data_3S9C # _entry.id 3S9C # _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 3S9C RCSB RCSB065924 WWPDB D_1000065924 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.details _pdbx_database_related.content_type PDB 3S9A . unspecified PDB 3S9B . unspecified PDB 3SBK . unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 3S9C _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 3S9C _cell.length_a 101.200 _cell.length_b 101.200 _cell.length_c 44.200 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 120.00 _cell.Z_PDB 6 _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 3S9C _symmetry.space_group_name_H-M 'P 61' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 169 _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 polymer syn 'Coagulation factor V' 1665.806 1 ? ? 'UNP residues 1561-1574' ? 3 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 2 ? ? ? ? 4 non-polymer man BETA-D-MANNOSE 180.156 1 ? ? ? ? 5 non-polymer man BETA-D-GLUCOSE 180.156 1 ? ? ? ? 6 non-polymer man ALPHA-D-GLUCOSE 180.156 1 ? ? ? ? 7 non-polymer syn 'ACETATE ION' 59.044 4 ? ? ? ? 8 non-polymer syn 'ZINC ION' 65.409 3 ? ? ? ? 9 water nat water 18.015 196 ? ? ? ? # loop_ _entity_name_com.entity_id _entity_name_com.name 1 'Factor V-activating proteinase gamma, Snake venom factor V activator gamma' 2 'Activated protein C cofactor, Proaccelerin, labile factor' # loop_ _entity_poly.entity_id _entity_poly.type _entity_poly.nstd_linkage _entity_poly.nstd_monomer _entity_poly.pdbx_seq_one_letter_code _entity_poly.pdbx_seq_one_letter_code_can _entity_poly.pdbx_strand_id _entity_poly.pdbx_target_identifier 1 'polypeptide(L)' no no ;VVGGDECNINEHPFLVALYTSASSTIHCAGALINREWVLTAAHCDRRNIRIKLGMHSKNIRNEDEQIRVPRGKYFCLNTK FPNGLDKDIMLIRLRRPVTYSTHIAPVSLPSRSRGVGSRCRIMGWGKISTTTYPDVPHCTNIFIVKHKWCEPLYPWVPAD SRTLCAGILKGGRDTCHGDSGGPLICNGEMHGIVAGGSEPCGQHLKPAVYTKVFDYNNWIQSIIAGNRTVTCPP ; ;VVGGDECNINEHPFLVALYTSASSTIHCAGALINREWVLTAAHCDRRNIRIKLGMHSKNIRNEDEQIRVPRGKYFCLNTK FPNGLDKDIMLIRLRRPVTYSTHIAPVSLPSRSRGVGSRCRIMGWGKISTTTYPDVPHCTNIFIVKHKWCEPLYPWVPAD SRTLCAGILKGGRDTCHGDSGGPLICNGEMHGIVAGGSEPCGQHLKPAVYTKVFDYNNWIQSIIAGNRTVTCPP ; A ? 2 'polypeptide(L)' no no SRDPDNIAAWYLRS SRDPDNIAAWYLRS B ? # 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 2 1 SER n 2 2 ARG n 2 3 ASP n 2 4 PRO n 2 5 ASP n 2 6 ASN n 2 7 ILE n 2 8 ALA n 2 9 ALA n 2 10 TRP n 2 11 TYR n 2 12 LEU n 2 13 ARG n 2 14 SER 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 ? # _pdbx_entity_src_syn.entity_id 2 _pdbx_entity_src_syn.pdbx_src_id 1 _pdbx_entity_src_syn.pdbx_alt_source_flag sample _pdbx_entity_src_syn.pdbx_beg_seq_num ? _pdbx_entity_src_syn.pdbx_end_seq_num ? _pdbx_entity_src_syn.organism_scientific 'Homo sapiens' _pdbx_entity_src_syn.organism_common_name human _pdbx_entity_src_syn.ncbi_taxonomy_id 9606 _pdbx_entity_src_syn.details 'synthetic peptide' # loop_ _struct_ref.id _struct_ref.db_name _struct_ref.db_code _struct_ref.pdbx_db_accession _struct_ref.entity_id _struct_ref.pdbx_seq_one_letter_code _struct_ref.pdbx_align_begin _struct_ref.pdbx_db_isoform 1 UNP VSPG_DABRU P18965 1 ;VVGGDECNINEHPFLVALYTSASSTIHCAGALINREWVLTAAHCDRRNIRIKLGMHSKNIRNEDEQIRVPRGKYFCLNTK FPNGLDKDIMLIRLRRPVTYSTHIAPVSLPSRSRGVGSRCRIMGWGKISTTEDTYPDVPHCTNIFIVKHKWCEPLYPWVP ADSRTLCAGILKGGRDTCHGDSGGPLICNGEMHGIVAGGSEPCGQHLKPAVYTKVFDYNNWIQSIIAGNRTVTCPP ; 1 ? 2 UNP FA5_HUMAN P12259 2 SRDPDNIAAWYLRS 1561 ? # loop_ _struct_ref_seq.align_id _struct_ref_seq.ref_id _struct_ref_seq.pdbx_PDB_id_code _struct_ref_seq.pdbx_strand_id _struct_ref_seq.seq_align_beg _struct_ref_seq.pdbx_seq_align_beg_ins_code _struct_ref_seq.seq_align_end _struct_ref_seq.pdbx_seq_align_end_ins_code _struct_ref_seq.pdbx_db_accession _struct_ref_seq.db_align_beg _struct_ref_seq.pdbx_db_align_beg_ins_code _struct_ref_seq.db_align_end _struct_ref_seq.pdbx_db_align_end_ins_code _struct_ref_seq.pdbx_auth_seq_align_beg _struct_ref_seq.pdbx_auth_seq_align_end 1 1 3S9C A 1 ? 234 G P18965 1 ? 236 ? 16 245 2 2 3S9C B 1 ? 14 ? P12259 1561 ? 1574 ? 1533 1546 # 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 3S9C ? A ? ? UNP P18965 GLU 132 DELETION ? 1 1 3S9C ? 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 ACT non-polymer . 'ACETATE ION' ? 'C2 H3 O2 -1' 59.044 ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 BGC saccharide . BETA-D-GLUCOSE ? 'C6 H12 O6' 180.156 BMA D-saccharide . BETA-D-MANNOSE ? 'C6 H12 O6' 180.156 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GLC saccharide . ALPHA-D-GLUCOSE ? 'C6 H12 O6' 180.156 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 ZN non-polymer . 'ZINC ION' ? 'Zn 2' 65.409 # _exptl.entry_id 3S9C _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.36 _exptl_crystal.density_percent_sol 47.99 _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 6.0 _exptl_crystal_grow.pdbx_details '20% PEG 3350, 0.2M zinc acetate, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K' _exptl_crystal_grow.pdbx_pH_range . # _diffrn.id 1 _diffrn.ambient_temp 100 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector CCD _diffrn_detector.type 'RAYONIX MX-225' _diffrn_detector.pdbx_collection_date 2009-10-13 _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.entry_id 3S9C _reflns.observed_criterion_sigma_I 0 _reflns.observed_criterion_sigma_F 0 _reflns.d_resolution_low 30 _reflns.d_resolution_high 1.8 _reflns.number_obs 24029 _reflns.number_all 24272 _reflns.percent_possible_obs 99.0 _reflns.pdbx_Rmerge_I_obs 0.047 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 46.3 _reflns.B_iso_Wilson_estimate 19.2 _reflns.pdbx_redundancy 10.9 _reflns.R_free_details ? _reflns.limit_h_max ? _reflns.limit_h_min ? _reflns.limit_k_max ? _reflns.limit_k_min ? _reflns.limit_l_max ? _reflns.limit_l_min ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? _reflns.pdbx_ordinal 1 _reflns.pdbx_diffrn_id 1 # _reflns_shell.d_res_high 1.80 _reflns_shell.d_res_low 1.86 _reflns_shell.percent_possible_all 91.8 _reflns_shell.Rmerge_I_obs 0.296 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs 6.9 _reflns_shell.pdbx_redundancy ? _reflns_shell.percent_possible_obs ? _reflns_shell.number_unique_all 2213 _reflns_shell.number_measured_all ? _reflns_shell.number_measured_obs ? _reflns_shell.number_unique_obs ? _reflns_shell.pdbx_chi_squared ? _reflns_shell.pdbx_rejects ? _reflns_shell.pdbx_netI_over_sigmaI_obs ? _reflns_shell.number_possible ? _reflns_shell.Rmerge_F_all ? _reflns_shell.Rmerge_F_obs ? _reflns_shell.Rmerge_I_all ? _reflns_shell.meanI_over_sigI_all ? _reflns_shell.pdbx_Rrim_I_all ? _reflns_shell.pdbx_Rpim_I_all ? _reflns_shell.pdbx_ordinal 1 _reflns_shell.pdbx_diffrn_id 1 # _refine.entry_id 3S9C _refine.ls_number_reflns_obs 23944 _refine.ls_number_reflns_all 24272 _refine.pdbx_ls_sigma_I 0 _refine.pdbx_ls_sigma_F 0.0 _refine.pdbx_data_cutoff_high_absF 1637135.50 _refine.pdbx_data_cutoff_low_absF 0.000000 _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 29.21 _refine.ls_d_res_high 1.80 _refine.ls_percent_reflns_obs 99.0 _refine.ls_R_factor_obs 0.183 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.183 _refine.ls_R_factor_R_free 0.218 _refine.ls_R_factor_R_free_error 0.006 _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 4.9 _refine.ls_number_reflns_R_free 1162 _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 33.9 _refine.aniso_B[1][1] -7.13 _refine.aniso_B[2][2] -7.13 _refine.aniso_B[3][3] 14.26 _refine.aniso_B[1][2] 0.00 _refine.aniso_B[1][3] 0.00 _refine.aniso_B[2][3] 0.00 _refine.solvent_model_details 'FLAT MODEL' _refine.solvent_model_param_ksol 0.42 _refine.solvent_model_param_bsol 64.5738 _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 3S9A' _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.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_diffrn_id 1 _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.pdbx_overall_ESU_R ? _refine.pdbx_TLS_residual_ADP_flag ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_analyze.entry_id 3S9C _refine_analyze.Luzzati_coordinate_error_obs 0.19 _refine_analyze.Luzzati_sigma_a_obs 0.17 _refine_analyze.Luzzati_d_res_low_obs 5.00 _refine_analyze.Luzzati_coordinate_error_free 0.24 _refine_analyze.Luzzati_sigma_a_free 0.24 _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_analyze.pdbx_refine_id 'X-RAY DIFFRACTION' # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 1880 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 82 _refine_hist.number_atoms_solvent 196 _refine_hist.number_atoms_total 2158 _refine_hist.d_res_high 1.80 _refine_hist.d_res_low 29.21 # 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_restraint_function _refine_ls_restr.pdbx_refine_id c_bond_d 0.011 ? ? ? ? 'X-RAY DIFFRACTION' c_angle_deg 1.6 ? ? ? ? 'X-RAY DIFFRACTION' c_dihedral_angle_d 25.1 ? ? ? ? 'X-RAY DIFFRACTION' c_improper_angle_d 3.56 ? ? ? ? '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 1.80 _refine_ls_shell.d_res_low 1.91 _refine_ls_shell.number_reflns_R_work 3597 _refine_ls_shell.R_factor_R_work 0.238 _refine_ls_shell.percent_reflns_obs 94.7 _refine_ls_shell.R_factor_R_free 0.246 _refine_ls_shell.R_factor_R_free_error 0.018 _refine_ls_shell.percent_reflns_R_free 4.8 _refine_ls_shell.number_reflns_R_free 182 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? _refine_ls_shell.number_reflns_obs 2204 _refine_ls_shell.redundancy_reflns_obs ? # 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 dna-rna_rep.param dna-rna.top 'X-RAY DIFFRACTION' 3 water_rep.param water.top 'X-RAY DIFFRACTION' 4 ion.param ion.top 'X-RAY DIFFRACTION' 5 carbohydrate.param carbohydrate.top 'X-RAY DIFFRACTION' 6 act_xplor.param act_xplor_top.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 3S9C _struct.title ;Russell's viper venom serine proteinase, RVV-V in complex with the fragment (residues 1533-1546) of human factor V ; _struct.pdbx_descriptor 'Vipera russelli proteinase RVV-V gamma (E.C.3.4.21.95), Coagulation factor V' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 3S9C _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 ? D N N 3 ? E N N 4 ? F N N 5 ? G N N 6 ? H N N 7 ? I N N 7 ? J N N 7 ? K N N 7 ? L N N 8 ? M N N 8 ? N N N 8 ? O N N 9 ? P N N 9 ? # _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 ? GLY A 226 ? TYR A 234 GLY A 244 1 ? 