data_3MJ6 # _entry.id 3MJ6 # _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 3MJ6 RCSB RCSB058610 WWPDB D_1000058610 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.details _pdbx_database_related.content_type PDB 3MJ7 . unspecified PDB 3MJ8 . unspecified PDB 3MJ9 . unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 3MJ6 _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 3MJ6 _cell.length_a 61.946 _cell.length_b 61.946 _cell.length_c 82.477 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 90.00 _cell.Z_PDB 4 _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 3MJ6 _symmetry.space_group_name_H-M 'P 43' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 78 _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 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 3 ? ? ? ? 3 non-polymer man ALPHA-L-FUCOSE 164.156 1 ? ? ? ? 4 non-polymer syn 'SODIUM ION' 22.990 1 ? ? ? ? 5 non-polymer syn 'FORMIC ACID' 46.025 8 ? ? ? ? 6 water nat water 18.015 129 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name 'Dendritic cell-specific protein CREA7, mCrea7' # _entity_poly.entity_id 1 _entity_poly.type 'polypeptide(L)' _entity_poly.nstd_linkage no _entity_poly.nstd_monomer no _entity_poly.pdbx_seq_one_letter_code ;RSQGLPGLTVSSPQLRVHVGESVLMGCVVQRTEEKHVDRVDWLFSKDKDDASEYVLFYYSNLSVPTGRFQNRSHLVGDTF HNDGSLLLQDVQKADEGIYTCEIRLKNESMVMKKPVELWVLPEEPRDLRVRVGDTTQMRCSIQSTEEKRVTKVNWMFSSG SHTEEETVLSYDSNMRSGKFQSLGRFRNRVDLTGDISRNDGSIKLQTVKESDQGIYTCSIYVGKLESRKTIVLHVVQDEF QRTISPTPPTDKGQQGILNGNQHHHHHH ; _entity_poly.pdbx_seq_one_letter_code_can ;RSQGLPGLTVSSPQLRVHVGESVLMGCVVQRTEEKHVDRVDWLFSKDKDDASEYVLFYYSNLSVPTGRFQNRSHLVGDTF HNDGSLLLQDVQKADEGIYTCEIRLKNESMVMKKPVELWVLPEEPRDLRVRVGDTTQMRCSIQSTEEKRVTKVNWMFSSG SHTEEETVLSYDSNMRSGKFQSLGRFRNRVDLTGDISRNDGSIKLQTVKESDQGIYTCSIYVGKLESRKTIVLHVVQDEF QRTISPTPPTDKGQQGILNGNQHHHHHH ; _entity_poly.pdbx_strand_id A _entity_poly.pdbx_target_identifier ? # 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 # _entity_src_gen.entity_id 1 _entity_src_gen.pdbx_src_id 1 _entity_src_gen.pdbx_alt_source_flag sample _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 mouse _entity_src_gen.gene_src_genus ? _entity_src_gen.pdbx_gene_src_gene 'Amica1, Gm638, Jaml' _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 'Mus musculus' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 10090 _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 'FRUIT FLY' _entity_src_gen.pdbx_host_org_scientific_name 'DROSOPHILA MELANOGASTER' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 7227 _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 plasmid _entity_src_gen.pdbx_host_org_vector ? _entity_src_gen.host_org_details ? _entity_src_gen.expression_system_id ? _entity_src_gen.plasmid_name 'PMT/BIP/V5-HIS A' _entity_src_gen.plasmid_details ? _entity_src_gen.pdbx_description ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code JAML1_MOUSE _struct_ref.pdbx_db_accession Q80UL9 _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ;QGLPGLTVSSPQLRVHVGESVLMGCVVQRTEEKHVDRVDWLFSKDKDDASEYVLFYYSNLSVPTGRFQNRSHLVGDTFHN DGSLLLQDVQKADEGIYTCEIRLKNESMVMKKPVELWVLPEEPKDLRVRVGDTTQMRCSIQSTEEKRVTKVNWMFSSGSH TEEETVLSYDSNMRSGKFQSLGRFRNRVDLTGDISRNDGSIKLQTVKESDRGIYTCSIYVGKLESRKTIVLHVVQDEFQR TISPTPPTDKGQQGILNGNQ ; _struct_ref.pdbx_align_begin 21 _struct_ref.pdbx_db_isoform ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 3MJ6 _struct_ref_seq.pdbx_strand_id A _struct_ref_seq.seq_align_beg 3 _struct_ref_seq.pdbx_seq_align_beg_ins_code ? _struct_ref_seq.seq_align_end 262 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession Q80UL9 _struct_ref_seq.db_align_beg 21 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 280 _struct_ref_seq.pdbx_db_align_end_ins_code ? _struct_ref_seq.pdbx_auth_seq_align_beg 1 _struct_ref_seq.pdbx_auth_seq_align_end 260 # 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 3MJ6 ARG A 1 ? UNP Q80UL9 ? ? 'EXPRESSION TAG' -1 1 1 3MJ6 SER A 2 ? UNP Q80UL9 ? ? 'EXPRESSION TAG' 0 2 1 3MJ6 ARG A 126 ? UNP Q80UL9 LYS 144 'ENGINEERED MUTATION' 124 3 1 3MJ6 GLN A 213 ? UNP Q80UL9 ARG 231 'ENGINEERED MUTATION' 211 4 1 3MJ6 HIS A 263 ? UNP Q80UL9 ? ? 'EXPRESSION TAG' 261 5 1 3MJ6 HIS A 264 ? UNP Q80UL9 ? ? 'EXPRESSION TAG' 262 6 1 3MJ6 HIS A 265 ? UNP Q80UL9 ? ? 'EXPRESSION TAG' 263 7 1 3MJ6 HIS A 266 ? UNP Q80UL9 ? ? 'EXPRESSION TAG' 264 8 1 3MJ6 HIS A 267 ? UNP Q80UL9 ? ? 'EXPRESSION TAG' 265 9 1 3MJ6 HIS A 268 ? UNP Q80UL9 ? ? 'EXPRESSION TAG' 266 10 # 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 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 FMT non-polymer . 'FORMIC ACID' ? 'C H2 O2' 46.025 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 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NA non-polymer . 'SODIUM ION' ? 'Na 1' 22.990 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 3MJ6 _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.58 _exptl_crystal.density_percent_sol 52.36 _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 7.25 _exptl_crystal_grow.pdbx_details '3.25 M NA-FORMATE, 0.1 M IMIDAZOLE, pH 7.25, 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 'ADSC QUANTUM 210' _diffrn_detector.pdbx_collection_date 2005-02-17 _diffrn_detector.details 'KOHZU: DOUBLE CRYSTAL SI(111)' # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator ? _diffrn_radiation.pdbx_diffrn_protocol MAD _diffrn_radiation.pdbx_scattering_type x-ray # loop_ _diffrn_radiation_wavelength.id _diffrn_radiation_wavelength.wavelength _diffrn_radiation_wavelength.wt 1 1.07812 1.0 2 0.99984 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'ALS BEAMLINE 8.2.1' _diffrn_source.pdbx_synchrotron_site ALS _diffrn_source.pdbx_synchrotron_beamline 8.2.1 _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_wavelength_list '1.07812, 0.99984' # _reflns.entry_id 3MJ6 _reflns.observed_criterion_sigma_I 0.000 _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 50.000 _reflns.d_resolution_high 2.19 _reflns.number_obs 15924 _reflns.number_all ? _reflns.percent_possible_obs 99.7 _reflns.pdbx_Rmerge_I_obs 0.08300 _reflns.pdbx_Rsym_value 0.08300 _reflns.pdbx_netI_over_sigmaI 11.1000 _reflns.B_iso_Wilson_estimate 34.90 _reflns.pdbx_redundancy 3.600 _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 2.19 _reflns_shell.d_res_low 2.24 _reflns_shell.percent_possible_all 99.2 _reflns_shell.Rmerge_I_obs 0.41500 _reflns_shell.pdbx_Rsym_value 0.41500 _reflns_shell.meanI_over_sigI_obs 2.000 _reflns_shell.pdbx_redundancy ? _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 3MJ6 _refine.ls_number_reflns_obs 15098 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F 0.000 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 50.00 _refine.ls_d_res_high 2.19 _refine.ls_percent_reflns_obs 99.3 _refine.ls_R_factor_obs 0.172 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.170 _refine.ls_R_factor_R_free 0.213 _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 799 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.962 _refine.correlation_coeff_Fo_to_Fc_free 0.947 _refine.B_iso_mean 37.609 _refine.aniso_B[1][1] 0.16000 _refine.aniso_B[2][2] 0.16000 _refine.aniso_B[3][3] -0.33000 _refine.aniso_B[1][2] 0.00000 _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. CNS WAS ALSO USED FOR THE REFINEMENT.' _refine.pdbx_starting_model 'OBTAINED BY MAD PHASING OF A TA6BR12 SOAKED JAML CRYSTAL AND SUBSEQUENT MR INTO THE NATIVE HIGH RESOLUTION DATA' _refine.pdbx_method_to_determine_struct MAD _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values 'MAXIMUM LIKELIHOOD' _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_overall_ESU_R 0.209 _refine.pdbx_overall_ESU_R_Free 0.176 _refine.overall_SU_ML 0.128 _refine.overall_SU_B 9.735 _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 1828 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 77 _refine_hist.number_atoms_solvent 129 _refine_hist.number_atoms_total 2034 _refine_hist.d_res_high 2.19 _refine_hist.d_res_low 50.00 # 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 0.016 0.021 ? 1967 'X-RAY DIFFRACTION' ? r_bond_other_d 0.010 0.020 ? 1357 'X-RAY DIFFRACTION' ? r_angle_refined_deg 1.716 1.988 ? 2655 'X-RAY DIFFRACTION' ? r_angle_other_deg 1.296 3.002 ? 3279 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 8.007 5.000 ? 236 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg 40.550 23.936 ? 94 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg 16.657 15.000 ? 353 'X-RAY DIFFRACTION' ? r_dihedral_angle_4_deg 22.573 15.000 ? 17 'X-RAY DIFFRACTION' ? r_chiral_restr 0.127 0.200 ? 303 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.006 0.020 ? 2122 'X-RAY DIFFRACTION' ? r_gen_planes_other 0.001 0.020 ? 384 'X-RAY DIFFRACTION' ? r_nbd_refined 0.201 0.200 ? 270 'X-RAY DIFFRACTION' ? r_nbd_other 0.210 0.200 ? 1380 'X-RAY DIFFRACTION' ? r_nbtor_refined 0.170 0.200 ? 889 'X-RAY DIFFRACTION' ? r_nbtor_other 0.096 0.200 ? 1165 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_refined 0.199 0.200 ? 113 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_metal_ion_refined 0.031 0.200 ? 3 'X-RAY DIFFRACTION' ? r_metal_ion_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_vdw_refined 0.141 0.200 ? 22 'X-RAY DIFFRACTION' ? r_symmetry_vdw_other 0.237 0.200 ? 52 'X-RAY DIFFRACTION' ? r_symmetry_hbond_refined 0.123 0.200 ? 14 '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 0.862 1.500 ? 1164 'X-RAY DIFFRACTION' ? r_mcbond_other 0.183 1.500 ? 475 'X-RAY DIFFRACTION' ? r_mcangle_it 1.642 2.000 ? 1879 'X-RAY DIFFRACTION' ? r_scbond_it 2.625 3.000 ? 825 'X-RAY DIFFRACTION' ? r_scangle_it 4.414 4.500 ? 773 '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 2.19 _refine_ls_shell.d_res_low 2.25 _refine_ls_shell.number_reflns_R_work 1032 _refine_ls_shell.R_factor_R_work 0.2100 _refine_ls_shell.percent_reflns_obs 94.20 _refine_ls_shell.R_factor_R_free 0.3040 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 57 _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 3MJ6 _struct.title 'Crystal structure of the gammadelta T cell costimulatory receptor Junctional Adhesion Molecule-Like Protein, JAML' _struct.pdbx_descriptor 'Junctional adhesion molecule-like' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 3MJ6 _struct_keywords.pdbx_keywords 'IMMUNE SYSTEM' _struct_keywords.text ;IMMUNOGLOBULIN TANDEM DOMAIN, CELL ADHESION, CELL JUNCTION, GLYCOPROTEIN, IMMUNOGLOBULIN DOMAIN, MEMBRANE, COSTIMULATION, TRANSMEMBRANE, 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 2 ? D N N 2 ? E N N 3 ? F N N 4 ? G N N 5 ? H N N 5 ? I N N 5 ? J N N 5 ? K N N 5 ? L N N 5 ? M N N 5 ? N N N 5 ? O N N 6 ? # _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 # _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 ? ? ? ? ? ? ? 2.063 ? disulf2 disulf ? ? A CYS 140 SG ? ? ? 1_555 A CYS 218 SG ? ? A CYS 138 A CYS 216 1_555 ? ? ? ? ? ? ? 2.160 ? covale1 covale ? ? A ASN 71 ND2 ? ? ? 1_555 C NAG . C1 ? ? A ASN 69 A NAG 401 1_555 ? ? ? ? ? ? ? 1.458 ? covale2 covale ? ? D NAG . O6 ? ? ? 1_555 E FUC . C1 ? ? A NAG 501 A FUC 502 1_555 ? ? ? ? ? ? ? 1.464 ? covale3 covale ? ? A ASN 107 ND2 ? ? ? 1_555 D NAG . C1 ? ? A ASN 105 A NAG 501 1_555 ? ? ? ? ? ? ? 1.465 ? covale4 covale ? ? A ASN 61 ND2 ? ? ? 1_555 B NAG . C1 ? ? A ASN 59 A NAG 301 1_555 ? ? ? ? ? ? ? 1.473 ? metalc1 metalc ? ? A VAL 37 O ? ? ? 1_555 F NA . NA ? ? A VAL 35 A NA 503 1_555 ? ? ? ? ? ? ? 2.369 ? metalc2 metalc ? ? A ASN 61 OD1 ? ? ? 1_555 F NA . NA ? ? A ASN 59 A NA 503 1_555 ? ? ? ? ? ? ? 2.379 ? metalc3 metalc ? ? F NA . NA ? ? ? 1_555 O HOH . O ? ? A NA 503 A HOH 609 1_555 ? ? ? ? ? ? ? 2.393 ? metalc4 metalc ? ? F NA . NA ? ? ? 1_555 O HOH . O ? ? A NA 503 A HOH 611 1_555 ? ? ? ? ? ? ? 2.428 ? metalc5 metalc ? ? F NA . NA ? ? ? 1_555 O HOH . O ? ? A NA 503 A HOH 610 1_555 ? ? ? ? ? ? ? 2.496 ? metalc6 metalc ? ? A TYR 58 OH ? ? ? 1_555 F NA . NA ? ? A TYR 56 A NA 503 1_555 ? ? ? ? ? ? ? 2.528 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? metalc ? ? # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 6 ? B ? 4 ? C ? 6 ? D ? 3 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense A 1 2 ? parallel A 2 3 ? anti-parallel A 3 4 ? anti-parallel A 4 5 ? anti-parallel A 5 6 ? anti-parallel B 1 2 ? anti-parallel B 2 3 ? anti-parallel B 3 4 ? parallel C 1 2 ? parallel C 2 3 ? anti-parallel C 3 4 ? anti-parallel C 4 5 ? anti-parallel C 5 6 ? anti-parallel D 1 2 ? anti-parallel D 2 3 ? anti-parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id A 1 GLN A 14 ? HIS A 18 ? GLN A 12 HIS A 16 A 2 VAL A 111 ? LEU A 121 ? VAL A 109 LEU A 119 A 3 GLY A 97 ? LEU A 105 ? GLY A 95 LEU A 103 A 4 VAL A 37 ? SER A 45 ? VAL A 35 SER A 43 A 5 GLU A 53 ? TYR A 59 ? GLU A 51 TYR A 57 A 6 LEU A 62 ? PRO A 65 ? LEU A 60 PRO A 63 B 1 SER A 73 ? LEU A 75 ? SER A 71 LEU A 73 B 2 LEU A 86 ? LEU A 88 ? LEU A 84 LEU A 86 B 3 VAL A 23 ? MET A 25 ? VAL A 21 MET A 23 B 4 GLN A 143 ? SER A 144 ? GLN A 141 SER A 142 C 1 ASP A 127 ? ARG A 131 ? ASP A 125 ARG A 129 C 2 LEU A 225 ? VAL A 236 ? LEU A 223 VAL A 234 C 3 GLY A 214 ? VAL A 222 ? GLY A 212 VAL A 220 C 4 LYS A 152 ? SER A 158 ? LYS A 150 SER A 156 C 5 GLU A 166 ? ASP A 172 ? GLU A 164 ASP A 170 C 6 LYS A 179 ? GLN A 181 ? LYS A 177 GLN A 179 D 1 THR A 136 ? MET A 138 ? THR A 134 MET A 136 D 2 ILE A 203 ? LEU A 205 ? ILE A 201 LEU A 203 D 3 VAL A 190 ? LEU A 192 ? VAL A 188 LEU A 190 # 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 LEU A 15 ? N LEU A 13 O TRP A 119 ? O TRP A 117 A 2 3 O LEU A 118 ? O LEU A 116 N GLY A 97 ? N GLY A 95 A 3 4 O ILE A 98 ? O ILE A 96 N SER A 45 ? N SER A 43 A 4 5 N PHE A 44 ? N PHE A 42 O GLU A 53 ? O GLU A 51 A 5 6 N PHE A 57 ? N PHE A 55 O VAL A 64 ? O VAL A 62 B 1 2 N HIS A 74 ? N HIS A 72 O LEU A 87 ? O LEU A 85 B 2 3 O LEU A 88 ? O LEU A 86 N VAL A 23 ? N VAL A 21 B 3 4 N LEU A 24 ? N LEU A 22 O GLN A 143 ? O GLN A 141 C 1 2 N LEU A 128 ? N LEU A 126 O VAL A 232 ? O VAL A 230 C 2 3 O ILE A 231 ? O ILE A 229 N TYR A 216 ? N TYR A 214 C 3 4 O TYR A 221 ? O TYR A 219 N LYS A 152 ? N LYS A 150 C 4 5 N TRP A 155 ? N TRP A 153 O LEU A 169 ? O LEU A 167 C 5 6 N SER A 170 ? N SER A 168 O PHE A 180 ? O PHE A 178 D 1 2 N THR A 136 ? N THR A 134 O LEU A 205 ? O LEU A 203 D 2 3 O LYS A 204 ? O LYS A 202 N ASP A 191 ? N ASP A 189 # 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 ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG A 301' AC2 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG A 401' AC3 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG A 501' AC4 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE FUC A 502' AC5 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE NA A 503' AC6 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE FMT A 601' AC7 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE FMT A 602' AC8 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE FMT A 604' AC9 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE FMT A 605' BC1 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE FMT A 606' BC2 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE FMT A 607' BC3 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE FMT A 608' # 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 1 ASN A 61 ? ASN A 59 . ? 1_555 ? 2 AC2 3 ASN A 71 ? ASN A 69 . ? 1_555 ? 3 AC2 3 HIS A 74 ? HIS A 72 . ? 1_555 ? 4 AC2 3 HOH O . ? HOH A 642 . ? 1_555 ? 5 AC3 3 ASN A 107 ? ASN A 105 . ? 1_555 ? 6 AC3 3 FUC E . ? FUC A 502 . ? 1_555 ? 7 AC3 3 HOH O . ? HOH A 644 . ? 1_555 ? 8 AC4 4 THR A 145 ? THR A 143 . ? 3_654 ? 9 AC4 4 GLU A 146 ? GLU A 144 . ? 3_654 ? 10 AC4 4 NAG D . ? NAG A 501 . ? 1_555 ? 11 AC4 4 HOH O . ? HOH A 644 . ? 1_555 ? 12 AC5 6 VAL A 37 ? VAL A 35 . ? 1_555 ? 13 AC5 6 TYR A 58 ? TYR A 56 . ? 1_555 ? 14 AC5 6 ASN A 61 ? ASN A 59 . ? 1_555 ? 15 AC5 6 HOH O . ? HOH A 609 . ? 1_555 ? 16 AC5 6 HOH O . ? HOH A 610 . ? 1_555 ? 17 AC5 6 HOH O . ? HOH A 611 . ? 1_555 ? 18 AC6 4 SER A 159 ? SER A 157 . ? 1_555 ? 19 AC6 4 GLY A 160 ? GLY A 158 . ? 1_555 ? 20 AC6 4 PHE A 180 ? PHE A 178 . ? 4_555 ? 21 AC6 4 GLN A 213 ? GLN A 211 . ? 1_555 ? 22 AC7 3 SER A 170 ? SER A 168 . ? 1_555 ? 23 AC7 3 MET A 175 ? MET A 173 . ? 1_555 ? 24 AC7 3 GLY A 178 ? GLY A 176 . ? 1_555 ? 25 AC8 5 SER A 45 ? SER A 43 . ? 1_555 ? 26 AC8 5 LYS A 46 ? LYS A 44 . ? 1_555 ? 27 AC8 5 ASP A 49 ? ASP A 47 . ? 1_555 ? 28 AC8 5 ALA A 51 ? ALA A 49 . ? 1_555 ? 29 AC8 5 GLU A 53 ? GLU A 51 . ? 1_555 ? 30 AC9 2 LYS A 93 ? LYS A 91 . ? 1_555 ? 31 AC9 2 PRO A 122 ? PRO A 120 . ? 1_555 ? 32 BC1 3 LYS A 35 ? LYS A 33 . ? 1_555 ? 33 BC1 3 HIS A 36 ? HIS A 34 . ? 1_555 ? 34 BC1 3 LYS A 106 ? LYS A 104 . ? 1_555 ? 35 BC2 4 GLU A 96 ? GLU A 94 . ? 1_555 ? 36 BC2 4 GLY A 97 ? GLY A 95 . ? 1_555 ? 37 BC2 4 LEU A 118 ? LEU A 116 . ? 1_555 ? 38 BC2 4 TRP A 119 ? TRP A 117 . ? 1_555 ? 39 BC3 6 GLU A 53 ? GLU A 51 . ? 1_555 ? 40 BC3 6 TYR A 54 ? TYR A 52 . ? 1_555 ? 41 BC3 6 ARG A 129 ? ARG A 127 . ? 3_654 ? 42 BC3 6 VAL A 130 ? VAL A 128 . ? 3_654 ? 43 BC3 6 THR A 136 ? THR A 134 . ? 3_654 ? 44 BC3 6 HOH O . ? HOH A 645 . ? 1_555 ? # _database_PDB_matrix.entry_id 3MJ6 _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 3MJ6 _atom_sites.fract_transf_matrix[1][1] 0.016143 _atom_sites.fract_transf_matrix[1][2] 0.000000 _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] 0.016143 _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] 0.012125 _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 NA 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 . SER A 1 12 ? 31.289 28.790 0.508 1.00 53.69 ? 10 SER A N 1 ATOM 2 C CA . SER A 1 12 ? 31.168 27.338 0.856 1.00 50.45 ? 10 SER A CA 1 ATOM 3 C C . SER A 1 12 ? 30.090 27.176 1.942 1.00 48.64 ? 10 SER A C 1 ATOM 4 O O . SER A 1 12 ? 30.183 27.833 2.969 1.00 50.13 ? 10 SER A O 1 ATOM 5 C CB . SER A 1 12 ? 32.523 26.798 1.377 1.00 50.63 ? 10 SER A CB 1 ATOM 6 O OG . SER A 1 12 ? 32.370 25.832 2.432 1.00 50.26 ? 10 SER A OG 1 ATOM 7 N N A PRO A 1 13 ? 29.095 26.292 1.726 0.50 45.86 ? 11 PRO A N 1 ATOM 8 N N B PRO A 1 13 ? 29.095 26.287 1.721 0.50 45.81 ? 11 PRO A N 1 ATOM 9 C CA A PRO A 1 13 ? 28.005 26.172 2.707 0.50 44.93 ? 11 PRO A CA 1 ATOM 10 C CA B PRO A 1 13 ? 28.015 26.111 2.706 0.50 44.78 ? 11 PRO A CA 1 ATOM 11 C C A PRO A 1 13 ? 28.491 25.709 4.076 0.50 43.36 ? 11 PRO A C 1 ATOM 12 C C B PRO A 1 13 ? 28.540 25.742 4.088 0.50 43.42 ? 11 PRO A C 1 ATOM 13 O O A PRO A 1 13 ? 29.375 24.857 4.152 0.50 41.37 ? 11 PRO A O 1 ATOM 14 O O B PRO A 1 13 ? 29.516 25.000 4.185 0.50 41.76 ? 11 PRO A O 1 ATOM 15 C CB A PRO A 1 13 ? 27.077 25.109 2.095 0.50 42.75 ? 11 PRO A CB 1 ATOM 16 C CB B PRO A 1 13 ? 27.195 24.935 2.146 0.50 42.32 ? 11 PRO A CB 1 ATOM 17 C CG A PRO A 1 13 ? 27.900 24.391 1.098 0.50 42.00 ? 11 PRO A CG 1 ATOM 18 C CG B PRO A 1 13 ? 27.545 24.849 0.710 0.50 42.76 ? 11 PRO A CG 1 ATOM 19 C CD A PRO A 1 13 ? 28.929 25.357 0.601 0.50 44.01 ? 11 PRO A CD 1 ATOM 20 C CD B PRO A 1 13 ? 28.936 25.392 0.559 0.50 44.04 ? 11 PRO A CD 1 ATOM 21 N N . GLN A 1 14 ? 27.895 26.268 5.131 1.00 43.69 ? 12 GLN A N 1 ATOM 22 C CA . GLN A 1 14 ? 28.189 25.892 6.504 1.00 42.19 ? 12 GLN A CA 1 ATOM 23 C C . GLN A 1 14 ? 26.938 25.351 7.178 1.00 39.63 ? 12 GLN A C 1 ATOM 24 O O . GLN A 1 14 ? 26.024 26.085 7.513 1.00 41.19 ? 12 GLN A O 1 ATOM 25 C CB . GLN A 1 14 ? 28.747 27.078 7.262 1.00 45.00 ? 12 GLN A CB 1 ATOM 26 C CG . GLN A 1 14 ? 30.075 27.537 6.646 1.00 48.23 ? 12 GLN A CG 1 ATOM 27 C CD . GLN A 1 14 ? 30.727 28.635 7.431 1.00 54.48 ? 12 GLN A CD 1 ATOM 28 O OE1 . GLN A 1 14 ? 30.052 29.479 8.022 1.00 57.13 ? 12 GLN A OE1 1 ATOM 29 N NE2 . GLN A 1 14 ? 32.054 28.636 7.449 1.00 58.08 ? 12 GLN A NE2 1 ATOM 30 N N . LEU A 1 15 ? 26.926 24.045 7.365 1.00 35.38 ? 13 LEU A N 1 ATOM 31 C CA . LEU A 1 15 ? 25.757 23.313 7.814 1.00 33.96 ? 13 LEU A CA 1 ATOM 32 C C . LEU A 1 15 ? 25.960 22.911 9.258 1.00 33.16 ? 13 LEU A C 1 ATOM 33 O O . LEU A 1 15 ? 26.987 22.298 9.584 1.00 32.91 ? 13 LEU A O 1 ATOM 34 C CB . LEU A 1 15 ? 25.622 22.046 6.992 1.00 31.13 ? 13 LEU A CB 1 ATOM 35 C CG . LEU A 1 15 ? 24.779 21.933 5.726 1.00 32.72 ? 13 LEU A CG 1 ATOM 36 C CD1 . LEU A 1 15 ? 24.379 23.242 5.072 1.00 34.12 ? 13 LEU A CD1 1 ATOM 37 C CD2 . LEU A 1 15 ? 25.472 20.924 4.756 1.00 28.17 ? 13 LEU A CD2 1 ATOM 38 N N . ARG A 1 16 ? 25.031 23.283 10.130 1.00 33.15 ? 14 ARG A N 1 ATOM 39 C CA . ARG A 1 16 ? 25.026 22.762 11.510 1.00 32.24 ? 14 ARG A CA 1 ATOM 40 C C . ARG A 1 16 ? 23.953 21.712 11.678 1.00 30.58 ? 14 ARG A C 1 ATOM 41 O O . ARG A 1 16 ? 22.834 21.890 11.182 1.00 30.02 ? 14 ARG A O 1 ATOM 42 C CB . ARG A 1 16 ? 24.741 23.856 12.519 1.00 34.77 ? 14 ARG A CB 1 ATOM 43 C CG . ARG A 1 16 ? 25.635 25.023 12.398 1.00 38.02 ? 14 ARG A CG 1 ATOM 44 C CD . ARG A 1 16 ? 25.756 25.741 13.694 1.00 42.85 ? 14 ARG A CD 1 ATOM 45 N NE . ARG A 1 16 ? 26.382 27.029 13.433 1.00 47.56 ? 14 ARG A NE 1 ATOM 46 C CZ . ARG A 1 16 ? 26.295 28.101 14.214 1.00 49.91 ? 14 ARG A CZ 1 ATOM 47 N NH1 . ARG A 1 16 ? 25.612 28.077 15.361 1.00 49.42 ? 14 ARG A NH1 1 ATOM 48 N NH2 . ARG A 1 16 ? 26.911 29.214 13.826 1.00 53.62 ? 14 ARG A NH2 1 ATOM 49 N N . VAL A 1 17 ? 24.308 20.643 12.381 1.00 29.01 ? 15 VAL A N 1 ATOM 50 C CA . VAL A 1 17 ? 23.390 19.595 12.777 1.00 29.50 ? 15 VAL A CA 1 ATOM 51 C C . VAL A 1 17 ? 23.677 19.167 14.222 1.00 29.39 ? 15 VAL A C 1 ATOM 52 O O . VAL A 1 17 ? 24.769 19.345 14.723 1.00 30.97 ? 15 VAL A O 1 ATOM 53 C CB . VAL A 1 17 ? 23.486 18.331 11.827 1.00 28.97 ? 15 VAL A CB 1 ATOM 54 C CG1 . VAL A 1 17 ? 23.043 18.676 10.386 1.00 28.55 ? 15 VAL A CG1 1 ATOM 55 C CG2 . VAL A 1 17 ? 24.868 17.745 11.825 1.00 27.44 ? 15 VAL A CG2 1 ATOM 56 N N . HIS A 1 18 ? 22.672 18.617 14.876 1.00 29.09 ? 16 HIS A N 1 ATOM 57 C CA . HIS A 1 18 ? 22.813 17.981 16.171 1.00 28.94 ? 16 HIS A CA 1 ATOM 58 C C . HIS A 1 18 ? 23.317 16.551 15.979 1.00 27.98 ? 16 HIS A C 1 ATOM 59 O O . HIS A 1 18 ? 23.089 15.948 14.926 1.00 26.82 ? 16 HIS A O 1 ATOM 60 C CB . HIS A 1 18 ? 21.466 17.959 16.882 1.00 29.71 ? 16 HIS A CB 1 ATOM 61 C CG . HIS A 1 18 ? 20.902 19.318 17.169 1.00 31.05 ? 16 HIS A CG 1 ATOM 62 N ND1 . HIS A 1 18 ? 21.281 20.062 18.267 1.00 32.44 ? 16 HIS A ND1 1 ATOM 63 C CD2 . HIS A 1 18 ? 19.975 20.052 16.516 1.00 31.13 ? 16 HIS A CD2 1 ATOM 64 C CE1 . HIS A 1 18 ? 20.629 21.209 18.256 1.00 35.52 ? 16 HIS A CE1 1 ATOM 65 N NE2 . HIS A 1 18 ? 19.826 21.226 17.205 1.00 34.52 ? 16 HIS A NE2 1 ATOM 66 N N . VAL A 1 19 ? 24.013 16.020 16.994 1.00 28.62 ? 17 VAL A N 1 ATOM 67 C CA . VAL A 1 19 ? 24.432 14.617 17.028 1.00 27.68 ? 17 VAL A CA 1 ATOM 68 C C . VAL A 1 19 ? 23.193 13.736 16.823 1.00 27.92 ? 17 VAL A C 1 ATOM 69 O O . VAL A 1 19 ? 22.143 14.020 17.361 1.00 28.26 ? 17 VAL A O 1 ATOM 70 C CB . VAL A 1 19 ? 25.204 14.254 18.345 1.00 29.39 ? 17 VAL A CB 1 ATOM 71 C CG1 . VAL A 1 19 ? 25.380 12.730 18.504 1.00 27.43 ? 17 VAL A CG1 1 ATOM 72 C CG2 . VAL A 1 19 ? 26.610 14.975 18.398 1.00 26.96 ? 17 VAL A CG2 1 ATOM 73 N N . GLY A 1 20 ? 23.311 12.737 15.951 1.00 28.10 ? 18 GLY A N 1 ATOM 74 C CA . GLY A 1 20 ? 22.195 11.835 15.646 1.00 29.67 ? 18 GLY A CA 1 ATOM 75 C C . GLY A 1 20 ? 21.476 12.156 14.343 1.00 29.31 ? 18 GLY A C 1 ATOM 76 O O . GLY A 1 20 ? 20.880 11.281 13.759 1.00 29.70 ? 18 GLY A O 1 ATOM 77 N N . GLU A 1 21 ? 21.545 13.404 13.882 1.00 29.18 ? 19 GLU A N 1 ATOM 78 C CA . GLU A 1 21 ? 20.843 13.818 12.679 1.00 29.29 ? 19 GLU A CA 1 ATOM 79 C C . GLU A 1 21 ? 21.532 13.336 11.389 1.00 28.19 ? 19 GLU A C 1 ATOM 80 O O . GLU A 1 21 ? 22.718 12.921 11.376 1.00 27.06 ? 19 GLU A O 1 ATOM 81 C CB . GLU A 1 21 ? 20.723 15.348 12.610 1.00 29.82 ? 19 GLU A CB 1 ATOM 82 C CG . GLU A 1 21 ? 19.736 16.001 13.572 1.00 33.15 ? 19 GLU A CG 1 ATOM 83 C CD . GLU A 1 21 ? 19.469 17.483 13.209 1.00 38.81 ? 19 GLU A CD 1 ATOM 84 O OE1 . GLU A 1 21 ? 20.284 18.374 13.537 1.00 38.16 ? 19 GLU A OE1 1 ATOM 85 O OE2 . GLU A 1 21 ? 18.424 17.761 12.576 1.00 44.27 ? 19 GLU A OE2 1 ATOM 86 N N . SER A 1 22 ? 20.773 13.426 10.306 1.00 27.61 ? 20 SER A N 1 ATOM 87 C CA . SER A 1 22 ? 21.280 13.188 8.975 1.00 26.63 ? 20 SER A CA 1 ATOM 88 C C . SER A 1 22 ? 21.530 14.541 8.314 1.00 26.77 ? 20 SER A C 1 ATOM 89 O O . SER A 1 22 ? 20.909 15.574 8.672 1.00 28.03 ? 20 SER A O 1 ATOM 90 C CB . SER A 1 22 ? 20.254 12.411 8.150 1.00 27.83 ? 20 SER A CB 1 ATOM 91 O OG . SER A 1 22 ? 20.141 11.051 8.529 1.00 26.42 ? 20 SER A OG 1 ATOM 92 N N . VAL A 1 23 ? 22.397 14.534 7.320 1.00 25.33 ? 21 VAL A N 1 ATOM 93 C CA . VAL A 1 23 ? 22.665 15.729 6.539 1.00 24.67 ? 21 VAL A CA 1 ATOM 94 C C . VAL A 1 23 ? 22.907 15.339 5.095 1.00 24.19 ? 21 VAL A C 1 ATOM 95 O O . VAL A 1 23 ? 23.595 14.369 4.804 1.00 23.03 ? 21 VAL A O 1 ATOM 96 C CB . VAL A 1 23 ? 23.900 16.524 7.145 1.00 25.05 ? 21 VAL A CB 1 ATOM 97 C CG1 . VAL A 1 23 ? 25.135 15.661 7.156 1.00 21.96 ? 21 VAL A CG1 1 ATOM 98 C CG2 . VAL A 1 23 ? 24.136 17.836 6.381 1.00 23.32 ? 21 VAL A CG2 1 ATOM 99 N N . LEU A 1 24 ? 22.265 16.063 4.188 1.00 25.37 ? 22 LEU A N 1 ATOM 100 C CA . LEU A 1 24 ? 22.446 15.867 2.758 1.00 24.58 ? 22 LEU A CA 1 ATOM 101 C C . LEU A 1 24 ? 23.300 17.000 2.233 1.00 24.14 ? 22 LEU A C 1 ATOM 102 O O . LEU A 1 24 ? 22.881 18.135 2.254 1.00 24.28 ? 22 LEU A O 1 ATOM 103 C CB . LEU A 1 24 ? 21.090 15.837 2.027 1.00 25.70 ? 22 LEU A CB 1 ATOM 104 C CG . LEU A 1 24 ? 21.023 15.176 0.639 1.00 25.30 ? 22 LEU A CG 1 ATOM 105 C CD1 . LEU A 1 24 ? 19.595 14.659 0.399 1.00 25.42 ? 22 LEU A CD1 1 ATOM 106 C CD2 . LEU A 1 24 ? 21.442 16.100 -0.494 1.00 26.52 ? 22 LEU A CD2 1 ATOM 107 N N . MET A 1 25 ? 24.499 16.668 1.767 1.00 23.67 ? 23 MET A N 1 ATOM 108 C CA . MET A 1 25 ? 25.408 17.649 1.200 1.00 24.94 ? 23 MET A CA 1 ATOM 109 C C . MET A 1 25 ? 25.358 17.558 -0.322 1.00 25.32 ? 23 MET A C 1 ATOM 110 O O . MET A 1 25 ? 25.757 16.542 -0.917 1.00 25.33 ? 23 MET A O 1 ATOM 111 C CB . MET A 1 25 ? 26.817 17.398 1.700 1.00 24.30 ? 23 MET A CB 1 ATOM 112 C CG . MET A 1 25 ? 26.912 17.454 3.221 1.00 26.72 ? 23 MET A CG 1 ATOM 113 S SD . MET A 1 25 ? 28.604 17.066 3.749 1.00 31.23 ? 23 MET A SD 1 ATOM 114 C CE . MET A 1 25 ? 28.351 16.196 5.295 1.00 31.46 ? 23 MET A CE 1 ATOM 115 N N . GLY A 1 26 ? 24.849 18.626 -0.919 1.00 26.65 ? 24 GLY A N 1 ATOM 116 C CA . GLY A 1 26 ? 24.629 18.709 -2.325 1.00 28.25 ? 24 GLY A CA 1 ATOM 117 C C . GLY A 1 26 ? 25.951 18.810 -3.040 1.00 28.75 ? 24 GLY A C 1 ATOM 118 O O . GLY A 1 26 ? 26.879 19.443 -2.550 1.00 28.13 ? 24 GLY A O 1 ATOM 119 N N . CYS A 1 27 ? 26.010 18.168 -4.200 1.00 29.27 ? 25 CYS A N 1 ATOM 120 C CA . CYS A 1 27 ? 27.099 18.304 -5.137 1.00 29.99 ? 25 CYS A CA 1 ATOM 121 C C . CYS A 1 27 ? 26.502 18.094 -6.557 1.00 30.47 ? 25 CYS A C 1 ATOM 122 O O . CYS A 1 27 ? 26.549 17.015 -7.119 1.00 30.15 ? 25 CYS A O 1 ATOM 123 C CB . CYS A 1 27 ? 28.209 17.311 -4.773 1.00 28.96 ? 25 CYS A CB 1 ATOM 124 S SG . CYS A 1 27 ? 29.685 17.387 -5.773 1.00 33.49 ? 25 CYS A SG 1 ATOM 125 N N . VAL A 1 28 ? 25.922 19.158 -7.098 1.00 32.28 ? 26 VAL A N 1 ATOM 126 C CA . VAL A 1 28 ? 25.204 19.137 -8.370 1.00 33.70 ? 26 VAL A CA 1 ATOM 127 C C . VAL A 1 28 ? 25.938 20.022 -9.365 1.00 35.26 ? 26 VAL A C 1 ATOM 128 O O . VAL A 1 28 ? 26.209 21.186 -9.080 1.00 36.33 ? 26 VAL A O 1 ATOM 129 C CB . VAL A 1 28 ? 23.741 19.650 -8.213 1.00 35.32 ? 26 VAL A CB 1 ATOM 130 C CG1 . VAL A 1 28 ? 22.988 19.624 -9.577 1.00 36.67 ? 26 VAL A CG1 1 ATOM 131 C CG2 . VAL A 1 28 ? 22.984 18.836 -7.184 1.00 34.01 ? 26 VAL A CG2 1 ATOM 132 N N . VAL A 1 29 ? 26.284 19.468 -10.524 1.00 36.18 ? 27 VAL A N 1 ATOM 133 C CA . VAL A 1 29 ? 27.006 20.225 -11.547 1.00 37.67 ? 27 VAL A CA 1 ATOM 134 C C . VAL A 1 29 ? 25.939 20.902 -12.389 1.00 41.16 ? 27 VAL A C 1 ATOM 135 O O . VAL A 1 29 ? 25.052 20.246 -12.917 1.00 42.04 ? 27 VAL A O 1 ATOM 136 C CB . VAL A 1 29 ? 27.926 19.310 -12.367 1.00 36.92 ? 27 VAL A CB 1 ATOM 137 C CG1 . VAL A 1 29 ? 28.619 20.057 -13.498 1.00 38.65 ? 27 VAL A CG1 1 ATOM 138 C CG2 . VAL A 1 29 ? 28.948 18.657 -11.459 1.00 33.03 ? 27 VAL A CG2 1 ATOM 139 N N . GLN A 1 30 ? 25.988 22.230 -12.468 1.00 44.01 ? 28 GLN A N 1 ATOM 140 C CA . GLN A 1 30 ? 25.023 22.969 -13.261 1.00 47.71 ? 28 GLN A CA 1 ATOM 141 C C . GLN A 1 30 ? 25.308 22.858 -14.756 1.00 48.26 ? 28 GLN A C 1 ATOM 142 O O . GLN A 1 30 ? 26.287 23.410 -15.246 1.00 48.03 ? 28 GLN A O 1 ATOM 143 C CB . GLN A 1 30 ? 25.023 24.446 -12.860 1.00 51.05 ? 28 GLN A CB 1 ATOM 144 C CG . GLN A 1 30 ? 24.838 24.690 -11.353 1.00 52.83 ? 28 GLN A CG 1 ATOM 145 C CD . GLN A 1 30 ? 23.623 23.972 -10.773 1.00 56.34 ? 28 GLN A CD 1 ATOM 146 O OE1 . GLN A 1 30 ? 22.575 23.871 -11.420 1.00 61.10 ? 28 GLN A OE1 1 ATOM 147 N NE2 . GLN A 1 30 ? 23.766 23.465 -9.545 1.00 56.47 ? 28 GLN A NE2 1 ATOM 148 N N . ARG A 1 31 ? 24.440 22.146 -15.468 1.00 48.74 ? 29 ARG A N 1 ATOM 149 C CA . ARG A 1 31 ? 24.500 22.062 -16.929 1.00 50.68 ? 29 ARG A CA 1 ATOM 150 C C . ARG A 1 31 ? 23.096 22.218 -17.516 1.00 54.35 ? 29 ARG A C 1 ATOM 151 O O . ARG A 1 31 ? 22.106 21.986 -16.831 1.00 53.85 ? 29 ARG A O 1 ATOM 152 C CB . ARG A 1 31 ? 25.107 20.728 -17.382 1.00 48.39 ? 29 ARG A CB 1 ATOM 153 C CG . ARG A 1 31 ? 26.567 20.471 -16.924 1.00 45.20 ? 29 ARG A CG 1 ATOM 154 C CD . ARG A 1 31 ? 27.619 21.286 -17.684 1.00 46.00 ? 29 ARG A CD 1 ATOM 155 N NE . ARG A 1 31 ? 28.980 20.938 -17.239 1.00 45.79 ? 29 ARG A NE 1 ATOM 156 C CZ . ARG A 1 31 ? 29.700 21.602 -16.320 1.00 45.59 ? 29 ARG A CZ 1 ATOM 157 N NH1 . ARG A 1 31 ? 29.211 22.668 -15.698 1.00 46.86 ? 29 ARG A NH1 1 ATOM 158 N NH2 . ARG A 1 31 ? 30.925 21.177 -15.982 1.00 43.04 ? 29 ARG A NH2 1 ATOM 159 N N . THR A 1 32 ? 23.002 22.603 -18.788 1.00 58.05 ? 30 THR A N 1 ATOM 160 C CA . THR A 1 32 ? 21.696 22.605 -19.442 1.00 62.39 ? 30 THR A CA 1 ATOM 161 C C . THR A 1 32 ? 21.314 21.170 -19.848 1.00 62.16 ? 30 THR A C 1 ATOM 162 O O . THR A 1 32 ? 20.135 20.805 -19.771 1.00 64.05 ? 30 THR A O 1 ATOM 163 C CB . THR A 1 32 ? 21.602 23.614 -20.624 1.00 66.47 ? 30 THR A CB 1 ATOM 164 O OG1 . THR A 1 32 ? 22.607 23.334 -21.602 1.00 66.71 ? 30 THR A OG1 1 ATOM 165 C CG2 . THR A 1 32 ? 21.793 25.027 -20.112 1.00 67.90 ? 30 THR A CG2 1 ATOM 166 N N . GLU A 1 33 ? 22.309 20.360 -20.227 1.00 60.12 ? 31 GLU A N 1 ATOM 167 C CA . GLU A 1 33 ? 22.086 18.949 -20.568 1.00 59.93 ? 31 GLU A CA 1 ATOM 168 C C . GLU A 1 33 ? 22.107 18.031 -19.324 1.00 56.44 ? 31 GLU A C 1 ATOM 169 O O . GLU A 1 33 ? 22.763 18.322 -18.324 1.00 53.26 ? 31 GLU A O 1 ATOM 170 C CB . GLU A 1 33 ? 23.116 18.475 -21.614 1.00 60.32 ? 31 GLU A CB 1 ATOM 171 C CG . GLU A 1 33 ? 22.832 17.053 -22.175 1.00 62.71 ? 31 GLU A CG 1 ATOM 172 C CD . GLU A 1 33 ? 23.564 16.726 -23.484 1.00 65.68 ? 31 GLU A CD 1 ATOM 173 O OE1 . GLU A 1 33 ? 24.741 16.289 -23.426 1.00 62.84 ? 31 GLU A OE1 1 ATOM 174 O OE2 . GLU A 1 33 ? 22.937 16.874 -24.571 1.00 71.20 ? 31 GLU A OE2 1 ATOM 175 N N . GLU A 1 34 ? 21.347 16.938 -19.395 1.00 56.88 ? 32 GLU A N 1 ATOM 176 C CA . GLU A 1 34 ? 21.347 15.906 -18.368 1.00 54.07 ? 32 GLU A CA 1 ATOM 177 C C . GLU A 1 34 ? 22.457 14.931 -18.682 1.00 51.15 ? 32 GLU A C 1 ATOM 178 O O . GLU A 1 34 ? 22.328 14.123 -19.615 1.00 52.96 ? 32 GLU A O 1 ATOM 179 C CB . GLU A 1 34 ? 20.023 15.141 -18.364 1.00 56.90 ? 32 GLU A CB 1 ATOM 180 C CG . GLU A 1 34 ? 18.865 15.887 -17.746 1.00 61.26 ? 32 GLU A CG 1 ATOM 181 C CD . GLU A 1 34 ? 17.586 15.042 -17.658 1.00 67.26 ? 32 GLU A CD 1 ATOM 182 O OE1 . GLU A 1 34 ? 17.651 13.904 -17.130 1.00 68.71 ? 32 GLU A OE1 1 ATOM 183 O OE2 . GLU A 1 34 ? 16.517 15.531 -18.088 1.00 71.26 ? 32 GLU A OE2 1 ATOM 184 N N . LYS A 1 35 ? 23.548 15.004 -17.918 1.00 46.34 ? 33 LYS A N 1 ATOM 185 C CA . LYS A 1 35 ? 24.724 14.182 -18.165 1.00 43.29 ? 33 LYS A CA 1 ATOM 186 C C . LYS A 1 35 ? 24.886 13.133 -17.068 1.00 40.44 ? 33 LYS A C 1 ATOM 187 O O . LYS A 1 35 ? 24.495 13.351 -15.935 1.00 39.10 ? 33 LYS A O 1 ATOM 188 C CB . LYS A 1 35 ? 25.985 15.047 -18.230 1.00 42.03 ? 33 LYS A CB 1 ATOM 189 C CG . LYS A 1 35 ? 25.947 16.187 -19.250 1.00 43.40 ? 33 LYS A CG 1 ATOM 190 C CD . LYS A 1 35 ? 27.343 16.532 -19.769 1.00 40.41 ? 33 LYS A CD 1 ATOM 191 C CE . LYS A 1 35 ? 27.323 17.770 -20.668 1.00 43.92 ? 33 LYS A CE 1 ATOM 192 N NZ . LYS A 1 35 ? 28.666 18.165 -21.177 1.00 41.98 ? 33 LYS A NZ 1 ATOM 193 N N . HIS A 1 36 ? 25.464 11.988 -17.408 1.00 39.15 ? 34 HIS A N 1 ATOM 194 C CA . HIS A 1 36 ? 25.831 11.002 -16.398 1.00 36.77 ? 34 HIS A CA 1 ATOM 195 C C . HIS A 1 36 ? 27.050 11.479 -15.613 1.00 32.95 ? 34 HIS A C 1 ATOM 196 O O . HIS A 1 36 ? 27.914 12.188 -16.142 1.00 31.51 ? 34 HIS A O 1 ATOM 197 C CB . HIS A 1 36 ? 26.203 9.671 -17.049 1.00 38.40 ? 34 HIS A CB 1 ATOM 198 C CG . HIS A 1 36 ? 25.070 8.967 -17.727 1.00 41.35 ? 34 HIS A CG 1 ATOM 199 N ND1 . HIS A 1 36 ? 25.137 7.633 -18.068 1.00 45.46 ? 34 HIS A ND1 1 ATOM 200 C CD2 . HIS A 1 36 ? 23.853 9.398 -18.132 1.00 46.40 ? 34 HIS A CD2 1 ATOM 201 C CE1 . HIS A 1 36 ? 24.024 7.280 -18.693 1.00 49.03 ? 34 HIS A CE1 1 ATOM 202 N NE2 . HIS A 1 36 ? 23.226 8.332 -18.742 1.00 49.32 ? 34 HIS A NE2 1 ATOM 203 N N . VAL A 1 37 ? 27.111 11.049 -14.360 1.00 30.60 ? 35 VAL A N 1 ATOM 204 C CA . VAL A 1 37 ? 28.264 11.242 -13.511 1.00 28.58 ? 35 VAL A CA 1 ATOM 205 C C . VAL A 1 37 ? 29.263 10.097 -13.744 1.00 28.74 ? 35 VAL A C 1 ATOM 206 O O . VAL A 1 37 ? 28.915 8.926 -13.584 1.00 28.38 ? 35 VAL A O 1 ATOM 207 C CB . VAL A 1 37 ? 27.828 11.317 -12.019 1.00 27.53 ? 35 VAL A CB 1 ATOM 208 C CG1 . VAL A 1 37 ? 29.024 11.465 -11.086 1.00 25.02 ? 35 VAL A CG1 1 ATOM 209 C CG2 . VAL A 1 37 ? 26.853 12.492 -11.834 1.00 26.88 ? 35 VAL A CG2 1 ATOM 210 N N . ASP A 1 38 ? 30.491 10.444 -14.135 1.00 28.21 ? 36 ASP A N 1 ATOM 211 C CA . ASP A 1 38 ? 31.567 9.469 -14.259 1.00 29.25 ? 36 ASP A CA 1 ATOM 212 C C . ASP A 1 38 ? 32.276 9.137 -12.918 1.00 28.34 ? 36 ASP A C 1 ATOM 213 O O . ASP A 1 38 ? 32.495 7.980 -12.582 1.00 28.98 ? 36 ASP A O 1 ATOM 214 C CB . ASP A 1 38 ? 32.584 9.954 -15.290 1.00 29.79 ? 36 ASP A CB 1 ATOM 215 C CG . ASP A 1 38 ? 32.424 9.283 -16.630 1.00 34.87 ? 36 ASP A CG 1 ATOM 216 O OD1 . ASP A 1 38 ? 31.500 8.455 -16.801 1.00 42.83 ? 36 ASP A OD1 1 ATOM 217 O OD2 . ASP A 1 38 ? 33.245 9.546 -17.531 1.00 41.87 ? 36 ASP A OD2 1 ATOM 218 N N . ARG A 1 39 ? 32.615 10.168 -12.157 1.00 27.51 ? 37 ARG A N 1 ATOM 219 C CA . ARG A 1 39 ? 33.417 10.039 -10.972 1.00 26.94 ? 37 ARG A CA 1 ATOM 220 C C . ARG A 1 39 ? 32.923 10.981 -9.895 1.00 24.51 ? 37 ARG A C 1 ATOM 221 O O . ARG A 1 39 ? 32.739 12.139 -10.190 1.00 21.40 ? 37 ARG A O 1 ATOM 222 C CB . ARG A 1 39 ? 34.856 10.472 -11.301 1.00 28.45 ? 37 ARG A CB 1 ATOM 223 C CG . ARG A 1 39 ? 35.833 9.408 -11.429 1.00 34.71 ? 37 ARG A CG 1 ATOM 224 C CD . ARG A 1 39 ? 36.077 8.818 -10.083 1.00 40.39 ? 37 ARG A CD 1 ATOM 225 N NE . ARG A 1 39 ? 37.136 9.492 -9.368 1.00 43.62 ? 37 ARG A NE 1 ATOM 226 C CZ . ARG A 1 39 ? 38.291 8.942 -9.060 1.00 48.25 ? 37 ARG A CZ 1 ATOM 227 N NH1 . ARG A 1 39 ? 38.563 7.699 -9.428 1.00 51.72 ? 37 ARG A NH1 1 ATOM 228 N NH2 . ARG A 1 39 ? 39.188 9.654 -8.377 1.00 51.27 ? 37 ARG A NH2 1 ATOM 229 N N . VAL A 1 40 ? 32.760 10.487 -8.657 1.00 23.65 ? 38 VAL A N 1 ATOM 230 C CA . VAL A 1 40 ? 32.586 11.342 -7.472 1.00 23.23 ? 38 VAL A CA 1 ATOM 231 C C . VAL A 1 40 ? 33.443 10.830 -6.342 1.00 23.49 ? 38 VAL A C 1 ATOM 232 O O . VAL A 1 40 ? 33.461 9.619 -6.078 1.00 23.42 ? 38 VAL A O 1 ATOM 233 C CB . VAL A 1 40 ? 31.142 11.368 -6.844 1.00 23.87 ? 38 VAL A CB 1 ATOM 234 C CG1 . VAL A 1 40 ? 30.974 12.688 -6.030 1.00 21.45 ? 38 VAL A CG1 1 ATOM 235 C CG2 . VAL A 1 40 ? 30.069 11.231 -7.850 1.00 24.51 ? 38 VAL A CG2 1 ATOM 236 N N . ASP A 1 41 ? 34.149 11.743 -5.668 1.00 23.92 ? 39 ASP A N 1 ATOM 237 C CA . ASP A 1 41 ? 34.856 11.430 -4.429 1.00 24.21 ? 39 ASP A CA 1 ATOM 238 C C . ASP A 1 41 ? 34.401 12.417 -3.378 1.00 23.38 ? 39 ASP A C 1 ATOM 239 O O . ASP A 1 41 ? 34.311 13.604 -3.658 1.00 23.10 ? 39 ASP A O 1 ATOM 240 C CB . ASP A 1 41 ? 36.356 11.612 -4.538 1.00 26.59 ? 39 ASP A CB 1 ATOM 241 C CG . ASP A 1 41 ? 36.988 10.809 -5.660 1.00 29.66 ? 39 ASP A CG 1 ATOM 242 O OD1 . ASP A 1 41 ? 36.824 9.570 -5.729 1.00 30.86 ? 39 ASP A OD1 1 ATOM 243 O OD2 . ASP A 1 41 ? 37.699 11.460 -6.440 1.00 33.94 ? 39 ASP A OD2 1 ATOM 244 N N . TRP A 1 42 ? 34.108 11.911 -2.180 1.00 21.97 ? 40 TRP A N 1 ATOM 245 C CA . TRP A 1 42 ? 33.858 12.724 -1.005 1.00 21.12 ? 40 TRP A CA 1 ATOM 246 C C . TRP A 1 42 ? 34.927 12.418 0.008 1.00 22.06 ? 40 TRP A C 1 ATOM 247 O O . TRP A 1 42 ? 35.075 11.269 0.393 1.00 21.94 ? 40 TRP A O 1 ATOM 248 C CB . TRP A 1 42 ? 32.518 12.388 -0.388 1.00 20.60 ? 40 TRP A CB 1 ATOM 249 C CG . TRP A 1 42 ? 31.361 12.963 -1.110 1.00 19.51 ? 40 TRP A CG 1 ATOM 250 C CD1 . TRP A 1 42 ? 30.613 12.365 -2.107 1.00 19.80 ? 40 TRP A CD1 1 ATOM 251 C CD2 . TRP A 1 42 ? 30.819 14.253 -0.916 1.00 18.63 ? 40 TRP A CD2 1 ATOM 252 N NE1 . TRP A 1 42 ? 29.639 13.220 -2.531 1.00 20.25 ? 40 TRP A NE1 1 ATOM 253 C CE2 . TRP A 1 42 ? 29.745 14.392 -1.819 1.00 21.05 ? 40 TRP A CE2 1 ATOM 254 C CE3 . TRP A 1 42 ? 31.122 15.315 -0.042 1.00 21.47 ? 40 TRP A CE3 1 ATOM 255 C CZ2 . TRP A 1 42 ? 28.957 15.538 -1.858 1.00 21.96 ? 40 TRP A CZ2 1 ATOM 256 C CZ3 . TRP A 1 42 ? 30.344 16.458 -0.092 1.00 19.90 ? 40 TRP A CZ3 1 ATOM 257 C CH2 . TRP A 1 42 ? 29.281 16.563 -0.991 1.00 22.04 ? 40 TRP A CH2 1 ATOM 258 N N . LEU A 1 43 ? 35.662 13.448 0.429 1.00 23.45 ? 41 LEU A N 1 ATOM 259 C CA . LEU A 1 43 ? 36.789 13.336 1.361 1.00 25.76 ? 41 LEU A CA 1 ATOM 260 C C . LEU A 1 43 ? 36.538 14.200 2.605 1.00 26.06 ? 41 LEU A C 1 ATOM 261 O O . LEU A 1 43 ? 36.092 15.344 2.472 1.00 26.46 ? 41 LEU A O 1 ATOM 262 C CB . LEU A 1 43 ? 38.069 13.903 0.742 1.00 27.53 ? 41 LEU A CB 1 ATOM 263 C CG . LEU A 1 43 ? 39.335 13.129 0.398 1.00 31.90 ? 41 LEU A CG 1 ATOM 264 C CD1 . LEU A 1 43 ? 40.432 14.196 0.350 1.00 36.82 ? 41 LEU A CD1 1 ATOM 265 C CD2 . LEU A 1 43 ? 39.734 11.980 1.314 1.00 27.84 ? 41 LEU A CD2 1 ATOM 266 N N . PHE A 1 44 ? 36.917 13.684 3.774 1.00 26.64 ? 42 PHE A N 1 ATOM 267 C CA . PHE A 1 44 ? 36.727 14.361 5.037 1.00 27.89 ? 42 PHE A CA 1 ATOM 268 C C . PHE A 1 44 ? 38.089 14.766 5.640 1.00 31.74 ? 42 PHE A C 1 ATOM 269 O O . PHE A 1 44 ? 39.047 13.966 5.701 1.00 31.29 ? 42 PHE A O 1 ATOM 270 C CB . PHE A 1 44 ? 35.913 13.483 6.011 1.00 27.25 ? 42 PHE A CB 1 ATOM 271 C CG . PHE A 1 44 ? 35.775 14.067 7.396 1.00 28.13 ? 42 PHE A CG 1 ATOM 272 C CD1 . PHE A 1 44 ? 35.136 15.277 7.598 1.00 26.22 ? 42 PHE A CD1 1 ATOM 273 C CD2 . PHE A 1 44 ? 36.336 13.433 8.494 1.00 31.87 ? 42 PHE A CD2 1 ATOM 274 C CE1 . PHE A 1 44 ? 35.051 15.839 8.886 1.00 27.00 ? 42 PHE A CE1 1 ATOM 275 C CE2 . PHE A 1 44 ? 36.218 13.977 9.784 1.00 31.50 ? 42 PHE A CE2 1 ATOM 276 C CZ . PHE A 1 44 ? 35.579 15.172 9.967 1.00 29.34 ? 42 PHE A CZ 1 ATOM 277 N N . SER A 1 45 ? 38.182 16.027 6.038 1.00 34.66 ? 43 SER A N 1 ATOM 278 C CA . SER A 1 45 ? 39.261 16.488 6.908 1.00 40.00 ? 43 SER A CA 1 ATOM 279 C C . SER A 1 45 ? 38.704 17.299 8.101 1.00 43.46 ? 43 SER A C 1 ATOM 280 O O . SER A 1 45 ? 37.814 18.129 7.927 1.00 41.41 ? 43 SER A O 1 ATOM 281 C CB . SER A 1 45 ? 40.271 17.302 6.107 1.00 41.71 ? 43 SER A CB 1 ATOM 282 O OG . SER A 1 45 ? 39.651 18.087 5.085 1.00 40.50 ? 43 SER A OG 1 ATOM 283 N N . LYS A 1 46 ? 39.230 17.028 9.312 1.00 49.43 ? 44 LYS A N 1 ATOM 284 C CA . LYS A 1 46 ? 38.813 17.721 10.576 1.00 52.42 ? 44 LYS A CA 1 ATOM 285 C C . LYS A 1 46 ? 39.172 19.205 10.667 1.00 56.08 ? 44 LYS A C 1 ATOM 286 O O . LYS A 1 46 ? 38.277 20.033 10.907 1.00 57.09 ? 44 LYS A O 1 ATOM 287 C CB . LYS A 1 46 ? 39.259 16.958 11.833 1.00 54.52 ? 44 LYS A CB 1 ATOM 288 C CG . LYS A 1 46 ? 38.247 15.863 12.167 1.00 54.29 ? 44 LYS A CG 1 ATOM 289 C CD . LYS A 1 46 ? 38.674 14.866 13.243 1.00 57.76 ? 44 LYS A CD 1 ATOM 290 C CE . LYS A 1 46 ? 37.536 13.834 13.459 1.00 56.84 ? 44 LYS A CE 1 ATOM 291 N NZ . LYS A 1 46 ? 37.928 12.385 13.372 1.00 58.09 ? 44 LYS A NZ 1 ATOM 292 N N . ASP A 1 47 ? 40.432 19.574 10.510 1.00 60.21 ? 45 ASP A N 1 ATOM 293 C CA . ASP A 1 47 ? 40.737 20.945 10.043 1.00 63.33 ? 45 ASP A CA 1 ATOM 294 C C . ASP A 1 47 ? 41.201 20.668 8.628 1.00 62.68 ? 45 ASP A C 1 ATOM 295 O O . ASP A 1 47 ? 40.483 19.965 7.904 1.00 61.50 ? 45 ASP A O 1 ATOM 296 C CB . ASP A 1 47 ? 41.714 21.796 10.937 1.00 68.03 ? 45 ASP A CB 1 ATOM 297 C CG . ASP A 1 47 ? 42.426 21.000 12.051 1.00 72.26 ? 45 ASP A CG 1 ATOM 298 O OD1 . ASP A 1 47 ? 41.762 20.622 13.051 1.00 74.40 ? 45 ASP A OD1 1 ATOM 299 O OD2 . ASP A 1 47 ? 43.673 20.839 11.975 1.00 77.27 ? 45 ASP A OD2 1 ATOM 300 N N . LYS A 1 48 ? 42.343 21.184 8.184 1.00 65.64 ? 46 LYS A N 1 ATOM 301 C CA . LYS A 1 48 ? 43.086 20.424 7.178 1.00 65.07 ? 46 LYS A CA 1 ATOM 302 C C . LYS A 1 48 ? 43.405 19.186 8.003 1.00 64.88 ? 46 LYS A C 1 ATOM 303 O O . LYS A 1 48 ? 42.963 18.075 7.663 1.00 62.34 ? 46 LYS A O 1 ATOM 304 C CB . LYS A 1 48 ? 44.364 21.109 6.707 1.00 68.61 ? 46 LYS A CB 1 ATOM 305 C CG . LYS A 1 48 ? 45.143 20.263 5.689 1.00 69.13 ? 46 LYS A CG 1 ATOM 306 C CD . LYS A 1 48 ? 46.628 20.553 5.675 1.00 74.08 ? 46 LYS A CD 1 ATOM 307 C CE . LYS A 1 48 ? 46.991 21.698 4.723 1.00 76.43 ? 46 LYS A CE 1 ATOM 308 N NZ . LYS A 1 48 ? 48.382 22.178 4.989 1.00 80.37 ? 46 LYS A NZ 1 ATOM 309 N N . ASP A 1 49 ? 44.098 19.443 9.134 1.00 66.97 ? 47 ASP A N 1 ATOM 310 C CA . ASP A 1 49 ? 44.392 18.466 10.197 1.00 67.01 ? 47 ASP A CA 1 ATOM 311 C C . ASP A 1 49 ? 45.733 17.888 9.889 1.00 67.82 ? 47 ASP A C 1 ATOM 312 O O . ASP A 1 49 ? 46.280 17.103 10.659 1.00 71.01 ? 47 ASP A O 1 ATOM 313 C CB . ASP A 1 49 ? 43.327 17.333 10.297 1.00 63.49 ? 47 ASP A CB 1 ATOM 314 C CG . ASP A 1 49 ? 43.505 16.465 11.541 1.00 66.49 ? 47 ASP A CG 1 ATOM 315 O OD1 . ASP A 1 49 ? 44.273 16.867 12.427 1.00 72.04 ? 47 ASP A OD1 1 ATOM 316 O OD2 . ASP A 1 49 ? 42.888 15.387 11.649 1.00 66.48 ? 47 ASP A OD2 1 ATOM 317 N N . ASP A 1 50 ? 46.278 18.293 8.753 1.00 65.84 ? 48 ASP A N 1 ATOM 318 C CA . ASP A 1 50 ? 47.169 17.416 8.000 1.00 64.70 ? 48 ASP A CA 1 ATOM 319 C C . ASP A 1 50 ? 46.684 15.999 7.648 1.00 59.36 ? 48 ASP A C 1 ATOM 320 O O . ASP A 1 50 ? 47.418 15.244 7.031 1.00 61.11 ? 48 ASP A O 1 ATOM 321 C CB . ASP A 1 50 ? 48.688 17.770 8.085 1.00 69.47 ? 48 ASP A CB 1 ATOM 322 C CG . ASP A 1 50 ? 49.443 17.658 6.738 1.00 71.12 ? 48 ASP A CG 1 ATOM 323 O OD1 . ASP A 1 50 ? 48.822 17.681 5.646 1.00 66.06 ? 48 ASP A OD1 1 ATOM 324 O OD2 . ASP A 1 50 ? 