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*** ***elNémo ID: 230405144641106419Job options:ID = 230405144641106419 JOBID = USERID = unknown PRIVAT = 0 NMODES = 5 DQMIN = -100 DQMAX = 100 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = 0 DORMSD = 0 NRBL = 0 CUTOFF = 10 CAONLY = 0 Input data for this run:data_1AJX # _entry.id 1AJX # _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 1AJX WWPDB D_1000170908 # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 1AJX _pdbx_database_status.recvd_initial_deposition_date 1997-05-11 _pdbx_database_status.deposit_site ? _pdbx_database_status.process_site ? _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.SG_entry ? _pdbx_database_status.pdb_format_compatible Y _pdbx_database_status.status_code_cs ? # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Backbro, K.' 1 'Unge, T.' 2 # _citation.id primary _citation.title 'Unexpected binding mode of a cyclic sulfamide HIV-1 protease inhibitor.' _citation.journal_abbrev J.Med.Chem. _citation.journal_volume 40 _citation.page_first 898 _citation.page_last 902 _citation.year 1997 _citation.journal_id_ASTM JMCMAR _citation.country US _citation.journal_id_ISSN 0022-2623 _citation.journal_id_CSD 0151 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 9083478 _citation.pdbx_database_id_DOI 10.1021/jm960588d # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Backbro, K.' 1 primary 'Lowgren, S.' 2 primary 'Osterlund, K.' 3 primary 'Atepo, J.' 4 primary 'Unge, T.' 5 primary 'Hulten, J.' 6 primary 'Bonham, N.M.' 7 primary 'Schaal, W.' 8 primary 'Karlen, A.' 9 primary 'Hallberg, A.' 10 # _cell.entry_id 1AJX _cell.length_a 59.000 _cell.length_b 86.800 _cell.length_c 46.800 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 90.00 _cell.Z_PDB 8 _cell.pdbx_unique_axis ? # _symmetry.entry_id 1AJX _symmetry.space_group_name_H-M 'P 21 21 2' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 18 # loop_ _entity.id _entity.type _entity.src_method _entity.pdbx_description _entity.formula_weight _entity.pdbx_number_of_molecules _entity.pdbx_ec _entity.pdbx_mutation _entity.pdbx_fragment _entity.details 1 polymer man 'HIV-1 PROTEASE' 10803.756 2 3.4.23.16 ? ? ? 2 non-polymer syn AHA001 538.633 1 ? ? ? ? 3 water nat water 18.015 111 ? ? ? ? # _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 ;PQITLWQRPLVTIKIGGQLKEALLDTGADDTVLEEMSLPGRWKPKMIGGIGGFIKVRQYDQILIEICGHKAIGTVLVGPT PVNIIGRNLLTQIGCTLNF ; _entity_poly.pdbx_seq_one_letter_code_can ;PQITLWQRPLVTIKIGGQLKEALLDTGADDTVLEEMSLPGRWKPKMIGGIGGFIKVRQYDQILIEICGHKAIGTVLVGPT PVNIIGRNLLTQIGCTLNF ; _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 PRO n 1 2 GLN n 1 3 ILE n 1 4 THR n 1 5 LEU n 1 6 TRP n 1 7 GLN n 1 8 ARG n 1 9 PRO n 1 10 LEU n 1 11 VAL n 1 12 THR n 1 13 ILE n 1 14 LYS n 1 15 ILE n 1 16 GLY n 1 17 GLY n 1 18 GLN n 1 19 LEU n 1 20 LYS n 1 21 GLU n 1 22 ALA n 1 23 LEU n 1 24 LEU n 1 25 ASP n 1 26 THR n 1 27 GLY n 1 28 ALA n 1 29 ASP n 1 30 ASP n 1 31 THR n 1 32 VAL n 1 33 LEU n 1 34 GLU n 1 35 GLU n 1 36 MET n 1 37 SER n 1 38 LEU n 1 39 PRO n 1 40 GLY n 1 41 ARG n 1 42 TRP n 1 43 LYS n 1 44 PRO n 1 45 LYS n 1 46 MET n 1 47 ILE n 1 48 GLY n 1 49 GLY n 1 50 ILE n 1 51 GLY n 1 52 GLY n 1 53 PHE n 1 54 ILE n 1 55 LYS n 1 56 VAL n 1 57 ARG n 1 58 GLN n 1 59 TYR n 1 60 ASP n 1 61 GLN n 1 62 ILE n 1 63 LEU n 1 64 ILE n 1 65 GLU n 1 66 ILE n 1 67 CYS n 1 68 GLY n 1 69 HIS n 1 70 LYS n 1 71 ALA n 1 72 ILE n 1 73 GLY n 1 74 THR n 1 75 VAL n 1 76 LEU n 1 77 VAL n 1 78 GLY n 1 79 PRO n 1 80 THR n 1 81 PRO n 1 82 VAL n 1 83 ASN n 1 84 ILE n 1 85 ILE n 1 86 GLY n 1 87 ARG n 1 88 ASN n 1 89 LEU n 1 90 LEU n 1 91 THR n 1 92 GLN n 1 93 ILE n 1 94 GLY n 1 95 CYS n 1 96 THR n 1 97 LEU n 1 98 ASN n 1 99 PHE n # _entity_src_gen.entity_id 1 _entity_src_gen.pdbx_src_id 1 _entity_src_gen.pdbx_alt_source_flag sample _entity_src_gen.pdbx_seq_type ? _entity_src_gen.pdbx_beg_seq_num ? _entity_src_gen.pdbx_end_seq_num ? _entity_src_gen.gene_src_common_name ? _entity_src_gen.gene_src_genus Lentivirus _entity_src_gen.pdbx_gene_src_gene PROTEASE _entity_src_gen.gene_src_species ? _entity_src_gen.gene_src_strain BH10 _entity_src_gen.gene_src_tissue ? _entity_src_gen.gene_src_tissue_fraction ? _entity_src_gen.gene_src_details ? _entity_src_gen.pdbx_gene_src_fragment ? _entity_src_gen.pdbx_gene_src_scientific_name 'Human immunodeficiency virus 1' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 11676 _entity_src_gen.pdbx_gene_src_variant ? _entity_src_gen.pdbx_gene_src_cell_line BL21 _entity_src_gen.pdbx_gene_src_atcc ? _entity_src_gen.pdbx_gene_src_organ ? _entity_src_gen.pdbx_gene_src_organelle ? _entity_src_gen.pdbx_gene_src_cell ? _entity_src_gen.pdbx_gene_src_cellular_location ? _entity_src_gen.host_org_common_name ? _entity_src_gen.pdbx_host_org_scientific_name 'Escherichia coli BL21(DE3)' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 469008 _entity_src_gen.host_org_genus Escherichia _entity_src_gen.pdbx_host_org_gene PROTEASE _entity_src_gen.pdbx_host_org_organ ? _entity_src_gen.host_org_species 'Escherichia coli' _entity_src_gen.pdbx_host_org_tissue ? _entity_src_gen.pdbx_host_org_tissue_fraction ? _entity_src_gen.pdbx_host_org_strain 'BL21 (DE3)' _entity_src_gen.pdbx_host_org_variant ? _entity_src_gen.pdbx_host_org_cell_line ? _entity_src_gen.pdbx_host_org_atcc ? _entity_src_gen.pdbx_host_org_culture_collection ? _entity_src_gen.pdbx_host_org_cell ? _entity_src_gen.pdbx_host_org_organelle ? _entity_src_gen.pdbx_host_org_cellular_location ? _entity_src_gen.pdbx_host_org_vector_type ? _entity_src_gen.pdbx_host_org_vector ? _entity_src_gen.host_org_details ? _entity_src_gen.expression_system_id ? _entity_src_gen.plasmid_name PET11C _entity_src_gen.plasmid_details ? _entity_src_gen.pdbx_description ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code POL_HV1B1 _struct_ref.entity_id 1 _struct_ref.pdbx_db_accession P03366 _struct_ref.pdbx_align_begin 1 _struct_ref.pdbx_seq_one_letter_code ;FFREDLAFLQGKAREFSSEQTRANSPTISSEQTRANSPTRRELQVWGRDNNSPSEAGADRQGTVSFNFPQITLWQRPLVT IKIGGQLKEALLDTGADDTVLEEMSLPGRWKPKMIGGIGGFIKVRQYDQILIEICGHKAIGTVLVGPTPVNIIGRNLLTQ IGCTLNFPISPIETVPVKLKPGMDGPKVKQWPLTEEKIKALVEICTEMEKEGKISKIGPENPYNTPVFAIKKKDSTKWRK LVDFRELNKRTQDFWEVQLGIPHPAGLKKKKSVTVLDVGDAYFSVPLDEDFRKYTAFTIPSINNETPGIRYQYNVLPQGW KGSPAIFQSSMTKILEPFKKQNPDIVIYQYMDDLYVGSDLEIGQHRTKIEELRQHLLRWGLTTPDKKHQKEPPFLWMGYE LHPDKWTVQPIVLPEKDSWTVNDIQKLVGKLNWASQIYPGIKVRQLCKLLRGTKALTEVIPLTEEAELELAENREILKEP VHGVYYDPSKDLIAEIQKQGQGQWTYQIYQEPFKNLKTGKYARMRGAHTNDVKQLTEAVQKITTESIVIWGKTPKFKLPI QKETWETWWTEYWQATWIPEWEFVNTPPLVKLWYQLEKEPIVGAETFYVDGAANRETKLGKAGYVTNKGRQKVVPLTNTT NQKTELQAIYLALQDSGLEVNIVTDSQYALGIIQAQPDKSESELVNQIIEQLIKKEKVYLAWVPAHKGIGGNEQVDKLVS AGIRKILFLDGIDKAQDEHEKYHSNWRAMASDFNLPPVVAKEIVASCDKCQLKGEAMHGQVDCSPGIWQLDCTHLEGKVI LVAVHVASGYIEAEVIPAETGQETAYFLLKLAGRWPVKTIHTDNGSNFTSATVKAACWWAGIKQEFGIPYNPQSQGVVES MNKELKKIIGQVRDQAEHLKTAVQMAVFIHNFKRKGGIGGYSAGERIVDIIATDIQTKELQKQITKIQNFRVYYRDSRNP LWKGPAKLLWKGEGAVVIQDNSDIKVVPRRKAKIIRDYGKQMAGDDCVASRQDED ; _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 1AJX A 1 ? 99 ? P03366 69 ? 167 ? 1 99 2 1 1AJX B 1 ? 99 ? P03366 69 ? 167 ? 1 99 # 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 AH1 non-polymer . AHA001 '(4R,5S, 6S, 7R)-1,3-DIBENZYL-4,7-BIS(PHENOXYMETHYL)-5,6-DIHYDROXY-1,3 DIAZEPAN-2-ONE' 'C33 H34 N2 O5' 538.633 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 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 # _exptl.entry_id 1AJX _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 2 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.8 _exptl_crystal.density_percent_sol 55.62 _exptl_crystal.description ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method 'VAPOR DIFFUSION' _exptl_crystal_grow.temp 277 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 5.5 _exptl_crystal_grow.pdbx_pH_range ? _exptl_crystal_grow.pdbx_details ;CRYSTALLIZATION WAS PERFORMED BY VAPOR DIFFUSION. PROTEASE (2 MG/ML) AND INHIBITOR (40 MM IN DMSO) WAS MIXED IN A RATIO OF 1:1 AND SUBJECTED TO COCRYSTALLIZATION. DROPS CONSISTING OF 5 MICROLITERS OF THE PROTEASE-INHIBITOR MIXTURE PLUS 5 MICROLITERS OF THE CRYSTALLIZATION BUFFER (50 MM MES PH 5.5, 0.4 M NACL AND 0.02% (W/V) NAN3) WERE EQUILIBRATED AGAINST THE SAME BUFFER AT 4 DEGREES C., vapor diffusion, temperature 277K ; # _diffrn.id 1 _diffrn.ambient_temp 278 _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 1996-04 _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator ? _diffrn_radiation.pdbx_diffrn_protocol ? _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 0.92 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'SRS BEAMLINE PX9.5' _diffrn_source.pdbx_synchrotron_site SRS _diffrn_source.pdbx_synchrotron_beamline PX9.5 _diffrn_source.pdbx_wavelength 0.92 _diffrn_source.pdbx_wavelength_list ? # _reflns.entry_id 1AJX _reflns.observed_criterion_sigma_I 2. _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 25.0 _reflns.d_resolution_high 2.0 _reflns.number_obs 14634 _reflns.number_all ? _reflns.percent_possible_obs 84.3 _reflns.pdbx_Rmerge_I_obs 0.0500000 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI ? _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy ? _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 # _reflns_shell.d_res_high 2.00 _reflns_shell.d_res_low 2.07 _reflns_shell.percent_possible_all 48. _reflns_shell.Rmerge_I_obs 0.1780000 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs ? _reflns_shell.pdbx_redundancy ? _reflns_shell.pdbx_diffrn_id ? _reflns_shell.pdbx_ordinal 1 # _refine.entry_id 1AJX _refine.ls_number_reflns_obs 14634 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F 2.0 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 8.00 _refine.ls_d_res_high 2.00 _refine.ls_percent_reflns_obs 84.3 _refine.ls_R_factor_obs 0.1610000 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.1610000 _refine.ls_R_factor_R_free 0.2370000 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 10. _refine.ls_number_reflns_R_free ? _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.B_iso_mean 21. _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 THROUGHOUT _refine.details ? _refine.pdbx_starting_model 'PDB ENTRY 1AJV' _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values ? _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_overall_ESU_R ? _refine.pdbx_overall_ESU_R_Free ? _refine.overall_SU_ML ? _refine.overall_SU_B ? _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.correlation_coeff_Fo_to_Fc ? _refine.correlation_coeff_Fo_to_Fc_free ? _refine.pdbx_solvent_vdw_probe_radii ? _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii ? _refine.pdbx_overall_phase_error ? _refine.overall_SU_R_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 1846 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 40 _refine_hist.number_atoms_solvent 112 _refine_hist.number_atoms_total 1998 _refine_hist.d_res_high 2.00 _refine_hist.d_res_low 8.00 # loop_ _refine_ls_restr.type _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.number _refine_ls_restr.pdbx_refine_id _refine_ls_restr.pdbx_restraint_function x_bond_d 0.025 ? ? ? 'X-RAY DIFFRACTION' ? x_bond_d_na ? ? ? ? 'X-RAY DIFFRACTION' ? x_bond_d_prot ? ? ? ? 'X-RAY DIFFRACTION' ? x_angle_d ? ? ? ? 'X-RAY DIFFRACTION' ? x_angle_d_na ? ? ? ? 'X-RAY DIFFRACTION' ? x_angle_d_prot ? ? ? ? 'X-RAY DIFFRACTION' ? x_angle_deg 2.43 ? ? ? 'X-RAY DIFFRACTION' ? x_angle_deg_na ? ? ? ? 'X-RAY DIFFRACTION' ? x_angle_deg_prot ? ? ? ? 'X-RAY DIFFRACTION' ? x_dihedral_angle_d 26.9 ? ? ? 'X-RAY DIFFRACTION' ? x_dihedral_angle_d_na ? ? ? ? 'X-RAY DIFFRACTION' ? x_dihedral_angle_d_prot ? ? ? ? 'X-RAY DIFFRACTION' ? x_improper_angle_d 1.9 ? ? ? 'X-RAY DIFFRACTION' ? x_improper_angle_d_na ? ? ? ? 'X-RAY DIFFRACTION' ? x_improper_angle_d_prot ? ? ? ? 'X-RAY DIFFRACTION' ? x_mcbond_it ? ? ? ? 'X-RAY DIFFRACTION' ? x_mcangle_it ? ? ? ? 'X-RAY DIFFRACTION' ? x_scbond_it ? ? ? ? 'X-RAY DIFFRACTION' ? x_scangle_it ? ? ? ? 'X-RAY DIFFRACTION' ? # _refine_ls_shell.pdbx_total_number_of_bins_used 10 _refine_ls_shell.d_res_high 2.00 _refine_ls_shell.d_res_low 2.07 _refine_ls_shell.number_reflns_R_work 1323 _refine_ls_shell.R_factor_R_work 0.1780000 _refine_ls_shell.percent_reflns_obs 77.5 _refine_ls_shell.R_factor_R_free ? _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free ? _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? # loop_ _pdbx_xplor_file.serial_no _pdbx_xplor_file.param_file _pdbx_xplor_file.topol_file _pdbx_xplor_file.pdbx_refine_id 1 PARHCSDX.PRO TOPHCSDX.PRO 'X-RAY DIFFRACTION' 2 AHA001.PAR AHA001.TOP 'X-RAY DIFFRACTION' # _struct.entry_id 1AJX _struct.title 'HIV-1 PROTEASE IN COMPLEX WITH THE CYCLIC UREA INHIBITOR AHA001' _struct.pdbx_descriptor 'HIV-1 PROTEASE, AHA001' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 1AJX _struct_keywords.pdbx_keywords 'ASPARTYL PROTEASE' _struct_keywords.text 'PROTEASE, ASPARTYL PROTEASE, NON-PEPTIDE INHIBITOR, DRUG DESIGN, HIV-1' # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 1 ? C N N 2 ? D N N 3 ? E N N 3 ? # _struct_biol.id 1 # 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 ARG A 87 ? LEU A 90 ? ARG A 87 LEU A 90 1 ? 4 HELX_P HELX_P2 2 ARG B 87 ? LEU B 90 ? ARG B 87 LEU B 90 1 ? 4 # _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 ? 2 ? B ? 3 ? C ? 2 ? D ? 4 ? E ? 3 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense A 1 2 ? anti-parallel B 1 2 ? anti-parallel B 2 3 ? anti-parallel C 1 2 ? anti-parallel D 1 2 ? anti-parallel D 2 3 ? anti-parallel D 3 4 ? anti-parallel E 1 2 ? anti-parallel E 2 3 ? anti-parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id A 1 LEU A 10 ? ILE A 15 ? LEU A 10 ILE A 15 A 2 GLN A 18 ? LEU A 23 ? GLN A 18 LEU A 23 B 1 LYS A 43 ? GLY A 49 ? LYS A 43 GLY A 49 B 2 GLY A 52 ? TYR A 59 ? GLY A 52 TYR A 59 B 3 VAL A 75 ? GLY A 78 ? VAL A 75 GLY A 78 C 1 ILE A 62 ? ILE A 66 ? ILE A 62 ILE A 66 C 2 HIS A 69 ? GLY A 73 ? HIS A 69 GLY A 73 D 1 GLN B 18 ? LEU B 23 ? GLN B 18 LEU B 23 D 2 LEU B 10 ? ILE B 15 ? LEU B 10 ILE B 15 D 3 ILE B 62 ? ILE B 66 ? ILE B 62 ILE B 66 D 4 HIS B 69 ? GLY B 73 ? HIS B 69 GLY B 73 E 1 LYS B 43 ? GLY B 49 ? LYS B 43 GLY B 49 E 2 GLY B 52 ? TYR B 59 ? GLY B 52 TYR B 59 E 3 VAL B 75 ? VAL B 77 ? VAL B 75 VAL B 77 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id A 1 2 O VAL A 11 ? O VAL A 11 N ALA A 22 ? N ALA A 22 B 1 2 O LYS A 43 ? O LYS A 43 N GLN A 58 ? N GLN A 58 B 2 3 O ARG A 57 ? O ARG A 57 N VAL A 77 ? N VAL A 77 C 1 2 O ILE A 62 ? O ILE A 62 N GLY A 73 ? N GLY A 73 D 1 2 O GLN B 18 ? O GLN B 18 N ILE B 15 ? N ILE B 15 D 2 3 O LYS B 14 ? O LYS B 14 N GLU B 65 ? N GLU B 65 D 3 4 O ILE B 62 ? O ILE B 62 N GLY B 73 ? N GLY B 73 E 1 2 O LYS B 43 ? O LYS B 43 N GLN B 58 ? N GLN B 58 E 2 3 O ARG B 57 ? O ARG B 57 N VAL B 77 ? N VAL B 77 # _struct_site.id AC1 _struct_site.pdbx_evidence_code Software _struct_site.pdbx_auth_asym_id ? _struct_site.pdbx_auth_comp_id ? _struct_site.pdbx_auth_seq_id ? _struct_site.pdbx_auth_ins_code ? _struct_site.pdbx_num_residues 17 _struct_site.details 'BINDING SITE FOR RESIDUE AH1 A 500' # loop_ _struct_site_gen.id _struct_site_gen.site_id _struct_site_gen.pdbx_num_res _struct_site_gen.label_comp_id _struct_site_gen.label_asym_id _struct_site_gen.label_seq_id _struct_site_gen.pdbx_auth_ins_code _struct_site_gen.auth_comp_id _struct_site_gen.auth_asym_id _struct_site_gen.auth_seq_id _struct_site_gen.label_atom_id _struct_site_gen.label_alt_id _struct_site_gen.symmetry _struct_site_gen.details 1 AC1 17 ASP A 25 ? ASP A 25 . ? 1_555 ? 2 AC1 17 GLY A 27 ? GLY A 27 . ? 1_555 ? 3 AC1 17 ALA A 28 ? ALA A 28 . ? 1_555 ? 4 AC1 17 VAL A 32 ? VAL A 32 . ? 1_555 ? 5 AC1 17 ILE A 50 ? ILE A 50 . ? 1_555 ? 6 AC1 17 PRO A 81 ? PRO A 81 . ? 1_555 ? 7 AC1 17 VAL A 82 ? VAL A 82 . ? 1_555 ? 8 AC1 17 ILE A 84 ? ILE A 84 . ? 1_555 ? 9 AC1 17 HOH D . ? HOH A 386 . ? 1_555 ? 10 AC1 17 ARG B 8 ? ARG B 8 . ? 1_555 ? 11 AC1 17 ASP B 25 ? ASP B 25 . ? 1_555 ? 12 AC1 17 GLY B 27 ? GLY B 27 . ? 1_555 ? 13 AC1 17 ALA B 28 ? ALA B 28 . ? 1_555 ? 14 AC1 17 ASP B 30 ? ASP B 30 . ? 1_555 ? 15 AC1 17 GLY B 48 ? GLY B 48 . ? 1_555 ? 16 AC1 17 GLY B 49 ? GLY B 49 . ? 1_555 ? 17 AC1 17 ILE B 50 ? ILE B 50 . ? 1_555 ? # _database_PDB_matrix.entry_id 1AJX _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 1AJX _atom_sites.fract_transf_matrix[1][1] 0.016949 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.000000 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.011521 _atom_sites.fract_transf_matrix[2][3] 0.000000 _atom_sites.fract_transf_matrix[3][1] 0.000000 _atom_sites.fract_transf_matrix[3][2] 0.000000 _atom_sites.fract_transf_matrix[3][3] 0.021368 _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 . PRO A 1 1 ? 29.188 40.272 5.386 1.00 30.87 ? 1 PRO A N 1 ATOM 2 C CA . PRO A 1 1 ? 29.924 39.009 5.093 1.00 31.10 ? 1 PRO A CA 1 ATOM 3 C C . PRO A 1 1 ? 29.380 38.360 3.820 1.00 29.14 ? 1 PRO A C 1 ATOM 4 O O . PRO A 1 1 ? 28.303 38.745 3.347 1.00 28.45 ? 1 PRO A O 1 ATOM 5 C CB . PRO A 1 1 ? 29.780 38.088 6.336 1.00 30.96 ? 1 PRO A CB 1 ATOM 6 C CG . PRO A 1 1 ? 28.475 38.662 7.015 1.00 32.10 ? 1 PRO A CG 1 ATOM 7 C CD . PRO A 1 1 ? 28.565 40.184 6.726 1.00 32.08 ? 1 PRO A CD 1 ATOM 8 N N . GLN A 1 2 ? 30.245 37.599 3.155 1.00 28.28 ? 2 GLN A N 1 ATOM 9 C CA . GLN A 1 2 ? 29.862 36.882 1.967 1.00 27.74 ? 2 GLN A CA 1 ATOM 10 C C . GLN A 1 2 ? 30.005 35.444 2.365 1.00 27.66 ? 2 GLN A C 1 ATOM 11 O O . GLN A 1 2 ? 31.123 34.949 2.451 1.00 28.91 ? 2 GLN A O 1 ATOM 12 C CB . GLN A 1 2 ? 30.802 37.118 0.851 1.00 28.67 ? 2 GLN A CB 1 ATOM 13 C CG . GLN A 1 2 ? 30.471 36.101 -0.209 1.00 33.95 ? 2 GLN A CG 1 ATOM 14 C CD . GLN A 1 2 ? 31.026 36.399 -1.585 1.00 37.25 ? 2 GLN A CD 1 ATOM 15 O OE1 . GLN A 1 2 ? 32.031 35.794 -1.982 1.00 39.86 ? 2 GLN A OE1 1 ATOM 16 N NE2 . GLN A 1 2 ? 30.323 37.256 -2.368 1.00 37.64 ? 2 GLN A NE2 1 ATOM 17 N N . ILE A 1 3 ? 28.887 34.749 2.476 1.00 25.09 ? 3 ILE A N 1 ATOM 18 C CA . ILE A 1 3 ? 28.873 33.386 2.940 1.00 22.14 ? 3 ILE A CA 1 ATOM 19 C C . ILE A 1 3 ? 28.710 32.352 1.830 1.00 22.26 ? 3 ILE A C 1 ATOM 20 O O . ILE A 1 3 ? 27.796 32.465 0.971 1.00 21.23 ? 3 ILE A O 1 ATOM 21 C CB . ILE A 1 3 ? 27.762 33.267 4.024 1.00 22.87 ? 3 ILE A CB 1 ATOM 22 C CG1 . ILE A 1 3 ? 28.084 34.196 5.211 1.00 24.48 ? 3 ILE A CG1 1 ATOM 23 C CG2 . ILE A 1 3 ? 27.484 31.854 4.492 1.00 21.21 ? 3 ILE A CG2 1 ATOM 24 C CD1 . ILE A 1 3 ? 26.906 34.318 6.294 1.00 22.67 ? 3 ILE A CD1 1 ATOM 25 N N . THR A 1 4 ? 29.759 31.502 1.716 1.00 22.09 ? 4 THR A N 1 ATOM 26 C CA . THR A 1 4 ? 29.764 30.315 0.815 1.00 20.83 ? 4 THR A CA 1 ATOM 27 C C . THR A 1 4 ? 28.858 29.153 1.400 1.00 18.52 ? 4 THR A C 1 ATOM 28 O O . THR A 1 4 ? 28.491 29.102 2.593 1.00 18.23 ? 4 THR A O 1 ATOM 29 C CB . THR A 1 4 ? 31.199 29.755 0.479 1.00 21.68 ? 4 THR A CB 1 ATOM 30 O OG1 . THR A 1 4 ? 31.838 29.199 1.664 1.00 20.48 ? 4 THR A OG1 1 ATOM 31 C CG2 . THR A 1 4 ? 32.000 30.865 -0.196 1.00 21.83 ? 4 THR A CG2 1 ATOM 32 N N . LEU A 1 5 ? 28.442 28.258 0.531 1.00 17.22 ? 5 LEU A N 1 ATOM 33 C CA . LEU A 1 5 ? 27.505 27.241 0.960 1.00 16.47 ? 5 LEU A CA 1 ATOM 34 C C . LEU A 1 5 ? 28.132 25.867 0.849 1.00 16.33 ? 5 LEU A C 1 ATOM 35 O O . LEU A 1 5 ? 27.440 24.904 0.561 1.00 16.81 ? 5 LEU A O 1 ATOM 36 C CB . LEU A 1 5 ? 26.216 27.345 0.126 1.00 14.15 ? 5 LEU A CB 1 ATOM 37 C CG . LEU A 1 5 ? 25.596 28.754 0.142 1.00 16.16 ? 5 LEU A CG 1 ATOM 38 C CD1 . LEU A 1 5 ? 24.501 28.959 -0.903 1.00 10.07 ? 5 LEU A CD1 1 ATOM 39 C CD2 . LEU A 1 5 ? 25.095 28.997 1.535 1.00 17.35 ? 5 LEU A CD2 1 ATOM 40 N N . TRP A 1 6 ? 29.458 25.821 0.972 1.00 15.69 ? 6 TRP A N 1 ATOM 41 C CA . TRP A 1 6 ? 30.150 24.548 0.987 1.00 17.03 ? 6 TRP A CA 1 ATOM 42 C C . TRP A 1 6 ? 