data_3S9A # _entry.id 3S9A # _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 3S9A RCSB RCSB065922 WWPDB D_1000065922 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.details _pdbx_database_related.content_type PDB 3S9B . unspecified PDB 3S9C . unspecified PDB 3SBK . unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 3S9A _pdbx_database_status.recvd_initial_deposition_date 2011-06-01 _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site PDBJ _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.SG_entry ? _pdbx_database_status.status_code_cs ? _pdbx_database_status.pdb_format_compatible Y # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Nakayama, D.' 1 'Ben Ammar, Y.' 2 'Takeda, S.' 3 # loop_ _citation.id _citation.title _citation.journal_abbrev _citation.journal_volume _citation.page_first _citation.page_last _citation.year _citation.journal_id_ASTM _citation.country _citation.journal_id_ISSN _citation.journal_id_CSD _citation.book_publisher _citation.pdbx_database_id_PubMed _citation.pdbx_database_id_DOI primary 'Structural basis of coagulation factor V recognition for cleavage by RVV-V' 'Febs Lett.' 585 3020 3025 2011 FEBLAL NE 0014-5793 0165 ? 21871889 10.1016/j.febslet.2011.08.022 1 ;Crystallization and preliminary X-ray crystallographic analysis of blood coagulation factor V-activating proteinase (RVV-V) from Russell's viper venom ; 'Acta Crystallogr.,Sect.F' 65 1306 1308 2009 ? DK 1744-3091 ? ? 20054136 10.1107/S1744309109046697 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Nakayama, D.' 1 primary 'Ben Ammar, Y.' 2 primary 'Miyata, T.' 3 primary 'Takeda, S.' 4 1 'Nakayama, D.' 5 1 'Ben Ammar, Y.' 6 1 'Takeda, S.' 7 # _cell.entry_id 3S9A _cell.length_a 78.928 _cell.length_b 78.928 _cell.length_c 157.370 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 120.00 _cell.Z_PDB 12 _cell.pdbx_unique_axis ? _cell.length_a_esd ? _cell.length_b_esd ? _cell.length_c_esd ? _cell.angle_alpha_esd ? _cell.angle_beta_esd ? _cell.angle_gamma_esd ? # _symmetry.entry_id 3S9A _symmetry.space_group_name_H-M 'P 65 2 2' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 179 _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 'Vipera russelli proteinase RVV-V gamma' 25960.971 1 3.4.21.95 ? ? ? 2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 1 ? ? ? ? 3 water nat water 18.015 170 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name 'Factor V-activating proteinase gamma, Snake venom factor V activator gamma' # _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 ;VVGGDECNINEHPFLVALYTSASSTIHCAGALINREWVLTAAHCDRRNIRIKLGMHSKNIRNEDEQIRVPRGKYFCLNTK FPNGLDKDIMLIRLRRPVTYSTHIAPVSLPSRSRGVGSRCRIMGWGKISTTTYPDVPHCTNIFIVKHKWCEPLYPWVPAD SRTLCAGILKGGRDTCHGDSGGPLICNGEMHGIVAGGSEPCGQHLKPAVYTKVFDYNNWIQSIIAGNRTVTCPP ; _entity_poly.pdbx_seq_one_letter_code_can ;VVGGDECNINEHPFLVALYTSASSTIHCAGALINREWVLTAAHCDRRNIRIKLGMHSKNIRNEDEQIRVPRGKYFCLNTK FPNGLDKDIMLIRLRRPVTYSTHIAPVSLPSRSRGVGSRCRIMGWGKISTTTYPDVPHCTNIFIVKHKWCEPLYPWVPAD SRTLCAGILKGGRDTCHGDSGGPLICNGEMHGIVAGGSEPCGQHLKPAVYTKVFDYNNWIQSIIAGNRTVTCPP ; _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 VAL 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 PRO n 1 14 PHE n 1 15 LEU n 1 16 VAL n 1 17 ALA n 1 18 LEU n 1 19 TYR n 1 20 THR n 1 21 SER n 1 22 ALA n 1 23 SER n 1 24 SER n 1 25 THR n 1 26 ILE n 1 27 HIS n 1 28 CYS n 1 29 ALA n 1 30 GLY n 1 31 ALA n 1 32 LEU n 1 33 ILE n 1 34 ASN n 1 35 ARG n 1 36 GLU n 1 37 TRP n 1 38 VAL n 1 39 LEU n 1 40 THR n 1 41 ALA n 1 42 ALA n 1 43 HIS n 1 44 CYS n 1 45 ASP n 1 46 ARG n 1 47 ARG n 1 48 ASN n 1 49 ILE n 1 50 ARG n 1 51 ILE n 1 52 LYS n 1 53 LEU n 1 54 GLY n 1 55 MET n 1 56 HIS n 1 57 SER n 1 58 LYS n 1 59 ASN n 1 60 ILE n 1 61 ARG n 1 62 ASN n 1 63 GLU n 1 64 ASP n 1 65 GLU n 1 66 GLN n 1 67 ILE n 1 68 ARG n 1 69 VAL n 1 70 PRO n 1 71 ARG n 1 72 GLY n 1 73 LYS n 1 74 TYR n 1 75 PHE n 1 76 CYS n 1 77 LEU n 1 78 ASN n 1 79 THR n 1 80 LYS n 1 81 PHE n 1 82 PRO n 1 83 ASN n 1 84 GLY n 1 85 LEU n 1 86 ASP n 1 87 LYS n 1 88 ASP n 1 89 ILE n 1 90 MET n 1 91 LEU n 1 92 ILE n 1 93 ARG n 1 94 LEU n 1 95 ARG n 1 96 ARG n 1 97 PRO n 1 98 VAL n 1 99 THR n 1 100 TYR n 1 101 SER n 1 102 THR n 1 103 HIS n 1 104 ILE n 1 105 ALA n 1 106 PRO n 1 107 VAL n 1 108 SER n 1 109 LEU n 1 110 PRO n 1 111 SER n 1 112 ARG n 1 113 SER n 1 114 ARG n 1 115 GLY n 1 116 VAL n 1 117 GLY n 1 118 SER n 1 119 ARG n 1 120 CYS n 1 121 ARG n 1 122 ILE n 1 123 MET n 1 124 GLY n 1 125 TRP n 1 126 GLY n 1 127 LYS n 1 128 ILE n 1 129 SER n 1 130 THR n 1 131 THR n 1 132 THR n 1 133 TYR n 1 134 PRO n 1 135 ASP n 1 136 VAL n 1 137 PRO n 1 138 HIS n 1 139 CYS n 1 140 THR n 1 141 ASN n 1 142 ILE n 1 143 PHE n 1 144 ILE n 1 145 VAL n 1 146 LYS n 1 147 HIS n 1 148 LYS n 1 149 TRP n 1 150 CYS n 1 151 GLU n 1 152 PRO n 1 153 LEU n 1 154 TYR n 1 155 PRO n 1 156 TRP n 1 157 VAL n 1 158 PRO n 1 159 ALA n 1 160 ASP n 1 161 SER n 1 162 ARG n 1 163 THR n 1 164 LEU n 1 165 CYS n 1 166 ALA n 1 167 GLY n 1 168 ILE n 1 169 LEU n 1 170 LYS n 1 171 GLY n 1 172 GLY n 1 173 ARG n 1 174 ASP n 1 175 THR n 1 176 CYS n 1 177 HIS n 1 178 GLY n 1 179 ASP n 1 180 SER n 1 181 GLY n 1 182 GLY n 1 183 PRO n 1 184 LEU n 1 185 ILE n 1 186 CYS n 1 187 ASN n 1 188 GLY n 1 189 GLU n 1 190 MET n 1 191 HIS n 1 192 GLY n 1 193 ILE n 1 194 VAL n 1 195 ALA n 1 196 GLY n 1 197 GLY n 1 198 SER n 1 199 GLU n 1 200 PRO n 1 201 CYS n 1 202 GLY n 1 203 GLN n 1 204 HIS n 1 205 LEU n 1 206 LYS n 1 207 PRO n 1 208 ALA n 1 209 VAL n 1 210 TYR n 1 211 THR n 1 212 LYS n 1 213 VAL n 1 214 PHE n 1 215 ASP n 1 216 TYR n 1 217 ASN n 1 218 ASN n 1 219 TRP n 1 220 ILE n 1 221 GLN n 1 222 SER n 1 223 ILE n 1 224 ILE n 1 225 ALA n 1 226 GLY n 1 227 ASN n 1 228 ARG n 1 229 THR n 1 230 VAL n 1 231 THR n 1 232 CYS n 1 233 PRO n 1 234 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 ;Siamese Russell's viper ; _entity_src_nat.pdbx_organism_scientific 'Daboia russellii siamensis' _entity_src_nat.pdbx_ncbi_taxonomy_id 343250 _entity_src_nat.genus ? _entity_src_nat.species ? _entity_src_nat.strain ? _entity_src_nat.tissue venom _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 VSPG_DABRU _struct_ref.pdbx_db_accession P18965 _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ;VVGGDECNINEHPFLVALYTSASSTIHCAGALINREWVLTAAHCDRRNIRIKLGMHSKNIRNEDEQIRVPRGKYFCLNTK FPNGLDKDIMLIRLRRPVTYSTHIAPVSLPSRSRGVGSRCRIMGWGKISTTEDTYPDVPHCTNIFIVKHKWCEPLYPWVP ADSRTLCAGILKGGRDTCHGDSGGPLICNGEMHGIVAGGSEPCGQHLKPAVYTKVFDYNNWIQSIIAGNRTVTCPP ; _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 3S9A _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 234 _struct_ref_seq.pdbx_seq_align_end_ins_code G _struct_ref_seq.pdbx_db_accession P18965 _struct_ref_seq.db_align_beg 1 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 236 _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_ _struct_ref_seq_dif.align_id _struct_ref_seq_dif.pdbx_pdb_id_code _struct_ref_seq_dif.mon_id _struct_ref_seq_dif.pdbx_pdb_strand_id _struct_ref_seq_dif.seq_num _struct_ref_seq_dif.pdbx_pdb_ins_code _struct_ref_seq_dif.pdbx_seq_db_name _struct_ref_seq_dif.pdbx_seq_db_accession_code _struct_ref_seq_dif.db_mon_id _struct_ref_seq_dif.pdbx_seq_db_seq_num _struct_ref_seq_dif.details _struct_ref_seq_dif.pdbx_auth_seq_num _struct_ref_seq_dif.pdbx_ordinal 1 3S9A ? A ? ? UNP P18965 GLU 132 DELETION ? 1 1 3S9A ? A ? ? UNP P18965 ASP 133 DELETION ? 2 # loop_ _chem_comp.id _chem_comp.type _chem_comp.mon_nstd_flag _chem_comp.name _chem_comp.pdbx_synonyms _chem_comp.formula _chem_comp.formula_weight ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? '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 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 3S9A _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.73 _exptl_crystal.density_percent_sol 54.87 _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.preparation ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method 'VAPOR DIFFUSION, SITTING DROP' _exptl_crystal_grow.temp 293 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 5.0 _exptl_crystal_grow.pdbx_pH_range ? _exptl_crystal_grow.pdbx_details '16% PEG 3350, 50mM sodium citrate, 50mM bis-tris propane , pH 5.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K' # _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 'RAYONIX MX225HE' _diffrn_detector.pdbx_collection_date 2009-04-21 _diffrn_detector.details mirrors # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator 'Rotated-inclined double-crystal' _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 1.0 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'SPRING-8 BEAMLINE BL41XU' _diffrn_source.pdbx_synchrotron_site SPring-8 _diffrn_source.pdbx_synchrotron_beamline BL41XU _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_wavelength_list 1.0 # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 3S9A _reflns.observed_criterion_sigma_I 0 _reflns.observed_criterion_sigma_F 0 _reflns.d_resolution_low 50 _reflns.d_resolution_high 1.9 _reflns.number_obs 23547 _reflns.number_all 23594 _reflns.percent_possible_obs 99.8 _reflns.pdbx_Rmerge_I_obs 0.063 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 22.8 _reflns.B_iso_Wilson_estimate 18.3 _reflns.pdbx_redundancy 7.0 _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_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_ordinal 1 _reflns_shell.d_res_high 1.90 _reflns_shell.d_res_low 1.97 _reflns_shell.percent_possible_all 100 _reflns_shell.Rmerge_I_obs 0.255 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs 8.6 _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 ? # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 3S9A _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 23544 _refine.ls_number_reflns_all 23594 _refine.pdbx_ls_sigma_I 0 _refine.pdbx_ls_sigma_F 0.0 _refine.pdbx_data_cutoff_high_absF 2221293.05 _refine.pdbx_data_cutoff_low_absF 0.000000 _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 35.28 _refine.ls_d_res_high 1.90 _refine.ls_percent_reflns_obs 99.6 _refine.ls_R_factor_obs 0.220 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.2190 _refine.ls_R_factor_R_free 0.2555 _refine.ls_R_factor_R_free_error 0.008 _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 4.9 _refine.ls_number_reflns_R_free 1149 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc ? _refine.correlation_coeff_Fo_to_Fc_free ? _refine.B_iso_mean 29.6516 _refine.aniso_B[1][1] -1.2530 _refine.aniso_B[2][2] -1.2530 _refine.aniso_B[3][3] 2.5060 _refine.aniso_B[1][2] 0.0000 _refine.aniso_B[1][3] 0.0000 _refine.aniso_B[2][3] 0.0000 _refine.solvent_model_details 'FLAT MODEL' _refine.solvent_model_param_ksol 0.4 _refine.solvent_model_param_bsol 54.4674 _refine.pdbx_solvent_vdw_probe_radii ? _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii ? _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details 'BULK SOLVENT MODEL USED' _refine.pdbx_starting_model 'PDB ENTRY 2AIQ' _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model RESTRAINED _refine.pdbx_stereochemistry_target_values 'Engh & Huber' _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_overall_ESU_R_Free ? _refine.overall_SU_ML ? _refine.pdbx_overall_phase_error ? _refine.overall_SU_B ? _refine.overall_SU_R_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? _refine.ls_redundancy_reflns_obs ? _refine.B_iso_min ? _refine.B_iso_max ? _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_overall_ESU_R ? # _refine_analyze.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_analyze.entry_id 3S9A _refine_analyze.Luzzati_coordinate_error_obs 0.23 _refine_analyze.Luzzati_sigma_a_obs 0.14 _refine_analyze.Luzzati_d_res_low_obs 5.00 _refine_analyze.Luzzati_coordinate_error_free 0.28 _refine_analyze.Luzzati_sigma_a_free 0.17 _refine_analyze.Luzzati_d_res_low_free ? _refine_analyze.number_disordered_residues ? _refine_analyze.occupancy_sum_hydrogen ? _refine_analyze.occupancy_sum_non_hydrogen ? _refine_analyze.pdbx_Luzzati_d_res_high_obs ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 1817 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 14 _refine_hist.number_atoms_solvent 170 _refine_hist.number_atoms_total 2001 _refine_hist.d_res_high 1.90 _refine_hist.d_res_low 35.28 # loop_ _refine_ls_restr.type _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.number _refine_ls_restr.pdbx_refine_id _refine_ls_restr.pdbx_restraint_function c_bond_d 0.005 ? ? ? 'X-RAY DIFFRACTION' ? c_angle_deg 1.3 ? ? ? 'X-RAY DIFFRACTION' ? c_dihedral_angle_d 24.7 ? ? ? 'X-RAY DIFFRACTION' ? c_improper_angle_d 2.61 ? ? ? 'X-RAY DIFFRACTION' ? c_mcbond_it 1.276 1.500 ? ? 'X-RAY DIFFRACTION' ? c_scbond_it 1.893 2.000 ? ? 'X-RAY DIFFRACTION' ? c_mcangle_it 1.928 2.000 ? ? 'X-RAY DIFFRACTION' ? c_scangle_it 2.843 2.500 ? ? 'X-RAY DIFFRACTION' ? # _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_ls_shell.pdbx_total_number_of_bins_used 6 _refine_ls_shell.d_res_high 1.90 _refine_ls_shell.d_res_low 2.02 _refine_ls_shell.number_reflns_R_work 3618 _refine_ls_shell.R_factor_R_work 0.242 _refine_ls_shell.percent_reflns_obs 99.2 _refine_ls_shell.R_factor_R_free 0.269 _refine_ls_shell.R_factor_R_free_error 0.019 _refine_ls_shell.percent_reflns_R_free 5.1 _refine_ls_shell.number_reflns_R_free 196 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? _refine_ls_shell.redundancy_reflns_obs ? _refine_ls_shell.number_reflns_obs ? # _pdbx_refine.pdbx_refine_id 'X-RAY DIFFRACTION' _pdbx_refine.entry_id 3S9A _pdbx_refine.R_factor_all_no_cutoff ? _pdbx_refine.R_factor_obs_no_cutoff ? _pdbx_refine.free_R_factor_no_cutoff ? _pdbx_refine.free_R_error_no_cutoff ? _pdbx_refine.free_R_val_test_set_size_perc_no_cutoff ? _pdbx_refine.free_R_val_test_set_ct_no_cutoff ? _pdbx_refine.R_factor_all_4sig_cutoff ? _pdbx_refine.R_factor_obs_4sig_cutoff ? _pdbx_refine.free_R_factor_4sig_cutoff ? _pdbx_refine.free_R_val_test_set_size_perc_4sig_cutoff ? _pdbx_refine.free_R_val_test_set_ct_4sig_cutoff ? _pdbx_refine.number_reflns_obs_4sig_cutoff ? # loop_ _pdbx_xplor_file.pdbx_refine_id _pdbx_xplor_file.serial_no _pdbx_xplor_file.param_file _pdbx_xplor_file.topol_file 'X-RAY DIFFRACTION' 1 protein_rep.param protein.top 'X-RAY DIFFRACTION' 2 water_rep.param water.top 'X-RAY DIFFRACTION' 3 ion.param ion.top 'X-RAY DIFFRACTION' 4 carbohydrate.param carbohydrate.top # _struct_ncs_dom.id 1 _struct_ncs_dom.details ? _struct_ncs_dom.pdbx_ens_id 1 # _struct_ncs_ens.id 1 _struct_ncs_ens.details ? # _struct.entry_id 3S9A _struct.title ;Russell's viper venom serine proteinase, RVV-V (closed-form) ; _struct.pdbx_descriptor 'Vipera russelli proteinase RVV-V gamma (E.C.3.4.21.95)' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 3S9A _struct_keywords.pdbx_keywords HYDROLASE _struct_keywords.text 'serine proteinase, double six-stranded beta-barrels, Hydrolase, glycosylation' # 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 3 ? # _struct_biol.id 1 _struct_biol.details ? # 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 41 ? ASP A 45 ? ALA A 55 ASP A 59 5 ? 5 HELX_P HELX_P2 2 GLY A 84 ? ASP A 88 ? GLY A 98 ASP A 102 5 ? 5 HELX_P HELX_P3 3 LYS A 146 ? CYS A 150 ? LYS A 164 CYS A 168 5 ? 5 HELX_P HELX_P4 4 TYR A 216 ? ALA A 225 ? TYR A 234 ALA A 243 1 ? 10 # _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 139 SG ? ? A CYS 22 A CYS 157 1_555 ? ? ? ? ? ? ? 2.023 ? disulf2 disulf ? ? A CYS 28 SG ? ? ? 1_555 A CYS 44 SG ? ? A CYS 42 A CYS 58 1_555 ? ? ? ? ? ? ? 2.032 ? disulf3 disulf ? ? A CYS 76 SG ? ? ? 1_555 A CYS 232 SG ? E A CYS 91 A CYS 245 1_555 ? ? ? ? ? ? ? 2.026 ? disulf4 disulf ? ? A CYS 120 SG ? ? ? 1_555 A CYS 186 SG ? ? A CYS 136 A CYS 201 1_555 ? ? ? ? ? ? ? 2.034 ? disulf5 disulf ? ? A CYS 150 SG ? ? ? 1_555 A CYS 165 SG ? ? A CYS 168 A CYS 182 1_555 ? ? ? ? ? ? ? 2.035 ? disulf6 disulf ? ? A CYS 176 SG ? ? ? 1_555 A CYS 201 SG ? ? A CYS 191 A CYS 220 1_555 ? ? ? ? ? ? ? 2.036 ? covale1 covale ? ? A ASN 227 ND2 ? ? ? 1_555 B NAG . C1 ? ? A ASN 245 A NAG 301 1_555 ? ? ? ? ? ? ? 1.155 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? # _struct_mon_prot_cis.pdbx_id 1 _struct_mon_prot_cis.label_comp_id GLU _struct_mon_prot_cis.label_seq_id 199 _struct_mon_prot_cis.label_asym_id A _struct_mon_prot_cis.label_alt_id . _struct_mon_prot_cis.pdbx_PDB_ins_code ? _struct_mon_prot_cis.auth_comp_id GLU _struct_mon_prot_cis.auth_seq_id 218 _struct_mon_prot_cis.auth_asym_id A _struct_mon_prot_cis.pdbx_label_comp_id_2 PRO _struct_mon_prot_cis.pdbx_label_seq_id_2 200 _struct_mon_prot_cis.pdbx_label_asym_id_2 A _struct_mon_prot_cis.pdbx_PDB_ins_code_2 ? _struct_mon_prot_cis.pdbx_auth_comp_id_2 PRO _struct_mon_prot_cis.pdbx_auth_seq_id_2 219 _struct_mon_prot_cis.pdbx_auth_asym_id_2 A _struct_mon_prot_cis.pdbx_PDB_model_num 1 _struct_mon_prot_cis.pdbx_omega_angle -0.16 # 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 138 ? VAL A 145 ? HIS A 156 VAL A 163 A 3 THR A 163 ? GLY A 167 ? THR A 180 GLY A 184 A 4 ALA A 208 ? LYS A 212 ? ALA A 226 LYS A 230 A 5 GLU A 189 ? GLY A 196 ? GLU A 208 GLY A 215 A 6 PRO A 183 ? CYS A 186 ? PRO A 198 CYS A 201 A 7 ARG A 119 ? GLY A 124 ? ARG A 135 GLY A 140 A 8 HIS A 138 ? VAL A 145 ? HIS A 156 VAL A 163 B 1 GLN A 66 ? ARG A 68 ? GLN A 81 ARG A 83 B 2 ILE A 49 ? LEU A 53 ? ILE A 64 LEU A 68 B 3 LEU A 15 ? THR A 20 ? LEU A 30 THR A 35 B 4 CYS A 28 ? ASN A 34 ? CYS A 42 ASN A 48 B 5 TRP A 37 ? THR A 40 ? TRP A 51 THR A 54 B 6 MET A 90 ? LEU A 94 ? MET A 104 LEU A 108 B 7 PRO A 70 ? PHE A 75 ? 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 139 ? O CYS A 157 A 2 3 N VAL A 145 ? N VAL A 163 O CYS A 165 ? O CYS A 182 A 3 4 N LEU A 164 ? N LEU A 181 O TYR A 210 ? O TYR A 228 A 4 5 O VAL A 209 ? O VAL A 227 N GLY A 196 ? N GLY A 215 A 5 6 O GLU A 189 ? O GLU A 208 N CYS A 186 ? N CYS A 201 A 6 7 O ILE A 185 ? O ILE A 200 N ARG A 121 ? N ARG A 137 A 7 8 N CYS A 120 ? N CYS A 136 O ILE A 142 ? O ILE A 160 B 1 2 O GLN A 66 ? O GLN A 81 N LEU A 53 ? N LEU A 68 B 2 3 O ARG A 50 ? O ARG A 65 N TYR A 19 ? N TYR A 34 B 3 4 N LEU A 18 ? N LEU A 33 O CYS A 28 ? O CYS A 42 B 4 5 N ALA A 31 ? N ALA A 45 O LEU A 39 ? O LEU A 53 B 5 6 N VAL A 38 ? N VAL A 52 O ILE A 92 ? O ILE A 106 B 6 7 O ARG A 93 ? O ARG A 107 N GLY A 72 ? N GLY A 87 # _struct_site.id AC1 _struct_site.pdbx_evidence_code Software _struct_site.pdbx_auth_asym_id ? _struct_site.pdbx_auth_comp_id ? _struct_site.pdbx_auth_seq_id ? _struct_site.pdbx_auth_ins_code ? _struct_site.pdbx_num_residues 1 _struct_site.details 'BINDING SITE FOR RESIDUE NAG A 301' # _struct_site_gen.id 1 _struct_site_gen.site_id AC1 _struct_site_gen.pdbx_num_res 1 _struct_site_gen.label_comp_id ASN _struct_site_gen.label_asym_id A _struct_site_gen.label_seq_id 227 _struct_site_gen.pdbx_auth_ins_code ? _struct_site_gen.auth_comp_id ASN _struct_site_gen.auth_asym_id A _struct_site_gen.auth_seq_id 245 _struct_site_gen.label_atom_id . _struct_site_gen.label_alt_id ? _struct_site_gen.symmetry 1_555 _struct_site_gen.details ? # _database_PDB_matrix.entry_id 3S9A _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 3S9A _atom_sites.fract_transf_matrix[1][1] 0.012670 _atom_sites.fract_transf_matrix[1][2] 0.007315 _atom_sites.fract_transf_matrix[1][3] 0.000000 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.014630 _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] 0.006354 _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 ? 23.998 26.344 27.579 1.00 21.10 ? 16 VAL A N 1 ATOM 2 C CA . VAL A 1 1 ? 24.794 26.248 26.322 1.00 20.94 ? 16 VAL A CA 1 ATOM 3 C C . VAL A 1 1 ? 25.355 27.625 25.981 1.00 22.99 ? 16 VAL A C 1 ATOM 4 O O . VAL A 1 1 ? 24.619 28.609 25.957 1.00 23.15 ? 16 VAL A O 1 ATOM 5 C CB . VAL A 1 1 ? 23.913 25.750 25.134 1.00 21.89 ? 16 VAL A CB 1 ATOM 6 C CG1 . VAL A 1 1 ? 24.700 25.811 23.821 1.00 20.17 ? 16 VAL A CG1 1 ATOM 7 C CG2 . VAL A 1 1 ? 23.457 24.317 25.390 1.00 18.43 ? 16 VAL A CG2 1 ATOM 8 N N . VAL A 1 2 ? 26.659 27.701 25.739 1.00 25.15 ? 17 VAL A N 1 ATOM 9 C CA . VAL A 1 2 ? 27.270 28.979 25.384 1.00 25.22 ? 17 VAL A CA 1 ATOM 10 C C . VAL A 1 2 ? 27.645 28.977 23.909 1.00 25.56 ? 17 VAL A C 1 ATOM 11 O O . VAL A 1 2 ? 27.949 27.928 23.342 1.00 23.79 ? 17 VAL A O 1 ATOM 12 C CB . VAL A 1 2 ? 28.543 29.282 26.227 1.00 26.11 ? 17 VAL A CB 1 ATOM 13 C CG1 . VAL A 1 2 ? 28.164 29.497 27.682 1.00 29.67 ? 17 VAL A CG1 1 ATOM 14 C CG2 . VAL A 1 2 ? 29.553 28.158 26.092 1.00 25.34 ? 17 VAL A CG2 1 ATOM 15 N N . GLY A 1 3 ? 27.602 30.155 23.291 1.00 26.55 ? 18 GLY A N 1 ATOM 16 C CA . GLY A 1 3 ? 27.954 30.271 21.889 1.00 27.37 ? 18 GLY A CA 1 ATOM 17 C C . GLY A 1 3 ? 26.847 29.861 20.937 1.00 28.39 ? 18 GLY A C 1 ATOM 18 O O . GLY A 1 3 ? 27.085 29.671 19.748 1.00 29.43 ? 18 GLY A O 1 ATOM 19 N N . GLY A 1 4 ? 25.631 29.728 21.453 1.00 29.46 ? 19 GLY A N 1 ATOM 20 C CA . GLY A 1 4 ? 24.526 29.335 20.603 1.00 28.62 ? 19 GLY A CA 1 ATOM 21 C C . GLY A 1 4 ? 23.396 30.342 20.595 1.00 28.94 ? 19 GLY A C 1 ATOM 22 O O . GLY A 1 4 ? 23.578 31.518 20.913 1.00 27.91 ? 19 GLY A O 1 ATOM 23 N N . ASP A 1 5 ? 22.214 29.869 20.229 1.00 27.45 ? 20 ASP A N 1 ATOM 24 C CA . ASP A 1 5 ? 21.042 30.720 20.172 1.00 27.28 ? 20 ASP A CA 1 ATOM 25 C C . ASP A 1 5 ? 19.840 29.918 20.636 1.00 23.42 ? 20 ASP A C 1 ATOM 26 O O . ASP A 1 5 ? 19.941 28.713 20.857 1.00 21.10 ? 20 ASP A O 1 ATOM 27 C CB . ASP A 1 5 ? 20.815 31.189 18.737 1.00 31.68 ? 20 ASP A CB 1 ATOM 28 C CG . ASP A 1 5 ? 19.776 32.283 18.640 1.00 38.92 ? 20 ASP A CG 1 ATOM 29 O OD1 . ASP A 1 5 ? 19.336 32.573 17.507 1.00 43.95 ? 20 ASP A OD1 1 ATOM 30 O OD2 . ASP A 1 5 ? 19.406 32.859 19.691 1.00 41.53 ? 20 ASP A OD2 1 ATOM 31 N N . GLU A 1 6 ? 18.706 30.592 20.795 1.00 21.75 ? 21 GLU A N 1 ATOM 32 C CA . GLU A 1 6 ? 17.481 29.918 21.202 1.00 20.42 ? 21 GLU A CA 1 ATOM 33 C C . GLU A 1 6 ? 17.192 28.816 20.185 1.00 20.29 ? 21 GLU A C 1 ATOM 34 O O . GLU A 1 6 ? 17.250 29.044 18.974 1.00 17.29 ? 21 GLU A O 1 ATOM 35 C CB . GLU A 1 6 ? 16.312 30.910 21.231 1.00 22.15 ? 21 GLU A CB 1 ATOM 36 C CG . GLU A 1 6 ? 14.962 30.284 21.571 1.00 19.75 ? 21 GLU A CG 1 ATOM 37 C CD . GLU A 1 6 ? 13.822 31.295 21.577 1.00 22.57 ? 21 GLU A CD 1 ATOM 38 O OE1 . GLU A 1 6 ? 14.095 32.513 21.595 1.00 23.01 ? 21 GLU A OE1 1 ATOM 39 O OE2 . GLU A 1 6 ? 12.649 30.874 21.583 1.00 23.03 ? 21 GLU A OE2 1 ATOM 40 N N . CYS A 1 7 ? 16.890 27.621 20.679 1.00 16.97 ? 22 CYS A N 1 ATOM 41 C CA . CYS A 1 7 ? 16.585 26.490 19.808 1.00 18.53 ? 22 CYS A CA 1 ATOM 42 C C . CYS A 1 7 ? 15.270 26.714 19.075 1.00 18.16 ? 22 CYS A C 1 ATOM 43 O O . CYS A 1 7 ? 14.416 27.461 19.540 1.00 18.19 ? 22 CYS A O 1 ATOM 44 C CB . CYS A 1 7 ? 16.396 25.215 20.620 1.00 18.80 ? 22 CYS A CB 1 ATOM 45 S SG . CYS A 1 7 ? 17.768 24.729 21.704 1.00 19.43 ? 22 CYS A SG 1 ATOM 46 N N . ASN A 1 8 ? 15.111 26.037 17.942 1.00 19.03 ? 23 ASN A N 1 ATOM 47 C CA . ASN A 1 8 ? 13.863 26.101 17.191 1.00 19.14 ? 23 ASN A CA 1 ATOM 48 C C . ASN A 1 8 ? 12.858 25.421 18.127 1.00 22.43 ? 23 ASN A C 1 ATOM 49 O O . ASN A 1 8 ? 13.179 24.405 18.755 1.00 20.29 ? 23 ASN A O 1 ATOM 50 C CB . ASN A 1 8 ? 14.019 25.331 15.875 1.00 20.00 ? 23 ASN A CB 1 ATOM 51 C CG . ASN A 1 8 ? 12.693 25.026 15.209 1.00 23.56 ? 23 ASN A CG 1 ATOM 52 O OD1 . ASN A 1 8 ? 11.987 24.102 15.609 1.00 22.58 ? 23 ASN A OD1 1 ATOM 53 N ND2 . ASN A 1 8 ? 12.344 25.808 14.186 1.00 24.23 ? 23 ASN A ND2 1 ATOM 54 N N . ILE A 1 9 ? 11.657 25.977 18.239 1.00 19.48 ? 24 ILE A N 1 ATOM 55 C CA . ILE A 1 9 ? 10.660 25.428 19.154 1.00 21.85 ? 24 ILE A CA 1 ATOM 56 C C . ILE A 1 9 ? 10.203 23.996 18.871 1.00 19.41 ? 24 ILE A C 1 ATOM 57 O O . ILE A 1 9 ? 9.636 23.341 19.747 1.00 21.67 ? 24 ILE A O 1 ATOM 58 C CB . ILE A 1 9 ? 9.421 26.351 19.227 1.00 24.36 ? 24 ILE A CB 1 ATOM 59 C CG1 . ILE A 1 9 ? 8.510 25.904 20.374 1.00 27.50 ? 24 ILE A CG1 1 ATOM 60 C CG2 . ILE A 1 9 ? 8.690 26.353 17.883 1.00 24.57 ? 24 ILE A CG2 1 ATOM 61 C CD1 . ILE A 1 9 ? 7.447 26.912 20.747 1.00 30.55 ? 24 ILE A CD1 1 ATOM 62 N N . ASN A 1 10 ? 10.464 23.500 17.669 1.00 18.63 ? 