50.710 17.586 6.797 1.00 76.63 ? 48 ASP A OD2 1 ATOM 325 N N . ALA A 1 51 ? 45.441 15.655 8.026 1.00 52.87 ? 49 ALA A N 1 ATOM 326 C CA . ALA A 1 51 ? 44.856 14.352 7.674 1.00 48.43 ? 49 ALA A CA 1 ATOM 327 C C . ALA A 1 51 ? 43.473 14.390 7.010 1.00 42.38 ? 49 ALA A C 1 ATOM 328 O O . ALA A 1 51 ? 42.605 15.230 7.274 1.00 41.07 ? 49 ALA A O 1 ATOM 329 C CB . ALA A 1 51 ? 44.831 13.433 8.869 1.00 49.14 ? 49 ALA A CB 1 ATOM 330 N N . SER A 1 52 ? 43.269 13.427 6.142 1.00 38.91 ? 50 SER A N 1 ATOM 331 C CA . SER A 1 52 ? 41.993 13.194 5.551 1.00 34.72 ? 50 SER A CA 1 ATOM 332 C C . SER A 1 52 ? 41.603 11.719 5.528 1.00 33.20 ? 50 SER A C 1 ATOM 333 O O . SER A 1 52 ? 42.404 10.834 5.750 1.00 34.18 ? 50 SER A O 1 ATOM 334 C CB . SER A 1 52 ? 41.961 13.739 4.141 1.00 32.85 ? 50 SER A CB 1 ATOM 335 O OG . SER A 1 52 ? 43.074 13.234 3.500 1.00 39.25 ? 50 SER A OG 1 ATOM 336 N N . GLU A 1 53 ? 40.338 11.490 5.226 1.00 30.92 ? 51 GLU A N 1 ATOM 337 C CA . GLU A 1 53 ? 39.804 10.159 5.087 1.00 31.65 ? 51 GLU A CA 1 ATOM 338 C C . GLU A 1 53 ? 38.667 10.174 4.108 1.00 27.96 ? 51 GLU A C 1 ATOM 339 O O . GLU A 1 53 ? 37.949 11.159 3.988 1.00 26.29 ? 51 GLU A O 1 ATOM 340 C CB . GLU A 1 53 ? 39.394 9.553 6.446 1.00 33.65 ? 51 GLU A CB 1 ATOM 341 C CG . GLU A 1 53 ? 38.382 10.293 7.235 1.00 37.00 ? 51 GLU A CG 1 ATOM 342 C CD . GLU A 1 53 ? 38.347 9.828 8.736 1.00 44.79 ? 51 GLU A CD 1 ATOM 343 O OE1 . GLU A 1 53 ? 38.289 8.604 9.006 1.00 47.72 ? 51 GLU A OE1 1 ATOM 344 O OE2 . GLU A 1 53 ? 38.367 10.698 9.638 1.00 47.01 ? 51 GLU A OE2 1 ATOM 345 N N . TYR A 1 54 ? 38.529 9.092 3.358 1.00 28.12 ? 52 TYR A N 1 ATOM 346 C CA . TYR A 1 54 ? 37.397 8.950 2.421 1.00 27.34 ? 52 TYR A CA 1 ATOM 347 C C . TYR A 1 54 ? 36.086 8.699 3.124 1.00 26.07 ? 52 TYR A C 1 ATOM 348 O O . TYR A 1 54 ? 36.004 7.952 4.069 1.00 25.84 ? 52 TYR A O 1 ATOM 349 C CB . TYR A 1 54 ? 37.655 7.872 1.365 1.00 29.01 ? 52 TYR A CB 1 ATOM 350 C CG . TYR A 1 54 ? 38.442 8.408 0.210 1.00 30.49 ? 52 TYR A CG 1 ATOM 351 C CD1 . TYR A 1 54 ? 39.828 8.401 0.244 1.00 33.51 ? 52 TYR A CD1 1 ATOM 352 C CD2 . TYR A 1 54 ? 37.805 8.978 -0.893 1.00 31.84 ? 52 TYR A CD2 1 ATOM 353 C CE1 . TYR A 1 54 ? 40.581 8.915 -0.784 1.00 35.26 ? 52 TYR A CE1 1 ATOM 354 C CE2 . TYR A 1 54 ? 38.568 9.510 -1.962 1.00 34.36 ? 52 TYR A CE2 1 ATOM 355 C CZ . TYR A 1 54 ? 39.955 9.464 -1.880 1.00 36.23 ? 52 TYR A CZ 1 ATOM 356 O OH . TYR A 1 54 ? 40.754 9.965 -2.883 1.00 41.39 ? 52 TYR A OH 1 ATOM 357 N N . VAL A 1 55 ? 35.062 9.396 2.654 1.00 25.00 ? 53 VAL A N 1 ATOM 358 C CA . VAL A 1 55 ? 33.699 9.146 3.066 1.00 24.57 ? 53 VAL A CA 1 ATOM 359 C C . VAL A 1 55 ? 33.136 8.115 2.049 1.00 25.87 ? 53 VAL A C 1 ATOM 360 O O . VAL A 1 55 ? 32.618 7.042 2.410 1.00 25.65 ? 53 VAL A O 1 ATOM 361 C CB . VAL A 1 55 ? 32.914 10.451 3.128 1.00 23.55 ? 53 VAL A CB 1 ATOM 362 C CG1 . VAL A 1 55 ? 31.416 10.175 3.397 1.00 23.07 ? 53 VAL A CG1 1 ATOM 363 C CG2 . VAL A 1 55 ? 33.511 11.367 4.220 1.00 23.67 ? 53 VAL A CG2 1 ATOM 364 N N . LEU A 1 56 ? 33.323 8.429 0.775 1.00 25.80 ? 54 LEU A N 1 ATOM 365 C CA . LEU A 1 56 ? 32.822 7.590 -0.294 1.00 26.87 ? 54 LEU A CA 1 ATOM 366 C C . LEU A 1 56 ? 33.556 7.964 -1.585 1.00 25.86 ? 54 LEU A C 1 ATOM 367 O O . LEU A 1 56 ? 33.925 9.133 -1.766 1.00 23.39 ? 54 LEU A O 1 ATOM 368 C CB . LEU A 1 56 ? 31.299 7.808 -0.390 1.00 26.01 ? 54 LEU A CB 1 ATOM 369 C CG . LEU A 1 56 ? 30.441 7.388 -1.570 1.00 28.69 ? 54 LEU A CG 1 ATOM 370 C CD1 . LEU A 1 56 ? 28.982 7.340 -1.047 1.00 28.40 ? 54 LEU A CD1 1 ATOM 371 C CD2 . LEU A 1 56 ? 30.597 8.317 -2.794 1.00 27.52 ? 54 LEU A CD2 1 ATOM 372 N N . PHE A 1 57 ? 33.814 6.955 -2.424 1.00 26.80 ? 55 PHE A N 1 ATOM 373 C CA . PHE A 1 57 ? 34.177 7.176 -3.811 1.00 27.53 ? 55 PHE A CA 1 ATOM 374 C C . PHE A 1 57 ? 33.264 6.416 -4.772 1.00 27.52 ? 55 PHE A C 1 ATOM 375 O O . PHE A 1 57 ? 32.607 5.458 -4.393 1.00 29.70 ? 55 PHE A O 1 ATOM 376 C CB . PHE A 1 57 ? 35.691 6.995 -4.106 1.00 29.94 ? 55 PHE A CB 1 ATOM 377 C CG . PHE A 1 57 ? 36.245 5.620 -3.876 1.00 32.61 ? 55 PHE A CG 1 ATOM 378 C CD1 . PHE A 1 57 ? 36.424 5.123 -2.591 1.00 35.62 ? 55 PHE A CD1 1 ATOM 379 C CD2 . PHE A 1 57 ? 36.716 4.863 -4.955 1.00 37.95 ? 55 PHE A CD2 1 ATOM 380 C CE1 . PHE A 1 57 ? 36.992 3.860 -2.369 1.00 36.21 ? 55 PHE A CE1 1 ATOM 381 C CE2 . PHE A 1 57 ? 37.311 3.605 -4.746 1.00 39.07 ? 55 PHE A CE2 1 ATOM 382 C CZ . PHE A 1 57 ? 37.420 3.105 -3.429 1.00 41.00 ? 55 PHE A CZ 1 ATOM 383 N N . TYR A 1 58 ? 33.185 6.903 -5.997 1.00 26.49 ? 56 TYR A N 1 ATOM 384 C CA . TYR A 1 58 ? 32.326 6.347 -7.023 1.00 27.20 ? 56 TYR A CA 1 ATOM 385 C C . TYR A 1 58 ? 33.061 6.436 -8.337 1.00 27.77 ? 56 TYR A C 1 ATOM 386 O O . TYR A 1 58 ? 33.582 7.469 -8.664 1.00 24.58 ? 56 TYR A O 1 ATOM 387 C CB . TYR A 1 58 ? 31.000 7.122 -7.046 1.00 27.32 ? 56 TYR A CB 1 ATOM 388 C CG . TYR A 1 58 ? 30.135 6.904 -8.252 1.00 27.62 ? 56 TYR A CG 1 ATOM 389 C CD1 . TYR A 1 58 ? 30.310 7.677 -9.403 1.00 28.81 ? 56 TYR A CD1 1 ATOM 390 C CD2 . TYR A 1 58 ? 29.103 5.962 -8.240 1.00 29.41 ? 56 TYR A CD2 1 ATOM 391 C CE1 . TYR A 1 58 ? 29.513 7.477 -10.535 1.00 29.03 ? 56 TYR A CE1 1 ATOM 392 C CE2 . TYR A 1 58 ? 28.295 5.773 -9.341 1.00 31.20 ? 56 TYR A CE2 1 ATOM 393 C CZ . TYR A 1 58 ? 28.506 6.546 -10.488 1.00 30.10 ? 56 TYR A CZ 1 ATOM 394 O OH . TYR A 1 58 ? 27.709 6.384 -11.572 1.00 34.38 ? 56 TYR A OH 1 ATOM 395 N N . TYR A 1 59 ? 33.142 5.301 -9.042 1.00 29.98 ? 57 TYR A N 1 ATOM 396 C CA . TYR A 1 59 ? 33.732 5.192 -10.351 1.00 31.16 ? 57 TYR A CA 1 ATOM 397 C C . TYR A 1 59 ? 33.089 3.969 -11.002 1.00 33.44 ? 57 TYR A C 1 ATOM 398 O O . TYR A 1 59 ? 32.641 3.065 -10.306 1.00 33.99 ? 57 TYR A O 1 ATOM 399 C CB . TYR A 1 59 ? 35.255 4.989 -10.255 1.00 32.30 ? 57 TYR A CB 1 ATOM 400 C CG . TYR A 1 59 ? 35.636 3.639 -9.713 1.00 34.02 ? 57 TYR A CG 1 ATOM 401 C CD1 . TYR A 1 59 ? 35.610 3.392 -8.354 1.00 34.67 ? 57 TYR A CD1 1 ATOM 402 C CD2 . TYR A 1 59 ? 35.981 2.608 -10.556 1.00 36.67 ? 57 TYR A CD2 1 ATOM 403 C CE1 . TYR A 1 59 ? 35.924 2.143 -7.857 1.00 37.33 ? 57 TYR A CE1 1 ATOM 404 C CE2 . TYR A 1 59 ? 36.297 1.351 -10.066 1.00 39.73 ? 57 TYR A CE2 1 ATOM 405 C CZ . TYR A 1 59 ? 36.270 1.136 -8.708 1.00 39.36 ? 57 TYR A CZ 1 ATOM 406 O OH . TYR A 1 59 ? 36.576 -0.105 -8.207 1.00 43.61 ? 57 TYR A OH 1 ATOM 407 N N . SER A 1 60 ? 33.057 3.951 -12.328 1.00 34.88 ? 58 SER A N 1 ATOM 408 C CA . SER A 1 60 ? 32.498 2.842 -13.109 1.00 37.87 ? 58 SER A CA 1 ATOM 409 C C . SER A 1 60 ? 31.153 2.378 -12.617 1.00 38.66 ? 58 SER A C 1 ATOM 410 O O . SER A 1 60 ? 30.929 1.191 -12.477 1.00 41.01 ? 58 SER A O 1 ATOM 411 C CB . SER A 1 60 ? 33.498 1.679 -13.200 1.00 39.81 ? 58 SER A CB 1 ATOM 412 O OG . SER A 1 60 ? 34.720 2.152 -13.759 1.00 41.88 ? 58 SER A OG 1 ATOM 413 N N . ASN A 1 61 ? 30.262 3.329 -12.350 1.00 39.11 ? 59 ASN A N 1 ATOM 414 C CA . ASN A 1 61 ? 28.858 3.061 -11.931 1.00 41.21 ? 59 ASN A CA 1 ATOM 415 C C . ASN A 1 61 ? 28.698 2.372 -10.567 1.00 41.31 ? 59 ASN A C 1 ATOM 416 O O . ASN A 1 61 ? 27.644 1.793 -10.271 1.00 42.91 ? 59 ASN A O 1 ATOM 417 C CB . ASN A 1 61 ? 28.079 2.289 -13.026 1.00 45.01 ? 59 ASN A CB 1 ATOM 418 C CG . ASN A 1 61 ? 27.854 3.116 -14.297 1.00 49.31 ? 59 ASN A CG 1 ATOM 419 O OD1 . ASN A 1 61 ? 27.877 4.345 -14.264 1.00 45.64 ? 59 ASN A OD1 1 ATOM 420 N ND2 . ASN A 1 61 ? 27.623 2.425 -15.421 1.00 61.45 ? 59 ASN A ND2 1 ATOM 421 N N . LEU A 1 62 ? 29.713 2.476 -9.712 1.00 40.23 ? 60 LEU A N 1 ATOM 422 C CA . LEU A 1 62 ? 29.615 1.885 -8.383 1.00 41.06 ? 60 LEU A CA 1 ATOM 423 C C . LEU A 1 62 ? 30.080 2.824 -7.270 1.00 37.54 ? 60 LEU A C 1 ATOM 424 O O . LEU A 1 62 ? 31.155 3.391 -7.361 1.00 35.26 ? 60 LEU A O 1 ATOM 425 C CB . LEU A 1 62 ? 30.338 0.524 -8.361 1.00 44.41 ? 60 LEU A CB 1 ATOM 426 C CG . LEU A 1 62 ? 31.861 0.349 -8.320 1.00 47.10 ? 60 LEU A CG 1 ATOM 427 C CD1 . LEU A 1 62 ? 32.254 -0.276 -6.957 1.00 53.13 ? 60 LEU A CD1 1 ATOM 428 C CD2 . LEU A 1 62 ? 32.357 -0.588 -9.452 1.00 50.43 ? 60 LEU A CD2 1 ATOM 429 N N . SER A 1 63 ? 29.240 3.038 -6.251 1.00 36.51 ? 61 SER A N 1 ATOM 430 C CA . SER A 1 63 ? 29.678 3.790 -5.086 1.00 35.57 ? 61 SER A CA 1 ATOM 431 C C . SER A 1 63 ? 30.248 2.854 -4.079 1.00 36.47 ? 61 SER A C 1 ATOM 432 O O . SER A 1 63 ? 29.773 1.741 -3.906 1.00 38.88 ? 61 SER A O 1 ATOM 433 C CB . SER A 1 63 ? 28.589 4.653 -4.435 1.00 33.76 ? 61 SER A CB 1 ATOM 434 O OG . SER A 1 63 ? 27.335 4.107 -4.638 1.00 39.22 ? 61 SER A OG 1 ATOM 435 N N . VAL A 1 64 ? 31.283 3.333 -3.406 1.00 36.11 ? 62 VAL A N 1 ATOM 436 C CA . VAL A 1 64 ? 31.909 2.580 -2.348 1.00 37.42 ? 62 VAL A CA 1 ATOM 437 C C . VAL A 1 64 ? 32.114 3.476 -1.113 1.00 35.07 ? 62 VAL A C 1 ATOM 438 O O . VAL A 1 64 ? 33.165 4.141 -0.967 1.00 34.49 ? 62 VAL A O 1 ATOM 439 C CB . VAL A 1 64 ? 33.167 1.771 -2.839 1.00 39.07 ? 62 VAL A CB 1 ATOM 440 C CG1 . VAL A 1 64 ? 33.575 2.146 -4.275 1.00 41.69 ? 62 VAL A CG1 1 ATOM 441 C CG2 . VAL A 1 64 ? 34.335 1.848 -1.865 1.00 40.57 ? 62 VAL A CG2 1 ATOM 442 N N A PRO A 1 65 ? 31.097 3.526 -0.240 0.50 34.42 ? 63 PRO A N 1 ATOM 443 N N B PRO A 1 65 ? 31.097 3.520 -0.231 0.50 34.37 ? 63 PRO A N 1 ATOM 444 C CA A PRO A 1 65 ? 31.260 4.097 1.100 0.50 33.40 ? 63 PRO A CA 1 ATOM 445 C CA B PRO A 1 65 ? 31.316 4.177 1.056 0.50 33.19 ? 63 PRO A CA 1 ATOM 446 C C A PRO A 1 65 ? 32.407 3.393 1.821 0.50 34.66 ? 63 PRO A C 1 ATOM 447 C C B PRO A 1 65 ? 32.392 3.414 1.822 0.50 34.58 ? 63 PRO A C 1 ATOM 448 O O A PRO A 1 65 ? 32.581 2.174 1.661 0.50 35.74 ? 63 PRO A O 1 ATOM 449 O O B PRO A 1 65 ? 32.501 2.185 1.695 0.50 35.75 ? 63 PRO A O 1 ATOM 450 C CB A PRO A 1 65 ? 29.912 3.812 1.776 0.50 34.01 ? 63 PRO A CB 1 ATOM 451 C CB B PRO A 1 65 ? 29.940 4.106 1.740 0.50 33.36 ? 63 PRO A CB 1 ATOM 452 C CG A PRO A 1 65 ? 28.946 3.666 0.650 0.50 34.26 ? 63 PRO A CG 1 ATOM 453 C CG B PRO A 1 65 ? 29.255 2.956 1.091 0.50 35.30 ? 63 PRO A CG 1 ATOM 454 C CD A PRO A 1 65 ? 29.721 3.053 -0.475 0.50 35.09 ? 63 PRO A CD 1 ATOM 455 C CD B PRO A 1 65 ? 29.730 2.975 -0.338 0.50 35.18 ? 63 PRO A CD 1 ATOM 456 N N . THR A 1 66 ? 33.203 4.159 2.571 1.00 33.51 ? 64 THR A N 1 ATOM 457 C CA . THR A 1 66 ? 34.481 3.651 3.086 1.00 35.24 ? 64 THR A CA 1 ATOM 458 C C . THR A 1 66 ? 34.651 4.001 4.546 1.00 34.54 ? 64 THR A C 1 ATOM 459 O O . THR A 1 66 ? 34.090 4.990 5.025 1.00 31.79 ? 64 THR A O 1 ATOM 460 C CB . THR A 1 66 ? 35.722 4.285 2.337 1.00 34.84 ? 64 THR A CB 1 ATOM 461 O OG1 . THR A 1 66 ? 35.728 5.687 2.577 1.00 35.29 ? 64 THR A OG1 1 ATOM 462 C CG2 . THR A 1 66 ? 35.674 4.089 0.843 1.00 34.48 ? 64 THR A CG2 1 ATOM 463 N N . GLY A 1 67 ? 35.443 3.178 5.218 1.00 36.14 ? 65 GLY A N 1 ATOM 464 C CA . GLY A 1 67 ? 35.965 3.480 6.535 1.00 37.86 ? 65 GLY A CA 1 ATOM 465 C C . GLY A 1 67 ? 34.904 3.622 7.596 1.00 37.58 ? 65 GLY A C 1 ATOM 466 O O . GLY A 1 67 ? 33.951 2.847 7.656 1.00 37.43 ? 65 GLY A O 1 ATOM 467 N N . ARG A 1 68 ? 35.056 4.633 8.429 1.00 37.29 ? 66 ARG A N 1 ATOM 468 C CA . ARG A 1 68 ? 34.094 4.838 9.464 1.00 38.07 ? 66 ARG A CA 1 ATOM 469 C C . ARG A 1 68 ? 32.807 5.445 8.948 1.00 35.11 ? 66 ARG A C 1 ATOM 470 O O . ARG A 1 68 ? 31.877 5.629 9.693 1.00 35.84 ? 66 ARG A O 1 ATOM 471 C CB . ARG A 1 68 ? 34.692 5.632 10.607 1.00 39.61 ? 66 ARG A CB 1 ATOM 472 C CG . ARG A 1 68 ? 34.919 7.056 10.310 1.00 38.96 ? 66 ARG A CG 1 ATOM 473 C CD . ARG A 1 68 ? 35.724 7.644 11.422 1.00 41.68 ? 66 ARG A CD 1 ATOM 474 N NE . ARG A 1 68 ? 35.893 9.039 11.110 1.00 41.11 ? 66 ARG A NE 1 ATOM 475 C CZ . ARG A 1 68 ? 35.019 9.982 11.383 1.00 39.68 ? 66 ARG A CZ 1 ATOM 476 N NH1 . ARG A 1 68 ? 33.918 9.716 12.066 1.00 41.70 ? 66 ARG A NH1 1 ATOM 477 N NH2 . ARG A 1 68 ? 35.285 11.218 10.992 1.00 40.07 ? 66 ARG A NH2 1 ATOM 478 N N . PHE A 1 69 ? 32.729 5.691 7.656 1.00 33.90 ? 67 PHE A N 1 ATOM 479 C CA . PHE A 1 69 ? 31.503 6.157 7.046 1.00 31.80 ? 67 PHE A CA 1 ATOM 480 C C . PHE A 1 69 ? 30.775 5.014 6.333 1.00 32.92 ? 67 PHE A C 1 ATOM 481 O O . PHE A 1 69 ? 29.721 5.216 5.750 1.00 32.33 ? 67 PHE A O 1 ATOM 482 C CB . PHE A 1 69 ? 31.825 7.283 6.057 1.00 29.85 ? 67 PHE A CB 1 ATOM 483 C CG . PHE A 1 69 ? 32.476 8.495 6.694 1.00 28.61 ? 67 PHE A CG 1 ATOM 484 C CD1 . PHE A 1 69 ? 31.699 9.494 7.265 1.00 25.53 ? 67 PHE A CD1 1 ATOM 485 C CD2 . PHE A 1 69 ? 33.858 8.621 6.746 1.00 29.44 ? 67 PHE A CD2 1 ATOM 486 C CE1 . PHE A 1 69 ? 32.263 10.614 7.823 1.00 26.17 ? 67 PHE A CE1 1 ATOM 487 C CE2 . PHE A 1 69 ? 34.432 9.752 7.338 1.00 29.06 ? 67 PHE A CE2 1 ATOM 488 C CZ . PHE A 1 69 ? 33.626 10.742 7.882 1.00 27.25 ? 67 PHE A CZ 1 ATOM 489 N N . GLN A 1 70 ? 31.312 3.812 6.423 1.00 35.41 ? 68 GLN A N 1 ATOM 490 C CA . GLN A 1 70 ? 30.949 2.746 5.511 1.00 38.07 ? 68 GLN A CA 1 ATOM 491 C C . GLN A 1 70 ? 29.473 2.374 5.594 1.00 39.04 ? 68 GLN A C 1 ATOM 492 O O . GLN A 1 70 ? 28.887 1.946 4.599 1.00 40.55 ? 68 GLN A O 1 ATOM 493 C CB . GLN A 1 70 ? 31.834 1.510 5.759 1.00 41.12 ? 68 GLN A CB 1 ATOM 494 C CG . GLN A 1 70 ? 31.738 0.469 4.641 1.00 44.49 ? 68 GLN A CG 1 ATOM 495 C CD . GLN A 1 70 ? 32.422 -0.843 4.945 1.00 48.78 ? 68 GLN A CD 1 ATOM 496 O OE1 . GLN A 1 70 ? 32.793 -1.125 6.081 1.00 52.27 ? 68 GLN A OE1 1 ATOM 497 N NE2 . GLN A 1 70 ? 32.581 -1.666 3.915 1.00 50.93 ? 68 GLN A NE2 1 ATOM 498 N N . ASN A 1 71 ? 28.881 2.531 6.772 1.00 39.60 ? 69 ASN A N 1 ATOM 499 C CA . ASN A 1 71 ? 27.500 2.168 6.980 1.00 41.82 ? 69 ASN A CA 1 ATOM 500 C C . ASN A 1 71 ? 26.522 3.327 7.135 1.00 38.26 ? 69 ASN A C 1 ATOM 501 O O . ASN A 1 71 ? 25.341 3.096 7.293 1.00 39.57 ? 69 ASN A O 1 ATOM 502 C CB . ASN A 1 71 ? 27.403 1.217 8.172 1.00 45.67 ? 69 ASN A CB 1 ATOM 503 C CG . ASN A 1 71 ? 27.310 -0.242 7.731 1.00 55.64 ? 69 ASN A CG 1 ATOM 504 O OD1 . ASN A 1 71 ? 28.236 -0.762 7.076 1.00 58.97 ? 69 ASN A OD1 1 ATOM 505 N ND2 . ASN A 1 71 ? 26.196 -0.929 8.090 1.00 69.29 ? 69 ASN A ND2 1 ATOM 506 N N . ARG A 1 72 ? 27.013 4.551 7.035 1.00 34.37 ? 70 ARG A N 1 ATOM 507 C CA . ARG A 1 72 ? 26.243 5.750 7.331 1.00 32.07 ? 70 ARG A CA 1 ATOM 508 C C . ARG A 1 72 ? 26.174 6.673 6.138 1.00 29.26 ? 70 ARG A C 1 ATOM 509 O O . ARG A 1 72 ? 25.556 7.701 6.225 1.00 27.97 ? 70 ARG A O 1 ATOM 510 C CB . ARG A 1 72 ? 26.944 6.558 8.446 1.00 31.38 ? 70 ARG A CB 1 ATOM 511 C CG . ARG A 1 72 ? 27.135 5.822 9.715 1.00 34.55 ? 70 ARG A CG 1 ATOM 512 C CD . ARG A 1 72 ? 27.534 6.715 10.872 1.00 34.31 ? 70 ARG A CD 1 ATOM 513 N NE . ARG A 1 72 ? 28.925 7.145 10.803 1.00 35.10 ? 70 ARG A NE 1 ATOM 514 C CZ . ARG A 1 72 ? 29.353 8.405 10.770 1.00 35.31 ? 70 ARG A CZ 1 ATOM 515 N NH1 . ARG A 1 72 ? 28.505 9.424 10.779 1.00 33.71 ? 70 ARG A NH1 1 ATOM 516 N NH2 . ARG A 1 72 ? 30.658 8.635 10.719 1.00 37.19 ? 70 ARG A NH2 1 ATOM 517 N N . SER A 1 73 ? 26.856 6.349 5.046 1.00 29.09 ? 71 SER A N 1 ATOM 518 C CA . SER A 1 73 ? 27.034 7.306 3.961 1.00 27.19 ? 71 SER A CA 1 ATOM 519 C C . SER A 1 73 ? 26.544 6.729 2.635 1.00 27.15 ? 71 SER A C 1 ATOM 520 O O . SER A 1 73 ? 26.644 5.527 2.390 1.00 28.71 ? 71 SER A O 1 ATOM 521 C CB . SER A 1 73 ? 28.490 7.796 3.894 1.00 26.06 ? 71 SER A CB 1 ATOM 522 O OG . SER A 1 73 ? 29.347 6.848 3.285 1.00 28.55 ? 71 SER A OG 1 ATOM 523 N N . HIS A 1 74 ? 25.961 7.586 1.795 1.00 26.06 ? 72 HIS A N 1 ATOM 524 C CA . HIS A 1 74 ? 25.237 7.115 0.605 1.00 27.01 ? 72 HIS A CA 1 ATOM 525 C C . HIS A 1 74 ? 25.267 8.191 -0.426 1.00 26.39 ? 72 HIS A C 1 ATOM 526 O O . HIS A 1 74 ? 25.092 9.360 -0.111 1.00 25.11 ? 72 HIS A O 1 ATOM 527 C CB . HIS A 1 74 ? 23.754 6.784 0.913 1.00 27.89 ? 72 HIS A CB 1 ATOM 528 C CG . HIS A 1 74 ? 23.541 5.993 2.168 1.00 28.58 ? 72 HIS A CG 1 ATOM 529 N ND1 . HIS A 1 74 ? 23.406 4.622 2.171 1.00 31.01 ? 72 HIS A ND1 1 ATOM 530 C CD2 . HIS A 1 74 ? 23.401 6.388 3.458 1.00 27.94 ? 72 HIS A CD2 1 ATOM 531 C CE1 . HIS A 1 74 ? 23.200 4.204 3.405 1.00 30.44 ? 72 HIS A CE1 1 ATOM 532 N NE2 . HIS A 1 74 ? 23.188 5.255 4.208 1.00 31.79 ? 72 HIS A NE2 1 ATOM 533 N N . LEU A 1 75 ? 25.458 7.774 -1.666 1.00 27.76 ? 73 LEU A N 1 ATOM 534 C CA . LEU A 1 75 ? 25.412 8.656 -2.816 1.00 28.00 ? 73 LEU A CA 1 ATOM 535 C C . LEU A 1 75 ? 23.968 8.697 -3.178 1.00 28.88 ? 73 LEU A C 1 ATOM 536 O O . LEU A 1 75 ? 23.434 7.723 -3.656 1.00 30.44 ? 73 LEU A O 1 ATOM 537 C CB . LEU A 1 75 ? 26.255 8.080 -3.973 1.00 28.96 ? 73 LEU A CB 1 ATOM 538 C CG . LEU A 1 75 ? 26.654 8.974 -5.152 1.00 30.70 ? 73 LEU A CG 1 ATOM 539 C CD1 . LEU A 1 75 ? 27.528 10.102 -4.647 1.00 28.24 ? 73 LEU A CD1 1 ATOM 540 C CD2 . LEU A 1 75 ? 27.408 8.216 -6.258 1.00 29.93 ? 73 LEU A CD2 1 ATOM 541 N N . VAL A 1 76 ? 23.317 9.824 -2.923 1.00 29.09 ? 74 VAL A N 1 ATOM 542 C CA . VAL A 1 76 ? 21.865 9.944 -3.153 1.00 30.56 ? 74 VAL A CA 1 ATOM 543 C C . VAL A 1 76 ? 21.569 10.815 -4.359 1.00 31.94 ? 74 VAL A C 1 ATOM 544 O O . VAL A 1 76 ? 20.452 10.932 -4.784 1.00 34.49 ? 74 VAL A O 1 ATOM 545 C CB . VAL A 1 76 ? 21.133 10.496 -1.901 1.00 30.83 ? 74 VAL A CB 1 ATOM 546 C CG1 . VAL A 1 76 ? 21.246 9.495 -0.754 1.00 30.22 ? 74 VAL A CG1 1 ATOM 547 C CG2 . VAL A 1 76 ? 21.685 11.881 -1.467 1.00 27.86 ? 74 VAL A CG2 1 ATOM 548 N N . GLY A 1 77 ? 22.582 11.423 -4.930 1.00 32.25 ? 75 GLY A N 1 ATOM 549 C CA . GLY A 1 77 ? 22.372 12.209 -6.104 1.00 33.86 ? 75 GLY A CA 1 ATOM 550 C C . GLY A 1 77 ? 21.988 11.345 -7.275 1.00 35.43 ? 75 GLY A C 1 ATOM 551 O O . GLY A 1 77 ? 22.394 10.190 -7.345 1.00 36.77 ? 75 GLY A O 1 ATOM 552 N N . ASP A 1 78 ? 21.207 11.908 -8.185 1.00 36.68 ? 76 ASP A N 1 ATOM 553 C CA . ASP A 1 78 ? 20.914 11.268 -9.468 1.00 38.07 ? 76 ASP A CA 1 ATOM 554 C C . ASP A 1 78 ? 22.162 11.250 -10.366 1.00 36.36 ? 76 ASP A C 1 ATOM 555 O O . ASP A 1 78 ? 22.479 12.234 -11.035 1.00 35.76 ? 76 ASP A O 1 ATOM 556 C CB . ASP A 1 78 ? 19.803 12.031 -10.159 1.00 40.75 ? 76 ASP A CB 1 ATOM 557 C CG . ASP A 1 78 ? 19.233 11.293 -11.332 1.00 44.74 ? 76 ASP A CG 1 ATOM 558 O OD1 . ASP A 1 78 ? 19.831 10.311 -11.819 1.00 47.04 ? 76 ASP A OD1 1 ATOM 559 O OD2 . ASP A 1 78 ? 18.152 11.704 -11.764 1.00 51.45 ? 76 ASP A OD2 1 ATOM 560 N N . THR A 1 79 ? 22.854 10.117 -10.388 1.00 35.01 ? 77 THR A N 1 ATOM 561 C CA . THR A 1 79 ? 24.031 9.953 -11.225 1.00 34.18 ? 77 THR A CA 1 ATOM 562 C C . THR A 1 79 ? 23.763 9.836 -12.749 1.00 36.97 ? 77 THR A C 1 ATOM 563 O O . THR A 1 79 ? 24.711 9.610 -13.508 1.00 36.09 ? 77 THR A O 1 ATOM 564 C CB . THR A 1 79 ? 24.867 8.735 -10.795 1.00 33.51 ? 77 THR A CB 1 ATOM 565 O OG1 . THR A 1 79 ? 24.149 7.521 -11.096 1.00 35.19 ? 77 THR A OG1 1 ATOM 566 C CG2 . THR A 1 79 ? 25.236 8.835 -9.329 1.00 30.38 ? 77 THR A CG2 1 ATOM 567 N N . PHE A 1 80 ? 22.507 9.972 -13.191 1.00 39.87 ? 78 PHE A N 1 ATOM 568 C CA . PHE A 1 80 ? 22.196 10.179 -14.623 1.00 43.16 ? 78 PHE A CA 1 ATOM 569 C C . PHE A 1 80 ? 21.802 11.634 -14.941 1.00 43.44 ? 78 PHE A C 1 ATOM 570 O O . PHE A 1 80 ? 21.519 11.966 -16.095 1.00 44.98 ? 78 PHE A O 1 ATOM 571 C CB . PHE A 1 80 ? 21.115 9.199 -15.094 1.00 47.28 ? 78 PHE A CB 1 ATOM 572 C CG . PHE A 1 80 ? 21.440 7.786 -14.755 1.00 50.86 ? 78 PHE A CG 1 ATOM 573 C CD1 . PHE A 1 80 ? 22.512 7.154 -15.359 1.00 53.10 ? 78 PHE A CD1 1 ATOM 574 C CD2 . PHE A 1 80 ? 20.738 7.110 -13.767 1.00 55.23 ? 78 PHE A CD2 1 ATOM 575 C CE1 . PHE A 1 80 ? 22.858 5.854 -15.032 1.00 54.08 ? 78 PHE A CE1 1 ATOM 576 C CE2 . PHE A 1 80 ? 21.089 5.808 -13.426 1.00 56.40 ? 78 PHE A CE2 1 ATOM 577 C CZ . PHE A 1 80 ? 22.167 5.185 -14.071 1.00 55.49 ? 78 PHE A CZ 1 ATOM 578 N N . HIS A 1 81 ? 21.845 12.500 -13.920 1.00 41.31 ? 79 HIS A N 1 ATOM 579 C CA . HIS A 1 81 ? 21.474 13.897 -14.056 1.00 42.05 ? 79 HIS A CA 1 ATOM 580 C C . HIS A 1 81 ? 22.417 14.743 -13.200 1.00 38.61 ? 79 HIS A C 1 ATOM 581 O O . HIS A 1 81 ? 21.968 15.477 -12.335 1.00 37.31 ? 79 HIS A O 1 ATOM 582 C CB . HIS A 1 81 ? 20.012 14.056 -13.637 1.00 45.21 ? 79 HIS A CB 1 ATOM 583 C CG . HIS A 1 81 ? 19.406 15.398 -13.942 1.00 51.86 ? 79 HIS A CG 1 ATOM 584 N ND1 . HIS A 1 81 ? 20.057 16.378 -14.665 1.00 58.09 ? 79 HIS A ND1 1 ATOM 585 C CD2 . HIS A 1 81 ? 18.184 15.908 -13.637 1.00 58.34 ? 79 HIS A CD2 1 ATOM 586 C CE1 . HIS A 1 81 ? 19.267 17.434 -14.782 1.00 61.10 ? 79 HIS A CE1 1 ATOM 587 N NE2 . HIS A 1 81 ? 18.126 17.174 -14.166 1.00 61.25 ? 79 HIS A NE2 1 ATOM 588 N N . ASN A 1 82 ? 23.735 14.601 -13.435 1.00 35.97 ? 80 ASN A N 1 ATOM 589 C CA . ASN A 1 82 ? 24.740 15.571 -12.974 1.00 33.98 ? 80 ASN A CA 1 ATOM 590 C C . ASN A 1 82 ? 24.919 15.735 -11.469 1.00 31.29 ? 80 ASN A C 1 ATOM 591 O O . ASN A 1 82 ? 25.345 16.782 -11.012 1.00 30.28 ? 80 ASN A O 1 ATOM 592 C CB . ASN A 1 82 ? 24.413 16.970 -13.531 1.00 36.33 ? 80 ASN A CB 1 ATOM 593 C CG . ASN A 1 82 ? 24.035 16.949 -14.990 1.00 38.86 ? 80 ASN A CG 1 ATOM 594 O OD1 . ASN A 1 82 ? 22.931 16.604 -15.325 1.00 46.48 ? 80 ASN A OD1 1 ATOM 595 N ND2 . ASN A 1 82 ? 24.933 17.352 -15.847 1.00 40.72 ? 80 ASN A ND2 1 ATOM 596 N N . ASP A 1 83 ? 24.580 14.713 -10.699 1.00 30.26 ? 81 ASP A N 1 ATOM 597 C CA . ASP A 1 83 ? 24.364 14.885 -9.274 1.00 28.77 ? 81 ASP A CA 1 ATOM 598 C C . ASP A 1 83 ? 25.106 13.835 -8.470 1.00 27.13 ? 81 ASP A C 1 ATOM 599 O O . ASP A 1 83 ? 24.788 12.654 -8.547 1.00 28.15 ? 81 ASP A O 1 ATOM 600 C CB . ASP A 1 83 ? 22.833 14.853 -9.027 1.00 30.82 ? 81 ASP A CB 1 ATOM 601 C CG . ASP A 1 83 ? 22.442 15.063 -7.572 1.00 27.95 ? 81 ASP A CG 1 ATOM 602 O OD1 . ASP A 1 83 ? 23.294 15.338 -6.726 1.00 25.24 ? 81 ASP A OD1 1 ATOM 603 O OD2 . ASP A 1 83 ? 21.253 14.891 -7.261 1.00 31.07 ? 81 ASP A OD2 1 ATOM 604 N N . GLY A 1 84 ? 26.092 14.280 -7.690 1.00 25.57 ? 82 GLY A N 1 ATOM 605 C CA . GLY A 1 84 ? 26.834 13.424 -6.791 1.00 24.41 ? 82 GLY A CA 1 ATOM 606 C C . GLY A 1 84 ? 26.612 13.701 -5.306 1.00 23.64 ? 82 GLY A C 1 ATOM 607 O O . GLY A 1 84 ? 27.518 13.490 -4.509 1.00 23.09 ? 82 GLY A O 1 ATOM 608 N N . SER A 1 85 ? 25.411 14.127 -4.943 1.00 23.79 ? 83 SER A N 1 ATOM 609 C CA . SER A 1 85 ? 25.088 14.499 -3.551 1.00 23.35 ? 83 SER A CA 1 ATOM 610 C C . SER A 1 85 ? 25.159 13.309 -2.577 1.00 23.08 ? 83 SER A C 1 ATOM 611 O O . SER A 1 85 ? 24.869 12.182 -2.926 1.00 22.90 ? 83 SER A O 1 ATOM 612 C CB . SER A 1 85 ? 23.712 15.165 -3.469 1.00 24.50 ? 83 SER A CB 1 ATOM 613 O OG . SER A 1 85 ? 23.605 16.310 -4.323 1.00 23.56 ? 83 SER A OG 1 ATOM 614 N N . LEU A 1 86 ? 25.567 13.614 -1.347 1.00 22.86 ? 84 LEU A N 1 ATOM 615 C CA . LEU A 1 86 ? 25.823 12.642 -0.297 1.00 22.76 ? 84 LEU A CA 1 ATOM 616 C C . LEU A 1 86 ? 24.807 12.810 0.838 1.00 22.77 ? 84 LEU A C 1 ATOM 617 O O . LEU A 1 86 ? 24.477 13.933 1.246 1.00 21.07 ? 84 LEU A O 1 ATOM 618 C CB . LEU A 1 86 ? 27.220 12.912 0.265 1.00 22.99 ? 84 LEU A CB 1 ATOM 619 C CG . LEU A 1 86 ? 27.750 12.218 1.521 1.00 24.58 ? 84 LEU A CG 1 ATOM 620 C CD1 . LEU A 1 86 ? 28.235 10.832 1.196 1.00 24.99 ? 84 LEU A CD1 1 ATOM 621 C CD2 . LEU A 1 86 ? 28.875 13.092 2.088 1.00 25.74 ? 84 LEU A CD2 1 ATOM 622 N N . LEU A 1 87 ? 24.315 11.677 1.329 1.00 22.95 ? 85 LEU A N 1 ATOM 623 C CA . LEU A 1 87 ? 23.576 11.616 2.564 1.00 23.50 ? 85 LEU A CA 1 ATOM 624 C C . LEU A 1 87 ? 24.465 10.975 3.598 1.00 23.38 ? 85 LEU A C 1 ATOM 625 O O . LEU A 1 87 ? 24.911 9.859 3.414 1.00 23.65 ? 85 LEU A O 1 ATOM 626 C CB . LEU A 1 87 ? 22.299 10.791 2.414 1.00 25.34 ? 85 LEU A CB 1 ATOM 627 C CG . LEU A 1 87 ? 21.418 10.687 3.662 1.00 25.59 ? 85 LEU A CG 1 ATOM 628 C CD1 . LEU A 1 87 ? 20.784 12.035 3.879 1.00 24.19 ? 85 LEU A CD1 1 ATOM 629 C CD2 . LEU A 1 87 ? 20.368 9.538 3.487 1.00 27.06 ? 85 LEU A CD2 1 ATOM 630 N N . LEU A 1 88 ? 24.736 11.701 4.684 1.00 24.21 ? 86 LEU A N 1 ATOM 631 C CA . LEU A 1 88 ? 25.416 11.151 5.852 1.00 24.53 ? 86 LEU A CA 1 ATOM 632 C C . LEU A 1 88 ? 24.423 11.055 6.981 1.00 25.31 ? 86 LEU A C 1 ATOM 633 O O . LEU A 1 88 ? 23.808 12.054 7.349 1.00 25.20 ? 86 LEU A O 1 ATOM 634 C CB . LEU A 1 88 ? 26.572 12.055 6.283 1.00 24.94 ? 86 LEU A CB 1 ATOM 635 C CG . LEU A 1 88 ? 27.431 11.663 7.506 1.00 25.43 ? 86 LEU A CG 1 ATOM 636 C CD1 . LEU A 1 88 ? 27.960 10.210 7.407 1.00 28.15 ? 86 LEU A CD1 1 ATOM 637 C CD2 . LEU A 1 88 ? 28.572 12.643 7.654 1.00 26.30 ? 86 LEU A CD2 1 ATOM 638 N N . GLN A 1 89 ? 24.308 9.857 7.550 1.00 26.12 ? 87 GLN A N 1 ATOM 639 C CA . GLN A 1 89 ? 23.400 9.555 8.602 1.00 27.92 ? 87 GLN A CA 1 ATOM 640 C C . GLN A 1 89 ? 24.118 9.458 9.958 1.00 29.29 ? 87 GLN A C 1 ATOM 641 O O . GLN A 1 89 ? 25.385 9.268 10.034 1.00 28.53 ? 87 GLN A O 1 ATOM 642 C CB . GLN A 1 89 ? 22.724 8.208 8.315 1.00 30.07 ? 87 GLN A CB 1 ATOM 643 C CG . GLN A 1 89 ? 22.014 8.149 6.998 1.00 30.92 ? 87 GLN A CG 1 ATOM 644 C CD . GLN A 1 89 ? 21.339 6.822 6.798 1.00 34.91 ? 87 GLN A CD 1 ATOM 645 O OE1 . GLN A 1 89 ? 22.005 5.818 6.550 1.00 37.21 ? 87 GLN A OE1 1 ATOM 646 N NE2 . GLN A 1 89 ? 20.010 6.804 6.908 1.00 36.38 ? 87 GLN A NE2 1 ATOM 647 N N . ASP A 1 90 ? 23.311 9.607 11.015 1.00 29.83 ? 88 ASP A N 1 ATOM 648 C CA . ASP A 1 90 ? 23.775 9.436 12.391 1.00 32.47 ? 88 ASP A CA 1 ATOM 649 C C . ASP A 1 90 ? 25.065 10.209 12.654 1.00 31.08 ? 88 ASP A C 1 ATOM 650 O O . ASP A 1 90 ? 26.059 9.631 13.095 1.00 32.12 ? 88 ASP A O 1 ATOM 651 C CB . ASP A 1 90 ? 23.995 7.942 12.633 1.00 35.24 ? 88 ASP A CB 1 ATOM 652 C CG . ASP A 1 90 ? 24.174 7.601 14.094 1.00 42.04 ? 88 ASP A CG 1 ATOM 653 O OD1 . ASP A 1 90 ? 23.396 8.154 14.929 1.00 46.29 ? 88 ASP A OD1 1 ATOM 654 O OD2 . ASP A 1 90 ? 25.094 6.766 14.387 1.00 46.88 ? 88 ASP A OD2 1 ATOM 655 N N . VAL A 1 91 ? 25.046 11.505 12.349 1.00 28.96 ? 89 VAL A N 1 ATOM 656 C CA . VAL A 1 91 ? 26.199 12.374 12.519 1.00 28.08 ? 89 VAL A CA 1 ATOM 657 C C . VAL A 1 91 ? 26.716 12.326 13.956 1.00 29.91 ? 89 VAL A C 1 ATOM 658 O O . VAL A 1 91 ? 25.951 12.313 14.908 1.00 31.06 ? 89 VAL A O 1 ATOM 659 C CB . VAL A 1 91 ? 25.861 13.847 12.126 1.00 28.41 ? 89 VAL A CB 1 ATOM 660 C CG1 . VAL A 1 91 ? 26.946 14.871 12.650 1.00 27.39 ? 89 VAL A CG1 1 ATOM 661 C CG2 . VAL A 1 91 ? 25.622 13.960 10.607 1.00 23.90 ? 89 VAL A CG2 1 ATOM 662 N N . GLN A 1 92 ? 28.034 12.256 14.075 1.00 30.67 ? 90 GLN A N 1 ATOM 663 C CA A GLN A 1 92 ? 28.668 12.232 15.384 0.50 32.56 ? 90 GLN A CA 1 ATOM 664 C CA B GLN A 1 92 ? 28.754 12.157 15.327 0.50 32.64 ? 90 GLN A CA 1 ATOM 665 C C . GLN A 1 92 ? 29.630 13.402 15.473 1.00 32.75 ? 90 GLN A C 1 ATOM 666 O O . GLN A 1 92 ? 29.923 14.071 14.483 1.00 30.97 ? 90 GLN A O 1 ATOM 667 C CB A GLN A 1 92 ? 29.368 10.877 15.642 0.50 34.41 ? 90 GLN A CB 1 ATOM 668 C CB B GLN A 1 92 ? 29.599 10.864 15.284 0.50 33.97 ? 90 GLN A CB 1 ATOM 669 C CG A GLN A 1 92 ? 28.396 9.675 15.890 0.50 34.66 ? 90 GLN A CG 1 ATOM 670 C CG B GLN A 1 92 ? 28.720 9.596 15.348 0.50 34.86 ? 90 GLN A CG 1 ATOM 671 C CD A GLN A 1 92 ? 27.378 9.927 17.010 0.50 35.48 ? 90 GLN A CD 1 ATOM 672 C CD B GLN A 1 92 ? 29.369 8.361 14.775 0.50 36.84 ? 90 GLN A CD 1 ATOM 673 O OE1 A GLN A 1 92 ? 27.751 10.174 18.161 0.50 37.89 ? 90 GLN A OE1 1 ATOM 674 O OE1 B GLN A 1 92 ? 30.540 8.093 15.024 0.50 37.62 ? 90 GLN A OE1 1 ATOM 675 N NE2 A GLN A 1 92 ? 26.082 9.854 16.672 0.50 34.38 ? 90 GLN A NE2 1 ATOM 676 N NE2 B GLN A 1 92 ? 28.588 7.572 14.023 0.50 37.99 ? 90 GLN A NE2 1 ATOM 677 N N . LYS A 1 93 ? 30.078 13.692 16.681 1.00 34.76 ? 91 LYS A N 1 ATOM 678 C CA . LYS A 1 93 ? 30.951 14.849 16.894 1.00 35.84 ? 91 LYS A CA 1 ATOM 679 C C . LYS A 1 93 ? 32.245 14.732 16.082 1.00 35.17 ? 91 LYS A C 1 ATOM 680 O O . LYS A 1 93 ? 32.766 15.733 15.575 1.00 34.25 ? 91 LYS A O 1 ATOM 681 C CB . LYS A 1 93 ? 31.269 15.005 18.373 1.00 39.17 ? 91 LYS A CB 1 ATOM 682 C CG . LYS A 1 93 ? 30.955 16.391 18.899 1.00 43.22 ? 91 LYS A CG 1 ATOM 683 C CD . LYS A 1 93 ? 31.914 17.462 18.369 1.00 46.74 ? 91 LYS A CD 1 ATOM 684 C CE . LYS A 1 93 ? 31.155 18.755 18.043 1.00 47.78 ? 91 LYS A CE 1 ATOM 685 N NZ . LYS A 1 93 ? 31.842 19.983 18.565 1.00 49.64 ? 91 LYS A NZ 1 ATOM 686 N N . ALA A 1 94 ? 32.749 13.502 15.956 1.00 35.00 ? 92 ALA A N 1 ATOM 687 C CA . ALA A 1 94 ? 33.941 13.214 15.139 1.00 34.73 ? 92 ALA A CA 1 ATOM 688 C C . ALA A 1 94 ? 33.733 13.461 13.652 1.00 32.46 ? 92 ALA A C 1 ATOM 689 O O . ALA A 1 94 ? 34.693 13.350 12.899 1.00 32.73 ? 92 ALA A O 1 ATOM 690 C CB . ALA A 1 94 ? 34.383 11.768 15.354 1.00 35.82 ? 92 ALA A CB 1 ATOM 691 N N . ASP A 1 95 ? 32.487 13.739 13.221 1.00 29.89 ? 93 ASP A N 1 ATOM 692 C CA . ASP A 1 95 ? 32.164 14.038 11.824 1.00 28.01 ? 93 ASP A CA 1 ATOM 693 C C . ASP A 1 95 ? 32.258 15.526 11.496 1.00 27.85 ? 93 ASP A C 1 ATOM 694 O O . ASP A 1 95 ? 32.051 15.926 10.342 1.00 26.42 ? 93 ASP A O 1 ATOM 695 C CB . ASP A 1 95 ? 30.771 13.509 11.440 1.00 26.76 ? 93 ASP A CB 1 ATOM 696 C CG . ASP A 1 95 ? 30.646 11.991 11.599 1.00 29.24 ? 93 ASP A CG 1 ATOM 697 O OD1 . ASP A 1 95 ? 31.658 11.283 11.553 1.00 32.82 ? 93 ASP A OD1 1 ATOM 698 O OD2 . ASP A 1 95 ? 29.520 11.489 11.754 1.00 31.55 ? 93 ASP A OD2 1 ATOM 699 N N . GLU A 1 96 ? 32.566 16.338 12.508 1.00 28.77 ? 94 GLU A N 1 ATOM 700 C CA . GLU A 1 96 ? 32.748 17.791 12.361 1.00 28.57 ? 94 GLU A CA 1 ATOM 701 C C . GLU A 1 96 ? 34.028 18.155 11.590 1.00 28.17 ? 94 GLU A C 1 ATOM 702 O O . GLU A 1 96 ? 35.135 17.745 11.952 1.00 27.57 ? 94 GLU A O 1 ATOM 703 C CB . GLU A 1 96 ? 32.796 18.444 13.740 1.00 30.90 ? 94 GLU A CB 1 ATOM 704 C CG . GLU A 1 96 ? 33.002 19.959 13.731 1.00 32.93 ? 94 GLU A CG 1 ATOM 705 C CD . GLU A 1 96 ? 32.598 20.614 15.047 1.00 36.42 ? 94 GLU A CD 1 ATOM 706 O OE1 . GLU A 1 96 ? 31.398 20.654 15.352 1.00 35.11 ? 94 GLU A OE1 1 ATOM 707 O OE2 . GLU A 1 96 ? 33.471 21.113 15.782 1.00 41.77 ? 94 GLU A OE2 1 ATOM 708 N N . GLY A 1 97 ? 33.870 18.943 10.529 1.00 26.66 ? 95 GLY A N 1 ATOM 709 C CA . GLY A 1 97 ? 35.000 19.338 9.714 1.00 27.92 ? 95 GLY A CA 1 ATOM 710 C C . GLY A 1 97 ? 34.528 19.578 8.315 1.00 27.25 ? 95 GLY A C 1 ATOM 711 O O . GLY A 1 97 ? 33.359 19.966 8.114 1.00 25.63 ? 95 GLY A O 1 ATOM 712 N N . ILE A 1 98 ? 35.415 19.344 7.353 1.00 27.25 ? 96 ILE A N 1 ATOM 713 C CA . ILE A 1 98 ? 35.181 19.746 5.970 1.00 27.27 ? 96 ILE A CA 1 ATOM 714 C C . ILE A 1 98 ? 35.059 18.547 5.046 1.00 26.11 ? 96 ILE A C 1 ATOM 715 O O . ILE A 1 98 ? 35.914 17.671 5.061 1.00 26.10 ? 96 ILE A O 1 ATOM 716 C CB . ILE A 1 98 ? 36.335 20.656 5.467 1.00 29.62 ? 96 ILE A CB 1 ATOM 717 C CG1 . ILE A 1 98 ? 36.473 21.876 6.359 1.00 32.73 ? 96 ILE A CG1 1 ATOM 718 C CG2 . ILE A 1 98 ? 36.084 21.138 4.036 1.00 29.05 ? 96 ILE A CG2 1 ATOM 719 C CD1 . ILE A 1 98 ? 37.845 22.412 6.386 1.00 39.79 ? 96 ILE A CD1 1 ATOM 720 N N . TYR A 1 99 ? 33.993 18.540 4.238 1.00 25.68 ? 97 TYR A N 1 ATOM 721 C CA . TYR A 1 99 ? 33.689 17.516 3.273 1.00 24.85 ? 97 TYR A CA 1 ATOM 722 C C . TYR A 1 99 ? 33.883 18.157 1.914 1.00 26.46 ? 97 TYR A C 1 ATOM 723 O O . TYR A 1 99 ? 33.295 19.217 1.627 1.00 27.25 ? 97 TYR A O 1 ATOM 724 C CB . TYR A 1 99 ? 32.249 17.013 3.464 1.00 23.82 ? 97 TYR A CB 1 ATOM 725 C CG . TYR A 1 99 ? 32.082 16.296 4.782 1.00 22.95 ? 97 TYR A CG 1 ATOM 726 C CD1 . TYR A 1 99 ? 32.008 17.007 5.996 1.00 23.96 ? 97 TYR A CD1 1 ATOM 727 C CD2 . TYR A 1 99 ? 32.026 14.913 4.826 1.00 22.28 ? 97 TYR A CD2 1 ATOM 728 C CE1 . TYR A 1 99 ? 31.885 16.325 7.239 1.00 23.68 ? 97 TYR A CE1 1 ATOM 729 C CE2 . TYR A 1 99 ? 31.881 14.245 6.011 1.00 22.79 ? 97 TYR A CE2 1 ATOM 730 C CZ . TYR A 1 99 ? 31.804 14.946 7.230 1.00 24.42 ? 97 TYR A CZ 1 ATOM 731 O OH . TYR A 1 99 ? 31.707 14.197 8.398 1.00 23.79 ? 97 TYR A OH 1 ATOM 732 N N . THR A 1 100 ? 34.761 17.560 1.100 1.00 26.02 ? 98 THR A N 1 ATOM 733 C CA . THR A 1 100 ? 35.009 18.076 -0.243 1.00 26.17 ? 98 THR A CA 1 ATOM 734 C C . THR A 1 100 ? 34.506 17.052 -1.260 1.00 24.71 ? 98 THR A C 1 ATOM 735 O O . THR A 1 100 ? 34.835 15.885 -1.190 1.00 24.12 ? 98 THR A O 1 ATOM 736 C CB . THR A 1 100 ? 36.495 18.449 -0.479 1.00 27.91 ? 98 THR A CB 1 ATOM 737 O OG1 . THR A 1 100 ? 36.938 19.335 0.565 1.00 28.94 ? 98 THR A OG1 1 ATOM 738 C CG2 . THR A 1 100 ? 36.663 19.163 -1.852 1.00 27.18 ? 98 THR A CG2 1 ATOM 739 N N . CYS A 1 101 ? 33.625 17.500 -2.136 1.00 24.50 ? 99 CYS A N 1 ATOM 740 C CA . CYS A 1 101 ? 33.172 16.722 -3.263 1.00 25.05 ? 99 CYS A CA 1 ATOM 741 C C . CYS A 1 101 ? 34.031 17.103 -4.470 1.00 24.46 ? 99 CYS A C 1 ATOM 742 O O . CYS A 1 101 ? 34.194 18.290 -4.777 1.00 24.76 ? 99 CYS A O 1 ATOM 743 C CB . CYS A 1 101 ? 31.717 17.051 -3.574 1.00 25.45 ? 99 CYS A CB 1 ATOM 744 S SG . CYS A 1 101 ? 31.033 16.083 -4.913 1.00 30.87 ? 99 CYS A SG 1 ATOM 745 N N . GLU A 1 102 ? 34.588 16.092 -5.127 1.00 23.39 ? 100 GLU A N 1 ATOM 746 C CA . GLU A 1 102 ? 35.185 16.223 -6.460 1.00 24.29 ? 100 GLU A CA 1 ATOM 747 C C . GLU A 1 102 ? 34.359 15.368 -7.426 1.00 23.29 ? 100 GLU A C 1 ATOM 748 O O . GLU A 1 102 ? 34.114 14.202 -7.165 1.00 22.96 ? 100 GLU A O 1 ATOM 749 C CB . GLU A 1 102 ? 36.627 15.791 -6.439 1.00 25.39 ? 100 GLU A CB 1 ATOM 750 C CG . GLU A 1 102 ? 37.395 16.568 -5.436 1.00 29.00 ? 100 GLU A CG 1 ATOM 751 C CD . GLU A 1 102 ? 38.879 16.713 -5.745 1.00 37.37 ? 100 GLU A CD 1 ATOM 752 O OE1 . GLU A 1 102 ? 39.384 16.044 -6.707 1.00 42.99 ? 100 GLU A OE1 1 ATOM 753 O OE2 . GLU A 1 102 ? 39.520 17.525 -5.006 1.00 39.83 ? 100 GLU A OE2 1 ATOM 754 N N . ILE A 1 103 ? 33.869 15.979 -8.494 1.00 22.61 ? 101 ILE A N 1 ATOM 755 C CA . ILE A 1 103 ? 32.910 15.310 -9.383 1.00 21.77 ? 101 ILE A CA 1 ATOM 756 C C . ILE A 1 103 ? 33.243 15.620 -10.843 1.00 22.47 ? 101 ILE A C 1 ATOM 757 O O . ILE A 1 103 ? 33.532 16.741 -11.175 1.00 22.97 ? 101 ILE A O 1 ATOM 758 C CB . ILE A 1 103 ? 31.439 15.707 -9.015 1.00 22.02 ? 101 ILE A CB 1 ATOM 759 C CG1 . ILE A 1 103 ? 30.449 15.038 -9.959 1.00 20.94 ? 101 ILE A CG1 1 ATOM 760 C CG2 . ILE A 1 103 ? 31.288 17.249 -8.940 1.00 20.42 ? 101 ILE A CG2 1 ATOM 761 C CD1 . ILE A 1 103 ? 29.022 14.899 -9.418 1.00 19.47 ? 101 ILE A CD1 1 ATOM 762 N N . ARG A 1 104 ? 33.279 14.589 -11.687 1.00 22.54 ? 102 ARG A N 1 ATOM 763 C CA . ARG A 1 104 ? 33.440 14.738 -13.115 1.00 23.17 ? 102 ARG A CA 1 ATOM 764 C C . ARG A 1 104 ? 32.289 14.035 -13.834 1.00 24.99 ? 102 ARG A C 1 ATOM 765 O O . ARG A 1 104 ? 31.893 12.890 -13.504 1.00 24.93 ? 102 ARG A O 1 ATOM 766 C CB . ARG A 1 104 ? 34.786 14.172 -13.576 1.00 23.44 ? 102 ARG A CB 1 ATOM 767 C CG . ARG A 1 104 ? 35.178 14.587 -14.949 1.00 22.35 ? 102 ARG A CG 1 ATOM 768 C CD . ARG A 1 104 ? 36.517 14.017 -15.403 1.00 22.13 ? 102 ARG A CD 1 ATOM 769 N NE . ARG A 1 104 ? 36.545 12.575 -15.252 1.00 23.97 ? 102 ARG A NE 1 ATOM 770 C CZ . ARG A 1 104 ? 35.925 11.708 -16.043 1.00 26.75 ? 102 ARG A CZ 1 ATOM 771 N NH1 . ARG A 1 104 ? 35.201 12.123 -17.085 1.00 29.70 ? 102 ARG A NH1 1 ATOM 772 N NH2 . ARG A 1 104 ? 36.017 10.403 -15.774 1.00 26.92 ? 102 ARG A NH2 1 ATOM 773 N N . LEU A 1 105 ? 31.767 14.723 -14.840 1.00 26.66 ? 103 LEU A N 1 ATOM 774 C CA . LEU A 1 105 ? 30.648 14.218 -15.607 1.00 27.80 ? 103 LEU A CA 1 ATOM 775 C C . LEU A 1 105 ? 31.153 13.457 -16.809 1.00 29.23 ? 103 LEU A C 1 ATOM 776 O O . LEU A 1 105 ? 32.275 13.650 -17.265 1.00 28.71 ? 103 LEU A O 1 ATOM 777 C CB . LEU A 1 105 ? 29.740 15.367 -16.047 1.00 29.13 ? 103 LEU A CB 1 ATOM 778 C CG . LEU A 1 105 ? 29.082 16.244 -14.952 1.00 26.43 ? 103 LEU A CG 1 ATOM 779 C CD1 . LEU A 1 105 ? 28.181 17.299 -15.626 1.00 27.62 ? 103 LEU A CD1 1 ATOM 780 C CD2 . LEU A 1 105 ? 28.339 15.373 -13.943 1.00 20.30 ? 103 LEU A CD2 1 ATOM 781 N N . LYS A 1 106 ? 30.317 12.548 -17.270 1.00 31.62 ? 104 LYS A N 1 ATOM 782 C CA . LYS A 1 106 ? 30.554 11.786 -18.487 1.00 34.41 ? 104 LYS A CA 1 ATOM 783 C C . LYS A 1 106 ? 30.774 12.714 -19.659 1.00 36.50 ? 104 LYS A C 1 ATOM 784 O O . LYS A 1 106 ? 30.037 13.682 -19.854 1.00 36.58 ? 104 LYS A O 1 ATOM 785 C CB . LYS A 1 106 ? 29.380 10.841 -18.770 1.00 35.91 ? 104 LYS A CB 1 ATOM 786 C CG . LYS A 1 106 ? 29.591 9.952 -20.006 1.00 40.65 ? 104 LYS A CG 1 ATOM 787 C CD . LYS A 1 106 ? 28.742 8.675 -19.961 1.00 44.26 ? 104 LYS A CD 1 ATOM 788 C CE . LYS A 1 106 ? 28.266 8.208 -21.349 1.00 50.60 ? 104 LYS A CE 1 ATOM 789 N NZ . LYS A 1 106 ? 26.728 8.218 -21.483 1.00 55.58 ? 104 LYS A NZ 1 ATOM 790 N N . ASN A 1 107 ? 31.855 12.435 -20.383 1.00 38.22 ? 105 ASN A N 1 ATOM 791 C CA . ASN A 1 107 ? 32.232 13.169 -21.571 1.00 41.48 ? 105 ASN A CA 1 ATOM 792 C C . ASN A 1 107 ? 32.752 14.572 -21.279 1.00 39.92 ? 105 ASN A C 1 ATOM 793 O O . ASN A 1 107 ? 32.772 15.413 -22.159 1.00 40.74 ? 105 ASN A O 1 ATOM 794 C CB . ASN A 1 107 ? 31.055 13.201 -22.564 1.00 45.45 ? 105 ASN A CB 1 ATOM 795 C CG . ASN A 1 107 ? 31.508 13.160 -24.005 1.00 54.39 ? 105 ASN A CG 1 ATOM 796 O OD1 . ASN A 1 107 ? 32.325 12.318 -24.372 1.00 60.77 ? 105 ASN A OD1 1 ATOM 797 N ND2 . ASN A 1 107 ? 30.956 14.078 -24.842 1.00 67.33 ? 105 ASN A ND2 1 ATOM 798 N N . GLU A 1 108 ? 33.187 14.813 -20.045 1.00 37.19 ? 106 GLU A N 1 ATOM 799 C CA . GLU A 1 108 ? 33.811 16.084 -19.675 1.00 36.63 ? 106 GLU A CA 1 ATOM 800 C C . GLU A 1 108 ? 35.168 15.812 -19.054 1.00 34.58 ? 106 GLU A C 1 ATOM 801 O O . GLU A 1 108 ? 35.384 14.765 -18.465 1.00 31.31 ? 106 GLU A O 1 ATOM 802 C CB . GLU A 1 108 ? 32.952 16.863 -18.670 1.00 36.73 ? 106 GLU A CB 1 ATOM 803 C CG . GLU A 1 108 ? 31.595 17.281 -19.238 1.00 38.97 ? 106 GLU A CG 1 ATOM 804 C CD . GLU A 1 108 ? 30.945 18.410 -18.467 1.00 39.94 ? 106 GLU A CD 1 ATOM 805 O OE1 . GLU A 1 108 ? 31.395 18.710 -17.338 1.00 38.45 ? 106 GLU A OE1 1 ATOM 806 O OE2 . GLU A 1 108 ? 29.976 19.004 -19.001 1.00 41.12 ? 106 GLU A OE2 1 ATOM 807 N N . SER A 1 109 ? 36.080 16.763 -19.223 1.00 35.09 ? 107 SER A N 1 ATOM 808 C CA . SER A 1 109 ? 37.405 16.683 -18.630 1.00 34.66 ? 107 SER A CA 1 ATOM 809 C C . SER A 1 109 ? 37.510 17.487 -17.343 1.00 33.50 ? 107 SER A C 1 ATOM 810 O O . SER A 1 109 ? 38.348 17.190 -16.528 1.00 32.62 ? 107 SER A O 1 ATOM 811 C CB . SER A 1 109 ? 38.459 17.141 -19.628 1.00 36.45 ? 107 SER A CB 1 ATOM 812 O OG . SER A 1 109 ? 38.725 16.087 -20.542 1.00 38.59 ? 107 SER A OG 1 ATOM 813 N N . MET A 1 110 ? 36.663 18.500 -17.174 1.00 34.13 ? 108 MET A N 1 ATOM 814 C CA . MET A 1 110 ? 36.730 19.396 -16.012 1.00 33.90 ? 108 MET A CA 1 ATOM 815 C C . MET A 1 110 ? 36.169 18.710 -14.788 1.00 30.20 ? 108 MET A C 1 ATOM 816 O O . MET A 1 110 ? 35.222 17.901 -14.884 1.00 29.91 ? 108 MET A O 1 ATOM 817 C CB . MET A 1 110 ? 35.946 20.682 -16.249 1.00 36.23 ? 108 MET A CB 1 ATOM 818 C CG . MET A 1 110 ? 36.660 21.736 -17.046 1.00 42.80 ? 108 MET A CG 1 ATOM 819 S SD . MET A 1 110 ? 35.637 23.244 -17.309 1.00 51.05 ? 108 MET A SD 1 ATOM 820 C CE . MET A 1 110 ? 34.607 23.156 -15.814 1.00 47.71 ? 108 MET A CE 1 ATOM 821 N N . VAL A 1 111 ? 36.775 18.999 -13.644 1.00 28.48 ? 109 VAL A N 1 ATOM 822 C CA . VAL A 1 111 ? 36.334 18.475 -12.361 1.00 26.25 ? 109 VAL A CA 1 ATOM 823 C C . VAL A 1 111 ? 35.852 19.639 -11.482 1.00 27.66 ? 109 VAL A C 1 ATOM 824 O O . VAL A 1 111 ? 36.530 20.662 -11.351 1.00 28.77 ? 109 VAL A O 1 ATOM 825 C CB . VAL A 1 111 ? 37.467 17.701 -11.679 1.00 26.15 ? 109 VAL A CB 1 ATOM 826 C CG1 . VAL A 1 111 ? 37.118 17.308 -10.279 1.00 21.77 ? 109 VAL A CG1 1 ATOM 827 C CG2 . VAL A 1 111 ? 37.878 16.440 -12.540 1.00 24.30 ? 109 VAL A CG2 1 ATOM 828 N N . MET A 1 112 ? 34.644 19.514 -10.955 1.00 26.76 ? 110 MET A N 1 ATOM 829 C CA . MET A 1 112 ? 34.122 20.455 -9.969 1.00 28.72 ? 110 MET A CA 1 ATOM 830 C C . MET A 1 112 ? 34.531 20.007 -8.569 1.00 26.09 ? 110 MET A C 1 ATOM 831 O O . MET A 1 112 ? 34.470 18.816 -8.237 1.00 24.32 ? 110 MET A O 1 ATOM 832 C CB . MET A 1 112 ? 32.585 20.506 -10.041 1.00 30.38 ? 110 MET A CB 1 ATOM 833 C CG . MET A 1 112 ? 31.916 21.605 -9.150 1.00 36.95 ? 110 MET A CG 1 ATOM 834 S SD . MET A 1 112 ? 30.089 21.413 -9.096 1.00 50.53 ? 110 MET A SD 1 ATOM 835 C CE . MET A 1 112 ? 29.864 20.078 -7.912 1.00 46.86 ? 110 MET A CE 1 ATOM 836 N N . LYS A 1 113 ? 34.972 20.964 -7.765 1.00 26.22 ? 111 LYS A N 1 ATOM 837 C CA . LYS A 1 113 ? 35.413 20.715 -6.384 1.00 25.47 ? 111 LYS A CA 1 ATOM 838 C C . LYS A 1 113 ? 34.674 21.672 -5.466 1.00 26.91 ? 111 LYS A C 1 ATOM 839 O O . LYS A 1 113 ? 34.762 22.875 -5.606 1.00 27.81 ? 111 LYS A O 1 ATOM 840 C CB . LYS A 1 113 ? 36.941 20.899 -6.236 1.00 26.44 ? 111 LYS A CB 1 ATOM 841 C CG . LYS A 1 113 ? 37.717 20.107 -7.249 1.00 24.89 ? 111 LYS A CG 1 ATOM 842 C CD . LYS A 1 113 ? 39.220 20.286 -7.164 1.00 27.77 ? 111 LYS A CD 1 ATOM 843 C CE . LYS A 1 113 ? 39.858 19.401 -8.244 1.00 29.40 ? 111 LYS A CE 1 ATOM 844 N NZ . LYS A 1 113 ? 41.320 19.334 -8.162 1.00 32.40 ? 111 LYS A NZ 1 ATOM 845 N N . LYS A 1 114 ? 33.955 21.095 -4.521 1.00 27.57 ? 112 LYS A N 1 ATOM 846 C CA . LYS A 1 114 ? 33.005 21.808 -3.697 1.00 29.58 ? 112 LYS A CA 1 ATOM 847 C C . LYS A 1 114 ? 33.223 21.448 -2.240 1.00 28.55 ? 112 LYS A C 1 ATOM 848 O O . LYS A 1 114 ? 32.886 20.348 -1.832 1.00 26.37 ? 112 LYS A O 1 ATOM 849 C CB . LYS A 1 114 ? 31.582 21.409 -4.107 1.00 28.55 ? 112 LYS A CB 1 ATOM 850 C CG . LYS A 1 114 ? 30.564 22.424 -3.559 1.00 35.99 ? 112 LYS A CG 1 ATOM 851 C CD . LYS A 1 114 ? 29.119 21.904 -3.489 1.00 38.28 ? 112 LYS A CD 1 ATOM 852 C CE . LYS A 1 114 ? 28.240 22.923 -2.799 1.00 42.42 ? 112 LYS A CE 1 ATOM 853 N NZ . LYS A 1 114 ? 27.033 22.293 -2.167 1.00 43.69 ? 112 LYS A NZ 1 ATOM 854 N N . PRO A 1 115 ? 33.816 22.352 -1.455 1.00 30.11 ? 113 PRO A N 1 ATOM 855 C CA . PRO A 1 115 ? 33.879 22.058 -0.034 1.00 30.42 ? 113 PRO A CA 1 ATOM 856 C C . PRO A 1 115 ? 32.612 22.464 0.732 1.00 30.31 ? 113 PRO A C 1 ATOM 857 O O . PRO A 1 115 ? 31.998 23.480 0.392 1.00 31.87 ? 113 PRO A O 1 ATOM 858 C CB . PRO A 1 115 ? 35.077 22.871 0.436 1.00 32.47 ? 113 PRO A CB 1 ATOM 859 C CG . PRO A 1 115 ? 35.085 24.044 -0.468 1.00 35.36 ? 113 PRO A CG 1 ATOM 860 C CD . PRO A 1 115 ? 34.487 23.615 -1.784 1.00 33.22 ? 113 PRO A CD 1 ATOM 861 N N . VAL A 1 116 ? 32.236 21.644 1.728 1.00 28.53 ? 114 VAL A N 1 ATOM 862 C CA . VAL A 1 116 ? 31.079 21.867 2.606 1.00 28.29 ? 114 VAL A CA 1 ATOM 863 C C . VAL A 1 116 ? 31.581 21.725 4.057 1.00 28.86 ? 114 VAL A C 1 ATOM 864 O O . VAL A 1 116 ? 32.216 20.730 4.412 1.00 27.37 ? 114 VAL A O 1 ATOM 865 C CB . VAL A 1 116 ? 29.948 20.803 2.393 1.00 26.35 ? 114 VAL A CB 1 ATOM 866 C CG1 . VAL A 1 116 ? 28.772 21.134 3.220 1.00 25.28 ? 114 VAL A CG1 1 ATOM 867 C CG2 . VAL A 1 116 ? 29.550 20.678 0.922 1.00 26.50 ? 114 VAL A CG2 1 ATOM 868 N N . GLU A 1 117 ? 31.302 22.704 4.901 1.00 30.03 ? 115 GLU A N 1 ATOM 869 C CA . GLU A 1 117 ? 31.664 22.596 6.310 1.00 31.22 ? 115 GLU A CA 1 ATOM 870 C C . GLU A 1 117 ? 30.497 22.098 7.150 1.00 29.55 ? 115 GLU A C 1 ATOM 871 O O . GLU A 1 117 ? 29.389 22.663 7.074 1.00 30.18 ? 115 GLU A O 1 ATOM 872 C CB . GLU A 1 117 ? 32.084 23.926 6.855 1.00 33.98 ? 