data_2AIP # _entry.id 2AIP # _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 2AIP RCSB RCSB033940 WWPDB D_1000033940 # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 2AIP _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 2AIP _cell.length_a 79.867 _cell.length_b 63.295 _cell.length_c 48.237 _cell.angle_alpha 90.00 _cell.angle_beta 99.80 _cell.angle_gamma 90.00 _cell.Z_PDB 4 _cell.pdbx_unique_axis ? # _symmetry.entry_id 2AIP _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 3 ? ? ? ? 5 non-polymer syn 'ACETATE ION' 59.044 1 ? ? ? ? 6 non-polymer syn GLYCEROL 92.094 1 ? ? ? ? 7 water nat water 18.015 183 ? ? ? ? # _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 2AIP _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 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 2AIP _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.15 _exptl_crystal.density_percent_sol 42.4 _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 2AIP _reflns.observed_criterion_sigma_F 2.5 _reflns.observed_criterion_sigma_I 2.5 _reflns.d_resolution_high 1.65 _reflns.d_resolution_low 19.03 _reflns.number_all ? _reflns.number_obs 28664 _reflns.percent_possible_obs 99.8 _reflns.pdbx_Rmerge_I_obs 0.09 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI ? _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 1.65 _reflns_shell.d_res_low 1.71 _reflns_shell.percent_possible_all 99.6 _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 2AIP _refine.ls_number_reflns_obs 27223 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F 2.5 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 19.03 _refine.ls_d_res_high 1.65 _refine.ls_percent_reflns_obs 99.49 _refine.ls_R_factor_obs 0.17086 _refine.ls_R_factor_all 0.1743 _refine.ls_R_factor_R_work 0.16949 _refine.ls_R_factor_R_free 0.19692 _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 1440 _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 0.954 _refine.B_iso_mean 21.121 _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 'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' _refine.pdbx_starting_model 'PDB entry 1BQY' _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 0.092 _refine.pdbx_overall_ESU_R_Free 0.090 _refine.overall_SU_ML 0.057 _refine.overall_SU_B 1.643 _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 183 _refine_hist.number_atoms_total 2007 _refine_hist.d_res_high 1.65 _refine_hist.d_res_low 19.03 # 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 0.011 0.022 ? 1878 'X-RAY DIFFRACTION' ? r_angle_refined_deg 1.493 1.996 ? 2561 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 6.219 5.000 ? 230 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg 36.602 24.156 ? 77 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg 12.548 15.000 ? 294 'X-RAY DIFFRACTION' ? r_dihedral_angle_4_deg 18.610 15.000 ? 12 'X-RAY DIFFRACTION' ? r_chiral_restr 0.097 0.200 ? 288 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.005 0.020 ? 1397 'X-RAY DIFFRACTION' ? r_nbd_refined 0.217 0.200 ? 1030 'X-RAY DIFFRACTION' ? r_nbtor_refined 0.323 0.200 ? 1320 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_refined 0.152 0.200 ? 232 'X-RAY DIFFRACTION' ? r_symmetry_vdw_refined 0.195 0.200 ? 69 'X-RAY DIFFRACTION' ? r_symmetry_hbond_refined 0.200 0.200 ? 25 'X-RAY DIFFRACTION' ? r_mcbond_it 0.802 1.500 ? 1168 'X-RAY DIFFRACTION' ? r_mcangle_it 1.393 2.000 ? 1862 'X-RAY DIFFRACTION' ? r_scbond_it 2.030 3.000 ? 779 'X-RAY DIFFRACTION' ? r_scangle_it 2.999 4.500 ? 699 'X-RAY DIFFRACTION' ? # _refine_ls_shell.pdbx_total_number_of_bins_used 20 _refine_ls_shell.d_res_high 1.65 _refine_ls_shell.d_res_low 1.687 _refine_ls_shell.number_reflns_R_work 1905 _refine_ls_shell.R_factor_R_work 0.225 _refine_ls_shell.percent_reflns_obs 94.00 _refine_ls_shell.R_factor_R_free 0.252 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 85 _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 2AIP _struct.title 'Crystal structure of native 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 2AIP _struct_keywords.pdbx_keywords HYDROLASE _struct_keywords.text 'Protein C activator, snake venom, trypsin-like enzyme, 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 4 ? G N N 4 ? H N N 5 ? I N N 6 ? J N N 7 ? # _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 ? ? ? ? ? ? ? 2.052 ? disulf2 disulf ? ? A CYS 25 SG ? ? ? 1_555 A CYS 41 SG ? ? A CYS 42 A CYS 58 1_555 ? ? ? ? ? ? ? 2.039 ? disulf3 disulf ? ? A CYS 73 SG ? ? ? 1_555 A CYS 229 SG ? E A CYS 91 A CYS 245 1_555 ? ? ? ? ? ? ? 2.010 ? disulf4 disulf ? ? A CYS 117 SG ? ? ? 1_555 A CYS 183 SG ? ? A CYS 136 A CYS 201 1_555 ? ? ? ? ? ? ? 2.062 ? disulf5 disulf ? ? A CYS 149 SG ? ? ? 1_555 A CYS 162 SG ? ? A CYS 168 A CYS 182 1_555 ? ? ? ? ? ? ? 2.066 ? disulf6 disulf ? ? A CYS 173 SG ? ? ? 1_555 A CYS 198 SG ? ? A CYS 191 A CYS 220 1_555 ? ? ? ? ? ? ? 2.037 ? covale1 covale ? ? A ASN 21 ND2 ? ? ? 1_555 D NDG . C1 ? ? A ASN 38 A NDG 801 1_555 ? ? ? ? ? ? ? 1.439 ? covale2 covale ? ? A ASN 78 ND2 ? A ? 1_555 C NAG . C1 ? ? A ASN 96 A NAG 701 1_555 ? ? ? ? ? ? ? 1.438 ? covale3 covale ? ? A ASN 129 ND2 ? ? ? 1_555 B NAG . C1 ? ? A ASN 148 A NAG 601 1_555 ? ? ? ? ? ? ? 1.442 ? # 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 0.23 2 ASN 196 A . ? ASN 218 A PRO 197 A ? PRO 219 A 1 1.41 # 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 ? ASN A 31 ? SER A 40 ASN A 48 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 ? PHE A 72 ? PRO A 85 PHE A 90 # 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 ? ? ? ? 2 'BINDING SITE FOR RESIDUE NAG A 601' AC2 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NAG A 701' AC3 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NDG A 801' AC4 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE SO4 A 301' AC5 Software ? ? ? ? 9 'BINDING SITE FOR RESIDUE SO4 A 302' AC6 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE SO4 A 303' AC7 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE ACT A 501' AC8 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE GOL A 401' # 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 2 PRO A 128 ? PRO A 147 . ? 1_555 ? 2 AC1 2 ASN A 129 ? ASN A 148 . ? 1_555 ? 3 AC2 2 ASN A 78 A ASN A 96 . ? 1_555 ? 4 AC2 2 GOL I . ? GOL A 401 . ? 1_555 ? 5 AC3 2 ASN A 21 ? ASN A 38 . ? 1_555 ? 6 AC3 2 ARG A 43 ? ARG A 60 . ? 1_555 ? 7 AC4 8 HIS A 40 ? HIS A 57 . ? 1_555 ? 8 AC4 8 ARG A 43 ? ARG A 60 . ? 1_555 ? 9 AC4 8 LYS A 174 ? LYS A 192 . ? 1_555 ? 10 AC4 8 GLY A 175 ? GLY A 193 . ? 1_555 ? 11 AC4 8 SER A 177 ? SER A 195 . ? 1_555 ? 12 AC4 8 HOH J . ? HOH A 846 . ? 1_555 ? 13 AC4 8 HOH J . ? HOH A 921 . ? 1_555 ? 14 AC4 8 HOH J . ? HOH A 976 . ? 1_555 ? 15 AC5 9 ASN A 109 ? ASN A 127 . ? 1_555 ? 16 AC5 9 PRO A 111 ? PRO A 129 . ? 1_555 ? 17 AC5 9 SER A 112 ? SER A 131 . ? 1_555 ? 18 AC5 9 SER A 115 ? SER A 134 . ? 1_555 ? 19 AC5 9 ASN A 184 ? ASN A 202 . ? 1_555 ? 20 AC5 9 GLN A 186 ? GLN A 208 . ? 1_555 ? 21 AC5 9 ARG A 202 ? ARG A 223 . ? 2_556 ? 22 AC5 9 HOH J . ? HOH A 870 . ? 2_555 ? 23 AC5 9 HOH J . ? HOH A 971 . ? 1_555 ? 24 AC6 8 ARG A 64 ? ARG A 82 . ? 4_555 ? 25 AC6 8 CYS A 73 ? CYS A 91 . ? 1_555 ? 26 AC6 8 LEU A 74 ? LEU A 92 . ? 1_555 ? 27 AC6 8 ASN A 75 ? ASN A 93 . ? 1_555 ? 28 AC6 8 THR A 228 D THR A 245 . ? 1_555 ? 29 AC6 8 CYS A 229 E CYS A 245 . ? 1_555 ? 30 AC6 8 HOH J . ? HOH A 860 . ? 1_555 ? 31 AC6 8 HOH J . ? HOH A 984 . ? 1_555 ? 32 AC7 3 LEU A 63 ? LEU A 81 . ? 1_555 ? 33 AC7 3 ARG A 65 ? ARG A 83 . ? 1_555 ? 34 AC7 3 ARG A 93 ? ARG A 110 . ? 1_555 ? 35 AC8 5 ARG A 39 ? ARG A 56 . ? 1_555 ? 36 AC8 5 THR A 80 ? THR A 97 . ? 1_555 ? 37 AC8 5 TRP A 82 ? TRP A 99 . ? 1_555 ? 38 AC8 5 NAG C . ? NAG A 701 . ? 1_555 ? 39 AC8 5 HOH J . ? HOH A 834 . ? 1_555 ? # _database_PDB_matrix.entry_id 2AIP _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 2AIP _atom_sites.fract_transf_matrix[1][1] 0.012521 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.002162 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.015799 _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] 0.021038 _atom_sites.fract_transf_vector[1] 0.00000 _atom_sites.fract_transf_vector[2] 0.00000 _atom_sites.fract_transf_vector[3] 0.00000 # loop_ _atom_type.symbol C N O S # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 N N . VAL A 1 1 ? 13.470 -8.569 17.480 1.00 14.95 ? 16 VAL A N 1 ATOM 2 C CA . VAL A 1 1 ? 12.116 -8.530 18.113 1.00 15.31 ? 16 VAL A CA 1 ATOM 3 C C . VAL A 1 1 ? 12.128 -9.418 19.346 1.00 15.96 ? 16 VAL A C 1 ATOM 4 O O . VAL A 1 1 ? 12.513 -10.572 19.261 1.00 15.92 ? 16 VAL A O 1 ATOM 5 C CB . VAL A 1 1 ? 11.013 -8.996 17.131 1.00 15.87 ? 16 VAL A CB 1 ATOM 6 C CG1 . VAL A 1 1 ? 9.679 -9.152 17.839 1.00 14.96 ? 16 VAL A CG1 1 ATOM 7 C CG2 . VAL A 1 1 ? 10.909 -8.006 15.998 1.00 14.39 ? 16 VAL A CG2 1 ATOM 8 N N . ILE A 1 2 ? 11.719 -8.847 20.479 1.00 16.10 ? 17 ILE A N 1 ATOM 9 C CA . ILE A 1 2 ? 11.613 -9.564 21.746 1.00 17.55 ? 17 ILE A CA 1 ATOM 10 C C . ILE A 1 2 ? 10.170 -9.987 21.957 1.00 17.06 ? 17 ILE A C 1 ATOM 11 O O . ILE A 1 2 ? 9.241 -9.212 21.692 1.00 17.92 ? 17 ILE A O 1 ATOM 12 C CB . ILE A 1 2 ? 11.961 -8.649 22.954 1.00 17.04 ? 17 ILE A CB 1 ATOM 13 C CG1 . ILE A 1 2 ? 13.255 -7.849 22.720 1.00 18.25 ? 17 ILE A CG1 1 ATOM 14 C CG2 . ILE A 1 2 ? 11.990 -9.461 24.263 1.00 18.71 ? 17 ILE A CG2 1 ATOM 15 C CD1 . ILE A 1 2 ? 14.498 -8.692 22.586 1.00 19.77 ? 17 ILE A CD1 1 ATOM 16 N N . GLY A 1 3 ? 9.972 -11.210 22.437 1.00 18.06 ? 18 GLY A N 1 ATOM 17 C CA . GLY A 1 3 ? 8.645 -11.657 22.829 1.00 18.18 ? 18 GLY A CA 1 ATOM 18 C C . GLY A 1 3 ? 7.731 -12.074 21.704 1.00 19.07 ? 18 GLY A C 1 ATOM 19 O O . GLY A 1 3 ? 6.529 -12.238 21.917 1.00 19.46 ? 18 GLY A O 1 ATOM 20 N N . GLY A 1 4 ? 8.304 -12.274 20.521 1.00 19.34 ? 19 GLY A N 1 ATOM 21 C CA . GLY A 1 4 ? 7.541 -12.672 19.354 1.00 20.14 ? 19 GLY A CA 1 ATOM 22 C C . GLY A 1 4 ? 7.830 -14.111 18.966 1.00 20.96 ? 19 GLY A C 1 ATOM 23 O O . GLY A 1 4 ? 8.351 -14.913 19.764 1.00 20.58 ? 19 GLY A O 1 ATOM 24 N N . ASP A 1 5 ? 7.492 -14.435 17.730 1.00 21.49 ? 20 ASP A N 1 ATOM 25 C CA . ASP A 1 5 ? 7.822 -15.738 17.178 1.00 22.18 ? 20 ASP A CA 1 ATOM 26 C C . ASP A 1 5 ? 8.280 -15.570 15.747 1.00 21.34 ? 20 ASP A C 1 ATOM 27 O O . ASP A 1 5 ? 8.171 -14.483 15.190 1.00 20.82 ? 20 ASP A O 1 ATOM 28 C CB A ASP A 1 5 ? 6.674 -16.745 17.378 0.50 22.81 ? 20 ASP A CB 1 ATOM 29 C CB B ASP A 1 5 ? 6.569 -16.619 17.102 0.50 22.53 ? 20 ASP A CB 1 ATOM 30 C CG A ASP A 1 5 ? 6.495 -17.167 18.860 0.60 25.19 ? 20 ASP A CG 1 ATOM 31 C CG B ASP A 1 5 ? 5.359 -15.926 16.461 0.40 24.01 ? 20 ASP A CG 1 ATOM 32 O OD1 A ASP A 1 5 ? 7.423 -17.785 19.449 0.60 28.43 ? 20 ASP A OD1 1 ATOM 33 O OD1 B ASP A 1 5 ? 4.306 -16.590 16.351 0.40 27.06 ? 20 ASP A OD1 1 ATOM 34 O OD2 A ASP A 1 5 ? 5.415 -16.874 19.416 0.60 28.58 ? 20 ASP A OD2 1 ATOM 35 O OD2 B ASP A 1 5 ? 5.426 -14.739 16.070 0.40 27.47 ? 20 ASP A OD2 1 ATOM 36 N N . GLU A 1 6 ? 8.777 -16.641 15.150 1.00 20.40 ? 21 GLU A N 1 ATOM 37 C CA . GLU A 1 6 ? 9.082 -16.595 13.744 1.00 20.17 ? 21 GLU A CA 1 ATOM 38 C C . GLU A 1 6 ? 7.870 -16.076 12.960 1.00 19.22 ? 21 GLU A C 1 ATOM 39 O O . GLU A 1 6 ? 6.737 -16.547 13.143 1.00 19.42 ? 21 GLU A O 1 ATOM 40 C CB . GLU A 1 6 ? 9.477 -17.969 13.236 1.00 20.40 ? 21 GLU A CB 1 ATOM 41 C CG . GLU A 1 6 ? 9.602 -18.022 11.736 1.00 21.23 ? 21 GLU A CG 1 ATOM 42 C CD . GLU A 1 6 ? 10.085 -19.365 11.240 1.00 24.56 ? 21 GLU A CD 1 ATOM 43 O OE1 . GLU A 1 6 ? 10.346 -20.252 12.089 1.00 24.70 ? 21 GLU A OE1 1 ATOM 44 O OE2 . GLU A 1 6 ? 10.202 -19.522 10.013 1.00 21.79 ? 21 GLU A OE2 1 ATOM 45 N N . CYS A 1 7 ? 8.120 -15.101 12.092 1.00 19.02 ? 22 CYS A N 1 ATOM 46 C CA . CYS A 1 7 ? 7.087 -14.587 11.203 1.00 18.28 ? 22 CYS A CA 1 ATOM 47 C C . CYS A 1 7 ? 6.593 -15.685 10.297 1.00 19.06 ? 22 CYS A C 1 ATOM 48 O O . CYS A 1 7 ? 7.338 -16.588 9.959 1.00 19.61 ? 22 CYS A O 1 ATOM 49 C CB . CYS A 1 7 ? 7.658 -13.495 10.312 1.00 18.04 ? 22 CYS A CB 1 ATOM 50 S SG . CYS A 1 7 ? 8.269 -12.095 11.231 1.00 17.22 ? 22 CYS A SG 1 ATOM 51 N N . ASN A 1 8 ? 5.350 -15.580 9.855 1.00 19.29 ? 23 ASN A N 1 ATOM 52 C CA . ASN A 1 8 ? 4.909 -16.444 8.782 1.00 19.54 ? 23 ASN A CA 1 ATOM 53 C C . ASN A 1 8 ? 5.721 -16.096 7.540 1.00 19.41 ? 23 ASN A C 1 ATOM 54 O O . ASN A 1 8 ? 5.943 -14.924 7.226 1.00 18.76 ? 23 ASN A O 1 ATOM 55 C CB . ASN A 1 8 ? 3.413 -16.284 8.534 1.00 20.25 ? 23 ASN A CB 1 ATOM 56 C CG . ASN A 1 8 ? 2.905 -17.155 7.402 1.00 22.03 ? 23 ASN A CG 1 ATOM 57 O OD1 . ASN A 1 8 ? 3.073 -16.838 6.229 1.00 23.92 ? 23 ASN A OD1 1 ATOM 58 N ND2 . ASN A 1 8 ? 2.240 -18.252 7.755 1.00 26.37 ? 23 ASN A ND2 1 ATOM 59 N N . ILE A 1 9 ? 6.188 -17.127 6.844 1.00 18.33 ? 24 ILE A N 1 ATOM 60 C CA . ILE A 1 9 ? 7.022 -16.920 5.666 1.00 18.19 ? 24 ILE A CA 1 ATOM 61 C C . ILE A 1 9 ? 6.379 -16.025 4.594 1.00 17.84 ? 24 ILE A C 1 ATOM 62 O O . ILE A 1 9 ? 7.076 -15.467 3.748 1.00 17.51 ? 24 ILE A O 1 ATOM 63 C CB . ILE A 1 9 ? 7.470 -18.271 5.059 1.00 18.73 ? 24 ILE A CB 1 ATOM 64 C CG1 . ILE A 1 9 ? 8.628 -18.054 4.081 1.00 18.46 ? 24 ILE A CG1 1 ATOM 65 C CG2 . ILE A 1 9 ? 6.269 -19.010 4.431 1.00 18.23 ? 24 ILE A CG2 1 ATOM 66 C CD1 . ILE A 1 9 ? 9.532 -19.250 3.975 1.00 18.26 ? 24 ILE A CD1 1 ATOM 67 N N . ASN A 1 10 ? 5.058 -15.887 4.636 1.00 17.40 ? 25 ASN A N 1 ATOM 68 C CA . ASN A 1 10 ? 4.341 -15.128 3.611 1.00 18.11 ? 25 ASN A CA 1 ATOM 69 C C . ASN A 1 10 ? 3.821 -13.783 4.096 1.00 17.78 ? 25 ASN A C 1 ATOM 70 O O . ASN A 1 10 ? 3.203 -13.058 3.319 1.00 18.31 ? 25 ASN A O 1 ATOM 71 C CB . ASN A 1 10 ? 3.155 -15.948 3.093 1.00 19.09 ? 25 ASN A CB 1 ATOM 72 C CG . ASN A 1 10 ? 3.592 -17.248 2.459 1.00 20.24 ? 25 ASN A CG 1 ATOM 73 O OD1 . ASN A 1 10 ? 4.457 -17.267 1.590 1.00 23.78 ? 25 ASN A OD1 1 ATOM 74 N ND2 . ASN A 1 10 ? 3.025 -18.348 2.926 1.00 24.33 ? 25 ASN A ND2 1 ATOM 75 N N . GLU A 1 11 ? 4.079 -13.443 5.354 1.00 17.48 ? 26 GLU A N 1 ATOM 76 C CA . GLU A 1 11 ? 3.426 -12.261 5.921 1.00 16.98 ? 26 GLU A CA 1 ATOM 77 C C . GLU A 1 11 ? 4.277 -11.006 5.830 1.00 16.62 ? 26 GLU A C 1 ATOM 78 O O . GLU A 1 11 ? 3.869 -9.953 6.316 1.00 17.14 ? 26 GLU A O 1 ATOM 79 C CB . GLU A 1 11 ? 2.997 -12.493 7.370 1.00 18.02 ? 26 GLU A CB 1 ATOM 80 C CG . GLU A 1 11 ? 4.148 -12.405 8.381 1.00 19.29 ? 26 GLU A CG 1 ATOM 81 C CD . GLU A 1 11 ? 3.641 -12.308 9.801 1.00 23.26 ? 26 GLU A CD 1 ATOM 82 O OE1 . GLU A 1 11 ? 3.036 -11.261 10.152 1.00 23.34 ? 26 GLU A OE1 1 ATOM 83 O OE2 . GLU A 1 11 ? 3.853 -13.275 10.549 1.00 20.76 ? 26 GLU A OE2 1 ATOM 84 N N . HIS A 1 12 ? 5.438 -11.108 5.191 1.00 15.14 ? 27 HIS A N 1 ATOM 85 C CA . HIS A 1 12 ? 6.392 -10.003 5.209 1.00 14.20 ? 27 HIS A CA 1 ATOM 86 C C . HIS A 1 12 ? 7.034 -9.778 3.844 1.00 13.96 ? 27 HIS A C 1 ATOM 87 O O . HIS A 1 12 ? 8.234 -9.527 3.745 1.00 13.57 ? 27 HIS A O 1 ATOM 88 C CB . HIS A 1 12 ? 7.422 -10.185 6.339 1.00 14.38 ? 27 HIS A CB 1 ATOM 89 C CG . HIS A 1 12 ? 8.241 -11.432 6.229 1.00 13.77 ? 27 HIS A CG 1 ATOM 90 N ND1 . HIS A 1 12 ? 9.353 -11.509 5.417 1.00 14.61 ? 27 HIS A ND1 1 ATOM 91 C CD2 . HIS A 1 12 ? 8.113 -12.649 6.813 1.00 14.44 ? 27 HIS A CD2 1 ATOM 92 C CE1 . HIS A 1 12 ? 9.880 -12.721 5.505 1.00 12.87 ? 27 HIS A CE1 1 ATOM 93 N NE2 . HIS A 1 12 ? 9.151 -13.431 6.351 1.00 14.57 ? 27 HIS A NE2 1 ATOM 94 N N . ARG A 1 13 ? 6.209 -9.838 2.794 1.00 13.51 ? 28 ARG A N 1 ATOM 95 C CA . ARG A 1 13 ? 6.727 -9.753 1.438 1.00 12.95 ? 28 ARG A CA 1 ATOM 96 C C . ARG A 1 13 ? 7.394 -8.419 1.120 1.00 13.28 ? 28 ARG A C 1 ATOM 97 O O . ARG A 1 13 ? 8.184 -8.334 0.191 1.00 13.18 ? 28 ARG A O 1 ATOM 98 C CB . ARG A 1 13 ? 5.662 -10.109 0.416 1.00 13.98 ? 28 ARG A CB 1 ATOM 99 C CG . ARG A 1 13 ? 5.254 -11.582 0.557 1.00 15.41 ? 28 ARG A CG 1 ATOM 100 C CD . ARG A 1 13 ? 3.952 -11.795 -0.175 1.00 20.20 ? 28 ARG A CD 1 ATOM 101 N NE . ARG A 1 13 ? 4.154 -11.833 -1.608 1.00 21.48 ? 28 ARG A NE 1 ATOM 102 C CZ . ARG A 1 13 ? 3.303 -11.345 -2.516 1.00 20.92 ? 28 ARG A CZ 1 ATOM 103 N NH1 . ARG A 1 13 ? 3.588 -11.456 -3.804 1.00 19.69 ? 28 ARG A NH1 1 ATOM 104 N NH2 . ARG A 1 13 ? 2.187 -10.711 -2.146 1.00 24.00 ? 28 ARG A NH2 1 ATOM 105 N N . PHE A 1 14 ? 7.080 -7.395 1.913 1.00 13.08 ? 29 PHE A N 1 ATOM 106 C CA . PHE A 1 14 ? 7.581 -6.033 1.739 1.00 12.73 ? 29 PHE A CA 1 ATOM 107 C C . PHE A 1 14 ? 8.802 -5.824 2.630 1.00 13.20 ? 29 PHE A C 1 ATOM 108 O O . PHE A 1 14 ? 9.427 -4.756 2.602 1.00 13.47 ? 29 PHE A O 1 ATOM 109 C CB . PHE A 1 14 ? 6.486 -5.060 2.205 1.00 12.51 ? 29 PHE A CB 1 ATOM 110 C CG . PHE A 1 14 ? 5.864 -5.495 3.497 1.00 12.69 ? 29 PHE A CG 1 ATOM 111 C CD1 . PHE A 1 14 ? 6.509 -5.233 4.703 1.00 12.82 ? 29 PHE A CD1 1 ATOM 112 C CD2 . PHE A 1 14 ? 4.692 -6.226 3.511 1.00 13.79 ? 29 PHE A CD2 1 ATOM 113 C CE1 . PHE A 1 14 ? 5.984 -5.669 5.912 1.00 14.43 ? 29 PHE A CE1 1 ATOM 114 C CE2 . PHE A 1 14 ? 4.156 -6.692 4.739 1.00 14.81 ? 29 PHE A CE2 1 ATOM 115 C CZ . PHE A 1 14 ? 4.809 -6.417 5.933 1.00 13.33 ? 29 PHE A CZ 1 ATOM 116 N N . LEU A 1 15 ? 9.150 -6.820 3.446 1.00 12.41 ? 30 LEU A N 1 ATOM 117 C CA . LEU A 1 15 ? 10.197 -6.570 4.430 1.00 11.74 ? 30 LEU A CA 1 ATOM 118 C C . LEU A 1 15 ? 11.556 -6.750 3.772 1.00 12.57 ? 30 LEU A C 1 ATOM 119 O O . LEU A 1 15 ? 11.841 -7.799 3.144 1.00 11.93 ? 30 LEU A O 1 ATOM 120 C CB . LEU A 1 15 ? 10.032 -7.502 5.631 1.00 11.87 ? 30 LEU A CB 1 ATOM 121 C CG . LEU A 1 15 ? 11.156 -7.485 6.669 1.00 11.22 ? 30 LEU A CG 1 ATOM 122 C CD1 . LEU A 1 15 ? 11.191 -6.159 7.426 1.00 13.66 ? 30 LEU A CD1 1 ATOM 123 C CD2 . LEU A 1 15 ? 10.951 -8.662 7.611 1.00 13.33 ? 30 LEU A CD2 1 ATOM 124 N N . ALA A 1 16 ? 12.375 -5.713 3.883 1.00 12.44 ? 31 ALA A N 1 ATOM 125 C CA . ALA A 1 16 ? 13.725 -5.726 3.337 1.00 13.20 ? 31 ALA A CA 1 ATOM 126 C C . ALA A 1 16 ? 14.699 -5.972 4.479 1.00 13.94 ? 31 ALA A C 1 ATOM 127 O O . ALA A 1 16 ? 14.462 -5.534 5.592 1.00 13.88 ? 31 ALA A O 1 ATOM 128 C CB . ALA A 1 16 ? 14.036 -4.389 2.698 1.00 13.24 ? 31 ALA A CB 1 ATOM 129 N N . LEU A 1 17 ? 15.776 -6.684 4.170 1.00 14.58 ? 32 LEU A N 1 ATOM 130 C CA . LEU A 1 17 ? 16.892 -6.906 5.076 1.00 16.00 ? 32 LEU A CA 1 ATOM 131 C C . LEU A 1 17 ? 17.982 -5.963 4.609 1.00 16.71 ? 32 LEU A C 1 ATOM 132 O O . LEU A 1 17 ? 18.398 -5.984 3.448 1.00 16.40 ? 32 LEU A O 1 ATOM 133 C CB . LEU A 1 17 ? 17.348 -8.363 4.978 1.00 16.16 ? 32 LEU A CB 1 ATOM 134 C CG . LEU A 1 17 ? 18.647 -8.810 5.649 1.00 19.53 ? 32 LEU A CG 1 ATOM 135 C CD1 . LEU A 1 17 ? 18.482 -8.910 7.123 1.00 21.05 ? 32 LEU A CD1 1 ATOM 136 C CD2 . LEU A 1 17 ? 19.011 -10.175 5.068 1.00 21.11 ? 32 LEU A CD2 1 ATOM 137 N N . VAL A 1 18 ? 18.424 -5.107 5.513 1.00 17.82 ? 33 VAL A N 1 ATOM 138 C CA . VAL A 1 18 ? 19.374 -4.068 5.160 1.00 19.10 ? 33 VAL A CA 1 ATOM 139 C C . VAL A 1 18 ? 20.658 -4.344 5.936 1.00 20.54 ? 33 VAL A C 1 ATOM 140 O O . VAL A 1 18 ? 20.639 -4.447 7.157 1.00 21.66 ? 33 VAL A O 1 ATOM 141 C CB . VAL A 1 18 ? 18.795 -2.680 5.443 1.00 18.69 ? 33 VAL A CB 1 ATOM 142 C CG1 . VAL A 1 18 ? 19.842 -1.595 5.224 1.00 19.58 ? 33 VAL A CG1 1 ATOM 143 C CG2 . VAL A 1 18 ? 17.598 -2.420 4.561 1.00 19.58 ? 33 VAL A CG2 1 ATOM 144 N N . TYR A 1 19 ? 21.758 -4.536 5.219 1.00 21.41 ? 34 TYR A N 1 ATOM 145 C CA . TYR A 1 19 ? 23.052 -4.753 5.864 1.00 22.98 ? 34 TYR A CA 1 ATOM 146 C C . TYR A 1 19 ? 23.955 -3.617 5.460 1.00 23.24 ? 34 TYR A C 1 ATOM 147 O O . TYR A 1 19 ? 24.116 -3.360 4.275 1.00 23.69 ? 34 TYR A O 1 ATOM 148 C CB . TYR A 1 19 ? 23.708 -6.060 5.416 1.00 24.97 ? 34 TYR A CB 1 ATOM 149 C CG . TYR A 1 19 ? 23.276 -7.296 6.143 1.00 27.91 ? 34 TYR A CG 1 ATOM 150 C CD1 . TYR A 1 19 ? 23.316 -7.369 7.539 1.00 29.49 ? 34 TYR A CD1 1 ATOM 151 C CD2 . TYR A 1 19 ? 22.866 -8.417 5.429 1.00 30.76 ? 34 TYR A CD2 1 ATOM 152 C CE1 . TYR A 1 19 ? 22.918 -8.531 8.200 1.00 29.73 ? 34 TYR A CE1 1 ATOM 153 C CE2 . TYR A 1 19 ? 22.476 -9.581 6.075 1.00 31.11 ? 34 TYR A CE2 1 ATOM 154 C CZ . TYR A 1 19 ? 22.500 -9.634 7.456 1.00 30.44 ? 34 TYR A CZ 1 ATOM 155 O OH . TYR A 1 19 ? 22.114 -10.805 8.078 1.00 30.34 ? 34 TYR A OH 1 ATOM 156 N N . ALA A 1 20 ? 24.539 -2.931 6.430 1.00 23.46 ? 36 ALA A N 1 ATOM 157 C CA . ALA A 1 20 ? 25.444 -1.839 6.120 1.00 24.19 ? 36 ALA A CA 1 ATOM 158 C C . ALA A 1 20 ? 26.565 -1.888 7.132 1.00 24.86 ? 36 ALA A C 1 ATOM 159 O O . ALA A 1 20 ? 26.304 -1.808 8.325 1.00 25.67 ? 36 ALA A O 1 ATOM 160 C CB . ALA A 1 20 ? 24.719 -0.510 6.198 1.00 23.92 ? 36 ALA A CB 1 ATOM 161 N N . ASN A 1 21 ? 27.802 -2.048 6.660 0.70 25.78 ? 38 ASN A N 1 ATOM 162 C CA . ASN A 1 21 ? 28.970 -2.046 7.549 0.70 26.24 ? 38 ASN A CA 1 ATOM 163 C C . ASN A 1 21 ? 28.795 -3.047 8.698 0.70 26.36 ? 38 ASN A C 1 ATOM 164 O O . ASN A 1 21 ? 29.015 -2.724 9.872 0.70 26.56 ? 38 ASN A O 1 ATOM 165 C CB . ASN A 1 21 ? 29.205 -0.623 8.070 0.50 26.81 ? 38 ASN A CB 1 ATOM 166 C CG . ASN A 1 21 ? 30.477 -0.489 8.888 0.50 28.21 ? 38 ASN A CG 1 ATOM 167 O OD1 . ASN A 1 21 ? 31.558 -0.889 8.457 0.50 29.92 ? 38 ASN A OD1 1 ATOM 168 N ND2 . ASN A 1 21 ? 30.349 0.089 10.077 0.50 30.93 ? 38 ASN A ND2 1 ATOM 169 N N . GLY A 1 22 ? 28.344 -4.251 8.350 0.70 26.35 ? 39 GLY A N 1 ATOM 170 C CA . GLY A 1 22 ? 28.107 -5.315 9.326 0.70 26.31 ? 39 GLY A CA 1 ATOM 171 C C . GLY A 1 22 ? 26.896 -5.117 10.219 0.70 26.28 ? 39 GLY A C 1 ATOM 172 O O . GLY A 1 22 ? 26.561 -5.991 11.019 0.70 26.92 ? 39 GLY A O 1 ATOM 173 N N . SER A 1 23 ? 26.238 -3.969 10.087 1.00 26.14 ? 40 SER A N 1 ATOM 174 C CA . SER A 1 23 ? 25.097 -3.644 10.933 1.00 25.15 ? 40 SER A CA 1 ATOM 175 C C . SER A 1 23 ? 23.786 -3.990 10.259 1.00 24.20 ? 