25 ASN A N 1 ATOM 63 C CA . ASN A 1 10 ? 10.049 22.147 17.312 1.00 19.95 ? 25 ASN A CA 1 ATOM 64 C C . ASN A 1 10 ? 11.192 21.130 17.229 1.00 19.45 ? 25 ASN A C 1 ATOM 65 O O . ASN A 1 10 ? 10.949 19.943 17.012 1.00 21.36 ? 25 ASN A O 1 ATOM 66 C CB . ASN A 1 10 ? 9.310 22.171 15.966 1.00 19.84 ? 25 ASN A CB 1 ATOM 67 C CG . ASN A 1 10 ? 8.109 23.089 15.978 1.00 20.44 ? 25 ASN A CG 1 ATOM 68 O OD1 . ASN A 1 10 ? 7.231 22.963 16.828 1.00 21.54 ? 25 ASN A OD1 1 ATOM 69 N ND2 . ASN A 1 10 ? 8.061 24.024 15.031 1.00 20.52 ? 25 ASN A ND2 1 ATOM 70 N N . GLU A 1 11 ? 12.427 21.580 17.421 1.00 18.23 ? 26 GLU A N 1 ATOM 71 C CA . GLU A 1 11 ? 13.576 20.682 17.292 1.00 18.08 ? 26 GLU A CA 1 ATOM 72 C C . GLU A 1 11 ? 13.992 19.915 18.549 1.00 18.28 ? 26 GLU A C 1 ATOM 73 O O . GLU A 1 11 ? 14.961 19.164 18.511 1.00 19.87 ? 26 GLU A O 1 ATOM 74 C CB . GLU A 1 11 ? 14.799 21.450 16.762 1.00 17.74 ? 26 GLU A CB 1 ATOM 75 C CG . GLU A 1 11 ? 15.511 22.354 17.795 1.00 18.57 ? 26 GLU A CG 1 ATOM 76 C CD . GLU A 1 11 ? 16.869 22.849 17.300 1.00 18.88 ? 26 GLU A CD 1 ATOM 77 O OE1 . GLU A 1 11 ? 17.722 22.007 16.965 1.00 19.78 ? 26 GLU A OE1 1 ATOM 78 O OE2 . GLU A 1 11 ? 17.090 24.075 17.246 1.00 19.81 ? 26 GLU A OE2 1 ATOM 79 N N . HIS A 1 12 ? 13.262 20.077 19.645 1.00 18.18 ? 27 HIS A N 1 ATOM 80 C CA . HIS A 1 12 ? 13.637 19.393 20.885 1.00 18.41 ? 27 HIS A CA 1 ATOM 81 C C . HIS A 1 12 ? 12.454 18.770 21.644 1.00 17.88 ? 27 HIS A C 1 ATOM 82 O O . HIS A 1 12 ? 12.384 18.836 22.873 1.00 18.21 ? 27 HIS A O 1 ATOM 83 C CB . HIS A 1 12 ? 14.378 20.397 21.784 1.00 15.97 ? 27 HIS A CB 1 ATOM 84 C CG . HIS A 1 12 ? 13.550 21.583 22.185 1.00 16.21 ? 27 HIS A CG 1 ATOM 85 N ND1 . HIS A 1 12 ? 12.683 21.557 23.255 1.00 15.97 ? 27 HIS A ND1 1 ATOM 86 C CD2 . HIS A 1 12 ? 13.457 22.830 21.658 1.00 14.92 ? 27 HIS A CD2 1 ATOM 87 C CE1 . HIS A 1 12 ? 12.093 22.733 23.375 1.00 16.39 ? 27 HIS A CE1 1 ATOM 88 N NE2 . HIS A 1 12 ? 12.544 23.525 22.416 1.00 16.25 ? 27 HIS A NE2 1 ATOM 89 N N . PRO A 1 13 ? 11.534 18.114 20.924 1.00 18.37 ? 28 PRO A N 1 ATOM 90 C CA . PRO A 1 13 ? 10.370 17.505 21.581 1.00 18.79 ? 28 PRO A CA 1 ATOM 91 C C . PRO A 1 13 ? 10.693 16.419 22.609 1.00 18.78 ? 28 PRO A C 1 ATOM 92 O O . PRO A 1 13 ? 9.878 16.122 23.480 1.00 18.53 ? 28 PRO A O 1 ATOM 93 C CB . PRO A 1 13 ? 9.556 16.978 20.403 1.00 19.82 ? 28 PRO A CB 1 ATOM 94 C CG . PRO A 1 13 ? 10.619 16.557 19.442 1.00 19.40 ? 28 PRO A CG 1 ATOM 95 C CD . PRO A 1 13 ? 11.620 17.700 19.512 1.00 17.99 ? 28 PRO A CD 1 ATOM 96 N N . PHE A 1 14 ? 11.886 15.843 22.503 1.00 18.86 ? 29 PHE A N 1 ATOM 97 C CA . PHE A 1 14 ? 12.340 14.789 23.406 1.00 18.72 ? 29 PHE A CA 1 ATOM 98 C C . PHE A 1 14 ? 13.102 15.341 24.610 1.00 17.77 ? 29 PHE A C 1 ATOM 99 O O . PHE A 1 14 ? 13.435 14.606 25.530 1.00 17.78 ? 29 PHE A O 1 ATOM 100 C CB . PHE A 1 14 ? 13.245 13.837 22.635 1.00 19.39 ? 29 PHE A CB 1 ATOM 101 C CG . PHE A 1 14 ? 14.220 14.546 21.749 1.00 21.59 ? 29 PHE A CG 1 ATOM 102 C CD1 . PHE A 1 14 ? 15.300 15.236 22.295 1.00 23.67 ? 29 PHE A CD1 1 ATOM 103 C CD2 . PHE A 1 14 ? 14.022 14.588 20.371 1.00 24.08 ? 29 PHE A CD2 1 ATOM 104 C CE1 . PHE A 1 14 ? 16.171 15.966 21.481 1.00 24.19 ? 29 PHE A CE1 1 ATOM 105 C CE2 . PHE A 1 14 ? 14.884 15.315 19.546 1.00 25.08 ? 29 PHE A CE2 1 ATOM 106 C CZ . PHE A 1 14 ? 15.961 16.006 20.104 1.00 24.61 ? 29 PHE A CZ 1 ATOM 107 N N . LEU A 1 15 ? 13.370 16.640 24.601 1.00 17.69 ? 30 LEU A N 1 ATOM 108 C CA . LEU A 1 15 ? 14.116 17.269 25.683 1.00 17.26 ? 30 LEU A CA 1 ATOM 109 C C . LEU A 1 15 ? 13.269 17.549 26.920 1.00 19.42 ? 30 LEU A C 1 ATOM 110 O O . LEU A 1 15 ? 12.252 18.239 26.850 1.00 19.79 ? 30 LEU A O 1 ATOM 111 C CB . LEU A 1 15 ? 14.750 18.579 25.186 1.00 16.02 ? 30 LEU A CB 1 ATOM 112 C CG . LEU A 1 15 ? 15.626 19.354 26.174 1.00 16.65 ? 30 LEU A CG 1 ATOM 113 C CD1 . LEU A 1 15 ? 16.874 18.543 26.495 1.00 16.38 ? 30 LEU A CD1 1 ATOM 114 C CD2 . LEU A 1 15 ? 16.017 20.702 25.585 1.00 16.93 ? 30 LEU A CD2 1 ATOM 115 N N . VAL A 1 16 ? 13.701 17.014 28.059 1.00 18.60 ? 31 VAL A N 1 ATOM 116 C CA . VAL A 1 16 ? 12.985 17.237 29.308 1.00 17.85 ? 31 VAL A CA 1 ATOM 117 C C . VAL A 1 16 ? 13.898 17.982 30.264 1.00 18.29 ? 31 VAL A C 1 ATOM 118 O O . VAL A 1 16 ? 15.119 17.883 30.172 1.00 17.82 ? 31 VAL A O 1 ATOM 119 C CB . VAL A 1 16 ? 12.529 15.906 29.958 1.00 18.58 ? 31 VAL A CB 1 ATOM 120 C CG1 . VAL A 1 16 ? 11.717 15.108 28.953 1.00 17.54 ? 31 VAL A CG1 1 ATOM 121 C CG2 . VAL A 1 16 ? 13.729 15.097 30.444 1.00 17.31 ? 31 VAL A CG2 1 ATOM 122 N N . ALA A 1 17 ? 13.303 18.741 31.175 1.00 18.95 ? 32 ALA A N 1 ATOM 123 C CA . ALA A 1 17 ? 14.086 19.494 32.142 1.00 20.48 ? 32 ALA A CA 1 ATOM 124 C C . ALA A 1 17 ? 13.948 18.824 33.499 1.00 20.82 ? 32 ALA A C 1 ATOM 125 O O . ALA A 1 17 ? 12.859 18.380 33.863 1.00 21.35 ? 32 ALA A O 1 ATOM 126 C CB . ALA A 1 17 ? 13.584 20.921 32.213 1.00 20.92 ? 32 ALA A CB 1 ATOM 127 N N . LEU A 1 18 ? 15.047 18.744 34.241 1.00 19.43 ? 33 LEU A N 1 ATOM 128 C CA . LEU A 1 18 ? 15.002 18.129 35.556 1.00 20.56 ? 33 LEU A CA 1 ATOM 129 C C . LEU A 1 18 ? 15.192 19.143 36.671 1.00 21.36 ? 33 LEU A C 1 ATOM 130 O O . LEU A 1 18 ? 16.060 20.013 36.597 1.00 20.16 ? 33 LEU A O 1 ATOM 131 C CB . LEU A 1 18 ? 16.077 17.047 35.693 1.00 20.99 ? 33 LEU A CB 1 ATOM 132 C CG . LEU A 1 18 ? 16.029 15.861 34.728 1.00 22.70 ? 33 LEU A CG 1 ATOM 133 C CD1 . LEU A 1 18 ? 17.083 14.833 35.150 1.00 24.19 ? 33 LEU A CD1 1 ATOM 134 C CD2 . LEU A 1 18 ? 14.643 15.238 34.735 1.00 23.49 ? 33 LEU A CD2 1 ATOM 135 N N . TYR A 1 19 ? 14.358 19.021 37.698 1.00 22.48 ? 34 TYR A N 1 ATOM 136 C CA . TYR A 1 19 ? 14.427 19.879 38.872 1.00 24.66 ? 34 TYR A CA 1 ATOM 137 C C . TYR A 1 19 ? 13.996 19.016 40.062 1.00 25.19 ? 34 TYR A C 1 ATOM 138 O O . TYR A 1 19 ? 13.997 17.788 39.957 1.00 22.65 ? 34 TYR A O 1 ATOM 139 C CB . TYR A 1 19 ? 13.531 21.120 38.692 1.00 25.26 ? 34 TYR A CB 1 ATOM 140 C CG . TYR A 1 19 ? 12.058 20.859 38.461 1.00 26.42 ? 34 TYR A CG 1 ATOM 141 C CD1 . TYR A 1 19 ? 11.109 21.235 39.413 1.00 29.97 ? 34 TYR A CD1 1 ATOM 142 C CD2 . TYR A 1 19 ? 11.605 20.269 37.279 1.00 29.64 ? 34 TYR A CD2 1 ATOM 143 C CE1 . TYR A 1 19 ? 9.747 21.038 39.198 1.00 30.26 ? 34 TYR A CE1 1 ATOM 144 C CE2 . TYR A 1 19 ? 10.244 20.063 37.052 1.00 30.91 ? 34 TYR A CE2 1 ATOM 145 C CZ . TYR A 1 19 ? 9.320 20.453 38.016 1.00 31.76 ? 34 TYR A CZ 1 ATOM 146 O OH . TYR A 1 19 ? 7.974 20.269 37.796 1.00 31.62 ? 34 TYR A OH 1 ATOM 147 N N . THR A 1 20 ? 13.653 19.628 41.193 1.00 27.93 ? 35 THR A N 1 ATOM 148 C CA . THR A 1 20 ? 13.239 18.839 42.357 1.00 29.53 ? 35 THR A CA 1 ATOM 149 C C . THR A 1 20 ? 12.021 19.432 43.053 1.00 31.09 ? 35 THR A C 1 ATOM 150 O O . THR A 1 20 ? 11.622 20.557 42.771 1.00 31.32 ? 35 THR A O 1 ATOM 151 C CB . THR A 1 20 ? 14.377 18.707 43.400 1.00 29.62 ? 35 THR A CB 1 ATOM 152 O OG1 . THR A 1 20 ? 14.651 19.987 43.988 1.00 29.91 ? 35 THR A OG1 1 ATOM 153 C CG2 . THR A 1 20 ? 15.636 18.180 42.741 1.00 28.89 ? 35 THR A CG2 1 ATOM 154 N N . SER A 1 21 ? 11.431 18.666 43.965 1.00 34.00 ? 36 SER A N 1 ATOM 155 C CA . SER A 1 21 ? 10.253 19.133 44.687 1.00 36.03 ? 36 SER A CA 1 ATOM 156 C C . SER A 1 21 ? 10.612 20.286 45.617 1.00 37.86 ? 36 SER A C 1 ATOM 157 O O . SER A 1 21 ? 9.734 20.934 46.189 1.00 38.57 ? 36 SER A O 1 ATOM 158 C CB . SER A 1 21 ? 9.635 17.995 45.504 1.00 36.57 ? 36 SER A CB 1 ATOM 159 O OG . SER A 1 21 ? 10.494 17.593 46.556 1.00 36.72 ? 36 SER A OG 1 ATOM 160 N N . ALA A 1 22 A 11.907 20.542 45.759 1.00 39.23 ? 36 ALA A N 1 ATOM 161 C CA . ALA A 1 22 A 12.387 21.610 46.624 1.00 39.95 ? 36 ALA A CA 1 ATOM 162 C C . ALA A 1 22 A 12.819 22.849 45.848 1.00 40.51 ? 36 ALA A C 1 ATOM 163 O O . ALA A 1 22 A 12.656 23.971 46.325 1.00 41.28 ? 36 ALA A O 1 ATOM 164 C CB . ALA A 1 22 A 13.543 21.101 47.470 1.00 41.56 ? 36 ALA A CB 1 ATOM 165 N N . SER A 1 23 ? 13.367 22.648 44.654 1.00 39.42 ? 37 SER A N 1 ATOM 166 C CA . SER A 1 23 ? 13.833 23.767 43.840 1.00 38.70 ? 37 SER A CA 1 ATOM 167 C C . SER A 1 23 ? 13.331 23.723 42.400 1.00 39.07 ? 37 SER A C 1 ATOM 168 O O . SER A 1 23 ? 13.329 22.670 41.760 1.00 38.74 ? 37 SER A O 1 ATOM 169 C CB . SER A 1 23 ? 15.362 23.808 43.840 1.00 38.65 ? 37 SER A CB 1 ATOM 170 O OG . SER A 1 23 ? 15.846 24.850 43.012 1.00 39.87 ? 37 SER A OG 1 ATOM 171 N N . SER A 1 24 ? 12.913 24.882 41.901 1.00 38.26 ? 38 SER A N 1 ATOM 172 C CA . SER A 1 24 ? 12.412 25.015 40.538 1.00 38.40 ? 38 SER A CA 1 ATOM 173 C C . SER A 1 24 ? 13.582 25.176 39.572 1.00 37.31 ? 38 SER A C 1 ATOM 174 O O . SER A 1 24 ? 13.394 25.275 38.360 1.00 37.51 ? 38 SER A O 1 ATOM 175 C CB . SER A 1 24 ? 11.497 26.235 40.437 1.00 39.85 ? 38 SER A CB 1 ATOM 176 O OG . SER A 1 24 ? 12.189 27.413 40.823 1.00 40.85 ? 38 SER A OG 1 ATOM 177 N N . THR A 1 25 ? 14.793 25.209 40.120 1.00 36.05 ? 39 THR A N 1 ATOM 178 C CA . THR A 1 25 ? 15.996 25.355 39.311 1.00 33.93 ? 39 THR A CA 1 ATOM 179 C C . THR A 1 25 ? 16.223 24.115 38.455 1.00 30.51 ? 39 THR A C 1 ATOM 180 O O . THR A 1 25 ? 16.134 22.992 38.949 1.00 29.81 ? 39 THR A O 1 ATOM 181 C CB . THR A 1 25 ? 17.239 25.564 40.202 1.00 36.02 ? 39 THR A CB 1 ATOM 182 O OG1 . THR A 1 25 ? 17.063 26.741 40.997 1.00 38.11 ? 39 THR A OG1 1 ATOM 183 C CG2 . THR A 1 25 ? 18.496 25.713 39.346 1.00 36.70 ? 39 THR A CG2 1 ATOM 184 N N . ILE A 1 26 ? 16.508 24.320 37.173 1.00 28.42 ? 40 ILE A N 1 ATOM 185 C CA . ILE A 1 26 ? 16.769 23.206 36.261 1.00 26.43 ? 40 ILE A CA 1 ATOM 186 C C . ILE A 1 26 ? 18.240 22.844 36.412 1.00 25.05 ? 40 ILE A C 1 ATOM 187 O O . ILE A 1 26 ? 19.116 23.548 35.902 1.00 24.77 ? 40 ILE A O 1 ATOM 188 C CB . ILE A 1 26 ? 16.486 23.602 34.798 1.00 23.92 ? 40 ILE A CB 1 ATOM 189 C CG1 . ILE A 1 26 ? 15.009 23.969 34.646 1.00 24.63 ? 40 ILE A CG1 1 ATOM 190 C CG2 . ILE A 1 26 ? 16.848 22.451 33.864 1.00 24.78 ? 40 ILE A CG2 1 ATOM 191 C CD1 . ILE A 1 26 ? 14.656 24.596 33.314 1.00 23.12 ? 40 ILE A CD1 1 ATOM 192 N N . HIS A 1 27 ? 18.512 21.748 37.117 1.00 22.89 ? 41 HIS A N 1 ATOM 193 C CA . HIS A 1 27 ? 19.888 21.343 37.356 1.00 22.20 ? 41 HIS A CA 1 ATOM 194 C C . HIS A 1 27 ? 20.439 20.411 36.287 1.00 20.57 ? 41 HIS A C 1 ATOM 195 O O . HIS A 1 27 ? 21.646 20.170 36.232 1.00 22.01 ? 41 HIS A O 1 ATOM 196 C CB . HIS A 1 27 ? 20.020 20.690 38.744 1.00 22.60 ? 41 HIS A CB 1 ATOM 197 C CG . HIS A 1 27 ? 19.296 19.385 38.876 1.00 21.40 ? 41 HIS A CG 1 ATOM 198 N ND1 . HIS A 1 27 ? 17.966 19.300 39.232 1.00 22.22 ? 41 HIS A ND1 1 ATOM 199 C CD2 . HIS A 1 27 ? 19.713 18.112 38.671 1.00 21.61 ? 41 HIS A CD2 1 ATOM 200 C CE1 . HIS A 1 27 ? 17.595 18.032 39.239 1.00 21.13 ? 41 HIS A CE1 1 ATOM 201 N NE2 . HIS A 1 27 ? 18.636 17.291 38.901 1.00 20.94 ? 41 HIS A NE2 1 ATOM 202 N N . CYS A 1 28 ? 19.550 19.899 35.440 1.00 20.00 ? 42 CYS A N 1 ATOM 203 C CA . CYS A 1 28 ? 19.924 18.992 34.359 1.00 19.69 ? 42 CYS A CA 1 ATOM 204 C C . CYS A 1 28 ? 18.780 18.880 33.357 1.00 18.19 ? 42 CYS A C 1 ATOM 205 O O . CYS A 1 28 ? 17.698 19.423 33.557 1.00 19.92 ? 42 CYS A O 1 ATOM 206 C CB . CYS A 1 28 ? 20.183 17.581 34.886 1.00 19.06 ? 42 CYS A CB 1 ATOM 207 S SG . CYS A 1 28 ? 21.771 17.200 35.689 1.00 21.04 ? 42 CYS A SG 1 ATOM 208 N N . ALA A 1 29 ? 19.039 18.145 32.285 1.00 18.98 ? 43 ALA A N 1 ATOM 209 C CA . ALA A 1 29 ? 18.037 17.889 31.263 1.00 18.49 ? 43 ALA A CA 1 ATOM 210 C C . ALA A 1 29 ? 18.053 16.379 31.073 1.00 17.39 ? 43 ALA A C 1 ATOM 211 O O . ALA A 1 29 ? 18.764 15.670 31.787 1.00 17.88 ? 43 ALA A O 1 ATOM 212 C CB . ALA A 1 29 ? 18.405 18.587 29.960 1.00 17.43 ? 43 ALA A CB 1 ATOM 213 N N . GLY A 1 30 ? 17.269 15.898 30.114 1.00 16.13 ? 44 GLY A N 1 ATOM 214 C CA . GLY A 1 30 ? 17.201 14.479 29.826 1.00 16.47 ? 44 GLY A CA 1 ATOM 215 C C . GLY A 1 30 ? 16.523 14.280 28.488 1.00 17.63 ? 44 GLY A C 1 ATOM 216 O O . GLY A 1 30 ? 16.072 15.249 27.876 1.00 16.79 ? 44 GLY A O 1 ATOM 217 N N . ALA A 1 31 ? 16.437 13.034 28.033 1.00 16.31 ? 45 ALA A N 1 ATOM 218 C CA . ALA A 1 31 ? 15.819 12.743 26.742 1.00 19.29 ? 45 ALA A CA 1 ATOM 219 C C . ALA A 1 31 ? 14.746 11.670 26.829 1.00 19.39 ? 45 ALA A C 1 ATOM 220 O O . ALA A 1 31 ? 14.965 10.602 27.398 1.00 17.91 ? 45 ALA A O 1 ATOM 221 C CB . ALA A 1 31 ? 16.895 12.320 25.738 1.00 18.29 ? 45 ALA A CB 1 ATOM 222 N N . LEU A 1 32 ? 13.582 11.963 26.257 1.00 19.98 ? 46 LEU A N 1 ATOM 223 C CA . LEU A 1 32 ? 12.465 11.020 26.250 1.00 20.03 ? 46 LEU A CA 1 ATOM 224 C C . LEU A 1 32 ? 12.765 9.890 25.269 1.00 20.56 ? 46 LEU A C 1 ATOM 225 O O . LEU A 1 32 ? 13.013 10.135 24.088 1.00 22.13 ? 46 LEU A O 1 ATOM 226 C CB . LEU A 1 32 ? 11.174 11.736 25.832 1.00 21.37 ? 46 LEU A CB 1 ATOM 227 C CG . LEU A 1 32 ? 9.874 10.946 26.002 1.00 21.52 ? 46 LEU A CG 1 ATOM 228 C CD1 . LEU A 1 32 ? 9.684 10.590 27.471 1.00 21.21 ? 46 LEU A CD1 1 ATOM 229 C CD2 . LEU A 1 32 ? 8.697 11.775 25.500 1.00 23.45 ? 46 LEU A CD2 1 ATOM 230 N N . ILE A 1 33 ? 12.740 8.656 25.766 1.00 20.00 ? 47 ILE A N 1 ATOM 231 C CA . ILE A 1 33 ? 13.016 7.474 24.950 1.00 23.80 ? 47 ILE A CA 1 ATOM 232 C C . ILE A 1 33 ? 11.711 6.910 24.380 1.00 24.23 ? 47 ILE A C 1 ATOM 233 O O . ILE A 1 33 ? 11.661 6.471 23.230 1.00 24.89 ? 47 ILE A O 1 ATOM 234 C CB . ILE A 1 33 ? 13.736 6.395 25.794 1.00 25.13 ? 47 ILE A CB 1 ATOM 235 C CG1 . ILE A 1 33 ? 15.039 6.970 26.361 1.00 27.32 ? 47 ILE A CG1 1 ATOM 236 C CG2 . ILE A 1 33 ? 14.029 5.163 24.952 1.00 28.49 ? 47 ILE A CG2 1 ATOM 237 C CD1 . ILE A 1 33 ? 15.983 7.529 25.297 1.00 27.80 ? 47 ILE A CD1 1 ATOM 238 N N . ASN A 1 34 ? 10.669 6.899 25.207 1.00 25.38 ? 48 ASN A N 1 ATOM 239 C CA . ASN A 1 34 ? 9.348 6.444 24.791 1.00 25.80 ? 48 ASN A CA 1 ATOM 240 C C . ASN A 1 34 ? 8.332 7.073 25.731 1.00 25.76 ? 48 ASN A C 1 ATOM 241 O O . ASN A 1 34 ? 8.673 7.977 26.492 1.00 24.41 ? 48 ASN A O 1 ATOM 242 C CB . ASN A 1 34 ? 9.232 4.906 24.779 1.00 28.76 ? 48 ASN A CB 1 ATOM 243 C CG . ASN A 1 34 ? 9.267 4.285 26.164 1.00 27.64 ? 48 ASN A CG 1 ATOM 244 O OD1 . ASN A 1 34 ? 9.062 4.951 27.173 1.00 28.20 ? 48 ASN A OD1 1 ATOM 245 N ND2 . ASN A 1 34 ? 9.511 2.979 26.208 1.00 32.91 ? 48 ASN A ND2 1 ATOM 246 N N . ARG A 1 35 ? 7.090 6.608 25.696 1.00 25.55 ? 49 ARG A N 1 ATOM 247 C CA . ARG A 1 35 ? 6.063 7.207 26.540 1.00 26.86 ? 49 ARG A CA 1 ATOM 248 C C . ARG A 1 35 ? 6.279 7.114 28.051 1.00 27.09 ? 49 ARG A C 1 ATOM 249 O O . ARG A 1 35 ? 5.673 7.877 28.807 1.00 26.87 ? 49 ARG A O 1 ATOM 250 C CB . ARG A 1 35 ? 4.690 6.627 26.178 1.00 28.95 ? 49 ARG A CB 1 ATOM 251 C CG . ARG A 1 35 ? 4.275 6.898 24.735 1.00 31.65 ? 49 ARG A CG 1 ATOM 252 C CD . ARG A 1 35 ? 2.853 6.432 24.456 1.00 34.67 ? 49 ARG A CD 1 ATOM 253 N NE . ARG A 1 35 ? 2.461 6.684 23.071 1.00 38.51 ? 49 ARG A NE 1 ATOM 254 C CZ . ARG A 1 35 ? 2.965 6.044 22.019 1.00 39.56 ? 49 ARG A CZ 1 ATOM 255 N NH1 . ARG A 1 35 ? 2.549 6.345 20.794 1.00 39.43 ? 49 ARG A NH1 1 ATOM 256 N NH2 . ARG A 1 35 ? 3.877 5.095 22.189 1.00 41.74 ? 49 ARG A NH2 1 ATOM 257 N N . GLU A 1 36 ? 7.153 6.214 28.498 1.00 26.81 ? 50 GLU A N 1 ATOM 258 C CA . GLU A 1 36 ? 7.381 6.047 29.933 1.00 28.13 ? 50 GLU A CA 1 ATOM 259 C C . GLU A 1 36 ? 8.825 6.131 30.406 1.00 26.60 ? 50 GLU A C 1 ATOM 260 O O . GLU A 1 36 ? 9.081 5.942 31.595 1.00 27.20 ? 50 GLU A O 1 ATOM 261 C CB . GLU A 1 36 ? 6.865 4.683 30.403 1.00 31.46 ? 50 GLU A CB 1 ATOM 262 C CG . GLU A 1 36 ? 5.401 4.395 30.200 1.00 36.83 ? 50 GLU A CG 1 ATOM 263 C CD . GLU A 1 36 ? 5.035 3.042 30.776 1.00 38.19 ? 50 GLU A CD 1 ATOM 264 O OE1 . GLU A 1 36 ? 5.232 2.851 31.995 1.00 38.42 ? 50 GLU A OE1 1 ATOM 265 O OE2 . GLU A 1 36 ? 4.567 2.172 30.013 1.00 41.48 ? 50 GLU A OE2 1 ATOM 266 N N . TRP A 1 37 ? 9.763 6.400 29.505 1.00 26.03 ? 51 TRP A N 1 ATOM 267 C CA . TRP A 1 37 ? 11.170 6.430 29.896 1.00 23.87 ? 51 TRP A CA 1 ATOM 268 C C . TRP A 1 37 ? 11.963 7.653 29.465 1.00 21.90 ? 51 TRP A C 1 ATOM 269 O O . TRP A 1 37 ? 11.767 8.173 28.372 1.00 21.92 ? 51 TRP A O 1 ATOM 270 C CB . TRP A 1 37 ? 11.879 5.184 29.358 1.00 24.11 ? 51 TRP A CB 1 ATOM 271 C CG . TRP A 1 37 ? 11.370 3.893 29.930 1.00 25.78 ? 51 TRP A CG 1 ATOM 272 C CD1 . TRP A 1 37 ? 10.311 3.156 29.484 1.00 25.37 ? 51 TRP A CD1 1 ATOM 273 C CD2 . TRP A 1 37 ? 11.908 3.189 31.055 1.00 25.18 ? 51 TRP A CD2 1 ATOM 274 N NE1 . TRP A 1 37 ? 10.158 2.031 30.262 1.00 25.51 ? 51 TRP A NE1 1 ATOM 275 C CE2 . TRP A 1 37 ? 11.125 2.026 31.233 1.00 25.21 ? 51 TRP A CE2 1 ATOM 276 C CE3 . TRP A 1 37 ? 12.978 3.428 31.930 1.00 24.77 ? 51 TRP A CE3 1 ATOM 277 C CZ2 . TRP A 1 37 ? 11.378 1.100 32.252 1.00 25.19 ? 51 TRP A CZ2 1 ATOM 278 C CZ3 . TRP A 1 37 ? 13.230 2.506 32.944 1.00 25.80 ? 51 TRP A CZ3 1 ATOM 279 C CH2 . TRP A 1 37 ? 12.432 1.356 33.095 1.00 25.36 ? 51 TRP A CH2 1 ATOM 280 N N . VAL A 1 38 ? 12.871 8.082 30.339 1.00 20.81 ? 52 VAL A N 1 ATOM 281 C CA . VAL A 1 38 ? 13.745 9.229 30.096 1.00 17.97 ? 52 VAL A CA 1 ATOM 282 C C . VAL A 1 38 ? 15.188 8.817 30.362 1.00 19.94 ? 52 VAL A C 1 ATOM 283 O O . VAL A 1 38 ? 15.477 8.161 31.365 1.00 17.95 ? 52 VAL A O 1 ATOM 284 C CB . VAL A 1 38 ? 13.397 10.416 31.038 1.00 18.88 ? 52 VAL A CB 1 ATOM 285 C CG1 . VAL A 1 38 ? 14.544 11.445 31.054 1.00 16.79 ? 52 VAL A CG1 1 ATOM 286 C CG2 . VAL A 1 38 ? 12.100 11.080 30.576 1.00 16.80 ? 52 VAL A CG2 1 ATOM 287 N N . LEU A 1 39 ? 16.089 9.193 29.460 1.00 17.96 ? 53 LEU A N 1 ATOM 288 C CA . LEU A 1 39 ? 17.499 8.882 29.630 1.00 17.35 ? 53 LEU A CA 1 ATOM 289 C C . LEU A 1 39 ? 18.199 10.181 30.023 1.00 18.08 ? 53 LEU A C 1 ATOM 290 O O . LEU A 1 39 ? 17.956 11.236 29.427 1.00 17.80 ? 53 LEU A O 1 ATOM 291 C CB . LEU A 1 39 ? 18.088 8.337 28.324 1.00 18.59 ? 53 LEU A CB 1 ATOM 292 C CG . LEU A 1 39 ? 19.533 7.837 28.361 1.00 19.74 ? 53 LEU A CG 1 ATOM 293 C CD1 . LEU A 1 39 ? 19.623 6.585 29.234 1.00 21.01 ? 53 LEU A CD1 1 ATOM 294 C CD2 . LEU A 1 39 ? 19.994 7.522 26.941 1.00 22.00 ? 53 LEU A CD2 1 ATOM 295 N N . THR A 1 40 ? 19.055 10.111 31.035 1.00 16.20 ? 54 THR A N 1 ATOM 296 C CA . THR A 1 40 ? 19.773 11.293 31.499 1.00 16.78 ? 54 THR A CA 1 ATOM 297 C C . THR A 1 40 ? 21.110 10.856 32.097 1.00 15.50 ? 54 THR A C 1 ATOM 298 O O . THR A 1 40 ? 21.510 9.702 31.931 1.00 15.38 ? 54 THR A O 1 ATOM 299 C CB . THR A 1 40 ? 18.926 12.071 32.545 1.00 17.46 ? 54 THR A CB 1 ATOM 300 O OG1 . THR A 1 40 ? 19.635 13.243 32.971 1.00 18.97 ? 54 THR A OG1 1 ATOM 301 C CG2 . THR A 1 40 ? 18.610 11.187 33.760 1.00 16.33 ? 54 THR A CG2 1 ATOM 302 N N . ALA A 1 41 ? 21.808 11.770 32.761 1.00 16.29 ? 55 ALA A N 1 ATOM 303 C CA . ALA A 1 41 ? 23.093 11.427 33.373 1.00 19.02 ? 55 ALA A CA 1 ATOM 304 C C . ALA A 1 41 ? 22.863 10.970 34.809 1.00 18.54 ? 55 ALA A C 1 ATOM 305 O O . ALA A 1 41 ? 21.992 11.492 35.497 1.00 17.79 ? 55 ALA A O 1 ATOM 306 C CB . ALA A 1 41 ? 24.031 12.633 33.355 1.00 17.99 ? 55 ALA A CB 1 ATOM 307 N N . ALA A 1 42 ? 23.649 9.998 35.254 1.00 19.58 ? 56 ALA A N 1 ATOM 308 C CA . ALA A 1 42 ? 23.524 9.487 36.617 1.00 20.20 ? 56 ALA A CA 1 ATOM 309 C C . ALA A 1 42 ? 23.739 10.576 37.677 1.00 20.54 ? 56 ALA A C 1 ATOM 310 O O . ALA A 1 42 ? 23.044 10.594 38.699 1.00 20.44 ? 56 ALA A O 1 ATOM 311 C CB . ALA A 1 42 ? 24.517 8.340 36.835 1.00 19.32 ? 56 ALA A CB 1 ATOM 312 N N . HIS A 1 43 ? 24.678 11.495 37.442 1.00 21.41 ? 57 HIS A N 1 ATOM 313 C CA . HIS A 1 43 ? 24.936 12.534 38.437 1.00 21.39 ? 57 HIS A CA 1 ATOM 314 C C . HIS A 1 43 ? 23.809 13.554 38.538 1.00 20.48 ? 57 HIS A C 1 ATOM 315 O O . HIS A 1 43 ? 23.828 14.434 39.395 1.00 18.84 ? 57 HIS A O 1 ATOM 316 C CB . HIS A 1 43 ? 26.287 13.237 38.191 1.00 22.32 ? 57 HIS A CB 1 ATOM 317 C CG . HIS A 1 43 ? 26.258 14.297 37.131 1.00 21.20 ? 57 HIS A CG 1 ATOM 318 N ND1 . HIS A 1 43 ? 26.733 14.085 35.856 1.00 22.88 ? 57 HIS A ND1 1 ATOM 319 C CD2 . HIS A 1 43 ? 25.852 15.589 37.170 1.00 24.03 ? 57 HIS A CD2 1 ATOM 320 C CE1 . HIS A 1 43 ? 26.624 15.199 35.154 1.00 22.81 ? 57 HIS A CE1 1 ATOM 321 N NE2 . HIS A 1 43 ? 26.092 16.127 35.928 1.00 25.09 ? 57 HIS A NE2 1 ATOM 322 N N . CYS A 1 44 ? 22.819 13.420 37.665 1.00 19.32 ? 58 CYS A N 1 ATOM 323 C CA . CYS A 1 44 ? 21.671 14.309 37.673 1.00 19.94 ? 58 CYS A CA 1 ATOM 324 C C . CYS A 1 44 ? 20.629 13.844 38.679 1.00 21.20 ? 58 CYS A C 1 ATOM 325 O O . CYS A 1 44 ? 19.645 14.536 38.941 1.00 19.16 ? 58 CYS A O 1 ATOM 326 C CB . CYS A 1 44 ? 21.051 14.347 36.290 1.00 21.58 ? 58 CYS A CB 1 ATOM 327 S SG . CYS A 1 44 ? 22.067 15.276 35.107 1.00 21.60 ? 58 CYS A SG 1 ATOM 328 N N . ASP A 1 45 ? 20.849 12.666 39.244 1.00 22.50 ? 59 ASP A N 1 ATOM 329 C CA . ASP A 1 45 ? 19.911 12.121 40.215 1.00 24.56 ? 59 ASP A CA 1 ATOM 330 C C . ASP A 1 45 ? 19.815 12.991 41.469 1.00 23.67 ? 59 ASP A C 1 ATOM 331 O O . ASP A 1 45 ? 20.802 13.576 41.909 1.00 24.35 ? 59 ASP A O 1 ATOM 332 C CB . ASP A 1 45 ? 20.321 10.695 40.589 1.00 24.80 ? 59 ASP A CB 1 ATOM 333 C CG . ASP A 1 45 ? 19.339 10.041 41.535 1.00 25.64 ? 59 ASP A CG 1 ATOM 334 O OD1 . ASP A 1 45 ? 18.120 10.166 41.303 1.00 26.06 ? 59 ASP A OD1 1 ATOM 335 O OD2 . ASP A 1 45 ? 19.786 9.399 42.504 1.00 28.71 ? 59 ASP A OD2 1 ATOM 336 N N . ARG A 1 46 ? 18.607 13.088 42.016 1.00 24.47 ? 60 ARG A N 1 ATOM 337 C CA . ARG A 1 46 ? 18.341 13.868 43.226 1.00 26.58 ? 60 ARG A CA 1 ATOM 338 C C . ARG A 1 46 ? 17.305 13.094 44.040 1.00 27.33 ? 60 ARG A C 1 ATOM 339 O O . ARG A 1 46 ? 16.642 12.204 43.512 1.00 27.30 ? 60 ARG A O 1 ATOM 340 C CB . ARG A 1 46 ? 17.795 15.257 42.871 1.00 24.72 ? 60 ARG A CB 1 ATOM 341 C CG . ARG A 1 46 ? 18.777 16.172 42.135 1.00 24.46 ? 60 ARG A CG 1 ATOM 342 C CD . ARG A 1 46 ? 19.922 16.620 43.047 1.00 26.09 ? 60 ARG A CD 1 ATOM 343 N NE . ARG A 1 46 ? 20.765 17.649 42.436 1.00 27.24 ? 60 ARG A NE 1 ATOM 344 C CZ . ARG A 1 46 ? 21.677 17.424 41.491 1.00 26.21 ? 60 ARG A CZ 1 ATOM 345 N NH1 . ARG A 1 46 ? 21.885 16.197 41.031 1.00 26.48 ? 60 ARG A NH1 1 ATOM 346 N NH2 . ARG A 1 46 ? 22.386 18.434 41.003 1.00 27.45 ? 60 ARG A NH2 1 ATOM 347 N N . ARG A 1 47 ? 17.148 13.436 45.316 1.00 29.22 ? 62 ARG A N 1 ATOM 348 C CA . ARG A 1 47 ? 16.194 12.718 46.157 1.00 30.69 ? 62 ARG A CA 1 ATOM 349 C C . ARG A 1 47 ? 14.760 12.736 45.633 1.00 30.17 ? 62 ARG A C 1 ATOM 350 O O . ARG A 1 47 ? 14.115 11.690 45.559 1.00 32.63 ? 62 ARG A O 1 ATOM 351 C CB . ARG A 1 47 ? 16.222 13.260 47.588 1.00 32.51 ? 62 ARG A CB 1 ATOM 352 C CG . ARG A 1 47 ? 15.440 12.392 48.570 1.00 36.42 ? 62 ARG A CG 1 ATOM 353 C CD . ARG A 1 47 ? 15.794 12.734 50.007 1.00 39.44 ? 62 ARG A CD 1 ATOM 354 N NE . ARG A 1 47 ? 15.197 11.799 50.958 1.00 42.43 ? 62 ARG A NE 1 ATOM 355 C CZ . ARG A 1 47 ? 15.335 11.892 52.276 1.00 42.34 ? 62 ARG A CZ 1 ATOM 356 N NH1 . ARG A 1 47 ? 14.760 11.002 53.073 1.00 42.91 ? 62 ARG A NH1 1 ATOM 357 N NH2 . ARG A 1 47 ? 16.053 12.877 52.798 1.00 43.67 ? 62 ARG A NH2 1 ATOM 358 N N . ASN A 1 48 ? 14.257 13.914 45.278 1.00 28.34 ? 63 ASN A N 1 ATOM 359 C CA . ASN A 1 48 ? 12.893 14.014 44.768 1.00 28.99 ? 63 ASN A CA 1 ATOM 360 C C . ASN A 1 48 ? 12.840 14.684 43.402 1.00 27.44 ? 63 ASN A C 1 ATOM 361 O O . ASN A 1 48 ? 12.414 15.828 43.274 1.00 25.31 ? 63 ASN A O 1 ATOM 362 C CB . ASN A 1 48 ? 12.005 14.784 45.750 1.00 30.41 ? 63 ASN A CB 1 ATOM 363 C CG . ASN A 1 48 ? 11.871 14.079 47.086 1.00 32.68 ? 63 ASN A CG 1 ATOM 364 O OD1 . ASN A 1 48 ? 12.411 14.530 48.096 1.00 35.92 ? 63 ASN A OD1 1 ATOM 365 N ND2 . ASN A 1 48 ? 11.157 12.958 47.095 1.00 32.61 ? 63 ASN A ND2 1 ATOM 366 N N . ILE A 1 49 ? 13.262 13.944 42.385 1.00 28.28 ? 64 ILE A N 1 ATOM 367 C CA . ILE A 1 49 ? 13.277 14.441 41.014 1.00 28.04 ? 64 ILE A CA 1 ATOM 368 C C . ILE A 1 49 ? 11.899 14.773 40.464 1.00 27.38 ? 64 ILE A C 1 ATOM 369 O O . ILE A 1 49 ? 10.916 14.072 40.719 1.00 26.63 ? 64 ILE A O 1 ATOM 370 C CB . ILE A 1 49 ? 13.926 13.409 40.059 1.00 29.58 ? 64 ILE A CB 1 ATOM 371 C CG1 . ILE A 1 49 ? 15.425 13.305 40.340 1.00 30.05 ? 64 ILE A CG1 1 ATOM 372 C CG2 . ILE A 1 49 ? 13.672 13.803 38.596 1.00 31.12 ? 64 ILE A CG2 1 ATOM 373 C CD1 . ILE A 1 49 ? 16.232 14.511 39.879 1.00 32.72 ? 64 ILE A CD1 1 ATOM 374 N N . ARG A 1 50 ? 11.846 15.865 39.712 1.00 26.94 ? 65 ARG A N 1 ATOM 375 C CA . ARG A 1 50 ? 