data_1DVY # _entry.id 1DVY # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.281 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 1DVY RCSB RCSB010422 WWPDB D_1000010422 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.details _pdbx_database_related.content_type PDB 1BMZ 'HUMAN TRANSTHYRETIN (PREALBUMIN)' unspecified PDB 1DVQ 'CRYSTAL STRUCTURE OF HUMAN TRANSTHYRETIN' unspecified PDB 1DVS 'CRYSTAL STRUCTURE OF HUMAN TRANSTHYRETIN IN COMPLEX WITH RESVERATROL' unspecified PDB 1DVT 'CRYSTAL STRUCTURE OF HUMAN TRANSTHYRETIN IN COMPLEX WITH FLURBIPROFEN' unspecified PDB 1DVU 'CRYSTAL STRUCTURE OF HUMAN TRANSTHYRETIN IN COMPLEX WITH DIBENZOFURAN-4,6-DICARBOXYLIC ACID' unspecified PDB 1DVX 'CRYSTAL STRUCTURE OF HUMAN TRANSTHYRETIN IN COMPLEX WITH DICLOFENAC' unspecified PDB 1DVZ ;CRYSTAL STRUCTURE OF HUMAN TRANSTHYRETIN IN COMPLEX WITH O-TRIFLUOROMETHYLPHENYL ANTHRANILIC ACID ; unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 1DVY _pdbx_database_status.recvd_initial_deposition_date 2000-01-23 _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site RCSB _pdbx_database_status.SG_entry . _pdbx_database_status.pdb_format_compatible Y _pdbx_database_status.status_code_mr ? _pdbx_database_status.status_code_sf ? _pdbx_database_status.status_code_cs ? # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Klabunde, T.' 1 'Petrassi, H.M.' 2 'Oza, V.B.' 3 'Kelly, J.W.' 4 'Sacchettini, J.C.' 5 # _citation.id primary _citation.title 'Rational design of potent human transthyretin amyloid disease inhibitors.' _citation.journal_abbrev Nat.Struct.Biol. _citation.journal_volume 7 _citation.page_first 312 _citation.page_last 321 _citation.year 2000 _citation.journal_id_ASTM NSBIEW _citation.country US _citation.journal_id_ISSN 1072-8368 _citation.journal_id_CSD 2024 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 10742177 _citation.pdbx_database_id_DOI 10.1038/74082 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Klabunde, T.' 1 primary 'Petrassi, H.M.' 2 primary 'Oza, V.B.' 3 primary 'Raman, P.' 4 primary 'Kelly, J.W.' 5 primary 'Sacchettini, J.C.' 6 # _cell.entry_id 1DVY _cell.length_a 43.290 _cell.length_b 86.030 _cell.length_c 65.230 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 90.00 _cell.Z_PDB 8 _cell.pdbx_unique_axis ? # _symmetry.entry_id 1DVY _symmetry.space_group_name_H-M 'P 21 21 2' _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 TRANSTHYRETIN 13420.968 2 ? ? ? ? 2 non-polymer syn 'N-(M-TRIFLUOROMETHYLPHENYL) PHENOXAZINE-4,6-DICARBOXYLIC ACID' 415.319 1 ? ? ? ? 3 water nat water 18.015 49 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name PREALBUMIN # _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 ;GPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEQFVEGIYKVEIDTKSYWK ALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTN ; _entity_poly.pdbx_seq_one_letter_code_can ;GPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEQFVEGIYKVEIDTKSYWK ALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTN ; _entity_poly.pdbx_strand_id A,B _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 GLY n 1 2 PRO n 1 3 THR n 1 4 GLY n 1 5 THR n 1 6 GLY n 1 7 GLU n 1 8 SER n 1 9 LYS n 1 10 CYS n 1 11 PRO n 1 12 LEU n 1 13 MET n 1 14 VAL n 1 15 LYS n 1 16 VAL n 1 17 LEU n 1 18 ASP n 1 19 ALA n 1 20 VAL n 1 21 ARG n 1 22 GLY n 1 23 SER n 1 24 PRO n 1 25 ALA n 1 26 ILE n 1 27 ASN n 1 28 VAL n 1 29 ALA n 1 30 VAL n 1 31 HIS n 1 32 VAL n 1 33 PHE n 1 34 ARG n 1 35 LYS n 1 36 ALA n 1 37 ALA n 1 38 ASP n 1 39 ASP n 1 40 THR n 1 41 TRP n 1 42 GLU n 1 43 PRO n 1 44 PHE n 1 45 ALA n 1 46 SER n 1 47 GLY n 1 48 LYS n 1 49 THR n 1 50 SER n 1 51 GLU n 1 52 SER n 1 53 GLY n 1 54 GLU n 1 55 LEU n 1 56 HIS n 1 57 GLY n 1 58 LEU n 1 59 THR n 1 60 THR n 1 61 GLU n 1 62 GLU n 1 63 GLN n 1 64 PHE n 1 65 VAL n 1 66 GLU n 1 67 GLY n 1 68 ILE n 1 69 TYR n 1 70 LYS n 1 71 VAL n 1 72 GLU n 1 73 ILE n 1 74 ASP n 1 75 THR n 1 76 LYS n 1 77 SER n 1 78 TYR n 1 79 TRP n 1 80 LYS n 1 81 ALA n 1 82 LEU n 1 83 GLY n 1 84 ILE n 1 85 SER n 1 86 PRO n 1 87 PHE n 1 88 HIS n 1 89 GLU n 1 90 HIS n 1 91 ALA n 1 92 GLU n 1 93 VAL n 1 94 VAL n 1 95 PHE n 1 96 THR n 1 97 ALA n 1 98 ASN n 1 99 ASP n 1 100 SER n 1 101 GLY n 1 102 PRO n 1 103 ARG n 1 104 ARG n 1 105 TYR n 1 106 THR n 1 107 ILE n 1 108 ALA n 1 109 ALA n 1 110 LEU n 1 111 LEU n 1 112 SER n 1 113 PRO n 1 114 TYR n 1 115 SER n 1 116 TYR n 1 117 SER n 1 118 THR n 1 119 THR n 1 120 ALA n 1 121 VAL n 1 122 VAL n 1 123 THR n 1 124 ASN 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 Homo _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 'Escherichia coli' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 562 _entity_src_gen.host_org_genus Escherichia _entity_src_gen.pdbx_host_org_gene ? _entity_src_gen.pdbx_host_org_organ ? _entity_src_gen.host_org_species ? _entity_src_gen.pdbx_host_org_tissue ? _entity_src_gen.pdbx_host_org_tissue_fraction ? _entity_src_gen.pdbx_host_org_strain ? _entity_src_gen.pdbx_host_org_variant ? _entity_src_gen.pdbx_host_org_cell_line ? _entity_src_gen.pdbx_host_org_atcc ? _entity_src_gen.pdbx_host_org_culture_collection ? _entity_src_gen.pdbx_host_org_cell ? _entity_src_gen.pdbx_host_org_organelle ? _entity_src_gen.pdbx_host_org_cellular_location ? _entity_src_gen.pdbx_host_org_vector_type ? _entity_src_gen.pdbx_host_org_vector ? _entity_src_gen.host_org_details ? _entity_src_gen.expression_system_id ? _entity_src_gen.plasmid_name ? _entity_src_gen.plasmid_details ? _entity_src_gen.pdbx_description ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code TTHY_HUMAN _struct_ref.entity_id 1 _struct_ref.pdbx_db_accession P02766 _struct_ref.pdbx_align_begin 1 _struct_ref.pdbx_seq_one_letter_code ;GPTGTGESKCPLMVKVLDAVRGSPAINVAMHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWK ALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTN ; _struct_ref.pdbx_db_isoform ? # loop_ _struct_ref_seq.align_id _struct_ref_seq.ref_id _struct_ref_seq.pdbx_PDB_id_code _struct_ref_seq.pdbx_strand_id _struct_ref_seq.seq_align_beg _struct_ref_seq.pdbx_seq_align_beg_ins_code _struct_ref_seq.seq_align_end _struct_ref_seq.pdbx_seq_align_end_ins_code _struct_ref_seq.pdbx_db_accession _struct_ref_seq.db_align_beg _struct_ref_seq.pdbx_db_align_beg_ins_code _struct_ref_seq.db_align_end _struct_ref_seq.pdbx_db_align_end_ins_code _struct_ref_seq.pdbx_auth_seq_align_beg _struct_ref_seq.pdbx_auth_seq_align_end 1 1 1DVY A 1 ? 124 ? P02766 1 ? 124 ? 1 124 2 1 1DVY B 1 ? 124 ? P02766 1 ? 124 ? 1 124 # 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 BPD non-polymer . 'N-(M-TRIFLUOROMETHYLPHENYL) PHENOXAZINE-4,6-DICARBOXYLIC ACID' ? 'C21 H12 F3 N O5' 415.319 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 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 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 1DVY _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.26 _exptl_crystal.density_percent_sol 45.61 _exptl_crystal.description ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method 'VAPOR DIFFUSION, HANGING DROP' _exptl_crystal_grow.temp 293 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 7.4 _exptl_crystal_grow.pdbx_details 'potassium chloride, potassium phosphate, ammonium sulfate, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 293K' _exptl_crystal_grow.pdbx_pH_range . # _diffrn.id 1 _diffrn.ambient_temp 293 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector 'IMAGE PLATE' _diffrn_detector.type MACSCIENCE _diffrn_detector.pdbx_collection_date 1998-11-11 _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 1.5418 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source 'ROTATING ANODE' _diffrn_source.type 'RIGAKU RU200' _diffrn_source.pdbx_synchrotron_site ? _diffrn_source.pdbx_synchrotron_beamline ? _diffrn_source.pdbx_wavelength 1.5418 _diffrn_source.pdbx_wavelength_list ? # _reflns.entry_id 1DVY _reflns.observed_criterion_sigma_I 0 _reflns.observed_criterion_sigma_F 0 _reflns.d_resolution_low 10 _reflns.d_resolution_high 1.8 _reflns.number_obs 22052 _reflns.number_all 22052 _reflns.percent_possible_obs 95.3 _reflns.pdbx_Rmerge_I_obs 0.0440000 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 18.0 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 3.43 _reflns.R_free_details ? _reflns.limit_h_max ? _reflns.limit_h_min ? _reflns.limit_k_max ? _reflns.limit_k_min ? _reflns.limit_l_max ? _reflns.limit_l_min ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.pdbx_ordinal 1 _reflns.pdbx_diffrn_id 1 # _reflns_shell.d_res_high 1.8 _reflns_shell.d_res_low 1.9 _reflns_shell.percent_possible_all 97.5 _reflns_shell.Rmerge_I_obs 0.1730000 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs ? _reflns_shell.pdbx_redundancy ? _reflns_shell.percent_possible_obs ? _reflns_shell.number_unique_all ? _reflns_shell.pdbx_ordinal 1 _reflns_shell.pdbx_diffrn_id 1 # _refine.entry_id 1DVY _refine.ls_number_reflns_obs 16092 _refine.ls_number_reflns_all 17037 _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F 3 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.ls_d_res_low 8 _refine.ls_d_res_high 1.9 _refine.ls_percent_reflns_obs 82.4 _refine.ls_R_factor_obs ? _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.2020000 _refine.ls_R_factor_R_free 0.2030000 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free ? _refine.ls_number_reflns_R_free 1578 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.B_iso_mean ? _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 ? _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_ls_cross_valid_method ? _refine.details ;The structure contains two PHENOX molecules that bind in each of two independent binding sites of the tetramer. Since the binding is along the 2-fold crystallographic axis, an occupancy of 0.5 corresponds to saturation of each of the binding sites. ; _refine.pdbx_starting_model ? _refine.pdbx_method_to_determine_struct ? _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values 'Engh & Huber' _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details 'randomly chosen subset of 10 % of observed reflections' _refine.pdbx_overall_ESU_R_Free ? _refine.overall_SU_B ? _refine.ls_redundancy_reflns_obs ? _refine.B_iso_min ? _refine.B_iso_max ? _refine.overall_SU_ML ? _refine.pdbx_overall_ESU_R ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.correlation_coeff_Fo_to_Fc ? _refine.correlation_coeff_Fo_to_Fc_free ? _refine.overall_SU_R_Cruickshank_DPI ? _refine.overall_SU_R_free ? _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.pdbx_solvent_vdw_probe_radii ? _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii ? _refine.pdbx_overall_phase_error ? _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 1771 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 30 _refine_hist.number_atoms_solvent 49 _refine_hist.number_atoms_total 1850 _refine_hist.d_res_high 1.9 _refine_hist.d_res_low 8 # 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 c_angle_deg 1.2327 ? ? ? 'X-RAY DIFFRACTION' ? c_bond_d 0.008 ? ? ? 'X-RAY DIFFRACTION' ? # _struct.entry_id 1DVY _struct.title 'CRYSTAL STRUCTURE OF TRANSTHYRETIN IN COMPLEX WITH N-(M-TRIFLUOROMETHYLPHENYL) PHENOXAZINE-4,6-DICARBOXYLIC ACID' _struct.pdbx_descriptor 'TRANSTHYRETIN / N-(M-TRIFLUOROMETHYLPHENYL) PHENOXAZINE-4,6-DICARBOXYLIC ACID COMPLEX' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 1DVY _struct_keywords.pdbx_keywords 'HORMONE/GROWTH FACTOR' _struct_keywords.text 'THYROXINE TRANSPORT, SIGNALING PROTEIN, HORMONE-GROWTH FACTOR COMPLEX' # 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 1 ? C N N 2 ? D N N 3 ? E N N 3 ? # _struct_biol.id 1 _struct_biol.details 'The biological assembly is a tetramer constructed from the homodimer (chain A and B) and a symmetry mate generated by the two-fold' _struct_biol.pdbx_parent_biol_id ? # 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 ASP A 74 ? ALA A 81 ? ASP A 74 ALA A 81 1 ? 8 HELX_P HELX_P2 2 ASP B 74 ? ALA B 81 ? ASP B 74 ALA B 81 1 ? 8 # _struct_conf_type.id HELX_P _struct_conf_type.criteria ? _struct_conf_type.reference ? # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 8 ? B ? 8 ? C ? 8 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense A 1 2 ? anti-parallel A 2 3 ? parallel A 3 4 ? anti-parallel A 4 5 ? anti-parallel A 5 6 ? anti-parallel A 6 7 ? parallel A 7 8 ? anti-parallel B 1 2 ? anti-parallel B 2 3 ? parallel B 3 4 ? anti-parallel B 4 5 ? anti-parallel B 5 6 ? anti-parallel B 6 7 ? parallel B 7 8 ? anti-parallel C 1 2 ? anti-parallel C 2 3 ? anti-parallel C 3 4 ? anti-parallel C 4 5 ? anti-parallel C 5 6 ? anti-parallel C 6 7 ? anti-parallel C 7 8 ? anti-parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id A 1 SER A 23 ? PRO A 24 ? SER A 23 PRO A 24 A 2 LEU A 12 ? ASP A 18 ? LEU A 12 ASP A 18 A 3 ARG A 104 ? SER A 112 ? ARG A 104 SER A 112 A 4 SER A 115 ? THR A 123 ? SER A 115 THR A 123 A 5 SER B 115 ? THR B 123 ? SER B 115 THR B 123 A 6 ARG B 104 ? SER B 112 ? ARG B 104 SER B 112 A 7 LEU B 12 ? ASP B 18 ? LEU B 12 ASP B 18 A 8 SER B 23 ? PRO B 24 ? SER B 23 PRO B 24 B 1 GLU A 54 ? LEU A 55 ? GLU A 54 LEU A 55 B 2 LEU A 12 ? ASP A 18 ? LEU A 12 ASP A 18 B 3 ARG A 104 ? SER A 112 ? ARG A 104 SER A 112 B 4 SER A 115 ? THR A 123 ? SER A 115 THR A 123 B 5 SER B 115 ? THR B 123 ? SER B 115 THR B 123 B 6 ARG B 104 ? SER B 112 ? ARG B 104 SER B 112 B 7 LEU B 12 ? ASP B 18 ? LEU B 12 ASP B 18 B 8 GLU B 54 ? LEU B 55 ? GLU B 54 LEU B 55 C 1 TRP A 41 ? LYS A 48 ? TRP A 41 LYS A 48 C 2 ALA A 29 ? LYS A 35 ? ALA A 29 LYS A 35 C 3 GLY A 67 ? ILE A 73 ? GLY A 67 ILE A 73 C 4 HIS A 88 ? ALA A 97 ? HIS A 88 ALA A 97 C 5 HIS B 88 ? ALA B 97 ? HIS B 88 ALA B 97 C 6 GLY B 67 ? ILE B 73 ? GLY B 67 ILE B 73 C 7 ALA B 29 ? LYS B 35 ? ALA B 29 LYS B 35 C 8 TRP B 41 ? LYS B 48 ? TRP B 41 LYS B 48 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id A 1 2 O SER A 23 ? O SER A 23 N ASP A 18 ? N ASP A 18 A 2 3 N MET A 13 ? N MET A 13 O TYR A 105 ? O TYR A 105 A 3 4 N SER A 112 ? N SER A 112 O SER A 115 ? O SER A 115 A 4 5 N THR A 118 ? N THR A 118 O TYR B 116 ? O TYR B 116 A 5 6 O THR B 123 ? O THR B 123 N ARG B 104 ? N ARG B 104 A 6 7 O TYR B 105 ? O TYR B 105 N MET B 13 ? N MET B 13 A 7 8 N ASP B 18 ? N ASP B 18 O SER B 23 ? O SER B 23 B 1 2 N LEU A 55 ? N LEU A 55 O VAL A 14 ? O VAL A 14 B 2 3 N MET A 13 ? N MET A 13 O TYR A 105 ? O TYR A 105 B 3 4 N SER A 112 ? N SER A 112 O SER A 115 ? O SER A 115 B 4 5 N THR A 118 ? N THR A 118 O TYR B 116 ? O TYR B 116 B 5 6 O THR B 123 ? O THR B 123 N ARG B 104 ? N ARG B 104 B 6 7 O TYR B 105 ? O TYR B 105 N MET B 13 ? N MET B 13 B 7 8 O VAL B 14 ? O VAL B 14 N LEU B 55 ? N LEU B 55 C 1 2 O GLY A 47 ? O GLY A 47 N VAL A 30 ? N VAL A 30 C 2 3 N LYS A 35 ? N LYS A 35 O ILE A 68 ? O ILE A 68 C 3 4 N ILE A 73 ? N ILE A 73 O ALA A 91 ? O ALA A 91 C 4 5 O VAL A 94 ? O VAL A 94 N GLU B 89 ? N GLU B 89 C 5 6 N ALA B 97 ? N ALA B 97 O GLY B 67 ? O GLY B 67 C 6 7 N GLU B 72 ? N GLU B 72 O HIS B 31 ? O HIS B 31 C 7 8 O ARG B 34 ? O ARG B 34 N GLU B 42 ? N GLU B 42 # _struct_site.id AC1 _struct_site.pdbx_evidence_code Software _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 21 _struct_site.details 'BINDING SITE FOR RESIDUE BPD A 125' # 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 21 MET A 13 ? MET A 13 . ? 1_555 ? 2 AC1 21 LYS A 15 ? LYS A 15 . ? 1_555 ? 3 AC1 21 LEU A 17 ? LEU A 17 . ? 1_555 ? 4 AC1 21 LEU A 17 ? LEU A 17 . ? 2_665 ? 5 AC1 21 GLU A 54 ? GLU A 54 . ? 1_555 ? 6 AC1 21 THR A 106 ? THR A 106 . ? 2_665 ? 7 AC1 21 THR A 106 ? THR A 106 . ? 1_555 ? 8 AC1 21 ALA A 108 ? ALA A 108 . ? 1_555 ? 9 AC1 21 ALA A 108 ? ALA A 108 . ? 2_665 ? 10 AC1 21 LEU A 110 ? LEU A 110 . ? 1_555 ? 11 AC1 21 VAL A 121 ? VAL A 121 . ? 2_665 ? 12 AC1 21 LYS B 15 ? LYS B 15 . ? 1_555 ? 13 AC1 21 LEU B 17 ? LEU B 17 . ? 2_665 ? 14 AC1 21 LEU B 17 ? LEU B 17 . ? 1_555 ? 15 AC1 21 GLU B 54 ? GLU B 54 . ? 1_555 ? 16 AC1 21 THR B 106 ? THR B 106 . ? 1_555 ? 17 AC1 21 THR B 106 ? THR B 106 . ? 2_665 ? 18 AC1 21 ALA B 108 ? ALA B 108 . ? 2_665 ? 19 AC1 21 ALA B 108 ? ALA B 108 . ? 1_555 ? 20 AC1 21 LEU B 110 ? LEU B 110 . ? 1_555 ? 21 AC1 21 VAL B 121 ? VAL B 121 . ? 2_665 ? # _database_PDB_matrix.entry_id 1DVY _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 1DVY _atom_sites.fract_transf_matrix[1][1] 0.023100 _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] 0.011624 _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] 0.015330 _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 F 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 . CYS A 1 10 ? 15.238 31.055 -7.658 1.00 42.81 ? 10 CYS A N 1 ATOM 2 C CA . CYS A 1 10 ? 16.038 31.063 -6.400 1.00 42.20 ? 10 CYS A CA 1 ATOM 3 C C . CYS A 1 10 ? 15.138 31.391 -5.209 1.00 36.69 ? 10 CYS A C 1 ATOM 4 O O . CYS A 1 10 ? 15.023 32.546 -4.797 1.00 38.55 ? 10 CYS A O 1 ATOM 5 C CB . CYS A 1 10 ? 17.167 32.094 -6.504 1.00 45.47 ? 10 CYS A CB 1 ATOM 6 S SG . CYS A 1 10 ? 18.468 31.916 -5.256 1.00 58.60 ? 10 CYS A SG 1 ATOM 7 N N . PRO A 1 11 ? 14.484 30.368 -4.642 1.00 33.02 ? 11 PRO A N 1 ATOM 8 C CA . PRO A 1 11 ? 13.588 30.536 -3.497 1.00 29.01 ? 11 PRO A CA 1 ATOM 9 C C . PRO A 1 11 ? 14.295 30.627 -2.143 1.00 25.70 ? 11 PRO A C 1 ATOM 10 O O . PRO A 1 11 ? 13.689 31.011 -1.145 1.00 22.43 ? 11 PRO A O 1 ATOM 11 C CB . PRO A 1 11 ? 12.695 29.306 -3.589 1.00 30.41 ? 11 PRO A CB 1 ATOM 12 C CG . PRO A 1 11 ? 13.641 28.270 -4.073 1.00 31.17 ? 11 PRO A CG 1 ATOM 13 C CD . PRO A 1 11 ? 14.399 28.993 -5.170 1.00 32.69 ? 11 PRO A CD 1 ATOM 14 N N . LEU A 1 12 ? 15.570 30.266 -2.105 1.00 22.63 ? 12 LEU A N 1 ATOM 15 C CA . LEU A 1 12 ? 16.310 30.312 -0.851 1.00 19.42 ? 12 LEU A CA 1 ATOM 16 C C . LEU A 1 12 ? 17.673 30.933 -1.076 1.00 21.58 ? 12 LEU A C 1 ATOM 17 O O . LEU A 1 12 ? 18.461 30.430 -1.871 1.00 22.76 ? 12 LEU A O 1 ATOM 18 C CB . LEU A 1 12 ? 16.471 28.901 -0.283 1.00 22.03 ? 12 LEU A CB 1 ATOM 19 C CG . LEU A 1 12 ? 17.245 28.733 1.026 1.00 26.30 ? 12 LEU A CG 1 ATOM 20 C CD1 . LEU A 1 12 ? 16.544 29.509 2.143 1.00 23.46 ? 12 LEU A CD1 1 ATOM 21 C CD2 . LEU A 1 12 ? 17.332 27.244 1.374 1.00 23.40 ? 12 LEU A CD2 1 ATOM 22 N N . MET A 1 13 ? 17.943 32.036 -0.383 1.00 19.91 ? 13 MET A N 1 ATOM 23 C CA . MET A 1 13 ? 19.227 32.704 -0.517 1.00 23.91 ? 13 MET A CA 1 ATOM 24 C C . MET A 1 13 ? 19.783 33.031 0.868 1.00 20.34 ? 13 MET A C 1 ATOM 25 O O . MET A 1 13 ? 19.028 33.290 1.803 1.00 16.97 ? 13 MET A O 1 ATOM 26 C CB . MET A 1 13 ? 19.084 33.987 -1.331 1.00 28.25 ? 13 MET A CB 1 ATOM 27 C CG . MET A 1 13 ? 20.425 34.611 -1.688 1.00 40.91 ? 13 MET A CG 1 ATOM 28 S SD . MET A 1 13 ? 20.269 36.257 -2.382 1.00 53.44 ? 13 MET A SD 1 ATOM 29 C CE . MET A 1 13 ? 20.447 37.251 -0.907 1.00 49.95 ? 13 MET A CE 1 ATOM 30 N N . VAL A 1 14 ? 21.106 33.006 0.993 1.00 18.68 ? 14 VAL A N 1 ATOM 31 C CA . VAL A 1 14 ? 21.747 33.290 2.271 1.00 16.51 ? 14 VAL A CA 1 ATOM 32 C C . VAL A 1 14 ? 22.774 34.388 2.069 1.00 19.31 ? 14 VAL A C 1 ATOM 33 O O . VAL A 1 14 ? 23.527 34.383 1.090 1.00 19.44 ? 14 VAL A O 1 ATOM 34 C CB . VAL A 1 14 ? 22.429 32.020 2.846 1.00 17.61 ? 14 VAL A CB 1 ATOM 35 C CG1 . VAL A 1 14 ? 23.097 32.334 4.192 1.00 18.68 ? 14 VAL A CG1 1 ATOM 36 C CG2 . VAL A 1 14 ? 21.395 30.917 3.010 1.00 19.67 ? 14 VAL A CG2 1 ATOM 37 N N . LYS A 1 15 ? 22.790 35.334 3.000 1.00 17.88 ? 15 LYS A N 1 ATOM 38 C CA . LYS A 1 15 ? 23.706 36.457 2.942 1.00 19.39 ? 15 LYS A CA 1 ATOM 39 C C . LYS A 1 15 ? 24.394 36.562 4.293 1.00 19.92 ? 15 LYS A C 1 ATOM 40 O O . LYS A 1 15 ? 23.731 36.635 5.328 1.00 19.15 ? 15 LYS A O 1 ATOM 41 C CB . LYS A 1 15 ? 22.918 37.736 2.654 1.00 23.90 ? 15 LYS A CB 1 ATOM 42 C CG . LYS A 1 15 ? 23.727 39.018 2.698 1.00 28.92 ? 15 LYS A CG 1 ATOM 43 C CD . LYS A 1 15 ? 24.556 39.213 1.445 1.00 36.29 ? 15 LYS A CD 1 ATOM 44 C CE . LYS A 1 15 ? 25.185 40.601 1.427 1.00 38.55 ? 15 LYS A CE 1 ATOM 45 N NZ . LYS A 1 15 ? 25.885 40.887 0.148 1.00 42.62 ? 15 LYS A NZ 1 ATOM 46 N N . VAL A 1 16 ? 25.720 36.569 4.285 1.00 18.41 ? 16 VAL A N 1 ATOM 47 C CA . VAL A 1 16 ? 26.463 36.641 5.531 1.00 18.80 ? 16 VAL A CA 1 ATOM 48 C C . VAL A 1 16 ? 27.438 37.814 5.514 1.00 18.80 ? 16 VAL A C 1 ATOM 49 O O . VAL A 1 16 ? 28.205 37.988 4.563 1.00 16.19 ? 16 VAL A O 1 ATOM 50 C CB . VAL A 1 16 ? 27.241 35.327 5.794 1.00 20.37 ? 16 VAL A CB 1 ATOM 51 C CG1 . VAL A 1 16 ? 27.813 35.333 7.211 1.00 20.11 ? 16 VAL A CG1 1 ATOM 52 C CG2 . VAL A 1 16 ? 26.325 34.123 5.593 1.00 21.06 ? 16 VAL A CG2 1 ATOM 53 N N . LEU A 1 17 ? 27.390 38.618 6.572 1.00 16.25 ? 17 LEU A N 1 ATOM 54 C CA . LEU A 1 17 ? 28.260 39.779 6.703 1.00 17.34 ? 17 LEU A CA 1 ATOM 55 C C . LEU A 1 17 ? 29.156 39.673 7.936 1.00 17.16 ? 17 LEU A C 1 ATOM 56 O O . LEU A 1 17 ? 28.798 39.043 8.928 1.00 16.26 ? 17 LEU A O 1 ATOM 57 C CB . LEU A 1 17 ? 27.430 41.059 6.809 1.00 18.67 ? 17 LEU A CB 1 ATOM 58 C CG . LEU A 1 17 ? 26.549 41.456 5.621 1.00 19.86 ? 17 LEU A CG 1 ATOM 59 C CD1 . LEU A 1 17 ? 25.857 42.758 5.963 1.00 23.18 ? 17 LEU A CD1 1 ATOM 60 C CD2 . LEU A 1 17 ? 27.392 41.621 4.361 1.00 24.06 ? 17 LEU A CD2 1 ATOM 61 N N . ASP A 1 18 ? 30.310 40.323 7.860 1.00 16.03 ? 18 ASP A N 1 ATOM 62 C CA . ASP A 1 18 ? 31.293 40.342 8.942 1.00 16.94 ? 18 ASP A CA 1 ATOM 63 C C . ASP A 1 18 ? 31.243 41.713 9.628 1.00 18.24 ? 18 ASP A C 1 ATOM 64 O O . ASP A 1 18 ? 31.596 42.725 9.025 1.00 16.71 ? 18 ASP A O 1 ATOM 65 C CB . ASP A 1 18 ? 32.679 40.104 8.345 1.00 19.06 ? 18 ASP A CB 1 ATOM 66 C CG . ASP A 1 18 ? 33.763 40.032 9.389 1.00 18.86 ? 18 ASP A CG 1 ATOM 67 O OD1 . ASP A 1 18 ? 33.721 40.808 10.367 1.00 17.35 ? 18 ASP A OD1 1 ATOM 68 O OD2 . ASP A 1 18 ? 34.675 39.203 9.214 1.00 22.68 ? 18 ASP A OD2 1 ATOM 69 N N . ALA A 1 19 ? 30.807 41.739 10.887 1.00 14.46 ? 19 ALA A N 1 ATOM 70 C CA . ALA A 1 19 ? 30.680 42.980 11.645 1.00 16.56 ? 19 ALA A CA 1 ATOM 71 C C . ALA A 1 19 ? 32.007 43.523 12.177 1.00 18.43 ? 19 ALA A C 1 ATOM 72 O O . ALA A 1 19 ? 32.077 44.665 12.636 1.00 19.62 ? 