data_1DVT # _entry.id 1DVT # _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 1DVT RCSB RCSB010417 WWPDB D_1000010417 # 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 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 1DVY ;CRYSTAL STRUCTURE OF TRANSTHYRETIN IN COMPLEX WITH N-(M-TRIFLUOROMETHYLPHENYL) PHENOXAZINE-4,6-DICARBOXYLIC ACID ; 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 1DVT _pdbx_database_status.recvd_initial_deposition_date 2000-01-22 _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 1DVT _cell.length_a 43.380 _cell.length_b 85.560 _cell.length_c 64.880 _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 1DVT _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 FLURBIPROFEN 244.261 1 ? ? ? ? 3 water nat water 18.015 57 ? ? ? ? # _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 1DVT A 1 ? 124 ? P02766 1 ? 124 ? 1 124 2 1 1DVT 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 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 FLP non-polymer . FLURBIPROFEN ? 'C15 H13 F O2' 244.261 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 1DVT _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.24 _exptl_crystal.density_percent_sol 45.13 _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 1999-02-02 _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 1DVT _reflns.observed_criterion_sigma_I 0 _reflns.observed_criterion_sigma_F 0 _reflns.d_resolution_low 10 _reflns.d_resolution_high 1.85 _reflns.number_obs 20907 _reflns.number_all 20907 _reflns.percent_possible_obs 98.8 _reflns.pdbx_Rmerge_I_obs 0.0580000 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 10.1 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 3.7 _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_diffrn_id 1 _reflns.pdbx_ordinal 1 # _reflns_shell.d_res_high 1.85 _reflns_shell.d_res_low 1.95 _reflns_shell.percent_possible_all 98.8 _reflns_shell.Rmerge_I_obs 0.3500000 _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_diffrn_id ? _reflns_shell.pdbx_ordinal 1 # _refine.entry_id 1DVT _refine.ls_number_reflns_obs 17529 _refine.ls_number_reflns_all 18509 _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F 2 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.ls_d_res_low 8.0 _refine.ls_d_res_high 1.9 _refine.ls_percent_reflns_obs 90.5 _refine.ls_R_factor_obs ? _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.1970000 _refine.ls_R_factor_R_free 0.2200000 _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 1745 _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 flurbiprofen 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 the 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 36 _refine_hist.number_atoms_solvent 57 _refine_hist.number_atoms_total 1864 _refine_hist.d_res_high 1.9 _refine_hist.d_res_low 8.0 # 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 1.261 ? ? ? 'X-RAY DIFFRACTION' ? c_bond_d 0.006 ? ? ? 'X-RAY DIFFRACTION' ? # _struct.entry_id 1DVT _struct.title 'CRYSTAL STRUCTURE OF HUMAN TRANSTHYRETIN IN COMPLEX WITH FLURBIPROFEN' _struct.pdbx_descriptor 'TRANSTHYRETIN / FLURBIPROFEN COMPLEX' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 1DVT _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 assemble is a tetramer constructed from the dimer (chain A and chain 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 ? LEU A 82 ? ASP A 74 LEU A 82 1 ? 9 HELX_P HELX_P2 2 ASP B 74 ? LEU B 82 ? ASP B 74 LEU B 82 1 ? 9 # _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 17 _struct_site.details 'BINDING SITE FOR RESIDUE FLP 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 17 LYS A 15 ? LYS A 15 . ? 1_555 ? 2 AC1 17 LYS A 15 ? LYS A 15 . ? 2_665 ? 3 AC1 17 LEU A 17 ? LEU A 17 . ? 2_665 ? 4 AC1 17 ALA A 108 ? ALA A 108 . ? 2_665 ? 5 AC1 17 ALA A 108 ? ALA A 108 . ? 1_555 ? 6 AC1 17 ALA A 109 ? ALA A 109 . ? 2_665 ? 7 AC1 17 LEU A 110 ? LEU A 110 . ? 1_555 ? 8 AC1 17 LEU A 110 ? LEU A 110 . ? 2_665 ? 9 AC1 17 SER A 117 ? SER A 117 . ? 2_665 ? 10 AC1 17 LYS B 15 ? LYS B 15 . ? 2_665 ? 11 AC1 17 LEU B 17 ? LEU B 17 . ? 2_665 ? 12 AC1 17 THR B 106 ? THR B 106 . ? 2_665 ? 13 AC1 17 ALA B 108 ? ALA B 108 . ? 2_665 ? 14 AC1 17 ALA B 109 ? ALA B 109 . ? 2_665 ? 15 AC1 17 LEU B 110 ? LEU B 110 . ? 1_555 ? 16 AC1 17 SER B 117 ? SER B 117 . ? 1_555 ? 17 AC1 17 THR B 119 ? THR B 119 . ? 1_555 ? # _database_PDB_matrix.entry_id 1DVT _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 1DVT _atom_sites.fract_transf_matrix[1][1] 0.023052 _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] 0.011688 _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] 0.015413 _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 ? 15.259 30.931 -7.470 1.00 43.20 ? 10 CYS A N 1 ATOM 2 C CA . CYS A 1 10 ? 16.090 31.057 -6.238 1.00 41.96 ? 10 CYS A CA 1 ATOM 3 C C . CYS A 1 10 ? 15.179 31.368 -5.048 1.00 36.40 ? 10 CYS A C 1 ATOM 4 O O . CYS A 1 10 ? 15.080 32.510 -4.600 1.00 36.49 ? 10 CYS A O 1 ATOM 5 C CB . CYS A 1 10 ? 17.128 32.170 -6.418 1.00 46.32 ? 10 CYS A CB 1 ATOM 6 S SG . CYS A 1 10 ? 18.663 31.944 -5.470 1.00 56.60 ? 10 CYS A SG 1 ATOM 7 N N . PRO A 1 11 ? 14.486 30.344 -4.534 1.00 30.47 ? 11 PRO A N 1 ATOM 8 C CA . PRO A 1 11 ? 13.570 30.468 -3.397 1.00 28.13 ? 11 PRO A CA 1 ATOM 9 C C . PRO A 1 11 ? 14.258 30.531 -2.034 1.00 24.45 ? 11 PRO A C 1 ATOM 10 O O . PRO A 1 11 ? 13.638 30.887 -1.035 1.00 23.00 ? 11 PRO A O 1 ATOM 11 C CB . PRO A 1 11 ? 12.688 29.232 -3.540 1.00 27.21 ? 11 PRO A CB 1 ATOM 12 C CG . PRO A 1 11 ? 13.641 28.226 -4.074 1.00 27.45 ? 11 PRO A CG 1 ATOM 13 C CD . PRO A 1 11 ? 14.387 29.001 -5.136 1.00 30.29 ? 11 PRO A CD 1 ATOM 14 N N . LEU A 1 12 ? 15.535 30.168 -1.994 1.00 22.77 ? 12 LEU A N 1 ATOM 15 C CA . LEU A 1 12 ? 16.290 30.190 -0.743 1.00 19.19 ? 12 LEU A CA 1 ATOM 16 C C . LEU A 1 12 ? 17.652 30.820 -0.993 1.00 21.76 ? 12 LEU A C 1 ATOM 17 O O . LEU A 1 12 ? 18.441 30.317 -1.793 1.00 21.54 ? 12 LEU A O 1 ATOM 18 C CB . LEU A 1 12 ? 16.457 28.769 -0.204 1.00 20.03 ? 12 LEU A CB 1 ATOM 19 C CG . LEU A 1 12 ? 17.147 28.600 1.151 1.00 24.15 ? 12 LEU A CG 1 ATOM 20 C CD1 . LEU A 1 12 ? 16.415 29.424 2.206 1.00 20.12 ? 12 LEU A CD1 1 ATOM 21 C CD2 . LEU A 1 12 ? 17.158 27.125 1.527 1.00 21.65 ? 12 LEU A CD2 1 ATOM 22 N N . MET A 1 13 ? 17.921 31.926 -0.309 1.00 18.40 ? 13 MET A N 1 ATOM 23 C CA . MET A 1 13 ? 19.179 32.638 -0.471 1.00 21.10 ? 13 MET A CA 1 ATOM 24 C C . MET A 1 13 ? 19.745 32.913 0.925 1.00 18.88 ? 13 MET A C 1 ATOM 25 O O . MET A 1 13 ? 18.990 33.173 1.857 1.00 14.77 ? 13 MET A O 1 ATOM 26 C CB . MET A 1 13 ? 18.914 33.945 -1.226 1.00 24.59 ? 13 MET A CB 1 ATOM 27 C CG . MET A 1 13 ? 20.075 34.466 -2.057 1.00 38.04 ? 13 MET A CG 1 ATOM 28 S SD . MET A 1 13 ? 21.260 35.447 -1.126 1.00 48.42 ? 13 MET A SD 1 ATOM 29 C CE . MET A 1 13 ? 20.595 37.113 -1.391 1.00 43.62 ? 13 MET A CE 1 ATOM 30 N N . VAL A 1 14 ? 21.065 32.829 1.068 1.00 16.84 ? 14 VAL A N 1 ATOM 31 C CA . VAL A 1 14 ? 21.706 33.075 2.356 1.00 15.37 ? 14 VAL A CA 1 ATOM 32 C C . VAL A 1 14 ? 22.780 34.134 2.156 1.00 17.94 ? 14 VAL A C 1 ATOM 33 O O . VAL A 1 14 ? 23.562 34.067 1.205 1.00 18.41 ? 14 VAL A O 1 ATOM 34 C CB . VAL A 1 14 ? 22.372 31.791 2.924 1.00 16.56 ? 14 VAL A CB 1 ATOM 35 C CG1 . VAL A 1 14 ? 23.105 32.114 4.238 1.00 18.91 ? 14 VAL A CG1 1 ATOM 36 C CG2 . VAL A 1 14 ? 21.316 30.713 3.150 1.00 18.17 ? 14 VAL A CG2 1 ATOM 37 N N . LYS A 1 15 ? 22.804 35.121 3.041 1.00 15.39 ? 15 LYS A N 1 ATOM 38 C CA . LYS A 1 15 ? 23.803 36.171 2.943 1.00 18.01 ? 15 LYS A CA 1 ATOM 39 C C . LYS A 1 15 ? 24.460 36.324 4.299 1.00 18.03 ? 15 LYS A C 1 ATOM 40 O O . LYS A 1 15 ? 23.784 36.427 5.319 1.00 17.63 ? 15 LYS A O 1 ATOM 41 C CB . LYS A 1 15 ? 23.164 37.482 2.500 1.00 21.98 ? 15 LYS A CB 1 ATOM 42 C CG . LYS A 1 15 ? 24.186 38.493 2.004 1.00 30.02 ? 15 LYS A CG 1 ATOM 43 C CD . LYS A 1 15 ? 23.540 39.544 1.127 1.00 36.79 ? 15 LYS A CD 1 ATOM 44 C CE . LYS A 1 15 ? 24.586 40.390 0.413 1.00 39.36 ? 15 LYS A CE 1 ATOM 45 N NZ . LYS A 1 15 ? 25.555 40.985 1.367 1.00 42.39 ? 15 LYS A NZ 1 ATOM 46 N N . VAL A 1 16 ? 25.785 36.339 4.309 1.00 16.30 ? 16 VAL A N 1 ATOM 47 C CA . VAL A 1 16 ? 26.512 36.426 5.559 1.00 16.59 ? 16 VAL A CA 1 ATOM 48 C C . VAL A 1 16 ? 27.487 37.596 5.543 1.00 18.70 ? 16 VAL A C 1 ATOM 49 O O . VAL A 1 16 ? 28.284 37.747 4.614 1.00 16.76 ? 16 VAL A O 1 ATOM 50 C CB . VAL A 1 16 ? 27.291 35.122 5.823 1.00 15.48 ? 16 VAL A CB 1 ATOM 51 C CG1 . VAL A 1 16 ? 27.817 35.104 7.259 1.00 16.14 ? 16 VAL A CG1 1 ATOM 52 C CG2 . VAL A 1 16 ? 26.393 33.914 5.550 1.00 17.47 ? 16 VAL A CG2 1 ATOM 53 N N . LEU A 1 17 ? 27.406 38.428 6.575 1.00 14.61 ? 17 LEU A N 1 ATOM 54 C CA . LEU A 1 17 ? 28.288 39.576 6.687 1.00 16.11 ? 17 LEU A CA 1 ATOM 55 C C . LEU A 1 17 ? 29.170 39.470 7.919 1.00 15.10 ? 17 LEU A C 1 ATOM 56 O O . LEU A 1 17 ? 28.799 38.857 8.925 1.00 15.13 ? 17 LEU A O 1 ATOM 57 C CB . LEU A 1 17 ? 27.482 40.875 6.770 1.00 15.34 ? 17 LEU A CB 1 ATOM 58 C CG . LEU A 1 17 ? 26.563 41.270 5.614 1.00 19.30 ? 17 LEU A CG 1 ATOM 59 C CD1 . LEU A 1 17 ? 25.955 42.621 5.952 1.00 21.07 ? 17 LEU A CD1 1 ATOM 60 C CD2 . LEU A 1 17 ? 27.341 41.368 4.305 1.00 21.48 ? 17 LEU A CD2 1 ATOM 61 N N . ASP A 1 18 ? 30.335 40.101 7.829 1.00 15.22 ? 18 ASP A N 1 ATOM 62 C CA . ASP A 1 18 ? 31.319 40.126 8.905 1.00 16.18 ? 18 ASP A CA 1 ATOM 63 C C . ASP A 1 18 ? 31.276 41.502 9.585 1.00 17.90 ? 18 ASP A C 1 ATOM 64 O O . ASP A 1 18 ? 31.626 42.521 8.973 1.00 16.01 ? 18 ASP A O 1 ATOM 65 C CB . ASP A 1 18 ? 32.699 39.871 8.302 1.00 17.39 ? 18 ASP A CB 1 ATOM 66 C CG . ASP A 1 18 ? 33.791 39.820 9.335 1.00 17.90 ? 18 ASP A CG 1 ATOM 67 O OD1 . ASP A 1 18 ? 33.754 40.616 10.290 1.00 18.50 ? 18 ASP A OD1 1 ATOM 68 O OD2 . ASP A 1 18 ? 34.698 38.984 9.171 1.00 22.08 ? 18 ASP A OD2 1 ATOM 69 N N . ALA A 1 19 ? 30.859 41.526 10.851 1.00 15.04 ? 19 ALA A N 1 ATOM 70 C CA . ALA A 1 19 ? 30.730 42.767 11.603 1.00 15.10 ? 19 ALA A CA 1 ATOM 71 C C . ALA A 1 19 ? 32.058 43.283 12.146 1.00 17.18 ? 19 ALA A C 1 ATOM 72 O O . ALA A 1 19 ? 32.144 44.417 12.597 1.00 16.69 ? 19 ALA A O 1 ATOM 73 C CB . ALA A 1 19 ? 29.724 42.580 12.763 1.00 17.05 ? 19 ALA A CB 1 ATOM 74 N N . VAL A 1 20 ? 33.090 42.449 12.096 1.00 15.50 ? 20 VAL A N 1 ATOM 75 C CA . VAL A 1 20 ? 34.406 42.836 12.594 1.00 18.59 ? 20 VAL A CA 1 ATOM 76 C C . VAL A 1 20 ? 35.234 43.539 11.526 1.00 21.09 ? 20 VAL A C 1 ATOM 77 O O . VAL A 1 20 ? 35.957 44.490 11.813 1.00 19.99 ? 20 VAL A O 1 ATOM 78 C CB . VAL A 1 20 ? 35.197 41.600 13.089 1.00 20.58 ? 20 VAL A CB 1 ATOM 79 C CG1 . VAL A 1 20 ? 36.611 42.000 13.477 1.00 23.21 ? 20 VAL A CG1 1 ATOM 80 C CG2 . VAL A 1 20 ? 34.493 40.978 14.279 1.00 20.19 ? 20 VAL A CG2 1 ATOM 81 N N . ARG A 1 21 ? 35.116 43.076 10.289 1.00 20.49 ? 21 ARG A N 1 ATOM 82 C CA . ARG A 1 21 ? 35.890 43.646 9.200 1.00 22.40 ? 21 ARG A CA 1 ATOM 83 C C . ARG A 1 21 ? 35.096 44.532 8.263 1.00 21.72 ? 21 ARG A C 1 ATOM 84 O O . ARG A 1 21 ? 35.676 45.146 7.367 1.00 20.11 ? 21 ARG A O 1 ATOM 85 C CB . ARG A 1 21 ? 36.544 42.521 8.404 1.00 25.16 ? 21 ARG A CB 1 ATOM 86 C CG . ARG A 1 21 ? 37.440 41.652 9.251 1.00 33.37 ? 21 ARG A CG 1 ATOM 87 C CD . ARG A 1 21 ? 37.435 40.234 8.749 1.00 39.00 ? 21 ARG A CD 1 ATOM 88 N NE . ARG A 1 21 ? 38.234 40.044 7.570 1.00 43.63 ? 21 ARG A NE 1 ATOM 89 C CZ . ARG A 1 21 ? 38.070 39.110 6.640 1.00 48.83 ? 21 ARG A CZ 1 ATOM 90 N NH1 . ARG A 1 21 ? 37.092 38.213 6.690 1.00 51.19 ? 21 ARG A NH1 1 ATOM 91 N NH2 . ARG A 1 21 ? 38.952 39.066 5.658 1.00 50.62 ? 21 ARG A NH2 1 ATOM 92 N N . GLY A 1 22 ? 33.782 44.602 8.468 1.00 19.03 ? 22 GLY A N 1 ATOM 93 C CA . GLY A 1 22 ? 32.943 45.424 7.612 1.00 17.08 ? 22 GLY A CA 1 ATOM 94 C C . GLY A 1 22 ? 32.960 44.901 6.191 1.00 19.71 ? 22 GLY A C 1 ATOM 95 O O . GLY A 1 22 ? 33.100 45.660 5.223 1.00 18.59 ? 22 GLY A O 1 ATOM 96 N N . SER A 1 23 ? 32.802 43.591 6.053 1.00 17.85 ? 23 SER A N 1 ATOM 97 C CA . SER A 1 23 ? 32.828 42.991 4.736 1.00 19.44 ? 23 SER A CA 1 ATOM 98 C C . SER A 1 23 ? 31.951 41.755 4.683 1.00 18.23 ? 23 SER A C 1 ATOM 99 O O . SER A 1 23 ? 31.451 41.293 5.708 1.00 18.04 ? 23 SER A O 1 ATOM 100 C CB . SER A 1 23 ? 34.263 42.598 4.390 1.00 23.33 ? 23 SER A CB 1 ATOM 101 O OG . SER A 1 23 ? 34.711 41.571 5.260 1.00 28.59 ? 23 SER A OG 1 ATOM 102 N N . PRO A 1 24 ? 31.729 41.223 3.474 1.00 17.45 ? 24 PRO A N 1 ATOM 103 C CA . PRO A 1 24 ? 30.908 40.019 3.345 1.00 17.75 ? 24 PRO A CA 1 ATOM 104 C C . PRO A 1 24 ? 31.726 38.898 3.980 1.00 18.21 ? 24 PRO A C 1 ATOM 105 O O . PRO A 1 24 ? 32.958 38.985 4.019 1.00 18.55 ? 24 PRO A O 1 ATOM 106 C CB . PRO A 1 24 ? 30.791 39.835 1.829 1.00 18.38 ? 24 PRO A CB 1 ATOM 107 C CG . PRO A 1 24 ? 30.984 41.220 1.284 1.00 21.79 ? 24 PRO A CG 1 ATOM 108 C CD . PRO A 1 24 ? 32.081 41.773 2.150 1.00 15.93 ? 24 PRO A CD 1 ATOM 109 N N . ALA A 1 25 ? 31.059 37.870 4.497 1.00 17.36 ? 25 ALA A N 1 ATOM 110 C CA . ALA A 1 25 ? 31.766 36.738 5.088 1.00 16.55 ? 25 ALA A CA 1 ATOM 111 C C . ALA A 1 25 ? 31.906 35.755 3.936 1.00 17.72 ? 25 ALA A C 1 ATOM 112 O O . ALA A 1 25 ? 30.933 35.123 3.529 1.00 15.78 ? 25 ALA A O 1 ATOM 113 C CB . ALA A 1 25 ? 30.949 36.124 6.223 1.00 16.35 ? 25 ALA A CB 1 ATOM 114 N N . ILE A 1 26 ? 33.125 35.642 3.419 1.00 17.69 ? 26 ILE A N 1 ATOM 115 C CA . ILE A 1 26 ? 33.432 34.799 2.272 1.00 19.53 ? 26 ILE A CA 1 ATOM 116 C C . ILE A 1 26 ? 33.867 33.383 2.618 1.00 18.58 ? 26 ILE A C 1 ATOM 117 O O . ILE A 1 26 ? 34.506 33.151 3.642 1.00 16.98 ? 26 ILE A O 1 ATOM 118 C CB . ILE A 1 26 ? 34.538 35.469 1.421 1.00 21.62 ? 26 ILE A CB 1 ATOM 119 C CG1 . ILE A 1 26 ? 34.100 36.885 1.052 1.00 22.51 ? 26 ILE A CG1 1 ATOM 120 C CG2 . ILE A 1 26 ? 34.803 34.663 0.152 1.00 24.25 ? 26 ILE A CG2 1 ATOM 121 C CD1 . ILE A 1 26 ? 35.204 37.725 0.433 1.00 27.94 ? 26 ILE A CD1 1 ATOM 122 N N . ASN A 1 27 ? 33.508 32.444 1.748 1.00 20.75 ? 27 ASN A N 1 ATOM 123 C CA . ASN A 1 27 ? 33.860 31.034 1.916 1.00 23.48 ? 27 ASN A CA 1 ATOM 124 C C . ASN A 1 27 ? 33.306 30.404 3.191 1.00 22.53 ? 27 ASN A C 1 ATOM 125 O O . ASN A 1 27 ? 33.930 29.521 3.782 1.00 21.31 ? 27 ASN A O 1 ATOM 126 C CB . ASN A 1 27 ? 35.384 30.857 1.879 1.00 30.12 ? 27 ASN A CB 1 ATOM 127 C CG . ASN A 1 27 ? 35.980 31.207 0.527 1.00 37.70 ? 27 ASN A CG 1 ATOM 128 O OD1 . ASN A 1 27 ? 35.530 30.714 -0.509 1.00 43.55 ? 27 ASN A OD1 1 ATOM 129 N ND2 . ASN A 1 27 ? 37.005 32.057 0.530 1.00 42.29 ? 27 ASN A ND2 1 ATOM 130 N N . VAL A 1 28 ? 32.136 30.863 3.623 1.00 19.40 ? 28 VAL A N 1 ATOM 131 C CA . VAL A 1 28 ? 31.515 30.302 4.815 1.00 19.55 ? 28 VAL A CA 1 ATOM 132 C C . VAL A 1 28 ? 30.680 29.104 4.387 1.00 16.52 ? 28 VAL A C 1 ATOM 133 O O . VAL A 1 28 ? 29.856 29.212 3.482 1.00 16.67 ? 28 VAL A O 1 ATOM 134 C CB . VAL A 1 28 ? 30.589 31.315 5.516 1.00 20.39 ? 28 VAL A CB 1 ATOM 135 C CG1 . VAL A 1 28 ? 29.903 30.649 6.699 1.00 19.09 ? 28 VAL A CG1 1 ATOM 136 C CG2 . VAL A 1 28 ? 31.396 32.523 5.990 1.00 21.30 ? 28 VAL A CG2 1 ATOM 137 N N . ALA A 1 29 ? 30.905 27.966 5.028 1.00 15.89 ? 29 ALA A N 1 ATOM 138 C CA . ALA A 1 29 ? 30.167 26.762 4.695 1.00 17.62 ? 29 ALA A CA 1 ATOM 139 C C . ALA A 1 29 ? 28.751 26.846 5.246 1.00 15.27 ? 29 ALA A C 1 ATOM 140 O O . ALA A 1 29 ? 28.531 27.239 6.400 1.00 15.66 ? 29 ALA A O 1 ATOM 141 C CB . ALA A 1 29 ? 30.891 25.521 5.259 1.00 16.49 ? 29 ALA A CB 1 ATOM 142 N N . VAL A 1 30 ? 27.791 26.479 4.409 1.00 14.25 ? 30 VAL A N 1 ATOM 143 C CA . VAL A 1 30 ? 26.383 26.488 4.795 1.00 15.36 ? 30 VAL A CA 1 ATOM 144 C C . VAL A 1 30 ? 25.774 25.134 4.452 1.00 15.38 ? 30 VAL A C 1 ATOM 145 O O . VAL A 1 30 ? 25.931 24.639 3.338 1.00 14.50 ? 30 VAL A O 1 ATOM 146 C CB . VAL A 1 30 ? 25.591 27.575 4.033 1.00 15.58 ? 30 VAL A CB 1 ATOM 147 C CG1 . VAL A 1 30 ? 24.104 27.464 4.350 1.00 17.65 ? 30 VAL A CG1 1 ATOM 148 C CG2 . VAL A 1 30 ? 26.107 28.954 4.399 1.00 16.47 ? 30 VAL A CG2 1 ATOM 149 N N . HIS A 1 31 ? 25.091 24.537 5.420 1.00 15.84 ? 31 HIS A N 1 ATOM 150 C CA . HIS A 1 31 ? 24.426 23.259 5.212 1.00 16.52 ? 31 HIS A CA 1 ATOM 151 C C . HIS A 1 31 ? 22.948 23.436 5.512 1.00 17.11 ? 31 HIS A C 1 ATOM 152 O O . HIS A 1 31 ? 22.579 24.016 6.529 1.00 16.36 ? 31 HIS A O 1 ATOM 153 C CB . HIS A 1 31 ? 24.987 22.177 6.132 1.00 17.47 ? 31 HIS A CB 1 ATOM 154 C CG . HIS A 1 31 ? 26.363 21.720 5.758 1.00 21.75 ? 31 HIS A CG 1 ATOM 155 N ND1 . HIS A 1 31 ? 27.489 22.476 5.993 1.00 23.76 ? 31 HIS A ND1 1 ATOM 156 C CD2 . HIS A 1 31 ? 26.791 20.587 5.153 1.00 22.17 ? 31 HIS A CD2 1 ATOM 157 C CE1 . HIS A 1 31 ? 28.553 21.828 5.550 1.00 21.93 ? 31 HIS A CE1 1 ATOM 158 N NE2 . HIS A 1 31 ? 28.156 20.680 5.035 1.00 24.72 ? 31 HIS A NE2 1 ATOM 159 N N . VAL A 1 32 ? 22.109 22.930 4.620 1.00 15.53 ? 32 VAL A N 1 ATOM 160 C CA . VAL A 1 32 ? 20.676 23.031 4.804 1.00 17.03 ? 32 VAL A CA 1 ATOM 161 C C . VAL A 1 32 ? 20.113 21.636 4.967 1.00 19.20 ? 32 VAL A C 1 ATOM 162 O O . VAL A 1 32 ? 20.520 20.705 4.261 1.00 18.73 ? 32 VAL A O 1 ATOM 163 C CB . VAL A 1 32 ? 20.008 23.703 3.602 1.00 16.78 ? 32 VAL A CB 1 ATOM 164 C CG1 . VAL A 1 32 ? 18.518 23.874 3.869 1.00 15.48 ? 32 VAL A CG1 1 ATOM 165 C CG2 . VAL A 1 32 ? 20.671 25.047 3.334 1.00 18.45 ? 32 VAL A CG2 1 ATOM 166 N N . PHE A 1 33 ? 19.183 21.497 5.905 1.00 16.57 ? 33 PHE A N 1 ATOM 167 C CA . PHE A 1 33 ? 18.547 20.219 6.180 1.00 19.43 ? 33 PHE A CA 1 ATOM 168 C C . PHE A 1 33 ? 17.040 20.385 6.196 1.00 21.37 ? 33 PHE A C 1 ATOM 169 O O . PHE A 1 33 ? 16.526 21.477 6.438 1.00 18.37 ? 33 PHE A O 1 ATOM 170 C CB . PHE A 1 33 ? 18.980 19.676 7.547 1.00 19.83 ? 33 PHE A CB 1 ATOM 171 C CG . PHE A 1 33 ? 20.468 19.620 7.740 1.00 21.35 ? 33 PHE A CG 1 ATOM 172 C CD1 . PHE A 1 33 ? 21.172 20.747 8.155 1.00 22.04 ? 33 PHE A CD1 1 ATOM 173 C CD2 . PHE A 1 33 ? 21.171 18.441 7.494 1.00 23.90 ? 33 PHE A CD2 1 ATOM 174 C CE1 . PHE A 1 33 ? 22.558 20.704 8.324 1.00 22.60 ? 33 PHE A CE1 1 ATOM 175 C CE2 . PHE A 1 33 ? 22.557 18.386 7.659 1.00 23.24 ? 33 PHE A CE2 1 ATOM 176 C CZ . PHE A 1 33 ? 23.250 19.520 8.075 1.00 23.84 ? 33 PHE A CZ 1 ATOM 177 N N . ARG A 1 34 ? 16.336 19.292 5.935 1.00 22.11 ? 34 ARG A N 1 ATOM 178 C CA . ARG A 1 34 ? 14.882 19.305 5.959 1.00 24.58 ? 34 ARG A CA 1 ATOM 179 C C . ARG A 1 34 ? 14.453 18.254 6.973 1.00 24.48 ? 34 ARG A C 1 ATOM 180 O O . ARG A 1 34 ? 15.007 17.151 7.016 1.00 23.94 ? 34 ARG A O 1 ATOM 181 C CB . ARG A 1 34 ? 14.308 18.982 4.581 1.00 24.12 ? 34 ARG A CB 1 ATOM 182 C CG . ARG A 1 34 ? 12.784 18.998 4.551 1.00 28.34 ? 34 ARG A CG 1 ATOM 183 C CD . ARG A 1 34 ? 12.236 18.880 3.142 1.00 31.64 ? 34 ARG A CD 1 ATOM 184 N NE . ARG A 1 34 ? 10.776 18.895 3.150 1.00 36.65 ? 34 ARG A NE 1 ATOM 185 C CZ . ARG A 1 34 ? 10.018 17.879 3.553 1.00 38.98 ? 34 ARG A CZ 1 ATOM 186 N NH1 . ARG A 1 34 ? 10.579 16.750 3.974 1.00 37.33 ? 34 ARG A NH1 1 ATOM 187 N NH2 . ARG A 1 34 ? 8.698 17.999 3.558 1.00 37.22 ? 34 ARG A NH2 1 ATOM 188 N N . LYS A 1 35 ? 13.481 18.592 7.807 1.00 25.56 ? 35 LYS A N 1 ATOM 189 C CA . LYS A 1 35 ? 13.033 17.647 8.813 1.00 30.20 ? 