data_4D01 # _entry.id 4D01 # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.279 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 4D01 PDBE EBI-60443 WWPDB D_1290060443 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.content_type _pdbx_database_related.details PDB 4UXU unspecified ;CRYSTAL STRUCTURE OF THE EXTRACELLULAR DOMAIN OF THE HUMAN ALPHA9 NICOTINIC ACETYLCHOLINE RECEPTOR IN COMPLEX WITH METHYLLYCACONITINE ; PDB 4UY2 unspecified 'CRYSTAL STRUCTURE OF THE COMPLEX OF THE EXTRACELLULAR DOMAIN OF HUMAN ALPHA9 NACHR WITH ALPHA-BUNGAROTOXIN.' # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 4D01 _pdbx_database_status.deposit_site PDBE _pdbx_database_status.process_site PDBE _pdbx_database_status.SG_entry . _pdbx_database_status.recvd_initial_deposition_date 2014-04-23 _pdbx_database_status.pdb_format_compatible Y _pdbx_database_status.status_code_sf ? _pdbx_database_status.status_code_mr ? _pdbx_database_status.status_code_cs ? _pdbx_database_status.methods_development_category ? # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Giastas, P.' 1 'Zouridakis, M.' 2 'Zarkadas, E.' 3 'Tzartos, S.J.' 4 # _citation.id primary _citation.title 'Crystal Structures of Free and Antagonist-Bound States of Human Alpha9 Nicotinic Receptor Extracellular Domain' _citation.journal_abbrev Nat.Struct.Mol.Biol. _citation.journal_volume 21 _citation.page_first 976 _citation.page_last ? _citation.year 2014 _citation.journal_id_ASTM ? _citation.country US _citation.journal_id_ISSN 1545-9993 _citation.journal_id_CSD ? _citation.book_publisher ? _citation.pdbx_database_id_PubMed 25282151 _citation.pdbx_database_id_DOI 10.1038/NSMB.2900 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Zouridakis, M.' 1 primary 'Giastas, P.' 2 primary 'Zarkadas, E.' 3 primary 'Chroni-Tzartou, D.' 4 primary 'Bregestovski, P.' 5 primary 'Tzartos, S.J.' 6 # _cell.entry_id 4D01 _cell.length_a 49.520 _cell.length_b 64.269 _cell.length_c 80.138 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 90.00 _cell.Z_PDB 4 _cell.pdbx_unique_axis ? # _symmetry.entry_id 4D01 _symmetry.space_group_name_H-M 'P 2 21 21' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 18 # 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 'NEURONAL ACETYLCHOLINE RECEPTOR SUBUNIT ALPHA-9' 25307.029 1 ? ? 'EXTRACELLULAR DOMAIN, RESIDUES 26-237' ? 2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 2 ? ? ? ? 3 non-polymer syn 1,2-ETHANEDIOL 62.068 4 ? ? ? ? 4 water nat water 18.015 206 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name 'NICOTINIC ACETYLCHOLINE RECEPTOR SUBUNIT ALPHA-9, NACHR ALPHA-9, HUMAN ALPHA9 NICOTINIC ACETYLCHOLINE RECEPTOR' # _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 ;ADGKYAQKLFNDLFEDYSNALRPVEDTDKVLNVTLQITLSQIKDMDERNQILTAYLWIRQIWHDAYLTWDRDQYDGLDSI RIPSDLVWRPDIVLYNKADDESSEPVNTNVVLRYDGLITWDAPAITKSSCVVDVTYFPFDNQQCNLTFGSWTYNGNQVDI FNALDSGDLSDFIEDVEWEVHGMPAVKNVISYGCCSEPYPDVTFTLLLKRRSHHHHHH ; _entity_poly.pdbx_seq_one_letter_code_can ;ADGKYAQKLFNDLFEDYSNALRPVEDTDKVLNVTLQITLSQIKDMDERNQILTAYLWIRQIWHDAYLTWDRDQYDGLDSI RIPSDLVWRPDIVLYNKADDESSEPVNTNVVLRYDGLITWDAPAITKSSCVVDVTYFPFDNQQCNLTFGSWTYNGNQVDI FNALDSGDLSDFIEDVEWEVHGMPAVKNVISYGCCSEPYPDVTFTLLLKRRSHHHHHH ; _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 ALA n 1 2 ASP n 1 3 GLY n 1 4 LYS n 1 5 TYR n 1 6 ALA n 1 7 GLN n 1 8 LYS n 1 9 LEU n 1 10 PHE n 1 11 ASN n 1 12 ASP n 1 13 LEU n 1 14 PHE n 1 15 GLU n 1 16 ASP n 1 17 TYR n 1 18 SER n 1 19 ASN n 1 20 ALA n 1 21 LEU n 1 22 ARG n 1 23 PRO n 1 24 VAL n 1 25 GLU n 1 26 ASP n 1 27 THR n 1 28 ASP n 1 29 LYS n 1 30 VAL n 1 31 LEU n 1 32 ASN n 1 33 VAL n 1 34 THR n 1 35 LEU n 1 36 GLN n 1 37 ILE n 1 38 THR n 1 39 LEU n 1 40 SER n 1 41 GLN n 1 42 ILE n 1 43 LYS n 1 44 ASP n 1 45 MET n 1 46 ASP n 1 47 GLU n 1 48 ARG n 1 49 ASN n 1 50 GLN n 1 51 ILE n 1 52 LEU n 1 53 THR n 1 54 ALA n 1 55 TYR n 1 56 LEU n 1 57 TRP n 1 58 ILE n 1 59 ARG n 1 60 GLN n 1 61 ILE n 1 62 TRP n 1 63 HIS n 1 64 ASP n 1 65 ALA n 1 66 TYR n 1 67 LEU n 1 68 THR n 1 69 TRP n 1 70 ASP n 1 71 ARG n 1 72 ASP n 1 73 GLN n 1 74 TYR n 1 75 ASP n 1 76 GLY n 1 77 LEU n 1 78 ASP n 1 79 SER n 1 80 ILE n 1 81 ARG n 1 82 ILE n 1 83 PRO n 1 84 SER n 1 85 ASP n 1 86 LEU n 1 87 VAL n 1 88 TRP n 1 89 ARG n 1 90 PRO n 1 91 ASP n 1 92 ILE n 1 93 VAL n 1 94 LEU n 1 95 TYR n 1 96 ASN n 1 97 LYS n 1 98 ALA n 1 99 ASP n 1 100 ASP n 1 101 GLU n 1 102 SER n 1 103 SER n 1 104 GLU n 1 105 PRO n 1 106 VAL n 1 107 ASN n 1 108 THR n 1 109 ASN n 1 110 VAL n 1 111 VAL n 1 112 LEU n 1 113 ARG n 1 114 TYR n 1 115 ASP n 1 116 GLY n 1 117 LEU n 1 118 ILE n 1 119 THR n 1 120 TRP n 1 121 ASP n 1 122 ALA n 1 123 PRO n 1 124 ALA n 1 125 ILE n 1 126 THR n 1 127 LYS n 1 128 SER n 1 129 SER n 1 130 CYS n 1 131 VAL n 1 132 VAL n 1 133 ASP n 1 134 VAL n 1 135 THR n 1 136 TYR n 1 137 PHE n 1 138 PRO n 1 139 PHE n 1 140 ASP n 1 141 ASN n 1 142 GLN n 1 143 GLN n 1 144 CYS n 1 145 ASN n 1 146 LEU n 1 147 THR n 1 148 PHE n 1 149 GLY n 1 150 SER n 1 151 TRP n 1 152 THR n 1 153 TYR n 1 154 ASN n 1 155 GLY n 1 156 ASN n 1 157 GLN n 1 158 VAL n 1 159 ASP n 1 160 ILE n 1 161 PHE n 1 162 ASN n 1 163 ALA n 1 164 LEU n 1 165 ASP n 1 166 SER n 1 167 GLY n 1 168 ASP n 1 169 LEU n 1 170 SER n 1 171 ASP n 1 172 PHE n 1 173 ILE n 1 174 GLU n 1 175 ASP n 1 176 VAL n 1 177 GLU n 1 178 TRP n 1 179 GLU n 1 180 VAL n 1 181 HIS n 1 182 GLY n 1 183 MET n 1 184 PRO n 1 185 ALA n 1 186 VAL n 1 187 LYS n 1 188 ASN n 1 189 VAL n 1 190 ILE n 1 191 SER n 1 192 TYR n 1 193 GLY n 1 194 CYS n 1 195 CYS n 1 196 SER n 1 197 GLU n 1 198 PRO n 1 199 TYR n 1 200 PRO n 1 201 ASP n 1 202 VAL n 1 203 THR n 1 204 PHE n 1 205 THR n 1 206 LEU n 1 207 LEU n 1 208 LEU n 1 209 LYS n 1 210 ARG n 1 211 ARG n 1 212 SER n 1 213 HIS n 1 214 HIS n 1 215 HIS n 1 216 HIS n 1 217 HIS n 1 218 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 HUMAN _entity_src_gen.gene_src_genus ? _entity_src_gen.pdbx_gene_src_gene ? _entity_src_gen.gene_src_species ? _entity_src_gen.gene_src_strain ? _entity_src_gen.gene_src_tissue ? _entity_src_gen.gene_src_tissue_fraction ? _entity_src_gen.gene_src_details ? _entity_src_gen.pdbx_gene_src_fragment ? _entity_src_gen.pdbx_gene_src_scientific_name 'HOMO SAPIENS' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 9606 _entity_src_gen.pdbx_gene_src_variant ? _entity_src_gen.pdbx_gene_src_cell_line ? _entity_src_gen.pdbx_gene_src_atcc ? _entity_src_gen.pdbx_gene_src_organ ? _entity_src_gen.pdbx_gene_src_organelle ? _entity_src_gen.pdbx_gene_src_cell ? _entity_src_gen.pdbx_gene_src_cellular_location ? _entity_src_gen.host_org_common_name ? _entity_src_gen.pdbx_host_org_scientific_name 'KOMAGATAELLA PASTORIS' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 4922 _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 X33 _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 PPICZAA _entity_src_gen.plasmid_details ? _entity_src_gen.pdbx_description ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code ACHA9_HUMAN _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ? _struct_ref.pdbx_align_begin ? _struct_ref.pdbx_db_accession Q9UGM1 _struct_ref.pdbx_db_isoform ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 4D01 _struct_ref_seq.pdbx_strand_id A _struct_ref_seq.seq_align_beg 1 _struct_ref_seq.pdbx_seq_align_beg_ins_code ? _struct_ref_seq.seq_align_end 212 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession Q9UGM1 _struct_ref_seq.db_align_beg 26 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 237 _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 212 # 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 4D01 HIS A 213 ? UNP Q9UGM1 ? ? 'expression tag' 213 1 1 4D01 HIS A 214 ? UNP Q9UGM1 ? ? 'expression tag' 214 2 1 4D01 HIS A 215 ? UNP Q9UGM1 ? ? 'expression tag' 215 3 1 4D01 HIS A 216 ? UNP Q9UGM1 ? ? 'expression tag' 216 4 1 4D01 HIS A 217 ? UNP Q9UGM1 ? ? 'expression tag' 217 5 1 4D01 HIS A 218 ? UNP Q9UGM1 ? ? 'expression tag' 218 6 # 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 EDO non-polymer . 1,2-ETHANEDIOL 'ETHYLENE GLYCOL' 'C2 H6 O2' 62.068 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 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 4D01 _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.4 _exptl_crystal.density_percent_sol 51 _exptl_crystal.description NONE # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method ? _exptl_crystal_grow.temp ? _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 7.5 _exptl_crystal_grow.pdbx_pH_range ? _exptl_crystal_grow.pdbx_details '100 MM SPG BUFFER PH 6.5, 25% PEG 3350' # _diffrn.id 1 _diffrn.ambient_temp 100 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector PIXEL _diffrn_detector.type 'DECTRIS PILATUS 2M' _diffrn_detector.pdbx_collection_date 2013-01-10 _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator ? _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 1.0000 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'SLS BEAMLINE X06DA' _diffrn_source.pdbx_synchrotron_site SLS _diffrn_source.pdbx_synchrotron_beamline X06DA _diffrn_source.pdbx_wavelength 1.0000 _diffrn_source.pdbx_wavelength_list ? # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 4D01 _reflns.observed_criterion_sigma_I 1.4 _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 42.00 _reflns.d_resolution_high 1.79 _reflns.number_obs 24313 _reflns.number_all ? _reflns.percent_possible_obs 99.3 _reflns.pdbx_Rmerge_I_obs 0.08 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 15.90 _reflns.B_iso_Wilson_estimate 32.7 _reflns.pdbx_redundancy 12.5 # _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_ordinal 1 _reflns_shell.d_res_high 1.79 _reflns_shell.d_res_low 42.00 _reflns_shell.percent_possible_all 95.4 _reflns_shell.Rmerge_I_obs 1.40 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs 1.20 _reflns_shell.pdbx_redundancy 11.4 # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 4D01 _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 24313 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F 1.33 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 42.126 _refine.ls_d_res_high 1.795 _refine.ls_percent_reflns_obs 98.81 _refine.ls_R_factor_obs 0.1960 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.1950 _refine.ls_R_factor_R_free 0.2497 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.1 _refine.ls_number_reflns_R_free 1240 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc ? _refine.correlation_coeff_Fo_to_Fc_free ? _refine.B_iso_mean 48 _refine.aniso_B[1][1] ? _refine.aniso_B[2][2] ? _refine.aniso_B[3][3] ? _refine.aniso_B[1][2] ? _refine.aniso_B[1][3] ? _refine.aniso_B[2][3] ? _refine.solvent_model_details 'FLAT BULK SOLVENT MODEL' _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.11 _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii 0.90 _refine.pdbx_ls_cross_valid_method ? _refine.details 'RESIDUES OF THE REGION 100-104 WAS EITHER LEFT UNMODELED OR WAS MODELED ONLY THEIR MAIN CHAIN ATOMS' _refine.pdbx_starting_model 'PDB ENTRY 2QC1' _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values ML _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details ? _refine.pdbx_overall_ESU_R ? _refine.pdbx_overall_ESU_R_Free ? _refine.overall_SU_ML 0.24 _refine.pdbx_overall_phase_error 28.07 _refine.overall_SU_B ? _refine.overall_SU_R_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 1721 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 44 _refine_hist.number_atoms_solvent 206 _refine_hist.number_atoms_total 1971 _refine_hist.d_res_high 1.795 _refine_hist.d_res_low 42.126 # 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 f_bond_d 0.013 ? ? 1840 'X-RAY DIFFRACTION' ? f_angle_d 1.459 ? ? 2509 'X-RAY DIFFRACTION' ? f_dihedral_angle_d 13.344 ? ? 664 'X-RAY DIFFRACTION' ? f_chiral_restr 0.082 ? ? 274 'X-RAY DIFFRACTION' ? f_plane_restr 0.008 ? ? 323 'X-RAY DIFFRACTION' ? # loop_ _refine_ls_shell.pdbx_refine_id _refine_ls_shell.pdbx_total_number_of_bins_used _refine_ls_shell.d_res_high _refine_ls_shell.d_res_low _refine_ls_shell.number_reflns_R_work _refine_ls_shell.R_factor_R_work _refine_ls_shell.percent_reflns_obs _refine_ls_shell.R_factor_R_free _refine_ls_shell.R_factor_R_free_error _refine_ls_shell.percent_reflns_R_free _refine_ls_shell.number_reflns_R_free _refine_ls_shell.number_reflns_all _refine_ls_shell.R_factor_all 'X-RAY DIFFRACTION' . 1.7945 1.8664 2380 0.3309 93.00 0.4005 . . 123 . . 'X-RAY DIFFRACTION' . 1.8664 1.9513 2517 0.2617 99.00 0.3133 . . 161 . . 'X-RAY DIFFRACTION' . 1.9513 2.0542 2551 0.2429 100.00 0.2904 . . 140 . . 'X-RAY DIFFRACTION' . 2.0542 2.1829 2533 0.2110 99.00 0.2385 . . 143 . . 'X-RAY DIFFRACTION' . 2.1829 2.3514 2554 0.2184 100.00 0.2886 . . 137 . . 'X-RAY DIFFRACTION' . 2.3514 2.5880 2570 0.2067 99.00 0.2607 . . 135 . . 'X-RAY DIFFRACTION' . 2.5880 2.9624 2581 0.1953 99.00 0.2694 . . 121 . . 'X-RAY DIFFRACTION' . 2.9624 3.7320 2605 0.1720 100.00 0.2424 . . 148 . . 'X-RAY DIFFRACTION' . 3.7320 42.1377 2782 0.1645 100.00 0.2158 . . 132 . . # _struct.entry_id 4D01 _struct.title 'Crystal Structure of the Extracellular Domain of the Human Alpha9 Nicotinic Acetylcholine Receptor' _struct.pdbx_descriptor 'NEURONAL ACETYLCHOLINE RECEPTOR SUBUNIT ALPHA-9' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 4D01 _struct_keywords.pdbx_keywords 'SIGNALING PROTEIN' _struct_keywords.text 'SIGNALING PROTEIN, LIGAND BINDING DOMAIN, CYS-LOOP RECEPTOR' # 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 3 ? E N N 3 ? F N N 3 ? G N N 3 ? H N N 4 ? # _struct_biol.id 1 # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 1 GLY A 3 ? PHE A 14 ? GLY A 3 PHE A 14 1 ? 12 HELX_P HELX_P2 2 ASP A 70 ? ASP A 75 ? ASP A 70 ASP A 75 5 ? 6 HELX_P HELX_P3 3 ASP A 85 ? VAL A 87 ? ASP A 85 VAL A 87 5 ? 3 # _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 130 SG ? ? ? 1_555 A CYS 144 SG ? ? A CYS 130 A CYS 144 1_555 ? ? ? ? ? ? ? 2.086 ? disulf2 disulf ? ? A CYS 194 SG ? ? ? 1_555 A CYS 195 SG ? ? A CYS 194 A CYS 195 1_555 ? ? ? ? ? ? ? 2.089 ? covale1 covale ? ? A ASN 32 ND2 ? ? ? 1_555 B NAG . C1 ? ? A ASN 32 A NAG 1216 1_555 ? ? ? ? ? ? ? 1.450 ? covale2 covale ? ? A ASN 145 ND2 ? ? ? 1_555 C NAG . C1 ? ? A ASN 145 A NAG 1217 1_555 ? ? ? ? ? ? ? 1.441 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? # loop_ _struct_mon_prot_cis.pdbx_id _struct_mon_prot_cis.label_comp_id _struct_mon_prot_cis.label_seq_id _struct_mon_prot_cis.label_asym_id _struct_mon_prot_cis.label_alt_id _struct_mon_prot_cis.pdbx_PDB_ins_code _struct_mon_prot_cis.auth_comp_id _struct_mon_prot_cis.auth_seq_id _struct_mon_prot_cis.auth_asym_id _struct_mon_prot_cis.pdbx_label_comp_id_2 _struct_mon_prot_cis.pdbx_label_seq_id_2 _struct_mon_prot_cis.pdbx_label_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_ins_code_2 _struct_mon_prot_cis.pdbx_auth_comp_id_2 _struct_mon_prot_cis.pdbx_auth_seq_id_2 _struct_mon_prot_cis.pdbx_auth_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_model_num _struct_mon_prot_cis.pdbx_omega_angle 1 ASP 100 A . ? ASP 100 A GLU 101 A ? GLU 101 A 1 -3.45 2 PHE 137 A . ? PHE 137 A PRO 138 A ? PRO 138 A 1 -0.01 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details AA ? 6 ? AB ? 6 ? AC ? 5 ? AD ? 2 ? AE ? 6 ? AF ? 2 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense AA 1 2 ? anti-parallel AA 2 3 ? anti-parallel AA 3 4 ? anti-parallel AA 4 5 ? anti-parallel AA 5 6 ? anti-parallel AB 1 2 ? anti-parallel AB 2 3 ? anti-parallel AB 3 4 ? anti-parallel AB 4 5 ? anti-parallel AB 5 6 ? parallel AC 1 2 ? anti-parallel AC 2 3 ? anti-parallel AC 3 4 ? anti-parallel AC 4 5 ? parallel AD 1 2 ? anti-parallel AE 1 2 ? anti-parallel AE 2 3 ? anti-parallel AE 3 4 ? anti-parallel AE 4 5 ? anti-parallel AE 5 6 ? anti-parallel AF 1 2 ? anti-parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id AA 1 SER A 79 ? PRO A 83 ? SER A 79 PRO A 83 AA 2 ASN A 109 ? ARG A 113 ? ASN A 109 ARG A 113 AA 3 ASP A 115 ? ASP A 133 ? ASP A 115 ASP A 133 AA 4 ASN A 141 ? SER A 150 ? ASN A 141 SER A 150 AA 5 PRO A 198 ? ARG A 210 ? PRO A 198 ARG A 210 AA 6 ALA A 185 ? SER A 191 ? ALA A 185 SER A 191 AB 1 SER A 79 ? PRO A 83 ? SER A 79 PRO A 83 AB 2 ASN A 109 ? ARG A 113 ? ASN A 109 ARG A 113 AB 3 ASP A 115 ? ASP A 133 ? ASP A 115 ASP A 133 AB 4 ILE A 51 ? THR A 68 ? ILE A 51 THR A 68 AB 5 LEU A 31 ? ASP A 46 ? LEU A 31 ASP A 46 AB 6 VAL A 158 ? ASN A 162 ? VAL A 158 ASN A 162 AC 1 SER A 79 ? PRO A 83 ? SER A 79 PRO A 83 AC 2 ASN A 109 ? ARG A 113 ? ASN A 109 ARG A 113 AC 3 ASP A 115 ? ASP A 133 ? ASP A 115 ASP A 133 AC 4 ASN A 141 ? SER A 150 ? ASN A 141 SER A 150 AC 5 ILE A 92 ? LEU A 94 ? ILE A 92 LEU A 94 AD 1 TRP A 178 ? GLY A 182 ? TRP A 178 GLY A 182 AD 2 PRO A 198 ? ARG A 210 ? PRO A 198 ARG A 210 AE 1 SER A 79 ? PRO A 83 ? SER A 79 PRO A 83 AE 2 ASN A 109 ? ARG A 113 ? ASN A 109 ARG A 113 AE 3 ASP A 115 ? ASP A 133 ? ASP A 115 ASP A 133 AE 4 ASN A 141 ? SER A 150 ? ASN A 141 SER A 150 AE 5 PRO A 198 ? ARG A 210 ? PRO A 198 ARG A 210 AE 6 TRP A 178 ? GLY A 182 ? TRP A 178 GLY A 182 AF 1 ALA A 185 ? SER A 191 ? ALA A 185 SER A 191 AF 2 PRO A 198 ? ARG A 210 ? PRO A 198 ARG A 210 # 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 AA 1 2 N ILE A 82 ? N ILE A 82 O VAL A 110 ? O VAL A 110 AA 2 3 O ARG A 113 ? O ARG A 113 N GLY A 116 ? N GLY A 116 AA 3 4 N ASP A 133 ? N ASP A 133 O ASN A 141 ? O ASN A 141 AA 4 5 N PHE A 148 ? N PHE A 148 O VAL A 202 ? O VAL A 202 AA 5 6 N THR A 203 ? N THR A 203 O VAL A 186 ? O VAL A 186 AB 1 2 N ILE A 82 ? N ILE A 82 O VAL A 110 ? O VAL A 110 AB 2 3 O ARG A 113 ? O ARG A 113 N GLY A 116 ? N GLY A 116 AB 3 4 N SER A 128 ? N SER A 128 O LEU A 52 ? O LEU A 52 AB 4 5 N HIS A 63 ? N HIS A 63 O ASN A 32 ? O ASN A 32 AB 5 6 N VAL A 33 ? N VAL A 33 O ASP A 159 ? O ASP A 159 AC 1 2 N ILE A 82 ? N ILE A 82 O VAL A 110 ? O VAL A 110 AC 2 3 O ARG A 113 ? O ARG A 113 N GLY A 116 ? N GLY A 116 AC 3 4 N ASP A 133 ? N ASP A 133 O ASN A 141 ? O ASN A 141 AC 4 5 N GLY A 149 ? N GLY A 149 O VAL A 93 ? O VAL A 93 AD 1 2 N HIS A 181 ? N HIS A 181 O LEU A 207 ? O LEU A 207 AE 1 2 N ILE A 82 ? N ILE A 82 O VAL A 110 ? O VAL A 110 AE 2 3 O ARG A 113 ? O ARG A 113 N GLY A 116 ? N GLY A 116 AE 3 4 N ASP A 133 ? N ASP A 133 O ASN A 141 ? O ASN A 141 AE 4 5 N PHE A 148 ? N PHE A 148 O VAL A 202 ? O VAL A 202 AE 5 6 N LYS A 209 ? N LYS A 209 O GLU A 179 ? O GLU A 179 AF 1 2 N ILE A 190 ? N ILE A 190 O TYR A 199 ? O TYR A 199 # 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 ? ? ? ? 2 'BINDING SITE FOR RESIDUE EDO A 1218' AC2 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE EDO A 1219' AC3 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE EDO A 1220' AC4 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE EDO A 1221' AC5 Software ? ? ? ? 4 'Binding site for Mono-Saccharide NAG A1216 bound to ASN A 32' AC6 Software ? ? ? ? 11 'Binding site for Mono-Saccharide NAG A1217 bound to ASN A 145' # 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 2 TYR A 55 ? TYR A 55 . ? 1_555 ? 2 AC1 2 HOH H . ? HOH A 2201 . ? 1_555 ? 3 AC2 7 ASN A 96 ? ASN A 96 . ? 1_555 ? 4 AC2 7 ASN A 145 ? ASN A 145 . ? 1_555 ? 5 AC2 7 THR A 147 ? THR A 147 . ? 1_555 ? 6 AC2 7 NAG C . ? NAG A 1217 . ? 1_555 ? 7 AC2 7 HOH H . ? HOH A 2187 . ? 1_555 ? 8 AC2 7 HOH H . ? HOH A 2202 . ? 1_555 ? 9 AC2 7 HOH H . ? HOH A 2203 . ? 1_555 ? 10 AC3 3 TYR A 199 ? TYR A 199 . ? 1_555 ? 11 AC3 3 HOH H . ? HOH A 2204 . ? 1_555 ? 12 AC3 3 HOH H . ? HOH A 2205 . ? 1_555 ? 13 AC4 1 HOH H . ? HOH A 2125 . ? 1_555 ? 14 AC5 4 VAL A 30 ? VAL A 30 . ? 1_555 ? 15 AC5 4 ASN A 32 ? ASN A 32 . ? 1_555 ? 16 AC5 4 ARG A 48 ? ARG A 48 . ? 1_655 ? 17 AC5 4 HOH H . ? HOH A 2041 . ? 1_555 ? 18 AC6 11 GLN A 143 ? GLN A 143 . ? 1_555 ? 19 AC6 11 ASN A 145 ? ASN A 145 . ? 1_555 ? 20 AC6 11 VAL A 186 ? VAL A 186 . ? 1_555 ? 21 AC6 11 ASN A 188 ? ASN A 188 . ? 1_555 ? 22 AC6 11 THR A 203 ? THR A 203 . ? 1_555 ? 23 AC6 11 THR A 205 ? THR A 205 . ? 1_555 ? 24 AC6 11 EDO E . ? EDO A 1219 . ? 1_555 ? 25 AC6 11 HOH H . ? HOH A 2176 . ? 1_555 ? 26 AC6 11 HOH H . ? HOH A 2187 . ? 1_555 ? 27 AC6 11 HOH H . ? HOH A 2198 . ? 1_555 ? 28 AC6 11 HOH H . ? HOH A 2200 . ? 1_555 ? # _database_PDB_matrix.entry_id 4D01 _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 4D01 _atom_sites.fract_transf_matrix[1][1] 0.020194 _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] 0.015560 _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] 0.012478 _atom_sites.fract_transf_vector[1] 0.00000 _atom_sites.fract_transf_vector[2] 0.00000 _atom_sites.fract_transf_vector[3] 0.00000 # loop_ _atom_type.symbol C N O S # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 N N . ASP A 1 2 ? 49.434 53.901 -0.821 1.00 91.78 ? 2 ASP A N 1 ATOM 2 C CA . ASP A 1 2 ? 50.455 53.429 0.114 1.00 95.18 ? 2 ASP A CA 1 ATOM 3 C C . ASP A 1 2 ? 49.886 52.395 1.092 1.00 87.15 ? 2 ASP A C 1 ATOM 4 O O . ASP A 1 2 ? 50.265 52.341 2.267 1.00 89.07 ? 2 ASP A O 1 ATOM 5 C CB . ASP A 1 2 ? 51.084 54.605 0.873 1.00 100.46 ? 2 ASP A CB 1 ATOM 6 C CG . ASP A 1 2 ? 50.051 55.518 1.506 1.00 99.73 ? 2 ASP A CG 1 ATOM 7 O OD1 . ASP A 1 2 ? 49.531 55.174 2.593 1.00 93.34 -1 2 ASP A OD1 1 ATOM 8 O OD2 . ASP A 1 2 ? 49.767 56.584 0.913 1.00 98.92 ? 2 ASP A OD2 1 ATOM 9 N N . GLY A 1 3 ? 48.974 51.578 0.581 1.00 70.54 ? 3 GLY A N 1 ATOM 10 C CA . GLY A 1 3 ? 48.476 50.421 1.305 1.00 69.22 ? 3 GLY A CA 1 ATOM 11 C C . GLY A 1 3 ? 49.395 49.237 1.080 1.00 64.81 ? 3 GLY A C 1 ATOM 12 O O . GLY A 1 3 ? 49.162 48.144 1.620 1.00 59.22 ? 3 GLY A O 1 ATOM 13 N N . LYS A 1 4 ? 50.446 49.464 0.286 1.00 67.57 ? 4 LYS A N 1 ATOM 14 C CA . LYS A 1 4 ? 51.438 48.438 -0.011 1.00 68.27 ? 4 LYS A CA 1 ATOM 15 C C . LYS A 1 4 ? 51.898 47.762 1.249 1.00 59.55 ? 4 LYS A C 1 ATOM 16 O O . LYS A 1 4 ? 52.035 46.544 1.289 1.00 62.40 ? 4 LYS A O 1 ATOM 17 C CB . LYS A 1 4 ? 52.663 49.028 -0.696 1.00 71.04 ? 4 LYS A CB 1 ATOM 18 C CG . LYS A 1 4 ? 53.735 47.986 -1.017 1.00 81.30 ? 4 LYS A CG 1 ATOM 19 C CD . LYS A 1 4 ? 54.966 48.602 -1.690 1.00 86.63 ? 4 LYS A CD 1 ATOM 20 C CE . LYS A 1 4 ? 55.978 47.533 -2.083 1.00 91.12 ? 4 LYS A CE 1 ATOM 21 N NZ . LYS A 1 4 ? 57.161 48.120 -2.783 1.00 100.06 1 4 LYS A NZ 1 ATOM 22 N N . TYR A 1 5 ? 52.159 48.548 2.287 1.00 56.28 ? 5 TYR A N 1 ATOM 23 C CA . TYR A 1 5 ? 52.599 47.940 3.539 1.00 55.88 ? 5 TYR A CA 1 ATOM 24 C C . TYR A 1 5 ? 51.488 47.187 4.249 1.00 58.09 ? 5 TYR A C 1 ATOM 25 O O . TYR A 1 5 ? 51.725 46.079 4.740 1.00 53.47 ? 5 TYR A O 1 ATOM 26 C CB . TYR A 1 5 ? 53.299 48.968 4.428 1.00 55.01 ? 5 TYR A CB 1 ATOM 27 C CG . TYR A 1 5 ? 54.689 49.206 3.910 1.00 63.29 ? 5 TYR A CG 1 ATOM 28 C CD1 . TYR A 1 5 ? 55.645 48.208 3.998 1.00 74.42 ? 5 TYR A CD1 1 ATOM 29 C CD2 . TYR A 1 5 ? 55.033 50.384 3.274 1.00 67.24 ? 5 TYR A CD2 1 ATOM 30 C CE1 . TYR A 1 5 ? 56.916 48.387 3.502 1.00 77.87 ? 5 TYR A CE1 1 ATOM 31 C CE2 . TYR A 1 5 ? 56.309 50.576 2.782 1.00 77.08 ? 5 TYR A CE2 1 ATOM 32 C CZ . TYR A 1 5 ? 57.245 49.569 2.897 1.00 82.64 ? 5 TYR A CZ 1 ATOM 33 O OH . TYR A 1 5 ? 58.526 49.726 2.409 1.00 87.25 ? 5 TYR A OH 1 ATOM 34 N N . ALA A 1 6 ? 50.270 47.725 4.276 1.00 45.33 ? 6 ALA A N 1 ATOM 35 C CA . ALA A 1 6 ? 49.166 46.967 4.864 1.00 44.19 ? 6 ALA A CA 1 ATOM 36 C C . ALA A 1 6 ? 48.970 45.594 4.169 1.00 50.14 ? 6 ALA A C 1 ATOM 37 O O . ALA A 1 6 ? 48.634 44.609 4.826 1.00 48.03 ? 6 ALA A O 1 ATOM 38 C CB . ALA A 1 6 ? 47.879 47.781 4.829 1.00 50.95 ? 6 ALA A CB 1 ATOM 39 N N . GLN A 1 7 ? 49.179 45.521 2.849 1.00 51.99 ? 7 GLN A N 1 ATOM 40 C CA . GLN A 1 7 ? 49.062 44.245 2.144 1.00 53.28 ? 7 GLN A CA 1 ATOM 41 C C . GLN A 1 7 ? 50.208 43.297 2.492 1.00 54.56 ? 7 GLN A C 1 ATOM 42 O O . GLN A 1 7 ? 50.004 42.082 2.656 1.00 55.14 ? 7 GLN A O 1 ATOM 43 C CB . GLN A 1 7 ? 49.093 44.435 0.632 1.00 52.05 ? 7 GLN A CB 1 ATOM 44 C CG . GLN A 1 7 ? 48.054 45.351 0.050 1.00 57.08 ? 7 GLN A CG 1 ATOM 45 C CD . GLN A 1 7 ? 48.288 45.583 -1.421 1.00 70.32 ? 7 GLN A CD 1 ATOM 46 O OE1 . GLN A 1 7 ? 48.555 44.644 -2.167 1.00 77.18 ? 7 GLN A OE1 1 ATOM 47 N NE2 . GLN A 1 7 ? 48.215 46.837 -1.845 1.00 78.70 ? 7 GLN A NE2 1 ATOM 48 N N . LYS A 1 8 ? 51.420 43.835 2.552 1.00 54.24 ? 8 LYS A N 1 ATOM 49 C CA . LYS A 1 8 ? 52.570 43.021 2.911 1.00 56.04 ? 8 LYS A CA 1 ATOM 50 C C . LYS A 1 8 ? 52.291 42.436 4.290 1.00 51.06 ? 8 LYS A C 1 ATOM 51 O O . LYS A 1 8 ? 52.382 41.220 4.484 1.00 56.99 ? 8 LYS A O 1 ATOM 52 C CB . LYS A 1 8 ? 53.865 43.840 2.894 1.00 59.70 ? 8 LYS A CB 1 ATOM 53 C CG . LYS A 1 8 ? 55.080 43.171 3.560 1.00 69.61 ? 8 LYS A CG 1 ATOM 54 C CD . LYS A 1 8 ? 56.125 42.666 2.571 1.00 79.23 ? 8 LYS A CD 1 ATOM 55 C CE . LYS A 1 8 ? 57.503 42.472 3.242 1.00 80.23 ? 8 LYS A CE 1 ATOM 56 N NZ . LYS A 1 8 ? 57.505 41.442 4.356 1.00 72.12 1 8 LYS A NZ 1 ATOM 57 N N . LEU A 1 9 ? 51.919 43.291 5.242 1.00 47.80 ? 9 LEU A N 1 ATOM 58 C CA . LEU A 1 9 ? 51.616 42.821 6.608 1.00 46.03 ? 9 LEU A CA 1 ATOM 59 C C . LEU A 1 9 ? 50.593 41.706 6.602 1.00 42.62 ? 9 LEU A C 1 ATOM 60 O O . LEU A 1 9 ? 50.793 40.650 7.222 1.00 42.65 ? 9 LEU A O 1 ATOM 61 C CB . LEU A 1 9 ? 51.104 43.981 7.489 1.00 50.19 ? 9 LEU A CB 1 ATOM 62 C CG . LEU A 1 9 ? 50.738 43.543 8.911 1.00 51.35 ? 9 LEU A CG 1 ATOM 63 C CD1 . LEU A 1 9 ? 51.980 43.043 9.645 1.00 44.07 ? 9 LEU A CD1 1 ATOM 64 C CD2 . LEU A 1 9 ? 50.028 44.641 9.689 1.00 51.06 ? 9 LEU A CD2 1 ATOM 65 N N . PHE A 1 10 ? 49.499 41.924 5.881 1.00 49.80 ? 10 PHE A N 1 ATOM 66 C CA . PHE A 1 10 ? 48.433 40.943 5.839 1.00 47.73 ? 10 PHE A CA 1 ATOM 67 C C . PHE A 1 10 ? 48.908 39.618 5.287 1.00 47.05 ? 10 PHE A C 1 ATOM 68 O O . PHE A 1 10 ? 48.622 38.574 5.841 1.00 51.20 ? 10 PHE A O 1 ATOM 69 C CB . PHE A 1 10 ? 47.254 41.413 5.012 1.00 50.33 ? 10 PHE A CB 1 ATOM 70 C CG . PHE A 1 10 ? 46.166 40.412 4.951 1.00 56.39 ? 10 PHE A CG 1 ATOM 71 C CD1 . PHE A 1 10 ? 46.222 39.366 4.042 1.00 55.21 ? 10 PHE A CD1 1 ATOM 72 C CD2 . PHE A 1 10 ? 45.101 40.481 5.830 1.00 51.13 ? 10 PHE A CD2 1 ATOM 73 C CE1 . PHE A 1 10 ? 45.219 38.423 4.008 1.00 58.80 ? 10 PHE A CE1 1 ATOM 74 C CE2 . PHE A 1 10 ? 44.098 39.534 5.798 1.00 51.20 ? 10 PHE A CE2 1 ATOM 75 C CZ . PHE A 1 10 ? 44.154 38.515 4.902 1.00 51.16 ? 10 PHE A CZ 1 ATOM 76 N N . ASN A 1 11 ? 49.601 39.667 4.162 1.00 48.99 ? 11 ASN A N 1 ATOM 77 C CA . ASN A 1 11 ? 50.137 38.447 3.583 1.00 59.35 ? 11 ASN A CA 1 ATOM 78 C C . ASN A 1 11 ? 51.076 37.762 4.566 1.00 55.08 ? 11 ASN A C 1 ATOM 79 O O . ASN A 1 11 ? 51.042 36.550 4.726 1.00 54.55 ? 11 ASN A O 1 ATOM 80 C CB . ASN A 1 11 ? 50.855 38.762 2.278 1.00 50.84 ? 11 ASN A CB 1 ATOM 81 C CG . ASN A 1 11 ? 49.895 38.984 1.130 1.00 67.44 ? 11 ASN A CG 1 ATOM 82 O OD1 . ASN A 1 11 ? 48.799 38.424 1.116 1.00 75.92 ? 11 ASN A OD1 1 ATOM 83 N ND2 . ASN A 1 11 ? 50.307 39.799 0.146 1.00 66.56 ? 11 ASN A ND2 1 ATOM 84 N N . ASP A 1 12 ? 51.892 38.557 5.252 1.00 53.07 ? 12 ASP A N 1 ATOM 85 C CA . ASP A 1 12 ? 52.816 38.026 6.234 1.00 49.91 ? 12 ASP A CA 1 ATOM 86 C C . ASP A 1 12 ? 52.122 37.429 7.460 1.00 53.03 ? 12 ASP A C 1 ATOM 87 O O . ASP A 1 12 ? 52.554 36.404 7.979 1.00 47.37 ? 12 ASP A O 1 ATOM 88 C CB . ASP A 1 12 ? 53.782 39.116 6.688 1.00 47.19 ? 12 ASP A CB 1 ATOM 89 C CG . ASP A 1 12 ? 54.807 39.462 5.613 1.00 62.15 ? 12 ASP A CG 1 ATOM 90 O OD1 . ASP A 1 12 ? 55.026 38.608 4.751 1.00 57.20 ? 12 ASP A OD1 1 ATOM 91 O OD2 . ASP A 1 12 ? 55.385 40.569 5.629 1.00 67.16 -1 12 ASP A OD2 1 ATOM 92 N N . LEU A 1 13 ? 51.104 38.094 7.953 1.00 45.72 ? 13 LEU A N 1 ATOM 93 C CA . LEU A 1 13 ? 50.460 37.679 9.191 1.00 43.27 ? 13 LEU A CA 1 ATOM 94 C C . LEU A 1 13 ? 49.803 36.361 8.978 1.00 41.42 ? 13 LEU A C 1 ATOM 95 O O . LEU A 1 13 ? 49.783 35.504 9.820 1.00 41.55 ? 13 LEU A O 1 ATOM 96 C CB . LEU A 1 13 ? 49.409 38.676 9.608 1.00 37.71 ? 13 LEU A CB 1 ATOM 97 C CG . LEU A 1 13 ? 49.882 39.951 10.268 1.00 42.69 ? 13 LEU A CG 1 ATOM 98 C CD1 . LEU A 1 13 ? 48.736 40.897 10.442 1.00 45.72 ? 13 LEU A CD1 1 ATOM 99 C CD2 . LEU A 1 13 ? 50.547 39.710 11.592 1.00 45.72 ? 13 LEU A CD2 1 ATOM 100 N N . PHE A 1 14 ? 49.220 36.241 7.821 1.00 40.04 ? 14 PHE A N 1 ATOM 101 C CA . PHE A 1 14 ? 48.460 35.096 7.505 1.00 46.77 ? 14 PHE A CA 1 ATOM 102 C C . PHE A 1 14 ? 49.195 34.064 6.643 1.00 48.93 ? 14 PHE A C 1 ATOM 103 O O . PHE A 1 14 ? 48.546 33.320 6.140 1.00 47.60 ? 14 PHE A O 1 ATOM 104 C CB . PHE A 1 14 ? 47.109 35.515 6.943 1.00 45.51 ? 14 PHE A CB 1 ATOM 105 C CG . PHE A 1 14 ? 46.267 36.339 7.901 1.00 42.44 ? 14 PHE A CG 1 ATOM 106 C CD1 . PHE A 1 14 ? 45.509 35.731 8.865 1.00 44.50 ? 14 PHE A CD1 1 ATOM 107 C CD2 . PHE A 1 14 ? 46.231 37.714 7.835 1.00 46.45 ? 14 PHE A CD2 1 ATOM 108 C CE1 . PHE A 1 14 ? 44.747 36.458 9.740 1.00 40.94 ? 14 PHE A CE1 1 ATOM 109 C CE2 . PHE A 1 14 ? 45.470 38.454 8.713 1.00 41.90 ? 14 PHE A CE2 1 ATOM 110 C CZ . PHE A 1 14 ? 44.726 37.821 9.672 1.00 43.83 ? 14 PHE A CZ 1 ATOM 111 N N . GLU A 1 15 ? 50.513 34.006 6.478 1.00 44.46 ? 15 GLU A N 1 ATOM 112 C CA . GLU A 1 15 ? 51.141 32.934 5.663 1.00 47.22 ? 15 GLU A CA 1 ATOM 113 C C . GLU A 1 15 ? 50.806 31.581 6.313 1.00 49.40 ? 15 GLU A C 1 ATOM 114 O O . GLU A 1 15 ? 50.566 30.604 5.661 1.00 61.06 ? 15 GLU A O 1 ATOM 115 C CB . GLU A 1 15 ? 52.626 33.125 5.482 1.00 60.55 ? 15 GLU A CB 1 ATOM 116 C CG . GLU A 1 15 ? 53.438 33.069 6.734 1.00 66.08 ? 15 GLU A CG 1 ATOM 117 C CD . GLU A 1 15 ? 54.856 32.650 6.437 1.00 89.23 ? 15 GLU A CD 1 ATOM 118 O OE1 . GLU A 1 15 ? 55.370 33.102 5.397 1.00 97.20 -1 15 GLU A OE1 1 ATOM 119 O OE2 . GLU A 1 15 ? 55.445 31.859 7.206 1.00 94.80 ? 15 GLU A OE2 1 ATOM 120 N N . ASP A 1 16 ? 50.796 31.550 7.624 1.00 53.25 ? 16 ASP A N 1 ATOM 121 C CA . ASP A 1 16 ? 50.631 30.313 8.365 1.00 53.85 ? 16 ASP A CA 1 ATOM 122 C C . ASP A 1 16 ? 49.899 30.746 9.619 1.00 56.31 ? 16 ASP A C 1 ATOM 123 O O . ASP A 1 16 ? 50.530 31.225 10.560 1.00 55.20 ? 16 ASP A O 1 ATOM 124 C CB . ASP A 1 16 ? 51.997 29.672 8.671 1.00 59.86 ? 16 ASP A CB 1 ATOM 125 C CG . ASP A 1 16 ? 51.873 28.236 9.212 1.00 69.08 ? 16 ASP A CG 1 ATOM 126 O OD1 . ASP A 1 16 ? 50.849 27.932 9.852 1.00 75.17 ? 16 ASP A OD1 1 ATOM 127 O OD2 . ASP A 1 16 ? 52.787 27.405 8.988 1.00 75.89 -1 16 ASP A OD2 1 ATOM 128 N N . TYR A 1 17 ? 48.570 30.645 9.603 1.00 43.49 ? 17 TYR A N 1 ATOM 129 C CA . TYR A 1 17 ? 47.726 31.176 10.708 1.00 44.43 ? 17 TYR A CA 1 ATOM 130 C C . TYR A 1 17 ? 46.374 30.521 10.640 1.00 47.48 ? 17 TYR A C 1 ATOM 131 O O . TYR A 1 17 ? 45.792 30.434 9.571 1.00 44.42 ? 17 TYR A O 1 ATOM 132 C CB . TYR A 1 17 ? 47.509 32.703 10.656 1.00 40.94 ? 17 TYR A CB 1 ATOM 133 C CG . TYR A 1 17 ? 46.535 33.187 11.759 1.00 41.56 ? 17 TYR A CG 1 ATOM 134 C CD1 . TYR A 1 17 ? 47.000 33.471 13.035 1.00 41.11 ? 17 TYR A CD1 1 ATOM 135 C CD2 . TYR A 1 17 ? 45.162 33.298 11.528 1.00 38.55 ? 17 TYR A CD2 1 ATOM 136 C CE1 . TYR A 1 17 ? 46.119 33.839 14.090 1.00 35.61 ? 17 TYR A CE1 1 ATOM 137 C CE2 . TYR A 1 17 ? 44.278 33.678 12.536 1.00 38.08 ? 17 TYR A CE2 1 ATOM 138 C CZ . TYR A 1 17 ? 44.773 33.966 13.827 1.00 35.88 ? 17 TYR A CZ 1 ATOM 139 O OH . TYR A 1 17 ? 43.943 34.349 14.875 1.00 36.97 ? 17 TYR A OH 1 ATOM 140 N N . SER A 1 18 ? 45.863 30.044 11.769 1.00 39.42 ? 18 SER A N 1 ATOM 141 C CA . SER A 1 18 ? 44.598 29.330 11.733 1.00 39.69 ? 18 SER A CA 1 ATOM 142 C C . SER A 1 18 ? 43.600 30.056 12.595 1.00 37.66 ? 18 SER A C 1 ATOM 143 O O . SER A 1 18 ? 43.848 30.280 13.788 1.00 37.01 ? 18 SER A O 1 ATOM 144 C CB . SER A 1 18 ? 44.759 27.906 12.242 1.00 43.71 ? 18 SER A CB 1 ATOM 145 O OG . SER A 1 18 ? 43.479 27.347 12.470 1.00 49.35 ? 18 SER A OG 1 ATOM 146 N N . ASN A 1 19 ? 42.454 30.421 12.027 1.00 40.74 ? 19 ASN A N 1 ATOM 147 C CA . ASN A 1 19 ? 41.421 31.042 12.868 1.00 37.59 ? 19 ASN A CA 1 ATOM 148 C C . ASN A 1 19 ? 40.686 30.055 13.786 1.00 41.30 ? 19 ASN A C 1 ATOM 149 O O . ASN A 1 19 ? 39.772 30.441 14.499 1.00 38.06 ? 19 ASN A O 1 ATOM 150 C CB . ASN A 1 19 ? 40.413 31.803 12.007 1.00 38.66 ? 19 ASN A CB 1 ATOM 151 C CG . ASN A 1 19 ? 39.571 30.895 11.163 1.00 48.56 ? 19 ASN A CG 1 ATOM 152 O OD1 . ASN A 1 19 ? 39.716 29.680 11.227 1.00 50.77 ? 19 ASN A OD1 1 ATOM 153 N ND2 . ASN A 1 19 ? 38.732 31.482 10.300 1.00 46.93 ? 19 ASN A ND2 1 ATOM 154 N N . ALA A 1 20 ? 41.102 28.789 13.796 1.00 40.11 ? 20 ALA A N 1 ATOM 155 C CA . ALA A 1 20 ? 40.481 27.783 14.642 1.00 41.93 ? 20 ALA A CA 1 ATOM 156 C C . ALA A 1 20 ? 41.317 27.489 15.904 1.00 43.66 ? 20 ALA A C 1 ATOM 157 O O . ALA A 1 20 ? 40.842 26.846 16.834 1.00 46.12 ? 20 ALA A O 1 ATOM 158 C CB . ALA A 1 20 ? 40.246 26.514 13.849 1.00 42.12 ? 20 ALA A CB 1 ATOM 159 N N . LEU A 1 21 ? 42.558 27.962 15.938 1.00 37.31 ? 21 LEU A N 1 ATOM 160 C CA . LEU A 1 21 ? 43.480 27.672 17.036 1.00 36.44 ? 21 LEU A CA 1 ATOM 161 C C . LEU A 1 21 ? 43.506 28.805 18.042 1.00 37.68 ? 21 LEU A C 1 ATOM 162 O O . LEU A 1 21 ? 43.843 29.966 17.688 1.00 35.07 ? 21 LEU A O 1 ATOM 163 C CB . LEU A 1 21 ? 44.900 27.448 16.517 1.00 44.53 ? 21 LEU A CB 1 ATOM 164 C CG . LEU A 1 21 ? 45.985 27.015 17.531 1.00 50.05 ? 21 LEU A CG 1 ATOM 165 C CD1 . LEU A 1 21 ? 45.773 25.599 18.051 1.00 50.23 ? 21 LEU A CD1 1 ATOM 166 C CD2 . LEU A 1 21 ? 47.398 27.145 16.957 1.00 57.95 ? 21 LEU A CD2 1 ATOM 167 N N . ARG A 1 22 ? 43.224 28.472 19.298 1.00 38.73 ? 22 ARG A N 1 ATOM 168 C CA . ARG A 1 22 ? 43.251 29.471 20.382 1.00 34.33 ? 22 ARG A CA 1 ATOM 169 C C . ARG A 1 22 ? 44.628 30.079 20.421 1.00 30.60 ? 22 ARG A C 1 ATOM 170 O O . ARG A 1 22 ? 45.634 29.378 20.568 1.00 36.01 ? 22 ARG A O 1 ATOM 171 C CB . ARG A 1 22 ? 42.885 28.835 21.728 1.00 37.24 ? 22 ARG A CB 1 ATOM 172 C CG . ARG A 1 22 ? 42.557 29.831 22.812 1.00 32.76 ? 22 ARG A CG 1 ATOM 173 C CD . ARG A 1 22 ? 41.932 29.108 24.045 1.00 33.82 ? 22 ARG A CD 1 ATOM 174 N NE . ARG A 1 22 ? 42.796 27.999 24.379 1.00 34.57 ? 22 ARG A NE 1 ATOM 175 C CZ . ARG A 1 22 ? 43.739 28.039 25.302 1.00 31.71 ? 22 ARG A CZ 1 ATOM 176 N NH1 . ARG A 1 22 ? 43.900 29.119 26.078 1.00 34.51 1 22 ARG A NH1 1 ATOM 177 N NH2 . ARG A 1 22 ? 44.523 26.993 25.441 1.00 33.76 ? 22 ARG A NH2 1 ATOM 178 N N . PRO A 1 23 ? 44.695 31.391 20.261 1.00 31.72 ? 23 PRO A N 1 ATOM 179 C CA . PRO A 1 23 ? 45.998 31.984 19.963 1.00 37.99 ? 23 PRO A CA 1 ATOM 180 C C . PRO A 1 23 ? 46.852 32.278 21.178 1.00 40.22 ? 23 PRO A C 1 ATOM 181 O O . PRO A 1 23 ? 47.103 33.443 21.521 1.00 37.09 ? 23 PRO A O 1 ATOM 182 C CB . PRO A 1 23 ? 45.630 33.262 19.193 1.00 38.43 ? 23 PRO A CB 1 ATOM 183 C CG . PRO A 1 23 ? 44.248 33.633 19.695 1.00 32.77 ? 23 PRO A CG 1 ATOM 184 C CD . PRO A 1 23 ? 43.572 32.330 20.056 1.00 31.66 ? 23 PRO A CD 1 ATOM 185 N N . VAL A 1 24 ? 47.320 31.221 21.816 1.00 36.40 ? 24 VAL A N 1 ATOM 186 C CA . VAL A 1 24 ? 48.248 31.344 22.934 1.00 34.05 ? 24 VAL A CA 1 ATOM 187 C C . VAL A 1 24 ? 49.511 30.592 22.592 1.00 45.28 ? 24 VAL A C 1 ATOM 188 O O . VAL A 1 24 ? 49.464 29.643 21.829 1.00 43.64 ? 24 VAL A O 1 ATOM 189 C CB . VAL A 1 24 ? 47.644 30.799 24.251 1.00 35.08 ? 24 VAL A CB 1 ATOM 190 C CG1 . VAL A 1 24 ? 46.400 31.582 24.618 1.00 39.97 ? 24 VAL A CG1 1 ATOM 191 C CG2 . VAL A 1 24 ? 47.300 29.331 24.124 1.00 36.98 ? 24 VAL A CG2 1 ATOM 192 N N . GLU A 1 25 ? 50.631 31.017 23.164 1.00 47.16 ? 25 GLU A N 1 ATOM 193 C CA . GLU A 1 25 ? 51.931 30.440 22.858 1.00 58.82 ? 25 GLU A CA 1 ATOM 194 C C . GLU A 1 25 ? 52.038 29.081 23.538 1.00 59.50 ? 25 GLU A C 1 ATOM 195 O O . GLU A 1 25 ? 52.712 28.181 23.064 1.00 67.13 ? 25 GLU A O 1 ATOM 196 C CB . GLU A 1 25 ? 53.041 31.380 23.341 1.00 65.10 ? 25 GLU A CB 1 ATOM 197 C CG . GLU A 1 25 ? 52.943 32.822 22.795 1.00 74.62 ? 25 GLU A CG 1 ATOM 198 C CD . GLU A 1 25 ? 52.017 33.753 23.614 1.00 81.59 ? 25 GLU A CD 1 ATOM 199 O OE1 . GLU A 1 25 ? 51.126 33.266 24.357 1.00 67.64 ? 25 GLU A OE1 1 ATOM 200 O OE2 . GLU A 1 25 ? 52.184 34.996 23.508 1.00 86.86 -1 25 GLU A OE2 1 ATOM 201 N N . ASP A 1 26 ? 51.338 28.935 24.648 1.00 42.00 ? 26 ASP A N 1 ATOM 202 C CA . ASP A 1 26 ? 51.385 27.695 25.421 1.00 48.79 ? 26 ASP A CA 1 ATOM 203 C C . ASP A 1 26 ? 49.974 27.289 25.808 1.00 55.67 ? 26 ASP A C 1 ATOM 204 O O . ASP A 1 26 ? 49.190 28.109 26.271 1.00 44.52 ? 26 ASP A O 1 ATOM 205 C CB . ASP A 1 26 ? 52.281 27.887 26.649 1.00 63.39 ? 26 ASP A CB 1 ATOM 206 C CG . ASP A 1 26 ? 51.966 26.908 27.786 1.00 78.92 ? 26 ASP A CG 1 ATOM 207 O OD1 . ASP A 1 26 ? 51.189 25.946 27.579 1.00 80.20 ? 26 ASP A OD1 1 ATOM 208 O OD2 . ASP A 1 26 ? 52.515 27.105 28.896 1.00 77.34 -1 26 ASP A OD2 1 ATOM 209 N N . THR A 1 27 ? 49.634 26.020 25.639 1.00 47.99 ? 27 THR A N 1 ATOM 210 C CA . THR A 1 27 ? 48.222 25.664 25.700 1.00 55.42 ? 27 THR A CA 1 ATOM 211 C C . THR A 1 27 ? 47.638 25.802 27.111 1.00 38.89 ? 27 THR A C 1 ATOM 212 O O . THR A 1 27 ? 46.452 26.060 27.256 1.00 43.18 ? 27 THR A O 1 ATOM 213 C CB . THR A 1 27 ? 47.980 24.254 25.140 1.00 59.34 ? 27 THR A CB 1 ATOM 214 O OG1 . THR A 1 27 ? 49.034 23.393 25.569 1.00 58.47 ? 27 THR A OG1 1 ATOM 215 C CG2 . THR A 1 27 ? 47.972 24.298 23.623 1.00 61.99 ? 27 THR A CG2 1 ATOM 216 N N . ASP A 1 28 ? 48.442 25.653 28.151 1.00 39.74 ? 28 ASP A N 1 ATOM 217 C CA . ASP A 1 28 ? 47.857 25.706 29.486 1.00 49.15 ? 28 ASP A CA 1 ATOM 218 C C . ASP A 1 28 ? 47.734 27.152 29.956 1.00 47.87 ? 28 ASP A C 1 ATOM 219 O O . ASP A 1 28 ? 47.363 27.405 31.093 1.00 59.70 ? 28 ASP A O 1 ATOM 220 C CB . ASP A 1 28 ? 48.618 24.853 30.499 1.00 58.87 ? 28 ASP A CB 1 ATOM 221 C CG . ASP A 1 28 ? 50.073 25.198 30.586 1.00 78.90 ? 28 ASP A CG 1 ATOM 222 O OD1 . ASP A 1 28 ? 50.396 26.403 30.580 1.00 84.88 -1 28 ASP A OD1 1 ATOM 223 O OD2 . ASP A 1 28 ? 50.897 24.255 30.675 1.00 86.99 ? 28 ASP A OD2 1 ATOM 224 N N . LYS A 1 29 ? 48.071 28.096 29.089 1.00 41.65 ? 29 LYS A N 1 ATOM 225 C CA . LYS A 1 29 ? 47.826 29.511 29.401 1.00 42.74 ? 29 LYS A CA 1 ATOM 226 C C . LYS A 1 29 ? 46.400 29.864 29.090 1.00 44.20 ? 29 LYS A C 1 ATOM 227 O O . LYS A 1 29 ? 45.811 29.357 28.146 1.00 43.06 ? 29 LYS A O 1 ATOM 228 C CB . LYS A 1 29 ? 48.755 30.447 28.610 1.00 44.10 ? 29 LYS A CB 1 ATOM 229 C CG . LYS A 1 29 ? 50.226 30.296 28.967 1.00 59.02 ? 29 LYS A CG 1 ATOM 230 C CD . LYS A 1 29 ? 50.457 30.028 30.462 1.00 68.66 ? 29 LYS A CD 1 ATOM 231 C CE . LYS A 1 29 ? 50.236 31.285 31.302 1.00 75.26 ? 29 LYS A CE 1 ATOM 232 N NZ . LYS A 1 29 ? 50.284 31.018 32.775 1.00 70.82 1 29 LYS A NZ 1 ATOM 233 N N . VAL A 1 30 ? 45.830 30.753 29.886 1.00 41.56 ? 30 VAL A N 1 ATOM 234 C CA . VAL A 1 30 ? 44.466 31.159 29.647 1.00 35.94 ? 30 VAL A CA 1 ATOM 235 C C . VAL A 1 30 ? 44.502 32.288 28.636 1.00 36.99 ? 30 VAL A C 1 ATOM 236 O O . VAL A 1 30 ? 45.490 32.993 28.522 1.00 46.70 ? 30 VAL A O 1 ATOM 237 C CB . VAL A 1 30 ? 43.806 31.684 30.944 1.00 42.40 ? 30 VAL A CB 1 ATOM 238 C CG1 . VAL A 1 30 ? 44.494 32.954 31.413 1.00 46.58 ? 30 VAL A CG1 1 ATOM 239 C CG2 . VAL A 1 30 ? 42.309 31.895 30.743 1.00 41.64 ? 30 VAL A CG2 1 ATOM 240 N N . LEU A 1 31 ? 43.425 32.484 27.918 1.00 31.54 ? 31 LEU A N 1 ATOM 241 C CA . LEU A 1 31 ? 43.303 33.708 27.140 1.00 32.12 ? 31 LEU A CA 1 ATOM 242 C C . LEU A 1 31 ? 42.148 34.543 27.696 1.00 29.04 ? 31 LEU A C 1 ATOM 243 O O . LEU A 1 31 ? 41.010 34.072 27.755 1.00 34.32 ? 31 LEU A O 1 ATOM 244 C CB . LEU A 1 31 ? 43.116 33.344 25.650 1.00 30.74 ? 31 LEU A CB 1 ATOM 245 C CG . LEU A 1 31 ? 43.032 34.473 24.611 1.00 37.00 ? 31 LEU A CG 1 ATOM 246 C CD1 . LEU A 1 31 ? 43.250 33.877 23.260 1.00 38.85 ? 31 LEU A CD1 1 ATOM 247 C CD2 . LEU A 1 31 ? 41.685 35.192 24.630 1.00 33.66 ? 31 LEU A CD2 1 ATOM 248 N N . ASN A 1 32 ? 42.446 35.792 28.093 1.00 29.98 ? 32 ASN A N 1 ATOM 249 C CA . ASN A 1 32 ? 41.481 36.689 28.689 1.00 28.12 ? 32 ASN A CA 1 ATOM 250 C C . ASN A 1 32 ? 40.849 37.597 27.681 1.00 34.50 ? 32 ASN A C 1 ATOM 251 O O . ASN A 1 32 ? 41.531 38.135 26.770 1.00 36.09 ? 32 ASN A O 1 ATOM 252 C CB . ASN A 1 32 ? 42.164 37.610 29.709 1.00 32.58 ? 32 ASN A CB 1 ATOM 253 C CG . ASN A 1 32 ? 42.853 36.848 30.845 1.00 40.18 ? 32 ASN A CG 1 ATOM 254 O OD1 . ASN A 1 32 ? 42.302 35.883 31.416 1.00 36.76 ? 32 ASN A OD1 1 ATOM 255 N ND2 . ASN A 1 32 ? 44.075 37.278 31.164 1.00 44.98 ? 32 ASN A ND2 1 ATOM 256 N N . VAL A 1 33 ? 39.549 37.780 27.852 1.00 29.07 ? 33 VAL A N 1 ATOM 257 C CA . VAL A 1 33 ? 38.758 38.624 26.998 1.00 27.27 ? 33 VAL A CA 1 ATOM 258 C C . VAL A 1 33 ? 37.951 39.565 27.862 1.00 32.67 ? 33 VAL A C 1 ATOM 259 O O . VAL A 1 33 ? 37.293 39.137 28.828 1.00 34.08 ? 33 VAL A O 1 ATOM 260 C CB . VAL A 1 33 ? 37.760 37.801 26.200 1.00 27.94 ? 33 VAL A CB 1 ATOM 261 C CG1 . VAL A 1 33 ? 37.024 38.717 25.165 1.00 32.79 ? 33 VAL A CG1 1 ATOM 262 C CG2 . VAL A 1 33 ? 38.433 36.656 25.501 1.00 36.74 ? 33 VAL A CG2 1 ATOM 263 N N . THR A 1 34 ? 37.982 40.848 27.536 1.00 31.59 ? 34 THR A N 1 ATOM 264 C CA . THR A 1 34 ? 37.114 41.792 28.207 1.00 27.67 ? 34 THR A CA 1 ATOM 265 C C . THR A 1 34 ? 35.943 42.100 27.326 1.00 39.29 ? 34 THR A C 1 ATOM 266 O O . THR A 1 34 ? 36.057 42.135 26.083 1.00 36.16 ? 34 THR A O 1 ATOM 267 C CB . THR A 1 34 ? 37.844 43.112 28.608 1.00 37.49 ? 34 THR A CB 1 ATOM 268 O OG1 . THR A 1 34 ? 38.097 43.891 27.431 1.00 39.43 ? 34 THR A OG1 1 ATOM 269 C CG2 . THR A 1 34 ? 39.159 42.800 29.329 1.00 36.40 ? 34 THR A CG2 1 ATOM 270 N N . LEU A 1 35 ? 34.800 42.295 27.975 1.00 30.79 ? 35 LEU A N 1 ATOM 271 C CA . LEU A 1 35 ? 33.583 42.506 27.251 1.00 33.25 ? 35 LEU A CA 1 ATOM 272 C C . LEU A 1 35 ? 32.958 43.792 27.746 1.00 33.29 ? 35 LEU A C 1 ATOM 273 O O . LEU A 1 35 ? 32.927 44.052 28.944 1.00 33.83 ? 35 LEU A O 1 ATOM 274 C CB . LEU A 1 35 ? 32.645 41.328 27.507 1.00 31.64 ? 35 LEU A CB 1 ATOM 275 C CG . LEU A 1 35 ? 31.443 41.168 26.572 1.00 51.01 ? 35 LEU A CG 1 ATOM 276 C CD1 . LEU A 1 35 ? 30.650 39.940 26.905 1.00 57.45 ? 35 LEU A CD1 1 ATOM 277 C CD2 . LEU A 1 35 ? 30.538 42.360 26.650 1.00 63.92 ? 35 LEU A CD2 1 ATOM 278 N N . GLN A 1 36 ? 32.494 44.617 26.811 1.00 33.89 ? 36 GLN A N 1 ATOM 279 C CA . GLN A 1 36 ? 31.730 45.805 27.139 1.00 35.84 ? 36 GLN A CA 1 ATOM 280 C C . GLN A 1 36 ? 30.462 45.768 26.319 1.00 42.47 ? 36 GLN A C 1 ATOM 281 O O . GLN A 1 36 ? 30.484 45.414 25.107 1.00 37.75 ? 36 GLN A O 1 ATOM 282 C CB . GLN A 1 36 ? 32.522 47.056 26.808 1.00 32.82 ? 36 GLN A CB 1 ATOM 283 C CG . GLN A 1 36 ? 31.720 48.323 26.822 1.00 39.66 ? 36 GLN A CG 1 ATOM 284 C CD . GLN A 1 36 ? 32.600 49.473 26.553 1.00 47.84 ? 36 GLN A CD 1 ATOM 285 O OE1 . GLN A 1 36 ? 