29.734 23.893 2.259 1.00 16.35 ? 6 TRP A C 1 ATOM 43 O O . TRP A 1 6 ? 29.675 22.705 2.322 1.00 17.61 ? 6 TRP A O 1 ATOM 44 C CB . TRP A 1 6 ? 31.672 24.686 1.001 1.00 14.15 ? 6 TRP A CB 1 ATOM 45 C CG . TRP A 1 6 ? 32.182 25.250 -0.281 1.00 16.75 ? 6 TRP A CG 1 ATOM 46 C CD1 . TRP A 1 6 ? 32.790 26.462 -0.455 1.00 18.99 ? 6 TRP A CD1 1 ATOM 47 C CD2 . TRP A 1 6 ? 32.170 24.625 -1.569 1.00 18.74 ? 6 TRP A CD2 1 ATOM 48 N NE1 . TRP A 1 6 ? 33.175 26.630 -1.761 1.00 19.93 ? 6 TRP A NE1 1 ATOM 49 C CE2 . TRP A 1 6 ? 32.809 25.518 -2.474 1.00 20.61 ? 6 TRP A CE2 1 ATOM 50 C CE3 . TRP A 1 6 ? 31.677 23.405 -2.060 1.00 20.24 ? 6 TRP A CE3 1 ATOM 51 C CZ2 . TRP A 1 6 ? 32.975 25.222 -3.862 1.00 22.15 ? 6 TRP A CZ2 1 ATOM 52 C CZ3 . TRP A 1 6 ? 31.848 23.121 -3.455 1.00 23.18 ? 6 TRP A CZ3 1 ATOM 53 C CH2 . TRP A 1 6 ? 32.491 24.025 -4.323 1.00 19.17 ? 6 TRP A CH2 1 ATOM 54 N N . GLN A 1 7 ? 29.461 24.659 3.302 1.00 15.20 ? 7 GLN A N 1 ATOM 55 C CA . GLN A 1 7 ? 29.015 24.083 4.566 1.00 13.81 ? 7 GLN A CA 1 ATOM 56 C C . GLN A 1 7 ? 27.693 24.759 4.912 1.00 13.03 ? 7 GLN A C 1 ATOM 57 O O . GLN A 1 7 ? 27.310 25.714 4.289 1.00 11.13 ? 7 GLN A O 1 ATOM 58 C CB . GLN A 1 7 ? 30.059 24.405 5.644 1.00 16.84 ? 7 GLN A CB 1 ATOM 59 C CG . GLN A 1 7 ? 31.449 23.688 5.349 1.00 25.16 ? 7 GLN A CG 1 ATOM 60 C CD . GLN A 1 7 ? 32.562 24.512 4.488 1.00 30.15 ? 7 GLN A CD 1 ATOM 61 O OE1 . GLN A 1 7 ? 32.673 25.759 4.521 1.00 32.22 ? 7 GLN A OE1 1 ATOM 62 N NE2 . GLN A 1 7 ? 33.421 23.757 3.780 1.00 33.85 ? 7 GLN A NE2 1 ATOM 63 N N . ARG A 1 8 ? 26.988 24.272 5.921 1.00 14.46 ? 8 ARG A N 1 ATOM 64 C CA . ARG A 1 8 ? 25.739 24.885 6.377 1.00 14.40 ? 8 ARG A CA 1 ATOM 65 C C . ARG A 1 8 ? 26.054 26.269 6.884 1.00 13.29 ? 8 ARG A C 1 ATOM 66 O O . ARG A 1 8 ? 27.030 26.429 7.617 1.00 12.98 ? 8 ARG A O 1 ATOM 67 C CB . ARG A 1 8 ? 25.141 24.089 7.509 1.00 15.96 ? 8 ARG A CB 1 ATOM 68 C CG . ARG A 1 8 ? 24.503 22.811 7.067 1.00 17.74 ? 8 ARG A CG 1 ATOM 69 C CD . ARG A 1 8 ? 24.018 22.125 8.237 1.00 18.58 ? 8 ARG A CD 1 ATOM 70 N NE . ARG A 1 8 ? 23.187 21.003 7.822 1.00 25.78 ? 8 ARG A NE 1 ATOM 71 C CZ . ARG A 1 8 ? 22.171 20.520 8.558 1.00 32.24 ? 8 ARG A CZ 1 ATOM 72 N NH1 . ARG A 1 8 ? 21.833 21.054 9.738 1.00 35.06 ? 8 ARG A NH1 1 ATOM 73 N NH2 . ARG A 1 8 ? 21.500 19.441 8.178 1.00 35.60 ? 8 ARG A NH2 1 ATOM 74 N N . PRO A 1 9 ? 25.262 27.290 6.471 1.00 12.53 ? 9 PRO A N 1 ATOM 75 C CA . PRO A 1 9 ? 25.527 28.655 6.918 1.00 13.64 ? 9 PRO A CA 1 ATOM 76 C C . PRO A 1 9 ? 25.001 28.909 8.340 1.00 15.02 ? 9 PRO A C 1 ATOM 77 O O . PRO A 1 9 ? 23.886 29.428 8.572 1.00 15.07 ? 9 PRO A O 1 ATOM 78 C CB . PRO A 1 9 ? 24.871 29.503 5.797 1.00 10.44 ? 9 PRO A CB 1 ATOM 79 C CG . PRO A 1 9 ? 23.588 28.674 5.465 1.00 11.91 ? 9 PRO A CG 1 ATOM 80 C CD . PRO A 1 9 ? 24.135 27.256 5.485 1.00 13.39 ? 9 PRO A CD 1 ATOM 81 N N . LEU A 1 10 ? 25.796 28.475 9.309 1.00 16.37 ? 10 LEU A N 1 ATOM 82 C CA . LEU A 1 10 ? 25.483 28.664 10.729 1.00 18.78 ? 10 LEU A CA 1 ATOM 83 C C . LEU A 1 10 ? 26.134 29.959 11.189 1.00 18.89 ? 10 LEU A C 1 ATOM 84 O O . LEU A 1 10 ? 27.253 30.288 10.759 1.00 21.04 ? 10 LEU A O 1 ATOM 85 C CB . LEU A 1 10 ? 26.089 27.576 11.581 1.00 20.02 ? 10 LEU A CB 1 ATOM 86 C CG . LEU A 1 10 ? 25.453 26.255 11.238 1.00 21.47 ? 10 LEU A CG 1 ATOM 87 C CD1 . LEU A 1 10 ? 26.270 25.126 11.827 1.00 21.80 ? 10 LEU A CD1 1 ATOM 88 C CD2 . LEU A 1 10 ? 24.045 26.298 11.837 1.00 20.10 ? 10 LEU A CD2 1 ATOM 89 N N . VAL A 1 11 ? 25.394 30.690 12.018 1.00 18.41 ? 11 VAL A N 1 ATOM 90 C CA . VAL A 1 11 ? 25.848 31.961 12.559 1.00 21.04 ? 11 VAL A CA 1 ATOM 91 C C . VAL A 1 11 ? 25.376 31.991 14.027 1.00 22.44 ? 11 VAL A C 1 ATOM 92 O O . VAL A 1 11 ? 24.498 31.192 14.421 1.00 21.15 ? 11 VAL A O 1 ATOM 93 C CB . VAL A 1 11 ? 25.237 33.222 11.814 1.00 19.40 ? 11 VAL A CB 1 ATOM 94 C CG1 . VAL A 1 11 ? 25.789 33.370 10.401 1.00 19.33 ? 11 VAL A CG1 1 ATOM 95 C CG2 . VAL A 1 11 ? 23.726 33.151 11.869 1.00 19.23 ? 11 VAL A CG2 1 ATOM 96 N N . THR A 1 12 ? 25.946 32.921 14.821 1.00 23.69 ? 12 THR A N 1 ATOM 97 C CA . THR A 1 12 ? 25.581 33.072 16.239 1.00 23.55 ? 12 THR A CA 1 ATOM 98 C C . THR A 1 12 ? 24.531 34.117 16.343 1.00 21.33 ? 12 THR A C 1 ATOM 99 O O . THR A 1 12 ? 24.591 35.125 15.685 1.00 22.34 ? 12 THR A O 1 ATOM 100 C CB . THR A 1 12 ? 26.782 33.525 17.104 1.00 28.98 ? 12 THR A CB 1 ATOM 101 O OG1 . THR A 1 12 ? 27.823 32.522 17.051 1.00 36.13 ? 12 THR A OG1 1 ATOM 102 C CG2 . THR A 1 12 ? 26.338 33.715 18.570 1.00 31.91 ? 12 THR A CG2 1 ATOM 103 N N . ILE A 1 13 ? 23.548 33.885 17.170 1.00 19.07 ? 13 ILE A N 1 ATOM 104 C CA . ILE A 1 13 ? 22.524 34.883 17.304 1.00 19.80 ? 13 ILE A CA 1 ATOM 105 C C . ILE A 1 13 ? 22.462 35.118 18.807 1.00 21.04 ? 13 ILE A C 1 ATOM 106 O O . ILE A 1 13 ? 22.958 34.293 19.571 1.00 21.63 ? 13 ILE A O 1 ATOM 107 C CB . ILE A 1 13 ? 21.124 34.397 16.723 1.00 18.63 ? 13 ILE A CB 1 ATOM 108 C CG1 . ILE A 1 13 ? 20.603 33.185 17.493 1.00 18.06 ? 13 ILE A CG1 1 ATOM 109 C CG2 . ILE A 1 13 ? 21.261 34.071 15.205 1.00 17.98 ? 13 ILE A CG2 1 ATOM 110 C CD1 . ILE A 1 13 ? 19.174 32.983 17.348 1.00 17.46 ? 13 ILE A CD1 1 ATOM 111 N N . LYS A 1 14 ? 21.995 36.303 19.213 1.00 23.08 ? 14 LYS A N 1 ATOM 112 C CA . LYS A 1 14 ? 21.804 36.687 20.619 1.00 23.86 ? 14 LYS A CA 1 ATOM 113 C C . LYS A 1 14 ? 20.278 36.935 20.756 1.00 23.44 ? 14 LYS A C 1 ATOM 114 O O . LYS A 1 14 ? 19.656 37.708 19.986 1.00 21.94 ? 14 LYS A O 1 ATOM 115 C CB . LYS A 1 14 ? 22.608 37.948 20.932 1.00 27.78 ? 14 LYS A CB 1 ATOM 116 C CG . LYS A 1 14 ? 22.979 38.059 22.421 1.00 35.92 ? 14 LYS A CG 1 ATOM 117 C CD . LYS A 1 14 ? 22.068 39.008 23.126 1.00 43.03 ? 14 LYS A CD 1 ATOM 118 C CE . LYS A 1 14 ? 20.630 38.418 23.275 1.00 47.48 ? 14 LYS A CE 1 ATOM 119 N NZ . LYS A 1 14 ? 19.498 39.341 23.811 1.00 45.93 ? 14 LYS A NZ 1 ATOM 120 N N . ILE A 1 15 ? 19.637 36.219 21.649 1.00 22.03 ? 15 ILE A N 1 ATOM 121 C CA . ILE A 1 15 ? 18.231 36.419 21.764 1.00 26.62 ? 15 ILE A CA 1 ATOM 122 C C . ILE A 1 15 ? 17.956 36.134 23.201 1.00 30.43 ? 15 ILE A C 1 ATOM 123 O O . ILE A 1 15 ? 18.600 35.266 23.772 1.00 32.61 ? 15 ILE A O 1 ATOM 124 C CB . ILE A 1 15 ? 17.432 35.443 20.858 1.00 24.65 ? 15 ILE A CB 1 ATOM 125 C CG1 . ILE A 1 15 ? 15.917 35.582 21.170 1.00 23.23 ? 15 ILE A CG1 1 ATOM 126 C CG2 . ILE A 1 15 ? 17.938 33.938 21.109 1.00 25.33 ? 15 ILE A CG2 1 ATOM 127 C CD1 . ILE A 1 15 ? 14.986 35.148 20.060 1.00 20.05 ? 15 ILE A CD1 1 ATOM 128 N N . GLY A 1 16 ? 17.099 36.928 23.835 1.00 34.87 ? 16 GLY A N 1 ATOM 129 C CA . GLY A 1 16 ? 16.762 36.716 25.261 1.00 36.09 ? 16 GLY A CA 1 ATOM 130 C C . GLY A 1 16 ? 17.985 36.785 26.158 1.00 36.84 ? 16 GLY A C 1 ATOM 131 O O . GLY A 1 16 ? 18.053 36.217 27.255 1.00 36.12 ? 16 GLY A O 1 ATOM 132 N N . GLY A 1 17 ? 18.979 37.482 25.634 1.00 36.73 ? 17 GLY A N 1 ATOM 133 C CA . GLY A 1 17 ? 20.223 37.616 26.334 1.00 38.57 ? 17 GLY A CA 1 ATOM 134 C C . GLY A 1 17 ? 21.035 36.348 26.179 1.00 40.42 ? 17 GLY A C 1 ATOM 135 O O . GLY A 1 17 ? 22.116 36.251 26.735 1.00 42.35 ? 17 GLY A O 1 ATOM 136 N N . GLN A 1 18 ? 20.507 35.359 25.466 1.00 38.28 ? 18 GLN A N 1 ATOM 137 C CA . GLN A 1 18 ? 21.216 34.119 25.244 1.00 35.97 ? 18 GLN A CA 1 ATOM 138 C C . GLN A 1 18 ? 21.892 34.042 23.876 1.00 33.02 ? 18 GLN A C 1 ATOM 139 O O . GLN A 1 18 ? 21.427 34.617 22.917 1.00 31.09 ? 18 GLN A O 1 ATOM 140 C CB . GLN A 1 18 ? 20.238 32.981 25.353 1.00 40.14 ? 18 GLN A CB 1 ATOM 141 C CG . GLN A 1 18 ? 19.611 32.738 26.732 1.00 46.22 ? 18 GLN A CG 1 ATOM 142 C CD . GLN A 1 18 ? 18.263 31.965 26.629 1.00 49.56 ? 18 GLN A CD 1 ATOM 143 O OE1 . GLN A 1 18 ? 18.212 30.715 26.387 1.00 49.76 ? 18 GLN A OE1 1 ATOM 144 N NE2 . GLN A 1 18 ? 17.157 32.717 26.800 1.00 51.98 ? 18 GLN A NE2 1 ATOM 145 N N . LEU A 1 19 ? 23.051 33.407 23.829 1.00 32.42 ? 19 LEU A N 1 ATOM 146 C CA . LEU A 1 19 ? 23.768 33.175 22.575 1.00 32.56 ? 19 LEU A CA 1 ATOM 147 C C . LEU A 1 19 ? 23.385 31.799 22.039 1.00 30.72 ? 19 LEU A C 1 ATOM 148 O O . LEU A 1 19 ? 23.307 30.826 22.803 1.00 31.79 ? 19 LEU A O 1 ATOM 149 C CB . LEU A 1 19 ? 25.263 33.241 22.753 1.00 34.60 ? 19 LEU A CB 1 ATOM 150 C CG . LEU A 1 19 ? 25.942 34.593 22.980 1.00 36.52 ? 19 LEU A CG 1 ATOM 151 C CD1 . LEU A 1 19 ? 27.409 34.435 22.498 1.00 37.92 ? 19 LEU A CD1 1 ATOM 152 C CD2 . LEU A 1 19 ? 25.330 35.638 22.184 1.00 36.31 ? 19 LEU A CD2 1 ATOM 153 N N . LYS A 1 20 ? 23.116 31.709 20.744 1.00 28.28 ? 20 LYS A N 1 ATOM 154 C CA . LYS A 1 20 ? 22.694 30.432 20.153 1.00 26.87 ? 20 LYS A CA 1 ATOM 155 C C . LYS A 1 20 ? 23.235 30.331 18.769 1.00 25.29 ? 20 LYS A C 1 ATOM 156 O O . LYS A 1 20 ? 23.592 31.340 18.193 1.00 26.64 ? 20 LYS A O 1 ATOM 157 C CB . LYS A 1 20 ? 21.172 30.375 20.036 1.00 27.48 ? 20 LYS A CB 1 ATOM 158 C CG . LYS A 1 20 ? 20.437 30.249 21.361 1.00 31.85 ? 20 LYS A CG 1 ATOM 159 C CD . LYS A 1 20 ? 18.939 30.057 21.217 1.00 35.56 ? 20 LYS A CD 1 ATOM 160 C CE . LYS A 1 20 ? 18.259 29.721 22.596 1.00 38.50 ? 20 LYS A CE 1 ATOM 161 N NZ . LYS A 1 20 ? 18.194 28.224 22.909 1.00 42.00 ? 20 LYS A NZ 1 ATOM 162 N N . GLU A 1 21 ? 23.287 29.116 18.234 1.00 23.68 ? 21 GLU A N 1 ATOM 163 C CA . GLU A 1 21 ? 23.737 28.864 16.844 1.00 23.95 ? 21 GLU A CA 1 ATOM 164 C C . GLU A 1 21 ? 22.498 28.655 15.945 1.00 18.50 ? 21 GLU A C 1 ATOM 165 O O . GLU A 1 21 ? 21.543 27.989 16.348 1.00 18.36 ? 21 GLU A O 1 ATOM 166 C CB . GLU A 1 21 ? 24.619 27.632 16.781 1.00 28.52 ? 21 GLU A CB 1 ATOM 167 C CG . GLU A 1 21 ? 25.933 27.857 16.055 1.00 35.76 ? 21 GLU A CG 1 ATOM 168 C CD . GLU A 1 21 ? 26.536 26.506 15.477 1.00 42.48 ? 21 GLU A CD 1 ATOM 169 O OE1 . GLU A 1 21 ? 26.049 25.323 15.813 1.00 39.99 ? 21 GLU A OE1 1 ATOM 170 O OE2 . GLU A 1 21 ? 27.500 26.681 14.636 1.00 46.61 ? 21 GLU A OE2 1 ATOM 171 N N . ALA A 1 22 ? 22.467 29.310 14.788 1.00 15.94 ? 22 ALA A N 1 ATOM 172 C CA . ALA A 1 22 ? 21.310 29.194 13.904 1.00 13.92 ? 22 ALA A CA 1 ATOM 173 C C . ALA A 1 22 ? 21.734 29.136 12.504 1.00 15.12 ? 22 ALA A C 1 ATOM 174 O O . ALA A 1 22 ? 22.830 29.622 12.154 1.00 18.01 ? 22 ALA A O 1 ATOM 175 C CB . ALA A 1 22 ? 20.399 30.323 14.061 1.00 13.59 ? 22 ALA A CB 1 ATOM 176 N N . LEU A 1 23 ? 20.847 28.554 11.700 1.00 12.94 ? 23 LEU A N 1 ATOM 177 C CA . LEU A 1 23 ? 21.053 28.407 10.284 1.00 13.69 ? 23 LEU A CA 1 ATOM 178 C C . LEU A 1 23 ? 20.347 29.552 9.497 1.00 11.81 ? 23 LEU A C 1 ATOM 179 O O . LEU A 1 23 ? 19.170 29.765 9.724 1.00 12.36 ? 23 LEU A O 1 ATOM 180 C CB . LEU A 1 23 ? 20.414 27.077 9.913 1.00 14.04 ? 23 LEU A CB 1 ATOM 181 C CG . LEU A 1 23 ? 20.501 26.495 8.519 1.00 14.25 ? 23 LEU A CG 1 ATOM 182 C CD1 . LEU A 1 23 ? 21.931 26.229 8.234 1.00 12.55 ? 23 LEU A CD1 1 ATOM 183 C CD2 . LEU A 1 23 ? 19.604 25.150 8.450 1.00 12.63 ? 23 LEU A CD2 1 ATOM 184 N N . LEU A 1 24 ? 21.037 30.222 8.562 1.00 11.01 ? 24 LEU A N 1 ATOM 185 C CA . LEU A 1 24 ? 20.452 31.263 7.649 1.00 12.55 ? 24 LEU A CA 1 ATOM 186 C C . LEU A 1 24 ? 19.713 30.443 6.585 1.00 13.37 ? 24 LEU A C 1 ATOM 187 O O . LEU A 1 24 ? 20.327 29.748 5.795 1.00 14.69 ? 24 LEU A O 1 ATOM 188 C CB . LEU A 1 24 ? 21.538 32.100 6.933 1.00 10.82 ? 24 LEU A CB 1 ATOM 189 C CG . LEU A 1 24 ? 22.439 32.708 8.008 1.00 13.95 ? 24 LEU A CG 1 ATOM 190 C CD1 . LEU A 1 24 ? 23.463 33.593 7.339 1.00 13.58 ? 24 LEU A CD1 1 ATOM 191 C CD2 . LEU A 1 24 ? 21.607 33.404 9.088 1.00 10.26 ? 24 LEU A CD2 1 ATOM 192 N N . ASP A 1 25 ? 18.405 30.540 6.574 1.00 11.98 ? 25 ASP A N 1 ATOM 193 C CA . ASP A 1 25 ? 17.571 29.703 5.727 1.00 12.57 ? 25 ASP A CA 1 ATOM 194 C C . ASP A 1 25 ? 16.652 30.484 4.781 1.00 9.18 ? 25 ASP A C 1 ATOM 195 O O . ASP A 1 25 ? 15.559 30.845 5.163 1.00 11.57 ? 25 ASP A O 1 ATOM 196 C CB . ASP A 1 25 ? 16.747 28.788 6.662 1.00 11.18 ? 25 ASP A CB 1 ATOM 197 C CG . ASP A 1 25 ? 16.067 27.628 5.931 1.00 15.88 ? 25 ASP A CG 1 ATOM 198 O OD1 . ASP A 1 25 ? 15.857 27.688 4.691 1.00 13.54 ? 25 ASP A OD1 1 ATOM 199 O OD2 . ASP A 1 25 ? 15.737 26.646 6.630 1.00 15.45 ? 25 ASP A OD2 1 ATOM 200 N N . THR A 1 26 ? 17.041 30.599 3.527 1.00 8.43 ? 26 THR A N 1 ATOM 201 C CA . THR A 1 26 ? 16.267 31.322 2.551 1.00 8.74 ? 26 THR A CA 1 ATOM 202 C C . THR A 1 26 ? 14.992 30.572 2.113 1.00 10.36 ? 26 THR A C 1 ATOM 203 O O . THR A 1 26 ? 14.055 31.176 1.562 1.00 11.97 ? 26 THR A O 1 ATOM 204 C CB . THR A 1 26 ? 17.106 31.635 1.293 1.00 7.85 ? 26 THR A CB 1 ATOM 205 O OG1 . THR A 1 26 ? 17.523 30.420 0.662 1.00 5.31 ? 26 THR A OG1 1 ATOM 206 C CG2 . THR A 1 26 ? 18.346 32.448 1.624 1.00 7.50 ? 26 THR A CG2 1 ATOM 207 N N . GLY A 1 27 ? 14.910 29.278 2.376 1.00 8.94 ? 27 GLY A N 1 ATOM 208 C CA . GLY A 1 27 ? 13.723 28.569 2.011 1.00 9.80 ? 27 GLY A CA 1 ATOM 209 C C . GLY A 1 27 ? 12.633 28.710 3.077 1.00 10.45 ? 27 GLY A C 1 ATOM 210 O O . GLY A 1 27 ? 11.465 28.371 2.850 1.00 12.31 ? 27 GLY A O 1 ATOM 211 N N . ALA A 1 28 ? 13.003 29.169 4.271 1.00 11.06 ? 28 ALA A N 1 ATOM 212 C CA . ALA A 1 28 ? 12.025 29.300 5.374 1.00 12.30 ? 28 ALA A CA 1 ATOM 213 C C . ALA A 1 28 ? 11.259 30.653 5.403 1.00 13.74 ? 28 ALA A C 1 ATOM 214 O O . ALA A 1 28 ? 11.907 31.678 5.511 1.00 14.47 ? 28 ALA A O 1 ATOM 215 C CB . ALA A 1 28 ? 12.750 29.131 6.700 1.00 9.29 ? 28 ALA A CB 1 ATOM 216 N N . ASP A 1 29 ? 9.922 30.679 5.365 1.00 13.83 ? 29 ASP A N 1 ATOM 217 C CA . ASP A 1 29 ? 9.299 31.976 5.484 1.00 16.13 ? 29 ASP A CA 1 ATOM 218 C C . ASP A 1 29 ? 9.510 32.606 6.885 1.00 15.58 ? 29 ASP A C 1 ATOM 219 O O . ASP A 1 29 ? 9.701 33.804 6.976 1.00 15.35 ? 29 ASP A O 1 ATOM 220 C CB . ASP A 1 29 ? 7.828 31.892 5.278 1.00 15.24 ? 29 ASP A CB 1 ATOM 221 C CG . ASP A 1 29 ? 7.460 31.423 3.906 1.00 18.97 ? 29 ASP A CG 1 ATOM 222 O OD1 . ASP A 1 29 ? 8.217 31.538 2.927 1.00 16.66 ? 29 ASP A OD1 1 ATOM 223 O OD2 . ASP A 1 29 ? 6.279 31.048 3.793 1.00 23.68 ? 29 ASP A OD2 1 ATOM 224 N N . ASP A 1 30 ? 9.475 31.788 7.947 1.00 15.58 ? 30 ASP A N 1 ATOM 225 C CA . ASP A 1 30 ? 9.570 32.242 9.360 1.00 15.40 ? 30 ASP A CA 1 ATOM 226 C C . ASP A 1 30 ? 10.771 31.774 10.105 1.00 12.99 ? 30 ASP A C 1 ATOM 227 O O . ASP A 1 30 ? 11.536 30.969 9.613 1.00 14.34 ? 30 ASP A O 1 ATOM 228 C CB . ASP A 1 30 ? 8.422 31.721 10.134 1.00 17.82 ? 30 ASP A CB 1 ATOM 229 C CG . ASP A 1 30 ? 7.113 31.914 9.407 1.00 26.20 ? 30 ASP A CG 1 ATOM 230 O OD1 . ASP A 1 30 ? 6.605 33.064 9.307 1.00 28.81 ? 30 ASP A OD1 1 ATOM 231 O OD2 . ASP A 1 30 ? 6.581 30.886 8.918 1.00 28.33 ? 30 ASP A OD2 1 ATOM 232 N N . THR A 1 31 ? 11.042 32.410 11.217 1.00 10.44 ? 31 THR A N 1 ATOM 233 C CA . THR A 1 31 ? 12.156 32.046 12.048 1.00 10.39 ? 31 THR A CA 1 ATOM 234 C C . THR A 1 31 ? 11.596 31.104 13.114 1.00 12.07 ? 31 THR A C 1 ATOM 235 O O . THR A 1 31 ? 10.554 31.386 13.741 1.00 10.57 ? 31 THR A O 1 ATOM 236 C CB . THR A 1 31 ? 12.637 33.292 12.687 1.00 10.84 ? 31 THR A CB 1 ATOM 237 O OG1 . THR A 1 31 ? 13.228 34.060 11.624 1.00 11.32 ? 31 THR A OG1 1 ATOM 238 C CG2 . THR A 1 31 ? 13.630 33.019 13.876 1.00 7.41 ? 31 THR A CG2 1 ATOM 239 N N . VAL A 1 32 ? 12.298 30.004 13.315 1.00 13.62 ? 32 VAL A N 1 ATOM 240 C CA . VAL A 1 32 ? 11.795 29.021 14.293 1.00 16.49 ? 32 VAL A CA 1 ATOM 241 C C . VAL A 1 32 ? 12.940 28.536 15.158 1.00 14.30 ? 32 VAL A C 1 ATOM 242 O O . VAL A 1 32 ? 13.967 28.144 14.635 1.00 12.77 ? 32 VAL A O 1 ATOM 243 C CB . VAL A 1 32 ? 10.910 27.863 13.607 1.00 17.67 ? 32 VAL A CB 1 ATOM 244 C CG1 . VAL A 1 32 ? 11.455 27.418 12.302 1.00 21.48 ? 32 VAL A CG1 1 ATOM 245 C CG2 . VAL A 1 32 ? 10.591 26.714 14.559 1.00 16.05 ? 32 VAL A CG2 1 ATOM 246 N N . LEU A 1 33 ? 12.797 28.703 16.466 1.00 11.40 ? 33 LEU A N 1 ATOM 247 C CA . LEU A 1 33 ? 13.866 28.307 17.370 1.00 14.42 ? 33 LEU A CA 1 ATOM 248 C C . LEU A 1 33 ? 13.383 27.178 18.265 1.00 15.43 ? 33 LEU A C 1 ATOM 249 O O . LEU A 1 33 ? 12.182 27.023 18.518 1.00 13.70 ? 33 LEU A O 1 ATOM 250 C CB . LEU A 1 33 ? 14.336 29.484 18.277 1.00 14.68 ? 33 LEU A CB 1 ATOM 251 C CG . LEU A 1 33 ? 14.886 30.795 17.596 1.00 18.43 ? 33 LEU A CG 1 ATOM 252 C CD1 . LEU A 1 33 ? 15.326 31.808 18.699 1.00 19.93 ? 33 LEU A CD1 1 ATOM 253 C CD2 . LEU A 1 33 ? 16.077 30.494 16.562 1.00 17.66 ? 33 LEU A CD2 1 ATOM 254 N N . GLU A 1 34 ? 14.333 26.451 18.828 1.00 16.87 ? 34 GLU A N 1 ATOM 255 C CA . GLU A 1 34 ? 14.005 25.325 19.698 1.00 19.00 ? 34 GLU A CA 1 ATOM 256 C C . GLU A 1 34 ? 13.408 25.884 21.017 1.00 19.13 ? 34 GLU A C 1 ATOM 257 O O . GLU A 1 34 ? 13.509 27.116 21.332 1.00 15.07 ? 34 GLU A O 1 ATOM 258 C CB . GLU A 1 34 ? 15.300 24.532 19.906 1.00 22.94 ? 34 GLU A CB 1 ATOM 259 C CG . GLU A 1 34 ? 16.237 25.249 20.830 1.00 29.36 ? 34 GLU A CG 1 ATOM 260 C CD . GLU A 1 34 ? 17.727 25.035 20.577 1.00 32.84 ? 34 GLU A CD 1 ATOM 261 O OE1 . GLU A 1 34 ? 18.129 23.960 19.992 1.00 30.41 ? 34 GLU A OE1 1 ATOM 262 O OE2 . GLU A 1 34 ? 18.456 26.009 21.016 1.00 34.39 ? 34 GLU A OE2 1 ATOM 263 N N . GLU A 1 35 ? 12.738 25.019 21.759 1.00 17.72 ? 35 GLU A N 1 ATOM 264 C CA . GLU A 1 35 ? 12.073 25.411 22.988 1.00 18.91 ? 35 GLU A CA 1 ATOM 265 C C . GLU A 1 35 ? 12.843 26.387 23.908 1.00 21.29 ? 35 GLU A C 1 ATOM 266 O O . GLU A 1 35 ? 13.994 26.111 24.262 1.00 20.69 ? 35 GLU A O 1 ATOM 267 C CB . GLU A 1 35 ? 11.731 24.165 23.792 1.00 19.48 ? 35 GLU A CB 1 ATOM 268 C CG . GLU A 1 35 ? 10.598 24.397 24.679 1.00 23.75 ? 35 GLU A CG 1 ATOM 269 C CD . GLU A 1 35 ? 9.410 24.887 23.895 1.00 28.20 ? 35 GLU A CD 1 ATOM 270 O OE1 . GLU A 1 35 ? 8.860 24.168 23.020 1.00 32.25 ? 35 GLU A OE1 1 ATOM 271 O OE2 . GLU A 1 35 ? 9.049 26.049 24.057 1.00 32.58 ? 35 GLU A OE2 1 ATOM 272 N N . MET A 1 36 ? 12.239 27.533 24.257 1.00 19.31 ? 36 MET A N 1 ATOM 273 C CA . MET A 1 36 ? 12.887 28.486 25.149 1.00 20.96 ? 36 MET A CA 1 ATOM 274 C C . MET A 1 36 ? 11.781 29.391 25.645 1.00 21.76 ? 36 MET A C 1 ATOM 275 O O . MET A 1 36 ? 10.611 29.300 25.229 1.00 22.27 ? 36 MET A O 1 ATOM 276 C CB . MET A 1 36 ? 13.964 29.269 24.431 1.00 19.53 ? 36 MET A CB 1 ATOM 277 C CG . MET A 1 36 ? 13.362 30.233 23.485 1.00 21.33 ? 36 MET A CG 1 ATOM 278 S SD . MET A 1 36 ? 14.576 31.172 22.583 1.00 27.14 ? 36 MET A SD 1 ATOM 279 C CE . MET A 1 36 ? 15.310 32.129 23.917 1.00 23.58 ? 36 MET A CE 1 ATOM 280 N N . SER A 1 37 ? 12.047 30.175 26.660 1.00 25.09 ? 37 SER A N 1 ATOM 281 C CA . SER A 1 37 ? 10.924 30.993 27.051 1.00 28.77 ? 37 SER A CA 1 ATOM 282 C C . SER A 1 37 ? 11.175 32.477 26.788 1.00 28.20 ? 37 SER A C 1 ATOM 283 O O . SER A 1 37 ? 12.265 32.993 26.929 1.00 27.84 ? 37 SER A O 1 ATOM 284 C CB . SER A 1 37 ? 10.544 30.730 28.482 1.00 33.14 ? 37 SER A CB 1 ATOM 285 O OG . SER A 1 37 ? 11.605 31.196 29.277 1.00 33.01 ? 37 SER A OG 1 ATOM 286 N N . LEU A 1 38 ? 10.187 33.095 26.209 1.00 27.46 ? 38 LEU A N 1 ATOM 287 C CA . LEU A 1 38 ? 10.307 34.461 25.915 1.00 27.71 ? 38 LEU A CA 1 ATOM 288 C C . LEU A 1 38 ? 9.135 34.967 26.672 1.00 30.02 ? 38 LEU A C 1 ATOM 289 O O . LEU A 1 38 ? 8.199 34.254 27.082 1.00 30.18 ? 38 LEU A O 1 ATOM 290 C CB . LEU A 1 38 ? 10.152 34.736 24.431 1.00 25.23 ? 38 LEU A CB 1 ATOM 291 C CG . LEU A 1 38 ? 11.333 34.174 23.690 1.00 24.39 ? 38 LEU A CG 1 ATOM 292 C CD1 . LEU A 1 38 ? 11.148 34.065 22.152 1.00 21.56 ? 38 LEU A CD1 1 ATOM 293 C CD2 . LEU A 1 38 ? 12.450 35.098 24.073 1.00 27.18 ? 38 LEU A CD2 1 ATOM 294 N N . PRO A 1 39 ? 9.237 36.216 26.978 1.00 33.46 ? 39 PRO A N 1 ATOM 295 C CA . PRO A 1 39 ? 8.258 37.000 27.707 1.00 34.84 ? 39 PRO A CA 1 ATOM 296 C C . PRO A 1 39 ? 7.221 37.494 26.725 1.00 34.71 ? 39 PRO A C 1 ATOM 297 O O . PRO A 1 39 ? 7.538 37.890 25.572 1.00 33.60 ? 39 PRO A O 1 ATOM 298 C CB . PRO A 1 39 ? 9.092 38.184 28.164 1.00 35.77 ? 39 PRO A CB 1 ATOM 299 C CG . PRO A 1 39 ? 9.898 38.450 26.896 1.00 35.89 ? 39 PRO A CG 1 ATOM 300 C CD . PRO A 1 39 ? 10.355 37.044 26.491 1.00 33.27 ? 39 PRO A CD 1 ATOM 301 N N . GLY A 1 40 ? 5.973 37.425 27.132 1.00 35.33 ? 40 GLY A N 1 ATOM 302 C CA . GLY A 1 40 ? 