40 SER A C 1 ATOM 176 O O . SER A 1 23 ? 23.598 -3.773 9.074 1.00 24.66 ? 40 SER A O 1 ATOM 177 C CB . SER A 1 23 ? 25.087 -2.178 11.306 1.00 25.95 ? 40 SER A CB 1 ATOM 178 O OG . SER A 1 23 ? 24.552 -1.402 10.255 0.50 26.82 ? 40 SER A OG 1 ATOM 179 N N . LEU A 1 24 ? 22.867 -4.480 11.066 1.00 21.93 ? 41 LEU A N 1 ATOM 180 C CA . LEU A 1 24 ? 21.655 -5.047 10.557 1.00 19.82 ? 41 LEU A CA 1 ATOM 181 C C . LEU A 1 24 ? 20.512 -4.071 10.763 1.00 18.52 ? 41 LEU A C 1 ATOM 182 O O . LEU A 1 24 ? 20.435 -3.390 11.784 1.00 18.21 ? 41 LEU A O 1 ATOM 183 C CB . LEU A 1 24 ? 21.419 -6.348 11.293 1.00 20.25 ? 41 LEU A CB 1 ATOM 184 C CG . LEU A 1 24 ? 20.084 -7.044 11.249 1.00 21.24 ? 41 LEU A CG 1 ATOM 185 C CD1 . LEU A 1 24 ? 19.814 -7.555 9.831 1.00 20.69 ? 41 LEU A CD1 1 ATOM 186 C CD2 . LEU A 1 24 ? 20.126 -8.195 12.235 1.00 23.76 ? 41 LEU A CD2 1 ATOM 187 N N . CYS A 1 25 ? 19.662 -3.977 9.754 1.00 16.50 ? 42 CYS A N 1 ATOM 188 C CA . CYS A 1 25 ? 18.446 -3.175 9.827 1.00 15.93 ? 42 CYS A CA 1 ATOM 189 C C . CYS A 1 25 ? 17.390 -3.841 8.990 1.00 14.81 ? 42 CYS A C 1 ATOM 190 O O . CYS A 1 25 ? 17.691 -4.733 8.188 1.00 15.27 ? 42 CYS A O 1 ATOM 191 C CB . CYS A 1 25 ? 18.685 -1.773 9.280 1.00 16.60 ? 42 CYS A CB 1 ATOM 192 S SG . CYS A 1 25 ? 19.404 -0.637 10.481 1.00 20.17 ? 42 CYS A SG 1 ATOM 193 N N . GLY A 1 26 ? 16.152 -3.410 9.185 1.00 13.68 ? 43 GLY A N 1 ATOM 194 C CA . GLY A 1 26 ? 15.067 -3.748 8.293 1.00 13.36 ? 43 GLY A CA 1 ATOM 195 C C . GLY A 1 26 ? 14.785 -2.584 7.379 1.00 13.27 ? 43 GLY A C 1 ATOM 196 O O . GLY A 1 26 ? 15.392 -1.515 7.498 1.00 13.36 ? 43 GLY A O 1 ATOM 197 N N . GLY A 1 27 ? 13.850 -2.791 6.468 1.00 12.85 ? 44 GLY A N 1 ATOM 198 C CA . GLY A 1 27 ? 13.401 -1.732 5.577 1.00 12.82 ? 44 GLY A CA 1 ATOM 199 C C . GLY A 1 27 ? 12.109 -2.219 4.985 1.00 12.52 ? 44 GLY A C 1 ATOM 200 O O . GLY A 1 27 ? 11.722 -3.355 5.215 1.00 12.66 ? 44 GLY A O 1 ATOM 201 N N . THR A 1 28 ? 11.434 -1.355 4.236 1.00 12.47 ? 45 THR A N 1 ATOM 202 C CA . THR A 1 28 ? 10.163 -1.720 3.666 1.00 12.78 ? 45 THR A CA 1 ATOM 203 C C . THR A 1 28 ? 10.183 -1.370 2.209 1.00 12.96 ? 45 THR A C 1 ATOM 204 O O . THR A 1 28 ? 10.506 -0.257 1.835 1.00 13.38 ? 45 THR A O 1 ATOM 205 C CB . THR A 1 28 ? 9.013 -0.971 4.359 1.00 13.05 ? 45 THR A CB 1 ATOM 206 O OG1 . THR A 1 28 ? 9.069 -1.251 5.764 1.00 13.31 ? 45 THR A OG1 1 ATOM 207 C CG2 . THR A 1 28 ? 7.634 -1.411 3.784 1.00 13.23 ? 45 THR A CG2 1 ATOM 208 N N . LEU A 1 29 ? 9.829 -2.349 1.390 1.00 12.11 ? 46 LEU A N 1 ATOM 209 C CA . LEU A 1 29 ? 9.719 -2.147 -0.032 1.00 13.33 ? 46 LEU A CA 1 ATOM 210 C C . LEU A 1 29 ? 8.382 -1.453 -0.258 1.00 12.98 ? 46 LEU A C 1 ATOM 211 O O . LEU A 1 29 ? 7.342 -2.013 0.029 1.00 13.66 ? 46 LEU A O 1 ATOM 212 C CB . LEU A 1 29 ? 9.717 -3.522 -0.706 1.00 12.87 ? 46 LEU A CB 1 ATOM 213 C CG . LEU A 1 29 ? 9.737 -3.561 -2.224 1.00 14.30 ? 46 LEU A CG 1 ATOM 214 C CD1 . LEU A 1 29 ? 11.099 -3.050 -2.754 1.00 15.37 ? 46 LEU A CD1 1 ATOM 215 C CD2 . LEU A 1 29 ? 9.454 -4.986 -2.705 1.00 14.14 ? 46 LEU A CD2 1 ATOM 216 N N . ILE A 1 30 ? 8.402 -0.221 -0.760 1.00 13.17 ? 47 ILE A N 1 ATOM 217 C CA . ILE A 1 30 ? 7.151 0.524 -0.927 1.00 13.13 ? 47 ILE A CA 1 ATOM 218 C C . ILE A 1 30 ? 6.642 0.531 -2.356 1.00 13.68 ? 47 ILE A C 1 ATOM 219 O O . ILE A 1 30 ? 5.526 0.945 -2.635 1.00 14.17 ? 47 ILE A O 1 ATOM 220 C CB . ILE A 1 30 ? 7.265 1.972 -0.370 1.00 12.98 ? 47 ILE A CB 1 ATOM 221 C CG1 . ILE A 1 30 ? 8.432 2.723 -1.001 1.00 13.26 ? 47 ILE A CG1 1 ATOM 222 C CG2 . ILE A 1 30 ? 7.417 1.920 1.139 1.00 12.62 ? 47 ILE A CG2 1 ATOM 223 C CD1 . ILE A 1 30 ? 8.308 4.261 -0.829 1.00 13.17 ? 47 ILE A CD1 1 ATOM 224 N N . ASN A 1 31 ? 7.484 0.069 -3.259 1.00 14.05 ? 48 ASN A N 1 ATOM 225 C CA . ASN A 1 31 ? 7.058 -0.196 -4.612 1.00 14.81 ? 48 ASN A CA 1 ATOM 226 C C . ASN A 1 31 ? 8.153 -1.065 -5.175 1.00 15.31 ? 48 ASN A C 1 ATOM 227 O O . ASN A 1 31 ? 9.031 -1.512 -4.432 1.00 16.12 ? 48 ASN A O 1 ATOM 228 C CB . ASN A 1 31 ? 6.861 1.117 -5.382 1.00 14.88 ? 48 ASN A CB 1 ATOM 229 C CG . ASN A 1 31 ? 8.126 1.968 -5.426 1.00 15.42 ? 48 ASN A CG 1 ATOM 230 O OD1 . ASN A 1 31 ? 9.205 1.457 -5.691 1.00 15.06 ? 48 ASN A OD1 1 ATOM 231 N ND2 . ASN A 1 31 ? 7.990 3.266 -5.182 1.00 18.29 ? 48 ASN A ND2 1 ATOM 232 N N . GLN A 1 32 ? 8.152 -1.294 -6.471 1.00 15.06 ? 49 GLN A N 1 ATOM 233 C CA . GLN A 1 32 ? 9.098 -2.279 -6.998 1.00 15.89 ? 49 GLN A CA 1 ATOM 234 C C . GLN A 1 32 ? 10.541 -1.796 -7.088 1.00 15.56 ? 49 GLN A C 1 ATOM 235 O O . GLN A 1 32 ? 11.437 -2.570 -7.423 1.00 15.62 ? 49 GLN A O 1 ATOM 236 C CB . GLN A 1 32 ? 8.586 -2.841 -8.313 1.00 16.13 ? 49 GLN A CB 1 ATOM 237 C CG . GLN A 1 32 ? 7.368 -3.710 -8.029 1.00 16.88 ? 49 GLN A CG 1 ATOM 238 C CD . GLN A 1 32 ? 6.832 -4.424 -9.246 1.00 17.53 ? 49 GLN A CD 1 ATOM 239 O OE1 . GLN A 1 32 ? 7.193 -4.104 -10.375 1.00 19.50 ? 49 GLN A OE1 1 ATOM 240 N NE2 . GLN A 1 32 ? 5.953 -5.388 -9.017 1.00 18.30 ? 49 GLN A NE2 1 ATOM 241 N N . GLU A 1 33 ? 10.778 -0.533 -6.754 1.00 14.95 ? 50 GLU A N 1 ATOM 242 C CA . GLU A 1 33 ? 12.099 0.025 -6.914 1.00 15.88 ? 50 GLU A CA 1 ATOM 243 C C . GLU A 1 33 ? 12.586 0.804 -5.733 1.00 14.63 ? 50 GLU A C 1 ATOM 244 O O . GLU A 1 33 ? 13.676 1.328 -5.793 1.00 13.90 ? 50 GLU A O 1 ATOM 245 C CB . GLU A 1 33 ? 12.134 0.974 -8.121 1.00 17.38 ? 50 GLU A CB 1 ATOM 246 C CG . GLU A 1 33 ? 12.302 0.299 -9.390 1.00 21.47 ? 50 GLU A CG 1 ATOM 247 C CD . GLU A 1 33 ? 12.462 1.289 -10.493 1.00 22.47 ? 50 GLU A CD 1 ATOM 248 O OE1 . GLU A 1 33 ? 13.475 2.013 -10.494 1.00 21.55 ? 50 GLU A OE1 1 ATOM 249 O OE2 . GLU A 1 33 ? 11.577 1.312 -11.356 1.00 25.01 ? 50 GLU A OE2 1 ATOM 250 N N . TRP A 1 34 ? 11.776 0.920 -4.676 1.00 13.28 ? 51 TRP A N 1 ATOM 251 C CA . TRP A 1 34 ? 12.129 1.833 -3.594 1.00 13.27 ? 51 TRP A CA 1 ATOM 252 C C . TRP A 1 34 ? 11.873 1.236 -2.237 1.00 12.87 ? 51 TRP A C 1 ATOM 253 O O . TRP A 1 34 ? 10.874 0.544 -2.019 1.00 12.87 ? 51 TRP A O 1 ATOM 254 C CB . TRP A 1 34 ? 11.304 3.108 -3.698 1.00 13.48 ? 51 TRP A CB 1 ATOM 255 C CG . TRP A 1 34 ? 11.565 3.945 -4.899 1.00 14.67 ? 51 TRP A CG 1 ATOM 256 C CD1 . TRP A 1 34 ? 11.115 3.747 -6.167 1.00 13.88 ? 51 TRP A CD1 1 ATOM 257 C CD2 . TRP A 1 34 ? 12.296 5.175 -4.915 1.00 14.16 ? 51 TRP A CD2 1 ATOM 258 N NE1 . TRP A 1 34 ? 11.544 4.773 -6.994 1.00 13.87 ? 51 TRP A NE1 1 ATOM 259 C CE2 . TRP A 1 34 ? 12.280 5.655 -6.250 1.00 13.76 ? 51 TRP A CE2 1 ATOM 260 C CE3 . TRP A 1 34 ? 12.994 5.899 -3.940 1.00 15.09 ? 51 TRP A CE3 1 ATOM 261 C CZ2 . TRP A 1 34 ? 12.890 6.850 -6.619 1.00 12.68 ? 51 TRP A CZ2 1 ATOM 262 C CZ3 . TRP A 1 34 ? 13.606 7.075 -4.311 1.00 13.59 ? 51 TRP A CZ3 1 ATOM 263 C CH2 . TRP A 1 34 ? 13.554 7.536 -5.645 1.00 13.67 ? 51 TRP A CH2 1 ATOM 264 N N . VAL A 1 35 ? 12.787 1.530 -1.327 1.00 12.68 ? 52 VAL A N 1 ATOM 265 C CA . VAL A 1 35 ? 12.742 1.018 0.016 1.00 12.65 ? 52 VAL A CA 1 ATOM 266 C C . VAL A 1 35 ? 12.843 2.183 0.984 1.00 12.64 ? 52 VAL A C 1 ATOM 267 O O . VAL A 1 35 ? 13.614 3.124 0.771 1.00 13.13 ? 52 VAL A O 1 ATOM 268 C CB . VAL A 1 35 ? 13.922 0.034 0.226 1.00 12.51 ? 52 VAL A CB 1 ATOM 269 C CG1 . VAL A 1 35 ? 14.193 -0.227 1.709 1.00 14.01 ? 52 VAL A CG1 1 ATOM 270 C CG2 . VAL A 1 35 ? 13.664 -1.273 -0.547 1.00 13.85 ? 52 VAL A CG2 1 ATOM 271 N N . LEU A 1 36 ? 12.051 2.110 2.048 1.00 11.88 ? 53 LEU A N 1 ATOM 272 C CA . LEU A 1 36 ? 12.127 3.060 3.137 1.00 12.80 ? 53 LEU A CA 1 ATOM 273 C C . LEU A 1 36 ? 12.755 2.361 4.325 1.00 12.63 ? 53 LEU A C 1 ATOM 274 O O . LEU A 1 36 ? 12.375 1.249 4.682 1.00 14.00 ? 53 LEU A O 1 ATOM 275 C CB . LEU A 1 36 ? 10.735 3.569 3.512 1.00 13.14 ? 53 LEU A CB 1 ATOM 276 C CG . LEU A 1 36 ? 10.242 4.815 2.781 1.00 17.25 ? 53 LEU A CG 1 ATOM 277 C CD1 . LEU A 1 36 ? 8.768 5.109 3.133 1.00 17.35 ? 53 LEU A CD1 1 ATOM 278 C CD2 . LEU A 1 36 ? 11.103 6.033 3.092 1.00 14.68 ? 53 LEU A CD2 1 ATOM 279 N N . THR A 1 37 ? 13.709 3.033 4.952 1.00 12.65 ? 54 THR A N 1 ATOM 280 C CA . THR A 1 37 ? 14.369 2.499 6.139 1.00 12.90 ? 54 THR A CA 1 ATOM 281 C C . THR A 1 37 ? 14.680 3.689 7.042 1.00 12.91 ? 54 THR A C 1 ATOM 282 O O . THR A 1 37 ? 14.141 4.771 6.829 1.00 13.27 ? 54 THR A O 1 ATOM 283 C CB . THR A 1 37 ? 15.615 1.644 5.764 1.00 13.28 ? 54 THR A CB 1 ATOM 284 O OG1 . THR A 1 37 ? 16.157 1.022 6.928 1.00 13.75 ? 54 THR A OG1 1 ATOM 285 C CG2 . THR A 1 37 ? 16.735 2.492 5.100 1.00 12.44 ? 54 THR A CG2 1 ATOM 286 N N . ALA A 1 38 ? 15.493 3.466 8.072 1.00 13.96 ? 55 ALA A N 1 ATOM 287 C CA . ALA A 1 38 ? 15.862 4.544 8.983 1.00 14.28 ? 55 ALA A CA 1 ATOM 288 C C . ALA A 1 38 ? 17.162 5.148 8.467 1.00 15.04 ? 55 ALA A C 1 ATOM 289 O O . ALA A 1 38 ? 18.044 4.422 8.003 1.00 16.87 ? 55 ALA A O 1 ATOM 290 C CB . ALA A 1 38 ? 16.063 3.992 10.378 1.00 14.86 ? 55 ALA A CB 1 ATOM 291 N N . ARG A 1 39 ? 17.310 6.461 8.564 1.00 16.34 ? 56 ARG A N 1 ATOM 292 C CA . ARG A 1 39 ? 18.558 7.036 8.085 1.00 16.89 ? 56 ARG A CA 1 ATOM 293 C C . ARG A 1 39 ? 19.721 6.559 8.933 1.00 17.37 ? 56 ARG A C 1 ATOM 294 O O . ARG A 1 39 ? 20.825 6.428 8.430 1.00 18.21 ? 56 ARG A O 1 ATOM 295 C CB . ARG A 1 39 ? 18.513 8.552 7.995 1.00 17.13 ? 56 ARG A CB 1 ATOM 296 C CG . ARG A 1 39 ? 18.406 9.256 9.295 1.00 18.64 ? 56 ARG A CG 1 ATOM 297 C CD . ARG A 1 39 ? 18.327 10.774 9.058 1.00 19.57 ? 56 ARG A CD 1 ATOM 298 N NE . ARG A 1 39 ? 18.112 11.442 10.329 1.00 21.21 ? 56 ARG A NE 1 ATOM 299 C CZ . ARG A 1 39 ? 19.084 11.904 11.103 1.00 22.21 ? 56 ARG A CZ 1 ATOM 300 N NH1 . ARG A 1 39 ? 20.348 11.796 10.718 1.00 21.65 ? 56 ARG A NH1 1 ATOM 301 N NH2 . ARG A 1 39 ? 18.786 12.465 12.262 1.00 23.34 ? 56 ARG A NH2 1 ATOM 302 N N . HIS A 1 40 ? 19.474 6.229 10.196 1.00 16.74 ? 57 HIS A N 1 ATOM 303 C CA . HIS A 1 40 ? 20.591 5.760 11.002 1.00 16.88 ? 57 HIS A CA 1 ATOM 304 C C . HIS A 1 40 ? 21.167 4.421 10.542 1.00 17.80 ? 57 HIS A C 1 ATOM 305 O O . HIS A 1 40 ? 22.234 4.018 10.987 1.00 17.02 ? 57 HIS A O 1 ATOM 306 C CB . HIS A 1 40 ? 20.271 5.797 12.498 1.00 17.53 ? 57 HIS A CB 1 ATOM 307 C CG . HIS A 1 40 ? 19.560 4.596 13.010 1.00 17.06 ? 57 HIS A CG 1 ATOM 308 N ND1 . HIS A 1 40 ? 18.243 4.637 13.410 1.00 16.75 ? 57 HIS A ND1 1 ATOM 309 C CD2 . HIS A 1 40 ? 19.994 3.339 13.252 1.00 16.67 ? 57 HIS A CD2 1 ATOM 310 C CE1 . HIS A 1 40 ? 17.887 3.443 13.848 1.00 16.48 ? 57 HIS A CE1 1 ATOM 311 N NE2 . HIS A 1 40 ? 18.928 2.634 13.756 1.00 16.96 ? 57 HIS A NE2 1 ATOM 312 N N . CYS A 1 41 ? 20.466 3.747 9.629 1.00 17.59 ? 58 CYS A N 1 ATOM 313 C CA . CYS A 1 41 ? 20.907 2.455 9.129 1.00 18.86 ? 58 CYS A CA 1 ATOM 314 C C . CYS A 1 41 ? 21.944 2.615 8.031 1.00 19.69 ? 58 CYS A C 1 ATOM 315 O O . CYS A 1 41 ? 22.525 1.635 7.579 1.00 20.46 ? 58 CYS A O 1 ATOM 316 C CB . CYS A 1 41 ? 19.713 1.660 8.610 1.00 18.74 ? 58 CYS A CB 1 ATOM 317 S SG . CYS A 1 41 ? 18.615 1.157 9.918 1.00 19.05 ? 58 CYS A SG 1 ATOM 318 N N . ASP A 1 42 ? 22.170 3.862 7.627 1.00 20.24 ? 59 ASP A N 1 ATOM 319 C CA . ASP A 1 42 ? 23.081 4.187 6.515 1.00 22.24 ? 59 ASP A CA 1 ATOM 320 C C . ASP A 1 42 ? 24.484 4.242 7.062 1.00 22.90 ? 59 ASP A C 1 ATOM 321 O O . ASP A 1 42 ? 25.035 5.321 7.251 1.00 23.75 ? 59 ASP A O 1 ATOM 322 C CB . ASP A 1 42 ? 22.717 5.543 5.920 1.00 21.80 ? 59 ASP A CB 1 ATOM 323 C CG . ASP A 1 42 ? 23.439 5.840 4.591 1.00 24.47 ? 59 ASP A CG 1 ATOM 324 O OD1 . ASP A 1 42 ? 23.861 4.900 3.896 1.00 29.86 ? 59 ASP A OD1 1 ATOM 325 O OD2 . ASP A 1 42 ? 23.552 7.029 4.245 1.00 28.99 ? 59 ASP A OD2 1 ATOM 326 N N . ARG A 1 43 ? 25.044 3.070 7.327 1.00 24.36 ? 60 ARG A N 1 ATOM 327 C CA . ARG A 1 43 ? 26.333 2.976 7.983 1.00 25.66 ? 60 ARG A CA 1 ATOM 328 C C . ARG A 1 43 ? 27.453 2.586 7.017 1.00 26.17 ? 60 ARG A C 1 ATOM 329 O O . ARG A 1 43 ? 28.590 2.366 7.435 1.00 26.48 ? 60 ARG A O 1 ATOM 330 C CB . ARG A 1 43 ? 26.237 1.996 9.144 1.00 26.03 ? 60 ARG A CB 1 ATOM 331 C CG . ARG A 1 43 ? 25.265 2.445 10.246 1.00 28.11 ? 60 ARG A CG 1 ATOM 332 C CD . ARG A 1 43 ? 25.098 1.340 11.259 1.00 31.91 ? 60 ARG A CD 1 ATOM 333 N NE . ARG A 1 43 ? 24.501 1.766 12.520 1.00 33.28 ? 60 ARG A NE 1 ATOM 334 C CZ . ARG A 1 43 ? 23.343 1.317 13.009 1.00 34.31 ? 60 ARG A CZ 1 ATOM 335 N NH1 . ARG A 1 43 ? 22.911 1.774 14.179 1.00 35.63 ? 60 ARG A NH1 1 ATOM 336 N NH2 . ARG A 1 43 ? 22.616 0.419 12.349 1.00 33.63 ? 60 ARG A NH2 1 ATOM 337 N N . GLY A 1 44 ? 27.122 2.493 5.734 1.00 26.37 ? 62 GLY A N 1 ATOM 338 C CA . GLY A 1 44 ? 28.124 2.298 4.691 1.00 26.35 ? 62 GLY A CA 1 ATOM 339 C C . GLY A 1 44 ? 27.982 1.005 3.923 1.00 26.17 ? 62 GLY A C 1 ATOM 340 O O . GLY A 1 44 ? 27.678 -0.034 4.507 1.00 26.73 ? 62 GLY A O 1 ATOM 341 N N . ASN A 1 45 ? 28.234 1.067 2.616 1.00 26.12 ? 63 ASN A N 1 ATOM 342 C CA . ASN A 1 45 ? 28.158 -0.088 1.731 1.00 26.07 ? 63 ASN A CA 1 ATOM 343 C C . ASN A 1 45 ? 26.891 -0.900 1.972 1.00 25.28 ? 63 ASN A C 1 ATOM 344 O O . ASN A 1 45 ? 26.945 -2.063 2.341 1.00 26.14 ? 63 ASN A O 1 ATOM 345 C CB . ASN A 1 45 ? 29.396 -0.980 1.880 1.00 26.98 ? 63 ASN A CB 1 ATOM 346 C CG . ASN A 1 45 ? 30.633 -0.360 1.277 0.50 27.38 ? 63 ASN A CG 1 ATOM 347 O OD1 . ASN A 1 45 ? 30.556 0.376 0.293 0.50 30.06 ? 63 ASN A OD1 1 ATOM 348 N ND2 . ASN A 1 45 ? 31.788 -0.660 1.860 0.50 29.64 ? 63 ASN A ND2 1 ATOM 349 N N . MET A 1 46 ? 25.753 -0.268 1.758 1.00 24.12 ? 64 MET A N 1 ATOM 350 C CA . MET A 1 46 ? 24.493 -0.905 2.046 1.00 23.31 ? 64 MET A CA 1 ATOM 351 C C . MET A 1 46 ? 24.157 -1.965 1.014 1.00 22.10 ? 64 MET A C 1 ATOM 352 O O . MET A 1 46 ? 24.305 -1.746 -0.191 1.00 22.00 ? 64 MET A O 1 ATOM 353 C CB . MET A 1 46 ? 23.407 0.141 2.086 1.00 23.06 ? 64 MET A CB 1 ATOM 354 C CG . MET A 1 46 ? 22.154 -0.370 2.665 1.00 23.33 ? 64 MET A CG 1 ATOM 355 S SD . MET A 1 46 ? 20.908 0.879 2.527 1.00 26.66 ? 64 MET A SD 1 ATOM 356 C CE . MET A 1 46 ? 21.758 2.304 3.229 1.00 22.61 ? 64 MET A CE 1 ATOM 357 N N . ARG A 1 47 ? 23.726 -3.113 1.517 1.00 20.61 ? 65 ARG A N 1 ATOM 358 C CA . ARG A 1 47 ? 23.207 -4.188 0.701 1.00 20.06 ? 65 ARG A CA 1 ATOM 359 C C . ARG A 1 47 ? 21.789 -4.370 1.176 1.00 18.87 ? 65 ARG A C 1 ATOM 360 O O . ARG A 1 47 ? 21.538 -4.369 2.381 1.00 19.22 ? 65 ARG A O 1 ATOM 361 C CB . ARG A 1 47 ? 23.994 -5.477 0.944 1.00 20.80 ? 65 ARG A CB 1 ATOM 362 C CG . ARG A 1 47 ? 25.480 -5.369 0.578 1.00 22.73 ? 65 ARG A CG 1 ATOM 363 C CD . ARG A 1 47 ? 26.231 -6.639 0.961 0.50 20.27 ? 65 ARG A CD 1 ATOM 364 N NE . ARG A 1 47 ? 27.622 -6.621 0.518 0.50 22.18 ? 65 ARG A NE 1 ATOM 365 C CZ . ARG A 1 47 ? 28.559 -7.474 0.931 0.50 23.16 ? 65 ARG A CZ 1 ATOM 366 N NH1 . ARG A 1 47 ? 29.801 -7.372 0.471 0.50 24.80 ? 65 ARG A NH1 1 ATOM 367 N NH2 . ARG A 1 47 ? 28.266 -8.428 1.806 0.50 23.45 ? 65 ARG A NH2 1 ATOM 368 N N . ILE A 1 48 ? 20.858 -4.466 0.230 1.00 17.21 ? 66 ILE A N 1 ATOM 369 C CA . ILE A 1 48 ? 19.449 -4.566 0.591 1.00 17.11 ? 66 ILE A CA 1 ATOM 370 C C . ILE A 1 48 ? 18.942 -5.874 0.012 1.00 17.11 ? 66 ILE A C 1 ATOM 371 O O . ILE A 1 48 ? 19.065 -6.101 -1.185 1.00 16.99 ? 66 ILE A O 1 ATOM 372 C CB . ILE A 1 48 ? 18.646 -3.355 0.035 1.00 17.11 ? 66 ILE A CB 1 ATOM 373 C CG1 . ILE A 1 48 ? 19.256 -2.038 0.558 1.00 17.52 ? 66 ILE A CG1 1 ATOM 374 C CG2 . ILE A 1 48 ? 17.147 -3.472 0.380 1.00 16.79 ? 66 ILE A CG2 1 ATOM 375 C CD1 . ILE A 1 48 ? 18.754 -0.804 -0.139 1.00 20.33 ? 66 ILE A CD1 1 ATOM 376 N N . TYR A 1 49 ? 18.402 -6.737 0.866 1.00 16.58 ? 67 TYR A N 1 ATOM 377 C CA . TYR A 1 49 ? 17.970 -8.052 0.417 1.00 16.43 ? 67 TYR A CA 1 ATOM 378 C C . TYR A 1 49 ? 16.474 -8.069 0.455 1.00 15.91 ? 67 TYR A C 1 ATOM 379 O O . TYR A 1 49 ? 15.873 -7.724 1.461 1.00 15.54 ? 67 TYR A O 1 ATOM 380 C CB . TYR A 1 49 ? 18.514 -9.149 1.319 1.00 16.98 ? 67 TYR A CB 1 ATOM 381 C CG . TYR A 1 49 ? 20.008 -9.266 1.267 1.00 19.31 ? 67 TYR A CG 1 ATOM 382 C CD1 . TYR A 1 49 ? 20.806 -8.456 2.060 1.00 19.29 ? 67 TYR A CD1 1 ATOM 383 C CD2 . TYR A 1 49 ? 20.619 -10.202 0.438 1.00 20.39 ? 67 TYR A CD2 1 ATOM 384 C CE1 . TYR A 1 49 ? 22.180 -8.551 2.026 1.00 21.07 ? 67 TYR A CE1 1 ATOM 385 C CE2 . TYR A 1 49 ? 21.992 -10.317 0.392 1.00 21.96 ? 67 TYR A CE2 1 ATOM 386 C CZ . TYR A 1 49 ? 22.767 -9.489 1.194 1.00 21.69 ? 67 TYR A CZ 1 ATOM 387 O OH . TYR A 1 49 ? 24.147 -9.592 1.162 1.00 23.97 ? 67 TYR A OH 1 ATOM 388 N N . LEU A 1 50 ? 15.873 -8.439 -0.667 1.00 15.25 ? 68 LEU A N 1 ATOM 389 C CA . LEU A 1 50 ? 14.420 -8.542 -0.753 1.00 14.38 ? 68 LEU A CA 1 ATOM 390 C C . LEU A 1 50 ? 14.052 -10.009 -0.827 1.00 14.84 ? 68 LEU A C 1 ATOM 391 O O . LEU A 1 50 ? 14.853 -10.814 -1.283 1.00 14.42 ? 68 LEU A O 1 ATOM 392 C CB . LEU A 1 50 ? 13.891 -7.810 -1.999 1.00 14.97 ? 68 LEU A CB 1 ATOM 393 C CG . LEU A 1 50 ? 14.052 -6.276 -2.039 1.00 14.66 ? 68 LEU A CG 1 ATOM 394 C CD1 . LEU A 1 50 ? 13.609 -5.631 -0.707 1.00 15.69 ? 68 LEU A CD1 1 ATOM 395 C CD2 . LEU A 1 50 ? 15.454 -5.818 -2.416 1.00 15.58 ? 68 LEU A CD2 1 ATOM 396 N N . GLY A 1 51 ? 12.839 -10.343 -0.402 1.00 14.10 ? 69 GLY A N 1 ATOM 397 C CA . GLY A 1 51 ? 12.343 -11.720 -0.475 1.00 14.56 ? 69 GLY A CA 1 ATOM 398 C C . GLY A 1 51 ? 13.048 -12.689 0.454 1.00 14.99 ? 69 GLY A C 1 ATOM 399 O O . GLY A 1 51 ? 13.011 -13.890 0.238 1.00 15.33 ? 69 GLY A O 1 ATOM 400 N N . MET A 1 52 ? 13.671 -12.167 1.509 1.00 14.66 ? 70 MET A N 1 ATOM 401 C CA . MET A 1 52 ? 14.354 -13.023 2.469 1.00 15.02 ? 70 MET A CA 1 ATOM 402 C C . MET A 1 52 ? 13.449 -13.420 3.613 1.00 15.21 ? 70 MET A C 1 ATOM 403 O O . MET A 1 52 ? 12.652 -12.612 4.101 1.00 14.07 ? 70 MET A O 1 ATOM 404 C CB . MET A 1 52 ? 15.569 -12.292 3.046 1.00 15.35 ? 70 MET A CB 1 ATOM 405 C CG . MET A 1 52 ? 16.682 -12.047 2.038 1.00 15.85 ? 70 MET A CG 1 ATOM 406 S SD . MET A 1 52 ? 17.576 -13.581 1.710 1.00 17.83 ? 70 MET A SD 1 ATOM 407 C CE . MET A 1 52 ? 18.574 -13.682 3.184 1.00 21.37 ? 70 MET A CE 1 ATOM 408 N N . HIS A 1 53 ? 13.582 -14.665 4.053 1.00 14.31 ? 71 HIS A N 1 ATOM 409 C CA . HIS A 1 53 ? 13.000 -15.091 5.306 1.00 13.96 ? 71 HIS A CA 1 ATOM 410 C C . HIS A 1 53 ? 14.123 -15.699 6.125 1.00 14.08 ? 71 HIS A C 1 ATOM 411 O O . HIS A 1 53 ? 14.756 -15.026 6.943 1.00 14.60 ? 71 HIS A O 1 ATOM 412 C CB . HIS A 1 53 ? 11.889 -16.111 5.076 1.00 14.53 ? 71 HIS A CB 1 ATOM 413 C CG . HIS A 1 53 ? 11.221 -16.554 6.336 1.00 14.18 ? 71 HIS A CG 1 ATOM 414 N ND1 . HIS A 1 53 ? 10.231 -15.818 6.949 1.00 14.31 ? 71 HIS A ND1 1 ATOM 415 C CD2 . HIS A 1 53 ? 11.406 -17.653 7.106 1.00 16.48 ? 71 HIS A CD2 1 ATOM 416 C CE1 . HIS A 1 53 ? 9.840 -16.440 8.048 1.00 16.42 ? 71 HIS A CE1 1 ATOM 417 N NE2 . HIS A 1 53 ? 10.528 -17.565 8.158 1.00 16.33 ? 71 HIS A NE2 1 ATOM 418 N N . ASN A 1 54 ? 14.414 -16.970 5.866 1.00 14.15 ? 72 ASN A N 1 ATOM 419 C CA . ASN A 1 54 ? 15.509 -17.612 6.574 1.00 14.33 ? 72 ASN A CA 1 ATOM 420 C C . ASN A 1 54 ? 16.837 -17.200 5.959 1.00 14.65 ? 72 ASN A C 1 ATOM 421 O O . ASN A 1 54 ? 17.067 -17.389 4.767 1.00 14.69 ? 72 ASN A O 1 ATOM 422 C CB . ASN A 1 54 ? 15.345 -19.125 6.543 1.00 14.25 ? 72 ASN A CB 1 ATOM 423 C CG . ASN A 1 54 ? 16.191 -19.817 7.579 1.00 14.89 ? 72 ASN A CG 1 ATOM 424 O OD1 . ASN A 1 54 ? 17.337 -19.444 7.815 1.00 15.19 ? 72 ASN A OD1 1 ATOM 425 N ND2 . ASN A 1 54 ? 15.629 -20.855 8.193 1.00 16.49 ? 72 ASN A ND2 1 ATOM 426 N N . LEU A 1 55 ? 17.707 -16.615 6.780 1.00 14.81 ? 73 LEU A N 1 ATOM 427 C CA . LEU A 1 55 ? 19.013 -16.193 6.335 1.00 15.35 ? 73 LEU A CA 1 ATOM 428 C C . LEU A 1 55 ? 19.919 -17.371 5.973 1.00 16.01 ? 73 LEU A C 1 ATOM 429 O O . LEU A 1 55 ? 20.960 -17.173 5.339 1.00 16.76 ? 73 LEU A O 1 ATOM 430 C CB . LEU A 1 55 ? 19.687 -15.392 7.442 1.00 15.16 ? 73 LEU A CB 1 ATOM 431 C CG . LEU A 1 55 ? 18.933 -14.168 7.964 1.00 16.83 ? 73 LEU A CG 1 ATOM 432 C CD1 . LEU A 1 55 ? 19.768 -13.498 9.041 1.00 19.08 ? 73 LEU A CD1 1 ATOM 433 C CD2 . LEU A 1 55 ? 18.617 -13.197 6.853 1.00 20.68 ? 73 LEU A CD2 1 ATOM 434 N N . LYS A 1 56 ? 19.519 -18.571 6.385 1.00 15.42 ? 74 LYS A N 1 ATOM 435 C CA . LYS A 1 56 ? 20.309 -19.783 6.167 1.00 15.95 ? 74 LYS A CA 1 ATOM 436 C C . LYS A 1 56 ? 19.631 -20.772 5.226 1.00 15.86 ? 74 LYS A C 1 ATOM 437 O O . LYS A 1 56 ? 20.193 -21.822 4.899 1.00 15.67 ? 74 LYS A O 1 ATOM 438 C CB . LYS A 1 56 ? 20.627 -20.445 7.497 1.00 15.92 ? 74 LYS A CB 1 ATOM 439 C CG . LYS A 1 56 ? 21.440 -19.536 8.374 1.00 18.64 ? 74 LYS A CG 1 ATOM 440 C CD . LYS A 1 56 ? 21.968 -20.247 9.577 1.00 22.71 ? 74 LYS A CD 1 ATOM 441 C CE . LYS A 1 56 ? 23.003 -19.354 10.256 1.00 26.67 ? 74 LYS A CE 1 ATOM 442 N NZ . LYS A 1 56 ? 23.347 -19.918 11.566 1.00 31.46 ? 74 LYS A NZ 1 ATOM 443 N N . VAL A 1 57 ? 18.421 -20.437 4.796 1.00 15.32 ? 75 VAL A N 1 ATOM 444 C CA . VAL A 1 57 ? 17.709 -21.235 3.819 1.00 15.32 ? 75 VAL A CA 1 ATOM 445 C C . VAL A 1 57 ? 17.113 -20.231 2.865 1.00 15.51 ? 75 VAL A C 1 ATOM 446 O O . VAL A 1 57 ? 16.002 -19.736 3.069 1.00 15.42 ? 75 VAL A O 1 ATOM 447 C CB . VAL A 1 57 ? 16.595 -22.103 4.456 1.00 14.72 ? 75 VAL A CB 1 ATOM 448 C CG1 . VAL A 1 57 ? 15.936 -22.995 3.377 1.00 17.46 ? 75 VAL A CG1 1 ATOM 449 C CG2 . VAL A 1 57 ? 17.146 -22.950 5.602 1.00 16.46 ? 75 VAL A CG2 1 ATOM 450 N N . LEU A 1 58 ? 17.854 -19.912 1.814 1.00 15.08 ? 76 LEU A N 1 ATOM 451 C CA . LEU A 1 58 ? 17.470 -18.749 1.025 1.00 15.56 ? 76 LEU A CA 1 ATOM 452 C C . LEU A 1 58 ? 16.225 -19.034 0.234 1.00 15.73 ? 76 LEU A C 1 ATOM 453 O O . LEU A 1 58 ? 16.159 -20.038 -0.471 1.00 15.66 ? 76 LEU A O 1 ATOM 454 C CB . LEU A 1 58 ? 18.606 -18.319 0.085 1.00 15.19 ? 76 LEU A CB 1 ATOM 455 C CG . LEU A 1 58 ? 19.918 -17.957 0.768 1.00 15.56 ? 76 LEU A CG 1 ATOM 456 C CD1 . LEU A 1 58 ? 20.926 -17.508 -0.240 1.00 16.40 ? 76 LEU A CD1 1 ATOM 457 C CD2 . LEU A 1 58 ? 