19 ALA A O 1 ATOM 73 C CB . ALA A 1 19 ? 29.698 42.780 12.811 1.00 17.24 ? 19 ALA A CB 1 ATOM 74 N N . VAL A 1 20 ? 33.051 42.705 12.125 1.00 17.91 ? 20 VAL A N 1 ATOM 75 C CA . VAL A 1 20 ? 34.361 43.113 12.615 1.00 18.72 ? 20 VAL A CA 1 ATOM 76 C C . VAL A 1 20 ? 35.182 43.790 11.523 1.00 20.30 ? 20 VAL A C 1 ATOM 77 O O . VAL A 1 20 ? 35.910 44.739 11.788 1.00 19.86 ? 20 VAL A O 1 ATOM 78 C CB . VAL A 1 20 ? 35.164 41.900 13.152 1.00 20.33 ? 20 VAL A CB 1 ATOM 79 C CG1 . VAL A 1 20 ? 36.572 42.330 13.539 1.00 24.11 ? 20 VAL A CG1 1 ATOM 80 C CG2 . VAL A 1 20 ? 34.462 41.303 14.362 1.00 22.47 ? 20 VAL A CG2 1 ATOM 81 N N . ARG A 1 21 ? 35.049 43.313 10.292 1.00 20.47 ? 21 ARG A N 1 ATOM 82 C CA . ARG A 1 21 ? 35.818 43.868 9.190 1.00 21.36 ? 21 ARG A CA 1 ATOM 83 C C . ARG A 1 21 ? 35.014 44.760 8.255 1.00 21.13 ? 21 ARG A C 1 ATOM 84 O O . ARG A 1 21 ? 35.585 45.402 7.372 1.00 19.37 ? 21 ARG A O 1 ATOM 85 C CB . ARG A 1 21 ? 36.451 42.728 8.395 1.00 24.43 ? 21 ARG A CB 1 ATOM 86 C CG . ARG A 1 21 ? 37.325 41.829 9.248 1.00 30.55 ? 21 ARG A CG 1 ATOM 87 C CD . ARG A 1 21 ? 37.333 40.418 8.710 1.00 36.33 ? 21 ARG A CD 1 ATOM 88 N NE . ARG A 1 21 ? 38.235 40.221 7.605 1.00 41.47 ? 21 ARG A NE 1 ATOM 89 C CZ . ARG A 1 21 ? 38.141 39.298 6.654 1.00 43.60 ? 21 ARG A CZ 1 ATOM 90 N NH1 . ARG A 1 21 ? 37.146 38.417 6.598 1.00 45.67 ? 21 ARG A NH1 1 ATOM 91 N NH2 . ARG A 1 21 ? 39.111 39.245 5.763 1.00 44.79 ? 21 ARG A NH2 1 ATOM 92 N N . GLY A 1 22 ? 33.697 44.799 8.447 1.00 18.31 ? 22 GLY A N 1 ATOM 93 C CA . GLY A 1 22 ? 32.850 45.615 7.592 1.00 17.93 ? 22 GLY A CA 1 ATOM 94 C C . GLY A 1 22 ? 32.885 45.120 6.158 1.00 19.92 ? 22 GLY A C 1 ATOM 95 O O . GLY A 1 22 ? 33.037 45.899 5.208 1.00 18.62 ? 22 GLY A O 1 ATOM 96 N N . SER A 1 23 ? 32.733 43.815 5.992 1.00 19.00 ? 23 SER A N 1 ATOM 97 C CA . SER A 1 23 ? 32.763 43.223 4.667 1.00 19.76 ? 23 SER A CA 1 ATOM 98 C C . SER A 1 23 ? 31.895 41.978 4.626 1.00 19.78 ? 23 SER A C 1 ATOM 99 O O . SER A 1 23 ? 31.410 41.509 5.661 1.00 17.99 ? 23 SER A O 1 ATOM 100 C CB . SER A 1 23 ? 34.200 42.844 4.314 1.00 23.80 ? 23 SER A CB 1 ATOM 101 O OG . SER A 1 23 ? 34.673 41.851 5.204 1.00 31.56 ? 23 SER A OG 1 ATOM 102 N N . PRO A 1 24 ? 31.663 41.440 3.421 1.00 19.80 ? 24 PRO A N 1 ATOM 103 C CA . PRO A 1 24 ? 30.848 40.230 3.310 1.00 18.95 ? 24 PRO A CA 1 ATOM 104 C C . PRO A 1 24 ? 31.692 39.115 3.925 1.00 19.80 ? 24 PRO A C 1 ATOM 105 O O . PRO A 1 24 ? 32.921 39.218 3.950 1.00 20.62 ? 24 PRO A O 1 ATOM 106 C CB . PRO A 1 24 ? 30.700 40.045 1.798 1.00 22.01 ? 24 PRO A CB 1 ATOM 107 C CG . PRO A 1 24 ? 30.857 41.430 1.251 1.00 26.04 ? 24 PRO A CG 1 ATOM 108 C CD . PRO A 1 24 ? 31.983 41.986 2.088 1.00 18.97 ? 24 PRO A CD 1 ATOM 109 N N . ALA A 1 25 ? 31.050 38.069 4.435 1.00 16.69 ? 25 ALA A N 1 ATOM 110 C CA . ALA A 1 25 ? 31.770 36.938 5.008 1.00 16.70 ? 25 ALA A CA 1 ATOM 111 C C . ALA A 1 25 ? 31.922 35.958 3.849 1.00 18.31 ? 25 ALA A C 1 ATOM 112 O O . ALA A 1 25 ? 30.958 35.333 3.418 1.00 14.87 ? 25 ALA A O 1 ATOM 113 C CB . ALA A 1 25 ? 30.961 36.306 6.152 1.00 15.66 ? 25 ALA A CB 1 ATOM 114 N N . ILE A 1 26 ? 33.142 35.844 3.340 1.00 18.80 ? 26 ILE A N 1 ATOM 115 C CA . ILE A 1 26 ? 33.427 34.998 2.196 1.00 21.86 ? 26 ILE A CA 1 ATOM 116 C C . ILE A 1 26 ? 33.851 33.585 2.555 1.00 20.34 ? 26 ILE A C 1 ATOM 117 O O . ILE A 1 26 ? 34.498 33.356 3.578 1.00 19.12 ? 26 ILE A O 1 ATOM 118 C CB . ILE A 1 26 ? 34.520 35.667 1.323 1.00 23.47 ? 26 ILE A CB 1 ATOM 119 C CG1 . ILE A 1 26 ? 34.069 37.086 0.965 1.00 24.93 ? 26 ILE A CG1 1 ATOM 120 C CG2 . ILE A 1 26 ? 34.772 34.855 0.051 1.00 24.68 ? 26 ILE A CG2 1 ATOM 121 C CD1 . ILE A 1 26 ? 35.112 37.901 0.213 1.00 30.47 ? 26 ILE A CD1 1 ATOM 122 N N . ASN A 1 27 ? 33.470 32.642 1.699 1.00 21.81 ? 27 ASN A N 1 ATOM 123 C CA . ASN A 1 27 ? 33.805 31.230 1.878 1.00 22.99 ? 27 ASN A CA 1 ATOM 124 C C . ASN A 1 27 ? 33.275 30.595 3.158 1.00 22.63 ? 27 ASN A C 1 ATOM 125 O O . ASN A 1 27 ? 33.911 29.715 3.739 1.00 21.42 ? 27 ASN A O 1 ATOM 126 C CB . ASN A 1 27 ? 35.322 31.037 1.793 1.00 30.96 ? 27 ASN A CB 1 ATOM 127 C CG . ASN A 1 27 ? 35.790 30.750 0.381 1.00 38.46 ? 27 ASN A CG 1 ATOM 128 O OD1 . ASN A 1 27 ? 35.378 29.760 -0.226 1.00 43.31 ? 27 ASN A OD1 1 ATOM 129 N ND2 . ASN A 1 27 ? 36.650 31.610 -0.150 1.00 42.64 ? 27 ASN A ND2 1 ATOM 130 N N . VAL A 1 28 ? 32.109 31.043 3.602 1.00 17.97 ? 28 VAL A N 1 ATOM 131 C CA . VAL A 1 28 ? 31.512 30.478 4.802 1.00 18.58 ? 28 VAL A CA 1 ATOM 132 C C . VAL A 1 28 ? 30.677 29.283 4.377 1.00 16.82 ? 28 VAL A C 1 ATOM 133 O O . VAL A 1 28 ? 29.835 29.393 3.483 1.00 16.53 ? 28 VAL A O 1 ATOM 134 C CB . VAL A 1 28 ? 30.603 31.495 5.513 1.00 19.35 ? 28 VAL A CB 1 ATOM 135 C CG1 . VAL A 1 28 ? 29.943 30.846 6.725 1.00 21.94 ? 28 VAL A CG1 1 ATOM 136 C CG2 . VAL A 1 28 ? 31.429 32.707 5.948 1.00 23.53 ? 28 VAL A CG2 1 ATOM 137 N N . ALA A 1 29 ? 30.915 28.146 5.015 1.00 16.71 ? 29 ALA A N 1 ATOM 138 C CA . ALA A 1 29 ? 30.181 26.932 4.692 1.00 18.12 ? 29 ALA A CA 1 ATOM 139 C C . ALA A 1 29 ? 28.759 27.021 5.239 1.00 14.91 ? 29 ALA A C 1 ATOM 140 O O . ALA A 1 29 ? 28.540 27.442 6.379 1.00 15.27 ? 29 ALA A O 1 ATOM 141 C CB . ALA A 1 29 ? 30.904 25.711 5.280 1.00 17.07 ? 29 ALA A CB 1 ATOM 142 N N . VAL A 1 30 ? 27.794 26.637 4.412 1.00 14.08 ? 30 VAL A N 1 ATOM 143 C CA . VAL A 1 30 ? 26.389 26.647 4.813 1.00 16.54 ? 30 VAL A CA 1 ATOM 144 C C . VAL A 1 30 ? 25.765 25.292 4.483 1.00 17.17 ? 30 VAL A C 1 ATOM 145 O O . VAL A 1 30 ? 25.916 24.790 3.374 1.00 16.96 ? 30 VAL A O 1 ATOM 146 C CB . VAL A 1 30 ? 25.588 27.740 4.063 1.00 16.15 ? 30 VAL A CB 1 ATOM 147 C CG1 . VAL A 1 30 ? 24.117 27.673 4.456 1.00 19.96 ? 30 VAL A CG1 1 ATOM 148 C CG2 . VAL A 1 30 ? 26.149 29.115 4.376 1.00 18.04 ? 30 VAL A CG2 1 ATOM 149 N N . HIS A 1 31 ? 25.079 24.699 5.455 1.00 16.05 ? 31 HIS A N 1 ATOM 150 C CA . HIS A 1 31 ? 24.416 23.419 5.247 1.00 17.58 ? 31 HIS A CA 1 ATOM 151 C C . HIS A 1 31 ? 22.941 23.603 5.554 1.00 18.11 ? 31 HIS A C 1 ATOM 152 O O . HIS A 1 31 ? 22.579 24.188 6.575 1.00 17.15 ? 31 HIS A O 1 ATOM 153 C CB . HIS A 1 31 ? 24.983 22.341 6.170 1.00 19.44 ? 31 HIS A CB 1 ATOM 154 C CG . HIS A 1 31 ? 26.377 21.920 5.824 1.00 21.23 ? 31 HIS A CG 1 ATOM 155 N ND1 . HIS A 1 31 ? 27.479 22.700 6.095 1.00 25.48 ? 31 HIS A ND1 1 ATOM 156 C CD2 . HIS A 1 31 ? 26.844 20.813 5.201 1.00 23.12 ? 31 HIS A CD2 1 ATOM 157 C CE1 . HIS A 1 31 ? 28.566 22.092 5.653 1.00 23.87 ? 31 HIS A CE1 1 ATOM 158 N NE2 . HIS A 1 31 ? 28.207 20.945 5.105 1.00 27.20 ? 31 HIS A NE2 1 ATOM 159 N N . VAL A 1 32 ? 22.096 23.105 4.663 1.00 16.85 ? 32 VAL A N 1 ATOM 160 C CA . VAL A 1 32 ? 20.663 23.210 4.850 1.00 17.38 ? 32 VAL A CA 1 ATOM 161 C C . VAL A 1 32 ? 20.099 21.816 5.040 1.00 18.41 ? 32 VAL A C 1 ATOM 162 O O . VAL A 1 32 ? 20.493 20.875 4.340 1.00 19.21 ? 32 VAL A O 1 ATOM 163 C CB . VAL A 1 32 ? 19.995 23.855 3.631 1.00 17.40 ? 32 VAL A CB 1 ATOM 164 C CG1 . VAL A 1 32 ? 18.509 24.071 3.907 1.00 15.15 ? 32 VAL A CG1 1 ATOM 165 C CG2 . VAL A 1 32 ? 20.691 25.173 3.305 1.00 19.85 ? 32 VAL A CG2 1 ATOM 166 N N . PHE A 1 33 ? 19.183 21.685 5.991 1.00 16.30 ? 33 PHE A N 1 ATOM 167 C CA . PHE A 1 33 ? 18.551 20.401 6.272 1.00 18.79 ? 33 PHE A CA 1 ATOM 168 C C . PHE A 1 33 ? 17.041 20.564 6.287 1.00 21.18 ? 33 PHE A C 1 ATOM 169 O O . PHE A 1 33 ? 16.529 21.660 6.513 1.00 18.17 ? 33 PHE A O 1 ATOM 170 C CB . PHE A 1 33 ? 18.980 19.858 7.638 1.00 18.50 ? 33 PHE A CB 1 ATOM 171 C CG . PHE A 1 33 ? 20.469 19.799 7.837 1.00 21.44 ? 33 PHE A CG 1 ATOM 172 C CD1 . PHE A 1 33 ? 21.181 20.936 8.213 1.00 22.31 ? 33 PHE A CD1 1 ATOM 173 C CD2 . PHE A 1 33 ? 21.160 18.606 7.651 1.00 23.96 ? 33 PHE A CD2 1 ATOM 174 C CE1 . PHE A 1 33 ? 22.567 20.885 8.403 1.00 24.02 ? 33 PHE A CE1 1 ATOM 175 C CE2 . PHE A 1 33 ? 22.547 18.541 7.838 1.00 25.04 ? 33 PHE A CE2 1 ATOM 176 C CZ . PHE A 1 33 ? 23.250 19.683 8.215 1.00 25.55 ? 33 PHE A CZ 1 ATOM 177 N N . ARG A 1 34 ? 16.340 19.461 6.052 1.00 21.16 ? 34 ARG A N 1 ATOM 178 C CA . ARG A 1 34 ? 14.885 19.453 6.064 1.00 24.08 ? 34 ARG A CA 1 ATOM 179 C C . ARG A 1 34 ? 14.446 18.378 7.058 1.00 24.30 ? 34 ARG A C 1 ATOM 180 O O . ARG A 1 34 ? 15.002 17.274 7.089 1.00 24.28 ? 34 ARG A O 1 ATOM 181 C CB . ARG A 1 34 ? 14.326 19.147 4.672 1.00 24.27 ? 34 ARG A CB 1 ATOM 182 C CG . ARG A 1 34 ? 12.799 19.156 4.632 1.00 29.88 ? 34 ARG A CG 1 ATOM 183 C CD . ARG A 1 34 ? 12.248 19.053 3.222 1.00 31.53 ? 34 ARG A CD 1 ATOM 184 N NE . ARG A 1 34 ? 10.788 19.107 3.232 1.00 35.92 ? 34 ARG A NE 1 ATOM 185 C CZ . ARG A 1 34 ? 10.006 18.121 3.663 1.00 37.60 ? 34 ARG A CZ 1 ATOM 186 N NH1 . ARG A 1 34 ? 10.540 16.994 4.114 1.00 36.82 ? 34 ARG A NH1 1 ATOM 187 N NH2 . ARG A 1 34 ? 8.689 18.271 3.663 1.00 36.75 ? 34 ARG A NH2 1 ATOM 188 N N . LYS A 1 35 ? 13.463 18.702 7.885 1.00 23.35 ? 35 LYS A N 1 ATOM 189 C CA . LYS A 1 35 ? 12.995 17.750 8.873 1.00 27.38 ? 35 LYS A CA 1 ATOM 190 C C . LYS A 1 35 ? 12.247 16.635 8.158 1.00 27.73 ? 35 LYS A C 1 ATOM 191 O O . LYS A 1 35 ? 11.292 16.888 7.418 1.00 24.88 ? 35 LYS A O 1 ATOM 192 C CB . LYS A 1 35 ? 12.087 18.447 9.887 1.00 30.96 ? 35 LYS A CB 1 ATOM 193 C CG . LYS A 1 35 ? 12.194 17.884 11.295 1.00 36.92 ? 35 LYS A CG 1 ATOM 194 C CD . LYS A 1 35 ? 11.395 18.722 12.280 1.00 40.98 ? 35 LYS A CD 1 ATOM 195 C CE . LYS A 1 35 ? 11.653 18.285 13.711 1.00 44.94 ? 35 LYS A CE 1 ATOM 196 N NZ . LYS A 1 35 ? 13.090 18.427 14.070 1.00 43.92 ? 35 LYS A NZ 1 ATOM 197 N N . ALA A 1 36 ? 12.699 15.403 8.365 1.00 32.40 ? 36 ALA A N 1 ATOM 198 C CA . ALA A 1 36 ? 12.080 14.244 7.733 1.00 36.46 ? 36 ALA A CA 1 ATOM 199 C C . ALA A 1 36 ? 10.867 13.757 8.516 1.00 38.64 ? 36 ALA A C 1 ATOM 200 O O . ALA A 1 36 ? 10.577 14.246 9.607 1.00 37.13 ? 36 ALA A O 1 ATOM 201 C CB . ALA A 1 36 ? 13.102 13.115 7.593 1.00 37.46 ? 36 ALA A CB 1 ATOM 202 N N . ALA A 1 37 ? 10.169 12.781 7.948 1.00 42.60 ? 37 ALA A N 1 ATOM 203 C CA . ALA A 1 37 ? 8.974 12.218 8.564 1.00 47.67 ? 37 ALA A CA 1 ATOM 204 C C . ALA A 1 37 ? 9.209 11.654 9.964 1.00 49.32 ? 37 ALA A C 1 ATOM 205 O O . ALA A 1 37 ? 8.269 11.532 10.747 1.00 50.73 ? 37 ALA A O 1 ATOM 206 C CB . ALA A 1 37 ? 8.395 11.134 7.662 1.00 48.77 ? 37 ALA A CB 1 ATOM 207 N N . ASP A 1 38 ? 10.456 11.318 10.278 1.00 52.18 ? 38 ASP A N 1 ATOM 208 C CA . ASP A 1 38 ? 10.784 10.753 11.585 1.00 53.99 ? 38 ASP A CA 1 ATOM 209 C C . ASP A 1 38 ? 11.511 11.722 12.517 1.00 54.31 ? 38 ASP A C 1 ATOM 210 O O . ASP A 1 38 ? 12.339 11.308 13.332 1.00 55.79 ? 38 ASP A O 1 ATOM 211 C CB . ASP A 1 38 ? 11.626 9.486 11.404 1.00 55.79 ? 38 ASP A CB 1 ATOM 212 C CG . ASP A 1 38 ? 12.972 9.767 10.764 1.00 59.19 ? 38 ASP A CG 1 ATOM 213 O OD1 . ASP A 1 38 ? 13.002 10.439 9.711 1.00 58.53 ? 38 ASP A OD1 1 ATOM 214 O OD2 . ASP A 1 38 ? 13.999 9.308 11.311 1.00 60.53 ? 38 ASP A OD2 1 ATOM 215 N N . ASP A 1 39 ? 11.201 13.010 12.397 1.00 53.36 ? 39 ASP A N 1 ATOM 216 C CA . ASP A 1 39 ? 11.818 14.035 13.237 1.00 52.29 ? 39 ASP A CA 1 ATOM 217 C C . ASP A 1 39 ? 13.336 14.104 13.108 1.00 49.77 ? 39 ASP A C 1 ATOM 218 O O . ASP A 1 39 ? 14.012 14.654 13.978 1.00 50.13 ? 39 ASP A O 1 ATOM 219 C CB . ASP A 1 39 ? 11.452 13.805 14.704 1.00 55.75 ? 39 ASP A CB 1 ATOM 220 C CG . ASP A 1 39 ? 9.969 13.948 14.962 1.00 59.12 ? 39 ASP A CG 1 ATOM 221 O OD1 . ASP A 1 39 ? 9.432 15.052 14.728 1.00 60.53 ? 39 ASP A OD1 1 ATOM 222 O OD2 . ASP A 1 39 ? 9.340 12.958 15.397 1.00 61.26 ? 39 ASP A OD2 1 ATOM 223 N N . THR A 1 40 ? 13.869 13.547 12.026 1.00 45.31 ? 40 THR A N 1 ATOM 224 C CA . THR A 1 40 ? 15.309 13.560 11.792 1.00 42.69 ? 40 THR A CA 1 ATOM 225 C C . THR A 1 40 ? 15.669 14.626 10.761 1.00 38.33 ? 40 THR A C 1 ATOM 226 O O . THR A 1 40 ? 14.886 14.912 9.855 1.00 37.93 ? 40 THR A O 1 ATOM 227 C CB . THR A 1 40 ? 15.803 12.189 11.271 1.00 42.44 ? 40 THR A CB 1 ATOM 228 O OG1 . THR A 1 40 ? 15.583 11.189 12.274 1.00 47.02 ? 40 THR A OG1 1 ATOM 229 C CG2 . THR A 1 40 ? 17.288 12.242 10.939 1.00 44.60 ? 40 THR A CG2 1 ATOM 230 N N . TRP A 1 41 ? 16.851 15.216 10.906 1.00 34.17 ? 41 TRP A N 1 ATOM 231 C CA . TRP A 1 41 ? 17.308 16.235 9.968 1.00 33.08 ? 41 TRP A CA 1 ATOM 232 C C . TRP A 1 41 ? 18.061 15.578 8.818 1.00 33.31 ? 41 TRP A C 1 ATOM 233 O O . TRP A 1 41 ? 19.137 15.016 9.022 1.00 36.64 ? 41 TRP A O 1 ATOM 234 C CB . TRP A 1 41 ? 18.247 17.230 10.657 1.00 30.49 ? 41 TRP A CB 1 ATOM 235 C CG . TRP A 1 41 ? 17.582 18.159 11.606 1.00 30.57 ? 41 TRP A CG 1 ATOM 236 C CD1 . TRP A 1 41 ? 17.760 18.219 12.961 1.00 32.32 ? 41 TRP A CD1 1 ATOM 237 C CD2 . TRP A 1 41 ? 16.641 19.189 11.279 1.00 30.60 ? 41 TRP A CD2 1 ATOM 238 N NE1 . TRP A 1 41 ? 16.989 19.226 13.495 1.00 32.17 ? 41 TRP A NE1 1 ATOM 239 C CE2 . TRP A 1 41 ? 16.292 19.836 12.485 1.00 30.89 ? 41 TRP A CE2 1 ATOM 240 C CE3 . TRP A 1 41 ? 16.060 19.629 10.081 1.00 27.62 ? 41 TRP A CE3 1 ATOM 241 C CZ2 . TRP A 1 41 ? 15.386 20.899 12.529 1.00 30.63 ? 41 TRP A CZ2 1 ATOM 242 C CZ3 . TRP A 1 41 ? 15.160 20.687 10.126 1.00 27.39 ? 41 TRP A CZ3 1 ATOM 243 C CH2 . TRP A 1 41 ? 14.833 21.309 11.342 1.00 29.46 ? 41 TRP A CH2 1 ATOM 244 N N . GLU A 1 42 ? 17.504 15.631 7.615 1.00 32.39 ? 42 GLU A N 1 ATOM 245 C CA . GLU A 1 42 ? 18.195 15.045 6.477 1.00 32.45 ? 42 GLU A CA 1 ATOM 246 C C . GLU A 1 42 ? 18.792 16.146 5.610 1.00 30.41 ? 42 GLU A C 1 ATOM 247 O O . GLU A 1 42 ? 18.196 17.209 5.453 1.00 26.87 ? 42 GLU A O 1 ATOM 248 C CB . GLU A 1 42 ? 17.252 14.173 5.650 1.00 36.77 ? 42 GLU A CB 1 ATOM 249 C CG . GLU A 1 42 ? 16.050 14.880 5.085 1.00 43.76 ? 42 GLU A CG 1 ATOM 250 C CD . GLU A 1 42 ? 15.186 13.947 4.253 1.00 47.76 ? 42 GLU A CD 1 ATOM 251 O OE1 . GLU A 1 42 ? 14.731 12.916 4.793 1.00 49.75 ? 42 GLU A OE1 1 ATOM 252 O OE2 . GLU A 1 42 ? 14.964 14.241 3.060 1.00 48.76 ? 42 GLU A OE2 1 ATOM 253 N N . PRO A 1 43 ? 19.991 15.907 5.055 1.00 27.09 ? 43 PRO A N 1 ATOM 254 C CA . PRO A 1 43 ? 20.683 16.873 4.200 1.00 26.15 ? 43 PRO A CA 1 ATOM 255 C C . PRO A 1 43 ? 19.790 17.319 3.051 1.00 27.55 ? 43 PRO A C 1 ATOM 256 O O . PRO A 1 43 ? 19.135 16.499 2.403 1.00 27.52 ? 43 PRO A O 1 ATOM 257 C CB . PRO A 1 43 ? 21.903 16.092 3.716 1.00 28.70 ? 43 PRO A CB 1 ATOM 258 C CG . PRO A 1 43 ? 22.197 15.190 4.873 1.00 29.03 ? 43 PRO A CG 1 ATOM 259 C CD . PRO A 1 43 ? 20.814 14.699 5.250 1.00 29.93 ? 43 PRO A CD 1 ATOM 260 N N . PHE A 1 44 ? 19.764 18.621 2.801 1.00 22.16 ? 44 PHE A N 1 ATOM 261 C CA . PHE A 1 44 ? 18.940 19.166 1.736 1.00 22.82 ? 44 PHE A CA 1 ATOM 262 C C . PHE A 1 44 ? 19.791 19.848 0.669 1.00 22.49 ? 44 PHE A C 1 ATOM 263 O O . PHE A 1 44 ? 19.586 19.644 -0.529 1.00 21.69 ? 44 PHE A O 1 ATOM 264 C CB . PHE A 1 44 ? 17.936 20.159 2.324 1.00 22.82 ? 44 PHE A CB 1 ATOM 265 C CG . PHE A 1 44 ? 16.981 20.718 1.319 1.00 23.83 ? 44 PHE A CG 1 ATOM 266 C CD1 . PHE A 1 44 ? 15.967 19.926 0.786 1.00 24.56 ? 44 PHE A CD1 1 ATOM 267 C CD2 . PHE A 1 44 ? 17.109 22.028 0.880 1.00 23.05 ? 44 PHE A CD2 1 ATOM 268 C CE1 . PHE A 1 44 ? 15.094 20.436 -0.175 1.00 22.78 ? 44 PHE A CE1 1 ATOM 269 C CE2 . PHE A 1 44 ? 16.245 22.542 -0.077 1.00 24.09 ? 44 PHE A CE2 1 ATOM 270 C CZ . PHE A 1 44 ? 15.235 21.741 -0.605 1.00 26.22 ? 44 PHE A CZ 1 ATOM 271 N N . ALA A 1 45 ? 20.754 20.652 1.113 1.00 19.72 ? 45 ALA A N 1 ATOM 272 C CA . ALA A 1 45 ? 21.637 21.370 0.201 1.00 20.28 ? 45 ALA A CA 1 ATOM 273 C C . ALA A 1 45 ? 22.756 22.010 1.004 1.00 19.39 ? 45 ALA A C 1 ATOM 274 O O . ALA A 1 45 ? 22.647 22.161 2.223 1.00 19.64 ? 45 ALA A O 1 ATOM 275 C CB . ALA A 1 45 ? 20.857 22.447 -0.546 1.00 21.13 ? 45 ALA A CB 1 ATOM 276 N N . SER A 1 46 ? 23.831 22.389 0.324 1.00 18.26 ? 46 SER A N 1 ATOM 277 C CA . SER A 1 46 ? 24.950 23.034 1.000 1.00 19.25 ? 46 SER A CA 1 ATOM 278 C C . SER A 1 46 ? 25.782 23.810 -0.002 1.00 18.68 ? 46 SER A C 1 ATOM 279 O O . SER A 1 46 ? 25.642 23.627 -1.210 1.00 17.39 ? 46 SER A O 1 ATOM 280 C CB . SER A 1 46 ? 25.828 22.002 1.721 1.00 15.43 ? 46 SER A CB 1 ATOM 281 O OG . SER A 1 46 ? 26.467 21.110 0.813 1.00 17.13 ? 46 SER A OG 1 ATOM 282 N N . GLY A 1 47 ? 26.642 24.683 0.508 1.00 20.48 ? 47 GLY A N 1 ATOM 283 C CA . GLY A 1 47 ? 27.493 25.475 -0.359 1.00 19.42 ? 47 GLY A CA 1 ATOM 284 C C . GLY A 1 47 ? 28.335 26.419 0.473 1.00 20.33 ? 47 GLY A C 1 ATOM 285 O O . GLY A 1 47 ? 28.329 26.338 1.704 1.00 19.52 ? 47 GLY A O 1 ATOM 286 N N . LYS A 1 48 ? 29.064 27.303 -0.201 1.00 19.04 ? 48 LYS A N 1 ATOM 287 C CA . LYS A 1 48 ? 29.910 28.285 0.465 1.00 20.60 ? 48 LYS A CA 1 ATOM 288 C C . LYS A 1 48 ? 29.561 29.664 -0.077 1.00 18.95 ? 48 LYS A C 1 ATOM 289 O O . LYS A 1 48 ? 29.232 29.808 -1.255 1.00 16.66 ? 48 LYS A O 1 ATOM 290 C CB . LYS A 1 48 ? 31.394 27.982 0.208 1.00 25.87 ? 48 LYS A CB 1 ATOM 291 C CG . LYS A 1 48 ? 31.961 26.859 1.071 1.00 32.38 ? 48 LYS A CG 1 ATOM 292 C CD . LYS A 1 48 ? 33.425 26.581 0.745 1.00 37.68 ? 48 LYS A CD 1 ATOM 293 C CE . LYS A 1 48 ? 34.063 25.679 1.796 1.00 38.46 ? 48 LYS A CE 1 ATOM 294 N NZ . LYS A 1 48 ? 34.129 26.363 3.122 1.00 42.05 ? 48 LYS A NZ 1 ATOM 295 N N . THR A 1 49 ? 29.617 30.680 0.779 1.00 17.47 ? 49 THR A N 1 ATOM 296 C CA . THR A 1 49 ? 29.304 32.034 0.336 1.00 18.42 ? 49 THR A CA 1 ATOM 297 C C . THR A 1 49 ? 30.347 32.541 -0.657 1.00 21.39 ? 49 THR A C 1 ATOM 298 O O . THR A 1 49 ? 31.532 32.212 -0.567 1.00 20.54 ? 49 THR A O 1 ATOM 299 C CB . THR A 1 49 ? 29.228 33.026 1.522 1.00 14.91 ? 49 THR A CB 1 ATOM 300 O OG1 . THR A 1 49 ? 30.467 33.013 2.244 1.00 16.71 ? 49 THR A OG1 1 ATOM 301 C CG2 . THR A 1 49 ? 28.096 32.634 2.460 1.00 17.15 ? 49 THR A CG2 1 ATOM 302 N N . SER A 1 50 ? 29.890 33.353 -1.602 1.00 21.02 ? 50 SER A N 1 ATOM 303 C CA . SER A 1 50 ? 30.761 33.912 -2.626 1.00 24.13 ? 50 SER A CA 1 ATOM 304 C C . SER A 1 50 ? 31.501 35.127 -2.084 1.00 24.77 ? 50 SER A C 1 ATOM 305 O O . SER A 1 50 ? 31.411 35.448 -0.897 1.00 20.93 ? 50 SER A O 1 ATOM 306 C CB . SER A 1 50 ? 29.929 34.343 -3.828 1.00 24.75 ? 50 SER A CB 1 ATOM 307 O OG . SER A 1 50 ? 29.089 35.423 -3.460 1.00 28.56 ? 50 SER A OG 1 ATOM 308 N N . GLU A 1 51 ? 32.216 35.809 -2.976 1.00 25.05 ? 51 GLU A N 1 ATOM 309 C CA . GLU A 1 51 ? 32.970 37.000 -2.611 1.00 26.03 ? 51 GLU A CA 1 ATOM 310 C C . GLU A 1 51 ? 32.046 38.130 -2.165 1.00 24.32 ? 51 GLU A C 1 ATOM 311 O O . GLU A 1 51 ? 32.490 39.095 -1.541 1.00 23.81 ? 51 GLU A O 1 ATOM 312 C CB . GLU A 1 51 ? 33.836 37.457 -3.789 1.00 30.37 ? 51 GLU A CB 1 ATOM 313 C CG . GLU A 1 51 ? 34.983 36.502 -4.085 1.00 39.50 ? 51 GLU A CG 1 ATOM 314 C CD . GLU A 1 51 ? 35.828 36.939 -5.265 1.00 45.14 ? 51 GLU A CD 1 ATOM 315 O OE1 . GLU A 1 51 ? 36.800 36.223 -5.589 1.00 48.51 ? 51 GLU A OE1 1 ATOM 316 O OE2 . GLU A 1 51 ? 35.524 37.993 -5.867 1.00 47.88 ? 51 GLU A OE2 1 ATOM 317 N N . SER A 1 52 ? 30.763 38.011 -2.485 1.00 22.14 ? 52 SER A N 1 ATOM 318 C CA . SER A 1 52 ? 29.790 39.023 -2.086 1.00 24.49 ? 52 SER A CA 1 ATOM 319 C C . SER A 1 52 ? 29.092 38.584 -0.795 1.00 22.52 ? 52 SER A C 1 ATOM 320 O O . SER A 1 52 ? 28.163 39.248 -0.314 1.00 17.82 ? 52 SER A O 1 ATOM 321 C CB . SER A 1 52 ? 28.749 39.228 -3.191 1.00 28.14 ? 52 SER A CB 1 ATOM 322 O OG . SER A 1 52 ? 28.007 38.040 -3.414 1.00 33.88 ? 52 SER A OG 1 ATOM 323 N N . GLY A 1 53 ? 29.547 37.461 -0.247 1.00 19.89 ? 53 GLY A N 1 ATOM 324 C CA . GLY A 1 53 ? 28.976 36.932 0.979 1.00 18.44 ? 53 GLY A CA 1 ATOM 325 C C . GLY A 1 53 ? 27.613 36.300 0.775 1.00 20.30 ? 53 GLY A C 1 ATOM 326 O O . GLY A 1 53 ? 26.866 36.097 1.733 1.00 20.03 ? 53 GLY A O 1 ATOM 327 N N . GLU A 1 54 ? 27.292 35.973 -0.471 1.00 21.73 ? 54 GLU A N 1 ATOM 328 C CA . GLU A 1 54 ? 26.001 35.376 -0.789 1.00 22.13 ? 54 GLU A CA 1 ATOM 329 C C . GLU A 1 54 ? 26.102 33.948 -1.282 1.00 20.95 ? 54 GLU A C 1 ATOM 330 O O . GLU A 1 54 ? 27.130 33.519 -1.800 1.00 20.69 ? 54 GLU A O 1 ATOM 331 C CB . GLU A 1 54 ? 25.291 36.201 -1.860 1.00 24.11 ? 54 GLU A CB 1 ATOM 332 C CG . GLU A 1 54 ? 25.268 37.690 -1.592 1.00 32.60 ? 54 GLU A CG 1 ATOM 333 C CD . GLU A 1 54 ? 24.564 38.460 -2.690 1.00 37.51 ? 54 GLU A CD 1 ATOM 334 O OE1 . GLU A 1 54 ? 24.881 38.230 -3.877 1.00 41.75 ? 54 GLU A OE1 1 ATOM 335 O OE2 . GLU A 1 54 ? 23.699 39.298 -2.369 1.00 40.34 ? 54 GLU A OE2 1 ATOM 336 N N . LEU A 1 55 ? 25.008 33.217 -1.118 1.00 18.21 ? 55 LEU A N 1 ATOM 337 C CA . LEU A 1 55 ? 24.930 31.843 -1.563 1.00 20.14 ? 55 LEU A CA 1 ATOM 338 C C . LEU A 1 55 ? 23.587 31.700 -2.255 1.00 21.48 ? 55 LEU A C 1 ATOM 339 O O . LEU A 1 55 ? 22.542 31.834 -1.621 1.00 20.74 ? 55 LEU A O 1 ATOM 340 C CB . LEU A 1 55 ? 25.033 30.886 -0.372 1.00 21.68 ? 55 LEU A CB 1 ATOM 341 C CG . LEU A 1 55 ? 24.903 29.390 -0.670 1.00 23.69 ? 55 LEU A CG 1 ATOM 342 C CD1 . LEU A 1 55 ? 25.888 28.974 -1.766 1.00 24.96 ? 55 LEU A CD1 1 ATOM 343 C CD2 . LEU A 1 55 ? 25.164 28.609 0.613 1.00 25.35 ? 55 LEU A CD2 1 ATOM 344 N N . HIS A 1 56 ? 23.629 31.469 -3.562 1.00 24.44 ? 56 HIS A N 1 ATOM 345 C CA . HIS A 1 56 ? 22.421 31.299 -4.366 1.00 29.23 ? 56 HIS A CA 1 ATOM 346 C C . HIS A 1 56 ? 22.426 29.907 -4.982 1.00 28.39 ? 56 HIS A C 1 ATOM 347 O O . HIS A 1 56 ? 23.430 29.200 -4.927 1.00 27.82 ? 56 HIS A O 1 ATOM 348 C CB . HIS A 1 56 ? 22.375 32.314 -5.515 1.00 32.37 ? 56 HIS A CB 1 ATOM 349 C CG . HIS A 1 56 ? 22.511 33.739 -5.084 1.00 37.85 ? 56 HIS A CG 1 ATOM 350 N ND1 . HIS A 1 56 ? 23.702 34.273 -4.643 1.00 39.40 ? 56 HIS A ND1 1 ATOM 351 C CD2 . HIS A 1 56 ? 21.609 34.749 -5.051 1.00 39.56 ? 56 HIS A CD2 1 ATOM 352 C CE1 . HIS A 1 56 ? 23.529 35.552 -4.359 1.00 39.34 ? 56 HIS A CE1 1 ATOM 353 N NE2 . HIS A 1 56 ? 22.269 35.866 -4.598 1.00 40.87 ? 56 HIS A NE2 1 ATOM 354 N N . GLY A 1 57 ? 21.300 29.530 -5.579 1.00 29.97 ? 57 GLY A N 1 ATOM 355 C CA . GLY A 1 57 ? 21.197 28.236 -6.231 1.00 29.95 ? 57 GLY A CA 1 ATOM 356 C C . GLY A 1 57 ? 21.226 27.033 -5.312 1.00 29.86 ? 57 GLY A C 1 ATOM 357 O O . GLY A 1 57 ? 21.717 25.970 -5.696 1.00 29.18 ? 57 GLY A O 1 ATOM 358 N N . LEU A 1 58 ? 20.708 27.184 -4.097 1.00 27.64 ? 58 LEU A N 1 ATOM 359 C CA . LEU A 1 58 ? 20.687 26.067 -3.165 1.00 26.52 ? 58 LEU A CA 1 ATOM 360 C C . LEU A 1 58 ? 19.619 25.059 -3.554 1.00 25.97 ? 