115 GLU A CB 1 ATOM 873 C CG . GLU A 1 117 ? 33.282 24.523 6.191 1.00 38.48 ? 115 GLU A CG 1 ATOM 874 C CD . GLU A 1 117 ? 33.646 25.837 6.857 1.00 45.49 ? 115 GLU A CD 1 ATOM 875 O OE1 . GLU A 1 117 ? 32.926 26.248 7.814 1.00 47.72 ? 115 GLU A OE1 1 ATOM 876 O OE2 . GLU A 1 117 ? 34.631 26.461 6.430 1.00 49.38 ? 115 GLU A OE2 1 ATOM 877 N N . LEU A 1 118 ? 30.770 21.082 7.966 1.00 27.32 ? 116 LEU A N 1 ATOM 878 C CA . LEU A 1 118 ? 29.800 20.510 8.880 1.00 26.92 ? 116 LEU A CA 1 ATOM 879 C C . LEU A 1 118 ? 30.170 20.811 10.331 1.00 28.31 ? 116 LEU A C 1 ATOM 880 O O . LEU A 1 118 ? 31.241 20.443 10.777 1.00 27.01 ? 116 LEU A O 1 ATOM 881 C CB . LEU A 1 118 ? 29.723 18.995 8.699 1.00 25.38 ? 116 LEU A CB 1 ATOM 882 C CG . LEU A 1 118 ? 28.539 18.324 9.426 1.00 26.01 ? 116 LEU A CG 1 ATOM 883 C CD1 . LEU A 1 118 ? 27.159 18.779 8.832 1.00 23.99 ? 116 LEU A CD1 1 ATOM 884 C CD2 . LEU A 1 118 ? 28.736 16.831 9.402 1.00 24.78 ? 116 LEU A CD2 1 ATOM 885 N N . TRP A 1 119 ? 29.261 21.482 11.047 1.00 29.81 ? 117 TRP A N 1 ATOM 886 C CA . TRP A 1 119 ? 29.410 21.807 12.460 1.00 31.93 ? 117 TRP A CA 1 ATOM 887 C C . TRP A 1 119 ? 28.417 20.963 13.226 1.00 29.64 ? 117 TRP A C 1 ATOM 888 O O . TRP A 1 119 ? 27.273 20.853 12.798 1.00 27.32 ? 117 TRP A O 1 ATOM 889 C CB . TRP A 1 119 ? 29.098 23.281 12.690 1.00 36.76 ? 117 TRP A CB 1 ATOM 890 C CG . TRP A 1 119 ? 29.966 24.099 11.896 1.00 40.59 ? 117 TRP A CG 1 ATOM 891 C CD1 . TRP A 1 119 ? 29.749 24.532 10.627 1.00 43.79 ? 117 TRP A CD1 1 ATOM 892 C CD2 . TRP A 1 119 ? 31.275 24.527 12.261 1.00 46.16 ? 117 TRP A CD2 1 ATOM 893 N NE1 . TRP A 1 119 ? 30.839 25.244 10.185 1.00 46.36 ? 117 TRP A NE1 1 ATOM 894 C CE2 . TRP A 1 119 ? 31.790 25.261 11.172 1.00 45.99 ? 117 TRP A CE2 1 ATOM 895 C CE3 . TRP A 1 119 ? 32.060 24.375 13.418 1.00 48.40 ? 117 TRP A CE3 1 ATOM 896 C CZ2 . TRP A 1 119 ? 33.058 25.832 11.186 1.00 47.83 ? 117 TRP A CZ2 1 ATOM 897 C CZ3 . TRP A 1 119 ? 33.324 24.962 13.446 1.00 50.46 ? 117 TRP A CZ3 1 ATOM 898 C CH2 . TRP A 1 119 ? 33.813 25.679 12.331 1.00 50.74 ? 117 TRP A CH2 1 ATOM 899 N N . VAL A 1 120 ? 28.837 20.400 14.358 1.00 28.56 ? 118 VAL A N 1 ATOM 900 C CA . VAL A 1 120 ? 28.008 19.440 15.100 1.00 27.85 ? 118 VAL A CA 1 ATOM 901 C C . VAL A 1 120 ? 27.734 20.001 16.479 1.00 29.80 ? 118 VAL A C 1 ATOM 902 O O . VAL A 1 120 ? 28.659 20.354 17.203 1.00 32.81 ? 118 VAL A O 1 ATOM 903 C CB . VAL A 1 120 ? 28.626 17.993 15.147 1.00 26.81 ? 118 VAL A CB 1 ATOM 904 C CG1 . VAL A 1 120 ? 27.720 17.031 15.899 1.00 26.44 ? 118 VAL A CG1 1 ATOM 905 C CG2 . VAL A 1 120 ? 28.868 17.468 13.759 1.00 23.13 ? 118 VAL A CG2 1 ATOM 906 N N . LEU A 1 121 ? 26.452 20.172 16.790 1.00 29.82 ? 119 LEU A N 1 ATOM 907 C CA . LEU A 1 121 ? 25.983 20.641 18.093 1.00 31.89 ? 119 LEU A CA 1 ATOM 908 C C . LEU A 1 121 ? 25.647 19.414 18.952 1.00 31.91 ? 119 LEU A C 1 ATOM 909 O O . LEU A 1 121 ? 25.533 18.324 18.422 1.00 29.36 ? 119 LEU A O 1 ATOM 910 C CB . LEU A 1 121 ? 24.725 21.482 17.898 1.00 32.61 ? 119 LEU A CB 1 ATOM 911 C CG . LEU A 1 121 ? 24.857 22.780 17.123 1.00 34.05 ? 119 LEU A CG 1 ATOM 912 C CD1 . LEU A 1 121 ? 23.502 23.314 16.721 1.00 33.88 ? 119 LEU A CD1 1 ATOM 913 C CD2 . LEU A 1 121 ? 25.615 23.778 17.974 1.00 39.49 ? 119 LEU A CD2 1 ATOM 914 N N . PRO A 1 122 ? 25.528 19.583 20.289 1.00 35.79 ? 120 PRO A N 1 ATOM 915 C CA . PRO A 1 122 ? 25.129 18.459 21.143 1.00 37.14 ? 120 PRO A CA 1 ATOM 916 C C . PRO A 1 122 ? 23.819 17.814 20.688 1.00 37.41 ? 120 PRO A C 1 ATOM 917 O O . PRO A 1 122 ? 22.980 18.472 20.067 1.00 36.95 ? 120 PRO A O 1 ATOM 918 C CB . PRO A 1 122 ? 24.961 19.099 22.530 1.00 39.38 ? 120 PRO A CB 1 ATOM 919 C CG . PRO A 1 122 ? 25.759 20.328 22.505 1.00 40.70 ? 120 PRO A CG 1 ATOM 920 C CD . PRO A 1 122 ? 25.819 20.800 21.076 1.00 38.20 ? 120 PRO A CD 1 ATOM 921 N N . GLU A 1 123 ? 23.670 16.523 20.967 1.00 39.19 ? 121 GLU A N 1 ATOM 922 C CA . GLU A 1 123 ? 22.451 15.777 20.625 1.00 40.27 ? 121 GLU A CA 1 ATOM 923 C C . GLU A 1 123 ? 21.204 16.429 21.236 1.00 41.66 ? 121 GLU A C 1 ATOM 924 O O . GLU A 1 123 ? 21.261 16.961 22.328 1.00 43.88 ? 121 GLU A O 1 ATOM 925 C CB . GLU A 1 123 ? 22.593 14.350 21.158 1.00 41.78 ? 121 GLU A CB 1 ATOM 926 C CG . GLU A 1 123 ? 21.428 13.434 20.882 1.00 45.43 ? 121 GLU A CG 1 ATOM 927 C CD . GLU A 1 123 ? 21.827 11.955 20.896 1.00 50.21 ? 121 GLU A CD 1 ATOM 928 O OE1 . GLU A 1 123 ? 22.690 11.599 21.730 1.00 54.09 ? 121 GLU A OE1 1 ATOM 929 O OE2 . GLU A 1 123 ? 21.283 11.168 20.066 1.00 52.01 ? 121 GLU A OE2 1 ATOM 930 N N . GLU A 1 124 ? 20.086 16.404 20.527 1.00 42.22 ? 122 GLU A N 1 ATOM 931 C CA . GLU A 1 124 ? 18.818 16.878 21.098 1.00 44.64 ? 122 GLU A CA 1 ATOM 932 C C . GLU A 1 124 ? 18.341 15.974 22.232 1.00 45.36 ? 122 GLU A C 1 ATOM 933 O O . GLU A 1 124 ? 18.550 14.776 22.212 1.00 44.37 ? 122 GLU A O 1 ATOM 934 C CB . GLU A 1 124 ? 17.719 16.932 20.036 1.00 45.53 ? 122 GLU A CB 1 ATOM 935 C CG . GLU A 1 124 ? 17.830 18.064 19.024 1.00 48.45 ? 122 GLU A CG 1 ATOM 936 C CD . GLU A 1 124 ? 16.754 17.956 17.931 1.00 52.91 ? 122 GLU A CD 1 ATOM 937 O OE1 . GLU A 1 124 ? 15.563 18.179 18.260 1.00 55.32 ? 122 GLU A OE1 1 ATOM 938 O OE2 . GLU A 1 124 ? 17.110 17.630 16.757 1.00 55.28 ? 122 GLU A OE2 1 ATOM 939 N N . PRO A 1 125 ? 17.703 16.555 23.247 1.00 38.27 ? 123 PRO A N 1 ATOM 940 C CA . PRO A 1 125 ? 17.094 15.680 24.218 1.00 38.25 ? 123 PRO A CA 1 ATOM 941 C C . PRO A 1 125 ? 16.078 14.745 23.576 1.00 36.28 ? 123 PRO A C 1 ATOM 942 O O . PRO A 1 125 ? 15.366 15.108 22.640 1.00 34.62 ? 123 PRO A O 1 ATOM 943 C CB . PRO A 1 125 ? 16.431 16.643 25.201 1.00 38.92 ? 123 PRO A CB 1 ATOM 944 C CG . PRO A 1 125 ? 17.118 17.912 25.046 1.00 39.48 ? 123 PRO A CG 1 ATOM 945 C CD . PRO A 1 125 ? 17.563 17.977 23.614 1.00 39.07 ? 123 PRO A CD 1 ATOM 946 N N . ARG A 1 126 ? 16.057 13.521 24.080 1.00 37.38 ? 124 ARG A N 1 ATOM 947 C CA . ARG A 1 126 ? 15.101 12.509 23.684 1.00 35.82 ? 124 ARG A CA 1 ATOM 948 C C . ARG A 1 126 ? 13.699 12.896 24.124 1.00 33.77 ? 124 ARG A C 1 ATOM 949 O O . ARG A 1 126 ? 12.736 12.650 23.386 1.00 31.84 ? 124 ARG A O 1 ATOM 950 C CB . ARG A 1 126 ? 15.501 11.166 24.314 1.00 39.04 ? 124 ARG A CB 1 ATOM 951 C CG . ARG A 1 126 ? 14.656 9.994 23.809 1.00 41.42 ? 124 ARG A CG 1 ATOM 952 C CD . ARG A 1 126 ? 15.184 8.656 24.324 1.00 47.83 ? 124 ARG A CD 1 ATOM 953 N NE . ARG A 1 126 ? 14.781 7.594 23.389 1.00 50.27 ? 124 ARG A NE 1 ATOM 954 C CZ . ARG A 1 126 ? 14.070 6.505 23.698 1.00 53.92 ? 124 ARG A CZ 1 ATOM 955 N NH1 . ARG A 1 126 ? 13.677 6.254 24.958 1.00 55.19 ? 124 ARG A NH1 1 ATOM 956 N NH2 . ARG A 1 126 ? 13.773 5.630 22.724 1.00 54.35 ? 124 ARG A NH2 1 ATOM 957 N N . ASP A 1 127 ? 13.589 13.528 25.297 1.00 34.09 ? 125 ASP A N 1 ATOM 958 C CA . ASP A 1 127 ? 12.283 13.843 25.897 1.00 33.73 ? 125 ASP A CA 1 ATOM 959 C C . ASP A 1 127 ? 11.784 15.256 25.526 1.00 31.85 ? 125 ASP A C 1 ATOM 960 O O . ASP A 1 127 ? 12.527 16.227 25.546 1.00 33.57 ? 125 ASP A O 1 ATOM 961 C CB . ASP A 1 127 ? 12.301 13.743 27.429 1.00 35.40 ? 125 ASP A CB 1 ATOM 962 C CG . ASP A 1 127 ? 12.438 12.296 27.977 1.00 40.36 ? 125 ASP A CG 1 ATOM 963 O OD1 . ASP A 1 127 ? 12.885 11.359 27.283 1.00 41.79 ? 125 ASP A OD1 1 ATOM 964 O OD2 . ASP A 1 127 ? 12.108 12.103 29.173 1.00 45.77 ? 125 ASP A OD2 1 ATOM 965 N N . LEU A 1 128 ? 10.497 15.353 25.268 1.00 30.11 ? 126 LEU A N 1 ATOM 966 C CA . LEU A 1 128 ? 9.802 16.618 25.035 1.00 29.10 ? 126 LEU A CA 1 ATOM 967 C C . LEU A 1 128 ? 8.685 16.704 26.039 1.00 29.30 ? 126 LEU A C 1 ATOM 968 O O . LEU A 1 128 ? 7.812 15.833 26.067 1.00 28.93 ? 126 LEU A O 1 ATOM 969 C CB . LEU A 1 128 ? 9.253 16.677 23.607 1.00 27.15 ? 126 LEU A CB 1 ATOM 970 C CG . LEU A 1 128 ? 8.392 17.877 23.187 1.00 27.38 ? 126 LEU A CG 1 ATOM 971 C CD1 . LEU A 1 128 ? 9.138 19.227 23.280 1.00 26.79 ? 126 LEU A CD1 1 ATOM 972 C CD2 . LEU A 1 128 ? 7.908 17.614 21.792 1.00 26.38 ? 126 LEU A CD2 1 ATOM 973 N N . ARG A 1 129 ? 8.734 17.738 26.868 1.00 30.39 ? 127 ARG A N 1 ATOM 974 C CA . ARG A 1 129 ? 7.794 17.951 27.957 1.00 33.13 ? 127 ARG A CA 1 ATOM 975 C C . ARG A 1 129 ? 6.645 18.905 27.548 1.00 32.17 ? 127 ARG A C 1 ATOM 976 O O . ARG A 1 129 ? 6.893 19.995 27.072 1.00 32.63 ? 127 ARG A O 1 ATOM 977 C CB . ARG A 1 129 ? 8.559 18.521 29.157 1.00 36.14 ? 127 ARG A CB 1 ATOM 978 C CG . ARG A 1 129 ? 7.974 18.184 30.520 1.00 42.78 ? 127 ARG A CG 1 ATOM 979 C CD . ARG A 1 129 ? 9.007 18.423 31.657 1.00 50.53 ? 127 ARG A CD 1 ATOM 980 N NE . ARG A 1 129 ? 10.029 17.358 31.709 1.00 54.91 ? 127 ARG A NE 1 ATOM 981 C CZ . ARG A 1 129 ? 11.241 17.463 32.269 1.00 59.67 ? 127 ARG A CZ 1 ATOM 982 N NH1 . ARG A 1 129 ? 11.659 18.592 32.840 1.00 61.84 ? 127 ARG A NH1 1 ATOM 983 N NH2 . ARG A 1 129 ? 12.060 16.416 32.259 1.00 61.98 ? 127 ARG A NH2 1 ATOM 984 N N . VAL A 1 130 ? 5.398 18.451 27.726 1.00 31.58 ? 128 VAL A N 1 ATOM 985 C CA A VAL A 1 130 ? 4.206 19.202 27.332 0.50 31.09 ? 128 VAL A CA 1 ATOM 986 C CA B VAL A 1 130 ? 4.196 19.199 27.334 0.50 30.97 ? 128 VAL A CA 1 ATOM 987 C C . VAL A 1 130 ? 3.154 19.101 28.444 1.00 32.56 ? 128 VAL A C 1 ATOM 988 O O . VAL A 1 130 ? 3.060 18.086 29.124 1.00 33.20 ? 128 VAL A O 1 ATOM 989 C CB A VAL A 1 130 ? 3.662 18.694 25.952 0.50 28.97 ? 128 VAL A CB 1 ATOM 990 C CB B VAL A 1 130 ? 3.572 18.680 25.993 0.50 28.88 ? 128 VAL A CB 1 ATOM 991 C CG1 A VAL A 1 130 ? 3.013 17.326 26.085 0.50 28.22 ? 128 VAL A CG1 1 ATOM 992 C CG1 B VAL A 1 130 ? 4.541 18.834 24.825 0.50 26.23 ? 128 VAL A CG1 1 ATOM 993 C CG2 A VAL A 1 130 ? 2.696 19.692 25.327 0.50 28.67 ? 128 VAL A CG2 1 ATOM 994 C CG2 B VAL A 1 130 ? 3.129 17.233 26.118 0.50 28.02 ? 128 VAL A CG2 1 ATOM 995 N N . ARG A 1 131 ? 2.389 20.171 28.649 1.00 33.82 ? 129 ARG A N 1 ATOM 996 C CA . ARG A 1 131 ? 1.319 20.172 29.641 1.00 35.56 ? 129 ARG A CA 1 ATOM 997 C C . ARG A 1 131 ? 0.028 19.749 28.962 1.00 33.81 ? 129 ARG A C 1 ATOM 998 O O . ARG A 1 131 ? -0.146 19.977 27.773 1.00 31.07 ? 129 ARG A O 1 ATOM 999 C CB . ARG A 1 131 ? 1.141 21.543 30.248 1.00 38.13 ? 129 ARG A CB 1 ATOM 1000 C CG . ARG A 1 131 ? 2.043 21.826 31.399 1.00 44.77 ? 129 ARG A CG 1 ATOM 1001 C CD . ARG A 1 131 ? 3.468 22.239 30.988 1.00 49.66 ? 129 ARG A CD 1 ATOM 1002 N NE . ARG A 1 131 ? 4.316 22.408 32.184 1.00 56.07 ? 129 ARG A NE 1 ATOM 1003 C CZ . ARG A 1 131 ? 5.649 22.293 32.212 1.00 59.33 ? 129 ARG A CZ 1 ATOM 1004 N NH1 . ARG A 1 131 ? 6.356 22.010 31.104 1.00 60.12 ? 129 ARG A NH1 1 ATOM 1005 N NH2 . ARG A 1 131 ? 6.283 22.457 33.362 1.00 61.94 ? 129 ARG A NH2 1 ATOM 1006 N N . VAL A 1 132 ? -0.860 19.113 29.723 1.00 35.06 ? 130 VAL A N 1 ATOM 1007 C CA . VAL A 1 132 ? -2.148 18.683 29.208 1.00 35.16 ? 130 VAL A CA 1 ATOM 1008 C C . VAL A 1 132 ? -2.837 19.926 28.658 1.00 36.87 ? 130 VAL A C 1 ATOM 1009 O O . VAL A 1 132 ? -2.772 21.020 29.262 1.00 37.79 ? 130 VAL A O 1 ATOM 1010 C CB . VAL A 1 132 ? -2.997 17.970 30.303 1.00 37.31 ? 130 VAL A CB 1 ATOM 1011 C CG1 . VAL A 1 132 ? -4.472 17.838 29.897 1.00 37.61 ? 130 VAL A CG1 1 ATOM 1012 C CG2 . VAL A 1 132 ? -2.455 16.622 30.581 1.00 35.60 ? 130 VAL A CG2 1 ATOM 1013 N N . GLY A 1 133 ? -3.408 19.798 27.464 1.00 36.74 ? 131 GLY A N 1 ATOM 1014 C CA . GLY A 1 133 ? -4.210 20.863 26.901 1.00 38.65 ? 131 GLY A CA 1 ATOM 1015 C C . GLY A 1 133 ? -3.413 21.742 25.970 1.00 39.29 ? 131 GLY A C 1 ATOM 1016 O O . GLY A 1 133 ? -3.992 22.511 25.216 1.00 40.52 ? 131 GLY A O 1 ATOM 1017 N N . ASP A 1 134 ? -2.086 21.640 26.010 1.00 38.73 ? 132 ASP A N 1 ATOM 1018 C CA . ASP A 1 134 ? -1.248 22.473 25.154 1.00 38.97 ? 132 ASP A CA 1 ATOM 1019 C C . ASP A 1 134 ? -1.056 21.862 23.764 1.00 37.05 ? 132 ASP A C 1 ATOM 1020 O O . ASP A 1 134 ? -1.368 20.712 23.498 1.00 35.16 ? 132 ASP A O 1 ATOM 1021 C CB . ASP A 1 134 ? 0.133 22.737 25.789 1.00 39.34 ? 132 ASP A CB 1 ATOM 1022 C CG . ASP A 1 134 ? 0.104 23.763 26.952 1.00 42.51 ? 132 ASP A CG 1 ATOM 1023 O OD1 . ASP A 1 134 ? -0.871 24.545 27.175 1.00 46.29 ? 132 ASP A OD1 1 ATOM 1024 O OD2 . ASP A 1 134 ? 1.125 23.799 27.655 1.00 44.24 ? 132 ASP A OD2 1 ATOM 1025 N N . THR A 1 135 ? -0.531 22.685 22.879 1.00 37.69 ? 133 THR A N 1 ATOM 1026 C CA . THR A 1 135 ? -0.195 22.293 21.548 1.00 36.72 ? 133 THR A CA 1 ATOM 1027 C C . THR A 1 135 ? 1.319 22.154 21.508 1.00 35.21 ? 133 THR A C 1 ATOM 1028 O O . THR A 1 135 ? 2.025 22.893 22.201 1.00 37.03 ? 133 THR A O 1 ATOM 1029 C CB . THR A 1 135 ? -0.663 23.375 20.576 1.00 38.23 ? 133 THR A CB 1 ATOM 1030 O OG1 . THR A 1 135 ? -2.094 23.304 20.487 1.00 41.57 ? 133 THR A OG1 1 ATOM 1031 C CG2 . THR A 1 135 ? -0.049 23.193 19.208 1.00 37.97 ? 133 THR A CG2 1 ATOM 1032 N N . THR A 1 136 ? 1.806 21.203 20.726 1.00 31.90 ? 134 THR A N 1 ATOM 1033 C CA . THR A 1 136 ? 3.231 21.060 20.498 1.00 31.03 ? 134 THR A CA 1 ATOM 1034 C C . THR A 1 136 ? 3.564 20.693 19.056 1.00 28.95 ? 134 THR A C 1 ATOM 1035 O O . THR A 1 136 ? 2.710 20.311 18.276 1.00 27.72 ? 134 THR A O 1 ATOM 1036 C CB . THR A 1 136 ? 3.907 20.041 21.501 1.00 30.65 ? 134 THR A CB 1 ATOM 1037 O OG1 . THR A 1 136 ? 5.320 20.293 21.550 1.00 33.12 ? 134 THR A OG1 1 ATOM 1038 C CG2 . THR A 1 136 ? 3.659 18.573 21.136 1.00 28.13 ? 134 THR A CG2 1 ATOM 1039 N N . GLN A 1 137 ? 4.824 20.874 18.713 1.00 29.87 ? 135 GLN A N 1 ATOM 1040 C CA . GLN A 1 137 ? 5.358 20.445 17.441 1.00 29.63 ? 135 GLN A CA 1 ATOM 1041 C C . GLN A 1 137 ? 6.236 19.264 17.728 1.00 28.80 ? 135 GLN A C 1 ATOM 1042 O O . GLN A 1 137 ? 6.816 19.165 18.798 1.00 29.19 ? 135 GLN A O 1 ATOM 1043 C CB . GLN A 1 137 ? 6.160 21.563 16.778 1.00 30.94 ? 135 GLN A CB 1 ATOM 1044 C CG . GLN A 1 137 ? 6.889 21.149 15.476 1.00 31.17 ? 135 GLN A CG 1 ATOM 1045 C CD . GLN A 1 137 ? 7.569 22.331 14.822 1.00 37.47 ? 135 GLN A CD 1 ATOM 1046 O OE1 . GLN A 1 137 ? 7.059 22.896 13.831 1.00 40.05 ? 135 GLN A OE1 1 ATOM 1047 N NE2 . GLN A 1 137 ? 8.717 22.750 15.392 1.00 37.51 ? 135 GLN A NE2 1 ATOM 1048 N N . MET A 1 138 ? 6.258 18.332 16.794 1.00 28.29 ? 136 MET A N 1 ATOM 1049 C CA . MET A 1 138 ? 7.271 17.317 16.755 1.00 28.35 ? 136 MET A CA 1 ATOM 1050 C C . MET A 1 138 ? 8.009 17.417 15.439 1.00 27.01 ? 136 MET A C 1 ATOM 1051 O O . MET A 1 138 ? 7.455 17.232 14.365 1.00 26.15 ? 136 MET A O 1 ATOM 1052 C CB . MET A 1 138 ? 6.656 15.958 16.988 1.00 29.09 ? 136 MET A CB 1 ATOM 1053 C CG . MET A 1 138 ? 6.320 15.779 18.468 1.00 35.23 ? 136 MET A CG 1 ATOM 1054 S SD . MET A 1 138 ? 5.377 14.317 18.624 1.00 43.74 ? 136 MET A SD 1 ATOM 1055 C CE . MET A 1 138 ? 3.770 14.993 18.206 1.00 48.54 ? 136 MET A CE 1 ATOM 1056 N N . ARG A 1 139 ? 9.281 17.718 15.560 1.00 27.07 ? 137 ARG A N 1 ATOM 1057 C CA . ARG A 1 139 ? 10.083 18.156 14.455 1.00 27.63 ? 137 ARG A CA 1 ATOM 1058 C C . ARG A 1 139 ? 10.886 17.006 13.932 1.00 26.98 ? 137 ARG A C 1 ATOM 1059 O O . ARG A 1 139 ? 11.314 16.175 14.694 1.00 25.55 ? 137 ARG A O 1 ATOM 1060 C CB . ARG A 1 139 ? 10.991 19.287 14.919 1.00 29.94 ? 137 ARG A CB 1 ATOM 1061 C CG . ARG A 1 139 ? 12.097 19.608 13.955 1.00 34.01 ? 137 ARG A CG 1 ATOM 1062 C CD . ARG A 1 139 ? 12.877 20.782 14.457 1.00 38.71 ? 137 ARG A CD 1 ATOM 1063 N NE . ARG A 1 139 ? 13.600 20.430 15.671 1.00 40.77 ? 137 ARG A NE 1 ATOM 1064 C CZ . ARG A 1 139 ? 14.050 21.321 16.545 1.00 42.43 ? 137 ARG A CZ 1 ATOM 1065 N NH1 . ARG A 1 139 ? 13.856 22.628 16.346 1.00 43.09 ? 137 ARG A NH1 1 ATOM 1066 N NH2 . ARG A 1 139 ? 14.692 20.898 17.621 1.00 43.89 ? 137 ARG A NH2 1 ATOM 1067 N N . CYS A 1 140 ? 11.016 16.951 12.606 1.00 27.08 ? 138 CYS A N 1 ATOM 1068 C CA . CYS A 1 140 ? 11.784 15.956 11.881 1.00 28.09 ? 138 CYS A CA 1 ATOM 1069 C C . CYS A 1 140 ? 12.086 16.478 10.458 1.00 27.01 ? 138 CYS A C 1 ATOM 1070 O O . CYS A 1 140 ? 11.178 16.694 9.673 1.00 26.03 ? 138 CYS A O 1 ATOM 1071 C CB . CYS A 1 140 ? 10.954 14.679 11.769 1.00 29.09 ? 138 CYS A CB 1 ATOM 1072 S SG . CYS A 1 140 ? 11.704 13.251 11.052 1.00 34.18 ? 138 CYS A SG 1 ATOM 1073 N N . SER A 1 141 ? 13.349 16.693 10.148 1.00 26.38 ? 139 SER A N 1 ATOM 1074 C CA . SER A 1 141 ? 13.722 17.282 8.882 1.00 27.71 ? 139 SER A CA 1 ATOM 1075 C C . SER A 1 141 ? 15.155 16.902 8.590 1.00 27.43 ? 139 SER A C 1 ATOM 1076 O O . SER A 1 141 ? 15.905 16.584 9.496 1.00 28.51 ? 139 SER A O 1 ATOM 1077 C CB . SER A 1 141 ? 13.523 18.805 8.919 1.00 27.92 ? 139 SER A CB 1 ATOM 1078 O OG . SER A 1 141 ? 14.448 19.449 9.789 1.00 31.30 ? 139 SER A OG 1 ATOM 1079 N N . ILE A 1 142 ? 15.537 16.864 7.325 1.00 26.65 ? 140 ILE A N 1 ATOM 1080 C CA . ILE A 1 142 ? 16.935 16.632 7.003 1.00 25.67 ? 140 ILE A CA 1 ATOM 1081 C C . ILE A 1 142 ? 17.585 17.952 6.629 1.00 25.34 ? 140 ILE A C 1 ATOM 1082 O O . ILE A 1 142 ? 17.066 18.677 5.787 1.00 25.11 ? 140 ILE A O 1 ATOM 1083 C CB . ILE A 1 142 ? 17.072 15.586 5.882 1.00 27.00 ? 140 ILE A CB 1 ATOM 1084 C CG1 . ILE A 1 142 ? 16.558 14.237 6.375 1.00 27.23 ? 140 ILE A CG1 1 ATOM 1085 C CG2 . ILE A 1 142 ? 18.555 15.424 5.366 1.00 25.86 ? 140 ILE A CG2 1 ATOM 1086 C CD1 . ILE A 1 142 ? 16.493 13.264 5.344 1.00 27.47 ? 140 ILE A CD1 1 ATOM 1087 N N . GLN A 1 143 ? 18.716 18.245 7.271 1.00 25.40 ? 141 GLN A N 1 ATOM 1088 C CA . GLN A 1 143 ? 19.592 19.377 6.930 1.00 26.05 ? 141 GLN A CA 1 ATOM 1089 C C . GLN A 1 143 ? 20.192 19.121 5.551 1.00 26.88 ? 141 GLN A C 1 ATOM 1090 O O . GLN A 1 143 ? 20.842 18.095 5.306 1.00 27.00 ? 141 GLN A O 1 ATOM 1091 C CB . GLN A 1 143 ? 20.701 19.537 7.984 1.00 26.06 ? 141 GLN A CB 1 ATOM 1092 C CG . GLN A 1 143 ? 21.676 20.655 7.730 1.00 27.87 ? 141 GLN A CG 1 ATOM 1093 C CD . GLN A 1 143 ? 21.088 22.052 7.906 1.00 26.54 ? 141 GLN A CD 1 ATOM 1094 O OE1 . GLN A 1 143 ? 20.407 22.587 7.012 1.00 24.43 ? 141 GLN A OE1 1 ATOM 1095 N NE2 . GLN A 1 143 ? 21.380 22.660 9.043 1.00 22.15 ? 141 GLN A NE2 1 ATOM 1096 N N . SER A 1 144 ? 19.977 20.082 4.662 1.00 27.69 ? 142 SER A N 1 ATOM 1097 C CA . SER A 1 144 ? 20.233 19.915 3.261 1.00 28.44 ? 142 SER A CA 1 ATOM 1098 C C . SER A 1 144 ? 20.438 21.259 2.566 1.00 29.80 ? 142 SER A C 1 ATOM 1099 O O . SER A 1 144 ? 19.789 22.234 2.870 1.00 29.14 ? 142 SER A O 1 ATOM 1100 C CB . SER A 1 144 ? 19.082 19.137 2.617 1.00 28.35 ? 142 SER A CB 1 ATOM 1101 O OG . SER A 1 144 ? 19.320 18.889 1.236 1.00 28.52 ? 142 SER A OG 1 ATOM 1102 N N . THR A 1 145 ? 21.373 21.266 1.623 1.00 30.90 ? 143 THR A N 1 ATOM 1103 C CA . THR A 1 145 ? 21.575 22.352 0.680 1.00 32.34 ? 143 THR A CA 1 ATOM 1104 C C . THR A 1 145 ? 20.645 22.240 -0.557 1.00 32.23 ? 143 THR A C 1 ATOM 1105 O O . THR A 1 145 ? 20.590 23.152 -1.382 1.00 33.04 ? 143 THR A O 1 ATOM 1106 C CB . THR A 1 145 ? 23.031 22.288 0.161 1.00 33.56 ? 143 THR A CB 1 ATOM 1107 O OG1 . THR A 1 145 ? 23.274 20.980 -0.352 1.00 31.93 ? 143 THR A OG1 1 ATOM 1108 C CG2 . THR A 1 145 ? 24.016 22.530 1.279 1.00 34.75 ? 143 THR A CG2 1 ATOM 1109 N N . GLU A 1 146 ? 19.948 21.117 -0.692 1.00 30.79 ? 144 GLU A N 1 ATOM 1110 C CA . GLU A 1 146 ? 19.168 20.824 -1.883 1.00 31.72 ? 144 GLU A CA 1 ATOM 1111 C C . GLU A 1 146 ? 17.687 20.624 -1.550 1.00 31.03 ? 144 GLU A C 1 ATOM 1112 O O . GLU A 1 146 ? 17.331 19.982 -0.548 1.00 30.38 ? 144 GLU A O 1 ATOM 1113 C CB . GLU A 1 146 ? 19.711 19.575 -2.568 1.00 32.72 ? 144 GLU A CB 1 ATOM 1114 C CG . GLU A 1 146 ? 21.196 19.609 -2.915 1.00 35.78 ? 144 GLU A CG 1 ATOM 1115 C CD . GLU A 1 146 ? 21.597 20.781 -3.829 1.00 42.64 ? 144 GLU A CD 1 ATOM 1116 O OE1 . GLU A 1 146 ? 20.924 20.984 -4.873 1.00 42.89 ? 144 GLU A OE1 1 ATOM 1117 O OE2 . GLU A 1 146 ? 22.620 21.473 -3.509 1.00 46.92 ? 144 GLU A OE2 1 ATOM 1118 N N . GLU A 1 147 ? 16.824 21.161 -2.404 1.00 32.06 ? 145 GLU A N 1 ATOM 1119 C CA . GLU A 1 147 ? 15.381 21.068 -2.216 1.00 31.78 ? 145 GLU A CA 1 ATOM 1120 C C . GLU A 1 147 ? 14.842 19.722 -2.671 1.00 30.77 ? 145 GLU A C 1 ATOM 1121 O O . GLU A 1 147 ? 15.464 19.042 -3.466 1.00 30.70 ? 145 GLU A O 1 ATOM 1122 C CB . GLU A 1 147 ? 14.668 22.183 -2.986 1.00 33.26 ? 145 GLU A CB 1 ATOM 1123 C CG . GLU A 1 147 ? 14.638 22.011 -4.538 1.00 38.57 ? 145 GLU A CG 1 ATOM 1124 C CD . GLU A 1 147 ? 13.790 23.071 -5.245 1.00 42.66 ? 145 GLU A CD 1 ATOM 1125 O OE1 . GLU A 1 147 ? 12.907 23.642 -4.558 1.00 40.66 ? 145 GLU A OE1 1 ATOM 1126 O OE2 . GLU A 1 147 ? 14.007 23.323 -6.482 1.00 48.15 ? 145 GLU A OE2 1 ATOM 1127 N N . LYS A 1 148 ? 13.676 19.344 -2.155 1.00 29.52 ? 146 LYS A N 1 ATOM 1128 C CA . LYS A 1 148 ? 12.915 18.238 -2.723 1.00 29.88 ? 146 LYS A CA 1 ATOM 1129 C C . LYS A 1 148 ? 13.697 16.910 -2.740 1.00 29.36 ? 146 LYS A C 1 ATOM 1130 O O . LYS A 1 148 ? 13.601 16.129 -3.663 1.00 29.51 ? 146 LYS A O 1 ATOM 1131 C CB . LYS A 1 148 ? 12.431 18.597 -4.154 1.00 31.73 ? 146 LYS A CB 1 ATOM 1132 C CG . LYS A 1 148 ? 11.326 19.640 -4.178 1.00 32.70 ? 146 LYS A CG 1 ATOM 1133 C CD . LYS A 1 148 ? 11.050 20.105 -5.596 1.00 37.78 ? 146 LYS A CD 1 ATOM 1134 C CE . LYS A 1 148 ? 10.096 21.283 -5.610 1.00 39.74 ? 146 LYS A CE 1 ATOM 1135 N NZ . LYS A 1 148 ? 9.963 21.894 -6.969 1.00 44.00 ? 146 LYS A NZ 1 ATOM 1136 N N . ARG A 1 149 ? 14.424 16.627 -1.678 1.00 28.05 ? 147 ARG A N 1 ATOM 1137 C CA . ARG A 1 149 ? 15.103 15.348 -1.601 1.00 28.15 ? 147 ARG A CA 1 ATOM 1138 C C . ARG A 1 149 ? 14.319 14.308 -0.826 1.00 27.37 ? 147 ARG A C 1 ATOM 1139 O O . ARG A 1 149 ? 14.362 13.130 -1.158 1.00 29.42 ? 147 ARG A O 1 ATOM 1140 C CB . ARG A 1 149 ? 16.499 15.560 -1.047 1.00 27.88 ? 147 ARG A CB 1 ATOM 1141 C CG . ARG A 1 149 ? 17.378 16.354 -1.968 1.00 28.60 ? 147 ARG A CG 1 ATOM 1142 C CD . ARG A 1 149 ? 17.364 15.791 -3.332 1.00 32.34 ? 147 ARG A CD 1 ATOM 1143 N NE . ARG A 1 149 ? 18.134 16.582 -4.274 1.00 36.30 ? 147 ARG A NE 1 ATOM 1144 C CZ . ARG A 1 149 ? 19.251 16.196 -4.880 1.00 36.92 ? 147 ARG A CZ 1 ATOM 1145 N NH1 . ARG A 1 149 ? 19.794 15.006 -4.651 1.00 38.58 ? 147 ARG A NH1 1 ATOM 1146 N NH2 . ARG A 1 149 ? 19.828 17.024 -5.731 1.00 37.81 ? 147 ARG A NH2 1 ATOM 1147 N N . VAL A 1 150 ? 13.570 14.736 0.172 1.00 26.22 ? 148 VAL A N 1 ATOM 1148 C CA . VAL A 1 150 ? 12.684 13.830 0.915 1.00 25.59 ? 148 VAL A CA 1 ATOM 1149 C C . VAL A 1 150 ? 11.498 13.320 0.076 1.00 27.09 ? 148 VAL A C 1 ATOM 1150 O O . VAL A 1 150 ? 10.732 14.116 -0.520 1.00 25.13 ? 148 VAL A O 1 ATOM 1151 C CB . VAL A 1 150 ? 12.207 14.526 2.250 1.00 24.65 ? 148 VAL A CB 1 ATOM 1152 C CG1 . VAL A 1 150 ? 11.020 13.820 2.885 1.00 22.96 ? 148 VAL A CG1 1 ATOM 1153 C CG2 . VAL A 1 150 ? 13.410 14.595 3.194 1.00 23.66 ? 148 VAL A CG2 1 ATOM 1154 N N . THR A 1 151 ? 11.368 11.987 0.050 1.00 28.29 ? 149 THR A N 1 ATOM 1155 C CA . THR A 1 151 ? 10.360 11.302 -0.755 1.00 30.17 ? 149 THR A CA 1 ATOM 1156 C C . THR A 1 151 ? 9.208 10.756 0.124 1.00 30.46 ? 149 THR A C 1 ATOM 1157 O O . THR A 1 151 ? 8.117 10.559 -0.376 1.00 29.63 ? 149 THR A O 1 ATOM 1158 C CB . THR A 1 151 ? 10.977 10.146 -1.564 1.00 31.45 ? 149 THR A CB 1 ATOM 1159 O OG1 . THR A 1 151 ? 11.638 9.245 -0.684 1.00 32.29 ? 149 THR A OG1 1 ATOM 1160 C CG2 . THR A 1 151 ? 12.005 10.648 -2.603 1.00 32.49 ? 149 THR A CG2 1 ATOM 1161 N N . LYS A 1 152 ? 9.454 10.549 1.425 1.00 29.48 ? 150 LYS A N 1 ATOM 1162 C CA . LYS A 1 152 ? 8.446 9.942 2.303 1.00 30.21 ? 150 LYS A CA 1 ATOM 1163 C C . LYS A 1 152 ? 8.708 10.351 3.746 1.00 28.40 ? 150 LYS A C 1 ATOM 1164 O O . LYS A 1 152 ? 9.877 10.522 4.155 1.00 28.24 ? 150 LYS A O 1 ATOM 1165 C CB . LYS A 1 152 ? 8.482 8.418 2.116 1.00 32.36 ? 150 LYS A CB 1 ATOM 1166 C CG . LYS A 1 152 ? 7.475 7.575 2.878 1.00 34.47 ? 150 LYS A CG 1 ATOM 1167 C CD . LYS A 1 152 ? 7.721 6.100 2.541 1.00 40.88 ? 150 LYS A CD 1 ATOM 1168 C CE . LYS A 1 152 ? 6.980 5.130 3.486 1.00 44.19 ? 150 LYS A CE 1 ATOM 1169 N NZ . LYS A 1 152 ? 5.697 4.594 2.928 1.00 50.29 ? 150 LYS A NZ 1 ATOM 1170 N N . VAL A 1 153 ? 7.617 10.592 4.482 1.00 27.60 ? 151 VAL A N 1 ATOM 1171 C CA . VAL A 1 153 ? 7.626 10.831 5.921 1.00 26.05 ? 151 VAL A CA 1 ATOM 1172 C C . VAL A 1 153 ? 6.508 9.990 6.554 1.00 26.38 ? 151 VAL A C 1 ATOM 1173 O O . VAL A 1 153 ? 5.375 10.005 6.093 1.00 26.25 ? 151 VAL A O 1 ATOM 1174 C CB . VAL A 1 153 ? 7.331 12.286 6.294 1.00 25.70 ? 151 VAL A CB 1 ATOM 1175 C CG1 . VAL A 1 153 ? 7.350 12.436 7.837 1.00 27.27 ? 151 VAL A CG1 1 ATOM 1176 C CG2 . VAL A 1 153 ? 8.338 13.233 5.688 1.00 25.49 ? 151 VAL A CG2 1 ATOM 1177 N N . ASN A 1 154 ? 6.836 9.284 7.619 1.00 26.02 ? 152 ASN A N 1 ATOM 1178 C CA . ASN A 1 154 ? 5.884 8.441 8.341 1.00 26.60 ? 152 ASN A CA 1 ATOM 1179 C C . ASN A 1 154 ? 6.109 8.717 9.827 1.00 24.62 ? 152 ASN A C 1 ATOM 1180 O O . ASN A 1 154 ? 7.248 8.661 10.289 1.00 23.32 ? 152 ASN A O 1 ATOM 1181 C CB . ASN A 1 154 ? 6.132 6.972 7.972 1.00 29.07 ? 152 ASN A CB 1 ATOM 1182 C CG . ASN A 1 154 ? 5.110 6.033 8.551 1.00 33.14 ? 152 ASN A CG 1 ATOM 1183 O OD1 . ASN A 1 154 ? 5.423 5.245 9.442 1.00 40.17 ? 152 ASN A OD1 1 ATOM 1184 N ND2 . ASN A 1 154 ? 3.887 6.095 8.047 1.00 36.93 ? 152 ASN A ND2 1 ATOM 1185 N N . TRP A 1 155 ? 5.044 9.088 10.541 1.00 23.19 ? 153 TRP A N 1 ATOM 1186 C CA . TRP A 1 155 ? 5.055 9.195 11.989 1.00 22.84 ? 153 TRP A CA 1 ATOM 1187 C C . TRP A 1 155 ? 4.256 8.069 12.606 1.00 23.52 ? 153 TRP A C 1 ATOM 1188 O O . TRP A 1 155 ? 3.156 7.811 12.178 1.00 22.91 ? 153 TRP A O 1 ATOM 1189 C CB . TRP A 1 155 ? 4.467 10.547 12.448 1.00 23.14 ? 153 TRP A CB 1 ATOM 1190 C CG . TRP A 1 155 ? 5.365 11.746 12.226 1.00 21.64 ? 153 TRP A CG 1 ATOM 1191 C CD1 . TRP A 1 155 ? 5.433 12.546 11.101 1.00 21.99 ? 153 TRP A CD1 1 ATOM 1192 C CD2 . TRP A 1 155 ? 6.314 12.274 13.154 1.00 21.35 ? 153 TRP A CD2 1 ATOM 1193 N NE1 . TRP A 1 155 ? 6.379 13.542 11.289 1.00 21.17 ? 153 TRP A NE1 1 ATOM 1194 C CE2 . TRP A 1 155 ? 6.928 13.397 12.541 1.00 21.28 ? 153 TRP A CE2 1 ATOM 1195 C CE3 . TRP A 1 155 ? 6.727 11.891 14.443 1.00 21.24 ? 153 TRP A CE3 1 ATOM 1196 C CZ2 . TRP A 1 155 ? 7.913 14.165 13.197 1.00 22.80 ? 153 TRP A CZ2 1 ATOM 1197 C CZ3 . TRP A 1 155 ? 7.670 12.638 15.088 1.00 21.79 ? 153 TRP A CZ3 1 ATOM 1198 C CH2 . TRP A 1 155 ? 8.284 13.761 14.454 1.00 22.14 ? 153 TRP A CH2 1 ATOM 1199 N N . MET A 1 156 ? 4.842 7.396 13.599 1.00 24.27 ? 154 MET A N 1 ATOM 1200 C CA . MET A 1 156 ? 4.201 6.319 14.342 1.00 25.54 ? 154 MET A CA 1 ATOM 1201 C C . MET A 1 156 ? 4.194 6.690 15.790 1.00 24.63 ? 154 MET A C 1 ATOM 1202 O O . MET A 1 156 ? 5.035 7.484 16.243 1.00 21.94 ? 154 MET A O 1 ATOM 1203 C CB . MET A 1 156 ? 4.993 5.013 14.269 1.00 27.56 ? 154 MET A CB 1 ATOM 1204 C CG . MET A 1 156 ? 5.220 4.468 12.900 1.00 33.31 ? 154 MET A CG 1 ATOM 1205 S SD . MET A 1 156 ? 3.702 3.821 12.214 1.00 40.74 ? 154 MET A SD 1 ATOM 1206 C CE . MET A 1 156 ? 3.738 2.105 12.655 1.00 44.16 ? 154 MET A CE 1 ATOM 1207 N N . PHE A 1 157 ? 3.259 6.075 16.516 1.00 25.29 ? 155 PHE A N 1 ATOM 1208 C CA . PHE A 1 157 ? 3.128 6.227 17.964 1.00 24.89 ? 155 PHE A CA 1 ATOM 1209 C C . PHE A 1 157 ? 3.005 4.883 18.650 1.00 26.86 ? 155 PHE A C 1 ATOM 1210 O O . PHE A 1 157 ? 2.268 4.002 18.204 1.00 26.34 ? 155 PHE A O 1 ATOM 1211 C CB . PHE A 1 157 ? 1.877 7.029 18.303 1.00 24.78 ? 155 PHE A CB 1 ATOM 1212 C CG . PHE A 1 157 ? 1.578 7.130 19.797 1.00 25.34 ? 155 PHE A CG 1 ATOM 1213 C CD1 . PHE A 1 157 ? 2.374 7.886 20.629 1.00 26.15 ? 155 PHE A CD1 1 ATOM 1214 C CD2 . PHE A 1 157 ? 0.472 6.495 20.346 1.00 28.01 ? 155 PHE A CD2 1 ATOM 1215 C CE1 . PHE A 1 157 ? 2.073 8.010 21.972 1.00 24.59 ? 155 PHE A CE1 1 ATOM 1216 C CE2 . PHE A 1 157 ? 0.168 6.617 21.685 1.00 28.44 ? 155 PHE A CE2 1 ATOM 1217 C CZ . PHE A 1 157 ? 0.947 7.376 22.493 1.00 28.41 ? 155 PHE A CZ 1 ATOM 1218 N N . SER A 1 158 ? 3.673 4.783 19.791 1.00 27.84 ? 156 SER A N 1 ATOM 1219 C CA . SER A 1 158 ? 3.439 3.737 20.741 1.00 30.62 ? 156 SER A CA 1 ATOM 1220 C C . SER A 1 158 ? 3.432 4.309 22.165 1.00 31.10 ? 156 SER A C 1 ATOM 1221 O O . SER A 1 158 ? 4.276 5.097 22.504 1.00 29.02 ? 156 SER A O 1 ATOM 1222 C CB . SER A 1 158 ? 4.541 2.707 20.627 1.00 31.58 ? 156 SER A CB 1 ATOM 1223 O OG . SER A 1 158 ? 4.146 1.547 21.320 1.00 39.33 ? 156 SER A OG 1 ATOM 1224 N N . SER A 1 159 ? 2.514 3.870 23.011 1.00 33.36 ? 157 SER A N 1 ATOM 1225 C CA . SER A 1 159 ? 2.672 4.079 24.439 1.00 36.91 ? 157 SER A CA 1 ATOM 1226 C C . SER A 1 159 ? 3.455 2.897 25.057 1.00 40.42 ? 157 SER A C 1 ATOM 1227 O O . SER A 1 159 ? 3.787 1.933 24.359 1.00 42.32 ? 157 SER A O 1 ATOM 1228 C CB . SER A 1 159 ? 1.308 4.246 25.097 1.00 37.08 ? 157 SER A CB 1 ATOM 1229 O OG . SER A 1 159 ? 0.720 2.986 25.262 1.00 41.06 ? 157 SER A OG 1 ATOM 1230 N N . GLY A 1 160 ? 3.754 2.960 26.353 1.00 43.65 ? 158 GLY A N 1 ATOM 1231 C CA . GLY A 1 160 ? 4.397 1.804 27.067 1.00 47.55 ? 158 GLY A CA 1 ATOM 1232 C C . GLY A 1 160 ? 3.623 0.478 27.013 1.00 50.84 ? 158 GLY A C 1 ATOM 1233 O O . GLY A 1 160 ? 4.212 -0.616 27.007 1.00 52.76 ? 158 GLY A O 1 ATOM 1234 N N . SER A 1 161 ? 2.293 0.603 26.937 1.00 52.37 ? 159 SER A N 1 ATOM 1235 C CA . SER A 1 161 ? 1.323 -0.523 26.895 1.00 55.22 ? 159 SER A CA 1 ATOM 1236 C C . SER A 1 161 ? 0.904 -1.012 25.479 1.00 55.46 ? 159 SER A C 1 ATOM 1237 O O . SER A 1 161 ? 0.061 -1.903 25.346 1.00 58.25 ? 159 SER A O 1 ATOM 1238 C CB . SER A 1 161 ? 0.049 -0.101 27.662 1.00 55.32 ? 159 SER A CB 1 ATOM 1239 O OG . SER A 1 161 ? -0.450 1.160 27.181 1.00 53.31 ? 159 SER A OG 1 ATOM 1240 N N . HIS A 1 162 ? 1.468 -0.448 24.420 1.00 54.01 ? 160 HIS A N 1 ATOM 1241 C CA . HIS A 1 162 ? 1.075 -0.876 23.073 1.00 54.36 ? 160 HIS A CA 1 ATOM 1242 C C . HIS A 1 162 ? 1.668 -2.227 22.682 1.00 57.02 ? 160 HIS A C 1 ATOM 1243 O O . HIS A 1 162 ? 2.852 -2.516 22.912 1.00 56.12 ? 160 HIS A O 1 ATOM 1244 C CB . HIS A 1 162 ? 1.465 0.161 22.019 1.00 51.65 ? 160 HIS A CB 1 ATOM 1245 C CG . HIS A 1 162 ? 0.523 1.318 21.914 1.00 49.99 ? 160 HIS A CG 1 ATOM 1246 N ND1 . HIS A 1 162 ? 0.166 1.885 20.709 1.00 50.73 ? 160 HIS A ND1 1 ATOM 1247 C CD2 . HIS A 1 162 ? -0.120 2.031 22.863 1.00 49.49 ? 160 HIS A CD2 1 ATOM 1248 C CE1 . HIS A 1 162 ? -0.658 2.891 20.920 1.00 47.32 ? 160 HIS A CE1 1 ATOM 1249 N NE2 . HIS A 1 162 ? -0.829 3.016 22.220 1.00 47.85 ? 160 HIS A NE2 1 ATOM 1250 N N . THR A 1 163 ? 0.818 -3.042 22.077 1.00 59.89 ? 161 THR A N 1 ATOM 1251 C CA . THR A 1 163 ? 1.255 -4.266 21.400 1.00 63.52 ? 161 THR A CA 1 ATOM 1252 C C . THR A 1 163 ? 1.759 -3.903 20.006 1.00 62.20 ? 161 THR A C 1 ATOM 1253 O O . THR A 1 163 ? 2.559 -4.642 19.405 1.00 64.09 ? 161 THR A O 1 ATOM 1254 C CB . THR A 1 163 ? 0.111 -5.301 21.279 1.00 66.65 ? 161 THR A CB 1 ATOM 1255 O OG1 . THR A 1 163 ? -0.283 -5.744 22.588 1.00 68.82 ? 161 THR A OG1 1 ATOM 1256 C CG2 . THR A 1 163 ? 0.556 -6.509 20.441 1.00 70.56 ? 161 THR A CG2 1 ATOM 1257 N N . GLU A 1 164 ? 1.286 -2.765 19.495 1.00 59.48 ? 162 GLU A N 1 ATOM 1258 C CA . GLU A 1 164 ? 1.631 -2.329 18.140 1.00 58.01 ? 162 GLU A CA 1 ATOM 1259 C C . GLU A 1 164 ? 1.660 -0.798 18.058 1.00 53.18 ? 162 GLU A C 1 ATOM 1260 O O . GLU A 1 164 ? 0.917 -0.100 18.732 1.00 51.67 ? 162 GLU A O 1 ATOM 1261 C CB . GLU A 1 164 ? 0.646 -2.936 17.103 1.00 60.35 ? 162 GLU A CB 1 ATOM 1262 C CG . GLU A 1 164 ? 1.300 -3.453 15.801 1.00 64.00 ? 162 GLU A CG 1 ATOM 1263 C CD . GLU A 1 164 ? 0.698 -4.788 15.313 1.00 71.68 ? 162 GLU A CD 1 ATOM 1264 O OE1 . GLU A 1 164 ? 0.661 -5.765 16.109 1.00 78.11 ? 162 GLU A OE1 1 ATOM 1265 O OE2 . GLU A 1 164 ? 0.271 -4.872 14.132 1.00 73.71 ? 162 GLU A OE2 1 ATOM 1266 N N . GLU A 1 165 ? 2.595 -0.315 17.258 1.00 50.82 ? 163 GLU A N 1 ATOM 1267 C CA . GLU A 1 165 ? 2.625 1.032 16.798 1.00 47.59 ? 163 GLU A CA 1 ATOM 1268 C C . GLU A 1 165 ? 1.365 1.381 16.020 1.00 46.23 ? 163 GLU A C 1 ATOM 1269 O O . GLU A 1 165 ? 0.867 0.568 15.242 1.00 47.44 ? 163 GLU A O 1 ATOM 1270 C CB . GLU A 1 165 ? 3.749 1.166 15.800 1.00 47.50 ? 163 GLU A CB 1 ATOM 1271 C CG . GLU A 1 165 ? 5.071 1.340 16.381 1.00 49.35 ? 163 GLU A CG 1 ATOM 1272 C CD . GLU A 1 165 ? 6.123 1.013 15.389 1.00 52.67 ? 163 GLU A CD 1 ATOM 1273 O OE1 . GLU A 1 165 ? 5.840 0.185 14.472 1.00 56.61 ? 163 GLU A OE1 1 ATOM 1274 O OE2 . GLU A 1 165 ? 7.232 1.575 15.542 1.00 53.90 ? 163 GLU A OE2 1 ATOM 1275 N N . GLU A 1 166 ? 0.904 2.613 16.163 1.00 42.36 ? 164 GLU A N 1 ATOM 1276 C CA . GLU A 1 166 ? -0.148 3.092 15.298 1.00 41.16 ? 164 GLU A CA 1 ATOM 1277 C C . GLU A 1 166 ? 0.345 4.286 14.503 1.00 36.58 ? 164 GLU A C 1 ATOM 1278 O O . GLU A 1 166 ? 1.270 4.964 14.942 1.00 32.54 ? 164 GLU A O 1 ATOM 1279 C CB . GLU A 1 166 ? -1.395 3.411 16.092 1.00 42.13 ? 164 GLU A CB 1 ATOM 1280 C CG . GLU A 1 166 ? -1.210 4.402 17.155 1.00 43.64 ? 164 GLU A CG 1 ATOM 1281 C CD . GLU A 1 166 ? -2.533 4.756 17.767 1.00 49.98 ? 164 GLU A CD 1 ATOM 1282 O OE1 . GLU A 1 166 ? -3.203 5.638 17.164 1.00 52.35 ? 164 GLU A OE1 1 ATOM 1283 O OE2 . GLU A 1 166 ? -2.898 4.136 18.814 1.00 51.62 ? 164 GLU A OE2 1 ATOM 1284 N N . THR A 1 167 ? -0.265 4.503 13.334 1.00 34.45 ? 165 THR A N 1 ATOM 1285 C CA . THR A 1 167 ? 0.162 5.553 12.407 1.00 33.07 ? 165 THR A CA 1 ATOM 1286 C C . THR A 1 167 ? -0.436 6.896 12.860 1.00 30.34 ? 165 THR A C 1 ATOM 1287 O O . THR A 1 167 ? -1.633 7.013 13.069 1.00 32.28 ? 165 THR A O 1 ATOM 1288 C CB . THR A 1 167 ? -0.212 5.214 10.930 1.00 34.93 ? 165 THR A CB 1 ATOM 1289 O OG1 . THR A 1 167 ? 0.379 3.962 10.562 1.00 38.45 ? 165 THR A OG1 1 ATOM 1290 C CG2 . THR A 1 167 ? 0.315 6.292 9.926 1.00 32.83 ? 165 THR A CG2 1 ATOM 1291 N N . VAL A 1 168 ? 0.411 7.891 13.055 1.00 27.27 ? 166 VAL A N 1 ATOM 1292 C CA . VAL A 1 168 ? -0.020 9.247 13.406 1.00 25.75 ? 166 VAL A CA 1 ATOM 1293 C C . VAL A 1 168 ? -0.283 10.059 12.142 1.00 26.37 ? 166 VAL A C 1 ATOM 1294 O O . VAL A 1 168 ? -1.345 10.667 11.967 1.00 26.99 ? 166 VAL A O 1 ATOM 1295 C CB . VAL A 1 168 ? 1.061 9.981 14.222 1.00 23.44 ? 166 VAL A CB 1 ATOM 1296 C CG1 . VAL A 1 168 ? 0.596 11.376 14.539 1.00 20.97 ? 166 VAL A CG1 1 ATOM 1297 C CG2 . VAL A 1 168 ? 1.371 9.219 15.469 1.00 23.09 ? 166 VAL A CG2 1 ATOM 1298 N N . LEU A 1 169 ? 0.709 10.046 11.256 1.00 26.48 ? 167 LEU A N 1 ATOM 1299 C CA . LEU A 1 169 ? 0.640 10.801 9.997 1.00 27.01 ? 167 LEU A CA 1 ATOM 1300 C C . LEU A 1 169 ? 1.601 10.175 9.030 1.00 26.83 ? 167 LEU A C 1 ATOM 1301 O O . LEU A 1 169 ? 2.670 9.756 9.415 1.00 25.10 ? 167 LEU A O 1 ATOM 1302 C CB . LEU A 1 169 ? 0.973 12.284 10.204 1.00 26.35 ? 167 LEU A CB 1 ATOM 1303 C CG . LEU A 1 169 ? 0.761 13.249 9.026 1.00 26.09 ? 167 LEU A CG 1 ATOM 1304 C CD1 . LEU A 1 169 ? 0.042 14.574 9.445 1.00 27.49 ? 167 LEU A CD1 1 ATOM 1305 C CD2 . LEU A 1 169 ? 2.087 13.527 8.342 1.00 24.96 ? 167 LEU A CD2 1 ATOM 1306 N N . SER A 1 170 ? 1.195 10.123 7.771 1.00 27.73 ? 168 SER A N 1 ATOM 1307 C CA . SER A 1 170 ? 2.017 9.588 6.721 1.00 28.89 ? 168 SER A CA 1 ATOM 1308 C C . SER A 1 170 ? 1.886 10.426 5.429 1.00 29.46 ? 168 SER A C 1 ATOM 1309 O O . SER A 1 170 ? 0.799 10.834 5.020 1.00 27.86 ? 168 SER A O 1 ATOM 1310 C CB . SER A 1 170 ? 1.602 8.135 6.476 1.00 31.21 ? 168 SER A CB 1 ATOM 1311 O OG . SER A 1 170 ? 2.248 7.639 5.346 1.00 34.27 ? 168 SER A OG 1 ATOM 1312 N N . TYR A 1 171 ? 3.025 10.700 4.815 1.00 29.50 ? 169 TYR A N 1 ATOM 1313 C CA . TYR A 1 171 ? 3.074 11.410 3.557 1.00 31.58 ? 169 TYR A CA 1 ATOM 1314 C C . TYR A 1 171 ? 4.041 10.669 2.634 1.00 31.72 ? 169 TYR A C 1 ATOM 1315 O O . TYR A 1 171 ? 5.171 10.381 3.023 1.00 29.86 ? 169 TYR A O 1 ATOM 1316 C CB . TYR A 1 171 ? 3.509 12.883 3.753 1.00 32.17 ? 169 TYR A CB 1 ATOM 1317 C CG . TYR A 1 171 ? 3.475 13.661 2.444 1.00 35.45 ? 169 TYR A CG 1 ATOM 1318 C CD1 . TYR A 1 171 ? 4.515 13.571 1.534 1.00 36.90 ? 169 TYR A CD1 1 ATOM 1319 C CD2 . TYR A 1 171 ? 2.360 14.411 2.091 1.00 40.68 ? 169 TYR A CD2 1 ATOM 1320 C CE1 . TYR A 1 171 ? 4.474 14.235 0.321 1.00 38.66 ? 169 TYR A CE1 1 ATOM 1321 C CE2 . TYR A 1 171 ? 2.298 15.072 0.870 1.00 43.35 ? 169 TYR A CE2 1 ATOM 1322 C CZ . TYR A 1 171 ? 3.373 14.979 -0.007 1.00 42.22 ? 169 TYR A CZ 1 ATOM 1323 O OH . TYR A 1 171 ? 3.318 15.635 -1.220 1.00 46.01 ? 169 TYR A OH 1 ATOM 1324 N N . ASP A 1 172 ? 3.597 10.339 1.432 1.00 33.48 ? 170 ASP A N 1 ATOM 1325 C CA . ASP A 1 172 ? 4.461 9.698 0.460 1.00 35.70 ? 170 ASP A CA 1 ATOM 1326 C C . ASP A 1 172 ? 4.416 10.465 -0.854 1.00 38.06 ? 170 ASP A C 1 ATOM 1327 O O . ASP A 1 172 ? 3.393 10.554 -1.493 1.00 39.32 ? 170 ASP A O 1 ATOM 1328 C CB . ASP A 1 172 ? 4.065 8.254 0.250 1.00 37.47 ? 170 ASP A CB 1 ATOM 1329 C CG . ASP A 1 172 ? 5.056 7.498 -0.628 1.00 40.31 ? 170 ASP A CG 1 ATOM 1330 O OD1 . ASP A 1 172 ? 5.742 8.128 -1.443 1.00 38.86 ? 170 ASP A OD1 1 ATOM 1331 O OD2 . ASP A 1 172 ? 5.134 6.257 -0.523 1.00 43.98 ? 170 ASP A OD2 1 ATOM 1332 N N . SER A 1 173 ? 5.561 11.018 -1.244 1.00 38.86 ? 171 SER A N 1 ATOM 1333 C CA . SER A 1 173 ? 5.651 11.892 -2.411 1.00 41.60 ? 171 SER A CA 1 ATOM 1334 C C . SER A 1 173 ? 5.478 11.155 -3.743 1.00 44.47 ? 171 SER A C 1 ATOM 1335 O O . SER A 1 173 ? 5.204 11.783 -4.749 1.00 46.56 ? 171 SER A O 1 ATOM 1336 C CB . SER A 1 173 ? 7.000 12.606 -2.413 1.00 40.50 ? 171 SER A CB 1 ATOM 1337 O OG . SER A 1 173 ? 7.958 11.693 -2.901 1.00 43.46 ? 171 SER A OG 1 ATOM 1338 N N . ASN A 1 174 ? 5.626 9.830 -3.734 1.00 46.23 ? 172 ASN A N 1 ATOM 1339 C CA . ASN A 1 174 ? 5.526 8.986 -4.922 1.00 49.66 ? 172 ASN A CA 1 ATOM 1340 C C . ASN A 1 174 ? 4.173 8.256 -5.016 1.00 52.67 ? 172 ASN A C 1 ATOM 1341 O O . ASN A 1 174 ? 4.046 7.250 -5.701 1.00 55.23 ? 172 ASN A O 1 ATOM 1342 C CB . ASN A 1 174 ? 6.678 7.957 -4.926 1.00 50.20 ? 172 ASN A CB 1 ATOM 1343 C CG . ASN A 1 174 ? 7.994 8.537 -5.452 1.00 50.39 ? 172 ASN A CG 1 ATOM 1344 O OD1 . ASN A 1 174 ? 8.087 8.928 -6.615 1.00 56.54 ? 172 ASN A OD1 1 ATOM 1345 N ND2 . ASN A 1 174 ? 9.009 8.580 -4.609 1.00 49.53 ? 172 ASN A ND2 1 ATOM 1346 N N . MET A 1 175 ? 3.175 8.761 -4.301 1.00 52.50 ? 173 MET A N 1 ATOM 1347 C CA . MET A 1 175 ? 1.811 8.298 -4.422 1.00 55.37 ? 173 MET A CA 1 ATOM 1348 C C . MET A 1 175 ? 0.972 9.484 -4.881 1.00 56.65 ? 173 MET A C 1 ATOM 1349 O O . MET A 1 175 ? 1.265 10.637 -4.520 1.00 55.05 ? 173 MET A O 1 ATOM 1350 C CB . MET A 1 175 ? 1.306 7.807 -3.058 1.00 54.25 ? 173 MET A CB 1 ATOM 1351 C CG . MET A 1 175 ? 1.839 6.454 -2.658 1.00 54.79 ? 173 MET A CG 1 ATOM 1352 S SD . MET A 1 175 ? 1.386 6.004 -0.982 1.00 57.46 ? 173 MET A SD 1 ATOM 1353 C CE . MET A 1 175 ? 1.899 4.298 -1.000 1.00 53.01 ? 173 MET A CE 1 ATOM 1354 N N . ARG A 1 176 ? -0.055 9.205 -5.682 1.00 60.32 ? 174 ARG A N 1 ATOM 1355 C CA . ARG A 1 176 ? -1.122 10.182 -5.952 1.00 62.25 ? 174 ARG A CA 1 ATOM 1356 C C . ARG A 1 176 ? -1.847 10.526 -4.652 1.00 60.41 ? 174 ARG A C 1 ATOM 1357 O O . ARG A 1 176 ? -2.313 11.645 -4.490 1.00 60.16 ? 174 ARG A O 1 ATOM 1358 C CB . ARG A 1 176 ? -2.156 9.654 -6.960 1.00 66.29 ? 174 ARG A CB 1 ATOM 1359 C CG . ARG A 1 176 ? -1.624 9.287 -8.332 1.00 70.10 ? 174 ARG A CG 1 ATOM 1360 C CD . ARG A 1 176 ? -2.768 9.005 -9.231 1.00 76.33 ? 174 ARG A CD 1 ATOM 1361 N NE . ARG A 1 176 ? -2.433 8.273 -10.451 1.00 81.29 ? 174 ARG A NE 1 ATOM 1362 C CZ . ARG A 1 176 ? -2.037 8.821 -11.600 1.00 84.66 ? 174 ARG A CZ 1 ATOM 1363 N NH1 . ARG A 1 176 ? -1.859 10.137 -11.725 1.00 83.37 ? 174 ARG A NH1 1 ATOM 1364 N NH2 . ARG A 1 176 ? -1.791 8.029 -12.638 1.00 88.57 ? 174 ARG A NH2 1 ATOM 1365 N N . SER A 1 177 ? -1.941 9.551 -3.745 1.00 59.90 ? 175 SER A N 1 ATOM 1366 C CA . SER A 1 177 ? -2.607 9.722 -2.433 1.00 59.27 ? 175 SER A CA 1 ATOM 1367 C C . SER A 1 177 ? -2.074 10.901 -1.623 1.00 55.89 ? 175 SER A C 1 ATOM 1368 O O . SER A 1 177 ? -2.830 11.744 -1.164 1.00 57.37 ? 175 SER A O 1 ATOM 1369 C CB . SER A 1 177 ? -2.502 8.418 -1.590 1.00 58.80 ? 175 SER A CB 1 ATOM 1370 O OG . SER A 1 177 ? -2.823 7.252 -2.377 1.00 62.50 ? 175 SER A OG 1 ATOM 1371 N N . GLY A 1 178 ? -0.773 10.951 -1.423 1.00 53.30 ? 176 GLY A N 1 ATOM 1372 C CA . GLY A 1 178 ? -0.169 12.046 -0.666 1.00 49.99 ? 176 GLY A CA 1 ATOM 1373 C C . GLY A 1 178 ? -0.185 11.919 0.846 1.00 47.25 ? 176 GLY A C 1 ATOM 1374 O O . GLY A 1 178 ? 0.778 11.395 1.420 1.00 46.16 ? 176 GLY A O 1 ATOM 1375 N N . LYS A 1 179 ? -1.247 12.413 1.502 1.00 44.82 ? 177 LYS A N 1 ATOM 1376 C CA . LYS A 1 179 ? -1.191 12.592 2.951 1.00 41.20 ? 177 LYS A CA 1 ATOM 1377 C C . LYS A 1 179 ? -2.260 11.822 3.707 1.00 39.34 ? 177 LYS A C 1 ATOM 1378 O O . LYS A 1 179 ? -3.425 11.989 3.424 1.00 39.80 ? 177 LYS A O 1 ATOM 1379 C CB . LYS A 1 179 ? -1.302 14.059 3.331 1.00 41.05 ? 177 LYS A CB 1 ATOM 1380 C CG . LYS A 1 179 ? -1.273 14.246 4.835 1.00 40.92 ? 177 LYS A CG 1 ATOM 1381 C CD . LYS A 1 179 ? -0.989 15.677 5.240 1.00 43.38 ? 177 LYS A CD 1 ATOM 1382 C CE . LYS A 1 179 ? -2.212 16.546 5.181 1.00 46.50 ? 177 LYS A CE 1 ATOM 1383 N NZ . LYS A 1 179 ? -1.907 17.972 5.588 1.00 48.93 ? 177 LYS A NZ 1 ATOM 1384 N N . PHE A 1 180 ? -1.856 10.992 4.667 1.00 35.62 ? 178 PHE A N 1 ATOM 1385 C CA . PHE A 1 180 ? -2.821 10.304 5.542 1.00 35.25 ? 178 PHE A CA 1 ATOM 1386 C C . PHE A 1 180 ? -2.641 10.803 6.964 1.00 31.70 ? 178 PHE A C 1 ATOM 1387 O O . PHE A 1 180 ? -1.519 10.874 7.453 1.00 27.29 ? 178 PHE A O 1 ATOM 1388 C CB . PHE A 1 180 ? -2.670 8.775 5.487 1.00 36.70 ? 178 PHE A CB 1 ATOM 1389 C CG . PHE A 1 180 ? -3.533 8.038 6.506 1.00 38.72 ? 178 PHE A CG 1 ATOM 1390 C CD1 . PHE A 1 180 ? -4.861 7.777 6.244 1.00 42.28 ? 178 PHE A CD1 1 ATOM 1391 C CD2 . PHE A 1 180 ? -3.008 7.648 7.756 1.00 40.56 ? 178 PHE A CD2 1 ATOM 1392 C CE1 . PHE A 1 180 ? -5.665 7.129 7.176 1.00 44.16 ? 178 PHE A CE1 1 ATOM 1393 C CE2 . PHE A 1 180 ? -3.821 6.978 8.689 1.00 39.98 ? 178 PHE A CE2 1 ATOM 1394 C CZ . PHE A 1 180 ? -5.149 6.738 8.384 1.00 41.24 ? 178 PHE A CZ 1 ATOM 1395 N N . GLN A 1 181 ? -3.756 11.164 7.609 1.00 31.18 ? 179 GLN A N 1 ATOM 1396 C CA . GLN A 1 181 ? -3.779 11.535 9.036 1.00 29.82 ? 179 GLN A CA 1 ATOM 1397 C C . GLN A 1 181 ? -4.560 10.535 9.848 1.00 29.28 ? 179 GLN A C 1 ATOM 1398 O O . GLN A 1 181 ? -5.501 9.974 9.373 1.00 31.01 ? 179 GLN A O 1 ATOM 1399 C CB . GLN A 1 181 ? -4.382 12.922 9.242 1.00 30.55 ? 179 GLN A CB 1 ATOM 1400 C CG . GLN A 1 181 ? -3.594 14.038 8.553 1.00 30.70 ? 179 GLN A CG 1 ATOM 1401 C CD . GLN A 1 181 ? -4.445 15.235 8.260 1.00 37.26 ? 179 GLN A CD 1 ATOM 1402 O OE1 . GLN A 1 181 ? -5.267 15.211 7.329 1.00 42.15 ? 179 GLN A OE1 1 ATOM 1403 N NE2 . GLN A 1 181 ? -4.278 16.295 9.049 1.00 38.92 ? 179 GLN A NE2 1 ATOM 1404 N N . SER A 1 182 ? -4.141 10.326 11.088 1.00 28.02 ? 180 SER A N 1 ATOM 1405 C CA . SER A 1 182 ? -4.767 9.374 12.013 1.00 28.50 ? 180 SER A CA 1 ATOM 1406 C C . SER A 1 182 ? -6.284 9.501 12.079 1.00 29.69 ? 180 SER A C 1 ATOM 1407 O O . SER A 1 182 ? -6.803 10.595 12.183 1.00 31.12 ? 180 SER A O 1 ATOM 1408 C CB . SER A 1 182 ? -4.196 9.562 13.414 1.00 26.72 ? 