19.686 -16.872 1.803 1.00 18.72 ? 76 LEU A CD2 1 ATOM 458 N N . ASN A 1 59 ? 15.242 -18.134 0.319 1.00 14.80 ? 77 ASN A N 1 ATOM 459 C CA . ASN A 1 59 ? 14.119 -18.225 -0.584 1.00 15.50 ? 77 ASN A CA 1 ATOM 460 C C . ASN A 1 59 ? 14.645 -18.180 -1.994 1.00 15.43 ? 77 ASN A C 1 ATOM 461 O O . ASN A 1 59 ? 15.545 -17.407 -2.304 1.00 17.28 ? 77 ASN A O 1 ATOM 462 C CB . ASN A 1 59 ? 13.150 -17.067 -0.368 1.00 14.87 ? 77 ASN A CB 1 ATOM 463 C CG . ASN A 1 59 ? 12.336 -17.224 0.898 1.00 15.30 ? 77 ASN A CG 1 ATOM 464 O OD1 . ASN A 1 59 ? 12.160 -18.337 1.409 1.00 15.66 ? 77 ASN A OD1 1 ATOM 465 N ND2 . ASN A 1 59 ? 11.803 -16.106 1.404 1.00 15.02 ? 77 ASN A ND2 1 ATOM 466 N N . LYS A 1 60 ? 14.049 -18.995 -2.860 1.00 17.15 ? 78 LYS A N 1 ATOM 467 C CA . LYS A 1 60 ? 14.470 -19.077 -4.252 1.00 17.62 ? 78 LYS A CA 1 ATOM 468 C C . LYS A 1 60 ? 14.395 -17.733 -4.946 1.00 17.45 ? 78 LYS A C 1 ATOM 469 O O . LYS A 1 60 ? 15.193 -17.436 -5.833 1.00 19.00 ? 78 LYS A O 1 ATOM 470 C CB . LYS A 1 60 ? 13.595 -20.089 -4.988 1.00 18.11 ? 78 LYS A CB 1 ATOM 471 C CG . LYS A 1 60 ? 13.872 -21.529 -4.616 0.50 19.37 ? 78 LYS A CG 1 ATOM 472 C CD . LYS A 1 60 ? 12.721 -22.417 -5.077 0.50 22.51 ? 78 LYS A CD 1 ATOM 473 C CE . LYS A 1 60 ? 13.093 -23.887 -5.058 0.50 24.66 ? 78 LYS A CE 1 ATOM 474 N NZ . LYS A 1 60 ? 13.773 -24.266 -6.318 0.50 26.13 ? 78 LYS A NZ 1 ATOM 475 N N . ASP A 1 61 ? 13.446 -16.902 -4.519 1.00 17.19 ? 79 ASP A N 1 ATOM 476 C CA . ASP A 1 61 ? 13.239 -15.625 -5.150 1.00 16.93 ? 79 ASP A CA 1 ATOM 477 C C . ASP A 1 61 ? 13.920 -14.476 -4.414 1.00 16.89 ? 79 ASP A C 1 ATOM 478 O O . ASP A 1 61 ? 13.707 -13.320 -4.765 1.00 17.09 ? 79 ASP A O 1 ATOM 479 C CB . ASP A 1 61 ? 11.743 -15.341 -5.322 1.00 17.61 ? 79 ASP A CB 1 ATOM 480 C CG . ASP A 1 61 ? 10.962 -15.426 -4.033 1.00 17.27 ? 79 ASP A CG 1 ATOM 481 O OD1 . ASP A 1 61 ? 11.339 -16.168 -3.113 1.00 17.02 ? 79 ASP A OD1 1 ATOM 482 O OD2 . ASP A 1 61 ? 9.915 -14.762 -3.958 1.00 18.07 ? 79 ASP A OD2 1 ATOM 483 N N . ALA A 1 62 ? 14.739 -14.784 -3.417 1.00 15.98 ? 80 ALA A N 1 ATOM 484 C CA . ALA A 1 62 ? 15.470 -13.717 -2.735 1.00 15.72 ? 80 ALA A CA 1 ATOM 485 C C . ALA A 1 62 ? 16.391 -12.974 -3.700 1.00 15.88 ? 80 ALA A C 1 ATOM 486 O O . ALA A 1 62 ? 16.959 -13.554 -4.635 1.00 16.03 ? 80 ALA A O 1 ATOM 487 C CB . ALA A 1 62 ? 16.262 -14.254 -1.544 1.00 16.21 ? 80 ALA A CB 1 ATOM 488 N N . LEU A 1 63 ? 16.523 -11.675 -3.479 1.00 16.30 ? 81 LEU A N 1 ATOM 489 C CA . LEU A 1 63 ? 17.321 -10.821 -4.352 1.00 16.20 ? 81 LEU A CA 1 ATOM 490 C C . LEU A 1 63 ? 18.180 -9.880 -3.522 1.00 16.60 ? 81 LEU A C 1 ATOM 491 O O . LEU A 1 63 ? 17.793 -9.498 -2.417 1.00 16.88 ? 81 LEU A O 1 ATOM 492 C CB . LEU A 1 63 ? 16.399 -10.003 -5.248 1.00 16.94 ? 81 LEU A CB 1 ATOM 493 C CG . LEU A 1 63 ? 15.569 -10.799 -6.265 1.00 18.47 ? 81 LEU A CG 1 ATOM 494 C CD1 . LEU A 1 63 ? 14.549 -9.887 -6.926 1.00 21.90 ? 81 LEU A CD1 1 ATOM 495 C CD2 . LEU A 1 63 ? 16.510 -11.371 -7.290 1.00 19.95 ? 81 LEU A CD2 1 ATOM 496 N N . ARG A 1 64 ? 19.325 -9.498 -4.078 1.00 16.59 ? 82 ARG A N 1 ATOM 497 C CA . ARG A 1 64 ? 20.210 -8.501 -3.473 1.00 18.13 ? 82 ARG A CA 1 ATOM 498 C C . ARG A 1 64 ? 20.205 -7.246 -4.338 1.00 16.96 ? 82 ARG A C 1 ATOM 499 O O . ARG A 1 64 ? 20.235 -7.316 -5.571 1.00 17.06 ? 82 ARG A O 1 ATOM 500 C CB . ARG A 1 64 ? 21.649 -9.055 -3.336 1.00 17.86 ? 82 ARG A CB 1 ATOM 501 C CG . ARG A 1 64 ? 22.640 -8.204 -2.515 1.00 20.50 ? 82 ARG A CG 1 ATOM 502 C CD . ARG A 1 64 ? 24.107 -8.669 -2.770 1.00 22.24 ? 82 ARG A CD 1 ATOM 503 N NE . ARG A 1 64 ? 24.303 -10.106 -2.606 0.50 28.15 ? 82 ARG A NE 1 ATOM 504 C CZ . ARG A 1 64 ? 24.943 -10.670 -1.584 0.50 30.84 ? 82 ARG A CZ 1 ATOM 505 N NH1 . ARG A 1 64 ? 25.062 -11.986 -1.514 0.50 32.33 ? 82 ARG A NH1 1 ATOM 506 N NH2 . ARG A 1 64 ? 25.469 -9.922 -0.629 0.50 33.46 ? 82 ARG A NH2 1 ATOM 507 N N . ARG A 1 65 ? 20.143 -6.096 -3.685 1.00 16.85 ? 83 ARG A N 1 ATOM 508 C CA . ARG A 1 65 ? 20.118 -4.824 -4.375 1.00 16.32 ? 83 ARG A CA 1 ATOM 509 C C . ARG A 1 65 ? 21.003 -3.871 -3.609 1.00 16.23 ? 83 ARG A C 1 ATOM 510 O O . ARG A 1 65 ? 21.459 -4.197 -2.513 1.00 15.95 ? 83 ARG A O 1 ATOM 511 C CB . ARG A 1 65 ? 18.689 -4.280 -4.415 1.00 16.72 ? 83 ARG A CB 1 ATOM 512 C CG . ARG A 1 65 ? 17.731 -5.105 -5.292 1.00 16.24 ? 83 ARG A CG 1 ATOM 513 C CD . ARG A 1 65 ? 18.092 -4.957 -6.771 1.00 16.83 ? 83 ARG A CD 1 ATOM 514 N NE . ARG A 1 65 ? 17.127 -5.594 -7.672 1.00 16.20 ? 83 ARG A NE 1 ATOM 515 C CZ . ARG A 1 65 ? 17.235 -6.830 -8.155 1.00 17.28 ? 83 ARG A CZ 1 ATOM 516 N NH1 . ARG A 1 65 ? 18.253 -7.597 -7.793 1.00 16.50 ? 83 ARG A NH1 1 ATOM 517 N NH2 . ARG A 1 65 ? 16.322 -7.299 -9.011 1.00 16.87 ? 83 ARG A NH2 1 ATOM 518 N N . PHE A 1 66 ? 21.266 -2.715 -4.196 1.00 16.28 ? 84 PHE A N 1 ATOM 519 C CA . PHE A 1 66 ? 21.956 -1.679 -3.473 1.00 17.85 ? 84 PHE A CA 1 ATOM 520 C C . PHE A 1 66 ? 21.355 -0.346 -3.838 1.00 17.05 ? 84 PHE A C 1 ATOM 521 O O . PHE A 1 66 ? 20.575 -0.251 -4.781 1.00 16.99 ? 84 PHE A O 1 ATOM 522 C CB . PHE A 1 66 ? 23.460 -1.740 -3.726 1.00 19.51 ? 84 PHE A CB 1 ATOM 523 C CG . PHE A 1 66 ? 23.834 -1.583 -5.148 1.00 21.63 ? 84 PHE A CG 1 ATOM 524 C CD1 . PHE A 1 66 ? 24.014 -0.308 -5.695 1.00 23.79 ? 84 PHE A CD1 1 ATOM 525 C CD2 . PHE A 1 66 ? 24.030 -2.706 -5.949 1.00 24.38 ? 84 PHE A CD2 1 ATOM 526 C CE1 . PHE A 1 66 ? 24.365 -0.153 -7.036 1.00 25.73 ? 84 PHE A CE1 1 ATOM 527 C CE2 . PHE A 1 66 ? 24.384 -2.563 -7.288 1.00 25.33 ? 84 PHE A CE2 1 ATOM 528 C CZ . PHE A 1 66 ? 24.552 -1.285 -7.831 1.00 24.15 ? 84 PHE A CZ 1 ATOM 529 N N . PRO A 1 67 ? 21.675 0.689 -3.067 1.00 16.51 ? 85 PRO A N 1 ATOM 530 C CA . PRO A 1 67 ? 21.065 1.982 -3.361 1.00 16.97 ? 85 PRO A CA 1 ATOM 531 C C . PRO A 1 67 ? 21.598 2.597 -4.642 1.00 17.67 ? 85 PRO A C 1 ATOM 532 O O . PRO A 1 67 ? 22.816 2.642 -4.843 1.00 18.50 ? 85 PRO A O 1 ATOM 533 C CB . PRO A 1 67 ? 21.456 2.848 -2.146 1.00 17.30 ? 85 PRO A CB 1 ATOM 534 C CG . PRO A 1 67 ? 21.901 1.876 -1.111 1.00 17.39 ? 85 PRO A CG 1 ATOM 535 C CD . PRO A 1 67 ? 22.508 0.732 -1.852 1.00 16.93 ? 85 PRO A CD 1 ATOM 536 N N . LYS A 1 68 ? 20.681 3.045 -5.502 1.00 16.78 ? 86 LYS A N 1 ATOM 537 C CA . LYS A 1 68 ? 21.010 3.812 -6.679 1.00 17.64 ? 86 LYS A CA 1 ATOM 538 C C . LYS A 1 68 ? 20.644 5.276 -6.438 1.00 16.86 ? 86 LYS A C 1 ATOM 539 O O . LYS A 1 68 ? 21.275 6.196 -6.999 1.00 17.12 ? 86 LYS A O 1 ATOM 540 C CB . LYS A 1 68 ? 20.244 3.238 -7.864 1.00 18.16 ? 86 LYS A CB 1 ATOM 541 C CG . LYS A 1 68 ? 20.398 3.999 -9.140 1.00 22.63 ? 86 LYS A CG 1 ATOM 542 C CD . LYS A 1 68 ? 19.735 3.233 -10.258 1.00 27.18 ? 86 LYS A CD 1 ATOM 543 C CE . LYS A 1 68 ? 18.230 3.287 -10.133 1.00 30.95 ? 86 LYS A CE 1 ATOM 544 N NZ . LYS A 1 68 ? 17.569 3.246 -11.469 1.00 35.50 ? 86 LYS A NZ 1 ATOM 545 N N . GLU A 1 69 ? 19.624 5.499 -5.606 1.00 16.02 ? 87 GLU A N 1 ATOM 546 C CA . GLU A 1 69 ? 19.286 6.849 -5.153 1.00 14.67 ? 87 GLU A CA 1 ATOM 547 C C . GLU A 1 69 ? 19.077 6.767 -3.657 1.00 15.43 ? 87 GLU A C 1 ATOM 548 O O . GLU A 1 69 ? 18.680 5.725 -3.137 1.00 14.49 ? 87 GLU A O 1 ATOM 549 C CB . GLU A 1 69 ? 18.028 7.407 -5.842 1.00 14.97 ? 87 GLU A CB 1 ATOM 550 C CG . GLU A 1 69 ? 18.165 7.422 -7.369 1.00 13.81 ? 87 GLU A CG 1 ATOM 551 C CD . GLU A 1 69 ? 17.000 8.035 -8.083 1.00 15.40 ? 87 GLU A CD 1 ATOM 552 O OE1 . GLU A 1 69 ? 16.894 7.782 -9.301 1.00 17.97 ? 87 GLU A OE1 1 ATOM 553 O OE2 . GLU A 1 69 ? 16.204 8.776 -7.466 1.00 17.42 ? 87 GLU A OE2 1 ATOM 554 N N . LYS A 1 70 ? 19.373 7.854 -2.967 1.00 15.55 ? 88 LYS A N 1 ATOM 555 C CA . LYS A 1 70 ? 19.321 7.845 -1.520 1.00 15.21 ? 88 LYS A CA 1 ATOM 556 C C . LYS A 1 70 ? 18.922 9.224 -1.070 1.00 15.40 ? 88 LYS A C 1 ATOM 557 O O . LYS A 1 70 ? 19.554 10.209 -1.455 1.00 15.81 ? 88 LYS A O 1 ATOM 558 C CB . LYS A 1 70 ? 20.693 7.479 -0.954 1.00 16.23 ? 88 LYS A CB 1 ATOM 559 C CG . LYS A 1 70 ? 20.749 7.490 0.562 1.00 18.74 ? 88 LYS A CG 1 ATOM 560 C CD . LYS A 1 70 ? 22.184 7.212 1.048 1.00 23.46 ? 88 LYS A CD 1 ATOM 561 C CE . LYS A 1 70 ? 22.667 5.823 0.678 1.00 25.36 ? 88 LYS A CE 1 ATOM 562 N NZ . LYS A 1 70 ? 24.070 5.581 1.231 1.00 27.66 ? 88 LYS A NZ 1 ATOM 563 N N . TYR A 1 71 ? 17.870 9.297 -0.260 1.00 14.05 ? 89 TYR A N 1 ATOM 564 C CA . TYR A 1 71 ? 17.375 10.566 0.214 1.00 13.83 ? 89 TYR A CA 1 ATOM 565 C C . TYR A 1 71 ? 17.082 10.489 1.690 1.00 14.14 ? 89 TYR A C 1 ATOM 566 O O . TYR A 1 71 ? 16.728 9.447 2.213 1.00 14.22 ? 89 TYR A O 1 ATOM 567 C CB . TYR A 1 71 ? 16.071 10.931 -0.478 1.00 13.32 ? 89 TYR A CB 1 ATOM 568 C CG . TYR A 1 71 ? 16.152 10.923 -1.982 1.00 13.22 ? 89 TYR A CG 1 ATOM 569 C CD1 . TYR A 1 71 ? 15.888 9.764 -2.700 1.00 13.55 ? 89 TYR A CD1 1 ATOM 570 C CD2 . TYR A 1 71 ? 16.463 12.081 -2.676 1.00 15.48 ? 89 TYR A CD2 1 ATOM 571 C CE1 . TYR A 1 71 ? 15.961 9.752 -4.101 1.00 13.92 ? 89 TYR A CE1 1 ATOM 572 C CE2 . TYR A 1 71 ? 16.543 12.090 -4.045 1.00 14.47 ? 89 TYR A CE2 1 ATOM 573 C CZ . TYR A 1 71 ? 16.288 10.932 -4.756 1.00 15.10 ? 89 TYR A CZ 1 ATOM 574 O OH . TYR A 1 71 ? 16.345 10.954 -6.125 1.00 15.22 ? 89 TYR A OH 1 ATOM 575 N N . PHE A 1 72 ? 17.188 11.639 2.335 1.00 14.65 ? 90 PHE A N 1 ATOM 576 C CA . PHE A 1 72 ? 16.813 11.776 3.726 1.00 15.47 ? 90 PHE A CA 1 ATOM 577 C C . PHE A 1 72 ? 16.609 13.267 3.934 1.00 15.09 ? 90 PHE A C 1 ATOM 578 O O . PHE A 1 72 ? 16.860 14.081 3.030 1.00 14.96 ? 90 PHE A O 1 ATOM 579 C CB . PHE A 1 72 ? 17.924 11.246 4.644 1.00 16.12 ? 90 PHE A CB 1 ATOM 580 C CG . PHE A 1 72 ? 19.294 11.740 4.271 1.00 19.92 ? 90 PHE A CG 1 ATOM 581 C CD1 . PHE A 1 72 ? 19.774 12.943 4.776 1.00 22.68 ? 90 PHE A CD1 1 ATOM 582 C CD2 . PHE A 1 72 ? 20.091 11.003 3.405 1.00 21.87 ? 90 PHE A CD2 1 ATOM 583 C CE1 . PHE A 1 72 ? 21.044 13.417 4.394 1.00 23.07 ? 90 PHE A CE1 1 ATOM 584 C CE2 . PHE A 1 72 ? 21.351 11.467 3.037 1.00 24.24 ? 90 PHE A CE2 1 ATOM 585 C CZ . PHE A 1 72 ? 21.809 12.665 3.528 1.00 21.19 ? 90 PHE A CZ 1 ATOM 586 N N . CYS A 1 73 ? 16.165 13.623 5.124 1.00 15.73 ? 91 CYS A N 1 ATOM 587 C CA . CYS A 1 73 ? 15.856 15.006 5.441 1.00 16.95 ? 91 CYS A CA 1 ATOM 588 C C . CYS A 1 73 ? 17.136 15.725 5.813 1.00 18.27 ? 91 CYS A C 1 ATOM 589 O O . CYS A 1 73 ? 17.920 15.248 6.622 1.00 19.00 ? 91 CYS A O 1 ATOM 590 C CB . CYS A 1 73 ? 14.892 15.064 6.612 1.00 16.71 ? 91 CYS A CB 1 ATOM 591 S SG . CYS A 1 73 ? 13.431 14.061 6.373 1.00 17.34 ? 91 CYS A SG 1 ATOM 592 N N . LEU A 1 74 ? 17.370 16.867 5.180 1.00 21.71 ? 92 LEU A N 1 ATOM 593 C CA . LEU A 1 74 ? 18.636 17.570 5.402 1.00 23.29 ? 92 LEU A CA 1 ATOM 594 C C . LEU A 1 74 ? 18.594 18.430 6.659 1.00 24.68 ? 92 LEU A C 1 ATOM 595 O O . LEU A 1 74 ? 19.615 18.598 7.338 1.00 26.25 ? 92 LEU A O 1 ATOM 596 C CB . LEU A 1 74 ? 19.008 18.414 4.174 1.00 23.00 ? 92 LEU A CB 1 ATOM 597 C CG . LEU A 1 74 ? 19.177 17.652 2.861 1.00 23.19 ? 92 LEU A CG 1 ATOM 598 C CD1 . LEU A 1 74 ? 19.640 18.604 1.778 1.00 24.06 ? 92 LEU A CD1 1 ATOM 599 C CD2 . LEU A 1 74 ? 20.188 16.532 3.023 1.00 24.15 ? 92 LEU A CD2 1 ATOM 600 N N . ASN A 1 75 ? 17.420 18.988 6.951 1.00 25.50 ? 93 ASN A N 1 ATOM 601 C CA . ASN A 1 75 ? 17.215 19.772 8.162 1.00 26.88 ? 93 ASN A CA 1 ATOM 602 C C . ASN A 1 75 ? 16.775 18.853 9.308 1.00 26.81 ? 93 ASN A C 1 ATOM 603 O O . ASN A 1 75 ? 15.600 18.558 9.462 1.00 27.43 ? 93 ASN A O 1 ATOM 604 C CB . ASN A 1 75 ? 16.142 20.848 7.930 1.00 27.42 ? 93 ASN A CB 1 ATOM 605 C CG . ASN A 1 75 ? 16.641 22.029 7.099 0.70 28.89 ? 93 ASN A CG 1 ATOM 606 O OD1 . ASN A 1 75 ? 17.757 22.519 7.286 0.70 30.28 ? 93 ASN A OD1 1 ATOM 607 N ND2 . ASN A 1 75 ? 15.782 22.524 6.207 0.70 30.53 ? 93 ASN A ND2 1 ATOM 608 N N . THR A 1 76 ? 17.713 18.396 10.117 1.00 27.51 ? 94 THR A N 1 ATOM 609 C CA . THR A 1 76 ? 17.304 17.626 11.280 1.00 28.12 ? 94 THR A CA 1 ATOM 610 C C . THR A 1 76 ? 17.709 18.334 12.560 1.00 28.46 ? 94 THR A C 1 ATOM 611 O O . THR A 1 76 ? 18.739 19.014 12.610 1.00 29.06 ? 94 THR A O 1 ATOM 612 C CB . THR A 1 76 ? 17.868 16.216 11.247 1.00 27.94 ? 94 THR A CB 1 ATOM 613 O OG1 . THR A 1 76 ? 19.277 16.273 11.013 1.00 29.97 ? 94 THR A OG1 1 ATOM 614 C CG2 . THR A 1 76 ? 17.181 15.387 10.146 1.00 27.82 ? 94 THR A CG2 1 ATOM 615 N N . ARG A 1 77 ? 16.890 18.191 13.590 1.00 28.30 ? 95 ARG A N 1 ATOM 616 C CA . ARG A 1 77 ? 17.244 18.765 14.882 1.00 28.31 ? 95 ARG A CA 1 ATOM 617 C C . ARG A 1 77 ? 18.425 18.052 15.488 1.00 28.65 ? 95 ARG A C 1 ATOM 618 O O . ARG A 1 77 ? 18.664 16.869 15.223 1.00 29.29 ? 95 ARG A O 1 ATOM 619 C CB . ARG A 1 77 ? 16.056 18.716 15.832 1.00 28.14 ? 95 ARG A CB 1 ATOM 620 C CG . ARG A 1 77 ? 14.979 19.670 15.436 1.00 28.03 ? 95 ARG A CG 1 ATOM 621 C CD . ARG A 1 77 ? 13.745 19.450 16.257 1.00 27.54 ? 95 ARG A CD 1 ATOM 622 N NE . ARG A 1 77 ? 13.949 19.843 17.650 1.00 26.32 ? 95 ARG A NE 1 ATOM 623 C CZ . ARG A 1 77 ? 12.954 20.125 18.480 1.00 28.02 ? 95 ARG A CZ 1 ATOM 624 N NH1 . ARG A 1 77 ? 13.211 20.472 19.732 1.00 28.66 ? 95 ARG A NH1 1 ATOM 625 N NH2 . ARG A 1 77 ? 11.695 20.059 18.053 1.00 28.44 ? 95 ARG A NH2 1 ATOM 626 N N . ASN A 1 78 A 19.177 18.781 16.301 1.00 28.43 ? 96 ASN A N 1 ATOM 627 C CA . ASN A 1 78 A 20.316 18.220 16.990 1.00 28.53 ? 96 ASN A CA 1 ATOM 628 C C . ASN A 1 78 A 19.945 17.879 18.430 1.00 27.66 ? 96 ASN A C 1 ATOM 629 O O . ASN A 1 78 A 20.612 17.067 19.068 1.00 27.85 ? 96 ASN A O 1 ATOM 630 C CB . ASN A 1 78 A 21.493 19.197 16.966 1.00 29.67 ? 96 ASN A CB 1 ATOM 631 C CG . ASN A 1 78 A 22.832 18.493 16.904 0.50 31.54 ? 96 ASN A CG 1 ATOM 632 O OD1 . ASN A 1 78 A 23.626 18.725 15.991 0.50 33.67 ? 96 ASN A OD1 1 ATOM 633 N ND2 . ASN A 1 78 A 23.092 17.634 17.880 0.50 35.21 ? 96 ASN A ND2 1 ATOM 634 N N . ASP A 1 79 ? 18.878 18.492 18.932 1.00 26.22 ? 96 ASP A N 1 ATOM 635 C CA . ASP A 1 79 ? 18.507 18.314 20.339 1.00 26.03 ? 96 ASP A CA 1 ATOM 636 C C . ASP A 1 79 ? 17.563 17.139 20.570 1.00 25.53 ? 96 ASP A C 1 ATOM 637 O O . ASP A 1 79 ? 17.391 16.687 21.696 1.00 25.39 ? 96 ASP A O 1 ATOM 638 C CB . ASP A 1 79 ? 17.899 19.603 20.909 1.00 25.99 ? 96 ASP A CB 1 ATOM 639 C CG . ASP A 1 79 ? 16.636 20.025 20.188 1.00 26.49 ? 96 ASP A CG 1 ATOM 640 O OD1 . ASP A 1 79 ? 16.489 19.712 18.991 1.00 27.16 ? 96 ASP A OD1 1 ATOM 641 O OD2 . ASP A 1 79 ? 15.780 20.676 20.806 1.00 27.38 ? 96 ASP A OD2 1 ATOM 642 N N . THR A 1 80 ? 16.932 16.649 19.509 1.00 25.72 ? 97 THR A N 1 ATOM 643 C CA . THR A 1 80 ? 16.106 15.447 19.655 1.00 25.57 ? 97 THR A CA 1 ATOM 644 C C . THR A 1 80 ? 16.867 14.232 19.133 1.00 25.08 ? 97 THR A C 1 ATOM 645 O O . THR A 1 80 ? 17.843 14.367 18.396 1.00 24.97 ? 97 THR A O 1 ATOM 646 C CB . THR A 1 80 ? 14.709 15.570 18.987 1.00 26.18 ? 97 THR A CB 1 ATOM 647 O OG1 . THR A 1 80 ? 14.864 15.888 17.602 1.00 25.86 ? 97 THR A OG1 1 ATOM 648 C CG2 . THR A 1 80 ? 13.847 16.640 19.677 1.00 26.07 ? 97 THR A CG2 1 ATOM 649 N N . ILE A 1 81 ? 16.434 13.046 19.547 1.00 24.29 ? 98 ILE A N 1 ATOM 650 C CA . ILE A 1 81 ? 17.149 11.819 19.220 1.00 23.34 ? 98 ILE A CA 1 ATOM 651 C C . ILE A 1 81 ? 16.762 11.334 17.829 1.00 22.25 ? 98 ILE A C 1 ATOM 652 O O . ILE A 1 81 ? 15.596 11.036 17.579 1.00 22.34 ? 98 ILE A O 1 ATOM 653 C CB . ILE A 1 81 ? 16.811 10.695 20.219 1.00 23.91 ? 98 ILE A CB 1 ATOM 654 C CG1 . ILE A 1 81 ? 16.994 11.170 21.671 1.00 25.47 ? 98 ILE A CG1 1 ATOM 655 C CG2 . ILE A 1 81 ? 17.634 9.431 19.902 1.00 24.43 ? 98 ILE A CG2 1 ATOM 656 C CD1 . ILE A 1 81 ? 16.065 10.428 22.658 1.00 29.73 ? 98 ILE A CD1 1 ATOM 657 N N . TRP A 1 82 ? 17.744 11.242 16.938 1.00 21.63 ? 99 TRP A N 1 ATOM 658 C CA . TRP A 1 82 ? 17.504 10.740 15.571 1.00 20.81 ? 99 TRP A CA 1 ATOM 659 C C . TRP A 1 82 ? 16.276 11.378 14.949 1.00 19.56 ? 99 TRP A C 1 ATOM 660 O O . TRP A 1 82 ? 15.331 10.712 14.516 1.00 19.08 ? 99 TRP A O 1 ATOM 661 C CB . TRP A 1 82 ? 17.435 9.206 15.572 1.00 21.67 ? 99 TRP A CB 1 ATOM 662 C CG . TRP A 1 82 ? 18.777 8.660 15.716 1.00 21.92 ? 99 TRP A CG 1 ATOM 663 C CD1 . TRP A 1 82 ? 19.311 8.059 16.821 1.00 23.11 ? 99 TRP A CD1 1 ATOM 664 C CD2 . TRP A 1 82 ? 19.810 8.691 14.729 1.00 21.42 ? 99 TRP A CD2 1 ATOM 665 N NE1 . TRP A 1 82 ? 20.619 7.702 16.573 1.00 24.52 ? 99 TRP A NE1 1 ATOM 666 C CE2 . TRP A 1 82 ? 20.952 8.089 15.300 1.00 23.62 ? 99 TRP A CE2 1 ATOM 667 C CE3 . TRP A 1 82 ? 19.890 9.192 13.419 1.00 22.47 ? 99 TRP A CE3 1 ATOM 668 C CZ2 . TRP A 1 82 ? 22.155 7.950 14.601 1.00 23.10 ? 99 TRP A CZ2 1 ATOM 669 C CZ3 . TRP A 1 82 ? 21.087 9.043 12.720 1.00 23.10 ? 99 TRP A CZ3 1 ATOM 670 C CH2 . TRP A 1 82 ? 22.206 8.432 13.321 1.00 23.01 ? 99 TRP A CH2 1 ATOM 671 N N . ASP A 1 83 ? 16.272 12.696 14.931 1.00 18.15 ? 100 ASP A N 1 ATOM 672 C CA . ASP A 1 83 ? 15.181 13.407 14.321 1.00 17.31 ? 100 ASP A CA 1 ATOM 673 C C . ASP A 1 83 ? 15.017 12.960 12.875 1.00 16.94 ? 100 ASP A C 1 ATOM 674 O O . ASP A 1 83 ? 16.006 12.754 12.173 1.00 17.71 ? 100 ASP A O 1 ATOM 675 C CB . ASP A 1 83 ? 15.450 14.911 14.344 1.00 17.53 ? 100 ASP A CB 1 ATOM 676 C CG . ASP A 1 83 ? 14.223 15.727 13.976 1.00 18.91 ? 100 ASP A CG 1 ATOM 677 O OD1 . ASP A 1 83 ? 13.061 15.317 14.291 1.00 20.26 ? 100 ASP A OD1 1 ATOM 678 O OD2 . ASP A 1 83 ? 14.409 16.795 13.361 1.00 22.88 ? 100 ASP A OD2 1 ATOM 679 N N . LYS A 1 84 ? 13.770 12.800 12.455 1.00 17.54 ? 101 LYS A N 1 ATOM 680 C CA . LYS A 1 84 ? 13.458 12.445 11.065 1.00 16.37 ? 101 LYS A CA 1 ATOM 681 C C . LYS A 1 84 ? 14.259 11.226 10.629 1.00 15.66 ? 101 LYS A C 1 ATOM 682 O O . LYS A 1 84 ? 15.046 11.246 9.653 1.00 14.91 ? 101 LYS A O 1 ATOM 683 C CB . LYS A 1 84 ? 13.733 13.641 10.162 1.00 17.15 ? 101 LYS A CB 1 ATOM 684 C CG . LYS A 1 84 ? 12.868 14.842 10.517 1.00 18.77 ? 101 LYS A CG 1 ATOM 685 C CD . LYS A 1 84 ? 13.076 15.983 9.561 1.00 23.55 ? 101 LYS A CD 1 ATOM 686 C CE . LYS A 1 84 ? 12.666 17.316 10.175 1.00 25.65 ? 101 LYS A CE 1 ATOM 687 N NZ . LYS A 1 84 ? 11.334 17.238 10.843 1.00 30.57 ? 101 LYS A NZ 1 ATOM 688 N N . ASP A 1 85 ? 14.073 10.141 11.371 1.00 14.22 ? 102 ASP A N 1 ATOM 689 C CA . ASP A 1 85 ? 14.884 8.975 11.125 1.00 13.91 ? 102 ASP A CA 1 ATOM 690 C C . ASP A 1 85 ? 14.258 8.151 10.015 1.00 13.85 ? 102 ASP A C 1 ATOM 691 O O . ASP A 1 85 ? 13.496 7.205 10.256 1.00 14.08 ? 102 ASP A O 1 ATOM 692 C CB . ASP A 1 85 ? 15.025 8.173 12.407 1.00 13.27 ? 102 ASP A CB 1 ATOM 693 C CG . ASP A 1 85 ? 16.166 7.194 12.356 1.00 13.89 ? 102 ASP A CG 1 ATOM 694 O OD1 . ASP A 1 85 ? 16.905 7.138 11.348 1.00 15.54 ? 102 ASP A OD1 1 ATOM 695 O OD2 . ASP A 1 85 ? 16.345 6.479 13.351 1.00 14.92 ? 102 ASP A OD2 1 ATOM 696 N N . ILE A 1 86 ? 14.580 8.549 8.784 1.00 13.05 ? 103 ILE A N 1 ATOM 697 C CA . ILE A 1 86 ? 13.949 7.982 7.607 1.00 12.94 ? 103 ILE A CA 1 ATOM 698 C C . ILE A 1 86 ? 14.872 8.206 6.439 1.00 13.42 ? 103 ILE A C 1 ATOM 699 O O . ILE A 1 86 ? 15.498 9.251 6.320 1.00 13.59 ? 103 ILE A O 1 ATOM 700 C CB . ILE A 1 86 ? 12.575 8.638 7.346 1.00 13.26 ? 103 ILE A CB 1 ATOM 701 C CG1 . ILE A 1 86 ? 11.872 8.016 6.129 1.00 13.56 ? 103 ILE A CG1 1 ATOM 702 C CG2 . ILE A 1 86 ? 12.671 10.168 7.240 1.00 14.42 ? 103 ILE A CG2 1 ATOM 703 C CD1 . ILE A 1 86 ? 10.452 8.515 5.954 1.00 13.85 ? 103 ILE A CD1 1 ATOM 704 N N . MET A 1 87 ? 14.955 7.206 5.585 1.00 13.12 ? 104 MET A N 1 ATOM 705 C CA . MET A 1 87 ? 15.800 7.295 4.418 1.00 14.63 ? 104 MET A CA 1 ATOM 706 C C . MET A 1 87 ? 15.084 6.543 3.323 1.00 14.32 ? 104 MET A C 1 ATOM 707 O O . MET A 1 87 ? 14.611 5.428 3.533 1.00 13.47 ? 104 MET A O 1 ATOM 708 C CB . MET A 1 87 ? 17.165 6.693 4.697 1.00 14.84 ? 104 MET A CB 1 ATOM 709 C CG . MET A 1 87 ? 17.967 6.471 3.455 1.00 17.09 ? 104 MET A CG 1 ATOM 710 S SD . MET A 1 87 ? 19.673 6.039 3.827 1.00 20.42 ? 104 MET A SD 1 ATOM 711 C CE . MET A 1 87 ? 20.295 7.630 4.350 1.00 24.60 ? 104 MET A CE 1 ATOM 712 N N . LEU A 1 88 ? 15.011 7.174 2.159 1.00 13.78 ? 105 LEU A N 1 ATOM 713 C CA . LEU A 1 88 ? 14.268 6.616 1.026 1.00 12.95 ? 105 LEU A CA 1 ATOM 714 C C . LEU A 1 88 ? 15.296 6.245 -0.010 1.00 13.41 ? 105 LEU A C 1 ATOM 715 O O . LEU A 1 88 ? 16.121 7.074 -0.396 1.00 14.30 ? 105 LEU A O 1 ATOM 716 C CB . LEU A 1 88 ? 13.345 7.684 0.473 1.00 13.04 ? 105 LEU A CB 1 ATOM 717 C CG . LEU A 1 88 ? 12.543 7.356 -0.783 1.00 13.52 ? 105 LEU A CG 1 ATOM 718 C CD1 . LEU A 1 88 ? 11.700 6.110 -0.523 1.00 14.70 ? 105 LEU A CD1 1 ATOM 719 C CD2 . LEU A 1 88 ? 11.663 8.551 -1.079 1.00 13.98 ? 105 LEU A CD2 1 ATOM 720 N N . ILE A 1 89 ? 15.253 4.993 -0.452 1.00 13.44 ? 106 ILE A N 1 ATOM 721 C CA . ILE A 1 89 ? 16.300 4.477 -1.302 1.00 13.03 ? 106 ILE A CA 1 ATOM 722 C C . ILE A 1 89 ? 15.658 3.933 -2.558 1.00 12.80 ? 106 ILE A C 1 ATOM 723 O O . ILE A 1 89 ? 14.662 3.243 -2.482 1.00 12.42 ? 106 ILE A O 1 ATOM 724 C CB . ILE A 1 89 ? 17.054 3.351 -0.581 1.00 13.93 ? 106 ILE A CB 1 ATOM 725 C CG1 . ILE A 1 89 ? 17.888 3.938 0.560 1.00 15.07 ? 106 ILE A CG1 1 ATOM 726 C CG2 . ILE A 1 89 ? 17.931 2.560 -1.561 1.00 14.92 ? 106 ILE A CG2 1 ATOM 727 C CD1 . ILE A 1 89 ? 18.384 2.908 1.507 1.00 20.15 ? 106 ILE A CD1 1 ATOM 728 N N . ARG A 1 90 ? 16.235 4.253 -3.703 1.00 12.55 ? 107 ARG A N 1 ATOM 729 C CA . ARG A 1 90 ? 15.840 3.604 -4.922 1.00 12.76 ? 107 ARG A CA 1 ATOM 730 C C . ARG A 1 90 ? 16.863 2.518 -5.167 1.00 13.23 ? 107 ARG A C 1 ATOM 731 O O . ARG A 1 90 ? 18.067 2.750 -5.117 1.00 12.96 ? 107 ARG A O 1 ATOM 732 C CB . ARG A 1 90 ? 15.833 4.574 -6.093 1.00 12.91 ? 107 ARG A CB 1 ATOM 733 C CG . ARG A 1 90 ? 15.264 3.938 -7.331 1.00 13.88 ? 107 ARG A CG 1 ATOM 734 C CD . ARG A 1 90 ? 15.332 4.905 -8.467 1.00 14.53 ? 107 ARG A CD 1 ATOM 735 N NE . ARG A 1 90 ? 14.678 4.361 -9.652 1.00 17.81 ? 107 ARG A NE 1 ATOM 736 C CZ . ARG A 1 90 ? 14.576 5.032 -10.792 1.00 22.71 ? 