58 LEU A C 1 ATOM 361 O O . LEU A 1 58 ? 19.806 23.856 -3.394 1.00 26.16 ? 58 LEU A O 1 ATOM 362 C CB . LEU A 1 58 ? 20.421 26.549 -1.737 1.00 26.32 ? 58 LEU A CB 1 ATOM 363 C CG . LEU A 1 58 ? 21.617 27.176 -1.015 1.00 26.64 ? 58 LEU A CG 1 ATOM 364 C CD1 . LEU A 1 58 ? 21.174 27.766 0.315 1.00 24.99 ? 58 LEU A CD1 1 ATOM 365 C CD2 . LEU A 1 58 ? 22.691 26.115 -0.805 1.00 25.72 ? 58 LEU A CD2 1 ATOM 366 N N . THR A 1 59 ? 18.502 25.553 -4.075 1.00 25.99 ? 59 THR A N 1 ATOM 367 C CA . THR A 1 59 ? 17.404 24.678 -4.454 1.00 25.73 ? 59 THR A CA 1 ATOM 368 C C . THR A 1 59 ? 16.550 25.323 -5.539 1.00 25.30 ? 59 THR A C 1 ATOM 369 O O . THR A 1 59 ? 16.865 26.410 -6.025 1.00 23.67 ? 59 THR A O 1 ATOM 370 C CB . THR A 1 59 ? 16.525 24.367 -3.219 1.00 26.29 ? 59 THR A CB 1 ATOM 371 O OG1 . THR A 1 59 ? 15.519 23.412 -3.565 1.00 26.37 ? 59 THR A OG1 1 ATOM 372 C CG2 . THR A 1 59 ? 15.854 25.643 -2.705 1.00 26.65 ? 59 THR A CG2 1 ATOM 373 N N . THR A 1 60 ? 15.481 24.638 -5.929 1.00 24.29 ? 60 THR A N 1 ATOM 374 C CA . THR A 1 60 ? 14.561 25.143 -6.943 1.00 27.76 ? 60 THR A CA 1 ATOM 375 C C . THR A 1 60 ? 13.170 25.184 -6.331 1.00 27.18 ? 60 THR A C 1 ATOM 376 O O . THR A 1 60 ? 12.938 24.593 -5.276 1.00 27.04 ? 60 THR A O 1 ATOM 377 C CB . THR A 1 60 ? 14.519 24.224 -8.180 1.00 27.79 ? 60 THR A CB 1 ATOM 378 O OG1 . THR A 1 60 ? 14.127 22.904 -7.778 1.00 26.01 ? 60 THR A OG1 1 ATOM 379 C CG2 . THR A 1 60 ? 15.880 24.171 -8.853 1.00 30.43 ? 60 THR A CG2 1 ATOM 380 N N . GLU A 1 61 ? 12.244 25.873 -6.986 1.00 28.40 ? 61 GLU A N 1 ATOM 381 C CA . GLU A 1 61 ? 10.888 25.962 -6.463 1.00 32.27 ? 61 GLU A CA 1 ATOM 382 C C . GLU A 1 61 ? 10.231 24.587 -6.360 1.00 31.52 ? 61 GLU A C 1 ATOM 383 O O . GLU A 1 61 ? 9.493 24.320 -5.417 1.00 32.95 ? 61 GLU A O 1 ATOM 384 C CB . GLU A 1 61 ? 10.034 26.891 -7.334 1.00 36.31 ? 61 GLU A CB 1 ATOM 385 C CG . GLU A 1 61 ? 10.000 26.524 -8.805 1.00 48.38 ? 61 GLU A CG 1 ATOM 386 C CD . GLU A 1 61 ? 9.066 27.416 -9.603 1.00 53.21 ? 61 GLU A CD 1 ATOM 387 O OE1 . GLU A 1 61 ? 9.215 28.657 -9.527 1.00 55.47 ? 61 GLU A OE1 1 ATOM 388 O OE2 . GLU A 1 61 ? 8.184 26.875 -10.308 1.00 56.77 ? 61 GLU A OE2 1 ATOM 389 N N . GLU A 1 62 ? 10.514 23.712 -7.322 1.00 29.71 ? 62 GLU A N 1 ATOM 390 C CA . GLU A 1 62 ? 9.929 22.370 -7.324 1.00 28.62 ? 62 GLU A CA 1 ATOM 391 C C . GLU A 1 62 ? 10.389 21.509 -6.150 1.00 27.06 ? 62 GLU A C 1 ATOM 392 O O . GLU A 1 62 ? 9.603 20.772 -5.560 1.00 26.32 ? 62 GLU A O 1 ATOM 393 C CB . GLU A 1 62 ? 10.259 21.654 -8.638 1.00 33.45 ? 62 GLU A CB 1 ATOM 394 C CG . GLU A 1 62 ? 9.618 22.278 -9.870 0.50 36.58 ? 62 GLU A CG 1 ATOM 395 C CD . GLU A 1 62 ? 8.101 22.184 -9.856 0.50 39.70 ? 62 GLU A CD 1 ATOM 396 O OE1 . GLU A 1 62 ? 7.573 21.051 -9.812 0.50 38.69 ? 62 GLU A OE1 1 ATOM 397 O OE2 . GLU A 1 62 ? 7.437 23.243 -9.889 0.50 41.34 ? 62 GLU A OE2 1 ATOM 398 N N . GLN A 1 63 ? 11.668 21.605 -5.812 1.00 24.12 ? 63 GLN A N 1 ATOM 399 C CA . GLN A 1 63 ? 12.231 20.825 -4.718 1.00 24.96 ? 63 GLN A CA 1 ATOM 400 C C . GLN A 1 63 ? 11.972 21.398 -3.327 1.00 20.88 ? 63 GLN A C 1 ATOM 401 O O . GLN A 1 63 ? 11.908 20.651 -2.352 1.00 20.71 ? 63 GLN A O 1 ATOM 402 C CB . GLN A 1 63 ? 13.739 20.676 -4.930 1.00 29.62 ? 63 GLN A CB 1 ATOM 403 C CG . GLN A 1 63 ? 14.513 20.202 -3.712 1.00 37.17 ? 63 GLN A CG 1 ATOM 404 C CD . GLN A 1 63 ? 16.011 20.122 -3.974 1.00 41.81 ? 63 GLN A CD 1 ATOM 405 O OE1 . GLN A 1 63 ? 16.486 19.212 -4.658 1.00 43.61 ? 63 GLN A OE1 1 ATOM 406 N NE2 . GLN A 1 63 ? 16.759 21.083 -3.442 1.00 41.04 ? 63 GLN A NE2 1 ATOM 407 N N . PHE A 1 64 ? 11.829 22.718 -3.248 1.00 21.22 ? 64 PHE A N 1 ATOM 408 C CA . PHE A 1 64 ? 11.618 23.428 -1.984 1.00 21.47 ? 64 PHE A CA 1 ATOM 409 C C . PHE A 1 64 ? 10.158 23.380 -1.522 1.00 21.28 ? 64 PHE A C 1 ATOM 410 O O . PHE A 1 64 ? 9.453 24.387 -1.548 1.00 21.93 ? 64 PHE A O 1 ATOM 411 C CB . PHE A 1 64 ? 12.077 24.880 -2.156 1.00 21.37 ? 64 PHE A CB 1 ATOM 412 C CG . PHE A 1 64 ? 12.247 25.640 -0.862 1.00 23.04 ? 64 PHE A CG 1 ATOM 413 C CD1 . PHE A 1 64 ? 12.921 25.074 0.214 1.00 23.38 ? 64 PHE A CD1 1 ATOM 414 C CD2 . PHE A 1 64 ? 11.790 26.953 -0.749 1.00 25.84 ? 64 PHE A CD2 1 ATOM 415 C CE1 . PHE A 1 64 ? 13.143 25.804 1.392 1.00 24.09 ? 64 PHE A CE1 1 ATOM 416 C CE2 . PHE A 1 64 ? 12.009 27.692 0.424 1.00 22.78 ? 64 PHE A CE2 1 ATOM 417 C CZ . PHE A 1 64 ? 12.686 27.114 1.491 1.00 24.59 ? 64 PHE A CZ 1 ATOM 418 N N . VAL A 1 65 ? 9.717 22.206 -1.086 1.00 21.64 ? 65 VAL A N 1 ATOM 419 C CA . VAL A 1 65 ? 8.338 22.026 -0.638 1.00 21.96 ? 65 VAL A CA 1 ATOM 420 C C . VAL A 1 65 ? 8.137 22.448 0.811 1.00 21.91 ? 65 VAL A C 1 ATOM 421 O O . VAL A 1 65 ? 9.102 22.752 1.521 1.00 20.30 ? 65 VAL A O 1 ATOM 422 C CB . VAL A 1 65 ? 7.893 20.556 -0.782 1.00 20.36 ? 65 VAL A CB 1 ATOM 423 C CG1 . VAL A 1 65 ? 7.916 20.147 -2.245 1.00 21.97 ? 65 VAL A CG1 1 ATOM 424 C CG2 . VAL A 1 65 ? 8.806 19.651 0.036 1.00 20.24 ? 65 VAL A CG2 1 ATOM 425 N N . GLU A 1 66 ? 6.881 22.454 1.247 1.00 21.69 ? 66 GLU A N 1 ATOM 426 C CA . GLU A 1 66 ? 6.562 22.839 2.619 1.00 25.13 ? 66 GLU A CA 1 ATOM 427 C C . GLU A 1 66 ? 7.321 21.948 3.582 1.00 24.26 ? 66 GLU A C 1 ATOM 428 O O . GLU A 1 66 ? 7.549 20.769 3.306 1.00 23.92 ? 66 GLU A O 1 ATOM 429 C CB . GLU A 1 66 ? 5.060 22.703 2.894 1.00 27.66 ? 66 GLU A CB 1 ATOM 430 C CG . GLU A 1 66 ? 4.188 23.652 2.101 1.00 35.32 ? 66 GLU A CG 1 ATOM 431 C CD . GLU A 1 66 ? 2.721 23.558 2.491 1.00 39.17 ? 66 GLU A CD 1 ATOM 432 O OE1 . GLU A 1 66 ? 2.144 22.458 2.360 1.00 37.13 ? 66 GLU A OE1 1 ATOM 433 O OE2 . GLU A 1 66 ? 2.147 24.582 2.926 1.00 44.96 ? 66 GLU A OE2 1 ATOM 434 N N . GLY A 1 67 ? 7.710 22.509 4.717 1.00 22.42 ? 67 GLY A N 1 ATOM 435 C CA . GLY A 1 67 ? 8.427 21.721 5.695 1.00 21.96 ? 67 GLY A CA 1 ATOM 436 C C . GLY A 1 67 ? 9.191 22.601 6.649 1.00 19.76 ? 67 GLY A C 1 ATOM 437 O O . GLY A 1 67 ? 9.119 23.826 6.565 1.00 19.56 ? 67 GLY A O 1 ATOM 438 N N . ILE A 1 68 ? 9.906 21.971 7.572 1.00 18.87 ? 68 ILE A N 1 ATOM 439 C CA . ILE A 1 68 ? 10.713 22.699 8.541 1.00 19.61 ? 68 ILE A CA 1 ATOM 440 C C . ILE A 1 68 ? 12.143 22.553 8.064 1.00 20.12 ? 68 ILE A C 1 ATOM 441 O O . ILE A 1 68 ? 12.624 21.441 7.849 1.00 20.48 ? 68 ILE A O 1 ATOM 442 C CB . ILE A 1 68 ? 10.575 22.107 9.956 1.00 22.68 ? 68 ILE A CB 1 ATOM 443 C CG1 . ILE A 1 68 ? 9.113 22.202 10.410 1.00 25.07 ? 68 ILE A CG1 1 ATOM 444 C CG2 . ILE A 1 68 ? 11.490 22.861 10.927 1.00 21.19 ? 68 ILE A CG2 1 ATOM 445 C CD1 . ILE A 1 68 ? 8.850 21.621 11.788 1.00 29.40 ? 68 ILE A CD1 1 ATOM 446 N N . TYR A 1 69 ? 12.813 23.682 7.878 1.00 15.16 ? 69 TYR A N 1 ATOM 447 C CA . TYR A 1 69 ? 14.184 23.681 7.400 1.00 14.62 ? 69 TYR A CA 1 ATOM 448 C C . TYR A 1 69 ? 15.149 24.265 8.410 1.00 15.91 ? 69 TYR A C 1 ATOM 449 O O . TYR A 1 69 ? 14.786 25.111 9.230 1.00 15.25 ? 69 TYR A O 1 ATOM 450 C CB . TYR A 1 69 ? 14.297 24.484 6.098 1.00 14.95 ? 69 TYR A CB 1 ATOM 451 C CG . TYR A 1 69 ? 13.569 23.855 4.931 1.00 17.29 ? 69 TYR A CG 1 ATOM 452 C CD1 . TYR A 1 69 ? 12.186 23.968 4.801 1.00 17.38 ? 69 TYR A CD1 1 ATOM 453 C CD2 . TYR A 1 69 ? 14.263 23.114 3.977 1.00 16.16 ? 69 TYR A CD2 1 ATOM 454 C CE1 . TYR A 1 69 ? 11.506 23.357 3.741 1.00 18.74 ? 69 TYR A CE1 1 ATOM 455 C CE2 . TYR A 1 69 ? 13.594 22.494 2.913 1.00 17.24 ? 69 TYR A CE2 1 ATOM 456 C CZ . TYR A 1 69 ? 12.220 22.622 2.805 1.00 20.19 ? 69 TYR A CZ 1 ATOM 457 O OH . TYR A 1 69 ? 11.572 22.018 1.751 1.00 19.82 ? 69 TYR A OH 1 ATOM 458 N N . LYS A 1 70 ? 16.389 23.803 8.340 1.00 16.60 ? 70 LYS A N 1 ATOM 459 C CA . LYS A 1 70 ? 17.422 24.306 9.222 1.00 17.78 ? 70 LYS A CA 1 ATOM 460 C C . LYS A 1 70 ? 18.600 24.743 8.381 1.00 17.25 ? 70 LYS A C 1 ATOM 461 O O . LYS A 1 70 ? 19.130 23.961 7.596 1.00 18.11 ? 70 LYS A O 1 ATOM 462 C CB . LYS A 1 70 ? 17.882 23.236 10.215 1.00 19.65 ? 70 LYS A CB 1 ATOM 463 C CG . LYS A 1 70 ? 19.095 23.689 11.029 1.00 22.98 ? 70 LYS A CG 1 ATOM 464 C CD . LYS A 1 70 ? 19.306 22.856 12.287 1.00 29.41 ? 70 LYS A CD 1 ATOM 465 C CE . LYS A 1 70 ? 19.712 21.429 11.978 1.00 32.21 ? 70 LYS A CE 1 ATOM 466 N NZ . LYS A 1 70 ? 20.020 20.694 13.244 1.00 35.99 ? 70 LYS A NZ 1 ATOM 467 N N . VAL A 1 71 ? 18.983 26.002 8.527 1.00 16.47 ? 71 VAL A N 1 ATOM 468 C CA . VAL A 1 71 ? 20.129 26.546 7.821 1.00 15.95 ? 71 VAL A CA 1 ATOM 469 C C . VAL A 1 71 ? 21.228 26.673 8.870 1.00 17.66 ? 71 VAL A C 1 ATOM 470 O O . VAL A 1 71 ? 21.087 27.411 9.849 1.00 17.09 ? 71 VAL A O 1 ATOM 471 C CB . VAL A 1 71 ? 19.822 27.929 7.221 1.00 15.98 ? 71 VAL A CB 1 ATOM 472 C CG1 . VAL A 1 71 ? 21.073 28.492 6.545 1.00 19.25 ? 71 VAL A CG1 1 ATOM 473 C CG2 . VAL A 1 71 ? 18.688 27.809 6.204 1.00 18.43 ? 71 VAL A CG2 1 ATOM 474 N N . GLU A 1 72 ? 22.303 25.920 8.678 1.00 15.52 ? 72 GLU A N 1 ATOM 475 C CA . GLU A 1 72 ? 23.425 25.936 9.604 1.00 19.85 ? 72 GLU A CA 1 ATOM 476 C C . GLU A 1 72 ? 24.589 26.672 8.952 1.00 18.61 ? 72 GLU A C 1 ATOM 477 O O . GLU A 1 72 ? 25.016 26.312 7.862 1.00 19.04 ? 72 GLU A O 1 ATOM 478 C CB . GLU A 1 72 ? 23.830 24.499 9.941 1.00 23.27 ? 72 GLU A CB 1 ATOM 479 C CG . GLU A 1 72 ? 25.082 24.372 10.778 1.00 31.76 ? 72 GLU A CG 1 ATOM 480 C CD . GLU A 1 72 ? 25.465 22.927 11.006 1.00 37.76 ? 72 GLU A CD 1 ATOM 481 O OE1 . GLU A 1 72 ? 24.663 22.196 11.621 1.00 37.67 ? 72 GLU A OE1 1 ATOM 482 O OE2 . GLU A 1 72 ? 26.562 22.525 10.563 1.00 42.53 ? 72 GLU A OE2 1 ATOM 483 N N . ILE A 1 73 ? 25.080 27.713 9.617 1.00 17.53 ? 73 ILE A N 1 ATOM 484 C CA . ILE A 1 73 ? 26.195 28.498 9.098 1.00 18.51 ? 73 ILE A CA 1 ATOM 485 C C . ILE A 1 73 ? 27.421 28.188 9.951 1.00 16.68 ? 73 ILE A C 1 ATOM 486 O O . ILE A 1 73 ? 27.394 28.395 11.162 1.00 16.97 ? 73 ILE A O 1 ATOM 487 C CB . ILE A 1 73 ? 25.869 30.009 9.157 1.00 19.63 ? 73 ILE A CB 1 ATOM 488 C CG1 . ILE A 1 73 ? 24.590 30.288 8.362 1.00 21.36 ? 73 ILE A CG1 1 ATOM 489 C CG2 . ILE A 1 73 ? 27.022 30.819 8.593 1.00 18.22 ? 73 ILE A CG2 1 ATOM 490 C CD1 . ILE A 1 73 ? 24.041 31.698 8.543 1.00 25.31 ? 73 ILE A CD1 1 ATOM 491 N N . ASP A 1 74 ? 28.482 27.677 9.323 1.00 16.56 ? 74 ASP A N 1 ATOM 492 C CA . ASP A 1 74 ? 29.702 27.325 10.053 1.00 19.52 ? 74 ASP A CA 1 ATOM 493 C C . ASP A 1 74 ? 30.536 28.556 10.372 1.00 17.55 ? 74 ASP A C 1 ATOM 494 O O . ASP A 1 74 ? 31.553 28.833 9.734 1.00 18.13 ? 74 ASP A O 1 ATOM 495 C CB . ASP A 1 74 ? 30.540 26.307 9.265 1.00 19.25 ? 74 ASP A CB 1 ATOM 496 C CG . ASP A 1 74 ? 31.814 25.897 10.007 1.00 30.31 ? 74 ASP A CG 1 ATOM 497 O OD1 . ASP A 1 74 ? 31.943 26.230 11.207 1.00 29.80 ? 74 ASP A OD1 1 ATOM 498 O OD2 . ASP A 1 74 ? 32.681 25.233 9.393 1.00 34.07 ? 74 ASP A OD2 1 ATOM 499 N N . THR A 1 75 ? 30.090 29.290 11.383 1.00 19.16 ? 75 THR A N 1 ATOM 500 C CA . THR A 1 75 ? 30.768 30.499 11.814 1.00 17.81 ? 75 THR A CA 1 ATOM 501 C C . THR A 1 75 ? 32.116 30.220 12.483 1.00 18.50 ? 75 THR A C 1 ATOM 502 O O . THR A 1 75 ? 33.063 30.983 12.309 1.00 19.00 ? 75 THR A O 1 ATOM 503 C CB . THR A 1 75 ? 29.874 31.289 12.794 1.00 17.11 ? 75 THR A CB 1 ATOM 504 O OG1 . THR A 1 75 ? 29.538 30.453 13.909 1.00 15.29 ? 75 THR A OG1 1 ATOM 505 C CG2 . THR A 1 75 ? 28.584 31.725 12.100 1.00 16.91 ? 75 THR A CG2 1 ATOM 506 N N . LYS A 1 76 ? 32.208 29.123 13.233 1.00 20.57 ? 76 LYS A N 1 ATOM 507 C CA . LYS A 1 76 ? 33.452 28.800 13.940 1.00 23.45 ? 76 LYS A CA 1 ATOM 508 C C . LYS A 1 76 ? 34.669 28.738 13.013 1.00 22.45 ? 76 LYS A C 1 ATOM 509 O O . LYS A 1 76 ? 35.688 29.378 13.273 1.00 22.26 ? 76 LYS A O 1 ATOM 510 C CB . LYS A 1 76 ? 33.306 27.476 14.696 1.00 25.75 ? 76 LYS A CB 1 ATOM 511 C CG . LYS A 1 76 ? 34.443 27.204 15.678 1.00 26.19 ? 76 LYS A CG 1 ATOM 512 C CD . LYS A 1 76 ? 34.184 25.960 16.513 1.00 29.85 ? 76 LYS A CD 1 ATOM 513 C CE . LYS A 1 76 ? 35.200 25.840 17.649 1.00 33.48 ? 76 LYS A CE 1 ATOM 514 N NZ . LYS A 1 76 ? 34.931 24.659 18.525 1.00 38.22 ? 76 LYS A NZ 1 ATOM 515 N N . SER A 1 77 ? 34.555 27.973 11.933 1.00 22.05 ? 77 SER A N 1 ATOM 516 C CA . SER A 1 77 ? 35.647 27.836 10.974 1.00 24.40 ? 77 SER A CA 1 ATOM 517 C C . SER A 1 77 ? 36.017 29.187 10.377 1.00 23.65 ? 77 SER A C 1 ATOM 518 O O . SER A 1 77 ? 37.187 29.460 10.108 1.00 23.26 ? 77 SER A O 1 ATOM 519 C CB . SER A 1 77 ? 35.248 26.870 9.858 1.00 24.76 ? 77 SER A CB 1 ATOM 520 O OG . SER A 1 77 ? 35.073 25.558 10.369 1.00 28.45 ? 77 SER A OG 1 ATOM 521 N N . TYR A 1 78 ? 35.011 30.032 10.172 1.00 23.14 ? 78 TYR A N 1 ATOM 522 C CA . TYR A 1 78 ? 35.232 31.359 9.612 1.00 23.59 ? 78 TYR A CA 1 ATOM 523 C C . TYR A 1 78 ? 36.163 32.189 10.497 1.00 23.33 ? 78 TYR A C 1 ATOM 524 O O . TYR A 1 78 ? 37.175 32.722 10.023 1.00 23.06 ? 78 TYR A O 1 ATOM 525 C CB . TYR A 1 78 ? 33.898 32.101 9.455 1.00 21.91 ? 78 TYR A CB 1 ATOM 526 C CG . TYR A 1 78 ? 34.049 33.501 8.890 1.00 19.90 ? 78 TYR A CG 1 ATOM 527 C CD1 . TYR A 1 78 ? 34.382 33.697 7.547 1.00 20.33 ? 78 TYR A CD1 1 ATOM 528 C CD2 . TYR A 1 78 ? 33.892 34.626 9.701 1.00 21.27 ? 78 TYR A CD2 1 ATOM 529 C CE1 . TYR A 1 78 ? 34.558 34.969 7.028 1.00 20.91 ? 78 TYR A CE1 1 ATOM 530 C CE2 . TYR A 1 78 ? 34.068 35.911 9.190 1.00 19.83 ? 78 TYR A CE2 1 ATOM 531 C CZ . TYR A 1 78 ? 34.401 36.072 7.851 1.00 18.89 ? 78 TYR A CZ 1 ATOM 532 O OH . TYR A 1 78 ? 34.578 37.329 7.322 1.00 21.46 ? 78 TYR A OH 1 ATOM 533 N N . TRP A 1 79 ? 35.820 32.300 11.779 1.00 21.01 ? 79 TRP A N 1 ATOM 534 C CA . TRP A 1 79 ? 36.623 33.080 12.715 1.00 22.98 ? 79 TRP A CA 1 ATOM 535 C C . TRP A 1 79 ? 37.993 32.475 12.982 1.00 23.50 ? 79 TRP A C 1 ATOM 536 O O . TRP A 1 79 ? 38.976 33.201 13.118 1.00 23.39 ? 79 TRP A O 1 ATOM 537 C CB . TRP A 1 79 ? 35.872 33.268 14.035 1.00 22.36 ? 79 TRP A CB 1 ATOM 538 C CG . TRP A 1 79 ? 34.658 34.118 13.873 1.00 22.63 ? 79 TRP A CG 1 ATOM 539 C CD1 . TRP A 1 79 ? 33.358 33.741 14.067 1.00 19.91 ? 79 TRP A CD1 1 ATOM 540 C CD2 . TRP A 1 79 ? 34.624 35.490 13.461 1.00 21.79 ? 79 TRP A CD2 1 ATOM 541 N NE1 . TRP A 1 79 ? 32.517 34.796 13.801 1.00 20.06 ? 79 TRP A NE1 1 ATOM 542 C CE2 . TRP A 1 79 ? 33.268 35.880 13.425 1.00 21.10 ? 79 TRP A CE2 1 ATOM 543 C CE3 . TRP A 1 79 ? 35.609 36.427 13.118 1.00 21.73 ? 79 TRP A CE3 1 ATOM 544 C CZ2 . TRP A 1 79 ? 32.868 37.170 13.057 1.00 20.21 ? 79 TRP A CZ2 1 ATOM 545 C CZ3 . TRP A 1 79 ? 35.212 37.713 12.751 1.00 23.33 ? 79 TRP A CZ3 1 ATOM 546 C CH2 . TRP A 1 79 ? 33.853 38.071 12.723 1.00 19.31 ? 79 TRP A CH2 1 ATOM 547 N N . LYS A 1 80 ? 38.057 31.151 13.064 1.00 26.11 ? 80 LYS A N 1 ATOM 548 C CA . LYS A 1 80 ? 39.327 30.467 13.300 1.00 31.26 ? 80 LYS A CA 1 ATOM 549 C C . LYS A 1 80 ? 40.312 30.823 12.185 1.00 31.04 ? 80 LYS A C 1 ATOM 550 O O . LYS A 1 80 ? 41.489 31.077 12.437 1.00 30.93 ? 80 LYS A O 1 ATOM 551 C CB . LYS A 1 80 ? 39.113 28.952 13.323 1.00 32.32 ? 80 LYS A CB 1 ATOM 552 C CG . LYS A 1 80 ? 38.167 28.471 14.413 1.00 37.89 ? 80 LYS A CG 1 ATOM 553 C CD . LYS A 1 80 ? 38.825 28.465 15.778 1.00 41.45 ? 80 LYS A CD 1 ATOM 554 C CE . LYS A 1 80 ? 39.882 27.377 15.863 1.00 45.64 ? 80 LYS A CE 1 ATOM 555 N NZ . LYS A 1 80 ? 39.309 26.042 15.532 1.00 47.10 ? 80 LYS A NZ 1 ATOM 556 N N . ALA A 1 81 ? 39.814 30.843 10.951 1.00 33.11 ? 81 ALA A N 1 ATOM 557 C CA . ALA A 1 81 ? 40.637 31.161 9.790 1.00 32.88 ? 81 ALA A CA 1 ATOM 558 C C . ALA A 1 81 ? 41.169 32.588 9.856 1.00 35.10 ? 81 ALA A C 1 ATOM 559 O O . ALA A 1 81 ? 42.120 32.936 9.155 1.00 34.83 ? 81 ALA A O 1 ATOM 560 C CB . ALA A 1 81 ? 39.830 30.956 8.512 1.00 34.42 ? 81 ALA A CB 1 ATOM 561 N N . LEU A 1 82 ? 40.556 33.413 10.699 1.00 33.41 ? 82 LEU A N 1 ATOM 562 C CA . LEU A 1 82 ? 40.982 34.797 10.853 1.00 34.05 ? 82 LEU A CA 1 ATOM 563 C C . LEU A 1 82 ? 41.801 34.982 12.128 1.00 32.89 ? 82 LEU A C 1 ATOM 564 O O . LEU A 1 82 ? 42.211 36.092 12.454 1.00 34.92 ? 82 LEU A O 1 ATOM 565 C CB . LEU A 1 82 ? 39.765 35.728 10.876 1.00 34.54 ? 82 LEU A CB 1 ATOM 566 C CG . LEU A 1 82 ? 38.927 35.763 9.594 1.00 35.23 ? 82 LEU A CG 1 ATOM 567 C CD1 . LEU A 1 82 ? 37.743 36.704 9.782 1.00 36.98 ? 82 LEU A CD1 1 ATOM 568 C CD2 . LEU A 1 82 ? 39.794 36.220 8.424 1.00 34.71 ? 82 LEU A CD2 1 ATOM 569 N N . GLY A 1 83 ? 42.023 33.888 12.849 1.00 32.87 ? 83 GLY A N 1 ATOM 570 C CA . GLY A 1 83 ? 42.805 33.948 14.073 1.00 31.87 ? 83 GLY A CA 1 ATOM 571 C C . GLY A 1 83 ? 42.035 34.422 15.290 1.00 33.84 ? 83 GLY A C 1 ATOM 572 O O . GLY A 1 83 ? 42.629 34.881 16.270 1.00 33.20 ? 83 GLY A O 1 ATOM 573 N N . ILE A 1 84 ? 40.711 34.312 15.234 1.00 32.39 ? 84 ILE A N 1 ATOM 574 C CA . ILE A 1 84 ? 39.866 34.730 16.343 1.00 34.34 ? 84 ILE A CA 1 ATOM 575 C C . ILE A 1 84 ? 39.143 33.527 16.936 1.00 33.68 ? 84 ILE A C 1 ATOM 576 O O . ILE A 1 84 ? 38.589 32.705 16.210 1.00 35.28 ? 84 ILE A O 1 ATOM 577 C CB . ILE A 1 84 ? 38.820 35.773 15.881 1.00 35.10 ? 84 ILE A CB 1 ATOM 578 C CG1 . ILE A 1 84 ? 39.526 37.054 15.426 1.00 34.70 ? 84 ILE A CG1 1 ATOM 579 C CG2 . ILE A 1 84 ? 37.849 36.078 17.012 1.00 35.10 ? 84 ILE A CG2 1 ATOM 580 C CD1 . ILE A 1 84 ? 38.607 38.070 14.772 1.00 37.53 ? 84 ILE A CD1 1 ATOM 581 N N . SER A 1 85 ? 39.167 33.417 18.259 1.00 33.59 ? 85 SER A N 1 ATOM 582 C CA . SER A 1 85 ? 38.491 32.324 18.948 1.00 33.00 ? 85 SER A CA 1 ATOM 583 C C . SER A 1 85 ? 37.053 32.775 19.174 1.00 31.03 ? 85 SER A C 1 ATOM 584 O O . SER A 1 85 ? 36.793 33.656 19.995 1.00 31.77 ? 85 SER A O 1 ATOM 585 C CB . SER A 1 85 ? 39.168 32.050 20.293 1.00 38.57 ? 85 SER A CB 1 ATOM 586 O OG . SER A 1 85 ? 39.198 33.225 21.089 1.00 44.41 ? 85 SER A OG 1 ATOM 587 N N . PRO A 1 86 ? 36.096 32.182 18.438 1.00 27.61 ? 86 PRO A N 1 ATOM 588 C CA . PRO A 1 86 ? 34.688 32.554 18.577 1.00 23.60 ? 86 PRO A CA 1 ATOM 589 C C . PRO A 1 86 ? 33.963 31.797 19.681 1.00 22.68 ? 86 PRO A C 1 ATOM 590 O O . PRO A 1 86 ? 34.430 30.767 20.150 1.00 23.87 ? 86 PRO A O 1 ATOM 591 C CB . PRO A 1 86 ? 34.128 32.237 17.199 1.00 22.56 ? 86 PRO A CB 1 ATOM 592 C CG . PRO A 1 86 ? 34.830 30.950 16.883 1.00 23.95 ? 86 PRO A CG 1 ATOM 593 C CD . PRO A 1 86 ? 36.274 31.219 17.335 1.00 24.99 ? 86 PRO A CD 1 ATOM 594 N N . PHE A 1 87 ? 32.805 32.308 20.075 1.00 18.71 ? 87 PHE A N 1 ATOM 595 C CA . PHE A 1 87 ? 32.015 31.683 21.129 1.00 18.90 ? 87 PHE A CA 1 ATOM 596 C C . PHE A 1 87 ? 31.155 30.529 20.631 1.00 19.39 ? 87 PHE A C 1 ATOM 597 O O . PHE A 1 87 ? 31.169 29.436 21.204 1.00 17.84 ? 87 PHE A O 1 ATOM 598 C CB . PHE A 1 87 ? 31.106 32.721 21.776 1.00 18.13 ? 87 PHE A CB 1 ATOM 599 C CG . PHE A 1 87 ? 30.242 32.168 22.873 1.00 18.51 ? 87 PHE A CG 1 ATOM 600 C CD1 . PHE A 1 87 ? 30.790 31.854 24.110 1.00 21.93 ? 87 PHE A CD1 1 ATOM 601 C CD2 . PHE A 1 87 ? 28.884 31.974 22.671 1.00 19.40 ? 87 PHE A CD2 1 ATOM 602 C CE1 . PHE A 1 87 ? 29.991 31.357 25.137 1.00 21.00 ? 87 PHE A CE1 1 ATOM 603 C CE2 . PHE A 1 87 ? 28.076 31.478 23.688 1.00 23.16 ? 87 PHE A CE2 1 ATOM 604 C CZ . PHE A 1 87 ? 28.631 31.170 24.924 1.00 20.97 ? 87 PHE A CZ 1 ATOM 605 N N . HIS A 1 88 ? 30.405 30.778 19.560 1.00 17.48 ? 88 HIS A N 1 ATOM 606 C CA . HIS A 1 88 ? 29.494 29.778 19.006 1.00 16.97 ? 88 HIS A CA 1 ATOM 607 C C . HIS A 1 88 ? 30.135 28.706 18.129 1.00 19.58 ? 88 HIS A C 1 ATOM 608 O O . HIS A 1 88 ? 31.136 28.953 17.455 1.00 19.11 ? 88 HIS A O 1 ATOM 609 C CB . HIS A 1 88 ? 28.400 30.485 18.197 1.00 19.15 ? 88 HIS A CB 1 ATOM 610 C CG . HIS A 1 88 ? 27.728 31.595 18.942 1.00 17.71 ? 88 HIS A CG 1 ATOM 611 N ND1 . HIS A 1 88 ? 28.188 32.895 18.917 1.00 19.83 ? 88 HIS A ND1 1 ATOM 612 C CD2 . HIS A 1 88 ? 26.661 31.590 19.775 1.00 19.49 ? 88 HIS A CD2 1 ATOM 613 C CE1 . HIS A 1 88 ? 27.434 33.642 19.703 1.00 19.56 ? 88 HIS A CE1 1 ATOM 614 N NE2 . HIS A 1 88 ? 26.500 32.874 20.237 1.00 21.01 ? 88 HIS A NE2 1 ATOM 615 N N . GLU A 1 89 ? 29.543 27.515 18.144 1.00 19.91 ? 89 GLU A N 1 ATOM 616 C CA . GLU A 1 89 ? 30.022 26.412 17.321 1.00 20.89 ? 89 GLU A CA 1 ATOM 617 C C . GLU A 1 89 ? 29.590 26.697 15.886 1.00 20.83 ? 89 GLU A C 1 ATOM 618 O O . GLU A 1 89 ? 30.305 26.406 14.918 1.00 18.46 ? 89 GLU A O 1 ATOM 619 C CB . GLU A 1 89 ? 29.415 25.091 17.807 1.00 19.81 ? 89 GLU A CB 1 ATOM 620 C CG . GLU A 1 89 ? 30.078 24.571 19.057 1.00 22.17 ? 89 GLU A CG 1 ATOM 621 C CD . GLU A 1 89 ? 31.542 24.278 18.824 1.00 24.39 ? 89 GLU A CD 1 ATOM 622 O OE1 . GLU A 1 89 ? 31.829 23.392 18.000 1.00 27.41 ? 89 GLU A OE1 1 ATOM 623 O OE2 . GLU A 1 89 ? 32.398 24.934 19.453 1.00 26.11 ? 89 GLU A OE2 1 ATOM 624 N N . HIS A 1 90 ? 28.407 27.283 15.768 1.00 20.70 ? 90 HIS A N 1 ATOM 625 C CA . HIS A 1 90 ? 27.834 27.649 14.480 1.00 21.23 ? 90 HIS A CA 1 ATOM 626 C C . HIS A 1 90 ? 26.579 28.457 14.748 1.00 20.67 ? 90 HIS A C 1 ATOM 627 O O . HIS A 1 90 ? 26.179 28.637 15.903 1.00 21.60 ? 90 HIS A O 1 ATOM 628 C CB . HIS A 1 90 ? 27.485 26.398 13.663 1.00 23.38 ? 90 HIS A CB 1 ATOM 629 C CG . HIS A 1 90 ? 26.539 25.463 14.351 1.00 28.28 ? 90 HIS A CG 1 ATOM 630 N ND1 . HIS A 1 90 ? 26.892 24.181 14.714 1.00 31.02 ? 90 HIS A ND1 1 ATOM 631 C CD2 . HIS A 1 90 ? 25.256 25.627 14.750 1.00 30.82 ? 90 HIS A CD2 1 ATOM 632 C CE1 . HIS A 1 90 ? 25.867 23.596 15.309 1.00 30.56 ? 90 HIS A CE1 1 ATOM 633 N NE2 . HIS A 1 90 ? 24.862 24.452 15.344 1.00 32.12 ? 90 HIS A NE2 1 ATOM 634 N N . ALA A 1 91 ? 25.965 28.963 13.688 1.00 20.58 ? 91 ALA A N 1 ATOM 635 C CA . ALA A 1 91 ? 24.735 29.720 13.824 1.00 20.37 ? 91 ALA A CA 1 ATOM 636 C C . ALA A 1 91 ? 23.661 28.907 13.120 1.00 22.92 ? 91 ALA A C 1 ATOM 637 O O . ALA A 1 91 ? 23.855 28.470 11.994 1.00 20.74 ? 91 ALA A O 1 ATOM 638 C CB . ALA A 1 91 ? 24.873 31.092 13.172 1.00 20.86 ? 91 ALA A CB 1 ATOM 639 N N . GLU A 1 92 ? 22.536 28.698 13.792 1.00 24.32 ? 92 GLU A N 1 ATOM 640 C CA . GLU A 1 92 ? 21.442 27.925 13.224 1.00 27.95 ? 92 GLU A CA 1 ATOM 641 C C . GLU A 1 92 ? 20.178 28.753 13.055 1.00 25.97 ? 92 GLU A C 1 ATOM 642 O O . GLU A 1 92 ? 19.832 29.560 13.916 1.00 26.26 ? 92 GLU A O 1 ATOM 643 C CB . GLU A 1 92 ? 21.122 26.719 14.114 1.00 33.58 ? 92 GLU A CB 1 ATOM 644 C CG . GLU A 1 92 ? 21.998 25.500 13.891 1.00 43.22 ? 92 GLU A CG 1 ATOM 645 C CD . GLU A 1 92 ? 21.570 24.327 14.755 1.00 48.49 ? 92 GLU A CD 1 ATOM 646 O OE1 . GLU A 1 92 ? 20.355 24.032 14.797 1.00 49.98 ? 