33.781 49.449 26.927 1.00 51.84 ? 36 GLN A OE1 1 ATOM 286 N NE2 . GLN A 1 36 ? 32.060 50.497 25.899 1.00 52.87 ? 36 GLN A NE2 1 ATOM 287 N N . ILE A 1 37 ? 29.350 46.094 26.982 1.00 38.34 ? 37 ILE A N 1 ATOM 288 C CA . ILE A 1 37 ? 28.079 46.099 26.295 1.00 39.19 ? 37 ILE A CA 1 ATOM 289 C C . ILE A 1 37 ? 27.654 47.522 26.273 1.00 39.42 ? 37 ILE A C 1 ATOM 290 O O . ILE A 1 37 ? 27.712 48.198 27.305 1.00 40.89 ? 37 ILE A O 1 ATOM 291 C CB . ILE A 1 37 ? 27.011 45.297 27.014 1.00 44.19 ? 37 ILE A CB 1 ATOM 292 C CG1 . ILE A 1 37 ? 27.338 43.800 27.003 1.00 46.61 ? 37 ILE A CG1 1 ATOM 293 C CG2 . ILE A 1 37 ? 25.680 45.533 26.362 1.00 49.21 ? 37 ILE A CG2 1 ATOM 294 C CD1 . ILE A 1 37 ? 27.309 43.149 25.677 1.00 56.73 ? 37 ILE A CD1 1 ATOM 295 N N . THR A 1 38 ? 27.236 47.987 25.092 1.00 39.87 ? 38 THR A N 1 ATOM 296 C CA . THR A 1 38 ? 26.663 49.300 24.953 1.00 36.48 ? 38 THR A CA 1 ATOM 297 C C . THR A 1 38 ? 25.241 49.099 24.502 1.00 47.73 ? 38 THR A C 1 ATOM 298 O O . THR A 1 38 ? 24.983 48.447 23.494 1.00 46.82 ? 38 THR A O 1 ATOM 299 C CB . THR A 1 38 ? 27.431 50.132 23.917 1.00 43.83 ? 38 THR A CB 1 ATOM 300 O OG1 . THR A 1 38 ? 28.762 50.356 24.395 1.00 46.81 ? 38 THR A OG1 1 ATOM 301 C CG2 . THR A 1 38 ? 26.741 51.471 23.662 1.00 46.47 ? 38 THR A CG2 1 ATOM 302 N N . LEU A 1 39 ? 24.290 49.615 25.267 1.00 39.84 ? 39 LEU A N 1 ATOM 303 C CA . LEU A 1 39 ? 22.912 49.415 24.885 1.00 38.83 ? 39 LEU A CA 1 ATOM 304 C C . LEU A 1 39 ? 22.597 50.451 23.805 1.00 48.62 ? 39 LEU A C 1 ATOM 305 O O . LEU A 1 39 ? 22.920 51.634 23.970 1.00 50.81 ? 39 LEU A O 1 ATOM 306 C CB . LEU A 1 39 ? 22.014 49.607 26.110 1.00 38.11 ? 39 LEU A CB 1 ATOM 307 C CG . LEU A 1 39 ? 20.526 49.784 25.832 1.00 42.95 ? 39 LEU A CG 1 ATOM 308 C CD1 . LEU A 1 39 ? 19.888 48.477 25.470 1.00 44.44 ? 39 LEU A CD1 1 ATOM 309 C CD2 . LEU A 1 39 ? 19.827 50.408 27.063 1.00 46.74 ? 39 LEU A CD2 1 ATOM 310 N N . SER A 1 40 ? 21.984 50.032 22.704 1.00 47.27 ? 40 SER A N 1 ATOM 311 C CA . SER A 1 40 ? 21.649 50.986 21.634 1.00 50.33 ? 40 SER A CA 1 ATOM 312 C C . SER A 1 40 ? 20.182 51.332 21.602 1.00 51.89 ? 40 SER A C 1 ATOM 313 O O . SER A 1 40 ? 19.799 52.454 21.245 1.00 55.41 ? 40 SER A O 1 ATOM 314 C CB . SER A 1 40 ? 22.021 50.430 20.257 1.00 54.30 ? 40 SER A CB 1 ATOM 315 O OG . SER A 1 40 ? 23.372 50.039 20.242 1.00 63.85 ? 40 SER A OG 1 ATOM 316 N N . GLN A 1 41 ? 19.352 50.364 21.955 1.00 46.05 ? 41 GLN A N 1 ATOM 317 C CA . GLN A 1 41 ? 17.923 50.568 21.899 1.00 49.90 ? 41 GLN A CA 1 ATOM 318 C C . GLN A 1 41 ? 17.186 49.445 22.603 1.00 51.13 ? 41 GLN A C 1 ATOM 319 O O . GLN A 1 41 ? 17.618 48.295 22.590 1.00 49.03 ? 41 GLN A O 1 ATOM 320 C CB . GLN A 1 41 ? 17.498 50.617 20.440 1.00 49.03 ? 41 GLN A CB 1 ATOM 321 C CG . GLN A 1 41 ? 16.015 50.506 20.208 1.00 57.42 ? 41 GLN A CG 1 ATOM 322 C CD . GLN A 1 41 ? 15.656 50.782 18.745 1.00 58.12 ? 41 GLN A CD 1 ATOM 323 O OE1 . GLN A 1 41 ? 16.537 50.848 17.877 1.00 57.93 ? 41 GLN A OE1 1 ATOM 324 N NE2 . GLN A 1 41 ? 14.373 50.945 18.472 1.00 55.63 ? 41 GLN A NE2 1 ATOM 325 N N . ILE A 1 42 ? 16.064 49.776 23.217 1.00 48.78 ? 42 ILE A N 1 ATOM 326 C CA . ILE A 1 42 ? 15.171 48.748 23.697 1.00 45.66 ? 42 ILE A CA 1 ATOM 327 C C . ILE A 1 42 ? 14.149 48.539 22.626 1.00 47.10 ? 42 ILE A C 1 ATOM 328 O O . ILE A 1 42 ? 13.202 49.328 22.516 1.00 52.75 ? 42 ILE A O 1 ATOM 329 C CB . ILE A 1 42 ? 14.428 49.195 24.951 1.00 52.02 ? 42 ILE A CB 1 ATOM 330 C CG1 . ILE A 1 42 ? 15.405 49.428 26.097 1.00 56.03 ? 42 ILE A CG1 1 ATOM 331 C CG2 . ILE A 1 42 ? 13.384 48.160 25.325 1.00 46.01 ? 42 ILE A CG2 1 ATOM 332 C CD1 . ILE A 1 42 ? 14.707 49.742 27.435 1.00 53.64 ? 42 ILE A CD1 1 ATOM 333 N N . LYS A 1 43 ? 14.331 47.508 21.799 1.00 47.51 ? 43 LYS A N 1 ATOM 334 C CA . LYS A 1 43 ? 13.478 47.351 20.629 1.00 54.39 ? 43 LYS A CA 1 ATOM 335 C C . LYS A 1 43 ? 12.055 47.010 21.043 1.00 48.69 ? 43 LYS A C 1 ATOM 336 O O . LYS A 1 43 ? 11.098 47.549 20.509 1.00 50.43 ? 43 LYS A O 1 ATOM 337 C CB . LYS A 1 43 ? 14.032 46.269 19.685 1.00 48.22 ? 43 LYS A CB 1 ATOM 338 C CG . LYS A 1 43 ? 13.300 46.152 18.362 1.00 50.17 ? 43 LYS A CG 1 ATOM 339 C CD . LYS A 1 43 ? 13.312 47.483 17.595 1.00 57.26 ? 43 LYS A CD 1 ATOM 340 C CE . LYS A 1 43 ? 12.648 47.407 16.244 1.00 63.56 ? 43 LYS A CE 1 ATOM 341 N NZ . LYS A 1 43 ? 11.195 47.205 16.332 1.00 69.95 1 43 LYS A NZ 1 ATOM 342 N N . ASP A 1 44 ? 11.922 46.090 21.987 1.00 52.71 ? 44 ASP A N 1 ATOM 343 C CA . ASP A 1 44 ? 10.617 45.607 22.369 1.00 47.51 ? 44 ASP A CA 1 ATOM 344 C C . ASP A 1 44 ? 10.650 44.973 23.737 1.00 48.45 ? 44 ASP A C 1 ATOM 345 O O . ASP A 1 44 ? 11.487 44.109 23.988 1.00 48.47 ? 44 ASP A O 1 ATOM 346 C CB . ASP A 1 44 ? 10.153 44.555 21.387 1.00 54.37 ? 44 ASP A CB 1 ATOM 347 C CG . ASP A 1 44 ? 8.734 44.139 21.630 1.00 62.36 ? 44 ASP A CG 1 ATOM 348 O OD1 . ASP A 1 44 ? 7.851 45.026 21.655 1.00 71.81 ? 44 ASP A OD1 1 ATOM 349 O OD2 . ASP A 1 44 ? 8.502 42.928 21.800 1.00 68.91 -1 44 ASP A OD2 1 ATOM 350 N N . MET A 1 45 ? 9.758 45.397 24.628 1.00 49.35 ? 45 MET A N 1 ATOM 351 C CA . MET A 1 45 ? 9.535 44.655 25.873 1.00 50.30 ? 45 MET A CA 1 ATOM 352 C C . MET A 1 45 ? 8.168 44.021 25.765 1.00 50.30 ? 45 MET A C 1 ATOM 353 O O . MET A 1 45 ? 7.138 44.693 25.788 1.00 51.23 ? 45 MET A O 1 ATOM 354 C CB . MET A 1 45 ? 9.597 45.548 27.104 1.00 51.47 ? 45 MET A CB 1 ATOM 355 C CG . MET A 1 45 ? 9.296 44.796 28.412 1.00 43.29 ? 45 MET A CG 1 ATOM 356 S SD . MET A 1 45 ? 10.580 43.598 28.848 1.00 51.29 ? 45 MET A SD 1 ATOM 357 C CE . MET A 1 45 ? 9.539 42.202 29.299 1.00 57.63 ? 45 MET A CE 1 ATOM 358 N N . ASP A 1 46 ? 8.180 42.710 25.589 1.00 49.04 ? 46 ASP A N 1 ATOM 359 C CA . ASP A 1 46 ? 6.980 41.916 25.410 1.00 51.34 ? 46 ASP A CA 1 ATOM 360 C C . ASP A 1 46 ? 6.502 41.411 26.768 1.00 55.04 ? 46 ASP A C 1 ATOM 361 O O . ASP A 1 46 ? 7.056 40.450 27.301 1.00 55.72 ? 46 ASP A O 1 ATOM 362 C CB . ASP A 1 46 ? 7.354 40.733 24.515 1.00 58.25 ? 46 ASP A CB 1 ATOM 363 C CG . ASP A 1 46 ? 6.169 39.913 24.093 1.00 59.01 ? 46 ASP A CG 1 ATOM 364 O OD1 . ASP A 1 46 ? 5.135 39.950 24.774 1.00 53.15 ? 46 ASP A OD1 1 ATOM 365 O OD2 . ASP A 1 46 ? 6.295 39.221 23.064 1.00 74.08 -1 46 ASP A OD2 1 ATOM 366 N N . GLU A 1 47 ? 5.490 42.047 27.342 1.00 57.24 ? 47 GLU A N 1 ATOM 367 C CA . GLU A 1 47 ? 4.994 41.623 28.653 1.00 65.78 ? 47 GLU A CA 1 ATOM 368 C C . GLU A 1 47 ? 4.108 40.385 28.581 1.00 68.49 ? 47 GLU A C 1 ATOM 369 O O . GLU A 1 47 ? 3.792 39.786 29.608 1.00 68.92 ? 47 GLU A O 1 ATOM 370 C CB . GLU A 1 47 ? 4.199 42.735 29.323 1.00 61.51 ? 47 GLU A CB 1 ATOM 371 C CG . GLU A 1 47 ? 4.926 44.040 29.414 1.00 59.30 ? 47 GLU A CG 1 ATOM 372 C CD . GLU A 1 47 ? 3.981 45.189 29.683 1.00 65.53 ? 47 GLU A CD 1 ATOM 373 O OE1 . GLU A 1 47 ? 3.104 45.045 30.560 1.00 72.54 ? 47 GLU A OE1 1 ATOM 374 O OE2 . GLU A 1 47 ? 4.106 46.225 28.997 1.00 71.25 -1 47 GLU A OE2 1 ATOM 375 N N . ARG A 1 48 ? 3.687 40.013 27.378 1.00 74.58 ? 48 ARG A N 1 ATOM 376 C CA . ARG A 1 48 ? 2.854 38.830 27.215 1.00 74.04 ? 48 ARG A CA 1 ATOM 377 C C . ARG A 1 48 ? 3.775 37.612 27.309 1.00 68.92 ? 48 ARG A C 1 ATOM 378 O O . ARG A 1 48 ? 3.514 36.682 28.061 1.00 68.52 ? 48 ARG A O 1 ATOM 379 C CB . ARG A 1 48 ? 2.110 38.845 25.872 1.00 80.19 ? 48 ARG A CB 1 ATOM 380 C CG . ARG A 1 48 ? 1.616 40.222 25.385 1.00 77.10 ? 48 ARG A CG 1 ATOM 381 C CD . ARG A 1 48 ? 0.399 40.736 26.123 1.00 76.06 ? 48 ARG A CD 1 ATOM 382 N NE . ARG A 1 48 ? -0.712 39.789 26.077 1.00 81.53 ? 48 ARG A NE 1 ATOM 383 C CZ . ARG A 1 48 ? -1.048 38.965 27.068 1.00 85.00 ? 48 ARG A CZ 1 ATOM 384 N NH1 . ARG A 1 48 ? -0.371 38.955 28.213 1.00 85.20 1 48 ARG A NH1 1 ATOM 385 N NH2 . ARG A 1 48 ? -2.069 38.139 26.923 1.00 87.15 ? 48 ARG A NH2 1 ATOM 386 N N . ASN A 1 49 ? 4.869 37.646 26.555 1.00 62.35 ? 49 ASN A N 1 ATOM 387 C CA . ASN A 1 49 ? 5.881 36.592 26.611 1.00 60.81 ? 49 ASN A CA 1 ATOM 388 C C . ASN A 1 49 ? 7.003 36.822 27.626 1.00 56.83 ? 49 ASN A C 1 ATOM 389 O O . ASN A 1 49 ? 7.809 35.921 27.882 1.00 52.66 ? 49 ASN A O 1 ATOM 390 C CB . ASN A 1 49 ? 6.503 36.421 25.232 1.00 56.82 ? 49 ASN A CB 1 ATOM 391 C CG . ASN A 1 49 ? 5.514 35.889 24.233 1.00 75.61 ? 49 ASN A CG 1 ATOM 392 O OD1 . ASN A 1 49 ? 4.845 34.890 24.491 1.00 82.01 ? 49 ASN A OD1 1 ATOM 393 N ND2 . ASN A 1 49 ? 5.381 36.570 23.102 1.00 78.76 ? 49 ASN A ND2 1 ATOM 394 N N . GLN A 1 50 ? 7.082 38.027 28.176 1.00 53.59 ? 50 GLN A N 1 ATOM 395 C CA . GLN A 1 50 ? 8.187 38.377 29.063 1.00 48.56 ? 50 GLN A CA 1 ATOM 396 C C . GLN A 1 50 ? 9.526 38.268 28.367 1.00 48.72 ? 50 GLN A C 1 ATOM 397 O O . GLN A 1 50 ? 10.489 37.707 28.894 1.00 53.10 ? 50 GLN A O 1 ATOM 398 C CB . GLN A 1 50 ? 8.145 37.504 30.317 1.00 52.16 ? 50 GLN A CB 1 ATOM 399 C CG . GLN A 1 50 ? 7.153 38.034 31.350 1.00 54.28 ? 50 GLN A CG 1 ATOM 400 C CD . GLN A 1 50 ? 7.535 39.423 31.852 1.00 56.90 ? 50 GLN A CD 1 ATOM 401 O OE1 . GLN A 1 50 ? 6.714 40.344 31.886 1.00 57.80 ? 50 GLN A OE1 1 ATOM 402 N NE2 . GLN A 1 50 ? 8.788 39.574 32.234 1.00 52.10 ? 50 GLN A NE2 1 ATOM 403 N N . ILE A 1 51 ? 9.578 38.819 27.161 1.00 44.62 ? 51 ILE A N 1 ATOM 404 C CA . ILE A 1 51 ? 10.794 38.817 26.378 1.00 41.02 ? 51 ILE A CA 1 ATOM 405 C C . ILE A 1 51 ? 11.209 40.228 26.015 1.00 45.69 ? 51 ILE A C 1 ATOM 406 O O . ILE A 1 51 ? 10.404 41.023 25.502 1.00 43.26 ? 51 ILE A O 1 ATOM 407 C CB . ILE A 1 51 ? 10.628 38.000 25.070 1.00 49.36 ? 51 ILE A CB 1 ATOM 408 C CG1 . ILE A 1 51 ? 10.143 36.584 25.391 1.00 47.76 ? 51 ILE A CG1 1 ATOM 409 C CG2 . ILE A 1 51 ? 11.908 37.992 24.302 1.00 47.06 ? 51 ILE A CG2 1 ATOM 410 C CD1 . ILE A 1 51 ? 11.135 35.744 26.135 1.00 54.81 ? 51 ILE A CD1 1 ATOM 411 N N . LEU A 1 52 ? 12.467 40.518 26.305 1.00 40.00 ? 52 LEU A N 1 ATOM 412 C CA . LEU A 1 52 ? 13.089 41.752 25.914 1.00 47.40 ? 52 LEU A CA 1 ATOM 413 C C . LEU A 1 52 ? 13.818 41.539 24.609 1.00 47.77 ? 52 LEU A C 1 ATOM 414 O O . LEU A 1 52 ? 14.599 40.604 24.485 1.00 43.99 ? 52 LEU A O 1 ATOM 415 C CB . LEU A 1 52 ? 14.090 42.180 26.968 1.00 38.72 ? 52 LEU A CB 1 ATOM 416 C CG . LEU A 1 52 ? 15.001 43.312 26.517 1.00 41.26 ? 52 LEU A CG 1 ATOM 417 C CD1 . LEU A 1 52 ? 14.229 44.622 26.379 1.00 44.32 ? 52 LEU A CD1 1 ATOM 418 C CD2 . LEU A 1 52 ? 16.163 43.479 27.476 1.00 43.33 ? 52 LEU A CD2 1 ATOM 419 N N . THR A 1 53 ? 13.541 42.390 23.627 1.00 42.22 ? 53 THR A N 1 ATOM 420 C CA . THR A 1 53 ? 14.390 42.486 22.454 1.00 41.51 ? 53 THR A CA 1 ATOM 421 C C . THR A 1 53 ? 15.225 43.765 22.575 1.00 42.46 ? 53 THR A C 1 ATOM 422 O O . THR A 1 53 ? 14.696 44.858 22.650 1.00 43.13 ? 53 THR A O 1 ATOM 423 C CB . THR A 1 53 ? 13.578 42.484 21.149 1.00 52.68 ? 53 THR A CB 1 ATOM 424 O OG1 . THR A 1 53 ? 12.732 41.325 21.110 1.00 52.44 ? 53 THR A OG1 1 ATOM 425 C CG2 . THR A 1 53 ? 14.516 42.490 19.927 1.00 47.18 ? 53 THR A CG2 1 ATOM 426 N N . ALA A 1 54 ? 16.537 43.601 22.602 1.00 42.41 ? 54 ALA A N 1 ATOM 427 C CA . ALA A 1 54 ? 17.465 44.711 22.733 1.00 48.44 ? 54 ALA A CA 1 ATOM 428 C C . ALA A 1 54 ? 18.433 44.741 21.553 1.00 53.07 ? 54 ALA A C 1 ATOM 429 O O . ALA A 1 54 ? 18.856 43.682 21.062 1.00 50.48 ? 54 ALA A O 1 ATOM 430 C CB . ALA A 1 54 ? 18.243 44.564 24.012 1.00 47.19 ? 54 ALA A CB 1 ATOM 431 N N . TYR A 1 55 ? 18.773 45.955 21.119 1.00 45.39 ? 55 TYR A N 1 ATOM 432 C CA . TYR A 1 55 ? 19.886 46.181 20.204 1.00 45.34 ? 55 TYR A CA 1 ATOM 433 C C . TYR A 1 55 ? 21.082 46.641 21.013 1.00 47.68 ? 55 TYR A C 1 ATOM 434 O O . TYR A 1 55 ? 20.978 47.608 21.791 1.00 44.89 ? 55 TYR A O 1 ATOM 435 C CB . TYR A 1 55 ? 19.550 47.273 19.201 1.00 45.86 ? 55 TYR A CB 1 ATOM 436 C CG . TYR A 1 55 ? 18.476 46.919 18.216 1.00 53.05 ? 55 TYR A CG 1 ATOM 437 C CD1 . TYR A 1 55 ? 17.985 45.625 18.111 1.00 48.27 ? 55 TYR A CD1 1 ATOM 438 C CD2 . TYR A 1 55 ? 17.940 47.890 17.390 1.00 56.41 ? 55 TYR A CD2 1 ATOM 439 C CE1 . TYR A 1 55 ? 16.981 45.321 17.189 1.00 51.13 ? 55 TYR A CE1 1 ATOM 440 C CE2 . TYR A 1 55 ? 16.949 47.600 16.499 1.00 58.30 ? 55 TYR A CE2 1 ATOM 441 C CZ . TYR A 1 55 ? 16.474 46.315 16.397 1.00 54.01 ? 55 TYR A CZ 1 ATOM 442 O OH . TYR A 1 55 ? 15.478 46.044 15.484 1.00 55.18 ? 55 TYR A OH 1 ATOM 443 N N . LEU A 1 56 ? 22.215 45.969 20.821 1.00 41.32 ? 56 LEU A N 1 ATOM 444 C CA . LEU A 1 56 ? 23.426 46.260 21.573 1.00 41.77 ? 56 LEU A CA 1 ATOM 445 C C . LEU A 1 56 ? 24.621 46.441 20.651 1.00 46.08 ? 56 LEU A C 1 ATOM 446 O O . LEU A 1 56 ? 24.613 45.947 19.524 1.00 48.95 ? 56 LEU A O 1 ATOM 447 C CB . LEU A 1 56 ? 23.758 45.067 22.471 1.00 44.80 ? 56 LEU A CB 1 ATOM 448 C CG . LEU A 1 56 ? 22.637 44.422 23.292 1.00 43.90 ? 56 LEU A CG 1 ATOM 449 C CD1 . LEU A 1 56 ? 23.142 43.148 23.952 1.00 45.18 ? 56 LEU A CD1 1 ATOM 450 C CD2 . LEU A 1 56 ? 22.144 45.398 24.321 1.00 50.75 ? 56 LEU A CD2 1 ATOM 451 N N . TRP A 1 57 ? 25.646 47.131 21.140 1.00 42.74 ? 57 TRP A N 1 ATOM 452 C CA . TRP A 1 57 ? 26.982 46.994 20.584 1.00 39.36 ? 57 TRP A CA 1 ATOM 453 C C . TRP A 1 57 ? 27.842 46.224 21.557 1.00 43.37 ? 57 TRP A C 1 ATOM 454 O O . TRP A 1 57 ? 28.006 46.607 22.726 1.00 50.08 ? 57 TRP A O 1 ATOM 455 C CB . TRP A 1 57 ? 27.610 48.341 20.266 1.00 41.15 ? 57 TRP A CB 1 ATOM 456 C CG . TRP A 1 57 ? 27.131 48.874 18.940 1.00 50.60 ? 57 TRP A CG 1 ATOM 457 C CD1 . TRP A 1 57 ? 26.080 49.707 18.710 1.00 56.30 ? 57 TRP A CD1 1 ATOM 458 C CD2 . TRP A 1 57 ? 27.686 48.563 17.664 1.00 54.34 ? 57 TRP A CD2 1 ATOM 459 N NE1 . TRP A 1 57 ? 25.945 49.942 17.350 1.00 48.08 ? 57 TRP A NE1 1 ATOM 460 C CE2 . TRP A 1 57 ? 26.923 49.242 16.693 1.00 53.68 ? 57 TRP A CE2 1 ATOM 461 C CE3 . TRP A 1 57 ? 28.757 47.766 17.247 1.00 60.14 ? 57 TRP A CE3 1 ATOM 462 C CZ2 . TRP A 1 57 ? 27.211 49.170 15.350 1.00 56.00 ? 57 TRP A CZ2 1 ATOM 463 C CZ3 . TRP A 1 57 ? 29.040 47.697 15.905 1.00 59.48 ? 57 TRP A CZ3 1 ATOM 464 C CH2 . TRP A 1 57 ? 28.263 48.389 14.971 1.00 60.23 ? 57 TRP A CH2 1 ATOM 465 N N . ILE A 1 58 ? 28.415 45.144 21.058 1.00 39.85 ? 58 ILE A N 1 ATOM 466 C CA . ILE A 1 58 ? 29.307 44.337 21.870 1.00 35.72 ? 58 ILE A CA 1 ATOM 467 C C . ILE A 1 58 ? 30.751 44.566 21.489 1.00 43.98 ? 58 ILE A C 1 ATOM 468 O O . ILE A 1 58 ? 31.126 44.441 20.318 1.00 43.72 ? 58 ILE A O 1 ATOM 469 C CB . ILE A 1 58 ? 28.958 42.883 21.704 1.00 41.61 ? 58 ILE A CB 1 ATOM 470 C CG1 . ILE A 1 58 ? 27.506 42.660 22.133 1.00 46.00 ? 58 ILE A CG1 1 ATOM 471 C CG2 . ILE A 1 58 ? 29.868 42.070 22.523 1.00 40.33 ? 58 ILE A CG2 1 ATOM 472 C CD1 . ILE A 1 58 ? 26.989 41.255 21.854 1.00 46.68 ? 58 ILE A CD1 1 ATOM 473 N N . ARG A 1 59 ? 31.557 44.911 22.486 1.00 34.83 ? 59 ARG A N 1 ATOM 474 C CA . ARG A 1 59 ? 32.966 45.139 22.282 1.00 35.22 ? 59 ARG A CA 1 ATOM 475 C C . ARG A 1 59 ? 33.769 44.111 23.030 1.00 34.04 ? 59 ARG A C 1 ATOM 476 O O . ARG A 1 59 ? 33.725 44.053 24.255 1.00 37.57 ? 59 ARG A O 1 ATOM 477 C CB . ARG A 1 59 ? 33.384 46.534 22.746 1.00 36.47 ? 59 ARG A CB 1 ATOM 478 C CG . ARG A 1 59 ? 34.889 46.757 22.638 1.00 41.81 ? 59 ARG A CG 1 ATOM 479 C CD . ARG A 1 59 ? 35.289 48.219 22.862 1.00 50.77 ? 59 ARG A CD 1 ATOM 480 N NE . ARG A 1 59 ? 35.247 48.950 21.593 1.00 46.68 ? 59 ARG A NE 1 ATOM 481 C CZ . ARG A 1 59 ? 36.122 49.877 21.200 1.00 55.50 ? 59 ARG A CZ 1 ATOM 482 N NH1 . ARG A 1 59 ? 37.137 50.241 21.982 1.00 57.54 1 59 ARG A NH1 1 ATOM 483 N NH2 . ARG A 1 59 ? 35.981 50.444 20.000 1.00 53.57 ? 59 ARG A NH2 1 ATOM 484 N N . GLN A 1 60 ? 34.513 43.311 22.279 1.00 33.15 ? 60 GLN A N 1 ATOM 485 C CA . GLN A 1 60 ? 35.377 42.307 22.831 1.00 33.04 ? 60 GLN A CA 1 ATOM 486 C C . GLN A 1 60 ? 36.825 42.648 22.550 1.00 37.29 ? 60 GLN A C 1 ATOM 487 O O . GLN A 1 60 ? 37.163 43.048 21.441 1.00 34.99 ? 60 GLN A O 1 ATOM 488 C CB . GLN A 1 60 ? 35.014 40.967 22.218 1.00 35.36 ? 60 GLN A CB 1 ATOM 489 C CG . GLN A 1 60 ? 33.551 40.657 22.386 1.00 30.70 ? 60 GLN A CG 1 ATOM 490 C CD . GLN A 1 60 ? 33.158 39.351 21.742 1.00 44.15 ? 60 GLN A CD 1 ATOM 491 O OE1 . GLN A 1 60 ? 33.888 38.360 21.825 1.00 39.15 ? 60 GLN A OE1 1 ATOM 492 N NE2 . GLN A 1 60 ? 32.018 39.347 21.069 1.00 47.40 ? 60 GLN A NE2 1 ATOM 493 N N . ILE A 1 61 ? 37.658 42.498 23.568 1.00 29.14 ? 61 ILE A N 1 ATOM 494 C CA . ILE A 1 61 ? 39.074 42.795 23.495 1.00 30.52 ? 61 ILE A CA 1 ATOM 495 C C . ILE A 1 61 ? 39.916 41.664 24.038 1.00 29.25 ? 61 ILE A C 1 ATOM 496 O O . ILE A 1 61 ? 39.689 41.194 25.148 1.00 35.70 ? 61 ILE A O 1 ATOM 497 C CB . ILE A 1 61 ? 39.401 44.054 24.302 1.00 30.68 ? 61 ILE A CB 1 ATOM 498 C CG1 . ILE A 1 61 ? 38.531 45.232 23.814 1.00 39.14 ? 61 ILE A CG1 1 ATOM 499 C CG2 . ILE A 1 61 ? 40.898 44.354 24.198 1.00 38.29 ? 61 ILE A CG2 1 ATOM 500 C CD1 . ILE A 1 61 ? 38.724 46.548 24.578 1.00 35.10 ? 61 ILE A CD1 1 ATOM 501 N N . TRP A 1 62 ? 40.927 41.257 23.282 1.00 27.52 ? 62 TRP A N 1 ATOM 502 C CA . TRP A 1 62 ? 41.817 40.186 23.704 1.00 28.48 ? 62 TRP A CA 1 ATOM 503 C C . TRP A 1 62 ? 43.103 40.296 22.931 1.00 37.75 ? 62 TRP A C 1 ATOM 504 O O . TRP A 1 62 ? 43.175 41.080 21.971 1.00 34.47 ? 62 TRP A O 1 ATOM 505 C CB . TRP A 1 62 ? 41.163 38.822 23.510 1.00 27.44 ? 62 TRP A CB 1 ATOM 506 C CG . TRP A 1 62 ? 41.008 38.372 22.066 1.00 26.23 ? 62 TRP A CG 1 ATOM 507 C CD1 . TRP A 1 62 ? 41.883 37.587 21.349 1.00 27.56 ? 62 TRP A CD1 1 ATOM 508 C CD2 . TRP A 1 62 ? 39.924 38.661 21.186 1.00 28.66 ? 62 TRP A CD2 1 ATOM 509 N NE1 . TRP A 1 62 ? 41.398 37.380 20.083 1.00 29.67 ? 62 TRP A NE1 1 ATOM 510 C CE2 . TRP A 1 62 ? 40.208 38.057 19.953 1.00 25.74 ? 62 TRP A CE2 1 ATOM 511 C CE3 . TRP A 1 62 ? 38.741 39.386 21.312 1.00 30.26 ? 62 TRP A CE3 1 ATOM 512 C CZ2 . TRP A 1 62 ? 39.368 38.151 18.871 1.00 30.96 ? 62 TRP A CZ2 1 ATOM 513 C CZ3 . TRP A 1 62 ? 37.909 39.493 20.210 1.00 34.53 ? 62 TRP A CZ3 1 ATOM 514 C CH2 . TRP A 1 62 ? 38.223 38.872 19.021 1.00 31.90 ? 62 TRP A CH2 1 ATOM 515 N N . HIS A 1 63 ? 44.109 39.527 23.342 1.00 31.44 ? 63 HIS A N 1 ATOM 516 C CA . HIS A 1 63 ? 45.365 39.437 22.617 1.00 34.03 ? 63 HIS A CA 1 ATOM 517 C C . HIS A 1 63 ? 45.501 38.149 21.816 1.00 33.83 ? 63 HIS A C 1 ATOM 518 O O . HIS A 1 63 ? 45.214 37.052 22.322 1.00 32.77 ? 63 HIS A O 1 ATOM 519 C CB . HIS A 1 63 ? 46.527 39.513 23.603 1.00 31.92 ? 63 HIS A CB 1 ATOM 520 C CG . HIS A 1 63 ? 46.842 40.919 24.014 1.00 39.38 ? 63 HIS A CG 1 ATOM 521 N ND1 . HIS A 1 63 ? 47.712 41.725 23.313 1.00 51.32 ? 63 HIS A ND1 1 ATOM 522 C CD2 . HIS A 1 63 ? 46.350 41.672 25.023 1.00 43.23 ? 63 HIS A CD2 1 ATOM 523 C CE1 . HIS A 1 63 ? 47.764 42.920 23.893 1.00 40.17 ? 63 HIS A CE1 1 ATOM 524 N NE2 . HIS A 1 63 ? 46.943 42.911 24.926 1.00 49.81 ? 63 HIS A NE2 1 ATOM 525 N N . ASP A 1 64 ? 45.955 38.270 20.581 1.00 34.09 ? 64 ASP A N 1 ATOM 526 C CA . ASP A 1 64 ? 46.289 37.111 19.787 1.00 29.63 ? 64 ASP A CA 1 ATOM 527 C C . ASP A 1 64 ? 47.800 36.996 19.748 1.00 40.50 ? 64 ASP A C 1 ATOM 528 O O . ASP A 1 64 ? 48.471 37.924 19.303 1.00 36.92 ? 64 ASP A O 1 ATOM 529 C CB . ASP A 1 64 ? 45.722 37.313 18.368 1.00 35.74 ? 64 ASP A CB 1 ATOM 530 C CG . ASP A 1 64 ? 45.915 36.103 17.473 1.00 30.26 ? 64 ASP A CG 1 ATOM 531 O OD1 . ASP A 1 64 ? 47.056 35.649 17.312 1.00 36.29 ? 64 ASP A OD1 1 ATOM 532 O OD2 . ASP A 1 64 ? 44.908 35.658 16.917 1.00 34.74 -1 64 ASP A OD2 1 ATOM 533 N N . ALA A 1 65 ? 48.354 35.872 20.200 1.00 37.60 ? 65 ALA A N 1 ATOM 534 C CA . ALA A 1 65 ? 49.804 35.729 20.242 1.00 37.52 ? 65 ALA A CA 1 ATOM 535 C C . ALA A 1 65 ? 50.458 35.675 18.877 1.00 32.55 ? 65 ALA A C 1 ATOM 536 O O . ALA A 1 65 ? 51.644 35.905 18.743 1.00 41.20 ? 65 ALA A O 1 ATOM 537 C CB . ALA A 1 65 ? 50.176 34.464 21.027 1.00 37.73 ? 65 ALA A CB 1 ATOM 538 N N . TYR A 1 66 ? 49.689 35.360 17.846 1.00 33.80 ? 66 TYR A N 1 ATOM 539 C CA . TYR A 1 66 ? 50.281 35.045 16.557 1.00 38.76 ? 66 TYR A CA 1 ATOM 540 C C . TYR A 1 66 ? 50.121 36.179 15.568 1.00 43.85 ? 66 TYR A C 1 ATOM 541 O O . TYR A 1 66 ? 50.668 36.131 14.478 1.00 48.24 ? 66 TYR A O 1 ATOM 542 C CB . TYR A 1 66 ? 49.633 33.789 15.981 1.00 41.48 ? 66 TYR A CB 1 ATOM 543 C CG . TYR A 1 66 ? 49.774 32.558 16.857 1.00 46.84 ? 66 TYR A CG 1 ATOM 544 C CD1 . TYR A 1 66 ? 51.007 32.163 17.359 1.00 58.24 ? 66 TYR A CD1 1 ATOM 545 C CD2 . TYR A 1 66 ? 48.665 31.798 17.187 1.00 41.86 ? 66 TYR A CD2 1 ATOM 546 C CE1 . TYR A 1 66 ? 51.134 31.018 18.155 1.00 60.65 ? 66 TYR A CE1 1 ATOM 547 C CE2 . TYR A 1 66 ? 48.780 30.659 17.976 1.00 47.89 ? 66 TYR A CE2 1 ATOM 548 C CZ . TYR A 1 66 ? 50.008 30.278 18.460 1.00 60.15 ? 66 TYR A CZ 1 ATOM 549 O OH . TYR A 1 66 ? 50.095 29.144 19.243 1.00 64.91 ? 66 TYR A OH 1 ATOM 550 N N . LEU A 1 67 ? 49.403 37.221 15.959 1.00 36.96 ? 67 LEU A N 1 ATOM 551 C CA . LEU A 1 67 ? 49.180 38.325 15.068 1.00 37.43 ? 67 LEU A CA 1 ATOM 552 C C . LEU A 1 67 ? 49.884 39.567 15.582 1.00 40.85 ? 67 LEU A C 1 ATOM 553 O O . LEU A 1 67 ? 49.269 40.626 15.741 1.00 42.29 ? 67 LEU A O 1 ATOM 554 C CB . LEU A 1 67 ? 47.695 38.583 14.885 1.00 39.12 ? 67 LEU A CB 1 ATOM 555 C CG . LEU A 1 67 ? 46.925 37.415 14.212 1.00 38.78 ? 67 LEU A CG 1 ATOM 556 C CD1 . LEU A 1 67 ? 45.472 37.689 14.204 1.00 38.65 ? 67 LEU A CD1 1 ATOM 557 C CD2 . LEU A 1 67 ? 47.384 37.217 12.772 1.00 38.51 ? 67 LEU A CD2 1 ATOM 558 N N . THR A 1 68 ? 51.182 39.444 15.808 1.00 42.58 ? 68 THR A N 1 ATOM 559 C CA . THR A 1 68 ? 51.977 40.630 16.141 1.00 42.54 ? 68 THR A CA 1 ATOM 560 C C . THR A 1 68 ? 52.977 40.964 15.049 1.00 42.50 ? 68 THR A C 1 ATOM 561 O O . THR A 1 68 ? 53.270 40.146 14.190 1.00 37.98 ? 68 THR A O 1 ATOM 562 C CB . THR A 1 68 ? 52.694 40.431 17.467 1.00 40.30 ? 68 THR A CB 1 ATOM 563 O OG1 . THR A 1 68 ? 53.676 39.411 17.309 1.00 38.31 ? 68 THR A OG1 1 ATOM 564 C CG2 . THR A 1 68 ? 51.699 40.001 18.560 1.00 45.83 ? 68 THR A CG2 1 ATOM 565 N N . TRP A 1 69 ? 53.505 42.186 15.062 1.00 40.39 ? 69 TRP A N 1 ATOM 566 C CA . TRP A 1 69 ? 54.515 42.536 14.090 1.00 39.16 ? 69 TRP A CA 1 ATOM 567 C C . TRP A 1 69 ? 55.317 43.740 14.513 1.00 41.25 ? 69 TRP A C 1 ATOM 568 O O . TRP A 1 69 ? 54.933 44.490 15.407 1.00 45.16 ? 69 TRP A O 1 ATOM 569 C CB . TRP A 1 69 ? 53.899 42.837 12.740 1.00 39.32 ? 69 TRP A CB 1 ATOM 570 C CG . TRP A 1 69 ? 53.094 44.130 12.706 1.00 44.64 ? 69 TRP A CG 1 ATOM 571 C CD1 . TRP A 1 69 ? 53.545 45.389 12.385 1.00 52.76 ? 69 TRP A CD1 1 ATOM 572 C CD2 . TRP A 1 69 ? 51.700 44.267 12.975 1.00 36.37 ? 69 TRP A CD2 1 ATOM 573 N NE1 . TRP A 1 69 ? 52.509 46.285 12.449 1.00 43.24 ? 69 TRP A NE1 1 ATOM 574 C CE2 . TRP A 1 69 ? 51.368 45.617 12.817 1.00 37.94 ? 69 TRP A CE2 1 ATOM 575 C CE3 . TRP A 1 69 ? 50.693 43.370 13.332 1.00 36.70 ? 69 TRP A CE3 1 ATOM 576 C CZ2 . TRP A 1 69 ? 50.070 46.084 13.010 1.00 35.59 ? 69 TRP A CZ2 1 ATOM 577 C CZ3 . TRP A 1 69 ? 49.423 43.842 13.531 1.00 34.89 ? 69 TRP A CZ3 1 ATOM 578 C CH2 . TRP A 1 69 ? 49.118 45.181 13.349 1.00 34.37 ? 69 TRP A CH2 1 ATOM 579 N N . ASP A 1 70 ? 56.433 43.897 13.820 1.00 41.16 ? 70 ASP A N 1 ATOM 580 C CA . ASP A 1 70 ? 57.379 44.947 14.072 1.00 50.54 ? 70 ASP A CA 1 ATOM 581 C C . ASP A 1 70 ? 56.956 46.109 13.194 1.00 49.99 ? 70 ASP A C 1 ATOM 582 O O . ASP A 1 70 ? 57.025 46.022 11.957 1.00 46.31 ? 70 ASP A O 1 ATOM 583 C CB . ASP A 1 70 ? 58.768 44.452 13.693 1.00 47.90 ? 70 ASP A CB 1 ATOM 584 C CG . ASP A 1 70 ? 59.819 45.494 13.899 1.00 52.39 ? 70 ASP A CG 1 ATOM 585 O OD1 . ASP A 1 70 ? 59.439 46.643 14.207 1.00 52.54 ? 70 ASP A OD1 1 ATOM 586 O OD2 . ASP A 1 70 ? 61.012 45.173 13.737 1.00 51.26 -1 70 ASP A OD2 1 ATOM 587 N N . ARG A 1 71 ? 56.495 47.183 13.831 1.00 51.11 ? 71 ARG A N 1 ATOM 588 C CA . ARG A 1 71 ? 56.065 48.379 13.117 1.00 51.52 ? 71 ARG A CA 1 ATOM 589 C C . ARG A 1 71 ? 57.123 48.860 12.133 1.00 53.08 ? 71 ARG A C 1 ATOM 590 O O . ARG A 1 71 ? 56.799 49.276 11.023 1.00 52.73 ? 71 ARG A O 1 ATOM 591 C CB . ARG A 1 71 ? 55.735 49.491 14.105 1.00 53.93 ? 71 ARG A CB 1 ATOM 592 C CG . ARG A 1 71 ? 54.448 49.259 14.852 1.00 52.58 ? 71 ARG A CG 1 ATOM 593 C CD . ARG A 1 71 ? 54.334 50.206 16.034 1.00 57.09 ? 71 ARG A CD 1 ATOM 594 N NE . ARG A 1 71 ? 55.224 49.798 17.113 1.00 52.27 ? 71 ARG A NE 1 ATOM 595 C CZ . ARG A 1 71 ? 55.372 50.440 18.266 1.00 52.66 ? 71 ARG A CZ 1 ATOM 596 N NH1 . ARG A 1 71 ? 54.696 51.553 18.502 1.00 51.05 1 71 ARG A NH1 1 ATOM 597 N NH2 . ARG A 1 71 ? 56.206 49.954 19.183 1.00 45.94 ? 71 ARG A NH2 1 ATOM 598 N N . ASP A 1 72 ? 58.386 48.771 12.532 1.00 50.47 ? 72 ASP A N 1 ATOM 599 C CA . ASP A 1 72 ? 59.496 49.229 11.686 1.00 52.79 ? 72 ASP A CA 1 ATOM 600 C C . ASP A 1 72 ? 59.599 48.492 10.348 1.00 50.07 ? 72 ASP A C 1 ATOM 601 O O . ASP A 1 72 ? 60.127 49.024 9.385 1.00 56.70 ? 72 ASP A O 1 ATOM 602 C CB . ASP A 1 72 ? 60.820 49.067 12.430 1.00 62.48 ? 72 ASP A CB 1 ATOM 603 C CG . ASP A 1 72 ? 60.958 50.023 13.591 1.00 73.59 ? 72 ASP A CG 1 ATOM 604 O OD1 . ASP A 1 72 ? 60.135 50.959 13.697 1.00 77.48 ? 72 ASP A OD1 1 ATOM 605 O OD2 . ASP A 1 72 ? 61.905 49.845 14.388 1.00 77.56 -1 72 ASP A OD2 1 ATOM 606 N N . GLN A 1 73 ? 59.137 47.252 10.300 1.00 52.22 ? 73 GLN A N 1 ATOM 607 C CA . GLN A 1 73 ? 59.242 46.463 9.080 1.00 53.90 ? 73 GLN A CA 1 ATOM 608 C C . GLN A 1 73 ? 58.099 46.781 8.115 1.00 58.72 ? 73 GLN A C 1 ATOM 609 O O . GLN A 1 73 ? 58.085 46.283 6.990 1.00 53.74 ? 73 GLN A O 1 ATOM 610 C CB . GLN A 1 73 ? 59.244 44.967 9.431 1.00 58.71 ? 73 GLN A CB 1 ATOM 611 C CG . GLN A 1 73 ? 60.414 44.556 10.330 1.00 63.02 ? 73 GLN A CG 1 ATOM 612 C CD . GLN A 1 73 ? 60.345 43.093 10.776 1.00 76.61 ? 73 GLN A CD 1 ATOM 613 O OE1 . GLN A 1 73 ? 59.644 42.274 10.176 1.00 85.87 ? 73 GLN A OE1 1 ATOM 614 N NE2 . GLN A 1 73 ? 61.075 42.762 11.841 1.00 80.87 ? 73 GLN A NE2 1 ATOM 615 N N . TYR A 1 74 ? 57.143 47.605 8.559 1.00 57.85 ? 74 TYR A N 1 ATOM 616 C CA . TYR A 1 74 ? 55.989 47.963 7.742 1.00 54.70 ? 74 TYR A CA 1 ATOM 617 C C . TYR A 1 74 ? 55.729 49.456 7.738 1.00 59.91 ? 74 TYR A C 1 ATOM 618 O O . TYR A 1 74 ? 54.598 49.905 7.911 1.00 59.18 ? 74 TYR A O 1 ATOM 619 C CB . TYR A 1 74 ? 54.760 47.194 8.219 1.00 55.45 ? 74 TYR A CB 1 ATOM 620 C CG . TYR A 1 74 ? 54.994 45.715 8.183 1.00 49.33 ? 74 TYR A CG 1 ATOM 621 C CD1 . TYR A 1 74 ? 55.614 45.065 9.242 1.00 49.31 ? 74 TYR A CD1 1 ATOM 622 C CD2 . TYR A 1 74 ? 54.604 44.959 7.090 1.00 53.61 ? 74 TYR A CD2 1 ATOM 623 C CE1 . TYR A 1 74 ? 55.823 43.684 9.222 1.00 42.62 ? 74 TYR A CE1 1 ATOM 624 C CE2 . TYR A 1 74 ? 54.824 43.582 7.045 1.00 51.23 ? 74 TYR A CE2 1 ATOM 625 C CZ . TYR A 1 74 ? 55.435 42.956 8.108 1.00 48.88 ? 74 TYR A CZ 1 ATOM 626 O OH . TYR A 1 74 ? 55.656 41.599 8.056 1.00 50.44 ? 74 TYR A OH 1 ATOM 627 N N . ASP A 1 75 ? 56.800 50.218 7.535 1.00 60.29 ? 75 ASP A N 1 ATOM 628 C CA . ASP A 1 75 ? 56.715 51.664 7.405 1.00 60.95 ? 75 ASP A CA 1 ATOM 629 C C . ASP A 1 75 ? 55.845 52.269 8.509 1.00 60.17 ? 75 ASP A C 1 ATOM 630 O O . ASP A 1 75 ? 55.074 53.188 8.273 1.00 54.99 ? 75 ASP A O 1 ATOM 631 C CB . ASP A 1 75 ? 56.187 52.008 6.010 1.00 59.79 ? 75 ASP A CB 1 ATOM 632 C CG . ASP A 1 75 ? 56.409 53.452 5.633 1.00 71.88 ? 75 ASP A CG 1 ATOM 633 O OD1 . ASP A 1 75 ? 57.310 54.107 6.206 1.00 76.36 ? 75 ASP A OD1 1 ATOM 634 O OD2 . ASP A 1 75 ? 55.671 53.928 4.750 1.00 78.70 -1 75 ASP A OD2 1 ATOM 635 N N . GLY A 1 76 ? 55.963 51.727 9.721 1.00 55.80 ? 76 GLY A N 1 ATOM 636 C CA . GLY A 1 76 ? 55.364 52.342 10.891 1.00 55.02 ? 76 GLY A CA 1 ATOM 637 C C . GLY A 1 76 ? 53.937 51.907 11.160 1.00 51.35 ? 76 GLY A C 1 ATOM 638 O O . GLY A 1 76 ? 53.350 52.228 12.196 1.00 52.83 ? 76 GLY A O 1 ATOM 639 N N . LEU A 1 77 ? 53.372 51.175 10.218 1.00 53.34 ? 77 LEU A N 1 ATOM 640 C CA . LEU A 1 77 ? 51.992 50.746 10.317 1.00 46.53 ? 77 LEU A CA 1 ATOM 641 C C . LEU A 1 77 ? 51.774 50.012 11.629 1.00 47.15 ? 77 LEU A C 1 ATOM 642 O O . LEU A 1 77 ? 52.456 49.032 11.912 1.00 51.78 ? 77 LEU A O 1 ATOM 643 C CB . LEU A 1 77 ? 51.669 49.845 9.130 1.00 53.59 ? 77 LEU A CB 1 ATOM 644 C CG . LEU A 1 77 ? 50.269 49.246 9.185 1.00 52.30 ? 77 LEU A CG 1 ATOM 645 C CD1 . LEU A 1 77 ? 49.252 50.363 9.021 1.00 55.78 ? 77 LEU A CD1 1 ATOM 646 C CD2 . LEU A 1 77 ? 50.109 48.192 8.097 1.00 55.15 ? 77 LEU A CD2 1 ATOM 647 N N . ASP A 1 78 ? 50.836 50.481 12.438 1.00 47.30 ? 78 ASP A N 1 ATOM 648 C CA . ASP A 1 78 ? 50.676 49.941 13.778 1.00 45.82 ? 78 ASP A CA 1 ATOM 649 C C . ASP A 1 78 ? 49.283 49.427 14.078 1.00 37.52 ? 78 ASP A C 1 ATOM 650 O O . ASP A 1 78 ? 49.024 48.988 15.171 1.00 43.21 ? 78 ASP A O 1 ATOM 651 C CB . ASP A 1 78 ? 51.025 50.989 14.828 1.00 55.06 ? 78 ASP A CB 1 ATOM 652 C CG . ASP A 1 78 ? 50.054 52.144 14.839 1.00 57.99 ? 78 ASP A CG 1 ATOM 653 O OD1 . ASP A 1 78 ? 49.063 52.106 14.084 1.00 60.57 ? 78 ASP A OD1 1 ATOM 654 O OD2 . ASP A 1 78 ? 50.289 53.082 15.616 1.00 55.84 -1 78 ASP A OD2 1 ATOM 655 N N . SER A 1 79 ? 48.400 49.464 13.087 1.00 47.42 ? 79 SER A N 1 ATOM 656 C CA . SER A 1 79 ? 47.032 49.024 13.286 1.00 44.20 ? 79 SER A CA 1 ATOM 657 C C . SER A 1 79 ? 46.425 48.677 11.944 1.00 47.18 ? 79 SER A C 1 ATOM 658 O O . SER A 1 79 ? 46.657 49.368 10.972 1.00 46.23 ? 79 SER A O 1 ATOM 659 C CB . SER A 1 79 ? 46.215 50.156 13.903 1.00 46.31 ? 79 SER A CB 1 ATOM 660 O OG . SER A 1 79 ? 44.904 49.715 14.178 1.00 51.95 ? 79 SER A OG 1 ATOM 661 N N . ILE A 1 80 ? 45.633 47.617 11.881 1.00 41.96 ? 80 ILE A N 1 ATOM 662 C CA . ILE A 1 80 ? 45.010 47.242 10.608 1.00 44.88 ? 80 ILE A CA 1 ATOM 663 C C . ILE A 1 80 ? 43.591 46.728 10.880 1.00 46.56 ? 80 ILE A C 1 ATOM 664 O O . ILE A 1 80 ? 43.325 46.153 11.949 1.00 39.16 ? 80 ILE A O 1 ATOM 665 C CB . ILE A 1 80 ? 45.927 46.241 9.855 1.00 51.83 ? 80 ILE A CB 1 ATOM 666 C CG1 . ILE A 1 80 ? 45.343 45.856 8.511 1.00 61.43 ? 80 ILE A CG1 1 ATOM 667 C CG2 . ILE A 1 80 ? 46.209 44.985 10.711 1.00 42.61 ? 80 ILE A CG2 1 ATOM 668 C CD1 . ILE A 1 80 ? 46.383 45.293 7.579 1.00 61.46 ? 80 ILE A CD1 1 ATOM 669 N N . ARG A 1 81 ? 42.661 47.008 9.974 1.00 42.70 ? 81 ARG A N 1 ATOM 670 C CA . ARG A 1 81 ? 41.307 46.477 10.102 1.00 42.82 ? 81 ARG A CA 1 ATOM 671 C C . ARG A 1 81 ? 41.204 45.213 9.235 1.00 54.07 ? 81 ARG A C 1 ATOM 672 O O . ARG A 1 81 ? 41.524 45.219 8.044 1.00 57.18 ? 81 ARG A O 1 ATOM 673 C CB . ARG A 1 81 ? 40.241 47.489 9.657 1.00 46.64 ? 81 ARG A CB 1 ATOM 674 C CG . ARG A 1 81 ? 39.978 48.607 10.608 1.00 55.47 ? 81 ARG A CG 1 ATOM 675 C CD . ARG A 1 81 ? 38.838 49.523 10.156 1.00 60.83 ? 81 ARG A CD 1 ATOM 676 N NE . ARG A 1 81 ? 38.532 50.471 11.225 1.00 64.97 ? 81 ARG A NE 1 ATOM 677 C CZ . ARG A 1 81 ? 37.544 50.326 12.105 1.00 69.57 ? 81 ARG A CZ 1 ATOM 678 N NH1 . ARG A 1 81 ? 36.719 49.284 12.033 1.00 74.13 1 81 ARG A NH1 1 ATOM 679 N NH2 . ARG A 1 81 ? 37.372 51.233 13.061 1.00 63.56 ? 81 ARG A NH2 1 ATOM 680 N N . ILE A 1 82 ? 40.738 44.144 9.845 1.00 54.59 ? 82 ILE A N 1 ATOM 681 C CA . ILE A 1 82 ? 40.779 42.801 9.287 1.00 49.72 ? 82 ILE A CA 1 ATOM 682 C C . ILE A 1 82 ? 39.369 42.279 9.418 1.00 50.07 ? 82 ILE A C 1 ATOM 683 O O . ILE A 1 82 ? 38.850 42.371 10.530 1.00 40.07 ? 82 ILE A O 1 ATOM 684 C CB . ILE A 1 82 ? 41.623 41.893 10.235 1.00 44.02 ? 82 ILE A CB 1 ATOM 685 C CG1 . ILE A 1 82 ? 43.071 42.381 10.319 1.00 51.37 ? 82 ILE A CG1 1 ATOM 686 C CG2 . ILE A 1 82 ? 41.594 40.438 9.803 1.00 51.77 ? 82 ILE A CG2 1 ATOM 687 C CD1 . ILE A 1 82 ? 43.779 42.427 8.964 1.00 52.34 ? 82 ILE A CD1 1 ATOM 688 N N . PRO A 1 83 ? 38.748 41.729 8.334 1.00 44.74 ? 83 PRO A N 1 ATOM 689 C CA . PRO A 1 83 ? 37.464 41.028 8.521 1.00 44.67 ? 83 PRO A CA 1 ATOM 690 C C . PRO A 1 83 ? 37.520 40.042 9.680 1.00 42.83 ? 83 PRO A C 1 ATOM 691 O O . PRO A 1 83 ? 38.482 39.270 9.816 1.00 43.91 ? 83 PRO A O 1 ATOM 692 C CB . PRO A 1 83 ? 37.268 40.285 7.195 1.00 48.19 ? 83 PRO A CB 1 ATOM 693 C CG . PRO A 1 83 ? 37.945 41.159 6.185 1.00 47.07 ? 83 PRO A CG 1 ATOM 694 C CD . PRO A 1 83 ? 39.161 41.712 6.913 1.00 43.81 ? 83 PRO A CD 1 ATOM 695 N N . SER A 1 84 ? 36.495 40.061 10.516 1.00 39.58 ? 84 SER A N 1 ATOM 696 C CA . SER A 1 84 ? 36.609 39.399 11.796 1.00 43.29 ? 84 SER A CA 1 ATOM 697 C C . SER A 1 84 ? 36.658 37.897 11.576 1.00 39.54 ? 84 SER A C 1 ATOM 698 O O . SER A 1 84 ? 37.236 37.199 12.381 1.00 41.06 ? 84 SER A O 1 ATOM 699 C CB . SER A 1 84 ? 35.453 39.778 12.732 1.00 36.14 ? 84 SER A CB 1 ATOM 700 O OG . SER A 1 84 ? 34.227 39.327 12.205 1.00 45.50 ? 84 SER A OG 1 ATOM 701 N N . ASP A 1 85 ? 36.110 37.409 10.461 1.00 38.86 ? 85 ASP A N 1 ATOM 702 C CA . ASP A 1 85 ? 36.084 35.967 10.245 1.00 43.94 ? 85 ASP A CA 1 ATOM 703 C C . ASP A 1 85 ? 37.477 35.403 9.994 1.00 45.54 ? 85 ASP A C 1 ATOM 704 O O . ASP A 1 85 ? 37.651 34.188 9.965 1.00 41.97 ? 85 ASP A O 1 ATOM 705 C CB . ASP A 1 85 ? 35.122 35.570 9.115 1.00 58.50 ? 85 ASP A CB 1 ATOM 706 C CG . ASP A 1 85 ? 35.395 36.302 7.823 1.00 63.98 ? 85 ASP A CG 1 ATOM 707 O OD1 . ASP A 1 85 ? 35.243 37.546 7.801 1.00 66.36 ? 85 ASP A OD1 1 ATOM 708 O OD2 . ASP A 1 85 ? 35.741 35.639 6.823 1.00 78.39 -1 85 ASP A OD2 1 ATOM 709 N N . LEU A 1 86 ? 38.472 36.267 9.835 1.00 39.40 ? 86 LEU A N 1 ATOM 710 C CA . LEU A 1 86 ? 39.833 35.814 9.538 1.00 44.32 ? 86 LEU A CA 1 ATOM 711 C C . LEU A 1 86 ? 40.644 35.491 10.777 1.00 44.44 ? 86 LEU A C 1 ATOM 712 O O . LEU A 1 86 ? 41.662 34.802 10.702 1.00 39.98 ? 86 LEU A O 1 ATOM 713 C CB . LEU A 1 86 ? 40.582 36.881 8.741 1.00 49.75 ? 86 LEU A CB 1 ATOM 714 C CG . LEU A 1 86 ? 39.917 37.177 7.401 1.00 51.87 ? 86 LEU A CG 1 ATOM 715 C CD1 . LEU A 1 86 ? 40.764 38.113 6.629 1.00 53.29 ? 86 LEU A CD1 1 ATOM 716 C CD2 . LEU A 1 86 ? 39.651 35.886 6.652 1.00 51.90 ? 86 LEU A CD2 1 ATOM 717 N N . VAL A 1 87 ? 40.229 36.023 11.917 1.00 36.83 ? 87 VAL A N 1 ATOM 718 C CA . VAL A 1 87 ? 40.975 35.800 13.113 1.00 34.88 ? 87 VAL A CA 1 ATOM 719 C C . VAL A 1 87 ? 40.243 34.805 14.013 1.00 30.02 ? 87 VAL A C 1 ATOM 720 O O . VAL A 1 87 ? 39.035 34.662 13.926 1.00 38.65 ? 87 VAL A O 1 ATOM 721 C CB . VAL A 1 87 ? 41.199 37.106 13.881 1.00 36.51 ? 87 VAL A CB 1 ATOM 722 C CG1 . VAL A 1 87 ? 41.919 38.094 12.987 1.00 32.31 ? 87 VAL A CG1 1 ATOM 723 C CG2 . VAL A 1 87 ? 39.881 37.686 14.374 1.00 33.52 ? 87 VAL A CG2 1 ATOM 724 N N . TRP A 1 88 ? 40.986 34.145 14.888 1.00 33.08 ? 88 TRP A N 1 ATOM 725 C CA . TRP A 1 88 ? 40.332 33.365 15.928 1.00 34.21 ? 88 TRP A CA 1 ATOM 726 C C . TRP A 1 88 ? 39.502 34.312 16.781 1.00 33.69 ? 88 TRP A C 1 ATOM 727 O O . TRP A 1 88 ? 39.911 35.460 17.046 1.00 30.40 ? 88 TRP A O 1 ATOM 728 C CB . TRP A 1 88 ? 41.349 32.660 16.792 1.00 30.85 ? 88 TRP A CB 1 ATOM 729 C CG . TRP A 1 88 ? 40.762 31.944 17.968 1.00 34.02 ? 88 TRP A CG 1 ATOM 730 C CD1 . TRP A 1 88 ? 40.440 30.613 18.056 1.00 34.88 ? 88 TRP A CD1 1 ATOM 731 C CD2 . TRP A 1 88 ? 40.489 32.517 19.261 1.00 32.71 ? 88 TRP A CD2 1 ATOM 732 N NE1 . TRP A 1 88 ? 39.961 30.334 19.337 1.00 29.03 ? 88 TRP A NE1 1 ATOM 733 C CE2 . TRP A 1 88 ? 39.985 31.487 20.079 1.00 37.12 ? 88 TRP A CE2 1 ATOM 734 C CE3 . TRP A 1 88 ? 40.609 33.810 19.793 1.00 28.87 ? 88 TRP A CE3 1 ATOM 735 C CZ2 . TRP A 1 88 ? 39.611 31.710 21.412 1.00 37.92 ? 88 TRP A CZ2 1 ATOM 736 C CZ3 . TRP A 1 88 ? 40.219 34.031 21.111 1.00 32.37 ? 88 TRP A CZ3 1 ATOM 737 C CH2 . TRP A 1 88 ? 39.736 32.984 21.905 1.00 32.93 ? 88 TRP A CH2 1 ATOM 738 N N . ARG A 1 89 ? 38.320 33.859 17.160 1.00 31.23 ? 89 ARG A N 1 ATOM 739 C CA . ARG A 1 89 ? 37.468 34.630 18.066 1.00 30.24 ? 89 ARG A CA 1 ATOM 740 C C . ARG A 1 89 ? 37.016 33.764 19.258 1.00 33.47 ? 89 ARG A C 1 ATOM 741 O O . ARG A 1 89 ? 37.003 32.544 19.171 1.00 36.58 ? 89 ARG A O 1 ATOM 742 C CB . ARG A 1 89 ? 36.273 35.133 17.267 1.00 38.47 ? 89 ARG A CB 1 ATOM 743 C CG . ARG A 1 89 ? 36.670 36.169 16.238 1.00 43.59 ? 89 ARG A CG 1 ATOM 744 C CD . ARG A 1 89 ? 35.535 36.535 15.327 1.00 49.61 ? 89 ARG A CD 1 ATOM 745 N NE . ARG A 1 89 ? 35.047 35.394 14.575 1.00 57.99 ? 89 ARG A NE 1 ATOM 746 C CZ . ARG A 1 89 ? 34.126 35.454 13.617 1.00 70.08 ? 89 ARG A CZ 1 ATOM 747 N NH1 . ARG A 1 89 ? 33.570 36.617 13.246 1.00 61.83 1 89 ARG A NH1 1 ATOM 748 N NH2 . ARG A 1 89 ? 33.769 34.332 13.010 1.00 63.29 ? 89 ARG A NH2 1 ATOM 749 N N . PRO A 1 90 ? 36.675 34.379 20.383 1.00 33.45 ? 90 PRO A N 1 ATOM 750 C CA . PRO A 1 90 ? 36.378 33.562 21.573 1.00 33.65 ? 90 PRO A CA 1 ATOM 751 C C . PRO A 1 90 ? 35.007 32.908 21.608 1.00 37.31 ? 90 PRO A C 1 ATOM 752 O O . PRO A 1 90 ? 34.726 32.122 22.528 1.00 42.38 ? 90 PRO A O 1 ATOM 753 C CB . PRO A 1 90 ? 36.515 34.543 22.738 1.00 34.19 ? 90 PRO A CB 1 ATOM 754 C CG . PRO A 1 90 ? 36.531 35.930 22.139 1.00 31.32 ? 90 PRO A CG 1 ATOM 755 C CD . PRO A 1 90 ? 37.019 35.770 20.720 1.00 30.78 ? 90 PRO A CD 1 ATOM 756 N N . ASP A 1 91 ? 34.166 33.217 20.640 1.00 36.50 ? 91 ASP A N 1 ATOM 757 C CA . ASP A 1 91 ? 32.887 32.550 20.554 1.00 34.03 ? 91 ASP A CA 1 ATOM 758 C C . ASP A 1 91 ? 31.986 32.943 21.693 1.00 34.84 ? 91 ASP A C 1 ATOM 759 O O . ASP A 1 91 ? 31.214 32.138 22.211 1.00 37.98 ? 91 ASP A O 1 ATOM 760 C CB . ASP A 1 91 ? 33.064 31.036 20.547 1.00 37.86 ? 91 ASP A CB 1 ATOM 761 C CG . ASP A 1 91 ? 31.914 30.342 19.902 1.00 56.53 ? 91 ASP A CG 1 ATOM 762 O OD1 . ASP A 1 91 ? 31.278 30.985 19.044 1.00 57.82 ? 91 ASP A OD1 1 ATOM 763 O OD2 . ASP A 1 91 ? 31.639 29.172 20.250 1.00 64.15 -1 91 ASP A OD2 1 ATOM 764 N N . ILE A 1 92 ? 32.053 34.200 22.065 1.00 33.90 ? 92 ILE A N 1 ATOM 765 C CA . ILE A 1 92 ? 31.202 34.676 23.124 1.00 32.44 ? 92 ILE A CA 1 ATOM 766 C C . ILE A 1 92 ? 29.810 34.931 22.561 1.00 44.06 ? 92 ILE A C 1 ATOM 767 O O . ILE A 1 92 ? 29.660 35.618 21.557 1.00 49.39 ? 92 ILE A O 1 ATOM 768 C CB . ILE A 1 92 ? 31.813 35.904 23.785 1.00 38.32 ? 92 ILE A CB 1 ATOM 769 C CG1 . ILE A 1 92 ? 33.012 35.434 24.621 1.00 37.36 ? 92 ILE A CG1 1 ATOM 770 C CG2 . ILE A 1 92 ? 30.780 36.635 24.641 1.00 41.43 ? 92 ILE A CG2 1 ATOM 771 C CD1 . ILE A 1 92 ? 34.001 36.488 24.819 1.00 46.98 ? 92 ILE A CD1 1 ATOM 772 N N . VAL A 1 93 ? 28.812 34.335 23.210 1.00 37.70 ? 93 VAL A N 1 ATOM 773 C CA . VAL A 1 93 ? 27.432 34.468 22.802 1.00 39.10 ? 93 VAL A CA 1 ATOM 774 C C . VAL A 1 93 ? 26.545 34.722 24.010 1.00 38.09 ? 93 VAL A C 1 ATOM 775 O O . VAL A 1 93 ? 26.965 34.555 25.153 1.00 36.66 ? 93 VAL A O 1 ATOM 776 C CB . VAL A 1 93 ? 26.938 33.196 22.130 1.00 43.75 ? 93 VAL A CB 1 ATOM 777 C CG1 . VAL A 1 93 ? 27.785 32.884 20.906 1.00 55.33 ? 93 VAL A CG1 1 ATOM 778 C CG2 . VAL A 1 93 ? 26.969 32.042 23.105 1.00 42.87 ? 93 VAL A CG2 1 ATOM 779 N N . LEU A 1 94 ? 25.314 35.130 23.723 1.00 42.26 ? 94 LEU A N 1 ATOM 780 C CA . LEU A 1 94 ? 24.282 35.242 24.717 1.00 34.48 ? 94 LEU A CA 1 ATOM 781 C C . LEU A 1 94 ? 23.822 33.857 25.116 1.00 40.57 ? 94 LEU A C 1 ATOM 782 O O . LEU A 1 94 ? 23.226 33.146 24.324 1.00 37.92 ? 94 LEU A O 1 ATOM 783 C CB . LEU A 1 94 ? 23.092 36.023 24.163 1.00 39.38 ? 94 LEU A CB 1 ATOM 784 C CG . LEU A 1 94 ? 21.973 36.253 25.172 1.00 39.05 ? 94 LEU A CG 1 ATOM 785 C CD1 . LEU A 1 94 ? 22.401 37.326 26.174 1.00 36.10 ? 94 LEU A CD1 1 ATOM 786 C CD2 . LEU A 1 94 ? 20.674 36.653 24.521 1.00 44.64 ? 94 LEU A CD2 1 ATOM 787 N N . TYR A 1 95 ? 24.110 33.464 26.350 1.00 35.68 ? 95 TYR A N 1 ATOM 788 C CA . TYR A 1 95 ? 23.662 32.187 26.883 1.00 36.09 ? 95 TYR A CA 1 ATOM 789 C C . TYR A 1 95 ? 22.180 32.067 27.030 1.00 43.84 ? 95 TYR A C 1 ATOM 790 O O . TYR A 1 95 ? 21.606 31.032 26.715 1.00 50.94 ? 95 TYR A O 1 ATOM 791 C CB . TYR A 1 95 ? 24.270 31.938 28.273 1.00 40.56 ? 95 TYR A CB 1 ATOM 792 C CG . TYR A 1 95 ? 25.694 31.455 28.265 1.00 38.83 ? 95 TYR A CG 1 ATOM 793 C CD1 . TYR A 1 95 ? 26.356 31.136 27.088 1.00 40.95 ? 95 TYR A CD1 1 ATOM 794 C CD2 . TYR A 1 95 ? 26.376 31.285 29.455 1.00 36.90 ? 95 TYR A CD2 1 ATOM 795 C CE1 . TYR A 1 95 ? 27.664 30.686 27.113 1.00 39.42 ? 95 TYR A CE1 1 ATOM 796 C CE2 . TYR A 1 95 ? 27.656 30.859 29.484 1.00 37.71 ? 95 TYR A CE2 1 ATOM 797 C CZ . TYR A 1 95 ? 28.297 30.528 28.336 1.00 36.23 ? 95 TYR A CZ 1 ATOM 798 O OH . TYR A 1 95 ? 29.597 30.100 28.415 1.00 36.72 ? 95 TYR A OH 1 ATOM 799 N N A ASN A 1 96 ? 21.577 33.180 27.428 0.11 44.57 ? 96 ASN A N 1 ATOM 800 N N B ASN A 1 96 ? 21.508 33.077 27.567 0.89 44.58 ? 96 ASN A N 1 ATOM 801 C CA A ASN A 1 96 ? 20.213 33.241 27.917 0.11 46.68 ? 96 ASN A CA 1 ATOM 802 C CA B ASN A 1 96 ? 20.109 32.865 27.915 0.89 48.19 ? 96 ASN A CA 1 ATOM 803 C C A ASN A 1 96 ? 19.178 33.440 26.813 0.11 50.82 ? 96 ASN A C 1 ATOM 804 C C B ASN A 1 96 ? 19.143 33.311 26.835 0.89 50.73 ? 96 ASN A C 1 ATOM 805 O O A ASN A 1 96 ? 18.093 33.958 27.075 0.11 52.24 ? 96 ASN A O 1 ATOM 806 O O B ASN A 1 96 ? 18.110 33.899 27.128 0.89 52.01 ? 96 ASN A O 1 ATOM 807 C CB A ASN A 1 96 ? 20.137 34.417 28.896 0.11 44.47 ? 96 ASN A CB 1 ATOM 808 C CB B ASN A 1 96 ? 19.753 33.517 29.248 0.89 43.09 ? 96 ASN A CB 1 ATOM 809 C CG A ASN A 1 96 ? 18.889 34.407 29.745 0.11 47.39 ? 96 ASN A CG 1 ATOM 810 C CG B ASN A 1 96 ? 20.101 35.010 29.305 0.89 40.82 ? 96 ASN A CG 1 ATOM 811 O OD1 A ASN A 1 96 ? 18.184 33.403 29.833 0.11 54.95 ? 96 ASN A OD1 1 ATOM 812 O OD1 B ASN A 1 96 ? 21.081 35.490 28.703 0.89 41.65 ? 96 ASN A OD1 1 ATOM 813 N ND2 A ASN A 1 96 ? 18.616 35.534 30.394 0.11 51.52 ? 96 ASN A ND2 1 ATOM 814 N ND2 B ASN A 1 96 ? 19.301 35.735 30.023 0.89 43.67 ? 96 ASN A ND2 1 ATOM 815 N N . LYS A 1 97 ? 19.493 33.035 25.583 1.00 55.44 ? 97 LYS A N 1 ATOM 816 C CA . LYS A 1 97 ? 18.615 33.363 24.466 1.00 56.15 ? 97 LYS A CA 1 ATOM 817 C C . LYS A 1 97 ? 17.292 32.652 24.651 1.00 53.69 ? 97 LYS A C 1 ATOM 818 O O . LYS A 1 97 ? 17.250 31.484 25.031 1.00 59.69 ? 97 LYS A O 1 ATOM 819 C CB . LYS A 1 97 ? 19.238 32.998 23.113 1.00 64.78 ? 97 LYS A CB 1 ATOM 820 C CG . LYS A 1 97 ? 19.666 31.562 23.002 1.00 69.26 ? 97 LYS A CG 1 ATOM 821 C CD . LYS A 1 97 ? 19.523 31.039 21.577 1.00 77.36 ? 97 LYS A CD 1 ATOM 822 C CE . LYS A 1 97 ? 20.226 31.926 20.577 1.00 77.90 ? 97 LYS A CE 1 ATOM 823 N NZ . LYS A 1 97 ? 21.677 32.035 20.874 1.00 81.07 1 97 LYS A NZ 1 ATOM 824 N N . ALA A 1 98 ? 16.208 33.380 24.419 1.00 47.56 ? 98 ALA A N 1 ATOM 825 C CA . ALA A 1 98 ? 14.884 32.803 24.423 1.00 59.49 ? 98 ALA A CA 1 ATOM 826 C C . ALA A 1 98 ? 14.512 32.476 22.972 1.00 66.07 ? 98 ALA A C 1 ATOM 827 O O . ALA A 1 98 ? 13.556 31.753 22.720 1.00 71.22 ? 98 ALA A O 1 ATOM 828 C CB . ALA A 1 98 ? 13.897 33.777 25.034 1.00 69.48 ? 98 ALA A CB 1 ATOM 829 N N . ASP A 1 99 ? 15.308 32.978 22.028 1.00 84.60 ? 99 ASP A N 1 ATOM 830 C CA . ASP A 1 99 ? 14.912 33.052 20.617 1.00 90.08 ? 99 ASP A CA 1 ATOM 831 C C . ASP A 1 99 ? 15.003 31.778 19.771 1.00 92.77 ? 99 ASP A C 1 ATOM 832 O O . ASP A 1 99 ? 15.356 30.700 20.267 1.00 92.17 ? 99 ASP A O 1 ATOM 833 N N . ASP A 1 100 ? 14.694 31.939 18.482 1.00 92.24 ? 