107 ARG A CZ 1 ATOM 737 N NH1 . ARG A 1 90 ? 13.955 4.484 -11.823 1.00 21.78 ? 107 ARG A NH1 1 ATOM 738 N NH2 . ARG A 1 90 ? 15.115 6.244 -10.901 1.00 23.73 ? 107 ARG A NH2 1 ATOM 739 N N . LEU A 1 91 ? 16.353 1.321 -5.415 1.00 13.06 ? 108 LEU A N 1 ATOM 740 C CA . LEU A 1 91 ? 17.183 0.162 -5.671 1.00 13.21 ? 108 LEU A CA 1 ATOM 741 C C . LEU A 1 91 ? 17.815 0.281 -7.042 1.00 14.13 ? 108 LEU A C 1 ATOM 742 O O . LEU A 1 91 ? 17.284 0.971 -7.934 1.00 15.44 ? 108 LEU A O 1 ATOM 743 C CB . LEU A 1 91 ? 16.335 -1.103 -5.614 1.00 12.81 ? 108 LEU A CB 1 ATOM 744 C CG . LEU A 1 91 ? 15.541 -1.245 -4.326 1.00 13.44 ? 108 LEU A CG 1 ATOM 745 C CD1 . LEU A 1 91 ? 14.633 -2.458 -4.457 1.00 15.58 ? 108 LEU A CD1 1 ATOM 746 C CD2 . LEU A 1 91 ? 16.505 -1.367 -3.143 1.00 14.02 ? 108 LEU A CD2 1 ATOM 747 N N . ASN A 1 92 ? 18.928 -0.419 -7.209 1.00 14.54 ? 109 ASN A N 1 ATOM 748 C CA . ASN A 1 92 ? 19.662 -0.385 -8.467 1.00 15.27 ? 109 ASN A CA 1 ATOM 749 C C . ASN A 1 92 ? 18.889 -1.001 -9.616 1.00 15.79 ? 109 ASN A C 1 ATOM 750 O O . ASN A 1 92 ? 19.072 -0.603 -10.757 1.00 17.07 ? 109 ASN A O 1 ATOM 751 C CB . ASN A 1 92 ? 21.019 -1.067 -8.324 1.00 15.29 ? 109 ASN A CB 1 ATOM 752 C CG . ASN A 1 92 ? 20.908 -2.496 -7.880 1.00 17.23 ? 109 ASN A CG 1 ATOM 753 O OD1 . ASN A 1 92 ? 20.376 -2.792 -6.814 1.00 16.06 ? 109 ASN A OD1 1 ATOM 754 N ND2 . ASN A 1 92 ? 21.426 -3.408 -8.701 1.00 17.92 ? 109 ASN A ND2 1 ATOM 755 N N . ARG A 1 93 ? 18.064 -1.991 -9.305 1.00 16.06 ? 110 ARG A N 1 ATOM 756 C CA . ARG A 1 93 ? 17.198 -2.615 -10.285 1.00 17.78 ? 110 ARG A CA 1 ATOM 757 C C . ARG A 1 93 ? 15.887 -2.928 -9.594 1.00 17.39 ? 110 ARG A C 1 ATOM 758 O O . ARG A 1 93 ? 15.878 -3.175 -8.386 1.00 16.79 ? 110 ARG A O 1 ATOM 759 C CB . ARG A 1 93 ? 17.795 -3.934 -10.783 1.00 18.65 ? 110 ARG A CB 1 ATOM 760 C CG . ARG A 1 93 ? 19.004 -3.798 -11.681 1.00 23.84 ? 110 ARG A CG 1 ATOM 761 C CD . ARG A 1 93 ? 19.194 -5.077 -12.487 1.00 29.71 ? 110 ARG A CD 1 ATOM 762 N NE . ARG A 1 93 ? 19.378 -6.274 -11.664 1.00 32.62 ? 110 ARG A NE 1 ATOM 763 C CZ . ARG A 1 93 ? 20.517 -6.611 -11.062 1.00 35.87 ? 110 ARG A CZ 1 ATOM 764 N NH1 . ARG A 1 93 ? 20.588 -7.731 -10.346 1.00 36.56 ? 110 ARG A NH1 1 ATOM 765 N NH2 . ARG A 1 93 ? 21.591 -5.833 -11.175 1.00 38.79 ? 110 ARG A NH2 1 ATOM 766 N N . PRO A 1 94 ? 14.775 -2.908 -10.348 1.00 17.69 ? 111 PRO A N 1 ATOM 767 C CA . PRO A 1 94 ? 13.490 -3.232 -9.756 1.00 17.30 ? 111 PRO A CA 1 ATOM 768 C C . PRO A 1 94 ? 13.434 -4.675 -9.304 1.00 18.26 ? 111 PRO A C 1 ATOM 769 O O . PRO A 1 94 ? 14.222 -5.521 -9.763 1.00 17.68 ? 111 PRO A O 1 ATOM 770 C CB . PRO A 1 94 ? 12.494 -2.997 -10.898 1.00 17.60 ? 111 PRO A CB 1 ATOM 771 C CG . PRO A 1 94 ? 13.221 -2.119 -11.854 1.00 17.97 ? 111 PRO A CG 1 ATOM 772 C CD . PRO A 1 94 ? 14.639 -2.548 -11.770 1.00 17.87 ? 111 PRO A CD 1 ATOM 773 N N . VAL A 1 95 ? 12.514 -4.928 -8.382 1.00 17.84 ? 112 VAL A N 1 ATOM 774 C CA . VAL A 1 95 ? 12.198 -6.277 -7.959 1.00 19.37 ? 112 VAL A CA 1 ATOM 775 C C . VAL A 1 95 ? 10.732 -6.507 -8.247 1.00 20.48 ? 112 VAL A C 1 ATOM 776 O O . VAL A 1 95 ? 9.856 -5.782 -7.731 1.00 21.64 ? 112 VAL A O 1 ATOM 777 C CB . VAL A 1 95 ? 12.487 -6.540 -6.451 1.00 19.07 ? 112 VAL A CB 1 ATOM 778 C CG1 . VAL A 1 95 ? 13.967 -6.436 -6.166 1.00 18.05 ? 112 VAL A CG1 1 ATOM 779 C CG2 . VAL A 1 95 ? 11.685 -5.595 -5.536 1.00 20.41 ? 112 VAL A CG2 1 ATOM 780 N N . ARG A 1 96 ? 10.462 -7.515 -9.053 1.00 20.51 ? 113 ARG A N 1 ATOM 781 C CA . ARG A 1 96 ? 9.087 -7.834 -9.385 1.00 20.67 ? 113 ARG A CA 1 ATOM 782 C C . ARG A 1 96 ? 8.411 -8.658 -8.301 1.00 19.66 ? 113 ARG A C 1 ATOM 783 O O . ARG A 1 96 ? 9.080 -9.301 -7.466 1.00 19.27 ? 113 ARG A O 1 ATOM 784 C CB . ARG A 1 96 ? 9.001 -8.486 -10.769 1.00 21.89 ? 113 ARG A CB 1 ATOM 785 C CG . ARG A 1 96 ? 9.508 -7.525 -11.861 1.00 23.91 ? 113 ARG A CG 1 ATOM 786 C CD . ARG A 1 96 ? 8.716 -6.229 -11.785 0.50 24.76 ? 113 ARG A CD 1 ATOM 787 N NE . ARG A 1 96 ? 9.333 -5.018 -12.340 0.50 26.26 ? 113 ARG A NE 1 ATOM 788 C CZ . ARG A 1 96 ? 10.282 -4.962 -13.269 0.50 27.44 ? 113 ARG A CZ 1 ATOM 789 N NH1 . ARG A 1 96 ? 10.709 -3.774 -13.680 0.50 26.12 ? 113 ARG A NH1 1 ATOM 790 N NH2 . ARG A 1 96 ? 10.805 -6.068 -13.794 0.50 28.80 ? 113 ARG A NH2 1 ATOM 791 N N . ASN A 1 97 ? 7.082 -8.633 -8.298 1.00 19.22 ? 114 ASN A N 1 ATOM 792 C CA . ASN A 1 97 ? 6.343 -9.396 -7.306 1.00 19.40 ? 114 ASN A CA 1 ATOM 793 C C . ASN A 1 97 ? 6.639 -10.876 -7.473 1.00 19.66 ? 114 ASN A C 1 ATOM 794 O O . ASN A 1 97 ? 6.758 -11.373 -8.598 1.00 19.95 ? 114 ASN A O 1 ATOM 795 C CB . ASN A 1 97 ? 4.841 -9.145 -7.410 1.00 19.98 ? 114 ASN A CB 1 ATOM 796 C CG . ASN A 1 97 ? 4.424 -7.824 -6.773 1.00 19.73 ? 114 ASN A CG 1 ATOM 797 O OD1 . ASN A 1 97 ? 5.209 -6.874 -6.694 1.00 20.77 ? 114 ASN A OD1 1 ATOM 798 N ND2 . ASN A 1 97 ? 3.172 -7.753 -6.338 1.00 22.51 ? 114 ASN A ND2 1 ATOM 799 N N . SER A 1 98 ? 6.792 -11.568 -6.356 1.00 19.01 ? 115 SER A N 1 ATOM 800 C CA . SER A 1 98 ? 7.055 -12.999 -6.381 1.00 19.29 ? 115 SER A CA 1 ATOM 801 C C . SER A 1 98 ? 6.488 -13.577 -5.090 1.00 18.71 ? 115 SER A C 1 ATOM 802 O O . SER A 1 98 ? 5.890 -12.846 -4.293 1.00 18.99 ? 115 SER A O 1 ATOM 803 C CB . SER A 1 98 ? 8.552 -13.273 -6.548 1.00 19.27 ? 115 SER A CB 1 ATOM 804 O OG . SER A 1 98 ? 9.287 -12.783 -5.447 1.00 20.34 ? 115 SER A OG 1 ATOM 805 N N . ALA A 1 99 ? 6.664 -14.879 -4.864 1.00 18.71 ? 116 ALA A N 1 ATOM 806 C CA . ALA A 1 99 ? 6.065 -15.501 -3.707 1.00 18.47 ? 116 ALA A CA 1 ATOM 807 C C . ALA A 1 99 ? 6.419 -14.714 -2.459 1.00 17.78 ? 116 ALA A C 1 ATOM 808 O O . ALA A 1 99 ? 5.591 -14.540 -1.575 1.00 19.21 ? 116 ALA A O 1 ATOM 809 C CB . ALA A 1 99 ? 6.518 -16.954 -3.569 1.00 19.17 ? 116 ALA A CB 1 ATOM 810 N N . HIS A 1 100 ? 7.651 -14.207 -2.410 1.00 16.84 ? 117 HIS A N 1 ATOM 811 C CA . HIS A 1 100 ? 8.153 -13.597 -1.174 1.00 15.57 ? 117 HIS A CA 1 ATOM 812 C C . HIS A 1 100 ? 8.492 -12.144 -1.297 1.00 14.98 ? 117 HIS A C 1 ATOM 813 O O . HIS A 1 100 ? 9.084 -11.571 -0.382 1.00 14.29 ? 117 HIS A O 1 ATOM 814 C CB . HIS A 1 100 ? 9.337 -14.397 -0.665 1.00 16.22 ? 117 HIS A CB 1 ATOM 815 C CG . HIS A 1 100 ? 9.007 -15.837 -0.461 1.00 16.30 ? 117 HIS A CG 1 ATOM 816 N ND1 . HIS A 1 100 ? 9.603 -16.839 -1.189 1.00 18.61 ? 117 HIS A ND1 1 ATOM 817 C CD2 . HIS A 1 100 ? 8.113 -16.440 0.361 1.00 16.45 ? 117 HIS A CD2 1 ATOM 818 C CE1 . HIS A 1 100 ? 9.103 -18.003 -0.816 1.00 18.82 ? 117 HIS A CE1 1 ATOM 819 N NE2 . HIS A 1 100 ? 8.185 -17.791 0.112 1.00 17.76 ? 117 HIS A NE2 1 ATOM 820 N N . ILE A 1 101 ? 8.108 -11.540 -2.420 1.00 14.34 ? 118 ILE A N 1 ATOM 821 C CA . ILE A 1 101 ? 8.396 -10.128 -2.653 1.00 13.84 ? 118 ILE A CA 1 ATOM 822 C C . ILE A 1 101 ? 7.152 -9.409 -3.138 1.00 13.88 ? 118 ILE A C 1 ATOM 823 O O . ILE A 1 101 ? 6.559 -9.805 -4.128 1.00 15.17 ? 118 ILE A O 1 ATOM 824 C CB . ILE A 1 101 ? 9.515 -9.933 -3.689 1.00 13.99 ? 118 ILE A CB 1 ATOM 825 C CG1 . ILE A 1 101 ? 10.828 -10.556 -3.201 1.00 13.91 ? 118 ILE A CG1 1 ATOM 826 C CG2 . ILE A 1 101 ? 9.697 -8.458 -4.026 1.00 15.77 ? 118 ILE A CG2 1 ATOM 827 C CD1 . ILE A 1 101 ? 11.995 -10.463 -4.208 1.00 14.67 ? 118 ILE A CD1 1 ATOM 828 N N . ALA A 1 102 ? 6.748 -8.363 -2.424 1.00 14.31 ? 119 ALA A N 1 ATOM 829 C CA . ALA A 1 102 ? 5.688 -7.478 -2.917 1.00 13.73 ? 119 ALA A CA 1 ATOM 830 C C . ALA A 1 102 ? 5.741 -6.214 -2.076 1.00 13.55 ? 119 ALA A C 1 ATOM 831 O O . ALA A 1 102 ? 5.986 -6.300 -0.884 1.00 13.25 ? 119 ALA A O 1 ATOM 832 C CB . ALA A 1 102 ? 4.332 -8.134 -2.795 1.00 14.76 ? 119 ALA A CB 1 ATOM 833 N N . PRO A 1 103 ? 5.503 -5.051 -2.694 1.00 14.18 ? 120 PRO A N 1 ATOM 834 C CA . PRO A 1 103 ? 5.575 -3.817 -1.925 1.00 13.89 ? 120 PRO A CA 1 ATOM 835 C C . PRO A 1 103 ? 4.381 -3.570 -1.029 1.00 14.37 ? 120 PRO A C 1 ATOM 836 O O . PRO A 1 103 ? 3.301 -4.144 -1.226 1.00 15.75 ? 120 PRO A O 1 ATOM 837 C CB . PRO A 1 103 ? 5.631 -2.734 -2.990 1.00 15.21 ? 120 PRO A CB 1 ATOM 838 C CG . PRO A 1 103 ? 4.929 -3.329 -4.180 1.00 14.56 ? 120 PRO A CG 1 ATOM 839 C CD . PRO A 1 103 ? 5.198 -4.812 -4.121 1.00 13.71 ? 120 PRO A CD 1 ATOM 840 N N . LEU A 1 104 ? 4.606 -2.721 -0.037 1.00 13.64 ? 121 LEU A N 1 ATOM 841 C CA . LEU A 1 104 ? 3.572 -2.269 0.845 1.00 14.90 ? 121 LEU A CA 1 ATOM 842 C C . LEU A 1 104 ? 3.574 -0.776 0.664 1.00 15.16 ? 121 LEU A C 1 ATOM 843 O O . LEU A 1 104 ? 4.579 -0.127 0.875 1.00 16.22 ? 121 LEU A O 1 ATOM 844 C CB . LEU A 1 104 ? 3.956 -2.580 2.290 1.00 14.98 ? 121 LEU A CB 1 ATOM 845 C CG . LEU A 1 104 ? 2.906 -2.882 3.367 1.00 20.20 ? 121 LEU A CG 1 ATOM 846 C CD1 . LEU A 1 104 ? 3.442 -2.508 4.724 1.00 19.51 ? 121 LEU A CD1 1 ATOM 847 C CD2 . LEU A 1 104 ? 1.524 -2.339 3.129 1.00 21.40 ? 121 LEU A CD2 1 ATOM 848 N N . SER A 1 105 ? 2.439 -0.237 0.280 1.00 15.84 ? 122 SER A N 1 ATOM 849 C CA . SER A 1 105 ? 2.391 1.150 -0.114 1.00 16.73 ? 122 SER A CA 1 ATOM 850 C C . SER A 1 105 ? 2.149 2.113 1.049 1.00 15.81 ? 122 SER A C 1 ATOM 851 O O . SER A 1 105 ? 2.341 1.777 2.219 1.00 15.28 ? 122 SER A O 1 ATOM 852 C CB . SER A 1 105 ? 1.364 1.302 -1.238 1.00 18.81 ? 122 SER A CB 1 ATOM 853 O OG . SER A 1 105 ? 1.894 0.680 -2.410 1.00 23.89 ? 122 SER A OG 1 ATOM 854 N N . LEU A 1 106 ? 1.733 3.329 0.703 1.00 14.33 ? 123 LEU A N 1 ATOM 855 C CA . LEU A 1 106 ? 1.724 4.413 1.668 1.00 13.50 ? 123 LEU A CA 1 ATOM 856 C C . LEU A 1 106 ? 0.402 4.481 2.389 1.00 13.86 ? 123 LEU A C 1 ATOM 857 O O . LEU A 1 106 ? -0.652 4.290 1.792 1.00 13.72 ? 123 LEU A O 1 ATOM 858 C CB . LEU A 1 106 ? 2.022 5.738 0.960 1.00 13.28 ? 123 LEU A CB 1 ATOM 859 C CG . LEU A 1 106 ? 3.361 5.819 0.212 1.00 13.81 ? 123 LEU A CG 1 ATOM 860 C CD1 . LEU A 1 106 ? 3.561 7.249 -0.270 1.00 14.97 ? 123 LEU A CD1 1 ATOM 861 C CD2 . LEU A 1 106 ? 4.533 5.392 1.120 1.00 14.02 ? 123 LEU A CD2 1 ATOM 862 N N . PRO A 1 107 ? 0.446 4.729 3.701 1.00 13.38 ? 124 PRO A N 1 ATOM 863 C CA . PRO A 1 107 ? -0.785 4.683 4.477 1.00 13.59 ? 124 PRO A CA 1 ATOM 864 C C . PRO A 1 107 ? -1.746 5.803 4.121 1.00 14.35 ? 124 PRO A C 1 ATOM 865 O O . PRO A 1 107 ? -1.345 6.914 3.777 1.00 13.47 ? 124 PRO A O 1 ATOM 866 C CB . PRO A 1 107 ? -0.297 4.882 5.928 1.00 13.98 ? 124 PRO A CB 1 ATOM 867 C CG . PRO A 1 107 ? 0.961 5.666 5.760 1.00 12.49 ? 124 PRO A CG 1 ATOM 868 C CD . PRO A 1 107 ? 1.610 5.119 4.524 1.00 13.91 ? 124 PRO A CD 1 ATOM 869 N N . SER A 1 108 ? -3.029 5.500 4.212 1.00 14.50 ? 125 SER A N 1 ATOM 870 C CA . SER A 1 108 ? -4.065 6.489 3.921 1.00 15.93 ? 125 SER A CA 1 ATOM 871 C C . SER A 1 108 ? -4.340 7.387 5.110 1.00 16.52 ? 125 SER A C 1 ATOM 872 O O . SER A 1 108 ? -5.004 8.397 4.992 1.00 16.84 ? 125 SER A O 1 ATOM 873 C CB . SER A 1 108 ? -5.347 5.752 3.543 1.00 16.41 ? 125 SER A CB 1 ATOM 874 O OG . SER A 1 108 ? -5.678 4.820 4.570 1.00 18.33 ? 125 SER A OG 1 ATOM 875 N N . ASN A 1 109 ? -3.816 7.020 6.272 1.00 16.56 ? 127 ASN A N 1 ATOM 876 C CA . ASN A 1 109 ? -4.099 7.752 7.488 1.00 17.92 ? 127 ASN A CA 1 ATOM 877 C C . ASN A 1 109 ? -3.144 7.265 8.551 1.00 18.23 ? 127 ASN A C 1 ATOM 878 O O . ASN A 1 109 ? -2.673 6.124 8.467 1.00 18.46 ? 127 ASN A O 1 ATOM 879 C CB . ASN A 1 109 ? -5.532 7.498 7.952 1.00 17.64 ? 127 ASN A CB 1 ATOM 880 C CG . ASN A 1 109 ? -5.813 6.034 8.185 1.00 18.49 ? 127 ASN A CG 1 ATOM 881 O OD1 . ASN A 1 109 ? -6.025 5.265 7.247 1.00 18.86 ? 127 ASN A OD1 1 ATOM 882 N ND2 . ASN A 1 109 ? -5.806 5.635 9.447 1.00 19.82 ? 127 ASN A ND2 1 ATOM 883 N N . PRO A 1 110 ? -2.873 8.119 9.553 1.00 19.35 ? 128 PRO A N 1 ATOM 884 C CA . PRO A 1 110 ? -2.065 7.673 10.670 1.00 19.59 ? 128 PRO A CA 1 ATOM 885 C C . PRO A 1 110 ? -2.907 6.761 11.572 1.00 19.84 ? 128 PRO A C 1 ATOM 886 O O . PRO A 1 110 ? -4.135 6.876 11.578 1.00 19.55 ? 128 PRO A O 1 ATOM 887 C CB . PRO A 1 110 ? -1.708 8.971 11.376 1.00 20.26 ? 128 PRO A CB 1 ATOM 888 C CG . PRO A 1 110 ? -2.850 9.880 11.087 1.00 20.59 ? 128 PRO A CG 1 ATOM 889 C CD . PRO A 1 110 ? -3.293 9.522 9.698 1.00 19.14 ? 128 PRO A CD 1 ATOM 890 N N . PRO A 1 111 ? -2.257 5.868 12.332 1.00 19.19 ? 129 PRO A N 1 ATOM 891 C CA . PRO A 1 111 ? -3.011 4.876 13.088 1.00 19.28 ? 129 PRO A CA 1 ATOM 892 C C . PRO A 1 111 ? -3.572 5.433 14.394 1.00 19.29 ? 129 PRO A C 1 ATOM 893 O O . PRO A 1 111 ? -2.956 6.300 15.034 1.00 20.15 ? 129 PRO A O 1 ATOM 894 C CB . PRO A 1 111 ? -1.955 3.821 13.398 1.00 19.17 ? 129 PRO A CB 1 ATOM 895 C CG . PRO A 1 111 ? -0.707 4.621 13.559 1.00 20.10 ? 129 PRO A CG 1 ATOM 896 C CD . PRO A 1 111 ? -0.804 5.730 12.552 1.00 19.77 ? 129 PRO A CD 1 ATOM 897 N N . SER A 1 112 ? -4.725 4.924 14.795 1.00 18.94 ? 131 SER A N 1 ATOM 898 C CA . SER A 1 112 ? -5.295 5.313 16.081 1.00 19.24 ? 131 SER A CA 1 ATOM 899 C C . SER A 1 112 ? -4.475 4.760 17.233 1.00 18.37 ? 131 SER A C 1 ATOM 900 O O . SER A 1 112 ? -3.947 3.656 17.158 1.00 17.99 ? 131 SER A O 1 ATOM 901 C CB . SER A 1 112 ? -6.710 4.774 16.190 1.00 19.66 ? 131 SER A CB 1 ATOM 902 O OG . SER A 1 112 ? -7.520 5.260 15.120 1.00 22.67 ? 131 SER A OG 1 ATOM 903 N N . VAL A 1 113 ? -4.365 5.540 18.305 1.00 17.76 ? 132 VAL A N 1 ATOM 904 C CA . VAL A 1 113 ? -3.855 4.995 19.557 1.00 17.33 ? 132 VAL A CA 1 ATOM 905 C C . VAL A 1 113 ? -4.729 3.799 19.908 1.00 17.15 ? 132 VAL A C 1 ATOM 906 O O . VAL A 1 113 ? -5.957 3.871 19.782 1.00 17.15 ? 132 VAL A O 1 ATOM 907 C CB . VAL A 1 113 ? -3.910 6.048 20.665 1.00 17.36 ? 132 VAL A CB 1 ATOM 908 C CG1 . VAL A 1 113 ? -3.618 5.426 22.015 1.00 17.00 ? 132 VAL A CG1 1 ATOM 909 C CG2 . VAL A 1 113 ? -2.911 7.154 20.351 1.00 17.76 ? 132 VAL A CG2 1 ATOM 910 N N . GLY A 1 114 ? -4.085 2.705 20.319 1.00 16.65 ? 133 GLY A N 1 ATOM 911 C CA . GLY A 1 114 ? -4.772 1.463 20.610 1.00 17.40 ? 133 GLY A CA 1 ATOM 912 C C . GLY A 1 114 ? -4.739 0.443 19.485 1.00 17.28 ? 133 GLY A C 1 ATOM 913 O O . GLY A 1 114 ? -5.017 -0.744 19.719 1.00 17.71 ? 133 GLY A O 1 ATOM 914 N N . SER A 1 115 ? -4.392 0.873 18.267 1.00 17.46 ? 134 SER A N 1 ATOM 915 C CA . SER A 1 115 ? -4.356 -0.046 17.129 1.00 17.96 ? 134 SER A CA 1 ATOM 916 C C . SER A 1 115 ? -3.341 -1.118 17.356 1.00 17.41 ? 134 SER A C 1 ATOM 917 O O . SER A 1 115 ? -2.302 -0.858 17.934 1.00 16.81 ? 134 SER A O 1 ATOM 918 C CB . SER A 1 115 ? -3.989 0.670 15.840 1.00 18.54 ? 134 SER A CB 1 ATOM 919 O OG . SER A 1 115 ? -4.909 1.691 15.606 1.00 22.81 ? 134 SER A OG 1 ATOM 920 N N . VAL A 1 116 ? -3.647 -2.313 16.870 1.00 16.57 ? 135 VAL A N 1 ATOM 921 C CA . VAL A 1 116 ? -2.705 -3.418 16.923 1.00 16.61 ? 135 VAL A CA 1 ATOM 922 C C . VAL A 1 116 ? -1.777 -3.298 15.733 1.00 16.29 ? 135 VAL A C 1 ATOM 923 O O . VAL A 1 116 ? -2.218 -3.083 14.610 1.00 16.38 ? 135 VAL A O 1 ATOM 924 C CB . VAL A 1 116 ? -3.441 -4.774 16.915 1.00 16.85 ? 135 VAL A CB 1 ATOM 925 C CG1 . VAL A 1 116 ? -2.433 -5.921 16.801 1.00 17.48 ? 135 VAL A CG1 1 ATOM 926 C CG2 . VAL A 1 116 ? -4.299 -4.892 18.184 1.00 19.09 ? 135 VAL A CG2 1 ATOM 927 N N . CYS A 1 117 ? -0.484 -3.411 16.002 1.00 15.12 ? 136 CYS A N 1 ATOM 928 C CA . CYS A 1 117 ? 0.519 -3.321 14.955 1.00 14.76 ? 136 CYS A CA 1 ATOM 929 C C . CYS A 1 117 ? 1.414 -4.524 15.009 1.00 15.00 ? 136 CYS A C 1 ATOM 930 O O . CYS A 1 117 ? 1.729 -5.038 16.088 1.00 16.52 ? 136 CYS A O 1 ATOM 931 C CB . CYS A 1 117 ? 1.389 -2.088 15.142 1.00 14.40 ? 136 CYS A CB 1 ATOM 932 S SG . CYS A 1 117 ? 0.480 -0.551 15.320 1.00 17.25 ? 136 CYS A SG 1 ATOM 933 N N . ARG A 1 118 ? 1.847 -4.941 13.837 1.00 14.72 ? 137 ARG A N 1 ATOM 934 C CA . ARG A 1 118 ? 2.839 -5.975 13.717 1.00 14.19 ? 137 ARG A CA 1 ATOM 935 C C . ARG A 1 118 ? 4.205 -5.333 13.663 1.00 14.14 ? 137 ARG A C 1 ATOM 936 O O . ARG A 1 118 ? 4.409 -4.344 12.953 1.00 13.43 ? 137 ARG A O 1 ATOM 937 C CB . ARG A 1 118 ? 2.624 -6.750 12.418 1.00 15.31 ? 137 ARG A CB 1 ATOM 938 C CG . ARG A 1 118 ? 3.361 -8.068 12.371 1.00 17.24 ? 137 ARG A CG 1 ATOM 939 C CD . ARG A 1 118 ? 2.613 -9.071 13.215 1.00 19.82 ? 137 ARG A CD 1 ATOM 940 N NE . ARG A 1 118 ? 2.874 -10.452 12.823 1.00 20.97 ? 137 ARG A NE 1 ATOM 941 C CZ . ARG A 1 118 ? 2.659 -11.485 13.629 1.00 22.81 ? 137 ARG A CZ 1 ATOM 942 N NH1 . ARG A 1 118 ? 2.214 -11.272 14.872 1.00 21.49 ? 137 ARG A NH1 1 ATOM 943 N NH2 . ARG A 1 118 ? 2.928 -12.725 13.215 1.00 20.35 ? 137 ARG A NH2 1 ATOM 944 N N . ILE A 1 119 ? 5.144 -5.900 14.412 1.00 13.43 ? 138 ILE A N 1 ATOM 945 C CA . ILE A 1 119 ? 6.545 -5.532 14.254 1.00 13.26 ? 138 ILE A CA 1 ATOM 946 C C . ILE A 1 119 ? 7.287 -6.768 13.802 1.00 13.81 ? 138 ILE A C 1 ATOM 947 O O . ILE A 1 119 ? 6.803 -7.895 13.972 1.00 14.01 ? 138 ILE A O 1 ATOM 948 C CB . ILE A 1 119 ? 7.161 -5.006 15.556 1.00 13.63 ? 138 ILE A CB 1 ATOM 949 C CG1 . ILE A 1 119 ? 6.795 -5.916 16.731 1.00 13.55 ? 138 ILE A CG1 1 ATOM 950 C CG2 . ILE A 1 119 ? 6.694 -3.559 15.800 1.00 14.18 ? 138 ILE A CG2 1 ATOM 951 C CD1 . ILE A 1 119 ? 7.671 -5.654 17.965 1.00 13.67 ? 138 ILE A CD1 1 ATOM 952 N N . MET A 1 120 ? 8.427 -6.555 13.167 1.00 13.60 ? 139 MET A N 1 ATOM 953 C CA . MET A 1 120 ? 9.140 -7.660 12.529 1.00 14.24 ? 139 MET A CA 1 ATOM 954 C C . MET A 1 120 ? 10.563 -7.274 12.256 1.00 13.59 ? 139 MET A C 1 ATOM 955 O O . MET A 1 120 ? 10.862 -6.117 11.953 1.00 13.44 ? 139 MET A O 1 ATOM 956 C CB . MET A 1 120 ? 8.478 -8.043 11.207 1.00 13.77 ? 139 MET A CB 1 ATOM 957 C CG . MET A 1 120 ? 8.341 -6.879 10.210 1.00 15.35 ? 139 MET A CG 1 ATOM 958 S SD . MET A 1 120 ? 7.367 -7.334 8.780 1.00 16.15 ? 139 MET A SD 1 ATOM 959 C CE . MET A 1 120 ? 5.738 -7.474 9.518 1.00 20.24 ? 139 MET A CE 1 ATOM 960 N N . GLY A 1 121 ? 11.442 -8.262 12.330 1.00 13.37 ? 140 GLY A N 1 ATOM 961 C CA . GLY A 1 121 ? 12.796 -8.044 11.919 1.00 13.26 ? 140 GLY A CA 1 ATOM 962 C C . GLY A 1 121 ? 13.690 -9.204 12.270 1.00 13.93 ? 140 GLY A C 1 ATOM 963 O O . GLY A 1 121 ? 13.267 -10.188 12.903 1.00 14.14 ? 140 GLY A O 1 ATOM 964 N N . TRP A 1 122 ? 14.933 -9.079 11.824 1.00 14.49 ? 141 TRP A N 1 ATOM 965 C CA . TRP A 1 122 ? 15.943 -10.073 12.121 1.00 14.51 ? 141 TRP A CA 1 ATOM 966 C C . TRP A 1 122 ? 16.792 -9.634 13.307 1.00 15.26 ? 141 TRP A C 1 ATOM 967 O O . TRP A 1 122 ? 17.854 -10.191 13.574 1.00 15.37 ? 141 TRP A O 1 ATOM 968 C CB . TRP A 1 122 ? 16.811 -10.282 10.901 1.00 14.63 ? 141 TRP A CB 1 ATOM 969 C CG . TRP A 1 122 ? 16.145 -11.002 9.777 1.00 14.66 ? 141 TRP A CG 1 ATOM 970 C CD1 . TRP A 1 122 ? 16.148 -12.347 9.549 1.00 15.46 ? 141 TRP A CD1 1 ATOM 971 C CD2 . TRP A 1 122 ? 15.440 -10.406 8.672 1.00 14.12 ? 141 TRP A CD2 1 ATOM 972 N NE1 . TRP A 1 122 ? 15.481 -12.632 8.368 1.00 15.99 ? 141 TRP A NE1 1 ATOM 973 C CE2 . TRP A 1 122 ? 15.033 -11.458 7.819 1.00 15.04 ? 141 TRP A CE2 1 ATOM 974 C CE3 . TRP A 1 122 ? 15.120 -9.077 8.319 1.00 13.26 ? 141 TRP A CE3 1 ATOM 975 C CZ2 . TRP A 1 122 ? 14.329 -11.234 6.639 1.00 15.90 ? 141 TRP A CZ2 1 ATOM 976 C CZ3 . TRP A 1 122 ? 14.411 -8.856 7.153 1.00 14.96 ? 141 TRP A CZ3 1 ATOM 977 C CH2 . TRP A 1 122 ? 14.021 -9.931 6.326 1.00 15.17 ? 141 TRP A CH2 1 ATOM 978 N N . GLY A 1 123 ? 16.298 -8.646 14.043 1.00 15.14 ? 142 GLY A N 1 ATOM 979 C CA . GLY A 1 123 ? 17.026 -8.133 15.190 1.00 15.37 ? 142 GLY A CA 1 ATOM 980 C C . GLY A 1 123 ? 17.058 -9.114 16.337 1.00 15.62 ? 142 GLY A C 1 ATOM 981 O O . GLY A 1 123 ? 16.434 -10.180 16.312 1.00 14.96 ? 142 GLY A O 1 ATOM 982 N N . THR A 1 124 ? 17.801 -8.747 17.363 1.00 15.56 ? 143 THR A N 1 ATOM 983 C CA . THR A 1 124 ? 17.935 -9.643 18.508 1.00 16.10 ? 143 THR A CA 1 ATOM 984 C C . THR A 1 124 ? 16.600 -10.014 19.123 1.00 16.43 ? 143 THR A C 1 ATOM 985 O O . THR A 1 124 ? 15.681 -9.198 19.203 1.00 15.88 ? 143 THR A O 1 ATOM 986 C CB . THR A 1 124 ? 18.870 -9.061 19.589 1.00 16.47 ? 143 THR A CB 1 ATOM 987 O OG1 . THR A 1 124 ? 19.017 -10.021 20.643 1.00 18.19 ? 143 THR A OG1 1 ATOM 988 C CG2 . THR A 1 124 ? 18.320 -7.771 20.162 1.00 15.97 ? 143 THR A CG2 1 ATOM 989 N N . ILE A 1 125 ? 16.507 -11.263 19.553 1.00 16.99 ? 144 ILE A N 1 ATOM 990 C CA . ILE A 1 125 ? 15.318 -11.750 20.224 1.00 17.89 ? 144 ILE A CA 1 ATOM 991 C C . ILE A 1 125 ? 15.529 -11.789 21.738 1.00 18.60 ? 144 ILE A C 1 ATOM 992 O O . ILE A 1 125 ? 14.642 -12.180 22.480 1.00 19.41 ? 144 ILE A O 1 ATOM 993 C CB . ILE A 1 125 ? 14.863 -13.121 19.691 1.00 18.64 ? 144 ILE A CB 1 ATOM 994 C CG1 . ILE A 1 125 ? 15.929 -14.201 19.947 1.00 19.56 ? 144 ILE A CG1 1 ATOM 995 C CG2 . ILE A 1 125 ? 14.527 -13.008 18.207 1.00 17.92 ? 144 ILE A CG2 1 ATOM 996 C CD1 . ILE A 1 125 ? 15.416 -15.601 19.712 1.00 19.98 ? 144 ILE A CD1 1 ATOM 997 N N . THR A 1 126 ? 16.711 -11.370 22.171 1.00 19.03 ? 145 THR A N 1 ATOM 998 C CA . THR A 1 126 ? 17.009 -11.215 23.590 1.00 19.98 ? 145 THR A CA 1 ATOM 999 C C . THR A 1 126 ? 17.617 -9.859 23.833 1.00 19.76 ? 145 THR A C 1 ATOM 1000 O O . THR A 1 126 ? 18.286 -9.291 22.966 1.00 19.52 ? 145 THR A O 1 ATOM 1001 C CB . THR A 1 126 ? 17.986 -12.277 24.107 1.00 19.55 ? 145 THR A CB 1 ATOM 1002 O OG1 . THR A 1 126 ? 19.207 -12.190 23.367 1.00 20.55 ? 145 THR A OG1 1 ATOM 1003 C CG2 . THR A 1 126 ? 17.382 -13.683 23.989 1.00 20.53 ? 145 THR A CG2 1 ATOM 1004 N N . SER A 1 127 ? 17.358 -9.326 25.021 1.00 20.95 ? 146 SER A N 1 ATOM 1005 C CA . SER A 1 127 ? 17.878 -8.036 25.427 1.00 22.24 ? 146 SER A CA 1 ATOM 1006 C C . SER A 1 127 ? 17.876 -8.007 26.948 1.00 23.32 ? 146 SER A C 1 ATOM 1007 O O . SER A 1 127 ? 16.842 -8.233 27.562 1.00 23.33 ? 146 SER A O 1 ATOM 1008 C CB . SER A 1 127 ? 17.012 -6.897 24.902 1.00 22.21 ? 146 SER A CB 1 ATOM 1009 O OG . SER A 1 127 ? 17.593 -5.649 25.242 1.00 21.42 ? 146 SER A OG 1 ATOM 1010 N N . PRO A 1 128 ? 19.036 -7.735 27.562 1.00 24.59 ? 147 PRO A N 1 ATOM 1011 C CA . PRO A 1 128 ? 