4.990 37.984 26.248 1.00 36.49 ? 40 GLY A CA 1 ATOM 303 C C . GLY A 1 40 ? 3.850 37.066 26.091 1.00 36.06 ? 40 GLY A C 1 ATOM 304 O O . GLY A 1 40 ? 3.800 36.012 26.720 1.00 37.53 ? 40 GLY A O 1 ATOM 305 N N . ARG A 1 41 ? 2.880 37.574 25.367 1.00 35.75 ? 41 ARG A N 1 ATOM 306 C CA . ARG A 1 41 ? 1.695 36.819 25.062 1.00 38.25 ? 41 ARG A CA 1 ATOM 307 C C . ARG A 1 41 ? 2.121 36.060 23.810 1.00 35.76 ? 41 ARG A C 1 ATOM 308 O O . ARG A 1 41 ? 2.984 36.548 23.056 1.00 34.16 ? 41 ARG A O 1 ATOM 309 C CB . ARG A 1 41 ? 0.524 37.769 24.704 1.00 41.56 ? 41 ARG A CB 1 ATOM 310 C CG . ARG A 1 41 ? -0.351 38.235 25.903 1.00 49.74 ? 41 ARG A CG 1 ATOM 311 C CD . ARG A 1 41 ? -1.199 37.050 26.504 1.00 56.04 ? 41 ARG A CD 1 ATOM 312 N NE . ARG A 1 41 ? -0.457 35.779 26.450 1.00 62.04 ? 41 ARG A NE 1 ATOM 313 C CZ . ARG A 1 41 ? -0.938 34.615 25.990 1.00 64.72 ? 41 ARG A CZ 1 ATOM 314 N NH1 . ARG A 1 41 ? -2.214 34.519 25.547 1.00 65.83 ? 41 ARG A NH1 1 ATOM 315 N NH2 . ARG A 1 41 ? -0.106 33.564 25.907 1.00 64.06 ? 41 ARG A NH2 1 ATOM 316 N N . TRP A 1 42 ? 1.598 34.851 23.639 1.00 33.91 ? 42 TRP A N 1 ATOM 317 C CA . TRP A 1 42 ? 1.896 34.086 22.441 1.00 29.99 ? 42 TRP A CA 1 ATOM 318 C C . TRP A 1 42 ? 0.614 33.443 21.870 1.00 28.94 ? 42 TRP A C 1 ATOM 319 O O . TRP A 1 42 ? -0.402 33.361 22.529 1.00 26.90 ? 42 TRP A O 1 ATOM 320 C CB . TRP A 1 42 ? 3.011 33.099 22.734 1.00 30.74 ? 42 TRP A CB 1 ATOM 321 C CG . TRP A 1 42 ? 2.632 32.120 23.787 1.00 33.49 ? 42 TRP A CG 1 ATOM 322 C CD1 . TRP A 1 42 ? 2.982 32.152 25.099 1.00 33.11 ? 42 TRP A CD1 1 ATOM 323 C CD2 . TRP A 1 42 ? 1.818 30.946 23.602 1.00 33.40 ? 42 TRP A CD2 1 ATOM 324 N NE1 . TRP A 1 42 ? 2.440 31.057 25.744 1.00 35.01 ? 42 TRP A NE1 1 ATOM 325 C CE2 . TRP A 1 42 ? 1.713 30.313 24.851 1.00 33.51 ? 42 TRP A CE2 1 ATOM 326 C CE3 . TRP A 1 42 ? 1.166 30.375 22.494 1.00 32.84 ? 42 TRP A CE3 1 ATOM 327 C CZ2 . TRP A 1 42 ? 0.988 29.151 25.029 1.00 33.55 ? 42 TRP A CZ2 1 ATOM 328 C CZ3 . TRP A 1 42 ? 0.452 29.223 22.673 1.00 33.01 ? 42 TRP A CZ3 1 ATOM 329 C CH2 . TRP A 1 42 ? 0.364 28.620 23.926 1.00 32.71 ? 42 TRP A CH2 1 ATOM 330 N N . LYS A 1 43 ? 0.671 33.069 20.597 1.00 28.19 ? 43 LYS A N 1 ATOM 331 C CA . LYS A 1 43 ? -0.437 32.498 19.852 1.00 26.94 ? 43 LYS A CA 1 ATOM 332 C C . LYS A 1 43 ? 0.019 31.131 19.296 1.00 24.62 ? 43 LYS A C 1 ATOM 333 O O . LYS A 1 43 ? 1.162 31.020 18.867 1.00 21.71 ? 43 LYS A O 1 ATOM 334 C CB . LYS A 1 43 ? -0.683 33.412 18.627 1.00 30.53 ? 43 LYS A CB 1 ATOM 335 C CG . LYS A 1 43 ? -2.052 34.014 18.528 1.00 40.10 ? 43 LYS A CG 1 ATOM 336 C CD . LYS A 1 43 ? -3.005 33.305 17.427 1.00 45.33 ? 43 LYS A CD 1 ATOM 337 C CE . LYS A 1 43 ? -3.625 31.897 17.873 1.00 47.15 ? 43 LYS A CE 1 ATOM 338 N NZ . LYS A 1 43 ? -3.514 30.716 16.861 1.00 43.07 ? 43 LYS A NZ 1 ATOM 339 N N . PRO A 1 44 ? -0.852 30.085 19.319 1.00 23.58 ? 44 PRO A N 1 ATOM 340 C CA . PRO A 1 44 ? -0.457 28.778 18.766 1.00 22.19 ? 44 PRO A CA 1 ATOM 341 C C . PRO A 1 44 ? -0.446 28.865 17.235 1.00 20.30 ? 44 PRO A C 1 ATOM 342 O O . PRO A 1 44 ? -1.269 29.543 16.597 1.00 19.82 ? 44 PRO A O 1 ATOM 343 C CB . PRO A 1 44 ? -1.580 27.857 19.223 1.00 21.38 ? 44 PRO A CB 1 ATOM 344 C CG . PRO A 1 44 ? -2.023 28.440 20.491 1.00 24.27 ? 44 PRO A CG 1 ATOM 345 C CD . PRO A 1 44 ? -2.006 29.924 20.229 1.00 23.31 ? 44 PRO A CD 1 ATOM 346 N N . LYS A 1 45 ? 0.430 28.093 16.629 1.00 19.03 ? 45 LYS A N 1 ATOM 347 C CA . LYS A 1 45 ? 0.531 28.095 15.153 1.00 18.93 ? 45 LYS A CA 1 ATOM 348 C C . LYS A 1 45 ? 1.012 26.701 14.751 1.00 16.34 ? 45 LYS A C 1 ATOM 349 O O . LYS A 1 45 ? 1.619 26.028 15.566 1.00 15.52 ? 45 LYS A O 1 ATOM 350 C CB . LYS A 1 45 ? 1.597 29.134 14.724 1.00 17.99 ? 45 LYS A CB 1 ATOM 351 C CG . LYS A 1 45 ? 1.641 29.395 13.308 1.00 21.46 ? 45 LYS A CG 1 ATOM 352 C CD . LYS A 1 45 ? 2.612 30.488 13.059 1.00 24.32 ? 45 LYS A CD 1 ATOM 353 C CE . LYS A 1 45 ? 2.854 30.732 11.563 1.00 28.20 ? 45 LYS A CE 1 ATOM 354 N NZ . LYS A 1 45 ? 1.649 31.102 10.815 1.00 29.29 ? 45 LYS A NZ 1 ATOM 355 N N . MET A 1 46 ? 0.705 26.264 13.536 1.00 14.26 ? 46 MET A N 1 ATOM 356 C CA . MET A 1 46 ? 1.193 24.987 13.057 1.00 15.66 ? 46 MET A CA 1 ATOM 357 C C . MET A 1 46 ? 2.097 25.303 11.868 1.00 16.43 ? 46 MET A C 1 ATOM 358 O O . MET A 1 46 ? 1.709 26.124 11.055 1.00 16.51 ? 46 MET A O 1 ATOM 359 C CB . MET A 1 46 ? 0.032 24.210 12.530 1.00 17.54 ? 46 MET A CB 1 ATOM 360 C CG . MET A 1 46 ? 0.330 22.809 12.435 1.00 31.05 ? 46 MET A CG 1 ATOM 361 S SD . MET A 1 46 ? 0.252 22.156 14.187 1.00 35.66 ? 46 MET A SD 1 ATOM 362 C CE . MET A 1 46 ? -1.343 22.888 14.431 1.00 33.02 ? 46 MET A CE 1 ATOM 363 N N . ILE A 1 47 ? 3.323 24.809 11.782 1.00 15.02 ? 47 ILE A N 1 ATOM 364 C CA . ILE A 1 47 ? 4.071 25.128 10.584 1.00 17.38 ? 47 ILE A CA 1 ATOM 365 C C . ILE A 1 47 ? 4.471 23.787 9.998 1.00 18.79 ? 47 ILE A C 1 ATOM 366 O O . ILE A 1 47 ? 4.789 22.886 10.738 1.00 20.34 ? 47 ILE A O 1 ATOM 367 C CB . ILE A 1 47 ? 5.308 25.960 10.772 1.00 17.54 ? 47 ILE A CB 1 ATOM 368 C CG1 . ILE A 1 47 ? 6.167 25.321 11.809 1.00 18.98 ? 47 ILE A CG1 1 ATOM 369 C CG2 . ILE A 1 47 ? 4.966 27.403 11.085 1.00 20.65 ? 47 ILE A CG2 1 ATOM 370 C CD1 . ILE A 1 47 ? 6.789 26.333 12.719 1.00 27.00 ? 47 ILE A CD1 1 ATOM 371 N N . GLY A 1 48 ? 4.477 23.654 8.672 1.00 20.37 ? 48 GLY A N 1 ATOM 372 C CA . GLY A 1 48 ? 4.782 22.349 8.100 1.00 23.77 ? 48 GLY A CA 1 ATOM 373 C C . GLY A 1 48 ? 5.912 22.371 7.142 1.00 24.09 ? 48 GLY A C 1 ATOM 374 O O . GLY A 1 48 ? 6.240 23.401 6.611 1.00 25.58 ? 48 GLY A O 1 ATOM 375 N N . GLY A 1 49 ? 6.528 21.246 6.932 1.00 24.87 ? 49 GLY A N 1 ATOM 376 C CA . GLY A 1 49 ? 7.598 21.222 5.997 1.00 26.63 ? 49 GLY A CA 1 ATOM 377 C C . GLY A 1 49 ? 7.800 19.809 5.573 1.00 26.70 ? 49 GLY A C 1 ATOM 378 O O . GLY A 1 49 ? 6.881 19.008 5.615 1.00 24.22 ? 49 GLY A O 1 ATOM 379 N N . ILE A 1 50 ? 9.029 19.497 5.211 1.00 27.24 ? 50 ILE A N 1 ATOM 380 C CA . ILE A 1 50 ? 9.360 18.128 4.863 1.00 28.61 ? 50 ILE A CA 1 ATOM 381 C C . ILE A 1 50 ? 9.109 17.367 6.132 1.00 27.95 ? 50 ILE A C 1 ATOM 382 O O . ILE A 1 50 ? 9.586 17.759 7.197 1.00 28.30 ? 50 ILE A O 1 ATOM 383 C CB . ILE A 1 50 ? 10.845 18.013 4.511 1.00 29.75 ? 50 ILE A CB 1 ATOM 384 C CG1 . ILE A 1 50 ? 11.051 18.619 3.085 1.00 32.65 ? 50 ILE A CG1 1 ATOM 385 C CG2 . ILE A 1 50 ? 11.365 16.622 4.801 1.00 27.85 ? 50 ILE A CG2 1 ATOM 386 C CD1 . ILE A 1 50 ? 11.531 17.668 2.001 1.00 32.53 ? 50 ILE A CD1 1 ATOM 387 N N . GLY A 1 51 ? 8.287 16.348 6.035 1.00 27.86 ? 51 GLY A N 1 ATOM 388 C CA . GLY A 1 51 ? 8.024 15.572 7.215 1.00 27.77 ? 51 GLY A CA 1 ATOM 389 C C . GLY A 1 51 ? 6.715 15.923 7.867 1.00 27.55 ? 51 GLY A C 1 ATOM 390 O O . GLY A 1 51 ? 6.311 15.201 8.750 1.00 29.91 ? 51 GLY A O 1 ATOM 391 N N . GLY A 1 52 ? 6.034 16.982 7.445 1.00 26.10 ? 52 GLY A N 1 ATOM 392 C CA . GLY A 1 52 ? 4.763 17.298 8.083 1.00 24.16 ? 52 GLY A CA 1 ATOM 393 C C . GLY A 1 52 ? 4.777 18.563 8.924 1.00 24.10 ? 52 GLY A C 1 ATOM 394 O O . GLY A 1 52 ? 5.740 19.330 8.872 1.00 24.57 ? 52 GLY A O 1 ATOM 395 N N . PHE A 1 53 ? 3.805 18.712 9.807 1.00 21.63 ? 53 PHE A N 1 ATOM 396 C CA . PHE A 1 53 ? 3.668 19.943 10.556 1.00 19.37 ? 53 PHE A CA 1 ATOM 397 C C . PHE A 1 53 ? 4.062 19.822 11.975 1.00 19.98 ? 53 PHE A C 1 ATOM 398 O O . PHE A 1 53 ? 3.951 18.731 12.521 1.00 21.58 ? 53 PHE A O 1 ATOM 399 C CB . PHE A 1 53 ? 2.204 20.350 10.560 1.00 19.48 ? 53 PHE A CB 1 ATOM 400 C CG . PHE A 1 53 ? 1.739 20.915 9.317 1.00 20.59 ? 53 PHE A CG 1 ATOM 401 C CD1 . PHE A 1 53 ? 1.540 20.105 8.216 1.00 22.18 ? 53 PHE A CD1 1 ATOM 402 C CD2 . PHE A 1 53 ? 1.555 22.275 9.210 1.00 19.30 ? 53 PHE A CD2 1 ATOM 403 C CE1 . PHE A 1 53 ? 1.167 20.654 6.976 1.00 21.11 ? 53 PHE A CE1 1 ATOM 404 C CE2 . PHE A 1 53 ? 1.186 22.853 8.009 1.00 21.29 ? 53 PHE A CE2 1 ATOM 405 C CZ . PHE A 1 53 ? 0.992 22.019 6.862 1.00 22.88 ? 53 PHE A CZ 1 ATOM 406 N N . ILE A 1 54 ? 4.436 20.938 12.609 1.00 17.61 ? 54 ILE A N 1 ATOM 407 C CA . ILE A 1 54 ? 4.761 20.971 14.053 1.00 18.48 ? 54 ILE A CA 1 ATOM 408 C C . ILE A 1 54 ? 4.015 22.160 14.659 1.00 17.41 ? 54 ILE A C 1 ATOM 409 O O . ILE A 1 54 ? 3.673 23.092 13.957 1.00 14.86 ? 54 ILE A O 1 ATOM 410 C CB . ILE A 1 54 ? 6.308 21.040 14.425 1.00 19.65 ? 54 ILE A CB 1 ATOM 411 C CG1 . ILE A 1 54 ? 7.008 22.272 13.815 1.00 19.28 ? 54 ILE A CG1 1 ATOM 412 C CG2 . ILE A 1 54 ? 6.987 19.758 13.997 1.00 21.19 ? 54 ILE A CG2 1 ATOM 413 C CD1 . ILE A 1 54 ? 8.387 22.583 14.412 1.00 17.22 ? 54 ILE A CD1 1 ATOM 414 N N . LYS A 1 55 ? 3.647 22.034 15.928 1.00 17.13 ? 55 LYS A N 1 ATOM 415 C CA . LYS A 1 55 ? 2.946 23.126 16.621 1.00 18.88 ? 55 LYS A CA 1 ATOM 416 C C . LYS A 1 55 ? 4.035 23.984 17.305 1.00 16.82 ? 55 LYS A C 1 ATOM 417 O O . LYS A 1 55 ? 5.009 23.458 17.890 1.00 15.94 ? 55 LYS A O 1 ATOM 418 C CB . LYS A 1 55 ? 1.949 22.590 17.645 1.00 20.19 ? 55 LYS A CB 1 ATOM 419 C CG . LYS A 1 55 ? 1.327 23.682 18.561 1.00 24.49 ? 55 LYS A CG 1 ATOM 420 C CD . LYS A 1 55 ? -0.226 23.868 18.327 1.00 34.13 ? 55 LYS A CD 1 ATOM 421 C CE . LYS A 1 55 ? -1.043 23.924 19.726 1.00 39.35 ? 55 LYS A CE 1 ATOM 422 N NZ . LYS A 1 55 ? -2.497 23.398 19.691 1.00 42.22 ? 55 LYS A NZ 1 ATOM 423 N N . VAL A 1 56 ? 3.883 25.287 17.173 1.00 15.07 ? 56 VAL A N 1 ATOM 424 C CA . VAL A 1 56 ? 4.837 26.235 17.730 1.00 15.63 ? 56 VAL A CA 1 ATOM 425 C C . VAL A 1 56 ? 4.075 27.358 18.418 1.00 15.19 ? 56 VAL A C 1 ATOM 426 O O . VAL A 1 56 ? 2.850 27.493 18.266 1.00 14.83 ? 56 VAL A O 1 ATOM 427 C CB . VAL A 1 56 ? 5.730 26.911 16.597 1.00 15.39 ? 56 VAL A CB 1 ATOM 428 C CG1 . VAL A 1 56 ? 6.742 25.905 15.989 1.00 11.48 ? 56 VAL A CG1 1 ATOM 429 C CG2 . VAL A 1 56 ? 4.804 27.471 15.476 1.00 11.91 ? 56 VAL A CG2 1 ATOM 430 N N . ARG A 1 57 ? 4.796 28.100 19.245 1.00 15.81 ? 57 ARG A N 1 ATOM 431 C CA . ARG A 1 57 ? 4.205 29.278 19.900 1.00 15.35 ? 57 ARG A CA 1 ATOM 432 C C . ARG A 1 57 ? 4.772 30.530 19.160 1.00 12.99 ? 57 ARG A C 1 ATOM 433 O O . ARG A 1 57 ? 5.967 30.675 19.002 1.00 12.65 ? 57 ARG A O 1 ATOM 434 C CB . ARG A 1 57 ? 4.549 29.216 21.384 1.00 17.10 ? 57 ARG A CB 1 ATOM 435 C CG . ARG A 1 57 ? 4.175 27.860 21.969 1.00 22.00 ? 57 ARG A CG 1 ATOM 436 C CD . ARG A 1 57 ? 4.581 27.733 23.422 1.00 28.79 ? 57 ARG A CD 1 ATOM 437 N NE . ARG A 1 57 ? 6.038 27.519 23.698 1.00 31.69 ? 57 ARG A NE 1 ATOM 438 C CZ . ARG A 1 57 ? 6.744 28.444 24.334 1.00 32.07 ? 57 ARG A CZ 1 ATOM 439 N NH1 . ARG A 1 57 ? 6.111 29.518 24.663 1.00 34.01 ? 57 ARG A NH1 1 ATOM 440 N NH2 . ARG A 1 57 ? 8.002 28.315 24.750 1.00 33.86 ? 57 ARG A NH2 1 ATOM 441 N N . GLN A 1 58 ? 3.914 31.416 18.680 1.00 12.96 ? 58 GLN A N 1 ATOM 442 C CA . GLN A 1 58 ? 4.325 32.577 17.944 1.00 12.99 ? 58 GLN A CA 1 ATOM 443 C C . GLN A 1 58 ? 4.430 33.773 18.828 1.00 16.00 ? 58 GLN A C 1 ATOM 444 O O . GLN A 1 58 ? 3.450 34.125 19.503 1.00 14.55 ? 58 GLN A O 1 ATOM 445 C CB . GLN A 1 58 ? 3.249 32.899 17.014 1.00 12.15 ? 58 GLN A CB 1 ATOM 446 C CG . GLN A 1 58 ? 3.650 33.932 16.186 1.00 19.96 ? 58 GLN A CG 1 ATOM 447 C CD . GLN A 1 58 ? 2.519 34.396 15.349 1.00 25.38 ? 58 GLN A CD 1 ATOM 448 O OE1 . GLN A 1 58 ? 1.670 33.599 14.940 1.00 27.85 ? 58 GLN A OE1 1 ATOM 449 N NE2 . GLN A 1 58 ? 2.446 35.716 15.121 1.00 25.51 ? 58 GLN A NE2 1 ATOM 450 N N . TYR A 1 59 ? 5.626 34.350 18.878 1.00 17.23 ? 59 TYR A N 1 ATOM 451 C CA . TYR A 1 59 ? 5.882 35.553 19.653 1.00 18.09 ? 59 TYR A CA 1 ATOM 452 C C . TYR A 1 59 ? 6.198 36.670 18.680 1.00 19.03 ? 59 TYR A C 1 ATOM 453 O O . TYR A 1 59 ? 7.048 36.532 17.860 1.00 19.05 ? 59 TYR A O 1 ATOM 454 C CB . TYR A 1 59 ? 7.073 35.402 20.577 1.00 18.05 ? 59 TYR A CB 1 ATOM 455 C CG . TYR A 1 59 ? 6.828 34.536 21.757 1.00 20.96 ? 59 TYR A CG 1 ATOM 456 C CD1 . TYR A 1 59 ? 7.014 33.162 21.631 1.00 18.85 ? 59 TYR A CD1 1 ATOM 457 C CD2 . TYR A 1 59 ? 6.512 35.089 23.025 1.00 19.78 ? 59 TYR A CD2 1 ATOM 458 C CE1 . TYR A 1 59 ? 6.932 32.363 22.704 1.00 23.75 ? 59 TYR A CE1 1 ATOM 459 C CE2 . TYR A 1 59 ? 6.397 34.278 24.132 1.00 22.13 ? 59 TYR A CE2 1 ATOM 460 C CZ . TYR A 1 59 ? 6.624 32.918 23.959 1.00 23.80 ? 59 TYR A CZ 1 ATOM 461 O OH . TYR A 1 59 ? 6.644 32.043 24.990 1.00 27.68 ? 59 TYR A OH 1 ATOM 462 N N . ASP A 1 60 ? 5.588 37.832 18.851 1.00 22.04 ? 60 ASP A N 1 ATOM 463 C CA . ASP A 1 60 ? 5.806 38.964 17.941 1.00 23.37 ? 60 ASP A CA 1 ATOM 464 C C . ASP A 1 60 ? 6.691 40.008 18.571 1.00 23.83 ? 60 ASP A C 1 ATOM 465 O O . ASP A 1 60 ? 6.911 40.004 19.798 1.00 24.71 ? 60 ASP A O 1 ATOM 466 C CB . ASP A 1 60 ? 4.465 39.612 17.626 1.00 23.75 ? 60 ASP A CB 1 ATOM 467 C CG . ASP A 1 60 ? 3.526 38.668 16.920 1.00 26.07 ? 60 ASP A CG 1 ATOM 468 O OD1 . ASP A 1 60 ? 3.958 37.919 16.056 1.00 28.19 ? 60 ASP A OD1 1 ATOM 469 O OD2 . ASP A 1 60 ? 2.348 38.654 17.185 1.00 28.87 ? 60 ASP A OD2 1 ATOM 470 N N . GLN A 1 61 ? 7.316 40.807 17.721 1.00 23.65 ? 61 GLN A N 1 ATOM 471 C CA . GLN A 1 61 ? 8.106 41.930 18.191 1.00 24.84 ? 61 GLN A CA 1 ATOM 472 C C . GLN A 1 61 ? 9.227 41.463 19.042 1.00 24.07 ? 61 GLN A C 1 ATOM 473 O O . GLN A 1 61 ? 9.431 41.989 20.137 1.00 25.94 ? 61 GLN A O 1 ATOM 474 C CB . GLN A 1 61 ? 7.190 42.881 19.018 1.00 28.16 ? 61 GLN A CB 1 ATOM 475 C CG . GLN A 1 61 ? 6.813 44.250 18.516 1.00 36.90 ? 61 GLN A CG 1 ATOM 476 C CD . GLN A 1 61 ? 5.841 44.274 17.360 1.00 42.58 ? 61 GLN A CD 1 ATOM 477 O OE1 . GLN A 1 61 ? 5.332 43.240 16.968 1.00 46.14 ? 61 GLN A OE1 1 ATOM 478 N NE2 . GLN A 1 61 ? 5.593 45.477 16.784 1.00 44.75 ? 61 GLN A NE2 1 ATOM 479 N N . ILE A 1 62 ? 9.953 40.453 18.605 1.00 23.01 ? 62 ILE A N 1 ATOM 480 C CA . ILE A 1 62 ? 11.102 40.015 19.392 1.00 21.42 ? 62 ILE A CA 1 ATOM 481 C C . ILE A 1 62 ? 12.369 40.624 18.824 1.00 21.75 ? 62 ILE A C 1 ATOM 482 O O . ILE A 1 62 ? 12.516 40.740 17.588 1.00 20.64 ? 62 ILE A O 1 ATOM 483 C CB . ILE A 1 62 ? 11.288 38.471 19.327 1.00 22.62 ? 62 ILE A CB 1 ATOM 484 C CG1 . ILE A 1 62 ? 10.083 37.789 19.971 1.00 20.91 ? 62 ILE A CG1 1 ATOM 485 C CG2 . ILE A 1 62 ? 12.635 38.060 19.983 1.00 19.80 ? 62 ILE A CG2 1 ATOM 486 C CD1 . ILE A 1 62 ? 9.632 38.341 21.370 1.00 20.98 ? 62 ILE A CD1 1 ATOM 487 N N . LEU A 1 63 ? 13.287 41.019 19.690 1.00 20.36 ? 63 LEU A N 1 ATOM 488 C CA . LEU A 1 63 ? 14.510 41.540 19.184 1.00 22.08 ? 63 LEU A CA 1 ATOM 489 C C . LEU A 1 63 ? 15.572 40.439 19.087 1.00 22.23 ? 63 LEU A C 1 ATOM 490 O O . LEU A 1 63 ? 15.709 39.607 19.949 1.00 21.20 ? 63 LEU A O 1 ATOM 491 C CB . LEU A 1 63 ? 15.042 42.719 20.002 1.00 24.49 ? 63 LEU A CB 1 ATOM 492 C CG . LEU A 1 63 ? 16.381 43.103 19.302 1.00 28.68 ? 63 LEU A CG 1 ATOM 493 C CD1 . LEU A 1 63 ? 16.250 44.359 18.513 1.00 32.62 ? 63 LEU A CD1 1 ATOM 494 C CD2 . LEU A 1 63 ? 17.564 43.215 20.221 1.00 33.63 ? 63 LEU A CD2 1 ATOM 495 N N . ILE A 1 64 ? 16.282 40.421 17.982 1.00 22.17 ? 64 ILE A N 1 ATOM 496 C CA . ILE A 1 64 ? 17.352 39.472 17.803 1.00 25.19 ? 64 ILE A CA 1 ATOM 497 C C . ILE A 1 64 ? 18.556 40.183 17.198 1.00 24.70 ? 64 ILE A C 1 ATOM 498 O O . ILE A 1 64 ? 18.442 41.092 16.364 1.00 25.79 ? 64 ILE A O 1 ATOM 499 C CB . ILE A 1 64 ? 17.023 38.273 16.772 1.00 27.64 ? 64 ILE A CB 1 ATOM 500 C CG1 . ILE A 1 64 ? 15.867 37.383 17.219 1.00 29.33 ? 64 ILE A CG1 1 ATOM 501 C CG2 . ILE A 1 64 ? 18.216 37.238 16.708 1.00 26.70 ? 64 ILE A CG2 1 ATOM 502 C CD1 . ILE A 1 64 ? 16.058 35.916 16.608 1.00 30.33 ? 64 ILE A CD1 1 ATOM 503 N N . GLU A 1 65 ? 19.708 39.680 17.542 1.00 23.79 ? 65 GLU A N 1 ATOM 504 C CA . GLU A 1 65 ? 20.921 40.192 16.999 1.00 28.13 ? 65 GLU A CA 1 ATOM 505 C C . GLU A 1 65 ? 21.581 39.085 16.190 1.00 27.44 ? 65 GLU A C 1 ATOM 506 O O . GLU A 1 65 ? 22.035 38.053 16.763 1.00 26.48 ? 65 GLU A O 1 ATOM 507 C CB . GLU A 1 65 ? 21.812 40.538 18.134 1.00 29.91 ? 65 GLU A CB 1 ATOM 508 C CG . GLU A 1 65 ? 22.356 41.800 17.937 1.00 38.83 ? 65 GLU A CG 1 ATOM 509 C CD . GLU A 1 65 ? 22.802 42.298 19.230 1.00 43.92 ? 65 GLU A CD 1 ATOM 510 O OE1 . GLU A 1 65 ? 21.911 42.893 19.926 1.00 49.14 ? 65 GLU A OE1 1 ATOM 511 O OE2 . GLU A 1 65 ? 23.984 41.990 19.579 1.00 44.37 ? 65 GLU A OE2 1 ATOM 512 N N . ILE A 1 66 ? 21.673 39.317 14.884 1.00 27.52 ? 66 ILE A N 1 ATOM 513 C CA . ILE A 1 66 ? 22.263 38.351 13.956 1.00 28.61 ? 66 ILE A CA 1 ATOM 514 C C . ILE A 1 66 ? 23.605 38.863 13.492 1.00 28.70 ? 66 ILE A C 1 ATOM 515 O O . ILE A 1 66 ? 23.689 39.844 12.776 1.00 26.48 ? 66 ILE A O 1 ATOM 516 C CB . ILE A 1 66 ? 21.306 38.009 12.703 1.00 28.38 ? 66 ILE A CB 1 ATOM 517 C CG1 . ILE A 1 66 ? 19.964 37.413 13.130 1.00 28.62 ? 66 ILE A CG1 1 ATOM 518 C CG2 . ILE A 1 66 ? 21.921 36.860 11.850 1.00 29.08 ? 66 ILE A CG2 1 ATOM 519 C CD1 . ILE A 1 66 ? 18.741 38.214 12.813 1.00 27.93 ? 66 ILE A CD1 1 ATOM 520 N N . CYS A 1 67 ? 24.660 38.208 13.936 1.00 33.03 ? 67 CYS A N 1 ATOM 521 C CA . CYS A 1 67 ? 25.984 38.625 13.548 1.00 39.18 ? 67 CYS A CA 1 ATOM 522 C C . CYS A 1 67 ? 26.128 40.073 13.803 1.00 41.03 ? 67 CYS A C 1 ATOM 523 O O . CYS A 1 67 ? 26.567 40.789 12.924 1.00 44.21 ? 67 CYS A O 1 ATOM 524 C CB . CYS A 1 67 ? 26.190 38.487 12.046 1.00 40.99 ? 67 CYS A CB 1 ATOM 525 S SG . CYS A 1 67 ? 26.546 36.894 11.506 1.00 49.77 ? 67 CYS A SG 1 ATOM 526 N N . GLY A 1 68 ? 25.630 40.576 14.914 1.00 43.50 ? 68 GLY A N 1 ATOM 527 C CA . GLY A 1 68 ? 25.792 42.011 15.143 1.00 42.45 ? 68 GLY A CA 1 ATOM 528 C C . GLY A 1 68 ? 24.773 42.941 14.530 1.00 42.13 ? 68 GLY A C 1 ATOM 529 O O . GLY A 1 68 ? 24.815 44.111 14.803 1.00 44.20 ? 68 GLY A O 1 ATOM 530 N N . HIS A 1 69 ? 23.859 42.481 13.687 1.00 41.78 ? 69 HIS A N 1 ATOM 531 C CA . HIS A 1 69 ? 22.860 43.424 13.163 1.00 39.82 ? 69 HIS A CA 1 ATOM 532 C C . HIS A 1 69 ? 21.572 43.124 13.904 1.00 37.56 ? 69 HIS A C 1 ATOM 533 O O . HIS A 1 69 ? 21.068 42.009 13.854 1.00 36.96 ? 69 HIS A O 1 ATOM 534 C CB . HIS A 1 69 ? 22.561 43.257 11.663 1.00 41.98 ? 69 HIS A CB 1 ATOM 535 C CG . HIS A 1 69 ? 23.777 43.169 10.769 1.00 45.03 ? 69 HIS A CG 1 ATOM 536 N ND1 . HIS A 1 69 ? 24.816 42.266 10.978 1.00 44.81 ? 69 HIS A ND1 1 ATOM 537 C CD2 . HIS A 1 69 ? 24.081 43.832 9.620 1.00 43.86 ? 69 HIS A CD2 1 ATOM 538 C CE1 . HIS A 1 69 ? 25.704 42.386 10.005 1.00 43.98 ? 69 HIS A CE1 1 ATOM 539 N NE2 . HIS A 1 69 ? 25.281 43.323 9.169 1.00 46.00 ? 69 HIS A NE2 1 ATOM 540 N N . LYS A 1 70 ? 21.084 44.110 14.634 1.00 34.87 ? 70 LYS A N 1 ATOM 541 C CA . LYS A 1 70 ? 19.844 43.982 15.327 1.00 33.47 ? 70 LYS A CA 1 ATOM 542 C C . LYS A 1 70 ? 18.731 43.848 14.270 1.00 31.90 ? 70 LYS A C 1 ATOM 543 O O . LYS A 1 70 ? 18.795 44.452 13.157 1.00 33.10 ? 70 LYS A O 1 ATOM 544 C CB . LYS A 1 70 ? 19.573 45.231 16.137 1.00 34.35 ? 70 LYS A CB 1 ATOM 545 C CG . LYS A 1 70 ? 20.052 45.186 17.545 1.00 41.44 ? 70 LYS A CG 1 ATOM 546 C CD . LYS A 1 70 ? 21.579 45.323 17.609 1.00 46.41 ? 70 LYS A CD 1 ATOM 547 C CE . LYS A 1 70 ? 22.116 46.045 18.924 1.00 48.15 ? 70 LYS A CE 1 ATOM 548 N NZ . LYS A 1 70 ? 23.668 45.879 19.155 1.00 51.73 ? 70 LYS A NZ 1 ATOM 549 N N . ALA A 1 71 ? 17.691 43.102 14.650 1.00 28.17 ? 71 ALA A N 1 ATOM 550 C CA . ALA A 1 71 ? 16.495 42.885 13.835 1.00 26.21 ? 71 ALA A CA 1 ATOM 551 C C . ALA A 1 71 ? 15.254 42.640 14.780 1.00 26.17 ? 71 ALA A C 1 ATOM 552 O O . ALA A 1 71 ? 15.375 42.175 15.953 1.00 25.86 ? 71 ALA A O 1 ATOM 553 C CB . ALA A 1 71 ? 16.707 41.719 12.846 1.00 24.72 ? 71 ALA A CB 1 ATOM 554 N N . ILE A 1 72 ? 14.083 43.041 14.313 1.00 23.60 ? 72 ILE A N 1 ATOM 555 C CA . ILE A 1 72 ? 12.913 42.831 15.105 1.00 23.15 ? 72 ILE A CA 1 ATOM 556 C C . ILE A 1 72 ? 11.941 42.042 14.262 1.00 20.10 ? 72 ILE A C 1 ATOM 557 O O . ILE A 1 72 ? 11.857 42.261 13.046 1.00 21.85 ? 72 ILE A O 1 ATOM 558 C CB . ILE A 1 72 ? 12.204 44.159 15.513 1.00 25.62 ? 72 ILE A CB 1 ATOM 559 C CG1 . ILE A 1 72 ? 13.169 45.109 16.238 1.00 28.22 ? 72 ILE A CG1 1 ATOM 560 C CG2 . ILE A 1 72 ? 10.995 43.819 16.422 1.00 24.61 ? 72 ILE A CG2 1 ATOM 561 C CD1 . ILE A 1 72 ? 