11 # _struct_conf_type.id HELX_P _struct_conf_type.criteria ? _struct_conf_type.reference ? # loop_ _struct_conn.id _struct_conn.conn_type_id _struct_conn.pdbx_leaving_atom_flag _struct_conn.pdbx_PDB_id _struct_conn.ptnr1_label_asym_id _struct_conn.ptnr1_label_comp_id _struct_conn.ptnr1_label_seq_id _struct_conn.ptnr1_label_atom_id _struct_conn.pdbx_ptnr1_label_alt_id _struct_conn.pdbx_ptnr1_PDB_ins_code _struct_conn.pdbx_ptnr1_standard_comp_id _struct_conn.ptnr1_symmetry _struct_conn.ptnr2_label_asym_id _struct_conn.ptnr2_label_comp_id _struct_conn.ptnr2_label_seq_id _struct_conn.ptnr2_label_atom_id _struct_conn.pdbx_ptnr2_label_alt_id _struct_conn.pdbx_ptnr2_PDB_ins_code _struct_conn.ptnr1_auth_asym_id _struct_conn.ptnr1_auth_comp_id _struct_conn.ptnr1_auth_seq_id _struct_conn.ptnr2_auth_asym_id _struct_conn.ptnr2_auth_comp_id _struct_conn.ptnr2_auth_seq_id _struct_conn.ptnr2_symmetry _struct_conn.pdbx_ptnr3_label_atom_id _struct_conn.pdbx_ptnr3_label_seq_id _struct_conn.pdbx_ptnr3_label_comp_id _struct_conn.pdbx_ptnr3_label_asym_id _struct_conn.pdbx_ptnr3_label_alt_id _struct_conn.pdbx_ptnr3_PDB_ins_code _struct_conn.details _struct_conn.pdbx_dist_value _struct_conn.pdbx_value_order disulf1 disulf ? ? A CYS 7 SG ? ? ? 1_555 A CYS 139 SG ? ? A CYS 22 A CYS 157 1_555 ? ? ? ? ? ? ? 2.029 ? disulf2 disulf ? ? A CYS 28 SG ? ? ? 1_555 A CYS 44 SG ? ? A CYS 42 A CYS 58 1_555 ? ? ? ? ? ? ? 2.044 ? disulf3 disulf ? ? A CYS 76 SG ? ? ? 1_555 A CYS 232 SG ? E A CYS 91 A CYS 245 1_555 ? ? ? ? ? ? ? 2.035 ? disulf4 disulf ? ? A CYS 120 SG ? ? ? 1_555 A CYS 186 SG ? ? A CYS 136 A CYS 201 1_555 ? ? ? ? ? ? ? 2.044 ? disulf5 disulf ? ? A CYS 150 SG ? ? ? 1_555 A CYS 165 SG ? ? A CYS 168 A CYS 182 1_555 ? ? ? ? ? ? ? 2.031 ? disulf6 disulf ? ? A CYS 176 SG ? ? ? 1_555 A CYS 201 SG ? ? A CYS 191 A CYS 220 1_555 ? ? ? ? ? ? ? 2.045 ? covale1 covale ? ? C NAG . O4 ? ? ? 1_555 D NAG . C1 ? ? A NAG 801 A NAG 802 1_555 ? ? ? ? ? ? ? 1.384 ? covale2 covale ? ? D NAG . O4 ? ? ? 1_555 E BMA . C1 ? ? A NAG 802 A BMA 803 1_555 ? ? ? ? ? ? ? 1.387 ? covale3 covale ? ? A ASN 227 ND2 ? ? ? 1_555 C NAG . C1 ? ? A ASN 245 A NAG 801 1_555 ? ? ? ? ? ? ? 1.447 ? metalc1 metalc ? ? I ACT . OXT ? ? ? 1_555 M ZN . ZN ? ? A ACT 902 A ZN 502 1_555 ? ? ? ? ? ? ? 1.874 ? metalc2 metalc ? ? A GLU 199 OE2 ? ? ? 1_555 L ZN . ZN ? ? A GLU 218 A ZN 501 1_555 ? ? ? ? ? ? ? 1.882 ? metalc3 metalc ? ? H ACT . OXT ? ? ? 1_555 L ZN . ZN ? ? A ACT 901 A ZN 501 1_555 ? ? ? ? ? ? ? 1.987 ? metalc4 metalc ? ? K ACT . O ? ? ? 1_555 N ZN . ZN ? ? A ACT 904 A ZN 503 1_555 ? ? ? ? ? ? ? 2.002 ? metalc5 metalc ? ? A HIS 177 NE2 ? ? ? 1_555 L ZN . ZN ? ? A HIS 192 A ZN 501 1_555 ? ? ? ? ? ? ? 2.015 ? metalc6 metalc ? ? A ASN 10 OD1 ? ? ? 1_555 N ZN . ZN ? ? A ASN 25 A ZN 503 1_555 ? ? ? ? ? ? ? 2.018 ? metalc7 metalc ? ? A HIS 103 NE2 ? ? ? 1_555 N ZN . ZN ? ? A HIS 117 A ZN 503 1_555 ? ? ? ? ? ? ? 2.127 ? metalc8 metalc ? ? J ACT . OXT ? ? ? 1_555 N ZN . ZN ? ? A ACT 903 A ZN 503 1_555 ? ? ? ? ? ? ? 2.127 ? metalc9 metalc ? ? A HIS 138 NE2 ? ? ? 1_555 M ZN . ZN ? ? A HIS 156 A ZN 502 1_555 ? ? ? ? ? ? ? 2.145 ? metalc10 metalc ? ? J ACT . O ? ? ? 1_555 N ZN . ZN ? ? A ACT 903 A ZN 503 1_555 ? ? ? ? ? ? ? 2.555 ? metalc11 metalc ? ? H ACT . O ? ? ? 1_555 L ZN . ZN ? ? A ACT 901 A ZN 501 1_555 ? ? ? ? ? ? ? 2.691 ? metalc12 metalc ? ? M ZN . ZN ? ? ? 1_555 O HOH . O ? ? A ZN 502 A HOH 367 1_555 ? ? ? ? ? ? ? 2.024 ? metalc13 metalc ? ? M ZN . ZN ? ? ? 1_555 O HOH . O ? ? A ZN 502 A HOH 368 1_555 ? ? ? ? ? ? ? 2.180 ? metalc14 metalc ? ? M ZN . ZN ? ? ? 1_555 O HOH . O ? ? A ZN 502 A HOH 150 1_555 ? ? ? ? ? ? ? 2.355 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? metalc ? ? # _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 0.42 # 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 SER A 23 ? ASN A 34 ? SER A 37 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 ? TYR A 74 ? PRO A 85 TYR A 89 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id A 1 2 N ASP A 5 ? N ASP A 20 O CYS A 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 LYS A 52 ? O LYS A 67 N ALA A 17 ? N ALA A 32 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 ARG A 71 ? N ARG A 86 # loop_ _struct_site.id _struct_site.pdbx_evidence_code _struct_site.pdbx_auth_asym_id _struct_site.pdbx_auth_comp_id _struct_site.pdbx_auth_seq_id _struct_site.pdbx_auth_ins_code _struct_site.pdbx_num_residues _struct_site.details AC1 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NAG A 801' AC2 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NAG A 802' AC3 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE BMA A 803' AC4 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE BGC A 701' AC5 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE GLC A 702' AC6 Software ? ? ? ? 9 'BINDING SITE FOR RESIDUE ACT A 901' AC7 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE ACT A 902' AC8 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE ACT A 903' AC9 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE ACT A 904' BC1 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN A 501' BC2 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE ZN A 502' BC3 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN A 503' # loop_ _struct_site_gen.id _struct_site_gen.site_id _struct_site_gen.pdbx_num_res _struct_site_gen.label_comp_id _struct_site_gen.label_asym_id _struct_site_gen.label_seq_id _struct_site_gen.pdbx_auth_ins_code _struct_site_gen.auth_comp_id _struct_site_gen.auth_asym_id _struct_site_gen.auth_seq_id _struct_site_gen.label_atom_id _struct_site_gen.label_alt_id _struct_site_gen.symmetry _struct_site_gen.details 1 AC1 2 ASN A 227 ? ASN A 245 . ? 1_555 ? 2 AC1 2 NAG D . ? NAG A 802 . ? 1_555 ? 3 AC2 2 NAG C . ? NAG A 801 . ? 1_555 ? 4 AC2 2 BMA E . ? BMA A 803 . ? 1_555 ? 5 AC3 3 HOH O . ? HOH A 405 . ? 1_555 ? 6 AC3 3 HOH O . ? HOH A 411 . ? 1_555 ? 7 AC3 3 NAG D . ? NAG A 802 . ? 1_555 ? 8 AC4 8 TYR A 19 ? TYR A 34 . ? 1_555 ? 9 AC4 8 SER A 24 ? SER A 38 . ? 1_555 ? 10 AC4 8 ILE A 26 ? ILE A 40 . ? 1_555 ? 11 AC4 8 LYS A 52 ? LYS A 67 . ? 1_555 ? 12 AC4 8 MET A 55 ? MET A 70 . ? 1_555 ? 13 AC4 8 LYS A 58 ? LYS A 73 . ? 1_555 ? 14 AC4 8 HOH O . ? HOH A 251 . ? 1_555 ? 15 AC4 8 HOH O . ? HOH A 342 . ? 1_555 ? 16 AC5 6 ARG A 119 ? ARG A 135 . ? 1_555 ? 17 AC5 6 ARG A 121 ? ARG A 137 . ? 1_555 ? 18 AC5 6 ASN A 141 ? ASN A 159 . ? 1_555 ? 19 AC5 6 CYS A 186 ? CYS A 201 . ? 1_555 ? 20 AC5 6 ASN A 187 ? ASN A 202 . ? 1_555 ? 21 AC5 6 GLY A 188 ? GLY A 207 . ? 1_555 ? 22 AC6 9 LYS A 127 ? LYS A 143 . ? 1_555 ? 23 AC6 9 THR A 130 ? THR A 146 . ? 1_555 ? 24 AC6 9 CYS A 176 ? CYS A 191 . ? 1_555 ? 25 AC6 9 HIS A 177 ? HIS A 192 . ? 1_555 ? 26 AC6 9 GLU A 199 ? GLU A 218 . ? 1_555 ? 27 AC6 9 PRO A 200 ? PRO A 219 . ? 1_555 ? 28 AC6 9 CYS A 201 ? CYS A 220 . ? 1_555 ? 29 AC6 9 HIS A 204 ? HIS A 222 . ? 3_564 ? 30 AC6 9 ZN L . ? ZN A 501 . ? 1_555 ? 31 AC7 5 ILE A 128 ? ILE A 144 . ? 1_555 ? 32 AC7 5 HIS A 138 ? HIS A 156 . ? 1_555 ? 33 AC7 5 HOH O . ? HOH A 326 . ? 1_555 ? 34 AC7 5 HOH O . ? HOH A 367 . ? 1_555 ? 35 AC7 5 ZN M . ? ZN A 502 . ? 1_555 ? 36 AC8 6 ASN A 10 ? ASN A 25 . ? 1_555 ? 37 AC8 6 THR A 102 ? THR A 116 . ? 1_555 ? 38 AC8 6 HIS A 103 ? HIS A 117 . ? 1_555 ? 39 AC8 6 HOH O . ? HOH A 388 . ? 1_555 ? 40 AC8 6 ZN N . ? ZN A 503 . ? 1_555 ? 41 AC8 6 ACT K . ? ACT A 904 . ? 1_555 ? 42 AC9 6 ILE A 9 ? ILE A 24 . ? 1_555 ? 43 AC9 6 ASN A 10 ? ASN A 25 . ? 1_555 ? 44 AC9 6 HIS A 103 ? HIS A 117 . ? 1_555 ? 45 AC9 6 HOH O . ? HOH A 283 . ? 1_555 ? 46 AC9 6 ZN N . ? ZN A 503 . ? 1_555 ? 47 AC9 6 ACT J . ? ACT A 903 . ? 1_555 ? 48 BC1 4 HIS A 177 ? HIS A 192 . ? 1_555 ? 49 BC1 4 GLU A 199 ? GLU A 218 . ? 1_555 ? 50 BC1 4 HIS A 204 ? HIS A 222 . ? 3_564 ? 51 BC1 4 ACT H . ? ACT A 901 . ? 1_555 ? 52 BC2 5 HOH O . ? HOH A 150 . ? 1_555 ? 53 BC2 5 HIS A 138 ? HIS A 156 . ? 1_555 ? 54 BC2 5 HOH O . ? HOH A 367 . ? 1_555 ? 55 BC2 5 HOH O . ? HOH A 368 . ? 1_555 ? 56 BC2 5 ACT I . ? ACT A 902 . ? 1_555 ? 57 BC3 4 ASN A 10 ? ASN A 25 . ? 1_555 ? 58 BC3 4 HIS A 103 ? HIS A 117 . ? 1_555 ? 59 BC3 4 ACT J . ? ACT A 903 . ? 1_555 ? 60 BC3 4 ACT K . ? ACT A 904 . ? 1_555 ? # _database_PDB_matrix.entry_id 3S9C _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 3S9C _atom_sites.fract_transf_matrix[1][1] 0.009881 _atom_sites.fract_transf_matrix[1][2] 0.005705 _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] 0.011410 _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] 0.022624 _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 ZN # 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 ? 8.405 45.701 -5.912 1.00 19.47 ? 16 VAL A N 1 ATOM 2 C CA . VAL A 1 1 ? 9.329 46.413 -4.949 1.00 20.91 ? 16 VAL A CA 1 ATOM 3 C C . VAL A 1 1 ? 9.519 47.849 -5.405 1.00 22.73 ? 16 VAL A C 1 ATOM 4 O O . VAL A 1 1 ? 9.928 48.087 -6.551 1.00 24.03 ? 16 VAL A O 1 ATOM 5 C CB . VAL A 1 1 ? 10.713 45.730 -4.892 1.00 21.77 ? 16 VAL A CB 1 ATOM 6 C CG1 . VAL A 1 1 ? 11.696 46.582 -4.094 1.00 21.76 ? 16 VAL A CG1 1 ATOM 7 C CG2 . VAL A 1 1 ? 10.585 44.343 -4.264 1.00 19.17 ? 16 VAL A CG2 1 ATOM 8 N N . VAL A 1 2 ? 9.199 48.797 -4.526 1.00 21.90 ? 17 VAL A N 1 ATOM 9 C CA . VAL A 1 2 ? 9.360 50.211 -4.860 1.00 23.21 ? 17 VAL A CA 1 ATOM 10 C C . VAL A 1 2 ? 10.606 50.771 -4.177 1.00 23.50 ? 17 VAL A C 1 ATOM 11 O O . VAL A 1 2 ? 11.020 50.271 -3.122 1.00 21.93 ? 17 VAL A O 1 ATOM 12 C CB . VAL A 1 2 ? 8.114 51.054 -4.448 1.00 23.59 ? 17 VAL A CB 1 ATOM 13 C CG1 . VAL A 1 2 ? 6.881 50.551 -5.171 1.00 22.13 ? 17 VAL A CG1 1 ATOM 14 C CG2 . VAL A 1 2 ? 7.906 51.027 -2.938 1.00 21.52 ? 17 VAL A CG2 1 ATOM 15 N N . GLY A 1 3 ? 11.200 51.803 -4.791 1.00 24.39 ? 18 GLY A N 1 ATOM 16 C CA . GLY A 1 3 ? 12.397 52.421 -4.240 1.00 26.01 ? 18 GLY A CA 1 ATOM 17 C C . GLY A 1 3 ? 13.692 51.668 -4.478 1.00 26.64 ? 18 GLY A C 1 ATOM 18 O O . GLY A 1 3 ? 14.744 52.015 -3.929 1.00 28.08 ? 18 GLY A O 1 ATOM 19 N N . GLY A 1 4 ? 13.638 50.630 -5.306 1.00 27.75 ? 19 GLY A N 1 ATOM 20 C CA . GLY A 1 4 ? 14.825 49.839 -5.567 1.00 28.09 ? 