS B 2 115 ? 6.989 -36.472 -4.710 1.00 57.08 ? 113 LYS B NZ 1 ATOM 2722 N N . PHE B 2 116 ? 1.194 -40.755 -3.919 1.00 51.67 ? 114 PHE B N 1 ATOM 2723 C CA . PHE B 2 116 ? 0.091 -41.680 -4.142 1.00 53.44 ? 114 PHE B CA 1 ATOM 2724 C C . PHE B 2 116 ? -0.793 -41.228 -5.285 1.00 55.12 ? 114 PHE B C 1 ATOM 2725 O O . PHE B 2 116 ? -1.316 -40.117 -5.265 1.00 55.57 ? 114 PHE B O 1 ATOM 2726 C CB . PHE B 2 116 ? -0.735 -41.791 -2.881 1.00 52.54 ? 114 PHE B CB 1 ATOM 2727 C CG . PHE B 2 116 ? -0.105 -42.646 -1.824 1.00 56.72 ? 114 PHE B CG 1 ATOM 2728 C CD1 . PHE B 2 116 ? -0.190 -44.029 -1.899 1.00 63.46 ? 114 PHE B CD1 1 ATOM 2729 C CD2 . PHE B 2 116 ? 0.557 -42.077 -0.745 1.00 57.46 ? 114 PHE B CD2 1 ATOM 2730 C CE1 . PHE B 2 116 ? 0.373 -44.827 -0.917 1.00 63.20 ? 114 PHE B CE1 1 ATOM 2731 C CE2 . PHE B 2 116 ? 1.133 -42.871 0.231 1.00 60.00 ? 114 PHE B CE2 1 ATOM 2732 C CZ . PHE B 2 116 ? 1.039 -44.251 0.138 1.00 62.96 ? 114 PHE B CZ 1 ATOM 2733 N N . LEU B 2 117 ? -0.956 -42.105 -6.271 1.00 56.78 ? 115 LEU B N 1 ATOM 2734 C CA . LEU B 2 117 ? -1.791 -41.825 -7.437 1.00 59.62 ? 115 LEU B CA 1 ATOM 2735 C C . LEU B 2 117 ? -3.139 -42.488 -7.283 1.00 63.95 ? 115 LEU B C 1 ATOM 2736 O O . LEU B 2 117 ? -3.274 -43.708 -7.411 1.00 65.90 ? 115 LEU B O 1 ATOM 2737 C CB . LEU B 2 117 ? -1.122 -42.310 -8.720 1.00 60.73 ? 115 LEU B CB 1 ATOM 2738 C CG . LEU B 2 117 ? -1.320 -41.362 -9.910 1.00 64.40 ? 115 LEU B CG 1 ATOM 2739 C CD1 . LEU B 2 117 ? -0.493 -41.812 -11.104 1.00 66.29 ? 115 LEU B CD1 1 ATOM 2740 C CD2 . LEU B 2 117 ? -2.799 -41.234 -10.280 1.00 65.45 ? 115 LEU B CD2 1 ATOM 2741 N N . LEU B 2 118 ? -4.143 -41.662 -7.023 1.00 66.17 ? 116 LEU B N 1 ATOM 2742 C CA . LEU B 2 118 ? -5.484 -42.151 -6.714 1.00 70.21 ? 116 LEU B CA 1 ATOM 2743 C C . LEU B 2 118 ? -6.380 -42.191 -7.935 1.00 74.05 ? 116 LEU B C 1 ATOM 2744 O O . LEU B 2 118 ? -6.416 -41.264 -8.746 1.00 75.72 ? 116 LEU B O 1 ATOM 2745 C CB . LEU B 2 118 ? -6.141 -41.294 -5.628 1.00 70.38 ? 116 LEU B CB 1 ATOM 2746 C CG . LEU B 2 118 ? -7.422 -41.894 -5.043 1.00 73.58 ? 116 LEU B CG 1 ATOM 2747 C CD1 . LEU B 2 118 ? -7.110 -43.181 -4.292 1.00 73.12 ? 116 LEU B CD1 1 ATOM 2748 C CD2 . LEU B 2 118 ? -8.109 -40.889 -4.142 1.00 76.30 ? 116 LEU B CD2 1 ATOM 2749 N N . THR B 2 119 ? -7.107 -43.297 -8.027 1.00 76.55 ? 117 THR B N 1 ATOM 2750 C CA . THR B 2 119 ? -8.020 -43.566 -9.136 1.00 79.16 ? 117 THR B CA 1 ATOM 2751 C C . THR B 2 119 ? -9.373 -44.022 -8.620 1.00 80.86 ? 117 THR B C 1 ATOM 2752 O O . THR B 2 119 ? -9.464 -44.944 -7.808 1.00 80.01 ? 117 THR B O 1 ATOM 2753 C CB . THR B 2 119 ? -7.448 -44.662 -10.054 1.00 80.52 ? 117 THR B CB 1 ATOM 2754 O OG1 . THR B 2 119 ? -6.080 -44.359 -10.361 1.00 81.81 ? 117 THR B OG1 1 ATOM 2755 C CG2 . THR B 2 119 ? -8.246 -44.769 -11.345 1.00 82.81 ? 117 THR B CG2 1 ATOM 2756 N N . VAL B 2 120 ? -10.418 -43.364 -9.111 1.00 82.68 ? 118 VAL B N 1 ATOM 2757 C CA . VAL B 2 120 ? -11.790 -43.642 -8.685 1.00 84.88 ? 118 VAL B CA 1 ATOM 2758 C C . VAL B 2 120 ? -12.688 -44.070 -9.840 1.00 88.12 ? 118 VAL B C 1 ATOM 2759 O O . VAL B 2 120 ? -13.126 -43.255 -10.654 1.00 89.74 ? 118 VAL B O 1 ATOM 2760 C CB . VAL B 2 120 ? -12.425 -42.422 -7.983 1.00 85.16 ? 118 VAL B CB 1 ATOM 2761 C CG1 . VAL B 2 120 ? -13.905 -42.692 -7.676 1.00 85.31 ? 118 VAL B CG1 1 ATOM 2762 C CG2 . VAL B 2 120 ? -11.644 -42.065 -6.711 1.00 77.52 ? 118 VAL B CG2 1 ATOM 2763 N N . LEU B 2 121 ? -12.964 -45.367 -9.880 1.00 89.81 ? 119 LEU B N 1 ATOM 2764 C CA . LEU B 2 121 ? -13.878 -45.950 -10.865 1.00 93.28 ? 119 LEU B CA 1 ATOM 2765 C C . LEU B 2 121 ? -15.310 -45.976 -10.353 1.00 95.59 ? 119 LEU B C 1 ATOM 2766 O O . LEU B 2 121 ? -15.565 -45.908 -9.149 1.00 94.82 ? 119 LEU B O 1 ATOM 2767 C CB . LEU B 2 121 ? -13.439 -47.369 -11.230 1.00 94.44 ? 119 LEU B CB 1 ATOM 2768 C CG . LEU B 2 121 ? -12.076 -47.464 -11.918 1.00 90.60 ? 119 LEU B CG 1 ATOM 2769 C CD1 . LEU B 2 121 ? -11.709 -48.921 -12.169 1.00 90.35 ? 119 LEU B CD1 1 ATOM 2770 C CD2 . LEU B 2 121 ? -12.080 -46.664 -13.221 1.00 88.30 ? 119 LEU B CD2 1 ATOM 2771 N N . VAL B 2 122 ? -16.232 -46.098 -11.294 1.00 98.75 ? 120 VAL B N 1 ATOM 2772 C CA . VAL B 2 122 ? -17.661 -46.051 -10.992 1.00 102.10 ? 120 VAL B CA 1 ATOM 2773 C C . VAL B 2 122 ? -18.403 -47.288 -11.478 1.00 106.24 ? 120 VAL B C 1 ATOM 2774 O O . VAL B 2 122 ? -18.414 -47.607 -12.667 1.00 106.99 ? 120 VAL B O 1 ATOM 2775 C CB . VAL B 2 122 ? -18.303 -44.796 -11.606 1.00 103.16 ? 120 VAL B CB 1 ATOM 2776 C CG1 . VAL B 2 122 ? -19.704 -44.602 -11.066 1.00 105.16 ? 120 VAL B CG1 1 ATOM 2777 C CG2 . VAL B 2 122 ? -17.436 -43.573 -11.323 1.00 98.35 ? 120 VAL B CG2 1 ATOM 2778 N N . LYS B 2 123 ? -19.016 -47.985 -10.530 1.00 91.17 ? 121 LYS B N 1 ATOM 2779 C CA . LYS B 2 123 ? -19.856 -49.146 -10.852 1.00 89.50 ? 121 LYS B CA 1 ATOM 2780 C C . LYS B 2 123 ? -21.058 -48.689 -11.675 1.00 88.62 ? 121 LYS B C 1 ATOM 2781 O O . LYS B 2 123 ? -21.778 -47.773 -11.270 1.00 89.21 ? 121 LYS B O 1 ATOM 2782 C CB . LYS B 2 123 ? -20.302 -49.904 -9.587 1.00 90.95 ? 121 LYS B CB 1 ATOM 2783 C CG . LYS B 2 123 ? -21.105 -49.084 -8.564 1.00 96.24 ? 121 LYS B CG 1 ATOM 2784 C CD . LYS B 2 123 ? -20.948 -49.647 -7.149 1.00 100.10 ? 121 LYS B CD 1 ATOM 2785 C CE . LYS B 2 123 ? -21.578 -48.734 -6.106 1.00 104.24 ? 121 LYS B CE 1 ATOM 2786 N NZ . LYS B 2 123 ? -21.799 -49.434 -4.808 1.00 104.73 ? 121 LYS B NZ 1 ATOM 2787 N N . PRO B 2 124 ? -21.269 -49.326 -12.843 1.00 87.10 ? 122 PRO B N 1 ATOM 2788 C CA . PRO B 2 124 ? -22.270 -48.864 -13.791 1.00 86.61 ? 122 PRO B CA 1 ATOM 2789 C C . PRO B 2 124 ? -23.660 -48.966 -13.215 1.00 88.19 ? 122 PRO B C 1 ATOM 2790 O O . PRO B 2 124 ? -24.090 -50.030 -12.765 1.00 87.22 ? 122 PRO B O 1 ATOM 2791 C CB . PRO B 2 124 ? -22.104 -49.819 -14.973 1.00 83.50 ? 122 PRO B CB 1 ATOM 2792 C CG . PRO B 2 124 ? -21.611 -51.067 -14.373 1.00 82.88 ? 122 PRO B CG 1 ATOM 2793 C CD . PRO B 2 124 ? -20.724 -50.639 -13.230 1.00 85.84 ? 122 PRO B CD 1 ATOM 2794 N N . SER B 2 125 ? -24.334 -47.828 -13.213 1.00 91.30 ? 123 SER B N 1 ATOM 2795 C CA . SER B 2 125 ? -25.704 -47.741 -12.735 1.00 93.98 ? 123 SER B CA 1 ATOM 2796 C C . SER B 2 125 ? -26.366 -46.468 -13.243 1.00 97.36 ? 123 SER B C 1 ATOM 2797 O O . SER B 2 125 ? -25.721 -45.424 -13.394 1.00 99.23 ? 123 SER B O 1 ATOM 2798 C CB . SER B 2 125 ? -25.750 -47.797 -11.208 1.00 96.27 ? 123 SER B CB 1 ATOM 2799 O OG . SER B 2 125 ? -26.994 -48.319 -10.775 1.00 98.36 ? 123 SER B OG 1 ATOM 2800 N N . GLY B 2 126 ? -27.658 -46.583 -13.525 1.00 98.72 ? 124 GLY B N 1 ATOM 2801 C CA . GLY B 2 126 ? -28.450 -45.457 -13.999 1.00 102.32 ? 124 GLY B CA 1 ATOM 2802 C C . GLY B 2 126 ? -28.530 -45.457 -15.508 1.00 100.47 ? 124 GLY B C 1 ATOM 2803 O O . GLY B 2 126 ? -28.309 -44.438 -16.160 1.00 102.67 ? 124 GLY B O 1 ATOM 2804 N N . THR B 2 127 ? -28.853 -46.616 -16.061 1.00 97.36 ? 125 THR B N 1 ATOM 2805 C CA . THR B 2 127 ? -28.958 -46.769 -17.506 1.00 95.66 ? 125 THR B CA 1 ATOM 2806 C C . THR B 2 127 ? -30.400 -46.639 -17.957 1.00 97.92 ? 125 THR B C 1 ATOM 2807 O O . THR B 2 127 ? -31.301 -47.269 -17.406 1.00 98.69 ? 125 THR B O 1 ATOM 2808 C CB . THR B 2 127 ? -28.408 -48.129 -17.980 1.00 91.98 ? 125 THR B CB 1 ATOM 2809 O OG1 . THR B 2 127 ? -29.353 -49.161 -17.682 1.00 90.92 ? 125 THR B OG1 1 ATOM 2810 C CG2 . THR B 2 127 ? -27.074 -48.451 -17.301 1.00 90.54 ? 125 THR B CG2 1 ATOM 2811 N N . ARG B 2 128 ? -30.599 -45.806 -18.967 1.00 99.84 ? 126 ARG B N 1 ATOM 2812 C CA . ARG B 2 128 ? -31.912 -45.634 -19.576 1.00 102.38 ? 126 ARG B CA 1 ATOM 2813 C C . ARG B 2 128 ? -32.053 -46.566 -20.761 1.00 99.07 ? 126 ARG B C 1 ATOM 2814 O O . ARG B 2 128 ? -31.148 -46.677 -21.590 1.00 96.18 ? 126 ARG B O 1 ATOM 2815 C CB . ARG B 2 128 ? -32.115 -44.193 -20.050 1.00 106.67 ? 126 ARG B CB 1 ATOM 2816 C CG . ARG B 2 128 ? -31.921 -43.134 -18.978 1.00 114.55 ? 126 ARG B CG 1 ATOM 2817 C CD . ARG B 2 128 ? -32.017 -41.725 -19.569 1.00 123.36 ? 126 ARG B CD 1 ATOM 2818 N NE . ARG B 2 128 ? -30.989 -41.472 -20.580 1.00 125.38 ? 126 ARG B NE 1 ATOM 2819 C CZ . ARG B 2 128 ? -30.828 -40.317 -21.222 1.00 131.84 ? 126 ARG B CZ 1 ATOM 2820 N NH1 . ARG B 2 128 ? -31.625 -39.286 -20.968 1.00 138.88 ? 126 ARG B NH1 1 ATOM 2821 N NH2 . ARG B 2 128 ? -29.863 -40.191 -22.122 1.00 131.05 ? 126 ARG B NH2 1 ATOM 2822 N N . CYS B 2 129 ? -33.200 -47.239 -20.809 1.00 100.06 ? 127 CYS B N 1 ATOM 2823 C CA . CYS B 2 129 ? -33.621 -48.038 -21.966 1.00 98.29 ? 127 CYS B CA 1 ATOM 2824 C C . CYS B 2 129 ? -34.745 -47.325 -22.688 1.00 100.82 ? 127 CYS B C 1 ATOM 2825 O O . CYS B 2 129 ? -35.843 -47.161 -22.148 1.00 104.23 ? 127 CYS B O 1 ATOM 2826 C CB . CYS B 2 129 ? -34.129 -49.418 -21.543 1.00 97.27 ? 127 CYS B CB 1 ATOM 2827 S SG . CYS B 2 129 ? -32.900 -50.526 -20.847 1.00 97.39 ? 127 CYS B SG 1 ATOM 2828 N N . PHE B 2 130 ? -34.478 -46.910 -23.918 1.00 99.57 ? 128 PHE B N 1 ATOM 2829 C CA . PHE B 2 130 ? -35.499 -46.218 -24.690 1.00 101.74 ? 128 PHE B CA 1 ATOM 2830 C C . PHE B 2 130 ? -35.459 -46.490 -26.188 1.00 99.75 ? 128 PHE B C 1 ATOM 2831 O O . PHE B 2 130 ? -34.409 -46.766 -26.776 1.00 96.38 ? 128 PHE B O 1 ATOM 2832 C CB . PHE B 2 130 ? -35.447 -44.713 -24.404 1.00 105.46 ? 128 PHE B CB 1 ATOM 2833 C CG . PHE B 2 130 ? -34.183 -44.040 -24.865 1.00 104.00 ? 128 PHE B CG 1 ATOM 2834 C CD1 . PHE B 2 130 ? -34.090 -43.510 -26.145 1.00 104.41 ? 128 PHE B CD1 1 ATOM 2835 C CD2 . PHE B 2 130 ? -33.101 -43.906 -24.008 1.00 103.14 ? 128 PHE B CD2 1 ATOM 2836 C CE1 . PHE B 2 130 ? -32.936 -42.877 -26.570 1.00 104.43 ? 128 PHE B CE1 1 ATOM 2837 C CE2 . PHE B 2 130 ? -31.941 -43.272 -24.426 1.00 102.89 ? 128 PHE B CE2 1 ATOM 2838 C CZ . PHE B 2 130 ? -31.858 -42.757 -25.709 1.00 104.13 ? 128 PHE B CZ 1 ATOM 2839 N N . VAL B 2 131 ? -36.652 -46.426 -26.769 1.00 101.42 ? 129 VAL B N 1 ATOM 2840 C CA . VAL B 2 131 ? -36.842 -46.435 -28.217 1.00 100.43 ? 129 VAL B CA 1 ATOM 2841 C C . VAL B 2 131 ? -36.951 -45.003 -28.705 1.00 103.29 ? 129 VAL B C 1 ATOM 2842 O O . VAL B 2 131 ? -37.305 -44.098 -27.948 1.00 106.04 ? 129 VAL B O 1 ATOM 2843 C CB . VAL B 2 131 ? -38.109 -47.218 -28.629 1.00 101.03 ? 129 VAL B CB 1 ATOM 2844 C CG1 . VAL B 2 131 ? -39.379 -46.443 -28.251 1.00 106.51 ? 129 VAL B CG1 1 ATOM 2845 C CG2 . VAL B 2 131 ? -38.081 -47.507 -30.116 1.00 99.55 ? 129 VAL B CG2 1 ATOM 2846 N N . ASP B 2 132 ? -36.637 -44.808 -29.978 1.00 102.95 ? 130 ASP B N 1 ATOM 2847 C CA . ASP B 2 132 ? -36.715 -43.476 -30.589 1.00 106.97 ? 130 ASP B CA 1 ATOM 2848 C C . ASP B 2 132 ? -38.037 -43.225 -31.336 1.00 110.31 ? 130 ASP B C 1 ATOM 2849 O O . ASP B 2 132 ? -38.202 -43.585 -32.501 1.00 109.35 ? 130 ASP B O 1 ATOM 2850 C CB . ASP B 2 132 ? -35.504 -43.217 -31.490 1.00 105.62 ? 130 ASP B CB 1 ATOM 2851 C CG . ASP B 2 132 ? -34.302 -42.728 -30.705 1.00 104.68 ? 130 ASP B CG 1 ATOM 2852 O OD1 . ASP B 2 132 ? -34.449 -41.756 -29.935 1.00 111.49 ? 130 ASP B OD1 1 ATOM 2853 O OD2 . ASP B 2 132 ? -33.212 -43.310 -30.852 1.00 101.06 ? 130 ASP B OD2 1 ATOM 2854 N N . GLY B 2 138 ? -42.727 -50.542 -40.672 1.00 106.49 ? 136 GLY B N 1 ATOM 2855 C CA . GLY B 2 138 ? -41.502 -50.768 -41.433 1.00 105.89 ? 136 GLY B CA 1 ATOM 2856 C C . GLY B 2 138 ? -40.585 -49.566 -41.364 1.00 105.86 ? 136 GLY B C 1 ATOM 2857 O O . GLY B 2 138 ? -40.023 -49.133 -42.369 1.00 106.78 ? 136 GLY B O 1 ATOM 2858 N N . ASN B 2 139 ? -40.436 -49.040 -40.153 1.00 105.49 ? 137 ASN B N 1 ATOM 2859 C CA . ASN B 2 139 ? -39.685 -47.804 -39.912 1.00 106.31 ? 137 ASN B CA 1 ATOM 2860 C C . ASN B 2 139 ? -38.175 -48.034 -39.774 1.00 104.36 ? 137 ASN B C 1 ATOM 2861 O O . ASN B 2 139 ? -37.650 -49.093 -40.140 1.00 102.17 ? 137 ASN B O 1 ATOM 2862 C CB . ASN B 2 139 ? -40.230 -47.086 -38.666 1.00 106.84 ? 137 ASN B CB 1 ATOM 2863 C CG . ASN B 2 139 ? -40.006 -45.587 -38.707 1.00 109.21 ? 137 ASN B CG 1 ATOM 2864 O OD1 . ASN B 2 139 ? -39.722 -45.019 -39.761 1.00 112.31 ? 137 ASN B OD1 1 ATOM 2865 N ND2 . ASN B 2 139 ? -40.134 -44.937 -37.553 1.00 108.11 ? 137 ASN B ND2 1 ATOM 2866 N N . ASP B 2 140 ? -37.506 -47.021 -39.229 1.00 105.72 ? 138 ASP B N 1 ATOM 2867 C CA . ASP B 2 140 ? -36.046 -46.948 -39.152 1.00 105.71 ? 138 ASP B CA 1 ATOM 2868 C C . ASP B 2 140 ? -35.605 -46.882 -37.678 1.00 103.89 ? 138 ASP B C 1 ATOM 2869 O O . ASP B 2 140 ? -34.781 -46.048 -37.288 1.00 104.21 ? 138 ASP B O 1 ATOM 2870 C CB . ASP B 2 140 ? -35.567 -45.709 -39.935 1.00 109.41 ? 138 ASP B CB 1 ATOM 2871 C CG . ASP B 2 140 ? -34.108 -45.804 -40.386 1.00 110.73 ? 138 ASP B CG 1 ATOM 2872 O OD1 . ASP B 2 140 ? -33.366 -46.671 -39.870 1.00 110.61 ? 138 ASP B OD1 1 ATOM 2873 O OD2 . ASP B 2 140 ? -33.706 -45.001 -41.261 1.00 113.56 ? 138 ASP B OD2 1 ATOM 2874 N N . PHE B 2 141 ? -36.150 -47.795 -36.876 1.00 102.64 ? 139 PHE B N 1 ATOM 2875 C CA . PHE B 2 141 ? -36.001 -47.772 -35.401 1.00 101.16 ? 139 PHE B CA 1 ATOM 2876 C C . PHE B 2 141 ? -34.573 -47.881 -34.881 1.00 98.10 ? 139 PHE B C 1 ATOM 2877 O O . PHE B 2 141 ? -33.649 -48.311 -35.573 1.00 97.20 ? 139 PHE B O 1 ATOM 2878 C CB . PHE B 2 141 ? -36.852 -48.876 -34.736 1.00 100.51 ? 139 PHE B CB 1 ATOM 2879 C CG . PHE B 2 141 ? -38.337 -48.657 -34.863 1.00 104.98 ? 139 PHE B CG 1 ATOM 2880 C CD1 . PHE B 2 141 ? -38.987 -47.741 -34.051 1.00 112.14 ? 139 PHE B CD1 1 ATOM 2881 C CD2 . PHE B 2 141 ? -39.077 -49.359 -35.802 1.00 106.76 ? 139 PHE B CD2 1 ATOM 2882 C CE1 . PHE B 2 141 ? -40.360 -47.527 -34.173 1.00 117.97 ? 139 PHE B CE1 1 ATOM 2883 C CE2 . PHE B 2 141 ? -40.444 -49.157 -35.927 1.00 113.42 ? 139 PHE B CE2 1 ATOM 2884 C CZ . PHE B 2 141 ? -41.087 -48.238 -35.113 1.00 118.00 ? 139 PHE B CZ 1 ATOM 2885 N N . LYS B 2 142 ? -34.428 -47.450 -33.635 1.00 97.03 ? 140 LYS B N 1 ATOM 2886 C CA . LYS B 2 142 ? -33.204 -47.655 -32.852 1.00 94.51 ? 140 LYS B CA 1 ATOM 2887 C C . LYS B 2 142 ? -33.531 -47.893 -31.383 1.00 92.48 ? 140 LYS B C 1 ATOM 2888 O O . LYS B 2 142 ? -34.133 -47.043 -30.725 1.00 93.58 ? 140 LYS B O 1 ATOM 2889 C CB . LYS B 2 142 ? -32.236 -46.473 -33.003 1.00 95.92 ? 140 LYS B CB 1 ATOM 2890 C CG . LYS B 2 142 ? -31.225 -46.687 -34.123 1.00 95.63 ? 140 LYS B CG 1 ATOM 2891 C CD . LYS B 2 142 ? -30.257 -45.533 -34.293 1.00 95.32 ? 140 LYS B CD 1 ATOM 2892 C CE . LYS B 2 142 ? -29.404 -45.736 -35.536 1.00 94.75 ? 140 LYS B CE 1 ATOM 2893 N NZ . LYS B 2 142 ? -28.678 -44.502 -35.919 1.00 99.17 ? 140 LYS B NZ 1 ATOM 2894 N N . LEU B 2 143 ? -33.150 -49.073 -30.895 1.00 89.85 ? 141 LEU B N 1 ATOM 2895 C CA . LEU B 2 143 ? -33.255 -49.405 -29.471 1.00 88.64 ? 141 LEU B CA 1 ATOM 2896 C C . LEU B 2 143 ? -31.931 -49.118 -28.768 1.00 87.36 ? 141 LEU B C 1 ATOM 2897 O O . LEU B 2 143 ? -30.847 -49.349 -29.306 1.00 85.78 ? 141 LEU B O 1 ATOM 2898 C CB . LEU B 2 143 ? -33.702 -50.856 -29.252 1.00 87.31 ? 141 LEU B CB 1 ATOM 2899 C CG . LEU B 2 143 ? -35.096 -51.237 -29.773 1.00 88.76 ? 141 LEU B CG 1 ATOM 2900 C CD1 . LEU B 2 143 ? -35.627 -52.425 -28.985 1.00 88.37 ? 141 LEU B CD1 1 ATOM 2901 C CD2 . LEU B 2 143 ? -36.095 -50.078 -29.712 1.00 86.28 ? 141 LEU B CD2 1 ATOM 2902 N N . LYS B 2 144 ? -32.047 -48.593 -27.557 1.00 88.15 ? 142 LYS B N 1 ATOM 2903 C CA . LYS B 2 144 ? -30.934 -47.920 -26.908 1.00 88.21 ? 142 LYS B CA 1 ATOM 2904 C C . LYS B 2 144 ? -30.857 -48.247 -25.420 1.00 87.95 ? 142 LYS B C 1 ATOM 2905 O O . LYS B 2 144 ? -31.871 -48.262 -24.716 1.00 88.52 ? 142 LYS B O 1 ATOM 2906 C CB . LYS B 2 144 ? -31.078 -46.407 -27.131 1.00 90.91 ? 142 LYS B CB 1 ATOM 2907 C CG . LYS B 2 144 ? -29.787 -45.706 -27.546 1.00 90.91 ? 142 LYS B CG 1 ATOM 2908 C CD . LYS B 2 144 ? -30.037 -44.339 -28.202 1.00 90.04 ? 142 LYS B CD 1 ATOM 2909 C CE . LYS B 2 144 ? -30.028 -44.411 -29.722 1.00 89.31 ? 142 LYS B CE 1 ATOM 2910 N NZ . LYS B 2 144 ? -30.024 -43.055 -30.353 1.00 91.16 ? 142 LYS B NZ 1 ATOM 2911 N N . CYS B 2 145 ? -29.636 -48.540 -24.979 1.00 87.07 ? 143 CYS B N 1 ATOM 2912 C CA . CYS B 2 145 ? -29.327 -48.815 -23.570 1.00 86.86 ? 143 CYS B CA 1 ATOM 2913 C C . CYS B 2 145 ? -28.199 -47.898 -23.129 1.00 87.04 ? 143 CYS B C 1 ATOM 2914 O O . CYS B 2 145 ? -27.031 -48.276 -23.150 1.00 85.93 ? 143 CYS B O 1 ATOM 2915 C CB . CYS B 2 145 ? -28.933 -50.288 -23.385 1.00 85.48 ? 143 CYS B CB 1 ATOM 2916 S SG . CYS B 2 145 ? -29.059 -50.940 -21.684 1.00 87.02 ? 143 CYS B SG 1 ATOM 2917 N N . GLU B 2 146 ? -28.571 -46.688 -22.734 1.00 89.51 ? 144 GLU B N 1 ATOM 2918 C CA . GLU B 2 146 ? -27.603 -45.624 -22.455 1.00 91.07 ? 144 GLU B CA 1 ATOM 2919 C C . GLU B 2 146 ? -27.334 -45.483 -20.957 1.00 91.27 ? 144 GLU B C 1 ATOM 2920 O O . GLU B 2 146 ? -28.218 -45.095 -20.199 1.00 94.07 ? 144 GLU B O 1 ATOM 2921 C CB . GLU B 2 146 ? -28.103 -44.293 -23.022 1.00 94.65 ? 144 GLU B CB 1 ATOM 2922 C CG . GLU B 2 146 ? -27.023 -43.226 -23.121 1.00 97.81 ? 144 GLU B CG 1 ATOM 2923 C CD . GLU B 2 146 ? -27.389 -42.090 -24.067 1.00 101.77 ? 144 GLU B CD 1 ATOM 2924 O OE1 . GLU B 2 146 ? -28.538 -42.058 -24.559 1.00 101.33 ? 144 GLU B OE1 1 ATOM 2925 O OE2 . GLU B 2 146 ? -26.520 -41.224 -24.318 1.00 104.61 ? 144 GLU B OE2 1 ATOM 2926 N N . PRO B 2 147 ? -26.107 -45.795 -20.524 1.00 89.27 ? 145 PRO B N 1 ATOM 2927 C CA . PRO B 2 147 ? -25.786 -45.740 -19.107 1.00 89.51 ? 145 PRO B CA 1 ATOM 2928 C C . PRO B 2 147 ? -25.184 -44.433 -18.657 1.00 92.33 ? 145 PRO B C 1 ATOM 2929 O O . PRO B 2 147 ? -24.521 -43.741 -19.429 1.00 93.00 ? 145 PRO B O 1 ATOM 2930 C CB . PRO B 2 147 ? -24.745 -46.852 -18.945 1.00 86.68 ? 145 PRO B CB 1 ATOM 2931 C CG . PRO B 2 147 ? -24.083 -46.978 -20.293 1.00 86.41 ? 145 PRO B CG 1 ATOM 2932 C CD . PRO B 2 147 ? -24.978 -46.305 -21.322 1.00 88.31 ? 145 PRO B CD 1 ATOM 2933 N N . LYS B 2 148 ? -25.460 -44.103 -17.403 1.00 94.52 ? 146 LYS B N 1 ATOM 2934 C CA . LYS B 2 148 ? -24.720 -43.064 -16.673 1.00 98.44 ? 146 LYS B CA 1 ATOM 2935 C C . LYS B 2 148 ? -25.139 -42.999 -15.196 1.00 100.28 ? 146 LYS B C 1 ATOM 2936 O O . LYS B 2 148 ? -26.328 -42.881 -14.894 1.00 101.52 ? 146 LYS B O 1 ATOM 2937 C CB . LYS B 2 148 ? -24.872 -41.687 -17.325 1.00 102.62 ? 146 LYS B CB 1 ATOM 2938 C CG . LYS B 2 148 ? -23.628 -40.827 -17.163 1.00 106.40 ? 146 LYS B CG 1 ATOM 2939 C CD . LYS B 2 148 ? -23.628 -39.643 -18.123 1.00 112.41 ? 146 LYS B CD 1 ATOM 2940 C CE . LYS B 2 148 ? -22.406 -38.753 -17.915 1.00 117.08 ? 146 LYS B CE 1 ATOM 2941 N NZ . LYS B 2 148 ? -22.453 -37.510 -18.739 1.00 121.52 ? 146 LYS B NZ 1 ATOM 2942 N N . GLU B 2 149 ? -24.173 -43.069 -14.279 1.00 100.18 ? 147 GLU B N 1 ATOM 2943 C CA . GLU B 2 149 ? -22.746 -43.121 -14.619 1.00 98.32 ? 147 GLU B CA 1 ATOM 2944 C C . GLU B 2 149 ? -22.262 -44.542 -14.815 1.00 92.54 ? 147 GLU B C 1 ATOM 2945 O O . GLU B 2 149 ? -22.922 -45.514 -14.446 1.00 90.28 ? 147 GLU B O 1 ATOM 2946 C CB . GLU B 2 149 ? -21.901 -42.457 -13.525 1.00 102.27 ? 147 GLU B CB 1 ATOM 2947 C CG . GLU B 2 149 ? -22.330 -41.035 -13.168 1.00 108.87 ? 147 GLU B CG 1 ATOM 2948 C CD . GLU B 2 149 ? -21.456 -40.409 -12.089 1.00 113.72 ? 147 GLU B CD 1 ATOM 2949 O OE1 . GLU B 2 149 ? -20.270 -40.127 -12.367 1.00 112.97 ? 147 GLU B OE1 1 ATOM 2950 O OE2 . GLU B 2 149 ? -21.959 -40.192 -10.965 1.00 117.61 ? 147 GLU B OE2 1 ATOM 2951 N N . GLY B 2 150 ? -21.085 -44.625 -15.414 1.00 90.82 ? 148 GLY B N 1 ATOM 2952 C CA . GLY B 2 150 ? -20.356 -45.887 -15.576 1.00 86.96 ? 148 GLY B CA 1 ATOM 2953 C C . GLY B 2 150 ? -18.898 -45.664 -15.935 1.00 87.14 ? 148 GLY B C 1 ATOM 2954 O O . GLY B 2 150 ? -18.364 -44.563 -15.776 1.00 90.70 ? 148 GLY B O 1 ATOM 2955 N N . SER B 2 151 ? -18.253 -46.720 -16.415 1.00 83.98 ? 149 SER B N 1 ATOM 2956 C CA . SER B 2 151 ? -16.890 -46.611 -16.945 1.00 85.22 ? 149 SER B CA 1 ATOM 2957 C C . SER B 2 151 ? -16.463 -47.816 -17.770 1.00 83.04 ? 149 SER B C 1 ATOM 2958 O O . SER B 2 151 ? -16.859 -48.959 -17.507 1.00 80.32 ? 149 SER B O 1 ATOM 2959 C CB . SER B 2 151 ? -15.869 -46.323 -15.836 1.00 87.78 ? 149 SER B CB 1 ATOM 2960 O OG . SER B 2 151 ? -16.237 -46.914 -14.608 1.00 87.35 ? 149 SER B OG 1 ATOM 2961 N N . LEU B 2 152 ? -15.637 -47.517 -18.770 1.00 84.20 ? 150 LEU B N 1 ATOM 2962 C CA . LEU B 2 152 ? -15.271 -48.466 -19.823 1.00 82.97 ? 150 LEU B CA 1 ATOM 2963 C C . LEU B 2 152 ? -14.093 -49.337 -19.415 1.00 83.49 ? 150 LEU B C 1 ATOM 2964 O O . LEU B 2 152 ? -13.353 -48.984 -18.504 1.00 85.35 ? 150 LEU B O 1 ATOM 2965 C CB . LEU B 2 152 ? -14.927 -47.714 -21.104 1.00 85.02 ? 150 LEU B CB 1 ATOM 2966 C CG . LEU B 2 152 ? -16.046 -46.822 -21.644 1.00 85.52 ? 150 LEU B CG 1 ATOM 2967 C CD1 . LEU B 2 152 ? -15.564 -46.087 -22.877 1.00 88.97 ? 150 LEU B CD1 1 ATOM 2968 C CD2 . LEU B 2 152 ? -17.295 -47.636 -21.949 1.00 81.67 ? 150 LEU B CD2 1 ATOM 2969 N N . PRO B 2 153 ? -13.924 -50.495 -20.075 1.00 82.50 ? 151 PRO B N 1 ATOM 2970 C CA . PRO B 2 153 ? -14.767 -51.017 -21.145 1.00 80.61 ? 151 PRO B CA 1 ATOM 2971 C C . PRO B 2 153 ? -16.038 -51.679 -20.618 1.00 76.87 ? 151 PRO B C 1 ATOM 2972 O O . PRO B 2 153 ? -15.980 -52.617 -19.813 1.00 75.24 ? 151 PRO B O 1 ATOM 2973 C CB . PRO B 2 153 ? -13.857 -52.042 -21.826 1.00 82.69 ? 151 PRO B CB 1 ATOM 2974 C CG . PRO B 2 153 ? -13.000 -52.562 -20.724 1.00 83.85 ? 151 PRO B CG 1 ATOM 2975 C CD . PRO B 2 153 ? -12.894 -51.472 -19.677 1.00 84.28 ? 151 PRO B CD 1 ATOM 2976 N N . LEU B 2 154 ? -17.169 -51.141 -21.070 1.00 74.56 ? 152 LEU B N 1 ATOM 2977 C CA . LEU B 2 154 ? -18.498 -51.655 -20.716 1.00 71.67 ? 152 LEU B CA 1 ATOM 2978 C C . LEU B 2 154 ? -18.910 -52.792 -21.619 1.00 71.93 ? 152 LEU B C 1 ATOM 2979 O O . LEU B 2 154 ? -18.544 -52.832 -22.792 1.00 72.92 ? 152 LEU B O 1 ATOM 2980 C CB . LEU B 2 154 ? -19.557 -50.555 -20.799 1.00 70.26 ? 152 LEU B CB 1 ATOM 2981 C CG . LEU B 2 154 ? -19.605 -49.610 -19.604 1.00 70.67 ? 152 LEU B CG 1 ATOM 2982 C CD1 . LEU B 2 154 ? -20.415 -48.373 -19.929 1.00 71.03 ? 152 LEU B CD1 1 ATOM 2983 C CD2 . LEU B 2 154 ? -20.179 -50.326 -18.394 1.00 69.61 ? 152 LEU B CD2 1 ATOM 2984 N N . GLN B 2 155 ? -19.669 -53.719 -21.044 1.00 72.18 ? 153 GLN B N 1 ATOM 2985 C CA . GLN B 2 155 ? -20.292 -54.811 -21.799 1.00 73.69 ? 153 GLN B CA 1 ATOM 2986 C C . GLN B 2 155 ? -21.814 -54.783 -21.662 1.00 73.98 ? 153 GLN B C 1 ATOM 2987 O O . GLN B 2 155 ? -22.354 -54.461 -20.600 1.00 73.13 ? 153 GLN B O 1 ATOM 2988 C CB . GLN B 2 155 ? -19.743 -56.163 -21.350 1.00 74.44 ? 153 GLN B CB 1 ATOM 2989 C CG . GLN B 2 155 ? -18.477 -56.572 -22.074 1.00 77.44 ? 153 GLN B CG 1 ATOM 2990 C CD . GLN B 2 155 ? -17.903 -57.888 -21.568 1.00 82.28 ? 153 GLN B CD 1 ATOM 2991 O OE1 . GLN B 2 155 ? -18.276 -58.376 -20.497 1.00 83.55 ? 153 GLN B OE1 1 ATOM 2992 N NE2 . GLN B 2 155 ? -16.986 -58.469 -22.337 1.00 82.55 ? 153 GLN B NE2 1 ATOM 2993 N N . PHE B 2 156 ? -22.489 -55.109 -22.762 1.00 76.10 ? 154 PHE B N 1 ATOM 2994 C CA . PHE B 2 156 ? -23.957 -55.168 -22.806 1.00 76.25 ? 154 PHE B CA 1 ATOM 2995 C C . PHE B 2 156 ? -24.430 -56.516 -23.318 1.00 78.70 ? 154 PHE B C 1 ATOM 2996 O O . PHE B 2 156 ? -23.830 -57.097 -24.220 1.00 80.23 ? 154 PHE B O 1 ATOM 2997 C CB . PHE B 2 156 ? -24.531 -54.076 -23.716 1.00 75.43 ? 154 PHE B CB 1 ATOM 2998 C CG . PHE B 2 156 ? -23.780 -52.780 -23.666 1.00 75.74 ? 154 PHE B CG 1 ATOM 2999 C CD1 . PHE B 2 156 ? -22.630 -52.603 -24.424 1.00 78.55 ? 154 PHE B CD1 1 ATOM 3000 C CD2 . PHE B 2 156 ? -24.223 -51.738 -22.872 1.00 75.00 ? 154 PHE B CD2 1 ATOM 3001 C CE1 . PHE B 2 156 ? -21.931 -51.412 -24.387 1.00 79.14 ? 154 PHE B CE1 1 ATOM 3002 C CE2 . PHE B 2 156 ? -23.533 -50.545 -22.828 1.00 77.53 ? 154 PHE B CE2 1 ATOM 3003 C CZ . PHE B 2 156 ? -22.381 -50.381 -23.587 1.00 79.93 ? 154 PHE B CZ 1 ATOM 3004 N N . GLU B 2 157 ? -25.518 -56.999 -22.734 1.00 80.69 ? 155 GLU B N 1 ATOM 3005 C CA . GLU B 2 157 ? -26.181 -58.217 -23.204 1.00 83.59 ? 155 GLU B CA 1 ATOM 3006 C C . GLU B 2 157 ? -27.702 -58.106 -23.120 1.00 84.57 ? 155 GLU B C 1 ATOM 3007 O O . GLU B 2 157 ? -28.277 -58.067 -22.029 1.00 85.85 ? 155 GLU B O 1 ATOM 3008 C CB . GLU B 2 157 ? -25.703 -59.413 -22.389 1.00 85.41 ? 155 GLU B CB 1 ATOM 3009 C CG . GLU B 2 157 ? -26.055 -60.754 -22.993 1.00 89.64 ? 155 GLU B CG 1 ATOM 3010 C CD . GLU B 2 157 ? -25.788 -61.895 -22.033 1.00 96.03 ? 155 GLU B CD 1 ATOM 3011 O OE1 . GLU B 2 157 ? -26.451 -61.953 -20.975 1.00 98.27 ? 155 GLU B OE1 1 ATOM 3012 O OE2 . GLU B 2 157 ? -24.912 -62.736 -22.330 1.00 100.92 ? 155 GLU B OE2 1 ATOM 3013 N N . TRP B 2 158 ? -28.340 -58.071 -24.286 1.00 84.79 ? 156 TRP B N 1 ATOM 3014 C CA . TRP B 2 158 ? -29.798 -57.920 -24.377 1.00 84.79 ? 156 TRP B CA 1 ATOM 3015 C C . TRP B 2 158 ? -30.435 -59.295 -24.516 1.00 87.77 ? 156 TRP B C 1 ATOM 3016 O O . TRP B 2 158 ? -29.843 -60.197 -25.120 1.00 90.36 ? 156 TRP B O 1 ATOM 3017 C CB . TRP B 2 158 ? -30.202 -57.072 -25.589 1.00 84.06 ? 156 TRP B CB 1 ATOM 3018 C CG . TRP B 2 158 ? -29.494 -55.751 -25.775 1.00 82.45 ? 156 TRP B CG 1 ATOM 3019 C CD1 . TRP B 2 158 ? -28.160 -55.550 -25.994 1.00 83.43 ? 156 TRP B CD1 1 ATOM 3020 C CD2 . TRP B 2 158 ? -30.103 -54.455 -25.831 1.00 81.99 ? 156 TRP B CD2 1 ATOM 3021 N NE1 . TRP B 2 158 ? -27.897 -54.211 -26.149 1.00 80.14 ? 156 TRP B NE1 1 ATOM 3022 C CE2 . TRP B 2 158 ? -29.073 -53.516 -26.058 1.00 81.88 ? 156 TRP B CE2 1 ATOM 3023 C CE3 . TRP B 2 158 ? -31.414 -53.994 -25.691 1.00 82.04 ? 156 TRP B CE3 1 ATOM 3024 C CZ2 . TRP B 2 158 ? -29.316 -52.145 -26.150 1.00 79.72 ? 156 TRP B CZ2 1 ATOM 3025 C CZ3 . TRP B 2 158 ? -31.654 -52.631 -25.788 1.00 82.69 ? 156 TRP B CZ3 1 ATOM 3026 C CH2 . TRP B 2 158 ? -30.610 -51.726 -26.018 1.00 81.04 ? 156 TRP B CH2 1 ATOM 3027 N N . GLN B 2 159 ? -31.643 -59.446 -23.969 1.00 88.64 ? 157 GLN B N 1 ATOM 3028 C CA . GLN B 2 159 ? -32.390 -60.725 -24.026 1.00 91.33 ? 157 GLN B CA 1 ATOM 3029 C C . GLN B 2 159 ? -33.922 -60.575 -24.141 1.00 92.49 ? 157 GLN B C 1 ATOM 3030 O O . GLN B 2 159 ? -34.450 -59.490 -24.415 1.00 90.82 ? 157 GLN B O 1 ATOM 3031 C CB . GLN B 2 159 ? -32.072 -61.582 -22.791 1.00 92.87 ? 157 GLN B CB 1 ATOM 3032 C CG . GLN B 2 159 ? -30.592 -61.842 -22.549 1.00 92.63 ? 157 GLN B CG 1 ATOM 3033 C CD . GLN B 2 159 ? -30.333 -62.517 -21.222 1.00 94.11 ? 157 GLN B CD 1 ATOM 3034 O OE1 . GLN B 2 159 ? -31.229 -63.119 -20.634 1.00 98.17 ? 157 GLN B OE1 1 ATOM 3035 N NE2 . GLN B 2 159 ? -29.104 -62.420 -20.741 1.00 93.59 ? 157 GLN B NE2 1 ATOM 3036 N N . LYS B 2 160 ? -34.615 -61.695 -23.938 1.00 95.32 ? 158 LYS B N 1 ATOM 3037 C CA . LYS B 2 160 ? -36.079 -61.743 -23.902 1.00 96.94 ? 158 LYS B CA 1 ATOM 3038 C C . LYS B 2 160 ? -36.578 -62.821 -22.947 1.00 100.95 ? 158 LYS B C 1 ATOM 3039 O O . LYS B 2 160 ? -35.890 -63.813 -22.706 1.00 102.57 ? 158 LYS B O 1 ATOM 3040 C CB . LYS B 2 160 ? -36.647 -62.001 -25.293 1.00 98.19 ? 158 LYS B CB 1 ATOM 3041 C CG . LYS B 2 160 ? -37.167 -60.756 -25.983 1.00 96.00 ? 158 LYS B CG 1 ATOM 3042 C CD . LYS B 2 160 ? -37.767 -61.086 -27.337 1.00 96.72 ? 158 LYS B CD 1 ATOM 3043 C CE . LYS B 2 160 ? -38.334 -59.852 -28.014 1.00 95.34 ? 158 LYS B CE 1 ATOM 3044 N NZ . LYS B 2 160 ? -39.164 -60.202 -29.203 1.00 97.62 ? 158 LYS B NZ 1 ATOM 3045 N N . MET B 2 167 ? -36.113 -63.726 -28.703 1.00 109.13 ? 165 MET B N 1 ATOM 3046 C CA . MET B 2 167 ? -35.118 -64.537 -29.390 1.00 111.27 ? 165 MET B CA 1 ATOM 3047 C C . MET B 2 167 ? -34.892 -64.018 -30.817 1.00 110.66 ? 165 MET B C 1 ATOM 3048 O O . MET B 2 167 ? -34.769 -64.815 -31.750 1.00 114.79 ? 165 MET B O 1 ATOM 3049 C CB . MET B 2 167 ? -35.594 -65.997 -29.442 1.00 117.00 ? 165 MET B CB 1 ATOM 3050 C CG . MET B 2 167 ? -36.187 -66.526 -28.133 1.00 118.82 ? 165 MET B CG 1 ATOM 3051 S SD . MET B 2 167 ? -35.069 -67.573 -27.179 1.00 122.27 ? 165 MET B SD 1 ATOM 3052 C CE . MET B 2 167 ? -35.309 -69.160 -27.981 1.00 126.52 ? 165 MET B CE 1 ATOM 3053 N N . PRO B 2 168 ? -34.816 -62.682 -30.991 1.00 106.39 ? 166 PRO B N 1 ATOM 3054 C CA . PRO B 2 168 ? -34.875 -62.067 -32.326 1.00 106.03 ? 166 PRO B CA 1 ATOM 3055 C C . PRO B 2 168 ? -33.665 -62.359 -33.202 1.00 107.12 ? 166 PRO B C 1 ATOM 3056 O O . PRO B 2 168 ? -32.529 -62.056 -32.841 1.00 105.30 ? 166 PRO B O 1 ATOM 3057 C CB . PRO B 2 168 ? -35.001 -60.571 -32.025 1.00 101.90 ? 166 PRO B CB 1 ATOM 3058 C CG . PRO B 2 168 ? -34.391 -60.392 -30.685 1.00 100.50 ? 166 PRO B CG 1 ATOM 3059 C CD . PRO B 2 168 ? -34.508 -61.697 -29.940 1.00 102.69 ? 166 PRO B CD 1 ATOM 3060 N N . THR B 2 169 ? -33.943 -62.941 -34.362 1.00 110.60 ? 167 THR B N 1 ATOM 3061 C CA . THR B 2 169 ? -32.898 -63.426 -35.270 1.00 113.45 ? 167 THR B CA 1 ATOM 3062 C C . THR B 2 169 ? -32.045 -62.328 -35.919 1.00 110.73 ? 167 THR B C 1 ATOM 3063 O O . THR B 2 169 ? -30.820 -62.441 -35.938 1.00 111.26 ? 167 THR B O 1 ATOM 3064 C CB . THR B 2 169 ? -33.468 -64.357 -36.370 1.00 119.07 ? 167 THR B CB 1 ATOM 3065 O OG1 . THR B 2 169 ? -34.822 -63.993 -36.673 1.00 119.88 ? 167 THR B OG1 1 ATOM 3066 C CG2 . THR B 2 169 ? -33.432 -65.809 -35.900 1.00 122.82 ? 167 THR B CG2 1 ATOM 3067 N N . PRO B 2 170 ? -32.676 -61.269 -36.464 1.00 108.43 ? 168 PRO B N 1 ATOM 3068 C CA . PRO B 2 170 ? -31.865 -60.253 -37.136 1.00 106.58 ? 168 PRO B CA 1 ATOM 3069 C C . PRO B 2 170 ? -31.299 -59.238 -36.154 1.00 101.92 ? 168 PRO B C 1 ATOM 3070 O O . PRO B 2 170 ? -30.653 -58.269 -36.558 1.00 100.77 ? 168 PRO B O 1 ATOM 3071 C CB . PRO B 2 170 ? -32.850 -59.583 -38.110 1.00 106.82 ? 168 PRO B CB 1 ATOM 3072 C CG . PRO B 2 170 ? -34.186 -60.249 -37.897 1.00 108.71 ? 168 PRO B CG 1 ATOM 3073 C CD . PRO B 2 170 ? -34.112 -60.985 -36.597 1.00 108.52 ? 168 PRO B CD 1 ATOM 3074 N N . TRP B 2 171 ? -31.550 -59.483 -34.872 1.00 99.45 ? 169 TRP B N 1 ATOM 3075 C CA . TRP B 2 171 ? -30.987 -58.673 -33.786 1.00 95.13 ? 169 TRP B CA 1 ATOM 3076 C C . TRP B 2 171 ? -29.867 -59.407 -33.054 1.00 94.75 ? 169 TRP B C 1 ATOM 3077 O O . TRP B 2 171 ? -29.099 -58.802 -32.310 1.00 92.65 ? 169 TRP B O 1 ATOM 3078 C CB . TRP B 2 171 ? -32.079 -58.283 -32.775 1.00 93.42 ? 169 TRP B CB 1 ATOM 3079 C CG . TRP B 2 171 ? -33.067 -57.266 -33.276 1.00 92.12 ? 169 TRP B CG 1 ATOM 3080 C CD1 . TRP B 2 171 ? -33.014 -56.580 -34.454 1.00 91.90 ? 169 TRP B CD1 1 ATOM 3081 C CD2 . TRP B 2 171 ? -34.233 -56.789 -32.589 1.00 92.42 ? 169 TRP B CD2 1 ATOM 3082 N NE1 . TRP B 2 171 ? -34.082 -55.725 -34.555 1.00 92.85 ? 169 TRP B NE1 1 ATOM 3083 C CE2 . TRP B 2 171 ? -34.846 -55.830 -33.422 1.00 92.77 ? 169 TRP B CE2 1 ATOM 3084 C CE3 . TRP B 2 171 ? -34.822 -57.087 -31.356 1.00 93.61 ? 169 TRP B CE3 1 ATOM 3085 C CZ2 . TRP B 2 171 ? -36.020 -55.164 -33.063 1.00 91.28 ? 169 TRP B CZ2 1 ATOM 3086 C CZ3 . TRP B 2 171 ? -35.990 -56.424 -30.999 1.00 94.58 ? 169 TRP B CZ3 1 ATOM 3087 C CH2 . TRP B 2 171 ? -36.575 -55.474 -31.852 1.00 92.84 ? 169 TRP B CH2 1 ATOM 3088 N N . LEU B 2 172 ? -29.784 -60.714 -33.273 1.00 97.10 ? 170 LEU B N 1 ATOM 3089 C CA . LEU B 2 172 ? -28.851 -61.569 -32.527 1.00 97.14 ? 170 LEU B CA 1 ATOM 3090 C C . LEU B 2 172 ? -27.431 -61.033 -32.564 1.00 95.74 ? 170 LEU B C 1 ATOM 3091 O O . LEU B 2 172 ? -26.672 -61.193 -31.610 1.00 94.00 ? 170 LEU B O 1 ATOM 3092 C CB . LEU B 2 172 ? -28.894 -63.012 -33.039 1.00 102.10 ? 170 LEU B CB 1 ATOM 3093 C CG . LEU B 2 172 ? -29.998 -63.834 -32.364 1.00 103.24 ? 170 LEU B CG 1 ATOM 3094 C CD1 . LEU B 2 172 ? -30.486 -64.987 -33.235 1.00 107.25 ? 170 LEU B CD1 1 ATOM 3095 C CD2 . LEU B 2 172 ? -29.515 -64.337 -31.003 1.00 102.38 ? 170 LEU B CD2 1 ATOM 3096 N N . ALA B 2 173 ? -27.091 -60.384 -33.669 1.00 96.47 ? 171 ALA B N 1 ATOM 3097 C CA . ALA B 2 173 ? -25.756 -59.818 -33.856 1.00 97.70 ? 171 ALA B CA 1 ATOM 3098 C C . ALA B 2 173 ? -25.544 -58.602 -32.963 1.00 94.15 ? 171 ALA B C 1 ATOM 3099 O O . ALA B 2 173 ? -24.420 -58.298 -32.563 1.00 94.23 ? 171 ALA B O 1 ATOM 3100 C CB . ALA B 2 173 ? -25.538 -59.441 -35.318 1.00 100.39 ? 171 ALA B CB 1 ATOM 3101 N N . GLU B 2 174 ? -26.640 -57.918 -32.659 1.00 92.24 ? 172 GLU B N 1 ATOM 3102 C CA . GLU B 2 174 ? -26.609 -56.675 -31.881 1.00 89.80 ? 172 GLU B CA 1 ATOM 3103 C C . GLU B 2 174 ? -26.705 -56.960 -30.404 1.00 87.29 ? 172 GLU B C 1 ATOM 3104 O O . GLU B 2 174 ? -26.575 -56.061 -29.576 1.00 85.28 ? 172 GLU B O 1 ATOM 3105 C CB . GLU B 2 174 ? -27.785 -55.777 -32.241 1.00 89.65 ? 172 GLU B CB 1 ATOM 3106 C CG . GLU B 2 174 ? -27.863 -55.359 -33.683 1.00 96.22 ? 172 GLU B CG 1 ATOM 3107 C CD . GLU B 2 174 ? -29.117 -54.550 -33.950 1.00 102.22 ? 172 GLU B CD 1 ATOM 3108 O OE1 . GLU B 2 174 ? -30.201 -54.963 -33.476 1.00 104.27 ? 172 GLU B OE1 1 ATOM 3109 O OE2 . GLU B 2 174 ? -29.019 -53.492 -34.612 1.00 109.37 ? 172 GLU B OE2 1 ATOM 3110 N N . MET B 2 175 ? -26.961 -58.220 -30.086 1.00 88.27 ? 173 MET B N 1 ATOM 3111 C CA . MET B 2 175 ? -27.111 -58.665 -28.698 1.00 87.23 ? 173 MET B CA 1 ATOM 3112 C C . MET B 2 175 ? -26.147 -57.995 -27.736 1.00 85.32 ? 173 MET B C 1 ATOM 3113 O O . MET B 2 175 ? -26.440 -57.854 -26.553 1.00 82.98 ? 173 MET B O 1 ATOM 3114 C CB . MET B 2 175 ? -26.879 -60.168 -28.582 1.00 90.59 ? 173 MET B CB 1 ATOM 3115 C CG . MET B 2 175 ? -28.135 -60.975 -28.441 1.00 92.58 ? 173 MET B CG 1 ATOM 3116 S SD . MET B 2 175 ? -27.789 -62.475 -27.508 1.00 98.09 ? 173 MET B SD 1 ATOM 3117 C CE . MET B 2 175 ? -27.359 -61.809 -25.898 1.00 91.96 ? 173 MET B CE 1 ATOM 3118 N N . THR B 2 176 ? -24.990 -57.609 -28.255 1.00 86.69 ? 174 THR B N 1 ATOM 3119 C CA . THR B 2 176 ? -23.877 -57.163 -27.425 1.00 86.90 ? 174 THR B CA 1 ATOM 3120 C C . THR B 2 176 ? -23.620 -55.675 -27.501 1.00 85.93 ? 174 THR B C 1 ATOM 3121 O O . THR B 2 176 ? -23.145 -55.060 -26.546 1.00 85.27 ? 174 THR B O 1 ATOM 3122 C CB . THR B 2 176 ? -22.606 -57.880 -27.841 1.00 89.83 ? 174 THR B CB 1 ATOM 3123 O OG1 . THR B 2 176 ? -22.720 -59.255 -27.468 1.00 93.56 ? 174 THR B OG1 1 ATOM 3124 C CG2 . THR B 2 176 ? -21.391 -57.263 -27.170 1.00 90.07 ? 174 THR B CG2 1 ATOM 3125 N N . SER B 2 177 ? -23.930 -55.108 -28.655 1.00 86.93 ? 175 SER B N 1 ATOM 3126 C CA . SER B 2 177 ? -23.805 -53.670 -28.871 1.00 86.76 ? 175 SER B CA 1 ATOM 3127 C C . SER B 2 177 ? -24.927 -52.936 -28.122 1.00 83.69 ? 175 SER B C 1 ATOM 3128 O O . SER B 2 177 ? -26.014 -53.477 -27.955 1.00 82.32 ? 175 SER B O 1 ATOM 3129 C CB . SER B 2 177 ? -23.858 -53.358 -30.369 1.00 89.06 ? 175 SER B CB 1 ATOM 3130 O OG . SER B 2 177 ? -24.879 -54.111 -31.006 1.00 91.60 ? 175 SER B OG 1 ATOM 3131 N N . PRO B 2 178 ? -24.662 -51.701 -27.669 1.00 82.60 ? 176 PRO B N 1 ATOM 3132 C CA . PRO B 2 178 ? -25.609 -50.969 -26.840 1.00 81.51 ? 176 PRO B CA 1 ATOM 3133 C C . PRO B 2 178 ? -26.730 -50.351 -27.646 1.00 82.38 ? 176 PRO B C 1 ATOM 3134 O O . PRO B 2 178 ? -27.639 -49.739 -27.085 1.00 83.16 ? 176 PRO B O 1 ATOM 3135 C CB . PRO B 2 178 ? -24.753 -49.860 -26.241 1.00 82.16 ? 176 PRO B CB 1 ATOM 3136 C CG . PRO B 2 178 ? -23.728 -49.595 -27.274 1.00 83.43 ? 176 PRO B CG 1 ATOM 3137 C CD . PRO B 2 178 ? -23.429 -50.929 -27.902 1.00 84.22 ? 176 PRO B CD 1 ATOM 3138 N N . VAL B 2 179 ? -26.653 -50.510 -28.959 1.00 83.17 ? 177 VAL B N 1 ATOM 3139 C CA . VAL B 2 179 ? -27.693 -49.995 -29.849 1.00 83.73 ? 177 VAL B CA 1 ATOM 3140 C C . VAL B 2 179 ? -28.198 -51.051 -30.821 1.00 83.50 ? 177 VAL B C 1 ATOM 3141 O O . VAL B 2 179 ? -27.432 -51.692 -31.542 1.00 83.92 ? 177 VAL B O 1 ATOM 3142 C CB . VAL B 2 179 ? -27.218 -48.759 -30.632 1.00 85.76 ? 177 VAL B CB 1 ATOM 3143 C CG1 . VAL B 2 179 ? -28.180 -48.454 -31.770 1.00 85.75 ? 177 VAL B CG1 1 ATOM 3144 C CG2 . VAL B 2 179 ? -27.088 -47.569 -29.695 1.00 85.07 ? 177 VAL B CG2 1 ATOM 3145 N N . ILE B 2 180 ? -29.510 -51.217 -30.811 1.00 82.99 ? 178 ILE B N 1 ATOM 3146 C CA . ILE B 2 180 ? -30.193 -52.086 -31.753 1.00 83.59 ? 178 ILE B CA 1 ATOM 3147 C C . ILE B 2 180 ? -30.843 -51.243 -32.840 1.00 84.71 ? 178 ILE B C 1 ATOM 3148 O O . ILE B 2 180 ? -32.039 -50.943 -32.781 1.00 84.60 ? 178 ILE B O 1 ATOM 3149 C CB . ILE B 2 180 ? -31.299 -52.927 -31.062 1.00 83.61 ? 178 ILE B CB 1 ATOM 3150 C CG1 . ILE B 2 180 ? -30.728 -53.735 -29.902 1.00 80.29 ? 178 ILE B CG1 1 ATOM 3151 C CG2 . ILE B 2 180 ? -32.015 -53.831 -32.077 1.00 85.18 ? 178 ILE B CG2 1 ATOM 3152 C CD1 . ILE B 2 180 ? -31.798 -54.447 -29.121 1.00 77.66 ? 178 ILE B CD1 1 ATOM 3153 N N . SER B 2 181 ? -30.042 -50.863 -33.828 1.00 85.33 ? 179 SER B N 1 ATOM 3154 C CA . SER B 2 181 ? -30.545 -50.105 -34.972 1.00 86.91 ? 179 SER B CA 1 ATOM 3155 C C . SER B 2 181 ? -31.463 -50.985 -35.810 1.00 87.22 ? 179 SER B C 1 ATOM 3156 O O . SER B 2 181 ? -31.025 -51.693 -36.711 1.00 88.16 ? 179 SER B O 1 ATOM 3157 C CB . SER B 2 181 ? -29.393 -49.558 -35.818 1.00 88.69 ? 179 SER B CB 1 ATOM 3158 O OG . SER B 2 181 ? -28.353 -50.508 -35.925 1.00 88.13 ? 179 SER B OG 1 ATOM 3159 N N . VAL B 2 182 ? -32.747 -50.916 -35.477 1.00 86.85 ? 180 VAL B N 1 ATOM 3160 C CA . VAL B 2 182 ? -33.797 -51.737 -36.094 1.00 87.13 ? 180 VAL B CA 1 ATOM 3161 C C . VAL B 2 182 ? -34.334 -51.092 -37.371 1.00 88.88 ? 180 VAL B C 1 ATOM 3162 O O . VAL B 2 182 ? -34.491 -49.875 -37.452 1.00 88.89 ? 180 VAL B O 1 ATOM 3163 C CB . VAL B 2 182 ? -34.958 -51.980 -35.091 1.00 86.63 ? 180 VAL B CB 1 ATOM 3164 C CG1 . VAL B 2 182 ? -36.071 -52.786 -35.733 1.00 88.04 ? 180 VAL B CG1 1 ATOM 3165 C CG2 . VAL B 2 182 ? -34.432 -52.684 -33.835 1.00 82.35 ? 180 VAL B CG2 1 ATOM 3166 N N . LYS B 2 183 ? -34.595 -51.924 -38.375 1.00 90.41 ? 181 LYS B N 1 ATOM 3167 C CA . LYS B 2 183 ? -35.076 -51.442 -39.682 1.00 93.18 ? 181 LYS B CA 1 ATOM 3168 C C . LYS B 2 183 ? -36.105 -52.366 -40.322 1.00 94.13 ? 181 LYS B C 1 ATOM 3169 O O . LYS B 2 183 ? -35.935 -53.584 -40.343 1.00 94.34 ? 181 LYS B O 1 ATOM 3170 C CB . LYS B 2 183 ? -33.897 -51.242 -40.650 1.00 94.91 ? 181 LYS B CB 1 ATOM 3171 C CG . LYS B 2 183 ? -32.886 -50.180 -40.202 1.00 95.62 ? 181 LYS B CG 1 ATOM 3172 C CD . LYS B 2 183 ? -31.929 -49.778 -41.319 1.00 98.63 ? 181 LYS B CD 1 ATOM 3173 C CE . LYS B 2 183 ? -30.825 -48.856 -40.797 1.00 99.10 ? 181 LYS B CE 1 ATOM 3174 N NZ . LYS B 2 183 ? -29.779 -48.568 -41.823 1.00 103.08 ? 181 LYS B NZ 1 ATOM 3175 N N . ASN B 2 184 ? -37.168 -51.760 -40.844 1.00 95.22 ? 182 ASN B N 1 ATOM 3176 C CA . ASN B 2 184 ? -38.210 -52.491 -41.566 1.00 97.28 ? 182 ASN B CA 1 ATOM 3177 C C . ASN B 2 184 ? -38.939 -53.486 -40.668 1.00 96.55 ? 182 ASN B C 1 ATOM 3178 O O . ASN B 2 184 ? -39.521 -53.111 -39.648 1.00 96.15 ? 182 ASN B O 1 ATOM 3179 C CB . ASN B 2 184 ? -37.615 -53.223 -42.775 1.00 99.14 ? 182 ASN B CB 1 ATOM 3180 C CG . ASN B 2 184 ? -38.676 -53.746 -43.722 1.00 102.55 ? 182 ASN B CG 1 ATOM 3181 O OD1 . ASN B 2 184 ? -39.813 -53.276 -43.715 1.00 104.57 ? 182 ASN B OD1 1 ATOM 3182 N ND2 . ASN B 2 184 ? -38.309 -54.719 -44.548 1.00 103.76 ? 182 ASN B ND2 1 ATOM 3183 N N . TYR B 2 193 ? -37.224 -59.801 -20.798 1.00 102.22 ? 191 TYR B N 1 ATOM 3184 C CA . TYR B 2 193 ? -36.645 -58.749 -21.631 1.00 98.98 ? 191 TYR B CA 1 ATOM 3185 C C . TYR B 2 193 ? -35.701 -57.842 -20.835 1.00 95.90 ? 191 TYR B C 1 ATOM 3186 O O . TYR B 2 193 ? -36.101 -57.211 -19.851 1.00 97.48 ? 191 TYR B O 1 ATOM 3187 C CB . TYR B 2 193 ? -37.758 -57.925 -22.278 1.00 100.14 ? 191 TYR B CB 1 ATOM 3188 C CG . TYR B 2 193 ? -37.336 -57.308 -23.583 1.00 99.71 ? 191 TYR B CG 1 ATOM 3189 C CD1 . TYR B 2 193 ? -36.333 -56.343 -23.627 1.00 98.60 ? 191 TYR B CD1 1 ATOM 3190 C CD2 . TYR B 2 193 ? -37.926 -57.698 -24.774 1.00 101.53 ? 191 TYR B CD2 1 ATOM 3191 C CE1 . TYR B 2 193 ? -35.937 -55.787 -24.823 1.00 97.37 ? 191 TYR B CE1 1 ATOM 3192 C CE2 . TYR B 2 193 ? -37.538 -57.147 -25.973 1.00 101.42 ? 191 TYR B CE2 1 ATOM 3193 C CZ . TYR B 2 193 ? -36.547 -56.193 -25.993 1.00 99.33 ? 191 TYR B CZ 1 ATOM 3194 O OH . TYR B 2 193 ? -36.173 -55.653 -27.198 1.00 101.59 ? 191 TYR B OH 1 ATOM 3195 N N . SER B 2 194 ? -34.450 -57.773 -21.291 1.00 91.64 ? 192 SER B N 1 ATOM 3196 C CA . SER B 2 194 ? -33.372 -57.130 -20.528 1.00 88.13 ? 192 SER B CA 1 ATOM 3197 C C . SER B 2 194 ? -32.407 -56.253 -21.323 1.00 85.21 ? 192 SER B C 1 ATOM 3198 O O . SER B 2 194 ? -32.484 -56.101 -22.546 1.00 83.67 ? 192 SER B O 1 ATOM 3199 C CB . SER B 2 194 ? -32.543 -58.203 -19.801 1.00 88.30 ? 192 SER B CB 1 ATOM 3200 O OG . SER B 2 194 ? -33.227 -58.727 -18.680 1.00 87.94 ? 192 SER B OG 1 ATOM 3201 N N . CYS B 2 195 ? -31.519 -55.650 -20.543 1.00 83.99 ? 193 CYS B N 1 ATOM 3202 C CA . CYS B 2 195 ? -30.242 -55.110 -21.014 1.00 81.42 ? 193 CYS B CA 1 ATOM 3203 C C . CYS B 2 195 ? -29.266 -55.050 -19.855 1.00 78.90 ? 193 CYS B C 1 ATOM 3204 O O . CYS B 2 195 ? -29.239 -54.074 -19.116 1.00 78.05 ? 193 CYS B O 1 ATOM 3205 C CB . CYS B 2 195 ? -30.389 -53.713 -21.614 1.00 81.62 ? 193 CYS B CB 1 ATOM 3206 S SG . CYS B 2 195 ? -28.769 -52.945 -21.917 1.00 83.94 ? 193 CYS B SG 1 ATOM 3207 N N . THR B 2 196 ? -28.474 -56.103 -19.706 1.00 78.01 ? 194 THR B N 1 ATOM 3208 C CA . THR B 2 196 ? -27.496 -56.198 -18.610 1.00 77.49 ? 194 THR B CA 1 ATOM 3209 C C . THR B 2 196 ? -26.190 -55.482 -18.937 1.00 75.11 ? 194 THR B C 1 ATOM 3210 O O . THR B 2 196 ? -25.585 -55.701 -19.985 1.00 74.61 ? 194 THR B O 1 ATOM 3211 C CB . THR B 2 196 ? -27.190 -57.666 -18.241 1.00 78.93 ? 194 THR B CB 1 ATOM 3212 O OG1 . THR B 2 196 ? -28.401 -58.317 -17.830 1.00 80.98 ? 194 THR B OG1 1 ATOM 3213 C CG2 . THR B 2 196 ? -26.163 -57.734 -17.115 1.00 77.69 ? 194 THR B CG2 1 ATOM 3214 N N . VAL B 2 197 ? -25.768 -54.627 -18.013 1.00 73.95 ? 195 VAL B N 1 ATOM 3215 C CA . VAL B 2 197 ? -24.602 -53.771 -18.215 1.00 72.68 ? 195 VAL B CA 1 ATOM 3216 C C . VAL B 2 197 ? -23.519 -54.018 -17.196 1.00 72.21 ? 195 VAL B C 1 ATOM 3217 O O . VAL B 2 197 ? -23.729 -53.906 -15.995 1.00 72.55 ? 195 VAL B O 1 ATOM 3218 C CB . VAL B 2 197 ? -24.983 -52.297 -18.153 1.00 72.76 ? 195 VAL B CB 1 ATOM 3219 C CG1 . VAL B 2 197 ? -23.735 -51.437 -18.246 1.00 73.34 ? 195 VAL B CG1 1 ATOM 3220 C CG2 . VAL B 2 197 ? -25.951 -51.972 -19.269 1.00 72.79 ? 195 VAL B CG2 1 ATOM 3221 N N . GLN B 2 198 ? -22.339 -54.319 -17.711 1.00 71.74 ? 196 GLN B N 1 ATOM 3222 C CA . GLN B 2 198 ? -21.243 -54.797 -16.883 1.00 72.77 ? 196 GLN B CA 1 ATOM 3223 C C . GLN B 2 198 ? -19.869 -54.233 -17.243 1.00 72.80 ? 196 GLN B C 1 ATOM 3224 O O . GLN B 2 198 ? -19.493 -54.121 -18.415 1.00 71.89 ? 196 GLN B O 1 ATOM 3225 C CB . GLN B 2 198 ? -21.239 -56.325 -16.947 1.00 74.00 ? 196 GLN B CB 1 ATOM 3226 C CG . GLN B 2 198 ? -19.889 -56.980 -17.119 1.00 77.39 ? 196 GLN B CG 1 ATOM 3227 C CD . GLN B 2 198 ? -20.001 -58.486 -17.262 1.00 82.00 ? 196 GLN B CD 1 ATOM 3228 O OE1 . GLN B 2 198 ? -20.779 -59.137 -16.560 1.00 80.68 ? 196 GLN B OE1 1 ATOM 3229 N NE2 . GLN B 2 198 ? -19.222 -59.049 -18.179 1.00 87.04 ? 196 GLN B NE2 1 ATOM 3230 N N . ASN B 2 199 ? -19.148 -53.847 -16.198 1.00 73.51 ? 197 ASN B N 1 ATOM 3231 C CA . ASN B 2 199 ? -17.710 -53.582 -16.292 1.00 74.91 ? 197 ASN B CA 1 ATOM 3232 C C . ASN B 2 199 ? -16.992 -54.456 -15.268 1.00 78.57 ? 197 ASN B C 1 ATOM 3233 O O . ASN B 2 199 ? -17.529 -55.477 -14.837 1.00 78.81 ? 197 ASN B O 1 ATOM 3234 C CB . ASN B 2 199 ? -17.374 -52.090 -16.119 1.00 73.83 ? 197 ASN B CB 1 ATOM 3235 C CG . ASN B 2 199 ? -17.729 -51.555 -14.747 1.00 69.29 ? 197 ASN B CG 1 ATOM 3236 O OD1 . ASN B 2 199 ? -17.958 -52.316 -13.809 1.00 65.55 ? 197 ASN B OD1 1 ATOM 3237 N ND2 . ASN B 2 199 ? -17.784 -50.236 -14.625 1.00 58.38 ? 197 ASN B ND2 1 ATOM 3238 N N . ARG B 2 200 ? -15.785 -54.069 -14.883 1.00 82.69 ? 198 ARG B N 1 ATOM 3239 C CA . ARG B 2 200 ? -14.995 -54.886 -13.965 1.00 86.82 ? 198 ARG B CA 1 ATOM 3240 C C . ARG B 2 200 ? -15.057 -54.340 -12.548 1.00 87.65 ? 198 ARG B C 1 ATOM 3241 O O . ARG B 2 200 ? -14.122 -54.508 -11.765 1.00 91.65 ? 198 ARG B O 1 ATOM 3242 C CB . ARG B 2 200 ? -13.546 -55.000 -14.438 1.00 90.04 ? 198 ARG B CB 1 ATOM 3243 C CG . ARG B 2 200 ? -13.373 -55.964 -15.603 1.00 95.56 ? 198 ARG B CG 1 ATOM 3244 C CD . ARG B 2 200 ? -11.903 -56.297 -15.849 1.00 103.92 ? 198 ARG B CD 1 ATOM 3245 N NE . ARG B 2 200 ? -11.750 -57.507 -16.655 1.00 109.89 ? 198 ARG B NE 1 ATOM 3246 C CZ . ARG B 2 200 ? -10.597 -58.140 -16.859 1.00 114.94 ? 198 ARG B CZ 1 ATOM 3247 N NH1 . ARG B 2 200 ? -9.473 -57.688 -16.318 1.00 116.69 ? 198 ARG B NH1 1 ATOM 3248 N NH2 . ARG B 2 200 ? -10.570 -59.235 -17.608 1.00 119.21 ? 198 ARG B NH2 1 ATOM 3249 N N . VAL B 2 201 ? -16.157 -53.670 -12.231 1.00 85.58 ? 199 VAL B N 1 ATOM 3250 C CA . VAL B 2 201 ? -16.387 -53.173 -10.866 1.00 85.83 ? 199 VAL B CA 1 ATOM 3251 C C . VAL B 2 201 ? -17.861 -53.195 -10.444 1.00 85.49 ? 199 VAL B C 1 ATOM 3252 O O . VAL B 2 201 ? -18.197 -52.787 -9.334 1.00 86.72 ? 199 VAL B O 1 ATOM 3253 C CB . VAL B 2 201 ? -15.845 -51.725 -10.682 1.00 86.61 ? 199 VAL B CB 1 ATOM 3254 C CG1 . VAL B 2 201 ? -14.409 -51.613 -11.162 1.00 85.89 ? 199 VAL B CG1 1 ATOM 3255 C CG2 . VAL B 2 201 ? -16.717 -50.718 -11.413 1.00 86.61 ? 199 VAL B CG2 1 ATOM 3256 N N . GLY B 2 202 ? -18.732 -53.664 -11.331 1.00 83.91 ? 200 GLY B N 1 ATOM 3257 C CA . GLY B 2 202 ? -20.172 -53.627 -11.074 1.00 83.98 ? 