180 SER A CB 1 ATOM 1409 O OG . SER A 1 182 ? -4.902 8.791 14.372 1.00 29.48 ? 180 SER A OG 1 ATOM 1410 N N . LEU A 1 183 ? -6.981 8.378 12.013 1.00 30.73 ? 181 LEU A N 1 ATOM 1411 C CA . LEU A 1 183 ? -8.454 8.347 12.190 1.00 33.45 ? 181 LEU A CA 1 ATOM 1412 C C . LEU A 1 183 ? -8.820 7.699 13.542 1.00 33.96 ? 181 LEU A C 1 ATOM 1413 O O . LEU A 1 183 ? -9.996 7.425 13.813 1.00 37.28 ? 181 LEU A O 1 ATOM 1414 C CB . LEU A 1 183 ? -9.144 7.595 11.039 1.00 34.98 ? 181 LEU A CB 1 ATOM 1415 C CG . LEU A 1 183 ? -8.998 8.174 9.623 1.00 36.00 ? 181 LEU A CG 1 ATOM 1416 C CD1 . LEU A 1 183 ? -9.566 7.217 8.594 1.00 36.89 ? 181 LEU A CD1 1 ATOM 1417 C CD2 . LEU A 1 183 ? -9.687 9.555 9.517 1.00 36.49 ? 181 LEU A CD2 1 ATOM 1418 N N . GLY A 1 184 ? -7.808 7.504 14.380 1.00 32.75 ? 182 GLY A N 1 ATOM 1419 C CA . GLY A 1 184 ? -7.922 6.889 15.696 1.00 33.87 ? 182 GLY A CA 1 ATOM 1420 C C . GLY A 1 184 ? -7.624 7.943 16.753 1.00 33.57 ? 182 GLY A C 1 ATOM 1421 O O . GLY A 1 184 ? -8.267 8.982 16.785 1.00 34.74 ? 182 GLY A O 1 ATOM 1422 N N . ARG A 1 185 ? -6.639 7.717 17.616 1.00 33.06 ? 183 ARG A N 1 ATOM 1423 C CA . ARG A 1 185 ? -6.501 8.593 18.761 1.00 32.53 ? 183 ARG A CA 1 ATOM 1424 C C . ARG A 1 185 ? -6.120 10.011 18.451 1.00 30.49 ? 183 ARG A C 1 ATOM 1425 O O . ARG A 1 185 ? -6.400 10.893 19.243 1.00 31.32 ? 183 ARG A O 1 ATOM 1426 C CB . ARG A 1 185 ? -5.572 8.013 19.801 1.00 32.76 ? 183 ARG A CB 1 ATOM 1427 C CG . ARG A 1 185 ? -4.129 8.198 19.577 1.00 32.67 ? 183 ARG A CG 1 ATOM 1428 C CD . ARG A 1 185 ? -3.371 7.927 20.885 1.00 34.30 ? 183 ARG A CD 1 ATOM 1429 N NE . ARG A 1 185 ? -3.410 6.511 21.153 1.00 38.25 ? 183 ARG A NE 1 ATOM 1430 C CZ . ARG A 1 185 ? -3.750 5.926 22.298 1.00 43.43 ? 183 ARG A CZ 1 ATOM 1431 N NH1 . ARG A 1 185 ? -4.063 6.633 23.382 1.00 46.16 ? 183 ARG A NH1 1 ATOM 1432 N NH2 . ARG A 1 185 ? -3.753 4.598 22.357 1.00 43.94 ? 183 ARG A NH2 1 ATOM 1433 N N . PHE A 1 186 ? -5.489 10.239 17.315 1.00 29.05 ? 184 PHE A N 1 ATOM 1434 C CA . PHE A 1 186 ? -5.032 11.557 16.937 1.00 27.65 ? 184 PHE A CA 1 ATOM 1435 C C . PHE A 1 186 ? -5.960 12.231 15.946 1.00 28.12 ? 184 PHE A C 1 ATOM 1436 O O . PHE A 1 186 ? -5.612 13.243 15.387 1.00 27.38 ? 184 PHE A O 1 ATOM 1437 C CB . PHE A 1 186 ? -3.595 11.474 16.372 1.00 26.55 ? 184 PHE A CB 1 ATOM 1438 C CG . PHE A 1 186 ? -2.596 10.927 17.356 1.00 25.72 ? 184 PHE A CG 1 ATOM 1439 C CD1 . PHE A 1 186 ? -2.202 11.681 18.434 1.00 26.75 ? 184 PHE A CD1 1 ATOM 1440 C CD2 . PHE A 1 186 ? -2.107 9.655 17.227 1.00 26.91 ? 184 PHE A CD2 1 ATOM 1441 C CE1 . PHE A 1 186 ? -1.323 11.190 19.364 1.00 26.84 ? 184 PHE A CE1 1 ATOM 1442 C CE2 . PHE A 1 186 ? -1.229 9.155 18.133 1.00 28.11 ? 184 PHE A CE2 1 ATOM 1443 C CZ . PHE A 1 186 ? -0.831 9.943 19.223 1.00 27.92 ? 184 PHE A CZ 1 ATOM 1444 N N . ARG A 1 187 ? -7.144 11.687 15.727 1.00 30.82 ? 185 ARG A N 1 ATOM 1445 C CA . ARG A 1 187 ? -8.025 12.223 14.680 1.00 32.90 ? 185 ARG A CA 1 ATOM 1446 C C . ARG A 1 187 ? -8.347 13.691 14.971 1.00 33.68 ? 185 ARG A C 1 ATOM 1447 O O . ARG A 1 187 ? -8.685 14.066 16.113 1.00 32.62 ? 185 ARG A O 1 ATOM 1448 C CB . ARG A 1 187 ? -9.312 11.408 14.570 1.00 35.50 ? 185 ARG A CB 1 ATOM 1449 C CG . ARG A 1 187 ? -10.236 11.893 13.445 1.00 38.77 ? 185 ARG A CG 1 ATOM 1450 C CD . ARG A 1 187 ? -11.278 10.875 13.123 1.00 43.97 ? 185 ARG A CD 1 ATOM 1451 N NE . ARG A 1 187 ? -12.167 10.665 14.268 1.00 48.76 ? 185 ARG A NE 1 ATOM 1452 C CZ . ARG A 1 187 ? -13.194 11.447 14.593 1.00 54.89 ? 185 ARG A CZ 1 ATOM 1453 N NH1 . ARG A 1 187 ? -13.514 12.516 13.853 1.00 56.51 ? 185 ARG A NH1 1 ATOM 1454 N NH2 . ARG A 1 187 ? -13.931 11.143 15.659 1.00 57.55 ? 185 ARG A NH2 1 ATOM 1455 N N . ASN A 1 188 ? -8.185 14.504 13.933 1.00 34.10 ? 186 ASN A N 1 ATOM 1456 C CA . ASN A 1 188 ? -8.420 15.943 13.973 1.00 35.83 ? 186 ASN A CA 1 ATOM 1457 C C . ASN A 1 188 ? -7.465 16.761 14.833 1.00 35.06 ? 186 ASN A C 1 ATOM 1458 O O . ASN A 1 188 ? -7.647 17.963 14.964 1.00 36.50 ? 186 ASN A O 1 ATOM 1459 C CB . ASN A 1 188 ? -9.853 16.259 14.380 1.00 38.08 ? 186 ASN A CB 1 ATOM 1460 C CG . ASN A 1 188 ? -10.862 15.777 13.378 1.00 40.73 ? 186 ASN A CG 1 ATOM 1461 O OD1 . ASN A 1 188 ? -11.909 15.284 13.768 1.00 45.12 ? 186 ASN A OD1 1 ATOM 1462 N ND2 . ASN A 1 188 ? -10.575 15.940 12.084 1.00 40.55 ? 186 ASN A ND2 1 ATOM 1463 N N . ARG A 1 189 ? -6.438 16.139 15.387 1.00 33.83 ? 187 ARG A N 1 ATOM 1464 C CA . ARG A 1 189 ? -5.486 16.854 16.237 1.00 32.79 ? 187 ARG A CA 1 ATOM 1465 C C . ARG A 1 189 ? -4.081 16.915 15.675 1.00 31.42 ? 187 ARG A C 1 ATOM 1466 O O . ARG A 1 189 ? -3.203 17.511 16.321 1.00 31.62 ? 187 ARG A O 1 ATOM 1467 C CB . ARG A 1 189 ? -5.439 16.189 17.608 1.00 32.37 ? 187 ARG A CB 1 ATOM 1468 C CG . ARG A 1 189 ? -6.794 16.217 18.306 1.00 35.31 ? 187 ARG A CG 1 ATOM 1469 C CD . ARG A 1 189 ? -6.679 15.857 19.757 1.00 34.93 ? 187 ARG A CD 1 ATOM 1470 N NE . ARG A 1 189 ? -6.290 14.462 19.994 1.00 34.53 ? 187 ARG A NE 1 ATOM 1471 C CZ . ARG A 1 189 ? -5.250 14.069 20.730 1.00 33.45 ? 187 ARG A CZ 1 ATOM 1472 N NH1 . ARG A 1 189 ? -4.413 14.939 21.292 1.00 34.84 ? 187 ARG A NH1 1 ATOM 1473 N NH2 . ARG A 1 189 ? -5.035 12.786 20.895 1.00 33.53 ? 187 ARG A NH2 1 ATOM 1474 N N . VAL A 1 190 ? -3.829 16.280 14.519 1.00 31.05 ? 188 VAL A N 1 ATOM 1475 C CA A VAL A 1 190 ? -2.484 16.274 13.907 0.50 29.50 ? 188 VAL A CA 1 ATOM 1476 C CA B VAL A 1 190 ? -2.488 16.274 13.914 0.50 29.57 ? 188 VAL A CA 1 ATOM 1477 C C . VAL A 1 190 ? -2.496 16.859 12.485 1.00 30.19 ? 188 VAL A C 1 ATOM 1478 O O . VAL A 1 190 ? -3.411 16.635 11.721 1.00 32.29 ? 188 VAL A O 1 ATOM 1479 C CB A VAL A 1 190 ? -1.811 14.849 13.896 0.50 28.49 ? 188 VAL A CB 1 ATOM 1480 C CB B VAL A 1 190 ? -1.859 14.844 13.932 0.50 28.62 ? 188 VAL A CB 1 ATOM 1481 C CG1 A VAL A 1 190 ? -1.169 14.545 15.233 0.50 26.33 ? 188 VAL A CG1 1 ATOM 1482 C CG1 B VAL A 1 190 ? -2.660 13.873 13.047 0.50 29.49 ? 188 VAL A CG1 1 ATOM 1483 C CG2 A VAL A 1 190 ? -2.813 13.736 13.505 0.50 29.48 ? 188 VAL A CG2 1 ATOM 1484 C CG2 B VAL A 1 190 ? -0.411 14.886 13.506 0.50 26.34 ? 188 VAL A CG2 1 ATOM 1485 N N . ASP A 1 191 ? -1.470 17.638 12.144 1.00 30.08 ? 189 ASP A N 1 ATOM 1486 C CA . ASP A 1 191 ? -1.255 18.070 10.787 1.00 30.16 ? 189 ASP A CA 1 ATOM 1487 C C . ASP A 1 191 ? 0.228 18.317 10.536 1.00 28.42 ? 189 ASP A C 1 ATOM 1488 O O . ASP A 1 191 ? 1.038 18.450 11.447 1.00 25.67 ? 189 ASP A O 1 ATOM 1489 C CB . ASP A 1 191 ? -2.128 19.293 10.437 1.00 33.60 ? 189 ASP A CB 1 ATOM 1490 C CG . ASP A 1 191 ? -2.542 19.342 8.907 1.00 37.09 ? 189 ASP A CG 1 ATOM 1491 O OD1 . ASP A 1 191 ? -1.844 18.720 8.040 1.00 37.51 ? 189 ASP A OD1 1 ATOM 1492 O OD2 . ASP A 1 191 ? -3.569 20.021 8.583 1.00 43.34 ? 189 ASP A OD2 1 ATOM 1493 N N . LEU A 1 192 ? 0.593 18.300 9.263 1.00 29.04 ? 190 LEU A N 1 ATOM 1494 C CA . LEU A 1 192 ? 1.963 18.566 8.843 1.00 28.83 ? 190 LEU A CA 1 ATOM 1495 C C . LEU A 1 192 ? 2.224 20.057 9.014 1.00 29.64 ? 190 LEU A C 1 ATOM 1496 O O . LEU A 1 192 ? 1.419 20.881 8.624 1.00 32.21 ? 190 LEU A O 1 ATOM 1497 C CB . LEU A 1 192 ? 2.088 18.152 7.382 1.00 29.52 ? 190 LEU A CB 1 ATOM 1498 C CG . LEU A 1 192 ? 3.357 17.660 6.739 1.00 30.26 ? 190 LEU A CG 1 ATOM 1499 C CD1 . LEU A 1 192 ? 4.277 16.813 7.610 1.00 24.04 ? 190 LEU A CD1 1 ATOM 1500 C CD2 . LEU A 1 192 ? 2.906 16.921 5.464 1.00 32.55 ? 190 LEU A CD2 1 ATOM 1501 N N . THR A 1 193 ? 3.295 20.427 9.676 1.00 28.68 ? 191 THR A N 1 ATOM 1502 C CA . THR A 1 193 ? 3.681 21.834 9.660 1.00 28.84 ? 191 THR A CA 1 ATOM 1503 C C . THR A 1 193 ? 4.891 22.056 8.732 1.00 27.35 ? 191 THR A C 1 ATOM 1504 O O . THR A 1 193 ? 5.148 23.171 8.309 1.00 27.51 ? 191 THR A O 1 ATOM 1505 C CB . THR A 1 193 ? 4.063 22.329 11.061 1.00 27.80 ? 191 THR A CB 1 ATOM 1506 O OG1 . THR A 1 193 ? 5.026 21.454 11.604 1.00 26.78 ? 191 THR A OG1 1 ATOM 1507 C CG2 . THR A 1 193 ? 2.858 22.437 11.979 1.00 31.80 ? 191 THR A CG2 1 ATOM 1508 N N . GLY A 1 194 ? 5.665 21.002 8.498 1.00 25.35 ? 192 GLY A N 1 ATOM 1509 C CA . GLY A 1 194 ? 6.795 21.057 7.609 1.00 25.79 ? 192 GLY A CA 1 ATOM 1510 C C . GLY A 1 194 ? 6.397 21.144 6.145 1.00 27.09 ? 192 GLY A C 1 ATOM 1511 O O . GLY A 1 194 ? 5.358 20.674 5.761 1.00 28.09 ? 192 GLY A O 1 ATOM 1512 N N . ASP A 1 195 ? 7.241 21.791 5.349 1.00 27.67 ? 193 ASP A N 1 ATOM 1513 C CA . ASP A 1 195 ? 7.156 21.779 3.896 1.00 28.33 ? 193 ASP A CA 1 ATOM 1514 C C . ASP A 1 195 ? 8.043 20.616 3.429 1.00 26.52 ? 193 ASP A C 1 ATOM 1515 O O . ASP A 1 195 ? 9.255 20.639 3.588 1.00 23.42 ? 193 ASP A O 1 ATOM 1516 C CB . ASP A 1 195 ? 7.637 23.126 3.366 1.00 29.84 ? 193 ASP A CB 1 ATOM 1517 C CG . ASP A 1 195 ? 7.456 23.299 1.887 1.00 33.77 ? 193 ASP A CG 1 ATOM 1518 O OD1 . ASP A 1 195 ? 7.172 22.323 1.157 1.00 37.66 ? 193 ASP A OD1 1 ATOM 1519 O OD2 . ASP A 1 195 ? 7.608 24.456 1.437 1.00 37.43 ? 193 ASP A OD2 1 ATOM 1520 N N . ILE A 1 196 ? 7.406 19.570 2.892 1.00 27.24 ? 194 ILE A N 1 ATOM 1521 C CA . ILE A 1 196 ? 8.120 18.367 2.472 1.00 26.24 ? 194 ILE A CA 1 ATOM 1522 C C . ILE A 1 196 ? 9.062 18.697 1.315 1.00 25.68 ? 194 ILE A C 1 ATOM 1523 O O . ILE A 1 196 ? 10.105 18.105 1.195 1.00 24.74 ? 194 ILE A O 1 ATOM 1524 C CB . ILE A 1 196 ? 7.137 17.220 2.084 1.00 27.79 ? 194 ILE A CB 1 ATOM 1525 C CG1 . ILE A 1 196 ? 6.270 16.828 3.284 1.00 28.04 ? 194 ILE A CG1 1 ATOM 1526 C CG2 . ILE A 1 196 ? 7.911 15.959 1.539 1.00 28.70 ? 194 ILE A CG2 1 ATOM 1527 C CD1 . ILE A 1 196 ? 6.974 15.946 4.270 1.00 29.98 ? 194 ILE A CD1 1 ATOM 1528 N N . SER A 1 197 ? 8.711 19.699 0.515 1.00 26.69 ? 195 SER A N 1 ATOM 1529 C CA . SER A 1 197 ? 9.538 20.125 -0.576 1.00 27.71 ? 195 SER A CA 1 ATOM 1530 C C . SER A 1 197 ? 10.804 20.775 -0.089 1.00 26.28 ? 195 SER A C 1 ATOM 1531 O O . SER A 1 197 ? 11.718 20.929 -0.852 1.00 25.97 ? 195 SER A O 1 ATOM 1532 C CB . SER A 1 197 ? 8.747 21.029 -1.564 1.00 31.12 ? 195 SER A CB 1 ATOM 1533 O OG . SER A 1 197 ? 8.543 22.358 -1.077 1.00 34.24 ? 195 SER A OG 1 ATOM 1534 N N . ARG A 1 198 ? 10.860 21.124 1.203 1.00 25.77 ? 196 ARG A N 1 ATOM 1535 C CA . ARG A 1 198 ? 12.044 21.674 1.850 1.00 25.33 ? 196 ARG A CA 1 ATOM 1536 C C . ARG A 1 198 ? 12.603 20.718 2.911 1.00 23.94 ? 196 ARG A C 1 ATOM 1537 O O . ARG A 1 198 ? 13.292 21.128 3.840 1.00 22.95 ? 196 ARG A O 1 ATOM 1538 C CB . ARG A 1 198 ? 11.699 23.031 2.471 1.00 26.41 ? 196 ARG A CB 1 ATOM 1539 C CG . ARG A 1 198 ? 11.343 24.100 1.453 1.00 29.05 ? 196 ARG A CG 1 ATOM 1540 C CD . ARG A 1 198 ? 12.536 24.476 0.593 1.00 31.35 ? 196 ARG A CD 1 ATOM 1541 N NE . ARG A 1 198 ? 12.137 25.344 -0.516 1.00 34.01 ? 196 ARG A NE 1 ATOM 1542 C CZ . ARG A 1 198 ? 12.971 25.821 -1.428 1.00 36.60 ? 196 ARG A CZ 1 ATOM 1543 N NH1 . ARG A 1 198 ? 14.265 25.533 -1.383 1.00 37.02 ? 196 ARG A NH1 1 ATOM 1544 N NH2 . ARG A 1 198 ? 12.506 26.577 -2.408 1.00 40.61 ? 196 ARG A NH2 1 ATOM 1545 N N . ASN A 1 199 ? 12.219 19.452 2.762 1.00 23.40 ? 197 ASN A N 1 ATOM 1546 C CA . ASN A 1 199 ? 12.764 18.328 3.457 1.00 22.24 ? 197 ASN A CA 1 ATOM 1547 C C . ASN A 1 199 ? 12.359 18.283 4.916 1.00 21.76 ? 197 ASN A C 1 ATOM 1548 O O . ASN A 1 199 ? 13.111 17.767 5.734 1.00 22.17 ? 197 ASN A O 1 ATOM 1549 C CB . ASN A 1 199 ? 14.282 18.277 3.327 1.00 22.72 ? 197 ASN A CB 1 ATOM 1550 C CG . ASN A 1 199 ? 14.754 18.366 1.894 1.00 23.81 ? 197 ASN A CG 1 ATOM 1551 O OD1 . ASN A 1 199 ? 14.395 17.527 1.073 1.00 26.97 ? 197 ASN A OD1 1 ATOM 1552 N ND2 . ASN A 1 199 ? 15.548 19.392 1.586 1.00 20.23 ? 197 ASN A ND2 1 ATOM 1553 N N . ASP A 1 200 ? 11.152 18.759 5.209 1.00 21.39 ? 198 ASP A N 1 ATOM 1554 C CA . ASP A 1 200 ? 10.698 18.945 6.554 1.00 20.85 ? 198 ASP A CA 1 ATOM 1555 C C . ASP A 1 200 ? 9.393 18.174 6.775 1.00 20.74 ? 198 ASP A C 1 ATOM 1556 O O . ASP A 1 200 ? 8.362 18.428 6.113 1.00 20.65 ? 198 ASP A O 1 ATOM 1557 C CB . ASP A 1 200 ? 10.545 20.441 6.780 1.00 21.71 ? 198 ASP A CB 1 ATOM 1558 C CG . ASP A 1 200 ? 10.185 20.799 8.200 1.00 23.25 ? 198 ASP A CG 1 ATOM 1559 O OD1 . ASP A 1 200 ? 9.894 19.892 8.998 1.00 24.48 ? 198 ASP A OD1 1 ATOM 1560 O OD2 . ASP A 1 200 ? 10.166 22.013 8.489 1.00 26.73 ? 198 ASP A OD2 1 ATOM 1561 N N . GLY A 1 201 ? 9.446 17.225 7.717 1.00 19.95 ? 199 GLY A N 1 ATOM 1562 C CA . GLY A 1 201 ? 8.308 16.384 8.028 1.00 20.27 ? 199 GLY A CA 1 ATOM 1563 C C . GLY A 1 201 ? 7.649 16.680 9.340 1.00 19.87 ? 199 GLY A C 1 ATOM 1564 O O . GLY A 1 201 ? 6.892 15.866 9.848 1.00 19.99 ? 199 GLY A O 1 ATOM 1565 N N . SER A 1 202 ? 7.869 17.884 9.856 1.00 21.44 ? 200 SER A N 1 ATOM 1566 C CA . SER A 1 202 ? 7.411 18.253 11.201 1.00 20.75 ? 200 SER A CA 1 ATOM 1567 C C . SER A 1 202 ? 5.883 18.265 11.260 1.00 21.36 ? 200 SER A C 1 ATOM 1568 O O . SER A 1 202 ? 5.188 18.654 10.292 1.00 21.89 ? 200 SER A O 1 ATOM 1569 C CB . SER A 1 202 ? 8.002 19.621 11.589 1.00 21.65 ? 200 SER A CB 1 ATOM 1570 O OG . SER A 1 202 ? 9.406 19.532 11.651 1.00 21.00 ? 200 SER A OG 1 ATOM 1571 N N . ILE A 1 203 ? 5.364 17.801 12.379 1.00 21.25 ? 201 ILE A N 1 ATOM 1572 C CA . ILE A 1 203 ? 3.934 17.829 12.657 1.00 22.33 ? 201 ILE A CA 1 ATOM 1573 C C . ILE A 1 203 ? 3.579 18.654 13.893 1.00 23.45 ? 201 ILE A C 1 ATOM 1574 O O . ILE A 1 203 ? 4.417 18.928 14.744 1.00 22.85 ? 201 ILE A O 1 ATOM 1575 C CB . ILE A 1 203 ? 3.339 16.393 12.749 1.00 21.55 ? 201 ILE A CB 1 ATOM 1576 C CG1 . ILE A 1 203 ? 4.041 15.541 13.833 1.00 21.76 ? 201 ILE A CG1 1 ATOM 1577 C CG2 . ILE A 1 203 ? 3.433 15.737 11.378 1.00 22.19 ? 201 ILE A CG2 1 ATOM 1578 C CD1 . ILE A 1 203 ? 3.287 14.269 14.153 1.00 19.32 ? 201 ILE A CD1 1 ATOM 1579 N N . LYS A 1 204 ? 2.321 19.060 13.957 1.00 25.62 ? 202 LYS A N 1 ATOM 1580 C CA . LYS A 1 204 ? 1.759 19.713 15.124 1.00 28.22 ? 202 LYS A CA 1 ATOM 1581 C C . LYS A 1 204 ? 0.734 18.772 15.772 1.00 28.62 ? 202 LYS A C 1 ATOM 1582 O O . LYS A 1 204 ? -0.023 18.120 15.063 1.00 30.18 ? 202 LYS A O 1 ATOM 1583 C CB . LYS A 1 204 ? 1.121 21.033 14.689 1.00 30.17 ? 202 LYS A CB 1 ATOM 1584 C CG . LYS A 1 204 ? 0.357 21.707 15.727 1.00 35.48 ? 202 LYS A CG 1 ATOM 1585 C CD . LYS A 1 204 ? -0.108 23.050 15.270 1.00 40.09 ? 202 LYS A CD 1 ATOM 1586 C CE . LYS A 1 204 ? -1.140 22.954 14.195 1.00 42.00 ? 202 LYS A CE 1 ATOM 1587 N NZ . LYS A 1 204 ? -1.835 24.263 14.198 1.00 48.75 ? 202 LYS A NZ 1 ATOM 1588 N N . LEU A 1 205 ? 0.772 18.663 17.099 1.00 28.45 ? 203 LEU A N 1 ATOM 1589 C CA . LEU A 1 205 ? -0.205 17.908 17.910 1.00 28.64 ? 203 LEU A CA 1 ATOM 1590 C C . LEU A 1 205 ? -0.937 18.878 18.821 1.00 30.50 ? 203 LEU A C 1 ATOM 1591 O O . LEU A 1 205 ? -0.301 19.539 19.637 1.00 30.73 ? 203 LEU A O 1 ATOM 1592 C CB . LEU A 1 205 ? 0.479 16.850 18.751 1.00 27.00 ? 203 LEU A CB 1 ATOM 1593 C CG . LEU A 1 205 ? -0.390 15.983 19.653 1.00 29.05 ? 203 LEU A CG 1 ATOM 1594 C CD1 . LEU A 1 205 ? -1.586 15.276 18.925 1.00 28.35 ? 203 LEU A CD1 1 ATOM 1595 C CD2 . LEU A 1 205 ? 0.482 14.956 20.403 1.00 26.78 ? 203 LEU A CD2 1 ATOM 1596 N N . GLN A 1 206 ? -2.257 18.978 18.651 1.00 32.35 ? 204 GLN A N 1 ATOM 1597 C CA . GLN A 1 206 ? -3.071 19.947 19.362 1.00 35.68 ? 204 GLN A CA 1 ATOM 1598 C C . GLN A 1 206 ? -3.773 19.343 20.569 1.00 35.79 ? 204 GLN A C 1 ATOM 1599 O O . GLN A 1 206 ? -4.029 18.137 20.627 1.00 35.29 ? 204 GLN A O 1 ATOM 1600 C CB . GLN A 1 206 ? -4.130 20.536 18.434 1.00 38.24 ? 204 GLN A CB 1 ATOM 1601 C CG . GLN A 1 206 ? -3.600 21.080 17.124 1.00 40.53 ? 204 GLN A CG 1 ATOM 1602 C CD . GLN A 1 206 ? -4.691 21.764 16.325 1.00 46.84 ? 204 GLN A CD 1 ATOM 1603 O OE1 . GLN A 1 206 ? -4.578 22.953 15.972 1.00 51.86 ? 204 GLN A OE1 1 ATOM 1604 N NE2 . GLN A 1 206 ? -5.781 21.036 16.077 1.00 49.94 ? 204 GLN A NE2 1 ATOM 1605 N N . THR A 1 207 ? -4.091 20.211 21.524 1.00 37.19 ? 205 THR A N 1 ATOM 1606 C CA . THR A 1 207 ? -4.801 19.839 22.759 1.00 38.04 ? 205 THR A CA 1 ATOM 1607 C C . THR A 1 207 ? -4.357 18.473 23.281 1.00 36.11 ? 205 THR A C 1 ATOM 1608 O O . THR A 1 207 ? -5.120 17.509 23.337 1.00 35.99 ? 205 THR A O 1 ATOM 1609 C CB . THR A 1 207 ? -6.314 19.940 22.557 1.00 40.49 ? 205 THR A CB 1 ATOM 1610 O OG1 . THR A 1 207 ? -6.603 21.158 21.840 1.00 42.74 ? 205 THR A OG1 1 ATOM 1611 C CG2 . THR A 1 207 ? -7.037 19.968 23.905 1.00 41.66 ? 205 THR A CG2 1 ATOM 1612 N N . VAL A 1 208 ? -3.078 18.424 23.639 1.00 33.93 ? 206 VAL A N 1 ATOM 1613 C CA . VAL A 1 208 ? -2.447 17.251 24.181 1.00 32.83 ? 206 VAL A CA 1 ATOM 1614 C C . VAL A 1 208 ? -3.193 16.680 25.402 1.00 33.56 ? 206 VAL A C 1 ATOM 1615 O O . VAL A 1 208 ? -3.646 17.417 26.266 1.00 34.59 ? 206 VAL A O 1 ATOM 1616 C CB . VAL A 1 208 ? -0.961 17.572 24.518 1.00 32.19 ? 206 VAL A CB 1 ATOM 1617 C CG1 . VAL A 1 208 ? -0.357 16.542 25.457 1.00 30.58 ? 206 VAL A CG1 1 ATOM 1618 C CG2 . VAL A 1 208 ? -0.150 17.679 23.210 1.00 31.75 ? 206 VAL A CG2 1 ATOM 1619 N N . LYS A 1 209 ? -3.314 15.355 25.422 1.00 33.87 ? 207 LYS A N 1 ATOM 1620 C CA . LYS A 1 209 ? -3.935 14.573 26.517 1.00 35.48 ? 207 LYS A CA 1 ATOM 1621 C C . LYS A 1 209 ? -2.870 13.708 27.204 1.00 34.71 ? 207 LYS A C 1 ATOM 1622 O O . LYS A 1 209 ? -1.809 13.446 26.619 1.00 33.44 ? 207 LYS A O 1 ATOM 1623 C CB . LYS A 1 209 ? -4.963 13.593 25.975 1.00 36.28 ? 207 LYS A CB 1 ATOM 1624 C CG . LYS A 1 209 ? -5.966 14.093 24.987 1.00 39.09 ? 207 LYS A CG 1 ATOM 1625 C CD . LYS A 1 209 ? -6.697 12.866 24.399 1.00 42.68 ? 207 LYS A CD 1 ATOM 1626 C CE . LYS A 1 209 ? -8.067 13.207 23.825 1.00 46.43 ? 207 LYS A CE 1 ATOM 1627 N NZ . LYS A 1 209 ? -8.025 14.148 22.673 1.00 49.22 ? 207 LYS A NZ 1 ATOM 1628 N N . GLU A 1 210 ? -3.162 13.261 28.421 1.00 36.06 ? 208 GLU A N 1 ATOM 1629 C CA . GLU A 1 210 ? -2.278 12.361 29.162 1.00 36.48 ? 208 GLU A CA 1 ATOM 1630 C C . GLU A 1 210 ? -2.057 11.063 28.416 1.00 34.69 ? 208 GLU A C 1 ATOM 1631 O O . GLU A 1 210 ? -0.983 10.489 28.478 1.00 33.74 ? 208 GLU A O 1 ATOM 1632 C CB . GLU A 1 210 ? -2.824 12.033 30.548 1.00 39.32 ? 208 GLU A CB 1 ATOM 1633 C CG . GLU A 1 210 ? -2.687 13.139 31.604 1.00 43.95 ? 208 GLU A CG 1 ATOM 1634 C CD . GLU A 1 210 ? -3.052 12.664 33.022 1.00 51.06 ? 208 GLU A CD 1 ATOM 1635 O OE1 . GLU A 1 210 ? -2.710 11.505 33.407 1.00 54.10 ? 208 GLU A OE1 1 ATOM 1636 O OE2 . GLU A 1 210 ? -3.674 13.462 33.773 1.00 56.71 ? 208 GLU A OE2 1 ATOM 1637 N N . SER A 1 211 ? -3.074 10.616 27.697 1.00 34.27 ? 209 SER A N 1 ATOM 1638 C CA . SER A 1 211 ? -2.983 9.375 26.945 1.00 34.03 ? 209 SER A CA 1 ATOM 1639 C C . SER A 1 211 ? -2.174 9.507 25.669 1.00 31.22 ? 209 SER A C 1 ATOM 1640 O O . SER A 1 211 ? -1.850 8.509 25.048 1.00 31.20 ? 209 SER A O 1 ATOM 1641 C CB . SER A 1 211 ? -4.384 8.821 26.657 1.00 35.29 ? 209 SER A CB 1 ATOM 1642 O OG . SER A 1 211 ? -5.154 9.794 26.007 1.00 36.80 ? 209 SER A OG 1 ATOM 1643 N N . ASP A 1 212 ? -1.827 10.734 25.280 1.00 30.35 ? 210 ASP A N 1 ATOM 1644 C CA . ASP A 1 212 ? -0.826 10.963 24.221 1.00 28.19 ? 210 ASP A CA 1 ATOM 1645 C C . ASP A 1 212 ? 0.624 10.709 24.661 1.00 27.75 ? 210 ASP A C 1 ATOM 1646 O O . ASP A 1 212 ? 1.547 10.797 23.825 1.00 26.36 ? 210 ASP A O 1 ATOM 1647 C CB . ASP A 1 212 ? -0.893 12.405 23.701 1.00 27.91 ? 210 ASP A CB 1 ATOM 1648 C CG . ASP A 1 212 ? -2.202 12.745 23.029 1.00 28.64 ? 210 ASP A CG 1 ATOM 1649 O OD1 . ASP A 1 212 ? -2.930 11.821 22.598 1.00 31.12 ? 210 ASP A OD1 1 ATOM 1650 O OD2 . ASP A 1 212 ? -2.501 13.969 22.926 1.00 27.65 ? 210 ASP A OD2 1 ATOM 1651 N N . GLN A 1 213 ? 0.849 10.452 25.958 1.00 28.66 ? 211 GLN A N 1 ATOM 1652 C CA . GLN A 1 213 ? 2.195 10.163 26.454 1.00 28.98 ? 211 GLN A CA 1 ATOM 1653 C C . GLN A 1 213 ? 2.784 8.845 25.849 1.00 29.92 ? 211 GLN A C 1 ATOM 1654 O O . GLN A 1 213 ? 2.116 7.818 25.801 1.00 30.70 ? 211 GLN A O 1 ATOM 1655 C CB . GLN A 1 213 ? 2.218 10.145 27.982 1.00 30.41 ? 211 GLN A CB 1 ATOM 1656 C CG . GLN A 1 213 ? 3.585 9.781 28.582 1.00 29.88 ? 211 GLN A CG 1 ATOM 1657 C CD . GLN A 1 213 ? 3.674 10.037 30.046 1.00 29.28 ? 211 GLN A CD 1 ATOM 1658 O OE1 . GLN A 1 213 ? 3.687 11.186 30.462 1.00 28.48 ? 211 GLN A OE1 1 ATOM 1659 N NE2 . GLN A 1 213 ? 3.763 8.970 30.853 1.00 28.12 ? 211 GLN A NE2 1 ATOM 1660 N N . GLY A 1 214 ? 4.038 8.887 25.394 1.00 29.34 ? 212 GLY A N 1 ATOM 1661 C CA . GLY A 1 214 ? 4.609 7.770 24.651 1.00 29.95 ? 212 GLY A CA 1 ATOM 1662 C C . GLY A 1 214 ? 5.745 8.152 23.713 1.00 29.31 ? 212 GLY A C 1 ATOM 1663 O O . GLY A 1 214 ? 6.306 9.249 23.811 1.00 28.38 ? 212 GLY A O 1 ATOM 1664 N N . ILE A 1 215 ? 6.086 7.213 22.822 1.00 29.46 ? 213 ILE A N 1 ATOM 1665 C CA . ILE A 1 215 ? 7.181 7.342 21.865 1.00 29.04 ? 213 ILE A CA 1 ATOM 1666 C C . ILE A 1 215 ? 6.625 7.624 20.494 1.00 27.20 ? 213 ILE A C 1 ATOM 1667 O O . ILE A 1 215 ? 5.799 6.850 19.987 1.00 27.25 ? 213 ILE A O 1 ATOM 1668 C CB . ILE A 1 215 ? 8.018 6.073 21.808 1.00 31.57 ? 213 ILE A CB 1 ATOM 1669 C CG1 . ILE A 1 215 ? 8.556 5.746 23.179 1.00 35.39 ? 213 ILE A CG1 1 ATOM 1670 C CG2 . ILE A 1 215 ? 9.216 6.227 20.889 1.00 31.40 ? 213 ILE A CG2 1 ATOM 1671 C CD1 . ILE A 1 215 ? 9.515 6.788 23.718 1.00 36.55 ? 213 ILE A CD1 1 ATOM 1672 N N . TYR A 1 216 ? 7.037 8.764 19.938 1.00 24.98 ? 214 TYR A N 1 ATOM 1673 C CA . TYR A 1 216 ? 6.746 9.157 18.566 1.00 23.63 ? 214 TYR A CA 1 ATOM 1674 C C . TYR A 1 216 ? 7.991 8.919 17.721 1.00 24.19 ? 214 TYR A C 1 ATOM 1675 O O . TYR A 1 216 ? 9.113 9.300 18.109 1.00 25.43 ? 214 TYR A O 1 ATOM 1676 C CB . TYR A 1 216 ? 6.300 10.633 18.493 1.00 21.72 ? 214 TYR A CB 1 ATOM 1677 C CG . TYR A 1 216 ? 4.982 10.844 19.192 1.00 20.91 ? 214 TYR A CG 1 ATOM 1678 C CD1 . TYR A 1 216 ? 4.907 10.847 20.580 1.00 22.05 ? 214 TYR A CD1 1 ATOM 1679 C CD2 . TYR A 1 216 ? 3.802 10.934 18.476 1.00 21.77 ? 214 TYR A CD2 1 ATOM 1680 C CE1 . TYR A 1 216 ? 3.700 10.977 21.237 1.00 22.00 ? 214 TYR A CE1 1 ATOM 1681 C CE2 . TYR A 1 216 ? 2.587 11.073 19.123 1.00 24.17 ? 214 TYR A CE2 1 ATOM 1682 C CZ . TYR A 1 216 ? 2.546 11.101 20.512 1.00 23.46 ? 214 TYR A CZ 1 ATOM 1683 O OH . TYR A 1 216 ? 1.350 11.254 21.170 1.00 24.17 ? 214 TYR A OH 1 ATOM 1684 N N . THR A 1 217 ? 7.804 8.230 16.605 1.00 24.83 ? 215 THR A N 1 ATOM 1685 C CA . THR A 1 217 ? 8.888 7.908 15.680 1.00 24.63 ? 215 THR A CA 1 ATOM 1686 C C . THR A 1 217 ? 8.640 8.511 14.284 1.00 23.63 ? 215 THR A C 1 ATOM 1687 O O . THR A 1 217 ? 7.574 8.361 13.729 1.00 23.34 ? 215 THR A O 1 ATOM 1688 C CB . THR A 1 217 ? 9.044 6.374 15.519 1.00 26.79 ? 215 THR A CB 1 ATOM 1689 O OG1 . THR A 1 217 ? 9.159 5.752 16.810 1.00 27.40 ? 215 THR A OG1 1 ATOM 1690 C CG2 . THR A 1 217 ? 10.292 6.056 14.691 1.00 25.40 ? 215 THR A CG2 1 ATOM 1691 N N . CYS A 1 218 ? 9.624 9.212 13.749 1.00 23.26 ? 216 CYS A N 1 ATOM 1692 C CA . CYS A 1 218 ? 9.581 9.705 12.389 1.00 25.08 ? 216 CYS A CA 1 ATOM 1693 C C . CYS A 1 218 ? 10.577 8.942 11.553 1.00 25.66 ? 216 CYS A C 1 ATOM 1694 O O . CYS A 1 218 ? 11.762 8.845 11.905 1.00 25.41 ? 216 CYS A O 1 ATOM 1695 C CB . CYS A 1 218 ? 9.958 11.161 12.373 1.00 25.17 ? 216 CYS A CB 1 ATOM 1696 S SG . CYS A 1 218 ? 9.990 11.964 10.782 1.00 29.55 ? 216 CYS A SG 1 ATOM 1697 N N . SER A 1 219 ? 10.074 8.331 10.489 1.00 25.62 ? 217 SER A N 1 ATOM 1698 C CA . SER A 1 219 ? 10.906 7.771 9.472 1.00 25.72 ? 217 SER A CA 1 ATOM 1699 C C . SER A 1 219 ? 10.825 8.760 8.324 1.00 25.56 ? 217 SER A C 1 ATOM 1700 O O . SER A 1 219 ? 9.753 9.004 7.777 1.00 25.52 ? 217 SER A O 1 ATOM 1701 C CB . SER A 1 219 ? 10.405 6.405 9.095 1.00 27.24 ? 217 SER A CB 1 ATOM 1702 O OG . SER A 1 219 ? 10.377 5.520 10.224 1.00 28.34 ? 217 SER A OG 1 ATOM 1703 N N . ILE A 1 220 ? 11.956 9.361 7.996 1.00 25.31 ? 218 ILE A N 1 ATOM 1704 C CA . ILE A 1 220 ? 12.039 10.346 6.934 1.00 25.36 ? 218 ILE A CA 1 ATOM 1705 C C . ILE A 1 220 ? 13.003 9.818 5.862 1.00 26.88 ? 218 ILE A C 1 ATOM 1706 O O . ILE A 1 220 ? 14.159 9.498 6.165 1.00 28.32 ? 218 ILE A O 1 ATOM 1707 C CB . ILE A 1 220 ? 12.395 11.730 7.507 1.00 24.32 ? 218 ILE A CB 1 ATOM 1708 C CG1 . ILE A 1 220 ? 12.267 12.802 6.436 1.00 26.13 ? 218 ILE A CG1 1 ATOM 1709 C CG2 . ILE A 1 220 ? 13.754 11.721 8.242 1.00 24.62 ? 218 ILE A CG2 1 ATOM 1710 C CD1 . ILE A 1 220 ? 12.204 14.204 7.001 1.00 24.38 ? 218 ILE A CD1 1 ATOM 1711 N N . TYR A 1 221 ? 12.495 9.669 4.629 1.00 26.81 ? 219 TYR A N 1 ATOM 1712 C CA . TYR A 1 221 ? 13.194 8.928 3.589 1.00 27.94 ? 219 TYR A CA 1 ATOM 1713 C C . TYR A 1 221 ? 13.727 9.845 2.500 1.00 27.38 ? 219 TYR A C 1 ATOM 1714 O O . TYR A 1 221 ? 13.055 10.780 2.071 1.00 26.14 ? 219 TYR A O 1 ATOM 1715 C CB . TYR A 1 221 ? 12.286 7.893 2.906 1.00 29.42 ? 219 TYR A CB 1 ATOM 1716 C CG . TYR A 1 221 ? 11.771 6.778 3.797 1.00 29.11 ? 219 TYR A CG 1 ATOM 1717 C CD1 . TYR A 1 221 ? 10.784 7.018 4.738 1.00 27.50 ? 219 TYR A CD1 1 ATOM 1718 C CD2 . TYR A 1 221 ? 12.254 5.471 3.674 1.00 33.25 ? 219 TYR A CD2 1 ATOM 1719 C CE1 . TYR A 1 221 ? 10.290 5.998 5.542 1.00 29.40 ? 219 TYR A CE1 1 ATOM 1720 C CE2 . TYR A 1 221 ? 11.764 4.444 4.479 1.00 33.19 ? 219 TYR A CE2 1 ATOM 1721 C CZ . TYR A 1 221 ? 10.778 4.728 5.406 1.00 31.88 ? 219 TYR A CZ 1 ATOM 1722 O OH . TYR A 1 221 ? 10.276 3.734 6.210 1.00 35.97 ? 219 TYR A OH 1 ATOM 1723 N N . VAL A 1 222 ? 14.940 9.547 2.058 1.00 27.21 ? 220 VAL A N 1 ATOM 1724 C CA . VAL A 1 222 ? 15.483 10.138 0.854 1.00 28.04 ? 220 VAL A CA 1 ATOM 1725 C C . VAL A 1 222 ? 15.604 8.954 -0.068 1.00 30.43 ? 220 VAL A C 1 ATOM 1726 O O . VAL A 1 222 ? 16.516 8.180 0.058 1.00 33.48 ? 220 VAL A O 1 ATOM 1727 C CB . VAL A 1 222 ? 16.880 10.770 1.062 1.00 26.97 ? 220 VAL A CB 1 ATOM 1728 C CG1 . VAL A 1 222 ? 17.456 11.171 -0.297 1.00 28.32 ? 220 VAL A CG1 1 ATOM 1729 C CG2 . VAL A 1 222 ? 16.806 11.961 2.029 1.00 23.84 ? 220 VAL A CG2 1 ATOM 1730 N N . GLY A 1 223 ? 14.657 8.759 -0.952 1.00 32.27 ? 221 GLY A N 1 ATOM 1731 C CA . GLY A 1 223 ? 14.590 7.478 -1.688 1.00 35.15 ? 221 GLY A CA 1 ATOM 1732 C C . GLY A 1 223 ? 14.249 6.302 -0.771 1.00 36.03 ? 221 GLY A C 1 ATOM 1733 O O . GLY A 1 223 ? 13.395 6.396 0.110 1.00 34.71 ? 221 GLY A O 1 ATOM 1734 N N . LYS A 1 224 ? 14.917 5.185 -0.957 1.00 38.48 ? 222 LYS A N 1 ATOM 1735 C CA . LYS A 1 224 ? 14.700 4.060 -0.075 1.00 40.28 ? 222 LYS A CA 1 ATOM 1736 C C . LYS A 1 224 ? 15.456 4.191 1.251 1.00 38.96 ? 222 LYS A C 1 ATOM 1737 O O . LYS A 1 224 ? 15.315 3.319 2.090 1.00 39.83 ? 222 LYS A O 1 ATOM 1738 C CB . LYS A 1 224 ? 15.109 2.743 -0.765 1.00 44.07 ? 222 LYS A CB 1 ATOM 1739 C CG . LYS A 1 224 ? 14.397 2.410 -2.089 1.00 47.77 ? 222 LYS A CG 1 ATOM 1740 C CD . LYS A 1 224 ? 12.871 2.343 -1.926 1.00 51.46 ? 222 LYS A CD 1 ATOM 1741 C CE . LYS A 1 224 ? 12.249 1.370 -2.931 1.00 56.36 ? 222 LYS A CE 1 ATOM 1742 N NZ . LYS A 1 224 ? 10.779 1.247 -2.732 1.00 59.05 ? 222 LYS A NZ 1 ATOM 1743 N N . LEU A 1 225 ? 16.282 5.238 1.421 1.00 37.82 ? 223 LEU A N 1 ATOM 1744 C CA . LEU A 1 225 ? 17.112 5.405 2.619 1.00 36.76 ? 223 LEU A CA 1 ATOM 1745 C C . LEU A 1 225 ? 16.344 6.126 3.716 1.00 33.89 ? 223 LEU A C 1 ATOM 1746 O O . LEU A 1 225 ? 15.967 7.259 3.573 1.00 31.79 ? 223 LEU A O 1 ATOM 1747 C CB . LEU A 1 225 ? 18.424 6.167 2.332 1.00 36.97 ? 223 LEU A CB 1 ATOM 1748 C CG . LEU A 1 225 ? 19.373 5.522 1.318 1.00 41.00 ? 223 LEU A CG 1 ATOM 1749 C CD1 . LEU A 1 225 ? 20.262 6.600 0.715 1.00 43.16 ? 223 LEU A CD1 1 ATOM 1750 C CD2 . LEU A 1 225 ? 20.191 4.418 1.951 1.00 44.41 ? 223 LEU A CD2 1 ATOM 1751 N N . GLU A 1 226 ? 16.189 5.446 4.834 1.00 34.37 ? 224 GLU A N 1 ATOM 1752 C CA . GLU A 1 226 ? 15.459 5.931 5.954 1.00 33.17 ? 224 GLU A CA 1 ATOM 1753 C C . GLU A 1 226 ? 16.421 6.544 6.957 1.00 33.19 ? 224 GLU A C 1 ATOM 1754 O O . GLU A 1 226 ? 17.480 5.986 7.233 1.00 34.03 ? 224 GLU A O 1 ATOM 1755 C CB . GLU A 1 226 ? 14.740 4.767 6.630 1.00 34.98 ? 224 GLU A CB 1 ATOM 1756 C CG . GLU A 1 226 ? 13.659 5.233 7.611 1.00 34.00 ? 224 GLU A CG 1 ATOM 1757 C CD . GLU A 1 226 ? 13.381 4.204 8.688 1.00 38.30 ? 224 GLU A CD 1 ATOM 1758 O OE1 . GLU A 1 226 ? 13.733 3.050 8.467 1.00 39.88 ? 224 GLU A OE1 1 ATOM 1759 O OE2 . GLU A 1 226 ? 12.797 4.551 9.746 1.00 40.87 ? 224 GLU A OE2 1 ATOM 1760 N N . SER A 1 227 ? 16.055 7.718 7.459 1.00 31.02 ? 225 SER A N 1 ATOM 1761 C CA . SER A 1 227 ? 16.617 8.247 8.659 1.00 30.99 ? 225 SER A CA 1 ATOM 1762 C C . SER A 1 227 ? 15.484 8.222 9.694 1.00 30.58 ? 225 SER A C 1 ATOM 1763 O O . SER A 1 227 ? 14.337 8.548 9.390 1.00 30.13 ? 225 SER A O 1 ATOM 1764 C CB . SER A 1 227 ? 17.088 9.665 8.390 1.00 30.62 ? 225 SER A CB 1 ATOM 1765 O OG . SER A 1 227 ? 18.082 9.671 7.365 1.00 32.67 ? 225 SER A OG 1 ATOM 1766 N N . ARG A 1 228 ? 15.801 7.857 10.922 1.00 31.76 ? 226 ARG A N 1 ATOM 1767 C CA . ARG A 1 228 ? 14.798 7.678 11.961 1.00 31.62 ? 226 ARG A CA 1 ATOM 1768 C C . ARG A 1 228 ? 15.041 8.557 13.195 1.00 31.55 ? 226 ARG A C 1 ATOM 1769 O O . ARG A 1 228 ? 16.163 8.696 13.688 1.00 32.62 ? 226 ARG A O 1 ATOM 1770 C CB . ARG A 1 228 ? 14.803 6.227 12.350 1.00 33.51 ? 226 ARG A CB 1 ATOM 1771 C CG . ARG A 1 228 ? 13.596 5.814 13.132 1.00 35.17 ? 226 ARG A CG 1 ATOM 1772 C CD . ARG A 1 228 ? 13.677 4.327 13.399 1.00 39.14 ? 226 ARG A CD 1 ATOM 1773 N NE . ARG A 1 228 ? 13.385 3.521 12.217 1.00 38.97 ? 226 ARG A NE 1 ATOM 1774 C CZ . ARG A 1 228 ? 13.641 2.218 12.131 1.00 44.43 ? 226 ARG A CZ 1 ATOM 1775 N NH1 . ARG A 1 228 ? 14.185 1.556 13.153 1.00 46.79 ? 226 ARG A NH1 1 ATOM 1776 N NH2 . ARG A 1 228 ? 13.354 1.558 11.024 1.00 45.63 ? 226 ARG A NH2 1 ATOM 1777 N N . LYS A 1 229 ? 13.980 9.163 13.689 1.00 31.24 ? 227 LYS A N 1 ATOM 1778 C CA . LYS A 1 229 ? 14.053 10.025 14.855 1.00 31.07 ? 227 LYS A CA 1 ATOM 1779 C C . LYS A 1 229 ? 13.063 9.575 15.924 1.00 30.57 ? 227 LYS A C 1 ATOM 1780 O O . LYS A 1 229 ? 11.892 9.403 15.625 1.00 28.75 ? 227 LYS A O 1 ATOM 1781 C CB . LYS A 1 229 ? 13.691 11.462 14.466 1.00 30.07 ? 227 LYS A CB 1 ATOM 1782 C CG . LYS A 1 229 ? 13.815 12.443 15.656 1.00 34.31 ? 227 LYS A CG 1 ATOM 1783 C CD . LYS A 1 229 ? 13.347 13.818 15.261 1.00 38.43 ? 227 LYS A CD 1 ATOM 1784 C CE . LYS A 1 229 ? 13.982 14.842 16.153 1.00 42.56 ? 227 LYS A CE 1 ATOM 1785 N NZ . LYS A 1 229 ? 13.499 14.656 17.532 1.00 46.69 ? 227 LYS A NZ 1 ATOM 1786 N N . THR A 1 230 ? 13.506 9.523 17.183 1.00 30.91 ? 228 THR A N 1 ATOM 1787 C CA . THR A 1 230 ? 12.609 9.193 18.293 1.00 30.98 ? 228 THR A CA 1 ATOM 1788 C C . THR A 1 230 ? 12.342 10.409 19.206 1.00 29.50 ? 228 THR A C 1 ATOM 1789 O O . THR A 1 230 ? 13.245 11.127 19.577 1.00 29.96 ? 228 THR A O 1 ATOM 1790 C CB . THR A 1 230 ? 13.181 8.013 19.075 1.00 33.59 ? 228 THR A CB 1 ATOM 1791 O OG1 . THR A 1 230 ? 13.408 6.961 18.146 1.00 35.47 ? 228 THR A OG1 1 ATOM 1792 C CG2 . THR A 1 230 ? 12.204 7.512 20.150 1.00 35.72 ? 228 THR A CG2 1 ATOM 1793 N N . ILE A 1 231 ? 11.079 10.666 19.511 1.00 27.26 ? 229 ILE A N 1 ATOM 1794 C CA . ILE A 1 231 ? 10.721 11.660 20.498 1.00 26.44 ? 229 ILE A CA 1 ATOM 1795 C C . ILE A 1 231 ? 9.918 10.984 21.607 1.00 26.37 ? 229 ILE A C 1 ATOM 1796 O O . ILE A 1 231 ? 8.945 10.298 21.330 1.00 25.61 ? 229 ILE A O 1 ATOM 1797 C CB . ILE A 1 231 ? 9.871 12.782 19.885 1.00 25.31 ? 229 ILE A CB 1 ATOM 1798 C CG1 . ILE A 1 231 ? 10.709 13.578 18.859 1.00 27.95 ? 229 ILE A CG1 1 ATOM 1799 C CG2 . ILE A 1 231 ? 9.292 13.729 20.947 1.00 22.83 ? 229 ILE A CG2 1 ATOM 1800 C CD1 . ILE A 1 231 ? 9.879 14.445 17.981 1.00 25.53 ? 229 ILE A CD1 1 ATOM 1801 N N . VAL A 1 232 ? 10.339 11.161 22.852 1.00 26.45 ? 230 VAL A N 1 ATOM 1802 C CA . VAL A 1 232 ? 9.528 10.714 23.986 1.00 27.28 ? 230 VAL A CA 1 ATOM 1803 C C . VAL A 1 232 ? 8.711 11.927 24.468 1.00 26.44 ? 230 VAL A C 1 ATOM 1804 O O . VAL A 1 232 ? 9.286 12.955 24.886 1.00 26.43 ? 230 VAL A O 1 ATOM 1805 C CB . VAL A 1 232 ? 10.378 10.085 25.105 1.00 29.03 ? 230 VAL A CB 1 ATOM 1806 C CG1 . VAL A 1 232 ? 9.511 9.627 26.284 1.00 28.54 ? 230 VAL A CG1 1 ATOM 1807 C CG2 . VAL A 1 232 ? 11.215 8.911 24.535 1.00 29.67 ? 230 VAL A CG2 1 ATOM 1808 N N . LEU A 1 233 ? 7.382 11.807 24.352 1.00 24.85 ? 231 LEU A N 1 ATOM 1809 C CA . LEU A 1 233 ? 6.470 12.820 24.807 1.00 24.35 ? 231 LEU A CA 1 ATOM 1810 C C . LEU A 1 233 ? 6.091 12.554 26.240 1.00 25.53 ? 231 LEU A C 1 ATOM 1811 O O . LEU A 1 233 ? 5.445 11.556 26.573 1.00 25.19 ? 231 LEU A O 1 ATOM 1812 C CB . LEU A 1 233 ? 5.242 12.907 23.917 1.00 24.27 ? 231 LEU A CB 1 ATOM 1813 C CG . LEU A 1 233 ? 4.317 14.129 24.124 1.00 26.84 ? 231 LEU A CG 1 ATOM 1814 C CD1 . LEU A 1 233 ? 4.959 15.386 23.464 1.00 26.02 ? 231 LEU A CD1 1 ATOM 1815 C CD2 . LEU A 1 233 ? 2.936 13.889 23.491 1.00 24.02 ? 231 LEU A CD2 1 ATOM 1816 N N . HIS A 1 234 ? 6.538 13.468 27.090 1.00 25.56 ? 232 HIS A N 1 ATOM 1817 C CA . HIS A 1 234 ? 6.293 13.413 28.479 1.00 27.16 ? 232 HIS A CA 1 ATOM 1818 C C . HIS A 1 234 ? 5.224 14.444 28.779 1.00 28.32 ? 232 HIS A C 1 ATOM 1819 O O . HIS A 1 234 ? 5.467 15.633 28.678 1.00 28.21 ? 232 HIS A O 1 ATOM 1820 C CB . HIS A 1 234 ? 7.590 13.696 29.226 1.00 27.52 ? 232 HIS A CB 1 ATOM 1821 C CG . HIS A 1 234 ? 7.466 13.542 30.698 1.00 27.70 ? 232 HIS A CG 1 ATOM 1822 N ND1 . HIS A 1 234 ? 8.461 13.907 31.569 1.00 27.33 ? 232 HIS A ND1 1 ATOM 1823 C CD2 . HIS A 1 234 ? 6.453 13.060 31.457 1.00 28.92 ? 232 HIS A CD2 1 ATOM 1824 C CE1 . HIS A 1 234 ? 8.073 13.641 32.803 1.00 32.05 ? 232 HIS A CE1 1 ATOM 1825 N NE2 . HIS A 1 234 ? 6.861 13.123 32.761 1.00 29.01 ? 232 HIS A NE2 1 ATOM 1826 N N . VAL A 1 235 ? 4.052 13.970 29.192 1.00 30.84 ? 233 VAL A N 1 ATOM 1827 C CA . VAL A 1 235 ? 2.893 14.813 29.467 1.00 31.97 ? 233 VAL A CA 1 ATOM 1828 C C . VAL A 1 235 ? 2.773 15.020 30.963 1.00 36.18 ? 233 VAL A C 1 ATOM 1829 O O . VAL A 1 235 ? 2.639 14.076 31.740 1.00 37.32 ? 233 VAL A O 1 ATOM 1830 C CB . VAL A 1 235 ? 1.593 14.221 28.868 1.00 31.41 ? 233 VAL A CB 1 ATOM 1831 C CG1 . VAL A 1 235 ? 0.405 15.201 29.049 1.00 31.38 ? 233 VAL A CG1 1 ATOM 1832 C CG2 . VAL A 1 235 ? 1.817 13.860 27.395 1.00 25.34 ? 233 VAL A CG2 1 ATOM 1833 N N . VAL A 1 236 ? 2.844 16.285 31.355 1.00 39.94 ? 234 VAL A N 1 ATOM 1834 C CA . VAL A 1 236 ? 2.909 16.667 32.748 1.00 44.53 ? 234 VAL A CA 1 ATOM 1835 C C . VAL A 1 236 ? 1.709 17.551 33.140 1.00 48.27 ? 234 VAL A C 1 ATOM 1836 O O . VAL A 1 236 ? 0.930 17.997 32.290 1.00 47.17 ? 234 VAL A O 1 ATOM 1837 C CB . VAL A 1 236 ? 4.279 17.321 33.057 1.00 45.69 ? 234 VAL A CB 1 ATOM 1838 C CG1 . VAL A 1 236 ? 5.415 16.366 32.659 1.00 43.29 ? 234 VAL A CG1 1 ATOM 1839 C CG2 . VAL A 1 236 ? 4.437 18.661 32.361 1.00 44.98 ? 234 VAL A CG2 1 ATOM 1840 N N . GLN A 1 237 ? 1.542 17.753 34.438 1.00 54.15 ? 235 GLN A N 1 ATOM 1841 C CA . GLN A 1 237 ? 0.427 18.558 34.984 1.00 58.45 ? 235 GLN A CA 1 ATOM 1842 C C . GLN A 1 237 ? 0.829 20.042 35.225 1.00 61.64 ? 235 GLN A C 1 ATOM 1843 O O . GLN A 1 237 ? 1.948 20.459 34.895 1.00 61.24 ? 235 GLN A O 1 ATOM 1844 C CB . GLN A 1 237 ? -0.118 17.900 36.275 1.00 60.91 ? 235 GLN A CB 1 ATOM 1845 C CG . GLN A 1 237 ? -1.656 17.812 36.352 1.00 63.68 ? 235 GLN A CG 1 ATOM 1846 C CD . GLN A 1 237 ? -2.298 17.216 35.081 1.00 65.20 ? 235 GLN A CD 1 ATOM 1847 O OE1 . GLN A 1 237 ? -2.974 17.930 34.314 1.00 66.84 ? 235 GLN A OE1 1 ATOM 1848 N NE2 . GLN A 1 237 ? -2.076 15.914 34.848 1.00 64.60 ? 235 GLN A NE2 1 ATOM 1849 N N . ASP A 1 238 ? -0.095 20.797 35.835 1.00 65.77 ? 236 ASP A N 1 ATOM 1850 C CA . ASP A 1 238 ? -0.125 22.279 35.853 1.00 68.50 ? 236 ASP A CA 1 ATOM 1851 C C . ASP A 1 238 ? 0.252 22.911 34.512 1.00 67.23 ? 236 ASP A C 1 ATOM 1852 O O . ASP A 1 238 ? -0.403 22.639 33.494 1.00 66.42 ? 236 ASP A O 1 ATOM 1853 C CB . ASP A 1 238 ? 0.660 22.878 37.046 1.00 71.84 ? 236 ASP A CB 1 ATOM 1854 C CG . ASP A 1 238 ? 2.174 22.753 36.908 1.00 71.51 ? 236 ASP A CG 1 ATOM 1855 O OD1 . ASP A 1 238 ? 2.713 23.057 35.824 1.00 69.08 ? 236 ASP A OD1 1 ATOM 1856 O OD2 . ASP A 1 238 ? 2.824 22.383 37.916 1.00 74.00 ? 236 ASP A OD2 1 HETATM 1857 C C1 . NAG B 2 . ? 27.085 3.184 -16.563 1.00 68.30 ? 301 NAG A C1 1 HETATM 1858 C C2 . NAG B 2 . ? 27.887 2.701 -17.790 1.00 72.22 ? 301 NAG A C2 1 HETATM 1859 C C3 . NAG B 2 . ? 27.319 3.221 -19.122 1.00 72.83 ? 301 NAG A C3 1 HETATM 1860 C C4 . NAG B 2 . ? 25.809 3.029 -19.185 1.00 72.02 ? 301 NAG A C4 1 HETATM 1861 C C5 . NAG B 2 . ? 25.158 3.614 -17.933 1.00 71.79 ? 301 NAG A C5 1 HETATM 1862 C C6 . NAG B 2 . ? 23.629 3.524 -17.994 1.00 72.15 ? 301 NAG A C6 1 HETATM 1863 C C7 . NAG B 2 . ? 30.249 2.150 -17.418 1.00 75.04 ? 301 NAG A C7 1 HETATM 1864 C C8 . NAG B 2 . ? 31.616 2.440 -17.979 1.00 74.90 ? 301 NAG A C8 1 HETATM 1865 N N2 . NAG B 2 . ? 29.300 3.062 -17.665 1.00 73.71 ? 301 NAG A N2 1 HETATM 1866 O O3 . NAG B 2 . ? 27.910 2.563 -20.232 1.00 73.61 ? 301 NAG A O3 1 HETATM 1867 O O4 . NAG B 2 . ? 25.309 3.658 -20.344 1.00 72.60 ? 301 NAG A O4 1 HETATM 1868 O O5 . NAG B 2 . ? 25.680 2.981 -16.767 1.00 69.79 ? 301 NAG A O5 1 HETATM 1869 O O6 . NAG B 2 . ? 23.189 2.185 -18.063 1.00 73.57 ? 301 NAG A O6 1 HETATM 1870 O O7 . NAG B 2 . ? 30.040 1.116 -16.771 1.00 74.92 ? 301 NAG A O7 1 HETATM 1871 C C1 . NAG C 2 . ? 24.953 -0.170 8.164 1.00 74.30 ? 401 NAG A C1 1 HETATM 1872 C C2 . NAG C 2 . ? 24.018 -0.619 7.034 1.00 79.32 ? 401 NAG A C2 1 HETATM 1873 C C3 . NAG C 2 . ? 22.528 -0.285 7.274 1.00 80.29 ? 401 NAG A C3 1 HETATM 1874 C C4 . NAG C 2 . ? 22.114 -0.044 8.739 1.00 80.38 ? 401 NAG A C4 1 HETATM 1875 C C5 . NAG C 2 . ? 23.237 0.608 9.557 1.00 79.42 ? 401 NAG A C5 1 HETATM 1876 C C6 . NAG C 2 . ? 22.884 0.876 11.030 1.00 79.80 ? 401 NAG A C6 1 HETATM 1877 C C7 . NAG C 2 . ? 24.243 -0.457 4.576 1.00 82.89 ? 401 NAG A C7 1 HETATM 1878 C C8 . NAG C 2 . ? 23.783 0.560 3.563 1.00 82.33 ? 401 NAG A C8 1 HETATM 1879 N N2 . NAG C 2 . ? 24.500 0.012 5.800 1.00 80.99 ? 401 NAG A N2 1 HETATM 1880 O O3 . NAG C 2 . ? 21.725 -1.332 6.753 1.00 81.40 ? 401 NAG A O3 1 HETATM 1881 O O4 . NAG C 2 . ? 20.943 0.754 8.788 1.00 80.64 ? 401 NAG A O4 1 HETATM 1882 O O5 . NAG C 2 . ? 24.356 -0.249 9.453 1.00 76.32 ? 401 NAG A O5 1 HETATM 1883 O O6 . NAG C 2 . ? 22.239 -0.225 11.647 1.00 80.27 ? 401 NAG A O6 1 HETATM 1884 O O7 . NAG C 2 . ? 24.374 -1.649 4.268 1.00 83.66 ? 401 NAG A O7 1 HETATM 1885 C C1 . NAG D 2 . ? 31.685 14.396 -26.072 1.00 73.54 ? 501 NAG A C1 1 HETATM 1886 C C2 . NAG D 2 . ? 30.852 14.085 -27.339 1.00 79.93 ? 501 NAG A C2 1 HETATM 1887 C C3 . NAG D 2 . ? 31.321 14.805 -28.613 1.00 81.47 ? 501 NAG A C3 1 HETATM 1888 C C4 . NAG D 2 . ? 31.677 16.264 -28.340 1.00 82.07 ? 501 NAG A C4 1 HETATM 1889 C C5 . NAG D 2 . ? 32.696 16.394 -27.197 1.00 81.60 ? 501 NAG A C5 1 HETATM 1890 C C6 . NAG D 2 . ? 32.871 17.886 -26.861 1.00 83.61 ? 501 NAG A C6 1 HETATM 1891 C C7 . NAG D 2 . ? 29.688 12.007 -28.031 1.00 82.79 ? 501 NAG A C7 1 HETATM 1892 C C8 . NAG D 2 . ? 29.515 11.837 -29.525 1.00 82.47 ? 501 NAG A C8 1 HETATM 1893 N N2 . NAG D 2 . ? 30.786 12.636 -27.579 1.00 81.33 ? 501 NAG A N2 1 HETATM 1894 O O3 . NAG D 2 . ? 30.293 14.782 -29.585 1.00 82.38 ? 501 NAG A O3 1 HETATM 1895 O O4 . NAG D 2 . ? 32.131 16.865 -29.545 1.00 82.77 ? 501 NAG A O4 1 HETATM 1896 O O5 . NAG D 2 . ? 32.248 15.714 -26.026 1.00 77.02 ? 501 NAG A O5 1 HETATM 1897 O O6 . NAG D 2 . ? 34.016 18.228 -26.078 1.00 87.06 ? 501 NAG A O6 1 HETATM 1898 O O7 . NAG D 2 . ? 28.834 11.556 -27.265 1.00 83.90 ? 501 NAG A O7 1 HETATM 1899 C C1 . FUC E 3 . ? 34.103 19.684 -25.957 1.00 89.81 ? 502 FUC A C1 1 HETATM 1900 C C2 . FUC E 3 . ? 34.247 20.161 -24.493 1.00 90.51 ? 502 FUC A C2 1 HETATM 1901 C C3 . FUC E 3 . ? 35.672 20.423 -23.971 1.00 90.96 ? 502 FUC A C3 1 HETATM 1902 C C4 . FUC E 3 . ? 36.796 20.570 -25.029 1.00 91.17 ? 502 FUC A C4 1 HETATM 1903 C C5 . FUC E 3 . ? 36.442 20.045 -26.436 1.00 91.06 ? 502 FUC A C5 1 HETATM 1904 C C6 . FUC E 3 . ? 37.321 20.665 -27.524 1.00 90.93 ? 502 FUC A C6 1 HETATM 1905 O O2 . FUC E 3 . ? 33.600 19.267 -23.602 1.00 91.10 ? 502 FUC A O2 1 HETATM 1906 O O3 . FUC E 3 . ? 35.624 21.553 -23.112 1.00 90.08 ? 502 FUC A O3 1 HETATM 1907 O O4 . FUC E 3 . ? 37.276 21.907 -25.090 1.00 90.82 ? 502 FUC A O4 1 HETATM 1908 O O5 . FUC E 3 . ? 35.093 20.278 -26.793 1.00 90.35 ? 502 FUC A O5 1 HETATM 1909 NA NA . NA F 4 . ? 28.415 6.645 -13.985 1.00 39.46 ? 503 NA A NA 1 HETATM 1910 C C . FMT G 5 . ? 3.588 6.166 28.735 1.00 40.23 ? 601 FMT A C 1 HETATM 1911 O O1 . FMT G 5 . ? 2.812 5.448 28.060 1.00 40.88 ? 601 FMT A O1 1 HETATM 1912 O O2 . FMT G 5 . ? 3.573 6.261 29.981 1.00 38.45 ? 601 FMT A O2 1 HETATM 1913 C C . FMT H 5 . ? 0.080 7.403 2.132 1.00 42.73 ? 602 FMT A C 1 HETATM 1914 O O1 . FMT H 5 . ? -0.630 8.377 1.927 1.00 43.04 ? 602 FMT A O1 1 HETATM 1915 O O2 . FMT H 5 . ? 0.921 7.410 3.008 1.00 41.77 ? 602 FMT A O2 1 HETATM 1916 C C . FMT I 5 . ? 7.884 17.444 35.828 1.00 66.98 ? 603 FMT A C 1 HETATM 1917 O O1 . FMT I 5 . ? 7.418 18.555 35.482 1.00 66.30 ? 603 FMT A O1 1 HETATM 1918 O O2 . FMT I 5 . ? 8.904 16.948 35.291 1.00 67.03 ? 603 FMT A O2 1 HETATM 1919 C C . FMT J 5 . ? 40.548 13.788 10.259 1.00 46.44 ? 604 FMT A C 1 HETATM 1920 O O1 . FMT J 5 . ? 40.222 12.799 9.594 1.00 46.50 ? 604 FMT A O1 1 HETATM 1921 O O2 . FMT J 5 . ? 40.861 14.855 9.719 1.00 45.60 ? 604 FMT A O2 1 HETATM 1922 C C . FMT K 5 . ? 28.779 18.175 20.760 1.00 68.26 ? 605 FMT A C 1 HETATM 1923 O O1 . FMT K 5 . ? 29.489 19.164 20.948 1.00 67.96 ? 605 FMT A O1 1 HETATM 1924 O O2 . FMT K 5 . ? 28.976 17.100 21.340 1.00 68.44 ? 605 FMT A O2 1 HETATM 1925 C C . FMT L 5 . ? 25.929 12.396 -20.739 1.00 61.52 ? 606 FMT A C 1 HETATM 1926 O O1 . FMT L 5 . ? 25.606 11.273 -20.336 1.00 61.07 ? 606 FMT A O1 1 HETATM 1927 O O2 . FMT L 5 . ? 27.111 12.694 -20.960 1.00 61.68 ? 606 FMT A O2 1 HETATM 1928 C C . FMT M 5 . ? 34.069 22.793 10.177 1.00 78.05 ? 607 FMT A C 1 HETATM 1929 O O1 . FMT M 5 . ? 34.886 23.685 9.904 1.00 78.21 ? 607 FMT A O1 1 HETATM 1930 O O2 . FMT M 5 . ? 33.695 22.599 11.341 1.00 77.93 ? 607 FMT A O2 1 HETATM 1931 C C . FMT N 5 . ? 39.903 5.823 3.646 1.00 53.10 ? 608 FMT A C 1 HETATM 1932 O O1 . FMT N 5 . ? 39.195 4.832 4.062 1.00 54.07 ? 608 FMT A O1 1 HETATM 1933 O O2 . FMT N 5 . ? 40.136 6.846 4.355 1.00 50.58 ? 608 FMT A O2 1 HETATM 1934 O O . HOH O 6 . ? 29.226 6.841 -16.228 1.00 28.88 ? 609 HOH A O 1 HETATM 1935 O O . HOH O 6 . ? 26.028 7.187 -14.472 1.00 31.91 ? 610 HOH A O 1 HETATM 1936 O O . HOH O 6 . ? 30.670 5.936 -13.432 1.00 27.76 ? 611 HOH A O 1 HETATM 1937 O O . HOH O 6 . ? 25.368 5.041 -11.574 1.00 37.73 ? 612 HOH A O 1 HETATM 1938 O O . HOH O 6 . ? 34.539 6.362 -13.776 1.00 31.09 ? 613 HOH A O 1 HETATM 1939 O O . HOH O 6 . ? 31.997 4.965 -15.969 1.00 46.37 ? 614 HOH A O 1 HETATM 1940 O O . HOH O 6 . ? 35.045 19.611 -19.836 1.00 35.35 ? 615 HOH A O 1 HETATM 1941 O O . HOH O 6 . ? 37.859 17.816 2.796 1.00 29.46 ? 