19 GLY A CA 1 ATOM 21 C C . GLY A 1 4 ? 15.340 49.937 -6.995 1.00 28.68 ? 19 GLY A C 1 ATOM 22 O O . GLY A 1 4 ? 15.070 50.908 -7.698 1.00 28.47 ? 19 GLY A O 1 ATOM 23 N N . ASP A 1 5 ? 16.091 48.925 -7.408 1.00 28.01 ? 20 ASP A N 1 ATOM 24 C CA . ASP A 1 5 ? 16.671 48.855 -8.753 1.00 31.07 ? 20 ASP A CA 1 ATOM 25 C C . ASP A 1 5 ? 16.593 47.402 -9.217 1.00 29.89 ? 20 ASP A C 1 ATOM 26 O O . ASP A 1 5 ? 16.256 46.517 -8.439 1.00 28.29 ? 20 ASP A O 1 ATOM 27 C CB . ASP A 1 5 ? 18.149 49.271 -8.699 1.00 34.66 ? 20 ASP A CB 1 ATOM 28 C CG . ASP A 1 5 ? 18.355 50.601 -7.990 1.00 40.26 ? 20 ASP A CG 1 ATOM 29 O OD1 . ASP A 1 5 ? 18.093 51.649 -8.620 1.00 43.78 ? 20 ASP A OD1 1 ATOM 30 O OD2 . ASP A 1 5 ? 18.768 50.603 -6.799 1.00 43.17 ? 20 ASP A OD2 1 ATOM 31 N N . GLU A 1 6 ? 16.916 47.160 -10.483 1.00 30.48 ? 21 GLU A N 1 ATOM 32 C CA . GLU A 1 6 ? 16.926 45.804 -11.020 1.00 28.78 ? 21 GLU A CA 1 ATOM 33 C C . GLU A 1 6 ? 17.907 44.984 -10.184 1.00 28.53 ? 21 GLU A C 1 ATOM 34 O O . GLU A 1 6 ? 19.007 45.439 -9.862 1.00 28.14 ? 21 GLU A O 1 ATOM 35 C CB . GLU A 1 6 ? 17.385 45.819 -12.486 1.00 29.28 ? 21 GLU A CB 1 ATOM 36 C CG . GLU A 1 6 ? 17.370 44.464 -13.165 1.00 31.66 ? 21 GLU A CG 1 ATOM 37 C CD . GLU A 1 6 ? 17.802 44.541 -14.631 1.00 34.42 ? 21 GLU A CD 1 ATOM 38 O OE1 . GLU A 1 6 ? 17.976 45.669 -15.141 1.00 34.91 ? 21 GLU A OE1 1 ATOM 39 O OE2 . GLU A 1 6 ? 17.960 43.483 -15.271 1.00 34.20 ? 21 GLU A OE2 1 ATOM 40 N N . CYS A 1 7 ? 17.505 43.774 -9.813 1.00 27.35 ? 22 CYS A N 1 ATOM 41 C CA . CYS A 1 7 ? 18.372 42.913 -9.028 1.00 26.46 ? 22 CYS A CA 1 ATOM 42 C C . CYS A 1 7 ? 19.504 42.464 -9.935 1.00 28.27 ? 22 CYS A C 1 ATOM 43 O O . CYS A 1 7 ? 19.342 42.462 -11.150 1.00 27.06 ? 22 CYS A O 1 ATOM 44 C CB . CYS A 1 7 ? 17.631 41.649 -8.615 1.00 27.66 ? 22 CYS A CB 1 ATOM 45 S SG . CYS A 1 7 ? 16.155 41.893 -7.584 1.00 25.63 ? 22 CYS A SG 1 ATOM 46 N N . ASN A 1 8 ? 20.630 42.068 -9.354 1.00 28.70 ? 23 ASN A N 1 ATOM 47 C CA . ASN A 1 8 ? 21.701 41.543 -10.189 1.00 31.38 ? 23 ASN A CA 1 ATOM 48 C C . ASN A 1 8 ? 21.178 40.193 -10.684 1.00 31.05 ? 23 ASN A C 1 ATOM 49 O O . ASN A 1 8 ? 20.635 39.412 -9.900 1.00 27.53 ? 23 ASN A O 1 ATOM 50 C CB . ASN A 1 8 ? 22.986 41.356 -9.401 1.00 32.82 ? 23 ASN A CB 1 ATOM 51 C CG . ASN A 1 8 ? 24.082 40.757 -10.251 1.00 36.10 ? 23 ASN A CG 1 ATOM 52 O OD1 . ASN A 1 8 ? 24.236 39.540 -10.312 1.00 37.08 ? 23 ASN A OD1 1 ATOM 53 N ND2 . ASN A 1 8 ? 24.824 41.610 -10.950 1.00 37.81 ? 23 ASN A ND2 1 ATOM 54 N N . ILE A 1 9 ? 21.335 39.932 -11.982 1.00 30.61 ? 24 ILE A N 1 ATOM 55 C CA . ILE A 1 9 ? 20.845 38.705 -12.598 1.00 29.95 ? 24 ILE A CA 1 ATOM 56 C C . ILE A 1 9 ? 21.342 37.406 -11.941 1.00 30.04 ? 24 ILE A C 1 ATOM 57 O O . ILE A 1 9 ? 20.714 36.359 -12.083 1.00 30.49 ? 24 ILE A O 1 ATOM 58 C CB . ILE A 1 9 ? 21.185 38.698 -14.115 1.00 31.27 ? 24 ILE A CB 1 ATOM 59 C CG1 . ILE A 1 9 ? 20.423 37.579 -14.824 1.00 29.36 ? 24 ILE A CG1 1 ATOM 60 C CG2 . ILE A 1 9 ? 22.691 38.497 -14.311 1.00 32.37 ? 24 ILE A CG2 1 ATOM 61 C CD1 . ILE A 1 9 ? 20.245 37.808 -16.300 1.00 31.70 ? 24 ILE A CD1 1 ATOM 62 N N . ASN A 1 10 ? 22.430 37.468 -11.187 1.00 29.40 ? 25 ASN A N 1 ATOM 63 C CA . ASN A 1 10 ? 22.958 36.252 -10.569 1.00 29.86 ? 25 ASN A CA 1 ATOM 64 C C . ASN A 1 10 ? 22.838 36.186 -9.051 1.00 30.00 ? 25 ASN A C 1 ATOM 65 O O . ASN A 1 10 ? 23.321 35.227 -8.438 1.00 29.23 ? 25 ASN A O 1 ATOM 66 C CB . ASN A 1 10 ? 24.441 36.068 -10.950 1.00 33.16 ? 25 ASN A CB 1 ATOM 67 C CG . ASN A 1 10 ? 24.646 35.907 -12.445 1.00 34.10 ? 25 ASN A CG 1 ATOM 68 O OD1 . ASN A 1 10 ? 24.002 35.089 -13.080 1.00 35.37 ? 25 ASN A OD1 1 ATOM 69 N ND2 . ASN A 1 10 ? 25.559 36.690 -13.010 1.00 36.07 ? 25 ASN A ND2 1 ATOM 70 N N . GLU A 1 11 ? 22.177 37.169 -8.444 1.00 26.21 ? 26 GLU A N 1 ATOM 71 C CA . GLU A 1 11 ? 22.072 37.214 -6.986 1.00 26.50 ? 26 GLU A CA 1 ATOM 72 C C . GLU A 1 11 ? 20.804 36.580 -6.409 1.00 24.28 ? 26 GLU A C 1 ATOM 73 O O . GLU A 1 11 ? 20.643 36.539 -5.189 1.00 27.62 ? 26 GLU A O 1 ATOM 74 C CB . GLU A 1 11 ? 22.120 38.676 -6.494 1.00 25.94 ? 26 GLU A CB 1 ATOM 75 C CG . GLU A 1 11 ? 20.840 39.491 -6.795 1.00 28.98 ? 26 GLU A CG 1 ATOM 76 C CD . GLU A 1 11 ? 20.777 40.813 -6.029 1.00 33.90 ? 26 GLU A CD 1 ATOM 77 O OE1 . GLU A 1 11 ? 20.698 40.769 -4.787 1.00 33.35 ? 26 GLU A OE1 1 ATOM 78 O OE2 . GLU A 1 11 ? 20.804 41.894 -6.664 1.00 33.32 ? 26 GLU A OE2 1 ATOM 79 N N . HIS A 1 12 ? 19.911 36.104 -7.263 1.00 23.66 ? 27 HIS A N 1 ATOM 80 C CA . HIS A 1 12 ? 18.648 35.542 -6.768 1.00 23.65 ? 27 HIS A CA 1 ATOM 81 C C . HIS A 1 12 ? 18.305 34.163 -7.326 1.00 22.98 ? 27 HIS A C 1 ATOM 82 O O . HIS A 1 12 ? 17.171 33.929 -7.761 1.00 23.45 ? 27 HIS A O 1 ATOM 83 C CB . HIS A 1 12 ? 17.518 36.531 -7.096 1.00 21.71 ? 27 HIS A CB 1 ATOM 84 C CG . HIS A 1 12 ? 17.385 36.846 -8.559 1.00 21.31 ? 27 HIS A CG 1 ATOM 85 N ND1 . HIS A 1 12 ? 16.710 36.031 -9.439 1.00 21.30 ? 27 HIS A ND1 1 ATOM 86 C CD2 . HIS A 1 12 ? 17.836 37.896 -9.295 1.00 24.11 ? 27 HIS A CD2 1 ATOM 87 C CE1 . HIS A 1 12 ? 16.738 36.564 -10.650 1.00 24.39 ? 27 HIS A CE1 1 ATOM 88 N NE2 . HIS A 1 12 ? 17.415 37.698 -10.591 1.00 23.52 ? 27 HIS A NE2 1 ATOM 89 N N . PRO A 1 13 ? 19.260 33.216 -7.277 1.00 22.88 ? 28 PRO A N 1 ATOM 90 C CA . PRO A 1 13 ? 19.008 31.871 -7.808 1.00 23.85 ? 28 PRO A CA 1 ATOM 91 C C . PRO A 1 13 ? 17.918 31.062 -7.097 1.00 22.78 ? 28 PRO A C 1 ATOM 92 O O . PRO A 1 13 ? 17.388 30.103 -7.647 1.00 22.24 ? 28 PRO A O 1 ATOM 93 C CB . PRO A 1 13 ? 20.379 31.211 -7.722 1.00 24.86 ? 28 PRO A CB 1 ATOM 94 C CG . PRO A 1 13 ? 20.953 31.785 -6.465 1.00 24.67 ? 28 PRO A CG 1 ATOM 95 C CD . PRO A 1 13 ? 20.561 33.273 -6.575 1.00 24.53 ? 28 PRO A CD 1 ATOM 96 N N . PHE A 1 14 ? 17.588 31.461 -5.879 1.00 21.34 ? 29 PHE A N 1 ATOM 97 C CA . PHE A 1 14 ? 16.541 30.789 -5.098 1.00 21.25 ? 29 PHE A CA 1 ATOM 98 C C . PHE A 1 14 ? 15.177 31.441 -5.365 1.00 20.45 ? 29 PHE A C 1 ATOM 99 O O . PHE A 1 14 ? 14.148 30.915 -4.961 1.00 20.03 ? 29 PHE A O 1 ATOM 100 C CB . PHE A 1 14 ? 16.866 30.926 -3.609 1.00 20.69 ? 29 PHE A CB 1 ATOM 101 C CG . PHE A 1 14 ? 17.245 32.322 -3.220 1.00 20.83 ? 29 PHE A CG 1 ATOM 102 C CD1 . PHE A 1 14 ? 16.268 33.295 -3.016 1.00 23.77 ? 29 PHE A CD1 1 ATOM 103 C CD2 . PHE A 1 14 ? 18.599 32.695 -3.151 1.00 24.45 ? 29 PHE A CD2 1 ATOM 104 C CE1 . PHE A 1 14 ? 16.625 34.625 -2.756 1.00 23.22 ? 29 PHE A CE1 1 ATOM 105 C CE2 . PHE A 1 14 ? 18.974 34.017 -2.891 1.00 24.94 ? 29 PHE A CE2 1 ATOM 106 C CZ . PHE A 1 14 ? 17.991 34.987 -2.695 1.00 25.29 ? 29 PHE A CZ 1 ATOM 107 N N . LEU A 1 15 ? 15.166 32.582 -6.054 1.00 19.97 ? 30 LEU A N 1 ATOM 108 C CA . LEU A 1 15 ? 13.899 33.273 -6.301 1.00 19.14 ? 30 LEU A CA 1 ATOM 109 C C . LEU A 1 15 ? 13.055 32.646 -7.409 1.00 20.82 ? 30 LEU A C 1 ATOM 110 O O . LEU A 1 15 ? 13.537 32.432 -8.531 1.00 21.99 ? 30 LEU A O 1 ATOM 111 C CB . LEU A 1 15 ? 14.176 34.745 -6.636 1.00 19.40 ? 30 LEU A CB 1 ATOM 112 C CG . LEU A 1 15 ? 12.952 35.658 -6.734 1.00 19.32 ? 30 LEU A CG 1 ATOM 113 C CD1 . LEU A 1 15 ? 12.203 35.727 -5.358 1.00 19.31 ? 30 LEU A CD1 1 ATOM 114 C CD2 . LEU A 1 15 ? 13.426 37.058 -7.117 1.00 18.80 ? 30 LEU A CD2 1 ATOM 115 N N . VAL A 1 16 ? 11.804 32.337 -7.103 1.00 20.75 ? 31 VAL A N 1 ATOM 116 C CA . VAL A 1 16 ? 10.920 31.765 -8.111 1.00 18.72 ? 31 VAL A CA 1 ATOM 117 C C . VAL A 1 16 ? 9.719 32.682 -8.318 1.00 19.73 ? 31 VAL A C 1 ATOM 118 O O . VAL A 1 16 ? 9.349 33.448 -7.432 1.00 18.63 ? 31 VAL A O 1 ATOM 119 C CB . VAL A 1 16 ? 10.455 30.316 -7.744 1.00 20.49 ? 31 VAL A CB 1 ATOM 120 C CG1 . VAL A 1 16 ? 11.657 29.458 -7.424 1.00 21.22 ? 31 VAL A CG1 1 ATOM 121 C CG2 . VAL A 1 16 ? 9.475 30.329 -6.550 1.00 20.68 ? 31 VAL A CG2 1 ATOM 122 N N . ALA A 1 17 ? 9.127 32.619 -9.503 1.00 19.80 ? 32 ALA A N 1 ATOM 123 C CA . ALA A 1 17 ? 7.971 33.443 -9.835 1.00 20.71 ? 32 ALA A CA 1 ATOM 124 C C . ALA A 1 17 ? 6.719 32.579 -9.949 1.00 22.72 ? 32 ALA A C 1 ATOM 125 O O . ALA A 1 17 ? 6.753 31.509 -10.542 1.00 23.38 ? 32 ALA A O 1 ATOM 126 C CB . ALA A 1 17 ? 8.215 34.178 -11.165 1.00 23.07 ? 32 ALA A CB 1 ATOM 127 N N . LEU A 1 18 ? 5.620 33.038 -9.357 1.00 20.91 ? 33 LEU A N 1 ATOM 128 C CA . LEU A 1 18 ? 4.380 32.278 -9.444 1.00 21.94 ? 33 LEU A CA 1 ATOM 129 C C . LEU A 1 18 ? 3.394 32.958 -10.378 1.00 22.61 ? 33 LEU A C 1 ATOM 130 O O . LEU A 1 18 ? 3.196 34.180 -10.329 1.00 22.87 ? 33 LEU A O 1 ATOM 131 C CB . LEU A 1 18 ? 3.734 32.116 -8.070 1.00 20.87 ? 33 LEU A CB 1 ATOM 132 C CG . LEU A 1 18 ? 4.638 31.520 -6.981 1.00 25.09 ? 33 LEU A CG 1 ATOM 133 C CD1 . LEU A 1 18 ? 3.828 31.300 -5.666 1.00 22.32 ? 33 LEU A CD1 1 ATOM 134 C CD2 . LEU A 1 18 ? 5.252 30.222 -7.469 1.00 23.92 ? 33 LEU A CD2 1 ATOM 135 N N . TYR A 1 19 ? 2.783 32.161 -11.243 1.00 23.26 ? 34 TYR A N 1 ATOM 136 C CA . TYR A 1 19 ? 1.774 32.682 -12.155 1.00 25.75 ? 34 TYR A CA 1 ATOM 137 C C . TYR A 1 19 ? 0.768 31.558 -12.344 1.00 26.16 ? 34 TYR A C 1 ATOM 138 O O . TYR A 1 19 ? 0.691 30.677 -11.499 1.00 24.00 ? 34 TYR A O 1 ATOM 139 C CB . TYR A 1 19 ? 2.408 33.135 -13.480 1.00 26.33 ? 34 TYR A CB 1 ATOM 140 C CG . TYR A 1 19 ? 3.204 32.084 -14.220 1.00 28.98 ? 34 TYR A CG 1 ATOM 141 C CD1 . TYR A 1 19 ? 2.758 31.580 -15.446 1.00 29.97 ? 34 TYR A CD1 1 ATOM 142 C CD2 . TYR A 1 19 ? 4.407 31.606 -13.707 1.00 30.53 ? 34 TYR A CD2 1 ATOM 143 C CE1 . TYR A 1 19 ? 3.487 30.633 -16.140 1.00 31.67 ? 34 TYR A CE1 1 ATOM 144 C CE2 . TYR A 1 19 ? 5.145 30.650 -14.392 1.00 32.17 ? 34 TYR A CE2 1 ATOM 145 C CZ . TYR A 1 19 ? 4.676 30.170 -15.610 1.00 31.36 ? 34 TYR A CZ 1 ATOM 146 O OH . TYR A 1 19 ? 5.392 29.214 -16.283 1.00 33.62 ? 34 TYR A OH 1 ATOM 147 N N . THR A 1 20 ? -0.036 31.586 -13.397 1.00 28.74 ? 35 THR A N 1 ATOM 148 C CA . THR A 1 20 ? -0.985 30.488 -13.595 1.00 29.95 ? 35 THR A CA 1 ATOM 149 C C . THR A 1 20 ? -0.989 30.091 -15.067 1.00 32.26 ? 35 THR A C 1 ATOM 150 O O . THR A 1 20 ? -0.342 30.730 -15.893 1.00 31.38 ? 35 THR A O 1 ATOM 151 C CB . THR A 1 20 ? -2.437 30.860 -13.210 1.00 30.03 ? 35 THR A CB 1 ATOM 152 O OG1 . THR A 1 20 ? -2.968 31.758 -14.185 1.00 29.90 ? 35 THR A OG1 1 ATOM 153 C CG2 . THR A 1 20 ? -2.497 31.506 -11.812 1.00 27.58 ? 