92 GLU A OE1 1 ATOM 647 O OE2 . GLU A 1 92 ? 22.444 23.694 15.385 1.00 50.80 ? 92 GLU A OE2 1 ATOM 648 N N . VAL A 1 93 ? 19.498 28.556 11.933 1.00 20.50 ? 93 VAL A N 1 ATOM 649 C CA . VAL A 1 93 ? 18.249 29.252 11.671 1.00 19.65 ? 93 VAL A CA 1 ATOM 650 C C . VAL A 1 93 ? 17.228 28.172 11.331 1.00 19.55 ? 93 VAL A C 1 ATOM 651 O O . VAL A 1 93 ? 17.380 27.461 10.340 1.00 16.99 ? 93 VAL A O 1 ATOM 652 C CB . VAL A 1 93 ? 18.384 30.227 10.492 1.00 19.77 ? 93 VAL A CB 1 ATOM 653 C CG1 . VAL A 1 93 ? 17.037 30.884 10.207 1.00 23.54 ? 93 VAL A CG1 1 ATOM 654 C CG2 . VAL A 1 93 ? 19.430 31.288 10.822 1.00 23.12 ? 93 VAL A CG2 1 ATOM 655 N N . VAL A 1 94 ? 16.196 28.042 12.159 1.00 17.41 ? 94 VAL A N 1 ATOM 656 C CA . VAL A 1 94 ? 15.173 27.021 11.940 1.00 19.31 ? 94 VAL A CA 1 ATOM 657 C C . VAL A 1 94 ? 13.815 27.658 11.687 1.00 19.93 ? 94 VAL A C 1 ATOM 658 O O . VAL A 1 94 ? 13.346 28.470 12.488 1.00 19.01 ? 94 VAL A O 1 ATOM 659 C CB . VAL A 1 94 ? 15.076 26.081 13.159 1.00 20.77 ? 94 VAL A CB 1 ATOM 660 C CG1 . VAL A 1 94 ? 14.068 24.975 12.889 1.00 20.04 ? 94 VAL A CG1 1 ATOM 661 C CG2 . VAL A 1 94 ? 16.457 25.498 13.475 1.00 20.80 ? 94 VAL A CG2 1 ATOM 662 N N . PHE A 1 95 ? 13.168 27.271 10.588 1.00 17.79 ? 95 PHE A N 1 ATOM 663 C CA . PHE A 1 95 ? 11.884 27.857 10.234 1.00 19.37 ? 95 PHE A CA 1 ATOM 664 C C . PHE A 1 95 ? 11.013 26.961 9.363 1.00 18.07 ? 95 PHE A C 1 ATOM 665 O O . PHE A 1 95 ? 11.513 26.081 8.662 1.00 16.58 ? 95 PHE A O 1 ATOM 666 C CB . PHE A 1 95 ? 12.115 29.170 9.478 1.00 19.12 ? 95 PHE A CB 1 ATOM 667 C CG . PHE A 1 95 ? 12.862 28.993 8.178 1.00 22.52 ? 95 PHE A CG 1 ATOM 668 C CD1 . PHE A 1 95 ? 14.225 28.720 8.174 1.00 20.68 ? 95 PHE A CD1 1 ATOM 669 C CD2 . PHE A 1 95 ? 12.189 29.072 6.960 1.00 20.83 ? 95 PHE A CD2 1 ATOM 670 C CE1 . PHE A 1 95 ? 14.914 28.523 6.972 1.00 23.69 ? 95 PHE A CE1 1 ATOM 671 C CE2 . PHE A 1 95 ? 12.866 28.878 5.753 1.00 25.14 ? 95 PHE A CE2 1 ATOM 672 C CZ . PHE A 1 95 ? 14.230 28.603 5.759 1.00 21.89 ? 95 PHE A CZ 1 ATOM 673 N N . THR A 1 96 ? 9.703 27.188 9.421 1.00 18.23 ? 96 THR A N 1 ATOM 674 C CA . THR A 1 96 ? 8.779 26.443 8.581 1.00 17.75 ? 96 THR A CA 1 ATOM 675 C C . THR A 1 96 ? 8.691 27.242 7.288 1.00 17.69 ? 96 THR A C 1 ATOM 676 O O . THR A 1 96 ? 8.560 28.471 7.306 1.00 19.53 ? 96 THR A O 1 ATOM 677 C CB . THR A 1 96 ? 7.386 26.337 9.206 1.00 19.98 ? 96 THR A CB 1 ATOM 678 O OG1 . THR A 1 96 ? 7.478 25.629 10.450 1.00 20.11 ? 96 THR A OG1 1 ATOM 679 C CG2 . THR A 1 96 ? 6.444 25.580 8.264 1.00 19.85 ? 96 THR A CG2 1 ATOM 680 N N . ALA A 1 97 ? 8.780 26.555 6.159 1.00 17.99 ? 97 ALA A N 1 ATOM 681 C CA . ALA A 1 97 ? 8.728 27.250 4.888 1.00 18.46 ? 97 ALA A CA 1 ATOM 682 C C . ALA A 1 97 ? 7.589 26.786 4.004 1.00 18.23 ? 97 ALA A C 1 ATOM 683 O O . ALA A 1 97 ? 7.177 25.626 4.060 1.00 20.03 ? 97 ALA A O 1 ATOM 684 C CB . ALA A 1 97 ? 10.053 27.084 4.155 1.00 20.47 ? 97 ALA A CB 1 ATOM 685 N N . ASN A 1 98 ? 7.083 27.719 3.204 1.00 21.19 ? 98 ASN A N 1 ATOM 686 C CA . ASN A 1 98 ? 6.013 27.469 2.246 1.00 23.92 ? 98 ASN A CA 1 ATOM 687 C C . ASN A 1 98 ? 4.716 26.884 2.801 1.00 28.29 ? 98 ASN A C 1 ATOM 688 O O . ASN A 1 98 ? 3.961 26.250 2.066 1.00 30.72 ? 98 ASN A O 1 ATOM 689 C CB . ASN A 1 98 ? 6.547 26.567 1.134 1.00 24.79 ? 98 ASN A CB 1 ATOM 690 C CG . ASN A 1 98 ? 7.865 27.064 0.571 1.00 27.59 ? 98 ASN A CG 1 ATOM 691 O OD1 . ASN A 1 98 ? 7.964 28.202 0.099 1.00 26.96 ? 98 ASN A OD1 1 ATOM 692 N ND2 . ASN A 1 98 ? 8.887 26.218 0.619 1.00 30.56 ? 98 ASN A ND2 1 ATOM 693 N N . ASP A 1 99 ? 4.446 27.123 4.079 1.00 29.80 ? 99 ASP A N 1 ATOM 694 C CA . ASP A 1 99 ? 3.241 26.612 4.729 1.00 36.35 ? 99 ASP A CA 1 ATOM 695 C C . ASP A 1 99 ? 1.939 27.135 4.120 1.00 39.43 ? 99 ASP A C 1 ATOM 696 O O . ASP A 1 99 ? 0.911 26.460 4.168 1.00 38.73 ? 99 ASP A O 1 ATOM 697 C CB . ASP A 1 99 ? 3.274 26.948 6.222 1.00 39.02 ? 99 ASP A CB 1 ATOM 698 C CG . ASP A 1 99 ? 3.730 28.369 6.487 1.00 43.35 ? 99 ASP A CG 1 ATOM 699 O OD1 . ASP A 1 99 ? 4.891 28.691 6.152 1.00 44.51 ? 99 ASP A OD1 1 ATOM 700 O OD2 . ASP A 1 99 ? 2.931 29.165 7.026 1.00 48.54 ? 99 ASP A OD2 1 ATOM 701 N N . SER A 1 100 ? 1.981 28.336 3.554 1.00 40.63 ? 100 SER A N 1 ATOM 702 C CA . SER A 1 100 ? 0.796 28.925 2.944 1.00 42.99 ? 100 SER A CA 1 ATOM 703 C C . SER A 1 100 ? 1.052 29.268 1.482 1.00 41.83 ? 100 SER A C 1 ATOM 704 O O . SER A 1 100 ? 0.506 30.235 0.954 1.00 43.25 ? 100 SER A O 1 ATOM 705 C CB . SER A 1 100 ? 0.384 30.183 3.711 1.00 45.22 ? 100 SER A CB 1 ATOM 706 O OG . SER A 1 100 ? 1.460 31.102 3.792 1.00 50.90 ? 100 SER A OG 1 ATOM 707 N N . GLY A 1 101 ? 1.885 28.464 0.831 1.00 40.22 ? 101 GLY A N 1 ATOM 708 C CA . GLY A 1 101 ? 2.205 28.701 -0.562 1.00 37.08 ? 101 GLY A CA 1 ATOM 709 C C . GLY A 1 101 ? 3.680 28.996 -0.758 1.00 35.46 ? 101 GLY A C 1 ATOM 710 O O . GLY A 1 101 ? 4.395 29.255 0.210 1.00 33.87 ? 101 GLY A O 1 ATOM 711 N N . PRO A 1 102 ? 4.168 28.957 -2.007 1.00 34.68 ? 102 PRO A N 1 ATOM 712 C CA . PRO A 1 102 ? 5.572 29.222 -2.337 1.00 32.03 ? 102 PRO A CA 1 ATOM 713 C C . PRO A 1 102 ? 5.999 30.651 -2.010 1.00 30.77 ? 102 PRO A C 1 ATOM 714 O O . PRO A 1 102 ? 5.327 31.613 -2.378 1.00 28.17 ? 102 PRO A O 1 ATOM 715 C CB . PRO A 1 102 ? 5.633 28.950 -3.838 1.00 35.45 ? 102 PRO A CB 1 ATOM 716 C CG . PRO A 1 102 ? 4.526 27.954 -4.056 1.00 35.09 ? 102 PRO A CG 1 ATOM 717 C CD . PRO A 1 102 ? 3.426 28.517 -3.201 1.00 34.53 ? 102 PRO A CD 1 ATOM 718 N N . ARG A 1 103 ? 7.125 30.781 -1.319 1.00 28.24 ? 103 ARG A N 1 ATOM 719 C CA . ARG A 1 103 ? 7.655 32.088 -0.957 1.00 26.89 ? 103 ARG A CA 1 ATOM 720 C C . ARG A 1 103 ? 9.141 32.103 -1.279 1.00 26.03 ? 103 ARG A C 1 ATOM 721 O O . ARG A 1 103 ? 9.735 31.053 -1.522 1.00 25.12 ? 103 ARG A O 1 ATOM 722 C CB . ARG A 1 103 ? 7.455 32.355 0.539 1.00 26.77 ? 103 ARG A CB 1 ATOM 723 C CG . ARG A 1 103 ? 6.003 32.510 0.984 1.00 30.81 ? 103 ARG A CG 1 ATOM 724 C CD . ARG A 1 103 ? 5.404 33.823 0.498 1.00 33.24 ? 103 ARG A CD 1 ATOM 725 N NE . ARG A 1 103 ? 4.019 33.987 0.939 1.00 38.26 ? 103 ARG A NE 1 ATOM 726 C CZ . ARG A 1 103 ? 2.981 33.336 0.421 1.00 39.69 ? 103 ARG A CZ 1 ATOM 727 N NH1 . ARG A 1 103 ? 3.161 32.471 -0.568 1.00 41.02 ? 103 ARG A NH1 1 ATOM 728 N NH2 . ARG A 1 103 ? 1.760 33.546 0.896 1.00 43.07 ? 103 ARG A NH2 1 ATOM 729 N N . ARG A 1 104 ? 9.728 33.297 -1.296 1.00 23.91 ? 104 ARG A N 1 ATOM 730 C CA . ARG A 1 104 ? 11.152 33.455 -1.555 1.00 24.52 ? 104 ARG A CA 1 ATOM 731 C C . ARG A 1 104 ? 11.745 33.868 -0.215 1.00 24.26 ? 104 ARG A C 1 ATOM 732 O O . ARG A 1 104 ? 11.271 34.816 0.416 1.00 20.59 ? 104 ARG A O 1 ATOM 733 C CB . ARG A 1 104 ? 11.397 34.540 -2.602 1.00 29.69 ? 104 ARG A CB 1 ATOM 734 C CG . ARG A 1 104 ? 10.656 34.313 -3.914 1.00 38.83 ? 104 ARG A CG 1 ATOM 735 C CD . ARG A 1 104 ? 11.613 34.219 -5.096 1.00 44.11 ? 104 ARG A CD 1 ATOM 736 N NE . ARG A 1 104 ? 12.456 35.406 -5.212 1.00 51.76 ? 104 ARG A NE 1 ATOM 737 C CZ . ARG A 1 104 ? 13.393 35.573 -6.142 1.00 56.15 ? 104 ARG A CZ 1 ATOM 738 N NH1 . ARG A 1 104 ? 13.612 34.626 -7.046 1.00 57.39 ? 104 ARG A NH1 1 ATOM 739 N NH2 . ARG A 1 104 ? 14.114 36.687 -6.165 1.00 56.84 ? 104 ARG A NH2 1 ATOM 740 N N . TYR A 1 105 ? 12.776 33.156 0.219 1.00 20.48 ? 105 TYR A N 1 ATOM 741 C CA . TYR A 1 105 ? 13.388 33.443 1.505 1.00 18.59 ? 105 TYR A CA 1 ATOM 742 C C . TYR A 1 105 ? 14.832 33.889 1.424 1.00 19.83 ? 105 TYR A C 1 ATOM 743 O O . TYR A 1 105 ? 15.651 33.234 0.784 1.00 18.02 ? 105 TYR A O 1 ATOM 744 C CB . TYR A 1 105 ? 13.337 32.204 2.403 1.00 19.68 ? 105 TYR A CB 1 ATOM 745 C CG . TYR A 1 105 ? 11.950 31.701 2.699 1.00 18.18 ? 105 TYR A CG 1 ATOM 746 C CD1 . TYR A 1 105 ? 11.276 30.896 1.789 1.00 19.08 ? 105 TYR A CD1 1 ATOM 747 C CD2 . TYR A 1 105 ? 11.302 32.044 3.887 1.00 17.49 ? 105 TYR A CD2 1 ATOM 748 C CE1 . TYR A 1 105 ? 9.988 30.442 2.047 1.00 18.53 ? 105 TYR A CE1 1 ATOM 749 C CE2 . TYR A 1 105 ? 10.012 31.593 4.158 1.00 20.51 ? 105 TYR A CE2 1 ATOM 750 C CZ . TYR A 1 105 ? 9.364 30.793 3.231 1.00 18.33 ? 105 TYR A CZ 1 ATOM 751 O OH . TYR A 1 105 ? 8.090 30.346 3.478 1.00 19.16 ? 105 TYR A OH 1 ATOM 752 N N . THR A 1 106 ? 15.133 35.016 2.063 1.00 18.53 ? 106 THR A N 1 ATOM 753 C CA . THR A 1 106 ? 16.501 35.486 2.140 1.00 19.63 ? 106 THR A CA 1 ATOM 754 C C . THR A 1 106 ? 16.841 35.444 3.625 1.00 19.12 ? 106 THR A C 1 ATOM 755 O O . THR A 1 106 ? 16.183 36.095 4.444 1.00 17.88 ? 106 THR A O 1 ATOM 756 C CB . THR A 1 106 ? 16.678 36.927 1.633 1.00 23.88 ? 106 THR A CB 1 ATOM 757 O OG1 . THR A 1 106 ? 16.329 36.996 0.246 1.00 24.09 ? 106 THR A OG1 1 ATOM 758 C CG2 . THR A 1 106 ? 18.138 37.352 1.795 1.00 26.49 ? 106 THR A CG2 1 ATOM 759 N N . ILE A 1 107 ? 17.846 34.646 3.966 1.00 16.31 ? 107 ILE A N 1 ATOM 760 C CA . ILE A 1 107 ? 18.288 34.500 5.338 1.00 19.34 ? 107 ILE A CA 1 ATOM 761 C C . ILE A 1 107 ? 19.586 35.284 5.453 1.00 19.95 ? 107 ILE A C 1 ATOM 762 O O . ILE A 1 107 ? 20.564 34.986 4.766 1.00 21.94 ? 107 ILE A O 1 ATOM 763 C CB . ILE A 1 107 ? 18.556 33.020 5.685 1.00 20.47 ? 107 ILE A CB 1 ATOM 764 C CG1 . ILE A 1 107 ? 17.282 32.191 5.489 1.00 23.71 ? 107 ILE A CG1 1 ATOM 765 C CG2 . ILE A 1 107 ? 19.061 32.903 7.114 1.00 23.05 ? 107 ILE A CG2 1 ATOM 766 C CD1 . ILE A 1 107 ? 16.130 32.586 6.395 1.00 27.24 ? 107 ILE A CD1 1 ATOM 767 N N . ALA A 1 108 ? 19.589 36.294 6.312 1.00 19.19 ? 108 ALA A N 1 ATOM 768 C CA . ALA A 1 108 ? 20.774 37.117 6.488 1.00 20.22 ? 108 ALA A CA 1 ATOM 769 C C . ALA A 1 108 ? 21.353 36.946 7.877 1.00 18.82 ? 108 ALA A C 1 ATOM 770 O O . ALA A 1 108 ? 20.613 36.810 8.850 1.00 19.56 ? 108 ALA A O 1 ATOM 771 C CB . ALA A 1 108 ? 20.428 38.570 6.248 1.00 21.23 ? 108 ALA A CB 1 ATOM 772 N N . ALA A 1 109 ? 22.680 36.949 7.959 1.00 17.18 ? 109 ALA A N 1 ATOM 773 C CA . ALA A 1 109 ? 23.365 36.809 9.233 1.00 17.88 ? 109 ALA A CA 1 ATOM 774 C C . ALA A 1 109 ? 24.492 37.837 9.333 1.00 18.15 ? 109 ALA A C 1 ATOM 775 O O . ALA A 1 109 ? 25.238 38.058 8.376 1.00 17.56 ? 109 ALA A O 1 ATOM 776 C CB . ALA A 1 109 ? 23.925 35.394 9.377 1.00 20.35 ? 109 ALA A CB 1 ATOM 777 N N . LEU A 1 110 ? 24.598 38.467 10.497 1.00 16.68 ? 110 LEU A N 1 ATOM 778 C CA . LEU A 1 110 ? 25.633 39.455 10.771 1.00 15.93 ? 110 LEU A CA 1 ATOM 779 C C . LEU A 1 110 ? 26.483 38.813 11.862 1.00 17.14 ? 110 LEU A C 1 ATOM 780 O O . LEU A 1 110 ? 25.993 38.530 12.952 1.00 17.19 ? 110 LEU A O 1 ATOM 781 C CB . LEU A 1 110 ? 24.995 40.753 11.262 1.00 15.98 ? 110 LEU A CB 1 ATOM 782 C CG . LEU A 1 110 ? 25.944 41.889 11.646 1.00 20.01 ? 110 LEU A CG 1 ATOM 783 C CD1 . LEU A 1 110 ? 26.874 42.196 10.482 1.00 20.08 ? 110 LEU A CD1 1 ATOM 784 C CD2 . LEU A 1 110 ? 25.140 43.111 12.027 1.00 20.69 ? 110 LEU A CD2 1 ATOM 785 N N . LEU A 1 111 ? 27.761 38.604 11.577 1.00 13.76 ? 111 LEU A N 1 ATOM 786 C CA . LEU A 1 111 ? 28.628 37.908 12.514 1.00 14.60 ? 111 LEU A CA 1 ATOM 787 C C . LEU A 1 111 ? 29.681 38.695 13.281 1.00 16.73 ? 111 LEU A C 1 ATOM 788 O O . LEU A 1 111 ? 30.354 39.560 12.729 1.00 14.60 ? 111 LEU A O 1 ATOM 789 C CB . LEU A 1 111 ? 29.353 36.784 11.773 1.00 14.68 ? 111 LEU A CB 1 ATOM 790 C CG . LEU A 1 111 ? 28.554 35.849 10.864 1.00 16.59 ? 111 LEU A CG 1 ATOM 791 C CD1 . LEU A 1 111 ? 29.530 34.873 10.200 1.00 17.66 ? 111 LEU A CD1 1 ATOM 792 C CD2 . LEU A 1 111 ? 27.495 35.103 11.670 1.00 14.33 ? 111 LEU A CD2 1 ATOM 793 N N . SER A 1 112 ? 29.824 38.345 14.556 1.00 16.68 ? 112 SER A N 1 ATOM 794 C CA . SER A 1 112 ? 30.829 38.918 15.443 1.00 17.86 ? 112 SER A CA 1 ATOM 795 C C . SER A 1 112 ? 31.338 37.709 16.225 1.00 19.31 ? 112 SER A C 1 ATOM 796 O O . SER A 1 112 ? 30.658 36.690 16.306 1.00 17.17 ? 112 SER A O 1 ATOM 797 C CB . SER A 1 112 ? 30.225 39.954 16.400 1.00 19.20 ? 112 SER A CB 1 ATOM 798 O OG . SER A 1 112 ? 29.897 41.149 15.719 1.00 25.98 ? 112 SER A OG 1 ATOM 799 N N . PRO A 1 113 ? 32.542 37.797 16.798 1.00 19.72 ? 113 PRO A N 1 ATOM 800 C CA . PRO A 1 113 ? 33.079 36.661 17.555 1.00 19.21 ? 113 PRO A CA 1 ATOM 801 C C . PRO A 1 113 ? 32.178 36.107 18.662 1.00 17.58 ? 113 PRO A C 1 ATOM 802 O O . PRO A 1 113 ? 32.050 34.893 18.801 1.00 16.30 ? 113 PRO A O 1 ATOM 803 C CB . PRO A 1 113 ? 34.401 37.206 18.087 1.00 19.57 ? 113 PRO A CB 1 ATOM 804 C CG . PRO A 1 113 ? 34.839 38.108 16.968 1.00 20.70 ? 113 PRO A CG 1 ATOM 805 C CD . PRO A 1 113 ? 33.561 38.849 16.637 1.00 18.09 ? 113 PRO A CD 1 ATOM 806 N N . TYR A 1 114 ? 31.560 36.986 19.445 1.00 15.83 ? 114 TYR A N 1 ATOM 807 C CA . TYR A 1 114 ? 30.681 36.544 20.529 1.00 16.78 ? 114 TYR A CA 1 ATOM 808 C C . TYR A 1 114 ? 29.220 36.892 20.321 1.00 15.27 ? 114 TYR A C 1 ATOM 809 O O . TYR A 1 114 ? 28.429 36.871 21.261 1.00 19.31 ? 114 TYR A O 1 ATOM 810 C CB . TYR A 1 114 ? 31.139 37.141 21.857 1.00 17.02 ? 114 TYR A CB 1 ATOM 811 C CG . TYR A 1 114 ? 32.350 36.448 22.426 1.00 22.69 ? 114 TYR A CG 1 ATOM 812 C CD1 . TYR A 1 114 ? 33.590 36.548 21.800 1.00 25.01 ? 114 TYR A CD1 1 ATOM 813 C CD2 . TYR A 1 114 ? 32.250 35.662 23.579 1.00 22.82 ? 114 TYR A CD2 1 ATOM 814 C CE1 . TYR A 1 114 ? 34.707 35.881 22.304 1.00 28.41 ? 114 TYR A CE1 1 ATOM 815 C CE2 . TYR A 1 114 ? 33.359 34.992 24.089 1.00 25.57 ? 114 TYR A CE2 1 ATOM 816 C CZ . TYR A 1 114 ? 34.582 35.108 23.446 1.00 29.37 ? 114 TYR A CZ 1 ATOM 817 O OH . TYR A 1 114 ? 35.686 34.459 23.949 1.00 34.57 ? 114 TYR A OH 1 ATOM 818 N N . SER A 1 115 ? 28.850 37.208 19.090 1.00 16.17 ? 115 SER A N 1 ATOM 819 C CA . SER A 1 115 ? 27.472 37.567 18.833 1.00 16.86 ? 115 SER A CA 1 ATOM 820 C C . SER A 1 115 ? 27.114 37.456 17.366 1.00 17.61 ? 115 SER A C 1 ATOM 821 O O . SER A 1 115 ? 27.973 37.541 16.492 1.00 19.77 ? 115 SER A O 1 ATOM 822 C CB . SER A 1 115 ? 27.230 39.007 19.302 1.00 17.67 ? 115 SER A CB 1 ATOM 823 O OG . SER A 1 115 ? 25.938 39.466 18.940 1.00 24.38 ? 115 SER A OG 1 ATOM 824 N N . TYR A 1 116 ? 25.840 37.234 17.098 1.00 17.36 ? 116 TYR A N 1 ATOM 825 C CA . TYR A 1 116 ? 25.386 37.210 15.723 1.00 16.61 ? 116 TYR A CA 1 ATOM 826 C C . TYR A 1 116 ? 23.916 37.531 15.711 1.00 19.13 ? 116 TYR A C 1 ATOM 827 O O . TYR A 1 116 ? 23.211 37.328 16.702 1.00 17.97 ? 116 TYR A O 1 ATOM 828 C CB . TYR A 1 116 ? 25.687 35.872 15.035 1.00 17.06 ? 116 TYR A CB 1 ATOM 829 C CG . TYR A 1 116 ? 24.934 34.669 15.546 1.00 20.72 ? 116 TYR A CG 1 ATOM 830 C CD1 . TYR A 1 116 ? 23.629 34.406 15.137 1.00 20.62 ? 116 TYR A CD1 1 ATOM 831 C CD2 . TYR A 1 116 ? 25.537 33.783 16.436 1.00 20.60 ? 116 TYR A CD2 1 ATOM 832 C CE1 . TYR A 1 116 ? 22.940 33.278 15.607 1.00 22.75 ? 116 TYR A CE1 1 ATOM 833 C CE2 . TYR A 1 116 ? 24.863 32.662 16.906 1.00 22.64 ? 116 TYR A CE2 1 ATOM 834 C CZ . TYR A 1 116 ? 23.571 32.416 16.490 1.00 23.82 ? 116 TYR A CZ 1 ATOM 835 O OH . TYR A 1 116 ? 22.923 31.298 16.958 1.00 29.82 ? 116 TYR A OH 1 ATOM 836 N N . SER A 1 117 ? 23.475 38.094 14.599 1.00 17.44 ? 117 SER A N 1 ATOM 837 C CA . SER A 1 117 ? 22.088 38.464 14.417 1.00 19.54 ? 117 SER A CA 1 ATOM 838 C C . SER A 1 117 ? 21.683 37.810 13.121 1.00 19.00 ? 117 SER A C 1 ATOM 839 O O . SER A 1 117 ? 22.503 37.653 12.213 1.00 17.71 ? 117 SER A O 1 ATOM 840 C CB . SER A 1 117 ? 21.950 39.985 14.272 1.00 21.93 ? 117 SER A CB 1 ATOM 841 O OG . SER A 1 117 ? 22.493 40.655 15.398 1.00 31.85 ? 117 SER A OG 1 ATOM 842 N N . THR A 1 118 ? 20.432 37.402 13.037 1.00 18.01 ? 118 THR A N 1 ATOM 843 C CA . THR A 1 118 ? 19.947 36.805 11.816 1.00 18.07 ? 118 THR A CA 1 ATOM 844 C C . THR A 1 118 ? 18.570 37.363 11.574 1.00 19.70 ? 118 THR A C 1 ATOM 845 O O . THR A 1 118 ? 17.789 37.532 12.507 1.00 21.64 ? 118 THR A O 1 ATOM 846 C CB . THR A 1 118 ? 19.873 35.265 11.890 1.00 21.97 ? 118 THR A CB 1 ATOM 847 O OG1 . THR A 1 118 ? 19.454 34.766 10.615 1.00 23.27 ? 118 THR A OG1 1 ATOM 848 C CG2 . THR A 1 118 ? 18.878 34.799 12.960 1.00 19.88 ? 118 THR A CG2 1 ATOM 849 N N . THR A 1 119 ? 18.288 37.681 10.322 1.00 18.54 ? 119 THR A N 1 ATOM 850 C CA . THR A 1 119 ? 16.991 38.204 9.978 1.00 18.36 ? 119 THR A CA 1 ATOM 851 C C . THR A 1 119 ? 16.542 37.504 8.719 1.00 17.94 ? 119 THR A C 1 ATOM 852 O O . THR A 1 119 ? 17.357 36.967 7.964 1.00 17.95 ? 119 THR A O 1 ATOM 853 C CB . THR A 1 119 ? 17.028 39.733 9.752 1.00 20.95 ? 119 THR A CB 1 ATOM 854 O OG1 . THR A 1 119 ? 15.688 40.228 9.648 1.00 24.45 ? 119 THR A OG1 1 ATOM 855 C CG2 . THR A 1 119 ? 17.775 40.076 8.478 1.00 26.20 ? 119 THR A CG2 1 ATOM 856 N N . ALA A 1 120 ? 15.239 37.488 8.505 1.00 15.90 ? 120 ALA A N 1 ATOM 857 C CA . ALA A 1 120 ? 14.700 36.858 7.321 1.00 20.01 ? 120 ALA A CA 1 ATOM 858 C C . ALA A 1 120 ? 13.851 37.865 6.578 1.00 18.42 ? 120 ALA A C 1 ATOM 859 O O . ALA A 1 120 ? 13.134 38.657 7.187 1.00 19.92 ? 120 ALA A O 1 ATOM 860 C CB . ALA A 1 120 ? 13.857 35.652 7.706 1.00 16.74 ? 120 ALA A CB 1 ATOM 861 N N . VAL A 1 121 ? 13.968 37.852 5.259 1.00 17.36 ? 121 VAL A N 1 ATOM 862 C CA . VAL A 1 121 ? 13.157 38.712 4.413 1.00 19.42 ? 121 VAL A CA 1 ATOM 863 C C . VAL A 1 121 ? 12.386 37.698 3.590 1.00 20.98 ? 121 VAL A C 1 ATOM 864 O O . VAL A 1 121 ? 12.982 36.854 2.914 1.00 21.18 ? 121 VAL A O 1 ATOM 865 C CB . VAL A 1 121 ? 14.011 39.599 3.497 1.00 22.81 ? 121 VAL A CB 1 ATOM 866 C CG1 . VAL A 1 121 ? 13.115 40.391 2.553 1.00 25.54 ? 121 VAL A CG1 1 ATOM 867 C CG2 . VAL A 1 121 ? 14.855 40.538 4.341 1.00 25.76 ? 121 VAL A CG2 1 ATOM 868 N N . VAL A 1 122 ? 11.066 37.756 3.683 1.00 20.25 ? 122 VAL A N 1 ATOM 869 C CA . VAL A 1 122 ? 10.203 36.822 2.971 1.00 22.45 ? 122 VAL A CA 1 ATOM 870 C C . VAL A 1 122 ? 9.387 37.567 1.925 1.00 26.19 ? 122 VAL A C 1 ATOM 871 O O . VAL A 1 122 ? 8.693 38.535 2.241 1.00 25.21 ? 122 VAL A O 1 ATOM 872 C CB . VAL A 1 122 ? 9.254 36.105 3.960 1.00 21.64 ? 122 VAL A CB 1 ATOM 873 C CG1 . VAL A 1 122 ? 8.415 35.064 3.225 1.00 23.83 ? 122 VAL A CG1 1 ATOM 874 C CG2 . VAL A 1 122 ? 10.070 35.445 5.060 1.00 21.85 ? 122 VAL A CG2 1 ATOM 875 N N . THR A 1 123 ? 9.482 37.107 0.681 1.00 28.99 ? 123 THR A N 1 ATOM 876 C CA . THR A 1 123 ? 8.781 37.723 -0.439 1.00 32.81 ? 123 THR A CA 1 ATOM 877 C C . THR A 1 123 ? 7.773 36.784 -1.092 1.00 34.90 ? 123 THR A C 1 ATOM 878 O O . THR A 1 123 ? 7.956 35.568 -1.107 1.00 28.52 ? 123 THR A O 1 ATOM 879 C CB . THR A 1 123 ? 9.785 38.179 -1.523 1.00 35.53 ? 123 THR A CB 1 ATOM 880 O OG1 . THR A 1 123 ? 10.623 39.211 -0.990 1.00 40.93 ? 123 THR A OG1 1 ATOM 881 C CG2 . THR A 1 123 ? 9.054 38.704 -2.754 1.00 39.21 ? 123 THR A CG2 1 ATOM 882 N N . ASN A 1 124 ? 6.704 37.364 -1.630 1.00 37.01 ? 124 ASN A N 1 ATOM 883 C CA . ASN A 1 124 ? 5.675 36.592 -2.308 1.00 42.32 ? 124 ASN A CA 1 ATOM 884 C C . ASN A 1 124 ? 5.629 37.027 -3.764 1.00 43.85 ? 124 ASN A C 1 ATOM 885 O O . ASN A 1 124 ? 4.679 37.753 -4.118 1.00 47.33 ? 124 ASN A O 1 ATOM 886 C CB . ASN A 1 124 ? 4.302 36.818 -1.667 1.00 45.60 ? 124 ASN A CB 1 ATOM 887 C CG . ASN A 1 124 ? 3.208 36.016 -2.349 1.00 50.17 ? 124 ASN A CG 1 ATOM 888 O OD1 . ASN A 1 124 ? 3.257 34.787 -2.383 1.00 52.98 ? 124 ASN A OD1 1 ATOM 889 N ND2 . ASN A 1 124 ? 2.220 36.709 -2.903 1.00 54.13 ? 124 ASN A ND2 1 ATOM 890 O OXT . ASN A 1 124 ? 6.551 36.656 -4.522 1.00 45.67 ? 124 ASN A OXT 1 ATOM 891 N N . CYS B 1 10 ? 26.101 30.741 40.052 1.00 46.26 ? 10 CYS B N 1 ATOM 892 C CA . CYS B 1 10 ? 25.419 30.727 38.725 1.00 46.78 ? 10 CYS B CA 1 ATOM 893 C C . CYS B 1 10 ? 26.424 30.757 37.577 1.00 42.42 ? 10 CYS B C 1 ATOM 894 O O . CYS B 1 10 ? 26.786 31.824 37.080 1.00 44.60 ? 10 CYS B O 1 ATOM 895 C CB . CYS B 1 10 ? 24.470 31.925 38.602 1.00 50.57 ? 10 CYS B CB 1 ATOM 896 S SG . CYS B 1 10 ? 22.988 31.837 39.643 1.00 60.23 ? 10 CYS B SG 1 ATOM 897 N N . PRO B 1 11 ? 26.891 29.578 37.140 1.00 38.19 ? 11 PRO B N 1 ATOM 898 C CA . PRO B 1 11 ? 27.858 29.499 36.042 1.00 36.47 ? 11 PRO B CA 1 ATOM 899 C C . PRO B 1 11 ? 27.217 29.849 34.699 1.00 33.24 ? 11 PRO B C 1 ATOM 900 O O . PRO B 1 11 ? 27.886 30.329 33.786 1.00 30.90 ? 11 PRO B O 1 ATOM 901 C CB . PRO B 1 11 ? 28.309 28.037 36.078 1.00 37.22 ? 11 PRO B CB 1 ATOM 902 C CG . PRO B 1 11 ? 28.030 27.611 37.489 1.00 40.89 ? 11 PRO B CG 1 ATOM 903 C CD . PRO B 1 11 ? 26.705 28.257 37.759 1.00 38.72 ? 11 PRO B CD 1 ATOM 904 N N . LEU B 1 12 ? 25.917 29.602 34.591 1.00 30.29 ? 12 LEU B N 1 ATOM 905 C CA . LEU B 1 12 ? 25.185 29.854 33.352 1.00 30.55 ? 12 LEU B CA 1 ATOM 906 C C . LEU B 1 12 ? 23.897 30.633 33.596 1.00 30.11 ? 12 LEU B C 1 ATOM 907 O O . LEU B 1 12 ? 23.061 30.231 34.405 1.00 32.15 ? 12 LEU B O 1 ATOM 908 C CB . LEU B 1 12 ? 24.861 28.521 32.674 1.00 29.81 ? 12 LEU B CB 1 ATOM 909 C CG . LEU B 1 12 ? 24.071 28.561 31.367 1.00 31.71 ? 12 LEU B CG 1 ATOM 910 C CD1 . LEU B 1 12 ? 24.896 29.261 30.293 1.00 30.76 ? 12 LEU B CD1 1 ATOM 911 C CD2 . LEU B 1 12 ? 23.731 27.141 30.937 1.00 31.98 ? 12 LEU B CD2 1 ATOM 912 N N . MET B 1 13 ? 23.739 31.746 32.885 1.00 27.67 ? 13 MET B N 1 ATOM 913 C CA . MET B 1 13 ? 22.559 32.591 33.031 1.00 28.94 ? 13 MET B CA 1 ATOM 914 C C . MET B 1 13 ? 22.010 32.957 31.653 1.00 22.71 ? 13 MET B C 1 ATOM 915 O O . MET B 1 13 ? 22.773 33.106 30.702 1.00 23.42 ? 13 MET B O 1 ATOM 916 C CB . MET B 1 13 ? 22.935 33.863 33.798 1.00 32.57 ? 13 MET B CB 1 ATOM 917 C CG . MET B 1 13 ? 23.564 33.580 35.156 1.00 45.08 ? 13 MET B CG 1 ATOM 918 S SD . MET B 1 13 ? 24.243 35.038 35.965 1.00 57.38 ? 13 MET B SD 1 ATOM 919 C CE . MET B 1 13 ? 25.987 34.890 35.532 1.00 53.26 ? 13 MET B CE 1 ATOM 920 N N . VAL B 1 14 ? 20.690 33.094 31.553 1.00 21.82 ? 14 VAL B N 1 ATOM 921 C CA . VAL B 1 14 ? 20.037 33.434 30.287 1.00 21.57 ? 14 VAL B CA 1 ATOM 922 C C . VAL B 1 14 ? 19.202 34.697 30.460 1.00 22.55 ? 14 VAL B C 1 ATOM 923 O O . VAL B 1 14 ? 18.500 34.853 31.461 1.00 24.09 ? 14 VAL B O 1 ATOM 924 C CB . VAL B 1 14 ? 19.134 32.264 29.790 1.00 20.90 ? 14 VAL B CB 1 ATOM 925 C CG1 . VAL B 1 14 ? 18.373 32.664 28.526 1.00 20.31 ? 14 VAL B CG1 1 ATOM 926 C CG2 . VAL B 1 14 ? 19.999 31.044 29.502 1.00 24.69 ? 14 VAL B CG2 1 ATOM 927 N N . LYS B 1 15 ? 19.300 35.607 29.492 1.00 20.77 ? 15 LYS B N 1 ATOM 928 C CA . LYS B 1 15 ? 18.561 36.869 29.529 1.00 21.88 ? 15 LYS B CA 1 ATOM 929 C C . LYS B 1 15 ? 