616 HOH A O 1 HETATM 1942 O O . HOH O 6 . ? 7.991 5.884 11.895 1.00 32.55 ? 617 HOH A O 1 HETATM 1943 O O . HOH O 6 . ? 1.646 12.483 -2.961 1.00 47.29 ? 618 HOH A O 1 HETATM 1944 O O . HOH O 6 . ? 9.096 23.526 6.668 1.00 23.85 ? 619 HOH A O 1 HETATM 1945 O O . HOH O 6 . ? 26.336 28.662 4.563 1.00 39.88 ? 620 HOH A O 1 HETATM 1946 O O . HOH O 6 . ? -7.197 13.196 11.260 1.00 37.43 ? 621 HOH A O 1 HETATM 1947 O O . HOH O 6 . ? 15.728 12.235 -3.229 1.00 32.62 ? 622 HOH A O 1 HETATM 1948 O O . HOH O 6 . ? 16.779 9.602 5.018 1.00 28.25 ? 623 HOH A O 1 HETATM 1949 O O . HOH O 6 . ? 15.325 24.569 17.908 1.00 33.96 ? 624 HOH A O 1 HETATM 1950 O O . HOH O 6 . ? -5.987 5.567 11.841 1.00 30.62 ? 625 HOH A O 1 HETATM 1951 O O . HOH O 6 . ? 17.582 21.513 20.777 1.00 42.45 ? 626 HOH A O 1 HETATM 1952 O O . HOH O 6 . ? 34.426 23.899 -9.145 1.00 42.66 ? 627 HOH A O 1 HETATM 1953 O O . HOH O 6 . ? 19.760 15.001 18.290 1.00 33.32 ? 628 HOH A O 1 HETATM 1954 O O . HOH O 6 . ? 16.361 10.042 17.733 1.00 31.92 ? 629 HOH A O 1 HETATM 1955 O O . HOH O 6 . ? 35.478 8.244 -17.548 1.00 44.66 ? 630 HOH A O 1 HETATM 1956 O O . HOH O 6 . ? -6.277 11.276 28.544 1.00 47.74 ? 631 HOH A O 1 HETATM 1957 O O . HOH O 6 . ? -8.371 13.231 18.563 1.00 22.38 ? 632 HOH A O 1 HETATM 1958 O O . HOH O 6 . ? 25.975 4.777 -2.045 1.00 30.11 ? 633 HOH A O 1 HETATM 1959 O O . HOH O 6 . ? 29.646 3.323 9.364 1.00 44.27 ? 634 HOH A O 1 HETATM 1960 O O . HOH O 6 . ? 20.313 10.067 11.097 1.00 27.91 ? 635 HOH A O 1 HETATM 1961 O O . HOH O 6 . ? 28.364 23.675 -11.620 1.00 46.57 ? 636 HOH A O 1 HETATM 1962 O O . HOH O 6 . ? 2.256 3.638 8.664 1.00 47.88 ? 637 HOH A O 1 HETATM 1963 O O . HOH O 6 . ? 4.233 19.882 2.501 1.00 29.69 ? 638 HOH A O 1 HETATM 1964 O O . HOH O 6 . ? -5.607 5.200 17.657 1.00 41.93 ? 639 HOH A O 1 HETATM 1965 O O . HOH O 6 . ? 32.605 17.307 -15.318 1.00 25.28 ? 640 HOH A O 1 HETATM 1966 O O . HOH O 6 . ? 36.009 0.567 3.499 1.00 41.28 ? 641 HOH A O 1 HETATM 1967 O O . HOH O 6 . ? 20.049 3.330 8.704 1.00 58.41 ? 642 HOH A O 1 HETATM 1968 O O . HOH O 6 . ? 23.386 25.512 9.352 1.00 27.18 ? 643 HOH A O 1 HETATM 1969 O O . HOH O 6 . ? 33.806 16.686 -23.835 1.00 51.77 ? 644 HOH A O 1 HETATM 1970 O O . HOH O 6 . ? 37.527 6.389 5.458 1.00 40.54 ? 645 HOH A O 1 HETATM 1971 O O . HOH O 6 . ? 33.768 10.380 -19.936 1.00 35.21 ? 646 HOH A O 1 HETATM 1972 O O . HOH O 6 . ? -0.116 7.052 26.897 1.00 40.40 ? 647 HOH A O 1 HETATM 1973 O O . HOH O 6 . ? 26.609 3.306 3.465 1.00 32.87 ? 648 HOH A O 1 HETATM 1974 O O . HOH O 6 . ? 6.747 5.358 17.826 1.00 22.68 ? 649 HOH A O 1 HETATM 1975 O O . HOH O 6 . ? 16.954 5.035 -2.837 1.00 41.39 ? 650 HOH A O 1 HETATM 1976 O O . HOH O 6 . ? -7.522 17.620 10.852 1.00 60.36 ? 651 HOH A O 1 HETATM 1977 O O . HOH O 6 . ? 14.416 13.371 20.128 1.00 44.37 ? 652 HOH A O 1 HETATM 1978 O O . HOH O 6 . ? 32.700 21.231 -13.360 1.00 39.44 ? 653 HOH A O 1 HETATM 1979 O O . HOH O 6 . ? -4.664 9.753 23.268 1.00 47.64 ? 654 HOH A O 1 HETATM 1980 O O . HOH O 6 . ? 25.267 21.461 -5.485 1.00 43.51 ? 655 HOH A O 1 HETATM 1981 O O . HOH O 6 . ? 17.089 19.242 -5.583 1.00 39.67 ? 656 HOH A O 1 HETATM 1982 O O . HOH O 6 . ? -5.824 14.307 29.398 1.00 40.97 ? 657 HOH A O 1 HETATM 1983 O O . HOH O 6 . ? 21.598 6.976 -9.534 1.00 43.02 ? 658 HOH A O 1 HETATM 1984 O O . HOH O 6 . ? 17.218 14.247 -11.025 1.00 53.77 ? 659 HOH A O 1 HETATM 1985 O O . HOH O 6 . ? -2.307 2.720 12.308 1.00 50.21 ? 660 HOH A O 1 HETATM 1986 O O . HOH O 6 . ? 20.114 20.007 -16.408 1.00 55.28 ? 661 HOH A O 1 HETATM 1987 O O . HOH O 6 . ? -7.772 16.688 23.400 1.00 47.19 ? 662 HOH A O 1 HETATM 1988 O O . HOH O 6 . ? 11.142 23.510 -2.822 1.00 43.21 ? 663 HOH A O 1 HETATM 1989 O O . HOH O 6 . ? 27.815 2.885 11.323 1.00 54.73 ? 664 HOH A O 1 HETATM 1990 O O . HOH O 6 . ? 19.006 7.471 11.272 1.00 47.43 ? 665 HOH A O 1 HETATM 1991 O O . HOH O 6 . ? -3.904 7.490 -14.182 1.00 42.97 ? 666 HOH A O 1 HETATM 1992 O O . HOH O 6 . ? 17.907 11.461 -6.826 1.00 46.77 ? 667 HOH A O 1 HETATM 1993 O O . HOH O 6 . ? 5.203 19.954 37.715 1.00 68.86 ? 668 HOH A O 1 HETATM 1994 O O . HOH O 6 . ? 25.297 21.352 -20.999 1.00 46.43 ? 669 HOH A O 1 HETATM 1995 O O . HOH O 6 . ? 13.309 24.551 10.044 1.00 36.89 ? 670 HOH A O 1 HETATM 1996 O O . HOH O 6 . ? 12.475 25.771 12.091 1.00 42.54 ? 671 HOH A O 1 HETATM 1997 O O . HOH O 6 . ? 13.561 17.396 22.157 1.00 38.42 ? 672 HOH A O 1 HETATM 1998 O O . HOH O 6 . ? 0.648 25.445 29.910 1.00 41.99 ? 673 HOH A O 1 HETATM 1999 O O . HOH O 6 . ? 12.452 8.799 -5.148 1.00 49.61 ? 674 HOH A O 1 HETATM 2000 O O . HOH O 6 . ? 5.430 20.374 -0.368 1.00 62.50 ? 675 HOH A O 1 HETATM 2001 O O . HOH O 6 . ? 22.353 3.824 8.154 1.00 46.39 ? 676 HOH A O 1 HETATM 2002 O O . HOH O 6 . ? 20.621 8.572 -19.562 1.00 57.33 ? 677 HOH A O 1 HETATM 2003 O O . HOH O 6 . ? 20.053 17.690 -11.000 1.00 46.44 ? 678 HOH A O 1 HETATM 2004 O O . HOH O 6 . ? 29.259 12.104 18.993 1.00 37.00 ? 679 HOH A O 1 HETATM 2005 O O . HOH O 6 . ? 22.553 7.715 -6.428 1.00 41.56 ? 680 HOH A O 1 HETATM 2006 O O . HOH O 6 . ? -0.506 21.138 6.229 1.00 59.95 ? 681 HOH A O 1 HETATM 2007 O O . HOH O 6 . ? 35.749 16.225 14.378 1.00 44.18 ? 682 HOH A O 1 HETATM 2008 O O . HOH O 6 . ? -6.363 17.673 26.949 1.00 46.84 ? 683 HOH A O 1 HETATM 2009 O O . HOH O 6 . ? 30.975 5.591 12.690 1.00 49.63 ? 684 HOH A O 1 HETATM 2010 O O . HOH O 6 . ? 37.835 9.413 14.480 1.00 41.98 ? 685 HOH A O 1 HETATM 2011 O O . HOH O 6 . ? 32.013 11.448 18.286 1.00 47.51 ? 686 HOH A O 1 HETATM 2012 O O . HOH O 6 . ? 26.100 15.219 22.444 1.00 39.82 ? 687 HOH A O 1 HETATM 2013 O O . HOH O 6 . ? -9.354 19.011 12.101 1.00 46.95 ? 688 HOH A O 1 HETATM 2014 O O . HOH O 6 . ? 6.900 24.828 7.659 1.00 45.20 ? 689 HOH A O 1 HETATM 2015 O O . HOH O 6 . ? 28.316 27.966 10.683 1.00 52.26 ? 690 HOH A O 1 HETATM 2016 O O . HOH O 6 . ? 22.193 20.342 -13.379 1.00 40.17 ? 691 HOH A O 1 HETATM 2017 O O . HOH O 6 . ? -7.450 10.170 21.990 1.00 40.65 ? 692 HOH A O 1 HETATM 2018 O O . HOH O 6 . ? 31.592 -0.342 0.872 1.00 45.81 ? 693 HOH A O 1 HETATM 2019 O O . HOH O 6 . ? 11.280 13.653 31.157 1.00 53.86 ? 694 HOH A O 1 HETATM 2020 O O . HOH O 6 . ? 21.505 8.275 16.734 1.00 49.08 ? 695 HOH A O 1 HETATM 2021 O O . HOH O 6 . ? 0.800 11.262 31.643 1.00 56.63 ? 696 HOH A O 1 HETATM 2022 O O . HOH O 6 . ? 11.974 21.606 10.926 1.00 54.41 ? 697 HOH A O 1 HETATM 2023 O O . HOH O 6 . ? 5.529 23.526 -1.341 1.00 62.66 ? 698 HOH A O 1 HETATM 2024 O O . HOH O 6 . ? -1.785 26.227 16.763 1.00 54.20 ? 699 HOH A O 1 HETATM 2025 O O . HOH O 6 . ? 2.971 22.461 27.143 1.00 32.18 ? 700 HOH A O 1 HETATM 2026 O O . HOH O 6 . ? 5.718 17.953 -1.647 1.00 53.48 ? 701 HOH A O 1 HETATM 2027 O O . HOH O 6 . ? -6.012 15.230 11.810 1.00 32.95 ? 702 HOH A O 1 HETATM 2028 O O . HOH O 6 . ? -7.534 20.002 27.342 1.00 55.94 ? 703 HOH A O 1 HETATM 2029 O O . HOH O 6 . ? 18.025 7.737 14.348 1.00 52.69 ? 704 HOH A O 1 HETATM 2030 O O . HOH O 6 . ? -3.646 6.662 14.750 1.00 38.96 ? 705 HOH A O 1 HETATM 2031 O O . HOH O 6 . ? 10.711 16.575 -0.908 1.00 32.81 ? 706 HOH A O 1 HETATM 2032 O O . HOH O 6 . ? 2.962 21.392 5.015 1.00 46.22 ? 707 HOH A O 1 HETATM 2033 O O . HOH O 6 . ? 17.340 12.491 13.538 1.00 39.86 ? 708 HOH A O 1 HETATM 2034 O O . HOH O 6 . ? 16.088 12.536 11.223 1.00 45.77 ? 709 HOH A O 1 HETATM 2035 O O . HOH O 6 . ? 17.077 19.954 14.924 1.00 52.15 ? 710 HOH A O 1 HETATM 2036 O O . HOH O 6 . ? 16.465 18.063 11.246 1.00 34.37 ? 711 HOH A O 1 HETATM 2037 O O . HOH O 6 . ? 16.539 14.499 12.840 1.00 47.39 ? 712 HOH A O 1 HETATM 2038 O O . HOH O 6 . ? 17.992 14.169 10.261 1.00 39.36 ? 713 HOH A O 1 HETATM 2039 O O . HOH O 6 . ? 18.979 16.537 9.889 1.00 37.80 ? 714 HOH A O 1 HETATM 2040 O O . HOH O 6 . ? 15.225 16.509 12.871 1.00 40.17 ? 715 HOH A O 1 HETATM 2041 O O . HOH O 6 . ? 15.158 19.441 12.679 1.00 53.60 ? 716 HOH A O 1 HETATM 2042 O O . HOH O 6 . ? 17.773 20.114 10.234 1.00 31.42 ? 717 HOH A O 1 HETATM 2043 O O . HOH O 6 . ? 16.617 20.574 8.804 1.00 27.19 ? 718 HOH A O 1 HETATM 2044 O O . HOH O 6 . ? 14.009 21.813 6.447 1.00 28.49 ? 719 HOH A O 1 HETATM 2045 O O . HOH O 6 . ? 16.030 20.873 6.574 1.00 29.05 ? 720 HOH A O 1 HETATM 2046 O O . HOH O 6 . ? 16.012 21.193 4.022 1.00 34.09 ? 721 HOH A O 1 HETATM 2047 O O . HOH O 6 . ? 12.484 23.523 7.761 1.00 26.59 ? 722 HOH A O 1 HETATM 2048 O O . HOH O 6 . ? 37.142 19.773 12.811 1.00 42.77 ? 723 HOH A O 1 HETATM 2049 O O . HOH O 6 . ? 18.433 11.880 -15.599 1.00 55.59 ? 724 HOH A O 1 HETATM 2050 O O . HOH O 6 . ? 37.362 17.582 -23.219 1.00 42.62 ? 725 HOH A O 1 HETATM 2051 O O . HOH O 6 . ? 35.922 28.290 8.046 1.00 54.49 ? 726 HOH A O 1 HETATM 2052 O O . HOH O 6 . ? 39.034 21.525 0.245 1.00 45.33 ? 727 HOH A O 1 HETATM 2053 O O . HOH O 6 . ? 25.033 4.631 -7.583 1.00 42.91 ? 728 HOH A O 1 HETATM 2054 O O . HOH O 6 . ? 26.782 1.641 -6.402 1.00 46.47 ? 729 HOH A O 1 HETATM 2055 O O . HOH O 6 . ? 13.104 8.685 27.929 1.00 47.71 ? 730 HOH A O 1 HETATM 2056 O O . HOH O 6 . ? 30.598 -1.374 9.071 1.00 62.71 ? 731 HOH A O 1 HETATM 2057 O O . HOH O 6 . ? -0.189 18.534 3.404 1.00 59.81 ? 732 HOH A O 1 HETATM 2058 O O . HOH O 6 . ? -5.177 5.054 26.090 1.00 53.78 ? 733 HOH A O 1 HETATM 2059 O O . HOH O 6 . ? 34.320 -3.572 7.267 1.00 51.32 ? 734 HOH A O 1 HETATM 2060 O O . HOH O 6 . ? 10.330 18.416 18.401 1.00 30.92 ? 735 HOH A O 1 HETATM 2061 O O . HOH O 6 . ? 18.293 7.581 -2.198 1.00 41.52 ? 736 HOH A O 1 HETATM 2062 O O . HOH O 6 . ? 1.959 26.245 32.047 1.00 50.04 ? 737 HOH A O 1 # loop_ _atom_site_anisotrop.id _atom_site_anisotrop.type_symbol _atom_site_anisotrop.pdbx_label_atom_id _atom_site_anisotrop.pdbx_label_alt_id _atom_site_anisotrop.pdbx_label_comp_id _atom_site_anisotrop.pdbx_label_asym_id _atom_site_anisotrop.pdbx_label_seq_id _atom_site_anisotrop.pdbx_PDB_ins_code _atom_site_anisotrop.U[1][1] _atom_site_anisotrop.U[2][2] _atom_site_anisotrop.U[3][3] _atom_site_anisotrop.U[1][2] _atom_site_anisotrop.U[1][3] _atom_site_anisotrop.U[2][3] _atom_site_anisotrop.pdbx_auth_seq_id _atom_site_anisotrop.pdbx_auth_comp_id _atom_site_anisotrop.pdbx_auth_asym_id _atom_site_anisotrop.pdbx_auth_atom_id 1 N N . SER A 12 ? 0.8756 0.4471 0.7173 -0.0515 0.1340 -0.0552 10 SER A N 2 C CA . SER A 12 ? 0.7872 0.4516 0.6781 -0.0465 0.1050 -0.0554 10 SER A CA 3 C C . SER A 12 ? 0.7585 0.4383 0.6513 -0.0227 0.0961 -0.0588 10 SER A C 4 O O . SER A 12 ? 0.7927 0.4437 0.6684 -0.0340 0.1044 -0.0760 10 SER A O 5 C CB . SER A 12 ? 0.7632 0.4762 0.6843 -0.0868 0.0963 -0.0748 10 SER A CB 6 O OG . SER A 12 ? 0.7278 0.5038 0.6782 -0.0831 0.0756 -0.0826 10 SER A OG 7 N N A PRO A 13 ? 0.7007 0.4281 0.6136 0.0066 0.0805 -0.0445 11 PRO A N 8 N N B PRO A 13 ? 0.6999 0.4276 0.6130 0.0067 0.0804 -0.0444 11 PRO A N 9 C CA A PRO A 13 ? 0.6828 0.4274 0.5971 0.0291 0.0749 -0.0467 11 PRO A CA 10 C CA B PRO A 13 ? 0.6792 0.4269 0.5952 0.0287 0.0740 -0.0467 11 PRO A CA 11 C C A PRO A 13 ? 0.6468 0.4231 0.5778 0.0072 0.0657 -0.0661 11 PRO A C 12 C C B PRO A 13 ? 0.6483 0.4230 0.5787 0.0059 0.0661 -0.0667 11 PRO A C 13 O O A PRO A 13 ? 0.5985 0.4175 0.5558 -0.0146 0.0538 -0.0711 11 PRO A O 14 O O B PRO A 13 ? 0.6064 0.4194 0.5609 -0.0183 0.0556 -0.0733 11 PRO A O 15 C CB A PRO A 13 ? 0.6272 0.4303 0.5666 0.0523 0.0595 -0.0307 11 PRO A CB 16 C CB B PRO A 13 ? 0.6176 0.4282 0.5621 0.0483 0.0572 -0.0320 11 PRO A CB 17 C CG A PRO A 13 ? 0.6044 0.4298 0.5617 0.0353 0.0526 -0.0257 11 PRO A CG 18 C CG B PRO A 13 ? 0.6254 0.4311 0.5684 0.0481 0.0586 -0.0190 11 PRO A CG 19 C CD A PRO A 13 ? 0.6561 0.4259 0.5903 0.0167 0.0688 -0.0285 11 PRO A CD 20 C CD B PRO A 13 ? 0.6576 0.4253 0.5906 0.0169 0.0694 -0.0281 11 PRO A CD 21 N N . GLN A 14 ? 0.6634 0.4202 0.5766 0.0170 0.0718 -0.0756 12 GLN A N 22 C CA . GLN A 14 ? 0.6309 0.4185 0.5537 0.0014 0.0635 -0.0930 12 GLN A CA 23 C C . GLN A 14 ? 0.5842 0.4060 0.5154 0.0285 0.0566 -0.0870 12 GLN A C 24 O O . GLN A 14 ? 0.6211 0.4138 0.5300 0.0514 0.0679 -0.0870 12 GLN A O 25 C CB . GLN A 14 ? 0.6954 0.4290 0.5855 -0.0191 0.0792 -0.1153 12 GLN A CB 26 C CG . GLN A 14 ? 0.7460 0.4552 0.6313 -0.0546 0.0870 -0.1242 12 GLN A CG 27 C CD . GLN A 14 ? 0.8517 0.5129 0.7055 -0.0853 0.1032 -0.1515 12 GLN A CD 28 O OE1 . GLN A 14 ? 0.9147 0.5222 0.7337 -0.0729 0.1181 -0.1594 12 GLN A OE1 29 N NE2 . GLN A 14 ? 0.8864 0.5691 0.7511 -0.1268 0.1015 -0.1680 12 GLN A NE2 30 N N . LEU A 15 ? 0.5001 0.3824 0.4619 0.0256 0.0404 -0.0817 13 LEU A N 31 C CA . LEU A 15 ? 0.4648 0.3865 0.4392 0.0456 0.0348 -0.0739 13 LEU A CA 32 C C . LEU A 15 ? 0.4469 0.3916 0.4214 0.0360 0.0300 -0.0858 13 LEU A C 33 O O . LEU A 15 ? 0.4330 0.3995 0.4177 0.0162 0.0209 -0.0908 13 LEU A O 34 C CB . LEU A 15 ? 0.4052 0.3701 0.4076 0.0451 0.0236 -0.0602 13 LEU A CB 35 C CG . LEU A 15 ? 0.4197 0.3946 0.4288 0.0624 0.0238 -0.0455 13 LEU A CG 36 C CD1 . LEU A 15 ? 0.4598 0.3920 0.4444 0.0831 0.0357 -0.0406 13 LEU A CD1 37 C CD2 . LEU A 15 ? 0.3492 0.3439 0.3773 0.0470 0.0151 -0.0394 13 LEU A CD2 38 N N . ARG A 16 ? 0.4519 0.3944 0.4131 0.0520 0.0366 -0.0901 14 ARG A N 39 C CA . ARG A 16 ? 0.4313 0.4024 0.3913 0.0468 0.0322 -0.0982 14 ARG A CA 40 C C . ARG A 16 ? 0.3895 0.4049 0.3674 0.0601 0.0292 -0.0851 14 ARG A C 41 O O . ARG A 16 ? 0.3787 0.4007 0.3612 0.0797 0.0349 -0.0770 14 ARG A O 42 C CB . ARG A 16 ? 0.4843 0.4234 0.4135 0.0527 0.0440 -0.1147 14 ARG A CB 43 C CG . ARG A 16 ? 0.5515 0.4369 0.4561 0.0362 0.0525 -0.1311 14 ARG A CG 44 C CD . ARG A 16 ? 0.6293 0.4948 0.5040 0.0289 0.0601 -0.1538 14 ARG A CD 45 N NE . ARG A 16 ? 0.7213 0.5199 0.5659 0.0130 0.0749 -0.1706 14 ARG A NE 46 C CZ . ARG A 16 ? 0.7808 0.5294 0.5863 0.0097 0.0911 -0.1922 14 ARG A CZ 47 N NH1 . ARG A 16 ? 0.7743 0.5369 0.5665 0.0235 0.0934 -0.2001 14 ARG A NH1 48 N NH2 . ARG A 16 ? 0.8607 0.5401 0.6367 -0.0094 0.1077 -0.2067 14 ARG A NH2 49 N N . VAL A 17 ? 0.3567 0.4033 0.3423 0.0497 0.0216 -0.0832 15 VAL A N 50 C CA . VAL A 17 ? 0.3477 0.4296 0.3437 0.0556 0.0227 -0.0730 15 VAL A CA 51 C C . VAL A 17 ? 0.3465 0.4423 0.3279 0.0515 0.0218 -0.0776 15 VAL A C 52 O O . VAL A 17 ? 0.3719 0.4626 0.3423 0.0419 0.0155 -0.0863 15 VAL A O 53 C CB . VAL A 17 ? 0.3274 0.4278 0.3454 0.0470 0.0172 -0.0591 15 VAL A CB 54 C CG1 . VAL A 17 ? 0.3190 0.4154 0.3501 0.0525 0.0175 -0.0541 15 VAL A CG1 55 C CG2 . VAL A 17 ? 0.3092 0.4060 0.3275 0.0342 0.0088 -0.0582 15 VAL A CG2 56 N N . HIS A 18 ? 0.3354 0.4538 0.3161 0.0585 0.0287 -0.0720 16 HIS A N 57 C CA . HIS A 18 ? 0.3337 0.4672 0.2986 0.0566 0.0298 -0.0710 16 HIS A CA 58 C C . HIS A 18 ? 0.3163 0.4591 0.2878 0.0483 0.0259 -0.0558 16 HIS A C 59 O O . HIS A 18 ? 0.2956 0.4379 0.2855 0.0431 0.0265 -0.0469 16 HIS A O 60 C CB . HIS A 18 ? 0.3389 0.4909 0.2991 0.0668 0.0426 -0.0699 16 HIS A CB 61 C CG . HIS A 18 ? 0.3637 0.5038 0.3123 0.0813 0.0497 -0.0838 16 HIS A CG 62 N ND1 . HIS A 18 ? 0.3955 0.5212 0.3158 0.0838 0.0516 -0.0991 16 HIS A ND1 63 C CD2 . HIS A 18 ? 0.3620 0.5013 0.3197 0.0968 0.0570 -0.0848 16 HIS A CD2 64 C CE1 . HIS A 18 ? 0.4440 0.5510 0.3545 0.0993 0.0618 -0.1095 16 HIS A CE1 65 N NE2 . HIS A 18 ? 0.4209 0.5367 0.3538 0.1104 0.0651 -0.0993 16 HIS A NE2 66 N N . VAL A 19 ? 0.3285 0.4782 0.2808 0.0488 0.0229 -0.0530 17 VAL A N 67 C CA . VAL A 19 ? 0.3173 0.4686 0.2656 0.0480 0.0237 -0.0357 17 VAL A CA 68 C C . VAL A 19 ? 0.3189 0.4693 0.2725 0.0433 0.0388 -0.0242 17 VAL A C 69 O O . VAL A 19 ? 0.3201 0.4828 0.2710 0.0446 0.0484 -0.0276 17 VAL A O 70 C CB . VAL A 19 ? 0.3443 0.5082 0.2640 0.0567 0.0200 -0.0322 17 VAL A CB 71 C CG1 . VAL A 19 ? 0.3269 0.4824 0.2328 0.0627 0.0274 -0.0095 17 VAL A CG1 72 C CG2 . VAL A 19 ? 0.3091 0.4868 0.2284 0.0557 0.0033 -0.0455 17 VAL A CG2 73 N N . GLY A 20 ? 0.3225 0.4601 0.2850 0.0356 0.0419 -0.0134 18 GLY A N 74 C CA . GLY A 20 ? 0.3413 0.4776 0.3084 0.0231 0.0576 -0.0061 18 GLY A CA 75 C C . GLY A 20 ? 0.3229 0.4715 0.3193 0.0130 0.0564 -0.0133 18 GLY A C 76 O O . GLY A 20 ? 0.3259 0.4740 0.3287 -0.0026 0.0662 -0.0096 18 GLY A O 77 N N . GLU A 21 ? 0.3134 0.4715 0.3238 0.0216 0.0455 -0.0239 19 GLU A N 78 C CA . GLU A 21 ? 0.3016 0.4757 0.3356 0.0188 0.0436 -0.0286 19 GLU A CA 79 C C . GLU A 21 ? 0.2897 0.4480 0.3334 0.0100 0.0372 -0.0256 19 GLU A C 80 O O . GLU A 21 ? 0.2866 0.4204 0.3211 0.0099 0.0325 -0.0212 19 GLU A O 81 C CB . GLU A 21 ? 0.3062 0.4838 0.3433 0.0357 0.0377 -0.0380 19 GLU A CB 82 C CG . GLU A 21 ? 0.3436 0.5414 0.3746 0.0481 0.0461 -0.0433 19 GLU A CG 83 C CD . GLU A 21 ? 0.4168 0.6094 0.4482 0.0682 0.0443 -0.0513 19 GLU A CD 84 O OE1 . GLU A 21 ? 0.4253 0.5848 0.4397 0.0741 0.0407 -0.0589 19 GLU A OE1 85 O OE2 . GLU A 21 ? 0.4712 0.6931 0.5177 0.0784 0.0479 -0.0501 19 GLU A OE2 86 N N . SER A 22 ? 0.2694 0.4482 0.3314 0.0050 0.0370 -0.0285 20 SER A N 87 C CA . SER A 22 ? 0.2574 0.4262 0.3282 -0.0015 0.0307 -0.0279 20 SER A CA 88 C C . SER A 22 ? 0.2576 0.4251 0.3342 0.0141 0.0210 -0.0315 20 SER A C 89 O O . SER A 22 ? 0.2696 0.4495 0.3460 0.0295 0.0217 -0.0349 20 SER A O 90 C CB . SER A 22 ? 0.2592 0.4555 0.3426 -0.0191 0.0369 -0.0303 20 SER A CB 91 O OG . SER A 22 ? 0.2497 0.4318 0.3222 -0.0394 0.0500 -0.0276 20 SER A OG 92 N N . VAL A 23 ? 0.2448 0.3940 0.3235 0.0113 0.0147 -0.0302 21 VAL A N 93 C CA . VAL A 23 ? 0.2391 0.3794 0.3190 0.0233 0.0088 -0.0316 21 VAL A CA 94 C C . VAL A 23 ? 0.2305 0.3713 0.3175 0.0163 0.0053 -0.0291 21 VAL A C 95 O O . VAL A 23 ? 0.2198 0.3488 0.3065 0.0036 0.0055 -0.0277 21 VAL A O 96 C CB . VAL A 23 ? 0.2586 0.3670 0.3263 0.0270 0.0059 -0.0351 21 VAL A CB 97 C CG1 . VAL A 23 ? 0.2231 0.3208 0.2904 0.0160 0.0026 -0.0329 21 VAL A CG1 98 C CG2 . VAL A 23 ? 0.2453 0.3328 0.3078 0.0363 0.0052 -0.0368 21 VAL A CG2 99 N N . LEU A 24 ? 0.2391 0.3953 0.3297 0.0274 0.0031 -0.0280 22 LEU A N 100 C CA . LEU A 24 ? 0.2269 0.3866 0.3204 0.0235 -0.0008 -0.0257 22 LEU A CA 101 C C . LEU A 24 ? 0.2363 0.3621 0.3189 0.0350 -0.0022 -0.0221 22 LEU A C 102 O O . LEU A 24 ? 0.2431 0.3623 0.3169 0.0540 0.0000 -0.0195 22 LEU A O 103 C CB . LEU A 24 ? 0.2213 0.4312 0.3239 0.0288 -0.0024 -0.0261 22 LEU A CB 104 C CG . LEU A 24 ? 0.2086 0.4379 0.3147 0.0170 -0.0064 -0.0276 22 LEU A CG 105 C CD1 . LEU A 24 ? 0.1838 0.4786 0.3033 0.0097 -0.0069 -0.0340 22 LEU A CD1 106 C CD2 . LEU A 24 ? 0.2319 0.4478 0.3278 0.0340 -0.0107 -0.0204 22 LEU A CD2 107 N N . MET A 25 ? 0.2386 0.3410 0.3196 0.0236 -0.0033 -0.0219 23 MET A N 108 C CA . MET A 25 ? 0.2686 0.3395 0.3395 0.0276 -0.0020 -0.0195 23 MET A CA 109 C C . MET A 25 ? 0.2721 0.3490 0.3410 0.0291 -0.0034 -0.0140 23 MET A C 110 O O . MET A 25 ? 0.2674 0.3526 0.3423 0.0162 -0.0052 -0.0155 23 MET A O 111 C CB . MET A 25 ? 0.2661 0.3186 0.3386 0.0139 -0.0019 -0.0236 23 MET A CB 112 C CG . MET A 25 ? 0.2970 0.3496 0.3685 0.0129 -0.0019 -0.0295 23 MET A CG 113 S SD . MET A 25 ? 0.3537 0.4042 0.4289 -0.0001 -0.0044 -0.0341 23 MET A SD 114 C CE . MET A 25 ? 0.3510 0.4191 0.4252 0.0024 -0.0064 -0.0350 23 MET A CE 115 N N . GLY A 26 ? 0.2955 0.3657 0.3515 0.0475 -0.0012 -0.0073 24 GLY A N 116 C CA . GLY A 26 ? 0.3148 0.3952 0.3635 0.0549 -0.0027 -0.0001 24 GLY A CA 117 C C . GLY A 26 ? 0.3344 0.3822 0.3758 0.0433 0.0012 0.0016 24 GLY A C 118 O O . GLY A 26 ? 0.3403 0.3523 0.3761 0.0369 0.0075 -0.0002 24 GLY A O 119 N N . CYS A 27 ? 0.3350 0.4005 0.3766 0.0385 -0.0018 0.0033 25 CYS A N 120 C CA . CYS A 27 ? 0.3550 0.3969 0.3875 0.0313 0.0032 0.0067 25 CYS A CA 121 C C . CYS A 27 ? 0.3564 0.4235 0.3780 0.0397 -0.0003 0.0123 25 CYS A C 122 O O . CYS A 27 ? 0.3425 0.4323 0.3706 0.0270 -0.0041 0.0055 25 CYS A O 123 C CB . CYS A 27 ? 0.3376 0.3772 0.3853 0.0105 0.0036 -0.0019 25 CYS A CB 124 S SG . CYS A 27 ? 0.4032 0.4236 0.4455 0.0001 0.0114 0.0002 25 CYS A SG 125 N N . VAL A 28 ? 0.3881 0.4494 0.3891 0.0632 0.0020 0.0246 26 VAL A N 126 C CA . VAL A 28 ? 0.3997 0.4940 0.3866 0.0781 -0.0029 0.0319 26 VAL A CA 127 C C . VAL A 28 ? 0.4428 0.4961 0.4007 0.0875 0.0075 0.0460 26 VAL A C 128 O O . VAL A 28 ? 0.4791 0.4833 0.4180 0.0997 0.0191 0.0561 26 VAL A O 129 C CB . VAL A 28 ? 0.4086 0.5416 0.3918 0.1068 -0.0088 0.0384 26 VAL A CB 130 C CG1 . VAL A 28 ? 0.4145 0.5963 0.3825 0.1247 -0.0162 0.0459 26 VAL A CG1 131 C CG2 . VAL A 28 ? 0.3687 0.5431 0.3802 0.0950 -0.0162 0.0245 26 VAL A CG2 132 N N . VAL A 29 ? 0.4519 0.5200 0.4028 0.0799 0.0060 0.0457 27 VAL A N 133 C CA . VAL A 29 ? 0.4930 0.5241 0.4142 0.0869 0.0177 0.0598 27 VAL A CA 134 C C . VAL A 29 ? 0.5399 0.5919 0.4322 0.1218 0.0147 0.0765 27 VAL A C 135 O O . VAL A 29 ? 0.5285 0.6432 0.4256 0.1278 0.0009 0.0719 27 VAL A O 136 C CB . VAL A 29 ? 0.4797 0.5179 0.4051 0.0643 0.0190 0.0516 27 VAL A CB 137 C CG1 . VAL A 29 ? 0.5233 0.5286 0.4165 0.0708 0.0325 0.0666 27 VAL A CG1 138 C CG2 . VAL A 29 ? 0.4259 0.4497 0.3792 0.0378 0.0220 0.0375 27 VAL A CG2 139 N N . GLN A 30 ? 0.6039 0.6042 0.4641 0.1458 0.0287 0.0955 28 GLN A N 140 C CA . GLN A 30 ? 0.6573 0.6721 0.4833 0.1877 0.0282 0.1161 28 GLN A CA 141 C C . GLN A 30 ? 0.6698 0.6953 0.4685 0.1926 0.0295 0.1264 28 GLN A C 142 O O . GLN A 30 ? 0.6954 0.6609 0.4686 0.1861 0.0471 0.1367 28 GLN A O 143 C CB . GLN A 30 ? 0.7361 0.6761 0.5273 0.2147 0.0478 0.1349 28 GLN A CB 144 C CG . GLN A 30 ? 0.7586 0.6783 0.5705 0.2096 0.0496 0.1238 28 GLN A CG 145 C CD . GLN A 30 ? 0.7651 0.7657 0.6098 0.2191 0.0295 0.1132 28 GLN A CD 146 O OE1 . GLN A 30 ? 0.8065 0.8693 0.6455 0.2480 0.0184 0.1215 28 GLN A OE1 147 N NE2 . GLN A 30 ? 0.7540 0.7588 0.6326 0.1939 0.0254 0.0945 28 GLN A NE2 148 N N . ARG A 31 ? 0.6480 0.7529 0.4511 0.2017 0.0116 0.1222 29 ARG A N 149 C CA . ARG A 31 ? 0.6754 0.8024 0.4476 0.2118 0.0103 0.1320 29 ARG A CA 150 C C . ARG A 31 ? 0.7011 0.9058 0.4582 0.2513 -0.0052 0.1420 29 ARG A C 151 O O . ARG A 31 ? 0.6678 0.9273 0.4508 0.2587 -0.0183 0.1332 29 ARG A O 152 C CB . ARG A 31 ? 0.6294 0.7859 0.4232 0.1716 0.0033 0.1086 29 ARG A CB 153 C CG . ARG A 31 ? 0.6042 0.6990 0.4141 0.1363 0.0179 0.0990 29 ARG A CG 154 C CD . ARG A 31 ? 0.6465 0.6797 0.4215 0.1389 0.0388 0.1169 29 ARG A CD 155 N NE . ARG A 31 ? 0.6489 0.6446 0.4462 0.1036 0.0506 0.1044 29 ARG A NE 156 C CZ . ARG A 31 ? 0.6613 0.6034 0.4673 0.0919 0.0642 0.1056 29 ARG A CZ 157 N NH1 . ARG A 31 ? 0.6945 0.6005 0.4857 0.1112 0.0702 0.1179 29 ARG A NH1 158 N NH2 . ARG A 31 ? 0.6260 0.5539 0.4555 0.0607 0.0722 0.0926 29 ARG A NH2 159 N N . THR A 32 ? 0.7581 0.9745 0.4731 0.2774 -0.0037 0.1605 30 THR A N 160 C CA . THR A 32 ? 0.7858 1.0963 0.4885 0.3138 -0.0219 0.1675 30 THR A CA 161 C C . THR A 32 ? 0.7411 1.1461 0.4744 0.2783 -0.0434 0.1360 30 THR A C 162 O O . THR A 32 ? 0.7273 1.2272 0.4790 0.2872 -0.0621 0.1258 30 THR A O 163 C CB . THR A 32 ? 0.8637 1.1580 0.5037 0.3631 -0.0129 0.2021 30 THR A CB 164 O OG1 . THR A 32 ? 0.8850 1.1477 0.5021 0.3406 -0.0040 0.2022 30 THR A OG1 165 C CG2 . THR A 32 ? 0.9260 1.1220 0.5320 0.3989 0.0114 0.2317 30 THR A CG2 166 N N . GLU A 33 ? 0.7225 1.1005 0.4612 0.2368 -0.0387 0.1191 31 GLU A N 167 C CA . GLU A 33 ? 0.6898 1.1357 0.4517 0.1978 -0.0534 0.0863 31 GLU A CA 168 C C . GLU A 33 ? 0.6304 1.0724 0.4417 0.1581 -0.0556 0.0593 31 GLU A C 169 O O . GLU A 33 ? 0.6077 0.9809 0.4349 0.1512 -0.0437 0.0633 31 GLU A O 170 C CB . GLU A 33 ? 0.7120 1.1291 0.4507 0.1766 -0.0449 0.0810 31 GLU A CB 171 C CG . GLU A 33 ? 0.7166 1.1998 0.4664 0.1393 -0.0577 0.0465 31 GLU A CG 172 C CD . GLU A 33 ? 0.7690 1.2430 0.4837 0.1307 -0.0514 0.0438 31 GLU A CD 173 O OE1 . GLU A 33 ? 0.7528 1.1628 0.4720 0.1053 -0.0360 0.0361 31 GLU A OE1 174 O OE2 . GLU A 33 ? 0.8281 1.3664 0.5108 0.1505 -0.0623 0.0485 31 GLU A OE2 175 N N . GLU A 34 ? 0.6037 1.1217 0.4358 0.1316 -0.0699 0.0316 32 GLU A N 176 C CA . GLU A 34 ? 0.5570 1.0697 0.4279 0.0910 -0.0694 0.0053 32 GLU A CA 177 C C . GLU A 34 ? 0.5376 1.0004 0.4056 0.0544 -0.0589 -0.0120 32 GLU A C 178 O O . GLU A 34 ? 0.5528 1.0525 0.4070 0.0344 -0.0632 -0.0309 32 GLU A O 179 C CB . GLU A 34 ? 0.5529 1.1665 0.4427 0.0741 -0.0855 -0.0184 32 GLU A CB 180 C CG . GLU A 34 ? 0.5835 1.2557 0.4884 0.1059 -0.0950 -0.0065 32 GLU A CG 181 C CD . GLU A 34 ? 0.6147 1.3956 0.5450 0.0810 -0.1092 -0.0339 32 GLU A CD 182 O OE1 . GLU A 34 ? 0.6293 1.4003 0.5812 0.0324 -0.1045 -0.0616 32 GLU A OE1 183 O OE2 . GLU A 34 ? 0.6347 1.5110 0.5620 0.1107 -0.1235 -0.0273 32 GLU A OE2 184 N N . LYS A 35 ? 0.4997 0.8823 0.3788 0.0466 -0.0447 -0.0067 33 LYS A N 185 C CA . LYS A 35 ? 0.4784 0.8116 0.3546 0.0202 -0.0324 -0.0190 33 LYS A CA 186 C C . LYS A 35 ? 0.4401 0.7512 0.3454 -0.0097 -0.0280 -0.0389 33 LYS A C 187 O O . LYS A 35 ? 0.4161 0.7253 0.3443 -0.0069 -0.0303 -0.0359 33 LYS A O 188 C CB . LYS A 35 ? 0.4889 0.7545 0.3536 0.0349 -0.0179 0.0026 33 LYS A CB 189 C CG . LYS A 35 ? 0.5175 0.7854 0.3462 0.0663 -0.0164 0.0271 33 LYS A CG 190 C CD . LYS A 35 ? 0.5052 0.7137 0.3164 0.0642 0.0018 0.0382 33 LYS A CD 191 C CE . LYS A 35 ? 0.5674 0.7637 0.3376 0.0960 0.0079 0.0665 33 LYS A CE 192 N NZ . LYS A 35 ? 0.5677 0.7074 0.3200 0.0904 0.0287 0.0775 33 LYS A NZ 193 N N . HIS A 36 ? 0.4323 0.7230 0.3323 -0.0361 -0.0197 -0.0583 34 HIS A N 194 C CA . HIS A 36 ? 0.4083 0.6613 0.3274 -0.0587 -0.0107 -0.0724 34 HIS A CA 195 C C . HIS A 36 ? 0.3750 0.5701 0.3068 -0.0466 -0.0006 -0.0561 34 HIS A C 196 O O . HIS A 36 ? 0.3673 0.5413 0.2885 -0.0323 0.0049 -0.0416 34 HIS A O 197 C CB . HIS A 36 ? 0.4404 0.6763 0.3423 -0.0852 -0.0004 -0.0961 34 HIS A CB 198 C CG . HIS A 36 ? 0.4640 0.7542 0.3529 -0.1087 -0.0076 -0.1204 34 HIS A CG 199 N ND1 . HIS A 36 ? 0.5283 0.7984 0.4005 -0.1406 0.0039 -0.1480 34 HIS A ND1 200 C CD2 . HIS A 36 ? 0.5025 0.8692 0.3911 -0.1060 -0.0241 -0.1228 34 HIS A CD2 201 C CE1 . HIS A 36 ? 0.5559 0.8890 0.4181 -0.1620 -0.0054 -0.1691 34 HIS A CE1 202 N NE2 . HIS A 36 ? 0.5335 0.9329 0.4076 -0.1404 -0.0238 -0.1539 34 HIS A NE2 203 N N . VAL A 37 ? 0.3454 0.5187 0.2985 -0.0547 0.0026 -0.0598 35 VAL A N 204 C CA . VAL A 37 ? 0.3303 0.4586 0.2970 -0.0479 0.0113 -0.0499 35 VAL A CA 205 C C . VAL A 37 ? 0.3461 0.4406 0.3054 -0.0587 0.0252 -0.0608 35 VAL A C 206 O O . VAL A 37 ? 0.3464 0.4317 0.3001 -0.0754 0.0304 -0.0772 35 VAL A O 207 C CB . VAL A 37 ? 0.3105 0.4358 0.2998 -0.0479 0.0078 -0.0478 35 VAL A CB 208 C CG1 . VAL A 37 ? 0.2865 0.3748 0.2893 -0.0418 0.0151 -0.0397 35 VAL A CG1 209 C CG2 . VAL A 37 ? 0.2902 0.4473 0.2840 -0.0322 -0.0036 -0.0367 35 VAL A CG2 210 N N . ASP A 38 ? 0.3468 0.4216 0.3036 -0.0489 0.0334 -0.0519 36 ASP A N 211 C CA . ASP A 38 ? 0.3710 0.4169 0.3232 -0.0512 0.0479 -0.0592 36 ASP A CA 212 C C . ASP A 38 ? 0.3600 0.3839 0.3327 -0.0452 0.0530 -0.0550 36 ASP A C 213 O O . ASP A 38 ? 0.3785 0.3776 0.3451 -0.0475 0.0628 -0.0637 36 ASP A O 214 C CB . ASP A 38 ? 0.3815 0.4266 0.3238 -0.0431 0.0557 -0.0521 36 ASP A CB 215 C CG . ASP A 38 ? 0.4545 0.5027 0.3674 -0.0504 0.0612 -0.0652 36 ASP A CG 216 O OD1 . ASP A 38 ? 0.5584 0.6107 0.4580 -0.0648 0.0585 -0.0820 36 ASP A OD1 217 O OD2 . ASP A 38 ? 0.5475 0.5947 0.4488 -0.0444 0.0698 -0.0608 36 ASP A OD2 218 N N . ARG A 39 ? 0.3403 0.3719 0.3332 -0.0367 0.0473 -0.0418 37 ARG A N 219 C CA . ARG A 39 ? 0.3296 0.3526 0.3415 -0.0296 0.0502 -0.0372 37 ARG A CA 220 C C . ARG A 39 ? 0.2903 0.3227 0.3184 -0.0286 0.0394 -0.0300 37 ARG A C 221 O O . ARG A 39 ? 0.2481 0.2886 0.2762 -0.0277 0.0349 -0.0230 37 ARG A O 222 C CB . ARG A 39 ? 0.3438 0.3731 0.3640 -0.0224 0.0582 -0.0310 37 ARG A CB 223 C CG . ARG A 39 ? 0.4266 0.4478 0.4443 -0.0135 0.0708 -0.0352 37 ARG A CG 224 C CD . ARG A 39 ? 0.4962 0.5125 0.5259 -0.0038 0.0706 -0.0334 37 ARG A CD 225 N NE . ARG A 39 ? 0.5196 0.5640 0.5739 0.0033 0.0686 -0.0262 37 ARG A NE 226 C CZ . ARG A 39 ? 0.5703 0.6294 0.6336 0.0194 0.0764 -0.0242 37 ARG A CZ 227 N NH1 . ARG A 39 ? 0.6273 0.6647 0.6732 0.0341 0.0892 -0.0271 37 ARG A NH1 228 N NH2 . ARG A 39 ? 0.5872 0.6849 0.6757 0.0212 0.0724 -0.0203 37 ARG A NH2 229 N N . VAL A 40 ? 0.2781 0.3047 0.3157 -0.0270 0.0378 -0.0310 38 VAL A N 230 C CA . VAL A 40 ? 0.2649 0.2995 0.3181 -0.0244 0.0298 -0.0252 38 VAL A CA 231 C C . VAL A 40 ? 0.2652 0.2980 0.3292 -0.0168 0.0326 -0.0236 38 VAL A C 232 O O . VAL A 40 ? 0.2723 0.2898 0.3279 -0.0127 0.0392 -0.0261 38 VAL A O 233 C CB . VAL A 40 ? 0.2718 0.3108 0.3242 -0.0286 0.0221 -0.0274 38 VAL A CB 234 C CG1 . VAL A 40 ? 0.2353 0.2813 0.2983 -0.0238 0.0150 -0.0210 38 VAL A CG1 235 C CG2 . VAL A 40 ? 0.2803 0.3306 0.3203 -0.0357 0.0195 -0.0327 38 VAL A CG2 236 N N . ASP A 41 ? 0.2608 0.3084 0.3399 -0.0149 0.0289 -0.0198 39 ASP A N 237 C CA . ASP A 41 ? 0.2569 0.3160 0.3470 -0.0065 0.0278 -0.0183 39 ASP A CA 238 C C . ASP A 41 ? 0.2417 0.3075 0.3391 -0.0113 0.0191 -0.0185 39 ASP A C 239 O O . ASP A 41 ? 0.2378 0.3030 0.3367 -0.0197 0.0173 -0.0191 39 ASP A O 240 C CB . ASP A 41 ? 0.2738 0.3591 0.3775 -0.0024 0.0317 -0.0178 39 ASP A CB 241 C CG . ASP A 41 ? 0.3161 0.3981 0.4130 0.0046 0.0425 -0.0179 39 ASP A CG 242 O OD1 . ASP A 41 ? 0.3428 0.4042 0.4257 0.0161 0.0492 -0.0177 39 ASP A OD1 243 O OD2 . ASP A 41 ? 0.3628 0.4602 0.4664 -0.0022 0.0465 -0.0186 39 ASP A OD2 244 N N . TRP A 42 ? 0.2236 0.2901 0.3209 -0.0048 0.0159 -0.0175 40 TRP A N 245 C CA . TRP A 42 ? 0.2080 0.2837 0.3107 -0.0072 0.0087 -0.0190 40 TRP A CA 246 C C . TRP A 42 ? 0.2087 0.3102 0.3193 0.0018 0.0066 -0.0185 40 TRP A C 247 O O . TRP A 42 ? 0.2104 0.3092 0.3140 0.0162 0.0100 -0.0129 40 TRP A O 248 C CB . TRP A 42 ? 0.2089 0.2711 0.3028 -0.0063 0.0069 -0.0182 40 TRP A CB 249 C CG . TRP A 42 ? 0.1994 0.2532 0.2889 -0.0129 0.0057 -0.0196 40 TRP A CG 250 C CD1 . TRP A 42 ? 0.2074 0.2553 0.2895 -0.0168 0.0085 -0.0205 40 TRP A CD1 251 C CD2 . TRP A 42 ? 0.1883 0.2418 0.2780 -0.0140 0.0019 -0.0205 40 TRP A CD2 252 N NE1 . TRP A 42 ? 0.2118 0.2657 0.2921 -0.0178 0.0046 -0.0205 40 TRP A NE1 253 C CE2 . TRP A 42 ? 0.2213 0.2740 0.3047 -0.0136 0.0016 -0.0192 40 TRP A CE2 254 C CE3 . TRP A 42 ? 0.2238 0.2767 0.3152 -0.0149 -0.0002 -0.0234 40 TRP A CE3 255 C CZ2 . TRP A 42 ? 0.2350 0.2858 0.3134 -0.0076 -0.0002 -0.0173 40 TRP A CZ2 256 C CZ3 . TRP A 42 ? 0.2107 0.2510 0.2943 -0.0125 0.0003 -0.0235 40 TRP A CZ3 257 C CH2 . TRP A 42 ? 0.2405 0.2794 0.3175 -0.0058 0.0005 -0.0187 40 TRP A CH2 258 N N . LEU A 43 ? 0.2143 0.3403 0.3362 -0.0069 0.0023 -0.0245 41 LEU A N 259 C CA . LEU A 43 ? 0.2259 0.3943 0.3584 -0.0010 -0.0020 -0.0269 41 LEU A CA 260 C C . LEU A 43 ? 0.2267 0.4053 0.3583 -0.0097 -0.0095 -0.0348 41 LEU A C 261 O O . LEU A 43 ? 0.2393 0.3983 0.3679 -0.0266 -0.0086 -0.0420 41 LEU A O 262 C CB . LEU A 43 ? 0.2316 0.4337 0.3807 -0.0121 0.0007 -0.0332 41 LEU A CB 263 C CG . LEU A 43 ? 0.2689 0.5125 0.4307 0.0019 0.0041 -0.0301 41 LEU A CG 264 C CD1 . LEU A 43 ? 0.3092 0.5991 0.4908 -0.0208 0.0040 -0.0424 41 LEU A CD1 265 C CD2 . LEU A 43 ? 0.2097 0.4793 0.3688 0.0314 0.0008 -0.0218 41 LEU A CD2 266 N N . PHE A 44 ? 0.2241 0.4329 0.3551 0.0035 -0.0155 -0.0332 42 PHE A N 267 C CA . PHE A 44 ? 0.2367 0.4594 0.3635 -0.0031 -0.0228 -0.0417 42 PHE A CA 268 C C . PHE A 44 ? 0.2597 0.5457 0.4004 -0.0097 -0.0296 -0.0527 42 PHE A C 269 O O . PHE A 44 ? 0.2362 0.5670 0.3858 0.0080 -0.0319 -0.0466 42 PHE A O 270 C CB . PHE A 44 ? 0.2386 0.4481 0.3485 0.0162 -0.0241 -0.0315 42 PHE A CB 271 C CG . PHE A 44 ? 0.2459 0.4747 0.3483 0.0128 -0.0315 -0.0398 42 PHE A CG 272 C CD1 . PHE A 44 ? 0.2297 0.4383 0.3281 -0.0063 -0.0314 -0.0525 42 PHE A CD1 273 C CD2 . PHE A 44 ? 0.2826 0.5500 0.3783 0.0310 -0.0376 -0.0349 42 PHE A CD2 274 C CE1 . PHE A 44 ? 0.2375 0.4624 0.3258 -0.0104 -0.0368 -0.0630 42 PHE A CE1 275 C CE2 . PHE A 44 ? 0.2742 0.5629 0.3599 0.0273 -0.0448 -0.0440 42 PHE A CE2 276 C CZ . PHE A 44 ? 0.2551 0.5219 0.3376 0.0049 -0.0442 -0.0594 42 PHE A CZ 277 N N . SER A 45 ? 0.2948 0.5860 0.4362 -0.0355 -0.0314 -0.0699 43 SER A N 278 C CA . SER A 45 ? 0.3376 0.6935 0.4886 -0.0480 -0.0393 -0.0856 43 SER A CA 279 C C . SER A 45 ? 0.3902 0.7367 0.5245 -0.0608 -0.0435 -0.0997 43 SER A C 280 O O . SER A 45 ? 0.3880 0.6769 0.5086 -0.0742 -0.0362 -0.1049 43 SER A O 281 C CB . SER A 45 ? 0.3455 0.7250 0.5142 -0.0772 -0.0335 -0.0996 43 SER A CB 282 O OG . SER A 45 ? 0.3554 0.6680 0.5155 -0.0947 -0.0210 -0.1001 43 SER A OG 283 N N . LYS A 46 ? 0.4468 0.8519 0.5797 -0.0529 -0.0548 -0.1050 44 LYS A N 284 C CA . LYS A 46 ? 0.4906 0.8963 0.6049 -0.0640 -0.0596 -0.1205 44 LYS A CA 285 C C . LYS A 46 ? 0.5389 0.9410 0.6509 -0.1066 -0.0549 -0.1498 44 LYS A C 286 O O . LYS A 46 ? 0.5785 0.9212 0.6693 -0.1181 -0.0472 -0.1584 44 LYS A O 287 C CB . LYS A 46 ? 0.4971 0.9687 0.6056 -0.0407 -0.0731 -0.1164 44 LYS A CB 288 C CG . LYS A 46 ? 0.5132 0.9464 0.6031 -0.0053 -0.0710 -0.0910 44 LYS A CG 289 C CD . LYS A 46 ? 0.5433 1.0299 0.6213 0.0274 -0.0806 -0.0778 44 LYS A CD 290 C CE . LYS A 46 ? 0.5588 0.9876 0.6133 0.0557 -0.0721 -0.0528 44 LYS A CE 291 N NZ . LYS A 46 ? 0.5745 1.0114 0.6214 0.0944 -0.0691 -0.0263 44 LYS A NZ 292 N N . ASP A 47 ? 0.5651 1.0271 0.6955 -0.1309 -0.0571 -0.1663 45 ASP A N 293 C CA . ASP A 47 ? 0.6152 1.0482 0.7430 -0.1768 -0.0440 -0.1905 45 ASP A CA 294 C C . ASP A 47 ? 0.6013 1.0300 0.7501 -0.1766 -0.0359 -0.1778 45 ASP A C 295 O O . ASP A 47 ? 0.6013 0.9866 0.7488 -0.1478 -0.0332 -0.1534 45 ASP A O 296 C CB . ASP A 47 ? 0.6535 1.1496 0.7818 -0.2171 -0.0480 -0.2254 45 ASP A CB 297 C CG . ASP A 47 ? 0.6675 1.2711 0.8069 -0.1986 -0.0692 -0.2275 45 ASP A CG 298 O OD1 . ASP A 47 ? 0.7026 1.3022 0.8222 -0.1742 -0.0781 -0.2211 45 ASP A OD1 299 O OD2 . ASP A 47 ? 0.6910 1.3880 0.8570 -0.2098 -0.0763 -0.2371 45 ASP A OD2 300 N N . LYS A 48 ? 0.6183 1.0909 0.7850 -0.2095 -0.0306 -0.1944 46 LYS A N 301 C CA . LYS A 48 ? 0.5884 1.1014 0.7825 -0.1962 -0.0299 -0.1798 46 LYS A CA 302 C C . LYS A 48 ? 0.5570 1.1459 0.7622 -0.1565 -0.0485 -0.1676 46 LYS A C 303 O O . LYS A 48 ? 0.5316 1.1012 0.7357 -0.1156 -0.0506 -0.1414 46 LYS A O 304 C CB . LYS A 48 ? 0.6081 1.1754 0.8234 -0.2384 -0.0215 -0.2009 46 LYS A CB 305 C CG . LYS A 48 ? 0.5890 1.2045 0.8331 -0.2200 -0.0200 -0.1851 46 LYS A CG 306 C CD . LYS A 48 ? 0.6062 1.3269 0.8815 -0.2513 -0.0194 -0.2062 46 LYS A CD 307 C CE . LYS A 48 ? 0.6491 1.3317 0.9231 -0.3033 0.0038 -0.2217 46 LYS A CE 308 N NZ . LYS A 48 ? 0.6534 1.4445 0.9559 -0.3468 0.0050 -0.2506 46 LYS A NZ 309 N N . ASP A 49 ? 0.5555 1.2238 0.7654 -0.1701 -0.0603 -0.1880 47 ASP A N 310 C CA . ASP A 49 ? 0.5301 1.2743 0.7418 -0.1327 -0.0787 -0.1788 47 ASP A CA 311 C C . ASP A 49 ? 0.4944 1.3437 0.7386 -0.1218 -0.0845 -0.1770 47 ASP A C 312 O O . ASP A 49 ? 0.5054 1.4378 0.7548 -0.0888 -0.0991 -0.1694 47 ASP A O 313 C CB . ASP A 49 ? 0.5118 1.1967 0.7037 -0.0824 -0.0802 -0.1465 47 ASP A CB 314 C CG . ASP A 49 ? 0.5326 1.2790 0.7146 -0.0452 -0.0957 -0.1364 47 ASP A CG 315 O OD1 . ASP A 49 ? 0.5729 1.4043 0.7602 -0.0592 -0.1076 -0.1563 47 ASP A OD1 316 O OD2 . ASP A 49 ? 0.5498 1.2604 0.7156 -0.0033 -0.0949 -0.1091 47 ASP A OD2 317 N N . ASP A 50 ? 0.4630 1.3112 0.7276 -0.1475 -0.0718 -0.1831 48 ASP A N 318 C CA . ASP A 50 ? 0.4188 1.3288 0.7107 -0.1205 -0.0710 -0.1681 48 ASP A CA 319 C C . ASP A 50 ? 0.3673 1.2390 0.6491 -0.0601 -0.0708 -0.1326 48 ASP A C 320 O O . ASP A 50 ? 0.3684 1.2851 0.6683 -0.0340 -0.0680 -0.1203 48 ASP A O 321 C CB . ASP A 50 ? 0.4228 1.4658 0.7509 -0.1466 -0.0753 -0.1912 48 ASP A CB 322 C CG . ASP A 50 ? 0.4275 1.4915 0.7832 -0.1529 -0.0610 -0.1870 48 ASP A CG 323 O OD1 . ASP A 50 ? 0.3996 1.3662 0.7442 -0.1537 -0.0453 -0.1738 48 ASP A OD1 324 O OD2 . ASP A 50 ? 0.4444 1.6336 0.8337 -0.1584 -0.0655 -0.1989 48 ASP A OD2 325 N N . ALA A 51 ? 0.3238 1.1103 0.5748 -0.0402 -0.0713 -0.1178 49 ALA A N 326 C CA . ALA A 51 ? 0.2900 1.0246 0.5256 0.0084 -0.0669 -0.0872 49 ALA A CA 327 C C . ALA A 51 ? 0.2600 0.8764 0.4740 0.0033 -0.0557 -0.0775 49 ALA A C 328 O O . ALA A 51 ? 0.2654 0.8296 0.4656 -0.0221 -0.0548 -0.0876 49 ALA A O 329 C CB . ALA A 51 ? 0.2937 1.0613 0.5120 0.0512 -0.0781 -0.0723 49 ALA A CB 330 N N . SER A 52 ? 0.2305 0.8080 0.4399 0.0301 -0.0465 -0.0580 50 SER A N 331 C CA . SER A 52 ? 0.2161 0.6978 0.4053 0.0314 -0.0375 -0.0474 50 SER A CA 332 C C . SER A 52 ? 0.2148 0.6623 0.3842 0.0729 -0.0319 -0.0243 50 SER A C 333 O O . SER A 52 ? 0.2131 0.7024 0.3830 0.1059 -0.0320 -0.0133 50 SER A O 334 C CB . SER A 52 ? 0.2007 0.6483 0.3993 0.0075 -0.0266 -0.0523 50 SER A CB 335 O OG . SER A 52 ? 0.2593 0.7561 0.4757 0.0202 -0.0224 -0.0490 50 SER A OG 336 N N . GLU A 53 ? 0.2187 0.5878 0.3686 0.0701 -0.0251 -0.0177 51 GLU A N 337 C CA . GLU A 53 ? 0.2519 0.5722 0.3785 0.0988 -0.0152 0.0006 51 GLU A CA 338 C C . GLU A 53 ? 0.2315 0.4815 0.3494 0.0814 -0.0062 0.0000 51 GLU A C 339 O O . GLU A 53 ? 0.2146 0.4475 0.3369 0.0550 -0.0098 -0.0101 51 GLU A O 340 C CB . GLU A 53 ? 0.2866 0.6024 0.3897 0.1209 -0.0182 0.0116 51 GLU A CB 341 C CG . GLU A 53 ? 0.3377 0.6347 0.4336 0.1002 -0.0243 0.0037 51 GLU A CG 342 C CD . GLU A 53 ? 0.4369 0.7534 0.5116 0.1234 -0.0292 0.0132 51 GLU A CD 343 O OE1 . GLU A 53 ? 0.4905 0.7821 0.5405 0.1548 -0.0198 0.0328 51 GLU A OE1 344 O OE2 . GLU A 53 ? 0.4519 0.8040 0.5304 0.1100 -0.0408 0.0010 51 GLU A OE2 345 N N . TYR A 54 ? 0.2512 0.4622 0.3549 0.0971 0.0063 0.0099 52 TYR A N 346 C CA . TYR A 54 ? 0.2650 0.4159 0.3580 0.0804 0.0146 0.0080 52 TYR A CA 347 C C . TYR A 54 ? 0.2681 0.3801 0.3425 0.0753 0.0159 0.0109 52 TYR A C 348 O O . TYR A 54 ? 0.2742 0.3771 0.3305 0.0933 0.0195 0.0207 52 TYR A O 349 C CB . TYR A 54 ? 0.3006 0.4206 0.3810 0.0939 0.0293 0.0134 52 TYR A CB 350 C CG . TYR A 54 ? 0.3045 0.4500 0.4042 0.0851 0.0298 0.0063 52 TYR A CG 351 C CD1 . TYR A 54 ? 0.3191 0.5191 0.4351 0.1015 0.0291 0.0078 52 TYR A CD1 352 C CD2 . TYR A 54 ? 0.3286 0.4508 0.4304 0.0606 0.0310 -0.0016 52 TYR A CD2 353 C CE1 . TYR A 54 ? 0.3260 0.5534 0.4603 0.0910 0.0316 0.0010 52 TYR A CE1 354 C CE2 . TYR A 54 ? 0.3485 0.4926 0.4646 0.0523 0.0335 -0.0066 52 TYR A CE2 355 C CZ . TYR A 54 ? 0.3497 0.5447 0.4823 0.0660 0.0347 -0.0056 52 TYR A CZ 356 O OH . TYR A 54 ? 0.4014 0.6223 0.5488 0.0563 0.0394 -0.0105 52 TYR A OH 357 N N . VAL A 55 ? 0.2594 0.3526 0.3378 0.0513 0.0137 0.0027 53 VAL A N 358 C CA . VAL A 55 ? 0.2691 0.3308 0.3335 0.0431 0.0169 0.0035 53 VAL A CA 359 C C . VAL A 55 ? 0.3046 0.3245 0.3537 0.0385 0.0304 0.0043 53 VAL A C 360 O O . VAL A 55 ? 0.3210 0.3061 0.3476 0.0422 0.0424 0.0097 53 VAL A O 361 C CB . VAL A 55 ? 0.2489 0.3206 0.3253 0.0247 0.0079 -0.0055 53 VAL A CB 362 C CG1 . VAL A 55 ? 0.2538 0.3032 0.3196 0.0162 0.0121 -0.0056 53 VAL A CG1 363 C CG2 . VAL A 55 ? 0.2364 0.3418 0.3212 0.0265 -0.0023 -0.0094 53 VAL A CG2 364 N N . LEU A 56 ? 0.3002 0.3219 0.3581 0.0294 0.0303 -0.0019 54 LEU A N 365 C CA . LEU A 56 ? 0.3298 0.3182 0.3729 0.0211 0.0416 -0.0056 54 LEU A CA 366 C C . LEU A 56 ? 0.3100 0.3102 0.3624 0.0195 0.0410 -0.0098 54 LEU A C 367 O O . LEU A 56 ? 0.2627 0.2924 0.3336 0.0149 0.0312 -0.0117 54 LEU A O 368 C CB . LEU A 56 ? 0.3216 0.3038 0.3629 -0.0003 0.0398 -0.0124 54 LEU A CB 369 C CG . LEU A 56 ? 0.3631 0.3314 0.3955 -0.0190 0.0456 -0.0221 54 LEU A CG 370 C CD1 . LEU A 56 ? 0.3585 0.3311 0.3894 -0.0355 0.0455 -0.0266 54 LEU A CD1 371 C CD2 . LEU A 56 ? 0.3367 0.3278 0.3812 -0.0235 0.0370 -0.0266 54 LEU A CD2 372 N N . PHE A 57 ? 0.3367 0.3094 0.3724 0.0234 0.0541 -0.0113 55 PHE A N 373 C CA . PHE A 57 ? 0.3435 0.3211 0.3816 0.0176 0.0560 -0.0173 55 PHE A CA 374 C C . PHE A 57 ? 0.3615 0.3064 0.3777 0.0014 0.0653 -0.0271 55 PHE A C 375 O O . PHE A 57 ? 0.4071 0.3181 0.4035 -0.0040 0.0754 -0.0296 55 PHE A O 376 C CB . PHE A 57 ? 0.3668 0.3602 0.4107 0.0377 0.0616 -0.0128 55 PHE A CB 377 C CG . PHE A 57 ? 0.4180 0.3810 0.4401 0.0612 0.0776 -0.0073 55 PHE A CG 378 C CD1 . PHE A 57 ? 0.4601 0.4182 0.4752 0.0807 0.0792 0.0031 55 PHE A CD1 379 C CD2 . PHE A 57 ? 0.4990 0.4384 0.5044 0.0685 0.0926 -0.0111 55 PHE A CD2 380 C CE1 . PHE A 57 ? 0.4876 0.4118 0.4763 0.1095 0.0968 0.0118 55 PHE A CE1 381 C CE2 . PHE A 57 ? 0.5335 0.4376 0.5135 0.0963 0.1109 -0.0047 55 PHE A CE2 382 C CZ . PHE A 57 ? 0.5643 0.4586 0.5349 0.1180 0.1133 0.0080 55 PHE A CZ 383 N N . TYR A 58 ? 0.3436 0.3009 0.3619 -0.0089 0.0624 -0.0335 56 TYR A N 384 C CA . TYR A 58 ? 0.3647 0.3052 0.3636 -0.0270 0.0681 -0.0459 56 TYR A CA 385 C C . TYR A 58 ? 0.3723 0.3170 0.3657 -0.0241 0.0724 -0.0493 56 TYR A C 386 O O . TYR A 58 ? 0.3171 0.2902 0.3265 -0.0195 0.0646 -0.0434 56 TYR A O 387 C CB . TYR A 58 ? 0.3543 0.3218 0.3620 -0.0442 0.0548 -0.0499 56 TYR A CB 388 C CG . TYR A 58 ? 0.3602 0.3355 0.3538 -0.0630 0.0548 -0.0632 56 TYR A CG 389 C CD1 . TYR A 58 ? 0.3672 0.3662 0.3614 -0.0611 0.0483 -0.0628 56 TYR A CD1 390 C CD2 . TYR A 58 ? 0.3920 0.3551 0.3702 -0.0848 0.0619 -0.0769 56 TYR A CD2 391 C CE1 . TYR A 58 ? 0.3697 0.3845 0.3486 -0.0766 0.0467 -0.0753 56 TYR A CE1 392 C CE2 . TYR A 58 ? 0.4125 0.3946 0.3786 -0.1051 0.0604 -0.0924 56 TYR A CE2 393 C CZ . TYR A 58 ? 0.3886 0.3998 0.3552 -0.0989 0.0513 -0.0910 56 TYR A CZ 394 O OH . TYR A 58 ? 0.4382 0.4767 0.3912 -0.1166 0.0479 -0.1060 56 TYR A OH 395 N N . TYR A 59 ? 0.4205 0.3310 0.3875 -0.0272 0.0880 -0.0593 57 TYR A N 396 C CA . TYR A 59 ? 0.4397 0.3495 0.3948 -0.0256 0.0951 -0.0653 57 TYR A CA 397 C C . TYR A 59 ? 0.4939 0.3627 0.4140 -0.0426 0.1099 -0.0832 57 TYR A C 398 O O . TYR A 59 ? 0.5188 0.3494 0.4232 -0.0485 0.1204 -0.0873 57 TYR A O 399 C CB . TYR A 59 ? 0.4529 0.3610 0.4134 0.0013 0.1051 -0.0561 57 TYR A CB 400 C CG . TYR A 59 ? 0.4980 0.3585 0.4361 0.0180 0.1239 -0.0558 57 TYR A CG 401 C CD1 . TYR A 59 ? 0.5078 0.3590 0.4507 0.0298 0.1231 -0.0455 57 TYR A CD1 402 C CD2 . TYR A 59 ? 0.5556 0.3754 0.4622 0.0233 0.1443 -0.0654 57 TYR A CD2 403 C CE1 . TYR A 59 ? 0.5680 0.3676 0.4829 0.0490 0.1429 -0.0421 57 TYR A CE1 404 C CE2 . TYR A 59 ? 0.6228 0.3861 0.5007 0.0420 0.1656 -0.0637 57 TYR A CE2 405 C CZ . TYR A 59 ? 0.6202 0.3732 0.5019 0.0560 0.1649 -0.0505 57 TYR A CZ 406 O OH . TYR A 59 ? 0.7066 0.3970 0.5535 0.0788 0.1883 -0.0454 57 TYR A OH 407 N N . SER A 60 ? 0.5153 0.3900 0.4200 -0.0522 0.1125 -0.0946 58 SER A N 408 C CA . SER A 60 ? 0.5775 0.4161 0.4454 -0.0730 0.1272 -0.1165 58 SER A CA 409 C C . SER A 60 ? 0.5930 0.4230 0.4528 -0.1018 0.1262 -0.1290 58 SER A C 410 O O . SER A 60 ? 0.6509 0.4264 0.4808 -0.1148 0.1462 -0.1421 58 SER A O 411 C CB . SER A 60 ? 0.6311 0.4103 0.4712 -0.0551 0.1532 -0.1192 58 SER A CB 412 O OG . SER A 60 ? 0.6465 0.4474 0.4974 -0.0303 0.1540 -0.1094 58 SER A OG 413 N N . ASN A 61 ? 0.5726 0.4556 0.4576 -0.1115 0.1052 -0.1249 59 ASN A N 414 C CA . ASN A 61 ? 0.5950 0.4913 0.4796 -0.1408 0.1015 -0.1374 59 ASN A CA 415 C C . ASN A 61 ? 0.6110 0.4652 0.4934 -0.1425 0.1136 -0.1327 59 ASN A C 416 O O . ASN A 61 ? 0.6362 0.4851 0.5090 -0.1721 0.1196 -0.1468 59 ASN A O 417 C CB . ASN A 61 ? 