35 THR A CG2 1 ATOM 154 N N . SER A 1 21 ? -1.720 29.033 -15.385 1.00 34.42 ? 36 SER A N 1 ATOM 155 C CA . SER A 1 21 ? -1.807 28.568 -16.761 1.00 37.65 ? 36 SER A CA 1 ATOM 156 C C . SER A 1 21 ? -2.681 29.539 -17.552 1.00 39.54 ? 36 SER A C 1 ATOM 157 O O . SER A 1 21 ? -2.593 29.617 -18.771 1.00 41.22 ? 36 SER A O 1 ATOM 158 C CB . SER A 1 21 ? -2.428 27.174 -16.797 1.00 37.02 ? 36 SER A CB 1 ATOM 159 O OG . SER A 1 21 ? -3.697 27.199 -16.163 1.00 34.39 ? 36 SER A OG 1 ATOM 160 N N . ALA A 1 22 A -3.508 30.298 -16.848 1.00 40.06 ? 36 ALA A N 1 ATOM 161 C CA . ALA A 1 22 A -4.410 31.227 -17.503 1.00 41.96 ? 36 ALA A CA 1 ATOM 162 C C . ALA A 1 22 A -3.818 32.590 -17.821 1.00 42.72 ? 36 ALA A C 1 ATOM 163 O O . ALA A 1 22 A -4.381 33.331 -18.636 1.00 43.08 ? 36 ALA A O 1 ATOM 164 C CB . ALA A 1 22 A -5.665 31.401 -16.660 1.00 41.85 ? 36 ALA A CB 1 ATOM 165 N N . SER A 1 23 ? -2.683 32.923 -17.203 1.00 41.92 ? 37 SER A N 1 ATOM 166 C CA . SER A 1 23 ? -2.078 34.231 -17.419 1.00 42.12 ? 37 SER A CA 1 ATOM 167 C C . SER A 1 23 ? -0.562 34.259 -17.226 1.00 41.07 ? 37 SER A C 1 ATOM 168 O O . SER A 1 23 ? -0.007 33.437 -16.493 1.00 41.94 ? 37 SER A O 1 ATOM 169 C CB . SER A 1 23 ? -2.741 35.233 -16.467 1.00 43.16 ? 37 SER A CB 1 ATOM 170 O OG . SER A 1 23 ? -2.025 36.451 -16.422 1.00 46.37 ? 37 SER A OG 1 ATOM 171 N N . SER A 1 24 ? 0.100 35.214 -17.873 1.00 40.08 ? 38 SER A N 1 ATOM 172 C CA . SER A 1 24 ? 1.552 35.361 -17.747 1.00 39.64 ? 38 SER A CA 1 ATOM 173 C C . SER A 1 24 ? 1.883 36.334 -16.608 1.00 36.99 ? 38 SER A C 1 ATOM 174 O O . SER A 1 24 ? 3.053 36.537 -16.258 1.00 36.82 ? 38 SER A O 1 ATOM 175 C CB . SER A 1 24 ? 2.162 35.887 -19.047 1.00 40.45 ? 38 SER A CB 1 ATOM 176 O OG . SER A 1 24 ? 1.869 37.266 -19.215 1.00 44.26 ? 38 SER A OG 1 ATOM 177 N N . THR A 1 25 ? 0.845 36.933 -16.037 1.00 34.72 ? 39 THR A N 1 ATOM 178 C CA . THR A 1 25 ? 1.000 37.872 -14.923 1.00 31.87 ? 39 THR A CA 1 ATOM 179 C C . THR A 1 25 ? 1.638 37.160 -13.737 1.00 29.08 ? 39 THR A C 1 ATOM 180 O O . THR A 1 25 ? 1.192 36.087 -13.351 1.00 27.61 ? 39 THR A O 1 ATOM 181 C CB . THR A 1 25 ? -0.361 38.402 -14.467 1.00 32.18 ? 39 THR A CB 1 ATOM 182 O OG1 . THR A 1 25 ? -0.968 39.113 -15.549 1.00 36.45 ? 39 THR A OG1 1 ATOM 183 C CG2 . THR A 1 25 ? -0.209 39.334 -13.255 1.00 33.65 ? 39 THR A CG2 1 ATOM 184 N N . ILE A 1 26 ? 2.686 37.748 -13.166 1.00 26.51 ? 40 ILE A N 1 ATOM 185 C CA . ILE A 1 26 ? 3.326 37.135 -11.996 1.00 24.33 ? 40 ILE A CA 1 ATOM 186 C C . ILE A 1 26 ? 2.578 37.673 -10.771 1.00 24.82 ? 40 ILE A C 1 ATOM 187 O O . ILE A 1 26 ? 2.652 38.871 -10.466 1.00 25.91 ? 40 ILE A O 1 ATOM 188 C CB . ILE A 1 26 ? 4.824 37.501 -11.944 1.00 23.08 ? 40 ILE A CB 1 ATOM 189 C CG1 . ILE A 1 26 ? 5.532 36.844 -13.130 1.00 24.31 ? 40 ILE A CG1 1 ATOM 190 C CG2 . ILE A 1 26 ? 5.480 36.998 -10.625 1.00 22.27 ? 40 ILE A CG2 1 ATOM 191 C CD1 . ILE A 1 26 ? 6.963 37.238 -13.277 1.00 26.66 ? 40 ILE A CD1 1 ATOM 192 N N . HIS A 1 27 ? 1.822 36.818 -10.087 1.00 22.66 ? 41 HIS A N 1 ATOM 193 C CA . HIS A 1 27 ? 1.069 37.315 -8.931 1.00 21.97 ? 41 HIS A CA 1 ATOM 194 C C . HIS A 1 27 ? 1.775 37.186 -7.579 1.00 21.72 ? 41 HIS A C 1 ATOM 195 O O . HIS A 1 27 ? 1.303 37.730 -6.593 1.00 20.14 ? 41 HIS A O 1 ATOM 196 C CB . HIS A 1 27 ? -0.310 36.637 -8.851 1.00 22.86 ? 41 HIS A CB 1 ATOM 197 C CG . HIS A 1 27 ? -0.257 35.174 -8.513 1.00 21.08 ? 41 HIS A CG 1 ATOM 198 N ND1 . HIS A 1 27 ? -0.126 34.188 -9.471 1.00 21.04 ? 41 HIS A ND1 1 ATOM 199 C CD2 . HIS A 1 27 ? -0.255 34.537 -7.320 1.00 21.39 ? 41 HIS A CD2 1 ATOM 200 C CE1 . HIS A 1 27 ? -0.040 33.007 -8.880 1.00 21.10 ? 41 HIS A CE1 1 ATOM 201 N NE2 . HIS A 1 27 ? -0.112 33.190 -7.572 1.00 20.23 ? 41 HIS A NE2 1 ATOM 202 N N . CYS A 1 28 ? 2.894 36.466 -7.540 1.00 19.85 ? 42 CYS A N 1 ATOM 203 C CA . CYS A 1 28 ? 3.651 36.273 -6.314 1.00 19.56 ? 42 CYS A CA 1 ATOM 204 C C . CYS A 1 28 ? 5.018 35.717 -6.644 1.00 19.80 ? 42 CYS A C 1 ATOM 205 O O . CYS A 1 28 ? 5.303 35.381 -7.791 1.00 20.07 ? 42 CYS A O 1 ATOM 206 C CB . CYS A 1 28 ? 2.980 35.226 -5.422 1.00 19.37 ? 42 CYS A CB 1 ATOM 207 S SG . CYS A 1 28 ? 1.595 35.791 -4.376 1.00 19.72 ? 42 CYS A SG 1 ATOM 208 N N . ALA A 1 29 ? 5.854 35.611 -5.616 1.00 18.85 ? 43 ALA A N 1 ATOM 209 C CA . ALA A 1 29 ? 7.155 34.995 -5.777 1.00 18.22 ? 43 ALA A CA 1 ATOM 210 C C . ALA A 1 29 ? 7.192 33.901 -4.708 1.00 18.89 ? 43 ALA A C 1 ATOM 211 O O . ALA A 1 29 ? 6.184 33.658 -3.993 1.00 17.32 ? 43 ALA A O 1 ATOM 212 C CB . ALA A 1 29 ? 8.279 36.013 -5.555 1.00 18.50 ? 43 ALA A CB 1 ATOM 213 N N . GLY A 1 30 ? 8.325 33.217 -4.650 1.00 18.56 ? 44 GLY A N 1 ATOM 214 C CA . GLY A 1 30 ? 8.544 32.164 -3.671 1.00 19.98 ? 44 GLY A CA 1 ATOM 215 C C . GLY A 1 30 ? 10.041 31.911 -3.608 1.00 20.11 ? 44 GLY A C 1 ATOM 216 O O . GLY A 1 30 ? 10.823 32.582 -4.280 1.00 19.89 ? 44 GLY A O 1 ATOM 217 N N . ALA A 1 31 ? 10.454 30.955 -2.789 1.00 19.83 ? 45 ALA A N 1 ATOM 218 C CA . ALA A 1 31 ? 11.873 30.638 -2.683 1.00 19.39 ? 45 ALA A CA 1 ATOM 219 C C . ALA A 1 31 ? 12.090 29.134 -2.750 1.00 21.80 ? 45 ALA A C 1 ATOM 220 O O . ALA A 1 31 ? 11.356 28.352 -2.133 1.00 20.84 ? 45 ALA A O 1 ATOM 221 C CB . ALA A 1 31 ? 12.430 31.182 -1.375 1.00 20.30 ? 45 ALA A CB 1 ATOM 222 N N . LEU A 1 32 ? 13.087 28.728 -3.526 1.00 20.95 ? 46 LEU A N 1 ATOM 223 C CA . LEU A 1 32 ? 13.426 27.308 -3.629 1.00 22.64 ? 46 LEU A CA 1 ATOM 224 C C . LEU A 1 32 ? 14.202 26.969 -2.365 1.00 22.31 ? 46 LEU A C 1 ATOM 225 O O . LEU A 1 32 ? 15.181 27.654 -2.060 1.00 23.20 ? 46 LEU A O 1 ATOM 226 C CB . LEU A 1 32 ? 14.332 27.086 -4.852 1.00 22.55 ? 46 LEU A CB 1 ATOM 227 C CG . LEU A 1 32 ? 14.668 25.629 -5.203 1.00 25.27 ? 46 LEU A CG 1 ATOM 228 C CD1 . LEU A 1 32 ? 13.393 24.897 -5.659 1.00 22.44 ? 46 LEU A CD1 1 ATOM 229 C CD2 . LEU A 1 32 ? 15.729 25.619 -6.335 1.00 24.96 ? 46 LEU A CD2 1 ATOM 230 N N . ILE A 1 33 ? 13.804 25.936 -1.616 1.00 23.98 ? 47 ILE A N 1 ATOM 231 C CA . ILE A 1 33 ? 14.567 25.623 -0.400 1.00 25.67 ? 47 ILE A CA 1 ATOM 232 C C . ILE A 1 33 ? 15.321 24.279 -0.491 1.00 27.42 ? 47 ILE A C 1 ATOM 233 O O . ILE A 1 33 ? 16.090 23.925 0.397 1.00 28.91 ? 47 ILE A O 1 ATOM 234 C CB . ILE A 1 33 ? 13.693 25.717 0.889 1.00 28.84 ? 47 ILE A CB 1 ATOM 235 C CG1 . ILE A 1 33 ? 12.420 24.907 0.747 1.00 29.35 ? 47 ILE A CG1 1 ATOM 236 C CG2 . ILE A 1 33 ? 13.317 27.187 1.166 1.00 25.81 ? 47 ILE A CG2 1 ATOM 237 C CD1 . ILE A 1 33 ? 11.578 24.952 2.019 1.00 31.14 ? 47 ILE A CD1 1 ATOM 238 N N . ASN A 1 34 ? 15.060 23.557 -1.573 1.00 27.34 ? 48 ASN A N 1 ATOM 239 C CA . ASN A 1 34 ? 15.764 22.321 -1.942 1.00 30.19 ? 48 ASN A CA 1 ATOM 240 C C . ASN A 1 34 ? 15.298 21.937 -3.344 1.00 29.92 ? 48 ASN A C 1 ATOM 241 O O . ASN A 1 34 ? 14.486 22.649 -3.947 1.00 30.59 ? 48 ASN A O 1 ATOM 242 C CB . ASN A 1 34 ? 15.605 21.177 -0.921 1.00 33.36 ? 48 ASN A CB 1 ATOM 243 C CG . ASN A 1 34 ? 14.238 20.562 -0.914 1.00 36.74 ? 48 ASN A CG 1 ATOM 244 O OD1 . ASN A 1 34 ? 13.625 20.334 -1.959 1.00 39.11 ? 48 ASN A OD1 1 ATOM 245 N ND2 . ASN A 1 34 ? 13.751 20.259 0.283 1.00 39.07 ? 48 ASN A ND2 1 ATOM 246 N N . ARG A 1 35 ? 15.796 20.830 -3.884 1.00 27.61 ? 49 ARG A N 1 ATOM 247 C CA . ARG A 1 35 ? 15.451 20.455 -5.246 1.00 27.39 ? 49 ARG A CA 1 ATOM 248 C C . ARG A 1 35 ? 13.995 20.246 -5.612 1.00 26.06 ? 49 ARG A C 1 ATOM 249 O O . ARG A 1 35 ? 13.642 20.320 -6.783 1.00 25.20 ? 49 ARG A O 1 ATOM 250 C CB . ARG A 1 35 ? 16.219 19.201 -5.665 1.00 27.02 ? 49 ARG A CB 1 ATOM 251 C CG . ARG A 1 35 ? 17.694 19.417 -5.808 1.00 31.12 ? 49 ARG A CG 1 ATOM 252 C CD . ARG A 1 35 ? 18.381 18.125 -6.275 1.00 32.61 ? 49 ARG A CD 1 ATOM 253 N NE . ARG A 1 35 ? 19.825 18.275 -6.202 1.00 34.10 ? 49 ARG A NE 1 ATOM 254 C CZ . ARG A 1 35 ? 20.515 18.263 -5.072 1.00 30.36 ? 49 ARG A CZ 1 ATOM 255 N NH1 . ARG A 1 35 ? 19.897 18.092 -3.910 1.00 31.83 ? 49 ARG A NH1 1 ATOM 256 N NH2 . ARG A 1 35 ? 21.824 18.439 -5.113 1.00 36.15 ? 49 ARG A NH2 1 ATOM 257 N N . GLU A 1 36 ? 13.145 19.955 -4.644 1.00 26.91 ? 50 GLU A N 1 ATOM 258 C CA . GLU A 1 36 ? 11.755 19.749 -5.015 1.00 27.99 ? 50 GLU A CA 1 ATOM 259 C C . GLU A 1 36 ? 10.755 20.506 -4.159 1.00 26.30 ? 50 GLU A C 1 ATOM 260 O O . GLU A 1 36 ? 9.558 20.217 -4.203 1.00 25.29 ? 50 GLU A O 1 ATOM 261 C CB . GLU A 1 36 ? 11.426 18.255 -5.030 1.00 32.59 ? 50 GLU A CB 1 ATOM 262 C CG . GLU A 1 36 ? 11.452 17.561 -3.702 1.00 38.42 ? 50 GLU A CG 1 ATOM 263 C CD . GLU A 1 36 ? 11.384 16.036 -3.859 1.00 43.03 ? 50 GLU A CD 1 ATOM 264 O OE1 . GLU A 1 36 ? 10.559 15.548 -4.662 1.00 44.08 ? 50 GLU A OE1 1 ATOM 265 O OE2 . GLU A 1 36 ? 12.162 15.333 -3.179 1.00 46.61 ? 50 GLU A OE2 1 ATOM 266 N N . TRP A 1 37 ? 11.228 21.503 -3.418 1.00 24.18 ? 51 TRP A N 1 ATOM 267 C CA . TRP A 1 37 ? 10.311 22.269 -2.566 1.00 24.52 ? 51 TRP A CA 1 ATOM 268 C C . TRP A 1 37 ? 10.421 23.786 -2.677 1.00 22.87 ? 51 TRP A C 1 ATOM 269 O O . TRP A 1 37 ? 11.512 24.342 -2.675 1.00 20.37 ? 51 TRP A O 1 ATOM 270 C CB . TRP A 1 37 ? 10.508 21.904 -1.102 1.00 25.16 ? 51 TRP A CB 1 ATOM 271 C CG . TRP A 1 37 ? 10.120 20.504 -0.804 1.00 29.72 ? 51 TRP A CG 1 ATOM 272 C CD1 . TRP A 1 37 ? 10.918 19.393 -0.881 1.00 30.47 ? 51 TRP A CD1 1 ATOM 273 C CD2 . TRP A 1 37 ? 8.831 20.054 -0.374 1.00 28.99 ? 51 TRP A CD2 1 ATOM 274 N NE1 . TRP A 1 37 ? 10.195 18.275 -0.513 1.00 31.12 ? 51 TRP A NE1 1 ATOM 275 C CE2 . TRP A 1 37 ? 8.914 18.652 -0.198 1.00 30.48 ? 51 TRP A CE2 1 ATOM 276 C CE3 . TRP A 1 37 ? 7.613 20.699 -0.119 1.00 28.77 ? 51 TRP A CE3 1 ATOM 277 C CZ2 . TRP A 1 37 ? 7.819 17.880 0.225 1.00 30.64 ? 51 TRP A CZ2 1 ATOM 278 C CZ3 . TRP A 1 37 ? 6.523 19.940 0.299 1.00 28.21 ? 51 TRP A CZ3 1 ATOM 279 C CH2 . TRP A 1 37 ? 6.637 18.537 0.470 1.00 32.33 ? 51 TRP A CH2 1 ATOM 280 N N . VAL A 1 38 ? 9.267 24.436 -2.744 1.00 22.83 ? 52 VAL A N 1 ATOM 281 C CA . VAL A 1 38 ? 9.212 25.891 -2.821 1.00 20.89 ? 52 VAL A CA 1 ATOM 282 C C . VAL A 1 38 ? 8.429 26.414 -1.630 1.00 22.12 ? 52 VAL A C 1 ATOM 283 O O . VAL A 1 38 ? 7.353 25.887 -1.320 1.00 20.23 ? 52 VAL A O 1 ATOM 284 C CB . VAL A 1 38 ? 8.531 26.364 -4.139 1.00 21.16 ? 52 VAL A CB 1 ATOM 285 C CG1 . VAL A 1 38 ? 8.131 27.854 -4.028 1.00 21.53 ? 