data_1FH2 # _entry.id 1FH2 # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.279 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 1FH2 RCSB RCSB011580 WWPDB D_1000011580 # _pdbx_database_related.db_name PDB _pdbx_database_related.db_id 1F86 _pdbx_database_related.details 'TRANSTHYRETIN T119M:L-T4 complex' _pdbx_database_related.content_type unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 1FH2 _pdbx_database_status.recvd_initial_deposition_date 2000-07-31 _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site RCSB _pdbx_database_status.status_code_sf REL _pdbx_database_status.SG_entry . _pdbx_database_status.status_code_mr ? _pdbx_database_status.pdb_format_compatible Y _pdbx_database_status.status_code_cs ? # _audit_author.name 'Sebastiao, M.P.' _audit_author.pdbx_ordinal 1 # _citation.id primary _citation.title 'Transthyretin stability as a key factor in amyloidogenesis: X-ray analysis at atomic resolution.' _citation.journal_abbrev J.Mol.Biol. _citation.journal_volume 306 _citation.page_first 733 _citation.page_last 744 _citation.year 2001 _citation.journal_id_ASTM JMOBAK _citation.country UK _citation.journal_id_ISSN 0022-2836 _citation.journal_id_CSD 0070 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 11243784 _citation.pdbx_database_id_DOI 10.1006/jmbi.2000.4415 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Sebastiao, M.P.' 1 primary 'Lamzin, V.' 2 primary 'Saraiva, M.J.' 3 primary 'Damas, A.M.' 4 # _cell.entry_id 1FH2 _cell.length_a 43.770 _cell.length_b 86.310 _cell.length_c 65.340 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 90.00 _cell.Z_PDB 8 _cell.pdbx_unique_axis ? _cell.length_a_esd ? _cell.length_b_esd ? _cell.length_c_esd ? _cell.angle_alpha_esd ? _cell.angle_beta_esd ? _cell.angle_gamma_esd ? # _symmetry.entry_id 1FH2 _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 _symmetry.space_group_name_Hall ? # loop_ _entity.id _entity.type _entity.src_method _entity.pdbx_description _entity.formula_weight _entity.pdbx_number_of_molecules _entity.pdbx_ec _entity.pdbx_mutation _entity.pdbx_fragment _entity.details 1 polymer nat TRANSTHYRETIN 13839.518 2 ? V30M/T119M ? ? 2 water nat water 18.015 98 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name 'PREALBUMIN, TBPA, TTR, ATTR' # _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 ;GPTGTGESKCPLMVKVLDAVRGSPAINVAMHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWK ALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTMAVVTNPKE ; _entity_poly.pdbx_seq_one_letter_code_can ;GPTGTGESKCPLMVKVLDAVRGSPAINVAMHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWK ALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTMAVVTNPKE ; _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 MET y 1 30 VAL y 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 GLU 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 MET y 1 119 THR y 1 120 ALA n 1 121 VAL n 1 122 VAL n 1 123 THR n 1 124 ASN n 1 125 PRO n 1 126 LYS n 1 127 GLU n # _entity_src_nat.entity_id 1 _entity_src_nat.pdbx_src_id 1 _entity_src_nat.pdbx_alt_source_flag sample _entity_src_nat.pdbx_beg_seq_num ? _entity_src_nat.pdbx_end_seq_num ? _entity_src_nat.common_name human _entity_src_nat.pdbx_organism_scientific 'Homo sapiens' _entity_src_nat.pdbx_ncbi_taxonomy_id 9606 _entity_src_nat.genus Homo _entity_src_nat.species ? _entity_src_nat.strain ? _entity_src_nat.tissue ? _entity_src_nat.tissue_fraction ? _entity_src_nat.pdbx_secretion ? _entity_src_nat.pdbx_fragment ? _entity_src_nat.pdbx_variant ? _entity_src_nat.pdbx_cell_line ? _entity_src_nat.pdbx_atcc ? _entity_src_nat.pdbx_cellular_location ? _entity_src_nat.pdbx_organ ? _entity_src_nat.pdbx_organelle ? _entity_src_nat.pdbx_cell ? _entity_src_nat.pdbx_plasmid_name ? _entity_src_nat.pdbx_plasmid_details ? _entity_src_nat.details ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code TTHY_HUMAN _struct_ref.pdbx_db_accession P02766 _struct_ref.entity_id 1 _struct_ref.pdbx_align_begin 21 _struct_ref.pdbx_seq_one_letter_code ;GPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWK ALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE ; _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 1FH2 A 1 ? 127 ? P02766 21 ? 147 ? 1 127 2 1 1FH2 B 1 ? 127 ? P02766 21 ? 147 ? 1 127 # loop_ _struct_ref_seq_dif.align_id _struct_ref_seq_dif.pdbx_pdb_id_code _struct_ref_seq_dif.mon_id _struct_ref_seq_dif.pdbx_pdb_strand_id _struct_ref_seq_dif.seq_num _struct_ref_seq_dif.pdbx_pdb_ins_code _struct_ref_seq_dif.pdbx_seq_db_name _struct_ref_seq_dif.pdbx_seq_db_accession_code _struct_ref_seq_dif.db_mon_id _struct_ref_seq_dif.pdbx_seq_db_seq_num _struct_ref_seq_dif.details _struct_ref_seq_dif.pdbx_auth_seq_num _struct_ref_seq_dif.pdbx_ordinal 1 1FH2 MET A 30 ? UNP P02766 VAL 50 MICROHETEROGENEITY 30 1 1 1FH2 MET A 119 ? UNP P02766 THR 139 MICROHETEROGENEITY 119 2 2 1FH2 MET B 30 ? UNP P02766 VAL 50 MICROHETEROGENEITY 30 3 2 1FH2 MET B 119 ? UNP P02766 THR 139 MICROHETEROGENEITY 119 4 # 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 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 1FH2 _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_percent_sol 44.93 _exptl_crystal.density_Matthews 2.23 _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.preparation ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method 'VAPOR DIFFUSION, SITTING DROP' _exptl_crystal_grow.pH 5.1 _exptl_crystal_grow.temp 287 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pdbx_details 'Ammonium Sulphate, Citrate Buffer, Glycerol, pH 5.1, VAPOR DIFFUSION, SITTING DROP, temperature 287K' _exptl_crystal_grow.pdbx_pH_range . # _diffrn.id 1 _diffrn.ambient_temp 277 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector 'IMAGE PLATE' _diffrn_detector.type MARRESEARCH _diffrn_detector.pdbx_collection_date 1997-11-14 _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.monochromator ? _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 0.99 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'EMBL/DESY, HAMBURG BEAMLINE X31' _diffrn_source.pdbx_wavelength 0.99 _diffrn_source.pdbx_synchrotron_site 'EMBL/DESY, Hamburg' _diffrn_source.pdbx_synchrotron_beamline X31 _diffrn_source.pdbx_wavelength_list ? # _reflns.entry_id 1FH2 _reflns.observed_criterion_sigma_I 2.0 _reflns.observed_criterion_sigma_F 2.0 _reflns.d_resolution_low 20 _reflns.d_resolution_high 1.8 _reflns.number_obs 120772 _reflns.number_all 121001 _reflns.percent_possible_obs 100 _reflns.pdbx_Rmerge_I_obs 0.0570000 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 20 _reflns.B_iso_Wilson_estimate 24 _reflns.pdbx_redundancy 5.9 _reflns.R_free_details ? _reflns.limit_h_max ? _reflns.limit_h_min ? _reflns.limit_k_max ? _reflns.limit_k_min ? _reflns.limit_l_max ? _reflns.limit_l_min ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? _reflns.pdbx_ordinal 1 _reflns.pdbx_diffrn_id 1 # _reflns_shell.d_res_high 1.80 _reflns_shell.d_res_low 1.82 _reflns_shell.percent_possible_obs ? _reflns_shell.percent_possible_all 100 _reflns_shell.Rmerge_I_obs 0.3180000 _reflns_shell.meanI_over_sigI_obs ? _reflns_shell.pdbx_Rsym_value ? _reflns_shell.pdbx_redundancy 5 _reflns_shell.number_unique_all 23677 _reflns_shell.number_measured_all ? _reflns_shell.number_measured_obs ? _reflns_shell.number_unique_obs ? _reflns_shell.pdbx_chi_squared ? _reflns_shell.pdbx_ordinal 1 _reflns_shell.pdbx_diffrn_id 1 # _refine.entry_id 1FH2 _refine.ls_number_reflns_obs ? _refine.ls_number_reflns_all 22140 _refine.pdbx_ls_sigma_I 2 _refine.pdbx_ls_sigma_F 4 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.ls_d_res_low 8 _refine.ls_d_res_high 1.8 _refine.ls_percent_reflns_obs ? _refine.ls_R_factor_obs 0.1667000 _refine.ls_R_factor_all 0.1765000 _refine.ls_R_factor_R_work 0.1700000 _refine.ls_R_factor_R_free 0.2128000 _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 1165 _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 ? _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 RANDOM _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_overall_phase_error ? _refine.pdbx_solvent_vdw_probe_radii ? _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii ? _refine.ls_wR_factor_R_free ? _refine.ls_wR_factor_R_work ? _refine.overall_FOM_free_R_set ? _refine.overall_FOM_work_R_set ? _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 1794 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 0 _refine_hist.number_atoms_solvent 98 _refine_hist.number_atoms_total 1892 _refine_hist.d_res_high 1.8 _refine_hist.d_res_low 8 # loop_ _refine_ls_restr.type _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.number _refine_ls_restr.pdbx_refine_id _refine_ls_restr.pdbx_restraint_function s_bond_d 0.012 ? ? ? 'X-RAY DIFFRACTION' ? s_angle_d 0.027 ? ? ? 'X-RAY DIFFRACTION' ? # _pdbx_refine.entry_id 1FH2 _pdbx_refine.R_factor_all_no_cutoff 0.1760000 _pdbx_refine.R_factor_obs_no_cutoff 0.1670000 _pdbx_refine.free_R_factor_no_cutoff 0.2130000 _pdbx_refine.free_R_val_test_set_size_perc_no_cutoff ? _pdbx_refine.free_R_val_test_set_ct_no_cutoff 1165 _pdbx_refine.R_factor_all_4sig_cutoff ? _pdbx_refine.R_factor_obs_4sig_cutoff ? _pdbx_refine.free_R_factor_4sig_cutoff ? _pdbx_refine.free_R_val_test_set_size_perc_4sig_cutoff ? _pdbx_refine.free_R_val_test_set_ct_4sig_cutoff ? _pdbx_refine.number_reflns_obs_4sig_cutoff ? _pdbx_refine.number_reflns_obs_no_cutoff ? _pdbx_refine.pdbx_refine_id 'X-RAY DIFFRACTION' _pdbx_refine.free_R_error_no_cutoff ? # _struct.entry_id 1FH2 _struct.title 'TRANSTHYRETIN STABILITY AS A KEY FACTOR IN AMYLOIDOGENESIS' _struct.pdbx_descriptor TRANSTHYRETIN _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 1FH2 _struct_keywords.pdbx_keywords 'TRANSPORT PROTEIN' _struct_keywords.text 'Amyloid, Transthyretin, Protein Stability, TRANSPORT PROTEIN' # 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 2 ? # _struct_biol.id 1 _struct_biol.details 'The biological assembly is a tetramer constructed from chains A and B by crystallographic two-fold symmetry.' _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 ? 12 ? B ? 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 ? anti-parallel A 3 4 ? anti-parallel A 4 5 ? parallel A 5 6 ? anti-parallel A 6 7 ? anti-parallel A 7 8 ? anti-parallel A 8 9 ? parallel A 9 10 ? anti-parallel A 10 11 ? anti-parallel A 11 12 ? anti-parallel B 1 2 ? anti-parallel B 2 3 ? anti-parallel B 3 4 ? anti-parallel B 4 5 ? anti-parallel B 5 6 ? anti-parallel B 6 7 ? anti-parallel B 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 GLU A 54 ? LEU A 55 ? GLU A 54 LEU A 55 A 2 LEU A 12 ? ASP A 18 ? LEU A 12 ASP A 18 A 3 SER A 23 ? PRO A 24 ? SER A 23 PRO A 24 A 4 LEU A 12 ? ASP A 18 ? LEU A 12 ASP A 18 A 5 ARG A 104 ? SER A 112 ? ARG A 104 SER A 112 A 6 SER A 115 ? THR A 123 ? SER A 115 THR A 123 A 7 SER B 115 ? THR B 123 ? SER B 115 THR B 123 A 8 ARG B 104 ? SER B 112 ? ARG B 104 SER B 112 A 9 LEU B 12 ? ASP B 18 ? LEU B 12 ASP B 18 A 10 SER B 23 ? PRO B 24 ? SER B 23 PRO B 24 A 11 LEU B 12 ? ASP B 18 ? LEU B 12 ASP B 18 A 12 GLU B 54 ? LEU B 55 ? GLU B 54 LEU B 55 B 1 TRP A 41 ? LYS A 48 ? TRP A 41 LYS A 48 B 2 ALA A 29 ? LYS A 35 ? ALA A 29 LYS A 35 B 3 GLY A 67 ? ILE A 73 ? GLY A 67 ILE A 73 B 4 HIS A 88 ? ALA A 97 ? HIS A 88 ALA A 97 B 5 HIS B 88 ? ALA B 97 ? HIS B 88 ALA B 97 B 6 GLY B 67 ? ILE B 73 ? GLY B 67 ILE B 73 B 7 ALA B 29 ? LYS B 35 ? ALA B 29 LYS B 35 B 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 N LEU A 55 ? N LEU A 55 O VAL A 14 ? O VAL A 14 A 2 3 N ASP A 18 ? N ASP A 18 O SER A 23 ? O SER A 23 A 3 4 O SER A 23 ? O SER A 23 N ASP A 18 ? N ASP A 18 A 4 5 N MET A 13 ? N MET A 13 O TYR A 105 ? O TYR A 105 A 5 6 N SER A 112 ? N SER A 112 O SER A 115 ? O SER A 115 A 6 7 N THR A 118 ? N THR A 118 O TYR B 116 ? O TYR B 116 A 7 8 O THR B 123 ? O THR B 123 N ARG B 104 ? N ARG B 104 A 8 9 N ILE B 107 ? N ILE B 107 O MET B 13 ? O MET B 13 A 9 10 N ASP B 18 ? N ASP B 18 O SER B 23 ? O SER B 23 A 10 11 O SER B 23 ? O SER B 23 N ASP B 18 ? N ASP B 18 A 11 12 N VAL B 14 ? N VAL B 14 O LEU B 55 ? O LEU B 55 B 1 2 O GLY A 47 ? O GLY A 47 N MET A 30 ? N MET A 30 B 2 3 N LYS A 35 ? N LYS A 35 O ILE A 68 ? O ILE A 68 B 3 4 N ILE A 73 ? N ILE A 73 O ALA A 91 ? O ALA A 91 B 4 5 O VAL A 94 ? O VAL A 94 N GLU B 89 ? N GLU B 89 B 5 6 N ALA B 97 ? N ALA B 97 O GLY B 67 ? O GLY B 67 B 6 7 N GLU B 72 ? N GLU B 72 O HIS B 31 ? O HIS B 31 B 7 8 O ARG B 34 ? O ARG B 34 N GLU B 42 ? N GLU B 42 # _database_PDB_matrix.entry_id 1FH2 _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 1FH2 _atom_sites.fract_transf_matrix[1][1] 0.02285 _atom_sites.fract_transf_matrix[1][2] 0.00000 _atom_sites.fract_transf_matrix[1][3] 0.00000 _atom_sites.fract_transf_matrix[2][1] 0.00000 _atom_sites.fract_transf_matrix[2][2] 0.01159 _atom_sites.fract_transf_matrix[2][3] 0.00000 _atom_sites.fract_transf_matrix[3][1] 0.00000 _atom_sites.fract_transf_matrix[3][2] 0.00000 _atom_sites.fract_transf_matrix[3][3] 0.01530 _atom_sites.fract_transf_vector[1] 0.00000 _atom_sites.fract_transf_vector[2] 0.00000 _atom_sites.fract_transf_vector[3] 0.00000 # loop_ _atom_type.symbol C N O S # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 N N . CYS A 1 10 ? 15.372 32.128 25.115 1.00 58.88 ? 10 CYS A N 1 ATOM 2 C CA . CYS A 1 10 ? 16.179 31.597 26.214 1.00 43.16 ? 10 CYS A CA 1 ATOM 3 C C . CYS A 1 10 ? 15.421 31.727 27.523 1.00 31.36 ? 10 CYS A C 1 ATOM 4 O O . CYS A 1 10 ? 15.330 32.838 28.054 1.00 37.02 ? 10 CYS A O 1 ATOM 5 C CB . CYS A 1 10 ? 17.523 32.318 26.324 1.00 46.12 ? 10 CYS A CB 1 ATOM 6 S SG . CYS A 1 10 ? 18.919 31.210 26.015 1.00 72.45 ? 10 CYS A SG 1 ATOM 7 N N . PRO A 1 11 ? 14.857 30.635 28.005 1.00 25.90 ? 11 PRO A N 1 ATOM 8 C CA . PRO A 1 11 ? 13.972 30.720 29.166 1.00 20.19 ? 11 PRO A CA 1 ATOM 9 C C . PRO A 1 11 ? 14.728 30.788 30.484 1.00 21.94 ? 11 PRO A C 1 ATOM 10 O O . PRO A 1 11 ? 14.085 31.056 31.494 1.00 15.69 ? 11 PRO A O 1 ATOM 11 C CB . PRO A 1 11 ? 13.222 29.392 29.112 1.00 24.45 ? 11 PRO A CB 1 ATOM 12 C CG . PRO A 1 11 ? 14.277 28.460 28.601 1.00 27.70 ? 11 PRO A CG 1 ATOM 13 C CD . PRO A 1 11 ? 14.974 29.251 27.517 1.00 27.91 ? 11 PRO A CD 1 ATOM 14 N N . LEU A 1 12 ? 16.030 30.536 30.520 1.00 14.57 ? 12 LEU A N 1 ATOM 15 C CA . LEU A 1 12 ? 16.708 30.495 31.827 1.00 10.72 ? 12 LEU A CA 1 ATOM 16 C C . LEU A 1 12 ? 18.105 31.075 31.623 1.00 20.48 ? 12 LEU A C 1 ATOM 17 O O . LEU A 1 12 ? 18.867 30.516 30.825 1.00 19.81 ? 12 LEU A O 1 ATOM 18 C CB . LEU A 1 12 ? 16.805 29.091 32.402 1.00 18.92 ? 12 LEU A CB 1 ATOM 19 C CG . LEU A 1 12 ? 17.516 28.888 33.740 1.00 21.08 ? 12 LEU A CG 1 ATOM 20 C CD1 . LEU A 1 12 ? 16.794 29.675 34.822 1.00 22.83 ? 12 LEU A CD1 1 ATOM 21 C CD2 . LEU A 1 12 ? 17.626 27.412 34.085 1.00 18.50 ? 12 LEU A CD2 1 ATOM 22 N N . MET A 1 13 ? 18.355 32.180 32.316 1.00 13.70 ? 13 MET A N 1 ATOM 23 C CA . MET A 1 13 ? 19.620 32.873 32.167 1.00 11.98 ? 13 MET A CA 1 ATOM 24 C C . MET A 1 13 ? 20.131 33.253 33.558 1.00 15.85 ? 13 MET A C 1 ATOM 25 O O . MET A 1 13 ? 19.328 33.591 34.421 1.00 17.93 ? 13 MET A O 1 ATOM 26 C CB . MET A 1 13 ? 19.521 34.131 31.324 1.00 21.78 ? 13 MET A CB 1 ATOM 27 C CG . MET A 1 13 ? 18.530 34.110 30.174 1.00 50.07 ? 13 MET A CG 1 ATOM 28 S SD . MET A 1 13 ? 18.193 35.770 29.540 1.00 59.18 ? 13 MET A SD 1 ATOM 29 C CE . MET A 1 13 ? 19.726 36.587 29.992 1.00 43.94 ? 13 MET A CE 1 ATOM 30 N N . VAL A 1 14 ? 21.448 33.163 33.702 1.00 12.28 ? 14 VAL A N 1 ATOM 31 C CA . VAL A 1 14 ? 22.060 33.500 34.990 1.00 10.63 ? 14 VAL A CA 1 ATOM 32 C C . VAL A 1 14 ? 23.107 34.578 34.758 1.00 16.59 ? 14 VAL A C 1 ATOM 33 O O . VAL A 1 14 ? 23.856 34.547 33.774 1.00 18.97 ? 14 VAL A O 1 ATOM 34 C CB . VAL A 1 14 ? 22.637 32.202 35.599 1.00 18.27 ? 14 VAL A CB 1 ATOM 35 C CG1 . VAL A 1 14 ? 23.237 32.417 36.977 1.00 18.85 ? 14 VAL A CG1 1 ATOM 36 C CG2 . VAL A 1 14 ? 21.549 31.141 35.693 1.00 20.00 ? 14 VAL A CG2 1 ATOM 37 N N . LYS A 1 15 ? 23.177 35.562 35.658 1.00 11.74 ? 15 LYS A N 1 ATOM 38 C CA . LYS A 1 15 ? 24.180 36.617 35.591 1.00 13.24 ? 15 LYS A CA 1 ATOM 39 C C . LYS A 1 15 ? 24.907 36.697 36.930 1.00 16.12 ? 15 LYS A C 1 ATOM 40 O O . LYS A 1 15 ? 24.254 36.678 37.994 1.00 14.94 ? 15 LYS A O 1 ATOM 41 C CB . LYS A 1 15 ? 23.512 37.947 35.259 1.00 17.82 ? 15 LYS A CB 1 ATOM 42 C CG . LYS A 1 15 ? 24.446 39.145 35.350 1.00 29.60 ? 15 LYS A CG 1 ATOM 43 C CD . LYS A 1 15 ? 25.187 39.392 34.053 1.00 39.06 ? 15 LYS A CD 1 ATOM 44 C CE . LYS A 1 15 ? 25.894 40.739 34.023 1.00 41.15 ? 15 LYS A CE 1 ATOM 45 N NZ . LYS A 1 15 ? 26.379 41.045 32.639 1.00 40.36 ? 15 LYS A NZ 1 ATOM 46 N N . VAL A 1 16 ? 26.233 36.750 36.906 1.00 10.64 ? 16 VAL A N 1 ATOM 47 C CA . VAL A 1 16 ? 26.922 36.750 38.210 1.00 10.97 ? 16 VAL A CA 1 ATOM 48 C C . VAL A 1 16 ? 27.900 37.929 38.236 1.00 13.31 ? 16 VAL A C 1 ATOM 49 O O . VAL A 1 16 ? 28.645 38.085 37.260 1.00 12.09 ? 16 VAL A O 1 ATOM 50 C CB . VAL A 1 16 ? 27.659 35.441 38.460 1.00 12.94 ? 16 VAL A CB 1 ATOM 51 C CG1 . VAL A 1 16 ? 28.222 35.363 39.886 1.00 15.29 ? 16 VAL A CG1 1 ATOM 52 C CG2 . VAL A 1 16 ? 26.730 34.242 38.222 1.00 17.66 ? 16 VAL A CG2 1 ATOM 53 N N . LEU A 1 17 ? 27.849 38.711 39.301 1.00 10.40 ? 17 LEU A N 1 ATOM 54 C CA . LEU A 1 17 ? 28.666 39.906 39.454 1.00 10.15 ? 17 LEU A CA 1 ATOM 55 C C . LEU A 1 17 ? 29.546 39.812 40.695 1.00 10.90 ? 17 LEU A C 1 ATOM 56 O O . LEU A 1 17 ? 29.185 39.238 41.727 1.00 12.95 ? 17 LEU A O 1 ATOM 57 C CB . LEU A 1 17 ? 27.781 41.175 39.536 1.00 11.33 ? 17 LEU A CB 1 ATOM 58 C CG . LEU A 1 17 ? 26.844 41.455 38.362 1.00 21.40 ? 17 LEU A CG 1 ATOM 59 C CD1 . LEU A 1 17 ? 25.995 42.689 38.660 1.00 23.70 ? 17 LEU A CD1 1 ATOM 60 C CD2 . LEU A 1 17 ? 27.617 41.707 37.074 1.00 26.46 ? 17 LEU A CD2 1 ATOM 61 N N . ASP A 1 18 ? 30.738 40.404 40.596 1.00 9.57 ? 18 ASP A N 1 ATOM 62 C CA . ASP A 1 18 ? 31.707 40.444 41.688 1.00 10.05 ? 18 ASP A CA 1 ATOM 63 C C . ASP A 1 18 ? 31.702 41.812 42.349 1.00 12.22 ? 18 ASP A C 1 ATOM 64 O O . ASP A 1 18 ? 32.103 42.775 41.685 1.00 11.19 ? 18 ASP A O 1 ATOM 65 C CB . ASP A 1 18 ? 33.077 40.146 41.068 1.00 12.18 ? 18 ASP A CB 1 ATOM 66 C CG . ASP A 1 18 ? 34.242 40.155 42.039 1.00 13.80 ? 18 ASP A CG 1 ATOM 67 O OD1 . ASP A 1 18 ? 34.212 40.817 43.079 1.00 10.93 ? 18 ASP A OD1 1 ATOM 68 O OD2 . ASP A 1 18 ? 35.244 39.448 41.767 1.00 17.34 ? 18 ASP A OD2 1 ATOM 69 N N . ALA A 1 19 ? 31.271 41.944 43.597 1.00 8.50 ? 19 ALA A N 1 ATOM 70 C CA . ALA A 1 19 ? 31.155 43.217 44.266 1.00 9.92 ? 19 ALA A CA 1 ATOM 71 C C . ALA A 1 19 ? 32.486 43.709 44.871 1.00 15.32 ? 19 ALA A C 1 ATOM 72 O O . ALA A 1 19 ? 32.523 44.823 45.399 1.00 13.89 ? 19 ALA A O 1 ATOM 73 C CB . ALA A 1 19 ? 30.164 43.146 45.428 1.00 9.96 ? 19 ALA A CB 1 ATOM 74 N N . VAL A 1 20 ? 33.523 42.883 44.842 1.00 11.70 ? 20 VAL A N 1 ATOM 75 C CA . VAL A 1 20 ? 34.844 43.279 45.353 1.00 14.78 ? 20 VAL A CA 1 ATOM 76 C C . VAL A 1 20 ? 35.611 44.016 44.244 1.00 16.45 ? 20 VAL A C 1 ATOM 77 O O . VAL A 1 20 ? 36.308 45.012 44.458 1.00 17.44 ? 20 VAL A O 1 ATOM 78 C CB . VAL A 1 20 ? 35.647 42.059 45.840 1.00 17.62 ? 20 VAL A CB 1 ATOM 79 C CG1 . VAL A 1 20 ? 37.072 42.463 46.202 1.00 24.94 ? 20 VAL A CG1 1 ATOM 80 C CG2 . VAL A 1 20 ? 34.989 41.406 47.060 1.00 18.38 ? 20 VAL A CG2 1 ATOM 81 N N . ARG A 1 21 ? 35.474 43.506 43.028 1.00 9.50 ? 21 ARG A N 1 ATOM 82 C CA . ARG A 1 21 ? 36.187 44.027 41.875 1.00 12.35 ? 21 ARG A CA 1 ATOM 83 C C . ARG A 1 21 ? 35.378 44.910 40.938 1.00 15.25 ? 21 ARG A C 1 ATOM 84 O O . ARG A 1 21 ? 35.996 45.463 40.017 1.00 18.31 ? 21 ARG A O 1 ATOM 85 C CB . ARG A 1 21 ? 36.720 42.845 41.047 1.00 17.10 ? 21 ARG A CB 1 ATOM 86 C CG . ARG A 1 21 ? 37.858 42.183 41.841 1.00 33.75 ? 21 ARG A CG 1 ATOM 87 C CD . ARG A 1 21 ? 37.961 40.716 41.470 1.00 42.63 ? 21 ARG A CD 1 ATOM 88 N NE . ARG A 1 21 ? 38.013 40.495 40.031 1.00 36.52 ? 21 ARG A NE 1 ATOM 89 C CZ . ARG A 1 21 ? 38.834 39.599 39.486 1.00 62.03 ? 21 ARG A CZ 1 ATOM 90 N NH1 . ARG A 1 21 ? 39.633 38.886 40.271 1.00 92.29 ? 21 ARG A NH1 1 ATOM 91 N NH2 . ARG A 1 21 ? 38.867 39.411 38.177 1.00 87.92 ? 21 ARG A NH2 1 ATOM 92 N N . GLY A 1 22 ? 34.064 45.020 41.138 1.00 9.67 ? 22 GLY A N 1 ATOM 93 C CA . GLY A 1 22 ? 33.240 45.830 40.245 1.00 11.03 ? 22 GLY A CA 1 ATOM 94 C C . GLY A 1 22 ? 33.235 45.320 38.825 1.00 16.84 ? 22 GLY A C 1 ATOM 95 O O . GLY A 1 22 ? 33.392 46.034 37.825 1.00 14.09 ? 22 GLY A O 1 ATOM 96 N N . SER A 1 23 ? 33.022 44.021 38.671 1.00 15.00 ? 23 SER A N 1 ATOM 97 C CA . SER A 1 23 ? 33.140 43.375 37.370 1.00 15.00 ? 23 SER A CA 1 ATOM 98 C C . SER A 1 23 ? 32.236 42.150 37.282 1.00 15.00 ? 23 SER A C 1 ATOM 99 O O . SER A 1 23 ? 31.862 41.630 38.332 1.00 15.33 ? 23 SER A O 1 ATOM 100 C CB A SER A 1 23 ? 34.593 42.968 37.112 0.50 15.00 ? 23 SER A CB 1 ATOM 101 C CB B SER A 1 23 ? 34.643 43.018 37.161 0.50 15.00 ? 23 SER A CB 1 ATOM 102 O OG A SER A 1 23 ? 34.711 41.563 36.970 0.50 15.00 ? 23 SER A OG 1 ATOM 103 O OG B SER A 1 23 ? 35.066 42.026 38.082 0.50 15.00 ? 23 SER A OG 1 ATOM 104 N N . PRO A 1 24 ? 31.991 41.682 36.079 1.00 14.85 ? 24 PRO A N 1 ATOM 105 C CA . PRO A 1 24 ? 31.306 40.393 35.932 1.00 11.06 ? 24 PRO A CA 1 ATOM 106 C C . PRO A 1 24 ? 32.187 39.347 36.591 1.00 13.01 ? 24 PRO A C 1 ATOM 107 O O . PRO A 1 24 ? 