35 LYS A CA 1 ATOM 190 C C . LYS A 1 35 ? 12.256 16.536 8.117 1.00 31.19 ? 35 LYS A C 1 ATOM 191 O O . LYS A 1 35 ? 11.284 16.795 7.407 1.00 29.69 ? 35 LYS A O 1 ATOM 192 C CB . LYS A 1 35 ? 12.161 18.351 9.854 1.00 32.01 ? 35 LYS A CB 1 ATOM 193 C CG . LYS A 1 35 ? 12.238 17.727 11.239 1.00 38.12 ? 35 LYS A CG 1 ATOM 194 C CD . LYS A 1 35 ? 11.521 18.581 12.267 1.00 42.89 ? 35 LYS A CD 1 ATOM 195 C CE . LYS A 1 35 ? 11.745 18.052 13.673 1.00 46.79 ? 35 LYS A CE 1 ATOM 196 N NZ . LYS A 1 35 ? 11.059 18.896 14.691 1.00 49.66 ? 35 LYS A NZ 1 ATOM 197 N N . ALA A 1 36 ? 12.705 15.300 8.310 1.00 35.35 ? 36 ALA A N 1 ATOM 198 C CA . ALA A 1 36 ? 12.063 14.147 7.690 1.00 39.91 ? 36 ALA A CA 1 ATOM 199 C C . ALA A 1 36 ? 10.871 13.655 8.499 1.00 42.87 ? 36 ALA A C 1 ATOM 200 O O . ALA A 1 36 ? 10.639 14.100 9.623 1.00 42.26 ? 36 ALA A O 1 ATOM 201 C CB . ALA A 1 36 ? 13.077 13.018 7.515 1.00 40.78 ? 36 ALA A CB 1 ATOM 202 N N . ALA A 1 37 ? 10.121 12.725 7.916 1.00 47.33 ? 37 ALA A N 1 ATOM 203 C CA . ALA A 1 37 ? 8.945 12.158 8.565 1.00 51.46 ? 37 ALA A CA 1 ATOM 204 C C . ALA A 1 37 ? 9.242 11.625 9.964 1.00 53.13 ? 37 ALA A C 1 ATOM 205 O O . ALA A 1 37 ? 8.420 11.760 10.869 1.00 54.83 ? 37 ALA A O 1 ATOM 206 C CB . ALA A 1 37 ? 8.365 11.049 7.700 1.00 52.10 ? 37 ALA A CB 1 ATOM 207 N N . ASP A 1 38 ? 10.416 11.027 10.142 1.00 55.88 ? 38 ASP A N 1 ATOM 208 C CA . ASP A 1 38 ? 10.799 10.468 11.436 1.00 57.58 ? 38 ASP A CA 1 ATOM 209 C C . ASP A 1 38 ? 11.465 11.491 12.355 1.00 58.03 ? 38 ASP A C 1 ATOM 210 O O . ASP A 1 38 ? 12.221 11.127 13.258 1.00 58.26 ? 38 ASP A O 1 ATOM 211 C CB . ASP A 1 38 ? 11.734 9.272 11.232 1.00 59.59 ? 38 ASP A CB 1 ATOM 212 C CG . ASP A 1 38 ? 13.085 9.675 10.676 1.00 62.58 ? 38 ASP A CG 1 ATOM 213 O OD1 . ASP A 1 38 ? 13.123 10.415 9.670 1.00 62.75 ? 38 ASP A OD1 1 ATOM 214 O OD2 . ASP A 1 38 ? 14.112 9.243 11.244 1.00 64.49 ? 38 ASP A OD2 1 ATOM 215 N N . ASP A 1 39 ? 11.177 12.769 12.122 1.00 57.60 ? 39 ASP A N 1 ATOM 216 C CA . ASP A 1 39 ? 11.734 13.853 12.929 1.00 56.35 ? 39 ASP A CA 1 ATOM 217 C C . ASP A 1 39 ? 13.259 13.909 12.897 1.00 53.30 ? 39 ASP A C 1 ATOM 218 O O . ASP A 1 39 ? 13.893 14.346 13.858 1.00 53.50 ? 39 ASP A O 1 ATOM 219 C CB . ASP A 1 39 ? 11.260 13.729 14.380 1.00 59.79 ? 39 ASP A CB 1 ATOM 220 C CG . ASP A 1 39 ? 9.756 13.845 14.512 1.00 62.45 ? 39 ASP A CG 1 ATOM 221 O OD1 . ASP A 1 39 ? 9.203 14.889 14.105 1.00 63.21 ? 39 ASP A OD1 1 ATOM 222 O OD2 . ASP A 1 39 ? 9.127 12.892 15.022 1.00 64.51 ? 39 ASP A OD2 1 ATOM 223 N N . THR A 1 40 ? 13.842 13.467 11.790 1.00 49.21 ? 40 THR A N 1 ATOM 224 C CA . THR A 1 40 ? 15.292 13.478 11.624 1.00 45.57 ? 40 THR A CA 1 ATOM 225 C C . THR A 1 40 ? 15.673 14.536 10.595 1.00 40.50 ? 40 THR A C 1 ATOM 226 O O . THR A 1 40 ? 14.898 14.825 9.683 1.00 39.57 ? 40 THR A O 1 ATOM 227 C CB . THR A 1 40 ? 15.810 12.104 11.137 1.00 45.80 ? 40 THR A CB 1 ATOM 228 O OG1 . THR A 1 40 ? 15.587 11.123 12.156 1.00 51.38 ? 40 THR A OG1 1 ATOM 229 C CG2 . THR A 1 40 ? 17.296 12.167 10.824 1.00 47.73 ? 40 THR A CG2 1 ATOM 230 N N . TRP A 1 41 ? 16.863 15.107 10.741 1.00 35.30 ? 41 TRP A N 1 ATOM 231 C CA . TRP A 1 41 ? 17.335 16.123 9.808 1.00 33.38 ? 41 TRP A CA 1 ATOM 232 C C . TRP A 1 41 ? 18.081 15.487 8.647 1.00 33.20 ? 41 TRP A C 1 ATOM 233 O O . TRP A 1 41 ? 19.195 14.988 8.814 1.00 33.81 ? 41 TRP A O 1 ATOM 234 C CB . TRP A 1 41 ? 18.277 17.108 10.501 1.00 31.49 ? 41 TRP A CB 1 ATOM 235 C CG . TRP A 1 41 ? 17.615 18.012 11.466 1.00 31.41 ? 41 TRP A CG 1 ATOM 236 C CD1 . TRP A 1 41 ? 17.806 18.051 12.818 1.00 31.71 ? 41 TRP A CD1 1 ATOM 237 C CD2 . TRP A 1 41 ? 16.668 19.042 11.163 1.00 29.02 ? 41 TRP A CD2 1 ATOM 238 N NE1 . TRP A 1 41 ? 17.040 19.046 13.375 1.00 31.30 ? 41 TRP A NE1 1 ATOM 239 C CE2 . TRP A 1 41 ? 16.330 19.669 12.383 1.00 29.34 ? 41 TRP A CE2 1 ATOM 240 C CE3 . TRP A 1 41 ? 16.074 19.497 9.980 1.00 26.84 ? 41 TRP A CE3 1 ATOM 241 C CZ2 . TRP A 1 41 ? 15.421 20.728 12.454 1.00 27.96 ? 41 TRP A CZ2 1 ATOM 242 C CZ3 . TRP A 1 41 ? 15.172 20.552 10.050 1.00 25.92 ? 41 TRP A CZ3 1 ATOM 243 C CH2 . TRP A 1 41 ? 14.855 21.155 11.280 1.00 26.49 ? 41 TRP A CH2 1 ATOM 244 N N . GLU A 1 42 ? 17.477 15.498 7.468 1.00 32.58 ? 42 GLU A N 1 ATOM 245 C CA . GLU A 1 42 ? 18.153 14.930 6.319 1.00 31.38 ? 42 GLU A CA 1 ATOM 246 C C . GLU A 1 42 ? 18.780 16.037 5.487 1.00 29.40 ? 42 GLU A C 1 ATOM 247 O O . GLU A 1 42 ? 18.189 17.107 5.314 1.00 24.90 ? 42 GLU A O 1 ATOM 248 C CB . GLU A 1 42 ? 17.184 14.113 5.464 1.00 35.83 ? 42 GLU A CB 1 ATOM 249 C CG . GLU A 1 42 ? 16.039 14.887 4.865 1.00 45.46 ? 42 GLU A CG 1 ATOM 250 C CD . GLU A 1 42 ? 15.199 14.023 3.939 1.00 50.45 ? 42 GLU A CD 1 ATOM 251 O OE1 . GLU A 1 42 ? 14.691 12.980 4.403 1.00 52.24 ? 42 GLU A OE1 1 ATOM 252 O OE2 . GLU A 1 42 ? 15.052 14.382 2.751 1.00 52.85 ? 42 GLU A OE2 1 ATOM 253 N N . PRO A 1 43 ? 20.002 15.800 4.979 1.00 26.49 ? 43 PRO A N 1 ATOM 254 C CA . PRO A 1 43 ? 20.711 16.781 4.160 1.00 25.33 ? 43 PRO A CA 1 ATOM 255 C C . PRO A 1 43 ? 19.813 17.225 3.013 1.00 25.36 ? 43 PRO A C 1 ATOM 256 O O . PRO A 1 43 ? 19.150 16.406 2.375 1.00 24.08 ? 43 PRO A O 1 ATOM 257 C CB . PRO A 1 43 ? 21.935 16.002 3.677 1.00 26.88 ? 43 PRO A CB 1 ATOM 258 C CG . PRO A 1 43 ? 22.227 15.105 4.845 1.00 27.76 ? 43 PRO A CG 1 ATOM 259 C CD . PRO A 1 43 ? 20.832 14.601 5.194 1.00 27.50 ? 43 PRO A CD 1 ATOM 260 N N . PHE A 1 44 ? 19.777 18.526 2.766 1.00 21.77 ? 44 PHE A N 1 ATOM 261 C CA . PHE A 1 44 ? 18.948 19.065 1.701 1.00 21.79 ? 44 PHE A CA 1 ATOM 262 C C . PHE A 1 44 ? 19.808 19.756 0.653 1.00 22.41 ? 44 PHE A C 1 ATOM 263 O O . PHE A 1 44 ? 19.635 19.550 -0.545 1.00 20.93 ? 44 PHE A O 1 ATOM 264 C CB . PHE A 1 44 ? 17.942 20.054 2.291 1.00 21.06 ? 44 PHE A CB 1 ATOM 265 C CG . PHE A 1 44 ? 16.977 20.604 1.291 1.00 22.38 ? 44 PHE A CG 1 ATOM 266 C CD1 . PHE A 1 44 ? 15.970 19.801 0.766 1.00 24.12 ? 44 PHE A CD1 1 ATOM 267 C CD2 . PHE A 1 44 ? 17.078 21.922 0.862 1.00 22.52 ? 44 PHE A CD2 1 ATOM 268 C CE1 . PHE A 1 44 ? 15.080 20.303 -0.173 1.00 22.50 ? 44 PHE A CE1 1 ATOM 269 C CE2 . PHE A 1 44 ? 16.194 22.429 -0.075 1.00 23.68 ? 44 PHE A CE2 1 ATOM 270 C CZ . PHE A 1 44 ? 15.191 21.613 -0.593 1.00 22.50 ? 44 PHE A CZ 1 ATOM 271 N N . ALA A 1 45 ? 20.743 20.578 1.114 1.00 20.82 ? 45 ALA A N 1 ATOM 272 C CA . ALA A 1 45 ? 21.621 21.297 0.208 1.00 19.92 ? 45 ALA A CA 1 ATOM 273 C C . ALA A 1 45 ? 22.763 21.888 1.003 1.00 19.40 ? 45 ALA A C 1 ATOM 274 O O . ALA A 1 45 ? 22.687 22.003 2.233 1.00 19.08 ? 45 ALA A O 1 ATOM 275 C CB . ALA A 1 45 ? 20.845 22.414 -0.502 1.00 19.28 ? 45 ALA A CB 1 ATOM 276 N N . SER A 1 46 ? 23.833 22.250 0.310 1.00 17.10 ? 46 SER A N 1 ATOM 277 C CA . SER A 1 46 ? 24.969 22.856 0.987 1.00 17.41 ? 46 SER A CA 1 ATOM 278 C C . SER A 1 46 ? 25.780 23.675 0.003 1.00 18.76 ? 46 SER A C 1 ATOM 279 O O . SER A 1 46 ? 25.638 23.530 -1.212 1.00 17.27 ? 46 SER A O 1 ATOM 280 C CB . SER A 1 46 ? 25.848 21.784 1.652 1.00 16.09 ? 46 SER A CB 1 ATOM 281 O OG . SER A 1 46 ? 26.442 20.923 0.692 1.00 18.80 ? 46 SER A OG 1 ATOM 282 N N . GLY A 1 47 ? 26.617 24.555 0.535 1.00 17.78 ? 47 GLY A N 1 ATOM 283 C CA . GLY A 1 47 ? 27.442 25.384 -0.321 1.00 18.44 ? 47 GLY A CA 1 ATOM 284 C C . GLY A 1 47 ? 28.307 26.294 0.518 1.00 19.15 ? 47 GLY A C 1 ATOM 285 O O . GLY A 1 47 ? 28.309 26.192 1.744 1.00 19.28 ? 47 GLY A O 1 ATOM 286 N N . LYS A 1 48 ? 29.046 27.175 -0.144 1.00 17.79 ? 48 LYS A N 1 ATOM 287 C CA . LYS A 1 48 ? 29.910 28.130 0.538 1.00 20.51 ? 48 LYS A CA 1 ATOM 288 C C . LYS A 1 48 ? 29.565 29.512 0.001 1.00 19.43 ? 48 LYS A C 1 ATOM 289 O O . LYS A 1 48 ? 29.241 29.663 -1.175 1.00 17.47 ? 48 LYS A O 1 ATOM 290 C CB . LYS A 1 48 ? 31.391 27.815 0.277 1.00 24.40 ? 48 LYS A CB 1 ATOM 291 C CG . LYS A 1 48 ? 31.971 26.743 1.200 1.00 32.01 ? 48 LYS A CG 1 ATOM 292 C CD . LYS A 1 48 ? 33.443 26.477 0.906 1.00 38.65 ? 48 LYS A CD 1 ATOM 293 C CE . LYS A 1 48 ? 34.094 25.655 2.013 1.00 37.59 ? 48 LYS A CE 1 ATOM 294 N NZ . LYS A 1 48 ? 34.162 26.437 3.288 1.00 43.22 ? 48 LYS A NZ 1 ATOM 295 N N . THR A 1 49 ? 29.608 30.520 0.862 1.00 16.71 ? 49 THR A N 1 ATOM 296 C CA . THR A 1 49 ? 29.292 31.870 0.421 1.00 18.46 ? 49 THR A CA 1 ATOM 297 C C . THR A 1 49 ? 30.338 32.352 -0.575 1.00 20.58 ? 49 THR A C 1 ATOM 298 O O . THR A 1 49 ? 31.513 31.991 -0.495 1.00 19.55 ? 49 THR A O 1 ATOM 299 C CB . THR A 1 49 ? 29.225 32.857 1.602 1.00 15.24 ? 49 THR A CB 1 ATOM 300 O OG1 . THR A 1 49 ? 30.460 32.830 2.321 1.00 14.61 ? 49 THR A OG1 1 ATOM 301 C CG2 . THR A 1 49 ? 28.087 32.485 2.538 1.00 17.10 ? 49 THR A CG2 1 ATOM 302 N N . SER A 1 50 ? 29.893 33.173 -1.514 1.00 19.66 ? 50 SER A N 1 ATOM 303 C CA . SER A 1 50 ? 30.763 33.707 -2.550 1.00 22.98 ? 50 SER A CA 1 ATOM 304 C C . SER A 1 50 ? 31.503 34.937 -2.040 1.00 24.46 ? 50 SER A C 1 ATOM 305 O O . SER A 1 50 ? 31.425 35.278 -0.855 1.00 19.60 ? 50 SER A O 1 ATOM 306 C CB . SER A 1 50 ? 29.923 34.104 -3.754 1.00 24.19 ? 50 SER A CB 1 ATOM 307 O OG . SER A 1 50 ? 29.070 35.177 -3.386 1.00 24.72 ? 50 SER A OG 1 ATOM 308 N N . GLU A 1 51 ? 32.204 35.605 -2.955 1.00 25.64 ? 51 GLU A N 1 ATOM 309 C CA . GLU A 1 51 ? 32.969 36.812 -2.644 1.00 27.71 ? 51 GLU A CA 1 ATOM 310 C C . GLU A 1 51 ? 32.067 37.922 -2.102 1.00 25.87 ? 51 GLU A C 1 ATOM 311 O O . GLU A 1 51 ? 32.532 38.823 -1.403 1.00 25.88 ? 51 GLU A O 1 ATOM 312 C CB . GLU A 1 51 ? 33.680 37.332 -3.901 1.00 33.71 ? 51 GLU A CB 1 ATOM 313 C CG . GLU A 1 51 ? 34.671 36.366 -4.533 1.00 45.97 ? 51 GLU A CG 1 ATOM 314 C CD . GLU A 1 51 ? 35.885 36.116 -3.666 1.00 51.31 ? 51 GLU A CD 1 ATOM 315 O OE1 . GLU A 1 51 ? 35.741 35.472 -2.607 1.00 56.39 ? 51 GLU A OE1 1 ATOM 316 O OE2 . GLU A 1 51 ? 36.988 36.568 -4.041 1.00 56.87 ? 51 GLU A OE2 1 ATOM 317 N N . SER A 1 52 ? 30.784 37.865 -2.438 1.00 23.52 ? 52 SER A N 1 ATOM 318 C CA . SER A 1 52 ? 29.836 38.877 -1.979 1.00 24.16 ? 52 SER A CA 1 ATOM 319 C C . SER A 1 52 ? 29.114 38.446 -0.700 1.00 21.98 ? 52 SER A C 1 ATOM 320 O O . SER A 1 52 ? 28.192 39.128 -0.237 1.00 18.62 ? 52 SER A O 1 ATOM 321 C CB . SER A 1 52 ? 28.807 39.163 -3.072 1.00 25.59 ? 52 SER A CB 1 ATOM 322 O OG . SER A 1 52 ? 28.038 38.005 -3.347 1.00 30.46 ? 52 SER A OG 1 ATOM 323 N N . GLY A 1 53 ? 29.537 37.317 -0.139 1.00 18.85 ? 53 GLY A N 1 ATOM 324 C CA . GLY A 1 53 ? 28.933 36.815 1.084 1.00 18.73 ? 53 GLY A CA 1 ATOM 325 C C . GLY A 1 53 ? 27.595 36.140 0.849 1.00 20.11 ? 53 GLY A C 1 ATOM 326 O O . GLY A 1 53 ? 26.881 35.814 1.793 1.00 19.13 ? 53 GLY A O 1 ATOM 327 N N . GLU A 1 54 ? 27.252 35.915 -0.414 1.00 21.99 ? 54 GLU A N 1 ATOM 328 C CA . GLU A 1 54 ? 25.979 35.291 -0.739 1.00 22.04 ? 54 GLU A CA 1 ATOM 329 C C . GLU A 1 54 ? 26.090 33.855 -1.217 1.00 22.32 ? 54 GLU A C 1 ATOM 330 O O . GLU A 1 54 ? 27.128 33.422 -1.718 1.00 21.25 ? 54 GLU A O 1 ATOM 331 C CB . GLU A 1 54 ? 25.255 36.107 -1.809 1.00 25.61 ? 54 GLU A CB 1 ATOM 332 C CG . GLU A 1 54 ? 25.147 37.586 -1.499 1.00 33.51 ? 54 GLU A CG 1 ATOM 333 C CD . GLU A 1 54 ? 24.317 38.334 -2.525 1.00 38.91 ? 54 GLU A CD 1 ATOM 334 O OE1 . GLU A 1 54 ? 24.581 38.181 -3.736 1.00 41.93 ? 54 GLU A OE1 1 ATOM 335 O OE2 . GLU A 1 54 ? 23.403 39.080 -2.121 1.00 43.50 ? 54 GLU A OE2 1 ATOM 336 N N . LEU A 1 55 ? 24.997 33.119 -1.059 1.00 19.20 ? 55 LEU A N 1 ATOM 337 C CA . LEU A 1 55 ? 24.935 31.738 -1.496 1.00 20.44 ? 55 LEU A CA 1 ATOM 338 C C . LEU A 1 55 ? 23.611 31.566 -2.222 1.00 22.45 ? 55 LEU A C 1 ATOM 339 O O . LEU A 1 55 ? 22.548 31.661 -1.611 1.00 20.39 ? 55 LEU A O 1 ATOM 340 C CB . LEU A 1 55 ? 25.020 30.791 -0.298 1.00 20.70 ? 55 LEU A CB 1 ATOM 341 C CG . LEU A 1 55 ? 24.934 29.284 -0.560 1.00 21.84 ? 55 LEU A CG 1 ATOM 342 C CD1 . LEU A 1 55 ? 25.902 28.855 -1.655 1.00 21.60 ? 55 LEU A CD1 1 ATOM 343 C CD2 . LEU A 1 55 ? 25.238 28.560 0.739 1.00 21.03 ? 55 LEU A CD2 1 ATOM 344 N N . HIS A 1 56 ? 23.684 31.350 -3.531 1.00 25.61 ? 56 HIS A N 1 ATOM 345 C CA . HIS A 1 56 ? 22.492 31.160 -4.352 1.00 29.83 ? 56 HIS A CA 1 ATOM 346 C C . HIS A 1 56 ? 22.479 29.745 -4.913 1.00 29.12 ? 56 HIS A C 1 ATOM 347 O O . HIS A 1 56 ? 23.444 28.994 -4.760 1.00 30.60 ? 56 HIS A O 1 ATOM 348 C CB . HIS A 1 56 ? 22.473 32.129 -5.542 1.00 33.15 ? 56 HIS A CB 1 ATOM 349 C CG . HIS A 1 56 ? 22.620 33.568 -5.167 1.00 37.25 ? 56 HIS A CG 1 ATOM 350 N ND1 . HIS A 1 56 ? 23.823 34.117 -4.778 1.00 39.28 ? 56 HIS A ND1 1 ATOM 351 C CD2 . HIS A 1 56 ? 21.718 34.578 -5.134 1.00 39.29 ? 56 HIS A CD2 1 ATOM 352 C CE1 . HIS A 1 56 ? 23.656 35.402 -4.522 1.00 38.72 ? 56 HIS A CE1 1 ATOM 353 N NE2 . HIS A 1 56 ? 22.388 35.707 -4.730 1.00 38.70 ? 56 HIS A NE2 1 ATOM 354 N N . GLY A 1 57 ? 21.383 29.402 -5.578 1.00 31.68 ? 57 GLY A N 1 ATOM 355 C CA . GLY A 1 57 ? 21.255 28.094 -6.192 1.00 30.83 ? 57 GLY A CA 1 ATOM 356 C C . GLY A 1 57 ? 21.240 26.916 -5.245 1.00 29.61 ? 57 GLY A C 1 ATOM 357 O O . GLY A 1 57 ? 21.674 25.826 -5.609 1.00 29.37 ? 57 GLY A O 1 ATOM 358 N N . LEU A 1 58 ? 20.752 27.119 -4.026 1.00 26.97 ? 58 LEU A N 1 ATOM 359 C CA . LEU A 1 58 ? 20.694 26.021 -3.075 1.00 26.41 ? 58 LEU A CA 1 ATOM 360 C C . LEU A 1 58 ? 19.625 25.014 -3.465 1.00 25.96 ? 58 LEU A C 1 ATOM 361 O O . LEU A 1 58 ? 19.817 23.812 -3.316 1.00 24.89 ? 58 LEU A O 1 ATOM 362 C CB . LEU A 1 58 ? 20.406 26.534 -1.664 1.00 25.19 ? 58 LEU A CB 1 ATOM 363 C CG . LEU A 1 58 ? 21.613 27.138 -0.949 1.00 24.26 ? 58 LEU A CG 1 ATOM 364 C CD1 . LEU A 1 58 ? 21.190 27.724 0.390 1.00 24.17 ? 58 LEU A CD1 1 ATOM 365 C CD2 . LEU A 1 58 ? 22.668 26.054 -0.761 1.00 23.22 ? 58 LEU A CD2 1 ATOM 366 N N . THR A 1 59 ? 18.507 25.505 -3.986 1.00 25.70 ? 59 THR A N 1 ATOM 367 C CA . THR A 1 59 ? 17.413 24.617 -4.352 1.00 26.44 ? 59 THR A CA 1 ATOM 368 C C . THR A 1 59 ? 16.545 25.237 -5.444 1.00 26.73 ? 59 THR A C 1 ATOM 369 O O . THR A 1 59 ? 16.847 26.317 -5.943 1.00 26.13 ? 59 THR A O 1 ATOM 370 C CB . THR A 1 59 ? 16.549 24.334 -3.109 1.00 25.17 ? 59 THR A CB 1 ATOM 371 O OG1 . THR A 1 59 ? 15.562 23.350 -3.413 1.00 24.57 ? 59 THR A OG1 1 ATOM 372 C CG2 . THR A 1 59 ? 15.870 25.617 -2.635 1.00 24.68 ? 59 THR A CG2 1 ATOM 373 N N . THR A 1 60 ? 15.471 24.543 -5.811 1.00 26.04 ? 60 THR A N 1 ATOM 374 C CA . THR A 1 60 ? 14.545 25.035 -6.827 1.00 28.34 ? 60 THR A CA 1 ATOM 375 C C . THR A 1 60 ? 13.145 25.090 -6.235 1.00 27.84 ? 60 THR A C 1 ATOM 376 O O . THR A 1 60 ? 12.884 24.495 -5.189 1.00 27.09 ? 60 THR A O 1 ATOM 377 C CB . THR A 1 60 ? 14.509 24.111 -8.059 1.00 27.63 ? 60 THR A CB 1 ATOM 378 O OG1 . THR A 1 60 ? 14.074 22.805 -7.659 1.00 27.49 ? 60 THR A OG1 1 ATOM 379 C CG2 . THR A 1 60 ? 15.885 24.015 -8.693 1.00 32.57 ? 60 THR A CG2 1 ATOM 380 N N . GLU A 1 61 ? 12.243 25.797 -6.904 1.00 29.89 ? 61 GLU A N 1 ATOM 381 C CA . GLU A 1 61 ? 10.873 25.910 -6.423 1.00 33.41 ? 61 GLU A CA 1 ATOM 382 C C . GLU A 1 61 ? 10.222 24.538 -6.299 1.00 31.30 ? 61 GLU A C 1 ATOM 383 O O . GLU A 1 61 ? 9.483 24.276 -5.352 1.00 33.66 ? 61 GLU A O 1 ATOM 384 C CB . GLU A 1 61 ? 10.041 26.782 -7.372 1.00 37.58 ? 61 GLU A CB 1 ATOM 385 C CG . GLU A 1 61 ? 10.508 28.224 -7.472 1.00 46.05 ? 61 GLU A CG 1 ATOM 386 C CD . GLU A 1 61 ? 9.642 29.055 -8.401 1.00 51.72 ? 61 GLU A CD 1 ATOM 387 O OE1 . GLU A 1 61 ? 9.916 30.266 -8.549 1.00 55.26 ? 61 GLU A OE1 1 ATOM 388 O OE2 . GLU A 1 61 ? 8.687 28.498 -8.985 1.00 54.32 ? 61 GLU A OE2 1 ATOM 389 N N . GLU A 1 62 ? 10.509 23.663 -7.255 1.00 29.54 ? 62 GLU A N 1 ATOM 390 C CA . GLU A 1 62 ? 9.925 22.325 -7.274 1.00 28.95 ? 62 GLU A CA 1 ATOM 391 C C . GLU A 1 62 ? 10.376 21.464 -6.102 1.00 26.53 ? 62 GLU A C 1 ATOM 392 O O . GLU A 1 62 ? 9.588 20.739 -5.515 1.00 24.84 ? 62 GLU A O 1 ATOM 393 C CB . GLU A 1 62 ? 10.286 21.619 -8.583 1.00 31.40 ? 62 GLU A CB 1 ATOM 394 C CG . GLU A 1 62 ? 9.373 20.455 -8.939 0.50 35.02 ? 62 GLU A CG 1 ATOM 395 C CD . GLU A 1 62 ? 8.017 20.911 -9.450 0.50 36.74 ? 62 GLU A CD 1 ATOM 396 O OE1 . GLU A 1 62 ? 7.303 21.620 -8.711 0.50 38.67 ? 62 GLU A OE1 1 ATOM 397 O OE2 . GLU A 1 62 ? 7.665 20.558 -10.594 0.50 39.09 ? 62 GLU A OE2 1 ATOM 398 N N . GLN A 1 63 ? 11.655 21.548 -5.764 1.00 24.66 ? 63 GLN A N 1 ATOM 399 C CA . GLN A 1 63 ? 12.210 20.755 -4.679 1.00 24.97 ? 63 GLN A CA 1 ATOM 400 C C . GLN A 1 63 ? 11.957 21.317 -3.283 1.00 21.57 ? 63 GLN A C 1 ATOM 401 O O . GLN A 1 63 ? 11.872 20.562 -2.318 1.00 19.55 ? 63 GLN A O 1 ATOM 402 C CB . GLN A 1 63 ? 13.713 20.590 -4.905 1.00 30.22 ? 63 GLN A CB 1 ATOM 403 C CG . GLN A 1 63 ? 14.501 20.135 -3.693 1.00 38.75 ? 63 GLN A CG 1 ATOM 404 C CD . GLN A 1 63 ? 15.989 20.042 -3.984 1.00 42.44 ? 63 GLN A CD 1 ATOM 405 O OE1 . GLN A 1 63 ? 16.429 19.181 -4.749 1.00 45.32 ? 63 GLN A OE1 1 ATOM 406 N NE2 . GLN A 1 63 ? 16.769 20.935 -3.383 1.00 41.60 ? 63 GLN A NE2 1 ATOM 407 N N . PHE A 1 64 ? 11.836 22.638 -3.194 1.00 21.20 ? 64 PHE A N 1 ATOM 408 C CA . PHE A 1 64 ? 11.621 23.341 -1.931 1.00 22.16 ? 64 PHE A CA 1 ATOM 409 C C . PHE A 1 64 ? 10.154 23.284 -1.496 1.00 21.88 ? 64 PHE A C 1 ATOM 410 O O . PHE A 1 64 ? 9.442 24.282 -1.546 1.00 22.18 ? 64 PHE A O 1 ATOM 411 C CB . PHE A 1 64 ? 12.076 24.793 -2.099 1.00 21.77 ? 64 PHE A CB 1 ATOM 412 C CG . PHE A 1 64 ? 12.263 25.538 -0.807 1.00 23.20 ? 64 PHE A CG 1 ATOM 413 C CD1 . PHE A 1 64 ? 12.902 24.940 0.273 1.00 24.31 ? 64 PHE A CD1 1 ATOM 414 C CD2 . PHE A 1 64 ? 11.848 26.862 -0.690 1.00 26.05 ? 64 PHE A CD2 1 ATOM 415 C CE1 . PHE A 1 64 ? 13.129 25.650 1.456 1.00 24.33 ? 64 PHE A CE1 1 ATOM 416 C CE2 . PHE A 1 64 ? 12.073 27.581 0.489 1.00 24.18 ? 64 PHE A CE2 1 ATOM 417 C CZ . PHE A 1 64 ? 12.714 26.972 1.560 1.00 24.61 ? 64 PHE A CZ 1 ATOM 418 N N . VAL A 1 65 ? 9.716 22.110 -1.056 1.00 21.28 ? 65 VAL A N 1 ATOM 419 C CA . VAL A 1 65 ? 8.332 21.926 -0.631 1.00 20.61 ? 65 VAL A CA 1 ATOM 420 C C . VAL A 1 65 ? 8.134 22.358 0.808 1.00 21.47 ? 65 VAL A C 1 ATOM 421 O O . VAL A 1 65 ? 9.104 22.661 1.515 1.00 18.87 ? 65 VAL A O 1 ATOM 422 C CB . VAL A 1 65 ? 7.902 20.454 -0.762 1.00 19.25 ? 65 VAL A CB 1 ATOM 423 C CG1 . VAL A 1 65 ? 7.927 20.039 -2.224 1.00 21.65 ? 65 VAL A CG1 1 ATOM 424 C CG2 . VAL A 1 65 ? 8.830 19.566 0.064 1.00 17.06 ? 65 VAL A CG2 1 ATOM 425 N N . GLU A 1 66 ? 6.878 22.376 1.242 1.00 21.77 ? 66 GLU A N 1 ATOM 426 C CA . GLU A 1 66 ? 6.563 22.774 2.605 1.00 24.37 ? 66 GLU A CA 1 ATOM 427 C C . GLU A 1 66 ? 7.328 21.880 3.555 1.00 23.29 ? 66 GLU A C 1 ATOM 428 O O . GLU A 1 66 ? 7.602 20.721 3.251 1.00 23.29 ? 66 GLU A O 1 ATOM 429 C CB . GLU A 1 66 ? 5.059 22.648 2.885 1.00 26.56 ? 66 GLU A CB 1 ATOM 430 C CG . GLU A 1 66 ? 4.192 23.575 2.043 1.00 37.68 ? 66 GLU A CG 1 ATOM 431 C CD . GLU A 1 66 ? 2.729 23.545 2.453 1.00 41.00 ? 66 GLU A CD 1 ATOM 432 O OE1 . GLU A 1 66 ? 2.150 22.438 2.497 1.00 39.04 ? 66 GLU A OE1 1 ATOM 433 O OE2 . GLU A 1 66 ? 2.159 24.626 2.724 1.00 45.46 ? 66 GLU A OE2 1 ATOM 434 N N . GLY A 1 67 ? 7.679 22.419 4.710 1.00 22.13 ? 67 GLY A N 1 ATOM 435 C CA . GLY A 1 67 ? 8.394 21.618 5.675 1.00 21.80 ? 67 GLY A CA 1 ATOM 436 C C . GLY A 1 67 ? 9.195 22.493 6.601 1.00 21.03 ? 67 GLY A C 1 ATOM 437 O O . GLY A 1 67 ? 