52 VAL A CG1 1 ATOM 286 C CG2 . VAL A 1 38 ? 9.503 26.179 -5.313 1.00 19.95 ? 52 VAL A CG2 1 ATOM 287 N N . LEU A 1 39 ? 8.962 27.449 -0.973 1.00 21.99 ? 53 LEU A N 1 ATOM 288 C CA . LEU A 1 39 ? 8.305 28.077 0.187 1.00 21.83 ? 53 LEU A CA 1 ATOM 289 C C . LEU A 1 39 ? 7.724 29.419 -0.286 1.00 21.39 ? 53 LEU A C 1 ATOM 290 O O . LEU A 1 39 ? 8.431 30.207 -0.910 1.00 20.75 ? 53 LEU A O 1 ATOM 291 C CB . LEU A 1 39 ? 9.331 28.317 1.304 1.00 21.68 ? 53 LEU A CB 1 ATOM 292 C CG . LEU A 1 39 ? 8.886 29.019 2.604 1.00 22.93 ? 53 LEU A CG 1 ATOM 293 C CD1 . LEU A 1 39 ? 7.842 28.161 3.313 1.00 21.64 ? 53 LEU A CD1 1 ATOM 294 C CD2 . LEU A 1 39 ? 10.087 29.292 3.517 1.00 24.78 ? 53 LEU A CD2 1 ATOM 295 N N . THR A 1 40 ? 6.448 29.679 0.002 1.00 20.10 ? 54 THR A N 1 ATOM 296 C CA . THR A 1 40 ? 5.822 30.931 -0.431 1.00 20.76 ? 54 THR A CA 1 ATOM 297 C C . THR A 1 40 ? 4.705 31.290 0.559 1.00 19.63 ? 54 THR A C 1 ATOM 298 O O . THR A 1 40 ? 4.678 30.756 1.673 1.00 21.32 ? 54 THR A O 1 ATOM 299 C CB . THR A 1 40 ? 5.285 30.773 -1.899 1.00 18.75 ? 54 THR A CB 1 ATOM 300 O OG1 . THR A 1 40 ? 4.705 31.996 -2.362 1.00 17.61 ? 54 THR A OG1 1 ATOM 301 C CG2 . THR A 1 40 ? 4.268 29.662 -1.986 1.00 20.83 ? 54 THR A CG2 1 ATOM 302 N N . ALA A 1 41 ? 3.805 32.199 0.186 1.00 19.92 ? 55 ALA A N 1 ATOM 303 C CA . ALA A 1 41 ? 2.728 32.568 1.108 1.00 19.39 ? 55 ALA A CA 1 ATOM 304 C C . ALA A 1 41 ? 1.459 31.803 0.729 1.00 19.96 ? 55 ALA A C 1 ATOM 305 O O . ALA A 1 41 ? 1.217 31.525 -0.446 1.00 18.75 ? 55 ALA A O 1 ATOM 306 C CB . ALA A 1 41 ? 2.462 34.090 1.068 1.00 20.89 ? 55 ALA A CB 1 ATOM 307 N N . ALA A 1 42 ? 0.643 31.472 1.731 1.00 19.32 ? 56 ALA A N 1 ATOM 308 C CA . ALA A 1 42 ? -0.598 30.758 1.486 1.00 20.28 ? 56 ALA A CA 1 ATOM 309 C C . ALA A 1 42 ? -1.548 31.510 0.560 1.00 19.86 ? 56 ALA A C 1 ATOM 310 O O . ALA A 1 42 ? -2.225 30.900 -0.271 1.00 20.17 ? 56 ALA A O 1 ATOM 311 C CB . ALA A 1 42 ? -1.312 30.454 2.837 1.00 22.13 ? 56 ALA A CB 1 ATOM 312 N N . HIS A 1 43 ? -1.606 32.845 0.665 1.00 21.06 ? 57 HIS A N 1 ATOM 313 C CA . HIS A 1 43 ? -2.534 33.561 -0.199 1.00 21.33 ? 57 HIS A CA 1 ATOM 314 C C . HIS A 1 43 ? -2.128 33.609 -1.666 1.00 20.31 ? 57 HIS A C 1 ATOM 315 O O . HIS A 1 43 ? -2.894 34.060 -2.507 1.00 20.04 ? 57 HIS A O 1 ATOM 316 C CB . HIS A 1 43 ? -2.867 34.962 0.372 1.00 20.87 ? 57 HIS A CB 1 ATOM 317 C CG . HIS A 1 43 ? -1.861 36.031 0.060 1.00 20.03 ? 57 HIS A CG 1 ATOM 318 N ND1 . HIS A 1 43 ? -0.932 36.483 0.978 1.00 20.88 ? 57 HIS A ND1 1 ATOM 319 C CD2 . HIS A 1 43 ? -1.715 36.809 -1.039 1.00 18.68 ? 57 HIS A CD2 1 ATOM 320 C CE1 . HIS A 1 43 ? -0.268 37.504 0.458 1.00 18.64 ? 57 HIS A CE1 1 ATOM 321 N NE2 . HIS A 1 43 ? -0.729 37.721 -0.764 1.00 17.34 ? 57 HIS A NE2 1 ATOM 322 N N . CYS A 1 44 ? -0.930 33.098 -1.976 1.00 21.08 ? 58 CYS A N 1 ATOM 323 C CA . CYS A 1 44 ? -0.437 33.047 -3.366 1.00 20.03 ? 58 CYS A CA 1 ATOM 324 C C . CYS A 1 44 ? -0.947 31.821 -4.101 1.00 21.48 ? 58 CYS A C 1 ATOM 325 O O . CYS A 1 44 ? -0.744 31.655 -5.307 1.00 19.49 ? 58 CYS A O 1 ATOM 326 C CB . CYS A 1 44 ? 1.095 33.011 -3.361 1.00 22.03 ? 58 CYS A CB 1 ATOM 327 S SG . CYS A 1 44 ? 1.845 34.565 -2.760 1.00 20.47 ? 58 CYS A SG 1 ATOM 328 N N . ASP A 1 45 ? -1.592 30.932 -3.368 1.00 21.33 ? 59 ASP A N 1 ATOM 329 C CA . ASP A 1 45 ? -2.119 29.713 -3.978 1.00 23.01 ? 59 ASP A CA 1 ATOM 330 C C . ASP A 1 45 ? -3.157 30.039 -5.056 1.00 22.81 ? 59 ASP A C 1 ATOM 331 O O . ASP A 1 45 ? -3.937 30.999 -4.933 1.00 21.76 ? 59 ASP A O 1 ATOM 332 C CB . ASP A 1 45 ? -2.756 28.827 -2.895 1.00 22.30 ? 59 ASP A CB 1 ATOM 333 C CG . ASP A 1 45 ? -3.127 27.456 -3.414 1.00 27.79 ? 59 ASP A CG 1 ATOM 334 O OD1 . ASP A 1 45 ? -4.005 26.816 -2.796 1.00 28.47 ? 59 ASP A OD1 1 ATOM 335 O OD2 . ASP A 1 45 ? -2.544 27.022 -4.429 1.00 26.48 ? 59 ASP A OD2 1 ATOM 336 N N . ARG A 1 46 ? -3.143 29.246 -6.126 1.00 23.31 ? 60 ARG A N 1 ATOM 337 C CA . ARG A 1 46 ? -4.101 29.377 -7.215 1.00 24.92 ? 60 ARG A CA 1 ATOM 338 C C . ARG A 1 46 ? -4.409 27.952 -7.656 1.00 26.44 ? 60 ARG A C 1 ATOM 339 O O . ARG A 1 46 ? -3.580 27.041 -7.505 1.00 26.68 ? 60 ARG A O 1 ATOM 340 C CB . ARG A 1 46 ? -3.513 30.168 -8.385 1.00 25.01 ? 60 ARG A CB 1 ATOM 341 C CG . ARG A 1 46 ? -3.223 31.631 -8.057 1.00 23.27 ? 60 ARG A CG 1 ATOM 342 C CD . ARG A 1 46 ? -4.509 32.440 -7.824 1.00 24.17 ? 60 ARG A CD 1 ATOM 343 N NE . ARG A 1 46 ? -4.225 33.884 -7.727 1.00 25.47 ? 60 ARG A NE 1 ATOM 344 C CZ . ARG A 1 46 ? -3.763 34.509 -6.639 1.00 23.78 ? 60 ARG A CZ 1 ATOM 345 N NH1 . ARG A 1 46 ? -3.522 33.855 -5.508 1.00 25.00 ? 60 ARG A NH1 1 ATOM 346 N NH2 . ARG A 1 46 ? -3.520 35.809 -6.692 1.00 24.96 ? 60 ARG A NH2 1 ATOM 347 N N . ARG A 1 47 ? -5.584 27.729 -8.205 1.00 29.13 ? 62 ARG A N 1 ATOM 348 C CA . ARG A 1 47 ? -5.898 26.358 -8.573 1.00 30.31 ? 62 ARG A CA 1 ATOM 349 C C . ARG A 1 47 ? -5.059 25.791 -9.707 1.00 31.00 ? 62 ARG A C 1 ATOM 350 O O . ARG A 1 47 ? -4.844 24.577 -9.763 1.00 33.11 ? 62 ARG A O 1 ATOM 351 C CB . ARG A 1 47 ? -7.393 26.232 -8.887 1.00 33.89 ? 62 ARG A CB 1 ATOM 352 C CG . ARG A 1 47 ? -7.869 26.995 -10.074 1.00 35.02 ? 62 ARG A CG 1 ATOM 353 C CD . ARG A 1 47 ? -9.373 26.717 -10.253 1.00 38.56 ? 62 ARG A CD 1 ATOM 354 N NE . ARG A 1 47 ? -9.813 27.001 -11.610 1.00 39.42 ? 62 ARG A NE 1 ATOM 355 C CZ . ARG A 1 47 ? -10.254 28.181 -12.032 1.00 41.69 ? 62 ARG A CZ 1 ATOM 356 N NH1 . ARG A 1 47 ? -10.623 28.322 -13.301 1.00 42.43 ? 62 ARG A NH1 1 ATOM 357 N NH2 . ARG A 1 47 ? -10.340 29.209 -11.194 1.00 41.99 ? 62 ARG A NH2 1 ATOM 358 N N . ASN A 1 48 ? -4.561 26.667 -10.577 1.00 29.26 ? 63 ASN A N 1 ATOM 359 C CA . ASN A 1 48 ? -3.762 26.285 -11.740 1.00 32.06 ? 63 ASN A CA 1 ATOM 360 C C . ASN A 1 48 ? -2.383 26.957 -11.694 1.00 30.41 ? 63 ASN A C 1 ATOM 361 O O . ASN A 1 48 ? -1.887 27.462 -12.703 1.00 29.43 ? 63 ASN A O 1 ATOM 362 C CB . ASN A 1 48 ? -4.498 26.746 -13.000 1.00 36.16 ? 63 ASN A CB 1 ATOM 363 C CG . ASN A 1 48 ? -4.938 28.228 -12.913 1.00 40.57 ? 63 ASN A CG 1 ATOM 364 O OD1 . ASN A 1 48 ? -5.048 28.802 -11.816 1.00 37.63 ? 63 ASN A OD1 1 ATOM 365 N ND2 . ASN A 1 48 ? -5.204 28.837 -14.070 1.00 42.21 ? 63 ASN A ND2 1 ATOM 366 N N . ILE A 1 49 ? -1.762 26.947 -10.527 1.00 30.62 ? 64 ILE A N 1 ATOM 367 C CA . ILE A 1 49 ? -0.476 27.614 -10.354 1.00 29.13 ? 64 ILE A CA 1 ATOM 368 C C . ILE A 1 49 ? 0.666 27.045 -11.215 1.00 29.77 ? 64 ILE A C 1 ATOM 369 O O . ILE A 1 49 ? 0.722 25.839 -11.496 1.00 27.90 ? 64 ILE A O 1 ATOM 370 C CB . ILE A 1 49 ? -0.120 27.621 -8.836 1.00 30.13 ? 64 ILE A CB 1 ATOM 371 C CG1 . ILE A 1 49 ? 0.746 28.835 -8.503 1.00 31.99 ? 64 ILE A CG1 1 ATOM 372 C CG2 . ILE A 1 49 ? 0.558 26.336 -8.437 1.00 29.96 ? 64 ILE A CG2 1 ATOM 373 C CD1 . ILE A 1 49 ? 0.986 28.999 -7.010 1.00 32.46 ? 64 ILE A CD1 1 ATOM 374 N N . ARG A 1 50 ? 1.542 27.942 -11.679 1.00 27.83 ? 65 ARG A N 1 ATOM 375 C CA . ARG A 1 50 ? 2.715 27.581 -12.485 1.00 27.75 ? 65 ARG A CA 1 ATOM 376 C C . ARG A 1 50 ? 3.904 28.254 -11.799 1.00 26.12 ? 65 ARG A C 1 ATOM 377 O O . ARG A 1 50 ? 3.769 29.349 -11.270 1.00 25.78 ? 65 ARG A O 1 ATOM 378 C CB . ARG A 1 50 ? 2.594 28.116 -13.921 1.00 30.36 ? 65 ARG A CB 1 ATOM 379 C CG . ARG A 1 50 ? 1.502 27.439 -14.762 1.00 35.69 ? 65 ARG A CG 1 ATOM 380 C CD . ARG A 1 50 ? 1.894 26.007 -15.070 1.00 39.16 ? 65 ARG A CD 1 ATOM 381 N NE . ARG A 1 50 ? 0.891 25.272 -15.842 1.00 42.56 ? 65 ARG A NE 1 ATOM 382 C CZ . ARG A 1 50 ? -0.212 24.732 -15.324 1.00 44.10 ? 65 ARG A CZ 1 ATOM 383 N NH1 . ARG A 1 50 ? -1.057 24.081 -16.110 1.00 45.24 ? 65 ARG A NH1 1 ATOM 384 N NH2 . ARG A 1 50 ? -0.475 24.836 -14.021 1.00 42.97 ? 65 ARG A NH2 1 ATOM 385 N N . ILE A 1 51 ? 5.056 27.600 -11.810 1.00 26.95 ? 66 ILE A N 1 ATOM 386 C CA . ILE A 1 51 ? 6.236 28.153 -11.163 1.00 26.64 ? 66 ILE A CA 1 ATOM 387 C C . ILE A 1 51 ? 7.415 28.228 -12.104 1.00 26.94 ? 66 ILE A C 1 ATOM 388 O O . ILE A 1 51 ? 7.802 27.206 -12.686 1.00 26.46 ? 66 ILE A O 1 ATOM 389 C CB . ILE A 1 51 ? 6.668 27.287 -9.960 1.00 25.65 ? 66 ILE A CB 1 ATOM 390 C CG1 . ILE A 1 51 ? 5.527 27.201 -8.940 1.00 28.82 ? 66 ILE A CG1 1 ATOM 391 C CG2 . ILE A 1 51 ? 7.892 27.870 -9.312 1.00 24.99 ? 66 ILE A CG2 1 ATOM 392 C CD1 . ILE A 1 51 ? 5.802 26.232 -7.841 1.00 32.98 ? 66 ILE A CD1 1 ATOM 393 N N . LYS A 1 52 ? 7.995 29.418 -12.233 1.00 26.15 ? 67 LYS A N 1 ATOM 394 C CA . LYS A 1 52 ? 9.174 29.600 -13.087 1.00 27.71 ? 67 LYS A CA 1 ATOM 395 C C . LYS A 1 52 ? 10.398 29.711 -12.180 1.00 26.97 ? 67 LYS A C 1 ATOM 396 O O . LYS A 1 52 ? 10.428 30.552 -11.266 1.00 25.45 ? 67 LYS A O 1 ATOM 397 C CB . LYS A 1 52 ? 9.051 30.877 -13.926 1.00 29.33 ? 67 LYS A CB 1 ATOM 398 C CG . LYS A 1 52 ? 9.735 30.810 -15.294 1.00 37.06 ? 67 LYS A CG 1 ATOM 399 C CD . LYS A 1 52 ? 8.844 30.119 -16.311 1.00 37.24 ? 67 LYS A CD 1 ATOM 400 C CE . LYS A 1 52 ? 9.431 30.156 -17.724 1.00 39.39 ? 67 LYS A CE 1 ATOM 401 N NZ . LYS A 1 52 ? 9.547 31.541 -18.281 1.00 37.85 ? 67 LYS A NZ 1 ATOM 402 N N . LEU A 1 53 ? 11.394 28.858 -12.425 1.00 24.75 ? 68 LEU A N 1 ATOM 403 C CA . LEU A 1 53 ? 12.628 28.851 -11.664 1.00 24.18 ? 68 LEU A CA 1 ATOM 404 C C . LEU A 1 53 ? 13.796 29.253 -12.582 1.00 24.66 ? 68 LEU A C 1 ATOM 405 O O . LEU A 1 53 ? 13.758 29.003 -13.788 1.00 25.38 ? 68 LEU A O 1 ATOM 406 C CB . LEU A 1 53 ? 12.883 27.458 -11.079 1.00 24.71 ? 68 LEU A CB 1 ATOM 407 C CG . LEU A 1 53 ? 11.764 26.911 -10.186 1.00 24.61 ? 68 LEU A CG 1 ATOM 408 C CD1 . LEU A 1 53 ? 10.877 25.962 -10.993 1.00 25.52 ? 68 LEU A CD1 1 ATOM 409 C CD2 . LEU A 1 53 ? 12.365 26.194 -8.998 1.00 25.86 ? 68 LEU A CD2 1 ATOM 410 N N . GLY A 1 54 ? 14.826 29.857 -12.008 1.00 24.43 ? 69 GLY A N 1 ATOM 411 C CA . GLY A 1 54 ? 15.965 30.273 -12.809 1.00 26.53 ? 69 GLY A CA 1 ATOM 412 C C . GLY A 1 54 ? 15.651 31.435 -13.730 1.00 27.13 ? 69 GLY A C 1 ATOM 413 O O . GLY A 1 54 ? 16.337 31.637 -14.746 1.00 26.93 ? 69 GLY A O 1 ATOM 414 N N . MET A 1 55 ? 14.631 32.224 -13.390 1.00 25.67 ? 70 MET A N 1 ATOM 415 C CA . MET A 1 55 ? 14.259 33.337 -14.248 1.00 26.01 ? 70 MET A CA 1 ATOM 416 C C . MET A 1 55 ? 14.652 34.704 -13.718 1.00 27.71 ? 70 MET A C 1 ATOM 417 O O . MET A 1 55 ? 14.730 34.911 -12.504 1.00 26.48 ? 70 MET A O 1 ATOM 418 C CB . MET A 1 55 ? 