33.409 39.521 36.668 1.00 14.91 ? 24 PRO A O 1 ATOM 108 C CB . PRO A 1 24 ? 31.244 40.159 34.428 1.00 13.91 ? 24 PRO A CB 1 ATOM 109 C CG . PRO A 1 24 ? 31.438 41.510 33.831 1.00 25.92 ? 24 PRO A CG 1 ATOM 110 C CD . PRO A 1 24 ? 32.349 42.261 34.764 1.00 16.38 ? 24 PRO A CD 1 ATOM 111 N N . ALA A 1 25 ? 31.538 38.271 37.049 1.00 13.55 ? 25 ALA A N 1 ATOM 112 C CA . ALA A 1 25 ? 32.271 37.140 37.621 1.00 14.36 ? 25 ALA A CA 1 ATOM 113 C C . ALA A 1 25 ? 32.438 36.096 36.514 1.00 17.48 ? 25 ALA A C 1 ATOM 114 O O . ALA A 1 25 ? 31.453 35.508 36.088 1.00 14.57 ? 25 ALA A O 1 ATOM 115 C CB . ALA A 1 25 ? 31.566 36.533 38.815 1.00 12.14 ? 25 ALA A CB 1 ATOM 116 N N . ILE A 1 26 ? 33.664 35.933 36.041 1.00 12.45 ? 26 ILE A N 1 ATOM 117 C CA . ILE A 1 26 ? 33.948 35.145 34.840 1.00 11.75 ? 26 ILE A CA 1 ATOM 118 C C . ILE A 1 26 ? 34.309 33.716 35.161 1.00 11.55 ? 26 ILE A C 1 ATOM 119 O O . ILE A 1 26 ? 34.981 33.522 36.191 1.00 16.02 ? 26 ILE A O 1 ATOM 120 C CB . ILE A 1 26 ? 35.122 35.884 34.139 1.00 24.76 ? 26 ILE A CB 1 ATOM 121 C CG1 . ILE A 1 26 ? 34.722 37.325 33.784 1.00 22.27 ? 26 ILE A CG1 1 ATOM 122 C CG2 . ILE A 1 26 ? 35.649 35.143 32.926 1.00 33.45 ? 26 ILE A CG2 1 ATOM 123 C CD1 . ILE A 1 26 ? 35.713 38.049 32.897 1.00 37.60 ? 26 ILE A CD1 1 ATOM 124 N N . ASN A 1 27 ? 33.898 32.735 34.367 1.00 14.81 ? 27 ASN A N 1 ATOM 125 C CA . ASN A 1 27 ? 34.313 31.353 34.607 1.00 20.31 ? 27 ASN A CA 1 ATOM 126 C C . ASN A 1 27 ? 33.749 30.755 35.880 1.00 18.96 ? 27 ASN A C 1 ATOM 127 O O . ASN A 1 27 ? 34.316 29.845 36.483 1.00 22.92 ? 27 ASN A O 1 ATOM 128 C CB . ASN A 1 27 ? 35.849 31.273 34.700 1.00 19.38 ? 27 ASN A CB 1 ATOM 129 C CG . ASN A 1 27 ? 36.399 30.408 33.577 1.00 49.69 ? 27 ASN A CG 1 ATOM 130 O OD1 . ASN A 1 27 ? 36.629 30.913 32.477 1.00 74.80 ? 27 ASN A OD1 1 ATOM 131 N ND2 . ASN A 1 27 ? 36.595 29.128 33.877 1.00 52.81 ? 27 ASN A ND2 1 ATOM 132 N N . VAL A 1 28 ? 32.612 31.262 36.347 1.00 14.06 ? 28 VAL A N 1 ATOM 133 C CA . VAL A 1 28 ? 32.007 30.671 37.543 1.00 13.02 ? 28 VAL A CA 1 ATOM 134 C C . VAL A 1 28 ? 31.223 29.422 37.146 1.00 11.76 ? 28 VAL A C 1 ATOM 135 O O . VAL A 1 28 ? 30.412 29.560 36.207 1.00 14.30 ? 28 VAL A O 1 ATOM 136 C CB . VAL A 1 28 ? 31.053 31.678 38.200 1.00 18.16 ? 28 VAL A CB 1 ATOM 137 C CG1 . VAL A 1 28 ? 30.264 31.034 39.335 1.00 20.17 ? 28 VAL A CG1 1 ATOM 138 C CG2 . VAL A 1 28 ? 31.863 32.878 38.722 1.00 17.41 ? 28 VAL A CG2 1 ATOM 139 N N . ALA A 1 29 ? 31.408 28.277 37.784 1.00 8.47 ? 29 ALA A N 1 ATOM 140 C CA . ALA A 1 29 ? 30.660 27.078 37.380 1.00 11.19 ? 29 ALA A CA 1 ATOM 141 C C . ALA A 1 29 ? 29.245 27.109 37.953 1.00 11.67 ? 29 ALA A C 1 ATOM 142 O O . ALA A 1 29 ? 29.057 27.519 39.090 1.00 12.12 ? 29 ALA A O 1 ATOM 143 C CB . ALA A 1 29 ? 31.332 25.800 37.866 1.00 16.25 ? 29 ALA A CB 1 ATOM 144 N N A MET A 1 30 ? 28.337 26.628 37.129 0.30 12.46 ? 30 MET A N 1 ATOM 145 C CA A MET A 1 30 ? 26.915 26.556 37.366 0.30 14.85 ? 30 MET A CA 1 ATOM 146 C C A MET A 1 30 ? 26.337 25.162 37.207 0.30 12.80 ? 30 MET A C 1 ATOM 147 O O A MET A 1 30 ? 26.590 24.533 36.181 0.30 15.99 ? 30 MET A O 1 ATOM 148 C CB A MET A 1 30 ? 26.233 27.450 36.314 0.30 13.55 ? 30 MET A CB 1 ATOM 149 C CG A MET A 1 30 ? 26.726 28.894 36.418 0.30 18.43 ? 30 MET A CG 1 ATOM 150 S SD A MET A 1 30 ? 25.339 29.903 36.982 0.30 40.10 ? 30 MET A SD 1 ATOM 151 C CE A MET A 1 30 ? 23.992 28.994 36.230 0.30 37.87 ? 30 MET A CE 1 ATOM 152 N N B VAL A 1 30 ? 28.270 26.710 37.151 0.70 10.08 ? 30 VAL A N 1 ATOM 153 C CA B VAL A 1 30 ? 26.880 26.650 37.583 0.70 14.24 ? 30 VAL A CA 1 ATOM 154 C C B VAL A 1 30 ? 26.274 25.289 37.241 0.70 12.27 ? 30 VAL A C 1 ATOM 155 O O B VAL A 1 30 ? 26.462 24.820 36.120 0.70 14.39 ? 30 VAL A O 1 ATOM 156 C CB B VAL A 1 30 ? 26.056 27.739 36.887 0.70 14.15 ? 30 VAL A CB 1 ATOM 157 C CG1 B VAL A 1 30 ? 24.465 27.509 37.080 0.70 14.56 ? 30 VAL A CG1 1 ATOM 158 C CG2 B VAL A 1 30 ? 26.844 29.276 37.314 0.70 18.02 ? 30 VAL A CG2 1 ATOM 159 N N . HIS A 1 31 ? 25.553 24.686 38.171 1.00 12.31 ? 31 HIS A N 1 ATOM 160 C CA . HIS A 1 31 ? 24.853 23.432 37.937 1.00 18.46 ? 31 HIS A CA 1 ATOM 161 C C . HIS A 1 31 ? 23.369 23.648 38.259 1.00 17.83 ? 31 HIS A C 1 ATOM 162 O O . HIS A 1 31 ? 23.104 24.226 39.311 1.00 15.33 ? 31 HIS A O 1 ATOM 163 C CB . HIS A 1 31 ? 25.384 22.303 38.807 1.00 20.88 ? 31 HIS A CB 1 ATOM 164 C CG . HIS A 1 31 ? 26.847 22.049 38.594 1.00 25.86 ? 31 HIS A CG 1 ATOM 165 N ND1 . HIS A 1 31 ? 27.305 21.003 37.837 1.00 27.85 ? 31 HIS A ND1 1 ATOM 166 C CD2 . HIS A 1 31 ? 27.937 22.706 39.050 1.00 23.01 ? 31 HIS A CD2 1 ATOM 167 C CE1 . HIS A 1 31 ? 28.633 21.012 37.822 1.00 25.59 ? 31 HIS A CE1 1 ATOM 168 N NE2 . HIS A 1 31 ? 29.036 22.038 38.546 1.00 26.47 ? 31 HIS A NE2 1 ATOM 169 N N . VAL A 1 32 ? 22.543 23.167 37.354 1.00 13.41 ? 32 VAL A N 1 ATOM 170 C CA . VAL A 1 32 ? 21.093 23.215 37.537 1.00 11.43 ? 32 VAL A CA 1 ATOM 171 C C . VAL A 1 32 ? 20.544 21.805 37.733 1.00 14.68 ? 32 VAL A C 1 ATOM 172 O O . VAL A 1 32 ? 20.899 20.849 37.036 1.00 14.25 ? 32 VAL A O 1 ATOM 173 C CB . VAL A 1 32 ? 20.419 23.863 36.324 1.00 15.04 ? 32 VAL A CB 1 ATOM 174 C CG1 . VAL A 1 32 ? 18.924 24.014 36.624 1.00 14.79 ? 32 VAL A CG1 1 ATOM 175 C CG2 . VAL A 1 32 ? 21.078 25.183 35.943 1.00 16.77 ? 32 VAL A CG2 1 ATOM 176 N N . PHE A 1 33 ? 19.643 21.656 38.683 1.00 12.58 ? 33 PHE A N 1 ATOM 177 C CA . PHE A 1 33 ? 19.019 20.387 39.022 1.00 13.15 ? 33 PHE A CA 1 ATOM 178 C C . PHE A 1 33 ? 17.496 20.578 38.973 1.00 21.11 ? 33 PHE A C 1 ATOM 179 O O . PHE A 1 33 ? 17.027 21.703 39.133 1.00 12.03 ? 33 PHE A O 1 ATOM 180 C CB . PHE A 1 33 ? 19.440 19.915 40.399 1.00 13.34 ? 33 PHE A CB 1 ATOM 181 C CG . PHE A 1 33 ? 20.948 19.819 40.596 1.00 19.82 ? 33 PHE A CG 1 ATOM 182 C CD1 . PHE A 1 33 ? 21.692 20.910 41.018 1.00 16.12 ? 33 PHE A CD1 1 ATOM 183 C CD2 . PHE A 1 33 ? 21.611 18.627 40.356 1.00 22.16 ? 33 PHE A CD2 1 ATOM 184 C CE1 . PHE A 1 33 ? 23.066 20.843 41.203 1.00 19.45 ? 33 PHE A CE1 1 ATOM 185 C CE2 . PHE A 1 33 ? 22.988 18.548 40.534 1.00 25.23 ? 33 PHE A CE2 1 ATOM 186 C CZ . PHE A 1 33 ? 23.722 19.640 40.961 1.00 22.00 ? 33 PHE A CZ 1 ATOM 187 N N . ARG A 1 34 ? 16.761 19.497 38.750 1.00 17.07 ? 34 ARG A N 1 ATOM 188 C CA . ARG A 1 34 ? 15.288 19.529 38.780 1.00 19.47 ? 34 ARG A CA 1 ATOM 189 C C . ARG A 1 34 ? 14.792 18.458 39.737 1.00 23.56 ? 34 ARG A C 1 ATOM 190 O O . ARG A 1 34 ? 15.327 17.331 39.800 1.00 19.50 ? 34 ARG A O 1 ATOM 191 C CB . ARG A 1 34 ? 14.740 19.362 37.353 1.00 18.80 ? 34 ARG A CB 1 ATOM 192 C CG . ARG A 1 34 ? 13.247 19.082 37.289 1.00 17.41 ? 34 ARG A CG 1 ATOM 193 C CD . ARG A 1 34 ? 12.703 18.986 35.857 1.00 26.06 ? 34 ARG A CD 1 ATOM 194 N NE . ARG A 1 34 ? 11.234 18.948 36.025 1.00 33.88 ? 34 ARG A NE 1 ATOM 195 C CZ . ARG A 1 34 ? 10.547 17.827 36.226 1.00 45.32 ? 34 ARG A CZ 1 ATOM 196 N NH1 . ARG A 1 34 ? 11.178 16.656 36.269 1.00 31.33 ? 34 ARG A NH1 1 ATOM 197 N NH2 . ARG A 1 34 ? 9.225 17.894 36.374 1.00 35.74 ? 34 ARG A NH2 1 ATOM 198 N N . LYS A 1 35 ? 13.781 18.766 40.555 1.00 14.43 ? 35 LYS A N 1 ATOM 199 C CA . LYS A 1 35 ? 13.371 17.783 41.559 1.00 16.55 ? 35 LYS A CA 1 ATOM 200 C C . LYS A 1 35 ? 12.593 16.682 40.849 1.00 21.68 ? 35 LYS A C 1 ATOM 201 O O . LYS A 1 35 ? 11.711 16.960 40.029 1.00 20.57 ? 35 LYS A O 1 ATOM 202 C CB . LYS A 1 35 ? 12.565 18.443 42.665 1.00 24.94 ? 35 LYS A CB 1 ATOM 203 C CG . LYS A 1 35 ? 12.658 17.777 44.027 1.00 26.92 ? 35 LYS A CG 1 ATOM 204 C CD . LYS A 1 35 ? 11.814 18.550 45.030 1.00 43.93 ? 35 LYS A CD 1 ATOM 205 C CE . LYS A 1 35 ? 12.614 18.899 46.274 1.00 56.10 ? 35 LYS A CE 1 ATOM 206 N NZ . LYS A 1 35 ? 11.908 19.912 47.113 1.00 79.79 ? 35 LYS A NZ 1 ATOM 207 N N . ALA A 1 36 ? 12.937 15.424 41.126 1.00 31.63 ? 36 ALA A N 1 ATOM 208 C CA . ALA A 1 36 ? 12.324 14.364 40.315 1.00 36.12 ? 36 ALA A CA 1 ATOM 209 C C . ALA A 1 36 ? 11.156 13.729 41.064 1.00 34.73 ? 36 ALA A C 1 ATOM 210 O O . ALA A 1 36 ? 10.935 14.080 42.222 1.00 36.08 ? 36 ALA A O 1 ATOM 211 C CB . ALA A 1 36 ? 13.340 13.310 39.920 1.00 50.20 ? 36 ALA A CB 1 ATOM 212 N N . ALA A 1 37 ? 10.462 12.834 40.375 1.00 41.32 ? 37 ALA A N 1 ATOM 213 C CA . ALA A 1 37 ? 9.272 12.178 40.905 1.00 47.93 ? 37 ALA A CA 1 ATOM 214 C C . ALA A 1 37 ? 9.527 11.662 42.315 1.00 51.91 ? 37 ALA A C 1 ATOM 215 O O . ALA A 1 37 ? 8.735 11.847 43.238 1.00 45.66 ? 37 ALA A O 1 ATOM 216 C CB . ALA A 1 37 ? 8.846 11.070 39.956 1.00 65.26 ? 37 ALA A CB 1 ATOM 217 N N . ASP A 1 38 ? 10.675 11.018 42.477 1.00 57.39 ? 38 ASP A N 1 ATOM 218 C CA . ASP A 1 38 ? 11.076 10.431 43.749 1.00 68.50 ? 38 ASP A CA 1 ATOM 219 C C . ASP A 1 38 ? 11.547 11.473 44.750 1.00 62.28 ? 38 ASP A C 1 ATOM 220 O O . ASP A 1 38 ? 12.006 11.158 45.855 1.00 43.39 ? 38 ASP A O 1 ATOM 221 C CB . ASP A 1 38 ? 12.172 9.386 43.499 1.00 82.68 ? 38 ASP A CB 1 ATOM 222 C CG . ASP A 1 38 ? 13.080 9.727 42.334 1.00 91.14 ? 38 ASP A CG 1 ATOM 223 O OD1 . ASP A 1 38 ? 12.575 9.988 41.221 1.00 102.76 ? 38 ASP A OD1 1 ATOM 224 O OD2 . ASP A 1 38 ? 14.316 9.732 42.529 1.00 97.24 ? 38 ASP A OD2 1 ATOM 225 N N . ASP A 1 39 ? 11.453 12.754 44.399 1.00 65.62 ? 39 ASP A N 1 ATOM 226 C CA . ASP A 1 39 ? 11.852 13.804 45.331 1.00 69.97 ? 39 ASP A CA 1 ATOM 227 C C . ASP A 1 39 ? 13.350 13.811 45.630 1.00 62.40 ? 39 ASP A C 1 ATOM 228 O O . ASP A 1 39 ? 13.736 14.026 46.781 1.00 68.47 ? 39 ASP A O 1 ATOM 229 C CB . ASP A 1 39 ? 11.082 13.672 46.651 1.00 77.68 ? 39 ASP A CB 1 ATOM 230 C CG . ASP A 1 39 ? 9.735 14.376 46.572 1.00 89.78 ? 39 ASP A CG 1 ATOM 231 O OD1 . ASP A 1 39 ? 9.545 15.217 45.663 1.00 100.10 ? 39 ASP A OD1 1 ATOM 232 O OD2 . ASP A 1 39 ? 8.872 14.076 47.416 1.00 114.40 ? 39 ASP A OD2 1 ATOM 233 N N . THR A 1 40 ? 14.144 13.587 44.601 1.00 52.12 ? 40 THR A N 1 ATOM 234 C CA . THR A 1 40 ? 15.598 13.681 44.604 1.00 41.01 ? 40 THR A CA 1 ATOM 235 C C . THR A 1 40 ? 16.021 14.671 43.518 1.00 28.82 ? 40 THR A C 1 ATOM 236 O O . THR A 1 40 ? 15.278 14.901 42.558 1.00 29.72 ? 40 THR A O 1 ATOM 237 C CB . THR A 1 40 ? 16.245 12.304 44.389 1.00 47.12 ? 40 THR A CB 1 ATOM 238 O OG1 . THR A 1 40 ? 17.659 12.376 44.643 1.00 73.68 ? 40 THR A OG1 1 ATOM 239 C CG2 . THR A 1 40 ? 16.103 11.842 42.948 1.00 34.13 ? 40 THR A CG2 1 ATOM 240 N N . TRP A 1 41 ? 17.198 15.268 43.629 1.00 28.73 ? 41 TRP A N 1 ATOM 241 C CA . TRP A 1 41 ? 17.630 16.238 42.621 1.00 28.76 ? 41 TRP A CA 1 ATOM 242 C C . TRP A 1 41 ? 18.322 15.584 41.440 1.00 23.67 ? 41 TRP A C 1 ATOM 243 O O . TRP A 1 41 ? 19.374 14.967 41.601 1.00 36.31 ? 41 TRP A O 1 ATOM 244 C CB . TRP A 1 41 ? 18.612 17.243 43.233 1.00 23.87 ? 41 TRP A CB 1 ATOM 245 C CG . TRP A 1 41 ? 17.946 18.115 44.241 1.00 30.01 ? 41 TRP A CG 1 ATOM 246 C CD1 . TRP A 1 41 ? 18.074 18.060 45.595 1.00 41.25 ? 41 TRP A CD1 1 ATOM 247 C CD2 . TRP A 1 41 ? 17.033 19.179 43.949 1.00 26.36 ? 41 TRP A CD2 1 ATOM 248 N NE1 . TRP A 1 41 ? 17.293 19.034 46.177 1.00 39.84 ? 41 TRP A NE1 1 ATOM 249 C CE2 . TRP A 1 41 ? 16.648 19.731 45.187 1.00 34.09 ? 41 TRP A CE2 1 ATOM 250 C CE3 . TRP A 1 41 ? 16.519 19.705 42.755 1.00 24.83 ? 41 TRP A CE3 1 ATOM 251 C CZ2 . TRP A 1 41 ? 15.760 20.797 45.282 1.00 23.36 ? 41 TRP A CZ2 1 ATOM 252 C CZ3 . TRP A 1 41 ? 15.640 20.761 42.877 1.00 19.88 ? 41 TRP A CZ3 1 ATOM 253 C CH2 . TRP A 1 41 ? 15.274 21.287 44.102 1.00 17.74 ? 41 TRP A CH2 1 ATOM 254 N N . GLU A 1 42 ? 17.754 15.729 40.270 1.00 18.63 ? 42 GLU A N 1 ATOM 255 C CA . GLU A 1 42 ? 18.335 15.201 39.038 1.00 20.91 ? 42 GLU A CA 1 ATOM 256 C C . GLU A 1 42 ? 19.101 16.256 38.252 1.00 25.00 ? 42 GLU A C 1 ATOM 257 O O . GLU A 1 42 ? 18.621 17.395 38.139 1.00 17.81 ? 42 GLU A O 1 ATOM 258 C CB . GLU A 1 42 ? 17.178 14.700 38.198 1.00 26.87 ? 42 GLU A CB 1 ATOM 259 C CG . GLU A 1 42 ? 17.497 13.621 37.180 1.00 49.27 ? 42 GLU A CG 1 ATOM 260 C CD . GLU A 1 42 ? 16.214 13.271 36.438 1.00 62.63 ? 42 GLU A CD 1 ATOM 261 O OE1 . GLU A 1 42 ? 16.013 13.848 35.349 1.00 102.86 ? 42 GLU A OE1 1 ATOM 262 O OE2 . GLU A 1 42 ? 15.442 12.451 36.967 1.00 68.92 ? 42 GLU A OE2 1 ATOM 263 N N . PRO A 1 43 ? 20.238 15.888 37.666 1.00 21.66 ? 43 PRO A N 1 ATOM 264 C CA . PRO A 1 43 ? 21.063 16.853 36.932 1.00 20.46 ? 43 PRO A CA 1 ATOM 265 C C . PRO A 1 43 ? 20.266 17.386 35.751 1.00 25.71 ? 43 PRO A C 1 ATOM 266 O O . PRO A 1 43 ? 19.656 16.556 35.068 1.00 23.53 ? 43 PRO A O 1 ATOM 267 C CB . PRO A 1 43 ? 22.254 16.048 36.425 1.00 27.70 ? 43 PRO A CB 1 ATOM 268 C CG . PRO A 1 43 ? 22.175 14.721 37.080 1.00 32.51 ? 43 PRO A CG 1 ATOM 269 C CD . PRO A 1 43 ? 20.790 14.524 37.623 1.00 26.71 ? 43 PRO A CD 1 ATOM 270 N N . PHE A 1 44 ? 20.239 18.690 35.515 1.00 13.57 ? 44 PHE A N 1 ATOM 271 C CA . PHE A 1 44 ? 19.424 19.209 34.394 1.00 14.12 ? 44 PHE A CA 1 ATOM 272 C C . PHE A 1 44 ? 20.243 19.930 33.347 1.00 20.16 ? 44 PHE A C 1 ATOM 273 O O . PHE A 1 44 ? 20.034 19.802 32.137 1.00 20.39 ? 44 PHE A O 1 ATOM 274 C CB . PHE A 1 44 ? 18.386 20.147 35.004 1.00 13.52 ? 44 PHE A CB 1 ATOM 275 C CG . PHE A 1 44 ? 17.456 20.778 33.990 1.00 16.60 ? 44 PHE A CG 1 ATOM 276 C CD1 . PHE A 1 44 ? 16.416 20.044 33.439 1.00 22.07 ? 44 PHE A CD1 1 ATOM 277 C CD2 . PHE A 1 44 ? 17.642 22.100 33.616 1.00 22.46 ? 44 PHE A CD2 1 ATOM 278 C CE1 . PHE A 1 44 ? 15.566 20.638 32.516 1.00 16.23 ? 44 PHE A CE1 1 ATOM 279 C CE2 . PHE A 1 44 ? 16.782 22.705 32.719 1.00 23.04 ? 44 PHE A CE2 1 ATOM 280 C CZ . PHE A 1 44 ? 15.732 21.966 32.199 1.00 19.49 ? 44 PHE A CZ 1 ATOM 281 N N . ALA A 1 45 ? 21.235 20.716 33.783 1.00 14.13 ? 45 ALA A N 1 ATOM 282 C CA . ALA A 1 45 ? 22.087 21.461 32.872 1.00 11.65 ? 45 ALA A CA 1 ATOM 283 C C . ALA A 1 45 ? 23.287 22.032 33.638 1.00 19.06 ? 45 ALA A C 1 ATOM 284 O O . ALA A 1 45 ? 23.188 22.201 34.849 1.00 16.84 ? 45 ALA A O 1 ATOM 285 C CB . ALA A 1 45 ? 21.352 22.621 32.224 1.00 13.75 ? 45 ALA A CB 1 ATOM 286 N N . SER A 1 46 ? 24.386 22.335 32.945 1.00 15.40 ? 46 SER A N 1 ATOM 287 C CA . SER A 1 46 ? 25.509 22.945 33.673 1.00 10.84 ? 46 SER A CA 1 ATOM 288 C C . SER A 1 46 ? 26.273 23.818 32.700 1.00 9.39 ? 46 SER A C 1 ATOM 289 O O . SER A 1 46 ? 26.083 23.779 31.487 1.00 13.25 ? 46 SER A O 1 ATOM 290 C CB . SER A 1 46 ? 26.413 21.886 34.294 1.00 15.95 ? 46 SER A CB 1 ATOM 291 O OG . SER A 1 46 ? 27.022 21.139 33.238 1.00 15.49 ? 46 SER A OG 1 ATOM 292 N N . GLY A 1 47 ? 27.172 24.648 33.223 1.00 13.75 ? 47 GLY A N 1 ATOM 293 C CA . GLY A 1 47 ? 27.900 25.559 32.323 1.00 13.93 ? 47 GLY A CA 1 ATOM 294 C C . GLY A 1 47 ? 28.770 26.511 33.150 1.00 12.78 ? 47 GLY A C 1 ATOM 295 O O . GLY A 1 47 ? 28.769 26.423 34.375 1.00 14.75 ? 47 GLY A O 1 ATOM 296 N N . LYS A 1 48 ? 29.487 27.397 32.466 1.00 14.28 ? 48 LYS A N 1 ATOM 297 C CA . LYS A 1 48 ? 30.382 28.357 33.093 1.00 15.69 ? 48 LYS A CA 1 ATOM 298 C C . LYS A 1 48 ? 30.002 29.748 32.620 1.00 12.33 ? 48 LYS A C 1 ATOM 299 O O . LYS A 1 48 ? 29.642 29.896 31.457 1.00 15.45 ? 48 LYS A O 1 ATOM 300 C CB . LYS A 1 48 ? 31.844 28.145 32.682 1.00 23.02 ? 48 LYS A CB 1 ATOM 301 C CG . LYS A 1 48 ? 32.672 27.254 33.589 1.00 35.69 ? 48 LYS A CG 1 ATOM 302 C CD . LYS A 1 48 ? 34.142 27.354 33.178 1.00 54.47 ? 48 LYS A CD 1 ATOM 303 C CE . LYS A 1 48 ? 34.858 26.018 33.263 1.00 56.87 ? 48 LYS A CE 1 ATOM 304 N NZ . LYS A 1 48 ? 34.853 25.446 34.640 1.00 35.17 ? 48 LYS A NZ 1 ATOM 305 N N . THR A 1 49 ? 30.086 30.746 33.497 1.00 13.03 ? 49 THR A N 1 ATOM 306 C CA . THR A 1 49 ? 29.774 32.074 32.965 1.00 12.26 ? 49 THR A CA 1 ATOM 307 C C . THR A 1 49 ? 30.852 32.580 32.019 1.00 14.25 ? 49 THR A C 1 ATOM 308 O O . THR A 1 49 ? 32.038 32.285 32.196 1.00 15.96 ? 49 THR A O 1 ATOM 309 C CB . THR A 1 49 ? 29.636 33.116 34.099 1.00 14.66 ? 49 THR A CB 1 ATOM 310 O OG1 . THR A 1 49 ? 30.834 33.128 34.895 1.00 11.95 ? 49 THR A OG1 1 ATOM 311 C CG2 . THR A 1 49 ? 28.484 32.744 35.028 1.00 14.73 ? 49 THR A CG2 1 ATOM 312 N N . SER A 1 50 ? 30.385 33.360 31.061 1.00 16.13 ? 50 SER A N 1 ATOM 313 C CA . SER A 1 50 ? 31.186 34.012 30.040 1.00 20.44 ? 50 SER A CA 1 ATOM 314 C C . SER A 1 50 ? 31.915 35.235 30.588 1.00 21.54 ? 50 SER A C 1 ATOM 315 O O . SER A 1 50 ? 31.824 35.582 31.762 1.00 15.80 ? 50 SER A O 1 ATOM 316 C CB . SER A 1 50 ? 30.287 34.482 28.882 1.00 17.42 ? 50 SER A CB 1 ATOM 317 O OG . SER A 1 50 ? 29.538 35.596 29.370 1.00 21.68 ? 50 SER A OG 1 ATOM 318 N N . GLU A 1 51 ? 32.643 35.890 29.679 1.00 21.47 ? 51 GLU A N 1 ATOM 319 C CA . GLU A 1 51 ? 33.402 37.065 30.103 1.00 25.79 ? 51 GLU A CA 1 ATOM 320 C C . GLU A 1 51 ? 32.470 38.191 30.501 1.00 19.19 ? 51 GLU A C 1 ATOM 321 O O . GLU A 1 51 ? 32.910 39.131 31.167 1.00 24.24 ? 51 GLU A O 1 ATOM 322 C CB . GLU A 1 51 ? 34.352 37.486 28.972 1.00 38.52 ? 51 GLU A CB 1 ATOM 323 C CG . GLU A 1 51 ? 35.729 36.829 29.131 1.00 52.20 ? 51 GLU A CG 1 ATOM 324 C CD . GLU A 1 51 ? 36.776 37.545 28.300 1.00 66.86 ? 51 GLU A CD 1 ATOM 325 O OE1 . GLU A 1 51 ? 37.555 38.341 28.863 1.00 89.35 ? 51 GLU A OE1 1 ATOM 326 O OE2 . GLU A 1 51 ? 36.806 37.305 27.074 1.00 88.25 ? 51 GLU A OE2 1 ATOM 327 N N . SER A 1 52 ? 31.184 38.138 30.113 1.00 16.48 ? 52 SER A N 1 ATOM 328 C CA . SER A 1 52 ? 30.243 39.143 30.596 1.00 18.35 ? 52 SER A CA 1 ATOM 329 C C . SER A 1 52 ? 29.528 38.689 31.868 1.00 16.57 ? 52 SER A C 1 ATOM 330 O O . SER A 1 52 ? 28.578 39.370 32.276 1.00 18.16 ? 52 SER A O 1 ATOM 331 C CB . SER A 1 52 ? 29.200 39.509 29.527 1.00 24.42 ? 52 SER A CB 1 ATOM 332 O OG . SER A 1 52 ? 28.436 38.364 29.192 1.00 32.09 ? 52 SER A OG 1 ATOM 333 N N . GLY A 1 53 ? 29.959 37.596 32.490 1.00 13.37 ? 53 GLY A N 1 ATOM 334 C CA . GLY A 1 53 ? 29.349 37.120 33.726 1.00 13.33 ? 53 GLY A CA 1 ATOM 335 C C . GLY A 1 53 ? 28.012 36.425 33.513 1.00 14.92 ? 53 GLY A C 1 ATOM 336 O O . GLY A 1 53 ? 27.243 36.185 34.445 1.00 16.50 ? 53 GLY A O 1 ATOM 337 N N . GLU A 1 54 ? 27.702 36.063 32.265 1.00 14.72 ? 54 GLU A N 1 ATOM 338 C CA . GLU A 1 54 ? 26.428 35.480 31.893 1.00 12.06 ? 54 GLU A CA 1 ATOM 339 C C . GLU A 1 54 ? 26.529 34.027 31.468 1.00 20.95 ? 54 GLU A C 1 ATOM 340 O O . GLU A 1 54 ? 27.553 33.597 30.947 1.00 17.26 ? 54 GLU A O 1 ATOM 341 C CB . GLU A 1 54 ? 25.815 36.308 30.744 1.00 19.20 ? 54 GLU A CB 1 ATOM 342 C CG . GLU A 1 54 ? 25.719 37.769 31.180 1.00 38.51 ? 54 GLU A CG 1 ATOM 343 C CD . GLU A 1 54 ? 25.044 38.685 30.176 1.00 54.91 ? 54 GLU A CD 1 ATOM 344 O OE1 . GLU A 1 54 ? 25.077 38.407 28.956 1.00 40.40 ? 54 GLU A OE1 1 ATOM 345 O OE2 . GLU A 1 54 ? 24.483 39.705 30.638 1.00 60.43 ? 54 GLU A OE2 1 ATOM 346 N N . LEU A 1 55 ? 25.418 33.325 31.718 1.00 16.46 ? 55 LEU A N 1 ATOM 347 C CA . LEU A 1 55 ? 25.249 31.964 31.218 1.00 13.08 ? 55 LEU A CA 1 ATOM 348 C C . LEU A 1 55 ? 23.867 31.850 30.573 1.00 15.57 ? 55 LEU A C 1 ATOM 349 O O . LEU A 1 55 ? 22.856 32.123 31.222 1.00 19.14 ? 55 LEU A O 1 ATOM 350 C CB . LEU A 1 55 ? 25.458 30.979 32.359 1.00 14.50 ? 55 LEU A CB 1 ATOM 351 C CG . LEU A 1 55 ? 25.373 29.495 32.053 1.00 21.73 ? 55 LEU A CG 1 ATOM 352 C CD1 . LEU A 1 55 ? 26.383 29.113 30.984 1.00 18.47 ? 55 LEU A CD1 1 ATOM 353 C CD2 . LEU A 1 55 ? 25.575 28.708 33.339 1.00 16.49 ? 55 LEU A CD2 1 ATOM 354 N N . HIS A 1 56 ? 23.854 31.507 29.295 1.00 17.61 ? 56 HIS A N 1 ATOM 355 C CA . HIS A 1 56 ? 22.653 31.224 28.539 1.00 26.95 ? 56 HIS A CA 1 ATOM 356 C C . HIS A 1 56 ? 22.778 29.843 27.865 1.00 26.54 ? 56 HIS A C 1 ATOM 357 O O . HIS A 1 56 ? 23.783 29.143 27.951 1.00 23.00 ? 56 HIS A O 1 ATOM 358 C CB . HIS A 1 56 ? 22.327 32.217 27.437 1.00 40.92 ? 56 HIS A CB 1 ATOM 359 C CG . HIS A 1 56 ? 23.061 33.502 27.337 1.00 62.16 ? 56 HIS A CG 1 ATOM 360 N ND1 . HIS A 1 56 ? 24.217 33.648 26.600 1.00 72.01 ? 56 HIS A ND1 1 ATOM 361 C CD2 . HIS A 1 56 ? 22.794 34.723 27.868 1.00 66.18 ? 56 HIS A CD2 1 ATOM 362 C CE1 . HIS A 1 56 ? 24.637 34.899 26.692 1.00 76.16 ? 56 HIS A CE1 1 ATOM 363 N NE2 . HIS A 1 56 ? 23.791 35.571 27.456 1.00 72.60 ? 56 HIS A NE2 1 ATOM 364 N N . GLY A 1 57 ? 21.699 29.495 27.161 1.00 25.96 ? 57 GLY A N 1 ATOM 365 C CA . GLY A 1 57 ? 21.759 28.232 26.425 1.00 22.86 ? 57 GLY A CA 1 ATOM 366 C C . GLY A 1 57 ? 21.688 27.034 27.319 1.00 28.06 ? 57 GLY A C 1 ATOM 367 O O . GLY A 1 57 ? 22.037 25.927 26.912 1.00 23.44 ? 57 GLY A O 1 ATOM 368 N N . LEU A 1 58 ? 21.229 27.217 28.557 1.00 26.14 ? 58 LEU A N 1 ATOM 369 C CA . LEU A 1 58 ? 21.121 26.059 29.435 1.00 21.18 ? 58 LEU A CA 1 ATOM 370 C C . LEU A 1 58 ? 20.007 25.121 28.986 1.00 28.36 ? 58 LEU A C 1 ATOM 371 O O . LEU A 1 58 ? 20.078 23.905 29.159 1.00 23.47 ? 58 LEU A O 1 ATOM 372 C CB . LEU A 1 58 ? 20.852 26.523 30.862 1.00 24.98 ? 58 LEU A CB 1 ATOM 373 C CG . LEU A 1 58 ? 22.014 27.165 31.618 1.00 24.71 ? 58 LEU A CG 1 ATOM 374 C CD1 . LEU A 1 58 ? 21.563 27.643 32.985 1.00 26.03 ? 58 LEU A CD1 1 ATOM 375 C CD2 . LEU A 1 58 ? 23.191 26.219 31.780 1.00 24.13 ? 58 LEU A CD2 1 ATOM 376 N N . THR A 1 59 ? 18.928 25.671 28.417 1.00 20.90 ? 59 THR A N 1 ATOM 377 C CA . THR A 1 59 ? 17.798 24.768 28.157 1.00 18.37 ? 59 THR A CA 1 ATOM 378 C C . THR A 1 59 ? 16.921 25.362 27.073 1.00 25.94 ? 59 THR A C 1 ATOM 379 O O . THR A 1 59 ? 17.195 26.470 26.614 1.00 28.49 ? 59 THR A O 1 ATOM 380 C CB . THR A 1 59 ? 16.981 24.524 29.440 1.00 18.45 ? 59 THR A CB 1 ATOM 381 O OG1 . THR A 1 59 ? 15.921 23.599 29.135 1.00 21.06 ? 59 THR A OG1 1 ATOM 382 C CG2 . THR A 1 59 ? 16.319 25.797 29.929 1.00 15.53 ? 