10.628 16.301 39.049 1.00 26.48 ? 65 ARG A CA 1 ATOM 376 C C . ARG A 1 50 ? 11.038 16.501 37.594 1.00 25.11 ? 65 ARG A C 1 ATOM 377 O O . ARG A 1 50 ? 12.129 17.008 37.314 1.00 23.26 ? 65 ARG A O 1 ATOM 378 C CB . ARG A 1 50 ? 10.097 17.590 39.677 1.00 29.25 ? 65 ARG A CB 1 ATOM 379 C CG . ARG A 1 50 ? 9.512 17.353 41.068 1.00 33.20 ? 65 ARG A CG 1 ATOM 380 C CD . ARG A 1 50 ? 8.750 18.552 41.603 1.00 39.12 ? 65 ARG A CD 1 ATOM 381 N NE . ARG A 1 50 ? 7.897 18.175 42.731 1.00 42.39 ? 65 ARG A NE 1 ATOM 382 C CZ . ARG A 1 50 ? 7.111 19.018 43.396 1.00 43.66 ? 65 ARG A CZ 1 ATOM 383 N NH1 . ARG A 1 50 ? 7.065 20.299 43.055 1.00 43.04 ? 65 ARG A NH1 1 ATOM 384 N NH2 . ARG A 1 50 ? 6.360 18.574 44.397 1.00 44.21 ? 65 ARG A NH2 1 ATOM 385 N N . ILE A 1 51 ? 10.178 16.075 36.675 1.00 23.35 ? 66 ILE A N 1 ATOM 386 C CA . ILE A 1 51 ? 10.481 16.162 35.252 1.00 22.05 ? 66 ILE A CA 1 ATOM 387 C C . ILE A 1 51 ? 9.425 16.930 34.471 1.00 21.65 ? 66 ILE A C 1 ATOM 388 O O . ILE A 1 51 ? 8.241 16.588 34.511 1.00 23.82 ? 66 ILE A O 1 ATOM 389 C CB . ILE A 1 51 ? 10.591 14.756 34.635 1.00 21.99 ? 66 ILE A CB 1 ATOM 390 C CG1 . ILE A 1 51 ? 11.552 13.899 35.464 1.00 23.20 ? 66 ILE A CG1 1 ATOM 391 C CG2 . ILE A 1 51 ? 11.060 14.860 33.182 1.00 21.83 ? 66 ILE A CG2 1 ATOM 392 C CD1 . ILE A 1 51 ? 11.729 12.494 34.928 1.00 28.30 ? 66 ILE A CD1 1 ATOM 393 N N . LYS A 1 52 ? 9.874 17.954 33.751 1.00 22.67 ? 67 LYS A N 1 ATOM 394 C CA . LYS A 1 52 ? 8.997 18.787 32.932 1.00 22.65 ? 67 LYS A CA 1 ATOM 395 C C . LYS A 1 52 ? 9.190 18.417 31.466 1.00 21.70 ? 67 LYS A C 1 ATOM 396 O O . LYS A 1 52 ? 10.301 18.516 30.933 1.00 21.77 ? 67 LYS A O 1 ATOM 397 C CB . LYS A 1 52 ? 9.334 20.272 33.148 1.00 25.64 ? 67 LYS A CB 1 ATOM 398 C CG . LYS A 1 52 ? 8.675 21.235 32.156 1.00 27.79 ? 67 LYS A CG 1 ATOM 399 C CD . LYS A 1 52 ? 7.163 21.296 32.324 1.00 28.48 ? 67 LYS A CD 1 ATOM 400 C CE . LYS A 1 52 ? 6.763 22.001 33.613 1.00 32.13 ? 67 LYS A CE 1 ATOM 401 N NZ . LYS A 1 52 ? 7.205 23.426 33.652 1.00 32.31 ? 67 LYS A NZ 1 ATOM 402 N N . LEU A 1 53 ? 8.114 17.977 30.820 1.00 19.40 ? 68 LEU A N 1 ATOM 403 C CA . LEU A 1 53 ? 8.170 17.605 29.412 1.00 20.05 ? 68 LEU A CA 1 ATOM 404 C C . LEU A 1 53 ? 7.329 18.591 28.592 1.00 20.00 ? 68 LEU A C 1 ATOM 405 O O . LEU A 1 53 ? 6.385 19.185 29.112 1.00 20.40 ? 68 LEU A O 1 ATOM 406 C CB . LEU A 1 53 ? 7.635 16.180 29.211 1.00 22.03 ? 68 LEU A CB 1 ATOM 407 C CG . LEU A 1 53 ? 8.211 15.071 30.103 1.00 20.90 ? 68 LEU A CG 1 ATOM 408 C CD1 . LEU A 1 53 ? 7.414 14.995 31.411 1.00 19.79 ? 68 LEU A CD1 1 ATOM 409 C CD2 . LEU A 1 53 ? 8.145 13.738 29.372 1.00 19.12 ? 68 LEU A CD2 1 ATOM 410 N N . GLY A 1 54 ? 7.687 18.764 27.320 1.00 21.71 ? 69 GLY A N 1 ATOM 411 C CA . GLY A 1 54 ? 6.949 19.664 26.441 1.00 20.74 ? 69 GLY A CA 1 ATOM 412 C C . GLY A 1 54 ? 7.218 21.144 26.642 1.00 21.82 ? 69 GLY A C 1 ATOM 413 O O . GLY A 1 54 ? 6.474 21.988 26.139 1.00 20.83 ? 69 GLY A O 1 ATOM 414 N N . MET A 1 55 ? 8.289 21.472 27.362 1.00 20.45 ? 70 MET A N 1 ATOM 415 C CA . MET A 1 55 ? 8.609 22.868 27.630 1.00 20.58 ? 70 MET A CA 1 ATOM 416 C C . MET A 1 55 ? 9.640 23.499 26.700 1.00 20.88 ? 70 MET A C 1 ATOM 417 O O . MET A 1 55 ? 10.547 22.836 26.200 1.00 19.78 ? 70 MET A O 1 ATOM 418 C CB . MET A 1 55 ? 9.089 23.024 29.083 1.00 22.28 ? 70 MET A CB 1 ATOM 419 C CG . MET A 1 55 ? 9.515 24.444 29.451 1.00 24.65 ? 70 MET A CG 1 ATOM 420 S SD . MET A 1 55 ? 9.976 24.670 31.196 1.00 26.68 ? 70 MET A SD 1 ATOM 421 C CE . MET A 1 55 ? 11.536 23.857 31.227 1.00 23.77 ? 70 MET A CE 1 ATOM 422 N N . HIS A 1 56 ? 9.469 24.793 26.461 1.00 20.54 ? 71 HIS A N 1 ATOM 423 C CA . HIS A 1 56 ? 10.410 25.567 25.662 1.00 21.70 ? 71 HIS A CA 1 ATOM 424 C C . HIS A 1 56 ? 10.728 26.750 26.566 1.00 21.89 ? 71 HIS A C 1 ATOM 425 O O . HIS A 1 56 ? 11.733 26.752 27.275 1.00 20.25 ? 71 HIS A O 1 ATOM 426 C CB . HIS A 1 56 ? 9.788 26.060 24.357 1.00 20.66 ? 71 HIS A CB 1 ATOM 427 C CG . HIS A 1 56 ? 10.747 26.822 23.492 1.00 19.87 ? 71 HIS A CG 1 ATOM 428 N ND1 . HIS A 1 56 ? 11.685 26.203 22.697 1.00 21.52 ? 71 HIS A ND1 1 ATOM 429 C CD2 . HIS A 1 56 ? 10.940 28.154 23.334 1.00 20.76 ? 71 HIS A CD2 1 ATOM 430 C CE1 . HIS A 1 56 ? 12.415 27.118 22.084 1.00 21.96 ? 71 HIS A CE1 1 ATOM 431 N NE2 . HIS A 1 56 ? 11.984 28.311 22.454 1.00 20.22 ? 71 HIS A NE2 1 ATOM 432 N N . SER A 1 57 ? 9.853 27.751 26.559 1.00 22.20 ? 72 SER A N 1 ATOM 433 C CA . SER A 1 57 ? 10.050 28.908 27.423 1.00 22.52 ? 72 SER A CA 1 ATOM 434 C C . SER A 1 57 ? 9.613 28.574 28.842 1.00 23.49 ? 72 SER A C 1 ATOM 435 O O . SER A 1 57 ? 8.620 27.875 29.050 1.00 21.84 ? 72 SER A O 1 ATOM 436 C CB . SER A 1 57 ? 9.240 30.106 26.925 1.00 22.78 ? 72 SER A CB 1 ATOM 437 O OG . SER A 1 57 ? 9.227 31.125 27.911 1.00 25.16 ? 72 SER A OG 1 ATOM 438 N N . LYS A 1 58 ? 10.360 29.082 29.816 1.00 24.80 ? 73 LYS A N 1 ATOM 439 C CA . LYS A 1 58 ? 10.049 28.852 31.219 1.00 29.41 ? 73 LYS A CA 1 ATOM 440 C C . LYS A 1 58 ? 8.975 29.829 31.697 1.00 31.03 ? 73 LYS A C 1 ATOM 441 O O . LYS A 1 58 ? 8.335 29.606 32.725 1.00 31.93 ? 73 LYS A O 1 ATOM 442 C CB . LYS A 1 58 ? 11.320 29.006 32.061 1.00 30.52 ? 73 LYS A CB 1 ATOM 443 C CG . LYS A 1 58 ? 12.343 27.906 31.811 1.00 32.64 ? 73 LYS A CG 1 ATOM 444 C CD . LYS A 1 58 ? 13.767 28.326 32.171 1.00 35.05 ? 73 LYS A CD 1 ATOM 445 C CE . LYS A 1 58 ? 13.900 28.756 33.616 1.00 36.02 ? 73 LYS A CE 1 ATOM 446 N NZ . LYS A 1 58 ? 15.292 29.207 33.906 1.00 36.12 ? 73 LYS A NZ 1 ATOM 447 N N . ASN A 1 59 ? 8.769 30.903 30.941 1.00 32.34 ? 74 ASN A N 1 ATOM 448 C CA . ASN A 1 59 ? 7.777 31.913 31.304 1.00 35.13 ? 74 ASN A CA 1 ATOM 449 C C . ASN A 1 59 ? 6.521 31.853 30.439 1.00 35.34 ? 74 ASN A C 1 ATOM 450 O O . ASN A 1 59 ? 5.464 32.353 30.833 1.00 36.44 ? 74 ASN A O 1 ATOM 451 C CB . ASN A 1 59 ? 8.393 33.312 31.216 1.00 36.73 ? 74 ASN A CB 1 ATOM 452 C CG . ASN A 1 59 ? 9.572 33.487 32.150 1.00 39.01 ? 74 ASN A CG 1 ATOM 453 O OD1 . ASN A 1 59 ? 9.468 33.235 33.347 1.00 40.10 ? 74 ASN A OD1 1 ATOM 454 N ND2 . ASN A 1 59 ? 10.702 33.926 31.606 1.00 40.06 ? 74 ASN A ND2 1 ATOM 455 N N . ILE A 1 60 ? 6.642 31.258 29.257 1.00 34.41 ? 75 ILE A N 1 ATOM 456 C CA . ILE A 1 60 ? 5.512 31.118 28.343 1.00 34.63 ? 75 ILE A CA 1 ATOM 457 C C . ILE A 1 60 ? 5.261 29.628 28.138 1.00 34.67 ? 75 ILE A C 1 ATOM 458 O O . ILE A 1 60 ? 5.861 28.999 27.270 1.00 34.94 ? 75 ILE A O 1 ATOM 459 C CB . ILE A 1 60 ? 5.800 31.760 26.973 1.00 34.43 ? 75 ILE A CB 1 ATOM 460 C CG1 . ILE A 1 60 ? 6.081 33.254 27.143 1.00 34.63 ? 75 ILE A CG1 1 ATOM 461 C CG2 . ILE A 1 60 ? 4.612 31.536 26.041 1.00 35.41 ? 75 ILE A CG2 1 ATOM 462 C CD1 . ILE A 1 60 ? 6.460 33.960 25.854 1.00 34.28 ? 75 ILE A CD1 1 ATOM 463 N N . ARG A 1 61 ? 4.365 29.075 28.943 1.00 35.26 ? 76 ARG A N 1 ATOM 464 C CA . ARG A 1 61 ? 4.040 27.655 28.895 1.00 36.09 ? 76 ARG A CA 1 ATOM 465 C C . ARG A 1 61 ? 3.447 27.126 27.588 1.00 34.90 ? 76 ARG A C 1 ATOM 466 O O . ARG A 1 61 ? 2.483 27.686 27.060 1.00 34.13 ? 76 ARG A O 1 ATOM 467 C CB . ARG A 1 61 ? 3.082 27.319 30.043 1.00 39.95 ? 76 ARG A CB 1 ATOM 468 C CG . ARG A 1 61 ? 3.679 27.533 31.430 1.00 46.55 ? 76 ARG A CG 1 ATOM 469 C CD . ARG A 1 61 ? 2.667 27.243 32.534 1.00 51.30 ? 76 ARG A CD 1 ATOM 470 N NE . ARG A 1 61 ? 1.631 28.270 32.632 1.00 55.67 ? 76 ARG A NE 1 ATOM 471 C CZ . ARG A 1 61 ? 1.842 29.510 33.067 1.00 57.38 ? 76 ARG A CZ 1 ATOM 472 N NH1 . ARG A 1 61 ? 3.057 29.886 33.450 1.00 57.77 ? 76 ARG A NH1 1 ATOM 473 N NH2 . ARG A 1 61 ? 0.837 30.377 33.118 1.00 57.57 ? 76 ARG A NH2 1 ATOM 474 N N . ASN A 1 62 ? 4.035 26.051 27.066 1.00 31.39 ? 77 ASN A N 1 ATOM 475 C CA . ASN A 1 62 ? 3.506 25.414 25.866 1.00 30.97 ? 77 ASN A CA 1 ATOM 476 C C . ASN A 1 62 ? 2.213 24.762 26.355 1.00 30.51 ? 77 ASN A C 1 ATOM 477 O O . ASN A 1 62 ? 2.123 24.336 27.509 1.00 28.67 ? 77 ASN A O 1 ATOM 478 C CB . ASN A 1 62 ? 4.446 24.323 25.335 1.00 29.54 ? 77 ASN A CB 1 ATOM 479 C CG . ASN A 1 62 ? 5.549 24.868 24.436 1.00 29.32 ? 77 ASN A CG 1 ATOM 480 O OD1 . ASN A 1 62 ? 5.422 25.945 23.848 1.00 28.61 ? 77 ASN A OD1 1 ATOM 481 N ND2 . ASN A 1 62 ? 6.629 24.105 24.303 1.00 25.49 ? 77 ASN A ND2 1 ATOM 482 N N . GLU A 1 63 ? 1.218 24.675 25.485 1.00 30.38 ? 78 GLU A N 1 ATOM 483 C CA . GLU A 1 63 ? -0.059 24.085 25.864 1.00 32.52 ? 78 GLU A CA 1 ATOM 484 C C . GLU A 1 63 ? 0.033 22.613 26.286 1.00 31.66 ? 78 GLU A C 1 ATOM 485 O O . GLU A 1 63 ? -0.748 22.148 27.117 1.00 33.50 ? 78 GLU A O 1 ATOM 486 C CB . GLU A 1 63 ? -1.043 24.222 24.702 1.00 35.26 ? 78 GLU A CB 1 ATOM 487 C CG . GLU A 1 63 ? -2.463 23.813 25.032 1.00 39.58 ? 78 GLU A CG 1 ATOM 488 C CD . GLU A 1 63 ? -3.389 23.965 23.841 1.00 42.49 ? 78 GLU A CD 1 ATOM 489 O OE1 . GLU A 1 63 ? -4.602 23.715 23.997 1.00 44.33 ? 78 GLU A OE1 1 ATOM 490 O OE2 . GLU A 1 63 ? -2.900 24.332 22.749 1.00 42.47 ? 78 GLU A OE2 1 ATOM 491 N N . ASP A 1 64 ? 0.989 21.881 25.725 1.00 30.67 ? 79 ASP A N 1 ATOM 492 C CA . ASP A 1 64 ? 1.123 20.465 26.039 1.00 29.10 ? 79 ASP A CA 1 ATOM 493 C C . ASP A 1 64 ? 2.192 20.073 27.057 1.00 28.85 ? 79 ASP A C 1 ATOM 494 O O . ASP A 1 64 ? 2.637 18.925 27.072 1.00 27.30 ? 79 ASP A O 1 ATOM 495 C CB . ASP A 1 64 ? 1.317 19.667 24.742 1.00 27.85 ? 79 ASP A CB 1 ATOM 496 C CG . ASP A 1 64 ? 2.367 20.273 23.823 1.00 29.75 ? 79 ASP A CG 1 ATOM 497 O OD1 . ASP A 1 64 ? 2.777 21.431 24.053 1.00 30.10 ? 79 ASP A OD1 1 ATOM 498 O OD2 . ASP A 1 64 ? 2.771 19.592 22.856 1.00 30.86 ? 79 ASP A OD2 1 ATOM 499 N N . GLU A 1 65 ? 2.598 21.008 27.911 1.00 27.87 ? 80 GLU A N 1 ATOM 500 C CA . GLU A 1 65 ? 3.598 20.690 28.929 1.00 28.37 ? 80 GLU A CA 1 ATOM 501 C C . GLU A 1 65 ? 3.037 19.636 29.871 1.00 28.22 ? 80 GLU A C 1 ATOM 502 O O . GLU A 1 65 ? 1.831 19.587 30.117 1.00 26.98 ? 80 GLU A O 1 ATOM 503 C CB . GLU A 1 65 ? 3.960 21.911 29.774 1.00 30.16 ? 80 GLU A CB 1 ATOM 504 C CG . GLU A 1 65 ? 4.745 23.004 29.084 1.00 32.17 ? 80 GLU A CG 1 ATOM 505 C CD . GLU A 1 65 ? 5.409 23.926 30.093 1.00 33.70 ? 80 GLU A CD 1 ATOM 506 O OE1 . GLU A 1 65 ? 4.921 23.996 31.242 1.00 34.89 ? 80 GLU A OE1 1 ATOM 507 O OE2 . GLU A 1 65 ? 6.410 24.583 29.744 1.00 35.06 ? 80 GLU A OE2 1 ATOM 508 N N . GLN A 1 66 ? 3.921 18.805 30.407 1.00 26.95 ? 81 GLN A N 1 ATOM 509 C CA . GLN A 1 66 ? 3.527 17.765 31.348 1.00 27.38 ? 81 GLN A CA 1 ATOM 510 C C . GLN A 1 66 ? 4.571 17.708 32.458 1.00 26.42 ? 81 GLN A C 1 ATOM 511 O O . GLN A 1 66 ? 5.740 18.023 32.235 1.00 24.11 ? 81 GLN A O 1 ATOM 512 C CB . GLN A 1 66 ? 3.446 16.406 30.647 1.00 28.79 ? 81 GLN A CB 1 ATOM 513 C CG . GLN A 1 66 ? 2.280 16.239 29.667 1.00 30.85 ? 81 GLN A CG 1 ATOM 514 C CD . GLN A 1 66 ? 0.924 16.239 30.357 1.00 32.89 ? 81 GLN A CD 1 ATOM 515 O OE1 . GLN A 1 66 ? 0.734 15.573 31.372 1.00 33.54 ? 81 GLN A OE1 1 ATOM 516 N NE2 . GLN A 1 66 ? -0.028 16.981 29.799 1.00 33.74 ? 81 GLN A NE2 1 ATOM 517 N N . ILE A 1 67 ? 4.139 17.326 33.654 1.00 26.88 ? 82 ILE A N 1 ATOM 518 C CA . ILE A 1 67 ? 5.038 17.198 34.794 1.00 27.00 ? 82 ILE A CA 1 ATOM 519 C C . ILE A 1 67 ? 4.951 15.754 35.276 1.00 27.79 ? 82 ILE A C 1 ATOM 520 O O . ILE A 1 67 ? 3.855 15.201 35.407 1.00 26.98 ? 82 ILE A O 1 ATOM 521 C CB . ILE A 1 67 ? 4.636 18.156 35.943 1.00 27.81 ? 82 ILE A CB 1 ATOM 522 C CG1 . ILE A 1 67 ? 4.880 19.607 35.511 1.00 30.40 ? 82 ILE A CG1 1 ATOM 523 C CG2 . ILE A 1 67 ? 5.429 17.826 37.206 1.00 28.00 ? 82 ILE A CG2 1 ATOM 524 C CD1 . ILE A 1 67 ? 4.483 20.647 36.551 1.00 32.46 ? 82 ILE A CD1 1 ATOM 525 N N . ARG A 1 68 ? 6.105 15.141 35.521 1.00 25.85 ? 83 ARG A N 1 ATOM 526 C CA . ARG A 1 68 ? 6.142 13.756 35.977 1.00 26.67 ? 83 ARG A CA 1 ATOM 527 C C . ARG A 1 68 ? 7.193 13.527 37.054 1.00 26.17 ? 83 ARG A C 1 ATOM 528 O O . ARG A 1 68 ? 8.133 14.312 37.212 1.00 26.36 ? 83 ARG A O 1 ATOM 529 C CB . ARG A 1 68 ? 6.426 12.817 34.800 1.00 24.55 ? 83 ARG A CB 1 ATOM 530 C CG . ARG A 1 68 ? 5.322 12.751 33.757 1.00 23.92 ? 83 ARG A CG 1 ATOM 531 C CD . ARG A 1 68 ? 4.102 11.977 34.269 1.00 22.26 ? 83 ARG A CD 1 ATOM 532 N NE . ARG A 1 68 ? 3.113 11.794 33.211 1.00 24.18 ? 83 ARG A NE 1 ATOM 533 C CZ . ARG A 1 68 ? 2.280 12.739 32.790 1.00 23.11 ? 83 ARG A CZ 1 ATOM 534 N NH1 . ARG A 1 68 ? 2.303 13.943 33.344 1.00 25.71 ? 83 ARG A NH1 1 ATOM 535 N NH2 . ARG A 1 68 ? 1.437 12.483 31.798 1.00 24.80 ? 83 ARG A NH2 1 ATOM 536 N N . VAL A 1 69 ? 7.007 12.449 37.804 1.00 26.25 ? 84 VAL A N 1 ATOM 537 C CA . VAL A 1 69 ? 7.936 12.068 38.855 1.00 26.71 ? 84 VAL A CA 1 ATOM 538 C C . VAL A 1 69 ? 8.367 10.636 38.557 1.00 25.74 ? 84 VAL A C 1 ATOM 539 O O . VAL A 1 69 ? 7.694 9.913 37.824 1.00 25.46 ? 84 VAL A O 1 ATOM 540 C CB . VAL A 1 69 ? 7.281 12.139 40.260 1.00 28.05 ? 84 VAL A CB 1 ATOM 541 C CG1 . VAL A 1 69 ? 6.879 13.572 40.571 1.00 29.24 ? 84 VAL A CG1 1 ATOM 542 C CG2 . VAL A 1 69 ? 6.070 11.223 40.323 1.00 27.59 ? 84 VAL A CG2 1 ATOM 543 N N . PRO A 1 70 ? 9.507 10.210 39.109 1.00 25.47 ? 85 PRO A N 1 ATOM 544 C CA . PRO A 1 70 ? 9.949 8.842 38.839 1.00 27.33 ? 85 PRO A CA 1 ATOM 545 C C . PRO A 1 70 ? 9.162 7.798 39.622 1.00 28.42 ? 85 PRO A C 1 ATOM 546 O O . PRO A 1 70 ? 8.521 8.111 40.624 1.00 28.63 ? 85 PRO A O 1 ATOM 547 C CB . PRO A 1 70 ? 11.417 8.854 39.273 1.00 25.12 ? 85 PRO A CB 1 ATOM 548 C CG . PRO A 1 70 ? 11.803 10.307 39.224 1.00 26.67 ? 85 PRO A CG 1 ATOM 549 C CD . PRO A 1 70 ? 10.571 10.988 39.761 1.00 25.59 ? 85 PRO A CD 1 ATOM 550 N N . ARG A 1 71 ? 9.217 6.563 39.137 1.00 30.22 ? 86 ARG A N 1 ATOM 551 C CA . ARG A 1 71 ? 8.600 5.419 39.797 1.00 30.59 ? 86 ARG A CA 1 ATOM 552 C C . ARG A 1 71 ? 9.737 4.405 39.871 1.00 30.34 ? 86 ARG A C 1 ATOM 553 O O . ARG A 1 71 ? 9.672 3.420 40.602 1.00 29.83 ? 86 ARG A O 1 ATOM 554 C CB . ARG A 1 71 ? 7.436 4.848 38.978 1.00 31.62 ? 86 ARG A CB 1 ATOM 555 C CG . ARG A 1 71 ? 7.822 4.306 37.615 1.00 36.80 ? 86 ARG A CG 1 ATOM 556 C CD . ARG A 1 71 ? 6.643 3.607 36.953 1.00 39.63 ? 86 ARG A CD 1 ATOM 557 N NE . ARG A 1 71 ? 6.239 2.411 37.688 1.00 41.64 ? 86 ARG A NE 1 ATOM 558 C CZ . ARG A 1 71 ? 5.245 1.605 37.323 1.00 43.57 ? 86 ARG A CZ 1 ATOM 559 N NH1 . ARG A 1 71 ? 4.543 1.865 36.227 1.00 43.86 ? 86 ARG A NH1 1 ATOM 560 N NH2 . ARG A 1 71 ? 4.956 0.534 38.050 1.00 42.88 ? 86 ARG A NH2 1 ATOM 561 N N . GLY A 1 72 ? 10.793 4.672 39.107 1.00 29.02 ? 87 GLY A N 1 ATOM 562 C CA . GLY A 1 72 ? 11.946 3.788 39.097 1.00 28.32 ? 87 GLY A CA 1 ATOM 563 C C . GLY A 1 72 ? 13.155 4.461 38.476 1.00 27.79 ? 87 GLY A C 1 ATOM 564 O O . GLY A 1 72 ? 13.016 5.228 37.524 1.00 27.53 ? 87 GLY A O 1 ATOM 565 N N . LYS A 1 73 ? 14.336 4.186 39.021 1.00 26.22 ? 88 LYS A N 1 ATOM 566 C CA . LYS A 1 73 ? 15.578 4.763 38.514 1.00 25.73 ? 88 LYS A CA 1 ATOM 567 C C . LYS A 1 73 ? 16.613 3.654 38.358 1.00 25.30 ? 88 LYS A C 1 ATOM 568 O O . LYS A 1 73 ? 16.829 2.864 39.277 1.00 25.16 ? 88 LYS A O 1 ATOM 569 C CB . LYS A 1 73 ? 16.079 5.856 39.467 1.00 26.31 ? 88 LYS A CB 1 ATOM 570 C CG . LYS A 1 73 ? 15.168 7.079 39.491 1.00 26.10 ? 88 LYS A CG 1 ATOM 571 C CD . LYS A 1 73 ? 15.730 8.244 40.298 1.00 27.70 ? 88 LYS A CD 1 ATOM 572 C CE . LYS A 1 73 ? 15.647 7.989 41.798 1.00 26.11 ? 88 LYS A CE 1 ATOM 573 N NZ . LYS A 1 73 ? 16.101 9.160 42.596 1.00 22.55 ? 88 LYS A NZ 1 ATOM 574 N N . TYR A 1 74 ? 17.254 3.591 37.195 1.00 22.93 ? 89 TYR A N 1 ATOM 575 C CA . TYR A 1 74 ? 18.223 2.534 36.946 1.00 21.41 ? 89 TYR A CA 1 ATOM 576 C C . TYR A 1 74 ? 19.603 3.027 36.552 1.00 23.03 ? 89 TYR A C 1 ATOM 577 O O . TYR A 1 74 ? 19.745 3.967 35.759 1.00 19.80 ? 89 TYR A O 1 ATOM 578 C CB . TYR A 1 74 ? 17.669 1.585 35.885 1.00 23.83 ? 89 TYR A CB 1 ATOM 579 C CG . TYR A 1 74 ? 16.250 1.151 36.200 1.00 28.81 ? 89 TYR A CG 1 ATOM 580 C CD1 . TYR A 1 74 ? 15.167 1.984 35.915 1.00 27.84 ? 89 TYR A CD1 1 ATOM 581 C CD2 . TYR A 1 74 ? 15.999 -0.057 36.850 1.00 29.71 ? 89 TYR A CD2 1 ATOM 582 C CE1 . TYR A 1 74 ? 13.871 1.630 36.274 1.00 30.85 ? 89 TYR A CE1 1 ATOM 583 C CE2 . TYR A 1 74 ? 14.702 -0.423 37.214 1.00 32.21 ? 89 TYR A CE2 1 ATOM 584 C CZ . TYR A 1 74 ? 13.647 0.427 36.926 1.00 33.06 ? 89 TYR A CZ 1 ATOM 585 O OH . TYR A 1 74 ? 12.372 0.086 37.302 1.00 35.60 ? 89 TYR A OH 1 ATOM 586 N N . PHE A 1 75 ? 20.617 2.373 37.112 1.00 21.61 ? 90 PHE A N 1 ATOM 587 C CA . PHE A 1 75 ? 22.006 2.736 36.862 1.00 21.87 ? 90 PHE A CA 1 ATOM 588 C C . PHE A 1 75 ? 22.868 1.549 36.454 1.00 23.35 ? 90 PHE A C 1 ATOM 589 O O . PHE A 1 75 ? 22.454 0.384 36.535 1.00 23.34 ? 90 PHE A O 1 ATOM 590 C CB . PHE A 1 75 ? 22.647 3.327 38.123 1.00 23.70 ? 90 PHE A CB 1 ATOM 591 C CG . PHE A 1 75 ? 21.832 4.390 38.798 1.00 25.35 ? 90 PHE A CG 1 ATOM 592 C CD1 . PHE A 1 75 ? 20.712 4.056 39.555 1.00 24.83 ? 90 PHE A CD1 1 ATOM 593 C CD2 . PHE A 1 75 ? 22.210 5.725 38.711 1.00 23.67 ? 90 PHE A CD2 1 ATOM 594 C CE1 . PHE A 1 75 ? 19.984 5.037 40.219 1.00 25.79 ? 90 PHE A CE1 1 ATOM 595 C CE2 . PHE A 1 75 ? 21.489 6.720 39.374 1.00 23.10 ? 90 PHE A CE2 1 ATOM 596 C CZ . PHE A 1 75 ? 20.373 6.375 40.132 1.00 25.63 ? 90 PHE A CZ 1 ATOM 597 N N . CYS A 1 76 ? 24.083 1.868 36.022 1.00 21.84 ? 91 CYS A N 1 ATOM 598 C CA . CYS A 1 76 ? 25.063 0.859 35.667 1.00 22.21 ? 91 CYS A CA 1 ATOM 599 C C . CYS A 1 76 ? 25.675 0.486 37.007 1.00 23.69 ? 91 CYS A C 1 ATOM 600 O O . CYS A 1 76 ? 26.000 1.370 37.803 1.00 24.08 ? 91 CYS A O 1 ATOM 601 C CB . CYS A 1 76 ? 26.155 1.445 34.783 1.00 24.29 ? 91 CYS A CB 1 ATOM 602 S SG . CYS A 1 76 ? 25.646 1.780 33.077 1.00 25.41 ? 91 CYS A SG 1 ATOM 603 N N . LEU A 1 77 ? 25.835 -0.807 37.265 1.00 24.92 ? 92 LEU A N 1 ATOM 604 C CA . LEU A 1 77 ? 26.399 -1.237 38.540 1.00 25.52 ? 92 LEU A CA 1 ATOM 605 C C . LEU A 1 77 ? 27.850 -1.678 38.427 1.00 26.92 ? 92 LEU A C 1 ATOM 606 O O . LEU A 1 77 ? 28.536 -1.840 39.439 1.00 28.86 ? 92 LEU A O 1 ATOM 607 C CB . LEU A 1 77 ? 25.549 -2.365 39.134 1.00 26.75 ? 92 LEU A CB 1 ATOM 608 C CG . LEU A 1 77 ? 24.051 -2.051 39.227 1.00 27.17 ? 92 LEU A CG 1 ATOM 609 C CD1 . LEU A 1 77 ? 23.332 -3.164 39.978 1.00 27.97 ? 92 LEU A CD1 1 ATOM 610 C CD2 . LEU A 1 77 ? 23.846 -0.711 39.928 1.00 27.09 ? 92 LEU A CD2 1 ATOM 611 N N . ASN A 1 78 ? 28.316 -1.869 37.198 1.00 27.98 ? 93 ASN A N 1 ATOM 612 C CA . ASN A 1 78 ? 29.692 -2.291 36.957 1.00 30.76 ? 93 ASN A CA 1 ATOM 613 C C . ASN A 1 78 ? 30.540 -1.112 36.484 1.00 30.94 ? 93 ASN A C 1 ATOM 614 O O . ASN A 1 78 ? 30.846 -0.993 35.300 1.00 34.00 ? 93 ASN A O 1 ATOM 615 C CB . ASN A 1 78 ? 29.712 -3.411 35.912 1.00 31.52 ? 93 ASN A CB 1 ATOM 616 C CG . ASN A 1 78 ? 29.089 -2.991 34.585 1.00 34.63 ? 93 ASN A CG 1 ATOM 617 O OD1 . ASN A 1 78 ? 28.081 -2.282 34.552 1.00 35.91 ? 93 ASN A OD1 1 ATOM 618 N ND2 . ASN A 1 78 ? 29.680 -3.443 33.488 1.00 33.31 ? 93 ASN A ND2 1 ATOM 619 N N . THR A 1 79 ? 30.922 -0.243 37.413 1.00 30.08 ? 94 THR A N 1 ATOM 620 C CA . THR A 1 79 ? 31.722 0.924 37.068 1.00 30.39 ? 94 THR A CA 1 ATOM 621 C C . THR A 1 79 ? 33.149 0.821 37.590 1.00 31.80 ? 94 THR A C 1 ATOM 622 O O . THR A 1 79 ? 33.410 0.183 38.612 1.00 31.01 ? 94 THR A O 1 ATOM 623 C CB . THR A 1 79 ? 31.090 2.227 37.618 1.00 28.93 ? 94 THR A CB 1 ATOM 624 O OG1 . THR A 1 79 ? 31.062 2.189 39.051 1.00 27.90 ? 94 THR A OG1 1 ATOM 625 C CG2 . THR A 1 79 ? 29.670 2.395 37.089 1.00 27.82 ? 94 THR A CG2 1 ATOM 626 N N . LYS A 1 80 ? 34.073 1.458 36.881 1.00 31.16 ? 95 LYS A N 1 ATOM 627 C CA . LYS A 1 80 ? 35.470 1.441 37.283 1.00 31.79 ? 95 LYS A CA 1 ATOM 628 C C . LYS A 1 80 ? 35.637 2.216 38.586 1.00 30.60 ? 95 LYS A C 1 ATOM 629 O O . LYS A 1 80 ? 36.463 1.860 39.423 1.00 31.90 ? 95 LYS A O 1 ATOM 630 C CB . LYS A 1 80 ? 36.344 2.053 36.181 1.00 31.60 ? 95 LYS A CB 1 ATOM 631 C CG . LYS A 1 80 ? 37.844 1.882 36.400 1.00 34.75 ? 95 LYS A CG 1 ATOM 632 C CD . LYS A 1 80 ? 38.636 2.351 35.186 1.00 33.55 ? 95 LYS A CD 1 ATOM 633 C CE . LYS A 1 80 ? 40.134 2.154 35.388 1.00 36.05 ? 95 LYS A CE 1 ATOM 634 N NZ . LYS A 1 80 ? 40.933 2.590 34.201 1.00 34.66 ? 95 LYS A NZ 1 ATOM 635 N N . PHE A 1 81 A 34.840 3.264 38.767 1.00 28.85 ? 95 PHE A N 1 ATOM 636 C CA . PHE A 1 81 A 34.917 4.082 39.976 1.00 27.54 ? 95 PHE A CA 1 ATOM 637 C C . PHE A 1 81 A 33.655 3.944 40.829 1.00 26.86 ? 95 PHE A C 1 ATOM 638 O O . PHE A 1 81 A 32.549 3.848 40.303 1.00 25.40 ? 95 PHE A O 1 ATOM 639 C CB . PHE A 1 81 A 35.146 5.539 39.584 1.00 28.73 ? 95 PHE A CB 1 ATOM 640 C CG . PHE A 1 81 A 36.340 5.730 38.686 1.00 31.32 ? 95 PHE A CG 1 ATOM 641 C CD1 . PHE A 1 81 A 36.264 6.538 37.561 1.00 31.70 ? 95 PHE A CD1 1 ATOM 642 C CD2 . PHE A 1 81 A 37.533 5.065 38.952 1.00 29.08 ? 95 PHE A CD2 1 ATOM 643 C CE1 . PHE A 1 81 A 37.361 6.680 36.706 1.00 32.98 ? 95 PHE A CE1 1 ATOM 644 C CE2 . PHE A 1 81 A 38.635 5.201 38.105 1.00 31.89 ? 95 PHE A CE2 1 ATOM 645 C CZ . PHE A 1 81 A 38.546 6.009 36.980 1.00 32.00 ? 95 PHE A CZ 1 ATOM 646 N N . PRO A 1 82 ? 33.808 3.939 42.164 1.00 26.94 ? 96 PRO A N 1 ATOM 647 C CA . PRO A 1 82 ? 32.668 3.803 43.080 1.00 26.84 ? 96 PRO A CA 1 ATOM 648 C C . PRO A 1 82 ? 31.544 4.839 42.964 1.00 25.79 ? 96 PRO A C 1 ATOM 649 O O . PRO A 1 82 ? 30.386 4.518 43.243 1.00 25.52 ? 96 PRO A O 1 ATOM 650 C CB . PRO A 1 82 ? 33.331 3.791 44.459 1.00 27.33 ? 96 PRO A CB 1 ATOM 651 C CG . PRO A 1 82 ? 34.555 4.640 44.252 1.00 27.64 ? 96 PRO A CG 1 ATOM 652 C CD . PRO A 1 82 ? 35.061 4.145 42.913 1.00 27.04 ? 96 PRO A CD 1 ATOM 653 N N . ASN A 1 83 ? 31.864 6.072 42.569 1.00 24.10 ? 97 ASN A N 1 ATOM 654 C CA . ASN A 1 83 ? 30.817 7.081 42.423 1.00 22.65 ? 97 ASN A CA 1 ATOM 655 C C . ASN A 1 83 ? 30.031 6.839 41.139 1.00 21.79 ? 97 ASN A C 1 ATOM 656 O O . ASN A 1 83 ? 29.026 7.502 40.885 1.00 21.60 ? 97 ASN A O 1 ATOM 657 C CB . ASN A 1 83 ? 31.390 8.504 42.417 1.00 24.47 ? 97 ASN A CB 1 ATOM 658 C CG . ASN A 1 83 ? 32.372 8.742 41.284 1.00 21.48 ? 97 ASN A CG 1 ATOM 659 O OD1 . ASN A 1 83 ? 32.394 8.015 40.288 1.00 25.37 ? 97 ASN A OD1 1 ATOM 660 N ND2 . ASN A 1 83 ? 33.191 9.773 41.432 1.00 27.46 ? 97 ASN A ND2 1 ATOM 661 N N . GLY A 1 84 ? 30.508 5.886 40.338 1.00 19.89 ? 98 GLY A N 1 ATOM 662 C CA . GLY A 1 84 ? 29.854 5.517 39.096 1.00 20.99 ? 98 GLY A CA 1 ATOM 663 C C . GLY A 1 84 ? 29.928 6.528 37.961 1.00 21.74 ? 98 GLY A C 1 ATOM 664 O O . GLY A 1 84 ? 29.284 6.343 36.929 1.00 20.17 ? 98 GLY A O 1 ATOM 665 N N . LEU A 1 85 ? 30.731 7.571 38.131 1.00 22.34 ? 99 LEU A N 1 ATOM 666 C CA . LEU A 1 85 ? 30.835 8.618 37.116 1.00 25.09 ? 99 LEU A CA 1 ATOM 667 C C . LEU A 1 85 ? 31.510 8.273 35.792 1.00 25.03 ? 99 LEU A C 1 ATOM 668 O O . LEU A 1 85 ? 31.427 9.056 34.840 1.00 23.61 ? 99 LEU A O 1 ATOM 669 C CB . LEU A 1 85 ? 31.485 9.861 37.725 1.00 25.59 ? 99 LEU A CB 1 ATOM 670 C CG . LEU A 1 85 ? 30.695 10.461 38.891 1.00 28.05 ? 99 LEU A CG 1 ATOM 671 C CD1 . LEU A 1 85 ? 31.398 11.708 39.397 1.00 28.25 ? 99 LEU A CD1 1 ATOM 672 C CD2 . LEU A 1 85 ? 29.275 10.791 38.447 1.00 28.48 ? 99 LEU A CD2 1 ATOM 673 N N . ASP A 1 86 ? 32.173 7.120 35.709 1.00 25.20 ? 100 ASP A N 1 ATOM 674 C CA . ASP A 1 86 ? 32.803 6.730 34.448 1.00 25.00 ? 100 ASP A CA 1 ATOM 675 C C . ASP A 1 86 ? 31.734 6.198 33.493 1.00 25.37 ? 100 ASP A C 1 ATOM 676 O O . ASP A 1 86 ? 31.970 6.053 32.300 1.00 25.10 ? 100 ASP A O 1 ATOM 677 C CB . ASP A 1 86 ? 33.906 5.684 34.668 1.00 25.50 ? 100 ASP A CB 1 ATOM 678 C CG . ASP A 1 86 ? 33.452 4.525 35.523 1.00 25.46 ? 100 ASP A CG 1 ATOM 679 O OD1 . ASP A 1 86 ? 33.135 4.763 36.704 1.00 23.16 ? 100 ASP A OD1 1 ATOM 680 O OD2 . ASP A 1 86 ? 33.413 3.385 35.010 1.00 24.09 ? 100 ASP A OD2 1 ATOM 681 N N . LYS A 1 87 ? 30.554 5.903 34.034 1.00 23.82 ? 101 LYS A N 1 ATOM 682 C CA . LYS A 1 87 ? 29.422 5.444 33.233 1.00 22.93 ? 101 LYS A CA 1 ATOM 683 C C . LYS A 1 87 ? 28.256 6.297 33.724 1.00 23.04 ? 101 LYS A C 1 ATOM 684 O O . LYS A 1 87 ? 27.327 5.810 34.377 1.00 23.48 ? 101 LYS A O 1 ATOM 685 C CB . LYS A 1 87 ? 29.153 3.949 33.456 1.00 23.57 ? 101 LYS A CB 1 ATOM 686 C CG . LYS A 1 87 ? 30.321 3.060 33.030 1.00 23.32 ? 101 LYS A CG 1 ATOM 687 C CD . LYS A 1 87 ? 29.970 1.582 33.021 1.00 26.01 ? 101 LYS A CD 1 ATOM 688 C CE . LYS A 1 87 ? 31.216 0.739 32.717 1.00 26.14 ? 101 LYS A CE 1 ATOM 689 N NZ . LYS A 1 87 ? 30.935 -0.727 32.686 1.00 28.28 ? 