100 ASP A N 1 ATOM 834 C CA . ASP A 1 100 ? 14.598 30.836 17.520 1.00 88.73 ? 100 ASP A CA 1 ATOM 835 C C . ASP A 1 100 ? 15.822 29.923 17.466 1.00 91.21 ? 100 ASP A C 1 ATOM 836 O O . ASP A 1 100 ? 15.721 28.714 17.716 1.00 86.63 ? 100 ASP A O 1 ATOM 837 N N . GLU A 1 101 ? 16.967 30.493 17.099 1.00 90.05 ? 101 GLU A N 1 ATOM 838 C CA . GLU A 1 101 ? 17.034 31.892 16.696 1.00 89.48 ? 101 GLU A CA 1 ATOM 839 C C . GLU A 1 101 ? 17.984 32.058 15.515 1.00 87.86 ? 101 GLU A C 1 ATOM 840 O O . GLU A 1 101 ? 18.832 32.949 15.513 1.00 94.78 ? 101 GLU A O 1 ATOM 841 N N . GLU A 1 104 ? 20.040 36.071 12.336 1.00 81.10 ? 104 GLU A N 1 ATOM 842 C CA . GLU A 1 104 ? 20.715 36.457 11.094 1.00 86.44 ? 104 GLU A CA 1 ATOM 843 C C . GLU A 1 104 ? 22.127 36.996 11.348 1.00 94.80 ? 104 GLU A C 1 ATOM 844 O O . GLU A 1 104 ? 22.387 37.587 12.401 1.00 91.37 ? 104 GLU A O 1 ATOM 845 N N . PRO A 1 105 ? 23.050 36.778 10.388 1.00 99.72 ? 105 PRO A N 1 ATOM 846 C CA . PRO A 1 105 ? 24.437 37.255 10.497 1.00 100.02 ? 105 PRO A CA 1 ATOM 847 C C . PRO A 1 105 ? 24.642 38.669 9.940 1.00 104.19 ? 105 PRO A C 1 ATOM 848 O O . PRO A 1 105 ? 23.880 39.080 9.060 1.00 112.41 ? 105 PRO A O 1 ATOM 849 C CB . PRO A 1 105 ? 25.225 36.243 9.644 1.00 99.55 ? 105 PRO A CB 1 ATOM 850 C CG . PRO A 1 105 ? 24.244 35.154 9.274 1.00 98.43 ? 105 PRO A CG 1 ATOM 851 C CD . PRO A 1 105 ? 22.907 35.809 9.290 1.00 99.57 ? 105 PRO A CD 1 ATOM 852 N N . VAL A 1 106 ? 25.652 39.385 10.446 1.00 86.81 ? 106 VAL A N 1 ATOM 853 C CA . VAL A 1 106 ? 26.036 40.711 9.935 1.00 83.52 ? 106 VAL A CA 1 ATOM 854 C C . VAL A 1 106 ? 27.539 40.918 10.104 1.00 84.15 ? 106 VAL A C 1 ATOM 855 O O . VAL A 1 106 ? 28.030 40.982 11.226 1.00 84.14 ? 106 VAL A O 1 ATOM 856 C CB . VAL A 1 106 ? 25.325 41.849 10.686 1.00 86.67 ? 106 VAL A CB 1 ATOM 857 C CG1 . VAL A 1 106 ? 25.928 43.203 10.306 1.00 88.81 ? 106 VAL A CG1 1 ATOM 858 C CG2 . VAL A 1 106 ? 23.821 41.826 10.411 1.00 94.30 ? 106 VAL A CG2 1 ATOM 859 N N . ASN A 1 107 ? 28.269 41.048 8.998 1.00 83.67 ? 107 ASN A N 1 ATOM 860 C CA . ASN A 1 107 ? 29.731 40.972 9.059 1.00 81.68 ? 107 ASN A CA 1 ATOM 861 C C . ASN A 1 107 ? 30.466 42.259 9.466 1.00 72.15 ? 107 ASN A C 1 ATOM 862 O O . ASN A 1 107 ? 30.021 43.384 9.187 1.00 67.79 ? 107 ASN A O 1 ATOM 863 C CB . ASN A 1 107 ? 30.297 40.421 7.752 1.00 84.21 ? 107 ASN A CB 1 ATOM 864 C CG . ASN A 1 107 ? 29.803 41.166 6.558 1.00 87.75 ? 107 ASN A CG 1 ATOM 865 O OD1 . ASN A 1 107 ? 29.568 42.372 6.624 1.00 87.45 ? 107 ASN A OD1 1 ATOM 866 N ND2 . ASN A 1 107 ? 29.621 40.454 5.449 1.00 92.86 ? 107 ASN A ND2 1 ATOM 867 N N . THR A 1 108 ? 31.609 42.056 10.122 1.00 48.55 ? 108 THR A N 1 ATOM 868 C CA . THR A 1 108 ? 32.333 43.123 10.812 1.00 45.55 ? 108 THR A CA 1 ATOM 869 C C . THR A 1 108 ? 33.831 42.953 10.672 1.00 42.03 ? 108 THR A C 1 ATOM 870 O O . THR A 1 108 ? 34.314 41.910 10.258 1.00 50.71 ? 108 THR A O 1 ATOM 871 C CB . THR A 1 108 ? 32.048 43.085 12.313 1.00 56.19 ? 108 THR A CB 1 ATOM 872 O OG1 . THR A 1 108 ? 32.249 41.746 12.787 1.00 51.72 ? 108 THR A OG1 1 ATOM 873 C CG2 . THR A 1 108 ? 30.612 43.511 12.601 1.00 61.73 ? 108 THR A CG2 1 ATOM 874 N N . ASN A 1 109 ? 34.567 43.979 11.076 1.00 40.83 ? 109 ASN A N 1 ATOM 875 C CA . ASN A 1 109 ? 36.005 43.938 11.040 1.00 40.99 ? 109 ASN A CA 1 ATOM 876 C C . ASN A 1 109 ? 36.462 44.036 12.448 1.00 44.74 ? 109 ASN A C 1 ATOM 877 O O . ASN A 1 109 ? 35.735 44.582 13.266 1.00 42.95 ? 109 ASN A O 1 ATOM 878 C CB . ASN A 1 109 ? 36.531 45.152 10.303 1.00 46.65 ? 109 ASN A CB 1 ATOM 879 C CG . ASN A 1 109 ? 36.178 45.116 8.854 1.00 55.25 ? 109 ASN A CG 1 ATOM 880 O OD1 . ASN A 1 109 ? 36.557 44.184 8.156 1.00 57.48 ? 109 ASN A OD1 1 ATOM 881 N ND2 . ASN A 1 109 ? 35.413 46.099 8.395 1.00 64.04 ? 109 ASN A ND2 1 ATOM 882 N N . VAL A 1 110 ? 37.668 43.545 12.729 1.00 36.47 ? 110 VAL A N 1 ATOM 883 C CA . VAL A 1 110 ? 38.293 43.855 13.981 1.00 36.78 ? 110 VAL A CA 1 ATOM 884 C C . VAL A 1 110 ? 39.384 44.883 13.733 1.00 39.93 ? 110 VAL A C 1 ATOM 885 O O . VAL A 1 110 ? 39.811 45.082 12.606 1.00 42.91 ? 110 VAL A O 1 ATOM 886 C CB . VAL A 1 110 ? 38.888 42.622 14.643 1.00 40.76 ? 110 VAL A CB 1 ATOM 887 C CG1 . VAL A 1 110 ? 37.833 41.511 14.713 1.00 41.75 ? 110 VAL A CG1 1 ATOM 888 C CG2 . VAL A 1 110 ? 40.080 42.162 13.868 1.00 45.04 ? 110 VAL A CG2 1 ATOM 889 N N . VAL A 1 111 ? 39.829 45.540 14.784 1.00 42.58 ? 111 VAL A N 1 ATOM 890 C CA . VAL A 1 111 ? 41.039 46.343 14.696 1.00 38.75 ? 111 VAL A CA 1 ATOM 891 C C . VAL A 1 111 ? 42.158 45.568 15.364 1.00 33.37 ? 111 VAL A C 1 ATOM 892 O O . VAL A 1 111 ? 42.077 45.214 16.561 1.00 39.77 ? 111 VAL A O 1 ATOM 893 C CB . VAL A 1 111 ? 40.843 47.708 15.345 1.00 38.44 ? 111 VAL A CB 1 ATOM 894 C CG1 . VAL A 1 111 ? 42.167 48.441 15.472 1.00 45.01 ? 111 VAL A CG1 1 ATOM 895 C CG2 . VAL A 1 111 ? 39.833 48.510 14.535 1.00 43.27 ? 111 VAL A CG2 1 ATOM 896 N N . LEU A 1 112 ? 43.217 45.326 14.621 1.00 39.01 ? 112 LEU A N 1 ATOM 897 C CA . LEU A 1 112 ? 44.340 44.558 15.141 1.00 41.84 ? 112 LEU A CA 1 ATOM 898 C C . LEU A 1 112 ? 45.542 45.484 15.287 1.00 42.52 ? 112 LEU A C 1 ATOM 899 O O . LEU A 1 112 ? 45.961 46.094 14.306 1.00 39.26 ? 112 LEU A O 1 ATOM 900 C CB . LEU A 1 112 ? 44.659 43.439 14.189 1.00 40.24 ? 112 LEU A CB 1 ATOM 901 C CG . LEU A 1 112 ? 45.984 42.707 14.344 1.00 33.70 ? 112 LEU A CG 1 ATOM 902 C CD1 . LEU A 1 112 ? 46.033 41.904 15.642 1.00 39.80 ? 112 LEU A CD1 1 ATOM 903 C CD2 . LEU A 1 112 ? 46.184 41.811 13.176 1.00 35.19 ? 112 LEU A CD2 1 ATOM 904 N N . ARG A 1 113 ? 46.092 45.559 16.500 1.00 38.28 ? 113 ARG A N 1 ATOM 905 C CA . ARG A 1 113 ? 47.212 46.442 16.800 1.00 37.51 ? 113 ARG A CA 1 ATOM 906 C C . ARG A 1 113 ? 48.478 45.601 16.743 1.00 39.27 ? 113 ARG A C 1 ATOM 907 O O . ARG A 1 113 ? 48.429 44.371 16.892 1.00 37.52 ? 113 ARG A O 1 ATOM 908 C CB . ARG A 1 113 ? 47.031 47.070 18.177 1.00 46.12 ? 113 ARG A CB 1 ATOM 909 C CG . ARG A 1 113 ? 47.977 48.225 18.500 1.00 45.52 ? 113 ARG A CG 1 ATOM 910 C CD . ARG A 1 113 ? 47.594 48.913 19.794 1.00 43.94 ? 113 ARG A CD 1 ATOM 911 N NE . ARG A 1 113 ? 47.823 48.071 20.976 1.00 49.85 ? 113 ARG A NE 1 ATOM 912 C CZ . ARG A 1 113 ? 47.438 48.394 22.205 1.00 55.91 ? 113 ARG A CZ 1 ATOM 913 N NH1 . ARG A 1 113 ? 46.808 49.542 22.418 1.00 56.88 1 113 ARG A NH1 1 ATOM 914 N NH2 . ARG A 1 113 ? 47.681 47.578 23.224 1.00 52.28 ? 113 ARG A NH2 1 ATOM 915 N N . TYR A 1 114 ? 49.602 46.263 16.498 1.00 41.55 ? 114 TYR A N 1 ATOM 916 C CA . TYR A 1 114 ? 50.876 45.600 16.226 1.00 38.80 ? 114 TYR A CA 1 ATOM 917 C C . TYR A 1 114 ? 51.271 44.672 17.339 1.00 34.68 ? 114 TYR A C 1 ATOM 918 O O . TYR A 1 114 ? 52.062 43.734 17.124 1.00 41.26 ? 114 TYR A O 1 ATOM 919 C CB . TYR A 1 114 ? 51.984 46.658 16.047 1.00 46.02 ? 114 TYR A CB 1 ATOM 920 C CG . TYR A 1 114 ? 52.315 47.328 17.360 1.00 44.82 ? 114 TYR A CG 1 ATOM 921 C CD1 . TYR A 1 114 ? 51.593 48.430 17.798 1.00 51.45 ? 114 TYR A CD1 1 ATOM 922 C CD2 . TYR A 1 114 ? 53.324 46.829 18.183 1.00 49.32 ? 114 TYR A CD2 1 ATOM 923 C CE1 . TYR A 1 114 ? 51.865 49.016 19.012 1.00 52.41 ? 114 TYR A CE1 1 ATOM 924 C CE2 . TYR A 1 114 ? 53.599 47.400 19.400 1.00 47.18 ? 114 TYR A CE2 1 ATOM 925 C CZ . TYR A 1 114 ? 52.870 48.512 19.805 1.00 51.14 ? 114 TYR A CZ 1 ATOM 926 O OH . TYR A 1 114 ? 53.136 49.118 21.009 1.00 55.19 ? 114 TYR A OH 1 ATOM 927 N N . ASP A 1 115 ? 50.702 44.858 18.531 1.00 42.67 ? 115 ASP A N 1 ATOM 928 C CA . ASP A 1 115 ? 51.056 43.992 19.670 1.00 40.18 ? 115 ASP A CA 1 ATOM 929 C C . ASP A 1 115 ? 50.079 42.806 19.864 1.00 40.18 ? 115 ASP A C 1 ATOM 930 O O . ASP A 1 115 ? 50.065 42.144 20.920 1.00 42.45 ? 115 ASP A O 1 ATOM 931 C CB . ASP A 1 115 ? 51.113 44.803 20.960 1.00 45.88 ? 115 ASP A CB 1 ATOM 932 C CG . ASP A 1 115 ? 49.766 45.323 21.350 1.00 50.46 ? 115 ASP A CG 1 ATOM 933 O OD1 . ASP A 1 115 ? 48.895 45.413 20.450 1.00 45.12 ? 115 ASP A OD1 1 ATOM 934 O OD2 . ASP A 1 115 ? 49.571 45.655 22.530 1.00 56.12 -1 115 ASP A OD2 1 ATOM 935 N N . GLY A 1 116 ? 49.270 42.520 18.842 1.00 38.84 ? 116 GLY A N 1 ATOM 936 C CA . GLY A 1 116 ? 48.336 41.403 18.914 1.00 37.01 ? 116 GLY A CA 1 ATOM 937 C C . GLY A 1 116 ? 47.006 41.763 19.550 1.00 36.11 ? 116 GLY A C 1 ATOM 938 O O . GLY A 1 116 ? 46.099 40.926 19.687 1.00 33.16 ? 116 GLY A O 1 ATOM 939 N N . LEU A 1 117 ? 46.846 43.028 19.934 1.00 37.97 ? 117 LEU A N 1 ATOM 940 C CA . LEU A 1 117 ? 45.638 43.386 20.675 1.00 34.16 ? 117 LEU A CA 1 ATOM 941 C C . LEU A 1 117 ? 44.535 43.508 19.672 1.00 33.35 ? 117 LEU A C 1 ATOM 942 O O . LEU A 1 117 ? 44.619 44.288 18.749 1.00 35.88 ? 117 LEU A O 1 ATOM 943 C CB . LEU A 1 117 ? 45.757 44.730 21.388 1.00 40.52 ? 117 LEU A CB 1 ATOM 944 C CG . LEU A 1 117 ? 44.502 45.065 22.190 1.00 38.24 ? 117 LEU A CG 1 ATOM 945 C CD1 . LEU A 1 117 ? 44.474 44.277 23.492 1.00 38.84 ? 117 LEU A CD1 1 ATOM 946 C CD2 . LEU A 1 117 ? 44.410 46.567 22.448 1.00 47.95 ? 117 LEU A CD2 1 ATOM 947 N N . ILE A 1 118 ? 43.482 42.745 19.860 1.00 33.42 ? 118 ILE A N 1 ATOM 948 C CA . ILE A 1 118 ? 42.374 42.795 18.943 1.00 36.44 ? 118 ILE A CA 1 ATOM 949 C C . ILE A 1 118 ? 41.215 43.435 19.635 1.00 29.85 ? 118 ILE A C 1 ATOM 950 O O . ILE A 1 118 ? 40.886 43.095 20.777 1.00 34.43 ? 118 ILE A O 1 ATOM 951 C CB . ILE A 1 118 ? 41.986 41.364 18.471 1.00 36.22 ? 118 ILE A CB 1 ATOM 952 C CG1 . ILE A 1 118 ? 42.994 40.894 17.434 1.00 42.33 ? 118 ILE A CG1 1 ATOM 953 C CG2 . ILE A 1 118 ? 40.619 41.353 17.815 1.00 41.30 ? 118 ILE A CG2 1 ATOM 954 C CD1 . ILE A 1 118 ? 42.874 39.433 17.090 1.00 46.64 ? 118 ILE A CD1 1 ATOM 955 N N . THR A 1 119 ? 40.633 44.399 18.955 1.00 34.46 ? 119 THR A N 1 ATOM 956 C CA . THR A 1 119 ? 39.420 45.038 19.415 1.00 34.44 ? 119 THR A CA 1 ATOM 957 C C . THR A 1 119 ? 38.314 44.783 18.416 1.00 39.67 ? 119 THR A C 1 ATOM 958 O O . THR A 1 119 ? 38.453 45.087 17.242 1.00 39.52 ? 119 THR A O 1 ATOM 959 C CB . THR A 1 119 ? 39.611 46.558 19.529 1.00 37.80 ? 119 THR A CB 1 ATOM 960 O OG1 . THR A 1 119 ? 40.685 46.801 20.444 1.00 40.36 ? 119 THR A OG1 1 ATOM 961 C CG2 . THR A 1 119 ? 38.363 47.159 20.061 1.00 40.16 ? 119 THR A CG2 1 ATOM 962 N N . TRP A 1 120 ? 37.219 44.205 18.890 1.00 34.86 ? 120 TRP A N 1 ATOM 963 C CA . TRP A 1 120 ? 36.146 43.788 18.005 1.00 35.01 ? 120 TRP A CA 1 ATOM 964 C C . TRP A 1 120 ? 34.806 44.374 18.474 1.00 32.77 ? 120 TRP A C 1 ATOM 965 O O . TRP A 1 120 ? 34.285 43.984 19.521 1.00 35.46 ? 120 TRP A O 1 ATOM 966 C CB . TRP A 1 120 ? 36.041 42.262 17.993 1.00 33.14 ? 120 TRP A CB 1 ATOM 967 C CG . TRP A 1 120 ? 35.055 41.749 17.007 1.00 37.40 ? 120 TRP A CG 1 ATOM 968 C CD1 . TRP A 1 120 ? 34.623 42.376 15.878 1.00 43.22 ? 120 TRP A CD1 1 ATOM 969 C CD2 . TRP A 1 120 ? 34.372 40.504 17.070 1.00 38.67 ? 120 TRP A CD2 1 ATOM 970 N NE1 . TRP A 1 120 ? 33.708 41.581 15.214 1.00 46.19 ? 120 TRP A NE1 1 ATOM 971 C CE2 . TRP A 1 120 ? 33.538 40.427 15.935 1.00 39.84 ? 120 TRP A CE2 1 ATOM 972 C CE3 . TRP A 1 120 ? 34.380 39.437 17.981 1.00 35.96 ? 120 TRP A CE3 1 ATOM 973 C CZ2 . TRP A 1 120 ? 32.737 39.320 15.682 1.00 42.55 ? 120 TRP A CZ2 1 ATOM 974 C CZ3 . TRP A 1 120 ? 33.586 38.341 17.715 1.00 45.54 ? 120 TRP A CZ3 1 ATOM 975 C CH2 . TRP A 1 120 ? 32.777 38.291 16.582 1.00 43.56 ? 120 TRP A CH2 1 ATOM 976 N N . ASP A 1 121 ? 34.305 45.342 17.709 1.00 40.46 ? 121 ASP A N 1 ATOM 977 C CA . ASP A 1 121 ? 32.992 45.938 17.912 1.00 45.64 ? 121 ASP A CA 1 ATOM 978 C C . ASP A 1 121 ? 32.007 45.323 16.944 1.00 50.42 ? 121 ASP A C 1 ATOM 979 O O . ASP A 1 121 ? 32.269 45.307 15.737 1.00 41.96 ? 121 ASP A O 1 ATOM 980 C CB . ASP A 1 121 ? 33.051 47.433 17.624 1.00 45.38 ? 121 ASP A CB 1 ATOM 981 C CG . ASP A 1 121 ? 33.835 48.203 18.660 1.00 47.98 ? 121 ASP A CG 1 ATOM 982 O OD1 . ASP A 1 121 ? 33.508 48.136 19.856 1.00 50.66 -1 121 ASP A OD1 1 ATOM 983 O OD2 . ASP A 1 121 ? 34.769 48.920 18.284 1.00 50.96 ? 121 ASP A OD2 1 ATOM 984 N N . ALA A 1 122 ? 30.883 44.830 17.452 1.00 45.75 ? 122 ALA A N 1 ATOM 985 C CA . ALA A 1 122 ? 29.862 44.211 16.597 1.00 50.42 ? 122 ALA A CA 1 ATOM 986 C C . ALA A 1 122 ? 28.456 44.463 17.121 1.00 50.08 ? 122 ALA A C 1 ATOM 987 O O . ALA A 1 122 ? 28.202 44.320 18.311 1.00 49.42 ? 122 ALA A O 1 ATOM 988 C CB . ALA A 1 122 ? 30.094 42.722 16.522 1.00 51.59 ? 122 ALA A CB 1 ATOM 989 N N . PRO A 1 123 ? 27.520 44.799 16.228 1.00 56.26 ? 123 PRO A N 1 ATOM 990 C CA . PRO A 1 123 ? 26.129 44.978 16.648 1.00 51.65 ? 123 PRO A CA 1 ATOM 991 C C . PRO A 1 123 ? 25.488 43.645 16.973 1.00 56.34 ? 123 PRO A C 1 ATOM 992 O O . PRO A 1 123 ? 25.957 42.616 16.495 1.00 50.64 ? 123 PRO A O 1 ATOM 993 C CB . PRO A 1 123 ? 25.473 45.550 15.397 1.00 55.98 ? 123 PRO A CB 1 ATOM 994 C CG . PRO A 1 123 ? 26.238 44.879 14.279 1.00 57.30 ? 123 PRO A CG 1 ATOM 995 C CD . PRO A 1 123 ? 27.659 44.810 14.759 1.00 51.32 ? 123 PRO A CD 1 ATOM 996 N N . ALA A 1 124 ? 24.423 43.653 17.764 1.00 48.88 ? 124 ALA A N 1 ATOM 997 C CA . ALA A 1 124 ? 23.738 42.413 18.126 1.00 51.48 ? 124 ALA A CA 1 ATOM 998 C C . ALA A 1 124 ? 22.298 42.675 18.528 1.00 51.02 ? 124 ALA A C 1 ATOM 999 O O . ALA A 1 124 ? 21.972 43.734 19.045 1.00 54.95 ? 124 ALA A O 1 ATOM 1000 C CB . ALA A 1 124 ? 24.460 41.713 19.264 1.00 47.42 ? 124 ALA A CB 1 ATOM 1001 N N . ILE A 1 125 ? 21.450 41.688 18.302 1.00 51.65 ? 125 ILE A N 1 ATOM 1002 C CA . ILE A 1 125 ? 20.065 41.741 18.710 1.00 48.15 ? 125 ILE A CA 1 ATOM 1003 C C . ILE A 1 125 ? 19.822 40.577 19.616 1.00 52.74 ? 125 ILE A C 1 ATOM 1004 O O . ILE A 1 125 ? 20.044 39.438 19.228 1.00 56.08 ? 125 ILE A O 1 ATOM 1005 C CB . ILE A 1 125 ? 19.130 41.625 17.515 1.00 53.88 ? 125 ILE A CB 1 ATOM 1006 C CG1 . ILE A 1 125 ? 19.352 42.790 16.545 1.00 52.84 ? 125 ILE A CG1 1 ATOM 1007 C CG2 . ILE A 1 125 ? 17.692 41.576 17.992 1.00 54.17 ? 125 ILE A CG2 1 ATOM 1008 C CD1 . ILE A 1 125 ? 18.591 42.658 15.209 1.00 60.05 ? 125 ILE A CD1 1 ATOM 1009 N N . THR A 1 126 ? 19.410 40.859 20.848 1.00 53.83 ? 126 THR A N 1 ATOM 1010 C CA . THR A 1 126 ? 19.212 39.813 21.851 1.00 49.41 ? 126 THR A CA 1 ATOM 1011 C C . THR A 1 126 ? 17.758 39.685 22.224 1.00 47.08 ? 126 THR A C 1 ATOM 1012 O O . THR A 1 126 ? 17.055 40.686 22.358 1.00 48.99 ? 126 THR A O 1 ATOM 1013 C CB . THR A 1 126 ? 19.969 40.107 23.145 1.00 53.89 ? 126 THR A CB 1 ATOM 1014 O OG1 . THR A 1 126 ? 19.587 41.397 23.636 1.00 54.67 ? 126 THR A OG1 1 ATOM 1015 C CG2 . THR A 1 126 ? 21.459 40.075 22.918 1.00 56.51 ? 126 THR A CG2 1 ATOM 1016 N N . LYS A 1 127 ? 17.321 38.445 22.378 1.00 45.90 ? 127 LYS A N 1 ATOM 1017 C CA . LYS A 1 127 ? 15.995 38.146 22.886 1.00 45.19 ? 127 LYS A CA 1 ATOM 1018 C C . LYS A 1 127 ? 16.148 37.282 24.106 1.00 48.31 ? 127 LYS A C 1 ATOM 1019 O O . LYS A 1 127 ? 16.767 36.211 24.075 1.00 48.85 ? 127 LYS A O 1 ATOM 1020 C CB . LYS A 1 127 ? 15.143 37.440 21.839 1.00 51.44 ? 127 LYS A CB 1 ATOM 1021 C CG . LYS A 1 127 ? 15.068 38.193 20.524 1.00 57.03 ? 127 LYS A CG 1 ATOM 1022 C CD . LYS A 1 127 ? 14.123 37.521 19.535 1.00 60.06 ? 127 LYS A CD 1 ATOM 1023 C CE . LYS A 1 127 ? 12.695 38.021 19.696 1.00 66.45 ? 127 LYS A CE 1 ATOM 1024 N NZ . LYS A 1 127 ? 11.747 37.342 18.769 1.00 76.53 1 127 LYS A NZ 1 ATOM 1025 N N . SER A 1 128 ? 15.600 37.746 25.208 1.00 40.39 ? 128 SER A N 1 ATOM 1026 C CA . SER A 1 128 ? 15.847 37.071 26.466 1.00 48.06 ? 128 SER A CA 1 ATOM 1027 C C . SER A 1 128 ? 14.689 37.330 27.376 1.00 42.52 ? 128 SER A C 1 ATOM 1028 O O . SER A 1 128 ? 13.983 38.317 27.204 1.00 42.63 ? 128 SER A O 1 ATOM 1029 C CB . SER A 1 128 ? 17.145 37.573 27.108 1.00 50.52 ? 128 SER A CB 1 ATOM 1030 O OG . SER A 1 128 ? 17.154 38.986 27.219 1.00 43.90 ? 128 SER A OG 1 ATOM 1031 N N . SER A 1 129 ? 14.514 36.446 28.348 1.00 41.14 ? 129 SER A N 1 ATOM 1032 C CA . SER A 1 129 ? 13.370 36.483 29.227 1.00 47.18 ? 129 SER A CA 1 ATOM 1033 C C . SER A 1 129 ? 13.648 37.412 30.377 1.00 44.12 ? 129 SER A C 1 ATOM 1034 O O . SER A 1 129 ? 14.799 37.561 30.794 1.00 41.67 ? 129 SER A O 1 ATOM 1035 C CB . SER A 1 129 ? 13.075 35.104 29.790 1.00 52.71 ? 129 SER A CB 1 ATOM 1036 O OG . SER A 1 129 ? 12.770 34.190 28.754 1.00 61.18 ? 129 SER A OG 1 ATOM 1037 N N . CYS A 1 130 ? 12.581 38.022 30.886 1.00 40.28 ? 130 CYS A N 1 ATOM 1038 C CA . CYS A 1 130 ? 12.696 38.986 31.961 1.00 39.72 ? 130 CYS A CA 1 ATOM 1039 C C . CYS A 1 130 ? 11.803 38.547 33.114 1.00 39.37 ? 130 CYS A C 1 ATOM 1040 O O . CYS A 1 130 ? 10.847 37.807 32.916 1.00 47.71 ? 130 CYS A O 1 ATOM 1041 C CB . CYS A 1 130 ? 12.236 40.357 31.472 1.00 41.30 ? 130 CYS A CB 1 ATOM 1042 S SG . CYS A 1 130 ? 13.235 41.061 30.125 1.00 46.27 ? 130 CYS A SG 1 ATOM 1043 N N . VAL A 1 131 ? 12.092 39.016 34.315 1.00 40.23 ? 131 VAL A N 1 ATOM 1044 C CA . VAL A 1 131 ? 11.222 38.725 35.450 1.00 43.38 ? 131 VAL A CA 1 ATOM 1045 C C . VAL A 1 131 ? 10.598 40.002 36.014 1.00 50.92 ? 131 VAL A C 1 ATOM 1046 O O . VAL A 1 131 ? 11.296 40.989 36.279 1.00 42.26 ? 131 VAL A O 1 ATOM 1047 C CB . VAL A 1 131 ? 11.979 38.014 36.545 1.00 38.86 ? 131 VAL A CB 1 ATOM 1048 C CG1 . VAL A 1 131 ? 11.098 37.817 37.743 1.00 50.59 ? 131 VAL A CG1 1 ATOM 1049 C CG2 . VAL A 1 131 ? 12.508 36.666 36.034 1.00 42.92 ? 131 VAL A CG2 1 ATOM 1050 N N . VAL A 1 132 ? 9.279 39.972 36.195 1.00 47.13 ? 132 VAL A N 1 ATOM 1051 C CA . VAL A 1 132 ? 8.558 41.132 36.700 1.00 51.40 ? 132 VAL A CA 1 ATOM 1052 C C . VAL A 1 132 ? 8.871 41.314 38.162 1.00 53.88 ? 132 VAL A C 1 ATOM 1053 O O . VAL A 1 132 ? 9.205 40.368 38.875 1.00 50.05 ? 132 VAL A O 1 ATOM 1054 C CB . VAL A 1 132 ? 7.031 41.006 36.488 1.00 47.43 ? 132 VAL A CB 1 ATOM 1055 C CG1 . VAL A 1 132 ? 6.273 42.136 37.183 1.00 58.15 ? 132 VAL A CG1 1 ATOM 1056 C CG2 . VAL A 1 132 ? 6.717 41.001 35.002 1.00 54.63 ? 132 VAL A CG2 1 ATOM 1057 N N . ASP A 1 133 ? 8.825 42.564 38.584 1.00 47.11 ? 133 ASP A N 1 ATOM 1058 C CA . ASP A 1 133 ? 8.845 42.886 39.986 1.00 54.93 ? 133 ASP A CA 1 ATOM 1059 C C . ASP A 1 133 ? 7.891 44.044 40.175 1.00 53.92 ? 133 ASP A C 1 ATOM 1060 O O . ASP A 1 133 ? 7.896 44.987 39.370 1.00 56.68 ? 133 ASP A O 1 ATOM 1061 C CB . ASP A 1 133 ? 10.240 43.298 40.428 1.00 52.91 ? 133 ASP A CB 1 ATOM 1062 C CG . ASP A 1 133 ? 10.217 43.996 41.782 1.00 61.42 ? 133 ASP A CG 1 ATOM 1063 O OD1 . ASP A 1 133 ? 10.037 45.240 41.839 1.00 57.77 -1 133 ASP A OD1 1 ATOM 1064 O OD2 . ASP A 1 133 ? 10.346 43.279 42.790 1.00 62.26 ? 133 ASP A OD2 1 ATOM 1065 N N . VAL A 1 134 ? 7.073 43.988 41.227 1.00 46.73 ? 134 VAL A N 1 ATOM 1066 C CA . VAL A 1 134 ? 6.216 45.117 41.563 1.00 43.57 ? 134 VAL A CA 1 ATOM 1067 C C . VAL A 1 134 ? 6.394 45.466 43.037 1.00 52.69 ? 134 VAL A C 1 ATOM 1068 O O . VAL A 1 134 ? 5.562 46.150 43.636 1.00 52.08 ? 134 VAL A O 1 ATOM 1069 C CB . VAL A 1 134 ? 4.728 44.827 41.264 1.00 54.51 ? 134 VAL A CB 1 ATOM 1070 C CG1 . VAL A 1 134 ? 4.541 44.500 39.779 1.00 56.40 ? 134 VAL A CG1 1 ATOM 1071 C CG2 . VAL A 1 134 ? 4.221 43.683 42.126 1.00 50.69 ? 134 VAL A CG2 1 ATOM 1072 N N . THR A 1 135 ? 7.495 44.978 43.604 1.00 47.89 ? 135 THR A N 1 ATOM 1073 C CA . THR A 1 135 ? 7.822 45.211 44.999 1.00 55.41 ? 135 THR A CA 1 ATOM 1074 C C . THR A 1 135 ? 8.343 46.633 45.206 1.00 51.38 ? 135 THR A C 1 ATOM 1075 O O . THR A 1 135 ? 7.939 47.308 46.137 1.00 59.15 ? 135 THR A O 1 ATOM 1076 C CB . THR A 1 135 ? 8.908 44.203 45.465 1.00 55.55 ? 135 THR A CB 1 ATOM 1077 O OG1 . THR A 1 135 ? 8.374 42.883 45.400 1.00 61.16 ? 135 THR A OG1 1 ATOM 1078 C CG2 . THR A 1 135 ? 9.345 44.484 46.894 1.00 66.62 ? 135 THR A CG2 1 ATOM 1079 N N . TYR A 1 136 ? 9.254 47.062 44.334 1.00 46.77 ? 136 TYR A N 1 ATOM 1080 C CA . TYR A 1 136 ? 9.935 48.348 44.479 1.00 55.85 ? 136 TYR A CA 1 ATOM 1081 C C . TYR A 1 136 ? 9.281 49.416 43.611 1.00 59.25 ? 136 TYR A C 1 ATOM 1082 O O . TYR A 1 136 ? 8.778 49.129 42.518 1.00 53.72 ? 136 TYR A O 1 ATOM 1083 C CB . TYR A 1 136 ? 11.412 48.208 44.070 1.00 57.32 ? 136 TYR A CB 1 ATOM 1084 C CG . TYR A 1 136 ? 12.199 47.190 44.869 1.00 58.31 ? 136 TYR A CG 1 ATOM 1085 C CD1 . TYR A 1 136 ? 12.474 47.397 46.229 1.00 70.64 ? 136 TYR A CD1 1 ATOM 1086 C CD2 . TYR A 1 136 ? 12.685 46.030 44.268 1.00 59.82 ? 136 TYR A CD2 1 ATOM 1087 C CE1 . TYR A 1 136 ? 13.203 46.463 46.971 1.00 66.77 ? 136 TYR A CE1 1 ATOM 1088 C CE2 . TYR A 1 136 ? 13.419 45.092 44.999 1.00 65.88 ? 136 TYR A CE2 1 ATOM 1089 C CZ . TYR A 1 136 ? 13.668 45.317 46.349 1.00 73.93 ? 136 TYR A CZ 1 ATOM 1090 O OH . TYR A 1 136 ? 14.390 44.394 47.071 1.00 78.22 ? 136 TYR A OH 1 ATOM 1091 N N . PHE A 1 137 ? 9.308 50.653 44.088 1.00 51.07 ? 137 PHE A N 1 ATOM 1092 C CA . PHE A 1 137 ? 8.741 51.753 43.341 1.00 47.97 ? 137 PHE A CA 1 ATOM 1093 C C . PHE A 1 137 ? 9.357 51.770 41.941 1.00 44.88 ? 137 PHE A C 1 ATOM 1094 O O . PHE A 1 137 ? 10.549 51.489 41.784 1.00 47.59 ? 137 PHE A O 1 ATOM 1095 C CB . PHE A 1 137 ? 9.030 53.058 44.067 1.00 56.68 ? 137 PHE A CB 1 ATOM 1096 C CG . PHE A 1 137 ? 8.531 54.260 43.346 1.00 59.26 ? 137 PHE A CG 1 ATOM 1097 C CD1 . PHE A 1 137 ? 7.216 54.683 43.491 1.00 62.36 ? 137 PHE A CD1 1 ATOM 1098 C CD2 . PHE A 1 137 ? 9.372 54.965 42.504 1.00 71.09 ? 137 PHE A CD2 1 ATOM 1099 C CE1 . PHE A 1 137 ? 6.748 55.795 42.808 1.00 60.04 ? 137 PHE A CE1 1 ATOM 1100 C CE2 . PHE A 1 137 ? 8.909 56.089 41.820 1.00 73.43 ? 137 PHE A CE2 1 ATOM 1101 C CZ . PHE A 1 137 ? 7.599 56.496 41.968 1.00 61.66 ? 137 PHE A CZ 1 ATOM 1102 N N . PRO A 1 138 ? 8.556 52.074 40.902 1.00 56.49 ? 138 PRO A N 1 ATOM 1103 C CA . PRO A 1 138 ? 7.122 52.413 40.839 1.00 52.85 ? 138 PRO A CA 1 ATOM 1104 C C . PRO A 1 138 ? 6.210 51.177 40.699 1.00 55.36 ? 138 PRO A C 1 ATOM 1105 O O . PRO A 1 138 ? 5.082 51.299 40.218 1.00 58.58 ? 138 PRO A O 1 ATOM 1106 C CB . PRO A 1 138 ? 7.038 53.280 39.582 1.00 60.02 ? 138 PRO A CB 1 ATOM 1107 C CG . PRO A 1 138 ? 8.083 52.641 38.657 1.00 62.48 ? 138 PRO A CG 1 ATOM 1108 C CD . PRO A 1 138 ? 9.198 52.162 39.567 1.00 54.29 ? 138 PRO A CD 1 ATOM 1109 N N . PHE A 1 139 ? 6.677 50.015 41.133 1.00 44.20 ? 139 PHE A N 1 ATOM 1110 C CA . PHE A 1 139 ? 5.835 48.844 41.264 1.00 47.05 ? 139 PHE A CA 1 ATOM 1111 C C . PHE A 1 139 ? 5.350 48.271 39.950 1.00 51.19 ? 139 PHE A C 1 ATOM 1112 O O . PHE A 1 139 ? 4.336 47.620 39.884 1.00 48.34 ? 139 PHE A O 1 ATOM 1113 C CB . PHE A 1 139 ? 4.658 49.166 42.147 1.00 52.06 ? 139 PHE A CB 1 ATOM 1114 C CG . PHE A 1 139 ? 5.037 49.908 43.378 1.00 60.03 ? 139 PHE A CG 1 ATOM 1115 C CD1 . PHE A 1 139 ? 5.991 49.412 44.223 1.00 61.55 ? 139 PHE A CD1 1 ATOM 1116 C CD2 . PHE A 1 139 ? 4.440 51.099 43.687 1.00 64.85 ? 139 PHE A CD2 1 ATOM 1117 C CE1 . PHE A 1 139 ? 6.351 50.085 45.353 1.00 51.89 ? 139 PHE A CE1 1 ATOM 1118 C CE2 . PHE A 1 139 ? 4.799 51.781 44.813 1.00 61.55 ? 139 PHE A CE2 1 ATOM 1119 C CZ . PHE A 1 139 ? 5.759 51.270 45.641 1.00 48.61 ? 139 PHE A CZ 1 ATOM 1120 N N . ASP A 1 140 ? 6.095 48.568 38.902 1.00 44.89 ? 140 ASP A N 1 ATOM 1121 C CA . ASP A 1 140 ? 5.854 48.015 37.576 1.00 44.65 ? 140 ASP A CA 1 ATOM 1122 C C . ASP A 1 140 ? 7.191 47.937 36.894 1.00 43.14 ? 140 ASP A C 1 ATOM 1123 O O . ASP A 1 140 ? 7.565 48.847 36.194 1.00 48.46 ? 140 ASP A O 1 ATOM 1124 C CB . ASP A 1 140 ? 4.905 48.918 36.810 1.00 45.33 ? 140 ASP A CB 1 ATOM 1125 C CG . ASP A 1 140 ? 4.103 48.190 35.800 1.00 57.17 ? 140 ASP A CG 1 ATOM 1126 O OD1 . ASP A 1 140 ? 4.553 47.141 35.372 1.00 52.92 ? 140 ASP A OD1 1 ATOM 1127 O OD2 . ASP A 1 140 ? 3.018 48.671 35.438 1.00 64.43 -1 140 ASP A OD2 1 ATOM 1128 N N . ASN A 1 141 ? 7.950 46.898 37.185 1.00 39.55 ? 141 ASN A N 1 ATOM 1129 C CA . ASN A 1 141 ? 9.335 46.829 36.721 1.00 44.14 ? 141 ASN A CA 1 ATOM 1130 C C . ASN A 1 141 ? 9.660 45.495 36.102 1.00 41.87 ? 141 ASN A C 1 ATOM 1131 O O . ASN A 1 141 ? 8.945 44.522 36.276 1.00 45.33 ? 141 ASN A O 1 ATOM 1132 C CB . ASN A 1 141 ? 10.269 46.995 37.900 1.00 39.74 ? 141 ASN A CB 1 ATOM 1133 C CG . ASN A 1 141 ? 9.783 48.055 38.846 1.00 49.15 ? 141 ASN A CG 1 ATOM 1134 O OD1 . ASN A 1 141 ? 9.490 49.184 38.431 1.00 53.05 ? 141 ASN A OD1 1 ATOM 1135 N ND2 . ASN A 1 141 ? 9.619 47.690 40.115 1.00 56.64 ? 141 ASN A ND2 1 ATOM 1136 N N . GLN A 1 142 ? 10.783 45.467 35.408 1.00 44.90 ? 142 GLN A N 1 ATOM 1137 C CA . GLN A 1 142 ? 11.266 44.270 34.758 1.00 36.76 ? 142 GLN A CA 1 ATOM 1138 C C . GLN A 1 142 ? 12.718 44.129 35.102 1.00 43.13 ? 142 GLN A C 1 ATOM 1139 O O . GLN A 1 142 ? 13.471 45.118 35.146 1.00 42.41 ? 142 GLN A O 1 ATOM 1140 C CB . GLN A 1 142 ? 11.124 44.432 33.252 1.00 36.42 ? 142 GLN A CB 1 ATOM 1141 C CG . GLN A 1 142 ? 9.670 44.497 32.756 1.00 44.06 ? 142 GLN A CG 1 ATOM 1142 C CD . GLN A 1 142 ? 8.975 43.133 32.802 1.00 55.38 ? 142 GLN A CD 1 ATOM 1143 O OE1 . GLN A 1 142 ? 9.575 42.122 33.193 1.00 48.42 ? 142 GLN A OE1 1 ATOM 1144 N NE2 . GLN A 1 142 ? 7.714 43.107 32.427 1.00 49.73 ? 142 GLN A NE2 1 ATOM 1145 N N . GLN A 1 143 ? 13.121 42.898 35.358 1.00 38.30 ? 143 GLN A N 1 ATOM 1146 C CA . GLN A 1 143 ? 14.516 42.594 35.576 1.00 37.82 ? 143 GLN A CA 1 ATOM 1147 C C . GLN A 1 143 ? 14.917 41.696 34.424 1.00 39.24 ? 143 GLN A C 1 ATOM 1148 O O . GLN A 1 143 ? 14.383 40.604 34.285 1.00 41.51 ? 143 GLN A O 1 ATOM 1149 C CB . GLN A 1 143 ? 14.697 41.879 36.923 1.00 48.17 ? 143 GLN A CB 1 ATOM 1150 C CG . GLN A 1 143 ? 16.085 41.275 37.085 1.00 57.64 ? 143 GLN A CG 1 ATOM 1151 C CD . GLN A 1 143 ? 16.278 40.466 38.366 1.00 65.25 ? 143 GLN A CD 1 ATOM 1152 O OE1 . GLN A 1 143 ? 17.220 39.669 38.463 1.00 65.95 ? 143 GLN A OE1 1 ATOM 1153 N NE2 . GLN A 1 143 ? 15.404 40.674 39.354 1.00 66.51 ? 143 GLN A NE2 1 ATOM 1154 N N . CYS A 1 144 ? 15.814 42.170 33.562 1.00 36.64 ? 144 CYS A N 1 ATOM 1155 C CA . CYS A 1 144 ? 16.141 41.463 32.336 1.00 36.84 ? 144 CYS A CA 1 ATOM 1156 C C . CYS A 1 144 ? 17.622 41.090 32.356 1.00 43.05 ? 144 CYS A C 1 ATOM 1157 O O . CYS A 1 144 ? 18.507 41.923 32.163 1.00 36.06 ? 144 CYS A O 1 ATOM 1158 C CB . CYS A 1 144 ? 15.827 42.338 31.142 1.00 46.72 ? 144 CYS A CB 1 ATOM 1159 S SG . CYS A 1 144 ? 14.066 42.749 31.026 1.00 42.59 ? 144 CYS A SG 1 ATOM 1160 N N . ASN A 1 145 ? 17.925 39.845 32.658 1.00 36.83 ? 145 ASN A N 1 ATOM 1161 C CA . ASN A 1 145 ? 19.335 39.464 32.680 1.00 38.04 ? 145 ASN A CA 1 ATOM 1162 C C . ASN A 1 145 ? 19.813 39.112 31.273 1.00 41.23 ? 145 ASN A C 1 ATOM 1163 O O . ASN A 1 145 ? 19.116 38.457 30.507 1.00 38.53 ? 145 ASN A O 1 ATOM 1164 C CB . ASN A 1 145 ? 19.597 38.254 33.593 1.00 36.57 ? 145 ASN A CB 1 ATOM 1165 C CG . ASN A 1 145 ? 19.735 38.611 35.013 1.00 38.91 ? 145 ASN A CG 1 ATOM 1166 O OD1 . ASN A 1 145 ? 19.860 39.797 35.389 1.00 39.06 ? 145 ASN A OD1 1 ATOM 1167 N ND2 . ASN A 1 145 ? 19.741 37.576 35.854 1.00 41.63 ? 145 ASN A ND2 1 ATOM 1168 N N . LEU A 1 146 ? 21.013 39.572 30.952 1.00 37.23 ? 146 LEU A N 1 ATOM 1169 C CA . LEU A 1 146 ? 21.713 39.165 29.754 1.00 39.13 ? 146 LEU A CA 1 ATOM 1170 C C . LEU A 1 146 ? 23.046 38.540 30.165 1.00 34.82 ? 146 LEU A C 1 ATOM 1171 O O . LEU A 1 146 ? 23.919 39.223 30.690 1.00 32.94 ? 146 LEU A O 1 ATOM 1172 C CB . LEU A 1 146 ? 21.952 40.366 28.861 1.00 44.44 ? 146 LEU A CB 1 ATOM 1173 C CG . LEU A 1 146 ? 20.730 41.244 28.584 1.00 46.23 ? 146 LEU A CG 1 ATOM 1174 C CD1 . LEU A 1 146 ? 21.206 42.607 28.151 1.00 53.55 ? 146 LEU A CD1 1 ATOM 1175 C CD2 . LEU A 1 146 ? 19.908 40.635 27.509 1.00 47.92 ? 146 LEU A CD2 1 ATOM 1176 N N . THR A 1 147 ? 23.195 37.249 29.895 1.00 38.26 ? 147 THR A N 1 ATOM 1177 C CA . THR A 1 147 ? 24.345 36.471 30.343 1.00 35.80 ? 147 THR A CA 1 ATOM 1178 C C . THR A 1 147 ? 25.194 36.054 29.129 1.00 34.66 ? 147 THR A C 1 ATOM 1179 O O . THR A 1 147 ? 24.691 35.491 28.181 1.00 35.13 ? 147 THR A O 1 ATOM 1180 C CB . THR A 1 147 ? 23.835 35.256 31.106 1.00 33.23 ? 147 THR A CB 1 ATOM 1181 O OG1 . THR A 1 147 ? 23.134 35.693 32.257 1.00 30.21 ? 147 THR A OG1 1 ATOM 1182 C CG2 . THR A 1 147 ? 24.979 34.339 31.569 1.00 30.24 ? 147 THR A CG2 1 ATOM 1183 N N . PHE A 1 148 ? 26.477 36.390 29.147 1.00 34.64 ? 148 PHE A N 1 ATOM 1184 C CA . PHE A 1 148 ? 27.344 36.165 27.991 1.00 33.35 ? 148 PHE A CA 1 ATOM 1185 C C . PHE A 1 148 ? 28.485 35.252 28.401 1.00 34.02 ? 148 PHE A C 1 ATOM 1186 O O . PHE A 1 148 ? 29.024 35.381 29.491 1.00 32.38 ? 148 PHE A O 1 ATOM 1187 C CB . PHE A 1 148 ? 27.951 37.463 27.488 1.00 32.53 ? 148 PHE A CB 1 ATOM 1188 C CG . PHE A 1 148 ? 26.957 38.397 26.888 1.00 30.62 ? 148 PHE A CG 1 ATOM 1189 C CD1 . PHE A 1 148 ? 26.625 38.303 25.547 1.00 33.18 ? 148 PHE A CD1 1 ATOM 1190 C CD2 . PHE A 1 148 ? 26.335 39.343 27.674 1.00 34.96 ? 148 PHE A CD2 1 ATOM 1191 C CE1 . PHE A 1 148 ? 25.682 39.156 24.990 1.00 40.51 ? 148 PHE A CE1 1 ATOM 1192 C CE2 . PHE A 1 148 ? 25.424 40.200 27.138 1.00 40.52 ? 148 PHE A CE2 1 ATOM 1193 C CZ . PHE A 1 148 ? 25.087 40.107 25.790 1.00 37.83 ? 148 PHE A CZ 1 ATOM 1194 N N . GLY A 1 149 ? 28.865 34.365 27.505 1.00 35.27 ? 149 GLY A N 1 ATOM 1195 C CA . GLY A 1 149 ? 29.938 33.450 27.781 1.00 31.80 ? 149 GLY A CA 1 ATOM 1196 C C . GLY A 1 149 ? 30.404 32.767 26.505 1.00 34.35 ? 149 GLY A C 1 ATOM 1197 O O . GLY A 1 149 ? 29.770 32.877 25.447 1.00 36.41 ? 149 GLY A O 1 ATOM 1198 N N . SER A 1 150 ? 31.518 32.064 26.601 1.00 31.44 ? 150 SER A N 1 ATOM 1199 C CA . SER A 1 150 ? 31.999 31.306 25.465 1.00 31.14 ? 150 SER A CA 1 ATOM 1200 C C . SER A 1 150 ? 31.118 30.103 25.269 1.00 37.96 ? 150 SER A C 1 ATOM 1201 O O . SER A 1 150 ? 30.753 29.415 26.203 1.00 34.90 ? 150 SER A O 1 ATOM 1202 C CB . SER A 1 150 ? 33.464 30.886 25.620 1.00 31.23 ? 150 SER A CB 1 ATOM 1203 O OG . SER A 1 150 ? 33.922 30.206 24.445 1.00 37.05 ? 150 SER A OG 1 ATOM 1204 N N . TRP A 1 151 ? 30.759 29.840 24.018 1.00 34.91 ? 151 TRP A N 1 ATOM 1205 C CA . TRP A 1 151 ? 30.017 28.635 23.698 1.00 39.67 ? 151 TRP A CA 1 ATOM 1206 C C . TRP A 1 151 ? 30.981 27.437 23.587 1.00 48.03 ? 151 TRP A C 1 ATOM 1207 O O . TRP A 1 151 ? 30.583 26.291 23.742 1.00 48.13 ? 151 TRP A O 1 ATOM 1208 C CB . TRP A 1 151 ? 29.282 28.842 22.344 1.00 42.80 ? 151 TRP A CB 1 ATOM 1209 C CG . TRP A 1 151 ? 28.089 27.957 22.127 1.00 49.99 ? 151 TRP A CG 1 ATOM 1210 C CD1 . TRP A 1 151 ? 27.936 27.023 21.148 1.00 60.31 ? 151 TRP A CD1 1 ATOM 1211 C CD2 . TRP A 1 151 ? 26.883 27.924 22.905 1.00 57.45 ? 151 TRP A CD2 1 ATOM 1212 N NE1 . TRP A 1 151 ? 26.708 26.404 21.263 1.00 64.04 ? 151 TRP A NE1 1 ATOM 1213 C CE2 . TRP A 1 151 ? 26.041 26.939 22.332 1.00 64.18 ? 151 TRP A CE2 1 ATOM 1214 C CE3 . TRP A 1 151 ? 26.433 28.622 24.022 1.00 57.55 ? 151 TRP A CE3 1 ATOM 1215 C CZ2 . TRP A 1 151 ? 24.782 26.634 22.851 1.00 56.08 ? 151 TRP A CZ2 1 ATOM 1216 C CZ3 . TRP A 1 151 ? 25.165 28.319 24.536 1.00 54.39 ? 151 TRP A CZ3 1 ATOM 1217 C CH2 . TRP A 1 151 ? 24.364 27.341 23.947 1.00 56.73 ? 151 TRP A CH2 1 ATOM 1218 N N . THR A 1 152 ? 32.250 27.715 23.286 1.00 45.14 ? 152 THR A N 1 ATOM 1219 C CA . THR A 1 152 ? 33.220 26.678 22.922 1.00 43.61 ? 152 THR A CA 1 ATOM 1220 C C . THR A 1 152 ? 34.191 26.312 24.037 1.00 47.63 ? 152 THR A C 1 ATOM 1221 O O . THR A 1 152 ? 34.515 25.143 24.219 1.00 41.98 ? 152 THR A O 1 ATOM 1222 C CB . THR A 1 152 ? 34.056 27.129 21.699 1.00 43.95 ? 152 THR A CB 1 ATOM 1223 O OG1 . THR A 1 152 ? 33.201 27.312 20.562 1.00 49.96 ? 152 THR A OG1 1 ATOM 1224 C CG2 . THR A 1 152 ? 35.137 26.097 21.359 1.00 53.08 ? 152 THR A CG2 1 ATOM 1225 N N . TYR A 1 153 ? 34.630 27.311 24.799 1.00 36.81 ? 153 TYR A N 1 ATOM 1226 C CA . TYR A 1 153 ? 35.780 27.161 25.706 1.00 31.96 ? 153 TYR A CA 1 ATOM 1227 C C . TYR A 1 153 ? 35.407 27.267 27.162 1.00 37.01 ? 153 TYR A C 1 ATOM 1228 O O . TYR A 1 153 ? 34.495 28.008 27.500 1.00 32.34 ? 153 TYR A O 1 ATOM 1229 C CB . TYR A 1 153 ? 36.802 28.267 25.403 1.00 35.07 ? 153 TYR A CB 1 ATOM 1230 C CG . TYR A 1 153 ? 37.368 28.187 24.036 1.00 34.07 ? 153 TYR A CG 1 ATOM 1231 C CD1 . TYR A 1 153 ? 38.313 27.218 23.706 1.00 35.75 ? 153 TYR A CD1 1 ATOM 1232 C CD2 . TYR A 1 153 ? 36.948 29.058 23.046 1.00 34.11 ? 153 TYR A CD2 1 ATOM 1233 C CE1 . TYR A 1 153 ? 38.819 27.123 22.421 1.00 40.26 ? 153 TYR A CE1 1 ATOM 1234 C CE2 . TYR A 1 153 ? 37.430 28.957 21.786 1.00 34.92 ? 153 TYR A CE2 1 ATOM 1235 C CZ . TYR A 1 153 ? 38.368 27.988 21.479 1.00 38.56 ? 153 TYR A CZ 1 ATOM 1236 O OH . TYR A 1 153 ? 38.846 27.928 20.225 1.00 36.43 ? 153 TYR A OH 1 ATOM 1237 N N . ASN A 1 154 ? 36.128 26.553 28.022 1.00 34.17 ? 154 ASN A N 1 ATOM 1238 C CA . ASN A 1 154 ? 35.933 26.680 29.451 1.00 31.62 ? 154 ASN A CA 1 ATOM 1239 C C . ASN A 1 154 ? 36.870 27.743 29.967 1.00 31.50 ? 154 ASN A C 1 ATOM 1240 O O . ASN A 1 154 ? 37.677 28.308 29.217 1.00 30.05 ? 154 ASN A O 1 ATOM 1241 C CB . ASN A 1 154 ? 36.121 25.371 30.209 1.00 34.91 ? 154 ASN A CB 1 ATOM 1242 C CG . ASN A 1 154 ? 37.549 24.872 30.163 1.00 35.54 ? 154 ASN A CG 1 ATOM 1243 O OD1 . ASN A 1 154 ? 38.491 25.627 30.445 1.00 39.02 ? 154 ASN A OD1 1 ATOM 1244 N ND2 . ASN A 1 154 ? 37.723 23.601 29.773 1.00 37.63 ? 154 ASN A ND2 1 ATOM 1245 N N . GLY A 1 155 ? 36.745 28.034 31.259 1.00 29.46 ? 155 GLY A N 1 ATOM 1246 C CA . GLY A 1 155 ? 37.396 29.184 31.821 1.00 30.51 ? 155 GLY A CA 1 ATOM 1247 C C . GLY A 1 155 ? 38.878 29.035 31.931 1.00 33.54 ? 155 GLY A C 1 ATOM 1248 O O . GLY A 1 155 ? 39.553 30.008 32.188 1.00 33.79 ? 155 GLY A O 1 ATOM 1249 N N . ASN A 1 156 ? 39.403 27.826 31.808 1.00 31.84 ? 156 ASN A N 1 ATOM 1250 C CA . ASN A 1 156 ? 40.854 27.684 31.804 1.00 28.56 ? 156 ASN A CA 1 ATOM 1251 C C . ASN A 1 156 ? 41.442 28.015 30.426 1.00 30.91 ? 156 ASN A C 1 ATOM 1252 O O . ASN A 1 156 ? 42.627 28.220 30.275 1.00 34.25 ? 156 ASN A O 1 ATOM 1253 C CB . ASN A 1 156 ? 41.264 26.257 32.203 1.00 37.91 ? 156 ASN A CB 1 ATOM 1254 C CG . ASN A 1 156 ? 41.043 25.998 33.686 1.00 41.23 ? 156 ASN A CG 1 ATOM 1255 O OD1 . ASN A 1 156 ? 41.078 26.925 34.508 1.00 43.69 ? 156 ASN A OD1 1 ATOM 1256 N ND2 . ASN A 1 156 ? 40.819 24.763 34.026 1.00 38.79 ? 156 ASN A ND2 1 ATOM 1257 N N . GLN A 1 157 ? 40.577 28.090 29.434 1.00 27.25 ? 157 GLN A N 1 ATOM 1258 C CA . GLN A 1 157 ? 40.976 28.291 28.063 1.00 30.92 ? 157 GLN A CA 1 ATOM 1259 C C . GLN A 1 157 ? 40.685 29.749 27.696 1.00 32.27 ? 157 GLN A C 1 ATOM 1260 O O . GLN A 1 157 ? 41.547 30.466 27.238 1.00 31.71 ? 157 GLN A O 1 ATOM 1261 C CB . GLN A 1 157 ? 40.164 27.365 27.217 1.00 33.07 ? 157 GLN A CB 1 ATOM 1262 C CG . GLN A 1 157 ? 40.552 25.886 27.378 1.00 37.69 ? 157 GLN A CG 1 ATOM 1263 C CD . GLN A 1 157 ? 39.532 24.956 26.773 1.00 42.36 ? 157 GLN A CD 1 ATOM 1264 O OE1 . GLN A 1 157 ? 38.330 25.244 26.738 1.00 33.82 ? 157 GLN A OE1 1 ATOM 1265 N NE2 . GLN A 1 157 ? 40.004 23.834 26.279 1.00 46.88 ? 157 GLN A NE2 1 ATOM 1266 N N . VAL A 1 158 ? 39.443 30.142 27.913 1.00 28.46 ? 158 VAL A N 1 ATOM 1267 C CA . VAL A 1 158 ? 39.009 31.535 27.729 1.00 28.38 ? 158 VAL A CA 1 ATOM 1268 C C . VAL A 1 158 ? 38.344 32.042 29.007 1.00 30.53 ? 158 VAL A C 1 ATOM 1269 O O . VAL A 1 158 ? 37.354 31.491 29.462 1.00 30.21 ? 158 VAL A O 1 ATOM 1270 C CB . VAL A 1 158 ? 38.065 31.665 26.540 1.00 32.64 ? 158 VAL A CB 1 ATOM 1271 C CG1 . VAL A 1 158 ? 37.514 33.092 26.420 1.00 34.30 ? 158 VAL A CG1 1 ATOM 1272 C CG2 . VAL A 1 158 ? 38.833 31.335 25.295 1.00 34.16 ? 158 VAL A CG2 1 ATOM 1273 N N . ASP A 1 159 ? 38.876 33.116 29.575 1.00 27.73 ? 159 ASP A N 1 ATOM 1274 C CA . ASP A 1 159 ? 38.266 33.696 30.762 1.00 28.32 ? 159 ASP A CA 1 ATOM 1275 C C . ASP A 1 159 ? 37.762 35.086 30.386 1.00 33.10 ? 159 ASP A C 1 ATOM 1276 O O . ASP A 1 159 ? 38.428 35.814 29.680 1.00 35.99 ? 159 ASP A O 1 ATOM 1277 C CB . ASP A 1 159 ? 39.259 33.750 31.901 1.00 27.32 ? 159 ASP A CB 1 ATOM 1278 C CG . ASP A 1 159 ? 38.589 34.006 33.262 1.00 32.99 ? 159 ASP A CG 1 ATOM 1279 O OD1 . ASP A 1 159 ? 37.333 33.941 33.358 1.00 35.75 ? 159 ASP A OD1 1 ATOM 1280 O OD2 . ASP A 1 159 ? 39.340 34.254 34.220 1.00 31.73 -1 159 ASP A OD2 1 ATOM 1281 N N . ILE A 1 160 ? 36.574 35.429 30.850 1.00 30.09 ? 160 ILE A N 1 ATOM 1282 C CA . ILE A 1 160 ? 35.905 36.628 30.405 1.00 29.82 ? 160 ILE A CA 1 ATOM 1283 C C . ILE A 1 160 ? 35.782 37.596 31.597 1.00 32.45 ? 160 ILE A C 1 ATOM 1284 O O . ILE A 1 160 ? 35.706 37.155 32.745 1.00 32.05 ? 160 ILE A O 1 ATOM 1285 C CB . ILE A 1 160 ? 34.534 36.275 29.791 1.00 35.70 ? 160 ILE A CB 1 ATOM 1286 C CG1 . ILE A 1 160 ? 33.834 37.510 29.234 1.00 40.09 ? 160 ILE A CG1 1 ATOM 1287 C CG2 . ILE A 1 160 ? 33.571 35.652 30.829 1.00 36.65 ? 160 ILE A CG2 1 ATOM 1288 C CD1 . ILE A 1 160 ? 32.678 37.152 28.298 1.00 37.62 ? 160 ILE A CD1 1 ATOM 1289 N N . PHE A 1 161 ? 35.795 38.904 31.312 1.00 31.71 ? 161 PHE A N 1 ATOM 1290 C CA . PHE A 1 161 ? 35.818 39.945 32.356 1.00 30.38 ? 161 PHE A CA 1 ATOM 1291 C C . PHE A 1 161 ? 35.019 41.118 31.884 1.00 30.40 ? 161 PHE A C 1 ATOM 1292 O O . PHE A 1 161 ? 34.974 41.420 30.695 1.00 34.23 ? 161 PHE A O 1 ATOM 1293 C CB . PHE A 1 161 ? 37.222 40.473 32.630 1.00 29.63 ? 161 PHE A CB 1 ATOM 1294 C CG . PHE A 1 161 ? 38.170 39.439 33.133 1.00 31.62 ? 161 PHE A CG 1 ATOM 1295 C CD1 . PHE A 1 161 ? 38.772 38.551 32.265 1.00 37.11 ? 161 PHE A CD1 1 ATOM 1296 C CD2 . PHE A 1 161 ? 38.454 39.354 34.484 1.00 30.77 ? 161 PHE A CD2 1 ATOM 1297 C CE1 . PHE A 1 161 ? 39.629 37.579 32.764 1.00 32.96 ? 161 PHE A CE1 1 ATOM 1298 C CE2 . PHE A 1 161 ? 39.300 38.413 34.961 1.00 38.66 ? 161 PHE A CE2 1 ATOM 1299 C CZ . PHE A 1 161 ? 39.899 37.526 34.099 1.00 35.77 ? 161 PHE A CZ 1 ATOM 1300 N N . ASN A 1 162 ? 34.388 41.796 32.815 1.00 28.47 ? 162 ASN A N 1 ATOM 1301 C CA . ASN A 1 162 ? 33.775 43.058 32.516 1.00 30.96 ? 162 ASN A CA 1 ATOM 1302 C C . ASN A 1 162 ? 34.790 44.175 32.320 1.00 30.65 ? 162 ASN A C 1 ATOM 1303 O O . ASN A 1 162 ? 35.662 44.365 33.155 1.00 33.48 ? 162 ASN A O 1 ATOM 1304 C CB . ASN A 1 162 ? 32.880 43.414 33.689 1.00 31.05 ? 162 ASN A CB 1 ATOM 1305 C CG . ASN A 1 162 ? 31.607 42.677 33.623 1.00 32.87 ? 162 ASN A CG 1 ATOM 1306 O OD1 . ASN A 1 162 ? 30.956 42.714 32.601 1.00 32.03 ? 162 ASN A OD1 1 ATOM 1307 N ND2 . ASN A 1 162 ? 31.269 41.944 34.657 1.00 33.30 ? 162 ASN A ND2 1 ATOM 1308 N N . ALA A 1 163 ? 34.640 44.931 31.231 1.00 38.44 ? 163 ALA A N 1 ATOM 1309 C CA . ALA A 1 163 ? 35.433 46.124 31.016 1.00 44.29 ? 163 ALA A CA 1 ATOM 1310 C C . ALA A 1 163 ? 34.937 47.227 31.932 1.00 39.91 ? 163 ALA A C 1 ATOM 1311 O O . ALA A 1 163 ? 35.692 48.102 32.291 1.00 37.51 ? 163 ALA A O 1 ATOM 1312 C CB . ALA A 1 163 ? 35.337 46.595 29.498 1.00 40.33 ? 163 ALA A CB 1 ATOM 1313 N N . LEU A 1 164 ? 33.649 47.215 32.253 1.00 30.21 ? 164 LEU A N 1 ATOM 1314 C CA . LEU A 1 164 ? 33.021 48.355 32.909 1.00 37.56 ? 164 LEU A CA 1 ATOM 1315 C C . LEU A 1 164 ? 32.221 47.843 34.091 1.00 38.24 ? 164 LEU A C 1 ATOM 1316 O O . LEU A 1 164 ? 31.949 46.682 34.169 1.00 35.07 ? 164 LEU A O 1 ATOM 1317 C CB . LEU A 1 164 ? 32.050 49.032 31.951 1.00 38.20 ? 164 LEU A CB 1 ATOM 1318 C CG . LEU A 1 164 ? 32.613 49.763 30.746 1.00 40.20 ? 164 LEU A CG 1 ATOM 1319 C CD1 . LEU A 1 164 ? 31.451 50.424 30.018 1.00 37.64 ? 164 LEU A CD1 1 ATOM 1320 C CD2 . LEU A 1 164 ? 33.615 50.791 31.181 1.00 41.40 ? 164 LEU A CD2 1 ATOM 1321 N N . ASP A 1 165 ? 31.781 48.701 34.984 1.00 35.15 ? 165 ASP A N 1 ATOM 1322 C CA . ASP A 1 165 ? 30.963 48.214 36.113 1.00 34.34 ? 165 ASP A CA 1 ATOM 1323 C C . ASP A 1 165 ? 29.533 47.913 35.688 1.00 41.30 ? 165 ASP A C 1 ATOM 1324 O O . ASP A 1 165 ? 28.761 47.223 36.377 1.00 33.82 ? 165 ASP A O 1 ATOM 1325 C CB . ASP A 1 165 ? 30.896 49.259 37.205 1.00 41.14 ? 165 ASP A CB 1 ATOM 1326 C CG . ASP A 1 165 ? 32.078 49.236 38.118 1.00 45.57 ? 165 ASP A CG 1 ATOM 1327 O OD1 . ASP A 1 165 ? 32.834 48.239 38.175 1.00 40.52 ? 165 ASP A OD1 1 ATOM 1328 O OD2 . ASP A 1 165 ? 32.224 50.241 38.812 1.00 49.52 -1 165 ASP A OD2 1 ATOM 1329 N N . SER A 1 166 ? 29.156 48.461 34.546 1.00 34.84 ? 166 SER A N 1 ATOM 1330 C CA A SER A 1 166 ? 27.784 48.390 34.079 0.39 35.41 ? 166 SER A CA 1 ATOM 1331 C CA B SER A 1 166 ? 27.791 48.372 34.085 0.61 33.80 ? 166 SER A CA 1 ATOM 1332 C C . SER A 1 166 ? 27.780 48.439 32.559 1.00 31.87 ? 166 SER A C 1 ATOM 1333 O O . SER A 1 166 ? 28.770 48.826 31.942 1.00 35.87 ? 166 SER A O 1 ATOM 1334 C CB A SER A 1 166 ? 26.971 49.582 34.604 0.39 43.26 ? 166 SER A CB 1 ATOM 1335 C CB B SER A 1 166 ? 26.974 49.538 34.651 0.61 44.91 ? 166 SER A CB 1 ATOM 1336 O OG A SER A 1 166 ? 26.948 49.639 36.019 0.39 37.85 ? 166 SER A OG 1 ATOM 1337 O OG B SER A 1 166 ? 27.561 50.782 34.300 0.61 48.36 ? 166 SER A OG 1 ATOM 1338 N N . GLY A 1 167 ? 26.662 48.075 31.965 1.00 32.00 ? 167 GLY A N 1 ATOM 1339 C CA . GLY A 1 167 ? 26.474 48.324 30.550 1.00 33.73 ? 167 GLY A CA 1 ATOM 1340 C C . GLY A 1 167 ? 26.516 49.812 30.308 1.00 44.60 ? 167 GLY A C 1 ATOM 1341 O O . GLY A 1 167 ? 26.154 50.595 31.189 1.00 39.36 ? 167 GLY A O 1 ATOM 1342 N N . ASP A 1 168 ? 26.952 50.201 29.109 1.00 38.93 ? 168 ASP A N 1 ATOM 1343 C CA . ASP A 1 168 ? 27.119 51.585 28.735 1.00 40.12 ? 168 ASP A CA 1 ATOM 1344 C C . ASP A 1 168 ? 25.786 52.126 28.274 1.00 44.34 ? 168 ASP A C 1 ATOM 1345 O O . ASP A 1 168 ? 25.248 51.702 27.252 1.00 43.19 ? 168 ASP A O 1 ATOM 1346 C CB . ASP A 1 168 ? 28.154 51.665 27.613 1.00 52.13 ? 168 ASP A CB 1 ATOM 1347 C CG . ASP A 1 168 ? 28.393 53.065 27.123 1.00 57.53 ? 168 ASP A CG 1 ATOM 1348 O OD1 . ASP A 1 168 ? 27.875 54.029 27.718 1.00 55.13 ? 168 ASP A OD1 1 ATOM 1349 O OD2 . ASP A 1 168 ? 29.136 53.194 26.132 1.00 74.58 -1 168 ASP A OD2 1 ATOM 1350 N N . LEU A 1 169 ? 25.251 53.066 29.034 1.00 42.63 ? 169 LEU A N 1 ATOM 1351 C CA . LEU A 1 169 ? 23.936 53.590 28.744 1.00 41.90 ? 169 LEU A CA 1 ATOM 1352 C C . LEU A 1 169 ? 24.043 55.020 28.272 1.00 49.40 ? 169 LEU A C 1 ATOM 1353 O O . LEU A 1 169 ? 23.057 55.739 28.268 1.00 43.15 ? 169 LEU A O 1 ATOM 1354 C CB . LEU A 1 169 ? 23.081 53.553 30.007 1.00 45.57 ? 169 LEU A CB 1 ATOM 1355 C CG . LEU A 1 169 ? 22.942 52.175 30.645 1.00 43.04 ? 169 LEU A CG 1 ATOM 1356 C CD1 . LEU A 1 169 ? 22.250 52.282 32.005 1.00 45.47 ? 169 LEU A CD1 1 ATOM 1357 C CD2 . LEU A 1 169 ? 22.167 51.266 29.724 1.00 45.06 ? 169 LEU A CD2 1 ATOM 1358 N N . SER A 1 170 ? 25.238 55.444 27.879 1.00 48.19 ? 170 SER A N 1 ATOM 1359 C CA . SER A 1 170 ? 25.412 56.856 27.499 1.00 57.37 ? 170 SER A CA 1 ATOM 1360 C C . SER A 1 170 ? 24.530 57.244 26.308 1.00 61.84 ? 170 SER A C 1 ATOM 1361 O O . SER A 1 170 ? 24.006 58.359 26.245 1.00 65.32 ? 170 SER A O 1 ATOM 1362 C CB . SER A 1 170 ? 26.885 57.160 27.193 1.00 58.38 ? 170 SER A CB 1 ATOM 1363 O OG . SER A 1 170 ? 27.362 56.416 26.079 1.00 57.78 ? 