14.017 45.950 15.272 1.00 33.38 ? 72 ILE A CD1 1 ATOM 562 N N . GLY A 1 73 ? 11.270 41.080 14.889 1.00 18.43 ? 73 GLY A N 1 ATOM 563 C CA . GLY A 1 73 ? 10.288 40.302 14.190 1.00 16.23 ? 73 GLY A CA 1 ATOM 564 C C . GLY A 1 73 ? 9.636 39.213 14.979 1.00 15.64 ? 73 GLY A C 1 ATOM 565 O O . GLY A 1 73 ? 9.856 39.050 16.177 1.00 15.71 ? 73 GLY A O 1 ATOM 566 N N . THR A 1 74 ? 8.778 38.491 14.303 1.00 14.15 ? 74 THR A N 1 ATOM 567 C CA . THR A 1 74 ? 8.084 37.367 14.900 1.00 14.90 ? 74 THR A CA 1 ATOM 568 C C . THR A 1 74 ? 9.082 36.211 14.955 1.00 13.71 ? 74 THR A C 1 ATOM 569 O O . THR A 1 74 ? 9.900 35.992 14.032 1.00 14.32 ? 74 THR A O 1 ATOM 570 C CB . THR A 1 74 ? 6.895 36.967 13.983 1.00 16.14 ? 74 THR A CB 1 ATOM 571 O OG1 . THR A 1 74 ? 6.023 38.082 13.896 1.00 19.73 ? 74 THR A OG1 1 ATOM 572 C CG2 . THR A 1 74 ? 6.098 35.776 14.495 1.00 14.82 ? 74 THR A CG2 1 ATOM 573 N N . VAL A 1 75 ? 8.954 35.446 16.007 1.00 12.05 ? 75 VAL A N 1 ATOM 574 C CA . VAL A 1 75 ? 9.778 34.308 16.282 1.00 14.31 ? 75 VAL A CA 1 ATOM 575 C C . VAL A 1 75 ? 8.797 33.212 16.748 1.00 14.71 ? 75 VAL A C 1 ATOM 576 O O . VAL A 1 75 ? 7.847 33.473 17.531 1.00 15.78 ? 75 VAL A O 1 ATOM 577 C CB . VAL A 1 75 ? 10.849 34.634 17.377 1.00 13.40 ? 75 VAL A CB 1 ATOM 578 C CG1 . VAL A 1 75 ? 11.511 33.403 17.863 1.00 15.33 ? 75 VAL A CG1 1 ATOM 579 C CG2 . VAL A 1 75 ? 11.983 35.464 16.752 1.00 16.65 ? 75 VAL A CG2 1 ATOM 580 N N . LEU A 1 76 ? 8.958 32.036 16.121 1.00 15.86 ? 76 LEU A N 1 ATOM 581 C CA . LEU A 1 76 ? 8.185 30.822 16.453 1.00 14.31 ? 76 LEU A CA 1 ATOM 582 C C . LEU A 1 76 ? 9.145 29.961 17.279 1.00 12.94 ? 76 LEU A C 1 ATOM 583 O O . LEU A 1 76 ? 10.299 29.777 16.927 1.00 14.63 ? 76 LEU A O 1 ATOM 584 C CB . LEU A 1 76 ? 7.754 30.064 15.193 1.00 13.35 ? 76 LEU A CB 1 ATOM 585 C CG . LEU A 1 76 ? 7.016 30.956 14.133 1.00 15.63 ? 76 LEU A CG 1 ATOM 586 C CD1 . LEU A 1 76 ? 6.687 30.124 12.881 1.00 14.41 ? 76 LEU A CD1 1 ATOM 587 C CD2 . LEU A 1 76 ? 5.745 31.687 14.749 1.00 11.63 ? 76 LEU A CD2 1 ATOM 588 N N . VAL A 1 77 ? 8.607 29.417 18.364 1.00 13.41 ? 77 VAL A N 1 ATOM 589 C CA . VAL A 1 77 ? 9.303 28.539 19.331 1.00 13.61 ? 77 VAL A CA 1 ATOM 590 C C . VAL A 1 77 ? 8.601 27.157 19.412 1.00 13.19 ? 77 VAL A C 1 ATOM 591 O O . VAL A 1 77 ? 7.374 27.011 19.609 1.00 11.78 ? 77 VAL A O 1 ATOM 592 C CB . VAL A 1 77 ? 9.396 29.232 20.780 1.00 12.60 ? 77 VAL A CB 1 ATOM 593 C CG1 . VAL A 1 77 ? 10.049 28.305 21.768 1.00 10.24 ? 77 VAL A CG1 1 ATOM 594 C CG2 . VAL A 1 77 ? 10.237 30.504 20.624 1.00 12.42 ? 77 VAL A CG2 1 ATOM 595 N N . GLY A 1 78 ? 9.398 26.140 19.170 1.00 13.83 ? 78 GLY A N 1 ATOM 596 C CA . GLY A 1 78 ? 8.842 24.825 19.221 1.00 13.86 ? 78 GLY A CA 1 ATOM 597 C C . GLY A 1 78 ? 9.878 23.750 19.100 1.00 14.25 ? 78 GLY A C 1 ATOM 598 O O . GLY A 1 78 ? 11.110 24.008 19.045 1.00 16.95 ? 78 GLY A O 1 ATOM 599 N N . PRO A 1 79 ? 9.392 22.533 18.867 1.00 14.59 ? 79 PRO A N 1 ATOM 600 C CA . PRO A 1 79 ? 10.291 21.401 18.747 1.00 17.06 ? 79 PRO A CA 1 ATOM 601 C C . PRO A 1 79 ? 11.083 21.271 17.445 1.00 21.79 ? 79 PRO A C 1 ATOM 602 O O . PRO A 1 79 ? 11.142 20.143 16.863 1.00 24.75 ? 79 PRO A O 1 ATOM 603 C CB . PRO A 1 79 ? 9.342 20.216 18.922 1.00 17.82 ? 79 PRO A CB 1 ATOM 604 C CG . PRO A 1 79 ? 7.966 20.732 18.383 1.00 17.43 ? 79 PRO A CG 1 ATOM 605 C CD . PRO A 1 79 ? 7.964 22.145 18.866 1.00 13.32 ? 79 PRO A CD 1 ATOM 606 N N . THR A 1 80 ? 11.696 22.362 16.957 1.00 21.78 ? 80 THR A N 1 ATOM 607 C CA . THR A 1 80 ? 12.442 22.293 15.723 1.00 19.48 ? 80 THR A CA 1 ATOM 608 C C . THR A 1 80 ? 13.761 21.614 15.980 1.00 21.40 ? 80 THR A C 1 ATOM 609 O O . THR A 1 80 ? 14.351 21.812 17.046 1.00 22.95 ? 80 THR A O 1 ATOM 610 C CB . THR A 1 80 ? 12.699 23.698 15.126 1.00 18.08 ? 80 THR A CB 1 ATOM 611 O OG1 . THR A 1 80 ? 13.514 23.541 13.967 1.00 16.15 ? 80 THR A OG1 1 ATOM 612 C CG2 . THR A 1 80 ? 13.442 24.548 16.119 1.00 12.99 ? 80 THR A CG2 1 ATOM 613 N N . PRO A 1 81 ? 14.297 20.861 14.981 1.00 22.91 ? 81 PRO A N 1 ATOM 614 C CA . PRO A 1 81 ? 15.589 20.148 15.084 1.00 23.43 ? 81 PRO A CA 1 ATOM 615 C C . PRO A 1 81 ? 16.814 21.103 15.106 1.00 23.82 ? 81 PRO A C 1 ATOM 616 O O . PRO A 1 81 ? 17.862 20.765 15.693 1.00 22.27 ? 81 PRO A O 1 ATOM 617 C CB . PRO A 1 81 ? 15.611 19.279 13.796 1.00 23.75 ? 81 PRO A CB 1 ATOM 618 C CG . PRO A 1 81 ? 14.728 20.094 12.823 1.00 25.40 ? 81 PRO A CG 1 ATOM 619 C CD . PRO A 1 81 ? 13.607 20.489 13.727 1.00 24.53 ? 81 PRO A CD 1 ATOM 620 N N . VAL A 1 82 ? 16.700 22.288 14.468 1.00 21.03 ? 82 VAL A N 1 ATOM 621 C CA . VAL A 1 82 ? 17.836 23.237 14.425 1.00 18.64 ? 82 VAL A CA 1 ATOM 622 C C . VAL A 1 82 ? 17.190 24.628 14.459 1.00 17.63 ? 82 VAL A C 1 ATOM 623 O O . VAL A 1 82 ? 15.995 24.750 14.154 1.00 15.19 ? 82 VAL A O 1 ATOM 624 C CB . VAL A 1 82 ? 18.698 22.992 13.098 1.00 21.28 ? 82 VAL A CB 1 ATOM 625 C CG1 . VAL A 1 82 ? 17.867 22.880 11.920 1.00 18.72 ? 82 VAL A CG1 1 ATOM 626 C CG2 . VAL A 1 82 ? 19.586 24.095 12.841 1.00 20.87 ? 82 VAL A CG2 1 ATOM 627 N N . ASN A 1 83 ? 17.913 25.598 15.027 1.00 15.63 ? 83 ASN A N 1 ATOM 628 C CA . ASN A 1 83 ? 17.455 26.967 15.062 1.00 13.90 ? 83 ASN A CA 1 ATOM 629 C C . ASN A 1 83 ? 17.475 27.473 13.590 1.00 13.18 ? 83 ASN A C 1 ATOM 630 O O . ASN A 1 83 ? 18.475 27.345 12.905 1.00 15.19 ? 83 ASN A O 1 ATOM 631 C CB . ASN A 1 83 ? 18.317 27.810 16.009 1.00 14.47 ? 83 ASN A CB 1 ATOM 632 C CG . ASN A 1 83 ? 18.122 27.408 17.453 1.00 17.27 ? 83 ASN A CG 1 ATOM 633 O OD1 . ASN A 1 83 ? 17.039 27.070 17.861 1.00 17.64 ? 83 ASN A OD1 1 ATOM 634 N ND2 . ASN A 1 83 ? 19.160 27.430 18.210 1.00 17.34 ? 83 ASN A ND2 1 ATOM 635 N N . ILE A 1 84 ? 16.397 28.088 13.122 1.00 11.56 ? 84 ILE A N 1 ATOM 636 C CA . ILE A 1 84 ? 16.362 28.532 11.745 1.00 10.35 ? 84 ILE A CA 1 ATOM 637 C C . ILE A 1 84 ? 15.973 30.031 11.713 1.00 9.19 ? 84 ILE A C 1 ATOM 638 O O . ILE A 1 84 ? 14.980 30.413 12.323 1.00 11.00 ? 84 ILE A O 1 ATOM 639 C CB . ILE A 1 84 ? 15.258 27.703 11.016 1.00 12.78 ? 84 ILE A CB 1 ATOM 640 C CG1 . ILE A 1 84 ? 15.738 26.263 10.800 1.00 10.67 ? 84 ILE A CG1 1 ATOM 641 C CG2 . ILE A 1 84 ? 14.746 28.409 9.706 1.00 13.28 ? 84 ILE A CG2 1 ATOM 642 C CD1 . ILE A 1 84 ? 14.667 25.412 10.489 1.00 15.18 ? 84 ILE A CD1 1 ATOM 643 N N . ILE A 1 85 ? 16.750 30.810 10.977 1.00 9.87 ? 85 ILE A N 1 ATOM 644 C CA . ILE A 1 85 ? 16.508 32.214 10.724 1.00 9.87 ? 85 ILE A CA 1 ATOM 645 C C . ILE A 1 85 ? 15.882 32.246 9.311 1.00 8.66 ? 85 ILE A C 1 ATOM 646 O O . ILE A 1 85 ? 16.520 31.928 8.348 1.00 9.58 ? 85 ILE A O 1 ATOM 647 C CB . ILE A 1 85 ? 17.855 33.063 10.826 1.00 8.98 ? 85 ILE A CB 1 ATOM 648 C CG1 . ILE A 1 85 ? 18.489 32.871 12.192 1.00 7.97 ? 85 ILE A CG1 1 ATOM 649 C CG2 . ILE A 1 85 ? 17.627 34.570 10.463 1.00 9.98 ? 85 ILE A CG2 1 ATOM 650 C CD1 . ILE A 1 85 ? 17.617 33.168 13.388 1.00 8.24 ? 85 ILE A CD1 1 ATOM 651 N N . GLY A 1 86 ? 14.622 32.629 9.225 1.00 6.95 ? 86 GLY A N 1 ATOM 652 C CA . GLY A 1 86 ? 13.937 32.679 7.955 1.00 9.13 ? 86 GLY A CA 1 ATOM 653 C C . GLY A 1 86 ? 13.868 34.074 7.370 1.00 10.08 ? 86 GLY A C 1 ATOM 654 O O . GLY A 1 86 ? 14.424 35.009 7.946 1.00 8.95 ? 86 GLY A O 1 ATOM 655 N N . ARG A 1 87 ? 13.204 34.186 6.225 1.00 9.88 ? 87 ARG A N 1 ATOM 656 C CA . ARG A 1 87 ? 13.122 35.411 5.461 1.00 9.88 ? 87 ARG A CA 1 ATOM 657 C C . ARG A 1 87 ? 12.583 36.601 6.219 1.00 12.20 ? 87 ARG A C 1 ATOM 658 O O . ARG A 1 87 ? 12.953 37.714 5.842 1.00 13.24 ? 87 ARG A O 1 ATOM 659 C CB . ARG A 1 87 ? 12.259 35.251 4.218 1.00 7.70 ? 87 ARG A CB 1 ATOM 660 C CG . ARG A 1 87 ? 12.895 34.281 3.195 1.00 11.37 ? 87 ARG A CG 1 ATOM 661 C CD . ARG A 1 87 ? 12.155 34.198 1.849 1.00 9.77 ? 87 ARG A CD 1 ATOM 662 N NE . ARG A 1 87 ? 10.761 33.901 2.044 1.00 11.15 ? 87 ARG A NE 1 ATOM 663 C CZ . ARG A 1 87 ? 9.755 34.797 2.079 1.00 12.74 ? 87 ARG A CZ 1 ATOM 664 N NH1 . ARG A 1 87 ? 9.933 36.108 1.920 1.00 11.98 ? 87 ARG A NH1 1 ATOM 665 N NH2 . ARG A 1 87 ? 8.537 34.344 2.291 1.00 10.66 ? 87 ARG A NH2 1 ATOM 666 N N . ASN A 1 88 ? 11.699 36.420 7.196 1.00 13.81 ? 88 ASN A N 1 ATOM 667 C CA . ASN A 1 88 ? 11.144 37.561 7.898 1.00 12.64 ? 88 ASN A CA 1 ATOM 668 C C . ASN A 1 88 ? 12.284 38.323 8.619 1.00 13.47 ? 88 ASN A C 1 ATOM 669 O O . ASN A 1 88 ? 12.191 39.537 8.785 1.00 17.02 ? 88 ASN A O 1 ATOM 670 C CB . ASN A 1 88 ? 10.018 37.120 8.845 1.00 12.99 ? 88 ASN A CB 1 ATOM 671 C CG . ASN A 1 88 ? 10.550 36.383 10.083 1.00 15.83 ? 88 ASN A CG 1 ATOM 672 O OD1 . ASN A 1 88 ? 11.260 35.394 9.958 1.00 15.57 ? 88 ASN A OD1 1 ATOM 673 N ND2 . ASN A 1 88 ? 10.267 36.928 11.294 1.00 16.97 ? 88 ASN A ND2 1 ATOM 674 N N . LEU A 1 89 ? 13.344 37.686 9.090 1.00 12.13 ? 89 LEU A N 1 ATOM 675 C CA . LEU A 1 89 ? 14.485 38.424 9.724 1.00 12.95 ? 89 LEU A CA 1 ATOM 676 C C . LEU A 1 89 ? 15.697 38.659 8.795 1.00 13.59 ? 89 LEU A C 1 ATOM 677 O O . LEU A 1 89 ? 16.416 39.620 8.935 1.00 12.62 ? 89 LEU A O 1 ATOM 678 C CB . LEU A 1 89 ? 14.955 37.723 10.988 1.00 13.80 ? 89 LEU A CB 1 ATOM 679 C CG . LEU A 1 89 ? 13.922 37.627 12.120 1.00 17.60 ? 89 LEU A CG 1 ATOM 680 C CD1 . LEU A 1 89 ? 14.549 36.995 13.434 1.00 16.69 ? 89 LEU A CD1 1 ATOM 681 C CD2 . LEU A 1 89 ? 13.412 39.029 12.443 1.00 15.87 ? 89 LEU A CD2 1 ATOM 682 N N . LEU A 1 90 ? 15.938 37.773 7.815 1.00 12.21 ? 90 LEU A N 1 ATOM 683 C CA . LEU A 1 90 ? 17.075 37.974 6.892 1.00 12.11 ? 90 LEU A CA 1 ATOM 684 C C . LEU A 1 90 ? 16.848 39.241 6.047 1.00 9.77 ? 90 LEU A C 1 ATOM 685 O O . LEU A 1 90 ? 17.786 39.833 5.593 1.00 12.97 ? 90 LEU A O 1 ATOM 686 C CB . LEU A 1 90 ? 17.262 36.738 5.912 1.00 10.93 ? 90 LEU A CB 1 ATOM 687 C CG . LEU A 1 90 ? 17.527 35.332 6.459 1.00 10.64 ? 90 LEU A CG 1 ATOM 688 C CD1 . LEU A 1 90 ? 17.298 34.263 5.368 1.00 9.33 ? 90 LEU A CD1 1 ATOM 689 C CD2 . LEU A 1 90 ? 18.940 35.365 6.982 1.00 13.17 ? 90 LEU A CD2 1 ATOM 690 N N . THR A 1 91 ? 15.623 39.563 5.708 1.00 10.26 ? 91 THR A N 1 ATOM 691 C CA . THR A 1 91 ? 15.410 40.784 4.956 1.00 12.71 ? 91 THR A CA 1 ATOM 692 C C . THR A 1 91 ? 15.845 42.001 5.797 1.00 14.23 ? 91 THR A C 1 ATOM 693 O O . THR A 1 91 ? 16.409 42.963 5.232 1.00 15.50 ? 91 THR A O 1 ATOM 694 C CB . THR A 1 91 ? 13.991 41.019 4.601 1.00 11.67 ? 91 THR A CB 1 ATOM 695 O OG1 . THR A 1 91 ? 13.184 41.043 5.791 1.00 13.40 ? 91 THR A OG1 1 ATOM 696 C CG2 . THR A 1 91 ? 13.522 40.017 3.553 1.00 11.30 ? 91 THR A CG2 1 ATOM 697 N N . GLN A 1 92 ? 15.587 41.993 7.108 1.00 12.75 ? 92 GLN A N 1 ATOM 698 C CA . GLN A 1 92 ? 15.955 43.110 7.979 1.00 11.49 ? 92 GLN A CA 1 ATOM 699 C C . GLN A 1 92 ? 17.460 43.314 8.114 1.00 12.31 ? 92 GLN A C 1 ATOM 700 O O . GLN A 1 92 ? 17.901 44.391 8.464 1.00 14.66 ? 92 GLN A O 1 ATOM 701 C CB . GLN A 1 92 ? 15.380 42.908 9.385 1.00 12.31 ? 92 GLN A CB 1 ATOM 702 C CG . GLN A 1 92 ? 13.882 42.751 9.387 1.00 10.97 ? 92 GLN A CG 1 ATOM 703 C CD . GLN A 1 92 ? 13.235 43.894 8.705 1.00 14.29 ? 92 GLN A CD 1 ATOM 704 O OE1 . GLN A 1 92 ? 12.820 43.838 7.515 1.00 16.70 ? 92 GLN A OE1 1 ATOM 705 N NE2 . GLN A 1 92 ? 13.142 44.978 9.443 1.00 10.57 ? 92 GLN A NE2 1 ATOM 706 N N . ILE A 1 93 ? 18.283 42.307 7.893 1.00 10.79 ? 93 ILE A N 1 ATOM 707 C CA . ILE A 1 93 ? 19.717 42.536 8.020 1.00 13.77 ? 93 ILE A CA 1 ATOM 708 C C . ILE A 1 93 ? 20.294 42.758 6.639 1.00 14.18 ? 93 ILE A C 1 ATOM 709 O O . ILE A 1 93 ? 21.496 42.786 6.450 1.00 15.19 ? 93 ILE A O 1 ATOM 710 C CB . ILE A 1 93 ? 20.460 41.371 8.857 1.00 15.14 ? 93 ILE A CB 1 ATOM 711 C CG1 . ILE A 1 93 ? 20.315 40.016 8.150 1.00 17.47 ? 93 ILE A CG1 1 ATOM 712 C CG2 . ILE A 1 93 ? 19.810 41.267 10.301 1.00 15.16 ? 93 ILE A CG2 1 ATOM 713 C CD1 . ILE A 1 93 ? 21.316 38.900 8.650 1.00 18.58 ? 93 ILE A CD1 1 ATOM 714 N N . GLY A 1 94 ? 19.431 42.826 5.640 1.00 12.55 ? 94 GLY A N 1 ATOM 715 C CA . GLY A 1 94 ? 19.957 43.094 4.332 1.00 15.64 ? 94 GLY A CA 1 ATOM 716 C C . GLY A 1 94 ? 20.590 41.902 3.610 1.00 18.31 ? 94 GLY A C 1 ATOM 717 O O . GLY A 1 94 ? 21.312 42.089 2.592 1.00 18.33 ? 94 GLY A O 1 ATOM 718 N N . CYS A 1 95 ? 20.234 40.685 4.004 1.00 16.15 ? 95 CYS A N 1 ATOM 719 C CA . CYS A 1 95 ? 20.851 39.521 3.349 1.00 16.34 ? 95 CYS A CA 1 ATOM 720 C C . CYS A 1 95 ? 20.258 39.217 1.944 1.00 14.91 ? 95 CYS A C 1 ATOM 721 O O . CYS A 1 95 ? 19.065 39.360 1.739 1.00 15.25 ? 95 CYS A O 1 ATOM 722 C CB . CYS A 1 95 ? 20.745 38.344 4.363 1.00 18.14 ? 95 CYS A CB 1 ATOM 723 S SG . CYS A 1 95 ? 21.185 36.731 3.708 1.00 23.07 ? 95 CYS A SG 1 ATOM 724 N N . THR A 1 96 ? 21.092 38.988 0.923 1.00 13.99 ? 96 THR A N 1 ATOM 725 C CA . THR A 1 96 ? 20.594 38.675 -0.403 1.00 14.04 ? 96 THR A CA 1 ATOM 726 C C . THR A 1 96 ? 21.350 37.366 -0.852 1.00 15.93 ? 96 THR A C 1 ATOM 727 O O . THR A 1 96 ? 22.410 37.026 -0.302 1.00 15.48 ? 96 THR A O 1 ATOM 728 C CB . THR A 1 96 ? 20.941 39.757 -1.436 1.00 13.13 ? 96 THR A CB 1 ATOM 729 O OG1 . THR A 1 96 ? 22.348 39.908 -1.468 1.00 14.66 ? 96 THR A OG1 1 ATOM 730 C CG2 . THR A 1 96 ? 20.354 41.041 -1.115 1.00 10.44 ? 96 THR A CG2 1 ATOM 731 N N . LEU A 1 97 ? 20.824 36.750 -1.911 1.00 15.18 ? 97 LEU A N 1 ATOM 732 C CA . LEU A 1 97 ? 21.345 35.553 -2.557 1.00 17.79 ? 97 LEU A CA 1 ATOM 733 C C . LEU A 1 97 ? 22.004 36.092 -3.807 1.00 17.78 ? 97 LEU A C 1 ATOM 734 O O . LEU A 1 97 ? 21.357 36.794 -4.567 1.00 18.81 ? 97 LEU A O 1 ATOM 735 C CB . LEU A 1 97 ? 20.162 34.679 -3.010 1.00 17.81 ? 97 LEU A CB 1 ATOM 736 C CG . LEU A 1 97 ? 19.968 33.259 -2.554 1.00 22.06 ? 97 LEU A CG 1 ATOM 737 C CD1 . LEU A 1 97 ? 20.616 33.004 -1.216 1.00 23.81 ? 97 LEU A CD1 1 ATOM 738 C CD2 . LEU A 1 97 ? 18.494 32.962 -2.519 1.00 18.61 ? 97 LEU A CD2 1 ATOM 739 N N . ASN A 1 98 ? 23.213 35.681 -4.111 1.00 16.79 ? 98 ASN A N 1 ATOM 740 C CA . ASN A 1 98 ? 23.881 36.230 -5.297 1.00 20.38 ? 98 ASN A CA 1 ATOM 741 C C . ASN A 1 98 ? 24.629 35.182 -6.170 1.00 22.36 ? 98 ASN A C 1 ATOM 742 O O . ASN A 1 98 ? 25.392 34.405 -5.617 1.00 23.48 ? 98 ASN A O 1 ATOM 743 C CB . ASN A 1 98 ? 24.943 37.265 -4.809 1.00 22.45 ? 98 ASN A CB 1 ATOM 744 C CG . ASN A 1 98 ? 24.307 38.469 -4.074 1.00 19.82 ? 98 ASN A CG 1 ATOM 745 O OD1 . ASN A 1 98 ? 24.165 38.460 -2.889 1.00 26.39 ? 98 ASN A OD1 1 ATOM 746 N ND2 . ASN A 1 98 ? 23.824 39.417 -4.820 1.00 23.80 ? 98 ASN A ND2 1 ATOM 747 N N . PHE A 1 99 ? 24.390 35.138 -7.479 1.00 21.23 ? 99 PHE A N 1 ATOM 748 C CA . PHE A 1 99 ? 25.114 34.224 -8.380 1.00 25.37 ? 99 PHE A CA 1 ATOM 749 C C . PHE A 1 99 ? 25.141 34.828 -9.814 1.00 27.31 ? 99 PHE A C 1 ATOM 750 O O . PHE A 1 99 ? 25.581 34.173 -10.798 1.00 27.14 ? 99 PHE A O 1 ATOM 751 C CB . PHE A 1 99 ? 24.497 32.826 -8.419 1.00 22.95 ? 99 PHE A CB 1 ATOM 752 C CG . PHE A 1 99 ? 23.074 32.790 -8.921 1.00 23.09 ? 99 PHE A CG 1 ATOM 753 C CD1 . PHE A 1 99 ? 22.024 33.147 -8.085 1.00 24.47 ? 99 PHE A CD1 1 ATOM 754 C CD2 . PHE A 1 99 ? 22.792 32.334 -10.190 1.00 22.55 ? 99 PHE A CD2 1 ATOM 755 C CE1 . PHE A 1 99 ? 20.725 33.048 -8.492 1.00 22.78 ? 99 PHE A CE1 1 ATOM 756 C CE2 . PHE A 1 99 ? 21.488 32.220 -10.629 1.00 26.03 ? 99 PHE A CE2 1 ATOM 757 C CZ . PHE A 1 99 ? 20.440 32.578 -9.775 1.00 26.38 ? 99 PHE A CZ 1 ATOM 758 O OXT . PHE A 1 99 ? 24.711 35.997 -9.928 1.00 28.84 ? 99 PHE A OXT 1 ATOM 759 N N . PRO B 1 1 ? 22.526 37.181 -10.983 1.00 32.82 ? 1 PRO B N 1 ATOM 760 C CA . PRO B 1 1 ? 21.632 38.189 -10.390 1.00 31.62 ? 1 PRO B CA 1 ATOM 761 C C . PRO B 1 1 ? 21.734 38.239 -8.869 1.00 30.31 ? 1 PRO B C 1 ATOM 762 O O . PRO B 1 1 ? 22.296 37.370 -8.240 1.00 31.40 ? 1 PRO B O 1 ATOM 763 C CB . PRO B 1 1 ? 20.226 37.734 -10.768 1.00 32.68 ? 1 PRO B CB 1 ATOM 764 C CG . PRO B 1 1 ? 20.367 36.255 -10.669 1.00 32.23 ? 1 PRO B CG 1 ATOM 765 C CD . PRO B 1 1 ? 21.704 36.040 -11.427 1.00 31.28 ? 1 PRO B CD 1 ATOM 766 N N . GLN B 1 2 ? 21.120 39.238 -8.281 1.00 27.94 ? 2 GLN B N 1 ATOM 767 C CA . GLN B 1 2 ? 21.106 39.373 -6.857 1.00 26.69 ? 2 GLN B CA 1 ATOM 768 C C . GLN B 1 2 ? 19.625 39.200 -6.539 1.00 25.94 ? 2 GLN B C 1 ATOM 769 O O . GLN B 1 2 ? 18.752 39.747 -7.203 1.00 26.37 ? 2 GLN B O 1 ATOM 770 C CB . GLN B 1 2 ? 21.586 40.744 -6.461 1.00 28.44 ? 2 GLN B CB 1 ATOM 771 C CG . GLN B 1 2 ? 21.309 40.998 -5.056 1.00 32.40 ? 2 GLN B CG 1 ATOM 772 C CD . GLN B 1 2 ? 22.004 42.204 -4.559 1.00 36.24 ? 2 GLN B CD 1 ATOM 773 O OE1 . GLN B 1 2 ? 23.175 42.127 -4.090 1.00 38.00 ? 2 GLN B OE1 1 ATOM 774 N NE2 . GLN B 1 2 ? 21.318 43.350 -4.651 1.00 35.37 ? 2 GLN B NE2 1 ATOM 775 N N . ILE B 1 3 ? 19.323 38.413 -5.531 1.00 22.77 ? 3 ILE B N 1 ATOM 776 C CA . ILE B 1 3 ? 17.928 38.142 -5.183 1.00 19.27 ? 3 ILE B CA 1 ATOM 777 C C . ILE B 1 3 ? 17.665 38.561 -3.726 1.00 17.31 ? 3 ILE B C 1 ATOM 778 O O . ILE B 1 3 ? 18.421 38.204 -2.801 1.00 14.91 ? 3 ILE B O 1 ATOM 779 C CB . ILE B 1 3 ? 17.661 36.605 -5.453 1.00 18.15 ? 3 ILE B CB 1 ATOM 780 C CG1 . ILE B 1 3 ? 17.936 36.342 -6.932 1.00 17.49 ? 3 ILE B CG1 1 ATOM 781 C CG2 . ILE B 1 3 ? 16.279 36.146 -4.919 1.00 16.10 ? 3 ILE B CG2 1 ATOM 782 C CD1 . ILE B 1 3 ? 17.761 34.986 -7.351 1.00 18.32 ? 3 ILE B CD1 1 ATOM 783 N N . THR B 1 4 ? 16.613 39.341 -3.525 1.00 13.23 ? 4 THR B N 1 ATOM 784 C CA . THR B 1 4 ? 16.332 39.785 -2.176 1.00 13.49 ? 4 THR B CA 1 ATOM 785 C C . THR B 1 4 ? 15.314 38.789 -1.604 1.00 12.90 ? 4 THR B C 1 ATOM 786 O O . THR B 1 4 ? 14.681 38.004 -2.320 1.00 15.15 ? 4 THR B O 1 ATOM 787 C CB . THR B 1 4 ? 15.737 41.303 -2.168 1.00 14.00 ? 4 THR B CB 1 ATOM 788 O OG1 . THR B 1 4 ? 14.585 41.329 -3.038 1.00 14.63 ? 4 THR B OG1 1 ATOM 789 C CG2 . THR B 1 4 ? 16.772 42.360 -2.630 1.00 13.60 ? 4 THR B CG2 1 ATOM 790 N N . LEU B 1 5 ? 15.029 38.935 -0.343 1.00 13.26 ? 5 LEU B N 1 ATOM 791 C CA . LEU B 1 5 ? 14.158 37.976 0.317 1.00 12.97 ? 5 LEU B CA 1 ATOM 792 C C . LEU B 1 5 ? 12.806 38.430 0.814 1.00 12.97 ? 5 LEU B C 1 ATOM 793 O O . LEU B 1 5 ? 12.179 37.743 1.613 1.00 13.09 ? 5 LEU B O 1 ATOM 794 C CB . LEU B 1 5 ? 14.942 37.254 1.447 1.00 10.53 ? 5 LEU B CB 1 ATOM 795 C CG . LEU B 1 5 ? 16.203 36.471 0.916 1.00 11.00 ? 5 LEU B CG 1 ATOM 796 C CD1 . LEU B 1 5 ? 17.088 36.076 2.116 1.00 11.17 ? 5 LEU B CD1 1 ATOM 797 C CD2 . LEU B 1 5 ? 15.847 35.240 0.002 1.00 6.50 ? 5 LEU B CD2 1 ATOM 798 N N . TRP B 1 6 ? 12.273 39.486 0.233 1.00 12.25 ? 6 TRP B N 1 ATOM 799 C CA . TRP B 1 6 ? 10.968 39.996 0.652 1.00 10.86 ? 6 TRP B CA 1 ATOM 800 C C . TRP B 1 6 ? 9.896 39.067 0.145 1.00 11.71 ? 6 TRP B C 1 ATOM 801 O O . TRP B 1 6 ? 8.835 38.977 0.724 1.00 11.11 ? 6 TRP B O 1 ATOM 802 C CB . TRP B 1 6 ? 10.755 41.430 0.076 1.00 13.35 ? 6 TRP B CB 1 ATOM 803 C CG . TRP B 1 6 ? 11.814 42.374 0.547 1.00 10.37 ? 6 TRP B CG 1 ATOM 804 C CD1 . TRP B 1 6 ? 12.948 42.769 -0.153 1.00 12.74 ? 6 TRP B CD1 1 ATOM 805 C CD2 . TRP B 1 6 ? 11.927 42.963 1.861 1.00 11.88 ? 6 TRP B CD2 1 ATOM 806 N NE1 . TRP B 1 6 ? 13.754 43.566 0.659 1.00 12.36 ? 6 TRP B NE1 1 ATOM 807 C CE2 . TRP B 1 6 ? 13.169 43.698 1.891 1.00 11.81 ? 6 TRP B CE2 1 ATOM 808 C CE3 . TRP B 1 6 ? 11.095 42.963 3.013 1.00 10.50 ? 6 TRP B CE3 1 ATOM 809 C CZ2 . TRP B 1 6 ? 13.598 44.417 3.023 1.00 8.80 ? 6 TRP B CZ2 1 ATOM 810 C CZ3 . TRP B 1 6 ? 11.519 43.677 4.144 1.00 8.85 ? 6 TRP B CZ3 1 ATOM 811 C CH2 . TRP B 1 6 ? 12.758 44.395 4.139 1.00 10.87 ? 6 TRP B CH2 1 ATOM 812 N N . GLN B 1 7 ? 10.211 38.333 -0.918 1.00 11.76 ? 7 GLN B N 1 ATOM 813 C CA . GLN B 1 7 ? 9.318 37.321 -1.562 1.00 14.53 ? 7 GLN B CA 1 ATOM 814 C C . GLN B 1 7 ? 10.067 35.926 -1.514 1.00 11.72 ? 7 GLN B C 1 ATOM 815 O O . GLN B 1 7 ? 11.284 35.913 -1.291 1.00 11.60 ? 7 GLN B O 1 ATOM 816 C CB . GLN B 1 7 ? 9.129 37.739 -3.036 1.00 19.52 ? 7 GLN B CB 1 ATOM 817 C CG . GLN B 1 7 ? 7.839 38.542 -3.507 1.00 34.63 ? 7 GLN B CG 1 ATOM 818 C CD . GLN B 1 7 ? 7.314 39.683 -2.553 1.00 44.60 ? 7 GLN B CD 1 ATOM 819 O OE1 . GLN B 1 7 ? 6.679 39.382 -1.485 1.00 49.19 ? 7 GLN B OE1 1 ATOM 820 N NE2 . GLN B 1 7 ? 7.496 41.013 -2.973 1.00 48.40 ? 7 GLN B NE2 1 ATOM 821 N N . ARG B 1 8 ? 