59 THR A CG2 1 ATOM 383 N N . THR A 1 60 ? 15.887 24.658 26.661 1.00 21.42 ? 60 THR A N 1 ATOM 384 C CA . THR A 1 60 ? 14.906 25.141 25.705 1.00 19.89 ? 60 THR A CA 1 ATOM 385 C C . THR A 1 60 ? 13.532 25.219 26.342 1.00 19.85 ? 60 THR A C 1 ATOM 386 O O . THR A 1 60 ? 13.248 24.610 27.368 1.00 25.68 ? 60 THR A O 1 ATOM 387 C CB . THR A 1 60 ? 14.847 24.190 24.490 1.00 27.12 ? 60 THR A CB 1 ATOM 388 O OG1 . THR A 1 60 ? 14.376 22.919 24.964 1.00 27.57 ? 60 THR A OG1 1 ATOM 389 C CG2 . THR A 1 60 ? 16.228 23.988 23.903 1.00 32.31 ? 60 THR A CG2 1 ATOM 390 N N . GLU A 1 61 ? 12.629 25.967 25.722 1.00 25.87 ? 61 GLU A N 1 ATOM 391 C CA . GLU A 1 61 ? 11.266 26.060 26.246 1.00 25.36 ? 61 GLU A CA 1 ATOM 392 C C . GLU A 1 61 ? 10.644 24.673 26.353 1.00 23.81 ? 61 GLU A C 1 ATOM 393 O O . GLU A 1 61 ? 10.011 24.336 27.356 1.00 29.10 ? 61 GLU A O 1 ATOM 394 C CB . GLU A 1 61 ? 10.426 26.970 25.347 1.00 34.39 ? 61 GLU A CB 1 ATOM 395 C CG . GLU A 1 61 ? 9.782 28.127 26.092 1.00 64.25 ? 61 GLU A CG 1 ATOM 396 C CD . GLU A 1 61 ? 8.862 28.972 25.228 1.00 77.91 ? 61 GLU A CD 1 ATOM 397 O OE1 . GLU A 1 61 ? 9.262 30.100 24.865 1.00 88.56 ? 61 GLU A OE1 1 ATOM 398 O OE2 . GLU A 1 61 ? 7.743 28.498 24.930 1.00 81.78 ? 61 GLU A OE2 1 ATOM 399 N N . GLU A 1 62 ? 10.844 23.872 25.310 1.00 21.62 ? 62 GLU A N 1 ATOM 400 C CA . GLU A 1 62 ? 10.294 22.516 25.284 1.00 23.12 ? 62 GLU A CA 1 ATOM 401 C C . GLU A 1 62 ? 10.764 21.674 26.446 1.00 20.29 ? 62 GLU A C 1 ATOM 402 O O . GLU A 1 62 ? 9.984 20.961 27.069 1.00 24.17 ? 62 GLU A O 1 ATOM 403 C CB . GLU A 1 62 ? 10.677 21.836 23.953 1.00 25.53 ? 62 GLU A CB 1 ATOM 404 C CG . GLU A 1 62 ? 10.299 20.361 23.914 1.00 44.65 ? 62 GLU A CG 1 ATOM 405 C CD . GLU A 1 62 ? 8.824 20.151 23.627 1.00 74.69 ? 62 GLU A CD 1 ATOM 406 O OE1 . GLU A 1 62 ? 8.258 20.930 22.825 1.00 105.19 ? 62 GLU A OE1 1 ATOM 407 O OE2 . GLU A 1 62 ? 8.215 19.214 24.195 1.00 90.64 ? 62 GLU A OE2 1 ATOM 408 N N . GLU A 1 63 ? 12.060 21.705 26.798 1.00 19.21 ? 63 GLU A N 1 ATOM 409 C CA . GLU A 1 63 ? 12.546 20.855 27.869 1.00 13.91 ? 63 GLU A CA 1 ATOM 410 C C . GLU A 1 63 ? 12.289 21.405 29.271 1.00 15.32 ? 63 GLU A C 1 ATOM 411 O O . GLU A 1 63 ? 12.289 20.689 30.270 1.00 16.92 ? 63 GLU A O 1 ATOM 412 C CB . GLU A 1 63 ? 14.080 20.675 27.739 1.00 21.32 ? 63 GLU A CB 1 ATOM 413 C CG . GLU A 1 63 ? 14.624 19.588 28.656 1.00 43.12 ? 63 GLU A CG 1 ATOM 414 C CD . GLU A 1 63 ? 15.881 18.944 28.090 1.00 62.50 ? 63 GLU A CD 1 ATOM 415 O OE1 . GLU A 1 63 ? 16.229 19.300 26.937 1.00 51.58 ? 63 GLU A OE1 1 ATOM 416 O OE2 . GLU A 1 63 ? 16.503 18.116 28.794 1.00 57.17 ? 63 GLU A OE2 1 ATOM 417 N N . PHE A 1 64 ? 12.086 22.725 29.311 1.00 14.82 ? 64 PHE A N 1 ATOM 418 C CA . PHE A 1 64 ? 11.977 23.428 30.591 1.00 12.90 ? 64 PHE A CA 1 ATOM 419 C C . PHE A 1 64 ? 10.534 23.353 31.108 1.00 16.60 ? 64 PHE A C 1 ATOM 420 O O . PHE A 1 64 ? 9.804 24.335 31.072 1.00 17.80 ? 64 PHE A O 1 ATOM 421 C CB . PHE A 1 64 ? 12.456 24.855 30.398 1.00 10.80 ? 64 PHE A CB 1 ATOM 422 C CG . PHE A 1 64 ? 12.667 25.676 31.686 1.00 15.60 ? 64 PHE A CG 1 ATOM 423 C CD1 . PHE A 1 64 ? 13.115 25.088 32.852 1.00 11.44 ? 64 PHE A CD1 1 ATOM 424 C CD2 . PHE A 1 64 ? 12.416 27.033 31.711 1.00 20.10 ? 64 PHE A CD2 1 ATOM 425 C CE1 . PHE A 1 64 ? 13.326 25.809 34.020 1.00 19.51 ? 64 PHE A CE1 1 ATOM 426 C CE2 . PHE A 1 64 ? 12.640 27.783 32.870 1.00 17.96 ? 64 PHE A CE2 1 ATOM 427 C CZ . PHE A 1 64 ? 13.099 27.182 34.014 1.00 18.73 ? 64 PHE A CZ 1 ATOM 428 N N . VAL A 1 65 ? 10.127 22.189 31.581 1.00 17.12 ? 65 VAL A N 1 ATOM 429 C CA . VAL A 1 65 ? 8.739 21.958 31.985 1.00 15.61 ? 65 VAL A CA 1 ATOM 430 C C . VAL A 1 65 ? 8.498 22.473 33.379 1.00 14.47 ? 65 VAL A C 1 ATOM 431 O O . VAL A 1 65 ? 9.451 22.864 34.066 1.00 13.24 ? 65 VAL A O 1 ATOM 432 C CB . VAL A 1 65 ? 8.415 20.446 31.931 1.00 19.20 ? 65 VAL A CB 1 ATOM 433 C CG1 . VAL A 1 65 ? 8.487 20.014 30.475 1.00 17.96 ? 65 VAL A CG1 1 ATOM 434 C CG2 . VAL A 1 65 ? 9.352 19.623 32.798 1.00 20.12 ? 65 VAL A CG2 1 ATOM 435 N N . GLU A 1 66 ? 7.248 22.447 33.785 1.00 11.43 ? 66 GLU A N 1 ATOM 436 C CA . GLU A 1 66 ? 6.894 22.746 35.170 1.00 15.04 ? 66 GLU A CA 1 ATOM 437 C C . GLU A 1 66 ? 7.722 21.963 36.144 1.00 16.40 ? 66 GLU A C 1 ATOM 438 O O . GLU A 1 66 ? 7.972 20.754 35.962 1.00 17.09 ? 66 GLU A O 1 ATOM 439 C CB . GLU A 1 66 ? 5.435 22.325 35.402 1.00 19.50 ? 66 GLU A CB 1 ATOM 440 C CG . GLU A 1 66 ? 4.485 23.160 36.199 1.00 39.56 ? 66 GLU A CG 1 ATOM 441 C CD . GLU A 1 66 ? 3.097 22.529 36.289 1.00 50.28 ? 66 GLU A CD 1 ATOM 442 O OE1 . GLU A 1 66 ? 2.459 22.255 35.246 1.00 41.74 ? 66 GLU A OE1 1 ATOM 443 O OE2 . GLU A 1 66 ? 2.658 22.301 37.439 1.00 75.63 ? 66 GLU A OE2 1 ATOM 444 N N . GLY A 1 67 ? 8.144 22.579 37.260 1.00 13.09 ? 67 GLY A N 1 ATOM 445 C CA . GLY A 1 67 ? 8.839 21.753 38.241 1.00 14.47 ? 67 GLY A CA 1 ATOM 446 C C . GLY A 1 67 ? 9.566 22.662 39.248 1.00 17.87 ? 67 GLY A C 1 ATOM 447 O O . GLY A 1 67 ? 9.413 23.875 39.176 1.00 17.34 ? 67 GLY A O 1 ATOM 448 N N . ILE A 1 68 ? 10.298 22.018 40.129 1.00 15.40 ? 68 ILE A N 1 ATOM 449 C CA . ILE A 1 68 ? 11.102 22.725 41.132 1.00 15.03 ? 68 ILE A CA 1 ATOM 450 C C . ILE A 1 68 ? 12.561 22.606 40.671 1.00 17.44 ? 68 ILE A C 1 ATOM 451 O O . ILE A 1 68 ? 13.021 21.480 40.426 1.00 16.13 ? 68 ILE A O 1 ATOM 452 C CB . ILE A 1 68 ? 10.898 22.153 42.537 1.00 17.43 ? 68 ILE A CB 1 ATOM 453 C CG1 . ILE A 1 68 ? 9.442 22.258 43.017 1.00 24.34 ? 68 ILE A CG1 1 ATOM 454 C CG2 . ILE A 1 68 ? 11.838 22.809 43.545 1.00 18.43 ? 68 ILE A CG2 1 ATOM 455 C CD1 . ILE A 1 68 ? 9.212 21.608 44.366 1.00 33.23 ? 68 ILE A CD1 1 ATOM 456 N N . TYR A 1 69 ? 13.203 23.756 40.514 1.00 14.99 ? 69 TYR A N 1 ATOM 457 C CA . TYR A 1 69 ? 14.570 23.767 40.002 1.00 12.34 ? 69 TYR A CA 1 ATOM 458 C C . TYR A 1 69 ? 15.517 24.306 41.070 1.00 14.96 ? 69 TYR A C 1 ATOM 459 O O . TYR A 1 69 ? 15.098 25.107 41.896 1.00 12.64 ? 69 TYR A O 1 ATOM 460 C CB . TYR A 1 69 ? 14.669 24.607 38.723 1.00 11.22 ? 69 TYR A CB 1 ATOM 461 C CG . TYR A 1 69 ? 13.973 23.905 37.565 1.00 17.57 ? 69 TYR A CG 1 ATOM 462 C CD1 . TYR A 1 69 ? 12.583 24.026 37.429 1.00 10.69 ? 69 TYR A CD1 1 ATOM 463 C CD2 . TYR A 1 69 ? 14.696 23.152 36.654 1.00 17.28 ? 69 TYR A CD2 1 ATOM 464 C CE1 . TYR A 1 69 ? 11.935 23.389 36.376 1.00 13.43 ? 69 TYR A CE1 1 ATOM 465 C CE2 . TYR A 1 69 ? 14.036 22.513 35.600 1.00 20.07 ? 69 TYR A CE2 1 ATOM 466 C CZ . TYR A 1 69 ? 12.673 22.630 35.473 1.00 20.40 ? 69 TYR A CZ 1 ATOM 467 O OH . TYR A 1 69 ? 12.016 22.010 34.426 1.00 19.00 ? 69 TYR A OH 1 ATOM 468 N N . LYS A 1 70 ? 16.765 23.848 41.011 1.00 11.89 ? 70 LYS A N 1 ATOM 469 C CA . LYS A 1 70 ? 17.792 24.391 41.893 1.00 9.98 ? 70 LYS A CA 1 ATOM 470 C C . LYS A 1 70 ? 18.984 24.841 41.057 1.00 15.51 ? 70 LYS A C 1 ATOM 471 O O . LYS A 1 70 ? 19.516 24.064 40.276 1.00 14.29 ? 70 LYS A O 1 ATOM 472 C CB . LYS A 1 70 ? 18.215 23.330 42.910 1.00 14.80 ? 70 LYS A CB 1 ATOM 473 C CG . LYS A 1 70 ? 19.356 23.850 43.788 1.00 18.63 ? 70 LYS A CG 1 ATOM 474 C CD . LYS A 1 70 ? 19.493 23.051 45.061 1.00 27.33 ? 70 LYS A CD 1 ATOM 475 C CE . LYS A 1 70 ? 19.979 21.641 44.786 1.00 37.66 ? 70 LYS A CE 1 ATOM 476 N NZ . LYS A 1 70 ? 20.769 21.120 45.945 1.00 50.37 ? 70 LYS A NZ 1 ATOM 477 N N . VAL A 1 71 ? 19.406 26.086 41.198 1.00 11.51 ? 71 VAL A N 1 ATOM 478 C CA . VAL A 1 71 ? 20.576 26.602 40.511 1.00 13.76 ? 71 VAL A CA 1 ATOM 479 C C . VAL A 1 71 ? 21.660 26.705 41.576 1.00 16.04 ? 71 VAL A C 1 ATOM 480 O O . VAL A 1 71 ? 21.446 27.464 42.535 1.00 14.31 ? 71 VAL A O 1 ATOM 481 C CB . VAL A 1 71 ? 20.330 27.990 39.893 1.00 17.36 ? 71 VAL A CB 1 ATOM 482 C CG1 . VAL A 1 71 ? 21.579 28.571 39.229 1.00 9.78 ? 71 VAL A CG1 1 ATOM 483 C CG2 . VAL A 1 71 ? 19.174 27.898 38.915 1.00 14.80 ? 71 VAL A CG2 1 ATOM 484 N N . GLU A 1 72 ? 22.740 25.964 41.383 1.00 11.01 ? 72 GLU A N 1 ATOM 485 C CA . GLU A 1 72 ? 23.826 26.009 42.361 1.00 11.08 ? 72 GLU A CA 1 ATOM 486 C C . GLU A 1 72 ? 25.008 26.736 41.721 1.00 14.95 ? 72 GLU A C 1 ATOM 487 O O . GLU A 1 72 ? 25.434 26.339 40.639 1.00 15.12 ? 72 GLU A O 1 ATOM 488 C CB . GLU A 1 72 ? 24.227 24.607 42.779 1.00 17.03 ? 72 GLU A CB 1 ATOM 489 C CG . GLU A 1 72 ? 25.292 24.462 43.849 1.00 26.75 ? 72 GLU A CG 1 ATOM 490 C CD . GLU A 1 72 ? 25.325 22.988 44.272 1.00 41.27 ? 72 GLU A CD 1 ATOM 491 O OE1 . GLU A 1 72 ? 24.480 22.596 45.100 1.00 51.97 ? 72 GLU A OE1 1 ATOM 492 O OE2 . GLU A 1 72 ? 26.183 22.265 43.727 1.00 62.18 ? 72 GLU A OE2 1 ATOM 493 N N . ILE A 1 73 ? 25.490 27.771 42.394 1.00 17.30 ? 73 ILE A N 1 ATOM 494 C CA . ILE A 1 73 ? 26.624 28.520 41.812 1.00 11.12 ? 73 ILE A CA 1 ATOM 495 C C . ILE A 1 73 ? 27.863 28.264 42.650 1.00 13.69 ? 73 ILE A C 1 ATOM 496 O O . ILE A 1 73 ? 27.801 28.484 43.855 1.00 10.63 ? 73 ILE A O 1 ATOM 497 C CB . ILE A 1 73 ? 26.258 30.015 41.790 1.00 18.46 ? 73 ILE A CB 1 ATOM 498 C CG1 . ILE A 1 73 ? 24.928 30.280 41.054 1.00 17.50 ? 73 ILE A CG1 1 ATOM 499 C CG2 . ILE A 1 73 ? 27.413 30.819 41.222 1.00 24.72 ? 73 ILE A CG2 1 ATOM 500 C CD1 . ILE A 1 73 ? 24.411 31.695 41.251 1.00 17.59 ? 73 ILE A CD1 1 ATOM 501 N N . ASP A 1 74 ? 28.957 27.802 42.031 1.00 11.53 ? 74 ASP A N 1 ATOM 502 C CA . ASP A 1 74 ? 30.127 27.449 42.845 1.00 15.96 ? 74 ASP A CA 1 ATOM 503 C C . ASP A 1 74 ? 30.949 28.690 43.158 1.00 16.42 ? 74 ASP A C 1 ATOM 504 O O . ASP A 1 74 ? 31.972 28.977 42.542 1.00 15.58 ? 74 ASP A O 1 ATOM 505 C CB . ASP A 1 74 ? 30.988 26.397 42.151 1.00 19.86 ? 74 ASP A CB 1 ATOM 506 C CG . ASP A 1 74 ? 32.250 26.055 42.930 1.00 36.25 ? 74 ASP A CG 1 ATOM 507 O OD1 . ASP A 1 74 ? 32.391 26.434 44.118 1.00 27.37 ? 74 ASP A OD1 1 ATOM 508 O OD2 . ASP A 1 74 ? 33.130 25.380 42.352 1.00 36.10 ? 74 ASP A OD2 1 ATOM 509 N N . THR A 1 75 ? 30.491 29.428 44.170 1.00 14.41 ? 75 THR A N 1 ATOM 510 C CA . THR A 1 75 ? 31.201 30.651 44.533 1.00 13.78 ? 75 THR A CA 1 ATOM 511 C C . THR A 1 75 ? 32.530 30.386 45.224 1.00 15.76 ? 75 THR A C 1 ATOM 512 O O . THR A 1 75 ? 33.441 31.211 45.103 1.00 14.99 ? 75 THR A O 1 ATOM 513 C CB . THR A 1 75 ? 30.276 31.483 45.446 1.00 13.11 ? 75 THR A CB 1 ATOM 514 O OG1 . THR A 1 75 ? 29.921 30.680 46.562 1.00 13.31 ? 75 THR A OG1 1 ATOM 515 C CG2 . THR A 1 75 ? 29.029 31.843 44.637 1.00 13.17 ? 75 THR A CG2 1 ATOM 516 N N . LYS A 1 76 ? 32.634 29.256 45.917 1.00 14.71 ? 76 LYS A N 1 ATOM 517 C CA . LYS A 1 76 ? 33.847 28.962 46.689 1.00 18.34 ? 76 LYS A CA 1 ATOM 518 C C . LYS A 1 76 ? 35.069 28.869 45.777 1.00 18.26 ? 76 LYS A C 1 ATOM 519 O O . LYS A 1 76 ? 36.094 29.500 46.043 1.00 17.71 ? 76 LYS A O 1 ATOM 520 C CB . LYS A 1 76 ? 33.665 27.671 47.495 1.00 16.46 ? 76 LYS A CB 1 ATOM 521 C CG . LYS A 1 76 ? 34.903 27.380 48.351 1.00 21.72 ? 76 LYS A CG 1 ATOM 522 C CD . LYS A 1 76 ? 34.655 26.169 49.239 1.00 31.32 ? 76 LYS A CD 1 ATOM 523 C CE . LYS A 1 76 ? 35.391 26.339 50.556 1.00 47.43 ? 76 LYS A CE 1 ATOM 524 N NZ . LYS A 1 76 ? 35.260 25.132 51.424 1.00 42.14 ? 76 LYS A NZ 1 ATOM 525 N N . SER A 1 77 ? 35.005 28.128 44.677 1.00 16.97 ? 77 SER A N 1 ATOM 526 C CA . SER A 1 77 ? 36.132 28.007 43.758 1.00 19.54 ? 77 SER A CA 1 ATOM 527 C C . SER A 1 77 ? 36.499 29.339 43.123 1.00 19.25 ? 77 SER A C 1 ATOM 528 O O . SER A 1 77 ? 37.670 29.645 42.848 1.00 18.79 ? 77 SER A O 1 ATOM 529 C CB . SER A 1 77 ? 35.844 27.009 42.614 1.00 18.21 ? 77 SER A CB 1 ATOM 530 O OG . SER A 1 77 ? 35.540 25.749 43.170 1.00 29.40 ? 77 SER A OG 1 ATOM 531 N N . TYR A 1 78 ? 35.473 30.144 42.839 1.00 17.95 ? 78 TYR A N 1 ATOM 532 C CA . TYR A 1 78 ? 35.725 31.485 42.296 1.00 17.03 ? 78 TYR A CA 1 ATOM 533 C C . TYR A 1 78 ? 36.592 32.325 43.220 1.00 17.25 ? 78 TYR A C 1 ATOM 534 O O . TYR A 1 78 ? 37.594 32.950 42.841 1.00 17.84 ? 78 TYR A O 1 ATOM 535 C CB . TYR A 1 78 ? 34.388 32.205 42.033 1.00 18.73 ? 78 TYR A CB 1 ATOM 536 C CG . TYR A 1 78 ? 34.571 33.627 41.525 1.00 17.97 ? 78 TYR A CG 1 ATOM 537 C CD1 . TYR A 1 78 ? 34.911 33.880 40.205 1.00 14.84 ? 78 TYR A CD1 1 ATOM 538 C CD2 . TYR A 1 78 ? 34.403 34.732 42.367 1.00 13.51 ? 78 TYR A CD2 1 ATOM 539 C CE1 . TYR A 1 78 ? 35.092 35.160 39.694 1.00 13.17 ? 78 TYR A CE1 1 ATOM 540 C CE2 . TYR A 1 78 ? 34.573 36.004 41.872 1.00 15.56 ? 78 TYR A CE2 1 ATOM 541 C CZ . TYR A 1 78 ? 34.907 36.216 40.553 1.00 16.05 ? 78 TYR A CZ 1 ATOM 542 O OH . TYR A 1 78 ? 35.083 37.491 40.072 1.00 20.74 ? 78 TYR A OH 1 ATOM 543 N N . TRP A 1 79 ? 36.225 32.419 44.499 1.00 13.42 ? 79 TRP A N 1 ATOM 544 C CA . TRP A 1 79 ? 37.004 33.233 45.435 1.00 12.40 ? 79 TRP A CA 1 ATOM 545 C C . TRP A 1 79 ? 38.370 32.618 45.730 1.00 17.33 ? 79 TRP A C 1 ATOM 546 O O . TRP A 1 79 ? 39.340 33.368 45.853 1.00 16.36 ? 79 TRP A O 1 ATOM 547 C CB . TRP A 1 79 ? 36.291 33.396 46.791 1.00 15.13 ? 79 TRP A CB 1 ATOM 548 C CG . TRP A 1 79 ? 35.087 34.289 46.629 1.00 11.96 ? 79 TRP A CG 1 ATOM 549 C CD1 . TRP A 1 79 ? 33.792 33.933 46.876 1.00 14.45 ? 79 TRP A CD1 1 ATOM 550 C CD2 . TRP A 1 79 ? 35.080 35.646 46.200 1.00 15.96 ? 79 TRP A CD2 1 ATOM 551 N NE1 . TRP A 1 79 ? 32.958 35.009 46.618 1.00 10.81 ? 79 TRP A NE1 1 ATOM 552 C CE2 . TRP A 1 79 ? 33.729 36.073 46.202 1.00 13.38 ? 79 TRP A CE2 1 ATOM 553 C CE3 . TRP A 1 79 ? 36.070 36.559 45.813 1.00 18.32 ? 79 TRP A CE3 1 ATOM 554 C CZ2 . TRP A 1 79 ? 33.346 37.357 45.834 1.00 13.77 ? 79 TRP A CZ2 1 ATOM 555 C CZ3 . TRP A 1 79 ? 35.675 37.831 45.446 1.00 19.16 ? 79 TRP A CZ3 1 ATOM 556 C CH2 . TRP A 1 79 ? 34.331 38.238 45.451 1.00 13.76 ? 79 TRP A CH2 1 ATOM 557 N N . LYS A 1 80 ? 38.433 31.301 45.854 1.00 16.69 ? 80 LYS A N 1 ATOM 558 C CA . LYS A 1 80 ? 39.742 30.675 46.123 1.00 22.74 ? 80 LYS A CA 1 ATOM 559 C C . LYS A 1 80 ? 40.740 30.937 45.007 1.00 25.39 ? 80 LYS A C 1 ATOM 560 O O . LYS A 1 80 ? 41.934 31.153 45.255 1.00 22.54 ? 80 LYS A O 1 ATOM 561 C CB . LYS A 1 80 ? 39.552 29.166 46.357 1.00 19.76 ? 80 LYS A CB 1 ATOM 562 C CG . LYS A 1 80 ? 38.959 28.962 47.758 1.00 28.62 ? 80 LYS A CG 1 ATOM 563 C CD . LYS A 1 80 ? 39.359 27.643 48.377 1.00 45.41 ? 80 LYS A CD 1 ATOM 564 C CE . LYS A 1 80 ? 38.829 26.466 47.575 1.00 55.12 ? 80 LYS A CE 1 ATOM 565 N NZ . LYS A 1 80 ? 39.736 25.289 47.686 1.00 69.04 ? 80 LYS A NZ 1 ATOM 566 N N . ALA A 1 81 ? 40.278 30.937 43.764 1.00 26.09 ? 81 ALA A N 1 ATOM 567 C CA . ALA A 1 81 ? 41.157 31.209 42.630 1.00 31.14 ? 81 ALA A CA 1 ATOM 568 C C . ALA A 1 81 ? 41.665 32.646 42.671 1.00 42.17 ? 81 ALA A C 1 ATOM 569 O O . ALA A 1 81 ? 42.668 32.945 42.023 1.00 36.11 ? 81 ALA A O 1 ATOM 570 C CB . ALA A 1 81 ? 40.442 30.895 41.318 1.00 22.72 ? 81 ALA A CB 1 ATOM 571 N N . LEU A 1 82 ? 41.018 33.538 43.416 1.00 28.74 ? 82 LEU A N 1 ATOM 572 C CA . LEU A 1 82 ? 41.460 34.913 43.568 1.00 25.36 ? 82 LEU A CA 1 ATOM 573 C C . LEU A 1 82 ? 42.328 35.090 44.811 1.00 22.63 ? 82 LEU A C 1 ATOM 574 O O . LEU A 1 82 ? 42.767 36.184 45.154 1.00 30.51 ? 82 LEU A O 1 ATOM 575 C CB . LEU A 1 82 ? 40.253 35.856 43.673 1.00 28.39 ? 82 LEU A CB 1 ATOM 576 C CG . LEU A 1 82 ? 39.357 35.942 42.442 1.00 29.13 ? 82 LEU A CG 1 ATOM 577 C CD1 . LEU A 1 82 ? 38.371 37.092 42.581 1.00 33.43 ? 82 LEU A CD1 1 ATOM 578 C CD2 . LEU A 1 82 ? 40.209 36.090 41.186 1.00 36.78 ? 82 LEU A CD2 1 ATOM 579 N N . GLY A 1 83 ? 42.580 34.011 45.539 1.00 24.20 ? 83 GLY A N 1 ATOM 580 C CA . GLY A 1 83 ? 43.393 34.064 46.741 1.00 22.05 ? 83 GLY A CA 1 ATOM 581 C C . GLY A 1 83 ? 42.591 34.342 47.998 1.00 33.01 ? 83 GLY A C 1 ATOM 582 O O . GLY A 1 83 ? 43.159 34.584 49.064 1.00 26.40 ? 83 GLY A O 1 ATOM 583 N N . ILE A 1 84 ? 41.257 34.297 47.882 1.00 22.14 ? 84 ILE A N 1 ATOM 584 C CA . ILE A 1 84 ? 40.411 34.627 49.026 1.00 20.43 ? 84 ILE A CA 1 ATOM 585 C C . ILE A 1 84 ? 39.705 33.414 49.576 1.00 21.53 ? 84 ILE A C 1 ATOM 586 O O . ILE A 1 84 ? 39.188 32.557 48.848 1.00 23.32 ? 84 ILE A O 1 ATOM 587 C CB . ILE A 1 84 ? 39.375 35.695 48.594 1.00 23.06 ? 84 ILE A CB 1 ATOM 588 C CG1 . ILE A 1 84 ? 39.966 37.097 48.522 1.00 23.09 ? 84 ILE A CG1 1 ATOM 589 C CG2 . ILE A 1 84 ? 38.172 35.622 49.520 1.00 24.36 ? 84 ILE A CG2 1 ATOM 590 C CD1 . ILE A 1 84 ? 39.492 37.974 47.399 1.00 25.55 ? 84 ILE A CD1 1 ATOM 591 N N . SER A 1 85 ? 39.686 33.282 50.901 1.00 20.98 ? 85 SER A N 1 ATOM 592 C CA . SER A 1 85 ? 38.965 32.115 51.441 1.00 25.75 ? 85 SER A CA 1 ATOM 593 C C . SER A 1 85 ? 37.592 32.603 51.891 1.00 20.57 ? 85 SER A C 1 ATOM 594 O O . SER A 1 85 ? 37.440 33.341 52.847 1.00 20.63 ? 85 SER A O 1 ATOM 595 C CB . SER A 1 85 ? 39.789 31.448 52.532 1.00 38.75 ? 85 SER A CB 1 ATOM 596 O OG . SER A 1 85 ? 39.106 30.367 53.133 1.00 59.66 ? 85 SER A OG 1 ATOM 597 N N . PRO A 1 86 ? 36.527 32.232 51.179 1.00 17.11 ? 86 PRO A N 1 ATOM 598 C CA . PRO A 1 86 ? 35.194 32.788 51.459 1.00 16.12 ? 86 PRO A CA 1 ATOM 599 C C . PRO A 1 86 ? 34.360 32.004 52.457 1.00 19.82 ? 86 PRO A C 1 ATOM 600 O O . PRO A 1 86 ? 34.690 30.913 52.896 1.00 20.65 ? 86 PRO A O 1 ATOM 601 C CB . PRO A 1 86 ? 34.568 32.659 50.068 1.00 12.70 ? 86 PRO A CB 1 ATOM 602 C CG . PRO A 1 86 ? 35.070 31.334 49.599 1.00 22.44 ? 86 PRO A CG 1 ATOM 603 C CD . PRO A 1 86 ? 36.506 31.266 50.085 1.00 16.66 ? 86 PRO A CD 1 ATOM 604 N N . PHE A 1 87 ? 33.214 32.532 52.878 1.00 12.26 ? 87 PHE A N 1 ATOM 605 C CA . PHE A 1 87 ? 32.424 31.920 53.924 1.00 11.36 ? 87 PHE A CA 1 ATOM 606 C C . PHE A 1 87 ? 31.604 30.758 53.396 1.00 12.61 ? 87 PHE A C 1 ATOM 607 O O . PHE A 1 87 ? 31.547 29.690 53.981 1.00 12.33 ? 87 PHE A O 1 ATOM 608 C CB . PHE A 1 87 ? 31.446 32.973 54.503 1.00 10.86 ? 87 PHE A CB 1 ATOM 609 C CG . PHE A 1 87 ? 30.545 32.418 55.607 1.00 16.56 ? 87 PHE A CG 1 ATOM 610 C CD1 . PHE A 1 87 ? 31.069 32.170 56.862 1.00 19.95 ? 87 PHE A CD1 1 ATOM 611 C CD2 . PHE A 1 87 ? 29.213 32.159 55.380 1.00 16.72 ? 87 PHE A CD2 1 ATOM 612 C CE1 . PHE A 1 87 ? 30.259 31.652 57.867 1.00 20.15 ? 87 PHE A CE1 1 ATOM 613 C CE2 . PHE A 1 87 ? 28.401 31.637 56.369 1.00 19.55 ? 87 PHE A CE2 1 ATOM 614 C CZ . PHE A 1 87 ? 28.934 31.396 57.617 1.00 16.31 ? 87 PHE A CZ 1 ATOM 615 N N . HIS A 1 88 ? 30.908 30.992 52.271 1.00 14.10 ? 88 HIS A N 1 ATOM 616 C CA . HIS A 1 88 ? 29.961 29.991 51.786 1.00 13.38 ? 88 HIS A CA 1 ATOM 617 C C . HIS A 1 88 ? 30.594 28.949 50.875 1.00 16.57 ? 88 HIS A C 1 ATOM 618 O O . HIS A 1 88 ? 31.522 29.226 50.116 1.00 18.09 ? 88 HIS A O 1 ATOM 619 C CB . HIS A 1 88 ? 28.857 30.650 50.935 1.00 13.03 ? 88 HIS A CB 1 ATOM 620 C CG . HIS A 1 88 ? 28.138 31.749 51.646 1.00 13.28 ? 88 HIS A CG 1 ATOM 621 N ND1 . HIS A 1 88 ? 28.458 33.083 51.523 1.00 15.55 ? 88 HIS A ND1 1 ATOM 622 C CD2 . HIS A 1 88 ? 27.090 31.695 52.507 1.00 15.82 ? 88 HIS A CD2 1 ATOM 623 C CE1 . HIS A 1 88 ? 27.649 33.810 52.276 1.00 18.65 ? 88 HIS A CE1 1 ATOM 624 N NE2 . HIS A 1 88 ? 26.813 32.977 52.877 1.00 21.84 ? 88 HIS A NE2 1 ATOM 625 N N . GLU A 1 89 ? 30.021 27.744 50.927 1.00 13.89 ? 89 GLU A N 1 ATOM 626 C CA . GLU A 1 89 ? 30.459 26.689 50.025 1.00 14.72 ? 89 GLU A CA 1 ATOM 627 C C . GLU A 1 89 ? 29.981 26.950 48.600 1.00 16.13 ? 89 GLU A C 1 ATOM 628 O O . GLU A 1 89 ? 30.647 26.656 47.623 1.00 15.45 ? 89 GLU A O 1 ATOM 629 C CB . GLU A 1 89 ? 29.893 25.318 50.478 1.00 13.89 ? 89 GLU A CB 1 ATOM 630 C CG . GLU A 1 89 ? 30.541 24.851 51.765 1.00 19.37 ? 89 GLU A CG 1 ATOM 631 C CD . GLU A 1 89 ? 32.015 24.546 51.522 1.00 24.36 ? 89 GLU A CD 1 ATOM 632 O OE1 . GLU A 1 89 ? 32.272 23.745 50.622 1.00 27.23 ? 89 GLU A OE1 1 ATOM 633 O OE2 . GLU A 1 89 ? 32.878 25.119 52.208 1.00 26.41 ? 89 GLU A OE2 1 ATOM 634 N N . HIS A 1 90 ? 28.757 27.467 48.510 1.00 13.94 ? 90 HIS A N 1 ATOM 635 C CA . HIS A 1 90 ? 28.173 27.764 47.208 1.00 12.80 ? 90 HIS A CA 1 ATOM 636 C C . HIS A 1 90 ? 26.966 28.642 47.476 1.00 11.39 ? 90 HIS A C 1 ATOM 637 O O . HIS A 1 90 ? 26.668 28.840 48.640 1.00 18.56 ? 90 HIS A O 1 ATOM 638 C CB . HIS A 1 90 ? 27.802 26.538 46.388 1.00 15.24 ? 90 HIS A CB 1 ATOM 639 C CG . HIS A 1 90 ? 27.238 25.349 47.071 1.00 25.51 ? 90 HIS A CG 1 ATOM 640 N ND1 . HIS A 1 90 ? 25.986 25.344 47.650 1.00 38.34 ? 90 HIS A ND1 1 ATOM 641 C CD2 . HIS A 1 90 ? 27.742 24.103 47.255 1.00 34.62 ? 90 HIS A CD2 1 ATOM 642 C CE1 . HIS A 1 90 ? 25.744 24.152 48.168 1.00 32.82 ? 90 HIS A CE1 1 ATOM 643 N NE2 . HIS A 1 90 ? 26.797 23.386 47.945 1.00 36.33 ? 90 HIS A NE2 1 ATOM 644 N N . ALA A 1 91 ? 26.378 29.123 46.389 1.00 12.65 ? 91 ALA A N 1 ATOM 645 C CA . ALA A 1 91 ? 25.140 29.889 46.486 1.00 15.45 ? 91 ALA A CA 1 ATOM 646 C C . ALA A 1 91 ? 24.069 29.026 45.837 1.00 22.23 ? 91 ALA A C 1 ATOM 647 O O . ALA A 1 91 ? 24.374 28.498 44.771 1.00 20.03 ? 91 ALA A O 1 ATOM 648 C CB . ALA A 1 91 ? 25.286 31.238 45.803 1.00 17.08 ? 91 ALA A CB 1 ATOM 649 N N . GLU A 1 92 ? 22.906 28.886 46.438 1.00 18.61 ? 92 GLU A N 1 ATOM 650 C CA . GLU A 1 92 ? 21.851 28.033 45.897 1.00 18.88 ? 92 GLU A CA 1 ATOM 651 C C . GLU A 1 92 ? 20.619 28.900 45.660 1.00 25.09 ? 92 GLU A C 1 ATOM 652 O O . GLU A 1 92 ? 20.418 29.800 46.482 1.00 21.86 ? 92 GLU A O 1 ATOM 653 C CB . GLU A 1 92 ? 21.461 26.915 46.860 1.00 29.93 ? 92 GLU A CB 1 ATOM 654 C CG . GLU A 1 92 ? 22.509 25.860 47.135 1.00 49.08 ? 92 GLU A CG 1 ATOM 655 C CD . GLU A 1 92 ? 22.075 24.816 48.141 1.00 59.64 ? 92 GLU A CD 1 ATOM 656 O OE1 . GLU A 1 92 ? 21.382 25.153 49.124 1.00 70.99 ? 92 GLU A OE1 1 ATOM 657 O OE2 . GLU A 1 92 ? 22.436 23.631 47.964 1.00 67.99 ? 92 GLU A OE2 1 ATOM 658 N N . VAL A 1 93 ? 19.873 28.651 44.598 1.00 14.39 ? 