data_2AIQ # _entry.id 2AIQ # _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 2AIQ RCSB RCSB033941 WWPDB D_1000033941 # _pdbx_database_related.db_name PDB _pdbx_database_related.db_id 2AIP _pdbx_database_related.details 'The same protein complexed with benzamidine inhibitor' _pdbx_database_related.content_type unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 2AIQ _pdbx_database_status.recvd_initial_deposition_date 2005-07-30 _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site RCSB _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 'Murakami, M.T.' 1 'Arni, R.K.' 2 # _citation.id primary _citation.title ;Thrombomodulin-independent Activation of Protein C and Specificity of Hemostatically Active Snake Venom Serine Proteinases: CRYSTAL STRUCTURES OF NATIVE AND INHIBITED AGKISTRODON CONTORTRIX CONTORTRIX PROTEIN C ACTIVATOR. ; _citation.journal_abbrev J.Biol.Chem. _citation.journal_volume 280 _citation.page_first 39309 _citation.page_last 39315 _citation.year 2005 _citation.journal_id_ASTM JBCHA3 _citation.country US _citation.journal_id_ISSN 0021-9258 _citation.journal_id_CSD 0071 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 16162508 _citation.pdbx_database_id_DOI 10.1074/jbc.M508502200 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Murakami, M.T.' 1 primary 'Arni, R.K.' 2 # _cell.entry_id 2AIQ _cell.length_a 80.516 _cell.length_b 63.463 _cell.length_c 48.216 _cell.angle_alpha 90.00 _cell.angle_beta 99.85 _cell.angle_gamma 90.00 _cell.Z_PDB 4 _cell.pdbx_unique_axis ? # _symmetry.entry_id 2AIQ _symmetry.space_group_name_H-M 'C 1 2 1' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 5 _symmetry.space_group_name_Hall ? # loop_ _entity.id _entity.type _entity.src_method _entity.pdbx_description _entity.formula_weight _entity.pdbx_number_of_molecules _entity.pdbx_ec _entity.pdbx_mutation _entity.pdbx_fragment _entity.details 1 polymer nat 'Protein C activator' 25132.881 1 3.4.21.74 ? ? ? 2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 2 ? ? ? ? 3 non-polymer man '2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE' 221.208 1 ? ? ? ? 4 non-polymer syn 'SULFATE ION' 96.063 1 ? ? ? ? 5 non-polymer syn 'ACETATE ION' 59.044 1 ? ? ? ? 6 non-polymer syn 'CHLORIDE ION' 35.453 1 ? ? ? ? 7 non-polymer syn BENZAMIDINE 120.152 1 ? ? ? ? 8 non-polymer syn GLYCEROL 92.094 1 ? ? ? ? 9 water nat water 18.015 229 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name 'Venombin A, Ancrod, ACC-C' # _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 ;VIGGDECNINEHRFLALVYANGSLCGGTLINQEWVLTARHCDRGNMRIYLGMHNLKVLNKDALRRFPKEKYFCLNTRNDT IWDKDIMLIRLNRPVRNSAHIAPLSLPSNPPSVGSVCRIMGWGTITSPNATLPDVPHCANINILDYAVCQAAYKGLAATT LCAGILEGGKDTCKGDSGGPLICNGQFQGILSVGGNPCAQPRKPGIYTKVFDYTDWIQSIISGNTDATCPP ; _entity_poly.pdbx_seq_one_letter_code_can ;VIGGDECNINEHRFLALVYANGSLCGGTLINQEWVLTARHCDRGNMRIYLGMHNLKVLNKDALRRFPKEKYFCLNTRNDT IWDKDIMLIRLNRPVRNSAHIAPLSLPSNPPSVGSVCRIMGWGTITSPNATLPDVPHCANINILDYAVCQAAYKGLAATT LCAGILEGGKDTCKGDSGGPLICNGQFQGILSVGGNPCAQPRKPGIYTKVFDYTDWIQSIISGNTDATCPP ; _entity_poly.pdbx_strand_id A _entity_poly.pdbx_target_identifier ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 VAL n 1 2 ILE n 1 3 GLY n 1 4 GLY n 1 5 ASP n 1 6 GLU n 1 7 CYS n 1 8 ASN n 1 9 ILE n 1 10 ASN n 1 11 GLU n 1 12 HIS n 1 13 ARG n 1 14 PHE n 1 15 LEU n 1 16 ALA n 1 17 LEU n 1 18 VAL n 1 19 TYR n 1 20 ALA n 1 21 ASN n 1 22 GLY n 1 23 SER n 1 24 LEU n 1 25 CYS n 1 26 GLY n 1 27 GLY n 1 28 THR n 1 29 LEU n 1 30 ILE n 1 31 ASN n 1 32 GLN n 1 33 GLU n 1 34 TRP n 1 35 VAL n 1 36 LEU n 1 37 THR n 1 38 ALA n 1 39 ARG n 1 40 HIS n 1 41 CYS n 1 42 ASP n 1 43 ARG n 1 44 GLY n 1 45 ASN n 1 46 MET n 1 47 ARG n 1 48 ILE n 1 49 TYR n 1 50 LEU n 1 51 GLY n 1 52 MET n 1 53 HIS n 1 54 ASN n 1 55 LEU n 1 56 LYS n 1 57 VAL n 1 58 LEU n 1 59 ASN n 1 60 LYS n 1 61 ASP n 1 62 ALA n 1 63 LEU n 1 64 ARG n 1 65 ARG n 1 66 PHE n 1 67 PRO n 1 68 LYS n 1 69 GLU n 1 70 LYS n 1 71 TYR n 1 72 PHE n 1 73 CYS n 1 74 LEU n 1 75 ASN n 1 76 THR n 1 77 ARG n 1 78 ASN n 1 79 ASP n 1 80 THR n 1 81 ILE n 1 82 TRP n 1 83 ASP n 1 84 LYS n 1 85 ASP n 1 86 ILE n 1 87 MET n 1 88 LEU n 1 89 ILE n 1 90 ARG n 1 91 LEU n 1 92 ASN n 1 93 ARG n 1 94 PRO n 1 95 VAL n 1 96 ARG n 1 97 ASN n 1 98 SER n 1 99 ALA n 1 100 HIS n 1 101 ILE n 1 102 ALA n 1 103 PRO n 1 104 LEU n 1 105 SER n 1 106 LEU n 1 107 PRO n 1 108 SER n 1 109 ASN n 1 110 PRO n 1 111 PRO n 1 112 SER n 1 113 VAL n 1 114 GLY n 1 115 SER n 1 116 VAL n 1 117 CYS n 1 118 ARG n 1 119 ILE n 1 120 MET n 1 121 GLY n 1 122 TRP n 1 123 GLY n 1 124 THR n 1 125 ILE n 1 126 THR n 1 127 SER n 1 128 PRO n 1 129 ASN n 1 130 ALA n 1 131 THR n 1 132 LEU n 1 133 PRO n 1 134 ASP n 1 135 VAL n 1 136 PRO n 1 137 HIS n 1 138 CYS n 1 139 ALA n 1 140 ASN n 1 141 ILE n 1 142 ASN n 1 143 ILE n 1 144 LEU n 1 145 ASP n 1 146 TYR n 1 147 ALA n 1 148 VAL n 1 149 CYS n 1 150 GLN n 1 151 ALA n 1 152 ALA n 1 153 TYR n 1 154 LYS n 1 155 GLY n 1 156 LEU n 1 157 ALA n 1 158 ALA n 1 159 THR n 1 160 THR n 1 161 LEU n 1 162 CYS n 1 163 ALA n 1 164 GLY n 1 165 ILE n 1 166 LEU n 1 167 GLU n 1 168 GLY n 1 169 GLY n 1 170 LYS n 1 171 ASP n 1 172 THR n 1 173 CYS n 1 174 LYS n 1 175 GLY n 1 176 ASP n 1 177 SER n 1 178 GLY n 1 179 GLY n 1 180 PRO n 1 181 LEU n 1 182 ILE n 1 183 CYS n 1 184 ASN n 1 185 GLY n 1 186 GLN n 1 187 PHE n 1 188 GLN n 1 189 GLY n 1 190 ILE n 1 191 LEU n 1 192 SER n 1 193 VAL n 1 194 GLY n 1 195 GLY n 1 196 ASN n 1 197 PRO n 1 198 CYS n 1 199 ALA n 1 200 GLN n 1 201 PRO n 1 202 ARG n 1 203 LYS n 1 204 PRO n 1 205 GLY n 1 206 ILE n 1 207 TYR n 1 208 THR n 1 209 LYS n 1 210 VAL n 1 211 PHE n 1 212 ASP n 1 213 TYR n 1 214 THR n 1 215 ASP n 1 216 TRP n 1 217 ILE n 1 218 GLN n 1 219 SER n 1 220 ILE n 1 221 ILE n 1 222 SER n 1 223 GLY n 1 224 ASN n 1 225 THR n 1 226 ASP n 1 227 ALA n 1 228 THR n 1 229 CYS n 1 230 PRO n 1 231 PRO n # _entity_src_nat.entity_id 1 _entity_src_nat.pdbx_src_id 1 _entity_src_nat.pdbx_alt_source_flag sample _entity_src_nat.pdbx_beg_seq_num ? _entity_src_nat.pdbx_end_seq_num ? _entity_src_nat.common_name 'southern copperhead' _entity_src_nat.pdbx_organism_scientific 'Agkistrodon contortrix contortrix' _entity_src_nat.pdbx_ncbi_taxonomy_id 8713 _entity_src_nat.genus Agkistrodon _entity_src_nat.species 'Agkistrodon contortrix' _entity_src_nat.strain contortrix _entity_src_nat.tissue ? _entity_src_nat.tissue_fraction ? _entity_src_nat.pdbx_secretion ? _entity_src_nat.pdbx_fragment ? _entity_src_nat.pdbx_variant ? _entity_src_nat.pdbx_cell_line ? _entity_src_nat.pdbx_atcc ? _entity_src_nat.pdbx_cellular_location ? _entity_src_nat.pdbx_organ ? _entity_src_nat.pdbx_organelle ? _entity_src_nat.pdbx_cell ? _entity_src_nat.pdbx_plasmid_name ? _entity_src_nat.pdbx_plasmid_details ? _entity_src_nat.details ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code VSP1_AGKCO _struct_ref.pdbx_db_accession P09872 _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ;VIGGDECNINEHRFLALVYANGSLCGGTLINQEWVLTARHCDRGNMRIYLGMHNLKVLNKDALRRFPKEKYFCLNTRNDT IWDKDIMLIRLNRPVRNSAHIAPLSLPSNPPSVGSVCRIMGWGTITSPNATLPDVPHCANINILDYAVCQAAYKGLAATT LCAGILEGGKDTCKGDSGGPLICNGQFQGILSVGGNPCAQPRKPGIYTKVFDYTDWIQSIISGNTDATCPP ; _struct_ref.pdbx_align_begin 1 _struct_ref.pdbx_db_isoform ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 2AIQ _struct_ref_seq.pdbx_strand_id A _struct_ref_seq.seq_align_beg 1 _struct_ref_seq.pdbx_seq_align_beg_ins_code ? _struct_ref_seq.seq_align_end 231 _struct_ref_seq.pdbx_seq_align_end_ins_code G _struct_ref_seq.pdbx_db_accession P09872 _struct_ref_seq.db_align_beg 1 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 231 _struct_ref_seq.pdbx_db_align_end_ins_code ? _struct_ref_seq.pdbx_auth_seq_align_beg 16 _struct_ref_seq.pdbx_auth_seq_align_end 245 # 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 ACT non-polymer . 'ACETATE ION' ? 'C2 H3 O2 -1' 59.044 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 BEN non-polymer . BENZAMIDINE ? 'C7 H8 N2' 120.152 CL non-polymer . 'CHLORIDE ION' ? 'Cl -1' 35.453 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 GOL non-polymer . GLYCEROL 'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3' 92.094 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 NDG D-saccharide . '2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE' ? 'C8 H15 N O6' 221.208 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 SO4 non-polymer . 'SULFATE ION' ? 'O4 S -2' 96.063 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 2AIQ _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.12 _exptl_crystal.density_percent_sol 41.7 _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.preparation ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method 'VAPOR DIFFUSION, HANGING DROP' _exptl_crystal_grow.temp 293 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 4.6 _exptl_crystal_grow.pdbx_details 'ammonium sulfate, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K' _exptl_crystal_grow.pdbx_pH_range . # _diffrn.id 1 _diffrn.ambient_temp 100 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector CCD _diffrn_detector.type MARRESEARCH _diffrn_detector.pdbx_collection_date 2005-05-19 _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator ? _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 1.438 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'LNLS BEAMLINE D03B-MX1' _diffrn_source.pdbx_synchrotron_site LNLS _diffrn_source.pdbx_synchrotron_beamline D03B-MX1 _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_wavelength_list 1.438 # _reflns.entry_id 2AIQ _reflns.observed_criterion_sigma_F 2.5 _reflns.observed_criterion_sigma_I 2.5 _reflns.d_resolution_high 1.54 _reflns.d_resolution_low 20.58 _reflns.number_all ? _reflns.number_obs 35447 _reflns.percent_possible_obs 99.9 _reflns.pdbx_Rmerge_I_obs 0.084 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 2.5 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy ? _reflns.R_free_details ? _reflns.limit_h_max ? _reflns.limit_h_min ? _reflns.limit_k_max ? _reflns.limit_k_min ? _reflns.limit_l_max ? _reflns.limit_l_min ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? _reflns.pdbx_ordinal 1 _reflns.pdbx_diffrn_id 1 # _reflns_shell.d_res_high 1.54 _reflns_shell.d_res_low 1.60 _reflns_shell.percent_possible_all 99.8 _reflns_shell.Rmerge_I_obs ? _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs ? _reflns_shell.pdbx_redundancy ? _reflns_shell.percent_possible_obs ? _reflns_shell.number_unique_all ? _reflns_shell.number_measured_all ? _reflns_shell.number_measured_obs ? _reflns_shell.number_unique_obs ? _reflns_shell.pdbx_chi_squared ? _reflns_shell.pdbx_ordinal 1 _reflns_shell.pdbx_diffrn_id 1 # _refine.entry_id 2AIQ _refine.ls_number_reflns_obs 33670 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F ? _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 20.58 _refine.ls_d_res_high 1.54 _refine.ls_percent_reflns_obs 99.81 _refine.ls_R_factor_obs 0.16922 _refine.ls_R_factor_all 0.1763 _refine.ls_R_factor_R_work 0.16812 _refine.ls_R_factor_R_free 0.19055 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.0 _refine.ls_number_reflns_R_free 1774 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.966 _refine.correlation_coeff_Fo_to_Fc_free 0.957 _refine.B_iso_mean 17.529 _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 MASK _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.20 _refine.pdbx_solvent_ion_probe_radii 0.80 _refine.pdbx_solvent_shrinkage_radii 0.80 _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details ? _refine.pdbx_starting_model 'PDB entry 2AIP' _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model isotropic _refine.pdbx_stereochemistry_target_values 'MAXIMUM LIKELIHOOD' _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_overall_ESU_R 0.075 _refine.pdbx_overall_ESU_R_Free 0.074 _refine.overall_SU_ML 0.046 _refine.overall_SU_B 1.237 _refine.ls_redundancy_reflns_obs ? _refine.B_iso_min ? _refine.B_iso_max ? _refine.overall_SU_R_Cruickshank_DPI ? _refine.overall_SU_R_free ? _refine.ls_wR_factor_R_free ? _refine.ls_wR_factor_R_work ? _refine.overall_FOM_free_R_set ? _refine.overall_FOM_work_R_set ? _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.pdbx_overall_phase_error ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 1757 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 67 _refine_hist.number_atoms_solvent 229 _refine_hist.number_atoms_total 2053 _refine_hist.d_res_high 1.54 _refine_hist.d_res_low 20.58 # 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 r_bond_refined_d 0.010 0.022 ? 1882 'X-RAY DIFFRACTION' ? r_angle_refined_deg 1.455 1.995 ? 2563 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 6.317 5.000 ? 230 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg 35.938 24.156 ? 77 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg 12.367 15.000 ? 297 'X-RAY DIFFRACTION' ? r_dihedral_angle_4_deg 21.094 15.000 ? 12 'X-RAY DIFFRACTION' ? r_chiral_restr 0.091 0.200 ? 288 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.005 0.020 ? 1408 'X-RAY DIFFRACTION' ? r_nbd_refined 0.220 0.200 ? 1052 'X-RAY DIFFRACTION' ? r_nbtor_refined 0.323 0.200 ? 1340 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_refined 0.126 0.200 ? 252 'X-RAY DIFFRACTION' ? r_symmetry_vdw_refined 0.195 0.200 ? 78 'X-RAY DIFFRACTION' ? r_symmetry_hbond_refined 0.167 0.200 ? 29 'X-RAY DIFFRACTION' ? r_mcbond_it 0.725 1.500 ? 1168 'X-RAY DIFFRACTION' ? r_mcangle_it 1.278 2.000 ? 1865 'X-RAY DIFFRACTION' ? r_scbond_it 1.915 3.000 ? 780 'X-RAY DIFFRACTION' ? r_scangle_it 2.929 4.500 ? 698 'X-RAY DIFFRACTION' ? # _refine_ls_shell.pdbx_total_number_of_bins_used 20 _refine_ls_shell.d_res_high 1.54 _refine_ls_shell.d_res_low 1.578 _refine_ls_shell.number_reflns_R_work 2397 _refine_ls_shell.R_factor_R_work 0.26 _refine_ls_shell.percent_reflns_obs 97.71 _refine_ls_shell.R_factor_R_free 0.281 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 125 _refine_ls_shell.number_reflns_obs ? _refine_ls_shell.redundancy_reflns_obs ? _refine_ls_shell.number_reflns_all ? _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_ls_shell.R_factor_all ? # _struct.entry_id 2AIQ _struct.title 'Crystal structure of benzamidine-inhibited protein C activator from the venom of copperhead snake Agkistrodon contortrix contortrix' _struct.pdbx_descriptor 'Protein C activator (E.C.3.4.21.74)' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 2AIQ _struct_keywords.pdbx_keywords HYDROLASE _struct_keywords.text 'Protein C activator, snake venom serine proteinase, hydrolase' # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 2 ? D N N 3 ? E N N 4 ? F N N 5 ? G N N 6 ? H N N 7 ? I N N 8 ? J N N 9 ? # _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 ALA A 38 ? ASP A 42 ? ALA A 55 ASP A 59 5 ? 5 HELX_P HELX_P2 2 ASP A 145 ? TYR A 153 ? ASP A 164 TYR A 172 1 ? 9 HELX_P HELX_P3 3 TYR A 213 ? GLY A 223 ? TYR A 234 GLY A 244 1 ? 11 # _struct_conf_type.id HELX_P _struct_conf_type.criteria ? _struct_conf_type.reference ? # loop_ _struct_conn.id _struct_conn.conn_type_id _struct_conn.pdbx_leaving_atom_flag _struct_conn.pdbx_PDB_id _struct_conn.ptnr1_label_asym_id _struct_conn.ptnr1_label_comp_id _struct_conn.ptnr1_label_seq_id _struct_conn.ptnr1_label_atom_id _struct_conn.pdbx_ptnr1_label_alt_id _struct_conn.pdbx_ptnr1_PDB_ins_code _struct_conn.pdbx_ptnr1_standard_comp_id _struct_conn.ptnr1_symmetry _struct_conn.ptnr2_label_asym_id _struct_conn.ptnr2_label_comp_id _struct_conn.ptnr2_label_seq_id _struct_conn.ptnr2_label_atom_id _struct_conn.pdbx_ptnr2_label_alt_id _struct_conn.pdbx_ptnr2_PDB_ins_code _struct_conn.ptnr1_auth_asym_id _struct_conn.ptnr1_auth_comp_id _struct_conn.ptnr1_auth_seq_id _struct_conn.ptnr2_auth_asym_id _struct_conn.ptnr2_auth_comp_id _struct_conn.ptnr2_auth_seq_id _struct_conn.ptnr2_symmetry _struct_conn.pdbx_ptnr3_label_atom_id _struct_conn.pdbx_ptnr3_label_seq_id _struct_conn.pdbx_ptnr3_label_comp_id _struct_conn.pdbx_ptnr3_label_asym_id _struct_conn.pdbx_ptnr3_label_alt_id _struct_conn.pdbx_ptnr3_PDB_ins_code _struct_conn.details _struct_conn.pdbx_dist_value _struct_conn.pdbx_value_order disulf1 disulf ? ? A CYS 7 SG ? ? ? 1_555 A CYS 138 SG ? ? A CYS 22 A CYS 157 1_555 ? ? ? ? ? ? ? 2.048 ? disulf2 disulf ? ? A CYS 25 SG ? ? ? 1_555 A CYS 41 SG ? ? A CYS 42 A CYS 58 1_555 ? ? ? ? ? ? ? 2.031 ? disulf3 disulf ? ? A CYS 73 SG ? ? ? 1_555 A CYS 229 SG ? E A CYS 91 A CYS 245 1_555 ? ? ? ? ? ? ? 2.019 ? disulf4 disulf ? ? A CYS 117 SG ? ? ? 1_555 A CYS 183 SG ? ? A CYS 136 A CYS 201 1_555 ? ? ? ? ? ? ? 2.043 ? disulf5 disulf ? ? A CYS 149 SG ? ? ? 1_555 A CYS 162 SG ? ? A CYS 168 A CYS 182 1_555 ? ? ? ? ? ? ? 2.052 ? disulf6 disulf ? ? A CYS 173 SG ? ? ? 1_555 A CYS 198 SG ? ? A CYS 191 A CYS 220 1_555 ? ? ? ? ? ? ? 2.046 ? covale1 covale ? ? A ASN 21 ND2 ? ? ? 1_555 D NDG . C1 ? ? A ASN 38 A NDG 901 1_555 ? ? ? ? ? ? ? 1.439 ? covale2 covale ? ? A ASN 78 ND2 ? A ? 1_555 C NAG . C1 ? ? A ASN 96 A NAG 801 1_555 ? ? ? ? ? ? ? 1.446 ? covale3 covale ? ? A ASN 129 ND2 ? ? ? 1_555 B NAG . C1 ? ? A ASN 148 A NAG 701 1_555 ? ? ? ? ? ? ? 1.440 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? # loop_ _struct_mon_prot_cis.pdbx_id _struct_mon_prot_cis.label_comp_id _struct_mon_prot_cis.label_seq_id _struct_mon_prot_cis.label_asym_id _struct_mon_prot_cis.label_alt_id _struct_mon_prot_cis.pdbx_PDB_ins_code _struct_mon_prot_cis.auth_comp_id _struct_mon_prot_cis.auth_seq_id _struct_mon_prot_cis.auth_asym_id _struct_mon_prot_cis.pdbx_label_comp_id_2 _struct_mon_prot_cis.pdbx_label_seq_id_2 _struct_mon_prot_cis.pdbx_label_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_ins_code_2 _struct_mon_prot_cis.pdbx_auth_comp_id_2 _struct_mon_prot_cis.pdbx_auth_seq_id_2 _struct_mon_prot_cis.pdbx_auth_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_model_num _struct_mon_prot_cis.pdbx_omega_angle 1 SER 127 A . ? SER 146 A PRO 128 A ? PRO 147 A 1 2.05 2 ASN 196 A . ? ASN 218 A PRO 197 A ? PRO 219 A 1 4.58 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 8 ? B ? 7 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense A 1 2 ? anti-parallel A 2 3 ? anti-parallel A 3 4 ? anti-parallel A 4 5 ? anti-parallel A 5 6 ? anti-parallel A 6 7 ? anti-parallel A 7 8 ? anti-parallel B 1 2 ? anti-parallel B 2 3 ? anti-parallel B 3 4 ? anti-parallel B 4 5 ? anti-parallel B 5 6 ? anti-parallel B 6 7 ? anti-parallel # 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 ASP A 5 ? GLU A 6 ? ASP A 20 GLU A 21 A 2 HIS A 137 ? LEU A 144 ? HIS A 156 LEU A 163 A 3 THR A 160 ? GLY A 164 ? THR A 180 GLY A 184 A 4 GLY A 205 ? LYS A 209 ? GLY A 226 LYS A 230 A 5 GLN A 186 ? GLY A 194 ? GLN A 208 GLY A 216 A 6 PRO A 180 ? CYS A 183 ? PRO A 198 CYS A 201 A 7 VAL A 116 ? GLY A 121 ? VAL A 135 GLY A 140 A 8 HIS A 137 ? LEU A 144 ? HIS A 156 LEU A 163 B 1 LEU A 63 ? ARG A 65 ? LEU A 81 ARG A 83 B 2 ARG A 47 ? LEU A 50 ? ARG A 65 LEU A 68 B 3 LEU A 15 ? ALA A 20 ? LEU A 30 ALA A 36 B 4 SER A 23 ? LEU A 29 ? SER A 40 LEU A 46 B 5 TRP A 34 ? THR A 37 ? TRP A 51 THR A 54 B 6 MET A 87 ? LEU A 91 ? MET A 104 LEU A 108 B 7 PRO A 67 ? TYR A 71 ? PRO A 85 TYR A 89 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id A 1 2 N ASP A 5 ? N ASP A 20 O CYS A 138 ? O CYS A 157 A 2 3 N LEU A 144 ? N LEU A 163 O CYS A 162 ? O CYS A 182 A 3 4 N LEU A 161 ? N LEU A 181 O TYR A 207 ? O TYR A 228 A 4 5 O ILE A 206 ? O ILE A 227 N VAL A 193 ? N VAL A 215 A 5 6 O GLN A 188 ? O GLN A 210 N LEU A 181 ? N LEU A 199 A 6 7 O ILE A 182 ? O ILE A 200 N ARG A 118 ? N ARG A 137 A 7 8 N CYS A 117 ? N CYS A 136 O ILE A 141 ? O ILE A 160 B 1 2 O ARG A 65 ? O ARG A 83 N ILE A 48 ? N ILE A 66 B 2 3 O TYR A 49 ? O TYR A 67 N LEU A 17 ? N LEU A 32 B 3 4 N VAL A 18 ? N VAL A 33 O CYS A 25 ? O CYS A 42 B 4 5 N THR A 28 ? N THR A 45 O LEU A 36 ? O LEU A 53 B 5 6 N VAL A 35 ? N VAL A 52 O ILE A 89 ? O ILE A 106 B 6 7 O ARG A 90 ? O ARG A 107 N LYS A 68 ? N LYS A 86 # loop_ _struct_site.id _struct_site.pdbx_evidence_code _struct_site.pdbx_auth_asym_id _struct_site.pdbx_auth_comp_id _struct_site.pdbx_auth_seq_id _struct_site.pdbx_auth_ins_code _struct_site.pdbx_num_residues _struct_site.details AC1 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE NAG A 701' AC2 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NAG A 801' AC3 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NDG A 901' AC4 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE SO4 A 301' AC5 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE ACT A 601' AC6 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CL A 1001' AC7 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE BEN A 401' AC8 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE GOL A 501' # 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 5 ARG A 77 ? ARG A 95 . ? 4_546 ? 2 AC1 5 PRO A 128 ? PRO A 147 . ? 1_555 ? 3 AC1 5 ASN A 129 ? ASN A 148 . ? 1_555 ? 4 AC1 5 ALA A 158 ? ALA A 178 . ? 4_546 ? 5 AC1 5 HOH J . ? HOH A 1204 . ? 1_555 ? 6 AC2 2 ASN A 78 A ASN A 96 . ? 1_555 ? 7 AC2 2 HOH J . ? HOH A 1157 . ? 1_555 ? 8 AC3 3 ASN A 21 ? ASN A 38 . ? 1_555 ? 9 AC3 3 ARG A 43 ? ARG A 60 . ? 1_555 ? 10 AC3 3 ASN A 45 ? ASN A 63 . ? 1_555 ? 11 AC4 8 HIS A 40 ? HIS A 57 . ? 1_555 ? 12 AC4 8 ARG A 43 ? ARG A 60 . ? 1_555 ? 13 AC4 8 LYS A 174 ? LYS A 192 . ? 1_555 ? 14 AC4 8 GLY A 175 ? GLY A 193 . ? 1_555 ? 15 AC4 8 SER A 177 ? SER A 195 . ? 1_555 ? 16 AC4 8 BEN H . ? BEN A 401 . ? 1_555 ? 17 AC4 8 HOH J . ? HOH A 1046 . ? 1_555 ? 18 AC4 8 HOH J . ? HOH A 1127 . ? 1_555 ? 19 AC5 5 LEU A 63 ? LEU A 81 . ? 1_555 ? 20 AC5 5 ARG A 65 ? ARG A 83 . ? 1_555 ? 21 AC5 5 ARG A 93 ? ARG A 110 . ? 1_555 ? 22 AC5 5 HOH J . ? HOH A 1031 . ? 4_545 ? 23 AC5 5 HOH J . ? HOH A 1172 . ? 1_555 ? 24 AC6 4 ARG A 64 ? ARG A 82 . ? 4_555 ? 25 AC6 4 LEU A 74 ? LEU A 92 . ? 1_555 ? 26 AC6 4 ASN A 75 ? ASN A 93 . ? 1_555 ? 27 AC6 4 CYS A 229 E CYS A 245 . ? 1_555 ? 28 AC7 8 ASP A 171 ? ASP A 189 . ? 1_555 ? 29 AC7 8 THR A 172 ? THR A 190 . ? 1_555 ? 30 AC7 8 SER A 177 ? SER A 195 . ? 1_555 ? 31 AC7 8 GLY A 194 ? GLY A 216 . ? 1_555 ? 32 AC7 8 GLY A 195 ? GLY A 217 . ? 1_555 ? 33 AC7 8 CYS A 198 ? CYS A 220 . ? 1_555 ? 34 AC7 8 GLY A 205 ? GLY A 226 . ? 1_555 ? 35 AC7 8 SO4 E . ? SO4 A 301 . ? 1_555 ? 36 AC8 6 ARG A 39 ? ARG A 56 . ? 1_555 ? 37 AC8 6 THR A 80 ? THR A 97 . ? 1_555 ? 38 AC8 6 ILE A 81 ? ILE A 98 . ? 1_555 ? 39 AC8 6 TRP A 82 ? TRP A 99 . ? 1_555 ? 40 AC8 6 HOH J . ? HOH A 1034 . ? 1_555 ? 41 AC8 6 HOH J . ? HOH A 1157 . ? 1_555 ? # _database_PDB_matrix.entry_id 2AIQ _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 2AIQ _atom_sites.fract_transf_matrix[1][1] 0.012420 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.002157 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.015757 _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] 0.021050 _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 CL 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 . VAL A 1 1 ? 13.614 -8.541 17.486 1.00 11.14 ? 16 VAL A N 1 ATOM 2 C CA . VAL A 1 1 ? 12.267 -8.506 18.129 1.00 12.09 ? 16 VAL A CA 1 ATOM 3 C C . VAL A 1 1 ? 12.313 -9.406 19.338 1.00 12.70 ? 16 VAL A C 1 ATOM 4 O O . VAL A 1 1 ? 12.736 -10.561 19.241 1.00 12.65 ? 16 VAL A O 1 ATOM 5 C CB . VAL A 1 1 ? 11.167 -9.007 17.163 1.00 11.91 ? 16 VAL A CB 1 ATOM 6 C CG1 . VAL A 1 1 ? 9.818 -9.166 17.865 1.00 11.99 ? 16 VAL A CG1 1 ATOM 7 C CG2 . VAL A 1 1 ? 11.055 -8.073 15.991 1.00 11.98 ? 16 VAL A CG2 1 ATOM 8 N N . ILE A 1 2 ? 11.884 -8.859 20.476 1.00 12.69 ? 17 ILE A N 1 ATOM 9 C CA . ILE A 1 2 ? 11.803 -9.595 21.733 1.00 13.67 ? 17 ILE A CA 1 ATOM 10 C C . ILE A 1 2 ? 10.376 -10.049 21.924 1.00 13.43 ? 17 ILE A C 1 ATOM 11 O O . ILE A 1 2 ? 9.443 -9.285 21.665 1.00 12.75 ? 17 ILE A O 1 ATOM 12 C CB . ILE A 1 2 ? 12.125 -8.677 22.936 1.00 13.39 ? 17 ILE A CB 1 ATOM 13 C CG1 . ILE A 1 2 ? 13.390 -7.831 22.709 1.00 14.04 ? 17 ILE A CG1 1 ATOM 14 C CG2 . ILE A 1 2 ? 12.231 -9.497 24.227 1.00 15.21 ? 17 ILE A CG2 1 ATOM 15 C CD1 . ILE A 1 2 ? 14.667 -8.626 22.500 1.00 15.17 ? 17 ILE A CD1 1 ATOM 16 N N . GLY A 1 3 ? 10.195 -11.273 22.421 1.00 13.94 ? 18 GLY A N 1 ATOM 17 C CA . GLY A 1 3 ? 8.859 -11.729 22.801 1.00 15.04 ? 18 GLY A CA 1 ATOM 18 C C . GLY A 1 3 ? 7.953 -12.175 21.678 1.00 15.43 ? 18 GLY A C 1 ATOM 19 O O . GLY A 1 3 ? 6.750 -12.349 21.878 1.00 16.06 ? 18 GLY A O 1 ATOM 20 N N . GLY A 1 4 ? 8.534 -12.389 20.502 1.00 15.59 ? 19 GLY A N 1 ATOM 21 C CA . GLY A 1 4 ? 7.770 -12.796 19.349 1.00 16.26 ? 19 GLY A CA 1 ATOM 22 C C . GLY A 1 4 ? 8.101 -14.207 18.932 1.00 16.93 ? 19 GLY A C 1 ATOM 23 O O . GLY A 1 4 ? 8.658 -14.993 19.700 1.00 16.81 ? 19 GLY A O 1 ATOM 24 N N . ASP A 1 5 ? 7.739 -14.522 17.697 1.00 17.05 ? 20 ASP A N 1 ATOM 25 C CA . ASP A 1 5 ? 8.017 -15.818 17.130 1.00 17.60 ? 20 ASP A CA 1 ATOM 26 C C . ASP A 1 5 ? 8.498 -15.633 15.706 1.00 16.97 ? 20 ASP A C 1 ATOM 27 O O . ASP A 1 5 ? 8.429 -14.535 15.155 1.00 16.56 ? 20 ASP A O 1 ATOM 28 C CB A ASP A 1 5 ? 6.809 -16.757 17.302 0.50 18.33 ? 20 ASP A CB 1 ATOM 29 C CB B ASP A 1 5 ? 6.725 -16.634 17.010 0.50 17.96 ? 20 ASP A CB 1 ATOM 30 C CG A ASP A 1 5 ? 6.579 -17.168 18.783 0.60 19.99 ? 20 ASP A CG 1 ATOM 31 C CG B ASP A 1 5 ? 5.582 -15.879 16.329 0.40 19.39 ? 20 ASP A CG 1 ATOM 32 O OD1 A ASP A 1 5 ? 7.512 -17.736 19.404 0.60 23.69 ? 20 ASP A OD1 1 ATOM 33 O OD1 B ASP A 1 5 ? 4.458 -16.423 16.310 0.40 22.23 ? 20 ASP A OD1 1 ATOM 34 O OD2 A ASP A 1 5 ? 5.469 -16.922 19.311 0.60 24.77 ? 20 ASP A OD2 1 ATOM 35 O OD2 B ASP A 1 5 ? 5.777 -14.761 15.809 0.40 21.87 ? 20 ASP A OD2 1 ATOM 36 N N . GLU A 1 6 ? 8.970 -16.708 15.098 1.00 16.40 ? 21 GLU A N 1 ATOM 37 C CA . GLU A 1 6 ? 