20.325 -7.453 26.957 1.00 25.37 ? 147 PRO A CA 1 ATOM 1012 C C . PRO A 1 128 ? 20.952 -8.711 26.338 1.00 26.05 ? 147 PRO A C 1 ATOM 1013 O O . PRO A 1 128 ? 20.405 -9.809 26.479 1.00 26.53 ? 147 PRO A O 1 ATOM 1014 C CB . PRO A 1 128 ? 21.155 -6.967 28.146 1.00 25.63 ? 147 PRO A CB 1 ATOM 1015 C CG . PRO A 1 128 ? 20.555 -7.597 29.323 1.00 25.54 ? 147 PRO A CG 1 ATOM 1016 C CD . PRO A 1 128 ? 19.096 -7.730 29.035 1.00 25.29 ? 147 PRO A CD 1 ATOM 1017 N N . ASN A 1 129 ? 22.085 -8.534 25.658 1.00 27.22 ? 148 ASN A N 1 ATOM 1018 C CA . ASN A 1 129 ? 22.845 -9.621 25.026 1.00 28.59 ? 148 ASN A CA 1 ATOM 1019 C C . ASN A 1 129 ? 22.181 -10.103 23.751 1.00 28.76 ? 148 ASN A C 1 ATOM 1020 O O . ASN A 1 129 ? 21.074 -10.640 23.773 1.00 30.37 ? 148 ASN A O 1 ATOM 1021 C CB . ASN A 1 129 ? 23.107 -10.793 25.983 1.00 29.74 ? 148 ASN A CB 1 ATOM 1022 C CG . ASN A 1 129 ? 23.647 -10.344 27.328 1.00 33.63 ? 148 ASN A CG 1 ATOM 1023 O OD1 . ASN A 1 129 ? 23.060 -10.663 28.374 1.00 38.33 ? 148 ASN A OD1 1 ATOM 1024 N ND2 . ASN A 1 129 ? 24.737 -9.563 27.309 1.00 35.78 ? 148 ASN A ND2 1 ATOM 1025 N N . ALA A 1 130 ? 22.879 -9.921 22.641 1.00 27.75 ? 149 ALA A N 1 ATOM 1026 C CA . ALA A 1 130 ? 22.315 -10.183 21.323 1.00 26.82 ? 149 ALA A CA 1 ATOM 1027 C C . ALA A 1 130 ? 22.118 -11.669 21.055 1.00 26.17 ? 149 ALA A C 1 ATOM 1028 O O . ALA A 1 130 ? 22.993 -12.493 21.329 1.00 26.74 ? 149 ALA A O 1 ATOM 1029 C CB . ALA A 1 130 ? 23.186 -9.559 20.260 1.00 27.16 ? 149 ALA A CB 1 ATOM 1030 N N . THR A 1 131 ? 20.942 -12.006 20.540 1.00 24.31 ? 150 THR A N 1 ATOM 1031 C CA . THR A 1 131 ? 20.665 -13.322 19.998 1.00 23.13 ? 150 THR A CA 1 ATOM 1032 C C . THR A 1 131 ? 19.973 -13.091 18.671 1.00 22.22 ? 150 THR A C 1 ATOM 1033 O O . THR A 1 131 ? 18.795 -12.790 18.632 1.00 21.60 ? 150 THR A O 1 ATOM 1034 C CB . THR A 1 131 ? 19.774 -14.132 20.927 1.00 24.02 ? 150 THR A CB 1 ATOM 1035 O OG1 . THR A 1 131 ? 20.430 -14.267 22.199 1.00 25.14 ? 150 THR A OG1 1 ATOM 1036 C CG2 . THR A 1 131 ? 19.474 -15.507 20.330 1.00 25.08 ? 150 THR A CG2 1 ATOM 1037 N N . LEU A 1 132 ? 20.730 -13.200 17.589 1.00 21.63 ? 151 LEU A N 1 ATOM 1038 C CA . LEU A 1 132 ? 20.180 -12.938 16.268 1.00 20.77 ? 151 LEU A CA 1 ATOM 1039 C C . LEU A 1 132 ? 19.555 -14.204 15.682 1.00 20.84 ? 151 LEU A C 1 ATOM 1040 O O . LEU A 1 132 ? 20.237 -15.240 15.552 1.00 21.26 ? 151 LEU A O 1 ATOM 1041 C CB . LEU A 1 132 ? 21.276 -12.406 15.348 1.00 20.82 ? 151 LEU A CB 1 ATOM 1042 C CG . LEU A 1 132 ? 21.930 -11.083 15.754 1.00 21.63 ? 151 LEU A CG 1 ATOM 1043 C CD1 . LEU A 1 132 ? 23.009 -10.685 14.776 1.00 22.92 ? 151 LEU A CD1 1 ATOM 1044 C CD2 . LEU A 1 132 ? 20.885 -9.965 15.907 1.00 22.87 ? 151 LEU A CD2 1 ATOM 1045 N N . PRO A 1 133 ? 18.262 -14.135 15.313 1.00 20.04 ? 152 PRO A N 1 ATOM 1046 C CA . PRO A 1 133 ? 17.530 -15.268 14.742 1.00 19.54 ? 152 PRO A CA 1 ATOM 1047 C C . PRO A 1 133 ? 17.909 -15.481 13.272 1.00 19.52 ? 152 PRO A C 1 ATOM 1048 O O . PRO A 1 133 ? 18.403 -14.558 12.612 1.00 19.16 ? 152 PRO A O 1 ATOM 1049 C CB . PRO A 1 133 ? 16.072 -14.827 14.842 1.00 19.32 ? 152 PRO A CB 1 ATOM 1050 C CG . PRO A 1 133 ? 16.138 -13.325 14.699 1.00 19.73 ? 152 PRO A CG 1 ATOM 1051 C CD . PRO A 1 133 ? 17.410 -12.930 15.419 1.00 19.87 ? 152 PRO A CD 1 ATOM 1052 N N . ASP A 1 134 ? 17.700 -16.700 12.785 1.00 19.09 ? 153 ASP A N 1 ATOM 1053 C CA . ASP A 1 134 ? 17.905 -16.998 11.372 1.00 19.47 ? 153 ASP A CA 1 ATOM 1054 C C . ASP A 1 134 ? 16.697 -16.594 10.555 1.00 18.60 ? 153 ASP A C 1 ATOM 1055 O O . ASP A 1 134 ? 16.790 -16.416 9.351 1.00 18.95 ? 153 ASP A O 1 ATOM 1056 C CB . ASP A 1 134 ? 18.118 -18.490 11.168 1.00 20.59 ? 153 ASP A CB 1 ATOM 1057 C CG . ASP A 1 134 ? 19.345 -19.005 11.873 1.00 23.17 ? 153 ASP A CG 1 ATOM 1058 O OD1 . ASP A 1 134 ? 20.307 -18.229 12.081 1.00 26.42 ? 153 ASP A OD1 1 ATOM 1059 O OD2 . ASP A 1 134 ? 19.346 -20.217 12.168 1.00 28.48 ? 153 ASP A OD2 1 ATOM 1060 N N . VAL A 1 135 ? 15.563 -16.448 11.227 1.00 17.43 ? 154 VAL A N 1 ATOM 1061 C CA . VAL A 1 135 ? 14.313 -16.099 10.573 1.00 16.90 ? 154 VAL A CA 1 ATOM 1062 C C . VAL A 1 135 ? 13.823 -14.824 11.231 1.00 16.53 ? 154 VAL A C 1 ATOM 1063 O O . VAL A 1 135 ? 14.111 -14.589 12.411 1.00 16.32 ? 154 VAL A O 1 ATOM 1064 C CB . VAL A 1 135 ? 13.271 -17.202 10.731 1.00 17.66 ? 154 VAL A CB 1 ATOM 1065 C CG1 . VAL A 1 135 ? 13.665 -18.401 9.893 1.00 17.59 ? 154 VAL A CG1 1 ATOM 1066 C CG2 . VAL A 1 135 ? 13.148 -17.615 12.212 1.00 17.44 ? 154 VAL A CG2 1 ATOM 1067 N N . PRO A 1 136 ? 13.062 -14.015 10.489 1.00 15.94 ? 155 PRO A N 1 ATOM 1068 C CA . PRO A 1 136 ? 12.609 -12.792 11.147 1.00 15.54 ? 155 PRO A CA 1 ATOM 1069 C C . PRO A 1 136 ? 11.571 -13.172 12.187 1.00 15.29 ? 155 PRO A C 1 ATOM 1070 O O . PRO A 1 136 ? 10.799 -14.121 11.989 1.00 16.12 ? 155 PRO A O 1 ATOM 1071 C CB . PRO A 1 136 ? 11.990 -11.985 10.002 1.00 15.17 ? 155 PRO A CB 1 ATOM 1072 C CG . PRO A 1 136 ? 11.547 -13.013 9.005 1.00 15.96 ? 155 PRO A CG 1 ATOM 1073 C CD . PRO A 1 136 ? 12.530 -14.164 9.128 1.00 15.92 ? 155 PRO A CD 1 ATOM 1074 N N . HIS A 1 137 ? 11.553 -12.437 13.288 1.00 15.36 ? 156 HIS A N 1 ATOM 1075 C CA . HIS A 1 137 ? 10.542 -12.638 14.304 1.00 15.09 ? 156 HIS A CA 1 ATOM 1076 C C . HIS A 1 137 ? 9.536 -11.511 14.219 1.00 15.28 ? 156 HIS A C 1 ATOM 1077 O O . HIS A 1 137 ? 9.856 -10.401 13.779 1.00 14.73 ? 156 HIS A O 1 ATOM 1078 C CB . HIS A 1 137 ? 11.178 -12.692 15.686 1.00 15.03 ? 156 HIS A CB 1 ATOM 1079 C CG . HIS A 1 137 ? 11.759 -14.034 16.010 1.00 16.49 ? 156 HIS A CG 1 ATOM 1080 N ND1 . HIS A 1 137 ? 11.560 -14.658 17.225 1.00 20.03 ? 156 HIS A ND1 1 ATOM 1081 C CD2 . HIS A 1 137 ? 12.497 -14.888 15.262 1.00 18.88 ? 156 HIS A CD2 1 ATOM 1082 C CE1 . HIS A 1 137 ? 12.164 -15.834 17.216 1.00 21.34 ? 156 HIS A CE1 1 ATOM 1083 N NE2 . HIS A 1 137 ? 12.736 -16.000 16.035 1.00 18.90 ? 156 HIS A NE2 1 ATOM 1084 N N . CYS A 1 138 ? 8.319 -11.836 14.614 1.00 14.97 ? 157 CYS A N 1 ATOM 1085 C CA . CYS A 1 138 ? 7.180 -10.945 14.500 1.00 15.56 ? 157 CYS A CA 1 ATOM 1086 C C . CYS A 1 138 ? 6.482 -10.933 15.831 1.00 15.20 ? 157 CYS A C 1 ATOM 1087 O O . CYS A 1 138 ? 6.420 -11.953 16.529 1.00 15.73 ? 157 CYS A O 1 ATOM 1088 C CB . CYS A 1 138 ? 6.199 -11.497 13.461 1.00 16.45 ? 157 CYS A CB 1 ATOM 1089 S SG . CYS A 1 138 ? 6.585 -11.047 11.758 1.00 19.05 ? 157 CYS A SG 1 ATOM 1090 N N . ALA A 1 139 ? 5.913 -9.792 16.177 1.00 13.95 ? 158 ALA A N 1 ATOM 1091 C CA . ALA A 1 139 ? 5.054 -9.714 17.348 1.00 13.92 ? 158 ALA A CA 1 ATOM 1092 C C . ALA A 1 139 ? 3.986 -8.666 17.101 1.00 15.15 ? 158 ALA A C 1 ATOM 1093 O O . ALA A 1 139 ? 4.124 -7.831 16.214 1.00 13.85 ? 158 ALA A O 1 ATOM 1094 C CB . ALA A 1 139 ? 5.863 -9.358 18.587 1.00 14.04 ? 158 ALA A CB 1 ATOM 1095 N N . ASN A 1 140 ? 2.922 -8.731 17.903 1.00 14.99 ? 159 ASN A N 1 ATOM 1096 C CA . ASN A 1 140 ? 1.895 -7.709 17.899 1.00 16.10 ? 159 ASN A CA 1 ATOM 1097 C C . ASN A 1 140 ? 2.102 -6.783 19.059 1.00 16.14 ? 159 ASN A C 1 ATOM 1098 O O . ASN A 1 140 ? 2.268 -7.214 20.205 1.00 16.58 ? 159 ASN A O 1 ATOM 1099 C CB . ASN A 1 140 ? 0.515 -8.341 18.018 1.00 17.00 ? 159 ASN A CB 1 ATOM 1100 C CG . ASN A 1 140 ? 0.186 -9.187 16.826 1.00 18.86 ? 159 ASN A CG 1 ATOM 1101 O OD1 . ASN A 1 140 ? 0.621 -8.893 15.726 1.00 20.88 ? 159 ASN A OD1 1 ATOM 1102 N ND2 . ASN A 1 140 ? -0.571 -10.256 17.039 1.00 23.00 ? 159 ASN A ND2 1 ATOM 1103 N N . ILE A 1 141 ? 2.068 -5.499 18.752 1.00 15.49 ? 160 ILE A N 1 ATOM 1104 C CA . ILE A 1 141 ? 2.182 -4.477 19.777 1.00 14.58 ? 160 ILE A CA 1 ATOM 1105 C C . ILE A 1 141 ? 1.049 -3.496 19.499 1.00 15.07 ? 160 ILE A C 1 ATOM 1106 O O . ILE A 1 141 ? 0.214 -3.757 18.648 1.00 15.53 ? 160 ILE A O 1 ATOM 1107 C CB . ILE A 1 141 ? 3.578 -3.804 19.795 1.00 15.12 ? 160 ILE A CB 1 ATOM 1108 C CG1 . ILE A 1 141 ? 3.885 -3.110 18.451 1.00 14.03 ? 160 ILE A CG1 1 ATOM 1109 C CG2 . ILE A 1 141 ? 4.669 -4.835 20.172 1.00 13.37 ? 160 ILE A CG2 1 ATOM 1110 C CD1 . ILE A 1 141 ? 5.080 -2.226 18.494 1.00 14.71 ? 160 ILE A CD1 1 ATOM 1111 N N . ASN A 1 142 ? 1.025 -2.379 20.208 1.00 14.85 ? 161 ASN A N 1 ATOM 1112 C CA . ASN A 1 142 ? -0.025 -1.406 19.988 1.00 15.38 ? 161 ASN A CA 1 ATOM 1113 C C . ASN A 1 142 ? 0.523 -0.030 19.802 1.00 14.60 ? 161 ASN A C 1 ATOM 1114 O O . ASN A 1 142 ? 1.608 0.286 20.292 1.00 15.26 ? 161 ASN A O 1 ATOM 1115 C CB . ASN A 1 142 ? -0.958 -1.350 21.196 1.00 16.94 ? 161 ASN A CB 1 ATOM 1116 C CG . ASN A 1 142 ? -1.722 -2.639 21.394 1.00 19.30 ? 161 ASN A CG 1 ATOM 1117 O OD1 . ASN A 1 142 ? -2.794 -2.842 20.811 1.00 25.11 ? 161 ASN A OD1 1 ATOM 1118 N ND2 . ASN A 1 142 ? -1.185 -3.504 22.226 1.00 21.67 ? 161 ASN A ND2 1 ATOM 1119 N N . ILE A 1 143 ? -0.250 0.823 19.139 1.00 13.99 ? 162 ILE A N 1 ATOM 1120 C CA . ILE A 1 143 ? 0.048 2.245 19.163 1.00 13.75 ? 162 ILE A CA 1 ATOM 1121 C C . ILE A 1 143 ? -0.308 2.724 20.549 1.00 14.34 ? 162 ILE A C 1 ATOM 1122 O O . ILE A 1 143 ? -1.430 2.508 21.032 1.00 15.11 ? 162 ILE A O 1 ATOM 1123 C CB . ILE A 1 143 ? -0.774 3.053 18.152 1.00 13.80 ? 162 ILE A CB 1 ATOM 1124 C CG1 . ILE A 1 143 ? -0.495 2.570 16.728 1.00 14.21 ? 162 ILE A CG1 1 ATOM 1125 C CG2 . ILE A 1 143 ? -0.443 4.515 18.282 1.00 14.96 ? 162 ILE A CG2 1 ATOM 1126 C CD1 . ILE A 1 143 ? 0.956 2.773 16.209 1.00 14.47 ? 162 ILE A CD1 1 ATOM 1127 N N . LEU A 1 144 ? 0.674 3.330 21.197 1.00 14.26 ? 163 LEU A N 1 ATOM 1128 C CA . LEU A 1 144 ? 0.491 3.834 22.525 1.00 15.58 ? 163 LEU A CA 1 ATOM 1129 C C . LEU A 1 144 ? 0.302 5.328 22.506 1.00 16.84 ? 163 LEU A C 1 ATOM 1130 O O . LEU A 1 144 ? 0.705 6.025 21.564 1.00 16.54 ? 163 LEU A O 1 ATOM 1131 C CB . LEU A 1 144 ? 1.682 3.463 23.413 1.00 15.43 ? 163 LEU A CB 1 ATOM 1132 C CG . LEU A 1 144 ? 2.012 1.971 23.524 1.00 14.65 ? 163 LEU A CG 1 ATOM 1133 C CD1 . LEU A 1 144 ? 3.218 1.831 24.423 1.00 16.31 ? 163 LEU A CD1 1 ATOM 1134 C CD2 . LEU A 1 144 ? 0.839 1.122 24.032 1.00 15.08 ? 163 LEU A CD2 1 ATOM 1135 N N . ASP A 1 145 ? -0.333 5.820 23.562 1.00 17.56 ? 164 ASP A N 1 ATOM 1136 C CA . ASP A 1 145 ? -0.426 7.233 23.795 1.00 19.56 ? 164 ASP A CA 1 ATOM 1137 C C . ASP A 1 145 ? 0.996 7.797 23.713 1.00 20.00 ? 164 ASP A C 1 ATOM 1138 O O . ASP A 1 145 ? 1.924 7.288 24.343 1.00 20.08 ? 164 ASP A O 1 ATOM 1139 C CB . ASP A 1 145 ? -1.006 7.449 25.191 1.00 20.06 ? 164 ASP A CB 1 ATOM 1140 C CG . ASP A 1 145 ? -1.294 8.889 25.488 1.00 23.68 ? 164 ASP A CG 1 ATOM 1141 O OD1 . ASP A 1 145 ? -2.151 9.118 26.365 1.00 26.94 ? 164 ASP A OD1 1 ATOM 1142 O OD2 . ASP A 1 145 ? -0.688 9.790 24.868 1.00 23.71 ? 164 ASP A OD2 1 ATOM 1143 N N . TYR A 1 146 ? 1.174 8.838 22.917 1.00 20.61 ? 165 TYR A N 1 ATOM 1144 C CA . TYR A 1 146 ? 2.498 9.392 22.695 1.00 21.13 ? 165 TYR A CA 1 ATOM 1145 C C . TYR A 1 146 ? 3.150 9.846 23.992 1.00 21.17 ? 165 TYR A C 1 ATOM 1146 O O . TYR A 1 146 ? 4.377 9.836 24.122 1.00 20.03 ? 165 TYR A O 1 ATOM 1147 C CB . TYR A 1 146 ? 2.390 10.546 21.715 1.00 22.49 ? 165 TYR A CB 1 ATOM 1148 C CG . TYR A 1 146 ? 3.706 10.965 21.172 1.00 24.61 ? 165 TYR A CG 1 ATOM 1149 C CD1 . TYR A 1 146 ? 4.398 10.138 20.291 1.00 24.72 ? 165 TYR A CD1 1 ATOM 1150 C CD2 . TYR A 1 146 ? 4.262 12.192 21.525 1.00 26.30 ? 165 TYR A CD2 1 ATOM 1151 C CE1 . TYR A 1 146 ? 5.604 10.508 19.779 1.00 26.85 ? 165 TYR A CE1 1 ATOM 1152 C CE2 . TYR A 1 146 ? 5.483 12.577 21.015 1.00 28.72 ? 165 TYR A CE2 1 ATOM 1153 C CZ . TYR A 1 146 ? 6.148 11.721 20.137 1.00 28.01 ? 165 TYR A CZ 1 ATOM 1154 O OH . TYR A 1 146 ? 7.366 12.081 19.613 1.00 29.65 ? 165 TYR A OH 1 ATOM 1155 N N . ALA A 1 147 ? 2.309 10.218 24.958 1.00 20.79 ? 166 ALA A N 1 ATOM 1156 C CA . ALA A 1 147 ? 2.780 10.691 26.250 1.00 21.20 ? 166 ALA A CA 1 ATOM 1157 C C . ALA A 1 147 ? 3.570 9.617 26.964 1.00 21.23 ? 166 ALA A C 1 ATOM 1158 O O . ALA A 1 147 ? 4.422 9.914 27.800 1.00 21.56 ? 166 ALA A O 1 ATOM 1159 C CB . ALA A 1 147 ? 1.603 11.149 27.109 1.00 21.16 ? 166 ALA A CB 1 ATOM 1160 N N . VAL A 1 148 ? 3.297 8.357 26.632 1.00 21.68 ? 167 VAL A N 1 ATOM 1161 C CA . VAL A 1 148 ? 4.048 7.263 27.203 1.00 21.22 ? 167 VAL A CA 1 ATOM 1162 C C . VAL A 1 148 ? 5.509 7.354 26.776 1.00 22.12 ? 167 VAL A C 1 ATOM 1163 O O . VAL A 1 148 ? 6.406 7.260 27.614 1.00 22.57 ? 167 VAL A O 1 ATOM 1164 C CB . VAL A 1 148 ? 3.443 5.890 26.834 1.00 21.27 ? 167 VAL A CB 1 ATOM 1165 C CG1 . VAL A 1 148 ? 4.334 4.755 27.340 1.00 20.70 ? 167 VAL A CG1 1 ATOM 1166 C CG2 . VAL A 1 148 ? 2.023 5.770 27.407 1.00 21.16 ? 167 VAL A CG2 1 ATOM 1167 N N . CYS A 1 149 ? 5.745 7.559 25.482 1.00 22.13 ? 168 CYS A N 1 ATOM 1168 C CA . CYS A 1 149 ? 7.102 7.710 24.981 1.00 22.48 ? 168 CYS A CA 1 ATOM 1169 C C . CYS A 1 149 ? 7.736 9.002 25.481 1.00 23.54 ? 168 CYS A C 1 ATOM 1170 O O . CYS A 1 149 ? 8.934 9.045 25.732 1.00 23.82 ? 168 CYS A O 1 ATOM 1171 C CB . CYS A 1 149 ? 7.125 7.673 23.460 1.00 22.86 ? 168 CYS A CB 1 ATOM 1172 S SG . CYS A 1 149 ? 7.034 5.996 22.840 1.00 22.31 ? 168 CYS A SG 1 ATOM 1173 N N . GLN A 1 150 ? 6.930 10.047 25.611 1.00 24.28 ? 169 GLN A N 1 ATOM 1174 C CA . GLN A 1 150 ? 7.423 11.334 26.092 1.00 25.92 ? 169 GLN A CA 1 ATOM 1175 C C . GLN A 1 150 ? 7.916 11.197 27.518 1.00 26.64 ? 169 GLN A C 1 ATOM 1176 O O . GLN A 1 150 ? 8.918 11.798 27.887 1.00 27.61 ? 169 GLN A O 1 ATOM 1177 C CB . GLN A 1 150 ? 6.330 12.396 26.016 1.00 25.48 ? 169 GLN A CB 1 ATOM 1178 C CG . GLN A 1 150 ? 6.043 12.876 24.629 1.00 26.43 ? 169 GLN A CG 1 ATOM 1179 C CD . GLN A 1 150 ? 4.924 13.891 24.616 1.00 27.90 ? 169 GLN A CD 1 ATOM 1180 O OE1 . GLN A 1 150 ? 3.851 13.642 25.162 1.00 27.78 ? 169 GLN A OE1 1 ATOM 1181 N NE2 . GLN A 1 150 ? 5.170 15.048 24.003 1.00 28.24 ? 169 GLN A NE2 1 ATOM 1182 N N . ALA A 1 151 ? 7.209 10.400 28.318 1.00 27.93 ? 170 ALA A N 1 ATOM 1183 C CA . ALA A 1 151 ? 7.576 10.190 29.714 1.00 28.31 ? 170 ALA A CA 1 ATOM 1184 C C . ALA A 1 151 ? 8.827 9.318 29.831 1.00 29.01 ? 170 ALA A C 1 ATOM 1185 O O . ALA A 1 151 ? 9.659 9.515 30.725 1.00 29.65 ? 170 ALA A O 1 ATOM 1186 C CB . ALA A 1 151 ? 6.425 9.566 30.478 1.00 28.44 ? 170 ALA A CB 1 ATOM 1187 N N . ALA A 1 152 ? 8.955 8.354 28.924 1.00 28.34 ? 171 ALA A N 1 ATOM 1188 C CA . ALA A 1 152 ? 10.052 7.398 28.951 1.00 28.24 ? 171 ALA A CA 1 ATOM 1189 C C . ALA A 1 152 ? 11.353 7.972 28.395 1.00 28.09 ? 171 ALA A C 1 ATOM 1190 O O . ALA A 1 152 ? 12.443 7.546 28.789 1.00 28.73 ? 171 ALA A O 1 ATOM 1191 C CB . ALA A 1 152 ? 9.671 6.159 28.160 1.00 28.11 ? 171 ALA A CB 1 ATOM 1192 N N . TYR A 1 153 ? 11.253 8.908 27.461 1.00 27.90 ? 172 TYR A N 1 ATOM 1193 C CA . TYR A 1 153 ? 12.445 9.309 26.713 1.00 28.10 ? 172 TYR A CA 1 ATOM 1194 C C . TYR A 1 153 ? 12.806 10.797 26.776 1.00 29.34 ? 172 TYR A C 1 ATOM 1195 O O . TYR A 1 153 ? 11.953 11.651 27.014 1.00 30.39 ? 172 TYR A O 1 ATOM 1196 C CB . TYR A 1 153 ? 12.369 8.795 25.271 1.00 26.79 ? 172 TYR A CB 1 ATOM 1197 C CG . TYR A 1 153 ? 12.211 7.287 25.198 1.00 25.06 ? 172 TYR A CG 1 ATOM 1198 C CD1 . TYR A 1 153 ? 13.114 6.436 25.844 1.00 24.59 ? 172 TYR A CD1 1 ATOM 1199 C CD2 . TYR A 1 153 ? 11.148 6.710 24.505 1.00 23.51 ? 172 TYR A CD2 1 ATOM 1200 C CE1 . TYR A 1 153 ? 12.968 5.049 25.793 1.00 22.33 ? 172 TYR A CE1 1 ATOM 1201 C CE2 . TYR A 1 153 ? 10.994 5.331 24.446 1.00 22.07 ? 172 TYR A CE2 1 ATOM 1202 C CZ . TYR A 1 153 ? 11.901 4.504 25.081 1.00 23.69 ? 172 TYR A CZ 1 ATOM 1203 O OH . TYR A 1 153 ? 11.757 3.137 25.019 1.00 22.95 ? 172 TYR A OH 1 ATOM 1204 N N . LYS A 1 154 ? 14.089 11.072 26.589 1.00 30.47 ? 174 LYS A N 1 ATOM 1205 C CA . LYS A 1 154 ? 14.603 12.433 26.601 1.00 31.89 ? 174 LYS A CA 1 ATOM 1206 C C . LYS A 1 154 ? 14.220 13.203 25.348 1.00 31.98 ? 174 LYS A C 1 ATOM 1207 O O . LYS A 1 154 ? 13.086 13.653 25.219 1.00 33.36 ? 174 LYS A O 1 ATOM 1208 C CB . LYS A 1 154 ? 16.117 12.430 26.870 1.00 32.12 ? 174 LYS A CB 1 ATOM 1209 C CG . LYS A 1 154 ? 16.527 12.534 28.354 0.50 33.07 ? 174 LYS A CG 1 ATOM 1210 C CD . LYS A 1 154 ? 15.424 12.123 29.330 0.50 34.39 ? 174 LYS A CD 1 ATOM 1211 C CE . LYS A 1 154 ? 14.496 13.295 29.655 0.50 35.33 ? 174 LYS A CE 1 ATOM 1212 N NZ . LYS A 1 154 ? 13.064 12.879 29.719 0.50 35.43 ? 174 LYS A NZ 1 ATOM 1213 N N . GLY A 1 155 ? 15.134 13.360 24.408 1.00 32.26 ? 175 GLY A N 1 ATOM 1214 C CA . GLY A 1 155 ? 14.800 14.128 23.214 1.00 30.84 ? 175 GLY A CA 1 ATOM 1215 C C . GLY A 1 155 ? 14.026 13.347 22.164 1.00 29.28 ? 175 GLY A C 1 ATOM 1216 O O . GLY A 1 155 ? 14.571 13.053 21.110 1.00 29.98 ? 175 GLY A O 1 ATOM 1217 N N . LEU A 1 156 ? 12.772 13.000 22.457 1.00 27.80 ? 176 LEU A N 1 ATOM 1218 C CA . LEU A 1 156 ? 11.916 12.248 21.529 1.00 26.79 ? 176 LEU A CA 1 ATOM 1219 C C . LEU A 1 156 ? 11.685 13.103 20.294 1.00 25.28 ? 176 LEU A C 1 ATOM 1220 O O . LEU A 1 156 ? 11.303 14.269 20.403 1.00 24.58 ? 176 LEU A O 1 ATOM 1221 C CB . LEU A 1 156 ? 10.563 11.961 22.195 1.00 27.24 ? 176 LEU A CB 1 ATOM 1222 C CG . LEU A 1 156 ? 9.763 10.657 22.125 1.00 30.58 ? 176 LEU A CG 1 ATOM 1223 C CD1 . LEU A 1 156 ? 8.347 10.939 22.537 1.00 32.39 ? 176 LEU A CD1 1 ATOM 1224 C CD2 . LEU A 1 156 ? 9.763 10.009 20.762 1.00 30.95 ? 176 LEU A CD2 1 ATOM 1225 N N . ALA A 1 157 ? 11.935 12.542 19.116 1.00 24.10 ? 177 ALA A N 1 ATOM 1226 C CA . ALA A 1 157 ? 11.671 13.273 17.885 1.00 23.57 ? 177 ALA A CA 1 ATOM 1227 C C . ALA A 1 157 ? 10.178 13.392 17.591 1.00 23.32 ? 177 ALA A C 1 ATOM 1228 O O . ALA A 1 157 ? 9.373 12.540 17.968 1.00 23.06 ? 177 ALA A O 1 ATOM 1229 C CB . ALA A 1 157 ? 12.390 12.626 16.724 1.00 23.59 ? 177 ALA A CB 1 ATOM 1230 N N . ALA A 1 158 ? 9.812 14.470 16.912 1.00 22.05 ? 178 ALA A N 1 ATOM 1231 C CA . ALA A 1 158 ? 8.470 14.646 16.419 1.00 21.69 ? 178 ALA A CA 1 ATOM 1232 C C . ALA A 1 158 ? 8.329 13.741 15.181 1.00 20.42 ? 178 ALA A C 1 ATOM 1233 O O . ALA A 1 158 ? 9.270 13.005 14.819 1.00 20.20 ? 178 ALA A O 1 ATOM 1234 C CB . ALA A 1 158 ? 8.221 16.117 16.072 1.00 22.18 ? 178 ALA A CB 1 ATOM 1235 N N . THR A 1 159 ? 7.164 13.786 14.556 1.00 19.69 ? 179 THR A N 1 ATOM 1236 C CA . THR A 1 159 ? 6.835 12.896 13.436 1.00 18.56 ? 179 THR A CA 1 ATOM 1237 C C . THR A 1 159 ? 7.181 11.443 13.768 1.00 17.55 ? 179 THR A C 1 ATOM 1238 O O . THR A 1 159 ? 7.781 10.712 12.973 1.00 15.42 ? 179 THR A O 1 ATOM 1239 C CB . THR A 1 159 ? 7.432 13.375 12.070 1.00 18.98 ? 179 THR A CB 1 ATOM 1240 O OG1 . THR A 1 159 ? 8.867 13.308 12.088 1.00 19.84 ? 179 THR A OG1 1 ATOM 1241 C CG2 . THR A 1 159 ? 7.014 14.825 11.799 1.00 19.99 ? 179 THR A CG2 1 ATOM 1242 N N . THR A 1 160 ? 6.806 11.048 14.980 1.00 16.48 ? 180 THR A N 1 ATOM 1243 C CA . THR A 1 160 ? 7.021 9.678 15.402 1.00 16.07 ? 180 THR A CA 1 ATOM 1244 C C . THR A 1 160 ? 5.766 9.119 16.016 1.00 16.15 ? 180 THR A C 1 ATOM 1245 O O . THR A 1 160 ? 4.887 9.868 16.443 1.00 16.20 ? 180 THR A O 1 ATOM 1246 C CB . THR A 1 160 ? 8.172 9.525 16.418 1.00 16.24 ? 180 THR A CB 1 ATOM 1247 O OG1 . THR A 1 160 ? 7.969 10.418 17.518 1.00 17.27 ? 180 THR A OG1 1 ATOM 1248 C CG2 . THR A 1 160 ? 9.528 9.795 15.783 1.00 15.38 ? 180 THR A CG2 1 ATOM 1249 N N . LEU A 1 161 ? 5.693 7.794 16.006 1.00 15.45 ? 181 LEU A N 1 ATOM 1250 C CA . LEU A 1 161 ? 4.674 7.030 16.708 1.00 14.90 ? 181 LEU A CA 1 ATOM 1251 C C . LEU A 1 161 ? 5.332 6.318 17.858 1.00 15.09 ? 181 LEU A C 1 ATOM 1252 O O . LEU A 1 161 ? 6.474 5.895 17.767 1.00 14.22 ? 181 LEU A O 1 ATOM 1253 C CB . LEU A 1 161 ? 4.072 5.982 15.791 1.00 15.03 ? 181 LEU A CB 1 ATOM 1254 C CG . LEU A 1 161 ? 3.214 6.496 14.641 1.00 16.57 ? 181 LEU A CG 1 ATOM 1255 C CD1 . LEU A 1 161 ? 3.052 5.387 13.602 1.00 16.91 ? 181 LEU A CD1 1 ATOM 1256 C CD2 . LEU A 1 161 ? 1.877 7.022 15.141 1.00 17.82 ? 181 LEU A CD2 1 ATOM 1257 N N . CYS A 1 162 ? 4.578 6.200 18.950 1.00 15.11 ? 182 CYS A N 1 ATOM 1258 C CA . CYS A 1 162 ? 5.000 5.496 20.139 1.00 15.76 ? 182 CYS A CA 1 ATOM 1259 C C . CYS A 1 162 ? 4.289 4.153 20.086 1.00 15.48 ? 182 CYS A C 1 ATOM 1260 O O . CYS A 1 162 ? 3.073 4.119 20.023 1.00 15.90 ? 182 CYS A O 1 ATOM 1261 C CB . CYS A 1 162 ? 4.509 6.285 21.360 1.00 16.23 ? 182 CYS A CB 1 ATOM 1262 S SG . CYS A 1 162 ? 5.013 5.574 22.906 1.00 17.78 ? 182 CYS A SG 1 ATOM 1263 N N . ALA A 1 163 ? 5.035 3.050 20.067 1.00 14.43 ? 183 ALA A N 1 ATOM 1264 C CA . ALA A 1 163 ? 4.375 1.751 19.920 1.00 13.74 ? 183 ALA A CA 1 ATOM 1265 C C . ALA A 1 163 ? 5.078 0.691 20.720 1.00 13.38 ? 183 ALA A C 1 ATOM 1266 O O . ALA A 1 163 ? 6.292 0.644 20.768 1.00 13.52 ? 183 ALA A O 1 ATOM 1267 C CB . ALA A 1 163 ? 4.295 1.346 18.447 1.00 14.46 ? 183 ALA A CB 1 ATOM 1268 N N . GLY A 1 164 ? 4.288 -0.163 21.336 1.00 13.57 ? 184 GLY A N 1 ATOM 1269 C CA . GLY A 1 164 ? 4.807 -1.202 22.180 1.00 14.22 ? 184 GLY A CA 1 ATOM 1270 C C . GLY A 1 164 ? 3.656 -1.788 22.965 1.00 15.58 ? 184 GLY A C 1 ATOM 1271 O O . GLY A 1 164 ? 2.481 -1.655 22.585 1.00 14.93 ? 184 GLY A O 1 ATOM 1272 N N . ILE A 1 165 ? 4.023 -2.443 24.057 1.00 16.59 ? 185 ILE A N 1 ATOM 1273 C CA . ILE A 1 165 ? 3.068 -2.986 25.007 1.00 19.07 ? 185 ILE A CA 1 ATOM 1274 C C . ILE A 1 165 ? 3.360 -2.196 26.268 1.00 19.45 ? 185 ILE A C 1 ATOM 1275 O O . ILE A 1 165 ? 4.508 -2.106 26.681 1.00 19.56 ? 185 ILE A O 1 ATOM 1276 C CB . ILE A 1 165 ? 3.309 -4.497 25.252 1.00 19.50 ? 185 ILE A CB 1 ATOM 1277 C CG1 . ILE A 1 165 ? 3.127 -5.302 23.961 1.00 22.27 ? 185 ILE A CG1 1 ATOM 1278 C CG2 . ILE A 1 165 ? 2.366 -5.019 26.329 1.00 21.60 ? 185 ILE A CG2 1 ATOM 1279 C CD1 . ILE A 1 165 ? 1.750 -5.217 23.380 1.00 23.26 ? 185 ILE A CD1 1 ATOM 1280 N N . LEU A 1 166 ? 2.336 -1.598 26.867 1.00 20.63 ? 186 LEU A N 1 ATOM 1281 C CA . LEU A 1 166 ? 2.577 -0.715 27.998 1.00 22.03 ? 186 LEU A CA 1 ATOM 1282 C C . LEU A 1 166 ? 