93 VAL A N 1 ATOM 659 C CA . VAL A 1 93 ? 18.636 29.363 44.294 1.00 10.53 ? 93 VAL A CA 1 ATOM 660 C C . VAL A 1 93 ? 17.602 28.262 43.970 1.00 14.69 ? 93 VAL A C 1 ATOM 661 O O . VAL A 1 93 ? 17.767 27.581 42.965 1.00 14.15 ? 93 VAL A O 1 ATOM 662 C CB . VAL A 1 93 ? 18.742 30.338 43.118 1.00 18.20 ? 93 VAL A CB 1 ATOM 663 C CG1 . VAL A 1 93 ? 17.418 31.026 42.806 1.00 16.37 ? 93 VAL A CG1 1 ATOM 664 C CG2 . VAL A 1 93 ? 19.802 31.406 43.412 1.00 20.51 ? 93 VAL A CG2 1 ATOM 665 N N . VAL A 1 94 ? 16.580 28.077 44.785 1.00 12.47 ? 94 VAL A N 1 ATOM 666 C CA . VAL A 1 94 ? 15.607 27.012 44.543 1.00 9.73 ? 94 VAL A CA 1 ATOM 667 C C . VAL A 1 94 ? 14.227 27.631 44.296 1.00 11.91 ? 94 VAL A C 1 ATOM 668 O O . VAL A 1 94 ? 13.795 28.475 45.098 1.00 13.21 ? 94 VAL A O 1 ATOM 669 C CB . VAL A 1 94 ? 15.499 26.041 45.727 1.00 14.31 ? 94 VAL A CB 1 ATOM 670 C CG1 . VAL A 1 94 ? 14.613 24.839 45.365 1.00 13.51 ? 94 VAL A CG1 1 ATOM 671 C CG2 . VAL A 1 94 ? 16.867 25.536 46.146 1.00 19.42 ? 94 VAL A CG2 1 ATOM 672 N N . PHE A 1 95 ? 13.579 27.226 43.215 1.00 11.53 ? 95 PHE A N 1 ATOM 673 C CA . PHE A 1 95 ? 12.308 27.890 42.891 1.00 13.60 ? 95 PHE A CA 1 ATOM 674 C C . PHE A 1 95 ? 11.422 26.955 42.076 1.00 13.44 ? 95 PHE A C 1 ATOM 675 O O . PHE A 1 95 ? 11.944 26.050 41.409 1.00 13.03 ? 95 PHE A O 1 ATOM 676 C CB . PHE A 1 95 ? 12.574 29.163 42.093 1.00 10.36 ? 95 PHE A CB 1 ATOM 677 C CG . PHE A 1 95 ? 13.317 28.990 40.783 1.00 16.28 ? 95 PHE A CG 1 ATOM 678 C CD1 . PHE A 1 95 ? 14.688 28.745 40.761 1.00 17.52 ? 95 PHE A CD1 1 ATOM 679 C CD2 . PHE A 1 95 ? 12.639 29.098 39.592 1.00 14.35 ? 95 PHE A CD2 1 ATOM 680 C CE1 . PHE A 1 95 ? 15.346 28.607 39.549 1.00 17.91 ? 95 PHE A CE1 1 ATOM 681 C CE2 . PHE A 1 95 ? 13.290 28.952 38.364 1.00 20.07 ? 95 PHE A CE2 1 ATOM 682 C CZ . PHE A 1 95 ? 14.651 28.725 38.352 1.00 15.63 ? 95 PHE A CZ 1 ATOM 683 N N . THR A 1 96 ? 10.121 27.199 42.133 1.00 13.82 ? 96 THR A N 1 ATOM 684 C CA . THR A 1 96 ? 9.207 26.547 41.195 1.00 11.89 ? 96 THR A CA 1 ATOM 685 C C . THR A 1 96 ? 9.147 27.296 39.887 1.00 14.78 ? 96 THR A C 1 ATOM 686 O O . THR A 1 96 ? 9.010 28.524 39.886 1.00 19.12 ? 96 THR A O 1 ATOM 687 C CB . THR A 1 96 ? 7.779 26.469 41.803 1.00 17.48 ? 96 THR A CB 1 ATOM 688 O OG1 . THR A 1 96 ? 7.860 25.651 42.975 1.00 17.57 ? 96 THR A OG1 1 ATOM 689 C CG2 . THR A 1 96 ? 6.831 25.771 40.842 1.00 23.19 ? 96 THR A CG2 1 ATOM 690 N N . ALA A 1 97 ? 9.255 26.614 38.753 1.00 12.13 ? 97 ALA A N 1 ATOM 691 C CA . ALA A 1 97 ? 9.161 27.301 37.476 1.00 14.72 ? 97 ALA A CA 1 ATOM 692 C C . ALA A 1 97 ? 7.950 26.854 36.644 1.00 16.80 ? 97 ALA A C 1 ATOM 693 O O . ALA A 1 97 ? 7.553 25.691 36.761 1.00 19.99 ? 97 ALA A O 1 ATOM 694 C CB . ALA A 1 97 ? 10.419 27.051 36.668 1.00 17.16 ? 97 ALA A CB 1 ATOM 695 N N . ASN A 1 98 ? 7.428 27.776 35.854 1.00 13.24 ? 98 ASN A N 1 ATOM 696 C CA . ASN A 1 98 ? 6.416 27.544 34.837 1.00 21.20 ? 98 ASN A CA 1 ATOM 697 C C . ASN A 1 98 ? 5.148 26.894 35.378 1.00 29.81 ? 98 ASN A C 1 ATOM 698 O O . ASN A 1 98 ? 4.488 26.108 34.673 1.00 26.83 ? 98 ASN A O 1 ATOM 699 C CB . ASN A 1 98 ? 6.973 26.617 33.753 1.00 18.22 ? 98 ASN A CB 1 ATOM 700 C CG . ASN A 1 98 ? 8.308 27.084 33.219 1.00 30.35 ? 98 ASN A CG 1 ATOM 701 O OD1 . ASN A 1 98 ? 9.292 26.341 33.195 1.00 30.99 ? 98 ASN A OD1 1 ATOM 702 N ND2 . ASN A 1 98 ? 8.322 28.326 32.792 1.00 17.62 ? 98 ASN A ND2 1 ATOM 703 N N . ASP A 1 99 ? 4.758 27.171 36.625 1.00 25.81 ? 99 ASP A N 1 ATOM 704 C CA . ASP A 1 99 ? 3.562 26.461 37.107 1.00 30.08 ? 99 ASP A CA 1 ATOM 705 C C . ASP A 1 99 ? 2.293 27.152 36.618 1.00 37.51 ? 99 ASP A C 1 ATOM 706 O O . ASP A 1 99 ? 1.198 26.594 36.727 1.00 34.32 ? 99 ASP A O 1 ATOM 707 C CB . ASP A 1 99 ? 3.590 26.315 38.619 1.00 35.28 ? 99 ASP A CB 1 ATOM 708 C CG . ASP A 1 99 ? 3.745 27.619 39.367 1.00 41.46 ? 99 ASP A CG 1 ATOM 709 O OD1 . ASP A 1 99 ? 4.491 28.490 38.874 1.00 43.02 ? 99 ASP A OD1 1 ATOM 710 O OD2 . ASP A 1 99 ? 3.132 27.757 40.449 1.00 51.70 ? 99 ASP A OD2 1 ATOM 711 N N . SER A 1 100 ? 2.424 28.351 36.067 1.00 35.38 ? 100 SER A N 1 ATOM 712 C CA . SER A 1 100 ? 1.300 29.049 35.460 1.00 40.33 ? 100 SER A CA 1 ATOM 713 C C . SER A 1 100 ? 1.655 29.374 34.014 1.00 39.24 ? 100 SER A C 1 ATOM 714 O O . SER A 1 100 ? 1.476 30.484 33.525 1.00 54.14 ? 100 SER A O 1 ATOM 715 C CB . SER A 1 100 ? 0.921 30.318 36.217 1.00 42.00 ? 100 SER A CB 1 ATOM 716 O OG . SER A 1 100 ? 1.824 30.618 37.267 1.00 64.66 ? 100 SER A OG 1 ATOM 717 N N . GLY A 1 101 ? 2.184 28.372 33.313 1.00 27.36 ? 101 GLY A N 1 ATOM 718 C CA . GLY A 1 101 ? 2.557 28.620 31.930 1.00 28.62 ? 101 GLY A CA 1 ATOM 719 C C . GLY A 1 101 ? 4.016 29.027 31.801 1.00 32.26 ? 101 GLY A C 1 ATOM 720 O O . GLY A 1 101 ? 4.655 29.388 32.789 1.00 31.92 ? 101 GLY A O 1 ATOM 721 N N . PRO A 1 102 ? 4.543 28.983 30.585 1.00 30.66 ? 102 PRO A N 1 ATOM 722 C CA . PRO A 1 102 ? 5.957 29.271 30.355 1.00 26.59 ? 102 PRO A CA 1 ATOM 723 C C . PRO A 1 102 ? 6.306 30.705 30.753 1.00 32.60 ? 102 PRO A C 1 ATOM 724 O O . PRO A 1 102 ? 5.553 31.638 30.471 1.00 26.53 ? 102 PRO A O 1 ATOM 725 C CB . PRO A 1 102 ? 6.130 29.159 28.839 1.00 26.45 ? 102 PRO A CB 1 ATOM 726 C CG . PRO A 1 102 ? 4.917 28.440 28.349 1.00 30.94 ? 102 PRO A CG 1 ATOM 727 C CD . PRO A 1 102 ? 3.817 28.692 29.335 1.00 27.46 ? 102 PRO A CD 1 ATOM 728 N N . ARG A 1 103 ? 7.458 30.872 31.388 1.00 19.00 ? 103 ARG A N 1 ATOM 729 C CA . ARG A 1 103 ? 7.942 32.216 31.710 1.00 13.39 ? 103 ARG A CA 1 ATOM 730 C C . ARG A 1 103 ? 9.421 32.265 31.367 1.00 19.55 ? 103 ARG A C 1 ATOM 731 O O . ARG A 1 103 ? 9.990 31.180 31.211 1.00 20.91 ? 103 ARG A O 1 ATOM 732 C CB . ARG A 1 103 ? 7.789 32.500 33.192 1.00 17.22 ? 103 ARG A CB 1 ATOM 733 C CG . ARG A 1 103 ? 6.353 32.574 33.669 1.00 32.07 ? 103 ARG A CG 1 ATOM 734 C CD . ARG A 1 103 ? 5.656 33.830 33.130 1.00 37.43 ? 103 ARG A CD 1 ATOM 735 N NE . ARG A 1 103 ? 4.299 33.848 33.683 1.00 48.13 ? 103 ARG A NE 1 ATOM 736 C CZ . ARG A 1 103 ? 3.276 33.132 33.227 1.00 50.51 ? 103 ARG A CZ 1 ATOM 737 N NH1 . ARG A 1 103 ? 3.416 32.317 32.187 1.00 42.83 ? 103 ARG A NH1 1 ATOM 738 N NH2 . ARG A 1 103 ? 2.095 33.245 33.831 1.00 48.10 ? 103 ARG A NH2 1 ATOM 739 N N . ARG A 1 104 ? 10.000 33.437 31.297 1.00 21.23 ? 104 ARG A N 1 ATOM 740 C CA . ARG A 1 104 ? 11.453 33.568 31.114 1.00 15.62 ? 104 ARG A CA 1 ATOM 741 C C . ARG A 1 104 ? 12.097 34.005 32.428 1.00 16.19 ? 104 ARG A C 1 ATOM 742 O O . ARG A 1 104 ? 11.592 34.939 33.059 1.00 14.85 ? 104 ARG A O 1 ATOM 743 C CB . ARG A 1 104 ? 11.743 34.576 30.008 1.00 27.42 ? 104 ARG A CB 1 ATOM 744 C CG . ARG A 1 104 ? 11.190 34.189 28.643 1.00 52.13 ? 104 ARG A CG 1 ATOM 745 C CD . ARG A 1 104 ? 11.370 35.304 27.626 1.00 60.93 ? 104 ARG A CD 1 ATOM 746 N NE . ARG A 1 104 ? 12.759 35.479 27.224 1.00 72.45 ? 104 ARG A NE 1 ATOM 747 C CZ . ARG A 1 104 ? 13.389 36.631 27.042 1.00 80.10 ? 104 ARG A CZ 1 ATOM 748 N NH1 . ARG A 1 104 ? 12.774 37.796 27.221 1.00 75.48 ? 104 ARG A NH1 1 ATOM 749 N NH2 . ARG A 1 104 ? 14.667 36.608 26.672 1.00 91.15 ? 104 ARG A NH2 1 ATOM 750 N N . TYR A 1 105 ? 13.184 33.372 32.849 1.00 10.59 ? 105 TYR A N 1 ATOM 751 C CA . TYR A 1 105 ? 13.731 33.672 34.165 1.00 15.13 ? 105 TYR A CA 1 ATOM 752 C C . TYR A 1 105 ? 15.167 34.170 34.046 1.00 17.30 ? 105 TYR A C 1 ATOM 753 O O . TYR A 1 105 ? 15.972 33.484 33.427 1.00 15.01 ? 105 TYR A O 1 ATOM 754 C CB . TYR A 1 105 ? 13.747 32.420 35.053 1.00 12.45 ? 105 TYR A CB 1 ATOM 755 C CG . TYR A 1 105 ? 12.367 31.864 35.350 1.00 17.27 ? 105 TYR A CG 1 ATOM 756 C CD1 . TYR A 1 105 ? 11.696 32.260 36.504 1.00 16.90 ? 105 TYR A CD1 1 ATOM 757 C CD2 . TYR A 1 105 ? 11.759 30.961 34.483 1.00 16.89 ? 105 TYR A CD2 1 ATOM 758 C CE1 . TYR A 1 105 ? 10.431 31.775 36.821 1.00 18.99 ? 105 TYR A CE1 1 ATOM 759 C CE2 . TYR A 1 105 ? 10.488 30.476 34.794 1.00 17.16 ? 105 TYR A CE2 1 ATOM 760 C CZ . TYR A 1 105 ? 9.846 30.883 35.945 1.00 16.97 ? 105 TYR A CZ 1 ATOM 761 O OH . TYR A 1 105 ? 8.582 30.386 36.215 1.00 16.90 ? 105 TYR A OH 1 ATOM 762 N N . THR A 1 106 ? 15.441 35.302 34.659 1.00 14.53 ? 106 THR A N 1 ATOM 763 C CA . THR A 1 106 ? 16.826 35.778 34.790 1.00 12.79 ? 106 THR A CA 1 ATOM 764 C C . THR A 1 106 ? 17.181 35.707 36.275 1.00 13.27 ? 106 THR A C 1 ATOM 765 O O . THR A 1 106 ? 16.519 36.338 37.110 1.00 18.91 ? 106 THR A O 1 ATOM 766 C CB . THR A 1 106 ? 16.994 37.198 34.256 1.00 20.38 ? 106 THR A CB 1 ATOM 767 O OG1 . THR A 1 106 ? 16.654 37.189 32.863 1.00 24.01 ? 106 THR A OG1 1 ATOM 768 C CG2 . THR A 1 106 ? 18.445 37.660 34.396 1.00 21.62 ? 106 THR A CG2 1 ATOM 769 N N . ILE A 1 107 ? 18.187 34.922 36.621 1.00 11.66 ? 107 ILE A N 1 ATOM 770 C CA . ILE A 1 107 ? 18.646 34.778 37.994 1.00 12.14 ? 107 ILE A CA 1 ATOM 771 C C . ILE A 1 107 ? 19.946 35.594 38.122 1.00 16.62 ? 107 ILE A C 1 ATOM 772 O O . ILE A 1 107 ? 20.902 35.294 37.391 1.00 19.85 ? 107 ILE A O 1 ATOM 773 C CB . ILE A 1 107 ? 18.908 33.306 38.344 1.00 18.57 ? 107 ILE A CB 1 ATOM 774 C CG1 . ILE A 1 107 ? 17.689 32.396 38.150 1.00 27.82 ? 107 ILE A CG1 1 ATOM 775 C CG2 . ILE A 1 107 ? 19.454 33.150 39.753 1.00 15.77 ? 107 ILE A CG2 1 ATOM 776 C CD1 . ILE A 1 107 ? 16.492 32.914 38.902 1.00 31.29 ? 107 ILE A CD1 1 ATOM 777 N N . ALA A 1 108 ? 19.978 36.607 38.953 1.00 12.18 ? 108 ALA A N 1 ATOM 778 C CA . ALA A 1 108 ? 21.217 37.392 39.129 1.00 12.09 ? 108 ALA A CA 1 ATOM 779 C C . ALA A 1 108 ? 21.781 37.121 40.508 1.00 17.62 ? 108 ALA A C 1 ATOM 780 O O . ALA A 1 108 ? 21.098 36.867 41.517 1.00 14.95 ? 108 ALA A O 1 ATOM 781 C CB . ALA A 1 108 ? 20.979 38.869 38.901 1.00 18.49 ? 108 ALA A CB 1 ATOM 782 N N . ALA A 1 109 ? 23.109 37.148 40.595 1.00 11.75 ? 109 ALA A N 1 ATOM 783 C CA . ALA A 1 109 ? 23.758 36.927 41.867 1.00 12.02 ? 109 ALA A CA 1 ATOM 784 C C . ALA A 1 109 ? 24.866 37.968 42.011 1.00 16.13 ? 109 ALA A C 1 ATOM 785 O O . ALA A 1 109 ? 25.590 38.137 41.033 1.00 14.83 ? 109 ALA A O 1 ATOM 786 C CB . ALA A 1 109 ? 24.302 35.500 41.944 1.00 17.08 ? 109 ALA A CB 1 ATOM 787 N N . LEU A 1 110 ? 24.979 38.610 43.156 1.00 10.22 ? 110 LEU A N 1 ATOM 788 C CA . LEU A 1 110 ? 26.021 39.588 43.451 1.00 8.90 ? 110 LEU A CA 1 ATOM 789 C C . LEU A 1 110 ? 26.896 38.996 44.540 1.00 11.09 ? 110 LEU A C 1 ATOM 790 O O . LEU A 1 110 ? 26.371 38.717 45.640 1.00 11.77 ? 110 LEU A O 1 ATOM 791 C CB A LEU A 1 110 ? 25.428 40.914 43.925 0.38 12.44 ? 110 LEU A CB 1 ATOM 792 C CB B LEU A 1 110 ? 25.396 40.901 43.923 0.62 11.91 ? 110 LEU A CB 1 ATOM 793 C CG A LEU A 1 110 ? 24.909 41.850 42.832 0.38 17.31 ? 110 LEU A CG 1 ATOM 794 C CG B LEU A 1 110 ? 26.367 42.023 44.262 0.62 16.31 ? 110 LEU A CG 1 ATOM 795 C CD1 A LEU A 1 110 ? 23.925 41.133 41.926 0.38 33.90 ? 110 LEU A CD1 1 ATOM 796 C CD1 B LEU A 1 110 ? 27.248 42.380 43.066 0.62 13.54 ? 110 LEU A CD1 1 ATOM 797 C CD2 A LEU A 1 110 ? 24.290 43.094 43.461 0.38 29.29 ? 110 LEU A CD2 1 ATOM 798 C CD2 B LEU A 1 110 ? 25.595 43.250 44.735 0.62 39.85 ? 110 LEU A CD2 1 ATOM 799 N N . LEU A 1 111 ? 28.179 38.766 44.311 1.00 8.94 ? 111 LEU A N 1 ATOM 800 C CA . LEU A 1 111 ? 29.003 38.027 45.274 1.00 6.63 ? 111 LEU A CA 1 ATOM 801 C C . LEU A 1 111 ? 30.010 38.874 46.033 1.00 10.43 ? 111 LEU A C 1 ATOM 802 O O . LEU A 1 111 ? 30.691 39.695 45.399 1.00 10.54 ? 111 LEU A O 1 ATOM 803 C CB . LEU A 1 111 ? 29.861 37.033 44.475 1.00 8.22 ? 111 LEU A CB 1 ATOM 804 C CG . LEU A 1 111 ? 29.087 36.026 43.610 1.00 15.58 ? 111 LEU A CG 1 ATOM 805 C CD1 . LEU A 1 111 ? 30.078 35.044 43.012 1.00 12.88 ? 111 LEU A CD1 1 ATOM 806 C CD2 . LEU A 1 111 ? 28.012 35.328 44.418 1.00 10.41 ? 111 LEU A CD2 1 ATOM 807 N N . SER A 1 112 ? 30.136 38.645 47.327 1.00 10.50 ? 112 SER A N 1 ATOM 808 C CA . SER A 1 112 ? 31.265 39.152 48.124 1.00 8.46 ? 112 SER A CA 1 ATOM 809 C C . SER A 1 112 ? 31.738 37.972 48.950 1.00 13.70 ? 112 SER A C 1 ATOM 810 O O . SER A 1 112 ? 31.029 36.967 49.093 1.00 12.53 ? 112 SER A O 1 ATOM 811 C CB A SER A 1 112 ? 30.883 40.320 49.012 0.50 11.33 ? 112 SER A CB 1 ATOM 812 C CB B SER A 1 112 ? 30.889 40.313 49.022 0.50 11.23 ? 112 SER A CB 1 ATOM 813 O OG A SER A 1 112 ? 31.082 40.022 50.385 0.50 38.06 ? 112 SER A OG 1 ATOM 814 O OG B SER A 1 112 ? 30.282 41.442 48.423 0.50 3.53 ? 112 SER A OG 1 ATOM 815 N N . PRO A 1 113 ? 32.944 38.004 49.495 1.00 12.86 ? 113 PRO A N 1 ATOM 816 C CA . PRO A 1 113 ? 33.417 36.826 50.244 1.00 13.72 ? 113 PRO A CA 1 ATOM 817 C C . PRO A 1 113 ? 32.549 36.362 51.396 1.00 11.94 ? 113 PRO A C 1 ATOM 818 O O . PRO A 1 113 ? 32.420 35.141 51.618 1.00 13.43 ? 113 PRO A O 1 ATOM 819 C CB . PRO A 1 113 ? 34.772 37.344 50.796 1.00 15.88 ? 113 PRO A CB 1 ATOM 820 C CG . PRO A 1 113 ? 35.202 38.327 49.742 1.00 18.76 ? 113 PRO A CG 1 ATOM 821 C CD . PRO A 1 113 ? 33.950 39.080 49.376 1.00 13.92 ? 113 PRO A CD 1 ATOM 822 N N . TYR A 1 114 ? 31.939 37.264 52.165 1.00 10.25 ? 114 TYR A N 1 ATOM 823 C CA . TYR A 1 114 ? 31.091 36.823 53.269 1.00 12.68 ? 114 TYR A CA 1 ATOM 824 C C . TYR A 1 114 ? 29.616 37.117 53.050 1.00 15.05 ? 114 TYR A C 1 ATOM 825 O O . TYR A 1 114 ? 28.844 37.069 54.015 1.00 13.65 ? 114 TYR A O 1 ATOM 826 C CB . TYR A 1 114 ? 31.510 37.524 54.573 1.00 10.38 ? 114 TYR A CB 1 ATOM 827 C CG . TYR A 1 114 ? 32.706 36.790 55.145 1.00 16.80 ? 114 TYR A CG 1 ATOM 828 C CD1 . TYR A 1 114 ? 33.936 36.934 54.529 1.00 25.28 ? 114 TYR A CD1 1 ATOM 829 C CD2 . TYR A 1 114 ? 32.570 35.970 56.256 1.00 14.64 ? 114 TYR A CD2 1 ATOM 830 C CE1 . TYR A 1 114 ? 35.035 36.268 55.034 1.00 34.79 ? 114 TYR A CE1 1 ATOM 831 C CE2 . TYR A 1 114 ? 33.676 35.306 56.755 1.00 16.39 ? 114 TYR A CE2 1 ATOM 832 C CZ . TYR A 1 114 ? 34.893 35.462 56.138 1.00 26.52 ? 114 TYR A CZ 1 ATOM 833 O OH . TYR A 1 114 ? 36.000 34.804 56.631 1.00 39.13 ? 114 TYR A OH 1 ATOM 834 N N . SER A 1 115 ? 29.174 37.444 51.834 1.00 14.74 ? 115 SER A N 1 ATOM 835 C CA . SER A 1 115 ? 27.770 37.817 51.637 1.00 10.43 ? 115 SER A CA 1 ATOM 836 C C . SER A 1 115 ? 27.401 37.610 50.187 1.00 15.70 ? 115 SER A C 1 ATOM 837 O O . SER A 1 115 ? 28.255 37.796 49.313 1.00 15.28 ? 115 SER A O 1 ATOM 838 C CB A SER A 1 115 ? 27.515 39.257 52.066 0.43 10.26 ? 115 SER A CB 1 ATOM 839 C CB B SER A 1 115 ? 27.585 39.265 52.068 0.57 10.42 ? 115 SER A CB 1 ATOM 840 O OG A SER A 1 115 ? 27.932 40.150 51.050 0.43 17.75 ? 115 SER A OG 1 ATOM 841 O OG B SER A 1 115 ? 26.351 39.840 51.706 0.57 13.80 ? 115 SER A OG 1 ATOM 842 N N . TYR A 1 116 ? 26.150 37.228 49.925 1.00 8.56 ? 116 TYR A N 1 ATOM 843 C CA . TYR A 1 116 ? 25.737 37.275 48.514 1.00 9.07 ? 116 TYR A CA 1 ATOM 844 C C . TYR A 1 116 ? 24.249 37.679 48.506 1.00 12.19 ? 116 TYR A C 1 ATOM 845 O O . TYR A 1 116 ? 23.570 37.481 49.513 1.00 16.98 ? 116 TYR A O 1 ATOM 846 C CB . TYR A 1 116 ? 25.935 35.999 47.731 1.00 15.24 ? 116 TYR A CB 1 ATOM 847 C CG . TYR A 1 116 ? 25.160 34.800 48.189 1.00 11.36 ? 116 TYR A CG 1 ATOM 848 C CD1 . TYR A 1 116 ? 23.871 34.489 47.810 1.00 16.94 ? 116 TYR A CD1 1 ATOM 849 C CD2 . TYR A 1 116 ? 25.792 33.919 49.071 1.00 18.10 ? 116 TYR A CD2 1 ATOM 850 C CE1 . TYR A 1 116 ? 23.222 33.354 48.281 1.00 18.60 ? 116 TYR A CE1 1 ATOM 851 C CE2 . TYR A 1 116 ? 25.173 32.782 49.555 1.00 21.07 ? 116 TYR A CE2 1 ATOM 852 C CZ . TYR A 1 116 ? 23.889 32.510 49.155 1.00 22.16 ? 116 TYR A CZ 1 ATOM 853 O OH . TYR A 1 116 ? 23.280 31.382 49.635 1.00 28.46 ? 116 TYR A OH 1 ATOM 854 N N . SER A 1 117 ? 23.833 38.224 47.399 1.00 11.61 ? 117 SER A N 1 ATOM 855 C CA . SER A 1 117 ? 22.483 38.627 47.109 1.00 10.97 ? 117 SER A CA 1 ATOM 856 C C . SER A 1 117 ? 22.058 37.912 45.827 1.00 15.93 ? 117 SER A C 1 ATOM 857 O O . SER A 1 117 ? 22.839 37.748 44.890 1.00 16.21 ? 117 SER A O 1 ATOM 858 C CB . SER A 1 117 ? 22.311 40.139 46.833 1.00 13.91 ? 117 SER A CB 1 ATOM 859 O OG . SER A 1 117 ? 22.786 40.852 47.966 1.00 25.18 ? 117 SER A OG 1 ATOM 860 N N . THR A 1 118 ? 20.794 37.511 45.824 1.00 10.80 ? 118 THR A N 1 ATOM 861 C CA . THR A 1 118 ? 20.287 36.930 44.578 1.00 10.48 ? 118 THR A CA 1 ATOM 862 C C . THR A 1 118 ? 18.918 37.553 44.316 1.00 16.60 ? 118 THR A C 1 ATOM 863 O O . THR A 1 118 ? 18.168 37.839 45.248 1.00 18.03 ? 118 THR A O 1 ATOM 864 C CB . THR A 1 118 ? 20.256 35.405 44.647 1.00 18.02 ? 118 THR A CB 1 ATOM 865 O OG1 . THR A 1 118 ? 19.925 34.944 43.331 1.00 22.11 ? 118 THR A OG1 1 ATOM 866 C CG2 . THR A 1 118 ? 19.177 34.904 45.599 1.00 15.94 ? 118 THR A CG2 1 ATOM 867 N N A MET A 1 119 ? 18.627 37.753 43.047 0.70 8.75 ? 119 MET A N 1 ATOM 868 C CA A MET A 1 119 ? 17.449 38.440 42.528 0.70 13.09 ? 119 MET A CA 1 ATOM 869 C C A MET A 1 119 ? 16.906 37.657 41.342 0.70 16.48 ? 119 MET A C 1 ATOM 870 O O A MET A 1 119 ? 17.679 37.072 40.574 0.70 19.64 ? 119 MET A O 1 ATOM 871 C CB A MET A 1 119 ? 17.867 39.856 42.165 0.70 15.71 ? 119 MET A CB 1 ATOM 872 C CG A MET A 1 119 ? 16.935 40.644 41.252 0.70 14.94 ? 119 MET A CG 1 ATOM 873 S SD A MET A 1 119 ? 15.399 40.957 42.136 0.70 30.50 ? 119 MET A SD 1 ATOM 874 C CE A MET A 1 119 ? 14.364 41.631 40.831 0.70 16.43 ? 119 MET A CE 1 ATOM 875 N N B THR A 1 119 ? 18.634 37.769 43.044 0.30 12.99 ? 119 THR A N 1 ATOM 876 C CA B THR A 1 119 ? 17.332 38.307 42.667 0.30 13.21 ? 119 THR A CA 1 ATOM 877 C C B THR A 1 119 ? 16.890 37.603 41.390 0.30 15.39 ? 119 THR A C 1 ATOM 878 O O B THR A 1 119 ? 17.697 37.055 40.642 0.30 19.35 ? 119 THR A O 1 ATOM 879 C CB B THR A 1 119 ? 17.386 39.818 42.500 0.30 11.42 ? 119 THR A CB 1 ATOM 880 O OG1 B THR A 1 119 ? 16.322 40.236 42.747 0.30 19.92 ? 119 THR A OG1 1 ATOM 881 C CG2 B THR A 1 119 ? 17.982 40.133 41.091 0.30 20.36 ? 119 THR A CG2 1 ATOM 882 N N . ALA A 1 120 ? 15.582 37.632 41.181 1.00 10.47 ? 120 ALA A N 1 ATOM 883 C CA . ALA A 1 120 ? 15.024 36.980 39.985 1.00 8.68 ? 120 ALA A CA 1 ATOM 884 C C . ALA A 1 120 ? 14.159 37.990 39.263 1.00 14.15 ? 120 ALA A C 1 ATOM 885 O O . ALA A 1 120 ? 13.406 38.739 39.882 1.00 16.64 ? 120 ALA A O 1 ATOM 886 C CB . ALA A 1 120 ? 14.242 35.749 40.414 1.00 12.19 ? 120 ALA A CB 1 ATOM 887 N N . VAL A 1 121 ? 14.301 38.020 37.942 1.00 9.72 ? 121 VAL A N 1 ATOM 888 C CA . VAL A 1 121 ? 13.389 38.804 37.133 1.00 9.69 ? 121 VAL A CA 1 ATOM 889 C C . VAL A 1 121 ? 12.613 37.776 36.315 1.00 18.23 ? 121 VAL A C 1 ATOM 890 O O . VAL A 1 121 ? 13.257 36.965 35.656 1.00 17.57 ? 121 VAL A O 1 ATOM 891 C CB . VAL A 1 121 ? 14.118 39.770 36.196 1.00 13.67 ? 121 VAL A CB 1 ATOM 892 C CG1 . VAL A 1 121 ? 13.122 40.542 35.335 1.00 17.82 ? 121 VAL A CG1 1 ATOM 893 C CG2 . VAL A 1 121 ? 14.982 40.713 37.023 1.00 21.34 ? 121 VAL A CG2 1 ATOM 894 N N . VAL A 1 122 ? 11.303 37.848 36.393 1.00 17.22 ? 122 VAL A N 1 ATOM 895 C CA . VAL A 1 122 ? 10.447 36.896 35.699 1.00 16.03 ? 122 VAL A CA 1 ATOM 896 C C . VAL A 1 122 ? 9.612 37.641 34.666 1.00 22.45 ? 122 VAL A C 1 ATOM 897 O O . VAL A 1 122 ? 8.899 38.590 35.031 1.00 18.09 ? 122 VAL A O 1 ATOM 898 C CB . VAL A 1 122 ? 9.572 36.140 36.716 1.00 17.68 ? 122 VAL A CB 1 ATOM 899 C CG1 . VAL A 1 122 ? 8.761 35.071 35.997 1.00 21.59 ? 122 VAL A CG1 1 ATOM 900 C CG2 . VAL A 1 122 ? 10.439 35.522 37.811 1.00 17.85 ? 122 VAL A CG2 1 ATOM 901 N N . THR A 1 123 ? 9.730 37.254 33.396 1.00 19.58 ? 123 THR A N 1 ATOM 902 C CA . THR A 1 123 ? 8.940 37.892 32.338 1.00 26.05 ? 123 THR A CA 1 ATOM 903 C C . THR A 1 123 ? 8.165 36.885 31.487 1.00 25.63 ? 123 THR A C 1 ATOM 904 O O . THR A 1 123 ? 8.293 35.669 31.595 1.00 23.09 ? 123 THR A O 1 ATOM 905 C CB . THR A 1 123 ? 9.829 38.752 31.423 1.00 27.92 ? 123 THR A CB 1 ATOM 906 O OG1 . THR A 1 123 ? 10.639 37.900 30.622 1.00 45.70 ? 123 THR A OG1 1 ATOM 907 C CG2 . THR A 1 123 ? 10.794 39.597 32.244 1.00 41.02 ? 123 THR A CG2 1 ATOM 908 N N . CYS B 1 10 ? 26.885 30.661 72.855 1.00 65.17 ? 10 CYS B N 1 ATOM 909 C CA . CYS B 1 10 ? 26.087 30.636 71.635 1.00 53.85 ? 10 CYS B CA 1 ATOM 910 C C . CYS B 1 10 ? 26.966 30.807 70.402 1.00 44.59 ? 10 CYS B C 1 ATOM 911 O O . CYS B 1 10 ? 27.227 31.932 69.975 1.00 46.07 ? 10 CYS B O 1 ATOM 912 C CB . CYS B 1 10 ? 25.018 31.731 71.666 1.00 56.92 ? 10 CYS B CB 1 ATOM 913 S SG . CYS B 1 10 ? 23.325 31.097 71.720 1.00 86.54 ? 10 CYS B SG 1 ATOM 914 N N . PRO B 1 11 ? 27.437 29.702 69.835 1.00 34.03 ? 11 PRO B N 1 ATOM 915 C CA . PRO B 1 11 ? 28.337 29.784 68.688 1.00 37.04 ? 11 PRO B CA 1 ATOM 916 C C . PRO B 1 11 ? 27.653 30.052 67.346 1.00 32.41 ? 11 PRO B C 1 ATOM 917 O O . PRO B 1 11 ? 28.403 30.353 66.420 1.00 25.64 ? 11 PRO B O 1 ATOM 918 C CB . PRO B 1 11 ? 28.937 28.371 68.633 1.00 33.05 ? 11 PRO B CB 1 ATOM 919 C CG . PRO B 1 11 ? 27.876 27.504 69.213 1.00 32.61 ? 11 PRO B CG 1 ATOM 920 C CD . PRO B 1 11 ? 27.179 28.317 70.259 1.00 28.72 ? 11 PRO B CD 1 ATOM 921 N N . LEU B 1 12 ? 26.334 29.898 67.289 1.00 22.98 ? 12 LEU B N 1 ATOM 922 C CA . LEU B 1 12 ? 25.606 30.050 66.036 1.00 22.46 ? 12 LEU B CA 1 ATOM 923 C C . LEU B 1 12 ? 24.311 30.812 66.273 1.00 27.68 ? 12 LEU B C 1 ATOM 924 O O . LEU B 1 12 ? 23.440 30.366 67.018 1.00 25.44 ? 12 LEU B O 1 ATOM 925 C CB . LEU B 1 12 ? 25.338 28.696 65.398 1.00 18.67 ? 12 LEU B CB 1 ATOM 926 C CG . LEU B 1 12 ? 24.587 28.682 64.059 1.00 22.38 ? 12 LEU B CG 1 ATOM 927 C CD1 . LEU B 1 12 ? 25.248 29.552 63.004 1.00 27.39 ? 12 LEU B CD1 1 ATOM 928 C CD2 . LEU B 1 12 ? 24.477 27.250 63.538 1.00 34.23 ? 12 LEU B CD2 1 ATOM 929 N N . MET B 1 13 ? 24.176 31.979 65.641 1.00 19.53 ? 13 MET B N 1 ATOM 930 C CA . MET B 1 13 ? 