17.885 37.059 28.180 1.00 19.92 ? 15 LYS B C 1 ATOM 930 O O . LYS B 1 15 ? 18.547 37.019 27.145 1.00 18.61 ? 15 LYS B O 1 ATOM 931 C CB . LYS B 1 15 ? 19.527 38.031 29.794 1.00 25.79 ? 15 LYS B CB 1 ATOM 932 C CG . LYS B 1 15 ? 18.908 39.426 29.739 1.00 30.58 ? 15 LYS B CG 1 ATOM 933 C CD . LYS B 1 15 ? 18.135 39.770 30.999 1.00 37.34 ? 15 LYS B CD 1 ATOM 934 C CE . LYS B 1 15 ? 17.744 41.246 31.008 1.00 38.28 ? 15 LYS B CE 1 ATOM 935 N NZ . LYS B 1 15 ? 17.098 41.654 32.286 1.00 42.59 ? 15 LYS B NZ 1 ATOM 936 N N . VAL B 1 16 ? 16.572 37.251 28.186 1.00 18.96 ? 16 VAL B N 1 ATOM 937 C CA . VAL B 1 16 ? 15.835 37.441 26.939 1.00 19.61 ? 16 VAL B CA 1 ATOM 938 C C . VAL B 1 16 ? 15.049 38.747 26.952 1.00 18.62 ? 16 VAL B C 1 ATOM 939 O O . VAL B 1 16 ? 14.319 39.041 27.906 1.00 18.78 ? 16 VAL B O 1 ATOM 940 C CB . VAL B 1 16 ? 14.857 36.272 26.685 1.00 19.94 ? 16 VAL B CB 1 ATOM 941 C CG1 . VAL B 1 16 ? 14.302 36.358 25.262 1.00 20.93 ? 16 VAL B CG1 1 ATOM 942 C CG2 . VAL B 1 16 ? 15.567 34.944 26.905 1.00 21.44 ? 16 VAL B CG2 1 ATOM 943 N N . LEU B 1 17 ? 15.209 39.529 25.887 1.00 18.47 ? 17 LEU B N 1 ATOM 944 C CA . LEU B 1 17 ? 14.530 40.812 25.759 1.00 18.91 ? 17 LEU B CA 1 ATOM 945 C C . LEU B 1 17 ? 13.636 40.824 24.529 1.00 17.75 ? 17 LEU B C 1 ATOM 946 O O . LEU B 1 17 ? 13.893 40.122 23.548 1.00 17.59 ? 17 LEU B O 1 ATOM 947 C CB . LEU B 1 17 ? 15.550 41.950 25.646 1.00 20.16 ? 17 LEU B CB 1 ATOM 948 C CG . LEU B 1 17 ? 16.483 42.229 26.826 1.00 23.71 ? 17 LEU B CG 1 ATOM 949 C CD1 . LEU B 1 17 ? 17.387 43.408 26.466 1.00 23.43 ? 17 LEU B CD1 1 ATOM 950 C CD2 . LEU B 1 17 ? 15.670 42.553 28.082 1.00 24.47 ? 17 LEU B CD2 1 ATOM 951 N N . ASP B 1 18 ? 12.598 41.646 24.597 1.00 17.71 ? 18 ASP B N 1 ATOM 952 C CA . ASP B 1 18 ? 11.621 41.808 23.529 1.00 17.89 ? 18 ASP B CA 1 ATOM 953 C C . ASP B 1 18 ? 11.887 43.150 22.839 1.00 17.75 ? 18 ASP B C 1 ATOM 954 O O . ASP B 1 18 ? 11.708 44.205 23.448 1.00 17.40 ? 18 ASP B O 1 ATOM 955 C CB . ASP B 1 18 ? 10.226 41.799 24.151 1.00 18.86 ? 18 ASP B CB 1 ATOM 956 C CG . ASP B 1 18 ? 9.116 41.905 23.128 1.00 20.10 ? 18 ASP B CG 1 ATOM 957 O OD1 . ASP B 1 18 ? 9.287 42.612 22.118 1.00 18.95 ? 18 ASP B OD1 1 ATOM 958 O OD2 . ASP B 1 18 ? 8.056 41.288 23.359 1.00 20.90 ? 18 ASP B OD2 1 ATOM 959 N N . ALA B 1 19 ? 12.306 43.103 21.572 1.00 16.31 ? 19 ALA B N 1 ATOM 960 C CA . ALA B 1 19 ? 12.613 44.309 20.801 1.00 17.46 ? 19 ALA B CA 1 ATOM 961 C C . ALA B 1 19 ? 11.386 45.045 20.266 1.00 20.29 ? 19 ALA B C 1 ATOM 962 O O . ALA B 1 19 ? 11.492 46.179 19.791 1.00 23.26 ? 19 ALA B O 1 ATOM 963 C CB . ALA B 1 19 ? 13.534 43.956 19.634 1.00 17.36 ? 19 ALA B CB 1 ATOM 964 N N . VAL B 1 20 ? 10.226 44.400 20.321 1.00 20.12 ? 20 VAL B N 1 ATOM 965 C CA . VAL B 1 20 ? 9.002 45.018 19.829 1.00 19.09 ? 20 VAL B CA 1 ATOM 966 C C . VAL B 1 20 ? 8.319 45.841 20.915 1.00 20.72 ? 20 VAL B C 1 ATOM 967 O O . VAL B 1 20 ? 7.789 46.915 20.644 1.00 20.58 ? 20 VAL B O 1 ATOM 968 C CB . VAL B 1 20 ? 7.996 43.953 19.324 1.00 20.01 ? 20 VAL B CB 1 ATOM 969 C CG1 . VAL B 1 20 ? 6.671 44.616 18.954 1.00 23.01 ? 20 VAL B CG1 1 ATOM 970 C CG2 . VAL B 1 20 ? 8.572 43.219 18.115 1.00 21.51 ? 20 VAL B CG2 1 ATOM 971 N N . ARG B 1 21 ? 8.345 45.331 22.143 1.00 21.16 ? 21 ARG B N 1 ATOM 972 C CA . ARG B 1 21 ? 7.693 46.006 23.258 1.00 22.31 ? 21 ARG B CA 1 ATOM 973 C C . ARG B 1 21 ? 8.641 46.760 24.185 1.00 21.07 ? 21 ARG B C 1 ATOM 974 O O . ARG B 1 21 ? 8.192 47.507 25.056 1.00 22.17 ? 21 ARG B O 1 ATOM 975 C CB . ARG B 1 21 ? 6.875 44.988 24.057 1.00 25.28 ? 21 ARG B CB 1 ATOM 976 C CG . ARG B 1 21 ? 5.888 44.208 23.193 1.00 30.85 ? 21 ARG B CG 1 ATOM 977 C CD . ARG B 1 21 ? 4.852 43.471 24.022 1.00 35.31 ? 21 ARG B CD 1 ATOM 978 N NE . ARG B 1 21 ? 5.384 42.342 24.748 1.00 40.20 ? 21 ARG B NE 1 ATOM 979 C CZ . ARG B 1 21 ? 4.843 41.752 25.809 1.00 43.32 ? 21 ARG B CZ 1 ATOM 980 N NH1 . ARG B 1 21 ? 5.481 40.717 26.322 1.00 44.76 ? 21 ARG B NH1 1 ATOM 981 N NH2 . ARG B 1 21 ? 3.716 42.177 26.374 1.00 45.23 ? 21 ARG B NH2 1 ATOM 982 N N . GLY B 1 22 ? 9.944 46.571 23.996 1.00 22.56 ? 22 GLY B N 1 ATOM 983 C CA . GLY B 1 22 ? 10.923 47.251 24.835 1.00 19.78 ? 22 GLY B CA 1 ATOM 984 C C . GLY B 1 22 ? 10.837 46.780 26.278 1.00 22.41 ? 22 GLY B C 1 ATOM 985 O O . GLY B 1 22 ? 10.871 47.572 27.224 1.00 18.82 ? 22 GLY B O 1 ATOM 986 N N . SER B 1 23 ? 10.734 45.471 26.450 1.00 20.82 ? 23 SER B N 1 ATOM 987 C CA . SER B 1 23 ? 10.628 44.902 27.780 1.00 21.41 ? 23 SER B CA 1 ATOM 988 C C . SER B 1 23 ? 11.283 43.537 27.850 1.00 20.98 ? 23 SER B C 1 ATOM 989 O O . SER B 1 23 ? 11.679 42.959 26.827 1.00 19.12 ? 23 SER B O 1 ATOM 990 C CB . SER B 1 23 ? 9.158 44.761 28.160 1.00 25.78 ? 23 SER B CB 1 ATOM 991 O OG . SER B 1 23 ? 8.527 43.824 27.309 1.00 31.38 ? 23 SER B OG 1 ATOM 992 N N . PRO B 1 24 ? 11.420 42.999 29.069 1.00 21.82 ? 24 PRO B N 1 ATOM 993 C CA . PRO B 1 24 ? 12.034 41.679 29.194 1.00 19.92 ? 24 PRO B CA 1 ATOM 994 C C . PRO B 1 24 ? 11.043 40.694 28.589 1.00 19.74 ? 24 PRO B C 1 ATOM 995 O O . PRO B 1 24 ? 9.839 40.962 28.567 1.00 21.08 ? 24 PRO B O 1 ATOM 996 C CB . PRO B 1 24 ? 12.161 41.497 30.707 1.00 24.40 ? 24 PRO B CB 1 ATOM 997 C CG . PRO B 1 24 ? 12.238 42.909 31.227 1.00 25.98 ? 24 PRO B CG 1 ATOM 998 C CD . PRO B 1 24 ? 11.207 43.613 30.392 1.00 21.57 ? 24 PRO B CD 1 ATOM 999 N N . ALA B 1 25 ? 11.541 39.575 28.077 1.00 17.13 ? 25 ALA B N 1 ATOM 1000 C CA . ALA B 1 25 ? 10.663 38.559 27.503 1.00 18.72 ? 25 ALA B CA 1 ATOM 1001 C C . ALA B 1 25 ? 10.352 37.617 28.662 1.00 19.81 ? 25 ALA B C 1 ATOM 1002 O O . ALA B 1 25 ? 11.190 36.820 29.074 1.00 18.75 ? 25 ALA B O 1 ATOM 1003 C CB . ALA B 1 25 ? 11.369 37.817 26.371 1.00 17.90 ? 25 ALA B CB 1 ATOM 1004 N N . ILE B 1 26 ? 9.140 37.726 29.186 1.00 19.95 ? 26 ILE B N 1 ATOM 1005 C CA . ILE B 1 26 ? 8.719 36.939 30.338 1.00 21.43 ? 26 ILE B CA 1 ATOM 1006 C C . ILE B 1 26 ? 8.072 35.600 30.005 1.00 19.92 ? 26 ILE B C 1 ATOM 1007 O O . ILE B 1 26 ? 7.382 35.460 28.996 1.00 18.80 ? 26 ILE B O 1 ATOM 1008 C CB . ILE B 1 26 ? 7.759 37.779 31.208 1.00 23.29 ? 26 ILE B CB 1 ATOM 1009 C CG1 . ILE B 1 26 ? 8.435 39.113 31.551 1.00 24.43 ? 26 ILE B CG1 1 ATOM 1010 C CG2 . ILE B 1 26 ? 7.389 37.024 32.485 1.00 26.16 ? 26 ILE B CG2 1 ATOM 1011 C CD1 . ILE B 1 26 ? 7.546 40.090 32.292 1.00 29.85 ? 26 ILE B CD1 1 ATOM 1012 N N . ASN B 1 27 ? 8.315 34.619 30.869 1.00 21.24 ? 27 ASN B N 1 ATOM 1013 C CA . ASN B 1 27 ? 7.765 33.279 30.715 1.00 25.72 ? 27 ASN B CA 1 ATOM 1014 C C . ASN B 1 27 ? 8.159 32.563 29.438 1.00 24.55 ? 27 ASN B C 1 ATOM 1015 O O . ASN B 1 27 ? 7.365 31.814 28.869 1.00 26.05 ? 27 ASN B O 1 ATOM 1016 C CB . ASN B 1 27 ? 6.246 33.322 30.817 1.00 31.34 ? 27 ASN B CB 1 ATOM 1017 C CG . ASN B 1 27 ? 5.766 33.123 32.228 1.00 38.35 ? 27 ASN B CG 1 ATOM 1018 O OD1 . ASN B 1 27 ? 6.013 32.078 32.831 1.00 41.89 ? 27 ASN B OD1 1 ATOM 1019 N ND2 . ASN B 1 27 ? 5.081 34.122 32.771 1.00 41.37 ? 27 ASN B ND2 1 ATOM 1020 N N . VAL B 1 28 ? 9.386 32.787 28.992 1.00 21.72 ? 28 VAL B N 1 ATOM 1021 C CA . VAL B 1 28 ? 9.872 32.142 27.785 1.00 22.03 ? 28 VAL B CA 1 ATOM 1022 C C . VAL B 1 28 ? 10.528 30.844 28.210 1.00 18.75 ? 28 VAL B C 1 ATOM 1023 O O . VAL B 1 28 ? 11.373 30.828 29.105 1.00 18.67 ? 28 VAL B O 1 ATOM 1024 C CB . VAL B 1 28 ? 10.914 33.011 27.050 1.00 20.90 ? 28 VAL B CB 1 ATOM 1025 C CG1 . VAL B 1 28 ? 11.432 32.265 25.823 1.00 23.54 ? 28 VAL B CG1 1 ATOM 1026 C CG2 . VAL B 1 28 ? 10.297 34.332 26.638 1.00 26.32 ? 28 VAL B CG2 1 ATOM 1027 N N . ALA B 1 29 ? 10.137 29.752 27.567 1.00 17.81 ? 29 ALA B N 1 ATOM 1028 C CA . ALA B 1 29 ? 10.700 28.456 27.895 1.00 18.20 ? 29 ALA B CA 1 ATOM 1029 C C . ALA B 1 29 ? 12.103 28.341 27.318 1.00 19.21 ? 29 ALA B C 1 ATOM 1030 O O . ALA B 1 29 ? 12.346 28.724 26.172 1.00 19.01 ? 29 ALA B O 1 ATOM 1031 C CB . ALA B 1 29 ? 9.810 27.348 27.348 1.00 18.21 ? 29 ALA B CB 1 ATOM 1032 N N . VAL B 1 30 ? 13.018 27.825 28.131 1.00 17.89 ? 30 VAL B N 1 ATOM 1033 C CA . VAL B 1 30 ? 14.403 27.631 27.741 1.00 18.18 ? 30 VAL B CA 1 ATOM 1034 C C . VAL B 1 30 ? 14.827 26.213 28.101 1.00 19.18 ? 30 VAL B C 1 ATOM 1035 O O . VAL B 1 30 ? 14.625 25.767 29.236 1.00 19.68 ? 30 VAL B O 1 ATOM 1036 C CB . VAL B 1 30 ? 15.345 28.607 28.487 1.00 17.64 ? 30 VAL B CB 1 ATOM 1037 C CG1 . VAL B 1 30 ? 16.791 28.327 28.114 1.00 18.05 ? 30 VAL B CG1 1 ATOM 1038 C CG2 . VAL B 1 30 ? 14.977 30.054 28.146 1.00 19.29 ? 30 VAL B CG2 1 ATOM 1039 N N . HIS B 1 31 ? 15.399 25.505 27.133 1.00 19.01 ? 31 HIS B N 1 ATOM 1040 C CA . HIS B 1 31 ? 15.881 24.149 27.353 1.00 20.17 ? 31 HIS B CA 1 ATOM 1041 C C . HIS B 1 31 ? 17.371 24.115 27.042 1.00 19.40 ? 31 HIS B C 1 ATOM 1042 O O . HIS B 1 31 ? 17.819 24.642 26.020 1.00 21.58 ? 31 HIS B O 1 ATOM 1043 C CB . HIS B 1 31 ? 15.153 23.152 26.450 1.00 20.01 ? 31 HIS B CB 1 ATOM 1044 C CG . HIS B 1 31 ? 13.718 22.941 26.810 1.00 23.50 ? 31 HIS B CG 1 ATOM 1045 N ND1 . HIS B 1 31 ? 12.738 23.872 26.539 1.00 27.29 ? 31 HIS B ND1 1 ATOM 1046 C CD2 . HIS B 1 31 ? 13.099 21.915 27.441 1.00 24.47 ? 31 HIS B CD2 1 ATOM 1047 C CE1 . HIS B 1 31 ? 11.578 23.431 26.989 1.00 25.56 ? 31 HIS B CE1 1 ATOM 1048 N NE2 . HIS B 1 31 ? 11.769 22.245 27.541 1.00 27.65 ? 31 HIS B NE2 1 ATOM 1049 N N . VAL B 1 32 ? 18.143 23.512 27.934 1.00 18.77 ? 32 VAL B N 1 ATOM 1050 C CA . VAL B 1 32 ? 19.580 23.409 27.730 1.00 19.12 ? 32 VAL B CA 1 ATOM 1051 C C . VAL B 1 32 ? 19.915 21.938 27.545 1.00 19.74 ? 32 VAL B C 1 ATOM 1052 O O . VAL B 1 32 ? 19.355 21.076 28.233 1.00 20.81 ? 32 VAL B O 1 ATOM 1053 C CB . VAL B 1 32 ? 20.360 23.956 28.939 1.00 16.97 ? 32 VAL B CB 1 ATOM 1054 C CG1 . VAL B 1 32 ? 21.853 23.919 28.656 1.00 15.93 ? 32 VAL B CG1 1 ATOM 1055 C CG2 . VAL B 1 32 ? 19.905 25.374 29.249 1.00 20.09 ? 32 VAL B CG2 1 ATOM 1056 N N . PHE B 1 33 ? 20.814 21.656 26.610 1.00 19.86 ? 33 PHE B N 1 ATOM 1057 C CA . PHE B 1 33 ? 21.231 20.289 26.327 1.00 21.08 ? 33 PHE B CA 1 ATOM 1058 C C . PHE B 1 33 ? 22.745 20.227 26.293 1.00 23.33 ? 33 PHE B C 1 ATOM 1059 O O . PHE B 1 33 ? 23.418 21.232 26.040 1.00 22.80 ? 33 PHE B O 1 ATOM 1060 C CB . PHE B 1 33 ? 20.711 19.816 24.961 1.00 22.55 ? 33 PHE B CB 1 ATOM 1061 C CG . PHE B 1 33 ? 19.230 19.978 24.775 1.00 25.17 ? 33 PHE B CG 1 ATOM 1062 C CD1 . PHE B 1 33 ? 18.693 21.204 24.390 1.00 23.75 ? 33 PHE B CD1 1 ATOM 1063 C CD2 . PHE B 1 33 ? 18.371 18.902 24.975 1.00 24.34 ? 33 PHE B CD2 1 ATOM 1064 C CE1 . PHE B 1 33 ? 17.320 21.359 24.203 1.00 25.43 ? 33 PHE B CE1 1 ATOM 1065 C CE2 . PHE B 1 33 ? 16.990 19.044 24.791 1.00 26.22 ? 33 PHE B CE2 1 ATOM 1066 C CZ . PHE B 1 33 ? 16.466 20.272 24.405 1.00 28.08 ? 33 PHE B CZ 1 ATOM 1067 N N . ARG B 1 34 ? 23.274 19.039 26.555 1.00 25.27 ? 34 ARG B N 1 ATOM 1068 C CA . ARG B 1 34 ? 24.707 18.817 26.520 1.00 25.62 ? 34 ARG B CA 1 ATOM 1069 C C . ARG B 1 34 ? 24.955 17.682 25.531 1.00 26.32 ? 34 ARG B C 1 ATOM 1070 O O . ARG B 1 34 ? 24.227 16.687 25.524 1.00 29.42 ? 34 ARG B O 1 ATOM 1071 C CB . ARG B 1 34 ? 25.231 18.435 27.909 1.00 25.48 ? 34 ARG B CB 1 ATOM 1072 C CG . ARG B 1 34 ? 26.726 18.170 27.924 1.00 30.70 ? 34 ARG B CG 1 ATOM 1073 C CD . ARG B 1 34 ? 27.280 18.015 29.332 1.00 33.79 ? 34 ARG B CD 1 ATOM 1074 N NE . ARG B 1 34 ? 28.734 17.861 29.307 1.00 38.07 ? 34 ARG B NE 1 ATOM 1075 C CZ . ARG B 1 34 ? 29.364 16.780 28.856 1.00 39.72 ? 34 ARG B CZ 1 ATOM 1076 N NH1 . ARG B 1 34 ? 28.669 15.747 28.393 1.00 41.70 ? 34 ARG B NH1 1 ATOM 1077 N NH2 . ARG B 1 34 ? 30.689 16.736 28.858 1.00 40.80 ? 34 ARG B NH2 1 ATOM 1078 N N . LYS B 1 35 ? 25.970 17.837 24.689 1.00 27.15 ? 35 LYS B N 1 ATOM 1079 C CA . LYS B 1 35 ? 26.283 16.813 23.703 1.00 30.52 ? 35 LYS B CA 1 ATOM 1080 C C . LYS B 1 35 ? 26.866 15.602 24.419 1.00 31.13 ? 35 LYS B C 1 ATOM 1081 O O . LYS B 1 35 ? 27.855 15.717 25.147 1.00 28.96 ? 35 LYS B O 1 ATOM 1082 C CB . LYS B 1 35 ? 27.283 17.354 22.678 1.00 31.65 ? 35 LYS B CB 1 ATOM 1083 C CG . LYS B 1 35 ? 27.084 16.799 21.275 1.00 37.04 ? 35 LYS B CG 1 ATOM 1084 C CD . LYS B 1 35 ? 28.012 17.479 20.278 1.00 42.30 ? 35 LYS B CD 1 ATOM 1085 C CE . LYS B 1 35 ? 27.681 17.070 18.850 1.00 45.31 ? 35 LYS B CE 1 ATOM 1086 N NZ . LYS B 1 35 ? 26.278 17.423 18.490 1.00 45.15 ? 35 LYS B NZ 1 ATOM 1087 N N . ALA B 1 36 ? 26.237 14.446 24.216 1.00 34.04 ? 36 ALA B N 1 ATOM 1088 C CA . ALA B 1 36 ? 26.676 13.207 24.846 1.00 37.89 ? 36 ALA B CA 1 ATOM 1089 C C . ALA B 1 36 ? 27.792 12.538 24.053 1.00 39.96 ? 36 ALA B C 1 ATOM 1090 O O . ALA B 1 36 ? 28.124 12.968 22.948 1.00 38.98 ? 36 ALA B O 1 ATOM 1091 C CB . ALA B 1 36 ? 25.499 12.256 24.997 1.00 37.74 ? 36 ALA B CB 1 ATOM 1092 N N . ALA B 1 37 ? 28.356 11.477 24.624 1.00 43.95 ? 37 ALA B N 1 ATOM 1093 C CA . ALA B 1 37 ? 29.448 10.738 23.998 1.00 48.01 ? 37 ALA B CA 1 ATOM 1094 C C . ALA B 1 37 ? 29.116 10.205 22.606 1.00 49.64 ? 37 ALA B C 1 ATOM 1095 O O . ALA B 1 37 ? 30.015 9.943 21.807 1.00 50.43 ? 37 ALA B O 1 ATOM 1096 C CB . ALA B 1 37 ? 29.874 9.585 24.905 1.00 49.01 ? 37 ALA B CB 1 ATOM 1097 N N . ASP B 1 38 ? 27.830 10.049 22.312 1.00 51.77 ? 38 ASP B N 1 ATOM 1098 C CA . ASP B 1 38 ? 27.413 9.528 21.015 1.00 53.67 ? 38 ASP B CA 1 ATOM 1099 C C . ASP B 1 38 ? 26.831 10.589 20.083 1.00 53.79 ? 38 ASP B C 1 ATOM 1100 O O . ASP B 1 38 ? 25.946 10.299 19.276 1.00 53.59 ? 38 ASP B O 1 ATOM 1101 C CB . ASP B 1 38 ? 26.394 8.402 21.212 1.00 56.05 ? 38 ASP B CB 1 ATOM 1102 C CG . ASP B 1 38 ? 25.116 8.883 21.867 1.00 58.39 ? 38 ASP B CG 1 ATOM 1103 O OD1 . ASP B 1 38 ? 25.202 9.548 22.921 1.00 59.25 ? 38 ASP B OD1 1 ATOM 1104 O OD2 . ASP B 1 38 ? 24.026 8.590 21.331 1.00 60.18 ? 38 ASP B OD2 1 ATOM 1105 N N . ASP B 1 39 ? 27.331 11.816 20.196 1.00 53.36 ? 39 ASP B N 1 ATOM 1106 C CA . ASP B 1 39 ? 26.874 12.918 19.353 1.00 52.72 ? 39 ASP B CA 1 ATOM 1107 C C . ASP B 1 39 ? 25.386 13.218 19.492 1.00 49.91 ? 39 ASP B C 1 ATOM 1108 O O . ASP B 1 39 ? 24.793 13.851 18.620 1.00 51.41 ? 39 ASP B O 1 ATOM 1109 C CB . ASP B 1 39 ? 27.188 12.622 17.883 1.00 55.62 ? 39 ASP B CB 1 ATOM 1110 C CG . ASP B 1 39 ? 28.676 12.537 17.611 1.00 59.19 ? 39 ASP B CG 1 ATOM 1111 O OD1 . ASP B 1 39 ? 29.376 13.550 17.826 1.00 60.48 ? 39 ASP B OD1 1 ATOM 1112 O OD2 . ASP B 1 39 ? 29.143 11.459 17.181 1.00 60.65 ? 39 ASP B OD2 1 ATOM 1113 N N . THR B 1 40 ? 24.784 12.766 20.587 1.00 46.00 ? 40 THR B N 1 ATOM 1114 C CA . THR B 1 40 ? 23.362 12.998 20.826 1.00 42.81 ? 40 THR B CA 1 ATOM 1115 C C . THR B 1 40 ? 23.164 14.117 21.850 1.00 39.42 ? 40 THR B C 1 ATOM 1116 O O . THR B 1 40 ? 23.997 14.312 22.733 1.00 37.61 ? 40 THR B O 1 ATOM 1117 C CB . THR B 1 40 ? 22.672 11.716 21.346 1.00 42.60 ? 40 THR B CB 1 ATOM 1118 O OG1 . THR B 1 40 ? 22.733 10.704 20.335 1.00 48.55 ? 40 THR B OG1 1 ATOM 1119 C CG2 . THR B 1 40 ? 21.215 11.985 21.688 1.00 44.61 ? 40 THR B CG2 1 ATOM 1120 N N . TRP B 1 41 ? 22.064 14.852 21.723 1.00 34.56 ? 41 TRP B N 1 ATOM 1121 C CA . TRP B 1 41 ? 21.765 15.935 22.652 1.00 33.46 ? 41 TRP B CA 1 ATOM 1122 C C . TRP B 1 41 ? 20.928 15.410 23.812 1.00 34.54 ? 41 TRP B C 1 ATOM 1123 O O . TRP B 1 41 ? 19.781 15.009 23.622 1.00 36.99 ? 41 TRP B O 1 ATOM 1124 C CB . TRP B 1 41 ? 20.985 17.055 21.955 1.00 32.62 ? 41 TRP B CB 1 ATOM 1125 C CG . TRP B 1 41 ? 21.787 17.874 20.988 1.00 31.04 ? 41 TRP B CG 1 ATOM 1126 C CD1 . TRP B 1 41 ? 21.613 17.948 19.632 1.00 32.82 ? 41 TRP B CD1 1 ATOM 1127 C CD2 . TRP B 1 41 ? 22.872 18.755 21.302 1.00 31.06 ? 41 TRP B CD2 1 ATOM 1128 N NE1 . TRP B 1 41 ? 22.521 18.820 19.086 1.00 33.13 ? 41 TRP B NE1 1 ATOM 1129 C CE2 . TRP B 1 41 ? 23.308 19.330 20.087 1.00 31.38 ? 41 TRP B CE2 1 ATOM 1130 C CE3 . TRP B 1 41 ? 23.519 19.116 22.495 1.00 28.27 ? 41 TRP B CE3 1 ATOM 1131 C CZ2 . TRP B 1 41 ? 24.365 20.246 20.027 1.00 29.11 ? 41 TRP B CZ2 1 ATOM 1132 C CZ3 . TRP B 1 41 ? 24.571 20.028 22.435 1.00 28.82 ? 41 TRP B CZ3 1 ATOM 1133 C CH2 . TRP B 1 41 ? 24.983 20.582 21.207 1.00 28.65 ? 41 TRP B CH2 1 ATOM 1134 N N . GLU B 1 42 ? 21.490 15.405 25.013 1.00 32.50 ? 42 GLU B N 1 ATOM 1135 C CA . GLU B 1 42 ? 20.733 14.935 26.162 1.00 33.00 ? 42 GLU B CA 1 ATOM 1136 C C . GLU B 1 42 ? 20.321 16.116 27.033 1.00 29.94 ? 42 GLU B C 1 ATOM 1137 O O . GLU B 1 42 ? 21.081 17.070 27.210 1.00 28.07 ? 42 GLU B O 1 ATOM 1138 C CB . GLU B 1 42 ? 21.546 13.927 26.982 1.00 36.34 ? 42 GLU B CB 1 ATOM 1139 C CG . GLU B 1 42 ? 22.863 14.446 27.524 1.00 43.75 ? 42 GLU B CG 1 ATOM 1140 C CD . GLU B 1 42 ? 23.588 13.405 28.359 1.00 48.00 ? 42 GLU B CD 1 ATOM 1141 O OE1 . GLU B 1 42 ? 23.895 12.318 27.824 1.00 49.55 ? 42 GLU B OE1 1 ATOM 1142 O OE2 . GLU B 1 42 ? 23.849 13.675 29.550 1.00 49.65 ? 42 GLU B OE2 1 ATOM 1143 N N . PRO B 1 43 ? 19.093 16.075 27.570 1.00 28.31 ? 43 PRO B N 1 ATOM 1144 C CA . PRO B 1 43 ? 18.557 17.133 28.430 1.00 27.23 ? 43 PRO B CA 1 ATOM 1145 C C . PRO B 1 43 ? 19.526 17.440 29.559 1.00 27.40 ? 43 PRO B C 1 ATOM 1146 O O . PRO B 1 43 ? 20.075 16.527 30.178 1.00 28.63 ? 43 PRO B O 1 ATOM 1147 C CB . PRO B 1 43 ? 17.255 16.528 28.941 1.00 28.89 ? 43 PRO B CB 1 ATOM 1148 C CG . PRO B 1 43 ? 16.811 15.689 27.784 1.00 29.10 ? 43 PRO B CG 1 ATOM 1149 C CD . PRO B 1 43 ? 18.095 15.009 27.369 1.00 30.30 ? 43 PRO B CD 1 ATOM 1150 N N . PHE B 1 44 ? 19.733 18.725 29.826 1.00 25.48 ? 44 PHE B N 1 ATOM 1151 C CA . PHE B 1 44 ? 20.650 19.139 30.878 1.00 24.07 ? 44 PHE B CA 1 ATOM 1152 C C . PHE B 1 44 ? 19.926 19.956 31.943 1.00 23.07 ? 44 PHE B C 1 ATOM 1153 O O . PHE B 1 44 ? 20.079 19.714 33.142 1.00 23.80 ? 44 PHE B O 1 ATOM 1154 C CB . PHE B 1 44 ? 21.796 19.958 30.273 1.00 24.05 ? 44 PHE B CB 1 ATOM 1155 C CG . PHE B 1 44 ? 22.843 20.368 31.267 1.00 23.60 ? 44 PHE B CG 1 ATOM 1156 C CD1 . PHE B 1 44 ? 23.718 19.428 31.806 1.00 25.99 ? 44 PHE B CD1 1 ATOM 1157 C CD2 . PHE B 1 44 ? 22.947 21.695 31.675 1.00 23.17 ? 44 PHE B CD2 1 ATOM 1158 C CE1 . PHE B 1 44 ? 24.687 19.808 32.740 1.00 24.20 ? 44 PHE B CE1 1 ATOM 1159 C CE2 . PHE B 1 44 ? 23.909 22.084 32.607 1.00 24.63 ? 44 PHE B CE2 1 ATOM 1160 C CZ . PHE B 1 44 ? 24.781 21.139 33.140 1.00 25.09 ? 44 PHE B CZ 1 ATOM 1161 N N . ALA B 1 45 ? 19.135 20.926 31.496 1.00 21.64 ? 45 ALA B N 1 ATOM 1162 C CA . ALA B 1 45 ? 18.381 21.787 32.398 1.00 21.92 ? 45 ALA B CA 1 ATOM 1163 C C . ALA B 1 45 ? 17.350 22.572 31.600 1.00 19.74 ? 45 ALA B C 1 ATOM 1164 O O . ALA B 1 45 ? 17.442 22.667 30.378 1.00 21.68 ? 45 ALA B O 1 ATOM 1165 C CB . ALA B 1 45 ? 19.326 22.744 33.119 1.00 21.08 ? 45 ALA B CB 1 ATOM 1166 N N . SER B 1 46 ? 16.361 23.126 32.289 1.00 18.80 ? 46 SER B N 1 ATOM 1167 C CA . SER B 1 46 ? 15.325 23.907 31.624 1.00 20.64 ? 46 SER B CA 1 ATOM 1168 C C . SER B 1 46 ? 14.599 24.790 32.617 1.00 21.64 ? 46 SER B C 1 ATOM 1169 O O . SER B 1 46 ? 14.710 24.607 33.827 1.00 25.02 ? 46 SER B O 1 ATOM 1170 C CB . SER B 1 46 ? 14.311 22.994 30.920 1.00 16.93 ? 46 SER B CB 1 ATOM 1171 O OG . SER B 1 46 ? 13.645 22.132 31.835 1.00 18.95 ? 46 SER B OG 1 ATOM 1172 N N . GLY B 1 47 ? 13.850 25.750 32.094 1.00 23.12 ? 47 GLY B N 1 ATOM 1173 C CA . GLY B 1 47 ? 13.110 26.653 32.946 1.00 23.62 ? 47 GLY B CA 1 ATOM 1174 C C . GLY B 1 47 ? 12.424 27.707 32.107 1.00 23.13 ? 47 GLY B C 1 ATOM 1175 O O . GLY B 1 47 ? 12.416 27.626 30.875 1.00 22.37 ? 47 GLY B O 1 ATOM 1176 N N . LYS B 1 48 ? 11.838 28.688 32.781 1.00 21.09 ? 48 LYS B N 1 ATOM 1177 C CA . LYS B 1 48 ? 11.151 29.789 32.122 1.00 22.71 ? 48 LYS B CA 1 ATOM 1178 C C . LYS B 1 48 ? 11.696 31.099 32.657 1.00 22.14 ? 48 LYS B C 1 ATOM 1179 O O . LYS B 1 48 ? 11.992 31.206 33.850 1.00 22.20 ? 48 LYS B O 1 ATOM 1180 C CB . LYS B 1 48 ? 9.648 29.713 32.384 1.00 25.54 ? 48 LYS B CB 1 ATOM 1181 C CG . LYS B 1 48 ? 8.937 28.664 31.563 1.00 31.26 ? 48 LYS B CG 1 ATOM 1182 C CD . LYS B 1 48 ? 7.454 28.636 31.879 1.00 37.51 ? 48 LYS B CD 1 ATOM 1183 C CE . LYS B 1 48 ? 6.694 27.848 30.827 1.00 39.58 ? 48 LYS B CE 1 ATOM 1184 N NZ . LYS B 1 48 ? 6.750 28.521 29.495 1.00 42.26 ? 48 LYS B NZ 1 ATOM 1185 N N . THR B 1 49 ? 11.836 32.091 31.779 1.00 18.90 ? 49 THR B N 1 ATOM 1186 C CA . THR B 1 49 ? 12.348 33.389 32.194 1.00 19.86 ? 49 THR B CA 1 ATOM 1187 C C . THR B 1 49 ? 11.407 34.054 33.193 1.00 21.74 ? 49 THR B C 1 ATOM 1188 O O . THR B 1 49 ? 10.185 33.884 33.127 1.00 21.61 ? 49 THR B O 1 ATOM 1189 C CB . THR B 1 49 ? 12.539 34.327 30.990 1.00 17.75 ? 49 THR B CB 1 ATOM 1190 O OG1 . THR B 1 49 ? 11.299 34.465 30.278 1.00 18.09 ? 49 THR B OG1 1 ATOM 1191 C CG2 . THR B 1 49 ? 13.606 33.768 30.056 1.00 17.40 ? 49 THR B CG2 1 ATOM 1192 N N . SER B 1 50 ? 11.992 34.809 34.116 1.00 24.79 ? 50 SER B N 1 ATOM 1193 C CA . SER B 1 50 ? 11.241 35.510 35.146 1.00 25.89 ? 50 SER B CA 1 ATOM 1194 C C . SER B 1 50 ? 10.690 36.819 34.606 1.00 27.07 ? 50 SER B C 1 ATOM 1195 O O . SER B 1 50 ? 10.804 37.112 33.413 1.00 25.18 ? 50 SER B O 1 ATOM 1196 C CB . SER B 1 50 ? 12.151 35.818 36.333 1.00 27.06 ? 50 SER B CB 1 ATOM 1197 O OG . SER B 1 50 ? 13.130 36.773 35.957 1.00 29.55 ? 50 SER B OG 1 ATOM 1198 N N . GLU B 1 51 ? 10.101 37.608 35.499 1.00 26.85 ? 51 GLU B N 1 ATOM 1199 C CA . GLU B 1 51 ? 9.533 38.899 35.130 1.00 28.78 ? 51 GLU B CA 1 ATOM 1200 C C . GLU B 1 51 ? 10.614 39.869 34.659 1.00 27.17 ? 51 GLU B C 1 ATOM 1201 O O . GLU B 1 51 ? 10.318 40.879 34.026 1.00 28.56 ? 51 GLU B O 1 ATOM 1202 C CB . GLU B 1 51 ? 8.760 39.490 36.316 1.00 30.88 ? 51 GLU B CB 1 ATOM 1203 C CG . GLU B 1 51 ? 7.470 38.745 36.611 1.00 38.62 ? 51 GLU B CG 1 ATOM 1204 C CD . GLU B 1 51 ? 6.700 39.320 37.785 1.00 44.23 ? 51 GLU B CD 1 ATOM 1205 O OE1 . GLU B 1 51 ? 5.626 38.769 38.109 1.00 48.05 ? 51 GLU B OE1 1 ATOM 1206 O OE2 . GLU B 1 51 ? 7.167 40.314 38.386 1.00 46.63 ? 51 GLU B OE2 1 ATOM 1207 N N . SER B 1 52 ? 11.868 39.558 34.966 1.00 25.26 ? 52 SER B N 1 ATOM 1208 C CA . SER B 1 52 ? 12.981 40.401 34.549 1.00 26.89 ? 52 SER B CA 1 ATOM 1209 C C . SER B 1 52 ? 13.589 39.833 33.264 1.00 25.34 ? 52 SER B C 1 ATOM 1210 O O . SER B 1 52 ? 14.604 40.326 32.771 1.00 23.59 ? 52 SER B O 1 ATOM 1211 C CB . SER B 1 52 ? 14.045 40.460 35.646 1.00 29.30 ? 52 SER B CB 1 ATOM 1212 O OG . SER B 1 52 ? 14.626 39.184 35.864 1.00 34.85 ? 