3.311 -1.477 29.093 1.00 22.33 ? 186 LEU A C 1 ATOM 1283 O O . LEU A 1 166 ? 4.207 -0.936 29.750 1.00 23.93 ? 186 LEU A O 1 ATOM 1284 C CB . LEU A 1 166 ? 1.251 -0.145 28.514 1.00 21.90 ? 186 LEU A CB 1 ATOM 1285 C CG . LEU A 1 166 ? 1.187 1.127 29.345 1.00 24.30 ? 186 LEU A CG 1 ATOM 1286 C CD1 . LEU A 1 166 ? 1.748 2.345 28.612 1.00 21.97 ? 186 LEU A CD1 1 ATOM 1287 C CD2 . LEU A 1 166 ? -0.270 1.382 29.716 1.00 23.02 ? 186 LEU A CD2 1 ATOM 1288 N N . GLU A 1 167 A 2.929 -2.734 29.279 1.00 22.64 ? 186 GLU A N 1 ATOM 1289 C CA . GLU A 1 167 A 3.515 -3.582 30.317 1.00 22.83 ? 186 GLU A CA 1 ATOM 1290 C C . GLU A 1 167 A 4.875 -4.177 29.916 1.00 21.95 ? 186 GLU A C 1 ATOM 1291 O O . GLU A 1 167 A 5.522 -4.878 30.699 1.00 22.65 ? 186 GLU A O 1 ATOM 1292 C CB . GLU A 1 167 A 2.509 -4.667 30.768 1.00 23.15 ? 186 GLU A CB 1 ATOM 1293 C CG . GLU A 1 167 A 1.971 -5.597 29.678 0.50 24.34 ? 186 GLU A CG 1 ATOM 1294 C CD . GLU A 1 167 A 0.641 -5.137 29.050 0.50 25.29 ? 186 GLU A CD 1 ATOM 1295 O OE1 . GLU A 1 167 A 0.328 -3.912 29.022 0.50 22.89 ? 186 GLU A OE1 1 ATOM 1296 O OE2 . GLU A 1 167 A -0.092 -6.031 28.559 0.50 25.78 ? 186 GLU A OE2 1 ATOM 1297 N N . GLY A 1 168 B 5.306 -3.887 28.688 1.00 20.59 ? 186 GLY A N 1 ATOM 1298 C CA . GLY A 1 168 B 6.524 -4.467 28.151 1.00 20.12 ? 186 GLY A CA 1 ATOM 1299 C C . GLY A 1 168 B 6.369 -5.916 27.726 1.00 19.79 ? 186 GLY A C 1 ATOM 1300 O O . GLY A 1 168 B 5.259 -6.454 27.668 1.00 20.38 ? 186 GLY A O 1 ATOM 1301 N N . GLY A 1 169 ? 7.493 -6.538 27.392 1.00 19.24 ? 187 GLY A N 1 ATOM 1302 C CA . GLY A 1 169 ? 7.516 -7.952 27.077 1.00 18.73 ? 187 GLY A CA 1 ATOM 1303 C C . GLY A 1 169 ? 7.628 -8.231 25.595 1.00 18.24 ? 187 GLY A C 1 ATOM 1304 O O . GLY A 1 169 ? 8.155 -9.263 25.199 1.00 18.30 ? 187 GLY A O 1 ATOM 1305 N N . LYS A 1 170 ? 7.111 -7.322 24.777 1.00 18.01 ? 188 LYS A N 1 ATOM 1306 C CA . LYS A 1 170 ? 7.223 -7.447 23.313 1.00 17.38 ? 188 LYS A CA 1 ATOM 1307 C C . LYS A 1 170 ? 7.696 -6.116 22.810 1.00 16.44 ? 188 LYS A C 1 ATOM 1308 O O . LYS A 1 170 ? 7.212 -5.082 23.252 1.00 17.23 ? 188 LYS A O 1 ATOM 1309 C CB . LYS A 1 170 ? 5.882 -7.783 22.682 1.00 17.84 ? 188 LYS A CB 1 ATOM 1310 C CG . LYS A 1 170 ? 5.361 -9.148 23.111 1.00 19.79 ? 188 LYS A CG 1 ATOM 1311 C CD . LYS A 1 170 ? 3.971 -9.392 22.570 1.00 23.46 ? 188 LYS A CD 1 ATOM 1312 C CE . LYS A 1 170 ? 3.434 -10.715 23.057 1.00 27.40 ? 188 LYS A CE 1 ATOM 1313 N NZ . LYS A 1 170 ? 2.063 -10.941 22.493 1.00 31.64 ? 188 LYS A NZ 1 ATOM 1314 N N . ASP A 1 171 ? 8.641 -6.144 21.881 1.00 16.11 ? 189 ASP A N 1 ATOM 1315 C CA . ASP A 1 171 ? 9.285 -4.921 21.461 1.00 16.05 ? 189 ASP A CA 1 ATOM 1316 C C . ASP A 1 171 ? 10.171 -5.271 20.292 1.00 15.76 ? 189 ASP A C 1 ATOM 1317 O O . ASP A 1 171 ? 10.557 -6.418 20.112 1.00 16.17 ? 189 ASP A O 1 ATOM 1318 C CB . ASP A 1 171 ? 10.142 -4.353 22.601 1.00 16.18 ? 189 ASP A CB 1 ATOM 1319 C CG . ASP A 1 171 ? 10.523 -2.900 22.401 1.00 17.15 ? 189 ASP A CG 1 ATOM 1320 O OD1 . ASP A 1 171 ? 10.042 -2.261 21.432 1.00 15.95 ? 189 ASP A OD1 1 ATOM 1321 O OD2 . ASP A 1 171 ? 11.331 -2.402 23.226 1.00 17.52 ? 189 ASP A OD2 1 ATOM 1322 N N . THR A 1 172 ? 10.513 -4.265 19.504 1.00 15.77 ? 190 THR A N 1 ATOM 1323 C CA . THR A 1 172 ? 11.631 -4.403 18.600 1.00 14.93 ? 190 THR A CA 1 ATOM 1324 C C . THR A 1 172 ? 12.925 -4.234 19.410 1.00 16.46 ? 190 THR A C 1 ATOM 1325 O O . THR A 1 172 ? 12.908 -3.849 20.594 1.00 16.01 ? 190 THR A O 1 ATOM 1326 C CB . THR A 1 172 ? 11.557 -3.343 17.499 1.00 14.87 ? 190 THR A CB 1 ATOM 1327 O OG1 . THR A 1 172 ? 11.203 -2.085 18.085 1.00 14.27 ? 190 THR A OG1 1 ATOM 1328 C CG2 . THR A 1 172 ? 10.500 -3.721 16.482 1.00 14.77 ? 190 THR A CG2 1 ATOM 1329 N N . CYS A 1 173 ? 14.053 -4.521 18.771 1.00 16.35 ? 191 CYS A N 1 ATOM 1330 C CA . CYS A 1 173 ? 15.307 -4.385 19.464 1.00 17.15 ? 191 CYS A CA 1 ATOM 1331 C C . CYS A 1 173 ? 16.419 -4.183 18.444 1.00 17.72 ? 191 CYS A C 1 ATOM 1332 O O . CYS A 1 173 ? 16.146 -4.009 17.263 1.00 16.70 ? 191 CYS A O 1 ATOM 1333 C CB . CYS A 1 173 ? 15.523 -5.610 20.332 1.00 17.46 ? 191 CYS A CB 1 ATOM 1334 S SG . CYS A 1 173 ? 16.645 -5.323 21.707 1.00 18.81 ? 191 CYS A SG 1 ATOM 1335 N N . LYS A 1 174 ? 17.662 -4.181 18.912 1.00 17.25 ? 192 LYS A N 1 ATOM 1336 C CA . LYS A 1 174 ? 18.814 -3.954 18.042 1.00 17.78 ? 192 LYS A CA 1 ATOM 1337 C C . LYS A 1 174 ? 18.775 -4.864 16.821 1.00 17.26 ? 192 LYS A C 1 ATOM 1338 O O . LYS A 1 174 ? 18.595 -6.063 16.945 1.00 17.02 ? 192 LYS A O 1 ATOM 1339 C CB . LYS A 1 174 ? 20.119 -4.135 18.831 1.00 19.26 ? 192 LYS A CB 1 ATOM 1340 C CG . LYS A 1 174 ? 20.230 -3.170 20.027 1.00 23.36 ? 192 LYS A CG 1 ATOM 1341 C CD . LYS A 1 174 ? 20.708 -1.769 19.617 0.50 24.63 ? 192 LYS A CD 1 ATOM 1342 C CE . LYS A 1 174 ? 20.809 -0.848 20.820 0.50 24.25 ? 192 LYS A CE 1 ATOM 1343 N NZ . LYS A 1 174 ? 19.462 -0.457 21.335 0.50 27.11 ? 192 LYS A NZ 1 ATOM 1344 N N . GLY A 1 175 ? 18.928 -4.270 15.637 1.00 16.64 ? 193 GLY A N 1 ATOM 1345 C CA . GLY A 1 175 ? 18.883 -5.040 14.405 1.00 16.06 ? 193 GLY A CA 1 ATOM 1346 C C . GLY A 1 175 ? 17.542 -4.899 13.701 1.00 16.24 ? 193 GLY A C 1 ATOM 1347 O O . GLY A 1 175 ? 17.438 -5.235 12.536 1.00 16.42 ? 193 GLY A O 1 ATOM 1348 N N . ASP A 1 176 ? 16.519 -4.425 14.419 1.00 15.43 ? 194 ASP A N 1 ATOM 1349 C CA . ASP A 1 176 ? 15.193 -4.253 13.839 1.00 14.81 ? 194 ASP A CA 1 ATOM 1350 C C . ASP A 1 176 ? 14.982 -2.849 13.295 1.00 15.00 ? 194 ASP A C 1 ATOM 1351 O O . ASP A 1 176 ? 13.993 -2.613 12.602 1.00 14.18 ? 194 ASP A O 1 ATOM 1352 C CB . ASP A 1 176 ? 14.096 -4.523 14.882 1.00 14.11 ? 194 ASP A CB 1 ATOM 1353 C CG . ASP A 1 176 ? 14.049 -5.950 15.343 1.00 14.49 ? 194 ASP A CG 1 ATOM 1354 O OD1 . ASP A 1 176 ? 14.301 -6.866 14.540 1.00 15.49 ? 194 ASP A OD1 1 ATOM 1355 O OD2 . ASP A 1 176 ? 13.704 -6.146 16.531 1.00 14.31 ? 194 ASP A OD2 1 ATOM 1356 N N . SER A 1 177 ? 15.892 -1.917 13.605 1.00 15.20 ? 195 SER A N 1 ATOM 1357 C CA . SER A 1 177 ? 15.708 -0.530 13.187 1.00 15.21 ? 195 SER A CA 1 ATOM 1358 C C . SER A 1 177 ? 15.527 -0.462 11.702 1.00 14.40 ? 195 SER A C 1 ATOM 1359 O O . SER A 1 177 ? 16.081 -1.284 10.960 1.00 14.29 ? 195 SER A O 1 ATOM 1360 C CB . SER A 1 177 ? 16.910 0.329 13.544 1.00 17.19 ? 195 SER A CB 1 ATOM 1361 O OG . SER A 1 177 ? 16.842 0.647 14.909 1.00 20.62 ? 195 SER A OG 1 ATOM 1362 N N . GLY A 1 178 ? 14.737 0.517 11.275 1.00 13.72 ? 196 GLY A N 1 ATOM 1363 C CA . GLY A 1 178 ? 14.474 0.698 9.870 1.00 13.60 ? 196 GLY A CA 1 ATOM 1364 C C . GLY A 1 178 ? 13.325 -0.155 9.384 1.00 13.44 ? 196 GLY A C 1 ATOM 1365 O O . GLY A 1 178 ? 12.783 0.094 8.302 1.00 13.95 ? 196 GLY A O 1 ATOM 1366 N N . GLY A 1 179 ? 12.977 -1.171 10.171 1.00 13.12 ? 197 GLY A N 1 ATOM 1367 C CA . GLY A 1 179 ? 11.910 -2.110 9.799 1.00 13.40 ? 197 GLY A CA 1 ATOM 1368 C C . GLY A 1 179 ? 10.540 -1.482 10.008 1.00 13.69 ? 197 GLY A C 1 ATOM 1369 O O . GLY A 1 179 ? 10.402 -0.456 10.693 1.00 14.09 ? 197 GLY A O 1 ATOM 1370 N N . PRO A 1 180 ? 9.505 -2.087 9.409 1.00 13.83 ? 198 PRO A N 1 ATOM 1371 C CA . PRO A 1 180 ? 8.158 -1.532 9.455 1.00 13.13 ? 198 PRO A CA 1 ATOM 1372 C C . PRO A 1 180 ? 7.366 -1.850 10.722 1.00 13.41 ? 198 PRO A C 1 ATOM 1373 O O . PRO A 1 180 ? 7.500 -2.942 11.310 1.00 13.81 ? 198 PRO A O 1 ATOM 1374 C CB . PRO A 1 180 ? 7.467 -2.204 8.271 1.00 13.47 ? 198 PRO A CB 1 ATOM 1375 C CG . PRO A 1 180 ? 8.168 -3.551 8.122 1.00 13.38 ? 198 PRO A CG 1 ATOM 1376 C CD . PRO A 1 180 ? 9.593 -3.317 8.594 1.00 14.40 ? 198 PRO A CD 1 ATOM 1377 N N . LEU A 1 181 ? 6.529 -0.884 11.069 1.00 12.73 ? 199 LEU A N 1 ATOM 1378 C CA . LEU A 1 181 ? 5.438 -1.050 12.022 1.00 12.71 ? 199 LEU A CA 1 ATOM 1379 C C . LEU A 1 181 ? 4.180 -1.061 11.161 1.00 12.81 ? 199 LEU A C 1 ATOM 1380 O O . LEU A 1 181 ? 3.874 -0.068 10.488 1.00 12.44 ? 199 LEU A O 1 ATOM 1381 C CB . LEU A 1 181 ? 5.439 0.147 12.978 1.00 12.56 ? 199 LEU A CB 1 ATOM 1382 C CG . LEU A 1 181 ? 4.317 0.225 14.004 1.00 12.23 ? 199 LEU A CG 1 ATOM 1383 C CD1 . LEU A 1 181 ? 4.559 -0.781 15.149 1.00 14.30 ? 199 LEU A CD1 1 ATOM 1384 C CD2 . LEU A 1 181 ? 4.204 1.650 14.507 1.00 12.80 ? 199 LEU A CD2 1 ATOM 1385 N N . ILE A 1 182 ? 3.486 -2.199 11.124 1.00 13.43 ? 200 ILE A N 1 ATOM 1386 C CA . ILE A 1 182 ? 2.320 -2.350 10.247 1.00 14.19 ? 200 ILE A CA 1 ATOM 1387 C C . ILE A 1 182 ? 1.101 -2.377 11.152 1.00 15.60 ? 200 ILE A C 1 ATOM 1388 O O . ILE A 1 182 ? 0.994 -3.258 11.973 1.00 15.76 ? 200 ILE A O 1 ATOM 1389 C CB . ILE A 1 182 ? 2.379 -3.688 9.459 1.00 15.45 ? 200 ILE A CB 1 ATOM 1390 C CG1 . ILE A 1 182 ? 3.728 -3.864 8.729 1.00 17.07 ? 200 ILE A CG1 1 ATOM 1391 C CG2 . ILE A 1 182 ? 1.167 -3.805 8.497 1.00 16.23 ? 200 ILE A CG2 1 ATOM 1392 C CD1 . ILE A 1 182 ? 4.056 -2.740 7.821 0.50 15.57 ? 200 ILE A CD1 1 ATOM 1393 N N . CYS A 1 183 ? 0.230 -1.385 11.031 1.00 15.89 ? 201 CYS A N 1 ATOM 1394 C CA . CYS A 1 183 ? -0.942 -1.305 11.911 1.00 16.97 ? 201 CYS A CA 1 ATOM 1395 C C . CYS A 1 183 ? -2.156 -1.396 11.055 1.00 18.40 ? 201 CYS A C 1 ATOM 1396 O O . CYS A 1 183 ? -2.278 -0.667 10.068 1.00 17.99 ? 201 CYS A O 1 ATOM 1397 C CB . CYS A 1 183 ? -0.964 -0.006 12.691 1.00 17.58 ? 201 CYS A CB 1 ATOM 1398 S SG . CYS A 1 183 ? 0.574 0.362 13.473 1.00 18.18 ? 201 CYS A SG 1 ATOM 1399 N N . ASN A 1 184 ? -3.035 -2.336 11.392 1.00 19.35 ? 202 ASN A N 1 ATOM 1400 C CA . ASN A 1 184 ? -4.246 -2.527 10.612 1.00 19.73 ? 202 ASN A CA 1 ATOM 1401 C C . ASN A 1 184 ? -3.942 -2.594 9.108 1.00 19.32 ? 202 ASN A C 1 ATOM 1402 O O . ASN A 1 184 ? -4.633 -2.002 8.274 1.00 19.86 ? 202 ASN A O 1 ATOM 1403 C CB . ASN A 1 184 ? -5.261 -1.438 10.973 1.00 20.79 ? 202 ASN A CB 1 ATOM 1404 C CG . ASN A 1 184 ? -5.705 -1.530 12.428 1.00 22.12 ? 202 ASN A CG 1 ATOM 1405 O OD1 . ASN A 1 184 ? -5.647 -2.604 13.039 1.00 26.69 ? 202 ASN A OD1 1 ATOM 1406 N ND2 . ASN A 1 184 ? -6.152 -0.428 12.982 1.00 28.46 ? 202 ASN A ND2 1 ATOM 1407 N N . GLY A 1 185 ? -2.892 -3.345 8.779 1.00 18.31 ? 207 GLY A N 1 ATOM 1408 C CA . GLY A 1 185 ? -2.547 -3.641 7.407 1.00 17.30 ? 207 GLY A CA 1 ATOM 1409 C C . GLY A 1 185 ? -1.842 -2.521 6.665 1.00 16.38 ? 207 GLY A C 1 ATOM 1410 O O . GLY A 1 185 ? -1.541 -2.672 5.477 1.00 16.55 ? 207 GLY A O 1 ATOM 1411 N N . GLN A 1 186 ? -1.534 -1.434 7.385 1.00 15.53 ? 208 GLN A N 1 ATOM 1412 C CA . GLN A 1 186 ? -0.914 -0.255 6.768 1.00 15.20 ? 208 GLN A CA 1 ATOM 1413 C C . GLN A 1 186 ? 0.489 -0.056 7.293 1.00 15.22 ? 208 GLN A C 1 ATOM 1414 O O . GLN A 1 186 ? 0.754 -0.272 8.465 1.00 15.45 ? 208 GLN A O 1 ATOM 1415 C CB . GLN A 1 186 ? -1.727 1.007 7.074 1.00 15.45 ? 208 GLN A CB 1 ATOM 1416 C CG . GLN A 1 186 ? -3.151 0.996 6.563 1.00 16.96 ? 208 GLN A CG 1 ATOM 1417 C CD . GLN A 1 186 ? -3.778 2.365 6.644 1.00 20.00 ? 208 GLN A CD 1 ATOM 1418 O OE1 . GLN A 1 186 ? -4.547 2.661 7.554 1.00 25.09 ? 208 GLN A OE1 1 ATOM 1419 N NE2 . GLN A 1 186 ? -3.437 3.210 5.706 1.00 23.67 ? 208 GLN A NE2 1 ATOM 1420 N N . PHE A 1 187 ? 1.371 0.406 6.418 1.00 13.98 ? 209 PHE A N 1 ATOM 1421 C CA . PHE A 1 187 ? 2.745 0.753 6.781 1.00 13.83 ? 209 PHE A CA 1 ATOM 1422 C C . PHE A 1 187 ? 2.752 2.068 7.529 1.00 13.69 ? 209 PHE A C 1 ATOM 1423 O O . PHE A 1 187 ? 2.623 3.113 6.917 1.00 14.34 ? 209 PHE A O 1 ATOM 1424 C CB . PHE A 1 187 ? 3.518 0.904 5.470 1.00 13.82 ? 209 PHE A CB 1 ATOM 1425 C CG . PHE A 1 187 ? 4.957 1.276 5.622 1.00 13.47 ? 209 PHE A CG 1 ATOM 1426 C CD1 . PHE A 1 187 ? 5.676 1.017 6.791 1.00 14.18 ? 209 PHE A CD1 1 ATOM 1427 C CD2 . PHE A 1 187 ? 5.622 1.866 4.539 1.00 12.91 ? 209 PHE A CD2 1 ATOM 1428 C CE1 . PHE A 1 187 ? 7.019 1.369 6.887 1.00 14.86 ? 209 PHE A CE1 1 ATOM 1429 C CE2 . PHE A 1 187 ? 6.966 2.229 4.636 1.00 15.46 ? 209 PHE A CE2 1 ATOM 1430 C CZ . PHE A 1 187 ? 7.669 1.971 5.804 1.00 14.18 ? 209 PHE A CZ 1 ATOM 1431 N N . GLN A 1 188 ? 2.898 2.038 8.855 1.00 12.56 ? 210 GLN A N 1 ATOM 1432 C CA . GLN A 1 188 ? 2.740 3.260 9.622 1.00 13.44 ? 210 GLN A CA 1 ATOM 1433 C C . GLN A 1 188 ? 4.007 3.794 10.251 1.00 12.54 ? 210 GLN A C 1 ATOM 1434 O O . GLN A 1 188 ? 4.106 4.980 10.532 1.00 12.67 ? 210 GLN A O 1 ATOM 1435 C CB . GLN A 1 188 ? 1.685 3.076 10.719 1.00 13.88 ? 210 GLN A CB 1 ATOM 1436 C CG . GLN A 1 188 ? 0.314 2.704 10.140 1.00 14.00 ? 210 GLN A CG 1 ATOM 1437 C CD . GLN A 1 188 ? -0.453 3.884 9.599 1.00 16.22 ? 210 GLN A CD 1 ATOM 1438 O OE1 . GLN A 1 188 ? -1.678 3.793 9.413 1.00 18.57 ? 210 GLN A OE1 1 ATOM 1439 N NE2 . GLN A 1 188 ? 0.229 4.994 9.352 1.00 12.66 ? 210 GLN A NE2 1 ATOM 1440 N N . GLY A 1 189 ? 4.953 2.907 10.528 1.00 12.29 ? 211 GLY A N 1 ATOM 1441 C CA . GLY A 1 189 ? 6.152 3.323 11.227 1.00 12.32 ? 211 GLY A CA 1 ATOM 1442 C C . GLY A 1 189 ? 7.404 2.661 10.688 1.00 12.79 ? 211 GLY A C 1 ATOM 1443 O O . GLY A 1 189 ? 7.368 1.569 10.124 1.00 11.97 ? 211 GLY A O 1 ATOM 1444 N N . ILE A 1 190 ? 8.514 3.365 10.860 1.00 12.07 ? 212 ILE A N 1 ATOM 1445 C CA . ILE A 1 190 ? 9.845 2.818 10.594 1.00 11.78 ? 212 ILE A CA 1 ATOM 1446 C C . ILE A 1 190 ? 10.551 2.842 11.933 1.00 12.70 ? 212 ILE A C 1 ATOM 1447 O O . ILE A 1 190 ? 10.658 3.903 12.532 1.00 13.44 ? 212 ILE A O 1 ATOM 1448 C CB . ILE A 1 190 ? 10.597 3.764 9.635 1.00 11.55 ? 212 ILE A CB 1 ATOM 1449 C CG1 . ILE A 1 190 ? 9.837 3.896 8.303 1.00 12.62 ? 212 ILE A CG1 1 ATOM 1450 C CG2 . ILE A 1 190 ? 12.064 3.340 9.468 1.00 12.49 ? 212 ILE A CG2 1 ATOM 1451 C CD1 . ILE A 1 190 ? 10.333 5.039 7.423 1.00 13.73 ? 212 ILE A CD1 1 ATOM 1452 N N . LEU A 1 191 ? 11.017 1.701 12.434 1.00 12.13 ? 213 LEU A N 1 ATOM 1453 C CA . LEU A 1 191 ? 11.662 1.735 13.750 1.00 11.84 ? 213 LEU A CA 1 ATOM 1454 C C . LEU A 1 191 ? 12.889 2.648 13.769 1.00 12.45 ? 213 LEU A C 1 ATOM 1455 O O . LEU A 1 191 ? 13.804 2.497 12.968 1.00 12.71 ? 213 LEU A O 1 ATOM 1456 C CB . LEU A 1 191 ? 12.047 0.336 14.204 1.00 11.95 ? 213 LEU A CB 1 ATOM 1457 C CG . LEU A 1 191 ? 12.792 0.332 15.542 1.00 12.24 ? 213 LEU A CG 1 ATOM 1458 C CD1 . LEU A 1 191 ? 11.896 0.847 16.691 1.00 12.91 ? 213 LEU A CD1 1 ATOM 1459 C CD2 . LEU A 1 191 ? 13.218 -1.066 15.785 1.00 13.52 ? 213 LEU A CD2 1 ATOM 1460 N N . SER A 1 192 ? 12.901 3.565 14.724 1.00 12.68 ? 214 SER A N 1 ATOM 1461 C CA . SER A 1 192 ? 14.025 4.458 14.902 1.00 13.88 ? 214 SER A CA 1 ATOM 1462 C C . SER A 1 192 ? 14.806 4.073 16.145 1.00 14.55 ? 214 SER A C 1 ATOM 1463 O O . SER A 1 192 ? 15.950 3.637 16.068 1.00 15.95 ? 214 SER A O 1 ATOM 1464 C CB . SER A 1 192 ? 13.532 5.892 15.016 1.00 13.91 ? 214 SER A CB 1 ATOM 1465 O OG . SER A 1 192 ? 14.615 6.761 15.279 1.00 14.41 ? 214 SER A OG 1 ATOM 1466 N N . VAL A 1 193 ? 14.184 4.246 17.298 1.00 14.96 ? 215 VAL A N 1 ATOM 1467 C CA . VAL A 1 193 ? 14.910 4.106 18.558 1.00 15.84 ? 215 VAL A CA 1 ATOM 1468 C C . VAL A 1 193 ? 13.994 3.493 19.579 1.00 16.29 ? 215 VAL A C 1 ATOM 1469 O O . VAL A 1 193 ? 12.797 3.415 19.382 1.00 16.41 ? 215 VAL A O 1 ATOM 1470 C CB . VAL A 1 193 ? 15.462 5.447 19.107 1.00 16.13 ? 215 VAL A CB 1 ATOM 1471 C CG1 . VAL A 1 193 ? 16.580 6.017 18.193 1.00 17.67 ? 215 VAL A CG1 1 ATOM 1472 C CG2 . VAL A 1 193 ? 14.362 6.450 19.345 1.00 17.97 ? 215 VAL A CG2 1 ATOM 1473 N N . GLY A 1 194 ? 14.583 2.998 20.650 1.00 16.64 ? 216 GLY A N 1 ATOM 1474 C CA . GLY A 1 194 ? 13.797 2.496 21.752 1.00 17.63 ? 216 GLY A CA 1 ATOM 1475 C C . GLY A 1 194 ? 14.701 2.322 22.943 1.00 19.13 ? 216 GLY A C 1 ATOM 1476 O O . GLY A 1 194 ? 15.862 2.697 22.914 1.00 19.46 ? 216 GLY A O 1 ATOM 1477 N N . GLY A 1 195 ? 14.144 1.746 23.995 1.00 20.44 ? 217 GLY A N 1 ATOM 1478 C CA . GLY A 1 195 ? 14.893 1.557 25.233 1.00 21.96 ? 217 GLY A CA 1 ATOM 1479 C C . GLY A 1 195 ? 15.849 0.389 25.114 1.00 22.96 ? 217 GLY A C 1 ATOM 1480 O O . GLY A 1 195 ? 15.610 -0.556 24.360 1.00 23.40 ? 217 GLY A O 1 ATOM 1481 N N . ASN A 1 196 ? 16.936 0.458 25.876 1.00 24.28 ? 218 ASN A N 1 ATOM 1482 C CA . ASN A 1 196 ? 17.908 -0.625 25.964 1.00 25.63 ? 218 ASN A CA 1 ATOM 1483 C C . ASN A 1 196 ? 18.187 -0.836 27.445 1.00 25.40 ? 218 ASN A C 1 ATOM 1484 O O . ASN A 1 196 ? 18.627 0.105 28.116 1.00 26.30 ? 218 ASN A O 1 ATOM 1485 C CB . ASN A 1 196 ? 19.198 -0.268 25.225 1.00 26.73 ? 218 ASN A CB 1 ATOM 1486 C CG . ASN A 1 196 ? 20.043 -1.489 24.896 1.00 30.56 ? 218 ASN A CG 1 ATOM 1487 O OD1 . ASN A 1 196 ? 19.522 -2.597 24.724 1.00 35.38 ? 218 ASN A OD1 1 ATOM 1488 N ND2 . ASN A 1 196 ? 21.355 -1.285 24.770 1.00 34.35 ? 218 ASN A ND2 1 ATOM 1489 N N . PRO A 1 197 ? 17.881 -2.036 27.978 1.00 24.49 ? 219 PRO A N 1 ATOM 1490 C CA . PRO A 1 197 ? 17.326 -3.212 27.309 1.00 23.66 ? 219 PRO A CA 1 ATOM 1491 C C . PRO A 1 197 ? 15.937 -2.996 26.719 1.00 22.40 ? 219 PRO A C 1 ATOM 1492 O O . PRO A 1 197 ? 15.207 -2.105 27.136 1.00 22.32 ? 219 PRO A O 1 ATOM 1493 C CB . PRO A 1 197 ? 17.273 -4.273 28.415 1.00 24.41 ? 219 PRO A CB 1 ATOM 1494 C CG . PRO A 1 197 ? 17.336 -3.514 29.693 1.00 25.19 ? 219 PRO A CG 1 ATOM 1495 C CD . PRO A 1 197 ? 18.130 -2.286 29.411 1.00 25.01 ? 219 PRO A CD 1 ATOM 1496 N N . CYS A 1 198 ? 15.609 -3.820 25.735 1.00 21.11 ? 220 CYS A N 1 ATOM 1497 C CA . CYS A 1 198 ? 14.359 -3.735 25.021 1.00 20.46 ? 220 CYS A CA 1 ATOM 1498 C C . CYS A 1 198 ? 13.235 -4.378 25.819 1.00 19.81 ? 220 CYS A C 1 ATOM 1499 O O . CYS A 1 198 ? 13.481 -5.174 26.733 1.00 20.15 ? 220 CYS A O 1 ATOM 1500 C CB . CYS A 1 198 ? 14.515 -4.443 23.673 1.00 20.28 ? 220 CYS A CB 1 ATOM 1501 S SG . CYS A 1 198 ? 15.884 -3.724 22.713 1.00 19.32 ? 220 CYS A SG 1 ATOM 1502 N N . ALA A 1 199 ? 12.007 -4.029 25.451 1.00 18.45 ? 221 ALA A N 1 ATOM 1503 C CA . ALA A 1 199 ? 10.802 -4.653 25.959 1.00 18.12 ? 221 ALA A CA 1 ATOM 1504 C C . ALA A 1 199 ? 10.550 -4.378 27.431 1.00 17.73 ? 221 ALA A C 1 ATOM 1505 O O . ALA A 1 199 ? 9.840 -5.133 28.086 1.00 18.32 ? 221 ALA A O 1 ATOM 1506 C CB . ALA A 1 199 ? 10.799 -6.173 25.678 1.00 17.49 ? 221 ALA A CB 1 ATOM 1507 N N . GLN A 1 200 A 11.131 -3.304 27.949 1.00 18.37 ? 221 GLN A N 1 ATOM 1508 C CA . GLN A 1 200 A 10.862 -2.923 29.334 1.00 18.88 ? 221 GLN A CA 1 ATOM 1509 C C . GLN A 1 200 A 9.474 -2.310 29.451 1.00 19.06 ? 221 GLN A C 1 ATOM 1510 O O . GLN A 1 200 A 8.961 -1.708 28.514 1.00 19.12 ? 221 GLN A O 1 ATOM 1511 C CB A GLN A 1 200 A 11.865 -1.861 29.807 0.50 19.01 ? 221 GLN A CB 1 ATOM 1512 C CB B GLN A 1 200 A 11.977 -2.044 29.896 0.50 18.96 ? 221 GLN A CB 1 ATOM 1513 C CG A GLN A 1 200 A 13.337 -2.258 29.814 0.50 19.54 ? 221 GLN A CG 1 ATOM 1514 C CG B GLN A 1 200 A 13.314 -2.786 29.976 0.50 19.06 ? 221 GLN A CG 1 ATOM 1515 C CD A GLN A 1 200 A 14.236 -1.118 30.276 0.50 19.72 ? 221 GLN A CD 1 ATOM 1516 C CD B GLN A 1 200 A 13.172 -4.211 30.512 0.50 19.97 ? 221 GLN A CD 1 ATOM 1517 O OE1 A GLN A 1 200 A 14.109 -0.629 31.401 0.50 23.23 ? 221 GLN A OE1 1 ATOM 1518 O OE1 B GLN A 1 200 A 12.825 -4.412 31.677 0.50 19.33 ? 221 GLN A OE1 1 ATOM 1519 N NE2 A GLN A 1 200 A 15.143 -0.677 29.402 0.50 19.78 ? 221 GLN A NE2 1 ATOM 1520 N NE2 B GLN A 1 200 A 13.429 -5.205 29.655 0.50 17.32 ? 221 GLN A NE2 1 ATOM 1521 N N . PRO A 1 201 ? 8.844 -2.472 30.619 1.00 19.52 ? 222 PRO A N 1 ATOM 1522 C CA . PRO A 1 201 ? 7.561 -1.813 30.834 1.00 19.59 ? 222 PRO A CA 1 ATOM 1523 C C . PRO A 1 201 ? 7.683 -0.313 30.619 1.00 19.66 ? 222 PRO A C 1 ATOM 1524 O O . PRO A 1 201 ? 8.650 0.296 31.072 1.00 20.35 ? 222 PRO A O 1 ATOM 1525 C CB . PRO A 1 201 ? 7.279 -2.097 32.314 1.00 18.96 ? 222 PRO A CB 1 ATOM 1526 C CG . PRO A 1 201 ? 8.008 -3.424 32.580 1.00 19.88 ? 222 PRO A CG 1 ATOM 1527 C CD . PRO A 1 201 ? 9.288 -3.261 31.789 1.00 19.95 ? 222 PRO A CD 1 ATOM 1528 N N . ARG A 1 202 ? 6.723 0.270 29.898 1.00 20.19 ? 223 ARG A N 1 ATOM 1529 C CA . ARG A 1 202 ? 6.649 1.720 29.683 1.00 20.70 ? 223 ARG A CA 1 ATOM 1530 C C . ARG A 1 202 ? 7.860 2.319 28.994 1.00 20.26 ? 223 ARG A C 1 ATOM 1531 O O . ARG A 1 202 ? 8.159 3.500 29.155 1.00 21.13 ? 223 ARG A O 1 ATOM 1532 C CB . ARG A 1 202 ? 6.350 2.457 30.998 1.00 21.01 ? 223 ARG A CB 1 ATOM 1533 C CG . ARG A 1 202 ? 4.902 2.361 31.375 1.00 24.76 ? 223 ARG A CG 1 ATOM 1534 C CD . ARG A 1 202 ? 4.604 3.206 32.606 1.00 27.69 ? 223 ARG A CD 1 ATOM 1535 N NE . ARG A 1 202 ? 3.422 2.700 33.286 1.00 30.23 ? 223 ARG A NE 1 ATOM 1536 C CZ . ARG A 1 202 ? 2.201 3.200 33.138 1.00 31.73 ? 223 ARG A CZ 1 ATOM 1537 N NH1 . ARG A 1 202 ? 1.187 2.656 33.800 1.00 32.52 ? 223 ARG A NH1 1 ATOM 1538 N NH2 . ARG A 1 202 ? 2.000 4.247 32.343 1.00 31.22 ? 223 ARG A NH2 1 ATOM 1539 N N . LYS A 1 203 ? 8.567 1.503 28.220 1.00 19.57 ? 224 LYS A N 1 ATOM 1540 C CA . LYS A 1 203 ? 9.664 1.997 27.414 1.00 19.40 ? 224 LYS A CA 1 ATOM 1541 C C . LYS A 1 203 ? 9.444 1.465 26.019 1.00 18.71 ? 224 LYS A C 1 ATOM 1542 O O . LYS A 1 203 ? 10.083 0.497 25.601 1.00 19.19 ? 224 LYS A O 1 ATOM 1543 C CB . LYS A 1 203 ? 11.012 1.577 27.985 1.00 20.20 ? 224 LYS A CB 1 ATOM 1544 C CG . LYS A 1 203 ? 11.267 2.220 29.322 1.00 22.21 ? 224 LYS A CG 1 ATOM 1545 C CD . LYS A 1 203 ? 12.656 1.984 29.833 1.00 27.18 ? 224 LYS A CD 1 ATOM 1546 C CE . LYS A 1 203 ? 12.843 2.831 31.099 1.00 29.81 ? 224 LYS A CE 1 ATOM 1547 N NZ . LYS A 1 203 ? 13.755 2.168 32.073 1.00 33.79 ? 224 LYS A NZ 1 ATOM 1548 N N . PRO A 1 204 ? 8.518 2.100 25.296 1.00 17.84 ? 225 PRO A N 1 ATOM 1549 C CA . PRO A 1 204 ? 8.121 1.622 23.973 1.00 17.33 ? 225 PRO A CA 1 ATOM 1550 C C . PRO A 1 204 ? 9.148 1.915 22.884 1.00 16.51 ? 225 PRO A C 1 ATOM 1551 O O . PRO A 1 204 ? 10.202 2.513 23.129 1.00 17.32 ? 225 PRO A O 1 ATOM 1552 C CB . PRO A 1 204 ? 6.829 2.405 23.701 1.00 17.84 ? 225 PRO A CB 1 ATOM 1553 C CG . PRO A 1 204 ? 6.454 3.059 25.040 1.00 18.15 ? 225 PRO A CG 1 ATOM 1554 C CD . PRO A 1 204 ? 