200 GLY B CA 1 ATOM 3258 C C . GLY B 2 202 ? -21.055 -54.005 -12.245 1.00 82.85 ? 200 GLY B C 1 ATOM 3259 O O . GLY B 2 202 ? -20.602 -54.089 -13.391 1.00 81.85 ? 200 GLY B O 1 ATOM 3260 N N . SER B 2 203 ? -22.324 -54.241 -11.925 1.00 83.53 ? 201 SER B N 1 ATOM 3261 C CA . SER B 2 203 ? -23.342 -54.632 -12.910 1.00 83.49 ? 201 SER B CA 1 ATOM 3262 C C . SER B 2 203 ? -24.641 -53.831 -12.779 1.00 84.34 ? 201 SER B C 1 ATOM 3263 O O . SER B 2 203 ? -24.776 -52.969 -11.910 1.00 86.38 ? 201 SER B O 1 ATOM 3264 C CB . SER B 2 203 ? -23.658 -56.128 -12.799 1.00 84.66 ? 201 SER B CB 1 ATOM 3265 O OG . SER B 2 203 ? -22.510 -56.920 -13.065 1.00 85.19 ? 201 SER B OG 1 ATOM 3266 N N . ASP B 2 204 ? -25.595 -54.144 -13.652 1.00 83.94 ? 202 ASP B N 1 ATOM 3267 C CA . ASP B 2 204 ? -26.822 -53.349 -13.799 1.00 85.30 ? 202 ASP B CA 1 ATOM 3268 C C . ASP B 2 204 ? -27.838 -54.011 -14.740 1.00 85.60 ? 202 ASP B C 1 ATOM 3269 O O . ASP B 2 204 ? -27.464 -54.702 -15.691 1.00 84.37 ? 202 ASP B O 1 ATOM 3270 C CB . ASP B 2 204 ? -26.477 -51.949 -14.325 1.00 84.78 ? 202 ASP B CB 1 ATOM 3271 C CG . ASP B 2 204 ? -27.406 -50.872 -13.794 1.00 85.86 ? 202 ASP B CG 1 ATOM 3272 O OD1 . ASP B 2 204 ? -27.693 -50.868 -12.576 1.00 88.43 ? 202 ASP B OD1 1 ATOM 3273 O OD2 . ASP B 2 204 ? -27.833 -50.013 -14.595 1.00 82.05 ? 202 ASP B OD2 1 ATOM 3274 N N . GLN B 2 205 ? -29.120 -53.780 -14.455 1.00 87.98 ? 203 GLN B N 1 ATOM 3275 C CA . GLN B 2 205 ? -30.243 -54.365 -15.216 1.00 88.27 ? 203 GLN B CA 1 ATOM 3276 C C . GLN B 2 205 ? -31.339 -53.358 -15.568 1.00 89.32 ? 203 GLN B C 1 ATOM 3277 O O . GLN B 2 205 ? -31.777 -52.566 -14.731 1.00 91.57 ? 203 GLN B O 1 ATOM 3278 C CB . GLN B 2 205 ? -30.867 -55.526 -14.442 1.00 90.54 ? 203 GLN B CB 1 ATOM 3279 C CG . GLN B 2 205 ? -30.700 -56.875 -15.111 1.00 89.59 ? 203 GLN B CG 1 ATOM 3280 C CD . GLN B 2 205 ? -31.996 -57.659 -15.125 1.00 92.01 ? 203 GLN B CD 1 ATOM 3281 O OE1 . GLN B 2 205 ? -33.074 -57.085 -15.270 1.00 92.26 ? 203 GLN B OE1 1 ATOM 3282 N NE2 . GLN B 2 205 ? -31.900 -58.974 -14.976 1.00 94.84 ? 203 GLN B NE2 1 ATOM 3283 N N . CYS B 2 206 ? -31.794 -53.433 -16.815 1.00 88.06 ? 204 CYS B N 1 ATOM 3284 C CA . CYS B 2 206 ? -32.729 -52.449 -17.382 1.00 89.58 ? 204 CYS B CA 1 ATOM 3285 C C . CYS B 2 206 ? -33.727 -53.074 -18.354 1.00 88.70 ? 204 CYS B C 1 ATOM 3286 O O . CYS B 2 206 ? -33.420 -54.049 -19.032 1.00 87.27 ? 204 CYS B O 1 ATOM 3287 C CB . CYS B 2 206 ? -31.926 -51.354 -18.089 1.00 88.83 ? 204 CYS B CB 1 ATOM 3288 S SG . CYS B 2 206 ? -32.887 -50.027 -18.862 1.00 95.19 ? 204 CYS B SG 1 ATOM 3289 N N . MET B 2 207 ? -34.921 -52.498 -18.423 1.00 90.59 ? 205 MET B N 1 ATOM 3290 C CA . MET B 2 207 ? -35.998 -53.073 -19.238 1.00 91.58 ? 205 MET B CA 1 ATOM 3291 C C . MET B 2 207 ? -36.685 -52.041 -20.131 1.00 91.89 ? 205 MET B C 1 ATOM 3292 O O . MET B 2 207 ? -36.843 -50.876 -19.760 1.00 93.13 ? 205 MET B O 1 ATOM 3293 C CB . MET B 2 207 ? -37.007 -53.798 -18.335 1.00 94.85 ? 205 MET B CB 1 ATOM 3294 C CG . MET B 2 207 ? -36.333 -54.568 -17.181 1.00 97.05 ? 205 MET B CG 1 ATOM 3295 S SD . MET B 2 207 ? -37.027 -56.185 -16.791 1.00 105.27 ? 205 MET B SD 1 ATOM 3296 C CE . MET B 2 207 ? -36.048 -56.655 -15.362 1.00 98.41 ? 205 MET B CE 1 ATOM 3297 N N . LEU B 2 208 ? -37.063 -52.493 -21.324 1.00 90.54 ? 206 LEU B N 1 ATOM 3298 C CA . LEU B 2 208 ? -37.647 -51.623 -22.354 1.00 91.01 ? 206 LEU B CA 1 ATOM 3299 C C . LEU B 2 208 ? -38.828 -52.278 -23.046 1.00 92.98 ? 206 LEU B C 1 ATOM 3300 O O . LEU B 2 208 ? -38.932 -53.507 -23.095 1.00 93.03 ? 206 LEU B O 1 ATOM 3301 C CB . LEU B 2 208 ? -36.592 -51.287 -23.413 1.00 87.93 ? 206 LEU B CB 1 ATOM 3302 C CG . LEU B 2 208 ? -36.673 -49.941 -24.145 1.00 88.50 ? 206 LEU B CG 1 ATOM 3303 C CD1 . LEU B 2 208 ? -35.359 -49.678 -24.871 1.00 87.00 ? 206 LEU B CD1 1 ATOM 3304 C CD2 . LEU B 2 208 ? -37.830 -49.872 -25.127 1.00 89.70 ? 206 LEU B CD2 1 ATOM 3305 N N . ARG B 2 209 ? -39.706 -51.437 -23.588 1.00 95.27 ? 207 ARG B N 1 ATOM 3306 C CA . ARG B 2 209 ? -40.819 -51.897 -24.431 1.00 96.89 ? 207 ARG B CA 1 ATOM 3307 C C . ARG B 2 209 ? -40.933 -51.149 -25.762 1.00 95.84 ? 207 ARG B C 1 ATOM 3308 O O . ARG B 2 209 ? -40.667 -49.951 -25.865 1.00 96.49 ? 207 ARG B O 1 ATOM 3309 C CB . ARG B 2 209 ? -42.148 -51.856 -23.668 1.00 101.72 ? 207 ARG B CB 1 ATOM 3310 C CG . ARG B 2 209 ? -43.269 -52.546 -24.428 1.00 106.95 ? 207 ARG B CG 1 ATOM 3311 C CD . ARG B 2 209 ? -44.150 -53.419 -23.552 1.00 113.43 ? 207 ARG B CD 1 ATOM 3312 N NE . ARG B 2 209 ? -44.568 -54.624 -24.273 1.00 116.28 ? 207 ARG B NE 1 ATOM 3313 C CZ . ARG B 2 209 ? -45.444 -54.641 -25.275 1.00 120.62 ? 207 ARG B CZ 1 ATOM 3314 N NH1 . ARG B 2 209 ? -46.014 -53.518 -25.694 1.00 125.09 ? 207 ARG B NH1 1 ATOM 3315 N NH2 . ARG B 2 209 ? -45.754 -55.788 -25.864 1.00 121.36 ? 207 ARG B NH2 1 ATOM 3316 N N . LEU B 2 210 ? -41.332 -51.911 -26.774 1.00 94.68 ? 208 LEU B N 1 ATOM 3317 C CA . LEU B 2 210 ? -41.443 -51.450 -28.166 1.00 93.46 ? 208 LEU B CA 1 ATOM 3318 C C . LEU B 2 210 ? -42.799 -51.840 -28.747 1.00 95.88 ? 208 LEU B C 1 ATOM 3319 O O . LEU B 2 210 ? -43.409 -52.823 -28.323 1.00 97.17 ? 208 LEU B O 1 ATOM 3320 C CB . LEU B 2 210 ? -40.298 -52.067 -28.994 1.00 89.46 ? 208 LEU B CB 1 ATOM 3321 C CG . LEU B 2 210 ? -40.378 -52.237 -30.513 1.00 87.31 ? 208 LEU B CG 1 ATOM 3322 C CD1 . LEU B 2 210 ? -40.676 -50.933 -31.228 1.00 88.95 ? 208 LEU B CD1 1 ATOM 3323 C CD2 . LEU B 2 210 ? -39.064 -52.811 -31.000 1.00 80.68 ? 208 LEU B CD2 1 ATOM 3324 N N . ASP B 2 211 ? -43.281 -51.053 -29.702 1.00 96.37 ? 209 ASP B N 1 ATOM 3325 C CA . ASP B 2 211 ? -44.518 -51.418 -30.391 1.00 98.99 ? 209 ASP B CA 1 ATOM 3326 C C . ASP B 2 211 ? -44.636 -50.954 -31.838 1.00 98.31 ? 209 ASP B C 1 ATOM 3327 O O . ASP B 2 211 ? -44.356 -49.803 -32.180 1.00 98.23 ? 209 ASP B O 1 ATOM 3328 C CB . ASP B 2 211 ? -45.724 -50.967 -29.582 1.00 104.15 ? 209 ASP B CB 1 ATOM 3329 C CG . ASP B 2 211 ? -46.758 -52.058 -29.460 1.00 108.12 ? 209 ASP B CG 1 ATOM 3330 O OD1 . ASP B 2 211 ? -46.881 -52.852 -30.417 1.00 113.30 ? 209 ASP B OD1 1 ATOM 3331 O OD2 . ASP B 2 211 ? -47.430 -52.139 -28.413 1.00 111.39 ? 209 ASP B OD2 1 ATOM 3332 N N . VAL B 2 212 ? -45.072 -51.896 -32.668 1.00 97.94 ? 210 VAL B N 1 ATOM 3333 C CA . VAL B 2 212 ? -45.208 -51.712 -34.112 1.00 98.00 ? 210 VAL B CA 1 ATOM 3334 C C . VAL B 2 212 ? -46.669 -51.789 -34.552 1.00 102.37 ? 210 VAL B C 1 ATOM 3335 O O . VAL B 2 212 ? -47.526 -52.288 -33.822 1.00 104.50 ? 210 VAL B O 1 ATOM 3336 C CB . VAL B 2 212 ? -44.399 -52.787 -34.881 1.00 95.33 ? 210 VAL B CB 1 ATOM 3337 C CG1 . VAL B 2 212 ? -44.996 -53.042 -36.269 1.00 97.12 ? 210 VAL B CG1 1 ATOM 3338 C CG2 . VAL B 2 212 ? -42.930 -52.386 -34.971 1.00 90.69 ? 210 VAL B CG2 1 HETATM 3339 C C1 . NAG C 3 . ? 29.613 -28.598 5.345 1.00 84.52 ? 401 NAG A C1 1 HETATM 3340 C C2 . NAG C 3 . ? 30.145 -29.952 4.898 1.00 90.24 ? 401 NAG A C2 1 HETATM 3341 C C3 . NAG C 3 . ? 30.758 -30.703 6.077 1.00 92.96 ? 401 NAG A C3 1 HETATM 3342 C C4 . NAG C 3 . ? 31.689 -29.813 6.910 1.00 96.21 ? 401 NAG A C4 1 HETATM 3343 C C5 . NAG C 3 . ? 31.105 -28.424 7.155 1.00 98.84 ? 401 NAG A C5 1 HETATM 3344 C C6 . NAG C 3 . ? 32.131 -27.474 7.774 1.00 107.50 ? 401 NAG A C6 1 HETATM 3345 C C7 . NAG C 3 . ? 28.850 -30.616 2.959 1.00 91.99 ? 401 NAG A C7 1 HETATM 3346 C C8 . NAG C 3 . ? 27.728 -31.437 2.393 1.00 90.88 ? 401 NAG A C8 1 HETATM 3347 N N2 . NAG C 3 . ? 29.084 -30.718 4.266 1.00 91.73 ? 401 NAG A N2 1 HETATM 3348 O O3 . NAG C 3 . ? 31.477 -31.801 5.557 1.00 95.00 ? 401 NAG A O3 1 HETATM 3349 O O4 . NAG C 3 . ? 31.965 -30.391 8.169 1.00 93.89 ? 401 NAG A O4 1 HETATM 3350 O O5 . NAG C 3 . ? 30.671 -27.878 5.935 1.00 92.81 ? 401 NAG A O5 1 HETATM 3351 O O6 . NAG C 3 . ? 31.534 -26.193 7.946 1.00 114.44 ? 401 NAG A O6 1 HETATM 3352 O O7 . NAG C 3 . ? 29.517 -29.888 2.226 1.00 96.57 ? 401 NAG A O7 1 HETATM 3353 C C1 . NAG D 3 . ? 33.394 -30.379 8.310 1.00 91.04 ? 402 NAG A C1 1 HETATM 3354 C C2 . NAG D 3 . ? 33.796 -30.547 9.775 1.00 92.39 ? 402 NAG A C2 1 HETATM 3355 C C3 . NAG D 3 . ? 35.321 -30.602 9.860 1.00 92.30 ? 402 NAG A C3 1 HETATM 3356 C C4 . NAG D 3 . ? 35.903 -31.605 8.868 1.00 86.74 ? 402 NAG A C4 1 HETATM 3357 C C5 . NAG D 3 . ? 35.349 -31.387 7.461 1.00 84.96 ? 402 NAG A C5 1 HETATM 3358 C C6 . NAG D 3 . ? 35.834 -32.436 6.451 1.00 83.61 ? 402 NAG A C6 1 HETATM 3359 C C7 . NAG D 3 . ? 33.555 -28.526 11.346 1.00 99.21 ? 402 NAG A C7 1 HETATM 3360 C C8 . NAG D 3 . ? 35.005 -28.239 11.643 1.00 103.74 ? 402 NAG A C8 1 HETATM 3361 N N2 . NAG D 3 . ? 33.103 -29.516 10.558 1.00 92.51 ? 402 NAG A N2 1 HETATM 3362 O O3 . NAG D 3 . ? 35.740 -30.873 11.185 1.00 99.59 ? 402 NAG A O3 1 HETATM 3363 O O4 . NAG D 3 . ? 37.284 -31.384 8.783 1.00 82.48 ? 402 NAG A O4 1 HETATM 3364 O O5 . NAG D 3 . ? 33.941 -31.393 7.498 1.00 88.67 ? 402 NAG A O5 1 HETATM 3365 O O6 . NAG D 3 . ? 35.838 -33.747 6.995 1.00 80.95 ? 402 NAG A O6 1 HETATM 3366 O O7 . NAG D 3 . ? 32.715 -27.801 11.868 1.00 99.40 ? 402 NAG A O7 1 HETATM 3367 C C1 . BMA E 4 . ? 38.010 -32.201 9.707 1.00 85.70 ? 403 BMA A C1 1 HETATM 3368 C C2 . BMA E 4 . ? 39.248 -32.682 8.960 1.00 87.52 ? 403 BMA A C2 1 HETATM 3369 C C3 . BMA E 4 . ? 40.354 -33.256 9.857 1.00 93.90 ? 403 BMA A C3 1 HETATM 3370 C C4 . BMA E 4 . ? 40.432 -32.578 11.233 1.00 98.32 ? 403 BMA A C4 1 HETATM 3371 C C5 . BMA E 4 . ? 39.053 -32.228 11.789 1.00 97.12 ? 403 BMA A C5 1 HETATM 3372 C C6 . BMA E 4 . ? 39.180 -31.442 13.091 1.00 104.09 ? 403 BMA A C6 1 HETATM 3373 O O2 . BMA E 4 . ? 39.738 -31.626 8.160 1.00 85.94 ? 403 BMA A O2 1 HETATM 3374 O O3 . BMA E 4 . ? 41.597 -33.213 9.166 1.00 95.04 ? 403 BMA A O3 1 HETATM 3375 O O4 . BMA E 4 . ? 41.065 -33.421 12.172 1.00 96.35 ? 403 BMA A O4 1 HETATM 3376 O O5 . BMA E 4 . ? 38.335 -31.464 10.855 1.00 86.94 ? 403 BMA A O5 1 HETATM 3377 O O6 . BMA E 4 . ? 37.947 -30.814 13.381 1.00 105.48 ? 403 BMA A O6 1 HETATM 3378 C C1 . MAN F 5 . ? 41.749 -34.350 8.273 1.00 95.45 ? 405 MAN A C1 1 HETATM 3379 C C2 . MAN F 5 . ? 43.228 -34.633 8.034 1.00 102.12 ? 405 MAN A C2 1 HETATM 3380 C C3 . MAN F 5 . ? 43.865 -33.651 7.066 1.00 100.41 ? 405 MAN A C3 1 HETATM 3381 C C4 . MAN F 5 . ? 43.069 -33.659 5.770 1.00 94.79 ? 405 MAN A C4 1 HETATM 3382 C C5 . MAN F 5 . ? 41.599 -33.357 6.048 1.00 88.70 ? 405 MAN A C5 1 HETATM 3383 C C6 . MAN F 5 . ? 40.792 -33.489 4.759 1.00 80.60 ? 405 MAN A C6 1 HETATM 3384 O O2 . MAN F 5 . ? 43.336 -35.929 7.496 1.00 104.76 ? 405 MAN A O2 1 HETATM 3385 O O3 . MAN F 5 . ? 45.207 -34.026 6.822 1.00 106.44 ? 405 MAN A O3 1 HETATM 3386 O O4 . MAN F 5 . ? 43.608 -32.702 4.886 1.00 93.63 ? 405 MAN A O4 1 HETATM 3387 O O5 . MAN F 5 . ? 41.064 -34.236 7.028 1.00 90.60 ? 405 MAN A O5 1 HETATM 3388 O O6 . MAN F 5 . ? 39.412 -33.363 5.032 1.00 78.35 ? 405 MAN A O6 1 HETATM 3389 C C1 . FUC G 6 . ? 31.562 -25.635 9.284 1.00 122.89 ? 406 FUC A C1 1 HETATM 3390 C C2 . FUC G 6 . ? 32.247 -24.304 9.072 1.00 125.86 ? 406 FUC A C2 1 HETATM 3391 C C3 . FUC G 6 . ? 31.329 -23.387 8.275 1.00 122.94 ? 406 FUC A C3 1 HETATM 3392 C C4 . FUC G 6 . ? 30.017 -23.220 9.035 1.00 120.57 ? 406 FUC A C4 1 HETATM 3393 C C5 . FUC G 6 . ? 29.384 -24.589 9.270 1.00 118.14 ? 406 FUC A C5 1 HETATM 3394 C C6 . FUC G 6 . ? 28.144 -24.461 10.149 1.00 116.70 ? 406 FUC A C6 1 HETATM 3395 O O2 . FUC G 6 . ? 33.393 -24.630 8.322 1.00 125.19 ? 406 FUC A O2 1 HETATM 3396 O O3 . FUC G 6 . ? 31.942 -22.136 8.042 1.00 125.26 ? 406 FUC A O3 1 HETATM 3397 O O4 . FUC G 6 . ? 30.267 -22.604 10.280 1.00 123.53 ? 406 FUC A O4 1 HETATM 3398 O O5 . FUC G 6 . ? 30.291 -25.477 9.900 1.00 121.15 ? 406 FUC A O5 1 HETATM 3399 C C1 . NAG H 3 . ? -6.480 -17.423 9.347 1.00 118.46 ? 501 NAG A C1 1 HETATM 3400 C C2 . NAG H 3 . ? -7.749 -18.126 8.895 1.00 123.61 ? 501 NAG A C2 1 HETATM 3401 C C3 . NAG H 3 . ? -8.793 -17.929 9.963 1.00 128.49 ? 501 NAG A C3 1 HETATM 3402 C C4 . NAG H 3 . ? -8.278 -18.447 11.293 1.00 127.07 ? 501 NAG A C4 1 HETATM 3403 C C5 . NAG H 3 . ? -6.925 -17.792 11.579 1.00 123.35 ? 501 NAG A C5 1 HETATM 3404 C C6 . NAG H 3 . ? -6.363 -18.259 12.919 1.00 122.66 ? 501 NAG A C6 1 HETATM 3405 C C7 . NAG H 3 . ? -8.135 -17.901 6.442 1.00 127.25 ? 501 NAG A C7 1 HETATM 3406 C C8 . NAG H 3 . ? -8.942 -17.123 5.448 1.00 131.44 ? 501 NAG A C8 1 HETATM 3407 N N2 . NAG H 3 . ? -8.365 -17.551 7.714 1.00 129.10 ? 501 NAG A N2 1 HETATM 3408 O O3 . NAG H 3 . ? -9.949 -18.609 9.546 1.00 132.22 ? 501 NAG A O3 1 HETATM 3409 O O4 . NAG H 3 . ? -9.218 -18.140 12.301 1.00 130.86 ? 501 NAG A O4 1 HETATM 3410 O O5 . NAG H 3 . ? -6.014 -18.057 10.520 1.00 116.63 ? 501 NAG A O5 1 HETATM 3411 O O6 . NAG H 3 . ? -7.288 -17.974 13.949 1.00 128.11 ? 501 NAG A O6 1 HETATM 3412 O O7 . NAG H 3 . ? -7.330 -18.759 6.062 1.00 118.49 ? 501 NAG A O7 1 HETATM 3413 C C1 . NAG I 3 . ? -9.455 -46.777 7.325 1.00 87.83 ? 301 NAG B C1 1 HETATM 3414 C C2 . NAG I 3 . ? -10.027 -47.510 8.536 1.00 86.34 ? 301 NAG B C2 1 HETATM 3415 C C3 . NAG I 3 . ? -9.754 -49.012 8.467 1.00 90.84 ? 301 NAG B C3 1 HETATM 3416 C C4 . NAG I 3 . ? -10.030 -49.568 7.079 1.00 94.58 ? 301 NAG B C4 1 HETATM 3417 C C5 . NAG I 3 . ? -9.296 -48.728 6.041 1.00 92.92 ? 301 NAG B C5 1 HETATM 3418 C C6 . NAG I 3 . ? -9.487 -49.242 4.614 1.00 94.87 ? 301 NAG B C6 1 HETATM 3419 C C7 . NAG I 3 . ? -9.750 -45.782 10.246 1.00 88.08 ? 301 NAG B C7 1 HETATM 3420 C C8 . NAG I 3 . ? -9.029 -45.337 11.490 1.00 78.33 ? 301 NAG B C8 1 HETATM 3421 N N2 . NAG I 3 . ? -9.418 -46.970 9.739 1.00 83.83 ? 301 NAG B N2 1 HETATM 3422 O O3 . NAG I 3 . ? -10.550 -49.706 9.403 1.00 100.04 ? 301 NAG B O3 1 HETATM 3423 O O4 . NAG I 3 . ? -9.581 -50.901 7.010 1.00 98.29 ? 301 NAG B O4 1 HETATM 3424 O O5 . NAG I 3 . ? -9.781 -47.410 6.113 1.00 90.03 ? 301 NAG B O5 1 HETATM 3425 O O6 . NAG I 3 . ? -10.794 -49.734 4.434 1.00 99.27 ? 301 NAG B O6 1 HETATM 3426 O O7 . NAG I 3 . ? -10.604 -45.056 9.743 1.00 89.37 ? 301 NAG B O7 1 HETATM 3427 C C1 . NAG J 3 . ? -10.672 -51.816 7.173 1.00 107.71 ? 302 NAG B C1 1 HETATM 3428 C C2 . NAG J 3 . ? -10.335 -53.012 6.296 1.00 111.52 ? 302 NAG B C2 1 HETATM 3429 C C3 . NAG J 3 . ? -11.242 -54.214 6.555 1.00 118.01 ? 302 NAG B C3 1 HETATM 3430 C C4 . NAG J 3 . ? -11.494 -54.423 8.041 1.00 122.35 ? 302 NAG B C4 1 HETATM 3431 C C5 . NAG J 3 . ? -11.919 -53.099 8.664 1.00 121.49 ? 302 NAG B C5 1 HETATM 3432 C C6 . NAG J 3 . ? -12.293 -53.244 10.138 1.00 124.64 ? 302 NAG B C6 1 HETATM 3433 C C7 . NAG J 3 . ? -11.223 -52.601 3.947 1.00 116.42 ? 302 NAG B C7 1 HETATM 3434 C C8 . NAG J 3 . ? -12.584 -53.219 4.115 1.00 117.59 ? 302 NAG B C8 1 HETATM 3435 N N2 . NAG J 3 . ? -10.291 -52.538 4.910 1.00 113.02 ? 302 NAG B N2 1 HETATM 3436 O O3 . NAG J 3 . ? -10.690 -55.376 5.974 1.00 117.32 ? 302 NAG B O3 1 HETATM 3437 O O4 . NAG J 3 . ? -12.523 -55.372 8.204 1.00 128.01 ? 302 NAG B O4 1 HETATM 3438 O O5 . NAG J 3 . ? -10.851 -52.188 8.520 1.00 111.59 ? 302 NAG B O5 1 HETATM 3439 O O6 . NAG J 3 . ? -11.253 -53.885 10.842 1.00 123.91 ? 302 NAG B O6 1 HETATM 3440 O O7 . NAG J 3 . ? -10.942 -52.114 2.859 1.00 115.02 ? 302 NAG B O7 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 . PRO A 13 ? 0.6748 0.8235 0.4319 -0.1154 -0.1750 0.1823 11 PRO A N 2 C CA . PRO A 13 ? 0.6889 0.7693 0.4442 -0.0940 -0.1448 0.1777 11 PRO A CA 3 C C . PRO A 13 ? 0.7007 0.7224 0.4396 -0.1211 -0.1195 0.1495 11 PRO A C 4 O O . PRO A 13 ? 0.6875 0.7237 0.4519 -0.1404 -0.1156 0.1300 11 PRO A O 5 C CB . PRO A 13 ? 0.6370 0.7502 0.4531 -0.0656 -0.1388 0.1784 11 PRO A CB 6 C CG . PRO A 13 ? 0.5985 0.7977 0.4441 -0.0569 -0.1670 0.1974 11 PRO A CG 7 C CD . PRO A 13 ? 0.6235 0.8500 0.4424 -0.0981 -0.1885 0.1914 11 PRO A CD 8 N N . GLN A 14 ? 0.7408 0.6975 0.4388 -0.1208 -0.1010 0.1502 12 GLN A N 9 C CA . GLN A 14 ? 0.7367 0.6410 0.4210 -0.1438 -0.0746 0.1267 12 GLN A CA 10 C C . GLN A 14 ? 0.7111 0.5759 0.4191 -0.1288 -0.0484 0.1197 12 GLN A C 11 O O . GLN A 14 ? 0.7493 0.5973 0.4563 -0.1040 -0.0447 0.1345 12 GLN A O 12 C CB . GLN A 14 ? 0.8107 0.6708 0.4265 -0.1620 -0.0686 0.1297 12 GLN A CB 13 C CG . GLN A 14 ? 0.8856 0.7807 0.4614 -0.1769 -0.0981 0.1406 12 GLN A CG 14 C CD . GLN A 14 ? 0.9618 0.8758 0.5408 -0.2106 -0.1022 0.1173 12 GLN A CD 15 O OE1 . GLN A 14 ? 1.0404 0.9087 0.5845 -0.2355 -0.0818 0.0981 12 GLN A OE1 16 N NE2 . GLN A 14 ? 0.9670 0.9451 0.5878 -0.2117 -0.1249 0.1187 12 GLN A NE2 17 N N . LEU A 15 ? 0.6487 0.4985 0.3780 -0.1448 -0.0298 0.0972 13 LEU A N 18 C CA . LEU A 15 ? 0.6157 0.4291 0.3630 -0.1412 -0.0044 0.0867 13 LEU A CA 19 C C . LEU A 15 ? 0.6087 0.3967 0.3544 -0.1643 0.0175 0.0690 13 LEU A C 20 O O . LEU A 15 ? 0.5883 0.3925 0.3393 -0.1784 0.0148 0.0596 13 LEU A O 21 C CB . LEU A 15 ? 0.5624 0.4059 0.3613 -0.1286 -0.0071 0.0783 13 LEU A CB 22 C CG . LEU A 15 ? 0.5754 0.4461 0.3856 -0.1021 -0.0222 0.0926 13 LEU A CG 23 C CD1 . LEU A 15 ? 0.5442 0.4531 0.3998 -0.0973 -0.0251 0.0799 13 LEU A CD1 24 C CD2 . LEU A 15 ? 0.5173 0.3412 0.3070 -0.0820 -0.0092 0.1047 13 LEU A CD2 25 N N . ARG A 16 ? 0.6379 0.3831 0.3763 -0.1675 0.0424 0.0655 14 ARG A N 26 C CA . ARG A 16 ? 0.6414 0.3654 0.3862 -0.1861 0.0687 0.0502 14 ARG A CA 27 C C . ARG A 16 ? 0.5878 0.3171 0.3829 -0.1864 0.0825 0.0378 14 ARG A C 28 O O . ARG A 16 ? 0.6060 0.3109 0.3974 -0.1815 0.0902 0.0410 14 ARG A O 29 C CB . ARG A 16 ? 0.7370 0.4072 0.4247 -0.1955 0.0895 0.0576 14 ARG A CB 30 C CG . ARG A 16 ? 0.9013 0.5604 0.5365 -0.2089 0.0876 0.0588 14 ARG A CG 31 C CD . ARG A 16 ? 1.0696 0.6733 0.6397 -0.2178 0.1092 0.0681 14 ARG A CD 32 N NE . ARG A 16 ? 1.2566 0.8554 0.7699 -0.2082 0.0847 0.0926 14 ARG A NE 33 C CZ . ARG A 16 ? 1.3793 0.9642 0.8841 -0.1878 0.0782 0.1145 14 ARG A CZ 34 N NH1 . ARG A 16 ? 1.3795 0.9468 0.9234 -0.1797 0.0961 0.1110 14 ARG A NH1 35 N NH2 . ARG A 16 ? 1.4601 1.0485 0.9163 -0.1758 0.0538 0.1406 14 ARG A NH2 36 N N . VAL A 17 ? 0.5155 0.2755 0.3562 -0.1929 0.0860 0.0243 15 VAL A N 37 C CA . VAL A 17 ? 0.4765 0.2521 0.3665 -0.1975 0.0962 0.0121 15 VAL A CA 38 C C . VAL A 17 ? 0.4607 0.2450 0.3821 -0.2092 0.1177 0.0023 15 VAL A C 39 O O . VAL A 17 ? 0.4621 0.2481 0.3783 -0.2093 0.1212 0.0025 15 VAL A O 40 C CB . VAL A 17 ? 0.4344 0.2569 0.3627 -0.1880 0.0733 0.0080 15 VAL A CB 41 C CG1 . VAL A 17 ? 0.4648 0.2738 0.3722 -0.1759 0.0630 0.0136 15 VAL A CG1 42 C CG2 . VAL A 17 ? 0.3743 0.2306 0.3119 -0.1819 0.0559 0.0121 15 VAL A CG2 43 N N . HIS A 18 ? 0.4699 0.2588 0.4254 -0.2198 0.1343 -0.0068 16 HIS A N 44 C CA . HIS A 18 ? 0.4340 0.2448 0.4349 -0.2283 0.1556 -0.0148 16 HIS A CA 45 C C . HIS A 18 ? 0.3752 0.2486 0.4359 -0.2208 0.1363 -0.0179 16 HIS A C 46 O O . HIS A 18 ? 0.3391 0.2372 0.4107 -0.2181 0.1133 -0.0198 16 HIS A O 47 C CB . HIS A 18 ? 0.4374 0.2345 0.4541 -0.2468 0.1821 -0.0225 16 HIS A CB 48 C CG . HIS A 18 ? 0.5336 0.2651 0.4893 -0.2551 0.2063 -0.0164 16 HIS A CG 49 N ND1 . HIS A 18 ? 0.6513 0.3592 0.5909 -0.2624 0.2375 -0.0166 16 HIS A ND1 50 C CD2 . HIS A 18 ? 0.5990 0.2811 0.5035 -0.2560 0.2063 -0.0083 16 HIS A CD2 51 C CE1 . HIS A 18 ? 0.7079 0.3562 0.5842 -0.2697 0.2534 -0.0083 16 HIS A CE1 52 N NE2 . HIS A 18 ? 0.6612 0.2927 0.5170 -0.2646 0.2343 -0.0013 16 HIS A NE2 53 N N . VAL A 19 ? 0.3661 0.2626 0.4624 -0.2159 0.1475 -0.0174 17 VAL A N 54 C CA . VAL A 19 ? 0.3261 0.2825 0.4789 -0.2055 0.1297 -0.0148 17 VAL A CA 55 C C . VAL A 19 ? 0.3293 0.3299 0.5252 -0.2172 0.1201 -0.0229 17 VAL A C 56 O O . VAL A 19 ? 0.3457 0.3449 0.5603 -0.2343 0.1405 -0.0315 17 VAL A O 57 C CB . VAL A 19 ? 0.3345 0.3086 0.5295 -0.1956 0.1499 -0.0111 17 VAL A CB 58 C CG1 . VAL A 19 ? 0.2786 0.3236 0.5402 -0.1847 0.1306 -0.0046 17 VAL A CG1 59 C CG2 . VAL A 19 ? 0.3001 0.2315 0.4528 -0.1856 0.1565 -0.0060 17 VAL A CG2 60 N N . GLY A 20 ? 0.3205 0.3596 0.5282 -0.2111 0.0898 -0.0210 18 GLY A N 61 C CA . GLY A 20 ? 0.3089 0.3950 0.5512 -0.2248 0.0751 -0.0310 18 GLY A CA 62 C C . GLY A 20 ? 0.3308 0.3872 0.5284 -0.2331 0.0635 -0.0408 18 GLY A C 63 O O . GLY A 20 ? 0.3588 0.4489 0.5659 -0.2396 0.0434 -0.0489 18 GLY A O 64 N N . GLU A 21 ? 0.3511 0.3435 0.4971 -0.2315 0.0769 -0.0393 19 GLU A N 65 C CA . GLU A 21 ? 0.3817 0.3374 0.4875 -0.2351 0.0728 -0.0466 19 GLU A CA 66 C C . GLU A 21 ? 0.3449 0.3064 0.4252 -0.2155 0.0501 -0.0393 19 GLU A C 67 O O . GLU A 21 ? 0.3239 0.3181 0.4164 -0.2030 0.0361 -0.0291 19 GLU A O 68 C CB . GLU A 21 ? 0.4365 0.3225 0.4993 -0.2388 0.0971 -0.0434 19 GLU A CB 69 C CG . GLU A 21 ? 0.5703 0.4447 0.6546 -0.2627 0.1251 -0.0521 19 GLU A CG 70 C CD . GLU A 21 ? 0.7551 0.5534 0.7880 -0.2673 0.1508 -0.0462 19 GLU A CD 71 O OE1 . GLU A 21 ? 0.8791 0.6446 0.8663 -0.2496 0.1489 -0.0305 19 GLU A OE1 72 O OE2 . GLU A 21 ? 0.8466 0.6189 0.8833 -0.2903 0.1725 -0.0562 19 GLU A OE2 73 N N . SER A 22 ? 0.3682 0.2941 0.4136 -0.2125 0.0504 -0.0437 20 SER A N 74 C CA . SER A 22 ? 0.3720 0.3071 0.3976 -0.1944 0.0329 -0.0389 20 SER A CA 75 C C . SER A 22 ? 0.3987 0.2924 0.3846 -0.1765 0.0367 -0.0248 20 SER A C 76 O O . SER A 22 ? 0.4516 0.2976 0.4138 -0.1780 0.0530 -0.0200 20 SER A O 77 C CB . SER A 22 ? 0.3925 0.3312 0.4153 -0.2024 0.0294 -0.0576 20 SER A CB 78 O OG . SER A 22 ? 0.3989 0.3910 0.4567 -0.2189 0.0176 -0.0687 20 SER A OG 79 N N . VAL A 23 ? 0.3928 0.3092 0.3718 -0.1595 0.0210 -0.0162 21 VAL A N 80 C CA . VAL A 23 ? 0.4190 0.3145 0.3689 -0.1410 0.0191 0.0000 21 VAL A CA 81 C C . VAL A 23 ? 0.4172 0.3378 0.3669 -0.1234 0.0081 0.0023 21 VAL A C 82 O O . VAL A 23 ? 0.4004 0.3637 0.3683 -0.1253 -0.0032 -0.0017 21 VAL A O 83 C CB . VAL A 23 ? 0.3870 0.2927 0.3313 -0.1418 0.0124 0.0141 21 VAL A CB 84 C CG1 . VAL A 23 ? 0.3240 0.2758 0.2950 -0.1461 0.0001 0.0131 21 VAL A CG1 85 C CG2 . VAL A 23 ? 0.4263 0.3281 0.3451 -0.1256 0.0036 0.0309 21 VAL A CG2 86 N N . LEU A 24 ? 0.4449 0.3380 0.3739 -0.1044 0.0136 0.0109 22 LEU A N 87 C CA . LEU A 24 ? 0.4449 0.3598 0.3765 -0.0833 0.0092 0.0137 22 LEU A CA 88 C C . LEU A 24 ? 0.4584 0.3964 0.3870 -0.0650 -0.0031 0.0376 22 LEU A C 89 O O . LEU A 24 ? 0.5156 0.4248 0.4257 -0.0496 0.0007 0.0529 22 LEU A O 90 C CB . LEU A 24 ? 0.4839 0.3504 0.3999 -0.0719 0.0289 0.0034 22 LEU A CB 91 C CG . LEU A 24 ? 0.4810 0.3661 0.4008 -0.0491 0.0318 0.0010 22 LEU A CG 92 C CD1 . LEU A 24 ? 0.5114 0.3400 0.4129 -0.0467 0.0561 -0.0196 22 LEU A CD1 93 C CD2 . LEU A 24 ? 0.4579 0.3624 0.3815 -0.0183 0.0254 0.0282 22 LEU A CD2 94 N N . MET A 25 ? 0.4173 0.4096 0.3640 -0.0681 -0.0183 0.0420 23 MET A N 95 C CA . MET A 25 ? 0.4163 0.4445 0.3662 -0.0581 -0.0330 0.0622 23 MET A CA 96 C C . MET A 25 ? 0.4269 0.4856 0.3921 -0.0317 -0.0318 0.0692 23 MET A C 97 O O . MET A 25 ? 0.4106 0.5062 0.3939 -0.0320 -0.0317 0.0625 23 MET A O 98 C CB . MET A 25 ? 0.3867 0.4517 0.3478 -0.0794 -0.0462 0.0627 23 MET A CB 99 C CG . MET A 25 ? 0.4322 0.4651 0.3800 -0.1007 -0.0428 0.0569 23 MET A CG 100 S SD . MET A 25 ? 0.5260 0.5847 0.4854 -0.1229 -0.0505 0.0557 23 MET A SD 101 C CE . MET A 25 ? 0.5576 0.6298 0.5412 -0.1239 -0.0454 0.0436 23 MET A CE 102 N N . GLY A 26 ? 0.4762 0.5184 0.4332 -0.0069 -0.0288 0.0849 24 GLY A N 103 C CA . GLY A 26 ? 0.5031 0.5701 0.4785 0.0259 -0.0227 0.0944 24 GLY A CA 104 C C . GLY A 26 ? 0.4834 0.6309 0.4908 0.0275 -0.0386 0.1061 24 GLY A C 105 O O . GLY A 26 ? 0.4567 0.6372 0.4662 0.0069 -0.0586 0.1144 24 GLY A O 106 N N . CYS A 27 ? 0.5033 0.6795 0.5340 0.0496 -0.0264 0.1044 25 CYS A N 107 C CA . CYS A 27 ? 0.4855 0.7441 0.5539 0.0550 -0.0363 0.1176 25 CYS A CA 108 C C . CYS A 27 ? 0.4968 0.7732 0.5898 0.0951 -0.0159 0.1224 25 CYS A C 109 O O . CYS A 27 ? 0.4971 0.7806 0.5960 0.0971 0.0028 0.1061 25 CYS A O 110 C CB . CYS A 27 ? 0.4527 0.7421 0.5273 0.0227 -0.0402 0.1039 25 CYS A CB 111 S SG . CYS A 27 ? 0.4941 0.8819 0.6111 0.0126 -0.0559 0.1212 25 CYS A SG 112 N N . VAL A 28 ? 0.5332 0.8161 0.6382 0.1286 -0.0184 0.1464 26 VAL A N 113 C CA . VAL A 28 ? 0.5692 0.8579 0.6986 0.1754 0.0057 0.1542 26 VAL A CA 114 C C . VAL A 28 ? 0.5663 0.9493 0.7490 0.2015 -0.0087 0.1857 26 VAL A C 115 O O . VAL A 28 ? 0.5743 0.9714 0.7622 0.2194 -0.0275 0.2141 26 VAL A O 116 C CB . VAL A 28 ? 0.6222 0.8222 0.7210 0.2037 0.0238 0.1577 26 VAL A CB 117 C CG1 . VAL A 28 ? 0.6650 0.8588 0.7871 0.2548 0.0554 0.1634 26 VAL A CG1 118 C CG2 . VAL A 28 ? 0.6490 0.7644 0.7007 0.1729 0.0366 0.1260 26 VAL A CG2 119 N N . VAL A 29 ? 0.5475 0.9983 0.7698 0.2027 0.0009 0.1811 27 VAL A N 120 C CA . VAL A 29 ? 0.5401 1.0956 0.8251 0.2249 -0.0092 0.2084 27 VAL A CA 121 C C . VAL A 29 ? 0.6133 1.1585 0.9224 0.2877 0.0146 0.2265 27 VAL A C 122 O O . VAL A 29 ? 0.6465 1.1735 0.9649 0.3134 0.0522 0.2123 27 VAL A O 123 C CB . VAL A 29 ? 0.5041 1.1298 0.8235 0.2062 0.0015 0.1966 27 VAL A CB 124 C CG1 . VAL A 29 ? 0.4816 1.2243 0.8751 0.2287 -0.0063 0.2249 27 VAL A CG1 125 C CG2 . VAL A 29 ? 0.4236 1.0490 0.7166 0.1463 -0.0185 0.1809 27 VAL A CG2 126 N N . GLN A 30 ? 0.6524 1.2052 0.9676 0.3135 -0.0058 0.2588 28 GLN A N 127 C CA . GLN A 30 ? 0.7353 1.2602 1.0664 0.3778 0.0175 0.2809 28 GLN A CA 128 C C . GLN A 30 ? 0.7474 1.3861 1.1609 0.4205 0.0202 0.3091 28 GLN A C 129 O O . GLN A 30 ? 0.7524 1.4789 1.2053 0.4310 -0.0145 0.3451 28 GLN A O 130 C CB . GLN A 30 ? 0.7829 1.2561 1.0783 0.3922 -0.0028 0.3080 28 GLN A CB 131 C CG . GLN A 30 ? 0.8841 1.2767 1.1708 0.4533 0.0323 0.3225 28 GLN A CG 132 C CD . GLN A 30 ? 0.9832 1.4232 1.3003 0.5036 0.0112 0.3765 28 GLN A CD 133 O OE1 . GLN A 30 ? 1.0078 1.5625 1.3656 0.4959 -0.0291 0.4021 28 GLN A OE1 134 N NE2 . GLN A 30 ? 1.0955 1.4474 1.3921 0.5546 0.0383 0.3949 28 GLN A NE2 135 N N . ARG A 31 ? 0.7596 1.3985 1.1982 0.4447 0.0628 0.2920 29 ARG A N 136 C CA . ARG A 31 ? 0.7688 1.5060 1.2899 0.4951 0.0781 0.3172 29 ARG A CA 137 C C . ARG A 31 ? 0.8555 1.5190 1.3757 0.5657 0.1152 0.3319 29 ARG A C 138 O O . ARG A 31 ? 0.9056 1.4576 1.3655 0.5712 0.1182 0.3306 29 ARG A O 139 C CB . ARG A 31 ? 0.7400 1.5250 1.2892 0.4790 0.1078 0.2898 29 ARG A CB 140 C CG . ARG A 31 ? 0.6480 1.5045 1.2017 0.4116 0.0760 0.2787 29 ARG A CG 141 C CD . ARG A 31 ? 0.6243 1.6191 1.2498 0.4085 0.0358 0.3151 29 ARG A CD 142 N NE . ARG A 31 ? 0.5535 1.6097 1.1834 0.3423 0.0122 0.3021 29 ARG A NE 143 C CZ . ARG A 31 ? 0.5751 1.6065 1.1588 0.2891 -0.0252 0.2955 29 ARG A CZ 144 N NH1 . ARG A 31 ? 0.6286 1.5811 1.1582 0.2923 -0.0444 0.3004 29 ARG A NH1 145 N NH2 . ARG A 31 ? 0.5273 1.6080 1.1169 0.2323 -0.0398 0.2838 29 ARG A NH2 146 N N . THR A 32 ? 0.8834 1.6064 1.4714 0.6196 0.1471 0.3459 30 THR A N 147 C CA . THR A 32 ? 0.9744 1.6274 1.5683 0.6936 0.1891 0.3615 30 THR A CA 148 C C . THR A 32 ? 1.0148 1.5834 1.5802 0.7023 0.2528 0.3168 30 THR A C 149 O O . THR A 32 ? 1.0849 1.6263 1.6775 0.7661 0.3002 0.3242 30 THR A O 150 C CB . THR A 32 ? 0.9974 1.7728 1.6913 0.7601 0.1847 0.4132 30 THR A CB 151 O OG1 . THR A 32 ? 0.9642 1.8625 1.7305 0.7530 0.1961 0.4055 30 THR A OG1 152 C CG2 . THR A 32 ? 0.9651 1.8174 1.6767 0.7528 0.1193 0.4589 30 THR A CG2 153 N N . GLU A 33 ? 0.9774 1.5030 1.4850 0.6381 0.2539 0.2707 31 GLU A N 154 C CA . GLU A 33 ? 1.0173 1.4663 1.4854 0.6351 0.3093 0.2239 31 GLU A CA 155 C C . GLU A 33 ? 0.9715 1.3668 1.3653 0.5613 0.3006 0.1775 31 GLU A C 156 O O . GLU A 33 ? 0.8954 1.3243 1.2761 0.5095 0.2539 0.1796 31 GLU A O 157 C CB . GLU A 33 ? 1.0167 1.5656 1.5562 0.6650 0.3422 0.2263 31 GLU A CB 158 C CG . GLU A 33 ? 0.9231 1.6177 1.5173 0.6246 0.3037 0.2389 31 GLU A CG 159 C CD . GLU A 33 ? 0.9564 1.7688 1.6407 0.6628 0.3338 0.2537 31 GLU A CD 160 O OE1 . GLU A 33 ? 1.0198 1.7987 1.7227 0.7230 0.3884 0.2517 31 GLU A OE1 161 O OE2 . GLU A 33 ? 0.9127 1.8509 1.6508 0.6315 0.3058 0.2668 31 GLU A OE2 162 N N . GLU A 34 ? 1.0279 1.3375 1.3725 0.5600 0.3485 0.1358 32 GLU A N 163 C CA . GLU A 34 ? 1.0067 1.2714 1.2825 0.4962 0.3465 0.0907 32 GLU A CA 164 C C . GLU A 34 ? 0.9283 1.3030 1.2350 0.4650 0.3354 0.0881 32 GLU A C 165 O O . GLU A 34 ? 0.9397 1.3711 1.2869 0.4924 0.3694 0.0885 32 GLU A O 166 C CB . GLU A 34 ? 1.1059 1.2565 1.3191 0.5035 0.4024 0.0458 32 GLU A CB 167 C CG . GLU A 34 ? 1.2005 1.2183 1.3644 0.5179 0.4170 0.0380 32 GLU A CG 168 C CD . GLU A 34 ? 1.1988 1.1711 1.3125 0.4612 0.3746 0.0289 32 GLU A CD 169 O OE1 . GLU A 34 ? 1.1279 1.1271 1.2142 0.4049 0.3512 0.0062 32 GLU A OE1 170 O OE2 . GLU A 34 ? 1.2705 1.1796 1.3727 0.4750 0.3666 0.0466 32 GLU A OE2 171 N N . LYS A 35 ? 0.8404 1.2406 1.1268 0.4076 0.2911 0.0856 33 LYS A N 172 C CA . LYS A 35 ? 0.7747 1.2664 1.0816 0.3713 0.2794 0.0841 33 LYS A CA 173 C C . LYS A 35 ? 0.7301 1.1798 0.9700 0.3099 0.2595 0.0565 33 LYS A C 174 O O . LYS A 35 ? 0.7155 1.1229 0.9260 0.2835 0.2262 0.0571 33 LYS A O 175 C CB . LYS A 35 ? 0.7115 1.3174 1.0911 0.3694 0.2396 0.1245 33 LYS A CB 176 C CG . LYS A 35 ? 0.7540 1.4427 1.2174 0.4269 0.2577 0.1552 33 LYS A CG 177 C CD . LYS A 35 ? 0.7181 1.5293 1.2498 0.4129 0.2130 0.1914 33 LYS A CD 178 C CE . LYS A 35 ? 0.7506 1.6523 1.3721 0.4729 0.2226 0.2277 33 LYS A CE 179 N NZ . LYS A 35 ? 0.7049 1.7355 1.3929 0.4526 0.1753 0.2610 33 LYS A NZ 180 N N . HIS A 36 ? 0.7189 1.1840 0.9359 0.2889 0.2812 0.0346 34 HIS A N 181 C CA . HIS A 36 ? 0.6868 1.1172 0.8402 0.2354 0.2642 0.0111 34 HIS A CA 182 C C . HIS A 36 ? 0.5941 1.0914 0.7733 0.1986 0.2204 0.0343 34 HIS A C 183 O O . HIS A 36 ? 0.5746 1.1606 0.8064 0.1991 0.2189 0.0551 34 HIS A O 184 C CB . HIS A 36 ? 0.7291 1.1539 0.8414 0.2251 0.3009 -0.0170 34 HIS A CB 185 C CG . HIS A 36 ? 0.8220 1.1708 0.8985 0.2563 0.3487 -0.0465 34 HIS A CG 186 N ND1 . HIS A 36 ? 0.8926 1.1619 0.9587 0.2816 0.3548 -0.0519 34 HIS A ND1 187 C CD2 . HIS A 36 ? 0.9333 1.2659 0.9766 0.2650 0.3961 -0.0735 34 HIS A CD2 188 C CE1 . HIS A 36 ? 0.9904 1.1942 1.0202 0.3045 0.4046 -0.0819 34 HIS A CE1 189 N NE2 . HIS A 36 ? 1.0235 1.2650 1.0378 0.2950 0.4306 -0.0968 34 HIS A NE2 190 N N . VAL A 37 ? 0.5522 1.0045 0.6952 0.1661 0.1875 0.0296 35 VAL A N 191 C CA . VAL A 37 ? 0.4845 0.9807 0.6406 0.1288 0.1494 0.0470 35 VAL A CA 192 C C . VAL A 37 ? 0.5012 1.0312 0.6400 0.0991 0.1568 0.0410 35 VAL A C 193 O O . VAL A 37 ? 0.5489 1.0365 0.6334 0.0870 0.1711 0.0173 35 VAL A O 194 C CB . VAL A 37 ? 0.4516 0.8856 0.5702 0.1029 0.1191 0.0407 35 VAL A CB 195 C CG1 . VAL A 37 ? 0.3738 0.8417 0.4958 0.0633 0.0887 0.0530 35 VAL A CG1 196 C CG2 . VAL A 37 ? 0.4172 0.8230 0.5519 0.1270 0.1083 0.0533 35 VAL A CG2 197 N N . ASP A 38 ? 0.4746 1.0812 0.6572 0.0852 0.1464 0.0634 36 ASP A N 198 C CA . ASP A 38 ? 0.4717 1.1115 0.6404 0.0557 0.1543 0.0640 36 ASP A CA 199 C C . ASP A 38 ? 0.4442 1.0604 0.5840 0.0147 0.1213 0.0689 36 ASP A C 200 O O . ASP A 38 ? 0.4537 1.0600 0.5546 -0.0091 0.1248 0.0649 36 ASP A O 201 C CB . ASP A 38 ? 0.4554 1.1900 0.6894 0.0592 0.1658 0.0852 36 ASP A CB 202 C CG . ASP A 38 ? 0.4673 1.2337 0.6865 0.0273 0.1787 0.0886 36 ASP A CG 203 O OD1 . ASP A 38 ? 0.4516 1.2124 0.6568 -0.0096 0.1540 0.0984 36 ASP A OD1 204 O OD2 . ASP A 38 ? 0.5049 1.2986 0.7250 0.0399 0.2164 0.0826 36 ASP A OD2 205 N N . ARG A 39 ? 0.4132 1.0174 0.5690 0.0088 0.0909 0.0786 37 ARG A N 206 C CA . ARG A 39 ? 0.4009 0.9854 0.5382 -0.0269 0.0632 0.0852 37 ARG A CA 207 C C . ARG A 39 ? 0.3653 0.9164 0.5053 -0.0285 0.0361 0.0879 37 ARG A C 208 O O . ARG A 39 ? 0.3883 0.9601 0.5608 -0.0102 0.0303 0.0965 37 ARG A O 209 C CB . ARG A 39 ? 0.3904 1.0357 0.5608 -0.0523 0.0593 0.1048 37 ARG A CB 210 C CG . ARG A 39 ? 0.4187 1.0787 0.5683 -0.0699 0.0783 0.1068 37 ARG A CG 211 C CD . ARG A 39 ? 0.3912 1.1177 0.5847 -0.0920 0.0811 0.1258 37 ARG A CD 212 N NE . ARG A 39 ? 0.4310 1.1909 0.6192 -0.0964 0.1122 0.1285 37 ARG A NE 213 C CZ . ARG A 39 ? 0.4883 1.2550 0.6625 -0.1288 0.1179 0.1411 37 ARG A CZ 214 N NH1 . ARG A 39 ? 0.5050 1.2448 0.6718 -0.1587 0.0955 0.1514 37 ARG A NH1 215 N NH2 . ARG A 39 ? 0.5721 1.3689 0.7382 -0.1307 0.1498 0.1439 37 ARG A NH2 216 N N . VAL A 40 ? 0.3247 0.8289 0.4317 -0.0503 0.0200 0.0833 38 VAL A N 217 C CA . VAL A 40 ? 0.3160 0.7935 0.4249 -0.0605 -0.0039 0.0880 38 VAL A CA 218 C C . VAL A 40 ? 0.3014 0.7585 0.3928 -0.0917 -0.0171 0.0925 38 VAL A C 219 O O . VAL A 40 ? 0.3002 0.7339 0.3637 -0.0987 -0.0136 0.0870 38 VAL A O 220 C CB . VAL A 40 ? 0.3455 0.7645 0.4319 -0.0446 -0.0059 0.0739 38 VAL A CB 221 C CG1 . VAL A 40 ? 0.3802 0.7785 0.4699 -0.0531 -0.0264 0.0812 38 VAL A CG1 222 C CG2 . VAL A 40 ? 0.3443 0.7628 0.4387 -0.0102 0.0132 0.0675 38 VAL A CG2 223 N N . ASP A 41 ? 0.2813 0.7469 0.3879 -0.1098 -0.0318 0.1030 39 ASP A N 224 C CA . ASP A 41 ? 0.2869 0.7170 0.3759 -0.1350 -0.0416 0.1057 39 ASP A CA 225 C C . ASP A 41 ? 0.2882 0.6787 0.3688 -0.1347 -0.0549 0.1005 39 ASP A C 226 O O . ASP A 41 ? 0.2984 0.7052 0.3920 -0.1330 -0.0639 0.1040 39 ASP A O 227 C CB . ASP A 41 ? 0.2920 0.7503 0.3958 -0.1636 -0.0429 0.1184 39 ASP A CB 228 C CG . ASP A 41 ? 0.3596 0.8548 0.4695 -0.1691 -0.0264 0.1263 39 ASP A CG 229 O OD1 . ASP A 41 ? 0.3729 0.8726 0.4720 -0.1490 -0.0143 0.1207 39 ASP A OD1 230 O OD2 . ASP A 41 ? 0.3368 0.8540 0.4590 -0.1960 -0.0235 0.1370 39 ASP A OD2 231 N N . TRP A 42 ? 0.2728 0.6155 0.3320 -0.1365 -0.0563 0.0935 40 TRP A N 232 C CA . TRP A 42 ? 0.2694 0.5722 0.3191 -0.1411 -0.0644 0.0891 40 TRP A CA 233 C C . TRP A 42 ? 0.2862 0.5640 0.3286 -0.1641 -0.0656 0.0937 40 TRP A C 234 O O . TRP A 42 ? 0.2750 0.5347 0.3112 -0.1651 -0.0612 0.0955 40 TRP A O 235 C CB . TRP A 42 ? 0.2759 0.5431 0.3128 -0.1265 -0.0614 0.0768 40 TRP A CB 236 C CG . TRP A 42 ? 0.2557 0.5224 0.2932 -0.1053 -0.0579 0.0708 40 TRP A CG 237 C CD1 . TRP A 42 ? 0.2656 0.5423 0.3025 -0.0878 -0.0474 0.0634 40 TRP A CD1 238 C CD2 . TRP A 42 ? 0.1654 0.4130 0.1989 -0.0979 -0.0621 0.0724 40 TRP A CD2 239 N NE1 . TRP A 42 ? 0.2140 0.4748 0.2503 -0.0680 -0.0429 0.0608 40 TRP A NE1 240 C CE2 . TRP A 42 ? 0.1962 0.4411 0.2305 -0.0732 -0.0533 0.0686 40 TRP A CE2 241 C CE3 . TRP A 42 ? 0.2064 0.4354 0.2307 -0.1100 -0.0708 0.0771 40 TRP A CE3 242 C CZ2 . TRP A 42 ? 0.2781 0.5026 0.3069 -0.0577 -0.0540 0.0738 40 TRP A CZ2 243 C CZ3 . TRP A 42 ? 0.2622 0.4753 0.2768 -0.0971 -0.0734 0.0810 40 TRP A CZ3 244 C CH2 . TRP A 42 ? 0.2757 0.4866 0.2938 -0.0700 -0.0656 0.0814 40 TRP A CH2 245 N N . LEU A 43 ? 0.3154 0.5914 0.3568 -0.1822 -0.0712 0.0961 41 LEU A N 246 C CA . LEU A 43 ? 0.3470 0.5865 0.3763 -0.2054 -0.0677 0.0970 41 LEU A CA 247 C C . LEU A 43 ? 0.3662 0.5602 0.3775 -0.2075 -0.0685 0.0877 41 LEU A C 248 O O . LEU A 43 ? 0.3978 0.5957 0.4035 -0.1994 -0.0757 0.0836 41 LEU A O 249 C CB . LEU A 43 ? 0.3515 0.6144 0.3852 -0.2338 -0.0699 0.1021 41 LEU A CB 250 C CG . LEU A 43 ? 0.3320 0.6447 0.3859 -0.2375 -0.0654 0.1125 41 LEU A CG 251 C CD1 . LEU A 43 ? 0.3373 0.7137 0.4144 -0.2372 -0.0757 0.1144 41 LEU A CD1 252 C CD2 . LEU A 43 ? 0.3477 0.6406 0.3953 -0.2677 -0.0551 0.1192 41 LEU A CD2 253 N N . PHE A 44 ? 0.3794 0.5283 0.3808 -0.2168 -0.0583 0.0862 42 PHE A N 254 C CA . PHE A 44 ? 0.3883 0.4901 0.3715 -0.2201 -0.0526 0.0763 42 PHE A CA 255 C C . PHE A 44 ? 0.4516 0.5159 0.4152 -0.2472 -0.0438 0.0724 42 PHE A C 256 O O . PHE A 44 ? 0.4665 0.5150 0.4338 -0.2561 -0.0336 0.0789 42 PHE A O 257 C CB . PHE A 44 ? 0.3796 0.4571 0.3727 -0.2015 -0.0429 0.0751 42 PHE A CB 258 C CG . PHE A 44 ? 0.3614 0.3892 0.3407 -0.2062 -0.0296 0.0661 42 PHE A CG 259 C CD1 . PHE A 44 ? 0.3622 0.3775 0.3268 -0.2040 -0.0299 0.0568 42 PHE A CD1 260 C CD2 . PHE A 44 ? 0.3520 0.3410 0.3302 -0.2121 -0.0132 0.0678 42 PHE A CD2 261 C CE1 . PHE A 44 ? 0.4126 0.3819 0.3607 -0.2098 -0.0137 0.0478 42 PHE A CE1 262 C CE2 . PHE A 44 ? 0.3545 0.2961 0.3196 -0.2151 0.0043 0.0579 42 PHE A CE2 263 C CZ . PHE A 44 ? 0.3980 0.3317 0.3474 -0.2153 0.0044 0.0470 42 PHE A CZ 264 N N . SER A 45 ? 0.4812 0.5257 0.4183 -0.2614 -0.0461 0.0618 43 SER A N 265 C CA . SER A 45 ? 0.5348 0.5353 0.4433 -0.2915 -0.0356 0.0522 43 SER A CA 266 C C . SER A 45 ? 0.5671 0.5209 0.4418 -0.2954 -0.0266 0.0383 43 SER A C 267 O O . SER A 45 ? 0.5495 0.5189 0.4114 -0.2889 -0.0384 0.0369 43 SER A O 268 C CB . SER A 45 ? 0.5454 0.5823 0.4467 -0.3220 -0.0508 0.0518 43 SER A CB 269 O OG . SER A 45 ? 0.6459 0.6505 0.5395 -0.3489 -0.0365 0.0493 43 SER A OG 270 N N . LYS A 46 ? 0.5928 0.4856 0.4530 -0.3034 -0.0021 0.0299 44 LYS A N 271 C CA . LYS A 46 ? 0.6123 0.4514 0.4358 -0.3108 0.0149 0.0141 44 LYS A CA 272 C C . LYS A 46 ? 0.6554 0.4906 0.4303 -0.3477 0.0033 0.0013 44 LYS A C 273 O O . LYS A 46 ? 0.6886 0.5383 0.4586 -0.3749 -0.0059 0.0000 44 LYS A O 274 C CB . LYS A 46 ? 0.6510 0.4249 0.4757 -0.3068 0.0488 0.0088 44 LYS A CB 275 C CG . LYS A 46 ? 0.5587 0.3429 0.4321 -0.2689 0.0583 0.0224 44 LYS A CG 276 C CD . LYS A 46 ? 0.6621 0.3845 0.5366 -0.2593 0.0941 0.0165 44 LYS A CD 277 C CE . LYS A 46 ? 0.8615 0.5500 0.7463 -0.2592 0.1101 0.0260 44 LYS A CE 278 N NZ . LYS A 46 ? 0.9765 0.5831 0.8417 -0.2612 0.1505 0.0141 44 LYS A NZ 279 N N . ASP A 47 ? 0.6805 0.4999 0.4188 -0.3502 0.0030 -0.0073 45 ASP A N 280 C CA . ASP A 47 ? 0.7435 0.5625 0.4273 -0.3846 -0.0114 -0.0185 45 ASP A CA 281 C C . ASP A 47 ? 0.8207 0.5939 0.4722 -0.4247 0.0029 -0.0372 45 ASP A C 282 O O . ASP A 47 ? 0.8575 0.5605 0.4987 -0.4252 0.0377 -0.0492 45 ASP A O 283 C CB . ASP A 47 ? 0.7859 0.5711 0.4251 -0.3803 -0.0021 -0.0258 45 ASP A CB 284 C CG . ASP A 47 ? 0.8847 0.6738 0.4591 -0.4145 -0.0210 -0.0347 45 ASP A CG 285 O OD1 . ASP A 47 ? 1.0172 0.7572 0.5419 -0.4504 -0.0067 -0.0569 45 ASP A OD1 286 O OD2 . ASP A 47 ? 0.9988 0.8377 0.5687 -0.4051 -0.0495 -0.0193 45 ASP A OD2 287 N N . LYS A 48 ? 0.8406 0.6564 0.4799 -0.4581 -0.0232 -0.0388 46 LYS A N 288 C CA . LYS A 48 ? 0.9201 0.6979 0.5181 -0.5084 -0.0153 -0.0603 46 LYS A CA 289 C C . LYS A 48 ? 0.9372 0.6776 0.5647 -0.5116 0.0099 -0.0599 46 LYS A C 290 O O . LYS A 48 ? 1.0046 0.6861 0.5970 -0.5499 0.0294 -0.0796 46 LYS A O 291 C CB . LYS A 48 ? 1.0050 0.7054 0.5294 -0.5295 0.0071 -0.0862 46 LYS A CB 292 C CG . LYS A 48 ? 1.1018 0.8050 0.5623 -0.5867 -0.0108 -0.1071 46 LYS A CG 293 C CD . LYS A 48 ? 1.2364 0.8485 0.6179 -0.6079 0.0201 -0.1363 46 LYS A CD 294 C CE . LYS A 48 ? 1.3273 0.9428 0.6327 -0.6696 -0.0008 -0.1601 46 LYS A CE 295 N NZ . LYS A 48 ? 1.3386 0.8761 0.5560 -0.6858 0.0246 -0.1863 46 LYS A NZ 296 N N . ASP A 49 ? 0.8766 0.6494 0.5645 -0.4725 0.0094 -0.0368 47 ASP A N 297 C CA . ASP A 49 ? 0.8758 0.6189 0.5932 -0.4679 0.0311 -0.0284 47 ASP A CA 298 C C . ASP A 49 ? 0.8223 0.6468 0.5876 -0.4636 0.0069 -0.0073 47 ASP A C 299 O O . ASP A 49 ? 0.7666 0.6557 0.5643 -0.4330 -0.0139 0.0078 47 ASP A O 300 C CB . ASP A 49 ? 0.8559 0.5555 0.5960 -0.4227 0.0580 -0.0197 47 ASP A CB 301 C CG . ASP A 49 ? 0.8182 0.5260 0.6061 -0.3978 0.0656 0.0035 47 ASP A CG 302 O OD1 . ASP A 49 ? 0.7533 0.4258 0.5353 -0.4194 0.0803 0.0048 47 ASP A OD1 303 O OD2 . ASP A 49 ? 0.8007 0.5458 0.6277 -0.3576 0.0583 0.0205 47 ASP A OD2 304 N N . ASP A 50 ? 0.8617 0.6781 0.6283 -0.4962 0.0134 -0.0079 48 ASP A N 305 C CA . ASP A 50 ? 0.8260 0.7208 0.6345 -0.5011 -0.0054 0.0098 48 ASP A CA 306 C C . ASP A 50 ? 0.7757 0.6745 0.6243 -0.4618 0.0061 0.0339 48 ASP A C 307 O O . ASP A 50 ? 0.7444 0.7136 0.6292 -0.4507 -0.0086 0.0505 48 ASP A O 308 C CB . ASP A 50 ? 0.8909 0.7812 0.6848 -0.5588 -0.0028 -0.0009 48 ASP A CB 309 C CG . ASP A 50 ? 0.9747 0.9158 0.7460 -0.5990 -0.0317 -0.0178 48 ASP A CG 310 O OD1 . ASP A 50 ? 0.9864 0.9804 0.7628 -0.5743 -0.0568 -0.0131 48 ASP A OD1 311 O OD2 . ASP A 50 ? 1.0111 0.9389 0.7582 -0.6556 -0.0297 -0.0348 48 ASP A OD2 312 N N . ALA A 51 ? 0.7799 0.6052 0.6210 -0.4398 0.0330 0.0364 49 ALA A N 313 C CA . ALA A 51 ? 0.7137 0.5486 0.5895 -0.3968 0.0387 0.0606 49 ALA A CA 314 C C . ALA A 51 ? 0.6262 0.5346 0.5283 -0.3651 0.0133 0.0668 49 ALA A C 315 O O . ALA A 51 ? 0.6079 0.5321 0.4987 -0.3646 0.0003 0.0542 49 ALA A O 316 C CB . ALA A 51 ? 0.7175 0.4751 0.5870 -0.3718 0.0669 0.0625 49 ALA A CB 317 N N . SER A 52 ? 0.5954 0.5434 0.5277 -0.3396 0.0084 0.0866 50 SER A N 318 C CA . SER A 52 ? 0.5423 0.5503 0.4970 -0.3096 -0.0108 0.0909 50 SER A CA 319 C C . SER A 52 ? 0.5163 0.5456 0.4935 -0.2816 -0.0094 0.1105 50 SER A C 320 O O . SER A 52 ? 0.5103 0.5303 0.4884 -0.2886 0.0008 0.1253 50 SER A O 321 C CB . SER A 52 ? 0.5252 0.6005 0.4878 -0.3240 -0.0316 0.0876 50 SER A CB 322 O OG . SER A 52 ? 0.5145 0.6289 0.4955 -0.3326 -0.0308 0.1009 50 SER A OG 323 N N . GLU A 53 ? 0.4791 0.5349 0.4696 -0.2523 -0.0194 0.1103 51 GLU A N 324 C CA . GLU A 53 ? 0.4469 0.5250 0.4521 -0.2279 -0.0212 0.1254 51 GLU A CA 325 C C . GLU A 53 ? 0.3854 0.5187 0.4011 -0.2119 -0.0361 0.1212 51 GLU A C 326 O O . GLU A 53 ? 0.3933 0.5347 0.4095 -0.2069 -0.0435 0.1078 51 GLU A O 327 C CB . GLU A 53 ? 0.4661 0.5069 0.4773 -0.2076 -0.0124 0.1307 51 GLU A CB 328 C CG . GLU A 53 ? 0.5389 0.5679 0.5545 -0.1972 -0.0134 0.1147 51 GLU A CG 329 C CD . GLU A 53 ? 0.6205 0.6114 0.6485 -0.1810 0.0015 0.1204 51 GLU A CD 330 O OE1 . GLU A 53 ? 0.6630 0.6647 0.7073 -0.1631 0.0010 0.1395 51 GLU A OE1 331 O OE2 . GLU A 53 ? 0.6784 0.6313 0.7001 -0.1849 0.0144 0.1071 51 GLU A OE2 332 N N . TYR A 54 ? 0.3709 0.5368 0.3903 -0.2048 -0.0375 0.1332 52 TYR A N 333 C CA . TYR A 54 ? 0.3371 0.5475 0.3612 -0.1885 -0.0463 0.1277 52 TYR A CA 334 C C . TYR A 54 ? 0.3075 0.5096 0.3340 -0.1696 -0.0522 0.1193 52 TYR A C 335 O O . TYR A 54 ? 0.3062 0.4922 0.3352 -0.1622 -0.0515 0.1275 52 TYR A O 336 C CB . TYR A 54 ? 0.3284 0.5706 0.3472 -0.1870 -0.0427 0.1413 52 TYR A CB 337 C CG . TYR A 54 ? 0.3933 0.6681 0.4184 -0.2034 -0.0371 0.1439 52 TYR A CG 338 C CD1 . TYR A 54 ? 0.3692 0.6294 0.3933 -0.2280 -0.0281 0.1548 52 TYR A CD1 339 C CD2 . TYR A 54 ? 0.4131 0.7336 0.4484 -0.1946 -0.0387 0.1351 52 TYR A CD2 340 C CE1 . TYR A 54 ? 0.4271 0.7257 0.4635 -0.2473 -0.0234 0.1565 52 TYR A CE1 341 C CE2 . TYR A 54 ? 0.3687 0.7304 0.4198 -0.2080 -0.0331 0.1391 52 TYR A CE2 342 C CZ . TYR A 54 ? 0.4353 0.7903 0.4888 -0.2365 -0.0268 0.1496 52 TYR A CZ 343 O OH . TYR A 54 ? 0.5015 0.9056 0.5767 -0.2554 -0.0215 0.1534 52 TYR A OH 344 N N . VAL A 55 ? 0.2883 0.5038 0.3165 -0.1620 -0.0571 0.1042 53 VAL A N 345 C CA . VAL A 55 ? 0.2855 0.4941 0.3157 -0.1496 -0.0609 0.0924 53 VAL A CA 346 C C . VAL A 55 ? 0.3033 0.5416 0.3264 -0.1404 -0.0640 0.0875 53 VAL A C 347 O O . VAL A 55 ? 0.3396 0.5838 0.3609 -0.1364 -0.0693 0.0868 53 VAL A O 348 C CB . VAL A 55 ? 0.2822 0.4751 0.3114 -0.1482 -0.0608 0.0789 53 VAL A CB 349 C CG1 . VAL A 55 ? 0.2293 0.4144 0.2592 -0.1388 -0.0614 0.0652 53 VAL A CG1 350 C CG2 . VAL A 55 ? 0.3306 0.4897 0.3573 -0.1597 -0.0568 0.0801 53 VAL A CG2 351 N N . LEU A 56 ? 0.2840 0.5437 0.3033 -0.1377 -0.0603 0.0838 54 LEU A N 352 C CA . LEU A 56 ? 0.2886 0.5717 0.2953 -0.1295 -0.0572 0.0764 54 LEU A CA 353 C C . LEU A 56 ? 0.3045 0.6181 0.3146 -0.1279 -0.0480 0.0816 54 LEU A C 354 O O . LEU A 56 ? 0.3196 0.6396 0.3456 -0.1274 -0.0471 0.0832 54 LEU A O 355 C CB . LEU A 56 ? 0.2827 0.5492 0.2845 -0.1206 -0.0561 0.0556 54 LEU A CB 356 C CG . LEU A 56 ? 0.3402 0.6183 0.3232 -0.1127 -0.0477 0.0408 54 LEU A CG 357 C CD1 . LEU A 56 ? 0.2303 0.4810 0.2028 -0.1124 -0.0474 0.0187 54 LEU A CD1 358 C CD2 . LEU A 56 ? 0.2677 0.5609 0.2582 -0.0999 -0.0349 0.0417 54 LEU A CD2 359 N N . PHE A 57 ? 0.2939 0.6316 0.2897 -0.1280 -0.0414 0.0855 55 PHE A N 360 C CA . PHE A 57 ? 0.2869 0.6593 0.2905 -0.1249 -0.0281 0.0887 55 PHE A CA 361 C C . PHE A 57 ? 0.3113 0.6980 0.2915 -0.1149 -0.0154 0.0772 55 PHE A C 362 O O . PHE A 57 ? 0.3324 0.7118 0.2829 -0.1187 -0.0190 0.0740 55 PHE A O 363 C CB . PHE A 57 ? 0.2900 0.6808 0.3028 -0.1423 -0.0249 0.1095 55 PHE A CB 364 C CG . PHE A 57 ? 0.2968 0.6890 0.2841 -0.1497 -0.0211 0.1225 55 PHE A CG 365 C CD1 . PHE A 57 ? 0.3515 0.7734 0.3225 -0.1477 -0.0059 0.1239 55 PHE A CD1 366 C CD2 . PHE A 57 ? 0.3522 0.7154 0.3306 -0.1570 -0.0306 0.1359 55 PHE A CD2 367 C CE1 . PHE A 57 ? 0.3920 0.8141 0.3317 -0.1549 -0.0028 0.1393 55 PHE A CE1 368 C CE2 . PHE A 57 ? 0.4127 0.7770 0.3657 -0.1606 -0.0285 0.1538 55 PHE A CE2 369 C CZ . PHE A 57 ? 0.4510 0.8447 0.3815 -0.1608 -0.0158 0.1561 55 PHE A CZ 370 N N . TYR A 58 ? 0.3142 0.7231 0.3081 -0.1015 -0.0002 0.0709 56 TYR A N 371 C CA . TYR A 58 ? 0.3403 0.7537 0.3120 -0.0879 0.0186 0.0540 56 TYR A CA 372 C C . TYR A 58 ? 0.3712 0.8311 0.3601 -0.0819 0.0403 0.0621 56 TYR A C 373 O O . TYR A 58 ? 0.3823 0.8717 0.4131 -0.0772 0.0411 0.0730 56 TYR A O 374 C CB . TYR A 58 ? 0.3227 0.7046 0.2962 -0.0694 0.0223 0.0341 56 TYR A CB 375 C CG . TYR A 58 ? 0.3890 0.7706 0.3470 -0.0509 0.0491 0.0160 56 TYR A CG 376 C CD1 . TYR A 58 ? 0.5372 0.8976 0.4472 -0.0571 0.0574 -0.0052 56 TYR A CD1 377 C CD2 . TYR A 58 ? 0.4072 0.8106 0.3978 -0.0267 0.0670 0.0197 56 TYR A CD2 378 C CE1 . TYR A 58 ? 0.6338 0.9849 0.5228 -0.0412 0.0871 -0.0260 56 TYR A CE1 379 C CE2 . TYR A 58 ? 0.4976 0.8954 0.4759 -0.0054 0.0972 0.0028 56 TYR A CE2 380 C CZ . TYR A 58 ? 0.6282 0.9949 0.5529 -0.0133 0.1094 -0.0218 56 TYR A CZ 381 O OH . TYR A 58 ? 0.7214 1.0747 0.6280 0.0071 0.1446 -0.0423 56 TYR A OH 382 N N . TYR A 59 ? 0.4003 0.8717 0.3565 -0.0843 0.0573 0.0577 57 TYR A N 383 C CA . TYR A 59 ? 0.4253 0.9434 0.3962 -0.0795 0.0841 0.0645 57 TYR A CA 384 C C . TYR A 59 ? 