101 LYS A NZ 1 ATOM 690 N N . ASP A 1 88 ? 28.342 7.588 33.412 1.00 21.75 ? 102 ASP A N 1 ATOM 691 C CA . ASP A 1 88 ? 27.360 8.583 33.829 1.00 21.30 ? 102 ASP A CA 1 ATOM 692 C C . ASP A 1 88 ? 26.092 8.515 32.980 1.00 22.75 ? 102 ASP A C 1 ATOM 693 O O . ASP A 1 88 ? 25.905 9.298 32.046 1.00 22.37 ? 102 ASP A O 1 ATOM 694 C CB . ASP A 1 88 ? 28.001 9.968 33.739 1.00 21.49 ? 102 ASP A CB 1 ATOM 695 C CG . ASP A 1 88 ? 27.360 10.984 34.664 1.00 21.44 ? 102 ASP A CG 1 ATOM 696 O OD1 . ASP A 1 88 ? 27.891 12.113 34.736 1.00 22.99 ? 102 ASP A OD1 1 ATOM 697 O OD2 . ASP A 1 88 ? 26.335 10.675 35.312 1.00 20.40 ? 102 ASP A OD2 1 ATOM 698 N N . ILE A 1 89 ? 25.224 7.567 33.312 1.00 20.83 ? 103 ILE A N 1 ATOM 699 C CA . ILE A 1 89 ? 23.976 7.378 32.578 1.00 21.24 ? 103 ILE A CA 1 ATOM 700 C C . ILE A 1 89 ? 22.921 6.818 33.525 1.00 23.21 ? 103 ILE A C 1 ATOM 701 O O . ILE A 1 89 ? 23.239 6.069 34.448 1.00 23.10 ? 103 ILE A O 1 ATOM 702 C CB . ILE A 1 89 ? 24.190 6.411 31.385 1.00 22.99 ? 103 ILE A CB 1 ATOM 703 C CG1 . ILE A 1 89 ? 22.873 6.166 30.648 1.00 22.67 ? 103 ILE A CG1 1 ATOM 704 C CG2 . ILE A 1 89 ? 24.771 5.094 31.877 1.00 24.10 ? 103 ILE A CG2 1 ATOM 705 C CD1 . ILE A 1 89 ? 23.047 5.385 29.354 1.00 25.17 ? 103 ILE A CD1 1 ATOM 706 N N . MET A 1 90 ? 21.668 7.187 33.308 1.00 21.41 ? 104 MET A N 1 ATOM 707 C CA . MET A 1 90 ? 20.593 6.706 34.173 1.00 23.75 ? 104 MET A CA 1 ATOM 708 C C . MET A 1 90 ? 19.265 6.705 33.438 1.00 22.75 ? 104 MET A C 1 ATOM 709 O O . MET A 1 90 ? 18.987 7.605 32.642 1.00 22.55 ? 104 MET A O 1 ATOM 710 C CB . MET A 1 90 ? 20.489 7.594 35.420 1.00 25.10 ? 104 MET A CB 1 ATOM 711 C CG . MET A 1 90 ? 19.182 7.449 36.205 1.00 30.40 ? 104 MET A CG 1 ATOM 712 S SD . MET A 1 90 ? 19.125 8.476 37.704 1.00 34.67 ? 104 MET A SD 1 ATOM 713 C CE . MET A 1 90 ? 19.058 10.084 37.024 1.00 32.71 ? 104 MET A CE 1 ATOM 714 N N . LEU A 1 91 ? 18.458 5.682 33.696 1.00 20.17 ? 105 LEU A N 1 ATOM 715 C CA . LEU A 1 91 ? 17.141 5.581 33.088 1.00 20.63 ? 105 LEU A CA 1 ATOM 716 C C . LEU A 1 91 ? 16.106 5.870 34.158 1.00 21.52 ? 105 LEU A C 1 ATOM 717 O O . LEU A 1 91 ? 16.197 5.361 35.283 1.00 24.34 ? 105 LEU A O 1 ATOM 718 C CB . LEU A 1 91 ? 16.901 4.180 32.514 1.00 19.67 ? 105 LEU A CB 1 ATOM 719 C CG . LEU A 1 91 ? 17.397 3.932 31.090 1.00 22.05 ? 105 LEU A CG 1 ATOM 720 C CD1 . LEU A 1 91 ? 17.252 2.448 30.738 1.00 20.68 ? 105 LEU A CD1 1 ATOM 721 C CD2 . LEU A 1 91 ? 16.592 4.804 30.120 1.00 21.08 ? 105 LEU A CD2 1 ATOM 722 N N . ILE A 1 92 ? 15.137 6.706 33.815 1.00 21.15 ? 106 ILE A N 1 ATOM 723 C CA . ILE A 1 92 ? 14.073 7.055 34.742 1.00 21.11 ? 106 ILE A CA 1 ATOM 724 C C . ILE A 1 92 ? 12.767 6.556 34.156 1.00 22.58 ? 106 ILE A C 1 ATOM 725 O O . ILE A 1 92 ? 12.468 6.829 32.995 1.00 20.94 ? 106 ILE A O 1 ATOM 726 C CB . ILE A 1 92 ? 13.947 8.587 34.927 1.00 22.04 ? 106 ILE A CB 1 ATOM 727 C CG1 . ILE A 1 92 ? 15.232 9.157 35.538 1.00 22.90 ? 106 ILE A CG1 1 ATOM 728 C CG2 . ILE A 1 92 ? 12.727 8.910 35.807 1.00 22.71 ? 106 ILE A CG2 1 ATOM 729 C CD1 . ILE A 1 92 ? 15.201 10.670 35.758 1.00 21.46 ? 106 ILE A CD1 1 ATOM 730 N N . ARG A 1 93 ? 12.003 5.794 34.931 1.00 23.16 ? 107 ARG A N 1 ATOM 731 C CA . ARG A 1 93 ? 10.708 5.355 34.436 1.00 24.08 ? 107 ARG A CA 1 ATOM 732 C C . ARG A 1 93 ? 9.720 6.345 35.038 1.00 22.04 ? 107 ARG A C 1 ATOM 733 O O . ARG A 1 93 ? 9.739 6.589 36.242 1.00 22.55 ? 107 ARG A O 1 ATOM 734 C CB . ARG A 1 93 ? 10.357 3.935 34.891 1.00 25.65 ? 107 ARG A CB 1 ATOM 735 C CG . ARG A 1 93 ? 9.055 3.445 34.255 1.00 27.77 ? 107 ARG A CG 1 ATOM 736 C CD . ARG A 1 93 ? 8.652 2.052 34.708 1.00 31.21 ? 107 ARG A CD 1 ATOM 737 N NE . ARG A 1 93 ? 7.474 1.593 33.977 1.00 33.25 ? 107 ARG A NE 1 ATOM 738 C CZ . ARG A 1 93 ? 6.855 0.437 34.198 1.00 35.85 ? 107 ARG A CZ 1 ATOM 739 N NH1 . ARG A 1 93 ? 7.300 -0.388 35.137 1.00 34.73 ? 107 ARG A NH1 1 ATOM 740 N NH2 . ARG A 1 93 ? 5.792 0.104 33.475 1.00 35.12 ? 107 ARG A NH2 1 ATOM 741 N N . LEU A 1 94 ? 8.874 6.930 34.197 1.00 24.10 ? 108 LEU A N 1 ATOM 742 C CA . LEU A 1 94 ? 7.892 7.900 34.664 1.00 23.97 ? 108 LEU A CA 1 ATOM 743 C C . LEU A 1 94 ? 6.755 7.178 35.387 1.00 24.64 ? 108 LEU A C 1 ATOM 744 O O . LEU A 1 94 ? 6.334 6.100 34.967 1.00 25.56 ? 108 LEU A O 1 ATOM 745 C CB . LEU A 1 94 ? 7.340 8.693 33.475 1.00 22.28 ? 108 LEU A CB 1 ATOM 746 C CG . LEU A 1 94 ? 8.405 9.329 32.571 1.00 22.53 ? 108 LEU A CG 1 ATOM 747 C CD1 . LEU A 1 94 ? 7.729 10.026 31.395 1.00 24.06 ? 108 LEU A CD1 1 ATOM 748 C CD2 . LEU A 1 94 ? 9.253 10.316 33.377 1.00 23.56 ? 108 LEU A CD2 1 ATOM 749 N N . ARG A 1 95 ? 6.266 7.777 36.468 1.00 27.41 ? 109 ARG A N 1 ATOM 750 C CA . ARG A 1 95 ? 5.184 7.180 37.248 1.00 29.00 ? 109 ARG A CA 1 ATOM 751 C C . ARG A 1 95 ? 3.963 6.940 36.359 1.00 30.64 ? 109 ARG A C 1 ATOM 752 O O . ARG A 1 95 ? 3.263 5.941 36.511 1.00 30.10 ? 109 ARG A O 1 ATOM 753 C CB . ARG A 1 95 ? 4.828 8.081 38.435 1.00 30.26 ? 109 ARG A CB 1 ATOM 754 C CG . ARG A 1 95 ? 4.014 7.376 39.523 1.00 32.75 ? 109 ARG A CG 1 ATOM 755 C CD . ARG A 1 95 ? 4.079 8.124 40.849 1.00 35.88 ? 109 ARG A CD 1 ATOM 756 N NE . ARG A 1 95 ? 3.429 9.429 40.783 1.00 38.03 ? 109 ARG A NE 1 ATOM 757 C CZ . ARG A 1 95 ? 3.439 10.323 41.767 1.00 38.19 ? 109 ARG A CZ 1 ATOM 758 N NH1 . ARG A 1 95 ? 4.068 10.058 42.902 1.00 38.22 ? 109 ARG A NH1 1 ATOM 759 N NH2 . ARG A 1 95 ? 2.814 11.484 41.614 1.00 38.02 ? 109 ARG A NH2 1 ATOM 760 N N . ARG A 1 96 ? 3.713 7.864 35.434 1.00 29.00 ? 110 ARG A N 1 ATOM 761 C CA . ARG A 1 96 ? 2.605 7.743 34.491 1.00 31.09 ? 110 ARG A CA 1 ATOM 762 C C . ARG A 1 96 ? 3.152 8.122 33.122 1.00 29.59 ? 110 ARG A C 1 ATOM 763 O O . ARG A 1 96 ? 3.991 9.010 33.010 1.00 28.36 ? 110 ARG A O 1 ATOM 764 C CB . ARG A 1 96 ? 1.454 8.685 34.856 1.00 33.69 ? 110 ARG A CB 1 ATOM 765 C CG . ARG A 1 96 ? 0.893 8.469 36.243 1.00 39.55 ? 110 ARG A CG 1 ATOM 766 C CD . ARG A 1 96 ? -0.406 9.232 36.465 1.00 42.67 ? 110 ARG A CD 1 ATOM 767 N NE . ARG A 1 96 ? -0.278 10.673 36.253 1.00 46.33 ? 110 ARG A NE 1 ATOM 768 C CZ . ARG A 1 96 ? -0.449 11.283 35.084 1.00 46.34 ? 110 ARG A CZ 1 ATOM 769 N NH1 . ARG A 1 96 ? -0.757 10.581 34.000 1.00 47.55 ? 110 ARG A NH1 1 ATOM 770 N NH2 . ARG A 1 96 ? -0.325 12.601 35.001 1.00 46.49 ? 110 ARG A NH2 1 ATOM 771 N N . PRO A 1 97 ? 2.689 7.447 32.063 1.00 29.88 ? 111 PRO A N 1 ATOM 772 C CA . PRO A 1 97 ? 3.158 7.740 30.706 1.00 29.87 ? 111 PRO A CA 1 ATOM 773 C C . PRO A 1 97 ? 2.699 9.107 30.223 1.00 29.33 ? 111 PRO A C 1 ATOM 774 O O . PRO A 1 97 ? 1.820 9.730 30.818 1.00 29.29 ? 111 PRO A O 1 ATOM 775 C CB . PRO A 1 97 ? 2.533 6.623 29.869 1.00 31.00 ? 111 PRO A CB 1 ATOM 776 C CG . PRO A 1 97 ? 2.290 5.518 30.868 1.00 32.24 ? 111 PRO A CG 1 ATOM 777 C CD . PRO A 1 97 ? 1.804 6.272 32.069 1.00 31.03 ? 111 PRO A CD 1 ATOM 778 N N . VAL A 1 98 ? 3.316 9.574 29.146 1.00 28.84 ? 112 VAL A N 1 ATOM 779 C CA . VAL A 1 98 ? 2.926 10.836 28.541 1.00 28.34 ? 112 VAL A CA 1 ATOM 780 C C . VAL A 1 98 ? 2.405 10.457 27.163 1.00 29.05 ? 112 VAL A C 1 ATOM 781 O O . VAL A 1 98 ? 2.669 9.355 26.669 1.00 29.94 ? 112 VAL A O 1 ATOM 782 C CB . VAL A 1 98 ? 4.120 11.812 28.375 1.00 25.77 ? 112 VAL A CB 1 ATOM 783 C CG1 . VAL A 1 98 ? 4.652 12.218 29.738 1.00 27.70 ? 112 VAL A CG1 1 ATOM 784 C CG2 . VAL A 1 98 ? 5.217 11.165 27.534 1.00 24.56 ? 112 VAL A CG2 1 ATOM 785 N N . THR A 1 99 ? 1.646 11.356 26.554 1.00 29.02 ? 113 THR A N 1 ATOM 786 C CA . THR A 1 99 ? 1.118 11.119 25.218 1.00 27.98 ? 113 THR A CA 1 ATOM 787 C C . THR A 1 99 ? 1.928 12.020 24.296 1.00 26.36 ? 113 THR A C 1 ATOM 788 O O . THR A 1 99 ? 2.237 13.154 24.657 1.00 26.99 ? 113 THR A O 1 ATOM 789 C CB . THR A 1 99 ? -0.374 11.496 25.138 1.00 30.68 ? 113 THR A CB 1 ATOM 790 O OG1 . THR A 1 99 ? -1.142 10.563 25.914 1.00 33.61 ? 113 THR A OG1 1 ATOM 791 C CG2 . THR A 1 99 ? -0.857 11.469 23.703 1.00 32.65 ? 113 THR A CG2 1 ATOM 792 N N . TYR A 1 100 ? 2.284 11.520 23.120 1.00 24.85 ? 114 TYR A N 1 ATOM 793 C CA . TYR A 1 100 ? 3.074 12.306 22.182 1.00 24.48 ? 114 TYR A CA 1 ATOM 794 C C . TYR A 1 100 ? 2.275 13.467 21.601 1.00 24.40 ? 114 TYR A C 1 ATOM 795 O O . TYR A 1 100 ? 1.067 13.365 21.390 1.00 24.25 ? 114 TYR A O 1 ATOM 796 C CB . TYR A 1 100 ? 3.588 11.420 21.045 1.00 23.11 ? 114 TYR A CB 1 ATOM 797 C CG . TYR A 1 100 ? 4.530 10.318 21.477 1.00 23.34 ? 114 TYR A CG 1 ATOM 798 C CD1 . TYR A 1 100 ? 4.680 9.169 20.702 1.00 25.50 ? 114 TYR A CD1 1 ATOM 799 C CD2 . TYR A 1 100 ? 5.275 10.420 22.657 1.00 25.14 ? 114 TYR A CD2 1 ATOM 800 C CE1 . TYR A 1 100 ? 5.546 8.143 21.088 1.00 25.22 ? 114 TYR A CE1 1 ATOM 801 C CE2 . TYR A 1 100 ? 6.146 9.396 23.052 1.00 24.81 ? 114 TYR A CE2 1 ATOM 802 C CZ . TYR A 1 100 ? 6.273 8.262 22.259 1.00 26.66 ? 114 TYR A CZ 1 ATOM 803 O OH . TYR A 1 100 ? 7.124 7.245 22.631 1.00 25.91 ? 114 TYR A OH 1 ATOM 804 N N . SER A 1 101 ? 2.964 14.573 21.349 1.00 23.51 ? 115 SER A N 1 ATOM 805 C CA . SER A 1 101 ? 2.344 15.760 20.775 1.00 22.86 ? 115 SER A CA 1 ATOM 806 C C . SER A 1 101 ? 3.441 16.511 20.030 1.00 22.51 ? 115 SER A C 1 ATOM 807 O O . SER A 1 101 ? 4.560 16.016 19.918 1.00 22.02 ? 115 SER A O 1 ATOM 808 C CB . SER A 1 101 ? 1.738 16.635 21.876 1.00 23.05 ? 115 SER A CB 1 ATOM 809 O OG . SER A 1 101 ? 2.724 17.078 22.795 1.00 23.40 ? 115 SER A OG 1 ATOM 810 N N . THR A 1 102 ? 3.127 17.690 19.507 1.00 21.20 ? 116 THR A N 1 ATOM 811 C CA . THR A 1 102 ? 4.129 18.456 18.778 1.00 21.57 ? 116 THR A CA 1 ATOM 812 C C . THR A 1 102 ? 5.363 18.715 19.641 1.00 21.28 ? 116 THR A C 1 ATOM 813 O O . THR A 1 102 ? 6.490 18.609 19.166 1.00 21.07 ? 116 THR A O 1 ATOM 814 C CB . THR A 1 102 ? 3.574 19.823 18.314 1.00 24.01 ? 116 THR A CB 1 ATOM 815 O OG1 . THR A 1 102 ? 2.489 19.614 17.402 1.00 24.22 ? 116 THR A OG1 1 ATOM 816 C CG2 . THR A 1 102 ? 4.659 20.637 17.619 1.00 23.65 ? 116 THR A CG2 1 ATOM 817 N N . HIS A 1 103 ? 5.144 19.037 20.911 1.00 19.65 ? 117 HIS A N 1 ATOM 818 C CA . HIS A 1 103 ? 6.253 19.353 21.799 1.00 20.24 ? 117 HIS A CA 1 ATOM 819 C C . HIS A 1 103 ? 6.727 18.219 22.706 1.00 20.71 ? 117 HIS A C 1 ATOM 820 O O . HIS A 1 103 ? 7.633 18.412 23.522 1.00 19.07 ? 117 HIS A O 1 ATOM 821 C CB . HIS A 1 103 ? 5.887 20.586 22.623 1.00 20.15 ? 117 HIS A CB 1 ATOM 822 C CG . HIS A 1 103 ? 5.514 21.766 21.783 1.00 21.49 ? 117 HIS A CG 1 ATOM 823 N ND1 . HIS A 1 103 ? 4.402 22.539 22.035 1.00 23.27 ? 117 HIS A ND1 1 ATOM 824 C CD2 . HIS A 1 103 ? 6.095 22.290 20.678 1.00 24.08 ? 117 HIS A CD2 1 ATOM 825 C CE1 . HIS A 1 103 ? 4.313 23.489 21.120 1.00 23.74 ? 117 HIS A CE1 1 ATOM 826 N NE2 . HIS A 1 103 ? 5.328 23.361 20.285 1.00 23.03 ? 117 HIS A NE2 1 ATOM 827 N N . ILE A 1 104 ? 6.113 17.047 22.573 1.00 20.28 ? 118 ILE A N 1 ATOM 828 C CA . ILE A 1 104 ? 6.525 15.883 23.358 1.00 21.04 ? 118 ILE A CA 1 ATOM 829 C C . ILE A 1 104 ? 6.629 14.682 22.416 1.00 22.24 ? 118 ILE A C 1 ATOM 830 O O . ILE A 1 104 ? 5.620 14.124 21.974 1.00 23.65 ? 118 ILE A O 1 ATOM 831 C CB . ILE A 1 104 ? 5.526 15.557 24.501 1.00 21.79 ? 118 ILE A CB 1 ATOM 832 C CG1 . ILE A 1 104 ? 5.491 16.710 25.508 1.00 20.92 ? 118 ILE A CG1 1 ATOM 833 C CG2 . ILE A 1 104 ? 5.951 14.268 25.208 1.00 22.39 ? 118 ILE A CG2 1 ATOM 834 C CD1 . ILE A 1 104 ? 4.563 16.489 26.687 1.00 20.95 ? 118 ILE A CD1 1 ATOM 835 N N . ALA A 1 105 ? 7.858 14.295 22.100 1.00 22.26 ? 119 ALA A N 1 ATOM 836 C CA . ALA A 1 105 ? 8.099 13.177 21.196 1.00 23.41 ? 119 ALA A CA 1 ATOM 837 C C . ALA A 1 105 ? 9.393 12.463 21.565 1.00 22.72 ? 119 ALA A C 1 ATOM 838 O O . ALA A 1 105 ? 10.292 13.057 22.155 1.00 23.63 ? 119 ALA A O 1 ATOM 839 C CB . ALA A 1 105 ? 8.166 13.677 19.765 1.00 23.41 ? 119 ALA A CB 1 ATOM 840 N N . PRO A 1 106 ? 9.509 11.177 21.203 1.00 24.48 ? 120 PRO A N 1 ATOM 841 C CA . PRO A 1 106 ? 10.706 10.395 21.515 1.00 24.04 ? 120 PRO A CA 1 ATOM 842 C C . PRO A 1 106 ? 11.894 10.675 20.601 1.00 24.78 ? 120 PRO A C 1 ATOM 843 O O . PRO A 1 106 ? 11.728 10.999 19.428 1.00 22.62 ? 120 PRO A O 1 ATOM 844 C CB . PRO A 1 106 ? 10.211 8.963 21.376 1.00 24.64 ? 120 PRO A CB 1 ATOM 845 C CG . PRO A 1 106 ? 9.297 9.068 20.190 1.00 25.89 ? 120 PRO A CG 1 ATOM 846 C CD . PRO A 1 106 ? 8.521 10.355 20.475 1.00 24.05 ? 120 PRO A CD 1 ATOM 847 N N . VAL A 1 107 ? 13.097 10.549 21.146 1.00 23.48 ? 121 VAL A N 1 ATOM 848 C CA . VAL A 1 107 ? 14.287 10.755 20.339 1.00 24.35 ? 121 VAL A CA 1 ATOM 849 C C . VAL A 1 107 ? 14.656 9.369 19.843 1.00 24.75 ? 121 VAL A C 1 ATOM 850 O O . VAL A 1 107 ? 14.336 8.374 20.487 1.00 26.52 ? 121 VAL A O 1 ATOM 851 C CB . VAL A 1 107 ? 15.466 11.327 21.166 1.00 25.67 ? 121 VAL A CB 1 ATOM 852 C CG1 . VAL A 1 107 ? 16.039 10.260 22.073 1.00 27.69 ? 121 VAL A CG1 1 ATOM 853 C CG2 . VAL A 1 107 ? 16.543 11.849 20.235 1.00 26.19 ? 121 VAL A CG2 1 ATOM 854 N N . SER A 1 108 ? 15.314 9.285 18.699 1.00 25.34 ? 122 SER A N 1 ATOM 855 C CA . SER A 1 108 ? 15.700 7.980 18.189 1.00 28.93 ? 122 SER A CA 1 ATOM 856 C C . SER A 1 108 ? 17.096 7.620 18.694 1.00 28.03 ? 122 SER A C 1 ATOM 857 O O . SER A 1 108 ? 17.980 8.472 18.762 1.00 27.74 ? 122 SER A O 1 ATOM 858 C CB . SER A 1 108 ? 15.675 7.979 16.661 1.00 30.66 ? 122 SER A CB 1 ATOM 859 O OG . SER A 1 108 ? 16.543 8.967 16.141 1.00 38.56 ? 122 SER A OG 1 ATOM 860 N N . LEU A 1 109 ? 17.276 6.363 19.079 1.00 28.61 ? 123 LEU A N 1 ATOM 861 C CA . LEU A 1 109 ? 18.568 5.897 19.552 1.00 29.67 ? 123 LEU A CA 1 ATOM 862 C C . LEU A 1 109 ? 19.460 5.739 18.328 1.00 30.58 ? 123 LEU A C 1 ATOM 863 O O . LEU A 1 109 ? 18.969 5.584 17.209 1.00 30.67 ? 123 LEU A O 1 ATOM 864 C CB . LEU A 1 109 ? 18.422 4.558 20.282 1.00 31.19 ? 123 LEU A CB 1 ATOM 865 C CG . LEU A 1 109 ? 17.758 4.615 21.666 1.00 32.43 ? 123 LEU A CG 1 ATOM 866 C CD1 . LEU A 1 109 ? 17.528 3.207 22.198 1.00 31.99 ? 123 LEU A CD1 1 ATOM 867 C CD2 . LEU A 1 109 ? 18.641 5.411 22.619 1.00 31.81 ? 123 LEU A CD2 1 ATOM 868 N N . PRO A 1 110 ? 20.785 5.784 18.522 1.00 30.66 ? 124 PRO A N 1 ATOM 869 C CA . PRO A 1 110 ? 21.718 5.645 17.401 1.00 31.75 ? 124 PRO A CA 1 ATOM 870 C C . PRO A 1 110 ? 21.662 4.263 16.754 1.00 32.16 ? 124 PRO A C 1 ATOM 871 O O . PRO A 1 110 ? 21.633 3.243 17.441 1.00 31.28 ? 124 PRO A O 1 ATOM 872 C CB . PRO A 1 110 ? 23.069 5.954 18.043 1.00 32.42 ? 124 PRO A CB 1 ATOM 873 C CG . PRO A 1 110 ? 22.899 5.446 19.438 1.00 31.68 ? 124 PRO A CG 1 ATOM 874 C CD . PRO A 1 110 ? 21.507 5.914 19.801 1.00 30.69 ? 124 PRO A CD 1 ATOM 875 N N . SER A 1 111 ? 21.628 4.242 15.426 1.00 33.82 ? 125 SER A N 1 ATOM 876 C CA . SER A 1 111 ? 21.567 2.988 14.684 1.00 35.64 ? 125 SER A CA 1 ATOM 877 C C . SER A 1 111 ? 22.968 2.475 14.373 1.00 37.31 ? 125 SER A C 1 ATOM 878 O O . SER A 1 111 ? 23.154 1.304 14.044 1.00 37.66 ? 125 SER A O 1 ATOM 879 C CB . SER A 1 111 ? 20.767 3.180 13.389 1.00 35.11 ? 125 SER A CB 1 ATOM 880 O OG . SER A 1 111 ? 21.225 4.304 12.657 1.00 35.35 ? 125 SER A OG 1 ATOM 881 N N . ARG A 1 112 ? 23.952 3.360 14.490 1.00 38.22 ? 127 ARG A N 1 ATOM 882 C CA . ARG A 1 112 ? 25.343 3.009 14.238 1.00 40.05 ? 127 ARG A CA 1 ATOM 883 C C . ARG A 1 112 ? 26.268 3.996 14.938 1.00 40.43 ? 127 ARG A C 1 ATOM 884 O O . ARG A 1 112 ? 25.872 5.119 15.248 1.00 41.47 ? 127 ARG A O 1 ATOM 885 C CB . ARG A 1 112 ? 25.627 3.011 12.734 1.00 42.45 ? 127 ARG A CB 1 ATOM 886 C CG . ARG A 1 112 ? 25.085 4.226 12.002 1.00 46.38 ? 127 ARG A CG 1 ATOM 887 C CD . ARG A 1 112 ? 25.517 4.227 10.542 1.00 50.33 ? 127 ARG A CD 1 ATOM 888 N NE . ARG A 1 112 ? 26.941 4.518 10.394 1.00 53.34 ? 127 ARG A NE 1 ATOM 889 C CZ . ARG A 1 112 ? 27.494 5.696 10.669 1.00 55.26 ? 127 ARG A CZ 1 ATOM 890 N NH1 . ARG A 1 112 ? 28.799 5.877 10.509 1.00 55.18 ? 127 ARG A NH1 1 ATOM 891 N NH2 . ARG A 1 112 ? 26.739 6.697 11.101 1.00 56.83 ? 127 ARG A NH2 1 ATOM 892 N N . SER A 1 113 ? 27.501 3.572 15.184 1.00 39.91 ? 128 SER A N 1 ATOM 893 C CA . SER A 1 113 ? 28.482 4.417 15.849 1.00 40.06 ? 128 SER A CA 1 ATOM 894 C C . SER A 1 113 ? 28.973 5.547 14.945 1.00 40.07 ? 128 SER A C 1 ATOM 895 O O . SER A 1 113 ? 29.155 5.359 13.742 1.00 40.05 ? 128 SER A O 1 ATOM 896 C CB . SER A 1 113 ? 29.678 3.571 16.300 1.00 39.32 ? 128 SER A CB 1 ATOM 897 O OG . SER A 1 113 ? 30.703 4.382 16.843 1.00 38.42 ? 128 SER A OG 1 ATOM 898 N N . ARG A 1 114 ? 29.165 6.720 15.538 1.00 39.43 ? 129 ARG A N 1 ATOM 899 C CA . ARG A 1 114 ? 29.668 7.893 14.830 1.00 39.08 ? 129 ARG A CA 1 ATOM 900 C C . ARG A 1 114 ? 30.869 8.389 15.619 1.00 38.40 ? 129 ARG A C 1 ATOM 901 O O . ARG A 1 114 ? 30.852 8.369 16.850 1.00 38.45 ? 129 ARG A O 1 ATOM 902 C CB . ARG A 1 114 ? 28.605 8.990 14.755 1.00 41.19 ? 129 ARG A CB 1 ATOM 903 C CG . ARG A 1 114 ? 27.670 8.872 13.560 1.00 44.33 ? 129 ARG A CG 1 ATOM 904 C CD . ARG A 1 114 ? 26.717 10.057 13.495 1.00 47.01 ? 129 ARG A CD 1 ATOM 905 N NE . ARG A 1 114 ? 25.883 10.026 12.297 1.00 50.65 ? 129 ARG A NE 1 ATOM 906 C CZ . ARG A 1 114 ? 26.328 10.255 11.065 1.00 52.10 ? 129 ARG A CZ 1 ATOM 907 N NH1 . ARG A 1 114 ? 27.608 10.540 10.857 1.00 53.05 ? 129 ARG A NH1 1 ATOM 908 N NH2 . ARG A 1 114 ? 25.492 10.192 10.038 1.00 52.34 ? 129 ARG A NH2 1 ATOM 909 N N . GLY A 1 115 ? 31.908 8.835 14.920 1.00 36.44 ? 131 GLY A N 1 ATOM 910 C CA . GLY A 1 115 ? 33.102 9.291 15.609 1.00 35.73 ? 131 GLY A CA 1 ATOM 911 C C . GLY A 1 115 ? 33.651 10.665 15.266 1.00 34.62 ? 131 GLY A C 1 ATOM 912 O O . GLY A 1 115 ? 32.921 11.570 14.862 1.00 33.41 ? 131 GLY A O 1 ATOM 913 N N . VAL A 1 116 ? 34.962 10.804 15.443 1.00 33.86 ? 132 VAL A N 1 ATOM 914 C CA . VAL A 1 116 ? 35.679 12.048 15.198 1.00 34.32 ? 132 VAL A CA 1 ATOM 915 C C . VAL A 1 116 ? 35.299 12.721 13.883 1.00 34.91 ? 132 VAL A C 1 ATOM 916 O O . VAL A 1 116 ? 35.312 12.095 12.825 1.00 34.68 ? 132 VAL A O 1 ATOM 917 C CB . VAL A 1 116 ? 37.205 11.807 15.218 1.00 34.81 ? 132 VAL A CB 1 ATOM 918 C CG1 . VAL A 1 116 ? 37.945 13.116 15.000 1.00 34.60 ? 132 VAL A CG1 1 ATOM 919 C CG2 . VAL A 1 116 ? 37.610 11.183 16.548 1.00 34.49 ? 132 VAL A CG2 1 ATOM 920 N N . GLY A 1 117 ? 34.965 14.006 13.966 1.00 34.94 ? 133 GLY A N 1 ATOM 921 C CA . GLY A 1 117 ? 34.579 14.751 12.783 1.00 34.76 ? 133 GLY A CA 1 ATOM 922 C C . GLY A 1 117 ? 33.080 14.956 12.679 1.00 34.36 ? 133 GLY A C 1 ATOM 923 O O . GLY A 1 117 ? 32.624 15.961 12.127 1.00 34.95 ? 133 GLY A O 1 ATOM 924 N N . SER A 1 118 ? 32.309 14.008 13.207 1.00 33.19 ? 134 SER A N 1 ATOM 925 C CA . SER A 1 118 ? 30.852 14.094 13.166 1.00 32.19 ? 134 SER A CA 1 ATOM 926 C C . SER A 1 118 ? 30.380 15.434 13.717 1.00 30.91 ? 134 SER A C 1 ATOM 927 O O . SER A 1 118 ? 30.850 15.880 14.764 1.00 31.07 ? 134 SER A O 1 ATOM 928 C CB . SER A 1 118 ? 30.220 12.969 13.996 1.00 32.57 ? 134 SER A CB 1 ATOM 929 O OG . SER A 1 118 ? 30.563 11.688 13.506 1.00 33.95 ? 134 SER A OG 1 ATOM 930 N N . ARG A 1 119 ? 29.463 16.086 13.006 1.00 29.90 ? 135 ARG A N 1 ATOM 931 C CA . ARG A 1 119 ? 28.924 17.358 13.472 1.00 29.91 ? 135 ARG A CA 1 ATOM 932 C C . ARG A 1 119 ? 27.646 17.034 14.240 1.00 28.77 ? 135 ARG A C 1 ATOM 933 O O . ARG A 1 119 ? 26.762 16.341 13.728 1.00 29.28 ? 135 ARG A O 1 ATOM 934 C CB . ARG A 1 119 ? 28.606 18.290 12.298 1.00 32.88 ? 135 ARG A CB 1 ATOM 935 C CG . ARG A 1 119 ? 28.229 19.697 12.736 1.00 37.46 ? 135 ARG A CG 1 ATOM 936 C CD . ARG A 1 119 ? 27.920 20.620 11.557 1.00 41.71 ? 135 ARG A CD 1 ATOM 937 N NE . ARG A 1 119 ? 26.735 20.201 10.810 1.00 45.32 ? 135 ARG A NE 1 ATOM 938 C CZ . ARG A 1 119 ? 26.735 19.294 9.837 1.00 47.27 ? 135 ARG A CZ 1 ATOM 939 N NH1 . ARG A 1 119 ? 27.865 18.698 9.474 1.00 48.15 ? 135 ARG A NH1 1 ATOM 940 N NH2 . ARG A 1 119 ? 25.599 18.975 9.228 1.00 48.14 ? 135 ARG A NH2 1 ATOM 941 N N . CYS A 1 120 ? 27.553 17.528 15.469 1.00 27.37 ? 136 CYS A N 1 ATOM 942 C CA . CYS A 1 120 ? 26.386 17.260 16.301 1.00 26.56 ? 136 CYS A CA 1 ATOM 943 C C . CYS A 1 120 ? 25.811 18.525 16.918 1.00 25.51 ? 136 CYS A C 1 ATOM 944 O O . CYS A 1 120 ? 26.398 19.600 16.831 1.00 26.04 ? 136 CYS A O 1 ATOM 945 C CB . CYS A 1 120 ? 26.754 16.289 17.421 1.00 26.23 ? 136 CYS A CB 1 ATOM 946 S SG . CYS A 1 120 ? 27.601 14.772 16.882 1.00 27.41 ? 136 CYS A SG 1 ATOM 947 N N . ARG A 1 121 ? 24.663 18.381 17.571 1.00 25.97 ? 137 ARG A N 1 ATOM 948 C CA . ARG A 1 121 ? 24.004 19.520 18.181 1.00 23.96 ? 137 ARG A CA 1 ATOM 949 C C . ARG A 1 121 ? 23.730 19.305 19.664 1.00 22.74 ? 137 ARG A C 1 ATOM 950 O O . ARG A 1 121 ? 23.352 18.210 20.083 1.00 22.36 ? 137 ARG A O 1 ATOM 951 C CB . ARG A 1 121 ? 22.694 19.783 17.448 1.00 25.40 ? 137 ARG A CB 1 ATOM 952 C CG . ARG A 1 121 ? 22.065 21.144 17.712 1.00 25.71 ? 137 ARG A CG 1 ATOM 953 C CD . ARG A 1 121 ? 21.066 21.419 16.602 1.00 25.38 ? 137 ARG A CD 1 ATOM 954 N NE . ARG A 1 121 ? 20.273 22.630 16.784 1.00 24.21 ? 137 ARG A NE 1 ATOM 955 C CZ . ARG A 1 121 ? 20.696 23.868 16.546 1.00 26.06 ? 137 ARG A CZ 1 ATOM 956 N NH1 . ARG A 1 121 ? 21.933 24.092 16.116 1.00 22.83 ? 137 ARG A NH1 1 ATOM 957 N NH2 . ARG A 1 121 ? 19.857 24.883 16.701 1.00 21.97 ? 137 ARG A NH2 1 ATOM 958 N N . ILE A 1 122 ? 23.943 20.353 20.452 1.00 20.71 ? 138 ILE A N 1 ATOM 959 C CA . ILE A 1 122 ? 23.682 20.291 21.881 1.00 20.28 ? 138 ILE A CA 1 ATOM 960 C C . ILE A 1 122 ? 22.586 21.296 22.199 1.00 20.17 ? 138 ILE A C 1 ATOM 961 O O . ILE A 1 122 ? 22.392 22.268 21.470 1.00 19.76 ? 138 ILE A O 1 ATOM 962 C CB . ILE A 1 122 ? 24.951 20.580 22.725 1.00 20.64 ? 138 ILE A CB 1 ATOM 963 C CG1 . ILE A 1 122 ? 25.577 21.918 22.318 1.00 22.31 ? 138 ILE A CG1 1 ATOM 964 C CG2 . ILE A 1 122 ? 25.938 19.437 22.560 1.00 17.25 ? 138 ILE A CG2 1 ATOM 965 C CD1 . ILE A 1 122 ? 26.726 22.351 23.228 1.00 23.34 ? 138 ILE A CD1 1 ATOM 966 N N . MET A 1 123 ? 21.872 21.055 23.290 1.00 19.58 ? 139 MET A N 1 ATOM 967 C CA . MET A 1 123 ? 20.752 21.896 23.681 1.00 19.05 ? 139 MET A CA 1 ATOM 968 C C . MET A 1 123 ? 20.478 21.774 25.173 1.00 19.85 ? 139 MET A C 1 ATOM 969 O O . MET A 1 123 ? 20.724 20.726 25.765 1.00 19.86 ? 139 MET A O 1 ATOM 970 C CB . MET A 1 123 ? 19.516 21.435 22.917 1.00 20.28 ? 139 MET A CB 1 ATOM 971 C CG . MET A 1 123 ? 19.283 19.938 23.068 1.00 23.55 ? 139 MET A CG 1 ATOM 972 S SD . MET A 1 123 ? 17.934 19.284 22.079 1.00 25.21 ? 139 MET A SD 1 ATOM 973 C CE . MET A 1 123 ? 18.703 19.195 20.488 1.00 25.18 ? 139 MET A CE 1 ATOM 974 N N . GLY A 1 124 ? 19.953 22.839 25.769 1.00 19.55 ? 140 GLY A N 1 ATOM 975 C CA . GLY A 1 124 ? 19.640 22.806 27.186 1.00 18.88 ? 140 GLY A CA 1 ATOM 976 C C . GLY A 1 124 ? 19.273 24.164 27.743 1.00 20.22 ? 140 GLY A C 1 ATOM 977 O O . GLY A 1 124 ? 19.324 25.171 27.033 1.00 21.66 ? 140 GLY A O 1 ATOM 978 N N . TRP A 1 125 ? 18.897 24.187 29.019 1.00 19.37 ? 141 TRP A N 1 ATOM 979 C CA . TRP A 1 125 ? 18.531 25.417 29.705 1.00 19.31 ? 141 TRP A CA 1 ATOM 980 C C . TRP A 1 125 ? 19.676 25.847 30.624 1.00 20.78 ? 141 TRP A C 1 ATOM 981 O O . TRP A 1 125 ? 19.480 26.659 31.533 1.00 20.56 ? 141 TRP A O 1 ATOM 982 C CB . TRP A 1 125 ? 17.265 25.203 30.540 1.00 18.96 ? 141 TRP A CB 1 ATOM 983 C CG . TRP A 1 125 ? 16.016 24.976 29.730 1.00 19.41 ? 141 TRP A CG 1 ATOM 984 C CD1 . TRP A 1 125 ? 15.187 25.931 29.216 1.00 21.01 ? 141 TRP A CD1 1 ATOM 985 C CD2 . TRP A 1 125 ? 15.450 23.714 29.364 1.00 20.94 ? 141 TRP A CD2 1 ATOM 986 N NE1 . TRP A 1 125 ? 14.134 25.342 28.556 1.00 21.18 ? 141 TRP A NE1 1 ATOM 987 C CE2 . TRP A 1 125 ? 14.270 23.982 28.630 1.00 21.36 ? 141 TRP A CE2 1 ATOM 988 C CE3 . TRP A 1 125 ? 15.822 22.381 29.583 1.00 21.63 ? 141 TRP A CE3 1 ATOM 989 C CZ2 . TRP A 1 125 ? 13.458 22.965 28.118 1.00 19.96 ? 141 TRP A CZ2 1 ATOM 990 C CZ3 . TRP A 1 125 ? 15.012 21.366 29.072 1.00 22.82 ? 141 TRP A CZ3 1 ATOM 991 C CH2 . TRP A 1 125 ? 13.843 21.667 28.348 1.00 19.52 ? 141 TRP A CH2 1 ATOM 992 N N . GLY A 1 126 ? 20.863 25.299 30.385 1.00 20.89 ? 142 GLY A N 1 ATOM 993 C CA . GLY A 1 126 ? 22.017 25.642 31.206 1.00 22.69 ? 142 GLY A CA 1 ATOM 994 C C . GLY A 1 126 ? 22.500 27.062 30.956 1.00 24.10 ? 142 GLY A C 1 ATOM 995 O O . GLY A 1 126 ? 21.970 27.764 30.090 1.00 22.61 ? 142 GLY A O 1 ATOM 996 N N . LYS A 1 127 ? 23.511 27.489 31.707 1.00 25.17 ? 143 LYS A N 1 ATOM 997 C CA . LYS A 1 127 ? 