22.932 32.726 65.787 1.00 23.30 ? 13 MET B CA 1 ATOM 931 C C . MET B 1 13 ? 22.350 33.078 64.417 1.00 21.60 ? 13 MET B C 1 ATOM 932 O O . MET B 1 13 ? 23.122 33.223 63.467 1.00 18.91 ? 13 MET B O 1 ATOM 933 C CB . MET B 1 13 ? 23.196 34.016 66.558 1.00 26.56 ? 13 MET B CB 1 ATOM 934 C CG . MET B 1 13 ? 24.315 33.866 67.589 1.00 44.39 ? 13 MET B CG 1 ATOM 935 S SD . MET B 1 13 ? 24.545 35.392 68.536 1.00 61.34 ? 13 MET B SD 1 ATOM 936 C CE . MET B 1 13 ? 23.171 36.365 67.912 1.00 58.65 ? 13 MET B CE 1 ATOM 937 N N . VAL B 1 14 ? 21.032 33.228 64.333 1.00 17.70 ? 14 VAL B N 1 ATOM 938 C CA . VAL B 1 14 ? 20.457 33.563 63.021 1.00 21.28 ? 14 VAL B CA 1 ATOM 939 C C . VAL B 1 14 ? 19.567 34.777 63.194 1.00 20.69 ? 14 VAL B C 1 ATOM 940 O O . VAL B 1 14 ? 18.870 34.949 64.195 1.00 20.78 ? 14 VAL B O 1 ATOM 941 C CB . VAL B 1 14 ? 19.679 32.409 62.372 1.00 21.20 ? 14 VAL B CB 1 ATOM 942 C CG1 . VAL B 1 14 ? 19.250 32.828 60.961 1.00 30.39 ? 14 VAL B CG1 1 ATOM 943 C CG2 . VAL B 1 14 ? 20.502 31.141 62.256 1.00 20.24 ? 14 VAL B CG2 1 ATOM 944 N N . LYS B 1 15 ? 19.617 35.663 62.208 1.00 17.04 ? 15 LYS B N 1 ATOM 945 C CA . LYS B 1 15 ? 18.785 36.865 62.251 1.00 18.04 ? 15 LYS B CA 1 ATOM 946 C C . LYS B 1 15 ? 18.119 37.063 60.898 1.00 18.29 ? 15 LYS B C 1 ATOM 947 O O . LYS B 1 15 ? 18.792 36.949 59.856 1.00 17.06 ? 15 LYS B O 1 ATOM 948 C CB . LYS B 1 15 ? 19.654 38.075 62.639 1.00 19.24 ? 15 LYS B CB 1 ATOM 949 C CG . LYS B 1 15 ? 18.833 39.360 62.454 1.00 35.04 ? 15 LYS B CG 1 ATOM 950 C CD . LYS B 1 15 ? 18.948 40.284 63.640 1.00 46.63 ? 15 LYS B CD 1 ATOM 951 C CE . LYS B 1 15 ? 17.608 40.483 64.324 1.00 54.10 ? 15 LYS B CE 1 ATOM 952 N NZ . LYS B 1 15 ? 17.759 41.299 65.563 1.00 57.61 ? 15 LYS B NZ 1 ATOM 953 N N . VAL B 1 16 ? 16.819 37.317 60.855 1.00 14.17 ? 16 VAL B N 1 ATOM 954 C CA . VAL B 1 16 ? 16.073 37.394 59.606 1.00 13.35 ? 16 VAL B CA 1 ATOM 955 C C . VAL B 1 16 ? 15.240 38.677 59.585 1.00 15.39 ? 16 VAL B C 1 ATOM 956 O O . VAL B 1 16 ? 14.530 38.914 60.571 1.00 16.29 ? 16 VAL B O 1 ATOM 957 C CB . VAL B 1 16 ? 15.123 36.188 59.420 1.00 13.67 ? 16 VAL B CB 1 ATOM 958 C CG1 . VAL B 1 16 ? 14.627 36.154 57.976 1.00 15.97 ? 16 VAL B CG1 1 ATOM 959 C CG2 . VAL B 1 16 ? 15.762 34.875 59.776 1.00 14.67 ? 16 VAL B CG2 1 ATOM 960 N N . LEU B 1 17 ? 15.349 39.463 58.535 1.00 12.28 ? 17 LEU B N 1 ATOM 961 C CA . LEU B 1 17 ? 14.714 40.774 58.454 1.00 15.53 ? 17 LEU B CA 1 ATOM 962 C C . LEU B 1 17 ? 13.828 40.821 57.212 1.00 13.38 ? 17 LEU B C 1 ATOM 963 O O . LEU B 1 17 ? 14.142 40.175 56.212 1.00 16.83 ? 17 LEU B O 1 ATOM 964 C CB . LEU B 1 17 ? 15.734 41.917 58.375 1.00 16.58 ? 17 LEU B CB 1 ATOM 965 C CG . LEU B 1 17 ? 16.698 42.026 59.557 1.00 22.85 ? 17 LEU B CG 1 ATOM 966 C CD1 . LEU B 1 17 ? 17.675 43.171 59.350 1.00 29.76 ? 17 LEU B CD1 1 ATOM 967 C CD2 . LEU B 1 17 ? 15.946 42.225 60.866 1.00 25.79 ? 17 LEU B CD2 1 ATOM 968 N N . ASP B 1 18 ? 12.764 41.585 57.284 1.00 11.68 ? 18 ASP B N 1 ATOM 969 C CA . ASP B 1 18 ? 11.772 41.730 56.214 1.00 15.31 ? 18 ASP B CA 1 ATOM 970 C C . ASP B 1 18 ? 12.011 43.078 55.548 1.00 14.50 ? 18 ASP B C 1 ATOM 971 O O . ASP B 1 18 ? 11.760 44.099 56.212 1.00 14.92 ? 18 ASP B O 1 ATOM 972 C CB . ASP B 1 18 ? 10.396 41.557 56.878 1.00 10.54 ? 18 ASP B CB 1 ATOM 973 C CG . ASP B 1 18 ? 9.233 41.757 55.943 1.00 16.11 ? 18 ASP B CG 1 ATOM 974 O OD1 . ASP B 1 18 ? 9.356 42.506 54.947 1.00 15.25 ? 18 ASP B OD1 1 ATOM 975 O OD2 . ASP B 1 18 ? 8.160 41.168 56.218 1.00 21.18 ? 18 ASP B OD2 1 ATOM 976 N N . ALA B 1 19 ? 12.467 43.119 54.296 1.00 10.13 ? 19 ALA B N 1 ATOM 977 C CA . ALA B 1 19 ? 12.732 44.383 53.621 1.00 9.57 ? 19 ALA B CA 1 ATOM 978 C C . ALA B 1 19 ? 11.516 45.077 53.016 1.00 12.00 ? 19 ALA B C 1 ATOM 979 O O . ALA B 1 19 ? 11.616 46.178 52.452 1.00 16.91 ? 19 ALA B O 1 ATOM 980 C CB . ALA B 1 19 ? 13.705 44.129 52.459 1.00 11.70 ? 19 ALA B CB 1 ATOM 981 N N . VAL B 1 20 ? 10.383 44.396 53.078 1.00 14.59 ? 20 VAL B N 1 ATOM 982 C CA . VAL B 1 20 ? 9.107 44.901 52.578 1.00 14.47 ? 20 VAL B CA 1 ATOM 983 C C . VAL B 1 20 ? 8.438 45.724 53.688 1.00 16.46 ? 20 VAL B C 1 ATOM 984 O O . VAL B 1 20 ? 7.980 46.838 53.419 1.00 19.88 ? 20 VAL B O 1 ATOM 985 C CB . VAL B 1 20 ? 8.170 43.789 52.097 1.00 15.12 ? 20 VAL B CB 1 ATOM 986 C CG1 . VAL B 1 20 ? 6.782 44.374 51.817 1.00 26.04 ? 20 VAL B CG1 1 ATOM 987 C CG2 . VAL B 1 20 ? 8.693 43.139 50.820 1.00 16.14 ? 20 VAL B CG2 1 ATOM 988 N N . ARG B 1 21 ? 8.409 45.188 54.903 1.00 16.87 ? 21 ARG B N 1 ATOM 989 C CA . ARG B 1 21 ? 7.760 45.950 55.983 1.00 22.08 ? 21 ARG B CA 1 ATOM 990 C C . ARG B 1 21 ? 8.716 46.681 56.921 1.00 24.11 ? 21 ARG B C 1 ATOM 991 O O . ARG B 1 21 ? 8.289 47.471 57.787 1.00 19.31 ? 21 ARG B O 1 ATOM 992 C CB . ARG B 1 21 ? 6.870 44.981 56.758 1.00 24.40 ? 21 ARG B CB 1 ATOM 993 C CG . ARG B 1 21 ? 5.805 44.360 55.853 1.00 26.02 ? 21 ARG B CG 1 ATOM 994 C CD . ARG B 1 21 ? 5.837 42.852 56.048 1.00 48.22 ? 21 ARG B CD 1 ATOM 995 N NE . ARG B 1 21 ? 5.030 42.438 57.186 1.00 51.06 ? 21 ARG B NE 1 ATOM 996 C CZ . ARG B 1 21 ? 5.474 41.782 58.244 1.00 57.47 ? 21 ARG B CZ 1 ATOM 997 N NH1 . ARG B 1 21 ? 6.753 41.445 58.337 1.00 77.34 ? 21 ARG B NH1 1 ATOM 998 N NH2 . ARG B 1 21 ? 4.630 41.459 59.216 1.00 55.05 ? 21 ARG B NH2 1 ATOM 999 N N . GLY B 1 22 ? 10.016 46.465 56.788 1.00 13.94 ? 22 GLY B N 1 ATOM 1000 C CA . GLY B 1 22 ? 11.039 47.156 57.590 1.00 14.41 ? 22 GLY B CA 1 ATOM 1001 C C . GLY B 1 22 ? 10.985 46.657 59.025 1.00 21.37 ? 22 GLY B C 1 ATOM 1002 O O . GLY B 1 22 ? 10.968 47.378 60.024 1.00 17.65 ? 22 GLY B O 1 ATOM 1003 N N . SER B 1 23 ? 10.928 45.334 59.156 1.00 14.26 ? 23 SER B N 1 ATOM 1004 C CA . SER B 1 23 ? 10.771 44.766 60.490 1.00 15.33 ? 23 SER B CA 1 ATOM 1005 C C . SER B 1 23 ? 11.509 43.443 60.617 1.00 16.21 ? 23 SER B C 1 ATOM 1006 O O . SER B 1 23 ? 11.935 42.793 59.647 1.00 14.65 ? 23 SER B O 1 ATOM 1007 C CB . SER B 1 23 ? 9.260 44.627 60.768 1.00 22.14 ? 23 SER B CB 1 ATOM 1008 O OG . SER B 1 23 ? 8.725 43.634 59.907 1.00 32.17 ? 23 SER B OG 1 ATOM 1009 N N . PRO B 1 24 ? 11.705 42.956 61.838 1.00 17.53 ? 24 PRO B N 1 ATOM 1010 C CA . PRO B 1 24 ? 12.182 41.581 61.959 1.00 17.20 ? 24 PRO B CA 1 ATOM 1011 C C . PRO B 1 24 ? 11.169 40.641 61.296 1.00 20.55 ? 24 PRO B C 1 ATOM 1012 O O . PRO B 1 24 ? 9.958 40.914 61.235 1.00 17.79 ? 24 PRO B O 1 ATOM 1013 C CB . PRO B 1 24 ? 12.222 41.335 63.466 1.00 20.37 ? 24 PRO B CB 1 ATOM 1014 C CG . PRO B 1 24 ? 12.085 42.661 64.127 1.00 22.18 ? 24 PRO B CG 1 ATOM 1015 C CD . PRO B 1 24 ? 11.480 43.614 63.142 1.00 19.29 ? 24 PRO B CD 1 ATOM 1016 N N . ALA B 1 25 ? 11.685 39.533 60.775 1.00 18.38 ? 25 ALA B N 1 ATOM 1017 C CA . ALA B 1 25 ? 10.817 38.493 60.224 1.00 19.46 ? 25 ALA B CA 1 ATOM 1018 C C . ALA B 1 25 ? 10.481 37.515 61.353 1.00 18.49 ? 25 ALA B C 1 ATOM 1019 O O . ALA B 1 25 ? 11.346 36.785 61.815 1.00 14.13 ? 25 ALA B O 1 ATOM 1020 C CB . ALA B 1 25 ? 11.456 37.745 59.056 1.00 17.11 ? 25 ALA B CB 1 ATOM 1021 N N . ILE B 1 26 ? 9.233 37.493 61.800 1.00 18.32 ? 26 ILE B N 1 ATOM 1022 C CA . ILE B 1 26 ? 8.871 36.795 63.043 1.00 14.49 ? 26 ILE B CA 1 ATOM 1023 C C . ILE B 1 26 ? 8.216 35.467 62.734 1.00 14.93 ? 26 ILE B C 1 ATOM 1024 O O . ILE B 1 26 ? 7.506 35.419 61.731 1.00 16.73 ? 26 ILE B O 1 ATOM 1025 C CB . ILE B 1 26 ? 7.962 37.737 63.855 1.00 19.33 ? 26 ILE B CB 1 ATOM 1026 C CG1 . ILE B 1 26 ? 8.737 38.975 64.339 1.00 20.78 ? 26 ILE B CG1 1 ATOM 1027 C CG2 . ILE B 1 26 ? 7.248 37.069 65.018 1.00 25.29 ? 26 ILE B CG2 1 ATOM 1028 C CD1 . ILE B 1 26 ? 7.800 40.130 64.653 1.00 34.68 ? 26 ILE B CD1 1 ATOM 1029 N N . ASN B 1 27 ? 8.502 34.465 63.562 1.00 16.93 ? 27 ASN B N 1 ATOM 1030 C CA . ASN B 1 27 ? 7.924 33.143 63.392 1.00 18.56 ? 27 ASN B CA 1 ATOM 1031 C C . ASN B 1 27 ? 8.342 32.423 62.121 1.00 21.89 ? 27 ASN B C 1 ATOM 1032 O O . ASN B 1 27 ? 7.587 31.653 61.509 1.00 23.29 ? 27 ASN B O 1 ATOM 1033 C CB . ASN B 1 27 ? 6.386 33.271 63.368 1.00 24.94 ? 27 ASN B CB 1 ATOM 1034 C CG . ASN B 1 27 ? 5.858 32.689 64.667 1.00 43.17 ? 27 ASN B CG 1 ATOM 1035 O OD1 . ASN B 1 27 ? 5.463 31.530 64.703 1.00 69.95 ? 27 ASN B OD1 1 ATOM 1036 N ND2 . ASN B 1 27 ? 5.882 33.517 65.700 1.00 38.69 ? 27 ASN B ND2 1 ATOM 1037 N N . VAL B 1 28 ? 9.579 32.677 61.696 1.00 16.88 ? 28 VAL B N 1 ATOM 1038 C CA . VAL B 1 28 ? 10.047 32.048 60.456 1.00 14.25 ? 28 VAL B CA 1 ATOM 1039 C C . VAL B 1 28 ? 10.695 30.741 60.855 1.00 12.83 ? 28 VAL B C 1 ATOM 1040 O O . VAL B 1 28 ? 11.528 30.730 61.772 1.00 18.24 ? 28 VAL B O 1 ATOM 1041 C CB . VAL B 1 28 ? 11.029 32.951 59.692 1.00 17.50 ? 28 VAL B CB 1 ATOM 1042 C CG1 . VAL B 1 28 ? 11.547 32.249 58.442 1.00 23.30 ? 28 VAL B CG1 1 ATOM 1043 C CG2 . VAL B 1 28 ? 10.359 34.267 59.302 1.00 20.92 ? 28 VAL B CG2 1 ATOM 1044 N N . ALA B 1 29 ? 10.340 29.656 60.177 1.00 16.34 ? 29 ALA B N 1 ATOM 1045 C CA . ALA B 1 29 ? 10.919 28.377 60.598 1.00 13.27 ? 29 ALA B CA 1 ATOM 1046 C C . ALA B 1 29 ? 12.305 28.203 60.006 1.00 13.68 ? 29 ALA B C 1 ATOM 1047 O O . ALA B 1 29 ? 12.591 28.605 58.872 1.00 22.44 ? 29 ALA B O 1 ATOM 1048 C CB . ALA B 1 29 ? 10.029 27.213 60.190 1.00 14.58 ? 29 ALA B CB 1 ATOM 1049 N N A MET B 1 30 ? 13.138 27.551 60.804 0.40 19.07 ? 30 MET B N 1 ATOM 1050 C CA A MET B 1 30 ? 14.487 27.254 60.366 0.40 21.67 ? 30 MET B CA 1 ATOM 1051 C C A MET B 1 30 ? 14.896 25.824 60.655 0.40 20.78 ? 30 MET B C 1 ATOM 1052 O O A MET B 1 30 ? 14.495 25.218 61.642 0.40 24.57 ? 30 MET B O 1 ATOM 1053 C CB A MET B 1 30 ? 15.454 28.198 61.087 0.40 22.80 ? 30 MET B CB 1 ATOM 1054 C CG A MET B 1 30 ? 15.847 29.375 60.203 0.40 30.57 ? 30 MET B CG 1 ATOM 1055 S SD A MET B 1 30 ? 17.068 30.369 61.083 0.40 31.44 ? 30 MET B SD 1 ATOM 1056 C CE A MET B 1 30 ? 16.119 31.871 61.300 0.40 15.45 ? 30 MET B CE 1 ATOM 1057 N N B VAL B 1 30 ? 13.224 27.620 60.768 0.60 16.85 ? 30 VAL B N 1 ATOM 1058 C CA B VAL B 1 30 ? 14.586 27.398 60.299 0.60 23.11 ? 30 VAL B CA 1 ATOM 1059 C C B VAL B 1 30 ? 15.103 26.015 60.678 0.60 19.83 ? 30 VAL B C 1 ATOM 1060 O O B VAL B 1 30 ? 14.924 25.648 61.842 0.60 20.72 ? 30 VAL B O 1 ATOM 1061 C CB B VAL B 1 30 ? 15.507 28.460 60.919 0.60 21.19 ? 30 VAL B CB 1 ATOM 1062 C CG1 B VAL B 1 30 ? 17.021 28.316 60.859 0.60 20.12 ? 30 VAL B CG1 1 ATOM 1063 C CG2 B VAL B 1 30 ? 15.095 30.190 60.894 0.60 17.12 ? 30 VAL B CG2 1 ATOM 1064 N N . HIS B 1 31 ? 15.720 25.302 59.748 1.00 16.83 ? 31 HIS B N 1 ATOM 1065 C CA . HIS B 1 31 ? 16.269 23.976 60.006 1.00 17.80 ? 31 HIS B CA 1 ATOM 1066 C C . HIS B 1 31 ? 17.770 24.033 59.756 1.00 18.21 ? 31 HIS B C 1 ATOM 1067 O O . HIS B 1 31 ? 18.184 24.648 58.763 1.00 23.21 ? 31 HIS B O 1 ATOM 1068 C CB . HIS B 1 31 ? 15.591 22.940 59.112 1.00 21.70 ? 31 HIS B CB 1 ATOM 1069 C CG . HIS B 1 31 ? 14.142 22.758 59.464 1.00 35.85 ? 31 HIS B CG 1 ATOM 1070 N ND1 . HIS B 1 31 ? 13.678 21.710 60.230 1.00 33.18 ? 31 HIS B ND1 1 ATOM 1071 C CD2 . HIS B 1 31 ? 13.068 23.522 59.165 1.00 29.60 ? 31 HIS B CD2 1 ATOM 1072 C CE1 . HIS B 1 31 ? 12.375 21.816 60.383 1.00 33.35 ? 31 HIS B CE1 1 ATOM 1073 N NE2 . HIS B 1 31 ? 11.981 22.904 59.746 1.00 35.71 ? 31 HIS B NE2 1 ATOM 1074 N N . VAL B 1 32 ? 18.539 23.429 60.623 1.00 15.76 ? 32 VAL B N 1 ATOM 1075 C CA . VAL B 1 32 ? 19.984 23.355 60.505 1.00 18.75 ? 32 VAL B CA 1 ATOM 1076 C C . VAL B 1 32 ? 20.377 21.880 60.337 1.00 29.24 ? 32 VAL B C 1 ATOM 1077 O O . VAL B 1 32 ? 19.891 21.014 61.067 1.00 21.14 ? 32 VAL B O 1 ATOM 1078 C CB . VAL B 1 32 ? 20.733 23.966 61.702 1.00 19.60 ? 32 VAL B CB 1 ATOM 1079 C CG1 . VAL B 1 32 ? 22.218 24.072 61.348 1.00 13.62 ? 32 VAL B CG1 1 ATOM 1080 C CG2 . VAL B 1 32 ? 20.171 25.330 62.082 1.00 18.45 ? 32 VAL B CG2 1 ATOM 1081 N N . PHE B 1 33 ? 21.232 21.654 59.360 1.00 18.61 ? 33 PHE B N 1 ATOM 1082 C CA . PHE B 1 33 ? 21.714 20.338 58.985 1.00 25.16 ? 33 PHE B CA 1 ATOM 1083 C C . PHE B 1 33 ? 23.234 20.291 59.054 1.00 26.69 ? 33 PHE B C 1 ATOM 1084 O O . PHE B 1 33 ? 23.905 21.301 58.803 1.00 20.87 ? 33 PHE B O 1 ATOM 1085 C CB . PHE B 1 33 ? 21.281 19.962 57.562 1.00 22.57 ? 33 PHE B CB 1 ATOM 1086 C CG . PHE B 1 33 ? 19.770 20.005 57.399 1.00 25.51 ? 33 PHE B CG 1 ATOM 1087 C CD1 . PHE B 1 33 ? 19.145 21.147 56.930 1.00 20.61 ? 33 PHE B CD1 1 ATOM 1088 C CD2 . PHE B 1 33 ? 19.012 18.888 57.728 1.00 30.85 ? 33 PHE B CD2 1 ATOM 1089 C CE1 . PHE B 1 33 ? 17.774 21.176 56.785 1.00 27.43 ? 33 PHE B CE1 1 ATOM 1090 C CE2 . PHE B 1 33 ? 17.634 18.913 57.594 1.00 32.19 ? 33 PHE B CE2 1 ATOM 1091 C CZ . PHE B 1 33 ? 17.025 20.061 57.128 1.00 38.66 ? 33 PHE B CZ 1 ATOM 1092 N N . ARG B 1 34 ? 23.725 19.103 59.368 1.00 21.18 ? 34 ARG B N 1 ATOM 1093 C CA . ARG B 1 34 ? 25.159 18.822 59.314 1.00 23.98 ? 34 ARG B CA 1 ATOM 1094 C C . ARG B 1 34 ? 25.448 17.774 58.243 1.00 24.01 ? 34 ARG B C 1 ATOM 1095 O O . ARG B 1 34 ? 24.741 16.777 58.107 1.00 30.15 ? 34 ARG B O 1 ATOM 1096 C CB . ARG B 1 34 ? 25.704 18.357 60.673 1.00 30.44 ? 34 ARG B CB 1 ATOM 1097 C CG . ARG B 1 34 ? 27.195 18.608 60.798 1.00 39.37 ? 34 ARG B CG 1 ATOM 1098 C CD . ARG B 1 34 ? 27.798 18.093 62.103 1.00 47.99 ? 34 ARG B CD 1 ATOM 1099 N NE . ARG B 1 34 ? 29.263 18.218 61.961 1.00 52.82 ? 34 ARG B NE 1 ATOM 1100 C CZ . ARG B 1 34 ? 30.016 17.145 61.747 1.00 56.85 ? 34 ARG B CZ 1 ATOM 1101 N NH1 . ARG B 1 34 ? 29.425 15.957 61.676 1.00 57.12 ? 34 ARG B NH1 1 ATOM 1102 N NH2 . ARG B 1 34 ? 31.327 17.260 61.613 1.00 49.90 ? 34 ARG B NH2 1 ATOM 1103 N N . LYS B 1 35 ? 26.483 18.005 57.450 1.00 20.41 ? 35 LYS B N 1 ATOM 1104 C CA . LYS B 1 35 ? 26.835 17.084 56.381 1.00 34.76 ? 35 LYS B CA 1 ATOM 1105 C C . LYS B 1 35 ? 27.422 15.828 57.030 1.00 39.00 ? 35 LYS B C 1 ATOM 1106 O O . LYS B 1 35 ? 28.420 15.902 57.751 1.00 27.80 ? 35 LYS B O 1 ATOM 1107 C CB . LYS B 1 35 ? 27.815 17.684 55.373 1.00 35.65 ? 35 LYS B CB 1 ATOM 1108 C CG . LYS B 1 35 ? 27.523 17.230 53.944 1.00 44.26 ? 35 LYS B CG 1 ATOM 1109 C CD . LYS B 1 35 ? 28.710 17.471 53.023 1.00 58.52 ? 35 LYS B CD 1 ATOM 1110 C CE . LYS B 1 35 ? 29.893 16.593 53.416 1.00 66.80 ? 35 LYS B CE 1 ATOM 1111 N NZ . LYS B 1 35 ? 30.984 16.608 52.399 1.00 67.86 ? 35 LYS B NZ 1 ATOM 1112 N N . ALA B 1 36 ? 26.742 14.725 56.758 1.00 43.45 ? 36 ALA B N 1 ATOM 1113 C CA . ALA B 1 36 ? 27.078 13.459 57.400 1.00 53.55 ? 36 ALA B CA 1 ATOM 1114 C C . ALA B 1 36 ? 28.252 12.802 56.699 1.00 63.14 ? 36 ALA B C 1 ATOM 1115 O O . ALA B 1 36 ? 28.300 12.859 55.468 1.00 70.85 ? 36 ALA B O 1 ATOM 1116 C CB . ALA B 1 36 ? 25.854 12.557 57.389 1.00 43.23 ? 36 ALA B CB 1 ATOM 1117 N N . ALA B 1 37 ? 29.181 12.196 57.438 1.00 68.32 ? 37 ALA B N 1 ATOM 1118 C CA . ALA B 1 37 ? 30.207 11.413 56.731 1.00 68.19 ? 37 ALA B CA 1 ATOM 1119 C C . ALA B 1 37 ? 29.453 10.350 55.923 1.00 67.35 ? 37 ALA B C 1 ATOM 1120 O O . ALA B 1 37 ? 29.030 9.340 56.476 1.00 80.22 ? 37 ALA B O 1 ATOM 1121 C CB . ALA B 1 37 ? 31.228 10.804 57.657 1.00 41.36 ? 37 ALA B CB 1 ATOM 1122 N N . ASP B 1 38 ? 29.291 10.654 54.650 1.00 60.51 ? 38 ASP B N 1 ATOM 1123 C CA . ASP B 1 38 ? 28.358 10.027 53.743 1.00 75.45 ? 38 ASP B CA 1 ATOM 1124 C C . ASP B 1 38 ? 27.953 11.034 52.659 1.00 81.11 ? 38 ASP B C 1 ATOM 1125 O O . ASP B 1 38 ? 27.592 10.653 51.552 1.00 99.00 ? 38 ASP B O 1 ATOM 1126 C CB . ASP B 1 38 ? 27.095 9.567 54.470 1.00 82.56 ? 38 ASP B CB 1 ATOM 1127 C CG . ASP B 1 38 ? 26.897 8.068 54.459 1.00 97.35 ? 38 ASP B CG 1 ATOM 1128 O OD1 . ASP B 1 38 ? 27.523 7.381 53.620 1.00 123.39 ? 38 ASP B OD1 1 ATOM 1129 O OD2 . ASP B 1 38 ? 26.109 7.572 55.301 1.00 114.00 ? 38 ASP B OD2 1 ATOM 1130 N N . ASP B 1 39 ? 28.035 12.289 53.053 1.00 77.61 ? 39 ASP B N 1 ATOM 1131 C CA . ASP B 1 39 ? 27.637 13.481 52.326 1.00 78.53 ? 39 ASP B CA 1 ATOM 1132 C C . ASP B 1 39 ? 26.118 13.581 52.283 1.00 58.97 ? 39 ASP B C 1 ATOM 1133 O O . ASP B 1 39 ? 25.483 14.129 51.393 1.00 57.25 ? 39 ASP B O 1 ATOM 1134 C CB . ASP B 1 39 ? 28.256 13.507 50.926 1.00 93.11 ? 39 ASP B CB 1 ATOM 1135 C CG . ASP B 1 39 ? 29.650 14.118 50.965 1.00 104.76 ? 39 ASP B CG 1 ATOM 1136 O OD1 . ASP B 1 39 ? 29.808 15.260 50.482 1.00 120.09 ? 39 ASP B OD1 1 ATOM 1137 O OD2 . ASP B 1 39 ? 30.578 13.458 51.486 1.00 116.15 ? 39 ASP B OD2 1 ATOM 1138 N N . THR B 1 40 ? 25.491 13.027 53.321 1.00 50.23 ? 40 THR B N 1 ATOM 1139 C CA . THR B 1 40 ? 24.036 13.166 53.411 1.00 46.90 ? 40 THR B CA 1 ATOM 1140 C C . THR B 1 40 ? 23.707 14.210 54.470 1.00 39.49 ? 40 THR B C 1 ATOM 1141 O O . THR B 1 40 ? 24.443 14.288 55.459 1.00 39.02 ? 40 THR B O 1 ATOM 1142 C CB . THR B 1 40 ? 23.425 11.795 53.730 1.00 48.42 ? 40 THR B CB 1 ATOM 1143 O OG1 . THR B 1 40 ? 22.311 11.551 52.860 1.00 62.49 ? 40 THR B OG1 1 ATOM 1144 C CG2 . THR B 1 40 ? 22.908 11.772 55.156 1.00 40.84 ? 40 THR B CG2 1 ATOM 1145 N N . TRP B 1 41 ? 22.666 15.024 54.326 1.00 33.83 ? 41 TRP B N 1 ATOM 1146 C CA . TRP B 1 41 ? 22.414 16.054 55.337 1.00 26.67 ? 41 TRP B CA 1 ATOM 1147 C C . TRP B 1 41 ? 21.719 15.474 56.555 1.00 32.39 ? 41 TRP B C 1 ATOM 1148 O O . TRP B 1 41 ? 20.681 14.823 56.463 1.00 53.46 ? 41 TRP B O 1 ATOM 1149 C CB . TRP B 1 41 ? 21.573 17.208 54.769 1.00 29.30 ? 41 TRP B CB 1 ATOM 1150 C CG . TRP B 1 41 ? 22.334 18.026 53.765 1.00 35.24 ? 41 TRP B CG 1 ATOM 1151 C CD1 . TRP B 1 41 ? 22.112 18.042 52.414 1.00 42.56 ? 41 TRP B CD1 1 ATOM 1152 C CD2 . TRP B 1 41 ? 23.424 18.932 54.001 1.00 40.51 ? 41 TRP B CD2 1 ATOM 1153 N NE1 . TRP B 1 41 ? 22.994 18.900 51.806 1.00 50.14 ? 41 TRP B NE1 1 ATOM 1154 C CE2 . TRP B 1 41 ? 23.809 19.460 52.751 1.00 39.73 ? 41 TRP B CE2 1 ATOM 1155 C CE3 . TRP B 1 41 ? 24.113 19.352 55.149 1.00 28.74 ? 41 TRP B CE3 1 ATOM 1156 C CZ2 . TRP B 1 41 ? 24.843 20.380 52.596 1.00 34.56 ? 41 TRP B CZ2 1 ATOM 1157 C CZ3 . TRP B 1 41 ? 25.135 20.263 54.989 1.00 27.21 ? 41 TRP B CZ3 1 ATOM 1158 C CH2 . TRP B 1 41 ? 25.492 20.765 53.737 1.00 27.08 ? 41 TRP B CH2 1 ATOM 1159 N N . GLU B 1 42 ? 22.285 15.715 57.728 1.00 31.76 ? 42 GLU B N 1 ATOM 1160 C CA . GLU B 1 42 ? 21.682 15.207 58.951 1.00 38.08 ? 42 GLU B CA 1 ATOM 1161 C C . GLU B 1 42 ? 21.031 16.332 59.740 1.00 36.71 ? 42 GLU B C 1 ATOM 1162 O O . GLU B 1 42 ? 21.684 17.353 59.984 1.00 28.00 ? 42 GLU B O 1 ATOM 1163 C CB . GLU B 1 42 ? 22.777 14.510 59.761 1.00 43.58 ? 42 GLU B CB 1 ATOM 1164 C CG . GLU B 1 42 ? 22.532 14.460 61.255 1.00 64.22 ? 42 GLU B CG 1 ATOM 1165 C CD . GLU B 1 42 ? 23.783 14.207 62.075 1.00 77.56 ? 42 GLU B CD 1 ATOM 1166 O OE1 . GLU B 1 42 ? 24.353 13.100 61.951 1.00 88.71 ? 42 GLU B OE1 1 ATOM 1167 O OE2 . GLU B 1 42 ? 24.181 15.118 62.842 1.00 72.78 ? 42 GLU B OE2 1 ATOM 1168 N N . PRO B 1 43 ? 19.781 16.183 60.160 1.00 35.36 ? 43 PRO B N 1 ATOM 1169 C CA . PRO B 1 43 ? 19.194 17.160 61.090 1.00 23.17 ? 43 PRO B CA 1 ATOM 1170 C C . PRO B 1 43 ? 20.070 17.375 62.314 1.00 33.19 ? 43 PRO B C 1 ATOM 1171 O O . PRO B 1 43 ? 20.632 16.472 62.923 1.00 31.05 ? 43 PRO B O 1 ATOM 1172 C CB . PRO B 1 43 ? 17.861 16.523 61.493 1.00 35.90 ? 43 PRO B CB 1 ATOM 1173 C CG . PRO B 1 43 ? 17.525 15.632 60.345 1.00 38.31 ? 43 PRO B CG 1 ATOM 1174 C CD . PRO B 1 43 ? 18.824 15.129 59.786 1.00 32.76 ? 43 PRO B CD 1 ATOM 1175 N N . PHE B 1 44 ? 20.177 18.647 62.689 1.00 31.03 ? 44 PHE B N 1 ATOM 1176 C CA . PHE B 1 44 ? 21.058 19.099 63.748 1.00 29.45 ? 44 PHE B CA 1 ATOM 1177 C C . PHE B 1 44 ? 20.311 19.994 64.723 1.00 29.11 ? 44 PHE B C 1 ATOM 1178 O O . PHE B 1 44 ? 20.431 19.831 65.931 1.00 28.37 ? 44 PHE B O 1 ATOM 1179 C CB . PHE B 1 44 ? 22.253 19.829 63.113 1.00 33.34 ? 44 PHE B CB 1 ATOM 1180 C CG . PHE B 1 44 ? 23.328 20.224 64.115 1.00 29.75 ? 44 PHE B CG 1 ATOM 1181 C CD1 . PHE B 1 44 ? 24.193 19.272 64.627 1.00 32.78 ? 44 PHE B CD1 1 ATOM 1182 C CD2 . PHE B 1 44 ? 23.449 21.543 64.513 1.00 21.63 ? 44 PHE B CD2 1 ATOM 1183 C CE1 . PHE B 1 44 ? 25.170 19.624 65.546 1.00 24.64 ? 44 PHE B CE1 1 ATOM 1184 C CE2 . PHE B 1 44 ? 24.398 21.904 65.440 1.00 24.37 ? 44 PHE B CE2 1 ATOM 1185 C CZ . PHE B 1 44 ? 25.257 20.941 65.932 1.00 27.35 ? 44 PHE B CZ 1 ATOM 1186 N N . ALA B 1 45 ? 19.509 20.940 64.236 1.00 18.13 ? 45 ALA B N 1 ATOM 1187 C CA . ALA B 1 45 ? 18.771 21.838 65.106 1.00 18.82 ? 45 ALA B CA 1 ATOM 1188 C C . ALA B 1 45 ? 17.672 22.557 64.329 1.00 19.25 ? 45 ALA B C 1 ATOM 1189 O O . ALA B 1 45 ? 17.779 22.586 63.105 1.00 23.02 ? 45 ALA B O 1 ATOM 1190 C CB . ALA B 1 45 ? 19.689 22.880 65.728 1.00 27.82 ? 45 ALA B CB 1 ATOM 1191 N N . SER B 1 46 ? 16.679 23.098 65.026 1.00 18.04 ? 46 SER B N 1 ATOM 1192 C CA . SER B 1 46 ? 15.623 23.867 64.353 1.00 22.63 ? 46 SER B CA 1 ATOM 1193 C C . SER B 1 46 ? 14.885 24.745 65.347 1.00 22.78 ? 46 SER B C 1 ATOM 1194 O O . SER B 1 46 ? 14.991 24.612 66.554 1.00 23.36 ? 46 SER B O 1 ATOM 1195 C CB . SER B 1 46 ? 14.616 22.988 63.616 1.00 19.84 ? 46 SER B CB 1 ATOM 1196 O OG . SER B 1 46 ? 13.928 22.163 64.545 1.00 19.47 ? 46 SER B OG 1 ATOM 1197 N N . GLY B 1 47 ? 14.115 25.704 64.833 1.00 15.99 ? 47 GLY B N 1 ATOM 1198 C CA . GLY B 1 47 ? 13.415 26.605 65.722 1.00 16.72 ? 47 GLY B CA 1 ATOM 1199 C C . GLY B 1 47 ? 12.654 27.587 64.816 1.00 26.22 ? 47 GLY B C 1 ATOM 1200 O O . GLY B 1 47 ? 12.688 27.421 63.585 1.00 24.88 ? 47 GLY B O 1 ATOM 1201 N N . LYS B 1 48 ? 11.997 28.535 65.450 1.00 19.92 ? 48 LYS B N 1 ATOM 1202 C CA . LYS B 1 48 ? 11.262 29.603 64.779 1.00 26.36 ? 48 LYS B CA 1 ATOM 1203 C C . LYS B 1 48 ? 11.842 30.922 65.281 1.00 21.91 ? 48 LYS B C 1 ATOM 1204 O O . LYS B 1 48 ? 