9.306 -16.655 13.699 1.00 15.95 ? 21 GLU A CA 1 ATOM 38 C C . GLU A 1 6 ? 8.117 -16.141 12.890 1.00 15.50 ? 21 GLU A C 1 ATOM 39 O O . GLU A 1 6 ? 6.993 -16.618 13.036 1.00 15.39 ? 21 GLU A O 1 ATOM 40 C CB . GLU A 1 6 ? 9.707 -18.040 13.193 1.00 16.01 ? 21 GLU A CB 1 ATOM 41 C CG . GLU A 1 6 ? 9.899 -18.078 11.680 1.00 17.71 ? 21 GLU A CG 1 ATOM 42 C CD . GLU A 1 6 ? 10.457 -19.392 11.186 1.00 20.22 ? 21 GLU A CD 1 ATOM 43 O OE1 . GLU A 1 6 ? 10.782 -20.255 12.035 1.00 21.26 ? 21 GLU A OE1 1 ATOM 44 O OE2 . GLU A 1 6 ? 10.578 -19.557 9.954 1.00 19.29 ? 21 GLU A OE2 1 ATOM 45 N N . CYS A 1 7 ? 8.368 -15.145 12.049 1.00 14.79 ? 22 CYS A N 1 ATOM 46 C CA . CYS A 1 7 ? 7.350 -14.660 11.134 1.00 14.33 ? 22 CYS A CA 1 ATOM 47 C C . CYS A 1 7 ? 6.904 -15.765 10.208 1.00 14.60 ? 22 CYS A C 1 ATOM 48 O O . CYS A 1 7 ? 7.691 -16.616 9.834 1.00 15.01 ? 22 CYS A O 1 ATOM 49 C CB . CYS A 1 7 ? 7.903 -13.541 10.266 1.00 14.72 ? 22 CYS A CB 1 ATOM 50 S SG . CYS A 1 7 ? 8.466 -12.114 11.171 1.00 14.25 ? 22 CYS A SG 1 ATOM 51 N N . ASN A 1 8 ? 5.650 -15.718 9.792 1.00 15.25 ? 23 ASN A N 1 ATOM 52 C CA . ASN A 1 8 ? 5.234 -16.576 8.699 1.00 15.74 ? 23 ASN A CA 1 ATOM 53 C C . ASN A 1 8 ? 6.048 -16.200 7.461 1.00 15.65 ? 23 ASN A C 1 ATOM 54 O O . ASN A 1 8 ? 6.263 -15.013 7.180 1.00 15.51 ? 23 ASN A O 1 ATOM 55 C CB . ASN A 1 8 ? 3.740 -16.429 8.444 1.00 16.27 ? 23 ASN A CB 1 ATOM 56 C CG . ASN A 1 8 ? 3.253 -17.332 7.350 1.00 19.42 ? 23 ASN A CG 1 ATOM 57 O OD1 . ASN A 1 8 ? 3.370 -17.020 6.168 1.00 19.52 ? 23 ASN A OD1 1 ATOM 58 N ND2 . ASN A 1 8 ? 2.687 -18.465 7.738 1.00 23.44 ? 23 ASN A ND2 1 ATOM 59 N N . ILE A 1 9 ? 6.504 -17.210 6.725 1.00 15.28 ? 24 ILE A N 1 ATOM 60 C CA . ILE A 1 9 ? 7.341 -16.981 5.553 1.00 15.24 ? 24 ILE A CA 1 ATOM 61 C C . ILE A 1 9 ? 6.691 -16.067 4.504 1.00 15.28 ? 24 ILE A C 1 ATOM 62 O O . ILE A 1 9 ? 7.388 -15.459 3.684 1.00 15.10 ? 24 ILE A O 1 ATOM 63 C CB . ILE A 1 9 ? 7.817 -18.330 4.917 1.00 15.43 ? 24 ILE A CB 1 ATOM 64 C CG1 . ILE A 1 9 ? 8.999 -18.081 3.980 1.00 15.81 ? 24 ILE A CG1 1 ATOM 65 C CG2 . ILE A 1 9 ? 6.654 -19.054 4.234 1.00 16.57 ? 24 ILE A CG2 1 ATOM 66 C CD1 . ILE A 1 9 ? 9.883 -19.288 3.737 1.00 16.42 ? 24 ILE A CD1 1 ATOM 67 N N . ASN A 1 10 ? 5.361 -15.961 4.544 1.00 15.67 ? 25 ASN A N 1 ATOM 68 C CA . ASN A 1 10 ? 4.629 -15.214 3.525 1.00 16.21 ? 25 ASN A CA 1 ATOM 69 C C . ASN A 1 10 ? 4.088 -13.879 4.001 1.00 15.74 ? 25 ASN A C 1 ATOM 70 O O . ASN A 1 10 ? 3.452 -13.162 3.225 1.00 16.45 ? 25 ASN A O 1 ATOM 71 C CB . ASN A 1 10 ? 3.473 -16.059 2.983 1.00 17.21 ? 25 ASN A CB 1 ATOM 72 C CG . ASN A 1 10 ? 3.944 -17.382 2.420 1.00 20.54 ? 25 ASN A CG 1 ATOM 73 O OD1 . ASN A 1 10 ? 4.884 -17.432 1.625 1.00 23.68 ? 25 ASN A OD1 1 ATOM 74 N ND2 . ASN A 1 10 ? 3.316 -18.467 2.855 1.00 24.27 ? 25 ASN A ND2 1 ATOM 75 N N . GLU A 1 11 ? 4.341 -13.546 5.263 1.00 15.48 ? 26 GLU A N 1 ATOM 76 C CA . GLU A 1 11 ? 3.675 -12.387 5.849 1.00 15.07 ? 26 GLU A CA 1 ATOM 77 C C . GLU A 1 11 ? 4.521 -11.131 5.790 1.00 14.69 ? 26 GLU A C 1 ATOM 78 O O . GLU A 1 11 ? 4.130 -10.099 6.328 1.00 15.23 ? 26 GLU A O 1 ATOM 79 C CB . GLU A 1 11 ? 3.255 -12.659 7.295 1.00 15.59 ? 26 GLU A CB 1 ATOM 80 C CG . GLU A 1 11 ? 4.392 -12.607 8.314 1.00 16.86 ? 26 GLU A CG 1 ATOM 81 C CD . GLU A 1 11 ? 3.859 -12.499 9.727 1.00 19.34 ? 26 GLU A CD 1 ATOM 82 O OE1 . GLU A 1 11 ? 3.242 -11.445 10.049 1.00 20.02 ? 26 GLU A OE1 1 ATOM 83 O OE2 . GLU A 1 11 ? 4.043 -13.459 10.496 1.00 19.17 ? 26 GLU A OE2 1 ATOM 84 N N . HIS A 1 12 ? 5.670 -11.202 5.125 1.00 13.60 ? 27 HIS A N 1 ATOM 85 C CA . HIS A 1 12 ? 6.591 -10.079 5.160 1.00 12.34 ? 27 HIS A CA 1 ATOM 86 C C . HIS A 1 12 ? 7.240 -9.844 3.807 1.00 11.55 ? 27 HIS A C 1 ATOM 87 O O . HIS A 1 12 ? 8.444 -9.609 3.704 1.00 10.40 ? 27 HIS A O 1 ATOM 88 C CB . HIS A 1 12 ? 7.607 -10.257 6.289 1.00 12.29 ? 27 HIS A CB 1 ATOM 89 C CG . HIS A 1 12 ? 8.458 -11.480 6.156 1.00 11.74 ? 27 HIS A CG 1 ATOM 90 N ND1 . HIS A 1 12 ? 9.579 -11.508 5.354 1.00 11.89 ? 27 HIS A ND1 1 ATOM 91 C CD2 . HIS A 1 12 ? 8.376 -12.697 6.742 1.00 12.60 ? 27 HIS A CD2 1 ATOM 92 C CE1 . HIS A 1 12 ? 10.136 -12.704 5.431 1.00 11.48 ? 27 HIS A CE1 1 ATOM 93 N NE2 . HIS A 1 12 ? 9.438 -13.437 6.282 1.00 12.35 ? 27 HIS A NE2 1 ATOM 94 N N . ARG A 1 13 ? 6.423 -9.885 2.760 1.00 10.72 ? 28 ARG A N 1 ATOM 95 C CA . ARG A 1 13 ? 6.960 -9.837 1.415 1.00 10.94 ? 28 ARG A CA 1 ATOM 96 C C . ARG A 1 13 ? 7.596 -8.485 1.095 1.00 10.40 ? 28 ARG A C 1 ATOM 97 O O . ARG A 1 13 ? 8.373 -8.362 0.168 1.00 10.99 ? 28 ARG A O 1 ATOM 98 C CB . ARG A 1 13 ? 5.885 -10.211 0.418 1.00 11.98 ? 28 ARG A CB 1 ATOM 99 C CG . ARG A 1 13 ? 5.475 -11.666 0.587 1.00 13.22 ? 28 ARG A CG 1 ATOM 100 C CD . ARG A 1 13 ? 4.191 -11.922 -0.182 1.00 17.55 ? 28 ARG A CD 1 ATOM 101 N NE . ARG A 1 13 ? 4.388 -11.917 -1.617 1.00 18.24 ? 28 ARG A NE 1 ATOM 102 C CZ . ARG A 1 13 ? 3.498 -11.453 -2.498 1.00 18.14 ? 28 ARG A CZ 1 ATOM 103 N NH1 . ARG A 1 13 ? 3.754 -11.511 -3.793 1.00 17.94 ? 28 ARG A NH1 1 ATOM 104 N NH2 . ARG A 1 13 ? 2.366 -10.895 -2.089 1.00 20.38 ? 28 ARG A NH2 1 ATOM 105 N N . PHE A 1 14 ? 7.249 -7.480 1.891 1.00 10.26 ? 29 PHE A N 1 ATOM 106 C CA . PHE A 1 14 ? 7.730 -6.115 1.712 1.00 10.11 ? 29 PHE A CA 1 ATOM 107 C C . PHE A 1 14 ? 8.949 -5.855 2.598 1.00 9.79 ? 29 PHE A C 1 ATOM 108 O O . PHE A 1 14 ? 9.550 -4.781 2.541 1.00 10.10 ? 29 PHE A O 1 ATOM 109 C CB . PHE A 1 14 ? 6.621 -5.159 2.149 1.00 9.89 ? 29 PHE A CB 1 ATOM 110 C CG . PHE A 1 14 ? 5.991 -5.574 3.430 1.00 9.69 ? 29 PHE A CG 1 ATOM 111 C CD1 . PHE A 1 14 ? 6.611 -5.295 4.638 1.00 10.37 ? 29 PHE A CD1 1 ATOM 112 C CD2 . PHE A 1 14 ? 4.824 -6.328 3.430 1.00 10.38 ? 29 PHE A CD2 1 ATOM 113 C CE1 . PHE A 1 14 ? 6.066 -5.732 5.827 1.00 10.48 ? 29 PHE A CE1 1 ATOM 114 C CE2 . PHE A 1 14 ? 4.271 -6.775 4.621 1.00 10.96 ? 29 PHE A CE2 1 ATOM 115 C CZ . PHE A 1 14 ? 4.879 -6.468 5.827 1.00 11.00 ? 29 PHE A CZ 1 ATOM 116 N N . LEU A 1 15 ? 9.327 -6.830 3.421 1.00 9.57 ? 30 LEU A N 1 ATOM 117 C CA . LEU A 1 15 ? 10.379 -6.594 4.392 1.00 9.47 ? 30 LEU A CA 1 ATOM 118 C C . LEU A 1 15 ? 11.739 -6.745 3.749 1.00 9.66 ? 30 LEU A C 1 ATOM 119 O O . LEU A 1 15 ? 12.051 -7.792 3.147 1.00 9.31 ? 30 LEU A O 1 ATOM 120 C CB . LEU A 1 15 ? 10.231 -7.556 5.574 1.00 8.91 ? 30 LEU A CB 1 ATOM 121 C CG . LEU A 1 15 ? 11.304 -7.474 6.654 1.00 8.58 ? 30 LEU A CG 1 ATOM 122 C CD1 . LEU A 1 15 ? 11.228 -6.154 7.411 1.00 9.29 ? 30 LEU A CD1 1 ATOM 123 C CD2 . LEU A 1 15 ? 11.102 -8.628 7.597 1.00 9.39 ? 30 LEU A CD2 1 ATOM 124 N N . ALA A 1 16 ? 12.531 -5.694 3.877 1.00 9.14 ? 31 ALA A N 1 ATOM 125 C CA . ALA A 1 16 ? 13.878 -5.675 3.352 1.00 9.84 ? 31 ALA A CA 1 ATOM 126 C C . ALA A 1 16 ? 14.849 -5.914 4.484 1.00 10.39 ? 31 ALA A C 1 ATOM 127 O O . ALA A 1 16 ? 14.604 -5.506 5.609 1.00 10.00 ? 31 ALA A O 1 ATOM 128 C CB . ALA A 1 16 ? 14.158 -4.315 2.688 1.00 10.53 ? 31 ALA A CB 1 ATOM 129 N N . LEU A 1 17 ? 15.955 -6.564 4.150 1.00 10.85 ? 32 LEU A N 1 ATOM 130 C CA . LEU A 1 17 ? 17.042 -6.772 5.072 1.00 11.60 ? 32 LEU A CA 1 ATOM 131 C C . LEU A 1 17 ? 18.140 -5.823 4.632 1.00 12.29 ? 32 LEU A C 1 ATOM 132 O O . LEU A 1 17 ? 18.587 -5.880 3.495 1.00 11.86 ? 32 LEU A O 1 ATOM 133 C CB . LEU A 1 17 ? 17.519 -8.214 4.969 1.00 11.86 ? 32 LEU A CB 1 ATOM 134 C CG . LEU A 1 17 ? 18.811 -8.573 5.692 1.00 14.18 ? 32 LEU A CG 1 ATOM 135 C CD1 . LEU A 1 17 ? 18.653 -8.490 7.197 1.00 17.16 ? 32 LEU A CD1 1 ATOM 136 C CD2 . LEU A 1 17 ? 19.147 -9.986 5.284 1.00 14.52 ? 32 LEU A CD2 1 ATOM 137 N N . VAL A 1 18 ? 18.565 -4.946 5.538 1.00 13.04 ? 33 VAL A N 1 ATOM 138 C CA . VAL A 1 18 ? 19.519 -3.918 5.185 1.00 14.64 ? 33 VAL A CA 1 ATOM 139 C C . VAL A 1 18 ? 20.798 -4.167 5.978 1.00 15.97 ? 33 VAL A C 1 ATOM 140 O O . VAL A 1 18 ? 20.777 -4.234 7.205 1.00 17.45 ? 33 VAL A O 1 ATOM 141 C CB . VAL A 1 18 ? 18.954 -2.514 5.471 1.00 14.41 ? 33 VAL A CB 1 ATOM 142 C CG1 . VAL A 1 18 ? 19.976 -1.441 5.129 1.00 14.96 ? 33 VAL A CG1 1 ATOM 143 C CG2 . VAL A 1 18 ? 17.673 -2.285 4.687 1.00 15.13 ? 33 VAL A CG2 1 ATOM 144 N N . TYR A 1 19 ? 21.901 -4.344 5.267 1.00 16.60 ? 34 TYR A N 1 ATOM 145 C CA . TYR A 1 19 ? 23.194 -4.472 5.921 1.00 17.42 ? 34 TYR A CA 1 ATOM 146 C C . TYR A 1 19 ? 24.025 -3.280 5.522 1.00 17.65 ? 34 TYR A C 1 ATOM 147 O O . TYR A 1 19 ? 24.046 -2.913 4.361 1.00 18.25 ? 34 TYR A O 1 ATOM 148 C CB . TYR A 1 19 ? 23.924 -5.734 5.474 1.00 18.79 ? 34 TYR A CB 1 ATOM 149 C CG . TYR A 1 19 ? 23.449 -7.014 6.103 1.00 20.00 ? 34 TYR A CG 1 ATOM 150 C CD1 . TYR A 1 19 ? 23.338 -7.146 7.489 1.00 21.49 ? 34 TYR A CD1 1 ATOM 151 C CD2 . TYR A 1 19 ? 23.141 -8.113 5.314 1.00 22.66 ? 34 TYR A CD2 1 ATOM 152 C CE1 . TYR A 1 19 ? 22.909 -8.333 8.059 1.00 21.22 ? 34 TYR A CE1 1 ATOM 153 C CE2 . TYR A 1 19 ? 22.721 -9.303 5.873 1.00 22.44 ? 34 TYR A CE2 1 ATOM 154 C CZ . TYR A 1 19 ? 22.604 -9.411 7.241 1.00 22.14 ? 34 TYR A CZ 1 ATOM 155 O OH . TYR A 1 19 ? 22.181 -10.605 7.781 1.00 23.58 ? 34 TYR A OH 1 ATOM 156 N N . ALA A 1 20 ? 24.694 -2.665 6.481 1.00 18.00 ? 36 ALA A N 1 ATOM 157 C CA . ALA A 1 20 ? 25.616 -1.581 6.177 1.00 19.22 ? 36 ALA A CA 1 ATOM 158 C C . ALA A 1 20 ? 26.784 -1.738 7.129 1.00 20.82 ? 36 ALA A C 1 ATOM 159 O O . ALA A 1 20 ? 26.684 -2.508 8.073 1.00 22.18 ? 36 ALA A O 1 ATOM 160 C CB . ALA A 1 20 ? 24.939 -0.242 6.346 1.00 18.16 ? 36 ALA A CB 1 ATOM 161 N N . ASN A 1 21 ? 27.894 -1.062 6.853 0.70 22.58 ? 38 ASN A N 1 ATOM 162 C CA . ASN A 1 21 ? 29.112 -1.183 7.659 0.70 23.91 ? 38 ASN A CA 1 ATOM 163 C C . ASN A 1 21 ? 28.825 -1.382 9.142 0.70 24.36 ? 38 ASN A C 1 ATOM 164 O O . ASN A 1 21 ? 28.416 -0.450 9.844 0.70 24.90 ? 38 ASN A O 1 ATOM 165 C CB . ASN A 1 21 ? 30.030 0.024 7.431 0.50 24.51 ? 38 ASN A CB 1 ATOM 166 C CG . ASN A 1 21 ? 31.360 -0.093 8.165 0.50 26.90 ? 38 ASN A CG 1 ATOM 167 O OD1 . ASN A 1 21 ? 31.404 -0.393 9.358 0.50 27.39 ? 38 ASN A OD1 1 ATOM 168 N ND2 . ASN A 1 21 ? 32.451 0.162 7.452 0.50 31.59 ? 38 ASN A ND2 1 ATOM 169 N N . GLY A 1 22 ? 29.020 -2.618 9.591 0.70 24.26 ? 39 GLY A N 1 ATOM 170 C CA . GLY A 1 22 ? 28.867 -2.996 10.991 0.70 24.50 ? 39 GLY A CA 1 ATOM 171 C C . GLY A 1 22 ? 27.445 -2.908 11.505 0.70 24.41 ? 39 GLY A C 1 ATOM 172 O O . GLY A 1 22 ? 27.222 -2.597 12.675 0.70 25.26 ? 39 GLY A O 1 ATOM 173 N N . SER A 1 23 ? 26.467 -3.187 10.645 1.00 23.96 ? 40 SER A N 1 ATOM 174 C CA . SER A 1 23 ? 25.093 -2.912 11.036 1.00 22.51 ? 40 SER A CA 1 ATOM 175 C C . SER A 1 23 ? 24.005 -3.676 10.306 1.00 21.16 ? 40 SER A C 1 ATOM 176 O O . SER A 1 23 ? 24.059 -3.884 9.107 1.00 21.62 ? 40 SER A O 1 ATOM 177 C CB . SER A 1 23 ? 24.813 -1.430 10.882 1.00 23.00 ? 40 SER A CB 1 ATOM 178 O OG . SER A 1 23 ? 24.897 -1.037 9.528 0.50 24.13 ? 40 SER A OG 1 ATOM 179 N N . LEU A 1 24 ? 22.991 -4.042 11.070 1.00 19.06 ? 41 LEU A N 1 ATOM 180 C CA . LEU A 1 24 ? 21.820 -4.739 10.575 1.00 17.00 ? 41 LEU A CA 1 ATOM 181 C C . LEU A 1 24 ? 20.617 -3.832 10.779 1.00 14.84 ? 41 LEU A C 1 ATOM 182 O O . LEU A 1 24 ? 20.472 -3.186 11.817 1.00 14.49 ? 41 LEU A O 1 ATOM 183 C CB . LEU A 1 24 ? 21.639 -6.029 11.368 1.00 18.09 ? 41 LEU A CB 1 ATOM 184 C CG . LEU A 1 24 ? 20.309 -6.773 11.348 1.00 17.33 ? 41 LEU A CG 1 ATOM 185 C CD1 . LEU A 1 24 ? 20.029 -7.379 9.973 1.00 19.71 ? 41 LEU A CD1 1 ATOM 186 C CD2 . LEU A 1 24 ? 20.301 -7.851 12.416 1.00 18.88 ? 41 LEU A CD2 1 ATOM 187 N N . CYS A 1 25 ? 19.779 -3.764 9.762 1.00 13.13 ? 42 CYS A N 1 ATOM 188 C CA . CYS A 1 25 ? 18.521 -3.044 9.858 1.00 11.64 ? 42 CYS A CA 1 ATOM 189 C C . CYS A 1 25 ? 17.503 -3.744 9.001 1.00 10.88 ? 42 CYS A C 1 ATOM 190 O O . CYS A 1 25 ? 17.837 -4.581 8.164 1.00 11.73 ? 42 CYS A O 1 ATOM 191 C CB . CYS A 1 25 ? 18.673 -1.625 9.335 1.00 11.36 ? 42 CYS A CB 1 ATOM 192 S SG . CYS A 1 25 ? 19.382 -0.507 10.542 1.00 14.09 ? 42 CYS A SG 1 ATOM 193 N N . GLY A 1 26 ? 16.258 -3.351 9.189 1.00 9.68 ? 43 GLY A N 1 ATOM 194 C CA . GLY A 1 26 ? 15.219 -3.699 8.261 1.00 9.45 ? 43 GLY A CA 1 ATOM 195 C C . GLY A 1 26 ? 14.910 -2.523 7.362 1.00 9.53 ? 43 GLY A C 1 ATOM 196 O O . GLY A 1 26 ? 15.504 -1.443 7.467 1.00 9.55 ? 43 GLY A O 1 ATOM 197 N N . GLY A 1 27 ? 13.976 -2.757 6.453 1.00 9.15 ? 44 GLY A N 1 ATOM 198 C CA . GLY A 1 27 ? 13.465 -1.710 5.591 1.00 9.08 ? 44 GLY A CA 1 ATOM 199 C C . GLY A 1 27 ? 12.183 -2.224 4.972 1.00 8.40 ? 44 GLY A C 1 ATOM 200 O O . GLY A 1 27 ? 11.782 -3.369 5.205 1.00 9.18 ? 44 GLY A O 1 ATOM 201 N N . THR A 1 28 ? 11.545 -1.373 4.181 1.00 8.77 ? 45 THR A N 1 ATOM 202 C CA . THR A 1 28 ? 10.252 -1.718 3.607 1.00 9.12 ? 45 THR A CA 1 ATOM 203 C C . THR A 1 28 ? 10.274 -1.357 2.153 1.00 9.38 ? 45 THR A C 1 ATOM 204 O O . THR A 1 28 ? 10.550 -0.228 1.785 1.00 9.59 ? 45 THR A O 1 ATOM 205 C CB . THR A 1 28 ? 9.117 -0.967 4.297 1.00 8.27 ? 45 THR A CB 1 ATOM 206 O OG1 . THR A 1 28 ? 9.163 -1.260 5.701 1.00 9.43 ? 45 THR A OG1 1 ATOM 207 C CG2 . THR A 1 28 ? 7.746 -1.387 3.726 1.00 9.20 ? 45 THR A CG2 1 ATOM 208 N N . LEU A 1 29 ? 9.969 -2.349 1.328 1.00 9.87 ? 46 LEU A N 1 ATOM 209 C CA . LEU A 1 29 ? 9.813 -2.149 -0.092 1.00 10.05 ? 46 LEU A CA 1 ATOM 210 C C . LEU A 1 29 ? 8.464 -1.477 -0.317 1.00 10.26 ? 46 LEU A C 1 ATOM 211 O O . LEU A 1 29 ? 7.444 -2.064 -0.017 1.00 10.48 ? 46 LEU A O 1 ATOM 212 C CB . LEU A 1 29 ? 9.874 -3.524 -0.774 1.00 10.19 ? 46 LEU A CB 1 ATOM 213 C CG . LEU A 1 29 ? 9.843 -3.538 -2.289 1.00 11.10 ? 46 LEU A CG 1 ATOM 214 C CD1 . LEU A 1 29 ? 11.179 -3.039 -2.852 1.00 11.67 ? 46 LEU A CD1 1 ATOM 215 C CD2 . LEU A 1 29 ? 9.520 -4.956 -2.750 1.00 11.46 ? 46 LEU A CD2 1 ATOM 216 N N . ILE A 1 30 ? 8.478 -0.240 -0.798 1.00 10.49 ? 47 ILE A N 1 ATOM 217 C CA . ILE A 1 30 ? 7.229 0.511 -0.975 1.00 10.95 ? 47 ILE A CA 1 ATOM 218 C C . ILE A 1 30 ? 6.705 0.504 -2.395 1.00 11.65 ? 47 ILE A C 1 ATOM 219 O O . ILE A 1 30 ? 5.559 0.876 -2.652 1.00 12.59 ? 47 ILE A O 1 ATOM 220 C CB . ILE A 1 30 ? 7.307 1.960 -0.448 1.00 11.14 ? 47 ILE A CB 1 ATOM 221 C CG1 . ILE A 1 30 ? 8.434 2.738 -1.131 1.00 10.33 ? 47 ILE A CG1 1 ATOM 222 C CG2 . ILE A 1 30 ? 7.463 1.950 1.069 1.00 11.79 ? 47 ILE A CG2 1 ATOM 223 C CD1 . ILE A 1 30 ? 8.286 4.271 -0.983 1.00 11.79 ? 47 ILE A CD1 1 ATOM 224 N N . ASN A 1 31 ? 7.564 0.094 -3.323 1.00 12.14 ? 48 ASN A N 1 ATOM 225 C CA . ASN A 1 31 ? 7.147 -0.169 -4.671 1.00 12.56 ? 48 ASN A CA 1 ATOM 226 C C . ASN A 1 31 ? 8.248 -1.032 -5.245 1.00 12.52 ? 48 ASN A C 1 ATOM 227 O O . ASN A 1 31 ? 9.095 -1.523 -4.492 1.00 13.39 ? 48 ASN A O 1 ATOM 228 C CB . ASN A 1 31 ? 6.943 1.142 -5.432 1.00 12.64 ? 48 ASN A CB 1 ATOM 229 C CG . ASN A 1 31 ? 8.183 1.989 -5.451 1.00 14.06 ? 48 ASN A CG 1 ATOM 230 O OD1 . ASN A 1 31 ? 9.267 1.490 -5.700 1.00 12.16 ? 48 ASN A OD1 1 ATOM 231 N ND2 . ASN A 1 31 ? 8.034 3.293 -5.175 1.00 16.14 ? 48 ASN A ND2 1 ATOM 232 N N . GLN A 1 32 ? 8.263 -1.236 -6.549 1.00 12.69 ? 49 GLN A N 1 ATOM 233 C CA . GLN A 1 32 ? 9.214 -2.207 -7.074 1.00 12.89 ? 49 GLN A CA 1 ATOM 234 C C . GLN A 1 32 ? 10.645 -1.721 -7.179 1.00 12.81 ? 49 GLN A C 1 ATOM 235 O O . GLN A 1 32 ? 11.529 -2.484 -7.527 1.00 12.89 ? 49 GLN A O 1 ATOM 236 C CB . GLN A 1 32 ? 8.701 -2.803 -8.373 1.00 13.55 ? 49 GLN A CB 1 ATOM 237 C CG . GLN A 1 32 ? 7.508 -3.709 -8.076 1.00 14.46 ? 49 GLN A CG 1 ATOM 238 C CD . GLN A 1 32 ? 6.941 -4.415 -9.294 1.00 15.05 ? 49 GLN A CD 1 ATOM 239 O OE1 . GLN A 1 32 ? 7.282 -4.087 -10.424 1.00 17.44 ? 49 GLN A OE1 1 ATOM 240 N NE2 . GLN A 1 32 ? 6.083 -5.403 -9.058 1.00 18.71 ? 49 GLN A NE2 1 ATOM 241 N N . GLU A 1 33 ? 10.886 -0.471 -6.803 1.00 12.34 ? 50 GLU A N 1 ATOM 242 C CA . GLU A 1 33 ? 12.217 0.091 -6.951 1.00 12.45 ? 50 GLU A CA 1 ATOM 243 C C . GLU A 1 33 ? 12.678 0.885 -5.753 1.00 11.32 ? 50 GLU A C 1 ATOM 244 O O . GLU A 1 33 ? 13.772 1.434 -5.780 1.00 10.61 ? 50 GLU A O 1 ATOM 245 C CB . GLU A 1 33 ? 12.256 1.032 -8.159 1.00 13.84 ? 50 GLU A CB 1 ATOM 246 C CG . GLU A 1 33 ? 12.305 0.350 -9.450 1.00 18.13 ? 50 GLU A CG 1 ATOM 247 C CD . GLU A 1 33 ? 12.547 1.323 -10.556 1.00 20.00 ? 50 GLU A CD 1 ATOM 248 O OE1 . GLU A 1 33 ? 13.549 2.073 -10.486 1.00 17.10 ? 50 GLU A OE1 1 ATOM 249 O OE2 . GLU A 1 33 ? 11.743 1.311 -11.501 1.00 22.20 ? 50 GLU A OE2 1 ATOM 250 N N . TRP A 1 34 ? 11.853 0.973 -4.713 1.00 9.86 ? 51 TRP A N 1 ATOM 251 C CA . TRP A 1 34 ? 12.170 1.895 -3.630 1.00 9.95 ? 51 TRP A CA 1 ATOM 252 C C . TRP A 1 34 ? 11.947 1.272 -2.271 1.00 9.43 ? 51 TRP A C 1 ATOM 253 O O . TRP A 1 34 ? 10.981 0.534 -2.060 1.00 9.37 ? 51 TRP A O 1 ATOM 254 C CB . TRP A 1 34 ? 11.314 3.147 -3.716 1.00 10.20 ? 51 TRP A CB 1 ATOM 255 C CG . TRP A 1 34 ? 11.577 4.028 -4.913 1.00 9.77 ? 51 TRP A CG 1 ATOM 256 C CD1 . TRP A 1 34 ? 11.126 3.846 -6.202 1.00 10.33 ? 51 TRP A CD1 1 ATOM 257 C CD2 . TRP A 1 34 ? 12.321 5.253 -4.922 1.00 10.60 ? 51 TRP A CD2 1 ATOM 258 N NE1 . TRP A 1 34 ? 11.556 4.879 -7.004 1.00 9.50 ? 51 TRP A NE1 1 ATOM 259 C CE2 . TRP A 1 34 ? 12.284 5.757 -6.243 1.00 10.98 ? 51 TRP A CE2 1 ATOM 260 C CE3 . TRP A 1 34 ? 13.009 5.975 -3.937 1.00 11.53 ? 51 TRP A CE3 1 ATOM 261 C CZ2 . TRP A 1 34 ? 12.903 6.950 -6.601 1.00 10.12 ? 51 TRP A CZ2 1 ATOM 262 C CZ3 . TRP A 1 34 ? 13.633 7.165 -4.296 1.00 10.36 ? 51 TRP A CZ3 1 ATOM 263 C CH2 . TRP A 1 34 ? 13.565 7.642 -5.617 1.00 10.32 ? 51 TRP A CH2 1 ATOM 264 N N . VAL A 1 35 ? 12.854 1.580 -1.351 1.00 9.59 ? 52 VAL A N 1 ATOM 265 C CA . VAL A 1 35 ? 12.814 1.072 -0.001 1.00 9.30 ? 52 VAL A CA 1 ATOM 266 C C . VAL A 1 35 ? 12.874 2.234 0.972 1.00 9.27 ? 52 VAL A C 1 ATOM 267 O O . VAL A 1 35 ? 13.626 3.183 0.774 1.00 9.69 ? 52 VAL A O 1 ATOM 268 C CB . VAL A 1 35 ? 14.004 0.116 0.250 1.00 9.44 ? 52 VAL A CB 1 ATOM 269 C CG1 . VAL A 1 35 ? 14.221 -0.151 1.735 1.00 10.47 ? 52 VAL A CG1 1 ATOM 270 C CG2 . VAL A 1 35 ? 13.769 -1.197 -0.494 1.00 10.34 ? 52 VAL A CG2 1 ATOM 271 N N . LEU A 1 36 ? 12.069 2.144 2.024 1.00 8.06 ? 53 LEU A N 1 ATOM 272 C CA . LEU A 1 36 ? 12.162 3.059 3.142 1.00 8.69 ? 53 LEU A CA 1 ATOM 273 C C . LEU A 1 36 ? 12.815 2.351 4.308 1.00 9.01 ? 53 LEU A C 1 ATOM 274 O O . LEU A 1 36 ? 12.457 1.238 4.670 1.00 9.75 ? 53 LEU A O 1 ATOM 275 C CB . LEU A 1 36 ? 10.773 3.512 3.567 1.00 8.93 ? 53 LEU A CB 1 ATOM 276 C CG . LEU A 1 36 ? 10.234 4.700 2.782 1.00 11.00 ? 53 LEU A CG 1 ATOM 277 C CD1 . LEU A 1 36 ? 8.786 4.887 3.179 1.00 12.92 ? 53 LEU A CD1 1 ATOM 278 C CD2 . LEU A 1 36 ? 11.031 5.979 3.047 1.00 9.92 ? 53 LEU A CD2 1 ATOM 279 N N . THR A 1 37 ? 13.763 3.039 4.921 1.00 9.23 ? 54 THR A N 1 ATOM 280 C CA . THR A 1 37 ? 14.426 2.522 6.105 1.00 9.38 ? 54 THR A CA 1 ATOM 281 C C . THR A 1 37 ? 14.707 3.707 7.033 1.00 9.30 ? 54 THR A C 1 ATOM 282 O O . THR A 1 37 ? 14.152 4.791 6.813 1.00 9.62 ? 54 THR A O 1 ATOM 283 C CB . THR A 1 37 ? 15.695 1.698 5.739 1.00 9.99 ? 54 THR A CB 1 ATOM 284 O OG1 . THR A 1 37 ? 16.216 1.080 6.914 1.00 9.90 ? 54 THR A OG1 1 ATOM 285 C CG2 . THR A 1 37 ? 16.775 2.564 5.103 1.00 9.95 ? 54 THR A CG2 1 ATOM 286 N N . ALA A 1 38 ? 15.503 3.495 8.077 1.00 9.81 ? 55 ALA A N 1 ATOM 287 C CA . ALA A 1 38 ? 15.849 4.565 9.003 1.00 9.44 ? 55 ALA A CA 1 ATOM 288 C C . ALA A 1 38 ? 17.139 5.181 8.513 1.00 10.14 ? 55 ALA A C 1 ATOM 289 O O . ALA A 1 38 ? 18.020 4.471 8.061 1.00 10.59 ? 55 ALA A O 1 ATOM 290 C CB . ALA A 1 38 ? 16.035 4.006 10.397 1.00 9.58 ? 55 ALA A CB 1 ATOM 291 N N . ARG A 1 39 ? 17.269 6.501 8.598 1.00 10.77 ? 56 ARG A N 1 ATOM 292 C CA . ARG A 1 39 ? 18.497 7.091 8.111 1.00 11.68 ? 56 ARG A CA 1 ATOM 293 C C . ARG A 1 39 ? 19.685 6.651 8.949 1.00 12.00 ? 56 ARG A C 1 ATOM 294 O O . ARG A 1 39 ? 20.789 6.582 8.438 1.00 13.42 ? 56 ARG A O 1 ATOM 295 C CB . ARG A 1 39 ? 18.404 8.607 8.016 1.00 12.36 ? 56 ARG A CB 1 ATOM 296 C CG . ARG A 1 39 ? 18.327 9.321 9.312 1.00 13.33 ? 56 ARG A CG 1 ATOM 297 C CD . ARG A 1 39 ? 18.243 10.830 9.056 1.00 17.50 ? 56 ARG A CD 1 ATOM 298 N NE . ARG A 1 39 ? 17.967 11.536 10.297 1.00 17.07 ? 56 ARG A NE 1 ATOM 299 C CZ . ARG A 1 39 ? 18.911 11.961 11.128 1.00 17.90 ? 56 ARG A CZ 1 ATOM 300 N NH1 . ARG A 1 39 ? 20.198 11.793 10.828 1.00 19.93 ? 56 ARG A NH1 1 ATOM 301 N NH2 . ARG A 1 39 ? 18.566 12.575 12.244 1.00 17.61 ? 56 ARG A NH2 1 ATOM 302 N N . HIS A 1 40 ? 19.463 6.308 10.215 1.00 12.18 ? 57 HIS A N 1 ATOM 303 C CA . HIS A 1 40 ? 20.600 5.876 11.028 1.00 12.51 ? 57 HIS A CA 1 ATOM 304 C C . HIS A 1 40 ? 21.170 4.538 10.596 1.00 12.97 ? 57 HIS A C 1 ATOM 305 O O . HIS A 1 40 ? 22.255 4.132 11.040 1.00 13.45 ? 57 HIS A O 1 ATOM 306 C CB . HIS A 1 40 ? 20.310 5.913 12.530 1.00 12.39 ? 57 HIS A CB 1 ATOM 307 C CG . HIS A 1 40 ? 19.634 4.693 13.065 1.00 11.57 ? 57 HIS A CG 1 ATOM 308 N ND1 . HIS A 1 40 ? 18.322 4.703 13.479 1.00 12.39 ? 57 HIS A ND1 1 ATOM 309 C CD2 . HIS A 1 40 ? 20.103 3.452 13.326 1.00 13.22 ? 57 HIS A CD2 1 ATOM 310 C CE1 . HIS A 1 40 ? 17.999 3.508 13.939 1.00 11.54 ? 57 HIS A CE1 1 ATOM 311 N NE2 . HIS A 1 40 ? 19.061 2.727 13.856 1.00 12.03 ? 57 HIS A NE2 1 ATOM 312 N N . CYS A 1 41 ? 20.447 3.854 9.715 1.00 13.73 ? 58 CYS A N 1 ATOM 313 C CA . CYS A 1 41 ? 20.893 2.582 9.213 1.00 14.86 ? 58 CYS A CA 1 ATOM 314 C C . CYS A 1 41 ? 21.922 2.759 8.126 1.00 15.99 ? 58 CYS A C 1 ATOM 315 O O . CYS A 1 41 ? 22.545 1.787 7.719 1.00 16.11 ? 58 CYS A O 1 ATOM 316 C CB . CYS A 1 41 ? 19.717 1.801 8.655 1.00 14.90 ? 58 CYS A CB 1 ATOM 317 S SG . CYS A 1 41 ? 18.610 1.278 9.958 1.00 15.07 ? 58 CYS A SG 1 ATOM 318 N N . ASP A 1 42 ? 22.088 3.988 7.649 1.00 17.22 ? 59 ASP A N 1 ATOM 319 C CA . ASP A 1 42 ? 23.045 4.232 6.582 1.00 18.90 ? 59 ASP A CA 1 ATOM 320 C C . ASP A 1 42 ? 24.438 4.392 7.150 1.00 19.39 ? 59 ASP A C 1 ATOM 321 O O . ASP A 1 42 ? 24.921 5.508 7.338 1.00 19.93 ? 59 ASP A O 1 ATOM 322 C CB . ASP A 1 42 ? 22.673 5.453 5.763 1.00 18.87 ? 59 ASP A CB 1 ATOM 323 C CG . ASP A 1 42 ? 23.538 5.591 4.526 1.00 21.44 ? 59 ASP A CG 1 ATOM 324 O OD1 . ASP A 1 42 ? 24.352 4.668 4.253 1.00 25.09 ? 59 ASP A OD1 1 ATOM 325 O OD2 . ASP A 1 42 ? 23.428 6.632 3.864 1.00 25.41 ? 59 ASP A OD2 1 ATOM 326 N N . ARG A 1 43 ? 25.077 3.260 7.402 1.00 20.25 ? 60 ARG A N 1 ATOM 327 C CA . ARG A 1 43 ? 26.371 3.251 8.061 1.00 21.48 ? 60 ARG A CA 1 ATOM 328 C C . ARG A 1 43 ? 27.504 2.939 7.074 1.00 21.93 ? 60 ARG A C 1 ATOM 329 O O . ARG A 1 43 ? 28.654 2.753 7.473 1.00 22.38 ? 60 ARG A O 1 ATOM 330 C CB . ARG A 1 43 ? 26.331 2.272 9.236 1.00 21.64 ? 60 ARG A CB 1 ATOM 331 C CG . ARG A 1 43 ? 25.412 2.735 10.390 1.00 23.72 ? 60 ARG A CG 1 ATOM 332 C CD . ARG A 1 43 ? 25.135 1.586 11.363 1.00 28.15 ? 60 ARG A CD 1 ATOM 333 N NE . ARG A 1 43 ? 24.503 1.991 12.622 1.00 30.25 ? 60 ARG A NE 1 ATOM 334 C CZ . ARG A 1 43 ? 23.358 1.502 13.113 1.00 30.58 ? 60 ARG A CZ 1 ATOM 335 N NH1 . ARG A 1 43 ? 22.907 1.955 14.276 1.00 31.15 ? 60 ARG A NH1 1 ATOM 336 N NH2 . ARG A 1 43 ? 22.663 0.569 12.466 1.00 29.18 ? 60 ARG A NH2 1 ATOM 337 N N . GLY A 1 44 ? 27.170 2.915 5.785 1.00 22.44 ? 62 GLY A N 1 ATOM 338 C CA . GLY A 1 44 ? 28.162 2.721 4.724 1.00 22.14 ? 62 GLY A CA 1 ATOM 339 C C . GLY A 1 44 ? 28.085 1.354 4.078 1.00 22.21 ? 62 GLY A C 1 ATOM 340 O O . GLY A 1 44 ? 27.756 0.371 4.738 1.00 22.55 ? 62 GLY A O 1 ATOM 341 N N . ASN A 1 45 ? 28.408 1.291 2.787 1.00 22.07 ? 63 ASN A N 1 ATOM 342 C CA . ASN A 1 45 ? 28.396 0.037 2.030 1.00 21.82 ? 63 ASN A CA 1 ATOM 343 C C . ASN A 1 45 ? 27.069 -0.701 2.195 1.00 21.04 ? 63 ASN A C 1 ATOM 344 O O . ASN A 1 45 ? 27.055 -1.865 2.597 1.00 21.44 ? 63 ASN A O 1 ATOM 345 C CB . ASN A 1 45 ? 29.536 -0.889 2.481 1.00 22.57 ? 63 ASN A CB 1 ATOM 346 C CG . ASN A 1 45 ? 30.897 -0.465 1.947 0.50 23.31 ? 63 ASN A CG 1 ATOM 347 O OD1 . ASN A 1 45 ? 31.020 0.508 1.204 0.50 25.02 ? 63 ASN A OD1 1 ATOM 348 N ND2 . ASN A 1 45 ? 31.930 -1.206 2.332 0.50 24.68 ? 63 ASN A ND2 1 ATOM 349 N N . MET A 1 46 ? 25.963 -0.026 1.903 1.00 20.21 ? 64 MET A N 1 ATOM 350 C CA . MET A 1 46 ? 24.667 -0.639 2.108 1.00 19.72 ? 64 MET A CA 1 ATOM 351 C C . MET A 1 46 ? 24.369 -1.695 1.067 1.00 18.55 ? 64 MET A C 1 ATOM 352 O O . MET A 1 46 ? 24.604 -1.495 -0.129 1.00 18.65 ? 64 MET A O 1 ATOM 353 C CB . MET A 1 46 ? 23.571 0.408 2.083 1.00 19.68 ? 64 MET A CB 1 ATOM 354 C CG . MET A 1 46 ? 22.313 -0.092 2.657 1.00 20.28 ? 64 MET A CG 1 ATOM 355 S SD . MET A 1 46 ? 21.067 1.161 2.456 1.00 24.07 ? 64 MET A SD 1 ATOM 356 C CE . MET A 1 46 ? 21.869 2.583 3.209 1.00 19.65 ? 64 MET A CE 1 ATOM 357 N N . ARG A 1 47 ? 23.852 -2.820 1.543 1.00 17.26 ? 65 ARG A N 1 ATOM 358 C CA . ARG A 1 47 ? 23.339 -3.869 0.682 1.00 16.45 ? 65 ARG A CA 1 ATOM 359 C C . ARG A 1 47 ? 21.934 -4.117 1.177 1.00 15.07 ? 65 ARG A C 1 ATOM 360 O O . ARG A 1 47 ? 21.697 -4.129 2.384 1.00 15.10 ? 65 ARG A O 1 ATOM 361 C CB . ARG A 1 47 ? 24.180 -5.136 0.823 1.00 17.63 ? 65 ARG A CB 1 ATOM 362 C CG . ARG A 1 47 ? 25.676 -4.880 0.688 1.00 20.64 ? 65 ARG A CG 1 ATOM 363 C CD . ARG A 1 47 ? 26.516 -6.057 1.132 0.50 21.86 ? 65 ARG A CD 1 ATOM 364 N NE . ARG A 1 47 ? 26.492 -6.288 2.579 0.50 23.10 ? 65 ARG A NE 1 ATOM 365 C CZ . ARG A 1 47 ? 27.364 -5.780 3.447 0.50 24.56 ? 65 ARG A CZ 1 ATOM 366 N NH1 . ARG A 1 47 ? 27.266 -6.078 4.735 0.50 23.88 ? 65 ARG A NH1 1 ATOM 367 N NH2 . ARG A 1 47 ? 28.337 -4.978 3.035 0.50 25.91 ? 65 ARG A NH2 1 ATOM 368 N N . ILE A 1 48 ? 20.997 -4.255 0.247 1.00 13.16 ? 66 ILE A N 1 ATOM 369 C CA . ILE A 1 48 ? 19.595 -4.420 0.607 1.00 12.59 ? 66 ILE A CA 1 ATOM 370 C C . ILE A 1 48 ? 19.108 -5.715 0.006 1.00 12.15 ? 66 ILE A C 1 ATOM 371 O O . ILE A 1 48 ? 19.208 -5.923 -1.201 1.00 13.17 ? 66 ILE A O 1 ATOM 372 C CB . ILE A 1 48 ? 18.737 -3.250 0.080 1.00 12.49 ? 66 ILE A CB 1 ATOM 373 C CG1 . ILE A 1 48 ? 19.257 -1.937 0.666 1.00 13.21 ? 66 ILE A CG1 1 ATOM 374 C CG2 . ILE A 1 48 ? 17.257 -3.478 0.424 1.00 13.01 ? 66 ILE A CG2 1 ATOM 375 C CD1 . ILE A 1 48 ? 18.736 -0.686 -0.007 1.00 16.28 ? 66 ILE A CD1 1 ATOM 376 N N . TYR A 1 49 ? 