9.164 23.718 6.496 1.00 20.50 ? 67 GLY A O 1 ATOM 438 N N . ILE A 1 68 ? 9.899 21.857 7.523 1.00 19.09 ? 68 ILE A N 1 ATOM 439 C CA . ILE A 1 68 ? 10.729 22.585 8.462 1.00 20.56 ? 68 ILE A CA 1 ATOM 440 C C . ILE A 1 68 ? 12.154 22.421 7.975 1.00 19.52 ? 68 ILE A C 1 ATOM 441 O O . ILE A 1 68 ? 12.621 21.301 7.735 1.00 19.85 ? 68 ILE A O 1 ATOM 442 C CB . ILE A 1 68 ? 10.588 22.024 9.891 1.00 21.85 ? 68 ILE A CB 1 ATOM 443 C CG1 . ILE A 1 68 ? 9.131 22.145 10.347 1.00 24.63 ? 68 ILE A CG1 1 ATOM 444 C CG2 . ILE A 1 68 ? 11.502 22.797 10.845 1.00 20.53 ? 68 ILE A CG2 1 ATOM 445 C CD1 . ILE A 1 68 ? 8.847 21.525 11.702 1.00 30.18 ? 68 ILE A CD1 1 ATOM 446 N N . TYR A 1 69 ? 12.835 23.544 7.803 1.00 16.86 ? 69 TYR A N 1 ATOM 447 C CA . TYR A 1 69 ? 14.203 23.529 7.323 1.00 15.38 ? 69 TYR A CA 1 ATOM 448 C C . TYR A 1 69 ? 15.163 24.114 8.329 1.00 16.54 ? 69 TYR A C 1 ATOM 449 O O . TYR A 1 69 ? 14.788 24.964 9.133 1.00 17.68 ? 69 TYR A O 1 ATOM 450 C CB . TYR A 1 69 ? 14.312 24.329 6.031 1.00 14.53 ? 69 TYR A CB 1 ATOM 451 C CG . TYR A 1 69 ? 13.571 23.698 4.883 1.00 18.57 ? 69 TYR A CG 1 ATOM 452 C CD1 . TYR A 1 69 ? 12.189 23.847 4.749 1.00 16.73 ? 69 TYR A CD1 1 ATOM 453 C CD2 . TYR A 1 69 ? 14.250 22.932 3.943 1.00 18.74 ? 69 TYR A CD2 1 ATOM 454 C CE1 . TYR A 1 69 ? 11.506 23.244 3.695 1.00 19.60 ? 69 TYR A CE1 1 ATOM 455 C CE2 . TYR A 1 69 ? 13.581 22.325 2.888 1.00 17.95 ? 69 TYR A CE2 1 ATOM 456 C CZ . TYR A 1 69 ? 12.213 22.486 2.770 1.00 19.40 ? 69 TYR A CZ 1 ATOM 457 O OH . TYR A 1 69 ? 11.568 21.891 1.712 1.00 18.01 ? 69 TYR A OH 1 ATOM 458 N N . LYS A 1 70 ? 16.404 23.646 8.274 1.00 15.90 ? 70 LYS A N 1 ATOM 459 C CA . LYS A 1 70 ? 17.443 24.157 9.151 1.00 16.87 ? 70 LYS A CA 1 ATOM 460 C C . LYS A 1 70 ? 18.620 24.584 8.304 1.00 16.69 ? 70 LYS A C 1 ATOM 461 O O . LYS A 1 70 ? 19.141 23.802 7.506 1.00 18.62 ? 70 LYS A O 1 ATOM 462 C CB . LYS A 1 70 ? 17.910 23.097 10.150 1.00 19.49 ? 70 LYS A CB 1 ATOM 463 C CG . LYS A 1 70 ? 19.073 23.583 11.016 1.00 22.33 ? 70 LYS A CG 1 ATOM 464 C CD . LYS A 1 70 ? 19.386 22.645 12.171 1.00 28.71 ? 70 LYS A CD 1 ATOM 465 C CE . LYS A 1 70 ? 19.897 21.304 11.684 1.00 33.91 ? 70 LYS A CE 1 ATOM 466 N NZ . LYS A 1 70 ? 20.288 20.439 12.834 1.00 36.98 ? 70 LYS A NZ 1 ATOM 467 N N . VAL A 1 71 ? 19.010 25.842 8.462 1.00 15.47 ? 71 VAL A N 1 ATOM 468 C CA . VAL A 1 71 ? 20.148 26.401 7.758 1.00 16.04 ? 71 VAL A CA 1 ATOM 469 C C . VAL A 1 71 ? 21.236 26.522 8.812 1.00 15.79 ? 71 VAL A C 1 ATOM 470 O O . VAL A 1 71 ? 21.087 27.249 9.792 1.00 17.69 ? 71 VAL A O 1 ATOM 471 C CB . VAL A 1 71 ? 19.840 27.794 7.187 1.00 16.00 ? 71 VAL A CB 1 ATOM 472 C CG1 . VAL A 1 71 ? 21.087 28.382 6.563 1.00 17.52 ? 71 VAL A CG1 1 ATOM 473 C CG2 . VAL A 1 71 ? 18.730 27.701 6.160 1.00 17.76 ? 71 VAL A CG2 1 ATOM 474 N N . GLU A 1 72 ? 22.316 25.777 8.619 1.00 17.44 ? 72 GLU A N 1 ATOM 475 C CA . GLU A 1 72 ? 23.432 25.775 9.547 1.00 17.74 ? 72 GLU A CA 1 ATOM 476 C C . GLU A 1 72 ? 24.596 26.502 8.888 1.00 17.54 ? 72 GLU A C 1 ATOM 477 O O . GLU A 1 72 ? 25.011 26.147 7.790 1.00 18.83 ? 72 GLU A O 1 ATOM 478 C CB . GLU A 1 72 ? 23.810 24.328 9.868 1.00 22.52 ? 72 GLU A CB 1 ATOM 479 C CG . GLU A 1 72 ? 24.954 24.158 10.838 1.00 32.45 ? 72 GLU A CG 1 ATOM 480 C CD . GLU A 1 72 ? 25.159 22.704 11.207 1.00 38.84 ? 72 GLU A CD 1 ATOM 481 O OE1 . GLU A 1 72 ? 25.567 21.916 10.328 1.00 43.37 ? 72 GLU A OE1 1 ATOM 482 O OE2 . GLU A 1 72 ? 24.901 22.348 12.374 1.00 41.10 ? 72 GLU A OE2 1 ATOM 483 N N . ILE A 1 73 ? 25.094 27.539 9.553 1.00 17.72 ? 73 ILE A N 1 ATOM 484 C CA . ILE A 1 73 ? 26.210 28.322 9.031 1.00 17.23 ? 73 ILE A CA 1 ATOM 485 C C . ILE A 1 73 ? 27.432 28.001 9.876 1.00 16.16 ? 73 ILE A C 1 ATOM 486 O O . ILE A 1 73 ? 27.415 28.210 11.091 1.00 16.72 ? 73 ILE A O 1 ATOM 487 C CB . ILE A 1 73 ? 25.889 29.835 9.106 1.00 18.54 ? 73 ILE A CB 1 ATOM 488 C CG1 . ILE A 1 73 ? 24.590 30.118 8.346 1.00 20.80 ? 73 ILE A CG1 1 ATOM 489 C CG2 . ILE A 1 73 ? 27.026 30.646 8.521 1.00 18.28 ? 73 ILE A CG2 1 ATOM 490 C CD1 . ILE A 1 73 ? 24.087 31.539 8.495 1.00 25.33 ? 73 ILE A CD1 1 ATOM 491 N N . ASP A 1 74 ? 28.483 27.480 9.240 1.00 15.67 ? 74 ASP A N 1 ATOM 492 C CA . ASP A 1 74 ? 29.699 27.112 9.965 1.00 19.82 ? 74 ASP A CA 1 ATOM 493 C C . ASP A 1 74 ? 30.518 28.343 10.315 1.00 18.66 ? 74 ASP A C 1 ATOM 494 O O . ASP A 1 74 ? 31.555 28.622 9.714 1.00 18.04 ? 74 ASP A O 1 ATOM 495 C CB . ASP A 1 74 ? 30.549 26.130 9.151 1.00 22.53 ? 74 ASP A CB 1 ATOM 496 C CG . ASP A 1 74 ? 31.806 25.688 9.895 1.00 31.49 ? 74 ASP A CG 1 ATOM 497 O OD1 . ASP A 1 74 ? 31.909 25.961 11.114 1.00 30.55 ? 74 ASP A OD1 1 ATOM 498 O OD2 . ASP A 1 74 ? 32.686 25.058 9.262 1.00 34.51 ? 74 ASP A OD2 1 ATOM 499 N N . THR A 1 75 ? 30.041 29.074 11.314 1.00 18.39 ? 75 THR A N 1 ATOM 500 C CA . THR A 1 75 ? 30.717 30.283 11.752 1.00 17.58 ? 75 THR A CA 1 ATOM 501 C C . THR A 1 75 ? 32.059 29.997 12.432 1.00 17.55 ? 75 THR A C 1 ATOM 502 O O . THR A 1 75 ? 32.991 30.791 12.327 1.00 16.97 ? 75 THR A O 1 ATOM 503 C CB . THR A 1 75 ? 29.818 31.077 12.728 1.00 17.80 ? 75 THR A CB 1 ATOM 504 O OG1 . THR A 1 75 ? 29.509 30.262 13.864 1.00 15.21 ? 75 THR A OG1 1 ATOM 505 C CG2 . THR A 1 75 ? 28.519 31.471 12.049 1.00 17.76 ? 75 THR A CG2 1 ATOM 506 N N . LYS A 1 76 ? 32.164 28.865 13.121 1.00 19.50 ? 76 LYS A N 1 ATOM 507 C CA . LYS A 1 76 ? 33.409 28.550 13.829 1.00 22.47 ? 76 LYS A CA 1 ATOM 508 C C . LYS A 1 76 ? 34.628 28.486 12.912 1.00 22.06 ? 76 LYS A C 1 ATOM 509 O O . LYS A 1 76 ? 35.648 29.114 13.183 1.00 22.62 ? 76 LYS A O 1 ATOM 510 C CB . LYS A 1 76 ? 33.278 27.235 14.595 1.00 23.29 ? 76 LYS A CB 1 ATOM 511 C CG . LYS A 1 76 ? 34.409 27.001 15.590 1.00 24.75 ? 76 LYS A CG 1 ATOM 512 C CD . LYS A 1 76 ? 34.170 25.751 16.419 1.00 30.89 ? 76 LYS A CD 1 ATOM 513 C CE . LYS A 1 76 ? 35.224 25.597 17.510 1.00 34.28 ? 76 LYS A CE 1 ATOM 514 N NZ . LYS A 1 76 ? 34.981 24.382 18.342 1.00 37.27 ? 76 LYS A NZ 1 ATOM 515 N N . SER A 1 77 ? 34.521 27.723 11.830 1.00 23.13 ? 77 SER A N 1 ATOM 516 C CA . SER A 1 77 ? 35.622 27.588 10.882 1.00 24.03 ? 77 SER A CA 1 ATOM 517 C C . SER A 1 77 ? 36.004 28.946 10.310 1.00 24.64 ? 77 SER A C 1 ATOM 518 O O . SER A 1 77 ? 37.178 29.224 10.081 1.00 23.04 ? 77 SER A O 1 ATOM 519 C CB . SER A 1 77 ? 35.227 26.651 9.742 1.00 25.24 ? 77 SER A CB 1 ATOM 520 O OG . SER A 1 77 ? 34.931 25.363 10.241 1.00 29.23 ? 77 SER A OG 1 ATOM 521 N N . TYR A 1 78 ? 34.999 29.787 10.081 1.00 23.03 ? 78 TYR A N 1 ATOM 522 C CA . TYR A 1 78 ? 35.221 31.125 9.546 1.00 22.00 ? 78 TYR A CA 1 ATOM 523 C C . TYR A 1 78 ? 36.134 31.952 10.451 1.00 22.79 ? 78 TYR A C 1 ATOM 524 O O . TYR A 1 78 ? 37.133 32.517 9.989 1.00 24.43 ? 78 TYR A O 1 ATOM 525 C CB . TYR A 1 78 ? 33.887 31.858 9.381 1.00 21.54 ? 78 TYR A CB 1 ATOM 526 C CG . TYR A 1 78 ? 34.044 33.266 8.859 1.00 20.28 ? 78 TYR A CG 1 ATOM 527 C CD1 . TYR A 1 78 ? 34.353 33.498 7.520 1.00 20.65 ? 78 TYR A CD1 1 ATOM 528 C CD2 . TYR A 1 78 ? 33.913 34.363 9.706 1.00 21.10 ? 78 TYR A CD2 1 ATOM 529 C CE1 . TYR A 1 78 ? 34.526 34.782 7.035 1.00 21.27 ? 78 TYR A CE1 1 ATOM 530 C CE2 . TYR A 1 78 ? 34.087 35.656 9.233 1.00 20.03 ? 78 TYR A CE2 1 ATOM 531 C CZ . TYR A 1 78 ? 34.393 35.854 7.891 1.00 21.64 ? 78 TYR A CZ 1 ATOM 532 O OH . TYR A 1 78 ? 34.563 37.120 7.395 1.00 22.80 ? 78 TYR A OH 1 ATOM 533 N N . TRP A 1 79 ? 35.790 32.030 11.736 1.00 18.95 ? 79 TRP A N 1 ATOM 534 C CA . TRP A 1 79 ? 36.592 32.799 12.686 1.00 20.51 ? 79 TRP A CA 1 ATOM 535 C C . TRP A 1 79 ? 37.962 32.197 12.961 1.00 21.46 ? 79 TRP A C 1 ATOM 536 O O . TRP A 1 79 ? 38.939 32.925 13.128 1.00 22.34 ? 79 TRP A O 1 ATOM 537 C CB . TRP A 1 79 ? 35.834 32.979 14.000 1.00 19.31 ? 79 TRP A CB 1 ATOM 538 C CG . TRP A 1 79 ? 34.638 33.851 13.837 1.00 19.66 ? 79 TRP A CG 1 ATOM 539 C CD1 . TRP A 1 79 ? 33.329 33.490 13.994 1.00 16.60 ? 79 TRP A CD1 1 ATOM 540 C CD2 . TRP A 1 79 ? 34.633 35.222 13.429 1.00 19.48 ? 79 TRP A CD2 1 ATOM 541 N NE1 . TRP A 1 79 ? 32.510 34.555 13.707 1.00 16.20 ? 79 TRP A NE1 1 ATOM 542 C CE2 . TRP A 1 79 ? 33.284 35.631 13.355 1.00 17.76 ? 79 TRP A CE2 1 ATOM 543 C CE3 . TRP A 1 79 ? 35.639 36.148 13.116 1.00 18.72 ? 79 TRP A CE3 1 ATOM 544 C CZ2 . TRP A 1 79 ? 32.914 36.926 12.978 1.00 16.03 ? 79 TRP A CZ2 1 ATOM 545 C CZ3 . TRP A 1 79 ? 35.268 37.437 12.742 1.00 18.78 ? 79 TRP A CZ3 1 ATOM 546 C CH2 . TRP A 1 79 ? 33.918 37.812 12.676 1.00 17.01 ? 79 TRP A CH2 1 ATOM 547 N N . LYS A 1 80 ? 38.045 30.874 13.011 1.00 24.34 ? 80 LYS A N 1 ATOM 548 C CA . LYS A 1 80 ? 39.335 30.232 13.260 1.00 30.17 ? 80 LYS A CA 1 ATOM 549 C C . LYS A 1 80 ? 40.317 30.563 12.141 1.00 30.58 ? 80 LYS A C 1 ATOM 550 O O . LYS A 1 80 ? 41.503 30.769 12.390 1.00 31.63 ? 80 LYS A O 1 ATOM 551 C CB . LYS A 1 80 ? 39.180 28.713 13.375 1.00 31.51 ? 80 LYS A CB 1 ATOM 552 C CG . LYS A 1 80 ? 38.360 28.260 14.577 1.00 36.41 ? 80 LYS A CG 1 ATOM 553 C CD . LYS A 1 80 ? 38.809 26.893 15.087 1.00 43.41 ? 80 LYS A CD 1 ATOM 554 C CE . LYS A 1 80 ? 38.839 25.834 13.983 1.00 47.77 ? 80 LYS A CE 1 ATOM 555 N NZ . LYS A 1 80 ? 37.494 25.567 13.390 1.00 52.64 ? 80 LYS A NZ 1 ATOM 556 N N . ALA A 1 81 ? 39.817 30.621 10.910 1.00 32.69 ? 81 ALA A N 1 ATOM 557 C CA . ALA A 1 81 ? 40.658 30.936 9.761 1.00 33.31 ? 81 ALA A CA 1 ATOM 558 C C . ALA A 1 81 ? 41.213 32.354 9.865 1.00 35.37 ? 81 ALA A C 1 ATOM 559 O O . ALA A 1 81 ? 42.218 32.678 9.234 1.00 38.51 ? 81 ALA A O 1 ATOM 560 C CB . ALA A 1 81 ? 39.863 30.774 8.475 1.00 32.45 ? 81 ALA A CB 1 ATOM 561 N N . LEU A 1 82 ? 40.560 33.196 10.662 1.00 34.23 ? 82 LEU A N 1 ATOM 562 C CA . LEU A 1 82 ? 41.008 34.571 10.846 1.00 34.52 ? 82 LEU A CA 1 ATOM 563 C C . LEU A 1 82 ? 41.847 34.710 12.112 1.00 33.38 ? 82 LEU A C 1 ATOM 564 O O . LEU A 1 82 ? 42.279 35.807 12.462 1.00 34.68 ? 82 LEU A O 1 ATOM 565 C CB . LEU A 1 82 ? 39.809 35.520 10.917 1.00 33.94 ? 82 LEU A CB 1 ATOM 566 C CG . LEU A 1 82 ? 38.970 35.653 9.644 1.00 35.86 ? 82 LEU A CG 1 ATOM 567 C CD1 . LEU A 1 82 ? 37.768 36.545 9.915 1.00 35.34 ? 82 LEU A CD1 1 ATOM 568 C CD2 . LEU A 1 82 ? 39.828 36.233 8.522 1.00 37.73 ? 82 LEU A CD2 1 ATOM 569 N N . GLY A 1 83 ? 42.066 33.592 12.798 1.00 32.86 ? 83 GLY A N 1 ATOM 570 C CA . GLY A 1 83 ? 42.863 33.608 14.012 1.00 33.07 ? 83 GLY A CA 1 ATOM 571 C C . GLY A 1 83 ? 42.095 34.064 15.235 1.00 34.41 ? 83 GLY A C 1 ATOM 572 O O . GLY A 1 83 ? 42.684 34.526 16.215 1.00 35.23 ? 83 GLY A O 1 ATOM 573 N N . ILE A 1 84 ? 40.774 33.931 15.182 1.00 33.59 ? 84 ILE A N 1 ATOM 574 C CA . ILE A 1 84 ? 39.921 34.341 16.287 1.00 33.45 ? 84 ILE A CA 1 ATOM 575 C C . ILE A 1 84 ? 39.173 33.135 16.847 1.00 33.84 ? 84 ILE A C 1 ATOM 576 O O . ILE A 1 84 ? 38.598 32.347 16.095 1.00 33.37 ? 84 ILE A O 1 ATOM 577 C CB . ILE A 1 84 ? 38.899 35.410 15.820 1.00 34.97 ? 84 ILE A CB 1 ATOM 578 C CG1 . ILE A 1 84 ? 39.638 36.685 15.398 1.00 34.79 ? 84 ILE A CG1 1 ATOM 579 C CG2 . ILE A 1 84 ? 37.902 35.705 16.929 1.00 35.54 ? 84 ILE A CG2 1 ATOM 580 C CD1 . ILE A 1 84 ? 38.751 37.753 14.790 1.00 38.00 ? 84 ILE A CD1 1 ATOM 581 N N . SER A 1 85 ? 39.202 32.985 18.167 1.00 32.75 ? 85 SER A N 1 ATOM 582 C CA . SER A 1 85 ? 38.511 31.890 18.841 1.00 33.34 ? 85 SER A CA 1 ATOM 583 C C . SER A 1 85 ? 37.092 32.372 19.125 1.00 30.81 ? 85 SER A C 1 ATOM 584 O O . SER A 1 85 ? 36.872 33.155 20.050 1.00 31.17 ? 85 SER A O 1 ATOM 585 C CB . SER A 1 85 ? 39.220 31.548 20.154 1.00 38.98 ? 85 SER A CB 1 ATOM 586 O OG . SER A 1 85 ? 39.370 32.706 20.964 1.00 46.07 ? 85 SER A OG 1 ATOM 587 N N . PRO A 1 86 ? 36.110 31.903 18.331 1.00 26.47 ? 86 PRO A N 1 ATOM 588 C CA . PRO A 1 86 ? 34.699 32.275 18.461 1.00 24.34 ? 86 PRO A CA 1 ATOM 589 C C . PRO A 1 86 ? 33.970 31.544 19.581 1.00 22.82 ? 86 PRO A C 1 ATOM 590 O O . PRO A 1 86 ? 34.427 30.517 20.064 1.00 25.99 ? 86 PRO A O 1 ATOM 591 C CB . PRO A 1 86 ? 34.135 31.907 17.097 1.00 24.44 ? 86 PRO A CB 1 ATOM 592 C CG . PRO A 1 86 ? 34.829 30.608 16.842 1.00 25.16 ? 86 PRO A CG 1 ATOM 593 C CD . PRO A 1 86 ? 36.278 30.911 17.254 1.00 26.35 ? 86 PRO A CD 1 ATOM 594 N N . PHE A 1 87 ? 32.814 32.074 19.963 1.00 18.99 ? 87 PHE A N 1 ATOM 595 C CA . PHE A 1 87 ? 32.013 31.478 21.020 1.00 19.16 ? 87 PHE A CA 1 ATOM 596 C C . PHE A 1 87 ? 31.159 30.317 20.522 1.00 19.03 ? 87 PHE A C 1 ATOM 597 O O . PHE A 1 87 ? 31.193 29.223 21.084 1.00 18.43 ? 87 PHE A O 1 ATOM 598 C CB . PHE A 1 87 ? 31.093 32.530 21.637 1.00 16.67 ? 87 PHE A CB 1 ATOM 599 C CG . PHE A 1 87 ? 30.223 31.998 22.737 1.00 18.90 ? 87 PHE A CG 1 ATOM 600 C CD1 . PHE A 1 87 ? 30.752 31.743 23.995 1.00 21.59 ? 87 PHE A CD1 1 ATOM 601 C CD2 . PHE A 1 87 ? 28.880 31.738 22.510 1.00 18.06 ? 87 PHE A CD2 1 ATOM 602 C CE1 . PHE A 1 87 ? 29.954 31.236 25.017 1.00 19.41 ? 87 PHE A CE1 1 ATOM 603 C CE2 . PHE A 1 87 ? 28.066 31.230 23.523 1.00 21.72 ? 87 PHE A CE2 1 ATOM 604 C CZ . PHE A 1 87 ? 28.606 30.978 24.780 1.00 19.23 ? 87 PHE A CZ 1 ATOM 605 N N . HIS A 1 88 ? 30.400 30.561 19.458 1.00 17.59 ? 88 HIS A N 1 ATOM 606 C CA . HIS A 1 88 ? 29.497 29.552 18.905 1.00 17.86 ? 88 HIS A CA 1 ATOM 607 C C . HIS A 1 88 ? 30.138 28.491 18.026 1.00 18.48 ? 88 HIS A C 1 ATOM 608 O O . HIS A 1 88 ? 31.106 28.752 17.316 1.00 20.52 ? 88 HIS A O 1 ATOM 609 C CB . HIS A 1 88 ? 28.388 30.238 18.101 1.00 16.93 ? 88 HIS A CB 1 ATOM 610 C CG . HIS A 1 88 ? 27.717 31.350 18.838 1.00 16.94 ? 88 HIS A CG 1 ATOM 611 N ND1 . HIS A 1 88 ? 28.180 32.647 18.810 1.00 18.88 ? 88 HIS A ND1 1 ATOM 612 C CD2 . HIS A 1 88 ? 26.648 31.350 19.669 1.00 21.52 ? 88 HIS A CD2 1 ATOM 613 C CE1 . HIS A 1 88 ? 27.427 33.400 19.591 1.00 20.18 ? 88 HIS A CE1 1 ATOM 614 N NE2 . HIS A 1 88 ? 26.490 32.637 20.125 1.00 23.72 ? 88 HIS A NE2 1 ATOM 615 N N . GLU A 1 89 ? 29.569 27.292 18.070 1.00 18.39 ? 89 GLU A N 1 ATOM 616 C CA . GLU A 1 89 ? 30.043 26.186 17.254 1.00 19.02 ? 89 GLU A CA 1 ATOM 617 C C . GLU A 1 89 ? 29.593 26.461 15.825 1.00 20.10 ? 89 GLU A C 1 ATOM 618 O O . GLU A 1 89 ? 30.276 26.129 14.856 1.00 19.82 ? 89 GLU A O 1 ATOM 619 C CB . GLU A 1 89 ? 29.440 24.870 17.753 1.00 20.38 ? 89 GLU A CB 1 ATOM 620 C CG . GLU A 1 89 ? 30.087 24.380 19.023 1.00 21.13 ? 89 GLU A CG 1 ATOM 621 C CD . GLU A 1 89 ? 31.568 24.133 18.828 1.00 24.60 ? 89 GLU A CD 1 ATOM 622 O OE1 . GLU A 1 89 ? 31.908 23.278 17.992 1.00 28.56 ? 89 GLU A OE1 1 ATOM 623 O OE2 . GLU A 1 89 ? 32.385 24.797 19.496 1.00 27.72 ? 89 GLU A OE2 1 ATOM 624 N N . HIS A 1 90 ? 28.423 27.078 15.715 1.00 19.35 ? 90 HIS A N 1 ATOM 625 C CA . HIS A 1 90 ? 27.850 27.432 14.430 1.00 20.41 ? 90 HIS A CA 1 ATOM 626 C C . HIS A 1 90 ? 26.599 28.253 14.685 1.00 18.97 ? 90 HIS A C 1 ATOM 627 O O . HIS A 1 90 ? 26.208 28.475 15.832 1.00 20.02 ? 90 HIS A O 1 ATOM 628 C CB . HIS A 1 90 ? 27.496 26.171 13.627 1.00 23.57 ? 90 HIS A CB 1 ATOM 629 C CG . HIS A 1 90 ? 26.560 25.242 14.336 1.00 28.22 ? 90 HIS A CG 1 ATOM 630 N ND1 . HIS A 1 90 ? 26.912 23.956 14.688 1.00 29.82 ? 90 HIS A ND1 1 ATOM 631 C CD2 . HIS A 1 90 ? 25.287 25.413 14.762 1.00 31.07 ? 90 HIS A CD2 1 ATOM 632 C CE1 . HIS A 1 90 ? 25.895 23.375 15.300 1.00 30.99 ? 90 HIS A CE1 1 ATOM 633 N NE2 . HIS A 1 90 ? 24.896 24.239 15.358 1.00 32.28 ? 90 HIS A NE2 1 ATOM 634 N N . ALA A 1 91 ? 25.979 28.721 13.614 1.00 17.49 ? 91 ALA A N 1 ATOM 635 C CA . ALA A 1 91 ? 24.756 29.481 13.733 1.00 19.59 ? 91 ALA A CA 1 ATOM 636 C C . ALA A 1 91 ? 23.691 28.675 12.998 1.00 21.59 ? 91 ALA A C 1 ATOM 637 O O . ALA A 1 91 ? 23.907 28.233 11.877 1.00 21.56 ? 91 ALA A O 1 ATOM 638 C CB . ALA A 1 91 ? 24.918 30.858 13.106 1.00 20.47 ? 91 ALA A CB 1 ATOM 639 N N . GLU A 1 92 ? 22.552 28.470 13.648 1.00 23.43 ? 92 GLU A N 1 ATOM 640 C CA . GLU A 1 92 ? 21.458 27.705 13.061 1.00 26.73 ? 92 GLU A CA 1 ATOM 641 C C . GLU A 1 92 ? 20.195 28.536 12.934 1.00 24.57 ? 92 GLU A C 1 ATOM 642 O O . GLU A 1 92 ? 19.868 29.322 13.815 1.00 25.31 ? 92 GLU A O 1 ATOM 643 C CB . GLU A 1 92 ? 21.139 26.480 13.920 1.00 31.24 ? 92 GLU A CB 1 ATOM 644 C CG . GLU A 1 92 ? 22.036 25.279 13.696 1.00 42.73 ? 92 GLU A CG 1 ATOM 645 C CD . GLU A 1 92 ? 21.642 24.110 14.582 1.00 49.32 ? 92 GLU A CD 1 ATOM 646 O OE1 . GLU A 1 92 ? 20.427 23.846 14.710 1.00 52.53 ? 92 GLU A OE1 1 ATOM 647 O OE2 . GLU A 1 92 ? 22.543 23.453 15.146 1.00 53.07 ? 92 GLU A OE2 1 ATOM 648 N N . VAL A 1 93 ? 19.488 28.356 11.828 1.00 19.94 ? 93 VAL A N 1 ATOM 649 C CA . VAL A 1 93 ? 18.238 29.064 11.600 1.00 19.32 ? 93 VAL A CA 1 ATOM 650 C C . VAL A 1 93 ? 17.231 27.977 11.241 1.00 18.18 ? 93 VAL A C 1 ATOM 651 O O . VAL A 1 93 ? 17.395 27.291 10.242 1.00 16.00 ? 93 VAL A O 1 ATOM 652 C CB . VAL A 1 93 ? 18.373 30.068 10.439 1.00 20.53 ? 93 VAL A CB 1 ATOM 653 C CG1 . VAL A 1 93 ? 17.066 30.820 10.239 1.00 22.75 ? 93 VAL A CG1 1 ATOM 654 C CG2 . VAL A 1 93 ? 19.503 31.048 10.745 1.00 24.49 ? 93 VAL A CG2 1 ATOM 655 N N . VAL A 1 94 ? 16.200 27.819 12.064 1.00 15.84 ? 94 VAL A N 1 ATOM 656 C CA . VAL A 1 94 ? 15.188 26.791 11.831 1.00 16.49 ? 94 VAL A CA 1 ATOM 657 C C . VAL A 1 94 ? 13.838 27.447 11.604 1.00 17.45 ? 94 VAL A C 1 ATOM 658 O O . VAL A 1 94 ? 13.394 28.256 12.423 1.00 16.38 ? 94 VAL A O 1 ATOM 659 C CB . VAL A 1 94 ? 15.098 25.839 13.038 1.00 16.68 ? 94 VAL A CB 1 ATOM 660 C CG1 . VAL A 1 94 ? 14.133 24.699 12.743 1.00 17.02 ? 94 VAL A CG1 1 ATOM 661 C CG2 . VAL A 1 94 ? 16.486 25.297 13.362 1.00 16.20 ? 94 VAL A CG2 1 ATOM 662 N N . PHE A 1 95 ? 13.186 27.095 10.498 1.00 15.75 ? 95 PHE A N 1 ATOM 663 C CA . PHE A 1 95 ? 11.901 27.693 10.155 1.00 17.75 ? 95 PHE A CA 1 ATOM 664 C C . PHE A 1 95 ? 11.013 26.800 9.305 1.00 17.07 ? 95 PHE A C 1 ATOM 665 O O . PHE A 1 95 ? 11.496 25.913 8.608 1.00 18.23 ? 95 PHE A O 1 ATOM 666 C CB . PHE A 1 95 ? 12.126 29.001 9.388 1.00 16.19 ? 95 PHE A CB 1 ATOM 667 C CG . PHE A 1 95 ? 12.863 28.822 8.082 1.00 18.71 ? 95 PHE A CG 1 ATOM 668 C CD1 . PHE A 1 95 ? 14.222 28.512 8.069 1.00 18.56 ? 95 PHE A CD1 1 ATOM 669 C CD2 . PHE A 1 95 ? 12.197 28.962 6.863 1.00 15.42 ? 95 PHE A CD2 1 ATOM 670 C CE1 . PHE A 1 95 ? 14.910 28.344 6.858 1.00 17.87 ? 95 PHE A CE1 1 ATOM 671 C CE2 . PHE A 1 95 ? 12.873 28.798 5.653 1.00 17.88 ? 95 PHE A CE2 1 ATOM 672 C CZ . PHE A 1 95 ? 14.234 28.487 5.652 1.00 17.60 ? 95 PHE A CZ 1 ATOM 673 N N . THR A 1 96 ? 9.706 27.043 9.369 1.00 18.00 ? 96 THR A N 1 ATOM 674 C CA . THR A 1 96 ? 8.774 26.296 8.539 1.00 17.81 ? 96 THR A CA 1 ATOM 675 C C . THR A 1 96 ? 8.713 27.097 7.253 1.00 16.64 ? 96 THR A C 1 ATOM 676 O O . THR A 1 96 ? 8.637 28.330 7.274 1.00 17.55 ? 96 THR A O 1 ATOM 677 C CB . THR A 1 96 ? 7.363 26.219 9.151 1.00 18.89 ? 96 THR A CB 1 ATOM 678 O OG1 . THR A 1 96 ? 7.425 25.541 10.413 1.00 21.36 ? 96 THR A OG1 1 ATOM 679 C CG2 . THR A 1 96 ? 6.429 25.450 8.215 1.00 21.63 ? 96 THR A CG2 1 ATOM 680 N N . ALA A 1 97 ? 8.759 26.411 6.124 1.00 17.14 ? 97 ALA A N 1 ATOM 681 C CA . ALA A 1 97 ? 8.734 27.111 4.858 1.00 18.07 ? 97 ALA A CA 1 ATOM 682 C C . ALA A 1 97 ? 7.601 26.651 3.964 1.00 17.69 ? 97 ALA A C 1 ATOM 683 O O . ALA A 1 97 ? 7.177 25.497 4.020 1.00 19.31 ? 97 ALA A O 1 ATOM 684 C CB . ALA A 1 97 ? 