0.4802 0.9960 0.4014 -0.0765 0.1081 0.0495 57 TYR A C 385 O O . TYR A 59 ? 0.5170 1.0116 0.3882 -0.0908 0.0989 0.0468 57 TYR A O 386 C CB . TYR A 59 ? 0.4014 0.9521 0.3929 -0.1023 0.0799 0.0915 57 TYR A CB 387 C CG . TYR A 59 ? 0.4631 1.0034 0.4084 -0.1219 0.0796 0.1031 57 TYR A CG 388 C CD1 . TYR A 59 ? 0.4606 0.9607 0.3700 -0.1282 0.0573 0.1024 57 TYR A CD1 389 C CD2 . TYR A 59 ? 0.5013 1.0752 0.4411 -0.1339 0.1017 0.1182 57 TYR A CD2 390 C CE1 . TYR A 59 ? 0.4127 0.9070 0.2809 -0.1421 0.0544 0.1187 57 TYR A CE1 391 C CE2 . TYR A 59 ? 0.5508 1.1112 0.4433 -0.1502 0.1013 0.1339 57 TYR A CE2 392 C CZ . TYR A 59 ? 0.4883 1.0090 0.3447 -0.1524 0.0762 0.1353 57 TYR A CZ 393 O OH . TYR A 59 ? 0.6061 1.1172 0.4161 -0.1645 0.0737 0.1558 57 TYR A OH 394 N N . SER A 60 ? 0.5098 1.0499 0.4452 -0.0568 0.1397 0.0402 58 SER A N 395 C CA . SER A 60 ? 0.5881 1.1215 0.4725 -0.0524 0.1692 0.0212 58 SER A CA 396 C C . SER A 60 ? 0.6203 1.0988 0.4432 -0.0603 0.1550 -0.0026 58 SER A C 397 O O . SER A 60 ? 0.6595 1.1329 0.4273 -0.0799 0.1488 -0.0025 58 SER A O 398 C CB . SER A 60 ? 0.6188 1.1878 0.4820 -0.0721 0.1827 0.0396 58 SER A CB 399 O OG . SER A 60 ? 0.6401 1.1962 0.4802 -0.0974 0.1528 0.0588 58 SER A OG 400 N N . ASN A 61 ? 0.6311 1.0711 0.4644 -0.0465 0.1486 -0.0209 59 ASN A N 401 C CA . ASN A 61 ? 0.6773 1.0650 0.4572 -0.0553 0.1405 -0.0500 59 ASN A CA 402 C C . ASN A 61 ? 0.6497 1.0343 0.4040 -0.0830 0.1032 -0.0402 59 ASN A C 403 O O . ASN A 61 ? 0.6898 1.0520 0.3926 -0.0982 0.0947 -0.0606 59 ASN A O 404 C CB . ASN A 61 ? 0.7597 1.1319 0.4799 -0.0533 0.1748 -0.0793 59 ASN A CB 405 C CG . ASN A 61 ? 0.8134 1.1770 0.5586 -0.0196 0.2166 -0.0934 59 ASN A CG 406 O OD1 . ASN A 61 ? 0.8577 1.2058 0.6501 0.0023 0.2154 -0.0907 59 ASN A OD1 407 N ND2 . ASN A 61 ? 0.8965 1.2693 0.6084 -0.0133 0.2553 -0.1071 59 ASN A ND2 408 N N . LEU A 62 ? 0.5871 0.9957 0.3794 -0.0896 0.0817 -0.0091 60 LEU A N 409 C CA . LEU A 62 ? 0.5530 0.9602 0.3315 -0.1093 0.0493 0.0060 60 LEU A CA 410 C C . LEU A 62 ? 0.5088 0.9028 0.3341 -0.1087 0.0259 0.0175 60 LEU A C 411 O O . LEU A 62 ? 0.4670 0.8753 0.3343 -0.1050 0.0263 0.0368 60 LEU A O 412 C CB . LEU A 62 ? 0.5363 0.9754 0.3033 -0.1200 0.0503 0.0354 60 LEU A CB 413 C CG . LEU A 62 ? 0.5592 1.0105 0.2673 -0.1245 0.0724 0.0264 60 LEU A CG 414 C CD1 . LEU A 62 ? 0.5626 1.0441 0.2677 -0.1331 0.0821 0.0587 60 LEU A CD1 415 C CD2 . LEU A 62 ? 0.5206 0.9573 0.1679 -0.1384 0.0530 0.0113 60 LEU A CD2 416 N N . SER A 63 ? 0.5152 0.8841 0.3312 -0.1157 0.0064 0.0045 61 SER A N 417 C CA . SER A 63 ? 0.4704 0.8228 0.3256 -0.1158 -0.0122 0.0124 61 SER A CA 418 C C . SER A 63 ? 0.4446 0.8063 0.3021 -0.1279 -0.0365 0.0336 61 SER A C 419 O O . SER A 63 ? 0.4668 0.8349 0.2972 -0.1375 -0.0508 0.0292 61 SER A O 420 C CB . SER A 63 ? 0.4769 0.7936 0.3300 -0.1144 -0.0130 -0.0149 61 SER A CB 421 O OG . SER A 63 ? 0.5124 0.8128 0.4039 -0.1117 -0.0235 -0.0060 61 SER A OG 422 N N . VAL A 64 ? 0.4045 0.7671 0.2956 -0.1271 -0.0408 0.0566 62 VAL A N 423 C CA . VAL A 64 ? 0.3839 0.7490 0.2809 -0.1338 -0.0571 0.0811 62 VAL A CA 424 C C . VAL A 64 ? 0.3602 0.7017 0.2937 -0.1328 -0.0658 0.0843 62 VAL A C 425 O O . VAL A 64 ? 0.3665 0.6993 0.3212 -0.1343 -0.0609 0.0975 62 VAL A O 426 C CB . VAL A 64 ? 0.3894 0.7686 0.2823 -0.1377 -0.0477 0.1077 62 VAL A CB 427 C CG1 . VAL A 64 ? 0.3498 0.7206 0.2467 -0.1410 -0.0605 0.1359 62 VAL A CG1 428 C CG2 . VAL A 64 ? 0.4237 0.8261 0.2758 -0.1393 -0.0353 0.1048 62 VAL A CG2 429 N N . PRO A 65 ? 0.3565 0.6876 0.2957 -0.1334 -0.0771 0.0703 63 PRO A N 430 C CA . PRO A 65 ? 0.3304 0.6399 0.3017 -0.1329 -0.0823 0.0757 63 PRO A CA 431 C C . PRO A 65 ? 0.3334 0.6467 0.3131 -0.1324 -0.0890 0.1034 63 PRO A C 432 O O . PRO A 65 ? 0.3571 0.6931 0.3217 -0.1315 -0.0993 0.1156 63 PRO A O 433 C CB . PRO A 65 ? 0.3434 0.6496 0.3189 -0.1363 -0.0909 0.0555 63 PRO A CB 434 C CG . PRO A 65 ? 0.3502 0.6808 0.2919 -0.1420 -0.0966 0.0436 63 PRO A CG 435 C CD . PRO A 65 ? 0.3673 0.7039 0.2841 -0.1379 -0.0824 0.0464 63 PRO A CD 436 N N . THR A 66 ? 0.3312 0.6199 0.3309 -0.1327 -0.0825 0.1142 64 THR A N 437 C CA . THR A 66 ? 0.3500 0.6294 0.3547 -0.1311 -0.0819 0.1417 64 THR A CA 438 C C . THR A 66 ? 0.3377 0.5877 0.3695 -0.1270 -0.0797 0.1459 64 THR A C 439 O O . THR A 66 ? 0.3150 0.5500 0.3607 -0.1286 -0.0772 0.1278 64 THR A O 440 C CB . THR A 66 ? 0.3637 0.6338 0.3590 -0.1403 -0.0685 0.1547 64 THR A CB 441 O OG1 . THR A 66 ? 0.3620 0.6049 0.3724 -0.1484 -0.0605 0.1464 64 THR A OG1 442 C CG2 . THR A 66 ? 0.3353 0.6356 0.3109 -0.1438 -0.0638 0.1469 64 THR A CG2 443 N N . GLY A 67 ? 0.3557 0.5939 0.3917 -0.1208 -0.0773 0.1718 65 GLY A N 444 C CA . GLY A 67 ? 0.3703 0.5721 0.4292 -0.1146 -0.0675 0.1801 65 GLY A CA 445 C C . GLY A 67 ? 0.3866 0.6011 0.4748 -0.1041 -0.0742 0.1713 65 GLY A C 446 O O . GLY A 67 ? 0.4019 0.6588 0.4975 -0.0975 -0.0910 0.1733 65 GLY A O 447 N N . ARG A 68 ? 0.3973 0.5767 0.5009 -0.1059 -0.0602 0.1601 66 ARG A N 448 C CA . ARG A 68 ? 0.3801 0.5687 0.5157 -0.0982 -0.0602 0.1510 66 ARG A CA 449 C C . ARG A 68 ? 0.3462 0.5509 0.4763 -0.1101 -0.0671 0.1232 66 ARG A C 450 O O . ARG A 68 ? 0.3669 0.5802 0.5212 -0.1096 -0.0659 0.1120 66 ARG A O 451 C CB . ARG A 68 ? 0.3975 0.5363 0.5471 -0.0948 -0.0367 0.1507 66 ARG A CB 452 C CG . ARG A 68 ? 0.3904 0.4861 0.5138 -0.1133 -0.0236 0.1299 66 ARG A CG 453 C CD . ARG A 68 ? 0.4129 0.4536 0.5397 -0.1120 0.0021 0.1296 66 ARG A CD 454 N NE . ARG A 68 ? 0.4458 0.4462 0.5374 -0.1339 0.0113 0.1131 66 ARG A NE 455 C CZ . ARG A 68 ? 0.5171 0.5151 0.5952 -0.1449 0.0101 0.0931 66 ARG A CZ 456 N NH1 . ARG A 68 ? 0.5488 0.5744 0.6455 -0.1379 0.0039 0.0853 66 ARG A NH1 457 N NH2 . ARG A 68 ? 0.5556 0.5238 0.5998 -0.1646 0.0144 0.0818 66 ARG A NH2 458 N N . PHE A 69 ? 0.3243 0.5318 0.4247 -0.1200 -0.0714 0.1133 67 PHE A N 459 C CA . PHE A 69 ? 0.2950 0.5107 0.3863 -0.1277 -0.0752 0.0892 67 PHE A CA 460 C C . PHE A 69 ? 0.2994 0.5550 0.3791 -0.1285 -0.0902 0.0858 67 PHE A C 461 O O . PHE A 69 ? 0.2848 0.5444 0.3523 -0.1350 -0.0918 0.0650 67 PHE A O 462 C CB . PHE A 69 ? 0.2643 0.4579 0.3326 -0.1341 -0.0681 0.0803 67 PHE A CB 463 C CG . PHE A 69 ? 0.2798 0.4358 0.3477 -0.1387 -0.0561 0.0821 67 PHE A CG 464 C CD1 . PHE A 69 ? 0.3168 0.4580 0.3810 -0.1418 -0.0504 0.0972 67 PHE A CD1 465 C CD2 . PHE A 69 ? 0.1837 0.3146 0.2486 -0.1426 -0.0489 0.0681 67 PHE A CD2 466 C CE1 . PHE A 69 ? 0.2993 0.4017 0.3555 -0.1512 -0.0385 0.0945 67 PHE A CE1 467 C CE2 . PHE A 69 ? 0.2455 0.3416 0.3004 -0.1499 -0.0385 0.0681 67 PHE A CE2 468 C CZ . PHE A 69 ? 0.2949 0.3770 0.3449 -0.1553 -0.0336 0.0793 67 PHE A CZ 469 N N . GLN A 70 ? 0.3179 0.5976 0.3969 -0.1220 -0.0993 0.1071 68 GLN A N 470 C CA . GLN A 70 ? 0.3744 0.6938 0.4325 -0.1242 -0.1148 0.1077 68 GLN A CA 471 C C . GLN A 70 ? 0.3962 0.7393 0.4568 -0.1341 -0.1254 0.0834 68 GLN A C 472 O O . GLN A 70 ? 0.4347 0.7925 0.4642 -0.1425 -0.1307 0.0688 68 GLN A O 473 C CB . GLN A 70 ? 0.4126 0.7569 0.4778 -0.1130 -0.1262 0.1389 68 GLN A CB 474 C CG . GLN A 70 ? 0.4575 0.8350 0.4867 -0.1151 -0.1394 0.1478 68 GLN A CG 475 C CD . GLN A 70 ? 0.5500 0.9400 0.5825 -0.1003 -0.1470 0.1869 68 GLN A CD 476 O OE1 . GLN A 70 ? 0.6603 1.0910 0.6735 -0.0983 -0.1661 0.2007 68 GLN A OE1 477 N NE2 . GLN A 70 ? 0.4500 0.8014 0.5036 -0.0898 -0.1313 0.2057 68 GLN A NE2 478 N N . ASN A 71 ? 0.3904 0.7357 0.4869 -0.1355 -0.1258 0.0778 69 ASN A N 479 C CA . ASN A 71 ? 0.4161 0.7876 0.5204 -0.1504 -0.1359 0.0552 69 ASN A CA 480 C C . ASN A 71 ? 0.3895 0.7214 0.4924 -0.1613 -0.1194 0.0280 69 ASN A C 481 O O . ASN A 71 ? 0.3924 0.7339 0.4986 -0.1781 -0.1225 0.0058 69 ASN A O 482 C CB . ASN A 71 ? 0.4247 0.8381 0.5776 -0.1468 -0.1478 0.0684 69 ASN A CB 483 C CG . ASN A 71 ? 0.5543 1.0214 0.7058 -0.1388 -0.1718 0.0931 69 ASN A CG 484 O OD1 . ASN A 71 ? 0.7037 1.1929 0.8156 -0.1491 -0.1862 0.0863 69 ASN A OD1 485 N ND2 . ASN A 71 ? 0.6659 1.1523 0.8573 -0.1189 -0.1750 0.1230 69 ASN A ND2 486 N N . ARG A 72 ? 0.3590 0.6462 0.4546 -0.1535 -0.1021 0.0307 70 ARG A N 487 C CA . ARG A 72 ? 0.3513 0.5976 0.4488 -0.1593 -0.0857 0.0136 70 ARG A CA 488 C C . ARG A 72 ? 0.3530 0.5642 0.4165 -0.1569 -0.0752 0.0031 70 ARG A C 489 O O . ARG A 72 ? 0.3475 0.5248 0.4049 -0.1614 -0.0633 -0.0114 70 ARG A O 490 C CB . ARG A 72 ? 0.3363 0.5596 0.4565 -0.1522 -0.0737 0.0266 70 ARG A CB 491 C CG . ARG A 72 ? 0.3444 0.5983 0.5075 -0.1500 -0.0772 0.0366 70 ARG A CG 492 C CD . ARG A 72 ? 0.3384 0.5591 0.5195 -0.1448 -0.0573 0.0418 70 ARG A CD 493 N NE . ARG A 72 ? 0.2883 0.4859 0.4579 -0.1333 -0.0517 0.0595 70 ARG A NE 494 C CZ . ARG A 72 ? 0.2846 0.4377 0.4459 -0.1331 -0.0332 0.0593 70 ARG A CZ 495 N NH1 . ARG A 72 ? 0.3376 0.4664 0.4989 -0.1410 -0.0187 0.0453 70 ARG A NH1 496 N NH2 . ARG A 72 ? 0.3629 0.4929 0.5109 -0.1281 -0.0279 0.0722 70 ARG A NH2 497 N N . SER A 73 ? 0.3347 0.5554 0.3789 -0.1484 -0.0781 0.0131 71 SER A N 498 C CA . SER A 73 ? 0.3341 0.5333 0.3565 -0.1408 -0.0680 0.0093 71 SER A CA 499 C C . SER A 73 ? 0.3644 0.5727 0.3607 -0.1402 -0.0660 -0.0050 71 SER A C 500 O O . SER A 73 ? 0.3740 0.6134 0.3585 -0.1426 -0.0743 -0.0015 71 SER A O 501 C CB . SER A 73 ? 0.3180 0.5235 0.3424 -0.1340 -0.0680 0.0300 71 SER A CB 502 O OG . SER A 73 ? 0.3444 0.5792 0.3700 -0.1348 -0.0769 0.0444 71 SER A OG 503 N N . HIS A 74 ? 0.3813 0.5580 0.3647 -0.1354 -0.0526 -0.0200 72 HIS A N 504 C CA . HIS A 74 ? 0.4244 0.5972 0.3805 -0.1324 -0.0433 -0.0373 72 HIS A CA 505 C C . HIS A 74 ? 0.4344 0.5899 0.3866 -0.1118 -0.0279 -0.0333 72 HIS A C 506 O O . HIS A 74 ? 0.4590 0.5970 0.4248 -0.1032 -0.0257 -0.0220 72 HIS A O 507 C CB . HIS A 74 ? 0.4776 0.6227 0.4206 -0.1474 -0.0379 -0.0645 72 HIS A CB 508 C CG . HIS A 74 ? 0.5164 0.6901 0.4712 -0.1690 -0.0554 -0.0688 72 HIS A CG 509 N ND1 . HIS A 74 ? 0.5828 0.7825 0.5161 -0.1852 -0.0652 -0.0847 72 HIS A ND1 510 C CD2 . HIS A 74 ? 0.4799 0.6647 0.4673 -0.1765 -0.0645 -0.0591 72 HIS A CD2 511 C CE1 . HIS A 74 ? 0.5632 0.7959 0.5202 -0.2012 -0.0832 -0.0821 72 HIS A CE1 512 N NE2 . HIS A 74 ? 0.5419 0.7658 0.5350 -0.1945 -0.0811 -0.0664 72 HIS A NE2 513 N N . LEU A 75 ? 0.4512 0.6153 0.3844 -0.1032 -0.0168 -0.0417 73 LEU A N 514 C CA . LEU A 75 ? 0.4617 0.6204 0.3989 -0.0792 -0.0005 -0.0361 73 LEU A CA 515 C C . LEU A 75 ? 0.5158 0.6246 0.4316 -0.0708 0.0207 -0.0595 73 LEU A C 516 O O . LEU A 75 ? 0.5392 0.6409 0.4278 -0.0728 0.0340 -0.0802 73 LEU A O 517 C CB . LEU A 75 ? 0.4631 0.6669 0.3991 -0.0727 0.0035 -0.0272 73 LEU A CB 518 C CG . LEU A 75 ? 0.5087 0.7313 0.4647 -0.0479 0.0173 -0.0145 73 LEU A CG 519 C CD1 . LEU A 75 ? 0.5282 0.7442 0.5111 -0.0388 0.0086 0.0030 73 LEU A CD1 520 C CD2 . LEU A 75 ? 0.4883 0.7653 0.4528 -0.0514 0.0167 0.0002 73 LEU A CD2 521 N N . VAL A 76 ? 0.5455 0.6140 0.4688 -0.0627 0.0255 -0.0560 74 VAL A N 522 C CA . VAL A 76 ? 0.6064 0.6114 0.5081 -0.0586 0.0469 -0.0766 74 VAL A CA 523 C C . VAL A 76 ? 0.6520 0.6380 0.5574 -0.0220 0.0680 -0.0671 74 VAL A C 524 O O . VAL A 76 ? 0.7029 0.6279 0.5895 -0.0104 0.0919 -0.0807 74 VAL A O 525 C CB . VAL A 76 ? 0.6079 0.5733 0.5128 -0.0728 0.0428 -0.0762 74 VAL A CB 526 C CG1 . VAL A 76 ? 0.5696 0.5554 0.4766 -0.1071 0.0260 -0.0886 74 VAL A CG1 527 C CG2 . VAL A 76 ? 0.5672 0.5445 0.4946 -0.0588 0.0320 -0.0457 74 VAL A CG2 528 N N . GLY A 77 ? 0.6305 0.6700 0.5626 -0.0038 0.0602 -0.0429 75 GLY A N 529 C CA . GLY A 77 ? 0.6697 0.7122 0.6172 0.0343 0.0773 -0.0291 75 GLY A CA 530 C C . GLY A 77 ? 0.7250 0.7589 0.6559 0.0482 0.1060 -0.0499 75 GLY A C 531 O O . GLY A 77 ? 0.7191 0.7793 0.6345 0.0294 0.1053 -0.0650 75 GLY A O 532 N N . ASP A 78 ? 0.7892 0.7826 0.7201 0.0827 0.1333 -0.0497 76 ASP A N 533 C CA . ASP A 78 ? 0.8578 0.8405 0.7753 0.1029 0.1678 -0.0686 76 ASP A CA 534 C C . ASP A 78 ? 0.8292 0.8952 0.7843 0.1231 0.1695 -0.0495 76 ASP A C 535 O O . ASP A 78 ? 0.8186 0.9207 0.8172 0.1558 0.1689 -0.0206 76 ASP A O 536 C CB . ASP A 78 ? 0.9354 0.8414 0.8431 0.1382 0.2022 -0.0731 76 ASP A CB 537 C CG . ASP A 78 ? 1.0463 0.9242 0.9298 0.1544 0.2437 -0.1009 76 ASP A CG 538 O OD1 . ASP A 78 ? 1.1220 0.9680 0.9578 0.1206 0.2514 -0.1378 76 ASP A OD1 539 O OD2 . ASP A 78 ? 1.1367 1.0281 1.0487 0.2004 0.2689 -0.0862 76 ASP A OD2 540 N N . THR A 79 ? 0.8252 0.9240 0.7626 0.1022 0.1720 -0.0652 77 THR A N 541 C CA . THR A 79 ? 0.8170 0.9981 0.7873 0.1104 0.1727 -0.0477 77 THR A CA 542 C C . THR A 79 ? 0.8714 1.0655 0.8672 0.1555 0.2104 -0.0441 77 THR A C 543 O O . THR A 79 ? 0.8464 1.1150 0.8786 0.1654 0.2157 -0.0282 77 THR A O 544 C CB . THR A 79 ? 0.8220 1.0252 0.7567 0.0769 0.1701 -0.0648 77 THR A CB 545 O OG1 . THR A 79 ? 0.8437 1.0217 0.7505 0.0406 0.1414 -0.0733 77 THR A OG1 546 C CG2 . THR A 79 ? 0.7925 1.0806 0.7621 0.0725 0.1608 -0.0401 77 THR A CG2 547 N N . PHE A 80 ? 0.9492 1.0704 0.9286 0.1831 0.2391 -0.0578 78 PHE A N 548 C CA . PHE A 80 ? 1.0088 1.1332 1.0149 0.2336 0.2802 -0.0535 78 PHE A CA 549 C C . PHE A 80 ? 1.0008 1.1333 1.0590 0.2770 0.2747 -0.0176 78 PHE A C 550 O O . PHE A 80 ? 1.0209 1.2026 1.1298 0.3206 0.2940 0.0029 78 PHE A O 551 C CB . PHE A 80 ? 1.1161 1.1468 1.0649 0.2405 0.3253 -0.0942 78 PHE A CB 552 C CG . PHE A 80 ? 1.1970 1.2185 1.0852 0.1968 0.3292 -0.1308 78 PHE A CG 553 C CD1 . PHE A 80 ? 1.2023 1.3048 1.0991 0.1818 0.3232 -0.1248 78 PHE A CD1 554 C CD2 . PHE A 80 ? 1.3098 1.2428 1.1302 0.1688 0.3388 -0.1703 78 PHE A CD2 555 C CE1 . PHE A 80 ? 1.2274 1.3222 1.0625 0.1432 0.3249 -0.1542 78 PHE A CE1 556 C CE2 . PHE A 80 ? 1.3374 1.2697 1.0992 0.1274 0.3378 -0.2024 78 PHE A CE2 557 C CZ . PHE A 80 ? 1.3037 1.3168 1.0710 0.1165 0.3301 -0.1926 78 PHE A CZ 558 N N . HIS A 81 ? 0.9762 1.0640 1.0221 0.2659 0.2490 -0.0085 79 HIS A N 559 C CA . HIS A 81 ? 0.9763 1.0665 1.0599 0.3042 0.2399 0.0280 79 HIS A CA 560 C C . HIS A 81 ? 0.8682 1.0323 0.9821 0.2811 0.1900 0.0575 79 HIS A C 561 O O . HIS A 81 ? 0.8603 0.9930 0.9627 0.2731 0.1665 0.0713 79 HIS A O 562 C CB . HIS A 81 ? 1.0551 1.0291 1.0964 0.3127 0.2552 0.0186 79 HIS A CB 563 C CG . HIS A 81 ? 1.1294 1.0961 1.2010 0.3576 0.2502 0.0593 79 HIS A CG 564 N ND1 . HIS A 81 ? 1.1926 1.2135 1.3199 0.4138 0.2637 0.0899 79 HIS A ND1 565 C CD2 . HIS A 81 ? 1.1734 1.0877 1.2266 0.3556 0.2334 0.0767 79 HIS A CD2 566 C CE1 . HIS A 81 ? 1.2201 1.2238 1.3605 0.4456 0.2520 0.1264 79 HIS A CE1 567 N NE2 . HIS A 81 ? 1.2164 1.1519 1.3086 0.4103 0.2346 0.1188 79 HIS A NE2 568 N N . ASN A 82 ? 0.7839 1.0419 0.9319 0.2673 0.1772 0.0649 80 ASN A N 569 C CA . ASN A 82 ? 0.7049 1.0443 0.8909 0.2504 0.1358 0.0942 80 ASN A CA 570 C C . ASN A 82 ? 0.6516 0.9600 0.8028 0.2055 0.1018 0.0899 80 ASN A C 571 O O . ASN A 82 ? 0.6025 0.9494 0.7726 0.1962 0.0701 0.1134 80 ASN A O 572 C CB . ASN A 82 ? 0.7198 1.0943 0.9518 0.2939 0.1269 0.1319 80 ASN A CB 573 C CG . ASN A 82 ? 0.7901 1.1850 1.0615 0.3497 0.1645 0.1402 80 ASN A CG 574 O OD1 . ASN A 82 ? 0.8919 1.2352 1.1389 0.3613 0.2051 0.1126 80 ASN A OD1 575 N ND2 . ASN A 82 ? 0.8021 1.2737 1.1346 0.3855 0.1517 0.1783 80 ASN A ND2 576 N N . ASP A 83 ? 0.6551 0.8983 0.7564 0.1771 0.1089 0.0596 81 ASP A N 577 C CA . ASP A 83 ? 0.6361 0.8367 0.7065 0.1431 0.0845 0.0548 81 ASP A CA 578 C C . ASP A 83 ? 0.5762 0.7903 0.6276 0.0981 0.0696 0.0383 81 ASP A C 579 O O . ASP A 83 ? 0.5950 0.7851 0.6180 0.0852 0.0844 0.0128 81 ASP A O 580 C CB . ASP A 83 ? 0.7078 0.8102 0.7393 0.1515 0.1046 0.0377 81 ASP A CB 581 C CG . ASP A 83 ? 0.7317 0.7911 0.7392 0.1236 0.0840 0.0379 81 ASP A CG 582 O OD1 . ASP A 83 ? 0.7009 0.8026 0.7196 0.1006 0.0552 0.0507 81 ASP A OD1 583 O OD2 . ASP A 83 ? 0.8150 0.7945 0.7914 0.1235 0.1003 0.0239 81 ASP A OD2 584 N N . GLY A 84 ? 0.5102 0.7595 0.5740 0.0747 0.0403 0.0538 82 GLY A N 585 C CA . GLY A 84 ? 0.4778 0.7380 0.5278 0.0365 0.0258 0.0446 82 GLY A CA 586 C C . GLY A 84 ? 0.4633 0.6823 0.4944 0.0134 0.0081 0.0426 82 GLY A C 587 O O . GLY A 84 ? 0.4250 0.6587 0.4550 -0.0136 -0.0078 0.0444 82 GLY A O 588 N N . SER A 85 ? 0.4910 0.6547 0.5073 0.0256 0.0147 0.0398 83 SER A N 589 C CA . SER A 85 ? 0.4780 0.6008 0.4774 0.0060 0.0034 0.0386 83 SER A CA 590 C C . SER A 85 ? 0.4516 0.5681 0.4392 -0.0247 -0.0016 0.0208 83 SER A C 591 O O . SER A 85 ? 0.4508 0.5665 0.4277 -0.0297 0.0077 0.0027 83 SER A O 592 C CB . SER A 85 ? 0.5269 0.5814 0.5062 0.0213 0.0191 0.0344 83 SER A CB 593 O OG . SER A 85 ? 0.5754 0.6350 0.5664 0.0560 0.0237 0.0557 83 SER A OG 594 N N . LEU A 86 ? 0.4261 0.5388 0.4142 -0.0442 -0.0161 0.0270 84 LEU A N 595 C CA . LEU A 86 ? 0.4155 0.5276 0.4010 -0.0693 -0.0227 0.0164 84 LEU A CA 596 C C . LEU A 86 ? 0.4286 0.4934 0.4035 -0.0812 -0.0178 0.0048 84 LEU A C 597 O O . LEU A 86 ? 0.4626 0.4945 0.4301 -0.0766 -0.0139 0.0116 84 LEU A O 598 C CB . LEU A 86 ? 0.3823 0.5240 0.3805 -0.0826 -0.0375 0.0314 84 LEU A CB 599 C CG . LEU A 86 ? 0.3576 0.5022 0.3589 -0.1018 -0.0433 0.0265 84 LEU A CG 600 C CD1 . LEU A 86 ? 0.3571 0.5353 0.3585 -0.1034 -0.0447 0.0240 84 LEU A CD1 601 C CD2 . LEU A 86 ? 0.3160 0.4631 0.3243 -0.1134 -0.0509 0.0393 84 LEU A CD2 602 N N . LEU A 87 ? 0.4100 0.4757 0.3840 -0.0980 -0.0183 -0.0113 85 LEU A N 603 C CA . LEU A 87 ? 0.4060 0.4421 0.3806 -0.1149 -0.0150 -0.0217 85 LEU A CA 604 C C . LEU A 87 ? 0.3883 0.4561 0.3828 -0.1299 -0.0278 -0.0168 85 LEU A C 605 O O . LEU A 87 ? 0.3879 0.4916 0.3879 -0.1348 -0.0373 -0.0187 85 LEU A O 606 C CB . LEU A 87 ? 0.4396 0.4514 0.4009 -0.1249 -0.0043 -0.0467 85 LEU A CB 607 C CG . LEU A 87 ? 0.4018 0.3868 0.3690 -0.1468 0.0013 -0.0584 85 LEU A CG 608 C CD1 . LEU A 87 ? 0.4347 0.3582 0.3855 -0.1399 0.0201 -0.0564 85 LEU A CD1 609 C CD2 . LEU A 87 ? 0.3432 0.3347 0.3067 -0.1690 0.0012 -0.0843 85 LEU A CD2 610 N N . LEU A 88 ? 0.3782 0.4302 0.3810 -0.1355 -0.0260 -0.0092 86 LEU A N 611 C CA . LEU A 88 ? 0.3609 0.4348 0.3864 -0.1457 -0.0322 -0.0038 86 LEU A CA 612 C C . LEU A 88 ? 0.3775 0.4389 0.4178 -0.1602 -0.0240 -0.0158 86 LEU A C 613 O O . LEU A 88 ? 0.4237 0.4454 0.4537 -0.1639 -0.0100 -0.0203 86 LEU A O 614 C CB . LEU A 88 ? 0.3441 0.4104 0.3678 -0.1425 -0.0322 0.0120 86 LEU A CB 615 C CG . LEU A 88 ? 0.3588 0.4401 0.4036 -0.1477 -0.0341 0.0200 86 LEU A CG 616 C CD1 . LEU A 88 ? 0.3325 0.4546 0.3898 -0.1448 -0.0466 0.0260 86 LEU A CD1 617 C CD2 . LEU A 88 ? 0.2889 0.3510 0.3214 -0.1488 -0.0306 0.0303 86 LEU A CD2 618 N N . GLN A 89 ? 0.3661 0.4653 0.4318 -0.1687 -0.0330 -0.0191 87 GLN A N 619 C CA . GLN A 89 ? 0.3764 0.4810 0.4664 -0.1855 -0.0275 -0.0312 87 GLN A CA 620 C C . GLN A 89 ? 0.3691 0.4998 0.4974 -0.1851 -0.0273 -0.0196 87 GLN A C 621 O O . GLN A 89 ? 0.3808 0.5323 0.5178 -0.1728 -0.0357 -0.0031 87 GLN A O 622 C CB . GLN A 89 ? 0.3890 0.5255 0.4810 -0.1986 -0.0396 -0.0473 87 GLN A CB 623 C CG . GLN A 89 ? 0.4467 0.5432 0.5037 -0.2039 -0.0297 -0.0665 87 GLN A CG 624 C CD . GLN A 89 ? 0.4671 0.5875 0.5208 -0.2248 -0.0383 -0.0887 87 GLN A CD 625 O OE1 . GLN A 89 ? 0.4486 0.6112 0.4972 -0.2234 -0.0559 -0.0871 87 GLN A OE1 626 N NE2 . GLN A 89 ? 0.5548 0.6466 0.6070 -0.2475 -0.0253 -0.1103 87 GLN A NE2 627 N N . ASP A 90 ? 0.3825 0.5094 0.5349 -0.1984 -0.0143 -0.0279 88 ASP A N 628 C CA . ASP A 90 ? 0.3822 0.5353 0.5787 -0.1962 -0.0080 -0.0184 88 ASP A CA 629 C C . ASP A 90 ? 0.3675 0.4916 0.5507 -0.1794 0.0013 -0.0022 88 ASP A C 630 O O . ASP A 90 ? 0.3676 0.5142 0.5695 -0.1662 -0.0046 0.0127 88 ASP A O 631 C CB . ASP A 90 ? 0.3747 0.5985 0.6113 -0.1954 -0.0295 -0.0128 88 ASP A CB 632 C CG . ASP A 90 ? 0.5294 0.7873 0.7846 -0.2208 -0.0372 -0.0329 88 ASP A CG 633 O OD1 . ASP A 90 ? 0.7150 0.9599 0.9880 -0.2382 -0.0189 -0.0454 88 ASP A OD1 634 O OD2 . ASP A 90 ? 0.5832 0.8803 0.8325 -0.2267 -0.0605 -0.0374 88 ASP A OD2 635 N N . VAL A 91 ? 0.3629 0.4336 0.5090 -0.1813 0.0160 -0.0052 89 VAL A N 636 C CA . VAL A 91 ? 0.3552 0.3940 0.4780 -0.1727 0.0243 0.0054 89 VAL A CA 637 C C . VAL A 91 ? 0.3602 0.3950 0.5098 -0.1702 0.0443 0.0094 89 VAL A C 638 O O . VAL A 91 ? 0.3490 0.3835 0.5215 -0.1778 0.0624 0.0025 89 VAL A O 639 C CB . VAL A 91 ? 0.3749 0.3627 0.4485 -0.1767 0.0328 0.0026 89 VAL A CB 640 C CG1 . VAL A 91 ? 0.3122 0.2723 0.3578 -0.1741 0.0385 0.0105 89 VAL A CG1 641 C CG2 . VAL A 91 ? 0.3459 0.3356 0.3965 -0.1724 0.0169 0.0012 89 VAL A CG2 642 N N . GLN A 92 ? 0.3800 0.4079 0.5252 -0.1601 0.0443 0.0201 90 GLN A N 643 C CA . GLN A 92 ? 0.4144 0.4289 0.5806 -0.1534 0.0674 0.0243 90 GLN A CA 644 C C . GLN A 92 ? 0.4459 0.4023 0.5626 -0.1586 0.0828 0.0217 90 GLN A C 645 O O . GLN A 92 ? 0.4627 0.4012 0.5352 -0.1660 0.0698 0.0208 90 GLN A O 646 C CB . GLN A 92 ? 0.4219 0.4704 0.6240 -0.1365 0.0572 0.0402 90 GLN A CB 647 C CG . GLN A 92 ? 0.4461 0.5589 0.6862 -0.1334 0.0334 0.0445 90 GLN A CG 648 C CD . GLN A 92 ? 0.5271 0.6669 0.7741 -0.1194 0.0138 0.0633 90 GLN A CD 649 O OE1 . GLN A 92 ? 0.6402 0.8332 0.9087 -0.1172 -0.0084 0.0686 90 GLN A OE1 650 N NE2 . GLN A 92 ? 0.4390 0.5403 0.6632 -0.1126 0.0224 0.0730 90 GLN A NE2 651 N N . LYS A 93 ? 0.4736 0.4035 0.5986 -0.1548 0.1108 0.0204 91 LYS A N 652 C CA . LYS A 93 ? 0.5102 0.3798 0.5801 -0.1653 0.1287 0.0130 91 LYS A CA 653 C C . LYS A 93 ? 0.4969 0.3550 0.5424 -0.1666 0.1137 0.0193 91 LYS A C 654 O O . LYS A 93 ? 0.5212 0.3458 0.5132 -0.1826 0.1113 0.0130 91 LYS A O 655 C CB . LYS A 93 ? 0.5490 0.3876 0.6319 -0.1605 0.1682 0.0072 91 LYS A CB 656 C CG . LYS A 93 ? 0.6490 0.4196 0.6641 -0.1764 0.1895 -0.0053 91 LYS A CG 657 C CD . LYS A 93 ? 0.6869 0.4376 0.6449 -0.1959 0.1841 -0.0132 91 LYS A CD 658 C CE . LYS A 93 ? 0.7227 0.4127 0.6052 -0.2152 0.1980 -0.0250 91 LYS A CE 659 N NZ . LYS A 93 ? 0.7347 0.4015 0.5587 -0.2313 0.1992 -0.0294 91 LYS A NZ 660 N N . ALA A 94 ? 0.4660 0.3569 0.5514 -0.1515 0.1023 0.0329 92 ALA A N 661 C CA . ALA A 94 ? 0.4298 0.3131 0.4995 -0.1527 0.0904 0.0422 92 ALA A CA 662 C C . ALA A 94 ? 0.4265 0.3352 0.4717 -0.1633 0.0603 0.0431 92 ALA A C 663 O O . ALA A 94 ? 0.4541 0.3632 0.4858 -0.1686 0.0496 0.0501 92 ALA A O 664 C CB . ALA A 94 ? 0.3877 0.2995 0.5054 -0.1309 0.0878 0.0610 92 ALA A CB 665 N N . ASP A 95 ? 0.4208 0.3485 0.4615 -0.1662 0.0501 0.0366 93 ASP A N 666 C CA . ASP A 95 ? 0.4085 0.3577 0.4280 -0.1714 0.0261 0.0375 93 ASP A CA 667 C C . ASP A 95 ? 0.4362 0.3562 0.4077 -0.1863 0.0262 0.0310 93 ASP A C 668 O O . ASP A 95 ? 0.4390 0.3774 0.3944 -0.1880 0.0081 0.0338 93 ASP A O 669 C CB . ASP A 95 ? 0.3956 0.3740 0.4324 -0.1650 0.0166 0.0344 93 ASP A CB 670 C CG . ASP A 95 ? 0.4258 0.4440 0.5056 -0.1543 0.0099 0.0398 93 ASP A CG 671 O OD1 . ASP A 95 ? 0.4747 0.5034 0.5703 -0.1473 0.0081 0.0513 93 ASP A OD1 672 O OD2 . ASP A 95 ? 0.4494 0.4873 0.5445 -0.1543 0.0062 0.0329 93 ASP A OD2 673 N N . GLU A 96 ? 0.4695 0.3458 0.4175 -0.1960 0.0473 0.0231 94 GLU A N 674 C CA . GLU A 96 ? 0.5114 0.3595 0.4049 -0.2133 0.0463 0.0168 94 GLU A CA 675 C C . GLU A 96 ? 0.5162 0.3707 0.3865 -0.2289 0.0301 0.0189 94 GLU A C 676 O O . GLU A 96 ? 0.5161 0.3480 0.3825 -0.2391 0.0407 0.0154 94 GLU A O 677 C CB . GLU A 96 ? 0.5662 0.3623 0.4330 -0.2224 0.0767 0.0049 94 GLU A CB 678 C CG . GLU A 96 ? 0.6398 0.4102 0.4458 -0.2383 0.0752 -0.0001 94 GLU A CG 679 C CD . GLU A 96 ? 0.7700 0.4911 0.5492 -0.2450 0.1094 -0.0118 94 GLU A CD 680 O OE1 . GLU A 96 ? 0.9324 0.6124 0.6818 -0.2589 0.1292 -0.0240 94 GLU A OE1 681 O OE2 . GLU A 96 ? 0.8048 0.5248 0.5908 -0.2378 0.1194 -0.0100 94 GLU A OE2 682 N N . GLY A 97 ? 0.5117 0.3973 0.3689 -0.2309 0.0060 0.0251 95 GLY A N 683 C CA . GLY A 97 ? 0.5191 0.4221 0.3565 -0.2498 -0.0115 0.0269 95 GLY A CA 684 C C . GLY A 97 ? 0.4921 0.4461 0.3347 -0.2419 -0.0381 0.0386 95 GLY A C 685 O O . GLY A 97 ? 0.4815 0.4411 0.3254 -0.2242 -0.0413 0.0438 95 GLY A O 686 N N . ILE A 98 ? 0.4883 0.4781 0.3363 -0.2551 -0.0542 0.0430 96 ILE A N 687 C CA . ILE A 98 ? 0.4554 0.5041 0.3191 -0.2451 -0.0776 0.0559 96 ILE A CA 688 C C . ILE A 98 ? 0.4076 0.4903 0.3162 -0.2275 -0.0773 0.0624 96 ILE A C 689 O O . ILE A 98 ? 0.4243 0.5010 0.3472 -0.2353 -0.0684 0.0606 96 ILE A O 690 C CB . ILE A 98 ? 0.4778 0.5606 0.3260 -0.2725 -0.0970 0.0576 96 ILE A CB 691 C CG1 . ILE A 98 ? 0.5579 0.6004 0.3498 -0.2977 -0.0961 0.0470 96 ILE A CG1 692 C CG2 . ILE A 98 ? 0.4116 0.5618 0.2814 -0.2555 -0.1205 0.0744 96 ILE A CG2 693 C CD1 . ILE A 98 ? 0.6524 0.7423 0.4225 -0.3183 -0.1251 0.0529 96 ILE A CD1 694 N N . TYR A 99 ? 0.3800 0.4922 0.3052 -0.2029 -0.0848 0.0705 97 TYR A N 695 C CA . TYR A 99 ? 0.3593 0.5060 0.3190 -0.1853 -0.0843 0.0750 97 TYR A CA 696 C C . TYR A 99 ? 0.3710 0.5760 0.3465 -0.1789 -0.0994 0.0864 97 TYR A C 697 O O . TYR A 99 ? 0.4006 0.6162 0.3671 -0.1683 -0.1095 0.0937 97 TYR A O 698 C CB . TYR A 99 ? 0.3526 0.4785 0.3174 -0.1618 -0.0749 0.0709 97 TYR A CB 699 C CG . TYR A 99 ? 0.3768 0.4637 0.3414 -0.1663 -0.0607 0.0615 97 TYR A CG 700 C CD1 . TYR A 99 ? 0.3409 0.3851 0.2837 -0.1760 -0.0515 0.0556 97 TYR A CD1 701 C CD2 . TYR A 99 ? 0.3542 0.4522 0.3411 -0.1602 -0.0563 0.0597 97 TYR A CD2 702 C CE1 . TYR A 99 ? 0.3549 0.3720 0.3068 -0.1773 -0.0364 0.0485 97 TYR A CE1 703 C CE2 . TYR A 99 ? 0.3176 0.3920 0.3122 -0.1617 -0.0461 0.0547 97 TYR A CE2 704 C CZ . TYR A 99 ? 0.3541 0.3899 0.3356 -0.1692 -0.0352 0.0492 97 TYR A CZ 705 O OH . TYR A 99 ? 0.3668 0.3860 0.3646 -0.1680 -0.0225 0.0455 97 TYR A OH 706 N N . THR A 100 ? 0.3614 0.6070 0.3625 -0.1838 -0.0999 0.0903 98 THR A N 707 C CA . THR A 100 ? 0.3623 0.6736 0.3881 -0.1780 -0.1113 0.1015 98 THR A CA 708 C C . THR A 100 ? 0.3586 0.7016 0.4129 -0.1558 -0.1015 0.1045 98 THR A C 709 O O . THR A 100 ? 0.3430 0.6886 0.4045 -0.1643 -0.0919 0.1023 98 THR A O 710 C CB . THR A 100 ? 0.3655 0.7095 0.3966 -0.2123 -0.1202 0.1037 98 THR A CB 711 O OG1 . THR A 100 ? 0.3828 0.6812 0.3774 -0.2385 -0.1232 0.0948 98 THR A OG1 712 C CG2 . THR A 100 ? 0.3208 0.7405 0.3791 -0.2080 -0.1370 0.1165 98 THR A CG2 713 N N . CYS A 101 ? 0.3748 0.7378 0.4410 -0.1262 -0.1021 0.1103 99 CYS A N 714 C CA . CYS A 101 ? 0.3836 0.7770 0.4739 -0.1025 -0.0896 0.1114 99 CYS A CA 715 C C . CYS A 101 ? 0.3720 0.8431 0.4991 -0.1075 -0.0946 0.1236 99 CYS A C 716 O O . CYS A 101 ? 0.3934 0.9056 0.5359 -0.1062 -0.1102 0.1356 99 CYS A O 717 C CB . CYS A 101 ? 0.3997 0.7733 0.4869 -0.0671 -0.0835 0.1124 99 CYS A CB 718 S SG . CYS A 101 ? 0.5126 0.9011 0.6172 -0.0364 -0.0603 0.1066 99 CYS A SG 719 N N . GLU A 102 ? 0.3399 0.8350 0.4808 -0.1150 -0.0818 0.1219 100 GLU A N 720 C CA . GLU A 102 ? 0.3261 0.8995 0.5079 -0.1175 -0.0795 0.1327 100 GLU A CA 721 C C . GLU A 102 ? 0.3191 0.9084 0.5145 -0.0866 -0.0569 0.1303 100 GLU A C 722 O O . GLU A 102 ? 0.3331 0.8925 0.5069 -0.0896 -0.0420 0.1207 100 GLU A O 723 C CB . GLU A 102 ? 0.3263 0.9121 0.5092 -0.1571 -0.0778 0.1335 100 GLU A CB 724 C CG . GLU A 102 ? 0.4027 0.9607 0.5651 -0.1924 -0.0941 0.1312 100 GLU A CG 725 C CD . GLU A 102 ? 0.5131 1.0804 0.6786 -0.2324 -0.0881 0.1329 100 GLU A CD 726 O OE1 . GLU A 102 ? 0.5177 1.1186 0.7027 -0.2320 -0.0722 0.1385 100 GLU A OE1 727 O OE2 . GLU A 102 ? 0.6151 1.1506 0.7598 -0.2651 -0.0960 0.1281 100 GLU A OE2 728 N N . ILE A 103 ? 0.3041 0.9401 0.5331 -0.0559 -0.0537 0.1395 101 ILE A N 729 C CA . ILE A 103 ? 0.3103 0.9450 0.5455 -0.0200 -0.0275 0.1337 101 ILE A CA 730 C C . ILE A 103 ? 0.3345 1.0553 0.6248 -0.0013 -0.0152 0.1466 101 ILE A C 731 O O . ILE A 103 ? 0.3411 1.1251 0.6725 0.0013 -0.0322 0.1643 101 ILE A O 732 C CB . ILE A 103 ? 0.3321 0.9099 0.5471 0.0130 -0.0254 0.1292 101 ILE A CB 733 C CG1 . ILE A 103 ? 0.3873 0.9490 0.6005 0.0469 0.0062 0.1180 101 ILE A CG1 734 C CG2 . ILE A 103 ? 0.3247 0.9360 0.5662 0.0309 -0.0439 0.1496 101 ILE A CG2 735 C CD1 . ILE A 103 ? 0.4345 0.9235 0.6203 0.0743 0.0136 0.1101 101 ILE A CD1 736 N N . ARG A 104 ? 0.3525 1.0799 0.6435 0.0107 0.0148 0.1378 102 ARG A N 737 C CA . ARG A 104 ? 0.3670 1.1748 0.7120 0.0327 0.0358 0.1479 102 ARG A CA 738 C C . ARG A 104 ? 0.4130 1.1909 0.7460 0.0726 0.0717 0.1343 102 ARG A C 739 O O . ARG A 104 ? 0.4433 1.1581 0.7239 0.0659 0.0863 0.1138 102 ARG A O 740 C CB . ARG A 104 ? 0.3562 1.2206 0.7196 -0.0029 0.0437 0.1520 102 ARG A CB 741 C CG . ARG A 104 ? 0.3874 1.3457 0.8148 0.0179 0.0688 0.1631 102 ARG A CG 742 C CD . ARG A 104 ? 0.3784 1.4015 0.8319 -0.0235 0.0749 0.1708 102 ARG A CD 743 N NE . ARG A 104 ? 0.4055 1.3832 0.8084 -0.0403 0.1000 0.1583 102 ARG A NE 744 C CZ . ARG A 104 ? 0.4212 1.4001 0.8150 -0.0164 0.1379 0.1492 102 ARG A CZ 745 N NH1 . ARG A 104 ? 0.4546 1.4726 0.8902 0.0284 0.1595 0.1500 102 ARG A NH1 746 N NH2 . ARG A 104 ? 0.4438 1.3816 0.7828 -0.0359 0.1553 0.1399 102 ARG A NH2 747 N N . LEU A 105 ? 0.4440 1.2708 0.8270 0.1141 0.0863 0.1463 103 LEU A N 748 C CA . LEU A 105 ? 0.4955 1.2906 0.8706 0.1572 0.1261 0.1331 103 LEU A CA 749 C C . LEU A 105 ? 0.5143 1.3718 0.9175 0.1601 0.1616 0.1306 103 LEU A C 750 O O . LEU A 105 ? 0.4814 1.4281 0.9347 0.1405 0.1552 0.1473 103 LEU A O 751 C CB . LEU A 105 ? 0.5167 1.3175 0.9283 0.2086 0.1270 0.1497 103 LEU A CB 752 C CG . LEU A 105 ? 0.5133 1.2563 0.8961 0.2052 0.0929 0.1563 103 LEU A CG 753 C CD1 . LEU A 105 ? 0.5454 1.2711 0.9490 0.2612 0.1013 0.1725 103 LEU A CD1 754 C CD2 . LEU A 105 ? 0.5040 1.1438 0.8102 0.1774 0.0922 0.1284 103 LEU A CD2 755 N N . LYS A 106 ? 0.5692 1.3767 0.9360 0.1809 0.2010 0.1079 104 LYS A N 756 C CA . LYS A 106 ? 0.6200 1.4740 0.9991 0.1834 0.2417 0.1014 104 LYS A CA 757 C C . LYS A 106 ? 0.6267 1.5798 1.0962 0.2217 0.2613 0.1235 104 LYS A C 758 O O . LYS A 106 ? 0.6331 1.6001 1.1457 0.2608 0.2525 0.1398 104 LYS A O 759 C CB . LYS A 106 ? 0.6923 1.4637 1.0024 0.1967 0.2809 0.0682 104 LYS A CB 760 C CG . LYS A 106 ? 0.7851 1.5221 1.1078 0.2542 0.3157 0.0600 104 LYS A CG 761 C CD . LYS A 106 ? 0.8910 1.5657 1.1502 0.2614 0.3645 0.0244 104 LYS A CD 762 C CE . LYS A 106 ? 0.9839 1.6216 1.2586 0.3211 0.4090 0.0154 104 LYS A CE 763 N NZ . LYS A 106 ? 0.9977 1.5423 1.2441 0.3374 0.3945 0.0091 104 LYS A NZ 764 N N . ASN A 107 ? 0.6308 1.6565 1.1304 0.2103 0.2882 0.1265 105 ASN A N 765 C CA . ASN A 107 ? 0.6377 1.7730 1.2325 0.2441 0.3107 0.1476 105 ASN A CA 766 C C . ASN A 107 ? 0.5868 1.7972 1.2519 0.2430 0.2632 0.1793 105 ASN A C 767 O O . ASN A 107 ? 0.5980 1.8775 1.3387 0.2881 0.2677 0.2006 105 ASN A O 768 C CB . ASN A 107 ? 0.7039 1.8055 1.3053 0.3092 0.3574 0.1372 105 ASN A CB 769 C CG . ASN A 107 ? 0.7609 1.8868 1.3631 0.3205 0.4186 0.1217 105 ASN A CG 770 O OD1 . ASN A 107 ? 0.8030 1.8418 1.3379 0.3361 0.4569 0.0914 105 ASN A OD1 771 N ND2 . ASN A 107 ? 0.7789 2.0238 1.4552 0.3095 0.4294 0.1410 105 ASN A ND2 772 N N . GLU A 108 ? 0.5407 1.7359 1.1772 0.1917 0.2179 0.1822 106 GLU A N 773 C CA . GLU A 108 ? 0.4997 1.7496 1.1813 0.1809 0.1684 0.2068 106 GLU A CA 774 C C . GLU A 108 ? 0.4468 1.6995 1.1037 0.1121 0.1342 0.2063 106 GLU A C 775 O O . GLU A 108 ? 0.4532 1.6153 1.0339 0.0831 0.1300 0.1879 106 GLU A O 776 C CB . GLU A 108 ? 0.5158 1.6867 1.1649 0.2145 0.1482 0.2078 106 GLU A CB 777 C CG . GLU A 108 ? 0.5337 1.7404 1.2061 0.2020 0.0954 0.2308 106 GLU A CG 778 C CD . GLU A 108 ? 0.6173 1.7602 1.2697 0.2474 0.0842 0.2391 106 GLU A CD 779 O OE1 . GLU A 108 ? 0.7060 1.8427 1.3827 0.3061 0.1156 0.2446 106 GLU A OE1 780 O OE2 . GLU A 108 ? 0.5686 1.6640 1.1798 0.2248 0.0472 0.2408 106 GLU A OE2 781 N N . SER A 109 ? 0.4047 1.7627 1.1278 0.0863 0.1111 0.2265 107 SER A N 782 C CA . SER A 109 ? 0.3723 1.7405 1.0798 0.0179 0.0889 0.2250 107 SER A CA 783 C C . SER A 109 ? 0.3521 1.6979 1.0398 -0.0085 0.0379 0.2300 107 SER A C 784 O O . SER A 109 ? 0.3418 1.7023 1.0242 -0.0646 0.0171 0.2299 107 SER A O 785 C CB . SER A 109 ? 0.3691 1.8663 1.1579 -0.0074 0.0992 0.2397 107 SER A CB 786 O OG . SER A 109 ? 0.3448 1.9368 1.1998 -0.0131 0.0608 0.2599 107 SER A OG 787 N N . MET A 110 ? 0.3509 1.6552 1.0233 0.0314 0.0214 0.2336 108 MET A N 788 C CA . MET A 110 ? 0.3319 1.6119 0.9798 0.0129 -0.0245 0.2391 108 MET A CA 789 C C . MET A 110 ? 0.3011 1.4471 0.8586 0.0013 -0.0274 0.2183 108 MET A C 790 O O . MET A 110 ? 0.2720 1.3450 0.7942 0.0356 -0.0047 0.2068 108 MET A O 791 C CB . MET A 110 ? 0.3527 1.6734 1.0395 0.0647 -0.0414 0.2613 108 MET A CB 792 C CG . MET A 110 ? 0.3987 1.8012 1.1192 0.0402 -0.0894 0.2815 108 MET A CG 793 S SD . MET A 110 ? 0.5090 2.0886 1.3365 0.0142 -0.0960 0.3001 108 MET A SD 794 C CE . MET A 110 ? 0.4962 2.1307 1.3940 0.0846 -0.0448 0.3107 108 MET A CE 795 N N . VAL A 111 ? 0.2863 1.4030 0.8091 -0.0488 -0.0537 0.2126 109 VAL A N 796 C CA . VAL A 111 ? 0.2980 1.2982 0.7437 -0.0623 -0.0590 0.1953 109 VAL A CA 797 C C . VAL A 111 ? 0.3117 1.2846 0.7341 -0.0640 -0.0930 0.2003 109 VAL A C 798 O O . VAL A 111 ? 0.3418 1.3698 0.7838 -0.0924 -0.1206 0.2097 109 VAL A O 799 C CB . VAL A 111 ? 0.2948 1.2639 0.7095 -0.1162 -0.0568 0.1843 109 VAL A CB 800 C CG1 . VAL A 111 ? 0.2379 1.0945 0.5829 -0.1190 -0.0553 0.1683 109 VAL A CG1 801 C CG2 . VAL A 111 ? 0.2904 1.3025 0.7304 -0.1242 -0.0259 0.1848 109 VAL A CG2 802 N N . MET A 112 ? 0.3218 1.2086 0.6985 -0.0376 -0.0901 0.1928 110 MET A N 803 C CA . MET A 112 ? 0.3451 1.2000 0.6954 -0.0315 -0.1168 0.1997 110 MET A CA 804 C C . MET A 112 ? 0.3309 1.0999 0.6188 -0.0670 -0.1261 0.1832 110 MET A C 805 O O . MET A 112 ? 0.3262 1.0266 0.5808 -0.0702 -0.1080 0.1667 110 MET A O 806 C CB . MET A 112 ? 0.3787 1.1945 0.7231 0.0241 -0.1041 0.2055 110 MET A CB 807 C CG . MET A 112 ? 0.4768 1.3693 0.8841 0.0695 -0.0903 0.2237 110 MET A CG 808 S SD . MET A 112 ? 0.6086 1.5947 1.0632 0.0899 -0.1265 0.2597 110 MET A SD 809 C CE . MET A 112 ? 0.6513 1.5308 1.0412 0.1167 -0.1352 0.2647 110 MET A CE 810 N N . LYS A 113 ? 0.3469 1.1232 0.6191 -0.0920 -0.1545 0.1884 111 LYS A N 811 C CA . LYS A 113 ? 0.3612 1.0629 0.5775 -0.1283 -0.1617 0.1730 111 LYS A CA 812 C C . LYS A 113 ? 0.3836 1.0310 0.5579 -0.1130 -0.1742 0.1764 111 LYS A C 813 O O . LYS A 113 ? 0.3880 1.0686 0.5570 -0.1200 -0.2002 0.1889 111 LYS A O 814 C CB . LYS A 113 ? 0.3872 1.1318 0.6083 -0.1807 -0.1797 0.1709 111 LYS A CB 815 C CG . LYS A 113 ? 0.4374 1.1417 0.6412 -0.2193 -0.1639 0.1546 111 LYS A CG 816 C CD . LYS A 113 ? 0.5166 1.3025 0.7621 -0.2550 -0.1683 0.1591 111 LYS A CD 817 C CE . LYS A 113 ? 0.5818 1.3247 0.7967 -0.3103 -0.1649 0.1446 111 LYS A CE 818 N NZ . LYS A 113 ? 0.5766 1.4003 0.8322 -0.3515 -0.1696 0.1483 111 LYS A NZ 819 N N . LYS A 114 ? 0.3825 0.9480 0.5246 -0.0954 -0.1558 0.1652 112 LYS A N 820 C CA . LYS A 114 ? 0.3989 0.9038 0.5002 -0.0806 -0.1601 0.1678 112 LYS A CA 821 C C . LYS A 114 ? 0.3956 0.8211 0.4504 -0.1084 -0.1524 0.1481 112 LYS A C 822 O O . LYS A 114 ? 0.3759 0.7624 0.4283 -0.1088 -0.1329 0.1335 112 LYS A O 823 C CB . LYS A 114 ? 0.4010 0.8766 0.5088 -0.0339 -0.1409 0.1718 112 LYS A CB 824 C CG . LYS A 114 ? 0.4412 0.9890 0.6015 0.0005 -0.1378 0.1887 112 LYS A CG 825 C CD . LYS A 114 ? 0.5388 1.0395 0.6979 0.0439 -0.1112 0.1865 112 LYS A CD 826 C CE . LYS A 114 ? 0.6149 1.1781 0.8231 0.0877 -0.1061 0.2078 112 LYS A CE 827 N NZ . LYS A 114 ? 0.6774 1.1795 0.8775 0.1283 -0.0742 0.2014 112 LYS A NZ 828 N N . PRO A 115 ? 0.4117 0.8164 0.4292 -0.1317 -0.1673 0.1480 113 PRO A N 829 C CA . PRO A 115 ? 0.4119 0.7420 0.3880 -0.1550 -0.1560 0.1299 113 PRO A CA 830 C C . PRO A 115 ? 0.4342 0.7002 0.3750 -0.1368 -0.1473 0.1304 113 PRO A C 831 O O . PRO A 115 ? 0.4478 0.7218 0.3806 -0.1137 -0.1565 0.1476 113 PRO A O 832 C CB . PRO A 115 ? 0.4296 0.7739 0.3810 -0.1952 -0.1737 0.1268 113 PRO A CB 833 C CG . PRO A 115 ? 0.4477 0.8575 0.4084 -0.1844 -0.2001 0.1480 113 PRO A CG 834 C CD . PRO A 115 ? 0.4297 0.8883 0.4432 -0.1434 -0.1958 0.1632 113 PRO A CD 835 N N . VAL A 116 ? 0.4343 0.6388 0.3567 -0.1469 -0.1285 0.1134 114 VAL A N 836 C CA . VAL A 116 ? 0.4689 0.6095 0.3583 -0.1382 -0.1158 0.1106 114 VAL A CA 837 C C . VAL A 116 ? 0.4766 0.5670 0.3395 -0.1654 -0.1026 0.0935 114 VAL A C 838 O O . VAL A 116 ? 0.4647 0.5517 0.3463 -0.1765 -0.0931 0.0818 114 VAL A O 839 C CB . VAL A 116 ? 0.4460 0.5636 0.3538 -0.1112 -0.0984 0.1074 114 VAL A CB 840 C CG1 . VAL A 116 ? 0.4187 0.5392 0.3524 -0.1192 -0.0874 0.0920 114 VAL A CG1 841 C CG2 . VAL A 116 ? 0.5422 0.5945 0.4173 -0.1075 -0.0835 0.1047 114 VAL A CG2 842 N N . GLU A 117 ? 0.5061 0.5572 0.3242 -0.1742 -0.1004 0.0940 115 GLU A N 843 C CA . GLU A 117 ? 0.5232 0.5253 0.3142 -0.1986 -0.0834 0.0773 115 GLU A CA 844 C C . GLU A 117 ? 0.5047 0.4588 0.2983 -0.1873 -0.0584 0.0701 115 GLU A C 845 O O . GLU A 117 ? 0.5095 0.4460 0.2931 -0.1702 -0.0546 0.0787 115 GLU A O 846 C CB . GLU A 117 ? 0.5886 0.5749 0.3228 -0.2205 -0.0919 0.0784 115 GLU A CB 847 C CG . GLU A 117 ? 0.6640 0.6028 0.3686 -0.2494 -0.0725 0.0579 115 GLU A CG 848 C CD . GLU A 117 ? 0.8492 0.7810 0.4928 -0.2791 -0.0847 0.0546 115 GLU A CD 849 O OE1 . GLU A 117 ? 0.8768 0.8230 0.4876 -0.2737 -0.1032 0.0706 115 GLU A OE1 850 O OE2 . GLU A 117 ? 0.9583 0.8682 0.5836 -0.3085 -0.0757 0.0363 115 GLU A OE2 851 N N . LEU A 118 ? 0.4828 0.4173 0.2932 -0.1969 -0.0407 0.0555 116 LEU A N 852 C CA . LEU A 118 ? 0.4843 0.3878 0.3093 -0.1893 -0.0182 0.0478 116 LEU A CA 853 C C . LEU A 118 ? 0.5124 0.3732 0.3171 -0.2056 0.0048 0.0361 116 LEU A C 854 O O . LEU A 118 ? 0.5230 0.3803 0.3349 -0.2167 0.0112 0.0283 116 LEU A O 855 C CB . LEU A 118 ? 0.4432 0.3744 0.3192 -0.1792 -0.0177 0.0438 116 LEU A CB 856 C CG . LEU A 118 ? 0.3999 0.3153 0.2993 -0.1734 -0.0003 0.0358 116 LEU A CG 857 C CD1 . LEU A 118 ? 0.5153 0.4189 0.4050 -0.1620 0.0001 0.0394 116 LEU A CD1 858 C CD2 . LEU A 118 ? 0.2777 0.2255 0.2211 -0.1684 -0.0033 0.0322 116 LEU A CD2 859 N N . TRP A 119 ? 0.5275 0.3518 0.3062 -0.2058 0.0210 0.0358 117 TRP A N 860 C CA . TRP A 119 ? 0.5595 0.3416 0.3205 -0.2186 0.0500 0.0242 117 TRP A CA 861 C C . TRP A 119 ? 0.5375 0.3170 0.3433 -0.2108 0.0713 0.0183 117 TRP A C 862 O O . TRP A 119 ? 0.5384 0.3230 0.3582 -0.2018 0.0692 0.0227 117 TRP A O 863 C CB . TRP A 119 ? 0.6384 0.3824 0.3339 -0.2278 0.0560 0.0290 117 TRP A CB 864 C CG . TRP A 119 ? 0.6687 0.4221 0.3178 -0.2397 0.0325 0.0343 117 TRP A CG 865 C CD1 . TRP A 119 ? 0.6702 0.4475 0.2969 -0.2322 0.0043 0.0525 117 TRP A CD1 866 C CD2 . TRP A 119 ? 0.6624 0.4044 0.2835 -0.2628 0.0346 0.0212 117 TRP A CD2 867 N NE1 . TRP A 119 ? 0.6909 0.4823 0.2799 -0.2518 -0.0149 0.0516 117 TRP A NE1 868 C CE2 . TRP A 119 ? 0.7029 0.4684 0.2840 -0.2736 0.0040 0.0304 117 TRP A CE2 869 C CE3 . TRP A 119 ? 0.6030 0.3154 0.2293 -0.2750 0.0611 0.0025 117 TRP A CE3 870 C CZ2 . TRP A 119 ? 0.7142 0.4738 0.2565 -0.3028 -0.0020 0.0180 117 TRP A CZ2 871 C CZ3 . TRP A 119 ? 0.7344 0.4304 0.3200 -0.3000 0.0594 -0.0095 117 TRP A CZ3 872 C CH2 . TRP A 119 ? 0.7617 0.4809 0.3035 -0.3171 0.0273 -0.0035 117 TRP A CH2 873 N N . VAL A 120 ? 0.5325 0.3037 0.3616 -0.2151 0.0933 0.0081 118 VAL A N 874 C CA . VAL A 120 ? 0.5043 0.2881 0.3859 -0.2089 0.1108 0.0034 118 VAL A CA 875 C C . VAL A 120 ? 0.5504 0.2979 0.4198 -0.2180 0.1472 -0.0046 118 VAL A C 876 O O . VAL A 120 ? 0.5685 0.2909 0.4208 -0.2234 0.1663 -0.0116 118 VAL A O 877 C CB . VAL A 120 ? 0.4710 0.2911 0.4074 -0.1996 0.1055 0.0030 118 VAL A CB 878 C CG1 . VAL A 120 ? 0.4639 0.3056 0.4585 -0.1946 0.1238 -0.0009 118 VAL A CG1 879 C CG2 . VAL A 120 ? 0.4011 0.2594 0.3501 -0.1915 0.0730 0.0108 118 VAL A CG2 880 N N . LEU A 121 ? 0.5665 0.3073 0.4426 -0.2209 0.1597 -0.0045 119 LEU A N 881 C CA . LEU A 121 ? 0.6391 0.3483 0.5062 -0.2313 0.1980 -0.0110 119 LEU A CA 882 C C . LEU A 121 ? 0.6203 0.3669 0.5659 -0.2277 0.2166 -0.0178 119 LEU A C 883 O O . LEU A 121 ? 0.5763 0.3707 0.5753 -0.2200 0.1962 -0.0161 119 LEU A O 884 C CB . LEU A 121 ? 0.6938 0.3720 0.5236 -0.2394 0.2043 -0.0048 119 LEU A CB 885 C CG . LEU A 121 ? 0.7473 0.3993 0.5080 -0.2371 0.1807 0.0087 119 LEU A CG 886 C CD1 . LEU A 121 ? 0.6637 0.2700 0.3807 -0.2438 0.1983 0.0179 119 LEU A CD1 887 C CD2 . LEU A 121 ? 0.6835 0.3189 0.3916 -0.2426 0.1756 0.0078 119 LEU A CD2 888 N N . PRO A 122 ? 0.6737 0.4026 0.6268 -0.2332 0.2559 -0.0249 120 PRO A N 889 C CA . PRO A 122 ? 0.6725 0.4483 0.7098 -0.2281 0.2738 -0.0287 120 PRO A CA 890 C C . PRO A 122 ? 0.6827 0.4941 0.7620 -0.2374 0.2652 -0.0290 120 PRO A C 891 O O . PRO A 122 ? 0.7209 0.5006 0.7574 -0.2499 0.2624 -0.0279 120 PRO A O 892 C CB . PRO A 122 ? 0.7247 0.4664 0.7498 -0.2351 0.3233 -0.0364 120 PRO A CB 893 C CG . PRO A 122 ? 0.7723 0.4476 0.7017 -0.2423 0.3276 -0.0384 120 PRO A CG 894 C CD . PRO A 122 ? 0.7352 0.4045 0.6199 -0.2456 0.2868 -0.0291 120 PRO A CD 895 N N . GLU A 123 ? 0.6803 0.5565 0.8421 -0.2316 0.2615 -0.0300 121 GLU A N 896 C CA . GLU A 123 ? 0.6890 0.6084 0.8974 -0.2459 0.2514 -0.0343 121 GLU A CA 897 C C . GLU A 123 ? 0.7343 0.6224 0.9294 -0.2701 0.2852 -0.0410 121 GLU A C 898 O O . GLU A 123 ? 0.7801 0.6462 0.9709 -0.2733 0.3236 -0.0426 121 GLU A O 899 C CB . GLU A 123 ? 0.6621 0.6655 0.9654 -0.2376 0.2455 -0.0331 121 GLU A CB 900 C CG . GLU A 123 ? 0.6861 0.7455 1.0332 -0.2539 0.2208 -0.0391 121 GLU A CG 901 C CD . GLU A 123 ? 0.7187 0.8716 1.1625 -0.2484 0.2151 -0.0358 121 GLU A CD 902 O OE1 . GLU A 123 ? 0.7081 0.8808 1.1883 -0.2248 0.2296 -0.0255 121 GLU A OE1 903 O OE2 . GLU A 123 ? 0.7467 0.9534 1.2296 -0.2678 0.1963 -0.0433 121 GLU A OE2 904 N N . GLU A 124 ? 0.8504 0.4945 0.7719 -0.1903 -0.0281 0.0262 122 GLU A N 905 C CA . GLU A 124 ? 0.8517 0.5122 0.7587 -0.1888 -0.0343 0.0224 122 GLU A CA 906 C C . GLU A 124 ? 0.8210 0.4951 0.7716 -0.1747 -0.0304 0.0470 122 GLU A C 907 O O . GLU A 124 ? 0.8130 0.5017 0.7899 -0.1667 -0.0402 0.0763 122 GLU A O 908 C CB . GLU A 124 ? 0.8379 0.5180 0.7046 -0.1933 -0.0611 0.0254 122 GLU A CB 909 C CG . GLU A 124 ? 0.9001 0.5797 0.7280 -0.2034 -0.0654 0.0046 122 GLU A CG 910 C CD . GLU A 124 ? 0.9788 0.6700 0.7734 -0.2027 -0.0816 0.0063 122 GLU A CD 911 O OE1 . GLU A 124 ? 0.9940 0.6899 0.7865 -0.1982 -0.0940 0.0207 122 GLU A OE1 912 O OE2 . GLU A 124 ? 0.9909 0.6860 0.7606 -0.2082 -0.0805 -0.0059 122 GLU A OE2 913 N N . PRO A 125 ? 0.8085 0.4856 0.7673 -0.1732 -0.0165 0.0377 123 PRO A N 914 C CA . PRO A 125 ? 0.7845 0.4856 0.7919 -0.1598 -0.0122 0.0630 123 PRO A CA 915 C C . PRO A 125 ? 0.7402 0.4783 0.7366 -0.1646 -0.0426 0.0859 123 PRO A C 916 O O . PRO A 125 ? 0.7384 0.4754 0.6863 -0.1777 -0.0597 0.0745 123 PRO A O 917 C CB . PRO A 125 ? 0.7923 0.4904 0.7999 -0.1623 0.0102 0.0415 123 PRO A CB 918 C CG . PRO A 125 ? 0.7939 0.4816 0.7380 -0.1807 0.0012 0.0151 123 PRO A CG 919 C CD . PRO A 125 ? 0.8209 0.4912 0.7425 -0.1857 -0.0081 0.0083 123 PRO A CD 920 N N . ARG A 126 ? 0.7229 0.4948 0.7654 -0.1550 -0.0479 0.1190 124 ARG A N 921 C CA . ARG A 126 ? 0.7011 0.5138 0.7308 -0.1666 -0.0770 0.1396 124 ARG A CA 922 C C . ARG A 126 ? 0.6754 0.5105 0.7013 -0.1768 -0.0780 0.1343 124 ARG A C 923 O O . ARG A 126 ? 0.6484 0.4983 0.6403 -0.1958 -0.0974 0.1330 124 ARG A O 924 C CB . ARG A 126 ? 0.7148 0.5679 0.7917 -0.1572 -0.0871 0.1822 124 ARG A CB 925 C CG . ARG A 126 ? 0.7789 0.6445 0.8178 -0.1722 -0.1132 0.1916 124 ARG A CG 926 C CD . ARG A 126 ? 0.8501 0.7654 0.9286 -0.1674 -0.1271 0.2388 124 ARG A CD 927 N NE . ARG A 126 ? 0.8740 0.8547 0.9624 -0.1820 -0.1469 0.2600 124 ARG A NE 928 C CZ . ARG A 126 ? 0.9170 0.9439 1.0675 -0.1694 -0.1427 0.2890 124 ARG A CZ 929 N NH1 . ARG A 126 ? 0.9518 0.9587 1.1614 -0.1383 -0.1151 0.2990 124 ARG A NH1 930 N NH2 . ARG A 126 ? 0.9198 1.0148 1.0750 -0.1893 -0.1638 0.3072 124 ARG A NH2 931 N N . ASP A 127 ? 0.6747 0.5077 0.7343 -0.1660 -0.0531 0.1282 125 ASP A N 932 C CA . ASP A 127 ? 0.6753 0.5321 0.7382 -0.1754 -0.0488 0.1243 125 ASP A CA 933 C C . ASP A 127 ? 0.6717 0.4906 0.6781 -0.1883 -0.0416 0.0908 125 ASP A C 934 O O . ASP A 127 ? 0.6905 0.4733 0.6791 -0.1838 -0.0262 0.0687 125 ASP A O 935 C CB . ASP A 127 ? 0.6953 0.5767 0.8283 -0.1561 -0.0220 0.1370 125 ASP A CB 936 C CG . ASP A 127 ? 0.7430 0.6790 0.9407 -0.1421 -0.0324 0.1817 125 ASP A CG 937 O OD1 . ASP A 127 ? 0.7658 0.7549 0.9630 -0.1587 -0.0581 0.2019 125 ASP A OD1 938 O OD2 . ASP A 127 ? 0.7707 0.6979 1.0198 -0.1161 -0.0144 0.1980 125 ASP A OD2 939 N N . LEU A 128 ? 0.6549 0.4855 0.6333 -0.2072 -0.0533 0.0894 126 LEU A N 940 C CA . LEU A 128 ? 0.6389 0.4391 0.5655 -0.2196 -0.0489 0.0675 126 LEU A CA 941 C C . LEU A 128 ? 0.6332 0.4587 0.5694 -0.2333 -0.0412 0.0713 126 LEU A C 942 O O . LEU A 128 ? 0.6339 0.4940 0.5879 -0.2450 -0.0537 0.0878 126 LEU A O 943 C CB . LEU A 128 ? 0.6340 0.4100 0.5099 -0.2300 -0.0707 0.0641 126 LEU A CB 944 C CG . LEU A 128 ? 0.6639 0.4057 0.4873 -0.2377 -0.0695 0.0498 126 LEU A CG 945 C CD1 . LEU A 128 ? 0.6532 0.3772 0.4629 -0.2278 -0.0583 0.0347 126 LEU A CD1 946 C CD2 . LEU A 128 ? 0.6713 0.3918 0.4596 -0.2442 -0.0869 0.0507 126 LEU A CD2 947 N N . ARG A 129 ? 0.6415 0.4557 0.5662 -0.2351 -0.0199 0.0560 127 ARG A N 948 C CA . ARG A 129 ? 0.6585 0.4987 0.5937 -0.2489 -0.0083 0.0593 127 ARG A CA 949 C C . ARG A 129 ? 0.6827 0.4931 0.5577 -0.2670 -0.0089 0.0496 127 ARG A C 950 O O . ARG A 129 ? 0.6995 0.4850 0.5413 -0.2645 0.0006 0.0350 127 ARG A O 951 C CB . ARG A 129 ? 0.6619 0.5227 0.6427 -0.2363 0.0242 0.0526 127 ARG A CB 952 C CG . ARG A 129 ? 