7.753 3.298 25.687 1.00 17.76 ? 225 PRO A CD 1 ATOM 1555 N N . GLY A 1 205 ? 8.844 1.467 21.675 1.00 15.53 ? 226 GLY A N 1 ATOM 1556 C CA . GLY A 1 205 ? 9.658 1.849 20.536 1.00 14.69 ? 226 GLY A CA 1 ATOM 1557 C C . GLY A 1 205 ? 9.143 3.135 19.922 1.00 14.42 ? 226 GLY A C 1 ATOM 1558 O O . GLY A 1 205 ? 7.955 3.487 20.023 1.00 14.48 ? 226 GLY A O 1 ATOM 1559 N N . ILE A 1 206 ? 10.060 3.833 19.268 1.00 13.75 ? 227 ILE A N 1 ATOM 1560 C CA . ILE A 1 206 ? 9.770 5.092 18.615 1.00 13.89 ? 227 ILE A CA 1 ATOM 1561 C C . ILE A 1 206 ? 9.948 4.831 17.140 1.00 12.42 ? 227 ILE A C 1 ATOM 1562 O O . ILE A 1 206 ? 11.027 4.434 16.694 1.00 12.70 ? 227 ILE A O 1 ATOM 1563 C CB . ILE A 1 206 ? 10.751 6.153 19.069 1.00 14.40 ? 227 ILE A CB 1 ATOM 1564 C CG1 . ILE A 1 206 ? 10.557 6.376 20.565 1.00 17.37 ? 227 ILE A CG1 1 ATOM 1565 C CG2 . ILE A 1 206 ? 10.568 7.438 18.299 1.00 14.67 ? 227 ILE A CG2 1 ATOM 1566 C CD1 . ILE A 1 206 ? 11.658 7.148 21.181 1.00 22.62 ? 227 ILE A CD1 1 ATOM 1567 N N . TYR A 1 207 ? 8.870 5.059 16.396 1.00 12.59 ? 228 TYR A N 1 ATOM 1568 C CA . TYR A 1 207 ? 8.820 4.708 14.989 1.00 12.18 ? 228 TYR A CA 1 ATOM 1569 C C . TYR A 1 207 ? 8.538 5.947 14.213 1.00 12.49 ? 228 TYR A C 1 ATOM 1570 O O . TYR A 1 207 ? 7.573 6.640 14.479 1.00 13.41 ? 228 TYR A O 1 ATOM 1571 C CB . TYR A 1 207 ? 7.694 3.695 14.728 1.00 12.54 ? 228 TYR A CB 1 ATOM 1572 C CG . TYR A 1 207 ? 7.907 2.398 15.448 1.00 12.57 ? 228 TYR A CG 1 ATOM 1573 C CD1 . TYR A 1 207 ? 7.550 2.265 16.790 1.00 13.12 ? 228 TYR A CD1 1 ATOM 1574 C CD2 . TYR A 1 207 ? 8.466 1.296 14.791 1.00 14.91 ? 228 TYR A CD2 1 ATOM 1575 C CE1 . TYR A 1 207 ? 7.764 1.071 17.473 1.00 12.24 ? 228 TYR A CE1 1 ATOM 1576 C CE2 . TYR A 1 207 ? 8.677 0.092 15.465 1.00 12.94 ? 228 TYR A CE2 1 ATOM 1577 C CZ . TYR A 1 207 ? 8.329 -0.007 16.806 1.00 12.88 ? 228 TYR A CZ 1 ATOM 1578 O OH . TYR A 1 207 ? 8.563 -1.182 17.477 1.00 14.22 ? 228 TYR A OH 1 ATOM 1579 N N . THR A 1 208 ? 9.367 6.222 13.222 1.00 11.46 ? 229 THR A N 1 ATOM 1580 C CA . THR A 1 208 ? 9.132 7.382 12.391 1.00 12.52 ? 229 THR A CA 1 ATOM 1581 C C . THR A 1 208 ? 7.767 7.224 11.738 1.00 12.79 ? 229 THR A C 1 ATOM 1582 O O . THR A 1 208 ? 7.444 6.153 11.240 1.00 13.04 ? 229 THR A O 1 ATOM 1583 C CB . THR A 1 208 ? 10.220 7.468 11.329 1.00 11.89 ? 229 THR A CB 1 ATOM 1584 O OG1 . THR A 1 208 ? 11.486 7.464 11.994 1.00 13.55 ? 229 THR A OG1 1 ATOM 1585 C CG2 . THR A 1 208 ? 10.047 8.753 10.495 1.00 13.29 ? 229 THR A CG2 1 ATOM 1586 N N . LYS A 1 209 ? 6.983 8.296 11.743 1.00 13.12 ? 230 LYS A N 1 ATOM 1587 C CA . LYS A 1 209 ? 5.574 8.223 11.382 1.00 13.22 ? 230 LYS A CA 1 ATOM 1588 C C . LYS A 1 209 ? 5.420 8.388 9.881 1.00 13.53 ? 230 LYS A C 1 ATOM 1589 O O . LYS A 1 209 ? 5.408 9.495 9.351 1.00 12.93 ? 230 LYS A O 1 ATOM 1590 C CB . LYS A 1 209 ? 4.804 9.302 12.148 1.00 14.10 ? 230 LYS A CB 1 ATOM 1591 C CG . LYS A 1 209 ? 3.309 9.262 12.030 1.00 16.10 ? 230 LYS A CG 1 ATOM 1592 C CD . LYS A 1 209 ? 2.762 10.265 13.021 1.00 19.17 ? 230 LYS A CD 1 ATOM 1593 C CE . LYS A 1 209 ? 1.297 10.437 12.921 1.00 22.16 ? 230 LYS A CE 1 ATOM 1594 N NZ . LYS A 1 209 ? 0.932 11.330 14.069 1.00 21.85 ? 230 LYS A NZ 1 ATOM 1595 N N . VAL A 1 210 ? 5.333 7.257 9.196 1.00 13.01 ? 231 VAL A N 1 ATOM 1596 C CA . VAL A 1 210 ? 5.347 7.232 7.722 1.00 13.17 ? 231 VAL A CA 1 ATOM 1597 C C . VAL A 1 210 ? 4.301 8.149 7.097 1.00 12.81 ? 231 VAL A C 1 ATOM 1598 O O . VAL A 1 210 ? 4.586 8.832 6.125 1.00 12.22 ? 231 VAL A O 1 ATOM 1599 C CB . VAL A 1 210 ? 5.158 5.788 7.226 1.00 12.42 ? 231 VAL A CB 1 ATOM 1600 C CG1 . VAL A 1 210 ? 5.085 5.746 5.704 1.00 13.53 ? 231 VAL A CG1 1 ATOM 1601 C CG2 . VAL A 1 210 ? 6.314 4.933 7.735 1.00 13.37 ? 231 VAL A CG2 1 ATOM 1602 N N . PHE A 1 211 ? 3.089 8.157 7.652 1.00 12.65 ? 232 PHE A N 1 ATOM 1603 C CA . PHE A 1 211 ? 2.029 9.027 7.118 1.00 12.90 ? 232 PHE A CA 1 ATOM 1604 C C . PHE A 1 211 ? 2.491 10.476 6.918 1.00 12.81 ? 232 PHE A C 1 ATOM 1605 O O . PHE A 1 211 ? 2.171 11.127 5.919 1.00 13.69 ? 232 PHE A O 1 ATOM 1606 C CB . PHE A 1 211 ? 0.845 9.028 8.083 1.00 13.10 ? 232 PHE A CB 1 ATOM 1607 C CG . PHE A 1 211 ? -0.262 9.924 7.650 1.00 13.64 ? 232 PHE A CG 1 ATOM 1608 C CD1 . PHE A 1 211 ? -1.142 9.522 6.651 1.00 14.59 ? 232 PHE A CD1 1 ATOM 1609 C CD2 . PHE A 1 211 ? -0.406 11.182 8.224 1.00 16.18 ? 232 PHE A CD2 1 ATOM 1610 C CE1 . PHE A 1 211 ? -2.177 10.370 6.237 1.00 12.17 ? 232 PHE A CE1 1 ATOM 1611 C CE2 . PHE A 1 211 ? -1.426 12.021 7.817 1.00 14.88 ? 232 PHE A CE2 1 ATOM 1612 C CZ . PHE A 1 211 ? -2.315 11.606 6.833 1.00 14.14 ? 232 PHE A CZ 1 ATOM 1613 N N . ASP A 1 212 ? 3.260 10.977 7.878 1.00 13.36 ? 233 ASP A N 1 ATOM 1614 C CA . ASP A 1 212 ? 3.703 12.377 7.859 1.00 14.42 ? 233 ASP A CA 1 ATOM 1615 C C . ASP A 1 212 ? 4.628 12.652 6.697 1.00 14.45 ? 233 ASP A C 1 ATOM 1616 O O . ASP A 1 212 ? 4.805 13.810 6.292 1.00 15.79 ? 233 ASP A O 1 ATOM 1617 C CB . ASP A 1 212 ? 4.449 12.681 9.152 1.00 14.29 ? 233 ASP A CB 1 ATOM 1618 C CG . ASP A 1 212 ? 3.514 12.879 10.332 1.00 18.19 ? 233 ASP A CG 1 ATOM 1619 O OD1 . ASP A 1 212 ? 2.290 12.769 10.148 1.00 19.37 ? 233 ASP A OD1 1 ATOM 1620 O OD2 . ASP A 1 212 ? 4.020 13.127 11.451 1.00 20.92 ? 233 ASP A OD2 1 ATOM 1621 N N . TYR A 1 213 ? 5.225 11.589 6.171 1.00 13.76 ? 234 TYR A N 1 ATOM 1622 C CA . TYR A 1 213 ? 6.222 11.713 5.114 1.00 13.20 ? 234 TYR A CA 1 ATOM 1623 C C . TYR A 1 213 ? 5.655 11.416 3.740 1.00 13.34 ? 234 TYR A C 1 ATOM 1624 O O . TYR A 1 213 ? 6.409 11.348 2.776 1.00 13.11 ? 234 TYR A O 1 ATOM 1625 C CB . TYR A 1 213 ? 7.402 10.789 5.425 1.00 12.65 ? 234 TYR A CB 1 ATOM 1626 C CG . TYR A 1 213 ? 8.205 11.326 6.570 1.00 13.48 ? 234 TYR A CG 1 ATOM 1627 C CD1 . TYR A 1 213 ? 7.814 11.093 7.899 1.00 13.02 ? 234 TYR A CD1 1 ATOM 1628 C CD2 . TYR A 1 213 ? 9.327 12.108 6.330 1.00 15.24 ? 234 TYR A CD2 1 ATOM 1629 C CE1 . TYR A 1 213 ? 8.533 11.600 8.946 1.00 14.48 ? 234 TYR A CE1 1 ATOM 1630 C CE2 . TYR A 1 213 ? 10.054 12.638 7.390 1.00 15.70 ? 234 TYR A CE2 1 ATOM 1631 C CZ . TYR A 1 213 ? 9.648 12.377 8.684 1.00 15.19 ? 234 TYR A CZ 1 ATOM 1632 O OH . TYR A 1 213 ? 10.347 12.909 9.741 1.00 15.38 ? 234 TYR A OH 1 ATOM 1633 N N . THR A 1 214 ? 4.342 11.236 3.633 1.00 14.88 ? 235 THR A N 1 ATOM 1634 C CA . THR A 1 214 ? 3.719 10.897 2.330 1.00 15.67 ? 235 THR A CA 1 ATOM 1635 C C . THR A 1 214 ? 4.114 11.876 1.239 1.00 15.44 ? 235 THR A C 1 ATOM 1636 O O . THR A 1 214 ? 4.528 11.469 0.143 1.00 13.87 ? 235 THR A O 1 ATOM 1637 C CB . THR A 1 214 ? 2.162 10.912 2.414 1.00 16.65 ? 235 THR A CB 1 ATOM 1638 O OG1 . THR A 1 214 ? 1.763 10.005 3.422 1.00 20.33 ? 235 THR A OG1 1 ATOM 1639 C CG2 . THR A 1 214 ? 1.542 10.478 1.076 1.00 18.99 ? 235 THR A CG2 1 ATOM 1640 N N . ASP A 1 215 ? 3.938 13.167 1.520 1.00 16.14 ? 236 ASP A N 1 ATOM 1641 C CA . ASP A 1 215 ? 4.200 14.192 0.505 1.00 17.27 ? 236 ASP A CA 1 ATOM 1642 C C . ASP A 1 215 ? 5.657 14.161 0.106 1.00 16.07 ? 236 ASP A C 1 ATOM 1643 O O . ASP A 1 215 ? 5.994 14.272 -1.066 1.00 15.62 ? 236 ASP A O 1 ATOM 1644 C CB . ASP A 1 215 ? 3.878 15.595 1.029 1.00 18.73 ? 236 ASP A CB 1 ATOM 1645 C CG . ASP A 1 215 ? 2.400 15.825 1.246 1.00 25.04 ? 236 ASP A CG 1 ATOM 1646 O OD1 . ASP A 1 215 ? 1.551 15.104 0.659 1.00 28.74 ? 236 ASP A OD1 1 ATOM 1647 O OD2 . ASP A 1 215 ? 2.092 16.778 2.003 1.00 32.04 ? 236 ASP A OD2 1 ATOM 1648 N N . TRP A 1 216 ? 6.526 14.007 1.089 1.00 14.86 ? 237 TRP A N 1 ATOM 1649 C CA . TRP A 1 216 ? 7.943 13.975 0.831 1.00 14.33 ? 237 TRP A CA 1 ATOM 1650 C C . TRP A 1 216 ? 8.299 12.779 -0.067 1.00 14.01 ? 237 TRP A C 1 ATOM 1651 O O . TRP A 1 216 ? 8.966 12.914 -1.097 1.00 13.72 ? 237 TRP A O 1 ATOM 1652 C CB . TRP A 1 216 ? 8.697 13.898 2.159 1.00 13.68 ? 237 TRP A CB 1 ATOM 1653 C CG . TRP A 1 216 ? 10.160 13.823 2.013 1.00 14.54 ? 237 TRP A CG 1 ATOM 1654 C CD1 . TRP A 1 216 ? 10.993 14.823 1.605 1.00 15.45 ? 237 TRP A CD1 1 ATOM 1655 C CD2 . TRP A 1 216 ? 10.989 12.702 2.302 1.00 13.88 ? 237 TRP A CD2 1 ATOM 1656 N NE1 . TRP A 1 216 ? 12.281 14.399 1.625 1.00 15.49 ? 237 TRP A NE1 1 ATOM 1657 C CE2 . TRP A 1 216 ? 12.320 13.093 2.042 1.00 15.93 ? 237 TRP A CE2 1 ATOM 1658 C CE3 . TRP A 1 216 ? 10.744 11.405 2.761 1.00 14.97 ? 237 TRP A CE3 1 ATOM 1659 C CZ2 . TRP A 1 216 ? 13.404 12.233 2.224 1.00 14.85 ? 237 TRP A CZ2 1 ATOM 1660 C CZ3 . TRP A 1 216 ? 11.817 10.548 2.951 1.00 14.24 ? 237 TRP A CZ3 1 ATOM 1661 C CH2 . TRP A 1 216 ? 13.142 10.966 2.684 1.00 15.11 ? 237 TRP A CH2 1 ATOM 1662 N N . ILE A 1 217 ? 7.814 11.616 0.325 1.00 13.22 ? 238 ILE A N 1 ATOM 1663 C CA . ILE A 1 217 ? 8.074 10.419 -0.460 1.00 13.50 ? 238 ILE A CA 1 ATOM 1664 C C . ILE A 1 217 ? 7.558 10.594 -1.889 1.00 13.85 ? 238 ILE A C 1 ATOM 1665 O O . ILE A 1 217 ? 8.271 10.324 -2.861 1.00 13.59 ? 238 ILE A O 1 ATOM 1666 C CB . ILE A 1 217 ? 7.423 9.226 0.194 1.00 13.25 ? 238 ILE A CB 1 ATOM 1667 C CG1 . ILE A 1 217 ? 8.091 8.974 1.544 1.00 12.50 ? 238 ILE A CG1 1 ATOM 1668 C CG2 . ILE A 1 217 ? 7.507 7.995 -0.723 1.00 14.63 ? 238 ILE A CG2 1 ATOM 1669 C CD1 . ILE A 1 217 ? 7.220 8.132 2.486 1.00 13.44 ? 238 ILE A CD1 1 ATOM 1670 N N . GLN A 1 218 ? 6.309 11.028 -2.016 1.00 13.48 ? 239 GLN A N 1 ATOM 1671 C CA . GLN A 1 218 ? 5.716 11.137 -3.343 1.00 14.23 ? 239 GLN A CA 1 ATOM 1672 C C . GLN A 1 218 ? 6.429 12.193 -4.148 1.00 15.10 ? 239 GLN A C 1 ATOM 1673 O O . GLN A 1 218 ? 6.608 12.045 -5.347 1.00 14.81 ? 239 GLN A O 1 ATOM 1674 C CB . GLN A 1 218 ? 4.234 11.469 -3.255 1.00 14.07 ? 239 GLN A CB 1 ATOM 1675 C CG . GLN A 1 218 ? 3.416 10.367 -2.643 1.00 13.68 ? 239 GLN A CG 1 ATOM 1676 C CD . GLN A 1 218 ? 1.941 10.605 -2.774 1.00 16.24 ? 239 GLN A CD 1 ATOM 1677 O OE1 . GLN A 1 218 ? 1.149 9.656 -2.916 1.00 17.53 ? 239 GLN A OE1 1 ATOM 1678 N NE2 . GLN A 1 218 ? 1.547 11.871 -2.725 1.00 15.26 ? 239 GLN A NE2 1 ATOM 1679 N N . SER A 1 219 ? 6.852 13.258 -3.481 1.00 15.01 ? 240 SER A N 1 ATOM 1680 C CA . SER A 1 219 ? 7.543 14.325 -4.194 1.00 16.07 ? 240 SER A CA 1 ATOM 1681 C C . SER A 1 219 ? 8.851 13.816 -4.756 1.00 17.04 ? 240 SER A C 1 ATOM 1682 O O . SER A 1 219 ? 9.177 14.054 -5.921 1.00 17.87 ? 240 SER A O 1 ATOM 1683 C CB A SER A 1 219 ? 7.766 15.516 -3.276 0.50 16.41 ? 240 SER A CB 1 ATOM 1684 C CB B SER A 1 219 ? 7.782 15.507 -3.269 0.50 16.82 ? 240 SER A CB 1 ATOM 1685 O OG A SER A 1 219 ? 6.530 16.130 -2.971 0.50 14.46 ? 240 SER A OG 1 ATOM 1686 O OG B SER A 1 219 ? 8.395 16.560 -3.983 0.50 18.70 ? 240 SER A OG 1 ATOM 1687 N N . ILE A 1 220 ? 9.591 13.077 -3.939 1.00 16.87 ? 241 ILE A N 1 ATOM 1688 C CA . ILE A 1 220 ? 10.875 12.543 -4.385 1.00 17.62 ? 241 ILE A CA 1 ATOM 1689 C C . ILE A 1 220 ? 10.716 11.571 -5.543 1.00 18.60 ? 241 ILE A C 1 ATOM 1690 O O . ILE A 1 220 ? 11.397 11.668 -6.577 1.00 19.07 ? 241 ILE A O 1 ATOM 1691 C CB . ILE A 1 220 ? 11.613 11.854 -3.214 1.00 17.91 ? 241 ILE A CB 1 ATOM 1692 C CG1 . ILE A 1 220 ? 12.051 12.876 -2.139 1.00 18.48 ? 241 ILE A CG1 1 ATOM 1693 C CG2 . ILE A 1 220 ? 12.804 11.074 -3.732 1.00 16.99 ? 241 ILE A CG2 1 ATOM 1694 C CD1 . ILE A 1 220 ? 13.215 13.799 -2.559 1.00 25.25 ? 241 ILE A CD1 1 ATOM 1695 N N . ILE A 1 221 ? 9.824 10.608 -5.370 1.00 18.26 ? 242 ILE A N 1 ATOM 1696 C CA . ILE A 1 221 ? 9.725 9.530 -6.336 1.00 19.61 ? 242 ILE A CA 1 ATOM 1697 C C . ILE A 1 221 ? 9.082 10.016 -7.625 1.00 21.69 ? 242 ILE A C 1 ATOM 1698 O O . ILE A 1 221 ? 9.431 9.544 -8.710 1.00 22.07 ? 242 ILE A O 1 ATOM 1699 C CB . ILE A 1 221 ? 8.987 8.341 -5.747 1.00 18.61 ? 242 ILE A CB 1 ATOM 1700 C CG1 . ILE A 1 221 ? 9.752 7.844 -4.513 1.00 18.03 ? 242 ILE A CG1 1 ATOM 1701 C CG2 . ILE A 1 221 ? 8.880 7.212 -6.774 1.00 18.14 ? 242 ILE A CG2 1 ATOM 1702 C CD1 . ILE A 1 221 ? 9.127 6.617 -3.880 1.00 16.67 ? 242 ILE A CD1 1 ATOM 1703 N N . SER A 1 222 ? 8.167 10.977 -7.507 1.00 23.81 ? 243 SER A N 1 ATOM 1704 C CA . SER A 1 222 ? 7.456 11.489 -8.675 1.00 27.23 ? 243 SER A CA 1 ATOM 1705 C C . SER A 1 222 ? 8.316 12.453 -9.465 1.00 28.87 ? 243 SER A C 1 ATOM 1706 O O . SER A 1 222 ? 7.941 12.865 -10.564 1.00 30.02 ? 243 SER A O 1 ATOM 1707 C CB . SER A 1 222 ? 6.129 12.110 -8.260 1.00 26.55 ? 243 SER A CB 1 ATOM 1708 O OG . SER A 1 222 ? 5.409 11.141 -7.529 1.00 29.21 ? 243 SER A OG 1 ATOM 1709 N N . GLY A 1 223 ? 9.465 12.813 -8.907 0.70 30.60 ? 244 GLY A N 1 ATOM 1710 C CA . GLY A 1 223 ? 10.491 13.511 -9.662 0.70 32.94 ? 244 GLY A CA 1 ATOM 1711 C C . GLY A 1 223 ? 10.483 15.020 -9.564 0.70 34.55 ? 244 GLY A C 1 ATOM 1712 O O . GLY A 1 223 ? 11.302 15.686 -10.206 0.70 34.90 ? 244 GLY A O 1 ATOM 1713 N N . ASN A 1 224 ? 9.572 15.583 -8.776 0.70 36.09 ? 245 ASN A N 1 ATOM 1714 C CA . ASN A 1 224 ? 9.588 17.030 -8.598 0.70 37.23 ? 245 ASN A CA 1 ATOM 1715 C C . ASN A 1 224 ? 10.678 17.417 -7.603 0.70 37.57 ? 245 ASN A C 1 ATOM 1716 O O . ASN A 1 224 ? 10.847 16.780 -6.563 0.70 37.93 ? 245 ASN A O 1 ATOM 1717 C CB . ASN A 1 224 ? 8.206 17.599 -8.266 0.70 37.55 ? 245 ASN A CB 1 ATOM 1718 C CG . ASN A 1 224 ? 7.744 17.252 -6.879 0.70 38.56 ? 245 ASN A CG 1 ATOM 1719 O OD1 . ASN A 1 224 ? 8.203 17.835 -5.892 0.70 41.69 ? 245 ASN A OD1 1 ATOM 1720 N ND2 . ASN A 1 224 ? 6.805 16.319 -6.789 0.70 39.66 ? 245 ASN A ND2 1 ATOM 1721 N N . THR A 1 225 A 11.420 18.458 -7.960 0.70 37.97 ? 245 THR A N 1 ATOM 1722 C CA . THR A 1 225 A 12.765 18.685 -7.436 0.70 38.14 ? 245 THR A CA 1 ATOM 1723 C C . THR A 1 225 A 12.857 19.236 -6.021 0.70 38.07 ? 245 THR A C 1 ATOM 1724 O O . THR A 1 225 A 12.140 20.169 -5.641 0.70 38.09 ? 245 THR A O 1 ATOM 1725 C CB . THR A 1 225 A 13.583 19.567 -8.387 0.70 38.21 ? 245 THR A CB 1 ATOM 1726 O OG1 . THR A 1 225 A 12.718 20.546 -8.969 0.70 38.60 ? 245 THR A OG1 1 ATOM 1727 C CG2 . THR A 1 225 A 14.190 18.713 -9.492 0.70 38.33 ? 245 THR A CG2 1 ATOM 1728 N N . ASP A 1 226 B 13.765 18.620 -5.265 0.70 37.81 ? 245 ASP A N 1 ATOM 1729 C CA . ASP A 1 226 B 14.077 18.960 -3.875 0.70 37.31 ? 245 ASP A CA 1 ATOM 1730 C C . ASP A 1 226 B 12.857 19.246 -2.990 0.70 36.21 ? 245 ASP A C 1 ATOM 1731 O O . ASP A 1 226 B 12.709 20.330 -2.402 0.70 36.62 ? 245 ASP A O 1 ATOM 1732 C CB . ASP A 1 226 B 15.158 20.045 -3.798 0.70 37.80 ? 245 ASP A CB 1 ATOM 1733 C CG . ASP A 1 226 B 16.550 19.512 -4.140 0.70 38.87 ? 245 ASP A CG 1 ATOM 1734 O OD1 . ASP A 1 226 B 16.746 18.979 -5.257 0.70 40.61 ? 245 ASP A OD1 1 ATOM 1735 O OD2 . ASP A 1 226 B 17.463 19.642 -3.295 0.70 41.21 ? 245 ASP A OD2 1 ATOM 1736 N N . ALA A 1 227 C 11.978 18.245 -2.956 1.00 34.84 ? 245 ALA A N 1 ATOM 1737 C CA . ALA A 1 227 C 10.982 18.024 -1.909 1.00 32.52 ? 245 ALA A CA 1 ATOM 1738 C C . ALA A 1 227 C 11.507 18.507 -0.571 1.00 31.06 ? 245 ALA A C 1 ATOM 1739 O O . ALA A 1 227 C 12.706 18.715 -0.415 1.00 31.70 ? 245 ALA A O 1 ATOM 1740 C CB . ALA A 1 227 C 10.724 16.546 -1.820 1.00 32.44 ? 245 ALA A CB 1 ATOM 1741 N N . THR A 1 228 D 10.626 18.657 0.408 1.00 28.96 ? 245 THR A N 1 ATOM 1742 C CA . THR A 1 228 D 11.073 18.945 1.766 1.00 27.12 ? 245 THR A CA 1 ATOM 1743 C C . THR A 1 228 D 10.402 18.009 2.760 1.00 25.61 ? 245 THR A C 1 ATOM 1744 O O . THR A 1 228 D 9.264 17.582 2.569 1.00 24.47 ? 245 THR A O 1 ATOM 1745 C CB . THR A 1 228 D 10.785 20.400 2.174 1.00 27.17 ? 245 THR A CB 1 ATOM 1746 O OG1 . THR A 1 228 D 9.373 20.623 2.152 1.00 28.65 ? 245 THR A OG1 1 ATOM 1747 C CG2 . THR A 1 228 D 11.451 21.365 1.219 1.00 27.91 ? 245 THR A CG2 1 ATOM 1748 N N . CYS A 1 229 E 11.115 17.685 3.829 1.00 24.61 ? 245 CYS A N 1 ATOM 1749 C CA . CYS A 1 229 E 10.530 16.864 4.873 1.00 23.94 ? 245 CYS A CA 1 ATOM 1750 C C . CYS A 1 229 E 9.539 17.636 5.717 1.00 25.40 ? 245 CYS A C 1 ATOM 1751 O O . CYS A 1 229 E 9.607 18.868 5.782 1.00 25.34 ? 245 CYS A O 1 ATOM 1752 C CB . CYS A 1 229 E 11.627 16.288 5.748 1.00 22.98 ? 245 CYS A CB 1 ATOM 1753 S SG . CYS A 1 229 E 12.431 14.968 4.884 1.00 19.41 ? 245 CYS A SG 1 ATOM 1754 N N . PRO A 1 230 F 8.617 16.919 6.375 1.00 26.28 ? 245 PRO A N 1 ATOM 1755 C CA . PRO A 1 230 F 7.702 17.558 7.310 1.00 28.16 ? 245 PRO A CA 1 ATOM 1756 C C . PRO A 1 230 F 8.468 18.070 8.524 1.00 31.01 ? 245 PRO A C 1 ATOM 1757 O O . PRO A 1 230 F 9.503 17.492 8.876 1.00 31.57 ? 245 PRO A O 1 ATOM 1758 C CB . PRO A 1 230 F 6.789 16.407 7.734 1.00 27.96 ? 245 PRO A CB 1 ATOM 1759 C CG . PRO A 1 230 F 7.616 15.186 7.541 1.00 25.95 ? 245 PRO A CG 1 ATOM 1760 C CD . PRO A 1 230 F 8.379 15.467 6.295 1.00 25.92 ? 245 PRO A CD 1 ATOM 1761 N N . PRO A 1 231 G 8.002 19.180 9.130 1.00 33.39 ? 245 PRO A N 1 ATOM 1762 C CA . PRO A 1 231 G 8.418 19.569 10.487 1.00 34.81 ? 245 PRO A CA 1 ATOM 1763 C C . PRO A 1 231 G 8.032 18.518 11.521 1.00 36.05 ? 245 PRO A C 1 ATOM 1764 O O . PRO A 1 231 G 6.841 18.216 11.687 1.00 37.31 ? 245 PRO A O 1 ATOM 1765 C CB . PRO A 1 231 G 7.622 20.857 10.746 1.00 35.06 ? 245 PRO A CB 1 ATOM 1766 C CG . PRO A 1 231 G 6.522 20.873 9.691 1.00 34.88 ? 245 PRO A CG 1 ATOM 1767 C CD . PRO A 1 231 G 7.108 20.178 8.513 1.00 33.63 ? 245 PRO A CD 1 ATOM 1768 O OXT . PRO A 1 231 G 8.881 17.946 12.223 1.00 37.23 ? 245 PRO A OXT 1 HETATM 1769 C C1 . NAG B 2 . ? 25.326 -9.369 28.611 0.50 38.33 ? 601 NAG A C1 1 HETATM 1770 C C2 . NAG B 2 . ? 26.138 -10.193 29.597 0.50 40.32 ? 601 NAG A C2 1 HETATM 1771 C C3 . NAG B 2 . ? 25.301 -10.451 30.854 0.50 40.42 ? 601 NAG A C3 1 HETATM 1772 C C4 . NAG B 2 . ? 24.418 -9.280 31.311 0.50 40.11 ? 601 NAG A C4 1 HETATM 1773 C C5 . NAG B 2 . ? 24.138 -8.158 30.294 0.50 39.58 ? 601 NAG A C5 1 HETATM 1774 C C6 . NAG B 2 . ? 24.164 -6.822 31.034 0.50 38.92 ? 601 NAG A C6 1 HETATM 1775 C C7 . NAG B 2 . ? 26.359 -12.660 29.331 0.50 41.87 ? 601 NAG A C7 1 HETATM 1776 C C8 . NAG B 2 . ? 25.381 -13.468 28.528 0.50 41.61 ? 601 NAG A C8 1 HETATM 1777 N N2 . NAG B 2 . ? 26.583 -11.406 28.922 0.50 40.95 ? 601 NAG A N2 1 HETATM 1778 O O3 . NAG B 2 . ? 26.160 -10.798 31.919 0.50 41.13 ? 601 NAG A O3 1 HETATM 1779 O O4 . NAG B 2 . ? 23.176 -9.793 31.750 0.50 40.09 ? 601 NAG A O4 1 HETATM 1780 O O5 . NAG B 2 . ? 25.034 -8.112 29.192 0.50 38.88 ? 601 NAG A O5 1 HETATM 1781 O O6 . NAG B 2 . ? 23.979 -5.742 30.147 0.50 38.39 ? 601 NAG A O6 1 HETATM 1782 O O7 . NAG B 2 . ? 26.923 -13.163 30.306 0.50 42.54 ? 601 NAG A O7 1 HETATM 1783 C C1 . NAG C 2 . ? 24.309 16.920 17.602 0.50 38.95 ? 701 NAG A C1 1 HETATM 1784 C C2 . NAG C 2 . ? 25.738 17.468 17.626 0.50 40.74 ? 701 NAG A C2 1 HETATM 1785 C C3 . NAG C 2 . ? 26.764 16.449 17.112 0.50 41.04 ? 701 NAG A C3 1 HETATM 1786 C C4 . NAG C 2 . ? 26.488 15.008 17.550 0.50 41.51 ? 701 NAG A C4 1 HETATM 1787 C C5 . NAG C 2 . ? 24.994 14.685 17.506 0.50 41.47 ? 701 NAG A C5 1 HETATM 1788 C C6 . NAG C 2 . ? 24.694 13.313 18.093 0.50 42.06 ? 701 NAG A C6 1 HETATM 1789 C C7 . NAG C 2 . ? 26.645 19.679 17.086 0.50 42.19 ? 701 NAG A C7 1 HETATM 1790 C C8 . NAG C 2 . ? 26.099 21.073 16.979 0.50 42.61 ? 701 NAG A C8 1 HETATM 1791 N N2 . NAG C 2 . ? 25.795 18.683 16.834 0.50 41.59 ? 701 NAG A N2 1 HETATM 1792 O O3 . NAG C 2 . ? 28.048 16.819 17.566 0.50 41.66 ? 701 NAG A O3 1 HETATM 1793 O O4 . NAG C 2 . ? 27.188 14.134 16.690 0.50 41.76 ? 701 NAG A O4 1 HETATM 1794 O O5 . NAG C 2 . ? 24.280 15.661 18.235 0.50 40.41 ? 701 NAG A O5 1 HETATM 1795 O O6 . NAG C 2 . ? 24.507 12.416 17.025 0.50 42.89 ? 701 NAG A O6 1 HETATM 1796 O O7 . NAG C 2 . ? 27.828 19.500 17.382 0.50 42.78 ? 701 NAG A O7 1 HETATM 1797 C C1 . NDG D 3 . ? 31.088 1.324 10.098 0.20 32.38 ? 801 NDG A C1 1 HETATM 1798 C C2 . NDG D 3 . ? 32.103 1.387 11.238 0.20 33.41 ? 801 NDG A C2 1 HETATM 1799 C C3 . NDG D 3 . ? 31.401 1.567 12.581 0.20 33.56 ? 801 NDG A C3 1 HETATM 1800 C C4 . NDG D 3 . ? 30.389 2.709 12.547 0.20 33.70 ? 801 NDG A C4 1 HETATM 1801 C C5 . NDG D 3 . ? 29.498 2.675 11.299 0.20 33.54 ? 801 NDG A C5 1 HETATM 1802 C C6 . NDG D 3 . ? 28.726 3.983 11.143 0.20 33.58 ? 801 NDG A C6 1 HETATM 1803 C C7 . NDG D 3 . ? 34.239 0.212 11.243 0.20 33.62 ? 801 NDG A C7 1 HETATM 1804 C C8 . NDG D 3 . ? 34.905 -0.689 10.240 0.20 33.46 ? 801 NDG A C8 1 HETATM 1805 O O . NDG D 3 . ? 30.256 2.473 10.114 0.20 33.09 ? 801 NDG A O 1 HETATM 1806 O O3 . NDG D 3 . ? 32.358 1.842 13.578 0.20 33.79 ? 801 NDG A O3 1 HETATM 1807 O O4 . NDG D 3 . ? 29.587 2.628 13.707 0.20 33.93 ? 801 NDG A O4 1 HETATM 1808 O O6 . NDG D 3 . ? 27.888 4.202 12.288 0.20 33.87 ? 801 NDG A O6 1 HETATM 1809 O O7 . NDG D 3 . ? 34.918 0.930 11.991 0.20 33.93 ? 801 NDG A O7 1 HETATM 1810 N N2 . NDG D 3 . ? 32.903 0.176 11.266 0.20 33.61 ? 801 NDG A N2 1 HETATM 1811 S S . SO4 E 4 . ? 20.000 -0.531 15.805 1.00 44.11 ? 301 SO4 A S 1 HETATM 1812 O O1 . SO4 E 4 . ? 21.162 -1.422 15.826 1.00 45.03 ? 301 SO4 A O1 1 HETATM 1813 O O2 . SO4 E 4 . ? 18.757 -1.318 15.749 1.00 43.08 ? 301 SO4 A O2 1 HETATM 1814 O O3 . SO4 E 4 . ? 20.114 0.307 14.611 1.00 41.84 ? 301 SO4 A O3 1 HETATM 1815 O O4 . SO4 E 4 . ? 19.986 0.280 17.023 1.00 44.27 ? 301 SO4 A O4 1 HETATM 1816 S S . SO4 F 4 . ? -6.152 2.892 12.390 1.00 40.08 ? 302 SO4 A S 1 HETATM 1817 O O1 . SO4 F 4 . ? -7.121 1.795 12.256 1.00 39.70 ? 302 SO4 A O1 1 HETATM 1818 O O2 . SO4 F 4 . ? -5.157 2.551 13.401 1.00 40.89 ? 302 SO4 A O2 1 HETATM 1819 O O3 . SO4 F 4 . ? -6.871 4.098 12.806 1.00 39.59 ? 302 SO4 A O3 1 HETATM 1820 O O4 . SO4 F 4 . ? -5.465 3.105 11.099 1.00 40.58 ? 302 SO4 A O4 1 HETATM 1821 S S . SO4 G 4 . ? 14.677 18.730 4.328 1.00 38.26 ? 303 SO4 A S 1 HETATM 1822 O O1 . SO4 G 4 . ? 13.370 19.090 3.815 1.00 38.22 ? 303 SO4 A O1 1 HETATM 1823 O O2 . SO4 G 4 . ? 14.534 18.385 5.749 1.00 39.61 ? 303 SO4 A O2 1 HETATM 1824 O O3 . SO4 G 4 . ? 15.602 19.865 4.258 1.00 38.11 ? 303 SO4 A O3 1 HETATM 1825 O O4 . SO4 G 4 . ? 15.235 17.636 3.518 1.00 37.79 ? 303 SO4 A O4 1 HETATM 1826 C C . ACT H 5 . ? 