52 SER B OG 1 ATOM 1213 N N . GLY B 1 53 ? 12.956 38.787 32.736 1.00 23.48 ? 53 GLY B N 1 ATOM 1214 C CA . GLY B 1 53 ? 13.421 38.156 31.513 1.00 21.38 ? 53 GLY B CA 1 ATOM 1215 C C . GLY B 1 53 ? 14.674 37.329 31.717 1.00 22.91 ? 53 GLY B C 1 ATOM 1216 O O . GLY B 1 53 ? 15.373 37.001 30.758 1.00 23.43 ? 53 GLY B O 1 ATOM 1217 N N . GLU B 1 54 ? 14.955 36.974 32.967 1.00 24.47 ? 54 GLU B N 1 ATOM 1218 C CA . GLU B 1 54 ? 16.147 36.206 33.280 1.00 24.98 ? 54 GLU B CA 1 ATOM 1219 C C . GLU B 1 54 ? 15.838 34.805 33.783 1.00 24.67 ? 54 GLU B C 1 ATOM 1220 O O . GLU B 1 54 ? 14.745 34.521 34.288 1.00 25.87 ? 54 GLU B O 1 ATOM 1221 C CB . GLU B 1 54 ? 16.989 36.936 34.334 1.00 26.53 ? 54 GLU B CB 1 ATOM 1222 C CG . GLU B 1 54 ? 17.240 38.407 34.045 1.00 34.25 ? 54 GLU B CG 1 ATOM 1223 C CD . GLU B 1 54 ? 18.050 39.085 35.136 1.00 38.36 ? 54 GLU B CD 1 ATOM 1224 O OE1 . GLU B 1 54 ? 17.689 38.942 36.323 1.00 42.35 ? 54 GLU B OE1 1 ATOM 1225 O OE2 . GLU B 1 54 ? 19.042 39.767 34.808 1.00 43.37 ? 54 GLU B OE2 1 ATOM 1226 N N . LEU B 1 55 ? 16.819 33.929 33.633 1.00 23.34 ? 55 LEU B N 1 ATOM 1227 C CA . LEU B 1 55 ? 16.697 32.556 34.088 1.00 24.16 ? 55 LEU B CA 1 ATOM 1228 C C . LEU B 1 55 ? 18.010 32.206 34.767 1.00 25.35 ? 55 LEU B C 1 ATOM 1229 O O . LEU B 1 55 ? 19.055 32.141 34.121 1.00 25.01 ? 55 LEU B O 1 ATOM 1230 C CB . LEU B 1 55 ? 16.427 31.620 32.905 1.00 25.00 ? 55 LEU B CB 1 ATOM 1231 C CG . LEU B 1 55 ? 16.330 30.125 33.209 1.00 24.85 ? 55 LEU B CG 1 ATOM 1232 C CD1 . LEU B 1 55 ? 15.281 29.867 34.288 1.00 27.87 ? 55 LEU B CD1 1 ATOM 1233 C CD2 . LEU B 1 55 ? 15.985 29.381 31.932 1.00 26.10 ? 55 LEU B CD2 1 ATOM 1234 N N . HIS B 1 56 ? 17.949 32.018 36.081 1.00 27.35 ? 56 HIS B N 1 ATOM 1235 C CA . HIS B 1 56 ? 19.120 31.684 36.882 1.00 30.53 ? 56 HIS B CA 1 ATOM 1236 C C . HIS B 1 56 ? 18.931 30.312 37.523 1.00 29.40 ? 56 HIS B C 1 ATOM 1237 O O . HIS B 1 56 ? 17.837 29.750 37.506 1.00 29.77 ? 56 HIS B O 1 ATOM 1238 C CB . HIS B 1 56 ? 19.324 32.703 38.014 1.00 32.87 ? 56 HIS B CB 1 ATOM 1239 C CG . HIS B 1 56 ? 19.396 34.127 37.559 1.00 38.33 ? 56 HIS B CG 1 ATOM 1240 N ND1 . HIS B 1 56 ? 18.291 34.831 37.135 1.00 40.29 ? 56 HIS B ND1 1 ATOM 1241 C CD2 . HIS B 1 56 ? 20.440 34.987 37.491 1.00 38.78 ? 56 HIS B CD2 1 ATOM 1242 C CE1 . HIS B 1 56 ? 18.650 36.065 36.829 1.00 40.92 ? 56 HIS B CE1 1 ATOM 1243 N NE2 . HIS B 1 56 ? 19.949 36.186 37.036 1.00 40.57 ? 56 HIS B NE2 1 ATOM 1244 N N . GLY B 1 57 ? 20.006 29.788 38.100 1.00 29.82 ? 57 GLY B N 1 ATOM 1245 C CA . GLY B 1 57 ? 19.941 28.500 38.769 1.00 31.29 ? 57 GLY B CA 1 ATOM 1246 C C . GLY B 1 57 ? 19.708 27.305 37.870 1.00 29.50 ? 57 GLY B C 1 ATOM 1247 O O . GLY B 1 57 ? 19.060 26.341 38.275 1.00 29.53 ? 57 GLY B O 1 ATOM 1248 N N . LEU B 1 58 ? 20.231 27.359 36.650 1.00 28.24 ? 58 LEU B N 1 ATOM 1249 C CA . LEU B 1 58 ? 20.066 26.256 35.713 1.00 27.24 ? 58 LEU B CA 1 ATOM 1250 C C . LEU B 1 58 ? 20.970 25.103 36.091 1.00 27.36 ? 58 LEU B C 1 ATOM 1251 O O . LEU B 1 58 ? 20.599 23.941 35.946 1.00 25.26 ? 58 LEU B O 1 ATOM 1252 C CB . LEU B 1 58 ? 20.393 26.707 34.287 1.00 28.13 ? 58 LEU B CB 1 ATOM 1253 C CG . LEU B 1 58 ? 19.290 27.492 33.580 1.00 26.45 ? 58 LEU B CG 1 ATOM 1254 C CD1 . LEU B 1 58 ? 19.803 27.999 32.238 1.00 25.65 ? 58 LEU B CD1 1 ATOM 1255 C CD2 . LEU B 1 58 ? 18.072 26.596 33.390 1.00 26.56 ? 58 LEU B CD2 1 ATOM 1256 N N . THR B 1 59 ? 22.157 25.431 36.591 1.00 26.51 ? 59 THR B N 1 ATOM 1257 C CA . THR B 1 59 ? 23.117 24.410 36.972 1.00 27.61 ? 59 THR B CA 1 ATOM 1258 C C . THR B 1 59 ? 24.069 24.931 38.044 1.00 27.92 ? 59 THR B C 1 ATOM 1259 O O . THR B 1 59 ? 23.934 26.063 38.511 1.00 28.29 ? 59 THR B O 1 ATOM 1260 C CB . THR B 1 59 ? 23.933 23.964 35.740 1.00 27.43 ? 59 THR B CB 1 ATOM 1261 O OG1 . THR B 1 59 ? 24.823 22.905 36.102 1.00 28.65 ? 59 THR B OG1 1 ATOM 1262 C CG2 . THR B 1 59 ? 24.744 25.133 35.187 1.00 28.09 ? 59 THR B CG2 1 ATOM 1263 N N . THR B 1 60 ? 25.025 24.096 38.434 1.00 28.36 ? 60 THR B N 1 ATOM 1264 C CA . THR B 1 60 ? 26.015 24.466 39.440 1.00 29.16 ? 60 THR B CA 1 ATOM 1265 C C . THR B 1 60 ? 27.394 24.290 38.822 1.00 29.25 ? 60 THR B C 1 ATOM 1266 O O . THR B 1 60 ? 27.530 23.668 37.773 1.00 29.46 ? 60 THR B O 1 ATOM 1267 C CB . THR B 1 60 ? 25.921 23.567 40.693 1.00 29.84 ? 60 THR B CB 1 ATOM 1268 O OG1 . THR B 1 60 ? 26.116 22.197 40.316 1.00 28.09 ? 60 THR B OG1 1 ATOM 1269 C CG2 . THR B 1 60 ? 24.560 23.722 41.361 1.00 31.26 ? 60 THR B CG2 1 ATOM 1270 N N . GLU B 1 61 ? 28.417 24.830 39.470 1.00 30.00 ? 61 GLU B N 1 ATOM 1271 C CA . GLU B 1 61 ? 29.766 24.711 38.938 1.00 33.84 ? 61 GLU B CA 1 ATOM 1272 C C . GLU B 1 61 ? 30.214 23.255 38.844 1.00 32.87 ? 61 GLU B C 1 ATOM 1273 O O . GLU B 1 61 ? 30.903 22.872 37.898 1.00 32.28 ? 61 GLU B O 1 ATOM 1274 C CB . GLU B 1 61 ? 30.748 25.510 39.798 1.00 37.71 ? 61 GLU B CB 1 ATOM 1275 C CG . GLU B 1 61 ? 30.722 25.159 41.273 1.00 47.98 ? 61 GLU B CG 1 ATOM 1276 C CD . GLU B 1 61 ? 31.778 25.913 42.060 1.00 52.74 ? 61 GLU B CD 1 ATOM 1277 O OE1 . GLU B 1 61 ? 31.804 27.161 41.975 1.00 55.02 ? 61 GLU B OE1 1 ATOM 1278 O OE2 . GLU B 1 61 ? 32.581 25.260 42.761 1.00 56.46 ? 61 GLU B OE2 1 ATOM 1279 N N . GLU B 1 62 ? 29.812 22.442 39.816 1.00 31.79 ? 62 GLU B N 1 ATOM 1280 C CA . GLU B 1 62 ? 30.186 21.033 39.825 1.00 30.72 ? 62 GLU B CA 1 ATOM 1281 C C . GLU B 1 62 ? 29.608 20.254 38.645 1.00 29.49 ? 62 GLU B C 1 ATOM 1282 O O . GLU B 1 62 ? 30.293 19.426 38.047 1.00 29.09 ? 62 GLU B O 1 ATOM 1283 C CB . GLU B 1 62 ? 29.741 20.381 41.138 0.50 32.83 ? 62 GLU B CB 1 ATOM 1284 C CG . GLU B 1 62 ? 30.469 20.907 42.367 0.50 36.72 ? 62 GLU B CG 1 ATOM 1285 C CD . GLU B 1 62 ? 31.953 20.590 42.346 0.50 39.04 ? 62 GLU B CD 1 ATOM 1286 O OE1 . GLU B 1 62 ? 32.304 19.391 42.307 0.50 39.17 ? 62 GLU B OE1 1 ATOM 1287 O OE2 . GLU B 1 62 ? 32.769 21.536 42.368 0.50 40.91 ? 62 GLU B OE2 1 ATOM 1288 N N . GLN B 1 63 ? 28.353 20.530 38.305 1.00 26.61 ? 63 GLN B N 1 ATOM 1289 C CA . GLN B 1 63 ? 27.679 19.840 37.208 1.00 28.05 ? 63 GLN B CA 1 ATOM 1290 C C . GLN B 1 63 ? 28.031 20.378 35.815 1.00 25.39 ? 63 GLN B C 1 ATOM 1291 O O . GLN B 1 63 ? 28.031 19.634 34.834 1.00 24.43 ? 63 GLN B O 1 ATOM 1292 C CB . GLN B 1 63 ? 26.160 19.912 37.434 1.00 31.28 ? 63 GLN B CB 1 ATOM 1293 C CG . GLN B 1 63 ? 25.296 19.529 36.243 1.00 38.71 ? 63 GLN B CG 1 ATOM 1294 C CD . GLN B 1 63 ? 23.804 19.680 36.528 1.00 42.00 ? 63 GLN B CD 1 ATOM 1295 O OE1 . GLN B 1 63 ? 23.207 18.859 37.228 1.00 45.40 ? 63 GLN B OE1 1 ATOM 1296 N NE2 . GLN B 1 63 ? 23.200 20.738 35.994 1.00 42.50 ? 63 GLN B NE2 1 ATOM 1297 N N . PHE B 1 64 ? 28.346 21.665 35.741 1.00 24.75 ? 64 PHE B N 1 ATOM 1298 C CA . PHE B 1 64 ? 28.659 22.324 34.474 1.00 24.34 ? 64 PHE B CA 1 ATOM 1299 C C . PHE B 1 64 ? 30.084 22.064 33.998 1.00 24.99 ? 64 PHE B C 1 ATOM 1300 O O . PHE B 1 64 ? 30.938 22.954 34.017 1.00 25.71 ? 64 PHE B O 1 ATOM 1301 C CB . PHE B 1 64 ? 28.413 23.831 34.625 1.00 23.13 ? 64 PHE B CB 1 ATOM 1302 C CG . PHE B 1 64 ? 28.339 24.579 33.319 1.00 22.56 ? 64 PHE B CG 1 ATOM 1303 C CD1 . PHE B 1 64 ? 27.537 24.119 32.276 1.00 24.00 ? 64 PHE B CD1 1 ATOM 1304 C CD2 . PHE B 1 64 ? 29.027 25.776 33.156 1.00 26.33 ? 64 PHE B CD2 1 ATOM 1305 C CE1 . PHE B 1 64 ? 27.421 24.847 31.088 1.00 23.77 ? 64 PHE B CE1 1 ATOM 1306 C CE2 . PHE B 1 64 ? 28.919 26.515 31.973 1.00 25.99 ? 64 PHE B CE2 1 ATOM 1307 C CZ . PHE B 1 64 ? 28.112 26.047 30.938 1.00 27.90 ? 64 PHE B CZ 1 ATOM 1308 N N . VAL B 1 65 ? 30.339 20.842 33.547 1.00 24.19 ? 65 VAL B N 1 ATOM 1309 C CA . VAL B 1 65 ? 31.667 20.473 33.082 1.00 23.07 ? 65 VAL B CA 1 ATOM 1310 C C . VAL B 1 65 ? 31.914 20.843 31.624 1.00 24.52 ? 65 VAL B C 1 ATOM 1311 O O . VAL B 1 65 ? 30.995 21.217 30.898 1.00 22.93 ? 65 VAL B O 1 ATOM 1312 C CB . VAL B 1 65 ? 31.901 18.954 33.245 1.00 22.14 ? 65 VAL B CB 1 ATOM 1313 C CG1 . VAL B 1 65 ? 31.882 18.581 34.719 1.00 25.06 ? 65 VAL B CG1 1 ATOM 1314 C CG2 . VAL B 1 65 ? 30.822 18.180 32.492 1.00 24.49 ? 65 VAL B CG2 1 ATOM 1315 N N . GLU B 1 66 ? 33.169 20.735 31.199 1.00 23.73 ? 66 GLU B N 1 ATOM 1316 C CA . GLU B 1 66 ? 33.524 21.034 29.820 1.00 26.51 ? 66 GLU B CA 1 ATOM 1317 C C . GLU B 1 66 ? 32.647 20.216 28.885 1.00 26.92 ? 66 GLU B C 1 ATOM 1318 O O . GLU B 1 66 ? 32.277 19.082 29.189 1.00 28.96 ? 66 GLU B O 1 ATOM 1319 C CB . GLU B 1 66 ? 34.986 20.681 29.549 1.00 30.19 ? 66 GLU B CB 1 ATOM 1320 C CG . GLU B 1 66 ? 35.985 21.487 30.341 1.00 35.28 ? 66 GLU B CG 1 ATOM 1321 C CD . GLU B 1 66 ? 37.413 21.154 29.957 1.00 38.01 ? 66 GLU B CD 1 ATOM 1322 O OE1 . GLU B 1 66 ? 37.817 19.982 30.100 1.00 42.10 ? 66 GLU B OE1 1 ATOM 1323 O OE2 . GLU B 1 66 ? 38.130 22.067 29.506 1.00 42.51 ? 66 GLU B OE2 1 ATOM 1324 N N . GLY B 1 67 ? 32.321 20.798 27.739 1.00 25.57 ? 67 GLY B N 1 ATOM 1325 C CA . GLY B 1 67 ? 31.491 20.092 26.785 1.00 25.22 ? 67 GLY B CA 1 ATOM 1326 C C . GLY B 1 67 ? 30.840 21.069 25.837 1.00 23.14 ? 67 GLY B C 1 ATOM 1327 O O . GLY B 1 67 ? 31.089 22.274 25.908 1.00 21.79 ? 67 GLY B O 1 ATOM 1328 N N . ILE B 1 68 ? 30.021 20.543 24.938 1.00 23.57 ? 68 ILE B N 1 ATOM 1329 C CA . ILE B 1 68 ? 29.314 21.374 23.975 1.00 22.58 ? 68 ILE B CA 1 ATOM 1330 C C . ILE B 1 68 ? 27.885 21.450 24.471 1.00 21.47 ? 68 ILE B C 1 ATOM 1331 O O . ILE B 1 68 ? 27.247 20.424 24.722 1.00 22.54 ? 68 ILE B O 1 ATOM 1332 C CB . ILE B 1 68 ? 29.350 20.754 22.564 1.00 24.28 ? 68 ILE B CB 1 ATOM 1333 C CG1 . ILE B 1 68 ? 30.801 20.631 22.088 1.00 25.40 ? 68 ILE B CG1 1 ATOM 1334 C CG2 . ILE B 1 68 ? 28.541 21.614 21.596 1.00 21.74 ? 68 ILE B CG2 1 ATOM 1335 C CD1 . ILE B 1 68 ? 30.955 20.015 20.705 1.00 30.90 ? 68 ILE B CD1 1 ATOM 1336 N N . TYR B 1 69 ? 27.388 22.670 24.633 1.00 19.70 ? 69 TYR B N 1 ATOM 1337 C CA . TYR B 1 69 ? 26.035 22.871 25.117 1.00 17.72 ? 69 TYR B CA 1 ATOM 1338 C C . TYR B 1 69 ? 25.154 23.585 24.116 1.00 18.85 ? 69 TYR B C 1 ATOM 1339 O O . TYR B 1 69 ? 25.625 24.368 23.291 1.00 19.58 ? 69 TYR B O 1 ATOM 1340 C CB . TYR B 1 69 ? 26.043 23.678 26.417 1.00 19.07 ? 69 TYR B CB 1 ATOM 1341 C CG . TYR B 1 69 ? 26.693 22.960 27.578 1.00 18.51 ? 69 TYR B CG 1 ATOM 1342 C CD1 . TYR B 1 69 ? 28.082 22.877 27.684 1.00 19.37 ? 69 TYR B CD1 1 ATOM 1343 C CD2 . TYR B 1 69 ? 25.918 22.342 28.560 1.00 21.61 ? 69 TYR B CD2 1 ATOM 1344 C CE1 . TYR B 1 69 ? 28.685 22.192 28.746 1.00 21.11 ? 69 TYR B CE1 1 ATOM 1345 C CE2 . TYR B 1 69 ? 26.513 21.654 29.624 1.00 19.19 ? 69 TYR B CE2 1 ATOM 1346 C CZ . TYR B 1 69 ? 27.891 21.586 29.709 1.00 22.46 ? 69 TYR B CZ 1 ATOM 1347 O OH . TYR B 1 69 ? 28.487 20.918 30.759 1.00 22.00 ? 69 TYR B OH 1 ATOM 1348 N N . LYS B 1 70 ? 23.861 23.304 24.195 1.00 19.16 ? 70 LYS B N 1 ATOM 1349 C CA . LYS B 1 70 ? 22.904 23.947 23.320 1.00 20.32 ? 70 LYS B CA 1 ATOM 1350 C C . LYS B 1 70 ? 21.819 24.571 24.174 1.00 19.87 ? 70 LYS B C 1 ATOM 1351 O O . LYS B 1 70 ? 21.215 23.903 25.021 1.00 20.89 ? 70 LYS B O 1 ATOM 1352 C CB . LYS B 1 70 ? 22.281 22.944 22.346 1.00 20.98 ? 70 LYS B CB 1 ATOM 1353 C CG . LYS B 1 70 ? 21.168 23.568 21.502 1.00 25.10 ? 70 LYS B CG 1 ATOM 1354 C CD . LYS B 1 70 ? 20.834 22.745 20.266 1.00 29.86 ? 70 LYS B CD 1 ATOM 1355 C CE . LYS B 1 70 ? 20.199 21.416 20.613 1.00 33.00 ? 70 LYS B CE 1 ATOM 1356 N NZ . LYS B 1 70 ? 19.771 20.704 19.371 1.00 36.92 ? 70 LYS B NZ 1 ATOM 1357 N N . VAL B 1 71 ? 21.590 25.862 23.963 1.00 18.80 ? 71 VAL B N 1 ATOM 1358 C CA . VAL B 1 71 ? 20.551 26.574 24.686 1.00 17.51 ? 71 VAL B CA 1 ATOM 1359 C C . VAL B 1 71 ? 19.469 26.852 23.661 1.00 17.50 ? 71 VAL B C 1 ATOM 1360 O O . VAL B 1 71 ? 19.704 27.551 22.673 1.00 17.91 ? 71 VAL B O 1 ATOM 1361 C CB . VAL B 1 71 ? 21.062 27.903 25.273 1.00 17.91 ? 71 VAL B CB 1 ATOM 1362 C CG1 . VAL B 1 71 ? 19.918 28.651 25.941 1.00 20.04 ? 71 VAL B CG1 1 ATOM 1363 C CG2 . VAL B 1 71 ? 22.164 27.629 26.290 1.00 19.15 ? 71 VAL B CG2 1 ATOM 1364 N N . GLU B 1 72 ? 18.291 26.285 23.890 1.00 18.49 ? 72 GLU B N 1 ATOM 1365 C CA . GLU B 1 72 ? 17.168 26.453 22.982 1.00 20.80 ? 72 GLU B CA 1 ATOM 1366 C C . GLU B 1 72 ? 16.109 27.337 23.624 1.00 20.59 ? 72 GLU B C 1 ATOM 1367 O O . GLU B 1 72 ? 15.607 27.044 24.716 1.00 18.95 ? 72 GLU B O 1 ATOM 1368 C CB . GLU B 1 72 ? 16.575 25.088 22.640 1.00 23.29 ? 72 GLU B CB 1 ATOM 1369 C CG . GLU B 1 72 ? 15.330 25.142 21.784 1.00 30.59 ? 72 GLU B CG 1 ATOM 1370 C CD . GLU B 1 72 ? 14.736 23.765 21.576 1.00 38.17 ? 72 GLU B CD 1 ATOM 1371 O OE1 . GLU B 1 72 ? 15.411 22.921 20.948 1.00 40.83 ? 72 GLU B OE1 1 ATOM 1372 O OE2 . GLU B 1 72 ? 13.603 23.527 22.051 1.00 42.16 ? 72 GLU B OE2 1 ATOM 1373 N N . ILE B 1 73 ? 15.777 28.424 22.940 1.00 19.02 ? 73 ILE B N 1 ATOM 1374 C CA . ILE B 1 73 ? 14.791 29.369 23.429 1.00 19.09 ? 73 ILE B CA 1 ATOM 1375 C C . ILE B 1 73 ? 13.520 29.242 22.588 1.00 19.30 ? 73 ILE B C 1 ATOM 1376 O O . ILE B 1 73 ? 13.545 29.435 21.373 1.00 18.71 ? 73 ILE B O 1 ATOM 1377 C CB . ILE B 1 73 ? 15.358 30.809 23.359 1.00 18.39 ? 73 ILE B CB 1 ATOM 1378 C CG1 . ILE B 1 73 ? 16.659 30.883 24.173 1.00 21.74 ? 73 ILE B CG1 1 ATOM 1379 C CG2 . ILE B 1 73 ? 14.349 31.797 23.900 1.00 19.62 ? 73 ILE B CG2 1 ATOM 1380 C CD1 . ILE B 1 73 ? 17.435 32.185 24.000 1.00 25.45 ? 73 ILE B CD1 1 ATOM 1381 N N . ASP B 1 74 ? 12.412 28.891 23.233 1.00 18.95 ? 74 ASP B N 1 ATOM 1382 C CA . ASP B 1 74 ? 11.148 28.735 22.520 1.00 20.89 ? 74 ASP B CA 1 ATOM 1383 C C . ASP B 1 74 ? 10.523 30.085 22.186 1.00 19.81 ? 74 ASP B C 1 ATOM 1384 O O . ASP B 1 74 ? 9.581 30.540 22.832 1.00 21.45 ? 74 ASP B O 1 ATOM 1385 C CB . ASP B 1 74 ? 10.172 27.888 23.337 1.00 21.96 ? 74 ASP B CB 1 ATOM 1386 C CG . ASP B 1 74 ? 8.845 27.667 22.618 1.00 31.40 ? 74 ASP B CG 1 ATOM 1387 O OD1 . ASP B 1 74 ? 8.727 28.042 21.429 1.00 32.76 ? 74 ASP B OD1 1 ATOM 1388 O OD2 . ASP B 1 74 ? 7.916 27.113 23.243 1.00 34.77 ? 74 ASP B OD2 1 ATOM 1389 N N . THR B 1 75 ? 11.057 30.717 21.152 1.00 19.43 ? 75 THR B N 1 ATOM 1390 C CA . THR B 1 75 ? 10.581 32.019 20.721 1.00 19.43 ? 75 THR B CA 1 ATOM 1391 C C . THR B 1 75 ? 9.206 31.962 20.055 1.00 19.31 ? 75 THR B C 1 ATOM 1392 O O . THR B 1 75 ? 8.405 32.886 20.192 1.00 19.69 ? 75 THR B O 1 ATOM 1393 C CB . THR B 1 75 ? 11.575 32.639 19.733 1.00 18.16 ? 75 THR B CB 1 ATOM 1394 O OG1 . THR B 1 75 ? 11.727 31.758 18.614 1.00 18.40 ? 75 THR B OG1 1 ATOM 1395 C CG2 . THR B 1 75 ? 12.939 32.842 20.399 1.00 19.06 ? 75 THR B CG2 1 ATOM 1396 N N . LYS B 1 76 ? 8.929 30.874 19.342 1.00 20.58 ? 76 LYS B N 1 ATOM 1397 C CA . LYS B 1 76 ? 7.659 30.739 18.633 1.00 23.56 ? 76 LYS B CA 1 ATOM 1398 C C . LYS B 1 76 ? 6.450 30.863 19.559 1.00 22.29 ? 76 LYS B C 1 ATOM 1399 O O . LYS B 1 76 ? 5.524 31.626 19.281 1.00 22.96 ? 76 LYS B O 1 ATOM 1400 C CB . LYS B 1 76 ? 7.610 29.406 17.880 1.00 24.19 ? 76 LYS B CB 1 ATOM 1401 C CG . LYS B 1 76 ? 6.461 29.315 16.887 1.00 25.88 ? 76 LYS B CG 1 ATOM 1402 C CD . LYS B 1 76 ? 6.504 28.019 16.096 1.00 28.58 ? 76 LYS B CD 1 ATOM 1403 C CE . LYS B 1 76 ? 5.498 28.044 14.950 1.00 32.33 ? 76 LYS B CE 1 ATOM 1404 N NZ . LYS B 1 76 ? 5.548 26.805 14.125 1.00 35.22 ? 76 LYS B NZ 1 ATOM 1405 N N . SER B 1 77 ? 6.466 30.119 20.659 1.00 21.84 ? 77 SER B N 1 ATOM 1406 C CA . SER B 1 77 ? 5.375 30.157 21.627 1.00 23.39 ? 77 SER B CA 1 ATOM 1407 C C . SER B 1 77 ? 5.215 31.552 22.213 1.00 23.11 ? 77 SER B C 1 ATOM 1408 O O . SER B 1 77 ? 4.100 31.992 22.484 1.00 22.83 ? 77 SER B O 1 ATOM 1409 C CB . SER B 1 77 ? 5.635 29.154 22.754 1.00 24.71 ? 77 SER B CB 1 ATOM 1410 O OG . SER B 1 77 ? 5.605 27.828 22.263 1.00 29.16 ? 77 SER B OG 1 ATOM 1411 N N . TYR B 1 78 ? 6.335 32.248 22.398 1.00 22.00 ? 78 TYR B N 1 ATOM 1412 C CA . TYR B 1 78 ? 6.323 33.599 22.953 1.00 20.87 ? 78 TYR B CA 1 ATOM 1413 C C . TYR B 1 78 ? 5.538 34.566 22.064 1.00 21.20 ? 78 TYR B C 1 ATOM 1414 O O . TYR B 1 78 ? 4.653 35.281 22.537 1.00 20.97 ? 78 TYR B O 1 ATOM 1415 C CB . TYR B 1 78 ? 7.756 34.120 23.111 1.00 21.55 ? 78 TYR B CB 1 ATOM 1416 C CG . TYR B 1 78 ? 7.829 35.528 23.655 1.00 19.66 ? 78 TYR B CG 1 ATOM 1417 C CD1 . TYR B 1 78 ? 7.559 35.789 25.002 1.00 19.30 ? 78 TYR B CD1 1 ATOM 1418 C CD2 . TYR B 1 78 ? 8.130 36.607 22.820 1.00 21.60 ? 78 TYR B CD2 1 ATOM 1419 C CE1 . TYR B 1 78 ? 7.583 37.076 25.504 1.00 21.90 ? 78 TYR B CE1 1 ATOM 1420 C CE2 . TYR B 1 78 ? 8.154 37.909 23.314 1.00 21.54 ? 78 TYR B CE2 1 ATOM 1421 C CZ . TYR B 1 78 ? 7.880 38.135 24.659 1.00 23.10 ? 78 TYR B CZ 1 ATOM 1422 O OH . TYR B 1 78 ? 7.906 39.413 25.169 1.00 23.67 ? 78 TYR B OH 1 ATOM 1423 N N . TRP B 1 79 ? 5.872 34.596 20.779 1.00 18.94 ? 79 TRP B N 1 ATOM 1424 C CA . TRP B 1 79 ? 5.194 35.483 19.845 1.00 21.26 ? 79 TRP B CA 1 ATOM 1425 C C . TRP B 1 79 ? 3.743 35.080 19.601 1.00 23.15 ? 79 TRP B C 1 ATOM 1426 O O . TRP B 1 79 ? 2.872 35.941 19.479 1.00 24.34 ? 79 TRP B O 1 ATOM 1427 C CB . TRP B 1 79 ? 5.957 35.539 18.518 1.00 19.28 ? 79 TRP B CB 1 ATOM 1428 C CG . TRP B 1 79 ? 7.289 36.193 18.658 1.00 22.77 ? 79 TRP B CG 1 ATOM 1429 C CD1 . TRP B 1 79 ? 8.512 35.618 18.469 1.00 21.12 ? 79 TRP B CD1 1 ATOM 1430 C CD2 . TRP B 1 79 ? 7.536 37.548 19.052 1.00 19.78 ? 79 TRP B CD2 1 ATOM 1431 N NE1 . TRP B 1 79 ? 9.509 36.533 18.725 1.00 19.38 ? 79 TRP B NE1 1 ATOM 1432 C CE2 . TRP B 1 79 ? 8.937 37.725 19.085 1.00 20.13 ? 79 TRP B CE2 1 ATOM 1433 C CE3 . TRP B 1 79 ? 6.707 38.630 19.385 1.00 21.09 ? 79 TRP B CE3 1 ATOM 1434 C CZ2 . TRP B 1 79 ? 9.532 38.941 19.438 1.00 18.66 ? 79 TRP B CZ2 1 ATOM 1435 C CZ3 . TRP B 1 79 ? 7.298 39.843 19.736 1.00 21.27 ? 79 TRP B CZ3 1 ATOM 1436 C CH2 . TRP B 1 79 ? 8.701 39.986 19.760 1.00 17.38 ? 79 TRP B CH2 1 ATOM 1437 N N . LYS B 1 80 ? 3.481 33.778 19.542 1.00 26.40 ? 80 LYS B N 1 ATOM 1438 C CA . LYS B 1 80 ? 2.120 33.294 19.331 1.00 30.84 ? 80 LYS B CA 1 ATOM 1439 C C . LYS B 1 80 ? 1.223 33.810 20.460 1.00 30.43 ? 80 LYS B C 1 ATOM 1440 O O . LYS B 1 80 ? 0.102 34.248 20.227 1.00 29.47 ? 80 LYS B O 1 ATOM 1441 C CB . LYS B 1 80 ? 2.099 31.762 19.317 1.00 33.03 ? 80 LYS B CB 1 ATOM 1442 C CG . LYS B 1 80 ? 2.958 31.132 18.230 1.00 39.38 ? 80 LYS B CG 1 ATOM 1443 C CD . LYS B 1 80 ? 2.298 31.197 16.866 1.00 42.65 ? 80 LYS B CD 1 ATOM 1444 C CE . LYS B 1 80 ? 1.098 30.266 16.806 1.00 45.55 ? 80 LYS B CE 1 ATOM 1445 N NZ . LYS B 1 80 ? 1.478 28.864 17.151 1.00 45.97 ? 80 LYS B NZ 1 ATOM 1446 N N . ALA B 1 81 ? 1.738 33.770 21.683 1.00 31.94 ? 81 ALA B N 1 ATOM 1447 C CA . ALA B 1 81 ? 0.985 34.225 22.847 1.00 32.99 ? 81 ALA B CA 1 ATOM 1448 C C . ALA B 1 81 ? 0.664 35.710 22.760 1.00 34.54 ? 81 ALA B C 1 ATOM 1449 O O . ALA B 1 81 ? -0.220 36.207 23.460 1.00 36.33 ? 81 ALA B O 1 ATOM 1450 C CB . ALA B 1 81 ? 1.769 33.934 24.120 1.00 33.79 ? 81 ALA B CB 1 ATOM 1451 N N . LEU B 1 82 ? 1.385 36.419 21.899 1.00 32.89 ? 82 LEU B N 1 ATOM 1452 C CA . LEU B 1 82 ? 1.172 37.847 21.726 1.00 32.93 ? 82 LEU B CA 1 ATOM 1453 C C . LEU B 1 82 ? 0.388 38.145 20.457 1.00 33.51 ? 82 LEU B C 1 ATOM 1454 O O . LEU B 1 82 ? 0.163 39.306 20.117 1.00 34.31 ? 82 LEU B O 1 ATOM 1455 C CB . LEU B 1 82 ? 2.515 38.580 21.693 1.00 34.69 ? 82 LEU B CB 1 ATOM 1456 C CG . LEU B 1 82 ? 3.354 38.459 22.969 1.00 35.27 ? 82 LEU B CG 1 ATOM 1457 C CD1 . LEU B 1 82 ? 4.687 39.172 22.778 1.00 36.56 ? 82 LEU B CD1 1 ATOM 1458 C CD2 . LEU B 1 82 ? 2.589 39.051 24.142 1.00 35.21 ? 82 LEU B CD2 1 ATOM 1459 N N . GLY B 1 83 ? -0.020 37.091 19.756 1.00 33.27 ? 83 GLY B N 1 ATOM 1460 C CA . GLY B 1 83 ? -0.784 37.264 18.534 1.00 31.23 ? 83 GLY B CA 1 ATOM 1461 C C . GLY B 1 83 ? 0.043 37.644 17.322 1.00 33.37 ? 83 GLY B C 1 ATOM 1462 O O . GLY B 1 83 ? -0.471 38.249 16.380 1.00 30.77 ? 83 GLY B O 1 ATOM 1463 N N . ILE B 1 84 ? 1.324 37.288 17.339 1.00 30.95 ? 84 ILE B N 1 ATOM 1464 C CA . ILE B 1 84 ? 2.220 37.590 16.230 1.00 32.13 ? 84 ILE B CA 1 ATOM 1465 C C . ILE B 1 84 ? 2.766 36.299 15.631 1.00 32.20 ? 84 ILE B C 1 ATOM 1466 O O . ILE B 1 84 ? 3.220 35.417 16.357 1.00 31.84 ? 84 ILE B O 1 ATOM 1467 C CB . ILE B 1 84 ? 3.409 38.459 16.700 1.00 34.95 ? 84 ILE B CB 1 ATOM 1468 C CG1 . ILE B 1 84 ? 2.895 39.823 17.168 1.00 33.92 ? 84 ILE B CG1 1 ATOM 1469 C CG2 . ILE B 1 84 ? 4.425 38.617 15.573 1.00 33.99 ? 84 ILE B CG2 1 ATOM 1470 C CD1 . ILE B 1 84 ? 3.956 40.699 17.794 1.00 38.73 ? 84 ILE B CD1 1 ATOM 1471 N N . SER B 1 85 ? 2.705 36.181 14.308 1.00 31.59 ? 85 SER B N 1 ATOM 1472 C CA . SER B 1 85 ? 3.212 34.988 13.642 1.00 32.47 ? 85 SER B CA 1 ATOM 1473 C C . SER B 1 85 ? 4.700 35.216 13.428 1.00 30.98 ? 85 SER B C 1 ATOM 1474 O O . SER B 1 85 ? 5.100 36.087 12.656 1.00 31.49 ? 85 SER B O 1 ATOM 1475 C CB . SER B 1 85 ? 2.504 34.778 12.301 1.00 35.49 ? 85 SER B CB 1 ATOM 1476 O OG . SER B 1 85 ? 2.603 35.936 11.493 1.00 43.32 ? 85 SER B OG 1 ATOM 1477 N N . PRO B 1 86 ? 5.543 34.451 14.136 1.00 27.98 ? 86 PRO B N 1 ATOM 1478 C CA . PRO B 1 86 ? 6.990 34.611 13.993 1.00 24.13 ? 86 PRO B CA 1 ATOM 1479 C C . PRO B 1 86 ? 7.571 33.761 12.868 1.00 23.84 ? 86 PRO B C 1 ATOM 1480 O O . PRO B 1 86 ? 6.909 32.866 12.340 1.00 24.27 ? 86 PRO B O 1 ATOM 1481 C CB . PRO B 1 86 ? 7.501 34.196 15.363 1.00 23.28 ? 86 PRO B CB 1 ATOM 1482 C CG . PRO B 1 86 ? 6.605 33.042 15.675 1.00 23.74 ? 86 PRO B CG 1 ATOM 1483 C CD . PRO B 1 86 ? 5.227 33.540 15.251 1.00 27.32 ? 86 PRO B CD 1 ATOM 1484 N N . PHE B 1 87 ? 8.818 34.043 12.515 1.00 20.66 ? 87 PHE B N 1 ATOM 1485 C CA . PHE B 1 87 ? 9.485 33.316 11.444 1.00 19.02 ? 87 PHE B CA 1 ATOM 1486 C C . PHE B 1 87 ? 10.155 32.043 11.939 1.00 18.09 ? 87 PHE B C 1 ATOM 1487 O O . PHE B 1 87 ? 9.958 30.963 11.380 1.00 18.62 ? 87 PHE B O 1 ATOM 1488 C CB . PHE B 1 87 ? 10.540 34.210 10.791 1.00 18.20 ? 87 PHE B CB 1 ATOM 1489 C CG . PHE B 1 87 ? 11.306 33.536 9.687 1.00 18.72 ? 87 PHE B CG 1 ATOM 1490 C CD1 . PHE B 1 87 ? 10.714 33.312 8.448 1.00 20.84 ? 87 PHE B CD1 1 ATOM 1491 C CD2 . PHE B 1 87 ? 12.617 33.120 9.888 1.00 19.44 ? 87 PHE B CD2 1 ATOM 1492 C CE1 . PHE B 1 87 ? 11.419 32.682 7.421 1.00 19.75 ? 87 PHE B CE1 1 ATOM 1493 C CE2 . PHE B 1 87 ? 13.329 32.492 8.871 1.00 22.06 ? 87 PHE B CE2 1 ATOM 1494 C CZ . PHE B 1 87 ? 12.723 32.274 7.632 1.00 21.04 ? 