18.566 -6.582 0.847 1.00 11.53 ? 67 TYR A N 1 ATOM 377 C CA . TYR A 1 49 ? 18.106 -7.876 0.386 1.00 11.56 ? 67 TYR A CA 1 ATOM 378 C C . TYR A 1 49 ? 16.611 -7.929 0.448 1.00 11.49 ? 67 TYR A C 1 ATOM 379 O O . TYR A 1 49 ? 16.016 -7.607 1.465 1.00 11.32 ? 67 TYR A O 1 ATOM 380 C CB . TYR A 1 49 ? 18.679 -8.989 1.257 1.00 11.60 ? 67 TYR A CB 1 ATOM 381 C CG . TYR A 1 49 ? 20.173 -9.087 1.145 1.00 12.69 ? 67 TYR A CG 1 ATOM 382 C CD1 . TYR A 1 49 ? 20.998 -8.366 1.995 1.00 13.40 ? 67 TYR A CD1 1 ATOM 383 C CD2 . TYR A 1 49 ? 20.762 -9.900 0.173 1.00 13.09 ? 67 TYR A CD2 1 ATOM 384 C CE1 . TYR A 1 49 ? 22.376 -8.443 1.893 1.00 14.26 ? 67 TYR A CE1 1 ATOM 385 C CE2 . TYR A 1 49 ? 22.137 -9.990 0.064 1.00 14.98 ? 67 TYR A CE2 1 ATOM 386 C CZ . TYR A 1 49 ? 22.939 -9.260 0.915 1.00 14.67 ? 67 TYR A CZ 1 ATOM 387 O OH . TYR A 1 49 ? 24.311 -9.352 0.790 1.00 16.93 ? 67 TYR A OH 1 ATOM 388 N N . LEU A 1 50 ? 16.009 -8.340 -0.660 1.00 11.04 ? 68 LEU A N 1 ATOM 389 C CA . LEU A 1 50 ? 14.567 -8.497 -0.730 1.00 11.28 ? 68 LEU A CA 1 ATOM 390 C C . LEU A 1 50 ? 14.255 -9.968 -0.838 1.00 11.07 ? 68 LEU A C 1 ATOM 391 O O . LEU A 1 50 ? 15.095 -10.755 -1.287 1.00 11.10 ? 68 LEU A O 1 ATOM 392 C CB . LEU A 1 50 ? 14.007 -7.765 -1.949 1.00 11.62 ? 68 LEU A CB 1 ATOM 393 C CG . LEU A 1 50 ? 14.101 -6.230 -2.015 1.00 13.10 ? 68 LEU A CG 1 ATOM 394 C CD1 . LEU A 1 50 ? 13.626 -5.576 -0.710 1.00 12.94 ? 68 LEU A CD1 1 ATOM 395 C CD2 . LEU A 1 50 ? 15.488 -5.727 -2.396 1.00 14.96 ? 68 LEU A CD2 1 ATOM 396 N N . GLY A 1 51 ? 13.049 -10.334 -0.417 1.00 10.73 ? 69 GLY A N 1 ATOM 397 C CA . GLY A 1 51 ? 12.602 -11.715 -0.496 1.00 10.83 ? 69 GLY A CA 1 ATOM 398 C C . GLY A 1 51 ? 13.318 -12.671 0.421 1.00 11.56 ? 69 GLY A C 1 ATOM 399 O O . GLY A 1 51 ? 13.310 -13.879 0.187 1.00 11.79 ? 69 GLY A O 1 ATOM 400 N N . MET A 1 52 ? 13.909 -12.135 1.491 1.00 10.94 ? 70 MET A N 1 ATOM 401 C CA . MET A 1 52 ? 14.612 -12.977 2.462 1.00 11.49 ? 70 MET A CA 1 ATOM 402 C C . MET A 1 52 ? 13.718 -13.407 3.598 1.00 11.78 ? 70 MET A C 1 ATOM 403 O O . MET A 1 52 ? 12.895 -12.631 4.089 1.00 11.16 ? 70 MET A O 1 ATOM 404 C CB . MET A 1 52 ? 15.799 -12.214 3.061 1.00 12.11 ? 70 MET A CB 1 ATOM 405 C CG . MET A 1 52 ? 16.936 -11.974 2.101 1.00 13.08 ? 70 MET A CG 1 ATOM 406 S SD . MET A 1 52 ? 17.819 -13.493 1.710 1.00 15.88 ? 70 MET A SD 1 ATOM 407 C CE . MET A 1 52 ? 18.567 -13.824 3.285 1.00 16.55 ? 70 MET A CE 1 ATOM 408 N N . HIS A 1 53 ? 13.898 -14.648 4.035 1.00 11.11 ? 71 HIS A N 1 ATOM 409 C CA . HIS A 1 53 ? 13.296 -15.084 5.273 1.00 11.17 ? 71 HIS A CA 1 ATOM 410 C C . HIS A 1 53 ? 14.440 -15.656 6.089 1.00 11.68 ? 71 HIS A C 1 ATOM 411 O O . HIS A 1 53 ? 15.068 -14.959 6.894 1.00 11.94 ? 71 HIS A O 1 ATOM 412 C CB . HIS A 1 53 ? 12.191 -16.119 5.035 1.00 11.83 ? 71 HIS A CB 1 ATOM 413 C CG . HIS A 1 53 ? 11.532 -16.586 6.295 1.00 12.24 ? 71 HIS A CG 1 ATOM 414 N ND1 . HIS A 1 53 ? 10.533 -15.870 6.919 1.00 12.18 ? 71 HIS A ND1 1 ATOM 415 C CD2 . HIS A 1 53 ? 11.716 -17.706 7.036 1.00 13.88 ? 71 HIS A CD2 1 ATOM 416 C CE1 . HIS A 1 53 ? 10.135 -16.525 7.998 1.00 13.90 ? 71 HIS A CE1 1 ATOM 417 N NE2 . HIS A 1 53 ? 10.832 -17.646 8.085 1.00 14.42 ? 71 HIS A NE2 1 ATOM 418 N N . ASN A 1 54 ? 14.752 -16.923 5.859 1.00 11.73 ? 72 ASN A N 1 ATOM 419 C CA . ASN A 1 54 ? 15.860 -17.520 6.577 1.00 11.76 ? 72 ASN A CA 1 ATOM 420 C C . ASN A 1 54 ? 17.194 -17.086 5.969 1.00 11.89 ? 72 ASN A C 1 ATOM 421 O O . ASN A 1 54 ? 17.430 -17.271 4.766 1.00 12.08 ? 72 ASN A O 1 ATOM 422 C CB . ASN A 1 54 ? 15.736 -19.043 6.562 1.00 12.01 ? 72 ASN A CB 1 ATOM 423 C CG . ASN A 1 54 ? 16.610 -19.713 7.618 1.00 12.40 ? 72 ASN A CG 1 ATOM 424 O OD1 . ASN A 1 54 ? 17.746 -19.300 7.888 1.00 12.47 ? 72 ASN A OD1 1 ATOM 425 N ND2 . ASN A 1 54 ? 16.064 -20.753 8.235 1.00 15.62 ? 72 ASN A ND2 1 ATOM 426 N N . LEU A 1 55 ? 18.054 -16.500 6.801 1.00 12.50 ? 73 LEU A N 1 ATOM 427 C CA . LEU A 1 55 ? 19.377 -16.071 6.356 1.00 13.09 ? 73 LEU A CA 1 ATOM 428 C C . LEU A 1 55 ? 20.238 -17.247 5.915 1.00 13.09 ? 73 LEU A C 1 ATOM 429 O O . LEU A 1 55 ? 21.244 -17.072 5.209 1.00 13.69 ? 73 LEU A O 1 ATOM 430 C CB . LEU A 1 55 ? 20.091 -15.294 7.466 1.00 13.79 ? 73 LEU A CB 1 ATOM 431 C CG . LEU A 1 55 ? 19.284 -14.095 7.969 1.00 14.11 ? 73 LEU A CG 1 ATOM 432 C CD1 . LEU A 1 55 ? 20.081 -13.358 9.051 1.00 16.82 ? 73 LEU A CD1 1 ATOM 433 C CD2 . LEU A 1 55 ? 18.916 -13.167 6.833 1.00 15.80 ? 73 LEU A CD2 1 ATOM 434 N N . LYS A 1 56 ? 19.838 -18.436 6.351 1.00 12.58 ? 74 LYS A N 1 ATOM 435 C CA . LYS A 1 56 ? 20.622 -19.633 6.089 1.00 12.65 ? 74 LYS A CA 1 ATOM 436 C C . LYS A 1 56 ? 19.944 -20.601 5.142 1.00 12.56 ? 74 LYS A C 1 ATOM 437 O O . LYS A 1 56 ? 20.489 -21.653 4.837 1.00 12.66 ? 74 LYS A O 1 ATOM 438 C CB . LYS A 1 56 ? 20.943 -20.329 7.404 1.00 12.88 ? 74 LYS A CB 1 ATOM 439 C CG . LYS A 1 56 ? 21.790 -19.460 8.316 1.00 14.09 ? 74 LYS A CG 1 ATOM 440 C CD . LYS A 1 56 ? 22.373 -20.253 9.435 1.00 18.41 ? 74 LYS A CD 1 ATOM 441 C CE . LYS A 1 56 ? 23.420 -19.409 10.154 1.00 21.38 ? 74 LYS A CE 1 ATOM 442 N NZ . LYS A 1 56 ? 24.002 -20.156 11.298 1.00 25.24 ? 74 LYS A NZ 1 ATOM 443 N N . VAL A 1 57 ? 18.739 -20.262 4.707 1.00 12.69 ? 75 VAL A N 1 ATOM 444 C CA . VAL A 1 57 ? 18.047 -21.076 3.737 1.00 12.81 ? 75 VAL A CA 1 ATOM 445 C C . VAL A 1 57 ? 17.473 -20.080 2.773 1.00 13.41 ? 75 VAL A C 1 ATOM 446 O O . VAL A 1 57 ? 16.362 -19.572 2.973 1.00 13.84 ? 75 VAL A O 1 ATOM 447 C CB . VAL A 1 57 ? 16.923 -21.939 4.356 1.00 12.62 ? 75 VAL A CB 1 ATOM 448 C CG1 . VAL A 1 57 ? 16.336 -22.854 3.293 1.00 14.99 ? 75 VAL A CG1 1 ATOM 449 C CG2 . VAL A 1 57 ? 17.450 -22.748 5.529 1.00 13.21 ? 75 VAL A CG2 1 ATOM 450 N N . LEU A 1 58 ? 18.255 -19.761 1.750 1.00 13.08 ? 76 LEU A N 1 ATOM 451 C CA . LEU A 1 58 ? 17.905 -18.644 0.895 1.00 13.46 ? 76 LEU A CA 1 ATOM 452 C C . LEU A 1 58 ? 16.682 -18.935 0.060 1.00 13.71 ? 76 LEU A C 1 ATOM 453 O O . LEU A 1 58 ? 16.625 -19.931 -0.681 1.00 14.09 ? 76 LEU A O 1 ATOM 454 C CB . LEU A 1 58 ? 19.069 -18.280 -0.015 1.00 13.05 ? 76 LEU A CB 1 ATOM 455 C CG . LEU A 1 58 ? 20.372 -17.839 0.635 1.00 15.96 ? 76 LEU A CG 1 ATOM 456 C CD1 . LEU A 1 58 ? 21.313 -17.358 -0.441 1.00 18.96 ? 76 LEU A CD1 1 ATOM 457 C CD2 . LEU A 1 58 ? 20.096 -16.739 1.671 1.00 18.70 ? 76 LEU A CD2 1 ATOM 458 N N . ASN A 1 59 ? 15.693 -18.052 0.159 1.00 12.77 ? 77 ASN A N 1 ATOM 459 C CA . ASN A 1 59 ? 14.541 -18.166 -0.700 1.00 12.61 ? 77 ASN A CA 1 ATOM 460 C C . ASN A 1 59 ? 14.999 -18.094 -2.135 1.00 12.58 ? 77 ASN A C 1 ATOM 461 O O . ASN A 1 59 ? 15.914 -17.328 -2.481 1.00 13.02 ? 77 ASN A O 1 ATOM 462 C CB . ASN A 1 59 ? 13.540 -17.039 -0.444 1.00 12.55 ? 77 ASN A CB 1 ATOM 463 C CG . ASN A 1 59 ? 12.752 -17.232 0.836 1.00 13.17 ? 77 ASN A CG 1 ATOM 464 O OD1 . ASN A 1 59 ? 12.632 -18.345 1.353 1.00 12.67 ? 77 ASN A OD1 1 ATOM 465 N ND2 . ASN A 1 59 ? 12.196 -16.132 1.353 1.00 13.26 ? 77 ASN A ND2 1 ATOM 466 N N . LYS A 1 60 ? 14.369 -18.902 -2.979 1.00 13.36 ? 78 LYS A N 1 ATOM 467 C CA . LYS A 1 60 ? 14.778 -18.973 -4.380 1.00 13.70 ? 78 LYS A CA 1 ATOM 468 C C . LYS A 1 60 ? 14.690 -17.629 -5.073 1.00 13.65 ? 78 LYS A C 1 ATOM 469 O O . LYS A 1 60 ? 15.465 -17.341 -5.983 1.00 14.93 ? 78 LYS A O 1 ATOM 470 C CB . LYS A 1 60 ? 13.961 -20.019 -5.130 1.00 14.64 ? 78 LYS A CB 1 ATOM 471 C CG . LYS A 1 60 ? 14.313 -21.422 -4.703 0.50 15.30 ? 78 LYS A CG 1 ATOM 472 C CD . LYS A 1 60 ? 13.520 -22.438 -5.490 0.50 18.05 ? 78 LYS A CD 1 ATOM 473 C CE . LYS A 1 60 ? 14.268 -23.750 -5.588 0.50 20.79 ? 78 LYS A CE 1 ATOM 474 N NZ . LYS A 1 60 ? 15.471 -23.622 -6.460 0.50 22.90 ? 78 LYS A NZ 1 ATOM 475 N N . ASP A 1 61 ? 13.758 -16.796 -4.604 1.00 13.31 ? 79 ASP A N 1 ATOM 476 C CA . ASP A 1 61 ? 13.531 -15.504 -5.200 1.00 13.86 ? 79 ASP A CA 1 ATOM 477 C C . ASP A 1 61 ? 14.216 -14.369 -4.440 1.00 13.35 ? 79 ASP A C 1 ATOM 478 O O . ASP A 1 61 ? 13.957 -13.209 -4.722 1.00 14.13 ? 79 ASP A O 1 ATOM 479 C CB . ASP A 1 61 ? 12.021 -15.238 -5.353 1.00 13.82 ? 79 ASP A CB 1 ATOM 480 C CG . ASP A 1 61 ? 11.247 -15.373 -4.049 1.00 14.74 ? 79 ASP A CG 1 ATOM 481 O OD1 . ASP A 1 61 ? 11.686 -16.090 -3.121 1.00 14.63 ? 79 ASP A OD1 1 ATOM 482 O OD2 . ASP A 1 61 ? 10.148 -14.769 -3.972 1.00 15.00 ? 79 ASP A OD2 1 ATOM 483 N N . ALA A 1 62 ? 15.103 -14.693 -3.497 1.00 13.16 ? 80 ALA A N 1 ATOM 484 C CA . ALA A 1 62 ? 15.826 -13.638 -2.783 1.00 13.75 ? 80 ALA A CA 1 ATOM 485 C C . ALA A 1 62 ? 16.711 -12.845 -3.737 1.00 13.66 ? 80 ALA A C 1 ATOM 486 O O . ALA A 1 62 ? 17.285 -13.390 -4.684 1.00 14.13 ? 80 ALA A O 1 ATOM 487 C CB . ALA A 1 62 ? 16.655 -14.206 -1.647 1.00 13.95 ? 80 ALA A CB 1 ATOM 488 N N . LEU A 1 63 ? 16.823 -11.549 -3.466 1.00 13.31 ? 81 LEU A N 1 ATOM 489 C CA . LEU A 1 63 ? 17.565 -10.646 -4.328 1.00 13.32 ? 81 LEU A CA 1 ATOM 490 C C . LEU A 1 63 ? 18.449 -9.728 -3.513 1.00 13.06 ? 81 LEU A C 1 ATOM 491 O O . LEU A 1 63 ? 18.069 -9.307 -2.415 1.00 12.85 ? 81 LEU A O 1 ATOM 492 C CB . LEU A 1 63 ? 16.590 -9.783 -5.123 1.00 13.78 ? 81 LEU A CB 1 ATOM 493 C CG . LEU A 1 63 ? 15.683 -10.509 -6.121 1.00 15.93 ? 81 LEU A CG 1 ATOM 494 C CD1 . LEU A 1 63 ? 14.667 -9.544 -6.707 1.00 17.99 ? 81 LEU A CD1 1 ATOM 495 C CD2 . LEU A 1 63 ? 16.529 -11.114 -7.217 1.00 17.70 ? 81 LEU A CD2 1 ATOM 496 N N . ARG A 1 64 ? 19.609 -9.398 -4.066 1.00 12.47 ? 82 ARG A N 1 ATOM 497 C CA . ARG A 1 64 ? 20.441 -8.350 -3.501 1.00 12.49 ? 82 ARG A CA 1 ATOM 498 C C . ARG A 1 64 ? 20.342 -7.106 -4.359 1.00 12.44 ? 82 ARG A C 1 ATOM 499 O O . ARG A 1 64 ? 20.363 -7.192 -5.585 1.00 12.81 ? 82 ARG A O 1 ATOM 500 C CB . ARG A 1 64 ? 21.904 -8.781 -3.407 1.00 12.70 ? 82 ARG A CB 1 ATOM 501 C CG . ARG A 1 64 ? 22.776 -7.718 -2.743 1.00 13.94 ? 82 ARG A CG 1 ATOM 502 C CD . ARG A 1 64 ? 24.259 -8.013 -2.852 1.00 17.00 ? 82 ARG A CD 1 ATOM 503 N NE . ARG A 1 64 ? 24.643 -9.153 -2.023 1.00 19.15 ? 82 ARG A NE 1 ATOM 504 C CZ . ARG A 1 64 ? 25.031 -10.339 -2.488 1.00 20.55 ? 82 ARG A CZ 1 ATOM 505 N NH1 . ARG A 1 64 ? 25.357 -11.306 -1.639 1.00 20.26 ? 82 ARG A NH1 1 ATOM 506 N NH2 . ARG A 1 64 ? 25.103 -10.554 -3.793 1.00 19.48 ? 82 ARG A NH2 1 ATOM 507 N N . ARG A 1 65 ? 20.217 -5.958 -3.695 1.00 12.14 ? 83 ARG A N 1 ATOM 508 C CA . ARG A 1 65 ? 20.169 -4.681 -4.372 1.00 12.28 ? 83 ARG A CA 1 ATOM 509 C C . ARG A 1 65 ? 21.027 -3.681 -3.621 1.00 12.43 ? 83 ARG A C 1 ATOM 510 O O . ARG A 1 65 ? 21.456 -3.933 -2.496 1.00 12.80 ? 83 ARG A O 1 ATOM 511 C CB . ARG A 1 65 ? 18.733 -4.167 -4.435 1.00 12.56 ? 83 ARG A CB 1 ATOM 512 C CG . ARG A 1 65 ? 17.794 -5.008 -5.309 1.00 12.32 ? 83 ARG A CG 1 ATOM 513 C CD . ARG A 1 65 ? 18.151 -4.834 -6.773 1.00 12.99 ? 83 ARG A CD 1 ATOM 514 N NE . ARG A 1 65 ? 17.203 -5.475 -7.680 1.00 12.81 ? 83 ARG A NE 1 ATOM 515 C CZ . ARG A 1 65 ? 17.328 -6.714 -8.146 1.00 13.46 ? 83 ARG A CZ 1 ATOM 516 N NH1 . ARG A 1 65 ? 18.345 -7.483 -7.755 1.00 13.03 ? 83 ARG A NH1 1 ATOM 517 N NH2 . ARG A 1 65 ? 16.432 -7.189 -9.007 1.00 12.75 ? 83 ARG A NH2 1 ATOM 518 N N . PHE A 1 66 ? 21.276 -2.555 -4.271 1.00 13.26 ? 84 PHE A N 1 ATOM 519 C CA . PHE A 1 66 ? 22.140 -1.523 -3.741 1.00 13.88 ? 84 PHE A CA 1 ATOM 520 C C . PHE A 1 66 ? 21.436 -0.196 -3.907 1.00 13.81 ? 84 PHE A C 1 ATOM 521 O O . PHE A 1 66 ? 20.595 -0.051 -4.783 1.00 13.35 ? 84 PHE A O 1 ATOM 522 C CB . PHE A 1 66 ? 23.453 -1.496 -4.525 1.00 14.97 ? 84 PHE A CB 1 ATOM 523 C CG . PHE A 1 66 ? 24.182 -2.793 -4.498 1.00 17.17 ? 84 PHE A CG 1 ATOM 524 C CD1 . PHE A 1 66 ? 23.950 -3.755 -5.470 1.00 17.95 ? 84 PHE A CD1 1 ATOM 525 C CD2 . PHE A 1 66 ? 25.080 -3.069 -3.469 1.00 18.77 ? 84 PHE A CD2 1 ATOM 526 C CE1 . PHE A 1 66 ? 24.606 -4.980 -5.429 1.00 19.18 ? 84 PHE A CE1 1 ATOM 527 C CE2 . PHE A 1 66 ? 25.754 -4.287 -3.424 1.00 19.41 ? 84 PHE A CE2 1 ATOM 528 C CZ . PHE A 1 66 ? 25.520 -5.237 -4.401 1.00 19.31 ? 84 PHE A CZ 1 ATOM 529 N N . PRO A 1 67 ? 21.779 0.783 -3.070 1.00 13.88 ? 85 PRO A N 1 ATOM 530 C CA . PRO A 1 67 ? 21.181 2.091 -3.299 1.00 14.30 ? 85 PRO A CA 1 ATOM 531 C C . PRO A 1 67 ? 21.682 2.730 -4.579 1.00 14.76 ? 85 PRO A C 1 ATOM 532 O O . PRO A 1 67 ? 22.898 2.778 -4.832 1.00 15.97 ? 85 PRO A O 1 ATOM 533 C CB . PRO A 1 67 ? 21.632 2.911 -2.082 1.00 14.69 ? 85 PRO A CB 1 ATOM 534 C CG . PRO A 1 67 ? 22.150 1.926 -1.115 1.00 15.46 ? 85 PRO A CG 1 ATOM 535 C CD . PRO A 1 67 ? 22.660 0.772 -1.894 1.00 14.22 ? 85 PRO A CD 1 ATOM 536 N N . LYS A 1 68 ? 20.738 3.176 -5.394 1.00 14.10 ? 86 LYS A N 1 ATOM 537 C CA . LYS A 1 68 ? 21.043 3.978 -6.564 1.00 14.36 ? 86 LYS A CA 1 ATOM 538 C C . LYS A 1 68 ? 20.711 5.452 -6.325 1.00 13.58 ? 86 LYS A C 1 ATOM 539 O O . LYS A 1 68 ? 21.380 6.348 -6.867 1.00 14.05 ? 86 LYS A O 1 ATOM 540 C CB . LYS A 1 68 ? 20.263 3.444 -7.753 1.00 15.39 ? 86 LYS A CB 1 ATOM 541 C CG . LYS A 1 68 ? 20.610 4.125 -9.044 1.00 19.36 ? 86 LYS A CG 1 ATOM 542 C CD . LYS A 1 68 ? 20.129 3.310 -10.218 1.00 23.80 ? 86 LYS A CD 1 ATOM 543 C CE . LYS A 1 68 ? 18.627 3.403 -10.381 1.00 26.91 ? 86 LYS A CE 1 ATOM 544 N NZ . LYS A 1 68 ? 18.228 2.734 -11.649 1.00 30.62 ? 86 LYS A NZ 1 ATOM 545 N N . GLU A 1 69 ? 19.653 5.704 -5.551 1.00 12.28 ? 87 GLU A N 1 ATOM 546 C CA . GLU A 1 69 ? 19.318 7.052 -5.094 1.00 11.43 ? 87 GLU A CA 1 ATOM 547 C C . GLU A 1 69 ? 19.105 6.974 -3.605 1.00 11.70 ? 87 GLU A C 1 ATOM 548 O O . GLU A 1 69 ? 18.689 5.942 -3.084 1.00 11.84 ? 87 GLU A O 1 ATOM 549 C CB . GLU A 1 69 ? 18.053 7.569 -5.777 1.00 11.49 ? 87 GLU A CB 1 ATOM 550 C CG . GLU A 1 69 ? 18.188 7.563 -7.283 1.00 11.01 ? 87 GLU A CG 1 ATOM 551 C CD . GLU A 1 69 ? 17.013 8.173 -8.001 1.00 11.79 ? 87 GLU A CD 1 ATOM 552 O OE1 . GLU A 1 69 ? 16.907 7.927 -9.220 1.00 14.94 ? 87 GLU A OE1 1 ATOM 553 O OE2 . GLU A 1 69 ? 16.221 8.933 -7.401 1.00 12.57 ? 87 GLU A OE2 1 ATOM 554 N N . LYS A 1 70 ? 19.388 8.063 -2.910 1.00 11.68 ? 88 LYS A N 1 ATOM 555 C CA . LYS A 1 70 ? 19.282 8.042 -1.470 1.00 12.52 ? 88 LYS A CA 1 ATOM 556 C C . LYS A 1 70 ? 18.884 9.413 -1.003 1.00 11.99 ? 88 LYS A C 1 ATOM 557 O O . LYS A 1 70 ? 19.501 10.412 -1.362 1.00 12.40 ? 88 LYS A O 1 ATOM 558 C CB . LYS A 1 70 ? 20.632 7.646 -0.884 1.00 13.35 ? 88 LYS A CB 1 ATOM 559 C CG . LYS A 1 70 ? 20.725 7.677 0.617 1.00 17.80 ? 88 LYS A CG 1 ATOM 560 C CD . LYS A 1 70 ? 22.177 7.428 1.041 1.00 22.00 ? 88 LYS A CD 1 ATOM 561 C CE . LYS A 1 70 ? 22.688 6.058 0.586 1.00 23.08 ? 88 LYS A CE 1 ATOM 562 N NZ . LYS A 1 70 ? 24.080 5.800 1.122 1.00 23.79 ? 88 LYS A NZ 1 ATOM 563 N N . TYR A 1 71 ? 17.829 9.455 -0.211 1.00 10.30 ? 89 TYR A N 1 ATOM 564 C CA . TYR A 1 71 ? 17.312 10.714 0.275 1.00 10.23 ? 89 TYR A CA 1 ATOM 565 C C . TYR A 1 71 ? 17.001 10.622 1.733 1.00 10.43 ? 89 TYR A C 1 ATOM 566 O O . TYR A 1 71 ? 16.588 9.585 2.236 1.00 10.35 ? 89 TYR A O 1 ATOM 567 C CB . TYR A 1 71 ? 16.014 11.046 -0.441 1.00 10.33 ? 89 TYR A CB 1 ATOM 568 C CG . TYR A 1 71 ? 16.121 11.054 -1.931 1.00 9.84 ? 89 TYR A CG 1 ATOM 569 C CD1 . TYR A 1 71 ? 15.893 9.892 -2.667 1.00 10.72 ? 89 TYR A CD1 1 ATOM 570 C CD2 . TYR A 1 71 ? 16.403 12.235 -2.610 1.00 11.24 ? 89 TYR A CD2 1 ATOM 571 C CE1 . TYR A 1 71 ? 15.977 9.898 -4.047 1.00 10.85 ? 89 TYR A CE1 1 ATOM 572 C CE2 . TYR A 1 71 ? 16.493 12.252 -3.979 1.00 11.26 ? 89 TYR A CE2 1 ATOM 573 C CZ . TYR A 1 71 ? 16.276 11.090 -4.690 1.00 11.74 ? 89 TYR A CZ 1 ATOM 574 O OH . TYR A 1 71 ? 16.339 11.124 -6.055 1.00 12.96 ? 89 TYR A OH 1 ATOM 575 N N . PHE A 1 72 ? 17.184 11.747 2.409 1.00 10.14 ? 90 PHE A N 1 ATOM 576 C CA . PHE A 1 72 ? 16.812 11.909 3.795 1.00 11.20 ? 90 PHE A CA 1 ATOM 577 C C . PHE A 1 72 ? 16.516 13.391 4.004 1.00 10.93 ? 90 PHE A C 1 ATOM 578 O O . PHE A 1 72 ? 16.687 14.211 3.085 1.00 11.68 ? 90 PHE A O 1 ATOM 579 C CB . PHE A 1 72 ? 17.931 11.408 4.730 1.00 11.29 ? 90 PHE A CB 1 ATOM 580 C CG . PHE A 1 72 ? 19.251 12.089 4.511 1.00 13.45 ? 90 PHE A CG 1 ATOM 581 C CD1 . PHE A 1 72 ? 19.556 13.259 5.196 1.00 14.88 ? 90 PHE A CD1 1 ATOM 582 C CD2 . PHE A 1 72 ? 20.185 11.556 3.627 1.00 15.74 ? 90 PHE A CD2 1 ATOM 583 C CE1 . PHE A 1 72 ? 20.783 13.911 4.993 1.00 15.81 ? 90 PHE A CE1 1 ATOM 584 C CE2 . PHE A 1 72 ? 21.413 12.197 3.424 1.00 15.59 ? 90 PHE A CE2 1 ATOM 585 C CZ . PHE A 1 72 ? 21.701 13.368 4.111 1.00 15.28 ? 90 PHE A CZ 1 ATOM 586 N N . CYS A 1 73 ? 16.055 13.718 5.202 1.00 11.35 ? 91 CYS A N 1 ATOM 587 C CA . CYS A 1 73 ? 15.593 15.057 5.500 1.00 12.16 ? 91 CYS A CA 1 ATOM 588 C C . CYS A 1 73 ? 16.752 15.951 5.844 1.00 12.93 ? 91 CYS A C 1 ATOM 589 O O . CYS A 1 73 ? 17.649 15.557 6.590 1.00 13.48 ? 91 CYS A O 1 ATOM 590 C CB . CYS A 1 73 ? 14.641 15.043 6.683 1.00 11.64 ? 91 CYS A CB 1 ATOM 591 S SG . CYS A 1 73 ? 13.240 13.956 6.442 1.00 12.18 ? 91 CYS A SG 1 ATOM 592 N N . LEU A 1 74 ? 16.681 17.172 5.320 1.00 14.68 ? 92 LEU A N 1 ATOM 593 C CA . LEU A 1 74 ? 17.692 18.194 5.592 1.00 16.10 ? 92 LEU A CA 1 ATOM 594 C C . LEU A 1 74 ? 17.180 19.251 6.566 1.00 16.93 ? 92 LEU A C 1 ATOM 595 O O . LEU A 1 74 ? 17.828 20.291 6.759 1.00 18.98 ? 92 LEU A O 1 ATOM 596 C CB . LEU A 1 74 ? 18.135 18.872 4.282 1.00 15.89 ? 92 LEU A CB 1 ATOM 597 C CG . LEU A 1 74 ? 18.685 17.982 3.165 1.00 16.00 ? 92 LEU A CG 1 ATOM 598 C CD1 . LEU A 1 74 ? 18.953 18.811 1.917 1.00 17.03 ? 92 LEU A CD1 1 ATOM 599 C CD2 . LEU A 1 74 ? 19.947 17.269 3.590 1.00 18.71 ? 92 LEU A CD2 1 ATOM 600 N N . ASN A 1 75 ? 16.012 19.015 7.155 1.00 16.62 ? 93 ASN A N 1 ATOM 601 C CA . ASN A 1 75 ? 15.430 19.955 8.116 1.00 17.19 ? 93 ASN A CA 1 ATOM 602 C C . ASN A 1 75 ? 15.322 19.317 9.498 1.00 17.66 ? 93 ASN A C 1 ATOM 603 O O . ASN A 1 75 ? 14.389 19.583 10.248 1.00 18.78 ? 93 ASN A O 1 ATOM 604 C CB . ASN A 1 75 ? 14.067 20.471 7.637 1.00 16.67 ? 93 ASN A CB 1 ATOM 605 C CG . ASN A 1 75 ? 13.061 19.371 7.440 0.70 16.03 ? 93 ASN A CG 1 ATOM 606 O OD1 . ASN A 1 75 ? 13.390 18.188 7.557 0.70 12.93 ? 93 ASN A OD1 1 ATOM 607 N ND2 . ASN A 1 75 ? 11.823 19.750 7.135 0.70 16.34 ? 93 ASN A ND2 1 ATOM 608 N N . THR A 1 76 ? 16.292 18.476 9.825 1.00 18.35 ? 94 THR A N 1 ATOM 609 C CA . THR A 1 76 ? 16.307 17.812 11.134 1.00 19.26 ? 94 THR A CA 1 ATOM 610 C C . THR A 1 76 ? 16.820 18.731 12.237 1.00 20.12 ? 94 THR A C 1 ATOM 611 O O . THR A 1 76 ? 17.560 19.687 11.978 1.00 21.15 ? 94 THR A O 1 ATOM 612 C CB . THR A 1 76 ? 17.168 16.542 11.122 1.00 19.55 ? 94 THR A CB 1 ATOM 613 O OG1 . THR A 1 76 ? 18.508 16.868 10.745 1.00 20.52 ? 94 THR A OG1 1 ATOM 614 C CG2 . THR A 1 76 ? 16.605 15.513 10.151 1.00 18.74 ? 94 THR A CG2 1 ATOM 615 N N . ARG A 1 77 ? 16.398 18.440 13.463 1.00 20.25 ? 95 ARG A N 1 ATOM 616 C CA . ARG A 1 77 ? 16.918 19.105 14.650 1.00 21.11 ? 95 ARG A CA 1 ATOM 617 C C . ARG A 1 77 ? 18.028 18.254 15.227 1.00 21.36 ? 95 ARG A C 1 ATOM 618 O O . ARG A 1 77 ? 18.111 17.063 14.943 1.00 21.80 ? 95 ARG A O 1 ATOM 619 C CB . ARG A 1 77 ? 15.851 19.192 15.720 1.00 21.32 ? 95 ARG A CB 1 ATOM 620 C CG . ARG A 1 77 ? 14.566 19.803 15.318 1.00 22.29 ? 95 ARG A CG 1 ATOM 621 C CD . ARG A 1 77 ? 13.536 19.384 16.324 1.00 21.78 ? 95 ARG A CD 1 ATOM 622 N NE . ARG A 1 77 ? 13.813 19.934 17.650 1.00 21.40 ? 95 ARG A NE 1 ATOM 623 C CZ . ARG A 1 77 ? 12.864 20.289 18.498 1.00 20.25 ? 95 ARG A CZ 1 ATOM 624 N NH1 . ARG A 1 77 ? 13.180 20.789 19.683 1.00 21.66 ? 95 ARG A NH1 1 ATOM 625 N NH2 . ARG A 1 77 ? 11.590 20.163 18.146 1.00 20.15 ? 95 ARG A NH2 1 ATOM 626 N N . ASN A 1 78 A 18.847 18.858 16.087 1.00 21.76 ? 96 ASN A N 1 ATOM 627 C CA . ASN A 1 78 A 19.953 18.170 16.746 1.00 22.39 ? 96 ASN A CA 1 ATOM 628 C C . ASN A 1 78 A 19.640 17.906 18.225 1.00 21.65 ? 96 ASN A C 1 ATOM 629 O O . ASN A 1 78 A 20.296 17.083 18.859 1.00 22.37 ? 96 ASN A O 1 ATOM 630 C CB . ASN A 1 78 A 21.246 18.999 16.609 1.00 23.59 ? 96 ASN A CB 1 ATOM 631 C CG . ASN A 1 78 A 22.534 18.175 16.807 0.50 26.21 ? 96 ASN A CG 1 ATOM 632 O OD1 . ASN A 1 78 A 23.309 17.991 15.870 0.50 28.79 ? 96 ASN A OD1 1 ATOM 633 N ND2 . ASN A 1 78 A 22.773 17.715 18.032 0.50 30.70 ? 96 ASN A ND2 1 ATOM 634 N N . ASP A 1 79 ? 18.637 18.598 18.767 1.00 20.52 ? 96 ASP A N 1 ATOM 635 C CA . ASP A 1 79 ? 18.302 18.440 20.194 1.00 20.41 ? 96 ASP A CA 1 ATOM 636 C C . ASP A 1 79 ? 17.325 17.305 20.495 1.00 20.17 ? 96 ASP A C 1 ATOM 637 O O . ASP A 1 79 ? 17.088 16.976 21.654 1.00 20.43 ? 96 ASP A O 1 ATOM 638 C CB . ASP A 1 79 ? 17.776 19.749 20.785 1.00 20.24 ? 96 ASP A CB 1 ATOM 639 C CG . ASP A 1 79 ? 16.521 20.227 20.112 1.00 20.59 ? 96 ASP A CG 1 ATOM 640 O OD1 . ASP A 1 79 ? 16.395 20.046 18.883 1.00 22.04 ? 96 ASP A OD1 1 ATOM 641 O OD2 . ASP A 1 79 ? 15.663 20.813 20.791 1.00 21.11 ? 96 ASP A OD2 1 ATOM 642 N N . THR A 1 80 ? 16.732 16.720 19.465 1.00 19.39 ? 97 THR A N 1 ATOM 643 C CA . THR A 1 80 ? 15.947 15.506 19.665 1.00 18.87 ? 97 THR A CA 1 ATOM 644 C C . THR A 1 80 ? 16.748 14.317 19.136 1.00 18.63 ? 97 THR A C 1 ATOM 645 O O . THR A 1 80 ? 17.721 14.498 18.401 1.00 18.38 ? 97 THR A O 1 ATOM 646 C CB . THR A 1 80 ? 14.552 15.594 19.005 1.00 18.78 ? 97 THR A CB 1 ATOM 647 O OG1 . THR A 1 80 ? 14.689 15.915 17.614 1.00 19.82 ? 97 THR A OG1 1 ATOM 648 C CG2 . THR A 1 80 ? 13.701 16.656 19.686 1.00 18.32 ? 97 THR A CG2 1 ATOM 649 N N . ILE A 1 81 ? 16.366 13.104 19.530 1.00 18.40 ? 98 ILE A N 1 ATOM 650 C CA . ILE A 1 81 ? 17.156 11.927 19.183 1.00 18.14 ? 98 ILE A CA 1 ATOM 651 C C . ILE A 1 81 ? 16.732 11.426 17.815 1.00 17.13 ? 98 ILE A C 1 ATOM 652 O O . ILE A 1 81 ? 15.557 11.125 17.598 1.00 16.64 ? 98 ILE A O 1 ATOM 653 C CB . ILE A 1 81 ? 17.033 10.789 20.224 1.00 19.25 ? 98 ILE A CB 1 ATOM 654 C CG1 . ILE A 1 81 ? 17.711 11.190 21.535 1.00 20.85 ? 98 ILE A CG1 1 ATOM 655 C CG2 . ILE A 1 81 ? 17.701 9.510 19.739 1.00 19.80 ? 98 ILE A CG2 1 ATOM 656 C CD1 . ILE A 1 81 ? 16.808 11.854 22.509 1.00 26.02 ? 98 ILE A CD1 1 ATOM 657 N N . TRP A 1 82 ? 17.699 11.367 16.903 1.00 16.27 ? 99 TRP A N 1 ATOM 658 C CA . TRP A 1 82 ? 17.466 10.855 15.556 1.00 15.70 ? 99 TRP A CA 1 ATOM 659 C C . TRP A 1 82 ? 16.196 11.434 14.964 1.00 14.80 ? 99 TRP A C 1 ATOM 660 O O . TRP A 1 82 ? 15.278 10.713 14.555 1.00 13.87 ? 99 TRP A O 1 ATOM 661 C CB . TRP A 1 82 ? 17.450 9.328 15.582 1.00 16.79 ? 99 TRP A CB 1 ATOM 662 C CG . TRP A 1 82 ? 18.834 8.811 15.702 1.00 16.99 ? 99 TRP A CG 1 ATOM 663 C CD1 . TRP A 1 82 ? 19.419 8.266 16.811 1.00 19.58 ? 99 TRP A CD1 1 ATOM 664 C CD2 . TRP A 1 82 ? 19.838 8.841 14.686 1.00 17.95 ? 99 TRP A CD2 1 ATOM 665 N NE1 . TRP A 1 82 ? 20.719 7.926 16.533 1.00 20.08 ? 99 TRP A NE1 1 ATOM 666 C CE2 . TRP A 1 82 ? 21.008 8.276 15.239 1.00 18.56 ? 99 TRP A CE2 1 ATOM 667 C CE3 . TRP A 1 82 ? 19.863 9.290 13.359 1.00 19.01 ? 99 TRP A CE3 1 ATOM 668 C CZ2 . TRP A 1 82 ? 22.198 8.141 14.507 1.00 18.88 ? 99 TRP A CZ2 1 ATOM 669 C CZ3 . TRP A 1 82 ? 21.052 9.151 12.627 1.00 18.89 ? 99 TRP A CZ3 1 ATOM 670 C CH2 . TRP A 1 82 ? 22.198 8.572 13.207 1.00 18.93 ? 99 TRP A CH2 1 ATOM 671 N N . ASP A 1 83 ? 16.137 12.760 14.929 1.00 13.39 ? 100 ASP A N 1 ATOM 672 C CA . ASP A 1 83 ? 14.995 13.426 14.341 1.00 12.43 ? 100 ASP A CA 1 ATOM 673 C C . ASP A 1 83 ? 14.823 12.967 12.898 1.00 11.77 ? 100 ASP A C 1 ATOM 674 O O . ASP A 1 83 ? 15.803 12.815 12.172 1.00 11.79 ? 100 ASP A O 1 ATOM 675 C CB . ASP A 1 83 ? 15.211 14.934 14.385 1.00 12.66 ? 100 ASP A CB 1 ATOM 676 C CG . ASP A 1 83 ? 13.965 15.714 14.017 1.00 13.67 ? 100 ASP A CG 1 ATOM 677 O OD1 . ASP A 1 83 ? 12.822 15.240 14.253 1.00 13.55 ? 100 ASP A OD1 1 ATOM 678 O OD2 . ASP A 1 83 ? 14.142 16.821 13.483 1.00 14.33 ? 100 ASP A OD2 1 ATOM 679 N N . LYS A 1 84 ? 13.569 12.739 12.503 1.00 11.66 ? 101 LYS A N 1 ATOM 680 C CA . LYS A 1 84 ? 13.249 12.372 11.125 1.00 11.18 ? 101 LYS A CA 1 ATOM 681 C C . LYS A 1 84 ? 14.114 11.200 10.677 1.00 10.85 ? 101 LYS A C 1 ATOM 682 O O . LYS A 1 84 ? 14.858 11.255 9.676 1.00 11.17 ? 101 LYS A O 1 ATOM 683 C CB . LYS A 1 84 ? 13.403 13.591 10.207 1.00 11.40 ? 101 LYS A CB 1 ATOM 684 C CG . LYS A 1 84 ? 12.629 14.776 10.727 1.00 12.64 ? 101 LYS A CG 1 ATOM 685 C CD . LYS A 1 84 ? 12.560 15.884 9.711 1.00 14.49 ? 101 LYS A CD 1 ATOM 686 C CE . LYS A 1 84 ? 12.080 17.169 10.357 1.00 15.44 ? 101 LYS A CE 1 ATOM 687 N NZ . LYS A 1 84 ? 10.733 17.069 10.970 1.00 17.26 ? 101 LYS A NZ 1 ATOM 688 N N . ASP A 1 85 ? 14.001 10.113 11.427 1.00 9.82 ? 102 ASP A N 1 ATOM 689 C CA . ASP A 1 85 ? 14.835 8.955 11.165 1.00 9.77 ? 102 ASP A CA 1 ATOM 690 C C . ASP A 1 85 ? 14.203 8.158 10.036 1.00 10.31 ? 102 ASP A C 1 ATOM 691 O O . ASP A 1 85 ? 13.461 7.199 10.250 1.00 10.61 ? 102 ASP A O 1 ATOM 692 C CB . ASP A 1 85 ? 14.994 8.124 12.430 1.00 9.53 ? 102 ASP A CB 1 ATOM 693 C CG . ASP A 1 85 ? 16.175 7.186 12.370 1.00 10.08 ? 102 ASP A CG 1 ATOM 694 O OD1 . ASP A 1 85 ? 16.897 7.163 11.356 1.00 9.98 ? 102 ASP A OD1 1 ATOM 695 O OD2 . ASP A 1 85 ? 16.367 6.454 13.359 1.00 11.73 ? 102 ASP A OD2 1 ATOM 696 N N . ILE A 1 86 ? 14.487 8.616 8.819 1.00 10.00 ? 103 ILE A N 1 ATOM 697 C CA . ILE A 1 86 ? 13.884 8.034 7.633 1.00 10.05 ? 103 ILE A CA 1 ATOM 698 C C . ILE A 1 86 ? 14.822 8.245 6.471 1.00 10.43 ? 103 ILE A C 1 ATOM 699 O O . ILE A 1 86 ? 15.461 9.280 6.360 1.00 10.76 ? 103 ILE A O 1 ATOM 700 C CB . ILE A 1 86 ? 12.501 8.665 7.353 1.00 10.52 ? 103 ILE A CB 1 ATOM 701 C CG1 . ILE A 1 86 ? 11.836 8.028 6.132 1.00 10.45 ? 103 ILE A CG1 1 ATOM 702 C CG2 . ILE A 1 86 ? 12.592 10.178 7.216 1.00 10.51 ? 103 ILE A CG2 1 ATOM 703 C CD1 . ILE A 1 86 ? 10.374 8.430 5.988 1.00 9.46 ? 103 ILE A CD1 1 ATOM 704 N N . MET A 1 87 ? 14.935 7.236 5.627 1.00 10.36 ? 104 MET A N 1 ATOM 705 C CA . MET A 1 87 ? 15.751 7.355 4.447 1.00 11.72 ? 104 MET A CA 1 ATOM 706 C C . MET A 1 87 ? 15.039 6.616 3.350 1.00 10.73 ? 104 MET A C 1 ATOM 707 O O . MET A 1 87 ? 14.564 5.488 3.536 1.00 10.46 ? 104 MET A O 1 ATOM 708 C CB . MET A 1 87 ? 17.125 6.763 4.680 1.00 12.67 ? 104 MET A CB 1 ATOM 709 C CG . MET A 1 87 ? 