24.050 28.843 31.564 1.00 26.45 ? 143 LYS A CA 1 ATOM 998 C C . LYS A 1 127 ? 24.464 29.220 30.143 1.00 25.83 ? 143 LYS A C 1 ATOM 999 O O . LYS A 1 127 ? 25.053 28.419 29.419 1.00 24.20 ? 143 LYS A O 1 ATOM 1000 C CB . LYS A 1 127 ? 25.256 29.034 32.489 1.00 29.17 ? 143 LYS A CB 1 ATOM 1001 C CG . LYS A 1 127 ? 24.920 29.052 33.968 1.00 33.25 ? 143 LYS A CG 1 ATOM 1002 C CD . LYS A 1 127 ? 26.155 29.383 34.796 1.00 37.40 ? 143 LYS A CD 1 ATOM 1003 C CE . LYS A 1 127 ? 25.821 29.498 36.276 1.00 39.84 ? 143 LYS A CE 1 ATOM 1004 N NZ . LYS A 1 127 ? 27.010 29.874 37.092 1.00 42.79 ? 143 LYS A NZ 1 ATOM 1005 N N . ILE A 1 128 ? 24.158 30.456 29.757 1.00 26.87 ? 144 ILE A N 1 ATOM 1006 C CA . ILE A 1 128 ? 24.520 30.960 28.435 1.00 29.87 ? 144 ILE A CA 1 ATOM 1007 C C . ILE A 1 128 ? 25.666 31.968 28.555 1.00 32.42 ? 144 ILE A C 1 ATOM 1008 O O . ILE A 1 128 ? 26.175 32.467 27.552 1.00 32.91 ? 144 ILE A O 1 ATOM 1009 C CB . ILE A 1 128 ? 23.318 31.635 27.729 1.00 29.33 ? 144 ILE A CB 1 ATOM 1010 C CG1 . ILE A 1 128 ? 22.731 32.730 28.624 1.00 29.73 ? 144 ILE A CG1 1 ATOM 1011 C CG2 . ILE A 1 128 ? 22.266 30.583 27.373 1.00 27.02 ? 144 ILE A CG2 1 ATOM 1012 C CD1 . ILE A 1 128 ? 21.563 33.488 27.992 1.00 31.53 ? 144 ILE A CD1 1 ATOM 1013 N N . SER A 1 129 ? 26.049 32.267 29.793 1.00 34.90 ? 145 SER A N 1 ATOM 1014 C CA . SER A 1 129 ? 27.153 33.178 30.089 1.00 38.83 ? 145 SER A CA 1 ATOM 1015 C C . SER A 1 129 ? 27.684 32.805 31.474 1.00 40.40 ? 145 SER A C 1 ATOM 1016 O O . SER A 1 129 ? 27.175 31.875 32.098 1.00 40.96 ? 145 SER A O 1 ATOM 1017 C CB . SER A 1 129 ? 26.692 34.641 30.065 1.00 39.15 ? 145 SER A CB 1 ATOM 1018 O OG . SER A 1 129 ? 25.823 34.931 31.142 1.00 43.33 ? 145 SER A OG 1 ATOM 1019 N N . THR A 1 130 ? 28.694 33.524 31.956 1.00 42.20 ? 146 THR A N 1 ATOM 1020 C CA . THR A 1 130 ? 29.292 33.226 33.258 1.00 43.89 ? 146 THR A CA 1 ATOM 1021 C C . THR A 1 130 ? 28.279 33.010 34.380 1.00 44.18 ? 146 THR A C 1 ATOM 1022 O O . THR A 1 130 ? 28.360 32.023 35.111 1.00 45.17 ? 146 THR A O 1 ATOM 1023 C CB . THR A 1 130 ? 30.268 34.339 33.705 1.00 45.08 ? 146 THR A CB 1 ATOM 1024 O OG1 . THR A 1 130 ? 29.529 35.499 34.107 1.00 47.31 ? 146 THR A OG1 1 ATOM 1025 C CG2 . THR A 1 130 ? 31.203 34.710 32.568 1.00 44.72 ? 146 THR A CG2 1 ATOM 1026 N N . THR A 1 131 ? 27.331 33.932 34.521 1.00 43.78 ? 147 THR A N 1 ATOM 1027 C CA . THR A 1 131 ? 26.320 33.816 35.568 1.00 43.97 ? 147 THR A CA 1 ATOM 1028 C C . THR A 1 131 ? 24.920 34.163 35.071 1.00 42.84 ? 147 THR A C 1 ATOM 1029 O O . THR A 1 131 ? 24.206 34.944 35.703 1.00 43.89 ? 147 THR A O 1 ATOM 1030 C CB . THR A 1 131 ? 26.650 34.733 36.775 1.00 45.69 ? 147 THR A CB 1 ATOM 1031 O OG1 . THR A 1 131 ? 26.876 36.071 36.313 1.00 47.32 ? 147 THR A OG1 1 ATOM 1032 C CG2 . THR A 1 131 ? 27.893 34.235 37.511 1.00 46.66 ? 147 THR A CG2 1 ATOM 1033 N N . THR A 1 132 ? 24.520 33.578 33.946 1.00 40.72 ? 148 THR A N 1 ATOM 1034 C CA . THR A 1 132 ? 23.197 33.852 33.393 1.00 37.93 ? 148 THR A CA 1 ATOM 1035 C C . THR A 1 132 ? 22.506 32.612 32.832 1.00 34.97 ? 148 THR A C 1 ATOM 1036 O O . THR A 1 132 ? 23.090 31.866 32.049 1.00 34.27 ? 148 THR A O 1 ATOM 1037 C CB . THR A 1 132 ? 23.269 34.901 32.256 1.00 39.98 ? 148 THR A CB 1 ATOM 1038 O OG1 . THR A 1 132 ? 23.833 36.120 32.755 1.00 40.94 ? 148 THR A OG1 1 ATOM 1039 C CG2 . THR A 1 132 ? 21.880 35.179 31.696 1.00 39.18 ? 148 THR A CG2 1 ATOM 1040 N N . TYR A 1 133 ? 21.259 32.401 33.241 1.00 32.81 ? 149 TYR A N 1 ATOM 1041 C CA . TYR A 1 133 ? 20.471 31.278 32.751 1.00 30.49 ? 149 TYR A CA 1 ATOM 1042 C C . TYR A 1 133 ? 19.409 31.824 31.800 1.00 27.40 ? 149 TYR A C 1 ATOM 1043 O O . TYR A 1 133 ? 18.824 32.874 32.051 1.00 27.03 ? 149 TYR A O 1 ATOM 1044 C CB . TYR A 1 133 ? 19.812 30.527 33.911 1.00 32.76 ? 149 TYR A CB 1 ATOM 1045 C CG . TYR A 1 133 ? 20.787 29.705 34.732 1.00 36.76 ? 149 TYR A CG 1 ATOM 1046 C CD1 . TYR A 1 133 ? 21.535 30.287 35.755 1.00 38.82 ? 149 TYR A CD1 1 ATOM 1047 C CD2 . TYR A 1 133 ? 20.980 28.348 34.465 1.00 37.25 ? 149 TYR A CD2 1 ATOM 1048 C CE1 . TYR A 1 133 ? 22.454 29.536 36.495 1.00 39.89 ? 149 TYR A CE1 1 ATOM 1049 C CE2 . TYR A 1 133 ? 21.896 27.589 35.195 1.00 38.72 ? 149 TYR A CE2 1 ATOM 1050 C CZ . TYR A 1 133 ? 22.628 28.189 36.209 1.00 40.40 ? 149 TYR A CZ 1 ATOM 1051 O OH . TYR A 1 133 ? 23.532 27.444 36.938 1.00 42.09 ? 149 TYR A OH 1 ATOM 1052 N N . PRO A 1 134 ? 19.155 31.119 30.689 1.00 24.59 ? 152 PRO A N 1 ATOM 1053 C CA . PRO A 1 134 ? 18.162 31.542 29.695 1.00 23.18 ? 152 PRO A CA 1 ATOM 1054 C C . PRO A 1 134 ? 16.723 31.207 30.068 1.00 24.20 ? 152 PRO A C 1 ATOM 1055 O O . PRO A 1 134 ? 16.476 30.327 30.892 1.00 25.35 ? 152 PRO A O 1 ATOM 1056 C CB . PRO A 1 134 ? 18.609 30.796 28.446 1.00 22.03 ? 152 PRO A CB 1 ATOM 1057 C CG . PRO A 1 134 ? 19.033 29.468 29.028 1.00 21.75 ? 152 PRO A CG 1 ATOM 1058 C CD . PRO A 1 134 ? 19.856 29.899 30.241 1.00 22.07 ? 152 PRO A CD 1 ATOM 1059 N N . ASP A 1 135 ? 15.772 31.908 29.456 1.00 22.91 ? 153 ASP A N 1 ATOM 1060 C CA . ASP A 1 135 ? 14.361 31.649 29.713 1.00 25.14 ? 153 ASP A CA 1 ATOM 1061 C C . ASP A 1 135 ? 13.859 30.599 28.721 1.00 24.11 ? 153 ASP A C 1 ATOM 1062 O O . ASP A 1 135 ? 12.782 30.033 28.887 1.00 25.19 ? 153 ASP A O 1 ATOM 1063 C CB . ASP A 1 135 ? 13.533 32.928 29.570 1.00 29.31 ? 153 ASP A CB 1 ATOM 1064 C CG . ASP A 1 135 ? 13.837 33.943 30.651 1.00 31.94 ? 153 ASP A CG 1 ATOM 1065 O OD1 . ASP A 1 135 ? 13.925 33.550 31.834 1.00 34.55 ? 153 ASP A OD1 1 ATOM 1066 O OD2 . ASP A 1 135 ? 13.976 35.138 30.316 1.00 36.84 ? 153 ASP A OD2 1 ATOM 1067 N N . VAL A 1 136 ? 14.659 30.352 27.691 1.00 22.05 ? 154 VAL A N 1 ATOM 1068 C CA . VAL A 1 136 ? 14.345 29.363 26.666 1.00 20.62 ? 154 VAL A CA 1 ATOM 1069 C C . VAL A 1 136 ? 15.596 28.524 26.451 1.00 20.89 ? 154 VAL A C 1 ATOM 1070 O O . VAL A 1 136 ? 16.704 28.963 26.763 1.00 20.43 ? 154 VAL A O 1 ATOM 1071 C CB . VAL A 1 136 ? 13.961 30.037 25.325 1.00 22.21 ? 154 VAL A CB 1 ATOM 1072 C CG1 . VAL A 1 136 ? 12.663 30.818 25.492 1.00 19.99 ? 154 VAL A CG1 1 ATOM 1073 C CG2 . VAL A 1 136 ? 15.090 30.969 24.869 1.00 21.37 ? 154 VAL A CG2 1 ATOM 1074 N N . PRO A 1 137 ? 15.440 27.302 25.924 1.00 20.22 ? 155 PRO A N 1 ATOM 1075 C CA . PRO A 1 137 ? 16.626 26.478 25.708 1.00 21.12 ? 155 PRO A CA 1 ATOM 1076 C C . PRO A 1 137 ? 17.480 27.006 24.559 1.00 21.46 ? 155 PRO A C 1 ATOM 1077 O O . PRO A 1 137 ? 16.957 27.515 23.559 1.00 21.34 ? 155 PRO A O 1 ATOM 1078 C CB . PRO A 1 137 ? 16.038 25.097 25.422 1.00 21.03 ? 155 PRO A CB 1 ATOM 1079 C CG . PRO A 1 137 ? 14.759 25.434 24.694 1.00 20.83 ? 155 PRO A CG 1 ATOM 1080 C CD . PRO A 1 137 ? 14.213 26.602 25.492 1.00 20.99 ? 155 PRO A CD 1 ATOM 1081 N N . HIS A 1 138 ? 18.795 26.919 24.721 1.00 19.65 ? 156 HIS A N 1 ATOM 1082 C CA . HIS A 1 138 ? 19.712 27.358 23.681 1.00 21.07 ? 156 HIS A CA 1 ATOM 1083 C C . HIS A 1 138 ? 20.358 26.163 23.008 1.00 21.18 ? 156 HIS A C 1 ATOM 1084 O O . HIS A 1 138 ? 20.579 25.118 23.632 1.00 20.40 ? 156 HIS A O 1 ATOM 1085 C CB . HIS A 1 138 ? 20.785 28.298 24.242 1.00 20.58 ? 156 HIS A CB 1 ATOM 1086 C CG . HIS A 1 138 ? 20.299 29.700 24.445 1.00 21.91 ? 156 HIS A CG 1 ATOM 1087 N ND1 . HIS A 1 138 ? 21.043 30.807 24.089 1.00 23.14 ? 156 HIS A ND1 1 ATOM 1088 C CD2 . HIS A 1 138 ? 19.141 30.175 24.959 1.00 21.02 ? 156 HIS A CD2 1 ATOM 1089 C CE1 . HIS A 1 138 ? 20.360 31.902 24.372 1.00 23.33 ? 156 HIS A CE1 1 ATOM 1090 N NE2 . HIS A 1 138 ? 19.203 31.546 24.901 1.00 23.46 ? 156 HIS A NE2 1 ATOM 1091 N N . CYS A 1 139 ? 20.667 26.341 21.728 1.00 21.40 ? 157 CYS A N 1 ATOM 1092 C CA . CYS A 1 139 ? 21.253 25.302 20.897 1.00 20.93 ? 157 CYS A CA 1 ATOM 1093 C C . CYS A 1 139 ? 22.481 25.800 20.139 1.00 22.55 ? 157 CYS A C 1 ATOM 1094 O O . CYS A 1 139 ? 22.649 26.999 19.923 1.00 22.37 ? 157 CYS A O 1 ATOM 1095 C CB . CYS A 1 139 ? 20.212 24.820 19.864 1.00 21.74 ? 157 CYS A CB 1 ATOM 1096 S SG . CYS A 1 139 ? 18.951 23.649 20.468 1.00 22.40 ? 157 CYS A SG 1 ATOM 1097 N N . THR A 1 140 ? 23.333 24.861 19.741 1.00 24.73 ? 158 THR A N 1 ATOM 1098 C CA . THR A 1 140 ? 24.517 25.167 18.944 1.00 24.89 ? 158 THR A CA 1 ATOM 1099 C C . THR A 1 140 ? 25.127 23.869 18.437 1.00 24.95 ? 158 THR A C 1 ATOM 1100 O O . THR A 1 140 ? 24.815 22.785 18.942 1.00 23.52 ? 158 THR A O 1 ATOM 1101 C CB . THR A 1 140 ? 25.591 25.959 19.733 1.00 25.29 ? 158 THR A CB 1 ATOM 1102 O OG1 . THR A 1 140 ? 26.514 26.545 18.804 1.00 26.18 ? 158 THR A OG1 1 ATOM 1103 C CG2 . THR A 1 140 ? 26.367 25.045 20.669 1.00 23.73 ? 158 THR A CG2 1 ATOM 1104 N N . ASN A 1 141 ? 25.986 23.981 17.430 1.00 23.31 ? 159 ASN A N 1 ATOM 1105 C CA . ASN A 1 141 ? 26.641 22.817 16.854 1.00 25.10 ? 159 ASN A CA 1 ATOM 1106 C C . ASN A 1 141 ? 28.093 22.724 17.300 1.00 23.86 ? 159 ASN A C 1 ATOM 1107 O O . ASN A 1 141 ? 28.780 23.734 17.425 1.00 24.32 ? 159 ASN A O 1 ATOM 1108 C CB . ASN A 1 141 ? 26.584 22.871 15.324 1.00 27.11 ? 159 ASN A CB 1 ATOM 1109 C CG . ASN A 1 141 ? 25.165 22.865 14.794 1.00 29.63 ? 159 ASN A CG 1 ATOM 1110 O OD1 . ASN A 1 141 ? 24.346 22.044 15.202 1.00 29.01 ? 159 ASN A OD1 1 ATOM 1111 N ND2 . ASN A 1 141 ? 24.869 23.777 13.868 1.00 31.62 ? 159 ASN A ND2 1 ATOM 1112 N N . ILE A 1 142 ? 28.541 21.497 17.549 1.00 24.28 ? 160 ILE A N 1 ATOM 1113 C CA . ILE A 1 142 ? 29.909 21.224 17.964 1.00 23.11 ? 160 ILE A CA 1 ATOM 1114 C C . ILE A 1 142 ? 30.359 19.999 17.176 1.00 22.76 ? 160 ILE A C 1 ATOM 1115 O O . ILE A 1 142 ? 29.597 19.464 16.373 1.00 24.30 ? 160 ILE A O 1 ATOM 1116 C CB . ILE A 1 142 ? 29.998 20.919 19.486 1.00 22.44 ? 160 ILE A CB 1 ATOM 1117 C CG1 . ILE A 1 142 ? 29.164 19.677 19.830 1.00 23.76 ? 160 ILE A CG1 1 ATOM 1118 C CG2 . ILE A 1 142 ? 29.519 22.118 20.284 1.00 23.46 ? 160 ILE A CG2 1 ATOM 1119 C CD1 . ILE A 1 142 ? 29.268 19.242 21.295 1.00 21.25 ? 160 ILE A CD1 1 ATOM 1120 N N . PHE A 1 143 ? 31.593 19.556 17.390 1.00 23.56 ? 161 PHE A N 1 ATOM 1121 C CA . PHE A 1 143 ? 32.090 18.381 16.685 1.00 24.71 ? 161 PHE A CA 1 ATOM 1122 C C . PHE A 1 143 ? 32.689 17.354 17.639 1.00 24.09 ? 161 PHE A C 1 ATOM 1123 O O . PHE A 1 143 ? 33.180 17.700 18.710 1.00 23.97 ? 161 PHE A O 1 ATOM 1124 C CB . PHE A 1 143 ? 33.173 18.767 15.669 1.00 26.19 ? 161 PHE A CB 1 ATOM 1125 C CG . PHE A 1 143 ? 32.693 19.692 14.585 1.00 28.88 ? 161 PHE A CG 1 ATOM 1126 C CD1 . PHE A 1 143 ? 32.513 21.048 14.838 1.00 29.44 ? 161 PHE A CD1 1 ATOM 1127 C CD2 . PHE A 1 143 ? 32.410 19.203 13.316 1.00 30.48 ? 161 PHE A CD2 1 ATOM 1128 C CE1 . PHE A 1 143 ? 32.057 21.909 13.836 1.00 31.99 ? 161 PHE A CE1 1 ATOM 1129 C CE2 . PHE A 1 143 ? 31.953 20.054 12.306 1.00 32.45 ? 161 PHE A CE2 1 ATOM 1130 C CZ . PHE A 1 143 ? 31.777 21.408 12.567 1.00 30.80 ? 161 PHE A CZ 1 ATOM 1131 N N . ILE A 1 144 ? 32.636 16.089 17.244 1.00 25.96 ? 162 ILE A N 1 ATOM 1132 C CA . ILE A 1 144 ? 33.236 15.034 18.044 1.00 27.44 ? 162 ILE A CA 1 ATOM 1133 C C . ILE A 1 144 ? 34.717 15.158 17.706 1.00 28.22 ? 162 ILE A C 1 ATOM 1134 O O . ILE A 1 144 ? 35.075 15.215 16.528 1.00 28.05 ? 162 ILE A O 1 ATOM 1135 C CB . ILE A 1 144 ? 32.747 13.638 17.619 1.00 26.93 ? 162 ILE A CB 1 ATOM 1136 C CG1 . ILE A 1 144 ? 31.251 13.493 17.916 1.00 26.63 ? 162 ILE A CG1 1 ATOM 1137 C CG2 . ILE A 1 144 ? 33.553 12.560 18.349 1.00 26.95 ? 162 ILE A CG2 1 ATOM 1138 C CD1 . ILE A 1 144 ? 30.670 12.167 17.477 1.00 26.67 ? 162 ILE A CD1 1 ATOM 1139 N N . VAL A 1 145 ? 35.564 15.233 18.729 1.00 28.66 ? 163 VAL A N 1 ATOM 1140 C CA . VAL A 1 145 ? 37.005 15.361 18.524 1.00 30.47 ? 163 VAL A CA 1 ATOM 1141 C C . VAL A 1 145 ? 37.753 14.165 19.102 1.00 31.39 ? 163 VAL A C 1 ATOM 1142 O O . VAL A 1 145 ? 37.142 13.274 19.698 1.00 32.00 ? 163 VAL A O 1 ATOM 1143 C CB . VAL A 1 145 ? 37.550 16.645 19.184 1.00 29.93 ? 163 VAL A CB 1 ATOM 1144 C CG1 . VAL A 1 145 ? 36.846 17.865 18.604 1.00 32.11 ? 163 VAL A CG1 1 ATOM 1145 C CG2 . VAL A 1 145 ? 37.352 16.582 20.695 1.00 30.21 ? 163 VAL A CG2 1 ATOM 1146 N N . LYS A 1 146 ? 39.073 14.141 18.919 1.00 30.21 ? 164 LYS A N 1 ATOM 1147 C CA . LYS A 1 146 ? 39.884 13.042 19.438 1.00 29.05 ? 164 LYS A CA 1 ATOM 1148 C C . LYS A 1 146 ? 39.687 12.948 20.940 1.00 27.28 ? 164 LYS A C 1 ATOM 1149 O O . LYS A 1 146 ? 39.756 13.948 21.649 1.00 25.06 ? 164 LYS A O 1 ATOM 1150 C CB . LYS A 1 146 ? 41.366 13.259 19.113 1.00 32.59 ? 164 LYS A CB 1 ATOM 1151 C CG . LYS A 1 146 ? 41.691 13.152 17.631 1.00 35.58 ? 164 LYS A CG 1 ATOM 1152 C CD . LYS A 1 146 ? 41.512 11.727 17.109 1.00 39.62 ? 164 LYS A CD 1 ATOM 1153 C CE . LYS A 1 146 ? 42.757 10.860 17.337 1.00 40.78 ? 164 LYS A CE 1 ATOM 1154 N NZ . LYS A 1 146 ? 43.169 10.775 18.767 1.00 43.33 ? 164 LYS A NZ 1 ATOM 1155 N N . HIS A 1 147 ? 39.446 11.734 21.414 1.00 29.19 ? 165 HIS A N 1 ATOM 1156 C CA . HIS A 1 147 ? 39.197 11.482 22.826 1.00 29.29 ? 165 HIS A CA 1 ATOM 1157 C C . HIS A 1 147 ? 40.339 11.936 23.736 1.00 29.50 ? 165 HIS A C 1 ATOM 1158 O O . HIS A 1 147 ? 40.132 12.201 24.922 1.00 28.86 ? 165 HIS A O 1 ATOM 1159 C CB . HIS A 1 147 ? 38.916 9.992 23.021 1.00 31.02 ? 165 HIS A CB 1 ATOM 1160 C CG . HIS A 1 147 ? 38.192 9.676 24.292 1.00 31.90 ? 165 HIS A CG 1 ATOM 1161 N ND1 . HIS A 1 147 ? 38.840 9.498 25.496 1.00 32.96 ? 165 HIS A ND1 1 ATOM 1162 C CD2 . HIS A 1 147 ? 36.871 9.522 24.549 1.00 32.81 ? 165 HIS A CD2 1 ATOM 1163 C CE1 . HIS A 1 147 ? 37.949 9.246 26.439 1.00 33.43 ? 165 HIS A CE1 1 ATOM 1164 N NE2 . HIS A 1 147 ? 36.747 9.255 25.890 1.00 33.21 ? 165 HIS A NE2 1 ATOM 1165 N N . LYS A 1 148 ? 41.537 12.037 23.172 1.00 29.21 ? 166 LYS A N 1 ATOM 1166 C CA . LYS A 1 148 ? 42.712 12.459 23.926 1.00 29.86 ? 166 LYS A CA 1 ATOM 1167 C C . LYS A 1 148 ? 42.579 13.864 24.514 1.00 29.53 ? 166 LYS A C 1 ATOM 1168 O O . LYS A 1 148 ? 43.269 14.200 25.474 1.00 29.43 ? 166 LYS A O 1 ATOM 1169 C CB . LYS A 1 148 ? 43.951 12.424 23.032 1.00 32.62 ? 166 LYS A CB 1 ATOM 1170 C CG . LYS A 1 148 ? 43.920 13.483 21.946 1.00 35.20 ? 166 LYS A CG 1 ATOM 1171 C CD . LYS A 1 148 ? 45.177 13.485 21.101 1.00 38.43 ? 166 LYS A CD 1 ATOM 1172 C CE . LYS A 1 148 ? 45.112 14.599 20.061 1.00 39.88 ? 166 LYS A CE 1 ATOM 1173 N NZ . LYS A 1 148 ? 46.263 14.576 19.114 1.00 42.41 ? 166 LYS A NZ 1 ATOM 1174 N N . TRP A 1 149 ? 41.709 14.693 23.939 1.00 29.39 ? 167 TRP A N 1 ATOM 1175 C CA . TRP A 1 149 ? 41.542 16.052 24.450 1.00 29.12 ? 167 TRP A CA 1 ATOM 1176 C C . TRP A 1 149 ? 40.873 16.090 25.813 1.00 30.26 ? 167 TRP A C 1 ATOM 1177 O O . TRP A 1 149 ? 41.174 16.950 26.640 1.00 30.52 ? 167 TRP A O 1 ATOM 1178 C CB . TRP A 1 149 ? 40.731 16.906 23.471 1.00 30.86 ? 167 TRP A CB 1 ATOM 1179 C CG . TRP A 1 149 ? 41.478 17.245 22.228 1.00 31.83 ? 167 TRP A CG 1 ATOM 1180 C CD1 . TRP A 1 149 ? 41.357 16.651 21.007 1.00 32.31 ? 167 TRP A CD1 1 ATOM 1181 C CD2 . TRP A 1 149 ? 42.504 18.236 22.094 1.00 34.48 ? 167 TRP A CD2 1 ATOM 1182 N NE1 . TRP A 1 149 ? 42.244 17.209 20.119 1.00 32.05 ? 167 TRP A NE1 1 ATOM 1183 C CE2 . TRP A 1 149 ? 42.961 18.185 20.761 1.00 33.70 ? 167 TRP A CE2 1 ATOM 1184 C CE3 . TRP A 1 149 ? 43.080 19.163 22.974 1.00 36.00 ? 167 TRP A CE3 1 ATOM 1185 C CZ2 . TRP A 1 149 ? 43.975 19.025 20.281 1.00 36.16 ? 167 TRP A CZ2 1 ATOM 1186 C CZ3 . TRP A 1 149 ? 44.090 20.000 22.497 1.00 38.72 ? 167 TRP A CZ3 1 ATOM 1187 C CH2 . TRP A 1 149 ? 44.524 19.923 21.161 1.00 36.71 ? 167 TRP A CH2 1 ATOM 1188 N N . CYS A 1 150 ? 39.969 15.148 26.046 1.00 29.73 ? 168 CYS A N 1 ATOM 1189 C CA . CYS A 1 150 ? 39.231 15.081 27.302 1.00 29.89 ? 168 CYS A CA 1 ATOM 1190 C C . CYS A 1 150 ? 39.940 14.351 28.442 1.00 29.82 ? 168 CYS A C 1 ATOM 1191 O O . CYS A 1 150 ? 39.803 14.716 29.612 1.00 29.02 ? 168 CYS A O 1 ATOM 1192 C CB . CYS A 1 150 ? 37.883 14.402 27.057 1.00 28.27 ? 168 CYS A CB 1 ATOM 1193 S SG . CYS A 1 150 ? 36.633 15.416 26.201 1.00 28.64 ? 168 CYS A SG 1 ATOM 1194 N N . GLU A 1 151 ? 40.692 13.317 28.094 1.00 29.96 ? 169 GLU A N 1 ATOM 1195 C CA . GLU A 1 151 ? 41.378 12.491 29.083 1.00 30.42 ? 169 GLU A CA 1 ATOM 1196 C C . GLU A 1 151 ? 42.209 13.182 30.164 1.00 30.69 ? 169 GLU A C 1 ATOM 1197 O O . GLU A 1 151 ? 42.018 12.920 31.351 1.00 30.85 ? 169 GLU A O 1 ATOM 1198 C CB . GLU A 1 151 ? 42.214 11.445 28.355 1.00 31.19 ? 169 GLU A CB 1 ATOM 1199 C CG . GLU A 1 151 ? 41.357 10.378 27.698 1.00 30.37 ? 169 GLU A CG 1 ATOM 1200 C CD . GLU A 1 151 ? 42.112 9.580 26.663 1.00 32.02 ? 169 GLU A CD 1 ATOM 1201 O OE1 . GLU A 1 151 ? 43.334 9.381 26.846 1.00 30.11 ? 169 GLU A OE1 1 ATOM 1202 O OE2 . GLU A 1 151 ? 41.476 9.146 25.677 1.00 29.25 ? 169 GLU A OE2 1 ATOM 1203 N N . PRO A 1 152 ? 43.143 14.063 29.781 1.00 31.31 ? 170 PRO A N 1 ATOM 1204 C CA . PRO A 1 152 ? 43.935 14.719 30.828 1.00 31.66 ? 170 PRO A CA 1 ATOM 1205 C C . PRO A 1 152 ? 43.120 15.711 31.651 1.00 31.24 ? 170 PRO A C 1 ATOM 1206 O O . PRO A 1 152 ? 43.523 16.106 32.746 1.00 31.12 ? 170 PRO A O 1 ATOM 1207 C CB . PRO A 1 152 ? 45.049 15.400 30.037 1.00 32.31 ? 170 PRO A CB 1 ATOM 1208 C CG . PRO A 1 152 ? 44.372 15.742 28.740 1.00 33.77 ? 170 PRO A CG 1 ATOM 1209 C CD . PRO A 1 152 ? 43.585 14.484 28.439 1.00 31.66 ? 170 PRO A CD 1 ATOM 1210 N N . LEU A 1 153 ? 41.961 16.099 31.130 1.00 30.93 ? 171 LEU A N 1 ATOM 1211 C CA . LEU A 1 153 ? 41.115 17.069 31.809 1.00 30.30 ? 171 LEU A CA 1 ATOM 1212 C C . LEU A 1 153 ? 40.131 16.485 32.812 1.00 28.96 ? 171 LEU A C 1 ATOM 1213 O O . LEU A 1 153 ? 39.844 17.099 33.838 1.00 30.04 ? 171 LEU A O 1 ATOM 1214 C CB . LEU A 1 153 ? 40.329 17.884 30.773 1.00 31.45 ? 171 LEU A CB 1 ATOM 1215 C CG . LEU A 1 153 ? 41.141 18.659 29.732 1.00 31.62 ? 171 LEU A CG 1 ATOM 1216 C CD1 . LEU A 1 153 ? 40.198 19.331 28.732 1.00 34.66 ? 171 LEU A CD1 1 ATOM 1217 C CD2 . LEU A 1 153 ? 42.003 19.695 30.433 1.00 31.92 ? 171 LEU A CD2 1 ATOM 1218 N N . TYR A 1 154 ? 39.612 15.301 32.520 1.00 29.03 ? 172 TYR A N 1 ATOM 1219 C CA . TYR A 1 154 ? 38.608 14.697 33.387 1.00 28.03 ? 172 TYR A CA 1 ATOM 1220 C C . TYR A 1 154 ? 39.016 13.346 33.962 1.00 26.96 ? 172 TYR A C 1 ATOM 1221 O O . TYR A 1 154 ? 39.056 12.333 33.263 1.00 25.76 ? 172 TYR A O 1 ATOM 1222 C CB . TYR A 1 154 ? 37.302 14.583 32.596 1.00 28.92 ? 172 TYR A CB 1 ATOM 1223 C CG . TYR A 1 154 ? 36.960 15.870 31.873 1.00 29.62 ? 172 TYR A CG 1 ATOM 1224 C CD1 . TYR A 1 154 ? 36.662 17.033 32.584 1.00 30.55 ? 172 TYR A CD1 1 ATOM 1225 C CD2 . TYR A 1 154 ? 36.987 15.941 30.480 1.00 31.81 ? 172 TYR A CD2 1 ATOM 1226 C CE1 . TYR A 1 154 ? 36.401 18.233 31.927 1.00 30.30 ? 172 TYR A CE1 1 ATOM 1227 C CE2 . TYR A 1 154 ? 36.730 17.136 29.813 1.00 30.55 ? 172 TYR A CE2 1 ATOM 1228 C CZ . TYR A 1 154 ? 36.439 18.277 30.542 1.00 31.34 ? 172 TYR A CZ 1 ATOM 1229 O OH . TYR A 1 154 ? 36.201 19.466 29.889 1.00 30.26 ? 172 TYR A OH 1 ATOM 1230 N N . PRO A 1 155 A 39.314 13.316 35.267 1.00 28.31 ? 172 PRO A N 1 ATOM 1231 C CA . PRO A 1 155 A 39.725 12.090 35.953 1.00 27.42 ? 172 PRO A CA 1 ATOM 1232 C C . PRO A 1 155 A 38.734 10.933 35.866 1.00 26.77 ? 172 PRO A C 1 ATOM 1233 O O . PRO A 1 155 A 39.133 9.771 35.897 1.00 25.97 ? 172 PRO A O 1 ATOM 1234 C CB . PRO A 1 155 A 39.950 12.562 37.392 1.00 29.36 ? 172 PRO A CB 1 ATOM 1235 C CG . PRO A 1 155 A 38.987 13.703 37.526 1.00 30.76 ? 172 PRO A CG 1 ATOM 1236 C CD . PRO A 1 155 A 39.178 14.430 36.220 1.00 29.07 ? 172 PRO A CD 1 ATOM 1237 N N . TRP A 1 156 ? 37.446 11.244 35.756 1.00 25.85 ? 173 TRP A N 1 ATOM 1238 C CA . TRP A 1 156 ? 36.428 10.203 35.671 1.00 27.41 ? 173 TRP A CA 1 ATOM 1239 C C . TRP A 1 156 ? 36.252 9.665 34.252 1.00 27.05 ? 173 TRP A C 1 ATOM 1240 O O . TRP A 1 156 ? 35.410 8.803 34.011 1.00 27.87 ? 173 TRP A O 1 ATOM 1241 C CB . TRP A 1 156 ? 35.086 10.736 36.177 1.00 28.31 ? 173 TRP A CB 1 ATOM 1242 C CG . TRP A 1 156 ? 35.132 11.248 37.583 1.00 31.61 ? 173 TRP A CG 1 ATOM 1243 C CD1 . TRP A 1 156 ? 34.584 12.410 38.048 1.00 32.91 ? 173 TRP A CD1 1 ATOM 1244 C CD2 . TRP A 1 156 ? 35.752 10.619 38.710 1.00 33.47 ? 173 TRP A CD2 1 ATOM 1245 N NE1 . TRP A 1 156 ? 34.828 12.545 39.393 1.00 33.81 ? 173 TRP A NE1 1 ATOM 1246 C CE2 . TRP A 1 156 ? 35.542 11.458 39.826 1.00 33.85 ? 173 TRP A CE2 1 ATOM 1247 C CE3 . TRP A 1 156 ? 36.466 9.425 38.886 1.00 34.35 ? 173 TRP A CE3 1 ATOM 1248 C CZ2 . TRP A 1 156 ? 36.021 11.145 41.102 1.00 36.18 ? 173 TRP A CZ2 1 ATOM 1249 C CZ3 . TRP A 1 156 ? 36.944 9.111 40.156 1.00 36.41 ? 173 TRP A CZ3 1 ATOM 1250 C CH2 . TRP A 1 156 ? 36.718 9.970 41.249 1.00 37.26 ? 173 TRP A CH2 1 ATOM 1251 N N . VAL A 1 157 ? 37.045 10.166 33.314 1.00 27.32 ? 174 VAL A N 1 ATOM 1252 C CA . VAL A 1 157 ? 36.931 9.715 31.935 1.00 26.91 ? 174 VAL A CA 1 ATOM 1253 C C . VAL A 1 157 ? 38.216 9.038 31.482 1.00 28.15 ? 174 VAL A C 1 ATOM 1254 O O . VAL A 1 157 ? 39.098 9.669 30.910 1.00 27.94 ? 174 VAL A O 1 ATOM 1255 C CB . VAL A 1 157 ? 36.606 10.895 30.999 1.00 27.88 ? 174 VAL A CB 1 ATOM 1256 C CG1 . VAL A 1 157 ? 36.386 10.393 29.572 1.00 28.62 ? 174 VAL A CG1 1 ATOM 1257 C CG2 . VAL A 1 157 ? 35.366 11.622 31.507 1.00 26.86 ? 174 VAL A CG2 1 ATOM 1258 N N . PRO A 1 158 ? 38.336 7.732 31.741 1.00 28.93 ? 175 PRO A N 1 ATOM 1259 C CA . PRO A 1 158 ? 39.541 7.006 31.340 1.00 29.66 ? 175 PRO A CA 1 ATOM 1260 C C . PRO A 1 158 ? 39.608 6.746 29.844 1.00 29.86 ? 175 PRO A C 1 ATOM 1261 O O . PRO A 1 158 ? 38.619 6.898 29.127 1.00 28.01 ? 175 PRO A O 1 ATOM 1262 C CB . PRO A 1 158 ? 39.448 5.719 32.150 1.00 28.27 ? 175 PRO A CB 1 ATOM 1263 C CG . PRO A 1 158 ? 37.986 5.486 32.237 1.00 31.98 ? 175 PRO A CG 1 ATOM 1264 C CD . PRO A 1 158 ? 37.449 6.871 32.543 1.00 29.29 ? 175 PRO A CD 1 ATOM 1265 N N . ALA A 1 159 ? 40.788 6.359 29.378 1.00 30.33 ? 176 ALA A N 1 ATOM 1266 C CA . ALA A 1 159 ? 40.971 6.058 27.971 1.00 29.80 ? 176 ALA A CA 1 ATOM 1267 C C . ALA A 1 159 ? 40.143 4.811 27.686 1.00 31.16 ? 176 ALA A C 1 ATOM 1268 O O . ALA A 1 159 ? 39.935 3.979 28.570 1.00 32.28 ? 176 ALA A O 1 ATOM 1269 C CB . ALA A 1 159 ? 42.441 5.800 27.679 1.00 29.70 ? 176 ALA A CB 1 ATOM 1270 N N . ASP A 1 160 ? 39.661 4.689 26.458 1.00 30.75 ? 177 ASP A N 1 ATOM 1271 C CA . ASP A 1 160 ? 38.851 3.544 26.065 1.00 32.50 ? 177 ASP A CA 1 ATOM 1272 C C . ASP A 1 160 ? 37.510 3.489 26.800 1.00 32.34 ? 177 ASP A C 1 ATOM 1273 O O . ASP A 1 160 ? 36.795 2.494 26.715 1.00 34.04 ? 177 ASP A O 1 ATOM 1274 C CB . ASP A 1 160 ? 39.624 2.234 26.281 1.00 33.16 ? 177 ASP A CB 1 ATOM 1275 C CG . ASP A 1 160 ? 40.920 2.185 25.491 1.00 32.63 ? 177 ASP A CG 1 ATOM 1276 O OD1 . ASP A 1 160 ? 40.974 2.777 24.394 1.00 33.39 ? 177 ASP A OD1 1 ATOM 1277 O OD2 . ASP A 1 160 ? 41.883 1.545 25.957 1.00 35.11 ? 177 ASP A OD2 1 ATOM 1278 N N . SER A 1 161 ? 37.168 4.549 27.527 1.00 31.33 ? 178 SER A N 1 ATOM 1279 C CA . SER A 1 161 ? 35.883 4.579 28.215 1.00 31.35 ? 178 SER A CA 1 ATOM 1280 C C . SER A 1 161 ? 34.801 4.819 27.160 1.00 31.13 ? 178 SER A C 1 ATOM 1281 O O . SER A 1 161 ? 35.087 5.309 26.065 1.00 29.53 ? 178 SER A O 1 ATOM 1282 C CB . SER A 1 161 ? 35.849 5.684 29.279 1.00 31.71 ? 178 SER A CB 1 ATOM 1283 O OG . SER A 1 161 ? 35.971 6.978 28.721 1.00 33.74 ? 178 SER A OG 1 ATOM 1284 N N . ARG A 1 162 ? 33.561 4.473 27.488 1.00 28.95 ? 179 ARG A N 1 ATOM 1285 C CA . ARG A 1 162 ? 32.456 4.623 26.551 1.00 29.35 ? 179 ARG A CA 1 ATOM 1286 C C . ARG A 1 162 ? 31.904 6.044 26.549 1.00 28.40 ? 179 ARG A C 1 ATOM 1287 O O . ARG A 1 162 ? 30.779 6.303 26.989 1.00 26.55 ? 179 ARG A O 1 ATOM 1288 C CB . ARG A 1 162 ? 31.367 3.607 26.895 1.00 29.93 ? 179 ARG A CB 1 ATOM 1289 C CG . ARG A 1 162 ? 31.901 2.176 26.957 1.00 33.75 ? 179 ARG A CG 1 ATOM 1290 C CD . ARG A 1 162 ? 30.848 1.191 27.423 1.00 35.25 ? 179 ARG A CD 1 ATOM 1291 N NE . ARG A 1 162 ? 31.369 -0.173 27.513 1.00 38.06 ? 179 ARG A NE 1 ATOM 1292 C CZ . ARG A 1 162 ? 31.744 -0.912 26.471 1.00 39.21 ? 179 ARG A CZ 1 ATOM 1293 N NH1 . ARG A 1 162 ? 31.661 -0.428 25.237 1.00 38.55 ? 179 ARG A NH1 1 ATOM 1294 N NH2 . ARG A 1 162 ? 32.195 -2.145 26.663 1.00 39.02 ? 179 ARG A NH2 1 ATOM 1295 N N . THR A 1 163 ? 32.716 6.964 26.044 1.00 27.32 ? 180 THR A N 1 ATOM 1296 C CA . THR A 1 163 ? 32.340 8.366 25.986 1.00 26.15 ? 