87 PHE B CZ 1 ATOM 1495 N N . HIS B 1 88 ? 10.953 32.182 12.992 1.00 16.14 ? 88 HIS B N 1 ATOM 1496 C CA . HIS B 1 88 ? 11.704 31.062 13.546 1.00 16.91 ? 88 HIS B CA 1 ATOM 1497 C C . HIS B 1 88 ? 10.910 30.104 14.425 1.00 19.03 ? 88 HIS B C 1 ATOM 1498 O O . HIS B 1 88 ? 9.960 30.496 15.100 1.00 18.36 ? 88 HIS B O 1 ATOM 1499 C CB . HIS B 1 88 ? 12.898 31.597 14.349 1.00 18.95 ? 88 HIS B CB 1 ATOM 1500 C CG . HIS B 1 88 ? 13.715 32.602 13.602 1.00 17.62 ? 88 HIS B CG 1 ATOM 1501 N ND1 . HIS B 1 88 ? 13.442 33.953 13.632 1.00 18.56 ? 88 HIS B ND1 1 ATOM 1502 C CD2 . HIS B 1 88 ? 14.772 32.449 12.771 1.00 19.19 ? 88 HIS B CD2 1 ATOM 1503 C CE1 . HIS B 1 88 ? 14.300 34.589 12.853 1.00 17.36 ? 88 HIS B CE1 1 ATOM 1504 N NE2 . HIS B 1 88 ? 15.118 33.699 12.320 1.00 18.77 ? 88 HIS B NE2 1 ATOM 1505 N N . GLU B 1 89 ? 11.314 28.838 14.401 1.00 18.70 ? 89 GLU B N 1 ATOM 1506 C CA . GLU B 1 89 ? 10.686 27.815 15.226 1.00 20.01 ? 89 GLU B CA 1 ATOM 1507 C C . GLU B 1 89 ? 11.149 28.033 16.661 1.00 19.92 ? 89 GLU B C 1 ATOM 1508 O O . GLU B 1 89 ? 10.398 27.833 17.618 1.00 18.78 ? 89 GLU B O 1 ATOM 1509 C CB . GLU B 1 89 ? 11.099 26.424 14.740 1.00 20.27 ? 89 GLU B CB 1 ATOM 1510 C CG . GLU B 1 89 ? 10.346 25.994 13.507 1.00 22.02 ? 89 GLU B CG 1 ATOM 1511 C CD . GLU B 1 89 ? 8.853 25.930 13.761 1.00 25.65 ? 89 GLU B CD 1 ATOM 1512 O OE1 . GLU B 1 89 ? 8.430 25.101 14.591 1.00 26.09 ? 89 GLU B OE1 1 ATOM 1513 O OE2 . GLU B 1 89 ? 8.107 26.714 13.145 1.00 26.56 ? 89 GLU B OE2 1 ATOM 1514 N N . HIS B 1 90 ? 12.400 28.445 16.792 1.00 18.32 ? 90 HIS B N 1 ATOM 1515 C CA . HIS B 1 90 ? 13.012 28.732 18.081 1.00 22.46 ? 90 HIS B CA 1 ATOM 1516 C C . HIS B 1 90 ? 14.371 29.354 17.799 1.00 19.75 ? 90 HIS B C 1 ATOM 1517 O O . HIS B 1 90 ? 14.767 29.489 16.640 1.00 21.88 ? 90 HIS B O 1 ATOM 1518 C CB . HIS B 1 90 ? 13.183 27.448 18.903 1.00 23.82 ? 90 HIS B CB 1 ATOM 1519 C CG . HIS B 1 90 ? 13.994 26.392 18.220 1.00 27.83 ? 90 HIS B CG 1 ATOM 1520 N ND1 . HIS B 1 90 ? 13.466 25.174 17.851 1.00 28.99 ? 90 HIS B ND1 1 ATOM 1521 C CD2 . HIS B 1 90 ? 15.293 26.370 17.834 1.00 30.65 ? 90 HIS B CD2 1 ATOM 1522 C CE1 . HIS B 1 90 ? 14.403 24.447 17.269 1.00 30.72 ? 90 HIS B CE1 1 ATOM 1523 N NE2 . HIS B 1 90 ? 15.521 25.150 17.246 1.00 32.50 ? 90 HIS B NE2 1 ATOM 1524 N N . ALA B 1 91 ? 15.071 29.757 18.851 1.00 21.83 ? 91 ALA B N 1 ATOM 1525 C CA . ALA B 1 91 ? 16.404 30.328 18.696 1.00 21.06 ? 91 ALA B CA 1 ATOM 1526 C C . ALA B 1 91 ? 17.344 29.360 19.399 1.00 23.75 ? 91 ALA B C 1 ATOM 1527 O O . ALA B 1 91 ? 17.066 28.923 20.521 1.00 20.73 ? 91 ALA B O 1 ATOM 1528 C CB . ALA B 1 91 ? 16.481 31.702 19.346 1.00 22.36 ? 91 ALA B CB 1 ATOM 1529 N N . GLU B 1 92 ? 18.441 29.016 18.738 1.00 23.94 ? 92 GLU B N 1 ATOM 1530 C CA . GLU B 1 92 ? 19.410 28.092 19.306 1.00 27.92 ? 92 GLU B CA 1 ATOM 1531 C C . GLU B 1 92 ? 20.780 28.735 19.459 1.00 25.46 ? 92 GLU B C 1 ATOM 1532 O O . GLU B 1 92 ? 21.223 29.496 18.604 1.00 25.72 ? 92 GLU B O 1 ATOM 1533 C CB . GLU B 1 92 ? 19.547 26.847 18.422 1.00 33.18 ? 92 GLU B CB 1 ATOM 1534 C CG . GLU B 1 92 ? 18.516 25.764 18.672 1.00 43.07 ? 92 GLU B CG 1 ATOM 1535 C CD . GLU B 1 92 ? 18.759 24.533 17.816 1.00 48.99 ? 92 GLU B CD 1 ATOM 1536 O OE1 . GLU B 1 92 ? 19.915 24.059 17.768 1.00 52.37 ? 92 GLU B OE1 1 ATOM 1537 O OE2 . GLU B 1 92 ? 17.796 24.035 17.196 1.00 50.70 ? 92 GLU B OE2 1 ATOM 1538 N N . VAL B 1 93 ? 21.443 28.427 20.565 1.00 21.14 ? 93 VAL B N 1 ATOM 1539 C CA . VAL B 1 93 ? 22.779 28.937 20.819 1.00 19.72 ? 93 VAL B CA 1 ATOM 1540 C C . VAL B 1 93 ? 23.605 27.718 21.178 1.00 18.95 ? 93 VAL B C 1 ATOM 1541 O O . VAL B 1 93 ? 23.332 27.054 22.180 1.00 21.44 ? 93 VAL B O 1 ATOM 1542 C CB . VAL B 1 93 ? 22.795 29.933 21.991 1.00 21.42 ? 93 VAL B CB 1 ATOM 1543 C CG1 . VAL B 1 93 ? 24.223 30.370 22.274 1.00 24.02 ? 93 VAL B CG1 1 ATOM 1544 C CG2 . VAL B 1 93 ? 21.922 31.138 21.655 1.00 23.78 ? 93 VAL B CG2 1 ATOM 1545 N N . VAL B 1 94 ? 24.595 27.414 20.347 1.00 18.90 ? 94 VAL B N 1 ATOM 1546 C CA . VAL B 1 94 ? 25.453 26.254 20.554 1.00 20.37 ? 94 VAL B CA 1 ATOM 1547 C C . VAL B 1 94 ? 26.862 26.746 20.785 1.00 20.92 ? 94 VAL B C 1 ATOM 1548 O O . VAL B 1 94 ? 27.421 27.477 19.962 1.00 16.47 ? 94 VAL B O 1 ATOM 1549 C CB . VAL B 1 94 ? 25.442 25.320 19.326 1.00 21.61 ? 94 VAL B CB 1 ATOM 1550 C CG1 . VAL B 1 94 ? 26.268 24.070 19.611 1.00 20.43 ? 94 VAL B CG1 1 ATOM 1551 C CG2 . VAL B 1 94 ? 24.005 24.938 18.980 1.00 23.64 ? 94 VAL B CG2 1 ATOM 1552 N N . PHE B 1 95 ? 27.439 26.335 21.905 1.00 19.85 ? 95 PHE B N 1 ATOM 1553 C CA . PHE B 1 95 ? 28.771 26.781 22.251 1.00 20.36 ? 95 PHE B CA 1 ATOM 1554 C C . PHE B 1 95 ? 29.519 25.754 23.081 1.00 22.03 ? 95 PHE B C 1 ATOM 1555 O O . PHE B 1 95 ? 28.922 24.852 23.671 1.00 18.60 ? 95 PHE B O 1 ATOM 1556 C CB . PHE B 1 95 ? 28.682 28.090 23.038 1.00 19.84 ? 95 PHE B CB 1 ATOM 1557 C CG . PHE B 1 95 ? 27.982 27.952 24.366 1.00 22.48 ? 95 PHE B CG 1 ATOM 1558 C CD1 . PHE B 1 95 ? 26.594 27.868 24.435 1.00 23.76 ? 95 PHE B CD1 1 ATOM 1559 C CD2 . PHE B 1 95 ? 28.714 27.892 25.550 1.00 23.51 ? 95 PHE B CD2 1 ATOM 1560 C CE1 . PHE B 1 95 ? 25.944 27.726 25.662 1.00 26.05 ? 95 PHE B CE1 1 ATOM 1561 C CE2 . PHE B 1 95 ? 28.071 27.748 26.784 1.00 26.69 ? 95 PHE B CE2 1 ATOM 1562 C CZ . PHE B 1 95 ? 26.687 27.665 26.837 1.00 23.66 ? 95 PHE B CZ 1 ATOM 1563 N N . THR B 1 96 ? 30.835 25.923 23.130 1.00 22.32 ? 96 THR B N 1 ATOM 1564 C CA . THR B 1 96 ? 31.705 25.043 23.895 1.00 23.55 ? 96 THR B CA 1 ATOM 1565 C C . THR B 1 96 ? 32.101 25.740 25.192 1.00 27.27 ? 96 THR B C 1 ATOM 1566 O O . THR B 1 96 ? 32.551 26.886 25.172 1.00 25.55 ? 96 THR B O 1 ATOM 1567 C CB . THR B 1 96 ? 32.995 24.718 23.115 1.00 24.99 ? 96 THR B CB 1 ATOM 1568 O OG1 . THR B 1 96 ? 32.668 23.940 21.958 1.00 24.11 ? 96 THR B OG1 1 ATOM 1569 C CG2 . THR B 1 96 ? 33.977 23.933 23.989 1.00 25.56 ? 96 THR B CG2 1 ATOM 1570 N N . ALA B 1 97 ? 31.900 25.061 26.316 1.00 27.80 ? 97 ALA B N 1 ATOM 1571 C CA . ALA B 1 97 ? 32.286 25.618 27.605 1.00 30.99 ? 97 ALA B CA 1 ATOM 1572 C C . ALA B 1 97 ? 33.755 25.222 27.736 1.00 35.31 ? 97 ALA B C 1 ATOM 1573 O O . ALA B 1 97 ? 34.081 24.035 27.756 1.00 33.17 ? 97 ALA B O 1 ATOM 1574 C CB . ALA B 1 97 ? 31.461 25.001 28.720 1.00 29.80 ? 97 ALA B CB 1 ATOM 1575 N N . ASN B 1 98 ? 34.629 26.223 27.795 1.00 41.58 ? 98 ASN B N 1 ATOM 1576 C CA . ASN B 1 98 ? 36.072 26.014 27.886 1.00 49.12 ? 98 ASN B CA 1 ATOM 1577 C C . ASN B 1 98 ? 36.517 25.571 29.271 1.00 52.19 ? 98 ASN B C 1 ATOM 1578 O O . ASN B 1 98 ? 37.270 24.604 29.410 1.00 55.24 ? 98 ASN B O 1 ATOM 1579 C CB . ASN B 1 98 ? 36.805 27.303 27.506 1.00 53.13 ? 98 ASN B CB 1 ATOM 1580 C CG . ASN B 1 98 ? 36.323 27.883 26.186 1.00 56.89 ? 98 ASN B CG 1 ATOM 1581 O OD1 . ASN B 1 98 ? 35.137 28.177 26.017 1.00 58.97 ? 98 ASN B OD1 1 ATOM 1582 N ND2 . ASN B 1 98 ? 37.245 28.055 25.243 1.00 58.01 ? 98 ASN B ND2 1 ATOM 1583 N N . ASP B 1 99 ? 36.063 26.288 30.294 1.00 54.50 ? 99 ASP B N 1 ATOM 1584 C CA . ASP B 1 99 ? 36.413 25.957 31.671 1.00 57.44 ? 99 ASP B CA 1 ATOM 1585 C C . ASP B 1 99 ? 37.906 26.163 31.921 1.00 58.79 ? 99 ASP B C 1 ATOM 1586 O O . ASP B 1 99 ? 38.535 25.420 32.677 1.00 60.38 ? 99 ASP B O 1 ATOM 1587 C CB . ASP B 1 99 ? 36.018 24.504 31.975 1.00 57.71 ? 99 ASP B CB 1 ATOM 1588 C CG . ASP B 1 99 ? 36.336 24.095 33.399 1.00 56.28 ? 99 ASP B CG 1 ATOM 1589 O OD1 . ASP B 1 99 ? 35.813 24.736 34.335 1.00 58.42 ? 99 ASP B OD1 1 ATOM 1590 O OD2 . ASP B 1 99 ? 37.109 23.132 33.580 1.00 54.68 ? 99 ASP B OD2 1 ATOM 1591 N N . SER B 1 100 ? 38.466 27.179 31.273 1.00 59.68 ? 100 SER B N 1 ATOM 1592 C CA . SER B 1 100 ? 39.875 27.513 31.421 1.00 60.28 ? 100 SER B CA 1 ATOM 1593 C C . SER B 1 100 ? 39.981 28.723 32.344 1.00 61.32 ? 100 SER B C 1 ATOM 1594 O O . SER B 1 100 ? 40.257 29.839 31.899 1.00 61.69 ? 100 SER B O 1 ATOM 1595 C CB . SER B 1 100 ? 40.487 27.839 30.057 1.00 60.90 ? 100 SER B CB 1 ATOM 1596 O OG . SER B 1 100 ? 39.817 28.928 29.443 1.00 60.92 ? 100 SER B OG 1 ATOM 1597 N N . GLY B 1 101 ? 39.751 28.492 33.632 1.00 62.30 ? 101 GLY B N 1 ATOM 1598 C CA . GLY B 1 101 ? 39.807 29.570 34.603 1.00 61.42 ? 101 GLY B CA 1 ATOM 1599 C C . GLY B 1 101 ? 38.408 29.930 35.070 1.00 61.10 ? 101 GLY B C 1 ATOM 1600 O O . GLY B 1 101 ? 37.428 29.484 34.470 1.00 62.03 ? 101 GLY B O 1 ATOM 1601 N N . PRO B 1 102 ? 38.276 30.730 36.142 1.00 59.75 ? 102 PRO B N 1 ATOM 1602 C CA . PRO B 1 102 ? 36.957 31.121 36.650 1.00 59.00 ? 102 PRO B CA 1 ATOM 1603 C C . PRO B 1 102 ? 36.137 31.804 35.558 1.00 57.30 ? 102 PRO B C 1 ATOM 1604 O O . PRO B 1 102 ? 36.543 32.842 35.031 1.00 58.30 ? 102 PRO B O 1 ATOM 1605 C CB . PRO B 1 102 ? 37.301 32.072 37.796 1.00 59.29 ? 102 PRO B CB 1 ATOM 1606 C CG . PRO B 1 102 ? 38.621 31.551 38.280 1.00 59.62 ? 102 PRO B CG 1 ATOM 1607 C CD . PRO B 1 102 ? 39.347 31.289 36.985 1.00 60.38 ? 102 PRO B CD 1 ATOM 1608 N N . ARG B 1 103 ? 34.990 31.223 35.215 1.00 53.93 ? 103 ARG B N 1 ATOM 1609 C CA . ARG B 1 103 ? 34.148 31.802 34.175 1.00 50.56 ? 103 ARG B CA 1 ATOM 1610 C C . ARG B 1 103 ? 32.645 31.637 34.370 1.00 46.47 ? 103 ARG B C 1 ATOM 1611 O O . ARG B 1 103 ? 32.150 30.555 34.690 1.00 45.61 ? 103 ARG B O 1 ATOM 1612 C CB . ARG B 1 103 ? 34.522 31.227 32.807 1.00 53.66 ? 103 ARG B CB 1 ATOM 1613 C CG . ARG B 1 103 ? 35.900 31.614 32.312 1.00 59.10 ? 103 ARG B CG 1 ATOM 1614 C CD . ARG B 1 103 ? 36.103 31.138 30.886 1.00 64.06 ? 103 ARG B CD 1 ATOM 1615 N NE . ARG B 1 103 ? 37.408 31.519 30.358 1.00 67.80 ? 103 ARG B NE 1 ATOM 1616 C CZ . ARG B 1 103 ? 37.802 31.286 29.110 1.00 70.13 ? 103 ARG B CZ 1 ATOM 1617 N NH1 . ARG B 1 103 ? 36.988 30.671 28.261 1.00 70.75 ? 103 ARG B NH1 1 ATOM 1618 N NH2 . ARG B 1 103 ? 39.008 31.666 28.710 1.00 70.74 ? 103 ARG B NH2 1 ATOM 1619 N N . ARG B 1 104 ? 31.928 32.736 34.165 1.00 40.44 ? 104 ARG B N 1 ATOM 1620 C CA . ARG B 1 104 ? 30.479 32.762 34.264 1.00 35.50 ? 104 ARG B CA 1 ATOM 1621 C C . ARG B 1 104 ? 30.009 33.042 32.840 1.00 33.32 ? 104 ARG B C 1 ATOM 1622 O O . ARG B 1 104 ? 30.615 33.857 32.139 1.00 30.86 ? 104 ARG B O 1 ATOM 1623 C CB . ARG B 1 104 ? 30.023 33.893 35.187 1.00 38.54 ? 104 ARG B CB 1 ATOM 1624 C CG . ARG B 1 104 ? 30.506 33.766 36.622 1.00 45.98 ? 104 ARG B CG 1 ATOM 1625 C CD . ARG B 1 104 ? 30.225 35.039 37.409 1.00 52.02 ? 104 ARG B CD 1 ATOM 1626 N NE . ARG B 1 104 ? 28.811 35.410 37.371 1.00 58.04 ? 104 ARG B NE 1 ATOM 1627 C CZ . ARG B 1 104 ? 28.306 36.493 37.954 1.00 59.13 ? 104 ARG B CZ 1 ATOM 1628 N NH1 . ARG B 1 104 ? 29.099 37.319 38.627 1.00 58.56 ? 104 ARG B NH1 1 ATOM 1629 N NH2 . ARG B 1 104 ? 27.008 36.754 37.863 1.00 60.49 ? 104 ARG B NH2 1 ATOM 1630 N N . TYR B 1 105 ? 28.950 32.366 32.409 1.00 28.40 ? 105 TYR B N 1 ATOM 1631 C CA . TYR B 1 105 ? 28.427 32.566 31.061 1.00 26.79 ? 105 TYR B CA 1 ATOM 1632 C C . TYR B 1 105 ? 27.032 33.171 31.085 1.00 23.96 ? 105 TYR B C 1 ATOM 1633 O O . TYR B 1 105 ? 26.129 32.637 31.723 1.00 23.73 ? 105 TYR B O 1 ATOM 1634 C CB . TYR B 1 105 ? 28.346 31.240 30.294 1.00 26.92 ? 105 TYR B CB 1 ATOM 1635 C CG . TYR B 1 105 ? 29.661 30.558 30.029 1.00 27.68 ? 105 TYR B CG 1 ATOM 1636 C CD1 . TYR B 1 105 ? 30.305 29.824 31.028 1.00 29.63 ? 105 TYR B CD1 1 ATOM 1637 C CD2 . TYR B 1 105 ? 30.259 30.628 28.771 1.00 29.10 ? 105 TYR B CD2 1 ATOM 1638 C CE1 . TYR B 1 105 ? 31.511 29.173 30.775 1.00 30.73 ? 105 TYR B CE1 1 ATOM 1639 C CE2 . TYR B 1 105 ? 31.462 29.987 28.508 1.00 30.50 ? 105 TYR B CE2 1 ATOM 1640 C CZ . TYR B 1 105 ? 32.083 29.259 29.512 1.00 31.69 ? 105 TYR B CZ 1 ATOM 1641 O OH . TYR B 1 105 ? 33.272 28.614 29.250 1.00 31.63 ? 105 TYR B OH 1 ATOM 1642 N N . THR B 1 106 ? 26.860 34.288 30.391 1.00 21.21 ? 106 THR B N 1 ATOM 1643 C CA . THR B 1 106 ? 25.558 34.918 30.296 1.00 20.41 ? 106 THR B CA 1 ATOM 1644 C C . THR B 1 106 ? 25.198 34.905 28.820 1.00 22.12 ? 106 THR B C 1 ATOM 1645 O O . THR B 1 106 ? 25.923 35.456 27.989 1.00 21.19 ? 106 THR B O 1 ATOM 1646 C CB . THR B 1 106 ? 25.563 36.375 30.796 1.00 22.80 ? 106 THR B CB 1 ATOM 1647 O OG1 . THR B 1 106 ? 25.890 36.409 32.189 1.00 24.59 ? 106 THR B OG1 1 ATOM 1648 C CG2 . THR B 1 106 ? 24.189 36.994 30.609 1.00 27.82 ? 106 THR B CG2 1 ATOM 1649 N N . ILE B 1 107 ? 24.096 34.238 28.498 1.00 19.63 ? 107 ILE B N 1 ATOM 1650 C CA . ILE B 1 107 ? 23.626 34.155 27.126 1.00 21.11 ? 107 ILE B CA 1 ATOM 1651 C C . ILE B 1 107 ? 22.453 35.114 27.008 1.00 19.92 ? 107 ILE B C 1 ATOM 1652 O O . ILE B 1 107 ? 21.446 34.953 27.694 1.00 21.33 ? 107 ILE B O 1 ATOM 1653 C CB . ILE B 1 107 ? 23.141 32.731 26.787 1.00 21.62 ? 107 ILE B CB 1 ATOM 1654 C CG1 . ILE B 1 107 ? 24.281 31.725 26.979 1.00 24.05 ? 107 ILE B CG1 1 ATOM 1655 C CG2 . ILE B 1 107 ? 22.626 32.682 25.358 1.00 22.03 ? 107 ILE B CG2 1 ATOM 1656 C CD1 . ILE B 1 107 ? 25.470 31.950 26.071 1.00 26.85 ? 107 ILE B CD1 1 ATOM 1657 N N . ALA B 1 108 ? 22.584 36.113 26.145 1.00 20.30 ? 108 ALA B N 1 ATOM 1658 C CA . ALA B 1 108 ? 21.516 37.080 25.968 1.00 21.24 ? 108 ALA B CA 1 ATOM 1659 C C . ALA B 1 108 ? 20.925 36.980 24.574 1.00 19.32 ? 108 ALA B C 1 ATOM 1660 O O . ALA B 1 108 ? 21.636 36.725 23.607 1.00 22.18 ? 108 ALA B O 1 ATOM 1661 C CB . ALA B 1 108 ? 22.045 38.480 26.210 1.00 21.56 ? 108 ALA B CB 1 ATOM 1662 N N . ALA B 1 109 ? 19.616 37.168 24.486 1.00 18.61 ? 109 ALA B N 1 ATOM 1663 C CA . ALA B 1 109 ? 18.920 37.123 23.212 1.00 19.16 ? 109 ALA B CA 1 ATOM 1664 C C . ALA B 1 109 ? 17.953 38.300 23.124 1.00 18.32 ? 109 ALA B C 1 ATOM 1665 O O . ALA B 1 109 ? 17.257 38.616 24.090 1.00 19.87 ? 109 ALA B O 1 ATOM 1666 C CB . ALA B 1 109 ? 18.164 35.821 23.076 1.00 20.81 ? 109 ALA B CB 1 ATOM 1667 N N . LEU B 1 110 ? 17.933 38.950 21.963 1.00 17.33 ? 110 LEU B N 1 ATOM 1668 C CA . LEU B 1 110 ? 17.055 40.085 21.697 1.00 17.50 ? 110 LEU B CA 1 ATOM 1669 C C . LEU B 1 110 ? 16.116 39.557 20.623 1.00 15.90 ? 110 LEU B C 1 ATOM 1670 O O . LEU B 1 110 ? 16.561 39.166 19.546 1.00 18.24 ? 110 LEU B O 1 ATOM 1671 C CB . LEU B 1 110 ? 17.874 41.271 21.168 1.00 17.25 ? 110 LEU B CB 1 ATOM 1672 C CG . LEU B 1 110 ? 17.102 42.536 20.782 1.00 21.37 ? 110 LEU B CG 1 ATOM 1673 C CD1 . LEU B 1 110 ? 16.230 43.007 21.946 1.00 20.96 ? 110 LEU B CD1 1 ATOM 1674 C CD2 . LEU B 1 110 ? 18.097 43.619 20.377 1.00 22.70 ? 110 LEU B CD2 1 ATOM 1675 N N . LEU B 1 111 ? 14.821 39.555 20.905 1.00 16.42 ? 111 LEU B N 1 ATOM 1676 C CA . LEU B 1 111 ? 13.865 38.985 19.971 1.00 15.95 ? 111 LEU B CA 1 ATOM 1677 C C . LEU B 1 111 ? 12.936 39.917 19.211 1.00 16.91 ? 111 LEU B C 1 ATOM 1678 O O . LEU B 1 111 ? 12.398 40.870 19.769 1.00 16.41 ? 111 LEU B O 1 ATOM 1679 C CB . LEU B 1 111 ? 12.997 37.967 20.714 1.00 15.64 ? 111 LEU B CB 1 ATOM 1680 C CG . LEU B 1 111 ? 13.661 36.945 21.638 1.00 18.30 ? 111 LEU B CG 1 ATOM 1681 C CD1 . LEU B 1 111 ? 12.569 36.119 22.320 1.00 18.14 ? 111 LEU B CD1 1 ATOM 1682 C CD2 . LEU B 1 111 ? 14.608 36.037 20.837 1.00 15.44 ? 111 LEU B CD2 1 ATOM 1683 N N . SER B 1 112 ? 12.759 39.606 17.927 1.00 16.74 ? 112 SER B N 1 ATOM 1684 C CA . SER B 1 112 ? 11.830 40.306 17.048 1.00 18.19 ? 112 SER B CA 1 ATOM 1685 C C . SER B 1 112 ? 11.133 39.182 16.276 1.00 17.93 ? 112 SER B C 1 ATOM 1686 O O . SER B 1 112 ? 11.646 38.068 16.201 1.00 16.01 ? 112 SER B O 1 ATOM 1687 C CB . SER B 1 112 ? 12.558 41.243 16.084 1.00 18.16 ? 112 SER B CB 1 ATOM 1688 O OG . SER B 1 112 ? 13.024 42.396 16.764 1.00 25.18 ? 112 SER B OG 1 ATOM 1689 N N . PRO B 1 113 ? 9.954 39.452 15.700 1.00 19.11 ? 113 PRO B N 1 ATOM 1690 C CA . PRO B 1 113 ? 9.243 38.406 14.952 1.00 18.13 ? 113 PRO B CA 1 ATOM 1691 C C . PRO B 1 113 ? 10.039 37.715 13.836 1.00 19.48 ? 113 PRO B C 1 ATOM 1692 O O . PRO B 1 113 ? 9.960 36.493 13.663 1.00 16.31 ? 113 PRO B O 1 ATOM 1693 C CB . PRO B 1 113 ? 8.012 39.146 14.427 1.00 19.92 ? 113 PRO B CB 1 ATOM 1694 C CG . PRO B 1 113 ? 7.723 40.107 15.545 1.00 19.19 ? 113 PRO B CG 1 ATOM 1695 C CD . PRO B 1 113 ? 9.106 40.645 15.871 1.00 18.48 ? 113 PRO B CD 1 ATOM 1696 N N . TYR B 1 114 ? 10.806 38.487 13.076 1.00 15.90 ? 114 TYR B N 1 ATOM 1697 C CA . TYR B 1 114 ? 11.584 37.915 11.986 1.00 16.90 ? 114 TYR B CA 1 ATOM 1698 C C . TYR B 1 114 ? 13.081 38.038 12.170 1.00 16.60 ? 114 TYR B C 1 ATOM 1699 O O . TYR B 1 114 ? 13.849 37.896 11.217 1.00 19.54 ? 114 TYR B O 1 ATOM 1700 C CB . TYR B 1 114 ? 11.196 38.566 10.660 1.00 16.41 ? 114 TYR B CB 1 ATOM 1701 C CG . TYR B 1 114 ? 9.885 38.058 10.099 1.00 20.40 ? 114 TYR B CG 1 ATOM 1702 C CD1 . TYR B 1 114 ? 8.675 38.372 10.716 1.00 23.57 ? 114 TYR B CD1 1 ATOM 1703 C CD2 . TYR B 1 114 ? 9.857 37.250 8.959 1.00 21.08 ? 114 TYR B CD2 1 ATOM 1704 C CE1 . TYR B 1 114 ? 7.467 37.900 10.218 1.00 27.10 ? 114 TYR B CE1 1 ATOM 1705 C CE2 . TYR B 1 114 ? 8.644 36.766 8.449 1.00 25.97 ? 114 TYR B CE2 1 ATOM 1706 C CZ . TYR B 1 114 ? 7.455 37.099 9.087 1.00 26.86 ? 114 TYR B CZ 1 ATOM 1707 O OH . TYR B 1 114 ? 6.247 36.650 8.599 1.00 31.89 ? 114 TYR B OH 1 ATOM 1708 N N . SER B 1 115 ? 13.509 38.287 13.396 1.00 16.70 ? 115 SER B N 1 ATOM 1709 C CA . SER B 1 115 ? 14.925 38.442 13.635 1.00 16.90 ? 115 SER B CA 1 ATOM 1710 C C . SER B 1 115 ? 15.272 38.288 15.106 1.00 16.27 ? 115 SER B C 1 ATOM 1711 O O . SER B 1 115 ? 14.445 38.506 15.979 1.00 18.57 ? 115 SER B O 1 ATOM 1712 C CB . SER B 1 115 ? 15.362 39.835 13.158 1.00 18.73 ? 115 SER B CB 1 ATOM 1713 O OG . SER B 1 115 ? 16.709 40.094 13.508 1.00 23.04 ? 115 SER B OG 1 ATOM 1714 N N . TYR B 1 116 ? 16.497 37.875 15.374 1.00 17.26 ? 116 TYR B N 1 ATOM 1715 C CA . TYR B 1 116 ? 16.945 37.798 16.753 1.00 18.30 ? 116 TYR B CA 1 ATOM 1716 C C . TYR B 1 116 ? 18.444 37.894 16.765 1.00 17.84 ? 116 TYR B C 1 ATOM 1717 O O . TYR B 1 116 ? 19.117 37.560 15.790 1.00 16.08 ? 116 TYR B O 1 ATOM 1718 C CB . TYR B 1 116 ? 16.447 36.529 17.454 1.00 17.29 ? 116 TYR B CB 1 ATOM 1719 C CG . TYR B 1 116 ? 17.013 35.227 16.948 1.00 21.94 ? 116 TYR B CG 1 ATOM 1720 C CD1 . TYR B 1 116 ? 18.262 34.776 17.365 1.00 19.71 ? 116 TYR B CD1 1 ATOM 1721 C CD2 . TYR B 1 116 ? 16.282 34.432 16.065 1.00 23.50 ? 116 TYR B CD2 1 ATOM 1722 C CE1 . TYR B 1 116 ? 18.773 33.560 16.915 1.00 23.86 ? 116 TYR B CE1 1 ATOM 1723 C CE2 . TYR B 1 116 ? 16.779 33.220 15.609 1.00 25.59 ? 116 TYR B CE2 1 ATOM 1724 C CZ . TYR B 1 116 ? 18.023 32.791 16.038 1.00 25.93 ? 116 TYR B CZ 1 ATOM 1725 O OH . TYR B 1 116 ? 18.513 31.586 15.592 1.00 31.03 ? 116 TYR B OH 1 ATOM 1726 N N . SER B 1 117 ? 18.960 38.417 17.863 1.00 15.10 ? 117 SER B N 1 ATOM 1727 C CA . SER B 1 117 ? 20.381 38.575 18.029 1.00 17.76 ? 117 SER B CA 1 ATOM 1728 C C . SER B 1 117 ? 20.691 37.866 19.324 1.00 18.87 ? 117 SER B C 1 ATOM 1729 O O . SER B 1 117 ? 19.856 37.820 20.233 1.00 17.85 ? 117 SER B O 1 ATOM 1730 C CB . SER B 1 117 ? 20.741 40.056 18.161 1.00 21.75 ? 117 SER B CB 1 ATOM 1731 O OG . SER B 1 117 ? 20.301 40.785 17.024 1.00 32.01 ? 117 SER B OG 1 ATOM 1732 N N . THR B 1 118 ? 21.876 37.288 19.402 1.00 16.79 ? 118 THR B N 1 ATOM 1733 C CA . THR B 1 118 ? 22.276 36.629 20.624 1.00 20.05 ? 118 THR B CA 1 ATOM 1734 C C . THR B 1 118 ? 23.721 36.988 20.864 1.00 18.81 ? 118 THR B C 1 ATOM 1735 O O . THR B 1 118 ? 24.519 37.062 19.932 1.00 20.81 ? 118 THR B O 1 ATOM 1736 C CB . THR B 1 118 ? 22.124 35.098 20.555 1.00 20.23 ? 118 THR B CB 1 ATOM 1737 O OG1 . THR B 1 118 ? 22.475 34.543 21.829 1.00 24.36 ? 118 THR B OG1 1 ATOM 1738 C CG2 . THR B 1 118 ? 23.035 34.497 19.484 1.00 18.72 ? 118 THR B CG2 1 ATOM 1739 N N . THR B 1 119 ? 24.054 37.244 22.118 1.00 17.84 ? 119 THR B N 1 ATOM 1740 C CA . THR B 1 119 ? 25.416 37.594 22.446 1.00 17.35 ? 119 THR B CA 1 ATOM 1741 C C . THR B 1 119 ? 25.779 36.856 23.714 1.00 19.05 ? 119 THR B C 1 ATOM 1742 O O . THR B 1 119 ? 24.911 36.469 24.500 1.00 18.18 ? 119 THR B O 1 ATOM 1743 C CB . THR B 1 119 ? 25.573 39.124 22.658 1.00 22.01 ? 119 THR B CB 1 ATOM 1744 O OG1 . THR B 1 119 ? 26.961 39.450 22.799 1.00 24.67 ? 119 THR B OG1 1 ATOM 1745 C CG2 . THR B 1 119 ? 24.843 39.575 23.904 1.00 26.12 ? 119 THR B CG2 1 ATOM 1746 N N . ALA B 1 120 ? 27.064 36.623 23.894 1.00 17.07 ? 120 ALA B N 1 ATOM 1747 C CA . ALA B 1 120 ? 27.521 35.940 25.086 1.00 19.25 ? 120 ALA B CA 1 ATOM 1748 C C . ALA B 1 120 ? 28.489 36.846 25.816 1.00 20.26 ? 120 ALA B C 1 ATOM 1749 O O . ALA B 1 120 ? 29.358 37.467 25.208 1.00 20.81 ? 120 ALA B O 1 ATOM 1750 C CB . ALA B 1 120 ? 28.207 34.637 24.713 1.00 18.27 ? 120 ALA B CB 1 ATOM 1751 N N . VAL B 1 121 ? 28.306 36.951 27.123 1.00 21.14 ? 121 VAL B N 1 ATOM 1752 C CA . VAL B 1 121 ? 29.196 37.746 27.943 1.00 24.19 ? 121 VAL B CA 1 ATOM 1753 C C . VAL B 1 121 ? 29.838 36.728 28.872 1.00 24.83 ? 121 VAL B C 1 ATOM 1754 O O . VAL B 1 121 ? 29.148 36.067 29.645 1.00 24.50 ? 121 VAL B O 1 ATOM 1755 C CB . VAL B 1 121 ? 28.435 38.783 28.782 1.00 25.31 ? 121 VAL B CB 1 ATOM 1756 C CG1 . VAL B 1 121 ? 29.430 39.684 29.507 1.00 28.09 ? 121 VAL B CG1 1 ATOM 1757 C CG2 . VAL B 1 121 ? 27.524 39.607 27.891 1.00 29.06 ? 121 VAL B CG2 1 ATOM 1758 N N . VAL B 1 122 ? 31.150 36.572 28.762 1.00 26.36 ? 122 VAL B N 1 ATOM 1759 C CA . VAL B 1 122 ? 31.866 35.627 29.606 1.00 29.88 ? 122 VAL B CA 1 ATOM 1760 C C . VAL B 1 122 ? 32.782 36.427 30.524 1.00 32.28 ? 122 VAL B C 1 ATOM 1761 O O . VAL B 1 122 ? 33.688 37.117 30.057 1.00 30.69 ? 122 VAL B O 1 ATOM 1762 C CB . VAL B 1 122 ? 32.700 34.644 28.753 1.00 30.57 ? 122 VAL B CB 1 ATOM 1763 C CG1 . VAL B 1 122 ? 33.356 33.595 29.647 1.00 34.97 ? 122 VAL B CG1 1 ATOM 1764 C CG2 . VAL B 1 122 ? 31.804 33.975 27.715 1.00 30.66 ? 122 VAL B CG2 1 ATOM 1765 N N . THR B 1 123 ? 32.527 36.342 31.826 1.00 33.74 ? 123 THR B N 1 ATOM 1766 C CA . THR B 1 123 ? 33.316 37.065 32.818 1.00 38.26 ? 123 THR B CA 1 ATOM 1767 C C . THR B 1 123 ? 33.831 36.144 33.917 1.00 40.46 ? 123 THR B C 1 ATOM 1768 O O . THR B 1 123 ? 35.034 36.237 34.244 1.00 43.41 ? 123 THR B O 1 ATOM 1769 C CB . THR B 1 123 ? 32.490 38.182 33.473 1.00 38.29 ? 123 THR B CB 1 ATOM 1770 O OG1 . THR B 1 123 ? 31.311 37.617 34.058 1.00 41.71 ? 123 THR B OG1 1 ATOM 1771 C CG2 . THR B 1 123 ? 32.092 39.227 32.441 1.00 40.52 ? 