17.922 6.574 3.406 1.00 13.20 ? 104 MET A CG 1 ATOM 710 S SD . MET A 1 87 ? 19.649 6.171 3.786 1.00 17.31 ? 104 MET A SD 1 ATOM 711 C CE A MET A 1 87 ? 20.245 7.774 4.314 0.50 14.45 ? 104 MET A CE 1 ATOM 712 C CE B MET A 1 87 ? 19.417 4.828 4.924 0.50 15.31 ? 104 MET A CE 1 ATOM 713 N N . LEU A 1 88 ? 14.953 7.292 2.214 1.00 10.24 ? 105 LEU A N 1 ATOM 714 C CA . LEU A 1 88 ? 14.278 6.735 1.054 1.00 10.02 ? 105 LEU A CA 1 ATOM 715 C C . LEU A 1 88 ? 15.341 6.395 0.030 1.00 10.03 ? 105 LEU A C 1 ATOM 716 O O . LEU A 1 88 ? 16.154 7.234 -0.345 1.00 10.82 ? 105 LEU A O 1 ATOM 717 C CB . LEU A 1 88 ? 13.303 7.766 0.502 1.00 10.12 ? 105 LEU A CB 1 ATOM 718 C CG . LEU A 1 88 ? 12.555 7.459 -0.793 1.00 12.02 ? 105 LEU A CG 1 ATOM 719 C CD1 . LEU A 1 88 ? 11.650 6.230 -0.650 1.00 11.92 ? 105 LEU A CD1 1 ATOM 720 C CD2 . LEU A 1 88 ? 11.734 8.668 -1.146 1.00 11.88 ? 105 LEU A CD2 1 ATOM 721 N N . ILE A 1 89 ? 15.324 5.144 -0.404 1.00 9.81 ? 106 ILE A N 1 ATOM 722 C CA . ILE A 1 89 ? 16.356 4.608 -1.271 1.00 9.96 ? 106 ILE A CA 1 ATOM 723 C C . ILE A 1 89 ? 15.709 4.079 -2.530 1.00 9.90 ? 106 ILE A C 1 ATOM 724 O O . ILE A 1 89 ? 14.726 3.346 -2.466 1.00 10.65 ? 106 ILE A O 1 ATOM 725 C CB . ILE A 1 89 ? 17.111 3.468 -0.578 1.00 10.74 ? 106 ILE A CB 1 ATOM 726 C CG1 . ILE A 1 89 ? 17.944 4.027 0.569 1.00 12.41 ? 106 ILE A CG1 1 ATOM 727 C CG2 . ILE A 1 89 ? 18.031 2.745 -1.562 1.00 11.52 ? 106 ILE A CG2 1 ATOM 728 C CD1 . ILE A 1 89 ? 18.328 2.977 1.589 1.00 14.04 ? 106 ILE A CD1 1 ATOM 729 N N . ARG A 1 90 ? 16.265 4.457 -3.674 1.00 9.43 ? 107 ARG A N 1 ATOM 730 C CA . ARG A 1 90 ? 15.901 3.784 -4.904 1.00 9.15 ? 107 ARG A CA 1 ATOM 731 C C . ARG A 1 90 ? 16.920 2.704 -5.145 1.00 9.59 ? 107 ARG A C 1 ATOM 732 O O . ARG A 1 90 ? 18.126 2.931 -5.024 1.00 9.55 ? 107 ARG A O 1 ATOM 733 C CB . ARG A 1 90 ? 15.891 4.745 -6.088 1.00 9.64 ? 107 ARG A CB 1 ATOM 734 C CG . ARG A 1 90 ? 15.287 4.132 -7.333 1.00 11.06 ? 107 ARG A CG 1 ATOM 735 C CD . ARG A 1 90 ? 15.398 5.078 -8.486 1.00 12.65 ? 107 ARG A CD 1 ATOM 736 N NE . ARG A 1 90 ? 14.794 4.488 -9.681 1.00 14.49 ? 107 ARG A NE 1 ATOM 737 C CZ . ARG A 1 90 ? 14.689 5.130 -10.835 1.00 18.82 ? 107 ARG A CZ 1 ATOM 738 N NH1 . ARG A 1 90 ? 14.135 4.526 -11.882 1.00 19.21 ? 107 ARG A NH1 1 ATOM 739 N NH2 . ARG A 1 90 ? 15.141 6.373 -10.942 1.00 21.31 ? 107 ARG A NH2 1 ATOM 740 N N . LEU A 1 91 ? 16.412 1.520 -5.454 1.00 9.44 ? 108 LEU A N 1 ATOM 741 C CA . LEU A 1 91 ? 17.260 0.355 -5.684 1.00 10.44 ? 108 LEU A CA 1 ATOM 742 C C . LEU A 1 91 ? 17.922 0.465 -7.041 1.00 11.45 ? 108 LEU A C 1 ATOM 743 O O . LEU A 1 91 ? 17.417 1.154 -7.944 1.00 12.64 ? 108 LEU A O 1 ATOM 744 C CB . LEU A 1 91 ? 16.419 -0.913 -5.638 1.00 10.80 ? 108 LEU A CB 1 ATOM 745 C CG . LEU A 1 91 ? 15.658 -1.135 -4.337 1.00 11.05 ? 108 LEU A CG 1 ATOM 746 C CD1 . LEU A 1 91 ? 14.802 -2.383 -4.495 1.00 12.87 ? 108 LEU A CD1 1 ATOM 747 C CD2 . LEU A 1 91 ? 16.601 -1.227 -3.112 1.00 12.17 ? 108 LEU A CD2 1 ATOM 748 N N . ASN A 1 92 ? 19.052 -0.221 -7.189 1.00 11.43 ? 109 ASN A N 1 ATOM 749 C CA . ASN A 1 92 ? 19.788 -0.165 -8.454 1.00 12.25 ? 109 ASN A CA 1 ATOM 750 C C . ASN A 1 92 ? 19.022 -0.782 -9.612 1.00 12.47 ? 109 ASN A C 1 ATOM 751 O O . ASN A 1 92 ? 19.210 -0.380 -10.753 1.00 13.50 ? 109 ASN A O 1 ATOM 752 C CB . ASN A 1 92 ? 21.160 -0.824 -8.319 1.00 12.21 ? 109 ASN A CB 1 ATOM 753 C CG . ASN A 1 92 ? 21.074 -2.287 -7.918 1.00 12.17 ? 109 ASN A CG 1 ATOM 754 O OD1 . ASN A 1 92 ? 20.508 -2.633 -6.895 1.00 13.22 ? 109 ASN A OD1 1 ATOM 755 N ND2 . ASN A 1 92 ? 21.637 -3.162 -8.747 1.00 15.77 ? 109 ASN A ND2 1 ATOM 756 N N . ARG A 1 93 ? 18.197 -1.777 -9.311 1.00 12.86 ? 110 ARG A N 1 ATOM 757 C CA . ARG A 1 93 ? 17.334 -2.420 -10.287 1.00 13.55 ? 110 ARG A CA 1 ATOM 758 C C . ARG A 1 93 ? 16.031 -2.764 -9.602 1.00 13.66 ? 110 ARG A C 1 ATOM 759 O O . ARG A 1 93 ? 16.012 -3.032 -8.405 1.00 12.91 ? 110 ARG A O 1 ATOM 760 C CB . ARG A 1 93 ? 17.973 -3.710 -10.799 1.00 15.10 ? 110 ARG A CB 1 ATOM 761 C CG . ARG A 1 93 ? 19.101 -3.478 -11.786 1.00 18.83 ? 110 ARG A CG 1 ATOM 762 C CD . ARG A 1 93 ? 19.396 -4.748 -12.562 1.00 22.87 ? 110 ARG A CD 1 ATOM 763 N NE . ARG A 1 93 ? 19.639 -5.882 -11.678 1.00 25.39 ? 110 ARG A NE 1 ATOM 764 C CZ . ARG A 1 93 ? 20.815 -6.174 -11.126 1.00 28.90 ? 110 ARG A CZ 1 ATOM 765 N NH1 . ARG A 1 93 ? 20.926 -7.240 -10.343 1.00 30.36 ? 110 ARG A NH1 1 ATOM 766 N NH2 . ARG A 1 93 ? 21.885 -5.415 -11.361 1.00 29.85 ? 110 ARG A NH2 1 ATOM 767 N N . PRO A 1 94 ? 14.929 -2.751 -10.355 1.00 14.14 ? 111 PRO A N 1 ATOM 768 C CA . PRO A 1 94 ? 13.638 -3.080 -9.770 1.00 14.25 ? 111 PRO A CA 1 ATOM 769 C C . PRO A 1 94 ? 13.574 -4.523 -9.339 1.00 15.31 ? 111 PRO A C 1 ATOM 770 O O . PRO A 1 94 ? 14.395 -5.346 -9.762 1.00 14.64 ? 111 PRO A O 1 ATOM 771 C CB . PRO A 1 94 ? 12.657 -2.878 -10.922 1.00 14.20 ? 111 PRO A CB 1 ATOM 772 C CG . PRO A 1 94 ? 13.387 -2.080 -11.923 1.00 15.67 ? 111 PRO A CG 1 ATOM 773 C CD . PRO A 1 94 ? 14.825 -2.391 -11.779 1.00 14.44 ? 111 PRO A CD 1 ATOM 774 N N . VAL A 1 95 ? 12.591 -4.817 -8.505 1.00 15.59 ? 112 VAL A N 1 ATOM 775 C CA . VAL A 1 95 ? 12.309 -6.180 -8.082 1.00 17.28 ? 112 VAL A CA 1 ATOM 776 C C . VAL A 1 95 ? 10.856 -6.480 -8.394 1.00 18.20 ? 112 VAL A C 1 ATOM 777 O O . VAL A 1 95 ? 9.947 -5.743 -7.968 1.00 20.13 ? 112 VAL A O 1 ATOM 778 C CB . VAL A 1 95 ? 12.581 -6.398 -6.562 1.00 17.17 ? 112 VAL A CB 1 ATOM 779 C CG1 . VAL A 1 95 ? 14.030 -6.147 -6.251 1.00 16.37 ? 112 VAL A CG1 1 ATOM 780 C CG2 . VAL A 1 95 ? 11.696 -5.501 -5.675 1.00 18.95 ? 112 VAL A CG2 1 ATOM 781 N N . ARG A 1 96 ? 10.631 -7.578 -9.099 1.00 18.20 ? 113 ARG A N 1 ATOM 782 C CA . ARG A 1 96 ? 9.273 -7.969 -9.432 1.00 18.35 ? 113 ARG A CA 1 ATOM 783 C C . ARG A 1 96 ? 8.617 -8.730 -8.293 1.00 17.37 ? 113 ARG A C 1 ATOM 784 O O . ARG A 1 96 ? 9.304 -9.311 -7.453 1.00 16.70 ? 113 ARG A O 1 ATOM 785 C CB . ARG A 1 96 ? 9.250 -8.770 -10.735 1.00 19.57 ? 113 ARG A CB 1 ATOM 786 C CG . ARG A 1 96 ? 9.684 -7.923 -11.931 1.00 22.15 ? 113 ARG A CG 1 ATOM 787 C CD . ARG A 1 96 ? 8.735 -6.732 -12.095 0.50 24.71 ? 113 ARG A CD 1 ATOM 788 N NE . ARG A 1 96 ? 9.332 -5.458 -12.521 0.50 26.40 ? 113 ARG A NE 1 ATOM 789 C CZ . ARG A 1 96 ? 10.464 -5.299 -13.208 0.50 27.08 ? 113 ARG A CZ 1 ATOM 790 N NH1 . ARG A 1 96 ? 10.857 -4.073 -13.535 0.50 27.18 ? 113 ARG A NH1 1 ATOM 791 N NH2 . ARG A 1 96 ? 11.200 -6.341 -13.581 0.50 27.59 ? 113 ARG A NH2 1 ATOM 792 N N . ASN A 1 97 ? 7.286 -8.703 -8.263 1.00 16.61 ? 114 ASN A N 1 ATOM 793 C CA . ASN A 1 97 ? 6.532 -9.472 -7.297 1.00 16.57 ? 114 ASN A CA 1 ATOM 794 C C . ASN A 1 97 ? 6.801 -10.955 -7.496 1.00 16.62 ? 114 ASN A C 1 ATOM 795 O O . ASN A 1 97 ? 6.866 -11.449 -8.624 1.00 17.46 ? 114 ASN A O 1 ATOM 796 C CB . ASN A 1 97 ? 5.028 -9.194 -7.400 1.00 16.73 ? 114 ASN A CB 1 ATOM 797 C CG . ASN A 1 97 ? 4.633 -7.844 -6.797 1.00 17.11 ? 114 ASN A CG 1 ATOM 798 O OD1 . ASN A 1 97 ? 5.439 -6.913 -6.734 1.00 18.39 ? 114 ASN A OD1 1 ATOM 799 N ND2 . ASN A 1 97 ? 3.377 -7.729 -6.382 1.00 19.80 ? 114 ASN A ND2 1 ATOM 800 N N . SER A 1 98 ? 6.990 -11.646 -6.390 1.00 16.53 ? 115 SER A N 1 ATOM 801 C CA . SER A 1 98 ? 7.222 -13.081 -6.411 1.00 16.16 ? 115 SER A CA 1 ATOM 802 C C . SER A 1 98 ? 6.705 -13.634 -5.099 1.00 16.13 ? 115 SER A C 1 ATOM 803 O O . SER A 1 98 ? 6.150 -12.891 -4.284 1.00 15.88 ? 115 SER A O 1 ATOM 804 C CB . SER A 1 98 ? 8.706 -13.378 -6.617 1.00 16.63 ? 115 SER A CB 1 ATOM 805 O OG . SER A 1 98 ? 9.478 -12.815 -5.567 1.00 18.02 ? 115 SER A OG 1 ATOM 806 N N . ALA A 1 99 ? 6.865 -14.937 -4.879 1.00 15.70 ? 116 ALA A N 1 ATOM 807 C CA . ALA A 1 99 ? 6.307 -15.548 -3.686 1.00 15.64 ? 116 ALA A CA 1 ATOM 808 C C . ALA A 1 99 ? 6.675 -14.749 -2.448 1.00 15.13 ? 116 ALA A C 1 ATOM 809 O O . ALA A 1 99 ? 5.853 -14.575 -1.555 1.00 16.98 ? 116 ALA A O 1 ATOM 810 C CB . ALA A 1 99 ? 6.773 -17.003 -3.546 1.00 16.38 ? 116 ALA A CB 1 ATOM 811 N N . HIS A 1 100 ? 7.906 -14.244 -2.415 1.00 14.88 ? 117 HIS A N 1 ATOM 812 C CA . HIS A 1 100 ? 8.398 -13.603 -1.205 1.00 13.44 ? 117 HIS A CA 1 ATOM 813 C C . HIS A 1 100 ? 8.742 -12.152 -1.359 1.00 13.12 ? 117 HIS A C 1 ATOM 814 O O . HIS A 1 100 ? 9.350 -11.578 -0.466 1.00 12.74 ? 117 HIS A O 1 ATOM 815 C CB . HIS A 1 100 ? 9.601 -14.368 -0.688 1.00 13.42 ? 117 HIS A CB 1 ATOM 816 C CG . HIS A 1 100 ? 9.320 -15.821 -0.517 1.00 13.95 ? 117 HIS A CG 1 ATOM 817 N ND1 . HIS A 1 100 ? 9.923 -16.788 -1.292 1.00 14.33 ? 117 HIS A ND1 1 ATOM 818 C CD2 . HIS A 1 100 ? 8.455 -16.468 0.300 1.00 14.88 ? 117 HIS A CD2 1 ATOM 819 C CE1 . HIS A 1 100 ? 9.471 -17.974 -0.929 1.00 15.26 ? 117 HIS A CE1 1 ATOM 820 N NE2 . HIS A 1 100 ? 8.576 -17.810 0.029 1.00 15.79 ? 117 HIS A NE2 1 ATOM 821 N N . ILE A 1 101 ? 8.326 -11.547 -2.467 1.00 12.40 ? 118 ILE A N 1 ATOM 822 C CA . ILE A 1 101 ? 8.596 -10.144 -2.680 1.00 12.41 ? 118 ILE A CA 1 ATOM 823 C C . ILE A 1 101 ? 7.328 -9.455 -3.167 1.00 11.95 ? 118 ILE A C 1 ATOM 824 O O . ILE A 1 101 ? 6.724 -9.877 -4.154 1.00 12.77 ? 118 ILE A O 1 ATOM 825 C CB . ILE A 1 101 ? 9.726 -9.926 -3.701 1.00 12.39 ? 118 ILE A CB 1 ATOM 826 C CG1 . ILE A 1 101 ? 11.029 -10.564 -3.222 1.00 11.54 ? 118 ILE A CG1 1 ATOM 827 C CG2 . ILE A 1 101 ? 9.941 -8.436 -3.968 1.00 12.73 ? 118 ILE A CG2 1 ATOM 828 C CD1 . ILE A 1 101 ? 12.157 -10.488 -4.221 1.00 13.63 ? 118 ILE A CD1 1 ATOM 829 N N . ALA A 1 102 ? 6.926 -8.391 -2.473 1.00 11.96 ? 119 ALA A N 1 ATOM 830 C CA . ALA A 1 102 ? 5.835 -7.532 -2.956 1.00 11.62 ? 119 ALA A CA 1 ATOM 831 C C . ALA A 1 102 ? 5.902 -6.261 -2.126 1.00 11.28 ? 119 ALA A C 1 ATOM 832 O O . ALA A 1 102 ? 6.181 -6.329 -0.937 1.00 11.69 ? 119 ALA A O 1 ATOM 833 C CB . ALA A 1 102 ? 4.494 -8.196 -2.766 1.00 11.53 ? 119 ALA A CB 1 ATOM 834 N N . PRO A 1 103 ? 5.661 -5.099 -2.755 1.00 11.73 ? 120 PRO A N 1 ATOM 835 C CA . PRO A 1 103 ? 5.703 -3.854 -1.981 1.00 10.98 ? 120 PRO A CA 1 ATOM 836 C C . PRO A 1 103 ? 4.521 -3.637 -1.052 1.00 11.57 ? 120 PRO A C 1 ATOM 837 O O . PRO A 1 103 ? 3.461 -4.241 -1.222 1.00 12.64 ? 120 PRO A O 1 ATOM 838 C CB . PRO A 1 103 ? 5.715 -2.773 -3.055 1.00 11.95 ? 120 PRO A CB 1 ATOM 839 C CG . PRO A 1 103 ? 5.014 -3.394 -4.218 1.00 12.63 ? 120 PRO A CG 1 ATOM 840 C CD . PRO A 1 103 ? 5.386 -4.853 -4.183 1.00 12.11 ? 120 PRO A CD 1 ATOM 841 N N . LEU A 1 104 ? 4.727 -2.768 -0.074 1.00 10.19 ? 121 LEU A N 1 ATOM 842 C CA . LEU A 1 104 ? 3.677 -2.327 0.823 1.00 11.55 ? 121 LEU A CA 1 ATOM 843 C C . LEU A 1 104 ? 3.652 -0.826 0.629 1.00 11.66 ? 121 LEU A C 1 ATOM 844 O O . LEU A 1 104 ? 4.668 -0.167 0.800 1.00 12.36 ? 121 LEU A O 1 ATOM 845 C CB . LEU A 1 104 ? 4.039 -2.647 2.271 1.00 12.14 ? 121 LEU A CB 1 ATOM 846 C CG . LEU A 1 104 ? 2.972 -2.991 3.318 1.00 17.38 ? 121 LEU A CG 1 ATOM 847 C CD1 . LEU A 1 104 ? 3.485 -2.641 4.699 1.00 16.34 ? 121 LEU A CD1 1 ATOM 848 C CD2 . LEU A 1 104 ? 1.600 -2.447 3.073 1.00 17.00 ? 121 LEU A CD2 1 ATOM 849 N N . SER A 1 105 ? 2.497 -0.303 0.258 1.00 11.80 ? 122 SER A N 1 ATOM 850 C CA . SER A 1 105 ? 2.382 1.076 -0.173 1.00 13.08 ? 122 SER A CA 1 ATOM 851 C C . SER A 1 105 ? 2.143 2.020 0.991 1.00 11.87 ? 122 SER A C 1 ATOM 852 O O . SER A 1 105 ? 2.326 1.649 2.153 1.00 11.28 ? 122 SER A O 1 ATOM 853 C CB . SER A 1 105 ? 1.249 1.173 -1.197 1.00 14.07 ? 122 SER A CB 1 ATOM 854 O OG . SER A 1 105 ? 1.603 0.558 -2.422 1.00 17.93 ? 122 SER A OG 1 ATOM 855 N N . LEU A 1 106 ? 1.734 3.251 0.674 1.00 10.61 ? 123 LEU A N 1 ATOM 856 C CA . LEU A 1 106 ? 1.719 4.316 1.661 1.00 10.51 ? 123 LEU A CA 1 ATOM 857 C C . LEU A 1 106 ? 0.395 4.364 2.395 1.00 10.52 ? 123 LEU A C 1 ATOM 858 O O . LEU A 1 106 ? -0.662 4.152 1.807 1.00 9.83 ? 123 LEU A O 1 ATOM 859 C CB . LEU A 1 106 ? 2.010 5.653 0.984 1.00 10.60 ? 123 LEU A CB 1 ATOM 860 C CG . LEU A 1 106 ? 3.387 5.689 0.310 1.00 10.62 ? 123 LEU A CG 1 ATOM 861 C CD1 . LEU A 1 106 ? 3.625 7.087 -0.263 1.00 11.61 ? 123 LEU A CD1 1 ATOM 862 C CD2 . LEU A 1 106 ? 4.542 5.269 1.260 1.00 11.02 ? 123 LEU A CD2 1 ATOM 863 N N . PRO A 1 107 ? 0.445 4.653 3.700 1.00 10.27 ? 124 PRO A N 1 ATOM 864 C CA . PRO A 1 107 ? -0.776 4.619 4.482 1.00 10.80 ? 124 PRO A CA 1 ATOM 865 C C . PRO A 1 107 ? -1.731 5.737 4.109 1.00 11.13 ? 124 PRO A C 1 ATOM 866 O O . PRO A 1 107 ? -1.312 6.835 3.746 1.00 10.28 ? 124 PRO A O 1 ATOM 867 C CB . PRO A 1 107 ? -0.279 4.805 5.920 1.00 11.23 ? 124 PRO A CB 1 ATOM 868 C CG . PRO A 1 107 ? 0.983 5.613 5.747 1.00 10.69 ? 124 PRO A CG 1 ATOM 869 C CD . PRO A 1 107 ? 1.618 5.053 4.511 1.00 10.25 ? 124 PRO A CD 1 ATOM 870 N N . SER A 1 108 ? -3.015 5.442 4.213 1.00 12.62 ? 125 SER A N 1 ATOM 871 C CA . SER A 1 108 ? -4.052 6.420 3.896 1.00 13.57 ? 125 SER A CA 1 ATOM 872 C C . SER A 1 108 ? -4.356 7.300 5.099 1.00 13.68 ? 125 SER A C 1 ATOM 873 O O . SER A 1 108 ? -5.017 8.313 4.985 1.00 14.08 ? 125 SER A O 1 ATOM 874 C CB . SER A 1 108 ? -5.310 5.693 3.443 1.00 13.96 ? 125 SER A CB 1 ATOM 875 O OG . SER A 1 108 ? -5.699 4.769 4.436 1.00 15.92 ? 125 SER A OG 1 ATOM 876 N N . ASN A 1 109 ? -3.863 6.906 6.266 1.00 13.48 ? 127 ASN A N 1 ATOM 877 C CA . ASN A 1 109 ? -4.136 7.620 7.498 1.00 13.78 ? 127 ASN A CA 1 ATOM 878 C C . ASN A 1 109 ? -3.178 7.108 8.555 1.00 13.94 ? 127 ASN A C 1 ATOM 879 O O . ASN A 1 109 ? -2.694 5.985 8.419 1.00 13.62 ? 127 ASN A O 1 ATOM 880 C CB . ASN A 1 109 ? -5.575 7.363 7.942 1.00 13.81 ? 127 ASN A CB 1 ATOM 881 C CG . ASN A 1 109 ? -5.856 5.892 8.142 1.00 13.29 ? 127 ASN A CG 1 ATOM 882 O OD1 . ASN A 1 109 ? -6.070 5.156 7.190 1.00 14.52 ? 127 ASN A OD1 1 ATOM 883 N ND2 . ASN A 1 109 ? -5.822 5.452 9.397 1.00 15.97 ? 127 ASN A ND2 1 ATOM 884 N N . PRO A 1 110 ? -2.913 7.918 9.597 1.00 14.23 ? 128 PRO A N 1 ATOM 885 C CA . PRO A 1 110 ? -2.109 7.386 10.685 1.00 14.36 ? 128 PRO A CA 1 ATOM 886 C C . PRO A 1 110 ? -2.982 6.497 11.575 1.00 14.88 ? 128 PRO A C 1 ATOM 887 O O . PRO A 1 110 ? -4.209 6.602 11.527 1.00 14.74 ? 128 PRO A O 1 ATOM 888 C CB . PRO A 1 110 ? -1.666 8.638 11.434 1.00 15.31 ? 128 PRO A CB 1 ATOM 889 C CG . PRO A 1 110 ? -2.731 9.617 11.207 1.00 15.14 ? 128 PRO A CG 1 ATOM 890 C CD . PRO A 1 110 ? -3.322 9.311 9.849 1.00 14.29 ? 128 PRO A CD 1 ATOM 891 N N . PRO A 1 111 ? -2.357 5.616 12.369 1.00 14.61 ? 129 PRO A N 1 ATOM 892 C CA . PRO A 1 111 ? -3.136 4.635 13.100 1.00 14.65 ? 129 PRO A CA 1 ATOM 893 C C . PRO A 1 111 ? -3.658 5.183 14.421 1.00 14.77 ? 129 PRO A C 1 ATOM 894 O O . PRO A 1 111 ? -2.974 5.959 15.092 1.00 15.68 ? 129 PRO A O 1 ATOM 895 C CB . PRO A 1 111 ? -2.117 3.536 13.379 1.00 14.47 ? 129 PRO A CB 1 ATOM 896 C CG . PRO A 1 111 ? -0.842 4.279 13.560 1.00 14.69 ? 129 PRO A CG 1 ATOM 897 C CD . PRO A 1 111 ? -0.910 5.474 12.625 1.00 14.57 ? 129 PRO A CD 1 ATOM 898 N N . SER A 1 112 ? -4.859 4.763 14.801 1.00 14.64 ? 131 SER A N 1 ATOM 899 C CA . SER A 1 112 ? -5.397 5.119 16.103 1.00 14.89 ? 131 SER A CA 1 ATOM 900 C C . SER A 1 112 ? -4.564 4.531 17.211 1.00 13.87 ? 131 SER A C 1 ATOM 901 O O . SER A 1 112 ? -4.075 3.419 17.098 1.00 13.05 ? 131 SER A O 1 ATOM 902 C CB . SER A 1 112 ? -6.809 4.576 16.250 1.00 15.74 ? 131 SER A CB 1 ATOM 903 O OG . SER A 1 112 ? -7.650 5.134 15.260 1.00 19.81 ? 131 SER A OG 1 ATOM 904 N N . VAL A 1 113 ? -4.400 5.302 18.282 1.00 12.82 ? 132 VAL A N 1 ATOM 905 C CA . VAL A 1 113 ? -3.901 4.751 19.523 1.00 12.51 ? 132 VAL A CA 1 ATOM 906 C C . VAL A 1 113 ? -4.736 3.529 19.871 1.00 12.04 ? 132 VAL A C 1 ATOM 907 O O . VAL A 1 113 ? -5.963 3.537 19.727 1.00 12.70 ? 132 VAL A O 1 ATOM 908 C CB . VAL A 1 113 ? -3.961 5.792 20.647 1.00 12.88 ? 132 VAL A CB 1 ATOM 909 C CG1 . VAL A 1 113 ? -3.642 5.164 21.980 1.00 12.94 ? 132 VAL A CG1 1 ATOM 910 C CG2 . VAL A 1 113 ? -2.991 6.903 20.334 1.00 13.63 ? 132 VAL A CG2 1 ATOM 911 N N . GLY A 1 114 ? -4.063 2.469 20.285 1.00 12.16 ? 133 GLY A N 1 ATOM 912 C CA . GLY A 1 114 ? -4.733 1.212 20.587 1.00 12.42 ? 133 GLY A CA 1 ATOM 913 C C . GLY A 1 114 ? -4.707 0.205 19.463 1.00 13.00 ? 133 GLY A C 1 ATOM 914 O O . GLY A 1 114 ? -4.985 -0.979 19.686 1.00 14.12 ? 133 GLY A O 1 ATOM 915 N N . SER A 1 115 ? -4.391 0.665 18.248 1.00 12.59 ? 134 SER A N 1 ATOM 916 C CA . SER A 1 115 ? -4.328 -0.228 17.091 1.00 12.90 ? 134 SER A CA 1 ATOM 917 C C . SER A 1 115 ? -3.326 -1.328 17.357 1.00 12.73 ? 134 SER A C 1 ATOM 918 O O . SER A 1 115 ? -2.297 -1.093 17.974 1.00 12.59 ? 134 SER A O 1 ATOM 919 C CB . SER A 1 115 ? -3.878 0.509 15.835 1.00 12.97 ? 134 SER A CB 1 ATOM 920 O OG . SER A 1 115 ? -4.840 1.458 15.453 1.00 15.60 ? 134 SER A OG 1 ATOM 921 N N . VAL A 1 116 ? -3.631 -2.524 16.870 1.00 12.46 ? 135 VAL A N 1 ATOM 922 C CA . VAL A 1 116 ? -2.676 -3.613 16.898 1.00 13.14 ? 135 VAL A CA 1 ATOM 923 C C . VAL A 1 116 ? -1.761 -3.462 15.701 1.00 12.49 ? 135 VAL A C 1 ATOM 924 O O . VAL A 1 116 ? -2.210 -3.222 14.578 1.00 13.56 ? 135 VAL A O 1 ATOM 925 C CB . VAL A 1 116 ? -3.384 -4.971 16.834 1.00 13.19 ? 135 VAL A CB 1 ATOM 926 C CG1 . VAL A 1 116 ? -2.364 -6.095 16.812 1.00 14.75 ? 135 VAL A CG1 1 ATOM 927 C CG2 . VAL A 1 116 ? -4.304 -5.128 18.046 1.00 15.26 ? 135 VAL A CG2 1 ATOM 928 N N . CYS A 1 117 ? -0.467 -3.603 15.959 1.00 11.93 ? 136 CYS A N 1 ATOM 929 C CA . CYS A 1 117 ? 0.527 -3.509 14.904 1.00 12.00 ? 136 CYS A CA 1 ATOM 930 C C . CYS A 1 117 ? 1.424 -4.717 14.931 1.00 11.99 ? 136 CYS A C 1 ATOM 931 O O . CYS A 1 117 ? 1.674 -5.299 15.975 1.00 12.87 ? 136 CYS A O 1 ATOM 932 C CB . CYS A 1 117 ? 1.410 -2.286 15.094 1.00 11.92 ? 136 CYS A CB 1 ATOM 933 S SG . CYS A 1 117 ? 0.476 -0.773 15.290 1.00 13.99 ? 136 CYS A SG 1 ATOM 934 N N . ARG A 1 118 ? 1.911 -5.080 13.764 1.00 11.58 ? 137 ARG A N 1 ATOM 935 C CA . ARG A 1 118 ? 2.929 -6.093 13.645 1.00 11.74 ? 137 ARG A CA 1 ATOM 936 C C . ARG A 1 118 ? 4.294 -5.427 13.593 1.00 11.00 ? 137 ARG A C 1 ATOM 937 O O . ARG A 1 118 ? 4.484 -4.444 12.890 1.00 10.57 ? 137 ARG A O 1 ATOM 938 C CB . ARG A 1 118 ? 2.733 -6.865 12.346 1.00 12.42 ? 137 ARG A CB 1 ATOM 939 C CG . ARG A 1 118 ? 3.444 -8.199 12.284 1.00 14.96 ? 137 ARG A CG 1 ATOM 940 C CD . ARG A 1 118 ? 2.715 -9.189 13.163 1.00 17.42 ? 137 ARG A CD 1 ATOM 941 N NE . ARG A 1 118 ? 3.030 -10.564 12.806 1.00 18.19 ? 137 ARG A NE 1 ATOM 942 C CZ . ARG A 1 118 ? 2.903 -11.590 13.647 1.00 20.25 ? 137 ARG A CZ 1 ATOM 943 N NH1 . ARG A 1 118 ? 2.486 -11.385 14.891 1.00 19.17 ? 137 ARG A NH1 1 ATOM 944 N NH2 . ARG A 1 118 ? 3.219 -12.823 13.248 1.00 19.61 ? 137 ARG A NH2 1 ATOM 945 N N . ILE A 1 119 ? 5.240 -5.989 14.335 1.00 10.32 ? 138 ILE A N 1 ATOM 946 C CA . ILE A 1 119 ? 6.640 -5.632 14.186 1.00 9.93 ? 138 ILE A CA 1 ATOM 947 C C . ILE A 1 119 ? 7.394 -6.859 13.707 1.00 10.99 ? 138 ILE A C 1 ATOM 948 O O . ILE A 1 119 ? 6.946 -8.005 13.875 1.00 10.82 ? 138 ILE A O 1 ATOM 949 C CB . ILE A 1 119 ? 7.249 -5.101 15.493 1.00 9.92 ? 138 ILE A CB 1 ATOM 950 C CG1 . ILE A 1 119 ? 6.890 -6.013 16.668 1.00 10.06 ? 138 ILE A CG1 1 ATOM 951 C CG2 . ILE A 1 119 ? 6.777 -3.683 15.736 1.00 11.78 ? 138 ILE A CG2 1 ATOM 952 C CD1 . ILE A 1 119 ? 7.741 -5.769 17.902 1.00 11.73 ? 138 ILE A CD1 1 ATOM 953 N N . MET A 1 120 ? 8.530 -6.615 13.082 1.00 10.23 ? 139 MET A N 1 ATOM 954 C CA . MET A 1 120 ? 9.265 -7.702 12.462 1.00 11.08 ? 139 MET A CA 1 ATOM 955 C C . MET A 1 120 ? 10.666 -7.278 12.201 1.00 10.81 ? 139 MET A C 1 ATOM 956 O O . MET A 1 120 ? 10.943 -6.114 11.919 1.00 10.84 ? 139 MET A O 1 ATOM 957 C CB . MET A 1 120 ? 8.653 -8.079 11.128 1.00 10.84 ? 139 MET A CB 1 ATOM 958 C CG . MET A 1 120 ? 8.464 -6.896 10.181 1.00 11.80 ? 139 MET A CG 1 ATOM 959 S SD . MET A 1 120 ? 7.492 -7.378 8.748 1.00 13.21 ? 139 MET A SD 1 ATOM 960 C CE . MET A 1 120 ? 5.867 -7.618 9.447 1.00 16.78 ? 139 MET A CE 1 ATOM 961 N N . GLY A 1 121 ? 11.555 -8.255 12.248 1.00 10.51 ? 140 GLY A N 1 ATOM 962 C CA . GLY A 1 121 ? 12.922 -7.986 11.870 1.00 10.36 ? 140 GLY A CA 1 ATOM 963 C C . GLY A 1 121 ? 13.852 -9.106 12.241 1.00 10.78 ? 140 GLY A C 1 ATOM 964 O O . GLY A 1 121 ? 13.466 -10.068 12.900 1.00 10.40 ? 140 GLY A O 1 ATOM 965 N N . TRP A 1 122 ? 15.090 -8.953 11.809 1.00 11.08 ? 141 TRP A N 1 ATOM 966 C CA . TRP A 1 122 ? 16.103 -9.931 12.123 1.00 11.32 ? 141 TRP A CA 1 ATOM 967 C C . TRP A 1 122 ? 16.964 -9.459 13.284 1.00 11.98 ? 141 TRP A C 1 ATOM 968 O O . TRP A 1 122 ? 18.056 -9.976 13.511 1.00 11.19 ? 141 TRP A O 1 ATOM 969 C CB . TRP A 1 122 ? 16.990 -10.155 10.912 1.00 11.76 ? 141 TRP A CB 1 ATOM 970 C CG . TRP A 1 122 ? 16.373 -10.894 9.795 1.00 11.66 ? 141 TRP A CG 1 ATOM 971 C CD1 . TRP A 1 122 ? 16.418 -12.235 9.589 1.00 12.39 ? 141 TRP A CD1 1 ATOM 972 C CD2 . TRP A 1 122 ? 15.648 -10.337 8.685 1.00 11.27 ? 141 TRP A CD2 1 ATOM 973 N NE1 . TRP A 1 122 ? 15.769 -12.562 8.421 1.00 13.04 ? 141 TRP A NE1 1 ATOM 974 C CE2 . TRP A 1 122 ? 15.290 -11.416 7.842 1.00 12.13 ? 141 TRP A CE2 1 ATOM 975 C CE3 . TRP A 1 122 ? 15.296 -9.035 8.310 1.00 11.91 ? 141 TRP A CE3 1 ATOM 976 C CZ2 . TRP A 1 122 ? 14.584 -11.231 6.656 1.00 12.53 ? 141 TRP A CZ2 1 ATOM 977 C CZ3 . TRP A 1 122 ? 14.595 -8.863 7.129 1.00 12.28 ? 141 TRP A CZ3 1 ATOM 978 C CH2 . TRP A 1 122 ? 14.243 -9.955 6.325 1.00 12.88 ? 141 TRP A CH2 1 ATOM 979 N N . GLY A 1 123 ? 16.465 -8.478 14.027 1.00 11.52 ? 142 GLY A N 1 ATOM 980 C CA . GLY A 1 123 ? 17.194 -7.946 15.167 1.00 11.58 ? 142 GLY A CA 1 ATOM 981 C C . GLY A 1 123 ? 17.224 -8.917 16.317 1.00 11.79 ? 142 GLY A C 1 ATOM 982 O O . GLY A 1 123 ? 16.641 -10.006 16.266 1.00 11.88 ? 142 GLY A O 1 ATOM 983 N N . THR A 1 124 ? 17.944 -8.524 17.356 1.00 11.94 ? 143 THR A N 1 ATOM 984 C CA . THR A 1 124 ? 18.138 -9.407 18.488 1.00 12.72 ? 143 THR A CA 1 ATOM 985 C C . THR A 1 124 ? 16.820 -9.846 19.113 1.00 13.18 ? 143 THR A C 1 ATOM 986 O O . THR A 1 124 ? 15.848 -9.078 19.166 1.00 13.05 ? 143 THR A O 1 ATOM 987 C CB . THR A 1 124 ? 19.070 -8.807 19.540 1.00 13.17 ? 143 THR A CB 1 ATOM 988 O OG1 . THR A 1 124 ? 19.246 -9.780 20.572 1.00 13.50 ? 143 THR A OG1 1 ATOM 989 C CG2 . THR A 1 124 ? 18.500 -7.526 20.146 1.00 14.18 ? 143 THR A CG2 1 ATOM 990 N N . ILE A 1 125 ? 16.795 -11.098 19.566 1.00 13.53 ? 144 ILE A N 1 ATOM 991 C CA . ILE A 1 125 ? 15.613 -11.645 20.204 1.00 14.29 ? 144 ILE A CA 1 ATOM 992 C C . ILE A 1 125 ? 15.825 -11.711 21.712 1.00 14.40 ? 144 ILE A C 1 ATOM 993 O O . ILE A 1 125 ? 14.937 -12.125 22.450 1.00 15.42 ? 144 ILE A O 1 ATOM 994 C CB . ILE A 1 125 ? 15.206 -13.023 19.643 1.00 14.47 ? 144 ILE A CB 1 ATOM 995 C CG1 . ILE A 1 125 ? 16.304 -14.073 19.875 1.00 16.74 ? 144 ILE A CG1 1 ATOM 996 C CG2 . ILE A 1 125 ? 14.866 -12.912 18.158 1.00 14.83 ? 144 ILE A CG2 1 ATOM 997 C CD1 . ILE A 1 125 ? 15.817 -15.484 19.572 1.00 17.14 ? 144 ILE A CD1 1 ATOM 998 N N . THR A 1 126 ? 17.012 -11.290 22.142 1.00 15.14 ? 145 THR A N 1 ATOM 999 C CA . THR A 1 126 ? 17.304 -11.117 23.558 1.00 15.54 ? 145 THR A CA 1 ATOM 1000 C C . THR A 1 126 ? 17.850 -9.719 23.799 1.00 15.67 ? 145 THR A C 1 ATOM 1001 O O . THR A 1 126 ? 18.473 -9.115 22.919 1.00 15.55 ? 145 THR A O 1 ATOM 1002 C CB . THR A 1 126 ? 18.363 -12.115 24.072 1.00 15.52 ? 145 THR A CB 1 ATOM 1003 O OG1 . THR A 1 126 ? 19.539 -12.003 23.265 1.00 17.11 ? 145 THR A OG1 1 ATOM 1004 C CG2 . THR A 1 126 ? 17.836 -13.542 24.051 1.00 16.86 ? 145 THR A CG2 1 ATOM 1005 N N . SER A 1 127 ? 17.619 -9.218 25.008 1.00 15.85 ? 146 SER A N 1 ATOM 1006 C CA . SER A 1 127 ? 18.074 -7.902 25.395 1.00 16.48 ? 146 SER A CA 1 ATOM 1007 C C . SER A 1 127 ? 18.077 -7.863 26.899 1.00 17.22 ? 146 SER A C 1 ATOM 1008 O O . SER A 1 127 ? 17.035 -8.073 27.506 1.00 17.08 ? 146 SER A O 1 ATOM 1009 C CB . SER A 1 127 ? 17.139 -6.811 24.875 1.00 16.12 ? 146 SER A CB 1 ATOM 1010 O OG . SER A 1 127 ? 17.643 -5.540 25.229 1.00 17.25 ? 146 SER A OG 1 ATOM 1011 N N . PRO A 1 128 ? 19.248 -7.600 27.502 1.00 18.42 ? 147 PRO A N 1 ATOM 1012 C CA . PRO A 1 128 ? 20.524 -7.304 26.861 1.00 19.52 ? 147 PRO A CA 1 ATOM 1013 C C . PRO A 1 128 ? 21.186 -8.548 26.262 1.00 20.70 ? 147 PRO A C 1 ATOM 1014 O O . PRO A 1 128 ? 20.635 -9.644 26.372 1.00 21.12 ? 147 PRO A O 1 ATOM 1015 C CB . PRO A 1 128 ? 21.360 -6.744 28.014 1.00 19.26 ? 147 PRO A CB 1 ATOM 1016 C CG . PRO A 1 128 ? 20.788 -7.349 29.226 1.00 18.96 ? 147 PRO A CG 1 ATOM 1017 C CD . PRO A 1 128 ? 19.352 -7.600 28.973 1.00 18.88 ? 147 PRO A CD 1 ATOM 1018 N N . ASN A 1 129 ? 22.342 -8.361 25.626 1.00 22.16 ? 148 ASN A N 1 ATOM 1019 C CA . ASN A 1 129 ? 23.102 -9.448 24.997 1.00 24.14 ? 148 ASN A CA 1 ATOM 1020 C C . ASN A 1 129 ? 22.448 -9.884 23.695 1.00 23.68 ? 148 ASN A C 1 ATOM 1021 O O . ASN A 1 129 ? 21.375 -10.487 23.713 1.00 25.26 ? 148 ASN A O 1 ATOM 1022 C CB . ASN A 1 129 ? 23.249 -10.668 25.927 1.00 25.32 ? 148 ASN A CB 1 ATOM 1023 C CG . ASN A 1 129 ? 23.756 -10.305 27.308 1.00 29.63 ? 148 ASN A CG 1 ATOM 1024 O OD1 . ASN A 1 129 ? 23.063 -10.529 28.310 1.00 32.19 ? 148 ASN A OD1 1 ATOM 1025 N ND2 . ASN A 1 129 ? 24.965 -9.738 27.370 1.00 33.76 ? 148 ASN A ND2 1 ATOM 1026 N N . ALA A 1 130 ? 23.106 -9.602 22.575 1.00 22.72 ? 149 ALA A N 1 ATOM 1027 C CA . ALA A 1 130 ? 22.566 -9.907 21.247 1.00 21.82 ? 149 ALA A CA 1 ATOM 1028 C C . ALA A 1 130 ? 22.416 -11.401 20.979 1.00 20.97 ? 149 ALA A C 1 ATOM 1029 O O . ALA A 1 130 ? 23.332 -12.191 21.239 1.00 22.19 ? 149 ALA A O 1 ATOM 1030 C CB . ALA A 1 130 ? 23.425 -9.275 20.171 1.00 22.14 ? 149 ALA A CB 1 ATOM 1031 N N . THR A 1 131 ? 21.244 -11.772 20.477 1.00 19.59 ? 150 THR A N 1 ATOM 1032 C CA . THR A 1 131 ? 21.000 -13.088 19.911 1.00 18.43 ? 150 THR A CA 1 ATOM 1033 C C . THR A 1 131 ? 20.302 -12.845 18.593 1.00 17.82 ? 150 THR A C 1 ATOM 1034 O O . THR A 1 131 ? 19.120 -12.507 18.562 1.00 17.31 ? 150 THR A O 1 ATOM 1035 C CB . THR A 1 131 ? 20.120 -13.955 20.810 1.00 18.48 ? 150 THR A CB 1 ATOM 1036 O OG1 . THR A 1 131 ? 20.748 -14.093 22.088 1.00 19.39 ? 