0.7256 0.5946 0.7629 -0.2103 0.0341 0.0592 127 ARG A CG 953 C CD . ARG A 129 ? 0.7757 0.7015 0.8815 -0.2016 0.0274 0.0908 127 ARG A CD 954 N NE . ARG A 129 ? 0.8538 0.7802 1.0124 -0.1734 0.0355 0.1039 127 ARG A NE 955 C CZ . ARG A 129 ? 0.8289 0.8062 1.0634 -0.1550 0.0383 0.1362 127 ARG A CZ 956 N NH1 . ARG A 129 ? 0.8098 0.8515 1.0791 -0.1640 0.0323 0.1570 127 ARG A NH1 957 N NH2 . ARG A 129 ? 0.8588 0.8252 1.1373 -0.1281 0.0476 0.1506 127 ARG A NH2 958 N N . VAL A 130 ? 0.6926 0.5075 0.5536 -0.2876 -0.0197 0.0597 128 VAL A N 959 C CA . VAL A 130 ? 0.7213 0.5031 0.5292 -0.3041 -0.0189 0.0574 128 VAL A CA 960 C C . VAL A 130 ? 0.7419 0.5466 0.5583 -0.3287 -0.0103 0.0656 128 VAL A C 961 O O . VAL A 130 ? 0.7180 0.5648 0.5756 -0.3377 -0.0138 0.0743 128 VAL A O 962 C CB . VAL A 130 ? 0.7317 0.4709 0.4994 -0.3070 -0.0392 0.0597 128 VAL A CB 963 C CG1 . VAL A 130 ? 0.6677 0.4012 0.4424 -0.2864 -0.0509 0.0550 128 VAL A CG1 964 C CG2 . VAL A 130 ? 0.7837 0.5272 0.5532 -0.3314 -0.0489 0.0669 128 VAL A CG2 965 N N . ARG A 131 ? 0.7785 0.5595 0.5550 -0.3413 0.0000 0.0656 129 ARG A N 966 C CA . ARG A 131 ? 0.8098 0.6061 0.5865 -0.3683 0.0111 0.0736 129 ARG A CA 967 C C . ARG A 131 ? 0.8168 0.5710 0.5581 -0.3905 -0.0012 0.0818 129 ARG A C 968 O O . ARG A 131 ? 0.8232 0.5249 0.5242 -0.3822 -0.0096 0.0829 129 ARG A O 969 C CB . ARG A 131 ? 0.8590 0.6538 0.6094 -0.3725 0.0329 0.0713 129 ARG A CB 970 C CG . ARG A 131 ? 0.9298 0.7711 0.7205 -0.3622 0.0568 0.0590 129 ARG A CG 971 C CD . ARG A 131 ? 1.0977 0.9894 0.9312 -0.3802 0.0721 0.0660 129 ARG A CD 972 N NE . ARG A 131 ? 1.1907 1.1308 1.0841 -0.3624 0.0955 0.0565 129 ARG A NE 973 C CZ . ARG A 131 ? 1.2973 1.2471 1.1873 -0.3589 0.1268 0.0404 129 ARG A CZ 974 N NH1 . ARG A 131 ? 1.3657 1.2889 1.1912 -0.3748 0.1342 0.0349 129 ARG A NH1 975 N NH2 . ARG A 131 ? 1.3330 1.3201 1.2848 -0.3397 0.1526 0.0307 129 ARG A NH2 976 N N . VAL A 132 ? 0.8101 0.5881 0.5690 -0.4195 0.0001 0.0870 130 VAL A N 977 C CA . VAL A 132 ? 0.8484 0.5790 0.5716 -0.4481 -0.0047 0.0904 130 VAL A CA 978 C C . VAL A 132 ? 0.8812 0.5468 0.5519 -0.4444 0.0042 0.0984 130 VAL A C 979 O O . VAL A 132 ? 0.8871 0.5630 0.5483 -0.4418 0.0183 0.1055 130 VAL A O 980 C CB . VAL A 132 ? 0.8718 0.6375 0.6136 -0.4891 0.0028 0.0951 130 VAL A CB 981 C CG1 . VAL A 132 ? 0.8875 0.5874 0.5852 -0.5211 0.0040 0.0950 130 VAL A CG1 982 C CG2 . VAL A 132 ? 0.8448 0.6860 0.6414 -0.4966 -0.0098 0.0943 130 VAL A CG2 983 N N . GLY A 133 ? 0.9025 0.5041 0.5403 -0.4437 -0.0028 0.0988 131 GLY A N 984 C CA . GLY A 133 ? 0.9514 0.4893 0.5456 -0.4364 0.0049 0.1140 131 GLY A CA 985 C C . GLY A 133 ? 0.9378 0.4637 0.5203 -0.3977 -0.0047 0.1160 131 GLY A C 986 O O . GLY A 133 ? 0.9821 0.4579 0.5349 -0.3847 -0.0032 0.1314 131 GLY A O 987 N N . ASP A 134 ? 0.8816 0.4555 0.4911 -0.3795 -0.0136 0.1027 132 ASP A N 988 C CA . ASP A 134 ? 0.8664 0.4384 0.4680 -0.3478 -0.0229 0.1014 132 ASP A CA 989 C C . ASP A 134 ? 0.8569 0.3875 0.4494 -0.3329 -0.0339 0.0989 132 ASP A C 990 O O . ASP A 134 ? 0.8714 0.3873 0.4713 -0.3453 -0.0370 0.0887 132 ASP A O 991 C CB . ASP A 134 ? 0.8328 0.4586 0.4683 -0.3354 -0.0258 0.0855 132 ASP A CB 992 C CG . ASP A 134 ? 0.9088 0.5735 0.5512 -0.3419 -0.0096 0.0835 132 ASP A CG 993 O OD1 . ASP A 134 ? 1.0836 0.7392 0.7005 -0.3576 0.0012 0.0963 132 ASP A OD1 994 O OD2 . ASP A 134 ? 0.9021 0.6033 0.5748 -0.3317 -0.0047 0.0693 132 ASP A OD2 995 N N . THR A 135 ? 0.8386 0.3578 0.4152 -0.3078 -0.0389 0.1076 133 THR A N 996 C CA . THR A 135 ? 0.8178 0.3164 0.3951 -0.2868 -0.0485 0.1025 133 THR A CA 997 C C . THR A 135 ? 0.7919 0.3376 0.3898 -0.2722 -0.0587 0.0887 133 THR A C 998 O O . THR A 135 ? 0.7960 0.3731 0.3919 -0.2674 -0.0580 0.0899 133 THR A O 999 C CB . THR A 135 ? 0.8359 0.2991 0.3909 -0.2661 -0.0473 0.1248 133 THR A CB 1000 O OG1 . THR A 135 ? 0.9048 0.3097 0.4440 -0.2777 -0.0339 0.1379 133 THR A OG1 1001 C CG2 . THR A 135 ? 0.8376 0.2931 0.4004 -0.2411 -0.0555 0.1185 133 THR A CG2 1002 N N . THR A 136 ? 0.7740 0.3221 0.3885 -0.2686 -0.0664 0.0748 134 THR A N 1003 C CA . THR A 136 ? 0.7352 0.3211 0.3724 -0.2572 -0.0739 0.0635 134 THR A CA 1004 C C . THR A 136 ? 0.7303 0.3053 0.3673 -0.2416 -0.0829 0.0584 134 THR A C 1005 O O . THR A 136 ? 0.7265 0.2807 0.3607 -0.2478 -0.0843 0.0531 134 THR A O 1006 C CB . THR A 136 ? 0.7161 0.3351 0.3857 -0.2699 -0.0738 0.0555 134 THR A CB 1007 O OG1 . THR A 136 ? 0.7226 0.3638 0.4141 -0.2565 -0.0809 0.0483 134 THR A OG1 1008 C CG2 . THR A 136 ? 0.7445 0.3514 0.4136 -0.2899 -0.0766 0.0545 134 THR A CG2 1009 N N . GLN A 137 ? 0.7255 0.3185 0.3636 -0.2251 -0.0874 0.0580 135 GLN A N 1010 C CA . GLN A 137 ? 0.7198 0.3129 0.3620 -0.2104 -0.0948 0.0533 135 GLN A CA 1011 C C . GLN A 137 ? 0.6779 0.2931 0.3442 -0.2151 -0.0993 0.0421 135 GLN A C 1012 O O . GLN A 137 ? 0.6720 0.3109 0.3579 -0.2207 -0.0965 0.0390 135 GLN A O 1013 C CB . GLN A 137 ? 0.7173 0.3313 0.3544 -0.1958 -0.0991 0.0581 135 GLN A CB 1014 C CG . GLN A 137 ? 0.7208 0.3460 0.3687 -0.1838 -0.1057 0.0516 135 GLN A CG 1015 C CD . GLN A 137 ? 0.7776 0.4310 0.4218 -0.1727 -0.1113 0.0582 135 GLN A CD 1016 O OE1 . GLN A 137 ? 0.8809 0.5332 0.5255 -0.1562 -0.1140 0.0674 135 GLN A OE1 1017 N NE2 . GLN A 137 ? 0.8403 0.5229 0.4817 -0.1833 -0.1115 0.0526 135 GLN A NE2 1018 N N . MET A 138 ? 0.6751 0.2820 0.3407 -0.2120 -0.1038 0.0379 136 MET A N 1019 C CA . MET A 138 ? 0.6600 0.2903 0.3455 -0.2155 -0.1099 0.0334 136 MET A CA 1020 C C . MET A 138 ? 0.6638 0.2988 0.3483 -0.2023 -0.1135 0.0299 136 MET A C 1021 O O . MET A 138 ? 0.6469 0.2638 0.3160 -0.1973 -0.1119 0.0268 136 MET A O 1022 C CB . MET A 138 ? 0.6737 0.3014 0.3564 -0.2338 -0.1125 0.0320 136 MET A CB 1023 C CG . MET A 138 ? 0.6931 0.3265 0.3822 -0.2504 -0.1096 0.0363 136 MET A CG 1024 S SD . MET A 138 ? 0.7938 0.4436 0.4816 -0.2798 -0.1169 0.0348 136 MET A SD 1025 C CE . MET A 138 ? 0.8390 0.4432 0.4869 -0.2818 -0.1119 0.0187 136 MET A CE 1026 N N . ARG A 139 ? 0.6636 0.3215 0.3660 -0.1978 -0.1149 0.0290 137 ARG A N 1027 C CA . ARG A 139 ? 0.6734 0.3416 0.3762 -0.1881 -0.1172 0.0260 137 ARG A CA 1028 C C . ARG A 139 ? 0.6593 0.3338 0.3670 -0.1910 -0.1208 0.0256 137 ARG A C 1029 O O . ARG A 139 ? 0.6378 0.3220 0.3590 -0.2002 -0.1236 0.0307 137 ARG A O 1030 C CB . ARG A 139 ? 0.6775 0.3640 0.3940 -0.1892 -0.1144 0.0215 137 ARG A CB 1031 C CG . ARG A 139 ? 0.8032 0.4918 0.5080 -0.1913 -0.1101 0.0197 137 ARG A CG 1032 C CD . ARG A 139 ? 0.9734 0.6688 0.6592 -0.1820 -0.1155 0.0263 137 ARG A CD 1033 N NE . ARG A 139 ? 1.0991 0.8218 0.7905 -0.1808 -0.1194 0.0217 137 ARG A NE 1034 C CZ . ARG A 139 ? 1.1807 0.9205 0.8690 -0.1687 -0.1254 0.0301 137 ARG A CZ 1035 N NH1 . ARG A 139 ? 1.1986 0.9224 0.8791 -0.1530 -0.1254 0.0440 137 ARG A NH1 1036 N NH2 . ARG A 139 ? 1.2462 1.0193 0.9429 -0.1724 -0.1290 0.0253 137 ARG A NH2 1037 N N . CYS A 140 ? 0.6583 0.3325 0.3562 -0.1825 -0.1202 0.0223 138 CYS A N 1038 C CA . CYS A 140 ? 0.6651 0.3500 0.3634 -0.1861 -0.1213 0.0205 138 CYS A CA 1039 C C . CYS A 140 ? 0.6681 0.3607 0.3633 -0.1731 -0.1170 0.0165 138 CYS A C 1040 O O . CYS A 140 ? 0.6951 0.3709 0.3797 -0.1611 -0.1104 0.0145 138 CYS A O 1041 C CB . CYS A 140 ? 0.6873 0.3592 0.3687 -0.1989 -0.1207 0.0173 138 CYS A CB 1042 S SG . CYS A 140 ? 0.8178 0.5142 0.4963 -0.2121 -0.1246 0.0192 138 CYS A SG 1043 N N . SER A 141 ? 0.6404 0.3587 0.3488 -0.1749 -0.1188 0.0173 139 SER A N 1044 C CA . SER A 141 ? 0.6299 0.3688 0.3424 -0.1645 -0.1150 0.0150 139 SER A CA 1045 C C . SER A 141 ? 0.6356 0.3991 0.3584 -0.1744 -0.1151 0.0155 139 SER A C 1046 O O . SER A 141 ? 0.6630 0.4257 0.3932 -0.1874 -0.1184 0.0208 139 SER A O 1047 C CB . SER A 141 ? 0.6328 0.3899 0.3542 -0.1557 -0.1182 0.0184 139 SER A CB 1048 O OG . SER A 141 ? 0.6014 0.3749 0.3339 -0.1699 -0.1219 0.0161 139 SER A OG 1049 N N . ILE A 142 ? 0.6265 0.4125 0.3532 -0.1667 -0.1095 0.0128 140 ILE A N 1050 C CA . ILE A 142 ? 0.6003 0.4165 0.3395 -0.1767 -0.1086 0.0141 140 ILE A CA 1051 C C . ILE A 142 ? 0.5990 0.4496 0.3547 -0.1703 -0.1100 0.0139 140 ILE A C 1052 O O . ILE A 142 ? 0.6256 0.4931 0.3865 -0.1518 -0.1062 0.0154 140 ILE A O 1053 C CB . ILE A 142 ? 0.6224 0.4495 0.3531 -0.1777 -0.0991 0.0108 140 ILE A CB 1054 C CG1 . ILE A 142 ? 0.6443 0.4487 0.3527 -0.1904 -0.0997 0.0113 140 ILE A CG1 1055 C CG2 . ILE A 142 ? 0.6258 0.4874 0.3709 -0.1900 -0.0972 0.0144 140 ILE A CG2 1056 C CD1 . ILE A 142 ? 0.6212 0.4452 0.3171 -0.2027 -0.0921 0.0104 140 ILE A CD1 1057 N N . GLN A 143 ? 0.5845 0.4471 0.3502 -0.1865 -0.1143 0.0129 141 GLN A N 1058 C CA . GLN A 143 ? 0.5669 0.4731 0.3453 -0.1900 -0.1179 0.0112 141 GLN A CA 1059 C C . GLN A 143 ? 0.5777 0.5243 0.3702 -0.1914 -0.1126 0.0125 141 GLN A C 1060 O O . GLN A 143 ? 0.5889 0.5276 0.3807 -0.2035 -0.1063 0.0121 141 GLN A O 1061 C CB . GLN A 143 ? 0.5710 0.4729 0.3512 -0.2145 -0.1190 0.0029 141 GLN A CB 1062 C CG . GLN A 143 ? 0.5761 0.4445 0.3445 -0.2133 -0.1207 -0.0001 141 GLN A CG 1063 C CD . GLN A 143 ? 0.5920 0.4797 0.3517 -0.1989 -0.1286 0.0052 141 GLN A CD 1064 O OE1 . GLN A 143 ? 0.5981 0.5346 0.3625 -0.2020 -0.1348 0.0073 141 GLN A OE1 1065 N NE2 . GLN A 143 ? 0.5312 0.3851 0.2795 -0.1845 -0.1287 0.0106 141 GLN A NE2 1066 N N . SER A 144 ? 0.5728 0.5677 0.3802 -0.1783 -0.1148 0.0174 142 SER A N 1067 C CA . SER A 144 ? 0.5742 0.6157 0.4012 -0.1732 -0.1070 0.0201 142 SER A CA 1068 C C . SER A 144 ? 0.5672 0.6812 0.4202 -0.1684 -0.1139 0.0288 142 SER A C 1069 O O . SER A 144 ? 0.5798 0.7080 0.4333 -0.1601 -0.1248 0.0371 142 SER A O 1070 C CB . SER A 144 ? 0.6002 0.6190 0.4227 -0.1466 -0.0936 0.0210 142 SER A CB 1071 O OG . SER A 144 ? 0.6316 0.7002 0.4781 -0.1349 -0.0819 0.0235 142 SER A OG 1072 N N . THR A 145 ? 0.5740 0.7415 0.4494 -0.1754 -0.1080 0.0296 143 THR A N 1073 C CA . THR A 145 ? 0.5631 0.8171 0.4709 -0.1714 -0.1152 0.0416 143 THR A CA 1074 C C . THR A 145 ? 0.5842 0.8661 0.5204 -0.1310 -0.1018 0.0548 143 THR A C 1075 O O . THR A 145 ? 0.5785 0.9392 0.5521 -0.1175 -0.1049 0.0712 143 THR A O 1076 C CB . THR A 145 ? 0.5534 0.8591 0.4740 -0.2090 -0.1157 0.0340 143 THR A CB 1077 O OG1 . THR A 145 ? 0.5273 0.8201 0.4501 -0.2111 -0.0984 0.0289 143 THR A OG1 1078 C CG2 . THR A 145 ? 0.5461 0.8169 0.4417 -0.2490 -0.1227 0.0183 143 THR A CG2 1079 N N . GLU A 146 ? 0.6204 0.8384 0.5397 -0.1129 -0.0852 0.0471 144 GLU A N 1080 C CA . GLU A 146 ? 0.6591 0.8836 0.6002 -0.0758 -0.0633 0.0518 144 GLU A CA 1081 C C . GLU A 146 ? 0.6909 0.8385 0.6111 -0.0494 -0.0539 0.0501 144 GLU A C 1082 O O . GLU A 146 ? 0.6803 0.7610 0.5613 -0.0658 -0.0563 0.0366 144 GLU A O 1083 C CB . GLU A 146 ? 0.6655 0.8937 0.6034 -0.0883 -0.0432 0.0367 144 GLU A CB 1084 C CG . GLU A 146 ? 0.6724 0.9618 0.6236 -0.1232 -0.0504 0.0362 144 GLU A CG 1085 C CD . GLU A 146 ? 0.7194 1.1082 0.7205 -0.1149 -0.0568 0.0532 144 GLU A CD 1086 O OE1 . GLU A 146 ? 0.7431 1.1687 0.7806 -0.0764 -0.0425 0.0652 144 GLU A OE1 1087 O OE2 . GLU A 146 ? 0.7359 1.1680 0.7413 -0.1480 -0.0748 0.0547 144 GLU A OE2 1088 N N . GLU A 147 ? 0.7219 0.8814 0.6720 -0.0088 -0.0421 0.0661 145 GLU A N 1089 C CA . GLU A 147 ? 0.7623 0.8455 0.6964 0.0164 -0.0295 0.0661 145 GLU A CA 1090 C C . GLU A 147 ? 0.7757 0.7986 0.6874 0.0184 0.0007 0.0397 145 GLU A C 1091 O O . GLU A 147 ? 0.7642 0.8110 0.6776 0.0075 0.0148 0.0249 145 GLU A O 1092 C CB . GLU A 147 ? 0.7988 0.9074 0.7757 0.0618 -0.0236 0.0970 145 GLU A CB 1093 C CG . GLU A 147 ? 0.8644 0.9953 0.8406 0.0599 -0.0531 0.1235 145 GLU A CG 1094 C CD . GLU A 147 ? 0.9903 1.1298 1.0031 0.1073 -0.0461 0.1606 145 GLU A CD 1095 O OE1 . GLU A 147 ? 1.0456 1.1279 1.0696 0.1404 -0.0143 0.1585 145 GLU A OE1 1096 O OE2 . GLU A 147 ? 1.0244 1.2272 1.0537 0.1100 -0.0709 0.1926 145 GLU A OE2 1097 N N . LYS A 148 ? 0.7916 0.7372 0.6785 0.0277 0.0104 0.0333 146 LYS A N 1098 C CA . LYS A 148 ? 0.8295 0.7108 0.6917 0.0295 0.0426 0.0062 146 LYS A CA 1099 C C . LYS A 148 ? 0.8096 0.6899 0.6352 -0.0090 0.0445 -0.0202 146 LYS A C 1100 O O . LYS A 148 ? 0.8502 0.7176 0.6665 -0.0084 0.0746 -0.0421 146 LYS A O 1101 C CB . LYS A 148 ? 0.8790 0.7732 0.7835 0.0708 0.0786 0.0088 146 LYS A CB 1102 C CG . LYS A 148 ? 0.9222 0.8222 0.8716 0.1159 0.0807 0.0432 146 LYS A CG 1103 C CD . LYS A 148 ? 1.0161 0.8187 0.9413 0.1262 0.0961 0.0385 146 LYS A CD 1104 C CE . LYS A 148 ? 1.0716 0.8752 1.0457 0.1764 0.1044 0.0785 146 LYS A CE 1105 N NZ . LYS A 148 ? 1.1621 0.9617 1.1840 0.2214 0.1499 0.0795 146 LYS A NZ 1106 N N . ARG A 149 ? 0.7501 0.6430 0.5551 -0.0420 0.0152 -0.0170 147 ARG A N 1107 C CA . ARG A 149 ? 0.7359 0.6369 0.5120 -0.0771 0.0142 -0.0317 147 ARG A CA 1108 C C . ARG A 149 ? 0.7450 0.5893 0.4724 -0.1027 0.0118 -0.0467 147 ARG A C 1109 O O . ARG A 149 ? 0.7530 0.5983 0.4511 -0.1275 0.0196 -0.0605 147 ARG A O 1110 C CB . ARG A 149 ? 0.6905 0.6402 0.4784 -0.0986 -0.0113 -0.0172 147 ARG A CB 1111 C CG . ARG A 149 ? 0.6676 0.6888 0.4983 -0.0872 -0.0083 -0.0066 147 ARG A CG 1112 C CD . ARG A 149 ? 0.7014 0.7434 0.5452 -0.0715 0.0236 -0.0179 147 ARG A CD 1113 N NE . ARG A 149 ? 0.7157 0.8355 0.5935 -0.0774 0.0236 -0.0092 147 ARG A NE 1114 C CZ . ARG A 149 ? 0.7477 0.8911 0.6124 -0.1065 0.0284 -0.0159 147 ARG A CZ 1115 N NH1 . ARG A 149 ? 0.7939 0.8937 0.6118 -0.1308 0.0322 -0.0286 147 ARG A NH1 1116 N NH2 . ARG A 149 ? 0.7376 0.9534 0.6362 -0.1137 0.0289 -0.0072 147 ARG A NH2 1117 N N . VAL A 150 ? 0.7442 0.5467 0.4631 -0.0990 0.0004 -0.0418 148 VAL A N 1118 C CA . VAL A 150 ? 0.7657 0.5200 0.4432 -0.1231 -0.0019 -0.0548 148 VAL A CA 1119 C C . VAL A 150 ? 0.8233 0.5353 0.4771 -0.1213 0.0306 -0.0815 148 VAL A C 1120 O O . VAL A 150 ? 0.8517 0.5401 0.5248 -0.0908 0.0538 -0.0850 148 VAL A O 1121 C CB . VAL A 150 ? 0.7503 0.4735 0.4275 -0.1206 -0.0199 -0.0430 148 VAL A CB 1122 C CG1 . VAL A 150 ? 0.7708 0.4494 0.4096 -0.1452 -0.0187 -0.0574 148 VAL A CG1 1123 C CG2 . VAL A 150 ? 0.7101 0.4680 0.4033 -0.1295 -0.0476 -0.0238 148 VAL A CG2 1124 N N . THR A 151 ? 0.8506 0.5542 0.4624 -0.1557 0.0334 -0.0993 149 THR A N 1125 C CA . THR A 151 ? 0.9151 0.5808 0.4932 -0.1661 0.0669 -0.1326 149 THR A CA 1126 C C . THR A 151 ? 0.9731 0.5835 0.5184 -0.1864 0.0654 -0.1453 149 THR A C 1127 O O . THR A 151 ? 1.0408 0.5943 0.5714 -0.1824 0.0960 -0.1700 149 THR A O 1128 C CB . THR A 151 ? 0.9177 0.6200 0.4621 -0.1997 0.0720 -0.1464 149 THR A CB 1129 O OG1 . THR A 151 ? 0.8693 0.6092 0.4405 -0.1797 0.0910 -0.1470 149 THR A OG1 1130 C CG2 . THR A 151 ? 0.9911 0.6541 0.4811 -0.2309 0.0968 -0.1837 149 THR A CG2 1131 N N . LYS A 152 ? 0.9557 0.5824 0.4931 -0.2081 0.0317 -0.1276 150 LYS A N 1132 C CA . LYS A 152 ? 1.0015 0.5932 0.5064 -0.2366 0.0264 -0.1383 150 LYS A CA 1133 C C . LYS A 152 ? 0.9642 0.5723 0.4868 -0.2394 -0.0087 -0.1092 150 LYS A C 1134 O O . LYS A 152 ? 0.9150 0.5698 0.4567 -0.2393 -0.0319 -0.0857 150 LYS A O 1135 C CB . LYS A 152 ? 1.0380 0.6479 0.4931 -0.2821 0.0309 -0.1601 150 LYS A CB 1136 C CG . LYS A 152 ? 1.0774 0.6794 0.4986 -0.3225 0.0166 -0.1660 150 LYS A CG 1137 C CD . LYS A 152 ? 1.1562 0.7922 0.5258 -0.3701 0.0194 -0.1848 150 LYS A CD 1138 C CE . LYS A 152 ? 1.2182 0.8644 0.5556 -0.4159 0.0008 -0.1872 150 LYS A CE 1139 N NZ . LYS A 152 ? 1.2846 0.9777 0.5682 -0.4674 -0.0008 -0.2015 150 LYS A NZ 1140 N N . VAL A 153 ? 0.9925 0.5576 0.5106 -0.2413 -0.0080 -0.1119 151 VAL A N 1141 C CA . VAL A 153 ? 0.9612 0.5388 0.4926 -0.2477 -0.0357 -0.0894 151 VAL A CA 1142 C C . VAL A 153 ? 1.0058 0.5613 0.5052 -0.2838 -0.0359 -0.1035 151 VAL A C 1143 O O . VAL A 153 ? 1.0445 0.5449 0.5226 -0.2896 -0.0117 -0.1270 151 VAL A O 1144 C CB . VAL A 153 ? 0.9468 0.5016 0.5092 -0.2143 -0.0370 -0.0730 151 VAL A CB 1145 C CG1 . VAL A 153 ? 0.8967 0.4627 0.4688 -0.2246 -0.0601 -0.0550 151 VAL A CG1 1146 C CG2 . VAL A 153 ? 0.9348 0.5211 0.5294 -0.1832 -0.0393 -0.0584 151 VAL A CG2 1147 N N . ASN A 154 ? 0.9833 0.5830 0.4835 -0.3079 -0.0619 -0.0874 152 ASN A N 1148 C CA . ASN A 154 ? 1.0132 0.6118 0.4871 -0.3475 -0.0672 -0.0968 152 ASN A CA 1149 C C . ASN A 154 ? 0.9618 0.5907 0.4640 -0.3501 -0.0925 -0.0691 152 ASN A C 1150 O O . ASN A 154 ? 0.9174 0.6001 0.4432 -0.3481 -0.1138 -0.0430 152 ASN A O 1151 C CB . ASN A 154 ? 1.0476 0.6876 0.4853 -0.3872 -0.0711 -0.1078 152 ASN A CB 1152 C CG . ASN A 154 ? 1.1394 0.8012 0.5532 -0.4339 -0.0836 -0.1118 152 ASN A CG 1153 O OD1 . ASN A 154 ? 1.2641 0.8790 0.6612 -0.4496 -0.0698 -0.1329 152 ASN A OD1 1154 N ND2 . ASN A 154 ? 1.1733 0.9099 0.5876 -0.4576 -0.1098 -0.0887 152 ASN A ND2 1155 N N . TRP A 155 ? 0.9617 0.5532 0.4629 -0.3545 -0.0865 -0.0745 153 TRP A N 1156 C CA . TRP A 155 ? 0.9021 0.5213 0.4293 -0.3600 -0.1053 -0.0523 153 TRP A CA 1157 C C . TRP A 155 ? 0.9339 0.5765 0.4372 -0.4080 -0.1120 -0.0611 153 TRP A C 1158 O O . TRP A 155 ? 0.9900 0.5883 0.4568 -0.4337 -0.0938 -0.0900 153 TRP A O 1159 C CB . TRP A 155 ? 0.8801 0.4519 0.4215 -0.3376 -0.0954 -0.0490 153 TRP A CB 1160 C CG . TRP A 155 ? 0.7960 0.3664 0.3664 -0.2955 -0.0964 -0.0333 153 TRP A CG 1161 C CD1 . TRP A 155 ? 0.7890 0.3264 0.3579 -0.2674 -0.0816 -0.0388 153 TRP A CD1 1162 C CD2 . TRP A 155 ? 0.6755 0.2825 0.2811 -0.2796 -0.1115 -0.0104 153 TRP A CD2 1163 N NE1 . TRP A 155 ? 0.7130 0.2711 0.3105 -0.2397 -0.0901 -0.0208 153 TRP A NE1 1164 C CE2 . TRP A 155 ? 0.6661 0.2613 0.2836 -0.2479 -0.1064 -0.0064 153 TRP A CE2 1165 C CE3 . TRP A 155 ? 0.6696 0.3198 0.3005 -0.2891 -0.1263 0.0067 153 TRP A CE3 1166 C CZ2 . TRP A 155 ? 0.6736 0.2938 0.3192 -0.2317 -0.1148 0.0085 153 TRP A CZ2 1167 C CZ3 . TRP A 155 ? 0.6714 0.3393 0.3350 -0.2672 -0.1308 0.0220 153 TRP A CZ3 1168 C CH2 . TRP A 155 ? 0.6746 0.3251 0.3414 -0.2417 -0.1246 0.0201 153 TRP A CH2 1169 N N . MET A 156 ? 0.9010 0.6149 0.4272 -0.4208 -0.1369 -0.0351 154 MET A N 1170 C CA . MET A 156 ? 0.9321 0.6900 0.4459 -0.4674 -0.1494 -0.0349 154 MET A CA 1171 C C . MET A 156 ? 0.8899 0.6788 0.4489 -0.4606 -0.1621 -0.0085 154 MET A C 1172 O O . MET A 156 ? 0.8479 0.6419 0.4488 -0.4225 -0.1655 0.0138 154 MET A O 1173 C CB . MET A 156 ? 0.9342 0.7676 0.4384 -0.4924 -0.1691 -0.0209 154 MET A CB 1174 C CG . MET A 156 ? 1.0106 0.8233 0.4626 -0.5093 -0.1546 -0.0507 154 MET A CG 1175 S SD . MET A 156 ? 1.1926 0.9459 0.5780 -0.5594 -0.1272 -0.1061 154 MET A SD 1176 C CE . MET A 156 ? 1.1469 0.9894 0.5200 -0.6241 -0.1547 -0.0958 154 MET A CE 1177 N N . PHE A 157 ? 0.9163 0.7263 0.4654 -0.5009 -0.1663 -0.0141 155 PHE A N 1178 C CA . PHE A 157 ? 0.8847 0.7364 0.4784 -0.5003 -0.1772 0.0106 155 PHE A CA 1179 C C . PHE A 157 ? 0.8864 0.8330 0.4909 -0.5414 -0.2007 0.0291 155 PHE A C 1180 O O . PHE A 157 ? 0.9083 0.8742 0.4687 -0.5868 -0.2051 0.0111 155 PHE A O 1181 C CB . PHE A 157 ? 0.9223 0.7117 0.5026 -0.5096 -0.1580 -0.0092 155 PHE A CB 1182 C CG . PHE A 157 ? 0.8939 0.7306 0.5148 -0.5181 -0.1661 0.0118 155 PHE A CG 1183 C CD1 . PHE A 157 ? 0.8994 0.7635 0.5744 -0.4782 -0.1703 0.0402 155 PHE A CD1 1184 C CD2 . PHE A 157 ? 0.9475 0.8024 0.5530 -0.5682 -0.1667 0.0011 155 PHE A CD2 1185 C CE1 . PHE A 157 ? 0.9368 0.8467 0.6527 -0.4841 -0.1733 0.0583 155 PHE A CE1 1186 C CE2 . PHE A 157 ? 0.9948 0.9005 0.6420 -0.5762 -0.1727 0.0215 155 PHE A CE2 1187 C CZ . PHE A 157 ? 0.9602 0.8944 0.6642 -0.5320 -0.1753 0.0507 155 PHE A CZ 1188 N N . SER A 158 ? 0.8582 0.8670 0.5228 -0.5253 -0.2142 0.0654 156 SER A N 1189 C CA . SER A 158 ? 0.8952 1.0038 0.5853 -0.5609 -0.2362 0.0899 156 SER A CA 1190 C C . SER A 158 ? 0.8865 1.0552 0.6563 -0.5273 -0.2441 0.1329 156 SER A C 1191 O O . SER A 158 ? 0.8605 1.0226 0.6672 -0.4803 -0.2417 0.1541 156 SER A O 1192 C CB . SER A 158 ? 0.9042 1.0827 0.5746 -0.5881 -0.2583 0.1033 156 SER A CB 1193 O OG . SER A 158 ? 0.8339 1.0492 0.5498 -0.5460 -0.2693 0.1435 156 SER A OG 1194 N N . SER A 159 ? 0.9305 1.1573 0.7287 -0.5529 -0.2504 0.1442 157 SER A N 1195 C CA . SER A 159 ? 0.9174 1.2333 0.7979 -0.5288 -0.2618 0.1922 157 SER A CA 1196 C C . SER A 159 ? 0.9650 1.3733 0.8540 -0.5447 -0.2906 0.2261 157 SER A C 1197 O O . SER A 159 ? 0.9952 1.4981 0.8905 -0.5889 -0.3121 0.2425 157 SER A O 1198 C CB . SER A 159 ? 0.9159 1.2803 0.8274 -0.5544 -0.2605 0.1966 157 SER A CB 1199 O OG . SER A 159 ? 0.9229 1.3280 0.7917 -0.6205 -0.2747 0.1810 157 SER A OG 1200 N N . GLY A 160 ? 0.9722 1.3558 0.8601 -0.5109 -0.2911 0.2380 158 GLY A N 1201 C CA . GLY A 160 ? 1.0209 1.4584 0.8829 -0.5320 -0.3137 0.2562 158 GLY A CA 1202 C C . GLY A 160 ? 1.0288 1.5696 0.9541 -0.5135 -0.3370 0.3218 158 GLY A C 1203 O O . GLY A 160 ? 1.0351 1.5593 0.9690 -0.4817 -0.3366 0.3424 158 GLY A O 1204 N N . SER A 161 ? 1.0469 1.6972 1.0181 -0.5347 -0.3570 0.3575 159 SER A N 1205 C CA . SER A 161 ? 1.0601 1.8315 1.0843 -0.5302 -0.3856 0.4257 159 SER A CA 1206 C C . SER A 161 ? 1.1191 2.0017 1.1152 -0.6006 -0.4157 0.4312 159 SER A C 1207 O O . SER A 161 ? 1.1253 2.0490 1.1424 -0.6255 -0.4170 0.4243 159 SER A O 1208 C CB . SER A 161 ? 1.0210 1.8351 1.1563 -0.4748 -0.3788 0.4780 159 SER A CB 1209 O OG . SER A 161 ? 1.0075 1.7100 1.1615 -0.4200 -0.3450 0.4579 159 SER A OG 1210 N N . HIS A 162 ? 1.1661 2.0987 1.1108 -0.6370 -0.4387 0.4413 160 HIS A N 1211 C CA . HIS A 162 ? 1.2252 2.2605 1.1226 -0.7161 -0.4671 0.4370 160 HIS A CA 1212 C C . HIS A 162 ? 1.2575 2.2202 1.0844 -0.7680 -0.4482 0.3599 160 HIS A C 1213 O O . HIS A 162 ? 1.2874 2.3273 1.1043 -0.8274 -0.4630 0.3531 160 HIS A O 1214 C CB . HIS A 162 ? 1.2225 2.4185 1.2065 -0.7207 -0.4979 0.5080 160 HIS A CB 1215 C CG . HIS A 162 ? 1.2219 2.5128 1.2600 -0.6890 -0.5232 0.5895 160 HIS A CG 1216 N ND1 . HIS A 162 ? 1.2431 2.7041 1.3087 -0.7253 -0.5645 0.6514 160 HIS A ND1 1217 C CD2 . HIS A 162 ? 1.1844 2.4245 1.2536 -0.6268 -0.5127 0.6219 160 HIS A CD2 1218 C CE1 . HIS A 162 ? 1.2372 2.7465 1.3512 -0.6825 -0.5782 0.7228 160 HIS A CE1 1219 N NE2 . HIS A 162 ? 1.2047 2.5771 1.3210 -0.6232 -0.5458 0.7045 160 HIS A NE2 1220 N N . THR A 163 ? 1.2438 2.0590 1.0249 -0.7451 -0.4146 0.3049 161 THR A N 1221 C CA . THR A 163 ? 1.2730 1.9959 0.9891 -0.7839 -0.3901 0.2340 161 THR A CA 1222 C C . THR A 163 ? 1.2873 1.8828 0.9257 -0.7795 -0.3635 0.1793 161 THR A C 1223 O O . THR A 163 ? 1.2530 1.7936 0.9043 -0.7249 -0.3535 0.1889 161 THR A O 1224 C CB . THR A 163 ? 1.2403 1.9119 1.0080 -0.7513 -0.3689 0.2273 161 THR A CB 1225 O OG1 . THR A 163 ? 1.1328 1.7710 0.9660 -0.6734 -0.3586 0.2590 161 THR A OG1 1226 C CG2 . THR A 163 ? 1.2433 2.0342 1.0611 -0.7863 -0.3887 0.2561 161 THR A CG2 1227 N N . GLU A 164 ? 1.3356 1.8867 0.8964 -0.8393 -0.3501 0.1213 162 GLU A N 1228 C CA . GLU A 164 ? 1.3559 1.7940 0.8406 -0.8438 -0.3217 0.0656 162 GLU A CA 1229 C C . GLU A 164 ? 1.3045 1.6130 0.8058 -0.7819 -0.2894 0.0456 162 GLU A C 1230 O O . GLU A 164 ? 1.2493 1.5526 0.8135 -0.7398 -0.2884 0.0709 162 GLU A O 1231 C CB . GLU A 164 ? 1.4391 1.8538 0.8422 -0.9241 -0.3086 0.0061 162 GLU A CB 1232 C CG . GLU A 164 ? 1.4808 2.0262 0.8493 -0.9970 -0.3400 0.0176 162 GLU A CG 1233 C CD . GLU A 164 ? 1.5306 2.1182 0.8730 -1.0761 -0.3438 -0.0092 162 GLU A CD 1234 O OE1 . GLU A 164 ? 1.4717 1.9668 0.8088 -1.0803 -0.3158 -0.0466 162 GLU A OE1 1235 O OE2 . GLU A 164 ? 1.5545 2.2731 0.8814 -1.1372 -0.3758 0.0096 162 GLU A OE2 1236 N N . GLU A 165 ? 1.3190 1.5281 0.7622 -0.7795 -0.2620 -0.0005 163 GLU A N 1237 C CA . GLU A 165 ? 1.2647 1.3606 0.7196 -0.7211 -0.2337 -0.0160 163 GLU A CA 1238 C C . GLU A 165 ? 1.3042 1.2878 0.7032 -0.7410 -0.1977 -0.0742 163 GLU A C 1239 O O . GLU A 165 ? 1.3843 1.3599 0.7229 -0.8000 -0.1880 -0.1129 163 GLU A O 1240 C CB . GLU A 165 ? 1.2375 1.3222 0.6951 -0.6786 -0.2333 -0.0029 163 GLU A CB 1241 C CG . GLU A 165 ? 1.2143 1.3958 0.7273 -0.6549 -0.2639 0.0569 163 GLU A CG 1242 C CD . GLU A 165 ? 1.2145 1.3702 0.7339 -0.6104 -0.2590 0.0692 163 GLU A CD 1243 O OE1 . GLU A 165 ? 1.1623 1.2421 0.7019 -0.5626 -0.2400 0.0607 163 GLU A OE1 1244 O OE2 . GLU A 165 ? 1.2377 1.4540 0.7405 -0.6266 -0.2745 0.0886 163 GLU A OE2 1245 N N . GLU A 166 ? 1.2471 1.1440 0.6680 -0.6909 -0.1766 -0.0783 164 GLU A N 1246 C CA . GLU A 166 ? 1.2793 1.0593 0.6602 -0.6919 -0.1393 -0.1230 164 GLU A CA 1247 C C . GLU A 166 ? 1.2093 0.9234 0.6010 -0.6299 -0.1225 -0.1226 164 GLU A C 1248 O O . GLU A 166 ? 1.1204 0.8646 0.5583 -0.5836 -0.1375 -0.0879 164 GLU A O 1249 C CB . GLU A 166 ? 1.2964 1.0359 0.6957 -0.6947 -0.1289 -0.1235 164 GLU A CB 1250 C CG . GLU A 166 ? 1.3309 1.1410 0.7330 -0.7526 -0.1456 -0.1190 164 GLU A CG 1251 C CD . GLU A 166 ? 1.3692 1.1303 0.7875 -0.7541 -0.1306 -0.1205 164 GLU A CD 1252 O OE1 . GLU A 166 ? 1.3227 1.0663 0.7850 -0.7008 -0.1296 -0.0943 164 GLU A OE1 1253 O OE2 . GLU A 166 ? 1.4588 1.1993 0.8431 -0.8121 -0.1184 -0.1487 164 GLU A OE2 1254 N N . THR A 167 ? 1.2402 0.8637 0.5910 -0.6311 -0.0888 -0.1620 165 THR A N 1255 C CA . THR A 167 ? 1.1922 0.7497 0.5550 -0.5735 -0.0688 -0.1629 165 THR A CA 1256 C C . THR A 167 ? 1.1700 0.6646 0.5604 -0.5391 -0.0561 -0.1523 165 THR A C 1257 O O . THR A 167 ? 1.2277 0.6534 0.5965 -0.5587 -0.0321 -0.1741 165 THR A O 1258 C CB . THR A 167 ? 1.2596 0.7475 0.5738 -0.5843 -0.0332 -0.2074 165 THR A CB 1259 O OG1 . THR A 167 ? 1.2584 0.8051 0.5471 -0.6056 -0.0430 -0.2144 165 THR A OG1 1260 C CG2 . THR A 167 ? 1.2382 0.6551 0.5741 -0.5235 -0.0096 -0.2048 165 THR A CG2 1261 N N . VAL A 168 ? 1.0723 0.5893 0.5080 -0.4902 -0.0705 -0.1188 166 VAL A N 1262 C CA . VAL A 168 ? 1.0473 0.5142 0.5060 -0.4560 -0.0600 -0.1055 166 VAL A CA 1263 C C . VAL A 168 ? 1.0969 0.4839 0.5411 -0.4264 -0.0303 -0.1217 166 VAL A C 1264 O O . VAL A 168 ? 1.1684 0.4799 0.5949 -0.4322 -0.0038 -0.1367 166 VAL A O 1265 C CB . VAL A 168 ? 0.9569 0.4731 0.4631 -0.4170 -0.0815 -0.0699 166 VAL A CB 1266 C CG1 . VAL A 168 ? 0.8695 0.3370 0.3907 -0.3832 -0.0697 -0.0578 166 VAL A CG1 1267 C CG2 . VAL A 168 ? 0.9089 0.5004 0.4398 -0.4399 -0.1055 -0.0505 166 VAL A CG2 1268 N N . LEU A 169 ? 1.0671 0.4734 0.5227 -0.3943 -0.0334 -0.1163 167 LEU A N 1269 C CA . LEU A 169 ? 1.0970 0.4448 0.5500 -0.3599 -0.0068 -0.1262 167 LEU A CA 1270 C C . LEU A 169 ? 1.0756 0.4563 0.5227 -0.3533 -0.0070 -0.1362 167 LEU A C 1271 O O . LEU A 169 ? 1.0144 0.4650 0.4722 -0.3587 -0.0327 -0.1220 167 LEU A O 1272 C CB . LEU A 169 ? 1.0603 0.3989 0.5495 -0.3117 -0.0104 -0.0956 167 LEU A CB 1273 C CG . LEU A 169 ? 1.0723 0.3712 0.5736 -0.2676 0.0113 -0.0928 167 LEU A CG 1274 C CD1 . LEU A 169 ? 1.0093 0.2832 0.5330 -0.2364 0.0126 -0.0639 167 LEU A CD1 1275 C CD2 . LEU A 169 ? 0.9513 0.3053 0.4710 -0.2444 -0.0006 -0.0864 167 LEU A CD2 1276 N N . SER A 170 ? 1.1322 0.4600 0.5648 -0.3406 0.0249 -0.1592 168 SER A N 1277 C CA . SER A 170 ? 1.1502 0.5053 0.5768 -0.3331 0.0311 -0.1709 168 SER A CA 1278 C C . SER A 170 ? 1.2041 0.5076 0.6438 -0.2919 0.0650 -0.1791 168 SER A C 1279 O O . SER A 170 ? 1.2647 0.4924 0.6998 -0.2837 0.0955 -0.1913 168 SER A O 1280 C CB . SER A 170 ? 1.1954 0.5647 0.5731 -0.3868 0.0368 -0.2041 168 SER A CB 1281 O OG . SER A 170 ? 1.3241 0.6139 0.6678 -0.4059 0.0767 -0.2433 168 SER A OG 1282 N N . TYR A 171 ? 1.1953 0.5431 0.6556 -0.2654 0.0600 -0.1693 169 TYR A N 1283 C CA . TYR A 171 ? 1.2475 0.5686 0.7294 -0.2238 0.0899 -0.1729 169 TYR A CA 1284 C C . TYR A 171 ? 1.2606 0.6265 0.7338 -0.2287 0.0959 -0.1879 169 TYR A C 1285 O O . TYR A 171 ? 1.2096 0.6410 0.6783 -0.2475 0.0668 -0.1770 169 TYR A O 1286 C CB . TYR A 171 ? 1.2045 0.5452 0.7362 -0.1761 0.0746 -0.1330 169 TYR A CB 1287 C CG . TYR A 171 ? 1.2525 0.5941 0.8172 -0.1312 0.0977 -0.1274 169 TYR A CG 1288 C CD1 . TYR A 171 ? 1.3704 0.6471 0.9518 -0.0994 0.1322 -0.1266 169 TYR A CD1 1289 C CD2 . TYR A 171 ? 1.2237 0.6330 0.8075 -0.1200 0.0864 -0.1200 169 TYR A CD2 1290 C CE1 . TYR A 171 ? 1.3906 0.6773 1.0115 -0.0543 0.1540 -0.1167 169 TYR A CE1 1291 C CE2 . TYR A 171 ? 1.2757 0.6972 0.8949 -0.0802 0.1072 -0.1135 169 TYR A CE2 1292 C CZ . TYR A 171 ? 1.3528 0.7165 0.9929 -0.0457 0.1406 -0.1110 169 TYR A CZ 1293 O OH . TYR A 171 ? 1.4119 0.7963 1.0962 -0.0021 0.1620 -0.0998 169 TYR A OH 1294 N N . ASP A 172 ? 1.3498 0.6789 0.8241 -0.2098 0.1365 -0.2106 170 ASP A N 1295 C CA . ASP A 172 ? 1.3938 0.7598 0.8555 -0.2169 0.1512 -0.2307 170 ASP A CA 1296 C C . ASP A 172 ? 1.4620 0.8020 0.9560 -0.1715 0.1931 -0.2385 170 ASP A C 1297 O O . ASP A 172 ? 1.5589 0.8309 1.0356 -0.1727 0.2392 -0.2731 170 ASP A O 1298 C CB . ASP A 172 ? 1.4558 0.8095 0.8529 -0.2754 0.1641 -0.2725 170 ASP A CB 1299 C CG . ASP A 172 ? 1.5152 0.9117 0.8905 -0.2896 0.1794 -0.2936 170 ASP A CG 1300 O OD1 . ASP A 172 ? 1.4876 0.9530 0.8881 -0.2750 0.1562 -0.2665 170 ASP A OD1 1301 O OD2 . ASP A 172 ? 1.6428 1.0029 0.9725 -0.3194 0.2169 -0.3394 170 ASP A OD2 1302 N N . SER A 173 ? 1.4286 0.8258 0.9714 -0.1334 0.1782 -0.2067 171 SER A N 1303 C CA . SER A 173 ? 1.4696 0.8659 1.0582 -0.0843 0.2116 -0.2029 171 SER A CA 1304 C C . SER A 173 ? 1.5644 0.9345 1.1264 -0.0963 0.2602 -0.2484 171 SER A C 1305 O O . SER A 173 ? 1.6392 0.9537 1.2216 -0.0651 0.3074 -0.2632 171 SER A O 1306 C CB . SER A 173 ? 1.3907 0.8770 1.0226 -0.0619 0.1843 -0.1699 171 SER A CB 1307 O OG . SER A 173 ? 1.3268 0.8337 0.9911 -0.0418 0.1495 -0.1295 171 SER A OG 1308 N N . ASN A 174 ? 1.5750 0.9875 1.0920 -0.1417 0.2495 -0.2686 172 ASN A N 1309 C CA . ASN A 174 ? 1.6677 1.0630 1.1415 -0.1689 0.2924 -0.3173 172 ASN A CA 1310 C C . ASN A 174 ? 1.7901 1.0809 1.2434 -0.1701 0.3435 -0.3570 172 ASN A C 1311 O O . ASN A 174 ? 1.8644 1.1202 1.3199 -0.1558 0.3983 -0.3905 172 ASN A O 1312 C CB . ASN A 174 ? 1.6546 1.0966 1.0657 -0.2324 0.2642 -0.3294 172 ASN A CB 1313 C CG . ASN A 174 ? 1.7749 1.1860 1.1199 -0.2783 0.3052 -0.3860 172 ASN A CG 1314 O OD1 . ASN A 174 ? 1.8386 1.2709 1.1763 -0.2776 0.3381 -0.4090 172 ASN A OD1 1315 N ND2 . ASN A 174 ? 1.8344 1.2009 1.1280 -0.3234 0.3037 -0.4103 172 ASN A ND2 1316 N N . MET A 175 ? 1.8156 1.0547 1.2528 -0.1858 0.3283 -0.3527 173 MET A N 1317 C CA . MET A 175 ? 1.9337 1.0641 1.3472 -0.1950 0.3747 -0.3895 173 MET A CA 1318 C C . MET A 175 ? 1.9539 1.0215 1.4286 -0.1335 0.3948 -0.3607 173 MET A C 1319 O O . MET A 175 ? 1.8714 0.9856 1.4028 -0.0887 0.3638 -0.3088 173 MET A O 1320 C CB . MET A 175 ? 1.9526 1.0622 1.3069 -0.2578 0.3508 -0.4053 173 MET A CB 1321 C CG . MET A 175 ? 1.9882 1.1374 1.2708 -0.3257 0.3489 -0.4455 173 MET A CG 1322 S SD . MET A 175 ? 2.0487 1.1742 1.2618 -0.4043 0.3305 -0.4707 173 MET A SD 1323 C CE . MET A 175 ? 2.1871 1.1742 1.3685 -0.4181 0.4093 -0.5356 173 MET A CE 1324 N N . ARG A 176 ? 2.0691 1.0297 1.5286 -0.1359 0.4484 -0.3955 174 ARG A N 1325 C CA . ARG A 176 ? 2.1128 0.9974 1.6293 -0.0767 0.4800 -0.3700 174 ARG A CA 1326 C C . ARG A 176 ? 2.0681 0.9458 1.5984 -0.0719 0.4366 -0.3239 174 ARG A C 1327 O O . ARG A 176 ? 1.9705 0.9211 1.5442 -0.0394 0.3920 -0.2708 174 ARG A O 1328 C CB . ARG A 176 ? 2.2530 1.0113 1.7444 -0.0868 0.5545 -0.4238 174 ARG A CB 1329 C CG . ARG A 176 ? 2.3103 1.0648 1.7918 -0.0862 0.6093 -0.4730 174 ARG A CG 1330 C CD . ARG A 176 ? 2.4600 1.0771 1.9253 -0.0889 0.6906 -0.5255 174 ARG A CD 1331 N NE . ARG A 176 ? 2.5346 1.1470 1.9779 -0.0994 0.7469 -0.5830 174 ARG A NE 1332 C CZ . ARG A 176 ? 2.6656 1.1644 2.1010 -0.0953 0.8302 -0.6362 174 ARG A CZ 1333 N NH1 . ARG A 176 ? 2.7578 1.1316 2.2077 -0.0799 0.8677 -0.6369 174 ARG A NH1 1334 N NH2 . ARG A 176 ? 2.7139 1.2212 2.1268 -0.1074 0.8797 -0.6895 174 ARG A NH2 1335 N N . SER A 177 ? 2.1446 0.9354 1.6347 -0.1089 0.4521 -0.3472 175 SER A N 1336 C CA . SER A 177 ? 2.1146 0.8912 1.6110 -0.1118 0.4169 -0.3086 175 SER A CA 1337 C C . SER A 177 ? 2.0225 0.8867 1.4847 -0.1607 0.3537 -0.3010 175 SER A C 1338 O O . SER A 177 ? 2.0459 0.8857 1.4641 -0.2133 0.3425 -0.3184 175 SER A O 1339 C CB . SER A 177 ? 2.2319 0.8814 1.6992 -0.1370 0.4605 -0.3370 175 SER A CB 1340 O OG . SER A 177 ? 2.3324 0.8912 1.8382 -0.0865 0.5235 -0.3397 175 SER A OG 1341 N N . GLY A 178 ? 1.9184 0.8851 1.4068 -0.1411 0.3146 -0.2725 176 GLY A N 1342 C CA . GLY A 178 ? 1.8248 0.8797 1.2871 -0.1817 0.2618 -0.2672 176 GLY A CA 1343 C C . GLY A 178 ? 1.7726 0.8392 1.2284 -0.2036 0.2212 -0.2418 176 GLY A C 1344 O O . GLY A 178 ? 1.7315 0.8526 1.1591 -0.2464 0.1874 -0.2459 176 GLY A O 1345 N N . LYS A 179 ? 1.7733 0.7923 1.2574 -0.1734 0.2257 -0.2128 177 LYS A N 1346 C CA . LYS A 179 ? 1.7151 0.7478 1.1978 -0.1896 0.1900 -0.1856 177 LYS A CA 1347 C C . LYS A 179 ? 1.7350 0.7232 1.1677 -0.2504 0.1976 -0.2190 177 LYS A C 1348 O O . LYS A 179 ? 1.8335 0.7329 1.2445 -0.2637 0.2411 -0.2499 177 LYS A O 1349 C CB . LYS A 179 ? 1.7383 0.7334 1.2609 -0.1429 0.1955 -0.1435 177 LYS A CB 1350 C CG . LYS A 179 ? 1.7127 0.7740 1.2861 -0.0893 0.1760 -0.1018 177 LYS A CG 1351 C CD . LYS A 179 ? 1.7808 0.8144 1.3875 -0.0500 0.1772 -0.0556 177 LYS A CD 1352 C CE . LYS A 179 ? 1.7191 0.8434 1.3641 -0.0167 0.1407 -0.0120 177 LYS A CE 1353 N NZ . LYS A 179 ? 1.7307 0.8465 1.3930 0.0041 0.1296 0.0341 177 LYS A NZ 1354 N N . PHE A 180 ? 1.6432 0.6947 1.0605 -0.2878 0.1570 -0.2126 178 PHE A N 1355 C CA . PHE A 180 ? 1.6739 0.7041 1.0490 -0.3491 0.1569 -0.2383 178 PHE A CA 1356 C C . PHE A 180 ? 1.6037 0.6783 0.9908 -0.3632 0.1184 -0.2075 178 PHE A C 1357 O O . PHE A 180 ? 1.5208 0.6819 0.9206 -0.3664 0.0800 -0.1884 178 PHE A O 1358 C CB . PHE A 180 ? 1.6859 0.7604 1.0175 -0.4005 0.1524 -0.2753 178 PHE A CB 1359 C CG . PHE A 180 ? 1.7452 0.8201 1.0358 -0.4685 0.1455 -0.2977 178 PHE A CG 1360 C CD1 . PHE A 180 ? 1.8578 0.8420 1.1101 -0.5052 0.1872 -0.3394 178 PHE A CD1 1361 C CD2 . PHE A 180 ? 1.6811 0.8471 0.9750 -0.4962 0.0995 -0.2762 178 PHE A CD2 1362 C CE1 . PHE A 180 ? 1.8994 0.8904 1.1133 -0.5741 0.1802 -0.3613 178 PHE A CE1 1363 C CE2 . PHE A 180 ? 1.7370 0.9160 0.9986 -0.5600 0.0917 -0.2936 178 PHE A CE2 1364 C CZ . PHE A 180 ? 1.7996 0.8942 1.0194 -0.6015 0.1306 -0.3369 178 PHE A CZ 1365 N N . GLN A 181 ? 1.6552 0.6659 1.0380 -0.3736 0.1332 -0.2043 179 GLN A N 1366 C CA . GLN A 181 ? 1.6120 0.6574 1.0057 -0.3888 0.1040 -0.1775 179 GLN A CA 1367 C C . GLN A 181 ? 1.6509 0.6983 1.0076 -0.4577 0.1028 -0.2058 179 GLN A C 1368 O O . GLN A 181 ? 1.7366 0.7083 1.0591 -0.4913 0.1372 -0.2409 179 GLN A O 1369 C CB . GLN A 181 ? 1.6363 0.6234 1.0535 -0.3533 0.1170 -0.1460 179 GLN A CB 1370 C CG . GLN A 181 ? 1.6208 0.6117 1.0737 -0.2882 0.1195 -0.1180 179 GLN A CG 1371 C CD . GLN A 181 ? 1.6330 0.6171 1.1135 -0.2544 0.1117 -0.0725 179 GLN A CD 1372 O OE1 . GLN A 181 ? 1.7131 0.6460 1.1841 -0.2711 0.1233 -0.0645 179 GLN A OE1 1373 N NE2 . GLN A 181 ? 1.5848 0.6242 1.0971 -0.2106 0.0921 -0.0420 179 GLN A NE2 1374 N N . SER A 182 ? 1.5874 0.7258 0.9544 -0.4784 0.0637 -0.1893 180 SER A N 1375 C CA . SER A 182 ? 1.6200 0.8017 0.9595 -0.5442 0.0509 -0.2095 180 SER A CA 1376 C C . SER A 182 ? 1.7267 0.8259 1.0255 -0.5939 0.0852 -0.2462 180 SER A C 1377 O O . SER A 182 ? 1.7977 0.8896 1.0533 -0.6423 0.0988 -0.2874 180 SER A O 1378 C CB . SER A 182 ? 1.5518 0.8114 0.9238 -0.5494 0.0154 -0.1749 180 SER A CB 1379 O OG . SER A 182 ? 1.5957 0.9139 0.9500 -0.6109 -0.0004 -0.1877 180 SER A OG 1380 N N . LEU A 183 ? 1.7499 0.7871 1.0605 -0.5847 0.1000 -0.2312 181 LEU A N 1381 C CA . LEU A 183 ? 1.8521 0.8055 1.1289 -0.6348 0.1330 -0.2605 181 LEU A CA 1382 C C . LEU A 183 ? 1.8437 0.8699 1.1044 -0.7055 0.1092 -0.2710 181 LEU A C 1383 O O . LEU A 183 ? 1.9229 0.8995 1.1526 -0.7618 0.1310 -0.2984 181 LEU A O 1384 C CB . LEU A 183 ? 1.9502 0.8118 1.1862 -0.6503 0.1791 -0.3099 181 LEU A CB 1385 C CG . LEU A 183 ? 2.0708 0.7966 1.2971 -0.6517 0.2280 -0.3197 181 LEU A CG 1386 C CD1 . LEU A 183 ? 2.0400 0.7110 1.3074 -0.5687 0.2438 -0.2824 181 LEU A CD1 1387 C CD2 . LEU A 183 ? 2.1989 0.8345 1.3714 -0.7050 0.2768 -0.3834 181 LEU A CD2 1388 N N . GLY A 184 ? 1.7508 0.8972 1.0362 -0.7018 0.0653 -0.2470 182 GLY A N 1389 C CA . GLY A 184 ? 1.7352 0.9738 1.0222 -0.7577 0.0366 -0.2432 182 GLY A CA 1390 C C . GLY A 184 ? 1.6772 0.9489 1.0096 -0.7380 0.0198 -0.2019 182 GLY A C 1391 O O . GLY A 184 ? 1.7290 0.9325 1.0578 -0.7468 0.0417 -0.2009 182 GLY A O 1392 N N . ARG A 185 ? 1.5741 0.9483 0.9493 -0.7111 -0.0163 -0.1674 183 ARG A N 1393 C CA . ARG A 185 ? 1.5108 0.9246 0.9309 -0.6910 -0.0300 -0.1306 183 ARG A CA 1394 C C . ARG A 185 ? 1.4685 0.8277 0.9071 -0.6236 -0.0199 -0.1091 183 ARG A C 1395 O O . ARG A 185 ? 1.4464 0.8211 0.9151 -0.6006 -0.0248 -0.0810 183 ARG A O 1396 C CB . ARG A 185 ? 1.4291 0.9720 0.8918 -0.6895 -0.0674 -0.1034 183 ARG A CB 1397 C CG . ARG A 185 ? 1.4152 1.0081 0.9209 -0.6898 -0.0760 -0.0750 183 ARG A CG 1398 C CD . ARG A 185 ? 1.3823 1.1016 0.9365 -0.6873 -0.1082 -0.0476 183 ARG A CD 1399 N NE . ARG A 185 ? 1.4453 1.2313 0.9822 -0.7425 -0.1249 -0.0600 183 ARG A NE 1400 C CZ . ARG A 185 ? 1.4093 1.3107 0.9832 -0.7456 -0.1549 -0.0343 183 ARG A CZ 1401 N NH1 . ARG A 185 ? 1.3268 1.2800 0.9600 -0.6945 -0.1675 0.0025 183 ARG A NH1 1402 N NH2 . ARG A 185 ? 1.4516 1.4172 1.0026 -0.8014 -0.1709 -0.0445 183 ARG A NH2 1403 N N . PHE A 186 ? 1.4684 0.7702 0.8884 -0.5942 -0.0053 -0.1227 184 PHE A N 1404 C CA . PHE A 186 ? 1.4296 0.6886 0.8672 -0.5318 0.0028 -0.1013 184 PHE A CA 1405 C C . PHE A 186 ? 1.5246 0.6691 0.9340 -0.5245 0.0404 -0.1184 184 PHE A C 1406 O O . PHE A 186 ? 1.5393 0.6490 0.9483 -0.4858 0.0521 -0.1213 184 PHE A O 1407 C CB . PHE A 186 ? 1.3532 0.6676 0.8112 -0.4921 -0.0174 -0.0912 184 PHE A CB 1408 C CG . PHE A 186 ? 1.2152 0.6347 0.6987 -0.5057 -0.0494 -0.0784 184 PHE A CG 1409 C CD1 . PHE A 186 ? 1.0939 0.5643 0.6160 -0.4897 -0.0646 -0.0497 184 PHE A CD1 1410 C CD2 . PHE A 186 ? 1.1406 0.6090 0.6104 -0.5349 -0.0619 -0.0933 184 PHE A CD2 1411 C CE1 . PHE A 186 ? 1.0206 0.5838 0.5745 -0.4973 -0.0893 -0.0346 184 PHE A CE1 1412 C CE2 . PHE A 186 ? 1.0784 0.6459 0.5780 -0.5437 -0.0911 -0.0732 184 PHE A CE2 1413 C CZ . PHE A 186 ? 1.0035 0.6159 0.5489 -0.5224 -0.1036 -0.0431 184 PHE A CZ 1414 N N . ARG A 187 ? 1.5934 0.6816 0.9830 -0.5637 0.0612 -0.1287 185 ARG A N 1415 C CA . ARG A 187 ? 1.6752 0.6411 1.0432 -0.5591 0.1028 -0.1391 185 ARG A CA 1416 C C . ARG A 187 ? 1.6415 0.5736 1.0358 -0.4973 0.1081 -0.0979 185 ARG A C 1417 O O . ARG A 187 ? 1.6273 0.5744 1.0360 -0.4940 0.0997 -0.0675 185 ARG A O 1418 C CB . ARG A 187 ? 1.7555 0.6749 1.1006 -0.6187 0.1217 -0.1530 185 ARG A CB 1419 C CG . ARG A 187 ? 1.8038 0.7462 1.1146 -0.6922 0.1222 -0.1978 185 ARG A CG 1420 C CD . ARG A 187 ? 1.8574 0.7886 1.1563 -0.7537 0.1298 -0.2027 185 ARG A CD 1421 N NE . ARG A 187 ? 1.9551 0.8953 1.2141 -0.8317 0.1363 -0.2499 185 ARG A NE 1422 C CZ . ARG A 187 ? 2.0941 1.0138 1.3328 -0.8990 0.1496 -0.2667 185 ARG A CZ 1423 N NH1 . ARG A 187 ? 2.1415 1.0265 1.3972 -0.8957 0.1592 -0.2385 185 ARG A NH1 1424 N NH2 . ARG A 187 ? 2.1725 1.1088 1.3710 -0.9742 0.1540 -0.3124 185 ARG A NH2 1425 N N . ASN A 188 ? 1.6335 0.5274 1.0340 -0.4503 0.1221 -0.0961 186 ASN A N 1426 C CA . ASN A 188 ? 1.6262 0.4845 1.0504 -0.3927 0.1305 -0.0556 186 ASN A CA 1427 C C . ASN A 188 ? 1.5263 0.4645 0.9762 -0.3700 0.0971 -0.0153 186 ASN A C 1428 O O . ASN A 188 ? 1.5299 0.4435 0.9897 -0.3441 0.1024 0.0215 186 ASN A O 1429 C CB . ASN A 188 ? 1.7264 0.4732 1.1381 -0.4006 0.1690 -0.0481 186 ASN A CB 1430 C CG . ASN A 188 ? 1.8835 0.5425 1.2636 -0.4380 0.2078 -0.0963 186 ASN A CG 1431 O OD1 . ASN A 188 ? 1.9650 0.6546 1.3192 -0.4923 0.2011 -0.1366 186 ASN A OD1 1432 N ND2 . ASN A 188 ? 2.0498 0.6003 1.4321 -0.4103 0.2504 -0.0919 186 ASN A ND2 1433 N N . ARG A 189 ? 1.4221 0.4549 0.8818 -0.3813 0.0650 -0.0218 187 ARG A N 1434 C CA . ARG A 189 ? 1.3278 0.4339 0.8115 -0.3608 0.0383 0.0091 187 ARG A CA 1435 C C . ARG A 189 ? 1.2204 0.4050 0.7231 -0.3406 0.0125 0.0055 187 ARG A C 1436 O O . ARG A 189 ? 1.1406 0.3973 0.6600 -0.3472 -0.0097 0.0115 187 ARG A O 1437 C CB . ARG A 189 ? 1.3264 0.4622 0.8096 -0.4000 0.0313 0.0139 187 ARG A CB 1438 C CG . ARG A 189 ? 1.3048 0.4837 0.7837 -0.4484 0.0216 -0.0135 187 ARG A CG 1439 C CD . ARG A 189 ? 1.2823 0.4889 0.7676 -0.4815 0.0192 -0.0018 187 ARG A CD 1440 N NE . ARG A 189 ? 1.2899 0.5679 0.7842 -0.5237 0.0031 -0.0179 187 ARG A NE 1441 C CZ . ARG A 189 ? 1.2373 0.6063 0.7623 -0.5128 -0.0222 -0.0114 187 ARG A CZ 1442 N NH1 . ARG A 189 ? 1.2117 0.6042 0.7563 -0.4654 -0.0323 0.0047 187 ARG A NH1 1443 N NH2 . ARG A 189 ? 1.2318 0.6692 0.7693 -0.5504 -0.0365 -0.0195 187 ARG A NH2 1444 N N . VAL A 190 ? 1.2088 0.3740 0.7113 -0.3146 0.0196 -0.0037 188 VAL A N 1445 C CA . VAL A 190 ? 1.1254 0.3542 0.6442 -0.2946 -0.0004 -0.0067 188 VAL A CA 1446 C C . VAL A 190 ? 1.1469 0.3456 0.6702 -0.2567 0.0133 -0.0065 188 VAL A C 1447 O O . VAL A 190 ? 1.2078 0.3455 0.7155 -0.2612 0.0390 -0.0265 188 VAL A O 1448 C CB . VAL A 190 ? 1.0919 0.3594 0.6018 -0.3304 -0.0109 -0.0336 188 VAL A CB 1449 C CG1 . VAL A 190 ? 1.2091 0.4166 0.6886 -0.3527 0.0139 -0.0657 188 VAL A CG1 1450 C CG2 . VAL A 190 ? 1.0424 0.3748 0.5712 -0.3107 -0.0314 -0.0303 188 VAL A CG2 1451 N N . ASP A 191 ? 1.1151 0.3588 0.6612 -0.2210 -0.0016 0.0146 189 ASP A N 1452 C CA . ASP A 191 ? 1.1425 0.3738 0.7018 -0.1819 0.0092 0.0210 189 ASP A CA 1453 C C . ASP A 191 ? 1.0760 0.3807 0.6588 -0.1568 -0.0138 0.0357 189 ASP A C 1454 O O . ASP A 191 ? 1.0602 0.4133 0.6493 -0.1625 -0.0345 0.0471 189 ASP A O 1455 C CB . ASP A 191 ? 1.2017 0.3721 0.7656 -0.1559 0.0306 0.0468 189 ASP A CB 1456 C CG . ASP A 191 ? 1.2892 0.4323 0.8702 -0.1176 0.0518 0.0493 189 ASP A CG 1457 O OD1 . ASP A 191 ? 1.4461 0.5082 1.0203 -0.1147 0.0854 0.0405 189 ASP A OD1 1458 O OD2 . ASP A 191 ? 1.3193 0.5209 0.9227 -0.0914 0.0378 0.0588 189 ASP A OD2 1459 N N . LEU A 192 ? 1.0726 0.3829 0.6685 -0.1308 -0.0062 0.0329 190 LEU A N 1460 C CA . LEU A 192 ? 1.0117 0.3905 0.6300 -0.1104 -0.0250 0.0438 190 LEU A CA 1461 C C . LEU A 192 ? 1.0132 0.4185 0.6473 -0.0858 -0.0351 0.0793 190 LEU A C 1462 O O . LEU A 192 ? 1.0266 0.4029 0.6706 -0.0589 -0.0213 0.1023 190 LEU A O 1463 C CB . LEU A 192 ? 1.0219 0.4024 0.6524 -0.0899 -0.0110 0.0327 190 LEU A CB 1464 C CG . LEU A 192 ? 0.9988 0.3678 0.6096 -0.1158 -0.0020 -0.0029 190 LEU A CG 1465 C CD1 . LEU A 192 ? 0.9892 0.3566 0.6123 -0.0925 0.0180 -0.0127 190 LEU A CD1 1466 C CD2 . LEU A 192 ? 0.9790 0.4061 0.5871 -0.1403 -0.0285 -0.0087 190 LEU A CD2 1467 N N . THR A 193 ? 0.9729 0.4357 0.6097 -0.0960 -0.0581 0.0840 191 THR A N 1468 C CA . THR A 193 ? 0.9669 0.4680 0.6101 -0.0836 -0.0707 0.1130 191 THR A CA 1469 C C . THR A 193 ? 0.9518 0.5007 0.6187 -0.0568 -0.0765 0.1263 191 THR A C 1470 O O . THR A 193 ? 0.9563 0.5375 0.6322 -0.0395 -0.0839 0.1571 191 THR A O 1471 C CB . THR A 193 ? 0.9206 0.4633 0.5561 -0.1084 -0.0876 0.1053 191 THR A CB 1472 O OG1 . THR A 193 ? 0.9301 0.5047 0.5752 -0.1175 -0.0953 0.0831 191 THR A OG1 1473 C CG2 . THR A 193 ? 0.9907 0.4989 0.6098 -0.1331 -0.0820 0.0972 191 THR A CG2 1474 N N . GLY A 194 ? 0.9458 0.5061 0.6230 -0.0557 -0.0737 0.1051 192 GLY A N 1475 C CA . GLY A 194 ? 0.9481 0.5606 0.6514 -0.0340 -0.0779 0.1144 192 GLY A CA 1476 C C . GLY A 194 ? 1.0017 0.5827 0.7187 -0.0129 -0.0550 0.1062 192 GLY A C 1477 O O . GLY A 194 ? 1.0645 0.5770 0.7698 -0.0115 -0.0336 0.0978 192 GLY A O 1478 N N . ASP A 195 ? 0.9950 0.6257 0.7362 0.0006 -0.0564 0.1058 193 ASP A N 1479 C CA . ASP A 195 ? 1.0413 0.6493 0.7976 0.0207 -0.0307 0.0944 193 ASP A CA 1480 C C . ASP A 195 ? 1.0069 0.6487 0.7618 0.0032 -0.0334 0.0680 193 ASP A C 1481 O O . ASP A 195 ? 0.9643 0.6641 0.7241 -0.0113 -0.0549 0.0693 193 ASP A O 1482 C CB . ASP A 195 ? 1.0813 0.7143 0.8792 0.0652 -0.0204 0.1280 193 ASP A CB 1483 C CG . ASP A 195 ? 1.0642 0.7924 0.8859 0.0703 -0.0478 0.1546 193 ASP A CG 1484 O OD1 . ASP A 195 ? 1.0441 0.8119 0.8505 0.0390 -0.0690 0.1389 193 ASP A OD1 1485 O OD2 . ASP A 195 ? 1.1344 0.8987 0.9912 0.1045 -0.0471 0.1922 193 ASP A OD2 1486 N N . ILE A 196 ? 1.0374 0.6390 0.7828 0.0017 -0.0088 0.0431 194 ILE A N 1487 C CA . ILE A 196 ? 1.0101 0.6372 0.7465 -0.0191 -0.0088 0.0184 194 ILE A CA 1488 C C . ILE A 196 ? 0.9763 0.6656 0.7494 0.0031 -0.0053 0.0281 194 ILE A C 1489 O O . ILE A 196 ? 0.9423 0.6734 0.7152 -0.0138 -0.0122 0.0174 194 ILE A O 1490 C CB . ILE A 196 ? 1.0670 0.6381 0.7754 -0.0328 0.0182 -0.0134 194 ILE A CB 1491 C CG1 . ILE A 196 ? 1.1081 0.6258 0.7799 -0.0617 0.0141 -0.0248 194 ILE A CG1 1492 C CG2 . ILE A 196 ? 1.0810 0.6903 0.7794 -0.0542 0.0168 -0.0327 194 ILE A CG2 1493 C CD1 . ILE A 196 ? 1.1011 0.6473 0.7509 -0.0996 -0.0099 -0.0339 194 ILE A CD1 1494 N N . SER A 197 ? 0.9888 0.6872 0.7965 0.0414 0.0057 0.0521 195 SER A N 1495 C CA . SER A 197 ? 0.9692 0.7389 0.8208 0.0655 0.0088 0.0665 195 SER A CA 1496 C C . SER A 197 ? 0.9018 0.7485 0.7591 0.0443 -0.0253 0.0773 195 SER A C 1497 O O . SER A 197 ? 0.8749 0.7889 0.7589 0.0458 -0.0278 0.0802 195 SER A O 1498 C CB . SER A 197 ? 1.0069 0.7807 0.9023 0.1141 0.0241 0.1001 195 SER A CB 1499 O OG . SER A 197 ? 1.0374 0.8008 0.9285 0.1191 0.0059 0.1293 195 SER A OG 1500 N N . ARG A 198 ? 0.8805 0.7152 0.7124 0.0220 -0.0482 0.0808 196 ARG A N 1501 C CA . ARG A 198 ? 0.8409 0.7325 0.6705 -0.0046 -0.0756 0.0833 196 ARG A CA 1502 C C . ARG A 198 ? 0.8029 0.6628 0.5999 -0.0405 -0.0807 0.0571 196 ARG A C 1503 O O . ARG A 198 ? 