9.421 34.775 -1.733 1.00 9.98 ? 8 ARG B N 1 ATOM 822 C CA . ARG B 1 8 ? 10.184 33.466 -1.716 1.00 10.93 ? 8 ARG B CA 1 ATOM 823 C C . ARG B 1 8 ? 11.085 33.488 -2.862 1.00 9.93 ? 8 ARG B C 1 ATOM 824 O O . ARG B 1 8 ? 10.649 33.930 -3.904 1.00 11.44 ? 8 ARG B O 1 ATOM 825 C CB . ARG B 1 8 ? 9.286 32.240 -1.946 1.00 10.39 ? 8 ARG B CB 1 ATOM 826 C CG . ARG B 1 8 ? 8.630 31.829 -0.703 1.00 13.89 ? 8 ARG B CG 1 ATOM 827 C CD . ARG B 1 8 ? 7.550 30.860 -0.969 1.00 18.24 ? 8 ARG B CD 1 ATOM 828 N NE . ARG B 1 8 ? 6.898 30.505 0.286 1.00 22.16 ? 8 ARG B NE 1 ATOM 829 C CZ . ARG B 1 8 ? 6.310 29.321 0.507 1.00 27.12 ? 8 ARG B CZ 1 ATOM 830 N NH1 . ARG B 1 8 ? 6.289 28.384 -0.454 1.00 26.95 ? 8 ARG B NH1 1 ATOM 831 N NH2 . ARG B 1 8 ? 5.759 29.037 1.692 1.00 25.93 ? 8 ARG B NH2 1 ATOM 832 N N . PRO B 1 9 ? 12.341 33.050 -2.709 1.00 7.93 ? 9 PRO B N 1 ATOM 833 C CA . PRO B 1 9 ? 13.326 33.008 -3.779 1.00 8.97 ? 9 PRO B CA 1 ATOM 834 C C . PRO B 1 9 ? 13.075 31.860 -4.825 1.00 10.49 ? 9 PRO B C 1 ATOM 835 O O . PRO B 1 9 ? 13.840 30.920 -4.889 1.00 9.92 ? 9 PRO B O 1 ATOM 836 C CB . PRO B 1 9 ? 14.658 32.853 -3.019 1.00 9.55 ? 9 PRO B CB 1 ATOM 837 C CG . PRO B 1 9 ? 14.299 32.031 -1.778 1.00 6.30 ? 9 PRO B CG 1 ATOM 838 C CD . PRO B 1 9 ? 12.923 32.594 -1.421 1.00 9.33 ? 9 PRO B CD 1 ATOM 839 N N . LEU B 1 10 ? 11.935 31.937 -5.541 1.00 12.54 ? 10 LEU B N 1 ATOM 840 C CA . LEU B 1 10 ? 11.490 30.979 -6.578 1.00 13.60 ? 10 LEU B CA 1 ATOM 841 C C . LEU B 1 10 ? 12.109 31.249 -7.933 1.00 14.56 ? 10 LEU B C 1 ATOM 842 O O . LEU B 1 10 ? 12.222 32.408 -8.328 1.00 15.97 ? 10 LEU B O 1 ATOM 843 C CB . LEU B 1 10 ? 9.979 30.982 -6.699 1.00 14.65 ? 10 LEU B CB 1 ATOM 844 C CG . LEU B 1 10 ? 9.312 30.390 -5.514 1.00 16.61 ? 10 LEU B CG 1 ATOM 845 C CD1 . LEU B 1 10 ? 7.930 30.849 -5.582 1.00 18.26 ? 10 LEU B CD1 1 ATOM 846 C CD2 . LEU B 1 10 ? 9.400 28.865 -5.572 1.00 21.23 ? 10 LEU B CD2 1 ATOM 847 N N . VAL B 1 11 ? 12.616 30.225 -8.600 1.00 12.72 ? 11 VAL B N 1 ATOM 848 C CA . VAL B 1 11 ? 13.257 30.397 -9.891 1.00 14.65 ? 11 VAL B CA 1 ATOM 849 C C . VAL B 1 11 ? 12.747 29.308 -10.753 1.00 15.67 ? 11 VAL B C 1 ATOM 850 O O . VAL B 1 11 ? 12.082 28.390 -10.271 1.00 14.40 ? 11 VAL B O 1 ATOM 851 C CB . VAL B 1 11 ? 14.746 30.215 -9.866 1.00 12.92 ? 11 VAL B CB 1 ATOM 852 C CG1 . VAL B 1 11 ? 15.349 31.276 -9.115 1.00 15.10 ? 11 VAL B CG1 1 ATOM 853 C CG2 . VAL B 1 11 ? 15.077 28.896 -9.305 1.00 14.91 ? 11 VAL B CG2 1 ATOM 854 N N . THR B 1 12 ? 12.936 29.486 -12.047 1.00 14.66 ? 12 THR B N 1 ATOM 855 C CA . THR B 1 12 ? 12.546 28.418 -12.967 1.00 16.82 ? 12 THR B CA 1 ATOM 856 C C . THR B 1 12 ? 13.778 27.544 -13.179 1.00 15.56 ? 12 THR B C 1 ATOM 857 O O . THR B 1 12 ? 14.915 28.038 -13.242 1.00 16.76 ? 12 THR B O 1 ATOM 858 C CB . THR B 1 12 ? 12.026 28.921 -14.355 1.00 17.90 ? 12 THR B CB 1 ATOM 859 O OG1 . THR B 1 12 ? 10.839 29.678 -14.122 1.00 23.37 ? 12 THR B OG1 1 ATOM 860 C CG2 . THR B 1 12 ? 11.610 27.762 -15.250 1.00 15.64 ? 12 THR B CG2 1 ATOM 861 N N . ILE B 1 13 ? 13.538 26.227 -13.199 1.00 16.31 ? 13 ILE B N 1 ATOM 862 C CA . ILE B 1 13 ? 14.609 25.234 -13.449 1.00 14.17 ? 13 ILE B CA 1 ATOM 863 C C . ILE B 1 13 ? 14.102 24.423 -14.648 1.00 14.62 ? 13 ILE B C 1 ATOM 864 O O . ILE B 1 13 ? 12.920 24.417 -14.925 1.00 15.53 ? 13 ILE B O 1 ATOM 865 C CB . ILE B 1 13 ? 14.807 24.260 -12.227 1.00 10.97 ? 13 ILE B CB 1 ATOM 866 C CG1 . ILE B 1 13 ? 13.463 23.530 -11.877 1.00 13.27 ? 13 ILE B CG1 1 ATOM 867 C CG2 . ILE B 1 13 ? 15.301 25.022 -11.019 1.00 7.61 ? 13 ILE B CG2 1 ATOM 868 C CD1 . ILE B 1 13 ? 13.624 22.224 -10.939 1.00 16.37 ? 13 ILE B CD1 1 ATOM 869 N N . LYS B 1 14 ? 15.007 23.832 -15.402 1.00 13.65 ? 14 LYS B N 1 ATOM 870 C CA . LYS B 1 14 ? 14.610 22.974 -16.518 1.00 16.68 ? 14 LYS B CA 1 ATOM 871 C C . LYS B 1 14 ? 15.195 21.609 -16.209 1.00 13.68 ? 14 LYS B C 1 ATOM 872 O O . LYS B 1 14 ? 16.422 21.463 -15.978 1.00 12.47 ? 14 LYS B O 1 ATOM 873 C CB . LYS B 1 14 ? 15.173 23.533 -17.850 1.00 14.88 ? 14 LYS B CB 1 ATOM 874 C CG . LYS B 1 14 ? 14.642 22.779 -19.128 1.00 21.20 ? 14 LYS B CG 1 ATOM 875 C CD . LYS B 1 14 ? 15.192 23.550 -20.322 1.00 21.11 ? 14 LYS B CD 1 ATOM 876 C CE . LYS B 1 14 ? 14.887 22.965 -21.651 1.00 26.63 ? 14 LYS B CE 1 ATOM 877 N NZ . LYS B 1 14 ? 15.758 23.733 -22.639 1.00 27.85 ? 14 LYS B NZ 1 ATOM 878 N N . ILE B 1 15 ? 14.330 20.627 -16.161 1.00 14.13 ? 15 ILE B N 1 ATOM 879 C CA . ILE B 1 15 ? 14.803 19.263 -15.863 1.00 17.98 ? 15 ILE B CA 1 ATOM 880 C C . ILE B 1 15 ? 13.986 18.331 -16.736 1.00 19.25 ? 15 ILE B C 1 ATOM 881 O O . ILE B 1 15 ? 12.750 18.401 -16.799 1.00 21.05 ? 15 ILE B O 1 ATOM 882 C CB . ILE B 1 15 ? 14.663 18.919 -14.314 1.00 16.21 ? 15 ILE B CB 1 ATOM 883 C CG1 . ILE B 1 15 ? 15.234 17.526 -14.016 1.00 19.58 ? 15 ILE B CG1 1 ATOM 884 C CG2 . ILE B 1 15 ? 13.236 19.091 -13.859 1.00 17.94 ? 15 ILE B CG2 1 ATOM 885 C CD1 . ILE B 1 15 ? 15.655 17.283 -12.565 1.00 17.40 ? 15 ILE B CD1 1 ATOM 886 N N . GLY B 1 16 ? 14.669 17.456 -17.426 1.00 23.02 ? 16 GLY B N 1 ATOM 887 C CA . GLY B 1 16 ? 13.965 16.556 -18.320 1.00 25.93 ? 16 GLY B CA 1 ATOM 888 C C . GLY B 1 16 ? 13.170 17.302 -19.407 1.00 27.13 ? 16 GLY B C 1 ATOM 889 O O . GLY B 1 16 ? 12.065 16.901 -19.682 1.00 29.34 ? 16 GLY B O 1 ATOM 890 N N . GLY B 1 17 ? 13.675 18.401 -19.979 1.00 26.98 ? 17 GLY B N 1 ATOM 891 C CA . GLY B 1 17 ? 12.930 19.100 -21.024 1.00 26.69 ? 17 GLY B CA 1 ATOM 892 C C . GLY B 1 17 ? 11.754 19.904 -20.496 1.00 28.23 ? 17 GLY B C 1 ATOM 893 O O . GLY B 1 17 ? 11.049 20.625 -21.231 1.00 28.51 ? 17 GLY B O 1 ATOM 894 N N . GLN B 1 18 ? 11.526 19.856 -19.210 1.00 27.08 ? 18 GLN B N 1 ATOM 895 C CA . GLN B 1 18 ? 10.421 20.644 -18.766 1.00 27.90 ? 18 GLN B CA 1 ATOM 896 C C . GLN B 1 18 ? 10.837 21.698 -17.763 1.00 25.02 ? 18 GLN B C 1 ATOM 897 O O . GLN B 1 18 ? 11.871 21.575 -17.072 1.00 22.75 ? 18 GLN B O 1 ATOM 898 C CB . GLN B 1 18 ? 9.369 19.735 -18.180 1.00 33.53 ? 18 GLN B CB 1 ATOM 899 C CG . GLN B 1 18 ? 9.973 18.950 -17.079 1.00 40.89 ? 18 GLN B CG 1 ATOM 900 C CD . GLN B 1 18 ? 9.428 17.558 -17.037 1.00 47.09 ? 18 GLN B CD 1 ATOM 901 O OE1 . GLN B 1 18 ? 10.209 16.570 -17.067 1.00 48.94 ? 18 GLN B OE1 1 ATOM 902 N NE2 . GLN B 1 18 ? 8.066 17.442 -16.959 1.00 47.98 ? 18 GLN B NE2 1 ATOM 903 N N . LEU B 1 19 ? 9.993 22.730 -17.691 1.00 21.95 ? 19 LEU B N 1 ATOM 904 C CA . LEU B 1 19 ? 10.215 23.847 -16.821 1.00 20.01 ? 19 LEU B CA 1 ATOM 905 C C . LEU B 1 19 ? 9.380 23.612 -15.566 1.00 18.51 ? 19 LEU B C 1 ATOM 906 O O . LEU B 1 19 ? 8.288 23.113 -15.617 1.00 17.80 ? 19 LEU B O 1 ATOM 907 C CB . LEU B 1 19 ? 9.786 25.123 -17.505 1.00 20.16 ? 19 LEU B CB 1 ATOM 908 C CG . LEU B 1 19 ? 10.523 25.530 -18.753 1.00 21.05 ? 19 LEU B CG 1 ATOM 909 C CD1 . LEU B 1 19 ? 9.957 26.874 -19.159 1.00 24.74 ? 19 LEU B CD1 1 ATOM 910 C CD2 . LEU B 1 19 ? 11.996 25.735 -18.434 1.00 21.54 ? 19 LEU B CD2 1 ATOM 911 N N . LYS B 1 20 ? 9.960 23.886 -14.421 1.00 18.91 ? 20 LYS B N 1 ATOM 912 C CA . LYS B 1 20 ? 9.307 23.748 -13.152 1.00 16.65 ? 20 LYS B CA 1 ATOM 913 C C . LYS B 1 20 ? 9.814 24.982 -12.347 1.00 18.66 ? 20 LYS B C 1 ATOM 914 O O . LYS B 1 20 ? 10.793 25.625 -12.725 1.00 17.16 ? 20 LYS B O 1 ATOM 915 C CB . LYS B 1 20 ? 9.809 22.456 -12.439 1.00 16.12 ? 20 LYS B CB 1 ATOM 916 C CG . LYS B 1 20 ? 9.281 21.233 -13.097 1.00 22.70 ? 20 LYS B CG 1 ATOM 917 C CD . LYS B 1 20 ? 9.724 20.018 -12.313 1.00 29.29 ? 20 LYS B CD 1 ATOM 918 C CE . LYS B 1 20 ? 9.311 18.762 -13.019 1.00 31.89 ? 20 LYS B CE 1 ATOM 919 N NZ . LYS B 1 20 ? 7.940 18.965 -13.624 1.00 37.21 ? 20 LYS B NZ 1 ATOM 920 N N . GLU B 1 21 ? 9.120 25.289 -11.252 1.00 17.41 ? 21 GLU B N 1 ATOM 921 C CA . GLU B 1 21 ? 9.538 26.329 -10.357 1.00 18.11 ? 21 GLU B CA 1 ATOM 922 C C . GLU B 1 21 ? 10.101 25.650 -9.116 1.00 13.83 ? 21 GLU B C 1 ATOM 923 O O . GLU B 1 21 ? 9.542 24.639 -8.653 1.00 13.01 ? 21 GLU B O 1 ATOM 924 C CB . GLU B 1 21 ? 8.334 27.146 -9.991 1.00 21.53 ? 21 GLU B CB 1 ATOM 925 C CG . GLU B 1 21 ? 8.724 28.323 -9.365 1.00 31.90 ? 21 GLU B CG 1 ATOM 926 C CD . GLU B 1 21 ? 7.545 29.260 -9.346 1.00 40.75 ? 21 GLU B CD 1 ATOM 927 O OE1 . GLU B 1 21 ? 6.473 28.806 -8.766 1.00 43.85 ? 21 GLU B OE1 1 ATOM 928 O OE2 . GLU B 1 21 ? 7.717 30.401 -9.914 1.00 41.51 ? 21 GLU B OE2 1 ATOM 929 N N . ALA B 1 22 ? 11.148 26.244 -8.546 1.00 11.75 ? 22 ALA B N 1 ATOM 930 C CA . ALA B 1 22 ? 11.813 25.714 -7.369 1.00 11.71 ? 22 ALA B CA 1 ATOM 931 C C . ALA B 1 22 ? 12.323 26.868 -6.462 1.00 13.15 ? 22 ALA B C 1 ATOM 932 O O . ALA B 1 22 ? 12.630 28.001 -6.942 1.00 14.01 ? 22 ALA B O 1 ATOM 933 C CB . ALA B 1 22 ? 12.975 24.820 -7.803 1.00 9.52 ? 22 ALA B CB 1 ATOM 934 N N . LEU B 1 23 ? 12.579 26.523 -5.210 1.00 10.35 ? 23 LEU B N 1 ATOM 935 C CA . LEU B 1 23 ? 12.986 27.442 -4.174 1.00 8.05 ? 23 LEU B CA 1 ATOM 936 C C . LEU B 1 23 ? 14.457 27.337 -3.946 1.00 10.60 ? 23 LEU B C 1 ATOM 937 O O . LEU B 1 23 ? 14.941 26.227 -3.801 1.00 10.49 ? 23 LEU B O 1 ATOM 938 C CB . LEU B 1 23 ? 12.222 27.002 -2.943 1.00 10.01 ? 23 LEU B CB 1 ATOM 939 C CG . LEU B 1 23 ? 12.278 27.843 -1.732 1.00 12.82 ? 23 LEU B CG 1 ATOM 940 C CD1 . LEU B 1 23 ? 11.598 29.114 -2.053 1.00 14.36 ? 23 LEU B CD1 1 ATOM 941 C CD2 . LEU B 1 23 ? 11.434 27.169 -0.757 1.00 15.83 ? 23 LEU B CD2 1 ATOM 942 N N . LEU B 1 24 ? 15.204 28.442 -3.929 1.00 8.86 ? 24 LEU B N 1 ATOM 943 C CA . LEU B 1 24 ? 16.652 28.385 -3.620 1.00 9.43 ? 24 LEU B CA 1 ATOM 944 C C . LEU B 1 24 ? 16.665 28.361 -2.065 1.00 8.38 ? 24 LEU B C 1 ATOM 945 O O . LEU B 1 24 ? 16.368 29.335 -1.422 1.00 10.39 ? 24 LEU B O 1 ATOM 946 C CB . LEU B 1 24 ? 17.372 29.616 -4.189 1.00 10.45 ? 24 LEU B CB 1 ATOM 947 C CG . LEU B 1 24 ? 17.104 29.805 -5.694 1.00 12.26 ? 24 LEU B CG 1 ATOM 948 C CD1 . LEU B 1 24 ? 17.708 31.182 -6.084 1.00 12.11 ? 24 LEU B CD1 1 ATOM 949 C CD2 . LEU B 1 24 ? 17.681 28.644 -6.558 1.00 12.54 ? 24 LEU B CD2 1 ATOM 950 N N . ASP B 1 25 ? 17.180 27.294 -1.507 1.00 7.61 ? 25 ASP B N 1 ATOM 951 C CA . ASP B 1 25 ? 17.102 27.050 -0.109 1.00 9.09 ? 25 ASP B CA 1 ATOM 952 C C . ASP B 1 25 ? 18.467 26.739 0.486 1.00 9.99 ? 25 ASP B C 1 ATOM 953 O O . ASP B 1 25 ? 18.967 25.618 0.438 1.00 9.49 ? 25 ASP B O 1 ATOM 954 C CB . ASP B 1 25 ? 16.091 25.887 0.052 1.00 10.07 ? 25 ASP B CB 1 ATOM 955 C CG . ASP B 1 25 ? 15.732 25.583 1.492 1.00 12.94 ? 25 ASP B CG 1 ATOM 956 O OD1 . ASP B 1 25 ? 16.450 25.968 2.442 1.00 15.32 ? 25 ASP B OD1 1 ATOM 957 O OD2 . ASP B 1 25 ? 14.695 24.980 1.640 1.00 13.68 ? 25 ASP B OD2 1 ATOM 958 N N . THR B 1 26 ? 19.017 27.740 1.154 1.00 9.69 ? 26 THR B N 1 ATOM 959 C CA . THR B 1 26 ? 20.321 27.611 1.754 1.00 9.28 ? 26 THR B CA 1 ATOM 960 C C . THR B 1 26 ? 20.217 26.723 3.039 1.00 10.34 ? 26 THR B C 1 ATOM 961 O O . THR B 1 26 ? 21.263 26.247 3.565 1.00 9.13 ? 26 THR B O 1 ATOM 962 C CB . THR B 1 26 ? 20.904 29.039 2.172 1.00 9.52 ? 26 THR B CB 1 ATOM 963 O OG1 . THR B 1 26 ? 20.037 29.626 3.139 1.00 8.97 ? 26 THR B OG1 1 ATOM 964 C CG2 . THR B 1 26 ? 21.126 30.021 0.946 1.00 10.71 ? 26 THR B CG2 1 ATOM 965 N N . GLY B 1 27 ? 18.991 26.484 3.551 1.00 10.30 ? 27 GLY B N 1 ATOM 966 C CA . GLY B 1 27 ? 18.916 25.638 4.748 1.00 9.98 ? 27 GLY B CA 1 ATOM 967 C C . GLY B 1 27 ? 18.918 24.108 4.416 1.00 12.35 ? 27 GLY B C 1 ATOM 968 O O . GLY B 1 27 ? 18.991 23.274 5.323 1.00 13.04 ? 27 GLY B O 1 ATOM 969 N N . ALA B 1 28 ? 18.706 23.774 3.148 1.00 9.58 ? 28 ALA B N 1 ATOM 970 C CA . ALA B 1 28 ? 18.623 22.393 2.663 1.00 9.43 ? 28 ALA B CA 1 ATOM 971 C C . ALA B 1 28 ? 19.933 21.909 2.189 1.00 9.75 ? 28 ALA B C 1 ATOM 972 O O . ALA B 1 28 ? 20.567 22.535 1.377 1.00 10.22 ? 28 ALA B O 1 ATOM 973 C CB . ALA B 1 28 ? 17.592 22.304 1.530 1.00 7.95 ? 28 ALA B CB 1 ATOM 974 N N . ASP B 1 29 ? 20.435 20.845 2.789 1.00 10.58 ? 29 ASP B N 1 ATOM 975 C CA . ASP B 1 29 ? 21.658 20.312 2.312 1.00 9.81 ? 29 ASP B CA 1 ATOM 976 C C . ASP B 1 29 ? 21.586 19.776 0.881 1.00 8.81 ? 29 ASP B C 1 ATOM 977 O O . ASP B 1 29 ? 22.533 19.874 0.120 1.00 9.57 ? 29 ASP B O 1 ATOM 978 C CB . ASP B 1 29 ? 22.038 19.149 3.193 1.00 11.79 ? 29 ASP B CB 1 ATOM 979 C CG . ASP B 1 29 ? 22.462 19.560 4.569 1.00 14.61 ? 29 ASP B CG 1 ATOM 980 O OD1 . ASP B 1 29 ? 22.837 20.693 4.867 1.00 11.71 ? 29 ASP B OD1 1 ATOM 981 O OD2 . ASP B 1 29 ? 22.451 18.632 5.363 1.00 18.59 ? 29 ASP B OD2 1 ATOM 982 N N . ASP B 1 30 ? 20.461 19.166 0.564 1.00 9.36 ? 30 ASP B N 1 ATOM 983 C CA . ASP B 1 30 ? 20.208 18.477 -0.689 1.00 9.89 ? 30 ASP B CA 1 ATOM 984 C C . ASP B 1 30 ? 19.057 19.113 -1.444 1.00 11.20 ? 30 ASP B C 1 ATOM 985 O O . ASP B 1 30 ? 18.212 19.876 -0.857 1.00 11.54 ? 30 ASP B O 1 ATOM 986 C CB . ASP B 1 30 ? 19.766 17.049 -0.357 1.00 14.88 ? 30 ASP B CB 1 ATOM 987 C CG . ASP B 1 30 ? 20.841 16.240 0.508 1.00 18.34 ? 30 ASP B CG 1 ATOM 988 O OD1 . ASP B 1 30 ? 22.011 16.130 0.087 1.00 19.77 ? 30 ASP B OD1 1 ATOM 989 O OD2 . ASP B 1 30 ? 20.477 15.724 1.574 1.00 19.48 ? 30 ASP B OD2 1 ATOM 990 N N . THR B 1 31 ? 18.949 18.678 -2.717 1.00 9.90 ? 31 THR B N 1 ATOM 991 C CA . THR B 1 31 ? 17.926 19.087 -3.656 1.00 8.68 ? 31 THR B CA 1 ATOM 992 C C . THR B 1 31 ? 16.821 18.015 -3.683 1.00 11.19 ? 31 THR B C 1 ATOM 993 O O . THR B 1 31 ? 17.075 16.839 -3.929 1.00 10.19 ? 31 THR B O 1 ATOM 994 C CB . THR B 1 31 ? 18.556 19.265 -5.028 1.00 8.66 ? 31 THR B CB 1 ATOM 995 O OG1 . THR B 1 31 ? 19.488 20.364 -4.991 1.00 10.63 ? 31 THR B OG1 1 ATOM 996 C CG2 . THR B 1 31 ? 17.512 19.424 -6.096 1.00 7.89 ? 31 THR B CG2 1 ATOM 997 N N . VAL B 1 32 ? 15.587 18.426 -3.411 1.00 11.73 ? 32 VAL B N 1 ATOM 998 C CA . VAL B 1 32 ? 14.459 17.509 -3.404 1.00 12.87 ? 32 VAL B CA 1 ATOM 999 C C . VAL B 1 32 ? 13.367 18.052 -4.281 1.00 13.55 ? 32 VAL B C 1 ATOM 1000 O O . VAL B 1 32 ? 12.858 19.163 -4.017 1.00 12.50 ? 32 VAL B O 1 ATOM 1001 C CB . VAL B 1 32 ? 13.799 17.342 -1.977 1.00 14.77 ? 32 VAL B CB 1 ATOM 1002 C CG1 . VAL B 1 32 ? 12.853 16.104 -2.003 1.00 13.81 ? 32 VAL B CG1 1 ATOM 1003 C CG2 . VAL B 1 32 ? 14.871 17.138 -0.956 1.00 16.81 ? 32 VAL B CG2 1 ATOM 1004 N N . LEU B 1 33 ? 12.935 17.239 -5.250 1.00 11.54 ? 33 LEU B N 1 ATOM 1005 C CA . LEU B 1 33 ? 11.884 17.616 -6.164 1.00 11.08 ? 33 LEU B CA 1 ATOM 1006 C C . LEU B 1 33 ? 10.628 16.780 -5.882 1.00 12.93 ? 33 LEU B C 1 ATOM 1007 O O . LEU B 1 33 ? 10.721 15.640 -5.364 1.00 11.93 ? 33 LEU B O 1 ATOM 1008 C CB . LEU B 1 33 ? 12.371 17.327 -7.592 1.00 9.98 ? 33 LEU B CB 1 ATOM 1009 C CG . LEU B 1 33 ? 13.633 18.132 -7.920 1.00 12.97 ? 33 LEU B CG 1 ATOM 1010 C CD1 . LEU B 1 33 ? 13.989 17.925 -9.348 1.00 14.72 ? 33 LEU B CD1 1 ATOM 1011 C CD2 . LEU B 1 33 ? 13.437 19.563 -7.736 1.00 10.90 ? 33 LEU B CD2 1 ATOM 1012 N N . GLU B 1 34 ? 9.470 17.305 -6.251 1.00 11.88 ? 34 GLU B N 1 ATOM 1013 C CA . GLU B 1 34 ? 8.221 16.560 -6.150 1.00 16.06 ? 34 GLU B CA 1 ATOM 1014 C C . GLU B 1 34 ? 8.286 15.362 -7.128 1.00 18.16 ? 34 GLU B C 1 ATOM 1015 O O . GLU B 1 34 ? 9.104 15.297 -8.071 1.00 16.92 ? 34 GLU B O 1 ATOM 1016 C CB . GLU B 1 34 ? 7.019 17.429 -6.491 1.00 15.94 ? 34 GLU B CB 1 ATOM 1017 C CG . GLU B 1 34 ? 6.922 18.637 -5.552 1.00 19.69 ? 34 GLU B CG 1 ATOM 1018 C CD . GLU B 1 34 ? 6.170 19.825 -6.178 1.00 21.01 ? 34 GLU B CD 1 ATOM 1019 O OE1 . GLU B 1 34 ? 5.468 19.610 -7.148 1.00 24.16 ? 34 GLU B OE1 1 ATOM 1020 O OE2 . GLU B 1 34 ? 6.272 21.006 -5.746 1.00 26.09 ? 34 GLU B OE2 1 ATOM 1021 N N . GLU B 1 35 ? 7.403 14.409 -6.896 1.00 19.58 ? 35 GLU B N 1 ATOM 1022 C CA . GLU B 1 35 ? 7.311 13.191 -7.661 1.00 21.09 ? 35 GLU B CA 1 ATOM 1023 C C . GLU B 1 35 ? 7.428 13.359 -9.136 1.00 22.00 ? 35 GLU B C 1 ATOM 1024 O O . GLU B 1 35 ? 6.795 14.234 -9.764 1.00 23.84 ? 35 GLU B O 1 ATOM 1025 C CB . GLU B 1 35 ? 6.023 12.509 -7.274 1.00 24.53 ? 35 GLU B CB 1 ATOM 1026 C CG . GLU B 1 35 ? 5.895 11.123 -7.782 1.00 31.24 ? 35 GLU B CG 1 ATOM 1027 C CD . GLU B 1 35 ? 7.114 10.287 -7.467 1.00 34.66 ? 35 GLU B CD 1 ATOM 1028 O OE1 . GLU B 1 35 ? 7.406 10.088 -6.254 1.00 34.01 ? 35 GLU B OE1 1 ATOM 1029 O OE2 . GLU B 1 35 ? 7.757 9.844 -8.473 1.00 37.00 ? 35 GLU B OE2 1 ATOM 1030 N N . MET B 1 36 ? 8.379 12.664 -9.705 1.00 21.43 ? 36 MET B N 1 ATOM 1031 C CA . MET B 1 36 ? 8.530 12.752 -11.135 1.00 24.05 ? 36 MET B CA 1 ATOM 1032 C C . MET B 1 36 ? 9.330 11.544 -11.583 1.00 24.13 ? 36 MET B C 1 ATOM 1033 O O . MET B 1 36 ? 9.865 10.782 -10.788 1.00 23.88 ? 36 MET B O 1 ATOM 1034 C CB . MET B 1 36 ? 9.246 14.033 -11.573 1.00 25.15 ? 36 MET B CB 1 ATOM 1035 C CG . MET B 1 36 ? 10.721 14.113 -11.115 1.00 25.37 ? 36 MET B CG 1 ATOM 1036 S SD . MET B 1 36 ? 11.553 15.584 -11.734 1.00 31.13 ? 36 MET B SD 1 ATOM 1037 C CE . MET B 1 36 ? 11.275 15.472 -13.556 1.00 31.68 ? 36 MET B CE 1 ATOM 1038 N N . SER B 1 37 ? 9.409 11.378 -12.891 1.00 27.93 ? 37 SER B N 1 ATOM 1039 C CA . SER B 1 37 ? 10.180 10.264 -13.408 1.00 29.64 ? 37 SER B CA 1 ATOM 1040 C C . SER B 1 37 ? 11.558 10.736 -13.936 1.00 27.18 ? 37 SER B C 1 ATOM 1041 O O . SER B 1 37 ? 11.700 11.728 -14.674 1.00 25.94 ? 37 SER B O 1 ATOM 1042 C CB . SER B 1 37 ? 9.394 9.608 -14.528 1.00 34.65 ? 37 SER B CB 1 ATOM 1043 O OG . SER B 1 37 ? 9.763 10.379 -15.707 1.00 40.26 ? 37 SER B OG 1 ATOM 1044 N N . LEU B 1 38 ? 12.579 10.058 -13.475 1.00 24.62 ? 38 LEU B N 1 ATOM 1045 C CA . LEU B 1 38 ? 13.896 10.376 -13.877 1.00 23.39 ? 38 LEU B CA 1 ATOM 1046 C C . LEU B 1 38 ? 14.540 9.093 -14.416 1.00 24.18 ? 38 LEU B C 1 ATOM 1047 O O . LEU B 1 38 ? 14.070 7.980 -14.161 1.00 22.87 ? 38 LEU B O 1 ATOM 1048 C CB . LEU B 1 38 ? 14.636 10.989 -12.703 1.00 22.74 ? 38 LEU B CB 1 ATOM 1049 C CG . LEU B 1 38 ? 14.336 12.473 -12.356 1.00 22.76 ? 38 LEU B CG 1 ATOM 1050 C CD1 . LEU B 1 38 ? 15.247 12.940 -11.210 1.00 19.79 ? 38 LEU B CD1 1 ATOM 1051 C CD2 . LEU B 1 38 ? 14.554 13.370 -13.578 1.00 19.55 ? 38 LEU B CD2 1 ATOM 1052 N N . PRO B 1 39 ? 15.609 9.235 -15.201 1.00 25.69 ? 39 PRO B N 1 ATOM 1053 C CA . PRO B 1 39 ? 16.195 8.025 -15.704 1.00 24.63 ? 39 PRO B CA 1 ATOM 1054 C C . PRO B 1 39 ? 17.254 7.429 -14.785 1.00 24.82 ? 39 PRO B C 1 ATOM 1055 O O . PRO B 1 39 ? 18.067 8.130 -14.060 1.00 26.58 ? 39 PRO B O 1 ATOM 1056 C CB . PRO B 1 39 ? 16.806 8.525 -17.020 1.00 25.63 ? 39 PRO B CB 1 ATOM 1057 C CG . PRO B 1 39 ? 17.468 9.772 -16.620 1.00 26.49 ? 39 PRO B CG 1 ATOM 1058 C CD . PRO B 1 39 ? 16.288 10.402 -15.808 1.00 24.39 ? 39 PRO B CD 1 ATOM 1059 N N . GLY B 1 40 ? 17.296 6.109 -14.924 1.00 22.22 ? 40 GLY B N 1 ATOM 1060 C CA . GLY B 1 40 ? 18.271 5.339 -14.202 1.00 21.38 ? 40 GLY B CA 1 ATOM 1061 C C . GLY B 1 40 ? 17.768 4.642 -12.978 1.00 17.72 ? 40 GLY B C 1 ATOM 1062 O O . GLY B 1 40 ? 16.577 4.471 -12.727 1.00 19.47 ? 40 GLY B O 1 ATOM 1063 N N . ARG B 1 41 ? 18.754 4.137 -12.253 1.00 18.82 ? 41 ARG B N 1 ATOM 1064 C CA . ARG B 1 41 ? 18.503 3.428 -11.027 1.00 17.39 ? 41 ARG B CA 1 ATOM 1065 C C . ARG B 1 41 ? 18.530 4.506 -9.934 1.00 19.37 ? 41 ARG B C 1 ATOM 1066 O O . ARG B 1 41 ? 19.223 5.538 -10.075 1.00 20.43 ? 41 ARG B O 1 ATOM 1067 C CB . ARG B 1 41 ? 19.661 2.450 -10.829 1.00 17.26 ? 41 ARG B CB 1 ATOM 1068 C CG . ARG B 1 41 ? 19.559 1.262 -11.770 1.00 20.80 ? 41 ARG B CG 1 ATOM 1069 C CD . ARG B 1 41 ? 20.546 0.173 -11.391 1.00 22.04 ? 41 ARG B CD 1 ATOM 1070 N NE . ARG B 1 41 ? 20.368 -0.420 -10.032 1.00 20.55 ? 41 ARG B NE 1 ATOM 1071 C CZ . ARG B 1 41 ? 19.458 -1.343 -9.693 1.00 19.05 ? 41 ARG B CZ 1 ATOM 1072 N NH1 . ARG B 1 41 ? 18.551 -1.844 -10.577 1.00 10.56 ? 41 ARG B NH1 1 ATOM 1073 N NH2 . ARG B 1 41 ? 19.556 -1.829 -8.452 1.00 18.43 ? 41 ARG B NH2 1 ATOM 1074 N N . TRP B 1 42 ? 17.872 4.233 -8.818 1.00 17.87 ? 42 TRP B N 1 ATOM 1075 C CA . TRP B 1 42 ? 17.853 5.110 -7.684 1.00 14.90 ? 42 TRP B CA 1 ATOM 1076 C C . TRP B 1 42 ? 18.207 4.264 -6.535 1.00 17.34 ? 42 TRP B C 1 ATOM 1077 O O . TRP B 1 42 ? 18.155 3.006 -6.597 1.00 15.52 ? 42 TRP B O 1 ATOM 1078 C CB . TRP B 1 42 ? 