150 THR A OG1 1 ATOM 1037 C CG2 . THR A 1 131 ? 19.936 -15.340 20.213 1.00 19.49 ? 150 THR A CG2 1 ATOM 1038 N N . LEU A 1 132 ? 21.051 -12.985 17.505 1.00 17.14 ? 151 LEU A N 1 ATOM 1039 C CA . LEU A 1 132 ? 20.510 -12.697 16.190 1.00 16.91 ? 151 LEU A CA 1 ATOM 1040 C C . LEU A 1 132 ? 19.890 -13.949 15.595 1.00 16.75 ? 151 LEU A C 1 ATOM 1041 O O . LEU A 1 132 ? 20.561 -14.981 15.468 1.00 16.81 ? 151 LEU A O 1 ATOM 1042 C CB . LEU A 1 132 ? 21.594 -12.157 15.269 1.00 17.00 ? 151 LEU A CB 1 ATOM 1043 C CG . LEU A 1 132 ? 22.239 -10.846 15.697 1.00 17.94 ? 151 LEU A CG 1 ATOM 1044 C CD1 . LEU A 1 132 ? 23.214 -10.390 14.639 1.00 19.23 ? 151 LEU A CD1 1 ATOM 1045 C CD2 . LEU A 1 132 ? 21.184 -9.771 15.970 1.00 18.59 ? 151 LEU A CD2 1 ATOM 1046 N N . PRO A 1 133 ? 18.599 -13.873 15.234 1.00 16.30 ? 152 PRO A N 1 ATOM 1047 C CA . PRO A 1 133 ? 17.902 -15.026 14.670 1.00 16.01 ? 152 PRO A CA 1 ATOM 1048 C C . PRO A 1 133 ? 18.248 -15.247 13.200 1.00 16.11 ? 152 PRO A C 1 ATOM 1049 O O . PRO A 1 133 ? 18.680 -14.311 12.510 1.00 15.99 ? 152 PRO A O 1 ATOM 1050 C CB . PRO A 1 133 ? 16.430 -14.640 14.805 1.00 16.20 ? 152 PRO A CB 1 ATOM 1051 C CG . PRO A 1 133 ? 16.432 -13.149 14.687 1.00 16.12 ? 152 PRO A CG 1 ATOM 1052 C CD . PRO A 1 133 ? 17.707 -12.696 15.360 1.00 15.96 ? 152 PRO A CD 1 ATOM 1053 N N . ASP A 1 134 ? 18.057 -16.479 12.736 1.00 15.97 ? 153 ASP A N 1 ATOM 1054 C CA . ASP A 1 134 ? 18.244 -16.793 11.323 1.00 16.46 ? 153 ASP A CA 1 ATOM 1055 C C . ASP A 1 134 ? 17.024 -16.394 10.516 1.00 15.75 ? 153 ASP A C 1 ATOM 1056 O O . ASP A 1 134 ? 17.115 -16.160 9.316 1.00 15.30 ? 153 ASP A O 1 ATOM 1057 C CB . ASP A 1 134 ? 18.442 -18.294 11.129 1.00 17.45 ? 153 ASP A CB 1 ATOM 1058 C CG . ASP A 1 134 ? 19.697 -18.818 11.780 1.00 20.06 ? 153 ASP A CG 1 ATOM 1059 O OD1 . ASP A 1 134 ? 20.674 -18.059 11.938 1.00 22.13 ? 153 ASP A OD1 1 ATOM 1060 O OD2 . ASP A 1 134 ? 19.699 -20.025 12.100 1.00 24.41 ? 153 ASP A OD2 1 ATOM 1061 N N . VAL A 1 135 ? 15.875 -16.363 11.182 1.00 14.96 ? 154 VAL A N 1 ATOM 1062 C CA . VAL A 1 135 ? 14.624 -16.031 10.531 1.00 14.40 ? 154 VAL A CA 1 ATOM 1063 C C . VAL A 1 135 ? 14.084 -14.769 11.187 1.00 13.70 ? 154 VAL A C 1 ATOM 1064 O O . VAL A 1 135 ? 14.333 -14.539 12.374 1.00 13.88 ? 154 VAL A O 1 ATOM 1065 C CB . VAL A 1 135 ? 13.594 -17.179 10.657 1.00 15.38 ? 154 VAL A CB 1 ATOM 1066 C CG1 . VAL A 1 135 ? 14.026 -18.379 9.824 1.00 14.85 ? 154 VAL A CG1 1 ATOM 1067 C CG2 . VAL A 1 135 ? 13.410 -17.592 12.117 1.00 15.00 ? 154 VAL A CG2 1 ATOM 1068 N N . PRO A 1 136 ? 13.338 -13.958 10.426 1.00 12.98 ? 155 PRO A N 1 ATOM 1069 C CA . PRO A 1 136 ? 12.835 -12.736 11.077 1.00 12.81 ? 155 PRO A CA 1 ATOM 1070 C C . PRO A 1 136 ? 11.823 -13.136 12.126 1.00 13.18 ? 155 PRO A C 1 ATOM 1071 O O . PRO A 1 136 ? 11.087 -14.111 11.941 1.00 13.47 ? 155 PRO A O 1 ATOM 1072 C CB . PRO A 1 136 ? 12.177 -11.958 9.927 1.00 12.31 ? 155 PRO A CB 1 ATOM 1073 C CG . PRO A 1 136 ? 11.797 -13.025 8.936 1.00 12.55 ? 155 PRO A CG 1 ATOM 1074 C CD . PRO A 1 136 ? 12.872 -14.081 9.036 1.00 13.72 ? 155 PRO A CD 1 ATOM 1075 N N . HIS A 1 137 ? 11.813 -12.414 13.243 1.00 12.70 ? 156 HIS A N 1 ATOM 1076 C CA . HIS A 1 137 ? 10.789 -12.613 14.261 1.00 12.97 ? 156 HIS A CA 1 ATOM 1077 C C . HIS A 1 137 ? 9.759 -11.510 14.178 1.00 12.96 ? 156 HIS A C 1 ATOM 1078 O O . HIS A 1 137 ? 10.058 -10.398 13.734 1.00 12.43 ? 156 HIS A O 1 ATOM 1079 C CB . HIS A 1 137 ? 11.414 -12.680 15.643 1.00 13.56 ? 156 HIS A CB 1 ATOM 1080 C CG . HIS A 1 137 ? 12.034 -14.007 15.935 1.00 14.77 ? 156 HIS A CG 1 ATOM 1081 N ND1 . HIS A 1 137 ? 11.866 -14.655 17.140 1.00 17.85 ? 156 HIS A ND1 1 ATOM 1082 C CD2 . HIS A 1 137 ? 12.803 -14.820 15.169 1.00 17.06 ? 156 HIS A CD2 1 ATOM 1083 C CE1 . HIS A 1 137 ? 12.511 -15.810 17.106 1.00 18.24 ? 156 HIS A CE1 1 ATOM 1084 N NE2 . HIS A 1 137 ? 13.078 -15.938 15.921 1.00 18.29 ? 156 HIS A NE2 1 ATOM 1085 N N . CYS A 1 138 ? 8.552 -11.853 14.596 1.00 12.27 ? 157 CYS A N 1 ATOM 1086 C CA . CYS A 1 138 ? 7.383 -10.998 14.464 1.00 12.60 ? 157 CYS A CA 1 ATOM 1087 C C . CYS A 1 138 ? 6.663 -11.009 15.774 1.00 12.50 ? 157 CYS A C 1 ATOM 1088 O O . CYS A 1 138 ? 6.663 -12.011 16.487 1.00 12.32 ? 157 CYS A O 1 ATOM 1089 C CB . CYS A 1 138 ? 6.440 -11.578 13.419 1.00 13.16 ? 157 CYS A CB 1 ATOM 1090 S SG . CYS A 1 138 ? 6.768 -11.108 11.718 1.00 15.54 ? 157 CYS A SG 1 ATOM 1091 N N . ALA A 1 139 ? 6.037 -9.887 16.094 1.00 11.60 ? 158 ALA A N 1 ATOM 1092 C CA . ALA A 1 139 ? 5.210 -9.807 17.274 1.00 11.67 ? 158 ALA A CA 1 ATOM 1093 C C . ALA A 1 139 ? 4.104 -8.807 17.034 1.00 12.18 ? 158 ALA A C 1 ATOM 1094 O O . ALA A 1 139 ? 4.185 -7.981 16.122 1.00 11.98 ? 158 ALA A O 1 ATOM 1095 C CB . ALA A 1 139 ? 6.029 -9.401 18.490 1.00 11.85 ? 158 ALA A CB 1 ATOM 1096 N N . ASN A 1 140 ? 3.055 -8.919 17.848 1.00 11.83 ? 159 ASN A N 1 ATOM 1097 C CA . ASN A 1 140 ? 1.995 -7.927 17.854 1.00 12.42 ? 159 ASN A CA 1 ATOM 1098 C C . ASN A 1 140 ? 2.171 -7.004 19.029 1.00 12.62 ? 159 ASN A C 1 ATOM 1099 O O . ASN A 1 140 ? 2.350 -7.447 20.170 1.00 13.27 ? 159 ASN A O 1 ATOM 1100 C CB . ASN A 1 140 ? 0.626 -8.594 17.943 1.00 13.15 ? 159 ASN A CB 1 ATOM 1101 C CG . ASN A 1 140 ? 0.316 -9.434 16.729 1.00 14.81 ? 159 ASN A CG 1 ATOM 1102 O OD1 . ASN A 1 140 ? 0.709 -9.102 15.611 1.00 16.19 ? 159 ASN A OD1 1 ATOM 1103 N ND2 . ASN A 1 140 ? -0.383 -10.545 16.945 1.00 20.54 ? 159 ASN A ND2 1 ATOM 1104 N N . ILE A 1 141 ? 2.133 -5.718 18.716 1.00 11.49 ? 160 ILE A N 1 ATOM 1105 C CA . ILE A 1 141 ? 2.185 -4.679 19.726 1.00 11.51 ? 160 ILE A CA 1 ATOM 1106 C C . ILE A 1 141 ? 1.071 -3.699 19.413 1.00 11.42 ? 160 ILE A C 1 ATOM 1107 O O . ILE A 1 141 ? 0.219 -3.959 18.565 1.00 12.37 ? 160 ILE A O 1 ATOM 1108 C CB . ILE A 1 141 ? 3.553 -3.989 19.771 1.00 11.10 ? 160 ILE A CB 1 ATOM 1109 C CG1 . ILE A 1 141 ? 3.870 -3.289 18.435 1.00 11.55 ? 160 ILE A CG1 1 ATOM 1110 C CG2 . ILE A 1 141 ? 4.646 -5.016 20.152 1.00 10.93 ? 160 ILE A CG2 1 ATOM 1111 C CD1 . ILE A 1 141 ? 5.086 -2.391 18.471 1.00 11.83 ? 160 ILE A CD1 1 ATOM 1112 N N . ASN A 1 142 ? 1.064 -2.587 20.130 1.00 11.53 ? 161 ASN A N 1 ATOM 1113 C CA . ASN A 1 142 ? -0.003 -1.624 19.991 1.00 12.29 ? 161 ASN A CA 1 ATOM 1114 C C . ASN A 1 142 ? 0.558 -0.251 19.796 1.00 11.54 ? 161 ASN A C 1 ATOM 1115 O O . ASN A 1 142 ? 1.666 0.038 20.272 1.00 12.21 ? 161 ASN A O 1 ATOM 1116 C CB . ASN A 1 142 ? -0.831 -1.606 21.269 1.00 13.33 ? 161 ASN A CB 1 ATOM 1117 C CG . ASN A 1 142 ? -1.608 -2.881 21.462 1.00 16.55 ? 161 ASN A CG 1 ATOM 1118 O OD1 . ASN A 1 142 ? -2.674 -3.077 20.858 1.00 22.90 ? 161 ASN A OD1 1 ATOM 1119 N ND2 . ASN A 1 142 ? -1.105 -3.738 22.323 1.00 20.48 ? 161 ASN A ND2 1 ATOM 1120 N N . ILE A 1 143 ? -0.212 0.599 19.112 1.00 11.14 ? 162 ILE A N 1 ATOM 1121 C CA . ILE A 1 143 ? 0.060 2.023 19.154 1.00 10.90 ? 162 ILE A CA 1 ATOM 1122 C C . ILE A 1 143 ? -0.304 2.487 20.541 1.00 10.92 ? 162 ILE A C 1 ATOM 1123 O O . ILE A 1 143 ? -1.425 2.275 21.014 1.00 11.34 ? 162 ILE A O 1 ATOM 1124 C CB . ILE A 1 143 ? -0.768 2.829 18.144 1.00 10.87 ? 162 ILE A CB 1 ATOM 1125 C CG1 . ILE A 1 143 ? -0.461 2.368 16.721 1.00 10.99 ? 162 ILE A CG1 1 ATOM 1126 C CG2 . ILE A 1 143 ? -0.479 4.314 18.285 1.00 11.92 ? 162 ILE A CG2 1 ATOM 1127 C CD1 . ILE A 1 143 ? 1.013 2.597 16.283 1.00 11.26 ? 162 ILE A CD1 1 ATOM 1128 N N . LEU A 1 144 ? 0.673 3.080 21.201 1.00 11.10 ? 163 LEU A N 1 ATOM 1129 C CA . LEU A 1 144 ? 0.494 3.598 22.535 1.00 11.67 ? 163 LEU A CA 1 ATOM 1130 C C . LEU A 1 144 ? 0.265 5.092 22.487 1.00 12.44 ? 163 LEU A C 1 ATOM 1131 O O . LEU A 1 144 ? 0.664 5.782 21.541 1.00 12.82 ? 163 LEU A O 1 ATOM 1132 C CB . LEU A 1 144 ? 1.709 3.288 23.411 1.00 12.03 ? 163 LEU A CB 1 ATOM 1133 C CG . LEU A 1 144 ? 2.074 1.804 23.476 1.00 12.41 ? 163 LEU A CG 1 ATOM 1134 C CD1 . LEU A 1 144 ? 3.288 1.628 24.353 1.00 13.31 ? 163 LEU A CD1 1 ATOM 1135 C CD2 . LEU A 1 144 ? 0.909 0.955 23.995 1.00 15.07 ? 163 LEU A CD2 1 ATOM 1136 N N . ASP A 1 145 ? -0.382 5.591 23.532 1.00 13.00 ? 164 ASP A N 1 ATOM 1137 C CA . ASP A 1 145 ? -0.494 7.009 23.750 1.00 14.21 ? 164 ASP A CA 1 ATOM 1138 C C . ASP A 1 145 ? 0.916 7.568 23.661 1.00 14.19 ? 164 ASP A C 1 ATOM 1139 O O . ASP A 1 145 ? 1.846 7.081 24.309 1.00 13.83 ? 164 ASP A O 1 ATOM 1140 C CB . ASP A 1 145 ? -1.058 7.230 25.147 1.00 14.37 ? 164 ASP A CB 1 ATOM 1141 C CG . ASP A 1 145 ? -1.359 8.687 25.449 1.00 17.65 ? 164 ASP A CG 1 ATOM 1142 O OD1 . ASP A 1 145 ? -2.216 8.921 26.333 1.00 21.08 ? 164 ASP A OD1 1 ATOM 1143 O OD2 . ASP A 1 145 ? -0.774 9.596 24.826 1.00 17.26 ? 164 ASP A OD2 1 ATOM 1144 N N . TYR A 1 146 ? 1.082 8.582 22.832 1.00 14.84 ? 165 TYR A N 1 ATOM 1145 C CA . TYR A 1 146 ? 2.395 9.172 22.637 1.00 15.38 ? 165 TYR A CA 1 ATOM 1146 C C . TYR A 1 146 ? 3.022 9.629 23.952 1.00 15.66 ? 165 TYR A C 1 ATOM 1147 O O . TYR A 1 146 ? 4.252 9.631 24.091 1.00 14.92 ? 165 TYR A O 1 ATOM 1148 C CB . TYR A 1 146 ? 2.275 10.325 21.654 1.00 16.57 ? 165 TYR A CB 1 ATOM 1149 C CG . TYR A 1 146 ? 3.579 10.852 21.148 1.00 17.67 ? 165 TYR A CG 1 ATOM 1150 C CD1 . TYR A 1 146 ? 4.353 10.115 20.243 1.00 18.10 ? 165 TYR A CD1 1 ATOM 1151 C CD2 . TYR A 1 146 ? 4.016 12.114 21.532 1.00 19.57 ? 165 TYR A CD2 1 ATOM 1152 C CE1 . TYR A 1 146 ? 5.544 10.615 19.763 1.00 20.32 ? 165 TYR A CE1 1 ATOM 1153 C CE2 . TYR A 1 146 ? 5.203 12.632 21.047 1.00 21.14 ? 165 TYR A CE2 1 ATOM 1154 C CZ . TYR A 1 146 ? 5.960 11.873 20.162 1.00 21.07 ? 165 TYR A CZ 1 ATOM 1155 O OH . TYR A 1 146 ? 7.142 12.389 19.685 1.00 23.35 ? 165 TYR A OH 1 ATOM 1156 N N . ALA A 1 147 ? 2.175 10.005 24.916 1.00 15.59 ? 166 ALA A N 1 ATOM 1157 C CA . ALA A 1 147 ? 2.649 10.439 26.230 1.00 16.36 ? 166 ALA A CA 1 ATOM 1158 C C . ALA A 1 147 ? 3.458 9.372 26.945 1.00 16.58 ? 166 ALA A C 1 ATOM 1159 O O . ALA A 1 147 ? 4.295 9.672 27.778 1.00 17.54 ? 166 ALA A O 1 ATOM 1160 C CB . ALA A 1 147 ? 1.478 10.888 27.112 1.00 16.79 ? 166 ALA A CB 1 ATOM 1161 N N . VAL A 1 148 ? 3.224 8.113 26.610 1.00 16.42 ? 167 VAL A N 1 ATOM 1162 C CA . VAL A 1 148 ? 4.004 7.046 27.213 1.00 16.22 ? 167 VAL A CA 1 ATOM 1163 C C . VAL A 1 148 ? 5.457 7.172 26.773 1.00 16.55 ? 167 VAL A C 1 ATOM 1164 O O . VAL A 1 148 ? 6.369 7.064 27.589 1.00 16.80 ? 167 VAL A O 1 ATOM 1165 C CB . VAL A 1 148 ? 3.442 5.657 26.840 1.00 16.42 ? 167 VAL A CB 1 ATOM 1166 C CG1 . VAL A 1 148 ? 4.352 4.557 27.358 1.00 16.26 ? 167 VAL A CG1 1 ATOM 1167 C CG2 . VAL A 1 148 ? 2.029 5.484 27.405 1.00 16.26 ? 167 VAL A CG2 1 ATOM 1168 N N . CYS A 1 149 ? 5.670 7.410 25.482 1.00 16.37 ? 168 CYS A N 1 ATOM 1169 C CA . CYS A 1 149 ? 7.024 7.603 24.972 1.00 17.21 ? 168 CYS A CA 1 ATOM 1170 C C . CYS A 1 149 ? 7.638 8.908 25.452 1.00 18.22 ? 168 CYS A C 1 ATOM 1171 O O . CYS A 1 149 ? 8.841 8.968 25.698 1.00 19.57 ? 168 CYS A O 1 ATOM 1172 C CB . CYS A 1 149 ? 7.042 7.546 23.457 1.00 16.98 ? 168 CYS A CB 1 ATOM 1173 S SG . CYS A 1 149 ? 7.011 5.868 22.844 1.00 15.87 ? 168 CYS A SG 1 ATOM 1174 N N . GLN A 1 150 ? 6.819 9.948 25.579 1.00 18.86 ? 169 GLN A N 1 ATOM 1175 C CA . GLN A 1 150 ? 7.298 11.225 26.106 1.00 20.01 ? 169 GLN A CA 1 ATOM 1176 C C . GLN A 1 150 ? 7.786 11.072 27.527 1.00 20.48 ? 169 GLN A C 1 ATOM 1177 O O . GLN A 1 150 ? 8.786 11.687 27.898 1.00 21.51 ? 169 GLN A O 1 ATOM 1178 C CB . GLN A 1 150 ? 6.194 12.272 26.060 1.00 19.85 ? 169 GLN A CB 1 ATOM 1179 C CG . GLN A 1 150 ? 5.912 12.757 24.677 1.00 21.18 ? 169 GLN A CG 1 ATOM 1180 C CD . GLN A 1 150 ? 4.755 13.728 24.638 1.00 21.95 ? 169 GLN A CD 1 ATOM 1181 O OE1 . GLN A 1 150 ? 3.676 13.449 25.169 1.00 22.85 ? 169 GLN A OE1 1 ATOM 1182 N NE2 . GLN A 1 150 ? 4.970 14.878 24.004 1.00 23.97 ? 169 GLN A NE2 1 ATOM 1183 N N . ALA A 1 151 ? 7.080 10.265 28.319 1.00 20.96 ? 170 ALA A N 1 ATOM 1184 C CA . ALA A 1 151 ? 7.463 10.005 29.706 1.00 21.97 ? 170 ALA A CA 1 ATOM 1185 C C . ALA A 1 151 ? 8.763 9.208 29.771 1.00 22.38 ? 170 ALA A C 1 ATOM 1186 O O . ALA A 1 151 ? 9.627 9.475 30.621 1.00 23.42 ? 170 ALA A O 1 ATOM 1187 C CB . ALA A 1 151 ? 6.357 9.257 30.441 1.00 22.03 ? 170 ALA A CB 1 ATOM 1188 N N . ALA A 1 152 ? 8.893 8.233 28.872 1.00 22.04 ? 171 ALA A N 1 ATOM 1189 C CA . ALA A 1 152 ? 10.046 7.336 28.851 1.00 22.14 ? 171 ALA A CA 1 ATOM 1190 C C . ALA A 1 152 ? 11.298 7.977 28.258 1.00 22.24 ? 171 ALA A C 1 ATOM 1191 O O . ALA A 1 152 ? 12.418 7.645 28.656 1.00 22.92 ? 171 ALA A O 1 ATOM 1192 C CB . ALA A 1 152 ? 9.710 6.061 28.087 1.00 22.28 ? 171 ALA A CB 1 ATOM 1193 N N . TYR A 1 153 ? 11.117 8.861 27.281 1.00 22.18 ? 172 TYR A N 1 ATOM 1194 C CA . TYR A 1 153 ? 12.244 9.313 26.471 1.00 22.30 ? 172 TYR A CA 1 ATOM 1195 C C . TYR A 1 153 ? 12.288 10.812 26.298 1.00 23.61 ? 172 TYR A C 1 ATOM 1196 O O . TYR A 1 153 ? 11.707 11.366 25.352 1.00 24.69 ? 172 TYR A O 1 ATOM 1197 C CB . TYR A 1 153 ? 12.222 8.677 25.085 1.00 21.32 ? 172 TYR A CB 1 ATOM 1198 C CG . TYR A 1 153 ? 12.083 7.188 25.093 1.00 18.92 ? 172 TYR A CG 1 ATOM 1199 C CD1 . TYR A 1 153 ? 13.012 6.387 25.761 1.00 18.30 ? 172 TYR A CD1 1 ATOM 1200 C CD2 . TYR A 1 153 ? 11.028 6.575 24.422 1.00 16.60 ? 172 TYR A CD2 1 ATOM 1201 C CE1 . TYR A 1 153 ? 12.896 5.011 25.768 1.00 17.38 ? 172 TYR A CE1 1 ATOM 1202 C CE2 . TYR A 1 153 ? 10.902 5.203 24.416 1.00 15.74 ? 172 TYR A CE2 1 ATOM 1203 C CZ . TYR A 1 153 ? 11.838 4.424 25.093 1.00 17.27 ? 172 TYR A CZ 1 ATOM 1204 O OH . TYR A 1 153 ? 11.729 3.063 25.086 1.00 16.84 ? 172 TYR A OH 1 ATOM 1205 N N . LYS A 1 154 ? 13.015 11.461 27.190 1.00 24.35 ? 174 LYS A N 1 ATOM 1206 C CA . LYS A 1 154 ? 13.242 12.886 27.066 1.00 24.70 ? 174 LYS A CA 1 ATOM 1207 C C . LYS A 1 154 ? 14.049 13.092 25.788 1.00 24.47 ? 174 LYS A C 1 ATOM 1208 O O . LYS A 1 154 ? 15.093 12.475 25.602 1.00 25.05 ? 174 LYS A O 1 ATOM 1209 C CB . LYS A 1 154 ? 14.018 13.424 28.267 1.00 25.15 ? 174 LYS A CB 1 ATOM 1210 C CG . LYS A 1 154 ? 14.002 12.552 29.502 0.50 26.17 ? 174 LYS A CG 1 ATOM 1211 C CD . LYS A 1 154 ? 15.238 12.821 30.336 0.50 27.58 ? 174 LYS A CD 1 ATOM 1212 C CE . LYS A 1 154 ? 16.516 12.318 29.663 0.50 28.13 ? 174 LYS A CE 1 ATOM 1213 N NZ . LYS A 1 154 ? 16.855 10.930 30.078 0.50 28.71 ? 174 LYS A NZ 1 ATOM 1214 N N . GLY A 1 155 ? 13.547 13.942 24.898 1.00 24.26 ? 175 GLY A N 1 ATOM 1215 C CA . GLY A 1 155 ? 14.236 14.233 23.640 1.00 23.35 ? 175 GLY A CA 1 ATOM 1216 C C . GLY A 1 155 ? 13.735 13.421 22.458 1.00 22.47 ? 175 GLY A C 1 ATOM 1217 O O . GLY A 1 155 ? 14.409 13.314 21.441 1.00 22.92 ? 175 GLY A O 1 ATOM 1218 N N . LEU A 1 156 ? 12.557 12.834 22.620 1.00 21.61 ? 176 LEU A N 1 ATOM 1219 C CA . LEU A 1 156 ? 11.865 12.086 21.580 1.00 20.80 ? 176 LEU A CA 1 ATOM 1220 C C . LEU A 1 156 ? 11.649 12.992 20.378 1.00 19.32 ? 176 LEU A C 1 ATOM 1221 O O . LEU A 1 156 ? 11.274 14.152 20.529 1.00 18.70 ? 176 LEU A O 1 ATOM 1222 C CB . LEU A 1 156 ? 10.489 11.696 22.134 1.00 21.28 ? 176 LEU A CB 1 ATOM 1223 C CG . LEU A 1 156 ? 9.679 10.425 21.900 1.00 25.20 ? 176 LEU A CG 1 ATOM 1224 C CD1 . LEU A 1 156 ? 8.318 10.648 22.499 1.00 26.15 ? 176 LEU A CD1 1 ATOM 1225 C CD2 . LEU A 1 156 ? 9.543 10.078 20.451 1.00 26.94 ? 176 LEU A CD2 1 ATOM 1226 N N . ALA A 1 157 ? 11.874 12.464 19.180 1.00 17.88 ? 177 ALA A N 1 ATOM 1227 C CA . ALA A 1 157 ? 11.599 13.215 17.964 1.00 17.03 ? 177 ALA A CA 1 ATOM 1228 C C . ALA A 1 157 ? 10.102 13.292 17.710 1.00 16.33 ? 177 ALA A C 1 ATOM 1229 O O . ALA A 1 157 ? 9.341 12.399 18.094 1.00 15.99 ? 177 ALA A O 1 ATOM 1230 C CB . ALA A 1 157 ? 12.300 12.569 16.781 1.00 17.31 ? 177 ALA A CB 1 ATOM 1231 N N . ALA A 1 158 ? 9.688 14.379 17.068 1.00 15.52 ? 178 ALA A N 1 ATOM 1232 C CA . ALA A 1 158 ? 8.330 14.504 16.579 1.00 15.34 ? 178 ALA A CA 1 ATOM 1233 C C . ALA A 1 158 ? 8.217 13.618 15.327 1.00 14.47 ? 178 ALA A C 1 ATOM 1234 O O . ALA A 1 158 ? 9.153 12.879 14.990 1.00 14.33 ? 178 ALA A O 1 ATOM 1235 C CB . ALA A 1 158 ? 8.015 15.951 16.271 1.00 15.99 ? 178 ALA A CB 1 ATOM 1236 N N . THR A 1 159 ? 7.074 13.682 14.665 1.00 13.21 ? 179 THR A N 1 ATOM 1237 C CA . THR A 1 159 ? 6.743 12.805 13.538 1.00 12.03 ? 179 THR A CA 1 ATOM 1238 C C . THR A 1 159 ? 7.096 11.360 13.818 1.00 11.46 ? 179 THR A C 1 ATOM 1239 O O . THR A 1 159 ? 7.708 10.678 12.990 1.00 10.61 ? 179 THR A O 1 ATOM 1240 C CB . THR A 1 159 ? 7.338 13.284 12.173 1.00 12.16 ? 179 THR A CB 1 ATOM 1241 O OG1 . THR A 1 159 ? 8.773 13.196 12.183 1.00 12.61 ? 179 THR A OG1 1 ATOM 1242 C CG2 . THR A 1 159 ? 6.894 14.717 11.885 1.00 12.98 ? 179 THR A CG2 1 ATOM 1243 N N . THR A 1 160 ? 6.689 10.918 15.003 1.00 11.22 ? 180 THR A N 1 ATOM 1244 C CA . THR A 1 160 ? 6.899 9.544 15.408 1.00 11.37 ? 180 THR A CA 1 ATOM 1245 C C . THR A 1 160 ? 5.642 8.974 16.031 1.00 11.54 ? 180 THR A C 1 ATOM 1246 O O . THR A 1 160 ? 4.772 9.713 16.508 1.00 12.04 ? 180 THR A O 1 ATOM 1247 C CB . THR A 1 160 ? 8.064 9.394 16.408 1.00 11.71 ? 180 THR A CB 1 ATOM 1248 O OG1 . THR A 1 160 ? 7.838 10.238 17.550 1.00 13.61 ? 180 THR A OG1 1 ATOM 1249 C CG2 . THR A 1 160 ? 9.402 9.746 15.773 1.00 12.56 ? 180 THR A CG2 1 ATOM 1250 N N . LEU A 1 161 ? 5.573 7.651 16.000 1.00 11.19 ? 181 LEU A N 1 ATOM 1251 C CA . LEU A 1 161 ? 4.577 6.883 16.718 1.00 10.84 ? 181 LEU A CA 1 ATOM 1252 C C . LEU A 1 161 ? 5.244 6.169 17.874 1.00 10.70 ? 181 LEU A C 1 ATOM 1253 O O . LEU A 1 161 ? 6.405 5.744 17.790 1.00 10.23 ? 181 LEU A O 1 ATOM 1254 C CB . LEU A 1 161 ? 3.968 5.833 15.801 1.00 11.21 ? 181 LEU A CB 1 ATOM 1255 C CG . LEU A 1 161 ? 3.102 6.401 14.689 1.00 12.67 ? 181 LEU A CG 1 ATOM 1256 C CD1 . LEU A 1 161 ? 2.889 5.308 13.658 1.00 12.95 ? 181 LEU A CD1 1 ATOM 1257 C CD2 . LEU A 1 161 ? 1.786 6.929 15.228 1.00 14.34 ? 181 LEU A CD2 1 ATOM 1258 N N . CYS A 1 162 ? 4.493 6.038 18.960 1.00 11.21 ? 182 CYS A N 1 ATOM 1259 C CA . CYS A 1 162 ? 4.918 5.300 20.125 1.00 11.14 ? 182 CYS A CA 1 ATOM 1260 C C . CYS A 1 162 ? 4.221 3.951 20.068 1.00 11.50 ? 182 CYS A C 1 ATOM 1261 O O . CYS A 1 162 ? 3.018 3.901 19.951 1.00 11.45 ? 182 CYS A O 1 ATOM 1262 C CB . CYS A 1 162 ? 4.451 6.062 21.351 1.00 11.89 ? 182 CYS A CB 1 ATOM 1263 S SG . CYS A 1 162 ? 5.018 5.382 22.899 1.00 13.04 ? 182 CYS A SG 1 ATOM 1264 N N . ALA A 1 163 ? 4.977 2.859 20.078 1.00 9.89 ? 183 ALA A N 1 ATOM 1265 C CA . ALA A 1 163 ? 4.327 1.566 19.921 1.00 10.42 ? 183 ALA A CA 1 ATOM 1266 C C . ALA A 1 163 ? 5.063 0.513 20.690 1.00 10.45 ? 183 ALA A C 1 ATOM 1267 O O . ALA A 1 163 ? 6.278 0.510 20.734 1.00 10.25 ? 183 ALA A O 1 ATOM 1268 C CB . ALA A 1 163 ? 4.231 1.184 18.448 1.00 10.49 ? 183 ALA A CB 1 ATOM 1269 N N . GLY A 1 164 ? 4.299 -0.365 21.305 1.00 10.25 ? 184 GLY A N 1 ATOM 1270 C CA . GLY A 1 164 ? 4.864 -1.431 22.109 1.00 10.65 ? 184 GLY A CA 1 ATOM 1271 C C . GLY A 1 164 ? 3.743 -2.021 22.912 1.00 11.89 ? 184 GLY A C 1 ATOM 1272 O O . GLY A 1 164 ? 2.571 -1.928 22.529 1.00 11.64 ? 184 GLY A O 1 ATOM 1273 N N . ILE A 1 165 ? 4.122 -2.608 24.039 1.00 12.52 ? 185 ILE A N 1 ATOM 1274 C CA . ILE A 1 165 ? 3.164 -3.141 24.983 1.00 14.06 ? 185 ILE A CA 1 ATOM 1275 C C . ILE A 1 165 ? 3.426 -2.339 26.226 1.00 14.87 ? 185 ILE A C 1 ATOM 1276 O O . ILE A 1 165 ? 4.564 -2.241 26.653 1.00 14.45 ? 185 ILE A O 1 ATOM 1277 C CB . ILE A 1 165 ? 3.424 -4.634 25.292 1.00 14.69 ? 185 ILE A CB 1 ATOM 1278 C CG1 . ILE A 1 165 ? 3.403 -5.496 24.021 1.00 17.10 ? 185 ILE A CG1 1 ATOM 1279 C CG2 . ILE A 1 165 ? 2.401 -5.146 26.319 1.00 15.39 ? 185 ILE A CG2 1 ATOM 1280 C CD1 . ILE A 1 165 ? 2.070 -5.557 23.327 1.00 17.99 ? 185 ILE A CD1 1 ATOM 1281 N N . LEU A 1 166 ? 2.386 -1.744 26.792 1.00 15.97 ? 186 LEU A N 1 ATOM 1282 C CA . LEU A 1 166 ? 2.577 -0.861 27.927 1.00 17.58 ? 186 LEU A CA 1 ATOM 1283 C C . LEU A 1 166 ? 3.337 -1.596 29.038 1.00 18.06 ? 186 LEU A C 1 ATOM 1284 O O . LEU A 1 166 ? 4.237 -1.032 29.667 1.00 19.68 ? 186 LEU A O 1 ATOM 1285 C CB . LEU A 1 166 ? 1.217 -0.346 28.408 1.00 17.62 ? 186 LEU A CB 1 ATOM 1286 C CG . LEU A 1 166 ? 1.165 0.862 29.334 1.00 18.83 ? 186 LEU A CG 1 ATOM 1287 C CD1 . LEU A 1 166 ? 1.777 2.115 28.697 1.00 19.10 ? 186 LEU A CD1 1 ATOM 1288 C CD2 . LEU A 1 166 ? -0.276 1.126 29.728 1.00 18.72 ? 186 LEU A CD2 1 ATOM 1289 N N . GLU A 1 167 A 2.991 -2.867 29.241 1.00 18.93 ? 186 GLU A N 1 ATOM 1290 C CA . GLU A 1 167 A 3.606 -3.702 30.278 1.00 19.26 ? 186 GLU A CA 1 ATOM 1291 C C . GLU A 1 167 A 4.963 -4.289 29.877 1.00 18.72 ? 186 GLU A C 1 ATOM 1292 O O . GLU A 1 167 A 5.600 -5.001 30.664 1.00 19.44 ? 186 GLU A O 1 ATOM 1293 C CB . GLU A 1 167 A 2.641 -4.812 30.725 1.00 19.94 ? 186 GLU A CB 1 ATOM 1294 C CG . GLU A 1 167 A 2.073 -5.700 29.612 0.50 20.49 ? 186 GLU A CG 1 ATOM 1295 C CD . GLU A 1 167 A 0.683 -5.277 29.102 0.50 20.96 ? 186 GLU A CD 1 ATOM 1296 O OE1 . GLU A 1 167 A 0.380 -4.058 28.987 0.50 16.90 ? 186 GLU A OE1 1 ATOM 1297 O OE2 . GLU A 1 167 A -0.107 -6.198 28.787 0.50 21.81 ? 186 GLU A OE2 1 ATOM 1298 N N . GLY A 1 168 B 5.398 -3.992 28.652 1.00 17.35 ? 186 GLY A N 1 ATOM 1299 C CA . GLY A 1 168 B 6.626 -4.575 28.114 1.00 17.06 ? 186 GLY A CA 1 ATOM 1300 C C . GLY A 1 168 B 6.455 -6.019 27.675 1.00 16.65 ? 186 GLY A C 1 ATOM 1301 O O . GLY A 1 168 B 5.333 -6.530 27.584 1.00 17.46 ? 186 GLY A O 1 ATOM 1302 N N . GLY A 1 169 ? 7.581 -6.666 27.392 1.00 16.15 ? 187 GLY A N 1 ATOM 1303 C CA . GLY A 1 169 ? 7.602 -8.097 27.095 1.00 15.84 ? 187 GLY A CA 1 ATOM 1304 C C . GLY A 1 169 ? 7.745 -8.387 25.609 1.00 15.66 ? 187 GLY A C 1 ATOM 1305 O O . GLY A 1 169 ? 8.326 -9.400 25.224 1.00 16.61 ? 187 GLY A O 1 ATOM 1306 N N . LYS A 1 170 ? 7.178 -7.519 24.775 1.00 14.91 ? 188 LYS A N 1 ATOM 1307 C CA . LYS A 1 170 ? 7.325 -7.644 23.328 1.00 14.19 ? 188 LYS A CA 1 ATOM 1308 C C . LYS A 1 170 ? 7.750 -6.292 22.829 1.00 13.14 ? 188 LYS A C 1 ATOM 1309 O O . LYS A 1 170 ? 7.235 -5.277 23.270 1.00 13.58 ? 188 LYS A O 1 ATOM 1310 C CB . LYS A 1 170 ? 6.017 -8.036 22.652 1.00 14.73 ? 188 LYS A CB 1 ATOM 1311 C CG . LYS A 1 170 ? 5.495 -9.386 23.111 1.00 16.20 ? 188 LYS A CG 1 ATOM 1312 C CD . LYS A 1 170 ? 4.175 -9.712 22.448 1.00 19.34 ? 188 LYS A CD 1 ATOM 1313 C CE . LYS A 1 170 ? 3.613 -11.015 22.988 1.00 22.78 ? 188 LYS A CE 1 ATOM 1314 N NZ . LYS A 1 170 ? 2.313 -11.362 22.353 1.00 27.61 ? 188 LYS A NZ 1 ATOM 1315 N N . ASP A 1 171 ? 8.690 -6.285 21.897 1.00 12.32 ? 189 ASP A N 1 ATOM 1316 C CA . ASP A 1 171 ? 9.280 -5.029 21.473 1.00 11.76 ? 189 ASP A CA 1 ATOM 1317 C C . ASP A 1 171 ? 10.185 -5.348 20.316 1.00 11.52 ? 189 ASP A C 1 ATOM 1318 O O . ASP A 1 171 ? 10.618 -6.487 20.135 1.00 11.94 ? 189 ASP A O 1 ATOM 1319 C CB . ASP A 1 171 ? 10.093 -4.426 22.642 1.00 11.83 ? 189 ASP A CB 1 ATOM 1320 C CG . ASP A 1 171 ? 10.464 -2.956 22.452 1.00 12.51 ? 189 ASP A CG 1 ATOM 1321 O OD1 . ASP A 1 171 ? 10.017 -2.325 21.475 1.00 11.84 ? 189 ASP A OD1 1 ATOM 1322 O OD2 . ASP A 1 171 ? 11.238 -2.439 23.298 1.00 12.62 ? 189 ASP A OD2 1 ATOM 1323 N N . THR A 1 172 ? 10.487 -4.333 19.526 1.00 10.76 ? 190 THR A N 1 ATOM 1324 C CA . THR A 1 172 ? 11.628 -4.436 18.633 1.00 10.75 ? 190 THR A CA 1 ATOM 1325 C C . THR A 1 172 ? 12.904 -4.234 19.436 1.00 11.82 ? 190 THR A C 1 ATOM 1326 O O . THR A 1 172 ? 12.872 -3.900 20.629 1.00 11.73 ? 190 THR A O 1 ATOM 1327 C CB . THR A 1 172 ? 11.560 -3.394 17.528 1.00 10.60 ? 190 THR A CB 1 ATOM 1328 O OG1 . THR A 1 172 ? 11.195 -2.135 18.099 1.00 10.20 ? 190 THR A OG1 1 ATOM 1329 C CG2 . THR A 1 172 ? 10.528 -3.784 16.493 1.00 10.17 ? 190 THR A CG2 1 ATOM 1330 N N . CYS A 1 173 ? 14.037 -4.428 18.777 1.00 11.77 ? 191 CYS A N 1 ATOM 1331 C CA . CYS A 1 173 ? 15.297 -4.240 19.448 1.00 12.25 ? 191 CYS A CA 1 ATOM 1332 C C . CYS A 1 173 ? 16.398 -3.987 18.439 1.00 12.62 ? 191 CYS A C 1 ATOM 1333 O O . CYS A 1 173 ? 16.129 -3.808 17.249 1.00 11.70 ? 191 CYS A O 1 ATOM 1334 C CB . CYS A 1 173 ? 15.585 -5.462 20.311 1.00 13.38 ? 191 CYS A CB 1 ATOM 1335 S SG . CYS A 1 173 ? 16.696 -5.140 21.703 1.00 14.27 ? 191 CYS A SG 1 ATOM 1336 N N . LYS A 1 174 ? 17.635 -3.943 18.924 1.00 12.65 ? 192 LYS A N 1 ATOM 1337 C CA . LYS A 1 174 ? 18.783 -3.675 18.069 1.00 13.17 ? 192 LYS A CA 1 ATOM 1338 C C . LYS A 1 174 ? 18.793 -4.617 16.874 1.00 12.89 ? 192 LYS A C 1 ATOM 1339 O O . LYS A 1 174 ? 18.672 -5.825 17.022 1.00 13.13 ? 192 LYS A O 1 ATOM 1340 C CB . LYS A 1 174 ? 20.071 -3.829 18.880 1.00 13.44 ? 192 LYS A CB 1 ATOM 1341 C CG . LYS A 1 174 ? 20.261 -2.703 19.881 1.00 17.30 ? 192 LYS A CG 1 ATOM 1342 C CD . LYS A 1 174 ? 21.408 -1.804 19.423 0.50 18.68 ? 192 LYS A CD 1 ATOM 1343 C CE . LYS A 1 174 ? 21.188 -0.364 19.799 0.50 21.01 ? 192 LYS A CE 1 ATOM 1344 N NZ . LYS A 1 174 ? 22.033 0.509 18.948 0.50 21.81 ? 192 LYS A NZ 1 ATOM 1345 N N . GLY A 1 175 ? 18.935 -4.032 15.689 1.00 12.30 ? 193 GLY A N 1 ATOM 1346 C CA . GLY A 1 175 ? 18.954 -4.793 14.458 1.00 12.05 ? 193 GLY A CA 1 ATOM 1347 C C . GLY A 1 175 ? 17.621 -4.730 13.737 1.00 12.01 ? 193 GLY A C 1 ATOM 1348 O O . GLY A 1 175 ? 17.550 -5.086 12.573 1.00 12.40 ? 193 GLY A O 1 ATOM 1349 N N . ASP A 1 176 ? 16.565 -4.313 14.446 1.00 10.97 ? 194 ASP A N 1 ATOM 1350 C CA . ASP A 1 176 ? 15.242 -4.204 13.854 1.00 10.79 ? 194 ASP A CA 1 ATOM 1351 C C . ASP A 1 176 ? 15.009 -2.817 13.293 1.00 10.38 ? 194 ASP A C 1 ATOM 1352 O O . ASP A 1 176 ? 14.006 -2.607 12.586 1.00 9.33 ? 194 ASP A O 1 ATOM 1353 C CB . ASP A 1 176 ? 14.134 -4.465 14.881 1.00 10.31 ? 194 ASP A CB 1 ATOM 1354 C CG . ASP A 1 176 ? 14.096 -5.878 15.367 1.00 10.70 ? 194 ASP A CG 1 ATOM 1355 O OD1 . ASP A 1 176 ? 14.339 -6.786 14.555 1.00 11.11 ? 194 ASP A OD1 1 ATOM 1356 O OD2 . ASP A 1 176 ? 13.775 -6.061 16.561 1.00 10.98 ? 194 ASP A OD2 1 ATOM 1357 N N . SER A 1 177 ? 15.883 -1.867 13.627 1.00 10.96 ? 195 SER A N 1 ATOM 1358 C CA . SER A 1 177 ? 15.693 -0.493 13.179 1.00 10.94 ? 195 SER A CA 1 ATOM 1359 C C . SER A 1 177 ? 15.552 -0.450 11.680 1.00 10.02 ? 195 SER A C 1 ATOM 1360 O O . SER A 1 177 ? 