180 THR A CA 1 ATOM 1297 C C . THR A 1 163 ? 32.862 9.024 24.718 1.00 26.80 ? 180 THR A C 1 ATOM 1298 O O . THR A 1 163 ? 33.818 8.548 24.108 1.00 27.00 ? 180 THR A O 1 ATOM 1299 C CB . THR A 1 163 ? 32.909 9.144 27.189 1.00 25.82 ? 180 THR A CB 1 ATOM 1300 O OG1 . THR A 1 163 ? 34.327 8.936 27.263 1.00 26.96 ? 180 THR A OG1 1 ATOM 1301 C CG2 . THR A 1 163 ? 32.258 8.677 28.492 1.00 25.74 ? 180 THR A CG2 1 ATOM 1302 N N . LEU A 1 164 ? 32.218 10.117 24.330 1.00 25.64 ? 181 LEU A N 1 ATOM 1303 C CA . LEU A 1 164 ? 32.625 10.881 23.157 1.00 25.10 ? 181 LEU A CA 1 ATOM 1304 C C . LEU A 1 164 ? 33.108 12.238 23.641 1.00 24.74 ? 181 LEU A C 1 ATOM 1305 O O . LEU A 1 164 ? 32.453 12.879 24.464 1.00 25.99 ? 181 LEU A O 1 ATOM 1306 C CB . LEU A 1 164 ? 31.443 11.089 22.205 1.00 24.70 ? 181 LEU A CB 1 ATOM 1307 C CG . LEU A 1 164 ? 30.757 9.845 21.641 1.00 25.00 ? 181 LEU A CG 1 ATOM 1308 C CD1 . LEU A 1 164 ? 29.473 10.257 20.929 1.00 27.63 ? 181 LEU A CD1 1 ATOM 1309 C CD2 . LEU A 1 164 ? 31.703 9.119 20.691 1.00 27.07 ? 181 LEU A CD2 1 ATOM 1310 N N . CYS A 1 165 ? 34.260 12.671 23.139 1.00 23.41 ? 182 CYS A N 1 ATOM 1311 C CA . CYS A 1 165 ? 34.804 13.974 23.497 1.00 21.80 ? 182 CYS A CA 1 ATOM 1312 C C . CYS A 1 165 ? 34.344 14.895 22.366 1.00 23.18 ? 182 CYS A C 1 ATOM 1313 O O . CYS A 1 165 ? 34.625 14.629 21.197 1.00 23.92 ? 182 CYS A O 1 ATOM 1314 C CB . CYS A 1 165 ? 36.334 13.907 23.554 1.00 24.74 ? 182 CYS A CB 1 ATOM 1315 S SG . CYS A 1 165 ? 37.169 15.376 24.238 1.00 27.04 ? 182 CYS A SG 1 ATOM 1316 N N . ALA A 1 166 ? 33.627 15.960 22.704 1.00 23.06 ? 183 ALA A N 1 ATOM 1317 C CA . ALA A 1 166 ? 33.126 16.863 21.675 1.00 24.68 ? 183 ALA A CA 1 ATOM 1318 C C . ALA A 1 166 ? 33.022 18.329 22.093 1.00 24.07 ? 183 ALA A C 1 ATOM 1319 O O . ALA A 1 166 ? 32.864 18.654 23.270 1.00 24.56 ? 183 ALA A O 1 ATOM 1320 C CB . ALA A 1 166 ? 31.769 16.364 21.183 1.00 23.15 ? 183 ALA A CB 1 ATOM 1321 N N . GLY A 1 167 ? 33.107 19.210 21.099 1.00 25.25 ? 184 GLY A N 1 ATOM 1322 C CA . GLY A 1 167 ? 33.021 20.635 21.349 1.00 24.29 ? 184 GLY A CA 1 ATOM 1323 C C . GLY A 1 167 ? 33.702 21.409 20.235 1.00 25.01 ? 184 GLY A C 1 ATOM 1324 O O . GLY A 1 167 ? 33.756 20.951 19.091 1.00 23.17 ? 184 GLY A O 1 ATOM 1325 N N . ILE A 1 168 ? 34.215 22.585 20.574 1.00 26.56 ? 185 ILE A N 1 ATOM 1326 C CA . ILE A 1 168 ? 34.913 23.437 19.617 1.00 29.58 ? 185 ILE A CA 1 ATOM 1327 C C . ILE A 1 168 ? 36.290 23.736 20.198 1.00 28.66 ? 185 ILE A C 1 ATOM 1328 O O . ILE A 1 168 ? 36.416 24.521 21.139 1.00 30.67 ? 185 ILE A O 1 ATOM 1329 C CB . ILE A 1 168 ? 34.155 24.766 19.393 1.00 29.66 ? 185 ILE A CB 1 ATOM 1330 C CG1 . ILE A 1 168 ? 32.745 24.482 18.864 1.00 28.71 ? 185 ILE A CG1 1 ATOM 1331 C CG2 . ILE A 1 168 ? 34.939 25.657 18.430 1.00 30.72 ? 185 ILE A CG2 1 ATOM 1332 C CD1 . ILE A 1 168 ? 32.707 23.744 17.537 1.00 27.57 ? 185 ILE A CD1 1 ATOM 1333 N N . LEU A 1 169 ? 37.316 23.103 19.639 1.00 29.82 ? 186 LEU A N 1 ATOM 1334 C CA . LEU A 1 169 ? 38.685 23.279 20.117 1.00 32.53 ? 186 LEU A CA 1 ATOM 1335 C C . LEU A 1 169 ? 39.099 24.738 20.249 1.00 34.20 ? 186 LEU A C 1 ATOM 1336 O O . LEU A 1 169 ? 39.903 25.089 21.115 1.00 33.60 ? 186 LEU A O 1 ATOM 1337 C CB . LEU A 1 169 ? 39.657 22.533 19.198 1.00 33.49 ? 186 LEU A CB 1 ATOM 1338 C CG . LEU A 1 169 ? 39.467 21.012 19.192 1.00 34.58 ? 186 LEU A CG 1 ATOM 1339 C CD1 . LEU A 1 169 ? 40.354 20.364 18.147 1.00 34.73 ? 186 LEU A CD1 1 ATOM 1340 C CD2 . LEU A 1 169 ? 39.783 20.466 20.570 1.00 35.64 ? 186 LEU A CD2 1 ATOM 1341 N N . LYS A 1 170 A 38.546 25.593 19.398 1.00 35.11 ? 186 LYS A N 1 ATOM 1342 C CA . LYS A 1 170 A 38.872 27.011 19.449 1.00 36.65 ? 186 LYS A CA 1 ATOM 1343 C C . LYS A 1 170 A 38.148 27.687 20.607 1.00 36.59 ? 186 LYS A C 1 ATOM 1344 O O . LYS A 1 170 A 38.500 28.794 21.007 1.00 37.03 ? 186 LYS A O 1 ATOM 1345 C CB . LYS A 1 170 A 38.496 27.682 18.128 1.00 38.95 ? 186 LYS A CB 1 ATOM 1346 C CG . LYS A 1 170 A 39.304 27.180 16.948 1.00 41.27 ? 186 LYS A CG 1 ATOM 1347 C CD . LYS A 1 170 A 38.785 27.737 15.635 1.00 44.10 ? 186 LYS A CD 1 ATOM 1348 C CE . LYS A 1 170 A 39.563 27.164 14.461 1.00 45.65 ? 186 LYS A CE 1 ATOM 1349 N NZ . LYS A 1 170 A 38.976 27.563 13.153 1.00 47.83 ? 186 LYS A NZ 1 ATOM 1350 N N . GLY A 1 171 B 37.141 27.010 21.151 1.00 35.09 ? 186 GLY A N 1 ATOM 1351 C CA . GLY A 1 171 B 36.385 27.567 22.259 1.00 34.50 ? 186 GLY A CA 1 ATOM 1352 C C . GLY A 1 171 B 35.189 28.367 21.775 1.00 33.90 ? 186 GLY A C 1 ATOM 1353 O O . GLY A 1 171 B 34.986 28.508 20.568 1.00 34.79 ? 186 GLY A O 1 ATOM 1354 N N . GLY A 1 172 ? 34.392 28.879 22.710 1.00 33.62 ? 187 GLY A N 1 ATOM 1355 C CA . GLY A 1 172 ? 33.229 29.672 22.343 1.00 32.23 ? 187 GLY A CA 1 ATOM 1356 C C . GLY A 1 172 ? 31.884 28.959 22.370 1.00 31.33 ? 187 GLY A C 1 ATOM 1357 O O . GLY A 1 172 ? 30.859 29.581 22.644 1.00 31.61 ? 187 GLY A O 1 ATOM 1358 N N . ARG A 1 173 ? 31.876 27.665 22.071 1.00 30.02 ? 188 ARG A N 1 ATOM 1359 C CA . ARG A 1 173 ? 30.637 26.885 22.074 1.00 29.47 ? 188 ARG A CA 1 ATOM 1360 C C . ARG A 1 173 ? 30.841 25.625 22.915 1.00 28.16 ? 188 ARG A C 1 ATOM 1361 O O . ARG A 1 173 ? 31.814 24.894 22.714 1.00 26.65 ? 188 ARG A O 1 ATOM 1362 C CB . ARG A 1 173 ? 30.244 26.523 20.642 1.00 29.77 ? 188 ARG A CB 1 ATOM 1363 C CG . ARG A 1 173 ? 29.788 27.730 19.822 1.00 33.96 ? 188 ARG A CG 1 ATOM 1364 C CD . ARG A 1 173 ? 29.337 27.324 18.427 1.00 36.81 ? 188 ARG A CD 1 ATOM 1365 N NE . ARG A 1 173 ? 30.463 27.064 17.539 1.00 42.09 ? 188 ARG A NE 1 ATOM 1366 C CZ . ARG A 1 173 ? 30.360 26.477 16.352 1.00 43.20 ? 188 ARG A CZ 1 ATOM 1367 N NH1 . ARG A 1 173 ? 31.443 26.289 15.608 1.00 46.28 ? 188 ARG A NH1 1 ATOM 1368 N NH2 . ARG A 1 173 ? 29.178 26.065 15.912 1.00 43.69 ? 188 ARG A NH2 1 ATOM 1369 N N . ASP A 1 174 ? 29.917 25.355 23.836 1.00 26.59 ? 189 ASP A N 1 ATOM 1370 C CA . ASP A 1 174 ? 30.080 24.202 24.719 1.00 25.93 ? 189 ASP A CA 1 ATOM 1371 C C . ASP A 1 174 ? 28.860 24.033 25.633 1.00 25.17 ? 189 ASP A C 1 ATOM 1372 O O . ASP A 1 174 ? 28.018 24.924 25.712 1.00 24.25 ? 189 ASP A O 1 ATOM 1373 C CB . ASP A 1 174 ? 31.358 24.459 25.536 1.00 26.28 ? 189 ASP A CB 1 ATOM 1374 C CG . ASP A 1 174 ? 31.705 23.345 26.504 1.00 26.13 ? 189 ASP A CG 1 ATOM 1375 O OD1 . ASP A 1 174 ? 31.378 22.173 26.241 1.00 25.17 ? 189 ASP A OD1 1 ATOM 1376 O OD2 . ASP A 1 174 ? 32.349 23.665 27.528 1.00 26.25 ? 189 ASP A OD2 1 ATOM 1377 N N . THR A 1 175 ? 28.747 22.881 26.294 1.00 24.64 ? 190 THR A N 1 ATOM 1378 C CA . THR A 1 175 ? 27.650 22.678 27.238 1.00 25.03 ? 190 THR A CA 1 ATOM 1379 C C . THR A 1 175 ? 28.116 23.367 28.516 1.00 25.27 ? 190 THR A C 1 ATOM 1380 O O . THR A 1 175 ? 29.312 23.603 28.685 1.00 26.06 ? 190 THR A O 1 ATOM 1381 C CB . THR A 1 175 ? 27.373 21.179 27.527 1.00 24.60 ? 190 THR A CB 1 ATOM 1382 O OG1 . THR A 1 175 ? 28.505 20.391 27.136 1.00 27.32 ? 190 THR A OG1 1 ATOM 1383 C CG2 . THR A 1 175 ? 26.134 20.716 26.767 1.00 28.84 ? 190 THR A CG2 1 ATOM 1384 N N . CYS A 1 176 ? 27.187 23.697 29.409 1.00 24.19 ? 191 CYS A N 1 ATOM 1385 C CA . CYS A 1 176 ? 27.545 24.390 30.646 1.00 26.99 ? 191 CYS A CA 1 ATOM 1386 C C . CYS A 1 176 ? 26.725 23.900 31.832 1.00 27.52 ? 191 CYS A C 1 ATOM 1387 O O . CYS A 1 176 ? 25.923 22.973 31.705 1.00 27.32 ? 191 CYS A O 1 ATOM 1388 C CB . CYS A 1 176 ? 27.337 25.897 30.473 1.00 29.97 ? 191 CYS A CB 1 ATOM 1389 S SG . CYS A 1 176 ? 28.174 26.581 29.004 1.00 33.93 ? 191 CYS A SG 1 ATOM 1390 N N . HIS A 1 177 ? 26.920 24.540 32.982 1.00 26.91 ? 192 HIS A N 1 ATOM 1391 C CA . HIS A 1 177 ? 26.198 24.170 34.195 1.00 27.15 ? 192 HIS A CA 1 ATOM 1392 C C . HIS A 1 177 ? 24.695 24.227 33.957 1.00 24.38 ? 192 HIS A C 1 ATOM 1393 O O . HIS A 1 177 ? 24.152 25.266 33.563 1.00 23.11 ? 192 HIS A O 1 ATOM 1394 C CB . HIS A 1 177 ? 26.585 25.101 35.349 1.00 29.20 ? 192 HIS A CB 1 ATOM 1395 C CG . HIS A 1 177 ? 26.040 24.674 36.676 1.00 34.65 ? 192 HIS A CG 1 ATOM 1396 N ND1 . HIS A 1 177 ? 24.835 25.127 37.169 1.00 37.48 ? 192 HIS A ND1 1 ATOM 1397 C CD2 . HIS A 1 177 ? 26.521 23.808 37.599 1.00 35.62 ? 192 HIS A CD2 1 ATOM 1398 C CE1 . HIS A 1 177 ? 24.597 24.558 38.338 1.00 36.27 ? 192 HIS A CE1 1 ATOM 1399 N NE2 . HIS A 1 177 ? 25.605 23.753 38.621 1.00 36.73 ? 192 HIS A NE2 1 ATOM 1400 N N . GLY A 1 178 ? 24.031 23.099 34.199 1.00 23.79 ? 193 GLY A N 1 ATOM 1401 C CA . GLY A 1 178 ? 22.596 23.013 33.994 1.00 21.41 ? 193 GLY A CA 1 ATOM 1402 C C . GLY A 1 178 ? 22.255 22.200 32.754 1.00 21.04 ? 193 GLY A C 1 ATOM 1403 O O . GLY A 1 178 ? 21.126 21.725 32.605 1.00 21.14 ? 193 GLY A O 1 ATOM 1404 N N . ASP A 1 179 ? 23.234 22.029 31.865 1.00 19.54 ? 194 ASP A N 1 ATOM 1405 C CA . ASP A 1 179 ? 23.029 21.269 30.631 1.00 19.87 ? 194 ASP A CA 1 ATOM 1406 C C . ASP A 1 179 ? 23.270 19.761 30.739 1.00 18.79 ? 194 ASP A C 1 ATOM 1407 O O . ASP A 1 179 ? 22.868 19.012 29.856 1.00 16.42 ? 194 ASP A O 1 ATOM 1408 C CB . ASP A 1 179 ? 23.928 21.801 29.508 1.00 19.40 ? 194 ASP A CB 1 ATOM 1409 C CG . ASP A 1 179 ? 23.520 23.172 29.026 1.00 22.23 ? 194 ASP A CG 1 ATOM 1410 O OD1 . ASP A 1 179 ? 22.307 23.389 28.803 1.00 21.86 ? 194 ASP A OD1 1 ATOM 1411 O OD2 . ASP A 1 179 ? 24.420 24.028 28.851 1.00 23.56 ? 194 ASP A OD2 1 ATOM 1412 N N . SER A 1 180 ? 23.925 19.302 31.799 1.00 17.46 ? 195 SER A N 1 ATOM 1413 C CA . SER A 1 180 ? 24.186 17.871 31.914 1.00 17.31 ? 195 SER A CA 1 ATOM 1414 C C . SER A 1 180 ? 22.941 16.999 31.853 1.00 16.81 ? 195 SER A C 1 ATOM 1415 O O . SER A 1 180 ? 21.852 17.403 32.270 1.00 19.38 ? 195 SER A O 1 ATOM 1416 C CB . SER A 1 180 ? 24.963 17.569 33.197 1.00 19.14 ? 195 SER A CB 1 ATOM 1417 O OG . SER A 1 180 ? 26.255 18.135 33.107 1.00 22.35 ? 195 SER A OG 1 ATOM 1418 N N . GLY A 1 181 ? 23.117 15.792 31.326 1.00 18.10 ? 196 GLY A N 1 ATOM 1419 C CA . GLY A 1 181 ? 22.014 14.860 31.210 1.00 16.29 ? 196 GLY A CA 1 ATOM 1420 C C . GLY A 1 181 ? 21.276 15.015 29.898 1.00 19.47 ? 196 GLY A C 1 ATOM 1421 O O . GLY A 1 181 ? 20.539 14.120 29.484 1.00 18.63 ? 196 GLY A O 1 ATOM 1422 N N . GLY A 1 182 ? 21.476 16.161 29.249 1.00 19.06 ? 197 GLY A N 1 ATOM 1423 C CA . GLY A 1 182 ? 20.823 16.422 27.981 1.00 19.94 ? 197 GLY A CA 1 ATOM 1424 C C . GLY A 1 182 ? 21.369 15.554 26.865 1.00 19.30 ? 197 GLY A C 1 ATOM 1425 O O . GLY A 1 182 ? 22.390 14.884 27.027 1.00 17.69 ? 197 GLY A O 1 ATOM 1426 N N . PRO A 1 183 ? 20.697 15.544 25.709 1.00 18.09 ? 198 PRO A N 1 ATOM 1427 C CA . PRO A 1 183 ? 21.130 14.741 24.568 1.00 19.17 ? 198 PRO A CA 1 ATOM 1428 C C . PRO A 1 183 ? 22.071 15.451 23.604 1.00 19.05 ? 198 PRO A C 1 ATOM 1429 O O . PRO A 1 183 ? 21.993 16.668 23.418 1.00 20.01 ? 198 PRO A O 1 ATOM 1430 C CB . PRO A 1 183 ? 19.816 14.386 23.891 1.00 18.71 ? 198 PRO A CB 1 ATOM 1431 C CG . PRO A 1 183 ? 19.039 15.659 24.048 1.00 18.45 ? 198 PRO A CG 1 ATOM 1432 C CD . PRO A 1 183 ? 19.333 16.065 25.496 1.00 20.02 ? 198 PRO A CD 1 ATOM 1433 N N . LEU A 1 184 ? 22.959 14.667 23.005 1.00 19.94 ? 199 LEU A N 1 ATOM 1434 C CA . LEU A 1 184 ? 23.888 15.156 21.989 1.00 20.91 ? 199 LEU A CA 1 ATOM 1435 C C . LEU A 1 184 ? 23.291 14.535 20.735 1.00 20.65 ? 199 LEU A C 1 ATOM 1436 O O . LEU A 1 184 ? 23.265 13.312 20.603 1.00 20.04 ? 199 LEU A O 1 ATOM 1437 C CB . LEU A 1 184 ? 25.297 14.602 22.212 1.00 21.74 ? 199 LEU A CB 1 ATOM 1438 C CG . LEU A 1 184 ? 26.292 14.850 21.071 1.00 22.54 ? 199 LEU A CG 1 ATOM 1439 C CD1 . LEU A 1 184 ? 26.638 16.333 20.993 1.00 22.45 ? 199 LEU A CD1 1 ATOM 1440 C CD2 . LEU A 1 184 ? 27.551 14.022 21.304 1.00 21.52 ? 199 LEU A CD2 1 ATOM 1441 N N . ILE A 1 185 ? 22.797 15.369 19.826 1.00 21.43 ? 200 ILE A N 1 ATOM 1442 C CA . ILE A 1 185 ? 22.167 14.871 18.611 1.00 21.70 ? 200 ILE A CA 1 ATOM 1443 C C . ILE A 1 185 ? 23.085 14.960 17.399 1.00 22.95 ? 200 ILE A C 1 ATOM 1444 O O . ILE A 1 185 ? 23.598 16.025 17.076 1.00 24.57 ? 200 ILE A O 1 ATOM 1445 C CB . ILE A 1 185 ? 20.871 15.663 18.278 1.00 21.96 ? 200 ILE A CB 1 ATOM 1446 C CG1 . ILE A 1 185 ? 19.898 15.629 19.468 1.00 21.12 ? 200 ILE A CG1 1 ATOM 1447 C CG2 . ILE A 1 185 ? 20.222 15.083 17.020 1.00 19.81 ? 200 ILE A CG2 1 ATOM 1448 C CD1 . ILE A 1 185 ? 19.506 14.229 19.920 1.00 19.60 ? 200 ILE A CD1 1 ATOM 1449 N N . CYS A 1 186 ? 23.279 13.832 16.730 1.00 24.51 ? 201 CYS A N 1 ATOM 1450 C CA . CYS A 1 186 ? 24.114 13.789 15.539 1.00 27.46 ? 201 CYS A CA 1 ATOM 1451 C C . CYS A 1 186 ? 23.279 13.125 14.452 1.00 28.54 ? 201 CYS A C 1 ATOM 1452 O O . CYS A 1 186 ? 22.846 11.980 14.604 1.00 28.97 ? 201 CYS A O 1 ATOM 1453 C CB . CYS A 1 186 ? 25.372 12.957 15.775 1.00 26.95 ? 201 CYS A CB 1 ATOM 1454 S SG . CYS A 1 186 ? 26.293 13.276 17.314 1.00 27.22 ? 201 CYS A SG 1 ATOM 1455 N N . ASN A 1 187 ? 23.050 13.845 13.362 1.00 30.67 ? 202 ASN A N 1 ATOM 1456 C CA . ASN A 1 187 ? 22.257 13.311 12.263 1.00 33.76 ? 202 ASN A CA 1 ATOM 1457 C C . ASN A 1 187 ? 20.914 12.758 12.735 1.00 32.69 ? 202 ASN A C 1 ATOM 1458 O O . ASN A 1 187 ? 20.561 11.622 12.427 1.00 33.34 ? 202 ASN A O 1 ATOM 1459 C CB . ASN A 1 187 ? 23.038 12.217 11.533 1.00 37.03 ? 202 ASN A CB 1 ATOM 1460 C CG . ASN A 1 187 ? 24.170 12.774 10.699 1.00 40.17 ? 202 ASN A CG 1 ATOM 1461 O OD1 . ASN A 1 187 ? 25.063 13.446 11.212 1.00 43.34 ? 202 ASN A OD1 1 ATOM 1462 N ND2 . ASN A 1 187 ? 24.138 12.498 9.401 1.00 42.52 ? 202 ASN A ND2 1 ATOM 1463 N N . GLY A 1 188 ? 20.184 13.566 13.500 1.00 32.67 ? 207 GLY A N 1 ATOM 1464 C CA . GLY A 1 188 ? 18.870 13.172 13.982 1.00 30.30 ? 207 GLY A CA 1 ATOM 1465 C C . GLY A 1 188 ? 18.769 12.043 14.991 1.00 30.63 ? 207 GLY A C 1 ATOM 1466 O O . GLY A 1 188 ? 17.663 11.591 15.295 1.00 29.11 ? 207 GLY A O 1 ATOM 1467 N N . GLU A 1 189 ? 19.903 11.581 15.512 1.00 27.79 ? 208 GLU A N 1 ATOM 1468 C CA . GLU A 1 189 ? 19.900 10.503 16.496 1.00 28.09 ? 208 GLU A CA 1 ATOM 1469 C C . GLU A 1 189 ? 20.647 10.942 17.750 1.00 25.96 ? 208 GLU A C 1 ATOM 1470 O O . GLU A 1 189 ? 21.556 11.763 17.678 1.00 23.28 ? 208 GLU A O 1 ATOM 1471 C CB . GLU A 1 189 ? 20.563 9.242 15.920 1.00 29.23 ? 208 GLU A CB 1 ATOM 1472 C CG . GLU A 1 189 ? 19.801 8.608 14.756 1.00 31.54 ? 208 GLU A CG 1 ATOM 1473 C CD . GLU A 1 189 ? 20.515 7.402 14.156 1.00 33.17 ? 208 GLU A CD 1 ATOM 1474 O OE1 . GLU A 1 189 ? 19.918 6.726 13.292 1.00 34.43 ? 208 GLU A OE1 1 ATOM 1475 O OE2 . GLU A 1 189 ? 21.670 7.130 14.542 1.00 33.82 ? 208 GLU A OE2 1 ATOM 1476 N N . MET A 1 190 ? 20.253 10.400 18.897 1.00 24.86 ? 209 MET A N 1 ATOM 1477 C CA . MET A 1 190 ? 20.919 10.734 20.151 1.00 23.46 ? 209 MET A CA 1 ATOM 1478 C C . MET A 1 190 ? 22.152 9.854 20.335 1.00 23.13 ? 209 MET A C 1 ATOM 1479 O O . MET A 1 190 ? 22.045 8.685 20.696 1.00 24.61 ? 209 MET A O 1 ATOM 1480 C CB . MET A 1 190 ? 19.972 10.540 21.331 1.00 23.40 ? 209 MET A CB 1 ATOM 1481 C CG . MET A 1 190 ? 20.624 10.824 22.681 1.00 23.85 ? 209 MET A CG 1 ATOM 1482 S SD . MET A 1 190 ? 19.447 10.677 24.019 1.00 26.72 ? 209 MET A SD 1 ATOM 1483 C CE . MET A 1 190 ? 19.075 8.960 23.943 1.00 26.86 ? 209 MET A CE 1 ATOM 1484 N N . HIS A 1 191 ? 23.324 10.427 20.091 1.00 22.12 ? 210 HIS A N 1 ATOM 1485 C CA . HIS A 1 191 ? 24.571 9.691 20.220 1.00 21.60 ? 210 HIS A CA 1 ATOM 1486 C C . HIS A 1 191 ? 25.232 9.907 21.575 1.00 20.81 ? 210 HIS A C 1 ATOM 1487 O O . HIS A 1 191 ? 26.115 9.151 21.969 1.00 20.82 ? 210 HIS A O 1 ATOM 1488 C CB . HIS A 1 191 ? 25.521 10.098 19.092 1.00 23.93 ? 210 HIS A CB 1 ATOM 1489 C CG . HIS A 1 191 ? 25.188 9.467 17.776 1.00 25.73 ? 210 HIS A CG 1 ATOM 1490 N ND1 . HIS A 1 191 ? 25.801 8.318 17.328 1.00 25.37 ? 210 HIS A ND1 1 ATOM 1491 C CD2 . HIS A 1 191 ? 24.255 9.782 16.847 1.00 25.65 ? 210 HIS A CD2 1 ATOM 1492 C CE1 . HIS A 1 191 ? 25.259 7.950 16.181 1.00 24.07 ? 210 HIS A CE1 1 ATOM 1493 N NE2 . HIS A 1 191 ? 24.319 8.821 15.867 1.00 27.21 ? 210 HIS A NE2 1 ATOM 1494 N N . GLY A 1 192 ? 24.798 10.934 22.294 1.00 19.87 ? 211 GLY A N 1 ATOM 1495 C CA . GLY A 1 192 ? 25.398 11.184 23.586 1.00 20.45 ? 211 GLY A CA 1 ATOM 1496 C C . GLY A 1 192 ? 24.484 11.761 24.642 1.00 20.05 ? 211 GLY A C 1 ATOM 1497 O O . GLY A 1 192 ? 23.391 12.260 24.354 1.00 20.39 ? 211 GLY A O 1 ATOM 1498 N N . ILE A 1 193 ? 24.945 11.657 25.884 1.00 18.91 ? 212 ILE A N 1 ATOM 1499 C CA . ILE A 1 193 ? 24.252 12.205 27.043 1.00 19.02 ? 212 ILE A CA 1 ATOM 1500 C C . ILE A 1 193 ? 25.310 13.110 27.657 1.00 17.35 ? 212 ILE A C 1 ATOM 1501 O O . ILE A 1 193 ? 26.410 12.650 27.947 1.00 19.56 ? 212 ILE A O 1 ATOM 1502 C CB . ILE A 1 193 ? 23.914 11.129 28.083 1.00 18.61 ? 212 ILE A CB 1 ATOM 1503 C CG1 . ILE A 1 193 ? 22.982 10.080 27.481 1.00 22.95 ? 212 ILE A CG1 1 ATOM 1504 C CG2 . ILE A 1 193 ? 23.275 11.780 29.301 1.00 15.63 ? 212 ILE A CG2 1 ATOM 1505 C CD1 . ILE A 1 193 ? 22.743 8.906 28.414 1.00 25.48 ? 212 ILE A CD1 1 ATOM 1506 N N . VAL A 1 194 ? 24.985 14.381 27.857 1.00 18.18 ? 213 VAL A N 1 ATOM 1507 C CA . VAL A 1 194 ? 25.945 15.325 28.427 1.00 17.11 ? 213 VAL A CA 1 ATOM 1508 C C . VAL A 1 194 ? 26.428 14.863 29.801 1.00 17.88 ? 213 VAL A C 1 ATOM 1509 O O . VAL A 1 194 ? 25.636 14.719 30.736 1.00 20.52 ? 213 VAL A O 1 ATOM 1510 C CB . VAL A 1 194 ? 25.334 16.732 28.588 1.00 18.01 ? 213 VAL A CB 1 ATOM 1511 C CG1 . VAL A 1 194 ? 26.373 17.690 29.174 1.00 18.23 ? 213 VAL A CG1 1 ATOM 1512 C CG2 . VAL A 1 194 ? 24.833 17.242 27.246 1.00 18.20 ? 213 VAL A CG2 1 ATOM 1513 N N . ALA A 1 195 ? 27.727 14.628 29.915 1.00 18.22 ? 214 ALA A N 1 ATOM 1514 C CA . ALA A 1 195 ? 28.307 14.201 31.182 1.00 20.32 ? 214 ALA A CA 1 ATOM 1515 C C . ALA A 1 195 ? 28.918 15.414 31.878 1.00 21.64 ? 214 ALA A C 1 ATOM 1516 O O . ALA A 1 195 ? 28.756 15.593 33.081 1.00 24.24 ? 214 ALA A O 1 ATOM 1517 C CB . ALA A 1 195 ? 29.365 13.128 30.938 1.00 18.78 ? 214 ALA A CB 1 ATOM 1518 N N . GLY A 1 196 ? 29.620 16.254 31.122 1.00 22.75 ? 215 GLY A N 1 ATOM 1519 C CA . GLY A 1 196 ? 30.209 17.432 31.728 1.00 23.13 ? 215 GLY A CA 1 ATOM 1520 C C . GLY A 1 196 ? 31.488 17.920 31.083 1.00 24.27 ? 215 GLY A C 1 ATOM 1521 O O . GLY A 1 196 ? 32.140 17.197 30.329 1.00 23.93 ? 215 GLY A O 1 ATOM 1522 N N . GLY A 1 197 ? 31.839 19.163 31.390 1.00 25.08 ? 216 GLY A N 1 ATOM 1523 C CA . GLY A 1 197 ? 33.045 19.759 30.847 1.00 27.34 ? 216 GLY A CA 1 ATOM 1524 C C . GLY A 1 197 ? 33.761 20.574 31.905 1.00 28.37 ? 216 GLY A C 1 ATOM 1525 O O . GLY A 1 197 ? 33.722 20.230 33.085 1.00 29.05 ? 216 GLY A O 1 ATOM 1526 N N . SER A 1 198 ? 34.397 21.666 31.492 1.00 28.36 ? 217 SER A N 1 ATOM 1527 C CA . SER A 1 198 ? 35.135 22.515 32.416 1.00 29.48 ? 217 SER A CA 1 ATOM 1528 C C . SER A 1 198 ? 34.402 23.807 32.779 1.00 32.29 ? 217 SER A C 1 ATOM 1529 O O . SER A 1 198 ? 33.514 24.263 32.054 1.00 31.08 ? 217 SER A O 1 ATOM 1530 C CB . SER A 1 198 ? 36.505 22.858 31.821 1.00 30.61 ? 217 SER A CB 1 ATOM 1531 O OG . SER A 1 198 ? 37.240 21.686 31.503 1.00 29.64 ? 217 SER A OG 1 ATOM 1532 N N . GLU A 1 199 ? 34.790 24.389 33.910 1.00 33.43 ? 218 GLU A N 1 ATOM 1533 C CA . GLU A 1 199 ? 34.198 25.630 34.392 1.00 35.88 ? 218 GLU A CA 1 ATOM 1534 C C . GLU A 1 199 ? 35.267 26.712 34.498 1.00 36.95 ? 218 GLU A C 1 ATOM 1535 O O . GLU A 1 199 ? 36.298 26.516 35.137 1.00 36.70 ? 218 GLU A O 1 ATOM 1536 C CB . GLU A 1 199 ? 33.558 25.415 35.765 1.00 38.86 ? 218 GLU A CB 1 ATOM 1537 C CG . GLU A 1 199 ? 32.347 24.493 35.753 1.00 43.22 ? 218 GLU A CG 1 ATOM 1538 C CD . GLU A 1 199 ? 31.150 25.108 35.058 1.00 45.16 ? 218 GLU A CD 1 ATOM 1539 O OE1 . GLU A 1 199 ? 31.285 25.519 33.886 1.00 46.43 ? 218 GLU A OE1 1 ATOM 1540 O OE2 . GLU A 1 199 ? 30.071 25.180 35.687 1.00 47.87 ? 218 GLU A OE2 1 ATOM 1541 N N . PRO A 1 200 ? 35.040 27.866 33.850 1.00 37.01 ? 219 PRO A N 1 ATOM 1542 C CA . PRO A 1 200 ? 33.840 28.140 33.054 1.00 35.65 ? 219 PRO A CA 1 ATOM 1543 C C . PRO A 1 200 ? 33.832 27.313 31.775 1.00 34.79 ? 219 PRO A C 1 ATOM 1544 O O . PRO A 1 200 ? 34.861 26.785 31.363 1.00 32.57 ? 219 PRO A O 1 ATOM 1545 C CB . PRO A 1 200 ? 33.947 29.635 32.779 1.00 36.78 ? 219 PRO A CB 1 ATOM 1546 C CG . PRO A 1 200 ? 35.427 29.841 32.686 1.00 37.46 ? 219 PRO A CG 1 ATOM 1547 C CD . PRO A 1 200 ? 35.936 29.035 33.864 1.00 36.43 ? 219 PRO A CD 1 ATOM 1548 N N . CYS A 1 201 ? 32.665 27.205 31.152 1.00 33.61 ? 220 CYS A N 1 ATOM 1549 C CA . CYS A 1 201 ? 32.526 26.437 29.923 1.00 33.94 ? 220 CYS A CA 1 ATOM 1550 C C . CYS A 1 201 ? 32.975 27.243 28.707 1.00 32.99 ? 220 CYS A C 1 ATOM 1551 O O . CYS A 1 201 ? 33.114 28.465 28.771 1.00 33.38 ? 220 CYS A O 1 ATOM 1552 C CB . CYS A 1 201 ? 31.067 26.006 29.744 1.00 34.11 ? 220 CYS A CB 1 ATOM 1553 S SG . CYS A 1 201 ? 29.885 27.389 29.755 1.00 35.48 ? 220 CYS A SG 1 ATOM 1554 N N . GLY A 1 202 ? 33.218 26.543 27.607 1.00 32.11 ? 221 GLY A N 1 ATOM 1555 C CA . GLY A 1 202 ? 33.628 27.203 26.381 1.00 32.79 ? 221 GLY A CA 1 ATOM 1556 C C . GLY A 1 202 ? 35.077 27.647 26.301 1.00 33.67 ? 221 GLY A C 1 ATOM 1557 O O . GLY A 1 202 ? 35.437 28.406 25.400 1.00 33.60 ? 221 GLY A O 1 ATOM 1558 N N . GLN A 1 203 A 35.913 27.189 27.229 1.00 32.97 ? 221 GLN A N 1 ATOM 1559 C CA . GLN A 1 203 A 37.324 27.564 27.204 1.00 33.56 ? 221 GLN A CA 1 ATOM 1560 C C . GLN A 1 203 A 38.032 26.932 26.016 1.00 33.69 ? 221 GLN A C 1 ATOM 1561 O O . GLN A 1 203 A 37.644 25.867 25.540 1.00 33.33 ? 221 GLN A O 1 ATOM 1562 C CB . GLN A 1 203 A 38.038 27.111 28.476 1.00 32.59 ? 221 GLN A CB 1 ATOM 1563 C CG . GLN A 1 203 A 37.652 27.844 29.732 1.00 33.44 ? 221 GLN A CG 1 ATOM 1564 C CD . GLN A 1 203 A 38.399 27.303 30.929 1.00 35.62 ? 221 GLN A CD 1 ATOM 1565 O OE1 . GLN A 1 203 A 39.632 27.248 30.931 1.00 35.30 ? 221 GLN A OE1 1 ATOM 1566 N NE2 . GLN A 1 203 A 37.660 26.891 31.951 1.00 33.74 ? 221 GLN A NE2 1 ATOM 1567 N N . HIS A 1 204 ? 39.080 27.600 25.552 1.00 34.99 ? 222 HIS A N 1 ATOM 1568 C CA . HIS A 1 204 ? 39.881 27.120 24.435 1.00 35.50 ? 222 HIS A CA 1 ATOM 1569 C C . HIS A 1 204 ? 40.514 25.781 24.815 1.00 33.86 ? 222 HIS A C 1 ATOM 1570 O O . HIS A 1 204 ? 40.969 25.603 25.943 1.00 34.28 ? 222 HIS A O 1 ATOM 1571 C CB . HIS A 1 204 ? 40.969 28.156 24.119 1.00 39.29 ? 222 HIS A CB 1 ATOM 1572 C CG . HIS A 1 204 ? 41.952 27.720 23.077 1.00 42.51 ? 222 HIS A CG 1 ATOM 1573 N ND1 . HIS A 1 204 ? 41.572 27.310 21.816 1.00 45.12 ? 222 HIS A ND1 1 ATOM 1574 C CD2 . HIS A 1 204 ? 43.306 27.669 23.096 1.00 43.96 ? 222 HIS A CD2 1 ATOM 1575 C CE1 . HIS A 1 204 ? 42.649 27.027 21.104 1.00 45.74 ? 222 HIS A CE1 1 ATOM 1576 N NE2 . HIS A 1 204 ? 43.714 27.237 21.857 1.00 44.60 ? 222 HIS A NE2 1 ATOM 1577 N N . LEU A 1 205 ? 40.520 24.840 23.875 1.00 32.20 ? 223 LEU A N 1 ATOM 1578 C CA . LEU A 1 205 ? 41.109 23.520 24.093 1.00 33.59 ? 223 LEU A CA 1 ATOM 1579 C C . LEU A 1 205 ? 40.469 22.684 25.203 1.00 32.63 ? 223 LEU A C 1 ATOM 1580 O O . LEU A 1 205 ? 41.095 21.755 25.719 1.00 30.69 ? 223 LEU A O 1 ATOM 1581 C CB . LEU A 1 205 ? 42.607 23.661 24.381 1.00 35.51 ? 223 LEU A CB 1 ATOM 1582 C CG . LEU A 1 205 ? 43.419 24.399 23.314 1.00 37.01 ? 223 LEU A CG 1 ATOM 1583 C CD1 . LEU A 1 205 ? 44.855 24.562 23.781 1.00 38.40 ? 223 LEU A CD1 1 ATOM 1584 C CD2 . LEU A 1 205 ? 43.363 23.627 22.007 1.00 37.78 ? 223 LEU A CD2 1 ATOM 1585 N N . LYS A 1 206 ? 39.232 22.998 25.573 1.00 31.19 ? 224 LYS A N 1 ATOM 1586 C CA . LYS A 1 206 ? 38.568 22.239 26.625 1.00 29.06 ? 224 LYS A CA 1 ATOM 1587 C C . LYS A 1 206 ? 37.180 21.727 26.250 1.00 26.45 ? 224 LYS A C 1 ATOM 1588 O O . LYS A 1 206 ? 36.166 22.225 26.730 1.00 29.15 ? 224 LYS A O 1 ATOM 1589 C CB . LYS A 1 206 ? 38.496 23.067 27.910 1.00 31.16 ? 224 LYS A CB 1 ATOM 1590 C CG . LYS A 1 206 ? 39.861 23.286 28.557 1.00 32.23 ? 224 LYS A CG 1 ATOM 1591 C CD . LYS A 1 206 ? 39.773 24.079 29.851 1.00 33.63 ? 224 LYS A CD 1 ATOM 1592 C CE . LYS A 1 206 ? 41.158 24.250 30.469 1.00 34.48 ? 224 LYS A CE 1 ATOM 1593 N NZ . LYS A 1 206 ? 41.132 25.058 31.714 1.00 37.48 ? 224 LYS A NZ 1 ATOM 1594 N N . PRO A 1 207 ? 37.126 20.715 25.378 1.00 25.25 ? 225 PRO A N 1 ATOM 1595 C CA . PRO A 1 207 ? 35.861 20.125 24.941 1.00 24.67 ? 225 PRO A CA 1 ATOM 1596 C C . PRO A 1 207 ? 35.221 19.385 26.119 1.00 24.73 ? 225 PRO A C 1 ATOM 1597 O O . PRO A 1 207 ? 