0.6530 0.5492 0.5079 -0.1752 0.1091 -0.1660 59 ASN A CB 418 C CG . ASN A 61 ? 0.6862 0.6431 0.5440 -0.1757 0.0920 -0.1700 59 ASN A CG 419 O OD1 . ASN A 61 ? 0.6159 0.6192 0.4990 -0.1560 0.0733 -0.1518 59 ASN A OD1 420 N ND2 . ASN A 61 ? 0.8520 0.8042 0.6786 -0.1985 0.1003 -0.1943 59 ASN A ND2 421 N N . LEU A 62 ? 0.6019 0.4331 0.4935 -0.1118 0.1168 -0.1128 60 LEU A N 422 C CA . LEU A 62 ? 0.6267 0.4203 0.5131 -0.1079 0.1275 -0.1046 60 LEU A CA 423 C C . LEU A 62 ? 0.5616 0.3852 0.4795 -0.0816 0.1124 -0.0824 60 LEU A C 424 O O . LEU A 62 ? 0.5228 0.3621 0.4550 -0.0563 0.1062 -0.0707 60 LEU A O 425 C CB . LEU A 62 ? 0.7090 0.4226 0.5556 -0.0980 0.1565 -0.1066 60 LEU A CB 426 C CG . LEU A 62 ? 0.7521 0.4432 0.5944 -0.0565 0.1649 -0.0910 60 LEU A CG 427 C CD1 . LEU A 62 ? 0.8469 0.4950 0.6767 -0.0320 0.1780 -0.0734 60 LEU A CD1 428 C CD2 . LEU A 62 ? 0.8234 0.4647 0.6282 -0.0562 0.1871 -0.1054 60 LEU A CD2 429 N N . SER A 63 ? 0.5404 0.3774 0.4696 -0.0906 0.1067 -0.0788 61 SER A N 430 C CA . SER A 63 ? 0.5140 0.3715 0.4661 -0.0674 0.0954 -0.0605 61 SER A CA 431 C C . SER A 63 ? 0.5487 0.3567 0.4804 -0.0500 0.1121 -0.0497 61 SER A C 432 O O . SER A 63 ? 0.6065 0.3632 0.5077 -0.0636 0.1323 -0.0555 61 SER A O 433 C CB . SER A 63 ? 0.4689 0.3700 0.4436 -0.0790 0.0802 -0.0599 61 SER A CB 434 O OG . SER A 63 ? 0.5414 0.4430 0.5060 -0.1095 0.0865 -0.0747 61 SER A OG 435 N N . VAL A 64 ? 0.5336 0.3583 0.4799 -0.0199 0.1046 -0.0338 62 VAL A N 436 C CA . VAL A 64 ? 0.5677 0.3584 0.4957 0.0053 0.1171 -0.0195 62 VAL A CA 437 C C . VAL A 64 ? 0.5154 0.3494 0.4678 0.0198 0.1000 -0.0070 62 VAL A C 438 O O . VAL A 64 ? 0.4885 0.3608 0.4612 0.0407 0.0885 0.0001 62 VAL A O 439 C CB . VAL A 64 ? 0.6062 0.3646 0.5138 0.0338 0.1328 -0.0141 62 VAL A CB 440 C CG1 . VAL A 64 ? 0.6289 0.4079 0.5471 0.0274 0.1287 -0.0253 62 VAL A CG1 441 C CG2 . VAL A 64 ? 0.6161 0.3949 0.5304 0.0737 0.1294 0.0051 62 VAL A CG2 442 N N A PRO A 65 ? 0.5084 0.3405 0.4589 0.0057 0.0991 -0.0065 63 PRO A N 443 N N B PRO A 65 ? 0.5079 0.3398 0.4583 0.0058 0.0992 -0.0065 63 PRO A N 444 C CA A PRO A 65 ? 0.4824 0.3421 0.4444 0.0209 0.0884 0.0050 63 PRO A CA 445 C CA B PRO A 65 ? 0.4779 0.3412 0.4422 0.0214 0.0870 0.0048 63 PRO A CA 446 C C A PRO A 65 ? 0.5107 0.3525 0.4539 0.0566 0.0972 0.0214 63 PRO A C 447 C C B PRO A 65 ? 0.5093 0.3518 0.4529 0.0561 0.0969 0.0212 63 PRO A C 448 O O A PRO A 65 ? 0.5549 0.3394 0.4637 0.0666 0.1192 0.0264 63 PRO A O 449 O O B PRO A 65 ? 0.5551 0.3394 0.4639 0.0649 0.1191 0.0260 63 PRO A O 450 C CB A PRO A 65 ? 0.4993 0.3427 0.4503 -0.0009 0.0954 0.0023 63 PRO A CB 451 C CB B PRO A 65 ? 0.4843 0.3403 0.4429 -0.0009 0.0904 0.0015 63 PRO A CB 452 C CG A PRO A 65 ? 0.5036 0.3427 0.4554 -0.0331 0.0993 -0.0148 63 PRO A CG 453 C CG B PRO A 65 ? 0.5350 0.3400 0.4661 -0.0230 0.1117 -0.0075 63 PRO A CG 454 C CD A PRO A 65 ? 0.5285 0.3388 0.4662 -0.0277 0.1087 -0.0189 63 PRO A CD 455 C CD B PRO A 65 ? 0.5316 0.3380 0.4669 -0.0262 0.1102 -0.0175 63 PRO A CD 456 N N . THR A 66 ? 0.4731 0.3640 0.4360 0.0764 0.0813 0.0289 64 THR A N 457 C CA . THR A 66 ? 0.4962 0.3942 0.4484 0.1149 0.0851 0.0436 64 THR A CA 458 C C . THR A 66 ? 0.4760 0.4069 0.4294 0.1307 0.0748 0.0538 64 THR A C 459 O O . THR A 66 ? 0.4240 0.3867 0.3970 0.1118 0.0601 0.0463 64 THR A O 460 C CB . THR A 66 ? 0.4644 0.4143 0.4452 0.1256 0.0739 0.0396 64 THR A CB 461 O OG1 . THR A 66 ? 0.4398 0.4468 0.4545 0.1089 0.0528 0.0310 64 THR A OG1 462 C CG2 . THR A 66 ? 0.4674 0.3941 0.4485 0.1115 0.0821 0.0290 64 THR A CG2 463 N N . GLY A 67 ? 0.5072 0.4299 0.4362 0.1683 0.0837 0.0711 65 GLY A N 464 C CA . GLY A 67 ? 0.5130 0.4829 0.4426 0.1919 0.0718 0.0818 65 GLY A CA 465 C C . GLY A 67 ? 0.5189 0.4739 0.4352 0.1780 0.0715 0.0840 65 GLY A C 466 O O . GLY A 67 ? 0.5483 0.4385 0.4354 0.1672 0.0905 0.0882 65 GLY A O 467 N N . ARG A 68 ? 0.4882 0.5038 0.4249 0.1750 0.0514 0.0790 66 ARG A N 468 C CA . ARG A 68 ? 0.5050 0.5121 0.4294 0.1638 0.0510 0.0802 66 ARG A CA 469 C C . ARG A 68 ? 0.4677 0.4576 0.4086 0.1236 0.0506 0.0639 66 ARG A C 470 O O . ARG A 68 ? 0.4816 0.4652 0.4149 0.1117 0.0523 0.0631 66 ARG A O 471 C CB . ARG A 68 ? 0.4988 0.5736 0.4325 0.1763 0.0317 0.0794 66 ARG A CB 472 C CG . ARG A 68 ? 0.4594 0.5883 0.4326 0.1519 0.0117 0.0579 66 ARG A CG 473 C CD . ARG A 68 ? 0.4701 0.6667 0.4470 0.1651 -0.0049 0.0556 66 ARG A CD 474 N NE . ARG A 68 ? 0.4388 0.6745 0.4486 0.1357 -0.0197 0.0325 66 ARG A NE 475 C CZ . ARG A 68 ? 0.4218 0.6489 0.4368 0.1101 -0.0236 0.0187 66 ARG A CZ 476 N NH1 . ARG A 68 ? 0.4656 0.6594 0.4596 0.1094 -0.0162 0.0246 66 ARG A NH1 477 N NH2 . ARG A 68 ? 0.4105 0.6621 0.4498 0.0857 -0.0330 -0.0010 66 ARG A NH2 478 N N . PHE A 69 ? 0.4477 0.4317 0.4086 0.1052 0.0498 0.0522 67 PHE A N 479 C CA . PHE A 69 ? 0.4207 0.3929 0.3946 0.0723 0.0501 0.0387 67 PHE A CA 480 C C . PHE A 69 ? 0.4614 0.3757 0.4135 0.0593 0.0712 0.0393 67 PHE A C 481 O O . PHE A 69 ? 0.4525 0.3623 0.4137 0.0317 0.0728 0.0277 67 PHE A O 482 C CB . PHE A 69 ? 0.3736 0.3799 0.3805 0.0594 0.0353 0.0248 67 PHE A CB 483 C CG . PHE A 69 ? 0.3346 0.3915 0.3608 0.0630 0.0178 0.0194 67 PHE A CG 484 C CD1 . PHE A 69 ? 0.2885 0.3593 0.3224 0.0493 0.0101 0.0110 67 PHE A CD1 485 C CD2 . PHE A 69 ? 0.3306 0.4224 0.3654 0.0790 0.0107 0.0211 67 PHE A CD2 486 C CE1 . PHE A 69 ? 0.2801 0.3879 0.3262 0.0481 -0.0028 0.0025 67 PHE A CE1 487 C CE2 . PHE A 69 ? 0.3042 0.4443 0.3555 0.0746 -0.0040 0.0117 67 PHE A CE2 488 C CZ . PHE A 69 ? 0.2795 0.4219 0.3339 0.0578 -0.0099 0.0017 67 PHE A CZ 489 N N . GLN A 70 ? 0.5181 0.3887 0.4386 0.0795 0.0886 0.0524 68 GLN A N 490 C CA . GLN A 70 ? 0.5796 0.3900 0.4770 0.0672 0.1103 0.0494 68 GLN A CA 491 C C . GLN A 70 ? 0.6060 0.3859 0.4914 0.0325 0.1241 0.0415 68 GLN A C 492 O O . GLN A 70 ? 0.6350 0.3893 0.5163 0.0061 0.1345 0.0284 68 GLN A O 493 C CB . GLN A 70 ? 0.6488 0.4077 0.5058 0.1017 0.1306 0.0674 68 GLN A CB 494 C CG . GLN A 70 ? 0.7223 0.4147 0.5534 0.0917 0.1540 0.0613 68 GLN A CG 495 C CD . GLN A 70 ? 0.8167 0.4395 0.5971 0.1271 0.1808 0.0803 68 GLN A CD 496 O OE1 . GLN A 70 ? 0.8699 0.4878 0.6285 0.1588 0.1847 0.1008 68 GLN A OE1 497 N NE2 . GLN A 70 ? 0.8708 0.4364 0.6278 0.1240 0.2011 0.0737 68 GLN A NE2 498 N N . ASN A 71 ? 0.6123 0.4005 0.4917 0.0311 0.1245 0.0480 69 ASN A N 499 C CA . ASN A 71 ? 0.6506 0.4186 0.5199 -0.0019 0.1393 0.0411 69 ASN A CA 500 C C . ASN A 71 ? 0.5730 0.4024 0.4783 -0.0226 0.1218 0.0284 69 ASN A C 501 O O . ASN A 71 ? 0.5911 0.4187 0.4938 -0.0501 0.1329 0.0214 69 ASN A O 502 C CB . ASN A 71 ? 0.7311 0.4479 0.5561 0.0100 0.1622 0.0594 69 ASN A CB 503 C CG . ASN A 71 ? 0.9021 0.5309 0.6812 0.0007 0.1957 0.0625 69 ASN A CG 504 O OD1 . ASN A 71 ? 0.9604 0.5558 0.7245 0.0212 0.2017 0.0666 69 ASN A OD1 505 N ND2 . ASN A 71 ? 1.0969 0.6848 0.8508 -0.0315 0.2207 0.0596 69 ASN A ND2 506 N N . ARG A 72 ? 0.4955 0.3776 0.4327 -0.0098 0.0970 0.0248 70 ARG A N 507 C CA . ARG A 72 ? 0.4398 0.3735 0.4050 -0.0192 0.0816 0.0159 70 ARG A CA 508 C C . ARG A 72 ? 0.3832 0.3499 0.3786 -0.0274 0.0661 0.0029 70 ARG A C 509 O O . ARG A 72 ? 0.3477 0.3516 0.3633 -0.0311 0.0550 -0.0037 70 ARG A O 510 C CB . ARG A 72 ? 0.4209 0.3818 0.3896 0.0053 0.0676 0.0231 70 ARG A CB 511 C CG . ARG A 72 ? 0.4791 0.4172 0.4163 0.0207 0.0792 0.0384 70 ARG A CG 512 C CD . ARG A 72 ? 0.4623 0.4383 0.4032 0.0382 0.0645 0.0406 70 ARG A CD 513 N NE . ARG A 72 ? 0.4614 0.4614 0.4107 0.0590 0.0491 0.0419 70 ARG A NE 514 C CZ . ARG A 72 ? 0.4421 0.4837 0.4160 0.0580 0.0304 0.0300 70 ARG A CZ 515 N NH1 . ARG A 72 ? 0.4109 0.4689 0.4010 0.0424 0.0246 0.0173 70 ARG A NH1 516 N NH2 . ARG A 72 ? 0.4554 0.5220 0.4358 0.0729 0.0194 0.0305 70 ARG A NH2 517 N N . SER A 73 ? 0.3863 0.3373 0.3815 -0.0265 0.0664 0.0007 71 SER A N 518 C CA . SER A 73 ? 0.3444 0.3248 0.3639 -0.0286 0.0515 -0.0080 71 SER A CA 519 C C . SER A 73 ? 0.3482 0.3182 0.3652 -0.0488 0.0585 -0.0181 71 SER A C 520 O O . SER A 73 ? 0.3893 0.3181 0.3833 -0.0562 0.0751 -0.0183 71 SER A O 521 C CB . SER A 73 ? 0.3257 0.3128 0.3518 -0.0075 0.0416 -0.0027 71 SER A CB 522 O OG . SER A 73 ? 0.3715 0.3297 0.3837 0.0002 0.0510 0.0012 71 SER A OG 523 N N . HIS A 74 ? 0.3160 0.3219 0.3523 -0.0572 0.0472 -0.0269 72 HIS A N 524 C CA . HIS A 74 ? 0.3267 0.3384 0.3612 -0.0793 0.0516 -0.0391 72 HIS A CA 525 C C . HIS A 74 ? 0.3019 0.3477 0.3532 -0.0734 0.0364 -0.0421 72 HIS A C 526 O O . HIS A 74 ? 0.2719 0.3447 0.3377 -0.0608 0.0250 -0.0381 72 HIS A O 527 C CB . HIS A 74 ? 0.3295 0.3644 0.3658 -0.1033 0.0582 -0.0480 72 HIS A CB 528 C CG . HIS A 74 ? 0.3538 0.3588 0.3735 -0.1085 0.0739 -0.0424 72 HIS A CG 529 N ND1 . HIS A 74 ? 0.4095 0.3669 0.4017 -0.1288 0.0961 -0.0460 72 HIS A ND1 530 C CD2 . HIS A 74 ? 0.3423 0.3550 0.3645 -0.0964 0.0727 -0.0333 72 HIS A CD2 531 C CE1 . HIS A 74 ? 0.4144 0.3500 0.3922 -0.1279 0.1085 -0.0371 72 HIS A CE1 532 N NE2 . HIS A 74 ? 0.4129 0.3854 0.4096 -0.1081 0.0935 -0.0295 72 HIS A NE2 533 N N . LEU A 75 ? 0.3237 0.3631 0.3679 -0.0824 0.0387 -0.0493 73 LEU A N 534 C CA . LEU A 75 ? 0.3136 0.3832 0.3670 -0.0779 0.0268 -0.0515 73 LEU A CA 535 C C . LEU A 75 ? 0.3077 0.4224 0.3672 -0.0940 0.0235 -0.0617 73 LEU A C 536 O O . LEU A 75 ? 0.3305 0.4458 0.3801 -0.1183 0.0319 -0.0748 73 LEU A O 537 C CB . LEU A 75 ? 0.3384 0.3839 0.3782 -0.0807 0.0322 -0.0556 73 LEU A CB 538 C CG . LEU A 75 ? 0.3531 0.4171 0.3965 -0.0711 0.0227 -0.0535 73 LEU A CG 539 C CD1 . LEU A 75 ? 0.3190 0.3803 0.3738 -0.0504 0.0162 -0.0406 73 LEU A CD1 540 C CD2 . LEU A 75 ? 0.3567 0.3969 0.3836 -0.0761 0.0311 -0.0596 73 LEU A CD2 541 N N . VAL A 76 ? 0.2921 0.4463 0.3667 -0.0804 0.0125 -0.0568 74 VAL A N 542 C CA . VAL A 76 ? 0.2877 0.5010 0.3723 -0.0903 0.0082 -0.0653 74 VAL A CA 543 C C . VAL A 76 ? 0.2912 0.5446 0.3778 -0.0765 -0.0041 -0.0638 74 VAL A C 544 O O . VAL A 76 ? 0.3011 0.6142 0.3952 -0.0805 -0.0098 -0.0705 74 VAL A O 545 C CB . VAL A 76 ? 0.2793 0.5150 0.3769 -0.0808 0.0074 -0.0604 74 VAL A CB 546 C CG1 . VAL A 76 ? 0.2855 0.4866 0.3763 -0.0969 0.0213 -0.0619 74 VAL A CG1 547 C CG2 . VAL A 76 ? 0.2451 0.4677 0.3457 -0.0488 -0.0003 -0.0465 74 VAL A CG2 548 N N . GLY A 77 ? 0.3074 0.5316 0.3861 -0.0596 -0.0074 -0.0544 75 GLY A N 549 C CA . GLY A 77 ? 0.3199 0.5732 0.3935 -0.0449 -0.0162 -0.0502 75 GLY A CA 550 C C . GLY A 77 ? 0.3330 0.6149 0.3981 -0.0660 -0.0169 -0.0646 75 GLY A C 551 O O . GLY A 77 ? 0.3625 0.6149 0.4197 -0.0902 -0.0074 -0.0761 75 GLY A O 552 N N . ASP A 78 ? 0.3307 0.6690 0.3940 -0.0550 -0.0272 -0.0641 76 ASP A N 553 C CA . ASP A 78 ? 0.3410 0.7133 0.3924 -0.0727 -0.0302 -0.0782 76 ASP A CA 554 C C . ASP A 78 ? 0.3424 0.6655 0.3738 -0.0685 -0.0262 -0.0735 76 ASP A C 555 O O . ASP A 78 ? 0.3379 0.6618 0.3591 -0.0428 -0.0313 -0.0585 76 ASP A O 556 C CB . ASP A 78 ? 0.3471 0.8007 0.4005 -0.0537 -0.0441 -0.0750 76 ASP A CB 557 C CG . ASP A 78 ? 0.3819 0.8921 0.4260 -0.0771 -0.0493 -0.0946 76 ASP A CG 558 O OD1 . ASP A 78 ? 0.4277 0.9021 0.4576 -0.1053 -0.0411 -0.1095 76 ASP A OD1 559 O OD2 . ASP A 78 ? 0.4367 1.0317 0.4864 -0.0660 -0.0614 -0.0960 76 ASP A OD2 560 N N . THR A 79 ? 0.3428 0.6216 0.3658 -0.0927 -0.0146 -0.0857 77 THR A N 561 C CA . THR A 79 ? 0.3521 0.5892 0.3573 -0.0898 -0.0085 -0.0836 77 THR A CA 562 C C . THR A 79 ? 0.3822 0.6550 0.3674 -0.0953 -0.0135 -0.0931 77 THR A C 563 O O . THR A 79 ? 0.3877 0.6276 0.3558 -0.0947 -0.0066 -0.0933 77 THR A O 564 C CB . THR A 79 ? 0.3658 0.5433 0.3641 -0.1078 0.0076 -0.0929 77 THR A CB 565 O OG1 . THR A 79 ? 0.3882 0.5745 0.3746 -0.1407 0.0147 -0.1165 77 THR A OG1 566 C CG2 . THR A 79 ? 0.3317 0.4772 0.3455 -0.0992 0.0118 -0.0822 77 THR A CG2 567 N N . PHE A 80 ? 0.3943 0.7393 0.3812 -0.0998 -0.0251 -0.1013 78 PHE A N 568 C CA . PHE A 80 ? 0.4265 0.8197 0.3936 -0.0957 -0.0340 -0.1054 78 PHE A CA 569 C C . PHE A 80 ? 0.4171 0.8502 0.3830 -0.0552 -0.0470 -0.0813 78 PHE A C 570 O O . PHE A 80 ? 0.4288 0.9051 0.3751 -0.0434 -0.0553 -0.0791 78 PHE A O 571 C CB . PHE A 80 ? 0.4592 0.9141 0.4230 -0.1313 -0.0375 -0.1349 78 PHE A CB 572 C CG . PHE A 80 ? 0.5243 0.9266 0.4815 -0.1711 -0.0200 -0.1581 78 PHE A CG 573 C CD1 . PHE A 80 ? 0.5817 0.9214 0.5144 -0.1783 -0.0069 -0.1642 78 PHE A CD1 574 C CD2 . PHE A 80 ? 0.5731 0.9797 0.5456 -0.1980 -0.0135 -0.1714 78 PHE A CD2 575 C CE1 . PHE A 80 ? 0.6185 0.8979 0.5385 -0.2087 0.0128 -0.1831 78 PHE A CE1 576 C CE2 . PHE A 80 ? 0.6141 0.9564 0.5725 -0.2317 0.0071 -0.1897 78 PHE A CE2 577 C CZ . PHE A 80 ? 0.6341 0.9096 0.5646 -0.2348 0.0206 -0.1949 78 PHE A CZ 578 N N . HIS A 81 ? 0.3921 0.8037 0.3736 -0.0320 -0.0466 -0.0625 79 HIS A N 579 C CA . HIS A 81 ? 0.3965 0.8290 0.3722 0.0090 -0.0539 -0.0386 79 HIS A CA 580 C C . HIS A 81 ? 0.3771 0.7345 0.3555 0.0265 -0.0440 -0.0194 79 HIS A C 581 O O . HIS A 81 ? 0.3568 0.7153 0.3456 0.0454 -0.0450 -0.0092 79 HIS A O 582 C CB . HIS A 81 ? 0.4041 0.9165 0.3972 0.0167 -0.0650 -0.0425 79 HIS A CB 583 C CG . HIS A 81 ? 0.4805 1.0277 0.4622 0.0647 -0.0726 -0.0186 79 HIS A CG 584 N ND1 . HIS A 81 ? 0.5832 1.0894 0.5348 0.0963 -0.0686 0.0047 79 HIS A ND1 585 C CD2 . HIS A 81 ? 0.5349 1.1536 0.5280 0.0890 -0.0816 -0.0137 79 HIS A CD2 586 C CE1 . HIS A 81 ? 0.6128 1.1551 0.5536 0.1399 -0.0739 0.0244 79 HIS A CE1 587 N NE2 . HIS A 81 ? 0.5820 1.1964 0.5490 0.1385 -0.0827 0.0137 79 HIS A NE2 588 N N . ASN A 82 ? 0.3672 0.6633 0.3362 0.0181 -0.0335 -0.0171 80 ASN A N 589 C CA . ASN A 82 ? 0.3640 0.5976 0.3294 0.0333 -0.0238 0.0007 80 ASN A CA 590 C C . ASN A 82 ? 0.3325 0.5365 0.3198 0.0305 -0.0202 0.0009 80 ASN A C 591 O O . ASN A 82 ? 0.3336 0.5004 0.3163 0.0460 -0.0143 0.0145 80 ASN A O 592 C CB . ASN A 82 ? 0.4015 0.6359 0.3431 0.0688 -0.0242 0.0235 80 ASN A CB 593 C CG . ASN A 82 ? 0.4286 0.7035 0.3445 0.0791 -0.0300 0.0267 80 ASN A CG 594 O OD1 . ASN A 82 ? 0.5015 0.8452 0.4195 0.0821 -0.0425 0.0190 80 ASN A OD1 595 N ND2 . ASN A 82 ? 0.4728 0.7106 0.3636 0.0843 -0.0206 0.0380 80 ASN A ND2 596 N N . ASP A 83 ? 0.3082 0.5264 0.3153 0.0097 -0.0220 -0.0148 81 ASP A N 597 C CA . ASP A 83 ? 0.2868 0.4943 0.3120 0.0109 -0.0212 -0.0144 81 ASP A CA 598 C C . ASP A 83 ? 0.2722 0.4492 0.3093 -0.0118 -0.0145 -0.0249 81 ASP A C 599 O O . ASP A 83 ? 0.2800 0.4700 0.3194 -0.0325 -0.0131 -0.0389 81 ASP A O 600 C CB . ASP A 83 ? 0.2890 0.5580 0.3239 0.0158 -0.0298 -0.0190 81 ASP A CB 601 C CG . ASP A 83 ? 0.2485 0.5133 0.3002 0.0190 -0.0282 -0.0186 81 ASP A CG 602 O OD1 . ASP A 83 ? 0.2298 0.4454 0.2837 0.0194 -0.0220 -0.0144 81 ASP A OD1 603 O OD2 . ASP A 83 ? 0.2664 0.5842 0.3298 0.0189 -0.0331 -0.0244 81 ASP A OD2 604 N N . GLY A 84 ? 0.2645 0.4008 0.3062 -0.0075 -0.0091 -0.0182 82 GLY A N 605 C CA . GLY A 84 ? 0.2547 0.3666 0.3061 -0.0204 -0.0035 -0.0242 82 GLY A CA 606 C C . GLY A 84 ? 0.2427 0.3497 0.3059 -0.0168 -0.0043 -0.0227 82 GLY A C 607 O O . GLY A 84 ? 0.2417 0.3258 0.3099 -0.0191 -0.0005 -0.0223 82 GLY A O 608 N N . SER A 85 ? 0.2341 0.3685 0.3011 -0.0098 -0.0091 -0.0222 83 SER A N 609 C CA . SER A 85 ? 0.2267 0.3585 0.3021 -0.0042 -0.0090 -0.0210 83 SER A CA 610 C C . SER A 85 ? 0.2232 0.3489 0.3049 -0.0197 -0.0046 -0.0277 83 SER A C 611 O O . SER A 85 ? 0.2194 0.3514 0.2991 -0.0357 -0.0010 -0.0350 83 SER A O 612 C CB . SER A 85 ? 0.2280 0.3971 0.3057 0.0099 -0.0134 -0.0189 83 SER A CB 613 O OG . SER A 85 ? 0.2205 0.3891 0.2855 0.0312 -0.0153 -0.0090 83 SER A OG 614 N N . LEU A 86 ? 0.2249 0.3341 0.3096 -0.0147 -0.0033 -0.0251 84 LEU A N 615 C CA . LEU A 86 ? 0.2276 0.3247 0.3125 -0.0227 0.0019 -0.0271 84 LEU A CA 616 C C . LEU A 86 ? 0.2207 0.3349 0.3095 -0.0207 0.0025 -0.0280 84 LEU A C 617 O O . LEU A 86 ? 0.1958 0.3179 0.2868 -0.0076 -0.0011 -0.0261 84 LEU A O 618 C CB . LEU A 86 ? 0.2384 0.3127 0.3225 -0.0164 0.0018 -0.0234 84 LEU A CB 619 C CG . LEU A 86 ? 0.2628 0.3271 0.3438 -0.0151 0.0051 -0.0215 84 LEU A CG 620 C CD1 . LEU A 86 ? 0.2769 0.3235 0.3492 -0.0191 0.0132 -0.0201 84 LEU A CD1 621 C CD2 . LEU A 86 ? 0.2768 0.3401 0.3612 -0.0079 0.0004 -0.0209 84 LEU A CD2 622 N N . LEU A 87 ? 0.2235 0.3389 0.3098 -0.0341 0.0098 -0.0310 85 LEU A N 623 C CA . LEU A 87 ? 0.2264 0.3527 0.3136 -0.0345 0.0138 -0.0309 85 LEU A CA 624 C C . LEU A 87 ? 0.2395 0.3339 0.3151 -0.0326 0.0195 -0.0256 85 LEU A C 625 O O . LEU A 87 ? 0.2550 0.3243 0.3194 -0.0405 0.0277 -0.0242 85 LEU A O 626 C CB . LEU A 87 ? 0.2398 0.3930 0.3299 -0.0541 0.0211 -0.0381 85 LEU A CB 627 C CG . LEU A 87 ? 0.2369 0.4070 0.3286 -0.0572 0.0280 -0.0382 85 LEU A CG 628 C CD1 . LEU A 87 ? 0.2033 0.4088 0.3071 -0.0371 0.0197 -0.0375 85 LEU A CD1 629 C CD2 . LEU A 87 ? 0.2491 0.4384 0.3405 -0.0870 0.0405 -0.0474 85 LEU A CD2 630 N N . LEU A 88 ? 0.2500 0.3450 0.3248 -0.0199 0.0158 -0.0228 86 LEU A N 631 C CA . LEU A 88 ? 0.2643 0.3416 0.3262 -0.0147 0.0199 -0.0170 86 LEU A CA 632 C C . LEU A 88 ? 0.2721 0.3608 0.3289 -0.0165 0.0262 -0.0167 86 LEU A C 633 O O . LEU A 88 ? 0.2612 0.3712 0.3253 -0.0105 0.0221 -0.0208 86 LEU A O 634 C CB . LEU A 88 ? 0.2692 0.3461 0.3322 -0.0020 0.0104 -0.0169 86 LEU A CB 635 C CG . LEU A 88 ? 0.2809 0.3541 0.3310 0.0077 0.0105 -0.0116 86 LEU A CG 636 C CD1 . LEU A 88 ? 0.3273 0.3789 0.3636 0.0110 0.0195 -0.0018 86 LEU A CD1 637 C CD2 . LEU A 88 ? 0.2862 0.3711 0.3421 0.0131 0.0001 -0.0168 86 LEU A CD2 638 N N . GLN A 89 ? 0.2940 0.3639 0.3346 -0.0232 0.0388 -0.0109 87 GLN A N 639 C CA . GLN A 89 ? 0.3175 0.3942 0.3494 -0.0281 0.0490 -0.0091 87 GLN A CA 640 C C . GLN A 89 ? 0.3458 0.4091 0.3578 -0.0121 0.0498 0.0001 87 GLN A C 641 O O . GLN A 89 ? 0.3445 0.3921 0.3473 0.0017 0.0446 0.0064 87 GLN A O 642 C CB . GLN A 89 ? 0.3547 0.4126 0.3750 -0.0507 0.0672 -0.0087 87 GLN A CB 643 C CG . GLN A 89 ? 0.3531 0.4314 0.3902 -0.0701 0.0664 -0.0201 87 GLN A CG 644 C CD . GLN A 89 ? 0.4150 0.4737 0.4376 -0.0993 0.0868 -0.0241 87 GLN A CD 645 O OE1 . GLN A 89 ? 0.4688 0.4765 0.4686 -0.1036 0.0982 -0.0200 87 GLN A OE1 646 N NE2 . GLN A 89 ? 0.4163 0.5152 0.4506 -0.1203 0.0935 -0.0331 87 GLN A NE2 647 N N . ASP A 90 ? 0.3503 0.4274 0.3558 -0.0125 0.0561 0.0005 88 ASP A N 648 C CA . ASP A 90 ? 0.3944 0.4633 0.3761 0.0016 0.0588 0.0094 88 ASP A CA 649 C C . ASP A 90 ? 0.3738 0.4510 0.3560 0.0199 0.0419 0.0078 88 ASP A C 650 O O . ASP A 90 ? 0.3967 0.4626 0.3612 0.0332 0.0412 0.0178 88 ASP A O 651 C CB . ASP A 90 ? 0.4526 0.4809 0.4055 -0.0004 0.0763 0.0239 88 ASP A CB 652 C CG . ASP A 90 ? 0.5518 0.5719 0.4738 0.0144 0.0836 0.0364 88 ASP A CG 653 O OD1 . ASP A 90 ? 0.5974 0.6416 0.5197 0.0123 0.0852 0.0321 88 ASP A OD1 654 O OD2 . ASP A 90 ? 0.6320 0.6223 0.5271 0.0312 0.0886 0.0514 88 ASP A OD2 655 N N . VAL A 91 ? 0.3340 0.4316 0.3349 0.0203 0.0298 -0.0048 89 VAL A N 656 C CA . VAL A 91 ? 0.3191 0.4260 0.3220 0.0289 0.0158 -0.0113 89 VAL A CA 657 C C . VAL A 91 ? 0.3457 0.4640 0.3265 0.0404 0.0136 -0.0088 89 VAL A C 658 O O . VAL A 91 ? 0.3636 0.4860 0.3306 0.0424 0.0206 -0.0078 89 VAL A O 659 C CB . VAL A 91 ? 0.3160 0.4305 0.3331 0.0258 0.0095 -0.0258 89 VAL A CB 660 C CG1 . VAL A 91 ? 0.3024 0.4238 0.3144 0.0280 -0.0008 -0.0373 89 VAL A CG1 661 C CG2 . VAL A 91 ? 0.2549 0.3624 0.2908 0.0190 0.0089 -0.0265 89 VAL A CG2 662 N N . GLN A 92 ? 0.3527 0.4822 0.3303 0.0487 0.0039 -0.0076 90 GLN A N 663 C CA A GLN A 92 ? 0.3761 0.5283 0.3326 0.0615 -0.0013 -0.0060 90 GLN A CA 664 C CA B GLN A 92 ? 0.3772 0.5292 0.3340 0.0622 -0.0015 -0.0050 90 GLN A CA 665 C C . GLN A 92 ? 0.3656 0.5469 0.3318 0.0559 -0.0163 -0.0243 90 GLN A C 666 O O . GLN A 92 ? 0.3377 0.5145 0.3245 0.0439 -0.0203 -0.0342 90 GLN A O 667 C CB A GLN A 92 ? 0.4074 0.5552 0.3447 0.0805 0.0029 0.0146 90 GLN A CB 668 C CB B GLN A 92 ? 0.3998 0.5474 0.3435 0.0797 0.0012 0.0140 90 GLN A CB 669 C CG A GLN A 92 ? 0.4309 0.5405 0.3456 0.0832 0.0232 0.0324 90 GLN A CG 670 C CG B GLN A 92 ? 0.4315 0.5384 0.3548 0.0826 0.0211 0.0321 90 GLN A CG 671 C CD A GLN A 92 ? 0.4456 0.5588 0.3437 0.0801 0.0305 0.0309 90 GLN A CD 672 C CD B GLN A 92 ? 0.4693 0.5491 0.3813 0.0960 0.0296 0.0489 90 GLN A CD 673 O OE1 A GLN A 92 ? 0.4748 0.6118 0.3531 0.0929 0.0248 0.0312 90 GLN A OE1 674 O OE1 B GLN A 92 ? 0.4753 0.5747 0.3792 0.1182 0.0223 0.0567 90 GLN A OE1 675 N NE2 A GLN A 92 ? 0.4347 0.5307 0.3409 0.0630 0.0436 0.0285 90 GLN A NE2 676 N NE2 B GLN A 92 ? 0.4993 0.5355 0.4087 0.0830 0.0464 0.0538 90 GLN A NE2 677 N N . LYS A 93 ? 0.3872 0.5980 0.3357 0.0620 -0.0231 -0.0302 91 LYS A N 678 C CA . LYS A 93 ? 0.3890 0.6296 0.3431 0.0498 -0.0355 -0.0527 91 LYS A CA 679 C C . LYS A 93 ? 0.3657 0.6307 0.3397 0.0472 -0.0444 -0.0535 91 LYS A C 680 O O . LYS A 93 ? 0.3470 0.6183 0.3360 0.0274 -0.0490 -0.0721 91 LYS A O 681 C CB . LYS A 93 ? 0.4276 0.7046 0.3562 0.0567 -0.0421 -0.0594 91 LYS A CB 682 C CG . LYS A 93 ? 0.4824 0.7565 0.4033 0.0385 -0.0426 -0.0863 91 LYS A CG 683 C CD . LYS A 93 ? 0.5178 0.8044 0.4539 0.0147 -0.0502 -0.1103 91 LYS A CD 684 C CE . LYS A 93 ? 0.5477 0.7862 0.4814 -0.0027 -0.0398 -0.1290 91 LYS A CE 685 N NZ . LYS A 93 ? 0.5720 0.8210 0.4930 -0.0273 -0.0429 -0.1607 91 LYS A NZ 686 N N . ALA A 94 ? 0.3612 0.6362 0.3326 0.0679 -0.0442 -0.0329 92 ALA A N 687 C CA . ALA A 94 ? 0.3429 0.6435 0.3334 0.0713 -0.0502 -0.0305 92 ALA A CA 688 C C . ALA A 94 ? 0.3178 0.5837 0.3318 0.0558 -0.0444 -0.0331 92 ALA A C 689 O O . ALA A 94 ? 0.3087 0.5951 0.3397 0.0557 -0.0479 -0.0333 92 ALA A O 690 C CB . ALA A 94 ? 0.3596 0.6668 0.3347 0.1039 -0.0468 -0.0049 92 ALA A CB 691 N N . ASP A 95 ? 0.3006 0.5202 0.3148 0.0455 -0.0352 -0.0339 93 ASP A N 692 C CA . ASP A 95 ? 0.2807 0.4705 0.3131 0.0327 -0.0302 -0.0360 93 ASP A CA 693 C C . ASP A 95 ? 0.2769 0.4630 0.3183 0.0119 -0.0328 -0.0557 93 ASP A C 694 O O . ASP A 95 ? 0.2631 0.4250 0.3159 0.0030 -0.0285 -0.0569 93 ASP A O 695 C CB . ASP A 95 ? 0.2792 0.4303 0.3072 0.0340 -0.0191 -0.0261 93 ASP A CB 696 C CG . ASP A 95 ? 0.3195 0.4579 0.3336 0.0489 -0.0108 -0.0072 93 ASP A CG 697 O OD1 . ASP A 95 ? 0.3620 0.5120 0.3729 0.0626 -0.0124 0.0014 93 ASP A OD1 698 O OD2 . ASP A 95 ? 0.3597 0.4749 0.3642 0.0471 -0.0003 -0.0010 93 ASP A OD2 699 N N . GLU A 96 ? 0.2850 0.4913 0.3167 0.0042 -0.0379 -0.0714 94 GLU A N 700 C CA . GLU A 96 ? 0.2867 0.4806 0.3182 -0.0182 -0.0365 -0.0928 94 GLU A CA 701 C C . GLU A 96 ? 0.2690 0.4838 0.3176 -0.0353 -0.0396 -0.1016 94 GLU A C 702 O O . GLU A 96 ? 0.2411 0.5091 0.2974 -0.0348 -0.0485 -0.1039 94 GLU A O 703 C CB . GLU A 96 ? 0.3171 0.5280 0.3291 -0.0244 -0.0398 -0.1102 94 GLU A CB 704 C CG . GLU A 96 ? 0.3533 0.5415 0.3566 -0.0505 -0.0345 -0.1357 94 GLU A CG 705 C CD . GLU A 96 ? 0.4070 0.5929 0.3838 -0.0542 -0.0331 -0.1530 94 GLU A CD 706 O OE1 . GLU A 96 ? 0.4051 0.5600 0.3690 -0.0394 -0.0255 -0.1468 94 GLU A OE1 707 O OE2 . GLU A 96 ? 0.4665 0.6856 0.4349 -0.0730 -0.0389 -0.1747 94 GLU A OE2 708 N N . GLY A 97 ? 0.2612 0.4376 0.3143 -0.0491 -0.0311 -0.1058 95 GLY A N 709 C CA . GLY A 97 ? 0.2675 0.4581 0.3351 -0.0684 -0.0302 -0.1135 95 GLY A CA 710 C C . GLY A 97 ? 0.2735 0.4174 0.3446 -0.0688 -0.0203 -0.1041 95 GLY A C 711 O O . GLY A 97 ? 0.2725 0.3708 0.3307 -0.0606 -0.0134 -0.0993 95 GLY A O 712 N N . ILE A 98 ? 0.2625 0.4228 0.3502 -0.0757 -0.0195 -0.1008 96 ILE A N 713 C CA . ILE A 98 ? 0.2764 0.3957 0.3642 -0.0802 -0.0093 -0.0942 96 ILE A CA 714 C C . ILE A 98 ? 0.2550 0.3818 0.3552 -0.0617 -0.0113 -0.0758 96 ILE A C 715 O O . ILE A 98 ? 0.2363 0.4044 0.3508 -0.0559 -0.0166 -0.0722 96 ILE A O 716 C CB . ILE A 98 ? 0.3030 0.4271 0.3951 -0.1101 -0.0016 -0.1084 96 ILE A CB 717 C CG1 . ILE A 98 ? 0.3535 0.4621 0.4279 -0.1346 0.0038 -0.1308 96 ILE A CG1 718 C CG2 . ILE A 98 ? 0.3141 0.3900 0.3995 -0.1132 0.0112 -0.0994 96 ILE A CG2 719 C CD1 . ILE A 98 ? 0.4275 0.5724 0.5117 -0.1688 0.0069 -0.1503 96 ILE A CD1 720 N N . TYR A 99 ? 0.2651 0.3530 0.3576 -0.0518 -0.0063 -0.0652 97 TYR A N 721 C CA . TYR A 99 ? 0.2528 0.3398 0.3517 -0.0389 -0.0062 -0.0513 97 TYR A CA 722 C C . TYR A 99 ? 0.2816 0.3456 0.3781 -0.0474 0.0019 -0.0493 97 TYR A C 723 O O . TYR A 99 ? 0.3085 0.3369 0.3900 -0.0503 0.0085 -0.0502 97 TYR A O 724 C CB . TYR A 99 ? 0.2473 0.3192 0.3384 -0.0242 -0.0073 -0.0434 97 TYR A CB 725 C CG . TYR A 99 ? 0.2306 0.3214 0.3201 -0.0161 -0.0124 -0.0432 97 TYR A CG 726 C CD1 . TYR A 99 ? 0.2445 0.3396 0.3262 -0.0192 -0.0146 -0.0526 97 TYR A CD1 727 C CD2 . TYR A 99 ? 0.2188 0.3183 0.3096 -0.0054 -0.0126 -0.0336 97 TYR A CD2 728 C CE1 . TYR A 99 ? 0.2362 0.3508 0.3126 -0.0100 -0.0189 -0.0509 97 TYR A CE1 729 C CE2 . TYR A 99 ? 0.2240 0.3344 0.3075 0.0038 -0.0144 -0.0303 97 TYR A CE2 730 C CZ . TYR A 99 ? 0.2432 0.3644 0.3201 0.0024 -0.0184 -0.0381 97 TYR A CZ 731 O OH . TYR A 99 ? 0.2347 0.3685 0.3007 0.0138 -0.0196 -0.0327 97 TYR A OH 732 N N . THR A 100 ? 0.2660 0.3486 0.3740 -0.0493 0.0033 -0.0459 98 THR A N 733 C CA . THR A 100 ? 0.2758 0.3389 0.3796 -0.0570 0.0122 -0.0426 98 THR A CA 734 C C . THR A 100 ? 0.2585 0.3188 0.3616 -0.0431 0.0117 -0.0319 98 THR A C 735 O O . THR A 100 ? 0.2412 0.3223 0.3529 -0.0349 0.0089 -0.0296 98 THR A O 736 C CB . THR A 100 ? 0.2857 0.3734 0.4013 -0.0761 0.0177 -0.0505 98 THR A CB 737 O OG1 . THR A 100 ? 0.2963 0.3917 0.4116 -0.0941 0.0178 -0.0649 98 THR A OG1 738 C CG2 . THR A 100 ? 0.2901 0.3479 0.3948 -0.0862 0.0306 -0.0461 98 THR A CG2 739 N N . CYS A 101 ? 0.2696 0.3026 0.3585 -0.0391 0.0152 -0.0257 99 CYS A N 740 C CA . CYS A 101 ? 0.2780 0.3109 0.3629 -0.0312 0.0154 -0.0189 99 CYS A CA 741 C C . CYS A 101 ? 0.2737 0.3011 0.3545 -0.0387 0.0243 -0.0164 99 CYS A C 742 O O . CYS A 101 ? 0.2889 0.2937 0.3581 -0.0459 0.0320 -0.0148 99 CYS A O 743 C CB . CYS A 101 ? 0.2920 0.3117 0.3633 -0.0210 0.0130 -0.0138 99 CYS A CB 744 S SG . CYS A 101 ? 0.3593 0.3895 0.4243 -0.0157 0.0115 -0.0101 99 CYS A SG 745 N N . GLU A 102 ? 0.2529 0.2963 0.3397 -0.0369 0.0259 -0.0160 100 GLU A N 746 C CA . GLU A 102 ? 0.2675 0.3079 0.3476 -0.0409 0.0349 -0.0126 100 GLU A CA 747 C C . GLU A 102 ? 0.2601 0.2971 0.3276 -0.0317 0.0330 -0.0098 100 GLU A C 748 O O . GLU A 102 ? 0.2521 0.2966 0.3234 -0.0268 0.0296 -0.0136 100 GLU A O 749 C CB . GLU A 102 ? 0.2667 0.3345 0.3637 -0.0463 0.0402 -0.0169 100 GLU A CB 750 C CG . GLU A 102 ? 0.3025 0.3859 0.4133 -0.0593 0.0404 -0.0235 100 GLU A CG 751 C CD . GLU A 102 ? 0.3922 0.5090 0.5187 -0.0719 0.0493 -0.0282 100 GLU A CD 752 O OE1 . GLU A 102 ? 0.4588 0.5878 0.5868 -0.0655 0.0557 -0.0250 100 GLU A OE1 753 O OE2 . GLU A 102 ? 0.4146 0.5478 0.5512 -0.0901 0.0508 -0.0369 100 GLU A OE2 754 N N . ILE A 103 ? 0.2621 0.2860 0.3109 -0.0299 0.0360 -0.0035 101 ILE A N 755 C CA . ILE A 103 ? 0.2544 0.2837 0.2893 -0.0233 0.0319 -0.0033 101 ILE A CA 756 C C . ILE A 103 ? 0.2710 0.2958 0.2870 -0.0229 0.0397 0.0023 101 ILE A C 757 O O . ILE A 103 ? 0.2867 0.2947 0.2915 -0.0230 0.0467 0.0111 101 ILE A O 758 C CB . ILE A 103 ? 0.2586 0.2907 0.2873 -0.0148 0.0225 -0.0007 101 ILE A CB 759 C CG1 . ILE A 103 ? 0.2424 0.2943 0.2589 -0.0120 0.0173 -0.0035 101 ILE A CG1 760 C CG2 . ILE A 103 ? 0.2498 0.2600 0.2661 -0.0076 0.0262 0.0096 101 ILE A CG2 761 C CD1 . ILE A 103 ? 0.2153 0.2892 0.2354 -0.0077 0.0074 -0.0065 101 ILE A CD1 762 N N . ARG A 104 ? 0.2707 0.3059 0.2799 -0.0236 0.0410 -0.0035 102 ARG A N 763 C CA . ARG A 104 ? 0.2860 0.3211 0.2732 -0.0222 0.0474 0.0005 102 ARG A CA 764 C C . ARG A 104 ? 0.3089 0.3608 0.2797 -0.0198 0.0393 -0.0058 102 ARG A C 765 O O . ARG A 104 ? 0.3038 0.3627 0.2806 -0.0262 0.0357 -0.0188 102 ARG A O 766 C CB . ARG A 104 ? 0.2874 0.3238 0.2794 -0.0274 0.0597 -0.0036 102 ARG A CB 767 C CG . ARG A 104 ? 0.2819 0.3159 0.2515 -0.0271 0.0697 0.0027 102 ARG A CG 768 C CD . ARG A 104 ? 0.2745 0.3158 0.2505 -0.0309 0.0835 -0.0021 102 ARG A CD 769 N NE . ARG A 104 ? 0.2946 0.3408 0.2754 -0.0274 0.0828 -0.0152 102 ARG A NE 770 C CZ . ARG A 104 ? 0.3382 0.3812 0.2970 -0.0267 0.0821 -0.0243 102 ARG A CZ 771 N NH1 . ARG A 104 ? 0.3829 0.4299 0.3158 -0.0274 0.0787 -0.0215 102 ARG A NH1 772 N NH2 . ARG A 104 ? 0.3429 0.3775 0.3024 -0.0250 0.0858 -0.0368 102 ARG A NH2 773 N N . LEU A 105 ? 0.3358 0.3942 0.2828 -0.0115 0.0379 0.0030 103 LEU A N 774 C CA . LEU A 105 ? 0.3460 0.4338 0.2764 -0.0097 0.0285 -0.0037 103 LEU A CA 775 C C . LEU A 105 ? 0.3691 0.4606 0.2809 -0.0166 0.0357 -0.0124 103 LEU A C 776 O O . LEU A 105 ? 0.3702 0.4437 0.2771 -0.0167 0.0483 -0.0072 103 LEU A O 777 C CB . LEU A 105 ? 0.3647 0.4660 0.2759 0.0094 0.0219 0.0120 103 LEU A CB 778 C CG . LEU A 105 ? 0.3285 0.4245 0.2512 0.0216 0.0164 0.0213 103 LEU A CG 779 C CD1 . LEU A 105 ? 0.3482 0.4578 0.2435 0.0482 0.0124 0.0387 103 LEU A CD1 780 C CD2 . LEU A 105 ? 0.2348 0.3540 0.1826 0.0113 0.0065 0.0060 103 LEU A CD2 781 N N . LYS A 106 ? 0.3942 0.5113 0.2960 -0.0250 0.0288 -0.0281 104 LYS A N 782 C CA . LYS A 106 ? 0.4355 0.5589 0.3129 -0.0328 0.0347 -0.0404 104 LYS A CA 783 C C . LYS A 106 ? 0.4686 0.5994 0.3189 -0.0188 0.0373 -0.0249 104 LYS A C 784 O O . LYS A 106 ? 0.4668 0.6165 0.3064 -0.0031 0.0285 -0.0099 104 LYS A O 785 C CB . LYS A 106 ? 0.4469 0.6029 0.3148 -0.0485 0.0254 -0.0621 104 LYS A CB 786 C CG . LYS A 106 ? 0.5157 0.6749 0.3540 -0.0608 0.0327 -0.0802 104 LYS A CG 787 C CD . LYS A 106 ? 0.5595 0.7307 0.3917 -0.0877 0.0311 -0.1094 104 LYS A CD 788 C CE . LYS A 106 ? 0.6402 0.8451 0.4374 -0.1008 0.0289 -0.1286 104 LYS A CE 789 N NZ . LYS A 106 ? 0.6804 0.9544 0.4769 -0.1135 0.0103 -0.1412 104 LYS A NZ 790 N N . ASN A 107 ? 0.5005 0.6131 0.3386 -0.0216 0.0519 -0.0265 105 ASN A N 791 C CA . ASN A 107 ? 0.5513 0.6655 0.3594 -0.0110 0.0591 -0.0125 105 ASN A CA 792 C C . ASN A 107 ? 0.5389 0.6283 0.3496 0.0011 0.0666 0.0132 105 ASN A C 793 O O . ASN A 107 ? 0.5604 0.6467 0.3408 0.0133 0.0721 0.0301 105 ASN A O 794 C CB . ASN A 107 ? 0.5980 0.7544 0.3746 -0.0046 0.0458 -0.0150 105 ASN A CB 795 C CG . ASN A 107 ? 0.7219 0.8841 0.4607 -0.0015 0.0551 -0.0140 105 ASN A CG 796 O OD1 . ASN A 107 ? 0.8088 0.9560 0.5443 -0.0137 0.0678 -0.0288 105 ASN A OD1 797 N ND2 . ASN A 107 ? 0.8893 1.0734 0.5956 0.0183 0.0497 0.0046 105 ASN A ND2 798 N N . GLU A 108 ? 0.5005 0.5692 0.3433 -0.0035 0.0687 0.0154 106 GLU A N 799 C CA . GLU A 108 ? 0.5024 0.5415 0.3477 0.0001 0.0793 0.0343 106 GLU A CA 800 C C . GLU A 108 ? 0.4706 0.4981 0.3451 -0.0145 0.0919 0.0278 106 GLU A C 801 O O . GLU A 108 ? 0.4179 0.4559 0.3158 -0.0206 0.0882 0.0123 106 GLU A O 802 C CB . GLU A 108 ? 0.5032 0.5345 0.3578 0.0092 0.0691 0.0427 106 GLU A CB 803 C CG . GLU A 108 ? 0.5338 0.5859 0.3610 0.0300 0.0569 0.0523 106 GLU A CG 804 C CD . GLU A 108 ? 0.5529 0.5862 0.3784 0.0465 0.0543 0.0675 106 GLU A CD 805 O OE1 . GLU A 108 ? 0.5349 0.5419 0.3843 0.0370 0.0587 0.0654 106 GLU A OE1 806 O OE2 . GLU A 108 ? 0.5724 0.6195 0.3704 0.0712 0.0482 0.0814 106 GLU A OE2 807 N N . SER A 109 ? 0.4854 0.4925 0.3553 -0.0197 0.1083 0.0401 107 SER A N 808 C CA . SER A 109 ? 0.4693 0.4785 0.3692 -0.0348 0.1203 0.0342 107 SER A CA 809 C C . SER A 109 ? 0.4520 0.4468 0.3739 -0.0429 0.1187 0.0365 107 SER A C 810 O O . SER A 109 ? 0.4250 0.4358 0.3787 -0.0535 0.1207 0.0271 107 SER A O 811 C CB . SER A 109 ? 0.4986 0.5034 0.3828 -0.0428 0.1423 0.0417 107 SER A CB 812 O OG . SER A 109 ? 0.5216 0.5475 0.3972 -0.0381 0.1454 0.0326 107 SER A OG 813 N N . MET A 110 ? 0.4760 0.4426 0.3782 -0.0357 0.1157 0.0487 108 MET A N 814 C CA . MET A 110 ? 0.4766 0.4202 0.3913 -0.0441 0.1174 0.0500 108 MET A CA 815 C C . MET A 110 ? 0.4135 0.3768 0.3573 -0.0404 0.0986 0.0379 108 MET A C 816 O O . MET A 110 ? 0.4042 0.3854 0.3470 -0.0274 0.0838 0.0341 108 MET A O 817 C CB . MET A 110 ? 0.5335 0.4321 0.4108 -0.0319 0.1233 0.0680 108 MET A CB 818 C CG . MET A 110 ? 0.6407 0.4991 0.4863 -0.0412 0.1487 0.0820 108 MET A CG 819 S SD . MET A 110 ? 0.7860 0.5773 0.5763 -0.0173 0.1590 0.1074 108 MET A SD 820 C CE . MET A 110 ? 0.7324 0.5321 0.5483 -0.0058 0.1374 0.0975 108 MET A CE 821 N N . VAL A 111 ? 0.3834 0.3465 0.3520 -0.0545 0.1002 0.0306 109 VAL A N 822 C CA . VAL A 111 ? 0.3419 0.3203 0.3353 -0.0514 0.0847 0.0209 109 VAL A CA 823 C C . VAL A 111 ? 0.3727 0.3195 0.3588 -0.0530 0.0852 0.0243 109 VAL A C 824 O O . VAL A 111 ? 0.3975 0.3189 0.3766 -0.0691 0.0999 0.0255 109 VAL A O 825 C CB . VAL A 111 ? 0.3179 0.3307 0.3449 -0.0621 0.0846 0.0084 109 VAL A CB 826 C CG1 . VAL A 111 ? 0.2517 0.2762 0.2993 -0.0589 0.0712 0.0008 109 VAL A CG1 827 C CG2 . VAL A 111 ? 0.2855 0.3226 0.3150 -0.0547 0.0864 0.0048 109 VAL A CG2 828 N N . MET A 112 ? 0.3623 0.3082 0.3462 -0.0373 0.0718 0.0253 110 MET A N 829 C CA . MET A 112 ? 0.3979 0.3168 0.3765 -0.0350 0.0716 0.0262 110 MET A CA 830 C C . MET A 112 ? 0.3471 0.2878 0.3566 -0.0466 0.0637 0.0117 110 MET A C 831 O O . MET A 112 ? 0.3063 0.2811 0.3365 -0.0431 0.0523 0.0052 110 MET A O 832 C CB . MET A 112 ? 0.4239 0.3425 0.3876 -0.0096 0.0609 0.0341 110 MET A CB 833 C CG . MET A 112 ? 0.5229 0.4076 0.4735 0.0002 0.0639 0.0376 110 MET A CG 834 S SD . MET A 112 ? 0.6886 0.5984 0.6329 0.0326 0.0487 0.0443 110 MET A SD 835 C CE . MET A 112 ? 0.6136 0.5693 0.5977 0.0212 0.0323 0.0269 110 MET A CE 836 N N . LYS A 113 ? 0.3566 0.2748 0.3647 -0.0607 0.0715 0.0066 111 LYS A N 837 C CA . LYS A 113 ? 0.3310 0.2727 0.3641 -0.0722 0.0643 -0.0077 111 LYS A CA 838 C C . LYS A 113 ? 0.3657 0.2729 0.3837 -0.0691 0.0654 -0.0097 111 LYS A C 839 O O . LYS A 113 ? 0.4012 0.2613 0.3942 -0.0771 0.0808 -0.0078 111 LYS A O 840 C CB . LYS A 113 ? 0.3308 0.2933 0.3804 -0.0994 0.0735 -0.0183 111 LYS A CB 841 C CG . LYS A 113 ? 0.2972 0.2904 0.3580 -0.1000 0.0767 -0.0153 111 LYS A CG 842 C CD . LYS A 113 ? 0.3160 0.3428 0.3965 -0.1254 0.0865 -0.0258 111 LYS A CD 843 C CE . LYS A 113 ? 0.3235 0.3807 0.4129 -0.1188 0.0904 -0.0212 111 LYS A CE 844 N NZ . LYS A 113 ? 0.3357 0.4443 0.4510 -0.1378 0.0982 -0.0312 111 LYS A NZ 845 N N . LYS A 114 ? 0.3634 0.2906 0.3937 -0.0574 0.0515 -0.0136 112 LYS A N 846 C CA . LYS A 114 ? 0.4025 0.3030 0.4185 -0.0470 0.0511 -0.0143 112 LYS A CA 847 C C . LYS A 114 ? 0.3744 0.3008 0.4094 -0.0550 0.0421 -0.0280 112 LYS A C 848 O O . LYS A 114 ? 0.3293 0.2908 0.3817 -0.0458 0.0295 -0.0280 112 LYS A O 849 C CB . LYS A 114 ? 0.3893 0.2968 0.3987 -0.0193 0.0427 -0.0030 112 LYS A CB 850 C CG . LYS A 114 ? 0.5018 0.3761 0.4894 -0.0022 0.0473 0.0003 112 LYS A CG 851 C CD . LYS A 114 ? 0.5196 0.4235 0.5114 0.0231 0.0359 0.0063 112 LYS A CD 852 C CE . LYS A 114 ? 0.5881 0.4634 0.5603 0.0422 0.0421 0.0082 112 LYS A CE 853 N NZ . LYS A 114 ? 0.5847 0.5029 0.5722 0.0579 0.0304 0.0070 112 LYS A NZ 854 N N . PRO A 115 ? 0.4026 0.3106 0.4309 -0.0739 0.0498 -0.0404 113 PRO A N 855 C CA . PRO A 115 ? 0.3932 0.3282 0.4345 -0.0781 0.0401 -0.0530 113 PRO A CA 856 C C . PRO A 115 ? 0.4052 0.3159 0.4305 -0.0601 0.0388 -0.0523 113 PRO A C 857 O O . PRO A 115 ? 0.4506 0.3113 0.4489 -0.0515 0.0507 -0.0475 113 PRO A O 858 C CB . PRO A 115 ? 0.4204 0.3530 0.4604 -0.1100 0.0491 -0.0703 113 PRO A CB 859 C CG . PRO A 115 ? 0.4871 0.3580 0.4982 -0.1189 0.0692 -0.0662 113 PRO A CG 860 C CD . PRO A 115 ? 0.4642 0.3271 0.4708 -0.0955 0.0689 -0.0453 113 PRO A CD 861 N N . VAL A 116 ? 0.3661 0.3119 0.4059 -0.0518 0.0261 -0.0554 114 VAL A N 862 C CA . VAL A 116 ? 0.3700 0.3056 0.3993 -0.0357 0.0244 -0.0561 114 VAL A CA 863 C C . VAL A 116 ? 0.3673 0.3271 0.4023 -0.0473 0.0185 -0.0710 114 VAL A C 864 O O . VAL A 116 ? 0.3274 0.3308 0.3816 -0.0511 0.0084 -0.0718 114 VAL A O 865 C CB . VAL A 116 ? 0.3327 0.2953 0.3732 -0.0142 0.0154 -0.0439 114 VAL A CB 866 C CG1 . VAL A 116 ? 0.3242 0.2814 0.3551 0.0016 0.0161 -0.0447 114 VAL A CG1 867 C CG2 . VAL A 116 ? 0.3371 0.2943 0.3754 -0.0044 0.0173 -0.0309 114 VAL A CG2 868 N N . GLU A 117 ? 0.3983 0.3295 0.4132 -0.0504 0.0254 -0.0825 115 GLU A N 869 C CA . GLU A 117 ? 0.4043 0.3616 0.4204 -0.0601 0.0190 -0.0975 115 GLU A CA 870 C C . GLU A 117 ? 0.3797 0.3490 0.3940 -0.0379 0.0137 -0.0924 115 GLU A C 871 O O . GLU A 117 ? 0.4031 0.3414 0.4022 -0.0209 0.0215 -0.0881 115 GLU A O 872 C CB . GLU A 117 ? 0.4599 0.3797 0.4516 -0.0810 0.0311 -0.1177 115 GLU A CB 873 C CG . GLU A 117 ? 0.5210 0.4291 0.5120 -0.1109 0.0398 -0.1270 115 GLU A CG 874 C CD . GLU A 117 ? 0.6338 0.4991 0.5956 -0.1377 0.0548 -0.1512 115 GLU A CD 875 O OE1 . GLU A 117 ? 0.6762 0.5196 0.6174 -0.1285 0.0575 -0.1597 115 GLU A OE1 876 O OE2 . GLU A 117 ? 0.6891 0.5407 0.6464 -0.1697 0.0657 -0.1631 115 GLU A OE2 877 N N . LEU A 118 ? 0.3319 0.3467 0.3593 -0.0369 0.0023 -0.0923 116 LEU A N 878 C CA . LEU A 118 ? 0.3229 0.3524 0.3475 -0.0204 -0.0010 -0.0878 116 LEU A CA 879 C C . LEU A 118 ? 0.3400 0.3842 0.3516 -0.0279 -0.0037 -0.1035 116 LEU A C 880 O O . LEU A 118 ? 0.3097 0.3888 0.3276 -0.0388 -0.0119 -0.1095 116 LEU A O 881 C CB . LEU A 118 ? 0.2869 0.3488 0.3286 -0.0112 -0.0084 -0.0726 116 LEU A CB 882 C CG . LEU A 118 ? 0.2930 0.3643 0.3309 0.0031 -0.0074 -0.0652 116 LEU A CG 883 C CD1 . LEU A 118 ? 0.2737 0.3277 0.3103 0.0144 -0.0002 -0.0605 116 LEU A CD1 884 C CD2 . LEU A 118 ? 0.2673 0.3601 0.3140 0.0070 -0.0110 -0.0527 116 LEU A CD2 885 N N . TRP A 119 ? 0.3728 0.3947 0.3651 -0.0197 0.0034 -0.1101 117 TRP A N 886 C CA . TRP A 119 ? 0.4019 0.4348 0.3765 -0.0250 0.0022 -0.1263 117 TRP A CA 887 C C . TRP A 119 ? 0.3658 0.4205 0.3399 -0.0052 0.0004 -0.1151 117 TRP A C 888 O O . TRP A 119 ? 0.3393 0.3817 0.3171 0.0106 0.0067 -0.1037 117 TRP A O 889 C CB . TRP A 119 ? 0.4895 0.4709 0.4363 -0.0305 0.0163 -0.1439 117 TRP A CB 890 C CG . TRP A 119 ? 0.5495 0.5003 0.4925 -0.0521 0.0228 -0.1535 117 TRP A CG 891 C CD1 . TRP A 119 ? 0.6034 0.5140 0.5466 -0.0475 0.0322 -0.1429 117 TRP A CD1 892 C CD2 . TRP A 119 ? 0.6168 0.5811 0.5560 -0.0846 0.0207 -0.1752 117 TRP A CD2 893 N NE1 . TRP A 119 ? 0.6453 0.5343 0.5821 -0.0761 0.0387 -0.1561 117 TRP A NE1 894 C CE2 . TRP A 119 ? 0.6290 0.5531 0.5653 -0.1016 0.0319 -0.1776 117 TRP A CE2 895 C CE3 . TRP A 119 ? 0.6301 0.6421 0.5668 -0.1016 0.0106 -0.1936 117 TRP A CE3 896 C CZ2 . TRP A 119 ? 0.6511 0.5813 0.5850 -0.1393 0.0349 -0.1990 117 TRP A CZ2 897 C CZ3 . TRP A 119 ? 0.6520 0.6778 0.5875 -0.1378 0.0110 -0.2164 117 TRP A CZ3 898 C CH2 . TRP A 119 ? 0.6692 0.6541 0.6046 -0.1585 0.0239 -0.2197 117 TRP A CH2 899 N N . VAL A 120 ? 0.3424 0.4324 0.3104 -0.0063 -0.0072 -0.1184 118 VAL A N 900 C CA . VAL A 120 ? 0.3279 0.4377 0.2926 0.0104 -0.0069 -0.1051 118 VAL A CA 901 C C . VAL A 120 ? 0.3600 0.4735 0.2987 0.0118 -0.0039 -0.1198 118 VAL A C 902 O O . VAL A 120 ? 0.3965 0.5276 0.3225 -0.0002 -0.0105 -0.1358 118 VAL A O 903 C CB . VAL A 120 ? 0.3003 0.4435 0.2750 0.0155 -0.0154 -0.0882 118 VAL A CB 904 C CG1 . VAL A 120 ? 0.2961 0.4474 0.2609 0.0297 -0.0099 -0.0737 118 VAL A CG1 905 C CG2 . VAL A 120 ? 0.2490 0.3840 0.2459 0.0138 -0.0161 -0.0762 118 VAL A CG2 906 N N . LEU A 121 ? 0.3674 0.4673 0.2981 0.0255 0.0068 -0.1169 119 LEU A N 907 C CA . LEU A 121 ? 0.4020 0.5037 0.3061 0.0307 0.0126 -0.1294 119 LEU A CA 908 C C . LEU A 121 ? 0.3921 0.5282 0.2922 0.0407 0.0112 -0.1139 119 LEU A C 909 O O . LEU A 121 ? 0.3508 0.4971 0.2677 0.0442 0.0098 -0.0940 119 LEU A O 910 C CB . LEU A 121 ? 0.4233 0.4943 0.3215 0.0446 0.0277 -0.1326 119 LEU A CB 911 C CG . LEU A 121 ? 0.4599 0.4826 0.3511 0.0414 0.0351 -0.1451 119 LEU A CG 912 C CD1 . LEU A 121 ? 0.4652 0.4671 0.3551 0.0658 0.0494 -0.1389 119 LEU A CD1 913 C CD2 . LEU A 121 ? 0.5465 0.5472 0.4066 0.0250 0.0378 -0.1726 119 LEU A CD2 914 N N . PRO A 122 ? 0.4459 0.5953 0.3188 0.0443 0.0133 -0.1233 120 PRO A N 915 C CA . PRO A 122 ? 0.4577 0.6331 0.3202 0.0553 0.0158 -0.1064 120 PRO A CA 916 C C . PRO A 122 ? 0.4577 0.6280 0.3357 0.0635 0.0289 -0.0885 120 PRO A C 917 O O . PRO A 122 ? 0.4525 0.6082 0.3434 0.0666 0.0367 -0.0932 120 PRO A O 918 C CB . PRO A 122 ? 0.4947 0.6781 0.3234 0.0582 0.0196 -0.1236 120 PRO A CB 919 C CG . PRO A 122 ? 0.5190 0.6889 0.3387 0.0434 0.0139 -0.1512 120 PRO A CG 920 C CD . PRO A 122 ? 0.4891 0.6271 0.3351 0.0365 0.0150 -0.1510 120 PRO A CD 921 N N . GLU A 123 ? 0.4770 0.6602 0.3520 0.0668 0.0324 -0.0682 121 GLU A N 922 C CA . GLU A 123 ? 0.4863 0.6698 0.3741 0.0671 0.0469 -0.0533 121 GLU A CA 923 C C . GLU A 123 ? 0.5027 0.6957 0.3846 0.0739 0.0605 -0.0620 121 GLU A C 924 O O . GLU A 123 ? 0.5378 0.7356 0.3938 0.0804 0.0622 -0.0726 121 GLU A O 925 C CB . GLU A 123 ? 0.5103 0.6960 0.3812 0.0681 0.0530 -0.0322 121 GLU A CB 926 C CG . GLU A 123 ? 0.5543 0.7379 0.4338 0.0605 0.0711 -0.0185 121 GLU A CG 927 C CD . GLU A 123 ? 0.6266 0.7908 0.4905 0.0580 0.0784 0.0035 121 GLU A CD 928 O OE1 . GLU A 123 ? 0.6865 0.8480 0.5207 0.0707 0.0741 0.0120 121 GLU A OE1 929 O OE2 . GLU A 123 ? 0.6489 0.8001 0.5273 0.0441 0.0891 0.0114 121 GLU A OE2 930 N N . GLU A 124 ? 0.4991 0.7004 0.4046 0.0734 0.0703 -0.0586 122 GLU A N 931 C CA . GLU A 124 ? 0.5239 0.7454 0.4269 0.0831 0.0853 -0.0642 122 GLU A CA 932 C C . GLU A 124 ? 0.5341 0.7725 0.4170 0.0803 0.0990 -0.0538 122 GLU A C 933 O O . GLU A 124 ? 0.5240 0.7582 0.4035 0.0691 0.1021 -0.0377 122 GLU A O 934 C CB . GLU A 124 ? 0.5170 0.7597 0.4534 0.0839 0.0916 -0.0616 122 GLU A CB 935 C CG . GLU A 124 ? 0.5544 0.7820 0.5044 0.0952 0.0838 -0.0709 122 GLU A CG 936 C CD . GLU A 124 ? 0.5891 0.8498 0.5715 0.0983 0.0880 -0.0654 122 GLU A CD 937 O OE1 . GLU A 124 ? 0.6049 0.9031 0.5940 0.1103 0.1006 -0.0671 122 GLU A OE1 938 O OE2 . GLU A 124 ? 0.6147 0.8700 0.6157 0.0890 0.0787 -0.0600 122 GLU A OE2 939 N N . PRO A 125 ? 0.4553 0.6278 0.3709 -0.0549 -0.0877 -0.0488 123 PRO A N 940 C CA . PRO A 125 ? 0.4569 0.6326 0.3640 -0.0456 -0.0954 -0.0311 123 PRO A CA 941 C C . PRO A 125 ? 0.4406 0.5767 0.3611 -0.0220 -0.0929 -0.0177 123 PRO A C 942 O O . PRO A 125 ? 0.4307 0.5295 0.3550 -0.0187 -0.0812 -0.0262 123 PRO A O 943 C CB . PRO A 125 ? 0.4810 0.6440 0.3536 -0.0684 -0.0845 -0.0452 123 PRO A CB 944 C CG . PRO A 125 ? 0.4896 0.6586 0.3520 -0.0931 -0.0756 -0.0691 123 PRO A CG 945 C CD . PRO A 125 ? 0.4794 0.6372 0.3680 -0.0828 -0.0731 -0.0716 123 PRO A CD 946 N N . ARG A 126 ? 0.4485 0.5958 0.3761 -0.0065 -0.1038 0.0044 124 ARG A N 947 C CA . ARG A 126 ? 0.4377 0.5489 0.3744 0.0112 -0.1013 0.0174 124 ARG A CA 948 C C . ARG A 126 ? 0.4288 0.5098 0.3444 0.0022 -0.0904 0.0134 124 ARG A C 949 O O . ARG A 126 ? 0.4132 0.4609 0.3359 0.0090 -0.0826 0.0127 124 ARG A O 950 C CB . ARG A 126 ? 0.4697 0.5984 0.4154 0.0279 -0.1135 0.0439 124 ARG A CB 951 C CG . ARG A 126 ? 0.5101 0.5968 0.4669 0.0445 -0.1092 0.0563 124 ARG A CG 952 C CD . ARG A 126 ? 0.5844 0.6806 0.5522 0.0641 -0.1181 0.0840 124 ARG A CD 953 N NE . ARG A 126 ? 0.6238 0.6768 0.6094 0.0799 -0.1111 0.0882 124 ARG A NE 954 C CZ . ARG A 126 ? 0.6817 0.7020 0.6648 0.0872 -0.1075 0.1057 124 ARG A CZ 955 N NH1 . ARG A 126 ? 