16.132 -1.270 10.954 1.00 10.15 ? 195 SER A O 1 ATOM 1361 C CB . SER A 1 177 ? 16.828 0.429 13.617 1.00 12.34 ? 195 SER A CB 1 ATOM 1362 O OG . SER A 1 177 ? 16.791 0.650 15.011 1.00 13.71 ? 195 SER A OG 1 ATOM 1363 N N . GLY A 1 178 ? 14.754 0.515 11.231 1.00 9.67 ? 196 GLY A N 1 ATOM 1364 C CA . GLY A 1 178 ? 14.491 0.676 9.820 1.00 9.98 ? 196 GLY A CA 1 ATOM 1365 C C . GLY A 1 178 ? 13.331 -0.160 9.342 1.00 9.90 ? 196 GLY A C 1 ATOM 1366 O O . GLY A 1 178 ? 12.794 0.103 8.282 1.00 10.05 ? 196 GLY A O 1 ATOM 1367 N N . GLY A 1 179 ? 13.001 -1.202 10.096 1.00 9.59 ? 197 GLY A N 1 ATOM 1368 C CA . GLY A 1 179 ? 11.923 -2.108 9.739 1.00 9.28 ? 197 GLY A CA 1 ATOM 1369 C C . GLY A 1 179 ? 10.561 -1.491 9.968 1.00 9.85 ? 197 GLY A C 1 ATOM 1370 O O . GLY A 1 179 ? 10.430 -0.471 10.644 1.00 9.81 ? 197 GLY A O 1 ATOM 1371 N N . PRO A 1 180 ? 9.532 -2.102 9.368 1.00 9.27 ? 198 PRO A N 1 ATOM 1372 C CA . PRO A 1 180 ? 8.183 -1.564 9.409 1.00 9.62 ? 198 PRO A CA 1 ATOM 1373 C C . PRO A 1 180 ? 7.400 -1.918 10.660 1.00 9.91 ? 198 PRO A C 1 ATOM 1374 O O . PRO A 1 180 ? 7.526 -3.012 11.216 1.00 9.95 ? 198 PRO A O 1 ATOM 1375 C CB . PRO A 1 180 ? 7.521 -2.209 8.200 1.00 9.79 ? 198 PRO A CB 1 ATOM 1376 C CG . PRO A 1 180 ? 8.227 -3.553 8.067 1.00 9.60 ? 198 PRO A CG 1 ATOM 1377 C CD . PRO A 1 180 ? 9.639 -3.321 8.539 1.00 10.07 ? 198 PRO A CD 1 ATOM 1378 N N . LEU A 1 181 ? 6.585 -0.958 11.064 1.00 9.16 ? 199 LEU A N 1 ATOM 1379 C CA . LEU A 1 181 ? 5.492 -1.152 11.988 1.00 9.39 ? 199 LEU A CA 1 ATOM 1380 C C . LEU A 1 181 ? 4.218 -1.161 11.122 1.00 9.42 ? 199 LEU A C 1 ATOM 1381 O O . LEU A 1 181 ? 3.901 -0.171 10.449 1.00 9.95 ? 199 LEU A O 1 ATOM 1382 C CB . LEU A 1 181 ? 5.482 0.029 12.949 1.00 9.74 ? 199 LEU A CB 1 ATOM 1383 C CG . LEU A 1 181 ? 4.327 0.087 13.926 1.00 9.58 ? 199 LEU A CG 1 ATOM 1384 C CD1 . LEU A 1 181 ? 4.580 -0.922 15.036 1.00 10.18 ? 199 LEU A CD1 1 ATOM 1385 C CD2 . LEU A 1 181 ? 4.163 1.483 14.493 1.00 9.49 ? 199 LEU A CD2 1 ATOM 1386 N N . ILE A 1 182 ? 3.518 -2.298 11.096 1.00 9.87 ? 200 ILE A N 1 ATOM 1387 C CA . ILE A 1 182 ? 2.350 -2.436 10.229 1.00 11.19 ? 200 ILE A CA 1 ATOM 1388 C C . ILE A 1 182 ? 1.117 -2.493 11.110 1.00 12.21 ? 200 ILE A C 1 ATOM 1389 O O . ILE A 1 182 ? 1.006 -3.386 11.906 1.00 12.74 ? 200 ILE A O 1 ATOM 1390 C CB . ILE A 1 182 ? 2.421 -3.734 9.400 1.00 11.72 ? 200 ILE A CB 1 ATOM 1391 C CG1 . ILE A 1 182 ? 3.787 -3.886 8.692 1.00 13.47 ? 200 ILE A CG1 1 ATOM 1392 C CG2 . ILE A 1 182 ? 1.229 -3.801 8.424 1.00 12.21 ? 200 ILE A CG2 1 ATOM 1393 C CD1 . ILE A 1 182 ? 4.152 -2.776 7.758 0.50 12.56 ? 200 ILE A CD1 1 ATOM 1394 N N . CYS A 1 183 ? 0.201 -1.548 10.959 1.00 12.67 ? 201 CYS A N 1 ATOM 1395 C CA . CYS A 1 183 ? -0.980 -1.511 11.823 1.00 13.96 ? 201 CYS A CA 1 ATOM 1396 C C . CYS A 1 183 ? -2.190 -1.511 10.950 1.00 15.26 ? 201 CYS A C 1 ATOM 1397 O O . CYS A 1 183 ? -2.253 -0.756 9.986 1.00 15.25 ? 201 CYS A O 1 ATOM 1398 C CB . CYS A 1 183 ? -1.010 -0.263 12.692 1.00 14.45 ? 201 CYS A CB 1 ATOM 1399 S SG . CYS A 1 183 ? 0.555 0.131 13.460 1.00 14.10 ? 201 CYS A SG 1 ATOM 1400 N N . ASN A 1 184 ? -3.137 -2.382 11.274 1.00 16.44 ? 202 ASN A N 1 ATOM 1401 C CA . ASN A 1 184 ? -4.359 -2.474 10.486 1.00 16.82 ? 202 ASN A CA 1 ATOM 1402 C C . ASN A 1 184 ? -4.028 -2.633 8.994 1.00 16.36 ? 202 ASN A C 1 ATOM 1403 O O . ASN A 1 184 ? -4.685 -2.056 8.137 1.00 16.69 ? 202 ASN A O 1 ATOM 1404 C CB . ASN A 1 184 ? -5.239 -1.238 10.737 1.00 18.08 ? 202 ASN A CB 1 ATOM 1405 C CG . ASN A 1 184 ? -5.428 -0.940 12.205 1.00 20.52 ? 202 ASN A CG 1 ATOM 1406 O OD1 . ASN A 1 184 ? -5.788 -1.817 12.985 1.00 23.95 ? 202 ASN A OD1 1 ATOM 1407 N ND2 . ASN A 1 184 ? -5.186 0.312 12.594 1.00 24.37 ? 202 ASN A ND2 1 ATOM 1408 N N . GLY A 1 185 ? -2.987 -3.415 8.703 1.00 14.88 ? 207 GLY A N 1 ATOM 1409 C CA . GLY A 1 185 ? -2.563 -3.716 7.347 1.00 14.63 ? 207 GLY A CA 1 ATOM 1410 C C . GLY A 1 185 ? -1.833 -2.605 6.607 1.00 13.68 ? 207 GLY A C 1 ATOM 1411 O O . GLY A 1 185 ? -1.524 -2.750 5.419 1.00 14.14 ? 207 GLY A O 1 ATOM 1412 N N . GLN A 1 186 ? -1.543 -1.518 7.325 1.00 13.45 ? 208 GLN A N 1 ATOM 1413 C CA . GLN A 1 186 ? -0.916 -0.326 6.740 1.00 13.17 ? 208 GLN A CA 1 ATOM 1414 C C . GLN A 1 186 ? 0.496 -0.136 7.260 1.00 12.57 ? 208 GLN A C 1 ATOM 1415 O O . GLN A 1 186 ? 0.767 -0.391 8.430 1.00 12.97 ? 208 GLN A O 1 ATOM 1416 C CB . GLN A 1 186 ? -1.714 0.928 7.085 1.00 13.05 ? 208 GLN A CB 1 ATOM 1417 C CG . GLN A 1 186 ? -3.168 0.898 6.607 1.00 13.71 ? 208 GLN A CG 1 ATOM 1418 C CD . GLN A 1 186 ? -3.777 2.286 6.538 1.00 15.58 ? 208 GLN A CD 1 ATOM 1419 O OE1 . GLN A 1 186 ? -4.586 2.665 7.372 1.00 21.90 ? 208 GLN A OE1 1 ATOM 1420 N NE2 . GLN A 1 186 ? -3.380 3.046 5.545 1.00 19.50 ? 208 GLN A NE2 1 ATOM 1421 N N . PHE A 1 187 ? 1.375 0.336 6.381 1.00 11.20 ? 209 PHE A N 1 ATOM 1422 C CA . PHE A 1 187 ? 2.748 0.689 6.730 1.00 10.72 ? 209 PHE A CA 1 ATOM 1423 C C . PHE A 1 187 ? 2.729 2.000 7.499 1.00 10.76 ? 209 PHE A C 1 ATOM 1424 O O . PHE A 1 187 ? 2.561 3.048 6.904 1.00 11.41 ? 209 PHE A O 1 ATOM 1425 C CB . PHE A 1 187 ? 3.517 0.859 5.418 1.00 10.40 ? 209 PHE A CB 1 ATOM 1426 C CG . PHE A 1 187 ? 4.964 1.220 5.569 1.00 10.31 ? 209 PHE A CG 1 ATOM 1427 C CD1 . PHE A 1 187 ? 5.665 0.970 6.737 1.00 10.16 ? 209 PHE A CD1 1 ATOM 1428 C CD2 . PHE A 1 187 ? 5.621 1.797 4.497 1.00 10.27 ? 209 PHE A CD2 1 ATOM 1429 C CE1 . PHE A 1 187 ? 7.009 1.311 6.841 1.00 10.30 ? 209 PHE A CE1 1 ATOM 1430 C CE2 . PHE A 1 187 ? 6.944 2.143 4.583 1.00 12.20 ? 209 PHE A CE2 1 ATOM 1431 C CZ . PHE A 1 187 ? 7.655 1.889 5.748 1.00 10.91 ? 209 PHE A CZ 1 ATOM 1432 N N . GLN A 1 188 ? 2.882 1.948 8.823 1.00 9.85 ? 210 GLN A N 1 ATOM 1433 C CA . GLN A 1 188 ? 2.716 3.155 9.629 1.00 10.18 ? 210 GLN A CA 1 ATOM 1434 C C . GLN A 1 188 ? 3.980 3.684 10.258 1.00 10.01 ? 210 GLN A C 1 ATOM 1435 O O . GLN A 1 188 ? 4.061 4.867 10.561 1.00 9.09 ? 210 GLN A O 1 ATOM 1436 C CB . GLN A 1 188 ? 1.692 2.940 10.743 1.00 10.71 ? 210 GLN A CB 1 ATOM 1437 C CG . GLN A 1 188 ? 0.303 2.552 10.223 1.00 10.88 ? 210 GLN A CG 1 ATOM 1438 C CD . GLN A 1 188 ? -0.503 3.707 9.664 1.00 12.82 ? 210 GLN A CD 1 ATOM 1439 O OE1 . GLN A 1 188 ? -1.721 3.578 9.459 1.00 16.51 ? 210 GLN A OE1 1 ATOM 1440 N NE2 . GLN A 1 188 ? 0.142 4.833 9.434 1.00 9.23 ? 210 GLN A NE2 1 ATOM 1441 N N . GLY A 1 189 ? 4.946 2.806 10.504 1.00 8.80 ? 211 GLY A N 1 ATOM 1442 C CA . GLY A 1 189 ? 6.151 3.237 11.191 1.00 8.97 ? 211 GLY A CA 1 ATOM 1443 C C . GLY A 1 189 ? 7.410 2.626 10.631 1.00 8.67 ? 211 GLY A C 1 ATOM 1444 O O . GLY A 1 189 ? 7.397 1.545 10.066 1.00 8.59 ? 211 GLY A O 1 ATOM 1445 N N . ILE A 1 190 ? 8.502 3.356 10.821 1.00 8.17 ? 212 ILE A N 1 ATOM 1446 C CA . ILE A 1 190 ? 9.835 2.858 10.552 1.00 8.23 ? 212 ILE A CA 1 ATOM 1447 C C . ILE A 1 190 ? 10.544 2.880 11.889 1.00 8.74 ? 212 ILE A C 1 ATOM 1448 O O . ILE A 1 190 ? 10.671 3.944 12.491 1.00 9.45 ? 212 ILE A O 1 ATOM 1449 C CB . ILE A 1 190 ? 10.551 3.808 9.600 1.00 8.43 ? 212 ILE A CB 1 ATOM 1450 C CG1 . ILE A 1 190 ? 9.819 3.840 8.261 1.00 8.67 ? 212 ILE A CG1 1 ATOM 1451 C CG2 . ILE A 1 190 ? 12.009 3.402 9.429 1.00 10.06 ? 212 ILE A CG2 1 ATOM 1452 C CD1 . ILE A 1 190 ? 10.319 4.940 7.346 1.00 10.77 ? 212 ILE A CD1 1 ATOM 1453 N N . LEU A 1 191 ? 11.008 1.736 12.378 1.00 8.19 ? 213 LEU A N 1 ATOM 1454 C CA . LEU A 1 191 ? 11.609 1.742 13.709 1.00 8.49 ? 213 LEU A CA 1 ATOM 1455 C C . LEU A 1 191 ? 12.828 2.642 13.740 1.00 8.73 ? 213 LEU A C 1 ATOM 1456 O O . LEU A 1 191 ? 13.731 2.525 12.921 1.00 9.43 ? 213 LEU A O 1 ATOM 1457 C CB . LEU A 1 191 ? 12.021 0.339 14.138 1.00 8.68 ? 213 LEU A CB 1 ATOM 1458 C CG . LEU A 1 191 ? 12.726 0.290 15.505 1.00 8.87 ? 213 LEU A CG 1 ATOM 1459 C CD1 . LEU A 1 191 ? 11.827 0.825 16.620 1.00 10.52 ? 213 LEU A CD1 1 ATOM 1460 C CD2 . LEU A 1 191 ? 13.130 -1.131 15.755 1.00 11.29 ? 213 LEU A CD2 1 ATOM 1461 N N . SER A 1 192 ? 12.850 3.525 14.734 1.00 9.50 ? 214 SER A N 1 ATOM 1462 C CA . SER A 1 192 ? 13.988 4.402 14.916 1.00 10.08 ? 214 SER A CA 1 ATOM 1463 C C . SER A 1 192 ? 14.782 4.047 16.164 1.00 10.75 ? 214 SER A C 1 ATOM 1464 O O . SER A 1 192 ? 15.942 3.647 16.095 1.00 11.33 ? 214 SER A O 1 ATOM 1465 C CB . SER A 1 192 ? 13.491 5.838 15.010 1.00 10.64 ? 214 SER A CB 1 ATOM 1466 O OG . SER A 1 192 ? 14.571 6.703 15.279 1.00 10.93 ? 214 SER A OG 1 ATOM 1467 N N . VAL A 1 193 ? 14.153 4.216 17.313 1.00 11.31 ? 215 VAL A N 1 ATOM 1468 C CA . VAL A 1 193 ? 14.865 4.105 18.573 1.00 11.92 ? 215 VAL A CA 1 ATOM 1469 C C . VAL A 1 193 ? 13.957 3.522 19.632 1.00 12.11 ? 215 VAL A C 1 ATOM 1470 O O . VAL A 1 193 ? 12.759 3.375 19.437 1.00 12.28 ? 215 VAL A O 1 ATOM 1471 C CB . VAL A 1 193 ? 15.423 5.487 19.072 1.00 12.74 ? 215 VAL A CB 1 ATOM 1472 C CG1 . VAL A 1 193 ? 16.498 6.041 18.135 1.00 15.06 ? 215 VAL A CG1 1 ATOM 1473 C CG2 . VAL A 1 193 ? 14.304 6.495 19.252 1.00 13.02 ? 215 VAL A CG2 1 ATOM 1474 N N . GLY A 1 194 ? 14.546 3.197 20.761 1.00 12.58 ? 216 GLY A N 1 ATOM 1475 C CA . GLY A 1 194 ? 13.770 2.715 21.877 1.00 12.47 ? 216 GLY A CA 1 ATOM 1476 C C . GLY A 1 194 ? 14.705 2.411 23.022 1.00 13.42 ? 216 GLY A C 1 ATOM 1477 O O . GLY A 1 194 ? 15.911 2.570 22.906 1.00 13.92 ? 216 GLY A O 1 ATOM 1478 N N . GLY A 1 195 ? 14.131 1.950 24.122 1.00 14.46 ? 217 GLY A N 1 ATOM 1479 C CA . GLY A 1 195 ? 14.929 1.706 25.314 1.00 16.02 ? 217 GLY A CA 1 ATOM 1480 C C . GLY A 1 195 ? 15.797 0.484 25.138 1.00 17.21 ? 217 GLY A C 1 ATOM 1481 O O . GLY A 1 195 ? 15.444 -0.457 24.431 1.00 17.96 ? 217 GLY A O 1 ATOM 1482 N N . ASN A 1 196 ? 16.954 0.517 25.781 1.00 18.29 ? 218 ASN A N 1 ATOM 1483 C CA . ASN A 1 196 ? 17.854 -0.626 25.815 1.00 19.38 ? 218 ASN A CA 1 ATOM 1484 C C . ASN A 1 196 ? 18.239 -0.760 27.278 1.00 19.56 ? 218 ASN A C 1 ATOM 1485 O O . ASN A 1 196 ? 18.768 0.194 27.852 1.00 21.06 ? 218 ASN A O 1 ATOM 1486 C CB . ASN A 1 196 ? 19.081 -0.371 24.929 1.00 19.92 ? 218 ASN A CB 1 ATOM 1487 C CG . ASN A 1 196 ? 19.751 -1.661 24.442 1.00 23.13 ? 218 ASN A CG 1 ATOM 1488 O OD1 . ASN A 1 196 ? 19.517 -2.747 24.968 1.00 26.17 ? 218 ASN A OD1 1 ATOM 1489 N ND2 . ASN A 1 196 ? 20.599 -1.532 23.423 1.00 26.98 ? 218 ASN A ND2 1 ATOM 1490 N N . PRO A 1 197 ? 17.939 -1.916 27.900 1.00 19.02 ? 219 PRO A N 1 ATOM 1491 C CA . PRO A 1 197 ? 17.356 -3.111 27.289 1.00 18.13 ? 219 PRO A CA 1 ATOM 1492 C C . PRO A 1 197 ? 15.958 -2.927 26.709 1.00 17.15 ? 219 PRO A C 1 ATOM 1493 O O . PRO A 1 197 ? 15.215 -2.041 27.121 1.00 17.06 ? 219 PRO A O 1 ATOM 1494 C CB . PRO A 1 197 ? 17.344 -4.127 28.434 1.00 18.50 ? 219 PRO A CB 1 ATOM 1495 C CG . PRO A 1 197 ? 17.349 -3.294 29.671 1.00 19.75 ? 219 PRO A CG 1 ATOM 1496 C CD . PRO A 1 197 ? 18.200 -2.121 29.338 1.00 19.09 ? 219 PRO A CD 1 ATOM 1497 N N . CYS A 1 198 ? 15.634 -3.770 25.736 1.00 16.40 ? 220 CYS A N 1 ATOM 1498 C CA . CYS A 1 198 ? 14.372 -3.677 25.021 1.00 15.25 ? 220 CYS A CA 1 ATOM 1499 C C . CYS A 1 198 ? 13.273 -4.377 25.786 1.00 14.98 ? 220 CYS A C 1 ATOM 1500 O O . CYS A 1 198 ? 13.541 -5.161 26.701 1.00 15.89 ? 220 CYS A O 1 ATOM 1501 C CB . CYS A 1 198 ? 14.528 -4.305 23.635 1.00 15.93 ? 220 CYS A CB 1 ATOM 1502 S SG . CYS A 1 198 ? 15.894 -3.557 22.721 1.00 15.01 ? 220 CYS A SG 1 ATOM 1503 N N . ALA A 1 199 ? 12.038 -4.089 25.403 1.00 13.97 ? 221 ALA A N 1 ATOM 1504 C CA . ALA A 1 199 ? 10.863 -4.779 25.939 1.00 13.89 ? 221 ALA A CA 1 ATOM 1505 C C . ALA A 1 199 ? 10.613 -4.498 27.416 1.00 13.87 ? 221 ALA A C 1 ATOM 1506 O O . ALA A 1 199 ? 9.915 -5.266 28.080 1.00 14.28 ? 221 ALA A O 1 ATOM 1507 C CB . ALA A 1 199 ? 10.952 -6.294 25.677 1.00 13.89 ? 221 ALA A CB 1 ATOM 1508 N N . GLN A 1 200 A 11.180 -3.405 27.921 1.00 13.95 ? 221 GLN A N 1 ATOM 1509 C CA . GLN A 1 200 A 10.944 -3.009 29.308 1.00 14.17 ? 221 GLN A CA 1 ATOM 1510 C C . GLN A 1 200 A 9.558 -2.378 29.434 1.00 14.25 ? 221 GLN A C 1 ATOM 1511 O O . GLN A 1 200 A 9.063 -1.749 28.505 1.00 14.09 ? 221 GLN A O 1 ATOM 1512 C CB A GLN A 1 200 A 11.944 -1.936 29.756 0.50 14.26 ? 221 GLN A CB 1 ATOM 1513 C CB B GLN A 1 200 A 12.059 -2.106 29.821 0.50 14.06 ? 221 GLN A CB 1 ATOM 1514 C CG A GLN A 1 200 A 13.419 -2.294 29.781 0.50 15.10 ? 221 GLN A CG 1 ATOM 1515 C CG B GLN A 1 200 A 13.408 -2.814 29.860 0.50 14.10 ? 221 GLN A CG 1 ATOM 1516 C CD A GLN A 1 200 A 14.280 -1.110 30.231 0.50 15.43 ? 221 GLN A CD 1 ATOM 1517 C CD B GLN A 1 200 A 13.324 -4.197 30.492 0.50 14.46 ? 221 GLN A CD 1 ATOM 1518 O OE1 A GLN A 1 200 A 14.164 -0.632 31.366 0.50 18.21 ? 221 GLN A OE1 1 ATOM 1519 O OE1 B GLN A 1 200 A 13.019 -4.328 31.675 0.50 14.14 ? 221 GLN A OE1 1 ATOM 1520 N NE2 A GLN A 1 200 A 15.131 -0.618 29.336 0.50 16.27 ? 221 GLN A NE2 1 ATOM 1521 N NE2 B GLN A 1 200 A 13.588 -5.242 29.697 0.50 12.79 ? 221 GLN A NE2 1 ATOM 1522 N N . PRO A 1 201 ? 8.917 -2.547 30.596 1.00 14.76 ? 222 PRO A N 1 ATOM 1523 C CA . PRO A 1 201 ? 7.647 -1.865 30.815 1.00 15.54 ? 222 PRO A CA 1 ATOM 1524 C C . PRO A 1 201 ? 7.748 -0.357 30.607 1.00 15.65 ? 222 PRO A C 1 ATOM 1525 O O . PRO A 1 201 ? 8.695 0.294 31.074 1.00 15.86 ? 222 PRO A O 1 ATOM 1526 C CB . PRO A 1 201 ? 7.340 -2.178 32.280 1.00 15.91 ? 222 PRO A CB 1 ATOM 1527 C CG . PRO A 1 201 ? 8.024 -3.485 32.510 1.00 16.22 ? 222 PRO A CG 1 ATOM 1528 C CD . PRO A 1 201 ? 9.301 -3.381 31.749 1.00 15.43 ? 222 PRO A CD 1 ATOM 1529 N N . ARG A 1 202 ? 6.774 0.190 29.877 1.00 15.87 ? 223 ARG A N 1 ATOM 1530 C CA . ARG A 1 202 ? 6.688 1.634 29.649 1.00 17.10 ? 223 ARG A CA 1 ATOM 1531 C C . ARG A 1 202 ? 7.911 2.230 28.955 1.00 16.39 ? 223 ARG A C 1 ATOM 1532 O O . ARG A 1 202 ? 8.188 3.428 29.064 1.00 17.05 ? 223 ARG A O 1 ATOM 1533 C CB . ARG A 1 202 ? 6.381 2.376 30.962 1.00 17.42 ? 223 ARG A CB 1 ATOM 1534 C CG . ARG A 1 202 ? 5.014 2.045 31.510 1.00 21.28 ? 223 ARG A CG 1 ATOM 1535 C CD . ARG A 1 202 ? 4.630 2.967 32.671 1.00 25.15 ? 223 ARG A CD 1 ATOM 1536 N NE . ARG A 1 202 ? 3.364 2.554 33.274 1.00 27.57 ? 223 ARG A NE 1 ATOM 1537 C CZ . ARG A 1 202 ? 2.187 3.128 33.027 1.00 28.15 ? 223 ARG A CZ 1 ATOM 1538 N NH1 . ARG A 1 202 ? 1.094 2.669 33.620 1.00 29.24 ? 223 ARG A NH1 1 ATOM 1539 N NH2 . ARG A 1 202 ? 2.104 4.164 32.199 1.00 27.44 ? 223 ARG A NH2 1 ATOM 1540 N N . LYS A 1 203 ? 8.646 1.390 28.231 1.00 15.64 ? 224 LYS A N 1 ATOM 1541 C CA . LYS A 1 203 ? 9.771 1.851 27.434 1.00 15.37 ? 224 LYS A CA 1 ATOM 1542 C C . LYS A 1 203 ? 9.591 1.305 26.027 1.00 14.87 ? 224 LYS A C 1 ATOM 1543 O O . LYS A 1 203 ? 10.288 0.376 25.610 1.00 14.83 ? 224 LYS A O 1 ATOM 1544 C CB . LYS A 1 203 ? 11.098 1.425 28.054 1.00 15.80 ? 224 LYS A CB 1 ATOM 1545 C CG . LYS A 1 203 ? 11.296 2.040 29.436 1.00 17.87 ? 224 LYS A CG 1 ATOM 1546 C CD . LYS A 1 203 ? 12.731 1.979 29.871 1.00 22.98 ? 224 LYS A CD 1 ATOM 1547 C CE . LYS A 1 203 ? 12.954 2.887 31.076 1.00 26.08 ? 224 LYS A CE 1 ATOM 1548 N NZ . LYS A 1 203 ? 14.274 2.632 31.726 1.00 29.48 ? 224 LYS A NZ 1 ATOM 1549 N N . PRO A 1 204 ? 8.636 1.899 25.296 1.00 14.17 ? 225 PRO A N 1 ATOM 1550 C CA . PRO A 1 204 ? 8.238 1.369 23.997 1.00 13.77 ? 225 PRO A CA 1 ATOM 1551 C C . PRO A 1 204 ? 9.198 1.741 22.873 1.00 13.02 ? 225 PRO A C 1 ATOM 1552 O O . PRO A 1 204 ? 10.242 2.372 23.102 1.00 13.13 ? 225 PRO A O 1 ATOM 1553 C CB . PRO A 1 204 ? 6.864 2.028 23.762 1.00 13.54 ? 225 PRO A CB 1 ATOM 1554 C CG . PRO A 1 204 ? 6.516 2.750 25.069 1.00 15.40 ? 225 PRO A CG 1 ATOM 1555 C CD . PRO A 1 204 ? 7.827 3.074 25.663 1.00 14.75 ? 225 PRO A CD 1 ATOM 1556 N N . GLY A 1 205 ? 8.839 1.321 21.667 1.00 11.77 ? 226 GLY A N 1 ATOM 1557 C CA . GLY A 1 205 ? 9.607 1.691 20.493 1.00 11.14 ? 226 GLY A CA 1 ATOM 1558 C C . GLY A 1 205 ? 9.114 3.003 19.932 1.00 10.57 ? 226 GLY A C 1 ATOM 1559 O O . GLY A 1 205 ? 7.936 3.346 20.057 1.00 10.42 ? 226 GLY A O 1 ATOM 1560 N N . ILE A 1 206 ? 10.028 3.718 19.292 1.00 10.30 ? 227 ILE A N 1 ATOM 1561 C CA . ILE A 1 206 ? 9.728 4.975 18.633 1.00 10.35 ? 227 ILE A CA 1 ATOM 1562 C C . ILE A 1 206 ? 9.895 4.742 17.143 1.00 9.89 ? 227 ILE A C 1 ATOM 1563 O O . ILE A 1 206 ? 10.964 4.336 16.705 1.00 9.57 ? 227 ILE A O 1 ATOM 1564 C CB . ILE A 1 206 ? 10.687 6.063 19.089 1.00 10.51 ? 227 ILE A CB 1 ATOM 1565 C CG1 . ILE A 1 206 ? 10.461 6.321 20.580 1.00 12.39 ? 227 ILE A CG1 1 ATOM 1566 C CG2 . ILE A 1 206 ? 10.446 7.330 18.324 1.00 10.53 ? 227 ILE A CG2 1 ATOM 1567 C CD1 . ILE A 1 206 ? 11.556 7.097 21.223 1.00 18.34 ? 227 ILE A CD1 1 ATOM 1568 N N . TYR A 1 207 ? 8.820 4.986 16.385 1.00 9.59 ? 228 TYR A N 1 ATOM 1569 C CA . TYR A 1 207 ? 8.769 4.642 14.971 1.00 9.37 ? 228 TYR A CA 1 ATOM 1570 C C . TYR A 1 207 ? 8.480 5.887 14.197 1.00 9.47 ? 228 TYR A C 1 ATOM 1571 O O . TYR A 1 207 ? 7.523 6.592 14.477 1.00 9.60 ? 228 TYR A O 1 ATOM 1572 C CB . TYR A 1 207 ? 7.644 3.624 14.721 1.00 9.40 ? 228 TYR A CB 1 ATOM 1573 C CG . TYR A 1 207 ? 7.877 2.325 15.439 1.00 8.66 ? 228 TYR A CG 1 ATOM 1574 C CD1 . TYR A 1 207 ? 7.547 2.194 16.793 1.00 9.52 ? 228 TYR A CD1 1 ATOM 1575 C CD2 . TYR A 1 207 ? 8.414 1.221 14.767 1.00 9.70 ? 228 TYR A CD2 1 ATOM 1576 C CE1 . TYR A 1 207 ? 7.758 1.013 17.472 1.00 8.42 ? 228 TYR A CE1 1 ATOM 1577 C CE2 . TYR A 1 207 ? 8.643 0.027 15.439 1.00 9.99 ? 228 TYR A CE2 1 ATOM 1578 C CZ . TYR A 1 207 ? 8.324 -0.064 16.784 1.00 9.30 ? 228 TYR A CZ 1 ATOM 1579 O OH . TYR A 1 207 ? 8.568 -1.245 17.444 1.00 10.63 ? 228 TYR A OH 1 ATOM 1580 N N . THR A 1 208 ? 9.317 6.195 13.226 1.00 8.69 ? 229 THR A N 1 ATOM 1581 C CA . THR A 1 208 ? 9.055 7.357 12.407 1.00 8.93 ? 229 THR A CA 1 ATOM 1582 C C . THR A 1 208 ? 7.704 7.189 11.740 1.00 9.38 ? 229 THR A C 1 ATOM 1583 O O . THR A 1 208 ? 7.398 6.118 11.231 1.00 9.27 ? 229 THR A O 1 ATOM 1584 C CB . THR A 1 208 ? 10.130 7.471 11.357 1.00 8.90 ? 229 THR A CB 1 ATOM 1585 O OG1 . THR A 1 208 ? 11.385 7.447 12.035 1.00 9.68 ? 229 THR A OG1 1 ATOM 1586 C CG2 . THR A 1 208 ? 9.973 8.761 10.554 1.00 10.73 ? 229 THR A CG2 1 ATOM 1587 N N . LYS A 1 209 ? 6.905 8.242 11.775 1.00 10.15 ? 230 LYS A N 1 ATOM 1588 C CA . LYS A 1 209 ? 5.494 8.130 11.430 1.00 9.84 ? 230 LYS A CA 1 ATOM 1589 C C . LYS A 1 209 ? 5.349 8.295 9.924 1.00 10.02 ? 230 LYS A C 1 ATOM 1590 O O . LYS A 1 209 ? 5.333 9.404 9.417 1.00 9.91 ? 230 LYS A O 1 ATOM 1591 C CB . LYS A 1 209 ? 4.723 9.212 12.186 1.00 10.17 ? 230 LYS A CB 1 ATOM 1592 C CG . LYS A 1 209 ? 3.232 9.152 12.062 1.00 12.68 ? 230 LYS A CG 1 ATOM 1593 C CD . LYS A 1 209 ? 2.711 10.193 12.998 1.00 15.46 ? 230 LYS A CD 1 ATOM 1594 C CE . LYS A 1 209 ? 1.227 10.241 13.042 1.00 19.66 ? 230 LYS A CE 1 ATOM 1595 N NZ . LYS A 1 209 ? 0.917 11.212 14.143 1.00 20.25 ? 230 LYS A NZ 1 ATOM 1596 N N . VAL A 1 210 ? 5.260 7.172 9.219 1.00 9.56 ? 231 VAL A N 1 ATOM 1597 C CA . VAL A 1 210 ? 5.299 7.154 7.760 1.00 9.72 ? 231 VAL A CA 1 ATOM 1598 C C . VAL A 1 210 ? 4.258 8.069 7.144 1.00 9.37 ? 231 VAL A C 1 ATOM 1599 O O . VAL A 1 210 ? 4.540 8.754 6.171 1.00 9.64 ? 231 VAL A O 1 ATOM 1600 C CB . VAL A 1 210 ? 5.117 5.714 7.245 1.00 9.99 ? 231 VAL A CB 1 ATOM 1601 C CG1 . VAL A 1 210 ? 5.018 5.689 5.729 1.00 9.54 ? 231 VAL A CG1 1 ATOM 1602 C CG2 . VAL A 1 210 ? 6.296 4.867 7.710 1.00 10.10 ? 231 VAL A CG2 1 ATOM 1603 N N . PHE A 1 211 ? 3.051 8.055 7.712 1.00 9.65 ? 232 PHE A N 1 ATOM 1604 C CA . PHE A 1 211 ? 1.970 8.871 7.169 1.00 9.76 ? 232 PHE A CA 1 ATOM 1605 C C . PHE A 1 211 ? 2.408 10.324 6.952 1.00 9.71 ? 232 PHE A C 1 ATOM 1606 O O . PHE A 1 211 ? 2.070 10.938 5.946 1.00 10.47 ? 232 PHE A O 1 ATOM 1607 C CB . PHE A 1 211 ? 0.769 8.848 8.103 1.00 10.28 ? 232 PHE A CB 1 ATOM 1608 C CG . PHE A 1 211 ? -0.340 9.765 7.668 1.00 9.96 ? 232 PHE A CG 1 ATOM 1609 C CD1 . PHE A 1 211 ? -1.210 9.400 6.653 1.00 10.49 ? 232 PHE A CD1 1 ATOM 1610 C CD2 . PHE A 1 211 ? -0.479 11.017 8.254 1.00 12.14 ? 232 PHE A CD2 1 ATOM 1611 C CE1 . PHE A 1 211 ? -2.232 10.267 6.259 1.00 10.92 ? 232 PHE A CE1 1 ATOM 1612 C CE2 . PHE A 1 211 ? -1.500 11.872 7.865 1.00 11.90 ? 232 PHE A CE2 1 ATOM 1613 C CZ . PHE A 1 211 ? -2.367 11.493 6.860 1.00 11.41 ? 232 PHE A CZ 1 ATOM 1614 N N . ASP A 1 212 ? 3.178 10.861 7.896 1.00 9.35 ? 233 ASP A N 1 ATOM 1615 C CA . ASP A 1 212 ? 3.585 12.271 7.836 1.00 10.41 ? 233 ASP A CA 1 ATOM 1616 C C . ASP A 1 212 ? 4.472 12.565 6.643 1.00 10.31 ? 233 ASP A C 1 ATOM 1617 O O . ASP A 1 212 ? 4.586 13.723 6.205 1.00 11.19 ? 233 ASP A O 1 ATOM 1618 C CB . ASP A 1 212 ? 4.355 12.635 9.101 1.00 10.49 ? 233 ASP A CB 1 ATOM 1619 C CG . ASP A 1 212 ? 3.463 12.776 10.324 1.00 13.99 ? 233 ASP A CG 1 ATOM 1620 O OD1 . ASP A 1 212 ? 2.228 12.624 10.207 1.00 15.59 ? 233 ASP A OD1 1 ATOM 1621 O OD2 . ASP A 1 212 ? 4.024 13.021 11.423 1.00 15.93 ? 233 ASP A OD2 1 ATOM 1622 N N . TYR A 1 213 ? 5.131 11.518 6.151 1.00 10.02 ? 234 TYR A N 1 ATOM 1623 C CA . TYR A 1 213 ? 6.126 11.636 5.104 1.00 9.42 ? 234 TYR A CA 1 ATOM 1624 C C . TYR A 1 213 ? 5.587 11.307 3.724 1.00 9.35 ? 234 TYR A C 1 ATOM 1625 O O . TYR A 1 213 ? 6.365 11.277 2.776 1.00 10.16 ? 234 TYR A O 1 ATOM 1626 C CB . TYR A 1 213 ? 7.318 10.731 5.431 1.00 8.82 ? 234 TYR A CB 1 ATOM 1627 C CG . TYR A 1 213 ? 8.094 11.283 6.597 1.00 8.80 ? 234 TYR A CG 1 ATOM 1628 C CD1 . TYR A 1 213 ? 7.703 11.015 7.911 1.00 10.00 ? 234 TYR A CD1 1 ATOM 1629 C CD2 . TYR A 1 213 ? 9.191 12.114 6.384 1.00 9.47 ? 234 TYR A CD2 1 ATOM 1630 C CE1 . TYR A 1 213 ? 8.405 11.559 8.994 1.00 10.62 ? 234 TYR A CE1 1 ATOM 1631 C CE2 . TYR A 1 213 ? 9.893 12.668 7.469 1.00 10.55 ? 234 TYR A CE2 1 ATOM 1632 C CZ . TYR A 1 213 ? 9.490 12.383 8.754 1.00 11.63 ? 234 TYR A CZ 1 ATOM 1633 O OH . TYR A 1 213 ? 10.182 12.938 9.819 1.00 11.43 ? 234 TYR A OH 1 ATOM 1634 N N . THR A 1 214 ? 4.276 11.063 3.612 1.00 10.42 ? 235 THR A N 1 ATOM 1635 C CA . THR A 1 214 ? 3.681 10.679 2.342 1.00 11.24 ? 235 THR A CA 1 ATOM 1636 C C . THR A 1 214 ? 4.041 11.666 1.254 1.00 11.09 ? 235 THR A C 1 ATOM 1637 O O . THR A 1 214 ? 4.508 11.288 0.179 1.00 10.58 ? 235 THR A O 1 ATOM 1638 C CB . THR A 1 214 ? 2.142 10.585 2.474 1.00 11.95 ? 235 THR A CB 1 ATOM 1639 O OG1 . THR A 1 214 ? 1.842 9.537 3.385 1.00 16.62 ? 235 THR A OG1 1 ATOM 1640 C CG2 . THR A 1 214 ? 1.485 10.277 1.112 1.00 14.89 ? 235 THR A CG2 1 ATOM 1641 N N . ASP A 1 215 ? 3.798 12.942 1.516 1.00 11.49 ? 236 ASP A N 1 ATOM 1642 C CA . ASP A 1 215 ? 4.003 13.927 0.468 1.00 11.49 ? 236 ASP A CA 1 ATOM 1643 C C . ASP A 1 215 ? 5.468 14.055 0.086 1.00 10.99 ? 236 ASP A C 1 ATOM 1644 O O . ASP A 1 215 ? 5.788 14.220 -1.089 1.00 11.52 ? 236 ASP A O 1 ATOM 1645 C CB . ASP A 1 215 ? 3.328 15.244 0.833 1.00 12.85 ? 236 ASP A CB 1 ATOM 1646 C CG . ASP A 1 215 ? 1.819 15.158 0.663 1.00 16.80 ? 236 ASP A CG 1 ATOM 1647 O OD1 . ASP A 1 215 ? 1.390 14.721 -0.419 1.00 24.59 ? 236 ASP A OD1 1 ATOM 1648 O OD2 . ASP A 1 215 ? 1.060 15.475 1.591 1.00 23.27 ? 236 ASP A OD2 1 ATOM 1649 N N . TRP A 1 216 ? 6.351 13.941 1.073 1.00 9.81 ? 237 TRP A N 1 ATOM 1650 C CA . TRP A 1 216 ? 7.767 13.997 0.815 1.00 10.25 ? 237 TRP A CA 1 ATOM 1651 C C . TRP A 1 216 ? 8.183 12.817 -0.062 1.00 9.81 ? 237 TRP A C 1 ATOM 1652 O O . TRP A 1 216 ? 8.875 12.980 -1.066 1.00 10.53 ? 237 TRP A O 1 ATOM 1653 C CB . TRP A 1 216 ? 8.522 13.982 2.138 1.00 10.14 ? 237 TRP A CB 1 ATOM 1654 C CG . TRP A 1 216 ? 9.985 13.937 2.009 1.00 10.83 ? 237 TRP A CG 1 ATOM 1655 C CD1 . TRP A 1 216 ? 10.805 14.959 1.632 1.00 11.91 ? 237 TRP A CD1 1 ATOM 1656 C CD2 . TRP A 1 216 ? 10.835 12.816 2.274 1.00 9.72 ? 237 TRP A CD2 1 ATOM 1657 N NE1 . TRP A 1 216 ? 12.120 14.549 1.663 1.00 11.19 ? 237 TRP A NE1 1 ATOM 1658 C CE2 . TRP A 1 216 ? 12.161 13.239 2.054 1.00 11.09 ? 237 TRP A CE2 1 ATOM 1659 C CE3 . TRP A 1 216 ? 10.607 11.503 2.704 1.00 10.08 ? 237 TRP A CE3 1 ATOM 1660 C CZ2 . TRP A 1 216 ? 13.241 12.387 2.213 1.00 9.58 ? 237 TRP A CZ2 1 ATOM 1661 C CZ3 . TRP A 1 216 ? 11.685 10.667 2.880 1.00 11.76 ? 237 TRP A CZ3 1 ATOM 1662 C CH2 . TRP A 1 216 ? 12.988 11.111 2.629 1.00 11.12 ? 237 TRP A CH2 1 ATOM 1663 N N . ILE A 1 217 ? 7.733 11.627 0.325 1.00 10.03 ? 238 ILE A N 1 ATOM 1664 C CA . ILE A 1 217 ? 8.041 10.430 -0.440 1.00 10.46 ? 238 ILE A CA 1 ATOM 1665 C C . ILE A 1 217 ? 7.544 10.574 -1.873 1.00 10.77 ? 238 ILE A C 1 ATOM 1666 O O . ILE A 1 217 ? 8.282 10.348 -2.825 1.00 11.06 ? 238 ILE A O 1 ATOM 1667 C CB . ILE A 1 217 ? 7.386 9.206 0.181 1.00 10.21 ? 238 ILE A CB 1 ATOM 1668 C CG1 . ILE A 1 217 ? 8.026 8.925 1.537 1.00 10.24 ? 238 ILE A CG1 1 ATOM 1669 C CG2 . ILE A 1 217 ? 7.577 7.983 -0.719 1.00 11.65 ? 238 ILE A CG2 1 ATOM 1670 C CD1 . ILE A 1 217 ? 7.186 8.034 2.448 1.00 10.34 ? 238 ILE A CD1 1 ATOM 1671 N N . GLN A 1 218 ? 6.285 10.972 -2.023 1.00 11.25 ? 239 GLN A N 1 ATOM 1672 C CA . GLN A 1 218 ? 5.728 11.103 -3.350 1.00 11.89 ? 239 GLN A CA 1 ATOM 1673 C C . GLN A 1 218 ? 6.451 12.164 -4.151 1.00 12.70 ? 239 GLN A C 1 ATOM 1674 O O . GLN A 1 218 ? 6.656 12.003 -5.342 1.00 13.37 ? 239 GLN A O 1 ATOM 1675 C CB . GLN A 1 218 ? 4.240 11.431 -3.275 1.00 12.01 ? 239 GLN A CB 1 ATOM 1676 C CG . GLN A 1 218 ? 3.436 10.287 -2.726 1.00 12.08 ? 239 GLN A CG 1 ATOM 1677 C CD . GLN A 1 218 ? 1.946 10.522 -2.810 1.00 12.76 ? 239 GLN A CD 1 ATOM 1678 O OE1 . GLN A 1 218 ? 1.161 9.580 -2.941 1.00 14.56 ? 239 GLN A OE1 1 ATOM 1679 N NE2 . GLN A 1 218 ? 1.550 11.776 -2.720 1.00 11.64 ? 239 GLN A NE2 1 ATOM 1680 N N . SER A 1 219 ? 6.806 13.269 -3.511 1.00 12.84 ? 240 SER A N 1 ATOM 1681 C CA . SER A 1 219 ? 7.468 14.342 -4.247 1.00 14.49 ? 240 SER A CA 1 ATOM 1682 C C . SER A 1 219 ? 8.798 13.851 -4.760 1.00 15.13 ? 240 SER A C 1 ATOM 1683 O O . SER A 1 219 ? 9.139 14.069 -5.913 1.00 15.74 ? 240 SER A O 1 ATOM 1684 C CB A SER A 1 219 ? 7.648 15.571 -3.372 0.50 14.45 ? 240 SER A CB 1 ATOM 1685 C CB B SER A 1 219 ? 7.645 15.580 -3.369 0.50 14.65 ? 240 SER A CB 1 ATOM 1686 O OG A SER A 1 219 ? 6.389 16.070 -2.984 0.50 15.30 ? 