35.857 19.197 27.159 1.00 24.03 ? 225 PRO A O 1 ATOM 1598 C CB . PRO A 1 207 ? 36.290 19.189 23.819 1.00 24.21 ? 225 PRO A CB 1 ATOM 1599 C CG . PRO A 1 207 ? 37.668 18.760 24.256 1.00 25.18 ? 225 PRO A CG 1 ATOM 1600 C CD . PRO A 1 207 ? 38.272 20.052 24.730 1.00 25.60 ? 225 PRO A CD 1 ATOM 1601 N N . ALA A 1 208 ? 33.967 18.976 25.960 1.00 24.38 ? 226 ALA A N 1 ATOM 1602 C CA . ALA A 1 208 ? 33.260 18.277 27.028 1.00 23.17 ? 226 ALA A CA 1 ATOM 1603 C C . ALA A 1 208 ? 33.074 16.784 26.758 1.00 22.80 ? 226 ALA A C 1 ATOM 1604 O O . ALA A 1 208 ? 33.341 16.292 25.656 1.00 21.37 ? 226 ALA A O 1 ATOM 1605 C CB . ALA A 1 208 ? 31.912 18.945 27.281 1.00 21.13 ? 226 ALA A CB 1 ATOM 1606 N N . VAL A 1 209 ? 32.617 16.069 27.787 1.00 21.71 ? 227 VAL A N 1 ATOM 1607 C CA . VAL A 1 209 ? 32.411 14.628 27.711 1.00 20.35 ? 227 VAL A CA 1 ATOM 1608 C C . VAL A 1 209 ? 30.941 14.252 27.601 1.00 19.02 ? 227 VAL A C 1 ATOM 1609 O O . VAL A 1 209 ? 30.098 14.774 28.328 1.00 18.99 ? 227 VAL A O 1 ATOM 1610 C CB . VAL A 1 209 ? 32.994 13.924 28.963 1.00 22.03 ? 227 VAL A CB 1 ATOM 1611 C CG1 . VAL A 1 209 ? 32.825 12.415 28.843 1.00 21.69 ? 227 VAL A CG1 1 ATOM 1612 C CG2 . VAL A 1 209 ? 34.458 14.285 29.119 1.00 23.91 ? 227 VAL A CG2 1 ATOM 1613 N N . TYR A 1 210 ? 30.651 13.330 26.692 1.00 19.28 ? 228 TYR A N 1 ATOM 1614 C CA . TYR A 1 210 ? 29.292 12.860 26.463 1.00 19.88 ? 228 TYR A CA 1 ATOM 1615 C C . TYR A 1 210 ? 29.284 11.341 26.495 1.00 18.91 ? 228 TYR A C 1 ATOM 1616 O O . TYR A 1 210 ? 30.064 10.692 25.805 1.00 19.15 ? 228 TYR A O 1 ATOM 1617 C CB . TYR A 1 210 ? 28.779 13.347 25.099 1.00 20.91 ? 228 TYR A CB 1 ATOM 1618 C CG . TYR A 1 210 ? 28.801 14.849 24.948 1.00 20.30 ? 228 TYR A CG 1 ATOM 1619 C CD1 . TYR A 1 210 ? 29.997 15.530 24.691 1.00 20.50 ? 228 TYR A CD1 1 ATOM 1620 C CD2 . TYR A 1 210 ? 27.640 15.602 25.133 1.00 20.33 ? 228 TYR A CD2 1 ATOM 1621 C CE1 . TYR A 1 210 ? 30.034 16.920 24.632 1.00 19.78 ? 228 TYR A CE1 1 ATOM 1622 C CE2 . TYR A 1 210 ? 27.667 16.990 25.079 1.00 20.55 ? 228 TYR A CE2 1 ATOM 1623 C CZ . TYR A 1 210 ? 28.870 17.642 24.832 1.00 20.39 ? 228 TYR A CZ 1 ATOM 1624 O OH . TYR A 1 210 ? 28.909 19.015 24.827 1.00 22.03 ? 228 TYR A OH 1 ATOM 1625 N N . THR A 1 211 ? 28.409 10.772 27.315 1.00 20.43 ? 229 THR A N 1 ATOM 1626 C CA . THR A 1 211 ? 28.312 9.328 27.402 1.00 21.47 ? 229 THR A CA 1 ATOM 1627 C C . THR A 1 211 ? 27.886 8.818 26.025 1.00 22.81 ? 229 THR A C 1 ATOM 1628 O O . THR A 1 211 ? 26.935 9.336 25.431 1.00 22.69 ? 229 THR A O 1 ATOM 1629 C CB . THR A 1 211 ? 27.290 8.934 28.479 1.00 21.25 ? 229 THR A CB 1 ATOM 1630 O OG1 . THR A 1 211 ? 27.695 9.517 29.723 1.00 20.94 ? 229 THR A OG1 1 ATOM 1631 C CG2 . THR A 1 211 ? 27.217 7.419 28.634 1.00 22.88 ? 229 THR A CG2 1 ATOM 1632 N N . LYS A 1 212 ? 28.602 7.820 25.514 1.00 21.91 ? 230 LYS A N 1 ATOM 1633 C CA . LYS A 1 212 ? 28.318 7.266 24.192 1.00 23.59 ? 230 LYS A CA 1 ATOM 1634 C C . LYS A 1 212 ? 27.136 6.305 24.216 1.00 22.09 ? 230 LYS A C 1 ATOM 1635 O O . LYS A 1 212 ? 27.293 5.122 24.492 1.00 23.26 ? 230 LYS A O 1 ATOM 1636 C CB . LYS A 1 212 ? 29.568 6.560 23.642 1.00 24.70 ? 230 LYS A CB 1 ATOM 1637 C CG . LYS A 1 212 ? 29.440 6.119 22.188 1.00 26.48 ? 230 LYS A CG 1 ATOM 1638 C CD . LYS A 1 212 ? 30.733 5.509 21.672 1.00 29.07 ? 230 LYS A CD 1 ATOM 1639 C CE . LYS A 1 212 ? 30.610 5.113 20.205 1.00 31.36 ? 230 LYS A CE 1 ATOM 1640 N NZ . LYS A 1 212 ? 31.810 4.374 19.729 1.00 33.10 ? 230 LYS A NZ 1 ATOM 1641 N N . VAL A 1 213 ? 25.955 6.831 23.901 1.00 22.12 ? 231 VAL A N 1 ATOM 1642 C CA . VAL A 1 213 ? 24.711 6.064 23.914 1.00 22.67 ? 231 VAL A CA 1 ATOM 1643 C C . VAL A 1 213 ? 24.685 4.753 23.122 1.00 22.80 ? 231 VAL A C 1 ATOM 1644 O O . VAL A 1 213 ? 24.127 3.758 23.588 1.00 21.56 ? 231 VAL A O 1 ATOM 1645 C CB . VAL A 1 213 ? 23.532 6.953 23.450 1.00 20.84 ? 231 VAL A CB 1 ATOM 1646 C CG1 . VAL A 1 213 ? 22.237 6.148 23.425 1.00 22.50 ? 231 VAL A CG1 1 ATOM 1647 C CG2 . VAL A 1 213 ? 23.394 8.145 24.394 1.00 21.31 ? 231 VAL A CG2 1 ATOM 1648 N N . PHE A 1 214 ? 25.280 4.749 21.936 1.00 24.60 ? 232 PHE A N 1 ATOM 1649 C CA . PHE A 1 214 ? 25.302 3.547 21.099 1.00 26.13 ? 232 PHE A CA 1 ATOM 1650 C C . PHE A 1 214 ? 25.744 2.321 21.892 1.00 27.49 ? 232 PHE A C 1 ATOM 1651 O O . PHE A 1 214 ? 25.138 1.254 21.793 1.00 26.85 ? 232 PHE A O 1 ATOM 1652 C CB . PHE A 1 214 ? 26.247 3.746 19.910 1.00 28.99 ? 232 PHE A CB 1 ATOM 1653 C CG . PHE A 1 214 ? 26.321 2.559 18.989 1.00 32.72 ? 232 PHE A CG 1 ATOM 1654 C CD1 . PHE A 1 214 ? 25.247 2.234 18.164 1.00 32.98 ? 232 PHE A CD1 1 ATOM 1655 C CD2 . PHE A 1 214 ? 27.459 1.759 18.954 1.00 32.88 ? 232 PHE A CD2 1 ATOM 1656 C CE1 . PHE A 1 214 ? 25.305 1.125 17.315 1.00 34.53 ? 232 PHE A CE1 1 ATOM 1657 C CE2 . PHE A 1 214 ? 27.527 0.649 18.110 1.00 33.56 ? 232 PHE A CE2 1 ATOM 1658 C CZ . PHE A 1 214 ? 26.447 0.333 17.289 1.00 34.02 ? 232 PHE A CZ 1 ATOM 1659 N N . ASP A 1 215 ? 26.803 2.480 22.679 1.00 28.84 ? 233 ASP A N 1 ATOM 1660 C CA . ASP A 1 215 ? 27.335 1.386 23.486 1.00 28.55 ? 233 ASP A CA 1 ATOM 1661 C C . ASP A 1 215 ? 26.332 0.848 24.499 1.00 27.87 ? 233 ASP A C 1 ATOM 1662 O O . ASP A 1 215 ? 26.426 -0.308 24.912 1.00 28.93 ? 233 ASP A O 1 ATOM 1663 C CB . ASP A 1 215 ? 28.599 1.843 24.224 1.00 30.63 ? 233 ASP A CB 1 ATOM 1664 C CG . ASP A 1 215 ? 29.818 1.905 23.320 1.00 31.04 ? 233 ASP A CG 1 ATOM 1665 O OD1 . ASP A 1 215 ? 29.658 2.135 22.106 1.00 32.72 ? 233 ASP A OD1 1 ATOM 1666 O OD2 . ASP A 1 215 ? 30.945 1.740 23.830 1.00 33.87 ? 233 ASP A OD2 1 ATOM 1667 N N . TYR A 1 216 ? 25.375 1.682 24.896 1.00 26.35 ? 234 TYR A N 1 ATOM 1668 C CA . TYR A 1 216 ? 24.370 1.279 25.874 1.00 25.44 ? 234 TYR A CA 1 ATOM 1669 C C . TYR A 1 216 ? 23.007 0.887 25.300 1.00 24.91 ? 234 TYR A C 1 ATOM 1670 O O . TYR A 1 216 ? 22.075 0.633 26.063 1.00 26.16 ? 234 TYR A O 1 ATOM 1671 C CB . TYR A 1 216 ? 24.160 2.394 26.902 1.00 23.33 ? 234 TYR A CB 1 ATOM 1672 C CG . TYR A 1 216 ? 25.387 2.723 27.728 1.00 23.80 ? 234 TYR A CG 1 ATOM 1673 C CD1 . TYR A 1 216 ? 26.384 3.564 27.233 1.00 22.25 ? 234 TYR A CD1 1 ATOM 1674 C CD2 . TYR A 1 216 ? 25.557 2.178 29.001 1.00 22.75 ? 234 TYR A CD2 1 ATOM 1675 C CE1 . TYR A 1 216 ? 27.521 3.854 27.985 1.00 22.31 ? 234 TYR A CE1 1 ATOM 1676 C CE2 . TYR A 1 216 ? 26.688 2.459 29.760 1.00 24.26 ? 234 TYR A CE2 1 ATOM 1677 C CZ . TYR A 1 216 ? 27.666 3.296 29.247 1.00 24.23 ? 234 TYR A CZ 1 ATOM 1678 O OH . TYR A 1 216 ? 28.789 3.574 29.993 1.00 23.52 ? 234 TYR A OH 1 ATOM 1679 N N . ASN A 1 217 ? 22.879 0.842 23.976 1.00 26.65 ? 235 ASN A N 1 ATOM 1680 C CA . ASN A 1 217 ? 21.599 0.486 23.359 1.00 26.64 ? 235 ASN A CA 1 ATOM 1681 C C . ASN A 1 217 ? 20.987 -0.795 23.918 1.00 28.09 ? 235 ASN A C 1 ATOM 1682 O O . ASN A 1 217 ? 19.817 -0.807 24.305 1.00 29.04 ? 235 ASN A O 1 ATOM 1683 C CB . ASN A 1 217 ? 21.739 0.352 21.836 1.00 26.10 ? 235 ASN A CB 1 ATOM 1684 C CG . ASN A 1 217 ? 21.711 1.693 21.123 1.00 27.14 ? 235 ASN A CG 1 ATOM 1685 O OD1 . ASN A 1 217 ? 21.313 2.706 21.697 1.00 24.24 ? 235 ASN A OD1 1 ATOM 1686 N ND2 . ASN A 1 217 ? 22.119 1.701 19.858 1.00 26.83 ? 235 ASN A ND2 1 ATOM 1687 N N . ASN A 1 218 ? 21.773 -1.868 23.965 1.00 29.35 ? 236 ASN A N 1 ATOM 1688 C CA . ASN A 1 218 ? 21.280 -3.145 24.475 1.00 30.97 ? 236 ASN A CA 1 ATOM 1689 C C . ASN A 1 218 ? 20.802 -3.049 25.924 1.00 29.64 ? 236 ASN A C 1 ATOM 1690 O O . ASN A 1 218 ? 19.751 -3.588 26.272 1.00 29.29 ? 236 ASN A O 1 ATOM 1691 C CB . ASN A 1 218 ? 22.361 -4.229 24.361 1.00 34.87 ? 236 ASN A CB 1 ATOM 1692 C CG . ASN A 1 218 ? 22.800 -4.477 22.923 1.00 40.45 ? 236 ASN A CG 1 ATOM 1693 O OD1 . ASN A 1 218 ? 21.975 -4.546 22.007 1.00 42.81 ? 236 ASN A OD1 1 ATOM 1694 N ND2 . ASN A 1 218 ? 24.107 -4.631 22.723 1.00 42.12 ? 236 ASN A ND2 1 ATOM 1695 N N . TRP A 1 219 ? 21.575 -2.368 26.767 1.00 28.30 ? 237 TRP A N 1 ATOM 1696 C CA . TRP A 1 219 ? 21.216 -2.201 28.172 1.00 27.22 ? 237 TRP A CA 1 ATOM 1697 C C . TRP A 1 219 ? 19.905 -1.421 28.287 1.00 28.03 ? 237 TRP A C 1 ATOM 1698 O O . TRP A 1 219 ? 19.014 -1.791 29.055 1.00 27.40 ? 237 TRP A O 1 ATOM 1699 C CB . TRP A 1 219 ? 22.328 -1.452 28.920 1.00 27.14 ? 237 TRP A CB 1 ATOM 1700 C CG . TRP A 1 219 ? 22.030 -1.200 30.376 1.00 26.25 ? 237 TRP A CG 1 ATOM 1701 C CD1 . TRP A 1 219 ? 22.013 -2.121 31.386 1.00 26.70 ? 237 TRP A CD1 1 ATOM 1702 C CD2 . TRP A 1 219 ? 21.689 0.057 30.974 1.00 26.18 ? 237 TRP A CD2 1 ATOM 1703 N NE1 . TRP A 1 219 ? 21.682 -1.515 32.577 1.00 26.10 ? 237 TRP A NE1 1 ATOM 1704 C CE2 . TRP A 1 219 ? 21.477 -0.178 32.352 1.00 26.57 ? 237 TRP A CE2 1 ATOM 1705 C CE3 . TRP A 1 219 ? 21.539 1.361 30.480 1.00 26.32 ? 237 TRP A CE3 1 ATOM 1706 C CZ2 . TRP A 1 219 ? 21.124 0.846 33.244 1.00 27.19 ? 237 TRP A CZ2 1 ATOM 1707 C CZ3 . TRP A 1 219 ? 21.186 2.383 31.371 1.00 26.66 ? 237 TRP A CZ3 1 ATOM 1708 C CH2 . TRP A 1 219 ? 20.984 2.114 32.735 1.00 24.11 ? 237 TRP A CH2 1 ATOM 1709 N N . ILE A 1 220 ? 19.796 -0.342 27.517 1.00 27.32 ? 238 ILE A N 1 ATOM 1710 C CA . ILE A 1 220 ? 18.598 0.491 27.524 1.00 27.42 ? 238 ILE A CA 1 ATOM 1711 C C . ILE A 1 220 ? 17.362 -0.290 27.073 1.00 29.00 ? 238 ILE A C 1 ATOM 1712 O O . ILE A 1 220 ? 16.324 -0.264 27.736 1.00 27.24 ? 238 ILE A O 1 ATOM 1713 C CB . ILE A 1 220 ? 18.766 1.715 26.598 1.00 27.82 ? 238 ILE A CB 1 ATOM 1714 C CG1 . ILE A 1 220 ? 19.866 2.634 27.139 1.00 27.20 ? 238 ILE A CG1 1 ATOM 1715 C CG2 . ILE A 1 220 ? 17.443 2.471 26.492 1.00 26.47 ? 238 ILE A CG2 1 ATOM 1716 C CD1 . ILE A 1 220 ? 20.290 3.718 26.164 1.00 28.19 ? 238 ILE A CD1 1 ATOM 1717 N N . GLN A 1 221 ? 17.475 -0.978 25.942 1.00 30.03 ? 239 GLN A N 1 ATOM 1718 C CA . GLN A 1 221 ? 16.359 -1.757 25.420 1.00 34.12 ? 239 GLN A CA 1 ATOM 1719 C C . GLN A 1 221 ? 15.921 -2.835 26.403 1.00 34.16 ? 239 GLN A C 1 ATOM 1720 O O . GLN A 1 221 ? 14.725 -3.055 26.609 1.00 34.31 ? 239 GLN A O 1 ATOM 1721 C CB . GLN A 1 221 ? 16.742 -2.402 24.087 1.00 36.60 ? 239 GLN A CB 1 ATOM 1722 C CG . GLN A 1 221 ? 16.790 -1.433 22.919 1.00 41.46 ? 239 GLN A CG 1 ATOM 1723 C CD . GLN A 1 221 ? 17.339 -2.076 21.665 1.00 45.02 ? 239 GLN A CD 1 ATOM 1724 O OE1 . GLN A 1 221 ? 16.849 -3.114 21.218 1.00 48.22 ? 239 GLN A OE1 1 ATOM 1725 N NE2 . GLN A 1 221 ? 18.364 -1.461 21.086 1.00 47.73 ? 239 GLN A NE2 1 ATOM 1726 N N . SER A 1 222 ? 16.899 -3.505 27.004 1.00 34.19 ? 240 SER A N 1 ATOM 1727 C CA . SER A 1 222 ? 16.629 -4.564 27.966 1.00 34.50 ? 240 SER A CA 1 ATOM 1728 C C . SER A 1 222 ? 15.871 -4.034 29.179 1.00 33.28 ? 240 SER A C 1 ATOM 1729 O O . SER A 1 222 ? 14.841 -4.590 29.565 1.00 33.79 ? 240 SER A O 1 ATOM 1730 C CB . SER A 1 222 ? 17.942 -5.209 28.424 1.00 34.74 ? 240 SER A CB 1 ATOM 1731 O OG . SER A 1 222 ? 18.625 -5.805 27.333 1.00 38.95 ? 240 SER A OG 1 ATOM 1732 N N . ILE A 1 223 ? 16.389 -2.963 29.777 1.00 32.14 ? 241 ILE A N 1 ATOM 1733 C CA . ILE A 1 223 ? 15.767 -2.356 30.951 1.00 32.29 ? 241 ILE A CA 1 ATOM 1734 C C . ILE A 1 223 ? 14.316 -1.991 30.661 1.00 33.44 ? 241 ILE A C 1 ATOM 1735 O O . ILE A 1 223 ? 13.416 -2.337 31.422 1.00 33.32 ? 241 ILE A O 1 ATOM 1736 C CB . ILE A 1 223 ? 16.525 -1.075 31.395 1.00 32.00 ? 241 ILE A CB 1 ATOM 1737 C CG1 . ILE A 1 223 ? 17.938 -1.433 31.868 1.00 31.84 ? 241 ILE A CG1 1 ATOM 1738 C CG2 . ILE A 1 223 ? 15.754 -0.364 32.505 1.00 31.90 ? 241 ILE A CG2 1 ATOM 1739 C CD1 . ILE A 1 223 ? 17.982 -2.297 33.118 1.00 31.96 ? 241 ILE A CD1 1 ATOM 1740 N N . ILE A 1 224 ? 14.092 -1.286 29.558 1.00 34.41 ? 242 ILE A N 1 ATOM 1741 C CA . ILE A 1 224 ? 12.742 -0.891 29.185 1.00 35.79 ? 242 ILE A CA 1 ATOM 1742 C C . ILE A 1 224 ? 11.877 -2.126 28.949 1.00 37.34 ? 242 ILE A C 1 ATOM 1743 O O . ILE A 1 224 ? 10.685 -2.127 29.259 1.00 37.59 ? 242 ILE A O 1 ATOM 1744 C CB . ILE A 1 224 ? 12.753 -0.015 27.908 1.00 35.15 ? 242 ILE A CB 1 ATOM 1745 C CG1 . ILE A 1 224 ? 13.426 1.327 28.211 1.00 35.04 ? 242 ILE A CG1 1 ATOM 1746 C CG2 . ILE A 1 224 ? 11.333 0.202 27.403 1.00 35.78 ? 242 ILE A CG2 1 ATOM 1747 C CD1 . ILE A 1 224 ? 13.483 2.278 27.024 1.00 35.18 ? 242 ILE A CD1 1 ATOM 1748 N N . ALA A 1 225 ? 12.489 -3.179 28.415 1.00 39.15 ? 243 ALA A N 1 ATOM 1749 C CA . ALA A 1 225 ? 11.783 -4.425 28.123 1.00 40.80 ? 243 ALA A CA 1 ATOM 1750 C C . ALA A 1 225 ? 11.325 -5.163 29.379 1.00 42.81 ? 243 ALA A C 1 ATOM 1751 O O . ALA A 1 225 ? 10.563 -6.128 29.296 1.00 43.17 ? 243 ALA A O 1 ATOM 1752 C CB . ALA A 1 225 ? 12.667 -5.334 27.279 1.00 39.85 ? 243 ALA A CB 1 ATOM 1753 N N . GLY A 1 226 ? 11.793 -4.716 30.539 1.00 43.93 ? 244 GLY A N 1 ATOM 1754 C CA . GLY A 1 226 ? 11.398 -5.353 31.781 1.00 46.84 ? 244 GLY A CA 1 ATOM 1755 C C . GLY A 1 226 ? 12.500 -6.146 32.456 1.00 48.24 ? 244 GLY A C 1 ATOM 1756 O O . GLY A 1 226 ? 12.310 -6.664 33.558 1.00 48.65 ? 244 GLY A O 1 ATOM 1757 N N . ASN A 1 227 ? 13.652 -6.251 31.801 1.00 49.20 ? 245 ASN A N 1 ATOM 1758 C CA . ASN A 1 227 ? 14.773 -6.988 32.367 1.00 50.61 ? 245 ASN A CA 1 ATOM 1759 C C . ASN A 1 227 ? 15.358 -6.180 33.521 1.00 50.67 ? 245 ASN A C 1 ATOM 1760 O O . ASN A 1 227 ? 15.573 -4.972 33.398 1.00 50.59 ? 245 ASN A O 1 ATOM 1761 C CB . ASN A 1 227 ? 15.845 -7.228 31.300 1.00 53.63 ? 245 ASN A CB 1 ATOM 1762 C CG . ASN A 1 227 ? 16.895 -8.232 31.743 1.00 57.68 ? 245 ASN A CG 1 ATOM 1763 O OD1 . ASN A 1 227 ? 17.497 -8.082 32.807 1.00 57.02 ? 245 ASN A OD1 1 ATOM 1764 N ND2 . ASN A 1 227 ? 17.118 -9.256 30.923 1.00 62.07 ? 245 ASN A ND2 1 ATOM 1765 N N . ARG A 1 228 A 15.609 -6.844 34.644 1.00 50.18 ? 245 ARG A N 1 ATOM 1766 C CA . ARG A 1 228 A 16.159 -6.168 35.813 1.00 49.45 ? 245 ARG A CA 1 ATOM 1767 C C . ARG A 1 228 A 17.443 -6.824 36.316 1.00 48.91 ? 245 ARG A C 1 ATOM 1768 O O . ARG A 1 228 A 17.859 -6.600 37.453 1.00 48.75 ? 245 ARG A O 1 ATOM 1769 C CB . ARG A 1 228 A 15.114 -6.136 36.931 1.00 49.47 ? 245 ARG A CB 1 ATOM 1770 C CG . ARG A 1 228 A 13.889 -5.284 36.611 1.00 49.80 ? 245 ARG A CG 1 ATOM 1771 C CD . ARG A 1 228 A 14.216 -3.797 36.660 1.00 49.91 ? 245 ARG A CD 1 ATOM 1772 N NE . ARG A 1 228 A 13.090 -2.963 36.243 1.00 49.76 ? 245 ARG A NE 1 ATOM 1773 C CZ . ARG A 1 228 A 12.698 -2.810 34.982 1.00 49.54 ? 245 ARG A CZ 1 ATOM 1774 N NH1 . ARG A 1 228 A 13.341 -3.431 34.001 1.00 49.45 ? 245 ARG A NH1 1 ATOM 1775 N NH2 . ARG A 1 228 A 11.661 -2.033 34.700 1.00 49.24 ? 245 ARG A NH2 1 ATOM 1776 N N . THR A 1 229 B 18.070 -7.630 35.463 1.00 48.02 ? 245 THR A N 1 ATOM 1777 C CA . THR A 1 229 B 19.308 -8.312 35.827 1.00 47.18 ? 245 THR A CA 1 ATOM 1778 C C . THR A 1 229 B 20.410 -8.049 34.807 1.00 45.32 ? 245 THR A C 1 ATOM 1779 O O . THR A 1 229 B 21.570 -8.387 35.034 1.00 45.17 ? 245 THR A O 1 ATOM 1780 C CB . THR A 1 229 B 19.100 -9.835 35.937 1.00 48.27 ? 245 THR A CB 1 ATOM 1781 O OG1 . THR A 1 229 B 18.714 -10.358 34.660 1.00 50.13 ? 245 THR A OG1 1 ATOM 1782 C CG2 . THR A 1 229 B 18.019 -10.151 36.964 1.00 48.83 ? 245 THR A CG2 1 ATOM 1783 N N . VAL A 1 230 C 20.042 -7.450 33.680 1.00 43.26 ? 245 VAL A N 1 ATOM 1784 C CA . VAL A 1 230 C 21.009 -7.137 32.635 1.00 40.72 ? 245 VAL A CA 1 ATOM 1785 C C . VAL A 1 230 C 22.016 -6.113 33.162 1.00 39.39 ? 245 VAL A C 1 ATOM 1786 O O . VAL A 1 230 C 21.687 -5.302 34.030 1.00 39.34 ? 245 VAL A O 1 ATOM 1787 C CB . VAL A 1 230 C 20.299 -6.572 31.381 1.00 40.84 ? 245 VAL A CB 1 ATOM 1788 C CG1 . VAL A 1 230 C 19.487 -5.340 31.753 1.00 39.68 ? 245 VAL A CG1 1 ATOM 1789 C CG2 . VAL A 1 230 C 21.319 -6.245 30.305 1.00 40.62 ? 245 VAL A CG2 1 ATOM 1790 N N . THR A 1 231 D 23.240 -6.154 32.642 1.00 37.71 ? 245 THR A N 1 ATOM 1791 C CA . THR A 1 231 D 24.291 -5.235 33.075 1.00 37.97 ? 245 THR A CA 1 ATOM 1792 C C . THR A 1 231 D 24.764 -4.341 31.933 1.00 36.73 ? 245 THR A C 1 ATOM 1793 O O . THR A 1 231 D 24.564 -4.661 30.763 1.00 36.14 ? 245 THR A O 1 ATOM 1794 C CB . THR A 1 231 D 25.518 -5.999 33.603 1.00 39.53 ? 245 THR A CB 1 ATOM 1795 O OG1 . THR A 1 231 D 26.191 -6.632 32.506 1.00 42.03 ? 245 THR A OG1 1 ATOM 1796 C CG2 . THR A 1 231 D 25.094 -7.061 34.610 1.00 38.98 ? 245 THR A CG2 1 ATOM 1797 N N . CYS A 1 232 E 25.395 -3.221 32.276 1.00 35.26 ? 245 CYS A N 1 ATOM 1798 C CA . CYS A 1 232 E 25.897 -2.301 31.261 1.00 35.22 ? 245 CYS A CA 1 ATOM 1799 C C . CYS A 1 232 E 27.139 -2.866 30.584 1.00 36.64 ? 245 CYS A C 1 ATOM 1800 O O . CYS A 1 232 E 27.768 -3.798 31.089 1.00 37.21 ? 245 CYS A O 1 ATOM 1801 C CB . CYS A 1 232 E 26.251 -0.945 31.878 1.00 32.29 ? 245 CYS A CB 1 ATOM 1802 S SG . CYS A 1 232 E 24.830 0.030 32.464 1.00 27.93 ? 245 CYS A SG 1 ATOM 1803 N N . PRO A 1 233 F 27.504 -2.311 29.421 1.00 38.36 ? 245 PRO A N 1 ATOM 1804 C CA . PRO A 1 233 F 28.692 -2.794 28.714 1.00 39.04 ? 245 PRO A CA 1 ATOM 1805 C C . PRO A 1 233 F 29.918 -2.597 29.605 1.00 40.88 ? 245 PRO A C 1 ATOM 1806 O O . PRO A 1 233 F 30.027 -1.591 30.305 1.00 40.44 ? 245 PRO A O 1 ATOM 1807 C CB . PRO A 1 233 F 28.722 -1.922 27.459 1.00 37.73 ? 245 PRO A CB 1 ATOM 1808 C CG . PRO A 1 233 F 28.044 -0.655 27.904 1.00 39.11 ? 245 PRO A CG 1 ATOM 1809 C CD . PRO A 1 233 F 26.885 -1.185 28.701 1.00 37.58 ? 245 PRO A CD 1 ATOM 1810 N N . PRO A 1 234 G 30.854 -3.559 29.592 1.00 42.47 ? 245 PRO A N 1 ATOM 1811 C CA . PRO A 1 234 G 32.071 -3.486 30.409 1.00 43.84 ? 245 PRO A CA 1 ATOM 1812 C C . PRO A 1 234 G 32.770 -2.130 30.369 1.00 44.57 ? 245 PRO A C 1 ATOM 1813 O O . PRO A 1 234 G 32.641 -1.427 29.347 1.00 45.65 ? 245 PRO A O 1 ATOM 1814 C CB . PRO A 1 234 G 32.934 -4.598 29.826 1.00 43.97 ? 245 PRO A CB 1 ATOM 1815 C CG . PRO A 1 234 G 31.920 -5.618 29.435 1.00 43.25 ? 245 PRO A CG 1 ATOM 1816 C CD . PRO A 1 234 G 30.860 -4.776 28.760 1.00 42.89 ? 245 PRO A CD 1 ATOM 1817 O OXT . PRO A 1 234 G 33.456 -1.797 31.358 1.00 46.17 ? 245 PRO A OXT 1 HETATM 1818 C C1 . NAG B 2 . ? 17.916 -10.091 30.892 1.00 66.05 ? 301 NAG A C1 1 HETATM 1819 C C2 . NAG B 2 . ? 17.080 -11.334 30.688 1.00 67.81 ? 301 NAG A C2 1 HETATM 1820 C C3 . NAG B 2 . ? 17.814 -12.423 29.938 1.00 68.49 ? 301 NAG A C3 1 HETATM 1821 C C4 . NAG B 2 . ? 19.335 -12.395 29.931 1.00 68.84 ? 301 NAG A C4 1 HETATM 1822 C C5 . NAG B 2 . ? 19.893 -11.029 30.194 1.00 68.82 ? 301 NAG A C5 1 HETATM 1823 C C6 . NAG B 2 . ? 20.975 -10.768 29.197 1.00 68.88 ? 301 NAG A C6 1 HETATM 1824 C C7 . NAG B 2 . ? 15.231 -11.893 32.015 1.00 69.43 ? 301 NAG A C7 1 HETATM 1825 C C8 . NAG B 2 . ? 14.654 -12.311 33.316 1.00 69.76 ? 301 NAG A C8 1 HETATM 1826 N N2 . NAG B 2 . ? 16.530 -11.750 31.941 1.00 68.77 ? 301 NAG A N2 1 HETATM 1827 O O3 . NAG B 2 . ? 17.448 -12.155 28.622 1.00 69.15 ? 301 NAG A O3 1 HETATM 1828 O O4 . NAG B 2 . ? 19.901 -13.328 30.826 1.00 69.56 ? 301 NAG A O4 1 HETATM 1829 O O5 . NAG B 2 . ? 18.877 -10.120 29.898 1.00 67.67 ? 301 NAG A O5 1 HETATM 1830 O O6 . NAG B 2 . ? 20.231 -10.682 28.025 1.00 69.76 ? 301 NAG A O6 1 HETATM 1831 O O7 . NAG B 2 . ? 14.493 -11.746 31.061 1.00 69.94 ? 301 NAG A O7 1 HETATM 1832 O O . HOH C 3 . ? 11.319 20.312 25.375 1.00 16.06 ? 1 HOH A O 1 HETATM 1833 O O . HOH C 3 . ? 21.346 27.038 27.499 1.00 18.32 ? 2 HOH A O 1 HETATM 1834 O O . HOH C 3 . ? 26.382 3.772 38.986 1.00 18.74 ? 3 HOH A O 1 HETATM 1835 O O . HOH C 3 . ? 22.777 18.709 24.845 1.00 23.64 ? 4 HOH A O 1 HETATM 1836 O O . HOH C 3 . ? 29.791 8.454 31.077 1.00 18.66 ? 5 HOH A O 1 HETATM 1837 O O . HOH C 3 . ? 9.712 17.048 26.197 1.00 21.67 ? 6 HOH A O 1 HETATM 1838 O O . HOH C 3 . ? 8.912 23.206 22.599 1.00 24.06 ? 7 HOH A O 1 HETATM 1839 O O . HOH C 3 . ? 34.398 22.353 28.892 1.00 25.52 ? 8 HOH A O 1 HETATM 1840 O O . HOH C 3 . ? 26.597 5.970 37.472 1.00 19.89 ? 9 HOH A O 1 HETATM 1841 O O . HOH C 3 . ? 19.256 21.800 30.490 1.00 20.42 ? 10 HOH A O 1 HETATM 1842 O O . HOH C 3 . ? 31.001 20.625 24.228 1.00 23.00 ? 11 HOH A O 1 HETATM 1843 O O . HOH C 3 . ? 9.302 20.459 23.423 1.00 17.89 ? 12 HOH A O 1 HETATM 1844 O O . HOH C 3 . ? 23.882 20.222 34.669 1.00 19.69 ? 13 HOH A O 1 HETATM 1845 O O . HOH C 3 . ? 10.536 19.917 28.521 1.00 19.60 ? 14 HOH A O 1 HETATM 1846 O O . HOH C 3 . ? 10.674 20.910 20.635 1.00 21.84 ? 15 HOH A O 1 HETATM 1847 O O . HOH C 3 . ? 24.771 -2.638 35.632 1.00 30.15 ? 61 HOH A O 1 HETATM 1848 O O . HOH C 3 . ? 29.362 19.991 29.829 1.00 37.16 ? 126 HOH A O 1 HETATM 1849 O O . HOH C 3 . ? 19.587 -1.993 37.978 1.00 47.81 ? 130 HOH A O 1 HETATM 1850 O O . HOH C 3 . ? 4.371 4.457 34.045 1.00 48.61 ? 150 HOH A O 1 HETATM 1851 O O . HOH C 3 . ? 22.615 26.717 15.449 1.00 46.73 ? 151 HOH A O 1 HETATM 1852 O O . HOH C 3 . ? 25.004 4.564 35.878 1.00 22.87 ? 246 HOH A O 1 HETATM 1853 O O . HOH C 3 . ? 7.123 28.073 25.104 1.00 25.30 ? 247 HOH A O 1 HETATM 1854 O O . HOH C 3 . ? 26.486 7.447 39.684 1.00 31.29 ? 248 HOH A O 1 HETATM 1855 O O . HOH C 3 . ? 23.971 30.213 23.858 1.00 24.26 ? 249 HOH A O 1 HETATM 1856 O O . HOH C 3 . ? 33.771 23.115 23.503 1.00 25.63 ? 250 HOH A O 1 HETATM 1857 O O . HOH C 3 . ? 30.234 5.707 29.705 1.00 24.75 ? 251 HOH A O 1 HETATM 1858 O O . HOH C 3 . ? 12.697 34.360 20.885 1.00 26.48 ? 252 HOH A O 1 HETATM 1859 O O . HOH C 3 . ? 35.510 25.087 29.064 1.00 25.97 ? 253 HOH A O 1 HETATM 1860 O O . HOH C 3 . ? 6.906 26.787 30.925 1.00 30.95 ? 254 HOH A O 1 HETATM 1861 O O . HOH C 3 . ? 15.885 9.032 45.344 1.00 27.25 ? 255 HOH A O 1 HETATM 1862 O O . HOH C 3 . ? 13.995 2.215 41.041 1.00 34.09 ? 256 HOH A O 1 HETATM 1863 O O . HOH C 3 . ? 20.018 0.337 39.240 1.00 24.37 ? 257 HOH A O 1 HETATM 1864 O O . HOH C 3 . ? 24.460 -1.941 26.019 1.00 29.12 ? 258 HOH A O 1 HETATM 1865 O O . HOH C 3 . ? 24.345 -2.014 22.620 1.00 33.62 ? 259 HOH A O 1 HETATM 1866 O O . HOH C 3 . ? 7.047 26.028 27.473 1.00 26.16 ? 260 HOH A O 1 HETATM 1867 O O . HOH C 3 . ? 20.709 19.721 28.462 1.00 28.77 ? 261 HOH A O 1 HETATM 1868 O O . HOH C 3 . ? 28.429 7.299 18.252 1.00 30.90 ? 262 HOH A O 1 HETATM 1869 O O . HOH C 3 . ? 13.522 11.031 42.808 1.00 29.22 ? 263 HOH A O 1 HETATM 1870 O O . HOH C 3 . ? 35.107 24.481 25.306 1.00 26.68 ? 264 HOH A O 1 HETATM 1871 O O . HOH C 3 . ? 31.932 9.969 32.058 1.00 31.11 ? 265 HOH A O 1 HETATM 1872 O O . HOH C 3 . ? 5.428 24.635 17.875 1.00 30.87 ? 266 HOH A O 1 HETATM 1873 O O . HOH C 3 . ? 24.172 16.782 13.326 1.00 33.87 ? 267 HOH A O 1 HETATM 1874 O O . HOH C 3 . ? 26.596 6.943 20.629 1.00 25.88 ? 268 HOH A O 1 HETATM 1875 O O . HOH C 3 . ? 31.213 22.843 31.264 1.00 34.84 ? 269 HOH A O 1 HETATM 1876 O O . HOH C 3 . ? 31.096 -1.667 40.142 1.00 37.83 ? 270 HOH A O 1 HETATM 1877 O O . HOH C 3 . ? 35.809 11.299 21.291 1.00 29.13 ? 271 HOH A O 1 HETATM 1878 O O . HOH C 3 . ? 17.445 28.368 32.664 1.00 32.75 ? 272 HOH A O 1 HETATM 1879 O O . HOH C 3 . ? 41.311 3.310 30.466 1.00 31.17 ? 273 HOH A O 1 HETATM 1880 O O . HOH C 3 . ? 17.037 21.327 40.802 1.00 30.76 ? 274 HOH A O 1 HETATM 1881 O O . HOH C 3 . ? 23.721 20.316 37.998 1.00 33.62 ? 275 HOH A O 1 HETATM 1882 O O . HOH C 3 . ? 25.847 19.211 36.320 1.00 31.13 ? 276 HOH A O 1 HETATM 1883 O O . HOH C 3 . ? 21.031 16.298 13.720 1.00 34.89 ? 277 HOH A O 1 HETATM 1884 O O . HOH C 3 . ? 29.114 23.042 36.809 1.00 44.28 ? 278 HOH A O 1 HETATM 1885 O O . HOH C 3 . ? 9.549 18.072 15.670 1.00 30.12 ? 279 HOH A O 1 HETATM 1886 O O . HOH C 3 . ? 36.190 14.004 35.493 1.00 29.14 ? 280 HOH A O 1 HETATM 1887 O O . HOH C 3 . ? 39.459 9.802 19.495 1.00 37.79 ? 281 HOH A O 1 HETATM 1888 O O . HOH C 3 . ? 30.115 20.311 33.458 1.00 33.42 ? 282 HOH A O 1 HETATM 1889 O O . HOH C 3 . ? 30.618 12.608 34.701 1.00 35.92 ? 283 HOH A O 1 HETATM 1890 O O . HOH C 3 . ? 16.890 3.612 42.015 1.00 29.88 ? 284 HOH A O 1 HETATM 1891 O O . HOH C 3 . ? 36.413 8.277 15.612 1.00 32.79 ? 285 HOH A O 1 HETATM 1892 O O . HOH C 3 . ? 0.931 8.987 22.600 1.00 37.03 ? 286 HOH A O 1 HETATM 1893 O O . HOH C 3 . ? 17.012 26.954 36.022 1.00 36.37 ? 287 HOH A O 1 HETATM 1894 O O . HOH C 3 . ? 32.700 4.077 30.307 1.00 26.10 ? 288 HOH A O 1 HETATM 1895 O O . HOH C 3 . ? 33.904 7.867 31.562 1.00 32.14 ? 289 HOH A O 1 HETATM 1896 O O . HOH C 3 . ? 42.520 15.153 35.360 1.00 47.33 ? 290 HOH A O 1 HETATM 1897 O O . HOH C 3 . ? 0.746 16.987 27.001 1.00 32.30 ? 291 HOH A O 1 HETATM 1898 O O . HOH C 3 . ? 13.646 6.174 21.532 1.00 30.55 ? 