123 THR B CG2 1 HETATM 1772 F F1 A BPD C 2 . ? 21.763 40.800 8.237 0.28 33.30 ? 125 BPD A F1 1 HETATM 1773 F F1 B BPD C 2 . ? 21.211 40.857 24.214 0.28 33.32 ? 125 BPD A F1 1 HETATM 1774 F F2 A BPD C 2 . ? 22.059 42.341 9.629 0.28 32.19 ? 125 BPD A F2 1 HETATM 1775 F F2 B BPD C 2 . ? 21.141 42.424 22.820 0.28 33.04 ? 125 BPD A F2 1 HETATM 1776 F F3 A BPD C 2 . ? 23.584 41.887 8.222 0.28 33.76 ? 125 BPD A F3 1 HETATM 1777 F F3 B BPD C 2 . ? 19.584 42.220 24.250 0.28 33.63 ? 125 BPD A F3 1 HETATM 1778 O O1 A BPD C 2 . ? 22.279 43.005 0.908 0.28 35.73 ? 125 BPD A O1 1 HETATM 1779 O O1 B BPD C 2 . ? 21.174 43.106 31.538 0.28 36.38 ? 125 BPD A O1 1 HETATM 1780 O O2 A BPD C 2 . ? 19.953 40.311 -1.376 0.28 34.84 ? 125 BPD A O2 1 HETATM 1781 O O2 B BPD C 2 . ? 23.080 40.075 33.788 0.28 35.38 ? 125 BPD A O2 1 HETATM 1782 O O3 A BPD C 2 . ? 21.720 41.607 -1.314 0.28 35.02 ? 125 BPD A O3 1 HETATM 1783 O O3 B BPD C 2 . ? 21.544 41.640 33.755 0.28 34.50 ? 125 BPD A O3 1 HETATM 1784 O O4 A BPD C 2 . ? 25.824 44.233 -0.891 0.28 35.12 ? 125 BPD A O4 1 HETATM 1785 O O4 B BPD C 2 . ? 17.903 44.884 33.398 0.28 35.75 ? 125 BPD A O4 1 HETATM 1786 O O5 A BPD C 2 . ? 23.845 43.253 -1.023 0.28 37.11 ? 125 BPD A O5 1 HETATM 1787 O O5 B BPD C 2 . ? 19.700 43.596 33.496 0.28 37.05 ? 125 BPD A O5 1 HETATM 1788 N N1 A BPD C 2 . ? 21.606 43.599 3.619 0.28 34.35 ? 125 BPD A N1 1 HETATM 1789 N N1 B BPD C 2 . ? 21.888 43.588 28.817 0.28 34.22 ? 125 BPD A N1 1 HETATM 1790 C C1 A BPD C 2 . ? 22.290 41.999 8.373 0.28 33.58 ? 125 BPD A C1 1 HETATM 1791 C C1 B BPD C 2 . ? 20.878 42.124 24.081 0.28 33.98 ? 125 BPD A C1 1 HETATM 1792 C C2 A BPD C 2 . ? 21.703 42.976 7.400 0.28 33.64 ? 125 BPD A C2 1 HETATM 1793 C C2 B BPD C 2 . ? 21.628 42.993 25.041 0.28 33.54 ? 125 BPD A C2 1 HETATM 1794 C C3 A BPD C 2 . ? 20.919 44.064 7.855 0.28 34.06 ? 125 BPD A C3 1 HETATM 1795 C C3 B BPD C 2 . ? 22.568 43.942 24.571 0.28 34.60 ? 125 BPD A C3 1 HETATM 1796 C C4 A BPD C 2 . ? 20.379 44.969 6.937 0.28 33.62 ? 125 BPD A C4 1 HETATM 1797 C C4 B BPD C 2 . ? 23.262 44.748 25.479 0.28 33.74 ? 125 BPD A C4 1 HETATM 1798 C C5 A BPD C 2 . ? 20.604 44.817 5.554 0.28 34.30 ? 125 BPD A C5 1 HETATM 1799 C C5 B BPD C 2 . ? 23.039 44.631 26.866 0.28 34.49 ? 125 BPD A C5 1 HETATM 1800 C C6 A BPD C 2 . ? 21.384 43.738 5.080 0.28 34.12 ? 125 BPD A C6 1 HETATM 1801 C C6 B BPD C 2 . ? 22.105 43.691 27.354 0.28 34.16 ? 125 BPD A C6 1 HETATM 1802 C C7 A BPD C 2 . ? 21.943 42.803 6.005 0.28 33.92 ? 125 BPD A C7 1 HETATM 1803 C C7 B BPD C 2 . ? 21.388 42.859 26.440 0.28 33.89 ? 125 BPD A C7 1 HETATM 1804 C C8 A BPD C 2 . ? 20.801 42.654 2.847 0.28 34.41 ? 125 BPD A C8 1 HETATM 1805 C C8 B BPD C 2 . ? 22.545 42.527 29.578 0.28 34.75 ? 125 BPD A C8 1 HETATM 1806 C C9 A BPD C 2 . ? 19.666 41.988 3.384 0.28 34.70 ? 125 BPD A C9 1 HETATM 1807 C C9 B BPD C 2 . ? 23.552 41.690 29.024 0.28 34.70 ? 125 BPD A C9 1 HETATM 1808 C C10 A BPD C 2 . ? 18.915 41.082 2.602 0.28 34.43 ? 125 BPD A C10 1 HETATM 1809 C C10 B BPD C 2 . ? 24.163 40.678 29.795 0.28 34.89 ? 125 BPD A C10 1 HETATM 1810 C C11 A BPD C 2 . ? 19.279 40.830 1.294 0.28 35.23 ? 125 BPD A C11 1 HETATM 1811 C C11 B BPD C 2 . ? 23.785 40.488 31.109 0.28 34.98 ? 125 BPD A C11 1 HETATM 1812 C C12 A BPD C 2 . ? 20.402 41.454 0.686 0.28 34.87 ? 125 BPD A C12 1 HETATM 1813 C C12 B BPD C 2 . ? 22.786 41.279 31.734 0.28 35.25 ? 125 BPD A C12 1 HETATM 1814 C C13 A BPD C 2 . ? 21.168 42.377 1.482 0.28 34.98 ? 125 BPD A C13 1 HETATM 1815 C C13 B BPD C 2 . ? 22.163 42.311 30.949 0.28 35.22 ? 125 BPD A C13 1 HETATM 1816 C C14 A BPD C 2 . ? 20.659 41.062 -0.760 0.28 35.09 ? 125 BPD A C14 1 HETATM 1817 C C14 B BPD C 2 . ? 22.494 40.931 33.184 0.28 35.12 ? 125 BPD A C14 1 HETATM 1818 C C16 A BPD C 2 . ? 22.866 44.078 3.053 0.28 34.25 ? 125 BPD A C16 1 HETATM 1819 C C16 B BPD C 2 . ? 20.730 44.260 29.404 0.28 34.69 ? 125 BPD A C16 1 HETATM 1820 C C17 A BPD C 2 . ? 23.815 44.850 3.781 0.28 34.26 ? 125 BPD A C17 1 HETATM 1821 C C17 B BPD C 2 . ? 19.904 45.172 28.691 0.28 33.76 ? 125 BPD A C17 1 HETATM 1822 C C18 A BPD C 2 . ? 25.009 45.284 3.182 0.28 34.23 ? 125 BPD A C18 1 HETATM 1823 C C18 B BPD C 2 . ? 18.806 45.789 29.310 0.28 34.78 ? 125 BPD A C18 1 HETATM 1824 C C19 A BPD C 2 . ? 25.300 44.976 1.862 0.28 34.84 ? 125 BPD A C19 1 HETATM 1825 C C19 B BPD C 2 . ? 18.490 45.531 30.635 0.28 34.50 ? 125 BPD A C19 1 HETATM 1826 C C20 A BPD C 2 . ? 24.403 44.211 1.068 0.28 35.41 ? 125 BPD A C20 1 HETATM 1827 C C20 B BPD C 2 . ? 19.267 44.633 31.415 0.28 35.29 ? 125 BPD A C20 1 HETATM 1828 C C21 A BPD C 2 . ? 23.168 43.756 1.675 0.28 34.86 ? 125 BPD A C21 1 HETATM 1829 C C21 B BPD C 2 . ? 20.403 43.988 30.786 0.28 35.04 ? 125 BPD A C21 1 HETATM 1830 C C22 A BPD C 2 . ? 24.806 43.925 -0.366 0.28 35.88 ? 125 BPD A C22 1 HETATM 1831 C C22 B BPD C 2 . ? 18.848 44.415 32.855 0.28 35.54 ? 125 BPD A C22 1 HETATM 1832 O O . HOH D 3 . ? 29.660 34.641 14.748 1.00 15.40 ? 126 HOH A O 1 HETATM 1833 O O . HOH D 3 . ? 30.390 33.290 17.285 1.00 25.39 ? 127 HOH A O 1 HETATM 1834 O O . HOH D 3 . ? 32.704 28.251 7.348 1.00 19.22 ? 128 HOH A O 1 HETATM 1835 O O . HOH D 3 . ? 24.571 29.082 17.943 1.00 18.92 ? 129 HOH A O 1 HETATM 1836 O O . HOH D 3 . ? 27.276 40.794 15.058 1.00 23.45 ? 130 HOH A O 1 HETATM 1837 O O . HOH D 3 . ? 31.256 31.174 15.635 1.00 19.57 ? 131 HOH A O 1 HETATM 1838 O O . HOH D 3 . ? 6.933 16.026 3.177 1.00 26.31 ? 132 HOH A O 1 HETATM 1839 O O . HOH D 3 . ? 35.824 46.843 5.149 1.00 25.31 ? 133 HOH A O 1 HETATM 1840 O O . HOH D 3 . ? 16.787 34.521 10.193 1.00 23.76 ? 134 HOH A O 1 HETATM 1841 O O . HOH D 3 . ? 8.300 30.601 9.008 1.00 25.05 ? 135 HOH A O 1 HETATM 1842 O O . HOH D 3 . ? 20.846 30.445 16.087 1.00 31.28 ? 136 HOH A O 1 HETATM 1843 O O . HOH D 3 . ? 9.273 28.522 -2.878 1.00 35.38 ? 137 HOH A O 1 HETATM 1844 O O . HOH D 3 . ? 23.019 19.556 4.058 1.00 28.84 ? 138 HOH A O 1 HETATM 1845 O O . HOH D 3 . ? 37.864 33.351 7.177 1.00 34.72 ? 139 HOH A O 1 HETATM 1846 O O . HOH D 3 . ? 17.914 28.709 -3.810 1.00 26.94 ? 140 HOH A O 1 HETATM 1847 O O . HOH D 3 . ? 40.651 35.017 19.694 1.00 43.44 ? 141 HOH A O 1 HETATM 1848 O O . HOH D 3 . ? 35.001 29.610 6.714 1.00 37.92 ? 142 HOH A O 1 HETATM 1849 O O . HOH D 3 . ? 26.087 31.639 -4.766 1.00 34.03 ? 143 HOH A O 1 HETATM 1850 O O . HOH D 3 . ? 18.124 18.231 -2.117 1.00 40.72 ? 144 HOH A O 1 HETATM 1851 O O . HOH D 3 . ? 9.713 19.033 7.137 1.00 29.77 ? 145 HOH A O 1 HETATM 1852 O O . HOH D 3 . ? 28.822 30.757 -3.636 1.00 37.12 ? 146 HOH A O 1 HETATM 1853 O O . HOH D 3 . ? 35.414 37.330 4.502 1.00 33.93 ? 147 HOH A O 1 HETATM 1854 O O . HOH D 3 . ? 34.629 25.490 6.006 1.00 44.97 ? 148 HOH A O 1 HETATM 1855 O O . HOH D 3 . ? 13.995 41.433 8.119 1.00 34.56 ? 149 HOH A O 1 HETATM 1856 O O . HOH D 3 . ? 23.350 18.612 1.502 1.00 40.69 ? 150 HOH A O 1 HETATM 1857 O O . HOH D 3 . ? -0.460 24.098 3.295 1.00 45.35 ? 151 HOH A O 1 HETATM 1858 O O . HOH E 3 . ? 12.295 35.833 17.760 1.00 18.53 ? 125 HOH B O 1 HETATM 1859 O O . HOH E 3 . ? 15.884 41.639 17.314 1.00 25.99 ? 126 HOH B O 1 HETATM 1860 O O . HOH E 3 . ? 25.041 33.816 22.403 1.00 24.06 ? 127 HOH B O 1 HETATM 1861 O O . HOH E 3 . ? 11.372 34.534 15.289 1.00 22.09 ? 128 HOH B O 1 HETATM 1862 O O . HOH E 3 . ? 16.550 29.624 14.613 1.00 23.51 ? 129 HOH B O 1 HETATM 1863 O O . HOH E 3 . ? 10.007 32.684 16.759 1.00 25.48 ? 130 HOH B O 1 HETATM 1864 O O . HOH E 3 . ? 8.613 28.706 11.639 1.00 26.92 ? 131 HOH B O 1 HETATM 1865 O O . HOH E 3 . ? 16.209 20.464 28.879 1.00 23.55 ? 132 HOH B O 1 HETATM 1866 O O . HOH E 3 . ? 8.194 29.950 25.300 1.00 29.48 ? 133 HOH B O 1 HETATM 1867 O O . HOH E 3 . ? 11.632 28.357 35.766 1.00 28.86 ? 134 HOH B O 1 HETATM 1868 O O . HOH E 3 . ? 8.127 48.825 27.382 1.00 31.25 ? 135 HOH B O 1 HETATM 1869 O O . HOH E 3 . ? 5.852 48.522 24.882 1.00 39.36 ? 136 HOH B O 1 HETATM 1870 O O . HOH E 3 . ? 28.822 40.449 24.306 1.00 35.60 ? 137 HOH B O 1 HETATM 1871 O O . HOH E 3 . ? 23.478 28.566 36.741 1.00 28.26 ? 138 HOH B O 1 HETATM 1872 O O . HOH E 3 . ? 17.483 41.303 37.301 1.00 49.78 ? 139 HOH B O 1 HETATM 1873 O O . HOH E 3 . ? 29.808 17.768 25.399 1.00 32.14 ? 140 HOH B O 1 HETATM 1874 O O . HOH E 3 . ? 28.769 36.517 32.632 1.00 29.66 ? 141 HOH B O 1 HETATM 1875 O O . HOH E 3 . ? 32.957 28.611 23.210 1.00 34.63 ? 142 HOH B O 1 HETATM 1876 O O . HOH E 3 . ? 34.424 21.850 20.867 1.00 38.13 ? 143 HOH B O 1 HETATM 1877 O O . HOH E 3 . ? 21.651 18.014 34.491 1.00 45.74 ? 144 HOH B O 1 HETATM 1878 O O . HOH E 3 . ? 7.120 39.528 27.871 1.00 33.19 ? 145 HOH B O 1 HETATM 1879 O O . HOH E 3 . ? 36.272 22.339 26.094 1.00 44.86 ? 146 HOH B O 1 HETATM 1880 O O . HOH E 3 . ? 5.054 39.605 7.786 1.00 33.51 ? 147 HOH B O 1 # 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 GLY 1 1 ? ? ? A . n A 1 2 PRO 2 2 ? ? ? A . n A 1 3 THR 3 3 ? ? ? A . n A 1 4 GLY 4 4 ? ? ? A . n A 1 5 THR 5 5 ? ? ? A . n A 1 6 GLY 6 6 ? ? ? A . n A 1 7 GLU 7 7 ? ? ? A . n A 1 8 SER 8 8 ? ? ? A . n A 1 9 LYS 9 9 ? ? ? A . n A 1 10 CYS 10 10 10 CYS CYS A . n A 1 11 PRO 11 11 11 PRO PRO A . n A 1 12 LEU 12 12 12 LEU LEU A . n A 1 13 MET 13 13 13 MET MET A . n A 1 14 VAL 14 14 14 VAL VAL A . n A 1 15 LYS 15 15 15 LYS LYS A . n A 1 16 VAL 16 16 16 VAL VAL A . n A 1 17 LEU 17 17 17 LEU LEU A . n A 1 18 ASP 18 18 18 ASP ASP A . n A 1 19 ALA 19 19 19 ALA ALA A . n A 1 20 VAL 20 20 20 VAL VAL A . n A 1 21 ARG 21 21 21 ARG ARG A . n A 1 22 GLY 22 22 22 GLY GLY A . n A 1 23 SER 23 23 23 SER SER A . n A 1 24 PRO 24 24 24 PRO PRO A . n A 1 25 ALA 25 25 25 ALA ALA A . n A 1 26 ILE 26 26 26 ILE ILE A . n A 1 27 ASN 27 27 27 ASN ASN A . n A 1 28 VAL 28 28 28 VAL VAL A . n A 1 29 ALA 29 29 29 ALA ALA A . n A 1 30 VAL 30 30 30 VAL VAL A . n A 1 31 HIS 31 31 31 HIS HIS A . n A 1 32 VAL 32 32 32 VAL VAL A . n A 1 33 PHE 33 33 33 PHE PHE A . n A 1 34 ARG 34 34 34 ARG ARG A . n A 1 35 LYS 35 35 35 LYS LYS A . n A 1 36 ALA 36 36 36 ALA ALA A . n A 1 37 ALA 37 37 37 ALA ALA A . n A 1 38 ASP 38 38 38 ASP ASP A . n A 1 39 ASP 39 39 39 ASP ASP A . n A 1 40 THR 40 40 40 THR THR A . n A 1 41 TRP 41 41 41 TRP TRP A . n A 1 42 GLU 42 42 42 GLU GLU A . n A 1 43 PRO 43 43 43 PRO PRO A . n A 1 44 PHE 44 44 44 PHE PHE A . n A 1 45 ALA 45 45 45 ALA ALA A . n A 1 46 SER 46 46 46 SER SER A . n A 1 47 GLY 47 47 47 GLY GLY A . n A 1 48 LYS 48 48 48 LYS LYS A . n A 1 49 THR 49 49 49 THR THR A . n A 1 50 SER 50 50 50 SER SER A . n A 1 51 GLU 51 51 51 GLU GLU A . n A 1 52 SER 52 52 52 SER SER A . n A 1 53 GLY 53 53 53 GLY GLY A . n A 1 54 GLU 54 54 54 GLU GLU A . n A 1 55 LEU 55 55 55 LEU LEU A . n A 1 56 HIS 56 56 56 HIS HIS A . n A 1 57 GLY 57 57 57 GLY GLY A . n A 1 58 LEU 58 58 58 LEU LEU A . n A 1 59 THR 59 59 59 THR THR A . n A 1 60 THR 60 60 60 THR THR A . n A 1 61 GLU 61 61 61 GLU GLU A . n A 1 62 GLU 62 62 62 GLU GLU A . n A 1 63 GLN 63 63 63 GLN GLN A . n A 1 64 PHE 64 64 64 PHE PHE A . n A 1 65 VAL 65 65 65 VAL VAL A . n A 1 66 GLU 66 66 66 GLU GLU A . n A 1 67 GLY 67 67 67 GLY GLY A . n A 1 68 ILE 68 68 68 ILE ILE A . n A 1 69 TYR 69 69 69 TYR TYR A . n A 1 70 LYS 70 70 70 LYS LYS A . n A 1 71 VAL 71 71 71 VAL VAL A . n A 1 72 GLU 72 72 72 GLU GLU A . n A 1 73 ILE 73 73 73 ILE ILE A . n A 1 74 ASP 74 74 74 ASP ASP A . n A 1 75 THR 75 75 75 THR THR A . n A 1 76 LYS 76 76 76 LYS LYS A . n A 1 77 SER 77 77 77 SER SER A . n A 1 78 TYR 78 78 78 TYR TYR A . n A 1 79 TRP 79 79 79 TRP TRP A . n A 1 80 LYS 80 80 80 LYS LYS A . n A 1 81 ALA 81 81 81 ALA ALA A . n A 1 82 LEU 82 82 82 LEU LEU A . n A 1 83 GLY 83 83 83 GLY GLY A . n A 1 84 ILE 84 84 84 ILE ILE A . n A 1 85 SER 85 85 85 SER SER A . n A 1 86 PRO 86 86 86 PRO PRO A . n A 1 87 PHE 87 87 87 PHE PHE A . n A 1 88 HIS 88 88 88 HIS HIS A . n A 1 89 GLU 89 89 89 GLU GLU A . n A 1 90 HIS 90 90 90 HIS HIS A . n A 1 91 ALA 91 91 91 ALA ALA A . n A 1 92 GLU 92 92 92 GLU GLU A . n A 1 93 VAL 93 93 93 VAL VAL A . n A 1 94 VAL 94 94 94 VAL VAL A . n A 1 95 PHE 95 95 95 PHE PHE A . n A 1 96 THR 96 96 96 THR THR A . n A 1 97 ALA 97 97 97 ALA ALA A . n A 1 98 ASN 98 98 98 ASN ASN A . n A 1 99 ASP 99 99 99 ASP ASP A . n A 1 100 SER 100 100 100 SER SER A . n A 1 101 GLY 101 101 101 GLY GLY A . n A 1 102 PRO 102 102 102 PRO PRO A . n A 1 103 ARG 103 103 103 ARG ARG A . n A 1 104 ARG 104 104 104 ARG ARG A . n A 1 105 TYR 105 105 105 TYR TYR A . n A 1 106 THR 106 106 106 THR THR A . n A 1 107 ILE 107 107 107 ILE ILE A . n A 1 108 ALA 108 108 108 ALA ALA A . n A 1 109 ALA 109 109 109 ALA ALA A . n A 1 110 LEU 110 110 110 LEU LEU A . n A 1 111 LEU 111 111 111 LEU LEU A . n A 1 112 SER 112 112 112 SER SER A . n A 1 113 PRO 113 113 113 PRO PRO A . n A 1 114 TYR 114 114 114 TYR TYR A . n A 1 115 SER 115 115 115 SER SER A . n A 1 116 TYR 116 116 116 TYR TYR A . n A 1 117 SER 117 117 117 SER SER A . n A 1 118 THR 118 118 118 THR THR A . n A 1 119 THR 119 119 119 THR THR A . n A 1 120 ALA 120 120 120 ALA ALA A . n A 1 121 VAL 121 121 121 VAL VAL A . n A 1 122 VAL 122 122 122 VAL VAL A . n A 1 123 THR 123 123 123 THR THR A . n A 1 124 ASN 124 124 124 ASN ASN A . n B 1 1 GLY 1 1 ? ? ? B . n B 1 2 PRO 2 2 ? ? ? B . n B 1 3 THR 3 3 ? ? ? B . n B 1 4 GLY 4 4 ? ? ? B . n B 1 5 THR 5 5 ? ? ? B . n B 1 6 GLY 6 6 ? ? ? B . n B 1 7 GLU 7 7 ? ? ? B . n B 1 8 SER 8 8 ? ? ? B . n B 1 9 LYS 9 9 ? ? ? B . n B 1 10 CYS 10 10 10 CYS CYS B . n B 1 11 PRO 11 11 11 PRO PRO B . n B 1 12 LEU 12 12 12 LEU LEU B . n B 1 13 MET 13 13 13 MET MET B . n B 1 14 VAL 14 14 14 VAL VAL B . n B 1 15 LYS 15 15 15 LYS LYS B . n B 1 16 VAL 16 16 16 VAL VAL B . n B 1 17 LEU 17 17 17 LEU LEU B . n B 1 18 ASP 18 18 18 ASP ASP B . n B 1 19 ALA 19 19 19 ALA ALA B . n B 1 20 VAL 20 20 20 VAL VAL B . n B 1 21 ARG 21 21 21 ARG ARG B . n B 1 22 GLY 22 22 22 GLY GLY B . n B 1 23 SER 23 23 23 SER SER B . n B 1 24 PRO 24 24 24 PRO PRO B . n B 1 25 ALA 25 25 25 ALA ALA B . n B 1 26 ILE 26 26 26 ILE ILE B . n B 1 27 ASN 27 27 27 ASN ASN B . n B 1 28 VAL 28 28 28 VAL VAL B . n B 1 29 ALA 29 29 29 ALA ALA B . n B 1 30 VAL 30 30 30 VAL VAL B . n B 1 31 HIS 31 31 31 HIS HIS B . n B 1 32 VAL 32 32 32 VAL VAL B . n B 1 33 PHE 33 33 33 PHE PHE B . n B 1 34 ARG 34 34 34 ARG ARG B . n B 1 35 LYS 35 35 35 LYS LYS B . n B 1 36 ALA 36 36 36 ALA ALA B . n B 1 37 ALA 37 37 37 ALA ALA B . n B 1 38 ASP 38 38 38 ASP ASP B . n B 1 39 ASP 39 39 39 ASP ASP B . n B 1 40 THR 40 40 40 THR THR B . n B 1 41 TRP 41 41 41 TRP TRP B . n B 1 42 GLU 42 42 42 GLU GLU B . n B 1 43 PRO 43 43 43 PRO PRO B . n B 1 44 PHE 44 44 44 PHE PHE B . n B 1 45 ALA 45 45 45 ALA ALA B . n B 1 46 SER 46 46 46 SER SER B . n B 1 47 GLY 47 47 47 GLY GLY B . n B 1 48 LYS 48 48 48 LYS LYS B . n B 1 49 THR 49 49 49 THR THR B . n B 1 50 SER 50 50 50 SER SER B . n B 1 51 GLU 51 51 51 GLU GLU B . n B 1 52 SER 52 52 52 SER SER B . n B 1 53 GLY 53 53 53 GLY GLY B . n B 1 54 GLU 54 54 54 GLU GLU B . n B 1 55 LEU 55 55 55 LEU LEU B . n B 1 56 HIS 56 56 56 HIS HIS B . n B 1 57 GLY 57 57 57 GLY GLY B . n B 1 58 LEU 58 58 58 LEU LEU B . n B 1 59 THR 59 59 59 THR THR B . n B 1 60 THR 60 60 60 THR THR B . n B 1 61 GLU 61 61 61 GLU GLU B . n B 1 62 GLU 62 62 62 GLU GLU B . n B 1 63 GLN 63 63 63 GLN GLN B . n B 1 64 PHE 64 64 64 PHE PHE B . n B 1 65 VAL 65 65 65 VAL VAL B . n B 1 66 GLU 66 66 66 GLU GLU B . n B 1 67 GLY 67 67 67 GLY GLY B . n B 1 68 ILE 68 68 68 ILE ILE B . n B 1 69 TYR 69 69 69 TYR TYR B . n B 1 70 LYS 70 70 70 LYS LYS B . n B 1 71 VAL 71 71 71 VAL VAL B . n B 1 72 GLU 72 72 72 GLU GLU B . n B 1 73 ILE 73 73 73 ILE ILE B . n B 1 74 ASP 74 74 74 ASP ASP B . n B 1 75 THR 75 75 75 THR THR B . n B 1 76 LYS 76 76 76 LYS LYS B . n B 1 77 SER 77 77 77 SER SER B . n B 1 78 TYR 78 78 78 TYR TYR B . n B 1 79 TRP 79 79 79 TRP TRP B . n B 1 80 LYS 80 80 80 LYS LYS B . n B 1 81 ALA 81 81 81 ALA ALA B . n B 1 82 LEU 82 82 82 LEU LEU B . n B 1 83 GLY 83 83 83 GLY GLY B . n B 1 84 ILE 84 84 84 ILE ILE B . n B 1 85 SER 85 85 85 SER SER B . n B 1 86 PRO 86 86 86 PRO PRO B . n B 1 87 PHE 87 87 87 PHE PHE B . n B 1 88 HIS 88 88 88 HIS HIS B . n B 1 89 GLU 89 89 89 GLU GLU B . n B 1 90 HIS 90 90 90 HIS HIS B . n B 1 91 ALA 91 91 91 ALA ALA B . n B 1 92 GLU 92 92 92 GLU GLU B . n B 1 93 VAL 93 93 93 VAL VAL B . n B 1 94 VAL 94 94 94 VAL VAL B . n B 1 95 PHE 95 95 95 PHE PHE B . n B 1 96 THR 96 96 96 THR THR B . n B 1 97 ALA 97 97 97 ALA ALA B . n B 1 98 ASN 98 98 98 ASN ASN B . n B 1 99 ASP 99 99 99 ASP ASP B . n B 1 100 SER 100 100 100 SER SER B . n B 1 101 GLY 101 101 101 GLY GLY B . n B 1 102 PRO 102 102 102 PRO PRO B . n B 1 103 ARG 103 103 103 ARG ARG B . n B 1 104 ARG 104 104 104 ARG ARG B . n B 1 105 TYR 105 105 105 TYR TYR B . n B 1 106 THR 106 106 106 THR THR B . n B 1 107 ILE 107 107 107 ILE ILE B . n B 1 108 ALA 108 108 108 ALA ALA B . n B 1 109 ALA 109 109 109 ALA ALA B . n B 1 110 LEU 110 110 110 LEU LEU B . n B 1 111 LEU 111 111 111 LEU LEU B . n B 1 112 SER 112 112 112 SER SER B . n B 1 113 PRO 113 113 113 PRO PRO B . n B 1 114 TYR 114 114 114 TYR TYR B . n B 1 115 SER 115 115 115 SER SER B . n B 1 116 TYR 116 116 116 TYR TYR B . n B 1 117 SER 117 117 117 SER SER B . n B 1 118 THR 118 118 118 THR THR B . n B 1 119 THR 119 119 119 THR THR B . n B 1 120 ALA 120 120 120 ALA ALA B . n B 1 121 VAL 121 121 121 VAL VAL B . n B 1 122 VAL 122 122 122 VAL VAL B . n B 1 123 THR 123 123 123 THR THR B . n B 1 124 ASN 124 124 ? ? ? B . n # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_and_software_defined_assembly _pdbx_struct_assembly.method_details PISA,PQS _pdbx_struct_assembly.oligomeric_details tetrameric _pdbx_struct_assembly.oligomeric_count 4 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1,2 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E # loop_ _pdbx_struct_assembly_prop.biol_id _pdbx_struct_assembly_prop.type _pdbx_struct_assembly_prop.value _pdbx_struct_assembly_prop.details 1 'ABSA (A^2)' 7770 ? 1 MORE -33 ? 1 'SSA (A^2)' 18800 ? # loop_ _pdbx_struct_oper_list.id _pdbx_struct_oper_list.type _pdbx_struct_oper_list.name _pdbx_struct_oper_list.symmetry_operation _pdbx_struct_oper_list.matrix[1][1] _pdbx_struct_oper_list.matrix[1][2] _pdbx_struct_oper_list.matrix[1][3] _pdbx_struct_oper_list.vector[1] _pdbx_struct_oper_list.matrix[2][1] _pdbx_struct_oper_list.matrix[2][2] _pdbx_struct_oper_list.matrix[2][3] _pdbx_struct_oper_list.vector[2] _pdbx_struct_oper_list.matrix[3][1] _pdbx_struct_oper_list.matrix[3][2] _pdbx_struct_oper_list.matrix[3][3] _pdbx_struct_oper_list.vector[3] 1 'identity operation' 1_555 x,y,z 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 2 'crystal symmetry operation' 2_665 -x+1,-y+1,z -1.0000000000 0.0000000000 0.0000000000 43.2900000000 0.0000000000 -1.0000000000 0.0000000000 86.0300000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 # _pdbx_struct_special_symmetry.id 1 _pdbx_struct_special_symmetry.PDB_model_num 1 _pdbx_struct_special_symmetry.auth_asym_id A _pdbx_struct_special_symmetry.auth_comp_id BPD _pdbx_struct_special_symmetry.auth_seq_id 125 _pdbx_struct_special_symmetry.PDB_ins_code ? _pdbx_struct_special_symmetry.label_asym_id C _pdbx_struct_special_symmetry.label_comp_id BPD _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 2001-01-23 2 'Structure model' 1 1 2008-04-27 3 'Structure model' 1 2 2011-07-13 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # 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' 'Version format compliance' 2 3 'Structure model' 'Derived calculations' 3 3 'Structure model' 'Version format compliance' # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal CNS refinement . ? 1 DENZO 'data reduction' . ? 2 SCALEPACK 'data scaling' . ? 3 CNS phasing . ? 4 # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 ASP A 39 ? ? 59.54 18.83 2 1 ASP B 39 ? ? 59.86 19.44 3 1 SER B 100 ? ? -102.56 73.38 # 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 GLY 1 ? A GLY 1 2 1 Y 1 A PRO 2 ? A PRO 2 3 1 Y 1 A THR 3 ? A THR 3 4 1 Y 1 A GLY 4 ? A GLY 4 5 1 Y 1 A THR 5 ? A THR 5 6 1 Y 1 A GLY 6 ? A GLY 6 7 1 Y 1 A GLU 7 ? A GLU 7 8 1 Y 1 A SER 8 ? A SER 8 9 1 Y 1 A LYS 9 ? A LYS 9 10 1 Y 1 B GLY 1 ? B GLY 1 11 1 Y 1 B PRO 2 ? B PRO 2 12 1 Y 1 B THR 3 ? B THR 3 13 1 Y 1 B GLY 4 ? B GLY 4 14 1 Y 1 B THR 5 ? B THR 5 15 1 Y 1 B GLY 6 ? B GLY 6 16 1 Y 1 B GLU 7 ? B GLU 7 17 1 Y 1 B SER 8 ? B SER 8 18 1 Y 1 B LYS 9 ? B LYS 9 19 1 Y 1 B ASN 124 ? B ASN 124 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 'N-(M-TRIFLUOROMETHYLPHENYL) PHENOXAZINE-4,6-DICARBOXYLIC ACID' BPD 3 water HOH # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code C 2 BPD 1 125 1 BPD BPP A . D 3 HOH 1 126 100 HOH WAT A . D 3 HOH 2 127 105 HOH WAT A . D 3 HOH 3 128 106 HOH WAT A . D 3 HOH 4 129 107 HOH WAT A . D 3 HOH 5 130 109 HOH WAT A . D 3 HOH 6 131 110 HOH WAT A . D 3 HOH 7 132 115 HOH WAT A . D 3 HOH 8 133 117 HOH WAT A . D 3 HOH 9 134 119 HOH WAT A . D 3 HOH 10 135 120 HOH WAT A . D 3 HOH 11 136 121 HOH WAT A . D 3 HOH 12 137 122 HOH WAT A . D 3 HOH 13 138 123 HOH WAT A . D 3 HOH 14 139 125 HOH WAT A . D 3 HOH 15 140 126 HOH WAT A . D 3 HOH 16 141 128 HOH WAT A . D 3 HOH 17 142 130 HOH WAT A . D 3 HOH 18 143 132 HOH WAT A . D 3 HOH 19 144 135 HOH WAT A . D 3 HOH 20 145 139 HOH WAT A . D 3 HOH 21 146 140 HOH WAT A . D 3 HOH 22 147 147 HOH WAT A . D 3 HOH 23 148 148 HOH WAT A . D 3 HOH 24 149 150 HOH WAT A . D 3 HOH 25 150 153 HOH WAT A . D 3 HOH 26 151 156 HOH WAT A . E 3 HOH 1 125 101 HOH WAT B . E 3 HOH 2 126 102 HOH WAT B . E 3 HOH 3 127 103 HOH WAT B . E 3 HOH 4 128 104 HOH WAT B . E 3 HOH 5 129 108 HOH WAT B . E 3 HOH 6 130 111 HOH WAT B . E 3 HOH 7 131 112 HOH WAT B . E 3 HOH 8 132 113 HOH WAT B . E 3 HOH 9 133 114 HOH WAT B . E 3 HOH 10 134 116 HOH WAT B . E 3 HOH 11 135 124 HOH WAT B . E 3 HOH 12 136 127 HOH WAT B . E 3 HOH 13 137 131 HOH WAT B . E 3 HOH 14 138 133 HOH WAT B . E 3 HOH 15 139 136 HOH WAT B . E 3 HOH 16 140 137 HOH WAT B . E 3 HOH 17 141 138 HOH WAT B . E 3 HOH 18 142 142 HOH WAT B . E 3 HOH 19 143 144 HOH WAT B . E 3 HOH 20 144 145 HOH WAT B . E 3 HOH 21 145 151 HOH WAT B . E 3 HOH 22 146 152 HOH WAT B . E 3 HOH 23 147 154 HOH WAT B . #