240 SER A OG 1 ATOM 1687 O OG B SER A 1 219 ? 8.315 16.613 -4.072 0.50 17.23 ? 240 SER A OG 1 ATOM 1688 N N . ILE A 1 220 ? 9.521 13.129 -3.915 1.00 14.72 ? 241 ILE A N 1 ATOM 1689 C CA . ILE A 1 220 ? 10.840 12.635 -4.310 1.00 15.45 ? 241 ILE A CA 1 ATOM 1690 C C . ILE A 1 220 ? 10.756 11.662 -5.473 1.00 16.10 ? 241 ILE A C 1 ATOM 1691 O O . ILE A 1 220 ? 11.501 11.782 -6.447 1.00 16.31 ? 241 ILE A O 1 ATOM 1692 C CB . ILE A 1 220 ? 11.551 11.967 -3.134 1.00 15.29 ? 241 ILE A CB 1 ATOM 1693 C CG1 . ILE A 1 220 ? 11.881 13.006 -2.051 1.00 15.92 ? 241 ILE A CG1 1 ATOM 1694 C CG2 . ILE A 1 220 ? 12.793 11.177 -3.613 1.00 16.11 ? 241 ILE A CG2 1 ATOM 1695 C CD1 A ILE A 1 220 ? 13.101 13.904 -2.310 0.50 16.54 ? 241 ILE A CD1 1 ATOM 1696 C CD1 B ILE A 1 220 ? 12.720 12.468 -0.995 0.50 14.64 ? 241 ILE A CD1 1 ATOM 1697 N N . ILE A 1 221 ? 9.858 10.691 -5.365 1.00 15.70 ? 242 ILE A N 1 ATOM 1698 C CA . ILE A 1 221 ? 9.789 9.619 -6.351 1.00 16.22 ? 242 ILE A CA 1 ATOM 1699 C C . ILE A 1 221 ? 9.155 10.084 -7.647 1.00 18.31 ? 242 ILE A C 1 ATOM 1700 O O . ILE A 1 221 ? 9.552 9.642 -8.730 1.00 18.90 ? 242 ILE A O 1 ATOM 1701 C CB . ILE A 1 221 ? 9.035 8.393 -5.804 1.00 15.64 ? 242 ILE A CB 1 ATOM 1702 C CG1 . ILE A 1 221 ? 9.716 7.889 -4.534 1.00 14.88 ? 242 ILE A CG1 1 ATOM 1703 C CG2 . ILE A 1 221 ? 8.974 7.281 -6.858 1.00 15.90 ? 242 ILE A CG2 1 ATOM 1704 C CD1 . ILE A 1 221 ? 9.046 6.653 -3.928 1.00 14.60 ? 242 ILE A CD1 1 ATOM 1705 N N . SER A 1 222 ? 8.181 10.982 -7.545 1.00 19.73 ? 243 SER A N 1 ATOM 1706 C CA . SER A 1 222 ? 7.409 11.374 -8.718 1.00 21.50 ? 243 SER A CA 1 ATOM 1707 C C . SER A 1 222 ? 8.089 12.460 -9.546 1.00 23.30 ? 243 SER A C 1 ATOM 1708 O O . SER A 1 222 ? 7.545 12.897 -10.564 1.00 23.83 ? 243 SER A O 1 ATOM 1709 C CB . SER A 1 222 ? 5.969 11.729 -8.329 1.00 21.36 ? 243 SER A CB 1 ATOM 1710 O OG A SER A 1 222 ? 5.480 10.760 -7.418 0.50 20.54 ? 243 SER A OG 1 ATOM 1711 O OG B SER A 1 222 ? 5.896 12.971 -7.655 0.50 21.77 ? 243 SER A OG 1 ATOM 1712 N N . GLY A 1 223 ? 9.280 12.887 -9.128 0.70 24.63 ? 244 GLY A N 1 ATOM 1713 C CA . GLY A 1 223 ? 10.086 13.795 -9.947 0.70 26.50 ? 244 GLY A CA 1 ATOM 1714 C C . GLY A 1 223 ? 11.021 14.680 -9.147 0.70 27.86 ? 244 GLY A C 1 ATOM 1715 O O . GLY A 1 223 ? 11.893 15.343 -9.705 0.70 28.79 ? 244 GLY A O 1 ATOM 1716 N N . ASN A 1 224 ? 10.832 14.666 -7.834 0.70 29.16 ? 245 ASN A N 1 ATOM 1717 C CA . ASN A 1 224 ? 11.517 15.547 -6.879 0.70 30.09 ? 245 ASN A CA 1 ATOM 1718 C C . ASN A 1 224 ? 11.934 16.926 -7.360 0.70 30.20 ? 245 ASN A C 1 ATOM 1719 O O . ASN A 1 224 ? 12.926 17.104 -8.075 0.70 30.71 ? 245 ASN A O 1 ATOM 1720 C CB . ASN A 1 224 ? 12.654 14.822 -6.111 0.70 30.55 ? 245 ASN A CB 1 ATOM 1721 C CG . ASN A 1 224 ? 14.042 15.062 -6.703 0.70 32.40 ? 245 ASN A CG 1 ATOM 1722 O OD1 . ASN A 1 224 ? 14.923 15.619 -6.037 0.70 33.45 ? 245 ASN A OD1 1 ATOM 1723 N ND2 . ASN A 1 224 ? 14.244 14.640 -7.951 0.70 34.21 ? 245 ASN A ND2 1 ATOM 1724 N N . THR A 1 225 A 11.128 17.904 -6.974 0.70 30.09 ? 245 THR A N 1 ATOM 1725 C CA . THR A 1 225 A 11.641 19.227 -6.707 0.70 29.54 ? 245 THR A CA 1 ATOM 1726 C C . THR A 1 225 A 12.601 18.984 -5.550 0.70 28.86 ? 245 THR A C 1 ATOM 1727 O O . THR A 1 225 A 12.840 17.832 -5.164 0.70 29.05 ? 245 THR A O 1 ATOM 1728 C CB . THR A 1 225 A 10.519 20.168 -6.248 0.70 29.89 ? 245 THR A CB 1 ATOM 1729 O OG1 . THR A 1 225 A 9.650 19.468 -5.344 0.70 30.54 ? 245 THR A OG1 1 ATOM 1730 C CG2 . THR A 1 225 A 9.704 20.656 -7.446 0.70 30.26 ? 245 THR A CG2 1 ATOM 1731 N N . ASP A 1 226 B 13.153 20.040 -4.973 0.70 27.51 ? 245 ASP A N 1 ATOM 1732 C CA . ASP A 1 226 B 13.910 19.861 -3.743 0.70 26.45 ? 245 ASP A CA 1 ATOM 1733 C C . ASP A 1 226 B 12.922 19.673 -2.583 0.70 25.77 ? 245 ASP A C 1 ATOM 1734 O O . ASP A 1 226 B 12.754 20.552 -1.734 0.70 25.76 ? 245 ASP A O 1 ATOM 1735 C CB . ASP A 1 226 B 14.852 21.038 -3.518 0.70 26.21 ? 245 ASP A CB 1 ATOM 1736 C CG . ASP A 1 226 B 14.138 22.372 -3.522 0.70 25.83 ? 245 ASP A CG 1 ATOM 1737 O OD1 . ASP A 1 226 B 14.553 23.238 -2.740 0.70 23.79 ? 245 ASP A OD1 1 ATOM 1738 O OD2 . ASP A 1 226 B 13.166 22.557 -4.291 0.70 25.41 ? 245 ASP A OD2 1 ATOM 1739 N N . ALA A 1 227 C 12.269 18.510 -2.575 1.00 25.05 ? 245 ALA A N 1 ATOM 1740 C CA . ALA A 1 227 C 11.196 18.193 -1.624 1.00 23.99 ? 245 ALA A CA 1 ATOM 1741 C C . ALA A 1 227 C 11.615 18.406 -0.181 1.00 23.29 ? 245 ALA A C 1 ATOM 1742 O O . ALA A 1 227 C 12.757 18.135 0.190 1.00 24.41 ? 245 ALA A O 1 ATOM 1743 C CB . ALA A 1 227 C 10.739 16.763 -1.817 1.00 24.37 ? 245 ALA A CB 1 ATOM 1744 N N . THR A 1 228 D 10.683 18.865 0.640 1.00 21.70 ? 245 THR A N 1 ATOM 1745 C CA . THR A 1 228 D 10.987 19.104 2.040 1.00 20.24 ? 245 THR A CA 1 ATOM 1746 C C . THR A 1 228 D 10.247 18.113 2.929 1.00 18.46 ? 245 THR A C 1 ATOM 1747 O O . THR A 1 228 D 9.092 17.783 2.692 1.00 17.77 ? 245 THR A O 1 ATOM 1748 C CB . THR A 1 228 D 10.646 20.542 2.444 1.00 20.70 ? 245 THR A CB 1 ATOM 1749 O OG1 . THR A 1 228 D 11.295 21.430 1.533 1.00 22.67 ? 245 THR A OG1 1 ATOM 1750 C CG2 . THR A 1 228 D 11.148 20.845 3.836 1.00 21.55 ? 245 THR A CG2 1 ATOM 1751 N N . CYS A 1 229 E 10.943 17.618 3.941 1.00 17.04 ? 245 CYS A N 1 ATOM 1752 C CA . CYS A 1 229 E 10.317 16.751 4.920 1.00 15.87 ? 245 CYS A CA 1 ATOM 1753 C C . CYS A 1 229 E 9.314 17.503 5.761 1.00 16.57 ? 245 CYS A C 1 ATOM 1754 O O . CYS A 1 229 E 9.426 18.718 5.928 1.00 16.77 ? 245 CYS A O 1 ATOM 1755 C CB . CYS A 1 229 E 11.375 16.140 5.821 1.00 15.07 ? 245 CYS A CB 1 ATOM 1756 S SG . CYS A 1 229 E 12.218 14.861 4.954 1.00 13.08 ? 245 CYS A SG 1 ATOM 1757 N N . PRO A 1 230 F 8.339 16.776 6.323 1.00 16.83 ? 245 PRO A N 1 ATOM 1758 C CA . PRO A 1 230 F 7.370 17.438 7.174 1.00 18.27 ? 245 PRO A CA 1 ATOM 1759 C C . PRO A 1 230 F 8.093 18.019 8.370 1.00 20.64 ? 245 PRO A C 1 ATOM 1760 O O . PRO A 1 230 F 9.112 17.454 8.803 1.00 20.14 ? 245 PRO A O 1 ATOM 1761 C CB . PRO A 1 230 F 6.463 16.292 7.628 1.00 18.13 ? 245 PRO A CB 1 ATOM 1762 C CG . PRO A 1 230 F 7.294 15.053 7.469 1.00 16.84 ? 245 PRO A CG 1 ATOM 1763 C CD . PRO A 1 230 F 8.093 15.329 6.233 1.00 17.06 ? 245 PRO A CD 1 ATOM 1764 N N . PRO A 1 231 G 7.584 19.143 8.900 1.00 22.90 ? 245 PRO A N 1 ATOM 1765 C CA . PRO A 1 231 G 8.211 19.754 10.061 1.00 24.69 ? 245 PRO A CA 1 ATOM 1766 C C . PRO A 1 231 G 7.986 18.899 11.301 1.00 25.49 ? 245 PRO A C 1 ATOM 1767 O O . PRO A 1 231 G 7.021 18.126 11.400 1.00 26.79 ? 245 PRO A O 1 ATOM 1768 C CB . PRO A 1 231 G 7.469 21.089 10.195 1.00 24.61 ? 245 PRO A CB 1 ATOM 1769 C CG . PRO A 1 231 G 6.141 20.855 9.564 1.00 24.61 ? 245 PRO A CG 1 ATOM 1770 C CD . PRO A 1 231 G 6.396 19.897 8.445 1.00 23.44 ? 245 PRO A CD 1 ATOM 1771 O OXT . PRO A 1 231 G 8.773 18.965 12.242 1.00 27.01 ? 245 PRO A OXT 1 HETATM 1772 C C1 . NAG B 2 . ? 25.380 -9.442 28.717 1.00 41.45 ? 701 NAG A C1 1 HETATM 1773 C C2 . NAG B 2 . ? 26.237 -10.025 29.840 1.00 45.59 ? 701 NAG A C2 1 HETATM 1774 C C3 . NAG B 2 . ? 25.459 -10.031 31.164 1.00 46.03 ? 701 NAG A C3 1 HETATM 1775 C C4 . NAG B 2 . ? 24.271 -9.055 31.234 1.00 45.98 ? 701 NAG A C4 1 HETATM 1776 C C5 . NAG B 2 . ? 24.233 -7.925 30.182 1.00 45.33 ? 701 NAG A C5 1 HETATM 1777 C C6 . NAG B 2 . ? 24.551 -6.580 30.833 1.00 45.27 ? 701 NAG A C6 1 HETATM 1778 C C7 . NAG B 2 . ? 26.245 -12.519 29.865 1.00 48.02 ? 701 NAG A C7 1 HETATM 1779 C C8 . NAG B 2 . ? 25.449 -13.269 28.834 1.00 48.24 ? 701 NAG A C8 1 HETATM 1780 N N2 . NAG B 2 . ? 26.759 -11.342 29.477 1.00 46.81 ? 701 NAG A N2 1 HETATM 1781 O O3 . NAG B 2 . ? 26.337 -9.795 32.250 1.00 46.49 ? 701 NAG A O3 1 HETATM 1782 O O4 . NAG B 2 . ? 23.069 -9.803 31.194 1.00 46.26 ? 701 NAG A O4 1 HETATM 1783 O O5 . NAG B 2 . ? 25.084 -8.104 29.054 1.00 43.72 ? 701 NAG A O5 1 HETATM 1784 O O6 . NAG B 2 . ? 24.696 -5.582 29.843 1.00 45.79 ? 701 NAG A O6 1 HETATM 1785 O O7 . NAG B 2 . ? 26.407 -13.001 30.991 1.00 48.24 ? 701 NAG A O7 1 HETATM 1786 C C1 . NAG C 2 . ? 23.936 16.857 18.080 0.50 34.72 ? 801 NAG A C1 1 HETATM 1787 C C2 . NAG C 2 . ? 25.418 17.217 17.923 0.50 36.90 ? 801 NAG A C2 1 HETATM 1788 C C3 . NAG C 2 . ? 26.271 15.950 17.799 0.50 37.21 ? 801 NAG A C3 1 HETATM 1789 C C4 . NAG C 2 . ? 25.995 14.978 18.946 0.50 37.48 ? 801 NAG A C4 1 HETATM 1790 C C5 . NAG C 2 . ? 24.492 14.766 19.143 0.50 37.18 ? 801 NAG A C5 1 HETATM 1791 C C6 . NAG C 2 . ? 24.215 13.990 20.429 0.50 37.62 ? 801 NAG A C6 1 HETATM 1792 C C7 . NAG C 2 . ? 26.633 18.966 16.725 0.50 38.30 ? 801 NAG A C7 1 HETATM 1793 C C8 . NAG C 2 . ? 26.324 20.400 17.045 0.50 38.23 ? 801 NAG A C8 1 HETATM 1794 N N2 . NAG C 2 . ? 25.621 18.099 16.787 0.50 37.24 ? 801 NAG A N2 1 HETATM 1795 O O3 . NAG C 2 . ? 27.642 16.285 17.800 0.50 37.56 ? 801 NAG A O3 1 HETATM 1796 O O4 . NAG C 2 . ? 26.630 13.745 18.682 0.50 37.92 ? 801 NAG A O4 1 HETATM 1797 O O5 . NAG C 2 . ? 23.819 16.012 19.214 0.50 36.45 ? 801 NAG A O5 1 HETATM 1798 O O6 . NAG C 2 . ? 22.829 13.984 20.701 0.50 38.65 ? 801 NAG A O6 1 HETATM 1799 O O7 . NAG C 2 . ? 27.778 18.631 16.418 0.50 38.96 ? 801 NAG A O7 1 HETATM 1800 C C1 . NDG D 3 . ? 32.117 1.037 6.359 0.50 35.92 ? 901 NDG A C1 1 HETATM 1801 C C2 . NDG D 3 . ? 33.198 1.372 5.331 0.50 38.49 ? 901 NDG A C2 1 HETATM 1802 C C3 . NDG D 3 . ? 34.211 2.372 5.895 0.50 38.91 ? 901 NDG A C3 1 HETATM 1803 C C4 . NDG D 3 . ? 33.537 3.549 6.602 0.50 39.08 ? 901 NDG A C4 1 HETATM 1804 C C5 . NDG D 3 . ? 32.386 3.098 7.506 0.50 38.65 ? 901 NDG A C5 1 HETATM 1805 C C6 . NDG D 3 . ? 31.601 4.295 8.035 0.50 39.20 ? 901 NDG A C6 1 HETATM 1806 C C7 . NDG D 3 . ? 34.598 0.123 3.764 0.50 39.69 ? 901 NDG A C7 1 HETATM 1807 C C8 . NDG D 3 . ? 35.947 -0.527 3.868 0.50 39.86 ? 901 NDG A C8 1 HETATM 1808 O O . NDG D 3 . ? 31.506 2.234 6.805 0.50 37.56 ? 901 NDG A O 1 HETATM 1809 O O3 . NDG D 3 . ? 35.022 2.869 4.850 0.50 39.32 ? 901 NDG A O3 1 HETATM 1810 O O4 . NDG D 3 . ? 34.504 4.239 7.367 0.50 39.81 ? 901 NDG A O4 1 HETATM 1811 O O6 . NDG D 3 . ? 30.742 4.787 7.028 0.50 39.94 ? 901 NDG A O6 1 HETATM 1812 O O7 . NDG D 3 . ? 34.219 0.597 2.691 0.50 40.03 ? 901 NDG A O7 1 HETATM 1813 N N2 . NDG D 3 . ? 33.867 0.161 4.880 0.50 39.00 ? 901 NDG A N2 1 HETATM 1814 S S . SO4 E 4 . ? 19.883 -0.363 15.871 1.00 23.39 ? 301 SO4 A S 1 HETATM 1815 O O1 . SO4 E 4 . ? 20.981 -1.297 16.091 1.00 25.28 ? 301 SO4 A O1 1 HETATM 1816 O O2 . SO4 E 4 . ? 18.656 -1.159 15.746 1.00 22.95 ? 301 SO4 A O2 1 HETATM 1817 O O3 . SO4 E 4 . ? 20.116 0.371 14.626 1.00 21.56 ? 301 SO4 A O3 1 HETATM 1818 O O4 . SO4 E 4 . ? 19.819 0.546 17.001 1.00 25.74 ? 301 SO4 A O4 1 HETATM 1819 C C . ACT F 5 . ? 18.392 -9.781 -10.376 1.00 37.14 ? 601 ACT A C 1 HETATM 1820 O O . ACT F 5 . ? 17.146 -9.741 -10.255 1.00 37.09 ? 601 ACT A O 1 HETATM 1821 O OXT . ACT F 5 . ? 19.067 -9.828 -9.317 1.00 36.77 ? 601 ACT A OXT 1 HETATM 1822 C CH3 . ACT F 5 . ? 19.041 -9.773 -11.727 1.00 37.52 ? 601 ACT A CH3 1 HETATM 1823 CL CL . CL G 6 . ? 14.068 18.237 3.974 1.00 18.07 ? 1001 CL A CL 1 HETATM 1824 C C1 . BEN H 7 . ? 14.580 -0.541 20.470 1.00 16.11 ? 401 BEN A C1 1 HETATM 1825 C C2 . BEN H 7 . ? 14.552 -0.342 19.083 1.00 17.25 ? 401 BEN A C2 1 HETATM 1826 C C3 . BEN H 7 . ? 15.719 -0.130 18.368 1.00 18.05 ? 401 BEN A C3 1 HETATM 1827 C C4 . BEN H 7 . ? 16.932 -0.099 19.045 1.00 17.44 ? 401 BEN A C4 1 HETATM 1828 C C5 . BEN H 7 . ? 16.971 -0.293 20.424 1.00 19.15 ? 401 BEN A C5 1 HETATM 1829 C C6 . BEN H 7 . ? 15.797 -0.518 21.139 1.00 18.01 ? 401 BEN A C6 1 HETATM 1830 C C . BEN H 7 . ? 13.309 -0.770 21.220 1.00 16.39 ? 401 BEN A C 1 HETATM 1831 N N1 . BEN H 7 . ? 12.224 -0.875 20.580 1.00 14.56 ? 401 BEN A N1 1 HETATM 1832 N N2 . BEN H 7 . ? 13.335 -0.841 22.558 1.00 16.61 ? 401 BEN A N2 1 HETATM 1833 C C1 . GOL I 8 . ? 21.236 11.781 16.401 1.00 31.18 ? 501 GOL A C1 1 HETATM 1834 O O1 . GOL I 8 . ? 20.355 12.308 17.371 1.00 28.26 ? 501 GOL A O1 1 HETATM 1835 C C2 . GOL I 8 . ? 21.393 12.770 15.249 1.00 32.12 ? 501 GOL A C2 1 HETATM 1836 O O2 . GOL I 8 . ? 20.143 13.041 14.651 1.00 32.96 ? 501 GOL A O2 1 HETATM 1837 C C3 . GOL I 8 . ? 22.345 12.198 14.204 1.00 33.27 ? 501 GOL A C3 1 HETATM 1838 O O3 . GOL I 8 . ? 22.105 12.769 12.931 1.00 33.67 ? 501 GOL A O3 1 HETATM 1839 O O . HOH J 9 . ? 13.290 -4.750 11.022 1.00 11.49 ? 1002 HOH A O 1 HETATM 1840 O O . HOH J 9 . ? 14.053 -10.521 15.537 1.00 12.82 ? 1003 HOH A O 1 HETATM 1841 O O . HOH J 9 . ? 10.715 0.680 6.796 1.00 11.10 ? 1004 HOH A O 1 HETATM 1842 O O . HOH J 9 . ? 15.649 -6.428 10.874 1.00 11.38 ? 1005 HOH A O 1 HETATM 1843 O O . HOH J 9 . ? 11.346 -10.484 3.498 1.00 10.10 ? 1006 HOH A O 1 HETATM 1844 O O . HOH J 9 . ? -7.105 3.551 22.183 1.00 14.07 ? 1007 HOH A O 1 HETATM 1845 O O . HOH J 9 . ? 9.660 -12.152 2.145 1.00 11.71 ? 1008 HOH A O 1 HETATM 1846 O O . HOH J 9 . ? 10.037 -14.795 2.873 1.00 12.46 ? 1009 HOH A O 1 HETATM 1847 O O . HOH J 9 . ? 8.957 -2.078 25.831 1.00 13.00 ? 1010 HOH A O 1 HETATM 1848 O O . HOH J 9 . ? 14.230 -9.368 2.567 1.00 11.28 ? 1011 HOH A O 1 HETATM 1849 O O . HOH J 9 . ? 7.940 -1.581 19.965 1.00 12.10 ? 1012 HOH A O 1 HETATM 1850 O O . HOH J 9 . ? 2.105 6.597 9.940 1.00 11.11 ? 1013 HOH A O 1 HETATM 1851 O O . HOH J 9 . ? 12.153 9.531 13.585 1.00 11.69 ? 1014 HOH A O 1 HETATM 1852 O O . HOH J 9 . ? 16.015 -16.199 2.624 1.00 12.41 ? 1015 HOH A O 1 HETATM 1853 O O . HOH J 9 . ? 15.690 11.837 7.200 1.00 12.31 ? 1016 HOH A O 1 HETATM 1854 O O . HOH J 9 . ? 13.523 9.151 15.945 1.00 12.61 ? 1017 HOH A O 1 HETATM 1855 O O . HOH J 9 . ? -2.722 1.996 23.553 1.00 13.04 ? 1018 HOH A O 1 HETATM 1856 O O . HOH J 9 . ? 7.183 -12.820 3.314 1.00 12.80 ? 1019 HOH A O 1 HETATM 1857 O O . HOH J 9 . ? -0.433 1.232 -3.992 1.00 14.58 ? 1020 HOH A O 1 HETATM 1858 O O . HOH J 9 . ? 11.245 -8.372 0.506 1.00 12.48 ? 1021 HOH A O 1 HETATM 1859 O O . HOH J 9 . ? 13.967 -18.800 3.725 1.00 14.12 ? 1022 HOH A O 1 HETATM 1860 O O . HOH J 9 . ? 13.285 10.025 18.679 1.00 15.10 ? 1023 HOH A O 1 HETATM 1861 O O . HOH J 9 . ? 10.266 15.406 13.179 1.00 16.17 ? 1024 HOH A O 1 HETATM 1862 O O . HOH J 9 . ? 11.059 11.935 13.416 1.00 12.47 ? 1025 HOH A O 1 HETATM 1863 O O . HOH J 9 . ? 5.553 14.646 3.733 1.00 14.04 ? 1026 HOH A O 1 HETATM 1864 O O . HOH J 9 . ? 16.503 -18.516 14.428 1.00 18.07 ? 1027 HOH A O 1 HETATM 1865 O O . HOH J 9 . ? 19.878 -11.800 12.288 1.00 14.77 ? 1028 HOH A O 1 HETATM 1866 O O . HOH J 9 . ? 12.566 -1.282 26.547 1.00 15.53 ? 1029 HOH A O 1 HETATM 1867 O O . HOH J 9 . ? 1.872 6.994 19.369 1.00 14.90 ? 1030 HOH A O 1 HETATM 1868 O O . HOH J 9 . ? 20.187 21.135 6.573 1.00 16.71 ? 1031 HOH A O 1 HETATM 1869 O O . HOH J 9 . ? 3.583 -10.269 2.927 1.00 16.38 ? 1032 HOH A O 1 HETATM 1870 O O . HOH J 9 . ? 9.445 -3.881 12.918 1.00 13.87 ? 1033 HOH A O 1 HETATM 1871 O O . HOH J 9 . ? 18.262 14.528 15.781 1.00 17.32 ? 1034 HOH A O 1 HETATM 1872 O O . HOH J 9 . ? 11.782 16.272 16.548 1.00 18.34 ? 1035 HOH A O 1 HETATM 1873 O O . HOH J 9 . ? 2.394 14.098 3.834 1.00 16.32 ? 1036 HOH A O 1 HETATM 1874 O O . HOH J 9 . ? 11.229 -12.823 19.331 1.00 15.14 ? 1037 HOH A O 1 HETATM 1875 O O . HOH J 9 . ? 6.912 -2.742 24.103 1.00 14.94 ? 1038 HOH A O 1 HETATM 1876 O O . HOH J 9 . ? 0.277 -1.868 -0.656 0.50 9.52 ? 1039 HOH A O 1 HETATM 1877 O O . HOH J 9 . ? 17.608 3.156 20.144 1.00 17.68 ? 1040 HOH A O 1 HETATM 1878 O O . HOH J 9 . ? 15.941 0.652 -10.237 1.00 19.57 ? 1041 HOH A O 1 HETATM 1879 O O . HOH J 9 . ? 2.907 -11.392 19.540 1.00 18.81 ? 1042 HOH A O 1 HETATM 1880 O O . HOH J 9 . ? 6.637 -0.337 26.560 1.00 16.83 ? 1043 HOH A O 1 HETATM 1881 O O . HOH J 9 . ? 1.806 -1.965 -2.874 1.00 17.57 ? 1044 HOH A O 1 HETATM 1882 O O . HOH J 9 . ? 6.444 5.650 29.898 1.00 25.13 ? 1045 HOH A O 1 HETATM 1883 O O . HOH J 9 . ? 18.198 2.643 17.453 1.00 22.61 ? 1046 HOH A O 1 HETATM 1884 O O . HOH J 9 . ? 0.258 12.710 4.857 1.00 18.26 ? 1047 HOH A O 1 HETATM 1885 O O . HOH J 9 . ? 13.011 -12.576 -7.208 1.00 21.25 ? 1048 HOH A O 1 HETATM 1886 O O . HOH J 9 . ? 5.532 -7.812 -10.798 1.00 21.89 ? 1049 HOH A O 1 HETATM 1887 O O . HOH J 9 . ? 12.104 18.565 13.437 1.00 22.83 ? 1050 HOH A O 1 HETATM 1888 O O . HOH J 9 . ? -6.301 -0.050 8.092 1.00 21.65 ? 1051 HOH A O 1 HETATM 1889 O O . HOH J 9 . ? 14.286 -7.814 26.881 1.00 20.07 ? 1052 HOH A O 1 HETATM 1890 O O . HOH J 9 . ? 2.943 14.037 13.737 1.00 28.07 ? 1053 HOH A O 1 HETATM 1891 O O . HOH J 9 . ? -1.016 9.652 21.146 1.00 24.27 ? 1054 HOH A O 1 HETATM 1892 O O . HOH J 9 . ? -0.205 -2.163 25.419 1.00 19.88 ? 1055 HOH A O 1 HETATM 1893 O O . HOH J 9 . ? -2.285 7.726 28.982 1.00 22.06 ? 1056 HOH A O 1 HETATM 1894 O O . HOH J 9 . ? 29.998 -4.729 6.925 1.00 31.74 ? 1057 HOH A O 1 HETATM 1895 O O . HOH J 9 . ? 16.039 22.587 17.696 1.00 23.09 ? 1058 HOH A O 1 HETATM 1896 O O . HOH J 9 . ? 12.405 -13.027 22.576 1.00 22.99 ? 1059 HOH A O 1 HETATM 1897 O O . HOH J 9 . ? 10.488 18.706 15.786 1.00 20.65 ? 1060 HOH A O 1 HETATM 1898 O O . HOH J 9 . ? 14.439 16.205 1.575 1.00 23.28 ? 1061 HOH A O 1 HETATM 1899 O O . HOH J 9 . ? 15.130 -5.911 -12.376 1.00 21.54 ? 1062 HOH A O 1 HETATM 1900 O O . HOH J 9 . ? 3.071 -9.129 8.691 1.00 26.92 ? 1063 HOH A O 1 HETATM 1901 O O . HOH J 9 . ? 11.650 8.338 -9.689 1.00 25.81 ? 1064 HOH A O 1 HETATM 1902 O O . HOH J 9 . ? -5.028 2.724 10.560 1.00 25.00 ? 1065 HOH A O 1 HETATM 1903 O O . HOH J 9 . ? 13.441 -21.531 7.340 1.00 30.27 ? 1066 HOH A O 1 HETATM 1904 O O . HOH J 9 . ? 18.948 7.166 -10.773 1.00 29.28 ? 1067 HOH A O 1 HETATM 1905 O O . HOH J 9 . ? 11.180 5.520 -9.674 1.00 24.73 ? 1068 HOH A O 1 HETATM 1906 O O . HOH J 9 . ? -6.351 3.049 12.695 1.00 27.64 ? 1069 HOH A O 1 HETATM 1907 O O . HOH J 9 . ? 25.425 -7.988 22.709 1.00 45.62 ? 1070 HOH A O 1 HETATM 1908 O O . HOH J 9 . ? 2.052 10.346 16.992 1.00 25.11 ? 1071 HOH A O 1 HETATM 1909 O O . HOH J 9 . ? 6.211 -19.884 7.730 1.00 26.83 ? 1072 HOH A O 1 HETATM 1910 O O . HOH J 9 . ? 8.001 0.846 -9.335 1.00 20.49 ? 1073 HOH A O 1 HETATM 1911 O O . HOH J 9 . ? -1.958 -5.499 4.972 1.00 31.85 ? 1074 HOH A O 1 HETATM 1912 O O . HOH J 9 . ? 16.973 -15.119 -6.673 1.00 22.83 ? 1075 HOH A O 1 HETATM 1913 O O . HOH J 9 . ? 19.856 -5.118 23.866 1.00 32.77 ? 1076 HOH A O 1 HETATM 1914 O O . HOH J 9 . ? 22.551 -2.359 -11.568 1.00 28.73 ? 1077 HOH A O 1 HETATM 1915 O O . HOH J 9 . ? 14.219 9.816 -9.035 1.00 29.58 ? 1078 HOH A O 1 HETATM 1916 O O . HOH J 9 . ? 4.760 15.221 14.737 1.00 30.10 ? 1079 HOH A O 1 HETATM 1917 O O . HOH J 9 . ? 1.435 14.527 -2.812 1.00 30.66 ? 1080 HOH A O 1 HETATM 1918 O O . HOH J 9 . ? 16.623 0.900 -12.659 1.00 32.33 ? 1081 HOH A O 1 HETATM 1919 O O . HOH J 9 . ? 21.597 10.470 8.587 1.00 28.78 ? 1082 HOH A O 1 HETATM 1920 O O . HOH J 9 . ? 21.518 -3.393 27.570 1.00 39.39 ? 1083 HOH A O 1 HETATM 1921 O O . HOH J 9 . ? -1.576 -5.195 10.307 1.00 27.64 ? 1084 HOH A O 1 HETATM 1922 O O . HOH J 9 . ? 14.875 -22.061 -0.744 1.00 29.58 ? 1085 HOH A O 1 HETATM 1923 O O . HOH J 9 . ? 3.582 -6.921 0.418 1.00 28.70 ? 1086 HOH A O 1 HETATM 1924 O O . HOH J 9 . ? -2.158 -0.609 24.227 1.00 20.10 ? 1087 HOH A O 1 HETATM 1925 O O . HOH J 9 . ? -0.032 8.594 18.103 1.00 18.51 ? 1088 HOH A O 1 HETATM 1926 O O . HOH J 9 . ? 19.777 22.450 19.327 1.00 23.97 ? 1089 HOH A O 1 HETATM 1927 O O . HOH J 9 . ? 10.342 -10.548 26.917 1.00 25.52 ? 1090 HOH A O 1 HETATM 1928 O O . HOH J 9 . ? 22.063 -11.020 10.753 1.00 26.82 ? 1091 HOH A O 1 HETATM 1929 O O . HOH J 9 . ? 11.165 -10.973 -7.898 1.00 28.62 ? 1092 HOH A O 1 HETATM 1930 O O . HOH J 9 . ? 1.471 -10.410 -5.869 1.00 34.16 ? 1093 HOH A O 1 HETATM 1931 O O . HOH J 9 . ? 3.858 -0.965 32.579 1.00 25.46 ? 1094 HOH A O 1 HETATM 1932 O O . HOH J 9 . ? 17.702 -22.018 10.313 1.00 26.41 ? 1095 HOH A O 1 HETATM 1933 O O . HOH J 9 . ? 3.892 15.709 -2.504 1.00 29.05 ? 1096 HOH A O 1 HETATM 1934 O O . HOH J 9 . ? 24.762 -8.679 -6.109 1.00 25.23 ? 1097 HOH A O 1 HETATM 1935 O O . HOH J 9 . ? 4.056 14.790 -5.642 1.00 26.77 ? 1098 HOH A O 1 HETATM 1936 O O . HOH J 9 . ? 9.563 -0.090 -11.320 1.00 31.84 ? 1099 HOH A O 1 HETATM 1937 O O . HOH J 9 . ? -1.828 7.935 16.455 1.00 29.17 ? 1100 HOH A O 1 HETATM 1938 O O . HOH J 9 . ? -6.341 -2.768 15.831 1.00 31.33 ? 1101 HOH A O 1 HETATM 1939 O O . HOH J 9 . ? -3.541 2.462 3.201 1.00 25.10 ? 1102 HOH A O 1 HETATM 1940 O O . HOH J 9 . ? -1.300 14.806 5.574 1.00 22.78 ? 1103 HOH A O 1 HETATM 1941 O O . HOH J 9 . ? 0.616 14.468 7.392 1.00 29.11 ? 1104 HOH A O 1 HETATM 1942 O O . HOH J 9 . ? 12.904 -9.230 -9.964 1.00 28.72 ? 1105 HOH A O 1 HETATM 1943 O O . HOH J 9 . ? 23.448 20.223 18.702 1.00 33.06 ? 1106 HOH A O 1 HETATM 1944 O O . HOH J 9 . ? 17.846 4.867 22.195 1.00 27.49 ? 1107 HOH A O 1 HETATM 1945 O O . HOH J 9 . ? 18.044 3.137 26.654 1.00 32.28 ? 1108 HOH A O 1 HETATM 1946 O O . HOH J 9 . ? 7.718 -16.725 -6.923 1.00 28.59 ? 1109 HOH A O 1 HETATM 1947 O O . HOH J 9 . ? 10.902 -13.206 25.320 1.00 35.42 ? 1110 HOH A O 1 HETATM 1948 O O . HOH J 9 . ? 4.039 12.092 29.282 1.00 30.84 ? 1111 HOH A O 1 HETATM 1949 O O . HOH J 9 . ? 18.731 21.561 16.789 1.00 28.78 ? 1112 HOH A O 1 HETATM 1950 O O . HOH J 9 . ? 23.832 -13.756 17.744 1.00 27.09 ? 1113 HOH A O 1 HETATM 1951 O O . HOH J 9 . ? 9.853 13.694 26.134 1.00 34.28 ? 1114 HOH A O 1 HETATM 1952 O O . HOH J 9 . ? -1.553 -3.051 27.392 1.00 29.31 ? 1115 HOH A O 1 HETATM 1953 O O . HOH J 9 . ? 11.860 -20.779 0.621 1.00 31.72 ? 1116 HOH A O 1 HETATM 1954 O O . HOH J 9 . ? 6.244 17.219 3.512 1.00 30.43 ? 1117 HOH A O 1 HETATM 1955 O O . HOH J 9 . ? 2.224 -9.177 0.752 1.00 27.94 ? 1118 HOH A O 1 HETATM 1956 O O . HOH J 9 . ? 18.106 -8.669 31.946 1.00 32.65 ? 1119 HOH A O 1 HETATM 1957 O O . HOH J 9 . ? 15.769 6.191 23.158 1.00 37.87 ? 1120 HOH A O 1 HETATM 1958 O O . HOH J 9 . ? 7.196 17.550 0.256 1.00 37.37 ? 1121 HOH A O 1 HETATM 1959 O O . HOH J 9 . ? 10.129 -0.486 33.217 1.00 32.41 ? 1122 HOH A O 1 HETATM 1960 O O . HOH J 9 . ? 6.523 -19.332 0.793 1.00 26.72 ? 1123 HOH A O 1 HETATM 1961 O O . HOH J 9 . ? 7.558 20.734 5.102 1.00 36.72 ? 1124 HOH A O 1 HETATM 1962 O O . HOH J 9 . ? 3.631 -15.695 -0.611 1.00 38.43 ? 1125 HOH A O 1 HETATM 1963 O O . HOH J 9 . ? 8.289 14.537 20.419 1.00 30.25 ? 1126 HOH A O 1 HETATM 1964 O O . HOH J 9 . ? 22.249 -2.650 13.814 1.00 35.17 ? 1127 HOH A O 1 HETATM 1965 O O . HOH J 9 . ? 9.261 -15.365 22.486 1.00 37.23 ? 1128 HOH A O 1 HETATM 1966 O O . HOH J 9 . ? -3.379 -4.714 12.889 1.00 27.59 ? 1129 HOH A O 1 HETATM 1967 O O . HOH J 9 . ? 12.961 -21.146 4.702 1.00 28.84 ? 1130 HOH A O 1 HETATM 1968 O O . HOH J 9 . ? 5.110 12.630 16.848 1.00 30.86 ? 1131 HOH A O 1 HETATM 1969 O O . HOH J 9 . ? 24.539 -0.281 -11.213 1.00 56.91 ? 1132 HOH A O 1 HETATM 1970 O O . HOH J 9 . ? -8.719 3.732 8.399 1.00 32.83 ? 1133 HOH A O 1 HETATM 1971 O O . HOH J 9 . ? 4.352 16.510 10.563 1.00 36.27 ? 1134 HOH A O 1 HETATM 1972 O O . HOH J 9 . ? 13.972 -18.381 15.279 1.00 37.99 ? 1135 HOH A O 1 HETATM 1973 O O . HOH J 9 . ? 14.078 11.989 -7.232 1.00 46.74 ? 1136 HOH A O 1 HETATM 1974 O O . HOH J 9 . ? -8.696 7.740 17.227 1.00 37.27 ? 1137 HOH A O 1 HETATM 1975 O O . HOH J 9 . ? 22.035 -5.941 -7.712 1.00 32.95 ? 1138 HOH A O 1 HETATM 1976 O O . HOH J 9 . ? 1.013 -8.812 21.828 1.00 34.27 ? 1139 HOH A O 1 HETATM 1977 O O . HOH J 9 . ? 7.982 -6.311 -5.920 1.00 28.68 ? 1140 HOH A O 1 HETATM 1978 O O . HOH J 9 . ? 9.015 11.140 32.686 1.00 37.11 ? 1141 HOH A O 1 HETATM 1979 O O . HOH J 9 . ? 14.807 -14.161 -8.764 1.00 39.10 ? 1142 HOH A O 1 HETATM 1980 O O . HOH J 9 . ? 5.726 11.278 -11.856 1.00 38.63 ? 1143 HOH A O 1 HETATM 1981 O O . HOH J 9 . ? 21.837 -1.157 7.994 1.00 31.90 ? 1144 HOH A O 1 HETATM 1982 O O . HOH J 9 . ? 10.816 12.899 30.583 1.00 57.59 ? 1145 HOH A O 1 HETATM 1983 O O . HOH J 9 . ? 1.270 13.756 24.041 1.00 39.45 ? 1146 HOH A O 1 HETATM 1984 O O . HOH J 9 . ? 26.270 0.044 -1.536 1.00 30.44 ? 1147 HOH A O 1 HETATM 1985 O O . HOH J 9 . ? 9.324 -18.979 16.699 1.00 37.28 ? 1148 HOH A O 1 HETATM 1986 O O . HOH J 9 . ? -1.070 -8.409 13.751 1.00 33.70 ? 1149 HOH A O 1 HETATM 1987 O O . HOH J 9 . ? -4.515 9.908 25.343 1.00 36.10 ? 1150 HOH A O 1 HETATM 1988 O O . HOH J 9 . ? 3.826 5.650 31.201 1.00 34.11 ? 1151 HOH A O 1 HETATM 1989 O O . HOH J 9 . ? 5.999 -5.080 -12.693 1.00 37.15 ? 1152 HOH A O 1 HETATM 1990 O O . HOH J 9 . ? 5.802 0.562 34.212 1.00 41.19 ? 1153 HOH A O 1 HETATM 1991 O O . HOH J 9 . ? 7.581 15.278 23.040 1.00 37.92 ? 1154 HOH A O 1 HETATM 1992 O O . HOH J 9 . ? 12.034 -15.019 20.798 1.00 33.63 ? 1155 HOH A O 1 HETATM 1993 O O . HOH J 9 . ? -0.104 13.019 11.680 1.00 44.27 ? 1156 HOH A O 1 HETATM 1994 O O . HOH J 9 . ? 21.331 14.733 18.064 1.00 36.03 ? 1157 HOH A O 1 HETATM 1995 O O . HOH J 9 . ? 24.081 5.609 12.292 1.00 34.40 ? 1158 HOH A O 1 HETATM 1996 O O . HOH J 9 . ? 6.310 -13.138 25.220 1.00 53.60 ? 1159 HOH A O 1 HETATM 1997 O O . HOH J 9 . ? 9.675 -19.963 -3.497 1.00 46.97 ? 1160 HOH A O 1 HETATM 1998 O O . HOH J 9 . ? 4.558 -13.163 20.512 1.00 42.75 ? 1161 HOH A O 1 HETATM 1999 O O . HOH J 9 . ? 16.046 2.670 28.360 1.00 55.83 ? 1162 HOH A O 1 HETATM 2000 O O . HOH J 9 . ? -1.282 12.034 24.251 1.00 34.72 ? 1163 HOH A O 1 HETATM 2001 O O . HOH J 9 . ? 22.167 -4.027 23.077 1.00 38.34 ? 1164 HOH A O 1 HETATM 2002 O O . HOH J 9 . ? 12.575 -1.704 33.402 1.00 36.59 ? 1165 HOH A O 1 HETATM 2003 O O . HOH J 9 . ? 22.497 -8.446 -7.329 1.00 34.54 ? 1166 HOH A O 1 HETATM 2004 O O . HOH J 9 . ? 8.253 19.706 -0.478 1.00 38.73 ? 1167 HOH A O 1 HETATM 2005 O O . HOH J 9 . ? 20.367 4.287 17.206 1.00 43.62 ? 1168 HOH A O 1 HETATM 2006 O O . HOH J 9 . ? 6.269 13.325 30.253 1.00 34.92 ? 1169 HOH A O 1 HETATM 2007 O O . HOH J 9 . ? 10.325 -18.541 -5.458 1.00 36.67 ? 1170 HOH A O 1 HETATM 2008 O O . HOH J 9 . ? 5.643 17.458 13.669 1.00 34.95 ? 1171 HOH A O 1 HETATM 2009 O O . HOH J 9 . ? 22.079 -9.979 -9.669 1.00 39.28 ? 1172 HOH A O 1 HETATM 2010 O O . HOH J 9 . ? -0.041 17.082 4.651 1.00 33.37 ? 