12.272 31.015 66.434 1.00 22.75 ? 48 LYS B O 1 ATOM 1205 C CB . LYS B 1 48 ? 9.768 29.591 65.041 1.00 35.87 ? 48 LYS B CB 1 ATOM 1206 C CG . LYS B 1 48 ? 8.956 28.686 64.136 1.00 46.61 ? 48 LYS B CG 1 ATOM 1207 C CD . LYS B 1 48 ? 7.536 28.533 64.668 1.00 54.25 ? 48 LYS B CD 1 ATOM 1208 C CE . LYS B 1 48 ? 7.455 28.896 66.143 1.00 52.44 ? 48 LYS B CE 1 ATOM 1209 N NZ . LYS B 1 48 ? 6.369 29.876 66.425 1.00 50.18 ? 48 LYS B NZ 1 ATOM 1210 N N . THR B 1 49 ? 11.888 31.931 64.412 1.00 17.56 ? 49 THR B N 1 ATOM 1211 C CA . THR B 1 49 ? 12.492 33.171 64.898 1.00 15.29 ? 49 THR B CA 1 ATOM 1212 C C . THR B 1 49 ? 11.574 33.865 65.900 1.00 21.29 ? 49 THR B C 1 ATOM 1213 O O . THR B 1 49 ? 10.345 33.741 65.811 1.00 16.42 ? 49 THR B O 1 ATOM 1214 C CB . THR B 1 49 ? 12.707 34.144 63.732 1.00 17.96 ? 49 THR B CB 1 ATOM 1215 O OG1 . THR B 1 49 ? 11.481 34.252 62.987 1.00 16.72 ? 49 THR B OG1 1 ATOM 1216 C CG2 . THR B 1 49 ? 13.736 33.603 62.760 1.00 16.04 ? 49 THR B CG2 1 ATOM 1217 N N . SER B 1 50 ? 12.198 34.599 66.803 1.00 19.48 ? 50 SER B N 1 ATOM 1218 C CA . SER B 1 50 ? 11.497 35.305 67.865 1.00 25.04 ? 50 SER B CA 1 ATOM 1219 C C . SER B 1 50 ? 10.904 36.601 67.337 1.00 33.10 ? 50 SER B C 1 ATOM 1220 O O . SER B 1 50 ? 11.061 36.950 66.155 1.00 19.68 ? 50 SER B O 1 ATOM 1221 C CB . SER B 1 50 ? 12.487 35.582 69.008 1.00 24.49 ? 50 SER B CB 1 ATOM 1222 O OG . SER B 1 50 ? 13.291 36.697 68.592 1.00 29.61 ? 50 SER B OG 1 ATOM 1223 N N . GLU B 1 51 ? 10.218 37.314 68.231 1.00 29.14 ? 51 GLU B N 1 ATOM 1224 C CA . GLU B 1 51 ? 9.680 38.635 67.940 1.00 23.48 ? 51 GLU B CA 1 ATOM 1225 C C . GLU B 1 51 ? 10.797 39.575 67.500 1.00 21.75 ? 51 GLU B C 1 ATOM 1226 O O . GLU B 1 51 ? 10.538 40.564 66.817 1.00 30.67 ? 51 GLU B O 1 ATOM 1227 C CB . GLU B 1 51 ? 8.941 39.227 69.138 1.00 32.02 ? 51 GLU B CB 1 ATOM 1228 C CG . GLU B 1 51 ? 7.427 39.235 68.954 1.00 60.07 ? 51 GLU B CG 1 ATOM 1229 C CD . GLU B 1 51 ? 6.708 38.366 69.968 1.00 82.12 ? 51 GLU B CD 1 ATOM 1230 O OE1 . GLU B 1 51 ? 6.789 38.673 71.182 1.00 111.72 ? 51 GLU B OE1 1 ATOM 1231 O OE2 . GLU B 1 51 ? 6.054 37.371 69.578 1.00 72.44 ? 51 GLU B OE2 1 ATOM 1232 N N . SER B 1 52 ? 12.057 39.319 67.822 1.00 21.98 ? 52 SER B N 1 ATOM 1233 C CA . SER B 1 52 ? 13.100 40.199 67.286 1.00 23.09 ? 52 SER B CA 1 ATOM 1234 C C . SER B 1 52 ? 13.770 39.620 66.042 1.00 20.44 ? 52 SER B C 1 ATOM 1235 O O . SER B 1 52 ? 14.866 40.052 65.655 1.00 18.51 ? 52 SER B O 1 ATOM 1236 C CB . SER B 1 52 ? 14.157 40.453 68.370 1.00 30.53 ? 52 SER B CB 1 ATOM 1237 O OG . SER B 1 52 ? 14.843 39.224 68.612 1.00 37.30 ? 52 SER B OG 1 ATOM 1238 N N . GLY B 1 53 ? 13.145 38.642 65.404 1.00 17.18 ? 53 GLY B N 1 ATOM 1239 C CA . GLY B 1 53 ? 13.680 38.064 64.170 1.00 15.52 ? 53 GLY B CA 1 ATOM 1240 C C . GLY B 1 53 ? 14.881 37.191 64.385 1.00 16.36 ? 53 GLY B C 1 ATOM 1241 O O . GLY B 1 53 ? 15.630 36.851 63.466 1.00 19.18 ? 53 GLY B O 1 ATOM 1242 N N . GLU B 1 54 ? 15.118 36.783 65.637 1.00 23.04 ? 54 GLU B N 1 ATOM 1243 C CA . GLU B 1 54 ? 16.337 36.059 65.956 1.00 21.92 ? 54 GLU B CA 1 ATOM 1244 C C . GLU B 1 54 ? 16.045 34.642 66.422 1.00 24.30 ? 54 GLU B C 1 ATOM 1245 O O . GLU B 1 54 ? 14.982 34.260 66.907 1.00 20.98 ? 54 GLU B O 1 ATOM 1246 C CB . GLU B 1 54 ? 17.162 36.741 67.056 1.00 25.35 ? 54 GLU B CB 1 ATOM 1247 C CG . GLU B 1 54 ? 17.877 38.011 66.660 1.00 46.81 ? 54 GLU B CG 1 ATOM 1248 C CD . GLU B 1 54 ? 18.185 38.891 67.863 1.00 60.81 ? 54 GLU B CD 1 ATOM 1249 O OE1 . GLU B 1 54 ? 18.347 38.322 68.963 1.00 72.58 ? 54 GLU B OE1 1 ATOM 1250 O OE2 . GLU B 1 54 ? 18.259 40.131 67.712 1.00 53.29 ? 54 GLU B OE2 1 ATOM 1251 N N . LEU B 1 55 ? 17.097 33.830 66.248 1.00 21.55 ? 55 LEU B N 1 ATOM 1252 C CA . LEU B 1 55 ? 17.028 32.455 66.728 1.00 22.63 ? 55 LEU B CA 1 ATOM 1253 C C . LEU B 1 55 ? 18.386 32.140 67.334 1.00 24.38 ? 55 LEU B C 1 ATOM 1254 O O . LEU B 1 55 ? 19.376 32.168 66.593 1.00 25.36 ? 55 LEU B O 1 ATOM 1255 C CB . LEU B 1 55 ? 16.672 31.505 65.584 1.00 19.50 ? 55 LEU B CB 1 ATOM 1256 C CG . LEU B 1 55 ? 16.478 30.035 65.887 1.00 28.27 ? 55 LEU B CG 1 ATOM 1257 C CD1 . LEU B 1 55 ? 15.565 29.813 67.085 1.00 27.98 ? 55 LEU B CD1 1 ATOM 1258 C CD2 . LEU B 1 55 ? 15.913 29.301 64.674 1.00 28.41 ? 55 LEU B CD2 1 ATOM 1259 N N . HIS B 1 56 ? 18.451 31.877 68.625 1.00 23.31 ? 56 HIS B N 1 ATOM 1260 C CA . HIS B 1 56 ? 19.741 31.426 69.166 1.00 36.93 ? 56 HIS B CA 1 ATOM 1261 C C . HIS B 1 56 ? 19.514 30.188 70.039 1.00 39.80 ? 56 HIS B C 1 ATOM 1262 O O . HIS B 1 56 ? 18.392 29.695 70.133 1.00 38.51 ? 56 HIS B O 1 ATOM 1263 C CB . HIS B 1 56 ? 20.494 32.494 69.944 1.00 45.07 ? 56 HIS B CB 1 ATOM 1264 C CG . HIS B 1 56 ? 19.645 33.427 70.744 1.00 55.85 ? 56 HIS B CG 1 ATOM 1265 N ND1 . HIS B 1 56 ? 19.511 34.760 70.413 1.00 69.89 ? 56 HIS B ND1 1 ATOM 1266 C CD2 . HIS B 1 56 ? 18.889 33.229 71.845 1.00 65.15 ? 56 HIS B CD2 1 ATOM 1267 C CE1 . HIS B 1 56 ? 18.708 35.343 71.283 1.00 77.60 ? 56 HIS B CE1 1 ATOM 1268 N NE2 . HIS B 1 56 ? 18.317 34.435 72.165 1.00 76.29 ? 56 HIS B NE2 1 ATOM 1269 N N . GLY B 1 57 ? 20.576 29.689 70.662 1.00 39.60 ? 57 GLY B N 1 ATOM 1270 C CA . GLY B 1 57 ? 20.441 28.488 71.481 1.00 36.08 ? 57 GLY B CA 1 ATOM 1271 C C . GLY B 1 57 ? 20.222 27.287 70.581 1.00 35.37 ? 57 GLY B C 1 ATOM 1272 O O . GLY B 1 57 ? 19.534 26.344 70.967 1.00 35.97 ? 57 GLY B O 1 ATOM 1273 N N . LEU B 1 58 ? 20.790 27.313 69.374 1.00 27.32 ? 58 LEU B N 1 ATOM 1274 C CA . LEU B 1 58 ? 20.622 26.203 68.447 1.00 25.53 ? 58 LEU B CA 1 ATOM 1275 C C . LEU B 1 58 ? 21.563 25.060 68.813 1.00 32.20 ? 58 LEU B C 1 ATOM 1276 O O . LEU B 1 58 ? 21.243 23.883 68.651 1.00 33.84 ? 58 LEU B O 1 ATOM 1277 C CB . LEU B 1 58 ? 20.906 26.613 67.001 1.00 25.12 ? 58 LEU B CB 1 ATOM 1278 C CG . LEU B 1 58 ? 19.872 27.551 66.375 1.00 24.63 ? 58 LEU B CG 1 ATOM 1279 C CD1 . LEU B 1 58 ? 20.344 28.025 65.014 1.00 24.83 ? 58 LEU B CD1 1 ATOM 1280 C CD2 . LEU B 1 58 ? 18.521 26.866 66.266 1.00 24.86 ? 58 LEU B CD2 1 ATOM 1281 N N . THR B 1 59 ? 22.736 25.444 69.307 1.00 28.34 ? 59 THR B N 1 ATOM 1282 C CA . THR B 1 59 ? 23.749 24.442 69.646 1.00 23.77 ? 59 THR B CA 1 ATOM 1283 C C . THR B 1 59 ? 24.652 24.926 70.767 1.00 27.48 ? 59 THR B C 1 ATOM 1284 O O . THR B 1 59 ? 24.551 26.027 71.302 1.00 26.44 ? 59 THR B O 1 ATOM 1285 C CB . THR B 1 59 ? 24.567 24.084 68.387 1.00 27.56 ? 59 THR B CB 1 ATOM 1286 O OG1 . THR B 1 59 ? 25.578 23.110 68.692 1.00 39.60 ? 59 THR B OG1 1 ATOM 1287 C CG2 . THR B 1 59 ? 25.297 25.313 67.872 1.00 27.24 ? 59 THR B CG2 1 ATOM 1288 N N . THR B 1 60 ? 25.591 24.071 71.156 1.00 29.42 ? 60 THR B N 1 ATOM 1289 C CA . THR B 1 60 ? 26.549 24.455 72.186 1.00 30.39 ? 60 THR B CA 1 ATOM 1290 C C . THR B 1 60 ? 27.950 24.362 71.598 1.00 21.26 ? 60 THR B C 1 ATOM 1291 O O . THR B 1 60 ? 28.094 23.729 70.555 1.00 26.91 ? 60 THR B O 1 ATOM 1292 C CB . THR B 1 60 ? 26.465 23.525 73.405 1.00 36.45 ? 60 THR B CB 1 ATOM 1293 O OG1 . THR B 1 60 ? 26.847 22.212 72.964 1.00 40.01 ? 60 THR B OG1 1 ATOM 1294 C CG2 . THR B 1 60 ? 25.033 23.469 73.922 1.00 38.77 ? 60 THR B CG2 1 ATOM 1295 N N . GLU B 1 61 ? 28.921 24.970 72.267 1.00 24.18 ? 61 GLU B N 1 ATOM 1296 C CA . GLU B 1 61 ? 30.288 24.916 71.755 1.00 39.58 ? 61 GLU B CA 1 ATOM 1297 C C . GLU B 1 61 ? 30.788 23.480 71.735 1.00 37.57 ? 61 GLU B C 1 ATOM 1298 O O . GLU B 1 61 ? 31.561 23.083 70.860 1.00 31.78 ? 61 GLU B O 1 ATOM 1299 C CB . GLU B 1 61 ? 31.203 25.825 72.581 1.00 50.42 ? 61 GLU B CB 1 ATOM 1300 C CG . GLU B 1 61 ? 32.044 26.762 71.725 1.00 64.80 ? 61 GLU B CG 1 ATOM 1301 C CD . GLU B 1 61 ? 32.513 28.014 72.435 1.00 80.23 ? 61 GLU B CD 1 ATOM 1302 O OE1 . GLU B 1 61 ? 32.279 29.127 71.907 1.00 90.98 ? 61 GLU B OE1 1 ATOM 1303 O OE2 . GLU B 1 61 ? 33.123 27.907 73.519 1.00 95.01 ? 61 GLU B OE2 1 ATOM 1304 N N . GLU B 1 62 ? 30.366 22.632 72.677 1.00 39.77 ? 62 GLU B N 1 ATOM 1305 C CA . GLU B 1 62 ? 30.876 21.265 72.632 1.00 36.71 ? 62 GLU B CA 1 ATOM 1306 C C . GLU B 1 62 ? 30.344 20.507 71.434 1.00 32.35 ? 62 GLU B C 1 ATOM 1307 O O . GLU B 1 62 ? 30.998 19.663 70.809 1.00 34.66 ? 62 GLU B O 1 ATOM 1308 C CB . GLU B 1 62 ? 30.511 20.509 73.920 1.00 39.79 ? 62 GLU B CB 1 ATOM 1309 C CG . GLU B 1 62 ? 31.603 19.518 74.320 1.00 47.36 ? 62 GLU B CG 1 ATOM 1310 C CD . GLU B 1 62 ? 32.932 20.211 74.572 1.00 55.10 ? 62 GLU B CD 1 ATOM 1311 O OE1 . GLU B 1 62 ? 32.923 21.327 75.139 1.00 77.09 ? 62 GLU B OE1 1 ATOM 1312 O OE2 . GLU B 1 62 ? 33.983 19.643 74.207 1.00 80.43 ? 62 GLU B OE2 1 ATOM 1313 N N . GLU B 1 63 ? 29.092 20.806 71.074 1.00 28.13 ? 63 GLU B N 1 ATOM 1314 C CA . GLU B 1 63 ? 28.519 20.030 69.974 1.00 30.30 ? 63 GLU B CA 1 ATOM 1315 C C . GLU B 1 63 ? 28.835 20.642 68.617 1.00 20.64 ? 63 GLU B C 1 ATOM 1316 O O . GLU B 1 63 ? 28.754 19.993 67.575 1.00 27.00 ? 63 GLU B O 1 ATOM 1317 C CB . GLU B 1 63 ? 27.009 19.963 70.160 1.00 32.98 ? 63 GLU B CB 1 ATOM 1318 C CG . GLU B 1 63 ? 26.301 18.869 69.376 1.00 52.65 ? 63 GLU B CG 1 ATOM 1319 C CD . GLU B 1 63 ? 24.812 18.909 69.700 1.00 73.10 ? 63 GLU B CD 1 ATOM 1320 O OE1 . GLU B 1 63 ? 24.484 19.459 70.777 1.00 92.49 ? 63 GLU B OE1 1 ATOM 1321 O OE2 . GLU B 1 63 ? 24.003 18.407 68.895 1.00 99.94 ? 63 GLU B OE2 1 ATOM 1322 N N . PHE B 1 64 ? 29.197 21.922 68.620 1.00 29.91 ? 64 PHE B N 1 ATOM 1323 C CA . PHE B 1 64 ? 29.418 22.571 67.316 1.00 34.37 ? 64 PHE B CA 1 ATOM 1324 C C . PHE B 1 64 ? 30.848 22.328 66.848 1.00 25.92 ? 64 PHE B C 1 ATOM 1325 O O . PHE B 1 64 ? 31.680 23.222 66.969 1.00 34.57 ? 64 PHE B O 1 ATOM 1326 C CB . PHE B 1 64 ? 29.108 24.059 67.399 1.00 22.25 ? 64 PHE B CB 1 ATOM 1327 C CG . PHE B 1 64 ? 28.849 24.781 66.087 1.00 20.84 ? 64 PHE B CG 1 ATOM 1328 C CD1 . PHE B 1 64 ? 28.050 24.240 65.102 1.00 17.11 ? 64 PHE B CD1 1 ATOM 1329 C CD2 . PHE B 1 64 ? 29.411 26.026 65.859 1.00 36.05 ? 64 PHE B CD2 1 ATOM 1330 C CE1 . PHE B 1 64 ? 27.809 24.903 63.907 1.00 28.52 ? 64 PHE B CE1 1 ATOM 1331 C CE2 . PHE B 1 64 ? 29.186 26.690 64.669 1.00 36.20 ? 64 PHE B CE2 1 ATOM 1332 C CZ . PHE B 1 64 ? 28.382 26.142 63.681 1.00 27.53 ? 64 PHE B CZ 1 ATOM 1333 N N . VAL B 1 65 ? 31.112 21.139 66.319 1.00 21.01 ? 65 VAL B N 1 ATOM 1334 C CA . VAL B 1 65 ? 32.434 20.763 65.837 1.00 20.60 ? 65 VAL B CA 1 ATOM 1335 C C . VAL B 1 65 ? 32.587 21.186 64.377 1.00 24.65 ? 65 VAL B C 1 ATOM 1336 O O . VAL B 1 65 ? 31.587 21.477 63.707 1.00 27.10 ? 65 VAL B O 1 ATOM 1337 C CB . VAL B 1 65 ? 32.690 19.249 65.991 1.00 21.22 ? 65 VAL B CB 1 ATOM 1338 C CG1 . VAL B 1 65 ? 32.565 18.856 67.458 1.00 22.74 ? 65 VAL B CG1 1 ATOM 1339 C CG2 . VAL B 1 65 ? 31.745 18.381 65.177 1.00 23.96 ? 65 VAL B CG2 1 ATOM 1340 N N . GLU B 1 66 ? 33.816 21.225 63.901 1.00 25.18 ? 66 GLU B N 1 ATOM 1341 C CA . GLU B 1 66 ? 34.149 21.508 62.515 1.00 27.06 ? 66 GLU B CA 1 ATOM 1342 C C . GLU B 1 66 ? 33.337 20.590 61.613 1.00 27.96 ? 66 GLU B C 1 ATOM 1343 O O . GLU B 1 66 ? 33.173 19.417 61.937 1.00 29.89 ? 66 GLU B O 1 ATOM 1344 C CB . GLU B 1 66 ? 35.637 21.270 62.202 1.00 26.62 ? 66 GLU B CB 1 ATOM 1345 C CG . GLU B 1 66 ? 36.549 22.349 62.768 1.00 29.02 ? 66 GLU B CG 1 ATOM 1346 C CD . GLU B 1 66 ? 38.006 22.146 62.390 1.00 42.65 ? 66 GLU B CD 1 ATOM 1347 O OE1 . GLU B 1 66 ? 38.521 21.021 62.564 1.00 32.66 ? 66 GLU B OE1 1 ATOM 1348 O OE2 . GLU B 1 66 ? 38.639 23.117 61.921 1.00 31.22 ? 66 GLU B OE2 1 ATOM 1349 N N . GLY B 1 67 ? 32.871 21.139 60.503 1.00 28.09 ? 67 GLY B N 1 ATOM 1350 C CA . GLY B 1 67 ? 32.129 20.356 59.528 1.00 22.46 ? 67 GLY B CA 1 ATOM 1351 C C . GLY B 1 67 ? 31.457 21.335 58.560 1.00 21.75 ? 67 GLY B C 1 ATOM 1352 O O . GLY B 1 67 ? 31.733 22.532 58.651 1.00 20.95 ? 67 GLY B O 1 ATOM 1353 N N . ILE B 1 68 ? 30.617 20.779 57.711 1.00 19.71 ? 68 ILE B N 1 ATOM 1354 C CA . ILE B 1 68 ? 29.853 21.599 56.774 1.00 24.33 ? 68 ILE B CA 1 ATOM 1355 C C . ILE B 1 68 ? 28.401 21.634 57.238 1.00 21.18 ? 68 ILE B C 1 ATOM 1356 O O . ILE B 1 68 ? 27.798 20.592 57.517 1.00 23.76 ? 68 ILE B O 1 ATOM 1357 C CB . ILE B 1 68 ? 29.946 21.073 55.337 1.00 24.78 ? 68 ILE B CB 1 ATOM 1358 C CG1 . ILE B 1 68 ? 31.385 20.928 54.836 1.00 35.62 ? 68 ILE B CG1 1 ATOM 1359 C CG2 . ILE B 1 68 ? 29.121 21.957 54.401 1.00 23.55 ? 68 ILE B CG2 1 ATOM 1360 C CD1 . ILE B 1 68 ? 31.493 20.625 53.358 1.00 38.49 ? 68 ILE B CD1 1 ATOM 1361 N N . TYR B 1 69 ? 27.869 22.851 57.300 1.00 17.26 ? 69 TYR B N 1 ATOM 1362 C CA . TYR B 1 69 ? 26.552 23.045 57.880 1.00 16.11 ? 69 TYR B CA 1 ATOM 1363 C C . TYR B 1 69 ? 25.638 23.733 56.872 1.00 21.45 ? 69 TYR B C 1 ATOM 1364 O O . TYR B 1 69 ? 26.152 24.541 56.114 1.00 16.81 ? 69 TYR B O 1 ATOM 1365 C CB . TYR B 1 69 ? 26.623 23.887 59.149 1.00 17.30 ? 69 TYR B CB 1 ATOM 1366 C CG . TYR B 1 69 ? 27.243 23.139 60.321 1.00 19.05 ? 69 TYR B CG 1 ATOM 1367 C CD1 . TYR B 1 69 ? 28.622 23.087 60.430 1.00 18.49 ? 69 TYR B CD1 1 ATOM 1368 C CD2 . TYR B 1 69 ? 26.459 22.493 61.275 1.00 22.86 ? 69 TYR B CD2 1 ATOM 1369 C CE1 . TYR B 1 69 ? 29.251 22.415 61.472 1.00 20.59 ? 69 TYR B CE1 1 ATOM 1370 C CE2 . TYR B 1 69 ? 27.088 21.827 62.318 1.00 20.63 ? 69 TYR B CE2 1 ATOM 1371 C CZ . TYR B 1 69 ? 28.458 21.792 62.406 1.00 23.95 ? 69 TYR B CZ 1 ATOM 1372 O OH . TYR B 1 69 ? 29.093 21.137 63.444 1.00 24.21 ? 69 TYR B OH 1 ATOM 1373 N N . LYS B 1 70 ? 24.363 23.391 56.914 1.00 14.55 ? 70 LYS B N 1 ATOM 1374 C CA . LYS B 1 70 ? 23.390 24.040 56.042 1.00 20.00 ? 70 LYS B CA 1 ATOM 1375 C C . LYS B 1 70 ? 22.292 24.639 56.907 1.00 23.55 ? 70 LYS B C 1 ATOM 1376 O O . LYS B 1 70 ? 21.780 23.957 57.804 1.00 19.25 ? 70 LYS B O 1 ATOM 1377 C CB . LYS B 1 70 ? 22.829 23.026 55.040 1.00 20.12 ? 70 LYS B CB 1 ATOM 1378 C CG . LYS B 1 70 ? 21.756 23.586 54.120 1.00 25.62 ? 70 LYS B CG 1 ATOM 1379 C CD . LYS B 1 70 ? 20.719 22.556 53.747 1.00 42.67 ? 70 LYS B CD 1 ATOM 1380 C CE . LYS B 1 70 ? 21.202 21.509 52.765 1.00 54.62 ? 70 LYS B CE 1 ATOM 1381 N NZ . LYS B 1 70 ? 20.043 20.898 52.045 1.00 62.36 ? 70 LYS B NZ 1 ATOM 1382 N N . VAL B 1 71 ? 21.959 25.899 56.614 1.00 15.36 ? 71 VAL B N 1 ATOM 1383 C CA . VAL B 1 71 ? 20.882 26.563 57.340 1.00 17.40 ? 71 VAL B CA 1 ATOM 1384 C C . VAL B 1 71 ? 19.782 26.774 56.298 1.00 18.54 ? 71 VAL B C 1 ATOM 1385 O O . VAL B 1 71 ? 20.049 27.409 55.274 1.00 13.72 ? 71 VAL B O 1 ATOM 1386 C CB . VAL B 1 71 ? 21.286 27.904 57.960 1.00 18.52 ? 71 VAL B CB 1 ATOM 1387 C CG1 . VAL B 1 71 ? 20.082 28.639 58.545 1.00 20.56 ? 71 VAL B CG1 1 ATOM 1388 C CG2 . VAL B 1 71 ? 22.345 27.730 59.030 1.00 13.31 ? 71 VAL B CG2 1 ATOM 1389 N N . GLU B 1 72 ? 18.614 26.217 56.578 1.00 14.45 ? 72 GLU B N 1 ATOM 1390 C CA . GLU B 1 72 ? 17.506 26.332 55.636 1.00 16.05 ? 72 GLU B CA 1 ATOM 1391 C C . GLU B 1 72 ? 16.415 27.199 56.253 1.00 16.48 ? 72 GLU B C 1 ATOM 1392 O O . GLU B 1 72 ? 15.936 26.895 57.344 1.00 16.63 ? 72 GLU B O 1 ATOM 1393 C CB . GLU B 1 72 ? 16.920 24.975 55.263 1.00 20.57 ? 72 GLU B CB 1 ATOM 1394 C CG . GLU B 1 72 ? 15.700 25.130 54.339 1.00 31.23 ? 72 GLU B CG 1 ATOM 1395 C CD . GLU B 1 72 ? 15.184 23.745 53.966 1.00 54.58 ? 72 GLU B CD 1 ATOM 1396 O OE1 . GLU B 1 72 ? 16.024 22.879 53.630 1.00 41.65 ? 72 GLU B OE1 1 ATOM 1397 O OE2 . GLU B 1 72 ? 13.954 23.546 54.024 1.00 75.28 ? 72 GLU B OE2 1 ATOM 1398 N N . ILE B 1 73 ? 16.085 28.276 55.558 1.00 16.36 ? 73 ILE B N 1 ATOM 1399 C CA . ILE B 1 73 ? 15.079 29.208 56.081 1.00 16.41 ? 73 ILE B CA 1 ATOM 1400 C C . ILE B 1 73 ? 13.803 29.128 55.277 1.00 14.49 ? 73 ILE B C 1 ATOM 1401 O O . ILE B 1 73 ? 13.857 29.309 54.045 1.00 15.97 ? 73 ILE B O 1 ATOM 1402 C CB . ILE B 1 73 ? 15.686 30.630 56.055 1.00 17.46 ? 73 ILE B CB 1 ATOM 1403 C CG1 . ILE B 1 73 ? 17.006 30.677 56.845 1.00 24.72 ? 73 ILE B CG1 1 ATOM 1404 C CG2 . ILE B 1 73 ? 14.676 31.648 56.510 1.00 12.65 ? 73 ILE B CG2 1 ATOM 1405 C CD1 . ILE B 1 73 ? 17.934 31.813 56.456 1.00 27.40 ? 73 ILE B CD1 1 ATOM 1406 N N . ASP B 1 74 ? 12.662 28.875 55.935 1.00 12.47 ? 74 ASP B N 1 ATOM 1407 C CA . ASP B 1 74 ? 11.417 28.689 55.164 1.00 14.94 ? 74 ASP B CA 1 ATOM 1408 C C . ASP B 1 74 ? 10.720 30.001 54.837 1.00 14.28 ? 74 ASP B C 1 ATOM 1409 O O . ASP B 1 74 ? 9.769 30.436 55.491 1.00 17.68 ? 74 ASP B O 1 ATOM 1410 C CB . ASP B 1 74 ? 10.457 27.748 55.881 1.00 20.85 ? 74 ASP B CB 1 ATOM 1411 C CG . ASP B 1 74 ? 9.231 27.397 55.056 1.00 34.75 ? 74 ASP B CG 1 ATOM 1412 O OD1 . ASP B 1 74 ? 9.079 27.851 53.895 1.00 31.58 ? 74 ASP B OD1 1 ATOM 1413 O OD2 . ASP B 1 74 ? 8.389 26.631 55.574 1.00 31.58 ? 74 ASP B OD2 1 ATOM 1414 N N . THR B 1 75 ? 11.231 30.647 53.778 1.00 12.98 ? 75 THR B N 1 ATOM 1415 C CA . THR B 1 75 ? 10.767 31.969 53.416 1.00 12.52 ? 75 THR B CA 1 ATOM 1416 C C . THR B 1 75 ? 9.439 31.883 52.675 1.00 14.20 ? 75 THR B C 1 ATOM 1417 O O . THR B 1 75 ? 8.666 32.836 52.684 1.00 16.97 ? 75 THR B O 1 ATOM 1418 C CB . THR B 1 75 ? 11.762 32.690 52.493 1.00 14.99 ? 75 THR B CB 1 ATOM 1419 O OG1 . THR B 1 75 ? 12.023 31.804 51.385 1.00 17.18 ? 75 THR B OG1 1 ATOM 1420 C CG2 . THR B 1 75 ? 13.064 32.967 53.221 1.00 15.89 ? 75 THR B CG2 1 ATOM 1421 N N . LYS B 1 76 ? 9.183 30.736 52.030 1.00 13.39 ? 76 LYS B N 1 ATOM 1422 C CA . LYS B 1 76 ? 7.928 30.680 51.260 1.00 12.85 ? 76 LYS B CA 1 ATOM 1423 C C . LYS B 1 76 ? 6.697 30.761 52.159 1.00 14.79 ? 76 LYS B C 1 ATOM 1424 O O . LYS B 1 76 ? 5.773 31.538 51.866 1.00 17.89 ? 76 LYS B O 1 ATOM 1425 C CB . LYS B 1 76 ? 7.875 29.398 50.432 1.00 17.54 ? 76 LYS B CB 1 ATOM 1426 C CG . LYS B 1 76 ? 6.667 29.316 49.491 1.00 20.40 ? 76 LYS B CG 1 ATOM 1427 C CD . LYS B 1 76 ? 6.778 27.991 48.720 1.00 25.36 ? 76 LYS B CD 1 ATOM 1428 C CE . LYS B 1 76 ? 5.771 27.954 47.575 1.00 36.71 ? 76 LYS B CE 1 ATOM 1429 N NZ . LYS B 1 76 ? 5.835 26.656 46.838 1.00 56.92 ? 76 LYS B NZ 1 ATOM 1430 N N . SER B 1 77 ? 6.672 29.980 53.238 1.00 18.02 ? 77 SER B N 1 ATOM 1431 C CA . SER B 1 77 ? 5.577 30.072 54.202 1.00 22.11 ? 77 SER B CA 1 ATOM 1432 C C . SER B 1 77 ? 5.454 31.460 54.808 1.00 21.57 ? 77 SER B C 1 ATOM 1433 O O . SER B 1 77 ? 4.336 31.901 55.093 1.00 22.95 ? 77 SER B O 1 ATOM 1434 C CB . SER B 1 77 ? 5.739 29.099 55.382 1.00 22.74 ? 77 SER B CB 1 ATOM 1435 O OG . SER B 1 77 ? 5.844 27.767 54.963 1.00 27.97 ? 77 SER B OG 1 ATOM 1436 N N . TYR B 1 78 ? 6.593 32.140 55.003 1.00 12.62 ? 78 TYR B N 1 ATOM 1437 C CA . TYR B 1 78 ? 6.529 33.482 55.587 1.00 19.61 ? 78 TYR B CA 1 ATOM 1438 C C . TYR B 1 78 ? 5.804 34.453 54.663 1.00 16.28 ? 78 TYR B C 1 ATOM 1439 O O . TYR B 1 78 ? 4.962 35.234 55.107 1.00 18.29 ? 78 TYR B O 1 ATOM 1440 C CB . TYR B 1 78 ? 7.945 33.994 55.928 1.00 15.32 ? 78 TYR B CB 1 ATOM 1441 C CG . TYR B 1 78 ? 7.976 35.455 56.362 1.00 18.69 ? 78 TYR B CG 1 ATOM 1442 C CD1 . TYR B 1 78 ? 7.727 35.759 57.703 1.00 16.15 ? 78 TYR B CD1 1 ATOM 1443 C CD2 . TYR B 1 78 ? 8.244 36.505 55.508 1.00 16.97 ? 78 TYR B CD2 1 ATOM 1444 C CE1 . TYR B 1 78 ? 7.744 37.055 58.161 1.00 14.99 ? 78 TYR B CE1 1 ATOM 1445 C CE2 . TYR B 1 78 ? 8.263 37.817 55.942 1.00 16.05 ? 78 TYR B CE2 1 ATOM 1446 C CZ . TYR B 1 78 ? 8.012 38.080 57.274 1.00 20.30 ? 78 TYR B CZ 1 ATOM 1447 O OH . TYR B 1 78 ? 8.010 39.362 57.776 1.00 19.10 ? 78 TYR B OH 1 ATOM 1448 N N . TRP B 1 79 ? 6.101 34.495 53.358 1.00 18.51 ? 79 TRP B N 1 ATOM 1449 C CA . TRP B 1 79 ? 5.456 35.407 52.424 1.00 18.70 ? 79 TRP B CA 1 ATOM 1450 C C . TRP B 1 79 ? 3.991 35.000 52.200 1.00 16.40 ? 79 TRP B C 1 ATOM 1451 O O . TRP B 1 79 ? 3.093 35.842 52.109 1.00 19.56 ? 79 TRP B O 1 ATOM 1452 C CB . TRP B 1 79 ? 6.196 35.470 51.071 1.00 13.65 ? 79 TRP B CB 1 ATOM 1453 C CG . TRP B 1 79 ? 7.563 36.095 51.226 1.00 15.32 ? 79 TRP B CG 1 ATOM 1454 C CD1 . TRP B 1 79 ? 8.782 35.505 50.990 1.00 16.02 ? 79 TRP B CD1 1 ATOM 1455 C CD2 . TRP B 1 79 ? 7.838 37.430 51.653 1.00 16.81 ? 79 TRP B CD2 1 ATOM 1456 N NE1 . TRP B 1 79 ? 9.807 36.422 51.256 1.00 12.58 ? 79 TRP B NE1 1 ATOM 1457 C CE2 . TRP B 1 79 ? 9.256 37.593 51.659 1.00 12.47 ? 79 TRP B CE2 1 ATOM 1458 C CE3 . TRP B 1 79 ? 7.043 38.512 52.037 1.00 21.59 ? 79 TRP B CE3 1 ATOM 1459 C CZ2 . TRP B 1 79 ? 9.844 38.801 52.036 1.00 15.59 ? 79 TRP B CZ2 1 ATOM 1460 C CZ3 . TRP B 1 79 ? 7.628 39.716 52.411 1.00 20.49 ? 79 TRP B CZ3 1 ATOM 1461 C CH2 . TRP B 1 79 ? 9.030 39.836 52.399 1.00 16.58 ? 79 TRP B CH2 1 ATOM 1462 N N . LYS B 1 80 ? 3.771 33.695 52.125 1.00 15.46 ? 80 LYS B N 1 ATOM 1463 C CA . LYS B 1 80 ? 2.370 33.262 51.959 1.00 26.19 ? 80 LYS B CA 1 ATOM 1464 C C . LYS B 1 80 ? 1.511 33.754 53.115 1.00 26.97 ? 80 LYS B C 1 ATOM 1465 O O . LYS B 1 80 ? 0.367 34.157 52.904 1.00 27.31 ? 80 LYS B O 1 ATOM 1466 C CB . LYS B 1 80 ? 2.325 31.734 51.806 1.00 22.34 ? 80 LYS B CB 1 ATOM 1467 C CG . LYS B 1 80 ? 2.749 31.352 50.384 1.00 28.98 ? 80 LYS B CG 1 ATOM 1468 C CD . LYS B 1 80 ? 3.154 29.893 50.290 1.00 35.72 ? 80 LYS B CD 1 ATOM 1469 C CE . LYS B 1 80 ? 2.043 29.068 49.640 1.00 51.97 ? 80 LYS B CE 1 ATOM 1470 N NZ . LYS B 1 80 ? 1.967 27.719 50.272 1.00 71.55 ? 80 LYS B NZ 1 ATOM 1471 N N . ALA B 1 81 ? 2.028 33.762 54.341 1.00 24.98 ? 81 ALA B N 1 ATOM 1472 C CA . ALA B 1 81 ? 1.287 34.242 55.498 1.00 27.30 ? 81 ALA B CA 1 ATOM 1473 C C . ALA B 1 81 ? 0.863 35.693 55.330 1.00 26.16 ? 81 ALA B C 1 ATOM 1474 O O . ALA B 1 81 ? -0.162 36.097 55.872 1.00 38.75 ? 81 ALA B O 1 ATOM 1475 C CB . ALA B 1 81 ? 2.113 34.122 56.770 1.00 28.89 ? 81 ALA B CB 1 ATOM 1476 N N . LEU B 1 82 ? 1.666 36.456 54.596 1.00 24.27 ? 