10.071 26.931 4.144 1.00 20.02 ? 97 ALA A CB 1 ATOM 685 N N . ASN A 1 98 ? 7.101 27.588 3.170 1.00 20.57 ? 98 ASN A N 1 ATOM 686 C CA . ASN A 1 98 ? 6.040 27.342 2.207 1.00 24.50 ? 98 ASN A CA 1 ATOM 687 C C . ASN A 1 98 ? 4.736 26.770 2.750 1.00 27.71 ? 98 ASN A C 1 ATOM 688 O O . ASN A 1 98 ? 3.943 26.224 1.986 1.00 29.13 ? 98 ASN A O 1 ATOM 689 C CB . ASN A 1 98 ? 6.587 26.434 1.111 1.00 23.59 ? 98 ASN A CB 1 ATOM 690 C CG . ASN A 1 98 ? 7.927 26.908 0.601 1.00 23.65 ? 98 ASN A CG 1 ATOM 691 O OD1 . ASN A 1 98 ? 8.072 28.063 0.203 1.00 25.59 ? 98 ASN A OD1 1 ATOM 692 N ND2 . ASN A 1 98 ? 8.918 26.026 0.616 1.00 22.62 ? 98 ASN A ND2 1 ATOM 693 N N . ASP A 1 99 ? 4.502 26.915 4.050 1.00 30.30 ? 99 ASP A N 1 ATOM 694 C CA . ASP A 1 99 ? 3.292 26.390 4.682 1.00 36.41 ? 99 ASP A CA 1 ATOM 695 C C . ASP A 1 99 ? 1.994 26.960 4.107 1.00 39.30 ? 99 ASP A C 1 ATOM 696 O O . ASP A 1 99 ? 0.945 26.316 4.178 1.00 39.86 ? 99 ASP A O 1 ATOM 697 C CB . ASP A 1 99 ? 3.341 26.644 6.189 1.00 39.45 ? 99 ASP A CB 1 ATOM 698 C CG . ASP A 1 99 ? 3.659 28.082 6.519 1.00 44.03 ? 99 ASP A CG 1 ATOM 699 O OD1 . ASP A 1 99 ? 4.738 28.563 6.105 1.00 46.37 ? 99 ASP A OD1 1 ATOM 700 O OD2 . ASP A 1 99 ? 2.832 28.735 7.189 1.00 48.16 ? 99 ASP A OD2 1 ATOM 701 N N . SER A 1 100 ? 2.057 28.164 3.546 1.00 40.06 ? 100 SER A N 1 ATOM 702 C CA . SER A 1 100 ? 0.876 28.786 2.959 1.00 42.14 ? 100 SER A CA 1 ATOM 703 C C . SER A 1 100 ? 1.165 29.139 1.508 1.00 40.68 ? 100 SER A C 1 ATOM 704 O O . SER A 1 100 ? 0.759 30.191 1.016 1.00 42.71 ? 100 SER A O 1 ATOM 705 C CB . SER A 1 100 ? 0.489 30.051 3.730 1.00 44.08 ? 100 SER A CB 1 ATOM 706 O OG . SER A 1 100 ? 1.452 31.075 3.553 1.00 50.72 ? 100 SER A OG 1 ATOM 707 N N . GLY A 1 101 ? 1.876 28.248 0.829 1.00 36.90 ? 101 GLY A N 1 ATOM 708 C CA . GLY A 1 101 ? 2.220 28.479 -0.557 1.00 33.95 ? 101 GLY A CA 1 ATOM 709 C C . GLY A 1 101 ? 3.694 28.801 -0.696 1.00 32.43 ? 101 GLY A C 1 ATOM 710 O O . GLY A 1 101 ? 4.368 29.068 0.302 1.00 30.10 ? 101 GLY A O 1 ATOM 711 N N . PRO A 1 102 ? 4.223 28.782 -1.927 1.00 30.64 ? 102 PRO A N 1 ATOM 712 C CA . PRO A 1 102 ? 5.632 29.072 -2.205 1.00 29.04 ? 102 PRO A CA 1 ATOM 713 C C . PRO A 1 102 ? 6.018 30.520 -1.932 1.00 28.80 ? 102 PRO A C 1 ATOM 714 O O . PRO A 1 102 ? 5.327 31.453 -2.347 1.00 28.73 ? 102 PRO A O 1 ATOM 715 C CB . PRO A 1 102 ? 5.774 28.705 -3.678 1.00 29.80 ? 102 PRO A CB 1 ATOM 716 C CG . PRO A 1 102 ? 4.418 29.041 -4.227 1.00 33.11 ? 102 PRO A CG 1 ATOM 717 C CD . PRO A 1 102 ? 3.495 28.474 -3.172 1.00 31.16 ? 102 PRO A CD 1 ATOM 718 N N . ARG A 1 103 ? 7.127 30.693 -1.224 1.00 26.03 ? 103 ARG A N 1 ATOM 719 C CA . ARG A 1 103 ? 7.640 32.012 -0.882 1.00 24.06 ? 103 ARG A CA 1 ATOM 720 C C . ARG A 1 103 ? 9.127 32.014 -1.191 1.00 24.13 ? 103 ARG A C 1 ATOM 721 O O . ARG A 1 103 ? 9.721 30.956 -1.386 1.00 24.14 ? 103 ARG A O 1 ATOM 722 C CB . ARG A 1 103 ? 7.441 32.290 0.612 1.00 24.82 ? 103 ARG A CB 1 ATOM 723 C CG . ARG A 1 103 ? 5.992 32.411 1.057 1.00 25.56 ? 103 ARG A CG 1 ATOM 724 C CD . ARG A 1 103 ? 5.401 33.753 0.648 1.00 29.75 ? 103 ARG A CD 1 ATOM 725 N NE . ARG A 1 103 ? 4.037 33.914 1.143 1.00 35.96 ? 103 ARG A NE 1 ATOM 726 C CZ . ARG A 1 103 ? 2.980 33.271 0.653 1.00 37.34 ? 103 ARG A CZ 1 ATOM 727 N NH1 . ARG A 1 103 ? 3.125 32.421 -0.354 1.00 37.78 ? 103 ARG A NH1 1 ATOM 728 N NH2 . ARG A 1 103 ? 1.775 33.475 1.173 1.00 41.35 ? 103 ARG A NH2 1 ATOM 729 N N . ARG A 1 104 ? 9.721 33.201 -1.245 1.00 22.70 ? 104 ARG A N 1 ATOM 730 C CA . ARG A 1 104 ? 11.152 33.320 -1.493 1.00 23.50 ? 104 ARG A CA 1 ATOM 731 C C . ARG A 1 104 ? 11.755 33.748 -0.164 1.00 21.38 ? 104 ARG A C 1 ATOM 732 O O . ARG A 1 104 ? 11.298 34.708 0.449 1.00 19.24 ? 104 ARG A O 1 ATOM 733 C CB . ARG A 1 104 ? 11.437 34.361 -2.575 1.00 28.94 ? 104 ARG A CB 1 ATOM 734 C CG . ARG A 1 104 ? 10.707 34.089 -3.888 1.00 40.73 ? 104 ARG A CG 1 ATOM 735 C CD . ARG A 1 104 ? 10.785 32.613 -4.262 1.00 50.04 ? 104 ARG A CD 1 ATOM 736 N NE . ARG A 1 104 ? 9.795 32.240 -5.270 1.00 58.10 ? 104 ARG A NE 1 ATOM 737 C CZ . ARG A 1 104 ? 9.421 30.989 -5.523 1.00 60.37 ? 104 ARG A CZ 1 ATOM 738 N NH1 . ARG A 1 104 ? 9.953 29.983 -4.841 1.00 62.00 ? 104 ARG A NH1 1 ATOM 739 N NH2 . ARG A 1 104 ? 8.505 30.742 -6.450 1.00 63.38 ? 104 ARG A NH2 1 ATOM 740 N N . TYR A 1 105 ? 12.778 33.030 0.277 1.00 17.97 ? 105 TYR A N 1 ATOM 741 C CA . TYR A 1 105 ? 13.400 33.326 1.558 1.00 16.28 ? 105 TYR A CA 1 ATOM 742 C C . TYR A 1 105 ? 14.841 33.774 1.452 1.00 16.57 ? 105 TYR A C 1 ATOM 743 O O . TYR A 1 105 ? 15.654 33.131 0.784 1.00 16.34 ? 105 TYR A O 1 ATOM 744 C CB . TYR A 1 105 ? 13.365 32.097 2.466 1.00 16.52 ? 105 TYR A CB 1 ATOM 745 C CG . TYR A 1 105 ? 11.985 31.560 2.733 1.00 17.74 ? 105 TYR A CG 1 ATOM 746 C CD1 . TYR A 1 105 ? 11.343 30.750 1.803 1.00 18.85 ? 105 TYR A CD1 1 ATOM 747 C CD2 . TYR A 1 105 ? 11.308 31.886 3.905 1.00 18.00 ? 105 TYR A CD2 1 ATOM 748 C CE1 . TYR A 1 105 ? 10.056 30.278 2.029 1.00 20.31 ? 105 TYR A CE1 1 ATOM 749 C CE2 . TYR A 1 105 ? 10.017 31.420 4.145 1.00 22.04 ? 105 TYR A CE2 1 ATOM 750 C CZ . TYR A 1 105 ? 9.398 30.616 3.197 1.00 20.64 ? 105 TYR A CZ 1 ATOM 751 O OH . TYR A 1 105 ? 8.114 30.168 3.410 1.00 19.20 ? 105 TYR A OH 1 ATOM 752 N N . THR A 1 106 ? 15.142 34.891 2.105 1.00 16.59 ? 106 THR A N 1 ATOM 753 C CA . THR A 1 106 ? 16.499 35.391 2.166 1.00 17.12 ? 106 THR A CA 1 ATOM 754 C C . THR A 1 106 ? 16.846 35.322 3.643 1.00 17.22 ? 106 THR A C 1 ATOM 755 O O . THR A 1 106 ? 16.174 35.935 4.479 1.00 15.30 ? 106 THR A O 1 ATOM 756 C CB . THR A 1 106 ? 16.629 36.845 1.685 1.00 19.44 ? 106 THR A CB 1 ATOM 757 O OG1 . THR A 1 106 ? 16.346 36.911 0.285 1.00 22.98 ? 106 THR A OG1 1 ATOM 758 C CG2 . THR A 1 106 ? 18.051 37.346 1.918 1.00 23.18 ? 106 THR A CG2 1 ATOM 759 N N . ILE A 1 107 ? 17.865 34.533 3.961 1.00 13.85 ? 107 ILE A N 1 ATOM 760 C CA . ILE A 1 107 ? 18.312 34.378 5.335 1.00 17.54 ? 107 ILE A CA 1 ATOM 761 C C . ILE A 1 107 ? 19.614 35.167 5.446 1.00 17.44 ? 107 ILE A C 1 ATOM 762 O O . ILE A 1 107 ? 20.591 34.859 4.771 1.00 20.56 ? 107 ILE A O 1 ATOM 763 C CB . ILE A 1 107 ? 18.585 32.895 5.661 1.00 19.52 ? 107 ILE A CB 1 ATOM 764 C CG1 . ILE A 1 107 ? 17.316 32.065 5.433 1.00 22.71 ? 107 ILE A CG1 1 ATOM 765 C CG2 . ILE A 1 107 ? 19.067 32.754 7.094 1.00 20.34 ? 107 ILE A CG2 1 ATOM 766 C CD1 . ILE A 1 107 ? 16.157 32.432 6.329 1.00 25.72 ? 107 ILE A CD1 1 ATOM 767 N N . ALA A 1 108 ? 19.620 36.191 6.282 1.00 16.44 ? 108 ALA A N 1 ATOM 768 C CA . ALA A 1 108 ? 20.815 37.006 6.447 1.00 16.45 ? 108 ALA A CA 1 ATOM 769 C C . ALA A 1 108 ? 21.381 36.823 7.839 1.00 17.90 ? 108 ALA A C 1 ATOM 770 O O . ALA A 1 108 ? 20.633 36.717 8.809 1.00 16.69 ? 108 ALA A O 1 ATOM 771 C CB . ALA A 1 108 ? 20.483 38.465 6.214 1.00 18.20 ? 108 ALA A CB 1 ATOM 772 N N . ALA A 1 109 ? 22.706 36.779 7.931 1.00 15.90 ? 109 ALA A N 1 ATOM 773 C CA . ALA A 1 109 ? 23.372 36.626 9.214 1.00 16.58 ? 109 ALA A CA 1 ATOM 774 C C . ALA A 1 109 ? 24.492 37.656 9.311 1.00 18.10 ? 109 ALA A C 1 ATOM 775 O O . ALA A 1 109 ? 25.205 37.898 8.341 1.00 18.16 ? 109 ALA A O 1 ATOM 776 C CB . ALA A 1 109 ? 23.940 35.215 9.336 1.00 18.41 ? 109 ALA A CB 1 ATOM 777 N N . LEU A 1 110 ? 24.624 38.280 10.475 1.00 15.06 ? 110 LEU A N 1 ATOM 778 C CA . LEU A 1 110 ? 25.676 39.258 10.716 1.00 13.63 ? 110 LEU A CA 1 ATOM 779 C C . LEU A 1 110 ? 26.508 38.624 11.821 1.00 15.80 ? 110 LEU A C 1 ATOM 780 O O . LEU A 1 110 ? 26.007 38.370 12.920 1.00 15.39 ? 110 LEU A O 1 ATOM 781 C CB . LEU A 1 110 ? 25.078 40.590 11.173 1.00 14.66 ? 110 LEU A CB 1 ATOM 782 C CG . LEU A 1 110 ? 26.109 41.674 11.503 1.00 16.58 ? 110 LEU A CG 1 ATOM 783 C CD1 . LEU A 1 110 ? 26.975 41.953 10.286 1.00 15.38 ? 110 LEU A CD1 1 ATOM 784 C CD2 . LEU A 1 110 ? 25.401 42.930 11.942 1.00 19.43 ? 110 LEU A CD2 1 ATOM 785 N N . LEU A 1 111 ? 27.779 38.380 11.530 1.00 12.17 ? 111 LEU A N 1 ATOM 786 C CA . LEU A 1 111 ? 28.647 37.686 12.462 1.00 15.10 ? 111 LEU A CA 1 ATOM 787 C C . LEU A 1 111 ? 29.712 38.477 13.205 1.00 15.95 ? 111 LEU A C 1 ATOM 788 O O . LEU A 1 111 ? 30.367 39.354 12.646 1.00 13.75 ? 111 LEU A O 1 ATOM 789 C CB . LEU A 1 111 ? 29.353 36.542 11.732 1.00 13.59 ? 111 LEU A CB 1 ATOM 790 C CG . LEU A 1 111 ? 28.563 35.623 10.791 1.00 16.90 ? 111 LEU A CG 1 ATOM 791 C CD1 . LEU A 1 111 ? 29.532 34.624 10.171 1.00 16.80 ? 111 LEU A CD1 1 ATOM 792 C CD2 . LEU A 1 111 ? 27.457 34.900 11.550 1.00 14.48 ? 111 LEU A CD2 1 ATOM 793 N N . SER A 1 112 ? 29.872 38.119 14.474 1.00 16.77 ? 112 SER A N 1 ATOM 794 C CA . SER A 1 112 ? 30.884 38.682 15.358 1.00 17.11 ? 112 SER A CA 1 ATOM 795 C C . SER A 1 112 ? 31.371 37.456 16.121 1.00 16.00 ? 112 SER A C 1 ATOM 796 O O . SER A 1 112 ? 30.672 36.441 16.192 1.00 15.84 ? 112 SER A O 1 ATOM 797 C CB . SER A 1 112 ? 30.293 39.717 16.321 1.00 19.82 ? 112 SER A CB 1 ATOM 798 O OG . SER A 1 112 ? 29.963 40.912 15.631 1.00 25.12 ? 112 SER A OG 1 ATOM 799 N N . PRO A 1 113 ? 32.578 37.517 16.685 1.00 16.96 ? 113 PRO A N 1 ATOM 800 C CA . PRO A 1 113 ? 33.086 36.357 17.422 1.00 16.86 ? 113 PRO A CA 1 ATOM 801 C C . PRO A 1 113 ? 32.169 35.826 18.525 1.00 16.57 ? 113 PRO A C 1 ATOM 802 O O . PRO A 1 113 ? 32.011 34.617 18.673 1.00 16.72 ? 113 PRO A O 1 ATOM 803 C CB . PRO A 1 113 ? 34.422 36.862 17.960 1.00 17.55 ? 113 PRO A CB 1 ATOM 804 C CG . PRO A 1 113 ? 34.888 37.753 16.843 1.00 16.93 ? 113 PRO A CG 1 ATOM 805 C CD . PRO A 1 113 ? 33.623 38.545 16.534 1.00 14.86 ? 113 PRO A CD 1 ATOM 806 N N . TYR A 1 114 ? 31.560 36.724 19.296 1.00 16.18 ? 114 TYR A N 1 ATOM 807 C CA . TYR A 1 114 ? 30.686 36.294 20.385 1.00 15.66 ? 114 TYR A CA 1 ATOM 808 C C . TYR A 1 114 ? 29.227 36.633 20.187 1.00 15.45 ? 114 TYR A C 1 ATOM 809 O O . TYR A 1 114 ? 28.438 36.576 21.124 1.00 17.44 ? 114 TYR A O 1 ATOM 810 C CB . TYR A 1 114 ? 31.165 36.899 21.706 1.00 15.07 ? 114 TYR A CB 1 ATOM 811 C CG . TYR A 1 114 ? 32.374 36.194 22.256 1.00 21.33 ? 114 TYR A CG 1 ATOM 812 C CD1 . TYR A 1 114 ? 33.609 36.294 21.620 1.00 22.43 ? 114 TYR A CD1 1 ATOM 813 C CD2 . TYR A 1 114 ? 32.280 35.396 23.400 1.00 19.95 ? 114 TYR A CD2 1 ATOM 814 C CE1 . TYR A 1 114 ? 34.727 35.615 22.110 1.00 27.26 ? 114 TYR A CE1 1 ATOM 815 C CE2 . TYR A 1 114 ? 33.390 34.715 23.893 1.00 22.36 ? 114 TYR A CE2 1 ATOM 816 C CZ . TYR A 1 114 ? 34.608 34.830 23.244 1.00 26.87 ? 114 TYR A CZ 1 ATOM 817 O OH . TYR A 1 114 ? 35.711 34.160 23.725 1.00 31.46 ? 114 TYR A OH 1 ATOM 818 N N . SER A 1 115 ? 28.856 36.977 18.965 1.00 14.73 ? 115 SER A N 1 ATOM 819 C CA . SER A 1 115 ? 27.480 37.337 18.718 1.00 14.62 ? 115 SER A CA 1 ATOM 820 C C . SER A 1 115 ? 27.138 37.214 17.248 1.00 16.24 ? 115 SER A C 1 ATOM 821 O O . SER A 1 115 ? 28.009 37.295 16.386 1.00 17.96 ? 115 SER A O 1 ATOM 822 C CB . SER A 1 115 ? 27.244 38.783 19.172 1.00 15.49 ? 115 SER A CB 1 ATOM 823 O OG . SER A 1 115 ? 25.933 39.229 18.850 1.00 21.51 ? 115 SER A OG 1 ATOM 824 N N . TYR A 1 116 ? 25.868 36.965 16.973 1.00 16.19 ? 116 TYR A N 1 ATOM 825 C CA . TYR A 1 116 ? 25.411 36.932 15.600 1.00 16.03 ? 116 TYR A CA 1 ATOM 826 C C . TYR A 1 116 ? 23.945 37.285 15.623 1.00 16.92 ? 116 TYR A C 1 ATOM 827 O O . TYR A 1 116 ? 23.258 37.122 16.634 1.00 14.46 ? 116 TYR A O 1 ATOM 828 C CB . TYR A 1 116 ? 25.662 35.576 14.923 1.00 18.91 ? 116 TYR A CB 1 ATOM 829 C CG . TYR A 1 116 ? 24.874 34.400 15.450 1.00 17.63 ? 116 TYR A CG 1 ATOM 830 C CD1 . TYR A 1 116 ? 23.543 34.192 15.086 1.00 20.88 ? 116 TYR A CD1 1 ATOM 831 C CD2 . TYR A 1 116 ? 25.477 33.476 16.294 1.00 19.77 ? 116 TYR A CD2 1 ATOM 832 C CE1 . TYR A 1 116 ? 22.830 33.073 15.557 1.00 20.17 ? 116 TYR A CE1 1 ATOM 833 C CE2 . TYR A 1 116 ? 24.785 32.368 16.762 1.00 20.52 ? 116 TYR A CE2 1 ATOM 834 C CZ . TYR A 1 116 ? 23.471 32.168 16.396 1.00 22.31 ? 116 TYR A CZ 1 ATOM 835 O OH . TYR A 1 116 ? 22.815 31.058 16.875 1.00 27.77 ? 116 TYR A OH 1 ATOM 836 N N . SER A 1 117 ? 23.488 37.838 14.516 1.00 17.08 ? 117 SER A N 1 ATOM 837 C CA . SER A 1 117 ? 22.108 38.224 14.385 1.00 17.37 ? 117 SER A CA 1 ATOM 838 C C . SER A 1 117 ? 21.696 37.639 13.068 1.00 15.28 ? 117 SER A C 1 ATOM 839 O O . SER A 1 117 ? 22.503 37.542 12.142 1.00 17.10 ? 117 SER A O 1 ATOM 840 C CB . SER A 1 117 ? 21.978 39.745 14.327 1.00 18.18 ? 117 SER A CB 1 ATOM 841 O OG . SER A 1 117 ? 22.581 40.356 15.455 1.00 26.75 ? 117 SER A OG 1 ATOM 842 N N . THR A 1 118 ? 20.451 37.210 12.986 1.00 15.11 ? 118 THR A N 1 ATOM 843 C CA . THR A 1 118 ? 19.967 36.667 11.746 1.00 15.87 ? 118 THR A CA 1 ATOM 844 C C . THR A 1 118 ? 18.589 37.235 11.547 1.00 17.24 ? 118 THR A C 1 ATOM 845 O O . THR A 1 118 ? 17.847 37.446 12.508 1.00 18.41 ? 118 THR A O 1 ATOM 846 C CB . THR A 1 118 ? 19.893 35.130 11.777 1.00 18.71 ? 118 THR A CB 1 ATOM 847 O OG1 . THR A 1 118 ? 19.442 34.661 10.505 1.00 19.57 ? 118 THR A OG1 1 ATOM 848 C CG2 . THR A 1 118 ? 18.933 34.644 12.854 1.00 18.70 ? 118 THR A CG2 1 ATOM 849 N N . THR A 1 119 ? 18.265 37.535 10.302 1.00 15.08 ? 119 THR A N 1 ATOM 850 C CA . THR A 1 119 ? 16.951 38.038 10.001 1.00 14.92 ? 119 THR A CA 1 ATOM 851 C C . THR A 1 119 ? 16.516 37.332 8.731 1.00 15.42 ? 119 THR A C 1 ATOM 852 O O . THR A 1 119 ? 17.336 36.748 8.019 1.00 15.21 ? 119 THR A O 1 ATOM 853 C CB . THR A 1 119 ? 16.943 39.572 9.808 1.00 17.82 ? 119 THR A CB 1 ATOM 854 O OG1 . THR A 1 119 ? 15.588 40.029 9.748 1.00 19.82 ? 119 THR A OG1 1 ATOM 855 C CG2 . THR A 1 119 ? 17.663 39.976 8.529 1.00 17.57 ? 119 THR A CG2 1 ATOM 856 N N . ALA A 1 120 ? 15.222 37.353 8.472 1.00 14.82 ? 120 ALA A N 1 ATOM 857 C CA . ALA A 1 120 ? 14.706 36.724 7.283 1.00 17.28 ? 120 ALA A CA 1 ATOM 858 C C . ALA A 1 120 ? 13.864 37.733 6.542 1.00 16.86 ? 120 ALA A C 1 ATOM 859 O O . ALA A 1 120 ? 13.189 38.559 7.153 1.00 18.18 ? 120 ALA A O 1 ATOM 860 C CB . ALA A 1 120 ? 13.862 35.511 7.658 1.00 16.25 ? 120 ALA A CB 1 ATOM 861 N N . VAL A 1 121 ? 13.933 37.680 5.221 1.00 17.46 ? 121 VAL A N 1 ATOM 862 C CA . VAL A 1 121 ? 13.122 38.544 4.377 1.00 19.40 ? 121 VAL A CA 1 ATOM 863 C C . VAL A 1 121 ? 12.362 37.547 3.529 1.00 19.55 ? 121 VAL A C 1 ATOM 864 O O . VAL A 1 121 ? 12.957 36.764 2.789 1.00 20.94 ? 121 VAL A O 1 ATOM 865 C CB . VAL A 1 121 ? 13.965 39.442 3.469 1.00 21.60 ? 121 VAL A CB 1 ATOM 866 C CG1 . VAL A 1 121 ? 13.061 40.165 2.466 1.00 22.80 ? 121 VAL A CG1 1 ATOM 867 C CG2 . VAL A 1 121 ? 14.722 40.450 4.313 1.00 23.31 ? 121 VAL A CG2 1 ATOM 868 N N . VAL A 1 122 ? 11.047 37.563 3.668 1.00 19.35 ? 122 VAL A N 1 ATOM 869 C CA . VAL A 1 122 ? 10.194 36.644 2.942 1.00 20.85 ? 122 VAL A CA 1 ATOM 870 C C . VAL A 1 122 ? 9.392 37.398 1.891 1.00 24.37 ? 122 VAL A C 1 ATOM 871 O O . VAL A 1 122 ? 8.703 38.370 2.203 1.00 23.31 ? 122 VAL A O 1 ATOM 872 C CB . VAL A 1 122 ? 9.255 35.923 3.924 1.00 22.10 ? 122 VAL A CB 1 ATOM 873 C CG1 . VAL A 1 122 ? 8.439 34.874 3.189 1.00 23.33 ? 122 VAL A CG1 1 ATOM 874 C CG2 . VAL A 1 122 ? 10.077 35.283 5.035 1.00 19.98 ? 122 VAL A CG2 1 ATOM 875 N N . THR A 1 123 ? 9.505 36.948 0.645 1.00 26.26 ? 123 THR A N 1 ATOM 876 C CA . THR A 1 123 ? 8.820 37.568 -0.484 1.00 30.62 ? 123 THR A CA 1 ATOM 877 C C . THR A 1 123 ? 7.816 36.614 -1.129 1.00 33.18 ? 123 THR A C 1 ATOM 878 O O . THR A 1 123 ? 7.956 35.397 -1.024 1.00 26.98 ? 123 THR A O 1 ATOM 879 C CB . THR A 1 123 ? 9.836 37.989 -1.562 1.00 34.11 ? 123 THR A CB 1 ATOM 880 O OG1 . THR A 1 123 ? 10.817 38.852 -0.977 1.00 40.11 ? 123 THR A OG1 1 ATOM 881 C CG2 . THR A 1 123 ? 9.140 38.716 -2.702 1.00 38.91 ? 123 THR A CG2 1 ATOM 882 N N . ASN A 1 124 ? 6.808 37.178 -1.794 1.00 37.10 ? 124 ASN A N 1 ATOM 883 C CA . ASN A 1 124 ? 5.782 36.388 -2.472 1.00 43.40 ? 124 ASN A CA 1 ATOM 884 C C . ASN A 1 124 ? 6.161 36.122 -3.925 1.00 45.11 ? 124 ASN A C 1 ATOM 885 O O . ASN A 1 124 ? 6.141 37.090 -4.714 1.00 47.49 ? 124 ASN A O 1 ATOM 886 C CB . ASN A 1 124 ? 4.433 37.111 -2.436 1.00 47.21 ? 124 ASN A CB 1 ATOM 887 C CG . ASN A 1 124 ? 3.854 37.197 -1.040 1.00 51.87 ? 124 ASN A CG 1 ATOM 888 O OD1 . ASN A 1 124 ? 2.754 37.719 -0.843 1.00 57.04 ? 124 ASN A OD1 1 ATOM 889 N ND2 . ASN A 1 124 ? 4.590 36.686 -0.060 1.00 54.89 ? 124 ASN A ND2 1 ATOM 890 O OXT . ASN A 1 124 ? 6.471 34.956 -4.257 1.00 48.05 ? 124 ASN A OXT 1 ATOM 891 N N . CYS B 1 10 ? 26.403 30.239 39.913 1.00 45.01 ? 10 CYS B N 1 ATOM 892 C CA . CYS B 1 10 ? 25.568 30.345 38.679 1.00 46.23 ? 10 CYS B CA 1 ATOM 893 C C . CYS B 1 10 ? 26.490 30.507 37.467 1.00 42.36 ? 10 CYS B C 1 ATOM 894 O O . CYS B 1 10 ? 26.705 31.616 36.982 1.00 44.71 ? 10 CYS B O 1 ATOM 895 C CB . CYS B 1 10 ? 24.628 31.550 38.794 1.00 49.16 ? 10 CYS B CB 1 ATOM 896 S SG . CYS B 1 10 ? 23.189 31.515 37.689 1.00 58.43 ? 10 CYS B SG 1 ATOM 897 N N . PRO B 1 11 ? 27.054 29.395 36.969 1.00 38.39 ? 11 PRO B N 1 ATOM 898 C CA . PRO B 1 11 ? 27.962 29.396 35.816 1.00 35.75 ? 11 PRO B CA 1 ATOM 899 C C . PRO B 1 11 ? 27.302 29.732 34.481 1.00 31.91 ? 11 PRO B C 1 ATOM 900 O O . PRO B 1 11 ? 27.963 30.194 33.554 1.00 29.13 ? 11 PRO B O 1 ATOM 901 C CB . PRO B 1 11 ? 28.525 27.973 35.815 1.00 37.50 ? 11 PRO B CB 1 ATOM 902 C CG . PRO B 1 11 ? 28.363 27.527 37.240 1.00 39.44 ? 11 PRO B CG 1 ATOM 903 C CD . PRO B 1 11 ? 27.008 28.059 37.583 1.00 39.22 ? 11 PRO B CD 1 ATOM 904 N N . LEU B 1 12 ? 26.000 29.495 34.386 1.00 30.29 ? 12 LEU B N 1 ATOM 905 C CA . LEU B 1 12 ? 25.271 29.748 33.149 1.00 29.08 ? 12 LEU B CA 1 ATOM 906 C C . LEU B 1 12 ? 23.972 30.505 33.393 1.00 29.05 ? 12 LEU B C 1 ATOM 907 O O . LEU B 1 12 ? 23.149 30.090 34.205 1.00 28.94 ? 12 LEU B O 1 ATOM 908 C CB . LEU B 1 12 ? 24.971 28.418 32.457 1.00 28.13 ? 12 LEU B CB 1 ATOM 909 C CG . LEU B 1 12 ? 24.169 28.457 31.155 1.00 30.69 ? 12 LEU B CG 1 ATOM 910 C CD1 . LEU B 1 12 ? 24.962 29.197 30.086 1.00 28.99 ? 12 LEU B CD1 1 ATOM 911 C CD2 . LEU B 1 12 ? 23.868 27.036 30.706 1.00 31.49 ? 12 LEU B CD2 1 ATOM 912 N N . MET B 1 13 ? 23.788 31.613 32.676 1.00 27.14 ? 13 MET B N 1 ATOM 913 C CA . MET B 1 13 ? 22.587 32.428 32.820 1.00 27.37 ? 13 MET B CA 1 ATOM 914 C C . MET B 1 13 ? 22.056 32.795 31.433 1.00 23.97 ? 13 MET B C 1 ATOM 915 O O . MET B 1 13 ? 22.827 33.006 30.503 1.00 24.18 ? 13 MET B O 1 ATOM 916 C CB . MET B 1 13 ? 22.913 33.697 33.621 1.00 30.75 ? 13 MET B CB 1 ATOM 917 C CG . MET B 1 13 ? 21.698 34.460 34.157 1.00 38.98 ? 13 MET B CG 1 ATOM 918 S SD . MET B 1 13 ? 21.089 35.795 33.089 1.00 50.25 ? 13 MET B SD 1 ATOM 919 C CE . MET B 1 13 ? 22.073 37.189 33.692 1.00 44.27 ? 13 MET B CE 1 ATOM 920 N N . VAL B 1 14 ? 20.738 32.862 31.303 1.00 21.74 ? 14 VAL B N 1 ATOM 921 C CA . VAL B 1 14 ? 20.112 33.198 30.032 1.00 21.54 ? 14 VAL B CA 1 ATOM 922 C C . VAL B 1 14 ? 19.225 34.418 30.210 1.00 22.27 ? 14 VAL B C 1 ATOM 923 O O . VAL B 1 14 ? 18.495 34.520 31.197 1.00 23.18 ? 14 VAL B O 1 ATOM 924 C CB . VAL B 1 14 ? 19.267 32.007 29.501 1.00 20.57 ? 14 VAL B CB 1 ATOM 925 C CG1 . VAL B 1 14 ? 18.520 32.393 28.229 1.00 20.61 ? 14 VAL B CG1 1 ATOM 926 C CG2 . VAL B 1 14 ? 20.183 30.823 29.226 1.00 21.55 ? 14 VAL B CG2 1 ATOM 927 N N . LYS B 1 15 ? 