170 SER A OG 1 ATOM 1364 N N . ASP A 1 171 ? 24.350 56.330 25.364 1.00 64.50 ? 171 ASP A N 1 ATOM 1365 C CA . ASP A 1 171 ? 23.650 56.699 24.137 1.00 72.88 ? 171 ASP A CA 1 ATOM 1366 C C . ASP A 1 171 ? 22.786 55.580 23.585 1.00 57.85 ? 171 ASP A C 1 ATOM 1367 O O . ASP A 1 171 ? 23.272 54.708 22.893 1.00 65.33 ? 171 ASP A O 1 ATOM 1368 C CB . ASP A 1 171 ? 24.652 57.154 23.069 1.00 71.29 ? 171 ASP A CB 1 ATOM 1369 C CG . ASP A 1 171 ? 23.970 57.655 21.804 1.00 75.54 ? 171 ASP A CG 1 ATOM 1370 O OD1 . ASP A 1 171 ? 23.629 58.859 21.749 1.00 82.94 ? 171 ASP A OD1 1 ATOM 1371 O OD2 . ASP A 1 171 ? 23.770 56.838 20.881 1.00 74.05 -1 171 ASP A OD2 1 ATOM 1372 N N . PHE A 1 172 ? 21.492 55.627 23.879 1.00 51.30 ? 172 PHE A N 1 ATOM 1373 C CA . PHE A 1 172 ? 20.584 54.615 23.379 1.00 47.95 ? 172 PHE A CA 1 ATOM 1374 C C . PHE A 1 172 ? 19.257 55.263 23.076 1.00 47.17 ? 172 PHE A C 1 ATOM 1375 O O . PHE A 1 172 ? 18.896 56.258 23.694 1.00 53.91 ? 172 PHE A O 1 ATOM 1376 C CB . PHE A 1 172 ? 20.434 53.428 24.344 1.00 50.67 ? 172 PHE A CB 1 ATOM 1377 C CG . PHE A 1 172 ? 19.687 53.735 25.613 1.00 48.25 ? 172 PHE A CG 1 ATOM 1378 C CD1 . PHE A 1 172 ? 20.334 54.319 26.674 1.00 49.29 ? 172 PHE A CD1 1 ATOM 1379 C CD2 . PHE A 1 172 ? 18.349 53.406 25.761 1.00 54.63 ? 172 PHE A CD2 1 ATOM 1380 C CE1 . PHE A 1 172 ? 19.663 54.598 27.849 1.00 54.44 ? 172 PHE A CE1 1 ATOM 1381 C CE2 . PHE A 1 172 ? 17.666 53.695 26.960 1.00 39.50 ? 172 PHE A CE2 1 ATOM 1382 C CZ . PHE A 1 172 ? 18.326 54.292 27.978 1.00 51.11 ? 172 PHE A CZ 1 ATOM 1383 N N . ILE A 1 173 ? 18.541 54.687 22.120 1.00 66.43 ? 173 ILE A N 1 ATOM 1384 C CA . ILE A 1 173 ? 17.361 55.311 21.544 1.00 67.96 ? 173 ILE A CA 1 ATOM 1385 C C . ILE A 1 173 ? 16.211 55.540 22.522 1.00 75.11 ? 173 ILE A C 1 ATOM 1386 O O . ILE A 1 173 ? 15.445 56.480 22.356 1.00 98.10 ? 173 ILE A O 1 ATOM 1387 C CB . ILE A 1 173 ? 16.875 54.513 20.345 1.00 74.44 ? 173 ILE A CB 1 ATOM 1388 C CG1 . ILE A 1 173 ? 17.623 55.002 19.102 1.00 77.35 ? 173 ILE A CG1 1 ATOM 1389 C CG2 . ILE A 1 173 ? 15.360 54.654 20.176 1.00 75.83 ? 173 ILE A CG2 1 ATOM 1390 C CD1 . ILE A 1 173 ? 17.126 54.413 17.792 1.00 85.53 ? 173 ILE A CD1 1 ATOM 1391 N N A GLU A 1 174 ? 16.110 54.681 23.526 0.41 61.65 ? 174 GLU A N 1 ATOM 1392 N N B GLU A 1 174 ? 16.071 54.674 23.517 0.59 61.53 ? 174 GLU A N 1 ATOM 1393 C CA A GLU A 1 174 ? 15.094 54.798 24.570 0.41 61.66 ? 174 GLU A CA 1 ATOM 1394 C CA B GLU A 1 174 ? 15.091 54.873 24.591 0.59 61.33 ? 174 GLU A CA 1 ATOM 1395 C C A GLU A 1 174 ? 13.725 54.298 24.131 0.41 61.38 ? 174 GLU A C 1 ATOM 1396 C C B GLU A 1 174 ? 13.662 54.469 24.202 0.59 61.73 ? 174 GLU A C 1 ATOM 1397 O O A GLU A 1 174 ? 13.321 54.450 22.977 0.41 61.75 ? 174 GLU A O 1 ATOM 1398 O O B GLU A 1 174 ? 13.161 54.852 23.145 0.59 62.30 ? 174 GLU A O 1 ATOM 1399 C CB A GLU A 1 174 ? 14.972 56.230 25.088 0.41 61.48 ? 174 GLU A CB 1 ATOM 1400 C CB B GLU A 1 174 ? 15.106 56.321 25.074 0.59 60.73 ? 174 GLU A CB 1 ATOM 1401 C CG A GLU A 1 174 ? 16.116 56.661 25.974 0.41 63.47 ? 174 GLU A CG 1 ATOM 1402 C CG B GLU A 1 174 ? 14.483 56.512 26.445 0.59 66.81 ? 174 GLU A CG 1 ATOM 1403 C CD A GLU A 1 174 ? 15.689 57.701 26.988 0.41 67.71 ? 174 GLU A CD 1 ATOM 1404 C CD B GLU A 1 174 ? 15.288 57.446 27.346 0.59 68.32 ? 174 GLU A CD 1 ATOM 1405 O OE1 A GLU A 1 174 ? 14.591 58.273 26.816 0.41 69.18 ? 174 GLU A OE1 1 ATOM 1406 O OE1 B GLU A 1 174 ? 15.799 58.469 26.842 0.59 69.66 -1 174 GLU A OE1 1 ATOM 1407 O OE2 A GLU A 1 174 ? 16.443 57.931 27.959 0.41 66.67 -1 174 GLU A OE2 1 ATOM 1408 O OE2 B GLU A 1 174 ? 15.404 57.154 28.559 0.59 65.57 ? 174 GLU A OE2 1 ATOM 1409 N N . ASP A 1 175 ? 13.019 53.704 25.085 1.00 49.90 ? 175 ASP A N 1 ATOM 1410 C CA . ASP A 1 175 ? 11.700 53.134 24.848 1.00 48.46 ? 175 ASP A CA 1 ATOM 1411 C C . ASP A 1 175 ? 10.599 53.982 25.482 1.00 47.65 ? 175 ASP A C 1 ATOM 1412 O O . ASP A 1 175 ? 10.777 54.574 26.547 1.00 53.89 ? 175 ASP A O 1 ATOM 1413 C CB . ASP A 1 175 ? 11.646 51.740 25.458 1.00 46.31 ? 175 ASP A CB 1 ATOM 1414 C CG . ASP A 1 175 ? 10.329 51.046 25.215 1.00 54.08 ? 175 ASP A CG 1 ATOM 1415 O OD1 . ASP A 1 175 ? 10.194 50.423 24.146 1.00 65.39 ? 175 ASP A OD1 1 ATOM 1416 O OD2 . ASP A 1 175 ? 9.438 51.113 26.092 1.00 54.79 -1 175 ASP A OD2 1 ATOM 1417 N N . VAL A 1 176 ? 9.456 54.017 24.811 1.00 49.16 ? 176 VAL A N 1 ATOM 1418 C CA . VAL A 1 176 ? 8.331 54.834 25.218 1.00 46.17 ? 176 VAL A CA 1 ATOM 1419 C C . VAL A 1 176 ? 7.690 54.412 26.538 1.00 46.23 ? 176 VAL A C 1 ATOM 1420 O O . VAL A 1 176 ? 7.198 55.261 27.281 1.00 47.69 ? 176 VAL A O 1 ATOM 1421 C CB . VAL A 1 176 ? 7.219 54.796 24.172 1.00 50.33 ? 176 VAL A CB 1 ATOM 1422 C CG1 . VAL A 1 176 ? 6.008 55.579 24.657 1.00 58.30 ? 176 VAL A CG1 1 ATOM 1423 C CG2 . VAL A 1 176 ? 7.704 55.356 22.870 1.00 48.86 ? 176 VAL A CG2 1 ATOM 1424 N N . GLU A 1 177 ? 7.620 53.109 26.798 1.00 44.36 ? 177 GLU A N 1 ATOM 1425 C CA . GLU A 1 177 ? 6.904 52.593 27.979 1.00 44.20 ? 177 GLU A CA 1 ATOM 1426 C C . GLU A 1 177 ? 7.851 52.333 29.134 1.00 45.27 ? 177 GLU A C 1 ATOM 1427 O O . GLU A 1 177 ? 7.462 52.431 30.298 1.00 44.61 ? 177 GLU A O 1 ATOM 1428 C CB . GLU A 1 177 ? 6.185 51.276 27.663 1.00 52.67 ? 177 GLU A CB 1 ATOM 1429 C CG . GLU A 1 177 ? 4.826 51.433 27.005 1.00 61.08 ? 177 GLU A CG 1 ATOM 1430 C CD . GLU A 1 177 ? 3.719 51.679 27.999 1.00 68.32 ? 177 GLU A CD 1 ATOM 1431 O OE1 . GLU A 1 177 ? 3.972 51.599 29.223 1.00 71.68 ? 177 GLU A OE1 1 ATOM 1432 O OE2 . GLU A 1 177 ? 2.587 51.958 27.549 1.00 81.76 -1 177 GLU A OE2 1 ATOM 1433 N N . TRP A 1 178 ? 9.086 51.997 28.820 1.00 40.84 ? 178 TRP A N 1 ATOM 1434 C CA . TRP A 1 178 ? 10.045 51.615 29.857 1.00 39.15 ? 178 TRP A CA 1 ATOM 1435 C C . TRP A 1 178 ? 11.236 52.547 30.009 1.00 44.85 ? 178 TRP A C 1 ATOM 1436 O O . TRP A 1 178 ? 11.889 52.900 29.033 1.00 51.90 ? 178 TRP A O 1 ATOM 1437 C CB . TRP A 1 178 ? 10.553 50.176 29.577 1.00 40.00 ? 178 TRP A CB 1 ATOM 1438 C CG . TRP A 1 178 ? 9.427 49.209 29.570 1.00 45.69 ? 178 TRP A CG 1 ATOM 1439 C CD1 . TRP A 1 178 ? 8.778 48.712 28.488 1.00 49.61 ? 178 TRP A CD1 1 ATOM 1440 C CD2 . TRP A 1 178 ? 8.795 48.634 30.719 1.00 37.66 ? 178 TRP A CD2 1 ATOM 1441 N NE1 . TRP A 1 178 ? 7.767 47.871 28.886 1.00 49.22 ? 178 TRP A NE1 1 ATOM 1442 C CE2 . TRP A 1 178 ? 7.754 47.810 30.254 1.00 45.96 ? 178 TRP A CE2 1 ATOM 1443 C CE3 . TRP A 1 178 ? 8.990 48.763 32.094 1.00 39.64 ? 178 TRP A CE3 1 ATOM 1444 C CZ2 . TRP A 1 178 ? 6.925 47.102 31.108 1.00 46.42 ? 178 TRP A CZ2 1 ATOM 1445 C CZ3 . TRP A 1 178 ? 8.165 48.065 32.941 1.00 41.84 ? 178 TRP A CZ3 1 ATOM 1446 C CH2 . TRP A 1 178 ? 7.153 47.234 32.448 1.00 43.81 ? 178 TRP A CH2 1 ATOM 1447 N N . GLU A 1 179 ? 11.527 52.937 31.245 1.00 43.92 ? 179 GLU A N 1 ATOM 1448 C CA . GLU A 1 179 ? 12.751 53.677 31.545 1.00 41.67 ? 179 GLU A CA 1 ATOM 1449 C C . GLU A 1 179 ? 13.796 52.717 32.025 1.00 43.09 ? 179 GLU A C 1 ATOM 1450 O O . GLU A 1 179 ? 13.473 51.765 32.730 1.00 44.83 ? 179 GLU A O 1 ATOM 1451 C CB . GLU A 1 179 ? 12.525 54.684 32.664 1.00 51.06 ? 179 GLU A CB 1 ATOM 1452 C CG . GLU A 1 179 ? 12.245 56.070 32.218 1.00 59.76 ? 179 GLU A CG 1 ATOM 1453 C CD . GLU A 1 179 ? 12.285 57.037 33.380 1.00 66.32 ? 179 GLU A CD 1 ATOM 1454 O OE1 . GLU A 1 179 ? 11.279 57.112 34.120 1.00 69.63 -1 179 GLU A OE1 1 ATOM 1455 O OE2 . GLU A 1 179 ? 13.329 57.704 33.555 1.00 68.37 ? 179 GLU A OE2 1 ATOM 1456 N N . VAL A 1 180 ? 15.055 52.967 31.677 1.00 44.89 ? 180 VAL A N 1 ATOM 1457 C CA . VAL A 1 180 ? 16.162 52.178 32.227 1.00 35.78 ? 180 VAL A CA 1 ATOM 1458 C C . VAL A 1 180 ? 16.626 52.750 33.567 1.00 43.85 ? 180 VAL A C 1 ATOM 1459 O O . VAL A 1 180 ? 16.996 53.937 33.701 1.00 43.50 ? 180 VAL A O 1 ATOM 1460 C CB . VAL A 1 180 ? 17.345 52.159 31.255 1.00 43.65 ? 180 VAL A CB 1 ATOM 1461 C CG1 . VAL A 1 180 ? 18.572 51.460 31.903 1.00 43.67 ? 180 VAL A CG1 1 ATOM 1462 C CG2 . VAL A 1 180 ? 16.942 51.507 29.971 1.00 43.93 ? 180 VAL A CG2 1 ATOM 1463 N N . HIS A 1 181 ? 16.607 51.905 34.577 1.00 43.75 ? 181 HIS A N 1 ATOM 1464 C CA . HIS A 1 181 ? 16.994 52.323 35.919 1.00 47.83 ? 181 HIS A CA 1 ATOM 1465 C C . HIS A 1 181 ? 18.470 51.994 36.173 1.00 49.93 ? 181 HIS A C 1 ATOM 1466 O O . HIS A 1 181 ? 19.175 52.700 36.878 1.00 48.52 ? 181 HIS A O 1 ATOM 1467 C CB . HIS A 1 181 ? 16.079 51.626 36.916 1.00 50.97 ? 181 HIS A CB 1 ATOM 1468 C CG . HIS A 1 181 ? 16.410 51.886 38.350 1.00 61.72 ? 181 HIS A CG 1 ATOM 1469 N ND1 . HIS A 1 181 ? 16.496 53.155 38.884 1.00 78.97 ? 181 HIS A ND1 1 ATOM 1470 C CD2 . HIS A 1 181 ? 16.644 51.031 39.375 1.00 67.37 ? 181 HIS A CD2 1 ATOM 1471 C CE1 . HIS A 1 181 ? 16.789 53.071 40.171 1.00 79.65 ? 181 HIS A CE1 1 ATOM 1472 N NE2 . HIS A 1 181 ? 16.879 51.793 40.495 1.00 77.17 ? 181 HIS A NE2 1 ATOM 1473 N N . GLY A 1 182 ? 18.960 50.926 35.576 1.00 45.06 ? 182 GLY A N 1 ATOM 1474 C CA . GLY A 1 182 ? 20.379 50.630 35.656 1.00 45.69 ? 182 GLY A CA 1 ATOM 1475 C C . GLY A 1 182 ? 20.687 49.413 34.817 1.00 41.06 ? 182 GLY A C 1 ATOM 1476 O O . GLY A 1 182 ? 19.758 48.803 34.272 1.00 37.77 ? 182 GLY A O 1 ATOM 1477 N N . MET A 1 183 ? 21.968 49.074 34.700 1.00 32.47 ? 183 MET A N 1 ATOM 1478 C CA . MET A 1 183 ? 22.402 47.868 34.015 1.00 31.11 ? 183 MET A CA 1 ATOM 1479 C C . MET A 1 183 ? 23.712 47.360 34.624 1.00 33.61 ? 183 MET A C 1 ATOM 1480 O O . MET A 1 183 ? 24.764 47.305 33.964 1.00 31.11 ? 183 MET A O 1 ATOM 1481 C CB . MET A 1 183 ? 22.613 48.153 32.526 1.00 40.33 ? 183 MET A CB 1 ATOM 1482 C CG . MET A 1 183 ? 22.719 46.927 31.647 1.00 38.29 ? 183 MET A CG 1 ATOM 1483 S SD . MET A 1 183 ? 22.774 47.413 29.899 1.00 38.81 ? 183 MET A SD 1 ATOM 1484 C CE . MET A 1 183 ? 22.843 45.828 29.077 1.00 39.18 ? 183 MET A CE 1 ATOM 1485 N N . PRO A 1 184 ? 23.678 47.014 35.905 1.00 35.08 ? 184 PRO A N 1 ATOM 1486 C CA . PRO A 1 184 ? 24.946 46.636 36.541 1.00 27.22 ? 184 PRO A CA 1 ATOM 1487 C C . PRO A 1 184 ? 25.446 45.305 36.031 1.00 32.59 ? 184 PRO A C 1 ATOM 1488 O O . PRO A 1 184 ? 24.660 44.466 35.601 1.00 35.70 ? 184 PRO A O 1 ATOM 1489 C CB . PRO A 1 184 ? 24.559 46.515 38.020 1.00 32.05 ? 184 PRO A CB 1 ATOM 1490 C CG . PRO A 1 184 ? 23.099 46.143 37.974 1.00 39.50 ? 184 PRO A CG 1 ATOM 1491 C CD . PRO A 1 184 ? 22.569 47.025 36.872 1.00 39.27 ? 184 PRO A CD 1 ATOM 1492 N N . ALA A 1 185 ? 26.763 45.126 36.049 1.00 33.97 ? 185 ALA A N 1 ATOM 1493 C CA . ALA A 1 185 ? 27.361 43.928 35.505 1.00 27.59 ? 185 ALA A CA 1 ATOM 1494 C C . ALA A 1 185 ? 28.047 43.142 36.621 1.00 31.51 ? 185 ALA A C 1 ATOM 1495 O O . ALA A 1 185 ? 28.549 43.719 37.569 1.00 31.09 ? 185 ALA A O 1 ATOM 1496 C CB . ALA A 1 185 ? 28.378 44.297 34.411 1.00 30.66 ? 185 ALA A CB 1 ATOM 1497 N N . VAL A 1 186 ? 28.043 41.820 36.483 1.00 30.09 ? 186 VAL A N 1 ATOM 1498 C CA . VAL A 1 186 ? 28.809 40.984 37.365 1.00 30.44 ? 186 VAL A CA 1 ATOM 1499 C C . VAL A 1 186 ? 29.451 39.898 36.541 1.00 31.45 ? 186 VAL A C 1 ATOM 1500 O O . VAL A 1 186 ? 29.119 39.678 35.369 1.00 33.37 ? 186 VAL A O 1 ATOM 1501 C CB . VAL A 1 186 ? 27.918 40.310 38.455 1.00 31.39 ? 186 VAL A CB 1 ATOM 1502 C CG1 . VAL A 1 186 ? 27.050 41.309 39.201 1.00 27.83 ? 186 VAL A CG1 1 ATOM 1503 C CG2 . VAL A 1 186 ? 27.053 39.234 37.807 1.00 37.08 ? 186 VAL A CG2 1 ATOM 1504 N N . LYS A 1 187 ? 30.399 39.217 37.156 1.00 30.04 ? 187 LYS A N 1 ATOM 1505 C CA . LYS A 1 187 ? 30.975 38.032 36.581 1.00 28.09 ? 187 LYS A CA 1 ATOM 1506 C C . LYS A 1 187 ? 30.658 36.866 37.499 1.00 25.50 ? 187 LYS A C 1 ATOM 1507 O O . LYS A 1 187 ? 30.802 36.986 38.702 1.00 29.04 ? 187 LYS A O 1 ATOM 1508 C CB . LYS A 1 187 ? 32.470 38.197 36.491 1.00 31.53 ? 187 LYS A CB 1 ATOM 1509 C CG . LYS A 1 187 ? 33.132 36.938 36.043 1.00 29.95 ? 187 LYS A CG 1 ATOM 1510 C CD . LYS A 1 187 ? 34.632 37.118 35.821 1.00 29.72 ? 187 LYS A CD 1 ATOM 1511 C CE . LYS A 1 187 ? 35.311 35.813 35.340 1.00 28.41 ? 187 LYS A CE 1 ATOM 1512 N NZ . LYS A 1 187 ? 36.748 36.098 35.145 1.00 31.76 1 187 LYS A NZ 1 ATOM 1513 N N . ASN A 1 188 ? 30.192 35.764 36.906 1.00 29.74 ? 188 ASN A N 1 ATOM 1514 C CA . ASN A 1 188 ? 29.920 34.518 37.639 1.00 29.36 ? 188 ASN A CA 1 ATOM 1515 C C . ASN A 1 188 ? 30.786 33.417 37.115 1.00 32.50 ? 188 ASN A C 1 ATOM 1516 O O . ASN A 1 188 ? 30.847 33.202 35.907 1.00 31.73 ? 188 ASN A O 1 ATOM 1517 C CB . ASN A 1 188 ? 28.489 34.057 37.390 1.00 32.38 ? 188 ASN A CB 1 ATOM 1518 C CG . ASN A 1 188 ? 27.467 35.063 37.861 1.00 31.89 ? 188 ASN A CG 1 ATOM 1519 O OD1 . ASN A 1 188 ? 27.326 35.279 39.051 1.00 32.37 ? 188 ASN A OD1 1 ATOM 1520 N ND2 . ASN A 1 188 ? 26.789 35.703 36.925 1.00 33.34 ? 188 ASN A ND2 1 ATOM 1521 N N . VAL A 1 189 ? 31.389 32.667 38.019 1.00 29.67 ? 189 VAL A N 1 ATOM 1522 C CA . VAL A 1 189 ? 32.141 31.496 37.624 1.00 23.36 ? 189 VAL A CA 1 ATOM 1523 C C . VAL A 1 189 ? 31.619 30.296 38.365 1.00 26.97 ? 189 VAL A C 1 ATOM 1524 O O . VAL A 1 189 ? 31.643 30.287 39.573 1.00 28.61 ? 189 VAL A O 1 ATOM 1525 C CB . VAL A 1 189 ? 33.595 31.655 37.982 1.00 29.13 ? 189 VAL A CB 1 ATOM 1526 C CG1 . VAL A 1 189 ? 34.386 30.414 37.566 1.00 30.15 ? 189 VAL A CG1 1 ATOM 1527 C CG2 . VAL A 1 189 ? 34.182 32.917 37.331 1.00 28.71 ? 189 VAL A CG2 1 ATOM 1528 N N . ILE A 1 190 ? 31.226 29.266 37.633 1.00 28.06 ? 190 ILE A N 1 ATOM 1529 C CA . ILE A 1 190 ? 30.661 28.080 38.248 1.00 28.13 ? 190 ILE A CA 1 ATOM 1530 C C . ILE A 1 190 ? 31.593 26.917 37.952 1.00 31.18 ? 190 ILE A C 1 ATOM 1531 O O . ILE A 1 190 ? 32.177 26.847 36.860 1.00 31.40 ? 190 ILE A O 1 ATOM 1532 C CB . ILE A 1 190 ? 29.217 27.788 37.750 1.00 36.00 ? 190 ILE A CB 1 ATOM 1533 C CG1 . ILE A 1 190 ? 28.609 26.691 38.636 1.00 35.36 ? 190 ILE A CG1 1 ATOM 1534 C CG2 . ILE A 1 190 ? 29.199 27.429 36.224 1.00 29.34 ? 190 ILE A CG2 1 ATOM 1535 C CD1 . ILE A 1 190 ? 27.162 26.402 38.423 1.00 35.28 ? 190 ILE A CD1 1 ATOM 1536 N N . SER A 1 191 ? 31.792 26.074 38.958 1.00 28.35 ? 191 SER A N 1 ATOM 1537 C CA . SER A 1 191 ? 32.506 24.816 38.780 1.00 26.67 ? 191 SER A CA 1 ATOM 1538 C C . SER A 1 191 ? 31.701 23.717 39.469 1.00 33.33 ? 191 SER A C 1 ATOM 1539 O O . SER A 1 191 ? 31.035 23.944 40.495 1.00 35.61 ? 191 SER A O 1 ATOM 1540 C CB . SER A 1 191 ? 33.909 24.938 39.353 1.00 36.61 ? 191 SER A CB 1 ATOM 1541 O OG . SER A 1 191 ? 33.847 25.198 40.715 1.00 45.15 ? 191 SER A OG 1 ATOM 1542 N N . TYR A 1 192 ? 31.781 22.519 38.903 1.00 31.41 ? 192 TYR A N 1 ATOM 1543 C CA . TYR A 1 192 ? 30.876 21.454 39.283 1.00 27.69 ? 192 TYR A CA 1 ATOM 1544 C C . TYR A 1 192 ? 31.602 20.414 40.100 1.00 29.79 ? 192 TYR A C 1 ATOM 1545 O O . TYR A 1 192 ? 32.652 19.951 39.700 1.00 32.57 ? 192 TYR A O 1 ATOM 1546 C CB . TYR A 1 192 ? 30.264 20.805 38.028 1.00 33.61 ? 192 TYR A CB 1 ATOM 1547 C CG . TYR A 1 192 ? 29.459 21.800 37.226 1.00 30.38 ? 192 TYR A CG 1 ATOM 1548 C CD1 . TYR A 1 192 ? 30.063 22.606 36.272 1.00 36.42 ? 192 TYR A CD1 1 ATOM 1549 C CD2 . TYR A 1 192 ? 28.119 21.982 37.480 1.00 38.30 ? 192 TYR A CD2 1 ATOM 1550 C CE1 . TYR A 1 192 ? 29.343 23.558 35.579 1.00 32.30 ? 192 TYR A CE1 1 ATOM 1551 C CE2 . TYR A 1 192 ? 27.391 22.939 36.799 1.00 38.79 ? 192 TYR A CE2 1 ATOM 1552 C CZ . TYR A 1 192 ? 27.992 23.694 35.831 1.00 35.22 ? 192 TYR A CZ 1 ATOM 1553 O OH . TYR A 1 192 ? 27.253 24.641 35.183 1.00 35.41 ? 192 TYR A OH 1 ATOM 1554 N N . GLY A 1 193 ? 31.016 20.022 41.224 1.00 33.15 ? 193 GLY A N 1 ATOM 1555 C CA . GLY A 1 193 ? 31.568 19.012 42.084 1.00 37.97 ? 193 GLY A CA 1 ATOM 1556 C C . GLY A 1 193 ? 32.887 19.430 42.696 1.00 37.17 ? 193 GLY A C 1 ATOM 1557 O O . GLY A 1 193 ? 33.165 20.607 42.896 1.00 39.94 ? 193 GLY A O 1 ATOM 1558 N N . CYS A 1 194 ? 33.726 18.453 42.993 1.00 36.73 ? 194 CYS A N 1 ATOM 1559 C CA . CYS A 1 194 ? 34.925 18.768 43.722 1.00 45.57 ? 194 CYS A CA 1 ATOM 1560 C C . CYS A 1 194 ? 35.921 19.424 42.797 1.00 51.87 ? 194 CYS A C 1 ATOM 1561 O O . CYS A 1 194 ? 36.681 20.285 43.216 1.00 55.34 ? 194 CYS A O 1 ATOM 1562 C CB . CYS A 1 194 ? 35.533 17.512 44.345 1.00 47.84 ? 194 CYS A CB 1 ATOM 1563 S SG . CYS A 1 194 ? 36.338 16.447 43.204 1.00 64.67 ? 194 CYS A SG 1 ATOM 1564 N N . CYS A 1 195 ? 35.919 19.049 41.523 1.00 45.45 ? 195 CYS A N 1 ATOM 1565 C CA . CYS A 1 195 ? 37.127 19.305 40.761 1.00 43.18 ? 195 CYS A CA 1 ATOM 1566 C C . CYS A 1 195 ? 37.022 19.801 39.301 1.00 47.48 ? 195 CYS A C 1 ATOM 1567 O O . CYS A 1 195 ? 38.041 19.899 38.638 1.00 52.97 ? 195 CYS A O 1 ATOM 1568 C CB . CYS A 1 195 ? 37.937 18.025 40.850 1.00 49.55 ? 195 CYS A CB 1 ATOM 1569 S SG . CYS A 1 195 ? 38.090 17.430 42.633 1.00 79.93 ? 195 CYS A SG 1 ATOM 1570 N N . SER A 1 196 ? 35.830 20.112 38.803 1.00 37.94 ? 196 SER A N 1 ATOM 1571 C CA . SER A 1 196 ? 35.686 20.530 37.396 1.00 33.53 ? 196 SER A CA 1 ATOM 1572 C C . SER A 1 196 ? 36.460 21.784 37.021 1.00 37.26 ? 196 SER A C 1 ATOM 1573 O O . SER A 1 196 ? 36.969 22.519 37.841 1.00 38.01 ? 196 SER A O 1 ATOM 1574 C CB . SER A 1 196 ? 34.203 20.686 36.977 1.00 38.59 ? 196 SER A CB 1 ATOM 1575 O OG . SER A 1 196 ? 33.682 22.029 36.985 1.00 36.22 ? 196 SER A OG 1 ATOM 1576 N N . GLU A 1 197 ? 36.522 22.002 35.716 1.00 30.13 ? 197 GLU A N 1 ATOM 1577 C CA . GLU A 1 197 ? 37.048 23.200 35.141 1.00 27.60 ? 197 GLU A CA 1 ATOM 1578 C C . GLU A 1 197 ? 36.027 24.257 35.506 1.00 28.81 ? 197 GLU A C 1 ATOM 1579 O O . GLU A 1 197 ? 34.878 23.925 35.761 1.00 32.54 ? 197 GLU A O 1 ATOM 1580 C CB . GLU A 1 197 ? 37.091 22.987 33.611 1.00 30.48 ? 197 GLU A CB 1 ATOM 1581 C CG . GLU A 1 197 ? 37.597 21.578 33.168 1.00 54.76 ? 197 GLU A CG 1 ATOM 1582 C CD . GLU A 1 197 ? 36.614 20.393 33.412 1.00 44.88 ? 197 GLU A CD 1 ATOM 1583 O OE1 . GLU A 1 197 ? 35.368 20.528 33.235 1.00 43.15 ? 197 GLU A OE1 1 ATOM 1584 O OE2 . GLU A 1 197 ? 37.109 19.309 33.787 1.00 69.40 -1 197 GLU A OE2 1 ATOM 1585 N N . PRO A 1 198 ? 36.438 25.530 35.551 1.00 28.35 ? 198 PRO A N 1 ATOM 1586 C CA . PRO A 1 198 ? 35.516 26.644 35.750 1.00 28.94 ? 198 PRO A CA 1 ATOM 1587 C C . PRO A 1 198 ? 34.805 27.080 34.477 1.00 33.04 ? 198 PRO A C 1 ATOM 1588 O O . PRO A 1 198 ? 35.352 26.942 33.375 1.00 28.89 ? 198 PRO A O 1 ATOM 1589 C CB . PRO A 1 198 ? 36.446 27.769 36.207 1.00 31.85 ? 198 PRO A CB 1 ATOM 1590 C CG . PRO A 1 198 ? 37.651 27.536 35.501 1.00 32.22 ? 198 PRO A CG 1 ATOM 1591 C CD . PRO A 1 198 ? 37.823 26.010 35.440 1.00 33.12 ? 198 PRO A CD 1 ATOM 1592 N N . TYR A 1 199 ? 33.622 27.662 34.657 1.00 30.01 ? 199 TYR A N 1 ATOM 1593 C CA . TYR A 1 199 ? 32.782 28.130 33.546 1.00 26.63 ? 199 TYR A CA 1 ATOM 1594 C C . TYR A 1 199 ? 32.292 29.526 33.860 1.00 29.09 ? 199 TYR A C 1 ATOM 1595 O O . TYR A 1 199 ? 31.424 29.711 34.689 1.00 31.47 ? 199 TYR A O 1 ATOM 1596 C CB . TYR A 1 199 ? 31.584 27.237 33.339 1.00 28.44 ? 199 TYR A CB 1 ATOM 1597 C CG . TYR A 1 199 ? 31.992 25.939 32.774 1.00 30.88 ? 199 TYR A CG 1 ATOM 1598 C CD1 . TYR A 1 199 ? 32.095 25.769 31.384 1.00 30.40 ? 199 TYR A CD1 1 ATOM 1599 C CD2 . TYR A 1 199 ? 32.333 24.885 33.601 1.00 30.63 ? 199 TYR A CD2 1 ATOM 1600 C CE1 . TYR A 1 199 ? 32.488 24.576 30.859 1.00 36.67 ? 199 TYR A CE1 1 ATOM 1601 C CE2 . TYR A 1 199 ? 32.735 23.647 33.072 1.00 34.47 ? 199 TYR A CE2 1 ATOM 1602 C CZ . TYR A 1 199 ? 32.809 23.528 31.686 1.00 41.11 ? 199 TYR A CZ 1 ATOM 1603 O OH . TYR A 1 199 ? 33.212 22.369 31.112 1.00 45.79 ? 199 TYR A OH 1 ATOM 1604 N N . PRO A 1 200 ? 32.921 30.525 33.250 1.00 27.96 ? 200 PRO A N 1 ATOM 1605 C CA . PRO A 1 200 ? 32.606 31.916 33.587 1.00 26.02 ? 200 PRO A CA 1 ATOM 1606 C C . PRO A 1 200 ? 31.599 32.530 32.660 1.00 34.66 ? 200 PRO A C 1 ATOM 1607 O O . PRO A 1 200 ? 31.481 32.134 31.502 1.00 33.67 ? 200 PRO A O 1 ATOM 1608 C CB . PRO A 1 200 ? 33.954 32.619 33.390 1.00 28.70 ? 200 PRO A CB 1 ATOM 1609 C CG . PRO A 1 200 ? 34.523 31.865 32.159 1.00 29.36 ? 200 PRO A CG 1 ATOM 1610 C CD . PRO A 1 200 ? 34.111 30.417 32.385 1.00 29.42 ? 200 PRO A CD 1 ATOM 1611 N N . ASP A 1 201 ? 30.887 33.537 33.160 1.00 31.76 ? 201 ASP A N 1 ATOM 1612 C CA . ASP A 1 201 ? 30.009 34.303 32.288 1.00 31.30 ? 201 ASP A CA 1 ATOM 1613 C C . ASP A 1 201 ? 30.054 35.689 32.825 1.00 31.71 ? 201 ASP A C 1 ATOM 1614 O O . ASP A 1 201 ? 30.477 35.885 33.951 1.00 26.94 ? 201 ASP A O 1 ATOM 1615 C CB . ASP A 1 201 ? 28.579 33.739 32.268 1.00 33.64 ? 201 ASP A CB 1 ATOM 1616 C CG . ASP A 1 201 ? 27.787 33.971 33.593 1.00 36.81 ? 201 ASP A CG 1 ATOM 1617 O OD1 . ASP A 1 201 ? 27.580 35.152 34.056 1.00 33.15 -1 201 ASP A OD1 1 ATOM 1618 O OD2 . ASP A 1 201 ? 27.288 32.962 34.166 1.00 39.27 ? 201 ASP A OD2 1 ATOM 1619 N N . VAL A 1 202 ? 29.605 36.667 32.047 1.00 27.98 ? 202 VAL A N 1 ATOM 1620 C CA . VAL A 1 202 ? 29.278 37.940 32.600 1.00 30.18 ? 202 VAL A CA 1 ATOM 1621 C C . VAL A 1 202 ? 27.808 38.170 32.437 1.00 33.85 ? 202 VAL A C 1 ATOM 1622 O O . VAL A 1 202 ? 27.241 37.839 31.413 1.00 33.30 ? 202 VAL A O 1 ATOM 1623 C CB . VAL A 1 202 ? 30.086 39.149 31.985 1.00 36.41 ? 202 VAL A CB 1 ATOM 1624 C CG1 . VAL A 1 202 ? 31.533 39.046 32.367 1.00 31.84 ? 202 VAL A CG1 1 ATOM 1625 C CG2 . VAL A 1 202 ? 29.937 39.223 30.507 1.00 33.68 ? 202 VAL A CG2 1 ATOM 1626 N N . THR A 1 203 ? 27.188 38.755 33.455 1.00 34.66 ? 203 THR A N 1 ATOM 1627 C CA . THR A 1 203 ? 25.767 38.995 33.392 1.00 28.53 ? 203 THR A CA 1 ATOM 1628 C C . THR A 1 203 ? 25.512 40.469 33.640 1.00 32.57 ? 203 THR A C 1 ATOM 1629 O O . THR A 1 203 ? 26.057 41.069 34.573 1.00 31.25 ? 203 THR A O 1 ATOM 1630 C CB . THR A 1 203 ? 25.010 38.105 34.413 1.00 35.46 ? 203 THR A CB 1 ATOM 1631 O OG1 . THR A 1 203 ? 25.133 36.733 34.011 1.00 33.33 ? 203 THR A OG1 1 ATOM 1632 C CG2 . THR A 1 203 ? 23.544 38.433 34.468 1.00 30.28 ? 203 THR A CG2 1 ATOM 1633 N N . PHE A 1 204 ? 24.684 41.035 32.775 1.00 32.18 ? 204 PHE A N 1 ATOM 1634 C CA . PHE A 1 204 ? 24.167 42.402 32.914 1.00 32.08 ? 204 PHE A CA 1 ATOM 1635 C C . PHE A 1 204 ? 22.721 42.282 33.364 1.00 31.84 ? 204 PHE A C 1 ATOM 1636 O O . PHE A 1 204 ? 21.941 41.515 32.795 1.00 34.37 ? 204 PHE A O 1 ATOM 1637 C CB . PHE A 1 204 ? 24.265 43.132 31.561 1.00 32.97 ? 204 PHE A CB 1 ATOM 1638 C CG . PHE A 1 204 ? 25.663 43.307 31.110 1.00 32.90 ? 204 PHE A CG 1 ATOM 1639 C CD1 . PHE A 1 204 ? 26.349 42.250 30.496 1.00 32.00 ? 204 PHE A CD1 1 ATOM 1640 C CD2 . PHE A 1 204 ? 26.327 44.496 31.336 1.00 34.84 ? 204 PHE A CD2 1 ATOM 1641 C CE1 . PHE A 1 204 ? 27.675 42.396 30.135 1.00 35.82 ? 204 PHE A CE1 1 ATOM 1642 C CE2 . PHE A 1 204 ? 27.642 44.649 30.976 1.00 35.16 ? 204 PHE A CE2 1 ATOM 1643 C CZ . PHE A 1 204 ? 28.327 43.593 30.388 1.00 35.08 ? 204 PHE A CZ 1 ATOM 1644 N N . THR A 1 205 ? 22.341 43.008 34.408 1.00 34.69 ? 205 THR A N 1 ATOM 1645 C CA . THR A 1 205 ? 20.959 43.017 34.798 1.00 31.94 ? 205 THR A CA 1 ATOM 1646 C C . THR A 1 205 ? 20.365 44.353 34.377 1.00 33.84 ? 205 THR A C 1 ATOM 1647 O O . THR A 1 205 ? 20.566 45.338 35.032 1.00 38.74 ? 205 THR A O 1 ATOM 1648 C CB . THR A 1 205 ? 20.806 42.843 36.333 1.00 39.68 ? 205 THR A CB 1 ATOM 1649 O OG1 . THR A 1 205 ? 21.393 41.596 36.746 1.00 38.63 ? 205 THR A OG1 1 ATOM 1650 C CG2 . THR A 1 205 ? 19.340 42.865 36.735 1.00 44.24 ? 205 THR A CG2 1 ATOM 1651 N N . LEU A 1 206 ? 19.653 44.365 33.285 1.00 33.71 ? 206 LEU A N 1 ATOM 1652 C CA . LEU A 1 206 ? 18.957 45.558 32.875 1.00 36.06 ? 206 LEU A CA 1 ATOM 1653 C C . LEU A 1 206 ? 17.688 45.688 33.718 1.00 36.17 ? 206 LEU A C 1 ATOM 1654 O O . LEU A 1 206 ? 16.809 44.814 33.696 1.00 44.37 ? 206 LEU A O 1 ATOM 1655 C CB . LEU A 1 206 ? 18.618 45.449 31.416 1.00 37.12 ? 206 LEU A CB 1 ATOM 1656 C CG . LEU A 1 206 ? 18.070 46.665 30.721 1.00 45.52 ? 206 LEU A CG 1 ATOM 1657 C CD1 . LEU A 1 206 ? 19.114 47.778 30.612 1.00 43.05 ? 206 LEU A CD1 1 ATOM 1658 C CD2 . LEU A 1 206 ? 17.582 46.196 29.352 1.00 50.97 ? 206 LEU A CD2 1 ATOM 1659 N N . LEU A 1 207 ? 17.615 46.785 34.438 1.00 38.98 ? 207 LEU A N 1 ATOM 1660 C CA . LEU A 1 207 ? 16.500 47.106 35.293 1.00 40.11 ? 207 LEU A CA 1 ATOM 1661 C C . LEU A 1 207 ? 15.631 48.136 34.612 1.00 38.60 ? 207 LEU A C 1 ATOM 1662 O O . LEU A 1 207 ? 16.075 49.280 34.390 1.00 37.76 ? 207 LEU A O 1 ATOM 1663 C CB . LEU A 1 207 ? 17.043 47.681 36.591 1.00 36.11 ? 207 LEU A CB 1 ATOM 1664 C CG . LEU A 1 207 ? 18.020 46.738 37.311 1.00 43.23 ? 207 LEU A CG 1 ATOM 1665 C CD1 . LEU A 1 207 ? 18.800 47.478 38.387 1.00 50.88 ? 207 LEU A CD1 1 ATOM 1666 C CD2 . LEU A 1 207 ? 17.290 45.530 37.913 1.00 44.36 ? 207 LEU A CD2 1 ATOM 1667 N N . LEU A 1 208 ? 14.411 47.729 34.249 1.00 38.63 ? 208 LEU A N 1 ATOM 1668 C CA . LEU A 1 208 ? 13.442 48.634 33.616 1.00 38.93 ? 208 LEU A CA 1 ATOM 1669 C C . LEU A 1 208 ? 12.308 48.956 34.566 1.00 39.91 ? 208 LEU A C 1 ATOM 1670 O O . LEU A 1 208 ? 11.858 48.097 35.322 1.00 43.21 ? 208 LEU A O 1 ATOM 1671 C CB . LEU A 1 208 ? 12.846 47.981 32.382 1.00 38.42 ? 208 LEU A CB 1 ATOM 1672 C CG . LEU A 1 208 ? 13.847 47.403 31.406 1.00 36.86 ? 208 LEU A CG 1 ATOM 1673 C CD1 . LEU A 1 208 ? 13.056 46.810 30.235 1.00 41.51 ? 208 LEU A CD1 1 ATOM 1674 C CD2 . LEU A 1 208 ? 14.818 48.472 30.973 1.00 43.27 ? 208 LEU A CD2 1 ATOM 1675 N N . LYS A 1 209 ? 11.819 50.186 34.492 1.00 39.20 ? 209 LYS A N 1 ATOM 1676 C CA . LYS A 1 209 ? 10.705 50.603 35.297 1.00 38.70 ? 209 LYS A CA 1 ATOM 1677 C C . LYS A 1 209 ? 9.747 51.362 34.377 1.00 38.89 ? 209 LYS A C 1 ATOM 1678 O O . LYS A 1 209 ? 10.180 52.070 33.455 1.00 44.22 ? 209 LYS A O 1 ATOM 1679 C CB . LYS A 1 209 ? 11.174 51.530 36.399 1.00 43.64 ? 209 LYS A CB 1 ATOM 1680 C CG . LYS A 1 209 ? 11.853 52.795 35.901 1.00 52.79 ? 209 LYS A CG 1 ATOM 1681 C CD . LYS A 1 209 ? 12.635 53.470 37.032 1.00 57.68 ? 209 LYS A CD 1 ATOM 1682 C CE . LYS A 1 209 ? 13.272 54.779 36.599 1.00 60.71 ? 209 LYS A CE 1 ATOM 1683 N NZ . LYS A 1 209 ? 14.334 55.118 37.561 1.00 57.76 1 209 LYS A NZ 1 ATOM 1684 N N . ARG A 1 210 ? 8.457 51.202 34.627 1.00 39.87 ? 210 ARG A N 1 ATOM 1685 C CA . ARG A 1 210 ? 7.463 51.737 33.733 1.00 42.15 ? 210 ARG A CA 1 ATOM 1686 C C . ARG A 1 210 ? 7.617 53.246 33.750 1.00 50.52 ? 210 ARG A C 1 ATOM 1687 O O . ARG A 1 210 ? 7.724 53.853 34.818 1.00 43.45 ? 210 ARG A O 1 ATOM 1688 C CB . ARG A 1 210 ? 6.074 51.316 34.193 1.00 44.65 ? 210 ARG A CB 1 ATOM 1689 C CG . ARG A 1 210 ? 4.934 51.926 33.397 1.00 56.78 ? 210 ARG A CG 1 ATOM 1690 C CD . ARG A 1 210 ? 4.559 51.021 32.253 1.00 63.46 ? 210 ARG A CD 1 ATOM 1691 N NE . ARG A 1 210 ? 4.231 49.685 32.733 1.00 61.53 ? 210 ARG A NE 1 ATOM 1692 C CZ . ARG A 1 210 ? 3.848 48.674 31.960 1.00 65.38 ? 210 ARG A CZ 1 ATOM 1693 N NH1 . ARG A 1 210 ? 3.717 48.833 30.642 1.00 59.07 1 210 ARG A NH1 1 ATOM 1694 N NH2 . ARG A 1 210 ? 3.584 47.494 32.510 1.00 65.29 ? 210 ARG A NH2 1 ATOM 1695 N N . ARG A 1 211 ? 7.627 53.847 32.565 1.00 43.62 ? 211 ARG A N 1 ATOM 1696 C CA . ARG A 1 211 ? 7.744 55.290 32.446 1.00 45.16 ? 211 ARG A CA 1 ATOM 1697 C C . ARG A 1 211 ? 6.535 55.997 33.010 1.00 52.08 ? 211 ARG A C 1 ATOM 1698 O O . ARG A 1 211 ? 5.399 55.649 32.713 1.00 54.66 ? 211 ARG A O 1 ATOM 1699 C CB . ARG A 1 211 ? 7.942 55.690 30.982 1.00 51.05 ? 211 ARG A CB 1 ATOM 1700 C CG . ARG A 1 211 ? 8.358 57.146 30.789 1.00 52.71 ? 211 ARG A CG 1 ATOM 1701 C CD . ARG A 1 211 ? 8.717 57.421 29.340 1.00 47.31 ? 211 ARG A CD 1 ATOM 1702 N NE . ARG A 1 211 ? 9.849 56.621 28.888 1.00 45.19 ? 211 ARG A NE 1 ATOM 1703 C CZ . ARG A 1 211 ? 11.121 56.970 29.053 1.00 51.03 ? 211 ARG A CZ 1 ATOM 1704 N NH1 . ARG A 1 211 ? 11.424 58.088 29.703 1.00 55.54 1 211 ARG A NH1 1 ATOM 1705 N NH2 . ARG A 1 211 ? 12.097 56.194 28.593 1.00 54.33 ? 211 ARG A NH2 1 ATOM 1706 N N . SER A 1 212 ? 6.803 57.003 33.834 1.00 60.85 ? 212 SER A N 1 ATOM 1707 C CA . SER A 1 212 ? 5.756 57.850 34.379 1.00 70.63 ? 212 SER A CA 1 ATOM 1708 C C . SER A 1 212 ? 5.299 58.828 33.322 1.00 65.75 ? 212 SER A C 1 ATOM 1709 O O . SER A 1 212 ? 6.101 59.376 32.564 1.00 64.05 ? 212 SER A O 1 ATOM 1710 C CB . SER A 1 212 ? 6.267 58.655 35.572 1.00 76.89 ? 212 SER A CB 1 ATOM 1711 O OG . SER A 1 212 ? 5.323 59.651 35.940 1.00 79.21 ? 212 SER A OG 1 ATOM 1712 N N . HIS A 1 213 ? 4.003 59.051 33.277 1.00 55.45 ? 213 HIS A N 1 ATOM 1713 C CA . HIS A 1 213 ? 3.459 60.067 32.416 1.00 60.22 ? 213 HIS A CA 1 ATOM 1714 C C . HIS A 1 213 ? 2.621 61.032 33.253 1.00 59.30 ? 213 HIS A C 1 ATOM 1715 O O . HIS A 1 213 ? 1.570 61.482 32.793 1.00 61.82 ? 213 HIS A O 1 ATOM 1716 C CB . HIS A 1 213 ? 2.629 59.402 31.315 1.00 68.30 ? 213 HIS A CB 1 ATOM 1717 C CG . HIS A 1 213 ? 1.760 58.291 31.810 1.00 71.29 ? 213 HIS A CG 1 ATOM 1718 N ND1 . HIS A 1 213 ? 2.246 57.026 32.070 1.00 74.26 ? 213 HIS A ND1 1 ATOM 1719 C CD2 . HIS A 1 213 ? 0.441 58.263 32.114 1.00 65.03 ? 213 HIS A CD2 1 ATOM 1720 C CE1 . HIS A 1 213 ? 1.257 56.263 32.502 1.00 75.49 ? 213 HIS A CE1 1 ATOM 1721 N NE2 . HIS A 1 213 ? 0.153 56.990 32.540 1.00 72.23 ? 213 HIS A NE2 1 ATOM 1722 N N . HIS A 1 214 ? 3.067 61.345 34.473 1.00 60.09 ? 214 HIS A N 1 ATOM 1723 C CA . HIS A 1 214 ? 2.309 62.237 35.378 1.00 71.08 ? 214 HIS A CA 1 ATOM 1724 C C . HIS A 1 214 ? 2.939 63.561 35.812 1.00 86.42 ? 214 HIS A C 1 ATOM 1725 O O . HIS A 1 214 ? 2.586 64.593 35.258 1.00 80.16 ? 214 HIS A O 1 ATOM 1726 C CB . HIS A 1 214 ? 1.809 61.517 36.635 1.00 72.60 ? 214 HIS A CB 1 ATOM 1727 C CG . HIS A 1 214 ? 1.002 62.392 37.542 1.00 83.20 ? 214 HIS A CG 1 ATOM 1728 N ND1 . HIS A 1 214 ? -0.152 63.021 37.132 1.00 90.19 ? 214 HIS A ND1 1 ATOM 1729 C CD2 . HIS A 1 214 ? 1.208 62.785 38.821 1.00 85.50 ? 214 HIS A CD2 1 ATOM 1730 C CE1 . HIS A 1 214 ? -0.636 63.740 38.125 1.00 90.21 ? 214 HIS A CE1 1 ATOM 1731 N NE2 . HIS A 1 214 ? 0.174 63.617 39.159 1.00 93.06 ? 214 HIS A NE2 1 ATOM 1732 N N . HIS A 1 215 ? 3.752 63.612 36.868 1.00 98.56 ? 215 HIS A N 1 ATOM 1733 C CA . HIS A 1 215 ? 4.091 65.009 37.298 1.00 92.65 ? 215 HIS A CA 1 ATOM 1734 C C . HIS A 1 215 ? 2.859 65.845 37.700 1.00 88.91 ? 215 HIS A C 1 ATOM 1735 O O . HIS A 1 215 ? 2.750 67.035 37.355 1.00 74.91 ? 215 HIS A O 1 ATOM 1736 C CB . HIS A 1 215 ? 4.819 65.746 36.177 1.00 91.12 ? 215 HIS A CB 1 ATOM 1737 C CG . HIS A 1 215 ? 5.892 64.932 35.535 1.00 89.85 ? 215 HIS A CG 1 ATOM 1738 N ND1 . HIS A 1 215 ? 7.031 64.555 36.206 1.00 95.88 ? 215 HIS A ND1 1 ATOM 1739 C CD2 . HIS A 1 215 ? 5.987 64.389 34.301 1.00 92.38 ? 215 HIS A CD2 1 ATOM 1740 C CE1 . HIS A 1 215 ? 7.789 63.823 35.414 1.00 93.08 ? 215 HIS A CE1 1 ATOM 1741 N NE2 . HIS A 1 215 ? 7.180 63.705 34.251 1.00 95.77 ? 215 HIS A NE2 1 HETATM 1742 C C1 . NAG B 2 . ? 44.504 36.968 32.514 1.00 47.89 ? 1216 NAG A C1 1 HETATM 1743 C C2 . NAG B 2 . ? 46.031 37.065 32.621 1.00 50.32 ? 1216 NAG A C2 1 HETATM 1744 C C3 . NAG B 2 . ? 46.447 36.869 34.073 1.00 56.03 ? 1216 NAG A C3 1 HETATM 1745 C C4 . NAG B 2 . ? 45.814 37.892 34.963 1.00 53.60 ? 1216 NAG A C4 1 HETATM 1746 C C5 . NAG B 2 . ? 44.323 38.087 34.745 1.00 57.11 ? 1216 NAG A C5 1 HETATM 1747 C C6 . NAG B 2 . ? 44.052 39.586 34.953 1.00 59.21 ? 1216 NAG A C6 1 HETATM 1748 C C7 . NAG B 2 . ? 47.086 36.202 30.594 1.00 58.43 ? 1216 NAG A C7 1 HETATM 1749 C C8 . NAG B 2 . ? 47.800 35.039 29.963 1.00 55.39 ? 1216 NAG A C8 1 HETATM 1750 N N2 . NAG B 2 . ? 46.682 36.021 31.849 1.00 50.98 ? 1216 NAG A N2 1 HETATM 1751 O O3 . NAG B 2 . ? 47.829 37.092 34.216 1.00 63.34 ? 1216 NAG A O3 1 HETATM 1752 O O4 . NAG B 2 . ? 46.048 37.490 36.285 1.00 60.53 ? 1216 NAG A O4 1 HETATM 1753 O O5 . NAG B 2 . ? 43.834 37.801 33.447 1.00 49.14 ? 1216 NAG A O5 1 HETATM 1754 O O6 . NAG B 2 . ? 43.225 39.838 36.053 1.00 58.07 ? 1216 NAG A O6 1 HETATM 1755 O O7 . NAG B 2 . ? 46.893 37.248 29.959 1.00 61.63 ? 1216 NAG A O7 1 HETATM 1756 C C1 . NAG C 2 . ? 20.135 37.958 37.186 1.00 40.77 ? 1217 NAG A C1 1 HETATM 1757 C C2 . NAG C 2 . ? 19.564 36.965 38.204 1.00 48.66 ? 1217 NAG A C2 1 HETATM 1758 C C3 . NAG C 2 . ? 20.095 37.240 39.604 1.00 40.23 ? 1217 NAG A C3 1 HETATM 1759 C C4 . NAG C 2 . ? 21.593 37.314 39.572 1.00 35.70 ? 1217 NAG A C4 1 HETATM 1760 C C5 . NAG C 2 . ? 22.076 38.319 38.544 1.00 37.80 ? 1217 NAG A C5 1 HETATM 1761 C C6 . NAG C 2 . ? 23.598 38.267 38.496 1.00 38.48 ? 1217 NAG A C6 1 HETATM 1762 C C7 . NAG C 2 . ? 17.375 35.927 37.897 1.00 55.92 ? 1217 NAG A C7 1 HETATM 1763 C C8 . NAG C 2 . ? 15.885 36.111 37.909 1.00 54.79 ? 1217 NAG A C8 1 HETATM 1764 N N2 . NAG C 2 . ? 18.117 36.985 38.258 1.00 53.16 ? 1217 NAG A N2 1 HETATM 1765 O O3 . NAG C 2 . ? 19.777 36.134 40.405 1.00 41.91 ? 1217 NAG A O3 1 HETATM 1766 O O4 . NAG C 2 . ? 22.030 37.696 40.850 1.00 41.99 ? 1217 NAG A O4 1 HETATM 1767 O O5 . NAG C 2 . ? 21.545 37.979 37.282 1.00 36.46 ? 1217 NAG A O5 1 HETATM 1768 O O6 . NAG C 2 . ? 24.071 36.987 38.063 1.00 34.70 ? 1217 NAG A O6 1 HETATM 1769 O O7 . NAG C 2 . ? 17.847 34.841 37.568 1.00 51.20 ? 1217 NAG A O7 1 HETATM 1770 C C1 . EDO D 3 . ? 22.038 47.430 16.703 1.00 66.16 ? 1218 EDO A C1 1 HETATM 1771 O O1 . EDO D 3 . ? 22.635 48.629 16.185 1.00 71.46 ? 1218 EDO A O1 1 HETATM 1772 C C2 . EDO D 3 . ? 21.831 46.382 15.614 1.00 67.80 ? 1218 EDO A C2 1 HETATM 1773 O O2 . EDO D 3 . ? 20.634 46.675 14.879 1.00 73.26 ? 1218 EDO A O2 1 HETATM 1774 C C1 . EDO E 3 . ? 20.054 34.034 34.782 1.00 52.80 ? 1219 EDO A C1 1 HETATM 1775 O O1 . EDO E 3 . ? 20.705 35.292 34.998 1.00 50.91 ? 1219 EDO A O1 1 HETATM 1776 C C2 . EDO E 3 . ? 20.041 33.731 33.293 1.00 52.37 ? 1219 EDO A C2 1 HETATM 1777 O O2 . EDO E 3 . ? 21.388 33.494 32.852 1.00 51.79 ? 1219 EDO A O2 1 HETATM 1778 C C1 . EDO F 3 . ? 28.230 25.701 30.950 1.00 58.48 ? 1220 EDO A C1 1 HETATM 1779 O O1 . EDO F 3 . ? 28.787 24.390 30.830 1.00 60.16 ? 1220 EDO A O1 1 HETATM 1780 C C2 . EDO F 3 . ? 27.373 26.018 29.734 1.00 64.86 ? 1220 EDO A C2 1 HETATM 1781 O O2 . EDO F 3 . ? 26.639 27.229 29.970 1.00 64.66 ? 1220 EDO A O2 1 HETATM 1782 C C1 . EDO G 3 . ? 31.049 51.486 16.523 1.00 66.83 ? 1221 EDO A C1 1 HETATM 1783 O O1 . EDO G 3 . ? 32.474 51.292 16.515 1.00 67.19 ? 1221 EDO A O1 1 HETATM 1784 C C2 . EDO G 3 . ? 30.582 51.826 17.921 1.00 71.26 ? 1221 EDO A C2 1 HETATM 1785 O O2 . EDO G 3 . ? 30.580 50.676 18.742 1.00 73.47 ? 1221 EDO A O2 1 HETATM 1786 O O . HOH H 4 . ? 20.069 30.093 30.528 1.00 67.21 ? 2001 HOH A O 1 HETATM 1787 O O . HOH H 4 . ? 47.646 50.631 -2.055 1.00 60.05 ? 2002 HOH A O 1 HETATM 1788 O O . HOH H 4 . ? 51.406 28.816 15.592 1.00 68.30 ? 2003 HOH A O 1 HETATM 1789 O O . HOH H 4 . ? 51.813 23.356 10.354 1.00 63.64 ? 2004 HOH A O 1 HETATM 1790 O O . HOH H 4 . ? 50.618 34.769 3.033 0.99 58.75 ? 2005 HOH A O 1 HETATM 1791 O O . HOH H 4 . ? 48.438 40.008 -1.673 1.00 57.49 ? 2006 HOH A O 1 HETATM 1792 O O . HOH H 4 . ? 46.561 37.141 -0.010 0.50 55.92 ? 2007 HOH A O 1 HETATM 1793 O O . HOH H 4 . ? 43.588 24.157 28.812 0.97 53.08 ? 2008 HOH A O 1 HETATM 1794 O O . HOH H 4 . ? 45.057 28.142 35.163 1.00 63.15 ? 2009 HOH A O 1 HETATM 1795 O O . HOH H 4 . ? 52.011 33.498 9.189 0.85 52.70 ? 2010 HOH A O 1 HETATM 1796 O O . HOH H 4 . ? 55.906 35.376 7.997 1.00 64.01 ? 2011 HOH A O 1 HETATM 1797 O O . HOH H 4 . ? 51.040 34.807 12.002 0.75 45.76 ? 2012 HOH A O 1 HETATM 1798 O O . HOH H 4 . ? 42.657 44.553 27.723 1.00 62.09 ? 2013 HOH A O 1 HETATM 1799 O O . HOH H 4 . ? 38.253 48.348 27.707 1.00 47.78 ? 2014 HOH A O 1 HETATM 1800 O O . HOH H 4 . ? 50.468 28.210 5.803 1.00 62.29 ? 2015 HOH A O 1 HETATM 1801 O O . HOH H 4 . ? 54.064 30.510 3.819 1.00 73.45 ? 2016 HOH A O 1 HETATM 1802 O O . HOH H 4 . ? 21.293 53.252 17.863 1.00 78.64 ? 2017 HOH A O 1 HETATM 1803 O O . HOH H 4 . ? 50.293 30.919 13.761 1.00 62.36 ? 2018 HOH A O 1 HETATM 1804 O O . HOH H 4 . ? 50.826 24.931 11.263 1.00 67.21 ? 2019 HOH A O 1 HETATM 1805 O O . HOH H 4 . ? 4.818 42.859 21.131 1.00 64.29 ? 2020 HOH A O 1 HETATM 1806 O O . HOH H 4 . ? 42.723 30.553 9.300 0.78 42.55 ? 2021 HOH A O 1 HETATM 1807 O O . HOH H 4 . ? 42.565 36.119 17.641 0.99 31.38 ? 2022 HOH A O 1 HETATM 1808 O O . HOH H 4 . ? 47.359 29.930 13.957 0.84 34.50 ? 2023 HOH A O 1 HETATM 1809 O O . HOH H 4 . ? 45.574 30.987 15.764 0.92 36.72 ? 2024 HOH A O 1 HETATM 1810 O O . HOH H 4 . ? 44.049 24.767 12.448 0.79 46.26 ? 2025 HOH A O 1 HETATM 1811 O O . HOH H 4 . ? 37.486 31.215 15.841 1.00 48.52 ? 2026 HOH A O 1 HETATM 1812 O O . HOH H 4 . ? 40.117 25.745 19.567 0.87 46.28 ? 2027 HOH A O 1 HETATM 1813 O O . HOH H 4 . ? 42.510 25.823 20.167 0.72 34.48 ? 2028 HOH A O 1 HETATM 1814 O O . HOH H 4 . ? 46.643 26.550 21.338 1.00 48.20 ? 2029 HOH A O 1 HETATM 1815 O O . HOH H 4 . ? 42.171 25.474 23.066 1.00 40.32 ? 2030 HOH A O 1 HETATM 1816 O O . HOH H 4 . ? 44.363 25.341 23.233 1.00 52.39 ? 2031 HOH A O 1 HETATM 1817 O O . HOH H 4 . ? 46.894 35.275 23.569 0.73 31.39 ? 2032 HOH A O 1 HETATM 1818 O O . HOH H 4 . ? 48.640 26.677 20.996 1.00 62.60 ? 2033 HOH A O 1 HETATM 1819 O O . HOH H 4 . ? 53.199 35.760 20.539 0.81 46.90 ? 2034 HOH A O 1 HETATM 1820 O O . HOH H 4 . ? 50.919 38.058 22.885 1.00 64.56 ? 2035 HOH A O 1 HETATM 1821 O O . HOH H 4 . ? 49.327 36.552 23.978 1.00 66.44 ? 2036 HOH A O 1 HETATM 1822 O O . HOH H 4 . ? 51.586 24.583 24.668 0.96 52.63 ? 2037 HOH A O 1 HETATM 1823 O O . HOH H 4 . ? 44.204 26.330 29.105 0.71 43.33 ? 2038 HOH A O 1 HETATM 1824 O O . HOH H 4 . ? 44.214 27.899 31.996 1.00 49.66 ? 2039 HOH A O 1 HETATM 1825 O O . HOH H 4 . ? 46.932 35.070 26.576 0.96 54.08 ? 2040 HOH A O 1 HETATM 1826 O O . HOH H 4 . ? 45.233 36.681 27.861 0.96 39.01 ? 2041 HOH A O 1 HETATM 1827 O O . HOH H 4 . ? 44.001 38.541 26.041 0.88 34.20 ? 2042 HOH A O 1 HETATM 1828 O O . HOH H 4 . ? 43.980 40.723 27.033 1.00 66.51 ? 2043 HOH A O 1 HETATM 1829 O O . HOH H 4 . ? 41.972 34.620 33.839 0.74 27.52 ? 2044 HOH A O 1 HETATM 1830 O O . HOH H 4 . ? 45.307 39.923 29.975 1.00 50.77 ? 2045 HOH A O 1 HETATM 1831 O O . HOH H 4 . ? 35.893 45.033 26.157 0.69 31.69 ? 2046 HOH A O 1 HETATM 1832 O O . HOH H 4 . ? 39.408 45.851 28.120 0.94 44.78 ? 2047 HOH A O 1 HETATM 1833 O O . HOH H 4 . ? 31.317 45.160 31.114 0.74 30.58 ? 2048 HOH A O 1 HETATM 1834 O O . HOH H 4 . ? 30.203 48.164 23.440 1.00 41.52 ? 2049 HOH A O 1 HETATM 1835 O O . HOH H 4 . ? 36.161 47.943 26.312 0.94 36.94 ? 2050 HOH A O 1 HETATM 1836 O O . HOH H 4 . ? 29.909 46.985 29.755 0.65 25.94 ? 2051 HOH A O 1 HETATM 1837 O O . HOH H 4 . ? 24.172 52.664 20.726 1.00 67.18 ? 2052 HOH A O 1 HETATM 1838 O O . HOH H 4 . ? 24.298 53.423 25.381 0.91 43.93 ? 2053 HOH A O 1 HETATM 1839 O O . HOH H 4 . ? 43.566 49.191 18.807 0.95 48.54 ? 2054 HOH A O 1 HETATM 1840 O O . HOH H 4 . ? 19.731 51.549 17.259 1.00 57.13 ? 2055 HOH A O 1 HETATM 1841 O O . HOH H 4 . ? 42.104 48.653 25.005 1.00 55.83 ? 2056 HOH A O 1 HETATM 1842 O O . HOH H 4 . ? 8.327 47.832 19.838 1.00 59.29 ? 2057 HOH A O 1 HETATM 1843 O O . HOH H 4 . ? 7.510 45.342 18.210 1.00 44.79 ? 2058 HOH A O 1 HETATM 1844 O O . HOH H 4 . ? 6.707 41.303 20.772 1.00 69.73 ? 2059 HOH A O 1 HETATM 1845 O O . HOH H 4 . ? 9.164 39.381 21.494 0.91 55.00 ? 2060 HOH A O 1 HETATM 1846 O O . HOH H 4 . ? 10.537 40.905 22.465 1.00 57.91 ? 2061 HOH A O 1 HETATM 1847 O O . HOH H 4 . ? 5.683 44.779 22.491 1.00 64.70 ? 2062 HOH A O 1 HETATM 1848 O O . HOH H 4 . ? 8.171 47.858 24.380 1.00 51.25 ? 2063 HOH A O 1 HETATM 1849 O O . HOH H 4 . ? 6.078 46.774 26.882 1.00 48.47 ? 2064 HOH A O 1 HETATM 1850 O O . HOH H 4 . ? 12.957 33.789 33.543 0.61 39.71 ? 2065 HOH A O 1 HETATM 1851 O O . HOH H 4 . ? 3.886 39.286 22.333 1.00 58.11 ? 2066 HOH A O 1 HETATM 1852 O O . HOH H 4 . ? 6.953 45.200 49.885 1.00 55.61 ? 2067 HOH A O 1 HETATM 1853 O O . HOH H 4 . ? 4.774 44.008 33.016 1.00 65.32 ? 2068 HOH A O 1 HETATM 1854 O O . HOH H 4 . ? 17.747 40.982 25.028 0.49 26.77 ? 2069 HOH A O 1 HETATM 1855 O O . HOH H 4 . ? 38.061 31.205 36.961 0.85 39.64 ? 2070 HOH A O 1 HETATM 1856 O O . HOH H 4 . ? 38.174 23.381 21.694 1.00 67.62 ? 2071 HOH A O 1 HETATM 1857 O O . HOH H 4 . ? 36.868 32.135 40.069 0.50 55.38 ? 2072 HOH A O 1 HETATM 1858 O O . HOH H 4 . ? 30.343 47.739 41.071 1.00 60.19 ? 2073 HOH A O 1 HETATM 1859 O O . HOH H 4 . ? 23.653 46.655 41.655 1.00 47.68 ? 2074 HOH A O 1 HETATM 1860 O O . HOH H 4 . ? 31.945 41.920 19.575 0.99 42.60 ? 2075 HOH A O 1 HETATM 1861 O O . HOH H 4 . ? 37.515 50.063 25.082 0.67 35.86 ? 2076 HOH A O 1 HETATM 1862 O O . HOH H 4 . ? 33.450 35.910 20.302 1.00 38.59 ? 2077 HOH A O 1 HETATM 1863 O O . HOH H 4 . ? 30.704 36.912 19.465 1.00 51.12 ? 2078 HOH A O 1 HETATM 1864 O O . HOH H 4 . ? 1.250 53.124 33.617 1.00 69.78 ? 2079 HOH A O 1 HETATM 1865 O O . HOH H 4 . ? 10.172 56.685 38.047 1.00 67.01 ? 2080 HOH A O 1 HETATM 1866 O O . HOH H 4 . ? 42.241 41.921 27.314 1.00 50.80 ? 2081 HOH A O 1 HETATM 1867 O O . HOH H 4 . ? 23.540 42.457 39.739 1.00 47.78 ? 2082 HOH A O 1 HETATM 1868 O O . HOH H 4 . ? 25.342 44.308 41.092 0.92 46.68 ? 2083 HOH A O 1 HETATM 1869 O O . HOH H 4 . ? 26.692 45.323 44.755 1.00 67.32 ? 2084 HOH A O 1 HETATM 1870 O O . HOH H 4 . ? 49.701 39.261 21.627 0.44 29.11 ? 2085 HOH A O 1 HETATM 1871 O O . HOH H 4 . ? 36.324 35.166 39.647 1.00 36.79 ? 2086 HOH A O 1 HETATM 1872 O O . HOH H 4 . ? 40.426 37.232 38.430 0.97 52.88 ? 2087 HOH A O 1 HETATM 1873 O O . HOH H 4 . ? 37.616 39.288 38.711 1.00 71.09 ? 2088 HOH A O 1 HETATM 1874 O O . HOH H 4 . ? 27.213 30.527 37.039 1.00 38.58 ? 2089 HOH A O 1 HETATM 1875 O O . HOH H 4 . ? 24.975 32.052 41.820 1.00 56.38 ? 2090 HOH A O 1 HETATM 1876 O O . HOH H 4 . ? 23.195 33.162 39.759 1.00 54.09 ? 2091 HOH A O 1 HETATM 1877 O O . HOH H 4 . ? 38.102 34.937 41.375 0.70 39.01 ? 2092 HOH A O 1 HETATM 1878 O O . HOH H 4 . ? 55.354 39.691 11.379 1.00 58.91 ? 2093 HOH A O 1 HETATM 1879 O O . HOH H 4 . ? 21.743 33.311 38.136 0.83 45.73 ? 2094 HOH A O 1 HETATM 1880 O O . HOH H 4 . ? 55.088 43.540 18.213 1.00 54.75 ? 2095 HOH A O 1 HETATM 1881 O O . HOH H 4 . ? 57.153 41.695 12.151 0.65 37.95 ? 2096 HOH A O 1 HETATM 1882 O O . HOH H 4 . ? 56.960 47.612 16.703 0.84 45.16 ? 2097 HOH A O 1 HETATM 1883 O O . HOH H 4 . ? 62.726 46.272 12.328 0.69 47.21 ? 2098 HOH A O 1 HETATM 1884 O O . HOH H 4 . ? 6.167 56.744 38.223 1.00 67.40 ? 2099 HOH A O 1 HETATM 1885 O O . HOH H 4 . ? 52.408 53.101 17.000 0.85 43.40 ? 2100 HOH A O 1 HETATM 1886 O O . HOH H 4 . ? 55.141 47.927 21.904 1.00 69.31 ? 2101 HOH A O 1 HETATM 1887 O O . HOH H 4 . ? 57.698 52.656 13.928 1.00 69.22 ? 2102 HOH A O 1 HETATM 1888 O O . HOH H 4 . ? 64.145 47.905 13.509 1.00 64.57 ? 2103 HOH A O 1 HETATM 1889 O O . HOH H 4 . ? 54.684 56.397 5.293 1.00 63.82 ? 2104 HOH A O 1 HETATM 1890 O O . HOH H 4 . ? 48.896 53.280 11.932 1.00 55.82 ? 2105 HOH A O 1 HETATM 1891 O O . HOH H 4 . ? 35.103 48.380 10.395 1.00 61.05 ? 2106 HOH A O 1 HETATM 1892 O O . HOH H 4 . ? 