1173 HOH A O 1 HETATM 2011 O O . HOH J 9 . ? -1.569 9.835 14.598 1.00 45.75 ? 1174 HOH A O 1 HETATM 2012 O O . HOH J 9 . ? 9.109 -2.479 -11.948 1.00 25.15 ? 1175 HOH A O 1 HETATM 2013 O O . HOH J 9 . ? 1.633 -0.632 33.011 1.00 36.82 ? 1176 HOH A O 1 HETATM 2014 O O . HOH J 9 . ? 19.209 -13.377 -7.313 1.00 35.35 ? 1177 HOH A O 1 HETATM 2015 O O . HOH J 9 . ? -1.363 -6.071 12.811 1.00 58.23 ? 1178 HOH A O 1 HETATM 2016 O O . HOH J 9 . ? 18.385 -5.648 32.572 1.00 45.80 ? 1179 HOH A O 1 HETATM 2017 O O . HOH J 9 . ? 2.985 17.526 8.751 1.00 35.72 ? 1180 HOH A O 1 HETATM 2018 O O . HOH J 9 . ? 23.978 6.041 -7.488 1.00 36.62 ? 1181 HOH A O 1 HETATM 2019 O O . HOH J 9 . ? 3.548 18.267 -1.538 1.00 34.99 ? 1182 HOH A O 1 HETATM 2020 O O . HOH J 9 . ? -0.986 -12.543 14.693 1.00 42.20 ? 1183 HOH A O 1 HETATM 2021 O O . HOH J 9 . ? -6.716 8.816 11.227 1.00 42.21 ? 1184 HOH A O 1 HETATM 2022 O O . HOH J 9 . ? 13.081 7.008 -13.581 1.00 36.97 ? 1185 HOH A O 1 HETATM 2023 O O . HOH J 9 . ? 25.743 1.390 -3.865 1.00 49.02 ? 1186 HOH A O 1 HETATM 2024 O O . HOH J 9 . ? 23.093 8.226 9.152 1.00 44.30 ? 1187 HOH A O 1 HETATM 2025 O O . HOH J 9 . ? 3.567 -8.649 26.345 1.00 37.74 ? 1188 HOH A O 1 HETATM 2026 O O . HOH J 9 . ? -4.122 -2.458 23.722 0.50 24.31 ? 1189 HOH A O 1 HETATM 2027 O O . HOH J 9 . ? -0.692 -11.111 20.344 1.00 50.88 ? 1190 HOH A O 1 HETATM 2028 O O . HOH J 9 . ? 21.862 -21.112 12.657 1.00 40.54 ? 1191 HOH A O 1 HETATM 2029 O O . HOH J 9 . ? -4.970 -5.014 21.328 1.00 33.17 ? 1192 HOH A O 1 HETATM 2030 O O . HOH J 9 . ? 3.231 17.039 4.331 1.00 33.59 ? 1193 HOH A O 1 HETATM 2031 O O . HOH J 9 . ? -1.221 -6.594 20.870 1.00 42.81 ? 1194 HOH A O 1 HETATM 2032 O O . HOH J 9 . ? 0.863 -4.187 -0.925 1.00 42.33 ? 1195 HOH A O 1 HETATM 2033 O O . HOH J 9 . ? -4.151 9.106 17.342 1.00 38.70 ? 1196 HOH A O 1 HETATM 2034 O O . HOH J 9 . ? 25.423 -11.061 17.761 1.00 39.55 ? 1197 HOH A O 1 HETATM 2035 O O . HOH J 9 . ? 6.893 -21.869 2.213 1.00 49.75 ? 1198 HOH A O 1 HETATM 2036 O O . HOH J 9 . ? 22.083 -11.923 3.240 1.00 37.16 ? 1199 HOH A O 1 HETATM 2037 O O . HOH J 9 . ? 12.865 10.029 31.271 1.00 44.37 ? 1200 HOH A O 1 HETATM 2038 O O . HOH J 9 . ? 0.448 -6.391 5.806 1.00 47.04 ? 1201 HOH A O 1 HETATM 2039 O O . HOH J 9 . ? 4.837 15.128 18.113 1.00 50.20 ? 1202 HOH A O 1 HETATM 2040 O O . HOH J 9 . ? 20.437 4.027 22.221 1.00 44.18 ? 1203 HOH A O 1 HETATM 2041 O O . HOH J 9 . ? 24.091 -3.229 28.558 1.00 59.02 ? 1204 HOH A O 1 HETATM 2042 O O . HOH J 9 . ? 11.370 16.117 22.345 1.00 34.72 ? 1205 HOH A O 1 HETATM 2043 O O . HOH J 9 . ? 19.869 16.141 7.928 1.00 41.41 ? 1206 HOH A O 1 HETATM 2044 O O . HOH J 9 . ? 10.357 -7.523 29.682 1.00 38.32 ? 1207 HOH A O 1 HETATM 2045 O O . HOH J 9 . ? 11.115 22.568 7.405 1.00 35.53 ? 1208 HOH A O 1 HETATM 2046 O O . HOH J 9 . ? 20.847 1.472 22.399 1.00 50.02 ? 1209 HOH A O 1 HETATM 2047 O O . HOH J 9 . ? 16.177 5.035 26.743 1.00 47.88 ? 1210 HOH A O 1 HETATM 2048 O O . HOH J 9 . ? 21.700 -15.948 10.964 1.00 43.66 ? 1211 HOH A O 1 HETATM 2049 O O . HOH J 9 . ? 3.481 17.150 24.672 1.00 51.40 ? 1212 HOH A O 1 HETATM 2050 O O . HOH J 9 . ? 5.094 -5.068 33.272 1.00 39.06 ? 1213 HOH A O 1 HETATM 2051 O O . HOH J 9 . ? 15.695 14.448 0.560 1.00 35.48 ? 1214 HOH A O 1 HETATM 2052 O O . HOH J 9 . ? 6.497 -20.279 -2.459 1.00 51.13 ? 1215 HOH A O 1 HETATM 2053 O O . HOH J 9 . ? 4.269 -15.379 13.437 1.00 42.04 ? 1216 HOH A O 1 HETATM 2054 O O . HOH J 9 . ? 21.251 7.518 -9.545 1.00 42.15 ? 1217 HOH A O 1 HETATM 2055 O O . HOH J 9 . ? 9.969 -12.653 -9.903 1.00 47.10 ? 1218 HOH A O 1 HETATM 2056 O O . HOH J 9 . ? 12.996 23.950 6.142 1.00 44.01 ? 1219 HOH A O 1 HETATM 2057 O O . HOH J 9 . ? -5.965 8.277 13.827 1.00 48.50 ? 1220 HOH A O 1 HETATM 2058 O O . HOH J 9 . ? 0.766 -15.216 5.278 1.00 47.93 ? 1221 HOH A O 1 HETATM 2059 O O . HOH J 9 . ? 26.753 -5.813 10.189 1.00 52.83 ? 1222 HOH A O 1 HETATM 2060 O O . HOH J 9 . ? 22.627 -0.190 9.910 1.00 44.62 ? 1223 HOH A O 1 HETATM 2061 O O . HOH J 9 . ? 11.877 -20.339 -2.221 1.00 22.06 ? 1224 HOH A O 1 HETATM 2062 O O . HOH J 9 . ? 21.944 15.882 15.426 1.00 47.12 ? 1225 HOH A O 1 HETATM 2063 O O . HOH J 9 . ? 3.628 -14.000 -6.732 1.00 38.85 ? 1226 HOH A O 1 HETATM 2064 O O . HOH J 9 . ? 5.471 -10.941 26.627 1.00 45.02 ? 1227 HOH A O 1 HETATM 2065 O O . HOH J 9 . ? 25.823 2.988 0.404 1.00 30.27 ? 1228 HOH A O 1 HETATM 2066 O O . HOH J 9 . ? 22.143 -14.586 3.703 1.00 39.18 ? 1229 HOH A O 1 HETATM 2067 O O . HOH J 9 . ? 15.113 16.308 -3.568 1.00 34.89 ? 1230 HOH A 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 VAL 1 16 16 VAL VAL A . n A 1 2 ILE 2 17 17 ILE ILE A . n A 1 3 GLY 3 18 18 GLY GLY A . n A 1 4 GLY 4 19 19 GLY GLY A . n A 1 5 ASP 5 20 20 ASP ASP A . n A 1 6 GLU 6 21 21 GLU GLU A . n A 1 7 CYS 7 22 22 CYS CYS A . n A 1 8 ASN 8 23 23 ASN ASN A . n A 1 9 ILE 9 24 24 ILE ILE A . n A 1 10 ASN 10 25 25 ASN ASN A . n A 1 11 GLU 11 26 26 GLU GLU A . n A 1 12 HIS 12 27 27 HIS HIS A . n A 1 13 ARG 13 28 28 ARG ARG A . n A 1 14 PHE 14 29 29 PHE PHE A . n A 1 15 LEU 15 30 30 LEU LEU A . n A 1 16 ALA 16 31 31 ALA ALA A . n A 1 17 LEU 17 32 32 LEU LEU A . n A 1 18 VAL 18 33 33 VAL VAL A . n A 1 19 TYR 19 34 34 TYR TYR A . n A 1 20 ALA 20 36 36 ALA ALA A . n A 1 21 ASN 21 38 38 ASN ASN A . n A 1 22 GLY 22 39 39 GLY GLY A . n A 1 23 SER 23 40 40 SER SER A . n A 1 24 LEU 24 41 41 LEU LEU A . n A 1 25 CYS 25 42 42 CYS CYS A . n A 1 26 GLY 26 43 43 GLY GLY A . n A 1 27 GLY 27 44 44 GLY GLY A . n A 1 28 THR 28 45 45 THR THR A . n A 1 29 LEU 29 46 46 LEU LEU A . n A 1 30 ILE 30 47 47 ILE ILE A . n A 1 31 ASN 31 48 48 ASN ASN A . n A 1 32 GLN 32 49 49 GLN GLN A . n A 1 33 GLU 33 50 50 GLU GLU A . n A 1 34 TRP 34 51 51 TRP TRP A . n A 1 35 VAL 35 52 52 VAL VAL A . n A 1 36 LEU 36 53 53 LEU LEU A . n A 1 37 THR 37 54 54 THR THR A . n A 1 38 ALA 38 55 55 ALA ALA A . n A 1 39 ARG 39 56 56 ARG ARG A . n A 1 40 HIS 40 57 57 HIS HIS A . n A 1 41 CYS 41 58 58 CYS CYS A . n A 1 42 ASP 42 59 59 ASP ASP A . n A 1 43 ARG 43 60 60 ARG ARG A . n A 1 44 GLY 44 62 62 GLY GLY A . n A 1 45 ASN 45 63 63 ASN ASN A . n A 1 46 MET 46 64 64 MET MET A . n A 1 47 ARG 47 65 65 ARG ARG A . n A 1 48 ILE 48 66 66 ILE ILE A . n A 1 49 TYR 49 67 67 TYR TYR A . n A 1 50 LEU 50 68 68 LEU LEU A . n A 1 51 GLY 51 69 69 GLY GLY A . n A 1 52 MET 52 70 70 MET MET A . n A 1 53 HIS 53 71 71 HIS HIS A . n A 1 54 ASN 54 72 72 ASN ASN A . n A 1 55 LEU 55 73 73 LEU LEU A . n A 1 56 LYS 56 74 74 LYS LYS A . n A 1 57 VAL 57 75 75 VAL VAL A . n A 1 58 LEU 58 76 76 LEU LEU A . n A 1 59 ASN 59 77 77 ASN ASN A . n A 1 60 LYS 60 78 78 LYS LYS A . n A 1 61 ASP 61 79 79 ASP ASP A . n A 1 62 ALA 62 80 80 ALA ALA A . n A 1 63 LEU 63 81 81 LEU LEU A . n A 1 64 ARG 64 82 82 ARG ARG A . n A 1 65 ARG 65 83 83 ARG ARG A . n A 1 66 PHE 66 84 84 PHE PHE A . n A 1 67 PRO 67 85 85 PRO PRO A . n A 1 68 LYS 68 86 86 LYS LYS A . n A 1 69 GLU 69 87 87 GLU GLU A . n A 1 70 LYS 70 88 88 LYS LYS A . n A 1 71 TYR 71 89 89 TYR TYR A . n A 1 72 PHE 72 90 90 PHE PHE A . n A 1 73 CYS 73 91 91 CYS CYS A . n A 1 74 LEU 74 92 92 LEU LEU A . n A 1 75 ASN 75 93 93 ASN ASN A . n A 1 76 THR 76 94 94 THR THR A . n A 1 77 ARG 77 95 95 ARG ARG A . n A 1 78 ASN 78 96 96 ASN ASN A A n A 1 79 ASP 79 96 96 ASP ASP A . n A 1 80 THR 80 97 97 THR THR A . n A 1 81 ILE 81 98 98 ILE ILE A . n A 1 82 TRP 82 99 99 TRP TRP A . n A 1 83 ASP 83 100 100 ASP ASP A . n A 1 84 LYS 84 101 101 LYS LYS A . n A 1 85 ASP 85 102 102 ASP ASP A . n A 1 86 ILE 86 103 103 ILE ILE A . n A 1 87 MET 87 104 104 MET MET A . n A 1 88 LEU 88 105 105 LEU LEU A . n A 1 89 ILE 89 106 106 ILE ILE A . n A 1 90 ARG 90 107 107 ARG ARG A . n A 1 91 LEU 91 108 108 LEU LEU A . n A 1 92 ASN 92 109 109 ASN ASN A . n A 1 93 ARG 93 110 110 ARG ARG A . n A 1 94 PRO 94 111 111 PRO PRO A . n A 1 95 VAL 95 112 112 VAL VAL A . n A 1 96 ARG 96 113 113 ARG ARG A . n A 1 97 ASN 97 114 114 ASN ASN A . n A 1 98 SER 98 115 115 SER SER A . n A 1 99 ALA 99 116 116 ALA ALA A . n A 1 100 HIS 100 117 117 HIS HIS A . n A 1 101 ILE 101 118 118 ILE ILE A . n A 1 102 ALA 102 119 119 ALA ALA A . n A 1 103 PRO 103 120 120 PRO PRO A . n A 1 104 LEU 104 121 121 LEU LEU A . n A 1 105 SER 105 122 122 SER SER A . n A 1 106 LEU 106 123 123 LEU LEU A . n A 1 107 PRO 107 124 124 PRO PRO A . n A 1 108 SER 108 125 125 SER SER A . n A 1 109 ASN 109 127 127 ASN ASN A . n A 1 110 PRO 110 128 128 PRO PRO A . n A 1 111 PRO 111 129 129 PRO PRO A . n A 1 112 SER 112 131 131 SER SER A . n A 1 113 VAL 113 132 132 VAL VAL A . n A 1 114 GLY 114 133 133 GLY GLY A . n A 1 115 SER 115 134 134 SER SER A . n A 1 116 VAL 116 135 135 VAL VAL A . n A 1 117 CYS 117 136 136 CYS CYS A . n A 1 118 ARG 118 137 137 ARG ARG A . n A 1 119 ILE 119 138 138 ILE ILE A . n A 1 120 MET 120 139 139 MET MET A . n A 1 121 GLY 121 140 140 GLY GLY A . n A 1 122 TRP 122 141 141 TRP TRP A . n A 1 123 GLY 123 142 142 GLY GLY A . n A 1 124 THR 124 143 143 THR THR A . n A 1 125 ILE 125 144 144 ILE ILE A . n A 1 126 THR 126 145 145 THR THR A . n A 1 127 SER 127 146 146 SER SER A . n A 1 128 PRO 128 147 147 PRO PRO A . n A 1 129 ASN 129 148 148 ASN ASN A . n A 1 130 ALA 130 149 149 ALA ALA A . n A 1 131 THR 131 150 150 THR THR A . n A 1 132 LEU 132 151 151 LEU LEU A . n A 1 133 PRO 133 152 152 PRO PRO A . n A 1 134 ASP 134 153 153 ASP ASP A . n A 1 135 VAL 135 154 154 VAL VAL A . n A 1 136 PRO 136 155 155 PRO PRO A . n A 1 137 HIS 137 156 156 HIS HIS A . n A 1 138 CYS 138 157 157 CYS CYS A . n A 1 139 ALA 139 158 158 ALA ALA A . n A 1 140 ASN 140 159 159 ASN ASN A . n A 1 141 ILE 141 160 160 ILE ILE A . n A 1 142 ASN 142 161 161 ASN ASN A . n A 1 143 ILE 143 162 162 ILE ILE A . n A 1 144 LEU 144 163 163 LEU LEU A . n A 1 145 ASP 145 164 164 ASP ASP A . n A 1 146 TYR 146 165 165 TYR TYR A . n A 1 147 ALA 147 166 166 ALA ALA A . n A 1 148 VAL 148 167 167 VAL VAL A . n A 1 149 CYS 149 168 168 CYS CYS A . n A 1 150 GLN 150 169 169 GLN GLN A . n A 1 151 ALA 151 170 170 ALA ALA A . n A 1 152 ALA 152 171 171 ALA ALA A . n A 1 153 TYR 153 172 172 TYR TYR A . n A 1 154 LYS 154 174 174 LYS LYS A . n A 1 155 GLY 155 175 175 GLY GLY A . n A 1 156 LEU 156 176 176 LEU LEU A . n A 1 157 ALA 157 177 177 ALA ALA A . n A 1 158 ALA 158 178 178 ALA ALA A . n A 1 159 THR 159 179 179 THR THR A . n A 1 160 THR 160 180 180 THR THR A . n A 1 161 LEU 161 181 181 LEU LEU A . n A 1 162 CYS 162 182 182 CYS CYS A . n A 1 163 ALA 163 183 183 ALA ALA A . n A 1 164 GLY 164 184 184 GLY GLY A . n A 1 165 ILE 165 185 185 ILE ILE A . n A 1 166 LEU 166 186 186 LEU LEU A . n A 1 167 GLU 167 186 186 GLU GLU A A n A 1 168 GLY 168 186 186 GLY GLY A B n A 1 169 GLY 169 187 187 GLY GLY A . n A 1 170 LYS 170 188 188 LYS LYS A . n A 1 171 ASP 171 189 189 ASP ASP A . n A 1 172 THR 172 190 190 THR THR A . n A 1 173 CYS 173 191 191 CYS CYS A . n A 1 174 LYS 174 192 192 LYS LYS A . n A 1 175 GLY 175 193 193 GLY GLY A . n A 1 176 ASP 176 194 194 ASP ASP A . n A 1 177 SER 177 195 195 SER SER A . n A 1 178 GLY 178 196 196 GLY GLY A . n A 1 179 GLY 179 197 197 GLY GLY A . n A 1 180 PRO 180 198 198 PRO PRO A . n A 1 181 LEU 181 199 199 LEU LEU A . n A 1 182 ILE 182 200 200 ILE ILE A . n A 1 183 CYS 183 201 201 CYS CYS A . n A 1 184 ASN 184 202 202 ASN ASN A . n A 1 185 GLY 185 207 207 GLY GLY A . n A 1 186 GLN 186 208 208 GLN GLN A . n A 1 187 PHE 187 209 209 PHE PHE A . n A 1 188 GLN 188 210 210 GLN GLN A . n A 1 189 GLY 189 211 211 GLY GLY A . n A 1 190 ILE 190 212 212 ILE ILE A . n A 1 191 LEU 191 213 213 LEU LEU A . n A 1 192 SER 192 214 214 SER SER A . n A 1 193 VAL 193 215 215 VAL VAL A . n A 1 194 GLY 194 216 216 GLY GLY A . n A 1 195 GLY 195 217 217 GLY GLY A . n A 1 196 ASN 196 218 218 ASN ASN A . n A 1 197 PRO 197 219 219 PRO PRO A . n A 1 198 CYS 198 220 220 CYS CYS A . n A 1 199 ALA 199 221 221 ALA ALA A . n A 1 200 GLN 200 221 221 GLN GLN A A n A 1 201 PRO 201 222 222 PRO PRO A . n A 1 202 ARG 202 223 223 ARG ARG A . n A 1 203 LYS 203 224 224 LYS LYS A . n A 1 204 PRO 204 225 225 PRO PRO A . n A 1 205 GLY 205 226 226 GLY GLY A . n A 1 206 ILE 206 227 227 ILE ILE A . n A 1 207 TYR 207 228 228 TYR TYR A . n A 1 208 THR 208 229 229 THR THR A . n A 1 209 LYS 209 230 230 LYS LYS A . n A 1 210 VAL 210 231 231 VAL VAL A . n A 1 211 PHE 211 232 232 PHE PHE A . n A 1 212 ASP 212 233 233 ASP ASP A . n A 1 213 TYR 213 234 234 TYR TYR A . n A 1 214 THR 214 235 235 THR THR A . n A 1 215 ASP 215 236 236 ASP ASP A . n A 1 216 TRP 216 237 237 TRP TRP A . n A 1 217 ILE 217 238 238 ILE ILE A . n A 1 218 GLN 218 239 239 GLN GLN A . n A 1 219 SER 219 240 240 SER SER A . n A 1 220 ILE 220 241 241 ILE ILE A . n A 1 221 ILE 221 242 242 ILE ILE A . n A 1 222 SER 222 243 243 SER SER A . n A 1 223 GLY 223 244 244 GLY GLY A . n A 1 224 ASN 224 245 245 ASN ASN A . n A 1 225 THR 225 245 245 THR THR A A n A 1 226 ASP 226 245 245 ASP ASP A B n A 1 227 ALA 227 245 245 ALA ALA A C n A 1 228 THR 228 245 245 THR THR A D n A 1 229 CYS 229 245 245 CYS CYS A E n A 1 230 PRO 230 245 245 PRO PRO A F n A 1 231 PRO 231 245 245 PRO PRO A G n # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code B 2 NAG 1 701 701 NAG NAG A . C 2 NAG 1 801 801 NAG NAG A . D 3 NDG 1 901 901 NDG NAG A . E 4 SO4 1 301 301 SO4 SO4 A . F 5 ACT 1 601 601 ACT ACT A . G 6 CL 1 1001 1001 CL CL A . H 7 BEN 1 401 401 BEN BDN A . I 8 GOL 1 501 501 GOL GOL A . J 9 HOH 1 1002 1 HOH HOH A . J 9 HOH 2 1003 2 HOH HOH A . J 9 HOH 3 1004 3 HOH HOH A . J 9 HOH 4 1005 4 HOH HOH A . J 9 HOH 5 1006 5 HOH HOH A . J 9 HOH 6 1007 6 HOH HOH A . J 9 HOH 7 1008 7 HOH HOH A . J 9 HOH 8 1009 8 HOH HOH A . J 9 HOH 9 1010 9 HOH HOH A . J 9 HOH 10 1011 10 HOH HOH A . J 9 HOH 11 1012 11 HOH HOH A . J 9 HOH 12 1013 12 HOH HOH A . J 9 HOH 13 1014 13 HOH HOH A . J 9 HOH 14 1015 14 HOH HOH A . J 9 HOH 15 1016 15 HOH HOH A . J 9 HOH 16 1017 16 HOH HOH A . J 9 HOH 17 1018 17 HOH HOH A . J 9 HOH 18 1019 18 HOH HOH A . J 9 HOH 19 1020 19 HOH HOH A . J 9 HOH 20 1021 20 HOH HOH A . J 9 HOH 21 1022 21 HOH HOH A . J 9 HOH 22 1023 22 HOH HOH A . J 9 HOH 23 1024 23 HOH HOH A . J 9 HOH 24 1025 24 HOH HOH A . J 9 HOH 25 1026 25 HOH HOH A . J 9 HOH 26 1027 26 HOH HOH A . J 9 HOH 27 1028 27 HOH HOH A . J 9 HOH 28 1029 28 HOH HOH A . J 9 HOH 29 1030 29 HOH HOH A . J 9 HOH 30 1031 30 HOH HOH A . J 9 HOH 31 1032 31 HOH HOH A . J 9 HOH 32 1033 32 HOH HOH A . J 9 HOH 33 1034 33 HOH HOH A . J 9 HOH 34 1035 34 HOH HOH A . J 9 HOH 35 1036 35 HOH HOH A . J 9 HOH 36 1037 36 HOH HOH A . J 9 HOH 37 1038 37 HOH HOH A . J 9 HOH 38 1039 38 HOH HOH A . J 9 HOH 39 1040 39 HOH HOH A . J 9 HOH 40 1041 40 HOH HOH A . J 9 HOH 41 1042 41 HOH HOH A . J 9 HOH 42 1043 42 HOH HOH A . J 9 HOH 43 1044 43 HOH HOH A . J 9 HOH 44 1045 44 HOH HOH A . J 9 HOH 45 1046 45 HOH HOH A . J 9 HOH 46 1047 46 HOH HOH A . J 9 HOH 47 1048 47 HOH HOH A . J 9 HOH 48 1049 48 HOH HOH A . J 9 HOH 49 1050 49 HOH HOH A . J 9 HOH 50 1051 50 HOH HOH A . J 9 HOH 51 1052 51 HOH HOH A . J 9 HOH 52 1053 52 HOH HOH A . J 9 HOH 53 1054 53 HOH HOH A . J 9 HOH 54 1055 54 HOH HOH A . J 9 HOH 55 1056 55 HOH HOH A . J 9 HOH 56 1057 56 HOH HOH A . J 9 HOH 57 1058 57 HOH HOH A . J 9 HOH 58 1059 58 HOH HOH A . J 9 HOH 59 1060 59 HOH HOH A . J 9 HOH 60 1061 60 HOH HOH A . J 9 HOH 61 1062 61 HOH HOH A . J 9 HOH 62 1063 62 HOH HOH A . J 9 HOH 63 1064 63 HOH HOH A . J 9 HOH 64 1065 64 HOH HOH A . J 9 HOH 65 1066 65 HOH HOH A . J 9 HOH 66 1067 66 HOH HOH A . J 9 HOH 67 1068 67 HOH HOH A . J 9 HOH 68 1069 68 HOH HOH A . J 9 HOH 69 1070 69 HOH HOH A . J 9 HOH 70 1071 70 HOH HOH A . J 9 HOH 71 1072 71 HOH HOH A . J 9 HOH 72 1073 72 HOH HOH A . J 9 HOH 73 1074 73 HOH HOH A . J 9 HOH 74 1075 74 HOH HOH A . J 9 HOH 75 1076 75 HOH HOH A . J 9 HOH 76 1077 76 HOH HOH A . J 9 HOH 77 1078 77 HOH HOH A . J 9 HOH 78 1079 78 HOH HOH A . J 9 HOH 79 1080 79 HOH HOH A . J 9 HOH 80 1081 80 HOH HOH A . J 9 HOH 81 1082 81 HOH HOH A . J 9 HOH 82 1083 82 HOH HOH A . J 9 HOH 83 1084 83 HOH HOH A . J 9 HOH 84 1085 84 HOH HOH A . J 9 HOH 85 1086 85 HOH HOH A . J 9 HOH 86 1087 86 HOH HOH A . J 9 HOH 87 1088 87 HOH HOH A . J 9 HOH 88 1089 88 HOH HOH A . J 9 HOH 89 1090 89 HOH HOH A . J 9 HOH 90 1091 90 HOH HOH A . J 9 HOH 91 1092 91 HOH HOH A . J 9 HOH 92 1093 92 HOH HOH A . J 9 HOH 93 1094 93 HOH HOH A . J 9 HOH 94 1095 94 HOH HOH A . J 9 HOH 95 1096 95 HOH HOH A . J 9 HOH 96 1097 96 HOH HOH A . J 9 HOH 97 1098 97 HOH HOH A . J 9 HOH 98 1099 98 HOH HOH A . J 9 HOH 99 1100 99 HOH HOH A . J 9 HOH 100 1101 100 HOH HOH A . J 9 HOH 101 1102 101 HOH HOH A . J 9 HOH 102 1103 102 HOH HOH A . J 9 HOH 103 1104 103 HOH HOH A . J 9 HOH 104 1105 104 HOH HOH A . J 9 HOH 105 1106 105 HOH HOH A . J 9 HOH 106 1107 106 HOH HOH A . J 9 HOH 107 1108 107 HOH HOH A . J 9 HOH 108 1109 108 HOH HOH A . J 9 HOH 109 1110 109 HOH HOH A . J 9 HOH 110 1111 110 HOH HOH A . J 9 HOH 111 1112 111 HOH HOH A . J 9 HOH 112 1113 112 HOH HOH A . J 9 HOH 113 1114 113 HOH HOH A . J 9 HOH 114 1115 114 HOH HOH A . J 9 HOH 115 1116 115 HOH HOH A . J 9 HOH 116 1117 116 HOH HOH A . J 9 HOH 117 1118 117 HOH HOH A . J 9 HOH 118 1119 118 HOH HOH A . J 9 HOH 119 1120 119 HOH HOH A . J 9 HOH 120 1121 120 HOH HOH A . J 9 HOH 121 1122 121 HOH HOH A . J 9 HOH 122 1123 122 HOH HOH A . J 9 HOH 123 1124 123 HOH HOH A . J 9 HOH 124 1125 124 HOH HOH A . J 9 HOH 125 1126 125 HOH HOH A . J 9 HOH 126 1127 126 HOH HOH A . J 9 HOH 127 1128 127 HOH HOH A . J 9 HOH 128 1129 128 HOH HOH A . J 9 HOH 129 1130 129 HOH HOH A . J 9 HOH 130 1131 130 HOH HOH A . J 9 HOH 131 1132 131 HOH HOH A . J 9 HOH 132 1133 132 HOH HOH A . J 9 HOH 133 1134 133 HOH HOH A . J 9 HOH 134 1135 134 HOH HOH A . J 9 HOH 135 1136 135 HOH HOH A . J 9 HOH 136 1137 136 HOH HOH A . J 9 HOH 137 1138 137 HOH HOH A . J 9 HOH 138 1139 138 HOH HOH A . J 9 HOH 139 1140 139 HOH HOH A . J 9 HOH 140 1141 140 HOH HOH A . J 9 HOH 141 1142 141 HOH HOH A . J 9 HOH 142 1143 142 HOH HOH A . J 9 HOH 143 1144 143 HOH HOH A . J 9 HOH 144 1145 144 HOH HOH A . J 9 HOH 145 1146 145 HOH HOH A . J 9 HOH 146 1147 146 HOH HOH A . J 9 HOH 147 1148 147 HOH HOH A . J 9 HOH 148 1149 148 HOH HOH A . J 9 HOH 149 1150 149 HOH HOH A . J 9 HOH 150 1151 150 HOH HOH A . J 9 HOH 151 1152 151 HOH HOH A . J 9 HOH 152 1153 152 HOH HOH A . J 9 HOH 153 1154 154 HOH HOH A . J 9 HOH 154 1155 155 HOH HOH A . J 9 HOH 155 1156 156 HOH HOH A . J 9 HOH 156 1157 157 HOH HOH A . J 9 HOH 157 1158 158 HOH HOH A . J 9 HOH 158 1159 159 HOH HOH A . J 9 HOH 159 1160 160 HOH HOH A . J 9 HOH 160 1161 161 HOH HOH A . J 9 HOH 161 1162 162 HOH HOH A . J 9 HOH 162 1163 163 HOH HOH A . J 9 HOH 163 1164 164 HOH HOH A . J 9 HOH 164 1165 165 HOH HOH A . J 9 HOH 165 1166 166 HOH HOH A . J 9 HOH 166 1167 167 HOH HOH A . J 9 HOH 167 1168 168 HOH HOH A . J 9 HOH 168 1169 169 HOH HOH A . J 9 HOH 169 1170 170 HOH HOH A . J 9 HOH 170 1171 171 HOH HOH A . J 9 HOH 171 1172 172 HOH HOH A . J 9 HOH 172 1173 173 HOH HOH A . J 9 HOH 173 1174 174 HOH HOH A . J 9 HOH 174 1175 175 HOH HOH A . J 9 HOH 175 1176 176 HOH HOH A . J 9 HOH 176 1177 177 HOH HOH A . J 9 HOH 177 1178 178 HOH HOH A . J 9 HOH 178 1179 179 HOH HOH A . J 9 HOH 179 1180 180 HOH HOH A . J 9 HOH 180 1181 181 HOH HOH A . J 9 HOH 181 1182 182 HOH HOH A . J 9 HOH 182 1183 183 HOH HOH A . J 9 HOH 183 1184 184 HOH HOH A . J 9 HOH 184 1185 185 HOH HOH A . J 9 HOH 185 1186 186 HOH HOH A . J 9 HOH 186 1187 187 HOH HOH A . J 9 HOH 187 1188 188 HOH HOH A . J 9 HOH 188 1189 189 HOH HOH A . J 9 HOH 189 1190 190 HOH HOH A . J 9 HOH 190 1191 191 HOH HOH A . J 9 HOH 191 1192 192 HOH HOH A . J 9 HOH 192 1193 193 HOH HOH A . J 9 HOH 193 1194 194 HOH HOH A . J 9 HOH 194 1195 195 HOH HOH A . J 9 HOH 195 1196 196 HOH HOH A . J 9 HOH 196 1197 197 HOH HOH A . J 9 HOH 197 1198 198 HOH HOH A . J 9 HOH 198 1199 199 HOH HOH A . J 9 HOH 199 1200 200 HOH HOH A . J 9 HOH 200 1201 201 HOH HOH A . J 9 HOH 201 1202 202 HOH HOH A . J 9 HOH 202 1203 203 HOH HOH A . J 9 HOH 203 1204 204 HOH HOH A . J 9 HOH 204 1205 205 HOH HOH A . J 9 HOH 205 1206 206 HOH HOH A . J 9 HOH 206 1207 207 HOH HOH A . J 9 HOH 207 1208 208 HOH HOH A . J 9 HOH 208 1209 209 HOH HOH A . J 9 HOH 209 1210 210 HOH HOH A . J 9 HOH 210 1211 211 HOH HOH A . J 9 HOH 211 1212 212 HOH HOH A . J 9 HOH 212 1213 213 HOH HOH A . J 9 HOH 213 1214 214 HOH HOH A . J 9 HOH 214 1215 215 HOH HOH A . J 9 HOH 215 1216 216 HOH HOH A . J 9 HOH 216 1217 217 HOH HOH A . J 9 HOH 217 1218 218 HOH HOH A . J 9 HOH 218 1219 219 HOH HOH A . J 9 HOH 219 1220 220 HOH HOH A . J 9 HOH 220 1221 221 HOH HOH A . J 9 HOH 221 1222 222 HOH HOH A . J 9 HOH 222 1223 223 HOH HOH A . J 9 HOH 223 1224 224 HOH HOH A . J 9 HOH 224 1225 225 HOH HOH A . J 9 HOH 225 1226 227 HOH HOH A . J 9 HOH 226 1227 228 HOH HOH A . J 9 HOH 227 1228 229 HOH HOH A . J 9 HOH 228 1229 230 HOH HOH A . J 9 HOH 229 1230 231 HOH HOH A . # loop_ _pdbx_struct_mod_residue.id _pdbx_struct_mod_residue.label_asym_id _pdbx_struct_mod_residue.label_comp_id _pdbx_struct_mod_residue.label_seq_id _pdbx_struct_mod_residue.auth_asym_id _pdbx_struct_mod_residue.auth_comp_id _pdbx_struct_mod_residue.auth_seq_id _pdbx_struct_mod_residue.PDB_ins_code _pdbx_struct_mod_residue.parent_comp_id _pdbx_struct_mod_residue.details 1 A ASN 21 A ASN 38 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 78 A ASN 96 A ASN 'GLYCOSYLATION SITE' 3 A ASN 129 A ASN 148 ? ASN 'GLYCOSYLATION SITE' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_defined_assembly _pdbx_struct_assembly.method_details ? _pdbx_struct_assembly.oligomeric_details monomeric _pdbx_struct_assembly.oligomeric_count 1 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I,J # _pdbx_struct_oper_list.id 1 _pdbx_struct_oper_list.type 'identity operation' _pdbx_struct_oper_list.name 1_555 _pdbx_struct_oper_list.symmetry_operation x,y,z _pdbx_struct_oper_list.matrix[1][1] 1.0000000000 _pdbx_struct_oper_list.matrix[1][2] 0.0000000000 _pdbx_struct_oper_list.matrix[1][3] 0.0000000000 _pdbx_struct_oper_list.vector[1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][2] 1.0000000000 _pdbx_struct_oper_list.matrix[2][3] 0.0000000000 _pdbx_struct_oper_list.vector[2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][1] 0.0000000000 _pdbx_struct_oper_list.matrix[3][2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][3] 1.0000000000 _pdbx_struct_oper_list.vector[3] 0.0000000000 # _pdbx_struct_special_symmetry.id 1 _pdbx_struct_special_symmetry.PDB_model_num 1 _pdbx_struct_special_symmetry.auth_asym_id A _pdbx_struct_special_symmetry.auth_comp_id HOH _pdbx_struct_special_symmetry.auth_seq_id 1189 _pdbx_struct_special_symmetry.PDB_ins_code ? _pdbx_struct_special_symmetry.label_asym_id J _pdbx_struct_special_symmetry.label_comp_id HOH _pdbx_struct_special_symmetry.label_seq_id . # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 2005-09-06 2 'Structure model' 1 1 2008-04-30 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' 'Non-polymer description' 3 3 'Structure model' 'Version format compliance' # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal REFMAC refinement 5.2.0005 ? 1 DENZO 'data reduction' . ? 2 SCALEPACK 'data scaling' . ? 3 AMoRE phasing . ? 4 # _pdbx_validate_rmsd_angle.id 1 _pdbx_validate_rmsd_angle.PDB_model_num 1 _pdbx_validate_rmsd_angle.auth_atom_id_1 CA _pdbx_validate_rmsd_angle.auth_asym_id_1 A _pdbx_validate_rmsd_angle.auth_comp_id_1 LEU _pdbx_validate_rmsd_angle.auth_seq_id_1 176 _pdbx_validate_rmsd_angle.PDB_ins_code_1 ? _pdbx_validate_rmsd_angle.label_alt_id_1 ? _pdbx_validate_rmsd_angle.auth_atom_id_2 CB _pdbx_validate_rmsd_angle.auth_asym_id_2 A _pdbx_validate_rmsd_angle.auth_comp_id_2 LEU _pdbx_validate_rmsd_angle.auth_seq_id_2 176 _pdbx_validate_rmsd_angle.PDB_ins_code_2 ? _pdbx_validate_rmsd_angle.label_alt_id_2 ? _pdbx_validate_rmsd_angle.auth_atom_id_3 CG _pdbx_validate_rmsd_angle.auth_asym_id_3 A _pdbx_validate_rmsd_angle.auth_comp_id_3 LEU _pdbx_validate_rmsd_angle.auth_seq_id_3 176 _pdbx_validate_rmsd_angle.PDB_ins_code_3 ? _pdbx_validate_rmsd_angle.label_alt_id_3 ? _pdbx_validate_rmsd_angle.angle_value 129.27 _pdbx_validate_rmsd_angle.angle_target_value 115.30 _pdbx_validate_rmsd_angle.angle_deviation 13.97 _pdbx_validate_rmsd_angle.angle_standard_deviation 2.30 _pdbx_validate_rmsd_angle.linker_flag N # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 HIS A 27 ? ? -140.59 44.90 2 1 ASN A 38 ? ? -35.03 105.27 3 1 ASN A 48 ? ? -161.23 -167.96 4 1 HIS A 71 ? ? -126.89 -85.08 5 1 ASN A 148 ? ? 75.10 111.09 6 1 ASN A 245 ? ? 30.06 101.21 7 1 THR A 245 A ? -62.06 -173.60 # _pdbx_validate_peptide_omega.id 1 _pdbx_validate_peptide_omega.PDB_model_num 1 _pdbx_validate_peptide_omega.auth_comp_id_1 ASN _pdbx_validate_peptide_omega.auth_asym_id_1 A _pdbx_validate_peptide_omega.auth_seq_id_1 245 _pdbx_validate_peptide_omega.PDB_ins_code_1 ? _pdbx_validate_peptide_omega.label_alt_id_1 ? _pdbx_validate_peptide_omega.auth_comp_id_2 THR _pdbx_validate_peptide_omega.auth_asym_id_2 A _pdbx_validate_peptide_omega.auth_seq_id_2 245 _pdbx_validate_peptide_omega.PDB_ins_code_2 A _pdbx_validate_peptide_omega.label_alt_id_2 ? _pdbx_validate_peptide_omega.omega 147.52 # _pdbx_validate_chiral.id 1 _pdbx_validate_chiral.PDB_model_num 1 _pdbx_validate_chiral.auth_atom_id C1 _pdbx_validate_chiral.label_alt_id ? _pdbx_validate_chiral.auth_asym_id A _pdbx_validate_chiral.auth_comp_id NAG _pdbx_validate_chiral.auth_seq_id 701 _pdbx_validate_chiral.PDB_ins_code ? _pdbx_validate_chiral.details PLANAR _pdbx_validate_chiral.omega . # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 N-ACETYL-D-GLUCOSAMINE NAG 3 '2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE' NDG 4 'SULFATE ION' SO4 5 'ACETATE ION' ACT 6 'CHLORIDE ION' CL 7 BENZAMIDINE BEN 8 GLYCEROL GOL 9 water HOH #