19.307 35.360 29.274 1.00 19.82 ? 15 LYS B N 1 ATOM 928 C CA . LYS B 1 15 ? 18.480 36.559 29.346 1.00 20.06 ? 15 LYS B CA 1 ATOM 929 C C . LYS B 1 15 ? 17.849 36.775 27.984 1.00 19.26 ? 15 LYS B C 1 ATOM 930 O O . LYS B 1 15 ? 18.532 36.725 26.959 1.00 20.28 ? 15 LYS B O 1 ATOM 931 C CB . LYS B 1 15 ? 19.308 37.784 29.752 1.00 24.46 ? 15 LYS B CB 1 ATOM 932 C CG . LYS B 1 15 ? 18.450 38.952 30.251 1.00 30.43 ? 15 LYS B CG 1 ATOM 933 C CD . LYS B 1 15 ? 19.261 39.919 31.109 1.00 37.48 ? 15 LYS B CD 1 ATOM 934 C CE . LYS B 1 15 ? 18.368 40.928 31.822 1.00 39.41 ? 15 LYS B CE 1 ATOM 935 N NZ . LYS B 1 15 ? 17.514 41.669 30.866 1.00 42.09 ? 15 LYS B NZ 1 ATOM 936 N N . VAL B 1 16 ? 16.539 36.997 27.977 1.00 16.03 ? 16 VAL B N 1 ATOM 937 C CA . VAL B 1 16 ? 15.805 37.197 26.738 1.00 17.36 ? 16 VAL B CA 1 ATOM 938 C C . VAL B 1 16 ? 15.032 38.499 26.768 1.00 18.74 ? 16 VAL B C 1 ATOM 939 O O . VAL B 1 16 ? 14.291 38.774 27.722 1.00 18.64 ? 16 VAL B O 1 ATOM 940 C CB . VAL B 1 16 ? 14.817 36.037 26.499 1.00 15.49 ? 16 VAL B CB 1 ATOM 941 C CG1 . VAL B 1 16 ? 14.287 36.091 25.070 1.00 17.87 ? 16 VAL B CG1 1 ATOM 942 C CG2 . VAL B 1 16 ? 15.513 34.710 26.760 1.00 20.09 ? 16 VAL B CG2 1 ATOM 943 N N . LEU B 1 17 ? 15.209 39.296 25.715 1.00 17.33 ? 17 LEU B N 1 ATOM 944 C CA . LEU B 1 17 ? 14.541 40.584 25.601 1.00 17.55 ? 17 LEU B CA 1 ATOM 945 C C . LEU B 1 17 ? 13.658 40.605 24.366 1.00 16.89 ? 17 LEU B C 1 ATOM 946 O O . LEU B 1 17 ? 13.927 39.918 23.378 1.00 16.12 ? 17 LEU B O 1 ATOM 947 C CB . LEU B 1 17 ? 15.565 41.717 25.493 1.00 17.54 ? 17 LEU B CB 1 ATOM 948 C CG . LEU B 1 17 ? 16.527 41.997 26.653 1.00 22.25 ? 17 LEU B CG 1 ATOM 949 C CD1 . LEU B 1 17 ? 17.362 43.225 26.300 1.00 23.38 ? 17 LEU B CD1 1 ATOM 950 C CD2 . LEU B 1 17 ? 15.748 42.244 27.947 1.00 22.95 ? 17 LEU B CD2 1 ATOM 951 N N . ASP B 1 18 ? 12.615 41.418 24.439 1.00 17.92 ? 18 ASP B N 1 ATOM 952 C CA . ASP B 1 18 ? 11.644 41.593 23.372 1.00 17.30 ? 18 ASP B CA 1 ATOM 953 C C . ASP B 1 18 ? 11.941 42.938 22.696 1.00 18.36 ? 18 ASP B C 1 ATOM 954 O O . ASP B 1 18 ? 11.834 43.990 23.324 1.00 17.52 ? 18 ASP B O 1 ATOM 955 C CB . ASP B 1 18 ? 10.244 41.595 23.995 1.00 18.83 ? 18 ASP B CB 1 ATOM 956 C CG . ASP B 1 18 ? 9.137 41.696 22.971 1.00 20.63 ? 18 ASP B CG 1 ATOM 957 O OD1 . ASP B 1 18 ? 9.311 42.402 21.964 1.00 18.60 ? 18 ASP B OD1 1 ATOM 958 O OD2 . ASP B 1 18 ? 8.074 41.080 23.192 1.00 22.31 ? 18 ASP B OD2 1 ATOM 959 N N . ALA B 1 19 ? 12.329 42.898 21.422 1.00 16.33 ? 19 ALA B N 1 ATOM 960 C CA . ALA B 1 19 ? 12.651 44.109 20.673 1.00 17.30 ? 19 ALA B CA 1 ATOM 961 C C . ALA B 1 19 ? 11.423 44.819 20.121 1.00 17.76 ? 19 ALA B C 1 ATOM 962 O O . ALA B 1 19 ? 11.526 45.939 19.641 1.00 19.43 ? 19 ALA B O 1 ATOM 963 C CB . ALA B 1 19 ? 13.604 43.780 19.521 1.00 16.54 ? 19 ALA B CB 1 ATOM 964 N N . VAL B 1 20 ? 10.268 44.163 20.180 1.00 18.04 ? 20 VAL B N 1 ATOM 965 C CA . VAL B 1 20 ? 9.030 44.754 19.681 1.00 18.57 ? 20 VAL B CA 1 ATOM 966 C C . VAL B 1 20 ? 8.342 45.596 20.753 1.00 21.12 ? 20 VAL B C 1 ATOM 967 O O . VAL B 1 20 ? 7.808 46.666 20.465 1.00 20.69 ? 20 VAL B O 1 ATOM 968 C CB . VAL B 1 20 ? 8.030 43.664 19.215 1.00 19.48 ? 20 VAL B CB 1 ATOM 969 C CG1 . VAL B 1 20 ? 6.699 44.308 18.825 1.00 21.45 ? 20 VAL B CG1 1 ATOM 970 C CG2 . VAL B 1 20 ? 8.602 42.899 18.030 1.00 21.65 ? 20 VAL B CG2 1 ATOM 971 N N . ARG B 1 21 ? 8.363 45.109 21.987 1.00 20.91 ? 21 ARG B N 1 ATOM 972 C CA . ARG B 1 21 ? 7.699 45.804 23.081 1.00 22.83 ? 21 ARG B CA 1 ATOM 973 C C . ARG B 1 21 ? 8.649 46.542 24.012 1.00 21.09 ? 21 ARG B C 1 ATOM 974 O O . ARG B 1 21 ? 8.207 47.240 24.921 1.00 22.02 ? 21 ARG B O 1 ATOM 975 C CB . ARG B 1 21 ? 6.858 44.805 23.885 1.00 26.40 ? 21 ARG B CB 1 ATOM 976 C CG . ARG B 1 21 ? 5.818 44.071 23.045 1.00 33.57 ? 21 ARG B CG 1 ATOM 977 C CD . ARG B 1 21 ? 4.834 43.311 23.910 1.00 37.99 ? 21 ARG B CD 1 ATOM 978 N NE . ARG B 1 21 ? 5.404 42.152 24.551 1.00 43.06 ? 21 ARG B NE 1 ATOM 979 C CZ . ARG B 1 21 ? 4.950 41.545 25.642 1.00 48.50 ? 21 ARG B CZ 1 ATOM 980 N NH1 . ARG B 1 21 ? 5.606 40.484 26.069 1.00 50.48 ? 21 ARG B NH1 1 ATOM 981 N NH2 . ARG B 1 21 ? 3.890 41.981 26.317 1.00 50.57 ? 21 ARG B NH2 1 ATOM 982 N N . GLY B 1 22 ? 9.951 46.389 23.780 1.00 20.85 ? 22 GLY B N 1 ATOM 983 C CA . GLY B 1 22 ? 10.940 47.045 24.621 1.00 19.92 ? 22 GLY B CA 1 ATOM 984 C C . GLY B 1 22 ? 10.847 46.560 26.057 1.00 21.55 ? 22 GLY B C 1 ATOM 985 O O . GLY B 1 22 ? 10.883 47.347 27.006 1.00 20.70 ? 22 GLY B O 1 ATOM 986 N N . SER B 1 23 ? 10.740 45.247 26.217 1.00 21.70 ? 23 SER B N 1 ATOM 987 C CA . SER B 1 23 ? 10.614 44.665 27.543 1.00 21.98 ? 23 SER B CA 1 ATOM 988 C C . SER B 1 23 ? 11.267 43.300 27.627 1.00 20.91 ? 23 SER B C 1 ATOM 989 O O . SER B 1 23 ? 11.661 42.711 26.613 1.00 22.13 ? 23 SER B O 1 ATOM 990 C CB . SER B 1 23 ? 9.138 44.515 27.895 1.00 24.93 ? 23 SER B CB 1 ATOM 991 O OG . SER B 1 23 ? 8.548 43.534 27.065 1.00 30.25 ? 23 SER B OG 1 ATOM 992 N N . PRO B 1 24 ? 11.404 42.773 28.848 1.00 20.46 ? 24 PRO B N 1 ATOM 993 C CA . PRO B 1 24 ? 12.016 41.453 28.992 1.00 19.70 ? 24 PRO B CA 1 ATOM 994 C C . PRO B 1 24 ? 11.040 40.458 28.372 1.00 19.99 ? 24 PRO B C 1 ATOM 995 O O . PRO B 1 24 ? 9.832 40.717 28.339 1.00 20.33 ? 24 PRO B O 1 ATOM 996 C CB . PRO B 1 24 ? 12.111 41.276 30.513 1.00 21.56 ? 24 PRO B CB 1 ATOM 997 C CG . PRO B 1 24 ? 12.146 42.687 31.037 1.00 22.68 ? 24 PRO B CG 1 ATOM 998 C CD . PRO B 1 24 ? 11.153 43.395 30.162 1.00 19.21 ? 24 PRO B CD 1 ATOM 999 N N . ALA B 1 25 ? 11.550 39.346 27.858 1.00 18.61 ? 25 ALA B N 1 ATOM 1000 C CA . ALA B 1 25 ? 10.682 38.323 27.275 1.00 19.70 ? 25 ALA B CA 1 ATOM 1001 C C . ALA B 1 25 ? 10.381 37.375 28.427 1.00 18.87 ? 25 ALA B C 1 ATOM 1002 O O . ALA B 1 25 ? 11.212 36.565 28.814 1.00 18.63 ? 25 ALA B O 1 ATOM 1003 C CB . ALA B 1 25 ? 11.392 37.588 26.142 1.00 17.06 ? 25 ALA B CB 1 ATOM 1004 N N . ILE B 1 26 ? 9.178 37.497 28.970 1.00 20.05 ? 26 ILE B N 1 ATOM 1005 C CA . ILE B 1 26 ? 8.749 36.710 30.119 1.00 19.10 ? 26 ILE B CA 1 ATOM 1006 C C . ILE B 1 26 ? 8.100 35.371 29.782 1.00 18.68 ? 26 ILE B C 1 ATOM 1007 O O . ILE B 1 26 ? 7.438 35.220 28.755 1.00 18.73 ? 26 ILE B O 1 ATOM 1008 C CB . ILE B 1 26 ? 7.773 37.552 30.968 1.00 22.11 ? 26 ILE B CB 1 ATOM 1009 C CG1 . ILE B 1 26 ? 8.422 38.903 31.289 1.00 22.16 ? 26 ILE B CG1 1 ATOM 1010 C CG2 . ILE B 1 26 ? 7.413 36.822 32.247 1.00 24.57 ? 26 ILE B CG2 1 ATOM 1011 C CD1 . ILE B 1 26 ? 7.477 39.913 31.900 1.00 27.15 ? 26 ILE B CD1 1 ATOM 1012 N N . ASN B 1 27 ? 8.306 34.401 30.664 1.00 21.04 ? 27 ASN B N 1 ATOM 1013 C CA . ASN B 1 27 ? 7.739 33.064 30.507 1.00 24.56 ? 27 ASN B CA 1 ATOM 1014 C C . ASN B 1 27 ? 8.160 32.345 29.239 1.00 24.12 ? 27 ASN B C 1 ATOM 1015 O O . ASN B 1 27 ? 7.382 31.579 28.662 1.00 24.52 ? 27 ASN B O 1 ATOM 1016 C CB . ASN B 1 27 ? 6.213 33.126 30.563 1.00 30.95 ? 27 ASN B CB 1 ATOM 1017 C CG . ASN B 1 27 ? 5.703 33.589 31.909 1.00 37.25 ? 27 ASN B CG 1 ATOM 1018 O OD1 . ASN B 1 27 ? 6.095 33.057 32.946 1.00 43.18 ? 27 ASN B OD1 1 ATOM 1019 N ND2 . ASN B 1 27 ? 4.823 34.583 31.903 1.00 40.63 ? 27 ASN B ND2 1 ATOM 1020 N N . VAL B 1 28 ? 9.387 32.590 28.803 1.00 21.92 ? 28 VAL B N 1 ATOM 1021 C CA . VAL B 1 28 ? 9.899 31.939 27.605 1.00 21.78 ? 28 VAL B CA 1 ATOM 1022 C C . VAL B 1 28 ? 10.553 30.637 28.036 1.00 19.01 ? 28 VAL B C 1 ATOM 1023 O O . VAL B 1 28 ? 11.386 30.623 28.937 1.00 19.14 ? 28 VAL B O 1 ATOM 1024 C CB . VAL B 1 28 ? 10.962 32.807 26.886 1.00 21.97 ? 28 VAL B CB 1 ATOM 1025 C CG1 . VAL B 1 28 ? 11.535 32.040 25.704 1.00 23.31 ? 28 VAL B CG1 1 ATOM 1026 C CG2 . VAL B 1 28 ? 10.346 34.113 26.417 1.00 25.29 ? 28 VAL B CG2 1 ATOM 1027 N N . ALA B 1 29 ? 10.170 29.542 27.396 1.00 18.35 ? 29 ALA B N 1 ATOM 1028 C CA . ALA B 1 29 ? 10.738 28.248 27.720 1.00 19.17 ? 29 ALA B CA 1 ATOM 1029 C C . ALA B 1 29 ? 12.148 28.137 27.156 1.00 17.88 ? 29 ALA B C 1 ATOM 1030 O O . ALA B 1 29 ? 12.402 28.503 26.004 1.00 18.80 ? 29 ALA B O 1 ATOM 1031 C CB . ALA B 1 29 ? 9.857 27.135 27.152 1.00 19.23 ? 29 ALA B CB 1 ATOM 1032 N N . VAL B 1 30 ? 13.058 27.641 27.982 1.00 17.23 ? 30 VAL B N 1 ATOM 1033 C CA . VAL B 1 30 ? 14.448 27.448 27.593 1.00 17.00 ? 30 VAL B CA 1 ATOM 1034 C C . VAL B 1 30 ? 14.869 26.029 27.952 1.00 18.91 ? 30 VAL B C 1 ATOM 1035 O O . VAL B 1 30 ? 14.667 25.579 29.087 1.00 19.91 ? 30 VAL B O 1 ATOM 1036 C CB . VAL B 1 30 ? 15.390 28.423 28.343 1.00 16.80 ? 30 VAL B CB 1 ATOM 1037 C CG1 . VAL B 1 30 ? 16.840 28.096 28.029 1.00 18.89 ? 30 VAL B CG1 1 ATOM 1038 C CG2 . VAL B 1 30 ? 15.074 29.865 27.952 1.00 16.01 ? 30 VAL B CG2 1 ATOM 1039 N N . HIS B 1 31 ? 15.439 25.323 26.984 1.00 18.82 ? 31 HIS B N 1 ATOM 1040 C CA . HIS B 1 31 ? 15.919 23.968 27.209 1.00 20.09 ? 31 HIS B CA 1 ATOM 1041 C C . HIS B 1 31 ? 17.405 23.933 26.901 1.00 19.52 ? 31 HIS B C 1 ATOM 1042 O O . HIS B 1 31 ? 17.849 24.464 25.885 1.00 22.11 ? 31 HIS B O 1 ATOM 1043 C CB . HIS B 1 31 ? 15.194 22.971 26.309 1.00 20.13 ? 31 HIS B CB 1 ATOM 1044 C CG . HIS B 1 31 ? 13.778 22.709 26.713 1.00 23.20 ? 31 HIS B CG 1 ATOM 1045 N ND1 . HIS B 1 31 ? 12.758 23.602 26.470 1.00 27.09 ? 31 HIS B ND1 1 ATOM 1046 C CD2 . HIS B 1 31 ? 13.215 21.658 27.354 1.00 24.78 ? 31 HIS B CD2 1 ATOM 1047 C CE1 . HIS B 1 31 ? 11.626 23.113 26.943 1.00 25.92 ? 31 HIS B CE1 1 ATOM 1048 N NE2 . HIS B 1 31 ? 11.875 21.935 27.485 1.00 27.63 ? 31 HIS B NE2 1 ATOM 1049 N N . VAL B 1 32 ? 18.174 23.319 27.785 1.00 18.99 ? 32 VAL B N 1 ATOM 1050 C CA . VAL B 1 32 ? 19.612 23.208 27.593 1.00 18.32 ? 32 VAL B CA 1 ATOM 1051 C C . VAL B 1 32 ? 19.957 21.740 27.441 1.00 21.94 ? 32 VAL B C 1 ATOM 1052 O O . VAL B 1 32 ? 19.404 20.881 28.147 1.00 23.14 ? 32 VAL B O 1 ATOM 1053 C CB . VAL B 1 32 ? 20.388 23.783 28.792 1.00 18.16 ? 32 VAL B CB 1 ATOM 1054 C CG1 . VAL B 1 32 ? 21.882 23.695 28.532 1.00 16.86 ? 32 VAL B CG1 1 ATOM 1055 C CG2 . VAL B 1 32 ? 19.975 25.220 29.032 1.00 18.67 ? 32 VAL B CG2 1 ATOM 1056 N N . PHE B 1 33 ? 20.855 21.456 26.506 1.00 20.99 ? 33 PHE B N 1 ATOM 1057 C CA . PHE B 1 33 ? 21.285 20.093 26.235 1.00 21.85 ? 33 PHE B CA 1 ATOM 1058 C C . PHE B 1 33 ? 22.800 20.041 26.202 1.00 24.70 ? 33 PHE B C 1 ATOM 1059 O O . PHE B 1 33 ? 23.468 21.047 25.943 1.00 22.80 ? 33 PHE B O 1 ATOM 1060 C CB . PHE B 1 33 ? 20.750 19.604 24.879 1.00 23.29 ? 33 PHE B CB 1 ATOM 1061 C CG . PHE B 1 33 ? 19.264 19.767 24.708 1.00 23.50 ? 33 PHE B CG 1 ATOM 1062 C CD1 . PHE B 1 33 ? 18.727 20.985 24.298 1.00 23.60 ? 33 PHE B CD1 1 ATOM 1063 C CD2 . PHE B 1 33 ? 18.401 18.703 24.956 1.00 25.80 ? 33 PHE B CD2 1 ATOM 1064 C CE1 . PHE B 1 33 ? 17.355 21.145 24.134 1.00 22.66 ? 33 PHE B CE1 1 ATOM 1065 C CE2 . PHE B 1 33 ? 17.019 18.850 24.797 1.00 25.38 ? 33 PHE B CE2 1 ATOM 1066 C CZ . PHE B 1 33 ? 16.496 20.076 24.384 1.00 27.33 ? 33 PHE B CZ 1 ATOM 1067 N N . ARG B 1 34 ? 23.339 18.860 26.476 1.00 25.10 ? 34 ARG B N 1 ATOM 1068 C CA . ARG B 1 34 ? 24.774 18.651 26.437 1.00 26.18 ? 34 ARG B CA 1 ATOM 1069 C C . ARG B 1 34 ? 25.019 17.533 25.433 1.00 27.32 ? 34 ARG B C 1 ATOM 1070 O O . ARG B 1 34 ? 24.295 16.535 25.421 1.00 28.88 ? 34 ARG B O 1 ATOM 1071 C CB . ARG B 1 34 ? 25.299 18.249 27.817 1.00 26.52 ? 34 ARG B CB 1 ATOM 1072 C CG . ARG B 1 34 ? 26.793 18.007 27.837 1.00 30.06 ? 34 ARG B CG 1 ATOM 1073 C CD . ARG B 1 34 ? 27.322 17.796 29.249 1.00 34.47 ? 34 ARG B CD 1 ATOM 1074 N NE . ARG B 1 34 ? 28.770 17.606 29.231 1.00 39.00 ? 34 ARG B NE 1 ATOM 1075 C CZ . ARG B 1 34 ? 29.370 16.508 28.782 1.00 41.01 ? 34 ARG B CZ 1 ATOM 1076 N NH1 . ARG B 1 34 ? 28.646 15.493 28.321 1.00 41.63 ? 34 ARG B NH1 1 ATOM 1077 N NH2 . ARG B 1 34 ? 30.694 16.431 28.777 1.00 40.24 ? 34 ARG B NH2 1 ATOM 1078 N N . LYS B 1 35 ? 26.026 17.700 24.584 1.00 27.93 ? 35 LYS B N 1 ATOM 1079 C CA . LYS B 1 35 ? 26.320 16.687 23.582 1.00 32.00 ? 35 LYS B CA 1 ATOM 1080 C C . LYS B 1 35 ? 26.925 15.475 24.279 1.00 33.03 ? 35 LYS B C 1 ATOM 1081 O O . LYS B 1 35 ? 27.920 15.591 24.993 1.00 30.30 ? 35 LYS B O 1 ATOM 1082 C CB . LYS B 1 35 ? 27.283 17.242 22.529 1.00 33.17 ? 35 LYS B CB 1 ATOM 1083 C CG . LYS B 1 35 ? 27.107 16.617 21.150 1.00 38.31 ? 35 LYS B CG 1 ATOM 1084 C CD . LYS B 1 35 ? 27.937 17.340 20.100 1.00 43.50 ? 35 LYS B CD 1 ATOM 1085 C CE . LYS B 1 35 ? 27.615 16.835 18.701 1.00 47.12 ? 35 LYS B CE 1 ATOM 1086 N NZ . LYS B 1 35 ? 28.406 17.547 17.658 1.00 50.08 ? 35 LYS B NZ 1 ATOM 1087 N N . ALA B 1 36 ? 26.301 14.317 24.081 1.00 36.27 ? 36 ALA B N 1 ATOM 1088 C CA . ALA B 1 36 ? 26.753 13.077 24.699 1.00 40.58 ? 36 ALA B CA 1 ATOM 1089 C C . ALA B 1 36 ? 27.842 12.403 23.878 1.00 43.59 ? 36 ALA B C 1 ATOM 1090 O O . ALA B 1 36 ? 28.115 12.799 22.745 1.00 43.61 ? 36 ALA B O 1 ATOM 1091 C CB . ALA B 1 36 ? 25.576 12.131 24.883 1.00 41.56 ? 36 ALA B CB 1 ATOM 1092 N N . ALA B 1 37 ? 28.454 11.377 24.460 1.00 47.72 ? 37 ALA B N 1 ATOM 1093 C CA . ALA B 1 37 ? 29.527 10.639 23.807 1.00 51.64 ? 37 ALA B CA 1 ATOM 1094 C C . ALA B 1 37 ? 29.145 10.148 22.412 1.00 53.62 ? 37 ALA B C 1 ATOM 1095 O O . ALA B 1 37 ? 29.970 10.152 21.496 1.00 54.23 ? 37 ALA B O 1 ATOM 1096 C CB . ALA B 1 37 ? 29.944 9.460 24.680 1.00 52.53 ? 37 ALA B CB 1 ATOM 1097 N N . ASP B 1 38 ? 27.893 9.730 22.252 1.00 55.94 ? 38 ASP B N 1 ATOM 1098 C CA . ASP B 1 38 ? 27.420 9.225 20.967 1.00 57.58 ? 38 ASP B CA 1 ATOM 1099 C C . ASP B 1 38 ? 26.907 10.333 20.051 1.00 57.70 ? 38 ASP B C 1 ATOM 1100 O O . ASP B 1 38 ? 26.094 10.087 19.159 1.00 57.22 ? 38 ASP B O 1 ATOM 1101 C CB . ASP B 1 38 ? 26.318 8.187 21.189 1.00 60.04 ? 38 ASP B CB 1 ATOM 1102 C CG . ASP B 1 38 ? 25.054 8.793 21.759 1.00 62.16 ? 38 ASP B CG 1 ATOM 1103 O OD1 . ASP B 1 38 ? 25.146 9.532 22.761 1.00 63.27 ? 38 ASP B OD1 1 ATOM 1104 O OD2 . ASP B 1 38 ? 23.968 8.524 21.205 1.00 63.98 ? 38 ASP B OD2 1 ATOM 1105 N N . ASP B 1 39 ? 27.389 11.552 20.277 1.00 57.79 ? 39 ASP B N 1 ATOM 1106 C CA . ASP B 1 39 ? 26.998 12.706 19.472 1.00 56.47 ? 39 ASP B CA 1 ATOM 1107 C C . ASP B 1 39 ? 25.501 12.995 19.518 1.00 53.91 ? 39 ASP B C 1 ATOM 1108 O O . ASP B 1 39 ? 24.932 13.514 18.559 1.00 54.16 ? 39 ASP B O 1 ATOM 1109 C CB . ASP B 1 39 ? 27.433 12.501 18.018 1.00 59.81 ? 39 ASP B CB 1 ATOM 1110 C CG . ASP B 1 39 ? 28.937 12.379 17.873 1.00 62.68 ? 39 ASP B CG 1 ATOM 1111 O OD1 . ASP B 1 39 ? 29.651 13.330 18.261 1.00 63.77 ? 39 ASP B OD1 1 ATOM 1112 O OD2 . ASP B 1 39 ? 29.405 11.332 17.373 1.00 64.39 ? 39 ASP B OD2 1 ATOM 1113 N N . THR B 1 40 ? 24.866 12.660 20.635 1.00 49.94 ? 40 THR B N 1 ATOM 1114 C CA . THR B 1 40 ? 23.435 12.894 20.802 1.00 46.60 ? 40 THR B CA 1 ATOM 1115 C C . THR B 1 40 ? 23.212 14.005 21.826 1.00 42.03 ? 40 THR B C 1 ATOM 1116 O O . THR B 1 40 ? 24.026 14.195 22.728 1.00 40.85 ? 40 THR B O 1 ATOM 1117 C CB . THR B 1 40 ? 22.716 11.615 21.288 1.00 47.08 ? 40 THR B CB 1 ATOM 1118 O OG1 . THR B 1 40 ? 22.781 10.614 20.265 1.00 51.93 ? 40 THR B OG1 1 ATOM 1119 C CG2 . THR B 1 40 ? 21.258 11.901 21.610 1.00 48.36 ? 40 THR B CG2 1 ATOM 1120 N N . TRP B 1 41 ? 22.112 14.738 21.683 1.00 36.67 ? 41 TRP B N 1 ATOM 1121 C CA . TRP B 1 41 ? 21.799 15.815 22.616 1.00 34.30 ? 41 TRP B CA 1 ATOM 1122 C C . TRP B 1 41 ? 20.977 15.304 23.790 1.00 33.00 ? 41 TRP B C 1 ATOM 1123 O O . TRP B 1 41 ? 19.807 14.956 23.632 1.00 35.16 ? 41 TRP B O 1 ATOM 1124 C CB . TRP B 1 41 ? 21.011 16.924 21.921 1.00 32.71 ? 41 TRP B CB 1 ATOM 1125 C CG . TRP B 1 41 ? 21.800 17.717 20.938 1.00 31.74 ? 41 TRP B CG 1 ATOM 1126 C CD1 . TRP B 1 41 ? 21.608 17.771 19.589 1.00 32.34 ? 41 TRP B CD1 1 ATOM 1127 C CD2 . TRP B 1 41 ? 22.892 18.597 21.227 1.00 30.32 ? 41 TRP B CD2 1 ATOM 1128 N NE1 . TRP B 1 41 ? 22.510 18.634 19.017 1.00 32.46 ? 41 TRP B NE1 1 ATOM 1129 C CE2 . TRP B 1 41 ? 23.312 19.154 19.999 1.00 31.07 ? 41 TRP B CE2 1 ATOM 1130 C CE3 . TRP B 1 41 ? 23.556 18.971 22.405 1.00 27.73 ? 41 TRP B CE3 1 ATOM 1131 C CZ2 . TRP B 1 41 ? 24.370 20.068 19.914 1.00 28.46 ? 41 TRP B CZ2 1 ATOM 1132 C CZ3 . TRP B 1 41 ? 24.605 19.878 22.322 1.00 26.97 ? 41 TRP B CZ3 1 ATOM 1133 C CH2 . TRP B 1 41 ? 25.002 20.417 21.083 1.00 27.69 ? 41 TRP B CH2 1 ATOM 1134 N N . GLU B 1 42 ? 21.577 15.261 24.972 1.00 32.20 ? 42 GLU B N 1 ATOM 1135 C CA . GLU B 1 42 ? 20.841 14.802 26.136 1.00 32.66 ? 42 GLU B CA 1 ATOM 1136 C C . GLU B 1 42 ? 20.390 15.983 26.986 1.00 31.26 ? 42 GLU B C 1 ATOM 1137 O O . GLU B 1 42 ? 21.139 16.941 27.197 1.00 29.19 ? 42 GLU B O 1 ATOM 1138 C CB . GLU B 1 42 ? 21.687 13.841 26.976 1.00 36.91 ? 42 GLU B CB 1 ATOM 1139 C CG . GLU B 1 42 ? 22.952 14.427 27.564 1.00 45.27 ? 42 GLU B CG 1 ATOM 1140 C CD . GLU B 1 42 ? 23.653 13.451 28.496 1.00 50.84 ? 42 GLU B CD 1 ATOM 1141 O OE1 . GLU B 1 42 ? 24.013 12.344 28.040 1.00 52.36 ? 42 GLU B OE1 1 ATOM 1142 O OE2 . GLU B 1 42 ? 23.840 13.789 29.686 1.00 52.69 ? 42 GLU B OE2 1 ATOM 1143 N N . PRO B 1 43 ? 19.140 15.941 27.465 1.00 29.00 ? 43 PRO B N 1 ATOM 1144 C CA . PRO B 1 43 ? 18.597 17.016 28.296 1.00 27.03 ? 43 PRO B CA 1 ATOM 1145 C C . PRO B 1 43 ? 19.563 17.318 29.432 1.00 27.11 ? 43 PRO B C 1 ATOM 1146 O O . PRO B 1 43 ? 20.110 16.406 30.055 1.00 26.82 ? 43 PRO B O 1 ATOM 1147 C CB . PRO B 1 43 ? 17.280 16.428 28.788 1.00 28.69 ? 43 PRO B CB 1 ATOM 1148 C CG . PRO B 1 43 ? 16.849 15.588 27.619 1.00 28.76 ? 43 PRO B CG 1 ATOM 1149 C CD . PRO B 1 43 ? 18.132 14.887 27.248 1.00 29.44 ? 43 PRO B CD 1 ATOM 1150 N N . PHE B 1 44 ? 19.777 18.602 29.694 1.00 24.66 ? 44 PHE B N 1 ATOM 1151 C CA . PHE B 1 44 ? 20.694 19.014 30.742 1.00 24.58 ? 44 PHE B CA 1 ATOM 1152 C C . PHE B 1 44 ? 19.966 19.839 31.791 1.00 24.54 ? 44 PHE B C 1 ATOM 1153 O O . PHE B 1 44 ? 20.099 19.600 32.988 1.00 23.56 ? 44 PHE B O 1 ATOM 1154 C CB . PHE B 1 44 ? 21.837 19.829 30.131 1.00 23.02 ? 44 PHE B CB 1 ATOM 1155 C CG . PHE B 1 44 ? 22.891 20.227 31.115 1.00 25.59 ? 44 PHE B CG 1 ATOM 1156 C CD1 . PHE B 1 44 ? 23.756 19.277 31.651 1.00 24.32 ? 44 PHE B CD1 1 ATOM 1157 C CD2 . PHE B 1 44 ? 23.020 21.553 31.511 1.00 21.92 ? 44 PHE B CD2 1 ATOM 1158 C CE1 . PHE B 1 44 ? 24.736 19.647 32.567 1.00 23.78 ? 44 PHE B CE1 1 ATOM 1159 C CE2 . PHE B 1 44 ? 23.994 21.934 32.427 1.00 25.41 ? 44 PHE B CE2 1 ATOM 1160 C CZ . PHE B 1 44 ? 24.854 20.979 32.955 1.00 22.26 ? 44 PHE B CZ 1 ATOM 1161 N N . ALA B 1 45 ? 19.196 20.816 31.331 1.00 23.64 ? 45 ALA B N 1 ATOM 1162 C CA . ALA B 1 45 ? 18.443 21.684 32.220 1.00 22.38 ? 45 ALA B CA 1 ATOM 1163 C C . ALA B 1 45 ? 17.386 22.426 31.419 1.00 20.08 ? 45 ALA B C 1 ATOM 1164 O O . ALA B 1 45 ? 17.458 22.494 30.192 1.00 21.66 ? 45 ALA B O 1 ATOM 1165 C CB . ALA B 1 45 ? 19.378 22.678 32.896 1.00 20.37 ? 45 ALA B CB 1 ATOM 1166 N N . SER B 1 46 ? 16.394 22.971 32.110 1.00 20.68 ? 46 SER B N 1 ATOM 1167 C CA . SER B 1 46 ? 15.337 23.714 31.441 1.00 19.51 ? 46 SER B CA 1 ATOM 1168 C C . SER B 1 46 ? 14.632 24.623 32.425 1.00 21.97 ? 46 SER B C 1 ATOM 1169 O O . SER B 1 46 ? 14.749 24.465 33.641 1.00 23.46 ? 46 SER B O 1 ATOM 1170 C CB . SER B 1 46 ? 14.320 22.765 30.799 1.00 18.10 ? 46 SER B CB 1 ATOM 1171 O OG . SER B 1 46 ? 13.672 21.971 31.777 1.00 19.54 ? 