32.232 39.241 9.742 0.98 50.43 ? 2107 HOH A O 1 HETATM 1893 O O . HOH H 4 . ? 41.999 33.223 8.454 0.67 35.13 ? 2108 HOH A O 1 HETATM 1894 O O . HOH H 4 . ? 36.127 33.541 13.646 0.99 49.25 ? 2109 HOH A O 1 HETATM 1895 O O . HOH H 4 . ? 36.141 30.153 18.142 1.00 49.42 ? 2110 HOH A O 1 HETATM 1896 O O . HOH H 4 . ? 24.416 35.802 21.051 0.50 51.16 ? 2111 HOH A O 1 HETATM 1897 O O . HOH H 4 . ? 25.215 37.420 21.049 0.50 57.49 ? 2112 HOH A O 1 HETATM 1898 O O . HOH H 4 . ? 30.669 29.581 30.869 0.72 27.12 ? 2113 HOH A O 1 HETATM 1899 O O . HOH H 4 . ? 15.949 33.941 28.515 0.85 47.48 ? 2114 HOH A O 1 HETATM 1900 O O . HOH H 4 . ? 16.714 34.235 31.376 1.00 55.77 ? 2115 HOH A O 1 HETATM 1901 O O . HOH H 4 . ? 12.573 31.367 24.914 1.00 71.60 ? 2116 HOH A O 1 HETATM 1902 O O . HOH H 4 . ? 20.365 34.534 17.769 1.00 68.51 ? 2117 HOH A O 1 HETATM 1903 O O . HOH H 4 . ? 33.391 46.522 11.254 1.00 46.66 ? 2118 HOH A O 1 HETATM 1904 O O . HOH H 4 . ? 35.777 46.254 15.285 0.91 36.00 ? 2119 HOH A O 1 HETATM 1905 O O . HOH H 4 . ? 43.086 46.569 18.882 0.89 35.72 ? 2120 HOH A O 1 HETATM 1906 O O . HOH H 4 . ? 46.714 46.781 25.905 1.00 63.91 ? 2121 HOH A O 1 HETATM 1907 O O . HOH H 4 . ? 52.149 41.855 22.189 0.82 56.22 ? 2122 HOH A O 1 HETATM 1908 O O . HOH H 4 . ? 40.959 48.767 22.294 0.61 32.90 ? 2123 HOH A O 1 HETATM 1909 O O . HOH H 4 . ? 32.173 47.093 13.486 0.98 57.87 ? 2124 HOH A O 1 HETATM 1910 O O . HOH H 4 . ? 31.014 48.555 20.748 0.55 31.39 ? 2125 HOH A O 1 HETATM 1911 O O . HOH H 4 . ? 18.432 37.430 17.620 1.00 59.62 ? 2126 HOH A O 1 HETATM 1912 O O . HOH H 4 . ? 18.821 36.295 21.160 0.84 38.31 ? 2127 HOH A O 1 HETATM 1913 O O . HOH H 4 . ? 16.379 39.371 29.803 0.56 22.77 ? 2128 HOH A O 1 HETATM 1914 O O . HOH H 4 . ? 16.166 37.548 33.498 0.92 39.78 ? 2129 HOH A O 1 HETATM 1915 O O . HOH H 4 . ? 15.684 35.469 33.651 1.00 66.33 ? 2130 HOH A O 1 HETATM 1916 O O . HOH H 4 . ? 7.818 37.447 35.968 0.64 45.14 ? 2131 HOH A O 1 HETATM 1917 O O . HOH H 4 . ? 13.109 41.948 43.330 1.00 63.40 ? 2132 HOH A O 1 HETATM 1918 O O . HOH H 4 . ? 6.201 47.227 48.083 1.00 43.01 ? 2133 HOH A O 1 HETATM 1919 O O . HOH H 4 . ? 9.762 39.356 45.276 0.99 69.04 ? 2134 HOH A O 1 HETATM 1920 O O . HOH H 4 . ? 5.976 45.093 35.414 0.65 41.11 ? 2135 HOH A O 1 HETATM 1921 O O . HOH H 4 . ? 32.861 32.166 28.947 0.66 24.72 ? 2136 HOH A O 1 HETATM 1922 O O . HOH H 4 . ? 34.788 30.426 28.968 1.00 32.74 ? 2137 HOH A O 1 HETATM 1923 O O . HOH H 4 . ? 40.739 22.615 29.849 1.00 57.17 ? 2138 HOH A O 1 HETATM 1924 O O . HOH H 4 . ? 40.825 30.365 34.774 1.00 48.20 ? 2139 HOH A O 1 HETATM 1925 O O . HOH H 4 . ? 40.613 23.196 36.771 1.00 57.30 ? 2140 HOH A O 1 HETATM 1926 O O . HOH H 4 . ? 40.519 23.635 23.077 1.00 63.72 ? 2141 HOH A O 1 HETATM 1927 O O . HOH H 4 . ? 43.187 23.583 26.408 0.97 49.83 ? 2142 HOH A O 1 HETATM 1928 O O . HOH H 4 . ? 36.899 31.264 34.642 0.60 27.88 ? 2143 HOH A O 1 HETATM 1929 O O . HOH H 4 . ? 38.986 33.760 36.861 0.85 42.58 ? 2144 HOH A O 1 HETATM 1930 O O . HOH H 4 . ? 35.014 41.025 35.467 0.86 28.66 ? 2145 HOH A O 1 HETATM 1931 O O . HOH H 4 . ? 39.063 44.156 33.427 1.00 69.58 ? 2146 HOH A O 1 HETATM 1932 O O . HOH H 4 . ? 32.750 51.221 34.956 1.00 50.50 ? 2147 HOH A O 1 HETATM 1933 O O . HOH H 4 . ? 28.344 47.247 39.177 0.93 44.91 ? 2148 HOH A O 1 HETATM 1934 O O . HOH H 4 . ? 34.328 47.023 40.116 0.94 38.45 ? 2149 HOH A O 1 HETATM 1935 O O . HOH H 4 . ? 29.614 52.054 39.107 1.00 60.65 ? 2150 HOH A O 1 HETATM 1936 O O . HOH H 4 . ? 23.989 50.933 36.068 1.00 48.29 ? 2151 HOH A O 1 HETATM 1937 O O . HOH H 4 . ? 28.042 51.897 37.102 1.00 65.29 ? 2152 HOH A O 1 HETATM 1938 O O . HOH H 4 . ? 26.858 49.494 39.415 0.99 68.97 ? 2153 HOH A O 1 HETATM 1939 O O . HOH H 4 . ? 30.279 52.066 34.169 0.84 52.07 ? 2154 HOH A O 1 HETATM 1940 O O . HOH H 4 . ? 25.277 52.493 33.331 1.00 64.14 ? 2155 HOH A O 1 HETATM 1941 O O . HOH H 4 . ? 30.596 54.148 30.382 1.00 72.51 ? 2156 HOH A O 1 HETATM 1942 O O . HOH H 4 . ? 26.390 54.383 31.101 1.00 49.06 ? 2157 HOH A O 1 HETATM 1943 O O . HOH H 4 . ? 24.151 60.002 28.377 0.98 57.61 ? 2158 HOH A O 1 HETATM 1944 O O . HOH H 4 . ? 24.680 61.406 20.605 1.00 74.50 ? 2159 HOH A O 1 HETATM 1945 O O . HOH H 4 . ? 19.414 58.210 26.059 1.00 73.54 ? 2160 HOH A O 1 HETATM 1946 O O . HOH H 4 . ? 16.069 58.780 22.959 1.00 59.70 ? 2161 HOH A O 1 HETATM 1947 O O . HOH H 4 . ? 13.979 59.135 29.918 1.00 65.13 ? 2162 HOH A O 1 HETATM 1948 O O . HOH H 4 . ? 15.879 55.607 30.254 1.00 50.22 ? 2163 HOH A O 1 HETATM 1949 O O . HOH H 4 . ? 14.089 53.637 27.564 0.95 50.54 ? 2164 HOH A O 1 HETATM 1950 O O . HOH H 4 . ? 2.344 53.809 31.012 1.00 65.55 ? 2165 HOH A O 1 HETATM 1951 O O . HOH H 4 . ? 9.111 58.023 34.497 0.90 56.57 ? 2166 HOH A O 1 HETATM 1952 O O . HOH H 4 . ? 9.549 55.361 36.082 1.00 58.87 ? 2167 HOH A O 1 HETATM 1953 O O . HOH H 4 . ? 12.243 60.177 33.077 1.00 71.39 ? 2168 HOH A O 1 HETATM 1954 O O . HOH H 4 . ? 20.760 55.386 34.368 1.00 77.36 ? 2169 HOH A O 1 HETATM 1955 O O . HOH H 4 . ? 22.275 54.927 35.679 1.00 78.24 ? 2170 HOH A O 1 HETATM 1956 O O . HOH H 4 . ? 24.130 41.696 37.209 0.58 24.08 ? 2171 HOH A O 1 HETATM 1957 O O . HOH H 4 . ? 27.561 44.953 39.905 0.73 33.03 ? 2172 HOH A O 1 HETATM 1958 O O . HOH H 4 . ? 37.783 36.635 37.586 1.00 43.90 ? 2173 HOH A O 1 HETATM 1959 O O . HOH H 4 . ? 28.803 30.873 35.007 0.87 32.09 ? 2174 HOH A O 1 HETATM 1960 O O . HOH H 4 . ? 28.061 33.349 40.695 0.84 28.59 ? 2175 HOH A O 1 HETATM 1961 O O . HOH H 4 . ? 24.754 35.329 40.001 0.99 36.13 ? 2176 HOH A O 1 HETATM 1962 O O . HOH H 4 . ? 25.046 33.107 35.505 1.00 46.09 ? 2177 HOH A O 1 HETATM 1963 O O . HOH H 4 . ? 33.795 28.312 40.645 0.83 26.22 ? 2178 HOH A O 1 HETATM 1964 O O . HOH H 4 . ? 34.275 23.079 42.195 0.74 39.93 ? 2179 HOH A O 1 HETATM 1965 O O . HOH H 4 . ? 24.961 25.053 35.797 1.00 56.39 ? 2180 HOH A O 1 HETATM 1966 O O . HOH H 4 . ? 32.547 17.809 35.179 1.00 58.56 ? 2181 HOH A O 1 HETATM 1967 O O . HOH H 4 . ? 39.352 19.477 35.355 1.00 56.83 ? 2182 HOH A O 1 HETATM 1968 O O . HOH H 4 . ? 37.489 25.140 39.118 0.64 38.59 ? 2183 HOH A O 1 HETATM 1969 O O . HOH H 4 . ? 31.014 19.535 33.584 1.00 61.79 ? 2184 HOH A O 1 HETATM 1970 O O . HOH H 4 . ? 28.445 29.089 32.916 0.87 31.87 ? 2185 HOH A O 1 HETATM 1971 O O . HOH H 4 . ? 26.235 30.879 32.760 0.68 32.37 ? 2186 HOH A O 1 HETATM 1972 O O . HOH H 4 . ? 22.963 35.104 36.328 1.00 38.22 ? 2187 HOH A O 1 HETATM 1973 O O . HOH H 4 . ? 20.966 43.590 40.214 1.00 60.09 ? 2188 HOH A O 1 HETATM 1974 O O . HOH H 4 . ? 5.426 54.771 36.661 1.00 56.90 ? 2189 HOH A O 1 HETATM 1975 O O . HOH H 4 . ? 4.229 55.644 30.085 1.00 64.94 ? 2190 HOH A O 1 HETATM 1976 O O . HOH H 4 . ? 9.942 60.121 31.068 1.00 47.14 ? 2191 HOH A O 1 HETATM 1977 O O . HOH H 4 . ? 3.632 58.399 35.658 0.61 33.66 ? 2192 HOH A O 1 HETATM 1978 O O . HOH H 4 . ? 0.310 55.469 35.108 1.00 52.79 ? 2193 HOH A O 1 HETATM 1979 O O . HOH H 4 . ? -0.458 57.574 35.846 1.00 71.29 ? 2194 HOH A O 1 HETATM 1980 O O . HOH H 4 . ? 2.081 68.191 39.311 0.50 70.96 ? 2195 HOH A O 1 HETATM 1981 O O . HOH H 4 . ? 44.312 43.805 34.149 1.00 62.86 ? 2196 HOH A O 1 HETATM 1982 O O . HOH H 4 . ? 46.162 42.925 33.755 1.00 64.70 ? 2197 HOH A O 1 HETATM 1983 O O . HOH H 4 . ? 20.001 33.700 40.187 1.00 63.13 ? 2198 HOH A O 1 HETATM 1984 O O . HOH H 4 . ? 23.710 40.196 41.870 0.87 50.37 ? 2199 HOH A O 1 HETATM 1985 O O . HOH H 4 . ? 23.493 35.698 42.143 1.00 59.49 ? 2200 HOH A O 1 HETATM 1986 O O . HOH H 4 . ? 18.769 46.470 12.848 1.00 73.00 ? 2201 HOH A O 1 HETATM 1987 O O . HOH H 4 . ? 22.697 31.813 34.144 1.00 62.73 ? 2202 HOH A O 1 HETATM 1988 O O . HOH H 4 . ? 21.731 31.078 31.145 1.00 72.28 ? 2203 HOH A O 1 HETATM 1989 O O . HOH H 4 . ? 24.211 27.487 29.411 1.00 75.21 ? 2204 HOH A O 1 HETATM 1990 O O . HOH H 4 . ? 27.947 26.230 26.765 1.00 78.01 ? 2205 HOH A O 1 HETATM 1991 O O . HOH H 4 . ? 28.836 19.231 34.169 1.00 70.33 ? 2206 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 . ASP A 2 ? 1.3392 1.0761 1.0719 -0.2911 0.1282 0.1710 2 ASP A N 2 C CA . ASP A 2 ? 1.3570 1.1201 1.1393 -0.2960 0.1324 0.1643 2 ASP A CA 3 C C . ASP A 2 ? 1.2508 1.0218 1.0388 -0.2896 0.1208 0.1484 2 ASP A C 4 O O . ASP A 2 ? 1.2583 1.0424 1.0834 -0.2922 0.1105 0.1428 2 ASP A O 5 C CB . ASP A 2 ? 1.4130 1.1736 1.2303 -0.3055 0.1227 0.1703 2 ASP A CB 6 C CG . ASP A 2 ? 1.4203 1.1487 1.2203 -0.3016 0.1002 0.1683 2 ASP A CG 7 O OD1 . ASP A 2 ? 1.3373 1.0647 1.1446 -0.2970 0.0840 0.1562 2 ASP A OD1 8 O OD2 . ASP A 2 ? 1.4252 1.1285 1.2047 -0.3018 0.1006 0.1799 2 ASP A OD2 9 N N . GLY A 3 ? 1.0559 0.8191 0.8053 -0.2822 0.1220 0.1415 3 GLY A N 10 C CA . GLY A 3 ? 1.0325 0.8081 0.7893 -0.2704 0.1142 0.1241 3 GLY A CA 11 C C . GLY A 3 ? 0.9631 0.7618 0.7378 -0.2677 0.1385 0.1180 3 GLY A C 12 O O . GLY A 3 ? 0.8858 0.6950 0.6691 -0.2572 0.1373 0.1041 3 GLY A O 13 N N . LYS A 4 ? 0.9937 0.7989 0.7748 -0.2763 0.1627 0.1299 4 LYS A N 14 C CA . LYS A 4 ? 0.9887 0.8152 0.7900 -0.2720 0.1919 0.1281 4 LYS A CA 15 C C . LYS A 4 ? 0.8514 0.7062 0.7050 -0.2640 0.1858 0.1216 4 LYS A C 16 O O . LYS A 4 ? 0.8828 0.7467 0.7414 -0.2520 0.2009 0.1125 4 LYS A O 17 C CB . LYS A 4 ? 1.0120 0.8521 0.8352 -0.2792 0.2132 0.1447 4 LYS A CB 18 C CG . LYS A 4 ? 1.1250 0.9896 0.9745 -0.2710 0.2464 0.1458 4 LYS A CG 19 C CD . LYS A 4 ? 1.1767 1.0609 1.0541 -0.2759 0.2660 0.1643 4 LYS A CD 20 C CE . LYS A 4 ? 1.2172 1.1256 1.1192 -0.2638 0.3007 0.1667 4 LYS A CE 21 N NZ . LYS A 4 ? 1.3141 1.2447 1.2430 -0.2688 0.3198 0.1863 4 LYS A NZ 22 N N . TYR A 5 ? 0.7938 0.6604 0.6841 -0.2714 0.1645 0.1268 5 TYR A N 23 C CA . TYR A 5 ? 0.7631 0.6588 0.7013 -0.2654 0.1556 0.1224 5 TYR A CA 24 C C . TYR A 5 ? 0.8005 0.6852 0.7215 -0.2517 0.1382 0.1048 5 TYR A C 25 O O . TYR A 5 ? 0.7285 0.6316 0.6714 -0.2396 0.1451 0.0987 5 TYR A O 26 C CB . TYR A 5 ? 0.7330 0.6449 0.7120 -0.2816 0.1383 0.1329 5 TYR A CB 27 C CG . TYR A 5 ? 0.8160 0.7568 0.8320 -0.2925 0.1608 0.1511 5 TYR A CG 28 C CD1 . TYR A 5 ? 0.9291 0.9097 0.9886 -0.2832 0.1810 0.1570 5 TYR A CD1 29 C CD2 . TYR A 5 ? 0.8720 0.8013 0.8814 -0.3075 0.1636 0.1632 5 TYR A CD2 30 C CE1 . TYR A 5 ? 0.9495 0.9615 1.0479 -0.2915 0.2042 0.1760 5 TYR A CE1 31 C CE2 . TYR A 5 ? 0.9739 0.9330 1.0217 -0.3133 0.1841 0.1798 5 TYR A CE2 32 C CZ . TYR A 5 ? 1.0151 1.0171 1.1077 -0.3076 0.2052 0.1872 5 TYR A CZ 33 O OH . TYR A 5 ? 1.0475 1.0837 1.1838 -0.3115 0.2273 0.2065 5 TYR A OH 34 N N . ALA A 6 ? 0.6611 0.5168 0.5444 -0.2520 0.1181 0.0983 6 ALA A N 35 C CA . ALA A 6 ? 0.6548 0.5022 0.5220 -0.2393 0.1039 0.0828 6 ALA A CA 36 C C . ALA A 6 ? 0.7378 0.5839 0.5834 -0.2291 0.1245 0.0729 6 ALA A C 37 O O . ALA A 6 ? 0.7071 0.5581 0.5598 -0.2184 0.1216 0.0615 6 ALA A O 38 C CB . ALA A 6 ? 0.7616 0.5811 0.5930 -0.2401 0.0828 0.0811 6 ALA A CB 39 N N . GLN A 7 ? 0.7748 0.6103 0.5904 -0.2334 0.1465 0.0769 7 GLN A N 40 C CA . GLN A 7 ? 0.8032 0.6299 0.5912 -0.2266 0.1694 0.0661 7 GLN A CA 41 C C . GLN A 7 ? 0.7981 0.6468 0.6279 -0.2167 0.1941 0.0669 7 GLN A C 42 O O . GLN A 7 ? 0.8092 0.6527 0.6332 -0.2058 0.2050 0.0548 7 GLN A O 43 C CB . GLN A 7 ? 0.8100 0.6172 0.5506 -0.2354 0.1891 0.0704 7 GLN A CB 44 C CG . GLN A 7 ? 0.8947 0.6825 0.5918 -0.2445 0.1688 0.0746 7 GLN A CG 45 C CD . GLN A 7 ? 1.0825 0.8541 0.7352 -0.2542 0.1896 0.0821 7 GLN A CD 46 O OE1 . GLN A 7 ? 1.1820 0.9433 0.8071 -0.2539 0.2158 0.0741 7 GLN A OE1 47 N NE2 . GLN A 7 ? 1.1939 0.9596 0.8367 -0.2629 0.1802 0.0978 7 GLN A NE2 48 N N . LYS A 8 ? 0.7719 0.6449 0.6441 -0.2205 0.2047 0.0828 8 LYS A N 49 C CA . LYS A 8 ? 0.7687 0.6707 0.6899 -0.2097 0.2276 0.0890 8 LYS A CA 50 C C . LYS A 8 ? 0.6907 0.6075 0.6419 -0.1993 0.2074 0.0822 8 LYS A C 51 O O . LYS A 8 ? 0.7631 0.6811 0.7211 -0.1842 0.2237 0.0758 8 LYS A O 52 C CB . LYS A 8 ? 0.7882 0.7225 0.7578 -0.2187 0.2357 0.1103 8 LYS A CB 53 C CG . LYS A 8 ? 0.8766 0.8548 0.9134 -0.2078 0.2508 0.1226 8 LYS A CG 54 C CD . LYS A 8 ? 0.9906 0.9794 1.0404 -0.2006 0.2956 0.1343 8 LYS A CD 55 C CE . LYS A 8 ? 0.9570 1.0028 1.0885 -0.1945 0.3056 0.1563 8 LYS A CE 56 N NZ . LYS A 8 ? 0.8364 0.9020 1.0017 -0.1763 0.2985 0.1538 8 LYS A NZ 57 N N . LEU A 9 ? 0.6427 0.5659 0.6076 -0.2071 0.1736 0.0832 9 LEU A N 58 C CA . LEU A 9 ? 0.6082 0.5436 0.5971 -0.1986 0.1528 0.0769 9 LEU A CA 59 C C . LEU A 9 ? 0.5843 0.4960 0.5392 -0.1861 0.1556 0.0594 9 LEU A C 60 O O . LEU A 9 ? 0.5739 0.4965 0.5502 -0.1724 0.1630 0.0565 9 LEU A O 61 C CB . LEU A 9 ? 0.6621 0.5933 0.6516 -0.2103 0.1175 0.0766 9 LEU A CB 62 C CG . LEU A 9 ? 0.6678 0.6080 0.6752 -0.2027 0.0962 0.0697 9 LEU A CG 63 C CD1 . LEU A 9 ? 0.5426 0.5250 0.6068 -0.1988 0.1015 0.0822 9 LEU A CD1 64 C CD2 . LEU A 9 ? 0.6740 0.5980 0.6682 -0.2128 0.0656 0.0658 9 LEU A CD2 65 N N . PHE A 10 ? 0.7033 0.5835 0.6055 -0.1915 0.1500 0.0491 10 PHE A N 66 C CA . PHE A 10 ? 0.6961 0.5542 0.5634 -0.1845 0.1496 0.0326 10 PHE A CA 67 C C . PHE A 10 ? 0.6920 0.5429 0.5529 -0.1749 0.1835 0.0272 10 PHE A C 68 O O . PHE A 10 ? 0.7451 0.5913 0.6089 -0.1642 0.1870 0.0179 10 PHE A O 69 C CB . PHE A 10 ? 0.7558 0.5876 0.5692 -0.1944 0.1384 0.0262 10 PHE A CB 70 C CG . PHE A 10 ? 0.8501 0.6632 0.6294 -0.1913 0.1364 0.0102 10 PHE A CG 71 C CD1 . PHE A 10 ? 0.8526 0.6464 0.5988 -0.1917 0.1629 0.0009 10 PHE A CD1 72 C CD2 . PHE A 10 ? 0.7833 0.5963 0.5630 -0.1888 0.1099 0.0043 10 PHE A CD2 73 C CE1 . PHE A 10 ? 0.9154 0.6901 0.6286 -0.1927 0.1605 -0.0147 10 PHE A CE1 74 C CE2 . PHE A 10 ? 0.7983 0.5971 0.5500 -0.1881 0.1079 -0.0095 10 PHE A CE2 75 C CZ . PHE A 10 ? 0.8150 0.5950 0.5338 -0.1913 0.1317 -0.0191 10 PHE A CZ 76 N N . ASN A 11 ? 0.7227 0.5679 0.5707 -0.1785 0.2109 0.0329 11 ASN A N 77 C CA . ASN A 11 ? 0.8611 0.6937 0.7004 -0.1682 0.2491 0.0282 11 ASN A CA 78 C C . ASN A 11 ? 0.7770 0.6388 0.6772 -0.1506 0.2599 0.0372 11 ASN A C 79 O O . ASN A 11 ? 0.7758 0.6242 0.6727 -0.1372 0.2788 0.0293 11 ASN A O 80 C CB . ASN A 11 ? 0.7626 0.5869 0.5822 -0.1746 0.2783 0.0357 11 ASN A CB 81 C CG . ASN A 11 ? 1.0093 0.7973 0.7558 -0.1898 0.2758 0.0246 11 ASN A CG 82 O OD1 . ASN A 11 ? 1.1380 0.9025 0.8443 -0.1932 0.2644 0.0085 11 ASN A OD1 83 N ND2 . ASN A 11 ? 1.0050 0.7902 0.7338 -0.2003 0.2861 0.0348 11 ASN A ND2 84 N N . ASP A 12 ? 0.7199 0.6214 0.6750 -0.1519 0.2465 0.0549 12 ASP A N 85 C CA . ASP A 12 ? 0.6469 0.5852 0.6645 -0.1371 0.2515 0.0680 12 ASP A CA 86 C C . ASP A 12 ? 0.6841 0.6222 0.7087 -0.1285 0.2291 0.0592 12 ASP A C 87 O O . ASP A 12 ? 0.5994 0.5482 0.6521 -0.1109 0.2441 0.0635 12 ASP A O 88 C CB . ASP A 12 ? 0.5799 0.5624 0.6506 -0.1467 0.2368 0.0888 12 ASP A CB 89 C CG . ASP A 12 ? 0.7617 0.7554 0.8442 -0.1505 0.2670 0.1033 12 ASP A CG 90 O OD1 . ASP A 12 ? 0.7116 0.6864 0.7753 -0.1390 0.3045 0.1001 12 ASP A OD1 91 O OD2 . ASP A 12 ? 0.8084 0.8267 0.9167 -0.1656 0.2553 0.1174 12 ASP A OD2 92 N N . LEU A 13 ? 0.6040 0.5296 0.6037 -0.1394 0.1952 0.0487 13 LEU A N 93 C CA . LEU A 13 ? 0.5696 0.4971 0.5773 -0.1324 0.1734 0.0421 13 LEU A CA 94 C C . LEU A 13 ? 0.5679 0.4634 0.5424 -0.1218 0.1912 0.0265 13 LEU A C 95 O O . LEU A 13 ? 0.5625 0.4617 0.5544 -0.1085 0.1919 0.0255 13 LEU A O 96 C CB . LEU A 13 ? 0.5095 0.4275 0.4957 -0.1454 0.1371 0.0347 13 LEU A CB 97 C CG . LEU A 13 ? 0.5550 0.4969 0.5701 -0.1575 0.1135 0.0469 13 LEU A CG 98 C CD1 . LEU A 13 ? 0.6127 0.5311 0.5935 -0.1679 0.0871 0.0377 13 LEU A CD1 99 C CD2 . LEU A 13 ? 0.5674 0.5413 0.6285 -0.1517 0.1001 0.0560 13 LEU A CD2 100 N N . PHE A 14 ? 0.5789 0.4408 0.5017 -0.1298 0.2045 0.0143 14 PHE A N 101 C CA . PHE A 14 ? 0.6893 0.5161 0.5717 -0.1266 0.2154 -0.0034 14 PHE A CA 102 C C . PHE A 14 ? 0.7293 0.5328 0.5970 -0.1172 0.2598 -0.0067 14 PHE A C 103 O O . PHE A 14 ? 0.7381 0.5055 0.5650 -0.1180 0.2720 -0.0229 14 PHE A O 104 C CB . PHE A 14 ? 0.6987 0.5022 0.5284 -0.1437 0.1938 -0.0170 14 PHE A CB 105 C CG . PHE A 14 ? 0.6499 0.4694 0.4933 -0.1475 0.1549 -0.0153 14 PHE A CG 106 C CD1 . PHE A 14 ? 0.6761 0.4923 0.5223 -0.1414 0.1412 -0.0233 14 PHE A CD1 107 C CD2 . PHE A 14 ? 0.6930 0.5269 0.5449 -0.1565 0.1349 -0.0056 14 PHE A CD2 108 C CE1 . PHE A 14 ? 0.6239 0.4513 0.4803 -0.1433 0.1098 -0.0221 14 PHE A CE1 109 C CE2 . PHE A 14 ? 0.6297 0.4714 0.4909 -0.1584 0.1033 -0.0048 14 PHE A CE2 110 C CZ . PHE A 14 ? 0.6543 0.4932 0.5177 -0.1512 0.0914 -0.0132 14 PHE A CZ 111 N N . GLU A 15 ? 0.6548 0.4777 0.5568 -0.1080 0.2857 0.0090 15 GLU A N 112 C CA . GLU A 15 ? 0.7021 0.4999 0.5922 -0.0953 0.3330 0.0072 15 GLU A CA 113 C C . GLU A 15 ? 0.7313 0.5141 0.6315 -0.0765 0.3479 0.0024 15 GLU A C 114 O O . GLU A 15 ? 0.9067 0.6450 0.7683 -0.0715 0.3817 -0.0104 15 GLU A O 115 C CB . GLU A 15 ? 0.8436 0.6745 0.7826 -0.0852 0.3579 0.0298 15 GLU A CB 116 C CG . GLU A 15 ? 0.8690 0.7540 0.8876 -0.0698 0.3473 0.0525 15 GLU A CG 117 C CD . GLU A 15 ? 1.1366 1.0488 1.2050 -0.0520 0.3863 0.0752 15 GLU A CD 118 O OE1 . GLU A 15 ? 1.2209 1.1608 1.3113 -0.0607 0.3887 0.0894 15 GLU A OE1 119 O OE2 . GLU A 15 ? 1.2030 1.1089 1.2901 -0.0287 0.4160 0.0801 15 GLU A OE2 120 N N . ASP A 16 ? 0.7530 0.5691 0.7014 -0.0667 0.3244 0.0128 16 ASP A N 121 C CA . ASP A 16 ? 0.7627 0.5642 0.7192 -0.0493 0.3357 0.0098 16 ASP A CA 122 C C . ASP A 16 ? 0.7811 0.6048 0.7536 -0.0543 0.2911 0.0094 16 ASP A C 123 O O . ASP A 16 ? 0.7340 0.6033 0.7601 -0.0479 0.2725 0.0280 16 ASP A O 124 C CB . ASP A 16 ? 0.8107 0.6381 0.8258 -0.0226 0.3674 0.0330 16 ASP A CB 125 C CG . ASP A 16 ? 0.9361 0.7367 0.9520 -0.0017 0.3898 0.0305 16 ASP A CG 126 O OD1 . ASP A 16 ? 1.0268 0.8094 1.0198 -0.0075 0.3676 0.0168 16 ASP A OD1 127 O OD2 . ASP A 16 ? 1.0162 0.8120 1.0555 0.0212 0.4316 0.0431 16 ASP A OD2 128 N N . TYR A 17 ? 0.6450 0.4378 0.5697 -0.0679 0.2734 -0.0110 17 TYR A N 129 C CA . TYR A 17 ? 0.6484 0.4582 0.5813 -0.0741 0.2319 -0.0129 17 TYR A CA 130 C C . TYR A 17 ? 0.7160 0.4874 0.6007 -0.0827 0.2273 -0.0338 17 TYR A C 131 O O . TYR A 17 ? 0.7040 0.4444 0.5394 -0.0972 0.2360 -0.0483 17 TYR A O 132 C CB . TYR A 17 ? 0.5963 0.4288 0.5304 -0.0908 0.1998 -0.0096 17 TYR A CB 133 C CG . TYR A 17 ? 0.6010 0.4419 0.5361 -0.0958 0.1624 -0.0136 17 TYR A CG 134 C CD1 . TYR A 17 ? 0.5704 0.4431 0.5484 -0.0880 0.1440 -0.0007 17 TYR A CD1 135 C CD2 . TYR A 17 ? 0.5850 0.4022 0.4775 -0.1080 0.1472 -0.0293 17 TYR A CD2 136 C CE1 . TYR A 17 ? 0.5012 0.3762 0.4757 -0.0912 0.1140 -0.0053 17 TYR A CE1 137 C CE2 . TYR A 17 ? 0.5759 0.3999 0.4712 -0.1098 0.1182 -0.0318 17 TYR A CE2 138 C CZ . TYR A 17 ? 0.5261 0.3764 0.4607 -0.1009 0.1028 -0.0205 17 TYR A CZ 139 O OH . TYR A 17 ? 0.5392 0.3925 0.4731 -0.1019 0.0770 -0.0233 17 TYR A OH 140 N N . SER A 18 ? 0.6089 0.3829 0.5062 -0.0755 0.2134 -0.0347 18 SER A N 141 C CA . SER A 18 ? 0.6377 0.3770 0.4932 -0.0844 0.2111 -0.0532 18 SER A CA 142 C C . SER A 18 ? 0.6051 0.3620 0.4637 -0.0922 0.1728 -0.0548 18 SER A C 143 O O . SER A 18 ? 0.5762 0.3588 0.4710 -0.0815 0.1569 -0.0438 18 SER A O 144 C CB . SER A 18 ? 0.6943 0.4111 0.5554 -0.0682 0.2358 -0.0542 18 SER A CB 145 O OG . SER A 18 ? 0.7855 0.4760 0.6136 -0.0789 0.2267 -0.0700 18 SER A OG 146 N N . ASN A 19 ? 0.6613 0.4050 0.4817 -0.1107 0.1580 -0.0673 19 ASN A N 147 C CA . ASN A 19 ? 0.6151 0.3736 0.4395 -0.1153 0.1256 -0.0678 19 ASN A CA 148 C C . ASN A 19 ? 0.6662 0.4129 0.4903 -0.1101 0.1249 -0.0738 19 ASN A C 149 O O . ASN A 19 ? 0.6210 0.3777 0.4474 -0.1128 0.1021 -0.0745 19 ASN A O 150 C CB . ASN A 19 ? 0.6409 0.3962 0.4318 -0.1344 0.1090 -0.0745 19 ASN A CB 151 C CG . ASN A 19 ? 0.7910 0.5165 0.5375 -0.1494 0.1199 -0.0896 19 ASN A CG 152 O OD1 . ASN A 19 ? 0.8300 0.5310 0.5678 -0.1458 0.1420 -0.0972 19 ASN A OD1 153 N ND2 . ASN A 19 ? 0.7804 0.5063 0.4964 -0.1675 0.1056 -0.0931 19 ASN A ND2 154 N N . ALA A 20 ? 0.6593 0.3833 0.4814 -0.1013 0.1521 -0.0768 20 ALA A N 155 C CA . ALA A 20 ? 0.6877 0.3966 0.5087 -0.0961 0.1549 -0.0813 20 ALA A CA 156 C C . ALA A 20 ? 0.6893 0.4164 0.5533 -0.0732 0.1570 -0.0657 20 ALA A C 157 O O . ALA A 20 ? 0.7209 0.4420 0.5895 -0.0668 0.1546 -0.0655 20 ALA A O 158 C CB . ALA A 20 ? 0.7174 0.3817 0.5015 -0.1035 0.1841 -0.0955 20 ALA A CB 159 N N . LEU A 21 ? 0.5900 0.3417 0.4857 -0.0620 0.1607 -0.0511 21 LEU A N 160 C CA . LEU A 21 ? 0.5571 0.3319 0.4955 -0.0415 0.1621 -0.0329 21 LEU A CA 161 C C . LEU A 21 ? 0.5531 0.3642 0.5145 -0.0430 0.1281 -0.0232 21 LEU A C 162 O O . LEU A 21 ? 0.5112 0.3423 0.4789 -0.0520 0.1140 -0.0201 21 LEU A O 163 C CB . LEU A 21 ? 0.6473 0.4325 0.6122 -0.0283 0.1875 -0.0192 21 LEU A CB 164 C CG . LEU A 21 ? 0.6910 0.5054 0.7053 -0.0054 0.1924 0.0045 21 LEU A CG 165 C CD1 . LEU A 21 ? 0.7036 0.4903 0.7148 0.0105 0.2134 0.0053 21 LEU A CD1 166 C CD2 . LEU A 21 ? 0.7717 0.6099 0.8204 0.0051 0.2122 0.0215 21 LEU A CD2 167 N N . ARG A 22 ? 0.5607 0.3779 0.5330 -0.0345 0.1166 -0.0180 22 ARG A N 168 C CA . ARG A 22 ? 0.4904 0.3360 0.4781 -0.0365 0.0858 -0.0099 22 ARG A CA 169 C C . ARG A 22 ? 0.4199 0.3001 0.4427 -0.0332 0.0819 0.0073 22 ARG A C 170 O O . ARG A 22 ? 0.4736 0.3684 0.5261 -0.0184 0.0977 0.0228 22 ARG A O 171 C CB . ARG A 22 ? 0.5261 0.3708 0.5181 -0.0262 0.0790 -0.0049 22 ARG A CB 172 C CG . ARG A 22 ? 0.4641 0.3251 0.4554 -0.0319 0.0486 -0.0028 22 ARG A CG 173 C CD . ARG A 22 ? 0.4826 0.3346 0.4677 -0.0231 0.0451 -0.0011 22 ARG A CD 174 N NE . ARG A 22 ? 0.4822 0.3404 0.4908 -0.0060 0.0618 0.0143 22 ARG A NE 175 C CZ . ARG A 22 ? 0.4273 0.3150 0.4625 0.0030 0.0514 0.0339 22 ARG A CZ 176 N NH1 . ARG A 22 ? 0.4555 0.3647 0.4912 -0.0063 0.0231 0.0378 22 ARG A NH1 177 N NH2 . ARG A 22 ? 0.4429 0.3371 0.5027 0.0209 0.0699 0.0503 22 ARG A NH2 178 N N . PRO A 23 ? 0.4299 0.3242 0.4513 -0.0470 0.0620 0.0064 23 PRO A N 179 C CA . PRO A 23 ? 0.4886 0.4137 0.5414 -0.0485 0.0621 0.0212 23 PRO A CA 180 C C . PRO A 23 ? 0.4936 0.4550 0.5795 -0.0456 0.0429 0.0396 23 PRO A C 181 O O . PRO A 23 ? 0.4474 0.4253 0.5367 -0.0597 0.0197 0.0424 23 PRO A O 182 C CB . PRO A 23 ? 0.5030 0.4217 0.5353 -0.0667 0.0504 0.0116 23 PRO A CB 183 C CG . PRO A 23 ? 0.4492 0.3465 0.4495 -0.0731 0.0325 -0.0024 23 PRO A CG 184 C CD . PRO A 23 ? 0.4445 0.3235 0.4349 -0.0618 0.0447 -0.0082 23 PRO A CD 185 N N . VAL A 24 ? 0.4338 0.4067 0.5425 -0.0284 0.0528 0.0530 24 VAL A N 186 C CA . VAL A 24 ? 0.3789 0.3926 0.5224 -0.0249 0.0351 0.0748 24 VAL A CA 187 C C . VAL A 24 ? 0.4959 0.5392 0.6853 -0.0082 0.0578 0.0975 24 VAL A C 188 O O . VAL A 24 ? 0.4834 0.5043 0.6706 0.0060 0.0898 0.0945 24 VAL A O 189 C CB . VAL A 24 ? 0.3984 0.4047 0.5297 -0.0176 0.0225 0.0757 24 VAL A CB 190 C CG1 . VAL A 24 ? 0.4839 0.4623 0.5724 -0.0323 0.0030 0.0549 24 VAL A CG1 191 C CG2 . VAL A 24 ? 0.4315 0.4135 0.5599 0.0027 0.0506 0.0753 24 VAL A CG2 192 N N . GLU A 25 ? 0.4895 0.5824 0.7198 -0.0107 0.0418 0.1208 25 GLU A N 193 C CA . GLU A 25 ? 0.6066 0.7382 0.8902 0.0055 0.0620 0.1475 25 GLU A CA 194 C C . GLU A 25 ? 0.6092 0.7420 0.9095 0.0320 0.0767 0.1630 25 GLU A C 195 O O . GLU A 25 ? 0.6932 0.8331 1.0243 0.0541 0.1085 0.1787 25 GLU A O 196 C CB . GLU A 25 ? 0.6530 0.8434 0.9771 -0.0092 0.0354 0.1694 25 GLU A CB 197 C CG . GLU A 25 ? 0.7811 0.9673 1.0867 -0.0378 0.0186 0.1550 25 GLU A CG 198 C CD . GLU A 25 ? 0.8923 1.0549 1.1528 -0.0592 -0.0154 0.1361 25 GLU A CD 199 O OE1 . GLU A 25 ? 0.7341 0.8704 0.9655 -0.0520 -0.0210 0.1260 25 GLU A OE1 200 O OE2 . GLU A 25 ? 0.9596 1.1276 1.2130 -0.0832 -0.0344 0.1315 25 GLU A OE2 201 N N . ASP A 26 ? 0.3988 0.5207 0.6762 0.0307 0.0559 0.1586 26 ASP A N 202 C CA . ASP A 26 ? 0.4806 0.6023 0.7707 0.0548 0.0669 0.1747 26 ASP A CA 203 C C . ASP A 26 ? 0.6025 0.6719 0.8409 0.0536 0.0661 0.1508 26 ASP A C 204 O O . ASP A 26 ? 0.4764 0.5339 0.6811 0.0345 0.0399 0.1339 26 ASP A O 205 C CB . ASP A 26 ? 0.6336 0.8137 0.9612 0.0551 0.0380 0.2053 26 ASP A CB 206 C CG . ASP A 26 ? 0.8340 1.0081 1.1565 0.0726 0.0357 0.2172 26 ASP A CG 207 O OD1 . ASP A 26 ? 0.8743 1.0005 1.1724 0.0877 0.0616 0.2049 26 ASP A OD1 208 O OD2 . ASP A 26 ? 0.7931 1.0106 1.1347 0.0694 0.0072 0.2398 26 ASP A OD2 209 N N . THR A 27 ? 0.5184 0.5547 0.7503 0.0739 0.0964 0.1499 27 THR A N 210 C CA . THR A 27 ? 0.6467 0.6301 0.8287 0.0687 0.1002 0.1239 27 THR A CA 211 C C . THR A 27 ? 0.4418 0.4290 0.6070 0.0646 0.0718 0.1258 27 THR A C 212 O O . THR A 27 ? 0.5200 0.4756 0.6450 0.0523 0.0634 0.1034 27 THR A O 213 C CB . THR A 27 ? 0.7131 0.6540 0.8875 0.0877 0.1410 0.1207 27 THR A CB 214 O OG1 . THR A 27 ? 0.6795 0.6449 0.8973 0.1140 0.1570 0.1521 27 THR A OG1 215 C CG2 . THR A 27 ? 0.7597 0.6747 0.9211 0.0818 0.1669 0.1037 27 THR A CG2 216 N N . ASP A 28 ? 0.4295 0.4563 0.6242 0.0742 0.0570 0.1533 28 ASP A N 217 C CA . ASP A 28 ? 0.5571 0.5818 0.7286 0.0703 0.0329 0.1545 28 ASP A CA 218 C C . ASP A 28 ? 0.5413 0.5828 0.6947 0.0443 -0.0038 0.1451 28 ASP A C 219 O O . ASP A 28 ? 0.6985 0.7403 0.8295 0.0379 -0.0264 0.1460 28 ASP A O 220 C CB . ASP A 28 ? 0.6602 0.7146 0.8619 0.0910 0.0316 0.1880 28 ASP A CB 221 C CG . ASP A 28 ? 0.8758 0.9929 1.1292 0.0937 0.0193 0.2181 28 ASP A CG 222 O OD1 . ASP A 28 ? 0.9423 1.0860 1.1966 0.0707 -0.0074 0.2140 28 ASP A OD1 223 O OD2 . ASP A 28 ? 0.9569 1.0968 1.2514 0.1187 0.0371 0.2475 28 ASP A OD2 224 N N . LYS A 29 ? 0.4568 0.5088 0.6171 0.0294 -0.0081 0.1366 29 LYS A N 225 C CA . LYS A 29 ? 0.4775 0.5327 0.6138 0.0036 -0.0384 0.1237 29 LYS A CA 226 C C . LYS A 29 ? 0.5276 0.5343 0.6175 -0.0051 -0.0349 0.0935 29 LYS A C 227 O O . LYS A 29 ? 0.5251 0.5038 0.6072 0.0010 -0.0109 0.0803 29 LYS A O 228 C CB . LYS A 29 ? 0.4762 0.5610 0.6385 -0.0102 -0.0445 0.1280 29 LYS A CB 229 C CG . LYS A 29 ? 0.6283 0.7718 0.8424 -0.0056 -0.0528 0.1609 29 LYS A CG 230 C CD . LYS A 29 ? 0.7424 0.9096 0.9568 -0.0038 -0.0768 0.1797 29 LYS A CD 231 C CE . LYS A 29 ? 0.8380 1.0042 1.0173 -0.0328 -0.1132 0.1691 29 LYS A CE 232 N NZ . LYS A 29 ? 0.7819 0.9616 0.9475 -0.0333 -0.1361 0.1834 29 LYS A NZ 233 N N . VAL A 30 ? 0.5083 0.5048 0.5660 -0.0202 -0.0586 0.0832 30 VAL A N 234 C CA . VAL A 30 ? 0.4638 0.4193 0.4823 -0.0269 -0.0554 0.0580 30 VAL A CA 235 C C . VAL A 30 ? 0.4791 0.4317 0.4948 -0.0423 -0.0586 0.0461 30 VAL A C 236 O O . VAL A 30 ? 0.5870 0.5660 0.6213 -0.0528 -0.0708 0.0553 30 VAL A O 237 C CB . VAL A 30 ? 0.5623 0.5034 0.5451 -0.0345 -0.0754 0.0523 30 VAL A CB 238 C CG1 . VAL A 30 ? 0.6118 0.5693 0.5886 -0.0543 -0.1020 0.0550 30 VAL A CG1 239 C CG2 . VAL A 30 ? 0.5773 0.4788 0.5260 -0.0359 -0.0671 0.0302 30 VAL A CG2 240 N N . LEU A 31 ? 0.4233 0.3435 0.4315 0.0227 0.0225 -0.0006 31 LEU A N 241 C CA . LEU A 31 ? 0.4305 0.3536 0.4364 0.0151 0.0144 -0.0011 31 LEU A CA 242 C C . LEU A 31 ? 0.3971 0.3168 0.3894 0.0177 0.0031 -0.0033 31 LEU A C 243 O O . LEU A 31 ? 0.4681 0.3859 0.4500 0.0182 0.0078 -0.0070 31 LEU A O 244 C CB . LEU A 31 ? 0.4136 0.3380 0.4164 0.0046 0.0265 -0.0037 31 LEU A CB 245 C CG . LEU A 31 ? 0.4938 0.4199 0.4920 -0.0043 0.0207 -0.0030 31 LEU A CG 246 C CD1 . LEU A 31 ? 0.5173 0.4448 0.5140 -0.0136 0.0347 -0.0048 31 LEU A CD1 247 C CD2 . LEU A 31 ? 0.4571 0.3813 0.4404 -0.0044 0.0116 -0.0052 31 LEU A CD2 248 N N . ASN A 32 ? 0.4089 0.3278 0.4025 0.0191 -0.0112 -0.0015 32 ASN A N 249 C CA . ASN A 32 ? 0.3906 0.3051 0.3728 0.0230 -0.0221 -0.0036 32 ASN A CA 250 C C . ASN A 32 ? 0.4737 0.3876 0.4496 0.0166 -0.0257 -0.0041 32 ASN A C 251 O O . ASN A 32 ? 0.4919 0.4065 0.4728 0.0092 -0.0264 -0.0012 32 ASN A O 252 C CB . ASN A 32 ? 0.4470 0.3584 0.4325 0.0280 -0.0361 -0.0020 32 ASN A CB 253 C CG . ASN A 32 ? 0.5412 0.4537 0.5316 0.0357 -0.0361 -0.0005 32 ASN A CG 254 O OD1 . ASN A 32 ? 0.5009 0.4115 0.4845 0.0415 -0.0291 -0.0014 32 ASN A OD1 255 N ND2 . ASN A 32 ? 0.5969 0.5127 0.5994 0.0356 -0.0441 0.0021 32 ASN A ND2 256 N N . VAL A 33 ? 0.4088 0.3217 0.3740 0.0196 -0.0278 -0.0073 33 VAL A N 257 C CA . VAL A 33 ? 0.3882 0.3013 0.3466 0.0159 -0.0325 -0.0074 33 VAL A CA 258 C C . VAL A 33 ? 0.4603 0.3685 0.4123 0.0241 -0.0433 -0.0091 33 VAL A C 259 O O . VAL A 33 ? 0.4792 0.3879 0.4277 0.0311 -0.0418 -0.0126 33 VAL A O 260 C CB . VAL A 33 ? 0.3960 0.3164 0.3491 0.0116 -0.0231 -0.0106 33 VAL A CB 261 C CG1 . VAL A 33 ? 0.4592 0.3815 0.4052 0.0077 -0.0295 -0.0093 33 VAL A CG1 262 C CG2 . VAL A 33 ? 0.5050 0.4284 0.4626 0.0045 -0.0099 -0.0108 33 VAL A CG2 263 N N . THR A 34 ? 0.4495 0.3514 0.3992 0.0234 -0.0533 -0.0067 34 THR A N 264 C CA . THR A 34 ? 0.4041 0.3001 0.3473 0.0315 -0.0625 -0.0088 34 THR A CA 265 C C . THR A 34 ? 0.5512 0.4521 0.4894 0.0311 -0.0632 -0.0086 34 THR A C 266 O O . THR A 34 ? 0.5109 0.4149 0.4482 0.0234 -0.0614 -0.0051 34 THR A O 267 C CB . THR A 34 ? 0.5327 0.4155 0.4762 0.0327 -0.0742 -0.0069 34 THR A CB 268 O OG1 . THR A 34 ? 0.5587 0.4375 0.5019 0.0258 -0.0770 -0.0018 34 THR A OG1 269 C CG2 . THR A 34 ? 0.5168 0.3983 0.4678 0.0313 -0.0748 -0.0067 34 THR A CG2 270 N N . LEU A 35 ? 0.4442 0.3469 0.3789 0.0397 -0.0656 -0.0124 35 LEU A N 271 C CA . LEU A 35 ? 0.4732 0.3844 0.4058 0.0408 -0.0669 -0.0127 35 LEU A CA 272 C C . LEU A 35 ? 0.4776 0.3803 0.4071 0.0507 -0.0770 -0.0128 35 LEU A C 273 O O . LEU A 35 ? 0.4872 0.3827 0.4154 0.0583 -0.0790 -0.0165 35 LEU A O 274 C CB . LEU A 35 ? 0.4474 0.3727 0.3820 0.0414 -0.0574 -0.0180 35 LEU A CB 275 C CG . LEU A 35 ? 0.6874 0.6278 0.6228 0.0392 -0.0568 -0.0191 35 LEU A CG 276 C CD1 . LEU A 35 ? 0.7634 0.7169 0.7024 0.0377 -0.0463 -0.0252 35 LEU A CD1 277 C CD2 . LEU A 35 ? 0.8512 0.7914 0.7862 0.0485 -0.0671 -0.0182 35 LEU A CD2 278 N N . GLN A 36 ? 0.4861 0.3883 0.4134 0.0508 -0.0834 -0.0086 36 GLN A N 279 C CA . GLN A 36 ? 0.5139 0.4086 0.4391 0.0615 -0.0922 -0.0084 36 GLN A CA 280 C C . GLN A 36 ? 0.5921 0.5025 0.5190 0.0640 -0.0935 -0.0074 36 GLN A C 281 O O . GLN A 36 ? 0.5301 0.4492 0.4552 0.0556 -0.0926 -0.0034 36 GLN A O 282 C CB . GLN A 36 ? 0.4839 0.3587 0.4045 0.0603 -0.1007 -0.0025 36 GLN A CB 283 C CG . GLN A 36 ? 0.5747 0.4397 0.4924 0.0709 -0.1095 -0.0006 36 GLN A CG 284 C CD . GLN A 36 ? 0.6876 0.5300 0.6002 0.0681 -0.1163 0.0050 36 GLN A CD 285 O OE1 . GLN A 36 ? 0.7413 0.5741 0.6543 0.0611 -0.1153 0.0043 36 GLN A OE1 286 N NE2 . GLN A 36 ? 0.7557 0.5892 0.6640 0.0733 -0.1232 0.0111 36 GLN A NE2 287 N N . ILE A 37 ? 0.5370 0.4524 0.4675 0.0755 -0.0955 -0.0114 37 ILE A N 288 C CA . ILE A 37 ? 0.5400 0.4736 0.4755 0.0792 -0.0979 -0.0107 37 ILE A CA 289 C C . ILE A 37 ? 0.5473 0.4692 0.4813 0.0907 -0.1082 -0.0067 37 ILE A C 290 O O . ILE A 37 ? 0.5712 0.4782 0.5042 0.0997 -0.1097 -0.0098 37 ILE A O 291 C CB . ILE A 37 ? 0.5940 0.5465 0.5385 0.0837 -0.0906 -0.0186 37 ILE A CB 292 C CG1 . ILE A 37 ? 0.6207 0.5837 0.5664 0.0721 -0.0792 -0.0225 37 ILE A CG1 293 C CG2 . ILE A 37 ? 0.6483 0.6207 0.6008 0.0890 -0.0954 -0.0179 37 ILE A CG2 294 C CD1 . ILE A 37 ? 0.7447 0.7208 0.6899 0.0606 -0.0780 -0.0203 37 ILE A CD1 295 N N . THR A 38 ? 0.5517 0.4789 0.4842 0.0906 -0.1153 0.0003 38 THR A N 296 C CA . THR A 38 ? 0.5122 0.4297 0.4441 0.1031 -0.1252 0.0054 38 THR A CA 297 C C . THR A 38 ? 0.6426 0.5866 0.5844 0.1098 -0.1280 0.0049 38 THR A C 298 O O . THR A 38 ? 0.6249 0.5874 0.5666 0.1014 -0.1286 0.0071 38 THR A O 299 C CB . THR A 38 ? 0.6153 0.5142 0.5356 0.0981 -0.1323 0.0161 38 THR A CB 300 O OG1 . THR A 38 ? 0.6628 0.5388 0.5771 0.0915 -0.1296 0.0159 38 THR A OG1 301 C CG2 . THR A 38 ? 0.6528 0.5409 0.5719 0.1120 -0.1426 0.0228 38 THR A CG2 302 N N . LEU A 39 ? 0.5384 0.4860 0.4895 0.1246 -0.1295 0.0011 39 LEU A N 303 C CA . LEU A 39 ? 0.5114 0.4880 0.4759 0.1313 -0.1322 0.0002 39 LEU A CA 304 C C . LEU A 39 ? 0.6381 0.6107 0.5987 0.1382 -0.1453 0.0114 39 LEU A C 305 O O . LEU A 39 ? 0.6768 0.6231 0.6308 0.1471 -0.1508 0.0166 39 LEU A O 306 C CB . LEU A 39 ? 0.4961 0.4786 0.4734 0.1454 -0.1277 -0.0078 39 LEU A CB 307 C CG . LEU A 39 ? 0.5422 0.5527 0.5371 0.1570 -0.1322 -0.0080 39 LEU A CG 308 C CD1 . LEU A 39 ? 0.5458 0.5907 0.5519 0.1466 -0.1269 -0.0131 39 LEU A CD1 309 C CD2 . LEU A 39 ? 0.5882 0.5947 0.5930 0.1742 -0.1282 -0.0143 39 LEU A CD2 310 N N . SER A 40 ? 0.6118 0.6089 0.5753 0.1338 -0.1506 0.0151 40 SER A N 311 C CA . SER A 40 ? 0.6534 0.6478 0.6113 0.1410 -0.1639 0.0270 40 SER A CA 312 C C . SER A 40 ? 0.6588 0.6782 0.6345 0.1567 -0.1712 0.0272 40 SER A C 313 O O . SER A 40 ? 0.7068 0.7171 0.6816 0.1707 -0.1817 0.0363 40 SER A O 314 C CB . SER A 40 ? 0.7050 0.7081 0.6501 0.1258 -0.1674 0.0330 40 SER A CB 315 O OG . SER A 40 ? 0.8373 0.8203 0.7685 0.1113 -0.1595 0.0325 40 SER A OG 316 N N . GLN A 41 ? 0.5686 0.6199 0.5614 0.1545 -0.1654 0.0175 41 GLN A N 317 C CA . GLN A 41 ? 0.6003 0.6817 0.6140 0.1680 -0.1717 0.0168 41 GLN A CA 318 C C . GLN A 41 ? 0.5992 0.7110 0.6325 0.1635 -0.1609 0.0038 41 GLN A C 319 O O . GLN A 41 ? 0.5720 0.6900 0.6010 0.1464 -0.1521 -0.0025 41 GLN A O 320 C CB . GLN A 41 ? 0.5842 0.6844 0.5942 0.1652 -0.1855 0.0260 41 GLN A CB 321 C CG . GLN A 41 ? 0.6689 0.8100 0.7030 0.1748 -0.1928 0.0241 41 GLN A CG 322 C CD . GLN A 41 ? 0.6753 0.8309 0.7021 0.1745 -0.2095 0.0354 41 GLN A CD 323 O OE1 . GLN A 41 ? 0.6875 0.8240 0.6894 0.1640 -0.2133 0.0432 41 GLN A OE1 324 N NE2 . GLN A 41 ? 0.6252 0.8153 0.6734 0.1861 -0.2195 0.0363 41 GLN A NE2 325 N N . ILE A 42 ? 0.5559 0.6862 0.6111 0.1789 -0.1608 -0.0001 42 ILE A N 326 C CA . ILE A 42 ? 0.4979 0.6625 0.5744 0.1745 -0.1516 -0.0112 42 ILE A CA 327 C C . ILE A 42 ? 0.4983 0.7015 0.5898 0.1739 -0.1631 -0.0085 42 ILE A C 328 O O . ILE A 42 ? 0.5589 0.7779 0.6673 0.1911 -0.1723 -0.0045 42 ILE A O 329 C CB . ILE A 42 ? 0.5715 0.7391 0.6661 0.1914 -0.1439 -0.0177 42 ILE A CB 330 C CG1 . ILE A 42 ? 0.6404 0.7700 0.7187 0.1924 -0.1332 -0.0214 42 ILE A CG1 331 C CG2 . ILE A 42 ? 0.4740 0.6811 0.5931 0.1865 -0.1347 -0.0282 42 ILE A CG2 332 C CD1 . ILE A 42 ? 0.6047 0.7360 0.6973 0.2074 -0.1230 -0.0297 42 ILE A CD1 333 N N . LYS A 43 ? 0.5004 0.7189 0.5857 0.1545 -0.1635 -0.0105 43 LYS A N 334 C CA . LYS A 43 ? 0.5728 0.8262 0.6674 0.1521 -0.1771 -0.0073 43 LYS A CA 335 C C . LYS A 43 ? 0.4752 0.7712 0.6038 0.1582 -0.1754 -0.0155 43 LYS A C 336 O O . LYS A 43 ? 0.4828 0.8053 0.6279 0.1700 -0.1890 -0.0107 43 LYS A O 337 C CB . LYS A 43 ? 0.4986 0.7567 0.5767 0.1285 -0.1763 -0.0095 43 LYS A CB 338 C CG . LYS A 43 ? 0.5117 0.8018 0.5926 0.1242 -0.1922 -0.0057 43 LYS A CG 339 C CD . LYS A 43 ? 0.6092 0.8876 0.6790 0.1397 -0.2101 0.0099 43 LYS A CD 340 C CE . LYS A 43 ? 0.6793 0.9879 0.7478 0.1359 -0.2276 0.0150 43 LYS A CE 341 N NZ . LYS A 43 ? 0.7331 1.0892 0.8354 0.1428 -0.2339 0.0093 43 LYS A NZ 342 N N . ASP A 44 ? 0.5200 0.8233 0.6596 0.1501 -0.1585 -0.0275 44 ASP A N 343 C CA . ASP A 44 ? 0.4292 0.7743 0.6017 0.1521 -0.1542 -0.0364 44 ASP A CA 344 C C . ASP A 44 ? 0.4410 0.7795 0.6204 0.1491 -0.1331 -0.0470 44 ASP A C 345 O O . ASP A 44 ? 0.4531 0.7728 0.6155 0.1333 -0.1216 -0.0514 44 ASP A O 346 C CB . ASP A 44 ? 0.5025 0.8820 0.6814 0.1331 -0.1589 -0.0411 44 ASP A CB 347 C CG . ASP A 44 ? 0.5754 1.0027 0.7914 0.1347 -0.1571 -0.0496 44 ASP A CG 348 O OD1 . ASP A 44 ? 0.6811 1.1286 0.9189 0.1541 -0.1668 -0.0454 44 ASP A OD1 349 O OD2 . ASP A 44 ? 0.6498 1.0942 0.8742 0.1166 -0.1454 -0.0605 44 ASP A OD2 350 N N . MET A 45 ? 0.4394 0.7926 0.6429 0.1649 -0.1275 -0.0509 45 MET A N 351 C CA . MET A 45 ? 0.4475 0.8030 0.6607 0.1606 -0.1067 -0.0619 45 MET A CA 352 C C . MET A 45 ? 0.4189 0.8251 0.6670 0.1567 -0.1043 -0.0696 45 MET A C 353 O O . MET A 45 ? 0.4129 0.8461 0.6876 0.1728 -0.1106 -0.0688 45 MET A O 354 C CB . MET A 45 ? 0.4705 0.8023 0.6827 0.1801 -0.0986 -0.0622 45 MET A CB 355 C CG . MET A 45 ? 0.3630 0.6981 0.5836 0.1764 -0.0766 -0.0731 45 MET A CG 356 S SD . MET A 45 ? 0.4849 0.7884 0.6754 0.1546 -0.0623 -0.0767 45 MET A SD 357 C CE . MET A 45 ? 0.5444 0.8851 0.7600 0.1404 -0.0445 -0.0883 45 MET A CE 358 N N . ASP A 46 ? 0.3985 0.8175 0.6471 0.1345 -0.0956 -0.0771 46 ASP A N 359 C CA . ASP A 46 ? 0.4012 0.8679 0.6816 0.1250 -0.0924 -0.0857 46 ASP A CA 360 C C . ASP A 46 ? 0.4413 0.9128 0.7372 0.1253 -0.0697 -0.0951 46 ASP A C 361 O O . ASP A 46 ? 0.4609 0.9138 0.7423 0.1104 -0.0536 -0.1003 46 ASP A O 362 C CB . ASP A 46 ? 0.4911 0.9627 0.7596 0.0990 -0.0932 -0.0895 46 ASP A CB 363 C CG . ASP A 46 ? 0.4737 0.9951 0.7732 0.0860 -0.0933 -0.0986 46 ASP A CG 364 O OD1 . ASP A 46 ? 0.3794 0.9296 0.7104 0.0933 -0.0857 -0.1041 46 ASP A OD1 365 O OD2 . ASP A 46 ? 0.6638 1.1953 0.9557 0.0678 -0.1007 -0.1007 46 ASP A OD2 366 N N . GLU A 47 ? 0.4519 0.9469 0.7762 0.1427 -0.0676 -0.0969 47 GLU A N 367 C CA . GLU A 47 ? 0.5538 1.0535 0.8921 0.1438 -0.0449 -0.1056 47 GLU A CA 368 C C . GLU A 47 ? 0.5660 1.1055 0.9306 0.1244 -0.0342 -0.1158 47 GLU A C 369 O O . GLU A 47 ? 0.5684 1.1095 0.9408 0.1200 -0.0130 -0.1231 47 GLU A O 370 C CB . GLU A 47 ? 0.4885 0.9997 0.8490 0.1696 -0.0441 -0.1049 47 GLU A CB 371 C CG . GLU A 47 ? 0.4805 0.9539 0.8187 0.1898 -0.0543 -0.0958 47 GLU A CG 372 C CD . GLU A 47 ? 0.5442 1.0363 0.9093 0.2158 -0.0587 -0.0943 47 GLU A CD 373 O OE1 . GLU A 47 ? 0.6174 1.1312 1.0074 0.2217 -0.0430 -0.1022 47 GLU A OE1 374 O OE2 . GLU A 47 ? 0.6203 1.1051 0.9817 0.2305 -0.0772 -0.0849 47 GLU A OE2 375 N N . ARG A 48 ? 0.6281 1.1997 1.0060 0.1125 -0.0488 -0.1163 48 ARG A N 376 C CA . ARG A 48 ? 0.6001 1.2099 1.0032 0.0918 -0.0401 -0.1268 48 ARG A CA 377 C C . ARG A 48 ? 0.5550 1.1341 0.9295 0.0682 -0.0265 -0.1307 48 ARG A C 378 O O . ARG A 48 ? 0.5469 1.1283 0.9284 0.0559 -0.0056 -0.1387 48 ARG A O 379 C CB . ARG A 48 ? 0.6556 1.3103 1.0809 0.0862 -0.0618 -0.1268 48 ARG A CB 380 C CG . ARG A 48 ? 0.6052 1.2783 1.0458 0.1114 -0.0834 -0.1178 48 ARG A CG 381 C CD . ARG A 48 ? 0.5662 1.2751 1.0486 0.1290 -0.0771 -0.1212 48 ARG A CD 382 N NE . ARG A 48 ? 0.6059 1.3658 1.1262 0.1127 -0.0698 -0.1325 48 ARG A NE 383 C CZ . ARG A 48 ? 0.6441 1.4085 1.1769 0.1018 -0.0446 -0.1424 48 ARG A CZ 384 N NH1 . ARG A 48 ? 0.6690 1.3904 1.1780 0.1063 -0.0246 -0.1423 48 ARG A NH1 385 N NH2 . ARG A 48 ? 0.6435 1.4557 1.2122 0.0858 -0.0392 -0.1525 48 ARG A NH2 386 N N . ASN A 49 ? 0.4928 1.0416 0.8345 0.0629 -0.0377 -0.1245 49 ASN A N 387 C CA . ASN A 49 ? 0.4942 1.0095 0.8067 0.0436 -0.0258 -0.1268 49 ASN A CA 388 C C . ASN A 49 ? 0.4706 0.9358 0.7528 0.0523 -0.0141 -0.1219 49 ASN A C 389 O O . ASN A 49 ? 0.4343 0.8718 0.6948 0.0384 -0.0016 -0.1237 49 ASN A O 390 C CB . ASN A 49 ? 0.4519 0.9619 0.7451 0.0318 -0.0425 -0.1236 49 ASN A CB 391 C CG . ASN A 49 ? 0.6663 1.2228 0.9839 0.0172 -0.0522 -0.1305 49 ASN A CG 392 O OD1 . ASN A 49 ? 0.7336 1.3119 1.0704 0.0012 -0.0388 -0.1410 49 ASN A OD1 393 N ND2 . ASN A 49 ? 0.7010 1.2735 1.0182 0.0225 -0.0756 -0.1248 49 ASN A ND2 394 N N . GLN A 50 ? 0.4342 0.8872 0.7146 0.0752 -0.0189 -0.1157 50 GLN A N 395 C CA . GLN A 50 ? 0.3962 0.8022 0.6466 0.0839 -0.0113 -0.1110 50 GLN A CA 396 C C . GLN A 50 ? 0.4200 0.7928 0.6381 0.0759 -0.0198 -0.1049 50 GLN A C 397 O O . GLN A 50 ? 0.4942 0.8344 0.6888 0.0690 -0.0087 -0.1046 50 GLN A O 398 C CB . GLN A 50 ? 0.4460 0.8414 0.6943 0.0774 0.0133 -0.1174 50 GLN A CB 399 C CG . GLN A 50 ? 0.4596 0.8723 0.7304 0.0929 0.0233 -0.1211 50 GLN A CG 400 C CD . GLN A 50 ? 0.5046 0.8938 0.7636 0.1168 0.0159 -0.1150 50 GLN A CD 401 O OE1 . GLN A 50 ? 0.5017 0.9120 0.7826 0.1337 0.0097 -0.1148 50 GLN A OE1 402 N NE2 . GLN A 50 ? 0.4697 0.8151 0.6947 0.1183 0.0164 -0.1103 50 GLN A NE2 403 N N . ILE A 51 ? 0.3653 0.7474 0.5825 0.0774 -0.0397 -0.0994 51 ILE A N 404 C CA . ILE A 51 ? 0.3390 0.6926 0.5270 0.0703 -0.0484 -0.0932 51 ILE A CA 405 C C . ILE A 51 ? 0.4068 0.7449 0.5845 0.0881 -0.0655 -0.0828 51 ILE A C 406 O O . ILE A 51 ? 0.3622 0.7246 0.5570 0.0995 -0.0794 -0.0796 51 ILE A O 407 C CB . ILE A 51 ? 0.4371 0.8118 0.6267 0.0508 -0.0556 -0.0962 51 ILE A CB 408 C CG1 . ILE A 51 ? 0.4077 0.7977 0.6091 0.0319 -0.0383 -0.1073 51 ILE A CG1 409 C CG2 . ILE A 51 ? 0.4284 0.7726 0.5872 0.0439 -0.0623 -0.0901 51 ILE A CG2 410 C CD1 . ILE A 51 ? 0.5163 0.8704 0.6960 0.0231 -0.0203 -0.1089 51 ILE A CD1 411 N N . LEU A 52 ? 0.3573 0.6549 0.5078 0.0902 -0.0640 -0.0775 52 LEU A N 412 C CA . LEU A 52 ? 0.4630 0.7390 0.5989 0.1032 -0.0786 -0.0675 52 LEU A CA 413 C C . LEU A 52 ? 0.4759 0.7452 0.5941 0.0905 -0.0891 -0.0623 52 LEU A C 414 O O . LEU A 52 ? 0.4375 0.6931 0.5409 0.0748 -0.0807 -0.0650 52 LEU A O 415 C CB . LEU A 52 ? 0.3727 0.6090 0.4894 0.1110 -0.0711 -0.0654 52 LEU A CB 416 C CG . LEU A 52 ? 0.4208 0.6285 0.5184 0.1195 -0.0845 -0.0554 52 LEU A CG 417 C CD1 . LEU A 52 ? 0.4522 0.6689 0.5627 0.1393 -0.0969 -0.0504 52 LEU A CD1 418 C CD2 . LEU A 52 ? 0.4667 0.6359 0.5437 0.1215 -0.0767 -0.0547 52 LEU A CD2 419 N N . THR A 53 ? 0.4019 0.6810 0.5211 0.0978 -0.1068 -0.0549 53 THR A N 420 C CA . THR A 53 ? 0.4053 0.6700 0.5019 0.0892 -0.1172 -0.0477 53 THR A CA 421 C C . THR A 53 ? 0.4344 0.6648 0.5141 0.1034 -0.1245 -0.0372 53 THR A C 422 O O . THR A 53 ? 0.4390 0.6722 0.5274 0.1208 -0.1340 -0.0317 53 THR A O 423 C CB . THR A 53 ? 0.5331 0.8307 0.6378 0.0851 -0.1325 -0.0457 53 THR A CB 424 O OG1 . THR A 53 ? 0.5128 0.8437 0.6359 0.0715 -0.1256 -0.0568 53 THR A OG1 425 C CG2 . THR A 53 ? 0.4783 0.7589 0.5554 0.0745 -0.1411 -0.0387 53 THR A CG2 426 N N . ALA A 54 ? 0.4522 0.6502 0.5089 0.0954 -0.1194 -0.0347 54 ALA A N 427 C CA . ALA A 54 ? 0.5455 0.7092 0.5856 0.1052 -0.1248 -0.0258 54 ALA A CA 428 C C . ALA A 54 ? 0.6167 0.7653 0.6346 0.0942 -0.1315 -0.0182 54 ALA A C 429 O O . ALA A 54 ? 0.5852 0.7375 0.5954 0.0771 -0.1252 -0.0222 54 ALA A O 430 C CB . ALA A 54 ? 0.5405 0.6783 0.5744 0.1063 -0.1117 -0.0300 54 ALA A CB 431 N N . TYR A 55 ? 0.5291 0.6592 0.5363 0.1041 -0.1430 -0.0075 55 TYR A N 432 C CA . TYR A 55 ? 0.5437 0.6515 0.5276 0.0954 -0.1471 0.0008 55 TYR A CA 433 C C . TYR A 55 ? 0.5889 0.6608 0.5621 0.0974 -0.1406 0.0025 55 TYR A C 434 O O . TYR A 55 ? 0.5570 0.6143 0.5343 0.1122 -0.1430 0.0044 55 TYR A O 435 C CB . TYR A 55 ? 0.5525 0.6600 0.5298 0.1045 -0.1636 0.0128 55 TYR A CB 436 C CG . TYR A 55 ? 0.6293 0.7722 0.6139 0.1020 -0.1734 0.0130 55 TYR A CG 437 C CD1 . TYR A 55 ? 0.5563 0.7274 0.5505 0.0885 -0.1669 0.0022 55 TYR A CD1 438 C CD2 . TYR A 55 ? 0.6712 0.8192 0.6530 0.1131 -0.1897 0.0241 55 TYR A CD2 439 C CE1 . TYR A 55 ? 0.5786 0.7840 0.5801 0.0852 -0.1773 0.0015 55 TYR A CE1 440 C CE2 . TYR A 55 ? 0.6814 0.8638 0.6700 0.1114 -0.2007 0.0245 55 TYR A CE2 441 C CZ . TYR A 55 ? 0.6139 0.8258 0.6126 0.0969 -0.1948 0.0127 55 TYR A CZ 442 O OH . TYR A 55 ? 0.6144 0.8621 0.6202 0.0941 -0.2070 0.0124 55 TYR A OH 443 N N . LEU A 56 ? 0.5174 0.5752 0.4773 0.0828 -0.1327 0.0015 56 LEU A N 444 C CA . LEU A 56 ? 0.5361 0.5635 0.4875 0.0826 -0.1266 0.0023 56 LEU A CA 445 C C . LEU A 56 ? 0.6031 0.6114 0.5363 0.0721 -0.1281 0.0100 56 LEU A C 446 O O . LEU A 56 ? 