0.7017 0.7292 0.6660 0.0829 -0.1112 0.1250 124 ARG A NH1 956 N NH2 . ARG A 126 ? 0.6957 0.6752 0.6940 0.0972 -0.0990 0.1033 124 ARG A NH2 957 N N . ASP A 127 ? 0.4362 0.5329 0.3261 -0.0143 -0.0890 0.0095 125 ASP A N 958 C CA . ASP A 127 ? 0.4461 0.5198 0.3155 -0.0216 -0.0773 0.0070 125 ASP A CA 959 C C . ASP A 127 ? 0.4335 0.4843 0.2922 -0.0332 -0.0597 -0.0165 125 ASP A C 960 O O . ASP A 127 ? 0.4549 0.5153 0.3052 -0.0471 -0.0562 -0.0330 125 ASP A O 961 C CB . ASP A 127 ? 0.4672 0.5675 0.3105 -0.0332 -0.0819 0.0151 125 ASP A CB 962 C CG . ASP A 127 ? 0.5231 0.6379 0.3724 -0.0194 -0.0957 0.0450 125 ASP A CG 963 O OD1 . ASP A 127 ? 0.5343 0.6448 0.4087 -0.0011 -0.1034 0.0586 125 ASP A OD1 964 O OD2 . ASP A 127 ? 0.5943 0.7242 0.4207 -0.0272 -0.0973 0.0555 125 ASP A OD2 965 N N . LEU A 128 ? 0.4212 0.4431 0.2798 -0.0280 -0.0475 -0.0166 126 LEU A N 966 C CA . LEU A 128 ? 0.4198 0.4172 0.2687 -0.0335 -0.0280 -0.0333 126 LEU A CA 967 C C . LEU A 128 ? 0.4303 0.4221 0.2608 -0.0373 -0.0173 -0.0317 126 LEU A C 968 O O . LEU A 128 ? 0.4237 0.4134 0.2623 -0.0283 -0.0196 -0.0169 126 LEU A O 969 C CB . LEU A 128 ? 0.3950 0.3705 0.2662 -0.0194 -0.0226 -0.0323 126 LEU A CB 970 C CG . LEU A 128 ? 0.4078 0.3575 0.2750 -0.0175 -0.0019 -0.0423 126 LEU A CG 971 C CD1 . LEU A 128 ? 0.4094 0.3474 0.2611 -0.0307 0.0102 -0.0611 126 LEU A CD1 972 C CD2 . LEU A 128 ? 0.3898 0.3318 0.2806 -0.0027 -0.0027 -0.0349 126 LEU A CD2 973 N N . ARG A 129 ? 0.4535 0.4431 0.2582 -0.0527 -0.0044 -0.0482 127 ARG A N 974 C CA . ARG A 129 ? 0.4964 0.4836 0.2789 -0.0590 0.0086 -0.0507 127 ARG A CA 975 C C . ARG A 129 ? 0.4943 0.4491 0.2789 -0.0507 0.0335 -0.0603 127 ARG A C 976 O O . ARG A 129 ? 0.5085 0.4406 0.2906 -0.0528 0.0472 -0.0757 127 ARG A O 977 C CB . ARG A 129 ? 0.5391 0.5450 0.2890 -0.0827 0.0099 -0.0658 127 ARG A CB 978 C CG . ARG A 129 ? 0.6261 0.6490 0.3504 -0.0917 0.0126 -0.0612 127 ARG A CG 979 C CD . ARG A 129 ? 0.7229 0.7809 0.4160 -0.1169 0.0050 -0.0713 127 ARG A CD 980 N NE . ARG A 129 ? 0.7613 0.8592 0.4659 -0.1138 -0.0229 -0.0498 127 ARG A NE 981 C CZ . ARG A 129 ? 0.8122 0.9516 0.5032 -0.1310 -0.0364 -0.0539 127 ARG A CZ 982 N NH1 . ARG A 129 ? 0.8471 0.9935 0.5092 -0.1584 -0.0253 -0.0821 127 ARG A NH1 983 N NH2 . ARG A 129 ? 0.8239 1.0001 0.5309 -0.1211 -0.0605 -0.0293 127 ARG A NH2 984 N N . VAL A 130 ? 0.4849 0.4395 0.2755 -0.0407 0.0396 -0.0488 128 VAL A N 985 C CA A VAL A 130 ? 0.4829 0.4170 0.2815 -0.0279 0.0620 -0.0522 128 VAL A CA 986 C CA B VAL A 130 ? 0.4814 0.4155 0.2800 -0.0278 0.0621 -0.0521 128 VAL A CA 987 C C . VAL A 130 ? 0.5036 0.4462 0.2875 -0.0305 0.0750 -0.0507 128 VAL A C 988 O O . VAL A 130 ? 0.5060 0.4709 0.2844 -0.0368 0.0626 -0.0382 128 VAL A O 989 C CB A VAL A 130 ? 0.4445 0.3788 0.2773 -0.0093 0.0549 -0.0368 128 VAL A CB 990 C CB B VAL A 130 ? 0.4433 0.3781 0.2760 -0.0089 0.0557 -0.0364 128 VAL A CB 991 C CG1 A VAL A 130 ? 0.4241 0.3795 0.2686 -0.0072 0.0419 -0.0183 128 VAL A CG1 992 C CG1 B VAL A 130 ? 0.4079 0.3345 0.2542 -0.0058 0.0456 -0.0385 128 VAL A CG1 993 C CG2 A VAL A 130 ? 0.4427 0.3601 0.2866 0.0065 0.0768 -0.0389 128 VAL A CG2 994 C CG2 B VAL A 130 ? 0.4215 0.3779 0.2653 -0.0083 0.0397 -0.0179 128 VAL A CG2 995 N N . ARG A 131 ? 0.5281 0.4519 0.3050 -0.0251 0.1020 -0.0628 129 ARG A N 996 C CA . ARG A 131 ? 0.5511 0.4841 0.3160 -0.0255 0.1185 -0.0630 129 ARG A CA 997 C C . ARG A 131 ? 0.5143 0.4595 0.3108 -0.0055 0.1218 -0.0448 129 ARG A C 998 O O . ARG A 131 ? 0.4735 0.4116 0.2956 0.0103 0.1210 -0.0386 129 ARG A O 999 C CB . ARG A 131 ? 0.6006 0.5065 0.3419 -0.0288 0.1495 -0.0869 129 ARG A CB 1000 C CG . ARG A 131 ? 0.6976 0.6045 0.3990 -0.0559 0.1502 -0.1069 129 ARG A CG 1001 C CD . ARG A 131 ? 0.7659 0.6610 0.4600 -0.0698 0.1391 -0.1193 129 ARG A CD 1002 N NE . ARG A 131 ? 0.8552 0.7649 0.5101 -0.0998 0.1369 -0.1376 129 ARG A NE 1003 C CZ . ARG A 131 ? 0.8941 0.8205 0.5398 -0.1184 0.1175 -0.1428 129 ARG A CZ 1004 N NH1 . ARG A 131 ? 0.8950 0.8217 0.5677 -0.1098 0.0994 -0.1322 129 ARG A NH1 1005 N NH2 . ARG A 131 ? 0.9320 0.8803 0.5412 -0.1465 0.1161 -0.1586 129 ARG A NH2 1006 N N . VAL A 132 ? 0.5232 0.4918 0.3172 -0.0083 0.1249 -0.0357 130 VAL A N 1007 C CA . VAL A 132 ? 0.5077 0.4970 0.3311 0.0061 0.1288 -0.0194 130 VAL A CA 1008 C C . VAL A 132 ? 0.5292 0.5048 0.3669 0.0277 0.1541 -0.0256 130 VAL A C 1009 O O . VAL A 132 ? 0.5558 0.5070 0.3732 0.0288 0.1781 -0.0436 130 VAL A O 1010 C CB . VAL A 132 ? 0.5293 0.5454 0.3429 -0.0037 0.1335 -0.0114 130 VAL A CB 1011 C CG1 . VAL A 132 ? 0.5143 0.5568 0.3578 0.0104 0.1451 0.0011 130 VAL A CG1 1012 C CG2 . VAL A 132 ? 0.5059 0.5336 0.3130 -0.0196 0.1083 0.0026 130 VAL A CG2 1013 N N . GLY A 133 ? 0.5118 0.5007 0.3833 0.0446 0.1493 -0.0112 131 GLY A N 1014 C CA . GLY A 133 ? 0.5312 0.5158 0.4213 0.0698 0.1725 -0.0093 131 GLY A CA 1015 C C . GLY A 133 ? 0.5502 0.5006 0.4420 0.0794 0.1741 -0.0146 131 GLY A C 1016 O O . GLY A 133 ? 0.5601 0.5076 0.4718 0.1031 0.1888 -0.0065 131 GLY A O 1017 N N . ASP A 134 ? 0.5575 0.4848 0.4293 0.0617 0.1596 -0.0260 132 ASP A N 1018 C CA . ASP A 134 ? 0.5715 0.4663 0.4430 0.0669 0.1618 -0.0318 132 ASP A CA 1019 C C . ASP A 134 ? 0.5326 0.4453 0.4300 0.0734 0.1391 -0.0158 132 ASP A C 1020 O O . ASP A 134 ? 0.4927 0.4383 0.4049 0.0693 0.1193 -0.0039 132 ASP A O 1021 C CB . ASP A 134 ? 0.5958 0.4635 0.4353 0.0432 0.1581 -0.0529 132 ASP A CB 1022 C CG . ASP A 134 ? 0.6562 0.4944 0.4648 0.0353 0.1871 -0.0754 132 ASP A CG 1023 O OD1 . ASP A 134 ? 0.7078 0.5321 0.5189 0.0523 0.2162 -0.0772 132 ASP A OD1 1024 O OD2 . ASP A 134 ? 0.6901 0.5201 0.4706 0.0107 0.1815 -0.0926 132 ASP A OD2 1025 N N . THR A 135 ? 0.5480 0.4356 0.4485 0.0819 0.1444 -0.0169 133 THR A N 1026 C CA . THR A 135 ? 0.5251 0.4255 0.4446 0.0864 0.1258 -0.0052 133 THR A CA 1027 C C . THR A 135 ? 0.5178 0.3993 0.4208 0.0670 0.1117 -0.0186 133 THR A C 1028 O O . THR A 135 ? 0.5587 0.4101 0.4384 0.0558 0.1237 -0.0357 133 THR A O 1029 C CB . THR A 135 ? 0.5435 0.4319 0.4772 0.1108 0.1433 0.0061 133 THR A CB 1030 O OG1 . THR A 135 ? 0.5671 0.4891 0.5230 0.1305 0.1515 0.0230 133 THR A OG1 1031 C CG2 . THR A 135 ? 0.5343 0.4291 0.4794 0.1119 0.1266 0.0147 133 THR A CG2 1032 N N . THR A 136 ? 0.4650 0.3667 0.3803 0.0618 0.0877 -0.0122 134 THR A N 1033 C CA . THR A 136 ? 0.4606 0.3516 0.3668 0.0476 0.0745 -0.0221 134 THR A CA 1034 C C . THR A 136 ? 0.4243 0.3269 0.3487 0.0531 0.0608 -0.0135 134 THR A C 1035 O O . THR A 136 ? 0.3953 0.3198 0.3380 0.0642 0.0567 -0.0001 134 THR A O 1036 C CB . THR A 136 ? 0.4556 0.3592 0.3497 0.0295 0.0578 -0.0283 134 THR A CB 1037 O OG1 . THR A 136 ? 0.4942 0.3880 0.3764 0.0161 0.0516 -0.0404 134 THR A OG1 1038 C CG2 . THR A 136 ? 0.4094 0.3393 0.3200 0.0297 0.0372 -0.0159 134 THR A CG2 1039 N N . GLN A 137 ? 0.4419 0.3331 0.3600 0.0436 0.0548 -0.0224 135 GLN A N 1040 C CA . GLN A 137 ? 0.4304 0.3334 0.3621 0.0454 0.0415 -0.0177 135 GLN A CA 1041 C C . GLN A 137 ? 0.4147 0.3323 0.3471 0.0335 0.0216 -0.0229 135 GLN A C 1042 O O . GLN A 137 ? 0.4250 0.3398 0.3442 0.0226 0.0194 -0.0309 135 GLN A O 1043 C CB . GLN A 137 ? 0.4565 0.3369 0.3821 0.0445 0.0521 -0.0227 135 GLN A CB 1044 C CG . GLN A 137 ? 0.4509 0.3454 0.3879 0.0439 0.0391 -0.0199 135 GLN A CG 1045 C CD . GLN A 137 ? 0.5408 0.4122 0.4707 0.0423 0.0524 -0.0222 135 GLN A CD 1046 O OE1 . GLN A 137 ? 0.5724 0.4410 0.5082 0.0554 0.0607 -0.0091 135 GLN A OE1 1047 N NE2 . GLN A 137 ? 0.5507 0.4074 0.4673 0.0252 0.0553 -0.0377 135 GLN A NE2 1048 N N . MET A 138 ? 0.3976 0.3323 0.3451 0.0364 0.0082 -0.0173 136 MET A N 1049 C CA . MET A 138 ? 0.3942 0.3373 0.3455 0.0296 -0.0075 -0.0216 136 MET A CA 1050 C C . MET A 138 ? 0.3731 0.3201 0.3330 0.0312 -0.0107 -0.0244 136 MET A C 1051 O O . MET A 138 ? 0.3560 0.3122 0.3253 0.0370 -0.0116 -0.0192 136 MET A O 1052 C CB . MET A 138 ? 0.3974 0.3515 0.3563 0.0296 -0.0176 -0.0149 136 MET A CB 1053 C CG . MET A 138 ? 0.4800 0.4316 0.4269 0.0248 -0.0160 -0.0126 136 MET A CG 1054 S SD . MET A 138 ? 0.5822 0.5420 0.5376 0.0235 -0.0233 -0.0024 136 MET A SD 1055 C CE . MET A 138 ? 0.6369 0.6082 0.5991 0.0292 -0.0109 0.0031 136 MET A CE 1056 N N . ARG A 139 ? 0.3761 0.3209 0.3317 0.0243 -0.0124 -0.0331 137 ARG A N 1057 C CA . ARG A 139 ? 0.3810 0.3277 0.3409 0.0236 -0.0109 -0.0371 137 ARG A CA 1058 C C . ARG A 139 ? 0.3629 0.3264 0.3356 0.0242 -0.0240 -0.0400 137 ARG A C 1059 O O . ARG A 139 ? 0.3419 0.3118 0.3171 0.0232 -0.0329 -0.0405 137 ARG A O 1060 C CB . ARG A 139 ? 0.4181 0.3536 0.3657 0.0127 -0.0019 -0.0462 137 ARG A CB 1061 C CG . ARG A 139 ? 0.4659 0.4081 0.4184 0.0077 -0.0016 -0.0515 137 ARG A CG 1062 C CD . ARG A 139 ? 0.5343 0.4635 0.4729 -0.0076 0.0095 -0.0616 137 ARG A CD 1063 N NE . ARG A 139 ? 0.5566 0.5017 0.4907 -0.0191 0.0010 -0.0698 137 ARG A NE 1064 C CZ . ARG A 139 ? 0.5861 0.5229 0.5033 -0.0366 0.0097 -0.0811 137 ARG A CZ 1065 N NH1 . ARG A 139 ? 0.6102 0.5137 0.5133 -0.0441 0.0299 -0.0865 137 ARG A NH1 1066 N NH2 . ARG A 139 ? 0.5977 0.5593 0.5108 -0.0472 -0.0009 -0.0866 137 ARG A NH2 1067 N N . CYS A 140 ? 0.3596 0.3298 0.3396 0.0272 -0.0237 -0.0406 138 CYS A N 1068 C CA . CYS A 140 ? 0.3640 0.3476 0.3558 0.0288 -0.0317 -0.0461 138 CYS A CA 1069 C C . CYS A 140 ? 0.3474 0.3386 0.3404 0.0282 -0.0264 -0.0485 138 CYS A C 1070 O O . CYS A 140 ? 0.3350 0.3283 0.3255 0.0309 -0.0231 -0.0425 138 CYS A O 1071 C CB . CYS A 140 ? 0.3745 0.3582 0.3725 0.0327 -0.0380 -0.0435 138 CYS A CB 1072 S SG . CYS A 140 ? 0.4330 0.4217 0.4439 0.0359 -0.0438 -0.0518 138 CYS A SG 1073 N N . SER A 141 ? 0.3351 0.3353 0.3318 0.0242 -0.0256 -0.0558 139 SER A N 1074 C CA . SER A 141 ? 0.3499 0.3576 0.3452 0.0218 -0.0190 -0.0573 139 SER A CA 1075 C C . SER A 141 ? 0.3368 0.3628 0.3427 0.0190 -0.0212 -0.0675 139 SER A C 1076 O O . SER A 141 ? 0.3458 0.3788 0.3586 0.0183 -0.0264 -0.0710 139 SER A O 1077 C CB . SER A 141 ? 0.3623 0.3540 0.3445 0.0170 -0.0067 -0.0508 139 SER A CB 1078 O OG . SER A 141 ? 0.4084 0.3942 0.3867 0.0065 -0.0030 -0.0574 139 SER A OG 1079 N N . ILE A 142 ? 0.3218 0.3608 0.3300 0.0184 -0.0175 -0.0715 140 ILE A N 1080 C CA . ILE A 142 ? 0.2985 0.3588 0.3182 0.0161 -0.0168 -0.0811 140 ILE A CA 1081 C C . ILE A 142 ? 0.2956 0.3595 0.3078 0.0039 -0.0069 -0.0805 140 ILE A C 1082 O O . ILE A 142 ? 0.2995 0.3551 0.2996 0.0012 0.0009 -0.0737 140 ILE A O 1083 C CB . ILE A 142 ? 0.3085 0.3817 0.3358 0.0224 -0.0169 -0.0895 140 ILE A CB 1084 C CG1 . ILE A 142 ? 0.3125 0.3751 0.3472 0.0322 -0.0241 -0.0916 140 ILE A CG1 1085 C CG2 . ILE A 142 ? 0.2805 0.3804 0.3216 0.0219 -0.0128 -0.0997 140 ILE A CG2 1086 C CD1 . ILE A 142 ? 0.3134 0.3793 0.3509 0.0353 -0.0213 -0.1020 140 ILE A CD1 1087 N N . GLN A 143 ? 0.2892 0.3674 0.3086 -0.0043 -0.0069 -0.0862 141 GLN A N 1088 C CA . GLN A 143 ? 0.2965 0.3820 0.3111 -0.0205 0.0035 -0.0890 141 GLN A CA 1089 C C . GLN A 143 ? 0.2972 0.4055 0.3185 -0.0196 0.0085 -0.0931 141 GLN A C 1090 O O . GLN A 143 ? 0.2842 0.4188 0.3230 -0.0109 0.0036 -0.1010 141 GLN A O 1091 C CB . GLN A 143 ? 0.2864 0.3939 0.3099 -0.0319 -0.0002 -0.0963 141 GLN A CB 1092 C CG . GLN A 143 ? 0.3071 0.4252 0.3266 -0.0538 0.0110 -0.1017 141 GLN A CG 1093 C CD . GLN A 143 ? 0.3126 0.3883 0.3076 -0.0687 0.0249 -0.0978 141 GLN A CD 1094 O OE1 . GLN A 143 ? 0.2988 0.3481 0.2814 -0.0650 0.0352 -0.0885 141 GLN A OE1 1095 N NE2 . GLN A 143 ? 0.2614 0.3314 0.2486 -0.0855 0.0267 -0.1045 141 GLN A NE2 1096 N N . SER A 144 ? 0.3163 0.4132 0.3226 -0.0277 0.0200 -0.0868 142 SER A N 1097 C CA . SER A 144 ? 0.3199 0.4352 0.3256 -0.0271 0.0256 -0.0880 142 SER A CA 1098 C C . SER A 144 ? 0.3457 0.4514 0.3353 -0.0416 0.0404 -0.0792 142 SER A C 1099 O O . SER A 144 ? 0.3533 0.4262 0.3277 -0.0451 0.0472 -0.0675 142 SER A O 1100 C CB . SER A 144 ? 0.3222 0.4325 0.3224 -0.0137 0.0202 -0.0842 142 SER A CB 1101 O OG . SER A 144 ? 0.3183 0.4505 0.3149 -0.0149 0.0254 -0.0878 142 SER A OG 1102 N N . THR A 145 ? 0.3489 0.4827 0.3425 -0.0491 0.0473 -0.0847 143 THR A N 1103 C CA . THR A 145 ? 0.3742 0.5030 0.3516 -0.0621 0.0623 -0.0747 143 THR A CA 1104 C C . THR A 145 ? 0.3778 0.5073 0.3396 -0.0526 0.0637 -0.0622 143 THR A C 1105 O O . THR A 145 ? 0.3958 0.5187 0.3407 -0.0598 0.0757 -0.0477 143 THR A O 1106 C CB . THR A 145 ? 0.3724 0.5404 0.3621 -0.0751 0.0690 -0.0869 143 THR A CB 1107 O OG1 . THR A 145 ? 0.3357 0.5371 0.3405 -0.0617 0.0620 -0.0993 143 THR A OG1 1108 C CG2 . THR A 145 ? 0.3790 0.5578 0.3837 -0.0884 0.0679 -0.0973 143 THR A CG2 1109 N N . GLU A 146 ? 0.3545 0.4942 0.3211 -0.0382 0.0519 -0.0674 144 GLU A N 1110 C CA . GLU A 146 ? 0.3663 0.5197 0.3191 -0.0329 0.0512 -0.0604 144 GLU A CA 1111 C C . GLU A 146 ? 0.3649 0.5021 0.3119 -0.0209 0.0418 -0.0492 144 GLU A C 1112 O O . GLU A 146 ? 0.3569 0.4819 0.3154 -0.0139 0.0323 -0.0565 144 GLU A O 1113 C CB . GLU A 146 ? 0.3648 0.5515 0.3268 -0.0313 0.0485 -0.0814 144 GLU A CB 1114 C CG . GLU A 146 ? 0.3916 0.6036 0.3643 -0.0405 0.0581 -0.0941 144 GLU A CG 1115 C CD . GLU A 146 ? 0.4816 0.7011 0.4372 -0.0549 0.0721 -0.0807 144 GLU A CD 1116 O OE1 . GLU A 146 ? 0.4894 0.7160 0.4241 -0.0553 0.0747 -0.0688 144 GLU A OE1 1117 O OE2 . GLU A 146 ? 0.5328 0.7542 0.4956 -0.0673 0.0808 -0.0818 144 GLU A OE2 1118 N N . GLU A 147 ? 0.3823 0.5241 0.3119 -0.0185 0.0445 -0.0297 145 GLU A N 1119 C CA . GLU A 147 ? 0.3818 0.5186 0.3073 -0.0071 0.0364 -0.0159 145 GLU A CA 1120 C C . GLU A 147 ? 0.3588 0.5238 0.2865 -0.0062 0.0247 -0.0305 145 GLU A C 1121 O O . GLU A 147 ? 0.3505 0.5394 0.2766 -0.0135 0.0258 -0.0471 145 GLU A O 1122 C CB . GLU A 147 ? 0.4059 0.5439 0.3138 -0.0027 0.0440 0.0144 145 GLU A CB 1123 C CG . GLU A 147 ? 0.4642 0.6448 0.3565 -0.0080 0.0443 0.0199 145 GLU A CG 1124 C CD . GLU A 147 ? 0.5195 0.7062 0.3953 0.0005 0.0498 0.0561 145 GLU A CD 1125 O OE1 . GLU A 147 ? 0.5007 0.6638 0.3804 0.0146 0.0505 0.0750 145 GLU A OE1 1126 O OE2 . GLU A 147 ? 0.5847 0.8012 0.4437 -0.0055 0.0544 0.0669 145 GLU A OE2 1127 N N . LYS A 148 ? 0.3431 0.5043 0.2740 0.0013 0.0154 -0.0255 146 LYS A N 1128 C CA . LYS A 148 ? 0.3394 0.5284 0.2675 -0.0019 0.0059 -0.0357 146 LYS A CA 1129 C C . LYS A 148 ? 0.3295 0.5199 0.2662 -0.0083 0.0045 -0.0669 146 LYS A C 1130 O O . LYS A 148 ? 0.3260 0.5407 0.2545 -0.0166 0.0038 -0.0812 146 LYS A O 1131 C CB . LYS A 148 ? 0.3560 0.5846 0.2650 -0.0065 0.0069 -0.0217 146 LYS A CB 1132 C CG . LYS A 148 ? 0.3683 0.6024 0.2715 0.0046 0.0064 0.0122 146 LYS A CG 1133 C CD . LYS A 148 ? 0.4251 0.7016 0.3088 0.0015 0.0080 0.0307 146 LYS A CD 1134 C CE . LYS A 148 ? 0.4502 0.7292 0.3307 0.0179 0.0107 0.0702 146 LYS A CE 1135 N NZ . LYS A 148 ? 0.4975 0.8164 0.3579 0.0173 0.0137 0.0947 146 LYS A NZ 1136 N N . ARG A 149 ? 0.3161 0.4805 0.2691 -0.0038 0.0048 -0.0771 147 ARG A N 1137 C CA . ARG A 149 ? 0.3143 0.4769 0.2784 -0.0045 0.0047 -0.1024 147 ARG A CA 1138 C C . ARG A 149 ? 0.3077 0.4530 0.2792 -0.0013 -0.0033 -0.1094 147 ARG A C 1139 O O . ARG A 149 ? 0.3332 0.4783 0.3062 -0.0045 -0.0023 -0.1289 147 ARG A O 1140 C CB . ARG A 149 ? 0.3085 0.4634 0.2875 -0.0009 0.0102 -0.1083 147 ARG A CB 1141 C CG . ARG A 149 ? 0.3132 0.4885 0.2852 -0.0080 0.0203 -0.1064 147 ARG A CG 1142 C CD . ARG A 149 ? 0.3558 0.5574 0.3156 -0.0146 0.0250 -0.1186 147 ARG A CD 1143 N NE . ARG A 149 ? 0.4017 0.6256 0.3520 -0.0226 0.0354 -0.1145 147 ARG A NE 1144 C CZ . ARG A 149 ? 0.4012 0.6448 0.3569 -0.0258 0.0451 -0.1318 147 ARG A CZ 1145 N NH1 . ARG A 149 ? 0.4171 0.6592 0.3897 -0.0188 0.0468 -0.1547 147 ARG A NH1 1146 N NH2 . ARG A 149 ? 0.4092 0.6738 0.3537 -0.0351 0.0550 -0.1247 147 ARG A NH2 1147 N N . VAL A 150 ? 0.2976 0.4266 0.2721 0.0039 -0.0093 -0.0941 148 VAL A N 1148 C CA . VAL A 150 ? 0.2926 0.4074 0.2723 0.0050 -0.0164 -0.0974 148 VAL A CA 1149 C C . VAL A 150 ? 0.3082 0.4446 0.2764 -0.0053 -0.0201 -0.1000 148 VAL A C 1150 O O . VAL A 150 ? 0.2784 0.4401 0.2363 -0.0074 -0.0219 -0.0838 148 VAL A O 1151 C CB . VAL A 150 ? 0.2856 0.3805 0.2704 0.0126 -0.0201 -0.0801 148 VAL A CB 1152 C CG1 . VAL A 150 ? 0.2659 0.3536 0.2529 0.0118 -0.0268 -0.0782 148 VAL A CG1 1153 C CG2 . VAL A 150 ? 0.2752 0.3525 0.2715 0.0182 -0.0185 -0.0844 148 VAL A CG2 1154 N N . THR A 151 ? 0.3259 0.4529 0.2962 -0.0119 -0.0203 -0.1197 149 THR A N 1155 C CA . THR A 151 ? 0.3466 0.4946 0.3050 -0.0278 -0.0226 -0.1292 149 THR A CA 1156 C C . THR A 151 ? 0.3525 0.4891 0.3159 -0.0317 -0.0292 -0.1249 149 THR A C 1157 O O . THR A 151 ? 0.3354 0.4997 0.2906 -0.0454 -0.0337 -0.1246 149 THR A O 1158 C CB . THR A 151 ? 0.3664 0.5092 0.3194 -0.0379 -0.0141 -0.1591 149 THR A CB 1159 O OG1 . THR A 151 ? 0.3860 0.4870 0.3537 -0.0287 -0.0093 -0.1701 149 THR A OG1 1160 C CG2 . THR A 151 ? 0.3751 0.5385 0.3209 -0.0373 -0.0064 -0.1647 149 THR A CG2 1161 N N . LYS A 152 ? 0.3473 0.4490 0.3239 -0.0208 -0.0299 -0.1204 150 LYS A N 1162 C CA . LYS A 152 ? 0.3594 0.4479 0.3403 -0.0254 -0.0343 -0.1169 150 LYS A CA 1163 C C . LYS A 152 ? 0.3415 0.4042 0.3334 -0.0101 -0.0363 -0.1021 150 LYS A C 1164 O O . LYS A 152 ? 0.3430 0.3887 0.3414 0.0014 -0.0336 -0.1030 150 LYS A O 1165 C CB . LYS A 152 ? 0.3951 0.4602 0.3741 -0.0379 -0.0288 -0.1408 150 LYS A CB 1166 C CG . LYS A 152 ? 0.4268 0.4748 0.4079 -0.0482 -0.0307 -0.1408 150 LYS A CG 1167 C CD . LYS A 152 ? 0.5203 0.5356 0.4973 -0.0607 -0.0206 -0.1667 150 LYS A CD 1168 C CE . LYS A 152 ? 0.5721 0.5548 0.5520 -0.0695 -0.0191 -0.1660 150 LYS A CE 1169 N NZ . LYS A 152 ? 0.6461 0.6496 0.6150 -0.0996 -0.0195 -0.1774 150 LYS A NZ 1170 N N . VAL A 153 ? 0.3294 0.3963 0.3230 -0.0109 -0.0407 -0.0880 151 VAL A N 1171 C CA . VAL A 153 ? 0.3150 0.3592 0.3154 -0.0006 -0.0421 -0.0759 151 VAL A CA 1172 C C . VAL A 153 ? 0.3206 0.3591 0.3225 -0.0102 -0.0443 -0.0746 151 VAL A C 1173 O O . VAL A 153 ? 0.3104 0.3768 0.3100 -0.0208 -0.0464 -0.0718 151 VAL A O 1174 C CB . VAL A 153 ? 0.3069 0.3629 0.3065 0.0093 -0.0418 -0.0572 151 VAL A CB 1175 C CG1 . VAL A 153 ? 0.3335 0.3658 0.3367 0.0165 -0.0420 -0.0490 151 VAL A CG1 1176 C CG2 . VAL A 153 ? 0.3040 0.3640 0.3005 0.0157 -0.0379 -0.0564 151 VAL A CG2 1177 N N . ASN A 154 ? 0.3253 0.3317 0.3314 -0.0068 -0.0437 -0.0748 152 ASN A N 1178 C CA . ASN A 154 ? 0.3363 0.3314 0.3430 -0.0166 -0.0440 -0.0722 152 ASN A CA 1179 C C . ASN A 154 ? 0.3166 0.2932 0.3258 -0.0049 -0.0452 -0.0580 152 ASN A C 1180 O O . ASN A 154 ? 0.3054 0.2635 0.3171 0.0064 -0.0453 -0.0579 152 ASN A O 1181 C CB . ASN A 154 ? 0.3772 0.3446 0.3826 -0.0274 -0.0390 -0.0893 152 ASN A CB 1182 C CG . ASN A 154 ? 0.4341 0.3872 0.4380 -0.0427 -0.0371 -0.0883 152 ASN A CG 1183 O OD1 . ASN A 154 ? 0.5350 0.4508 0.5406 -0.0387 -0.0338 -0.0846 152 ASN A OD1 1184 N ND2 . ASN A 154 ? 0.4721 0.4578 0.4732 -0.0609 -0.0390 -0.0901 152 ASN A ND2 1185 N N . TRP A 155 ? 0.2947 0.2829 0.3033 -0.0077 -0.0460 -0.0459 153 TRP A N 1186 C CA . TRP A 155 ? 0.2959 0.2687 0.3033 -0.0012 -0.0460 -0.0342 153 TRP A CA 1187 C C . TRP A 155 ? 0.3093 0.2684 0.3161 -0.0133 -0.0447 -0.0316 153 TRP A C 1188 O O . TRP A 155 ? 0.2949 0.2723 0.3030 -0.0272 -0.0437 -0.0333 153 TRP A O 1189 C CB . TRP A 155 ? 0.2934 0.2865 0.2992 0.0057 -0.0442 -0.0228 153 TRP A CB 1190 C CG . TRP A 155 ? 0.2747 0.2693 0.2781 0.0172 -0.0426 -0.0229 153 TRP A CG 1191 C CD1 . TRP A 155 ? 0.2731 0.2851 0.2773 0.0203 -0.0409 -0.0242 153 TRP A CD1 1192 C CD2 . TRP A 155 ? 0.2777 0.2572 0.2762 0.0242 -0.0420 -0.0214 153 TRP A CD2 1193 N NE1 . TRP A 155 ? 0.2671 0.2699 0.2673 0.0283 -0.0376 -0.0239 153 TRP A NE1 1194 C CE2 . TRP A 155 ? 0.2756 0.2604 0.2724 0.0294 -0.0386 -0.0237 153 TRP A CE2 1195 C CE3 . TRP A 155 ? 0.2826 0.2476 0.2769 0.0249 -0.0442 -0.0178 153 TRP A CE3 1196 C CZ2 . TRP A 155 ? 0.3000 0.2753 0.2910 0.0323 -0.0364 -0.0253 153 TRP A CZ2 1197 C CZ3 . TRP A 155 ? 0.2926 0.2544 0.2810 0.0287 -0.0439 -0.0184 153 TRP A CZ3 1198 C CH2 . TRP A 155 ? 0.2958 0.2624 0.2829 0.0310 -0.0398 -0.0238 153 TRP A CH2 1199 N N . MET A 156 ? 0.3292 0.2588 0.3340 -0.0086 -0.0446 -0.0261 154 MET A N 1200 C CA . MET A 156 ? 0.3530 0.2624 0.3551 -0.0191 -0.0417 -0.0199 154 MET A CA 1201 C C . MET A 156 ? 0.3439 0.2518 0.3403 -0.0120 -0.0429 -0.0039 154 MET A C 1202 O O . MET A 156 ? 0.3089 0.2218 0.3030 0.0012 -0.0462 -0.0004 154 MET A O 1203 C CB . MET A 156 ? 0.3916 0.2608 0.3947 -0.0176 -0.0384 -0.0241 154 MET A CB 1204 C CG . MET A 156 ? 0.4660 0.3278 0.4719 -0.0246 -0.0343 -0.0436 154 MET A CG 1205 S SD . MET A 156 ? 0.5583 0.4292 0.5604 -0.0553 -0.0294 -0.0549 154 MET A SD 1206 C CE . MET A 156 ? 0.6231 0.4339 0.6210 -0.0657 -0.0181 -0.0565 154 MET A CE 1207 N N . PHE A 157 ? 0.3554 0.2574 0.3480 -0.0237 -0.0394 0.0047 155 PHE A N 1208 C CA . PHE A 157 ? 0.3539 0.2542 0.3378 -0.0204 -0.0392 0.0204 155 PHE A CA 1209 C C . PHE A 157 ? 0.3911 0.2595 0.3701 -0.0280 -0.0358 0.0309 155 PHE A C 1210 O O . PHE A 157 ? 0.3878 0.2437 0.3691 -0.0446 -0.0303 0.0266 155 PHE A O 1211 C CB . PHE A 157 ? 0.3422 0.2739 0.3252 -0.0271 -0.0353 0.0239 155 PHE A CB 1212 C CG . PHE A 157 ? 0.3531 0.2851 0.3246 -0.0273 -0.0324 0.0380 155 PHE A CG 1213 C CD1 . PHE A 157 ? 0.3662 0.2995 0.3277 -0.0155 -0.0347 0.0418 155 PHE A CD1 1214 C CD2 . PHE A 157 ? 0.3866 0.3215 0.3561 -0.0422 -0.0266 0.0461 155 PHE A CD2 1215 C CE1 . PHE A 157 ? 0.3496 0.2874 0.2973 -0.0180 -0.0314 0.0527 155 PHE A CE1 1216 C CE2 . PHE A 157 ? 0.3949 0.3336 0.3521 -0.0434 -0.0228 0.0587 155 PHE A CE2 1217 C CZ . PHE A 157 ? 0.3978 0.3383 0.3433 -0.0311 -0.0252 0.0617 155 PHE A CZ 1218 N N . SER A 158 ? 0.4097 0.2677 0.3804 -0.0176 -0.0384 0.0459 156 SER A N 1219 C CA . SER A 158 ? 0.4559 0.2890 0.4185 -0.0230 -0.0346 0.0630 156 SER A CA 1220 C C . SER A 158 ? 0.4606 0.3121 0.4091 -0.0191 -0.0372 0.0789 156 SER A C 1221 O O . SER A 158 ? 0.4298 0.2979 0.3748 -0.0068 -0.0437 0.0789 156 SER A O 1222 C CB . SER A 158 ? 0.4792 0.2752 0.4453 -0.0104 -0.0348 0.0692 156 SER A CB 1223 O OG . SER A 158 ? 0.5908 0.3537 0.5497 -0.0178 -0.0277 0.0861 156 SER A OG 1224 N N . SER A 159 ? 0.4932 0.3423 0.4320 -0.0319 -0.0313 0.0915 157 SER A N 1225 C CA . SER A 159 ? 0.5403 0.4003 0.4620 -0.0287 -0.0331 0.1092 157 SER A CA 1226 C C . SER A 159 ? 0.5971 0.4258 0.5128 -0.0205 -0.0352 0.1316 157 SER A C 1227 O O . SER A 159 ? 0.6295 0.4230 0.5555 -0.0171 -0.0325 0.1316 157 SER A O 1228 C CB . SER A 159 ? 0.5394 0.4168 0.4528 -0.0455 -0.0243 0.1132 157 SER A CB 1229 O OG . SER A 159 ? 0.5994 0.4495 0.5112 -0.0593 -0.0175 0.1256 157 SER A OG 1230 N N . GLY A 160 ? 0.6396 0.4809 0.5380 -0.0166 -0.0387 0.1512 158 GLY A N 1231 C CA . GLY A 160 ? 0.6999 0.5152 0.5916 -0.0070 -0.0401 0.1799 158 GLY A CA 1232 C C . GLY A 160 ? 0.7568 0.5266 0.6481 -0.0190 -0.0278 0.1923 158 GLY A C 1233 O O . GLY A 160 ? 0.7933 0.5236 0.6877 -0.0078 -0.0250 0.2098 158 GLY A O 1234 N N . SER A 161 ? 0.7750 0.5509 0.6639 -0.0421 -0.0189 0.1827 159 SER A N 1235 C CA . SER A 161 ? 0.8238 0.5635 0.7110 -0.0627 -0.0053 0.1902 159 SER A CA 1236 C C . SER A 161 ? 0.8299 0.5431 0.7344 -0.0755 0.0019 0.1667 159 SER A C 1237 O O . SER A 161 ? 0.8751 0.5601 0.7782 -0.0978 0.0142 0.1679 159 SER A O 1238 C CB . SER A 161 ? 0.8181 0.5902 0.6938 -0.0839 0.0010 0.1927 159 SER A CB 1239 O OG . SER A 161 ? 0.7745 0.5919 0.6592 -0.0864 -0.0017 0.1685 159 SER A OG 1240 N N . HIS A 162 ? 0.8031 0.5269 0.7220 -0.0645 -0.0047 0.1446 160 HIS A N 1241 C CA . HIS A 162 ? 0.8094 0.5147 0.7412 -0.0787 0.0017 0.1210 160 HIS A CA 1242 C C . HIS A 162 ? 0.8641 0.5048 0.7975 -0.0754 0.0112 0.1249 160 HIS A C 1243 O O . HIS A 162 ? 0.8596 0.4784 0.7944 -0.0494 0.0082 0.1382 160 HIS A O 1244 C CB . HIS A 162 ? 0.7598 0.4980 0.7047 -0.0689 -0.0073 0.0971 160 HIS A CB 1245 C CG . HIS A 162 ? 0.7199 0.5117 0.6677 -0.0785 -0.0103 0.0864 160 HIS A CG 1246 N ND1 . HIS A 162 ? 0.7167 0.5341 0.6767 -0.0840 -0.0122 0.0646 160 HIS A ND1 1247 C CD2 . HIS A 162 ? 0.7049 0.5302 0.6451 -0.0812 -0.0103 0.0958 160 HIS A CD2 1248 C CE1 . HIS A 162 ? 0.6575 0.5208 0.6195 -0.0872 -0.0132 0.0634 160 HIS A CE1 1249 N NE2 . HIS A 162 ? 0.6667 0.5342 0.6170 -0.0853 -0.0112 0.0804 160 HIS A NE2 1250 N N . THR A 163 ? 0.9097 0.5221 0.8436 -0.1025 0.0240 0.1126 161 THR A N 1251 C CA . THR A 163 ? 0.9772 0.5234 0.9130 -0.1042 0.0374 0.1061 161 THR A CA 1252 C C . THR A 163 ? 0.9531 0.5089 0.9014 -0.0987 0.0339 0.0757 161 THR A C 1253 O O . THR A 163 ? 0.9917 0.4997 0.9439 -0.0875 0.0425 0.0686 161 THR A O 1254 C CB . THR A 163 ? 1.0316 0.5412 0.9596 -0.1421 0.0550 0.1009 161 THR A CB 1255 O OG1 . THR A 163 ? 1.0686 0.5630 0.9834 -0.1469 0.0606 0.1319 161 THR A OG1 1256 C CG2 . THR A 163 ? 1.1057 0.5412 1.0339 -0.1463 0.0723 0.0872 161 THR A CG2 1257 N N . GLU A 164 ? 0.8962 0.5132 0.8506 -0.1054 0.0227 0.0590 162 GLU A N 1258 C CA . GLU A 164 ? 0.8685 0.5028 0.8326 -0.1035 0.0189 0.0314 162 GLU A CA 1259 C C . GLU A 164 ? 0.7833 0.4837 0.7537 -0.0913 0.0033 0.0285 162 GLU A C 1260 O O . GLU A 164 ? 0.7522 0.4906 0.7203 -0.0965 -0.0014 0.0380 162 GLU A O 1261 C CB . GLU A 164 ? 0.9009 0.5285 0.8638 -0.1397 0.0291 0.0059 162 GLU A CB 1262 C CG . GLU A 164 ? 0.9565 0.5535 0.9218 -0.1402 0.0364 -0.0205 162 GLU A CG 1263 C CD . GLU A 164 ? 1.0744 0.6185 1.0306 -0.1741 0.0560 -0.0374 162 GLU A CD 1264 O OE1 . GLU A 164 ? 1.1775 0.6641 1.1263 -0.1773 0.0693 -0.0210 162 GLU A OE1 1265 O OE2 . GLU A 164 ? 1.0956 0.6545 1.0503 -0.1990 0.0591 -0.0672 162 GLU A OE2 1266 N N . GLU A 165 ? 0.7481 0.4569 0.7259 -0.0738 -0.0024 0.0159 163 GLU A N 1267 C CA . GLU A 165 ? 0.6877 0.4492 0.6712 -0.0664 -0.0132 0.0077 163 GLU A CA 1268 C C . GLU A 165 ? 0.6571 0.4567 0.6430 -0.0909 -0.0130 -0.0068 163 GLU A C 1269 O O . GLU A 165 ? 0.6773 0.4630 0.6622 -0.1134 -0.0056 -0.0222 163 GLU A O 1270 C CB . GLU A 165 ? 0.6862 0.4420 0.6766 -0.0511 -0.0151 -0.0071 163 GLU A CB 1271 C CG . GLU A 165 ? 0.7118 0.4582 0.7053 -0.0230 -0.0198 0.0056 163 GLU A CG 1272 C CD . GLU A 165 ? 0.7567 0.4861 0.7583 -0.0109 -0.0164 -0.0091 163 GLU A CD 1273 O OE1 . GLU A 165 ? 0.8159 0.5185 0.8166 -0.0253 -0.0059 -0.0270 163 GLU A OE1 1274 O OE2 . GLU A 165 ? 0.7652 0.5094 0.7733 0.0113 -0.0231 -0.0039 163 GLU A OE2 1275 N N . GLU A 166 ? 0.5903 0.4396 0.5796 -0.0858 -0.0203 -0.0026 164 GLU A N 1276 C CA . GLU A 166 ? 0.5577 0.4530 0.5530 -0.1020 -0.0217 -0.0135 164 GLU A CA 1277 C C . GLU A 166 ? 0.4873 0.4145 0.4881 -0.0851 -0.0290 -0.0196 164 GLU A C 1278 O O . GLU A 166 ? 0.4387 0.3593 0.4384 -0.0630 -0.0326 -0.0129 164 GLU A O 1279 C CB . GLU A 166 ? 0.5585 0.4868 0.5555 -0.1125 -0.0199 -0.0010 164 GLU A CB 1280 C CG . GLU A 166 ? 0.5741 0.5152 0.5690 -0.0920 -0.0224 0.0145 164 GLU A CG 1281 C CD . GLU A 166 ? 0.6403 0.6197 0.6388 -0.1021 -0.0181 0.0237 164 GLU A CD 1282 O OE1 . GLU A 166 ? 0.6509 0.6780 0.6602 -0.0997 -0.0197 0.0209 164 GLU A OE1 1283 O OE2 . GLU A 166 ? 0.6689 0.6323 0.6601 -0.1116 -0.0125 0.0351 164 GLU A OE2 1284 N N . THR A 167 ? 0.4468 0.4098 0.4524 -0.0977 -0.0307 -0.0317 165 THR A N 1285 C CA . THR A 167 ? 0.4183 0.4107 0.4276 -0.0838 -0.0363 -0.0364 165 THR A CA 1286 C C . THR A 167 ? 0.3684 0.4010 0.3836 -0.0699 -0.0385 -0.0211 165 THR A C 1287 O O . THR A 167 ? 0.3796 0.4462 0.4006 -0.0796 -0.0370 -0.0142 165 THR A O 1288 C CB . THR A 167 ? 0.4335 0.4510 0.4429 -0.1029 -0.0373 -0.0542 165 THR A CB 1289 O OG1 . THR A 167 ? 0.4957 0.4674 0.4979 -0.1153 -0.0313 -0.0712 165 THR A OG1 1290 C CG2 . THR A 167 ? 0.3966 0.4434 0.4076 -0.0877 -0.0427 -0.0564 165 THR A CG2 1291 N N . VAL A 168 ? 0.3319 0.3587 0.3457 -0.0477 -0.0401 -0.0162 166 VAL A N 1292 C CA . VAL A 168 ? 0.3021 0.3567 0.3195 -0.0325 -0.0383 -0.0040 166 VAL A CA 1293 C C . VAL A 168 ? 0.2954 0.3877 0.3189 -0.0278 -0.0403 -0.0046 166 VAL A C 1294 O O . VAL A 168 ? 0.2865 0.4203 0.3187 -0.0254 -0.0386 0.0055 166 VAL A O 1295 C CB . VAL A 168 ? 0.2843 0.3117 0.2944 -0.0144 -0.0371 -0.0003 166 VAL A CB 1296 C CG1 . VAL A 168 ? 0.2459 0.2934 0.2575 -0.0005 -0.0312 0.0091 166 VAL A CG1 1297 C CG2 . VAL A 168 ? 0.2924 0.2897 0.2952 -0.0176 -0.0366 0.0036 166 VAL A CG2 1298 N N . LEU A 169 ? 0.3022 0.3824 0.3217 -0.0252 -0.0435 -0.0147 167 LEU A N 1299 C CA . LEU A 169 ? 0.2971 0.4105 0.3188 -0.0205 -0.0455 -0.0140 167 LEU A CA 1300 C C . LEU A 169 ? 0.3018 0.4003 0.3174 -0.0278 -0.0484 -0.0307 167 LEU A C 1301 O O . LEU A 169 ? 0.2941 0.3537 0.3058 -0.0239 -0.0474 -0.0383 167 LEU A O 1302 C CB . LEU A 169 ? 0.2888 0.4020 0.3105 0.0019 -0.0409 -0.0016 167 LEU A CB 1303 C CG . LEU A 169 ? 0.2732 0.4208 0.2973 0.0108 -0.0407 0.0068 167 LEU A CG 1304 C CD1 . LEU A 169 ? 0.2837 0.4465 0.3141 0.0308 -0.0322 0.0270 167 LEU A CD1 1305 C CD2 . LEU A 169 ? 0.2686 0.3953 0.2845 0.0149 -0.0412 -0.0016 167 LEU A CD2 1306 N N . SER A 170 ? 0.3015 0.4359 0.3164 -0.0380 -0.0514 -0.0358 168 SER A N 1307 C CA . SER A 170 ? 0.3214 0.4475 0.3287 -0.0462 -0.0522 -0.0536 168 SER A CA 1308 C C . SER A 170 ? 0.3146 0.4857 0.3190 -0.0438 -0.0550 -0.0491 168 SER A C 1309 O O . SER A 170 ? 0.2765 0.4971 0.2850 -0.0470 -0.0585 -0.0372 168 SER A O 1310 C CB . SER A 170 ? 0.3547 0.4730 0.3583 -0.0722 -0.0513 -0.0719 168 SER A CB 1311 O OG . SER A 170 ? 0.3975 0.5125 0.3923 -0.0819 -0.0497 -0.0916 168 SER A OG 1312 N N . TYR A 171 ? 0.3220 0.4789 0.3200 -0.0368 -0.0532 -0.0562 169 TYR A N 1313 C CA . TYR A 171 ? 0.3377 0.5324 0.3297 -0.0354 -0.0549 -0.0519 169 TYR A CA 1314 C C . TYR A 171 ? 0.3470 0.5295 0.3286 -0.0467 -0.0526 -0.0756 169 TYR A C 1315 O O . TYR A 171 ? 0.3370 0.4780 0.3196 -0.0396 -0.0479 -0.0856 169 TYR A O 1316 C CB . TYR A 171 ? 0.3459 0.5365 0.3398 -0.0118 -0.0513 -0.0315 169 TYR A CB 1317 C CG . TYR A 171 ? 0.3767 0.6069 0.3632 -0.0093 -0.0521 -0.0217 169 TYR A CG 1318 C CD1 . TYR A 171 ? 0.4000 0.6258 0.3761 -0.0138 -0.0501 -0.0345 169 TYR A CD1 1319 C CD2 . TYR A 171 ? 0.4260 0.7029 0.4166 -0.0023 -0.0544 0.0016 169 TYR A CD2 1320 C CE1 . TYR A 171 ? 0.4126 0.6769 0.3794 -0.0132 -0.0506 -0.0242 169 TYR A CE1 1321 C CE2 . TYR A 171 ? 0.4490 0.7662 0.4319 0.0007 -0.0557 0.0144 169 TYR A CE2 1322 C CZ . TYR A 171 ? 0.4419 0.7511 0.4113 -0.0060 -0.0539 0.0012 169 TYR A CZ 1323 O OH . TYR A 171 ? 0.4794 0.8301 0.4385 -0.0040 -0.0549 0.0157 169 TYR A OH 1324 N N . ASP A 172 ? 0.3593 0.5816 0.3313 -0.0645 -0.0552 -0.0851 170 ASP A N 1325 C CA . ASP A 172 ? 0.3941 0.6085 0.3539 -0.0759 -0.0506 -0.1094 170 ASP A CA 1326 C C . ASP A 172 ? 0.4109 0.6765 0.3590 -0.0780 -0.0534 -0.1025 170 ASP A C 1327 O O . ASP A 172 ? 0.4106 0.7295 0.3537 -0.0906 -0.0600 -0.0960 170 ASP A O 1328 C CB . ASP A 172 ? 0.4219 0.6267 0.3752 -0.1025 -0.0478 -0.1360 170 ASP A CB 1329 C CG . ASP A 172 ? 0.4687 0.6532 0.4097 -0.1121 -0.0386 -0.1649 170 ASP A CG 1330 O OD1 . ASP A 172 ? 0.4464 0.6494 0.3805 -0.1052 -0.0373 -0.1641 170 ASP A OD1 1331 O OD2 . ASP A 172 ? 0.5282 0.6769 0.4659 -0.1269 -0.0305 -0.1887 170 ASP A OD2 1332 N N . SER A 173 ? 0.4267 0.6792 0.3707 -0.0660 -0.0482 -0.1025 171 SER A N 1333 C CA . SER A 173 ? 0.4509 0.7468 0.3829 -0.0647 -0.0492 -0.0909 171 SER A CA 1334 C C . SER A 173 ? 0.4807 0.8151 0.3937 -0.0903 -0.0497 -0.1127 171 SER A C 1335 O O . SER A 173 ? 0.4944 0.8795 0.3951 -0.0935 -0.0534 -0.1001 171 SER A O 1336 C CB . SER A 173 ? 0.4461 0.7141 0.3785 -0.0486 -0.0415 -0.0876 171 SER A CB 1337 O OG . SER A 173 ? 0.4915 0.7421 0.4178 -0.0587 -0.0344 -0.1171 171 SER A OG 1338 N N . ASN A 174 ? 0.5128 0.8219 0.4219 -0.1088 -0.0447 -0.1447 172 ASN A N 1339 C CA . ASN A 174 ? 0.5544 0.8900 0.4426 -0.1371 -0.0416 -0.1732 172 ASN A CA 1340 C C . ASN A 174 ? 0.5832 0.9516 0.4666 -0.1648 -0.0483 -0.1818 172 ASN A C 1341 O O . ASN A 174 ? 0.6193 0.9929 0.4861 -0.1938 -0.0431 -0.2134 172 ASN A O 1342 C CB . ASN A 174 ? 0.5807 0.8602 0.4666 -0.1400 -0.0266 -0.2069 172 ASN A CB 1343 C CG . ASN A 174 ? 0.5857 0.8602 0.4688 -0.1246 -0.0189 -0.2071 172 ASN A CG 1344 O OD1 . ASN A 174 ? 0.6551 0.9732 0.5200 -0.1340 -0.0185 -0.2086 172 ASN A OD1 1345 N ND2 . ASN A 174 ? 0.5850 0.8113 0.4854 -0.1025 -0.0127 -0.2050 172 ASN A ND2 1346 N N . MET A 175 ? 0.5689 0.9588 0.4670 -0.1569 -0.0583 -0.1551 173 MET A N 1347 C CA . MET A 175 ? 0.5897 1.0275 0.4864 -0.1820 -0.0666 -0.1568 173 MET A CA 1348 C C . MET A 175 ? 0.5791 1.0943 0.4792 -0.1714 -0.0791 -0.1208 173 MET A C 1349 O O . MET A 175 ? 0.5576 1.0656 0.4686 -0.1393 -0.0797 -0.0904 173 MET A O 1350 C CB . MET A 175 ? 0.5828 0.9805 0.4980 -0.1796 -0.0657 -0.1542 173 MET A CB 1351 C CG . MET A 175 ? 0.6140 0.9429 0.5250 -0.1948 -0.0533 -0.1876 173 MET A CG 1352 S SD . MET A 175 ? 0.6578 0.9364 0.5891 -0.1874 -0.0517 -0.1778 173 MET A SD 1353 C CE . MET A 175 ? 0.6286 0.8376 0.5479 -0.2121 -0.0352 -0.2188 173 MET A CE 1354 N N . ARG A 176 ? 0.6041 1.1934 0.4944 -0.1985 -0.0881 -0.1238 174 ARG A N 1355 C CA . ARG A 176 ? 0.5981 1.2696 0.4976 -0.1879 -0.1011 -0.0857 174 ARG A CA 1356 C C . ARG A 176 ? 0.5697 1.2283 0.4973 -0.1677 -0.1029 -0.0621 174 ARG A C 1357 O O . ARG A 176 ? 0.5506 1.2425 0.4926 -0.1397 -0.1073 -0.0242 174 ARG A O 1358 C CB . ARG A 176 ? 0.6238 1.3857 0.5094 -0.2255 -0.1117 -0.0958 174 ARG A CB 1359 C CG . ARG A 176 ? 0.6736 1.4626 0.5272 -0.2511 -0.1103 -0.1209 174 ARG A CG 1360 C CD . ARG A 176 ? 0.7221 1.6143 0.5639 -0.2855 -0.1234 -0.1229 174 ARG A CD 1361 N NE . ARG A 176 ? 0.7884 1.7051 0.5951 -0.3242 -0.1204 -0.1602 174 ARG A NE 1362 C CZ . ARG A 176 ? 0.8226 1.7871 0.6069 -0.3233 -0.1234 -0.1521 174 ARG A CZ 1363 N NH1 . ARG A 176 ? 0.7957 1.7832 0.5888 -0.2842 -0.1288 -0.1059 174 ARG A NH1 1364 N NH2 . ARG A 176 ? 0.8766 1.8617 0.6270 -0.3632 -0.1189 -0.1918 174 ARG A NH2 1365 N N . SER A 177 ? 0.5775 1.1867 0.5118 -0.1818 -0.0977 -0.0842 175 SER A N 1366 C CA . SER A 177 ? 0.5667 1.1599 0.5253 -0.1669 -0.0976 -0.0663 175 SER A CA 1367 C C . SER A 177 ? 0.5327 1.0858 0.5051 -0.1238 -0.0929 -0.0377 175 SER A C 1368 O O . SER A 177 ? 0.5356 1.1190 0.5253 -0.1027 -0.0954 -0.0073 175 SER A O 1369 C CB . SER A 177 ? 0.5818 1.1119 0.5404 -0.1886 -0.0899 -0.0961 175 SER A CB 1370 O OG . SER A 177 ? 0.6277 1.1784 0.5688 -0.2321 -0.0896 -0.1292 175 SER A OG 1371 N N . GLY A 178 ? 0.5249 1.0101 0.4901 -0.1116 -0.0846 -0.0487 176 GLY A N 1372 C CA . GLY A 178 ? 0.4933 0.9378 0.4683 -0.0764 -0.0789 -0.0264 176 GLY A CA 1373 C C . GLY A 178 ? 0.4713 0.8634 0.4605 -0.0653 -0.0739 -0.0247 176 GLY A C 1374 O O . GLY A 178 ? 0.4791 0.8095 0.4652 -0.0653 -0.0681 -0.0423 176 GLY A O 1375 N N . LYS A 179 ? 0.4262 0.8456 0.4312 -0.0544 -0.0754 -0.0023 177 LYS A N 1376 C CA . LYS A 179 ? 0.3928 0.7640 0.4088 -0.0390 -0.0689 0.0035 177 LYS A CA 1377 C C . LYS A 179 ? 0.3607 0.7466 0.3873 -0.0543 -0.0705 0.0007 177 LYS A C 1378 O O . LYS A 179 ? 0.3421 0.7913 0.3789 -0.0582 -0.0752 0.0144 177 LYS A O 1379 C CB . LYS A 179 ? 0.3876 0.7597 0.4124 -0.0066 -0.0629 0.0327 177 LYS A CB 1380 C CG . LYS A 179 ? 0.3989 0.7244 0.4315 0.0060 -0.0551 0.0356 177 LYS A CG 1381 C CD . LYS A 179 ? 0.4366 0.7400 0.4716 0.0357 -0.0447 0.0559 177 LYS A CD 1382 C CE . LYS A 179 ? 0.4553 0.8065 0.5049 0.0544 -0.0410 0.0841 177 LYS A CE 1383 N NZ . LYS A 179 ? 0.4972 0.8148 0.5471 0.0840 -0.0263 0.1026 177 LYS A NZ 1384 N N . PHE A 180 ? 0.3326 0.6633 0.3574 -0.0624 -0.0665 -0.0150 178 PHE A N 1385 C CA . PHE A 180 ? 0.3228 0.6597 0.3568 -0.0764 -0.0658 -0.0154 178 PHE A CA 1386 C C . PHE A 180 ? 0.2895 0.5852 0.3298 -0.0550 -0.0587 -0.0033 178 PHE A C 1387 O O . PHE A 180 ? 0.2547 0.4949 0.2874 -0.0442 -0.0550 -0.0091 178 PHE A O 1388 C CB . PHE A 180 ? 0.3540 0.6622 0.3783 -0.1082 -0.0651 -0.0426 178 PHE A CB 1389 C CG . PHE A 180 ? 0.3789 0.6817 0.4105 -0.1236 -0.0621 -0.0423 178 PHE A CG 1390 C CD1 . PHE A 180 ? 0.4001 0.7659 0.4403 -0.1450 -0.0657 -0.0393 178 PHE A CD1 1391 C CD2 . PHE A 180 ? 0.4239 0.6634 0.4538 -0.1165 -0.0556 -0.0427 178 PHE A CD2 1392 C CE1 . PHE A 180 ? 0.4223 0.7859 0.4696 -0.1610 -0.0617 -0.0383 178 PHE A CE1 1393 C CE2 . PHE A 180 ? 0.4163 0.6518 0.4511 -0.1316 -0.0518 -0.0403 178 PHE A CE2 1394 C CZ . PHE A 180 ? 0.4089 0.7054 0.4525 -0.1542 -0.0543 -0.0385 178 PHE A CZ 1395 N N . GLN A 181 ? 0.2673 0.5961 0.3214 -0.0496 -0.0565 0.0132 179 GLN A N 1396 C CA . GLN A 181 ? 0.2598 0.5552 0.3179 -0.0340 -0.0483 0.0224 179 GLN A CA 1397 C C . GLN A 181 ? 0.2509 0.5483 0.3131 -0.0549 -0.0469 0.0179 179 GLN A C 1398 O O . GLN A 181 ? 0.2548 0.5993 0.3241 -0.0758 -0.0509 0.0159 179 GLN A O 1399 C CB . GLN A 181 ? 0.2551 0.5802 0.3255 -0.0059 -0.0418 0.0462 179 GLN A CB 1400 C CG . GLN A 181 ? 0.2624 0.5766 0.3273 0.0163 -0.0397 0.0539 179 GLN A CG 1401 C CD . GLN A 181 ? 0.3258 0.6850 0.4048 0.0407 -0.0340 0.0798 179 GLN A CD 1402 O OE1 . GLN A 181 ? 0.3627 0.7873 0.4517 0.0372 -0.0408 0.0905 179 GLN A OE1 1403 N NE2 . GLN A 181 ? 0.3574 0.6841 0.4372 0.0658 -0.0204 0.0906 179 GLN A NE2 1404 N N . SER A 182 ? 0.2534 0.5013 0.3100 -0.0507 -0.0411 0.0169 180 SER A N 1405 C CA . SER A 182 ? 0.2618 0.5020 0.3192 -0.0697 -0.0379 0.0149 180 SER A CA 1406 C C . SER A 182 ? 0.2494 0.5549 0.3238 -0.0773 -0.0361 0.0265 180 SER A C 1407 O O . SER A 182 ? 0.2519 0.5921 0.3383 -0.0550 -0.0320 0.0426 180 SER A O 1408 C CB . SER A 182 ? 0.2583 0.4496 0.3075 -0.0562 -0.0314 0.0198 180 SER A CB 1409 O OG . SER A 182 ? 0.2939 0.4829 0.3435 -0.0722 -0.0269 0.0226 180 SER A OG 1410 N N . LEU A 183 ? 0.2565 0.5784 0.3326 -0.1089 -0.0374 0.0182 181 LEU A N 1411 C CA . LEU A 183 ? 0.2626 0.6518 0.3567 -0.1212 -0.0353 0.0284 181 LEU A CA 1412 C C . LEU A 183 ? 0.2788 0.6415 0.3702 -0.1334 -0.0264 0.0306 181 LEU A C 1413 O O . LEU A 183 ? 0.2999 0.7120 0.4048 -0.1501 -0.0231 0.0363 181 LEU A O 1414 C CB . LEU A 183 ? 0.2626 0.7052 0.3612 -0.1546 -0.0430 0.0171 181 LEU A CB 1415 C CG . LEU A 183 ? 0.2603 0.7467 0.3609 -0.1474 -0.0526 0.0169 181 LEU A CG 1416 C CD1 . LEU A 183 ? 0.2572 0.7887 0.3556 -0.1884 -0.0597 -0.0001 181 LEU A CD1 1417 C CD2 . LEU A 183 ? 0.2378 0.7890 0.3595 -0.1147 -0.0524 0.0437 181 LEU A CD2 1418 N N . GLY A 184 ? 0.2930 0.5838 0.3677 -0.1243 -0.0228 0.0278 182 GLY A N 1419 C CA . GLY A 184 ? 0.3211 0.5780 0.3879 -0.1334 -0.0149 0.0319 182 GLY A CA 1420 C C . GLY A 184 ? 0.3229 0.5660 0.3865 -0.1030 -0.0083 0.0443 182 GLY A C 1421 O O . GLY A 184 ? 0.3186 0.6057 0.3959 -0.0848 -0.0037 0.0543 182 GLY A O 1422 N N . ARG A 185 ? 0.3423 0.5260 0.3878 -0.0966 -0.0068 0.0437 183 ARG A N 1423 C CA . ARG A 185 ? 0.3406 0.5157 0.3797 -0.0759 0.0009 0.0529 183 ARG A CA 1424 C C . ARG A 185 ? 0.3110 0.4940 0.3535 -0.0472 0.0026 0.0540 183 ARG A C 1425 O O . ARG A 185 ? 0.3194 0.5096 0.3610 -0.0317 0.0129 0.0604 183 ARG A O 1426 C CB . ARG A 185 ? 0.3692 0.4886 0.3871 -0.0777 0.0010 0.0539 183 ARG A CB 1427 C CG . ARG A 185 ? 0.3854 0.4636 0.3923 -0.0638 -0.0062 0.0476 183 ARG A CG 1428 C CD . ARG A 185 ? 0.4250 0.4657 0.4123 -0.0607 -0.0049 0.0541 183 ARG A CD 1429 N NE . ARG A 185 ? 0.4857 0.5004 0.4674 -0.0797 -0.0057 0.0585 183 ARG A NE 1430 C CZ . ARG A 185 ? 0.5582 0.5631 0.5288 -0.0897 -0.0001 0.0705 183 ARG A CZ 1431 N NH1 . ARG A 185 ? 0.5901 0.6118 0.5519 -0.0832 0.0065 0.0780 183 ARG A NH1 1432 N NH2 . ARG A 185 ? 0.5763 0.5506 0.5425 -0.1070 0.0007 0.0750 183 ARG A NH2 1433 N N . PHE A 186 ? 0.2933 0.4724 0.3381 -0.0411 -0.0055 0.0474 184 PHE A N 1434 C CA . PHE A 186 ? 0.2750 0.4546 0.3211 -0.0156 -0.0030 0.0492 184 PHE A CA 1435 C C . PHE A 186 ? 0.2555 0.4913 0.3217 -0.0065 -0.0020 0.0575 184 PHE A C 1436 O O . PHE A 186 ? 0.2453 0.4817 0.3134 0.0136 -0.0001 0.0610 184 PHE A O 1437 C CB . PHE A 186 ? 0.2786 0.4172 0.3129 -0.0126 -0.0115 0.0388 184 PHE A CB 1438 C CG . PHE A 186 ? 0.2899 0.3803 0.3070 -0.0164 -0.0130 0.0344 184 PHE A CG 1439 C CD1 . PHE A 186 ? 0.3128 0.3853 0.3184 -0.0046 -0.0061 0.0370 184 PHE A CD1 1440 C CD2 . PHE A 186 ? 0.3150 0.3804 0.3272 -0.0318 -0.0201 0.0285 184 PHE A CD2 1441 C CE1 . PHE A 186 ? 0.3304 0.3695 0.3201 -0.0084 -0.0090 0.0357 184 PHE A CE1 1442 C CE2 . PHE A 186 ? 0.3474 0.3746 0.3461 -0.0317 -0.0215 0.0294 184 PHE A CE2 1443 C CZ . PHE A 186 ? 0.3516 0.3700 0.3391 -0.0200 -0.0173 0.0341 184 PHE A CZ 1444 N N . ARG A 187 ? 0.2679 0.5539 0.3493 -0.0215 -0.0029 0.0622 185 ARG A N 1445 C CA . ARG A 187 ? 0.2654 0.6168 0.3677 -0.0141 -0.0049 0.0723 185 ARG A CA 1446 C C . ARG A 187 ? 0.2676 0.6324 0.3796 0.0205 0.0085 0.0877 185 ARG A C 1447 O O . ARG A 187 ? 0.2575 0.6127 0.3691 0.0302 0.0220 0.0918 185 ARG A O 1448 C CB . ARG A 187 ? 0.2730 0.6845 0.3914 -0.0385 -0.0071 0.0751 185 ARG A CB 1449 C CG . ARG A 187 ? 0.2797 0.7722 0.4211 -0.0325 -0.0117 0.0874 185 ARG A CG 1450 C CD . ARG A 187 ? 0.3219 0.8735 0.4754 -0.0666 -0.0178 0.0841 185 ARG A CD 1451 N NE . ARG A 187 ? 0.3732 0.9428 0.5368 -0.0725 -0.0069 0.0905 185 ARG A NE 1452 C CZ . ARG A 187 ? 0.4229 1.0522 0.6106 -0.0522 0.0027 0.1090 185 ARG A CZ 1453 N NH1 . ARG A 187 ? 0.4212 1.0990 0.6270 -0.0222 0.0028 0.1259 185 ARG A NH1 1454 N NH2 . ARG A 187 ? 0.4499 1.0925 0.6443 -0.0612 0.0136 0.1122 185 ARG A NH2 1455 N N . ASN A 188 ? 0.2651 0.6471 0.3834 0.0388 0.0062 0.0957 186 ASN A N 1456 C CA . ASN A 188 ? 0.2818 0.6701 0.4093 0.0741 0.0206 0.1121 186 ASN A CA 1457 C C . ASN A 188 ? 0.3020 0.6196 0.4103 0.0903 0.0338 0.1056 186 ASN A C 1458 O O . ASN A 188 ? 0.3207 0.6324 0.4339 0.1183 0.0499 0.1167 186 ASN A O 1459 C CB . ASN A 188 ? 0.2819 0.7307 0.4344 0.0861 0.0317 0.1289 186 ASN A CB 1460 C CG . ASN A 188 ? 0.2795 0.8133 0.4548 0.0749 0.0197 0.1397 186 ASN A CG 1461 O OD1 . ASN A 188 ? 0.3126 0.8973 0.5044 0.0630 0.0213 0.1438 186 ASN A OD1 1462 N ND2 . ASN A 188 ? 0.2699 0.8251 0.4458 0.0770 0.0080 0.1445 186 ASN A ND2 1463 N N . ARG A 189 ? 0.3113 0.5761 0.3978 0.0730 0.0281 0.0880 187 ARG A N 1464 C CA . ARG A 189 ? 0.3248 0.5297 0.3915 0.0828 0.0388 0.0797 187 ARG A CA 1465 C C . ARG A 189 ? 0.3264 0.4901 0.3775 0.0793 0.0300 0.0691 187 ARG A C 1466 O O . ARG A 189 ? 0.3497 0.4678 0.3839 0.0838 0.0377 0.0608 187 ARG A O 1467 C CB . ARG A 189 ? 0.3309 0.5144 0.3845 0.0676 0.0412 0.0706 187 ARG A CB 1468 C CG . ARG A 189 ? 0.3505 0.5731 0.4180 0.0711 0.0534 0.0801 187 ARG A CG 1469 C CD . ARG A 189 ? 0.3602 0.5572 0.4100 0.0599 0.0601 0.0725 187 ARG A CD 1470 N NE . ARG A 189 ? 0.3622 0.5476 0.4020 0.0329 0.0449 0.0665 187 ARG A NE 1471 C CZ . ARG A 189 ? 0.3711 0.5123 0.3877 0.0233 0.0402 0.0578 187 ARG A CZ 1472 N NH1 . ARG A 189 ? 0.4059 0.5129 0.4048 0.0337 0.0473 0.0507 187 ARG A NH1 1473 N NH2 . ARG A 189 ? 0.3769 0.5091 0.3879 0.0025 0.0288 0.0568 187 ARG A NH2 1474 N N . VAL A 190 ? 0.3144 0.4954 0.3697 0.0687 0.0148 0.0673 188 VAL A N 1475 C CA A VAL A 190 ? 0.3104 0.4577 0.3528 0.0650 0.0070 0.0568 188 VAL A CA 1476 C CA B VAL A 190 ? 0.3114 0.4586 0.3537 0.0650 0.0071 0.0568 188 VAL A CA 1477 C C . VAL A 190 ? 