0.7859 0.6601 0.5723 -0.0646 -0.0982 0.0550 196 ARG A O 1504 C CB . ARG A 198 ? 0.8398 0.7509 0.6680 -0.0032 -0.0950 0.1076 196 ARG A CB 1505 C CG . ARG A 198 ? 0.9069 0.8851 0.7740 0.0265 -0.0997 0.1427 196 ARG A CG 1506 C CD . ARG A 198 ? 1.0114 1.0055 0.8688 0.0262 -0.1182 0.1703 196 ARG A CD 1507 N NE . ARG A 198 ? 1.0511 1.0334 0.8704 -0.0137 -0.1336 0.1507 196 ARG A NE 1508 C CZ . ARG A 198 ? 1.0426 1.0533 0.8460 -0.0274 -0.1509 0.1653 196 ARG A CZ 1509 N NH1 . ARG A 198 ? 1.0337 1.0926 0.8539 -0.0060 -0.1598 0.2047 196 ARG A NH1 1510 N NH2 . ARG A 198 ? 1.0393 1.0327 0.8110 -0.0624 -0.1576 0.1420 196 ARG A NH2 1511 N N . ASN A 199 ? 0.8003 0.6188 0.5827 -0.0434 -0.0628 0.0380 197 ASN A N 1512 C CA . ASN A 199 ? 0.7730 0.5730 0.5295 -0.0748 -0.0666 0.0189 197 ASN A CA 1513 C C . ASN A 199 ? 0.7343 0.5046 0.4702 -0.0937 -0.0813 0.0191 197 ASN A C 1514 O O . ASN A 199 ? 0.6969 0.4733 0.4257 -0.1169 -0.0914 0.0142 197 ASN A O 1515 C CB . ASN A 199 ? 0.7557 0.6092 0.5254 -0.0903 -0.0740 0.0175 197 ASN A CB 1516 C CG . ASN A 199 ? 0.7994 0.6980 0.5974 -0.0712 -0.0606 0.0207 197 ASN A CG 1517 O OD1 . ASN A 199 ? 0.8569 0.7418 0.6509 -0.0643 -0.0394 0.0086 197 ASN A OD1 1518 N ND2 . ASN A 199 ? 0.8652 0.8230 0.6920 -0.0648 -0.0715 0.0361 197 ASN A ND2 1519 N N . ASP A 200 ? 0.7445 0.4826 0.4745 -0.0818 -0.0799 0.0272 198 ASP A N 1520 C CA . ASP A 200 ? 0.7356 0.4463 0.4478 -0.0982 -0.0900 0.0275 198 ASP A CA 1521 C C . ASP A 200 ? 0.7634 0.4166 0.4536 -0.1026 -0.0780 0.0183 198 ASP A C 1522 O O . ASP A 200 ? 0.8151 0.4360 0.5046 -0.0844 -0.0615 0.0200 198 ASP A O 1523 C CB . ASP A 200 ? 0.7458 0.4732 0.4649 -0.0890 -0.1001 0.0460 198 ASP A CB 1524 C CG . ASP A 200 ? 0.7546 0.4653 0.4584 -0.1083 -0.1089 0.0443 198 ASP A CG 1525 O OD1 . ASP A 200 ? 0.7936 0.4827 0.4877 -0.1259 -0.1082 0.0319 198 ASP A OD1 1526 O OD2 . ASP A 200 ? 0.8064 0.5315 0.5088 -0.1063 -0.1161 0.0570 198 ASP A OD2 1527 N N . GLY A 201 ? 0.7416 0.3833 0.4165 -0.1278 -0.0851 0.0098 199 GLY A N 1528 C CA . GLY A 201 ? 0.7786 0.3763 0.4303 -0.1424 -0.0766 -0.0013 199 GLY A CA 1529 C C . GLY A 201 ? 0.7814 0.3670 0.4279 -0.1558 -0.0860 0.0052 199 GLY A C 1530 O O . GLY A 201 ? 0.8099 0.3793 0.4415 -0.1779 -0.0860 -0.0029 199 GLY A O 1531 N N . SER A 202 ? 0.7607 0.3606 0.4191 -0.1453 -0.0936 0.0197 200 SER A N 1532 C CA . SER A 202 ? 0.7434 0.3347 0.3974 -0.1573 -0.0989 0.0254 200 SER A CA 1533 C C . SER A 202 ? 0.7790 0.3216 0.4162 -0.1582 -0.0869 0.0268 200 SER A C 1534 O O . SER A 202 ? 0.8254 0.3417 0.4606 -0.1391 -0.0748 0.0323 200 SER A O 1535 C CB . SER A 202 ? 0.7122 0.3327 0.3762 -0.1500 -0.1070 0.0371 200 SER A CB 1536 O OG . SER A 202 ? 0.6687 0.3245 0.3469 -0.1563 -0.1144 0.0316 200 SER A OG 1537 N N . ILE A 203 ? 0.7704 0.3017 0.3994 -0.1805 -0.0885 0.0235 201 ILE A N 1538 C CA . ILE A 203 ? 0.8036 0.2875 0.4158 -0.1887 -0.0766 0.0248 201 ILE A CA 1539 C C . ILE A 203 ? 0.7977 0.2905 0.4117 -0.1993 -0.0816 0.0362 201 ILE A C 1540 O O . ILE A 203 ? 0.7573 0.2903 0.3855 -0.2049 -0.0921 0.0373 201 ILE A O 1541 C CB . ILE A 203 ? 0.8314 0.2900 0.4259 -0.2157 -0.0689 0.0050 201 ILE A CB 1542 C CG1 . ILE A 203 ? 0.7679 0.2693 0.3700 -0.2418 -0.0840 0.0023 201 ILE A CG1 1543 C CG2 . ILE A 203 ? 0.8277 0.2768 0.4149 -0.2092 -0.0595 -0.0106 201 ILE A CG2 1544 C CD1 . ILE A 203 ? 0.7402 0.2279 0.3221 -0.2772 -0.0799 -0.0133 201 ILE A CD1 1545 N N . LYS A 204 ? 0.8489 0.3005 0.4493 -0.2015 -0.0704 0.0449 202 LYS A N 1546 C CA . LYS A 204 ? 0.8583 0.3145 0.4562 -0.2172 -0.0712 0.0543 202 LYS A CA 1547 C C . LYS A 204 ? 0.8736 0.2939 0.4577 -0.2462 -0.0611 0.0449 202 LYS A C 1548 O O . LYS A 204 ? 0.9029 0.2730 0.4718 -0.2494 -0.0474 0.0362 202 LYS A O 1549 C CB . LYS A 204 ? 0.8976 0.3424 0.4885 -0.2003 -0.0672 0.0787 202 LYS A CB 1550 C CG . LYS A 204 ? 0.9711 0.3514 0.5486 -0.1921 -0.0499 0.0898 202 LYS A CG 1551 C CD . LYS A 204 ? 1.1049 0.4789 0.6754 -0.1806 -0.0474 0.1221 202 LYS A CD 1552 C CE . LYS A 204 ? 1.2059 0.5307 0.7776 -0.1522 -0.0329 0.1437 202 LYS A CE 1553 N NZ . LYS A 204 ? 1.2274 0.5838 0.8182 -0.1218 -0.0397 0.1452 202 LYS A NZ 1554 N N . LEU A 205 ? 0.8512 0.2995 0.4427 -0.2685 -0.0658 0.0452 203 LEU A N 1555 C CA . LEU A 205 ? 0.8812 0.3093 0.4626 -0.3022 -0.0581 0.0387 203 LEU A CA 1556 C C . LEU A 205 ? 0.9126 0.3275 0.4883 -0.3067 -0.0497 0.0564 203 LEU A C 1557 O O . LEU A 205 ? 0.8608 0.3188 0.4504 -0.3021 -0.0554 0.0657 203 LEU A O 1558 C CB . LEU A 205 ? 0.8256 0.3104 0.4267 -0.3253 -0.0707 0.0299 203 LEU A CB 1559 C CG . LEU A 205 ? 0.9329 0.4091 0.5229 -0.3670 -0.0661 0.0191 203 LEU A CG 1560 C CD1 . LEU A 205 ? 1.0545 0.4740 0.6126 -0.3802 -0.0547 -0.0012 203 LEU A CD1 1561 C CD2 . LEU A 205 ? 0.9463 0.4969 0.5643 -0.3859 -0.0823 0.0194 203 LEU A CD2 1562 N N . GLN A 206 ? 0.9892 0.3413 0.5431 -0.3178 -0.0331 0.0602 204 GLN A N 1563 C CA . GLN A 206 ? 1.0253 0.3524 0.5686 -0.3132 -0.0231 0.0851 204 GLN A CA 1564 C C . GLN A 206 ? 1.0339 0.3873 0.5801 -0.3437 -0.0210 0.0889 204 GLN A C 1565 O O . GLN A 206 ? 1.0609 0.4457 0.6099 -0.3371 -0.0227 0.1051 204 GLN A O 1566 C CB . GLN A 206 ? 1.0967 0.3396 0.6202 -0.3073 -0.0026 0.0942 204 GLN A CB 1567 C CG . GLN A 206 ? 1.1035 0.3303 0.6319 -0.2679 -0.0024 0.0987 204 GLN A CG 1568 C CD . GLN A 206 ? 1.2139 0.3858 0.7365 -0.2416 0.0132 0.1308 204 GLN A CD 1569 O OE1 . GLN A 206 ? 1.3363 0.4345 0.8459 -0.2537 0.0362 0.1346 204 GLN A OE1 1570 N NE2 . GLN A 206 ? 1.2154 0.4241 0.7491 -0.2060 0.0015 0.1562 204 GLN A NE2 1571 N N . THR A 207 ? 1.0412 0.3871 0.5861 -0.3802 -0.0161 0.0732 205 THR A N 1572 C CA . THR A 207 ? 1.0514 0.4269 0.6033 -0.4106 -0.0122 0.0787 205 THR A CA 1573 C C . THR A 207 ? 1.0153 0.4588 0.5950 -0.4313 -0.0251 0.0627 205 THR A C 1574 O O . THR A 207 ? 1.0516 0.4917 0.6273 -0.4643 -0.0254 0.0470 205 THR A O 1575 C CB . THR A 207 ? 1.1443 0.4540 0.6720 -0.4428 0.0080 0.0819 205 THR A CB 1576 O OG1 . THR A 207 ? 1.1562 0.4104 0.6645 -0.4194 0.0205 0.1084 205 THR A OG1 1577 C CG2 . THR A 207 ? 1.1348 0.4882 0.6745 -0.4817 0.0111 0.0836 205 THR A CG2 1578 N N . VAL A 208 ? 0.9637 0.4709 0.5721 -0.4124 -0.0350 0.0677 206 VAL A N 1579 C CA . VAL A 208 ? 0.9235 0.5015 0.5686 -0.4222 -0.0474 0.0606 206 VAL A CA 1580 C C . VAL A 208 ? 0.9443 0.5557 0.6039 -0.4620 -0.0419 0.0628 206 VAL A C 1581 O O . VAL A 208 ? 0.9401 0.5545 0.6003 -0.4693 -0.0289 0.0731 206 VAL A O 1582 C CB . VAL A 208 ? 0.8556 0.4829 0.5318 -0.3899 -0.0530 0.0652 206 VAL A CB 1583 C CG1 . VAL A 208 ? 0.8375 0.5398 0.5621 -0.3986 -0.0591 0.0674 206 VAL A CG1 1584 C CG2 . VAL A 208 ? 0.7977 0.4052 0.4649 -0.3615 -0.0628 0.0595 206 VAL A CG2 1585 N N . LYS A 209 ? 0.9621 0.6005 0.6296 -0.4913 -0.0518 0.0531 207 LYS A N 1586 C CA . LYS A 209 ? 0.9932 0.6815 0.6801 -0.5343 -0.0514 0.0547 207 LYS A CA 1587 C C . LYS A 209 ? 0.9567 0.7424 0.6971 -0.5279 -0.0689 0.0632 207 LYS A C 1588 O O . LYS A 209 ? 0.9449 0.7420 0.6961 -0.4976 -0.0806 0.0642 207 LYS A O 1589 C CB . LYS A 209 ? 1.0561 0.7045 0.7069 -0.5807 -0.0497 0.0365 207 LYS A CB 1590 C CG . LYS A 209 ? 1.1245 0.6611 0.7238 -0.5754 -0.0324 0.0261 207 LYS A CG 1591 C CD . LYS A 209 ? 1.2140 0.7056 0.7784 -0.6267 -0.0235 0.0025 207 LYS A CD 1592 C CE . LYS A 209 ? 1.2882 0.6602 0.8095 -0.6201 0.0019 -0.0040 207 LYS A CE 1593 N NZ . LYS A 209 ? 1.4060 0.7228 0.8908 -0.6569 0.0130 -0.0364 207 LYS A NZ 1594 N N . GLU A 210 ? 0.9653 0.8233 0.7428 -0.5555 -0.0698 0.0727 208 GLU A N 1595 C CA . GLU A 210 ? 0.9474 0.9064 0.7836 -0.5506 -0.0869 0.0879 208 GLU A CA 1596 C C . GLU A 210 ? 0.9592 0.9319 0.7786 -0.5688 -0.1090 0.0812 208 GLU A C 1597 O O . GLU A 210 ? 0.9285 0.9561 0.7820 -0.5469 -0.1252 0.0955 208 GLU A O 1598 C CB . GLU A 210 ? 0.9653 1.0087 0.8469 -0.5823 -0.0847 0.1014 208 GLU A CB 1599 C CG . GLU A 210 ? 0.9872 1.0609 0.9130 -0.5551 -0.0647 0.1144 208 GLU A CG 1600 C CD . GLU A 210 ? 1.0660 1.2479 1.0559 -0.5786 -0.0648 0.1327 208 GLU A CD 1601 O OE1 . GLU A 210 ? 1.0856 1.3479 1.1140 -0.5889 -0.0867 0.1474 208 GLU A OE1 1602 O OE2 . GLU A 210 ? 1.1408 1.3339 1.1435 -0.5880 -0.0433 0.1349 208 GLU A OE2 1603 N N . SER A 211 ? 1.0144 0.9340 0.7797 -0.6102 -0.1067 0.0594 209 SER A N 1604 C CA . SER A 211 ? 1.0395 0.9706 0.7780 -0.6386 -0.1236 0.0463 209 SER A CA 1605 C C . SER A 211 ? 1.0143 0.9112 0.7384 -0.5970 -0.1299 0.0431 209 SER A C 1606 O O . SER A 211 ? 1.0338 0.9534 0.7416 -0.6129 -0.1449 0.0367 209 SER A O 1607 C CB . SER A 211 ? 1.1159 0.9754 0.7931 -0.6908 -0.1103 0.0158 209 SER A CB 1608 O OG . SER A 211 ? 1.1640 0.9073 0.7999 -0.6653 -0.0883 0.0018 209 SER A OG 1609 N N . ASP A 212 ? 0.9734 0.8218 0.7019 -0.5478 -0.1184 0.0476 210 ASP A N 1610 C CA . ASP A 212 ? 0.9489 0.7602 0.6625 -0.5100 -0.1217 0.0432 210 ASP A CA 1611 C C . ASP A 212 ? 0.8781 0.7563 0.6435 -0.4753 -0.1353 0.0663 210 ASP A C 1612 O O . ASP A 212 ? 0.8530 0.7121 0.6137 -0.4455 -0.1390 0.0660 210 ASP A O 1613 C CB . ASP A 212 ? 0.9596 0.6851 0.6470 -0.4794 -0.1029 0.0360 210 ASP A CB 1614 C CG . ASP A 212 ? 1.0455 0.6926 0.6846 -0.5067 -0.0861 0.0179 210 ASP A CG 1615 O OD1 . ASP A 212 ? 1.1327 0.7821 0.7510 -0.5515 -0.0874 0.0027 210 ASP A OD1 1616 O OD2 . ASP A 212 ? 1.0774 0.6610 0.6988 -0.4853 -0.0706 0.0198 210 ASP A OD2 1617 N N . GLN A 213 ? 0.8409 0.7978 0.6593 -0.4801 -0.1405 0.0877 211 GLN A N 1618 C CA . GLN A 213 ? 0.7712 0.7875 0.6494 -0.4443 -0.1470 0.1135 211 GLN A CA 1619 C C . GLN A 213 ? 0.7637 0.8305 0.6498 -0.4493 -0.1702 0.1277 211 GLN A C 1620 O O . GLN A 213 ? 0.7851 0.9228 0.6824 -0.4840 -0.1871 0.1397 211 GLN A O 1621 C CB . GLN A 213 ? 0.7553 0.8434 0.6940 -0.4468 -0.1415 0.1340 211 GLN A CB 1622 C CG . GLN A 213 ? 0.7199 0.8694 0.7305 -0.4090 -0.1424 0.1633 211 GLN A CG 1623 C CD . GLN A 213 ? 0.7321 0.9305 0.8009 -0.4016 -0.1250 0.1765 211 GLN A CD 1624 O OE1 . GLN A 213 ? 0.6270 0.7814 0.6939 -0.3812 -0.1004 0.1634 211 GLN A OE1 1625 N NE2 . GLN A 213 ? 0.7634 1.0596 0.8837 -0.4210 -0.1370 0.2025 211 GLN A NE2 1626 N N . GLY A 214 ? 0.7391 0.7747 0.6179 -0.4178 -0.1714 0.1277 212 GLY A N 1627 C CA . GLY A 214 ? 0.7263 0.8079 0.6103 -0.4206 -0.1921 0.1447 212 GLY A CA 1628 C C . GLY A 214 ? 0.6997 0.7425 0.5796 -0.3840 -0.1893 0.1456 212 GLY A C 1629 O O . GLY A 214 ? 0.6790 0.6902 0.5823 -0.3479 -0.1740 0.1462 212 GLY A O 1630 N N . ILE A 215 ? 0.7037 0.7521 0.5510 -0.3982 -0.2031 0.1436 213 ILE A N 1631 C CA . ILE A 215 ? 0.6859 0.7025 0.5259 -0.3697 -0.2013 0.1445 213 ILE A CA 1632 C C . ILE A 215 ? 0.7125 0.6616 0.4869 -0.3801 -0.1941 0.1093 213 ILE A C 1633 O O . ILE A 215 ? 0.7639 0.7189 0.4964 -0.4145 -0.2009 0.0952 213 ILE A O 1634 C CB . ILE A 215 ? 0.6802 0.7634 0.5405 -0.3723 -0.2212 0.1774 213 ILE A CB 1635 C CG1 . ILE A 215 ? 0.6595 0.8116 0.5983 -0.3517 -0.2260 0.2212 213 ILE A CG1 1636 C CG2 . ILE A 215 ? 0.6493 0.6910 0.4924 -0.3494 -0.2166 0.1731 213 ILE A CG2 1637 C CD1 . ILE A 215 ? 0.6716 0.9114 0.6336 -0.3634 -0.2508 0.2638 213 ILE A CD1 1638 N N . TYR A 216 ? 0.6994 0.5873 0.4669 -0.3504 -0.1787 0.0951 214 TYR A N 1639 C CA . TYR A 216 ? 0.7195 0.5493 0.4375 -0.3504 -0.1703 0.0682 214 TYR A CA 1640 C C . TYR A 216 ? 0.7041 0.5422 0.4288 -0.3308 -0.1746 0.0779 214 TYR A C 1641 O O . TYR A 216 ? 0.6664 0.5212 0.4318 -0.3065 -0.1751 0.0980 214 TYR A O 1642 C CB . TYR A 216 ? 0.7245 0.4920 0.4308 -0.3329 -0.1528 0.0512 214 TYR A CB 1643 C CG . TYR A 216 ? 0.7059 0.4642 0.4053 -0.3549 -0.1472 0.0451 214 TYR A CG 1644 C CD1 . TYR A 216 ? 0.6727 0.4751 0.4118 -0.3580 -0.1503 0.0627 214 TYR A CD1 1645 C CD2 . TYR A 216 ? 0.7333 0.4380 0.3893 -0.3733 -0.1359 0.0225 214 TYR A CD2 1646 C CE1 . TYR A 216 ? 0.7621 0.5607 0.4955 -0.3817 -0.1445 0.0578 214 TYR A CE1 1647 C CE2 . TYR A 216 ? 0.7597 0.4516 0.4082 -0.3974 -0.1290 0.0178 214 TYR A CE2 1648 C CZ . TYR A 216 ? 0.7700 0.5115 0.4559 -0.4031 -0.1345 0.0354 214 TYR A CZ 1649 O OH . TYR A 216 ? 0.7826 0.5148 0.4613 -0.4303 -0.1266 0.0311 214 TYR A OH 1650 N N . THR A 217 ? 0.7400 0.5650 0.4240 -0.3445 -0.1745 0.0622 215 THR A N 1651 C CA . THR A 217 ? 0.7408 0.5825 0.4252 -0.3351 -0.1793 0.0722 215 THR A CA 1652 C C . THR A 217 ? 0.7684 0.5616 0.4133 -0.3304 -0.1652 0.0440 215 THR A C 1653 O O . THR A 217 ? 0.8322 0.6107 0.4353 -0.3546 -0.1591 0.0212 215 THR A O 1654 C CB . THR A 217 ? 0.7639 0.6706 0.4425 -0.3648 -0.1974 0.0910 215 THR A CB 1655 O OG1 . THR A 217 ? 0.7874 0.7478 0.5106 -0.3673 -0.2105 0.1214 215 THR A OG1 1656 C CG2 . THR A 217 ? 0.7398 0.6675 0.4220 -0.3551 -0.2025 0.1086 215 THR A CG2 1657 N N . CYS A 218 ? 0.7490 0.5194 0.4099 -0.3000 -0.1577 0.0448 216 CYS A N 1658 C CA . CYS A 218 ? 0.7634 0.4981 0.3998 -0.2885 -0.1441 0.0239 216 CYS A CA 1659 C C . CYS A 218 ? 0.7672 0.5297 0.3956 -0.2937 -0.1473 0.0294 216 CYS A C 1660 O O . CYS A 218 ? 0.7621 0.5639 0.4129 -0.2954 -0.1596 0.0551 216 CYS A O 1661 C CB . CYS A 218 ? 0.7417 0.4511 0.3987 -0.2581 -0.1367 0.0238 216 CYS A CB 1662 S SG . CYS A 218 ? 0.7644 0.4459 0.4048 -0.2392 -0.1217 0.0061 216 CYS A SG 1663 N N . SER A 219 ? 0.7814 0.5219 0.3787 -0.2957 -0.1334 0.0064 217 SER A N 1664 C CA . SER A 219 ? 0.7752 0.5413 0.3551 -0.3062 -0.1322 0.0060 217 SER A CA 1665 C C . SER A 219 ? 0.7741 0.5085 0.3435 -0.2882 -0.1114 -0.0164 217 SER A C 1666 O O . SER A 219 ? 0.8148 0.5139 0.3577 -0.2922 -0.0936 -0.0428 217 SER A O 1667 C CB . SER A 219 ? 0.8217 0.6118 0.3623 -0.3456 -0.1360 -0.0024 217 SER A CB 1668 O OG . SER A 219 ? 0.8289 0.6749 0.3865 -0.3606 -0.1590 0.0308 217 SER A OG 1669 N N . ILE A 220 ? 0.7308 0.4783 0.3251 -0.2680 -0.1120 -0.0049 218 ILE A N 1670 C CA . ILE A 220 ? 0.7315 0.4624 0.3294 -0.2460 -0.0950 -0.0191 218 ILE A CA 1671 C C . ILE A 220 ? 0.7499 0.5117 0.3385 -0.2542 -0.0890 -0.0197 218 ILE A C 1672 O O . ILE A 220 ? 0.7566 0.5518 0.3518 -0.2667 -0.1020 0.0012 218 ILE A O 1673 C CB . ILE A 220 ? 0.6844 0.4117 0.3174 -0.2211 -0.1005 -0.0071 218 ILE A CB 1674 C CG1 . ILE A 220 ? 0.7226 0.4386 0.3635 -0.1963 -0.0854 -0.0175 218 ILE A CG1 1675 C CG2 . ILE A 220 ? 0.6595 0.4177 0.3162 -0.2240 -0.1123 0.0131 218 ILE A CG2 1676 C CD1 . ILE A 220 ? 0.6953 0.4024 0.3581 -0.1770 -0.0910 -0.0087 218 ILE A CD1 1677 N N . TYR A 221 ? 0.7734 0.5234 0.3466 -0.2481 -0.0668 -0.0423 219 TYR A N 1678 C CA . TYR A 221 ? 0.7889 0.5699 0.3475 -0.2597 -0.0566 -0.0469 219 TYR A CA 1679 C C . TYR A 221 ? 0.7961 0.5821 0.3769 -0.2337 -0.0383 -0.0547 219 TYR A C 1680 O O . TYR A 221 ? 0.8161 0.5745 0.4104 -0.2082 -0.0243 -0.0655 219 TYR A O 1681 C CB . TYR A 221 ? 0.8520 0.6245 0.3624 -0.2863 -0.0398 -0.0736 219 TYR A CB 1682 C CG . TYR A 221 ? 0.8828 0.6597 0.3630 -0.3204 -0.0554 -0.0714 219 TYR A CG 1683 C CD1 . TYR A 221 ? 0.8684 0.6095 0.3483 -0.3206 -0.0592 -0.0777 219 TYR A CD1 1684 C CD2 . TYR A 221 ? 0.8601 0.6830 0.3108 -0.3551 -0.0657 -0.0618 219 TYR A CD2 1685 C CE1 . TYR A 221 ? 0.9207 0.6754 0.3759 -0.3549 -0.0737 -0.0757 219 TYR A CE1 1686 C CE2 . TYR A 221 ? 0.9137 0.7546 0.3389 -0.3887 -0.0824 -0.0567 219 TYR A CE2 1687 C CZ . TYR A 221 ? 0.9206 0.7285 0.3496 -0.3888 -0.0862 -0.0650 219 TYR A CZ 1688 O OH . TYR A 221 ? 0.9826 0.8167 0.3900 -0.4247 -0.1033 -0.0595 219 TYR A OH 1689 N N . VAL A 222 ? 0.7942 0.6204 0.3803 -0.2411 -0.0382 -0.0452 220 VAL A N 1690 C CA . VAL A 222 ? 0.7956 0.6418 0.3948 -0.2264 -0.0163 -0.0559 220 VAL A CA 1691 C C . VAL A 222 ? 0.8445 0.7128 0.4051 -0.2551 -0.0035 -0.0667 220 VAL A C 1692 O O . VAL A 222 ? 0.8432 0.7460 0.3977 -0.2766 -0.0166 -0.0465 220 VAL A O 1693 C CB . VAL A 222 ? 0.7504 0.6316 0.3899 -0.2161 -0.0273 -0.0349 220 VAL A CB 1694 C CG1 . VAL A 222 ? 0.7282 0.6390 0.3905 -0.1976 -0.0051 -0.0444 220 VAL A CG1 1695 C CG2 . VAL A 222 ? 0.7060 0.5689 0.3715 -0.2001 -0.0453 -0.0230 220 VAL A CG2 1696 N N . GLY A 223 ? 0.8862 0.7315 0.4182 -0.2576 0.0239 -0.0983 221 GLY A N 1697 C CA . GLY A 223 ? 0.9320 0.7947 0.4141 -0.2927 0.0374 -0.1150 221 GLY A CA 1698 C C . GLY A 223 ? 0.9382 0.8117 0.3879 -0.3284 0.0092 -0.0986 221 GLY A C 1699 O O . GLY A 223 ? 0.9521 0.7973 0.4021 -0.3287 -0.0060 -0.0958 221 GLY A O 1700 N N . LYS A 224 ? 0.9555 0.8763 0.3806 -0.3581 0.0016 -0.0832 222 LYS A N 1701 C CA . LYS A 224 ? 0.9683 0.9147 0.3615 -0.3943 -0.0242 -0.0626 222 LYS A CA 1702 C C . LYS A 224 ? 0.9015 0.8571 0.3369 -0.3826 -0.0583 -0.0173 222 LYS A C 1703 O O . LYS A 224 ? 0.9228 0.8982 0.3482 -0.4028 -0.0820 0.0060 222 LYS A O 1704 C CB . LYS A 224 ? 1.0043 1.0039 0.3542 -0.4311 -0.0194 -0.0569 222 LYS A CB 1705 C CG . LYS A 224 ? 1.1079 1.1007 0.4081 -0.4495 0.0195 -0.1070 222 LYS A CG 1706 C CD . LYS A 224 ? 1.1360 1.0926 0.3932 -0.4718 0.0290 -0.1449 222 LYS A CD 1707 C CE . LYS A 224 ? 1.1468 1.1520 0.3483 -0.5266 0.0066 -0.1332 222 LYS A CE 1708 N NZ . LYS A 224 ? 1.1914 1.1639 0.3468 -0.5569 0.0179 -0.1755 222 LYS A NZ 1709 N N . LEU A 225 ? 0.8365 0.7808 0.3206 -0.3510 -0.0589 -0.0053 223 LEU A N 1710 C CA . LEU A 225 ? 0.7913 0.7384 0.3154 -0.3410 -0.0837 0.0328 223 LEU A CA 1711 C C . LEU A 225 ? 0.7699 0.6829 0.3104 -0.3272 -0.0957 0.0302 223 LEU A C 1712 O O . LEU A 225 ? 0.7630 0.6411 0.3128 -0.3062 -0.0848 0.0060 223 LEU A O 1713 C CB . LEU A 225 ? 0.7546 0.7030 0.3193 -0.3206 -0.0781 0.0419 223 LEU A CB 1714 C CG . LEU A 225 ? 0.7629 0.7495 0.3165 -0.3375 -0.0678 0.0517 223 LEU A CG 1715 C CD1 . LEU A 225 ? 0.6948 0.6842 0.2884 -0.3204 -0.0590 0.0525 223 LEU A CD1 1716 C CD2 . LEU A 225 ? 0.7006 0.7151 0.2444 -0.3619 -0.0858 0.0932 223 LEU A CD2 1717 N N . GLU A 226 ? 0.7701 0.6979 0.3167 -0.3386 -0.1177 0.0588 224 GLU A N 1718 C CA . GLU A 226 ? 0.7600 0.6636 0.3221 -0.3294 -0.1284 0.0582 224 GLU A CA 1719 C C . GLU A 226 ? 0.7252 0.6187 0.3379 -0.3074 -0.1386 0.0840 224 GLU A C 1720 O O . GLU A 226 ? 0.7174 0.6312 0.3520 -0.3089 -0.1464 0.1167 224 GLU A O 1721 C CB . GLU A 226 ? 0.7817 0.7137 0.3178 -0.3590 -0.1439 0.0681 224 GLU A CB 1722 C CG . GLU A 226 ? 0.7961 0.7039 0.3438 -0.3537 -0.1506 0.0605 224 GLU A CG 1723 C CD . GLU A 226 ? 0.8880 0.8325 0.4112 -0.3877 -0.1664 0.0683 224 GLU A CD 1724 O OE1 . GLU A 226 ? 0.7726 0.7712 0.2755 -0.4144 -0.1782 0.0900 224 GLU A OE1 1725 O OE2 . GLU A 226 ? 0.8866 0.8101 0.4110 -0.3899 -0.1676 0.0545 224 GLU A OE2 1726 N N . SER A 227 ? 0.7067 0.5653 0.3361 -0.2880 -0.1355 0.0682 225 SER A N 1727 C CA . SER A 227 ? 0.6827 0.5288 0.3528 -0.2720 -0.1428 0.0853 225 SER A CA 1728 C C . SER A 227 ? 0.6965 0.5338 0.3643 -0.2748 -0.1502 0.0816 225 SER A C 1729 O O . SER A 227 ? 0.7058 0.5183 0.3534 -0.2732 -0.1429 0.0556 225 SER A O 1730 C CB . SER A 227 ? 0.6556 0.4767 0.3451 -0.2510 -0.1324 0.0702 225 SER A CB 1731 O OG . SER A 227 ? 0.6969 0.5323 0.3887 -0.2528 -0.1249 0.0718 225 SER A OG 1732 N N . ARG A 228 ? 0.7110 0.5704 0.4027 -0.2788 -0.1631 0.1108 226 ARG A N 1733 C CA . ARG A 228 ? 0.7167 0.5798 0.4150 -0.2833 -0.1712 0.1132 226 ARG A CA 1734 C C . ARG A 228 ? 0.6850 0.5272 0.4257 -0.2609 -0.1674 0.1195 226 ARG A C 1735 O O . ARG A 228 ? 0.6805 0.5219 0.4556 -0.2479 -0.1642 0.1385 226 ARG A O 1736 C CB . ARG A 228 ? 0.7375 0.6548 0.4401 -0.3035 -0.1889 0.1457 226 ARG A CB 1737 C CG . ARG A 228 ? 0.8262 0.7709 0.4769 -0.3372 -0.1943 0.1334 226 ARG A CG 1738 C CD . ARG A 228 ? 0.9021 0.9145 0.5603 -0.3596 -0.2163 0.1710 226 ARG A CD 1739 N NE . ARG A 228 ? 1.0295 1.0784 0.6317 -0.3990 -0.2220 0.1610 226 ARG A NE 1740 C CZ . ARG A 228 ? 1.1140 1.2361 0.7100 -0.4259 -0.2431 0.1956 226 ARG A CZ 1741 N NH1 . ARG A 228 ? 1.1113 1.2775 0.7622 -0.4120 -0.2602 0.2477 226 ARG A NH1 1742 N NH2 . ARG A 228 ? 1.1734 1.3274 0.7088 -0.4674 -0.2455 0.1789 226 ARG A NH2 1743 N N . LYS A 229 ? 0.6785 0.5012 0.4146 -0.2591 -0.1649 0.1024 227 LYS A N 1744 C CA . LYS A 229 ? 0.6638 0.4744 0.4353 -0.2436 -0.1605 0.1074 227 LYS A CA 1745 C C . LYS A 229 ? 0.6758 0.5053 0.4509 -0.2560 -0.1680 0.1126 227 LYS A C 1746 O O . LYS A 229 ? 0.6853 0.5138 0.4251 -0.2754 -0.1714 0.0973 227 LYS A O 1747 C CB . LYS A 229 ? 0.6622 0.4332 0.4233 -0.2303 -0.1484 0.0815 227 LYS A CB 1748 C CG . LYS A 229 ? 0.6612 0.4189 0.4531 -0.2162 -0.1395 0.0823 227 LYS A CG 1749 C CD . LYS A 229 ? 0.6681 0.3989 0.4410 -0.2086 -0.1315 0.0592 227 LYS A CD 1750 C CE . LYS A 229 ? 0.7096 0.4303 0.5039 -0.2012 -0.1210 0.0550 227 LYS A CE 1751 N NZ . LYS A 229 ? 0.8163 0.5221 0.5882 -0.1991 -0.1177 0.0395 227 LYS A NZ 1752 N N . THR A 230 ? 0.6590 0.5055 0.4787 -0.2461 -0.1676 0.1332 228 THR A N 1753 C CA . THR A 230 ? 0.6587 0.5312 0.4901 -0.2574 -0.1735 0.1398 228 THR A CA 1754 C C . THR A 230 ? 0.6419 0.4962 0.5038 -0.2407 -0.1593 0.1350 228 THR A C 1755 O O . THR A 230 ? 0.6470 0.4944 0.5464 -0.2204 -0.1480 0.1447 228 THR A O 1756 C CB . THR A 230 ? 0.6658 0.6033 0.5291 -0.2661 -0.1893 0.1784 228 THR A CB 1757 O OG1 . THR A 230 ? 0.6566 0.6065 0.5827 -0.2413 -0.1810 0.2045 228 THR A OG1 1758 C CG2 . THR A 230 ? 0.6936 0.6507 0.5382 -0.2747 -0.1995 0.1926 228 THR A CG2 1759 N N . ILE A 231 ? 0.6386 0.4817 0.4814 -0.2520 -0.1571 0.1182 229 ILE A N 1760 C CA . ILE A 231 ? 0.6216 0.4537 0.4868 -0.2418 -0.1431 0.1130 229 ILE A CA 1761 C C . ILE A 231 ? 0.6172 0.4911 0.5022 -0.2579 -0.1489 0.1258 229 ILE A C 1762 O O . ILE A 231 ? 0.6271 0.5115 0.4819 -0.2844 -0.1599 0.1204 229 ILE A O 1763 C CB . ILE A 231 ? 0.6270 0.4106 0.4517 -0.2422 -0.1338 0.0852 229 ILE A CB 1764 C CG1 . ILE A 231 ? 0.6282 0.3810 0.4344 -0.2285 -0.1296 0.0729 229 ILE A CG1 1765 C CG2 . ILE A 231 ? 0.6628 0.4419 0.5054 -0.2364 -0.1193 0.0813 229 ILE A CG2 1766 C CD1 . ILE A 231 ? 0.6214 0.3373 0.3898 -0.2272 -0.1241 0.0536 229 ILE A CD1 1767 N N . VAL A 232 ? 0.5859 0.4840 0.5229 -0.2435 -0.1386 0.1411 230 VAL A N 1768 C CA . VAL A 232 ? 0.5778 0.5226 0.5426 -0.2566 -0.1407 0.1538 230 VAL A CA 1769 C C . VAL A 232 ? 0.5884 0.5045 0.5419 -0.2586 -0.1230 0.1327 230 VAL A C 1770 O O . VAL A 232 ? 0.5655 0.4664 0.5430 -0.2386 -0.1024 0.1273 230 VAL A O 1771 C CB . VAL A 232 ? 0.5666 0.5676 0.6059 -0.2379 -0.1380 0.1893 230 VAL A CB 1772 C CG1 . VAL A 232 ? 0.5696 0.6229 0.6431 -0.2495 -0.1362 0.2003 230 VAL A CG1 1773 C CG2 . VAL A 232 ? 0.5598 0.6043 0.6106 -0.2412 -0.1597 0.2201 230 VAL A CG2 1774 N N . LEU A 233 ? 0.6176 0.5262 0.5325 -0.2864 -0.1295 0.1205 231 LEU A N 1775 C CA . LEU A 233 ? 0.6325 0.5129 0.5282 -0.2941 -0.1148 0.1044 231 LEU A CA 1776 C C . LEU A 233 ? 0.6357 0.5692 0.5714 -0.3071 -0.1104 0.1178 231 LEU A C 1777 O O . LEU A 233 ? 0.6433 0.6150 0.5792 -0.3354 -0.1240 0.1258 231 LEU A O 1778 C CB . LEU A 233 ? 0.6583 0.4916 0.4925 -0.3163 -0.1195 0.0857 231 LEU A CB 1779 C CG . LEU A 233 ? 0.6869 0.4906 0.5001 -0.3270 -0.1051 0.0761 231 LEU A CG 1780 C CD1 . LEU A 233 ? 0.6754 0.4424 0.4770 -0.3022 -0.0912 0.0680 231 LEU A CD1 1781 C CD2 . LEU A 233 ? 0.7078 0.4703 0.4719 -0.3543 -0.1078 0.0637 231 LEU A CD2 1782 N N . HIS A 234 ? 0.6436 0.5821 0.6122 -0.2889 -0.0893 0.1180 232 HIS A N 1783 C CA . HIS A 234 ? 0.6550 0.6400 0.6608 -0.2994 -0.0781 0.1269 232 HIS A CA 1784 C C . HIS A 234 ? 0.6819 0.6267 0.6408 -0.3187 -0.0666 0.1080 232 HIS A C 1785 O O . HIS A 234 ? 0.6969 0.5849 0.6143 -0.3095 -0.0581 0.0913 232 HIS A O 1786 C CB . HIS A 234 ? 0.6426 0.6534 0.7115 -0.2687 -0.0543 0.1354 232 HIS A CB 1787 C CG . HIS A 234 ? 0.6702 0.7151 0.7938 -0.2441 -0.0605 0.1603 232 HIS A CG 1788 N ND1 . HIS A 234 ? 0.6876 0.8085 0.8595 -0.2500 -0.0780 0.1935 232 HIS A ND1 1789 C CD2 . HIS A 234 ? 0.7013 0.7165 0.8400 -0.2152 -0.0509 0.1601 232 HIS A CD2 1790 C CE1 . HIS A 234 ? 0.6799 0.8156 0.8955 -0.2222 -0.0795 0.2169 232 HIS A CE1 1791 N NE2 . HIS A 234 ? 0.6864 0.7537 0.8827 -0.2011 -0.0615 0.1957 232 HIS A NE2 1792 N N . VAL A 235 ? 0.6985 0.6784 0.6662 -0.3470 -0.0668 0.1142 233 VAL A N 1793 C CA . VAL A 235 ? 0.7323 0.6778 0.6600 -0.3692 -0.0543 0.1022 233 VAL A CA 1794 C C . VAL A 235 ? 0.7488 0.7504 0.7202 -0.3799 -0.0373 0.1112 233 VAL A C 1795 O O . VAL A 235 ? 0.7444 0.8169 0.7636 -0.3928 -0.0452 0.1278 233 VAL A O 1796 C CB . VAL A 235 ? 0.7652 0.6802 0.6444 -0.4049 -0.0689 0.0960 233 VAL A CB 1797 C CG1 . VAL A 235 ? 0.7977 0.6811 0.6451 -0.4304 -0.0537 0.0905 233 VAL A CG1 1798 C CG2 . VAL A 235 ? 0.7681 0.6216 0.6019 -0.3923 -0.0792 0.0844 233 VAL A CG2 1799 N N . VAL A 236 ? 0.7860 0.7628 0.7412 -0.3759 -0.0138 0.1015 234 VAL A N 1800 C CA . VAL A 236 ? 0.8172 0.8455 0.8116 -0.3851 0.0084 0.1071 234 VAL A CA 1801 C C . VAL A 236 ? 0.8672 0.8636 0.8130 -0.4149 0.0206 0.1012 234 VAL A C 1802 O O . VAL A 236 ? 0.9002 0.8325 0.7884 -0.4122 0.0243 0.0919 234 VAL A O 1803 C CB . VAL A 236 ? 0.8063 0.8514 0.8420 -0.3504 0.0356 0.1015 234 VAL A CB 1804 C CG1 . VAL A 236 ? 0.8160 0.9179 0.8955 -0.3592 0.0634 0.1056 234 VAL A CG1 1805 C CG2 . VAL A 236 ? 0.7821 0.8547 0.8732 -0.3190 0.0276 0.1126 234 VAL A CG2 1806 N N . GLN A 237 ? 0.8838 0.9304 0.8557 -0.4446 0.0262 0.1106 235 GLN A N 1807 C CA . GLN A 237 ? 0.9317 0.9584 0.8687 -0.4730 0.0439 0.1090 235 GLN A CA 1808 C C . GLN A 237 ? 0.9267 1.0216 0.9164 -0.4709 0.0722 0.1125 235 GLN A C 1809 O O . GLN A 237 ? 0.8994 1.0743 0.9577 -0.4732 0.0721 0.1244 235 GLN A O 1810 C CB . GLN A 237 ? 0.9729 0.9902 0.8862 -0.5193 0.0312 0.1138 235 GLN A CB 1811 C CG . GLN A 237 ? 1.0216 1.0043 0.8934 -0.5494 0.0506 0.1155 235 GLN A CG 1812 C CD . GLN A 237 ? 1.1175 1.0558 0.9501 -0.5930 0.0408 0.1157 235 GLN A CD 1813 O OE1 . GLN A 237 ? 1.1563 1.0594 0.9692 -0.5946 0.0212 0.1085 235 GLN A OE1 1814 N NE2 . GLN A 237 ? 1.2551 1.1926 1.0753 -0.6314 0.0576 0.1219 235 GLN A NE2 1815 N N . ASP A 238 ? 0.9449 1.0131 0.9028 -0.4672 0.0971 0.1036 236 ASP A N 1816 C CA . ASP A 238 ? 0.9525 1.0799 0.9547 -0.4642 0.1308 0.1016 236 ASP A CA 1817 C C . ASP A 238 ? 0.9716 1.1418 0.9859 -0.5060 0.1379 0.1139 236 ASP A C 1818 O O . ASP A 238 ? 1.0259 1.1517 0.9814 -0.5377 0.1382 0.1168 236 ASP A O 1819 C CB . ASP A 238 ? 0.9774 1.0694 0.9367 -0.4518 0.1572 0.0845 236 ASP A CB 1820 C CG . ASP A 238 ? 0.9963 1.0769 0.9745 -0.4106 0.1629 0.0681 236 ASP A CG 1821 O OD1 . ASP A 238 ? 0.8799 0.9533 0.8807 -0.3914 0.1384 0.0730 236 ASP A OD1 1822 O OD2 . ASP A 238 ? 1.0748 1.1537 1.0438 -0.4008 0.1937 0.0492 236 ASP A OD2 1823 N N . GLU A 239 ? 0.9439 1.2032 1.0389 -0.5059 0.1426 0.1246 237 GLU A N 1824 C CA . GLU A 239 ? 0.9679 1.2897 1.0902 -0.5443 0.1562 0.1355 237 GLU A CA 1825 C C . GLU A 239 ? 0.9872 1.3093 1.0977 -0.5397 0.1974 0.1244 237 GLU A C 1826 O O . GLU A 239 ? 0.9936 1.3116 1.1189 -0.5019 0.2179 0.1102 237 GLU A O 1827 C CB . GLU A 239 ? 0.9419 1.3749 1.1640 -0.5395 0.1515 0.1534 237 GLU A CB 1828 C CG . GLU A 239 ? 0.9119 1.3592 1.1447 -0.5479 0.1091 0.1658 237 GLU A CG 1829 C CD . GLU A 239 ? 0.9493 1.5025 1.2405 -0.5868 0.0965 0.1867 237 GLU A CD 1830 O OE1 . GLU A 239 ? 0.9053 1.5276 1.2397 -0.6038 0.1211 0.1939 237 GLU A OE1 1831 O OE2 . GLU A 239 ? 0.9500 1.5228 1.2422 -0.6039 0.0617 0.1955 237 GLU A OE2 1832 N N . PHE A 240 ? 1.0061 1.3284 1.0843 -0.5813 0.2111 0.1292 238 PHE A N 1833 C CA . PHE A 240 ? 1.0244 1.3388 1.0713 -0.5841 0.2487 0.1191 238 PHE A CA 1834 C C . PHE A 240 ? 1.0259 1.4379 1.1446 -0.5911 0.2851 0.1210 238 PHE A C 1835 O O . PHE A 240 ? 1.0453 1.4946 1.1691 -0.6334 0.2920 0.1338 238 PHE A O 1836 C CB . PHE A 240 ? 1.0757 1.3205 1.0333 -0.6229 0.2448 0.1271 238 PHE A CB 1837 C CG . PHE A 240 ? 1.0551 1.2035 0.9405 -0.6078 0.2196 0.1250 238 PHE A CG 1838 C CD1 . PHE A 240 ? 1.0281 1.1407 0.8671 -0.5850 0.2311 0.1135 238 PHE A CD1 1839 C CD2 . PHE A 240 ? 1.0169 1.1154 0.8817 -0.6182 0.1861 0.1332 238 PHE A CD2 1840 C CE1 . PHE A 240 ? 0.9920 1.0279 0.7713 -0.5706 0.2071 0.1151 238 PHE A CE1 1841 C CE2 . PHE A 240 ? 0.9778 0.9922 0.7832 -0.6010 0.1662 0.1325 238 PHE A CE2 1842 C CZ . PHE A 240 ? 0.9750 0.9619 0.7409 -0.5759 0.1754 0.1258 238 PHE A CZ 1843 N N . GLN A 241 ? 1.0013 1.4516 1.1767 -0.5495 0.3115 0.1074 239 GLN A N 1844 C CA . GLN A 241 ? 1.0094 1.5527 1.2619 -0.5461 0.3545 0.1064 239 GLN A CA 1845 C C . GLN A 241 ? 1.0422 1.5693 1.2799 -0.5220 0.4017 0.0770 239 GLN A C 1846 O O . GLN A 241 ? 1.0617 1.6557 1.3526 -0.5195 0.4468 0.0698 239 GLN A O 1847 C CB . GLN A 241 ? 0.9592 1.5878 1.3263 -0.5163 0.3477 0.1229 239 GLN A CB 1848 C CG . GLN A 241 ? 0.9115 1.5713 1.2958 -0.5441 0.3009 0.1497 239 GLN A CG 1849 C CD . GLN A 241 ? 0.8962 1.5828 1.2557 -0.6052 0.3007 0.1601 239 GLN A CD 1850 O OE1 . GLN A 241 ? 0.9069 1.6450 1.2889 -0.6204 0.3387 0.1585 239 GLN A OE1 1851 N NE2 . GLN A 241 ? 0.8673 1.5161 1.1793 -0.6428 0.2613 0.1690 239 GLN A NE2 1852 N N . ILE B 5 ? 0.5593 0.9606 0.6646 -0.1651 0.1016 -0.0970 3 ILE B N 1853 C CA . ILE B 5 ? 0.5722 0.9299 0.6610 -0.1791 0.0788 -0.0906 3 ILE B CA 1854 C C . ILE B 5 ? 0.5354 0.9022 0.6375 -0.1904 0.0636 -0.0529 3 ILE B C 1855 O O . ILE B 5 ? 0.5089 0.8895 0.6441 -0.1785 0.0633 -0.0369 3 ILE B O 1856 C CB . ILE B 5 ? 0.6031 0.9130 0.7102 -0.1622 0.0687 -0.1073 3 ILE B CB 1857 C CG1 . ILE B 5 ? 0.6444 0.9471 0.7444 -0.1438 0.0862 -0.1496 3 ILE B CG1 1858 C CG2 . ILE B 5 ? 0.6272 0.8923 0.7141 -0.1819 0.0448 -0.1009 3 ILE B CG2 1859 C CD1 . ILE B 5 ? 0.7122 0.9554 0.8210 -0.1291 0.0733 -0.1714 3 ILE B CD1 1860 N N . THR B 6 ? 0.5673 0.9292 0.6433 -0.2132 0.0508 -0.0399 4 THR B N 1861 C CA . THR B 6 ? 0.5545 0.9278 0.6431 -0.2233 0.0364 -0.0062 4 THR B CA 1862 C C . THR B 6 ? 0.5825 0.9270 0.6577 -0.2413 0.0152 0.0008 4 THR B C 1863 O O . THR B 6 ? 0.6208 0.9310 0.6763 -0.2465 0.0103 -0.0210 4 THR B O 1864 C CB . THR B 6 ? 0.5285 0.9398 0.6060 -0.2337 0.0414 0.0113 4 THR B CB 1865 O OG1 . THR B 6 ? 0.5579 0.9787 0.6473 -0.2413 0.0269 0.0396 4 THR B OG1 1866 C CG2 . THR B 6 ? 0.5973 1.0107 0.6331 -0.2516 0.0430 0.0006 4 THR B CG2 1867 N N . THR B 7 ? 0.5632 0.9237 0.6497 -0.2513 0.0029 0.0302 5 THR B N 1868 C CA . THR B 7 ? 0.6100 0.9537 0.6894 -0.2712 -0.0178 0.0424 5 THR B CA 1869 C C . THR B 7 ? 0.6083 0.9843 0.6749 -0.2887 -0.0242 0.0617 5 THR B C 1870 O O . THR B 7 ? 0.5683 0.9789 0.6481 -0.2818 -0.0180 0.0781 5 THR B O 1871 C CB . THR B 7 ? 0.5994 0.9365 0.7097 -0.2680 -0.0291 0.0629 5 THR B CB 1872 O OG1 . THR B 7 ? 0.5204 0.8977 0.6530 -0.2585 -0.0225 0.0838 5 THR B OG1 1873 C CG2 . THR B 7 ? 0.6162 0.9159 0.7407 -0.2511 -0.0277 0.0463 5 THR B CG2 1874 N N . PRO B 8 ? 0.6522 1.0155 0.6936 -0.3109 -0.0383 0.0592 6 PRO B N 1875 C CA . PRO B 8 ? 0.6538 1.0491 0.6837 -0.3274 -0.0468 0.0778 6 PRO B CA 1876 C C . PRO B 8 ? 0.6316 1.0588 0.6910 -0.3304 -0.0571 0.1097 6 PRO B C 1877 O O . PRO B 8 ? 0.6205 1.0491 0.7075 -0.3204 -0.0561 0.1194 6 PRO B O 1878 C CB . PRO B 8 ? 0.7067 1.0770 0.7032 -0.3519 -0.0619 0.0652 6 PRO B CB 1879 C CG . PRO B 8 ? 0.7626 1.0863 0.7460 -0.3443 -0.0557 0.0324 6 PRO B CG 1880 C CD . PRO B 8 ? 0.7088 1.0257 0.7273 -0.3201 -0.0458 0.0340 6 PRO B CD 1881 N N . GLU B 9 ? 0.6457 1.1013 0.6984 -0.3445 -0.0674 0.1259 7 GLU B N 1882 C CA . GLU B 9 ? 0.6382 1.1330 0.7198 -0.3465 -0.0765 0.1548 7 GLU B CA 1883 C C . GLU B 9 ? 0.6695 1.1583 0.7529 -0.3707 -0.0961 0.1642 7 GLU B C 1884 O O . GLU B 9 ? 0.6993 1.1829 0.7602 -0.3925 -0.1101 0.1622 7 GLU B O 1885 C CB . GLU B 9 ? 0.6324 1.1640 0.7121 -0.3474 -0.0799 0.1696 7 GLU B CB 1886 C CG . GLU B 9 ? 0.6524 1.1790 0.7120 -0.3373 -0.0671 0.1584 7 GLU B CG 1887 C CD . GLU B 9 ? 0.7691 1.2802 0.7864 -0.3569 -0.0730 0.1454 7 GLU B CD 1888 O OE1 . GLU B 9 ? 0.8483 1.3712 0.8553 -0.3773 -0.0914 0.1563 7 GLU B OE1 1889 O OE2 . GLU B 9 ? 0.7455 1.2366 0.7393 -0.3527 -0.0592 0.1241 7 GLU B OE2 1890 N N . GLN B 10 ? 0.6718 1.1621 0.7804 -0.3694 -0.0983 0.1759 8 GLN B N 1891 C CA . GLN B 10 ? 0.7072 1.1902 0.8189 -0.3960 -0.1181 0.1878 8 GLN B CA 1892 C C . GLN B 10 ? 0.6995 1.2206 0.8102 -0.4172 -0.1337 0.2049 8 GLN B C 1893 O O . GLN B 10 ? 0.6625 1.2340 0.7917 -0.4075 -0.1300 0.2213 8 GLN B O 1894 C CB . GLN B 10 ? 0.6896 1.1867 0.8324 -0.3933 -0.1183 0.2074 8 GLN B CB 1895 C CG . GLN B 10 ? 0.7499 1.2008 0.8928 -0.3792 -0.1109 0.1931 8 GLN B CG 1896 C CD . GLN B 10 ? 0.7925 1.2588 0.9626 -0.3792 -0.1130 0.2159 8 GLN B CD 1897 O OE1 . GLN B 10 ? 0.7807 1.2426 0.9615 -0.3580 -0.1011 0.2129 8 GLN B OE1 1898 N NE2 . GLN B 10 ? 0.7645 1.2529 0.9453 -0.4050 -0.1287 0.2403 8 GLN B NE2 1899 N N . ARG B 11 ? 0.7376 1.2320 0.8272 -0.4459 -0.1525 0.1999 9 ARG B N 1900 C CA . ARG B 11 ? 0.7491 1.2763 0.8348 -0.4714 -0.1717 0.2152 9 ARG B CA 1901 C C . ARG B 11 ? 0.7401 1.2933 0.8530 -0.4946 -0.1880 0.2419 9 ARG B C 1902 O O . ARG B 11 ? 0.7731 1.2853 0.8800 -0.5136 -0.1995 0.2387 9 ARG B O 1903 C CB . ARG B 11 ? 0.8094 1.2928 0.8499 -0.4926 -0.1842 0.1915 9 ARG B CB 1904 C CG . ARG B 11 ? 0.8794 1.3422 0.8888 -0.4736 -0.1672 0.1650 9 ARG B CG 1905 C CD . ARG B 11 ? 0.9998 1.4319 0.9603 -0.4959 -0.1788 0.1422 9 ARG B CD 1906 N NE . ARG B 11 ? 1.0767 1.4426 1.0118 -0.4967 -0.1761 0.1084 9 ARG B NE 1907 C CZ . ARG B 11 ? 1.1483 1.4786 1.0365 -0.5086 -0.1794 0.0777 9 ARG B CZ 1908 N NH1 . ARG B 11 ? 1.1885 1.5439 1.0465 -0.5240 -0.1866 0.0789 9 ARG B NH1 1909 N NH2 . ARG B 11 ? 1.1953 1.4649 1.0661 -0.5043 -0.1761 0.0451 9 ARG B NH2 1910 N N . ILE B 12 ? 0.6925 1.3152 0.8369 -0.4930 -0.1895 0.2688 10 ILE B N 1911 C CA . ILE B 12 ? 0.6746 1.3403 0.8495 -0.5163 -0.2034 0.2979 10 ILE B CA 1912 C C . ILE B 12 ? 0.6673 1.3786 0.8475 -0.5412 -0.2240 0.3149 10 ILE B C 1913 O O . ILE B 12 ? 0.6365 1.3964 0.8301 -0.5259 -0.2207 0.3233 10 ILE B O 1914 C CB . ILE B 12 ? 0.6205 1.3439 0.8362 -0.4937 -0.1867 0.3175 10 ILE B CB 1915 C CG1 . ILE B 12 ? 0.6074 1.2904 0.8193 -0.4716 -0.1689 0.3040 10 ILE B CG1 1916 C CG2 . ILE B 12 ? 0.6315 1.4091 0.8784 -0.5205 -0.1999 0.3489 10 ILE B CG2 1917 C CD1 . ILE B 12 ? 0.6341 1.2450 0.8234 -0.4901 -0.1793 0.2919 10 ILE B CD1 1918 N N . GLU B 13 ? 0.6970 1.3908 0.8683 -0.5801 -0.2473 0.3211 11 GLU B N 1919 C CA . GLU B 13 ? 0.6958 1.4323 0.8724 -0.6114 -0.2718 0.3390 11 GLU B CA 1920 C C . GLU B 13 ? 0.6794 1.4779 0.8992 -0.6339 -0.2818 0.3738 11 GLU B C 1921 O O . GLU B 13 ? 0.6983 1.4698 0.9201 -0.6558 -0.2889 0.3804 11 GLU B O 1922 C CB . GLU B 13 ? 0.7476 1.4190 0.8779 -0.6441 -0.2938 0.3183 11 GLU B CB 1923 C CG . GLU B 13 ? 0.7560 1.4665 0.8815 -0.6726 -0.3187 0.3307 11 GLU B CG 1924 C CD . GLU B 13 ? 0.8308 1.4735 0.9006 -0.7013 -0.3384 0.3032 11 GLU B CD 1925 O OE1 . GLU B 13 ? 0.9206 1.4919 0.9678 -0.7155 -0.3436 0.2841 11 GLU B OE1 1926 O OE2 . GLU B 13 ? 0.7804 1.4405 0.8281 -0.7093 -0.3497 0.3002 11 GLU B OE2 1927 N N . LYS B 14 ? 0.6402 1.5242 0.8959 -0.6282 -0.2830 0.3971 12 LYS B N 1928 C CA . LYS B 14 ? 0.6210 1.5832 0.9235 -0.6468 -0.2894 0.4315 12 LYS B CA 1929 C C . LYS B 14 ? 0.6272 1.6566 0.9504 -0.6701 -0.3123 0.4530 12 LYS B C 1930 O O . LYS B 14 ? 0.6151 1.6418 0.9214 -0.6645 -0.3209 0.4441 12 LYS B O 1931 C CB . LYS B 14 ? 0.5555 1.5760 0.8968 -0.6083 -0.2615 0.4411 12 LYS B CB 1932 C CG . LYS B 14 ? 0.5448 1.5199 0.8767 -0.5961 -0.2435 0.4318 12 LYS B CG 1933 C CD . LYS B 14 ? 0.5595 1.5096 0.8881 -0.6388 -0.2602 0.4469 12 LYS B CD 1934 C CE . LYS B 14 ? 0.5418 1.4807 0.8771 -0.6272 -0.2430 0.4514 12 LYS B CE 1935 N NZ . LYS B 14 ? 0.4939 1.5316 0.8725 -0.6108 -0.2252 0.4739 12 LYS B NZ 1936 N N . ALA B 15 ? 0.6381 1.7318 0.9990 -0.6984 -0.3230 0.4836 13 ALA B N 1937 C CA . ALA B 15 ? 0.6419 1.8187 1.0355 -0.7201 -0.3439 0.5097 13 ALA B CA 1938 C C . ALA B 15 ? 0.5878 1.8629 1.0353 -0.6812 -0.3247 0.5258 13 ALA B C 1939 O O . ALA B 15 ? 0.5635 1.8458 1.0237 -0.6440 -0.2962 0.5190 13 ALA B O 1940 C CB . ALA B 15 ? 0.6662 1.8680 1.0758 -0.7733 -0.3662 0.5358 13 ALA B CB 1941 N N . LYS B 16 ? 0.5728 1.9239 1.0525 -0.6902 -0.3420 0.5464 14 LYS B N 1942 C CA . LYS B 16 ? 0.5234 1.9730 1.0598 -0.6523 -0.3279 0.5617 14 LYS B CA 1943 C C . LYS B 16 ? 0.4985 2.0226 1.0807 -0.6526 -0.3105 0.5816 14 LYS B C 1944 O O . LYS B 16 ? 0.5286 2.0427 1.1048 -0.6923 -0.3173 0.5934 14 LYS B O 1945 C CB . LYS B 16 ? 0.5418 2.0593 1.1059 -0.6664 -0.3552 0.5826 14 LYS B CB 1946 C CG . LYS B 16 ? 0.4884 2.1081 1.1156 -0.6239 -0.3445 0.5980 14 LYS B CG 1947 C CD . LYS B 16 ? 0.5058 2.1899 1.1603 -0.6423 -0.3765 0.6214 14 LYS B CD 1948 C CE . LYS B 16 ? 0.4886 2.2936 1.2207 -0.6069 -0.3685 0.6428 14 LYS B CE 1949 N NZ . LYS B 16 ? 0.4992 2.3790 1.2661 -0.6289 -0.4026 0.6707 14 LYS B NZ 1950 N N . GLY B 17 ? 0.4541 2.0493 1.0795 -0.6069 -0.2878 0.5842 15 GLY B N 1951 C CA . GLY B 17 ? 0.4241 2.1208 1.1030 -0.6021 -0.2705 0.6051 15 GLY B CA 1952 C C . GLY B 17 ? 0.4151 2.0871 1.0790 -0.6061 -0.2487 0.6013 15 GLY B C 1953 O O . GLY B 17 ? 0.4012 2.1585 1.1039 -0.6065 -0.2336 0.6194 15 GLY B O 1954 N N . GLU B 18 ? 0.4344 1.9940 1.0428 -0.6091 -0.2473 0.5785 16 GLU B N 1955 C CA . GLU B 18 ? 0.4418 1.9672 1.0319 -0.6162 -0.2316 0.5767 16 GLU B CA 1956 C C . GLU B 18 ? 0.4000 1.8680 0.9650 -0.5688 -0.2052 0.5463 16 GLU B C 1957 O O . GLU B 18 ? 0.3697 1.8439 0.9416 -0.5265 -0.1944 0.5295 16 GLU B O 1958 C CB . GLU B 18 ? 0.5018 1.9475 1.0536 -0.6682 -0.2561 0.5812 16 GLU B CB 1959 C CG . GLU B 18 ? 0.5271 1.8528 1.0232 -0.6635 -0.2653 0.5494 16 GLU B CG 1960 C CD . GLU B 18 ? 0.5902 1.8665 1.0606 -0.7151 -0.2994 0.5540 16 GLU B CD 1961 O OE1 . GLU B 18 ? 0.5016 1.8451 1.0003 -0.7453 -0.3192 0.5784 16 GLU B OE1 1962 O OE2 . GLU B 18 ? 0.6383 1.8106 1.0614 -0.7247 -0.3066 0.5321 16 GLU B OE2 1963 N N . THR B 19 ? 0.4053 1.8180 0.9429 -0.5771 -0.1968 0.5412 17 THR B N 1964 C CA . THR B 19 ? 0.3792 1.7586 0.9012 -0.5351 -0.1701 0.5180 17 THR B CA 1965 C C . THR B 19 ? 0.4121 1.6732 0.8834 -0.5352 -0.1738 0.4939 17 THR B C 1966 O O . THR B 19 ? 0.4508 1.6602 0.9005 -0.5701 -0.1881 0.5008 17 THR B O 1967 C CB . THR B 19 ? 0.3604 1.7999 0.9018 -0.5348 -0.1506 0.5336 17 THR B CB 1968 O OG1 . THR B 19 ? 0.3520 1.9082 0.9426 -0.5195 -0.1388 0.5473 17 THR B OG1 1969 C CG2 . THR B 19 ? 0.2913 1.6852 0.8095 -0.4989 -0.1280 0.5097 17 THR B CG2 1970 N N . ALA B 20 ? 0.4084 1.6293 0.8635 -0.4953 -0.1608 0.4661 18 ALA B N 1971 C CA . ALA B 20 ? 0.4315 1.5483 0.8417 -0.4906 -0.1619 0.4407 18 ALA B CA 1972 C C . ALA B 20 ? 0.4267 1.5259 0.8302 -0.4696 -0.1410 0.4323 18 ALA B C 1973 O O . ALA B 20 ? 0.4276 1.5768 0.8512 -0.4377 -0.1211 0.4292 18 ALA B O 1974 C CB . ALA B 20 ? 0.4304 1.5168 0.8259 -0.4641 -0.1610 0.4184 18 ALA B CB 1975 N N . TYR B 21 ? 0.4579 1.4854 0.8337 -0.4869 -0.1474 0.4278 19 TYR B N 1976 C CA . TYR B 21 ? 0.4547 1.4515 0.8190 -0.4694 -0.1319 0.4196 19 TYR B CA 1977 C C . TYR B 21 ? 0.4318 1.3463 0.7654 -0.4464 -0.1266 0.3884 19 TYR B C 1978 O O . TYR B 21 ? 0.4240 1.2679 0.7327 -0.4622 -0.1402 0.3780 19 TYR B O 1979 C CB . TYR B 21 ? 0.5000 1.4792 0.8604 -0.5036 -0.1436 0.4411 19 TYR B CB 1980 C CG . TYR B 21 ? 0.4967 1.4417 0.8446 -0.4878 -0.1319 0.4353 19 TYR B CG 1981 C CD1 . TYR B 21 ? 0.5224 1.5246 0.8837 -0.4637 -0.1104 0.4380 19 TYR B CD1 1982 C CD2 . TYR B 21 ? 0.5290 1.3859 0.8522 -0.4960 -0.1430 0.4261 19 TYR B CD2 1983 C CE1 . TYR B 21 ? 0.5141 1.4883 0.8627 -0.4512 -0.1017 0.4341 19 TYR B CE1 1984 C CE2 . TYR B 21 ? 0.5390 1.3685 0.8543 -0.4814 -0.1345 0.4235 19 TYR B CE2 1985 C CZ . TYR B 21 ? 0.5338 1.4232 0.8610 -0.4604 -0.1145 0.4286 19 TYR B CZ 1986 O OH . TYR B 21 ? 0.6091 1.4750 0.9271 -0.4473 -0.1079 0.4269 19 TYR B OH 1987 N N . LEU B 22 ? 0.4143 1.3407 0.7509 -0.4093 -0.1064 0.3729 20 LEU B N 1988 C CA . LEU B 22 ? 0.4208 1.2823 0.7330 -0.3864 -0.0993 0.3448 20 LEU B CA 1989 C C . LEU B 22 ? 0.3912 1.2360 0.6992 -0.3715 -0.0865 0.3402 20 LEU B C 1990 O O . LEU B 22 ? 0.3608 1.2511 0.6826 -0.3509 -0.0714 0.3413 20 LEU B O 1991 C CB . LEU B 22 ? 0.4073 1.2895 0.7249 -0.3577 -0.0898 0.3312 20 LEU B CB 1992 C CG . LEU B 22 ? 0.4755 1.3739 0.7961 -0.3698 -0.1043 0.3364 20 LEU B CG 1993 C CD1 . LEU B 22 ? 0.4232 1.3526 0.7576 -0.3387 -0.0954 0.3299 20 LEU B CD1 1994 C CD2 . LEU B 22 ? 0.4817 1.3101 0.7682 -0.3856 -0.1165 0.3214 20 LEU B CD2 1995 N N . PRO B 23 ? 0.4213 1.2018 0.7109 -0.3817 -0.0939 0.3348 21 PRO B N 1996 C CA . PRO B 23 ? 0.4325 1.1918 0.7181 -0.3693 -0.0859 0.3323 21 PRO B CA 1997 C C . PRO B 23 ? 0.4053 1.1398 0.6820 -0.3367 -0.0708 0.3064 21 PRO B C 1998 O O . PRO B 23 ? 0.3857 1.0769 0.6480 -0.3295 -0.0710 0.2859 21 PRO B O 1999 C CB . PRO B 23 ? 0.4819 1.1758 0.7541 -0.3915 -0.1033 0.3349 21 PRO B CB 2000 C CG . PRO B 23 ? 0.5005 1.1600 0.7588 -0.4013 -0.1132 0.3203 21 PRO B CG 2001 C CD . PRO B 23 ? 0.4481 1.1700 0.7195 -0.4052 -0.1122 0.3294 21 PRO B CD 2002 N N . CYS B 24 ? 0.3986 1.1640 0.6829 -0.3196 -0.0580 0.3082 22 CYS B N 2003 C CA . CYS B 24 ? 0.3924 1.1394 0.6703 -0.2911 -0.0448 0.2863 22 CYS B CA 2004 C C . CYS B 24 ? 0.3798 1.1395 0.6596 -0.2840 -0.0390 0.2924 22 CYS B C 2005 O O . CYS B 24 ? 0.3532 1.1580 0.6389 -0.2695 -0.0272 0.2915 22 CYS B O 2006 C CB . CYS B 24 ? 0.3807 1.1609 0.6652 -0.2715 -0.0342 0.2755 22 CYS B CB 2007 S SG . CYS B 24 ? 0.3372 1.0887 0.6130 -0.2423 -0.0217 0.2490 22 CYS B SG 2008 N N . LYS B 25 ? 0.4047 1.1224 0.6785 -0.2941 -0.0488 0.2980 23 LYS B N 2009 C CA . LYS B 25 ? 0.4196 1.1427 0.6936 -0.2908 -0.0480 0.3076 23 LYS B CA 2010 C C . LYS B 25 ? 0.4133 1.1007 0.6824 -0.2682 -0.0421 0.2861 23 LYS B C 2011 O O . LYS B 25 ? 0.4114 1.0502 0.6765 -0.2631 -0.0446 0.2695 23 LYS B O 2012 C CB . LYS B 25 ? 0.4609 1.1608 0.7352 -0.3165 -0.0658 0.3321 23 LYS B CB 2013 C CG . LYS B 25 ? 0.4978 1.2420 0.7789 -0.3441 -0.0726 0.3590 23 LYS B CG 2014 C CD . LYS B 25 ? 0.5573 1.2675 0.8376 -0.3722 -0.0933 0.3844 23 LYS B CD 2015 C CE . LYS B 25 ? 0.6066 1.3648 0.8948 -0.4041 -0.1010 0.4149 23 LYS B CE 2016 N NZ . LYS B 25 ? 0.6791 1.3937 0.9656 -0.4350 -0.1248 0.4409 23 LYS B NZ 2017 N N . PHE B 26 ? 0.3943 1.1106 0.6635 -0.2556 -0.0340 0.2859 24 PHE B N 2018 C CA . PHE B 26 ? 0.3727 1.0664 0.6398 -0.2353 -0.0283 0.2669 24 PHE B CA 2019 C C . PHE B 26 ? 0.3756 1.0787 0.6420 -0.2340 -0.0323 0.2784 24 PHE B C 2020 O O . PHE B 26 ? 0.3842 1.1270 0.6479 -0.2445 -0.0337 0.2980 24 PHE B O 2021 C CB . PHE B 26 ? 0.3448 1.0601 0.6103 -0.2170 -0.0140 0.2466 24 PHE B CB 2022 C CG . PHE B 26 ? 0.3442 1.1154 0.6092 -0.2127 -0.0059 0.2513 24 PHE B CG 2023 C CD1 . PHE B 26 ? 0.3776 1.1659 0.6370 -0.2041 -0.0023 0.2486 24 PHE B CD1 2024 C CD2 . PHE B 26 ? 0.3998 1.2096 0.6702 -0.2165 -0.0020 0.2571 24 PHE B CD2 2025 C CE1 . PHE B 26 ? 0.4321 1.2729 0.6876 -0.1992 0.0064 0.2488 24 PHE B CE1 2026 C CE2 . PHE B 26 ? 0.4701 1.3358 0.7415 -0.2094 0.0077 0.2581 24 PHE B CE2 2027 C CZ . PHE B 26 ? 0.4698 1.3501 0.7318 -0.2006 0.0126 0.2526 24 PHE B CZ 2028 N N . THR B 27 ? 0.3738 1.0433 0.6431 -0.2217 -0.0343 0.2667 25 THR B N 2029 C CA . THR B 27 ? 0.3762 1.0506 0.6467 -0.2181 -0.0402 0.2757 25 THR B CA 2030 C C . THR B 27 ? 0.3606 1.0425 0.6305 -0.1990 -0.0303 0.2537 25 THR B C 2031 O O . THR B 27 ? 0.3627 1.0154 0.6391 -0.1880 -0.0268 0.2351 25 THR B O 2032 C CB . THR B 27 ? 0.4008 1.0268 0.6817 -0.2199 -0.0552 0.2835 25 THR B CB 2033 O OG1 . THR B 27 ? 0.4592 1.0641 0.7401 -0.2386 -0.0661 0.2994 25 THR B OG1 2034 C CG2 . THR B 27 ? 0.3864 1.0220 0.6699 -0.2196 -0.0658 0.3011 25 THR B CG2 2035 N N . LEU B 28 ? 0.3485 1.0711 0.6094 -0.1968 -0.0259 0.2556 26 LEU B N 2036 C CA . LEU B 28 ? 0.3302 1.0599 0.5884 -0.1817 -0.0188 0.2348 26 LEU B CA 2037 C C . LEU B 28 ? 0.3317 1.0433 0.5988 -0.1771 -0.0285 0.2368 26 LEU B C 2038 O O . LEU B 28 ? 0.3554 1.0628 0.6266 -0.1847 -0.0415 0.2581 26 LEU B O 2039 C CB . LEU B 28 ? 0.3263 1.1036 0.5692 -0.1803 -0.0117 0.2323 26 LEU B CB 2040 C CG . LEU B 28 ? 0.3410 1.1399 0.5808 -0.1772 0.0002 0.2235 26 LEU B CG 2041 C CD1 . LEU B 28 ? 0.2433 1.0939 0.4692 -0.1744 0.0081 0.2206 26 LEU B CD1 2042 C CD2 . LEU B 28 ? 0.3573 1.1284 0.6022 -0.1638 0.0069 0.1992 26 LEU B CD2 2043 N N . SER B 29 ? 0.3131 1.0149 0.5855 -0.1651 -0.0233 0.2160 27 SER B N 2044 C CA . SER B 29 ? 0.3183 1.0128 0.6031 -0.1592 -0.0315 0.2159 27 SER B CA 2045 C C . SER B 29 ? 0.2905 1.0160 0.5637 -0.1576 -0.0317 0.2094 27 SER B C 2046 O O . SER B 29 ? 0.2724 1.0144 0.5305 -0.1561 -0.0223 0.1959 27 SER B O 2047 C CB . SER B 29 ? 0.3197 0.9855 0.6214 -0.1497 -0.0262 0.1983 27 SER B CB 2048 O OG . SER B 29 ? 0.3777 1.0131 0.6881 -0.1509 -0.0285 0.2030 27 SER B OG 2049 N N . PRO B 30 ? 0.2787 1.0116 0.5593 -0.1573 -0.0439 0.2188 28 PRO B N 2050 C CA . PRO B 30 ? 0.2869 1.0502 0.5532 -0.1590 -0.0478 0.2148 28 PRO B CA 2051 C C . PRO B 30 ? 0.2764 1.0407 0.5359 -0.1534 -0.0376 0.1867 28 PRO B C 2052 O O . PRO B 30 ? 0.2824 1.0695 0.5207 -0.1553 -0.0363 0.1773 28 PRO B O 2053 C CB . PRO B 30 ? 0.3066 1.0682 0.5929 -0.1571 -0.0638 0.2272 28 PRO B CB 2054 C CG . PRO B 30 ? 0.2855 1.0212 0.5895 -0.1566 -0.0711 0.2466 28 PRO B CG 2055 C CD . PRO B 30 ? 0.2816 0.9933 0.5853 -0.1547 -0.0567 0.2340 28 PRO B CD 2056 N N . GLU B 31 ? 0.2710 1.0098 0.5469 -0.1473 -0.0309 0.1733 29 GLU B N 2057 C CA . GLU B 31 ? 0.2799 1.0135 0.5511 -0.1446 -0.0236 0.1501 29 GLU B CA 2058 C C . GLU B 31 ? 0.2975 1.0355 0.5477 -0.1430 -0.0141 0.1402 29 GLU B C 2059 O O . GLU B 31 ? 0.3190 1.0599 0.5561 -0.1408 -0.0118 0.1227 29 GLU B O 2060 C CB . GLU B 31 ? 0.2703 0.9780 0.5606 -0.1412 -0.0166 0.1417 29 GLU B CB 2061 C CG . GLU B 31 ? 