0.6384 0.6577 0.5637 0.0617 -0.1294 0.0121 56 LEU A O 447 C CB . LEU A 56 ? 0.5719 0.6020 0.5283 0.0748 -0.1122 -0.0077 56 LEU A CB 448 C CG . LEU A 56 ? 0.5474 0.5999 0.5208 0.0791 -0.1059 -0.0170 56 LEU A CG 449 C CD1 . LEU A 56 ? 0.5640 0.6152 0.5374 0.0687 -0.0912 -0.0247 56 LEU A CD1 450 C CD2 . LEU A 56 ? 0.6338 0.6793 0.6150 0.0964 -0.1087 -0.0174 56 LEU A CD2 451 N N . TRP A 57 ? 0.5724 0.5527 0.4987 0.0742 -0.1273 0.0136 57 TRP A N 452 C CA . TRP A 57 ? 0.5397 0.5030 0.4527 0.0617 -0.1234 0.0178 57 TRP A CA 453 C C . TRP A 57 ? 0.5914 0.5478 0.5085 0.0561 -0.1119 0.0106 57 TRP A C 454 O O . TRP A 57 ? 0.6786 0.6235 0.6007 0.0641 -0.1110 0.0074 57 TRP A O 455 C CB . TRP A 57 ? 0.5746 0.5119 0.4772 0.0659 -0.1312 0.0282 57 TRP A CB 456 C CG . TRP A 57 ? 0.6963 0.6378 0.5885 0.0663 -0.1409 0.0381 57 TRP A CG 457 C CD1 . TRP A 57 ? 0.7660 0.7126 0.6605 0.0797 -0.1521 0.0434 57 TRP A CD1 458 C CD2 . TRP A 57 ? 0.7488 0.6903 0.6258 0.0532 -0.1399 0.0438 57 TRP A CD2 459 N NE1 . TRP A 57 ? 0.6655 0.6154 0.5460 0.0757 -0.1595 0.0531 57 TRP A NE1 460 C CE2 . TRP A 57 ? 0.7416 0.6879 0.6100 0.0590 -0.1517 0.0531 57 TRP A CE2 461 C CE3 . TRP A 57 ? 0.8259 0.7638 0.6954 0.0376 -0.1296 0.0421 57 TRP A CE3 462 C CZ2 . TRP A 57 ? 0.7772 0.7235 0.6271 0.0490 -0.1537 0.0606 57 TRP A CZ2 463 C CZ3 . TRP A 57 ? 0.8232 0.7611 0.6757 0.0277 -0.1305 0.0488 57 TRP A CZ3 464 C CH2 . TRP A 57 ? 0.8350 0.7769 0.6766 0.0330 -0.1425 0.0579 57 TRP A CH2 465 N N . ILE A 58 ? 0.5460 0.5085 0.4596 0.0427 -0.1032 0.0080 58 ILE A N 466 C CA . ILE A 58 ? 0.4946 0.4508 0.4117 0.0375 -0.0924 0.0025 58 ILE A CA 467 C C . ILE A 58 ? 0.6077 0.5460 0.5174 0.0294 -0.0901 0.0078 58 ILE A C 468 O O . ILE A 58 ? 0.6072 0.5460 0.5080 0.0200 -0.0891 0.0122 58 ILE A O 469 C CB . ILE A 58 ? 0.5618 0.5364 0.4827 0.0289 -0.0823 -0.0049 58 ILE A CB 470 C CG1 . ILE A 58 ? 0.6074 0.6018 0.5385 0.0360 -0.0838 -0.0107 58 ILE A CG1 471 C CG2 . ILE A 58 ? 0.5471 0.5140 0.4713 0.0252 -0.0715 -0.0092 58 ILE A CG2 472 C CD1 . ILE A 58 ? 0.6082 0.6219 0.5434 0.0261 -0.0743 -0.0184 58 ILE A CD1 473 N N . ARG A 59 ? 0.4957 0.4187 0.4089 0.0328 -0.0894 0.0071 59 ARG A N 474 C CA . ARG A 59 ? 0.5065 0.4146 0.4169 0.0253 -0.0871 0.0113 59 ARG A CA 475 C C . ARG A 59 ? 0.4887 0.3985 0.4063 0.0213 -0.0774 0.0058 59 ARG A C 476 O O . ARG A 59 ? 0.5324 0.4396 0.4553 0.0284 -0.0776 0.0013 59 ARG A O 477 C CB . ARG A 59 ? 0.5297 0.4172 0.4386 0.0314 -0.0961 0.0158 59 ARG A CB 478 C CG . ARG A 59 ? 0.6018 0.4756 0.5111 0.0225 -0.0935 0.0193 59 ARG A CG 479 C CD . ARG A 59 ? 0.7237 0.5754 0.6301 0.0258 -0.1024 0.0243 59 ARG A CD 480 N NE . ARG A 59 ? 0.6778 0.5219 0.5738 0.0217 -0.1058 0.0338 59 ARG A NE 481 C CZ . ARG A 59 ? 0.7971 0.6226 0.6891 0.0160 -0.1080 0.0407 59 ARG A CZ 482 N NH1 . ARG A 59 ? 0.8245 0.6379 0.7239 0.0131 -0.1082 0.0385 59 ARG A NH1 483 N NH2 . ARG A 59 ? 0.7788 0.5977 0.6588 0.0127 -0.1102 0.0502 59 ARG A NH2 484 N N . GLN A 60 ? 0.4764 0.3900 0.3930 0.0105 -0.0688 0.0065 60 GLN A N 485 C CA . GLN A 60 ? 0.4722 0.3871 0.3962 0.0069 -0.0591 0.0027 60 GLN A CA 486 C C . GLN A 60 ? 0.5285 0.4333 0.4550 0.0003 -0.0576 0.0075 60 GLN A C 487 O O . GLN A 60 ? 0.5024 0.4041 0.4228 -0.0070 -0.0573 0.0128 60 GLN A O 488 C CB . GLN A 60 ? 0.4975 0.4257 0.4203 0.0001 -0.0481 -0.0017 60 GLN A CB 489 C CG . GLN A 60 ? 0.4345 0.3751 0.3567 0.0046 -0.0497 -0.0066 60 GLN A CG 490 C CD . GLN A 60 ? 0.6013 0.5543 0.5220 -0.0039 -0.0391 -0.0119 60 GLN A CD 491 O OE1 . GLN A 60 ? 0.5376 0.4887 0.4612 -0.0091 -0.0279 -0.0145 60 GLN A OE1 492 N NE2 . GLN A 60 ? 0.6396 0.6052 0.5561 -0.0055 -0.0427 -0.0137 60 GLN A NE2 493 N N . ILE A 61 ? 0.4237 0.3243 0.3593 0.0028 -0.0567 0.0058 61 ILE A N 494 C CA . ILE A 61 ? 0.4410 0.3351 0.3836 -0.0029 -0.0557 0.0094 61 ILE A CA 495 C C . ILE A 61 ? 0.4191 0.3196 0.3727 -0.0038 -0.0469 0.0065 61 ILE A C 496 O O . ILE A 61 ? 0.4991 0.4014 0.4558 0.0036 -0.0475 0.0024 61 ILE A O 497 C CB . ILE A 61 ? 0.4467 0.3277 0.3912 0.0017 -0.0674 0.0110 61 ILE A CB 498 C CG1 . ILE A 61 ? 0.5606 0.4324 0.4942 0.0046 -0.0762 0.0145 61 ILE A CG1 499 C CG2 . ILE A 61 ? 0.5412 0.4180 0.4957 -0.0059 -0.0665 0.0143 61 ILE A CG2 500 C CD1 . ILE A 61 ? 0.5150 0.3703 0.4484 0.0095 -0.0873 0.0152 61 ILE A CD1 501 N N . TRP A 62 ? 0.3942 0.2975 0.3538 -0.0123 -0.0385 0.0089 62 TRP A N 502 C CA . TRP A 62 ? 0.4001 0.3097 0.3722 -0.0123 -0.0295 0.0071 62 TRP A CA 503 C C . TRP A 62 ? 0.5140 0.4247 0.4954 -0.0211 -0.0237 0.0111 62 TRP A C 504 O O . TRP A 62 ? 0.4761 0.3823 0.4512 -0.0282 -0.0248 0.0152 62 TRP A O 505 C CB . TRP A 62 ? 0.3860 0.3025 0.3543 -0.0119 -0.0181 0.0025 62 TRP A CB 506 C CG . TRP A 62 ? 0.3720 0.2918 0.3328 -0.0214 -0.0081 0.0023 62 TRP A CG 507 C CD1 . TRP A 62 ? 0.3862 0.3088 0.3523 -0.0281 0.0051 0.0022 62 TRP A CD1 508 C CD2 . TRP A 62 ? 0.4074 0.3283 0.3533 -0.0250 -0.0104 0.0018 62 TRP A CD2 509 N NE1 . TRP A 62 ? 0.4168 0.3408 0.3698 -0.0364 0.0113 0.0011 62 TRP A NE1 510 C CE2 . TRP A 62 ? 0.3713 0.2948 0.3118 -0.0347 0.0009 0.0013 62 TRP A CE2 511 C CE3 . TRP A 62 ? 0.4308 0.3513 0.3677 -0.0205 -0.0212 0.0018 62 TRP A CE3 512 C CZ2 . TRP A 62 ? 0.4418 0.3679 0.3667 -0.0406 0.0006 0.0007 62 TRP A CZ2 513 C CZ3 . TRP A 62 ? 0.4879 0.4123 0.4119 -0.0255 -0.0218 0.0021 62 TRP A CZ3 514 C CH2 . TRP A 62 ? 0.4559 0.3831 0.3732 -0.0357 -0.0116 0.0015 62 TRP A CH2 515 N N . HIS A 63 ? 0.4270 0.3440 0.4237 -0.0203 -0.0171 0.0105 63 HIS A N 516 C CA . HIS A 63 ? 0.4541 0.3755 0.4634 -0.0282 -0.0088 0.0137 63 HIS A CA 517 C C . HIS A 63 ? 0.4495 0.3767 0.4593 -0.0316 0.0083 0.0114 63 HIS A C 518 O O . HIS A 63 ? 0.4347 0.3645 0.4458 -0.0256 0.0142 0.0077 63 HIS A O 519 C CB . HIS A 63 ? 0.4189 0.3454 0.4486 -0.0246 -0.0136 0.0147 63 HIS A CB 520 C CG . HIS A 63 ? 0.5146 0.4349 0.5468 -0.0266 -0.0277 0.0171 63 HIS A CG 521 N ND1 . HIS A 63 ? 0.6634 0.5830 0.7036 -0.0365 -0.0271 0.0212 63 HIS A ND1 522 C CD2 . HIS A 63 ? 0.5678 0.4807 0.5941 -0.0205 -0.0419 0.0155 63 HIS A CD2 523 C CE1 . HIS A 63 ? 0.5251 0.4362 0.5648 -0.0368 -0.0408 0.0219 63 HIS A CE1 524 N NE2 . HIS A 63 ? 0.6517 0.5584 0.6825 -0.0269 -0.0499 0.0181 63 HIS A NE2 525 N N . ASP A 64 ? 0.4533 0.3809 0.4609 -0.0414 0.0172 0.0136 64 ASP A N 526 C CA . ASP A 64 ? 0.3950 0.3269 0.4040 -0.0454 0.0347 0.0108 64 ASP A CA 527 C C . ASP A 64 ? 0.5226 0.4617 0.5544 -0.0475 0.0421 0.0135 64 ASP A C 528 O O . ASP A 64 ? 0.4756 0.4148 0.5124 -0.0545 0.0399 0.0180 64 ASP A O 529 C CB . ASP A 64 ? 0.4806 0.4083 0.4688 -0.0553 0.0403 0.0109 64 ASP A CB 530 C CG . ASP A 64 ? 0.4117 0.3417 0.3965 -0.0604 0.0590 0.0063 64 ASP A CG 531 O OD1 . ASP A 64 ? 0.4812 0.4156 0.4820 -0.0619 0.0705 0.0067 64 ASP A OD1 532 O OD2 . ASP A 64 ? 0.4753 0.4030 0.4415 -0.0633 0.0617 0.0019 64 ASP A OD2 533 N N . ALA A 65 ? 0.4788 0.4241 0.5256 -0.0416 0.0512 0.0112 65 ALA A N 534 C CA . ALA A 65 ? 0.4658 0.4212 0.5384 -0.0418 0.0576 0.0139 65 ALA A CA 535 C C . ALA A 65 ? 0.4018 0.3594 0.4755 -0.0524 0.0734 0.0145 65 ALA A C 536 O O . ALA A 65 ? 0.5012 0.4680 0.5962 -0.0553 0.0778 0.0175 65 ALA A O 537 C CB . ALA A 65 ? 0.4618 0.4226 0.5494 -0.0311 0.0641 0.0119 65 ALA A CB 538 N N . TYR A 66 ? 0.4279 0.3779 0.4785 -0.0587 0.0823 0.0113 66 TYR A N 539 C CA . TYR A 66 ? 0.4911 0.4420 0.5396 -0.0680 0.1004 0.0105 66 TYR A CA 540 C C . TYR A 66 ? 0.5632 0.5084 0.5944 -0.0794 0.0975 0.0147 66 TYR A C 541 O O . TYR A 66 ? 0.6200 0.5653 0.6475 -0.0883 0.1117 0.0153 66 TYR A O 542 C CB . TYR A 66 ? 0.5327 0.4781 0.5654 -0.0683 0.1146 0.0031 66 TYR A CB 543 C CG . TYR A 66 ? 0.5949 0.5424 0.6425 -0.0573 0.1203 -0.0006 66 TYR A CG 544 C CD1 . TYR A 66 ? 0.7264 0.6834 0.8032 -0.0506 0.1262 0.0017 66 TYR A CD1 545 C CD2 . TYR A 66 ? 0.5393 0.4794 0.5719 -0.0534 0.1196 -0.0060 66 TYR A CD2 546 C CE1 . TYR A 66 ? 0.7528 0.7099 0.8418 -0.0393 0.1314 -0.0004 66 TYR A CE1 547 C CE2 . TYR A 66 ? 0.6122 0.5511 0.6563 -0.0434 0.1259 -0.0085 66 TYR A CE2 548 C CZ . TYR A 66 ? 0.7559 0.7025 0.8271 -0.0359 0.1314 -0.0052 66 TYR A CZ 549 O OH . TYR A 66 ? 0.8139 0.7575 0.8947 -0.0249 0.1373 -0.0065 66 TYR A OH 550 N N . LEU A 67 ? 0.4816 0.4208 0.5019 -0.0787 0.0798 0.0182 67 LEU A N 551 C CA . LEU A 67 ? 0.4963 0.4275 0.4986 -0.0881 0.0760 0.0235 67 LEU A CA 552 C C . LEU A 67 ? 0.5346 0.4656 0.5521 -0.0897 0.0649 0.0300 67 LEU A C 553 O O . LEU A 67 ? 0.5600 0.4814 0.5653 -0.0899 0.0506 0.0339 67 LEU A O 554 C CB . LEU A 67 ? 0.5297 0.4523 0.5043 -0.0868 0.0655 0.0225 67 LEU A CB 555 C CG . LEU A 67 ? 0.5313 0.4540 0.4882 -0.0883 0.0762 0.0153 67 LEU A CG 556 C CD1 . LEU A 67 ? 0.5382 0.4567 0.4736 -0.0862 0.0637 0.0141 67 LEU A CD1 557 C CD2 . LEU A 67 ? 0.5330 0.4537 0.4764 -0.0998 0.0924 0.0154 67 LEU A CD2 558 N N . THR A 68 ? 0.5439 0.4853 0.5888 -0.0911 0.0719 0.0310 68 THR A N 559 C CA . THR A 68 ? 0.5378 0.4799 0.5985 -0.0959 0.0633 0.0367 68 THR A CA 560 C C . THR A 68 ? 0.5347 0.4790 0.6011 -0.1085 0.0781 0.0409 68 THR A C 561 O O . THR A 68 ? 0.4769 0.4255 0.5408 -0.1119 0.0961 0.0388 68 THR A O 562 C CB . THR A 68 ? 0.4952 0.4499 0.5862 -0.0878 0.0554 0.0348 68 THR A CB 563 O OG1 . THR A 68 ? 0.4573 0.4271 0.5710 -0.0866 0.0710 0.0327 68 THR A OG1 564 C CG2 . THR A 68 ? 0.5689 0.5205 0.6520 -0.0750 0.0430 0.0306 68 THR A CG2 565 N N . TRP A 69 ? 0.5070 0.4472 0.5803 -0.1162 0.0715 0.0468 69 TRP A N 566 C CA . TRP A 69 ? 0.4879 0.4309 0.5690 -0.1290 0.0865 0.0513 69 TRP A CA 567 C C . TRP A 69 ? 0.5080 0.4510 0.6084 -0.1363 0.0780 0.0561 69 TRP A C 568 O O . TRP A 69 ? 0.5601 0.4957 0.6603 -0.1325 0.0596 0.0565 69 TRP A O 569 C CB . TRP A 69 ? 0.5069 0.4342 0.5528 -0.1374 0.0946 0.0554 69 TRP A CB 570 C CG . TRP A 69 ? 0.5887 0.4963 0.6113 -0.1397 0.0788 0.0619 69 TRP A CG 571 C CD1 . TRP A 69 ? 0.6956 0.5919 0.7171 -0.1499 0.0766 0.0699 69 TRP A CD1 572 C CD2 . TRP A 69 ? 0.4960 0.3922 0.4938 -0.1313 0.0642 0.0610 69 TRP A CD2 573 N NE1 . TRP A 69 ? 0.5897 0.4669 0.5864 -0.1472 0.0613 0.0742 69 TRP A NE1 574 C CE2 . TRP A 69 ? 0.5267 0.4051 0.5098 -0.1354 0.0533 0.0688 69 TRP A CE2 575 C CE3 . TRP A 69 ? 0.5023 0.4020 0.4901 -0.1208 0.0599 0.0544 69 TRP A CE3 576 C CZ2 . TRP A 69 ? 0.5090 0.3744 0.4690 -0.1279 0.0381 0.0701 69 TRP A CZ2 577 C CZ3 . TRP A 69 ? 0.4903 0.3788 0.4564 -0.1147 0.0450 0.0554 69 TRP A CZ3 578 C CH2 . TRP A 69 ? 0.4936 0.3658 0.4463 -0.1178 0.0343 0.0633 69 TRP A CH2 579 N N . ASP A 70 ? 0.4987 0.4497 0.6154 -0.1475 0.0931 0.0592 70 ASP A N 580 C CA . ASP A 70 ? 0.6091 0.5628 0.7484 -0.1574 0.0892 0.0634 70 ASP A CA 581 C C . ASP A 70 ? 0.6200 0.5495 0.7300 -0.1684 0.0890 0.0714 70 ASP A C 582 O O . ASP A 70 ? 0.5812 0.5050 0.6736 -0.1766 0.1057 0.0754 70 ASP A O 583 C CB . ASP A 70 ? 0.5572 0.5332 0.7296 -0.1639 0.1077 0.0628 70 ASP A CB 584 C CG . ASP A 70 ? 0.6031 0.5850 0.8025 -0.1761 0.1053 0.0666 70 ASP A CG 585 O OD1 . ASP A 70 ? 0.6148 0.5790 0.8024 -0.1807 0.0906 0.0700 70 ASP A OD1 586 O OD2 . ASP A 70 ? 0.5704 0.5742 0.8032 -0.1814 0.1185 0.0659 70 ASP A OD2 587 N N . ARG A 71 ? 0.6416 0.5557 0.7445 -0.1680 0.0706 0.0738 71 ARG A N 588 C CA . ARG A 71 ? 0.6645 0.5527 0.7401 -0.1769 0.0684 0.0825 71 ARG A CA 589 C C . ARG A 71 ? 0.6819 0.5699 0.7650 -0.1938 0.0860 0.0891 71 ARG A C 590 O O . ARG A 71 ? 0.6932 0.5636 0.7469 -0.2010 0.0944 0.0968 71 ARG A O 591 C CB . ARG A 71 ? 0.6996 0.5731 0.7763 -0.1748 0.0475 0.0829 71 ARG A CB 592 C CG . ARG A 71 ? 0.6906 0.5573 0.7497 -0.1591 0.0312 0.0785 71 ARG A CG 593 C CD . ARG A 71 ? 0.7485 0.6052 0.8156 -0.1562 0.0119 0.0763 71 ARG A CD 594 N NE . ARG A 71 ? 0.6684 0.5469 0.7706 -0.1545 0.0074 0.0689 71 ARG A NE 595 C CZ . ARG A 71 ? 0.6701 0.5458 0.7848 -0.1529 -0.0086 0.0648 71 ARG A CZ 596 N NH1 . ARG A 71 ? 0.6647 0.5145 0.7604 -0.1527 -0.0207 0.0668 71 ARG A NH1 597 N NH2 . ARG A 71 ? 0.5672 0.4656 0.7129 -0.1510 -0.0127 0.0585 71 ARG A NH2 598 N N . ASP A 72 ? 0.6288 0.5374 0.7513 -0.2000 0.0917 0.0864 72 ASP A N 599 C CA . ASP A 72 ? 0.6528 0.5645 0.7886 -0.2171 0.1096 0.0921 72 ASP A CA 600 C C . ASP A 72 ? 0.6231 0.5374 0.7421 -0.2212 0.1333 0.0945 72 ASP A C 601 O O . ASP A 72 ? 0.7117 0.6184 0.8242 -0.2354 0.1485 0.1016 72 ASP A O 602 C CB . ASP A 72 ? 0.7491 0.6894 0.9355 -0.2211 0.1111 0.0871 72 ASP A CB 603 C CG . ASP A 72 ? 0.8856 0.8218 1.0887 -0.2227 0.0899 0.0854 72 ASP A CG 604 O OD1 . ASP A 72 ? 0.9534 0.8615 1.1291 -0.2230 0.0770 0.0891 72 ASP A OD1 605 O OD2 . ASP A 72 ? 0.9140 0.8752 1.1576 -0.2237 0.0861 0.0801 72 ASP A OD2 606 N N . GLN A 73 ? 0.6490 0.5738 0.7614 -0.2094 0.1376 0.0880 73 GLN A N 607 C CA . GLN A 73 ? 0.6748 0.6021 0.7710 -0.2130 0.1604 0.0882 73 GLN A CA 608 C C . GLN A 73 ? 0.7619 0.6627 0.8064 -0.2144 0.1597 0.0940 73 GLN A C 609 O O . GLN A 73 ? 0.7069 0.6053 0.7298 -0.2191 0.1777 0.0949 73 GLN A O 610 C CB . GLN A 73 ? 0.7241 0.6718 0.8348 -0.2001 0.1661 0.0781 73 GLN A CB 611 C CG . GLN A 73 ? 0.7519 0.7281 0.9143 -0.1971 0.1674 0.0732 73 GLN A CG 612 C CD . GLN A 73 ? 0.9141 0.9071 1.0895 -0.1823 0.1712 0.0644 73 GLN A CD 613 O OE1 . GLN A 73 ? 1.0430 1.0282 1.1914 -0.1775 0.1797 0.0611 73 GLN A OE1 614 N NE2 . GLN A 73 ? 0.9470 0.9624 1.1634 -0.1751 0.1645 0.0606 73 GLN A NE2 615 N N . TYR A 74 ? 0.7639 0.6455 0.7885 -0.2099 0.1388 0.0978 74 TYR A N 616 C CA . TYR A 74 ? 0.7475 0.6056 0.7251 -0.2093 0.1345 0.1040 74 TYR A CA 617 C C . TYR A 74 ? 0.8267 0.6598 0.7897 -0.2149 0.1225 0.1146 74 TYR A C 618 O O . TYR A 74 ? 0.8313 0.6478 0.7695 -0.2069 0.1059 0.1174 74 TYR A O 619 C CB . TYR A 74 ? 0.7612 0.6214 0.7242 -0.1939 0.1212 0.0969 74 TYR A CB 620 C CG . TYR A 74 ? 0.6728 0.5536 0.6479 -0.1888 0.1343 0.0867 74 TYR A CG 621 C CD1 . TYR A 74 ? 0.6528 0.5543 0.6667 -0.1817 0.1328 0.0789 74 TYR A CD1 622 C CD2 . TYR A 74 ? 0.7371 0.6158 0.6839 -0.1908 0.1481 0.0849 74 TYR A CD2 623 C CE1 . TYR A 74 ? 0.5588 0.4769 0.5837 -0.1758 0.1453 0.0702 74 TYR A CE1 624 C CE2 . TYR A 74 ? 0.6981 0.5930 0.6554 -0.1863 0.1613 0.0749 74 TYR A CE2 625 C CZ . TYR A 74 ? 0.6490 0.5627 0.6457 -0.1784 0.1603 0.0680 74 TYR A CZ 626 O OH . TYR A 74 ? 0.6608 0.5880 0.6677 -0.1731 0.1740 0.0589 74 TYR A OH 627 N N . ASP A 75 ? 0.8267 0.6573 0.8067 -0.2288 0.1318 0.1204 75 ASP A N 628 C CA . ASP A 75 ? 0.8486 0.6524 0.8149 -0.2368 0.1243 0.1313 75 ASP A CA 629 C C . ASP A 75 ? 0.8431 0.6349 0.8082 -0.2252 0.0987 0.1295 75 ASP A C 630 O O . ASP A 75 ? 0.7959 0.5610 0.7326 -0.2239 0.0887 0.1379 75 ASP A O 631 C CB . ASP A 75 ? 0.8568 0.6381 0.7770 -0.2425 0.1334 0.1425 75 ASP A CB 632 C CG . ASP A 75 ? 1.0235 0.7765 0.9310 -0.2542 0.1330 0.1558 75 ASP A CG 633 O OD1 . ASP A 75 ? 1.0696 0.8237 1.0080 -0.2633 0.1332 0.1559 75 ASP A OD1 634 O OD2 . ASP A 75 ? 1.1317 0.8611 0.9974 -0.2545 0.1321 0.1664 75 ASP A OD2 635 N N . GLY A 76 ? 0.7711 0.5825 0.7664 -0.2161 0.0885 0.1186 76 GLY A N 636 C CA . GLY A 76 ? 0.7631 0.5648 0.7625 -0.2069 0.0660 0.1157 76 GLY A CA 637 C C . GLY A 76 ? 0.7262 0.5236 0.7013 -0.1902 0.0526 0.1124 76 GLY A C 638 O O . GLY A 76 ? 0.7455 0.5377 0.7241 -0.1802 0.0349 0.1083 76 GLY A O 639 N N . LEU A 77 ? 0.7590 0.5586 0.7092 -0.1877 0.0614 0.1139 77 LEU A N 640 C CA . LEU A 77 ? 0.6815 0.4785 0.6080 -0.1737 0.0500 0.1112 77 LEU A CA 641 C C . LEU A 77 ? 0.6756 0.4903 0.6254 -0.1613 0.0396 0.0995 77 LEU A C 642 O O . LEU A 77 ? 0.7192 0.5557 0.6925 -0.1612 0.0485 0.0921 77 LEU A O 643 C CB . LEU A 77 ? 0.7769 0.5798 0.6794 -0.1754 0.0637 0.1117 77 LEU A CB 644 C CG . LEU A 77 ? 0.7671 0.5719 0.6480 -0.1624 0.0530 0.1074 77 LEU A CG 645 C CD1 . LEU A 77 ? 0.8278 0.6095 0.6820 -0.1577 0.0376 0.1166 77 LEU A CD1 646 C CD2 . LEU A 77 ? 0.8067 0.6206 0.6682 -0.1657 0.0678 0.1049 77 LEU A CD2 647 N N . ASP A 78 ? 0.6831 0.4879 0.6263 -0.1503 0.0214 0.0980 78 ASP A N 648 C CA . ASP A 78 ? 0.6528 0.4714 0.6168 -0.1393 0.0110 0.0878 78 ASP A CA 649 C C . ASP A 78 ? 0.5531 0.3727 0.4998 -0.1251 0.0012 0.0835 78 ASP A C 650 O O . ASP A 78 ? 0.6177 0.4466 0.5775 -0.1154 -0.0070 0.0756 78 ASP A O 651 C CB . ASP A 78 ? 0.7679 0.5763 0.7479 -0.1396 -0.0021 0.0871 78 ASP A CB 652 C CG . ASP A 78 ? 0.8218 0.6035 0.7782 -0.1349 -0.0152 0.0929 78 ASP A CG 653 O OD1 . ASP A 78 ? 0.8662 0.6400 0.7953 -0.1301 -0.0157 0.0978 78 ASP A OD1 654 O OD2 . ASP A 78 ? 0.7956 0.5647 0.7615 -0.1359 -0.0252 0.0923 78 ASP A OD2 655 N N . SER A 79 ? 0.6912 0.5022 0.6083 -0.1243 0.0024 0.0888 79 SER A N 656 C CA . SER A 79 ? 0.6547 0.4684 0.5564 -0.1120 -0.0070 0.0850 79 SER A CA 657 C C . SER A 79 ? 0.7023 0.5149 0.5755 -0.1152 -0.0002 0.0894 79 SER A C 658 O O . SER A 79 ? 0.7004 0.4995 0.5567 -0.1236 0.0042 0.0991 79 SER A O 659 C CB . SER A 79 ? 0.6899 0.4859 0.5839 -0.1034 -0.0243 0.0882 79 SER A CB 660 O OG . SER A 79 ? 0.7630 0.5647 0.6463 -0.0910 -0.0330 0.0839 79 SER A OG 661 N N . ILE A 80 ? 0.6338 0.4602 0.5003 -0.1092 0.0005 0.0824 80 ILE A N 662 C CA . ILE A 80 ? 0.6801 0.5068 0.5182 -0.1130 0.0058 0.0852 80 ILE A CA 663 C C . ILE A 80 ? 0.7018 0.5369 0.5304 -0.1021 -0.0050 0.0795 80 ILE A C 664 O O . ILE A 80 ? 0.5985 0.4442 0.4451 -0.0940 -0.0090 0.0707 80 ILE A O 665 C CB . ILE A 80 ? 0.7638 0.6011 0.6044 -0.1236 0.0261 0.0814 80 ILE A CB 666 C CG1 . ILE A 80 ? 0.8964 0.7329 0.7047 -0.1289 0.0320 0.0833 80 ILE A CG1 667 C CG2 . ILE A 80 ? 0.6327 0.4882 0.4982 -0.1189 0.0320 0.0692 80 ILE A CG2 668 C CD1 . ILE A 80 ? 0.8967 0.7363 0.7022 -0.1413 0.0532 0.0827 80 ILE A CD1 669 N N . ARG A 81 ? 0.6636 0.4942 0.4647 -0.1016 -0.0107 0.0850 81 ARG A N 670 C CA . ARG A 81 ? 0.6640 0.5059 0.4572 -0.0929 -0.0201 0.0793 81 ARG A CA 671 C C . ARG A 81 ? 0.8060 0.6613 0.5870 -0.1004 -0.0081 0.0722 81 ARG A C 672 O O . ARG A 81 ? 0.8540 0.7046 0.6139 -0.1102 0.0003 0.0770 81 ARG A O 673 C CB . ARG A 81 ? 0.7226 0.5548 0.4946 -0.0866 -0.0355 0.0888 81 ARG A CB 674 C CG . ARG A 81 ? 0.8350 0.6548 0.6178 -0.0761 -0.0490 0.0931 81 ARG A CG 675 C CD . ARG A 81 ? 0.9123 0.7236 0.6753 -0.0676 -0.0640 0.1025 81 ARG A CD 676 N NE . ARG A 81 ? 0.9641 0.7640 0.7403 -0.0559 -0.0757 0.1040 81 ARG A NE 677 C CZ . ARG A 81 ? 1.0153 0.8254 0.8025 -0.0433 -0.0855 0.0972 81 ARG A CZ 678 N NH1 . ARG A 81 ? 1.0656 0.8981 0.8528 -0.0410 -0.0856 0.0890 81 ARG A NH1 679 N NH2 . ARG A 81 ? 0.9401 0.7371 0.7377 -0.0333 -0.0944 0.0982 81 ARG A NH2 680 N N . ILE A 82 ? 0.8036 0.6740 0.5965 -0.0961 -0.0068 0.0607 82 ILE A N 681 C CA . ILE A 82 ? 0.7399 0.6218 0.5274 -0.1031 0.0066 0.0513 82 ILE A CA 682 C C . ILE A 82 ? 0.7424 0.6364 0.5235 -0.0974 -0.0030 0.0446 82 ILE A C 683 O O . ILE A 82 ? 0.6087 0.5069 0.4067 -0.0872 -0.0122 0.0418 82 ILE A O 684 C CB . ILE A 82 ? 0.6562 0.5446 0.4719 -0.1018 0.0179 0.0425 82 ILE A CB 685 C CG1 . ILE A 82 ? 0.7470 0.6278 0.5769 -0.1066 0.0266 0.0480 82 ILE A CG1 686 C CG2 . ILE A 82 ? 0.7522 0.6505 0.5644 -0.1074 0.0322 0.0317 82 ILE A CG2 687 C CD1 . ILE A 82 ? 0.7672 0.6423 0.5793 -0.1192 0.0404 0.0526 82 ILE A CD1 688 N N . PRO A 83 ? 0.6807 0.5810 0.4383 -0.1042 -0.0009 0.0416 83 PRO A N 689 C CA . PRO A 83 ? 0.6751 0.5906 0.4316 -0.1006 -0.0082 0.0327 83 PRO A CA 690 C C . PRO A 83 ? 0.6407 0.5640 0.4227 -0.0963 -0.0018 0.0218 83 PRO A C 691 O O . PRO A 83 ? 0.6517 0.5729 0.4437 -0.1008 0.0139 0.0166 83 PRO A O 692 C CB . PRO A 83 ? 0.7268 0.6469 0.4573 -0.1126 -0.0004 0.0280 83 PRO A CB 693 C CG . PRO A 83 ? 0.7243 0.6306 0.4334 -0.1187 0.0017 0.0397 83 PRO A CG 694 C CD . PRO A 83 ? 0.6798 0.5743 0.4104 -0.1161 0.0081 0.0453 83 PRO A CD 695 N N . SER A 84 ? 0.5929 0.5252 0.3856 -0.0870 -0.0132 0.0186 84 SER A N 696 C CA . SER A 84 ? 0.6307 0.5666 0.4474 -0.0808 -0.0087 0.0113 84 SER A CA 697 C C . SER A 84 ? 0.5810 0.5236 0.3979 -0.0885 0.0063 -0.0005 84 SER A C 698 O O . SER A 84 ? 0.5949 0.5360 0.4290 -0.0862 0.0159 -0.0052 84 SER A O 699 C CB . SER A 84 ? 0.5343 0.4780 0.3609 -0.0693 -0.0230 0.0104 84 SER A CB 700 O OG . SER A 84 ? 0.6513 0.6094 0.4681 -0.0718 -0.0280 0.0051 84 SER A OG 701 N N . ASP A 85 ? 0.5771 0.5256 0.3737 -0.0979 0.0085 -0.0049 85 ASP A N 702 C CA . ASP A 85 ? 0.6404 0.5931 0.4360 -0.1059 0.0231 -0.0173 85 ASP A CA 703 C C . ASP A 85 ? 0.6633 0.6054 0.4618 -0.1115 0.0420 -0.0188 85 ASP A C 704 O O . ASP A 85 ? 0.6172 0.5592 0.4183 -0.1163 0.0564 -0.0288 85 ASP A O 705 C CB . ASP A 85 ? 0.8294 0.7915 0.6018 -0.1156 0.0201 -0.0232 85 ASP A CB 706 C CG . ASP A 85 ? 0.9093 0.8661 0.6555 -0.1223 0.0172 -0.0154 85 ASP A CG 707 O OD1 . ASP A 85 ? 0.9415 0.8959 0.6841 -0.1158 0.0032 -0.0036 85 ASP A OD1 708 O OD2 . ASP A 85 ? 1.0989 1.0527 0.8267 -0.1340 0.0292 -0.0211 85 ASP A OD2 709 N N . LEU A 86 ? 0.5881 0.5213 0.3877 -0.1106 0.0427 -0.0090 86 LEU A N 710 C CA . LEU A 86 ? 0.6513 0.5769 0.4558 -0.1159 0.0609 -0.0098 86 LEU A CA 711 C C . LEU A 86 ? 0.6435 0.5677 0.4775 -0.1076 0.0664 -0.0104 86 LEU A C 712 O O . LEU A 86 ? 0.5848 0.5061 0.4282 -0.1101 0.0827 -0.0134 86 LEU A O 713 C CB . LEU A 86 ? 0.7267 0.6441 0.5196 -0.1204 0.0605 0.0011 86 LEU A CB 714 C CG . LEU A 86 ? 0.7647 0.6817 0.5243 -0.1289 0.0563 0.0030 86 LEU A CG 715 C CD1 . LEU A 86 ? 0.7902 0.6969 0.5378 -0.1341 0.0594 0.0139 86 LEU A CD1 716 C CD2 . LEU A 86 ? 0.7688 0.6895 0.5136 -0.1385 0.0692 -0.0096 86 LEU A CD2 717 N N . VAL A 87 ? 0.5414 0.4680 0.3899 -0.0972 0.0528 -0.0071 87 VAL A N 718 C CA . VAL A 87 ? 0.5086 0.4343 0.3824 -0.0891 0.0558 -0.0070 87 VAL A CA 719 C C . VAL A 87 ? 0.4426 0.3730 0.3251 -0.0834 0.0568 -0.0152 87 VAL A C 720 O O . VAL A 87 ? 0.5534 0.4891 0.4258 -0.0839 0.0502 -0.0193 87 VAL A O 721 C CB . VAL A 87 ? 0.5268 0.4495 0.4110 -0.0816 0.0411 0.0021 87 VAL A CB 722 C CG1 . VAL A 87 ? 0.4787 0.3948 0.3542 -0.0883 0.0412 0.0107 87 VAL A CG1 723 C CG2 . VAL A 87 ? 0.4898 0.4154 0.3686 -0.0747 0.0244 0.0028 87 VAL A CG2 724 N N . TRP A 88 ? 0.4755 0.4044 0.3772 -0.0778 0.0649 -0.0169 88 TRP A N 725 C CA . TRP A 88 ? 0.4862 0.4172 0.3963 -0.0709 0.0645 -0.0224 88 TRP A CA 726 C C . TRP A 88 ? 0.4781 0.4122 0.3900 -0.0627 0.0465 -0.0185 88 TRP A C 727 O O . TRP A 88 ? 0.4357 0.3675 0.3517 -0.0589 0.0360 -0.0110 88 TRP A O 728 C CB . TRP A 88 ? 0.4382 0.3661 0.3681 -0.0644 0.0740 -0.0224 88 TRP A CB 729 C CG . TRP A 88 ? 0.4759 0.4036 0.4133 -0.0563 0.0734 -0.0260 88 TRP A CG 730 C CD1 . TRP A 88 ? 0.4880 0.4125 0.4246 -0.0576 0.0863 -0.0334 88 TRP A CD1 731 C CD2 . TRP A 88 ? 0.4560 0.3849 0.4020 -0.0458 0.0603 -0.0221 88 TRP A CD2 732 N NE1 . TRP A 88 ? 0.4117 0.3356 0.3558 -0.0484 0.0820 -0.0334 88 TRP A NE1 733 C CE2 . TRP A 88 ? 0.5114 0.4384 0.4605 -0.0411 0.0661 -0.0268 88 TRP A CE2 734 C CE3 . TRP A 88 ? 0.4058 0.3356 0.3555 -0.0404 0.0448 -0.0156 88 TRP A CE3 735 C CZ2 . TRP A 88 ? 0.5197 0.4466 0.4746 -0.0309 0.0572 -0.0247 88 TRP A CZ2 736 C CZ3 . TRP A 88 ? 0.4483 0.3778 0.4038 -0.0303 0.0356 -0.0147 88 TRP A CZ3 737 C CH2 . TRP A 88 ? 0.4550 0.3835 0.4126 -0.0256 0.0419 -0.0191 88 TRP A CH2 738 N N . ARG A 89 ? 0.4464 0.3853 0.3549 -0.0608 0.0436 -0.0240 89 ARG A N 739 C CA . ARG A 89 ? 0.4316 0.3741 0.3434 -0.0520 0.0286 -0.0217 89 ARG A CA 740 C C . ARG A 89 ? 0.4690 0.4124 0.3903 -0.0454 0.0326 -0.0266 89 ARG A C 741 O O . ARG A 89 ? 0.5087 0.4509 0.4304 -0.0494 0.0458 -0.0328 89 ARG A O 742 C CB . ARG A 89 ? 0.5379 0.4882 0.4354 -0.0560 0.0193 -0.0224 89 ARG A CB 743 C CG . ARG A 89 ? 0.6077 0.5547 0.4938 -0.0604 0.0132 -0.0152 89 ARG A CG 744 C CD . ARG A 89 ? 0.6865 0.6418 0.5567 -0.0645 0.0044 -0.0155 89 ARG A CD 745 N NE . ARG A 89 ? 0.7935 0.7556 0.6543 -0.0744 0.0139 -0.0246 89 ARG A NE 746 C CZ . ARG A 89 ? 0.9485 0.9200 0.7940 -0.0807 0.0079 -0.0267 89 ARG A CZ 747 N NH1 . ARG A 89 ? 0.8455 0.8206 0.6829 -0.0770 -0.0076 -0.0191 89 ARG A NH1 748 N NH2 . ARG A 89 ? 0.8634 0.8401 0.7011 -0.0909 0.0175 -0.0365 89 ARG A NH2 749 N N . PRO A 90 ? 0.4665 0.4101 0.3942 -0.0354 0.0222 -0.0240 90 PRO A N 750 C CA . PRO A 90 ? 0.4670 0.4095 0.4021 -0.0289 0.0272 -0.0275 90 PRO A CA 751 C C . PRO A 90 ? 0.5121 0.4622 0.4431 -0.0314 0.0300 -0.0346 90 PRO A C 752 O O . PRO A 90 ? 0.5755 0.5235 0.5112 -0.0275 0.0366 -0.0376 90 PRO A O 753 C CB . PRO A 90 ? 0.4729 0.4124 0.4138 -0.0177 0.0149 -0.0226 90 PRO A CB 754 C CG . PRO A 90 ? 0.4381 0.3777 0.3744 -0.0185 0.0024 -0.0175 90 PRO A CG 755 C CD . PRO A 90 ? 0.4331 0.3733 0.3630 -0.0293 0.0086 -0.0168 90 PRO A CD 756 N N . ASP A 91 ? 0.5016 0.4609 0.4242 -0.0380 0.0252 -0.0369 91 ASP A N 757 C CA . ASP A 91 ? 0.4674 0.4370 0.3884 -0.0425 0.0280 -0.0445 91 ASP A CA 758 C C . ASP A 91 ? 0.4736 0.4487 0.4014 -0.0328 0.0208 -0.0444 91 ASP A C 759 O O . ASP A 91 ? 0.5107 0.4903 0.4422 -0.0338 0.0277 -0.0502 91 ASP A O 760 C CB . ASP A 91 ? 0.5176 0.4817 0.4393 -0.0492 0.0455 -0.0513 91 ASP A CB 761 C CG . ASP A 91 ? 0.7521 0.7269 0.6690 -0.0597 0.0494 -0.0604 91 ASP A CG 762 O OD1 . ASP A 91 ? 0.7666 0.7534 0.6769 -0.0641 0.0392 -0.0608 91 ASP A OD1 763 O OD2 . ASP A 91 ? 0.8488 0.8201 0.7683 -0.0637 0.0622 -0.0668 91 ASP A OD2 764 N N . ILE A 92 ? 0.4616 0.4359 0.3907 -0.0240 0.0078 -0.0382 92 ILE A N 765 C CA . ILE A 92 ? 0.4397 0.4185 0.3743 -0.0141 0.0012 -0.0385 92 ILE A CA 766 C C . ILE A 92 ? 0.5810 0.5773 0.5156 -0.0164 -0.0052 -0.0421 92 ILE A C 767 O O . ILE A 92 ? 0.6488 0.6503 0.5777 -0.0192 -0.0141 -0.0392 92 ILE A O 768 C CB . ILE A 92 ? 0.5171 0.4863 0.4527 -0.0037 -0.0096 -0.0317 92 ILE A CB 769 C CG1 . ILE A 92 ? 0.5082 0.4643 0.4469 -0.0007 -0.0030 -0.0297 92 ILE A CG1 770 C CG2 . ILE A 92 ? 0.5536 0.5282 0.4926 0.0066 -0.0180 -0.0325 92 ILE A CG2 771 C CD1 . ILE A 92 ? 0.6332 0.5797 0.5723 0.0039 -0.0121 -0.0234 92 ILE A CD1 772 N N . VAL A 93 ? 0.4952 0.5009 0.4364 -0.0154 -0.0003 -0.0479 93 VAL A N 773 C CA . VAL A 93 ? 0.5047 0.5307 0.4502 -0.0174 -0.0057 -0.0522 93 VAL A CA 774 C C . VAL A 93 ? 0.4865 0.5190 0.4418 -0.0071 -0.0067 -0.0539 93 VAL A C 775 O O . VAL A 93 ? 0.4722 0.4924 0.4283 -0.0005 -0.0010 -0.0529 93 VAL A O 776 C CB . VAL A 93 ? 0.5604 0.5961 0.5058 -0.0314 0.0048 -0.0606 93 VAL A CB 777 C CG1 . VAL A 93 ? 0.7132 0.7420 0.6469 -0.0420 0.0075 -0.0602 93 VAL A CG1 778 C CG2 . VAL A 93 ? 0.5502 0.5784 0.5002 -0.0328 0.0203 -0.0652 93 VAL A CG2 779 N N . LEU A 94 ? 0.5302 0.5828 0.4926 -0.0057 -0.0141 -0.0564 94 LEU A N 780 C CA . LEU A 94 ? 0.4242 0.4878 0.3981 0.0022 -0.0129 -0.0596 94 LEU A CA 781 C C . LEU A 94 ? 0.4978 0.5665 0.4770 -0.0067 0.0027 -0.0674 94 LEU A C 782 O O . LEU A 94 ? 0.4582 0.5417 0.4408 -0.0187 0.0059 -0.0733 94 LEU A O 783 C CB . LEU A 94 ? 0.4756 0.5623 0.4584 0.0060 -0.0252 -0.0600 94 LEU A CB 784 C CG . LEU A 94 ? 0.4621 0.5624 0.4593 0.0156 -0.0239 -0.0635 94 LEU A CG 785 C CD1 . LEU A 94 ? 0.4316 0.5147 0.4255 0.0314 -0.0286 -0.0582 94 LEU A CD1 786 C CD2 . LEU A 94 ? 0.5186 0.6482 0.5292 0.0165 -0.0334 -0.0657 94 LEU A CD2 787 N N . TYR A 95 ? 0.3389 0.5379 0.4790 -0.0188 0.0331 -0.1535 95 TYR A N 788 C CA . TYR A 95 ? 0.3239 0.5517 0.4957 -0.0289 0.0330 -0.1438 95 TYR A CA 789 C C . TYR A 95 ? 0.4104 0.6565 0.5990 -0.0208 0.0387 -0.1568 95 TYR A C 790 O O . TYR A 95 ? 0.4830 0.7460 0.7066 -0.0181 0.0357 -0.1549 95 TYR A O 791 C CB . TYR A 95 ? 0.3777 0.6232 0.5403 -0.0550 0.0353 -0.1250 95 TYR A CB 792 C CG . TYR A 95 ? 0.3552 0.5954 0.5247 -0.0674 0.0269 -0.1015 95 TYR A CG 793 C CD1 . TYR A 95 ? 0.3827 0.6031 0.5703 -0.0556 0.0213 -0.1016 95 TYR A CD1 794 C CD2 . TYR A 95 ? 0.3270 0.5870 0.4882 -0.0936 0.0250 -0.0780 95 TYR A CD2 795 C CE1 . TYR A 95 ? 0.3596 0.5756 0.5626 -0.0670 0.0158 -0.0806 95 TYR A CE1 796 C CE2 . TYR A 95 ? 0.3333 0.5910 0.5085 -0.1052 0.0163 -0.0527 95 TYR A CE2 797 C CZ . TYR A 95 ? 0.3139 0.5483 0.5143 -0.0909 0.0124 -0.0539 95 TYR A CZ 798 O OH . TYR A 95 ? 0.3134 0.5461 0.5358 -0.1030 0.0056 -0.0282 95 TYR A OH 799 N N A ASN A 96 ? 0.4280 0.6688 0.5967 -0.0163 0.0480 -0.1722 96 ASN A N 800 N N B ASN A 96 ? 0.4263 0.6710 0.5967 -0.0183 0.0488 -0.1715 96 ASN A N 801 C CA A ASN A 96 ? 0.4433 0.7032 0.6271 -0.0129 0.0580 -0.1853 96 ASN A CA 802 C CA B ASN A 96 ? 0.4574 0.7241 0.6495 -0.0141 0.0564 -0.1823 96 ASN A CA 803 C C A ASN A 96 ? 0.4889 0.7453 0.6968 0.0112 0.0537 -0.1966 96 ASN A C 804 C C B ASN A 96 ? 0.4861 0.7450 0.6962 0.0105 0.0535 -0.1958 96 ASN A C 805 O O A ASN A 96 ? 0.5001 0.7636 0.7211 0.0188 0.0631 -0.2101 96 ASN A O 806 O O B ASN A 96 ? 0.4969 0.7615 0.7176 0.0177 0.0632 -0.2096 96 ASN A O 807 C CB A ASN A 96 ? 0.4251 0.6811 0.5833 -0.0220 0.0740 -0.2006 96 ASN A CB 808 C CB B ASN A 96 ? 0.3947 0.6742 0.5683 -0.0295 0.0732 -0.1930 96 ASN A CB 809 C CG A ASN A 96 ? 0.4487 0.7307 0.6213 -0.0270 0.0895 -0.2153 96 ASN A CG 810 C CG B ASN A 96 ? 0.3834 0.6365 0.5310 -0.0259 0.0824 -0.2100 96 ASN A CG 811 O OD1 A ASN A 96 ? 0.5279 0.8345 0.7254 -0.0280 0.0871 -0.2084 96 ASN A OD1 812 O OD1 B ASN A 96 ? 0.4082 0.6350 0.5394 -0.0210 0.0744 -0.2044 96 ASN A OD1 813 N ND2 A ASN A 96 ? 0.5065 0.7836 0.6674 -0.0316 0.1079 -0.2381 96 ASN A ND2 814 N ND2 B ASN A 96 ? 0.4164 0.6771 0.5658 -0.0291 0.1008 -0.2319 96 ASN A ND2 815 N N . LYS A 97 ? 0.5471 0.7964 0.7630 0.0210 0.0403 -0.1914 97 LYS A N 816 C CA . LYS A 97 ? 0.5501 0.8010 0.7823 0.0399 0.0331 -0.1985 97 LYS A CA 817 C C . LYS A 97 ? 0.4985 0.7769 0.7645 0.0428 0.0355 -0.2042 97 LYS A C 818 O O . LYS A 97 ? 0.5631 0.8589 0.8459 0.0321 0.0362 -0.2002 97 LYS A O 819 C CB . LYS A 97 ? 0.6618 0.9087 0.8909 0.0433 0.0194 -0.1942 97 LYS A CB 820 C CG . LYS A 97 ? 0.7081 0.9678 0.9554 0.0316 0.0174 -0.1920 97 LYS A CG 821 C CD . LYS A 97 ? 0.8028 1.0742 1.0622 0.0351 0.0078 -0.1998 97 LYS A CD 822 C CE . LYS A 97 ? 0.8247 1.0812 1.0538 0.0395 0.0005 -0.1978 97 LYS A CE 823 N NZ . LYS A 97 ? 0.8793 1.1124 1.0886 0.0310 0.0042 -0.1905 97 LYS A NZ 824 N N . ALA A 98 ? 0.4139 0.6965 0.6965 0.0570 0.0370 -0.2115 98 ALA A N 825 C CA . ALA A 98 ? 0.5444 0.8534 0.8625 0.0620 0.0376 -0.2166 98 ALA A CA 826 C C . ALA A 98 ? 0.6188 0.9399 0.9514 0.0711 0.0199 -0.2140 98 ALA A C 827 O O . ALA A 98 ? 0.6661 1.0120 1.0278 0.0728 0.0161 -0.2176 98 ALA A O 828 C CB . ALA A 98 ? 0.6646 0.9746 1.0007 0.0707 0.0510 -0.2262 98 ALA A CB 829 N N . ASP A 99 ? 0.8656 1.1727 1.1759 0.0738 0.0092 -0.2078 99 ASP A N 830 C CA . ASP A 99 ? 0.9272 1.2510 1.2444 0.0799 -0.0080 -0.2036 99 ASP A CA 831 C C . ASP A 99 ? 0.9521 1.2988 1.2740 0.0689 -0.0164 -0.2111 99 ASP A C 832 O O . ASP A 99 ? 0.9413 1.2890 1.2716 0.0584 -0.0086 -0.2185 99 ASP A O 833 N N . ASP A 100 ? 0.9389 1.3068 1.2591 0.0694 -0.0320 -0.2083 100 ASP A N 834 C CA . ASP A 100 ? 0.8825 1.2799 1.2090 0.0561 -0.0391 -0.2215 100 ASP A CA 835 C C . ASP A 100 ? 0.9211 1.3070 1.2376 0.0415 -0.0302 -0.2346 100 ASP A C 836 O O . ASP A 100 ? 0.8503 1.2456 1.1955 0.0327 -0.0225 -0.2485 100 ASP A O 837 N N . GLU A 101 ? 0.9238 1.2904 1.2074 0.0388 -0.0310 -0.2290 101 GLU A N 838 C CA . GLU A 101 ? 0.9278 1.2865 1.1856 0.0483 -0.0412 -0.2106 101 GLU A CA 839 C C . GLU A 101 ? 0.9157 1.2805 1.1420 0.0368 -0.0480 -0.2109 101 GLU A C 840 O O . GLU A 101 ? 1.0199 1.3607 1.2206 0.0403 -0.0485 -0.1978 101 GLU A O 841 N N . GLU A 104 ? 0.8630 1.2346 0.9839 0.0315 -0.0918 -0.1321 104 GLU A N 842 C CA . GLU A 104 ? 0.9337 1.3295 1.0213 0.0156 -0.1026 -0.1195 104 GLU A CA 843 C C . GLU A 104 ? 1.0611 1.4162 1.1246 0.0172 -0.0928 -0.1154 104 GLU A C 844 O O . GLU A 104 ? 1.0286 1.3394 1.1038 0.0340 -0.0845 -0.1094 104 GLU A O 845 N N . PRO A 105 ? 1.1286 1.5016 1.1585 -0.0028 -0.0923 -0.1214 105 PRO A N 846 C CA . PRO A 105 ? 1.1515 1.4903 1.1587 -0.0036 -0.0835 -0.1171 105 PRO A CA 847 C C . PRO A 105 ? 1.2075 1.5482 1.2031 0.0003 -0.0990 -0.0779 105 PRO A C 848 O O . PRO A 105 ? 1.2966 1.6808 1.2936 -0.0057 -0.1183 -0.0543 105 PRO A O 849 C CB . PRO A 105 ? 1.1448 1.5089 1.1289 -0.0294 -0.0732 -0.1461 105 PRO A CB 850 C CG . PRO A 105 ? 1.1120 1.5176 1.1105 -0.0412 -0.0736 -0.1707 105 PRO A CG 851 C CD . PRO A 105 ? 1.1147 1.5396 1.1290 -0.0289 -0.0937 -0.1436 105 PRO A CD 852 N N . VAL A 106 ? 1.0043 1.3013 0.9929 0.0087 -0.0916 -0.0686 106 VAL A N 853 C CA . VAL A 106 ? 0.9657 1.2598 0.9479 0.0115 -0.1039 -0.0317 106 VAL A CA 854 C C . VAL A 106 ? 0.9933 1.2526 0.9513 0.0074 -0.0914 -0.0366 106 VAL A C 855 O O . VAL A 106 ? 1.0057 1.2182 0.9728 0.0190 -0.0780 -0.0478 106 VAL A O 856 C CB . VAL A 106 ? 1.0007 1.2679 1.0246 0.0356 -0.1094 -0.0067 106 VAL A CB 857 C CG1 . VAL A 106 ? 1.0310 1.2853 1.0581 0.0393 -0.1179 0.0296 106 VAL A CG1 858 C CG2 . VAL A 106 ? 1.0740 1.3787 1.1302 0.0404 -0.1243 0.0063 106 VAL A CG2 859 N N . ASN A 107 ? 0.9889 1.2745 0.9158 -0.0111 -0.0959 -0.0272 107 ASN A N 860 C CA . ASN A 107 ? 0.9802 1.2388 0.8843 -0.0186 -0.0815 -0.0385 107 ASN A CA 861 C C . ASN A 107 ? 0.8719 1.0893 0.7800 -0.0060 -0.0831 -0.0112 107 ASN A C 862 O O . ASN A 107 ? 0.8100 1.0323 0.7332 0.0022 -0.0983 0.0246 107 ASN A O 863 C CB . ASN A 107 ? 1.0085 1.3133 0.8779 -0.0471 -0.0796 -0.0491 107 ASN A CB 864 C CG . ASN A 107 ? 1.0413 1.3978 0.8951 -0.0596 -0.1013 -0.0139 107 ASN A CG 865 O OD1 . ASN A 107 ? 1.0357 1.3816 0.9053 -0.0461 -0.1165 0.0271 107 ASN A OD1 866 N ND2 . ASN A 107 ? 1.0947 1.5115 0.9221 -0.0879 -0.1030 -0.0287 107 ASN A ND2 867 N N . THR A 108 ? 0.5886 0.7669 0.4892 -0.0057 -0.0672 -0.0277 108 THR A N 868 C CA . THR A 108 ? 0.5636 0.6957 0.4714 0.0063 -0.0648 -0.0113 108 THR A CA 869 C C . THR A 108 ? 0.5319 0.6479 0.4170 -0.0055 -0.0535 -0.0190 108 THR A C 870 O O . THR A 108 ? 0.6404 0.7743 0.5120 -0.0206 -0.0437 -0.0420 108 THR A O 871 C CB . THR A 108 ? 0.7037 0.7961 0.6353 0.0216 -0.0555 -0.0262 108 THR A CB 872 O OG1 . THR A 108 ? 0.6477 0.7412 0.5762 0.0144 -0.0434 -0.0565 108 THR A OG1 873 C CG2 . THR A 108 ? 0.7610 0.8611 0.7235 0.0361 -0.0638 -0.0173 108 THR A CG2 874 N N . ASN A 109 ? 0.5276 0.6080 0.4155 0.0016 -0.0531 -0.0017 109 ASN A N 875 C CA . ASN A 109 ? 0.5415 0.6032 0.4126 -0.0079 -0.0431 -0.0059 109 ASN A CA 876 C C . ASN A 109 ? 0.5997 0.6156 0.4846 0.0010 -0.0340 -0.0163 109 ASN A C 877 O O . ASN A 109 ? 0.5766 0.5746 0.4806 0.0141 -0.0364 -0.0136 109 ASN A O 878 C CB . ASN A 109 ? 0.6160 0.6776 0.4788 -0.0099 -0.0519 0.0268 109 ASN A CB 879 C CG . ASN A 109 ? 0.7131 0.8290 0.5570 -0.0246 -0.0627 0.0426 109 ASN A CG 880 O OD1 . ASN A 109 ? 0.7390 0.8855 0.5596 -0.0432 -0.0548 0.0225 109 ASN A OD1 881 N ND2 . ASN A 109 ? 0.8141 0.9466 0.6725 -0.0185 -0.0804 0.0784 109 ASN A ND2 882 N N . VAL A 110 ? 0.5026 0.5027 0.3803 -0.0082 -0.0231 -0.0275 110 VAL A N 883 C CA . VAL A 110 ? 0.5167 0.4779 0.4029 -0.0044 -0.0176 -0.0298 110 VAL A CA 884 C C . VAL A 110 ? 0.5668 0.5066 0.4438 -0.0069 -0.0183 -0.0116 110 VAL A C 885 O O . VAL A 110 ? 0.6033 0.5603 0.4667 -0.0137 -0.0206 0.0003 110 VAL A O 886 C CB . VAL A 110 ? 0.5652 0.5238 0.4598 -0.0133 -0.0073 -0.0487 110 VAL A CB 887 C CG1 . VAL A 110 ? 0.5649 0.5486 0.4728 -0.0123 -0.0060 -0.0659 110 VAL A CG1 888 C CG2 . VAL A 110 ? 0.6187 0.5843 0.5083 -0.0261 0.0002 -0.0507 110 VAL A CG2 889 N N . VAL A 111 ? 0.6094 0.5151 0.4933 -0.0039 -0.0158 -0.0103 111 VAL A N 890 C CA . VAL A 111 ? 0.5704 0.4535 0.4483 -0.0086 -0.0146 0.0031 111 VAL A CA 891 C C . VAL A 111 ? 0.5062 0.3789 0.3827 -0.0202 -0.0066 -0.0076 111 VAL A C 892 O O . VAL A 111 ? 0.5880 0.4509 0.4720 -0.0225 -0.0041 -0.0185 111 VAL A O 893 C CB . VAL A 111 ? 0.5717 0.4252 0.4638 -0.0001 -0.0165 0.0116 111 VAL A CB 894 C CG1 . VAL A 111 ? 0.6648 0.4923 0.5532 -0.0069 -0.0139 0.0213 111 VAL A CG1 895 C CG2 . VAL A 111 ? 0.6235 0.4897 0.5309 0.0115 -0.0255 0.0303 111 VAL A CG2 896 N N . LEU A 112 ? 0.5782 0.4559 0.4481 -0.0294 -0.0027 -0.0025 112 LEU A N 897 C CA . LEU A 112 ? 0.6132 0.4838 0.4930 -0.0405 0.0047 -0.0086 112 LEU A CA 898 C C . LEU A 112 ? 0.6317 0.4768 0.5071 -0.0453 0.0045 0.0060 112 LEU A C 899 O O . LEU A 112 ? 0.5932 0.4402 0.4583 -0.0459 0.0043 0.0180 112 LEU A O 900 C CB . LEU A 112 ? 0.5817 0.4790 0.4683 -0.0488 0.0136 -0.0191 112 LEU A CB 901 C CG . LEU A 112 ? 0.4928 0.3858 0.4018 -0.0606 0.0237 -0.0218 112 LEU A CG 902 C CD1 . LEU A 112 ? 0.5627 0.4497 0.4999 -0.0633 0.0232 -0.0245 112 LEU A CD1 903 C CD2 . LEU A 112 ? 0.4993 0.4205 0.4174 -0.0693 0.0367 -0.0375 112 LEU A CD2 904 N N . ARG A 113 ? 0.5818 0.4077 0.4648 -0.0511 0.0039 0.0058 113 ARG A N 905 C CA . ARG A 113 ? 0.5810 0.3826 0.4614 -0.0575 0.0031 0.0177 113 ARG A CA 906 C C . ARG A 113 ? 0.5966 0.4032 0.4924 -0.0698 0.0082 0.0214 113 ARG A C 907 O O . ARG A 113 ? 0.5620 0.3862 0.4775 -0.0739 0.0121 0.0141 113 ARG A O 908 C CB . ARG A 113 ? 0.6966 0.4801 0.5756 -0.0611 -0.0002 0.0130 113 ARG A CB 909 C CG . ARG A 113 ? 0.6987 0.4561 0.5749 -0.0677 -0.0010 0.0213 113 ARG A CG 910 C CD . ARG A 113 ? 0.6838 0.4281 0.5578 -0.0738 -0.0009 0.0084 113 ARG A CD 911 N NE . ARG A 113 ? 0.7542 0.5132 0.6266 -0.0906 -0.0029 0.0028 113 ARG A NE 912 C CZ . ARG A 113 ? 0.8331 0.5930 0.6983 -0.1024 -0.0018 -0.0117 113 ARG A CZ 913 N NH1 . ARG A 113 ? 0.8512 0.5936 0.7162 -0.0973 0.0044 -0.0271 113 ARG A NH1 914 N NH2 . ARG A 113 ? 0.7808 0.5622 0.6434 -0.1212 -0.0059 -0.0103 113 ARG A NH2 915 N N . TYR A 114 ? 0.6310 0.4223 0.5253 -0.0753 0.0092 0.0337 114 TYR A N 916 C CA . TYR A 114 ? 0.5878 0.3836 0.5026 -0.0860 0.0159 0.0391 114 TYR A CA 917 C C . TYR A 114 ? 0.5247 0.3256 0.4674 -0.0962 0.0139 0.0403 114 TYR A C 918 O O . TYR A 114 ? 0.5930 0.4047 0.5698 -0.1034 0.0211 0.0428 114 TYR A O 919 C CB . TYR A 114 ? 0.6883 0.4632 0.5969 -0.0908 0.0151 0.0542 114 TYR A CB 920 C CG . TYR A 114 ? 0.6804 0.4348 0.5876 -0.0978 0.0065 0.0594 114 TYR A CG 921 C CD1 . TYR A 114 ? 0.7757 0.5137 0.6656 -0.0922 0.0016 0.0554 114 TYR A CD1 922 C CD2 . TYR A 114 ? 0.7302 0.4856 0.6581 -0.1126 0.0041 0.0674 114 TYR A CD2 923 C CE1 . TYR A 114 ? 0.7933 0.5170 0.6810 -0.1031 -0.0029 0.0529 114 TYR A CE1 924 C CE2 . TYR A 114 ? 0.7087 0.4537 0.6305 -0.1245 -0.0044 0.0706 114 TYR A CE2 925 C CZ . TYR A 114 ? 0.7718 0.5009 0.6703 -0.1207 -0.0065 0.0602 114 TYR A CZ 926 O OH . TYR A 114 ? 0.8280 0.5499 0.7191 -0.1366 -0.0117 0.0566 114 TYR A OH 927 N N . ASP A 115 ? 0.6298 0.4273 0.5642 -0.0987 0.0051 0.0392 115 ASP A N 928 C CA . ASP A 115 ? 0.5855 0.3956 0.5455 -0.1125 0.0000 0.0472 115 ASP A CA 929 C C . ASP A 115 ? 0.5717 0.4048 0.5500 -0.1091 0.0013 0.0388 115 ASP A C 930 O O . ASP A 115 ? 0.5892 0.4372 0.5865 -0.1206 -0.0052 0.0480 115 ASP A O 931 C CB . ASP A 115 ? 0.6672 0.4692 0.6068 -0.1248 -0.0097 0.0510 115 ASP A CB 932 C CG . ASP A 115 ? 0.7348 0.5349 0.6476 -0.1173 -0.0101 0.0335 115 ASP A CG 933 O OD1 . ASP A 115 ? 0.6701 0.4683 0.5759 -0.0997 -0.0051 0.0230 115 ASP A OD1 934 O OD2 . ASP A 115 ? 0.8095 0.6131 0.7096 -0.1307 -0.0148 0.0297 115 ASP A OD2 935 N N . GLY A 116 ? 0.5540 0.3939 0.5278 -0.0957 0.0090 0.0235 116 GLY A N 936 C CA . GLY A 116 ? 0.5172 0.3783 0.5109 -0.0922 0.0114 0.0132 116 GLY A CA 937 C C . GLY A 116 ? 0.5139 0.3771 0.4811 -0.0859 0.0051 0.0045 116 GLY A C 938 O O . GLY A 116 ? 0.4663 0.3470 0.4467 -0.0825 0.0062 -0.0039 116 GLY A O 939 N N . LEU A 117 ? 0.4860 0.4941 0.4626 -0.0103 0.0238 0.1398 117 LEU A N 940 C CA . LEU A 117 ? 0.4461 0.4364 0.4156 -0.0105 0.0122 0.1295 117 LEU A CA 941 C C . LEU A 117 ? 0.4427 0.4333 0.3910 -0.0048 0.0128 0.1284 117 LEU A C 942 O O . LEU A 117 ? 0.4742 0.4693 0.4196 -0.0049 0.0152 0.1421 117 LEU A O 943 C CB . LEU A 117 ? 0.5261 0.5027 0.5108 -0.0181 0.0023 0.1367 117 LEU A CB 944 C CG . LEU A 117 ? 0.5056 0.4641 0.4830 -0.0169 -0.0084 0.1249 117 LEU A CG 945 C CD1 . LEU A 117 ? 0.5136 0.4680 0.4943 -0.0177 -0.0127 0.1106 117 LEU A CD1 946 C CD2 . LEU A 117 ? 0.6302 0.5735 0.6182 -0.0224 -0.0162 0.1333 117 LEU A CD2 947 N N . ILE A 118 ? 0.4496 0.4365 0.3836 -0.0002 0.0103 0.1130 118 ILE A N 948 C CA . ILE A 118 ? 0.4934 0.4832 0.4078 0.0048 0.0095 0.1107 118 ILE A CA 949 C C . ILE A 118 ? 0.4150 0.3902 0.3289 0.0049 -0.0019 0.1053 118 ILE A C 950 O O . ILE A 118 ? 0.4745 0.4399 0.3937 0.0037 -0.0069 0.0937 118 ILE A O 951 C CB . ILE A 118 ? 0.4930 0.4920 0.3912 0.0097 0.0160 0.0960 118 ILE A CB 952 C CG1 . ILE A 118 ? 0.5664 0.5815 0.4606 0.0116 0.0287 0.1025 118 ILE A CG1 953 C CG2 . ILE A 118 ? 0.5629 0.5643 0.4420 0.0137 0.0115 0.0895 118 ILE A CG2 954 C CD1 . ILE A 118 ? 0.6229 0.6443 0.5049 0.0158 0.0367 0.0869 118 ILE A CD1 955 N N . THR A 119 ? 0.4755 0.4500 0.3839 0.0069 -0.0055 0.1151 119 THR A N 956 C CA . THR A 119 ? 0.4794 0.4422 0.3868 0.0092 -0.0153 0.1109 119 THR A CA 957 C C . THR A 119 ? 0.5483 0.5223 0.4368 0.0156 -0.0162 0.1085 119 THR A C 958 O O . THR A 119 ? 0.5455 0.5311 0.4248 0.0178 -0.0127 0.1205 119 THR A O 959 C CB . THR A 119 ? 0.5220 0.4720 0.4423 0.0068 -0.0201 0.1259 119 THR A CB 960 O OG1 . THR A 119 ? 0.5514 0.4925 0.4897 -0.0006 -0.0202 0.1273 119 THR A OG1 961 C CG2 . THR A 119 ? 0.5561 0.4934 0.4764 0.0106 -0.0291 0.1202 119 THR A CG2 962 N N . TRP A 120 ? 0.4897 0.4622 0.3727 0.0180 -0.0210 0.0931 120 TRP A N 963 C CA . TRP A 120 ? 0.4927 0.4787 0.3588 0.0229 -0.0227 0.0880 120 TRP A CA 964 C C . TRP A 120 ? 0.4655 0.4453 0.3345 0.0266 -0.0324 0.0844 120 TRP A C 965 O O . TRP A 120 ? 0.5002 0.4719 0.3751 0.0257 -0.0354 0.0712 120 TRP A O 966 C CB . TRP A 120 ? 0.4695 0.4634 0.3263 0.0220 -0.0178 0.0706 120 TRP A CB 967 C CG . TRP A 120 ? 0.5242 0.5338 0.3632 0.0252 -0.0194 0.0638 120 TRP A CG 968 C CD1 . TRP A 120 ? 0.5974 0.6200 0.4248 0.0291 -0.0223 0.0744 120 TRP A CD1 969 C CD2 . TRP A 120 ? 0.5410 0.5558 0.3724 0.0243 -0.0188 0.0451 120 TRP A CD2 970 N NE1 . TRP A 120 ? 0.6353 0.6728 0.4470 0.0304 -0.0244 0.0623 120 TRP A NE1 971 C CE2 . TRP A 120 ? 0.5557 0.5877 0.3705 0.0270 -0.0221 0.0436 120 TRP A CE2 972 C CE3 . TRP A 120 ? 0.5074 0.5140 0.3449 0.0212 -0.0159 0.0299 120 TRP A CE3 973 C CZ2 . TRP A 120 ? 0.5902 0.6311 0.3952 0.0255 -0.0229 0.0259 120 TRP A CZ2 974 C CZ3 . TRP A 120 ? 0.6294 0.6431 0.4577 0.0201 -0.0156 0.0137 120 TRP A CZ3 975 C CH2 . TRP A 120 ? 0.6040 0.6344 0.4167 0.0218 -0.0192 0.0110 120 TRP A CH2 976 N N . ASP A 121 ? 0.5624 0.5465 0.4283 0.0312 -0.0367 0.0977 121 ASP A N 977 C CA . ASP A 121 ? 0.6278 0.6099 0.4964 0.0368 -0.0454 0.0967 121 ASP A CA 978 C C . ASP A 121 ? 0.6865 0.6905 0.5389 0.0407 -0.0481 0.0917 121 ASP A C 979 O O . ASP A 121 ? 0.5788 0.5980 0.4176 0.0420 -0.0457 0.1010 121 ASP A O 980 C CB . ASP A 121 ? 0.6246 0.5979 0.5015 0.0404 -0.0486 0.1164 121 ASP A CB 981 C CG . ASP A 121 ? 0.6595 0.6091 0.5544 0.0360 -0.0481 0.1197 121 ASP A CG 982 O OD1 . ASP A 121 ? 0.6947 0.6316 0.5985 0.0349 -0.0510 0.1069 121 ASP A OD1 983 O OD2 . ASP A 121 ? 0.6972 0.6415 0.5977 0.0333 -0.0449 0.1353 121 ASP A OD2 984 N N . ALA A 122 ? 0.6258 0.6331 0.4795 0.0421 -0.0530 0.0774 122 ALA A N 985 C CA . ALA A 122 ? 