12.743 33.322 -14.489 1.00 26.30 ? 70 MET A CB 1 ATOM 419 C CG . MET A 1 55 ? 12.206 34.451 -15.372 1.00 29.76 ? 70 MET A CG 1 ATOM 420 S SD . MET A 1 55 ? 10.426 34.292 -15.661 1.00 32.59 ? 70 MET A SD 1 ATOM 421 C CE . MET A 1 55 ? 9.748 35.107 -14.161 1.00 28.53 ? 70 MET A CE 1 ATOM 422 N N . HIS A 1 56 ? 14.924 35.627 -14.643 1.00 27.58 ? 71 HIS A N 1 ATOM 423 C CA . HIS A 1 56 ? 15.220 37.012 -14.296 1.00 27.70 ? 71 HIS A CA 1 ATOM 424 C C . HIS A 1 56 ? 14.137 37.760 -15.089 1.00 29.93 ? 71 HIS A C 1 ATOM 425 O O . HIS A 1 56 ? 13.010 37.963 -14.609 1.00 27.76 ? 71 HIS A O 1 ATOM 426 C CB . HIS A 1 56 ? 16.631 37.402 -14.768 1.00 29.22 ? 71 HIS A CB 1 ATOM 427 C CG . HIS A 1 56 ? 17.041 38.790 -14.375 1.00 30.26 ? 71 HIS A CG 1 ATOM 428 N ND1 . HIS A 1 56 ? 17.304 39.150 -13.070 1.00 29.20 ? 71 HIS A ND1 1 ATOM 429 C CD2 . HIS A 1 56 ? 17.211 39.914 -15.118 1.00 29.38 ? 71 HIS A CD2 1 ATOM 430 C CE1 . HIS A 1 56 ? 17.615 40.435 -13.024 1.00 31.44 ? 71 HIS A CE1 1 ATOM 431 N NE2 . HIS A 1 56 ? 17.564 40.922 -14.253 1.00 29.59 ? 71 HIS A NE2 1 ATOM 432 N N . SER A 1 57 ? 14.448 38.124 -16.330 1.00 30.86 ? 72 SER A N 1 ATOM 433 C CA . SER A 1 57 ? 13.465 38.787 -17.164 1.00 32.82 ? 72 SER A CA 1 ATOM 434 C C . SER A 1 57 ? 12.318 37.842 -17.545 1.00 35.07 ? 72 SER A C 1 ATOM 435 O O . SER A 1 57 ? 12.551 36.687 -17.931 1.00 34.38 ? 72 SER A O 1 ATOM 436 C CB . SER A 1 57 ? 14.116 39.311 -18.450 1.00 35.10 ? 72 SER A CB 1 ATOM 437 O OG . SER A 1 57 ? 13.111 39.618 -19.394 1.00 35.79 ? 72 SER A OG 1 ATOM 438 N N . LYS A 1 58 ? 11.091 38.347 -17.430 1.00 36.22 ? 73 LYS A N 1 ATOM 439 C CA . LYS A 1 58 ? 9.868 37.616 -17.768 1.00 40.99 ? 73 LYS A CA 1 ATOM 440 C C . LYS A 1 58 ? 9.825 37.223 -19.246 1.00 42.90 ? 73 LYS A C 1 ATOM 441 O O . LYS A 1 58 ? 9.122 36.277 -19.622 1.00 42.96 ? 73 LYS A O 1 ATOM 442 C CB . LYS A 1 58 ? 8.627 38.492 -17.565 1.00 42.82 ? 73 LYS A CB 1 ATOM 443 C CG . LYS A 1 58 ? 8.150 38.737 -16.166 1.00 46.13 ? 73 LYS A CG 1 ATOM 444 C CD . LYS A 1 58 ? 6.873 39.583 -16.240 1.00 46.63 ? 73 LYS A CD 1 ATOM 445 C CE . LYS A 1 58 ? 5.807 38.891 -17.107 1.00 48.35 ? 73 LYS A CE 1 ATOM 446 N NZ . LYS A 1 58 ? 4.488 39.590 -17.114 1.00 48.37 ? 73 LYS A NZ 1 ATOM 447 N N . ASN A 1 59 ? 10.537 37.985 -20.074 1.00 44.55 ? 74 ASN A N 1 ATOM 448 C CA . ASN A 1 59 ? 10.526 37.773 -21.523 1.00 48.13 ? 74 ASN A CA 1 ATOM 449 C C . ASN A 1 59 ? 11.775 37.141 -22.124 1.00 49.44 ? 74 ASN A C 1 ATOM 450 O O . ASN A 1 59 ? 11.696 36.439 -23.132 1.00 51.25 ? 74 ASN A O 1 ATOM 451 C CB . ASN A 1 59 ? 10.260 39.109 -22.232 1.00 49.12 ? 74 ASN A CB 1 ATOM 452 C CG . ASN A 1 59 ? 9.086 39.866 -21.631 1.00 50.74 ? 74 ASN A CG 1 ATOM 453 O OD1 . ASN A 1 59 ? 8.028 39.287 -21.366 1.00 51.21 ? 74 ASN A OD1 1 ATOM 454 N ND2 . ASN A 1 59 ? 9.266 41.173 -21.416 1.00 52.59 ? 74 ASN A ND2 1 ATOM 455 N N . ILE A 1 60 ? 12.924 37.412 -21.520 1.00 48.68 ? 75 ILE A N 1 ATOM 456 C CA . ILE A 1 60 ? 14.191 36.869 -21.990 1.00 47.61 ? 75 ILE A CA 1 ATOM 457 C C . ILE A 1 60 ? 14.556 35.674 -21.108 1.00 47.07 ? 75 ILE A C 1 ATOM 458 O O . ILE A 1 60 ? 14.933 35.853 -19.953 1.00 45.87 ? 75 ILE A O 1 ATOM 459 C CB . ILE A 1 60 ? 15.301 37.916 -21.866 1.00 47.42 ? 75 ILE A CB 1 ATOM 460 C CG1 . ILE A 1 60 ? 14.834 39.238 -22.475 1.00 48.32 ? 75 ILE A CG1 1 ATOM 461 C CG2 . ILE A 1 60 ? 16.561 37.411 -22.542 1.00 47.64 ? 75 ILE A CG2 1 ATOM 462 C CD1 . ILE A 1 60 ? 15.861 40.342 -22.387 1.00 48.78 ? 75 ILE A CD1 1 ATOM 463 N N . ARG A 1 61 ? 14.454 34.465 -21.655 1.00 46.14 ? 76 ARG A N 1 ATOM 464 C CA . ARG A 1 61 ? 14.755 33.248 -20.894 1.00 46.48 ? 76 ARG A CA 1 ATOM 465 C C . ARG A 1 61 ? 16.232 32.960 -20.643 1.00 44.78 ? 76 ARG A C 1 ATOM 466 O O . ARG A 1 61 ? 17.064 33.164 -21.523 1.00 45.23 ? 76 ARG A O 1 ATOM 467 C CB . ARG A 1 61 ? 14.156 32.029 -21.599 1.00 48.79 ? 76 ARG A CB 1 ATOM 468 C CG . ARG A 1 61 ? 12.650 32.046 -21.736 1.00 52.45 ? 76 ARG A CG 1 ATOM 469 C CD . ARG A 1 61 ? 12.144 30.835 -22.522 1.00 55.81 ? 76 ARG A CD 1 ATOM 470 N NE . ARG A 1 61 ? 12.479 29.555 -21.895 1.00 58.41 ? 76 ARG A NE 1 ATOM 471 C CZ . ARG A 1 61 ? 13.653 28.936 -22.012 1.00 59.55 ? 76 ARG A CZ 1 ATOM 472 N NH1 . ARG A 1 61 ? 13.858 27.777 -21.401 1.00 59.87 ? 76 ARG A NH1 1 ATOM 473 N NH2 . ARG A 1 61 ? 14.621 29.465 -22.748 1.00 61.15 ? 76 ARG A NH2 1 ATOM 474 N N . ASN A 1 62 ? 16.555 32.499 -19.434 1.00 41.27 ? 77 ASN A N 1 ATOM 475 C CA . ASN A 1 62 ? 17.924 32.118 -19.105 1.00 39.42 ? 77 ASN A CA 1 ATOM 476 C C . ASN A 1 62 ? 18.050 30.697 -19.655 1.00 38.73 ? 77 ASN A C 1 ATOM 477 O O . ASN A 1 62 ? 17.054 29.987 -19.765 1.00 37.11 ? 77 ASN A O 1 ATOM 478 C CB . ASN A 1 62 ? 18.169 32.080 -17.589 1.00 36.98 ? 77 ASN A CB 1 ATOM 479 C CG . ASN A 1 62 ? 18.422 33.453 -17.000 1.00 37.03 ? 77 ASN A CG 1 ATOM 480 O OD1 . ASN A 1 62 ? 18.900 34.358 -17.688 1.00 35.08 ? 77 ASN A OD1 1 ATOM 481 N ND2 . ASN A 1 62 ? 18.125 33.611 -15.713 1.00 33.84 ? 77 ASN A ND2 1 ATOM 482 N N . GLU A 1 63 ? 19.267 30.279 -19.984 1.00 39.45 ? 78 GLU A N 1 ATOM 483 C CA . GLU A 1 63 ? 19.479 28.949 -20.538 1.00 39.03 ? 78 GLU A CA 1 ATOM 484 C C . GLU A 1 63 ? 18.949 27.829 -19.638 1.00 38.24 ? 78 GLU A C 1 ATOM 485 O O . GLU A 1 63 ? 18.451 26.813 -20.126 1.00 37.08 ? 78 GLU A O 1 ATOM 486 C CB . GLU A 1 63 ? 20.973 28.733 -20.797 1.00 42.69 ? 78 GLU A CB 1 ATOM 487 C CG . GLU A 1 63 ? 21.300 27.408 -21.493 1.00 46.87 ? 78 GLU A CG 1 ATOM 488 C CD . GLU A 1 63 ? 21.512 26.244 -20.532 1.00 48.79 ? 78 GLU A CD 1 ATOM 489 O OE1 . GLU A 1 63 ? 21.504 25.081 -21.002 1.00 49.95 ? 78 GLU A OE1 1 ATOM 490 O OE2 . GLU A 1 63 ? 21.706 26.490 -19.318 1.00 50.23 ? 78 GLU A OE2 1 ATOM 491 N N . ASP A 1 64 ? 19.058 28.013 -18.325 1.00 36.04 ? 79 ASP A N 1 ATOM 492 C CA . ASP A 1 64 ? 18.607 26.992 -17.389 1.00 34.39 ? 79 ASP A CA 1 ATOM 493 C C . ASP A 1 64 ? 17.238 27.225 -16.739 1.00 34.03 ? 79 ASP A C 1 ATOM 494 O O . ASP A 1 64 ? 16.917 26.565 -15.752 1.00 34.84 ? 79 ASP A O 1 ATOM 495 C CB . ASP A 1 64 ? 19.661 26.783 -16.287 1.00 34.16 ? 79 ASP A CB 1 ATOM 496 C CG . ASP A 1 64 ? 20.062 28.080 -15.587 1.00 32.96 ? 79 ASP A CG 1 ATOM 497 O OD1 . ASP A 1 64 ? 20.530 28.008 -14.428 1.00 34.19 ? 79 ASP A OD1 1 ATOM 498 O OD2 . ASP A 1 64 ? 19.930 29.167 -16.185 1.00 33.27 ? 79 ASP A OD2 1 ATOM 499 N N . GLU A 1 65 ? 16.451 28.146 -17.296 1.00 32.68 ? 80 GLU A N 1 ATOM 500 C CA . GLU A 1 65 ? 15.114 28.478 -16.781 1.00 33.18 ? 80 GLU A CA 1 ATOM 501 C C . GLU A 1 65 ? 14.203 27.254 -16.855 1.00 33.95 ? 80 GLU A C 1 ATOM 502 O O . GLU A 1 65 ? 14.195 26.534 -17.857 1.00 34.02 ? 80 GLU A O 1 ATOM 503 C CB . GLU A 1 65 ? 14.527 29.624 -17.599 1.00 32.41 ? 80 GLU A CB 1 ATOM 504 C CG . GLU A 1 65 ? 13.314 30.313 -16.989 1.00 32.26 ? 80 GLU A CG 1 ATOM 505 C CD . GLU A 1 65 ? 13.080 31.675 -17.614 1.00 31.29 ? 80 GLU A CD 1 ATOM 506 O OE1 . GLU A 1 65 ? 14.046 32.454 -17.676 1.00 35.21 ? 80 GLU A OE1 1 ATOM 507 O OE2 . GLU A 1 65 ? 11.953 31.975 -18.046 1.00 35.00 ? 80 GLU A OE2 1 ATOM 508 N N . GLN A 1 66 ? 13.427 27.034 -15.801 1.00 32.69 ? 81 GLN A N 1 ATOM 509 C CA . GLN A 1 66 ? 12.538 25.874 -15.716 1.00 33.77 ? 81 GLN A CA 1 ATOM 510 C C . GLN A 1 66 ? 11.108 26.237 -15.312 1.00 32.89 ? 81 GLN A C 1 ATOM 511 O O . GLN A 1 66 ? 10.880 27.212 -14.593 1.00 29.86 ? 81 GLN A O 1 ATOM 512 C CB . GLN A 1 66 ? 13.052 24.898 -14.656 1.00 34.79 ? 81 GLN A CB 1 ATOM 513 C CG . GLN A 1 66 ? 14.451 24.367 -14.854 1.00 39.06 ? 81 GLN A CG 1 ATOM 514 C CD . GLN A 1 66 ? 14.515 23.363 -15.967 1.00 40.44 ? 81 GLN A CD 1 ATOM 515 O OE1 . GLN A 1 66 ? 13.670 22.465 -16.055 1.00 42.07 ? 81 GLN A OE1 1 ATOM 516 N NE2 . GLN A 1 66 ? 15.521 23.493 -16.824 1.00 43.19 ? 81 GLN A NE2 1 ATOM 517 N N . ILE A 1 67 ? 10.165 25.418 -15.760 1.00 31.55 ? 82 ILE A N 1 ATOM 518 C CA . ILE A 1 67 ? 8.762 25.579 -15.409 1.00 33.12 ? 82 ILE A CA 1 ATOM 519 C C . ILE A 1 67 ? 8.362 24.331 -14.630 1.00 33.12 ? 82 ILE A C 1 ATOM 520 O O . ILE A 1 67 ? 8.729 23.212 -15.005 1.00 32.86 ? 82 ILE A O 1 ATOM 521 C CB . ILE A 1 67 ? 7.846 25.655 -16.648 1.00 34.22 ? 82 ILE A CB 1 ATOM 522 C CG1 . ILE A 1 67 ? 8.147 26.917 -17.448 1.00 34.14 ? 82 ILE A CG1 1 ATOM 523 C CG2 . ILE A 1 67 ? 6.383 25.668 -16.207 1.00 36.95 ? 82 ILE A CG2 1 ATOM 524 C CD1 . ILE A 1 67 ? 7.333 27.048 -18.714 1.00 35.93 ? 82 ILE A CD1 1 ATOM 525 N N . ARG A 1 68 ? 7.636 24.513 -13.533 1.00 30.47 ? 83 ARG A N 1 ATOM 526 C CA . ARG A 1 68 ? 7.155 23.370 -12.758 1.00 28.32 ? 83 ARG A CA 1 ATOM 527 C C . ARG A 1 68 ? 5.733 23.628 -12.299 1.00 28.14 ? 83 ARG A C 1 ATOM 528 O O . ARG A 1 68 ? 5.270 24.777 -12.274 1.00 26.97 ? 83 ARG A O 1 ATOM 529 C CB . ARG A 1 68 ? 8.023 23.115 -11.521 1.00 27.55 ? 83 ARG A CB 1 ATOM 530 C CG . ARG A 1 68 ? 9.426 22.627 -11.800 1.00 28.96 ? 83 ARG A CG 1 ATOM 531 C CD . ARG A 1 68 ? 9.429 21.193 -12.386 1.00 30.23 ? 83 ARG A CD 1 ATOM 532 N NE . ARG A 1 68 ? 10.787 20.653 -12.505 1.00 29.26 ? 83 ARG A NE 1 ATOM 533 C CZ . ARG A 1 68 ? 11.610 20.885 -13.527 1.00 31.13 ? 83 ARG A CZ 1 ATOM 534 N NH1 . ARG A 1 68 ? 11.232 21.647 -14.550 1.00 28.61 ? 83 ARG A NH1 1 ATOM 535 N NH2 . ARG A 1 68 ? 12.827 20.364 -13.517 1.00 30.79 ? 83 ARG A NH2 1 ATOM 536 N N . VAL A 1 69 ? 5.045 22.548 -11.951 1.00 27.94 ? 84 VAL A N 1 ATOM 537 C CA . VAL A 1 69 ? 3.694 22.633 -11.426 1.00 29.59 ? 84 VAL A CA 1 ATOM 538 C C . VAL A 1 69 ? 3.799 21.840 -10.141 1.00 28.91 ? 84 VAL A C 1 ATOM 539 O O . VAL A 1 69 ? 4.718 21.050 -9.966 1.00 30.23 ? 84 VAL A O 1 ATOM 540 C CB . VAL A 1 69 ? 2.632 21.980 -12.346 1.00 30.95 ? 84 VAL A CB 1 ATOM 541 C CG1 . VAL A 1 69 ? 2.625 22.675 -13.701 1.00 33.37 ? 84 VAL A CG1 1 ATOM 542 C CG2 . VAL A 1 69 ? 2.906 20.471 -12.484 1.00 31.73 ? 84 VAL A CG2 1 ATOM 543 N N . PRO A 1 70 ? 2.858 22.038 -9.221 1.00 29.88 ? 85 PRO A N 1 ATOM 544 C CA . PRO A 1 70 ? 2.888 21.325 -7.951 1.00 28.78 ? 85 PRO A CA 1 ATOM 545 C C . PRO A 1 70 ? 2.499 19.857 -8.024 1.00 29.76 ? 85 PRO A C 1 ATOM 546 O O . PRO A 1 70 ? 1.749 19.458 -8.905 1.00 31.51 ? 85 PRO A O 1 ATOM 547 C CB . PRO A 1 70 ? 1.859 22.079 -7.101 1.00 27.44 ? 85 PRO A CB 1 ATOM 548 C CG . PRO A 1 70 ? 1.616 23.361 -7.831 1.00 29.37 ? 