16.485 5.685 -7.475 1.00 13.11 ? 42 TRP B CB 1 ATOM 1079 C CG . TRP B 1 42 ? 15.357 4.709 -7.297 1.00 13.21 ? 42 TRP B CG 1 ATOM 1080 C CD1 . TRP B 1 42 ? 14.571 4.100 -8.299 1.00 10.53 ? 42 TRP B CD1 1 ATOM 1081 C CD2 . TRP B 1 42 ? 14.826 4.302 -6.075 1.00 10.68 ? 42 TRP B CD2 1 ATOM 1082 N NE1 . TRP B 1 42 ? 13.608 3.333 -7.719 1.00 11.14 ? 42 TRP B NE1 1 ATOM 1083 C CE2 . TRP B 1 42 ? 13.737 3.438 -6.352 1.00 9.85 ? 42 TRP B CE2 1 ATOM 1084 C CE3 . TRP B 1 42 ? 15.144 4.595 -4.774 1.00 11.47 ? 42 TRP B CE3 1 ATOM 1085 C CZ2 . TRP B 1 42 ? 12.968 2.867 -5.362 1.00 11.97 ? 42 TRP B CZ2 1 ATOM 1086 C CZ3 . TRP B 1 42 ? 14.345 4.007 -3.762 1.00 13.80 ? 42 TRP B CZ3 1 ATOM 1087 C CH2 . TRP B 1 42 ? 13.280 3.162 -4.067 1.00 11.98 ? 42 TRP B CH2 1 ATOM 1088 N N . LYS B 1 43 ? 18.655 4.963 -5.507 1.00 18.09 ? 43 LYS B N 1 ATOM 1089 C CA . LYS B 1 43 ? 19.092 4.415 -4.210 1.00 18.86 ? 43 LYS B CA 1 ATOM 1090 C C . LYS B 1 43 ? 18.178 5.043 -3.140 1.00 18.65 ? 43 LYS B C 1 ATOM 1091 O O . LYS B 1 43 ? 17.609 6.140 -3.355 1.00 17.24 ? 43 LYS B O 1 ATOM 1092 C CB . LYS B 1 43 ? 20.571 4.835 -3.938 1.00 21.90 ? 43 LYS B CB 1 ATOM 1093 C CG . LYS B 1 43 ? 21.594 3.996 -4.693 1.00 30.13 ? 43 LYS B CG 1 ATOM 1094 C CD . LYS B 1 43 ? 23.029 4.529 -4.494 1.00 37.57 ? 43 LYS B CD 1 ATOM 1095 C CE . LYS B 1 43 ? 23.222 5.918 -5.225 1.00 43.76 ? 43 LYS B CE 1 ATOM 1096 N NZ . LYS B 1 43 ? 24.686 6.562 -5.377 1.00 47.94 ? 43 LYS B NZ 1 ATOM 1097 N N . PRO B 1 44 ? 18.015 4.381 -1.985 1.00 17.02 ? 44 PRO B N 1 ATOM 1098 C CA . PRO B 1 44 ? 17.155 4.940 -0.943 1.00 16.14 ? 44 PRO B CA 1 ATOM 1099 C C . PRO B 1 44 ? 17.886 5.971 -0.035 1.00 17.17 ? 44 PRO B C 1 ATOM 1100 O O . PRO B 1 44 ? 19.111 5.926 0.120 1.00 15.98 ? 44 PRO B O 1 ATOM 1101 C CB . PRO B 1 44 ? 16.739 3.688 -0.182 1.00 15.90 ? 44 PRO B CB 1 ATOM 1102 C CG . PRO B 1 44 ? 17.997 2.907 -0.200 1.00 16.73 ? 44 PRO B CG 1 ATOM 1103 C CD . PRO B 1 44 ? 18.566 3.071 -1.578 1.00 16.72 ? 44 PRO B CD 1 ATOM 1104 N N . LYS B 1 45 ? 17.153 6.972 0.466 1.00 17.75 ? 45 LYS B N 1 ATOM 1105 C CA . LYS B 1 45 ? 17.729 7.983 1.312 1.00 18.07 ? 45 LYS B CA 1 ATOM 1106 C C . LYS B 1 45 ? 16.643 8.533 2.198 1.00 19.23 ? 45 LYS B C 1 ATOM 1107 O O . LYS B 1 45 ? 15.504 8.649 1.796 1.00 21.49 ? 45 LYS B O 1 ATOM 1108 C CB . LYS B 1 45 ? 18.336 9.112 0.477 1.00 19.49 ? 45 LYS B CB 1 ATOM 1109 C CG . LYS B 1 45 ? 18.781 10.167 1.369 1.00 21.39 ? 45 LYS B CG 1 ATOM 1110 C CD . LYS B 1 45 ? 19.965 10.796 0.842 1.00 26.55 ? 45 LYS B CD 1 ATOM 1111 C CE . LYS B 1 45 ? 20.659 11.721 1.847 1.00 26.71 ? 45 LYS B CE 1 ATOM 1112 N NZ . LYS B 1 45 ? 21.637 12.570 1.093 1.00 34.77 ? 45 LYS B NZ 1 ATOM 1113 N N . MET B 1 46 ? 17.015 8.894 3.406 1.00 19.41 ? 46 MET B N 1 ATOM 1114 C CA . MET B 1 46 ? 16.101 9.426 4.393 1.00 22.62 ? 46 MET B CA 1 ATOM 1115 C C . MET B 1 46 ? 16.591 10.802 4.720 1.00 22.42 ? 46 MET B C 1 ATOM 1116 O O . MET B 1 46 ? 17.810 11.018 4.870 1.00 21.72 ? 46 MET B O 1 ATOM 1117 C CB . MET B 1 46 ? 16.162 8.601 5.668 1.00 30.07 ? 46 MET B CB 1 ATOM 1118 C CG . MET B 1 46 ? 15.447 7.204 5.547 1.00 35.15 ? 46 MET B CG 1 ATOM 1119 S SD . MET B 1 46 ? 13.970 7.377 6.519 1.00 45.58 ? 46 MET B SD 1 ATOM 1120 C CE . MET B 1 46 ? 14.787 8.337 7.957 1.00 43.21 ? 46 MET B CE 1 ATOM 1121 N N . ILE B 1 47 ? 15.662 11.761 4.667 1.00 22.10 ? 47 ILE B N 1 ATOM 1122 C CA . ILE B 1 47 ? 16.013 13.133 4.962 1.00 21.70 ? 47 ILE B CA 1 ATOM 1123 C C . ILE B 1 47 ? 15.156 13.645 6.123 1.00 20.10 ? 47 ILE B C 1 ATOM 1124 O O . ILE B 1 47 ? 13.956 13.342 6.192 1.00 20.84 ? 47 ILE B O 1 ATOM 1125 C CB . ILE B 1 47 ? 15.898 14.094 3.709 1.00 22.11 ? 47 ILE B CB 1 ATOM 1126 C CG1 . ILE B 1 47 ? 14.458 14.256 3.298 1.00 23.21 ? 47 ILE B CG1 1 ATOM 1127 C CG2 . ILE B 1 47 ? 16.887 13.693 2.562 1.00 21.74 ? 47 ILE B CG2 1 ATOM 1128 C CD1 . ILE B 1 47 ? 14.361 14.932 2.034 1.00 28.24 ? 47 ILE B CD1 1 ATOM 1129 N N . GLY B 1 48 ? 15.806 14.394 7.019 1.00 19.64 ? 48 GLY B N 1 ATOM 1130 C CA . GLY B 1 48 ? 15.156 14.991 8.170 1.00 19.49 ? 48 GLY B CA 1 ATOM 1131 C C . GLY B 1 48 ? 14.650 16.383 7.821 1.00 18.95 ? 48 GLY B C 1 ATOM 1132 O O . GLY B 1 48 ? 15.411 17.181 7.257 1.00 19.71 ? 48 GLY B O 1 ATOM 1133 N N . GLY B 1 49 ? 13.363 16.633 8.028 1.00 19.86 ? 49 GLY B N 1 ATOM 1134 C CA . GLY B 1 49 ? 12.769 17.933 7.714 1.00 18.60 ? 49 GLY B CA 1 ATOM 1135 C C . GLY B 1 49 ? 12.347 18.513 9.021 1.00 20.99 ? 49 GLY B C 1 ATOM 1136 O O . GLY B 1 49 ? 12.674 17.993 10.101 1.00 21.13 ? 49 GLY B O 1 ATOM 1137 N N . ILE B 1 50 ? 11.527 19.537 8.963 1.00 22.49 ? 50 ILE B N 1 ATOM 1138 C CA . ILE B 1 50 ? 11.070 20.179 10.185 1.00 24.65 ? 50 ILE B CA 1 ATOM 1139 C C . ILE B 1 50 ? 10.028 19.272 10.930 1.00 26.81 ? 50 ILE B C 1 ATOM 1140 O O . ILE B 1 50 ? 9.989 19.198 12.179 1.00 26.24 ? 50 ILE B O 1 ATOM 1141 C CB . ILE B 1 50 ? 10.557 21.609 9.879 1.00 23.59 ? 50 ILE B CB 1 ATOM 1142 C CG1 . ILE B 1 50 ? 10.943 22.456 11.026 1.00 25.45 ? 50 ILE B CG1 1 ATOM 1143 C CG2 . ILE B 1 50 ? 9.096 21.668 9.446 1.00 25.92 ? 50 ILE B CG2 1 ATOM 1144 C CD1 . ILE B 1 50 ? 12.426 22.487 11.075 1.00 26.73 ? 50 ILE B CD1 1 ATOM 1145 N N . GLY B 1 51 ? 9.217 18.556 10.161 1.00 27.26 ? 51 GLY B N 1 ATOM 1146 C CA . GLY B 1 51 ? 8.231 17.705 10.797 1.00 30.38 ? 51 GLY B CA 1 ATOM 1147 C C . GLY B 1 51 ? 8.643 16.231 10.932 1.00 32.13 ? 51 GLY B C 1 ATOM 1148 O O . GLY B 1 51 ? 7.801 15.415 11.272 1.00 35.45 ? 51 GLY B O 1 ATOM 1149 N N . GLY B 1 52 ? 9.902 15.884 10.661 1.00 31.20 ? 52 GLY B N 1 ATOM 1150 C CA . GLY B 1 52 ? 10.368 14.504 10.749 1.00 30.48 ? 52 GLY B CA 1 ATOM 1151 C C . GLY B 1 52 ? 11.111 14.061 9.491 1.00 29.22 ? 52 GLY B C 1 ATOM 1152 O O . GLY B 1 52 ? 11.451 14.837 8.641 1.00 28.07 ? 52 GLY B O 1 ATOM 1153 N N . PHE B 1 53 ? 11.198 12.759 9.316 1.00 31.28 ? 53 PHE B N 1 ATOM 1154 C CA . PHE B 1 53 ? 11.909 12.128 8.205 1.00 31.80 ? 53 PHE B CA 1 ATOM 1155 C C . PHE B 1 53 ? 11.002 11.633 7.083 1.00 31.28 ? 53 PHE B C 1 ATOM 1156 O O . PHE B 1 53 ? 9.800 11.364 7.291 1.00 32.97 ? 53 PHE B O 1 ATOM 1157 C CB . PHE B 1 53 ? 12.772 10.987 8.747 1.00 31.76 ? 53 PHE B CB 1 ATOM 1158 C CG . PHE B 1 53 ? 13.852 11.450 9.644 1.00 32.21 ? 53 PHE B CG 1 ATOM 1159 C CD1 . PHE B 1 53 ? 13.554 11.933 10.902 1.00 34.97 ? 53 PHE B CD1 1 ATOM 1160 C CD2 . PHE B 1 53 ? 15.133 11.571 9.174 1.00 34.76 ? 53 PHE B CD2 1 ATOM 1161 C CE1 . PHE B 1 53 ? 14.500 12.556 11.670 1.00 35.55 ? 53 PHE B CE1 1 ATOM 1162 C CE2 . PHE B 1 53 ? 16.111 12.191 9.926 1.00 34.82 ? 53 PHE B CE2 1 ATOM 1163 C CZ . PHE B 1 53 ? 15.796 12.698 11.179 1.00 35.78 ? 53 PHE B CZ 1 ATOM 1164 N N . ILE B 1 54 ? 11.498 11.758 5.865 1.00 27.82 ? 54 ILE B N 1 ATOM 1165 C CA . ILE B 1 54 ? 10.791 11.254 4.726 1.00 24.72 ? 54 ILE B CA 1 ATOM 1166 C C . ILE B 1 54 ? 11.817 10.378 3.931 1.00 23.27 ? 54 ILE B C 1 ATOM 1167 O O . ILE B 1 54 ? 13.000 10.478 4.120 1.00 20.98 ? 54 ILE B O 1 ATOM 1168 C CB . ILE B 1 54 ? 10.033 12.380 3.910 1.00 27.98 ? 54 ILE B CB 1 ATOM 1169 C CG1 . ILE B 1 54 ? 10.978 13.450 3.280 1.00 24.81 ? 54 ILE B CG1 1 ATOM 1170 C CG2 . ILE B 1 54 ? 8.993 13.015 4.829 1.00 27.79 ? 54 ILE B CG2 1 ATOM 1171 C CD1 . ILE B 1 54 ? 10.673 13.823 1.839 1.00 23.54 ? 54 ILE B CD1 1 ATOM 1172 N N . LYS B 1 55 ? 11.331 9.353 3.275 1.00 23.17 ? 55 LYS B N 1 ATOM 1173 C CA . LYS B 1 55 ? 12.153 8.466 2.465 1.00 23.90 ? 55 LYS B CA 1 ATOM 1174 C C . LYS B 1 55 ? 11.989 9.014 1.051 1.00 21.21 ? 55 LYS B C 1 ATOM 1175 O O . LYS B 1 55 ? 10.851 9.356 0.646 1.00 22.90 ? 55 LYS B O 1 ATOM 1176 C CB . LYS B 1 55 ? 11.635 7.029 2.570 1.00 27.83 ? 55 LYS B CB 1 ATOM 1177 C CG . LYS B 1 55 ? 12.592 6.170 3.351 1.00 36.11 ? 55 LYS B CG 1 ATOM 1178 C CD . LYS B 1 55 ? 12.755 4.686 2.737 1.00 41.97 ? 55 LYS B CD 1 ATOM 1179 C CE . LYS B 1 55 ? 14.244 4.067 2.844 1.00 43.99 ? 55 LYS B CE 1 ATOM 1180 N NZ . LYS B 1 55 ? 14.396 2.505 2.604 1.00 41.89 ? 55 LYS B NZ 1 ATOM 1181 N N . VAL B 1 56 ? 13.085 9.139 0.311 1.00 16.15 ? 56 VAL B N 1 ATOM 1182 C CA . VAL B 1 56 ? 13.022 9.724 -1.035 1.00 16.88 ? 56 VAL B CA 1 ATOM 1183 C C . VAL B 1 56 ? 13.861 8.823 -1.906 1.00 16.00 ? 56 VAL B C 1 ATOM 1184 O O . VAL B 1 56 ? 14.530 7.951 -1.377 1.00 17.14 ? 56 VAL B O 1 ATOM 1185 C CB . VAL B 1 56 ? 13.641 11.168 -1.045 1.00 14.28 ? 56 VAL B CB 1 ATOM 1186 C CG1 . VAL B 1 56 ? 12.863 12.073 -0.112 1.00 13.47 ? 56 VAL B CG1 1 ATOM 1187 C CG2 . VAL B 1 56 ? 15.014 11.094 -0.500 1.00 12.81 ? 56 VAL B CG2 1 ATOM 1188 N N . ARG B 1 57 ? 13.837 9.009 -3.212 1.00 14.39 ? 57 ARG B N 1 ATOM 1189 C CA . ARG B 1 57 ? 14.648 8.209 -4.091 1.00 13.55 ? 57 ARG B CA 1 ATOM 1190 C C . ARG B 1 57 ? 15.818 9.080 -4.556 1.00 15.02 ? 57 ARG B C 1 ATOM 1191 O O . ARG B 1 57 ? 15.586 10.148 -5.023 1.00 17.31 ? 57 ARG B O 1 ATOM 1192 C CB . ARG B 1 57 ? 13.823 7.867 -5.290 1.00 13.88 ? 57 ARG B CB 1 ATOM 1193 C CG . ARG B 1 57 ? 12.495 7.271 -4.919 1.00 14.60 ? 57 ARG B CG 1 ATOM 1194 C CD . ARG B 1 57 ? 11.831 6.564 -6.140 1.00 14.51 ? 57 ARG B CD 1 ATOM 1195 N NE . ARG B 1 57 ? 11.633 7.365 -7.342 1.00 17.22 ? 57 ARG B NE 1 ATOM 1196 C CZ . ARG B 1 57 ? 10.565 8.142 -7.550 1.00 18.50 ? 57 ARG B CZ 1 ATOM 1197 N NH1 . ARG B 1 57 ? 9.626 8.231 -6.629 1.00 19.19 ? 57 ARG B NH1 1 ATOM 1198 N NH2 . ARG B 1 57 ? 10.412 8.781 -8.712 1.00 23.87 ? 57 ARG B NH2 1 ATOM 1199 N N . GLN B 1 58 ? 17.031 8.608 -4.554 1.00 10.89 ? 58 GLN B N 1 ATOM 1200 C CA . GLN B 1 58 ? 18.137 9.376 -4.956 1.00 10.75 ? 58 GLN B CA 1 ATOM 1201 C C . GLN B 1 58 ? 18.611 9.016 -6.310 1.00 12.79 ? 58 GLN B C 1 ATOM 1202 O O . GLN B 1 58 ? 18.782 7.848 -6.601 1.00 14.02 ? 58 GLN B O 1 ATOM 1203 C CB . GLN B 1 58 ? 19.258 9.134 -3.958 1.00 9.96 ? 58 GLN B CB 1 ATOM 1204 C CG . GLN B 1 58 ? 20.570 9.705 -4.433 1.00 14.28 ? 58 GLN B CG 1 ATOM 1205 C CD . GLN B 1 58 ? 21.670 9.574 -3.391 1.00 18.56 ? 58 GLN B CD 1 ATOM 1206 O OE1 . GLN B 1 58 ? 21.425 9.574 -2.211 1.00 21.27 ? 58 GLN B OE1 1 ATOM 1207 N NE2 . GLN B 1 58 ? 22.883 9.438 -3.841 1.00 20.20 ? 58 GLN B NE2 1 ATOM 1208 N N . TYR B 1 59 ? 18.697 9.975 -7.217 1.00 12.51 ? 59 TYR B N 1 ATOM 1209 C CA . TYR B 1 59 ? 19.261 9.744 -8.562 1.00 13.16 ? 59 TYR B CA 1 ATOM 1210 C C . TYR B 1 59 ? 20.523 10.567 -8.657 1.00 15.99 ? 59 TYR B C 1 ATOM 1211 O O . TYR B 1 59 ? 20.545 11.760 -8.313 1.00 16.80 ? 59 TYR B O 1 ATOM 1212 C CB . TYR B 1 59 ? 18.381 10.262 -9.691 1.00 11.90 ? 59 TYR B CB 1 ATOM 1213 C CG . TYR B 1 59 ? 17.041 9.578 -9.770 1.00 12.96 ? 59 TYR B CG 1 ATOM 1214 C CD1 . TYR B 1 59 ? 16.005 9.905 -8.862 1.00 14.83 ? 59 TYR B CD1 1 ATOM 1215 C CD2 . TYR B 1 59 ? 16.819 8.551 -10.697 1.00 12.71 ? 59 TYR B CD2 1 ATOM 1216 C CE1 . TYR B 1 59 ? 14.781 9.214 -8.889 1.00 16.54 ? 59 TYR B CE1 1 ATOM 1217 C CE2 . TYR B 1 59 ? 15.631 7.868 -10.725 1.00 14.05 ? 59 TYR B CE2 1 ATOM 1218 C CZ . TYR B 1 59 ? 14.622 8.188 -9.838 1.00 17.15 ? 59 TYR B CZ 1 ATOM 1219 O OH . TYR B 1 59 ? 13.455 7.482 -9.887 1.00 18.97 ? 59 TYR B OH 1 ATOM 1220 N N . ASP B 1 60 ? 21.553 9.990 -9.210 1.00 16.04 ? 60 ASP B N 1 ATOM 1221 C CA . ASP B 1 60 ? 22.800 10.705 -9.406 1.00 19.06 ? 60 ASP B CA 1 ATOM 1222 C C . ASP B 1 60 ? 23.070 11.254 -10.853 1.00 18.48 ? 60 ASP B C 1 ATOM 1223 O O . ASP B 1 60 ? 22.462 10.809 -11.850 1.00 16.89 ? 60 ASP B O 1 ATOM 1224 C CB . ASP B 1 60 ? 23.961 9.834 -8.922 1.00 22.74 ? 60 ASP B CB 1 ATOM 1225 C CG . ASP B 1 60 ? 23.753 9.346 -7.490 1.00 26.48 ? 60 ASP B CG 1 ATOM 1226 O OD1 . ASP B 1 60 ? 23.086 10.024 -6.698 1.00 28.87 ? 60 ASP B OD1 1 ATOM 1227 O OD2 . ASP B 1 60 ? 24.210 8.237 -7.178 1.00 31.42 ? 60 ASP B OD2 1 ATOM 1228 N N . GLN B 1 61 ? 23.972 12.228 -10.941 1.00 17.34 ? 61 GLN B N 1 ATOM 1229 C CA . GLN B 1 61 ? 24.332 12.851 -12.210 1.00 20.86 ? 61 GLN B CA 1 ATOM 1230 C C . GLN B 1 61 ? 23.185 13.273 -13.108 1.00 19.34 ? 61 GLN B C 1 ATOM 1231 O O . GLN B 1 61 ? 23.186 13.014 -14.317 1.00 20.31 ? 61 GLN B O 1 ATOM 1232 C CB . GLN B 1 61 ? 25.332 11.980 -12.978 1.00 26.35 ? 61 GLN B CB 1 ATOM 1233 C CG . GLN B 1 61 ? 26.741 12.597 -13.053 1.00 32.62 ? 61 GLN B CG 1 ATOM 1234 C CD . GLN B 1 61 ? 27.757 11.612 -13.619 1.00 40.41 ? 61 GLN B CD 1 ATOM 1235 O OE1 . GLN B 1 61 ? 28.202 10.695 -12.888 1.00 42.42 ? 61 GLN B OE1 1 ATOM 1236 N NE2 . GLN B 1 61 ? 28.105 11.757 -14.919 1.00 38.49 ? 61 GLN B NE2 1 ATOM 1237 N N . ILE B 1 62 ? 22.255 14.013 -12.537 1.00 18.00 ? 62 ILE B N 1 ATOM 1238 C CA . ILE B 1 62 ? 21.089 14.454 -13.304 1.00 16.92 ? 62 ILE B CA 1 ATOM 1239 C C . ILE B 1 62 ? 21.420 15.859 -13.724 1.00 17.88 ? 62 ILE B C 1 ATOM 1240 O O . ILE B 1 62 ? 22.015 16.640 -12.911 1.00 16.77 ? 62 ILE B O 1 ATOM 1241 C CB . ILE B 1 62 ? 19.821 14.460 -12.405 1.00 15.94 ? 62 ILE B CB 1 ATOM 1242 C CG1 . ILE B 1 62 ? 19.521 12.995 -11.937 1.00 18.24 ? 62 ILE B CG1 1 ATOM 1243 C CG2 . ILE B 1 62 ? 18.643 15.056 -13.164 1.00 15.89 ? 62 ILE B CG2 1 ATOM 1244 C CD1 . ILE B 1 62 ? 19.161 11.992 -13.064 1.00 14.42 ? 62 ILE B CD1 1 ATOM 1245 N N . LEU B 1 63 ? 21.148 16.169 -15.000 1.00 18.85 ? 63 LEU B N 1 ATOM 1246 C CA . LEU B 1 63 ? 21.359 17.547 -15.545 1.00 19.64 ? 63 LEU B CA 1 ATOM 1247 C C . LEU B 1 63 ? 20.093 18.411 -15.211 1.00 18.07 ? 63 LEU B C 1 ATOM 1248 O O . LEU B 1 63 ? 18.951 18.059 -15.533 1.00 16.92 ? 63 LEU B O 1 ATOM 1249 C CB . LEU B 1 63 ? 21.629 17.573 -17.084 1.00 23.21 ? 63 LEU B CB 1 ATOM 1250 C CG . LEU B 1 63 ? 21.717 18.990 -17.759 1.00 27.61 ? 63 LEU B CG 1 ATOM 1251 C CD1 . LEU B 1 63 ? 23.058 19.751 -17.522 1.00 29.81 ? 63 LEU B CD1 1 ATOM 1252 C CD2 . LEU B 1 63 ? 21.450 18.898 -19.234 1.00 30.67 ? 63 LEU B CD2 1 ATOM 1253 N N . ILE B 1 64 ? 20.327 19.553 -14.605 1.00 17.92 ? 64 ILE B N 1 ATOM 1254 C CA . ILE B 1 64 ? 19.274 20.472 -14.279 1.00 19.67 ? 64 ILE B CA 1 ATOM 1255 C C . ILE B 1 64 ? 19.819 21.878 -14.572 1.00 18.97 ? 64 ILE B C 1 ATOM 1256 O O . ILE B 1 64 ? 20.903 22.207 -14.209 1.00 20.95 ? 64 ILE B O 1 ATOM 1257 C CB . ILE B 1 64 ? 18.861 20.236 -12.810 1.00 22.87 ? 64 ILE B CB 1 ATOM 1258 C CG1 . ILE B 1 64 ? 17.876 21.287 -12.287 1.00 21.78 ? 64 ILE B CG1 1 ATOM 1259 C CG2 . ILE B 1 64 ? 20.101 20.082 -11.924 1.00 25.69 ? 64 ILE B CG2 1 ATOM 1260 C CD1 . ILE B 1 64 ? 17.178 20.752 -11.003 1.00 23.91 ? 64 ILE B CD1 1 ATOM 1261 N N . GLU B 1 65 ? 19.089 22.709 -15.265 1.00 17.33 ? 65 GLU B N 1 ATOM 1262 C CA . GLU B 1 65 ? 19.561 24.071 -15.534 1.00 20.31 ? 65 GLU B CA 1 ATOM 1263 C C . GLU B 1 65 ? 18.835 24.964 -14.548 1.00 20.64 ? 65 GLU B C 1 ATOM 1264 O O . GLU B 1 65 ? 17.642 24.918 -14.434 1.00 20.79 ? 65 GLU B O 1 ATOM 1265 C CB . GLU B 1 65 ? 19.177 24.401 -16.968 1.00 22.90 ? 65 GLU B CB 1 ATOM 1266 C CG . GLU B 1 65 ? 19.397 25.798 -17.380 1.00 32.55 ? 65 GLU B CG 1 ATOM 1267 C CD . GLU B 1 65 ? 18.793 26.034 -18.776 1.00 36.40 ? 65 GLU B CD 1 ATOM 1268 O OE1 . GLU B 1 65 ? 18.761 25.022 -19.567 1.00 39.49 ? 65 GLU B OE1 1 ATOM 1269 O OE2 . GLU B 1 65 ? 18.316 27.177 -19.031 1.00 38.72 ? 65 GLU B OE2 1 ATOM 1270 N N . ILE B 1 66 ? 19.523 25.851 -13.871 1.00 22.74 ? 66 ILE B N 1 ATOM 1271 C CA . ILE B 1 66 ? 18.849 26.654 -12.816 1.00 23.96 ? 66 ILE B CA 1 ATOM 1272 C C . ILE B 1 66 ? 19.094 28.089 -13.203 1.00 24.35 ? 66 ILE B C 1 ATOM 1273 O O . ILE B 1 66 ? 20.237 28.514 -13.178 1.00 22.52 ? 66 ILE B O 1 ATOM 1274 C CB . ILE B 1 66 ? 19.482 26.371 -11.385 1.00 21.49 ? 66 ILE B CB 1 ATOM 1275 C CG1 . ILE B 1 66 ? 19.376 24.868 -11.029 1.00 21.77 ? 66 ILE B CG1 1 ATOM 1276 C CG2 . ILE B 1 66 ? 18.697 27.139 -10.299 1.00 21.94 ? 66 ILE B CG2 1 ATOM 1277 C CD1 . ILE B 1 66 ? 20.429 24.393 -10.057 1.00 22.16 ? 66 ILE B CD1 1 ATOM 1278 N N . CYS B 1 67 ? 18.050 28.832 -13.546 1.00 28.53 ? 67 CYS B N 1 ATOM 1279 C CA . CYS B 1 67 ? 18.281 30.241 -14.016 1.00 34.79 ? 67 CYS B CA 1 ATOM 1280 C C . CYS B 1 67 ? 19.348 30.356 -15.125 1.00 34.66 ? 67 CYS B C 1 ATOM 1281 O O . CYS B 1 67 ? 20.238 31.229 -15.071 1.00 36.95 ? 67 CYS B O 1 ATOM 1282 C CB . CYS B 1 67 ? 18.744 31.155 -12.885 1.00 36.30 ? 67 CYS B CB 1 ATOM 1283 S SG . CYS B 1 67 ? 17.446 31.357 -11.798 1.00 45.65 ? 67 CYS B SG 1 ATOM 1284 N N . GLY B 1 68 ? 19.310 29.420 -16.067 1.00 34.85 ? 68 GLY B N 1 ATOM 1285 C CA . GLY B 1 68 ? 20.268 29.438 -17.138 1.00 32.63 ? 68 GLY B CA 1 ATOM 1286 C C . GLY B 1 68 ? 21.588 28.796 -16.806 1.00 32.01 ? 68 GLY B C 1 ATOM 1287 O O . GLY B 1 68 ? 22.452 28.763 -17.674 1.00 33.89 ? 68 GLY B O 1 ATOM 1288 N N . HIS B 1 69 ? 21.798 28.355 -15.564 1.00 30.09 ? 69 HIS B N 1 ATOM 1289 C CA . HIS B 1 69 ? 23.074 27.693 -15.208 1.00 28.69 ? 69 HIS B CA 1 ATOM 1290 C C . HIS B 1 69 ? 22.838 26.207 -15.225 1.00 26.35 ? 69 HIS B C 1 ATOM 1291 O O . HIS B 1 69 ? 21.899 25.734 -14.593 1.00 24.13 ? 69 HIS B O 1 ATOM 1292 C CB . HIS B 1 69 ? 23.526 28.061 -13.817 1.00 29.59 ? 69 HIS B CB 1 ATOM 1293 C CG . HIS B 1 69 ? 23.815 29.502 -13.666 1.00 37.26 ? 69 HIS B CG 1 ATOM 1294 N ND1 . HIS B 1 69 ? 22.841 30.476 -13.835 1.00 40.01 ? 69 HIS B ND1 1 ATOM 1295 C CD2 . HIS B 1 69 ? 24.992 30.160 -13.533 1.00 37.55 ? 69 HIS B CD2 1 ATOM 1296 C CE1 . HIS B 1 69 ? 23.409 31.669 -13.839 1.00 39.06 ? 69 HIS B CE1 1 ATOM 1297 N NE2 . HIS B 1 69 ? 24.711 31.501 -13.658 1.00 40.82 ? 69 HIS B NE2 1 ATOM 1298 N N . LYS B 1 70 ? 23.660 25.502 -15.993 1.00 25.67 ? 70 LYS B N 1 ATOM 1299 C CA . LYS B 1 70 ? 23.591 24.048 -16.101 1.00 26.28 ? 70 LYS B CA 1 ATOM 1300 C C . LYS B 1 70 ? 24.397 23.430 -14.975 1.00 23.12 ? 70 LYS B C 1 ATOM 1301 O O . LYS B 1 70 ? 25.486 23.882 -14.696 1.00 24.81 ? 70 LYS B O 1 ATOM 1302 C CB . LYS B 1 70 ? 24.101 23.548 -17.484 1.00 27.94 ? 70 LYS B CB 1 ATOM 1303 C CG . LYS B 1 70 ? 23.144 23.937 -18.643 1.00 34.53 ? 70 LYS B CG 1 ATOM 1304 C CD . LYS B 1 70 ? 23.395 23.136 -19.965 1.00 41.42 ? 70 LYS B CD 1 ATOM 1305 C CE . LYS B 1 70 ? 22.225 22.087 -20.281 1.00 46.45 ? 70 LYS B CE 1 ATOM 1306 N NZ . LYS B 1 70 ? 22.491 21.100 -21.458 1.00 48.20 ? 70 LYS B NZ 1 ATOM 1307 N N . ALA B 1 71 ? 23.757 22.582 -14.188 1.00 20.61 ? 71 ALA B N 1 ATOM 1308 C CA . ALA B 1 71 ? 24.393 21.858 -13.089 1.00 18.44 ? 71 ALA B CA 1 ATOM 1309 C C . ALA B 1 71 ? 24.129 20.369 -13.368 1.00 18.07 ? 71 ALA B C 1 ATOM 1310 O O . ALA B 1 71 ? 23.201 20.019 -14.147 1.00 17.07 ? 71 ALA B O 1 ATOM 1311 C CB . ALA B 1 71 ? 23.797 22.254 -11.707 1.00 17.68 ? 71 ALA B CB 1 ATOM 1312 N N . ILE B 1 72 ? 25.016 19.509 -12.840 1.00 16.74 ? 72 ILE B N 1 ATOM 1313 C CA . ILE B 1 72 ? 24.825 18.072 -12.971 1.00 16.96 ? 72 ILE B CA 1 ATOM 1314 C C . ILE B 1 72 ? 25.038 17.479 -11.637 1.00 15.51 ? 72 ILE B C 1 ATOM 1315 O O . ILE B 1 72 ? 26.149 17.533 -11.150 1.00 14.98 ? 72 ILE B O 1 ATOM 1316 C CB . ILE B 1 72 ? 25.794 17.357 -13.996 1.00 17.03 ? 72 ILE B CB 1 ATOM 1317 C CG1 . ILE B 1 72 ? 25.805 18.138 -15.372 1.00 15.61 ? 72 ILE B CG1 1 ATOM 1318 C CG2 . ILE B 1 72 ? 25.335 15.829 -14.074 1.00 8.98 ? 72 ILE B CG2 1 ATOM 1319 C CD1 . ILE B 1 72 ? 26.707 17.602 -16.415 1.00 15.20 ? 72 ILE B CD1 1 ATOM 1320 N N . GLY B 1 73 ? 24.033 16.883 -11.031 1.00 13.93 ? 73 GLY B N 1 ATOM 1321 C CA . GLY B 1 73 ? 24.339 16.344 -9.747 1.00 12.49 ? 73 GLY B CA 1 ATOM 1322 C C . GLY B 1 73 ? 23.242 15.490 -9.228 1.00 13.32 ? 73 GLY B C 1 ATOM 1323 O O . GLY B 1 73 ? 22.441 15.051 -10.018 1.00 12.30 ? 73 GLY B O 1 ATOM 1324 N N . THR B 1 74 ? 23.243 15.250 -7.909 1.00 12.94 ? 74 THR B N 1 ATOM 1325 C CA . THR B 1 74 ? 22.281 14.382 -7.212 1.00 13.66 ? 74 THR B CA 1 ATOM 1326 C C . THR B 1 74 ? 20.955 15.050 -6.932 1.00 13.98 ? 74 THR B C 1 ATOM 1327 O O . THR B 1 74 ? 20.916 16.218 -6.475 1.00 13.58 ? 74 THR B O 1 ATOM 1328 C CB . THR B 1 74 ? 22.901 13.881 -5.903 1.00 14.11 ? 74 THR B CB 1 ATOM 1329 O OG1 . THR B 1 74 ? 24.100 13.177 -6.242 1.00 16.68 ? 74 THR B OG1 1 ATOM 1330 C CG2 . THR B 1 74 ? 21.977 12.953 -5.179 1.00 10.99 ? 74 THR B CG2 1 ATOM 1331 N N . VAL B 1 75 ? 19.874 14.393 -7.298 1.00 9.90 ? 75 VAL B N 1 ATOM 1332 C CA . VAL B 1 75 ? 