0.3476 1.0503 0.6647 -0.1382 -0.0217 0.1496 29 GLU B CG 2062 C CD . GLU B 31 ? 0.4349 1.1208 0.7596 -0.1356 -0.0215 0.1617 29 GLU B CD 2063 O OE1 . GLU B 31 ? 0.4418 1.1075 0.7677 -0.1342 -0.0118 0.1542 29 GLU B OE1 2064 O OE2 . GLU B 31 ? 0.5010 1.1921 0.8293 -0.1364 -0.0328 0.1795 29 GLU B OE2 2065 N N . ASP B 32 ? 0.3001 1.0378 0.5490 -0.1438 -0.0097 0.1517 30 ASP B N 2066 C CA . ASP B 32 ? 0.3037 1.0434 0.5430 -0.1401 0.0004 0.1437 30 ASP B CA 2067 C C . ASP B 32 ? 0.3188 1.0916 0.5378 -0.1383 0.0027 0.1384 30 ASP B C 2068 O O . ASP B 32 ? 0.3263 1.1271 0.5378 -0.1432 0.0033 0.1531 30 ASP B O 2069 C CB . ASP B 32 ? 0.3033 1.0366 0.5494 -0.1443 0.0025 0.1591 30 ASP B CB 2070 C CG . ASP B 32 ? 0.3053 1.0048 0.5675 -0.1448 0.0019 0.1591 30 ASP B CG 2071 O OD1 . ASP B 32 ? 0.4381 1.1224 0.7058 -0.1409 0.0044 0.1453 30 ASP B OD1 2072 O OD2 . ASP B 32 ? 0.1959 0.8846 0.4642 -0.1501 -0.0011 0.1723 30 ASP B OD2 2073 N N . GLN B 33 ? 0.3204 1.0901 0.5301 -0.1319 0.0042 0.1164 31 GLN B N 2074 C CA . GLN B 33 ? 0.3274 1.1269 0.5147 -0.1288 0.0056 0.1048 31 GLN B CA 2075 C C . GLN B 33 ? 0.3189 1.1184 0.4990 -0.1153 0.0155 0.0834 31 GLN B C 2076 O O . GLN B 33 ? 0.3462 1.1755 0.5083 -0.1095 0.0203 0.0720 31 GLN B O 2077 C CB . GLN B 33 ? 0.3389 1.1345 0.5183 -0.1328 -0.0043 0.0939 31 GLN B CB 2078 C CG . GLN B 33 ? 0.4018 1.2353 0.5613 -0.1402 -0.0107 0.1022 31 GLN B CG 2079 C CD . GLN B 33 ? 0.3889 1.2333 0.5597 -0.1504 -0.0183 0.1345 31 GLN B CD 2080 O OE1 . GLN B 33 ? 0.3296 1.2071 0.4867 -0.1571 -0.0188 0.1509 31 GLN B OE1 2081 N NE2 . GLN B 33 ? 0.3660 1.1825 0.5622 -0.1516 -0.0243 0.1438 31 GLN B NE2 2082 N N . GLY B 34 ? 0.2968 1.0643 0.4909 -0.1094 0.0182 0.0778 32 GLY B N 2083 C CA . GLY B 34 ? 0.2943 1.0552 0.4864 -0.0943 0.0246 0.0589 32 GLY B CA 2084 C C . GLY B 34 ? 0.2793 1.0783 0.4718 -0.0862 0.0344 0.0639 32 GLY B C 2085 O O . GLY B 34 ? 0.2706 1.1022 0.4624 -0.0956 0.0362 0.0836 32 GLY B O 2086 N N . PRO B 35 ? 0.2691 1.0658 0.4648 -0.0688 0.0399 0.0471 33 PRO B N 2087 C CA . PRO B 35 ? 0.2618 1.1030 0.4634 -0.0606 0.0498 0.0530 33 PRO B CA 2088 C C . PRO B 35 ? 0.2387 1.0807 0.4579 -0.0720 0.0487 0.0799 33 PRO B C 2089 O O . PRO B 35 ? 0.2465 1.0487 0.4761 -0.0747 0.0432 0.0839 33 PRO B O 2090 C CB . PRO B 35 ? 0.2705 1.1007 0.4780 -0.0365 0.0533 0.0287 33 PRO B CB 2091 C CG . PRO B 35 ? 0.2884 1.0730 0.4834 -0.0338 0.0452 0.0062 33 PRO B CG 2092 C CD . PRO B 35 ? 0.2786 1.0361 0.4738 -0.0557 0.0363 0.0230 33 PRO B CD 2093 N N . LEU B 36 ? 0.2185 1.1056 0.4387 -0.0810 0.0531 0.0985 34 LEU B N 2094 C CA . LEU B 36 ? 0.1991 1.0898 0.4351 -0.0928 0.0511 0.1227 34 LEU B CA 2095 C C . LEU B 36 ? 0.2134 1.1117 0.4661 -0.0779 0.0551 0.1169 34 LEU B C 2096 O O . LEU B 36 ? 0.2147 1.1450 0.4699 -0.0593 0.0634 0.1016 34 LEU B O 2097 C CB . LEU B 36 ? 0.2051 1.1436 0.4390 -0.1086 0.0532 0.1459 34 LEU B CB 2098 C CG . LEU B 36 ? 0.1899 1.1316 0.4401 -0.1227 0.0493 0.1696 34 LEU B CG 2099 C CD1 . LEU B 36 ? 0.1355 1.0263 0.3857 -0.1384 0.0378 0.1816 34 LEU B CD1 2100 C CD2 . LEU B 36 ? 0.2136 1.2149 0.4647 -0.1359 0.0534 0.1904 34 LEU B CD2 2101 N N . ASP B 37 ? 0.2134 1.0837 0.4777 -0.0853 0.0486 0.1288 35 ASP B N 2102 C CA . ASP B 37 ? 0.2175 1.0907 0.4987 -0.0729 0.0486 0.1271 35 ASP B CA 2103 C C . ASP B 37 ? 0.1954 1.0576 0.4859 -0.0892 0.0413 0.1477 35 ASP B C 2104 O O . ASP B 37 ? 0.1889 1.0075 0.4726 -0.1007 0.0348 0.1511 35 ASP B O 2105 C CB . ASP B 37 ? 0.2377 1.0667 0.5173 -0.0565 0.0452 0.1067 35 ASP B CB 2106 C CG . ASP B 37 ? 0.3086 1.1391 0.6067 -0.0409 0.0428 0.1058 35 ASP B CG 2107 O OD1 . ASP B 37 ? 0.3594 1.1937 0.6675 -0.0520 0.0378 0.1246 35 ASP B OD1 2108 O OD2 . ASP B 37 ? 0.3681 1.1952 0.6708 -0.0175 0.0444 0.0863 35 ASP B OD2 2109 N N . ILE B 38 ? 0.2035 1.1090 0.5097 -0.0900 0.0427 0.1603 36 ILE B N 2110 C CA . ILE B 38 ? 0.2032 1.1034 0.5174 -0.1074 0.0341 0.1797 36 ILE B CA 2111 C C . ILE B 38 ? 0.2191 1.1310 0.5521 -0.0940 0.0308 0.1800 36 ILE B C 2112 O O . ILE B 38 ? 0.2225 1.1734 0.5712 -0.0731 0.0370 0.1722 36 ILE B O 2113 C CB . ILE B 38 ? 0.1946 1.1370 0.5132 -0.1282 0.0340 0.2015 36 ILE B CB 2114 C CG1 . ILE B 38 ? 0.2053 1.1362 0.5066 -0.1417 0.0345 0.2056 36 ILE B CG1 2115 C CG2 . ILE B 38 ? 0.1733 1.1025 0.4974 -0.1479 0.0226 0.2186 36 ILE B CG2 2116 C CD1 . ILE B 38 ? 0.1491 1.1390 0.4527 -0.1528 0.0394 0.2216 36 ILE B CD1 2117 N N . GLU B 39 ? 0.2273 1.1068 0.5586 -0.1058 0.0203 0.1887 37 GLU B N 2118 C CA . GLU B 39 ? 0.2397 1.1238 0.5870 -0.0954 0.0132 0.1922 37 GLU B CA 2119 C C . GLU B 39 ? 0.2215 1.0968 0.5664 -0.1192 0.0014 0.2103 37 GLU B C 2120 O O . GLU B 39 ? 0.2517 1.0802 0.5766 -0.1335 -0.0036 0.2095 37 GLU B O 2121 C CB . GLU B 39 ? 0.2630 1.1001 0.6041 -0.0780 0.0106 0.1767 37 GLU B CB 2122 C CG . GLU B 39 ? 0.3225 1.1702 0.6853 -0.0567 0.0040 0.1773 37 GLU B CG 2123 C CD . GLU B 39 ? 0.4140 1.2064 0.7693 -0.0448 -0.0027 0.1672 37 GLU B CD 2124 O OE1 . GLU B 39 ? 0.4652 1.2121 0.7982 -0.0607 -0.0049 0.1662 37 GLU B OE1 2125 O OE2 . GLU B 39 ? 0.4570 1.2525 0.8306 -0.0194 -0.0064 0.1608 37 GLU B OE2 2126 N N . TRP B 40 ? 0.2023 1.1263 0.5674 -0.1240 -0.0029 0.2257 38 TRP B N 2127 C CA . TRP B 40 ? 0.1835 1.1034 0.5467 -0.1476 -0.0168 0.2426 38 TRP B CA 2128 C C . TRP B 40 ? 0.2230 1.1373 0.5960 -0.1362 -0.0274 0.2457 38 TRP B C 2129 O O . TRP B 40 ? 0.2486 1.1968 0.6477 -0.1117 -0.0263 0.2447 38 TRP B O 2130 C CB . TRP B 40 ? 0.1315 1.1082 0.5118 -0.1654 -0.0194 0.2615 38 TRP B CB 2131 C CG . TRP B 40 ? -0.0731 0.8969 0.2929 -0.1880 -0.0166 0.2667 38 TRP B CG 2132 C CD1 . TRP B 40 ? 0.0027 0.9965 0.3696 -0.1836 -0.0047 0.2645 38 TRP B CD1 2133 C CD2 . TRP B 40 ? -0.1238 0.8134 0.2247 -0.2188 -0.0276 0.2759 38 TRP B CD2 2134 N NE1 . TRP B 40 ? -0.0938 0.8824 0.2590 -0.2095 -0.0089 0.2747 38 TRP B NE1 2135 C CE2 . TRP B 40 ? 0.0055 0.9442 0.3478 -0.2303 -0.0229 0.2804 38 TRP B CE2 2136 C CE3 . TRP B 40 ? -0.0736 0.8305 0.2617 -0.2373 -0.0416 0.2793 38 TRP B CE3 2137 C CZ2 . TRP B 40 ? 0.0303 0.9327 0.3568 -0.2573 -0.0326 0.2878 38 TRP B CZ2 2138 C CZ3 . TRP B 40 ? -0.0087 0.8618 0.3087 -0.2645 -0.0497 0.2834 38 TRP B CZ3 2139 C CH2 . TRP B 40 ? 0.0594 0.9271 0.3743 -0.2732 -0.0457 0.2876 38 TRP B CH2 2140 N N . LEU B 41 ? 0.2357 1.1078 0.5873 -0.1534 -0.0380 0.2494 39 LEU B N 2141 C CA . LEU B 41 ? 0.2517 1.1155 0.6070 -0.1485 -0.0512 0.2569 39 LEU B CA 2142 C C . LEU B 41 ? 0.2618 1.1363 0.6116 -0.1753 -0.0667 0.2739 39 LEU B C 2143 O O . LEU B 41 ? 0.2521 1.1030 0.5775 -0.2009 -0.0683 0.2730 39 LEU B O 2144 C CB . LEU B 41 ? 0.2654 1.0697 0.5955 -0.1456 -0.0508 0.2461 39 LEU B CB 2145 C CG . LEU B 41 ? 0.2364 1.0216 0.5686 -0.1223 -0.0390 0.2287 39 LEU B CG 2146 C CD1 . LEU B 41 ? 0.2842 1.0136 0.5887 -0.1304 -0.0391 0.2216 39 LEU B CD1 2147 C CD2 . LEU B 41 ? 0.2207 1.0264 0.5814 -0.0922 -0.0419 0.2278 39 LEU B CD2 2148 N N . ILE B 42 ? 0.2792 1.1893 0.6531 -0.1680 -0.0792 0.2885 40 ILE B N 2149 C CA . ILE B 42 ? 0.3039 1.2243 0.6718 -0.1932 -0.0980 0.3059 40 ILE B CA 2150 C C . ILE B 42 ? 0.3293 1.2129 0.6786 -0.1925 -0.1103 0.3095 40 ILE B C 2151 O O . ILE B 42 ? 0.3292 1.2044 0.6915 -0.1667 -0.1108 0.3086 40 ILE B O 2152 C CB . ILE B 42 ? 0.3032 1.2959 0.7121 -0.1903 -0.1078 0.3248 40 ILE B CB 2153 C CG1 . ILE B 42 ? 0.3051 1.3069 0.7027 -0.2243 -0.1286 0.3420 40 ILE B CG1 2154 C CG2 . ILE B 42 ? 0.3167 1.3318 0.7588 -0.1548 -0.1117 0.3286 40 ILE B CG2 2155 C CD1 . ILE B 42 ? 0.2064 1.2814 0.6462 -0.2232 -0.1424 0.3639 40 ILE B CD1 2156 N N . SER B 43 ? 0.3613 1.2219 0.6783 -0.2225 -0.1208 0.3136 41 SER B N 2157 C CA . SER B 43 ? 0.4100 1.2391 0.7011 -0.2296 -0.1331 0.3194 41 SER B CA 2158 C C . SER B 43 ? 0.4522 1.3101 0.7422 -0.2517 -0.1560 0.3394 41 SER B C 2159 O O . SER B 43 ? 0.4462 1.2885 0.7030 -0.2823 -0.1621 0.3368 41 SER B O 2160 C CB . SER B 43 ? 0.4114 1.1861 0.6574 -0.2458 -0.1229 0.3021 41 SER B CB 2161 O OG . SER B 43 ? 0.4667 1.2117 0.6908 -0.2457 -0.1284 0.3059 41 SER B OG 2162 N N . PRO B 44 ? 0.5017 1.4028 0.8292 -0.2355 -0.1699 0.3585 42 PRO B N 2163 C CA . PRO B 44 ? 0.5471 1.4857 0.8810 -0.2552 -0.1940 0.3804 42 PRO B CA 2164 C C . PRO B 44 ? 0.6000 1.5028 0.8850 -0.2829 -0.2086 0.3848 42 PRO B C 2165 O O . PRO B 44 ? 0.5997 1.4659 0.8643 -0.2753 -0.2086 0.3847 42 PRO B O 2166 C CB . PRO B 44 ? 0.5494 1.5283 0.9321 -0.2232 -0.2048 0.3979 42 PRO B CB 2167 C CG . PRO B 44 ? 0.5111 1.4899 0.9204 -0.1888 -0.1828 0.3815 42 PRO B CG 2168 C CD . PRO B 44 ? 0.4959 1.4128 0.8633 -0.1960 -0.1646 0.3591 42 PRO B CD 2169 N N . SER B 45 ? 0.6415 1.5565 0.9070 -0.3167 -0.2212 0.3885 43 SER B N 2170 C CA . SER B 45 ? 0.7007 1.5873 0.9141 -0.3478 -0.2350 0.3893 43 SER B CA 2171 C C . SER B 45 ? 0.7265 1.5532 0.8956 -0.3479 -0.2169 0.3679 43 SER B C 2172 O O . SER B 45 ? 0.7680 1.5709 0.8933 -0.3665 -0.2243 0.3684 43 SER B O 2173 C CB . SER B 45 ? 0.7321 1.6448 0.9532 -0.3482 -0.2618 0.4177 43 SER B CB 2174 O OG . SER B 45 ? 0.7339 1.7089 0.9981 -0.3501 -0.2798 0.4379 43 SER B OG 2175 N N . ASP B 46 ? 0.7159 1.5240 0.8979 -0.3275 -0.1931 0.3501 44 ASP B N 2176 C CA . ASP B 46 ? 0.7545 1.5126 0.9026 -0.3266 -0.1732 0.3279 44 ASP B CA 2177 C C . ASP B 46 ? 0.7791 1.5138 0.9131 -0.3165 -0.1728 0.3342 44 ASP B C 2178 O O . ASP B 46 ? 0.8131 1.5120 0.9163 -0.3207 -0.1576 0.3179 44 ASP B O 2179 C CB . ASP B 46 ? 0.7934 1.5253 0.8933 -0.3579 -0.1723 0.3107 44 ASP B CB 2180 C CG . ASP B 46 ? 0.8527 1.5957 0.9624 -0.3717 -0.1741 0.3038 44 ASP B CG 2181 O OD1 . ASP B 46 ? 0.8686 1.6491 1.0221 -0.3605 -0.1771 0.3164 44 ASP B OD1 2182 O OD2 . ASP B 46 ? 0.9866 1.7011 1.0603 -0.3939 -0.1727 0.2856 44 ASP B OD2 2183 N N . ASN B 47 ? 0.7798 1.5346 0.9375 -0.3035 -0.1900 0.3585 45 ASN B N 2184 C CA . ASN B 47 ? 0.7747 1.5027 0.9197 -0.2961 -0.1932 0.3689 45 ASN B CA 2185 C C . ASN B 47 ? 0.7502 1.4447 0.8974 -0.2783 -0.1694 0.3494 45 ASN B C 2186 O O . ASN B 47 ? 0.7203 1.4216 0.9021 -0.2544 -0.1577 0.3390 45 ASN B O 2187 C CB . ASN B 47 ? 0.7749 1.5248 0.9556 -0.2772 -0.2158 0.3976 45 ASN B CB 2188 C CG . ASN B 47 ? 0.7088 1.4696 0.9430 -0.2386 -0.2078 0.3935 45 ASN B CG 2189 O OD1 . ASN B 47 ? 0.6529 1.3965 0.9050 -0.2162 -0.2135 0.4028 45 ASN B OD1 2190 N ND2 . ASN B 47 ? 0.6887 1.4776 0.9472 -0.2316 -0.1956 0.3797 45 ASN B ND2 2191 N N . GLN B 48 ? 0.7507 1.4131 0.8592 -0.2923 -0.1624 0.3446 46 GLN B N 2192 C CA . GLN B 48 ? 0.7291 1.3627 0.8318 -0.2846 -0.1387 0.3231 46 GLN B CA 2193 C C . GLN B 48 ? 0.7038 1.3172 0.8265 -0.2636 -0.1397 0.3319 46 GLN B C 2194 O O . GLN B 48 ? 0.7150 1.3035 0.8308 -0.2605 -0.1238 0.3187 46 GLN B O 2195 C CB . GLN B 48 ? 0.7618 1.3772 0.8145 -0.3109 -0.1277 0.3104 46 GLN B CB 2196 C CG . GLN B 48 ? 0.8118 1.4348 0.8446 -0.3279 -0.1221 0.2914 46 GLN B CG 2197 C CD . GLN B 48 ? 0.9012 1.5155 0.8803 -0.3564 -0.1203 0.2842 46 GLN B CD 2198 O OE1 . GLN B 48 ? 0.9572 1.5791 0.9127 -0.3724 -0.1366 0.3039 46 GLN B OE1 2199 N NE2 . GLN B 48 ? 0.9352 1.5349 0.8944 -0.3619 -0.1008 0.2557 46 GLN B NE2 2200 N N . ILE B 49 ? 0.6683 1.2921 0.8182 -0.2488 -0.1598 0.3541 47 ILE B N 2201 C CA . ILE B 49 ? 0.6398 1.2381 0.8112 -0.2268 -0.1644 0.3619 47 ILE B CA 2202 C C . ILE B 49 ? 0.5908 1.2001 0.8080 -0.1928 -0.1571 0.3481 47 ILE B C 2203 O O . ILE B 49 ? 0.5676 1.1502 0.7986 -0.1741 -0.1516 0.3400 47 ILE B O 2204 C CB . ILE B 49 ? 0.6714 1.2675 0.8470 -0.2269 -0.1927 0.3947 47 ILE B CB 2205 C CG1 . ILE B 49 ? 0.7100 1.2959 0.8343 -0.2630 -0.1996 0.4099 47 ILE B CG1 2206 C CG2 . ILE B 49 ? 0.6609 1.2244 0.8633 -0.2012 -0.1996 0.4009 47 ILE B CG2 2207 C CD1 . ILE B 49 ? 0.7134 1.3130 0.8347 -0.2719 -0.2304 0.4445 47 ILE B CD1 2208 N N . VAL B 50 ? 0.5601 1.2106 0.7992 -0.1866 -0.1571 0.3452 48 VAL B N 2209 C CA . VAL B 50 ? 0.5220 1.1943 0.8047 -0.1548 -0.1503 0.3343 48 VAL B CA 2210 C C . VAL B 50 ? 0.4963 1.2080 0.7884 -0.1591 -0.1382 0.3224 48 VAL B C 2211 O O . VAL B 50 ? 0.5045 1.2416 0.7874 -0.1803 -0.1458 0.3314 48 VAL B O 2212 C CB . VAL B 50 ? 0.5327 1.2264 0.8550 -0.1298 -0.1708 0.3534 48 VAL B CB 2213 C CG1 . VAL B 50 ? 0.4768 1.1944 0.8417 -0.0948 -0.1598 0.3372 48 VAL B CG1 2214 C CG2 . VAL B 50 ? 0.5731 1.2235 0.8890 -0.1254 -0.1878 0.3701 48 VAL B CG2 2215 N N . ASP B 51 ? 0.4735 1.1890 0.7827 -0.1405 -0.1206 0.3028 49 ASP B N 2216 C CA . ASP B 51 ? 0.4458 1.2034 0.7720 -0.1397 -0.1100 0.2948 49 ASP B CA 2217 C C . ASP B 51 ? 0.4192 1.2102 0.7891 -0.1051 -0.1070 0.2909 49 ASP B C 2218 O O . ASP B 51 ? 0.4356 1.2050 0.8185 -0.0802 -0.1097 0.2870 49 ASP B O 2219 C CB . ASP B 51 ? 0.4407 1.1781 0.7447 -0.1506 -0.0904 0.2746 49 ASP B CB 2220 C CG . ASP B 51 ? 0.5016 1.2056 0.7640 -0.1800 -0.0900 0.2728 49 ASP B CG 2221 O OD1 . ASP B 51 ? 0.5660 1.2762 0.8136 -0.1998 -0.1036 0.2862 49 ASP B OD1 2222 O OD2 . ASP B 51 ? 0.5334 1.2084 0.7783 -0.1830 -0.0759 0.2569 49 ASP B OD2 2223 N N . GLN B 52 ? 0.3788 1.2231 0.7711 -0.1042 -0.1015 0.2915 50 GLN B N 2224 C CA . GLN B 52 ? 0.3674 1.2540 0.8001 -0.0717 -0.0940 0.2844 50 GLN B CA 2225 C C . GLN B 52 ? 0.3236 1.2371 0.7570 -0.0742 -0.0741 0.2705 50 GLN B C 2226 O O . GLN B 52 ? 0.3034 1.2261 0.7210 -0.1023 -0.0715 0.2752 50 GLN B O 2227 C CB . GLN B 52 ? 0.3835 1.3281 0.8549 -0.0622 -0.1085 0.3039 50 GLN B CB 2228 C CG . GLN B 52 ? 0.4537 1.3821 0.9462 -0.0342 -0.1240 0.3108 50 GLN B CG 2229 C CD . GLN B 52 ? 0.5057 1.4958 1.0427 -0.0208 -0.1396 0.3307 50 GLN B CD 2230 O OE1 . GLN B 52 ? 0.5648 1.5774 1.1421 0.0173 -0.1404 0.3263 50 GLN B OE1 2231 N NE2 . GLN B 52 ? 0.5089 1.5272 1.0401 -0.0514 -0.1529 0.3518 50 GLN B NE2 2232 N N . VAL B 53 ? 0.3047 1.2279 0.7550 -0.0447 -0.0612 0.2531 51 VAL B N 2233 C CA . VAL B 53 ? 0.2772 1.2332 0.7292 -0.0447 -0.0425 0.2411 51 VAL B CA 2234 C C . VAL B 53 ? 0.2715 1.3074 0.7576 -0.0434 -0.0415 0.2540 51 VAL B C 2235 O O . VAL B 53 ? 0.2740 1.3483 0.7957 -0.0190 -0.0470 0.2584 51 VAL B O 2236 C CB . VAL B 53 ? 0.2876 1.2309 0.7420 -0.0147 -0.0287 0.2156 51 VAL B CB 2237 C CG1 . VAL B 53 ? 0.2246 1.2096 0.6776 -0.0180 -0.0104 0.2066 51 VAL B CG1 2238 C CG2 . VAL B 53 ? 0.2422 1.1092 0.6655 -0.0182 -0.0306 0.2040 51 VAL B CG2 2239 N N . ILE B 54 ? 0.2594 1.3209 0.7363 -0.0703 -0.0355 0.2612 52 ILE B N 2240 C CA . ILE B 54 ? 0.2552 1.3971 0.7630 -0.0751 -0.0330 0.2753 52 ILE B CA 2241 C C . ILE B 54 ? 0.2618 1.4415 0.7739 -0.0638 -0.0114 0.2619 52 ILE B C 2242 O O . ILE B 54 ? 0.2801 1.5198 0.8242 -0.0372 -0.0019 0.2563 52 ILE B O 2243 C CB . ILE B 54 ? 0.2478 1.3959 0.7448 -0.1170 -0.0457 0.2975 52 ILE B CB 2244 C CG1 . ILE B 54 ? 0.1978 1.3116 0.6606 -0.1449 -0.0391 0.2943 52 ILE B CG1 2245 C CG2 . ILE B 54 ? 0.2819 1.3858 0.7650 -0.1276 -0.0657 0.3060 52 ILE B CG2 2246 C CD1 . ILE B 54 ? 0.1198 1.2171 0.5656 -0.1848 -0.0547 0.3108 52 ILE B CD1 2247 N N . ILE B 55 ? 0.2574 1.4022 0.7369 -0.0818 -0.0038 0.2555 53 ILE B N 2248 C CA . ILE B 55 ? 0.2463 1.4210 0.7223 -0.0739 0.0149 0.2436 53 ILE B CA 2249 C C . ILE B 55 ? 0.2579 1.3679 0.7010 -0.0681 0.0212 0.2226 53 ILE B C 2250 O O . ILE B 55 ? 0.2547 1.3016 0.6727 -0.0842 0.0130 0.2231 53 ILE B O 2251 C CB . ILE B 55 ? 0.2288 1.4477 0.7035 -0.1065 0.0176 0.2637 53 ILE B CB 2252 C CG1 . ILE B 55 ? 0.2555 1.5376 0.7385 -0.0936 0.0374 0.2561 53 ILE B CG1 2253 C CG2 . ILE B 55 ? 0.2132 1.3687 0.6523 -0.1363 0.0111 0.2680 53 ILE B CG2 2254 C CD1 . ILE B 55 ? 0.2808 1.6142 0.7640 -0.1263 0.0404 0.2795 53 ILE B CD1 2255 N N . LEU B 56 ? 0.2715 1.4043 0.7161 -0.0451 0.0363 0.2035 54 LEU B N 2256 C CA . LEU B 56 ? 0.2817 1.3634 0.6992 -0.0358 0.0422 0.1811 54 LEU B CA 2257 C C . LEU B 56 ? 0.3008 1.4243 0.7085 -0.0353 0.0582 0.1730 54 LEU B C 2258 O O . LEU B 56 ? 0.3113 1.5071 0.7379 -0.0256 0.0692 0.1738 54 LEU B O 2259 C CB . LEU B 56 ? 0.2934 1.3448 0.7196 -0.0019 0.0401 0.1596 54 LEU B CB 2260 C CG . LEU B 56 ? 0.3157 1.3252 0.7207 0.0142 0.0463 0.1319 54 LEU B CG 2261 C CD1 . LEU B 56 ? 0.3207 1.2701 0.6943 -0.0104 0.0413 0.1341 54 LEU B CD1 2262 C CD2 . LEU B 56 ? 0.3231 1.2997 0.7414 0.0456 0.0399 0.1149 54 LEU B CD2 2263 N N . TYR B 57 ? 0.3121 1.3934 0.6901 -0.0465 0.0592 0.1661 55 TYR B N 2264 C CA . TYR B 57 ? 0.3226 1.4353 0.6846 -0.0488 0.0714 0.1595 55 TYR B CA 2265 C C . TYR B 57 ? 0.3316 1.3994 0.6730 -0.0313 0.0740 0.1313 55 TYR B C 2266 O O . TYR B 57 ? 0.3098 1.3145 0.6358 -0.0402 0.0650 0.1293 55 TYR B O 2267 C CB . TYR B 57 ? 0.3279 1.4342 0.6740 -0.0839 0.0663 0.1831 55 TYR B CB 2268 C CG . TYR B 57 ? 0.3444 1.4906 0.6743 -0.0922 0.0761 0.1853 55 TYR B CG 2269 C CD1 . TYR B 57 ? 0.2892 1.4049 0.5939 -0.0879 0.0779 0.1691 55 TYR B CD1 2270 C CD2 . TYR B 57 ? 0.3927 1.6099 0.7319 -0.1073 0.0821 0.2062 55 TYR B CD2 2271 C CE1 . TYR B 57 ? 0.3338 1.4877 0.6209 -0.0972 0.0849 0.1732 55 TYR B CE1 2272 C CE2 . TYR B 57 ? 0.3785 1.6349 0.7000 -0.1179 0.0902 0.2116 55 TYR B CE2 2273 C CZ . TYR B 57 ? 0.3800 1.6037 0.6742 -0.1123 0.0912 0.1950 55 TYR B CZ 2274 O OH . TYR B 57 ? 0.3977 1.6621 0.6714 -0.1244 0.0975 0.2023 55 TYR B OH 2275 N N . SER B 58 ? 0.3528 1.4566 0.6941 -0.0074 0.0865 0.1087 56 SER B N 2276 C CA . SER B 58 ? 0.3725 1.4350 0.6950 0.0109 0.0877 0.0779 56 SER B CA 2277 C C . SER B 58 ? 0.4051 1.5177 0.7199 0.0317 0.1034 0.0528 56 SER B C 2278 O O . SER B 58 ? 0.4120 1.5859 0.7479 0.0501 0.1146 0.0481 56 SER B O 2279 C CB . SER B 58 ? 0.3864 1.3939 0.7217 0.0316 0.0779 0.0646 56 SER B CB 2280 O OG . SER B 58 ? 0.4028 1.3832 0.7259 0.0545 0.0802 0.0316 56 SER B OG 2281 N N . GLY B 59 ? 0.4281 1.5155 0.7128 0.0292 0.1039 0.0352 57 GLY B N 2282 C CA . GLY B 59 ? 0.4731 1.6044 0.7401 0.0444 0.1181 0.0091 57 GLY B CA 2283 C C . GLY B 59 ? 0.4778 1.6905 0.7431 0.0264 0.1299 0.0317 57 GLY B C 2284 O O . GLY B 59 ? 0.5003 1.7799 0.7620 0.0398 0.1465 0.0174 57 GLY B O 2285 N N . ASP B 60 ? 0.4656 1.6708 0.7336 -0.0048 0.1207 0.0677 58 ASP B N 2286 C CA . ASP B 60 ? 0.4663 1.7390 0.7371 -0.0286 0.1268 0.0980 58 ASP B CA 2287 C C . ASP B 60 ? 0.4462 1.7950 0.7459 -0.0119 0.1410 0.0970 58 ASP B C 2288 O O . ASP B 60 ? 0.4453 1.8729 0.7411 -0.0157 0.1558 0.1010 58 ASP B O 2289 C CB . ASP B 60 ? 0.5115 1.8137 0.7482 -0.0437 0.1321 0.0992 58 ASP B CB 2290 C CG . ASP B 60 ? 0.5758 1.9169 0.8108 -0.0793 0.1291 0.1408 58 ASP B CG 2291 O OD1 . ASP B 60 ? 0.6302 2.0076 0.8918 -0.0876 0.1307 0.1626 58 ASP B OD1 2292 O OD2 . ASP B 60 ? 0.6663 2.0006 0.8742 -0.0998 0.1234 0.1528 58 ASP B OD2 2293 N N . LYS B 61 ? 0.4296 1.7564 0.7592 0.0068 0.1358 0.0921 59 LYS B N 2294 C CA . LYS B 61 ? 0.4229 1.8182 0.7897 0.0217 0.1447 0.0969 59 LYS B CA 2295 C C . LYS B 61 ? 0.3916 1.7532 0.7855 0.0139 0.1284 0.1186 59 LYS B C 2296 O O . LYS B 61 ? 0.3941 1.6785 0.7851 0.0202 0.1147 0.1111 59 LYS B O 2297 C CB . LYS B 61 ? 0.4527 1.8691 0.8311 0.0670 0.1577 0.0570 59 LYS B CB 2298 C CG . LYS B 61 ? 0.4753 1.9252 0.8222 0.0767 0.1744 0.0294 59 LYS B CG 2299 C CD . LYS B 61 ? 0.4926 2.0026 0.8591 0.1190 0.1934 -0.0045 59 LYS B CD 2300 C CE . LYS B 61 ? 0.5270 2.0935 0.8595 0.1223 0.2134 -0.0276 59 LYS B CE 2301 N NZ . LYS B 61 ? 0.4514 2.1224 0.8081 0.1496 0.2381 -0.0438 59 LYS B NZ 2302 N N . ILE B 62 ? 0.3703 1.7939 0.7889 -0.0027 0.1294 0.1467 60 ILE B N 2303 C CA . ILE B 62 ? 0.3430 1.7465 0.7862 -0.0147 0.1132 0.1698 60 ILE B CA 2304 C C . ILE B 62 ? 0.3578 1.7744 0.8369 0.0213 0.1126 0.1556 60 ILE B C 2305 O O . ILE B 62 ? 0.3861 1.8561 0.8822 0.0535 0.1279 0.1339 60 ILE B O 2306 C CB . ILE B 62 ? 0.3249 1.7882 0.7806 -0.0507 0.1112 0.2072 60 ILE B CB 2307 C CG1 . ILE B 62 ? 0.2896 1.7127 0.7113 -0.0882 0.1034 0.2257 60 ILE B CG1 2308 C CG2 . ILE B 62 ? 0.3038 1.7637 0.7895 -0.0581 0.0958 0.2267 60 ILE B CG2 2309 C CD1 . ILE B 62 ? 0.2357 1.7045 0.6652 -0.1272 0.0985 0.2632 60 ILE B CD1 2310 N N . TYR B 63 ? 0.3454 1.7118 0.8353 0.0165 0.0941 0.1674 61 TYR B N 2311 C CA . TYR B 63 ? 0.3414 1.7182 0.8682 0.0462 0.0881 0.1623 61 TYR B CA 2312 C C . TYR B 63 ? 0.3370 1.7195 0.8839 0.0229 0.0707 0.1942 61 TYR B C 2313 O O . TYR B 63 ? 0.3183 1.6367 0.8442 -0.0023 0.0553 0.2069 61 TYR B O 2314 C CB . TYR B 63 ? 0.3518 1.6453 0.8676 0.0723 0.0799 0.1375 61 TYR B CB 2315 C CG . TYR B 63 ? 0.3476 1.6279 0.8446 0.0981 0.0937 0.1018 61 TYR B CG 2316 C CD1 . TYR B 63 ? 0.3587 1.6727 0.8801 0.1410 0.1036 0.0751 61 TYR B CD1 2317 C CD2 . TYR B 63 ? 0.3816 1.6136 0.8370 0.0806 0.0953 0.0932 61 TYR B CD2 2318 C CE1 . TYR B 63 ? 0.3918 1.6892 0.8924 0.1643 0.1151 0.0386 61 TYR B CE1 2319 C CE2 . TYR B 63 ? 0.3908 1.6095 0.8264 0.1019 0.1056 0.0597 61 TYR B CE2 2320 C CZ . TYR B 63 ? 0.3987 1.6486 0.8550 0.1430 0.1155 0.0315 61 TYR B CZ 2321 O OH . TYR B 63 ? 0.4451 1.6797 0.8791 0.1639 0.1249 -0.0052 61 TYR B OH 2322 N N . ASP B 64 ? 0.3617 1.8264 0.9503 0.0326 0.0737 0.2053 62 ASP B N 2323 C CA . ASP B 64 ? 0.3687 1.8545 0.9833 0.0133 0.0562 0.2352 62 ASP B CA 2324 C C . ASP B 64 ? 0.4060 1.8976 1.0584 0.0521 0.0479 0.2273 62 ASP B C 2325 O O . ASP B 64 ? 0.3894 1.9216 1.0759 0.0483 0.0353 0.2487 62 ASP B O 2326 C CB . ASP B 64 ? 0.3549 1.9406 0.9931 -0.0097 0.0641 0.2590 62 ASP B CB 2327 C CG . ASP B 64 ? 0.3753 2.0535 1.0415 0.0222 0.0884 0.2426 62 ASP B CG 2328 O OD1 . ASP B 64 ? 0.2493 1.9109 0.8905 0.0400 0.1046 0.2155 62 ASP B OD1 2329 O OD2 . ASP B 64 ? 0.4101 2.1792 1.1229 0.0298 0.0913 0.2555 62 ASP B OD2 2330 N N . ASN B 65 ? 0.4626 1.9077 1.1070 0.0881 0.0530 0.1968 63 ASN B N 2331 C CA . ASN B 65 ? 0.5082 1.9647 1.1907 0.1363 0.0507 0.1804 63 ASN B CA 2332 C C . ASN B 65 ? 0.5223 1.9365 1.2216 0.1388 0.0238 0.1983 63 ASN B C 2333 O O . ASN B 65 ? 0.5484 1.9833 1.2885 0.1760 0.0176 0.1937 63 ASN B O 2334 C CB . ASN B 65 ? 0.5392 1.9423 1.2005 0.1691 0.0612 0.1413 63 ASN B CB 2335 C CG . ASN B 65 ? 0.5899 2.0246 1.2928 0.2241 0.0665 0.1165 63 ASN B CG 2336 O OD1 . ASN B 65 ? 0.5864 2.1067 1.3369 0.2410 0.0705 0.1253 63 ASN B OD1 2337 N ND2 . ASN B 65 ? 0.6113 1.9771 1.2978 0.2529 0.0664 0.0844 63 ASN B ND2 2338 N N . TYR B 66 ? 0.5167 1.8741 1.1848 0.0999 0.0077 0.2186 64 TYR B N 2339 C CA . TYR B 66 ? 0.5344 1.8412 1.2064 0.0979 -0.0182 0.2348 64 TYR B CA 2340 C C . TYR B 66 ? 0.5155 1.8379 1.1849 0.0564 -0.0351 0.2682 64 TYR B C 2341 O O . TYR B 66 ? 0.4899 1.8549 1.1537 0.0253 -0.0283 0.2804 64 TYR B O 2342 C CB . TYR B 66 ? 0.5501 1.7512 1.1811 0.0975 -0.0252 0.2211 64 TYR B CB 2343 C CG . TYR B 66 ? 0.5570 1.7257 1.1512 0.0930 -0.0065 0.1968 64 TYR B CG 2344 C CD1 . TYR B 66 ? 0.5546 1.7146 1.1148 0.0542 -0.0006 0.2046 64 TYR B CD1 2345 C CD2 . TYR B 66 ? 0.5905 1.7337 1.1838 0.1278 0.0028 0.1659 64 TYR B CD2 2346 C CE1 . TYR B 66 ? 0.5759 1.7091 1.1049 0.0506 0.0140 0.1848 64 TYR B CE1 2347 C CE2 . TYR B 66 ? 0.5900 1.7060 1.1489 0.1221 0.0176 0.1445 64 TYR B CE2 2348 C CZ . TYR B 66 ? 0.5776 1.6910 1.1054 0.0836 0.0229 0.1554 64 TYR B CZ 2349 O OH . TYR B 66 ? 0.5709 1.6599 1.0668 0.0782 0.0352 0.1365 64 TYR B OH 2350 N N . TYR B 67 ? 0.5254 1.8079 1.1961 0.0550 -0.0586 0.2827 65 TYR B N 2351 C CA . TYR B 67 ? 0.5187 1.8182 1.1910 0.0211 -0.0789 0.3133 65 TYR B CA 2352 C C . TYR B 67 ? 0.5130 1.9189 1.2365 0.0245 -0.0779 0.3291 65 TYR B C 2353 O O . TYR B 67 ? 0.4967 1.9469 1.2168 -0.0076 -0.0719 0.3403 65 TYR B O 2354 C CB . TYR B 67 ? 0.5070 1.7662 1.1298 -0.0263 -0.0781 0.3182 65 TYR B CB 2355 C CG . TYR B 67 ? 0.5182 1.7538 1.1231 -0.0604 -0.1021 0.3412 65 TYR B CG 2356 C CD1 . TYR B 67 ? 0.5232 1.8157 1.1432 -0.0891 -0.1126 0.3636 65 TYR B CD1 2357 C CD2 . TYR B 67 ? 0.5508 1.7089 1.1210 -0.0664 -0.1145 0.3402 65 TYR B CD2 2358 C CE1 . TYR B 67 ? 0.5622 1.8325 1.1616 -0.1216 -0.1354 0.3818 65 TYR B CE1 2359 C CE2 . TYR B 67 ? 0.5764 1.7163 1.1252 -0.0984 -0.1354 0.3592 65 TYR B CE2 2360 C CZ . TYR B 67 ? 0.5982 1.7930 1.1607 -0.1253 -0.1461 0.3786 65 TYR B CZ 2361 O OH . TYR B 67 ? 0.6634 1.8402 1.2012 -0.1585 -0.1680 0.3950 65 TYR B OH 2362 N N . PRO B 68 ? 0.5241 1.9722 1.2979 0.0639 -0.0845 0.3306 66 PRO B N 2363 C CA . PRO B 68 ? 0.5150 2.0737 1.3471 0.0760 -0.0817 0.3432 66 PRO B CA 2364 C C . PRO B 68 ? 0.5014 2.1080 1.3373 0.0286 -0.0962 0.3754 66 PRO B C 2365 O O . PRO B 68 ? 0.4930 2.1968 1.3684 0.0242 -0.0891 0.3869 66 PRO B O 2366 C CB . PRO B 68 ? 0.5434 2.1067 1.4200 0.1203 -0.0986 0.3456 66 PRO B CB 2367 C CG . PRO B 68 ? 0.5610 2.0285 1.4077 0.1454 -0.0963 0.3206 66 PRO B CG 2368 C CD . PRO B 68 ? 0.5507 1.9402 1.3304 0.1019 -0.0950 0.3195 66 PRO B CD 2369 N N . ASP B 69 ? 0.4996 2.0400 1.2941 -0.0074 -0.1166 0.3891 67 ASP B N 2370 C CA . ASP B 69 ? 0.4952 2.0672 1.2849 -0.0561 -0.1328 0.4164 67 ASP B CA 2371 C C . ASP B 69 ? 0.4705 2.0667 1.2427 -0.0876 -0.1141 0.4140 67 ASP B C 2372 O O . ASP B 69 ? 0.4740 2.1391 1.2674 -0.1164 -0.1190 0.4349 67 ASP B O 2373 C CB . ASP B 69 ? 0.5140 2.0034 1.2552 -0.0870 -0.1564 0.4257 67 ASP B CB 2374 C CG . ASP B 69 ? 0.5300 2.0315 1.2501 -0.1420 -0.1700 0.4450 67 ASP B CG 2375 O OD1 . ASP B 69 ? 0.5424 2.0199 1.2295 -0.1694 -0.1572 0.4368 67 ASP B OD1 2376 O OD2 . ASP B 69 ? 0.5763 2.1084 1.3123 -0.1585 -0.1956 0.4685 67 ASP B OD2 2377 N N . LEU B 70 ? 0.4538 1.9950 1.1892 -0.0822 -0.0939 0.3902 68 LEU B N 2378 C CA . LEU B 70 ? 0.4404 1.9883 1.1516 -0.1135 -0.0789 0.3892 68 LEU B CA 2379 C C . LEU B 70 ? 0.4296 2.0503 1.1693 -0.0891 -0.0520 0.3782 68 LEU B C 2380 O O . LEU B 70 ? 0.4274 2.0522 1.1457 -0.1082 -0.0368 0.3752 68 LEU B O 2381 C CB . LEU B 70 ? 0.4388 1.8840 1.0898 -0.1273 -0.0749 0.3723 68 LEU B CB 2382 C CG . LEU B 70 ? 0.4545 1.8393 1.0682 -0.1674 -0.0967 0.3841 68 LEU B CG 2383 C CD1 . LEU B 70 ? 0.4099 1.6979 0.9713 -0.1711 -0.0910 0.3642 68 LEU B CD1 2384 C CD2 . LEU B 70 ? 0.4945 1.9182 1.1092 -0.2125 -0.1040 0.4051 68 LEU B CD2 2385 N N . LYS B 71 ? 0.4288 2.1075 1.2164 -0.0460 -0.0468 0.3720 69 LYS B N 2386 C CA . LYS B 71 ? 0.4178 2.1746 1.2346 -0.0179 -0.0194 0.3577 69 LYS B CA 2387 C C . LYS B 71 ? 0.3948 2.2358 1.2236 -0.0554 -0.0114 0.3796 69 LYS B C 2388 O O . LYS B 71 ? 0.3979 2.3149 1.2669 -0.0706 -0.0226 0.4053 69 LYS B O 2389 C CB . LYS B 71 ? 0.4368 2.2561 1.3132 0.0333 -0.0183 0.3509 69 LYS B CB 2390 C CG . LYS B 71 ? 0.4379 2.3456 1.3459 0.0663 0.0122 0.3318 69 LYS B CG 2391 C CD . LYS B 71 ? 0.4490 2.4109 1.4179 0.1229 0.0128 0.3207 69 LYS B CD 2392 C CE . LYS B 71 ? 0.4648 2.5019 1.4564 0.1614 0.0464 0.2921 69 LYS B CE 2393 N NZ . LYS B 71 ? 0.4705 2.5701 1.5281 0.2199 0.0484 0.2794 69 LYS B NZ 2394 N N . GLY B 72 ? 0.3695 2.1972 1.1638 -0.0717 0.0066 0.3714 70 GLY B N 2395 C CA . GLY B 72 ? 0.3521 2.2604 1.1556 -0.1058 0.0169 0.3921 70 GLY B CA 2396 C C . GLY B 72 ? 0.3424 2.2099 1.1159 -0.1648 -0.0031 0.4189 70 GLY B C 2397 O O . GLY B 72 ? 0.3506 2.2756 1.1302 -0.2012 -0.0005 0.4419 70 GLY B O 2398 N N . ARG B 73 ? 0.3328 2.0995 1.0723 -0.1748 -0.0231 0.4152 71 ARG B N 2399 C CA . ARG B 73 ? 0.3248 2.0459 1.0361 -0.2274 -0.0446 0.4363 71 ARG B CA 2400 C C . ARG B 73 ? 0.3261 1.9427 0.9788 -0.2446 -0.0443 0.4237 71 ARG B C 2401 O O . ARG B 73 ? 0.3473 1.9216 0.9749 -0.2866 -0.0609 0.4378 71 ARG B O 2402 C CB . ARG B 73 ? 0.3307 2.0337 1.0524 -0.2337 -0.0717 0.4470 71 ARG B CB 2403 C CG . ARG B 73 ? 0.3020 2.1152 1.0852 -0.2276 -0.0776 0.4674 71 ARG B CG 2404 C CD . ARG B 73 ? 0.2853 2.0896 1.0736 -0.2551 -0.1101 0.4883 71 ARG B CD 2405 N NE . ARG B 73 ? 0.3200 2.0492 1.0891 -0.2321 -0.1234 0.4749 71 ARG B NE 2406 C CZ . ARG B 73 ? 0.3646 1.9963 1.0811 -0.2550 -0.1380 0.4693 71 ARG B CZ 2407 N NH1 . ARG B 73 ? 0.3741 1.9654 1.0532 -0.2990 -0.1424 0.4737 71 ARG B NH1 2408 N NH2 . ARG B 73 ? 0.3492 1.9246 1.0511 -0.2338 -0.1485 0.4597 71 ARG B NH2 2409 N N . VAL B 74 ? 0.3060 1.8820 0.9382 -0.2127 -0.0266 0.3969 72 VAL B N 2410 C CA . VAL B 74 ? 0.3144 1.7987 0.8962 -0.2259 -0.0255 0.3850 72 VAL B CA 2411 C C . VAL B 74 ? 0.3226 1.8199 0.8915 -0.2147 -0.0026 0.3732 72 VAL B C 2412 O O . VAL B 74 ? 0.3249 1.8599 0.9093 -0.1775 0.0155 0.3553 72 VAL B O 2413 C CB . VAL B 74 ? 0.3267 1.7202 0.8826 -0.2063 -0.0329 0.3639 72 VAL B CB 2414 C CG1 . VAL B 74 ? 0.3409 1.7426 0.9121 -0.1569 -0.0191 0.3407 72 VAL B CG1 2415 C CG2 . VAL B 74 ? 0.2539 1.5621 0.7631 -0.2229 -0.0327 0.3540 72 VAL B CG2 2416 N N . HIS B 75 ? 0.3282 1.7915 0.8676 -0.2469 -0.0049 0.3827 73 HIS B N 2417 C CA . HIS B 75 ? 0.3205 1.7984 0.8442 -0.2435 0.0135 0.3774 73 HIS B CA 2418 C C . HIS B 75 ? 0.2928 1.6862 0.7745 -0.2647 0.0068 0.3765 73 HIS B C 2419 O O . HIS B 75 ? 0.2960 1.6435 0.7652 -0.2966 -0.0116 0.3908 73 HIS B O 2420 C CB . HIS B 75 ? 0.3265 1.9042 0.8744 -0.2658 0.0207 0.4035 73 HIS B CB 2421 C CG . HIS B 75 ? 0.4051 2.0831 0.9971 -0.2381 0.0348 0.4005 73 HIS B CG 2422 N ND1 . HIS B 75 ? 0.4944 2.2323 1.0934 -0.2086 0.0601 0.3840 73 HIS B ND1 2423 C CD2 . HIS B 75 ? 0.4937 2.2277 1.1266 -0.2355 0.0268 0.4120 73 HIS B CD2 2424 C CE1 . HIS B 75 ? 0.4825 2.3074 1.1264 -0.1859 0.0686 0.3832 73 HIS B CE1 2425 N NE2 . HIS B 75 ? 0.4784 2.3038 1.1457 -0.2014 0.0481 0.4015 73 HIS B NE2 2426 N N . PHE B 76 ? 0.2510 1.6258 0.7123 -0.2459 0.0212 0.3588 74 PHE B N 2427 C CA . PHE B 76 ? 0.2257 1.5371 0.6530 -0.2646 0.0162 0.3613 74 PHE B CA 2428 C C . PHE B 76 ? 0.2222 1.5716 0.6512 -0.3041 0.0105 0.3943 74 PHE B C 2429 O O . PHE B 76 ? 0.1948 1.6270 0.6377 -0.3065 0.0233 0.4060 74 PHE B O 2430 C CB . PHE B 76 ? 0.2153 1.5181 0.6240 -0.2393 0.0324 0.3397 74 PHE B CB 2431 C CG . PHE B 76 ? 0.1898 1.4372 0.5898 -0.2062 0.0352 0.3084 74 PHE B CG 2432 C CD1 . PHE B 76 ? 0.2266 1.3879 0.6058 -0.2109 0.0237 0.3006 74 PHE B CD1 2433 C CD2 . PHE B 76 ? 0.1416 1.4230 0.5540 -0.1704 0.0496 0.2862 74 PHE B CD2 2434 C CE1 . PHE B 76 ? 0.1933 1.3077 0.5647 -0.1840 0.0263 0.2747 74 PHE B CE1 2435 C CE2 . PHE B 76 ? 0.1949 1.4216 0.5992 -0.1430 0.0499 0.2598 74 PHE B CE2 2436 C CZ . PHE B 76 ? 0.1836 1.3282 0.5670 -0.1517 0.0382 0.2557 74 PHE B CZ 2437 N N . THR B 77 ? 0.2305 1.5189 0.6445 -0.3352 -0.0089 0.4088 75 THR B N 2438 C CA . THR B 77 ? 0.2565 1.5666 0.6704 -0.3766 -0.0191 0.4426 75 THR B CA 2439 C C . THR B 77 ? 0.2718 1.6069 0.6715 -0.3764 -0.0070 0.4492 75 THR B C 2440 O O . THR B 77 ? 0.2935 1.7100 0.7045 -0.3900 0.0018 0.4698 75 THR B O 2441 C CB . THR B 77 ? 0.2848 1.5065 0.6806 -0.4049 -0.0431 0.4508 75 THR B CB 2442 O OG1 . THR B 77 ? 0.1877 1.3277 0.5589 -0.3835 -0.0424 0.4255 75 THR B OG1 2443 C CG2 . THR B 77 ? 0.3206 1.5340 0.7294 -0.4172 -0.0579 0.4521 75 THR B CG2 2444 N N . SER B 78 ? 0.3050 1.5725 0.6793 -0.3619 -0.0070 0.4321 76 SER B N 2445 C CA . SER B 78 ? 0.3280 1.6080 0.6838 -0.3612 0.0012 0.4370 76 SER B CA 2446 C C . SER B 78 ? 0.3591 1.7321 0.7217 -0.3433 0.0247 0.4311 76 SER B C 2447 O O . SER B 78 ? 0.3231 1.7377 0.7039 -0.3162 0.0384 0.4110 76 SER B O 2448 C CB . SER B 78 ? 0.3220 1.5229 0.6549 -0.3389 0.0000 0.4119 76 SER B CB 2449 O OG . SER B 78 ? 0.2413 1.4685 0.5580 -0.3296 0.0113 0.4095 76 SER B OG 2450 N N . ASN B 79 ? 0.4291 1.8310 0.7752 -0.3582 0.0283 0.4485 77 ASN B N 2451 C CA . ASN B 79 ? 0.4633 1.9468 0.8047 -0.3423 0.0513 0.4402 77 ASN B CA 2452 C C . ASN B 79 ? 0.4888 1.9251 0.8077 -0.3077 0.0588 0.4043 77 ASN B C 2453 O O . ASN B 79 ? 0.5126 1.9660 0.8373 -0.2721 0.0743 0.3713 77 ASN B O 2454 C CB . ASN B 79 ? 0.4953 2.0264 0.8230 -0.3782 0.0492 0.4777 77 ASN B CB 2455 C CG . ASN B 79 ? 0.5538 2.0972 0.8982 -0.4228 0.0318 0.5194 77 ASN B CG 2456 O OD1 . ASN B 79 ? 0.4976 2.1253 0.8664 -0.4347 0.0403 0.5340 77 ASN B OD1 2457 N ND2 . ASN B 79 ? 0.6180 2.0776 0.9510 -0.4478 0.0065 0.5384 77 ASN B ND2 2458 N N . ASP B 80 ? 0.4921 1.8642 0.7876 -0.3189 0.0450 0.4118 78 ASP B N 2459 C CA . ASP B 80 ? 0.4763 1.8061 0.7500 -0.2930 0.0490 0.3834 78 ASP B CA 2460 C C . ASP B 80 ? 0.4485 1.6872 0.7251 -0.2781 0.0378 0.3631 78 ASP B C 2461 O O . ASP B 80 ? 0.4396 1.6133 0.7076 -0.2901 0.0215 0.3727 78 ASP B O 2462 C CB . ASP B 80 ? 0.5098 1.8347 0.7579 -0.3128 0.0407 0.4049 78 ASP B CB 2463 C CG . ASP B 80 ? 0.5261 1.8409 0.7509 -0.2881 0.0487 0.3770 78 ASP B CG 2464 O OD1 . ASP B 80 ? 0.5978 1.9179 0.8256 -0.2564 0.0629 0.3407 78 ASP B OD1 2465 O OD2 . ASP B 80 ? 0.5507 1.8506 0.7547 -0.3013 0.0387 0.3923 78 ASP B OD2 2466 N N . VAL B 81 ? 0.4228 1.6594 0.7122 -0.2506 0.0471 0.3349 79 VAL B N 2467 C CA . VAL B 81 ? 0.3950 1.5549 0.6886 -0.2388 0.0379 0.3177 79 VAL B CA 2468 C C . VAL B 81 ? 0.3895 1.4895 0.6635 -0.2279 0.0339 0.3016 79 VAL B C 2469 O O . VAL B 81 ? 0.3986 1.4323 0.6712 -0.2314 0.0220 0.3000 79 VAL B O 2470 C CB . VAL B 81 ? 0.3636 1.5381 0.6753 -0.2124 0.0473 0.2946 79 VAL B CB 2471 C CG1 . VAL B 81 ? 0.4163 1.5174 0.7233 -0.1950 0.0421 0.2714 79 VAL B CG1 2472 C CG2 . VAL B 81 ? 0.3549 1.5610 0.6901 -0.2284 0.0421 0.3141 79 VAL B CG2 2473 N N . LYS B 82 ? 0.3868 1.5146 0.6455 -0.2156 0.0439 0.2895 80 LYS B N 2474 C CA . LYS B 82 ? 0.3724 1.4535 0.6139 -0.2056 0.0398 0.2741 80 LYS B CA 2475 C C . LYS B 82 ? 0.3830 1.4276 0.6178 -0.2281 0.0231 0.2990 80 LYS B C 2476 O O . LYS B 82 ? 0.4021 1.3932 0.6330 -0.2222 0.0150 0.2903 80 LYS B O 2477 C CB . LYS B 82 ? 0.3829 1.5079 0.6058 -0.1931 0.0517 0.2590 80 LYS B CB 2478 C CG . LYS B 82 ? 0.3811 1.5372 0.6091 -0.1655 0.0680 0.2287 80 LYS B CG 2479 C CD . LYS B 82 ? 0.3856 1.5814 0.5901 -0.1547 0.0789 0.2108 80 LYS B CD 2480 C CE . LYS B 82 ? 0.3618 1.6140 0.5502 -0.1791 0.0797 0.2387 80 LYS B CE 2481 N NZ . LYS B 82 ? 0.4197 1.7253 0.5838 -0.1672 0.0941 0.2180 80 LYS B NZ 2482 N N . SER B 83 ? 0.3985 1.4745 0.6341 -0.2539 0.0174 0.3311 81 SER B N 2483 C CA . SER B 83 ? 0.4222 1.4642 0.6521 -0.2758 -0.0009 0.3585 81 SER B CA 2484 C C . SER B 83 ? 0.4135 1.3777 0.6545 -0.2745 -0.0141 0.3534 81 SER B C 2485 O O . SER B 83 ? 0.4449 1.3679 0.6854 -0.2868 -0.0305 0.3706 81 SER B O 2486 C CB . SER B 83 ? 0.4564 1.5396 0.6882 -0.3077 -0.0072 0.3969 81 SER B CB 2487 O OG . SER B 83 ? 0.4692 1.5482 0.7196 -0.3188 -0.0102 0.4039 81 SER B OG 2488 N N . GLY B 84 ? 0.3833 1.3286 0.6340 -0.2590 -0.0072 0.3298 82 GLY B N 2489 C CA . GLY B 84 ? 0.3769 1.2548 0.6350 -0.2576 -0.0169 0.3216 82 GLY B CA 2490 C C . GLY B 84 ? 0.3681 1.2414 0.6369 -0.2716 -0.0213 0.3293 82 GLY B C 2491 O O . GLY B 84 ? 0.3704 1.1906 0.6415 -0.2806 -0.0336 0.3312 82 GLY B O 2492 N N . ASP B 85 ? 0.3402 1.2707 0.6159 -0.2726 -0.0118 0.3321 83 ASP B N 2493 C CA . ASP B 85 ? 0.3440 1.2799 0.6320 -0.2870 -0.0171 0.3408 83 ASP B CA 2494 C C . ASP B 85 ? 0.3050 1.2800 0.6045 -0.2698 -0.0048 0.3255 83 ASP B C 2495 O O . ASP B 85 ? 0.2950 1.3362 0.6014 -0.2631 0.0072 0.3275 83 ASP B O 2496 C CB . ASP B 85 ? 0.3654 1.3385 0.6583 -0.3183 -0.0255 0.3750 83 ASP B CB 2497 C CG . ASP B 85 ? 0.4335 1.4028 0.7383 -0.3379 -0.0357 0.3851 83 ASP B CG 2498 O OD1 . ASP B 85 ? 0.4601 1.4514 0.7753 -0.3253 -0.0284 0.3714 83 ASP B OD1 2499 O OD2 . ASP B 85 ? 0.5632 1.5041 0.8665 -0.3663 -0.0530 0.4071 83 ASP B OD2 2500 N N . ALA B 86 ? 0.2714 1.2060 0.5732 -0.2635 -0.0089 0.3112 84 ALA B N 2501 C CA . ALA B 86 ? 0.2414 1.1993 0.5543 -0.2450 -0.0011 0.2967 84 ALA B CA 2502 C C . ALA B 86 ? 0.2378 1.2073 0.5632 -0.2626 -0.0111 0.3100 84 ALA B C 2503 O O . ALA B 86 ? 0.2293 1.2147 0.5657 -0.2498 -0.0089 0.3018 84 ALA B O 2504 C CB . ALA B 86 ? 0.2297 1.1351 0.5331 -0.2238 0.0015 0.2708 84 ALA B CB 2505 N N . SER B 87 ? 0.2510 1.2112 0.5749 -0.2930 -0.0243 0.3315 85 SER B N 2506 C CA . SER B 87 ? 0.2412 1.2075 0.5744 -0.3150 -0.0373 0.3445 85 SER B CA 2507 C C . SER B 87 ? 0.2221 1.2687 0.5804 -0.3107 -0.0307 0.3535 85 SER B C 2508 O O . SER B 87 ? 0.2293 1.3364 0.5982 -0.3005 -0.0172 0.3575 85 SER B O 2509 C CB . SER B 87 ? 0.2652 1.2117 0.5938 -0.3510 -0.0538 0.3684 85 SER B CB 2510 O OG . SER B 87 ? 0.2611 1.1433 0.5717 -0.3504 -0.0584 0.3620 85 SER B OG 2511 N N . ILE B 88 ? 0.2153 1.2649 0.5831 -0.3183 -0.0407 0.3560 86 ILE B N 2512 C CA . ILE B 88 ? 0.2094 1.3371 0.6068 -0.3147 -0.0377 0.3665 86 ILE B CA 2513 C C . ILE B 88 ? 0.2454 1.3918 0.6543 -0.3493 -0.0561 0.3894 86 ILE B C 2514 O O . ILE B 88 ? 0.2648 1.3520 0.6553 -0.3727 -0.0728 0.3910 86 ILE B O 2515 C CB . ILE B 88 ? 0.1640 1.2942 0.5705 -0.2808 -0.0316 0.3463 86 ILE B CB 2516 C CG1 . ILE B 88 ? 0.1025 1.1704 0.4930 -0.2874 -0.0465 0.3386 86 ILE B CG1 2517 C CG2 . ILE B 88 ? 0.0974 1.2140 0.4951 -0.2489 -0.0151 0.3242 86 ILE B CG2 2518 C CD1 . ILE B 88 ? 0.1660 1.2354 0.5653 -0.2590 -0.0446 0.3251 86 ILE B CD1 2519 N N . ASN B 89 ? 0.2657 1.4986 0.7063 -0.3514 -0.0523 0.4057 87 ASN B N 2520 C CA . ASN B 89 ? 0.3259 1.5960 0.7866 -0.3799 -0.0694 0.4273 87 ASN B CA 2521 C C . ASN B 89 ? 0.3247 1.6379 0.8120 -0.3557 -0.0688 0.4213 87 ASN B C 2522 O O . ASN B 89 ? 0.3423 1.7009 0.8487 -0.3204 -0.0512 0.4104 87 ASN B O 2523 C CB . ASN B 89 ? 0.3262 1.6734 0.8087 -0.4080 -0.0684 0.4576 87 ASN B CB 2524 C CG . ASN B 89 ? 0.3995 1.6979 0.8603 -0.4507 -0.0848 0.4760 87 ASN B CG 2525 O OD1 . ASN B 89 ? 0.4204 1.6271 0.8515 -0.4571 -0.0968 0.4634 87 ASN B OD1 2526 N ND2 . ASN B 89 ? 0.5072 1.8676 0.9840 -0.4802 -0.0858 0.5061 87 ASN B ND2 2527 N N . VAL B 90 ? 0.3295 1.6252 0.8164 -0.3750 -0.0895 0.4280 88 VAL B N 2528 C CA . VAL B 90 ? 0.3159 1.6544 0.8301 -0.3589 -0.0958 0.4295 88 VAL B CA 2529 C C . VAL B 90 ? 0.3457 1.7554 0.8901 -0.3926 -0.1108 0.4591 88 VAL B C 2530 O O . VAL B 90 ? 0.3729 1.7501 0.9004 -0.4335 -0.1311 0.4712 88 VAL B O 2531 C CB . VAL B 90 ? 0.3300 1.5936 0.8164 -0.3565 -0.1101 0.4149 88 VAL B CB 2532 C CG1 . VAL B 90 ? 0.2903 1.5981 0.8052 -0.3400 -0.1194 0.4203 88 VAL B CG1 2533 C CG2 . VAL B 90 ? 0.2962 1.4862 0.7510 -0.3291 -0.0960 0.3871 88 VAL B CG2 2534 N N . THR B 91 ? 0.3367 1.8450 0.9270 -0.3752 -0.1009 0.4697 89 THR B N 2535 C CA . THR B 91 ? 0.3568 1.9523 0.9834 -0.4066 -0.1111 0.5004 89 THR B CA 2536 C C . THR B 91 ? 0.3614 2.0008 1.0198 -0.4037 -0.1286 0.5103 89 THR B C 2537 O O . THR B 91 ? 0.3460 1.9786 1.0132 -0.3652 -0.1263 0.4950 89 THR B O 2538 C CB . THR B 91 ? 0.3579 2.0517 1.0183 -0.3950 -0.0871 0.5099 89 THR B CB 2539 O OG1 . THR B 91 ? 0.3653 2.0946 1.0485 -0.3405 -0.0671 0.4888 89 THR B OG1 2540 C CG2 . THR B 91 ? 0.3383 1.9950 0.9658 -0.4095 -0.0754 0.5088 89 THR B CG2 2541 N N . ASN B 92 ? 0.3744 2.0570 1.0495 -0.4476 -0.1485 0.5380 90 ASN B N 2542 C CA . ASN B 92 ? 0.3734 2.1072 1.0808 -0.4553 -0.1701 0.5539 90 ASN B CA 2543 C C . ASN B 92 ? 0.3860 2.0381 1.0619 -0.4437 -0.1864 0.5367 90 ASN B C 2544 O O . ASN B 92 ? 0.3788 2.0492 1.0751 -0.4056 -0.1851 0.5295 90 ASN B O 2545 C CB . ASN B 92 ? 0.3476 2.1981 1.1179 -0.4182 -0.1546 0.5607 90 ASN B CB 2546 C CG . ASN B 92 ? 0.3244 2.2620 1.1424 -0.4379 -0.1767 0.5886 90 ASN B CG 2547 O OD1 . ASN B 92 ? 0.2599 2.2772 1.1288 -0.4021 -0.1711 0.5912 90 ASN B OD1 2548 N ND2 . ASN B 92 ? 0.3474 2.2693 1.1504 -0.4941 -0.2032 0.6089 90 ASN B ND2 2549 N N . LEU B 93 ? 0.4096 1.9709 1.0347 -0.4772 -0.2021 0.5305 91 LEU B N 2550 C CA . LEU B 93 ? 0.4194 1.8960 1.0038 -0.4698 -0.2144 0.5114 91 LEU B CA 2551 C C . LEU B 93 ? 0.4340 1.9477 1.0368 -0.4778 -0.2402 0.5261 91 LEU B C 2552 O O . LEU B 93 ? 0.4390 2.0011 1.0605 -0.5156 -0.2611 0.5494 91 LEU B O 2553 C CB . LEU B 93 ? 0.4458 1.8201 0.9717 -0.5025 -0.2232 0.4979 91 LEU B CB 2554 C CG . LEU B 93 ? 0.3912 1.6982 0.8869 -0.4807 -0.1996 0.4743 91 LEU B CG 2555 C CD1 . LEU B 93 ? 0.3643 1.5709 0.8063 -0.5081 -0.2106 0.4589 91 LEU B CD1 2556 C CD2 . LEU B 93 ? 0.3757 1.6699 0.8719 -0.4305 -0.1822 0.4545 91 LEU B CD2 2557 N N . GLN B 94 ? 0.4354 1.9257 1.0330 -0.4427 -0.2398 0.5138 92 GLN B N 2558 C CA . GLN B 94 ? 0.4480 1.9601 1.0556 -0.4456 -0.2656 0.5267 92 GLN B CA 2559 C C . GLN B 94 ? 0.4610 1.8790 1.0118 -0.4439 -0.2739 0.5080 92 GLN B C 2560 O O . GLN B 94 ? 0.4771 1.8196 0.9878 -0.4346 -0.2572 0.4841 92 GLN B O 2561 C CB . GLN B 94 ? 0.4284 2.0196 1.0955 -0.3998 -0.2594 0.5361 92 GLN B CB 2562 C CG . GLN B 94 ? 0.4084 2.0866 1.1286 -0.3815 -0.2367 0.5427 92 GLN B CG 2563 C CD . GLN B 94 ? 0.4094 2.1563 1.1535 -0.4270 -0.2468 0.5678 92 GLN B CD 2564 O OE1 . GLN B 94 ? 0.4702 2.2150 1.2036 -0.4691 -0.2753 0.5835 92 GLN B OE1 2565 N NE2 . GLN B 94 ? 0.3980 2.2074 1.1729 -0.4211 -0.2241 0.5721 92 GLN B NE2 2566 N N . LEU B 95 ? 0.4840 1.9130 1.0333 -0.4525 -0.2998 0.5203 93 LEU B N 2567 C CA . LEU B 95 ? 0.5091 1.8579 1.0006 -0.4595 -0.3108 0.5064 93 LEU B CA 2568 C C . LEU B 95 ? 0.4921 1.8041 0.9774 -0.4134 -0.2935 0.4919 93 LEU B C 2569 O O . LEU B 95 ? 0.5177 1.7556 0.9514 -0.4158 -0.2924 0.4752 93 LEU B O 2570 C CB . LEU B 95 ? 0.5456 1.9217 1.0346 -0.4853 -0.3459 0.5268 93 LEU B CB 2571 C CG . LEU B 95 ? 0.5739 1.9402 1.0348 -0.5423 -0.3675 0.5304 93 LEU B CG 2572 C CD1 . LEU B 95 ? 0.5628 1.9479 1.0114 -0.5680 -0.4031 0.5472 93 LEU B CD1 2573 C CD2 . LEU B 95 ? 0.5842 1.8512 0.9798 -0.5601 -0.3560 0.4996 93 LEU B CD2 2574 N N . SER B 96 ? 0.4666 1.8314 1.0048 -0.3722 -0.2798 0.4975 94 SER B N 2575 C CA . SER B 96 ? 0.4562 1.7868 0.9941 -0.3270 -0.2651 0.4842 94 SER B CA 2576 C C . SER B 96 ? 0.4327 1.7043 0.9419 -0.3161 -0.2359 0.4567 94 SER B C 2577 O O . SER B 96 ? 0.4380 1.6637 0.9336 -0.2871 -0.2236 0.4418 94 SER B O 2578 C CB . SER B 96 ? 0.4406 1.8464 1.0463 -0.2846 -0.2616 0.4963 94 SER B CB 2579 O OG . SER B 96 ? 0.4549 1.9230 1.0991 -0.2799 -0.2434 0.4962 94 SER B OG 2580 N N . ASP B 97 ? 0.4218 1.6942 0.9221 -0.3416 -0.2274 0.4522 95 ASP B N 2581 C CA . ASP B 97 ? 0.4089 1.6350 0.8876 -0.3327 -0.2017 0.4298 95 ASP B CA 2582 C C . ASP B 97 ? 0.4328 1.5707 0.8502 -0.3543 -0.2036 0.4120 95 ASP B C 2583 O O . ASP B 97 ? 0.4055 1.4962 0.7998 -0.3504 -0.1855 0.3931 95 ASP B O 2584 C CB . ASP B 97 ? 0.3985 1.6683 0.8982 -0.3498 -0.1928 0.4366 95 ASP B CB 2585 C CG . ASP B 97 ? 0.3867 1.7547 0.9482 -0.3295 -0.1880 0.4532 95 ASP B CG 2586 O OD1 . ASP B 97 ? 0.4017 1.7923 0.9904 -0.2903 -0.1842 0.4513 95 ASP B OD1 2587 O OD2 . ASP B 97 ? 0.4017 1.8249 0.9855 -0.3527 -0.1882 0.4681 95 ASP B OD2 2588 N N . ILE B 98 ? 0.4581 1.5783 0.8498 -0.3769 -0.2260 0.4182 96 ILE B N 2589 C CA . ILE B 98 ? 0.4837 1.5264 0.8158 -0.3965 -0.2278 0.3995 96 ILE B CA 2590 C C . ILE B 98 ? 0.4863 1.4837 0.8015 -0.3650 -0.2109 0.3833 96 ILE B C 2591 O O . ILE B 98 ? 0.4899 1.5075 0.8286 -0.3366 -0.2113 0.3917 96 ILE B O 2592 C CB . ILE B 98 ? 0.5143 1.5543 0.8198 -0.4272 -0.2557 0.4092 96 ILE B CB 2593 C CG1 . ILE B 98 ? 0.5757 1.6493 0.8908 -0.4656 -0.2739 0.4221 96 ILE B CG1 2594 C CG2 . ILE B 98 ? 0.5190 1.4830 0.7616 -0.4409 -0.2534 0.3863 96 ILE B CG2 2595 C CD1 . ILE B 98 ? 0.5931 1.6791 0.8890 -0.4973 -0.3054 0.4352 96 ILE B CD1 2596 N N . GLY B 99 ? 0.4844 1.4203 0.7614 -0.3700 -0.1967 0.3603 97 GLY B N 2597 C CA . GLY B 99 ? 0.4744 1.3685 0.7351 -0.3448 -0.1803 0.3450 97 GLY B CA 2598 C C . GLY B 99 ? 0.4735 1.3175 0.7094 -0.3459 -0.1611 0.3212 97 GLY B C 2599 O O . GLY B 99 ? 0.4931 1.3190 0.7126 -0.3698 -0.1635 0.3140 97 GLY B O 2600 N N . THR B 100 ? 0.4553 1.2759 0.6904 -0.3196 -0.1439 0.3096 98 THR B N 2601 C CA . THR B 100 ? 0.4412 1.2182 0.6576 -0.3159 -0.1255 0.2880 98 THR B CA 2602 C C . THR B 100 ? 0.4069 1.2024 0.6552 -0.2889 -0.1094 0.2861 98 THR B C 2603 O O . THR B 100 ? 0.3863 1.2005 0.6564 -0.2639 -0.1061 0.2907 98 THR B O 2604 C CB . THR B 100 ? 0.4545 1.1852 0.6349 -0.3138 -0.1190 0.2734 98 THR B CB 2605 O OG1 . THR B 100 ? 0.5109 1.2247 0.6551 -0.3416 -0.1321 0.2711 98 THR B OG1 2606 C CG2 . THR B 100 ? 0.4036 1.0981 0.5739 -0.3052 -0.0993 0.2522 98 THR B CG2 2607 N N . TYR B 101 ? 0.4077 1.1963 0.6570 -0.2954 -0.1012 0.2794 99 TYR B N 2608 C CA . TYR B 101 ? 0.3858 1.1993 0.6621 -0.2764 -0.0876 0.2796 99 TYR B CA 2609 C C . TYR B 101 ? 0.3739 1.1437 0.6331 -0.2679 -0.0724 0.2608 99 TYR B C 2610 O O . TYR B 101 ? 0.4050 1.1356 0.6405 -0.2837 -0.0728 0.2510 99 TYR B O 2611 C CB . TYR B 101 ? 0.3873 1.2412 0.6835 -0.2938 -0.0932 0.2946 99 TYR B CB 2612 C CG . TYR B 101 ? 0.4041 1.3180 0.7288 -0.2973 -0.1062 0.3150 99 TYR B CG 2613 C CD1 . TYR B 101 ? 0.4272 1.3408 0.7406 -0.3222 -0.1261 0.3245 99 TYR B CD1 2614 C CD2 . TYR B 101 ? 0.4199 1.3938 0.7832 -0.2751 -0.0988 0.3237 99 TYR B CD2 2615 C CE1 . TYR B 101 ? 0.4539 1.4271 0.7969 -0.3256 -0.1399 0.3450 99 TYR B CE1 2616 C CE2 . TYR B 101 ? 0.4242 1.4596 0.8195 -0.2756 -0.1105 0.3425 99 TYR B CE2 2617 C CZ . TYR B 101 ? 0.4197 1.4554 0.8063 -0.3013 -0.1318 0.3546 99 TYR B CZ 2618 O OH . TYR B 101 ? 0.3610 1.4620 0.7826 -0.3020 -0.1452 0.3750 99 TYR B OH 2619 N N . GLN B 102 ? 0.3417 1.1187 0.6145 -0.2417 -0.0599 0.2548 100 GLN B N 2620 C CA . GLN B 102 ? 0.3106 1.0504 0.5698 -0.2313 -0.0467 0.2378 100 GLN B CA 2621 C C . GLN B 102 ? 0.2789 1.0419 0.5567 -0.2156 -0.0353 0.2359 100 GLN B C 2622 O O . GLN B 102 ? 0.2478 1.0501 0.5480 -0.1991 -0.0327 0.2407 100 GLN B O 2623 C CB . GLN B 102 ? 0.3068 1.0237 0.5566 -0.2178 -0.0445 0.2303 100 GLN B CB 2624 C CG . GLN B 102 ? 0.3209 1.0013 0.5566 -0.2109 -0.0324 0.2136 100 GLN B CG 2625 C CD . GLN B 102 ? 0.3174 0.9743 0.5410 -0.2049 -0.0321 0.2095 100 GLN B CD 2626 O OE1 . GLN B 102 ? 0.3813 1.0093 0.5894 -0.2064 -0.0241 0.1977 100 GLN B OE1 2627 N NE2 . GLN B 102 ? 0.2473 0.9185 0.4797 -0.1988 -0.0418 0.2211 100 GLN B NE2 2628 N N . CYS B 103 ? 