85 PRO A CG 1 ATOM 549 C CD . PRO A 1 70 ? 1.718 22.964 -9.268 1.00 29.64 ? 85 PRO A CD 1 ATOM 550 N N . ARG A 1 71 ? 3.014 19.065 -7.094 1.00 29.79 ? 86 ARG A N 1 ATOM 551 C CA . ARG A 1 71 ? 2.578 17.684 -6.990 1.00 32.59 ? 86 ARG A CA 1 ATOM 552 C C . ARG A 1 71 ? 1.928 17.639 -5.603 1.00 32.84 ? 86 ARG A C 1 ATOM 553 O O . ARG A 1 71 ? 1.314 16.642 -5.218 1.00 35.40 ? 86 ARG A O 1 ATOM 554 C CB . ARG A 1 71 ? 3.736 16.678 -7.096 1.00 34.27 ? 86 ARG A CB 1 ATOM 555 C CG . ARG A 1 71 ? 4.825 16.830 -6.072 1.00 39.53 ? 86 ARG A CG 1 ATOM 556 C CD . ARG A 1 71 ? 5.806 15.671 -6.158 1.00 42.36 ? 86 ARG A CD 1 ATOM 557 N NE . ARG A 1 71 ? 5.188 14.402 -5.773 1.00 44.76 ? 86 ARG A NE 1 ATOM 558 C CZ . ARG A 1 71 ? 5.861 13.264 -5.624 1.00 46.90 ? 86 ARG A CZ 1 ATOM 559 N NH1 . ARG A 1 71 ? 7.171 13.238 -5.834 1.00 47.46 ? 86 ARG A NH1 1 ATOM 560 N NH2 . ARG A 1 71 ? 5.230 12.154 -5.256 1.00 48.40 ? 86 ARG A NH2 1 ATOM 561 N N . GLY A 1 72 ? 2.039 18.744 -4.862 1.00 30.67 ? 87 GLY A N 1 ATOM 562 C CA . GLY A 1 72 ? 1.447 18.809 -3.536 1.00 27.77 ? 87 GLY A CA 1 ATOM 563 C C . GLY A 1 72 ? 1.546 20.204 -2.929 1.00 29.23 ? 87 GLY A C 1 ATOM 564 O O . GLY A 1 72 ? 2.496 20.946 -3.205 1.00 28.38 ? 87 GLY A O 1 ATOM 565 N N . LYS A 1 73 ? 0.571 20.571 -2.104 1.00 27.46 ? 88 LYS A N 1 ATOM 566 C CA . LYS A 1 73 ? 0.573 21.881 -1.458 1.00 26.96 ? 88 LYS A CA 1 ATOM 567 C C . LYS A 1 73 ? 0.286 21.671 0.019 1.00 27.32 ? 88 LYS A C 1 ATOM 568 O O . LYS A 1 73 ? -0.617 20.915 0.376 1.00 28.43 ? 88 LYS A O 1 ATOM 569 C CB . LYS A 1 73 ? -0.494 22.767 -2.071 1.00 26.15 ? 88 LYS A CB 1 ATOM 570 C CG . LYS A 1 73 ? -0.332 23.002 -3.568 1.00 26.07 ? 88 LYS A CG 1 ATOM 571 C CD . LYS A 1 73 ? -1.544 23.792 -4.028 1.00 27.22 ? 88 LYS A CD 1 ATOM 572 C CE . LYS A 1 73 ? -1.531 24.035 -5.496 1.00 29.07 ? 88 LYS A CE 1 ATOM 573 N NZ . LYS A 1 73 ? -2.777 24.722 -5.896 1.00 24.50 ? 88 LYS A NZ 1 ATOM 574 N N . TYR A 1 74 ? 1.033 22.344 0.874 1.00 25.69 ? 89 TYR A N 1 ATOM 575 C CA . TYR A 1 74 ? 0.879 22.178 2.304 1.00 26.66 ? 89 TYR A CA 1 ATOM 576 C C . TYR A 1 74 ? 0.731 23.478 3.070 1.00 28.74 ? 89 TYR A C 1 ATOM 577 O O . TYR A 1 74 ? 1.521 24.414 2.903 1.00 27.54 ? 89 TYR A O 1 ATOM 578 C CB . TYR A 1 74 ? 2.057 21.382 2.859 1.00 26.44 ? 89 TYR A CB 1 ATOM 579 C CG . TYR A 1 74 ? 2.216 20.064 2.146 1.00 27.76 ? 89 TYR A CG 1 ATOM 580 C CD1 . TYR A 1 74 ? 2.921 19.981 0.952 1.00 27.69 ? 89 TYR A CD1 1 ATOM 581 C CD2 . TYR A 1 74 ? 1.551 18.930 2.599 1.00 29.95 ? 89 TYR A CD2 1 ATOM 582 C CE1 . TYR A 1 74 ? 2.954 18.798 0.203 1.00 32.84 ? 89 TYR A CE1 1 ATOM 583 C CE2 . TYR A 1 74 ? 1.573 17.734 1.864 1.00 32.98 ? 89 TYR A CE2 1 ATOM 584 C CZ . TYR A 1 74 ? 2.270 17.673 0.668 1.00 34.55 ? 89 TYR A CZ 1 ATOM 585 O OH . TYR A 1 74 ? 2.250 16.515 -0.081 1.00 35.45 ? 89 TYR A OH 1 ATOM 586 N N . PHE A 1 75 ? -0.283 23.508 3.924 1.00 28.09 ? 90 PHE A N 1 ATOM 587 C CA . PHE A 1 75 ? -0.589 24.670 4.739 1.00 30.60 ? 90 PHE A CA 1 ATOM 588 C C . PHE A 1 75 ? -0.592 24.298 6.220 1.00 34.67 ? 90 PHE A C 1 ATOM 589 O O . PHE A 1 75 ? -0.572 23.116 6.586 1.00 33.87 ? 90 PHE A O 1 ATOM 590 C CB . PHE A 1 75 ? -1.975 25.213 4.384 1.00 28.78 ? 90 PHE A CB 1 ATOM 591 C CG . PHE A 1 75 ? -2.198 25.428 2.913 1.00 27.99 ? 90 PHE A CG 1 ATOM 592 C CD1 . PHE A 1 75 ? -2.578 24.376 2.090 1.00 25.79 ? 90 PHE A CD1 1 ATOM 593 C CD2 . PHE A 1 75 ? -2.023 26.692 2.352 1.00 27.52 ? 90 PHE A CD2 1 ATOM 594 C CE1 . PHE A 1 75 ? -2.785 24.570 0.728 1.00 27.68 ? 90 PHE A CE1 1 ATOM 595 C CE2 . PHE A 1 75 ? -2.227 26.897 0.990 1.00 26.24 ? 90 PHE A CE2 1 ATOM 596 C CZ . PHE A 1 75 ? -2.606 25.844 0.180 1.00 27.56 ? 90 PHE A CZ 1 ATOM 597 N N . CYS A 1 76 ? -0.625 25.320 7.066 1.00 36.13 ? 91 CYS A N 1 ATOM 598 C CA . CYS A 1 76 ? -0.664 25.119 8.502 1.00 38.30 ? 91 CYS A CA 1 ATOM 599 C C . CYS A 1 76 ? -1.995 24.487 8.841 1.00 39.96 ? 91 CYS A C 1 ATOM 600 O O . CYS A 1 76 ? -3.035 24.897 8.322 1.00 37.67 ? 91 CYS A O 1 ATOM 601 C CB . CYS A 1 76 ? -0.561 26.447 9.228 1.00 38.45 ? 91 CYS A CB 1 ATOM 602 S SG . CYS A 1 76 ? 1.129 27.048 9.276 1.00 36.88 ? 91 CYS A SG 1 ATOM 603 N N . LEU A 1 77 ? -1.948 23.493 9.721 1.00 43.17 ? 92 LEU A N 1 ATOM 604 C CA . LEU A 1 77 ? -3.141 22.782 10.144 1.00 44.25 ? 92 LEU A CA 1 ATOM 605 C C . LEU A 1 77 ? -3.962 23.614 11.116 1.00 44.14 ? 92 LEU A C 1 ATOM 606 O O . LEU A 1 77 ? -5.187 23.707 10.999 1.00 43.06 ? 92 LEU A O 1 ATOM 607 C CB . LEU A 1 77 ? -2.729 21.471 10.814 1.00 46.48 ? 92 LEU A CB 1 ATOM 608 C CG . LEU A 1 77 ? -2.095 20.460 9.862 1.00 48.11 ? 92 LEU A CG 1 ATOM 609 C CD1 . LEU A 1 77 ? -1.401 19.346 10.643 1.00 50.30 ? 92 LEU A CD1 1 ATOM 610 C CD2 . LEU A 1 77 ? -3.187 19.909 8.958 1.00 48.58 ? 92 LEU A CD2 1 ATOM 611 N N . ASN A 1 78 ? -3.256 24.219 12.065 1.00 43.31 ? 93 ASN A N 1 ATOM 612 C CA . ASN A 1 78 ? -3.846 25.020 13.123 1.00 43.25 ? 93 ASN A CA 1 ATOM 613 C C . ASN A 1 78 ? -3.683 26.521 12.930 1.00 42.30 ? 93 ASN A C 1 ATOM 614 O O . ASN A 1 78 ? -2.570 27.041 13.058 1.00 43.56 ? 93 ASN A O 1 ATOM 615 C CB . ASN A 1 78 ? -3.194 24.623 14.444 1.00 43.05 ? 93 ASN A CB 1 ATOM 616 C CG . ASN A 1 78 ? -1.668 24.732 14.399 1.00 44.73 ? 93 ASN A CG 1 ATOM 617 O OD1 . ASN A 1 78 ? -1.020 24.172 13.519 1.00 45.46 ? 93 ASN A OD1 1 ATOM 618 N ND2 . ASN A 1 78 ? -1.093 25.451 15.357 1.00 44.00 ? 93 ASN A ND2 1 ATOM 619 N N . THR A 1 79 ? -4.777 27.224 12.644 1.00 39.94 ? 94 THR A N 1 ATOM 620 C CA . THR A 1 79 ? -4.694 28.676 12.476 1.00 39.05 ? 94 THR A CA 1 ATOM 621 C C . THR A 1 79 ? -5.851 29.371 13.178 1.00 39.26 ? 94 THR A C 1 ATOM 622 O O . THR A 1 79 ? -6.911 28.783 13.366 1.00 39.79 ? 94 THR A O 1 ATOM 623 C CB . THR A 1 79 ? -4.720 29.110 10.985 1.00 37.78 ? 94 THR A CB 1 ATOM 624 O OG1 . THR A 1 79 ? -5.993 28.792 10.413 1.00 35.40 ? 94 THR A OG1 1 ATOM 625 C CG2 . THR A 1 79 ? -3.605 28.417 10.198 1.00 36.91 ? 94 THR A CG2 1 ATOM 626 N N . LYS A 1 80 ? -5.641 30.624 13.567 1.00 38.40 ? 95 LYS A N 1 ATOM 627 C CA . LYS A 1 80 ? -6.691 31.385 14.228 1.00 39.14 ? 95 LYS A CA 1 ATOM 628 C C . LYS A 1 80 ? -7.792 31.795 13.254 1.00 38.57 ? 95 LYS A C 1 ATOM 629 O O . LYS A 1 80 ? -8.977 31.698 13.583 1.00 38.78 ? 95 LYS A O 1 ATOM 630 C CB . LYS A 1 80 ? -6.122 32.640 14.890 1.00 40.91 ? 95 LYS A CB 1 ATOM 631 C CG . LYS A 1 80 ? -5.645 32.437 16.314 1.00 45.18 ? 95 LYS A CG 1 ATOM 632 C CD . LYS A 1 80 ? -4.131 32.457 16.418 1.00 48.33 ? 95 LYS A CD 1 ATOM 633 C CE . LYS A 1 80 ? -3.682 32.371 17.882 1.00 50.41 ? 95 LYS A CE 1 ATOM 634 N NZ . LYS A 1 80 ? -2.188 32.317 18.023 1.00 52.95 ? 95 LYS A NZ 1 ATOM 635 N N . PHE A 1 81 A -7.401 32.253 12.061 1.00 36.00 ? 95 PHE A N 1 ATOM 636 C CA . PHE A 1 81 A -8.363 32.693 11.045 1.00 34.25 ? 95 PHE A CA 1 ATOM 637 C C . PHE A 1 81 A -8.845 31.519 10.202 1.00 33.40 ? 95 PHE A C 1 ATOM 638 O O . PHE A 1 81 A -8.074 30.616 9.871 1.00 31.15 ? 95 PHE A O 1 ATOM 639 C CB . PHE A 1 81 A -7.744 33.718 10.081 1.00 34.28 ? 95 PHE A CB 1 ATOM 640 C CG . PHE A 1 81 A -7.177 34.939 10.743 1.00 35.13 ? 95 PHE A CG 1 ATOM 641 C CD1 . PHE A 1 81 A -6.508 35.893 9.979 1.00 35.05 ? 95 PHE A CD1 1 ATOM 642 C CD2 . PHE A 1 81 A -7.292 35.140 12.118 1.00 36.12 ? 95 PHE A CD2 1 ATOM 643 C CE1 . PHE A 1 81 A -5.958 37.028 10.563 1.00 36.57 ? 95 PHE A CE1 1 ATOM 644 C CE2 . PHE A 1 81 A -6.745 36.273 12.720 1.00 37.27 ? 95 PHE A CE2 1 ATOM 645 C CZ . PHE A 1 81 A -6.072 37.224 11.937 1.00 37.93 ? 95 PHE A CZ 1 ATOM 646 N N . PRO A 1 82 ? -10.132 31.525 9.827 1.00 33.68 ? 96 PRO A N 1 ATOM 647 C CA . PRO A 1 82 ? -10.602 30.406 9.009 1.00 33.56 ? 96 PRO A CA 1 ATOM 648 C C . PRO A 1 82 ? -9.824 30.277 7.702 1.00 32.97 ? 96 PRO A C 1 ATOM 649 O O . PRO A 1 82 ? -9.570 29.165 7.260 1.00 32.48 ? 96 PRO A O 1 ATOM 650 C CB . PRO A 1 82 ? -12.094 30.703 8.800 1.00 33.77 ? 96 PRO A CB 1 ATOM 651 C CG . PRO A 1 82 ? -12.215 32.192 9.039 1.00 36.30 ? 96 PRO A CG 1 ATOM 652 C CD . PRO A 1 82 ? -11.233 32.444 10.173 1.00 35.79 ? 96 PRO A CD 1 ATOM 653 N N . ASN A 1 83 ? -9.417 31.401 7.100 1.00 32.21 ? 97 ASN A N 1 ATOM 654 C CA . ASN A 1 83 ? -8.667 31.327 5.844 1.00 30.22 ? 97 ASN A CA 1 ATOM 655 C C . ASN A 1 83 ? -7.183 31.071 6.038 1.00 31.34 ? 97 ASN A C 1 ATOM 656 O O . ASN A 1 83 ? -6.430 31.033 5.068 1.00 30.79 ? 97 ASN A O 1 ATOM 657 C CB . ASN A 1 83 ? -8.875 32.586 4.980 1.00 31.37 ? 97 ASN A CB 1 ATOM 658 C CG . ASN A 1 83 ? -8.398 33.866 5.643 1.00 30.88 ? 97 ASN A CG 1 ATOM 659 O OD1 . ASN A 1 83 ? -7.589 33.859 6.580 1.00 32.15 ? 97 ASN A OD1 1 ATOM 660 N ND2 . ASN A 1 83 ? -8.881 34.987 5.130 1.00 32.64 ? 97 ASN A ND2 1 ATOM 661 N N . GLY A 1 84 ? -6.776 30.909 7.298 1.00 30.18 ? 98 GLY A N 1 ATOM 662 C CA . GLY A 1 84 ? -5.387 30.619 7.627 1.00 30.11 ? 98 GLY A CA 1 ATOM 663 C C . GLY A 1 84 ? -4.381 31.718 7.362 1.00 29.57 ? 98 GLY A C 1 ATOM 664 O O . GLY A 1 84 ? -3.178 31.499 7.524 1.00 30.89 ? 98 GLY A O 1 ATOM 665 N N . LEU A 1 85 ? -4.848 32.908 7.015 1.00 27.85 ? 99 LEU A N 1 ATOM 666 C CA . LEU A 1 85 ? -3.908 33.989 6.699 1.00 28.65 ? 99 LEU A CA 1 ATOM 667 C C . LEU A 1 85 ? -3.219 34.671 7.880 1.00 28.78 ? 99 LEU A C 1 ATOM 668 O O . LEU A 1 85 ? -2.462 35.644 7.710 1.00 28.75 ? 99 LEU A O 1 ATOM 669 C CB . LEU A 1 85 ? -4.581 34.998 5.773 1.00 27.89 ? 99 LEU A CB 1 ATOM 670 C CG . LEU A 1 85 ? -4.985 34.354 4.430 1.00 29.00 ? 99 LEU A CG 1 ATOM 671 C CD1 . LEU A 1 85 ? -5.282 35.461 3.433 1.00 31.08 ? 99 LEU A CD1 1 ATOM 672 C CD2 . LEU A 1 85 ? -3.848 33.425 3.871 1.00 29.83 ? 99 LEU A CD2 1 ATOM 673 N N . ASP A 1 86 ? -3.473 34.162 9.080 1.00 28.05 ? 100 ASP A N 1 ATOM 674 C CA . ASP A 1 86 ? -2.771 34.660 10.252 1.00 28.68 ? 100 ASP A CA 1 ATOM 675 C C . ASP A 1 86 ? -1.417 33.910 10.233 1.00 27.86 ? 100 ASP A C 1 ATOM 676 O O . ASP A 1 86 ? -0.462 34.298 10.896 1.00 27.34 ? 100 ASP A O 1 ATOM 677 C CB . ASP A 1 86 ? -3.542 34.351 11.534 1.00 30.55 ? 100 ASP A CB 1 ATOM 678 C CG . ASP A 1 86 ? -4.013 32.913 11.598 1.00 31.50 ? 100 ASP A CG 1 ATOM 679 O OD1 . ASP A 1 86 ? -4.779 32.497 10.706 1.00 30.42 ? 100 ASP A OD1 1 ATOM 680 O OD2 . ASP A 1 86 ? -3.615 32.206 12.545 1.00 34.11 ? 100 ASP A OD2 1 ATOM 681 N N . LYS A 1 87 ? -1.349 32.824 9.476 1.00 27.02 ? 