18.570 14.993 -7.068 1.00 11.39 ? 75 VAL B CA 1 ATOM 1333 C C . VAL B 1 75 ? 17.758 13.960 -6.340 1.00 11.86 ? 75 VAL B C 1 ATOM 1334 O O . VAL B 1 75 ? 17.889 12.749 -6.642 1.00 13.12 ? 75 VAL B O 1 ATOM 1335 C CB . VAL B 1 75 ? 17.900 15.321 -8.429 1.00 13.51 ? 75 VAL B CB 1 ATOM 1336 C CG1 . VAL B 1 75 ? 16.485 15.721 -8.170 1.00 16.96 ? 75 VAL B CG1 1 ATOM 1337 C CG2 . VAL B 1 75 ? 18.627 16.471 -9.172 1.00 14.13 ? 75 VAL B CG2 1 ATOM 1338 N N . LEU B 1 76 ? 17.006 14.363 -5.345 1.00 9.78 ? 76 LEU B N 1 ATOM 1339 C CA . LEU B 1 76 ? 16.145 13.436 -4.597 1.00 10.76 ? 76 LEU B CA 1 ATOM 1340 C C . LEU B 1 76 ? 14.704 13.771 -5.019 1.00 13.77 ? 76 LEU B C 1 ATOM 1341 O O . LEU B 1 76 ? 14.362 14.916 -5.354 1.00 13.46 ? 76 LEU B O 1 ATOM 1342 C CB . LEU B 1 76 ? 16.319 13.596 -3.071 1.00 7.95 ? 76 LEU B CB 1 ATOM 1343 C CG . LEU B 1 76 ? 17.760 13.766 -2.562 1.00 10.11 ? 76 LEU B CG 1 ATOM 1344 C CD1 . LEU B 1 76 ? 17.818 14.078 -1.061 1.00 6.73 ? 76 LEU B CD1 1 ATOM 1345 C CD2 . LEU B 1 76 ? 18.629 12.479 -2.957 1.00 10.92 ? 76 LEU B CD2 1 ATOM 1346 N N . VAL B 1 77 ? 13.888 12.745 -5.096 1.00 13.55 ? 77 VAL B N 1 ATOM 1347 C CA . VAL B 1 77 ? 12.481 12.856 -5.501 1.00 16.32 ? 77 VAL B CA 1 ATOM 1348 C C . VAL B 1 77 ? 11.685 12.237 -4.325 1.00 18.01 ? 77 VAL B C 1 ATOM 1349 O O . VAL B 1 77 ? 11.927 11.074 -3.871 1.00 17.42 ? 77 VAL B O 1 ATOM 1350 C CB . VAL B 1 77 ? 12.196 12.068 -6.847 1.00 16.37 ? 77 VAL B CB 1 ATOM 1351 C CG1 . VAL B 1 77 ? 10.762 12.244 -7.281 1.00 17.38 ? 77 VAL B CG1 1 ATOM 1352 C CG2 . VAL B 1 77 ? 13.184 12.529 -7.984 1.00 17.75 ? 77 VAL B CG2 1 ATOM 1353 N N . GLY B 1 78 ? 10.682 12.966 -3.894 1.00 17.88 ? 78 GLY B N 1 ATOM 1354 C CA . GLY B 1 78 ? 9.903 12.498 -2.783 1.00 18.22 ? 78 GLY B CA 1 ATOM 1355 C C . GLY B 1 78 ? 8.739 13.410 -2.512 1.00 19.28 ? 78 GLY B C 1 ATOM 1356 O O . GLY B 1 78 ? 8.495 14.411 -3.243 1.00 18.38 ? 78 GLY B O 1 ATOM 1357 N N . PRO B 1 79 ? 8.007 13.111 -1.430 1.00 20.49 ? 79 PRO B N 1 ATOM 1358 C CA . PRO B 1 79 ? 6.840 13.947 -1.117 1.00 20.48 ? 79 PRO B CA 1 ATOM 1359 C C . PRO B 1 79 ? 7.224 15.281 -0.451 1.00 20.24 ? 79 PRO B C 1 ATOM 1360 O O . PRO B 1 79 ? 7.051 15.498 0.701 1.00 22.55 ? 79 PRO B O 1 ATOM 1361 C CB . PRO B 1 79 ? 5.990 13.013 -0.239 1.00 19.76 ? 79 PRO B CB 1 ATOM 1362 C CG . PRO B 1 79 ? 7.186 12.300 0.674 1.00 19.97 ? 79 PRO B CG 1 ATOM 1363 C CD . PRO B 1 79 ? 8.207 12.003 -0.446 1.00 18.67 ? 79 PRO B CD 1 ATOM 1364 N N . THR B 1 80 ? 7.694 16.214 -1.228 1.00 20.47 ? 80 THR B N 1 ATOM 1365 C CA . THR B 1 80 ? 8.050 17.462 -0.678 1.00 17.80 ? 80 THR B CA 1 ATOM 1366 C C . THR B 1 80 ? 6.945 18.422 -1.080 1.00 19.37 ? 80 THR B C 1 ATOM 1367 O O . THR B 1 80 ? 6.358 18.299 -2.152 1.00 19.56 ? 80 THR B O 1 ATOM 1368 C CB . THR B 1 80 ? 9.438 17.876 -1.224 1.00 17.25 ? 80 THR B CB 1 ATOM 1369 O OG1 . THR B 1 80 ? 9.738 19.181 -0.764 1.00 18.82 ? 80 THR B OG1 1 ATOM 1370 C CG2 . THR B 1 80 ? 9.445 17.881 -2.733 1.00 14.33 ? 80 THR B CG2 1 ATOM 1371 N N . PRO B 1 81 ? 6.651 19.433 -0.228 1.00 19.84 ? 81 PRO B N 1 ATOM 1372 C CA . PRO B 1 81 ? 5.589 20.388 -0.562 1.00 19.09 ? 81 PRO B CA 1 ATOM 1373 C C . PRO B 1 81 ? 5.943 21.300 -1.745 1.00 19.59 ? 81 PRO B C 1 ATOM 1374 O O . PRO B 1 81 ? 5.066 21.856 -2.375 1.00 19.05 ? 81 PRO B O 1 ATOM 1375 C CB . PRO B 1 81 ? 5.458 21.223 0.713 1.00 17.20 ? 81 PRO B CB 1 ATOM 1376 C CG . PRO B 1 81 ? 6.031 20.456 1.751 1.00 17.89 ? 81 PRO B CG 1 ATOM 1377 C CD . PRO B 1 81 ? 7.172 19.713 1.123 1.00 19.36 ? 81 PRO B CD 1 ATOM 1378 N N . VAL B 1 82 ? 7.241 21.515 -1.976 1.00 18.25 ? 82 VAL B N 1 ATOM 1379 C CA . VAL B 1 82 ? 7.738 22.382 -3.040 1.00 15.58 ? 82 VAL B CA 1 ATOM 1380 C C . VAL B 1 82 ? 9.056 21.857 -3.581 1.00 14.58 ? 82 VAL B C 1 ATOM 1381 O O . VAL B 1 82 ? 9.812 21.223 -2.837 1.00 13.35 ? 82 VAL B O 1 ATOM 1382 C CB . VAL B 1 82 ? 8.058 23.862 -2.512 1.00 19.11 ? 82 VAL B CB 1 ATOM 1383 C CG1 . VAL B 1 82 ? 6.792 24.639 -2.296 1.00 23.83 ? 82 VAL B CG1 1 ATOM 1384 C CG2 . VAL B 1 82 ? 8.933 23.845 -1.245 1.00 18.23 ? 82 VAL B CG2 1 ATOM 1385 N N . ASN B 1 83 ? 9.369 22.196 -4.830 1.00 9.13 ? 83 ASN B N 1 ATOM 1386 C CA . ASN B 1 83 ? 10.630 21.811 -5.364 1.00 11.02 ? 83 ASN B CA 1 ATOM 1387 C C . ASN B 1 83 ? 11.669 22.650 -4.618 1.00 11.75 ? 83 ASN B C 1 ATOM 1388 O O . ASN B 1 83 ? 11.520 23.856 -4.491 1.00 12.16 ? 83 ASN B O 1 ATOM 1389 C CB . ASN B 1 83 ? 10.694 22.099 -6.844 1.00 9.30 ? 83 ASN B CB 1 ATOM 1390 C CG . ASN B 1 83 ? 9.816 21.194 -7.651 1.00 13.32 ? 83 ASN B CG 1 ATOM 1391 O OD1 . ASN B 1 83 ? 9.724 19.980 -7.394 1.00 11.40 ? 83 ASN B OD1 1 ATOM 1392 N ND2 . ASN B 1 83 ? 9.209 21.748 -8.669 1.00 12.49 ? 83 ASN B ND2 1 ATOM 1393 N N . ILE B 1 84 ? 12.749 22.031 -4.178 1.00 10.86 ? 84 ILE B N 1 ATOM 1394 C CA . ILE B 1 84 ? 13.791 22.690 -3.389 1.00 9.39 ? 84 ILE B CA 1 ATOM 1395 C C . ILE B 1 84 ? 15.163 22.466 -3.983 1.00 10.25 ? 84 ILE B C 1 ATOM 1396 O O . ILE B 1 84 ? 15.541 21.339 -4.197 1.00 7.39 ? 84 ILE B O 1 ATOM 1397 C CB . ILE B 1 84 ? 13.795 22.115 -1.914 1.00 9.58 ? 84 ILE B CB 1 ATOM 1398 C CG1 . ILE B 1 84 ? 12.616 22.683 -1.124 1.00 12.35 ? 84 ILE B CG1 1 ATOM 1399 C CG2 . ILE B 1 84 ? 15.017 22.563 -1.100 1.00 8.41 ? 84 ILE B CG2 1 ATOM 1400 C CD1 . ILE B 1 84 ? 12.259 21.714 0.065 1.00 17.33 ? 84 ILE B CD1 1 ATOM 1401 N N . ILE B 1 85 ? 15.892 23.549 -4.249 1.00 8.91 ? 85 ILE B N 1 ATOM 1402 C CA . ILE B 1 85 ? 17.259 23.506 -4.755 1.00 9.92 ? 85 ILE B CA 1 ATOM 1403 C C . ILE B 1 85 ? 18.099 23.697 -3.498 1.00 11.37 ? 85 ILE B C 1 ATOM 1404 O O . ILE B 1 85 ? 17.985 24.712 -2.829 1.00 11.88 ? 85 ILE B O 1 ATOM 1405 C CB . ILE B 1 85 ? 17.531 24.681 -5.731 1.00 10.14 ? 85 ILE B CB 1 ATOM 1406 C CG1 . ILE B 1 85 ? 16.615 24.567 -6.968 1.00 10.06 ? 85 ILE B CG1 1 ATOM 1407 C CG2 . ILE B 1 85 ? 18.932 24.571 -6.269 1.00 11.90 ? 85 ILE B CG2 1 ATOM 1408 C CD1 . ILE B 1 85 ? 16.838 23.182 -7.698 1.00 11.65 ? 85 ILE B CD1 1 ATOM 1409 N N . GLY B 1 86 ? 18.933 22.731 -3.173 1.00 11.39 ? 86 GLY B N 1 ATOM 1410 C CA . GLY B 1 86 ? 19.737 22.836 -1.972 1.00 10.74 ? 86 GLY B CA 1 ATOM 1411 C C . GLY B 1 86 ? 21.209 23.161 -2.199 1.00 8.87 ? 86 GLY B C 1 ATOM 1412 O O . GLY B 1 86 ? 21.699 23.338 -3.302 1.00 9.25 ? 86 GLY B O 1 ATOM 1413 N N . ARG B 1 87 ? 21.975 23.108 -1.125 1.00 10.26 ? 87 ARG B N 1 ATOM 1414 C CA . ARG B 1 87 ? 23.353 23.493 -1.240 1.00 9.72 ? 87 ARG B CA 1 ATOM 1415 C C . ARG B 1 87 ? 24.220 22.726 -2.201 1.00 10.78 ? 87 ARG B C 1 ATOM 1416 O O . ARG B 1 87 ? 25.192 23.253 -2.749 1.00 13.01 ? 87 ARG B O 1 ATOM 1417 C CB . ARG B 1 87 ? 23.967 23.479 0.105 1.00 8.69 ? 87 ARG B CB 1 ATOM 1418 C CG . ARG B 1 87 ? 23.323 24.466 1.098 1.00 5.33 ? 87 ARG B CG 1 ATOM 1419 C CD . ARG B 1 87 ? 24.276 24.635 2.357 1.00 9.28 ? 87 ARG B CD 1 ATOM 1420 N NE . ARG B 1 87 ? 24.341 23.398 3.129 1.00 11.10 ? 87 ARG B NE 1 ATOM 1421 C CZ . ARG B 1 87 ? 25.367 22.564 3.175 1.00 12.95 ? 87 ARG B CZ 1 ATOM 1422 N NH1 . ARG B 1 87 ? 26.481 22.824 2.526 1.00 10.26 ? 87 ARG B NH1 1 ATOM 1423 N NH2 . ARG B 1 87 ? 25.189 21.391 3.774 1.00 15.35 ? 87 ARG B NH2 1 ATOM 1424 N N . ASN B 1 88 ? 23.896 21.464 -2.417 1.00 10.91 ? 88 ASN B N 1 ATOM 1425 C CA . ASN B 1 88 ? 24.705 20.683 -3.314 1.00 10.26 ? 88 ASN B CA 1 ATOM 1426 C C . ASN B 1 88 ? 24.646 21.323 -4.718 1.00 11.85 ? 88 ASN B C 1 ATOM 1427 O O . ASN B 1 88 ? 25.650 21.239 -5.477 1.00 13.48 ? 88 ASN B O 1 ATOM 1428 C CB . ASN B 1 88 ? 24.222 19.213 -3.318 1.00 11.93 ? 88 ASN B CB 1 ATOM 1429 C CG . ASN B 1 88 ? 22.867 19.007 -4.031 1.00 11.46 ? 88 ASN B CG 1 ATOM 1430 O OD1 . ASN B 1 88 ? 21.853 19.632 -3.705 1.00 11.33 ? 88 ASN B OD1 1 ATOM 1431 N ND2 . ASN B 1 88 ? 22.885 18.146 -5.059 1.00 13.21 ? 88 ASN B ND2 1 ATOM 1432 N N . LEU B 1 89 ? 23.515 21.973 -5.083 1.00 10.64 ? 89 LEU B N 1 ATOM 1433 C CA . LEU B 1 89 ? 23.454 22.559 -6.428 1.00 11.83 ? 89 LEU B CA 1 ATOM 1434 C C . LEU B 1 89 ? 23.702 24.032 -6.355 1.00 11.99 ? 89 LEU B C 1 ATOM 1435 O O . LEU B 1 89 ? 24.281 24.567 -7.307 1.00 13.95 ? 89 LEU B O 1 ATOM 1436 C CB . LEU B 1 89 ? 22.187 22.224 -7.220 1.00 8.19 ? 89 LEU B CB 1 ATOM 1437 C CG . LEU B 1 89 ? 21.916 20.719 -7.465 1.00 10.30 ? 89 LEU B CG 1 ATOM 1438 C CD1 . LEU B 1 89 ? 20.652 20.636 -8.259 1.00 12.47 ? 89 LEU B CD1 1 ATOM 1439 C CD2 . LEU B 1 89 ? 23.072 20.067 -8.251 1.00 10.51 ? 89 LEU B CD2 1 ATOM 1440 N N . LEU B 1 90 ? 23.322 24.677 -5.255 1.00 11.54 ? 90 LEU B N 1 ATOM 1441 C CA . LEU B 1 90 ? 23.621 26.128 -5.116 1.00 11.89 ? 90 LEU B CA 1 ATOM 1442 C C . LEU B 1 90 ? 25.161 26.363 -5.214 1.00 13.52 ? 90 LEU B C 1 ATOM 1443 O O . LEU B 1 90 ? 25.587 27.315 -5.830 1.00 14.53 ? 90 LEU B O 1 ATOM 1444 C CB . LEU B 1 90 ? 23.028 26.717 -3.814 1.00 13.49 ? 90 LEU B CB 1 ATOM 1445 C CG . LEU B 1 90 ? 21.498 26.577 -3.624 1.00 13.28 ? 90 LEU B CG 1 ATOM 1446 C CD1 . LEU B 1 90 ? 21.069 27.045 -2.169 1.00 9.13 ? 90 LEU B CD1 1 ATOM 1447 C CD2 . LEU B 1 90 ? 20.867 27.384 -4.732 1.00 11.20 ? 90 LEU B CD2 1 ATOM 1448 N N . THR B 1 91 ? 25.996 25.470 -4.670 1.00 14.47 ? 91 THR B N 1 ATOM 1449 C CA . THR B 1 91 ? 27.427 25.625 -4.807 1.00 14.32 ? 91 THR B CA 1 ATOM 1450 C C . THR B 1 91 ? 27.910 25.473 -6.292 1.00 17.60 ? 91 THR B C 1 ATOM 1451 O O . THR B 1 91 ? 28.904 26.069 -6.677 1.00 13.77 ? 91 THR B O 1 ATOM 1452 C CB . THR B 1 91 ? 28.209 24.584 -3.987 1.00 15.35 ? 91 THR B CB 1 ATOM 1453 O OG1 . THR B 1 91 ? 27.769 23.303 -4.378 1.00 15.94 ? 91 THR B OG1 1 ATOM 1454 C CG2 . THR B 1 91 ? 28.015 24.771 -2.516 1.00 13.17 ? 91 THR B CG2 1 ATOM 1455 N N . GLN B 1 92 ? 27.213 24.669 -7.102 1.00 16.80 ? 92 GLN B N 1 ATOM 1456 C CA . GLN B 1 92 ? 27.632 24.466 -8.478 1.00 17.49 ? 92 GLN B CA 1 ATOM 1457 C C . GLN B 1 92 ? 27.316 25.731 -9.281 1.00 19.06 ? 92 GLN B C 1 ATOM 1458 O O . GLN B 1 92 ? 27.961 25.966 -10.286 1.00 19.99 ? 92 GLN B O 1 ATOM 1459 C CB . GLN B 1 92 ? 26.932 23.278 -9.140 1.00 15.91 ? 92 GLN B CB 1 ATOM 1460 C CG . GLN B 1 92 ? 27.362 21.947 -8.636 1.00 15.69 ? 92 GLN B CG 1 ATOM 1461 C CD . GLN B 1 92 ? 26.975 20.863 -9.582 1.00 15.61 ? 92 GLN B CD 1 ATOM 1462 O OE1 . GLN B 1 92 ? 26.621 21.113 -10.755 1.00 17.56 ? 92 GLN B OE1 1 ATOM 1463 N NE2 . GLN B 1 92 ? 27.052 19.648 -9.115 1.00 15.28 ? 92 GLN B NE2 1 ATOM 1464 N N . ILE B 1 93 ? 26.259 26.479 -8.935 1.00 18.87 ? 93 ILE B N 1 ATOM 1465 C CA . ILE B 1 93 ? 26.001 27.731 -9.671 1.00 16.35 ? 93 ILE B CA 1 ATOM 1466 C C . ILE B 1 93 ? 26.708 28.949 -9.079 1.00 16.40 ? 93 ILE B C 1 ATOM 1467 O O . ILE B 1 93 ? 26.546 30.043 -9.566 1.00 17.80 ? 93 ILE B O 1 ATOM 1468 C CB . ILE B 1 93 ? 24.542 27.992 -9.866 1.00 16.82 ? 93 ILE B CB 1 ATOM 1469 C CG1 . ILE B 1 93 ? 23.850 28.267 -8.523 1.00 16.97 ? 93 ILE B CG1 1 ATOM 1470 C CG2 . ILE B 1 93 ? 23.850 26.800 -10.678 1.00 14.57 ? 93 ILE B CG2 1 ATOM 1471 C CD1 . ILE B 1 93 ? 22.410 28.683 -8.781 1.00 18.07 ? 93 ILE B CD1 1 ATOM 1472 N N . GLY B 1 94 ? 27.534 28.748 -8.069 1.00 14.64 ? 94 GLY B N 1 ATOM 1473 C CA . GLY B 1 94 ? 28.260 29.858 -7.474 1.00 16.45 ? 94 GLY B CA 1 ATOM 1474 C C . GLY B 1 94 ? 27.465 30.786 -6.558 1.00 17.56 ? 94 GLY B C 1 ATOM 1475 O O . GLY B 1 94 ? 27.780 31.963 -6.339 1.00 16.04 ? 94 GLY B O 1 ATOM 1476 N N . CYS B 1 95 ? 26.438 30.234 -5.949 1.00 17.22 ? 95 CYS B N 1 ATOM 1477 C CA . CYS B 1 95 ? 25.590 31.064 -5.081 1.00 18.36 ? 95 CYS B CA 1 ATOM 1478 C C . CYS B 1 95 ? 26.153 31.332 -3.723 1.00 17.79 ? 95 CYS B C 1 ATOM 1479 O O . CYS B 1 95 ? 26.759 30.412 -3.110 1.00 19.80 ? 95 CYS B O 1 ATOM 1480 C CB . CYS B 1 95 ? 24.212 30.363 -4.960 1.00 21.16 ? 95 CYS B CB 1 ATOM 1481 S SG . CYS B 1 95 ? 22.881 31.316 -4.299 1.00 22.74 ? 95 CYS B SG 1 ATOM 1482 N N . THR B 1 96 ? 26.035 32.581 -3.243 1.00 15.03 ? 96 THR B N 1 ATOM 1483 C CA . THR B 1 96 ? 26.485 32.918 -1.885 1.00 16.30 ? 96 THR B CA 1 ATOM 1484 C C . THR B 1 96 ? 25.377 33.787 -1.262 1.00 16.14 ? 96 THR B C 1 ATOM 1485 O O . THR B 1 96 ? 24.487 34.322 -1.974 1.00 16.57 ? 96 THR B O 1 ATOM 1486 C CB . THR B 1 96 ? 27.779 33.841 -1.824 1.00 16.81 ? 96 THR B CB 1 ATOM 1487 O OG1 . THR B 1 96 ? 27.677 34.816 -2.859 1.00 18.40 ? 96 THR B OG1 1 ATOM 1488 C CG2 . THR B 1 96 ? 29.021 33.089 -1.993 1.00 20.74 ? 96 THR B CG2 1 ATOM 1489 N N . LEU B 1 97 ? 25.471 33.918 0.058 1.00 15.90 ? 97 LEU B N 1 ATOM 1490 C CA . LEU B 1 97 ? 24.602 34.774 0.866 1.00 17.17 ? 97 LEU B CA 1 ATOM 1491 C C . LEU B 1 97 ? 25.456 35.963 1.171 1.00 16.21 ? 97 LEU B C 1 ATOM 1492 O O . LEU B 1 97 ? 26.645 35.822 1.494 1.00 16.95 ? 97 LEU B O 1 ATOM 1493 C CB . LEU B 1 97 ? 24.195 34.120 2.198 1.00 17.53 ? 97 LEU B CB 1 ATOM 1494 C CG . LEU B 1 97 ? 23.048 33.121 2.144 1.00 17.58 ? 97 LEU B CG 1 ATOM 1495 C CD1 . LEU B 1 97 ? 23.042 32.298 3.384 1.00 15.27 ? 97 LEU B CD1 1 ATOM 1496 C CD2 . LEU B 1 97 ? 21.706 33.931 2.023 1.00 18.46 ? 97 LEU B CD2 1 ATOM 1497 N N . ASN B 1 98 ? 24.864 37.134 1.035 1.00 16.21 ? 98 ASN B N 1 ATOM 1498 C CA . ASN B 1 98 ? 25.594 38.368 1.285 1.00 20.32 ? 98 ASN B CA 1 ATOM 1499 C C . ASN B 1 98 ? 24.859 39.368 2.151 1.00 20.77 ? 98 ASN B C 1 ATOM 1500 O O . ASN B 1 98 ? 23.681 39.586 1.933 1.00 20.59 ? 98 ASN B O 1 ATOM 1501 C CB . ASN B 1 98 ? 25.873 39.038 -0.042 1.00 19.59 ? 98 ASN B CB 1 ATOM 1502 C CG . ASN B 1 98 ? 26.707 38.199 -0.897 1.00 23.56 ? 98 ASN B CG 1 ATOM 1503 O OD1 . ASN B 1 98 ? 27.918 38.214 -0.798 1.00 26.58 ? 98 ASN B OD1 1 ATOM 1504 N ND2 . ASN B 1 98 ? 26.081 37.395 -1.698 1.00 22.91 ? 98 ASN B ND2 1 ATOM 1505 N N . PHE B 1 99 ? 25.512 39.869 3.183 1.00 21.57 ? 99 PHE B N 1 ATOM 1506 C CA . PHE B 1 99 ? 24.902 40.931 3.974 1.00 24.93 ? 99 PHE B CA 1 ATOM 1507 C C . PHE B 1 99 ? 26.025 41.810 4.581 1.00 27.33 ? 99 PHE B C 1 ATOM 1508 O O . PHE B 1 99 ? 25.696 42.766 5.315 1.00 27.16 ? 99 PHE B O 1 ATOM 1509 C CB . PHE B 1 99 ? 23.893 40.463 5.036 1.00 23.88 ? 99 PHE B CB 1 ATOM 1510 C CG . PHE B 1 99 ? 24.465 39.534 6.071 1.00 25.77 ? 99 PHE B CG 1 ATOM 1511 C CD1 . PHE B 1 99 ? 24.454 38.170 5.861 1.00 21.11 ? 99 PHE B CD1 1 ATOM 1512 C CD2 . PHE B 1 99 ? 24.986 40.025 7.281 1.00 23.84 ? 99 PHE B CD2 1 ATOM 1513 C CE1 . PHE B 1 99 ? 24.945 37.333 6.822 1.00 20.04 ? 99 PHE B CE1 1 ATOM 1514 C CE2 . PHE B 1 99 ? 25.491 39.145 8.266 1.00 25.39 ? 99 PHE B CE2 1 ATOM 1515 C CZ . PHE B 1 99 ? 25.467 37.824 8.031 1.00 22.42 ? 99 PHE B CZ 1 ATOM 1516 O OXT . PHE B 1 99 ? 27.224 41.550 4.286 1.00 27.08 ? 99 PHE B OXT 1 HETATM 1517 N N01 . AH1 C 2 . ? 11.741 23.343 5.989 1.00 19.81 ? 500 AH1 A N01 1 HETATM 1518 C C02 . AH1 C 2 . ? 12.265 22.028 6.051 1.00 20.51 ? 500 AH1 A C02 1 HETATM 1519 N N03 . AH1 C 2 . ? 13.507 21.739 5.638 1.00 19.11 ? 500 AH1 A N03 1 HETATM 1520 C C04 . AH1 C 2 . ? 14.652 22.663 5.760 1.00 20.96 ? 500 AH1 A C04 1 HETATM 1521 C C05 . AH1 C 2 . ? 14.574 23.829 4.674 1.00 18.24 ? 500 AH1 A C05 1 HETATM 1522 C C06 . AH1 C 2 . ? 13.431 24.851 4.942 1.00 18.09 ? 500 AH1 A C06 1 HETATM 1523 C C07 . AH1 C 2 . ? 11.994 24.268 4.839 1.00 19.29 ? 500 AH1 A C07 1 HETATM 1524 C C08 . AH1 C 2 . ? 10.453 23.612 6.669 1.00 19.69 ? 500 AH1 A C08 1 HETATM 1525 C C09 . AH1 C 2 . ? 10.285 24.954 7.281 1.00 19.77 ? 500 AH1 A C09 1 HETATM 1526 C C10 . AH1 C 2 . ? 9.180 25.737 6.968 1.00 19.95 ? 500 AH1 A C10 1 HETATM 1527 C C11 . AH1 C 2 . ? 9.039 27.011 7.522 1.00 22.27 ? 500 AH1 A C11 1 HETATM 1528 C C12 . AH1 C 2 . ? 10.011 27.526 8.396 1.00 18.67 ? 500 AH1 A C12 1 HETATM 1529 C C13 . AH1 C 2 . ? 11.100 26.732 8.696 1.00 19.27 ? 500 AH1 A C13 1 HETATM 1530 C C14 . AH1 C 2 . ? 11.227 25.436 8.130 1.00 17.22 ? 500 AH1 A C14 1 HETATM 1531 O O15 . AH1 C 2 . ? 11.549 21.091 6.503 1.00 17.64 ? 500 AH1 A O15 1 HETATM 1532 C C16 . AH1 C 2 . ? 13.925 20.389 5.492 1.00 18.94 ? 500 AH1 A C16 1 HETATM 1533 C C17 . AH1 C 2 . ? 14.841 19.956 4.360 1.00 21.20 ? 500 AH1 A C17 1 HETATM 1534 C C18 . AH1 C 2 . ? 16.112 19.365 4.620 1.00 19.23 ? 500 AH1 A C18 1 HETATM 1535 C C19 . AH1 C 2 . ? 16.890 18.931 3.539 1.00 22.81 ? 500 AH1 A C19 1 HETATM 1536 C C20 . AH1 C 2 . ? 16.459 19.059 2.217 1.00 19.48 ? 500 AH1 A C20 1 HETATM 1537 C C21 . AH1 C 2 . ? 15.222 19.650 1.938 1.00 21.62 ? 500 AH1 A C21 1 HETATM 1538 C C22 . AH1 C 2 . ? 14.399 20.099 3.000 1.00 19.56 ? 500 AH1 A C22 1 HETATM 1539 C C23 . AH1 C 2 . ? 14.603 23.293 7.116 1.00 19.82 ? 500 AH1 A C23 1 HETATM 1540 O O24 . AH1 C 2 . ? 14.744 22.495 8.337 1.00 22.97 ? 500 AH1 A O24 1 HETATM 1541 C C25 . AH1 C 2 . ? 15.782 21.774 8.660 1.00 22.46 ? 500 AH1 A C25 1 HETATM 1542 C C26 . AH1 C 2 . ? 15.625 20.603 9.466 1.00 26.14 ? 500 AH1 A C26 1 HETATM 1543 C C27 . AH1 C 2 . ? 16.778 19.855 9.822 1.00 25.90 ? 500 AH1 A C27 1 HETATM 1544 C C28 . AH1 C 2 . ? 18.069 20.270 9.368 1.00 25.42 ? 500 AH1 A C28 1 HETATM 1545 C C29 . AH1 C 2 . ? 18.226 21.418 8.555 1.00 25.26 ? 500 AH1 A C29 1 HETATM 1546 C C30 . AH1 C 2 . ? 17.084 22.167 8.209 1.00 24.88 ? 500 AH1 A C30 1 HETATM 1547 O O31 . AH1 C 2 . ? 15.746 24.539 4.742 1.00 14.56 ? 500 AH1 A O31 1 HETATM 1548 O O32 . AH1 C 2 . ? 13.550 25.840 3.984 1.00 21.72 ? 500 AH1 A O32 1 HETATM 1549 C C33 . AH1 C 2 . ? 11.832 23.452 3.515 1.00 19.18 ? 500 AH1 A C33 1 HETATM 1550 O O34 . AH1 C 2 . ? 10.461 23.135 3.063 1.00 22.93 ? 500 AH1 A O34 1 HETATM 1551 C C35 . AH1 C 2 . ? 9.524 24.083 2.747 1.00 22.24 ? 500 AH1 A C35 1 HETATM 1552 C C36 . AH1 C 2 . ? 9.909 25.327 2.231 1.00 23.26 ? 500 AH1 A C36 1 HETATM 1553 C C37 . AH1 C 2 . ? 8.945 26.310 1.880 1.00 26.71 ? 500 AH1 A C37 1 HETATM 1554 C C38 . AH1 C 2 . ? 7.565 26.060 2.052 1.00 26.63 ? 500 AH1 A C38 1 HETATM 1555 C C39 . AH1 C 2 . ? 7.175 24.809 2.588 1.00 26.74 ? 500 AH1 A C39 1 HETATM 1556 C C40 . AH1 C 2 . ? 8.171 23.826 2.927 1.00 23.99 ? 500 AH1 A C40 1 HETATM 1557 O O . HOH D 3 . ? 23.380 42.130 -0.019 1.00 31.33 ? 306 HOH A O 1 HETATM 1558 O O . HOH D 3 . ? 27.569 32.212 -11.076 1.00 26.23 ? 311 HOH A O 1 HETATM 1559 O O . HOH D 3 . ? 27.862 21.597 7.009 1.00 27.73 ? 313 HOH A O 1 HETATM 1560 O O . HOH D 3 . ? 28.772 28.340 4.756 1.00 27.44 ? 314 HOH A O 1 HETATM 1561 O O . HOH D 3 . ? 31.049 27.488 3.323 1.00 21.35 ? 317 HOH A O 1 HETATM 1562 O O . HOH D 3 . ? 34.304 27.136 3.370 1.00 28.48 ? 318 HOH A O 1 HETATM 1563 O O . HOH D 3 . ? 3.329 15.880 11.933 1.00 58.70 ? 319 HOH A O 1 HETATM 1564 O O . HOH D 3 . ? 4.007 26.157 7.317 1.00 46.40 ? 320 HOH A O 1 HETATM 1565 O O . HOH D 3 . ? 4.265 19.239 17.145 1.00 28.69 ? 321 HOH A O 1 HETATM 1566 O O . HOH D 3 . ? 6.031 37.552 10.942 1.00 47.84 ? 326 HOH A O 1 HETATM 1567 O O . HOH D 3 . ? 6.539 40.878 14.994 1.00 24.11 ? 327 HOH A O 1 HETATM 1568 O O . HOH D 3 . ? 8.598 28.384 4.635 1.00 21.28 ? 330 HOH A O 1 HETATM 1569 O O . HOH D 3 . ? 8.775 35.982 5.623 1.00 23.39 ? 331 HOH A O 1 HETATM 1570 O O . HOH D 3 . ? 8.233 39.178 11.244 1.00 9.77 ? 332 HOH A O 1 HETATM 1571 O O . HOH D 3 . ? 8.997 33.823 12.330 1.00 21.92 ? 333 HOH A O 1 HETATM 1572 O O . HOH D 3 . ? 9.926 38.084 4.304 1.00 27.87 ? 334 HOH A O 1 HETATM 1573 O O . HOH D 3 . ? 10.423 40.461 5.481 1.00 18.44 ? 335 HOH A O 1 HETATM 1574 O O . HOH D 3 . ? 11.109 31.247 1.428 1.00 20.50 ? 338 HOH A O 1 HETATM 1575 O O . HOH D 3 . ? 12.347 41.261 22.385 1.00 42.15 ? 339 HOH A O 1 HETATM 1576 O O . HOH D 3 . ? 14.189 45.233 11.916 1.00 24.17 ? 343 HOH A O 1 HETATM 1577 O O . HOH D 3 . ? 15.692 39.561 22.720 1.00 29.10 ? 345 HOH A O 1 HETATM 1578 O O . HOH D 3 . ? 16.855 43.035 2.425 1.00 14.96 ? 349 HOH A O 1 HETATM 1579 O O . HOH D 3 . ? 16.652 45.910 11.354 1.00 23.22 ? 350 HOH A O 1 HETATM 1580 O O . HOH D 3 . ? 1.559 25.980 20.654 1.00 39.55 ? 352 HOH A O 1 HETATM 1581 O O . HOH D 3 . ? 1.931 36.064 19.195 1.00 31.43 ? 353 HOH A O 1 HETATM 1582 O O . HOH D 3 . ? 7.016 25.752 21.757 1.00 53.66 ? 354 HOH A O 1 HETATM 1583 O O . HOH D 3 . ? 8.707 21.822 22.151 1.00 47.33 ? 355 HOH A O 1 HETATM 1584 O O . HOH D 3 . ? 11.861 44.282 20.137 1.00 49.19 ? 358 HOH A O 1 HETATM 1585 O O . HOH D 3 . ? 