0.2873 1.0265 0.5549 -0.2199 -0.0289 0.2282 101 CYS B N 2629 C CA . CYS B 103 ? 0.2773 1.0358 0.5562 -0.2086 -0.0193 0.2269 101 CYS B CA 2630 C C . CYS B 103 ? 0.2425 0.9716 0.5127 -0.1928 -0.0094 0.2100 101 CYS B C 2631 O O . CYS B 103 ? 0.2269 0.9195 0.4831 -0.1990 -0.0083 0.2021 101 CYS B O 2632 C CB . CYS B 103 ? 0.2844 1.0447 0.5622 -0.2285 -0.0235 0.2373 101 CYS B CB 2633 S SG . CYS B 103 ? 0.2779 1.0747 0.5675 -0.2213 -0.0145 0.2434 101 CYS B SG 2634 N N . LYS B 104 ? 0.2277 0.9751 0.5082 -0.1721 -0.0028 0.2040 102 LYS B N 2635 C CA . LYS B 104 ? 0.2423 0.9654 0.5164 -0.1581 0.0044 0.1884 102 LYS B CA 2636 C C . LYS B 104 ? 0.2308 0.9754 0.5098 -0.1478 0.0121 0.1835 102 LYS B C 2637 O O . LYS B 104 ? 0.2084 0.9851 0.4984 -0.1330 0.0161 0.1809 102 LYS B O 2638 C CB . LYS B 104 ? 0.2569 0.9721 0.5345 -0.1429 0.0031 0.1826 102 LYS B CB 2639 C CG . LYS B 104 ? 0.2996 0.9835 0.5644 -0.1529 -0.0035 0.1847 102 LYS B CG 2640 C CD . LYS B 104 ? 0.3589 1.0362 0.6297 -0.1381 -0.0077 0.1839 102 LYS B CD 2641 C CE . LYS B 104 ? 0.3871 1.0339 0.6416 -0.1499 -0.0143 0.1882 102 LYS B CE 2642 N NZ . LYS B 104 ? 0.4681 1.0969 0.7266 -0.1363 -0.0187 0.1872 102 LYS B NZ 2643 N N . VAL B 105 ? 0.2280 0.9539 0.4983 -0.1544 0.0139 0.1806 103 VAL B N 2644 C CA . VAL B 105 ? 0.2127 0.9555 0.4828 -0.1481 0.0190 0.1771 103 VAL B CA 2645 C C . VAL B 105 ? 0.2187 0.9354 0.4824 -0.1378 0.0222 0.1605 103 VAL B C 2646 O O . VAL B 105 ? 0.2260 0.9096 0.4846 -0.1433 0.0208 0.1564 103 VAL B O 2647 C CB . VAL B 105 ? 0.2093 0.9528 0.4768 -0.1640 0.0152 0.1901 103 VAL B CB 2648 C CG1 . VAL B 105 ? 0.2225 1.0018 0.4900 -0.1608 0.0190 0.1941 103 VAL B CG1 2649 C CG2 . VAL B 105 ? 0.1311 0.8809 0.4022 -0.1815 0.0080 0.2066 103 VAL B CG2 2650 N N . LYS B 106 ? 0.2107 0.9450 0.4747 -0.1236 0.0267 0.1501 104 LYS B N 2651 C CA . LYS B 106 ? 0.2098 0.9213 0.4676 -0.1161 0.0277 0.1342 104 LYS B CA 2652 C C . LYS B 106 ? 0.2171 0.9523 0.4689 -0.1106 0.0305 0.1274 104 LYS B C 2653 O O . LYS B 106 ? 0.2327 1.0004 0.4844 -0.1003 0.0351 0.1226 104 LYS B O 2654 C CB . LYS B 106 ? 0.2142 0.9077 0.4741 -0.1037 0.0268 0.1227 104 LYS B CB 2655 C CG . LYS B 106 ? 0.2375 0.9031 0.4979 -0.1114 0.0226 0.1291 104 LYS B CG 2656 C CD . LYS B 106 ? 0.2329 0.8828 0.4968 -0.0996 0.0187 0.1235 104 LYS B CD 2657 C CE . LYS B 106 ? 0.2154 0.8457 0.4770 -0.1103 0.0135 0.1347 104 LYS B CE 2658 N NZ . LYS B 106 ? 0.2644 0.8817 0.5316 -0.0991 0.0065 0.1351 104 LYS B NZ 2659 N N . LYS B 107 ? 0.2083 0.9301 0.4552 -0.1174 0.0278 0.1266 105 LYS B N 2660 C CA . LYS B 107 ? 0.2119 0.9522 0.4498 -0.1144 0.0280 0.1198 105 LYS B CA 2661 C C . LYS B 107 ? 0.2174 0.9308 0.4538 -0.1171 0.0233 0.1109 105 LYS B C 2662 O O . LYS B 107 ? 0.2057 0.9129 0.4464 -0.1258 0.0191 0.1202 105 LYS B O 2663 C CB . LYS B 107 ? 0.2096 0.9806 0.4449 -0.1244 0.0267 0.1379 105 LYS B CB 2664 C CG . LYS B 107 ? 0.2661 1.0690 0.4875 -0.1213 0.0281 0.1319 105 LYS B CG 2665 C CD . LYS B 107 ? 0.2600 1.1067 0.4766 -0.1305 0.0295 0.1511 105 LYS B CD 2666 C CE . LYS B 107 ? 0.2431 1.1144 0.4425 -0.1344 0.0266 0.1515 105 LYS B CE 2667 N NZ . LYS B 107 ? 0.2520 1.1069 0.4417 -0.1242 0.0258 0.1259 105 LYS B NZ 2668 N N . ALA B 108 ? 0.2297 0.9271 0.4622 -0.1091 0.0232 0.0930 106 ALA B N 2669 C CA . ALA B 108 ? 0.2362 0.9069 0.4704 -0.1141 0.0184 0.0853 106 ALA B CA 2670 C C . ALA B 108 ? 0.2443 0.9261 0.4804 -0.1227 0.0136 0.0924 106 ALA B C 2671 O O . ALA B 108 ? 0.2451 0.9524 0.4717 -0.1225 0.0114 0.0933 106 ALA B O 2672 C CB . ALA B 108 ? 0.2566 0.9141 0.4824 -0.1064 0.0158 0.0649 106 ALA B CB 2673 N N . PRO B 109 ? 0.2439 0.9093 0.4925 -0.1298 0.0118 0.0976 107 PRO B N 2674 C CA . PRO B 109 ? 0.2305 0.8705 0.4862 -0.1326 0.0152 0.0960 107 PRO B CA 2675 C C . PRO B 109 ? 0.2149 0.8510 0.4753 -0.1348 0.0194 0.1077 107 PRO B C 2676 O O . PRO B 109 ? 0.2445 0.8630 0.5073 -0.1385 0.0226 0.1074 107 PRO B O 2677 C CB . PRO B 109 ? 0.2135 0.8496 0.4804 -0.1396 0.0122 0.0941 107 PRO B CB 2678 C CG . PRO B 109 ? 0.1945 0.8514 0.4673 -0.1395 0.0076 0.1031 107 PRO B CG 2679 C CD . PRO B 109 ? 0.2541 0.9293 0.5114 -0.1352 0.0060 0.1047 107 PRO B CD 2680 N N . GLY B 110 ? 0.2023 0.8546 0.4623 -0.1347 0.0182 0.1184 108 GLY B N 2681 C CA . GLY B 110 ? 0.1951 0.8403 0.4589 -0.1393 0.0194 0.1293 108 GLY B CA 2682 C C . GLY B 110 ? 0.1952 0.8373 0.4536 -0.1392 0.0223 0.1306 108 GLY B C 2683 O O . GLY B 110 ? 0.1743 0.8296 0.4282 -0.1329 0.0233 0.1275 108 GLY B O 2684 N N . VAL B 111 ? 0.2066 0.8327 0.4657 -0.1454 0.0232 0.1344 109 VAL B N 2685 C CA . VAL B 111 ? 0.2298 0.8545 0.4840 -0.1478 0.0235 0.1382 109 VAL B CA 2686 C C . VAL B 111 ? 0.2394 0.8520 0.4915 -0.1578 0.0215 0.1447 109 VAL B C 2687 O O . VAL B 111 ? 0.2663 0.8607 0.5187 -0.1609 0.0231 0.1396 109 VAL B O 2688 C CB . VAL B 111 ? 0.2522 0.8615 0.5023 -0.1459 0.0254 0.1305 109 VAL B CB 2689 C CG1 . VAL B 111 ? 0.2056 0.7983 0.4567 -0.1503 0.0287 0.1235 109 VAL B CG1 2690 C CG2 . VAL B 111 ? 0.2666 0.8719 0.5115 -0.1508 0.0234 0.1372 109 VAL B CG2 2691 N N . ALA B 112 ? 0.2570 0.8813 0.5075 -0.1628 0.0180 0.1545 110 ALA B N 2692 C CA . ALA B 112 ? 0.2713 0.8816 0.5170 -0.1751 0.0136 0.1598 110 ALA B CA 2693 C C . ALA B 112 ? 0.2677 0.8872 0.5092 -0.1810 0.0099 0.1662 110 ALA B C 2694 O O . ALA B 112 ? 0.2434 0.8865 0.4907 -0.1737 0.0102 0.1700 110 ALA B O 2695 C CB . ALA B 112 ? 0.2702 0.8838 0.5206 -0.1821 0.0076 0.1708 110 ALA B CB 2696 N N . ASN B 113 ? 0.2803 0.8810 0.5123 -0.1934 0.0058 0.1663 111 ASN B N 2697 C CA . ASN B 113 ? 0.2802 0.8853 0.5050 -0.2021 0.0002 0.1717 111 ASN B CA 2698 C C . ASN B 113 ? 0.3110 0.9018 0.5266 -0.2200 -0.0082 0.1750 111 ASN B C 2699 O O . ASN B 113 ? 0.3190 0.8805 0.5263 -0.2240 -0.0074 0.1649 111 ASN B O 2700 C CB . ASN B 113 ? 0.2990 0.8894 0.5121 -0.1999 0.0039 0.1632 111 ASN B CB 2701 C CG . ASN B 113 ? 0.3660 0.9626 0.5707 -0.2089 -0.0041 0.1714 111 ASN B CG 2702 O OD1 . ASN B 113 ? 0.4284 1.0115 0.6169 -0.2237 -0.0088 0.1698 111 ASN B OD1 2703 N ND2 . ASN B 113 ? 0.3829 0.9993 0.5982 -0.1994 -0.0070 0.1794 111 ASN B ND2 2704 N N . LYS B 114 ? 0.3214 0.9339 0.5403 -0.2300 -0.0171 0.1884 112 LYS B N 2705 C CA . LYS B 114 ? 0.3477 0.9485 0.5573 -0.2507 -0.0284 0.1932 112 LYS B CA 2706 C C . LYS B 114 ? 0.3621 0.9807 0.5671 -0.2603 -0.0369 0.2012 112 LYS B C 2707 O O . LYS B 114 ? 0.3646 1.0204 0.5859 -0.2530 -0.0380 0.2130 112 LYS B O 2708 C CB . LYS B 114 ? 0.3653 0.9814 0.5886 -0.2601 -0.0350 0.2083 112 LYS B CB 2709 C CG . LYS B 114 ? 0.4288 1.0055 0.6458 -0.2691 -0.0400 0.2038 112 LYS B CG 2710 C CD . LYS B 114 ? 0.4942 1.0767 0.7160 -0.2924 -0.0549 0.2224 112 LYS B CD 2711 C CE . LYS B 114 ? 0.5722 1.1274 0.7983 -0.2964 -0.0602 0.2272 112 LYS B CE 2712 N NZ . LYS B 114 ? 0.6153 1.1859 0.8497 -0.3205 -0.0744 0.2521 112 LYS B NZ 2713 N N . LYS B 115 ? 0.3790 0.9721 0.5618 -0.2758 -0.0437 0.1940 113 LYS B N 2714 C CA . LYS B 115 ? 0.3786 0.9872 0.5532 -0.2884 -0.0549 0.2027 113 LYS B CA 2715 C C . LYS B 115 ? 0.3744 0.9862 0.5474 -0.3126 -0.0705 0.2121 113 LYS B C 2716 O O . LYS B 115 ? 0.3711 0.9481 0.5306 -0.3252 -0.0744 0.2024 113 LYS B O 2717 C CB . LYS B 115 ? 0.4075 0.9900 0.5524 -0.2925 -0.0530 0.1886 113 LYS B CB 2718 C CG . LYS B 115 ? 0.4522 1.0290 0.5965 -0.2739 -0.0388 0.1804 113 LYS B CG 2719 C CD . LYS B 115 ? 0.4784 1.0826 0.6368 -0.2627 -0.0414 0.1949 113 LYS B CD 2720 C CE . LYS B 115 ? 0.5018 1.0910 0.6500 -0.2531 -0.0318 0.1876 113 LYS B CE 2721 N NZ . LYS B 115 ? 0.4826 1.0534 0.6327 -0.2435 -0.0169 0.1715 113 LYS B NZ 2722 N N . PHE B 116 ? 0.3736 1.0274 0.5623 -0.3187 -0.0805 0.2310 114 PHE B N 2723 C CA . PHE B 116 ? 0.3909 1.0578 0.5817 -0.3452 -0.0978 0.2442 114 PHE B CA 2724 C C . PHE B 116 ? 0.4080 1.0950 0.5913 -0.3574 -0.1119 0.2527 114 PHE B C 2725 O O . PHE B 116 ? 0.3951 1.1198 0.5967 -0.3430 -0.1114 0.2642 114 PHE B O 2726 C CB . PHE B 116 ? 0.3529 1.0662 0.5773 -0.3442 -0.0979 0.2642 114 PHE B CB 2727 C CG . PHE B 116 ? 0.4114 1.1046 0.6392 -0.3443 -0.0917 0.2620 114 PHE B CG 2728 C CD1 . PHE B 116 ? 0.5102 1.1729 0.7280 -0.3696 -0.1043 0.2643 114 PHE B CD1 2729 C CD2 . PHE B 116 ? 0.4134 1.1162 0.6537 -0.3202 -0.0757 0.2589 114 PHE B CD2 2730 C CE1 . PHE B 116 ? 0.5122 1.1543 0.7346 -0.3698 -0.1017 0.2661 114 PHE B CE1 2731 C CE2 . PHE B 116 ? 0.4502 1.1366 0.6930 -0.3213 -0.0725 0.2599 114 PHE B CE2 2732 C CZ . PHE B 116 ? 0.5006 1.1564 0.7354 -0.3458 -0.0859 0.2650 114 PHE B CZ 2733 N N . LEU B 117 ? 0.4470 1.1071 0.6031 -0.3835 -0.1258 0.2464 115 LEU B N 2734 C CA . LEU B 117 ? 0.4814 1.1591 0.6248 -0.4003 -0.1426 0.2548 115 LEU B CA 2735 C C . LEU B 117 ? 0.5182 1.2313 0.6805 -0.4252 -0.1619 0.2755 115 LEU B C 2736 O O . LEU B 117 ? 0.5564 1.2428 0.7048 -0.4509 -0.1732 0.2712 115 LEU B O 2737 C CB . LEU B 117 ? 0.5275 1.1566 0.6235 -0.4154 -0.1463 0.2325 115 LEU B CB 2738 C CG . LEU B 117 ? 0.5760 1.2189 0.6521 -0.4175 -0.1529 0.2367 115 LEU B CG 2739 C CD1 . LEU B 117 ? 0.6319 1.2299 0.6568 -0.4306 -0.1514 0.2113 115 LEU B CD1 2740 C CD2 . LEU B 117 ? 0.5689 1.2580 0.6598 -0.4357 -0.1763 0.2619 115 LEU B CD2 2741 N N . LEU B 118 ? 0.5148 1.2886 0.7106 -0.4173 -0.1665 0.2980 116 LEU B N 2742 C CA . LEU B 118 ? 0.5397 1.3640 0.7638 -0.4382 -0.1825 0.3215 116 LEU B CA 2743 C C . LEU B 118 ? 0.5863 1.4280 0.7992 -0.4632 -0.2067 0.3319 116 LEU B C 2744 O O . LEU B 118 ? 0.6075 1.4572 0.8123 -0.4532 -0.2107 0.3335 116 LEU B O 2745 C CB . LEU B 118 ? 0.5033 1.3945 0.7763 -0.4137 -0.1726 0.3397 116 LEU B CB 2746 C CG . LEU B 118 ? 0.5120 1.4641 0.8195 -0.4345 -0.1836 0.3643 116 LEU B CG 2747 C CD1 . LEU B 118 ? 0.5180 1.4423 0.8181 -0.4552 -0.1819 0.3630 116 LEU B CD1 2748 C CD2 . LEU B 118 ? 0.5060 1.5318 0.8613 -0.4060 -0.1723 0.3788 116 LEU B CD2 2749 N N . THR B 119 ? 0.6163 1.4633 0.8288 -0.4980 -0.2249 0.3407 117 THR B N 2750 C CA . THR B 119 ? 0.6480 1.5114 0.8483 -0.5295 -0.2519 0.3508 117 THR B CA 2751 C C . THR B 119 ? 0.6345 1.5621 0.8756 -0.5523 -0.2677 0.3794 117 THR B C 2752 O O . THR B 119 ? 0.6218 1.5445 0.8736 -0.5679 -0.2669 0.3839 117 THR B O 2753 C CB . THR B 119 ? 0.7075 1.4985 0.8534 -0.5585 -0.2630 0.3265 117 THR B CB 2754 O OG1 . THR B 119 ? 0.7537 1.4891 0.8655 -0.5361 -0.2437 0.2983 117 THR B OG1 2755 C CG2 . THR B 119 ? 0.7398 1.5436 0.8631 -0.5893 -0.2906 0.3326 117 THR B CG2 2756 N N . VAL B 120 ? 0.6287 1.6188 0.8938 -0.5550 -0.2831 0.4008 118 VAL B N 2757 C CA . VAL B 120 ? 0.6154 1.6829 0.9266 -0.5749 -0.2980 0.4309 118 VAL B CA 2758 C C . VAL B 120 ? 0.6553 1.7389 0.9541 -0.6145 -0.3313 0.4428 118 VAL B C 2759 O O . VAL B 120 ? 0.6642 1.7787 0.9667 -0.6077 -0.3437 0.4522 118 VAL B O 2760 C CB . VAL B 120 ? 0.5726 1.7221 0.9410 -0.5381 -0.2859 0.4499 118 VAL B CB 2761 C CG1 . VAL B 120 ? 0.5271 1.7681 0.9461 -0.5596 -0.3019 0.4816 118 VAL B CG1 2762 C CG2 . VAL B 120 ? 0.4747 1.6147 0.8562 -0.5029 -0.2542 0.4384 118 VAL B CG2 2763 N N . LEU B 121 ? 0.6890 1.7503 0.9732 -0.6571 -0.3478 0.4435 119 LEU B N 2764 C CA . LEU B 121 ? 0.7318 1.8082 1.0041 -0.7019 -0.3824 0.4550 119 LEU B CA 2765 C C . LEU B 121 ? 0.7073 1.8837 1.0408 -0.7191 -0.3963 0.4924 119 LEU B C 2766 O O . LEU B 121 ? 0.6669 1.8907 1.0453 -0.7053 -0.3793 0.5071 119 LEU B O 2767 C CB . LEU B 121 ? 0.7905 1.7844 1.0134 -0.7416 -0.3960 0.4341 119 LEU B CB 2768 C CG . LEU B 121 ? 0.7945 1.6934 0.9546 -0.7286 -0.3847 0.3942 119 LEU B CG 2769 C CD1 . LEU B 121 ? 0.8322 1.6505 0.9503 -0.7645 -0.3984 0.3720 119 LEU B CD1 2770 C CD2 . LEU B 121 ? 0.7737 1.6777 0.9034 -0.7246 -0.3947 0.3882 119 LEU B CD2 2771 N N . VAL B 122 ? 0.7360 1.9468 1.0692 -0.7510 -0.4277 0.5076 120 VAL B N 2772 C CA . VAL B 122 ? 0.7229 2.0392 1.1173 -0.7686 -0.4443 0.5450 120 VAL B CA 2773 C C . VAL B 122 ? 0.7803 2.0943 1.1618 -0.8316 -0.4789 0.5558 120 VAL B C 2774 O O . VAL B 122 ? 0.8183 2.0927 1.1542 -0.8600 -0.5047 0.5450 120 VAL B O 2775 C CB . VAL B 122 ? 0.7032 2.0890 1.1276 -0.7436 -0.4531 0.5620 120 VAL B CB 2776 C CG1 . VAL B 122 ? 0.6628 2.1694 1.1633 -0.7491 -0.4625 0.5997 120 VAL B CG1 2777 C CG2 . VAL B 122 ? 0.6483 2.0149 1.0735 -0.6844 -0.4231 0.5470 120 VAL B CG2 2778 N N . LYS B 123 ? 0.9579 1.4487 1.0576 -0.3844 -0.0922 0.2237 121 LYS B N 2779 C CA . LYS B 123 ? 0.9007 1.4313 1.0687 -0.3416 -0.0640 0.2085 121 LYS B CA 2780 C C . LYS B 123 ? 0.9172 1.3760 1.0739 -0.2879 -0.0720 0.1392 121 LYS B C 2781 O O . LYS B 123 ? 0.9528 1.3716 1.0652 -0.2801 -0.0887 0.0793 121 LYS B O 2782 C CB . LYS B 123 ? 0.8779 1.4997 1.0782 -0.3654 -0.0453 0.2060 121 LYS B CB 2783 C CG . LYS B 123 ? 0.9579 1.5869 1.1118 -0.3777 -0.0542 0.1415 121 LYS B CG 2784 C CD . LYS B 123 ? 0.9645 1.7043 1.1344 -0.4290 -0.0411 0.1668 121 LYS B CD 2785 C CE . LYS B 123 ? 1.0302 1.7875 1.1427 -0.4419 -0.0504 0.1001 121 LYS B CE 2786 N NZ . LYS B 123 ? 0.9837 1.8741 1.1215 -0.4849 -0.0330 0.1143 121 LYS B NZ 2787 N N . PRO B 124 ? 0.8901 1.3338 1.0854 -0.2475 -0.0618 0.1455 122 PRO B N 2788 C CA . PRO B 124 ? 0.9100 1.2865 1.0943 -0.1994 -0.0724 0.0907 122 PRO B CA 2789 C C . PRO B 124 ? 0.9163 1.3205 1.1140 -0.1779 -0.0651 0.0279 122 PRO B C 2790 O O . PRO B 124 ? 0.8628 1.3419 1.1092 -0.1830 -0.0431 0.0346 122 PRO B O 2791 C CB . PRO B 124 ? 0.8538 1.2358 1.0829 -0.1696 -0.0573 0.1182 122 PRO B CB 2792 C CG . PRO B 124 ? 0.8042 1.2620 1.0829 -0.1882 -0.0343 0.1628 122 PRO B CG 2793 C CD . PRO B 124 ? 0.8374 1.3322 1.0919 -0.2406 -0.0395 0.1974 122 PRO B CD 2794 N N . SER B 125 ? 0.9903 1.3366 1.1422 -0.1552 -0.0878 -0.0305 123 SER B N 2795 C CA . SER B 125 ? 1.0087 1.3929 1.1691 -0.1244 -0.0829 -0.0979 123 SER B CA 2796 C C . SER B 125 ? 1.0983 1.3898 1.2113 -0.0785 -0.1146 -0.1589 123 SER B C 2797 O O . SER B 125 ? 1.1732 1.3692 1.2278 -0.0879 -0.1470 -0.1556 123 SER B O 2798 C CB . SER B 125 ? 1.0118 1.4815 1.1645 -0.1590 -0.0725 -0.1092 123 SER B CB 2799 O OG . SER B 125 ? 0.9947 1.5588 1.1837 -0.1399 -0.0546 -0.1497 123 SER B OG 2800 N N . GLY B 126 ? 1.0971 1.4175 1.2362 -0.0309 -0.1091 -0.2101 124 GLY B N 2801 C CA . GLY B 126 ? 1.1803 1.4231 1.2841 0.0241 -0.1398 -0.2717 124 GLY B CA 2802 C C . GLY B 126 ? 1.1762 1.3493 1.2920 0.0501 -0.1524 -0.2539 124 GLY B C 2803 O O . GLY B 126 ? 1.2564 1.3179 1.3268 0.0655 -0.1899 -0.2593 124 GLY B O 2804 N N . THR B 127 ? 1.0961 1.3336 1.2695 0.0511 -0.1247 -0.2310 125 THR B N 2805 C CA . THR B 127 ? 1.0866 1.2751 1.2731 0.0735 -0.1323 -0.2153 125 THR B CA 2806 C C . THR B 127 ? 1.1017 1.3102 1.3087 0.1260 -0.1375 -0.2689 125 THR B C 2807 O O . THR B 127 ? 1.0657 1.3735 1.3105 0.1330 -0.1164 -0.2939 125 THR B O 2808 C CB . THR B 127 ? 1.0107 1.2434 1.2408 0.0477 -0.1038 -0.1615 125 THR B CB 2809 O OG1 . THR B 127 ? 0.9517 1.2716 1.2312 0.0518 -0.0807 -0.1771 125 THR B OG1 2810 C CG2 . THR B 127 ? 0.9892 1.2380 1.2128 -0.0009 -0.0928 -0.1082 125 THR B CG2 2811 N N . ARG B 128 ? 1.1632 1.2847 1.3454 0.1588 -0.1689 -0.2809 126 ARG B N 2812 C CA . ARG B 128 ? 1.1834 1.3202 1.3862 0.2114 -0.1782 -0.3249 126 ARG B CA 2813 C C . ARG B 128 ? 1.1234 1.2792 1.3618 0.2070 -0.1644 -0.2947 126 ARG B C 2814 O O . ARG B 128 ? 1.1091 1.2117 1.3334 0.1859 -0.1690 -0.2504 126 ARG B O 2815 C CB . ARG B 128 ? 1.2910 1.3154 1.4464 0.2523 -0.2270 -0.3539 126 ARG B CB 2816 C CG . ARG B 128 ? 1.4252 1.3972 1.5299 0.2612 -0.2516 -0.3904 126 ARG B CG 2817 C CD . ARG B 128 ? 1.6023 1.4313 1.6534 0.2984 -0.3115 -0.4112 126 ARG B CD 2818 N NE . ARG B 128 ? 1.6693 1.4036 1.6911 0.2574 -0.3372 -0.3463 126 ARG B NE 2819 C CZ . ARG B 128 ? 1.8128 1.4131 1.7836 0.2680 -0.3961 -0.3408 126 ARG B CZ 2820 N NH1 . ARG B 128 ? 1.9365 1.4616 1.8785 0.3269 -0.4383 -0.4013 126 ARG B NH1 2821 N NH2 . ARG B 128 ? 1.8291 1.3738 1.7765 0.2204 -0.4159 -0.2734 126 ARG B NH2 2822 N N . CYS B 129 ? 1.0928 1.3345 1.3745 0.2254 -0.1486 -0.3198 127 CYS B N 2823 C CA . CYS B 129 ? 1.0561 1.3125 1.3661 0.2276 -0.1424 -0.3048 127 CYS B CA 2824 C C . CYS B 129 ? 1.0899 1.3387 1.4020 0.2784 -0.1674 -0.3424 127 CYS B C 2825 O O . CYS B 129 ? 1.1009 1.4251 1.4342 0.3085 -0.1667 -0.3847 127 CYS B O 2826 C CB . CYS B 129 ? 0.9939 1.3520 1.3498 0.2007 -0.1129 -0.2977 127 CYS B CB 2827 S SG . CYS B 129 ? 0.9893 1.3576 1.3534 0.1437 -0.0870 -0.2462 127 CYS B SG 2828 N N . PHE B 130 ? 1.1069 1.2777 1.3985 0.2882 -0.1901 -0.3247 128 PHE B N 2829 C CA . PHE B 130 ? 1.1378 1.2960 1.4319 0.3356 -0.2188 -0.3531 128 PHE B CA 2830 C C . PHE B 130 ? 1.1229 1.2514 1.4158 0.3301 -0.2285 -0.3253 128 PHE B C 2831 O O . PHE B 130 ? 1.1015 1.1867 1.3739 0.2977 -0.2244 -0.2845 128 PHE B O 2832 C CB . PHE B 130 ? 1.2275 1.2985 1.4812 0.3723 -0.2595 -0.3778 128 PHE B CB 2833 C CG . PHE B 130 ? 1.2654 1.2182 1.4680 0.3440 -0.2865 -0.3358 128 PHE B CG 2834 C CD1 . PHE B 130 ? 1.3004 1.1840 1.4827 0.3490 -0.3209 -0.3108 128 PHE B CD1 2835 C CD2 . PHE B 130 ? 1.2747 1.1961 1.4482 0.3075 -0.2806 -0.3171 128 PHE B CD2 2836 C CE1 . PHE B 130 ? 1.3474 1.1391 1.4815 0.3146 -0.3493 -0.2650 128 PHE B CE1 2837 C CE2 . PHE B 130 ? 1.3188 1.1462 1.4444 0.2743 -0.3085 -0.2724 128 PHE B CE2 2838 C CZ . PHE B 130 ? 1.3618 1.1272 1.4674 0.2763 -0.3433 -0.2451 128 PHE B CZ 2839 N N . VAL B 131 ? 1.1229 1.2917 1.4390 0.3634 -0.2404 -0.3494 129 VAL B N 2840 C CA . VAL B 131 ? 1.1203 1.2639 1.4315 0.3663 -0.2583 -0.3310 129 VAL B CA 2841 C C . VAL B 131 ? 1.1944 1.2536 1.4765 0.4030 -0.3075 -0.3349 129 VAL B C 2842 O O . VAL B 131 ? 1.2396 1.2744 1.5149 0.4414 -0.3284 -0.3673 129 VAL B O 2843 C CB . VAL B 131 ? 1.0824 1.3216 1.4348 0.3751 -0.2479 -0.3491 129 VAL B CB 2844 C CG1 . VAL B 131 ? 1.1267 1.4175 1.5025 0.4308 -0.2679 -0.3913 129 VAL B CG1 2845 C CG2 . VAL B 131 ? 1.0746 1.2917 1.4163 0.3628 -0.2589 -0.3251 129 VAL B CG2 2846 N N . ASP B 132 ? 1.2124 1.2255 1.4738 0.3910 -0.3292 -0.3020 130 ASP B N 2847 C CA . ASP B 132 ? 1.3031 1.2272 1.5343 0.4171 -0.3850 -0.2937 130 ASP B CA 2848 C C . ASP B 132 ? 1.3246 1.2840 1.5826 0.4610 -0.4092 -0.3134 130 ASP B C 2849 O O . ASP B 132 ? 1.3038 1.2861 1.5647 0.4451 -0.4129 -0.2896 130 ASP B O 2850 C CB . ASP B 132 ? 1.3228 1.1803 1.5099 0.3719 -0.4031 -0.2368 130 ASP B CB 2851 C CG . ASP B 132 ? 1.3462 1.1361 1.4952 0.3430 -0.4090 -0.2162 130 ASP B CG 2852 O OD1 . ASP B 132 ? 1.4620 1.1821 1.5920 0.3686 -0.4407 -0.2389 130 ASP B OD1 2853 O OD2 . ASP B 132 ? 1.2983 1.1070 1.4345 0.2968 -0.3838 -0.1790 130 ASP B OD2 2854 N N . GLY B 138 ? 1.1042 1.5582 1.3839 0.2607 -0.3664 -0.2805 136 GLY B N 2855 C CA . GLY B 138 ? 1.1306 1.5340 1.3585 0.2416 -0.3565 -0.2696 136 GLY B CA 2856 C C . GLY B 138 ? 1.1504 1.5048 1.3672 0.2609 -0.3693 -0.2406 136 GLY B C 2857 O O . GLY B 138 ? 1.1765 1.5231 1.3578 0.2497 -0.3853 -0.2151 136 GLY B O 2858 N N . ASN B 139 ? 1.1465 1.4715 1.3900 0.2850 -0.3649 -0.2431 137 ASN B N 2859 C CA . ASN B 139 ? 1.1805 1.4459 1.4127 0.3016 -0.3858 -0.2163 137 ASN B CA 2860 C C . ASN B 139 ? 1.1806 1.4063 1.3783 0.2792 -0.3622 -0.1997 137 ASN B C 2861 O O . ASN B 139 ? 1.1530 1.3981 1.3308 0.2573 -0.3325 -0.2084 137 ASN B O 2862 C CB . ASN B 139 ? 1.1797 1.4302 1.4497 0.3409 -0.3952 -0.2326 137 ASN B CB 2863 C CG . ASN B 139 ? 1.2364 1.4187 1.4942 0.3663 -0.4409 -0.2084 137 ASN B CG 2864 O OD1 . ASN B 139 ? 1.2930 1.4522 1.5220 0.3526 -0.4732 -0.1733 137 ASN B OD1 2865 N ND2 . ASN B 139 ? 1.2282 1.3757 1.5038 0.4014 -0.4477 -0.2268 137 ASN B ND2 2866 N N . ASP B 140 ? 1.2191 1.3891 1.4087 0.2874 -0.3790 -0.1773 138 ASP B N 2867 C CA . ASP B 140 ? 1.2395 1.3813 1.3957 0.2637 -0.3667 -0.1491 138 ASP B CA 2868 C C . ASP B 140 ? 1.2235 1.3282 1.3957 0.2728 -0.3481 -0.1599 138 ASP B C 2869 O O . ASP B 140 ? 1.2509 1.3059 1.4028 0.2649 -0.3646 -0.1325 138 ASP B O 2870 C CB . ASP B 140 ? 1.3086 1.4179 1.4306 0.2495 -0.4140 -0.0997 138 ASP B CB 2871 C CG . ASP B 140 ? 1.3332 1.4598 1.4142 0.2125 -0.4023 -0.0614 138 ASP B CG 2872 O OD1 . ASP B 140 ? 1.3242 1.4721 1.4065 0.2078 -0.3584 -0.0745 138 ASP B OD1 2873 O OD2 . ASP B 140 ? 1.3798 1.5068 1.4281 0.1875 -0.4396 -0.0146 138 ASP B OD2 2874 N N . PHE B 141 ? 1.1872 1.3202 1.3925 0.2825 -0.3163 -0.1966 139 PHE B N 2875 C CA . PHE B 141 ? 1.1672 1.2826 1.3937 0.2918 -0.2994 -0.2117 139 PHE B CA 2876 C C . PHE B 141 ? 1.1444 1.2330 1.3498 0.2700 -0.2796 -0.1882 139 PHE B C 2877 O O . PHE B 141 ? 1.1374 1.2381 1.3178 0.2495 -0.2670 -0.1658 139 PHE B O 2878 C CB . PHE B 141 ? 1.1285 1.2975 1.3930 0.2942 -0.2707 -0.2469 139 PHE B CB 2879 C CG . PHE B 141 ? 1.1597 1.3746 1.4543 0.3178 -0.2896 -0.2703 139 PHE B CG 2880 C CD1 . PHE B 141 ? 1.2418 1.4600 1.5589 0.3537 -0.3072 -0.2874 139 PHE B CD1 2881 C CD2 . PHE B 141 ? 1.1659 1.4262 1.4641 0.3066 -0.2912 -0.2768 139 PHE B CD2 2882 C CE1 . PHE B 141 ? 1.2844 1.5641 1.6336 0.3831 -0.3242 -0.3089 139 PHE B CE1 2883 C CE2 . PHE B 141 ? 1.2206 1.5394 1.5493 0.3262 -0.3094 -0.2932 139 PHE B CE2 2884 C CZ . PHE B 141 ? 1.2636 1.5990 1.6210 0.3669 -0.3250 -0.3082 139 PHE B CZ 2885 N N . LYS B 142 ? 1.1363 1.1986 1.3519 0.2771 -0.2779 -0.1950 140 LYS B N 2886 C CA . LYS B 142 ? 1.1126 1.1612 1.3171 0.2556 -0.2558 -0.1759 140 LYS B CA 2887 C C . LYS B 142 ? 1.0736 1.1331 1.3069 0.2630 -0.2370 -0.2022 140 LYS B C 2888 O O . LYS B 142 ? 1.0925 1.1319 1.3312 0.2853 -0.2574 -0.2224 140 LYS B O 2889 C CB . LYS B 142 ? 1.1623 1.1558 1.3266 0.2395 -0.2872 -0.1357 140 LYS B CB 2890 C CG . LYS B 142 ? 1.1599 1.1792 1.2943 0.2125 -0.2844 -0.0951 140 LYS B CG 2891 C CD . LYS B 142 ? 1.1836 1.1620 1.2760 0.1836 -0.3204 -0.0448 140 LYS B CD 2892 C CE . LYS B 142 ? 1.1666 1.2021 1.2314 0.1570 -0.3185 -0.0040 140 LYS B CE 2893 N NZ . LYS B 142 ? 1.2479 1.2510 1.2690 0.1198 -0.3664 0.0534 140 LYS B NZ 2894 N N . LEU B 143 ? 1.0232 1.1173 1.2735 0.2464 -0.2005 -0.2032 141 LEU B N 2895 C CA . LEU B 143 ? 0.9924 1.1082 1.2675 0.2417 -0.1811 -0.2173 141 LEU B CA 2896 C C . LEU B 143 ? 0.9914 1.0806 1.2471 0.2212 -0.1738 -0.1878 141 LEU B C 2897 O O . LEU B 143 ? 0.9802 1.0625 1.2166 0.2055 -0.1666 -0.1553 141 LEU B O 2898 C CB . LEU B 143 ? 0.9490 1.1137 1.2547 0.2293 -0.1544 -0.2296 141 LEU B CB 2899 C CG . LEU B 143 ? 0.9471 1.1518 1.2735 0.2391 -0.1625 -0.2566 141 LEU B CG 2900 C CD1 . LEU B 143 ? 0.9151 1.1699 1.2726 0.2167 -0.1443 -0.2655 141 LEU B CD1 2901 C CD2 . LEU B 143 ? 0.9087 1.1269 1.2426 0.2705 -0.1880 -0.2788 141 LEU B CD2 2902 N N . LYS B 144 ? 1.0014 1.0870 1.2611 0.2223 -0.1763 -0.2004 142 LYS B N 2903 C CA . LYS B 144 ? 1.0240 1.0723 1.2554 0.2024 -0.1827 -0.1745 142 LYS B CA 2904 C C . LYS B 144 ? 1.0036 1.0855 1.2525 0.1893 -0.1618 -0.1844 142 LYS B C 2905 O O . LYS B 144 ? 0.9913 1.1100 1.2622 0.2057 -0.1587 -0.2218 142 LYS B O 2906 C CB . LYS B 144 ? 1.0946 1.0706 1.2892 0.2170 -0.2278 -0.1788 142 LYS B CB 2907 C CG . LYS B 144 ? 1.1270 1.0508 1.2763 0.1856 -0.2502 -0.1291 142 LYS B CG 2908 C CD . LYS B 144 ? 1.1566 0.9971 1.2671 0.1959 -0.3058 -0.1245 142 LYS B CD 2909 C CE . LYS B 144 ? 1.1464 0.9970 1.2501 0.1926 -0.3180 -0.0978 142 LYS B CE 2910 N NZ . LYS B 144 ? 1.2129 0.9776 1.2733 0.1886 -0.3794 -0.0757 142 LYS B NZ 2911 N N . CYS B 145 ? 0.9946 1.0788 1.2347 0.1586 -0.1472 -0.1476 143 CYS B N 2912 C CA . CYS B 145 ? 0.9773 1.0942 1.2288 0.1371 -0.1296 -0.1456 143 CYS B CA 2913 C C . CYS B 145 ? 1.0073 1.0818 1.2181 0.1121 -0.1457 -0.1162 143 CYS B C 2914 O O . CYS B 145 ? 0.9898 1.0787 1.1965 0.0851 -0.1338 -0.0713 143 CYS B O 2915 C CB . CYS B 145 ? 0.9309 1.0995 1.2173 0.1194 -0.0971 -0.1230 143 CYS B CB 2916 S SG . CYS B 145 ? 0.9193 1.1519 1.2351 0.0921 -0.0762 -0.1241 143 CYS B SG 2917 N N . GLU B 146 ? 1.0666 1.0889 1.2453 0.1228 -0.1763 -0.1428 144 GLU B N 2918 C CA . GLU B 146 ? 1.1257 1.0825 1.2520 0.0953 -0.2059 -0.1168 144 GLU B CA 2919 C C . GLU B 146 ? 1.1259 1.0993 1.2425 0.0738 -0.1986 -0.1271 144 GLU B C 2920 O O . GLU B 146 ? 1.1617 1.1360 1.2765 0.0988 -0.2042 -0.1795 144 GLU B O 2921 C CB . GLU B 146 ? 1.2168 1.0780 1.3016 0.1193 -0.2566 -0.1383 144 GLU B CB 2922 C CG . GLU B 146 ? 1.3052 1.0827 1.3284 0.0802 -0.2988 -0.0964 144 GLU B CG 2923 C CD . GLU B 146 ? 1.4019 1.0790 1.3861 0.0967 -0.3552 -0.0983 144 GLU B CD 2924 O OE1 . GLU B 146 ? 1.3902 1.0631 1.3968 0.1461 -0.3606 -0.1385 144 GLU B OE1 2925 O OE2 . GLU B 146 ? 1.4798 1.0845 1.4104 0.0562 -0.3980 -0.0544 144 GLU B OE2 2926 N N . PRO B 147 ? 1.0946 1.0927 1.2046 0.0287 -0.1859 -0.0774 145 PRO B N 2927 C CA . PRO B 147 ? 1.0919 1.1162 1.1928 0.0013 -0.1778 -0.0812 145 PRO B CA 2928 C C . PRO B 147 ? 1.1780 1.1190 1.2109 -0.0253 -0.2192 -0.0768 145 PRO B C 2929 O O . PRO B 147 ? 1.2214 1.0968 1.2156 -0.0442 -0.2519 -0.0411 145 PRO B O 2930 C CB . PRO B 147 ? 1.0202 1.1195 1.1538 -0.0329 -0.1443 -0.0234 145 PRO B CB 2931 C CG . PRO B 147 ? 1.0213 1.1087 1.1532 -0.0316 -0.1486 0.0182 145 PRO B CG 2932 C CD . PRO B 147 ? 1.0724 1.0954 1.1877 0.0041 -0.1753 -0.0157 145 PRO B CD 2933 N N . LYS B 148 ? 1.2099 1.1564 1.2250 -0.0293 -0.2208 -0.1141 146 LYS B N 2934 C CA . LYS B 148 ? 1.3056 1.1824 1.2525 -0.0673 -0.2562 -0.1075 146 LYS B CA 2935 C C . LYS B 148 ? 1.3184 1.2359 1.2559 -0.0670 -0.2451 -0.1570 146 LYS B C 2936 O O . LYS B 148 ? 1.3250 1.2589 1.2735 -0.0164 -0.2412 -0.2254 146 LYS B O 2937 C CB . LYS B 148 ? 1.4272 1.1618 1.3101 -0.0525 -0.3174 -0.1252 146 LYS B CB 2938 C CG . LYS B 148 ? 1.5245 1.1809 1.3373 -0.1168 -0.3603 -0.0751 146 LYS B CG 2939 C CD . LYS B 148 ? 1.6666 1.1826 1.4219 -0.1148 -0.4260 -0.0674 146 LYS B CD 2940 C CE . LYS B 148 ? 1.7783 1.2136 1.4565 -0.1905 -0.4772 -0.0125 146 LYS B CE 2941 N NZ . LYS B 148 ? 1.9081 1.1884 1.5208 -0.1959 -0.5537 -0.0037 146 LYS B NZ 2942 N N . GLU B 149 ? 1.3139 1.2617 1.2309 -0.1234 -0.2400 -0.1220 147 GLU B N 2943 C CA . GLU B 149 ? 1.2971 1.2389 1.1996 -0.1824 -0.2476 -0.0391 147 GLU B CA 2944 C C . GLU B 149 ? 1.1602 1.2202 1.1358 -0.1945 -0.1988 0.0160 147 GLU B C 2945 O O . GLU B 149 ? 1.0859 1.2271 1.1171 -0.1728 -0.1620 -0.0039 147 GLU B O 2946 C CB . GLU B 149 ? 1.3757 1.2934 1.2167 -0.2407 -0.2710 -0.0247 147 GLU B CB 2947 C CG . GLU B 149 ? 1.5322 1.3156 1.2888 -0.2286 -0.3261 -0.0868 147 GLU B CG 2948 C CD . GLU B 149 ? 1.6265 1.3801 1.3140 -0.2929 -0.3525 -0.0730 147 GLU B CD 2949 O OE1 . GLU B 149 ? 1.6366 1.3637 1.2921 -0.3566 -0.3770 0.0001 147 GLU B OE1 2950 O OE2 . GLU B 149 ? 1.6800 1.4460 1.3429 -0.2817 -0.3496 -0.1352 147 GLU B OE2 2951 N N . GLY B 150 ? 1.1371 1.2051 1.1084 -0.2299 -0.2038 0.0871 148 GLY B N 2952 C CA . GLY B 150 ? 1.0327 1.2065 1.0647 -0.2401 -0.1641 0.1450 148 GLY B CA 2953 C C . GLY B 150 ? 1.0350 1.2302 1.0456 -0.2875 -0.1771 0.2228 148 GLY B C 2954 O O . GLY B 150 ? 1.1220 1.2570 1.0672 -0.3308 -0.2175 0.2395 148 GLY B O 2955 N N . SER B 151 ? 0.9477 1.2316 1.0116 -0.2789 -0.1456 0.2704 149 SER B N 2956 C CA . SER B 151 ? 0.9496 1.2853 1.0030 -0.3131 -0.1529 0.3458 149 SER B CA 2957 C C . SER B 151 ? 0.8714 1.2972 0.9866 -0.2744 -0.1171 0.3760 149 SER B C 2958 O O . SER B 151 ? 0.8061 1.2685 0.9773 -0.2389 -0.0846 0.3585 149 SER B O 2959 C CB . SER B 151 ? 0.9756 1.3549 1.0047 -0.3784 -0.1624 0.3947 149 SER B CB 2960 O OG . SER B 151 ? 0.9504 1.3615 1.0070 -0.3801 -0.1401 0.3726 149 SER B OG 2961 N N . LEU B 152 ? 0.8797 1.3404 0.9790 -0.2839 -0.1280 0.4221 150 LEU B N 2962 C CA . LEU B 152 ? 0.8228 1.3629 0.9670 -0.2375 -0.0995 0.4399 150 LEU B CA 2963 C C . LEU B 152 ? 0.7741 1.4379 0.9602 -0.2406 -0.0735 0.4975 150 LEU B C 2964 O O . LEU B 152 ? 0.7905 1.4905 0.9618 -0.2936 -0.0835 0.5408 150 LEU B O 2965 C CB . LEU B 152 ? 0.8604 1.4035 0.9665 -0.2470 -0.1235 0.4638 150 LEU B CB 2966 C CG . LEU B 152 ? 0.9214 1.3409 0.9870 -0.2403 -0.1554 0.4136 150 LEU B CG 2967 C CD1 . LEU B 152 ? 0.9727 1.4078 0.9998 -0.2618 -0.1842 0.4527 150 LEU B CD1 2968 C CD2 . LEU B 152 ? 0.8715 1.2533 0.9783 -0.1741 -0.1298 0.3450 150 LEU B CD2 2969 N N . PRO B 153 ? 0.7235 1.4504 0.9608 -0.1809 -0.0424 0.4963 151 PRO B N 2970 C CA . PRO B 153 ? 0.7079 1.3948 0.9602 -0.1199 -0.0307 0.4443 151 PRO B CA 2971 C C . PRO B 153 ? 0.6784 1.2846 0.9579 -0.0920 -0.0206 0.3836 151 PRO B C 2972 O O . PRO B 153 ? 0.6364 1.2649 0.9573 -0.0825 -0.0039 0.3889 151 PRO B O 2973 C CB . PRO B 153 ? 0.6845 1.4811 0.9763 -0.0710 -0.0040 0.4720 151 PRO B CB 2974 C CG . PRO B 153 ? 0.6647 1.5315 0.9896 -0.0867 0.0070 0.5185 151 PRO B CG 2975 C CD . PRO B 153 ? 0.6925 1.5315 0.9782 -0.1659 -0.0179 0.5436 151 PRO B CD 2976 N N . LEU B 154 ? 0.6861 1.2060 0.9411 -0.0838 -0.0350 0.3320 152 LEU B N 2977 C CA . LEU B 154 ? 0.6631 1.1199 0.9400 -0.0602 -0.0285 0.2737 152 LEU B CA 2978 C C . LEU B 154 ? 0.6554 1.1119 0.9655 -0.0042 -0.0106 0.2469 152 LEU B C 2979 O O . LEU B 154 ? 0.6635 1.1425 0.9645 0.0225 -0.0082 0.2512 152 LEU B O 2980 C CB . LEU B 154 ? 0.6861 1.0598 0.9239 -0.0702 -0.0537 0.2290 152 LEU B CB 2981 C CG . LEU B 154 ? 0.7116 1.0562 0.9171 -0.1159 -0.0731 0.2279 152 LEU B CG 2982 C CD1 . LEU B 154 ? 0.7615 1.0179 0.9194 -0.1159 -0.1062 0.1880 152 LEU B CD1 2983 C CD2 . LEU B 154 ? 0.6806 1.0442 0.9202 -0.1188 -0.0556 0.2068 152 LEU B CD2 2984 N N . GLN B 155 ? 0.6547 1.0885 0.9992 0.0087 -0.0010 0.2204 153 GLN B N 2985 C CA . GLN B 155 ? 0.6746 1.0820 1.0432 0.0548 0.0077 0.1871 153 GLN B CA 2986 C C . GLN B 155 ? 0.6969 1.0476 1.0663 0.0522 -0.0007 0.1359 153 GLN B C 2987 O O . GLN B 155 ? 0.6857 1.0351 1.0578 0.0208 -0.0054 0.1287 153 GLN B O 2988 C CB . GLN B 155 ? 0.6619 1.0940 1.0725 0.0730 0.0198 0.2106 153 GLN B CB 2989 C CG . GLN B 155 ? 0.6790 1.1682 1.0953 0.1105 0.0310 0.2408 153 GLN B CG 2990 C CD . GLN B 155 ? 0.7208 1.2258 1.1797 0.1367 0.0375 0.2639 153 GLN B CD 2991 O OE1 . GLN B 155 ? 0.7363 1.2186 1.2195 0.1106 0.0315 0.2732 153 GLN B OE1 2992 N NE2 . GLN B 155 ? 0.7066 1.2558 1.1742 0.1903 0.0473 0.2739 153 GLN B NE2 2993 N N . PHE B 156 ? 0.7363 1.0532 1.1020 0.0855 -0.0026 0.1002 154 PHE B N 2994 C CA . PHE B 156 ? 0.7503 1.0276 1.1194 0.0862 -0.0112 0.0539 154 PHE B CA 2995 C C . PHE B 156 ? 0.7831 1.0340 1.1731 0.1113 -0.0092 0.0346 154 PHE B C 2996 O O . PHE B 156 ? 0.8059 1.0507 1.1918 0.1452 -0.0041 0.0364 154 PHE B O 2997 C CB . PHE B 156 ? 0.7593 1.0112 1.0956 0.0958 -0.0249 0.0264 154 PHE B CB 2998 C CG . PHE B 156 ? 0.7725 1.0304 1.0751 0.0765 -0.0359 0.0519 154 PHE B CG 2999 C CD1 . PHE B 156 ? 0.8042 1.0910 1.0892 0.0808 -0.0341 0.0872 154 PHE B CD1 3000 C CD2 . PHE B 156 ? 0.7760 1.0132 1.0605 0.0533 -0.0515 0.0402 154 PHE B CD2 3001 C CE1 . PHE B 156 ? 0.8219 1.1138 1.0714 0.0514 -0.0513 0.1188 154 PHE B CE1 3002 C CE2 . PHE B 156 ? 0.8261 1.0486 1.0712 0.0305 -0.0706 0.0643 154 PHE B CE2 3003 C CZ . PHE B 156 ? 0.8538 1.1021 1.0811 0.0240 -0.0724 0.1080 154 PHE B CZ 3004 N N . GLU B 157 ? 0.8061 1.0450 1.2149 0.0931 -0.0159 0.0155 155 GLU B N 3005 C CA . GLU B 157 ? 0.8519 1.0516 1.2728 0.1050 -0.0239 -0.0041 155 GLU B CA 3006 C C . GLU B 157 ? 0.8627 1.0634 1.2872 0.0855 -0.0356 -0.0369 155 GLU B C 3007 O O . GLU B 157 ? 0.8600 1.0990 1.3029 0.0508 -0.0379 -0.0313 155 GLU B O 3008 C CB . GLU B 157 ? 0.8679 1.0601 1.3170 0.0930 -0.0266 0.0276 155 GLU B CB 3009 C CG . GLU B 157 ? 0.9426 1.0689 1.3944 0.1107 -0.0424 0.0124 155 GLU B CG 3010 C CD . GLU B 157 ? 1.0207 1.1274 1.5006 0.0896 -0.0561 0.0475 155 GLU B CD 3011 O OE1 . GLU B 157 ? 1.0323 1.1703 1.5311 0.0382 -0.0645 0.0643 155 GLU B OE1 3012 O OE2 . GLU B 157 ? 1.0953 1.1607 1.5784 0.1259 -0.0605 0.0592 155 GLU B OE2 3013 N N . TRP B 158 ? 0.8807 1.0532 1.2878 0.1077 -0.0427 -0.0698 156 TRP B N 3014 C CA . TRP B 158 ? 0.8749 1.0608 1.2858 0.0939 -0.0547 -0.1002 156 TRP B CA 3015 C C . TRP B 158 ? 0.9199 1.0742 1.3408 0.0782 -0.0700 -0.1047 156 TRP B C 3016 O O . TRP B 158 ? 0.9757 1.0713 1.3862 0.0973 -0.0744 -0.1025 156 TRP B O 3017 C CB . TRP B 158 ? 0.8775 1.0531 1.2631 0.1218 -0.0592 -0.1292 156 TRP B CB 3018 C CG . TRP B 158 ? 0.8619 1.0443 1.2265 0.1366 -0.0548 -0.1211 156 TRP B CG 3019 C CD1 . TRP B 158 ? 0.8810 1.0582 1.2306 0.1467 -0.0457 -0.0938 156 TRP B CD1 3020 C CD2 . TRP B 158 ? 0.8564 1.0494 1.2094 0.1421 -0.0655 -0.1384 156 TRP B CD2 3021 N NE1 . TRP B 158 ? 0.8459 1.0267 1.1723 0.1475 -0.0528 -0.0879 156 TRP B NE1 3022 C CE2 . TRP B 158 ? 0.8685 1.0475 1.1951 0.1477 -0.0670 -0.1170 156 TRP B CE2 3023 C CE3 . TRP B 158 ? 0.8463 1.0624 1.2086 0.1443 -0.0771 -0.1687 156 TRP B CE3 3024 C CZ2 . TRP B 158 ? 0.8532 1.0178 1.1579 0.1530 -0.0853 -0.1250 156 TRP B CZ2 3025 C CZ3 . TRP B 158 ? 0.8627 1.0715 1.2075 0.1609 -0.0913 -0.1818 156 TRP B CZ3 3026 C CH2 . TRP B 158 ? 0.8644 1.0363 1.1784 0.1640 -0.0980 -0.1600 156 TRP B CH2 3027 N N . GLN B 159 ? 0.9115 1.1070 1.3495 0.0437 -0.0813 -0.1116 157 GLN B N 3028 C CA . GLN B 159 ? 0.9524 1.1210 1.3965 0.0126 -0.1046 -0.1092 157 GLN B CA 3029 C C . GLN B 159 ? 0.9456 1.1720 1.3964 -0.0126 -0.1179 -0.1298 157 GLN B C 3030 O O . GLN B 159 ? 0.9082 1.1846 1.3578 0.0078 -0.1094 -0.1543 157 GLN B O 3031 C CB . GLN B 159 ? 0.9617 1.1373 1.4295 -0.0286 -0.1125 -0.0682 157 GLN B CB 3032 C CG . GLN B 159 ? 0.9731 1.1048 1.4416 -0.0055 -0.1021 -0.0414 157 GLN B CG 3033 C CD . GLN B 159 ? 0.9756 1.1289 1.4711 -0.0499 -0.1112 0.0044 157 GLN B CD 3034 O OE1 . GLN B 159 ? 1.0137 1.1932 1.5230 -0.1017 -0.1325 0.0190 157 GLN B OE1 3035 N NE2 . GLN B 159 ? 0.9667 1.1193 1.4702 -0.0347 -0.0975 0.0325 157 GLN B NE2 3036 N N . LYS B 160 ? 0.9821 1.2002 1.4394 -0.0580 -0.1433 -0.1164 158 LYS B N 3037 C CA . LYS B 160 ? 0.9737 1.2679 1.4417 -0.0949 -0.1594 -0.1247 158 LYS B CA 3038 C C . LYS B 160 ? 1.0084 1.3330 1.4942 -0.1658 -0.1848 -0.0861 158 LYS B C 3039 O O . LYS B 160 ? 1.0590 1.2992 1.5390 -0.1837 -0.2015 -0.0581 158 LYS B O 3040 C CB . LYS B 160 ? 1.0165 1.2575 1.4570 -0.0815 -0.1762 -0.1535 158 LYS B CB 3041 C CG . LYS B 160 ? 0.9712 1.2668 1.4097 -0.0420 -0.1622 -0.1867 158 LYS B CG 3042 C CD . LYS B 160 ? 1.0037 1.2563 1.4148 -0.0371 -0.1812 -0.2104 158 LYS B CD 3043 C CE . LYS B 160 ? 0.9666 1.2766 1.3791 0.0000 -0.1726 -0.2369 158 LYS B CE 3044 N NZ . LYS B 160 ? 1.0072 1.3037 1.3982 -0.0081 -0.1945 -0.2549 158 LYS B NZ 3045 N N . MET B 167 ? 1.2845 1.2458 1.6162 -0.0273 -0.2186 -0.2175 165 MET B N 3046 C CA . MET B 167 ? 1.3637 1.2052 1.6587 0.0083 -0.2255 -0.2334 165 MET B CA 3047 C C . MET B 167 ? 1.3721 1.2010 1.6316 0.0584 -0.2126 -0.2734 165 MET B C 3048 O O . MET B 167 ? 1.4675 1.2105 1.6836 0.0735 -0.2310 -0.3026 165 MET B O 3049 C CB . MET B 167 ? 1.4776 1.2206 1.7472 -0.0352 -0.2724 -0.2311 165 MET B CB 3050 C CG . MET B 167 ? 1.4791 1.2546 1.7809 -0.1071 -0.2960 -0.1844 165 MET B CG 3051 S SD . MET B 167 ? 1.5528 1.2305 1.8622 -0.1091 -0.3130 -0.1483 165 MET B SD 3052 C CE . MET B 167 ? 1.6865 1.1841 1.9366 -0.1268 -0.3760 -0.1673 165 MET B CE 3053 N N . PRO B 168 ? 1.2857 1.1971 1.5595 0.0835 -0.1848 -0.2749 166 PRO B N 3054 C CA . PRO B 168 ? 1.2877 1.2097 1.5313 0.1155 -0.1790 -0.3040 166 PRO B CA 3055 C C . PRO B 168 ? 1.3318 1.2002 1.5382 0.1657 -0.1677 -0.3236 166 PRO B C 3056 O O . PRO B 168 ? 1.3015 1.1811 1.5181 0.1954 -0.1451 -0.3075 166 PRO B O 3057 C CB . PRO B 168 ? 1.1960 1.2080 1.4677 0.1255 -0.1593 -0.2905 166 PRO B CB 3058 C CG . PRO B 168 ? 1.1607 1.1921 1.4655 0.1197 -0.1440 -0.2610 166 PRO B CG 3059 C CD . PRO B 168 ? 1.2006 1.1872 1.5138 0.0849 -0.1607 -0.2481 166 PRO B CD 3060 N N . THR B 169 ? 1.4062 1.2281 1.5679 0.1741 -0.1841 -0.3591 167 THR B N 3061 C CA . THR B 169 ? 1.4719 1.2475 1.5910 0.2255 -0.1765 -0.3884 167 THR B CA 3062 C C . THR B 169 ? 1.4136 1.2669 1.5268 0.2651 -0.1464 -0.3846 167 THR B C 3063 O O . THR B 169 ? 1.4204 1.2786 1.5283 0.3064 -0.1274 -0.3823 167 THR B O 3064 C CB . THR B 169 ? 1.5856 1.2894 1.6489 0.2229 -0.2051 -0.4347 167 THR B CB 3065 O OG1 . THR B 169 ? 1.5831 1.3238 1.6479 0.1760 -0.2230 -0.4343 167 THR B OG1 3066 C CG2 . THR B 169 ? 1.6790 1.2614 1.7264 0.2131 -0.2360 -0.4449 167 THR B CG2 3067 N N . PRO B 170 ? 1.3623 1.2811 1.4764 0.2514 -0.1458 -0.3799 168 PRO B N 3068 C CA . PRO B 170 ? 1.3201 1.3069 1.4226 0.2793 -0.1260 -0.3692 168 PRO B CA 3069 C C . PRO B 170 ? 1.2330 1.2651 1.3745 0.2756 -0.1098 -0.3252 168 PRO B C 3070 O O . PRO B 170 ? 1.2027 1.2898 1.3365 0.2867 -0.0999 -0.3051 168 PRO B O 3071 C CB . PRO B 170 ? 1.3162 1.3404 1.4021 0.2618 -0.1414 -0.3784 168 PRO B CB 3072 C CG . PRO B 170 ? 1.3511 1.3360 1.4433 0.2259 -0.1662 -0.3944 168 PRO B CG 3073 C CD . PRO B 170 ? 1.3543 1.2922 1.4766 0.2116 -0.1668 -0.3824 168 PRO B CD 3074 N N . TRP B 171 ? 1.1968 1.2063 1.3754 0.2545 -0.1110 -0.3088 169 TRP B N 3075 C CA . TRP B 171 ? 1.1200 1.1630 1.3315 0.2488 -0.0970 -0.2715 169 TRP B CA 3076 C C . TRP B 171 ? 1.1186 1.1405 1.3409 0.2638 -0.0826 -0.2565 169 TRP B C 3077 O O . TRP B 171 ? 1.0748 1.1295 1.3158 0.2627 -0.0688 -0.2241 169 TRP B O 3078 C CB . TRP B 171 ? 1.0820 1.1382 1.3293 0.2147 -0.1070 -0.2626 169 TRP B CB 3079 C CG . TRP B 171 ? 1.0536 1.1460 1.3006 0.2087 -0.1203 -0.2695 169 TRP B CG 3080 C CD1 . TRP B 171 ? 1.0544 1.1634 1.2740 0.2235 -0.1263 -0.2738 169 TRP B CD1 3081 C CD2 . TRP B 171 ? 1.0362 1.1618 1.3135 0.1894 -0.1312 -0.2703 169 TRP B CD2 3082 N NE1 . TRP B 171 ? 1.0528 1.1900 1.2849 0.2162 -0.1434 -0.2762 169 TRP B NE1 3083 C CE2 . TRP B 171 ? 1.0351 1.1866 1.3032 0.1998 -0.1452 -0.2772 169 TRP B CE2 3084 C CE3 . TRP B 171 ? 1.0326 1.1801 1.3442 0.1651 -0.1313 -0.2652 169 TRP B CE3 3085 C CZ2 . TRP B 171 ? 0.9931 1.1880 1.2872 0.1962 -0.1588 -0.2831 169 TRP B CZ2 3086 C CZ3 . TRP B 171 ? 1.0176 1.2227 1.3533 0.1584 -0.1416 -0.2724 169 TRP B CZ3 3087 C CH2 . TRP B 171 ? 0.9910 1.2174 1.3190 0.1785 -0.1550 -0.2834 169 TRP B CH2 3088 N N . LEU B 172 ? 1.1730 1.1351 1.3812 0.2778 -0.0902 -0.2799 170 LEU B N 3089 C CA . LEU B 172 ? 1.1799 1.1090 1.4021 0.2951 -0.0841 -0.2662 170 LEU B CA 3090 C C . LEU B 172 ? 1.1412 1.1314 1.3651 0.3287 -0.0585 -0.2425 170 LEU B C 3091 O O . LEU B 172 ? 1.1075 1.1058 1.3581 0.3305 -0.0494 -0.2119 170 LEU B O 3092 C CB . LEU B 172 ? 1.2818 1.1217 1.4758 0.3177 -0.1031 -0.3028 170 LEU B CB 3093 C CG . LEU B 172 ? 1.3161 1.0853 1.5212 0.2697 -0.1343 -0.3024 170 LEU B CG 3094 C CD1 . LEU B 172 ? 1.4144 1.0868 1.5740 0.2770 -0.1648 -0.3470 170 LEU B CD1 3095 C CD2 . LEU B 172 ? 1.2999 1.0477 1.5422 0.2557 -0.1370 -0.2643 170 LEU B CD2 3096 N N . ALA B 173 ? 1.1423 1.1858 1.3372 0.3495 -0.0492 -0.2518 171 ALA B N 3097 C CA . ALA B 173 ? 1.1324 1.2560 1.3239 0.3744 -0.0276 -0.2244 171 ALA B CA 3098 C C . ALA B 173 ? 1.0643 1.2324 1.2806 0.3372 -0.0230 -0.1757 171 ALA B C 3099 O O . ALA B 173 ? 1.0443 1.2662 1.2699 0.3433 -0.0088 -0.1401 171 ALA B O 3100 C CB . ALA B 173 ? 1.1611 1.3421 1.3112 0.3965 -0.0234 -0.2433 171 ALA B CB 3101 N N . GLU B 174 ? 1.0445 1.1913 1.2689 0.3005 -0.0375 -0.1764 172 GLU B N 3102 C CA . GLU B 174 ? 1.0004 1.1730 1.2387 0.2689 -0.0400 -0.1416 172 GLU B CA 3103 C C . GLU B 174 ? 0.9637 1.1159 1.2371 0.2477 -0.0374 -0.1267 172 GLU B C 3104 O O . GLU B 174 ? 0.9292 1.0989 1.2122 0.2236 -0.0384 -0.1017 172 GLU B O 3105 C CB . GLU B 174 ? 1.0045 1.1665 1.2352 0.2502 -0.0595 -0.1552 172 GLU B CB 3106 C CG . GLU B 174 ? 1.0916 1.2766 1.2879 0.2614 -0.0680 -0.1647 172 GLU B CG 3107 C CD . GLU B 174 ? 1.1728 1.3426 1.3684 0.2461 -0.0913 -0.1766 172 GLU B CD 3108 O OE1 . GLU B 174 ? 1.2005 1.3436 1.4177 0.2388 -0.0974 -0.2000 172 GLU B OE1 3109 O OE2 . GLU B 174 ? 1.2637 1.4538 1.4382 0.2403 -0.1064 -0.1587 172 GLU B OE2 3110 N N . MET B 175 ? 0.9849 1.0961 1.2728 0.2537 -0.0383 -0.1424 173 MET B N 3111 C CA . MET B 175 ? 0.9653 1.0624 1.2868 0.2276 -0.0393 -0.1247 173 MET B CA 3112 C C . MET B 175 ? 0.9217 1.0626 1.2574 0.2144 -0.0268 -0.0831 173 MET B C 3113 O O . MET B 175 ? 0.8820 1.0305 1.2404 0.1829 -0.0284 -0.0681 173 MET B O 3114 C CB . MET B 175 ? 1.0223 1.0682 1.3515 0.2431 -0.0444 -0.1309 173 MET B CB 3115 C CG . MET B 175 ? 1.0637 1.0564 1.3976 0.2173 -0.0668 -0.1527 173 MET B CG 3116 S SD . MET B 175 ? 1.1468 1.0778 1.5022 0.2093 -0.0821 -0.1323 173 MET B SD 3117 C CE . MET B 175 ? 1.0331 1.0331 1.4280 0.1723 -0.0680 -0.0815 173 MET B CE 3118 N N . THR B 176 ? 0.9313 1.1111 1.2515 0.2355 -0.0155 -0.0633 174 THR B N 3119 C CA . THR B 176 ? 0.9148 1.1412 1.2457 0.2225 -0.0050 -0.0182 174 THR B CA 3120 C C . THR B 176 ? 0.8991 1.1584 1.2074 0.1987 -0.0102 0.0029 174 THR B C 3121 O O . THR B 176 ? 0.8825 1.1618 1.1954 0.1694 -0.0105 0.0345 174 THR B O 3122 C CB . THR B 176 ? 0.9394 1.2023 1.2715 0.2615 0.0091 -0.0020 174 THR B CB 3123 O OG1 . THR B 176 ? 0.9952 1.2097 1.3497 0.2813 0.0066 -0.0142 174 THR B OG1 3124 C CG2 . THR B 176 ? 0.9169 1.2493 1.2561 0.2447 0.0188 0.0509 174 THR B CG2 3125 N N . SER B 177 ? 0.9212 1.1808 1.2010 0.2083 -0.0190 -0.0131 175 SER B N 3126 C CA . SER B 177 ? 0.9242 1.1958 1.1764 0.1834 -0.0351 0.0076 175 SER B CA 3127 C C . SER B 177 ? 0.9005 1.1226 1.1566 0.1613 -0.0527 -0.0117 175 SER B C 3128 O O . SER B 177 ? 0.8859 1.0811 1.1607 0.1690 -0.0528 -0.0469 175 SER B O 3129 C CB . SER B 177 ? 0.9574 1.2474 1.1792 0.1987 -0.0432 -0.0008 175 SER B CB 3130 O OG . SER B 177 ? 0.9995 1.2557 1.2253 0.2226 -0.0431 -0.0474 175 SER B OG 3131 N N . PRO B 178 ? 0.8966 1.1098 1.1321 0.1342 -0.0702 0.0107 176 PRO B N 3132 C CA . PRO B 178 ? 0.8967 1.0676 1.1329 0.1225 -0.0869 -0.0127 176 PRO B CA 3133 C C . PRO B 178 ? 0.9238 1.0589 1.1473 0.1389 -0.1099 -0.0446 176 PRO B C 3134 O O . PRO B 178 ? 0.9426 1.0490 1.1680 0.1419 -0.1251 -0.0717 176 PRO B O 3135 C CB . PRO B 178 ? 0.9177 1.0795 1.1247 0.0904 -0.1039 0.0229 176 PRO B CB 3136 C CG . PRO B 178 ? 0.9322 1.1245 1.1133 0.0826 -0.1097 0.0637 176 PRO B CG 3137 C CD . PRO B 178 ? 0.9161 1.1613 1.1226 0.1119 -0.0789 0.0597 176 PRO B CD 3138 N N . VAL B 179 ? 0.9348 1.0804 1.1450 0.1523 -0.1126 -0.0419 177 VAL B N 3139 C CA . VAL B 179 ? 0.9542 1.0736 1.1537 0.1669 -0.1357 -0.0668 177 VAL B CA 3140 C C . VAL B 179 ? 0.9405 1.0813 1.1506 0.1880 -0.1219 -0.0914 177 VAL B C 3141 O O . VAL B 179 ? 0.9383 1.1115 1.1388 0.1945 -0.1068 -0.0796 177 VAL B O 3142 C CB . VAL B 179 ? 0.9996 1.1010 1.1580 0.1521 -0.1687 -0.0344 177 VAL B CB 3143 C CG1 . VAL B 179 ? 1.0070 1.0942 1.1568 0.1686 -0.1908 -0.0535 177 VAL B CG1 3144 C CG2 . VAL B 179 ? 1.0148 1.0631 1.1543 0.1328 -0.1965 -0.0225 177 VAL B CG2 3145 N N . ILE B 180 ? 0.9328 1.0600 1.1606 0.1996 -0.1287 -0.1280 178 ILE B N 3146 C CA . ILE B 180 ? 0.9357 1.0733 1.1671 0.2130 -0.1246 -0.1539 178 ILE B CA 3147 C C . ILE B 180 ? 0.9583 1.0903 1.1699 0.2200 -0.1521 -0.1585 178 ILE B C 3148 O O . ILE B 180 ? 0.9538 1.0803 1.1803 0.2282 -0.1678 -0.1820 178 ILE B O 3149 C CB . ILE B 180 ? 0.9238 1.0643 1.1887 0.2120 -0.1178 -0.1850 178 ILE B CB 3150 C CG1 . ILE B 180 ? 0.8734 1.0179 1.1596 0.1994 -0.0968 -0.1744 178 ILE B CG1 3151 C CG2 . ILE B 180 ? 0.9445 1.0868 1.2053 0.2180 -0.1201 -0.2101 178 ILE B CG2 3152 C CD1 . ILE B 180 ? 0.8249 0.9835 1.1424 0.1865 -0.0958 -0.1946 178 ILE B CD1 3153 N N . SER B 181 ? 0.9725 1.1178 1.1520 0.2159 -0.1591 -0.1326 179 SER B N 3154 C CA . SER B 181 ? 0.9998 1.1452 1.1573 0.2167 -0.1886 -0.1280 179 SER B CA 3155 C C . SER B 181 ? 0.9961 1.1596 1.1581 0.2286 -0.1836 -0.1626 179 SER B C 3156 O O . SER B 181 ? 1.0052 1.1982 1.1465 0.2313 -0.1707 -0.1669 179 SER B O 3157 C CB . SER B 181 ? 1.0252 1.1998 1.1449 0.1999 -0.1977 -0.0847 179 SER B CB 3158 O OG . SER B 181 ? 1.0034 1.2262 1.1187 0.2036 -0.1642 -0.0798 179 SER B OG 3159 N N . VAL B 182 ? 0.9870 1.1385 1.1744 0.2361 -0.1954 -0.1886 180 VAL B N 3160 C CA . VAL B 182 ? 0.9821 1.1517 1.1768 0.2395 -0.1954 -0.2199 180 VAL B CA 3161 C C . VAL B 182 ? 1.0058 1.1907 1.1804 0.2409 -0.2237 -0.2144 180 VAL B C 3162 O O . VAL B 182 ? 1.0113 1.1825 1.1834 0.2451 -0.2524 -0.1941 180 VAL B O 3163 C CB . VAL B 182 ? 0.9601 1.1362 1.1952 0.2417 -0.1954 -0.2443 180 VAL B CB 3164 C CG1 . VAL B 182 ? 0.9677 1.1690 1.2082 0.2354 -0.2011 -0.2695 180 VAL B CG1 3165 C CG2 . VAL B 182 ? 0.9023 1.0704 1.1564 0.2329 -0.1697 -0.2445 180 VAL B CG2 3166 N N . LYS B 183 ? 1.0238 1.2311 1.1802 0.2366 -0.2194 -0.2323 181 LYS B N 3167 C CA . LYS B 183 ? 1.0578 1.2912 1.1915 0.2327 -0.2452 -0.2256 181 LYS B CA 3168 C C . LYS B 183 ? 1.0639 1.3172 1.1955 0.2267 -0.2470 -0.2587 181 LYS B C 3169 O O . LYS B 183 ? 1.0738 1.3172 1.1935 0.2224 -0.2269 -0.2853 181 LYS B O 3170 C CB . LYS B 183 ? 1.0854 1.3450 1.1757 0.2246 -0.2428 -0.2002 181 LYS B CB 3171 C CG . LYS B 183 ? 1.1003 1.3481 1.1849 0.2180 -0.2514 -0.1558 181 LYS B CG 3172 C CD . LYS B 183 ? 1.1354 1.4350 1.1770 0.2004 -0.2595 -0.1199 181 LYS B CD 3173 C CE . LYS B 183 ? 1.1472 1.4386 1.1797 0.1835 -0.2690 -0.0706 181 LYS B CE 3174 N NZ . LYS B 183 ? 1.1859 1.5535 1.1771 0.1593 -0.2740 -0.0293 181 LYS B NZ 3175 N N . ASN B 184 ? 1.0667 1.3433 1.2078 0.2261 -0.2761 -0.2552 182 ASN B N 3176 C CA . ASN B 184 ? 1.0848 1.3907 1.2207 0.2132 -0.2847 -0.2797 182 ASN B CA 3177 C C . ASN B 184 ? 1.0679 1.3686 1.2320 0.2048 -0.2726 -0.3071 182 ASN B C 3178 O O . ASN B 184 ? 1.0445 1.3570 1.2516 0.2134 -0.2750 -0.3048 182 ASN B O 3179 C CB . ASN B 184 ? 1.1228 1.4389 1.2051 0.2011 -0.2765 -0.2921 182 ASN B CB 3180 C CG . ASN B 184 ? 