0.6819 0.7115 0.5223 0.0445 -0.0571 0.0708 122 ALA A CA 986 C C . ALA A 122 ? 0.6737 0.7059 0.5232 0.0489 -0.0654 0.0649 122 ALA A C 987 O O . ALA A 122 ? 0.6656 0.6850 0.5272 0.0474 -0.0653 0.0549 122 ALA A O 988 C CB . ALA A 122 ? 0.6977 0.7342 0.5283 0.0385 -0.0515 0.0534 122 ALA A CB 989 N N . PRO A 123 ? 0.7476 0.7989 0.5910 0.0546 -0.0724 0.0712 123 PRO A N 990 C CA . PRO A 123 ? 0.6836 0.7418 0.5371 0.0594 -0.0802 0.0659 123 PRO A CA 991 C C . PRO A 123 ? 0.7403 0.8088 0.5917 0.0535 -0.0802 0.0446 123 PRO A C 992 O O . PRO A 123 ? 0.6702 0.7453 0.5085 0.0471 -0.0758 0.0355 123 PRO A O 993 C CB . PRO A 123 ? 0.7338 0.8143 0.5789 0.0663 -0.0877 0.0797 123 PRO A CB 994 C CG . PRO A 123 ? 0.7535 0.8470 0.5767 0.0615 -0.0835 0.0802 123 PRO A CG 995 C CD . PRO A 123 ? 0.6845 0.7561 0.5095 0.0563 -0.0734 0.0813 123 PRO A CD 996 N N . ALA A 124 ? 0.6407 0.7107 0.5058 0.0557 -0.0843 0.0367 124 ALA A N 997 C CA . ALA A 124 ? 0.6701 0.7498 0.5362 0.0494 -0.0840 0.0176 124 ALA A CA 998 C C . ALA A 124 ? 0.6553 0.7474 0.5358 0.0543 -0.0909 0.0145 124 ALA A C 999 O O . ALA A 124 ? 0.7036 0.7875 0.5968 0.0622 -0.0930 0.0234 124 ALA A O 1000 C CB . ALA A 124 ? 0.6241 0.6829 0.4948 0.0428 -0.0754 0.0067 124 ALA A CB 1001 N N . ILE A 125 ? 0.6571 0.7687 0.5368 0.0491 -0.0938 0.0012 125 ILE A N 1002 C CA . ILE A 125 ? 0.6023 0.7293 0.4978 0.0521 -0.0995 -0.0035 125 ILE A CA 1003 C C . ILE A 125 ? 0.6597 0.7825 0.5618 0.0431 -0.0940 -0.0212 125 ILE A C 1004 O O . ILE A 125 ? 0.7037 0.8309 0.5962 0.0338 -0.0917 -0.0326 125 ILE A O 1005 C CB . ILE A 125 ? 0.6656 0.8254 0.5561 0.0532 -0.1097 -0.0024 125 ILE A CB 1006 C CG1 . ILE A 125 ? 0.6531 0.8189 0.5359 0.0629 -0.1153 0.0179 125 ILE A CG1 1007 C CG2 . ILE A 125 ? 0.6566 0.8349 0.5666 0.0554 -0.1152 -0.0081 125 ILE A CG2 1008 C CD1 . ILE A 125 ? 0.7361 0.9368 0.6088 0.0639 -0.1262 0.0207 125 ILE A CD1 1009 N N . THR A 126 ? 0.6714 0.7841 0.5896 0.0460 -0.0910 -0.0233 126 THR A N 1010 C CA . THR A 126 ? 0.6149 0.7220 0.5402 0.0380 -0.0845 -0.0376 126 THR A CA 1011 C C . THR A 126 ? 0.5729 0.7002 0.5155 0.0391 -0.0881 -0.0433 126 THR A C 1012 O O . THR A 126 ? 0.5909 0.7257 0.5448 0.0491 -0.0924 -0.0353 126 THR A O 1013 C CB . THR A 126 ? 0.6797 0.7593 0.6086 0.0392 -0.0765 -0.0367 126 THR A CB 1014 O OG1 . THR A 126 ? 0.6876 0.7625 0.6269 0.0499 -0.0788 -0.0279 126 THR A OG1 1015 C CG2 . THR A 126 ? 0.7239 0.7845 0.6389 0.0365 -0.0721 -0.0323 126 THR A CG2 1016 N N . LYS A 127 ? 0.5540 0.6900 0.4999 0.0288 -0.0858 -0.0567 127 LYS A N 1017 C CA . LYS A 127 ? 0.5325 0.6873 0.4972 0.0274 -0.0872 -0.0631 127 LYS A CA 1018 C C . LYS A 127 ? 0.5751 0.7148 0.5457 0.0202 -0.0769 -0.0722 127 LYS A C 1019 O O . LYS A 127 ? 0.5880 0.7174 0.5505 0.0102 -0.0718 -0.0801 127 LYS A O 1020 C CB . LYS A 127 ? 0.6014 0.7857 0.5673 0.0204 -0.0953 -0.0704 127 LYS A CB 1021 C CG . LYS A 127 ? 0.6697 0.8713 0.6260 0.0270 -0.1061 -0.0608 127 LYS A CG 1022 C CD . LYS A 127 ? 0.6965 0.9312 0.6543 0.0197 -0.1157 -0.0690 127 LYS A CD 1023 C CE . LYS A 127 ? 0.7603 1.0236 0.7411 0.0257 -0.1231 -0.0653 127 LYS A CE 1024 N NZ . LYS A 127 ? 0.8751 1.1735 0.8592 0.0173 -0.1337 -0.0740 127 LYS A NZ 1025 N N . SER A 128 ? 0.4707 0.6086 0.4553 0.0257 -0.0731 -0.0706 128 SER A N 1026 C CA . SER A 128 ? 0.5721 0.6942 0.5598 0.0204 -0.0628 -0.0765 128 SER A CA 1027 C C . SER A 128 ? 0.4912 0.6264 0.4979 0.0246 -0.0603 -0.0776 128 SER A C 1028 O O . SER A 128 ? 0.4851 0.6335 0.5011 0.0348 -0.0654 -0.0720 128 SER A O 1029 C CB . SER A 128 ? 0.6170 0.7097 0.5926 0.0243 -0.0575 -0.0710 128 SER A CB 1030 O OG . SER A 128 ? 0.5343 0.6223 0.5113 0.0364 -0.0608 -0.0621 128 SER A OG 1031 N N . SER A 129 ? 0.4730 0.6043 0.4858 0.0173 -0.0516 -0.0839 129 SER A N 1032 C CA . SER A 129 ? 0.5382 0.6848 0.5696 0.0195 -0.0474 -0.0858 129 SER A CA 1033 C C . SER A 129 ? 0.5056 0.6360 0.5349 0.0299 -0.0414 -0.0816 129 SER A C 1034 O O . SER A 129 ? 0.4879 0.5931 0.5021 0.0304 -0.0382 -0.0797 129 SER A O 1035 C CB . SER A 129 ? 0.6049 0.7541 0.6436 0.0066 -0.0396 -0.0933 129 SER A CB 1036 O OG . SER A 129 ? 0.7067 0.8697 0.7482 -0.0044 -0.0450 -0.0996 129 SER A OG 1037 N N . CYS A 130 ? 0.4463 0.5926 0.4916 0.0381 -0.0399 -0.0809 130 CYS A N 1038 C CA . CYS A 130 ? 0.4442 0.5769 0.4882 0.0491 -0.0342 -0.0788 130 CYS A CA 1039 C C . CYS A 130 ? 0.4313 0.5762 0.4884 0.0480 -0.0242 -0.0832 130 CYS A C 1040 O O . CYS A 130 ? 0.5236 0.6926 0.5966 0.0416 -0.0237 -0.0859 130 CYS A O 1041 C CB . CYS A 130 ? 0.4596 0.5988 0.5109 0.0635 -0.0408 -0.0730 130 CYS A CB 1042 S SG . CYS A 130 ? 0.5318 0.6578 0.5684 0.0665 -0.0519 -0.0647 130 CYS A SG 1043 N N . VAL A 131 ? 0.4494 0.5790 0.5000 0.0539 -0.0162 -0.0842 131 VAL A N 1044 C CA . VAL A 131 ? 0.4813 0.6238 0.5431 0.0546 -0.0056 -0.0875 131 VAL A CA 1045 C C . VAL A 131 ? 0.5731 0.7191 0.6424 0.0705 -0.0027 -0.0878 131 VAL A C 1046 O O . VAL A 131 ? 0.4751 0.5989 0.5319 0.0790 -0.0038 -0.0876 131 VAL A O 1047 C CB . VAL A 131 ? 0.4348 0.5597 0.4818 0.0475 0.0035 -0.0892 131 VAL A CB 1048 C CG1 . VAL A 131 ? 0.5757 0.7143 0.6321 0.0494 0.0153 -0.0914 131 VAL A CG1 1049 C CG2 . VAL A 131 ? 0.4887 0.6102 0.5317 0.0325 0.0023 -0.0889 131 VAL A CG2 1050 N N . VAL A 132 ? 0.5086 0.6825 0.5997 0.0744 0.0013 -0.0887 132 VAL A N 1051 C CA . VAL A 132 ? 0.5572 0.7372 0.6587 0.0907 0.0052 -0.0895 132 VAL A CA 1052 C C . VAL A 132 ? 0.5982 0.7624 0.6868 0.0941 0.0173 -0.0946 132 VAL A C 1053 O O . VAL A 132 ? 0.5540 0.7144 0.6331 0.0837 0.0243 -0.0963 132 VAL A O 1054 C CB . VAL A 132 ? 0.4843 0.7026 0.6154 0.0941 0.0067 -0.0885 132 VAL A CB 1055 C CG1 . VAL A 132 ? 0.6141 0.8385 0.7570 0.1121 0.0137 -0.0900 132 VAL A CG1 1056 C CG2 . VAL A 132 ? 0.5659 0.8014 0.7085 0.0923 -0.0073 -0.0834 132 VAL A CG2 1057 N N . ASP A 133 ? 0.5166 0.6699 0.6036 0.1089 0.0193 -0.0971 133 ASP A N 1058 C CA . ASP A 133 ? 0.6220 0.7659 0.6991 0.1147 0.0313 -0.1039 133 ASP A CA 1059 C C . ASP A 133 ? 0.6007 0.7540 0.6942 0.1327 0.0352 -0.1065 133 ASP A C 1060 O O . ASP A 133 ? 0.6354 0.7822 0.7358 0.1422 0.0268 -0.1033 133 ASP A O 1061 C CB . ASP A 133 ? 0.6173 0.7258 0.6671 0.1132 0.0292 -0.1071 133 ASP A CB 1062 C CG . ASP A 133 ? 0.7323 0.8300 0.7713 0.1225 0.0396 -0.1160 133 ASP A CG 1063 O OD1 . ASP A 133 ? 0.6885 0.7758 0.7308 0.1364 0.0394 -0.1202 133 ASP A OD1 1064 O OD2 . ASP A 133 ? 0.7461 0.8460 0.7733 0.1161 0.0484 -0.1188 133 ASP A OD2 1065 N N . VAL A 134 ? 0.5023 0.6709 0.6025 0.1381 0.0486 -0.1116 134 VAL A N 1066 C CA . VAL A 134 ? 0.4552 0.6305 0.5699 0.1568 0.0547 -0.1157 134 VAL A CA 1067 C C . VAL A 134 ? 0.5811 0.7427 0.6781 0.1625 0.0682 -0.1262 134 VAL A C 1068 O O . VAL A 134 ? 0.5666 0.7379 0.6745 0.1770 0.0782 -0.1319 134 VAL A O 1069 C CB . VAL A 134 ? 0.5689 0.7857 0.7166 0.1611 0.0585 -0.1114 134 VAL A CB 1070 C CG1 . VAL A 134 ? 0.5824 0.8146 0.7460 0.1551 0.0437 -0.1020 134 VAL A CG1 1071 C CG2 . VAL A 134 ? 0.5123 0.7510 0.6627 0.1509 0.0709 -0.1127 134 VAL A CG2 1072 N N . THR A 135 ? 0.5365 0.6769 0.6060 0.1513 0.0682 -0.1289 135 THR A N 1073 C CA . THR A 135 ? 0.6434 0.7708 0.6911 0.1543 0.0792 -0.1389 135 THR A CA 1074 C C . THR A 135 ? 0.6062 0.7034 0.6426 0.1668 0.0767 -0.1481 135 THR A C 1075 O O . THR A 135 ? 0.7067 0.8017 0.7392 0.1784 0.0873 -0.1586 135 THR A O 1076 C CB . THR A 135 ? 0.6577 0.7730 0.6800 0.1378 0.0779 -0.1369 135 THR A CB 1077 O OG1 . THR A 135 ? 0.7164 0.8575 0.7499 0.1266 0.0824 -0.1291 135 THR A OG1 1078 C CG2 . THR A 135 ? 0.8110 0.9131 0.8073 0.1406 0.0873 -0.1470 135 THR A CG2 1079 N N . TYR A 136 ? 0.5573 0.6310 0.5887 0.1638 0.0631 -0.1445 136 TYR A N 1080 C CA . TYR A 136 ? 0.6871 0.7279 0.7072 0.1723 0.0594 -0.1524 136 TYR A CA 1081 C C . TYR A 136 ? 0.7223 0.7624 0.7664 0.1873 0.0555 -0.1492 136 TYR A C 1082 O O . TYR A 136 ? 0.6393 0.6983 0.7036 0.1869 0.0489 -0.1376 136 TYR A O 1083 C CB . TYR A 136 ? 0.7207 0.7355 0.7217 0.1595 0.0474 -0.1490 136 TYR A CB 1084 C CG . TYR A 136 ? 0.7414 0.7549 0.7191 0.1452 0.0496 -0.1504 136 TYR A CG 1085 C CD1 . TYR A 136 ? 0.9077 0.9120 0.8641 0.1466 0.0577 -0.1623 136 TYR A CD1 1086 C CD2 . TYR A 136 ? 0.7585 0.7797 0.7347 0.1308 0.0436 -0.1398 136 TYR A CD2 1087 C CE1 . TYR A 136 ? 0.8657 0.8705 0.8006 0.1342 0.0591 -0.1616 136 TYR A CE1 1088 C CE2 . TYR A 136 ? 0.8424 0.8618 0.7989 0.1189 0.0458 -0.1395 136 TYR A CE2 1089 C CZ . TYR A 136 ? 0.9535 0.9656 0.8897 0.1208 0.0533 -0.1494 136 TYR A CZ 1090 O OH . TYR A 136 ? 1.0143 1.0264 0.9311 0.1098 0.0549 -0.1472 136 TYR A OH 1091 N N . PHE A 137 ? 0.6271 0.6448 0.6686 0.2006 0.0592 -0.1593 137 PHE A N 1092 C CA . PHE A 137 ? 0.5817 0.5949 0.6459 0.2165 0.0563 -0.1557 137 PHE A CA 1093 C C . PHE A 137 ? 0.5434 0.5488 0.6129 0.2099 0.0407 -0.1412 137 PHE A C 1094 O O . PHE A 137 ? 0.5905 0.5768 0.6408 0.1965 0.0330 -0.1397 137 PHE A O 1095 C CB . PHE A 137 ? 0.7059 0.6861 0.7616 0.2284 0.0612 -0.1699 137 PHE A CB 1096 C CG . PHE A 137 ? 0.7342 0.7043 0.8133 0.2456 0.0587 -0.1656 137 PHE A CG 1097 C CD1 . PHE A 137 ? 0.7586 0.7488 0.8619 0.2638 0.0686 -0.1671 137 PHE A CD1 1098 C CD2 . PHE A 137 ? 0.8937 0.8352 0.9723 0.2440 0.0468 -0.1587 137 PHE A CD2 1099 C CE1 . PHE A 137 ? 0.7246 0.7056 0.8513 0.2811 0.0662 -0.1614 137 PHE A CE1 1100 C CE2 . PHE A 137 ? 0.9192 0.8504 1.0203 0.2606 0.0447 -0.1525 137 PHE A CE2 1101 C CZ . PHE A 137 ? 0.7556 0.7064 0.8808 0.2794 0.0541 -0.1536 137 PHE A CZ 1102 N N . PRO A 138 ? 0.6761 0.6986 0.7716 0.2194 0.0359 -0.1297 138 PRO A N 1103 C CA . PRO A 138 ? 0.6115 0.6610 0.7354 0.2360 0.0426 -0.1279 138 PRO A CA 1104 C C . PRO A 138 ? 0.6240 0.7177 0.7616 0.2290 0.0451 -0.1224 138 PRO A C 1105 O O . PRO A 138 ? 0.6460 0.7684 0.8112 0.2395 0.0457 -0.1157 138 PRO A O 1106 C CB . PRO A 138 ? 0.6984 0.7418 0.8402 0.2459 0.0317 -0.1147 138 PRO A CB 1107 C CG . PRO A 138 ? 0.7367 0.7733 0.8638 0.2282 0.0182 -0.1047 138 PRO A CG 1108 C CD . PRO A 138 ? 0.6504 0.6647 0.7477 0.2137 0.0213 -0.1158 138 PRO A CD 1109 N N . PHE A 139 ? 0.4870 0.5857 0.6067 0.2114 0.0464 -0.1246 139 PHE A N 1110 C CA . PHE A 139 ? 0.5067 0.6431 0.6378 0.2040 0.0523 -0.1224 139 PHE A CA 1111 C C . PHE A 139 ? 0.5433 0.7069 0.6949 0.1989 0.0412 -0.1094 139 PHE A C 1112 O O . PHE A 139 ? 0.4875 0.6873 0.6618 0.1997 0.0448 -0.1062 139 PHE A O 1113 C CB . PHE A 139 ? 0.5583 0.7145 0.7051 0.2183 0.0675 -0.1296 139 PHE A CB 1114 C CG . PHE A 139 ? 0.6750 0.8034 0.8024 0.2270 0.0780 -0.1440 139 PHE A CG 1115 C CD1 . PHE A 139 ? 0.7113 0.8199 0.8072 0.2147 0.0807 -0.1518 139 PHE A CD1 1116 C CD2 . PHE A 139 ? 0.7338 0.8560 0.8743 0.2478 0.0850 -0.1503 139 PHE A CD2 1117 C CE1 . PHE A 139 ? 0.6036 0.6882 0.6799 0.2217 0.0893 -0.1664 139 PHE A CE1 1118 C CE2 . PHE A 139 ? 0.7074 0.8028 0.8286 0.2552 0.0947 -0.1660 139 PHE A CE2 1119 C CZ . PHE A 139 ? 0.5607 0.6376 0.6487 0.2414 0.0962 -0.1744 139 PHE A CZ 1120 N N . ASP A 140 ? 0.4718 0.6190 0.6148 0.1926 0.0275 -0.1021 140 ASP A N 1121 C CA . ASP A 140 ? 0.4558 0.6269 0.6139 0.1873 0.0157 -0.0905 140 ASP A CA 1122 C C . ASP A 140 ? 0.4531 0.5961 0.5899 0.1781 0.0048 -0.0863 140 ASP A C 1123 O O . ASP A 140 ? 0.5253 0.6524 0.6634 0.1869 -0.0027 -0.0800 140 ASP A O 1124 C CB . ASP A 140 ? 0.4495 0.6378 0.6351 0.2055 0.0123 -0.0833 140 ASP A CB 1125 C CG . ASP A 140 ? 0.5803 0.8060 0.7860 0.2007 0.0022 -0.0731 140 ASP A CG 1126 O OD1 . ASP A 140 ? 0.5288 0.7585 0.7233 0.1832 -0.0044 -0.0715 140 ASP A OD1 1127 O OD2 . ASP A 140 ? 0.6545 0.9059 0.8874 0.2146 0.0006 -0.0669 140 ASP A OD2 1128 N N . ASN A 141 ? 0.4165 0.5522 0.5340 0.1611 0.0052 -0.0894 141 ASN A N 1129 C CA . ASN A 141 ? 0.4912 0.5992 0.5866 0.1513 -0.0029 -0.0868 141 ASN A CA 1130 C C . ASN A 141 ? 0.4604 0.5805 0.5500 0.1340 -0.0080 -0.0835 141 ASN A C 1131 O O . ASN A 141 ? 0.4926 0.6377 0.5919 0.1270 -0.0039 -0.0852 141 ASN A O 1132 C CB . ASN A 141 ? 0.4528 0.5313 0.5257 0.1486 0.0041 -0.0960 141 ASN A CB 1133 C CG . ASN A 141 ? 0.5735 0.6432 0.6509 0.1641 0.0131 -0.1041 141 ASN A CG 1134 O OD1 . ASN A 141 ? 0.6214 0.6838 0.7105 0.1779 0.0103 -0.1013 141 ASN A OD1 1135 N ND2 . ASN A 141 ? 0.6704 0.7422 0.7395 0.1626 0.0247 -0.1138 141 ASN A ND2 1136 N N . GLN A 142 ? 0.5105 0.6111 0.5845 0.1269 -0.0162 -0.0792 142 GLN A N 1137 C CA . GLN A 142 ? 0.4079 0.5148 0.4741 0.1112 -0.0210 -0.0769 142 GLN A CA 1138 C C . GLN A 142 ? 0.5064 0.5831 0.5490 0.1033 -0.0207 -0.0786 142 GLN A C 1139 O O . GLN A 142 ? 0.5084 0.5607 0.5422 0.1091 -0.0232 -0.0772 142 GLN A O 1140 C CB . GLN A 142 ? 0.3972 0.5164 0.4701 0.1121 -0.0329 -0.0679 142 GLN A CB 1141 C CG . GLN A 142 ? 0.4738 0.6283 0.5719 0.1190 -0.0356 -0.0649 142 GLN A CG 1142 C CD . GLN A 142 ? 0.6050 0.7869 0.7123 0.1064 -0.0331 -0.0695 142 GLN A CD 1143 O OE1 . GLN A 142 ? 0.5241 0.6968 0.6188 0.0930 -0.0289 -0.0744 142 GLN A OE1 1144 N NE2 . GLN A 142 ? 0.5145 0.7298 0.6453 0.1106 -0.0356 -0.0675 142 GLN A NE2 1145 N N . GLN A 143 ? 0.4477 0.5260 0.4816 0.0899 -0.0177 -0.0811 143 GLN A N 1146 C CA . GLN A 143 ? 0.4565 0.5103 0.4700 0.0816 -0.0182 -0.0813 143 GLN A CA 1147 C C . GLN A 143 ? 0.4733 0.5332 0.4843 0.0711 -0.0246 -0.0770 143 GLN A C 1148 O O . GLN A 143 ? 0.4940 0.5714 0.5117 0.0630 -0.0225 -0.0789 143 GLN A O 1149 C CB . GLN A 143 ? 0.5918 0.6416 0.5968 0.0760 -0.0083 -0.0872 143 GLN A CB 1150 C CG . GLN A 143 ? 0.7244 0.7548 0.7110 0.0659 -0.0092 -0.0860 143 GLN A CG 1151 C CD . GLN A 143 ? 0.8243 0.8528 0.8021 0.0601 -0.0002 -0.0894 143 GLN A CD 1152 O OE1 . GLN A 143 ? 0.8400 0.8590 0.8069 0.0511 -0.0001 -0.0871 143 GLN A OE1 1153 N NE2 . GLN A 143 ? 0.8355 0.8738 0.8179 0.0659 0.0080 -0.0941 143 GLN A NE2 1154 N N . CYS A 144 ? 0.4478 0.4940 0.4502 0.0713 -0.0320 -0.0714 144 CYS A N 1155 C CA . CYS A 144 ? 0.4490 0.5024 0.4483 0.0633 -0.0381 -0.0677 144 CYS A CA 1156 C C . CYS A 144 ? 0.5408 0.5723 0.5228 0.0556 -0.0377 -0.0664 144 CYS A C 1157 O O . CYS A 144 ? 0.4607 0.4746 0.4349 0.0590 -0.0410 -0.0617 144 CYS A O 1158 C CB . CYS A 144 ? 0.5695 0.6309 0.5745 0.0710 -0.0470 -0.0603 144 CYS A CB 1159 S SG . CYS A 144 ? 0.4994 0.5909 0.5278 0.0810 -0.0485 -0.0602 144 CYS A SG 1160 N N . ASN A 145 ? 0.4633 0.4952 0.4409 0.0454 -0.0330 -0.0701 145 ASN A N 1161 C CA . ASN A 145 ? 0.4896 0.5027 0.4530 0.0392 -0.0324 -0.0681 145 ASN A CA 1162 C C . ASN A 145 ? 0.5305 0.5466 0.4895 0.0349 -0.0379 -0.0646 145 ASN A C 1163 O O . ASN A 145 ? 0.4887 0.5220 0.4533 0.0311 -0.0398 -0.0671 145 ASN A O 1164 C CB . ASN A 145 ? 0.4731 0.4831 0.4332 0.0309 -0.0246 -0.0719 145 ASN A CB 1165 C CG . ASN A 145 ? 0.5073 0.5079 0.4634 0.0341 -0.0194 -0.0737 145 ASN A CG 1166 O OD1 . ASN A 145 ? 0.5130 0.5046 0.4666 0.0418 -0.0215 -0.0736 145 ASN A OD1 1167 N ND2 . ASN A 145 ? 0.5419 0.5435 0.4965 0.0280 -0.0122 -0.0754 145 ASN A ND2 1168 N N . LEU A 146 ? 0.4885 0.4887 0.4375 0.0352 -0.0403 -0.0592 146 LEU A N 1169 C CA . LEU A 146 ? 0.5147 0.5155 0.4565 0.0308 -0.0432 -0.0558 146 LEU A CA 1170 C C . LEU A 146 ? 0.4684 0.4533 0.4013 0.0249 -0.0387 -0.0552 146 LEU A C 1171 O O . LEU A 146 ? 0.4510 0.4208 0.3797 0.0270 -0.0389 -0.0512 146 LEU A O 1172 C CB . LEU A 146 ? 0.5833 0.5822 0.5231 0.0376 -0.0498 -0.0473 146 LEU A CB 1173 C CG . LEU A 146 ? 0.5980 0.6103 0.5482 0.0463 -0.0547 -0.0452 146 LEU A CG 1174 C CD1 . LEU A 146 ? 0.6949 0.6961 0.6437 0.0539 -0.0593 -0.0351 146 LEU A CD1 1175 C CD2 . LEU A 146 ? 0.6106 0.6464 0.5636 0.0440 -0.0588 -0.0467 146 LEU A CD2 1176 N N . THR A 147 ? 0.5114 0.4998 0.4425 0.0175 -0.0349 -0.0593 147 THR A N 1177 C CA . THR A 147 ? 0.4865 0.4618 0.4120 0.0125 -0.0296 -0.0587 147 THR A CA 1178 C C . THR A 147 ? 0.4747 0.4490 0.3932 0.0097 -0.0300 -0.0567 147 THR A C 1179 O O . THR A 147 ? 0.4771 0.4623 0.3952 0.0069 -0.0309 -0.0611 147 THR A O 1180 C CB . THR A 147 ? 0.4514 0.4292 0.3819 0.0070 -0.0230 -0.0646 147 THR A CB 1181 O OG1 . THR A 147 ? 0.4111 0.3906 0.3463 0.0102 -0.0215 -0.0657 147 THR A OG1 1182 C CG2 . THR A 147 ? 0.4192 0.3841 0.3455 0.0027 -0.0171 -0.0626 147 THR A CG2 1183 N N . PHE A 148 ? 0.4802 0.4428 0.3933 0.0105 -0.0295 -0.0502 148 PHE A N 1184 C CA . PHE A 148 ? 0.4659 0.4287 0.3725 0.0091 -0.0291 -0.0471 148 PHE A CA 1185 C C . PHE A 148 ? 0.4781 0.4308 0.3836 0.0057 -0.0225 -0.0464 148 PHE A C 1186 O O . PHE A 148 ? 0.4596 0.4034 0.3674 0.0059 -0.0213 -0.0432 148 PHE A O 1187 C CB . PHE A 148 ? 0.4576 0.4172 0.3610 0.0136 -0.0339 -0.0375 148 PHE A CB 1188 C CG . PHE A 148 ? 0.4297 0.3990 0.3345 0.0185 -0.0404 -0.0355 148 PHE A CG 1189 C CD1 . PHE A 148 ? 0.4596 0.4421 0.3589 0.0189 -0.0430 -0.0349 148 PHE A CD1 1190 C CD2 . PHE A 148 ? 0.4838 0.4498 0.3950 0.0232 -0.0436 -0.0346 148 PHE A CD2 1191 C CE1 . PHE A 148 ? 0.5480 0.5417 0.4493 0.0242 -0.0497 -0.0314 148 PHE A CE1 1192 C CE2 . PHE A 148 ? 0.5500 0.5249 0.4645 0.0290 -0.0492 -0.0317 148 PHE A CE2 1193 C CZ . PHE A 148 ? 0.5126 0.5020 0.4227 0.0296 -0.0526 -0.0292 148 PHE A CZ 1194 N N . GLY A 149 ? 0.4946 0.4494 0.3962 0.0030 -0.0185 -0.0493 149 GLY A N 1195 C CA . GLY A 149 ? 0.4533 0.3992 0.3556 0.0010 -0.0115 -0.0483 149 GLY A CA 1196 C C . GLY A 149 ? 0.4866 0.4355 0.3830 -0.0002 -0.0074 -0.0516 149 GLY A C 1197 O O . GLY A 149 ? 0.5114 0.4704 0.4017 -0.0006 -0.0103 -0.0562 149 GLY A O 1198 N N . SER A 150 ? 0.4519 0.3931 0.3497 -0.0002 -0.0005 -0.0494 150 SER A N 1199 C CA . SER A 150 ? 0.4495 0.3922 0.3416 -0.0007 0.0053 -0.0541 150 SER A CA 1200 C C . SER A 150 ? 0.5358 0.4778 0.4287 -0.0053 0.0090 -0.0674 150 SER A C 1201 O O . SER A 150 ? 0.4966 0.4316 0.3978 -0.0078 0.0118 -0.0699 150 SER A O 1202 C CB . SER A 150 ? 0.4518 0.3872 0.3476 0.0018 0.0126 -0.0477 150 SER A CB 1203 O OG . SER A 150 ? 0.5270 0.4644 0.4165 0.0024 0.0194 -0.0532 150 SER A OG 1204 N N . TRP A 151 ? 0.4975 0.4475 0.3814 -0.0069 0.0089 -0.0760 151 TRP A N 1205 C CA . TRP A 151 ? 0.5580 0.5067 0.4427 -0.0127 0.0125 -0.0906 151 TRP A CA 1206 C C . TRP A 151 ? 0.6677 0.6028 0.5544 -0.0125 0.0239 -0.0948 151 TRP A C 1207 O O . TRP A 151 ? 0.6700 0.5966 0.5623 -0.0171 0.0292 -0.1049 151 TRP A O 1208 C CB . TRP A 151 ? 0.5965 0.5608 0.4690 -0.0148 0.0070 -0.0994 151 TRP A CB 1209 C CG . TRP A 151 ? 0.6853 0.6536 0.5605 -0.0225 0.0058 -0.1146 151 TRP A CG 1210 C CD1 . TRP A 151 ? 0.8180 0.7875 0.6860 -0.0274 0.0090 -0.1296 151 TRP A CD1 1211 C CD2 . TRP A 151 ? 0.7744 0.7469 0.6613 -0.0270 0.0013 -0.1170 151 TRP A CD2 1212 N NE1 . TRP A 151 ? 0.8612 0.8351 0.7367 -0.0356 0.0059 -0.1413 151 TRP A NE1 1213 C CE2 . TRP A 151 ? 0.8581 0.8348 0.7459 -0.0354 0.0015 -0.1331 151 TRP A CE2 1214 C CE3 . TRP A 151 ? 0.7721 0.7457 0.6687 -0.0248 -0.0025 -0.1078 151 TRP A CE3 1215 C CZ2 . TRP A 151 ? 0.7492 0.7323 0.6495 -0.0421 -0.0019 -0.1387 151 TRP A CZ2 1216 C CZ3 . TRP A 151 ? 0.7262 0.7064 0.6337 -0.0303 -0.0050 -0.1136 151 TRP A CZ3 1217 C CH2 . TRP A 151 ? 0.7532 0.7388 0.6635 -0.0390 -0.0047 -0.1281 151 TRP A CH2 1218 N N . THR A 152 ? 0.6328 0.5662 0.5161 -0.0069 0.0280 -0.0867 152 THR A N 1219 C CA . THR A 152 ? 0.6165 0.5399 0.5007 -0.0048 0.0394 -0.0908 152 THR A CA 1220 C C . THR A 152 ? 0.6669 0.5783 0.5647 -0.0010 0.0453 -0.0803 152 THR A C 1221 O O . THR A 152 ? 0.5970 0.4959 0.5021 -0.0006 0.0544 -0.0850 152 THR A O 1222 C CB . THR A 152 ? 0.6218 0.5544 0.4937 -0.0004 0.0419 -0.0889 152 THR A CB 1223 O OG1 . THR A 152 ? 0.6988 0.6437 0.5559 -0.0036 0.0370 -0.0993 152 THR A OG1 1224 C CG2 . THR A 152 ? 0.7399 0.6629 0.6141 0.0034 0.0550 -0.0928 152 THR A CG2 1225 N N . TYR A 153 ? 0.5273 0.4424 0.4291 0.0018 0.0397 -0.0661 153 TYR A N 1226 C CA . TYR A 153 ? 0.4641 0.3729 0.3771 0.0061 0.0437 -0.0542 153 TYR A CA 1227 C C . TYR A 153 ? 0.5268 0.4313 0.4481 0.0045 0.0392 -0.0479 153 TYR A C 1228 O O . TYR A 153 ? 0.4672 0.3765 0.3850 0.0016 0.0311 -0.0486 153 TYR A O 1229 C CB . TYR A 153 ? 0.5010 0.4191 0.4122 0.0099 0.0408 -0.0424 153 TYR A CB 1230 C CG . TYR A 153 ? 0.4891 0.4132 0.3923 0.0125 0.0468 -0.0457 153 TYR A CG 1231 C CD1 . TYR A 153 ? 0.5102 0.4295 0.4184 0.0168 0.0584 -0.0472 153 TYR A CD1 1232 C CD2 . TYR A 153 ? 0.4902 0.4253 0.3804 0.0114 0.0417 -0.0471 153 TYR A CD2 1233 C CE1 . TYR A 153 ? 0.5683 0.4941 0.4674 0.0197 0.0652 -0.0514 153 TYR A CE1 1234 C CE2 . TYR A 153 ? 0.5014 0.4435 0.3819 0.0138 0.0478 -0.0500 153 TYR A CE2 1235 C CZ . TYR A 153 ? 0.5477 0.4853 0.4322 0.0178 0.0598 -0.0529 153 TYR A CZ 1236 O OH . TYR A 153 ? 0.5217 0.4674 0.3950 0.0207 0.0667 -0.0562 153 TYR A OH 1237 N N . ASN A 154 ? 0.4900 0.3865 0.4219 0.0072 0.0446 -0.0411 154 ASN A N 1238 C CA . ASN A 154 ? 0.4564 0.3508 0.3941 0.0064 0.0405 -0.0333 154 ASN A CA 1239 C C . ASN A 154 ? 0.4521 0.3538 0.3912 0.0091 0.0342 -0.0209 154 ASN A C 1240 O O . ASN A 154 ? 0.4321 0.3399 0.3698 0.0114 0.0338 -0.0175 154 ASN A O 1241 C CB . ASN A 154 ? 0.4984 0.3813 0.4466 0.0076 0.0486 -0.0308 154 ASN A CB 1242 C CG . ASN A 154 ? 0.5043 0.3849 0.4613 0.0141 0.0553 -0.0222 154 ASN A CG 1243 O OD1 . ASN A 154 ? 0.5447 0.4339 0.5039 0.0173 0.0509 -0.0116 154 ASN A OD1 1244 N ND2 . ASN A 154 ? 0.5324 0.4014 0.4959 0.0162 0.0661 -0.0272 154 ASN A ND2 1245 N N . GLY A 155 ? 0.4253 0.3272 0.3668 0.0084 0.0291 -0.0145 155 GLY A N 1246 C CA . GLY A 155 ? 0.4364 0.3451 0.3777 0.0090 0.0209 -0.0056 155 GLY A CA 1247 C C . GLY A 155 ? 0.4705 0.3828 0.4210 0.0127 0.0231 0.0050 155 GLY A C 1248 O O . GLY A 155 ? 0.4710 0.3900 0.4228 0.0122 0.0163 0.0117 155 GLY A O 1249 N N . ASN A 156 ? 0.4479 0.3555 0.4064 0.0164 0.0323 0.0068 156 ASN A N 1250 C CA . ASN A 156 ? 0.4007 0.3142 0.3702 0.0212 0.0350 0.0175 156 ASN A CA 1251 C C . ASN A 156 ? 0.4288 0.3476 0.3978 0.0228 0.0390 0.0155 156 ASN A C 1252 O O . ASN A 156 ? 0.4653 0.3925 0.4434 0.0258 0.0402 0.0244 156 ASN A O 1253 C CB . ASN A 156 ? 0.5179 0.4243 0.4983 0.0263 0.0443 0.0218 156 ASN A CB 1254 C CG . ASN A 156 ? 0.5596 0.4648 0.5421 0.0258 0.0402 0.0294 156 ASN A CG 1255 O OD1 . ASN A 156 ? 0.5894 0.5027 0.5678 0.0230 0.0300 0.0341 156 ASN A OD1 1256 N ND2 . ASN A 156 ? 0.5301 0.4252 0.5186 0.0284 0.0482 0.0305 156 ASN A ND2 1257 N N . GLN A 157 ? 0.3872 0.3028 0.3452 0.0205 0.0408 0.0041 157 GLN A N 1258 C CA . GLN A 157 ? 0.4334 0.3542 0.3874 0.0221 0.0456 0.0011 157 GLN A CA 1259 C C . GLN A 157 ? 0.4506 0.3793 0.3962 0.0183 0.0363 0.0027 157 GLN A C 1260 O O . GLN A 157 ? 0.4398 0.3771 0.3882 0.0191 0.0357 0.0105 157 GLN A O 1261 C CB . GLN A 157 ? 0.4657 0.3787 0.4120 0.0219 0.0530 -0.0131 157 GLN A CB 1262 C CG . GLN A 157 ? 0.5245 0.4269 0.4805 0.0263 0.0643 -0.0153 157 GLN A CG 1263 C CD . GLN A 157 ? 0.5896 0.4811 0.5388 0.0236 0.0700 -0.0315 157 GLN A CD 1264 O OE1 . GLN A 157 ? 0.4846 0.3758 0.4248 0.0176 0.0638 -0.0395 157 GLN A OE1 1265 N NE2 . GLN A 157 ? 0.6481 0.5309 0.6024 0.0280 0.0819 -0.0368 157 GLN A NE2 1266 N N . VAL A 158 ? 0.4065 0.3318 0.3432 0.0144 0.0298 -0.0041 158 VAL A N 1267 C CA . VAL A 158 ? 0.4060 0.3361 0.3360 0.0115 0.0204 -0.0023 158 VAL A CA 1268 C C . VAL A 158 ? 0.4344 0.3606 0.3649 0.0088 0.0119 -0.0020 158 VAL A C 1269 O O . VAL A 158 ? 0.4328 0.3542 0.3606 0.0076 0.0123 -0.0092 158 VAL A O 1270 C CB . VAL A 158 ? 0.4633 0.3959 0.3810 0.0106 0.0207 -0.0113 158 VAL A CB 1271 C CG1 . VAL A 158 ? 0.4848 0.4212 0.3972 0.0088 0.0111 -0.0081 158 VAL A CG1 1272 C CG2 . VAL A 158 ? 0.4816 0.4198 0.3964 0.0134 0.0289 -0.0110 158 VAL A CG2 1273 N N . ASP A 159 ? 0.3970 0.3256 0.3310 0.0074 0.0047 0.0059 159 ASP A N 1274 C CA . ASP A 159 ? 0.4062 0.3312 0.3387 0.0052 -0.0032 0.0047 159 ASP A CA 1275 C C . ASP A 159 ? 0.4684 0.3934 0.3960 0.0037 -0.0104 0.0041 159 ASP A C 1276 O O . ASP A 159 ? 0.5031 0.4313 0.4328 0.0033 -0.0116 0.0103 159 ASP A O 1277 C CB . ASP A 159 ? 0.3903 0.3169 0.3308 0.0046 -0.0064 0.0126 159 ASP A CB 1278 C CG . ASP A 159 ? 0.4647 0.3878 0.4010 0.0029 -0.0124 0.0096 159 ASP A CG 1279 O OD1 . ASP A 159 ? 0.5033 0.4226 0.4325 0.0028 -0.0122 0.0016 159 ASP A OD1 1280 O OD2 . ASP A 159 ? 0.4465 0.3723 0.3868 0.0016 -0.0172 0.0153 159 ASP A OD2 1281 N N . ILE A 160 ? 0.4332 0.3548 0.3553 0.0033 -0.0145 -0.0025 160 ILE A N 1282 C CA . ILE A 160 ? 0.4314 0.3522 0.3496 0.0036 -0.0203 -0.0036 160 ILE A CA 1283 C C . ILE A 160 ? 0.4662 0.3813 0.3855 0.0024 -0.0275 -0.0038 160 ILE A C 1284 O O . ILE A 160 ? 0.4617 0.3752 0.3807 0.0017 -0.0277 -0.0064 160 ILE A O 1285 C CB . ILE A 160 ? 0.5069 0.4306 0.4191 0.0050 -0.0188 -0.0120 160 ILE A CB 1286 C CG1 . ILE A 160 ? 0.5632 0.4877 0.4725 0.0068 -0.0247 -0.0113 160 ILE A CG1 1287 C CG2 . ILE A 160 ? 0.5197 0.4415 0.4315 0.0045 -0.0179 -0.0194 160 ILE A CG2 1288 C CD1 . ILE A 160 ? 0.5311 0.4632 0.4351 0.0082 -0.0238 -0.0175 160 ILE A CD1 1289 N N . PHE A 161 ? 0.4577 0.3693 0.3778 0.0022 -0.0331 -0.0009 161 PHE A N 1290 C CA . PHE A 161 ? 0.4430 0.3469 0.3644 0.0007 -0.0400 -0.0023 161 PHE A CA 1291 C C . PHE A 161 ? 0.4454 0.3438 0.3658 0.0031 -0.0439 -0.0034 161 PHE A C 1292 O O . PHE A 161 ? 0.4929 0.3939 0.4137 0.0047 -0.0430 0.0018 161 PHE A O 1293 C CB . PHE A 161 ? 0.4316 0.3340 0.3602 -0.0038 -0.0435 0.0051 161 PHE A CB 1294 C CG . PHE A 161 ? 0.4534 0.3626 0.3855 -0.0055 -0.0406 0.0085 161 PHE A CG 1295 C CD1 . PHE A 161 ? 0.5193 0.4359 0.4550 -0.0042 -0.0337 0.0139 161 PHE A CD1 1296 C CD2 . PHE A 161 ? 0.4429 0.3517 0.3745 -0.0077 -0.0446 0.0063 161 PHE A CD2 1297 C CE1 . PHE A 161 ? 0.4630 0.3854 0.4039 -0.0044 -0.0306 0.0177 161 PHE A CE1 1298 C CE2 . PHE A 161 ? 0.5390 0.4553 0.4748 -0.0083 -0.0425 0.0111 161 PHE A CE2 1299 C CZ . PHE A 161 ? 0.4983 0.4210 0.4400 -0.0063 -0.0354 0.0173 161 PHE A CZ 1300 N N . ASN A 162 ? 0.4239 0.3151 0.3428 0.0042 -0.0479 -0.0097 162 ASN A N 1301 C CA . ASN A 162 ? 0.4574 0.3407 0.3780 0.0072 -0.0518 -0.0100 162 ASN A CA 1302 C C . ASN A 162 ? 0.4543 0.3285 0.3818 0.0035 -0.0562 -0.0027 162 ASN A C 1303 O O . ASN A 162 ? 0.4908 0.3607 0.4208 -0.0016 -0.0593 -0.0033 162 ASN A O 1304 C CB . ASN A 162 ? 0.4616 0.3391 0.3790 0.0098 -0.0536 -0.0203 162 ASN A CB 1305 C CG . ASN A 162 ? 0.4829 0.3693 0.3968 0.0142 -0.0496 -0.0260 162 ASN A CG 1306 O OD1 . ASN A 162 ? 0.4698 0.3618 0.3853 0.0177 -0.0488 -0.0237 162 ASN A OD1 1307 N ND2 . ASN A 162 ? 0.4885 0.3784 0.3982 0.0137 -0.0469 -0.0326 162 ASN A ND2 1308 N N . ALA A 163 ? 0.5527 0.4245 0.4834 0.0058 -0.0569 0.0048 163 ALA A N 1309 C CA . ALA A 163 ? 0.6275 0.4886 0.5666 0.0023 -0.0606 0.0125 163 ALA A CA 1310 C C . ALA A 163 ? 0.5769 0.4215 0.5182 0.0034 -0.0656 0.0049 163 ALA A C 1311 O O . ALA A 163 ? 0.5481 0.3809 0.4964 -0.0019 -0.0696 0.0065 163 ALA A O 1312 C CB . ALA A 163 ? 0.5757 0.4398 0.5168 0.0054 -0.0590 0.0249 163 ALA A CB 1313 N N . LEU A 164 ? 0.4557 0.2998 0.3923 0.0104 -0.0649 -0.0036 164 LEU A N 1314 C CA . LEU A 164 ? 0.5533 0.3812 0.4925 0.0140 -0.0681 -0.0106 164 LEU A CA 1315 C C . LEU A 164 ? 0.5635 0.3944 0.4950 0.0168 -0.0667 -0.0246 164 LEU A C 1316 O O . LEU A 164 ? 0.5206 0.3657 0.4462 0.0171 -0.0631 -0.0266 164 LEU A O 1317 C CB . LEU A 164 ? 0.5607 0.3868 0.5041 0.0225 -0.0678 -0.0048 164 LEU A CB 1318 C CG . LEU A 164 ? 0.5849 0.4068 0.5356 0.0216 -0.0689 0.0107 164 LEU A CG 1319 C CD1 . LEU A 164 ? 0.5517 0.3726 0.5057 0.0318 -0.0692 0.0155 164 LEU A CD1 1320 C CD2 . LEU A 164 ? 0.6036 0.4065 0.5629 0.0147 -0.0724 0.0126 164 LEU A CD2 1321 N N . ASP A 165 ? 0.5290 0.3463 0.4604 0.0194 -0.0686 -0.0344 165 ASP A N 1322 C CA . ASP A 165 ? 0.5199 0.3420 0.4428 0.0228 -0.0659 -0.0473 165 ASP A CA 1323 C C . ASP A 165 ? 0.6043 0.4368 0.5281 0.0321 -0.0615 -0.0484 165 ASP A C 1324 O O . ASP A 165 ? 0.5081 0.3505 0.4264 0.0348 -0.0576 -0.0562 165 ASP A O 1325 C CB . ASP A 165 ? 0.6124 0.4170 0.5337 0.0234 -0.0685 -0.0591 165 ASP A CB 1326 C CG . ASP A 165 ? 0.6716 0.4720 0.5878 0.0136 -0.0729 -0.0635 165 ASP A CG 1327 O OD1 . ASP A 165 ? 0.6044 0.4179 0.5172 0.0076 -0.0731 -0.0585 165 ASP A OD1 1328 O OD2 . ASP A 165 ? 0.7272 0.5110 0.6433 0.0122 -0.0764 -0.0727 165 ASP A OD2 1329 N N . SER A 166 ? 0.5202 0.3518 0.4519 0.0370 -0.0624 -0.0398 166 SER A N 1330 C CA A SER A 166 ? 0.5228 0.3648 0.4580 0.0463 -0.0600 -0.0400 166 SER A CA 1331 C CA B SER A 166 ? 0.5024 0.3446 0.4374 0.0462 -0.0599 -0.0401 166 SER A CA 1332 C C . SER A 166 ? 0.4738 0.3234 0.4139 0.0480 -0.0616 -0.0264 166 SER A C 1333 O O . SER A 166 ? 0.5262 0.3685 0.4680 0.0435 -0.0640 -0.0169 166 SER A O 1334 C CB A SER A 166 ? 0.6247 0.4532 0.5657 0.0551 -0.0601 -0.0468 166 SER A CB 1335 C CB B SER A 166 ? 0.6457 0.4745 0.5863 0.0549 -0.0599 -0.0472 166 SER A CB 1336 O OG A SER A 166 ? 0.5608 0.3821 0.4952 0.0541 -0.0582 -0.0606 166 SER A OG 1337 O OG B SER A 166 ? 0.6938 0.5024 0.6414 0.0550 -0.0638 -0.0415 166 SER A OG 1338 N N . GLY A 167 ? 0.4694 0.3348 0.4116 0.0543 -0.0604 -0.0253 167 GLY A N 1339 C CA . GLY A 167 ? 0.4874 0.3607 0.4334 0.0578 -0.0630 -0.0128 167 GLY A CA 1340 C C . GLY A 167 ? 0.6281 0.4836 0.5828 0.0637 -0.0660 -0.0055 167 GLY A C 1341 O O . GLY A 167 ? 0.5649 0.4059 0.5246 0.0684 -0.0656 -0.0130 167 GLY A O 1342 N N . ASP A 168 ? 0.5554 0.4117 0.5118 0.0637 -0.0684 0.0092 168 ASP A N 1343 C CA . ASP A 168 ? 0.5735 0.4119 0.5391 0.0684 -0.0709 0.0196 168 ASP A CA 1344 C C . ASP A 168 ? 0.6218 0.4673 0.5954 0.0813 -0.0724 0.0238 168 ASP A C 1345 O O . ASP A 168 ? 0.6010 0.4677 0.5725 0.0848 -0.0741 0.0318 168 ASP A O 1346 C CB . ASP A 168 ? 0.7258 0.5655 0.6893 0.0628 -0.0719 0.0355 168 ASP A CB 1347 C CG . ASP A 168 ? 0.7969 0.6182 0.7709 0.0666 -0.0739 0.0493 168 ASP A CG 1348 O OD1 . ASP A 168 ? 0.7693 0.5727 0.7529 0.0731 -0.0746 0.0454 168 ASP A OD1 1349 O OD2 . ASP A 168 ? 1.0123 0.8364 0.9851 0.0629 -0.0740 0.0644 168 ASP A OD2 1350 N N . LEU A 169 ? 0.6027 0.4313 0.5856 0.0888 -0.0719 0.0179 169 LEU A N 1351 C CA . LEU A 169 ? 0.5877 0.4234 0.5809 0.1026 -0.0727 0.0211 169 LEU A CA 1352 C C . LEU A 169 ? 0.6857 0.5004 0.6909 0.1098 -0.0747 0.0343 169 LEU A C 1353 O O . LEU A 169 ? 0.6034 0.4158 0.6204 0.1228 -0.0747 0.0363 169 LEU A O 1354 C CB . LEU A 169 ? 0.6338 0.4676 0.6303 0.1080 -0.0690 0.0036 169 LEU A CB 1355 C CG . LEU A 169 ? 0.5990 0.4512 0.5850 0.1008 -0.0661 -0.0093 169 LEU A CG 1356 C CD1 . LEU A 169 ? 0.6309 0.4780 0.6189 0.1056 -0.0612 -0.0258 169 LEU A CD1 1357 C CD2 . LEU A 169 ? 0.6145 0.4976 0.5999 0.1023 -0.0677 -0.0040 169 LEU A CD2 1358 N N . SER A 170 ? 0.6760 0.4751 0.6800 0.1018 -0.0757 0.0442 170 SER A N 1359 C CA . SER A 170 ? 0.7960 0.5709 0.8131 0.1076 -0.0768 0.0574 170 SER A CA 1360 C C . SER A 170 ? 0.8453 0.6349 0.8693 0.1202 -0.0795 0.0758 170 SER A C 1361 O O . SER A 170 ? 0.8899 0.6635 0.9283 0.1315 -0.0797 0.0830 170 SER A O 1362 C CB . SER A 170 ? 0.8144 0.5737 0.8301 0.0952 -0.0772 0.0667 170 SER A CB 1363 O OG . SER A 170 ? 0.8025 0.5843 0.8084 0.0898 -0.0780 0.0799 170 SER A OG 1364 N N . ASP A 171 ? 0.8723 0.6923 0.8862 0.1187 -0.0817 0.0832 171 ASP A N 1365 C CA . ASP A 171 ? 0.9715 0.8079 0.9897 0.1294 -0.0855 0.1025 171 ASP A CA 1366 C C . ASP A 171 ? 0.7715 0.6457 0.7809 0.1314 -0.0884 0.0998 171 ASP A C 1367 O O . ASP A 171 ? 0.8650 0.7572 0.8601 0.1230 -0.0892 0.1025 171 ASP A O 1368 C CB . ASP A 171 ? 0.9543 0.7851 0.9693 0.1247 -0.0863 0.1239 171 ASP A CB 1369 C CG . ASP A 171 ? 1.0016 0.8483 1.0201 0.1364 -0.0905 0.1463 171 ASP A CG 1370 O OD1 . ASP A 171 ? 1.0963 0.9244 1.1306 0.1471 -0.0909 0.1581 171 ASP A OD1 1371 O OD2 . ASP A 171 ? 0.9769 0.8546 0.9823 0.1352 -0.0934 0.1517 171 ASP A OD2 1372 N N . PHE A 172 ? 0.6812 0.5676 0.7004 0.1425 -0.0896 0.0941 172 PHE A N 1373 C CA . PHE A 172 ? 0.6282 0.5514 0.6422 0.1438 -0.0931 0.0910 172 PHE A CA 1374 C C . PHE A 172 ? 0.6085 0.5451 0.6386 0.1603 -0.0969 0.0992 172 PHE A C 1375 O O . PHE A 172 ? 0.6955 0.6117 0.7412 0.1706 -0.0945 0.0992 172 PHE A O 1376 C CB . PHE A 172 ? 0.6620 0.5937 0.6696 0.1352 -0.0895 0.0686 172 PHE A CB 1377 C CG . PHE A 172 ? 0.6304 0.5523 0.6504 0.1421 -0.0854 0.0543 172 PHE A CG 1378 C CD1 . PHE A 172 ? 0.6536 0.5438 0.6753 0.1398 -0.0806 0.0456 172 PHE A CD1 1379 C CD2 . PHE A 172 ? 0.7000 0.6462 0.7296 0.1501 -0.0862 0.0486 172 PHE A CD2 1380 C CE1 . PHE A 172 ? 0.7187 0.6003 0.7493 0.1463 -0.0760 0.0313 172 PHE A CE1 1381 C CE2 . PHE A 172 ? 0.5073 0.4455 0.5481 0.1570 -0.0809 0.0353 172 PHE A CE2 1382 C CZ . PHE A 172 ? 0.6654 0.5710 0.7054 0.1554 -0.0756 0.0266 172 PHE A CZ 1383 N N . ILE A 173 ? 0.8419 0.8136 0.8685 0.1627 -0.1030 0.1059 173 ILE A N 1384 C CA . ILE A 173 ? 0.8502 0.8405 0.8917 0.1785 -0.1086 0.1188 173 ILE A CA 1385 C C . ILE A 173 ? 0.9334 0.9259 0.9944 0.1894 -0.1060 0.1073 173 ILE A C 1386 O O . ILE A 173 ? 1.2185 1.2116 1.2974 0.2052 -0.1080 0.1186 173 ILE A O 1387 C CB . ILE A 173 ? 0.9220 0.9529 0.9535 0.1766 -0.1167 0.1258 173 ILE A CB 1388 C CG1 . ILE A 173 ? 0.9631 0.9928 0.9833 0.1765 -0.1204 0.1483 173 ILE A CG1 1389 C CG2 . ILE A 173 ? 0.9239 0.9843 0.9729 0.1901 -0.1225 0.1288 173 ILE A CG2 1390 C CD1 . ILE A 173 ? 1.0569 1.1273 1.0657 0.1765 -0.1294 0.1578 173 ILE A CD1 1391 N N A GLU A 174 ? 0.7634 0.7576 0.8213 0.1813 -0.1010 0.0857 174 GLU A N 1392 N N B GLU A 174 ? 0.7615 0.7566 0.8197 0.1815 -0.1011 0.0858 174 GLU A N 1393 C CA A GLU A 174 ? 0.7572 0.7539 0.8316 0.1901 -0.0965 0.0728 174 GLU A CA 1394 C CA B GLU A 174 ? 0.7533 0.7484 0.8284 0.1908 -0.0963 0.0731 174 GLU A CA 1395 C C A GLU A 174 ? 0.7359 0.7744 0.8218 0.1968 -0.1017 0.0740 174 GLU A C 1396 C C B GLU A 174 ? 0.7404 0.7763 0.8289 0.1990 -0.1013 0.0746 174 GLU A C 1397 O O A GLU A 174 ? 0.7321 0.7935 0.8204 0.2023 -0.1102 0.0902 174 GLU A O 1398 O O B GLU A 174 ? 0.7387 0.7944 0.8338 0.2078 -0.1091 0.0919 174 GLU A O 1399 C CB A GLU A 174 ? 0.7595 0.7261 0.8505 0.2046 -0.0925 0.0775 174 GLU A CB 1400 C CB B GLU A 174 ? 0.7515 0.7141 0.8417 0.2042 -0.0924 0.0785 174 GLU A CB 1401 C CG A GLU A 174 ? 0.8010 0.7261 0.8843 0.1972 -0.0860 0.0683 174 GLU A CG 1402 C CG B GLU A 174 ? 0.8281 0.7804 0.9301 0.2108 -0.0843 0.0604 174 GLU A CG 1403 C CD A GLU A 174 ? 0.8579 0.7572 0.9575 0.2098 -0.0795 0.0606 174 GLU A CD 1404 C CD B GLU A 174 ? 0.8622 0.7694 0.9641 0.2111 -0.0777 0.0535 174 GLU A CD 1405 O OE1 A GLU A 174 ? 0.8664 0.7771 0.9852 0.2265 -0.0801 0.0673 174 GLU A OE1 1406 O OE1 B GLU A 174 ? 0.8856 0.7692 0.9920 0.2159 -0.0795 0.0680 174 GLU A OE1 1407 O OE2 A GLU A 174 ? 0.8569 0.7258 0.9503 0.2033 -0.0738 0.0473 174 GLU A OE2 1408 O OE2 B GLU A 174 ? 0.8328 0.7285 0.9299 0.2063 -0.0707 0.0337 174 GLU A OE2 1409 N N . ASP A 175 ? 0.5844 0.6339 0.6776 0.1958 -0.0966 0.0570 175 ASP A N 1410 C CA . ASP A 175 ? 0.5481 0.6384 0.6549 0.2001 -0.1005 0.0554 175 ASP A CA 1411 C C . ASP A 175 ? 0.5282 0.6212 0.6609 0.2184 -0.0965 0.0553 175 ASP A C 1412 O O . ASP A 175 ? 0.6155 0.6797 0.7524 0.2235 -0.0874 0.0464 175 ASP A O 1413 C CB . ASP A 175 ? 0.5191 0.6230 0.6175 0.1849 -0.0966 0.0369 175 ASP A CB 1414 C CG . ASP A 175 ? 0.5982 0.7452 0.7115 0.1862 -0.1006 0.0342 175 ASP A CG 1415 O OD1 . ASP A 175 ? 0.7346 0.9080 0.8419 0.1796 -0.1098 0.0396 175 ASP A OD1 1416 O OD2 . ASP A 175 ? 0.5985 0.7539 0.7295 0.1933 -0.0945 0.0260 175 ASP A OD2 1417 N N . VAL A 176 ? 0.5296 0.6588 0.6796 0.2282 -0.1034 0.0648 176 VAL A N 1418 C CA . VAL A 176 ? 0.4797 0.6171 0.6574 0.2477 -0.1005 0.0679 176 VAL A CA 1419 C C . VAL A 176 ? 0.4756 0.6174 0.6636 0.2478 -0.0897 0.0483 176 VAL A C 1420 O O . VAL A 176 ? 0.4925 0.6218 0.6976 0.2632 -0.0820 0.0457 176 VAL A O 1421 C CB . VAL A 176 ? 0.5117 0.6944 0.7063 0.2566 -0.1116 0.0825 176 VAL A CB 1422 C CG1 . VAL A 176 ? 0.5981 0.7924 0.8245 0.2777 -0.1076 0.0852 176 VAL A CG1 1423 C CG2 . VAL A 176 ? 0.4963 0.6776 0.6824 0.2600 -0.1220 0.1045 176 VAL A CG2 1424 N N . GLU A 177 ? 0.4483 0.6097 0.6275 0.2318 -0.0887 0.0352 177 GLU A N 1425 C CA . GLU A 177 ? 0.4391 0.6112 0.6289 0.2311 -0.0785 0.0187 177 GLU A CA 1426 C C . GLU A 177 ? 0.4708 0.6082 0.6412 0.2209 -0.0679 0.0028 177 GLU A C 1427 O O . GLU A 177 ? 0.4619 0.5937 0.6392 0.2257 -0.0569 -0.0093 177 GLU A O 1428 C CB . GLU A 177 ? 0.5306 0.7456 0.7250 0.2190 -0.0828 0.0139 177 GLU A CB 1429 C CG . GLU A 177 ? 0.6133 0.8721 0.8353 0.2305 -0.0902 0.0240 177 GLU A CG 1430 C CD . GLU A 177 ? 0.6914 0.9647 0.9397 0.2428 -0.0801 0.0171 177 GLU A CD 1431 O OE1 . GLU A 177 ? 0.7432 0.9944 0.9858 0.2408 -0.0669 0.0030 177 GLU A OE1 1432 O OE2 . GLU A 177 ? 0.8410 1.1497 1.1159 0.2549 -0.0852 0.0262 177 GLU A OE2 1433 N N . TRP A 178 ? 0.4297 0.5459 0.5760 0.2072 -0.0710 0.0031 178 TRP A N 1434 C CA . TRP A 178 ? 0.4243 0.5119 0.5515 0.1957 -0.0626 -0.0110 178 TRP A CA 1435 C C . TRP A 178 ? 0.5150 0.5598 0.6292 0.1969 -0.0616 -0.0086 178 TRP A C 1436 O O . TRP A 178 ? 0.6095 0.6456 0.7171 0.1955 -0.0692 0.0043 178 TRP A O 1437 C CB . TRP A 178 ? 0.4366 0.5365 0.5468 0.1757 -0.0653 -0.0160 178 TRP A CB 1438 C CG . TRP A 178 ? 0.4913 0.6300 0.6147 0.1721 -0.0652 -0.0206 178 TRP A CG 1439 C CD1 . TRP A 178 ? 0.5269 0.6995 0.6585 0.1696 -0.0747 -0.0135 178 TRP A CD1 1440 C CD2 . TRP A 178 ? 0.3838 0.5325 0.5147 0.1700 -0.0550 -0.0334 178 TRP A CD2 1441 N NE1 . TRP A 178 ? 0.5070 0.7100 0.6530 0.1655 -0.0714 -0.0215 178 TRP A NE1 1442 C CE2 . TRP A 178 ? 0.4704 0.6593 0.6166 0.1660 -0.0588 -0.0329 178 TRP A CE2 1443 C CE3 . TRP A 178 ? 0.4171 0.5458 0.5431 0.1713 -0.0431 -0.0450 178 TRP A CE3 1444 C CZ2 . TRP A 178 ? 0.4655 0.6745 0.6238 0.1626 -0.0503 -0.0424 178 TRP A CZ2 1445 C CZ3 . TRP A 178 ? 0.4349 0.5841 0.5706 0.1690 -0.0345 -0.0541 178 TRP A CZ3 1446 C CH2 . TRP A 178 ? 0.4412 0.6298 0.5936 0.1644 -0.0377 -0.0522 178 TRP A CH2 1447 N N . GLU A 179 ? 0.5131 0.5320 0.6235 0.1989 -0.0523 -0.0213 179 GLU A N 1448 C CA . GLU A 179 ? 0.5027 0.4807 0.5997 0.1962 -0.0512 -0.0225 179 GLU A CA 1449 C C . GLU A 179 ? 0.5312 0.5002 0.6058 0.1779 -0.0496 -0.0318 179 GLU A C 1450 O O . GLU A 179 ? 0.5496 0.5336 0.6202 0.1713 -0.0444 -0.0427 179 GLU A O 1451 C CB . GLU A 179 ? 0.6275 0.5809 0.7317 0.2082 -0.0424 -0.0331 179 GLU A CB 1452 C CG . GLU A 179 ? 0.7376 0.6748 0.8584 0.2250 -0.0441 -0.0225 179 GLU A CG 1453 C CD . GLU A 179 ? 0.8304 0.7357 0.9539 0.2341 -0.0348 -0.0363 179 GLU A CD 1454 O OE1 . GLU A 179 ? 0.8644 0.7815 0.9996 0.2451 -0.0267 -0.0461 179 GLU A OE1 1455 O OE2 . GLU A 179 ? 0.8717 0.7406 0.9855 0.2296 -0.0355 -0.0380 179 GLU A OE2 1456 N N . VAL A 180 ? 0.5666 0.5114 0.6277 0.1698 -0.0535 -0.0267 180 VAL A N 1457 C CA . VAL A 180 ? 0.4617 0.3951 0.5028 0.1537 -0.0517 -0.0353 180 VAL A CA 1458 C C . VAL A 180 ? 0.5754 0.4803 0.6104 0.1543 -0.0451 -0.0490 180 VAL A C 1459 O O . VAL A 180 ? 0.5790 0.4562 0.6175 0.1605 -0.0453 -0.0482 180 VAL A O 1460 C CB . VAL A 180 ? 0.5684 0.4913 0.5988 0.1445 -0.0585 -0.0236 180 VAL A CB 1461 C CG1 . VAL A 180 ? 0.5793 0.4885 0.5914 0.1292 -0.0563 -0.0320 180 VAL A CG1 1462 C CG2 . VAL A 180 ? 0.5617 0.5135 0.5939 0.1428 -0.0648 -0.0123 180 VAL A CG2 1463 N N . HIS A 181 ? 0.5752 0.4866 0.6006 0.1473 -0.0392 -0.0620 181 HIS A N 1464 C CA . HIS A 181 ? 0.6373 0.5263 0.6538 0.1471 -0.0331 -0.0766 181 HIS A CA 1465 C C . HIS A 181 ? 0.6759 0.5470 0.6740 0.1322 -0.0361 -0.0784 181 HIS A C 1466 O O . HIS A 181 ? 0.6690 0.5142 0.6602 0.1308 -0.0355 -0.0861 181 HIS A O 1467 C CB . HIS A 181 ? 0.6704 0.5792 0.6870 0.1492 -0.0244 -0.0882 181 HIS A CB 1468 C CG . HIS A 181 ? 0.8168 0.7078 0.8205 0.1484 -0.0175 -0.1040 181 HIS A CG 1469 N ND1 . HIS A 181 ? 1.0435 0.9081 1.0489 0.1575 -0.0153 -0.1121 181 HIS A ND1 1470 C CD2 . HIS A 181 ? 0.8914 0.7883 0.8800 0.1400 -0.0123 -0.1136 181 HIS A CD2 1471 C CE1 . HIS A 181 ? 1.0602 0.9158 1.0503 0.1540 -0.0095 -0.1272 181 HIS A CE1 1472 N NE2 . HIS A 181 ? 1.0257 0.9014 1.0051 0.1437 -0.0077 -0.1274 181 HIS A NE2 1473 N N . GLY A 182 ? 0.6120 0.4971 0.6030 0.1210 -0.0395 -0.0717 182 GLY A N 1474 C CA . GLY A 182 ? 0.6296 0.5002 0.6063 0.1081 -0.0428 -0.0709 182 GLY A CA 1475 C C . GLY A 182 ? 0.5661 0.4557 0.5383 0.0986 -0.0455 -0.0627 182 GLY A C 1476 O O . GLY A 182 ? 0.5142 0.4275 0.4935 0.1012 -0.0450 -0.0597 182 GLY A O 1477 N N . MET A 183 ? 0.4640 0.3439 0.4257 0.0877 -0.0483 -0.0596 183 MET A N 1478 C CA . MET A 183 ? 0.4438 0.3387 0.3998 0.0785 -0.0495 -0.0539 183 MET A CA 1479 C C . MET A 183 ? 0.4829 0.3673 0.4267 0.0675 -0.0492 -0.0564 183 MET A C 1480 O O . MET A 183 ? 0.4542 0.3330 0.3949 0.0612 -0.0527 -0.0485 183 MET A O 1481 C CB . MET A 183 ? 0.5579 0.4562 0.5182 0.0794 -0.0551 -0.0402 183 MET A CB 1482 C CG . MET A 183 ? 0.5272 0.4449 0.4828 0.0724 -0.0558 -0.0358 183 MET A CG 1483 S SD . MET A 183 ? 0.5304 0.4550 0.4891 0.0758 -0.0622 -0.0201 183 MET A SD 1484 C CE . MET A 183 ? 0.5303 0.4775 0.4809 0.0668 -0.0618 -0.0205 183 MET A CE 1485 N N . PRO A 184 ? 0.5043 0.3871 0.4414 0.0655 -0.0450 -0.0668 184 PRO A N 1486 C CA . PRO A 184 ? 0.4115 0.2852 0.3377 0.0559 -0.0458 -0.0684 184 PRO A CA 1487 C C . PRO A 184 ? 0.4764 0.3629 0.3989 0.0480 -0.0451 -0.0624 184 PRO A C 1488 O O . PRO A 184 ? 0.5092 0.4124 0.4349 0.0487 -0.0422 -0.0616 184 PRO A O 1489 C CB . PRO A 184 ? 0.4751 0.3486 0.3940 0.0572 -0.0410 -0.0804 184 PRO A CB 1490 C CG . PRO A 184 ? 0.5613 0.4524 0.4873 0.0643 -0.0356 -0.0830 184 PRO A CG 1491 C CD . PRO A 184 ? 0.5546 0.4443 0.4932 0.0721 -0.0392 -0.0769 184 PRO A CD 1492 N N . ALA A 185 ? 0.4982 0.3770 0.4155 0.0404 -0.0476 -0.0585 185 ALA A N 1493 C CA . ALA A 185 ? 0.4149 0.3035 0.3297 0.0339 -0.0463 -0.0525 185 ALA A CA 1494 C C . ALA A 185 ? 0.4673 0.3558 0.3741 0.0280 -0.0441 -0.0557 185 ALA A C 1495 O O . ALA A 185 ? 0.4669 0.3457 0.3689 0.0268 -0.0463 -0.0600 185 ALA A O 1496 C CB . ALA A 185 ? 0.4549 0.3379 0.3723 0.0308 -0.0504 -0.0425 185 ALA A CB 1497 N N . VAL A 186 ? 0.4460 0.3457 0.3516 0.0245 -0.0399 -0.0536 186 VAL A N 1498 C CA . VAL A 186 ? 0.4523 0.3527 0.3517 0.0194 -0.0379 -0.0531 186 VAL A CA 1499 C C . VAL A 186 ? 0.4624 0.3682 0.3642 0.0152 -0.0358 -0.0460 186 VAL A C 1500 O O . VAL A 186 ? 0.4837 0.3943 0.3899 0.0160 -0.0351 -0.0438 186 VAL A O 1501 C CB . VAL A 186 ? 0.4631 0.3713 0.3582 0.0206 -0.0321 -0.0589 186 VAL A CB 1502 C CG1 . VAL A 186 ? 0.4196 0.3249 0.3127 0.0264 -0.0321 -0.0674 186 VAL A CG1 1503 C CG2 . VAL A 186 ? 0.5292 0.4494 0.4304 0.0202 -0.0266 -0.0579 186 VAL A CG2 1504 N N . LYS A 187 ? 0.4457 0.3512 0.3443 0.0111 -0.0348 -0.0427 187 LYS A N 1505 C CA . LYS A 187 ? 0.4187 0.3285 0.3200 0.0082 -0.0310 -0.0370 187 LYS A CA 1506 C C . LYS A 187 ? 0.3851 0.2997 0.2840 0.0070 -0.0251 -0.0377 187 LYS A C 1507 O O . LYS A 187 ? 0.4321 0.3462 0.3252 0.0068 -0.0259 -0.0385 187 LYS A O 1508 C CB . LYS A 187 ? 0.4631 0.3692 0.3658 0.0052 -0.0344 -0.0299 187 LYS A CB 1509 C CG . LYS A 187 ? 