82 LEU B N 1 ATOM 1477 C CA . LEU B 1 82 ? 1.406 37.864 54.368 1.00 24.69 ? 82 LEU B CA 1 ATOM 1478 C C . LEU B 1 82 ? 0.584 38.116 53.115 1.00 32.58 ? 82 LEU B C 1 ATOM 1479 O O . LEU B 1 82 ? 0.284 39.262 52.772 1.00 32.09 ? 82 LEU B O 1 ATOM 1480 C CB . LEU B 1 82 ? 2.712 38.660 54.192 1.00 26.43 ? 82 LEU B CB 1 ATOM 1481 C CG . LEU B 1 82 ? 3.609 38.685 55.434 1.00 40.16 ? 82 LEU B CG 1 ATOM 1482 C CD1 . LEU B 1 82 ? 4.671 39.767 55.293 1.00 49.59 ? 82 LEU B CD1 1 ATOM 1483 C CD2 . LEU B 1 82 ? 2.772 38.894 56.683 1.00 35.99 ? 82 LEU B CD2 1 ATOM 1484 N N . GLY B 1 83 ? 0.241 37.053 52.391 1.00 28.03 ? 83 GLY B N 1 ATOM 1485 C CA . GLY B 1 83 ? -0.493 37.284 51.155 1.00 20.54 ? 83 GLY B CA 1 ATOM 1486 C C . GLY B 1 83 ? 0.327 37.701 49.969 1.00 25.83 ? 83 GLY B C 1 ATOM 1487 O O . GLY B 1 83 ? -0.176 38.316 49.023 1.00 25.71 ? 83 GLY B O 1 ATOM 1488 N N . ILE B 1 84 ? 1.620 37.342 49.977 1.00 24.33 ? 84 ILE B N 1 ATOM 1489 C CA . ILE B 1 84 ? 2.486 37.705 48.854 1.00 27.17 ? 84 ILE B CA 1 ATOM 1490 C C . ILE B 1 84 ? 3.049 36.459 48.193 1.00 25.45 ? 84 ILE B C 1 ATOM 1491 O O . ILE B 1 84 ? 3.546 35.543 48.857 1.00 23.48 ? 84 ILE B O 1 ATOM 1492 C CB . ILE B 1 84 ? 3.631 38.630 49.333 1.00 34.90 ? 84 ILE B CB 1 ATOM 1493 C CG1 . ILE B 1 84 ? 3.135 39.911 49.996 1.00 31.59 ? 84 ILE B CG1 1 ATOM 1494 C CG2 . ILE B 1 84 ? 4.589 38.941 48.189 1.00 31.40 ? 84 ILE B CG2 1 ATOM 1495 C CD1 . ILE B 1 84 ? 4.149 40.627 50.855 1.00 47.08 ? 84 ILE B CD1 1 ATOM 1496 N N . SER B 1 85 ? 2.965 36.375 46.873 1.00 21.93 ? 85 SER B N 1 ATOM 1497 C CA . SER B 1 85 ? 3.490 35.248 46.131 1.00 31.74 ? 85 SER B CA 1 ATOM 1498 C C . SER B 1 85 ? 5.004 35.407 45.987 1.00 26.69 ? 85 SER B C 1 ATOM 1499 O O . SER B 1 85 ? 5.460 36.345 45.340 1.00 29.84 ? 85 SER B O 1 ATOM 1500 C CB . SER B 1 85 ? 2.847 35.159 44.744 1.00 37.75 ? 85 SER B CB 1 ATOM 1501 O OG . SER B 1 85 ? 2.868 33.814 44.289 1.00 53.06 ? 85 SER B OG 1 ATOM 1502 N N . PRO B 1 86 ? 5.781 34.545 46.617 1.00 18.05 ? 86 PRO B N 1 ATOM 1503 C CA . PRO B 1 86 ? 7.245 34.725 46.558 1.00 15.84 ? 86 PRO B CA 1 ATOM 1504 C C . PRO B 1 86 ? 7.879 33.900 45.458 1.00 18.84 ? 86 PRO B C 1 ATOM 1505 O O . PRO B 1 86 ? 7.244 32.985 44.937 1.00 22.36 ? 86 PRO B O 1 ATOM 1506 C CB . PRO B 1 86 ? 7.684 34.094 47.893 1.00 20.36 ? 86 PRO B CB 1 ATOM 1507 C CG . PRO B 1 86 ? 6.785 32.901 47.926 1.00 20.62 ? 86 PRO B CG 1 ATOM 1508 C CD . PRO B 1 86 ? 5.437 33.374 47.419 1.00 21.26 ? 86 PRO B CD 1 ATOM 1509 N N . PHE B 1 87 ? 9.125 34.212 45.122 1.00 14.46 ? 87 PHE B N 1 ATOM 1510 C CA . PHE B 1 87 ? 9.802 33.440 44.084 1.00 13.86 ? 87 PHE B CA 1 ATOM 1511 C C . PHE B 1 87 ? 10.466 32.180 44.605 1.00 14.18 ? 87 PHE B C 1 ATOM 1512 O O . PHE B 1 87 ? 10.371 31.127 43.970 1.00 14.81 ? 87 PHE B O 1 ATOM 1513 C CB . PHE B 1 87 ? 10.860 34.386 43.452 1.00 12.91 ? 87 PHE B CB 1 ATOM 1514 C CG . PHE B 1 87 ? 11.699 33.663 42.396 1.00 14.47 ? 87 PHE B CG 1 ATOM 1515 C CD1 . PHE B 1 87 ? 11.165 33.411 41.148 1.00 20.70 ? 87 PHE B CD1 1 ATOM 1516 C CD2 . PHE B 1 87 ? 13.001 33.252 42.659 1.00 14.50 ? 87 PHE B CD2 1 ATOM 1517 C CE1 . PHE B 1 87 ? 11.887 32.770 40.145 1.00 14.85 ? 87 PHE B CE1 1 ATOM 1518 C CE2 . PHE B 1 87 ? 13.722 32.608 41.656 1.00 15.85 ? 87 PHE B CE2 1 ATOM 1519 C CZ . PHE B 1 87 ? 13.171 32.365 40.415 1.00 12.37 ? 87 PHE B CZ 1 ATOM 1520 N N . HIS B 1 88 ? 11.195 32.243 45.723 1.00 10.46 ? 88 HIS B N 1 ATOM 1521 C CA . HIS B 1 88 ? 12.015 31.134 46.196 1.00 14.64 ? 88 HIS B CA 1 ATOM 1522 C C . HIS B 1 88 ? 11.205 30.132 47.020 1.00 16.08 ? 88 HIS B C 1 ATOM 1523 O O . HIS B 1 88 ? 10.269 30.504 47.737 1.00 17.14 ? 88 HIS B O 1 ATOM 1524 C CB . HIS B 1 88 ? 13.174 31.647 47.073 1.00 11.20 ? 88 HIS B CB 1 ATOM 1525 C CG . HIS B 1 88 ? 14.049 32.619 46.333 1.00 14.14 ? 88 HIS B CG 1 ATOM 1526 N ND1 . HIS B 1 88 ? 13.885 33.969 46.409 1.00 14.17 ? 88 HIS B ND1 1 ATOM 1527 C CD2 . HIS B 1 88 ? 15.096 32.422 45.492 1.00 13.37 ? 88 HIS B CD2 1 ATOM 1528 C CE1 . HIS B 1 88 ? 14.781 34.602 45.657 1.00 15.91 ? 88 HIS B CE1 1 ATOM 1529 N NE2 . HIS B 1 88 ? 15.529 33.665 45.091 1.00 20.87 ? 88 HIS B NE2 1 ATOM 1530 N N . GLU B 1 89 ? 11.568 28.871 46.931 1.00 11.98 ? 89 GLU B N 1 ATOM 1531 C CA . GLU B 1 89 ? 11.015 27.819 47.800 1.00 13.59 ? 89 GLU B CA 1 ATOM 1532 C C . GLU B 1 89 ? 11.503 27.941 49.231 1.00 20.67 ? 89 GLU B C 1 ATOM 1533 O O . GLU B 1 89 ? 10.786 27.728 50.219 1.00 19.59 ? 89 GLU B O 1 ATOM 1534 C CB . GLU B 1 89 ? 11.425 26.447 47.234 1.00 19.16 ? 89 GLU B CB 1 ATOM 1535 C CG . GLU B 1 89 ? 10.643 26.044 46.002 1.00 13.91 ? 89 GLU B CG 1 ATOM 1536 C CD . GLU B 1 89 ? 9.142 26.065 46.292 1.00 20.98 ? 89 GLU B CD 1 ATOM 1537 O OE1 . GLU B 1 89 ? 8.732 25.329 47.215 1.00 24.71 ? 89 GLU B OE1 1 ATOM 1538 O OE2 . GLU B 1 89 ? 8.415 26.812 45.617 1.00 25.73 ? 89 GLU B OE2 1 ATOM 1539 N N . HIS B 1 90 ? 12.774 28.317 49.377 1.00 14.95 ? 90 HIS B N 1 ATOM 1540 C CA . HIS B 1 90 ? 13.381 28.606 50.678 1.00 16.64 ? 90 HIS B CA 1 ATOM 1541 C C . HIS B 1 90 ? 14.713 29.317 50.465 1.00 20.48 ? 90 HIS B C 1 ATOM 1542 O O . HIS B 1 90 ? 15.168 29.489 49.328 1.00 22.72 ? 90 HIS B O 1 ATOM 1543 C CB . HIS B 1 90 ? 13.599 27.336 51.502 1.00 21.77 ? 90 HIS B CB 1 ATOM 1544 C CG . HIS B 1 90 ? 14.302 26.239 50.751 1.00 30.05 ? 90 HIS B CG 1 ATOM 1545 N ND1 . HIS B 1 90 ? 13.701 25.046 50.434 1.00 31.06 ? 90 HIS B ND1 1 ATOM 1546 C CD2 . HIS B 1 90 ? 15.553 26.144 50.239 1.00 34.00 ? 90 HIS B CD2 1 ATOM 1547 C CE1 . HIS B 1 90 ? 14.550 24.280 49.768 1.00 35.83 ? 90 HIS B CE1 1 ATOM 1548 N NE2 . HIS B 1 90 ? 15.699 24.927 49.638 1.00 37.53 ? 90 HIS B NE2 1 ATOM 1549 N N . ALA B 1 91 ? 15.378 29.744 51.517 1.00 15.32 ? 91 ALA B N 1 ATOM 1550 C CA . ALA B 1 91 ? 16.729 30.305 51.367 1.00 20.05 ? 91 ALA B CA 1 ATOM 1551 C C . ALA B 1 91 ? 17.685 29.358 52.097 1.00 25.34 ? 91 ALA B C 1 ATOM 1552 O O . ALA B 1 91 ? 17.333 28.951 53.211 1.00 19.65 ? 91 ALA B O 1 ATOM 1553 C CB . ALA B 1 91 ? 16.827 31.721 51.907 1.00 17.26 ? 91 ALA B CB 1 ATOM 1554 N N . GLU B 1 92 ? 18.813 29.017 51.507 1.00 15.53 ? 92 GLU B N 1 ATOM 1555 C CA . GLU B 1 92 ? 19.762 28.072 52.067 1.00 17.79 ? 92 GLU B CA 1 ATOM 1556 C C . GLU B 1 92 ? 21.105 28.792 52.260 1.00 22.35 ? 92 GLU B C 1 ATOM 1557 O O . GLU B 1 92 ? 21.468 29.628 51.436 1.00 24.26 ? 92 GLU B O 1 ATOM 1558 C CB . GLU B 1 92 ? 20.022 26.855 51.193 1.00 30.45 ? 92 GLU B CB 1 ATOM 1559 C CG . GLU B 1 92 ? 18.837 26.376 50.385 1.00 61.98 ? 92 GLU B CG 1 ATOM 1560 C CD . GLU B 1 92 ? 18.590 24.882 50.514 1.00 74.65 ? 92 GLU B CD 1 ATOM 1561 O OE1 . GLU B 1 92 ? 18.089 24.466 51.584 1.00 86.85 ? 92 GLU B OE1 1 ATOM 1562 O OE2 . GLU B 1 92 ? 18.897 24.142 49.553 1.00 55.43 ? 92 GLU B OE2 1 ATOM 1563 N N . VAL B 1 93 ? 21.816 28.496 53.328 1.00 10.86 ? 93 VAL B N 1 ATOM 1564 C CA . VAL B 1 93 ? 23.135 29.077 53.587 1.00 8.80 ? 93 VAL B CA 1 ATOM 1565 C C . VAL B 1 93 ? 24.014 27.871 53.914 1.00 10.94 ? 93 VAL B C 1 ATOM 1566 O O . VAL B 1 93 ? 23.677 27.241 54.912 1.00 18.24 ? 93 VAL B O 1 ATOM 1567 C CB . VAL B 1 93 ? 23.115 30.052 54.766 1.00 18.71 ? 93 VAL B CB 1 ATOM 1568 C CG1 . VAL B 1 93 ? 24.517 30.603 54.986 1.00 23.88 ? 93 VAL B CG1 1 ATOM 1569 C CG2 . VAL B 1 93 ? 22.117 31.180 54.555 1.00 21.07 ? 93 VAL B CG2 1 ATOM 1570 N N . VAL B 1 94 ? 25.007 27.569 53.123 1.00 10.70 ? 94 VAL B N 1 ATOM 1571 C CA . VAL B 1 94 ? 25.854 26.404 53.307 1.00 10.45 ? 94 VAL B CA 1 ATOM 1572 C C . VAL B 1 94 ? 27.282 26.907 53.543 1.00 18.82 ? 94 VAL B C 1 ATOM 1573 O O . VAL B 1 94 ? 27.767 27.708 52.735 1.00 13.66 ? 94 VAL B O 1 ATOM 1574 C CB . VAL B 1 94 ? 25.797 25.454 52.094 1.00 15.61 ? 94 VAL B CB 1 ATOM 1575 C CG1 . VAL B 1 94 ? 26.574 24.177 52.364 1.00 19.11 ? 94 VAL B CG1 1 ATOM 1576 C CG2 . VAL B 1 94 ? 24.351 25.140 51.741 1.00 27.60 ? 94 VAL B CG2 1 ATOM 1577 N N . PHE B 1 95 ? 27.871 26.447 54.648 1.00 15.04 ? 95 PHE B N 1 ATOM 1578 C CA . PHE B 1 95 ? 29.199 26.930 55.015 1.00 15.68 ? 95 PHE B CA 1 ATOM 1579 C C . PHE B 1 95 ? 29.997 25.885 55.791 1.00 18.82 ? 95 PHE B C 1 ATOM 1580 O O . PHE B 1 95 ? 29.452 25.013 56.463 1.00 16.39 ? 95 PHE B O 1 ATOM 1581 C CB . PHE B 1 95 ? 29.064 28.212 55.852 1.00 12.18 ? 95 PHE B CB 1 ATOM 1582 C CG . PHE B 1 95 ? 28.400 28.032 57.200 1.00 16.54 ? 95 PHE B CG 1 ATOM 1583 C CD1 . PHE B 1 95 ? 27.032 27.975 57.321 1.00 20.34 ? 95 PHE B CD1 1 ATOM 1584 C CD2 . PHE B 1 95 ? 29.181 27.938 58.350 1.00 15.60 ? 95 PHE B CD2 1 ATOM 1585 C CE1 . PHE B 1 95 ? 26.403 27.825 58.548 1.00 20.28 ? 95 PHE B CE1 1 ATOM 1586 C CE2 . PHE B 1 95 ? 28.565 27.780 59.578 1.00 24.03 ? 95 PHE B CE2 1 ATOM 1587 C CZ . PHE B 1 95 ? 27.194 27.707 59.686 1.00 20.02 ? 95 PHE B CZ 1 ATOM 1588 N N . THR B 1 96 ? 31.313 26.013 55.738 1.00 18.32 ? 96 THR B N 1 ATOM 1589 C CA . THR B 1 96 ? 32.195 25.269 56.641 1.00 19.94 ? 96 THR B CA 1 ATOM 1590 C C . THR B 1 96 ? 32.400 25.977 57.966 1.00 21.38 ? 96 THR B C 1 ATOM 1591 O O . THR B 1 96 ? 32.638 27.187 58.035 1.00 23.87 ? 96 THR B O 1 ATOM 1592 C CB . THR B 1 96 ? 33.584 25.049 55.990 1.00 27.49 ? 96 THR B CB 1 ATOM 1593 O OG1 . THR B 1 96 ? 33.390 24.289 54.792 1.00 28.51 ? 96 THR B OG1 1 ATOM 1594 C CG2 . THR B 1 96 ? 34.482 24.238 56.909 1.00 27.10 ? 96 THR B CG2 1 ATOM 1595 N N . ALA B 1 97 ? 32.308 25.235 59.076 1.00 21.53 ? 97 ALA B N 1 ATOM 1596 C CA . ALA B 1 97 ? 32.733 25.810 60.363 1.00 22.57 ? 97 ALA B CA 1 ATOM 1597 C C . ALA B 1 97 ? 34.165 25.359 60.642 1.00 32.98 ? 97 ALA B C 1 ATOM 1598 O O . ALA B 1 97 ? 34.481 24.165 60.604 1.00 28.38 ? 97 ALA B O 1 ATOM 1599 C CB . ALA B 1 97 ? 31.754 25.412 61.443 1.00 31.30 ? 97 ALA B CB 1 ATOM 1600 N N . ASN B 1 98 ? 35.085 26.284 60.898 1.00 40.72 ? 98 ASN B N 1 ATOM 1601 C CA . ASN B 1 98 ? 36.486 25.943 61.153 1.00 35.61 ? 98 ASN B CA 1 ATOM 1602 C C . ASN B 1 98 ? 36.870 26.420 62.539 1.00 45.62 ? 98 ASN B C 1 ATOM 1603 O O . ASN B 1 98 ? 36.504 27.555 62.859 1.00 51.20 ? 98 ASN B O 1 ATOM 1604 C CB . ASN B 1 98 ? 37.419 26.578 60.123 1.00 49.43 ? 98 ASN B CB 1 ATOM 1605 C CG . ASN B 1 98 ? 37.649 25.635 58.952 1.00 69.74 ? 98 ASN B CG 1 ATOM 1606 O OD1 . ASN B 1 98 ? 37.644 24.417 59.143 1.00 94.41 ? 98 ASN B OD1 1 ATOM 1607 N ND2 . ASN B 1 98 ? 37.840 26.184 57.758 1.00 87.72 ? 98 ASN B ND2 1 ATOM 1608 N N . ASP B 1 99 ? 37.555 25.612 63.343 1.00 49.07 ? 99 ASP B N 1 ATOM 1609 C CA . ASP B 1 99 ? 37.814 26.047 64.722 1.00 42.00 ? 99 ASP B CA 1 ATOM 1610 C C . ASP B 1 99 ? 38.953 27.053 64.760 1.00 45.92 ? 99 ASP B C 1 ATOM 1611 O O . ASP B 1 99 ? 38.935 27.965 65.579 1.00 69.63 ? 99 ASP B O 1 ATOM 1612 C CB . ASP B 1 99 ? 38.102 24.842 65.621 1.00 42.67 ? 99 ASP B CB 1 ATOM 1613 C CG . ASP B 1 99 ? 36.762 24.346 66.160 1.00 41.34 ? 99 ASP B CG 1 ATOM 1614 O OD1 . ASP B 1 99 ? 35.880 25.187 66.410 1.00 66.24 ? 99 ASP B OD1 1 ATOM 1615 O OD2 . ASP B 1 99 ? 36.616 23.130 66.319 1.00 54.52 ? 99 ASP B OD2 1 ATOM 1616 N N . SER B 1 100 ? 39.868 26.820 63.840 1.00 54.48 ? 100 SER B N 1 ATOM 1617 C CA . SER B 1 100 ? 40.915 27.718 63.395 1.00 77.19 ? 100 SER B CA 1 ATOM 1618 C C . SER B 1 100 ? 40.520 29.176 63.618 1.00 87.17 ? 100 SER B C 1 ATOM 1619 O O . SER B 1 100 ? 40.884 29.801 64.623 1.00 88.40 ? 100 SER B O 1 ATOM 1620 C CB . SER B 1 100 ? 41.201 27.438 61.912 1.00 75.82 ? 100 SER B CB 1 ATOM 1621 O OG . SER B 1 100 ? 40.293 26.465 61.398 1.00 54.52 ? 100 SER B OG 1 ATOM 1622 N N . GLY B 1 101 ? 39.751 29.731 62.681 1.00 87.96 ? 101 GLY B N 1 ATOM 1623 C CA . GLY B 1 101 ? 39.284 31.097 62.766 1.00 87.71 ? 101 GLY B CA 1 ATOM 1624 C C . GLY B 1 101 ? 38.431 31.390 63.987 1.00 88.74 ? 101 GLY B C 1 ATOM 1625 O O . GLY B 1 101 ? 38.516 30.714 65.010 1.00 70.88 ? 101 GLY B O 1 ATOM 1626 N N . PRO B 1 102 ? 37.595 32.420 63.866 1.00 89.60 ? 102 PRO B N 1 ATOM 1627 C CA . PRO B 1 102 ? 36.763 32.907 64.965 1.00 84.20 ? 102 PRO B CA 1 ATOM 1628 C C . PRO B 1 102 ? 35.710 31.894 65.408 1.00 67.57 ? 102 PRO B C 1 ATOM 1629 O O . PRO B 1 102 ? 35.416 30.922 64.722 1.00 43.41 ? 102 PRO B O 1 ATOM 1630 C CB . PRO B 1 102 ? 36.077 34.146 64.378 1.00 91.73 ? 102 PRO B CB 1 ATOM 1631 C CG . PRO B 1 102 ? 36.875 34.505 63.169 1.00 92.54 ? 102 PRO B CG 1 ATOM 1632 C CD . PRO B 1 102 ? 37.389 33.199 62.628 1.00 91.68 ? 102 PRO B CD 1 ATOM 1633 N N . ARG B 1 103 ? 35.132 32.129 66.580 1.00 59.17 ? 103 ARG B N 1 ATOM 1634 C CA . ARG B 1 103 ? 34.255 31.170 67.226 1.00 57.66 ? 103 ARG B CA 1 ATOM 1635 C C . ARG B 1 103 ? 32.770 31.451 67.075 1.00 41.14 ? 103 ARG B C 1 ATOM 1636 O O . ARG B 1 103 ? 31.982 30.500 67.095 1.00 45.32 ? 103 ARG B O 1 ATOM 1637 C CB . ARG B 1 103 ? 34.581 31.132 68.732 1.00 68.17 ? 103 ARG B CB 1 ATOM 1638 C CG . ARG B 1 103 ? 35.696 32.075 69.145 1.00 77.69 ? 103 ARG B CG 1 ATOM 1639 C CD . ARG B 1 103 ? 36.932 31.305 69.587 1.00 88.02 ? 103 ARG B CD 1 ATOM 1640 N NE . ARG B 1 103 ? 37.534 30.549 68.490 1.00 91.79 ? 103 ARG B NE 1 ATOM 1641 C CZ . ARG B 1 103 ? 38.833 30.538 68.219 1.00 90.59 ? 103 ARG B CZ 1 ATOM 1642 N NH1 . ARG B 1 103 ? 39.678 31.237 68.964 1.00 94.44 ? 103 ARG B NH1 1 ATOM 1643 N NH2 . ARG B 1 103 ? 39.302 29.826 67.205 1.00 71.43 ? 103 ARG B NH2 1 ATOM 1644 N N . ARG B 1 104 ? 32.344 32.707 66.941 1.00 28.51 ? 104 ARG B N 1 ATOM 1645 C CA . ARG B 1 104 ? 30.903 32.960 66.908 1.00 26.68 ? 104 ARG B CA 1 ATOM 1646 C C . ARG B 1 104 ? 30.427 33.294 65.491 1.00 30.78 ? 104 ARG B C 1 ATOM 1647 O O . ARG B 1 104 ? 31.038 34.100 64.784 1.00 26.13 ? 104 ARG B O 1 ATOM 1648 C CB . ARG B 1 104 ? 30.522 34.075 67.874 1.00 27.86 ? 104 ARG B CB 1 ATOM 1649 C CG . ARG B 1 104 ? 30.772 33.763 69.344 1.00 49.98 ? 104 ARG B CG 1 ATOM 1650 C CD . ARG B 1 104 ? 30.705 35.015 70.203 1.00 65.36 ? 104 ARG B CD 1 ATOM 1651 N NE . ARG B 1 104 ? 29.420 35.146 70.889 1.00 82.50 ? 104 ARG B NE 1 ATOM 1652 C CZ . ARG B 1 104 ? 29.214 35.981 71.903 1.00 93.81 ? 104 ARG B CZ 1 ATOM 1653 N NH1 . ARG B 1 104 ? 30.211 36.746 72.332 1.00 101.76 ? 104 ARG B NH1 1 ATOM 1654 N NH2 . ARG B 1 104 ? 28.027 36.059 72.489 1.00 103.21 ? 104 ARG B NH2 1 ATOM 1655 N N . TYR B 1 105 ? 29.321 32.658 65.100 1.00 18.17 ? 105 TYR B N 1 ATOM 1656 C CA . TYR B 1 105 ? 28.836 32.855 63.731 1.00 21.11 ? 105 TYR B CA 1 ATOM 1657 C C . TYR B 1 105 ? 27.458 33.490 63.784 1.00 23.92 ? 105 TYR B C 1 ATOM 1658 O O . TYR B 1 105 ? 26.546 32.889 64.368 1.00 21.60 ? 105 TYR B O 1 ATOM 1659 C CB . TYR B 1 105 ? 28.739 31.540 62.959 1.00 20.60 ? 105 TYR B CB 1 ATOM 1660 C CG . TYR B 1 105 ? 30.032 30.815 62.698 1.00 23.02 ? 105 TYR B CG 1 ATOM 1661 C CD1 . TYR B 1 105 ? 30.650 30.056 63.685 1.00 31.34 ? 105 TYR B CD1 1 ATOM 1662 C CD2 . TYR B 1 105 ? 30.636 30.903 61.446 1.00 24.41 ? 105 TYR B CD2 1 ATOM 1663 C CE1 . TYR B 1 105 ? 31.843 29.394 63.436 1.00 34.44 ? 105 TYR B CE1 1 ATOM 1664 C CE2 . TYR B 1 105 ? 31.817 30.242 61.197 1.00 27.84 ? 105 TYR B CE2 1 ATOM 1665 C CZ . TYR B 1 105 ? 32.414 29.495 62.183 1.00 27.85 ? 105 TYR B CZ 1 ATOM 1666 O OH . TYR B 1 105 ? 33.590 28.852 61.895 1.00 32.75 ? 105 TYR B OH 1 ATOM 1667 N N . THR B 1 106 ? 27.305 34.668 63.198 1.00 20.44 ? 106 THR B N 1 ATOM 1668 C CA . THR B 1 106 ? 25.956 35.235 63.083 1.00 13.14 ? 106 THR B CA 1 ATOM 1669 C C . THR B 1 106 ? 25.547 35.172 61.615 1.00 19.08 ? 106 THR B C 1 ATOM 1670 O O . THR B 1 106 ? 26.255 35.764 60.805 1.00 20.10 ? 106 THR B O 1 ATOM 1671 C CB . THR B 1 106 ? 25.891 36.678 63.578 1.00 23.51 ? 106 THR B CB 1 ATOM 1672 O OG1 . THR B 1 106 ? 26.266 36.642 64.973 1.00 31.60 ? 106 THR B OG1 1 ATOM 1673 C CG2 . THR B 1 106 ? 24.495 37.260 63.481 1.00 25.71 ? 106 THR B CG2 1 ATOM 1674 N N . ILE B 1 107 ? 24.481 34.445 61.322 1.00 20.56 ? 107 ILE B N 1 ATOM 1675 C CA . ILE B 1 107 ? 23.984 34.371 59.947 1.00 15.40 ? 107 ILE B CA 1 ATOM 1676 C C . ILE B 1 107 ? 22.804 35.324 59.796 1.00 20.86 ? 107 ILE B C 1 ATOM 1677 O O . ILE B 1 107 ? 21.832 35.123 60.511 1.00 17.87 ? 107 ILE B O 1 ATOM 1678 C CB . ILE B 1 107 ? 23.503 32.968 59.561 1.00 18.10 ? 107 ILE B CB 1 ATOM 1679 C CG1 . ILE B 1 107 ? 24.570 31.889 59.730 1.00 31.38 ? 107 ILE B CG1 1 ATOM 1680 C CG2 . ILE B 1 107 ? 22.934 33.018 58.139 1.00 21.72 ? 107 ILE B CG2 1 ATOM 1681 C CD1 . ILE B 1 107 ? 25.929 32.299 59.219 1.00 34.28 ? 107 ILE B CD1 1 ATOM 1682 N N . ALA B 1 108 ? 22.899 36.305 58.905 1.00 14.34 ? 108 ALA B N 1 ATOM 1683 C CA . ALA B 1 108 ? 21.741 37.182 58.752 1.00 12.29 ? 108 ALA B CA 1 ATOM 1684 C C . ALA B 1 108 ? 21.170 37.067 57.344 1.00 17.79 ? 108 ALA B C 1 ATOM 1685 O O . ALA B 1 108 ? 21.825 36.806 56.338 1.00 17.23 ? 108 ALA B O 1 ATOM 1686 C CB . ALA B 1 108 ? 22.086 38.616 59.085 1.00 20.20 ? 108 ALA B CB 1 ATOM 1687 N N . ALA B 1 109 ? 19.850 37.252 57.256 1.00 11.98 ? 109 ALA B N 1 ATOM 1688 C CA . ALA B 1 109 ? 19.175 37.082 55.987 1.00 10.63 ? 109 ALA B CA 1 ATOM 1689 C C . ALA B 1 109 ? 18.198 38.252 55.834 1.00 17.40 ? 109 ALA B C 1 ATOM 1690 O O . ALA B 1 109 ? 17.484 38.500 56.801 1.00 18.78 ? 109 ALA B O 1 ATOM 1691 C CB . ALA B 1 109 ? 18.385 35.789 55.894 1.00 18.23 ? 109 ALA B CB 1 ATOM 1692 N N . LEU B 1 110 ? 18.205 38.896 54.688 1.00 12.67 ? 110 LEU B N 1 ATOM 1693 C CA . LEU B 1 110 ? 17.302 40.006 54.422 1.00 11.51 ? 110 LEU B CA 1 ATOM 1694 C C . LEU B 1 110 ? 16.358 39.595 53.304 1.00 12.68 ? 110 LEU B C 1 ATOM 1695 O O . LEU B 1 110 ? 16.880 39.303 52.229 1.00 10.59 ? 110 LEU B O 1 ATOM 1696 C CB . LEU B 1 110 ? 18.084 41.254 54.043 1.00 15.02 ? 110 LEU B CB 1 ATOM 1697 C CG . LEU B 1 110 ? 17.251 42.471 53.641 1.00 21.35 ? 110 LEU B CG 1 ATOM 1698 C CD1 . LEU B 1 110 ? 16.417 43.019 54.786 1.00 21.55 ? 110 LEU B CD1 1 ATOM 1699 C CD2 . LEU B 1 110 ? 18.160 43.576 53.111 1.00 41.42 ? 110 LEU B CD2 1 ATOM 1700 N N . LEU B 1 111 ? 15.050 39.589 53.567 1.00 11.03 ? 111 LEU B N 1 ATOM 1701 C CA . LEU B 1 111 ? 14.120 38.954 52.638 1.00 13.07 ? 111 LEU B CA 1 ATOM 1702 C C . LEU B 1 111 ? 13.256 39.930 51.858 1.00 13.65 ? 111 LEU B C 1 ATOM 1703 O O . LEU B 1 111 ? 12.687 40.835 52.468 1.00 11.58 ? 111 LEU B O 1 ATOM 1704 C CB . LEU B 1 111 ? 13.162 38.023 53.402 1.00 12.55 ? 111 LEU B CB 1 ATOM 1705 C CG . LEU B 1 111 ? 13.788 37.010 54.345 1.00 15.54 ? 111 LEU B CG 1 ATOM 1706 C CD1 . LEU B 1 111 ? 12.682 36.109 54.905 1.00 17.00 ? 111 LEU B CD1 1 ATOM 1707 C CD2 . LEU B 1 111 ? 14.894 36.196 53.661 1.00 13.51 ? 111 LEU B CD2 1 ATOM 1708 N N . SER B 1 112 ? 13.132 39.680 50.559 1.00 11.12 ? 112 SER B N 1 ATOM 1709 C CA . SER B 1 112 ? 12.118 40.307 49.727 1.00 8.75 ? 112 SER B CA 1 ATOM 1710 C C . SER B 1 112 ? 11.435 39.173 48.951 1.00 13.50 ? 112 SER B C 1 ATOM 1711 O O . SER B 1 112 ? 11.977 38.074 48.888 1.00 14.11 ? 112 SER B O 1 ATOM 1712 C CB . SER B 1 112 ? 12.683 41.349 48.771 1.00 12.04 ? 112 SER B CB 1 ATOM 1713 O OG . SER B 1 112 ? 13.208 42.472 49.472 1.00 20.96 ? 112 SER B OG 1 ATOM 1714 N N . PRO B 1 113 ? 10.257 39.420 48.370 1.00 14.36 ? 113 PRO B N 1 ATOM 1715 C CA . PRO B 1 113 ? 9.578 38.349 47.641 1.00 11.81 ? 113 PRO B CA 1 ATOM 1716 C C . PRO B 1 113 ? 10.421 37.786 46.510 1.00 14.53 ? 113 PRO B C 1 ATOM 1717 O O . PRO B 1 113 ? 10.375 36.561 46.321 1.00 10.04 ? 113 PRO B O 1 ATOM 1718 C CB . PRO B 1 113 ? 8.303 39.041 47.114 1.00 10.98 ? 113 PRO B CB 1 ATOM 1719 C CG . PRO B 1 113 ? 8.073 40.124 48.137 1.00 17.62 ? 113 PRO B CG 1 ATOM 1720 C CD . PRO B 1 113 ? 9.469 40.658 48.418 1.00 13.10 ? 113 PRO B CD 1 ATOM 1721 N N . TYR B 1 114 ? 11.182 38.575 45.756 1.00 11.48 ? 114 TYR B N 1 ATOM 1722 C CA . TYR B 1 114 ? 11.936 38.055 44.626 1.00 10.53 ? 114 TYR B CA 1 ATOM 1723 C C . TYR B 1 114 ? 13.450 38.177 44.821 1.00 13.19 ? 114 TYR B C 1 ATOM 1724 O O . TYR B 1 114 ? 14.184 38.033 43.836 1.00 13.25 ? 114 TYR B O 1 ATOM 1725 C CB . TYR B 1 114 ? 11.566 38.789 43.330 1.00 10.44 ? 114 TYR B CB 1 ATOM 1726 C CG . TYR B 1 114 ? 10.270 38.213 42.766 1.00 10.72 ? 114 TYR B CG 1 ATOM 1727 C CD1 . TYR B 1 114 ? 9.081 38.701 43.324 1.00 21.04 ? 114 TYR B CD1 1 ATOM 1728 C CD2 . TYR B 1 114 ? 10.255 37.262 41.765 1.00 11.82 ? 114 TYR B CD2 1 ATOM 1729 C CE1 . TYR B 1 114 ? 7.881 38.208 42.848 1.00 27.72 ? 114 TYR B CE1 1 ATOM 1730 C CE2 . TYR B 1 114 ? 9.044 36.756 41.279 1.00 14.45 ? 114 TYR B CE2 1 ATOM 1731 C CZ . TYR B 1 114 ? 7.881 37.257 41.848 1.00 26.36 ? 114 TYR B CZ 1 ATOM 1732 O OH . TYR B 1 114 ? 6.651 36.805 41.413 1.00 35.67 ? 114 TYR B OH 1 ATOM 1733 N N . SER B 1 115 ? 13.889 38.460 46.039 1.00 12.16 ? 115 SER B N 1 ATOM 1734 C CA . SER B 1 115 ? 15.338 38.588 46.232 1.00 14.21 ? 115 SER B CA 1 ATOM 1735 C C . SER B 1 115 ? 15.698 38.280 47.662 1.00 17.50 ? 115 SER B C 1 ATOM 1736 O O . SER B 1 115 ? 14.920 38.600 48.568 1.00 14.75 ? 115 SER B O 1 ATOM 1737 C CB A SER B 1 115 ? 15.784 40.014 45.886 0.33 14.52 ? 115 SER B CB 1 ATOM 1738 C CB B SER B 1 115 ? 15.823 39.999 45.867 0.67 14.44 ? 115 SER B CB 1 ATOM 1739 O OG A SER B 1 115 ? 15.611 40.820 47.045 0.33 20.68 ? 115 SER B OG 1 ATOM 1740 O OG B SER B 1 115 ? 17.188 40.149 46.235 0.67 12.81 ? 115 SER B OG 1 ATOM 1741 N N . TYR B 1 116 ? 16.854 37.678 47.923 1.00 11.94 ? 116 TYR B N 1 ATOM 1742 C CA . TYR B 1 116 ? 17.266 37.684 49.323 1.00 9.10 ? 116 TYR B CA 1 ATOM 1743 C C . TYR B 1 116 ? 18.785 37.925 49.384 1.00 11.73 ? 116 TYR B C 1 ATOM 1744 O O . TYR B 1 116 ? 19.466 37.694 48.390 1.00 13.82 ? 116 TYR B O 1 ATOM 1745 C CB . TYR B 1 116 ? 16.881 36.448 50.100 1.00 12.36 ? 116 TYR B CB 1 ATOM 1746 C CG . TYR B 1 116 ? 