0.3085 0.4805 0.3581 0.0753 0.0044 0.0660 188 VAL A C 1478 O O . VAL A 190 ? 0.3134 0.5362 0.3771 0.0741 -0.0007 0.0759 188 VAL A O 1479 C CB A VAL A 190 ? 0.3052 0.4370 0.3401 0.0415 -0.0074 0.0420 188 VAL A CB 1480 C CB B VAL A 190 ? 0.3065 0.4392 0.3417 0.0414 -0.0071 0.0423 188 VAL A CB 1481 C CG1 A VAL A 190 ? 0.2957 0.3880 0.3166 0.0363 -0.0052 0.0344 188 VAL A CG1 1482 C CG1 B VAL A 190 ? 0.2997 0.4746 0.3463 0.0254 -0.0170 0.0425 188 VAL A CG1 1483 C CG2 A VAL A 190 ? 0.3009 0.4720 0.3470 0.0235 -0.0152 0.0427 188 VAL A CG2 1484 C CG2 B VAL A 190 ? 0.2930 0.3913 0.3166 0.0407 -0.0124 0.0314 188 VAL A CG2 1485 N N . ASP A 191 ? 0.3216 0.4608 0.3607 0.0839 0.0083 0.0635 189 ASP A N 1486 C CA . ASP A 191 ? 0.3159 0.4730 0.3571 0.0902 0.0049 0.0713 189 ASP A CA 1487 C C . ASP A 191 ? 0.3131 0.4279 0.3390 0.0864 0.0041 0.0592 189 ASP A C 1488 O O . ASP A 191 ? 0.2955 0.3692 0.3105 0.0832 0.0086 0.0478 189 ASP A O 1489 C CB . ASP A 191 ? 0.3480 0.5284 0.4004 0.1161 0.0180 0.0954 189 ASP A CB 1490 C CG . ASP A 191 ? 0.3715 0.6051 0.4325 0.1197 0.0090 0.1110 189 ASP A CG 1491 O OD1 . ASP A 191 ? 0.3782 0.6162 0.4307 0.1031 -0.0039 0.0999 189 ASP A OD1 1492 O OD2 . ASP A 191 ? 0.4323 0.7062 0.5085 0.1403 0.0157 0.1352 189 ASP A OD2 1493 N N . LEU A 192 ? 0.3155 0.4475 0.3404 0.0842 -0.0027 0.0611 190 LEU A N 1494 C CA . LEU A 192 ? 0.3271 0.4282 0.3400 0.0805 -0.0026 0.0512 190 LEU A CA 1495 C C . LEU A 192 ? 0.3492 0.4208 0.3563 0.0974 0.0145 0.0623 190 LEU A C 1496 O O . LEU A 192 ? 0.3742 0.4620 0.3875 0.1149 0.0236 0.0828 190 LEU A O 1497 C CB . LEU A 192 ? 0.3248 0.4592 0.3376 0.0733 -0.0127 0.0516 190 LEU A CB 1498 C CG . LEU A 192 ? 0.3416 0.4627 0.3454 0.0608 -0.0188 0.0347 190 LEU A CG 1499 C CD1 . LEU A 192 ? 0.2748 0.3626 0.2758 0.0498 -0.0226 0.0143 190 LEU A CD1 1500 C CD2 . LEU A 192 ? 0.3548 0.5220 0.3597 0.0499 -0.0292 0.0333 190 LEU A CD2 1501 N N . THR A 193 ? 0.3553 0.3835 0.3509 0.0925 0.0208 0.0496 191 THR A N 1502 C CA . THR A 193 ? 0.3713 0.3662 0.3582 0.1032 0.0388 0.0570 191 THR A CA 1503 C C . THR A 193 ? 0.3583 0.3440 0.3369 0.0949 0.0368 0.0520 191 THR A C 1504 O O . THR A 193 ? 0.3695 0.3344 0.3415 0.1027 0.0511 0.0623 191 THR A O 1505 C CB . THR A 193 ? 0.3759 0.3281 0.3523 0.0997 0.0511 0.0446 191 THR A CB 1506 O OG1 . THR A 193 ? 0.3664 0.3135 0.3377 0.0811 0.0384 0.0248 191 THR A OG1 1507 C CG2 . THR A 193 ? 0.4233 0.3795 0.4055 0.1108 0.0598 0.0511 191 THR A CG2 1508 N N . GLY A 194 ? 0.3289 0.3265 0.3078 0.0793 0.0216 0.0360 192 GLY A N 1509 C CA . GLY A 194 ? 0.3366 0.3332 0.3100 0.0710 0.0193 0.0297 192 GLY A CA 1510 C C . GLY A 194 ? 0.3418 0.3712 0.3164 0.0762 0.0166 0.0442 192 GLY A C 1511 O O . GLY A 194 ? 0.3404 0.4044 0.3224 0.0807 0.0095 0.0533 192 GLY A O 1512 N N . ASP A 195 ? 0.3545 0.3760 0.3209 0.0739 0.0230 0.0469 193 ASP A N 1513 C CA . ASP A 195 ? 0.3526 0.4078 0.3160 0.0746 0.0192 0.0579 193 ASP A CA 1514 C C . ASP A 195 ? 0.3242 0.3958 0.2876 0.0577 0.0070 0.0349 193 ASP A C 1515 O O . ASP A 195 ? 0.2922 0.3447 0.2529 0.0489 0.0097 0.0207 193 ASP A O 1516 C CB . ASP A 195 ? 0.3827 0.4153 0.3356 0.0805 0.0356 0.0738 193 ASP A CB 1517 C CG . ASP A 195 ? 0.4224 0.4912 0.3695 0.0836 0.0336 0.0915 193 ASP A CG 1518 O OD1 . ASP A 195 ? 0.4560 0.5698 0.4051 0.0766 0.0189 0.0857 193 ASP A OD1 1519 O OD2 . ASP A 195 ? 0.4777 0.5282 0.4161 0.0921 0.0484 0.1117 193 ASP A OD2 1520 N N . ILE A 196 ? 0.3198 0.4281 0.2873 0.0529 -0.0054 0.0303 194 ILE A N 1521 C CA . ILE A 196 ? 0.3036 0.4224 0.2711 0.0384 -0.0140 0.0069 194 ILE A CA 1522 C C . ILE A 196 ? 0.2962 0.4254 0.2541 0.0331 -0.0097 0.0048 194 ILE A C 1523 O O . ILE A 196 ? 0.2858 0.4095 0.2446 0.0246 -0.0103 -0.0146 194 ILE A O 1524 C CB . ILE A 196 ? 0.3109 0.4635 0.2814 0.0306 -0.0251 0.0007 194 ILE A CB 1525 C CG1 . ILE A 196 ? 0.3143 0.4564 0.2947 0.0335 -0.0283 0.0019 194 ILE A CG1 1526 C CG2 . ILE A 196 ? 0.3220 0.4782 0.2904 0.0157 -0.0296 -0.0260 194 ILE A CG2 1527 C CD1 . ILE A 196 ? 0.3479 0.4580 0.3331 0.0280 -0.0305 -0.0172 194 ILE A CD1 1528 N N . SER A 197 ? 0.3070 0.4509 0.2564 0.0398 -0.0037 0.0272 195 SER A N 1529 C CA . SER A 197 ? 0.3201 0.4745 0.2582 0.0344 0.0020 0.0292 195 SER A CA 1530 C C . SER A 197 ? 0.3146 0.4316 0.2522 0.0315 0.0128 0.0228 195 SER A C 1531 O O . SER A 197 ? 0.3106 0.4349 0.2414 0.0235 0.0177 0.0182 195 SER A O 1532 C CB . SER A 197 ? 0.3573 0.5397 0.2853 0.0439 0.0056 0.0602 195 SER A CB 1533 O OG . SER A 197 ? 0.4079 0.5577 0.3356 0.0592 0.0190 0.0845 195 SER A OG 1534 N N . ARG A 198 ? 0.3180 0.3987 0.2623 0.0357 0.0168 0.0211 196 ARG A N 1535 C CA . ARG A 198 ? 0.3230 0.3721 0.2672 0.0286 0.0257 0.0115 196 ARG A CA 1536 C C . ARG A 198 ? 0.3038 0.3461 0.2599 0.0231 0.0171 -0.0112 196 ARG A C 1537 O O . ARG A 198 ? 0.2983 0.3176 0.2560 0.0181 0.0218 -0.0180 196 ARG A O 1538 C CB . ARG A 198 ? 0.3513 0.3629 0.2892 0.0357 0.0405 0.0286 196 ARG A CB 1539 C CG . ARG A 198 ? 0.3888 0.4000 0.3150 0.0434 0.0526 0.0551 196 ARG A CG 1540 C CD . ARG A 198 ? 0.4201 0.4338 0.3374 0.0300 0.0601 0.0521 196 ARG A CD 1541 N NE . ARG A 198 ? 0.4560 0.4757 0.3605 0.0380 0.0700 0.0808 196 ARG A NE 1542 C CZ . ARG A 198 ? 0.4913 0.5148 0.3846 0.0279 0.0790 0.0857 196 ARG A CZ 1543 N NH1 . ARG A 198 ? 0.4955 0.5203 0.3909 0.0091 0.0797 0.0624 196 ARG A NH1 1544 N NH2 . ARG A 198 ? 0.5439 0.5745 0.4246 0.0372 0.0874 0.1160 196 ARG A NH2 1545 N N . ASN A 199 ? 0.2876 0.3507 0.2507 0.0237 0.0051 -0.0213 197 ASN A N 1546 C CA . ASN A 199 ? 0.2698 0.3309 0.2443 0.0208 -0.0029 -0.0402 197 ASN A CA 1547 C C . ASN A 199 ? 0.2696 0.3085 0.2487 0.0247 -0.0059 -0.0389 197 ASN A C 1548 O O . ASN A 199 ? 0.2742 0.3069 0.2611 0.0226 -0.0097 -0.0500 197 ASN A O 1549 C CB . ASN A 199 ? 0.2729 0.3378 0.2524 0.0141 0.0004 -0.0536 197 ASN A CB 1550 C CG . ASN A 199 ? 0.2812 0.3690 0.2546 0.0091 0.0055 -0.0556 197 ASN A CG 1551 O OD1 . ASN A 199 ? 0.3153 0.4224 0.2870 0.0087 0.0015 -0.0622 197 ASN A OD1 1552 N ND2 . ASN A 199 ? 0.2383 0.3240 0.2063 0.0028 0.0156 -0.0508 197 ASN A ND2 1553 N N . ASP A 200 ? 0.2684 0.3009 0.2434 0.0313 -0.0041 -0.0245 198 ASP A N 1554 C CA . ASP A 200 ? 0.2681 0.2797 0.2443 0.0347 -0.0033 -0.0221 198 ASP A CA 1555 C C . ASP A 200 ? 0.2614 0.2843 0.2424 0.0394 -0.0107 -0.0173 198 ASP A C 1556 O O . ASP A 200 ? 0.2547 0.2953 0.2347 0.0449 -0.0097 -0.0042 198 ASP A O 1557 C CB . ASP A 200 ? 0.2897 0.2785 0.2565 0.0383 0.0112 -0.0098 198 ASP A CB 1558 C CG . ASP A 200 ? 0.3183 0.2824 0.2826 0.0399 0.0159 -0.0104 198 ASP A CG 1559 O OD1 . ASP A 200 ? 0.3305 0.2994 0.3004 0.0394 0.0064 -0.0165 198 ASP A OD1 1560 O OD2 . ASP A 200 ? 0.3743 0.3119 0.3294 0.0411 0.0309 -0.0045 198 ASP A OD2 1561 N N . GLY A 201 ? 0.2517 0.2679 0.2383 0.0368 -0.0179 -0.0265 199 GLY A N 1562 C CA . GLY A 201 ? 0.2516 0.2761 0.2426 0.0372 -0.0240 -0.0239 199 GLY A CA 1563 C C . GLY A 201 ? 0.2516 0.2618 0.2417 0.0410 -0.0211 -0.0173 199 GLY A C 1564 O O . GLY A 201 ? 0.2503 0.2647 0.2444 0.0390 -0.0260 -0.0168 199 GLY A O 1565 N N . SER A 202 ? 0.2796 0.2723 0.2629 0.0450 -0.0109 -0.0127 200 SER A N 1566 C CA . SER A 202 ? 0.2779 0.2538 0.2568 0.0471 -0.0053 -0.0103 200 SER A CA 1567 C C . SER A 202 ? 0.2794 0.2690 0.2632 0.0552 -0.0025 0.0024 200 SER A C 1568 O O . SER A 202 ? 0.2783 0.2868 0.2666 0.0628 0.0002 0.0141 200 SER A O 1569 C CB . SER A 202 ? 0.3014 0.2520 0.2693 0.0469 0.0086 -0.0114 200 SER A CB 1570 O OG . SER A 202 ? 0.2953 0.2419 0.2606 0.0364 0.0048 -0.0238 200 SER A OG 1571 N N . ILE A 203 ? 0.2792 0.2653 0.2630 0.0533 -0.0037 0.0015 201 ILE A N 1572 C CA . ILE A 203 ? 0.2855 0.2874 0.2754 0.0600 0.0006 0.0127 201 ILE A CA 1573 C C . ILE A 203 ? 0.3090 0.2911 0.2911 0.0655 0.0144 0.0143 201 ILE A C 1574 O O . ILE A 203 ? 0.3136 0.2712 0.2835 0.0592 0.0176 0.0042 201 ILE A O 1575 C CB . ILE A 203 ? 0.2666 0.2882 0.2642 0.0504 -0.0114 0.0108 201 ILE A CB 1576 C CG1 . ILE A 203 ? 0.2780 0.2794 0.2693 0.0411 -0.0173 0.0015 201 ILE A CG1 1577 C CG2 . ILE A 203 ? 0.2656 0.3084 0.2692 0.0448 -0.0206 0.0080 201 ILE A CG2 1578 C CD1 . ILE A 203 ? 0.2420 0.2535 0.2386 0.0322 -0.0238 0.0029 201 ILE A CD1 1579 N N . LYS A 204 ? 0.3289 0.3260 0.3184 0.0770 0.0234 0.0268 202 LYS A N 1580 C CA . LYS A 204 ? 0.3688 0.3511 0.3525 0.0833 0.0389 0.0278 202 LYS A CA 1581 C C . LYS A 204 ? 0.3626 0.3707 0.3542 0.0790 0.0338 0.0313 202 LYS A C 1582 O O . LYS A 204 ? 0.3658 0.4088 0.3721 0.0785 0.0252 0.0396 202 LYS A O 1583 C CB . LYS A 204 ? 0.3934 0.3713 0.3815 0.1039 0.0578 0.0412 202 LYS A CB 1584 C CG . LYS A 204 ? 0.4658 0.4312 0.4510 0.1141 0.0771 0.0430 202 LYS A CG 1585 C CD . LYS A 204 ? 0.5274 0.4790 0.5168 0.1375 0.0989 0.0569 202 LYS A CD 1586 C CE . LYS A 204 ? 0.5280 0.5274 0.5405 0.1547 0.0943 0.0804 202 LYS A CE 1587 N NZ . LYS A 204 ? 0.6164 0.6012 0.6345 0.1830 0.1206 0.0967 202 LYS A NZ 1588 N N . LEU A 205 ? 0.3695 0.3623 0.3494 0.0725 0.0386 0.0241 203 LEU A N 1589 C CA . LEU A 205 ? 0.3637 0.3768 0.3478 0.0676 0.0379 0.0282 203 LEU A CA 1590 C C . LEU A 205 ? 0.3910 0.3975 0.3703 0.0788 0.0594 0.0299 203 LEU A C 1591 O O . LEU A 205 ? 0.4109 0.3858 0.3710 0.0762 0.0697 0.0188 203 LEU A O 1592 C CB . LEU A 205 ? 0.3506 0.3528 0.3227 0.0503 0.0259 0.0202 203 LEU A CB 1593 C CG . LEU A 205 ? 0.3711 0.3890 0.3437 0.0418 0.0252 0.0252 203 LEU A CG 1594 C CD1 . LEU A 205 ? 0.3430 0.3976 0.3365 0.0399 0.0210 0.0352 203 LEU A CD1 1595 C CD2 . LEU A 205 ? 0.3519 0.3543 0.3112 0.0273 0.0131 0.0212 203 LEU A CD2 1596 N N . GLN A 206 ? 0.3977 0.4367 0.3947 0.0905 0.0671 0.0428 204 GLN A N 1597 C CA . GLN A 206 ? 0.4407 0.4769 0.4381 0.1064 0.0910 0.0462 204 GLN A CA 1598 C C . GLN A 206 ? 0.4382 0.4896 0.4319 0.0970 0.0948 0.0443 204 GLN A C 1599 O O . GLN A 206 ? 0.4221 0.4978 0.4210 0.0814 0.0793 0.0471 204 GLN A O 1600 C CB . GLN A 206 ? 0.4535 0.5232 0.4761 0.1300 0.0995 0.0653 204 GLN A CB 1601 C CG . GLN A 206 ? 0.4830 0.5464 0.5105 0.1401 0.0953 0.0725 204 GLN A CG 1602 C CD . GLN A 206 ? 0.5427 0.6427 0.5943 0.1671 0.1056 0.0958 204 GLN A CD 1603 O OE1 . GLN A 206 ? 0.6149 0.6898 0.6658 0.1887 0.1230 0.1042 204 GLN A OE1 1604 N NE2 . GLN A 206 ? 0.5544 0.7154 0.6279 0.1659 0.0965 0.1076 204 GLN A NE2 1605 N N . THR A 207 ? 0.4652 0.4994 0.4483 0.1060 0.1179 0.0390 205 THR A N 1606 C CA . THR A 207 ? 0.4734 0.5219 0.4501 0.0987 0.1268 0.0366 205 THR A CA 1607 C C . THR A 207 ? 0.4509 0.5049 0.4160 0.0725 0.1057 0.0335 205 THR A C 1608 O O . THR A 207 ? 0.4341 0.5217 0.4116 0.0638 0.0980 0.0428 205 THR A O 1609 C CB . THR A 207 ? 0.4794 0.5749 0.4843 0.1157 0.1384 0.0526 205 THR A CB 1610 O OG1 . THR A 207 ? 0.5051 0.5949 0.5239 0.1443 0.1554 0.0607 205 THR A OG1 1611 C CG2 . THR A 207 ? 0.4943 0.5981 0.4904 0.1132 0.1567 0.0481 205 THR A CG2 1612 N N . VAL A 208 ? 0.4423 0.4628 0.3840 0.0600 0.0974 0.0213 206 VAL A N 1613 C CA . VAL A 208 ? 0.4332 0.4525 0.3618 0.0395 0.0790 0.0204 206 VAL A CA 1614 C C . VAL A 208 ? 0.4400 0.4762 0.3591 0.0292 0.0850 0.0242 206 VAL A C 1615 O O . VAL A 208 ? 0.4575 0.4921 0.3648 0.0331 0.1050 0.0181 206 VAL A O 1616 C CB . VAL A 208 ? 0.4436 0.4311 0.3485 0.0311 0.0731 0.0070 206 VAL A CB 1617 C CG1 . VAL A 208 ? 0.4284 0.4177 0.3158 0.0134 0.0590 0.0084 206 VAL A CG1 1618 C CG2 . VAL A 208 ? 0.4373 0.4147 0.3543 0.0362 0.0613 0.0063 206 VAL A CG2 1619 N N . LYS A 209 ? 0.4378 0.4875 0.3615 0.0155 0.0694 0.0340 207 LYS A N 1620 C CA . LYS A 209 ? 0.4566 0.5212 0.3703 0.0018 0.0722 0.0413 207 LYS A CA 1621 C C . LYS A 209 ? 0.4607 0.5064 0.3519 -0.0131 0.0571 0.0435 207 LYS A C 1622 O O . LYS A 209 ? 0.4503 0.4783 0.3421 -0.0126 0.0420 0.0415 207 LYS A O 1623 C CB . LYS A 209 ? 0.4493 0.5428 0.3866 -0.0050 0.0672 0.0540 207 LYS A CB 1624 C CG . LYS A 209 ? 0.4645 0.5894 0.4312 0.0081 0.0742 0.0573 207 LYS A CG 1625 C CD . LYS A 209 ? 0.4944 0.6471 0.4801 -0.0078 0.0636 0.0670 207 LYS A CD 1626 C CE . LYS A 209 ? 0.5146 0.7197 0.5296 -0.0001 0.0728 0.0742 207 LYS A CE 1627 N NZ . LYS A 209 ? 0.5409 0.7562 0.5732 0.0214 0.0729 0.0740 207 LYS A NZ 1628 N N . GLU A 210 ? 0.4815 0.5346 0.3539 -0.0248 0.0616 0.0494 208 GLU A N 1629 C CA . GLU A 210 ? 0.4977 0.5393 0.3492 -0.0371 0.0477 0.0577 208 GLU A CA 1630 C C . GLU A 210 ? 0.4730 0.5049 0.3402 -0.0413 0.0313 0.0704 208 GLU A C 1631 O O . GLU A 210 ? 0.4692 0.4843 0.3284 -0.0424 0.0173 0.0755 208 GLU A O 1632 C CB . GLU A 210 ? 0.5365 0.5922 0.3655 -0.0495 0.0568 0.0659 208 GLU A CB 1633 C CG . GLU A 210 ? 0.6028 0.6630 0.4039 -0.0505 0.0717 0.0515 208 GLU A CG 1634 C CD . GLU A 210 ? 0.6967 0.7731 0.4702 -0.0655 0.0780 0.0611 208 GLU A CD 1635 O OE1 . GLU A 210 ? 0.7384 0.8139 0.5034 -0.0753 0.0638 0.0806 208 GLU A OE1 1636 O OE2 . GLU A 210 ? 0.7691 0.8578 0.5280 -0.0670 0.0987 0.0498 208 GLU A OE2 1637 N N . SER A 211 ? 0.4561 0.5000 0.3460 -0.0440 0.0342 0.0746 209 SER A N 1638 C CA . SER A 211 ? 0.4529 0.4840 0.3561 -0.0518 0.0224 0.0827 209 SER A CA 1639 C C . SER A 211 ? 0.4174 0.4342 0.3348 -0.0420 0.0115 0.0734 209 SER A C 1640 O O . SER A 211 ? 0.4203 0.4200 0.3453 -0.0473 0.0024 0.0767 209 SER A O 1641 C CB . SER A 211 ? 0.4553 0.5096 0.3758 -0.0641 0.0299 0.0882 209 SER A CB 1642 O OG . SER A 211 ? 0.4582 0.5425 0.3975 -0.0541 0.0381 0.0798 209 SER A OG 1643 N N . ASP A 212 ? 0.4042 0.4252 0.3238 -0.0284 0.0144 0.0613 210 ASP A N 1644 C CA . ASP A 212 ? 0.3790 0.3854 0.3067 -0.0195 0.0044 0.0529 210 ASP A CA 1645 C C . ASP A 212 ? 0.3854 0.3709 0.2982 -0.0180 -0.0064 0.0532 210 ASP A C 1646 O O . ASP A 212 ? 0.3688 0.3440 0.2889 -0.0114 -0.0146 0.0467 210 ASP A O 1647 C CB . ASP A 212 ? 0.3710 0.3854 0.3042 -0.0061 0.0130 0.0421 210 ASP A CB 1648 C CG . ASP A 212 ? 0.3645 0.4062 0.3177 -0.0016 0.0220 0.0444 210 ASP A CG 1649 O OD1 . ASP A 212 ? 0.3861 0.4435 0.3527 -0.0115 0.0178 0.0506 210 ASP A OD1 1650 O OD2 . ASP A 212 ? 0.3488 0.3972 0.3047 0.0120 0.0344 0.0402 210 ASP A OD2 1651 N N . GLN A 213 ? 0.4040 0.3889 0.2962 -0.0238 -0.0063 0.0614 211 GLN A N 1652 C CA . GLN A 213 ? 0.4152 0.3913 0.2947 -0.0220 -0.0179 0.0656 211 GLN A CA 1653 C C . GLN A 213 ? 0.4294 0.3863 0.3213 -0.0193 -0.0295 0.0761 211 GLN A C 1654 O O . GLN A 213 ? 0.4411 0.3872 0.3381 -0.0260 -0.0277 0.0866 211 GLN A O 1655 C CB . GLN A 213 ? 0.4385 0.4253 0.2915 -0.0297 -0.0156 0.0746 211 GLN A CB 1656 C CG . GLN A 213 ? 0.4354 0.4243 0.2754 -0.0278 -0.0293 0.0835 211 GLN A CG 1657 C CD . GLN A 213 ? 0.4312 0.4398 0.2414 -0.0371 -0.0274 0.0889 211 GLN A CD 1658 O OE1 . GLN A 213 ? 0.4223 0.4426 0.2174 -0.0423 -0.0192 0.0720 211 GLN A OE1 1659 N NE2 . GLN A 213 ? 0.4195 0.4303 0.2188 -0.0399 -0.0336 0.1128 211 GLN A NE2 1660 N N . GLY A 214 ? 0.4220 0.3737 0.3189 -0.0102 -0.0393 0.0722 212 GLY A N 1661 C CA . GLY A 214 ? 0.4317 0.3629 0.3433 -0.0042 -0.0465 0.0782 212 GLY A CA 1662 C C . GLY A 214 ? 0.4194 0.3510 0.3432 0.0064 -0.0532 0.0664 212 GLY A C 1663 O O . GLY A 214 ? 0.4039 0.3520 0.3223 0.0080 -0.0542 0.0563 212 GLY A O 1664 N N . ILE A 215 ? 0.4229 0.3346 0.3620 0.0119 -0.0557 0.0670 213 ILE A N 1665 C CA . ILE A 215 ? 0.4132 0.3246 0.3657 0.0224 -0.0607 0.0570 213 ILE A CA 1666 C C . ILE A 215 ? 0.3870 0.2951 0.3513 0.0186 -0.0558 0.0404 213 ILE A C 1667 O O . ILE A 215 ? 0.3909 0.2841 0.3603 0.0111 -0.0512 0.0396 213 ILE A O 1668 C CB . ILE A 215 ? 0.4489 0.3403 0.4103 0.0338 -0.0644 0.0688 213 ILE A CB 1669 C CG1 . ILE A 215 ? 0.4980 0.3988 0.4479 0.0395 -0.0705 0.0905 213 ILE A CG1 1670 C CG2 . ILE A 215 ? 0.4399 0.3368 0.4163 0.0460 -0.0684 0.0583 213 ILE A CG2 1671 C CD1 . ILE A 215 ? 0.5024 0.4404 0.4460 0.0421 -0.0788 0.0875 213 ILE A CD1 1672 N N . TYR A 216 ? 0.3528 0.2770 0.3193 0.0214 -0.0562 0.0278 214 TYR A N 1673 C CA . TYR A 216 ? 0.3314 0.2583 0.3080 0.0204 -0.0530 0.0143 214 TYR A CA 1674 C C . TYR A 216 ? 0.3361 0.2598 0.3232 0.0289 -0.0571 0.0069 214 TYR A C 1675 O O . TYR A 216 ? 0.3488 0.2821 0.3353 0.0356 -0.0616 0.0077 214 TYR A O 1676 C CB . TYR A 216 ? 0.3034 0.2471 0.2749 0.0191 -0.0476 0.0083 214 TYR A CB 1677 C CG . TYR A 216 ? 0.2933 0.2430 0.2581 0.0130 -0.0409 0.0145 214 TYR A CG 1678 C CD1 . TYR A 216 ? 0.3123 0.2621 0.2632 0.0102 -0.0397 0.0226 214 TYR A CD1 1679 C CD2 . TYR A 216 ? 0.2980 0.2585 0.2709 0.0095 -0.0358 0.0135 214 TYR A CD2 1680 C CE1 . TYR A 216 ? 0.3112 0.2684 0.2565 0.0046 -0.0319 0.0279 214 TYR A CE1 1681 C CE2 . TYR A 216 ? 0.3254 0.2974 0.2957 0.0049 -0.0288 0.0201 214 TYR A CE2 1682 C CZ . TYR A 216 ? 0.3222 0.2906 0.2786 0.0027 -0.0260 0.0267 214 TYR A CZ 1683 O OH . TYR A 216 ? 0.3275 0.3094 0.2813 -0.0018 -0.0171 0.0325 214 TYR A OH 1684 N N . THR A 217 ? 0.3447 0.2579 0.3410 0.0272 -0.0549 -0.0009 215 THR A N 1685 C CA . THR A 217 ? 0.3400 0.2494 0.3466 0.0352 -0.0558 -0.0101 215 THR A CA 1686 C C . THR A 217 ? 0.3220 0.2440 0.3317 0.0303 -0.0528 -0.0244 215 THR A C 1687 O O . THR A 217 ? 0.3181 0.2424 0.3264 0.0202 -0.0499 -0.0281 215 THR A O 1688 C CB . THR A 217 ? 0.3751 0.2550 0.3879 0.0379 -0.0528 -0.0088 215 THR A CB 1689 O OG1 . THR A 217 ? 0.3882 0.2556 0.3971 0.0432 -0.0549 0.0093 215 THR A OG1 1690 C CG2 . THR A 217 ? 0.3543 0.2317 0.3792 0.0500 -0.0515 -0.0180 215 THR A CG2 1691 N N . CYS A 218 ? 0.3118 0.2467 0.3253 0.0365 -0.0537 -0.0310 216 CYS A N 1692 C CA . CYS A 218 ? 0.3302 0.2773 0.3454 0.0331 -0.0507 -0.0423 216 CYS A CA 1693 C C . CYS A 218 ? 0.3365 0.2778 0.3607 0.0384 -0.0489 -0.0531 216 CYS A C 1694 O O . CYS A 218 ? 0.3303 0.2731 0.3619 0.0489 -0.0506 -0.0517 216 CYS A O 1695 C CB . CYS A 218 ? 0.3272 0.2907 0.3383 0.0348 -0.0499 -0.0415 216 CYS A CB 1696 S SG . CYS A 218 ? 0.3772 0.3574 0.3880 0.0322 -0.0455 -0.0496 216 CYS A SG 1697 N N . SER A 219 ? 0.3376 0.2747 0.3613 0.0307 -0.0448 -0.0643 217 SER A N 1698 C CA . SER A 219 ? 0.3380 0.2717 0.3675 0.0338 -0.0398 -0.0787 217 SER A CA 1699 C C . SER A 219 ? 0.3287 0.2897 0.3529 0.0277 -0.0390 -0.0856 217 SER A C 1700 O O . SER A 219 ? 0.3265 0.3002 0.3429 0.0163 -0.0394 -0.0862 217 SER A O 1701 C CB . SER A 219 ? 0.3664 0.2739 0.3948 0.0261 -0.0335 -0.0888 217 SER A CB 1702 O OG . SER A 219 ? 0.3891 0.2671 0.4206 0.0320 -0.0330 -0.0778 217 SER A OG 1703 N N . ILE A 220 ? 0.3196 0.2936 0.3486 0.0352 -0.0379 -0.0883 218 ILE A N 1704 C CA . ILE A 220 ? 0.3142 0.3121 0.3374 0.0303 -0.0357 -0.0920 218 ILE A CA 1705 C C . ILE A 220 ? 0.3302 0.3332 0.3579 0.0320 -0.0292 -0.1082 218 ILE A C 1706 O O . ILE A 220 ? 0.3453 0.3454 0.3853 0.0430 -0.0272 -0.1109 218 ILE A O 1707 C CB . ILE A 220 ? 0.2982 0.3062 0.3196 0.0334 -0.0374 -0.0804 218 ILE A CB 1708 C CG1 . ILE A 220 ? 0.3177 0.3445 0.3308 0.0284 -0.0334 -0.0793 218 ILE A CG1 1709 C CG2 . ILE A 220 ? 0.2983 0.3068 0.3303 0.0417 -0.0386 -0.0805 218 ILE A CG2 1710 C CD1 . ILE A 220 ? 0.2976 0.3237 0.3049 0.0292 -0.0315 -0.0669 218 ILE A CD1 1711 N N . TYR A 221 ? 0.3287 0.3433 0.3468 0.0211 -0.0256 -0.1190 219 TYR A N 1712 C CA . TYR A 221 ? 0.3424 0.3579 0.3614 0.0200 -0.0169 -0.1386 219 TYR A CA 1713 C C . TYR A 221 ? 0.3272 0.3731 0.3399 0.0166 -0.0136 -0.1415 219 TYR A C 1714 O O . TYR A 221 ? 0.3086 0.3749 0.3099 0.0091 -0.0170 -0.1315 219 TYR A O 1715 C CB . TYR A 221 ? 0.3676 0.3739 0.3762 0.0052 -0.0129 -0.1542 219 TYR A CB 1716 C CG . TYR A 221 ? 0.3744 0.3446 0.3871 0.0049 -0.0123 -0.1545 219 TYR A CG 1717 C CD1 . TYR A 221 ? 0.3553 0.3226 0.3668 0.0016 -0.0206 -0.1381 219 TYR A CD1 1718 C CD2 . TYR A 221 ? 0.4364 0.3732 0.4536 0.0081 -0.0010 -0.1709 219 TYR A CD2 1719 C CE1 . TYR A 221 ? 0.3895 0.3242 0.4032 -0.0008 -0.0191 -0.1369 219 TYR A CE1 1720 C CE2 . TYR A 221 ? 0.4478 0.3460 0.4672 0.0071 0.0016 -0.1689 219 TYR A CE2 1721 C CZ . TYR A 221 ? 0.4317 0.3308 0.4487 0.0014 -0.0082 -0.1514 219 TYR A CZ 1722 O OH . TYR A 221 ? 0.4957 0.3575 0.5134 -0.0015 -0.0048 -0.1476 219 TYR A OH 1723 N N . VAL A 222 ? 0.3211 0.3706 0.3423 0.0234 -0.0056 -0.1536 220 VAL A N 1724 C CA . VAL A 222 ? 0.3246 0.4023 0.3383 0.0178 0.0007 -0.1606 220 VAL A CA 1725 C C . VAL A 222 ? 0.3583 0.4301 0.3678 0.0131 0.0112 -0.1853 220 VAL A C 1726 O O . VAL A 222 ? 0.3966 0.4549 0.4204 0.0249 0.0198 -0.1967 220 VAL A O 1727 C CB . VAL A 222 ? 0.3018 0.3934 0.3295 0.0275 0.0040 -0.1569 220 VAL A CB 1728 C CG1 . VAL A 222 ? 0.3124 0.4322 0.3315 0.0200 0.0133 -0.1668 220 VAL A CG1 1729 C CG2 . VAL A 222 ? 0.2614 0.3541 0.2904 0.0283 -0.0040 -0.1362 220 VAL A CG2 1730 N N . GLY A 223 ? 0.3846 0.4665 0.3749 -0.0039 0.0115 -0.1940 221 GLY A N 1731 C CA . GLY A 223 ? 0.4283 0.4960 0.4111 -0.0130 0.0230 -0.2218 221 GLY A CA 1732 C C . GLY A 223 ? 0.4515 0.4741 0.4435 -0.0085 0.0249 -0.2266 221 GLY A C 1733 O O . GLY A 223 ? 0.4378 0.4499 0.4312 -0.0102 0.0146 -0.2110 221 GLY A O 1734 N N . LYS A 224 ? 0.4900 0.4837 0.4885 -0.0018 0.0401 -0.2472 222 LYS A N 1735 C CA . LYS A 224 ? 0.5262 0.4708 0.5336 0.0051 0.0447 -0.2487 222 LYS A CA 1736 C C . LYS A 224 ? 0.5053 0.4374 0.5375 0.0320 0.0391 -0.2257 222 LYS A C 1737 O O . LYS A 224 ? 0.5268 0.4196 0.5670 0.0406 0.0419 -0.2210 222 LYS A O 1738 C CB . LYS A 224 ? 0.5868 0.4965 0.5912 0.0040 0.0670 -0.2794 222 LYS A CB 1739 C CG . LYS A 224 ? 0.6395 0.5597 0.6158 -0.0270 0.0752 -0.3084 222 LYS A CG 1740 C CD . LYS A 224 ? 0.6911 0.6133 0.6507 -0.0539 0.0639 -0.3051 222 LYS A CD 1741 C CE . LYS A 224 ? 0.7657 0.6751 0.7006 -0.0849 0.0782 -0.3405 222 LYS A CE 1742 N NZ . LYS A 224 ? 0.8015 0.7190 0.7232 -0.1129 0.0673 -0.3373 222 LYS A NZ 1743 N N . LEU A 225 ? 0.4759 0.4420 0.5191 0.0437 0.0322 -0.2117 223 LEU A N 1744 C CA . LEU A 225 ? 0.4551 0.4205 0.5210 0.0662 0.0263 -0.1919 223 LEU A CA 1745 C C . LEU A 225 ? 0.4192 0.3870 0.4814 0.0618 0.0098 -0.1688 223 LEU A C 1746 O O . LEU A 225 ? 0.3874 0.3806 0.4398 0.0513 0.0016 -0.1609 223 LEU A O 1747 C CB . LEU A 225 ? 0.4403 0.4442 0.5201 0.0769 0.0280 -0.1902 223 LEU A CB 1748 C CG . LEU A 225 ? 0.4873 0.4956 0.5750 0.0852 0.0462 -0.2121 223 LEU A CG 1749 C CD1 . LEU A 225 ? 0.4974 0.5536 0.5889 0.0829 0.0464 -0.2118 223 LEU A CD1 1750 C CD2 . LEU A 225 ? 0.5300 0.5146 0.6429 0.1124 0.0558 -0.2107 223 LEU A CD2 1751 N N . GLU A 226 ? 0.4320 0.3716 0.5024 0.0721 0.0070 -0.1571 224 GLU A N 1752 C CA . GLU A 226 ? 0.4186 0.3566 0.4849 0.0685 -0.0060 -0.1372 224 GLU A CA 1753 C C . GLU A 226 ? 0.4071 0.3658 0.4881 0.0836 -0.0139 -0.1200 224 GLU A C 1754 O O . GLU A 226 ? 0.4113 0.3712 0.5105 0.1023 -0.0100 -0.1177 224 GLU A O 1755 C CB . GLU A 226 ? 0.4562 0.3522 0.5208 0.0688 -0.0033 -0.1337 224 GLU A CB 1756 C CG . GLU A 226 ? 0.4470 0.3426 0.5023 0.0591 -0.0150 -0.1165 224 GLU A CG 1757 C CD . GLU A 226 ? 0.5125 0.3716 0.5711 0.0659 -0.0138 -0.1045 224 GLU A CD 1758 O OE1 . GLU A 226 ? 0.5415 0.3678 0.6060 0.0738 -0.0020 -0.1122 224 GLU A OE1 1759 O OE2 . GLU A 226 ? 0.5457 0.4070 0.6000 0.0633 -0.0228 -0.0872 224 GLU A OE2 1760 N N . SER A 227 ? 0.3761 0.3537 0.4489 0.0749 -0.0240 -0.1086 225 SER A N 1761 C CA . SER A 227 ? 0.3684 0.3607 0.4485 0.0822 -0.0327 -0.0926 225 SER A CA 1762 C C . SER A 227 ? 0.3733 0.3468 0.4420 0.0762 -0.0395 -0.0798 225 SER A C 1763 O O . SER A 227 ? 0.3746 0.3410 0.4293 0.0629 -0.0396 -0.0817 225 SER A O 1764 C CB . SER A 227 ? 0.3543 0.3780 0.4310 0.0736 -0.0348 -0.0933 225 SER A CB 1765 O OG . SER A 227 ? 0.3704 0.4139 0.4569 0.0770 -0.0272 -0.1053 225 SER A OG 1766 N N . ARG A 228 ? 0.3871 0.3578 0.4620 0.0862 -0.0452 -0.0653 226 ARG A N 1767 C CA . ARG A 228 ? 0.3948 0.3476 0.4588 0.0813 -0.0501 -0.0526 226 ARG A CA 1768 C C . ARG A 228 ? 0.3885 0.3627 0.4476 0.0795 -0.0591 -0.0397 226 ARG A C 1769 O O . ARG A 228 ? 0.3905 0.3892 0.4596 0.0879 -0.0636 -0.0343 226 ARG A O 1770 C CB . ARG A 228 ? 0.4263 0.3493 0.4975 0.0931 -0.0465 -0.0458 226 ARG A CB 1771 C CG . ARG A 228 ? 0.4597 0.3581 0.5184 0.0845 -0.0480 -0.0356 226 ARG A CG 1772 C CD . ARG A 228 ? 0.5202 0.3815 0.5855 0.0959 -0.0411 -0.0286 226 ARG A CD 1773 N NE . ARG A 228 ? 0.5276 0.3598 0.5934 0.0907 -0.0285 -0.0476 226 ARG A NE 1774 C CZ . ARG A 228 ? 0.6077 0.4003 0.6803 0.1014 -0.0170 -0.0478 226 ARG A CZ 1775 N NH1 . ARG A 228 ? 0.6392 0.4179 0.7206 0.1213 -0.0174 -0.0256 226 ARG A NH1 1776 N NH2 . ARG A 228 ? 0.6329 0.3986 0.7024 0.0923 -0.0037 -0.0697 226 ARG A NH2 1777 N N . LYS A 229 ? 0.3916 0.3601 0.4352 0.0676 -0.0607 -0.0359 227 LYS A N 1778 C CA . LYS A 229 ? 0.3875 0.3713 0.4216 0.0625 -0.0662 -0.0275 227 LYS A CA 1779 C C . LYS A 229 ? 0.3901 0.3579 0.4134 0.0599 -0.0682 -0.0152 227 LYS A C 1780 O O . LYS A 229 ? 0.3748 0.3253 0.3922 0.0534 -0.0640 -0.0168 227 LYS A O 1781 C CB . LYS A 229 ? 0.3761 0.3673 0.3991 0.0502 -0.0620 -0.0357 227 LYS A CB 1782 C CG . LYS A 229 ? 0.4303 0.4327 0.4405 0.0420 -0.0640 -0.0320 227 LYS A CG 1783 C CD . LYS A 229 ? 0.4878 0.4857 0.4865 0.0319 -0.0555 -0.0392 227 LYS A CD 1784 C CE . LYS A 229 ? 0.5400 0.5494 0.5276 0.0213 -0.0545 -0.0426 227 LYS A CE 1785 N NZ . LYS A 229 ? 0.5969 0.6049 0.5723 0.0184 -0.0577 -0.0354 227 LYS A NZ 1786 N N . THR A 230 ? 0.3916 0.3719 0.4109 0.0625 -0.0748 -0.0029 228 THR A N 1787 C CA . THR A 230 ? 0.4006 0.3696 0.4067 0.0584 -0.0761 0.0099 228 THR A CA 1788 C C . THR A 230 ? 0.3827 0.3676 0.3706 0.0459 -0.0764 0.0084 228 THR A C 1789 O O . THR A 230 ? 0.3813 0.3906 0.3664 0.0425 -0.0801 0.0050 228 THR A O 1790 C CB . THR A 230 ? 0.4321 0.3997 0.4444 0.0715 -0.0817 0.0282 228 THR A CB 1791 O OG1 . THR A 230 ? 0.4581 0.4032 0.4865 0.0832 -0.0768 0.0260 228 THR A OG1 1792 C CG2 . THR A 230 ? 0.4690 0.4214 0.4666 0.0666 -0.0816 0.0435 228 THR A CG2 1793 N N . ILE A 231 ? 0.3628 0.3343 0.3385 0.0378 -0.0707 0.0091 229 ILE A N 1794 C CA . ILE A 231 ? 0.3557 0.3362 0.3126 0.0275 -0.0677 0.0077 229 ILE A CA 1795 C C . ILE A 231 ? 0.3604 0.3354 0.3061 0.0252 -0.0682 0.0219 229 ILE A C 1796 O O . ILE A 231 ? 0.3552 0.3129 0.3049 0.0257 -0.0645 0.0267 229 ILE A O 1797 C CB . ILE A 231 ? 0.3458 0.3176 0.2982 0.0218 -0.0564 -0.0039 229 ILE A CB 1798 C CG1 . ILE A 231 ? 0.3752 0.3518 0.3349 0.0221 -0.0545 -0.0160 229 ILE A CG1 1799 C CG2 . ILE A 231 ? 0.3207 0.2935 0.2530 0.0127 -0.0484 -0.0062 229 ILE A CG2 1800 C CD1 . ILE A 231 ? 0.3482 0.3141 0.3077 0.0217 -0.0438 -0.0219 229 ILE A CD1 1801 N N . VAL A 232 ? 0.3605 0.3533 0.2911 0.0204 -0.0726 0.0284 230 VAL A N 1802 C CA . VAL A 232 ? 0.3769 0.3676 0.2921 0.0157 -0.0713 0.0415 230 VAL A CA 1803 C C . VAL A 232 ? 0.3719 0.3639 0.2688 0.0036 -0.0598 0.0293 230 VAL A C 1804 O O . VAL A 232 ? 0.3715 0.3772 0.2553 -0.0048 -0.0578 0.0175 230 VAL A O 1805 C CB . VAL A 232 ? 0.3945 0.4068 0.3016 0.0183 -0.0825 0.0591 230 VAL A CB 1806 C CG1 . VAL A 232 ? 0.3953 0.4058 0.2834 0.0120 -0.0802 0.0744 230 VAL A CG1 1807 C CG2 . VAL A 232 ? 0.3970 0.4043 0.3261 0.0356 -0.0906 0.0721 230 VAL A CG2 1808 N N . LEU A 233 ? 0.3563 0.3341 0.2538 0.0024 -0.0505 0.0310 231 LEU A N 1809 C CA . LEU A 233 ? 0.3545 0.3325 0.2383 -0.0046 -0.0367 0.0222 231 LEU A CA 1810 C C . LEU A 233 ? 0.3732 0.3613 0.2357 -0.0129 -0.0351 0.0315 231 LEU A C 1811 O O . LEU A 233 ? 0.3694 0.3546 0.2330 -0.0131 -0.0366 0.0468 231 LEU A O 1812 C CB . LEU A 233 ? 0.3520 0.3201 0.2502 -0.0002 -0.0273 0.0205 231 LEU A CB 1813 C CG . LEU A 233 ? 0.3870 0.3551 0.2777 -0.0009 -0.0100 0.0114 231 LEU A CG 1814 C CD1 . LEU A 233 ? 0.3794 0.3390 0.2703 0.0023 -0.0039 -0.0033 231 LEU A CD1 1815 C CD2 . LEU A 233 ? 0.3445 0.3164 0.2517 0.0038 -0.0031 0.0172 231 LEU A CD2 1816 N N . HIS A 234 ? 0.3769 0.3768 0.2176 -0.0222 -0.0312 0.0211 232 HIS A N 1817 C CA . HIS A 234 ? 0.4008 0.4151 0.2160 -0.0327 -0.0287 0.0263 232 HIS A CA 1818 C C . HIS A 234 ? 0.4221 0.4282 0.2256 -0.0375 -0.0076 0.0119 232 HIS A C 1819 O O . HIS A 234 ? 0.4259 0.4247 0.2213 -0.0415 0.0031 -0.0076 232 HIS A O 1820 C CB . HIS A 234 ? 0.4031 0.4421 0.2004 -0.0423 -0.0388 0.0228 232 HIS A CB 1821 C CG . HIS A 234 ? 0.4078 0.4693 0.1755 -0.0548 -0.0390 0.0301 232 HIS A CG 1822 N ND1 . HIS A 234 ? 0.4000 0.4931 0.1452 -0.0685 -0.0466 0.0255 232 HIS A ND1 1823 C CD2 . HIS A 234 ? 0.4272 0.4886 0.1828 -0.0576 -0.0323 0.0420 232 HIS A CD2 1824 C CE1 . HIS A 234 ? 0.4624 0.5740 0.1813 -0.0785 -0.0452 0.0348 232 HIS A CE1 1825 N NE2 . HIS A 234 ? 0.4289 0.5199 0.1535 -0.0717 -0.0361 0.0453 232 HIS A NE2 1826 N N . VAL A 235 ? 0.4543 0.4610 0.2566 -0.0374 -0.0001 0.0220 233 VAL A N 1827 C CA . VAL A 235 ? 0.4719 0.4748 0.2680 -0.0380 0.0217 0.0116 233 VAL A CA 1828 C C . VAL A 235 ? 0.5315 0.5489 0.2943 -0.0521 0.0295 0.0087 233 VAL A C 1829 O O . VAL A 235 ? 0.5444 0.5767 0.2970 -0.0583 0.0220 0.0259 233 VAL A O 1830 C CB . VAL A 235 ? 0.4571 0.4596 0.2766 -0.0299 0.0267 0.0232 233 VAL A CB 1831 C CG1 . VAL A 235 ? 0.4563 0.4606 0.2754 -0.0255 0.0507 0.0134 233 VAL A CG1 1832 C CG2 . VAL A 235 ? 0.3738 0.3666 0.2224 -0.0196 0.0163 0.0260 233 VAL A CG2 1833 N N . VAL A 236 ? 0.5874 0.5984 0.3315 -0.0581 0.0463 -0.0137 234 VAL A N 1834 C CA . VAL A 236 ? 0.6533 0.6781 0.3604 -0.0752 0.0553 -0.0234 234 VAL A CA 1835 C C . VAL A 236 ? 0.7070 0.7214 0.4056 -0.0732 0.0852 -0.0379 234 VAL A C 1836 O O . VAL A 236 ? 0.6906 0.6880 0.4136 -0.0568 0.0985 -0.0401 234 VAL A O 1837 C CB . VAL A 236 ? 0.6734 0.7035 0.3591 -0.0903 0.0488 -0.0405 234 VAL A CB 1838 C CG1 . VAL A 236 ? 0.6327 0.6800 0.3323 -0.0877 0.0199 -0.0226 234 VAL A CG1 1839 C CG2 . VAL A 236 ? 0.6735 0.6729 0.3627 -0.0883 0.0661 -0.0658 234 VAL A CG2 1840 N N . GLN A 237 ? 0.7882 0.8168 0.4526 -0.0890 0.0959 -0.0459 235 GLN A N 1841 C CA . GLN A 237 ? 0.8490 0.8701 0.5019 -0.0875 0.1273 -0.0610 235 GLN A CA 1842 C C . GLN A 237 ? 0.9062 0.9007 0.5353 -0.0958 0.1505 -0.0951 235 GLN A C 1843 O O . GLN A 237 ? 0.9067 0.8901 0.5300 -0.1043 0.1412 -0.1067 235 GLN A O 1844 C CB . GLN A 237 ? 0.8786 0.9297 0.5061 -0.1009 0.1299 -0.0511 235 GLN A CB 1845 C CG . GLN A 237 ? 0.9067 0.9635 0.5494 -0.0893 0.1508 -0.0444 235 GLN A CG 1846 C CD . GLN A 237 ? 0.9112 0.9652 0.6010 -0.0690 0.1422 -0.0246 235 GLN A CD 1847 O OE1 . GLN A 237 ? 0.9279 0.9692 0.6425 -0.0508 0.1586 -0.0315 235 GLN A OE1 1848 N NE2 . GLN A 237 ? 0.8955 0.9618 0.5972 -0.0722 0.1173 0.0003 235 GLN A NE2 1849 N N . ASP A 238 ? 0.9666 0.9512 0.5813 -0.0944 0.1821 -0.1112 236 ASP A N 1850 C CA . ASP A 238 ? 1.0191 0.9641 0.6196 -0.0940 0.2144 -0.1428 236 ASP A CA 1851 C C . ASP A 238 ? 1.0056 0.9149 0.6339 -0.0775 0.2148 -0.1449 236 ASP A C 1852 O O . ASP A 238 ? 0.9826 0.8909 0.6501 -0.0520 0.2113 -0.1250 236 ASP A O 1853 C CB . ASP A 238 ? 1.0786 1.0239 0.6272 -0.1265 0.2235 -0.1724 236 ASP A CB 1854 C CG . ASP A 238 ? 1.0750 1.0299 0.6123 -0.1471 0.1966 -0.1762 236 ASP A CG 1855 O OD1 . ASP A 238 ? 1.0442 0.9756 0.6051 -0.1376 0.1898 -0.1758 236 ASP A OD1 1856 O OD2 . ASP A 238 ? 1.1059 1.0962 0.6096 -0.1733 0.1831 -0.1794 236 ASP A OD2 # 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 10 SER SER 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 ? ? ? A . n A 1 240 PHE 240 238 ? ? ? A . n A 1 241 GLN 241 239 ? ? ? 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 # 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 A ASN 107 A ASN 105 ? ASN 'GLYCOSYLATION SITE' 3 A ASN 61 A ASN 59 ? 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 monomeric _pdbx_struct_assembly.oligomeric_count 1 # _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,K,L,M,N,O # _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_struct_conn_angle.id _pdbx_struct_conn_angle.ptnr1_label_atom_id _pdbx_struct_conn_angle.ptnr1_label_alt_id _pdbx_struct_conn_angle.ptnr1_label_asym_id _pdbx_struct_conn_angle.ptnr1_label_comp_id _pdbx_struct_conn_angle.ptnr1_label_seq_id _pdbx_struct_conn_angle.ptnr1_auth_atom_id _pdbx_struct_conn_angle.ptnr1_auth_asym_id _pdbx_struct_conn_angle.ptnr1_auth_comp_id _pdbx_struct_conn_angle.ptnr1_auth_seq_id _pdbx_struct_conn_angle.ptnr1_PDB_ins_code _pdbx_struct_conn_angle.ptnr1_symmetry _pdbx_struct_conn_angle.ptnr2_label_atom_id _pdbx_struct_conn_angle.ptnr2_label_alt_id _pdbx_struct_conn_angle.ptnr2_label_asym_id _pdbx_struct_conn_angle.ptnr2_label_comp_id _pdbx_struct_conn_angle.ptnr2_label_seq_id _pdbx_struct_conn_angle.ptnr2_auth_atom_id _pdbx_struct_conn_angle.ptnr2_auth_asym_id _pdbx_struct_conn_angle.ptnr2_auth_comp_id _pdbx_struct_conn_angle.ptnr2_auth_seq_id _pdbx_struct_conn_angle.ptnr2_PDB_ins_code _pdbx_struct_conn_angle.ptnr2_symmetry _pdbx_struct_conn_angle.ptnr3_label_atom_id _pdbx_struct_conn_angle.ptnr3_label_alt_id _pdbx_struct_conn_angle.ptnr3_label_asym_id _pdbx_struct_conn_angle.ptnr3_label_comp_id _pdbx_struct_conn_angle.ptnr3_label_seq_id _pdbx_struct_conn_angle.ptnr3_auth_atom_id _pdbx_struct_conn_angle.ptnr3_auth_asym_id _pdbx_struct_conn_angle.ptnr3_auth_comp_id _pdbx_struct_conn_angle.ptnr3_auth_seq_id _pdbx_struct_conn_angle.ptnr3_PDB_ins_code _pdbx_struct_conn_angle.ptnr3_symmetry _pdbx_struct_conn_angle.value _pdbx_struct_conn_angle.value_esd 1 O ? A VAL 37 ? A VAL 35 ? 1_555 NA ? F NA . ? A NA 503 ? 1_555 OD1 ? A ASN 61 ? A ASN 59 ? 1_555 176.9 ? 2 O ? A VAL 37 ? A VAL 35 ? 1_555 NA ? F NA . ? A NA 503 ? 1_555 O ? O HOH . ? A HOH 609 ? 1_555 90.5 ? 3 OD1 ? A ASN 61 ? A ASN 59 ? 1_555 NA ? F NA . ? A NA 503 ? 1_555 O ? O HOH . ? A HOH 609 ? 1_555 92.6 ? 4 O ? A VAL 37 ? A VAL 35 ? 1_555 NA ? F NA . ? A NA 503 ? 1_555 O ? O HOH . ? A HOH 611 ? 1_555 92.7 ? 5 OD1 ? A ASN 61 ? A ASN 59 ? 1_555 NA ? F NA . ? A NA 503 ? 1_555 O ? O HOH . ? A HOH 611 ? 1_555 87.4 ? 6 O ? O HOH . ? A HOH 609 ? 1_555 NA ? F NA . ? A NA 503 ? 1_555 O ? O HOH . ? A HOH 611 ? 1_555 85.6 ? 7 O ? A VAL 37 ? A VAL 35 ? 1_555 NA ? F NA . ? A NA 503 ? 1_555 O ? O HOH . ? A HOH 610 ? 1_555 91.5 ? 8 OD1 ? A ASN 61 ? A ASN 59 ? 1_555 NA ? F NA . ? A NA 503 ? 1_555 O ? O HOH . ? A HOH 610 ? 1_555 88.3 ? 9 O ? O HOH . ? A HOH 609 ? 1_555 NA ? F NA . ? A NA 503 ? 1_555 O ? O HOH . ? A HOH 610 ? 1_555 97.1 ? 10 O ? O HOH . ? A HOH 611 ? 1_555 NA ? F NA . ? A NA 503 ? 1_555 O ? O HOH . ? A HOH 610 ? 1_555 175.1 ? 11 O ? A VAL 37 ? A VAL 35 ? 1_555 NA ? F NA . ? A NA 503 ? 1_555 OH ? A TYR 58 ? A TYR 56 ? 1_555 89.8 ? 12 OD1 ? A ASN 61 ? A ASN 59 ? 1_555 NA ? F NA . ? A NA 503 ? 1_555 OH ? A TYR 58 ? A TYR 56 ? 1_555 87.1 ? 13 O ? O HOH . ? A HOH 609 ? 1_555 NA ? F NA . ? A NA 503 ? 1_555 OH ? A TYR 58 ? A TYR 56 ? 1_555 176.2 ? 14 O ? O HOH . ? A HOH 611 ? 1_555 NA ? F NA . ? A NA 503 ? 1_555 OH ? A TYR 58 ? A TYR 56 ? 1_555 90.7 ? 15 O ? O HOH . ? A HOH 610 ? 1_555 NA ? F NA . ? A NA 503 ? 1_555 OH ? A TYR 58 ? A TYR 56 ? 1_555 86.7 ? # 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 30.1028 14.2243 -0.2836 -0.2362 -0.1808 -0.1477 -0.0121 0.0001 -0.0210 3.1244 1.8808 7.1322 -0.4362 -2.4036 0.5467 -0.0622 -0.0357 0.0615 -0.0476 0.0377 -0.0866 -0.0644 -0.0248 0.0245 'X-RAY DIFFRACTION' 2 ? refined 5.3045 12.8850 13.4525 -0.1731 -0.1837 -0.1763 0.0249 -0.0374 -0.0139 3.9754 1.6649 4.6304 0.9059 -1.8826 -0.4667 0.0777 0.1514 -0.1887 0.1177 0.1057 0.0518 0.1115 -0.3087 -0.1835 # 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 10 ? ? A 122 ? ? ? ? 'X-RAY DIFFRACTION' 2 2 A 123 ? ? A 236 ? ? ? ? # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal SHELX 'model building' . ? 1 RESOLVE 'model building' . ? 2 PHASER phasing . ? 3 REFMAC refinement 5.2.0019 ? 4 HKL-2000 'data reduction' . ? 5 HKL-2000 'data scaling' . ? 6 SHELX phasing . ? 7 RESOLVE phasing . ? 8 # _pdbx_validate_close_contact.id 1 _pdbx_validate_close_contact.PDB_model_num 1 _pdbx_validate_close_contact.auth_atom_id_1 O _pdbx_validate_close_contact.auth_asym_id_1 A _pdbx_validate_close_contact.auth_comp_id_1 HOH _pdbx_validate_close_contact.auth_seq_id_1 717 _pdbx_validate_close_contact.PDB_ins_code_1 ? _pdbx_validate_close_contact.label_alt_id_1 ? _pdbx_validate_close_contact.auth_atom_id_2 O _pdbx_validate_close_contact.auth_asym_id_2 A _pdbx_validate_close_contact.auth_comp_id_2 HOH _pdbx_validate_close_contact.auth_seq_id_2 718 _pdbx_validate_close_contact.PDB_ins_code_2 ? _pdbx_validate_close_contact.label_alt_id_2 ? _pdbx_validate_close_contact.dist 1.90 # 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 ASP A 45 ? ? -107.64 -130.15 2 1 ASP A 47 ? ? 93.51 -4.15 3 1 ASP A 48 ? ? 52.48 1.73 4 1 ASP A 76 ? ? -69.88 98.67 5 1 HIS A 79 ? ? -142.32 55.48 6 1 CYS A 138 ? ? -161.14 115.48 7 1 ASN A 197 ? ? 72.11 32.83 8 1 THR A 205 ? ? 37.47 63.45 # loop_ _pdbx_validate_peptide_omega.id _pdbx_validate_peptide_omega.PDB_model_num _pdbx_validate_peptide_omega.auth_comp_id_1 _pdbx_validate_peptide_omega.auth_asym_id_1 _pdbx_validate_peptide_omega.auth_seq_id_1 _pdbx_validate_peptide_omega.PDB_ins_code_1 _pdbx_validate_peptide_omega.label_alt_id_1 _pdbx_validate_peptide_omega.auth_comp_id_2 _pdbx_validate_peptide_omega.auth_asym_id_2 _pdbx_validate_peptide_omega.auth_seq_id_2 _pdbx_validate_peptide_omega.PDB_ins_code_2 _pdbx_validate_peptide_omega.label_alt_id_2 _pdbx_validate_peptide_omega.omega 1 1 ASP A 45 ? ? LYS A 46 ? ? 149.44 2 1 ASP A 47 ? ? ASP A 48 ? ? -149.44 # 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 GLU 237 ? A GLU 239 13 1 Y 1 A PHE 238 ? A PHE 240 14 1 Y 1 A GLN 239 ? A GLN 241 15 1 Y 1 A ARG 240 ? A ARG 242 16 1 Y 1 A THR 241 ? A THR 243 17 1 Y 1 A ILE 242 ? A ILE 244 18 1 Y 1 A SER 243 ? A SER 245 19 1 Y 1 A PRO 244 ? A PRO 246 20 1 Y 1 A THR 245 ? A THR 247 21 1 Y 1 A PRO 246 ? A PRO 248 22 1 Y 1 A PRO 247 ? A PRO 249 23 1 Y 1 A THR 248 ? A THR 250 24 1 Y 1 A ASP 249 ? A ASP 251 25 1 Y 1 A LYS 250 ? A LYS 252 26 1 Y 1 A GLY 251 ? A GLY 253 27 1 Y 1 A GLN 252 ? A GLN 254 28 1 Y 1 A GLN 253 ? A GLN 255 29 1 Y 1 A GLY 254 ? A GLY 256 30 1 Y 1 A ILE 255 ? A ILE 257 31 1 Y 1 A LEU 256 ? A LEU 258 32 1 Y 1 A ASN 257 ? A ASN 259 33 1 Y 1 A GLY 258 ? A GLY 260 34 1 Y 1 A ASN 259 ? A ASN 261 35 1 Y 1 A GLN 260 ? A GLN 262 36 1 Y 1 A HIS 261 ? A HIS 263 37 1 Y 1 A HIS 262 ? A HIS 264 38 1 Y 1 A HIS 263 ? A HIS 265 39 1 Y 1 A HIS 264 ? A HIS 266 40 1 Y 1 A HIS 265 ? A HIS 267 41 1 Y 1 A HIS 266 ? A HIS 268 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 N-ACETYL-D-GLUCOSAMINE NAG 3 ALPHA-L-FUCOSE FUC 4 'SODIUM ION' NA 5 'FORMIC ACID' FMT 6 water HOH # 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 B 2 NAG 1 301 301 NAG NAG A . C 2 NAG 1 401 401 NAG NAG A . D 2 NAG 1 501 501 NAG NAG A . E 3 FUC 2 502 502 FUC FUC A . F 4 NA 1 503 503 NA NA A . G 5 FMT 1 601 601 FMT FMT A . H 5 FMT 1 602 602 FMT FMT A . I 5 FMT 1 603 603 FMT FMT A . J 5 FMT 1 604 604 FMT FMT A . K 5 FMT 1 605 605 FMT FMT A . L 5 FMT 1 606 606 FMT FMT A . M 5 FMT 1 607 607 FMT FMT A . N 5 FMT 1 608 608 FMT FMT A . O 6 HOH 1 609 609 HOH HOH A . O 6 HOH 2 610 610 HOH HOH A . O 6 HOH 3 611 611 HOH HOH A . O 6 HOH 4 612 612 HOH HOH A . O 6 HOH 5 613 613 HOH HOH A . O 6 HOH 6 614 614 HOH HOH A . O 6 HOH 7 615 615 HOH HOH A . O 6 HOH 8 616 616 HOH HOH A . O 6 HOH 9 617 617 HOH HOH A . O 6 HOH 10 618 618 HOH HOH A . O 6 HOH 11 619 619 HOH HOH A . O 6 HOH 12 620 620 HOH HOH A . O 6 HOH 13 621 621 HOH HOH A . O 6 HOH 14 622 622 HOH HOH A . O 6 HOH 15 623 623 HOH HOH A . O 6 HOH 16 624 624 HOH HOH A . O 6 HOH 17 625 625 HOH HOH A . O 6 HOH 18 626 626 HOH HOH A . O 6 HOH 19 627 627 HOH HOH A . O 6 HOH 20 628 628 HOH HOH A . O 6 HOH 21 629 629 HOH HOH A . O 6 HOH 22 630 630 HOH HOH A . O 6 HOH 23 631 631 HOH HOH A . O 6 HOH 24 632 632 HOH HOH A . O 6 HOH 25 633 633 HOH HOH A . O 6 HOH 26 634 634 HOH HOH A . O 6 HOH 27 635 635 HOH HOH A . O 6 HOH 28 636 636 HOH HOH A . O 6 HOH 29 637 637 HOH HOH A . O 6 HOH 30 638 638 HOH HOH A . O 6 HOH 31 639 639 HOH HOH A . O 6 HOH 32 640 640 HOH HOH A . O 6 HOH 33 641 641 HOH HOH A . O 6 HOH 34 642 642 HOH HOH A . O 6 HOH 35 643 643 HOH HOH A . O 6 HOH 36 644 644 HOH HOH A . O 6 HOH 37 645 645 HOH HOH A . O 6 HOH 38 646 646 HOH HOH A . O 6 HOH 39 647 647 HOH HOH A . O 6 HOH 40 648 648 HOH HOH A . O 6 HOH 41 649 649 HOH HOH A . O 6 HOH 42 650 650 HOH HOH A . O 6 HOH 43 651 651 HOH HOH A . O 6 HOH 44 652 652 HOH HOH A . O 6 HOH 45 653 653 HOH HOH A . O 6 HOH 46 654 654 HOH HOH A . O 6 HOH 47 655 655 HOH HOH A . O 6 HOH 48 656 656 HOH HOH A . O 6 HOH 49 657 657 HOH HOH A . O 6 HOH 50 658 658 HOH HOH A . O 6 HOH 51 659 659 HOH HOH A . O 6 HOH 52 660 660 HOH HOH A . O 6 HOH 53 661 661 HOH HOH A . O 6 HOH 54 662 662 HOH HOH A . O 6 HOH 55 663 663 HOH HOH A . O 6 HOH 56 664 664 HOH HOH A . O 6 HOH 57 665 665 HOH HOH A . O 6 HOH 58 666 666 HOH HOH A . O 6 HOH 59 667 667 HOH HOH A . O 6 HOH 60 668 668 HOH HOH A . O 6 HOH 61 669 669 HOH HOH A . O 6 HOH 62 670 670 HOH HOH A . O 6 HOH 63 671 671 HOH HOH A . O 6 HOH 64 672 672 HOH HOH A . O 6 HOH 65 673 673 HOH HOH A . O 6 HOH 66 674 674 HOH HOH A . O 6 HOH 67 675 675 HOH HOH A . O 6 HOH 68 676 676 HOH HOH A . O 6 HOH 69 677 677 HOH HOH A . O 6 HOH 70 678 678 HOH HOH A . O 6 HOH 71 679 679 HOH HOH A . O 6 HOH 72 680 680 HOH HOH A . O 6 HOH 73 681 681 HOH HOH A . O 6 HOH 74 682 682 HOH HOH A . O 6 HOH 75 683 683 HOH HOH A . O 6 HOH 76 684 684 HOH HOH A . O 6 HOH 77 685 685 HOH HOH A . O 6 HOH 78 686 686 HOH HOH A . O 6 HOH 79 687 687 HOH HOH A . O 6 HOH 80 688 688 HOH HOH A . O 6 HOH 81 689 689 HOH HOH A . O 6 HOH 82 690 690 HOH HOH A . O 6 HOH 83 691 691 HOH HOH A . O 6 HOH 84 692 692 HOH HOH A . O 6 HOH 85 693 693 HOH HOH A . O 6 HOH 86 694 694 HOH HOH A . O 6 HOH 87 695 695 HOH HOH A . O 6 HOH 88 696 696 HOH HOH A . O 6 HOH 89 697 697 HOH HOH A . O 6 HOH 90 698 698 HOH HOH A . O 6 HOH 91 699 699 HOH HOH A . O 6 HOH 92 700 700 HOH HOH A . O 6 HOH 93 701 701 HOH HOH A . O 6 HOH 94 702 702 HOH HOH A . O 6 HOH 95 703 703 HOH HOH A . O 6 HOH 96 704 704 HOH HOH A . O 6 HOH 97 705 705 HOH HOH A . O 6 HOH 98 706 706 HOH HOH A . O 6 HOH 99 707 707 HOH HOH A . O 6 HOH 100 708 708 HOH HOH A . O 6 HOH 101 709 709 HOH HOH A . O 6 HOH 102 710 710 HOH HOH A . O 6 HOH 103 711 711 HOH HOH A . O 6 HOH 104 712 712 HOH HOH A . O 6 HOH 105 713 713 HOH HOH A . O 6 HOH 106 714 714 HOH HOH A . O 6 HOH 107 715 715 HOH HOH A . O 6 HOH 108 716 716 HOH HOH A . O 6 HOH 109 717 717 HOH HOH A . O 6 HOH 110 718 718 HOH HOH A . O 6 HOH 111 719 719 HOH HOH A . O 6 HOH 112 720 720 HOH HOH A . O 6 HOH 113 721 721 HOH HOH A . O 6 HOH 114 722 722 HOH HOH A . O 6 HOH 115 723 723 HOH HOH A . O 6 HOH 116 724 724 HOH HOH A . O 6 HOH 117 725 725 HOH HOH A . O 6 HOH 118 726 726 HOH HOH A . O 6 HOH 119 727 727 HOH HOH A . O 6 HOH 120 728 728 HOH HOH A . O 6 HOH 121 729 729 HOH HOH A . O 6 HOH 122 730 730 HOH HOH A . O 6 HOH 123 731 731 HOH HOH A . O 6 HOH 124 732 732 HOH HOH A . O 6 HOH 125 733 733 HOH HOH A . O 6 HOH 126 734 734 HOH HOH A . O 6 HOH 127 735 735 HOH HOH A . O 6 HOH 128 736 736 HOH HOH A . O 6 HOH 129 737 737 HOH HOH A . #