46 SER B OG 1 ATOM 1172 N N . GLY B 1 47 ? 13.894 25.580 31.889 1.00 20.35 ? 47 GLY B N 1 ATOM 1173 C CA . GLY B 1 47 ? 13.177 26.507 32.734 1.00 20.99 ? 47 GLY B CA 1 ATOM 1174 C C . GLY B 1 47 ? 12.483 27.545 31.884 1.00 22.15 ? 47 GLY B C 1 ATOM 1175 O O . GLY B 1 47 ? 12.493 27.465 30.653 1.00 23.20 ? 47 GLY B O 1 ATOM 1176 N N . LYS B 1 48 ? 11.867 28.510 32.548 1.00 20.53 ? 48 LYS B N 1 ATOM 1177 C CA . LYS B 1 48 ? 11.172 29.596 31.874 1.00 23.99 ? 48 LYS B CA 1 ATOM 1178 C C . LYS B 1 48 ? 11.716 30.901 32.414 1.00 22.72 ? 48 LYS B C 1 ATOM 1179 O O . LYS B 1 48 ? 11.991 31.008 33.605 1.00 22.68 ? 48 LYS B O 1 ATOM 1180 C CB . LYS B 1 48 ? 9.671 29.514 32.136 1.00 26.32 ? 48 LYS B CB 1 ATOM 1181 C CG . LYS B 1 48 ? 8.957 28.517 31.253 1.00 32.54 ? 48 LYS B CG 1 ATOM 1182 C CD . LYS B 1 48 ? 7.468 28.512 31.530 1.00 38.22 ? 48 LYS B CD 1 ATOM 1183 C CE . LYS B 1 48 ? 6.712 27.797 30.425 1.00 39.65 ? 48 LYS B CE 1 ATOM 1184 N NZ . LYS B 1 48 ? 6.798 28.543 29.140 1.00 43.30 ? 48 LYS B NZ 1 ATOM 1185 N N . THR B 1 49 ? 11.888 31.885 31.538 1.00 20.97 ? 49 THR B N 1 ATOM 1186 C CA . THR B 1 49 ? 12.407 33.182 31.955 1.00 20.86 ? 49 THR B CA 1 ATOM 1187 C C . THR B 1 49 ? 11.459 33.844 32.950 1.00 21.20 ? 49 THR B C 1 ATOM 1188 O O . THR B 1 49 ? 10.238 33.682 32.875 1.00 20.10 ? 49 THR B O 1 ATOM 1189 C CB . THR B 1 49 ? 12.600 34.112 30.748 1.00 17.98 ? 49 THR B CB 1 ATOM 1190 O OG1 . THR B 1 49 ? 11.357 34.256 30.053 1.00 18.22 ? 49 THR B OG1 1 ATOM 1191 C CG2 . THR B 1 49 ? 13.647 33.534 29.803 1.00 17.13 ? 49 THR B CG2 1 ATOM 1192 N N . SER B 1 50 ? 12.041 34.587 33.882 1.00 24.27 ? 50 SER B N 1 ATOM 1193 C CA . SER B 1 50 ? 11.285 35.273 34.921 1.00 25.49 ? 50 SER B CA 1 ATOM 1194 C C . SER B 1 50 ? 10.717 36.589 34.410 1.00 26.69 ? 50 SER B C 1 ATOM 1195 O O . SER B 1 50 ? 10.791 36.888 33.219 1.00 24.22 ? 50 SER B O 1 ATOM 1196 C CB . SER B 1 50 ? 12.197 35.557 36.106 1.00 25.19 ? 50 SER B CB 1 ATOM 1197 O OG . SER B 1 50 ? 13.176 36.517 35.739 1.00 27.04 ? 50 SER B OG 1 ATOM 1198 N N . GLU B 1 51 ? 10.164 37.375 35.331 1.00 27.60 ? 51 GLU B N 1 ATOM 1199 C CA . GLU B 1 51 ? 9.578 38.672 35.004 1.00 29.83 ? 51 GLU B CA 1 ATOM 1200 C C . GLU B 1 51 ? 10.622 39.625 34.428 1.00 26.98 ? 51 GLU B C 1 ATOM 1201 O O . GLU B 1 51 ? 10.283 40.566 33.715 1.00 27.96 ? 51 GLU B O 1 ATOM 1202 C CB . GLU B 1 51 ? 8.966 39.313 36.255 1.00 34.78 ? 51 GLU B CB 1 ATOM 1203 C CG . GLU B 1 51 ? 7.835 38.528 36.895 1.00 46.08 ? 51 GLU B CG 1 ATOM 1204 C CD . GLU B 1 51 ? 6.588 38.476 36.034 1.00 51.87 ? 51 GLU B CD 1 ATOM 1205 O OE1 . GLU B 1 51 ? 6.618 37.812 34.977 1.00 56.64 ? 51 GLU B OE1 1 ATOM 1206 O OE2 . GLU B 1 51 ? 5.576 39.105 36.414 1.00 56.83 ? 51 GLU B OE2 1 ATOM 1207 N N . SER B 1 52 ? 11.886 39.383 34.749 1.00 25.32 ? 52 SER B N 1 ATOM 1208 C CA . SER B 1 52 ? 12.968 40.233 34.265 1.00 25.71 ? 52 SER B CA 1 ATOM 1209 C C . SER B 1 52 ? 13.607 39.662 33.000 1.00 23.74 ? 52 SER B C 1 ATOM 1210 O O . SER B 1 52 ? 14.639 40.149 32.541 1.00 24.27 ? 52 SER B O 1 ATOM 1211 C CB . SER B 1 52 ? 14.030 40.391 35.348 1.00 26.61 ? 52 SER B CB 1 ATOM 1212 O OG . SER B 1 52 ? 14.682 39.158 35.594 1.00 32.88 ? 52 SER B OG 1 ATOM 1213 N N . GLY B 1 53 ? 12.986 38.623 32.452 1.00 22.94 ? 53 GLY B N 1 ATOM 1214 C CA . GLY B 1 53 ? 13.483 37.996 31.243 1.00 22.04 ? 53 GLY B CA 1 ATOM 1215 C C . GLY B 1 53 ? 14.713 37.143 31.464 1.00 23.08 ? 53 GLY B C 1 ATOM 1216 O O . GLY B 1 53 ? 15.350 36.718 30.505 1.00 22.79 ? 53 GLY B O 1 ATOM 1217 N N . GLU B 1 54 ? 15.042 36.877 32.726 1.00 23.98 ? 54 GLU B N 1 ATOM 1218 C CA . GLU B 1 54 ? 16.223 36.090 33.046 1.00 24.41 ? 54 GLU B CA 1 ATOM 1219 C C . GLU B 1 54 ? 15.902 34.687 33.539 1.00 25.18 ? 54 GLU B C 1 ATOM 1220 O O . GLU B 1 54 ? 14.799 34.406 34.026 1.00 26.61 ? 54 GLU B O 1 ATOM 1221 C CB . GLU B 1 54 ? 17.070 36.808 34.106 1.00 28.91 ? 54 GLU B CB 1 ATOM 1222 C CG . GLU B 1 54 ? 17.407 38.258 33.780 1.00 35.39 ? 54 GLU B CG 1 ATOM 1223 C CD . GLU B 1 54 ? 18.346 38.885 34.798 1.00 40.14 ? 54 GLU B CD 1 ATOM 1224 O OE1 . GLU B 1 54 ? 18.048 38.808 36.006 1.00 42.39 ? 54 GLU B OE1 1 ATOM 1225 O OE2 . GLU B 1 54 ? 19.379 39.460 34.391 1.00 44.41 ? 54 GLU B OE2 1 ATOM 1226 N N . LEU B 1 55 ? 16.882 33.807 33.402 1.00 22.64 ? 55 LEU B N 1 ATOM 1227 C CA . LEU B 1 55 ? 16.748 32.428 33.847 1.00 25.68 ? 55 LEU B CA 1 ATOM 1228 C C . LEU B 1 55 ? 18.041 32.050 34.551 1.00 26.65 ? 55 LEU B C 1 ATOM 1229 O O . LEU B 1 55 ? 19.097 31.948 33.924 1.00 25.77 ? 55 LEU B O 1 ATOM 1230 C CB . LEU B 1 55 ? 16.488 31.502 32.655 1.00 25.47 ? 55 LEU B CB 1 ATOM 1231 C CG . LEU B 1 55 ? 16.351 30.003 32.931 1.00 24.80 ? 55 LEU B CG 1 ATOM 1232 C CD1 . LEU B 1 55 ? 15.316 29.747 34.015 1.00 26.09 ? 55 LEU B CD1 1 ATOM 1233 C CD2 . LEU B 1 55 ? 15.961 29.305 31.641 1.00 25.91 ? 55 LEU B CD2 1 ATOM 1234 N N . HIS B 1 56 ? 17.952 31.879 35.867 1.00 28.40 ? 56 HIS B N 1 ATOM 1235 C CA . HIS B 1 56 ? 19.105 31.526 36.685 1.00 31.80 ? 56 HIS B CA 1 ATOM 1236 C C . HIS B 1 56 ? 18.940 30.126 37.258 1.00 31.46 ? 56 HIS B C 1 ATOM 1237 O O . HIS B 1 56 ? 17.887 29.500 37.122 1.00 33.33 ? 56 HIS B O 1 ATOM 1238 C CB . HIS B 1 56 ? 19.264 32.496 37.865 1.00 34.02 ? 56 HIS B CB 1 ATOM 1239 C CG . HIS B 1 56 ? 19.325 33.939 37.475 1.00 38.21 ? 56 HIS B CG 1 ATOM 1240 N ND1 . HIS B 1 56 ? 18.211 34.658 37.102 1.00 40.06 ? 56 HIS B ND1 1 ATOM 1241 C CD2 . HIS B 1 56 ? 20.368 34.802 37.414 1.00 38.51 ? 56 HIS B CD2 1 ATOM 1242 C CE1 . HIS B 1 56 ? 18.564 35.901 36.829 1.00 39.80 ? 56 HIS B CE1 1 ATOM 1243 N NE2 . HIS B 1 56 ? 19.867 36.015 37.010 1.00 38.65 ? 56 HIS B NE2 1 ATOM 1244 N N . GLY B 1 57 ? 19.994 29.651 37.912 1.00 33.19 ? 57 GLY B N 1 ATOM 1245 C CA . GLY B 1 57 ? 19.961 28.346 38.543 1.00 31.58 ? 57 GLY B CA 1 ATOM 1246 C C . GLY B 1 57 ? 19.741 27.173 37.619 1.00 30.71 ? 57 GLY B C 1 ATOM 1247 O O . GLY B 1 57 ? 19.108 26.195 38.003 1.00 30.48 ? 57 GLY B O 1 ATOM 1248 N N . LEU B 1 58 ? 20.258 27.261 36.399 1.00 29.38 ? 58 LEU B N 1 ATOM 1249 C CA . LEU B 1 58 ? 20.105 26.170 35.452 1.00 27.45 ? 58 LEU B CA 1 ATOM 1250 C C . LEU B 1 58 ? 21.016 25.016 35.828 1.00 27.78 ? 58 LEU B C 1 ATOM 1251 O O . LEU B 1 58 ? 20.650 23.851 35.683 1.00 26.15 ? 58 LEU B O 1 ATOM 1252 C CB . LEU B 1 58 ? 20.436 26.641 34.031 1.00 27.42 ? 58 LEU B CB 1 ATOM 1253 C CG . LEU B 1 58 ? 19.326 27.431 33.341 1.00 24.77 ? 58 LEU B CG 1 ATOM 1254 C CD1 . LEU B 1 58 ? 19.813 27.954 31.992 1.00 26.24 ? 58 LEU B CD1 1 ATOM 1255 C CD2 . LEU B 1 58 ? 18.119 26.530 33.162 1.00 25.12 ? 58 LEU B CD2 1 ATOM 1256 N N . THR B 1 59 ? 22.199 25.346 36.333 1.00 28.03 ? 59 THR B N 1 ATOM 1257 C CA . THR B 1 59 ? 23.167 24.324 36.696 1.00 28.15 ? 59 THR B CA 1 ATOM 1258 C C . THR B 1 59 ? 24.129 24.821 37.772 1.00 28.95 ? 59 THR B C 1 ATOM 1259 O O . THR B 1 59 ? 24.010 25.946 38.249 1.00 29.46 ? 59 THR B O 1 ATOM 1260 C CB . THR B 1 59 ? 23.982 23.914 35.456 1.00 26.38 ? 59 THR B CB 1 ATOM 1261 O OG1 . THR B 1 59 ? 24.856 22.830 35.786 1.00 27.79 ? 59 THR B OG1 1 ATOM 1262 C CG2 . THR B 1 59 ? 24.816 25.091 34.961 1.00 25.99 ? 59 THR B CG2 1 ATOM 1263 N N . THR B 1 60 ? 25.080 23.971 38.145 1.00 29.95 ? 60 THR B N 1 ATOM 1264 C CA . THR B 1 60 ? 26.078 24.314 39.156 1.00 29.82 ? 60 THR B CA 1 ATOM 1265 C C . THR B 1 60 ? 27.467 24.153 38.555 1.00 29.70 ? 60 THR B C 1 ATOM 1266 O O . THR B 1 60 ? 27.629 23.532 37.509 1.00 28.71 ? 60 THR B O 1 ATOM 1267 C CB . THR B 1 60 ? 25.981 23.389 40.384 1.00 30.65 ? 60 THR B CB 1 ATOM 1268 O OG1 . THR B 1 60 ? 26.200 22.033 39.975 1.00 30.97 ? 60 THR B OG1 1 ATOM 1269 C CG2 . THR B 1 60 ? 24.613 23.509 41.037 1.00 32.32 ? 60 THR B CG2 1 ATOM 1270 N N . GLU B 1 61 ? 28.470 24.710 39.221 1.00 31.23 ? 61 GLU B N 1 ATOM 1271 C CA . GLU B 1 61 ? 29.840 24.618 38.732 1.00 34.65 ? 61 GLU B CA 1 ATOM 1272 C C . GLU B 1 61 ? 30.300 23.168 38.621 1.00 33.39 ? 61 GLU B C 1 ATOM 1273 O O . GLU B 1 61 ? 31.026 22.803 37.696 1.00 33.87 ? 61 GLU B O 1 ATOM 1274 C CB . GLU B 1 61 ? 30.787 25.372 39.667 1.00 38.43 ? 61 GLU B CB 1 ATOM 1275 C CG . GLU B 1 61 ? 30.544 26.864 39.737 1.00 46.91 ? 61 GLU B CG 1 ATOM 1276 C CD . GLU B 1 61 ? 31.538 27.567 40.641 1.00 52.16 ? 61 GLU B CD 1 ATOM 1277 O OE1 . GLU B 1 61 ? 31.473 28.810 40.744 1.00 55.87 ? 61 GLU B OE1 1 ATOM 1278 O OE2 . GLU B 1 61 ? 32.385 26.875 41.248 1.00 54.49 ? 61 GLU B OE2 1 ATOM 1279 N N . GLU B 1 62 ? 29.871 22.344 39.569 1.00 32.41 ? 62 GLU B N 1 ATOM 1280 C CA . GLU B 1 62 ? 30.256 20.941 39.596 1.00 31.26 ? 62 GLU B CA 1 ATOM 1281 C C . GLU B 1 62 ? 29.699 20.162 38.405 1.00 30.35 ? 62 GLU B C 1 ATOM 1282 O O . GLU B 1 62 ? 30.405 19.367 37.784 1.00 29.60 ? 62 GLU B O 1 ATOM 1283 C CB . GLU B 1 62 ? 29.770 20.298 40.898 0.50 31.81 ? 62 GLU B CB 1 ATOM 1284 C CG . GLU B 1 62 ? 30.499 19.021 41.273 0.50 35.26 ? 62 GLU B CG 1 ATOM 1285 C CD . GLU B 1 62 ? 31.905 19.282 41.780 0.50 36.97 ? 62 GLU B CD 1 ATOM 1286 O OE1 . GLU B 1 62 ? 32.711 19.880 41.038 0.50 38.76 ? 62 GLU B OE1 1 ATOM 1287 O OE2 . GLU B 1 62 ? 32.205 18.888 42.927 0.50 39.08 ? 62 GLU B OE2 1 ATOM 1288 N N . GLN B 1 63 ? 28.432 20.404 38.089 1.00 29.07 ? 63 GLN B N 1 ATOM 1289 C CA . GLN B 1 63 ? 27.756 19.716 36.993 1.00 29.56 ? 63 GLN B CA 1 ATOM 1290 C C . GLN B 1 63 ? 28.106 20.257 35.602 1.00 26.70 ? 63 GLN B C 1 ATOM 1291 O O . GLN B 1 63 ? 28.113 19.515 34.622 1.00 26.05 ? 63 GLN B O 1 ATOM 1292 C CB . GLN B 1 63 ? 26.239 19.793 37.225 1.00 31.76 ? 63 GLN B CB 1 ATOM 1293 C CG . GLN B 1 63 ? 25.370 19.431 36.033 1.00 40.27 ? 63 GLN B CG 1 ATOM 1294 C CD . GLN B 1 63 ? 23.880 19.559 36.340 1.00 43.32 ? 63 GLN B CD 1 ATOM 1295 O OE1 . GLN B 1 63 ? 23.322 18.762 37.096 1.00 47.42 ? 63 GLN B OE1 1 ATOM 1296 N NE2 . GLN B 1 63 ? 23.235 20.570 35.760 1.00 42.04 ? 63 GLN B NE2 1 ATOM 1297 N N . PHE B 1 64 ? 28.413 21.546 35.529 1.00 26.64 ? 64 PHE B N 1 ATOM 1298 C CA . PHE B 1 64 ? 28.721 22.202 34.262 1.00 25.21 ? 64 PHE B CA 1 ATOM 1299 C C . PHE B 1 64 ? 30.149 21.948 33.799 1.00 26.22 ? 64 PHE B C 1 ATOM 1300 O O . PHE B 1 64 ? 30.987 22.848 33.814 1.00 30.31 ? 64 PHE B O 1 ATOM 1301 C CB . PHE B 1 64 ? 28.469 23.707 34.411 1.00 23.78 ? 64 PHE B CB 1 ATOM 1302 C CG . PHE B 1 64 ? 28.372 24.447 33.104 1.00 23.68 ? 64 PHE B CG 1 ATOM 1303 C CD1 . PHE B 1 64 ? 27.592 23.955 32.063 1.00 24.99 ? 64 PHE B CD1 1 ATOM 1304 C CD2 . PHE B 1 64 ? 29.026 25.663 32.933 1.00 28.82 ? 64 PHE B CD2 1 ATOM 1305 C CE1 . PHE B 1 64 ? 27.461 24.666 30.868 1.00 26.03 ? 64 PHE B CE1 1 ATOM 1306 C CE2 . PHE B 1 64 ? 28.904 26.384 31.742 1.00 28.06 ? 64 PHE B CE2 1 ATOM 1307 C CZ . PHE B 1 64 ? 28.117 25.882 30.708 1.00 27.86 ? 64 PHE B CZ 1 ATOM 1308 N N . VAL B 1 65 ? 30.422 20.724 33.364 1.00 25.19 ? 65 VAL B N 1 ATOM 1309 C CA . VAL B 1 65 ? 31.754 20.356 32.915 1.00 22.69 ? 65 VAL B CA 1 ATOM 1310 C C . VAL B 1 65 ? 31.994 20.740 31.460 1.00 24.22 ? 65 VAL B C 1 ATOM 1311 O O . VAL B 1 65 ? 31.071 21.124 30.743 1.00 22.45 ? 65 VAL B O 1 ATOM 1312 C CB . VAL B 1 65 ? 31.986 18.831 33.063 1.00 21.78 ? 65 VAL B CB 1 ATOM 1313 C CG1 . VAL B 1 65 ? 31.904 18.431 34.529 1.00 24.38 ? 65 VAL B CG1 1 ATOM 1314 C CG2 . VAL B 1 65 ? 30.953 18.064 32.247 1.00 20.62 ? 65 VAL B CG2 1 ATOM 1315 N N . GLU B 1 66 ? 33.245 20.635 31.029 1.00 25.26 ? 66 GLU B N 1 ATOM 1316 C CA . GLU B 1 66 ? 33.589 20.949 29.652 1.00 27.61 ? 66 GLU B CA 1 ATOM 1317 C C . GLU B 1 66 ? 32.712 20.124 28.728 1.00 27.75 ? 66 GLU B C 1 ATOM 1318 O O . GLU B 1 66 ? 32.310 19.011 29.059 1.00 29.54 ? 66 GLU B O 1 ATOM 1319 C CB . GLU B 1 66 ? 35.054 20.614 29.368 1.00 30.05 ? 66 GLU B CB 1 ATOM 1320 C CG . GLU B 1 66 ? 36.038 21.385 30.211 1.00 36.89 ? 66 GLU B CG 1 ATOM 1321 C CD . GLU B 1 66 ? 37.475 21.123 29.803 1.00 39.66 ? 66 GLU B CD 1 ATOM 1322 O OE1 . GLU B 1 66 ? 37.903 19.951 29.808 1.00 43.36 ? 66 GLU B OE1 1 ATOM 1323 O OE2 . GLU B 1 66 ? 38.176 22.098 29.475 1.00 42.99 ? 66 GLU B OE2 1 ATOM 1324 N N . GLY B 1 67 ? 32.420 20.676 27.559 1.00 26.41 ? 67 GLY B N 1 ATOM 1325 C CA . GLY B 1 67 ? 31.592 19.958 26.615 1.00 25.31 ? 67 GLY B CA 1 ATOM 1326 C C . GLY B 1 67 ? 30.901 20.928 25.693 1.00 23.25 ? 67 GLY B C 1 ATOM 1327 O O . GLY B 1 67 ? 31.119 22.139 25.773 1.00 21.84 ? 67 GLY B O 1 ATOM 1328 N N . ILE B 1 68 ? 30.072 20.395 24.809 1.00 22.36 ? 68 ILE B N 1 ATOM 1329 C CA . ILE B 1 68 ? 29.344 21.226 23.872 1.00 23.06 ? 68 ILE B CA 1 ATOM 1330 C C . ILE B 1 68 ? 27.916 21.286 24.364 1.00 22.89 ? 68 ILE B C 1 ATOM 1331 O O . ILE B 1 68 ? 27.282 20.256 24.618 1.00 22.71 ? 68 ILE B O 1 ATOM 1332 C CB . ILE B 1 68 ? 29.393 20.641 22.447 1.00 25.16 ? 68 ILE B CB 1 ATOM 1333 C CG1 . ILE B 1 68 ? 30.850 20.546 21.979 1.00 25.87 ? 68 ILE B CG1 1 ATOM 1334 C CG2 . ILE B 1 68 ? 28.593 21.525 21.497 1.00 22.65 ? 68 ILE B CG2 1 ATOM 1335 C CD1 . ILE B 1 68 ? 31.034 19.897 20.615 1.00 30.79 ? 68 ILE B CD1 1 ATOM 1336 N N . TYR B 1 69 ? 27.417 22.504 24.521 1.00 21.60 ? 69 TYR B N 1 ATOM 1337 C CA . TYR B 1 69 ? 26.066 22.701 25.001 1.00 19.85 ? 69 TYR B CA 1 ATOM 1338 C C . TYR B 1 69 ? 25.190 23.419 24.006 1.00 19.92 ? 69 TYR B C 1 ATOM 1339 O O . TYR B 1 69 ? 25.664 24.213 23.193 1.00 21.28 ? 69 TYR B O 1 ATOM 1340 C CB . TYR B 1 69 ? 26.071 23.495 26.306 1.00 19.67 ? 69 TYR B CB 1 ATOM 1341 C CG . TYR B 1 69 ? 26.735 22.781 27.451 1.00 19.72 ? 69 TYR B CG 1 ATOM 1342 C CD1 . TYR B 1 69 ? 28.123 22.749 27.569 1.00 19.81 ? 69 TYR B CD1 1 ATOM 1343 C CD2 . TYR B 1 69 ? 25.972 22.127 28.421 1.00 22.10 ? 69 TYR B CD2 1 ATOM 1344 C CE1 . TYR B 1 69 ? 28.734 22.080 28.633 1.00 22.43 ? 69 TYR B CE1 1 ATOM 1345 C CE2 . TYR B 1 69 ? 26.573 21.459 29.482 1.00 20.57 ? 69 TYR B CE2 1 ATOM 1346 C CZ . TYR B 1 69 ? 27.952 21.443 29.581 1.00 23.45 ? 69 TYR B CZ 1 ATOM 1347 O OH . TYR B 1 69 ? 28.556 20.798 30.635 1.00 23.61 ? 69 TYR B OH 1 ATOM 1348 N N . LYS B 1 70 ? 23.897 23.126 24.081 1.00 19.06 ? 70 LYS B N 1 ATOM 1349 C CA . LYS B 1 70 ? 22.931 23.773 23.220 1.00 18.36 ? 70 LYS B CA 1 ATOM 1350 C C . LYS B 1 70 ? 21.839 24.382 24.081 1.00 19.82 ? 70 LYS B C 1 ATOM 1351 O O . LYS B 1 70 ? 21.241 23.707 24.931 1.00 21.11 ? 70 LYS B O 1 ATOM 1352 C CB . LYS B 1 70 ? 22.312 22.779 22.231 1.00 18.54 ? 70 LYS B CB 1 ATOM 1353 C CG . LYS B 1 70 ? 21.266 23.430 21.328 1.00 24.89 ? 70 LYS B CG 1 ATOM 1354 C CD . LYS B 1 70 ? 20.807 22.516 20.203 1.00 28.76 ? 70 LYS B CD 1 ATOM 1355 C CE . LYS B 1 70 ? 20.023 21.321 20.721 1.00 34.13 ? 70 LYS B CE 1 ATOM 1356 N NZ . LYS B 1 70 ? 19.490 20.498 19.590 1.00 38.99 ? 70 LYS B NZ 1 ATOM 1357 N N . VAL B 1 71 ? 21.607 25.673 23.872 1.00 16.98 ? 71 VAL B N 1 ATOM 1358 C CA . VAL B 1 71 ? 20.573 26.398 24.576 1.00 16.72 ? 71 VAL B CA 1 ATOM 1359 C C . VAL B 1 71 ? 19.504 26.658 23.535 1.00 18.66 ? 71 VAL B C 1 ATOM 1360 O O . VAL B 1 71 ? 19.748 27.330 22.532 1.00 18.52 ? 71 VAL B O 1 ATOM 1361 C CB . VAL B 1 71 ? 21.087 27.741 25.125 1.00 17.41 ? 71 VAL B CB 1 ATOM 1362 C CG1 . VAL B 1 71 ? 19.939 28.520 25.747 1.00 18.58 ? 71 VAL B CG1 1 ATOM 1363 C CG2 . VAL B 1 71 ? 22.179 27.496 26.152 1.00 18.09 ? 71 VAL B CG2 1 ATOM 1364 N N . GLU B 1 72 ? 18.322 26.100 23.770 1.00 17.90 ? 72 GLU B N 1 ATOM 1365 C CA . GLU B 1 72 ? 17.202 26.248 22.857 1.00 19.27 ? 72 GLU B CA 1 ATOM 1366 C C . GLU B 1 72 ? 16.146 27.135 23.507 1.00 20.02 ? 72 GLU B C 1 ATOM 1367 O O . GLU B 1 72 ? 15.660 26.844 24.606 1.00 20.54 ? 72 GLU B O 1 ATOM 1368 C CB . GLU B 1 72 ? 16.614 24.876 22.547 1.00 22.01 ? 72 GLU B CB 1 ATOM 1369 C CG . GLU B 1 72 ? 15.471 24.891 21.564 1.00 32.09 ? 72 GLU B CG 1 ATOM 1370 C CD . GLU B 1 72 ? 15.039 23.490 21.199 1.00 39.55 ? 72 GLU B CD 1 ATOM 1371 O OE1 . GLU B 1 72 ? 14.526 22.775 22.089 1.00 44.23 ? 72 GLU B OE1 1 ATOM 1372 O OE2 . GLU B 1 72 ? 15.227 23.102 20.028 1.00 41.33 ? 72 GLU B OE2 1 ATOM 1373 N N . ILE B 1 73 ? 15.812 28.228 22.833 1.00 17.69 ? 73 ILE B N 1 ATOM 1374 C CA . ILE B 1 73 ? 14.827 29.164 23.337 1.00 17.78 ? 73 ILE B CA 1 ATOM 1375 C C . ILE B 1 73 ? 13.555 29.028 22.502 1.00 18.87 ? 73 ILE B C 1 ATOM 1376 O O . ILE B 1 73 ? 13.573 29.237 21.283 1.00 19.68 ? 73 ILE B O 1 ATOM 1377 C CB . ILE B 1 73 ? 15.379 30.608 23.261 1.00 18.95 ? 73 ILE B CB 1 ATOM 1378 C CG1 . ILE B 1 73 ? 16.702 30.689 24.034 1.00 22.81 ? 73 ILE B CG1 1 ATOM 1379 C CG2 . ILE B 1 73 ? 14.371 31.585 23.825 1.00 18.76 ? 73 ILE B CG2 1 ATOM 1380 C CD1 . ILE B 1 73 ? 17.432 32.018 23.882 1.00 25.86 ? 73 ILE B CD1 1 ATOM 1381 N N . ASP B 1 74 ? 12.454 28.657 23.149 1.00 18.10 ? 74 ASP B N 1 ATOM 1382 C CA . ASP B 1 74 ? 11.189 28.497 22.436 1.00 20.45 ? 74 ASP B CA 1 ATOM 1383 C C . ASP B 1 74 ? 10.572 29.847 22.080 1.00 20.44 ? 74 ASP B C 1 ATOM 1384 O O . ASP B 1 74 ? 9.614 30.303 22.695 1.00 18.76 ? 74 ASP B O 1 ATOM 1385 C CB . ASP B 1 74 ? 10.210 27.665 23.264 1.00 24.56 ? 74 ASP B CB 1 ATOM 1386 C CG . ASP B 1 74 ? 8.894 27.414 22.539 1.00 31.58 ? 74 ASP B CG 1 ATOM 1387 O OD1 . ASP B 1 74 ? 8.791 27.727 21.331 1.00 31.77 ? 74 ASP B OD1 1 ATOM 1388 O OD2 . ASP B 1 74 ? 7.958 26.895 23.179 1.00 35.19 ? 74 ASP B OD2 1 ATOM 1389 N N . THR B 1 75 ? 11.127 30.477 21.054 1.00 20.07 ? 75 THR B N 1 ATOM 1390 C CA . THR B 1 75 ? 10.654 31.778 20.621 1.00 18.96 ? 75 THR B CA 1 ATOM 1391 C C . THR B 1 75 ? 9.283 31.708 19.950 1.00 19.71 ? 75 THR B C 1 ATOM 1392 O O . THR B 1 75 ? 8.487 32.641 20.051 1.00 18.30 ? 75 THR B O 1 ATOM 1393 C CB . THR B 1 75 ? 11.647 32.397 19.634 1.00 19.97 ? 75 THR B CB 1 ATOM 1394 O OG1 . THR B 1 75 ? 11.757 31.540 18.494 1.00 17.80 ? 75 THR B OG1 1 ATOM 1395 C CG2 . THR B 1 75 ? 13.027 32.554 20.285 1.00 18.65 ? 75 THR B CG2 1 ATOM 1396 N N . LYS B 1 76 ? 9.002 30.601 19.271 1.00 20.36 ? 76 LYS B N 1 ATOM 1397 C CA . LYS B 1 76 ? 7.730 30.463 18.568 1.00 23.08 ? 76 LYS B CA 1 ATOM 1398 C C . LYS B 1 76 ? 6.518 30.589 19.483 1.00 22.17 ? 76 LYS B C 1 ATOM 1399 O O . LYS B 1 76 ? 5.586 31.340 19.189 1.00 22.05 ? 76 LYS B O 1 ATOM 1400 C CB . LYS B 1 76 ? 7.674 29.133 17.816 1.00 23.68 ? 76 LYS B CB 1 ATOM 1401 C CG . LYS B 1 76 ? 6.538 29.074 16.810 1.00 26.05 ? 76 LYS B CG 1 ATOM 1402 C CD . LYS B 1 76 ? 6.556 27.779 16.020 1.00 31.80 ? 76 LYS B CD 1 ATOM 1403 C CE . LYS B 1 76 ? 5.499 27.785 14.930 1.00 33.50 ? 76 LYS B CE 1 ATOM 1404 N NZ . LYS B 1 76 ? 5.510 26.515 14.151 1.00 36.97 ? 76 LYS B NZ 1 ATOM 1405 N N . SER B 1 77 ? 6.530 29.856 20.590 1.00 22.02 ? 77 SER B N 1 ATOM 1406 C CA . SER B 1 77 ? 5.428 29.898 21.544 1.00 23.63 ? 77 SER B CA 1 ATOM 1407 C C . SER B 1 77 ? 5.259 31.304 22.093 1.00 22.10 ? 77 SER B C 1 ATOM 1408 O O . SER B 1 77 ? 4.144 31.758 22.314 1.00 22.59 ? 77 SER B O 1 ATOM 1409 C CB . SER B 1 77 ? 5.688 28.932 22.703 1.00 25.17 ? 77 SER B CB 1 ATOM 1410 O OG . SER B 1 77 ? 5.745 27.593 22.245 1.00 29.99 ? 77 SER B OG 1 ATOM 1411 N N . TYR B 1 78 ? 6.379 31.991 22.298 1.00 21.52 ? 78 TYR B N 1 ATOM 1412 C CA . TYR B 1 78 ? 6.367 33.346 22.829 1.00 20.59 ? 78 TYR B CA 1 ATOM 1413 C C . TYR B 1 78 ? 5.594 34.311 21.931 1.00 21.63 ? 78 TYR B C 1 ATOM 1414 O O . TYR B 1 78 ? 4.730 35.056 22.401 1.00 21.78 ? 