17.129 -9.501 -11.055 1.00 44.32 ? 501 ACT A C 1 HETATM 1827 O O . ACT H 5 . ? 16.045 -9.821 -10.522 1.00 44.46 ? 501 ACT A O 1 HETATM 1828 O OXT . ACT H 5 . ? 18.163 -9.748 -10.394 1.00 44.04 ? 501 ACT A OXT 1 HETATM 1829 C CH3 . ACT H 5 . ? 17.162 -8.844 -12.405 1.00 44.58 ? 501 ACT A CH3 1 HETATM 1830 C C1 . GOL I 6 . ? 21.365 11.608 16.308 1.00 40.97 ? 401 GOL A C1 1 HETATM 1831 O O1 . GOL I 6 . ? 20.539 12.092 17.347 1.00 39.59 ? 401 GOL A O1 1 HETATM 1832 C C2 . GOL I 6 . ? 21.446 12.614 15.164 1.00 41.77 ? 401 GOL A C2 1 HETATM 1833 O O2 . GOL I 6 . ? 20.166 12.855 14.618 1.00 41.12 ? 401 GOL A O2 1 HETATM 1834 C C3 . GOL I 6 . ? 22.374 12.084 14.074 1.00 42.40 ? 401 GOL A C3 1 HETATM 1835 O O3 . GOL I 6 . ? 22.186 12.799 12.863 1.00 43.34 ? 401 GOL A O3 1 HETATM 1836 O O . HOH J 7 . ? 13.168 -4.851 11.021 1.00 14.05 ? 802 HOH A O 1 HETATM 1837 O O . HOH J 7 . ? 13.824 -10.569 15.537 1.00 15.79 ? 803 HOH A O 1 HETATM 1838 O O . HOH J 7 . ? 10.699 0.691 6.869 1.00 13.86 ? 804 HOH A O 1 HETATM 1839 O O . HOH J 7 . ? 15.470 -6.494 10.876 1.00 14.65 ? 805 HOH A O 1 HETATM 1840 O O . HOH J 7 . ? 11.129 -10.530 3.540 1.00 11.73 ? 806 HOH A O 1 HETATM 1841 O O . HOH J 7 . ? -7.078 3.778 22.237 1.00 20.26 ? 807 HOH A O 1 HETATM 1842 O O . HOH J 7 . ? 9.392 -12.198 2.195 1.00 14.62 ? 808 HOH A O 1 HETATM 1843 O O . HOH J 7 . ? 9.715 -14.786 2.930 1.00 14.79 ? 809 HOH A O 1 HETATM 1844 O O . HOH J 7 . ? 8.865 -1.952 25.843 1.00 16.20 ? 810 HOH A O 1 HETATM 1845 O O . HOH J 7 . ? 14.045 -9.449 2.525 1.00 13.90 ? 811 HOH A O 1 HETATM 1846 O O . HOH J 7 . ? 7.998 -1.398 19.949 1.00 17.51 ? 812 HOH A O 1 HETATM 1847 O O . HOH J 7 . ? 2.145 6.725 9.912 1.00 14.02 ? 813 HOH A O 1 HETATM 1848 O O . HOH J 7 . ? 12.193 9.647 13.529 1.00 15.48 ? 814 HOH A O 1 HETATM 1849 O O . HOH J 7 . ? 15.700 -16.194 2.614 1.00 14.77 ? 815 HOH A O 1 HETATM 1850 O O . HOH J 7 . ? 15.758 11.720 7.162 1.00 15.54 ? 816 HOH A O 1 HETATM 1851 O O . HOH J 7 . ? 13.557 9.139 15.890 1.00 15.43 ? 817 HOH A O 1 HETATM 1852 O O . HOH J 7 . ? -2.698 2.287 23.549 1.00 15.24 ? 818 HOH A O 1 HETATM 1853 O O . HOH J 7 . ? 6.950 -12.780 3.350 1.00 16.51 ? 819 HOH A O 1 HETATM 1854 O O . HOH J 7 . ? -0.484 1.165 -3.984 1.00 18.60 ? 820 HOH A O 1 HETATM 1855 O O . HOH J 7 . ? 11.078 -8.373 0.496 1.00 14.62 ? 821 HOH A O 1 HETATM 1856 O O . HOH J 7 . ? 13.637 -18.800 3.729 1.00 17.62 ? 822 HOH A O 1 HETATM 1857 O O . HOH J 7 . ? 13.300 10.089 18.624 1.00 20.78 ? 823 HOH A O 1 HETATM 1858 O O . HOH J 7 . ? 10.210 15.510 13.033 1.00 25.36 ? 824 HOH A O 1 HETATM 1859 O O . HOH J 7 . ? 11.140 12.082 13.309 1.00 20.20 ? 825 HOH A O 1 HETATM 1860 O O . HOH J 7 . ? 5.794 14.750 3.742 1.00 16.42 ? 826 HOH A O 1 HETATM 1861 O O . HOH J 7 . ? 16.221 -18.635 14.536 1.00 23.84 ? 827 HOH A O 1 HETATM 1862 O O . HOH J 7 . ? 19.590 -12.014 12.371 1.00 18.69 ? 828 HOH A O 1 HETATM 1863 O O . HOH J 7 . ? 12.687 -1.204 26.638 1.00 19.58 ? 829 HOH A O 1 HETATM 1864 O O . HOH J 7 . ? 1.955 7.130 19.360 1.00 16.79 ? 830 HOH A O 1 HETATM 1865 O O . HOH J 7 . ? 20.015 21.226 6.712 1.00 22.87 ? 831 HOH A O 1 HETATM 1866 O O . HOH J 7 . ? 3.329 -10.183 2.914 1.00 19.71 ? 832 HOH A O 1 HETATM 1867 O O . HOH J 7 . ? 9.382 -3.837 12.960 1.00 19.08 ? 833 HOH A O 1 HETATM 1868 O O . HOH J 7 . ? 18.471 14.358 15.780 1.00 22.91 ? 834 HOH A O 1 HETATM 1869 O O . HOH J 7 . ? 11.869 16.265 16.377 1.00 26.77 ? 835 HOH A O 1 HETATM 1870 O O . HOH J 7 . ? 2.606 14.258 3.980 1.00 20.00 ? 836 HOH A O 1 HETATM 1871 O O . HOH J 7 . ? 10.937 -12.881 19.343 1.00 17.85 ? 837 HOH A O 1 HETATM 1872 O O . HOH J 7 . ? 6.858 -2.659 24.186 1.00 20.94 ? 838 HOH A O 1 HETATM 1873 O O . HOH J 7 . ? 0.328 -1.733 -0.598 0.50 9.95 ? 839 HOH A O 1 HETATM 1874 O O . HOH J 7 . ? 17.614 2.983 20.045 1.00 26.22 ? 840 HOH A O 1 HETATM 1875 O O . HOH J 7 . ? 15.842 0.496 -10.224 1.00 19.05 ? 841 HOH A O 1 HETATM 1876 O O . HOH J 7 . ? 2.734 -11.171 19.517 1.00 21.82 ? 842 HOH A O 1 HETATM 1877 O O . HOH J 7 . ? 6.559 -0.190 26.558 1.00 20.34 ? 843 HOH A O 1 HETATM 1878 O O . HOH J 7 . ? 1.679 -1.663 -2.964 1.00 19.27 ? 844 HOH A O 1 HETATM 1879 O O . HOH J 7 . ? 6.601 5.841 29.879 1.00 30.65 ? 845 HOH A O 1 HETATM 1880 O O . HOH J 7 . ? 18.211 2.556 17.443 1.00 36.07 ? 846 HOH A O 1 HETATM 1881 O O . HOH J 7 . ? 0.388 12.918 4.862 1.00 22.59 ? 847 HOH A O 1 HETATM 1882 O O . HOH J 7 . ? 12.748 -12.740 -7.194 1.00 24.52 ? 848 HOH A O 1 HETATM 1883 O O . HOH J 7 . ? 5.383 -7.728 -10.806 1.00 31.32 ? 849 HOH A O 1 HETATM 1884 O O . HOH J 7 . ? 12.555 18.591 13.186 1.00 42.26 ? 850 HOH A O 1 HETATM 1885 O O . HOH J 7 . ? -6.331 -0.073 8.026 1.00 21.23 ? 851 HOH A O 1 HETATM 1886 O O . HOH J 7 . ? 14.066 -7.873 26.826 1.00 25.61 ? 852 HOH A O 1 HETATM 1887 O O . HOH J 7 . ? 3.027 13.933 13.619 1.00 36.32 ? 853 HOH A O 1 HETATM 1888 O O . HOH J 7 . ? -0.954 9.925 21.383 1.00 36.30 ? 854 HOH A O 1 HETATM 1889 O O . HOH J 7 . ? -0.207 -1.874 25.470 1.00 27.91 ? 855 HOH A O 1 HETATM 1890 O O . HOH J 7 . ? -2.224 7.966 29.012 1.00 29.32 ? 856 HOH A O 1 HETATM 1891 O O . HOH J 7 . ? 16.042 22.602 17.638 1.00 31.46 ? 857 HOH A O 1 HETATM 1892 O O . HOH J 7 . ? 12.141 -13.018 22.724 1.00 29.70 ? 858 HOH A O 1 HETATM 1893 O O . HOH J 7 . ? 10.558 18.677 15.738 1.00 31.87 ? 859 HOH A O 1 HETATM 1894 O O . HOH J 7 . ? 14.421 16.282 1.491 1.00 25.88 ? 860 HOH A O 1 HETATM 1895 O O . HOH J 7 . ? 14.771 -5.935 -12.300 1.00 25.93 ? 861 HOH A O 1 HETATM 1896 O O . HOH J 7 . ? 2.963 -9.061 8.714 1.00 29.89 ? 862 HOH A O 1 HETATM 1897 O O . HOH J 7 . ? 11.583 8.372 -9.654 1.00 30.25 ? 863 HOH A O 1 HETATM 1898 O O . HOH J 7 . ? 12.820 -21.274 7.399 1.00 34.37 ? 864 HOH A O 1 HETATM 1899 O O . HOH J 7 . ? 18.966 7.179 -10.858 1.00 35.49 ? 865 HOH A O 1 HETATM 1900 O O . HOH J 7 . ? 10.891 5.376 -9.608 1.00 28.53 ? 866 HOH A O 1 HETATM 1901 O O . HOH J 7 . ? 25.039 -7.508 22.372 1.00 53.80 ? 867 HOH A O 1 HETATM 1902 O O . HOH J 7 . ? 2.169 10.500 16.899 1.00 28.04 ? 868 HOH A O 1 HETATM 1903 O O . HOH J 7 . ? 5.890 -19.801 7.891 1.00 27.06 ? 869 HOH A O 1 HETATM 1904 O O . HOH J 7 . ? 7.882 0.924 -9.529 1.00 33.91 ? 870 HOH A O 1 HETATM 1905 O O . HOH J 7 . ? -1.699 -5.416 4.979 1.00 36.05 ? 871 HOH A O 1 HETATM 1906 O O . HOH J 7 . ? 16.626 -15.274 -6.623 1.00 30.10 ? 872 HOH A O 1 HETATM 1907 O O . HOH J 7 . ? 19.601 -5.008 23.830 1.00 31.09 ? 873 HOH A O 1 HETATM 1908 O O . HOH J 7 . ? 22.239 -2.370 -11.680 1.00 37.81 ? 874 HOH A O 1 HETATM 1909 O O . HOH J 7 . ? 14.256 9.782 -9.187 1.00 32.23 ? 875 HOH A O 1 HETATM 1910 O O . HOH J 7 . ? 5.047 15.435 14.657 1.00 39.79 ? 876 HOH A O 1 HETATM 1911 O O . HOH J 7 . ? 16.510 0.759 -12.640 1.00 30.42 ? 877 HOH A O 1 HETATM 1912 O O . HOH J 7 . ? 21.683 10.402 8.529 1.00 27.85 ? 878 HOH A O 1 HETATM 1913 O O . HOH J 7 . ? 21.332 -3.952 26.890 1.00 42.38 ? 879 HOH A O 1 HETATM 1914 O O . HOH J 7 . ? -1.523 -5.180 10.474 1.00 30.56 ? 880 HOH A O 1 HETATM 1915 O O . HOH J 7 . ? 14.367 -22.147 -0.398 1.00 36.04 ? 881 HOH A O 1 HETATM 1916 O O . HOH J 7 . ? 3.436 -7.025 0.483 1.00 26.05 ? 882 HOH A O 1 HETATM 1917 O O . HOH J 7 . ? -2.284 -0.284 24.168 1.00 25.65 ? 883 HOH A O 1 HETATM 1918 O O . HOH J 7 . ? 0.174 8.813 18.106 1.00 26.71 ? 884 HOH A O 1 HETATM 1919 O O . HOH J 7 . ? 19.730 22.409 19.386 1.00 29.25 ? 885 HOH A O 1 HETATM 1920 O O . HOH J 7 . ? 9.945 -10.578 26.960 1.00 28.70 ? 886 HOH A O 1 HETATM 1921 O O . HOH J 7 . ? 21.808 -11.443 11.142 1.00 42.68 ? 887 HOH A O 1 HETATM 1922 O O . HOH J 7 . ? 11.185 -10.755 -8.011 1.00 31.81 ? 888 HOH A O 1 HETATM 1923 O O . HOH J 7 . ? 1.409 -10.617 -6.280 1.00 41.65 ? 889 HOH A O 1 HETATM 1924 O O . HOH J 7 . ? 3.873 -0.822 32.621 1.00 25.95 ? 890 HOH A O 1 HETATM 1925 O O . HOH J 7 . ? 17.366 -22.188 10.360 1.00 36.15 ? 891 HOH A O 1 HETATM 1926 O O . HOH J 7 . ? 3.780 15.484 -2.729 1.00 36.66 ? 892 HOH A O 1 HETATM 1927 O O . HOH J 7 . ? 4.007 14.904 -5.464 1.00 38.93 ? 893 HOH A O 1 HETATM 1928 O O . HOH J 7 . ? 9.515 -0.248 -11.129 1.00 31.97 ? 894 HOH A O 1 HETATM 1929 O O . HOH J 7 . ? -1.213 8.675 14.927 1.00 41.34 ? 895 HOH A O 1 HETATM 1930 O O . HOH J 7 . ? -6.102 -2.792 15.744 1.00 34.61 ? 896 HOH A O 1 HETATM 1931 O O . HOH J 7 . ? -3.516 2.545 3.259 1.00 33.70 ? 897 HOH A O 1 HETATM 1932 O O . HOH J 7 . ? -1.047 14.983 5.605 1.00 36.10 ? 898 HOH A O 1 HETATM 1933 O O . HOH J 7 . ? 0.691 14.428 7.243 1.00 47.08 ? 899 HOH A O 1 HETATM 1934 O O . HOH J 7 . ? 12.600 -9.256 -9.931 1.00 30.02 ? 900 HOH A O 1 HETATM 1935 O O . HOH J 7 . ? 23.855 20.128 19.123 1.00 48.84 ? 901 HOH A O 1 HETATM 1936 O O . HOH J 7 . ? 17.817 4.992 22.150 1.00 41.11 ? 902 HOH A O 1 HETATM 1937 O O . HOH J 7 . ? 17.251 3.049 27.223 1.00 42.48 ? 903 HOH A O 1 HETATM 1938 O O . HOH J 7 . ? 7.776 -16.592 -7.006 1.00 35.29 ? 904 HOH A O 1 HETATM 1939 O O . HOH J 7 . ? 21.419 18.624 22.022 1.00 36.80 ? 905 HOH A O 1 HETATM 1940 O O . HOH J 7 . ? 4.400 12.239 29.200 1.00 39.57 ? 906 HOH A O 1 HETATM 1941 O O . HOH J 7 . ? 18.447 21.330 17.099 1.00 41.17 ? 907 HOH A O 1 HETATM 1942 O O . HOH J 7 . ? 23.446 -13.915 17.841 1.00 43.46 ? 908 HOH A O 1 HETATM 1943 O O . HOH J 7 . ? 9.866 13.583 26.192 1.00 39.64 ? 909 HOH A O 1 HETATM 1944 O O . HOH J 7 . ? -1.480 -2.880 27.264 1.00 33.97 ? 910 HOH A O 1 HETATM 1945 O O . HOH J 7 . ? 11.546 -20.851 0.615 1.00 36.98 ? 911 HOH A O 1 HETATM 1946 O O . HOH J 7 . ? 6.525 17.296 3.464 1.00 35.64 ? 912 HOH A O 1 HETATM 1947 O O . HOH J 7 . ? 1.955 -9.280 0.735 1.00 38.41 ? 913 HOH A O 1 HETATM 1948 O O . HOH J 7 . ? 16.111 6.301 23.331 1.00 46.89 ? 914 HOH A O 1 HETATM 1949 O O . HOH J 7 . ? 7.805 17.568 0.043 1.00 38.35 ? 915 HOH A O 1 HETATM 1950 O O . HOH J 7 . ? 10.113 -0.405 33.270 1.00 39.32 ? 916 HOH A O 1 HETATM 1951 O O . HOH J 7 . ? 6.241 -19.340 0.919 1.00 31.15 ? 917 HOH A O 1 HETATM 1952 O O . HOH J 7 . ? 7.834 20.842 5.283 1.00 45.31 ? 918 HOH A O 1 HETATM 1953 O O . HOH J 7 . ? 3.447 -15.582 -0.573 1.00 42.08 ? 919 HOH A O 1 HETATM 1954 O O . HOH J 7 . ? 8.154 14.638 20.322 1.00 41.66 ? 920 HOH A O 1 HETATM 1955 O O . HOH J 7 . ? 22.263 -3.019 13.679 1.00 38.05 ? 921 HOH A O 1 HETATM 1956 O O . HOH J 7 . ? 9.101 -15.117 22.301 1.00 44.89 ? 922 HOH A O 1 HETATM 1957 O O . HOH J 7 . ? -2.916 -4.849 12.830 1.00 36.64 ? 923 HOH A O 1 HETATM 1958 O O . HOH J 7 . ? 12.316 -21.084 5.017 1.00 38.93 ? 924 HOH A O 1 HETATM 1959 O O . HOH J 7 . ? 4.222 16.556 10.502 1.00 42.32 ? 925 HOH A O 1 HETATM 1960 O O . HOH J 7 . ? 13.988 -18.354 15.559 1.00 36.81 ? 926 HOH A O 1 HETATM 1961 O O . HOH J 7 . ? 21.962 -6.094 -7.497 1.00 28.16 ? 927 HOH A O 1 HETATM 1962 O O . HOH J 7 . ? 0.597 -8.261 21.897 1.00 36.31 ? 928 HOH A O 1 HETATM 1963 O O . HOH J 7 . ? 7.794 -6.175 -5.834 1.00 28.64 ? 929 HOH A O 1 HETATM 1964 O O . HOH J 7 . ? 9.321 11.233 32.812 1.00 47.75 ? 930 HOH A O 1 HETATM 1965 O O . HOH J 7 . ? 14.818 -14.388 -8.813 1.00 43.12 ? 931 HOH A O 1 HETATM 1966 O O . HOH J 7 . ? 5.693 11.667 -11.939 1.00 46.85 ? 932 HOH A O 1 HETATM 1967 O O . HOH J 7 . ? 10.603 13.036 30.651 1.00 52.48 ? 933 HOH A O 1 HETATM 1968 O O . HOH J 7 . ? 1.579 13.707 24.057 1.00 37.88 ? 934 HOH A O 1 HETATM 1969 O O . HOH J 7 . ? 26.156 -0.442 -1.579 1.00 37.12 ? 935 HOH A O 1 HETATM 1970 O O . HOH J 7 . ? 9.186 -18.924 16.829 1.00 35.76 ? 936 HOH A O 1 HETATM 1971 O O . HOH J 7 . ? -1.071 -8.555 13.833 1.00 34.95 ? 937 HOH A O 1 HETATM 1972 O O . HOH J 7 . ? 3.804 5.729 31.229 1.00 39.33 ? 938 HOH A O 1 HETATM 1973 O O . HOH J 7 . ? 5.608 0.696 34.180 1.00 37.49 ? 939 HOH A O 1 HETATM 1974 O O . HOH J 7 . ? 7.730 15.432 22.850 1.00 44.43 ? 940 HOH A O 1 HETATM 1975 O O . HOH J 7 . ? 11.490 -14.884 21.117 1.00 46.97 ? 941 HOH A O 1 HETATM 1976 O O . HOH J 7 . ? 0.275 13.195 11.745 1.00 38.64 ? 942 HOH A O 1 HETATM 1977 O O . HOH J 7 . ? 24.095 5.423 12.393 1.00 41.29 ? 943 HOH A O 1 HETATM 1978 O O . HOH J 7 . ? 5.557 -12.550 24.750 1.00 42.85 ? 944 HOH A O 1 HETATM 1979 O O . HOH J 7 . ? 9.727 -19.657 -3.570 1.00 44.84 ? 945 HOH A O 1 HETATM 1980 O O . HOH J 7 . ? 12.461 -1.751 33.556 1.00 34.75 ? 946 HOH A O 1 HETATM 1981 O O . HOH J 7 . ? 20.526 4.029 17.019 1.00 50.25 ? 947 HOH A O 1 HETATM 1982 O O . HOH J 7 . ? 9.721 -18.474 -5.749 1.00 45.34 ? 948 HOH A O 1 HETATM 1983 O O . HOH J 7 . ? 9.012 -2.590 -11.887 1.00 38.41 ? 949 HOH A O 1 HETATM 1984 O O . HOH J 7 . ? 1.539 -0.649 33.087 1.00 38.58 ? 950 HOH A O 1 HETATM 1985 O O . HOH J 7 . ? 23.848 5.858 -7.654 1.00 37.56 ? 951 HOH A O 1 HETATM 1986 O O . HOH J 7 . ? -6.613 8.658 11.337 1.00 47.87 ? 952 HOH A O 1 HETATM 1987 O O . HOH J 7 . ? 23.147 8.193 9.490 1.00 47.62 ? 953 HOH A O 1 HETATM 1988 O O . HOH J 7 . ? -4.163 -2.076 23.935 0.50 54.42 ? 954 HOH A O 1 HETATM 1989 O O . HOH J 7 . ? -0.710 -11.359 20.124 1.00 46.76 ? 955 HOH A O 1 HETATM 1990 O O . HOH J 7 . ? -4.939 -4.804 21.428 1.00 51.67 ? 956 HOH A O 1 HETATM 1991 O O . HOH J 7 . ? -1.397 -6.274 21.665 1.00 46.99 ? 957 HOH A O 1 HETATM 1992 O O . HOH J 7 . ? 0.842 -3.999 -0.765 1.00 37.03 ? 958 HOH A O 1 HETATM 1993 O O . HOH J 7 . ? 13.194 9.980 31.150 1.00 47.46 ? 959 HOH A O 1 HETATM 1994 O O . HOH J 7 . ? 0.374 -6.433 5.786 1.00 40.99 ? 960 HOH A O 1 HETATM 1995 O O . HOH J 7 . ? 4.629 14.903 17.722 1.00 50.53 ? 961 HOH A O 1 HETATM 1996 O O . HOH J 7 . ? 10.949 14.557 24.409 1.00 46.81 ? 962 HOH A O 1 HETATM 1997 O O . HOH J 7 . ? 11.180 16.151 22.398 1.00 39.33 ? 963 HOH A O 1 HETATM 1998 O O . HOH J 7 . ? 10.292 -7.758 29.634 1.00 39.86 ? 964 HOH A O 1 HETATM 1999 O O . HOH J 7 . ? 21.459 -15.807 11.021 1.00 48.11 ? 965 HOH A O 1 HETATM 2000 O O . HOH J 7 . ? 4.824 -4.918 33.350 1.00 30.27 ? 966 HOH A O 1 HETATM 2001 O O . HOH J 7 . ? 15.576 14.603 0.529 1.00 39.72 ? 967 HOH A O 1 HETATM 2002 O O . HOH J 7 . ? 4.317 -15.325 13.730 1.00 33.81 ? 968 HOH A O 1 HETATM 2003 O O . HOH J 7 . ? 21.273 7.489 -9.555 1.00 40.43 ? 969 HOH A O 1 HETATM 2004 O O . HOH J 7 . ? 0.883 -18.648 4.903 1.00 50.90 ? 970 HOH A O 1 HETATM 2005 O O . HOH J 7 . ? -3.251 1.942 10.577 1.00 25.99 ? 971 HOH A O 1 HETATM 2006 O O . HOH J 7 . ? 11.607 -20.492 -2.084 1.00 27.94 ? 972 HOH A O 1 HETATM 2007 O O . HOH J 7 . ? 3.529 -13.064 -7.106 1.00 46.96 ? 973 HOH A O 1 HETATM 2008 O O . HOH J 7 . ? 24.093 -5.373 -2.942 1.00 30.60 ? 974 HOH A O 1 HETATM 2009 O O . HOH J 7 . ? 12.051 -0.126 24.238 1.00 25.48 ? 975 HOH A O 1 HETATM 2010 O O . HOH J 7 . ? 18.998 -2.268 13.667 1.00 32.51 ? 976 HOH A O 1 HETATM 2011 O O . HOH J 7 . ? 15.841 -0.360 18.722 1.00 38.68 ? 977 HOH A O 1 HETATM 2012 O O . HOH J 7 . ? 12.043 -0.658 20.389 1.00 20.40 ? 978 HOH A O 1 HETATM 2013 O O . HOH J 7 . ? 14.409 -0.799 20.995 1.00 37.61 ? 979 HOH A O 1 HETATM 2014 O O . HOH J 7 . ? 25.875 2.959 0.278 1.00 35.58 ? 980 HOH A O 1 HETATM 2015 O O . HOH J 7 . ? 25.908 -8.839 3.033 1.00 48.53 ? 981 HOH A O 1 HETATM 2016 O O . HOH J 7 . ? 20.885 -6.658 22.488 1.00 43.02 ? 982 HOH A O 1 HETATM 2017 O O . HOH J 7 . ? 7.646 6.600 32.780 1.00 49.60 ? 983 HOH A O 1 HETATM 2018 O O . HOH J 7 . ? 12.501 19.548 6.983 1.00 32.09 ? 984 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 1 601 601 NAG NAG A . C 2 NAG 1 701 701 NAG NAG A . D 3 NDG 1 801 801 NDG NAG A . E 4 SO4 1 301 301 SO4 SO4 A . F 4 SO4 1 302 302 SO4 SO4 A . G 4 SO4 1 303 303 SO4 SO4 A . H 5 ACT 1 501 501 ACT ACT A . I 6 GOL 1 401 401 GOL GOL A . J 7 HOH 1 802 1 HOH HOH A . J 7 HOH 2 803 2 HOH HOH A . J 7 HOH 3 804 3 HOH HOH A . J 7 HOH 4 805 4 HOH HOH A . J 7 HOH 5 806 5 HOH HOH A . J 7 HOH 6 807 6 HOH HOH A . J 7 HOH 7 808 7 HOH HOH A . J 7 HOH 8 809 8 HOH HOH A . J 7 HOH 9 810 9 HOH HOH A . J 7 HOH 10 811 10 HOH HOH A . J 7 HOH 11 812 11 HOH HOH A . J 7 HOH 12 813 12 HOH HOH A . J 7 HOH 13 814 13 HOH HOH A . J 7 HOH 14 815 14 HOH HOH A . J 7 HOH 15 816 15 HOH HOH A . J 7 HOH 16 817 16 HOH HOH A . J 7 HOH 17 818 17 HOH HOH A . J 7 HOH 18 819 18 HOH HOH A . J 7 HOH 19 820 19 HOH HOH A . J 7 HOH 20 821 20 HOH HOH A . J 7 HOH 21 822 21 HOH HOH A . J 7 HOH 22 823 22 HOH HOH A . J 7 HOH 23 824 23 HOH HOH A . J 7 HOH 24 825 24 HOH HOH A . J 7 HOH 25 826 25 HOH HOH A . J 7 HOH 26 827 26 HOH HOH A . J 7 HOH 27 828 27 HOH HOH A . J 7 HOH 28 829 28 HOH HOH A . J 7 HOH 29 830 29 HOH HOH A . J 7 HOH 30 831 30 HOH HOH A . J 7 HOH 31 832 31 HOH HOH A . J 7 HOH 32 833 32 HOH HOH A . J 7 HOH 33 834 33 HOH HOH A . J 7 HOH 34 835 34 HOH HOH A . J 7 HOH 35 836 35 HOH HOH A . J 7 HOH 36 837 36 HOH HOH A . J 7 HOH 37 838 37 HOH HOH A . J 7 HOH 38 839 38 HOH HOH A . J 7 HOH 39 840 39 HOH HOH A . J 7 HOH 40 841 40 HOH HOH A . J 7 HOH 41 842 41 HOH HOH A . J 7 HOH 42 843 42 HOH HOH A . J 7 HOH 43 844 43 HOH HOH A . J 7 HOH 44 845 44 HOH HOH A . J 7 HOH 45 846 45 HOH HOH A . J 7 HOH 46 847 46 HOH HOH A . J 7 HOH 47 848 47 HOH HOH A . J 7 HOH 48 849 48 HOH HOH A . J 7 HOH 49 850 49 HOH HOH A . J 7 HOH 50 851 50 HOH HOH A . J 7 HOH 51 852 51 HOH HOH A . J 7 HOH 52 853 52 HOH HOH A . J 7 HOH 53 854 53 HOH HOH A . J 7 HOH 54 855 54 HOH HOH A . J 7 HOH 55 856 55 HOH HOH A . J 7 HOH 56 857 56 HOH HOH A . J 7 HOH 57 858 57 HOH HOH A . J 7 HOH 58 859 58 HOH HOH A . J 7 HOH 59 860 59 HOH HOH A . J 7 HOH 60 861 60 HOH HOH A . J 7 HOH 61 862 61 HOH HOH A . J 7 HOH 62 863 62 HOH HOH A . J 7 HOH 63 864 63 HOH HOH A . J 7 HOH 64 865 64 HOH HOH A . J 7 HOH 65 866 65 HOH HOH A . J 7 HOH 66 867 66 HOH HOH A . J 7 HOH 67 868 67 HOH HOH A . J 7 HOH 68 869 68 HOH HOH A . J 7 HOH 69 870 69 HOH HOH A . J 7 HOH 70 871 70 HOH HOH A . J 7 HOH 71 872 71 HOH HOH A . J 7 HOH 72 873 72 HOH HOH A . J 7 HOH 73 874 73 HOH HOH A . J 7 HOH 74 875 74 HOH HOH A . J 7 HOH 75 876 75 HOH HOH A . J 7 HOH 76 877 76 HOH HOH A . J 7 HOH 77 878 77 HOH HOH A . J 7 HOH 78 879 78 HOH HOH A . J 7 HOH 79 880 79 HOH HOH A . J 7 HOH 80 881 80 HOH HOH A . J 7 HOH 81 882 81 HOH HOH A . J 7 HOH 82 883 82 HOH HOH A . J 7 HOH 83 884 83 HOH HOH A . J 7 HOH 84 885 84 HOH HOH A . J 7 HOH 85 886 85 HOH HOH A . J 7 HOH 86 887 86 HOH HOH A . J 7 HOH 87 888 87 HOH HOH A . J 7 HOH 88 889 88 HOH HOH A . J 7 HOH 89 890 89 HOH HOH A . J 7 HOH 90 891 90 HOH HOH A . J 7 HOH 91 892 91 HOH HOH A . J 7 HOH 92 893 92 HOH HOH A . J 7 HOH 93 894 93 HOH HOH A . J 7 HOH 94 895 94 HOH HOH A . J 7 HOH 95 896 95 HOH HOH A . J 7 HOH 96 897 96 HOH HOH A . J 7 HOH 97 898 97 HOH HOH A . J 7 HOH 98 899 98 HOH HOH A . J 7 HOH 99 900 99 HOH HOH A . J 7 HOH 100 901 100 HOH HOH A . J 7 HOH 101 902 101 HOH HOH A . J 7 HOH 102 903 102 HOH HOH A . J 7 HOH 103 904 103 HOH HOH A . J 7 HOH 104 905 104 HOH HOH A . J 7 HOH 105 906 105 HOH HOH A . J 7 HOH 106 907 106 HOH HOH A . J 7 HOH 107 908 107 HOH HOH A . J 7 HOH 108 909 108 HOH HOH A . J 7 HOH 109 910 109 HOH HOH A . J 7 HOH 110 911 110 HOH HOH A . J 7 HOH 111 912 111 HOH HOH A . J 7 HOH 112 913 112 HOH HOH A . J 7 HOH 113 914 114 HOH HOH A . J 7 HOH 114 915 115 HOH HOH A . J 7 HOH 115 916 116 HOH HOH A . J 7 HOH 116 917 117 HOH HOH A . J 7 HOH 117 918 118 HOH HOH A . J 7 HOH 118 919 119 HOH HOH A . J 7 HOH 119 920 120 HOH HOH A . J 7 HOH 120 921 121 HOH HOH A . J 7 HOH 121 922 122 HOH HOH A . J 7 HOH 122 923 123 HOH HOH A . J 7 HOH 123 924 124 HOH HOH A . J 7 HOH 124 925 126 HOH HOH A . J 7 HOH 125 926 127 HOH HOH A . J 7 HOH 126 927 129 HOH HOH A . J 7 HOH 127 928 130 HOH HOH A . J 7 HOH 128 929 131 HOH HOH A . J 7 HOH 129 930 132 HOH HOH A . J 7 HOH 130 931 133 HOH HOH A . J 7 HOH 131 932 134 HOH HOH A . J 7 HOH 132 933 135 HOH HOH A . J 7 HOH 133 934 136 HOH HOH A . J 7 HOH 134 935 137 HOH HOH A . J 7 HOH 135 936 138 HOH HOH A . J 7 HOH 136 937 139 HOH HOH A . J 7 HOH 137 938 140 HOH HOH A . J 7 HOH 138 939 141 HOH HOH A . J 7 HOH 139 940 143 HOH HOH A . J 7 HOH 140 941 144 HOH HOH A . J 7 HOH 141 942 145 HOH HOH A . J 7 HOH 142 943 146 HOH HOH A . J 7 HOH 143 944 147 HOH HOH A . J 7 HOH 144 945 148 HOH HOH A . J 7 HOH 145 946 149 HOH HOH A . J 7 HOH 146 947 150 HOH HOH A . J 7 HOH 147 948 151 HOH HOH A . J 7 HOH 148 949 152 HOH HOH A . J 7 HOH 149 950 153 HOH HOH A . J 7 HOH 150 951 154 HOH HOH A . J 7 HOH 151 952 155 HOH HOH A . J 7 HOH 152 953 156 HOH HOH A . J 7 HOH 153 954 157 HOH HOH A . J 7 HOH 154 955 158 HOH HOH A . J 7 HOH 155 956 159 HOH HOH A . J 7 HOH 156 957 160 HOH HOH A . J 7 HOH 157 958 161 HOH HOH A . J 7 HOH 158 959 163 HOH HOH A . J 7 HOH 159 960 164 HOH HOH A . J 7 HOH 160 961 165 HOH HOH A . J 7 HOH 161 962 166 HOH HOH A . J 7 HOH 162 963 167 HOH HOH A . J 7 HOH 163 964 168 HOH HOH A . J 7 HOH 164 965 169 HOH HOH A . J 7 HOH 165 966 170 HOH HOH A . J 7 HOH 166 967 171 HOH HOH A . J 7 HOH 167 968 172 HOH HOH A . J 7 HOH 168 969 173 HOH HOH A . J 7 HOH 169 970 174 HOH HOH A . J 7 HOH 170 971 175 HOH HOH A . J 7 HOH 171 972 176 HOH HOH A . J 7 HOH 172 973 177 HOH HOH A . J 7 HOH 173 974 178 HOH HOH A . J 7 HOH 174 975 179 HOH HOH A . J 7 HOH 175 976 180 HOH HOH A . J 7 HOH 176 977 181 HOH HOH A . J 7 HOH 177 978 182 HOH HOH A . J 7 HOH 178 979 183 HOH HOH A . J 7 HOH 179 980 184 HOH HOH A . J 7 HOH 180 981 185 HOH HOH A . J 7 HOH 181 982 186 HOH HOH A . J 7 HOH 182 983 187 HOH HOH A . J 7 HOH 183 984 188 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 # 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 # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 ASN A 48 ? ? -163.76 -169.18 2 1 HIS A 71 ? ? -125.89 -83.19 3 1 ASN A 148 ? ? 75.45 116.36 4 1 LYS A 174 ? ? -73.30 -102.11 5 1 SER A 214 ? ? -107.43 -67.07 6 1 ALA A 245 C ? -31.94 165.07 # _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 601 _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 GLYCEROL GOL 7 water HOH #