17.515 35.141 49.704 1.00 17.24 ? 116 TYR B CG 1 ATOM 1747 C CD1 . TYR B 1 116 ? 18.750 34.720 50.180 1.00 21.01 ? 116 TYR B CD1 1 ATOM 1748 C CD2 . TYR B 1 116 ? 16.832 34.303 48.814 1.00 23.07 ? 116 TYR B CD2 1 ATOM 1749 C CE1 . TYR B 1 116 ? 19.323 33.503 49.800 1.00 15.91 ? 116 TYR B CE1 1 ATOM 1750 C CE2 . TYR B 1 116 ? 17.376 33.095 48.431 1.00 20.03 ? 116 TYR B CE2 1 ATOM 1751 C CZ . TYR B 1 116 ? 18.603 32.705 48.919 1.00 25.35 ? 116 TYR B CZ 1 ATOM 1752 O OH . TYR B 1 116 ? 19.086 31.487 48.496 1.00 40.53 ? 116 TYR B OH 1 ATOM 1753 N N . SER B 1 117 ? 19.214 38.427 50.529 1.00 10.31 ? 117 SER B N 1 ATOM 1754 C CA . SER B 1 117 ? 20.629 38.694 50.742 1.00 12.85 ? 117 SER B CA 1 ATOM 1755 C C . SER B 1 117 ? 21.031 37.998 52.028 1.00 15.76 ? 117 SER B C 1 ATOM 1756 O O . SER B 1 117 ? 20.261 37.948 52.985 1.00 15.69 ? 117 SER B O 1 ATOM 1757 C CB A SER B 1 117 ? 20.944 40.185 50.799 0.38 17.79 ? 117 SER B CB 1 ATOM 1758 C CB B SER B 1 117 ? 20.914 40.193 50.857 0.62 17.22 ? 117 SER B CB 1 ATOM 1759 O OG A SER B 1 117 ? 20.379 40.798 51.937 0.38 29.13 ? 117 SER B OG 1 ATOM 1760 O OG B SER B 1 117 ? 20.500 40.876 49.685 0.62 15.31 ? 117 SER B OG 1 ATOM 1761 N N . THR B 1 118 ? 22.237 37.430 52.040 1.00 10.69 ? 118 THR B N 1 ATOM 1762 C CA . THR B 1 118 ? 22.578 36.786 53.317 1.00 12.51 ? 118 THR B CA 1 ATOM 1763 C C . THR B 1 118 ? 24.020 37.187 53.593 1.00 20.20 ? 118 THR B C 1 ATOM 1764 O O . THR B 1 118 ? 24.785 37.380 52.655 1.00 15.25 ? 118 THR B O 1 ATOM 1765 C CB . THR B 1 118 ? 22.362 35.281 53.309 1.00 15.18 ? 118 THR B CB 1 ATOM 1766 O OG1 . THR B 1 118 ? 22.729 34.773 54.605 1.00 22.89 ? 118 THR B OG1 1 ATOM 1767 C CG2 . THR B 1 118 ? 23.249 34.527 52.337 1.00 16.30 ? 118 THR B CG2 1 ATOM 1768 N N A MET B 1 119 ? 24.349 37.312 54.866 0.60 9.20 ? 119 MET B N 1 ATOM 1769 C CA A MET B 1 119 ? 25.648 37.830 55.300 0.60 11.33 ? 119 MET B CA 1 ATOM 1770 C C A MET B 1 119 ? 26.071 37.021 56.519 0.60 15.44 ? 119 MET B C 1 ATOM 1771 O O A MET B 1 119 ? 25.236 36.550 57.295 0.60 16.39 ? 119 MET B O 1 ATOM 1772 C CB A MET B 1 119 ? 25.548 39.316 55.608 0.60 12.79 ? 119 MET B CB 1 ATOM 1773 C CG A MET B 1 119 ? 26.530 39.926 56.597 0.60 14.37 ? 119 MET B CG 1 ATOM 1774 S SD A MET B 1 119 ? 28.120 40.263 55.833 0.60 35.85 ? 119 MET B SD 1 ATOM 1775 C CE A MET B 1 119 ? 29.044 41.114 57.111 0.60 9.77 ? 119 MET B CE 1 ATOM 1776 N N B THR B 1 119 ? 24.342 37.323 54.867 0.40 12.18 ? 119 THR B N 1 ATOM 1777 C CA B THR B 1 119 ? 25.697 37.740 55.220 0.40 11.71 ? 119 THR B CA 1 ATOM 1778 C C B THR B 1 119 ? 26.074 37.026 56.511 0.40 14.45 ? 119 THR B C 1 ATOM 1779 O O B THR B 1 119 ? 25.224 36.646 57.314 0.40 16.25 ? 119 THR B O 1 ATOM 1780 C CB B THR B 1 119 ? 25.789 39.253 55.357 0.40 12.10 ? 119 THR B CB 1 ATOM 1781 O OG1 B THR B 1 119 ? 27.535 39.827 55.430 0.40 15.10 ? 119 THR B OG1 1 ATOM 1782 C CG2 B THR B 1 119 ? 25.174 39.669 56.791 0.40 8.37 ? 119 THR B CG2 1 ATOM 1783 N N . ALA B 1 120 ? 27.373 36.836 56.675 1.00 10.14 ? 120 ALA B N 1 ATOM 1784 C CA . ALA B 1 120 ? 27.850 36.154 57.878 1.00 12.08 ? 120 ALA B CA 1 ATOM 1785 C C . ALA B 1 120 ? 28.763 37.128 58.595 1.00 15.59 ? 120 ALA B C 1 ATOM 1786 O O . ALA B 1 120 ? 29.591 37.748 57.926 1.00 15.04 ? 120 ALA B O 1 ATOM 1787 C CB . ALA B 1 120 ? 28.579 34.861 57.538 1.00 18.27 ? 120 ALA B CB 1 ATOM 1788 N N . VAL B 1 121 ? 28.582 37.230 59.902 1.00 18.02 ? 121 VAL B N 1 ATOM 1789 C CA . VAL B 1 121 ? 29.575 37.928 60.718 1.00 16.82 ? 121 VAL B CA 1 ATOM 1790 C C . VAL B 1 121 ? 30.243 36.855 61.589 1.00 18.38 ? 121 VAL B C 1 ATOM 1791 O O . VAL B 1 121 ? 29.566 36.111 62.296 1.00 21.54 ? 121 VAL B O 1 ATOM 1792 C CB . VAL B 1 121 ? 28.965 39.020 61.594 1.00 21.87 ? 121 VAL B CB 1 ATOM 1793 C CG1 . VAL B 1 121 ? 30.062 39.892 62.188 1.00 31.95 ? 121 VAL B CG1 1 ATOM 1794 C CG2 . VAL B 1 121 ? 27.967 39.862 60.806 1.00 31.33 ? 121 VAL B CG2 1 ATOM 1795 N N . VAL B 1 122 ? 31.553 36.774 61.504 1.00 23.29 ? 122 VAL B N 1 ATOM 1796 C CA . VAL B 1 122 ? 32.306 35.773 62.271 1.00 25.94 ? 122 VAL B CA 1 ATOM 1797 C C . VAL B 1 122 ? 33.200 36.506 63.258 1.00 31.10 ? 122 VAL B C 1 ATOM 1798 O O . VAL B 1 122 ? 34.052 37.277 62.836 1.00 23.83 ? 122 VAL B O 1 ATOM 1799 C CB . VAL B 1 122 ? 33.070 34.862 61.305 1.00 29.82 ? 122 VAL B CB 1 ATOM 1800 C CG1 . VAL B 1 122 ? 33.804 33.745 62.022 1.00 41.69 ? 122 VAL B CG1 1 ATOM 1801 C CG2 . VAL B 1 122 ? 32.071 34.298 60.284 1.00 30.01 ? 122 VAL B CG2 1 ATOM 1802 N N . THR B 1 123 ? 32.969 36.298 64.549 1.00 35.47 ? 123 THR B N 1 ATOM 1803 C CA . THR B 1 123 ? 33.686 37.036 65.578 1.00 34.15 ? 123 THR B CA 1 ATOM 1804 C C . THR B 1 123 ? 34.100 36.111 66.724 1.00 35.70 ? 123 THR B C 1 ATOM 1805 O O . THR B 1 123 ? 34.035 34.889 66.569 1.00 35.96 ? 123 THR B O 1 ATOM 1806 C CB . THR B 1 123 ? 32.850 38.182 66.170 1.00 36.05 ? 123 THR B CB 1 ATOM 1807 O OG1 . THR B 1 123 ? 31.634 37.653 66.727 1.00 37.89 ? 123 THR B OG1 1 ATOM 1808 C CG2 . THR B 1 123 ? 32.467 39.186 65.089 1.00 45.31 ? 123 THR B CG2 1 HETATM 1809 O O . HOH C 2 . ? 30.069 34.876 47.382 1.00 13.08 ? 128 HOH A O 1 HETATM 1810 O O . HOH C 2 . ? 31.759 31.374 48.470 1.00 14.05 ? 129 HOH A O 1 HETATM 1811 O O . HOH C 2 . ? 30.854 33.495 50.132 1.00 15.68 ? 130 HOH A O 1 HETATM 1812 O O . HOH C 2 . ? 25.002 29.251 50.767 1.00 17.59 ? 131 HOH A O 1 HETATM 1813 O O . HOH C 2 . ? 33.195 28.415 40.096 1.00 17.38 ? 132 HOH A O 1 HETATM 1814 O O . HOH C 2 . ? 7.345 16.152 35.763 1.00 23.05 ? 133 HOH A O 1 HETATM 1815 O O . HOH C 2 . ? 10.098 19.064 39.961 1.00 22.31 ? 134 HOH A O 1 HETATM 1816 O O . HOH C 2 . ? 8.706 30.709 41.593 1.00 26.34 ? 135 HOH A O 1 HETATM 1817 O O . HOH C 2 . ? 18.597 28.831 28.880 1.00 26.58 ? 136 HOH A O 1 HETATM 1818 O O . HOH C 2 . ? 17.189 34.659 42.693 1.00 29.48 ? 137 HOH A O 1 HETATM 1819 O O . HOH C 2 . ? 23.630 19.507 36.714 1.00 22.68 ? 138 HOH A O 1 HETATM 1820 O O . HOH C 2 . ? 4.619 30.084 35.448 1.00 33.44 ? 139 HOH A O 1 HETATM 1821 O O . HOH C 2 . ? 13.768 37.146 32.348 1.00 28.30 ? 140 HOH A O 1 HETATM 1822 O O . HOH C 2 . ? 27.563 40.921 47.715 1.00 27.82 ? 141 HOH A O 1 HETATM 1823 O O . HOH C 2 . ? 35.946 37.305 37.236 1.00 28.40 ? 142 HOH A O 1 HETATM 1824 O O . HOH C 2 . ? 36.254 47.012 37.582 1.00 28.40 ? 143 HOH A O 1 HETATM 1825 O O . HOH C 2 . ? 38.288 33.331 39.940 1.00 31.55 ? 144 HOH A O 1 HETATM 1826 O O . HOH C 2 . ? 32.466 27.234 53.382 1.00 36.91 ? 145 HOH A O 1 HETATM 1827 O O . HOH C 2 . ? 25.421 41.001 49.145 1.00 28.37 ? 146 HOH A O 1 HETATM 1828 O O . HOH C 2 . ? 29.048 30.761 29.054 1.00 36.40 ? 147 HOH A O 1 HETATM 1829 O O . HOH C 2 . ? 9.857 28.821 29.666 1.00 30.40 ? 148 HOH A O 1 HETATM 1830 O O . HOH C 2 . ? 25.500 18.434 37.529 1.00 32.69 ? 149 HOH A O 1 HETATM 1831 O O . HOH C 2 . ? 26.810 31.758 27.931 1.00 33.39 ? 150 HOH A O 1 HETATM 1832 O O . HOH C 2 . ? 35.629 29.632 39.342 1.00 33.72 ? 151 HOH A O 1 HETATM 1833 O O . HOH C 2 . ? 32.964 29.339 55.979 1.00 36.70 ? 152 HOH A O 1 HETATM 1834 O O . HOH C 2 . ? 27.354 24.605 28.952 1.00 47.12 ? 153 HOH A O 1 HETATM 1835 O O . HOH C 2 . ? 35.261 27.269 36.636 1.00 45.02 ? 154 HOH A O 1 HETATM 1836 O O . HOH C 2 . ? 26.143 18.591 33.241 1.00 40.21 ? 155 HOH A O 1 HETATM 1837 O O . HOH C 2 . ? 38.629 46.770 45.275 1.00 39.70 ? 156 HOH A O 1 HETATM 1838 O O . HOH C 2 . ? 22.252 15.265 42.487 1.00 57.93 ? 157 HOH A O 1 HETATM 1839 O O . HOH C 2 . ? 25.758 17.048 39.345 1.00 48.07 ? 158 HOH A O 1 HETATM 1840 O O . HOH C 2 . ? 27.681 17.905 35.409 1.00 55.02 ? 159 HOH A O 1 HETATM 1841 O O . HOH C 2 . ? 25.460 27.439 27.718 1.00 46.82 ? 160 HOH A O 1 HETATM 1842 O O . HOH C 2 . ? 7.382 31.377 38.239 1.00 35.33 ? 161 HOH A O 1 HETATM 1843 O O . HOH C 2 . ? 38.599 46.717 40.332 1.00 42.40 ? 162 HOH A O 1 HETATM 1844 O O . HOH C 2 . ? 6.031 37.156 29.697 1.00 58.96 ? 163 HOH A O 1 HETATM 1845 O O . HOH C 2 . ? 17.171 21.346 28.691 1.00 49.17 ? 164 HOH A O 1 HETATM 1846 O O . HOH C 2 . ? 6.172 23.995 43.733 1.00 41.84 ? 165 HOH A O 1 HETATM 1847 O O . HOH C 2 . ? 13.633 16.023 36.959 1.00 40.09 ? 166 HOH A O 1 HETATM 1848 O O . HOH C 2 . ? 11.905 24.120 22.374 1.00 43.69 ? 167 HOH A O 1 HETATM 1849 O O . HOH C 2 . ? 23.946 18.711 34.156 1.00 37.23 ? 168 HOH A O 1 HETATM 1850 O O . HOH C 2 . ? 8.951 41.471 34.489 1.00 41.23 ? 169 HOH A O 1 HETATM 1851 O O . HOH C 2 . ? 16.370 19.666 49.350 1.00 50.93 ? 170 HOH A O 1 HETATM 1852 O O . HOH C 2 . ? 21.259 30.627 48.844 1.00 29.36 ? 171 HOH A O 1 HETATM 1853 O O . HOH C 2 . ? 40.976 35.021 52.619 1.00 44.55 ? 172 HOH A O 1 HETATM 1854 O O . HOH C 2 . ? 38.579 35.193 55.015 1.00 53.25 ? 173 HOH A O 1 HETATM 1855 O O . HOH C 2 . ? 7.151 35.471 28.408 1.00 54.63 ? 174 HOH A O 1 HETATM 1856 O O . HOH C 2 . ? 30.941 21.791 49.479 1.00 58.76 ? 175 HOH A O 1 HETATM 1857 O O . HOH C 2 . ? 13.373 30.873 23.145 1.00 78.21 ? 176 HOH A O 1 HETATM 1858 O O . HOH C 2 . ? 28.479 42.818 32.400 1.00 55.52 ? 177 HOH A O 1 HETATM 1859 O O . HOH C 2 . ? 13.124 27.617 23.614 1.00 58.05 ? 178 HOH A O 1 HETATM 1860 O O . HOH C 2 . ? 39.736 27.790 42.397 1.00 52.10 ? 179 HOH A O 1 HETATM 1861 O O . HOH C 2 . ? 27.166 35.450 27.838 1.00 62.69 ? 180 HOH A O 1 HETATM 1862 O O . HOH C 2 . ? 16.588 15.757 33.398 1.00 68.77 ? 181 HOH A O 1 HETATM 1863 O O . HOH C 2 . ? 43.254 30.623 47.301 1.00 50.38 ? 182 HOH A O 1 HETATM 1864 O O . HOH C 2 . ? 38.240 42.103 37.588 1.00 44.00 ? 183 HOH A O 1 HETATM 1865 O O . HOH C 2 . ? 19.403 14.319 45.699 1.00 66.77 ? 184 HOH A O 1 HETATM 1866 O O . HOH D 2 . ? 16.791 29.827 47.151 1.00 15.31 ? 128 HOH B O 1 HETATM 1867 O O . HOH D 2 . ? 12.661 35.907 50.456 1.00 16.61 ? 129 HOH B O 1 HETATM 1868 O O . HOH D 2 . ? 11.654 34.767 47.858 1.00 17.52 ? 130 HOH B O 1 HETATM 1869 O O . HOH D 2 . ? 10.407 32.582 49.421 1.00 15.46 ? 131 HOH B O 1 HETATM 1870 O O . HOH D 2 . ? 25.260 34.109 55.364 1.00 23.67 ? 132 HOH B O 1 HETATM 1871 O O . HOH D 2 . ? 8.825 28.677 44.268 1.00 19.72 ? 133 HOH B O 1 HETATM 1872 O O . HOH D 2 . ? 8.438 29.929 57.883 1.00 23.43 ? 134 HOH B O 1 HETATM 1873 O O . HOH D 2 . ? 16.014 41.537 50.135 1.00 27.25 ? 135 HOH B O 1 HETATM 1874 O O . HOH D 2 . ? 23.327 28.637 69.046 1.00 30.94 ? 136 HOH B O 1 HETATM 1875 O O . HOH D 2 . ? 30.228 17.754 58.101 1.00 30.96 ? 137 HOH B O 1 HETATM 1876 O O . HOH D 2 . ? 7.213 39.579 60.522 1.00 30.09 ? 138 HOH B O 1 HETATM 1877 O O . HOH D 2 . ? 29.496 36.610 65.403 1.00 41.75 ? 139 HOH B O 1 HETATM 1878 O O . HOH D 2 . ? 12.126 28.040 68.228 1.00 37.18 ? 140 HOH B O 1 HETATM 1879 O O . HOH D 2 . ? 34.132 27.231 65.041 1.00 49.60 ? 141 HOH B O 1 HETATM 1880 O O . HOH D 2 . ? 8.241 48.613 60.283 1.00 34.14 ? 142 HOH B O 1 HETATM 1881 O O . HOH D 2 . ? 18.080 41.613 48.738 1.00 38.16 ? 143 HOH B O 1 HETATM 1882 O O . HOH D 2 . ? 17.021 20.226 61.459 1.00 37.17 ? 144 HOH B O 1 HETATM 1883 O O . HOH D 2 . ? 33.890 24.608 64.628 1.00 44.37 ? 145 HOH B O 1 HETATM 1884 O O . HOH D 2 . ? 5.592 48.686 57.186 1.00 45.97 ? 146 HOH B O 1 HETATM 1885 O O . HOH D 2 . ? 34.414 29.427 59.425 1.00 44.85 ? 147 HOH B O 1 HETATM 1886 O O . HOH D 2 . ? 5.487 48.086 52.862 1.00 49.34 ? 148 HOH B O 1 HETATM 1887 O O . HOH D 2 . ? 6.611 32.096 58.962 1.00 38.16 ? 149 HOH B O 1 HETATM 1888 O O . HOH D 2 . ? 18.123 21.245 49.056 1.00 58.00 ? 150 HOH B O 1 HETATM 1889 O O . HOH D 2 . ? 15.680 25.604 69.007 1.00 49.54 ? 151 HOH B O 1 HETATM 1890 O O . HOH D 2 . ? 6.122 28.861 61.555 1.00 39.05 ? 152 HOH B O 1 HETATM 1891 O O . HOH D 2 . ? 35.317 22.079 53.601 1.00 53.63 ? 153 HOH B O 1 HETATM 1892 O O . HOH D 2 . ? 6.240 30.222 44.981 1.00 56.61 ? 154 HOH B O 1 HETATM 1893 O O . HOH D 2 . ? 34.776 17.589 76.376 1.00 49.91 ? 155 HOH B O 1 HETATM 1894 O O . HOH D 2 . ? 13.261 31.924 69.031 1.00 38.78 ? 156 HOH B O 1 HETATM 1895 O O . HOH D 2 . ? 4.339 35.741 57.729 1.00 41.46 ? 157 HOH B O 1 HETATM 1896 O O . HOH D 2 . ? 35.913 27.848 67.144 1.00 60.44 ? 158 HOH B O 1 HETATM 1897 O O . HOH D 2 . ? 36.314 39.569 62.887 1.00 54.79 ? 159 HOH B O 1 HETATM 1898 O O . HOH D 2 . ? 16.402 27.909 70.151 1.00 43.80 ? 160 HOH B O 1 HETATM 1899 O O . HOH D 2 . ? 9.053 36.274 70.180 1.00 51.18 ? 161 HOH B O 1 HETATM 1900 O O . HOH D 2 . ? 29.285 23.615 75.384 1.00 61.15 ? 162 HOH B O 1 HETATM 1901 O O . HOH D 2 . ? 5.271 26.864 51.885 1.00 60.22 ? 163 HOH B O 1 HETATM 1902 O O . HOH D 2 . ? 33.150 23.764 68.931 1.00 62.03 ? 164 HOH B O 1 HETATM 1903 O O . HOH D 2 . ? 41.209 23.551 62.061 1.00 57.83 ? 165 HOH B O 1 HETATM 1904 O O . HOH D 2 . ? 37.744 22.399 52.151 1.00 62.32 ? 166 HOH B O 1 HETATM 1905 O O . HOH D 2 . ? 36.963 29.242 60.831 1.00 62.82 ? 167 HOH B O 1 HETATM 1906 O O . HOH D 2 . ? 8.044 32.710 67.160 1.00 55.42 ? 168 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 MET 30 30 30 MET MET A . y A 1 30 VAL 30 30 30 VAL VAL A . y 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 GLU 63 63 63 GLU GLU 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 MET 119 119 119 MET MET A . y A 1 119 THR 119 119 119 THR THR A . y 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 ? ? ? A . n A 1 125 PRO 125 125 ? ? ? A . n A 1 126 LYS 126 126 ? ? ? A . n A 1 127 GLU 127 127 ? ? ? 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 MET 30 30 30 MET MET B . y B 1 30 VAL 30 30 30 VAL VAL B . y 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 GLU 63 63 63 GLU GLU 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 MET 119 119 119 MET MET B . y B 1 119 THR 119 119 119 THR THR B . y 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 B 1 125 PRO 125 125 ? ? ? B . n B 1 126 LYS 126 126 ? ? ? B . n B 1 127 GLU 127 127 ? ? ? B . n # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code C 2 HOH 1 128 2 HOH HOH A . C 2 HOH 2 129 3 HOH HOH A . C 2 HOH 3 130 4 HOH HOH A . C 2 HOH 4 131 7 HOH HOH A . C 2 HOH 5 132 9 HOH HOH A . C 2 HOH 6 133 10 HOH HOH A . C 2 HOH 7 134 13 HOH HOH A . C 2 HOH 8 135 14 HOH HOH A . C 2 HOH 9 136 15 HOH HOH A . C 2 HOH 10 137 17 HOH HOH A . C 2 HOH 11 138 18 HOH HOH A . C 2 HOH 12 139 19 HOH HOH A . C 2 HOH 13 140 20 HOH HOH A . C 2 HOH 14 141 21 HOH HOH A . C 2 HOH 15 142 24 HOH HOH A . C 2 HOH 16 143 25 HOH HOH A . C 2 HOH 17 144 28 HOH HOH A . C 2 HOH 18 145 34 HOH HOH A . C 2 HOH 19 146 35 HOH HOH A . C 2 HOH 20 147 36 HOH HOH A . C 2 HOH 21 148 37 HOH HOH A . C 2 HOH 22 149 39 HOH HOH A . C 2 HOH 23 150 40 HOH HOH A . C 2 HOH 24 151 42 HOH HOH A . C 2 HOH 25 152 43 HOH HOH A . C 2 HOH 26 153 45 HOH HOH A . C 2 HOH 27 154 46 HOH HOH A . C 2 HOH 28 155 49 HOH HOH A . C 2 HOH 29 156 50 HOH HOH A . C 2 HOH 30 157 51 HOH HOH A . C 2 HOH 31 158 54 HOH HOH A . C 2 HOH 32 159 57 HOH HOH A . C 2 HOH 33 160 59 HOH HOH A . C 2 HOH 34 161 60 HOH HOH A . C 2 HOH 35 162 62 HOH HOH A . C 2 HOH 36 163 63 HOH HOH A . C 2 HOH 37 164 64 HOH HOH A . C 2 HOH 38 165 65 HOH HOH A . C 2 HOH 39 166 66 HOH HOH A . C 2 HOH 40 167 67 HOH HOH A . C 2 HOH 41 168 68 HOH HOH A . C 2 HOH 42 169 69 HOH HOH A . C 2 HOH 43 170 73 HOH HOH A . C 2 HOH 44 171 74 HOH HOH A . C 2 HOH 45 172 75 HOH HOH A . C 2 HOH 46 173 79 HOH HOH A . C 2 HOH 47 174 80 HOH HOH A . C 2 HOH 48 175 82 HOH HOH A . C 2 HOH 49 176 84 HOH HOH A . C 2 HOH 50 177 85 HOH HOH A . C 2 HOH 51 178 89 HOH HOH A . C 2 HOH 52 179 91 HOH HOH A . C 2 HOH 53 180 93 HOH HOH A . C 2 HOH 54 181 97 HOH HOH A . C 2 HOH 55 182 98 HOH HOH A . C 2 HOH 56 183 99 HOH HOH A . C 2 HOH 57 184 103 HOH HOH A . D 2 HOH 1 128 1 HOH HOH B . D 2 HOH 2 129 5 HOH HOH B . D 2 HOH 3 130 6 HOH HOH B . D 2 HOH 4 131 8 HOH HOH B . D 2 HOH 5 132 11 HOH HOH B . D 2 HOH 6 133 12 HOH HOH B . D 2 HOH 7 134 16 HOH HOH B . D 2 HOH 8 135 22 HOH HOH B . D 2 HOH 9 136 23 HOH HOH B . D 2 HOH 10 137 26 HOH HOH B . D 2 HOH 11 138 27 HOH HOH B . D 2 HOH 12 139 29 HOH HOH B . D 2 HOH 13 140 30 HOH HOH B . D 2 HOH 14 141 31 HOH HOH B . D 2 HOH 15 142 32 HOH HOH B . D 2 HOH 16 143 33 HOH HOH B . D 2 HOH 17 144 38 HOH HOH B . D 2 HOH 18 145 41 HOH HOH B . D 2 HOH 19 146 44 HOH HOH B . D 2 HOH 20 147 47 HOH HOH B . D 2 HOH 21 148 48 HOH HOH B . D 2 HOH 22 149 52 HOH HOH B . D 2 HOH 23 150 53 HOH HOH B . D 2 HOH 24 151 55 HOH HOH B . D 2 HOH 25 152 56 HOH HOH B . D 2 HOH 26 153 70 HOH HOH B . D 2 HOH 27 154 72 HOH HOH B . D 2 HOH 28 155 76 HOH HOH B . D 2 HOH 29 156 77 HOH HOH B . D 2 HOH 30 157 78 HOH HOH B . D 2 HOH 31 158 83 HOH HOH B . D 2 HOH 32 159 86 HOH HOH B . D 2 HOH 33 160 87 HOH HOH B . D 2 HOH 34 161 88 HOH HOH B . D 2 HOH 35 162 90 HOH HOH B . D 2 HOH 36 163 92 HOH HOH B . D 2 HOH 37 164 94 HOH HOH B . D 2 HOH 38 165 96 HOH HOH B . D 2 HOH 39 166 100 HOH HOH B . D 2 HOH 40 167 101 HOH HOH B . D 2 HOH 41 168 102 HOH HOH B . # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_and_software_defined_assembly _pdbx_struct_assembly.method_details PISA,PQS _pdbx_struct_assembly.oligomeric_details tetrameric _pdbx_struct_assembly.oligomeric_count 4 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1,2 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D # loop_ _pdbx_struct_assembly_prop.biol_id _pdbx_struct_assembly_prop.type _pdbx_struct_assembly_prop.value _pdbx_struct_assembly_prop.details 1 'ABSA (A^2)' 6360 ? 1 MORE -55 ? 1 'SSA (A^2)' 19160 ? # 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 43.7700000000 0.0000000000 -1.0000000000 0.0000000000 86.3100000000 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 2001-07-25 2 'Structure model' 1 1 2008-04-27 3 'Structure model' 1 2 2011-07-13 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # loop_ _pdbx_audit_revision_group.ordinal _pdbx_audit_revision_group.revision_ordinal _pdbx_audit_revision_group.data_content_type _pdbx_audit_revision_group.group 1 2 'Structure model' 'Version format compliance' 2 3 'Structure model' 'Derived calculations' 3 3 'Structure model' 'Version format compliance' # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal X-PLOR 'model building' . ? 1 SHELXL-97 refinement . ? 2 DENZO 'data reduction' . ? 3 SCALEPACK 'data scaling' . ? 4 X-PLOR phasing . ? 5 # loop_ _pdbx_validate_rmsd_bond.id _pdbx_validate_rmsd_bond.PDB_model_num _pdbx_validate_rmsd_bond.auth_atom_id_1 _pdbx_validate_rmsd_bond.auth_asym_id_1 _pdbx_validate_rmsd_bond.auth_comp_id_1 _pdbx_validate_rmsd_bond.auth_seq_id_1 _pdbx_validate_rmsd_bond.PDB_ins_code_1 _pdbx_validate_rmsd_bond.label_alt_id_1 _pdbx_validate_rmsd_bond.auth_atom_id_2 _pdbx_validate_rmsd_bond.auth_asym_id_2 _pdbx_validate_rmsd_bond.auth_comp_id_2 _pdbx_validate_rmsd_bond.auth_seq_id_2 _pdbx_validate_rmsd_bond.PDB_ins_code_2 _pdbx_validate_rmsd_bond.label_alt_id_2 _pdbx_validate_rmsd_bond.bond_value _pdbx_validate_rmsd_bond.bond_target_value _pdbx_validate_rmsd_bond.bond_deviation _pdbx_validate_rmsd_bond.bond_standard_deviation _pdbx_validate_rmsd_bond.linker_flag 1 1 CB A VAL 30 ? B CG2 A VAL 30 ? B 1.779 1.524 0.255 0.021 N 2 1 CB A THR 119 ? B OG1 A THR 119 ? B 1.170 1.428 -0.258 0.020 N 3 1 CB B VAL 30 ? B CG2 B VAL 30 ? B 1.779 1.524 0.255 0.021 N 4 1 CB B THR 119 ? B OG1 B THR 119 ? B 1.839 1.428 0.411 0.020 N # loop_ _pdbx_validate_rmsd_angle.id _pdbx_validate_rmsd_angle.PDB_model_num _pdbx_validate_rmsd_angle.auth_atom_id_1 _pdbx_validate_rmsd_angle.auth_asym_id_1 _pdbx_validate_rmsd_angle.auth_comp_id_1 _pdbx_validate_rmsd_angle.auth_seq_id_1 _pdbx_validate_rmsd_angle.PDB_ins_code_1 _pdbx_validate_rmsd_angle.label_alt_id_1 _pdbx_validate_rmsd_angle.auth_atom_id_2 _pdbx_validate_rmsd_angle.auth_asym_id_2 _pdbx_validate_rmsd_angle.auth_comp_id_2 _pdbx_validate_rmsd_angle.auth_seq_id_2 _pdbx_validate_rmsd_angle.PDB_ins_code_2 _pdbx_validate_rmsd_angle.label_alt_id_2 _pdbx_validate_rmsd_angle.auth_atom_id_3 _pdbx_validate_rmsd_angle.auth_asym_id_3 _pdbx_validate_rmsd_angle.auth_comp_id_3 _pdbx_validate_rmsd_angle.auth_seq_id_3 _pdbx_validate_rmsd_angle.PDB_ins_code_3 _pdbx_validate_rmsd_angle.label_alt_id_3 _pdbx_validate_rmsd_angle.angle_value _pdbx_validate_rmsd_angle.angle_target_value _pdbx_validate_rmsd_angle.angle_deviation _pdbx_validate_rmsd_angle.angle_standard_deviation _pdbx_validate_rmsd_angle.linker_flag 1 1 CG1 A VAL 30 ? B CB A VAL 30 ? B CG2 A VAL 30 ? B 121.96 110.90 11.06 1.60 N 2 1 CB A TYR 116 ? ? CG A TYR 116 ? ? CD1 A TYR 116 ? ? 125.42 121.00 4.42 0.60 N 3 1 CA B VAL 30 ? B CB B VAL 30 ? B CG1 B VAL 30 ? B 121.00 110.90 10.10 1.50 N 4 1 CA B VAL 30 ? B CB B VAL 30 ? B CG2 B VAL 30 ? B 121.86 110.90 10.96 1.50 N 5 1 CB B TYR 114 ? ? CG B TYR 114 ? ? CD1 B TYR 114 ? ? 116.23 121.00 -4.77 0.60 N # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 ALA B 37 ? ? -58.23 99.27 2 1 ASP B 38 ? ? 151.55 -26.98 3 1 PHE B 44 ? ? -130.76 -44.95 4 1 SER B 100 ? ? -25.75 -82.94 # 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 A ASN 124 ? A ASN 124 11 1 Y 1 A PRO 125 ? A PRO 125 12 1 Y 1 A LYS 126 ? A LYS 126 13 1 Y 1 A GLU 127 ? A GLU 127 14 1 Y 1 B GLY 1 ? B GLY 1 15 1 Y 1 B PRO 2 ? B PRO 2 16 1 Y 1 B THR 3 ? B THR 3 17 1 Y 1 B GLY 4 ? B GLY 4 18 1 Y 1 B THR 5 ? B THR 5 19 1 Y 1 B GLY 6 ? B GLY 6 20 1 Y 1 B GLU 7 ? B GLU 7 21 1 Y 1 B SER 8 ? B SER 8 22 1 Y 1 B LYS 9 ? B LYS 9 23 1 Y 1 B ASN 124 ? B ASN 124 24 1 Y 1 B PRO 125 ? B PRO 125 25 1 Y 1 B LYS 126 ? B LYS 126 26 1 Y 1 B GLU 127 ? B GLU 127 # _pdbx_entity_nonpoly.entity_id 2 _pdbx_entity_nonpoly.name water _pdbx_entity_nonpoly.comp_id HOH #