78 TYR B O 1 ATOM 1415 C CB . TYR B 1 78 ? 7.799 33.850 22.996 1.00 22.15 ? 78 TYR B CB 1 ATOM 1416 C CG . TYR B 1 78 ? 7.871 35.269 23.505 1.00 22.46 ? 78 TYR B CG 1 ATOM 1417 C CD1 . TYR B 1 78 ? 7.607 35.561 24.845 1.00 20.86 ? 78 TYR B CD1 1 ATOM 1418 C CD2 . TYR B 1 78 ? 8.161 36.322 22.645 1.00 22.35 ? 78 TYR B CD2 1 ATOM 1419 C CE1 . TYR B 1 78 ? 7.629 36.861 25.310 1.00 23.31 ? 78 TYR B CE1 1 ATOM 1420 C CE2 . TYR B 1 78 ? 8.183 37.636 23.102 1.00 20.95 ? 78 TYR B CE2 1 ATOM 1421 C CZ . TYR B 1 78 ? 7.916 37.896 24.435 1.00 22.84 ? 78 TYR B CZ 1 ATOM 1422 O OH . TYR B 1 78 ? 7.925 39.189 24.896 1.00 23.61 ? 78 TYR B OH 1 ATOM 1423 N N . TRP B 1 79 ? 5.912 34.304 20.639 1.00 19.16 ? 79 TRP B N 1 ATOM 1424 C CA . TRP B 1 79 ? 5.242 35.183 19.693 1.00 19.71 ? 79 TRP B CA 1 ATOM 1425 C C . TRP B 1 79 ? 3.788 34.784 19.446 1.00 22.57 ? 79 TRP B C 1 ATOM 1426 O O . TRP B 1 79 ? 2.921 35.646 19.308 1.00 24.05 ? 79 TRP B O 1 ATOM 1427 C CB . TRP B 1 79 ? 6.012 35.227 18.368 1.00 18.23 ? 79 TRP B CB 1 ATOM 1428 C CG . TRP B 1 79 ? 7.336 35.916 18.510 1.00 19.45 ? 79 TRP B CG 1 ATOM 1429 C CD1 . TRP B 1 79 ? 8.571 35.362 18.354 1.00 15.81 ? 79 TRP B CD1 1 ATOM 1430 C CD2 . TRP B 1 79 ? 7.552 37.278 18.911 1.00 18.81 ? 79 TRP B CD2 1 ATOM 1431 N NE1 . TRP B 1 79 ? 9.548 36.294 18.640 1.00 17.44 ? 79 TRP B NE1 1 ATOM 1432 C CE2 . TRP B 1 79 ? 8.949 37.476 18.983 1.00 17.97 ? 79 TRP B CE2 1 ATOM 1433 C CE3 . TRP B 1 79 ? 6.700 38.349 19.219 1.00 18.58 ? 79 TRP B CE3 1 ATOM 1434 C CZ2 . TRP B 1 79 ? 9.516 38.703 19.354 1.00 18.22 ? 79 TRP B CZ2 1 ATOM 1435 C CZ3 . TRP B 1 79 ? 7.264 39.571 19.587 1.00 19.45 ? 79 TRP B CZ3 1 ATOM 1436 C CH2 . TRP B 1 79 ? 8.662 39.735 19.652 1.00 19.28 ? 79 TRP B CH2 1 ATOM 1437 N N . LYS B 1 80 ? 3.509 33.487 19.398 1.00 25.58 ? 80 LYS B N 1 ATOM 1438 C CA . LYS B 1 80 ? 2.133 33.052 19.181 1.00 29.33 ? 80 LYS B CA 1 ATOM 1439 C C . LYS B 1 80 ? 1.237 33.548 20.319 1.00 29.44 ? 80 LYS B C 1 ATOM 1440 O O . LYS B 1 80 ? 0.090 33.934 20.097 1.00 28.37 ? 80 LYS B O 1 ATOM 1441 C CB . LYS B 1 80 ? 2.052 31.523 19.079 1.00 32.56 ? 80 LYS B CB 1 ATOM 1442 C CG . LYS B 1 80 ? 2.783 30.935 17.877 1.00 37.54 ? 80 LYS B CG 1 ATOM 1443 C CD . LYS B 1 80 ? 2.134 29.636 17.389 1.00 43.67 ? 80 LYS B CD 1 ATOM 1444 C CE . LYS B 1 80 ? 1.984 28.595 18.495 1.00 47.44 ? 80 LYS B CE 1 ATOM 1445 N NZ . LYS B 1 80 ? 3.291 28.140 19.058 1.00 52.09 ? 80 LYS B NZ 1 ATOM 1446 N N . ALA B 1 81 ? 1.769 33.554 21.535 1.00 30.37 ? 81 ALA B N 1 ATOM 1447 C CA . ALA B 1 81 ? 1.002 34.006 22.692 1.00 32.54 ? 81 ALA B CA 1 ATOM 1448 C C . ALA B 1 81 ? 0.658 35.484 22.573 1.00 34.76 ? 81 ALA B C 1 ATOM 1449 O O . ALA B 1 81 ? -0.280 35.966 23.208 1.00 37.23 ? 81 ALA B O 1 ATOM 1450 C CB . ALA B 1 81 ? 1.785 33.754 23.969 1.00 32.19 ? 81 ALA B CB 1 ATOM 1451 N N . LEU B 1 82 ? 1.422 36.205 21.761 1.00 33.74 ? 82 LEU B N 1 ATOM 1452 C CA . LEU B 1 82 ? 1.189 37.625 21.558 1.00 33.32 ? 82 LEU B CA 1 ATOM 1453 C C . LEU B 1 82 ? 0.378 37.875 20.294 1.00 34.03 ? 82 LEU B C 1 ATOM 1454 O O . LEU B 1 82 ? 0.133 39.021 19.926 1.00 34.81 ? 82 LEU B O 1 ATOM 1455 C CB . LEU B 1 82 ? 2.522 38.376 21.468 1.00 34.37 ? 82 LEU B CB 1 ATOM 1456 C CG . LEU B 1 82 ? 3.370 38.356 22.739 1.00 35.52 ? 82 LEU B CG 1 ATOM 1457 C CD1 . LEU B 1 82 ? 4.706 39.028 22.480 1.00 35.28 ? 82 LEU B CD1 1 ATOM 1458 C CD2 . LEU B 1 82 ? 2.617 39.059 23.863 1.00 36.91 ? 82 LEU B CD2 1 ATOM 1459 N N . GLY B 1 83 ? -0.029 36.799 19.628 1.00 32.96 ? 83 GLY B N 1 ATOM 1460 C CA . GLY B 1 83 ? -0.815 36.940 18.417 1.00 32.66 ? 83 GLY B CA 1 ATOM 1461 C C . GLY B 1 83 ? 0.010 37.295 17.197 1.00 33.81 ? 83 GLY B C 1 ATOM 1462 O O . GLY B 1 83 ? -0.498 37.885 16.241 1.00 33.02 ? 83 GLY B O 1 ATOM 1463 N N . ILE B 1 84 ? 1.287 36.928 17.222 1.00 32.79 ? 84 ILE B N 1 ATOM 1464 C CA . ILE B 1 84 ? 2.189 37.209 16.114 1.00 33.03 ? 84 ILE B CA 1 ATOM 1465 C C . ILE B 1 84 ? 2.752 35.914 15.542 1.00 32.45 ? 84 ILE B C 1 ATOM 1466 O O . ILE B 1 84 ? 3.216 35.057 16.289 1.00 31.82 ? 84 ILE B O 1 ATOM 1467 C CB . ILE B 1 84 ? 3.358 38.104 16.583 1.00 35.02 ? 84 ILE B CB 1 ATOM 1468 C CG1 . ILE B 1 84 ? 2.817 39.468 17.014 1.00 35.06 ? 84 ILE B CG1 1 ATOM 1469 C CG2 . ILE B 1 84 ? 4.387 38.249 15.471 1.00 35.63 ? 84 ILE B CG2 1 ATOM 1470 C CD1 . ILE B 1 84 ? 3.861 40.393 17.606 1.00 39.12 ? 84 ILE B CD1 1 ATOM 1471 N N . SER B 1 85 ? 2.698 35.770 14.219 1.00 31.20 ? 85 SER B N 1 ATOM 1472 C CA . SER B 1 85 ? 3.221 34.574 13.567 1.00 33.25 ? 85 SER B CA 1 ATOM 1473 C C . SER B 1 85 ? 4.698 34.829 13.299 1.00 30.61 ? 85 SER B C 1 ATOM 1474 O O . SER B 1 85 ? 5.056 35.602 12.412 1.00 30.61 ? 85 SER B O 1 ATOM 1475 C CB . SER B 1 85 ? 2.480 34.303 12.254 1.00 37.15 ? 85 SER B CB 1 ATOM 1476 O OG . SER B 1 85 ? 2.444 35.468 11.451 1.00 44.85 ? 85 SER B OG 1 ATOM 1477 N N . PRO B 1 86 ? 5.576 34.184 14.080 1.00 27.99 ? 86 PRO B N 1 ATOM 1478 C CA . PRO B 1 86 ? 7.024 34.334 13.951 1.00 24.54 ? 86 PRO B CA 1 ATOM 1479 C C . PRO B 1 86 ? 7.609 33.510 12.811 1.00 24.12 ? 86 PRO B C 1 ATOM 1480 O O . PRO B 1 86 ? 6.964 32.610 12.275 1.00 25.21 ? 86 PRO B O 1 ATOM 1481 C CB . PRO B 1 86 ? 7.518 33.865 15.306 1.00 24.03 ? 86 PRO B CB 1 ATOM 1482 C CG . PRO B 1 86 ? 6.632 32.693 15.548 1.00 24.97 ? 86 PRO B CG 1 ATOM 1483 C CD . PRO B 1 86 ? 5.252 33.202 15.132 1.00 27.57 ? 86 PRO B CD 1 ATOM 1484 N N . PHE B 1 87 ? 8.850 33.810 12.467 1.00 19.71 ? 87 PHE B N 1 ATOM 1485 C CA . PHE B 1 87 ? 9.520 33.111 11.389 1.00 19.37 ? 87 PHE B CA 1 ATOM 1486 C C . PHE B 1 87 ? 10.191 31.833 11.868 1.00 18.69 ? 87 PHE B C 1 ATOM 1487 O O . PHE B 1 87 ? 10.009 30.769 11.285 1.00 19.34 ? 87 PHE B O 1 ATOM 1488 C CB . PHE B 1 87 ? 10.580 34.013 10.765 1.00 17.45 ? 87 PHE B CB 1 ATOM 1489 C CG . PHE B 1 87 ? 11.357 33.354 9.666 1.00 17.38 ? 87 PHE B CG 1 ATOM 1490 C CD1 . PHE B 1 87 ? 10.790 33.170 8.412 1.00 19.74 ? 87 PHE B CD1 1 ATOM 1491 C CD2 . PHE B 1 87 ? 12.649 32.897 9.892 1.00 18.08 ? 87 PHE B CD2 1 ATOM 1492 C CE1 . PHE B 1 87 ? 11.497 32.542 7.398 1.00 19.28 ? 87 PHE B CE1 1 ATOM 1493 C CE2 . PHE B 1 87 ? 13.365 32.266 8.883 1.00 19.65 ? 87 PHE B CE2 1 ATOM 1494 C CZ . PHE B 1 87 ? 12.786 32.089 7.634 1.00 19.15 ? 87 PHE B CZ 1 ATOM 1495 N N . HIS B 1 88 ? 10.972 31.954 12.934 1.00 17.14 ? 88 HIS B N 1 ATOM 1496 C CA . HIS B 1 88 ? 11.726 30.827 13.471 1.00 17.97 ? 88 HIS B CA 1 ATOM 1497 C C . HIS B 1 88 ? 10.937 29.868 14.343 1.00 18.08 ? 88 HIS B C 1 ATOM 1498 O O . HIS B 1 88 ? 10.008 30.262 15.046 1.00 17.43 ? 88 HIS B O 1 ATOM 1499 C CB . HIS B 1 88 ? 12.926 31.339 14.273 1.00 16.98 ? 88 HIS B CB 1 ATOM 1500 C CG . HIS B 1 88 ? 13.757 32.343 13.540 1.00 18.12 ? 88 HIS B CG 1 ATOM 1501 N ND1 . HIS B 1 88 ? 13.495 33.696 13.577 1.00 18.86 ? 88 HIS B ND1 1 ATOM 1502 C CD2 . HIS B 1 88 ? 14.817 32.187 12.712 1.00 19.19 ? 88 HIS B CD2 1 ATOM 1503 C CE1 . HIS B 1 88 ? 14.357 34.330 12.802 1.00 18.82 ? 88 HIS B CE1 1 ATOM 1504 N NE2 . HIS B 1 88 ? 15.169 33.438 12.265 1.00 22.94 ? 88 HIS B NE2 1 ATOM 1505 N N . GLU B 1 89 ? 11.318 28.599 14.282 1.00 17.66 ? 89 GLU B N 1 ATOM 1506 C CA . GLU B 1 89 ? 10.695 27.573 15.100 1.00 18.93 ? 89 GLU B CA 1 ATOM 1507 C C . GLU B 1 89 ? 11.163 27.775 16.535 1.00 20.21 ? 89 GLU B C 1 ATOM 1508 O O . GLU B 1 89 ? 10.423 27.528 17.485 1.00 20.51 ? 89 GLU B O 1 ATOM 1509 C CB . GLU B 1 89 ? 11.109 26.187 14.603 1.00 21.04 ? 89 GLU B CB 1 ATOM 1510 C CG . GLU B 1 89 ? 10.387 25.790 13.348 1.00 21.07 ? 89 GLU B CG 1 ATOM 1511 C CD . GLU B 1 89 ? 8.891 25.763 13.554 1.00 24.28 ? 89 GLU B CD 1 ATOM 1512 O OE1 . GLU B 1 89 ? 8.423 24.960 14.387 1.00 28.87 ? 89 GLU B OE1 1 ATOM 1513 O OE2 . GLU B 1 89 ? 8.183 26.547 12.896 1.00 28.68 ? 89 GLU B OE2 1 ATOM 1514 N N . HIS B 1 90 ? 12.409 28.217 16.670 1.00 18.80 ? 90 HIS B N 1 ATOM 1515 C CA . HIS B 1 90 ? 13.024 28.490 17.963 1.00 21.37 ? 90 HIS B CA 1 ATOM 1516 C C . HIS B 1 90 ? 14.381 29.122 17.694 1.00 20.49 ? 90 HIS B C 1 ATOM 1517 O O . HIS B 1 90 ? 14.773 29.298 16.538 1.00 22.02 ? 90 HIS B O 1 ATOM 1518 C CB . HIS B 1 90 ? 13.206 27.199 18.770 1.00 24.64 ? 90 HIS B CB 1 ATOM 1519 C CG . HIS B 1 90 ? 14.009 26.151 18.064 1.00 28.86 ? 90 HIS B CG 1 ATOM 1520 N ND1 . HIS B 1 90 ? 13.481 24.930 17.706 1.00 29.69 ? 90 HIS B ND1 1 ATOM 1521 C CD2 . HIS B 1 90 ? 15.293 26.147 17.633 1.00 32.03 ? 90 HIS B CD2 1 ATOM 1522 C CE1 . HIS B 1 90 ? 14.405 24.218 17.085 1.00 32.28 ? 90 HIS B CE1 1 ATOM 1523 N NE2 . HIS B 1 90 ? 15.514 24.934 17.027 1.00 34.10 ? 90 HIS B NE2 1 ATOM 1524 N N . ALA B 1 91 ? 15.086 29.480 18.758 1.00 19.62 ? 91 ALA B N 1 ATOM 1525 C CA . ALA B 1 91 ? 16.412 30.062 18.626 1.00 21.12 ? 91 ALA B CA 1 ATOM 1526 C C . ALA B 1 91 ? 17.351 29.105 19.344 1.00 23.12 ? 91 ALA B C 1 ATOM 1527 O O . ALA B 1 91 ? 17.055 28.650 20.453 1.00 22.72 ? 91 ALA B O 1 ATOM 1528 C CB . ALA B 1 91 ? 16.457 31.438 19.269 1.00 21.02 ? 91 ALA B CB 1 ATOM 1529 N N . GLU B 1 92 ? 18.468 28.784 18.703 1.00 23.72 ? 92 GLU B N 1 ATOM 1530 C CA . GLU B 1 92 ? 19.440 27.870 19.285 1.00 26.34 ? 92 GLU B CA 1 ATOM 1531 C C . GLU B 1 92 ? 20.807 28.520 19.409 1.00 24.62 ? 92 GLU B C 1 ATOM 1532 O O . GLU B 1 92 ? 21.231 29.283 18.542 1.00 26.94 ? 92 GLU B O 1 ATOM 1533 C CB . GLU B 1 92 ? 19.571 26.605 18.429 1.00 31.47 ? 92 GLU B CB 1 ATOM 1534 C CG . GLU B 1 92 ? 18.520 25.537 18.680 1.00 43.05 ? 92 GLU B CG 1 ATOM 1535 C CD . GLU B 1 92 ? 18.728 24.311 17.806 1.00 49.40 ? 92 GLU B CD 1 ATOM 1536 O OE1 . GLU B 1 92 ? 19.890 23.870 17.671 1.00 53.07 ? 92 GLU B OE1 1 ATOM 1537 O OE2 . GLU B 1 92 ? 17.736 23.783 17.260 1.00 53.65 ? 92 GLU B OE2 1 ATOM 1538 N N . VAL B 1 93 ? 21.489 28.224 20.505 1.00 20.91 ? 93 VAL B N 1 ATOM 1539 C CA . VAL B 1 93 ? 22.828 28.740 20.732 1.00 20.00 ? 93 VAL B CA 1 ATOM 1540 C C . VAL B 1 93 ? 23.656 27.520 21.106 1.00 19.34 ? 93 VAL B C 1 ATOM 1541 O O . VAL B 1 93 ? 23.395 26.879 22.120 1.00 21.61 ? 93 VAL B O 1 ATOM 1542 C CB . VAL B 1 93 ? 22.847 29.760 21.878 1.00 21.70 ? 93 VAL B CB 1 ATOM 1543 C CG1 . VAL B 1 93 ? 24.254 30.306 22.071 1.00 22.89 ? 93 VAL B CG1 1 ATOM 1544 C CG2 . VAL B 1 93 ? 21.871 30.881 21.569 1.00 24.74 ? 93 VAL B CG2 1 ATOM 1545 N N . VAL B 1 94 ? 24.632 27.191 20.268 1.00 18.27 ? 94 VAL B N 1 ATOM 1546 C CA . VAL B 1 94 ? 25.487 26.030 20.489 1.00 18.41 ? 94 VAL B CA 1 ATOM 1547 C C . VAL B 1 94 ? 26.893 26.534 20.716 1.00 19.79 ? 94 VAL B C 1 ATOM 1548 O O . VAL B 1 94 ? 27.441 27.263 19.889 1.00 15.81 ? 94 VAL B O 1 ATOM 1549 C CB . VAL B 1 94 ? 25.467 25.085 19.272 1.00 19.07 ? 94 VAL B CB 1 ATOM 1550 C CG1 . VAL B 1 94 ? 26.261 23.821 19.575 1.00 18.69 ? 94 VAL B CG1 1 ATOM 1551 C CG2 . VAL B 1 94 ? 24.027 24.734 18.921 1.00 20.34 ? 94 VAL B CG2 1 ATOM 1552 N N . PHE B 1 95 ? 27.473 26.147 21.846 1.00 18.49 ? 95 PHE B N 1 ATOM 1553 C CA . PHE B 1 95 ? 28.804 26.611 22.189 1.00 19.14 ? 95 PHE B CA 1 ATOM 1554 C C . PHE B 1 95 ? 29.581 25.582 22.992 1.00 21.79 ? 95 PHE B C 1 ATOM 1555 O O . PHE B 1 95 ? 29.008 24.663 23.576 1.00 19.96 ? 95 PHE B O 1 ATOM 1556 C CB . PHE B 1 95 ? 28.694 27.902 23.004 1.00 16.97 ? 95 PHE B CB 1 ATOM 1557 C CG . PHE B 1 95 ? 28.001 27.726 24.333 1.00 19.32 ? 95 PHE B CG 1 ATOM 1558 C CD1 . PHE B 1 95 ? 26.615 27.610 24.406 1.00 21.51 ? 95 PHE B CD1 1 ATOM 1559 C CD2 . PHE B 1 95 ? 28.736 27.693 25.514 1.00 18.55 ? 95 PHE B CD2 1 ATOM 1560 C CE1 . PHE B 1 95 ? 25.969 27.469 25.641 1.00 20.89 ? 95 PHE B CE1 1 ATOM 1561 C CE2 . PHE B 1 95 ? 28.102 27.553 26.752 1.00 22.38 ? 95 PHE B CE2 1 ATOM 1562 C CZ . PHE B 1 95 ? 26.717 27.442 26.812 1.00 21.06 ? 95 PHE B CZ 1 ATOM 1563 N N . THR B 1 96 ? 30.896 25.749 23.016 1.00 23.23 ? 96 THR B N 1 ATOM 1564 C CA . THR B 1 96 ? 31.748 24.847 23.769 1.00 26.94 ? 96 THR B CA 1 ATOM 1565 C C . THR B 1 96 ? 32.147 25.542 25.060 1.00 28.26 ? 96 THR B C 1 ATOM 1566 O O . THR B 1 96 ? 32.656 26.661 25.036 1.00 28.24 ? 96 THR B O 1 ATOM 1567 C CB . THR B 1 96 ? 33.021 24.485 22.979 1.00 26.37 ? 96 THR B CB 1 ATOM 1568 O OG1 . THR B 1 96 ? 32.662 23.705 21.832 1.00 27.71 ? 96 THR B OG1 1 ATOM 1569 C CG2 . THR B 1 96 ? 33.988 23.684 23.851 1.00 29.59 ? 96 THR B CG2 1 ATOM 1570 N N . ALA B 1 97 ? 31.876 24.897 26.187 1.00 28.98 ? 97 ALA B N 1 ATOM 1571 C CA . ALA B 1 97 ? 32.247 25.460 27.476 1.00 33.62 ? 97 ALA B CA 1 ATOM 1572 C C . ALA B 1 97 ? 33.712 25.066 27.639 1.00 38.11 ? 97 ALA B C 1 ATOM 1573 O O . ALA B 1 97 ? 34.036 23.881 27.697 1.00 35.31 ? 97 ALA B O 1 ATOM 1574 C CB . ALA B 1 97 ? 31.400 24.854 28.578 1.00 32.49 ? 97 ALA B CB 1 ATOM 1575 N N . ASN B 1 98 ? 34.591 26.062 27.688 1.00 44.80 ? 98 ASN B N 1 ATOM 1576 C CA . ASN B 1 98 ? 36.024 25.820 27.800 1.00 53.03 ? 98 ASN B CA 1 ATOM 1577 C C . ASN B 1 98 ? 36.464 25.499 29.220 1.00 56.66 ? 98 ASN B C 1 ATOM 1578 O O . ASN B 1 98 ? 37.304 24.622 29.432 1.00 59.58 ? 98 ASN B O 1 ATOM 1579 C CB . ASN B 1 98 ? 36.797 27.032 27.282 1.00 56.89 ? 98 ASN B CB 1 ATOM 1580 C CG . ASN B 1 98 ? 38.213 26.685 26.880 1.00 61.24 ? 98 ASN B CG 1 ATOM 1581 O OD1 . ASN B 1 98 ? 38.960 26.079 27.652 1.00 64.09 ? 98 ASN B OD1 1 ATOM 1582 N ND2 . ASN B 1 98 ? 38.595 27.071 25.667 1.00 62.64 ? 98 ASN B ND2 1 ATOM 1583 N N . ASP B 1 99 ? 35.915 26.220 30.192 1.00 59.92 ? 99 ASP B N 1 ATOM 1584 C CA . ASP B 1 99 ? 36.242 25.976 31.593 1.00 63.35 ? 99 ASP B CA 1 ATOM 1585 C C . ASP B 1 99 ? 37.650 26.425 31.991 1.00 64.75 ? 99 ASP B C 1 ATOM 1586 O O . ASP B 1 99 ? 37.930 26.621 33.174 1.00 65.80 ? 99 ASP B O 1 ATOM 1587 C CB . ASP B 1 99 ? 36.042 24.481 31.900 1.00 64.52 ? 99 ASP B CB 1 ATOM 1588 C CG . ASP B 1 99 ? 36.489 24.097 33.292 1.00 64.19 ? 99 ASP B CG 1 ATOM 1589 O OD1 . ASP B 1 99 ? 37.712 24.063 33.535 1.00 66.33 ? 99 ASP B OD1 1 ATOM 1590 O OD2 . ASP B 1 99 ? 35.616 23.827 34.144 1.00 65.05 ? 99 ASP B OD2 1 ATOM 1591 N N . SER B 1 100 ? 38.530 26.599 31.010 1.00 66.14 ? 100 SER B N 1 ATOM 1592 C CA . SER B 1 100 ? 39.899 27.028 31.282 1.00 67.13 ? 100 SER B CA 1 ATOM 1593 C C . SER B 1 100 ? 39.918 28.377 32.000 1.00 67.99 ? 100 SER B C 1 ATOM 1594 O O . SER B 1 100 ? 40.008 29.429 31.366 1.00 68.30 ? 100 SER B O 1 ATOM 1595 C CB . SER B 1 100 ? 40.692 27.132 29.977 1.00 68.20 ? 100 SER B CB 1 ATOM 1596 O OG . SER B 1 100 ? 40.163 28.143 29.137 1.00 68.88 ? 100 SER B OG 1 ATOM 1597 N N . GLY B 1 101 ? 39.838 28.335 33.327 1.00 68.53 ? 101 GLY B N 1 ATOM 1598 C CA . GLY B 1 101 ? 39.839 29.555 34.114 1.00 67.83 ? 101 GLY B CA 1 ATOM 1599 C C . GLY B 1 101 ? 38.443 29.903 34.598 1.00 67.77 ? 101 GLY B C 1 ATOM 1600 O O . GLY B 1 101 ? 37.460 29.524 33.958 1.00 68.27 ? 101 GLY B O 1 ATOM 1601 N N . PRO B 1 102 ? 38.316 30.619 35.730 1.00 66.69 ? 102 PRO B N 1 ATOM 1602 C CA . PRO B 1 102 ? 37.009 31.003 36.276 1.00 65.93 ? 102 PRO B CA 1 ATOM 1603 C C . PRO B 1 102 ? 36.174 31.741 35.230 1.00 64.36 ? 102 PRO B C 1 ATOM 1604 O O . PRO B 1 102 ? 36.541 32.836 34.797 1.00 64.96 ? 102 PRO B O 1 ATOM 1605 C CB . PRO B 1 102 ? 37.381 31.900 37.455 1.00 66.35 ? 102 PRO B CB 1 ATOM 1606 C CG . PRO B 1 102 ? 38.689 31.329 37.906 1.00 66.66 ? 102 PRO B CG 1 ATOM 1607 C CD . PRO B 1 102 ? 39.404 31.107 36.595 1.00 66.85 ? 102 PRO B CD 1 ATOM 1608 N N . ARG B 1 103 ? 35.055 31.145 34.824 1.00 60.97 ? 103 ARG B N 1 ATOM 1609 C CA . ARG B 1 103 ? 34.206 31.770 33.815 1.00 56.93 ? 103 ARG B CA 1 ATOM 1610 C C . ARG B 1 103 ? 32.705 31.563 34.004 1.00 52.10 ? 103 ARG B C 1 ATOM 1611 O O . ARG B 1 103 ? 32.229 30.444 34.201 1.00 51.39 ? 103 ARG B O 1 ATOM 1612 C CB . ARG B 1 103 ? 34.605 31.278 32.420 1.00 59.88 ? 103 ARG B CB 1 ATOM 1613 C CG . ARG B 1 103 ? 36.054 31.555 32.052 1.00 64.55 ? 103 ARG B CG 1 ATOM 1614 C CD . ARG B 1 103 ? 36.400 30.947 30.708 1.00 69.61 ? 103 ARG B CD 1 ATOM 1615 N NE . ARG B 1 103 ? 37.823 31.070 30.404 1.00 73.91 ? 103 ARG B NE 1 ATOM 1616 C CZ . ARG B 1 103 ? 38.393 30.600 29.300 1.00 76.07 ? 103 ARG B CZ 1 ATOM 1617 N NH1 . ARG B 1 103 ? 37.661 29.972 28.388 1.00 77.00 ? 103 ARG B NH1 1 ATOM 1618 N NH2 . ARG B 1 103 ? 39.696 30.756 29.107 1.00 77.74 ? 103 ARG B NH2 1 ATOM 1619 N N . ARG B 1 104 ? 31.970 32.668 33.939 1.00 45.52 ? 104 ARG B N 1 ATOM 1620 C CA . ARG B 1 104 ? 30.520 32.661 34.062 1.00 40.37 ? 104 ARG B CA 1 ATOM 1621 C C . ARG B 1 104 ? 30.006 32.944 32.655 1.00 35.44 ? 104 ARG B C 1 ATOM 1622 O O . ARG B 1 104 ? 30.522 33.831 31.975 1.00 32.77 ? 104 ARG B O 1 ATOM 1623 C CB . ARG B 1 104 ? 30.055 33.774 35.004 1.00 43.92 ? 104 ARG B CB 1 ATOM 1624 C CG . ARG B 1 104 ? 30.541 33.653 36.446 1.00 52.37 ? 104 ARG B CG 1 ATOM 1625 C CD . ARG B 1 104 ? 29.783 32.580 37.216 1.00 59.10 ? 104 ARG B CD 1 ATOM 1626 N NE . ARG B 1 104 ? 30.165 31.221 36.837 1.00 65.45 ? 104 ARG B NE 1 ATOM 1627 C CZ . ARG B 1 104 ? 31.323 30.649 37.157 1.00 67.89 ? 104 ARG B CZ 1 ATOM 1628 N NH1 . ARG B 1 104 ? 32.224 31.317 37.864 1.00 69.75 ? 104 ARG B NH1 1 ATOM 1629 N NH2 . ARG B 1 104 ? 31.577 29.403 36.775 1.00 69.14 ? 104 ARG B NH2 1 ATOM 1630 N N . TYR B 1 105 ? 29.000 32.197 32.215 1.00 28.57 ? 105 TYR B N 1 ATOM 1631 C CA . TYR B 1 105 ? 28.453 32.402 30.878 1.00 27.41 ? 105 TYR B CA 1 ATOM 1632 C C . TYR B 1 105 ? 27.061 33.015 30.908 1.00 23.38 ? 105 TYR B C 1 ATOM 1633 O O . TYR B 1 105 ? 26.152 32.490 31.552 1.00 22.72 ? 105 TYR B O 1 ATOM 1634 C CB . TYR B 1 105 ? 28.374 31.080 30.103 1.00 26.90 ? 105 TYR B CB 1 ATOM 1635 C CG . TYR B 1 105 ? 29.697 30.400 29.839 1.00 28.65 ? 105 TYR B CG 1 ATOM 1636 C CD1 . TYR B 1 105 ? 30.351 29.691 30.844 1.00 31.92 ? 105 TYR B CD1 1 ATOM 1637 C CD2 . TYR B 1 105 ? 30.286 30.447 28.575 1.00 30.00 ? 105 TYR B CD2 1 ATOM 1638 C CE1 . TYR B 1 105 ? 31.556 29.041 30.599 1.00 33.68 ? 105 TYR B CE1 1 ATOM 1639 C CE2 . TYR B 1 105 ? 31.492 29.800 28.319 1.00 32.60 ? 105 TYR B CE2 1 ATOM 1640 C CZ . TYR B 1 105 ? 32.120 29.098 29.337 1.00 32.96 ? 105 TYR B CZ 1 ATOM 1641 O OH . TYR B 1 105 ? 33.304 28.446 29.096 1.00 35.48 ? 105 TYR B OH 1 ATOM 1642 N N . THR B 1 106 ? 26.902 34.132 30.204 1.00 21.24 ? 106 THR B N 1 ATOM 1643 C CA . THR B 1 106 ? 25.612 34.790 30.102 1.00 18.93 ? 106 THR B CA 1 ATOM 1644 C C . THR B 1 106 ? 25.240 34.756 28.624 1.00 19.73 ? 106 THR B C 1 ATOM 1645 O O . THR B 1 106 ? 25.967 35.284 27.780 1.00 19.63 ? 106 THR B O 1 ATOM 1646 C CB . THR B 1 106 ? 25.665 36.253 30.578 1.00 20.71 ? 106 THR B CB 1 ATOM 1647 O OG1 . THR B 1 106 ? 25.938 36.286 31.984 1.00 24.84 ? 106 THR B OG1 1 ATOM 1648 C CG2 . THR B 1 106 ? 24.335 36.951 30.323 1.00 24.50 ? 106 THR B CG2 1 ATOM 1649 N N . ILE B 1 107 ? 24.128 34.097 28.320 1.00 17.00 ? 107 ILE B N 1 ATOM 1650 C CA . ILE B 1 107 ? 23.647 33.997 26.946 1.00 19.65 ? 107 ILE B CA 1 ATOM 1651 C C . ILE B 1 107 ? 22.473 34.955 26.829 1.00 17.27 ? 107 ILE B C 1 ATOM 1652 O O . ILE B 1 107 ? 21.463 34.785 27.506 1.00 22.15 ? 107 ILE B O 1 ATOM 1653 C CB . ILE B 1 107 ? 23.158 32.573 26.624 1.00 20.23 ? 107 ILE B CB 1 ATOM 1654 C CG1 . ILE B 1 107 ? 24.289 31.562 26.839 1.00 23.54 ? 107 ILE B CG1 1 ATOM 1655 C CG2 . ILE B 1 107 ? 22.656 32.507 25.185 1.00 21.81 ? 107 ILE B CG2 1 ATOM 1656 C CD1 . ILE B 1 107 ? 