13.121 22.234 21.537 1.00 22.32 ? 359 HOH A O 1 HETATM 1586 O O . HOH D 3 . ? 10.757 34.652 29.311 1.00 47.88 ? 364 HOH A O 1 HETATM 1587 O O . HOH D 3 . ? 16.366 28.172 21.203 1.00 42.40 ? 368 HOH A O 1 HETATM 1588 O O . HOH D 3 . ? 19.953 45.115 10.717 1.00 37.51 ? 374 HOH A O 1 HETATM 1589 O O . HOH D 3 . ? 19.910 46.703 6.955 1.00 34.26 ? 375 HOH A O 1 HETATM 1590 O O . HOH D 3 . ? 20.857 25.092 15.877 1.00 33.07 ? 378 HOH A O 1 HETATM 1591 O O . HOH D 3 . ? 22.799 26.762 19.694 1.00 36.82 ? 379 HOH A O 1 HETATM 1592 O O . HOH D 3 . ? 28.230 34.459 13.566 1.00 46.90 ? 382 HOH A O 1 HETATM 1593 O O . HOH D 3 . ? 1.661 17.674 15.277 1.00 37.55 ? 385 HOH A O 1 HETATM 1594 O O . HOH D 3 . ? 6.198 27.574 7.663 1.00 56.55 ? 386 HOH A O 1 HETATM 1595 O O . HOH D 3 . ? 5.435 38.468 21.785 1.00 45.15 ? 387 HOH A O 1 HETATM 1596 O O . HOH D 3 . ? 4.317 24.093 21.297 1.00 45.23 ? 388 HOH A O 1 HETATM 1597 O O . HOH D 3 . ? 6.686 17.460 17.890 1.00 37.74 ? 390 HOH A O 1 HETATM 1598 O O . HOH D 3 . ? 6.924 36.348 1.619 1.00 51.79 ? 391 HOH A O 1 HETATM 1599 O O . HOH D 3 . ? 6.806 35.178 10.038 1.00 44.50 ? 394 HOH A O 1 HETATM 1600 O O . HOH D 3 . ? 14.456 21.293 19.678 1.00 38.04 ? 398 HOH A O 1 HETATM 1601 O O . HOH D 3 . ? 18.607 40.153 21.577 1.00 48.96 ? 403 HOH A O 1 HETATM 1602 O O . HOH D 3 . ? 26.805 21.823 11.121 1.00 54.27 ? 409 HOH A O 1 HETATM 1603 O O . HOH D 3 . ? 24.736 32.756 26.277 1.00 50.01 ? 410 HOH A O 1 HETATM 1604 O O . HOH D 3 . ? 28.859 25.229 9.058 1.00 37.23 ? 413 HOH A O 1 HETATM 1605 O O . HOH D 3 . ? 29.137 29.054 7.347 1.00 62.02 ? 414 HOH A O 1 HETATM 1606 O O . HOH E 3 . ? 19.421 20.142 5.494 1.00 19.91 ? 301 HOH B O 1 HETATM 1607 O O . HOH E 3 . ? 20.597 1.286 -7.161 1.00 26.63 ? 302 HOH B O 1 HETATM 1608 O O . HOH E 3 . ? 20.447 16.323 -3.478 1.00 15.71 ? 303 HOH B O 1 HETATM 1609 O O . HOH E 3 . ? 21.403 6.642 -7.546 1.00 26.46 ? 304 HOH B O 1 HETATM 1610 O O . HOH E 3 . ? 22.164 24.014 4.918 1.00 20.53 ? 305 HOH B O 1 HETATM 1611 O O . HOH E 3 . ? 25.638 13.106 -8.574 1.00 20.58 ? 307 HOH B O 1 HETATM 1612 O O . HOH E 3 . ? 25.330 16.748 -6.060 1.00 13.62 ? 308 HOH B O 1 HETATM 1613 O O . HOH E 3 . ? 27.523 18.717 -6.313 1.00 31.81 ? 309 HOH B O 1 HETATM 1614 O O . HOH E 3 . ? 27.442 21.647 -0.718 1.00 42.64 ? 310 HOH B O 1 HETATM 1615 O O . HOH E 3 . ? 28.132 15.654 -11.853 1.00 26.81 ? 312 HOH B O 1 HETATM 1616 O O . HOH E 3 . ? 28.656 28.923 -2.445 1.00 24.55 ? 315 HOH B O 1 HETATM 1617 O O . HOH E 3 . ? 30.860 26.736 -9.873 1.00 41.62 ? 316 HOH B O 1 HETATM 1618 O O . HOH E 3 . ? 5.490 14.420 -4.991 1.00 33.19 ? 322 HOH B O 1 HETATM 1619 O O . HOH E 3 . ? 6.595 15.894 3.477 1.00 33.79 ? 323 HOH B O 1 HETATM 1620 O O . HOH E 3 . ? 6.622 23.636 -10.669 1.00 31.86 ? 324 HOH B O 1 HETATM 1621 O O . HOH E 3 . ? 6.414 34.883 -1.666 1.00 23.98 ? 325 HOH B O 1 HETATM 1622 O O . HOH E 3 . ? 8.046 24.357 -6.246 1.00 23.78 ? 328 HOH B O 1 HETATM 1623 O O . HOH E 3 . ? 8.361 34.593 -5.197 1.00 30.69 ? 329 HOH B O 1 HETATM 1624 O O . HOH E 3 . ? 11.494 20.446 -23.911 1.00 27.65 ? 336 HOH B O 1 HETATM 1625 O O . HOH E 3 . ? 11.346 5.579 -1.797 1.00 44.68 ? 337 HOH B O 1 HETATM 1626 O O . HOH E 3 . ? 12.989 36.502 -3.576 1.00 20.94 ? 340 HOH B O 1 HETATM 1627 O O . HOH E 3 . ? 13.401 12.931 -17.443 1.00 32.14 ? 341 HOH B O 1 HETATM 1628 O O . HOH E 3 . ? 14.404 5.454 0.123 1.00 32.07 ? 342 HOH B O 1 HETATM 1629 O O . HOH E 3 . ? 14.769 5.309 -14.300 1.00 39.44 ? 344 HOH B O 1 HETATM 1630 O O . HOH E 3 . ? 16.675 13.968 -16.616 1.00 38.74 ? 346 HOH B O 1 HETATM 1631 O O . HOH E 3 . ? 16.418 40.497 1.328 1.00 13.27 ? 347 HOH B O 1 HETATM 1632 O O . HOH E 3 . ? 16.162 45.502 0.274 1.00 20.81 ? 348 HOH B O 1 HETATM 1633 O O . HOH E 3 . ? 17.382 16.805 -17.211 1.00 25.09 ? 351 HOH B O 1 HETATM 1634 O O . HOH E 3 . ? 8.306 17.572 -9.856 1.00 36.80 ? 356 HOH B O 1 HETATM 1635 O O . HOH E 3 . ? 12.060 39.703 -2.961 1.00 20.93 ? 360 HOH B O 1 HETATM 1636 O O . HOH E 3 . ? 13.761 5.348 -11.988 1.00 41.28 ? 361 HOH B O 1 HETATM 1637 O O . HOH E 3 . ? 14.068 16.089 11.614 1.00 31.53 ? 362 HOH B O 1 HETATM 1638 O O . HOH E 3 . ? 14.200 31.938 -13.173 1.00 26.85 ? 363 HOH B O 1 HETATM 1639 O O . HOH E 3 . ? 16.278 19.328 -19.768 1.00 32.43 ? 366 HOH B O 1 HETATM 1640 O O . HOH E 3 . ? 16.572 27.392 -15.963 1.00 29.81 ? 367 HOH B O 1 HETATM 1641 O O . HOH E 3 . ? 18.121 17.705 6.841 1.00 32.37 ? 369 HOH B O 1 HETATM 1642 O O . HOH E 3 . ? 18.661 43.368 -5.691 1.00 44.21 ? 370 HOH B O 1 HETATM 1643 O O . HOH E 3 . ? 19.665 8.421 4.330 1.00 48.91 ? 371 HOH B O 1 HETATM 1644 O O . HOH E 3 . ? 19.668 13.978 -16.909 1.00 30.07 ? 372 HOH B O 1 HETATM 1645 O O . HOH E 3 . ? 19.375 41.202 -10.040 1.00 44.35 ? 373 HOH B O 1 HETATM 1646 O O . HOH E 3 . ? 20.631 7.551 -11.066 1.00 36.93 ? 376 HOH B O 1 HETATM 1647 O O . HOH E 3 . ? 20.965 14.357 8.347 1.00 56.43 ? 377 HOH B O 1 HETATM 1648 O O . HOH E 3 . ? 23.479 44.378 5.084 1.00 41.00 ? 380 HOH B O 1 HETATM 1649 O O . HOH E 3 . ? 25.271 19.517 0.389 1.00 24.98 ? 381 HOH B O 1 HETATM 1650 O O . HOH E 3 . ? 28.285 34.615 -5.589 1.00 34.63 ? 383 HOH B O 1 HETATM 1651 O O . HOH E 3 . ? 28.743 20.931 -2.997 1.00 42.50 ? 384 HOH B O 1 HETATM 1652 O O . HOH E 3 . ? 6.632 10.676 -4.185 1.00 40.15 ? 389 HOH B O 1 HETATM 1653 O O . HOH E 3 . ? 7.058 9.291 -10.816 1.00 41.74 ? 392 HOH B O 1 HETATM 1654 O O . HOH E 3 . ? 7.034 20.407 -10.295 1.00 39.51 ? 393 HOH B O 1 HETATM 1655 O O . HOH E 3 . ? 5.698 25.142 -20.664 1.00 57.69 ? 395 HOH B O 1 HETATM 1656 O O . HOH E 3 . ? 8.326 8.957 3.426 1.00 35.13 ? 396 HOH B O 1 HETATM 1657 O O . HOH E 3 . ? 9.377 8.006 5.762 1.00 41.25 ? 397 HOH B O 1 HETATM 1658 O O . HOH E 3 . ? 16.512 27.243 -21.358 1.00 42.10 ? 399 HOH B O 1 HETATM 1659 O O . HOH E 3 . ? 18.174 20.539 -18.206 1.00 33.69 ? 400 HOH B O 1 HETATM 1660 O O . HOH E 3 . ? 18.822 17.023 9.514 1.00 54.02 ? 401 HOH B O 1 HETATM 1661 O O . HOH E 3 . ? 18.270 15.000 6.472 1.00 48.40 ? 402 HOH B O 1 HETATM 1662 O O . HOH E 3 . ? 20.535 34.102 -14.282 1.00 44.44 ? 404 HOH B O 1 HETATM 1663 O O . HOH E 3 . ? 20.782 -0.621 -5.407 1.00 46.29 ? 405 HOH B O 1 HETATM 1664 O O . HOH E 3 . ? 23.107 -2.221 -11.353 1.00 43.61 ? 407 HOH B O 1 HETATM 1665 O O . HOH E 3 . ? 22.316 9.703 -14.567 1.00 39.60 ? 408 HOH B O 1 HETATM 1666 O O . HOH E 3 . ? 26.017 27.396 -17.853 1.00 44.81 ? 411 HOH B O 1 HETATM 1667 O O . HOH E 3 . ? 27.131 17.788 -2.274 1.00 47.44 ? 412 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 PRO 1 1 1 PRO PRO A . n A 1 2 GLN 2 2 2 GLN GLN A . n A 1 3 ILE 3 3 3 ILE ILE A . n A 1 4 THR 4 4 4 THR THR A . n A 1 5 LEU 5 5 5 LEU LEU A . n A 1 6 TRP 6 6 6 TRP TRP A . n A 1 7 GLN 7 7 7 GLN GLN A . n A 1 8 ARG 8 8 8 ARG ARG A . n A 1 9 PRO 9 9 9 PRO PRO A . n A 1 10 LEU 10 10 10 LEU LEU A . n A 1 11 VAL 11 11 11 VAL VAL A . n A 1 12 THR 12 12 12 THR THR A . n A 1 13 ILE 13 13 13 ILE ILE A . n A 1 14 LYS 14 14 14 LYS LYS A . n A 1 15 ILE 15 15 15 ILE ILE A . n A 1 16 GLY 16 16 16 GLY GLY A . n A 1 17 GLY 17 17 17 GLY GLY A . n A 1 18 GLN 18 18 18 GLN GLN A . n A 1 19 LEU 19 19 19 LEU LEU A . n A 1 20 LYS 20 20 20 LYS LYS A . n A 1 21 GLU 21 21 21 GLU GLU A . n A 1 22 ALA 22 22 22 ALA ALA A . n A 1 23 LEU 23 23 23 LEU LEU A . n A 1 24 LEU 24 24 24 LEU LEU A . n A 1 25 ASP 25 25 25 ASP ASP A . n A 1 26 THR 26 26 26 THR THR A . n A 1 27 GLY 27 27 27 GLY GLY A . n A 1 28 ALA 28 28 28 ALA ALA A . n A 1 29 ASP 29 29 29 ASP ASP A . n A 1 30 ASP 30 30 30 ASP ASP A . n A 1 31 THR 31 31 31 THR THR A . n A 1 32 VAL 32 32 32 VAL VAL A . n A 1 33 LEU 33 33 33 LEU LEU A . n A 1 34 GLU 34 34 34 GLU GLU A . n A 1 35 GLU 35 35 35 GLU GLU A . n A 1 36 MET 36 36 36 MET MET A . n A 1 37 SER 37 37 37 SER SER A . n A 1 38 LEU 38 38 38 LEU LEU A . n A 1 39 PRO 39 39 39 PRO PRO A . n A 1 40 GLY 40 40 40 GLY GLY A . n A 1 41 ARG 41 41 41 ARG ARG A . n A 1 42 TRP 42 42 42 TRP TRP A . n A 1 43 LYS 43 43 43 LYS LYS A . n A 1 44 PRO 44 44 44 PRO PRO A . n A 1 45 LYS 45 45 45 LYS LYS A . n A 1 46 MET 46 46 46 MET MET A . n A 1 47 ILE 47 47 47 ILE ILE A . n A 1 48 GLY 48 48 48 GLY GLY A . n A 1 49 GLY 49 49 49 GLY GLY A . n A 1 50 ILE 50 50 50 ILE ILE A . n A 1 51 GLY 51 51 51 GLY GLY A . n A 1 52 GLY 52 52 52 GLY GLY A . n A 1 53 PHE 53 53 53 PHE PHE A . n A 1 54 ILE 54 54 54 ILE ILE A . n A 1 55 LYS 55 55 55 LYS LYS A . n A 1 56 VAL 56 56 56 VAL VAL A . n A 1 57 ARG 57 57 57 ARG ARG A . n A 1 58 GLN 58 58 58 GLN GLN A . n A 1 59 TYR 59 59 59 TYR TYR A . n A 1 60 ASP 60 60 60 ASP ASP A . n A 1 61 GLN 61 61 61 GLN GLN A . n A 1 62 ILE 62 62 62 ILE ILE A . n A 1 63 LEU 63 63 63 LEU LEU A . n A 1 64 ILE 64 64 64 ILE ILE A . n A 1 65 GLU 65 65 65 GLU GLU A . n A 1 66 ILE 66 66 66 ILE ILE A . n A 1 67 CYS 67 67 67 CYS CYS A . n A 1 68 GLY 68 68 68 GLY GLY A . n A 1 69 HIS 69 69 69 HIS HIS A . n A 1 70 LYS 70 70 70 LYS LYS A . n A 1 71 ALA 71 71 71 ALA ALA A . n A 1 72 ILE 72 72 72 ILE ILE A . n A 1 73 GLY 73 73 73 GLY GLY A . n A 1 74 THR 74 74 74 THR THR A . n A 1 75 VAL 75 75 75 VAL VAL A . n A 1 76 LEU 76 76 76 LEU LEU A . n A 1 77 VAL 77 77 77 VAL VAL A . n A 1 78 GLY 78 78 78 GLY GLY A . n A 1 79 PRO 79 79 79 PRO PRO A . n A 1 80 THR 80 80 80 THR THR A . n A 1 81 PRO 81 81 81 PRO PRO A . n A 1 82 VAL 82 82 82 VAL VAL A . n A 1 83 ASN 83 83 83 ASN ASN A . n A 1 84 ILE 84 84 84 ILE ILE A . n A 1 85 ILE 85 85 85 ILE ILE A . n A 1 86 GLY 86 86 86 GLY GLY A . n A 1 87 ARG 87 87 87 ARG ARG A . n A 1 88 ASN 88 88 88 ASN ASN A . n A 1 89 LEU 89 89 89 LEU LEU A . n A 1 90 LEU 90 90 90 LEU LEU A . n A 1 91 THR 91 91 91 THR THR A . n A 1 92 GLN 92 92 92 GLN GLN A . n A 1 93 ILE 93 93 93 ILE ILE A . n A 1 94 GLY 94 94 94 GLY GLY A . n A 1 95 CYS 95 95 95 CYS CYS A . n A 1 96 THR 96 96 96 THR THR A . n A 1 97 LEU 97 97 97 LEU LEU A . n A 1 98 ASN 98 98 98 ASN ASN A . n A 1 99 PHE 99 99 99 PHE PHE A . n B 1 1 PRO 1 1 1 PRO PRO B . n B 1 2 GLN 2 2 2 GLN GLN B . n B 1 3 ILE 3 3 3 ILE ILE B . n B 1 4 THR 4 4 4 THR THR B . n B 1 5 LEU 5 5 5 LEU LEU B . n B 1 6 TRP 6 6 6 TRP TRP B . n B 1 7 GLN 7 7 7 GLN GLN B . n B 1 8 ARG 8 8 8 ARG ARG B . n B 1 9 PRO 9 9 9 PRO PRO B . n B 1 10 LEU 10 10 10 LEU LEU B . n B 1 11 VAL 11 11 11 VAL VAL B . n B 1 12 THR 12 12 12 THR THR B . n B 1 13 ILE 13 13 13 ILE ILE B . n B 1 14 LYS 14 14 14 LYS LYS B . n B 1 15 ILE 15 15 15 ILE ILE B . n B 1 16 GLY 16 16 16 GLY GLY B . n B 1 17 GLY 17 17 17 GLY GLY B . n B 1 18 GLN 18 18 18 GLN GLN B . n B 1 19 LEU 19 19 19 LEU LEU B . n B 1 20 LYS 20 20 20 LYS LYS B . n B 1 21 GLU 21 21 21 GLU GLU B . n B 1 22 ALA 22 22 22 ALA ALA B . n B 1 23 LEU 23 23 23 LEU LEU B . n B 1 24 LEU 24 24 24 LEU LEU B . n B 1 25 ASP 25 25 25 ASP ASP B . n B 1 26 THR 26 26 26 THR THR B . n B 1 27 GLY 27 27 27 GLY GLY B . n B 1 28 ALA 28 28 28 ALA ALA B . n B 1 29 ASP 29 29 29 ASP ASP B . n B 1 30 ASP 30 30 30 ASP ASP B . n B 1 31 THR 31 31 31 THR THR B . n B 1 32 VAL 32 32 32 VAL VAL B . n B 1 33 LEU 33 33 33 LEU LEU B . n B 1 34 GLU 34 34 34 GLU GLU B . n B 1 35 GLU 35 35 35 GLU GLU B . n B 1 36 MET 36 36 36 MET MET B . n B 1 37 SER 37 37 37 SER SER B . n B 1 38 LEU 38 38 38 LEU LEU B . n B 1 39 PRO 39 39 39 PRO PRO B . n B 1 40 GLY 40 40 40 GLY GLY B . n B 1 41 ARG 41 41 41 ARG ARG B . n B 1 42 TRP 42 42 42 TRP TRP B . n B 1 43 LYS 43 43 43 LYS LYS B . n B 1 44 PRO 44 44 44 PRO PRO B . n B 1 45 LYS 45 45 45 LYS LYS B . n B 1 46 MET 46 46 46 MET MET B . n B 1 47 ILE 47 47 47 ILE ILE B . n B 1 48 GLY 48 48 48 GLY GLY B . n B 1 49 GLY 49 49 49 GLY GLY B . n B 1 50 ILE 50 50 50 ILE ILE B . n B 1 51 GLY 51 51 51 GLY GLY B . n B 1 52 GLY 52 52 52 GLY GLY B . n B 1 53 PHE 53 53 53 PHE PHE B . n B 1 54 ILE 54 54 54 ILE ILE B . n B 1 55 LYS 55 55 55 LYS LYS B . n B 1 56 VAL 56 56 56 VAL VAL B . n B 1 57 ARG 57 57 57 ARG ARG B . n B 1 58 GLN 58 58 58 GLN GLN B . n B 1 59 TYR 59 59 59 TYR TYR B . n B 1 60 ASP 60 60 60 ASP ASP B . n B 1 61 GLN 61 61 61 GLN GLN B . n B 1 62 ILE 62 62 62 ILE ILE B . n B 1 63 LEU 63 63 63 LEU LEU B . n B 1 64 ILE 64 64 64 ILE ILE B . n B 1 65 GLU 65 65 65 GLU GLU B . n B 1 66 ILE 66 66 66 ILE ILE B . n B 1 67 CYS 67 67 67 CYS CYS B . n B 1 68 GLY 68 68 68 GLY GLY B . n B 1 69 HIS 69 69 69 HIS HIS B . n B 1 70 LYS 70 70 70 LYS LYS B . n B 1 71 ALA 71 71 71 ALA ALA B . n B 1 72 ILE 72 72 72 ILE ILE B . n B 1 73 GLY 73 73 73 GLY GLY B . n B 1 74 THR 74 74 74 THR THR B . n B 1 75 VAL 75 75 75 VAL VAL B . n B 1 76 LEU 76 76 76 LEU LEU B . n B 1 77 VAL 77 77 77 VAL VAL B . n B 1 78 GLY 78 78 78 GLY GLY B . n B 1 79 PRO 79 79 79 PRO PRO B . n B 1 80 THR 80 80 80 THR THR B . n B 1 81 PRO 81 81 81 PRO PRO B . n B 1 82 VAL 82 82 82 VAL VAL B . n B 1 83 ASN 83 83 83 ASN ASN B . n B 1 84 ILE 84 84 84 ILE ILE B . n B 1 85 ILE 85 85 85 ILE ILE B . n B 1 86 GLY 86 86 86 GLY GLY B . n B 1 87 ARG 87 87 87 ARG ARG B . n B 1 88 ASN 88 88 88 ASN ASN B . n B 1 89 LEU 89 89 89 LEU LEU B . n B 1 90 LEU 90 90 90 LEU LEU B . n B 1 91 THR 91 91 91 THR THR B . n B 1 92 GLN 92 92 92 GLN GLN B . n B 1 93 ILE 93 93 93 ILE ILE B . n B 1 94 GLY 94 94 94 GLY GLY B . n B 1 95 CYS 95 95 95 CYS CYS B . n B 1 96 THR 96 96 96 THR THR B . n B 1 97 LEU 97 97 97 LEU LEU B . n B 1 98 ASN 98 98 98 ASN ASN B . n B 1 99 PHE 99 99 99 PHE PHE 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 AH1 1 500 500 AH1 AH1 A . D 3 HOH 1 306 306 HOH HOH A . D 3 HOH 2 311 311 HOH HOH A . D 3 HOH 3 313 313 HOH HOH A . D 3 HOH 4 314 314 HOH HOH A . D 3 HOH 5 317 317 HOH HOH A . D 3 HOH 6 318 318 HOH HOH A . D 3 HOH 7 319 319 HOH HOH A . D 3 HOH 8 320 320 HOH HOH A . D 3 HOH 9 321 321 HOH HOH A . D 3 HOH 10 326 326 HOH HOH A . D 3 HOH 11 327 327 HOH HOH A . D 3 HOH 12 330 330 HOH HOH A . D 3 HOH 13 331 331 HOH HOH A . D 3 HOH 14 332 332 HOH HOH A . D 3 HOH 15 333 333 HOH HOH A . D 3 HOH 16 334 334 HOH HOH A . D 3 HOH 17 335 335 HOH HOH A . D 3 HOH 18 338 338 HOH HOH A . D 3 HOH 19 339 339 HOH HOH A . D 3 HOH 20 343 343 HOH HOH A . D 3 HOH 21 345 345 HOH HOH A . D 3 HOH 22 349 349 HOH HOH A . D 3 HOH 23 350 350 HOH HOH A . D 3 HOH 24 352 352 HOH HOH A . D 3 HOH 25 353 353 HOH HOH A . D 3 HOH 26 354 354 HOH HOH A . D 3 HOH 27 355 355 HOH HOH A . D 3 HOH 28 358 358 HOH HOH A . D 3 HOH 29 359 359 HOH HOH A . D 3 HOH 30 364 364 HOH HOH A . D 3 HOH 31 368 368 HOH HOH A . D 3 HOH 32 374 374 HOH HOH A . D 3 HOH 33 375 375 HOH HOH A . D 3 HOH 34 378 378 HOH HOH A . D 3 HOH 35 379 379 HOH HOH A . D 3 HOH 36 382 382 HOH HOH A . D 3 HOH 37 385 385 HOH HOH A . D 3 HOH 38 386 386 HOH HOH A . D 3 HOH 39 387 387 HOH HOH A . D 3 HOH 40 388 388 HOH HOH A . D 3 HOH 41 390 390 HOH HOH A . D 3 HOH 42 391 391 HOH HOH A . D 3 HOH 43 394 394 HOH HOH A . D 3 HOH 44 398 398 HOH HOH A . D 3 HOH 45 403 403 HOH HOH A . D 3 HOH 46 409 409 HOH HOH A . D 3 HOH 47 410 410 HOH HOH A . D 3 HOH 48 413 413 HOH HOH A . D 3 HOH 49 414 414 HOH HOH A . E 3 HOH 1 301 301 HOH HOH B . E 3 HOH 2 302 302 HOH HOH B . E 3 HOH 3 303 303 HOH HOH B . E 3 HOH 4 304 304 HOH HOH B . E 3 HOH 5 305 305 HOH HOH B . E 3 HOH 6 307 307 HOH HOH B . E 3 HOH 7 308 308 HOH HOH B . E 3 HOH 8 309 309 HOH HOH B . E 3 HOH 9 310 310 HOH HOH B . E 3 HOH 10 312 312 HOH HOH B . E 3 HOH 11 315 315 HOH HOH B . E 3 HOH 12 316 316 HOH HOH B . E 3 HOH 13 322 322 HOH HOH B . E 3 HOH 14 323 323 HOH HOH B . E 3 HOH 15 324 324 HOH HOH B . E 3 HOH 16 325 325 HOH HOH B . E 3 HOH 17 328 328 HOH HOH B . E 3 HOH 18 329 329 HOH HOH B . E 3 HOH 19 336 336 HOH HOH B . E 3 HOH 20 337 337 HOH HOH B . E 3 HOH 21 340 340 HOH HOH B . E 3 HOH 22 341 341 HOH HOH B . E 3 HOH 23 342 342 HOH HOH B . E 3 HOH 24 344 344 HOH HOH B . E 3 HOH 25 346 346 HOH HOH B . E 3 HOH 26 347 347 HOH HOH B . E 3 HOH 27 348 348 HOH HOH B . E 3 HOH 28 351 351 HOH HOH B . E 3 HOH 29 356 356 HOH HOH B . E 3 HOH 30 360 360 HOH HOH B . E 3 HOH 31 361 361 HOH HOH B . E 3 HOH 32 362 362 HOH HOH B . E 3 HOH 33 363 363 HOH HOH B . E 3 HOH 34 366 366 HOH HOH B . E 3 HOH 35 367 367 HOH HOH B . E 3 HOH 36 369 369 HOH HOH B . E 3 HOH 37 370 370 HOH HOH B . E 3 HOH 38 371 371 HOH HOH B . E 3 HOH 39 372 372 HOH HOH B . E 3 HOH 40 373 373 HOH HOH B . E 3 HOH 41 376 376 HOH HOH B . E 3 HOH 42 377 377 HOH HOH B . E 3 HOH 43 380 380 HOH HOH B . E 3 HOH 44 381 381 HOH HOH B . E 3 HOH 45 383 383 HOH HOH B . E 3 HOH 46 384 384 HOH HOH B . E 3 HOH 47 389 389 HOH HOH B . E 3 HOH 48 392 392 HOH HOH B . E 3 HOH 49 393 393 HOH HOH B . E 3 HOH 50 395 395 HOH HOH B . E 3 HOH 51 396 396 HOH HOH B . E 3 HOH 52 397 397 HOH HOH B . E 3 HOH 53 399 399 HOH HOH B . E 3 HOH 54 400 400 HOH HOH B . E 3 HOH 55 401 401 HOH HOH B . E 3 HOH 56 402 402 HOH HOH B . E 3 HOH 57 404 404 HOH HOH B . E 3 HOH 58 405 405 HOH HOH B . E 3 HOH 59 407 407 HOH HOH B . E 3 HOH 60 408 408 HOH HOH B . E 3 HOH 61 411 411 HOH HOH B . E 3 HOH 62 412 412 HOH HOH B . # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_and_software_defined_assembly _pdbx_struct_assembly.method_details PISA _pdbx_struct_assembly.oligomeric_details dimeric _pdbx_struct_assembly.oligomeric_count 2 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E # 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)' 4850 ? 1 MORE -33 ? 1 'SSA (A^2)' 9050 ? # _pdbx_struct_oper_list.id 1 _pdbx_struct_oper_list.type 'identity operation' _pdbx_struct_oper_list.name 1_555 _pdbx_struct_oper_list.symmetry_operation x,y,z _pdbx_struct_oper_list.matrix[1][1] 1.0000000000 _pdbx_struct_oper_list.matrix[1][2] 0.0000000000 _pdbx_struct_oper_list.matrix[1][3] 0.0000000000 _pdbx_struct_oper_list.vector[1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][2] 1.0000000000 _pdbx_struct_oper_list.matrix[2][3] 0.0000000000 _pdbx_struct_oper_list.vector[2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][1] 0.0000000000 _pdbx_struct_oper_list.matrix[3][2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][3] 1.0000000000 _pdbx_struct_oper_list.vector[3] 0.0000000000 # loop_ _pdbx_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 1997-09-17 2 'Structure model' 1 1 2008-03-24 3 'Structure model' 1 2 2011-07-13 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # loop_ _pdbx_audit_revision_group.ordinal _pdbx_audit_revision_group.revision_ordinal _pdbx_audit_revision_group.data_content_type _pdbx_audit_revision_group.group 1 2 'Structure model' 'Version format compliance' 2 3 'Structure model' 'Version format compliance' # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal X-PLOR 'model building' . ? 1 X-PLOR refinement 3.1 ? 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 CD A GLU 21 ? ? OE1 A GLU 21 ? ? 1.323 1.252 0.071 0.011 N 2 1 CB A GLU 65 ? ? CG A GLU 65 ? ? 1.388 1.517 -0.129 0.019 N 3 1 CB B GLU 21 ? ? CG B GLU 21 ? ? 1.389 1.517 -0.128 0.019 N 4 1 CB B CYS 67 ? ? SG B CYS 67 ? ? 1.705 1.812 -0.107 0.016 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 NE A ARG 57 ? ? CZ A ARG 57 ? ? NH1 A ARG 57 ? ? 116.23 120.30 -4.07 0.50 N 2 1 NE A ARG 57 ? ? CZ A ARG 57 ? ? NH2 A ARG 57 ? ? 125.83 120.30 5.53 0.50 N 3 1 NE A ARG 87 ? ? CZ A ARG 87 ? ? NH1 A ARG 87 ? ? 123.46 120.30 3.16 0.50 N 4 1 CB B ASP 29 ? ? CG B ASP 29 ? ? OD1 B ASP 29 ? ? 124.18 118.30 5.88 0.90 N 5 1 CB B ASP 29 ? ? CG B ASP 29 ? ? OD2 B ASP 29 ? ? 112.72 118.30 -5.58 0.90 N 6 1 NE B ARG 41 ? ? CZ B ARG 41 ? ? NH2 B ARG 41 ? ? 115.83 120.30 -4.47 0.50 N # _pdbx_validate_torsion.id 1 _pdbx_validate_torsion.PDB_model_num 1 _pdbx_validate_torsion.auth_comp_id PRO _pdbx_validate_torsion.auth_asym_id A _pdbx_validate_torsion.auth_seq_id 79 _pdbx_validate_torsion.PDB_ins_code ? _pdbx_validate_torsion.label_alt_id ? _pdbx_validate_torsion.phi -75.55 _pdbx_validate_torsion.psi 46.40 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 AHA001 AH1 3 water HOH # If you find results from this site helpful for your research, please cite one of our papers:
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