292 HOH A O 1 HETATM 1899 O O . HOH C 3 . ? 40.056 16.207 17.054 1.00 37.54 ? 293 HOH A O 1 HETATM 1900 O O . HOH C 3 . ? 33.443 0.302 41.408 1.00 45.20 ? 294 HOH A O 1 HETATM 1901 O O . HOH C 3 . ? 22.054 -2.459 35.174 1.00 34.28 ? 295 HOH A O 1 HETATM 1902 O O . HOH C 3 . ? 4.184 11.586 37.686 1.00 30.45 ? 296 HOH A O 1 HETATM 1903 O O . HOH C 3 . ? 17.197 31.268 17.463 1.00 30.54 ? 297 HOH A O 1 HETATM 1904 O O . HOH C 3 . ? 1.425 17.494 34.347 1.00 31.81 ? 298 HOH A O 1 HETATM 1905 O O . HOH C 3 . ? 27.143 20.446 31.161 1.00 30.13 ? 299 HOH A O 1 HETATM 1906 O O . HOH C 3 . ? 18.120 22.547 14.256 1.00 38.54 ? 300 HOH A O 1 HETATM 1907 O O . HOH C 3 . ? 9.650 23.641 34.707 1.00 40.61 ? 302 HOH A O 1 HETATM 1908 O O . HOH C 3 . ? 6.070 4.266 24.262 1.00 33.41 ? 303 HOH A O 1 HETATM 1909 O O . HOH C 3 . ? 37.809 24.512 16.710 1.00 41.57 ? 304 HOH A O 1 HETATM 1910 O O . HOH C 3 . ? 34.253 3.180 32.302 1.00 32.78 ? 305 HOH A O 1 HETATM 1911 O O . HOH C 3 . ? 24.429 9.319 40.910 1.00 39.07 ? 306 HOH A O 1 HETATM 1912 O O . HOH C 3 . ? 17.971 19.485 16.757 1.00 40.00 ? 307 HOH A O 1 HETATM 1913 O O . HOH C 3 . ? 41.478 10.160 32.736 1.00 44.47 ? 308 HOH A O 1 HETATM 1914 O O . HOH C 3 . ? 30.983 32.144 22.737 1.00 43.06 ? 309 HOH A O 1 HETATM 1915 O O . HOH C 3 . ? 1.339 15.761 24.720 1.00 36.52 ? 310 HOH A O 1 HETATM 1916 O O . HOH C 3 . ? 34.222 5.224 21.154 1.00 41.08 ? 311 HOH A O 1 HETATM 1917 O O . HOH C 3 . ? 25.836 32.048 24.742 1.00 38.48 ? 312 HOH A O 1 HETATM 1918 O O . HOH C 3 . ? 0.285 7.389 26.807 1.00 34.17 ? 313 HOH A O 1 HETATM 1919 O O . HOH C 3 . ? 25.102 -0.914 20.185 1.00 37.13 ? 314 HOH A O 1 HETATM 1920 O O . HOH C 3 . ? 40.507 8.382 34.345 1.00 37.53 ? 315 HOH A O 1 HETATM 1921 O O . HOH C 3 . ? 32.675 6.699 18.374 1.00 36.69 ? 316 HOH A O 1 HETATM 1922 O O . HOH C 3 . ? 0.887 20.241 20.590 1.00 39.98 ? 317 HOH A O 1 HETATM 1923 O O . HOH C 3 . ? 28.287 18.276 34.757 1.00 38.18 ? 318 HOH A O 1 HETATM 1924 O O . HOH C 3 . ? 3.285 23.133 33.372 1.00 44.57 ? 319 HOH A O 1 HETATM 1925 O O . HOH C 3 . ? 28.158 -2.060 23.821 1.00 40.90 ? 320 HOH A O 1 HETATM 1926 O O . HOH C 3 . ? 12.288 -1.872 39.217 1.00 49.57 ? 321 HOH A O 1 HETATM 1927 O O . HOH C 3 . ? 7.736 5.398 20.957 1.00 35.78 ? 322 HOH A O 1 HETATM 1928 O O . HOH C 3 . ? -3.727 24.150 20.176 1.00 38.58 ? 323 HOH A O 1 HETATM 1929 O O . HOH C 3 . ? 9.878 22.635 42.882 1.00 37.18 ? 324 HOH A O 1 HETATM 1930 O O . HOH C 3 . ? 23.088 9.574 13.566 1.00 44.31 ? 325 HOH A O 1 HETATM 1931 O O . HOH C 3 . ? 33.280 2.825 22.891 1.00 41.23 ? 326 HOH A O 1 HETATM 1932 O O . HOH C 3 . ? 43.415 18.367 27.086 1.00 43.77 ? 327 HOH A O 1 HETATM 1933 O O . HOH C 3 . ? 22.527 9.531 43.096 1.00 35.62 ? 328 HOH A O 1 HETATM 1934 O O . HOH C 3 . ? 28.927 27.403 36.875 1.00 49.24 ? 329 HOH A O 1 HETATM 1935 O O . HOH C 3 . ? 27.175 36.146 32.949 1.00 54.12 ? 330 HOH A O 1 HETATM 1936 O O . HOH C 3 . ? 35.300 7.426 22.373 1.00 44.71 ? 331 HOH A O 1 HETATM 1937 O O . HOH C 3 . ? 21.769 24.486 37.199 1.00 32.93 ? 332 HOH A O 1 HETATM 1938 O O . HOH C 3 . ? 7.931 15.446 43.753 1.00 60.61 ? 333 HOH A O 1 HETATM 1939 O O . HOH C 3 . ? 42.534 10.162 21.219 1.00 34.44 ? 334 HOH A O 1 HETATM 1940 O O . HOH C 3 . ? 11.753 9.163 17.362 1.00 50.73 ? 335 HOH A O 1 HETATM 1941 O O . HOH C 3 . ? 39.798 1.867 31.951 1.00 54.49 ? 336 HOH A O 1 HETATM 1942 O O . HOH C 3 . ? 22.250 18.947 9.512 1.00 53.95 ? 337 HOH A O 1 HETATM 1943 O O . HOH C 3 . ? 36.853 23.104 35.369 1.00 37.24 ? 338 HOH A O 1 HETATM 1944 O O . HOH C 3 . ? 37.149 6.050 24.414 1.00 39.22 ? 339 HOH A O 1 HETATM 1945 O O . HOH C 3 . ? 42.654 8.226 23.185 1.00 31.24 ? 340 HOH A O 1 HETATM 1946 O O . HOH C 3 . ? 32.777 21.510 35.170 1.00 45.35 ? 341 HOH A O 1 HETATM 1947 O O . HOH C 3 . ? 12.850 -2.651 24.647 1.00 37.11 ? 342 HOH A O 1 HETATM 1948 O O . HOH C 3 . ? 2.644 30.797 30.733 1.00 46.56 ? 343 HOH A O 1 HETATM 1949 O O . HOH C 3 . ? 17.041 20.699 45.062 1.00 42.01 ? 344 HOH A O 1 HETATM 1950 O O . HOH C 3 . ? 15.296 16.317 45.747 1.00 39.23 ? 345 HOH A O 1 HETATM 1951 O O . HOH C 3 . ? 15.132 4.371 19.030 1.00 40.53 ? 346 HOH A O 1 HETATM 1952 O O . HOH C 3 . ? 31.718 8.440 12.336 1.00 46.72 ? 347 HOH A O 1 HETATM 1953 O O . HOH C 3 . ? 16.425 0.395 40.264 1.00 36.62 ? 348 HOH A O 1 HETATM 1954 O O . HOH C 3 . ? 26.244 22.896 10.612 1.00 57.64 ? 349 HOH A O 1 HETATM 1955 O O . HOH C 3 . ? 9.810 13.735 42.969 1.00 34.67 ? 350 HOH A O 1 HETATM 1956 O O . HOH C 3 . ? 0.994 13.636 27.996 1.00 42.16 ? 351 HOH A O 1 HETATM 1957 O O . HOH C 3 . ? 16.823 32.923 33.493 1.00 48.23 ? 352 HOH A O 1 HETATM 1958 O O . HOH C 3 . ? 20.419 20.586 42.885 1.00 49.71 ? 353 HOH A O 1 HETATM 1959 O O . HOH C 3 . ? 10.369 5.087 21.286 1.00 39.17 ? 354 HOH A O 1 HETATM 1960 O O . HOH C 3 . ? 12.864 26.850 43.770 1.00 45.64 ? 355 HOH A O 1 HETATM 1961 O O . HOH C 3 . ? 10.214 31.705 21.743 1.00 42.95 ? 356 HOH A O 1 HETATM 1962 O O . HOH C 3 . ? 34.769 7.364 42.927 1.00 33.01 ? 357 HOH A O 1 HETATM 1963 O O . HOH C 3 . ? 42.762 12.806 34.199 1.00 37.03 ? 358 HOH A O 1 HETATM 1964 O O . HOH C 3 . ? 23.447 21.705 40.472 1.00 42.35 ? 359 HOH A O 1 HETATM 1965 O O . HOH C 3 . ? 18.564 2.093 43.258 1.00 38.09 ? 360 HOH A O 1 HETATM 1966 O O . HOH C 3 . ? 24.559 17.834 38.935 1.00 41.64 ? 361 HOH A O 1 HETATM 1967 O O . HOH C 3 . ? 10.685 24.072 36.944 1.00 46.38 ? 362 HOH A O 1 HETATM 1968 O O . HOH C 3 . ? 40.427 26.362 11.010 1.00 45.25 ? 363 HOH A O 1 HETATM 1969 O O . HOH C 3 . ? 7.820 1.105 27.273 1.00 31.62 ? 364 HOH A O 1 HETATM 1970 O O . HOH C 3 . ? 36.861 22.086 17.096 1.00 51.40 ? 365 HOH A O 1 HETATM 1971 O O . HOH C 3 . ? 11.508 8.823 42.933 1.00 40.64 ? 366 HOH A O 1 HETATM 1972 O O . HOH C 3 . ? 33.224 17.768 34.055 1.00 41.14 ? 367 HOH A O 1 HETATM 1973 O O . HOH C 3 . ? 29.139 15.177 10.266 1.00 53.24 ? 368 HOH A O 1 HETATM 1974 O O . HOH C 3 . ? 25.367 15.056 41.715 1.00 40.80 ? 369 HOH A O 1 HETATM 1975 O O . HOH C 3 . ? 22.554 24.243 12.308 1.00 47.43 ? 370 HOH A O 1 HETATM 1976 O O . HOH C 3 . ? -6.249 24.914 22.286 1.00 52.94 ? 371 HOH A O 1 HETATM 1977 O O . HOH C 3 . ? 14.481 26.948 36.675 1.00 47.61 ? 372 HOH A O 1 HETATM 1978 O O . HOH C 3 . ? 6.450 20.844 40.021 1.00 41.33 ? 373 HOH A O 1 HETATM 1979 O O . HOH C 3 . ? 15.751 11.801 17.201 1.00 57.85 ? 374 HOH A O 1 HETATM 1980 O O . HOH C 3 . ? 20.072 34.003 35.299 1.00 46.51 ? 375 HOH A O 1 HETATM 1981 O O . HOH C 3 . ? 41.672 8.766 19.078 1.00 54.71 ? 376 HOH A O 1 HETATM 1982 O O . HOH C 3 . ? 1.523 25.725 22.815 1.00 38.07 ? 377 HOH A O 1 HETATM 1983 O O . HOH C 3 . ? 13.579 9.541 50.051 1.00 49.20 ? 378 HOH A O 1 HETATM 1984 O O . HOH C 3 . ? 32.702 5.299 14.923 1.00 46.27 ? 379 HOH A O 1 HETATM 1985 O O . HOH C 3 . ? 28.506 1.079 14.324 1.00 49.24 ? 380 HOH A O 1 HETATM 1986 O O . HOH C 3 . ? 37.251 22.802 23.280 1.00 40.66 ? 381 HOH A O 1 HETATM 1987 O O . HOH C 3 . ? 23.890 -8.463 31.132 1.00 49.93 ? 382 HOH A O 1 HETATM 1988 O O . HOH C 3 . ? 39.326 26.500 34.079 1.00 50.78 ? 383 HOH A O 1 HETATM 1989 O O . HOH C 3 . ? 27.019 13.997 12.796 1.00 47.99 ? 384 HOH A O 1 HETATM 1990 O O . HOH C 3 . ? 19.129 27.073 42.881 1.00 48.85 ? 385 HOH A O 1 HETATM 1991 O O . HOH C 3 . ? 40.003 6.384 24.189 1.00 47.68 ? 386 HOH A O 1 HETATM 1992 O O . HOH C 3 . ? 1.808 10.583 39.166 1.00 52.51 ? 387 HOH A O 1 HETATM 1993 O O . HOH C 3 . ? 23.620 13.139 42.863 1.00 43.09 ? 388 HOH A O 1 HETATM 1994 O O . HOH C 3 . ? 22.666 -0.884 18.524 1.00 42.05 ? 389 HOH A O 1 HETATM 1995 O O . HOH C 3 . ? -0.682 20.419 28.979 1.00 42.02 ? 390 HOH A O 1 HETATM 1996 O O . HOH C 3 . ? 7.531 1.197 40.954 1.00 58.15 ? 391 HOH A O 1 HETATM 1997 O O . HOH C 3 . ? 25.412 -4.389 27.461 1.00 55.92 ? 392 HOH A O 1 HETATM 1998 O O . HOH C 3 . ? 20.599 19.880 45.406 1.00 56.86 ? 393 HOH A O 1 HETATM 1999 O O . HOH C 3 . ? -1.584 14.416 32.044 1.00 55.65 ? 394 HOH A O 1 HETATM 2000 O O . HOH C 3 . ? 0.534 22.912 21.782 1.00 53.46 ? 395 HOH A O 1 HETATM 2001 O O . HOH C 3 . ? 29.502 -0.993 21.286 1.00 45.09 ? 396 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 VAL 2 17 17 VAL VAL 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 PRO 13 28 28 PRO PRO 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 VAL 16 31 31 VAL VAL A . n A 1 17 ALA 17 32 32 ALA ALA A . n A 1 18 LEU 18 33 33 LEU LEU A . n A 1 19 TYR 19 34 34 TYR TYR A . n A 1 20 THR 20 35 35 THR THR A . n A 1 21 SER 21 36 36 SER SER A . n A 1 22 ALA 22 36 36 ALA ALA A A n A 1 23 SER 23 37 37 SER SER A . n A 1 24 SER 24 38 38 SER SER A . n A 1 25 THR 25 39 39 THR THR A . n A 1 26 ILE 26 40 40 ILE ILE A . n A 1 27 HIS 27 41 41 HIS HIS A . n A 1 28 CYS 28 42 42 CYS CYS A . n A 1 29 ALA 29 43 43 ALA ALA A . n A 1 30 GLY 30 44 44 GLY GLY A . n A 1 31 ALA 31 45 45 ALA ALA A . n A 1 32 LEU 32 46 46 LEU LEU A . n A 1 33 ILE 33 47 47 ILE ILE A . n A 1 34 ASN 34 48 48 ASN ASN A . n A 1 35 ARG 35 49 49 ARG ARG A . n A 1 36 GLU 36 50 50 GLU GLU A . n A 1 37 TRP 37 51 51 TRP TRP A . n A 1 38 VAL 38 52 52 VAL VAL A . n A 1 39 LEU 39 53 53 LEU LEU A . n A 1 40 THR 40 54 54 THR THR A . n A 1 41 ALA 41 55 55 ALA ALA A . n A 1 42 ALA 42 56 56 ALA ALA A . n A 1 43 HIS 43 57 57 HIS HIS A . n A 1 44 CYS 44 58 58 CYS CYS A . n A 1 45 ASP 45 59 59 ASP ASP A . n A 1 46 ARG 46 60 60 ARG ARG A . n A 1 47 ARG 47 62 62 ARG ARG A . n A 1 48 ASN 48 63 63 ASN ASN A . n A 1 49 ILE 49 64 64 ILE ILE A . n A 1 50 ARG 50 65 65 ARG ARG A . n A 1 51 ILE 51 66 66 ILE ILE A . n A 1 52 LYS 52 67 67 LYS LYS A . n A 1 53 LEU 53 68 68 LEU LEU A . n A 1 54 GLY 54 69 69 GLY GLY A . n A 1 55 MET 55 70 70 MET MET A . n A 1 56 HIS 56 71 71 HIS HIS A . n A 1 57 SER 57 72 72 SER SER A . n A 1 58 LYS 58 73 73 LYS LYS A . n A 1 59 ASN 59 74 74 ASN ASN A . n A 1 60 ILE 60 75 75 ILE ILE A . n A 1 61 ARG 61 76 76 ARG ARG A . n A 1 62 ASN 62 77 77 ASN ASN A . n A 1 63 GLU 63 78 78 GLU GLU A . n A 1 64 ASP 64 79 79 ASP ASP A . n A 1 65 GLU 65 80 80 GLU GLU A . n A 1 66 GLN 66 81 81 GLN GLN A . n A 1 67 ILE 67 82 82 ILE ILE A . n A 1 68 ARG 68 83 83 ARG ARG A . n A 1 69 VAL 69 84 84 VAL VAL A . n A 1 70 PRO 70 85 85 PRO PRO A . n A 1 71 ARG 71 86 86 ARG ARG A . n A 1 72 GLY 72 87 87 GLY GLY A . n A 1 73 LYS 73 88 88 LYS LYS A . n A 1 74 TYR 74 89 89 TYR TYR A . n A 1 75 PHE 75 90 90 PHE PHE A . n A 1 76 CYS 76 91 91 CYS CYS A . n A 1 77 LEU 77 92 92 LEU LEU A . n A 1 78 ASN 78 93 93 ASN ASN A . n A 1 79 THR 79 94 94 THR THR A . n A 1 80 LYS 80 95 95 LYS LYS A . n A 1 81 PHE 81 95 95 PHE PHE A A n A 1 82 PRO 82 96 96 PRO PRO A . n A 1 83 ASN 83 97 97 ASN ASN A . n A 1 84 GLY 84 98 98 GLY GLY A . n A 1 85 LEU 85 99 99 LEU LEU A . n A 1 86 ASP 86 100 100 ASP ASP A . n A 1 87 LYS 87 101 101 LYS LYS A . n A 1 88 ASP 88 102 102 ASP ASP A . n A 1 89 ILE 89 103 103 ILE ILE A . n A 1 90 MET 90 104 104 MET MET A . n A 1 91 LEU 91 105 105 LEU LEU A . n A 1 92 ILE 92 106 106 ILE ILE A . n A 1 93 ARG 93 107 107 ARG ARG A . n A 1 94 LEU 94 108 108 LEU LEU A . n A 1 95 ARG 95 109 109 ARG ARG A . n A 1 96 ARG 96 110 110 ARG ARG A . n A 1 97 PRO 97 111 111 PRO PRO A . n A 1 98 VAL 98 112 112 VAL VAL A . n A 1 99 THR 99 113 113 THR THR A . n A 1 100 TYR 100 114 114 TYR TYR A . n A 1 101 SER 101 115 115 SER SER A . n A 1 102 THR 102 116 116 THR THR A . n A 1 103 HIS 103 117 117 HIS HIS A . n A 1 104 ILE 104 118 118 ILE ILE A . n A 1 105 ALA 105 119 119 ALA ALA A . n A 1 106 PRO 106 120 120 PRO PRO A . n A 1 107 VAL 107 121 121 VAL VAL A . n A 1 108 SER 108 122 122 SER SER A . n A 1 109 LEU 109 123 123 LEU LEU A . n A 1 110 PRO 110 124 124 PRO PRO A . n A 1 111 SER 111 125 125 SER SER A . n A 1 112 ARG 112 127 127 ARG ARG A . n A 1 113 SER 113 128 128 SER SER A . n A 1 114 ARG 114 129 129 ARG ARG A . n A 1 115 GLY 115 131 131 GLY GLY A . n A 1 116 VAL 116 132 132 VAL VAL A . n A 1 117 GLY 117 133 133 GLY GLY A . n A 1 118 SER 118 134 134 SER SER A . n A 1 119 ARG 119 135 135 ARG ARG A . n A 1 120 CYS 120 136 136 CYS CYS A . n A 1 121 ARG 121 137 137 ARG ARG A . n A 1 122 ILE 122 138 138 ILE ILE A . n A 1 123 MET 123 139 139 MET MET A . n A 1 124 GLY 124 140 140 GLY GLY A . n A 1 125 TRP 125 141 141 TRP TRP A . n A 1 126 GLY 126 142 142 GLY GLY A . n A 1 127 LYS 127 143 143 LYS LYS A . n A 1 128 ILE 128 144 144 ILE ILE A . n A 1 129 SER 129 145 145 SER SER A . n A 1 130 THR 130 146 146 THR THR A . n A 1 131 THR 131 147 147 THR THR A . n A 1 132 THR 132 148 148 THR THR A . n A 1 133 TYR 133 149 149 TYR TYR A . n A 1 134 PRO 134 152 152 PRO PRO A . n A 1 135 ASP 135 153 153 ASP ASP A . n A 1 136 VAL 136 154 154 VAL VAL A . n A 1 137 PRO 137 155 155 PRO PRO A . n A 1 138 HIS 138 156 156 HIS HIS A . n A 1 139 CYS 139 157 157 CYS CYS A . n A 1 140 THR 140 158 158 THR THR A . n A 1 141 ASN 141 159 159 ASN ASN A . n A 1 142 ILE 142 160 160 ILE ILE A . n A 1 143 PHE 143 161 161 PHE PHE A . n A 1 144 ILE 144 162 162 ILE ILE A . n A 1 145 VAL 145 163 163 VAL VAL A . n A 1 146 LYS 146 164 164 LYS LYS A . n A 1 147 HIS 147 165 165 HIS HIS A . n A 1 148 LYS 148 166 166 LYS LYS A . n A 1 149 TRP 149 167 167 TRP TRP A . n A 1 150 CYS 150 168 168 CYS CYS A . n A 1 151 GLU 151 169 169 GLU GLU A . n A 1 152 PRO 152 170 170 PRO PRO A . n A 1 153 LEU 153 171 171 LEU LEU A . n A 1 154 TYR 154 172 172 TYR TYR A . n A 1 155 PRO 155 172 172 PRO PRO A A n A 1 156 TRP 156 173 173 TRP TRP A . n A 1 157 VAL 157 174 174 VAL VAL A . n A 1 158 PRO 158 175 175 PRO PRO A . n A 1 159 ALA 159 176 176 ALA ALA A . n A 1 160 ASP 160 177 177 ASP ASP A . n A 1 161 SER 161 178 178 SER SER A . n A 1 162 ARG 162 179 179 ARG ARG A . n A 1 163 THR 163 180 180 THR THR A . n A 1 164 LEU 164 181 181 LEU LEU A . n A 1 165 CYS 165 182 182 CYS CYS A . n A 1 166 ALA 166 183 183 ALA ALA A . n A 1 167 GLY 167 184 184 GLY GLY A . n A 1 168 ILE 168 185 185 ILE ILE A . n A 1 169 LEU 169 186 186 LEU LEU A . n A 1 170 LYS 170 186 186 LYS LYS A A n A 1 171 GLY 171 186 186 GLY GLY A B n A 1 172 GLY 172 187 187 GLY GLY A . n A 1 173 ARG 173 188 188 ARG ARG A . n A 1 174 ASP 174 189 189 ASP ASP A . n A 1 175 THR 175 190 190 THR THR A . n A 1 176 CYS 176 191 191 CYS CYS A . n A 1 177 HIS 177 192 192 HIS HIS A . n A 1 178 GLY 178 193 193 GLY GLY A . n A 1 179 ASP 179 194 194 ASP ASP A . n A 1 180 SER 180 195 195 SER SER A . n A 1 181 GLY 181 196 196 GLY GLY A . n A 1 182 GLY 182 197 197 GLY GLY A . n A 1 183 PRO 183 198 198 PRO PRO A . n A 1 184 LEU 184 199 199 LEU LEU A . n A 1 185 ILE 185 200 200 ILE ILE A . n A 1 186 CYS 186 201 201 CYS CYS A . n A 1 187 ASN 187 202 202 ASN ASN A . n A 1 188 GLY 188 207 207 GLY GLY A . n A 1 189 GLU 189 208 208 GLU GLU A . n A 1 190 MET 190 209 209 MET MET A . n A 1 191 HIS 191 210 210 HIS HIS A . n A 1 192 GLY 192 211 211 GLY GLY A . n A 1 193 ILE 193 212 212 ILE ILE A . n A 1 194 VAL 194 213 213 VAL VAL A . n A 1 195 ALA 195 214 214 ALA ALA A . n A 1 196 GLY 196 215 215 GLY GLY A . n A 1 197 GLY 197 216 216 GLY GLY A . n A 1 198 SER 198 217 217 SER SER A . n A 1 199 GLU 199 218 218 GLU GLU A . n A 1 200 PRO 200 219 219 PRO PRO A . n A 1 201 CYS 201 220 220 CYS CYS A . n A 1 202 GLY 202 221 221 GLY GLY A . n A 1 203 GLN 203 221 221 GLN GLN A A n A 1 204 HIS 204 222 222 HIS HIS A . n A 1 205 LEU 205 223 223 LEU LEU A . n A 1 206 LYS 206 224 224 LYS LYS A . n A 1 207 PRO 207 225 225 PRO PRO A . n A 1 208 ALA 208 226 226 ALA ALA A . n A 1 209 VAL 209 227 227 VAL VAL A . n A 1 210 TYR 210 228 228 TYR TYR A . n A 1 211 THR 211 229 229 THR THR A . n A 1 212 LYS 212 230 230 LYS LYS A . n A 1 213 VAL 213 231 231 VAL VAL A . n A 1 214 PHE 214 232 232 PHE PHE A . n A 1 215 ASP 215 233 233 ASP ASP A . n A 1 216 TYR 216 234 234 TYR TYR A . n A 1 217 ASN 217 235 235 ASN ASN A . n A 1 218 ASN 218 236 236 ASN ASN A . n A 1 219 TRP 219 237 237 TRP TRP A . n A 1 220 ILE 220 238 238 ILE ILE A . n A 1 221 GLN 221 239 239 GLN GLN A . n A 1 222 SER 222 240 240 SER SER A . n A 1 223 ILE 223 241 241 ILE ILE A . n A 1 224 ILE 224 242 242 ILE ILE A . n A 1 225 ALA 225 243 243 ALA ALA A . n A 1 226 GLY 226 244 244 GLY GLY A . n A 1 227 ASN 227 245 245 ASN ASN A . n A 1 228 ARG 228 245 245 ARG ARG A A n A 1 229 THR 229 245 245 THR THR A B n A 1 230 VAL 230 245 245 VAL VAL A C n A 1 231 THR 231 245 245 THR THR A D n A 1 232 CYS 232 245 245 CYS CYS A E n A 1 233 PRO 233 245 245 PRO PRO A F n A 1 234 PRO 234 245 245 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 1 301 301 NAG NAG A . C 3 HOH 1 1 1 HOH TIP A . C 3 HOH 2 2 2 HOH TIP A . C 3 HOH 3 3 3 HOH TIP A . C 3 HOH 4 4 4 HOH TIP A . C 3 HOH 5 5 5 HOH TIP A . C 3 HOH 6 6 6 HOH TIP A . C 3 HOH 7 7 7 HOH TIP A . C 3 HOH 8 8 8 HOH TIP A . C 3 HOH 9 9 9 HOH TIP A . C 3 HOH 10 10 10 HOH TIP A . C 3 HOH 11 11 11 HOH TIP A . C 3 HOH 12 12 12 HOH TIP A . C 3 HOH 13 13 13 HOH TIP A . C 3 HOH 14 14 14 HOH TIP A . C 3 HOH 15 15 15 HOH TIP A . C 3 HOH 16 61 61 HOH TIP A . C 3 HOH 17 126 126 HOH TIP A . C 3 HOH 18 130 130 HOH TIP A . C 3 HOH 19 150 150 HOH TIP A . C 3 HOH 20 151 151 HOH TIP A . C 3 HOH 21 246 16 HOH TIP A . C 3 HOH 22 247 17 HOH TIP A . C 3 HOH 23 248 18 HOH TIP A . C 3 HOH 24 249 19 HOH TIP A . C 3 HOH 25 250 20 HOH TIP A . C 3 HOH 26 251 21 HOH TIP A . C 3 HOH 27 252 22 HOH TIP A . C 3 HOH 28 253 23 HOH TIP A . C 3 HOH 29 254 24 HOH TIP A . C 3 HOH 30 255 25 HOH TIP A . C 3 HOH 31 256 26 HOH TIP A . C 3 HOH 32 257 27 HOH TIP A . C 3 HOH 33 258 28 HOH TIP A . C 3 HOH 34 259 29 HOH TIP A . C 3 HOH 35 260 30 HOH TIP A . C 3 HOH 36 261 31 HOH TIP A . C 3 HOH 37 262 32 HOH TIP A . C 3 HOH 38 263 33 HOH TIP A . C 3 HOH 39 264 34 HOH TIP A . C 3 HOH 40 265 35 HOH TIP A . C 3 HOH 41 266 36 HOH TIP A . C 3 HOH 42 267 37 HOH TIP A . C 3 HOH 43 268 38 HOH TIP A . C 3 HOH 44 269 39 HOH TIP A . C 3 HOH 45 270 40 HOH TIP A . C 3 HOH 46 271 41 HOH TIP A . C 3 HOH 47 272 42 HOH TIP A . C 3 HOH 48 273 43 HOH TIP A . C 3 HOH 49 274 44 HOH TIP A . C 3 HOH 50 275 45 HOH TIP A . C 3 HOH 51 276 46 HOH TIP A . C 3 HOH 52 277 47 HOH TIP A . C 3 HOH 53 278 48 HOH TIP A . C 3 HOH 54 279 49 HOH TIP A . C 3 HOH 55 280 50 HOH TIP A . C 3 HOH 56 281 51 HOH TIP A . C 3 HOH 57 282 52 HOH TIP A . C 3 HOH 58 283 53 HOH TIP A . C 3 HOH 59 284 54 HOH TIP A . C 3 HOH 60 285 55 HOH TIP A . C 3 HOH 61 286 56 HOH TIP A . C 3 HOH 62 287 57 HOH TIP A . C 3 HOH 63 288 58 HOH TIP A . C 3 HOH 64 289 59 HOH TIP A . C 3 HOH 65 290 60 HOH TIP A . C 3 HOH 66 291 62 HOH TIP A . C 3 HOH 67 292 63 HOH TIP A . C 3 HOH 68 293 64 HOH TIP A . C 3 HOH 69 294 65 HOH TIP A . C 3 HOH 70 295 66 HOH TIP A . C 3 HOH 71 296 67 HOH TIP A . C 3 HOH 72 297 68 HOH TIP A . C 3 HOH 73 298 69 HOH TIP A . C 3 HOH 74 299 70 HOH TIP A . C 3 HOH 75 300 71 HOH TIP A . C 3 HOH 76 302 72 HOH TIP A . C 3 HOH 77 303 73 HOH TIP A . C 3 HOH 78 304 74 HOH TIP A . C 3 HOH 79 305 75 HOH TIP A . C 3 HOH 80 306 76 HOH TIP A . C 3 HOH 81 307 77 HOH TIP A . C 3 HOH 82 308 78 HOH TIP A . C 3 HOH 83 309 79 HOH TIP A . C 3 HOH 84 310 80 HOH TIP A . C 3 HOH 85 311 81 HOH TIP A . C 3 HOH 86 312 82 HOH TIP A . C 3 HOH 87 313 83 HOH TIP A . C 3 HOH 88 314 84 HOH TIP A . C 3 HOH 89 315 85 HOH TIP A . C 3 HOH 90 316 86 HOH TIP A . C 3 HOH 91 317 87 HOH TIP A . C 3 HOH 92 318 88 HOH TIP A . C 3 HOH 93 319 89 HOH TIP A . C 3 HOH 94 320 90 HOH TIP A . C 3 HOH 95 321 91 HOH TIP A . C 3 HOH 96 322 92 HOH TIP A . C 3 HOH 97 323 93 HOH TIP A . C 3 HOH 98 324 94 HOH TIP A . C 3 HOH 99 325 95 HOH TIP A . C 3 HOH 100 326 96 HOH TIP A . C 3 HOH 101 327 97 HOH TIP A . C 3 HOH 102 328 98 HOH TIP A . C 3 HOH 103 329 99 HOH TIP A . C 3 HOH 104 330 100 HOH TIP A . C 3 HOH 105 331 101 HOH TIP A . C 3 HOH 106 332 102 HOH TIP A . C 3 HOH 107 333 103 HOH TIP A . C 3 HOH 108 334 104 HOH TIP A . C 3 HOH 109 335 105 HOH TIP A . C 3 HOH 110 336 106 HOH TIP A . C 3 HOH 111 337 107 HOH TIP A . C 3 HOH 112 338 108 HOH TIP A . C 3 HOH 113 339 109 HOH TIP A . C 3 HOH 114 340 110 HOH TIP A . C 3 HOH 115 341 111 HOH TIP A . C 3 HOH 116 342 112 HOH TIP A . C 3 HOH 117 343 113 HOH TIP A . C 3 HOH 118 344 114 HOH TIP A . C 3 HOH 119 345 115 HOH TIP A . C 3 HOH 120 346 116 HOH TIP A . C 3 HOH 121 347 117 HOH TIP A . C 3 HOH 122 348 118 HOH TIP A . C 3 HOH 123 349 119 HOH TIP A . C 3 HOH 124 350 120 HOH TIP A . C 3 HOH 125 351 121 HOH TIP A . C 3 HOH 126 352 122 HOH TIP A . C 3 HOH 127 353 123 HOH TIP A . C 3 HOH 128 354 124 HOH TIP A . C 3 HOH 129 355 125 HOH TIP A . C 3 HOH 130 356 127 HOH TIP A . C 3 HOH 131 357 128 HOH TIP A . C 3 HOH 132 358 129 HOH TIP A . C 3 HOH 133 359 131 HOH TIP A . C 3 HOH 134 360 132 HOH TIP A . C 3 HOH 135 361 133 HOH TIP A . C 3 HOH 136 362 134 HOH TIP A . C 3 HOH 137 363 135 HOH TIP A . C 3 HOH 138 364 136 HOH TIP A . C 3 HOH 139 365 137 HOH TIP A . C 3 HOH 140 366 138 HOH TIP A . C 3 HOH 141 367 139 HOH TIP A . C 3 HOH 142 368 140 HOH TIP A . C 3 HOH 143 369 141 HOH TIP A . C 3 HOH 144 370 142 HOH TIP A . C 3 HOH 145 371 143 HOH TIP A . C 3 HOH 146 372 144 HOH TIP A . C 3 HOH 147 373 145 HOH TIP A . C 3 HOH 148 374 146 HOH TIP A . C 3 HOH 149 375 147 HOH TIP A . C 3 HOH 150 376 148 HOH TIP A . C 3 HOH 151 377 149 HOH TIP A . C 3 HOH 152 378 152 HOH TIP A . C 3 HOH 153 379 153 HOH TIP A . C 3 HOH 154 380 154 HOH TIP A . C 3 HOH 155 381 155 HOH TIP A . C 3 HOH 156 382 156 HOH TIP A . C 3 HOH 157 383 157 HOH TIP A . C 3 HOH 158 384 158 HOH TIP A . C 3 HOH 159 385 159 HOH TIP A . C 3 HOH 160 386 160 HOH TIP A . C 3 HOH 161 387 161 HOH TIP A . C 3 HOH 162 388 162 HOH TIP A . C 3 HOH 163 389 163 HOH TIP A . C 3 HOH 164 390 164 HOH TIP A . C 3 HOH 165 391 165 HOH TIP A . C 3 HOH 166 392 166 HOH TIP A . C 3 HOH 167 393 167 HOH TIP A . C 3 HOH 168 394 168 HOH TIP A . C 3 HOH 169 395 169 HOH TIP A . C 3 HOH 170 396 170 HOH TIP A . # _pdbx_struct_mod_residue.id 1 _pdbx_struct_mod_residue.label_asym_id A _pdbx_struct_mod_residue.label_comp_id ASN _pdbx_struct_mod_residue.label_seq_id 227 _pdbx_struct_mod_residue.auth_asym_id A _pdbx_struct_mod_residue.auth_comp_id ASN _pdbx_struct_mod_residue.auth_seq_id 245 _pdbx_struct_mod_residue.PDB_ins_code ? _pdbx_struct_mod_residue.parent_comp_id ASN _pdbx_struct_mod_residue.details 'GLYCOSYLATION SITE' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_and_software_defined_assembly _pdbx_struct_assembly.method_details PISA _pdbx_struct_assembly.oligomeric_details 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 # _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 2011-09-07 2 'Structure model' 1 1 2013-07-03 # _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 ? # _pdbx_audit_revision_group.ordinal 1 _pdbx_audit_revision_group.revision_ordinal 2 _pdbx_audit_revision_group.data_content_type 'Structure model' _pdbx_audit_revision_group.group 'Database references' # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal CNS refinement 1.3 ? 1 HKL-2000 'data collection' . ? 2 HKL-2000 'data reduction' . ? 3 HKL-2000 'data scaling' . ? 4 MOLREP phasing . ? 5 # _pdbx_entry_details.entry_id 3S9A _pdbx_entry_details.nonpolymer_details ? _pdbx_entry_details.sequence_details 'THE RESIDUE NUMBERING IS NOT SEQUENTIAL. THE RESIDUE NUMBERING IS BASED ON THE TOPOLOGICAL EQUIVALENCE TO CHYMOTRYPSINOGEN.' _pdbx_entry_details.compound_details ? _pdbx_entry_details.source_details ? # _pdbx_validate_close_contact.id 1 _pdbx_validate_close_contact.PDB_model_num 1 _pdbx_validate_close_contact.auth_atom_id_1 ND2 _pdbx_validate_close_contact.auth_asym_id_1 A _pdbx_validate_close_contact.auth_comp_id_1 ASN _pdbx_validate_close_contact.auth_seq_id_1 245 _pdbx_validate_close_contact.PDB_ins_code_1 ? _pdbx_validate_close_contact.label_alt_id_1 ? _pdbx_validate_close_contact.auth_atom_id_2 C2 _pdbx_validate_close_contact.auth_asym_id_2 A _pdbx_validate_close_contact.auth_comp_id_2 NAG _pdbx_validate_close_contact.auth_seq_id_2 301 _pdbx_validate_close_contact.PDB_ins_code_2 ? _pdbx_validate_close_contact.label_alt_id_2 ? _pdbx_validate_close_contact.dist 2.09 # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 HIS A 71 ? ? -127.80 -82.04 2 1 ASN A 93 ? ? -103.48 76.81 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 N-ACETYL-D-GLUCOSAMINE NAG 3 water HOH #