25.477 31.756 25.938 1.00 26.56 ? 107 ILE B CD1 1 ATOM 1657 N N . ALA B 1 108 ? 22.603 35.965 25.982 1.00 16.87 ? 108 ALA B N 1 ATOM 1658 C CA . ALA B 1 108 ? 21.531 36.933 25.820 1.00 16.56 ? 108 ALA B CA 1 ATOM 1659 C C . ALA B 1 108 ? 20.951 36.825 24.424 1.00 17.05 ? 108 ALA B C 1 ATOM 1660 O O . ALA B 1 108 ? 21.675 36.624 23.458 1.00 19.93 ? 108 ALA B O 1 ATOM 1661 C CB . ALA B 1 108 ? 22.057 38.349 26.054 1.00 19.85 ? 108 ALA B CB 1 ATOM 1662 N N . ALA B 1 109 ? 19.638 36.945 24.330 1.00 17.26 ? 109 ALA B N 1 ATOM 1663 C CA . ALA B 1 109 ? 18.960 36.876 23.047 1.00 17.08 ? 109 ALA B CA 1 ATOM 1664 C C . ALA B 1 109 ? 17.990 38.047 22.954 1.00 16.46 ? 109 ALA B C 1 ATOM 1665 O O . ALA B 1 109 ? 17.282 38.343 23.912 1.00 18.70 ? 109 ALA B O 1 ATOM 1666 C CB . ALA B 1 109 ? 18.209 35.573 22.937 1.00 19.24 ? 109 ALA B CB 1 ATOM 1667 N N . LEU B 1 110 ? 17.976 38.720 21.810 1.00 15.54 ? 110 LEU B N 1 ATOM 1668 C CA . LEU B 1 110 ? 17.067 39.841 21.584 1.00 14.71 ? 110 LEU B CA 1 ATOM 1669 C C . LEU B 1 110 ? 16.143 39.323 20.500 1.00 15.19 ? 110 LEU B C 1 ATOM 1670 O O . LEU B 1 110 ? 16.602 38.972 19.411 1.00 15.37 ? 110 LEU B O 1 ATOM 1671 C CB . LEU B 1 110 ? 17.841 41.066 21.089 1.00 15.35 ? 110 LEU B CB 1 ATOM 1672 C CG . LEU B 1 110 ? 16.996 42.311 20.797 1.00 17.94 ? 110 LEU B CG 1 ATOM 1673 C CD1 . LEU B 1 110 ? 16.205 42.726 22.030 1.00 16.82 ? 110 LEU B CD1 1 ATOM 1674 C CD2 . LEU B 1 110 ? 17.923 43.439 20.351 1.00 20.74 ? 110 LEU B CD2 1 ATOM 1675 N N . LEU B 1 111 ? 14.846 39.295 20.786 1.00 15.77 ? 111 LEU B N 1 ATOM 1676 C CA . LEU B 1 111 ? 13.873 38.739 19.860 1.00 15.42 ? 111 LEU B CA 1 ATOM 1677 C C . LEU B 1 111 ? 12.936 39.675 19.115 1.00 16.35 ? 111 LEU B C 1 ATOM 1678 O O . LEU B 1 111 ? 12.413 40.635 19.678 1.00 15.49 ? 111 LEU B O 1 ATOM 1679 C CB . LEU B 1 111 ? 13.005 37.718 20.601 1.00 15.55 ? 111 LEU B CB 1 ATOM 1680 C CG . LEU B 1 111 ? 13.646 36.700 21.546 1.00 15.95 ? 111 LEU B CG 1 ATOM 1681 C CD1 . LEU B 1 111 ? 12.526 35.898 22.202 1.00 18.98 ? 111 LEU B CD1 1 ATOM 1682 C CD2 . LEU B 1 111 ? 14.610 35.781 20.793 1.00 13.61 ? 111 LEU B CD2 1 ATOM 1683 N N . SER B 1 112 ? 12.734 39.361 17.836 1.00 15.61 ? 112 SER B N 1 ATOM 1684 C CA . SER B 1 112 ? 11.802 40.071 16.965 1.00 16.93 ? 112 SER B CA 1 ATOM 1685 C C . SER B 1 112 ? 11.116 38.933 16.211 1.00 16.29 ? 112 SER B C 1 ATOM 1686 O O . SER B 1 112 ? 11.646 37.824 16.146 1.00 15.36 ? 112 SER B O 1 ATOM 1687 C CB . SER B 1 112 ? 12.530 40.995 15.986 1.00 19.96 ? 112 SER B CB 1 ATOM 1688 O OG . SER B 1 112 ? 13.081 42.108 16.666 1.00 24.75 ? 112 SER B OG 1 ATOM 1689 N N . PRO B 1 113 ? 9.929 39.180 15.641 1.00 16.05 ? 113 PRO B N 1 ATOM 1690 C CA . PRO B 1 113 ? 9.241 38.108 14.915 1.00 16.24 ? 113 PRO B CA 1 ATOM 1691 C C . PRO B 1 113 ? 10.061 37.432 13.811 1.00 17.98 ? 113 PRO B C 1 ATOM 1692 O O . PRO B 1 113 ? 10.022 36.207 13.667 1.00 16.41 ? 113 PRO B O 1 ATOM 1693 C CB . PRO B 1 113 ? 7.993 38.809 14.376 1.00 16.31 ? 113 PRO B CB 1 ATOM 1694 C CG . PRO B 1 113 ? 7.689 39.795 15.476 1.00 17.28 ? 113 PRO B CG 1 ATOM 1695 C CD . PRO B 1 113 ? 9.061 40.362 15.783 1.00 14.79 ? 113 PRO B CD 1 ATOM 1696 N N . TYR B 1 114 ? 10.808 38.215 13.039 1.00 14.84 ? 114 TYR B N 1 ATOM 1697 C CA . TYR B 1 114 ? 11.602 37.644 11.949 1.00 15.44 ? 114 TYR B CA 1 ATOM 1698 C C . TYR B 1 114 ? 13.101 37.756 12.128 1.00 15.89 ? 114 TYR B C 1 ATOM 1699 O O . TYR B 1 114 ? 13.868 37.560 11.183 1.00 16.15 ? 114 TYR B O 1 ATOM 1700 C CB . TYR B 1 114 ? 11.219 38.293 10.620 1.00 14.75 ? 114 TYR B CB 1 ATOM 1701 C CG . TYR B 1 114 ? 9.903 37.811 10.073 1.00 19.37 ? 114 TYR B CG 1 ATOM 1702 C CD1 . TYR B 1 114 ? 8.703 38.142 10.698 1.00 23.09 ? 114 TYR B CD1 1 ATOM 1703 C CD2 . TYR B 1 114 ? 9.859 36.985 8.953 1.00 19.16 ? 114 TYR B CD2 1 ATOM 1704 C CE1 . TYR B 1 114 ? 7.483 37.657 10.221 1.00 27.55 ? 114 TYR B CE1 1 ATOM 1705 C CE2 . TYR B 1 114 ? 8.645 36.495 8.466 1.00 22.28 ? 114 TYR B CE2 1 ATOM 1706 C CZ . TYR B 1 114 ? 7.463 36.834 9.106 1.00 25.82 ? 114 TYR B CZ 1 ATOM 1707 O OH . TYR B 1 114 ? 6.261 36.353 8.639 1.00 31.39 ? 114 TYR B OH 1 ATOM 1708 N N . SER B 1 115 ? 13.529 38.050 13.343 1.00 14.70 ? 115 SER B N 1 ATOM 1709 C CA . SER B 1 115 ? 14.939 38.204 13.587 1.00 13.72 ? 115 SER B CA 1 ATOM 1710 C C . SER B 1 115 ? 15.277 38.007 15.056 1.00 16.45 ? 115 SER B C 1 ATOM 1711 O O . SER B 1 115 ? 14.439 38.178 15.931 1.00 18.11 ? 115 SER B O 1 ATOM 1712 C CB . SER B 1 115 ? 15.362 39.616 13.147 1.00 13.85 ? 115 SER B CB 1 ATOM 1713 O OG . SER B 1 115 ? 16.716 39.879 13.466 1.00 20.67 ? 115 SER B OG 1 ATOM 1714 N N . TYR B 1 116 ? 16.508 37.604 15.319 1.00 16.09 ? 116 TYR B N 1 ATOM 1715 C CA . TYR B 1 116 ? 16.962 37.501 16.692 1.00 16.44 ? 116 TYR B CA 1 ATOM 1716 C C . TYR B 1 116 ? 18.459 37.616 16.674 1.00 16.50 ? 116 TYR B C 1 ATOM 1717 O O . TYR B 1 116 ? 19.118 37.316 15.675 1.00 14.90 ? 116 TYR B O 1 ATOM 1718 C CB . TYR B 1 116 ? 16.504 36.209 17.377 1.00 16.96 ? 116 TYR B CB 1 ATOM 1719 C CG . TYR B 1 116 ? 17.098 34.931 16.860 1.00 19.36 ? 116 TYR B CG 1 ATOM 1720 C CD1 . TYR B 1 116 ? 18.377 34.519 17.241 1.00 21.24 ? 116 TYR B CD1 1 ATOM 1721 C CD2 . TYR B 1 116 ? 16.365 34.111 16.005 1.00 21.20 ? 116 TYR B CD2 1 ATOM 1722 C CE1 . TYR B 1 116 ? 18.907 33.316 16.781 1.00 21.84 ? 116 TYR B CE1 1 ATOM 1723 C CE2 . TYR B 1 116 ? 16.879 32.917 15.544 1.00 23.29 ? 116 TYR B CE2 1 ATOM 1724 C CZ . TYR B 1 116 ? 18.144 32.521 15.931 1.00 22.85 ? 116 TYR B CZ 1 ATOM 1725 O OH . TYR B 1 116 ? 18.629 31.323 15.471 1.00 29.61 ? 116 TYR B OH 1 ATOM 1726 N N . SER B 1 117 ? 18.990 38.118 17.771 1.00 16.76 ? 117 SER B N 1 ATOM 1727 C CA . SER B 1 117 ? 20.412 38.279 17.893 1.00 17.64 ? 117 SER B CA 1 ATOM 1728 C C . SER B 1 117 ? 20.740 37.636 19.211 1.00 18.08 ? 117 SER B C 1 ATOM 1729 O O . SER B 1 117 ? 19.929 37.632 20.134 1.00 19.21 ? 117 SER B O 1 ATOM 1730 C CB . SER B 1 117 ? 20.790 39.762 17.934 1.00 17.36 ? 117 SER B CB 1 ATOM 1731 O OG . SER B 1 117 ? 20.300 40.437 16.782 1.00 25.01 ? 117 SER B OG 1 ATOM 1732 N N . THR B 1 118 ? 21.918 37.053 19.290 1.00 16.67 ? 118 THR B N 1 ATOM 1733 C CA . THR B 1 118 ? 22.319 36.448 20.530 1.00 18.34 ? 118 THR B CA 1 ATOM 1734 C C . THR B 1 118 ? 23.762 36.809 20.729 1.00 18.02 ? 118 THR B C 1 ATOM 1735 O O . THR B 1 118 ? 24.533 36.910 19.773 1.00 18.73 ? 118 THR B O 1 ATOM 1736 C CB . THR B 1 118 ? 22.170 34.924 20.513 1.00 19.02 ? 118 THR B CB 1 ATOM 1737 O OG1 . THR B 1 118 ? 22.573 34.407 21.785 1.00 22.51 ? 118 THR B OG1 1 ATOM 1738 C CG2 . THR B 1 118 ? 23.041 34.299 19.428 1.00 16.69 ? 118 THR B CG2 1 ATOM 1739 N N . THR B 1 119 ? 24.126 37.044 21.975 1.00 17.35 ? 119 THR B N 1 ATOM 1740 C CA . THR B 1 119 ? 25.493 37.382 22.271 1.00 15.52 ? 119 THR B CA 1 ATOM 1741 C C . THR B 1 119 ? 25.833 36.644 23.545 1.00 16.19 ? 119 THR B C 1 ATOM 1742 O O . THR B 1 119 ? 24.949 36.222 24.289 1.00 14.08 ? 119 THR B O 1 ATOM 1743 C CB . THR B 1 119 ? 25.682 38.909 22.469 1.00 18.26 ? 119 THR B CB 1 ATOM 1744 O OG1 . THR B 1 119 ? 27.076 39.203 22.582 1.00 20.23 ? 119 THR B OG1 1 ATOM 1745 C CG2 . THR B 1 119 ? 25.002 39.385 23.735 1.00 20.27 ? 119 THR B CG2 1 ATOM 1746 N N . ALA B 1 120 ? 27.116 36.440 23.770 1.00 17.12 ? 120 ALA B N 1 ATOM 1747 C CA . ALA B 1 120 ? 27.537 35.769 24.978 1.00 17.00 ? 120 ALA B CA 1 ATOM 1748 C C . ALA B 1 120 ? 28.463 36.720 25.707 1.00 19.32 ? 120 ALA B C 1 ATOM 1749 O O . ALA B 1 120 ? 29.305 37.377 25.094 1.00 19.49 ? 120 ALA B O 1 ATOM 1750 C CB . ALA B 1 120 ? 28.264 34.473 24.638 1.00 17.51 ? 120 ALA B CB 1 ATOM 1751 N N . VAL B 1 121 ? 28.268 36.821 27.013 1.00 21.62 ? 121 VAL B N 1 ATOM 1752 C CA . VAL B 1 121 ? 29.106 37.659 27.847 1.00 22.50 ? 121 VAL B CA 1 ATOM 1753 C C . VAL B 1 121 ? 29.759 36.655 28.787 1.00 24.61 ? 121 VAL B C 1 ATOM 1754 O O . VAL B 1 121 ? 29.084 36.035 29.613 1.00 23.93 ? 121 VAL B O 1 ATOM 1755 C CB . VAL B 1 121 ? 28.274 38.668 28.662 1.00 25.72 ? 121 VAL B CB 1 ATOM 1756 C CG1 . VAL B 1 121 ? 29.204 39.601 29.435 1.00 27.04 ? 121 VAL B CG1 1 ATOM 1757 C CG2 . VAL B 1 121 ? 27.370 39.466 27.735 1.00 25.98 ? 121 VAL B CG2 1 ATOM 1758 N N . VAL B 1 122 ? 31.063 36.470 28.625 1.00 24.65 ? 122 VAL B N 1 ATOM 1759 C CA . VAL B 1 122 ? 31.811 35.530 29.445 1.00 28.25 ? 122 VAL B CA 1 ATOM 1760 C C . VAL B 1 122 ? 32.765 36.309 30.345 1.00 30.64 ? 122 VAL B C 1 ATOM 1761 O O . VAL B 1 122 ? 33.694 36.960 29.869 1.00 31.13 ? 122 VAL B O 1 ATOM 1762 C CB . VAL B 1 122 ? 32.605 34.550 28.557 1.00 28.31 ? 122 VAL B CB 1 ATOM 1763 C CG1 . VAL B 1 122 ? 33.261 33.471 29.414 1.00 32.88 ? 122 VAL B CG1 1 ATOM 1764 C CG2 . VAL B 1 122 ? 31.669 33.921 27.523 1.00 27.11 ? 122 VAL B CG2 1 ATOM 1765 N N . THR B 1 123 ? 32.522 36.237 31.649 1.00 32.15 ? 123 THR B N 1 ATOM 1766 C CA . THR B 1 123 ? 33.340 36.948 32.620 1.00 35.79 ? 123 THR B CA 1 ATOM 1767 C C . THR B 1 123 ? 33.860 36.031 33.720 1.00 38.45 ? 123 THR B C 1 ATOM 1768 O O . THR B 1 123 ? 33.477 34.841 33.727 1.00 39.34 ? 123 THR B O 1 ATOM 1769 C CB . THR B 1 123 ? 32.533 38.075 33.272 1.00 36.54 ? 123 THR B CB 1 ATOM 1770 O OG1 . THR B 1 123 ? 31.319 37.534 33.805 1.00 39.81 ? 123 THR B OG1 1 ATOM 1771 C CG2 . THR B 1 123 ? 32.195 39.150 32.249 1.00 37.64 ? 123 THR B CG2 1 HETATM 1772 C C A FLP C 2 . ? 21.415 42.739 11.213 0.50 19.95 ? 125 FLP A C 1 HETATM 1773 C C B FLP C 2 . ? 21.966 41.005 21.358 0.50 19.95 ? 125 FLP A C 1 HETATM 1774 C C1 A FLP C 2 . ? 21.245 42.475 9.835 0.50 19.95 ? 125 FLP A C1 1 HETATM 1775 C C1 B FLP C 2 . ? 22.026 41.312 22.741 0.50 19.95 ? 125 FLP A C1 1 HETATM 1776 C C2 A FLP C 2 . ? 21.624 43.444 8.827 0.50 19.95 ? 125 FLP A C2 1 HETATM 1777 C C2 B FLP C 2 . ? 21.866 42.668 23.223 0.50 19.95 ? 125 FLP A C2 1 HETATM 1778 C C3 A FLP C 2 . ? 22.183 44.693 9.302 0.50 19.95 ? 125 FLP A C3 1 HETATM 1779 C C3 B FLP C 2 . ? 21.643 43.689 22.227 0.50 19.95 ? 125 FLP A C3 1 HETATM 1780 C C4 A FLP C 2 . ? 22.348 44.948 10.682 0.50 19.95 ? 125 FLP A C4 1 HETATM 1781 C C4 B FLP C 2 . ? 21.586 43.379 20.850 0.50 19.95 ? 125 FLP A C4 1 HETATM 1782 C C5 A FLP C 2 . ? 21.964 43.972 11.628 0.50 19.95 ? 125 FLP A C5 1 HETATM 1783 C C5 B FLP C 2 . ? 21.747 42.044 20.420 0.50 19.95 ? 125 FLP A C5 1 HETATM 1784 C C6 A FLP C 2 . ? 21.453 43.178 7.448 0.50 19.95 ? 125 FLP A C6 1 HETATM 1785 C C6 B FLP C 2 . ? 21.926 42.974 24.606 0.50 19.95 ? 125 FLP A C6 1 HETATM 1786 C C7 A FLP C 2 . ? 22.121 42.051 6.836 0.50 19.95 ? 125 FLP A C7 1 HETATM 1787 C C7 B FLP C 2 . ? 20.957 42.401 25.515 0.50 19.95 ? 125 FLP A C7 1 HETATM 1788 C C8 A FLP C 2 . ? 21.965 41.760 5.465 0.50 19.95 ? 125 FLP A C8 1 HETATM 1789 C C8 B FLP C 2 . ? 20.985 42.679 26.897 0.50 19.95 ? 125 FLP A C8 1 HETATM 1790 C C9 A FLP C 2 . ? 21.141 42.577 4.630 0.50 19.95 ? 125 FLP A C9 1 HETATM 1791 C C9 B FLP C 2 . ? 21.978 43.541 27.448 0.50 19.95 ? 125 FLP A C9 1 HETATM 1792 C C10 A FLP C 2 . ? 20.480 43.689 5.204 0.50 19.95 ? 125 FLP A C10 1 HETATM 1793 C C10 B FLP C 2 . ? 22.943 44.120 26.579 0.50 19.95 ? 125 FLP A C10 1 HETATM 1794 C C11 A FLP C 2 . ? 20.623 43.995 6.578 0.50 19.95 ? 125 FLP A C11 1 HETATM 1795 C C11 B FLP C 2 . ? 22.930 43.853 25.191 0.50 19.95 ? 125 FLP A C11 1 HETATM 1796 C C12 A FLP C 2 . ? 20.939 42.290 3.108 0.50 19.95 ? 125 FLP A C12 1 HETATM 1797 C C12 B FLP C 2 . ? 22.045 43.877 28.970 0.50 19.95 ? 125 FLP A C12 1 HETATM 1798 C C13 A FLP C 2 . ? 20.534 40.822 2.814 0.50 19.95 ? 125 FLP A C13 1 HETATM 1799 C C13 B FLP C 2 . ? 22.046 42.620 29.885 0.50 19.95 ? 125 FLP A C13 1 HETATM 1800 C C14 A FLP C 2 . ? 22.200 42.698 2.282 0.50 19.95 ? 125 FLP A C14 1 HETATM 1801 C C14 B FLP C 2 . ? 20.906 44.867 29.376 0.50 19.95 ? 125 FLP A C14 1 HETATM 1802 O O A FLP C 2 . ? 23.333 42.272 2.601 0.50 19.95 ? 125 FLP A O 1 HETATM 1803 O O B FLP C 2 . ? 19.703 44.575 29.167 0.50 19.95 ? 125 FLP A O 1 HETATM 1804 O O1 A FLP C 2 . ? 22.038 43.457 1.307 0.50 19.95 ? 125 FLP A O1 1 HETATM 1805 O O1 B FLP C 2 . ? 21.235 45.951 29.907 0.50 19.95 ? 125 FLP A O1 1 HETATM 1806 F F A FLP C 2 . ? 19.941 45.086 7.037 0.50 19.95 ? 125 FLP A F 1 HETATM 1807 F F B FLP C 2 . ? 23.904 44.460 24.441 0.50 19.95 ? 125 FLP A F 1 HETATM 1808 O O . HOH D 3 . ? 29.748 34.399 14.556 1.00 17.35 ? 126 HOH A O 1 HETATM 1809 O O . HOH D 3 . ? 24.568 28.903 17.901 1.00 17.86 ? 127 HOH A O 1 HETATM 1810 O O . HOH D 3 . ? 32.696 27.989 7.309 1.00 19.44 ? 128 HOH A O 1 HETATM 1811 O O . HOH D 3 . ? 30.366 33.105 17.177 1.00 18.53 ? 129 HOH A O 1 HETATM 1812 O O . HOH D 3 . ? 27.221 40.602 15.103 1.00 22.26 ? 130 HOH A O 1 HETATM 1813 O O . HOH D 3 . ? 31.319 30.955 15.629 1.00 18.74 ? 131 HOH A O 1 HETATM 1814 O O . HOH D 3 . ? 6.991 15.830 3.173 1.00 25.83 ? 132 HOH A O 1 HETATM 1815 O O . HOH D 3 . ? 35.834 46.530 5.017 1.00 29.84 ? 133 HOH A O 1 HETATM 1816 O O . HOH D 3 . ? 9.632 18.936 7.012 1.00 27.36 ? 134 HOH A O 1 HETATM 1817 O O . HOH D 3 . ? 8.375 30.417 8.966 1.00 23.53 ? 135 HOH A O 1 HETATM 1818 O O . HOH D 3 . ? 16.795 34.370 10.162 1.00 22.99 ? 136 HOH A O 1 HETATM 1819 O O . HOH D 3 . ? 17.948 28.543 -3.789 1.00 29.40 ? 137 HOH A O 1 HETATM 1820 O O . HOH D 3 . ? 13.217 37.063 0.058 1.00 30.33 ? 138 HOH A O 1 HETATM 1821 O O . HOH D 3 . ? 23.036 19.393 4.046 1.00 33.14 ? 139 HOH A O 1 HETATM 1822 O O . HOH D 3 . ? 20.708 29.931 16.118 1.00 34.30 ? 140 HOH A O 1 HETATM 1823 O O . HOH D 3 . ? 9.372 28.452 -2.765 1.00 31.86 ? 141 HOH A O 1 HETATM 1824 O O . HOH D 3 . ? 13.985 41.249 8.052 1.00 25.69 ? 142 HOH A O 1 HETATM 1825 O O . HOH D 3 . ? 37.728 32.866 7.092 1.00 33.67 ? 143 HOH A O 1 HETATM 1826 O O . HOH D 3 . ? 25.262 18.023 4.681 1.00 39.03 ? 144 HOH A O 1 HETATM 1827 O O . HOH D 3 . ? 25.463 16.692 6.958 1.00 37.80 ? 145 HOH A O 1 HETATM 1828 O O . HOH D 3 . ? 35.311 37.224 4.412 1.00 32.47 ? 146 HOH A O 1 HETATM 1829 O O . HOH D 3 . ? 28.708 30.499 -3.672 1.00 35.01 ? 147 HOH A O 1 HETATM 1830 O O . HOH D 3 . ? 27.122 17.724 2.681 1.00 42.99 ? 148 HOH A O 1 HETATM 1831 O O . HOH D 3 . ? 26.307 31.362 -4.714 1.00 38.19 ? 149 HOH A O 1 HETATM 1832 O O . HOH D 3 . ? 22.305 21.198 16.427 1.00 40.82 ? 150 HOH A O 1 HETATM 1833 O O . HOH D 3 . ? 25.377 18.407 0.806 1.00 45.77 ? 151 HOH A O 1 HETATM 1834 O O . HOH D 3 . ? 40.640 34.839 19.680 1.00 43.76 ? 152 HOH A O 1 HETATM 1835 O O . HOH D 3 . ? 38.228 45.858 12.255 1.00 37.04 ? 153 HOH A O 1 HETATM 1836 O O . HOH D 3 . ? 4.397 32.416 4.355 1.00 48.63 ? 154 HOH A O 1 HETATM 1837 O O . HOH D 3 . ? 34.870 29.681 6.625 1.00 36.13 ? 155 HOH A O 1 HETATM 1838 O O . HOH D 3 . ? 4.134 30.024 2.845 1.00 37.60 ? 156 HOH A O 1 HETATM 1839 O O . HOH D 3 . ? 7.442 32.724 7.447 1.00 51.09 ? 157 HOH A O 1 HETATM 1840 O O . HOH D 3 . ? 27.967 41.994 -0.369 1.00 45.48 ? 158 HOH A O 1 HETATM 1841 O O . HOH D 3 . ? 34.203 25.558 6.464 1.00 43.69 ? 159 HOH A O 1 HETATM 1842 O O . HOH E 3 . ? 16.544 29.350 14.448 1.00 18.78 ? 125 HOH B O 1 HETATM 1843 O O . HOH E 3 . ? 12.261 35.632 17.693 1.00 18.74 ? 126 HOH B O 1 HETATM 1844 O O . HOH E 3 . ? 16.041 41.479 16.994 1.00 24.76 ? 127 HOH B O 1 HETATM 1845 O O . HOH E 3 . ? 11.340 34.364 15.192 1.00 20.46 ? 128 HOH B O 1 HETATM 1846 O O . HOH E 3 . ? 10.054 32.462 16.653 1.00 23.73 ? 129 HOH B O 1 HETATM 1847 O O . HOH E 3 . ? 25.131 33.668 22.287 1.00 26.18 ? 130 HOH B O 1 HETATM 1848 O O . HOH E 3 . ? 8.437 28.643 11.385 1.00 26.96 ? 131 HOH B O 1 HETATM 1849 O O . HOH E 3 . ? 8.119 29.873 25.045 1.00 28.78 ? 132 HOH B O 1 HETATM 1850 O O . HOH E 3 . ? 11.621 28.011 35.516 1.00 29.56 ? 133 HOH B O 1 HETATM 1851 O O . HOH E 3 . ? 28.907 40.319 24.241 1.00 28.64 ? 134 HOH B O 1 HETATM 1852 O O . HOH E 3 . ? 29.819 17.505 25.264 1.00 27.64 ? 135 HOH B O 1 HETATM 1853 O O . HOH E 3 . ? 28.899 36.444 32.309 1.00 31.07 ? 136 HOH B O 1 HETATM 1854 O O . HOH E 3 . ? 16.491 21.413 16.148 1.00 47.47 ? 137 HOH B O 1 HETATM 1855 O O . HOH E 3 . ? 8.274 48.814 27.247 1.00 35.04 ? 138 HOH B O 1 HETATM 1856 O O . HOH E 3 . ? 7.153 39.489 27.805 1.00 33.70 ? 139 HOH B O 1 HETATM 1857 O O . HOH E 3 . ? 23.427 28.371 36.378 1.00 33.30 ? 140 HOH B O 1 HETATM 1858 O O . HOH E 3 . ? 33.019 28.523 23.048 1.00 37.57 ? 141 HOH B O 1 HETATM 1859 O O . HOH E 3 . ? 16.529 20.193 28.596 1.00 29.88 ? 142 HOH B O 1 HETATM 1860 O O . HOH E 3 . ? 4.892 47.453 19.506 1.00 49.84 ? 143 HOH B O 1 HETATM 1861 O O . HOH E 3 . ? 34.928 36.103 37.164 1.00 47.84 ? 144 HOH B O 1 HETATM 1862 O O . HOH E 3 . ? 12.919 31.814 36.133 1.00 42.15 ? 145 HOH B O 1 HETATM 1863 O O . HOH E 3 . ? 4.158 35.526 25.133 1.00 37.33 ? 146 HOH B O 1 HETATM 1864 O O . HOH E 3 . ? 15.317 32.656 37.129 1.00 39.83 ? 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_defined_assembly _pdbx_struct_assembly.method_details ? _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_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 43.3800000000 0.0000000000 -1.0000000000 0.0000000000 85.5600000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 2001-01-22 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' '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 ASN A 98 ? ? 56.96 19.98 2 1 ASP B 99 ? ? 71.96 -19.34 3 1 SER B 100 ? ? -59.02 87.43 # 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 FLURBIPROFEN FLP 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 FLP 1 125 1 FLP IBU A . D 3 HOH 1 126 100 HOH WAT A . D 3 HOH 2 127 101 HOH WAT A . D 3 HOH 3 128 102 HOH WAT A . D 3 HOH 4 129 105 HOH WAT A . D 3 HOH 5 130 108 HOH WAT A . D 3 HOH 6 131 109 HOH WAT A . D 3 HOH 7 132 111 HOH WAT A . D 3 HOH 8 133 112 HOH WAT A . D 3 HOH 9 134 114 HOH WAT A . D 3 HOH 10 135 115 HOH WAT A . D 3 HOH 11 136 118 HOH WAT A . D 3 HOH 12 137 119 HOH WAT A . D 3 HOH 13 138 121 HOH WAT A . D 3 HOH 14 139 123 HOH WAT A . D 3 HOH 15 140 124 HOH WAT A . D 3 HOH 16 141 125 HOH WAT A . D 3 HOH 17 142 126 HOH WAT A . D 3 HOH 18 143 128 HOH WAT A . D 3 HOH 19 144 130 HOH WAT A . D 3 HOH 20 145 131 HOH WAT A . D 3 HOH 21 146 136 HOH WAT A . D 3 HOH 22 147 137 HOH WAT A . D 3 HOH 23 148 138 HOH WAT A . D 3 HOH 24 149 139 HOH WAT A . D 3 HOH 25 150 142 HOH WAT A . D 3 HOH 26 151 144 HOH WAT A . D 3 HOH 27 152 145 HOH WAT A . D 3 HOH 28 153 146 HOH WAT A . D 3 HOH 29 154 147 HOH WAT A . D 3 HOH 30 155 148 HOH WAT A . D 3 HOH 31 156 149 HOH WAT A . D 3 HOH 32 157 153 HOH WAT A . D 3 HOH 33 158 155 HOH WAT A . D 3 HOH 34 159 156 HOH WAT A . E 3 HOH 1 125 103 HOH WAT B . E 3 HOH 2 126 104 HOH WAT B . E 3 HOH 3 127 106 HOH WAT B . E 3 HOH 4 128 107 HOH WAT B . E 3 HOH 5 129 110 HOH WAT B . E 3 HOH 6 130 113 HOH WAT B . E 3 HOH 7 131 116 HOH WAT B . E 3 HOH 8 132 117 HOH WAT B . E 3 HOH 9 133 120 HOH WAT B . E 3 HOH 10 134 122 HOH WAT B . E 3 HOH 11 135 127 HOH WAT B . E 3 HOH 12 136 129 HOH WAT B . E 3 HOH 13 137 132 HOH WAT B . E 3 HOH 14 138 133 HOH WAT B . E 3 HOH 15 139 134 HOH WAT B . E 3 HOH 16 140 135 HOH WAT B . E 3 HOH 17 141 140 HOH WAT B . E 3 HOH 18 142 141 HOH WAT B . E 3 HOH 19 143 143 HOH WAT B . E 3 HOH 20 144 150 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 . #