1.1616 1.5076 1.2274 0.1826 -0.2941 -0.3127 182 ASN B CG 3181 O OD1 . ASN B 184 ? 1.1677 1.5429 1.2628 0.1789 -0.3177 -0.3049 182 ASN B OD1 3182 N ND2 . ASN B 184 ? 1.1944 1.5368 1.2112 0.1734 -0.2843 -0.3410 182 ASN B ND2 3183 N N . TYR B 193 ? 0.9035 1.5380 1.4423 -0.1326 -0.1204 -0.1163 191 TYR B N 3184 C CA . TYR B 193 ? 0.8915 1.4604 1.4088 -0.0669 -0.1054 -0.1487 191 TYR B CA 3185 C C . TYR B 193 ? 0.8520 1.4262 1.3657 -0.0455 -0.0841 -0.1479 191 TYR B C 3186 O O . TYR B 193 ? 0.8354 1.5071 1.3613 -0.0502 -0.0751 -0.1582 191 TYR B O 3187 C CB . TYR B 193 ? 0.8864 1.5130 1.4053 -0.0359 -0.1084 -0.1875 191 TYR B CB 3188 C CG . TYR B 193 ? 0.9212 1.4544 1.4129 0.0154 -0.1084 -0.2099 191 TYR B CG 3189 C CD1 . TYR B 193 ? 0.9307 1.4116 1.4042 0.0537 -0.0956 -0.2157 191 TYR B CD1 3190 C CD2 . TYR B 193 ? 0.9581 1.4605 1.4390 0.0183 -0.1244 -0.2211 191 TYR B CD2 3191 C CE1 . TYR B 193 ? 0.9481 1.3561 1.3954 0.0915 -0.0993 -0.2280 191 TYR B CE1 3192 C CE2 . TYR B 193 ? 0.9894 1.4200 1.4441 0.0599 -0.1253 -0.2379 191 TYR B CE2 3193 C CZ . TYR B 193 ? 0.9826 1.3700 1.4217 0.0955 -0.1129 -0.2394 191 TYR B CZ 3194 O OH . TYR B 193 ? 1.0397 1.3685 1.4517 0.1284 -0.1175 -0.2489 191 TYR B OH 3195 N N . SER B 194 ? 0.8376 1.3129 1.3312 -0.0218 -0.0775 -0.1371 192 SER B N 3196 C CA . SER B 194 ? 0.7970 1.2678 1.2838 -0.0152 -0.0619 -0.1236 192 SER B CA 3197 C C . SER B 194 ? 0.7946 1.1910 1.2521 0.0275 -0.0560 -0.1309 192 SER B C 3198 O O . SER B 194 ? 0.7973 1.1434 1.2384 0.0565 -0.0622 -0.1468 192 SER B O 3199 C CB . SER B 194 ? 0.8002 1.2547 1.3002 -0.0525 -0.0619 -0.0770 192 SER B CB 3200 O OG . SER B 194 ? 0.7575 1.3013 1.2823 -0.1031 -0.0673 -0.0595 192 SER B OG 3201 N N . CYS B 195 ? 0.7801 1.1818 1.2294 0.0237 -0.0462 -0.1157 193 CYS B N 3202 C CA . CYS B 195 ? 0.7761 1.1177 1.1999 0.0433 -0.0419 -0.0993 193 CYS B CA 3203 C C . CYS B 195 ? 0.7357 1.1004 1.1616 0.0166 -0.0324 -0.0661 193 CYS B C 3204 O O . CYS B 195 ? 0.7217 1.1112 1.1328 0.0109 -0.0324 -0.0766 193 CYS B O 3205 C CB . CYS B 195 ? 0.7974 1.1126 1.1911 0.0743 -0.0512 -0.1269 193 CYS B CB 3206 S SG . CYS B 195 ? 0.8554 1.1195 1.2144 0.0780 -0.0514 -0.0937 193 CYS B SG 3207 N N . THR B 196 ? 0.7227 1.0762 1.1650 0.0023 -0.0274 -0.0277 194 THR B N 3208 C CA . THR B 196 ? 0.7040 1.0867 1.1535 -0.0260 -0.0197 0.0125 194 THR B CA 3209 C C . THR B 196 ? 0.6905 1.0483 1.1152 -0.0123 -0.0149 0.0343 194 THR B C 3210 O O . THR B 196 ? 0.6988 1.0201 1.1161 0.0160 -0.0137 0.0423 194 THR B O 3211 C CB . THR B 196 ? 0.7121 1.0938 1.1932 -0.0461 -0.0223 0.0504 194 THR B CB 3212 O OG1 . THR B 196 ? 0.7206 1.1345 1.2218 -0.0742 -0.0326 0.0400 194 THR B OG1 3213 C CG2 . THR B 196 ? 0.6804 1.0999 1.1716 -0.0754 -0.0160 0.0968 194 THR B CG2 3214 N N . VAL B 197 ? 0.6716 1.0581 1.0802 -0.0362 -0.0138 0.0441 195 VAL B N 3215 C CA . VAL B 197 ? 0.6712 1.0409 1.0493 -0.0364 -0.0157 0.0682 195 VAL B CA 3216 C C . VAL B 197 ? 0.6480 1.0607 1.0350 -0.0706 -0.0087 0.1179 195 VAL B C 3217 O O . VAL B 197 ? 0.6376 1.0912 1.0275 -0.1041 -0.0079 0.1194 195 VAL B O 3218 C CB . VAL B 197 ? 0.6949 1.0391 1.0307 -0.0361 -0.0308 0.0352 195 VAL B CB 3219 C CG1 . VAL B 197 ? 0.7207 1.0461 1.0198 -0.0523 -0.0403 0.0701 195 VAL B CG1 3220 C CG2 . VAL B 197 ? 0.7119 1.0143 1.0395 0.0010 -0.0411 -0.0072 195 VAL B CG2 3221 N N . GLN B 198 ? 0.6401 1.0551 1.0304 -0.0606 -0.0039 0.1589 196 GLN B N 3222 C CA . GLN B 198 ? 0.6303 1.0950 1.0396 -0.0856 0.0030 0.2138 196 GLN B CA 3223 C C . GLN B 198 ? 0.6299 1.1178 1.0186 -0.0886 0.0030 0.2564 196 GLN B C 3224 O O . GLN B 198 ? 0.6257 1.1025 1.0036 -0.0572 0.0035 0.2569 196 GLN B O 3225 C CB . GLN B 198 ? 0.6298 1.0965 1.0854 -0.0664 0.0086 0.2305 196 GLN B CB 3226 C CG . GLN B 198 ? 0.6562 1.1516 1.1326 -0.0481 0.0149 0.2814 196 GLN B CG 3227 C CD . GLN B 198 ? 0.7103 1.1792 1.2260 -0.0195 0.0116 0.2880 196 GLN B CD 3228 O OE1 . GLN B 198 ? 0.6912 1.1472 1.2272 -0.0444 0.0022 0.2854 196 GLN B OE1 3229 N NE2 . GLN B 198 ? 0.7738 1.2359 1.2975 0.0326 0.0160 0.2966 196 GLN B NE2 3230 N N . ASN B 199 ? 0.6269 1.1586 1.0076 -0.1325 0.0009 0.2936 197 ASN B N 3231 C CA . ASN B 199 ? 0.6306 1.2128 1.0028 -0.1460 0.0011 0.3511 197 ASN B CA 3232 C C . ASN B 199 ? 0.6415 1.2899 1.0537 -0.1655 0.0098 0.4022 197 ASN B C 3233 O O . ASN B 199 ? 0.6332 1.2774 1.0841 -0.1562 0.0147 0.3959 197 ASN B O 3234 C CB . ASN B 199 ? 0.6414 1.2096 0.9542 -0.1889 -0.0187 0.3564 197 ASN B CB 3235 C CG . ASN B 199 ? 0.5924 1.1570 0.8834 -0.2369 -0.0277 0.3443 197 ASN B CG 3236 O OD1 . ASN B 199 ? 0.5210 1.1239 0.8457 -0.2488 -0.0163 0.3498 197 ASN B OD1 3237 N ND2 . ASN B 199 ? 0.4903 1.0071 0.7208 -0.2655 -0.0519 0.3269 197 ASN B ND2 3238 N N . ARG B 200 ? 0.6758 1.3872 1.0787 -0.1968 0.0076 0.4577 198 ARG B N 3239 C CA . ARG B 200 ? 0.6904 1.4743 1.1342 -0.2132 0.0138 0.5141 198 ARG B CA 3240 C C . ARG B 200 ? 0.6999 1.5075 1.1230 -0.2817 0.0052 0.5265 198 ARG B C 3241 O O . ARG B 200 ? 0.7214 1.6026 1.1583 -0.3154 0.0047 0.5849 198 ARG B O 3242 C CB . ARG B 200 ? 0.6996 1.5651 1.1565 -0.1987 0.0188 0.5745 198 ARG B CB 3243 C CG . ARG B 200 ? 0.7575 1.6240 1.2495 -0.1205 0.0311 0.5659 198 ARG B CG 3244 C CD . ARG B 200 ? 0.8177 1.7954 1.3355 -0.0979 0.0391 0.6287 198 ARG B CD 3245 N NE . ARG B 200 ? 0.8789 1.8578 1.4386 -0.0139 0.0499 0.6165 198 ARG B NE 3246 C CZ . ARG B 200 ? 0.8991 1.9734 1.4949 0.0305 0.0583 0.6606 198 ARG B CZ 3247 N NH1 . ARG B 200 ? 0.8815 2.0714 1.4809 -0.0072 0.0584 0.7277 198 ARG B NH1 3248 N NH2 . ARG B 200 ? 0.9490 2.0047 1.5756 0.1153 0.0645 0.6356 198 ARG B NH2 3249 N N . VAL B 201 ? 0.7036 1.4562 1.0920 -0.2995 -0.0020 0.4694 199 VAL B N 3250 C CA . VAL B 201 ? 0.7068 1.4839 1.0704 -0.3580 -0.0091 0.4656 199 VAL B CA 3251 C C . VAL B 201 ? 0.7134 1.4608 1.0741 -0.3545 -0.0079 0.4004 199 VAL B C 3252 O O . VAL B 201 ? 0.7267 1.5039 1.0644 -0.3963 -0.0118 0.3855 199 VAL B O 3253 C CB . VAL B 201 ? 0.7458 1.5058 1.0392 -0.4013 -0.0285 0.4673 199 VAL B CB 3254 C CG1 . VAL B 201 ? 0.7209 1.5285 1.0138 -0.4122 -0.0322 0.5363 199 VAL B CG1 3255 C CG2 . VAL B 201 ? 0.7944 1.4580 1.0385 -0.3784 -0.0430 0.3998 199 VAL B CG2 3256 N N . GLY B 202 ? 0.7020 1.4023 1.0839 -0.3055 -0.0026 0.3616 200 GLY B N 3257 C CA . GLY B 202 ? 0.7085 1.3942 1.0881 -0.2992 -0.0023 0.3003 200 GLY B CA 3258 C C . GLY B 202 ? 0.7074 1.3371 1.1033 -0.2466 0.0000 0.2601 200 GLY B C 3259 O O . GLY B 202 ? 0.7079 1.2963 1.1056 -0.2104 0.0004 0.2681 200 GLY B O 3260 N N . SER B 203 ? 0.7080 1.3510 1.1149 -0.2458 0.0011 0.2182 201 SER B N 3261 C CA . SER B 203 ? 0.7163 1.3174 1.1385 -0.2045 0.0009 0.1787 201 SER B CA 3262 C C . SER B 203 ? 0.7333 1.3391 1.1322 -0.1950 -0.0029 0.1118 201 SER B C 3263 O O . SER B 203 ? 0.7592 1.3956 1.1272 -0.2147 -0.0055 0.0890 201 SER B O 3264 C CB . SER B 203 ? 0.7076 1.3286 1.1806 -0.2108 0.0017 0.2056 201 SER B CB 3265 O OG . SER B 203 ? 0.7117 1.3171 1.2081 -0.2022 0.0021 0.2599 201 SER B OG 3266 N N . ASP B 204 ? 0.7326 1.3112 1.1456 -0.1615 -0.0044 0.0787 202 ASP B N 3267 C CA . ASP B 204 ? 0.7551 1.3365 1.1495 -0.1374 -0.0094 0.0143 202 ASP B CA 3268 C C . ASP B 204 ? 0.7546 1.3227 1.1751 -0.1100 -0.0111 -0.0074 202 ASP B C 3269 O O . ASP B 204 ? 0.7521 1.2677 1.1858 -0.0942 -0.0119 0.0141 202 ASP B O 3270 C CB . ASP B 204 ? 0.7892 1.2988 1.1330 -0.1113 -0.0221 -0.0127 202 ASP B CB 3271 C CG . ASP B 204 ? 0.8083 1.3325 1.1216 -0.0959 -0.0313 -0.0753 202 ASP B CG 3272 O OD1 . ASP B 204 ? 0.8145 1.4175 1.1279 -0.1213 -0.0246 -0.0869 202 ASP B OD1 3273 O OD2 . ASP B 204 ? 0.7903 1.2495 1.0778 -0.0558 -0.0472 -0.1137 202 ASP B OD2 3274 N N . GLN B 205 ? 0.7646 1.3886 1.1898 -0.1036 -0.0124 -0.0521 203 GLN B N 3275 C CA . GLN B 205 ? 0.7575 1.3897 1.2066 -0.0864 -0.0165 -0.0727 203 GLN B CA 3276 C C . GLN B 205 ? 0.7714 1.4173 1.2050 -0.0450 -0.0225 -0.1349 203 GLN B C 3277 O O . GLN B 205 ? 0.7849 1.4901 1.2042 -0.0396 -0.0214 -0.1700 203 GLN B O 3278 C CB . GLN B 205 ? 0.7438 1.4660 1.2304 -0.1326 -0.0154 -0.0484 203 GLN B CB 3279 C CG . GLN B 205 ? 0.7410 1.4109 1.2521 -0.1454 -0.0244 -0.0098 203 GLN B CG 3280 C CD . GLN B 205 ? 0.7433 1.4735 1.2791 -0.1698 -0.0355 -0.0150 203 GLN B CD 3281 O OE1 . GLN B 205 ? 0.7277 1.5159 1.2618 -0.1526 -0.0348 -0.0580 203 GLN B OE1 3282 N NE2 . GLN B 205 ? 0.7761 1.4932 1.3340 -0.2105 -0.0501 0.0312 203 GLN B NE2 3283 N N . CYS B 206 ? 0.7718 1.3659 1.2081 -0.0131 -0.0305 -0.1496 204 CYS B N 3284 C CA . CYS B 206 ? 0.7972 1.3866 1.2197 0.0341 -0.0411 -0.2028 204 CYS B CA 3285 C C . CYS B 206 ? 0.7742 1.3754 1.2205 0.0463 -0.0468 -0.2126 204 CYS B C 3286 O O . CYS B 206 ? 0.7667 1.3255 1.2236 0.0307 -0.0472 -0.1824 204 CYS B O 3287 C CB . CYS B 206 ? 0.8377 1.3188 1.2188 0.0649 -0.0540 -0.2084 204 CYS B CB 3288 S SG . CYS B 206 ? 0.9383 1.3818 1.2968 0.1264 -0.0778 -0.2661 204 CYS B SG 3289 N N . MET B 207 ? 0.7767 1.4365 1.2288 0.0772 -0.0533 -0.2572 205 MET B N 3290 C CA . MET B 207 ? 0.7698 1.4639 1.2459 0.0824 -0.0603 -0.2653 205 MET B CA 3291 C C . MET B 207 ? 0.7860 1.4551 1.2504 0.1406 -0.0755 -0.3072 205 MET B C 3292 O O . MET B 207 ? 0.8065 1.4782 1.2538 0.1805 -0.0821 -0.3439 205 MET B O 3293 C CB . MET B 207 ? 0.7510 1.5911 1.2616 0.0459 -0.0544 -0.2634 205 MET B CB 3294 C CG . MET B 207 ? 0.7638 1.6403 1.2833 -0.0120 -0.0437 -0.2221 205 MET B CG 3295 S SD . MET B 207 ? 0.8249 1.7936 1.3813 -0.0861 -0.0509 -0.1771 205 MET B SD 3296 C CE . MET B 207 ? 0.7267 1.7260 1.2866 -0.1411 -0.0417 -0.1314 205 MET B CE 3297 N N . LEU B 208 ? 0.7776 1.4142 1.2482 0.1452 -0.0848 -0.3011 206 LEU B N 3298 C CA . LEU B 208 ? 0.7976 1.4022 1.2583 0.1956 -0.1031 -0.3303 206 LEU B CA 3299 C C . LEU B 208 ? 0.7919 1.4618 1.2790 0.1904 -0.1100 -0.3349 206 LEU B C 3300 O O . LEU B 208 ? 0.7805 1.4723 1.2819 0.1432 -0.1055 -0.3085 206 LEU B O 3301 C CB . LEU B 208 ? 0.8136 1.2871 1.2404 0.2060 -0.1124 -0.3113 206 LEU B CB 3302 C CG . LEU B 208 ? 0.8510 1.2600 1.2518 0.2550 -0.1373 -0.3326 206 LEU B CG 3303 C CD1 . LEU B 208 ? 0.8802 1.1808 1.2446 0.2462 -0.1438 -0.3004 206 LEU B CD1 3304 C CD2 . LEU B 208 ? 0.8508 1.2903 1.2671 0.2821 -0.1533 -0.3512 206 LEU B CD2 3305 N N . ARG B 209 ? 0.8115 1.5058 1.3024 0.2384 -0.1259 -0.3668 207 ARG B N 3306 C CA . ARG B 209 ? 0.8053 1.5582 1.3178 0.2371 -0.1368 -0.3698 207 ARG B CA 3307 C C . ARG B 209 ? 0.8227 1.5011 1.3178 0.2791 -0.1590 -0.3793 207 ARG B C 3308 O O . ARG B 209 ? 0.8567 1.4767 1.3328 0.3262 -0.1730 -0.3969 207 ARG B O 3309 C CB . ARG B 209 ? 0.7979 1.7188 1.3481 0.2459 -0.1346 -0.3936 207 ARG B CB 3310 C CG . ARG B 209 ? 0.8300 1.8295 1.4042 0.2259 -0.1461 -0.3854 207 ARG B CG 3311 C CD . ARG B 209 ? 0.8459 2.0096 1.4545 0.1764 -0.1386 -0.3732 207 ARG B CD 3312 N NE . ARG B 209 ? 0.8800 2.0465 1.4917 0.1158 -0.1517 -0.3404 207 ARG B NE 3313 C CZ . ARG B 209 ? 0.9219 2.1201 1.5409 0.1236 -0.1696 -0.3443 207 ARG B CZ 3314 N NH1 . ARG B 209 ? 0.9630 2.1972 1.5926 0.1935 -0.1767 -0.3769 207 ARG B NH1 3315 N NH2 . ARG B 209 ? 0.9368 2.1248 1.5497 0.0608 -0.1847 -0.3151 207 ARG B NH2 3316 N N . LEU B 210 ? 0.8072 1.4849 1.3053 0.2557 -0.1662 -0.3647 208 LEU B N 3317 C CA . LEU B 210 ? 0.8177 1.4350 1.2983 0.2811 -0.1872 -0.3655 208 LEU B CA 3318 C C . LEU B 210 ? 0.8077 1.5211 1.3142 0.2765 -0.1999 -0.3717 208 LEU B C 3319 O O . LEU B 210 ? 0.7882 1.5875 1.3164 0.2338 -0.1928 -0.3639 208 LEU B O 3320 C CB . LEU B 210 ? 0.8154 1.3227 1.2610 0.2519 -0.1828 -0.3389 208 LEU B CB 3321 C CG . LEU B 210 ? 0.8096 1.2739 1.2337 0.2508 -0.1983 -0.3322 208 LEU B CG 3322 C CD1 . LEU B 210 ? 0.8388 1.2853 1.2555 0.2968 -0.2237 -0.3401 208 LEU B CD1 3323 C CD2 . LEU B 210 ? 0.7675 1.1413 1.1568 0.2299 -0.1870 -0.3122 208 LEU B CD2 3324 N N . ASP B 211 ? 0.8182 1.5213 1.3220 0.3160 -0.2229 -0.3810 209 ASP B N 3325 C CA . ASP B 211 ? 0.8135 1.6079 1.3396 0.3088 -0.2374 -0.3818 209 ASP B CA 3326 C C . ASP B 211 ? 0.8290 1.5701 1.3362 0.3278 -0.2626 -0.3758 209 ASP B C 3327 O O . ASP B 211 ? 0.8521 1.5330 1.3473 0.3754 -0.2805 -0.3807 209 ASP B O 3328 C CB . ASP B 211 ? 0.8137 1.7584 1.3851 0.3429 -0.2394 -0.4054 209 ASP B CB 3329 C CG . ASP B 211 ? 0.8091 1.8898 1.4092 0.2912 -0.2368 -0.3932 209 ASP B CG 3330 O OD1 . ASP B 211 ? 0.8898 1.9411 1.4740 0.2465 -0.2474 -0.3730 209 ASP B OD1 3331 O OD2 . ASP B 211 ? 0.7929 2.0123 1.4272 0.2908 -0.2265 -0.4028 209 ASP B OD2 3332 N N . VAL B 212 ? 0.8189 1.5821 1.3202 0.2844 -0.2680 -0.3630 210 VAL B N 3333 C CA . VAL B 212 ? 0.8394 1.5657 1.3184 0.2872 -0.2904 -0.3544 210 VAL B CA 3334 C C . VAL B 212 ? 0.8435 1.6924 1.3537 0.2869 -0.3100 -0.3560 210 VAL B C 3335 O O . VAL B 212 ? 0.8203 1.7855 1.3646 0.2686 -0.3041 -0.3595 210 VAL B O 3336 C CB . VAL B 212 ? 0.8492 1.4898 1.2830 0.2363 -0.2827 -0.3419 210 VAL B CB 3337 C CG1 . VAL B 212 ? 0.8733 1.5278 1.2888 0.2192 -0.3049 -0.3371 210 VAL B CG1 3338 C CG2 . VAL B 212 ? 0.8402 1.3665 1.2392 0.2500 -0.2717 -0.3347 210 VAL B CG2 3339 C C1 . NAG C . ? 0.8289 1.3674 1.0151 -0.1089 -0.1999 0.1508 401 NAG A C1 3340 C C2 . NAG C . ? 0.8881 1.4225 1.1183 -0.0791 -0.1920 0.1874 401 NAG A C2 3341 C C3 . NAG C . ? 0.9003 1.4944 1.1373 -0.0614 -0.2192 0.2252 401 NAG A C3 3342 C C4 . NAG C . ? 0.9102 1.5876 1.1576 -0.0793 -0.2531 0.2133 401 NAG A C4 3343 C C5 . NAG C . ? 0.9635 1.6299 1.1622 -0.1154 -0.2548 0.1681 401 NAG A C5 3344 C C6 . NAG C . ? 1.0436 1.7847 1.2561 -0.1411 -0.2842 0.1482 401 NAG A C6 3345 C C7 . NAG C . ? 0.9547 1.3663 1.1742 -0.0737 -0.1402 0.1778 401 NAG A C7 3346 C C8 . NAG C . ? 0.9714 1.3174 1.1642 -0.0701 -0.1176 0.1851 401 NAG A C8 3347 N N2 . NAG C . ? 0.9381 1.4011 1.1460 -0.0701 -0.1657 0.1953 401 NAG A N2 3348 O O3 . NAG C . ? 0.9091 1.5009 1.1994 -0.0306 -0.2090 0.2569 401 NAG A O3 3349 O O4 . NAG C . ? 0.8679 1.6002 1.0991 -0.0673 -0.2829 0.2474 401 NAG A O4 3350 O O5 . NAG C . ? 0.9053 1.5105 1.1107 -0.1239 -0.2251 0.1398 401 NAG A O5 3351 O O6 . NAG C . ? 1.1577 1.8707 1.3199 -0.1739 -0.2785 0.1039 401 NAG A O6 3352 O O7 . NAG C . ? 1.0011 1.4188 1.2495 -0.0823 -0.1350 0.1565 401 NAG A O7 3353 C C1 . NAG D . ? 0.7826 1.5987 1.0778 -0.0608 -0.3077 0.2603 402 NAG A C1 3354 C C2 . NAG D . ? 0.7814 1.6770 1.0519 -0.0598 -0.3505 0.2869 402 NAG A C2 3355 C C3 . NAG D . ? 0.7203 1.7164 1.0703 -0.0505 -0.3789 0.3046 402 NAG A C3 3356 C C4 . NAG D . ? 0.6285 1.6093 1.0580 -0.0089 -0.3542 0.3353 402 NAG A C4 3357 C C5 . NAG D . ? 0.6348 1.5225 1.0710 -0.0154 -0.3073 0.3027 402 NAG A C5 3358 C C6 . NAG D . ? 0.6055 1.4634 1.1077 0.0244 -0.2763 0.3293 402 NAG A C6 3359 C C7 . NAG D . ? 0.8817 1.8354 1.0524 -0.1319 -0.3917 0.2245 402 NAG A C7 3360 C C8 . NAG D . ? 0.8842 1.9446 1.1128 -0.1423 -0.4289 0.2281 402 NAG A C8 3361 N N2 . NAG D . ? 0.8096 1.7020 1.0034 -0.0977 -0.3616 0.2510 402 NAG A N2 3362 O O3 . NAG D . ? 0.7926 1.8696 1.1217 -0.0459 -0.4226 0.3361 402 NAG A O3 3363 O O4 . NAG D . ? 0.5148 1.5920 1.0270 -0.0065 -0.3748 0.3407 402 NAG A O4 3364 O O5 . NAG D . ? 0.7357 1.5388 1.0945 -0.0254 -0.2891 0.2900 402 NAG A O5 3365 O O6 . NAG D . ? 0.5727 1.4272 1.0758 0.0659 -0.2798 0.3827 402 NAG A O6 3366 O O7 . NAG D . ? 0.9190 1.8411 1.0166 -0.1581 -0.3875 0.1940 402 NAG A O7 3367 C C1 . BMA E . ? 0.5184 1.6793 1.0583 0.0257 -0.4098 0.3942 403 BMA A C1 3368 C C2 . BMA E . ? 0.4858 1.7005 1.1393 0.0583 -0.4009 0.4168 403 BMA A C2 3369 C C3 . BMA E . ? 0.5060 1.8450 1.2166 0.0894 -0.4450 0.4699 403 BMA A C3 3370 C C4 . BMA E . ? 0.5509 1.9771 1.2076 0.0543 -0.5023 0.4654 403 BMA A C4 3371 C C5 . BMA E . ? 0.6056 1.9460 1.1387 0.0248 -0.4978 0.4406 403 BMA A C5 3372 C C6 . BMA E . ? 0.6859 2.1087 1.1604 -0.0158 -0.5499 0.4272 403 BMA A C6 3373 O O2 . BMA E . ? 0.4452 1.6785 1.1414 0.0229 -0.3895 0.3690 403 BMA A O2 3374 O O3 . BMA E . ? 0.4575 1.8713 1.2823 0.1030 -0.4401 0.4733 403 BMA A O3 3375 O O4 . BMA E . ? 0.4891 2.0028 1.1688 0.0929 -0.5417 0.5280 403 BMA A O4 3376 O O5 . BMA E . ? 0.5147 1.7645 1.0242 -0.0063 -0.4582 0.3852 403 BMA A O5 3377 O O6 . BMA E . ? 0.7660 2.1057 1.1360 -0.0510 -0.5354 0.3875 403 BMA A O6 3378 C C1 . MAN F . ? 0.4641 1.8192 1.3435 0.1582 -0.3955 0.5054 405 MAN A C1 3379 C C2 . MAN F . ? 0.4676 1.9376 1.4751 0.1907 -0.4032 0.5344 405 MAN A C2 3380 C C3 . MAN F . ? 0.4142 1.9153 1.4855 0.1547 -0.3839 0.4851 405 MAN A C3 3381 C C4 . MAN F . ? 0.4030 1.7592 1.4393 0.1489 -0.3215 0.4496 405 MAN A C4 3382 C C5 . MAN F . ? 0.4033 1.6526 1.3141 0.1183 -0.3199 0.4234 405 MAN A C5 3383 C C6 . MAN F . ? 0.3571 1.4699 1.2353 0.1164 -0.2619 0.3948 405 MAN A C6 3384 O O2 . MAN F . ? 0.5063 1.9197 1.5543 0.2539 -0.3647 0.5776 405 MAN A O2 3385 O O3 . MAN F . ? 0.4127 2.0217 1.6100 0.1895 -0.3855 0.5157 405 MAN A O3 3386 O O4 . MAN F . ? 0.3654 1.7429 1.4494 0.1132 -0.3022 0.4050 405 MAN A O4 3387 O O5 . MAN F . ? 0.4499 1.6839 1.3087 0.1474 -0.3404 0.4674 405 MAN A O5 3388 O O6 . MAN F . ? 0.3942 1.4162 1.1667 0.0954 -0.2601 0.3782 405 MAN A O6 3389 C C1 . FUC G . ? 1.2672 2.0243 1.3777 -0.1972 -0.3058 0.0916 406 FUC A C1 3390 C C2 . FUC G . ? 1.2953 2.0678 1.4189 -0.2345 -0.3089 0.0477 406 FUC A C2 3391 C C3 . FUC G . ? 1.2969 1.9813 1.3927 -0.2453 -0.2726 0.0117 406 FUC A C3 3392 C C4 . FUC G . ? 1.3067 1.9502 1.3243 -0.2449 -0.2637 0.0035 406 FUC A C4 3393 C C5 . FUC G . ? 1.2788 1.9206 1.2894 -0.2115 -0.2638 0.0474 406 FUC A C5 3394 C C6 . FUC G . ? 1.2947 1.9089 1.2305 -0.2134 -0.2548 0.0412 406 FUC A C6 3395 O O2 . FUC G . ? 1.2457 2.0593 1.4517 -0.2262 -0.3127 0.0615 406 FUC A O2 3396 O O3 . FUC G . ? 1.3233 2.0084 1.4275 -0.2806 -0.2703 -0.0284 406 FUC A O3 3397 O O4 . FUC G . ? 1.3473 2.0302 1.3161 -0.2730 -0.2865 -0.0166 406 FUC A O4 3398 O O5 . FUC G . ? 1.2851 1.9977 1.3203 -0.2004 -0.2948 0.0828 406 FUC A O5 3399 C C1 . NAG H . ? 0.8430 2.1267 1.5312 0.3207 0.4908 0.1305 501 NAG A C1 3400 C C2 . NAG H . ? 0.8182 2.2555 1.6229 0.3140 0.4822 0.1643 501 NAG A C2 3401 C C3 . NAG H . ? 0.8430 2.3478 1.6914 0.3374 0.5497 0.1609 501 NAG A C3 3402 C C4 . NAG H . ? 0.8788 2.3198 1.6295 0.2964 0.5823 0.1333 501 NAG A C4 3403 C C5 . NAG H . ? 0.9232 2.2103 1.5534 0.2996 0.5777 0.1006 501 NAG A C5 3404 C C6 . NAG H . ? 0.9698 2.1953 1.4955 0.2599 0.6056 0.0744 501 NAG A C6 3405 C C7 . NAG H . ? 0.7978 2.3223 1.7150 0.3410 0.3949 0.2136 501 NAG A C7 3406 C C8 . NAG H . ? 0.7933 2.3954 1.8055 0.3984 0.3816 0.2451 501 NAG A C8 3407 N N2 . NAG H . ? 0.8350 2.3393 1.7308 0.3581 0.4575 0.1929 501 NAG A N2 3408 O O3 . NAG H . ? 0.8022 2.4575 1.7641 0.3258 0.5405 0.1920 501 NAG A O3 3409 O O4 . NAG H . ? 0.8988 2.3922 1.6812 0.3220 0.6518 0.1270 501 NAG A O4 3410 O O5 . NAG H . ? 0.8611 2.1020 1.4685 0.2775 0.5122 0.1082 501 NAG A O5 3411 O O6 . NAG H . ? 1.0179 2.2876 1.5621 0.2819 0.6746 0.0661 501 NAG A O6 3412 O O7 . NAG H . ? 0.7187 2.2013 1.5821 0.2860 0.3514 0.2093 501 NAG A O7 3413 C C1 . NAG I . ? 0.5216 1.8351 0.9805 -0.5226 -0.1042 0.5274 301 NAG B C1 3414 C C2 . NAG I . ? 0.4778 1.8549 0.9480 -0.5537 -0.1022 0.5627 301 NAG B C2 3415 C C3 . NAG I . ? 0.5642 1.8724 1.0148 -0.5997 -0.1282 0.5852 301 NAG B C3 3416 C C4 . NAG I . ? 0.6318 1.8838 1.0779 -0.6235 -0.1547 0.5821 301 NAG B C4 3417 C C5 . NAG I . ? 0.6352 1.8292 1.0659 -0.5848 -0.1499 0.5417 301 NAG B C5 3418 C C6 . NAG I . ? 0.6831 1.8192 1.1022 -0.6071 -0.1753 0.5345 301 NAG B C6 3419 C C7 . NAG I . ? 0.4636 1.9393 0.9435 -0.4902 -0.0534 0.5401 301 NAG B C7 3420 C C8 . NAG I . ? 0.3410 1.8305 0.8049 -0.4661 -0.0318 0.5296 301 NAG B C8 3421 N N2 . NAG I . ? 0.4409 1.8416 0.9029 -0.5260 -0.0784 0.5544 301 NAG B N2 3422 O O3 . NAG I . ? 0.6527 2.0298 1.1185 -0.6371 -0.1308 0.6250 301 NAG B O3 3423 O O4 . NAG I . ? 0.7134 1.8837 1.1374 -0.6589 -0.1785 0.5950 301 NAG B O4 3424 O O5 . NAG I . ? 0.5654 1.8356 1.0200 -0.5503 -0.1294 0.5310 301 NAG B O5 3425 O O6 . NAG I . ? 0.7110 1.9068 1.1541 -0.6470 -0.1917 0.5640 301 NAG B O6 3426 O O7 . NAG I . ? 0.4518 1.9834 0.9603 -0.4761 -0.0488 0.5347 301 NAG B O7 3427 C C1 . NAG J . ? 0.8128 2.0255 1.2541 -0.7111 -0.1976 0.6341 302 NAG B C1 3428 C C2 . NAG J . ? 0.9053 2.0093 1.3225 -0.7438 -0.2303 0.6325 302 NAG B C2 3429 C C3 . NAG J . ? 0.9782 2.0990 1.4065 -0.8052 -0.2562 0.6756 302 NAG B C3 3430 C C4 . NAG J . ? 1.0054 2.1963 1.4472 -0.8201 -0.2450 0.7130 302 NAG B C4 3431 C C5 . NAG J . ? 0.9470 2.2554 1.4136 -0.7834 -0.2098 0.7076 302 NAG B C5 3432 C C6 . NAG J . ? 0.9538 2.3492 1.4327 -0.7995 -0.1958 0.7437 302 NAG B C6 3433 C C7 . NAG J . ? 0.9714 2.0615 1.3904 -0.7514 -0.2525 0.6042 302 NAG B C7 3434 C C8 . NAG J . ? 0.9531 2.1148 1.4001 -0.8026 -0.2703 0.6447 302 NAG B C8 3435 N N2 . NAG J . ? 0.9392 2.0073 1.3478 -0.7278 -0.2356 0.6003 302 NAG B N2 3436 O O3 . NAG J . ? 1.0177 2.0209 1.4189 -0.8307 -0.2858 0.6712 302 NAG B O3 3437 O O4 . NAG J . ? 1.0599 2.2861 1.5178 -0.8793 -0.2677 0.7560 302 NAG B O4 3438 O O5 . NAG J . ? 0.8418 2.1073 1.2908 -0.7283 -0.1902 0.6663 302 NAG B O5 3439 O O6 . NAG J . ? 0.9783 2.3012 1.4286 -0.8018 -0.2010 0.7499 302 NAG B O6 3440 O O7 . NAG J . ? 0.9709 2.0237 1.3757 -0.7314 -0.2540 0.5741 302 NAG B O7 # 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 ARG 1 -1 ? ? ? A . n A 1 2 SER 2 0 ? ? ? A . n A 1 3 GLN 3 1 ? ? ? A . n A 1 4 GLY 4 2 ? ? ? A . n A 1 5 LEU 5 3 ? ? ? A . n A 1 6 PRO 6 4 ? ? ? A . n A 1 7 GLY 7 5 ? ? ? A . n A 1 8 LEU 8 6 ? ? ? A . n A 1 9 THR 9 7 ? ? ? A . n A 1 10 VAL 10 8 ? ? ? A . n A 1 11 SER 11 9 ? ? ? A . n A 1 12 SER 12 10 ? ? ? A . n A 1 13 PRO 13 11 11 PRO PRO A . n A 1 14 GLN 14 12 12 GLN GLN A . n A 1 15 LEU 15 13 13 LEU LEU A . n A 1 16 ARG 16 14 14 ARG ARG A . n A 1 17 VAL 17 15 15 VAL VAL A . n A 1 18 HIS 18 16 16 HIS HIS A . n A 1 19 VAL 19 17 17 VAL VAL A . n A 1 20 GLY 20 18 18 GLY GLY A . n A 1 21 GLU 21 19 19 GLU GLU A . n A 1 22 SER 22 20 20 SER SER A . n A 1 23 VAL 23 21 21 VAL VAL A . n A 1 24 LEU 24 22 22 LEU LEU A . n A 1 25 MET 25 23 23 MET MET A . n A 1 26 GLY 26 24 24 GLY GLY A . n A 1 27 CYS 27 25 25 CYS CYS A . n A 1 28 VAL 28 26 26 VAL VAL A . n A 1 29 VAL 29 27 27 VAL VAL A . n A 1 30 GLN 30 28 28 GLN GLN A . n A 1 31 ARG 31 29 29 ARG ARG A . n A 1 32 THR 32 30 30 THR THR A . n A 1 33 GLU 33 31 31 GLU GLU A . n A 1 34 GLU 34 32 32 GLU GLU A . n A 1 35 LYS 35 33 33 LYS LYS A . n A 1 36 HIS 36 34 34 HIS HIS A . n A 1 37 VAL 37 35 35 VAL VAL A . n A 1 38 ASP 38 36 36 ASP ASP A . n A 1 39 ARG 39 37 37 ARG ARG A . n A 1 40 VAL 40 38 38 VAL VAL A . n A 1 41 ASP 41 39 39 ASP ASP A . n A 1 42 TRP 42 40 40 TRP TRP A . n A 1 43 LEU 43 41 41 LEU LEU A . n A 1 44 PHE 44 42 42 PHE PHE A . n A 1 45 SER 45 43 43 SER SER A . n A 1 46 LYS 46 44 44 LYS LYS A . n A 1 47 ASP 47 45 45 ASP ASP A . n A 1 48 LYS 48 46 46 LYS LYS A . n A 1 49 ASP 49 47 47 ASP ASP A . n A 1 50 ASP 50 48 48 ASP ASP A . n A 1 51 ALA 51 49 49 ALA ALA A . n A 1 52 SER 52 50 50 SER SER A . n A 1 53 GLU 53 51 51 GLU GLU A . n A 1 54 TYR 54 52 52 TYR TYR A . n A 1 55 VAL 55 53 53 VAL VAL A . n A 1 56 LEU 56 54 54 LEU LEU A . n A 1 57 PHE 57 55 55 PHE PHE A . n A 1 58 TYR 58 56 56 TYR TYR A . n A 1 59 TYR 59 57 57 TYR TYR A . n A 1 60 SER 60 58 58 SER SER A . n A 1 61 ASN 61 59 59 ASN ASN A . n A 1 62 LEU 62 60 60 LEU LEU A . n A 1 63 SER 63 61 61 SER SER A . n A 1 64 VAL 64 62 62 VAL VAL A . n A 1 65 PRO 65 63 63 PRO PRO A . n A 1 66 THR 66 64 64 THR THR A . n A 1 67 GLY 67 65 65 GLY GLY A . n A 1 68 ARG 68 66 66 ARG ARG A . n A 1 69 PHE 69 67 67 PHE PHE A . n A 1 70 GLN 70 68 68 GLN GLN A . n A 1 71 ASN 71 69 69 ASN ASN A . n A 1 72 ARG 72 70 70 ARG ARG A . n A 1 73 SER 73 71 71 SER SER A . n A 1 74 HIS 74 72 72 HIS HIS A . n A 1 75 LEU 75 73 73 LEU LEU A . n A 1 76 VAL 76 74 74 VAL VAL A . n A 1 77 GLY 77 75 75 GLY GLY A . n A 1 78 ASP 78 76 76 ASP ASP A . n A 1 79 THR 79 77 77 THR THR A . n A 1 80 PHE 80 78 78 PHE PHE A . n A 1 81 HIS 81 79 79 HIS HIS A . n A 1 82 ASN 82 80 80 ASN ASN A . n A 1 83 ASP 83 81 81 ASP ASP A . n A 1 84 GLY 84 82 82 GLY GLY A . n A 1 85 SER 85 83 83 SER SER A . n A 1 86 LEU 86 84 84 LEU LEU A . n A 1 87 LEU 87 85 85 LEU LEU A . n A 1 88 LEU 88 86 86 LEU LEU A . n A 1 89 GLN 89 87 87 GLN GLN A . n A 1 90 ASP 90 88 88 ASP ASP A . n A 1 91 VAL 91 89 89 VAL VAL A . n A 1 92 GLN 92 90 90 GLN GLN A . n A 1 93 LYS 93 91 91 LYS LYS A . n A 1 94 ALA 94 92 92 ALA ALA A . n A 1 95 ASP 95 93 93 ASP ASP A . n A 1 96 GLU 96 94 94 GLU GLU A . n A 1 97 GLY 97 95 95 GLY GLY A . n A 1 98 ILE 98 96 96 ILE ILE A . n A 1 99 TYR 99 97 97 TYR TYR A . n A 1 100 THR 100 98 98 THR THR A . n A 1 101 CYS 101 99 99 CYS CYS A . n A 1 102 GLU 102 100 100 GLU GLU A . n A 1 103 ILE 103 101 101 ILE ILE A . n A 1 104 ARG 104 102 102 ARG ARG A . n A 1 105 LEU 105 103 103 LEU LEU A . n A 1 106 LYS 106 104 104 LYS LYS A . n A 1 107 ASN 107 105 105 ASN ASN A . n A 1 108 GLU 108 106 106 GLU GLU A . n A 1 109 SER 109 107 107 SER SER A . n A 1 110 MET 110 108 108 MET MET A . n A 1 111 VAL 111 109 109 VAL VAL A . n A 1 112 MET 112 110 110 MET MET A . n A 1 113 LYS 113 111 111 LYS LYS A . n A 1 114 LYS 114 112 112 LYS LYS A . n A 1 115 PRO 115 113 113 PRO PRO A . n A 1 116 VAL 116 114 114 VAL VAL A . n A 1 117 GLU 117 115 115 GLU GLU A . n A 1 118 LEU 118 116 116 LEU LEU A . n A 1 119 TRP 119 117 117 TRP TRP A . n A 1 120 VAL 120 118 118 VAL VAL A . n A 1 121 LEU 121 119 119 LEU LEU A . n A 1 122 PRO 122 120 120 PRO PRO A . n A 1 123 GLU 123 121 121 GLU GLU A . n A 1 124 GLU 124 122 122 GLU GLU A . n A 1 125 PRO 125 123 123 PRO PRO A . n A 1 126 ARG 126 124 124 ARG ARG A . n A 1 127 ASP 127 125 125 ASP ASP A . n A 1 128 LEU 128 126 126 LEU LEU A . n A 1 129 ARG 129 127 127 ARG ARG A . n A 1 130 VAL 130 128 128 VAL VAL A . n A 1 131 ARG 131 129 129 ARG ARG A . n A 1 132 VAL 132 130 130 VAL VAL A . n A 1 133 GLY 133 131 131 GLY GLY A . n A 1 134 ASP 134 132 132 ASP ASP A . n A 1 135 THR 135 133 133 THR THR A . n A 1 136 THR 136 134 134 THR THR A . n A 1 137 GLN 137 135 135 GLN GLN A . n A 1 138 MET 138 136 136 MET MET A . n A 1 139 ARG 139 137 137 ARG ARG A . n A 1 140 CYS 140 138 138 CYS CYS A . n A 1 141 SER 141 139 139 SER SER A . n A 1 142 ILE 142 140 140 ILE ILE A . n A 1 143 GLN 143 141 141 GLN GLN A . n A 1 144 SER 144 142 142 SER SER A . n A 1 145 THR 145 143 143 THR THR A . n A 1 146 GLU 146 144 144 GLU GLU A . n A 1 147 GLU 147 145 145 GLU GLU A . n A 1 148 LYS 148 146 146 LYS LYS A . n A 1 149 ARG 149 147 147 ARG ARG A . n A 1 150 VAL 150 148 148 VAL VAL A . n A 1 151 THR 151 149 149 THR THR A . n A 1 152 LYS 152 150 150 LYS LYS A . n A 1 153 VAL 153 151 151 VAL VAL A . n A 1 154 ASN 154 152 152 ASN ASN A . n A 1 155 TRP 155 153 153 TRP TRP A . n A 1 156 MET 156 154 154 MET MET A . n A 1 157 PHE 157 155 155 PHE PHE A . n A 1 158 SER 158 156 156 SER SER A . n A 1 159 SER 159 157 157 SER SER A . n A 1 160 GLY 160 158 158 GLY GLY A . n A 1 161 SER 161 159 159 SER SER A . n A 1 162 HIS 162 160 160 HIS HIS A . n A 1 163 THR 163 161 161 THR THR A . n A 1 164 GLU 164 162 162 GLU GLU A . n A 1 165 GLU 165 163 163 GLU GLU A . n A 1 166 GLU 166 164 164 GLU GLU A . n A 1 167 THR 167 165 165 THR THR A . n A 1 168 VAL 168 166 166 VAL VAL A . n A 1 169 LEU 169 167 167 LEU LEU A . n A 1 170 SER 170 168 168 SER SER A . n A 1 171 TYR 171 169 169 TYR TYR A . n A 1 172 ASP 172 170 170 ASP ASP A . n A 1 173 SER 173 171 171 SER SER A . n A 1 174 ASN 174 172 172 ASN ASN A . n A 1 175 MET 175 173 173 MET MET A . n A 1 176 ARG 176 174 174 ARG ARG A . n A 1 177 SER 177 175 175 SER SER A . n A 1 178 GLY 178 176 176 GLY GLY A . n A 1 179 LYS 179 177 177 LYS LYS A . n A 1 180 PHE 180 178 178 PHE PHE A . n A 1 181 GLN 181 179 179 GLN GLN A . n A 1 182 SER 182 180 180 SER SER A . n A 1 183 LEU 183 181 181 LEU LEU A . n A 1 184 GLY 184 182 182 GLY GLY A . n A 1 185 ARG 185 183 183 ARG ARG A . n A 1 186 PHE 186 184 184 PHE PHE A . n A 1 187 ARG 187 185 185 ARG ARG A . n A 1 188 ASN 188 186 186 ASN ASN A . n A 1 189 ARG 189 187 187 ARG ARG A . n A 1 190 VAL 190 188 188 VAL VAL A . n A 1 191 ASP 191 189 189 ASP ASP A . n A 1 192 LEU 192 190 190 LEU LEU A . n A 1 193 THR 193 191 191 THR THR A . n A 1 194 GLY 194 192 192 GLY GLY A . n A 1 195 ASP 195 193 193 ASP ASP A . n A 1 196 ILE 196 194 194 ILE ILE A . n A 1 197 SER 197 195 195 SER SER A . n A 1 198 ARG 198 196 196 ARG ARG A . n A 1 199 ASN 199 197 197 ASN ASN A . n A 1 200 ASP 200 198 198 ASP ASP A . n A 1 201 GLY 201 199 199 GLY GLY A . n A 1 202 SER 202 200 200 SER SER A . n A 1 203 ILE 203 201 201 ILE ILE A . n A 1 204 LYS 204 202 202 LYS LYS A . n A 1 205 LEU 205 203 203 LEU LEU A . n A 1 206 GLN 206 204 204 GLN GLN A . n A 1 207 THR 207 205 205 THR THR A . n A 1 208 VAL 208 206 206 VAL VAL A . n A 1 209 LYS 209 207 207 LYS LYS A . n A 1 210 GLU 210 208 208 GLU GLU A . n A 1 211 SER 211 209 209 SER SER A . n A 1 212 ASP 212 210 210 ASP ASP A . n A 1 213 GLN 213 211 211 GLN GLN A . n A 1 214 GLY 214 212 212 GLY GLY A . n A 1 215 ILE 215 213 213 ILE ILE A . n A 1 216 TYR 216 214 214 TYR TYR A . n A 1 217 THR 217 215 215 THR THR A . n A 1 218 CYS 218 216 216 CYS CYS A . n A 1 219 SER 219 217 217 SER SER A . n A 1 220 ILE 220 218 218 ILE ILE A . n A 1 221 TYR 221 219 219 TYR TYR A . n A 1 222 VAL 222 220 220 VAL VAL A . n A 1 223 GLY 223 221 221 GLY GLY A . n A 1 224 LYS 224 222 222 LYS LYS A . n A 1 225 LEU 225 223 223 LEU LEU A . n A 1 226 GLU 226 224 224 GLU GLU A . n A 1 227 SER 227 225 225 SER SER A . n A 1 228 ARG 228 226 226 ARG ARG A . n A 1 229 LYS 229 227 227 LYS LYS A . n A 1 230 THR 230 228 228 THR THR A . n A 1 231 ILE 231 229 229 ILE ILE A . n A 1 232 VAL 232 230 230 VAL VAL A . n A 1 233 LEU 233 231 231 LEU LEU A . n A 1 234 HIS 234 232 232 HIS HIS A . n A 1 235 VAL 235 233 233 VAL VAL A . n A 1 236 VAL 236 234 234 VAL VAL A . n A 1 237 GLN 237 235 235 GLN GLN A . n A 1 238 ASP 238 236 236 ASP ASP A . n A 1 239 GLU 239 237 237 GLU GLU A . n A 1 240 PHE 240 238 238 PHE PHE A . n A 1 241 GLN 241 239 239 GLN GLN A . n A 1 242 ARG 242 240 ? ? ? A . n A 1 243 THR 243 241 ? ? ? A . n A 1 244 ILE 244 242 ? ? ? A . n A 1 245 SER 245 243 ? ? ? A . n A 1 246 PRO 246 244 ? ? ? A . n A 1 247 THR 247 245 ? ? ? A . n A 1 248 PRO 248 246 ? ? ? A . n A 1 249 PRO 249 247 ? ? ? A . n A 1 250 THR 250 248 ? ? ? A . n A 1 251 ASP 251 249 ? ? ? A . n A 1 252 LYS 252 250 ? ? ? A . n A 1 253 GLY 253 251 ? ? ? A . n A 1 254 GLN 254 252 ? ? ? A . n A 1 255 GLN 255 253 ? ? ? A . n A 1 256 GLY 256 254 ? ? ? A . n A 1 257 ILE 257 255 ? ? ? A . n A 1 258 LEU 258 256 ? ? ? A . n A 1 259 ASN 259 257 ? ? ? A . n A 1 260 GLY 260 258 ? ? ? A . n A 1 261 ASN 261 259 ? ? ? A . n A 1 262 GLN 262 260 ? ? ? A . n A 1 263 HIS 263 261 ? ? ? A . n A 1 264 HIS 264 262 ? ? ? A . n A 1 265 HIS 265 263 ? ? ? A . n A 1 266 HIS 266 264 ? ? ? A . n A 1 267 HIS 267 265 ? ? ? A . n A 1 268 HIS 268 266 ? ? ? A . n B 2 1 SER 1 -1 ? ? ? B . n B 2 2 GLY 2 0 ? ? ? B . n B 2 3 LEU 3 1 ? ? ? B . n B 2 4 SER 4 2 ? ? ? B . n B 2 5 ILE 5 3 3 ILE ILE B . n B 2 6 THR 6 4 4 THR THR B . n B 2 7 THR 7 5 5 THR THR B . n B 2 8 PRO 8 6 6 PRO PRO B . n B 2 9 GLU 9 7 7 GLU GLU B . n B 2 10 GLN 10 8 8 GLN GLN B . n B 2 11 ARG 11 9 9 ARG ARG B . n B 2 12 ILE 12 10 10 ILE ILE B . n B 2 13 GLU 13 11 11 GLU GLU B . n B 2 14 LYS 14 12 12 LYS LYS B . n B 2 15 ALA 15 13 13 ALA ALA B . n B 2 16 LYS 16 14 14 LYS LYS B . n B 2 17 GLY 17 15 15 GLY GLY B . n B 2 18 GLU 18 16 16 GLU GLU B . n B 2 19 THR 19 17 17 THR THR B . n B 2 20 ALA 20 18 18 ALA ALA B . n B 2 21 TYR 21 19 19 TYR TYR B . n B 2 22 LEU 22 20 20 LEU LEU B . n B 2 23 PRO 23 21 21 PRO PRO B . n B 2 24 CYS 24 22 22 CYS CYS B . n B 2 25 LYS 25 23 23 LYS LYS B . n B 2 26 PHE 26 24 24 PHE PHE B . n B 2 27 THR 27 25 25 THR THR B . n B 2 28 LEU 28 26 26 LEU LEU B . n B 2 29 SER 29 27 27 SER SER B . n B 2 30 PRO 30 28 28 PRO PRO B . n B 2 31 GLU 31 29 29 GLU GLU B . n B 2 32 ASP 32 30 30 ASP ASP B . n B 2 33 GLN 33 31 31 GLN GLN B . n B 2 34 GLY 34 32 32 GLY GLY B . n B 2 35 PRO 35 33 33 PRO PRO B . n B 2 36 LEU 36 34 34 LEU LEU B . n B 2 37 ASP 37 35 35 ASP ASP B . n B 2 38 ILE 38 36 36 ILE ILE B . n B 2 39 GLU 39 37 37 GLU GLU B . n B 2 40 TRP 40 38 38 TRP TRP B . n B 2 41 LEU 41 39 39 LEU LEU B . n B 2 42 ILE 42 40 40 ILE ILE B . n B 2 43 SER 43 41 41 SER SER B . n B 2 44 PRO 44 42 42 PRO PRO B . n B 2 45 SER 45 43 43 SER SER B . n B 2 46 ASP 46 44 44 ASP ASP B . n B 2 47 ASN 47 45 45 ASN ASN B . n B 2 48 GLN 48 46 46 GLN GLN B . n B 2 49 ILE 49 47 47 ILE ILE B . n B 2 50 VAL 50 48 48 VAL VAL B . n B 2 51 ASP 51 49 49 ASP ASP B . n B 2 52 GLN 52 50 50 GLN GLN B . n B 2 53 VAL 53 51 51 VAL VAL B . n B 2 54 ILE 54 52 52 ILE ILE B . n B 2 55 ILE 55 53 53 ILE ILE B . n B 2 56 LEU 56 54 54 LEU LEU B . n B 2 57 TYR 57 55 55 TYR TYR B . n B 2 58 SER 58 56 56 SER SER B . n B 2 59 GLY 59 57 57 GLY GLY B . n B 2 60 ASP 60 58 58 ASP ASP B . n B 2 61 LYS 61 59 59 LYS LYS B . n B 2 62 ILE 62 60 60 ILE ILE B . n B 2 63 TYR 63 61 61 TYR TYR B . n B 2 64 ASP 64 62 62 ASP ASP B . n B 2 65 ASN 65 63 63 ASN ASN B . n B 2 66 TYR 66 64 64 TYR TYR B . n B 2 67 TYR 67 65 65 TYR TYR B . n B 2 68 PRO 68 66 66 PRO PRO B . n B 2 69 ASP 69 67 67 ASP ASP B . n B 2 70 LEU 70 68 68 LEU LEU B . n B 2 71 LYS 71 69 69 LYS LYS B . n B 2 72 GLY 72 70 70 GLY GLY B . n B 2 73 ARG 73 71 71 ARG ARG B . n B 2 74 VAL 74 72 72 VAL VAL B . n B 2 75 HIS 75 73 73 HIS HIS B . n B 2 76 PHE 76 74 74 PHE PHE B . n B 2 77 THR 77 75 75 THR THR B . n B 2 78 SER 78 76 76 SER SER B . n B 2 79 ASN 79 77 77 ASN ASN B . n B 2 80 ASP 80 78 78 ASP ASP B . n B 2 81 VAL 81 79 79 VAL VAL B . n B 2 82 LYS 82 80 80 LYS LYS B . n B 2 83 SER 83 81 81 SER SER B . n B 2 84 GLY 84 82 82 GLY GLY B . n B 2 85 ASP 85 83 83 ASP ASP B . n B 2 86 ALA 86 84 84 ALA ALA B . n B 2 87 SER 87 85 85 SER SER B . n B 2 88 ILE 88 86 86 ILE ILE B . n B 2 89 ASN 89 87 87 ASN ASN B . n B 2 90 VAL 90 88 88 VAL VAL B . n B 2 91 THR 91 89 89 THR THR B . n B 2 92 ASN 92 90 90 ASN ASN B . n B 2 93 LEU 93 91 91 LEU LEU B . n B 2 94 GLN 94 92 92 GLN GLN B . n B 2 95 LEU 95 93 93 LEU LEU B . n B 2 96 SER 96 94 94 SER SER B . n B 2 97 ASP 97 95 95 ASP ASP B . n B 2 98 ILE 98 96 96 ILE ILE B . n B 2 99 GLY 99 97 97 GLY GLY B . n B 2 100 THR 100 98 98 THR THR B . n B 2 101 TYR 101 99 99 TYR TYR B . n B 2 102 GLN 102 100 100 GLN GLN B . n B 2 103 CYS 103 101 101 CYS CYS B . n B 2 104 LYS 104 102 102 LYS LYS B . n B 2 105 VAL 105 103 103 VAL VAL B . n B 2 106 LYS 106 104 104 LYS LYS B . n B 2 107 LYS 107 105 105 LYS LYS B . n B 2 108 ALA 108 106 106 ALA ALA B . n B 2 109 PRO 109 107 107 PRO PRO B . n B 2 110 GLY 110 108 108 GLY GLY B . n B 2 111 VAL 111 109 109 VAL VAL B . n B 2 112 ALA 112 110 110 ALA ALA B . n B 2 113 ASN 113 111 111 ASN ASN B . n B 2 114 LYS 114 112 112 LYS LYS B . n B 2 115 LYS 115 113 113 LYS LYS B . n B 2 116 PHE 116 114 114 PHE PHE B . n B 2 117 LEU 117 115 115 LEU LEU B . n B 2 118 LEU 118 116 116 LEU LEU B . n B 2 119 THR 119 117 117 THR THR B . n B 2 120 VAL 120 118 118 VAL VAL B . n B 2 121 LEU 121 119 119 LEU LEU B . n B 2 122 VAL 122 120 120 VAL VAL B . n B 2 123 LYS 123 121 121 LYS LYS B . n B 2 124 PRO 124 122 122 PRO PRO B . n B 2 125 SER 125 123 123 SER SER B . n B 2 126 GLY 126 124 124 GLY GLY B . n B 2 127 THR 127 125 125 THR THR B . n B 2 128 ARG 128 126 126 ARG ARG B . n B 2 129 CYS 129 127 127 CYS CYS B . n B 2 130 PHE 130 128 128 PHE PHE B . n B 2 131 VAL 131 129 129 VAL VAL B . n B 2 132 ASP 132 130 130 ASP ASP B . n B 2 133 GLY 133 131 ? ? ? B . n B 2 134 SER 134 132 ? ? ? B . n B 2 135 GLU 135 133 ? ? ? B . n B 2 136 GLU 136 134 ? ? ? B . n B 2 137 ILE 137 135 ? ? ? B . n B 2 138 GLY 138 136 136 GLY GLY B . n B 2 139 ASN 139 137 137 ASN ASN B . n B 2 140 ASP 140 138 138 ASP ASP B . n B 2 141 PHE 141 139 139 PHE PHE B . n B 2 142 LYS 142 140 140 LYS LYS B . n B 2 143 LEU 143 141 141 LEU LEU B . n B 2 144 LYS 144 142 142 LYS LYS B . n B 2 145 CYS 145 143 143 CYS CYS B . n B 2 146 GLU 146 144 144 GLU GLU B . n B 2 147 PRO 147 145 145 PRO PRO B . n B 2 148 LYS 148 146 146 LYS LYS B . n B 2 149 GLU 149 147 147 GLU GLU B . n B 2 150 GLY 150 148 148 GLY GLY B . n B 2 151 SER 151 149 149 SER SER B . n B 2 152 LEU 152 150 150 LEU LEU B . n B 2 153 PRO 153 151 151 PRO PRO B . n B 2 154 LEU 154 152 152 LEU LEU B . n B 2 155 GLN 155 153 153 GLN GLN B . n B 2 156 PHE 156 154 154 PHE PHE B . n B 2 157 GLU 157 155 155 GLU GLU B . n B 2 158 TRP 158 156 156 TRP TRP B . n B 2 159 GLN 159 157 157 GLN GLN B . n B 2 160 LYS 160 158 158 LYS LYS B . n B 2 161 LEU 161 159 ? ? ? B . n B 2 162 SER 162 160 ? ? ? B . n B 2 163 ASP 163 161 ? ? ? B . n B 2 164 SER 164 162 ? ? ? B . n B 2 165 GLN 165 163 ? ? ? B . n B 2 166 THR 166 164 ? ? ? B . n B 2 167 MET 167 165 165 MET MET B . n B 2 168 PRO 168 166 166 PRO PRO B . n B 2 169 THR 169 167 167 THR THR B . n B 2 170 PRO 170 168 168 PRO PRO B . n B 2 171 TRP 171 169 169 TRP TRP B . n B 2 172 LEU 172 170 170 LEU LEU B . n B 2 173 ALA 173 171 171 ALA ALA B . n B 2 174 GLU 174 172 172 GLU GLU B . n B 2 175 MET 175 173 173 MET MET B . n B 2 176 THR 176 174 174 THR THR B . n B 2 177 SER 177 175 175 SER SER B . n B 2 178 PRO 178 176 176 PRO PRO B . n B 2 179 VAL 179 177 177 VAL VAL B . n B 2 180 ILE 180 178 178 ILE ILE B . n B 2 181 SER 181 179 179 SER SER B . n B 2 182 VAL 182 180 180 VAL VAL B . n B 2 183 LYS 183 181 181 LYS LYS B . n B 2 184 ASN 184 182 182 ASN ASN B . n B 2 185 ALA 185 183 ? ? ? B . n B 2 186 SER 186 184 ? ? ? B . n B 2 187 SER 187 185 ? ? ? B . n B 2 188 GLU 188 186 ? ? ? B . n B 2 189 TYR 189 187 ? ? ? B . n B 2 190 SER 190 188 ? ? ? B . n B 2 191 GLY 191 189 ? ? ? B . n B 2 192 THR 192 190 ? ? ? B . n B 2 193 TYR 193 191 191 TYR TYR B . n B 2 194 SER 194 192 192 SER SER B . n B 2 195 CYS 195 193 193 CYS CYS B . n B 2 196 THR 196 194 194 THR THR B . n B 2 197 VAL 197 195 195 VAL VAL B . n B 2 198 GLN 198 196 196 GLN GLN B . n B 2 199 ASN 199 197 197 ASN ASN B . n B 2 200 ARG 200 198 198 ARG ARG B . n B 2 201 VAL 201 199 199 VAL VAL B . n B 2 202 GLY 202 200 200 GLY GLY B . n B 2 203 SER 203 201 201 SER SER B . n B 2 204 ASP 204 202 202 ASP ASP B . n B 2 205 GLN 205 203 203 GLN GLN B . n B 2 206 CYS 206 204 204 CYS CYS B . n B 2 207 MET 207 205 205 MET MET B . n B 2 208 LEU 208 206 206 LEU LEU B . n B 2 209 ARG 209 207 207 ARG ARG B . n B 2 210 LEU 210 208 208 LEU LEU B . n B 2 211 ASP 211 209 209 ASP ASP B . n B 2 212 VAL 212 210 210 VAL VAL B . n B 2 213 VAL 213 211 ? ? ? B . n B 2 214 PRO 214 212 ? ? ? B . n B 2 215 PRO 215 213 ? ? ? B . n B 2 216 SER 216 214 ? ? ? B . n B 2 217 ASN 217 215 ? ? ? B . n B 2 218 ARG 218 216 ? ? ? B . n B 2 219 ALA 219 217 ? ? ? B . n B 2 220 HIS 220 218 ? ? ? B . n B 2 221 HIS 221 219 ? ? ? B . n B 2 222 HIS 222 220 ? ? ? B . n B 2 223 HIS 223 221 ? ? ? B . n B 2 224 HIS 224 222 ? ? ? B . n B 2 225 HIS 225 223 ? ? ? B . n # 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 71 A ASN 69 ? ASN 'GLYCOSYLATION SITE' 2 B ASN 89 B ASN 87 ? ASN 'GLYCOSYLATION SITE' 3 A ASN 107 A ASN 105 ? 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 dimeric _pdbx_struct_assembly.oligomeric_count 2 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I,J # 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)' 3150 ? 1 MORE 17 ? 1 'SSA (A^2)' 24580 ? # _pdbx_struct_oper_list.id 1 _pdbx_struct_oper_list.type 'identity operation' _pdbx_struct_oper_list.name 1_555 _pdbx_struct_oper_list.symmetry_operation x,y,z _pdbx_struct_oper_list.matrix[1][1] 1.0000000000 _pdbx_struct_oper_list.matrix[1][2] 0.0000000000 _pdbx_struct_oper_list.matrix[1][3] 0.0000000000 _pdbx_struct_oper_list.vector[1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][2] 1.0000000000 _pdbx_struct_oper_list.matrix[2][3] 0.0000000000 _pdbx_struct_oper_list.vector[2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][1] 0.0000000000 _pdbx_struct_oper_list.matrix[3][2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][3] 1.0000000000 _pdbx_struct_oper_list.vector[3] 0.0000000000 # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 2010-09-22 2 'Structure model' 1 1 2011-07-13 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # _pdbx_audit_revision_group.ordinal 1 _pdbx_audit_revision_group.revision_ordinal 2 _pdbx_audit_revision_group.data_content_type 'Structure model' _pdbx_audit_revision_group.group 'Version format compliance' # 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 15.4786 -23.3421 -3.5617 -0.3588 -0.1463 -0.3376 -0.1023 -0.0560 0.0585 4.4564 4.8715 6.1221 0.9923 -2.2903 -0.6554 0.0547 -0.3424 0.2055 -0.0650 0.1763 0.2132 -0.3231 -0.7405 -0.2310 'X-RAY DIFFRACTION' 2 ? refined 36.9490 -5.0550 -10.6205 0.1437 -0.2791 -0.2486 -0.2865 -0.1061 -0.0062 6.6756 3.3248 5.6604 2.4503 -2.6630 -1.2769 0.4787 -0.6063 0.4532 0.3139 -0.3405 -0.1205 -1.0413 0.4492 -0.1382 'X-RAY DIFFRACTION' 3 ? refined -2.0593 -37.8049 2.9744 -0.4082 0.5348 -0.0574 -0.2309 -0.0351 0.2841 4.2735 2.4418 4.0191 0.9609 1.3823 -0.5280 -0.0286 -0.4694 -0.0179 -0.2213 0.3641 0.5213 0.2309 -1.2365 -0.3355 'X-RAY DIFFRACTION' 4 ? refined -29.4149 -52.2047 -24.7645 0.1038 0.2935 0.4264 0.1346 -0.0775 -0.1252 7.9554 1.6137 11.1319 1.6962 4.8985 -1.9125 0.0291 -0.2623 -0.0977 -0.3065 -0.7984 0.3141 -0.4603 -0.2748 0.7693 # 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 11 ? ? A 121 ? ? ? ? 'X-RAY DIFFRACTION' 2 1 A 401 ? ? A 501 ? ? ? ? 'X-RAY DIFFRACTION' 3 2 A 122 ? ? A 239 ? ? ? ? 'X-RAY DIFFRACTION' 4 3 B 3 ? ? B 120 ? ? ? ? 'X-RAY DIFFRACTION' 5 3 B 301 ? ? B 302 ? ? ? ? 'X-RAY DIFFRACTION' 6 4 B 121 ? ? B 210 ? ? ? ? # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal PHASER phasing . ? 1 REFMAC refinement 5.4.0069 ? 2 HKL-2000 'data scaling' . ? 3 # 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 CYS A 25 ? ? -154.40 84.52 2 1 HIS A 79 ? ? -107.54 54.21 3 1 SER A 156 ? ? 177.42 138.27 4 1 GLU A 162 ? ? -66.58 -178.86 5 1 ARG A 174 ? ? -69.55 -93.09 6 1 SER A 180 ? ? -28.85 -60.24 7 1 PRO B 6 ? ? -69.27 -172.23 8 1 GLU B 16 ? ? -117.48 -163.74 9 1 SER B 43 ? ? 47.38 17.51 10 1 TYR B 65 ? ? 57.30 73.59 11 1 LYS B 69 ? ? -54.26 108.58 12 1 SER B 81 ? ? -57.69 -4.37 13 1 LYS B 146 ? ? -173.48 127.20 14 1 MET B 173 ? ? -38.43 -28.75 15 1 SER B 179 ? ? -68.28 91.54 16 1 ASN B 197 ? ? -124.05 -158.30 17 1 ASP B 202 ? ? -172.81 148.45 # 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 ARG -1 ? A ARG 1 2 1 Y 1 A SER 0 ? A SER 2 3 1 Y 1 A GLN 1 ? A GLN 3 4 1 Y 1 A GLY 2 ? A GLY 4 5 1 Y 1 A LEU 3 ? A LEU 5 6 1 Y 1 A PRO 4 ? A PRO 6 7 1 Y 1 A GLY 5 ? A GLY 7 8 1 Y 1 A LEU 6 ? A LEU 8 9 1 Y 1 A THR 7 ? A THR 9 10 1 Y 1 A VAL 8 ? A VAL 10 11 1 Y 1 A SER 9 ? A SER 11 12 1 Y 1 A SER 10 ? A SER 12 13 1 Y 1 A ARG 240 ? A ARG 242 14 1 Y 1 A THR 241 ? A THR 243 15 1 Y 1 A ILE 242 ? A ILE 244 16 1 Y 1 A SER 243 ? A SER 245 17 1 Y 1 A PRO 244 ? A PRO 246 18 1 Y 1 A THR 245 ? A THR 247 19 1 Y 1 A PRO 246 ? A PRO 248 20 1 Y 1 A PRO 247 ? A PRO 249 21 1 Y 1 A THR 248 ? A THR 250 22 1 Y 1 A ASP 249 ? A ASP 251 23 1 Y 1 A LYS 250 ? A LYS 252 24 1 Y 1 A GLY 251 ? A GLY 253 25 1 Y 1 A GLN 252 ? A GLN 254 26 1 Y 1 A GLN 253 ? A GLN 255 27 1 Y 1 A GLY 254 ? A GLY 256 28 1 Y 1 A ILE 255 ? A ILE 257 29 1 Y 1 A LEU 256 ? A LEU 258 30 1 Y 1 A ASN 257 ? A ASN 259 31 1 Y 1 A GLY 258 ? A GLY 260 32 1 Y 1 A ASN 259 ? A ASN 261 33 1 Y 1 A GLN 260 ? A GLN 262 34 1 Y 1 A HIS 261 ? A HIS 263 35 1 Y 1 A HIS 262 ? A HIS 264 36 1 Y 1 A HIS 263 ? A HIS 265 37 1 Y 1 A HIS 264 ? A HIS 266 38 1 Y 1 A HIS 265 ? A HIS 267 39 1 Y 1 A HIS 266 ? A HIS 268 40 1 Y 1 B SER -1 ? B SER 1 41 1 Y 1 B GLY 0 ? B GLY 2 42 1 Y 1 B LEU 1 ? B LEU 3 43 1 Y 1 B SER 2 ? B SER 4 44 1 Y 1 B GLY 131 ? B GLY 133 45 1 Y 1 B SER 132 ? B SER 134 46 1 Y 1 B GLU 133 ? B GLU 135 47 1 Y 1 B GLU 134 ? B GLU 136 48 1 Y 1 B ILE 135 ? B ILE 137 49 1 Y 1 B LEU 159 ? B LEU 161 50 1 Y 1 B SER 160 ? B SER 162 51 1 Y 1 B ASP 161 ? B ASP 163 52 1 Y 1 B SER 162 ? B SER 164 53 1 Y 1 B GLN 163 ? B GLN 165 54 1 Y 1 B THR 164 ? B THR 166 55 1 Y 1 B ALA 183 ? B ALA 185 56 1 Y 1 B SER 184 ? B SER 186 57 1 Y 1 B SER 185 ? B SER 187 58 1 Y 1 B GLU 186 ? B GLU 188 59 1 Y 1 B TYR 187 ? B TYR 189 60 1 Y 1 B SER 188 ? B SER 190 61 1 Y 1 B GLY 189 ? B GLY 191 62 1 Y 1 B THR 190 ? B THR 192 63 1 Y 1 B VAL 211 ? B VAL 213 64 1 Y 1 B PRO 212 ? B PRO 214 65 1 Y 1 B PRO 213 ? B PRO 215 66 1 Y 1 B SER 214 ? B SER 216 67 1 Y 1 B ASN 215 ? B ASN 217 68 1 Y 1 B ARG 216 ? B ARG 218 69 1 Y 1 B ALA 217 ? B ALA 219 70 1 Y 1 B HIS 218 ? B HIS 220 71 1 Y 1 B HIS 219 ? B HIS 221 72 1 Y 1 B HIS 220 ? B HIS 222 73 1 Y 1 B HIS 221 ? B HIS 223 74 1 Y 1 B HIS 222 ? B HIS 224 75 1 Y 1 B HIS 223 ? B HIS 225 # 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 ALPHA-L-FUCOSE FUC # 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 1 401 401 NAG NAG A . D 3 NAG 2 402 402 NAG NAG A . E 4 BMA 3 403 403 BMA BMA A . F 5 MAN 4 405 405 MAN MAN A . G 6 FUC 5 406 406 FUC FUC A . H 3 NAG 1 501 501 NAG NAG A . I 3 NAG 1 301 301 NAG NAG B . J 3 NAG 2 302 302 NAG NAG B . #