0.4406 0.3508 0.3467 0.0034 -0.0293 -0.0242 187 LYS A CG 1510 C CD . LYS A 187 ? 0.4365 0.3459 0.3468 0.0012 -0.0321 -0.0162 187 LYS A CD 1511 C CE . LYS A 187 ? 0.4170 0.3303 0.3322 0.0010 -0.0255 -0.0106 187 LYS A CE 1512 N NZ . LYS A 187 ? 0.4568 0.3718 0.3780 -0.0005 -0.0282 -0.0024 187 LYS A NZ 1513 N N . ASN A 188 ? 0.4359 0.3552 0.3390 0.0059 -0.0192 -0.0375 188 ASN A N 1514 C CA . ASN A 188 ? 0.4299 0.3522 0.3334 0.0041 -0.0124 -0.0363 188 ASN A CA 1515 C C . ASN A 188 ? 0.4690 0.3891 0.3769 0.0020 -0.0084 -0.0306 188 ASN A C 1516 O O . ASN A 188 ? 0.4579 0.3778 0.3697 0.0014 -0.0075 -0.0318 188 ASN A O 1517 C CB . ASN A 188 ? 0.4646 0.3933 0.3723 0.0038 -0.0077 -0.0423 188 ASN A CB 1518 C CG . ASN A 188 ? 0.4578 0.3905 0.3636 0.0072 -0.0099 -0.0482 188 ASN A CG 1519 O OD1 . ASN A 188 ? 0.4654 0.3987 0.3656 0.0085 -0.0088 -0.0490 188 ASN A OD1 1520 N ND2 . ASN A 188 ? 0.4735 0.4097 0.3836 0.0094 -0.0130 -0.0522 188 ASN A ND2 1521 N N . VAL A 189 ? 0.4337 0.3529 0.3409 0.0013 -0.0055 -0.0244 189 VAL A N 1522 C CA . VAL A 189 ? 0.3526 0.2689 0.2660 0.0005 -0.0002 -0.0186 189 VAL A CA 1523 C C . VAL A 189 ? 0.3977 0.3135 0.3135 -0.0007 0.0075 -0.0161 189 VAL A C 1524 O O . VAL A 189 ? 0.4192 0.3377 0.3302 -0.0001 0.0073 -0.0115 189 VAL A O 1525 C CB . VAL A 189 ? 0.4258 0.3416 0.3394 0.0017 -0.0038 -0.0099 189 VAL A CB 1526 C CG1 . VAL A 189 ? 0.4369 0.3498 0.3589 0.0025 0.0029 -0.0034 189 VAL A CG1 1527 C CG2 . VAL A 189 ? 0.4207 0.3366 0.3334 0.0018 -0.0113 -0.0110 189 VAL A CG2 1528 N N . ILE A 190 ? 0.4102 0.3226 0.3334 -0.0028 0.0144 -0.0186 190 ILE A N 1529 C CA . ILE A 190 ? 0.4102 0.3204 0.3383 -0.0050 0.0226 -0.0159 190 ILE A CA 1530 C C . ILE A 190 ? 0.4491 0.3506 0.3849 -0.0042 0.0287 -0.0095 190 ILE A C 1531 O O . ILE A 190 ? 0.4521 0.3499 0.3909 -0.0034 0.0287 -0.0125 190 ILE A O 1532 C CB . ILE A 190 ? 0.5074 0.4203 0.4403 -0.0093 0.0261 -0.0256 190 ILE A CB 1533 C CG1 . ILE A 190 ? 0.4979 0.4093 0.4365 -0.0123 0.0347 -0.0210 190 ILE A CG1 1534 C CG2 . ILE A 190 ? 0.4225 0.3318 0.3604 -0.0115 0.0270 -0.0336 190 ILE A CG2 1535 C CD1 . ILE A 190 ? 0.4929 0.4096 0.4382 -0.0175 0.0384 -0.0289 190 ILE A CD1 1536 N N . SER A 191 ? 0.4133 0.3122 0.3518 -0.0036 0.0338 0.0003 191 SER A N 1537 C CA . SER A 191 ? 0.3920 0.2809 0.3405 -0.0021 0.0415 0.0073 191 SER A CA 1538 C C . SER A 191 ? 0.4759 0.3598 0.4306 -0.0052 0.0503 0.0114 191 SER A C 1539 O O . SER A 191 ? 0.5043 0.3953 0.4535 -0.0064 0.0500 0.0149 191 SER A O 1540 C CB . SER A 191 ? 0.5173 0.4088 0.4651 0.0035 0.0380 0.0198 191 SER A CB 1541 O OG . SER A 191 ? 0.6254 0.5244 0.5657 0.0043 0.0349 0.0282 191 SER A OG 1542 N N . TYR A 192 ? 0.4520 0.3231 0.4185 -0.0065 0.0590 0.0110 192 TYR A N 1543 C CA . TYR A 192 ? 0.4043 0.2683 0.3796 -0.0114 0.0681 0.0124 192 TYR A CA 1544 C C . TYR A 192 ? 0.4314 0.2864 0.4141 -0.0074 0.0752 0.0289 192 TYR A C 1545 O O . TYR A 192 ? 0.4674 0.3141 0.4562 -0.0023 0.0774 0.0332 192 TYR A O 1546 C CB . TYR A 192 ? 0.4795 0.3337 0.4640 -0.0174 0.0730 -0.0021 192 TYR A CB 1547 C CG . TYR A 192 ? 0.4371 0.3024 0.4147 -0.0211 0.0656 -0.0168 192 TYR A CG 1548 C CD1 . TYR A 192 ? 0.5147 0.3838 0.4852 -0.0178 0.0588 -0.0233 192 TYR A CD1 1549 C CD2 . TYR A 192 ? 0.5342 0.4081 0.5130 -0.0272 0.0653 -0.0223 192 TYR A CD2 1550 C CE1 . TYR A 192 ? 0.4611 0.3410 0.4253 -0.0202 0.0517 -0.0342 192 TYR A CE1 1551 C CE2 . TYR A 192 ? 0.5381 0.4241 0.5118 -0.0291 0.0579 -0.0339 192 TYR A CE2 1552 C CZ . TYR A 192 ? 0.4946 0.3827 0.4609 -0.0256 0.0511 -0.0397 192 TYR A CZ 1553 O OH . TYR A 192 ? 0.4945 0.3948 0.4563 -0.0268 0.0438 -0.0491 192 TYR A OH 1554 N N . GLY A 193 ? 0.4731 0.3305 0.4561 -0.0092 0.0794 0.0389 193 GLY A N 1555 C CA . GLY A 193 ? 0.5343 0.3842 0.5243 -0.0054 0.0865 0.0570 193 GLY A CA 1556 C C . GLY A 193 ? 0.5238 0.3818 0.5068 0.0034 0.0799 0.0701 193 GLY A C 1557 O O . GLY A 193 ? 0.5585 0.4307 0.5283 0.0051 0.0696 0.0671 193 GLY A O 1558 N N . CYS A 194 ? 0.5177 0.3666 0.5111 0.0091 0.0857 0.0850 194 CYS A N 1559 C CA . CYS A 194 ? 0.6277 0.4877 0.6161 0.0171 0.0790 0.0998 194 CYS A CA 1560 C C . CYS A 194 ? 0.7061 0.5693 0.6953 0.0208 0.0722 0.0922 194 CYS A C 1561 O O . CYS A 194 ? 0.7480 0.6261 0.7286 0.0241 0.0621 0.0967 194 CYS A O 1562 C CB . CYS A 194 ? 0.6552 0.5063 0.6563 0.0234 0.0873 0.1205 194 CYS A CB 1563 S SG . CYS A 194 ? 0.8682 0.6980 0.8911 0.0286 0.0965 0.1191 194 CYS A SG 1564 N N . CYS A 195 ? 0.6260 0.4759 0.6249 0.0197 0.0775 0.0800 195 CYS A N 1565 C CA . CYS A 195 ? 0.5951 0.4467 0.5988 0.0257 0.0746 0.0791 195 CYS A CA 1566 C C . CYS A 195 ? 0.6510 0.4996 0.6534 0.0227 0.0737 0.0601 195 CYS A C 1567 O O . CYS A 195 ? 0.7184 0.5682 0.7261 0.0279 0.0734 0.0603 195 CYS A O 1568 C CB . CYS A 195 ? 0.6741 0.5136 0.6951 0.0333 0.0842 0.0926 195 CYS A CB 1569 S SG . CYS A 195 ? 1.0566 0.9023 1.0781 0.0378 0.0847 0.1190 195 CYS A SG 1570 N N . SER A 196 ? 0.5331 0.3795 0.5289 0.0149 0.0733 0.0449 196 SER A N 1571 C CA . SER A 196 ? 0.4787 0.3234 0.4721 0.0123 0.0724 0.0279 196 SER A CA 1572 C C . SER A 196 ? 0.5239 0.3825 0.5093 0.0149 0.0626 0.0268 196 SER A C 1573 O O . SER A 196 ? 0.5311 0.4015 0.5115 0.0171 0.0548 0.0362 196 SER A O 1574 C CB . SER A 196 ? 0.5448 0.3883 0.5331 0.0033 0.0722 0.0129 196 SER A CB 1575 O OG . SER A 196 ? 0.5142 0.3723 0.4897 0.0005 0.0619 0.0068 196 SER A OG 1576 N N . GLU A 197 ? 0.4346 0.2913 0.4189 0.0141 0.0635 0.0147 197 GLU A N 1577 C CA . GLU A 197 ? 0.4011 0.2695 0.3782 0.0150 0.0555 0.0120 197 GLU A CA 1578 C C . GLU A 197 ? 0.4175 0.2941 0.3829 0.0096 0.0466 0.0066 197 GLU A C 1579 O O . GLU A 197 ? 0.4665 0.3395 0.4304 0.0049 0.0488 0.0012 197 GLU A O 1580 C CB . GLU A 197 ? 0.4392 0.3025 0.4163 0.0148 0.0606 -0.0006 197 GLU A CB 1581 C CG . GLU A 197 ? 0.7476 0.5964 0.7367 0.0190 0.0732 -0.0012 197 GLU A CG 1582 C CD . GLU A 197 ? 0.6257 0.4588 0.6206 0.0146 0.0811 -0.0065 197 GLU A CD 1583 O OE1 . GLU A 197 ? 0.6059 0.4388 0.5948 0.0067 0.0788 -0.0173 197 GLU A OE1 1584 O OE2 . GLU A 197 ? 0.9362 0.7571 0.9435 0.0191 0.0898 0.0012 197 GLU A OE2 1585 N N . PRO A 198 ? 0.4104 0.2979 0.3689 0.0100 0.0372 0.0083 198 PRO A N 1586 C CA . PRO A 198 ? 0.4191 0.3131 0.3672 0.0061 0.0292 0.0020 198 PRO A CA 1587 C C . PRO A 198 ? 0.4724 0.3668 0.4162 0.0033 0.0283 -0.0105 198 PRO A C 1588 O O . PRO A 198 ? 0.4197 0.3129 0.3651 0.0048 0.0311 -0.0134 198 PRO A O 1589 C CB . PRO A 198 ? 0.4542 0.3570 0.3991 0.0079 0.0201 0.0091 198 PRO A CB 1590 C CG . PRO A 198 ? 0.4561 0.3594 0.4085 0.0114 0.0228 0.0139 198 PRO A CG 1591 C CD . PRO A 198 ? 0.4674 0.3616 0.4294 0.0143 0.0337 0.0166 198 PRO A CD 1592 N N . TYR A 199 ? 0.4347 0.3329 0.3726 0.0000 0.0241 -0.0171 199 TYR A N 1593 C CA . TYR A 199 ? 0.3921 0.2937 0.3259 -0.0025 0.0218 -0.0280 199 TYR A CA 1594 C C . TYR A 199 ? 0.4230 0.3320 0.3503 -0.0022 0.0129 -0.0288 199 TYR A C 1595 O O . TYR A 199 ? 0.4527 0.3642 0.3786 -0.0034 0.0116 -0.0303 199 TYR A O 1596 C CB . TYR A 199 ? 0.4147 0.3139 0.3520 -0.0070 0.0270 -0.0368 199 TYR A CB 1597 C CG . TYR A 199 ? 0.4467 0.3361 0.3905 -0.0077 0.0358 -0.0391 199 TYR A CG 1598 C CD1 . TYR A 199 ? 0.4416 0.3305 0.3830 -0.0083 0.0374 -0.0481 199 TYR A CD1 1599 C CD2 . TYR A 199 ? 0.4439 0.3242 0.3957 -0.0070 0.0430 -0.0321 199 TYR A CD2 1600 C CE1 . TYR A 199 ? 0.5226 0.4010 0.4695 -0.0085 0.0464 -0.0521 199 TYR A CE1 1601 C CE2 . TYR A 199 ? 0.4940 0.3623 0.4534 -0.0068 0.0523 -0.0346 199 TYR A CE2 1602 C CZ . TYR A 199 ? 0.5794 0.4465 0.5361 -0.0076 0.0539 -0.0457 199 TYR A CZ 1603 O OH . TYR A 199 ? 0.6407 0.4952 0.6039 -0.0070 0.0634 -0.0504 199 TYR A OH 1604 N N . PRO A 200 ? 0.4089 0.3208 0.3327 -0.0003 0.0074 -0.0270 200 PRO A N 1605 C CA . PRO A 200 ? 0.3847 0.3004 0.3036 0.0006 -0.0009 -0.0269 200 PRO A CA 1606 C C . PRO A 200 ? 0.4935 0.4140 0.4096 0.0004 -0.0040 -0.0339 200 PRO A C 1607 O O . PRO A 200 ? 0.4803 0.4029 0.3960 -0.0004 -0.0018 -0.0378 200 PRO A O 1608 C CB . PRO A 200 ? 0.4186 0.3339 0.3379 0.0021 -0.0046 -0.0193 200 PRO A CB 1609 C CG . PRO A 200 ? 0.4261 0.3413 0.3481 0.0027 0.0014 -0.0194 200 PRO A CG 1610 C CD . PRO A 200 ? 0.4271 0.3381 0.3527 0.0017 0.0094 -0.0230 200 PRO A CD 1611 N N . ASP A 201 ? 0.4568 0.3796 0.3705 0.0016 -0.0095 -0.0357 201 ASP A N 1612 C CA . ASP A 201 ? 0.4495 0.3780 0.3619 0.0030 -0.0137 -0.0400 201 ASP A CA 1613 C C . ASP A 201 ? 0.4560 0.3821 0.3667 0.0059 -0.0201 -0.0376 201 ASP A C 1614 O O . ASP A 201 ? 0.3975 0.3189 0.3070 0.0059 -0.0208 -0.0356 201 ASP A O 1615 C CB . ASP A 201 ? 0.4757 0.4114 0.3912 0.0013 -0.0114 -0.0478 201 ASP A CB 1616 C CG . ASP A 201 ? 0.5149 0.4519 0.4319 0.0022 -0.0111 -0.0495 201 ASP A CG 1617 O OD1 . ASP A 201 ? 0.4692 0.4059 0.3843 0.0061 -0.0158 -0.0491 201 ASP A OD1 1618 O OD2 . ASP A 201 ? 0.5443 0.4828 0.4650 -0.0009 -0.0052 -0.0516 201 ASP A OD2 1619 N N . VAL A 202 ? 0.4080 0.3369 0.3183 0.0086 -0.0249 -0.0378 202 VAL A N 1620 C CA . VAL A 202 ? 0.4371 0.3623 0.3474 0.0121 -0.0300 -0.0378 202 VAL A CA 1621 C C . VAL A 202 ? 0.4799 0.4132 0.3930 0.0153 -0.0309 -0.0433 202 VAL A C 1622 O O . VAL A 202 ? 0.4695 0.4119 0.3839 0.0152 -0.0310 -0.0446 202 VAL A O 1623 C CB . VAL A 202 ? 0.5181 0.4371 0.4283 0.0136 -0.0353 -0.0309 202 VAL A CB 1624 C CG1 . VAL A 202 ? 0.4623 0.3750 0.3724 0.0101 -0.0351 -0.0254 202 VAL A CG1 1625 C CG2 . VAL A 202 ? 0.4814 0.4071 0.3911 0.0148 -0.0361 -0.0276 202 VAL A CG2 1626 N N . THR A 203 ? 0.4904 0.4218 0.4045 0.0183 -0.0315 -0.0470 203 THR A N 1627 C CA . THR A 203 ? 0.4079 0.3490 0.3272 0.0222 -0.0316 -0.0518 203 THR A CA 1628 C C . THR A 203 ? 0.4607 0.3954 0.3815 0.0289 -0.0361 -0.0516 203 THR A C 1629 O O . THR A 203 ? 0.4489 0.3722 0.3661 0.0295 -0.0368 -0.0527 203 THR A O 1630 C CB . THR A 203 ? 0.4929 0.4404 0.4140 0.0202 -0.0255 -0.0574 203 THR A CB 1631 O OG1 . THR A 203 ? 0.4641 0.4161 0.3862 0.0141 -0.0213 -0.0576 203 THR A OG1 1632 C CG2 . THR A 203 ? 0.4208 0.3802 0.3495 0.0247 -0.0251 -0.0622 203 THR A CG2 1633 N N . PHE A 204 ? 0.4513 0.3936 0.3778 0.0338 -0.0393 -0.0505 204 PHE A N 1634 C CA . PHE A 204 ? 0.4502 0.3874 0.3814 0.0419 -0.0427 -0.0502 204 PHE A CA 1635 C C . PHE A 204 ? 0.4402 0.3908 0.3789 0.0466 -0.0398 -0.0565 204 PHE A C 1636 O O . PHE A 204 ? 0.4649 0.4325 0.4085 0.0450 -0.0390 -0.0576 204 PHE A O 1637 C CB . PHE A 204 ? 0.4603 0.3984 0.3939 0.0454 -0.0483 -0.0416 204 PHE A CB 1638 C CG . PHE A 204 ? 0.4652 0.3919 0.3931 0.0408 -0.0500 -0.0345 204 PHE A CG 1639 C CD1 . PHE A 204 ? 0.4536 0.3861 0.3761 0.0342 -0.0481 -0.0324 204 PHE A CD1 1640 C CD2 . PHE A 204 ? 0.4950 0.4049 0.4240 0.0428 -0.0530 -0.0303 204 PHE A CD2 1641 C CE1 . PHE A 204 ? 0.5062 0.4299 0.4250 0.0304 -0.0486 -0.0255 204 PHE A CE1 1642 C CE2 . PHE A 204 ? 0.5030 0.4041 0.4290 0.0377 -0.0542 -0.0233 204 PHE A CE2 1643 C CZ . PHE A 204 ? 0.5009 0.4099 0.4219 0.0318 -0.0518 -0.0204 204 PHE A CZ 1644 N N . THR A 205 ? 0.4780 0.4220 0.4181 0.0521 -0.0378 -0.0616 205 THR A N 1645 C CA . THR A 205 ? 0.4355 0.3935 0.3845 0.0580 -0.0343 -0.0669 205 THR A CA 1646 C C . THR A 205 ? 0.4574 0.4131 0.4154 0.0688 -0.0382 -0.0646 205 THR A C 1647 O O . THR A 205 ? 0.5251 0.4650 0.4817 0.0741 -0.0378 -0.0675 205 THR A O 1648 C CB . THR A 205 ? 0.5362 0.4910 0.4803 0.0579 -0.0275 -0.0749 205 THR A CB 1649 O OG1 . THR A 205 ? 0.5249 0.4814 0.4614 0.0485 -0.0239 -0.0748 205 THR A OG1 1650 C CG2 . THR A 205 ? 0.5849 0.5564 0.5398 0.0645 -0.0225 -0.0798 205 THR A CG2 1651 N N . LEU A 206 ? 0.4476 0.4187 0.4146 0.0721 -0.0419 -0.0595 206 LEU A N 1652 C CA . LEU A 206 ? 0.4735 0.4453 0.4513 0.0837 -0.0453 -0.0556 206 LEU A CA 1653 C C . LEU A 206 ? 0.4673 0.4510 0.4561 0.0914 -0.0398 -0.0629 206 LEU A C 1654 O O . LEU A 206 ? 0.5612 0.5676 0.5570 0.0890 -0.0373 -0.0656 206 LEU A O 1655 C CB . LEU A 206 ? 0.4798 0.4679 0.4626 0.0845 -0.0519 -0.0466 206 LEU A CB 1656 C CG . LEU A 206 ? 0.5823 0.5717 0.5757 0.0965 -0.0570 -0.0382 206 LEU A CG 1657 C CD1 . LEU A 206 ? 0.5617 0.5238 0.5502 0.0990 -0.0593 -0.0315 206 LEU A CD1 1658 C CD2 . LEU A 206 ? 0.6421 0.6560 0.6385 0.0953 -0.0634 -0.0308 206 LEU A CD2 1659 N N . LEU A 207 ? 0.5074 0.4754 0.4982 0.1003 -0.0376 -0.0665 207 LEU A N 1660 C CA . LEU A 207 ? 0.5157 0.4921 0.5164 0.1096 -0.0311 -0.0739 207 LEU A CA 1661 C C . LEU A 207 ? 0.4889 0.4711 0.5065 0.1233 -0.0344 -0.0680 207 LEU A C 1662 O O . LEU A 207 ? 0.4851 0.4461 0.5034 0.1299 -0.0376 -0.0641 207 LEU A O 1663 C CB . LEU A 207 ? 0.4761 0.4295 0.4663 0.1111 -0.0259 -0.0836 207 LEU A CB 1664 C CG . LEU A 207 ? 0.5742 0.5214 0.5470 0.0982 -0.0237 -0.0878 207 LEU A CG 1665 C CD1 . LEU A 207 ? 0.6834 0.6059 0.6437 0.0986 -0.0220 -0.0960 207 LEU A CD1 1666 C CD2 . LEU A 207 ? 0.5809 0.5502 0.5544 0.0938 -0.0164 -0.0919 207 LEU A CD2 1667 N N . LEU A 208 ? 0.4745 0.4858 0.5072 0.1274 -0.0339 -0.0664 208 LEU A N 1668 C CA . LEU A 208 ? 0.4683 0.4908 0.5200 0.1417 -0.0372 -0.0595 208 LEU A CA 1669 C C . LEU A 208 ? 0.4726 0.5056 0.5383 0.1529 -0.0285 -0.0675 208 LEU A C 1670 O O . LEU A 208 ? 0.5094 0.5573 0.5750 0.1477 -0.0214 -0.0753 208 LEU A O 1671 C CB . LEU A 208 ? 0.4488 0.5014 0.5095 0.1387 -0.0446 -0.0509 208 LEU A CB 1672 C CG . LEU A 208 ? 0.4355 0.4838 0.4813 0.1266 -0.0519 -0.0446 208 LEU A CG 1673 C CD1 . LEU A 208 ? 0.4802 0.5615 0.5354 0.1248 -0.0592 -0.0385 208 LEU A CD1 1674 C CD2 . LEU A 208 ? 0.5281 0.5493 0.5667 0.1307 -0.0561 -0.0364 208 LEU A CD2 1675 N N . LYS A 209 ? 0.4614 0.4874 0.5405 0.1687 -0.0284 -0.0645 209 LYS A N 1676 C CA . LYS A 209 ? 0.4464 0.4831 0.5411 0.1818 -0.0196 -0.0715 209 LYS A CA 1677 C C . LYS A 209 ? 0.4352 0.4885 0.5539 0.1970 -0.0248 -0.0601 209 LYS A C 1678 O O . LYS A 209 ? 0.5067 0.5473 0.6261 0.2010 -0.0331 -0.0487 209 LYS A O 1679 C CB . LYS A 209 ? 0.5228 0.5267 0.6085 0.1884 -0.0122 -0.0823 209 LYS A CB 1680 C CG . LYS A 209 ? 0.6493 0.6218 0.7347 0.1954 -0.0179 -0.0762 209 LYS A CG 1681 C CD . LYS A 209 ? 0.7280 0.6648 0.7987 0.1953 -0.0120 -0.0898 209 LYS A CD 1682 C CE . LYS A 209 ? 0.7767 0.6800 0.8500 0.2017 -0.0168 -0.0845 209 LYS A CE 1683 N NZ . LYS A 209 ? 0.7565 0.6272 0.8109 0.1944 -0.0142 -0.0976 209 LYS A NZ 1684 N N . ARG A 210 ? 0.4310 0.5141 0.5699 0.2055 -0.0197 -0.0619 210 ARG A N 1685 C CA . ARG A 210 ? 0.4437 0.5503 0.6075 0.2191 -0.0255 -0.0500 210 ARG A CA 1686 C C . ARG A 210 ? 0.5574 0.6349 0.7274 0.2363 -0.0246 -0.0463 210 ARG A C 1687 O O . ARG A 210 ? 0.4767 0.5308 0.6435 0.2432 -0.0146 -0.0579 210 ARG A O 1688 C CB . ARG A 210 ? 0.4555 0.5992 0.6417 0.2252 -0.0184 -0.0542 210 ARG A CB 1689 C CG . ARG A 210 ? 0.5899 0.7617 0.8057 0.2415 -0.0237 -0.0421 210 ARG A CG 1690 C CD . ARG A 210 ? 0.6603 0.8682 0.8825 0.2311 -0.0357 -0.0326 210 ARG A CD 1691 N NE . ARG A 210 ? 0.6285 0.8598 0.8496 0.2156 -0.0310 -0.0420 210 ARG A NE 1692 C CZ . ARG A 210 ? 0.6647 0.9282 0.8912 0.2032 -0.0393 -0.0385 210 ARG A CZ 1693 N NH1 . ARG A 210 ? 0.5776 0.8572 0.8096 0.2047 -0.0534 -0.0261 210 ARG A NH1 1694 N NH2 . ARG A 210 ? 0.6581 0.9380 0.8845 0.1890 -0.0333 -0.0474 210 ARG A NH2 1695 N N . ARG A 211 ? 0.4667 0.5455 0.6451 0.2430 -0.0350 -0.0301 211 ARG A N 1696 C CA . ARG A 211 ? 0.4926 0.5435 0.6799 0.2595 -0.0348 -0.0236 211 ARG A CA 1697 C C . ARG A 211 ? 0.5681 0.6294 0.7813 0.2802 -0.0262 -0.0268 211 ARG A C 1698 O O . ARG A 211 ? 0.5806 0.6815 0.8146 0.2866 -0.0273 -0.0218 211 ARG A O 1699 C CB . ARG A 211 ? 0.5644 0.6194 0.7558 0.2622 -0.0479 -0.0026 211 ARG A CB 1700 C CG . ARG A 211 ? 0.5958 0.6144 0.7927 0.2759 -0.0481 0.0063 211 ARG A CG 1701 C CD . ARG A 211 ? 0.5263 0.5487 0.7225 0.2757 -0.0607 0.0286 211 ARG A CD 1702 N NE . ARG A 211 ? 0.5098 0.5271 0.6802 0.2551 -0.0664 0.0291 211 ARG A NE 1703 C CZ . ARG A 211 ? 0.6020 0.5816 0.7551 0.2465 -0.0654 0.0275 211 ARG A CZ 1704 N NH1 . ARG A 211 ? 0.6699 0.6121 0.8281 0.2554 -0.0592 0.0235 211 ARG A NH1 1705 N NH2 . ARG A 211 ? 0.6511 0.6303 0.7829 0.2289 -0.0701 0.0288 211 ARG A NH2 1706 N N . SER A 212 ? 0.6915 0.7168 0.9038 0.2904 -0.0175 -0.0359 212 SER A N 1707 C CA . SER A 212 ? 0.8062 0.8345 1.0428 0.3125 -0.0079 -0.0396 212 SER A CA 1708 C C . SER A 212 ? 0.7359 0.7664 0.9959 0.3300 -0.0153 -0.0196 212 SER A C 1709 O O . SER A 212 ? 0.7248 0.7309 0.9778 0.3281 -0.0236 -0.0074 212 SER A O 1710 C CB . SER A 212 ? 0.9035 0.8886 1.1295 0.3175 0.0036 -0.0574 212 SER A CB 1711 O OG . SER A 212 ? 0.9254 0.9080 1.1761 0.3412 0.0126 -0.0596 212 SER A OG 1712 N N . HIS A 213 ? 0.5855 0.6467 0.8745 0.3475 -0.0120 -0.0150 213 HIS A N 1713 C CA . HIS A 213 ? 0.6366 0.7004 0.9511 0.3677 -0.0175 0.0041 213 HIS A CA 1714 C C . HIS A 213 ? 0.6205 0.6742 0.9584 0.3874 -0.0035 -0.0037 213 HIS A C 1715 O O . HIS A 213 ? 0.6344 0.7122 1.0022 0.3993 -0.0051 0.0086 213 HIS A O 1716 C CB . HIS A 213 ? 0.7158 0.8329 1.0464 0.3673 -0.0295 0.0214 213 HIS A CB 1717 C CG . HIS A 213 ? 0.7367 0.8974 1.0747 0.3606 -0.0250 0.0109 213 HIS A CG 1718 N ND1 . HIS A 213 ? 0.7790 0.9485 1.0939 0.3368 -0.0257 0.0000 213 HIS A ND1 1719 C CD2 . HIS A 213 ? 0.6351 0.8328 1.0028 0.3745 -0.0189 0.0102 213 HIS A CD2 1720 C CE1 . HIS A 213 ? 0.7765 0.9855 1.1064 0.3357 -0.0204 -0.0066 213 HIS A CE1 1721 N NE2 . HIS A 213 ? 0.7182 0.9461 1.0802 0.3580 -0.0162 -0.0008 213 HIS A NE2 1722 N N . HIS A 214 ? 0.6473 0.6652 0.9708 0.3857 0.0096 -0.0247 214 HIS A N 1723 C CA . HIS A 214 ? 0.7828 0.7920 1.1257 0.3983 0.0255 -0.0358 214 HIS A CA 1724 C C . HIS A 214 ? 0.9945 0.9500 1.3392 0.4043 0.0322 -0.0406 214 HIS A C 1725 O O . HIS A 214 ? 0.9081 0.8578 1.2796 0.4167 0.0282 -0.0290 214 HIS A O 1726 C CB . HIS A 214 ? 0.8016 0.8243 1.1327 0.3931 0.0391 -0.0581 214 HIS A CB 1727 C CG . HIS A 214 ? 0.9308 0.9499 1.2806 0.4057 0.0562 -0.0693 214 HIS A CG 1728 N ND1 . HIS A 214 ? 1.0031 1.0340 1.3898 0.4223 0.0568 -0.0586 214 HIS A ND1 1729 C CD2 . HIS A 214 ? 0.9687 0.9747 1.3054 0.4041 0.0726 -0.0910 214 HIS A CD2 1730 C CE1 . HIS A 214 ? 1.0020 1.0266 1.3989 0.4308 0.0734 -0.0741 214 HIS A CE1 1731 N NE2 . HIS A 214 ? 1.0536 1.0631 1.4192 0.4199 0.0841 -0.0932 214 HIS A NE2 1732 N N . HIS A 215 ? 1.1698 1.0872 1.4878 0.3955 0.0411 -0.0596 215 HIS A N 1733 C CA . HIS A 215 ? 1.1099 0.9789 1.4316 0.4012 0.0505 -0.0654 215 HIS A CA 1734 C C . HIS A 215 ? 1.0478 0.9263 1.4042 0.4184 0.0609 -0.0692 215 HIS A C 1735 O O . HIS A 215 ? 0.8736 0.7263 1.2463 0.4257 0.0579 -0.0693 215 HIS A O 1736 C CB . HIS A 215 ? 1.0985 0.9402 1.4234 0.3996 0.0383 -0.0460 215 HIS A CB 1737 C CG . HIS A 215 ? 1.0915 0.9337 1.3886 0.3836 0.0245 -0.0398 215 HIS A CG 1738 N ND1 . HIS A 215 ? 1.1876 1.0041 1.4511 0.3672 0.0252 -0.0570 215 HIS A ND1 1739 C CD2 . HIS A 215 ? 1.1144 0.9820 1.4136 0.3806 0.0086 -0.0198 215 HIS A CD2 1740 C CE1 . HIS A 215 ? 1.1542 0.9791 1.4033 0.3552 0.0106 -0.0478 215 HIS A CE1 1741 N NE2 . HIS A 215 ? 1.1718 1.0270 1.4398 0.3635 0.0013 -0.0253 215 HIS A NE2 # 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 ALA 1 1 ? ? ? A . n A 1 2 ASP 2 2 2 ASP ASP A . n A 1 3 GLY 3 3 3 GLY GLY A . n A 1 4 LYS 4 4 4 LYS LYS A . n A 1 5 TYR 5 5 5 TYR TYR A . n A 1 6 ALA 6 6 6 ALA ALA A . n A 1 7 GLN 7 7 7 GLN GLN A . n A 1 8 LYS 8 8 8 LYS LYS A . n A 1 9 LEU 9 9 9 LEU LEU A . n A 1 10 PHE 10 10 10 PHE PHE A . n A 1 11 ASN 11 11 11 ASN ASN A . n A 1 12 ASP 12 12 12 ASP ASP A . n A 1 13 LEU 13 13 13 LEU LEU A . n A 1 14 PHE 14 14 14 PHE PHE A . n A 1 15 GLU 15 15 15 GLU GLU A . n A 1 16 ASP 16 16 16 ASP ASP A . n A 1 17 TYR 17 17 17 TYR TYR A . n A 1 18 SER 18 18 18 SER SER A . n A 1 19 ASN 19 19 19 ASN ASN A . n A 1 20 ALA 20 20 20 ALA ALA A . n A 1 21 LEU 21 21 21 LEU LEU A . n A 1 22 ARG 22 22 22 ARG ARG A . n A 1 23 PRO 23 23 23 PRO PRO A . n A 1 24 VAL 24 24 24 VAL VAL A . n A 1 25 GLU 25 25 25 GLU GLU A . n A 1 26 ASP 26 26 26 ASP ASP A . n A 1 27 THR 27 27 27 THR THR A . n A 1 28 ASP 28 28 28 ASP ASP A . n A 1 29 LYS 29 29 29 LYS LYS A . n A 1 30 VAL 30 30 30 VAL VAL A . n A 1 31 LEU 31 31 31 LEU LEU A . n A 1 32 ASN 32 32 32 ASN ASN A . n A 1 33 VAL 33 33 33 VAL VAL A . n A 1 34 THR 34 34 34 THR THR A . n A 1 35 LEU 35 35 35 LEU LEU A . n A 1 36 GLN 36 36 36 GLN GLN A . n A 1 37 ILE 37 37 37 ILE ILE A . n A 1 38 THR 38 38 38 THR THR A . n A 1 39 LEU 39 39 39 LEU LEU A . n A 1 40 SER 40 40 40 SER SER A . n A 1 41 GLN 41 41 41 GLN GLN A . n A 1 42 ILE 42 42 42 ILE ILE A . n A 1 43 LYS 43 43 43 LYS LYS A . n A 1 44 ASP 44 44 44 ASP ASP A . n A 1 45 MET 45 45 45 MET MET A . n A 1 46 ASP 46 46 46 ASP ASP A . n A 1 47 GLU 47 47 47 GLU GLU A . n A 1 48 ARG 48 48 48 ARG ARG A . n A 1 49 ASN 49 49 49 ASN ASN A . n A 1 50 GLN 50 50 50 GLN GLN A . n A 1 51 ILE 51 51 51 ILE ILE A . n A 1 52 LEU 52 52 52 LEU LEU A . n A 1 53 THR 53 53 53 THR THR A . n A 1 54 ALA 54 54 54 ALA ALA A . n A 1 55 TYR 55 55 55 TYR TYR A . n A 1 56 LEU 56 56 56 LEU LEU A . n A 1 57 TRP 57 57 57 TRP TRP A . n A 1 58 ILE 58 58 58 ILE ILE A . n A 1 59 ARG 59 59 59 ARG ARG A . n A 1 60 GLN 60 60 60 GLN GLN A . n A 1 61 ILE 61 61 61 ILE ILE A . n A 1 62 TRP 62 62 62 TRP TRP A . n A 1 63 HIS 63 63 63 HIS HIS A . n A 1 64 ASP 64 64 64 ASP ASP A . n A 1 65 ALA 65 65 65 ALA ALA A . n A 1 66 TYR 66 66 66 TYR TYR A . n A 1 67 LEU 67 67 67 LEU LEU A . n A 1 68 THR 68 68 68 THR THR A . n A 1 69 TRP 69 69 69 TRP TRP A . n A 1 70 ASP 70 70 70 ASP ASP A . n A 1 71 ARG 71 71 71 ARG ARG A . n A 1 72 ASP 72 72 72 ASP ASP A . n A 1 73 GLN 73 73 73 GLN GLN A . n A 1 74 TYR 74 74 74 TYR TYR A . n A 1 75 ASP 75 75 75 ASP ASP A . n A 1 76 GLY 76 76 76 GLY GLY A . n A 1 77 LEU 77 77 77 LEU LEU A . n A 1 78 ASP 78 78 78 ASP ASP A . n A 1 79 SER 79 79 79 SER SER A . n A 1 80 ILE 80 80 80 ILE ILE A . n A 1 81 ARG 81 81 81 ARG ARG A . n A 1 82 ILE 82 82 82 ILE ILE A . n A 1 83 PRO 83 83 83 PRO PRO A . n A 1 84 SER 84 84 84 SER SER A . n A 1 85 ASP 85 85 85 ASP ASP A . n A 1 86 LEU 86 86 86 LEU LEU A . n A 1 87 VAL 87 87 87 VAL VAL A . n A 1 88 TRP 88 88 88 TRP TRP A . n A 1 89 ARG 89 89 89 ARG ARG A . n A 1 90 PRO 90 90 90 PRO PRO A . n A 1 91 ASP 91 91 91 ASP ASP A . n A 1 92 ILE 92 92 92 ILE ILE A . n A 1 93 VAL 93 93 93 VAL VAL A . n A 1 94 LEU 94 94 94 LEU LEU A . n A 1 95 TYR 95 95 95 TYR TYR A . n A 1 96 ASN 96 96 96 ASN ASN A . n A 1 97 LYS 97 97 97 LYS LYS A . n A 1 98 ALA 98 98 98 ALA ALA A . n A 1 99 ASP 99 99 99 ASP ASP A . n A 1 100 ASP 100 100 100 ASP ASP A . n A 1 101 GLU 101 101 101 GLU GLU A . n A 1 102 SER 102 102 ? ? ? A . n A 1 103 SER 103 103 ? ? ? A . n A 1 104 GLU 104 104 104 GLU GLU A . n A 1 105 PRO 105 105 105 PRO PRO A . n A 1 106 VAL 106 106 106 VAL VAL A . n A 1 107 ASN 107 107 107 ASN ASN A . n A 1 108 THR 108 108 108 THR THR A . n A 1 109 ASN 109 109 109 ASN ASN A . n A 1 110 VAL 110 110 110 VAL VAL A . n A 1 111 VAL 111 111 111 VAL VAL A . n A 1 112 LEU 112 112 112 LEU LEU A . n A 1 113 ARG 113 113 113 ARG ARG A . n A 1 114 TYR 114 114 114 TYR TYR A . n A 1 115 ASP 115 115 115 ASP ASP A . n A 1 116 GLY 116 116 116 GLY GLY A . n A 1 117 LEU 117 117 117 LEU LEU A . n A 1 118 ILE 118 118 118 ILE ILE A . n A 1 119 THR 119 119 119 THR THR A . n A 1 120 TRP 120 120 120 TRP TRP A . n A 1 121 ASP 121 121 121 ASP ASP A . n A 1 122 ALA 122 122 122 ALA ALA A . n A 1 123 PRO 123 123 123 PRO PRO A . n A 1 124 ALA 124 124 124 ALA ALA A . n A 1 125 ILE 125 125 125 ILE ILE A . n A 1 126 THR 126 126 126 THR THR A . n A 1 127 LYS 127 127 127 LYS LYS A . n A 1 128 SER 128 128 128 SER SER A . n A 1 129 SER 129 129 129 SER SER A . n A 1 130 CYS 130 130 130 CYS CYS A . n A 1 131 VAL 131 131 131 VAL VAL A . n A 1 132 VAL 132 132 132 VAL VAL A . n A 1 133 ASP 133 133 133 ASP ASP A . n A 1 134 VAL 134 134 134 VAL VAL A . n A 1 135 THR 135 135 135 THR THR A . n A 1 136 TYR 136 136 136 TYR TYR A . n A 1 137 PHE 137 137 137 PHE PHE A . n A 1 138 PRO 138 138 138 PRO PRO A . n A 1 139 PHE 139 139 139 PHE PHE A . n A 1 140 ASP 140 140 140 ASP ASP A . n A 1 141 ASN 141 141 141 ASN ASN A . n A 1 142 GLN 142 142 142 GLN GLN A . n A 1 143 GLN 143 143 143 GLN GLN A . n A 1 144 CYS 144 144 144 CYS CYS A . n A 1 145 ASN 145 145 145 ASN ASN A . n A 1 146 LEU 146 146 146 LEU LEU A . n A 1 147 THR 147 147 147 THR THR A . n A 1 148 PHE 148 148 148 PHE PHE A . n A 1 149 GLY 149 149 149 GLY GLY A . n A 1 150 SER 150 150 150 SER SER A . n A 1 151 TRP 151 151 151 TRP TRP A . n A 1 152 THR 152 152 152 THR THR A . n A 1 153 TYR 153 153 153 TYR TYR A . n A 1 154 ASN 154 154 154 ASN ASN A . n A 1 155 GLY 155 155 155 GLY GLY A . n A 1 156 ASN 156 156 156 ASN ASN A . n A 1 157 GLN 157 157 157 GLN GLN A . n A 1 158 VAL 158 158 158 VAL VAL A . n A 1 159 ASP 159 159 159 ASP ASP A . n A 1 160 ILE 160 160 160 ILE ILE A . n A 1 161 PHE 161 161 161 PHE PHE A . n A 1 162 ASN 162 162 162 ASN ASN A . n A 1 163 ALA 163 163 163 ALA ALA A . n A 1 164 LEU 164 164 164 LEU LEU A . n A 1 165 ASP 165 165 165 ASP ASP A . n A 1 166 SER 166 166 166 SER SER A . n A 1 167 GLY 167 167 167 GLY GLY A . n A 1 168 ASP 168 168 168 ASP ASP A . n A 1 169 LEU 169 169 169 LEU LEU A . n A 1 170 SER 170 170 170 SER SER A . n A 1 171 ASP 171 171 171 ASP ASP A . n A 1 172 PHE 172 172 172 PHE PHE A . n A 1 173 ILE 173 173 173 ILE ILE A . n A 1 174 GLU 174 174 174 GLU GLU A . n A 1 175 ASP 175 175 175 ASP ASP A . n A 1 176 VAL 176 176 176 VAL VAL A . n A 1 177 GLU 177 177 177 GLU GLU A . n A 1 178 TRP 178 178 178 TRP TRP A . n A 1 179 GLU 179 179 179 GLU GLU A . n A 1 180 VAL 180 180 180 VAL VAL A . n A 1 181 HIS 181 181 181 HIS HIS A . n A 1 182 GLY 182 182 182 GLY GLY A . n A 1 183 MET 183 183 183 MET MET A . n A 1 184 PRO 184 184 184 PRO PRO A . n A 1 185 ALA 185 185 185 ALA ALA A . n A 1 186 VAL 186 186 186 VAL VAL A . n A 1 187 LYS 187 187 187 LYS LYS A . n A 1 188 ASN 188 188 188 ASN ASN A . n A 1 189 VAL 189 189 189 VAL VAL A . n A 1 190 ILE 190 190 190 ILE ILE A . n A 1 191 SER 191 191 191 SER SER A . n A 1 192 TYR 192 192 192 TYR TYR A . n A 1 193 GLY 193 193 193 GLY GLY A . n A 1 194 CYS 194 194 194 CYS CYS A . n A 1 195 CYS 195 195 195 CYS CYS A . n A 1 196 SER 196 196 196 SER SER A . n A 1 197 GLU 197 197 197 GLU GLU A . n A 1 198 PRO 198 198 198 PRO PRO A . n A 1 199 TYR 199 199 199 TYR TYR A . n A 1 200 PRO 200 200 200 PRO PRO A . n A 1 201 ASP 201 201 201 ASP ASP A . n A 1 202 VAL 202 202 202 VAL VAL A . n A 1 203 THR 203 203 203 THR THR A . n A 1 204 PHE 204 204 204 PHE PHE A . n A 1 205 THR 205 205 205 THR THR A . n A 1 206 LEU 206 206 206 LEU LEU A . n A 1 207 LEU 207 207 207 LEU LEU A . n A 1 208 LEU 208 208 208 LEU LEU A . n A 1 209 LYS 209 209 209 LYS LYS A . n A 1 210 ARG 210 210 210 ARG ARG A . n A 1 211 ARG 211 211 211 ARG ARG A . n A 1 212 SER 212 212 212 SER SER A . n A 1 213 HIS 213 213 213 HIS HIS A . n A 1 214 HIS 214 214 214 HIS HIS A . n A 1 215 HIS 215 215 215 HIS HIS A . n A 1 216 HIS 216 216 ? ? ? A . n A 1 217 HIS 217 217 ? ? ? A . n A 1 218 HIS 218 218 ? ? ? A . n # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code B 2 NAG 1 1216 1216 NAG NAG A . C 2 NAG 1 1217 1217 NAG NAG A . D 3 EDO 1 1218 1218 EDO EDO A . E 3 EDO 1 1219 1219 EDO EDO A . F 3 EDO 1 1220 1220 EDO EDO A . G 3 EDO 1 1221 1221 EDO EDO A . H 4 HOH 1 2001 2001 HOH HOH A . H 4 HOH 2 2002 2002 HOH HOH A . H 4 HOH 3 2003 2003 HOH HOH A . H 4 HOH 4 2004 2004 HOH HOH A . H 4 HOH 5 2005 2005 HOH HOH A . H 4 HOH 6 2006 2006 HOH HOH A . H 4 HOH 7 2007 2007 HOH HOH A . H 4 HOH 8 2008 2008 HOH HOH A . H 4 HOH 9 2009 2009 HOH HOH A . H 4 HOH 10 2010 2010 HOH HOH A . H 4 HOH 11 2011 2011 HOH HOH A . H 4 HOH 12 2012 2012 HOH HOH A . H 4 HOH 13 2013 2013 HOH HOH A . H 4 HOH 14 2014 2014 HOH HOH A . H 4 HOH 15 2015 2015 HOH HOH A . H 4 HOH 16 2016 2016 HOH HOH A . H 4 HOH 17 2017 2017 HOH HOH A . H 4 HOH 18 2018 2018 HOH HOH A . H 4 HOH 19 2019 2019 HOH HOH A . H 4 HOH 20 2020 2020 HOH HOH A . H 4 HOH 21 2021 2021 HOH HOH A . H 4 HOH 22 2022 2022 HOH HOH A . H 4 HOH 23 2023 2023 HOH HOH A . H 4 HOH 24 2024 2024 HOH HOH A . H 4 HOH 25 2025 2025 HOH HOH A . H 4 HOH 26 2026 2026 HOH HOH A . H 4 HOH 27 2027 2027 HOH HOH A . H 4 HOH 28 2028 2028 HOH HOH A . H 4 HOH 29 2029 2029 HOH HOH A . H 4 HOH 30 2030 2030 HOH HOH A . H 4 HOH 31 2031 2031 HOH HOH A . H 4 HOH 32 2032 2032 HOH HOH A . H 4 HOH 33 2033 2033 HOH HOH A . H 4 HOH 34 2034 2034 HOH HOH A . H 4 HOH 35 2035 2035 HOH HOH A . H 4 HOH 36 2036 2036 HOH HOH A . H 4 HOH 37 2037 2037 HOH HOH A . H 4 HOH 38 2038 2038 HOH HOH A . H 4 HOH 39 2039 2039 HOH HOH A . H 4 HOH 40 2040 2040 HOH HOH A . H 4 HOH 41 2041 2041 HOH HOH A . H 4 HOH 42 2042 2042 HOH HOH A . H 4 HOH 43 2043 2043 HOH HOH A . H 4 HOH 44 2044 2044 HOH HOH A . H 4 HOH 45 2045 2045 HOH HOH A . H 4 HOH 46 2046 2046 HOH HOH A . H 4 HOH 47 2047 2047 HOH HOH A . H 4 HOH 48 2048 2048 HOH HOH A . H 4 HOH 49 2049 2049 HOH HOH A . H 4 HOH 50 2050 2050 HOH HOH A . H 4 HOH 51 2051 2051 HOH HOH A . H 4 HOH 52 2052 2052 HOH HOH A . H 4 HOH 53 2053 2053 HOH HOH A . H 4 HOH 54 2054 2054 HOH HOH A . H 4 HOH 55 2055 2055 HOH HOH A . H 4 HOH 56 2056 2056 HOH HOH A . H 4 HOH 57 2057 2057 HOH HOH A . H 4 HOH 58 2058 2058 HOH HOH A . H 4 HOH 59 2059 2059 HOH HOH A . H 4 HOH 60 2060 2060 HOH HOH A . H 4 HOH 61 2061 2061 HOH HOH A . H 4 HOH 62 2062 2062 HOH HOH A . H 4 HOH 63 2063 2063 HOH HOH A . H 4 HOH 64 2064 2064 HOH HOH A . H 4 HOH 65 2065 2065 HOH HOH A . H 4 HOH 66 2066 2066 HOH HOH A . H 4 HOH 67 2067 2067 HOH HOH A . H 4 HOH 68 2068 2068 HOH HOH A . H 4 HOH 69 2069 2069 HOH HOH A . H 4 HOH 70 2070 2070 HOH HOH A . H 4 HOH 71 2071 2071 HOH HOH A . H 4 HOH 72 2072 2072 HOH HOH A . H 4 HOH 73 2073 2073 HOH HOH A . H 4 HOH 74 2074 2074 HOH HOH A . H 4 HOH 75 2075 2075 HOH HOH A . H 4 HOH 76 2076 2076 HOH HOH A . H 4 HOH 77 2077 2077 HOH HOH A . H 4 HOH 78 2078 2078 HOH HOH A . H 4 HOH 79 2079 2079 HOH HOH A . H 4 HOH 80 2080 2080 HOH HOH A . H 4 HOH 81 2081 2081 HOH HOH A . H 4 HOH 82 2082 2082 HOH HOH A . H 4 HOH 83 2083 2083 HOH HOH A . H 4 HOH 84 2084 2084 HOH HOH A . H 4 HOH 85 2085 2085 HOH HOH A . H 4 HOH 86 2086 2086 HOH HOH A . H 4 HOH 87 2087 2087 HOH HOH A . H 4 HOH 88 2088 2088 HOH HOH A . H 4 HOH 89 2089 2089 HOH HOH A . H 4 HOH 90 2090 2090 HOH HOH A . H 4 HOH 91 2091 2091 HOH HOH A . H 4 HOH 92 2092 2092 HOH HOH A . H 4 HOH 93 2093 2093 HOH HOH A . H 4 HOH 94 2094 2094 HOH HOH A . H 4 HOH 95 2095 2095 HOH HOH A . H 4 HOH 96 2096 2096 HOH HOH A . H 4 HOH 97 2097 2097 HOH HOH A . H 4 HOH 98 2098 2098 HOH HOH A . H 4 HOH 99 2099 2099 HOH HOH A . H 4 HOH 100 2100 2100 HOH HOH A . H 4 HOH 101 2101 2101 HOH HOH A . H 4 HOH 102 2102 2102 HOH HOH A . H 4 HOH 103 2103 2103 HOH HOH A . H 4 HOH 104 2104 2104 HOH HOH A . H 4 HOH 105 2105 2105 HOH HOH A . H 4 HOH 106 2106 2106 HOH HOH A . H 4 HOH 107 2107 2107 HOH HOH A . H 4 HOH 108 2108 2108 HOH HOH A . H 4 HOH 109 2109 2109 HOH HOH A . H 4 HOH 110 2110 2110 HOH HOH A . H 4 HOH 111 2111 2111 HOH HOH A . H 4 HOH 112 2112 2112 HOH HOH A . H 4 HOH 113 2113 2113 HOH HOH A . H 4 HOH 114 2114 2114 HOH HOH A . H 4 HOH 115 2115 2115 HOH HOH A . H 4 HOH 116 2116 2116 HOH HOH A . H 4 HOH 117 2117 2117 HOH HOH A . H 4 HOH 118 2118 2118 HOH HOH A . H 4 HOH 119 2119 2119 HOH HOH A . H 4 HOH 120 2120 2120 HOH HOH A . H 4 HOH 121 2121 2121 HOH HOH A . H 4 HOH 122 2122 2122 HOH HOH A . H 4 HOH 123 2123 2123 HOH HOH A . H 4 HOH 124 2124 2124 HOH HOH A . H 4 HOH 125 2125 2125 HOH HOH A . H 4 HOH 126 2126 2126 HOH HOH A . H 4 HOH 127 2127 2127 HOH HOH A . H 4 HOH 128 2128 2128 HOH HOH A . H 4 HOH 129 2129 2129 HOH HOH A . H 4 HOH 130 2130 2130 HOH HOH A . H 4 HOH 131 2131 2131 HOH HOH A . H 4 HOH 132 2132 2132 HOH HOH A . H 4 HOH 133 2133 2133 HOH HOH A . H 4 HOH 134 2134 2134 HOH HOH A . H 4 HOH 135 2135 2135 HOH HOH A . H 4 HOH 136 2136 2136 HOH HOH A . H 4 HOH 137 2137 2137 HOH HOH A . H 4 HOH 138 2138 2138 HOH HOH A . H 4 HOH 139 2139 2139 HOH HOH A . H 4 HOH 140 2140 2140 HOH HOH A . H 4 HOH 141 2141 2141 HOH HOH A . H 4 HOH 142 2142 2142 HOH HOH A . H 4 HOH 143 2143 2143 HOH HOH A . H 4 HOH 144 2144 2144 HOH HOH A . H 4 HOH 145 2145 2145 HOH HOH A . H 4 HOH 146 2146 2146 HOH HOH A . H 4 HOH 147 2147 2147 HOH HOH A . H 4 HOH 148 2148 2148 HOH HOH A . H 4 HOH 149 2149 2149 HOH HOH A . H 4 HOH 150 2150 2150 HOH HOH A . H 4 HOH 151 2151 2151 HOH HOH A . H 4 HOH 152 2152 2152 HOH HOH A . H 4 HOH 153 2153 2153 HOH HOH A . H 4 HOH 154 2154 2154 HOH HOH A . H 4 HOH 155 2155 2155 HOH HOH A . H 4 HOH 156 2156 2156 HOH HOH A . H 4 HOH 157 2157 2157 HOH HOH A . H 4 HOH 158 2158 2158 HOH HOH A . H 4 HOH 159 2159 2159 HOH HOH A . H 4 HOH 160 2160 2160 HOH HOH A . H 4 HOH 161 2161 2161 HOH HOH A . H 4 HOH 162 2162 2162 HOH HOH A . H 4 HOH 163 2163 2163 HOH HOH A . H 4 HOH 164 2164 2164 HOH HOH A . H 4 HOH 165 2165 2165 HOH HOH A . H 4 HOH 166 2166 2166 HOH HOH A . H 4 HOH 167 2167 2167 HOH HOH A . H 4 HOH 168 2168 2168 HOH HOH A . H 4 HOH 169 2169 2169 HOH HOH A . H 4 HOH 170 2170 2170 HOH HOH A . H 4 HOH 171 2171 2171 HOH HOH A . H 4 HOH 172 2172 2172 HOH HOH A . H 4 HOH 173 2173 2173 HOH HOH A . H 4 HOH 174 2174 2174 HOH HOH A . H 4 HOH 175 2175 2175 HOH HOH A . H 4 HOH 176 2176 2176 HOH HOH A . H 4 HOH 177 2177 2177 HOH HOH A . H 4 HOH 178 2178 2178 HOH HOH A . H 4 HOH 179 2179 2179 HOH HOH A . H 4 HOH 180 2180 2180 HOH HOH A . H 4 HOH 181 2181 2181 HOH HOH A . H 4 HOH 182 2182 2182 HOH HOH A . H 4 HOH 183 2183 2183 HOH HOH A . H 4 HOH 184 2184 2184 HOH HOH A . H 4 HOH 185 2185 2185 HOH HOH A . H 4 HOH 186 2186 2186 HOH HOH A . H 4 HOH 187 2187 2187 HOH HOH A . H 4 HOH 188 2188 2188 HOH HOH A . H 4 HOH 189 2189 2189 HOH HOH A . H 4 HOH 190 2190 2190 HOH HOH A . H 4 HOH 191 2191 2191 HOH HOH A . H 4 HOH 192 2192 2192 HOH HOH A . H 4 HOH 193 2193 2193 HOH HOH A . H 4 HOH 194 2194 2194 HOH HOH A . H 4 HOH 195 2195 2195 HOH HOH A . H 4 HOH 196 2196 2196 HOH HOH A . H 4 HOH 197 2197 2197 HOH HOH A . H 4 HOH 198 2198 2198 HOH HOH A . H 4 HOH 199 2199 2199 HOH HOH A . H 4 HOH 200 2200 2200 HOH HOH A . H 4 HOH 201 2201 2201 HOH HOH A . H 4 HOH 202 2202 2202 HOH HOH A . H 4 HOH 203 2203 2203 HOH HOH A . H 4 HOH 204 2204 2204 HOH HOH A . H 4 HOH 205 2205 2205 HOH HOH A . H 4 HOH 206 2206 2206 HOH HOH A . # 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 32 A ASN 32 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 145 A ASN 145 ? 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 # _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 # _pdbx_struct_special_symmetry.id 1 _pdbx_struct_special_symmetry.PDB_model_num 1 _pdbx_struct_special_symmetry.auth_asym_id A _pdbx_struct_special_symmetry.auth_comp_id HOH _pdbx_struct_special_symmetry.auth_seq_id 2072 _pdbx_struct_special_symmetry.PDB_ins_code ? _pdbx_struct_special_symmetry.label_asym_id H _pdbx_struct_special_symmetry.label_comp_id HOH _pdbx_struct_special_symmetry.label_seq_id . # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 2014-10-01 2 'Structure model' 1 1 2014-10-08 3 'Structure model' 1 2 2014-10-15 4 'Structure model' 1 3 2014-11-19 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # loop_ _pdbx_audit_revision_group.ordinal _pdbx_audit_revision_group.revision_ordinal _pdbx_audit_revision_group.data_content_type _pdbx_audit_revision_group.group 1 2 'Structure model' 'Database references' 2 3 'Structure model' 'Database references' 3 4 'Structure model' 'Database references' # loop_ _pdbx_refine_tls.pdbx_refine_id _pdbx_refine_tls.id _pdbx_refine_tls.details _pdbx_refine_tls.method _pdbx_refine_tls.origin_x _pdbx_refine_tls.origin_y _pdbx_refine_tls.origin_z _pdbx_refine_tls.T[1][1] _pdbx_refine_tls.T[2][2] _pdbx_refine_tls.T[3][3] _pdbx_refine_tls.T[1][2] _pdbx_refine_tls.T[1][3] _pdbx_refine_tls.T[2][3] _pdbx_refine_tls.L[1][1] _pdbx_refine_tls.L[2][2] _pdbx_refine_tls.L[3][3] _pdbx_refine_tls.L[1][2] _pdbx_refine_tls.L[1][3] _pdbx_refine_tls.L[2][3] _pdbx_refine_tls.S[1][1] _pdbx_refine_tls.S[1][2] _pdbx_refine_tls.S[1][3] _pdbx_refine_tls.S[2][1] _pdbx_refine_tls.S[2][2] _pdbx_refine_tls.S[2][3] _pdbx_refine_tls.S[3][1] _pdbx_refine_tls.S[3][2] _pdbx_refine_tls.S[3][3] 'X-RAY DIFFRACTION' 1 ? refined 48.7613 35.9854 12.5707 0.4652 0.3936 0.4914 -0.1077 0.1261 0.0266 2.0851 3.1610 3.4929 0.7469 -1.3760 -1.6466 -0.3799 0.1475 -0.2122 -0.5524 -0.1809 -0.9078 0.2188 0.6531 0.5711 'X-RAY DIFFRACTION' 2 ? refined 33.7775 42.3805 19.4146 0.3770 0.3105 0.2745 -0.0076 -0.0620 0.0092 1.3298 1.7167 1.6332 0.0962 -0.4508 0.0827 -0.2765 0.3035 0.1590 -0.2470 0.0821 -0.0276 -0.2310 -0.2487 0.1562 'X-RAY DIFFRACTION' 3 ? refined 32.2295 39.5996 18.0307 0.4081 0.4347 0.3870 0.0166 -0.0078 -0.1089 7.1308 2.6267 0.5770 2.9227 -0.8722 -0.6256 -0.0196 0.4234 0.1323 -0.1227 -0.0967 0.2384 -0.3878 -0.3287 -0.0003 'X-RAY DIFFRACTION' 4 ? refined 22.5012 42.3829 31.5330 0.3229 0.2854 0.2653 0.0480 -0.0460 -0.0485 2.2865 1.3472 1.4802 -0.0691 -0.3039 -0.3236 -0.0501 0.1651 0.2647 0.0106 -0.0511 0.1903 -0.2033 -0.3244 0.0909 # 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 ? ? ? ? ? ? ? ? ? 'CHAIN A AND (RESID 2 THROUGH 30 )' 'X-RAY DIFFRACTION' 2 2 ? ? ? ? ? ? ? ? ? 'CHAIN A AND (RESID 31 THROUGH 94 )' 'X-RAY DIFFRACTION' 3 3 ? ? ? ? ? ? ? ? ? 'CHAIN A AND (RESID 95 THROUGH 116 )' 'X-RAY DIFFRACTION' 4 4 ? ? ? ? ? ? ? ? ? 'CHAIN A AND (RESID 117 THROUGH 215 )' # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal PHENIX refinement '(PHENIX.REFINE)' ? 1 XDS 'data reduction' . ? 2 SCALA 'data scaling' . ? 3 PHASER phasing . ? 4 # _pdbx_entry_details.entry_id 4D01 _pdbx_entry_details.compound_details ? _pdbx_entry_details.source_details ? _pdbx_entry_details.nonpolymer_details ? _pdbx_entry_details.sequence_details 'EXTRACELLULAR DOMAIN' # loop_ _pdbx_validate_close_contact.id _pdbx_validate_close_contact.PDB_model_num _pdbx_validate_close_contact.auth_atom_id_1 _pdbx_validate_close_contact.auth_asym_id_1 _pdbx_validate_close_contact.auth_comp_id_1 _pdbx_validate_close_contact.auth_seq_id_1 _pdbx_validate_close_contact.PDB_ins_code_1 _pdbx_validate_close_contact.label_alt_id_1 _pdbx_validate_close_contact.auth_atom_id_2 _pdbx_validate_close_contact.auth_asym_id_2 _pdbx_validate_close_contact.auth_comp_id_2 _pdbx_validate_close_contact.auth_seq_id_2 _pdbx_validate_close_contact.PDB_ins_code_2 _pdbx_validate_close_contact.label_alt_id_2 _pdbx_validate_close_contact.dist 1 1 O A HOH 2001 ? ? O A HOH 2203 ? ? 2.03 2 1 O A HOH 2029 ? ? O A HOH 2033 ? ? 2.03 3 1 O A HOH 2169 ? ? O A HOH 2170 ? ? 2.06 4 1 O A HOH 2004 ? ? O A HOH 2019 ? ? 2.07 5 1 O A HOH 2196 ? ? O A HOH 2197 ? ? 2.09 6 1 O A HOH 2043 ? ? O A HOH 2081 ? ? 2.13 # _pdbx_validate_symm_contact.id 1 _pdbx_validate_symm_contact.PDB_model_num 1 _pdbx_validate_symm_contact.auth_atom_id_1 O _pdbx_validate_symm_contact.auth_asym_id_1 A _pdbx_validate_symm_contact.auth_comp_id_1 HOH _pdbx_validate_symm_contact.auth_seq_id_1 2091 _pdbx_validate_symm_contact.PDB_ins_code_1 ? _pdbx_validate_symm_contact.label_alt_id_1 ? _pdbx_validate_symm_contact.site_symmetry_1 1_555 _pdbx_validate_symm_contact.auth_atom_id_2 O _pdbx_validate_symm_contact.auth_asym_id_2 A _pdbx_validate_symm_contact.auth_comp_id_2 HOH _pdbx_validate_symm_contact.auth_seq_id_2 2091 _pdbx_validate_symm_contact.PDB_ins_code_2 ? _pdbx_validate_symm_contact.label_alt_id_2 ? _pdbx_validate_symm_contact.site_symmetry_2 2_566 _pdbx_validate_symm_contact.dist 2.15 # _pdbx_validate_rmsd_bond.id 1 _pdbx_validate_rmsd_bond.PDB_model_num 1 _pdbx_validate_rmsd_bond.auth_atom_id_1 C _pdbx_validate_rmsd_bond.auth_asym_id_1 A _pdbx_validate_rmsd_bond.auth_comp_id_1 PHE _pdbx_validate_rmsd_bond.auth_seq_id_1 14 _pdbx_validate_rmsd_bond.PDB_ins_code_1 ? _pdbx_validate_rmsd_bond.label_alt_id_1 ? _pdbx_validate_rmsd_bond.auth_atom_id_2 O _pdbx_validate_rmsd_bond.auth_asym_id_2 A _pdbx_validate_rmsd_bond.auth_comp_id_2 PHE _pdbx_validate_rmsd_bond.auth_seq_id_2 14 _pdbx_validate_rmsd_bond.PDB_ins_code_2 ? _pdbx_validate_rmsd_bond.label_alt_id_2 ? _pdbx_validate_rmsd_bond.bond_value 1.108 _pdbx_validate_rmsd_bond.bond_target_value 1.229 _pdbx_validate_rmsd_bond.bond_deviation -0.121 _pdbx_validate_rmsd_bond.bond_standard_deviation 0.019 _pdbx_validate_rmsd_bond.linker_flag N # 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 LEU A 67 ? ? -113.06 55.21 2 1 ASN A 96 ? B -94.97 40.65 3 1 GLU A 174 ? A 78.80 144.87 4 1 GLU A 174 ? B 80.16 132.26 5 1 MET A 183 ? ? -150.50 61.53 6 1 HIS A 214 ? ? -117.54 -86.07 # loop_ _pdbx_distant_solvent_atoms.id _pdbx_distant_solvent_atoms.PDB_model_num _pdbx_distant_solvent_atoms.auth_atom_id _pdbx_distant_solvent_atoms.label_alt_id _pdbx_distant_solvent_atoms.auth_asym_id _pdbx_distant_solvent_atoms.auth_comp_id _pdbx_distant_solvent_atoms.auth_seq_id _pdbx_distant_solvent_atoms.PDB_ins_code _pdbx_distant_solvent_atoms.neighbor_macromolecule_distance _pdbx_distant_solvent_atoms.neighbor_ligand_distance 1 1 O ? A HOH 2084 ? 7.59 . 2 1 O ? A HOH 2092 ? 6.48 . # loop_ _pdbx_unobs_or_zero_occ_atoms.id _pdbx_unobs_or_zero_occ_atoms.PDB_model_num _pdbx_unobs_or_zero_occ_atoms.polymer_flag _pdbx_unobs_or_zero_occ_atoms.occupancy_flag _pdbx_unobs_or_zero_occ_atoms.auth_asym_id _pdbx_unobs_or_zero_occ_atoms.auth_comp_id _pdbx_unobs_or_zero_occ_atoms.auth_seq_id _pdbx_unobs_or_zero_occ_atoms.PDB_ins_code _pdbx_unobs_or_zero_occ_atoms.auth_atom_id _pdbx_unobs_or_zero_occ_atoms.label_alt_id _pdbx_unobs_or_zero_occ_atoms.label_asym_id _pdbx_unobs_or_zero_occ_atoms.label_comp_id _pdbx_unobs_or_zero_occ_atoms.label_seq_id _pdbx_unobs_or_zero_occ_atoms.label_atom_id 1 1 Y 1 A ASP 99 ? CB ? A ASP 99 CB 2 1 Y 1 A ASP 99 ? CG ? A ASP 99 CG 3 1 Y 1 A ASP 99 ? OD1 ? A ASP 99 OD1 4 1 Y 1 A ASP 99 ? OD2 ? A ASP 99 OD2 5 1 Y 1 A ASP 100 ? CB ? A ASP 100 CB 6 1 Y 1 A ASP 100 ? CG ? A ASP 100 CG 7 1 Y 1 A ASP 100 ? OD1 ? A ASP 100 OD1 8 1 Y 1 A ASP 100 ? OD2 ? A ASP 100 OD2 9 1 Y 1 A GLU 101 ? CB ? A GLU 101 CB 10 1 Y 1 A GLU 101 ? CG ? A GLU 101 CG 11 1 Y 1 A GLU 101 ? CD ? A GLU 101 CD 12 1 Y 1 A GLU 101 ? OE1 ? A GLU 101 OE1 13 1 Y 1 A GLU 101 ? OE2 ? A GLU 101 OE2 14 1 Y 1 A GLU 104 ? CB ? A GLU 104 CB 15 1 Y 1 A GLU 104 ? CG ? A GLU 104 CG 16 1 Y 1 A GLU 104 ? CD ? A GLU 104 CD 17 1 Y 1 A GLU 104 ? OE1 ? A GLU 104 OE1 18 1 Y 1 A GLU 104 ? OE2 ? A GLU 104 OE2 # 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 ALA 1 ? A ALA 1 2 1 Y 1 A SER 102 ? A SER 102 3 1 Y 1 A SER 103 ? A SER 103 4 1 Y 1 A HIS 216 ? A HIS 216 5 1 Y 1 A HIS 217 ? A HIS 217 6 1 Y 1 A HIS 218 ? A HIS 218 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 N-ACETYL-D-GLUCOSAMINE NAG 3 1,2-ETHANEDIOL EDO 4 water HOH #