101 LYS A N 1 ATOM 682 C CA . LYS A 1 87 ? -0.108 32.059 9.332 1.00 28.37 ? 101 LYS A CA 1 ATOM 683 C C . LYS A 1 87 ? 0.009 31.935 7.808 1.00 29.05 ? 101 LYS A C 1 ATOM 684 O O . LYS A 1 87 ? -0.274 30.891 7.210 1.00 27.48 ? 101 LYS A O 1 ATOM 685 C CB . LYS A 1 87 ? -0.229 30.687 10.014 1.00 30.88 ? 101 LYS A CB 1 ATOM 686 C CG . LYS A 1 87 ? -0.492 30.802 11.535 1.00 32.32 ? 101 LYS A CG 1 ATOM 687 C CD . LYS A 1 87 ? -0.409 29.469 12.256 1.00 33.31 ? 101 LYS A CD 1 ATOM 688 C CE . LYS A 1 87 ? -0.791 29.614 13.743 1.00 37.21 ? 101 LYS A CE 1 ATOM 689 N NZ . LYS A 1 87 ? -0.726 28.289 14.450 1.00 37.20 ? 101 LYS A NZ 1 ATOM 690 N N . ASP A 1 88 ? 0.411 33.044 7.189 1.00 26.83 ? 102 ASP A N 1 ATOM 691 C CA . ASP A 1 88 ? 0.475 33.118 5.738 1.00 25.45 ? 102 ASP A CA 1 ATOM 692 C C . ASP A 1 88 ? 1.747 32.471 5.204 1.00 24.12 ? 102 ASP A C 1 ATOM 693 O O . ASP A 1 88 ? 2.740 33.138 4.949 1.00 23.40 ? 102 ASP A O 1 ATOM 694 C CB . ASP A 1 88 ? 0.376 34.587 5.314 1.00 22.97 ? 102 ASP A CB 1 ATOM 695 C CG . ASP A 1 88 ? -0.162 34.757 3.898 1.00 21.90 ? 102 ASP A CG 1 ATOM 696 O OD1 . ASP A 1 88 ? -0.285 33.753 3.158 1.00 22.33 ? 102 ASP A OD1 1 ATOM 697 O OD2 . ASP A 1 88 ? -0.462 35.903 3.517 1.00 23.63 ? 102 ASP A OD2 1 ATOM 698 N N . ILE A 1 89 ? 1.685 31.158 5.028 1.00 23.72 ? 103 ILE A N 1 ATOM 699 C CA . ILE A 1 89 ? 2.825 30.381 4.583 1.00 23.40 ? 103 ILE A CA 1 ATOM 700 C C . ILE A 1 89 ? 2.330 29.090 3.918 1.00 24.19 ? 103 ILE A C 1 ATOM 701 O O . ILE A 1 89 ? 1.305 28.544 4.289 1.00 23.87 ? 103 ILE A O 1 ATOM 702 C CB . ILE A 1 89 ? 3.730 30.060 5.814 1.00 25.49 ? 103 ILE A CB 1 ATOM 703 C CG1 . ILE A 1 89 ? 4.986 29.302 5.386 1.00 25.02 ? 103 ILE A CG1 1 ATOM 704 C CG2 . ILE A 1 89 ? 2.934 29.219 6.863 1.00 28.49 ? 103 ILE A CG2 1 ATOM 705 C CD1 . ILE A 1 89 ? 5.958 29.013 6.528 1.00 25.03 ? 103 ILE A CD1 1 ATOM 706 N N . MET A 1 90 ? 3.022 28.629 2.884 1.00 23.96 ? 104 MET A N 1 ATOM 707 C CA . MET A 1 90 ? 2.645 27.374 2.247 1.00 25.61 ? 104 MET A CA 1 ATOM 708 C C . MET A 1 90 ? 3.865 26.776 1.580 1.00 25.15 ? 104 MET A C 1 ATOM 709 O O . MET A 1 90 ? 4.784 27.496 1.182 1.00 23.95 ? 104 MET A O 1 ATOM 710 C CB . MET A 1 90 ? 1.521 27.549 1.214 1.00 26.49 ? 104 MET A CB 1 ATOM 711 C CG . MET A 1 90 ? 1.938 28.055 -0.127 1.00 27.51 ? 104 MET A CG 1 ATOM 712 S SD . MET A 1 90 ? 0.603 28.088 -1.374 1.00 32.24 ? 104 MET A SD 1 ATOM 713 C CE . MET A 1 90 ? 0.268 26.561 -1.668 1.00 21.54 ? 104 MET A CE 1 ATOM 714 N N . LEU A 1 91 ? 3.883 25.450 1.527 1.00 23.48 ? 105 LEU A N 1 ATOM 715 C CA . LEU A 1 91 ? 4.957 24.716 0.886 1.00 24.25 ? 105 LEU A CA 1 ATOM 716 C C . LEU A 1 91 ? 4.389 24.067 -0.355 1.00 23.62 ? 105 LEU A C 1 ATOM 717 O O . LEU A 1 91 ? 3.263 23.547 -0.354 1.00 26.08 ? 105 LEU A O 1 ATOM 718 C CB . LEU A 1 91 ? 5.511 23.641 1.820 1.00 26.01 ? 105 LEU A CB 1 ATOM 719 C CG . LEU A 1 91 ? 6.559 24.126 2.816 1.00 27.62 ? 105 LEU A CG 1 ATOM 720 C CD1 . LEU A 1 91 ? 6.816 23.041 3.856 1.00 26.90 ? 105 LEU A CD1 1 ATOM 721 C CD2 . LEU A 1 91 ? 7.850 24.500 2.067 1.00 23.54 ? 105 LEU A CD2 1 ATOM 722 N N . ILE A 1 92 ? 5.150 24.146 -1.435 1.00 23.73 ? 106 ILE A N 1 ATOM 723 C CA . ILE A 1 92 ? 4.748 23.551 -2.694 1.00 22.35 ? 106 ILE A CA 1 ATOM 724 C C . ILE A 1 92 ? 5.783 22.493 -3.049 1.00 25.38 ? 106 ILE A C 1 ATOM 725 O O . ILE A 1 92 ? 6.979 22.798 -3.104 1.00 23.85 ? 106 ILE A O 1 ATOM 726 C CB . ILE A 1 92 ? 4.764 24.560 -3.841 1.00 21.86 ? 106 ILE A CB 1 ATOM 727 C CG1 . ILE A 1 92 ? 3.737 25.672 -3.569 1.00 23.31 ? 106 ILE A CG1 1 ATOM 728 C CG2 . ILE A 1 92 ? 4.491 23.839 -5.154 1.00 23.24 ? 106 ILE A CG2 1 ATOM 729 C CD1 . ILE A 1 92 ? 3.630 26.723 -4.673 1.00 21.04 ? 106 ILE A CD1 1 ATOM 730 N N . ARG A 1 93 ? 5.342 21.254 -3.272 1.00 25.72 ? 107 ARG A N 1 ATOM 731 C CA . ARG A 1 93 ? 6.293 20.225 -3.667 1.00 26.25 ? 107 ARG A CA 1 ATOM 732 C C . ARG A 1 93 ? 6.236 20.228 -5.186 1.00 26.37 ? 107 ARG A C 1 ATOM 733 O O . ARG A 1 93 ? 5.147 20.166 -5.762 1.00 25.48 ? 107 ARG A O 1 ATOM 734 C CB . ARG A 1 93 ? 5.887 18.858 -3.119 1.00 29.30 ? 107 ARG A CB 1 ATOM 735 C CG . ARG A 1 93 ? 6.858 17.780 -3.532 1.00 32.79 ? 107 ARG A CG 1 ATOM 736 C CD . ARG A 1 93 ? 6.663 16.476 -2.776 1.00 35.21 ? 107 ARG A CD 1 ATOM 737 N NE . ARG A 1 93 ? 7.597 15.499 -3.319 1.00 40.29 ? 107 ARG A NE 1 ATOM 738 C CZ . ARG A 1 93 ? 7.861 14.313 -2.785 1.00 43.53 ? 107 ARG A CZ 1 ATOM 739 N NH1 . ARG A 1 93 ? 7.257 13.931 -1.661 1.00 43.83 ? 107 ARG A NH1 1 ATOM 740 N NH2 . ARG A 1 93 ? 8.729 13.504 -3.391 1.00 44.64 ? 107 ARG A NH2 1 ATOM 741 N N . LEU A 1 94 ? 7.393 20.337 -5.845 1.00 25.16 ? 108 LEU A N 1 ATOM 742 C CA . LEU A 1 94 ? 7.424 20.368 -7.305 1.00 25.99 ? 108 LEU A CA 1 ATOM 743 C C . LEU A 1 94 ? 7.124 18.988 -7.863 1.00 27.01 ? 108 LEU A C 1 ATOM 744 O O . LEU A 1 94 ? 7.563 18.001 -7.301 1.00 27.13 ? 108 LEU A O 1 ATOM 745 C CB . LEU A 1 94 ? 8.807 20.813 -7.804 1.00 27.21 ? 108 LEU A CB 1 ATOM 746 C CG . LEU A 1 94 ? 9.208 22.192 -7.263 1.00 26.65 ? 108 LEU A CG 1 ATOM 747 C CD1 . LEU A 1 94 ? 10.559 22.574 -7.846 1.00 26.41 ? 108 LEU A CD1 1 ATOM 748 C CD2 . LEU A 1 94 ? 8.124 23.221 -7.631 1.00 25.08 ? 108 LEU A CD2 1 ATOM 749 N N . ARG A 1 95 ? 6.392 18.933 -8.964 1.00 29.40 ? 109 ARG A N 1 ATOM 750 C CA . ARG A 1 95 ? 6.042 17.649 -9.572 1.00 34.14 ? 109 ARG A CA 1 ATOM 751 C C . ARG A 1 95 ? 7.310 16.838 -9.896 1.00 36.22 ? 109 ARG A C 1 ATOM 752 O O . ARG A 1 95 ? 7.325 15.603 -9.758 1.00 36.83 ? 109 ARG A O 1 ATOM 753 C CB . ARG A 1 95 ? 5.229 17.868 -10.842 1.00 35.83 ? 109 ARG A CB 1 ATOM 754 C CG . ARG A 1 95 ? 4.813 16.557 -11.505 1.00 41.18 ? 109 ARG A CG 1 ATOM 755 C CD . ARG A 1 95 ? 4.122 16.787 -12.824 1.00 46.13 ? 109 ARG A CD 1 ATOM 756 N NE . ARG A 1 95 ? 2.722 17.156 -12.653 1.00 51.43 ? 109 ARG A NE 1 ATOM 757 C CZ . ARG A 1 95 ? 1.890 17.433 -13.656 1.00 53.09 ? 109 ARG A CZ 1 ATOM 758 N NH1 . ARG A 1 95 ? 2.320 17.388 -14.913 1.00 54.42 ? 109 ARG A NH1 1 ATOM 759 N NH2 . ARG A 1 95 ? 0.623 17.739 -13.400 1.00 54.17 ? 109 ARG A NH2 1 ATOM 760 N N . ARG A 1 96 ? 8.349 17.548 -10.347 1.00 36.06 ? 110 ARG A N 1 ATOM 761 C CA . ARG A 1 96 ? 9.669 16.977 -10.668 1.00 36.78 ? 110 ARG A CA 1 ATOM 762 C C . ARG A 1 96 ? 10.695 17.909 -10.036 1.00 35.68 ? 110 ARG A C 1 ATOM 763 O O . ARG A 1 96 ? 10.535 19.136 -10.074 1.00 33.00 ? 110 ARG A O 1 ATOM 764 C CB . ARG A 1 96 ? 9.914 16.963 -12.174 1.00 40.30 ? 110 ARG A CB 1 ATOM 765 C CG . ARG A 1 96 ? 9.114 15.945 -12.936 1.00 45.01 ? 110 ARG A CG 1 ATOM 766 C CD . ARG A 1 96 ? 8.857 16.474 -14.336 1.00 50.35 ? 110 ARG A CD 1 ATOM 767 N NE . ARG A 1 96 ? 10.085 16.950 -14.976 1.00 52.40 ? 110 ARG A NE 1 ATOM 768 C CZ . ARG A 1 96 ? 10.157 18.060 -15.701 1.00 52.86 ? 110 ARG A CZ 1 ATOM 769 N NH1 . ARG A 1 96 ? 9.075 18.809 -15.870 1.00 54.62 ? 110 ARG A NH1 1 ATOM 770 N NH2 . ARG A 1 96 ? 11.302 18.413 -16.269 1.00 53.81 ? 110 ARG A NH2 1 ATOM 771 N N . PRO A 1 97 ? 11.772 17.351 -9.462 1.00 34.74 ? 111 PRO A N 1 ATOM 772 C CA . PRO A 1 97 ? 12.759 18.240 -8.850 1.00 32.98 ? 111 PRO A CA 1 ATOM 773 C C . PRO A 1 97 ? 13.510 19.003 -9.922 1.00 31.61 ? 111 PRO A C 1 ATOM 774 O O . PRO A 1 97 ? 13.369 18.727 -11.116 1.00 31.81 ? 111 PRO A O 1 ATOM 775 C CB . PRO A 1 97 ? 13.695 17.289 -8.109 1.00 33.88 ? 111 PRO A CB 1 ATOM 776 C CG . PRO A 1 97 ? 12.969 15.952 -8.106 1.00 36.21 ? 111 PRO A CG 1 ATOM 777 C CD . PRO A 1 97 ? 12.200 15.947 -9.377 1.00 34.93 ? 111 PRO A CD 1 ATOM 778 N N . VAL A 1 98 ? 14.280 19.994 -9.491 1.00 28.76 ? 112 VAL A N 1 ATOM 779 C CA . VAL A 1 98 ? 15.106 20.730 -10.424 1.00 29.33 ? 112 VAL A CA 1 ATOM 780 C C . VAL A 1 98 ? 16.548 20.318 -10.129 1.00 28.94 ? 112 VAL A C 1 ATOM 781 O O . VAL A 1 98 ? 16.838 19.743 -9.088 1.00 28.23 ? 112 VAL A O 1 ATOM 782 C CB . VAL A 1 98 ? 15.002 22.262 -10.234 1.00 27.30 ? 112 VAL A CB 1 ATOM 783 C CG1 . VAL A 1 98 ? 13.663 22.744 -10.731 1.00 28.88 ? 112 VAL A CG1 1 ATOM 784 C CG2 . VAL A 1 98 ? 15.208 22.632 -8.754 1.00 25.74 ? 112 VAL A CG2 1 ATOM 785 N N . THR A 1 99 ? 17.433 20.620 -11.069 1.00 28.77 ? 113 THR A N 1 ATOM 786 C CA . THR A 1 99 ? 18.861 20.358 -10.929 1.00 28.45 ? 113 THR A CA 1 ATOM 787 C C . THR A 1 99 ? 19.451 21.722 -10.566 1.00 27.09 ? 113 THR A C 1 ATOM 788 O O . THR A 1 99 ? 19.109 22.717 -11.208 1.00 28.29 ? 113 THR A O 1 ATOM 789 C CB . THR A 1 99 ? 19.459 19.929 -12.285 1.00 28.96 ? 113 THR A CB 1 ATOM 790 O OG1 . THR A 1 99 ? 18.839 18.710 -12.708 1.00 33.52 ? 113 THR A OG1 1 ATOM 791 C CG2 . THR A 1 99 ? 20.966 19.756 -12.190 1.00 29.16 ? 113 THR A CG2 1 ATOM 792 N N . TYR A 1 100 ? 20.312 21.782 -9.556 1.00 27.10 ? 114 TYR A N 1 ATOM 793 C CA . TYR A 1 100 ? 20.908 23.064 -9.186 1.00 26.18 ? 114 TYR A CA 1 ATOM 794 C C . TYR A 1 100 ? 21.786 23.497 -10.347 1.00 28.81 ? 114 TYR A C 1 ATOM 795 O O . TYR A 1 100 ? 22.479 22.683 -10.959 1.00 28.16 ? 114 TYR A O 1 ATOM 796 C CB . TYR A 1 100 ? 21.723 22.957 -7.900 1.00 26.78 ? 114 TYR A CB 1 ATOM 797 C CG . TYR A 1 100 ? 20.921 22.568 -6.684 1.00 27.26 ? 114 TYR A CG 1 ATOM 798 C CD1 . TYR A 1 100 ? 19.564 22.928 -6.563 1.00 26.58 ? 114 TYR A CD1 1 ATOM 799 C CD2 . TYR A 1 100 ? 21.510 21.865 -5.643 1.00 26.98 ? 114 TYR A CD2 1 ATOM 800 C CE1 . TYR A 1 100 ? 18.841 22.586 -5.441 1.00 25.61 ? 114 TYR A CE1 1 ATOM 801 C CE2 . TYR A 1 100 ? 20.795 21.521 -4.512 1.00 28.46 ? 114 TYR A CE2 1 ATOM 802 C CZ . TYR A 1 100 ? 19.451 21.886 -4.420 1.00 27.22 ? 114 TYR A CZ 1 ATOM 803 O OH . TYR A 1 100 ? 18.734 21.524 -3.310 1.00 30.01 ? 114 TYR A OH 1 ATOM 804 N N . SER A 1 101 ? 21.722 24.775 -10.675 1.00 28.46 ? 115 SER A N 1 ATOM 805 C CA . SER A 1 101 ? 22.479 25.306 -11.784 1.00 30.28 ? 115 SER A CA 1 ATOM 806 C C . SER A 1 101 ? 22.827 26.754 -11.513 1.00 30.19 ? 115 SER A C 1 ATOM 807 O O . SER A 1 101 ? 22.548 27.283 -10.431 1.00 29.68 ? 115 SER A O 1 ATOM 808 C CB . SER A 1 101 ? 21.670 25.183 -13.073 1.00 29.27 ? 115 SER A CB 1 ATOM 809 O OG . SER A 1 101 ? 20.424 25.842 -12.958 1.00 33.31 ? 115 SER A OG 1 ATOM 810 N N . THR A 1 102 ? 23.453 27.383 -12.491 1.00 30.04 ? 116 THR A N 1 ATOM 811 C CA . THR A 1 102 ? 23.876 28.768 -12.361 1.00 29.82 ? 116 THR A CA 1 ATOM 812 C C . THR A 1 102 ? 22.813 29.691 -11.789 1.00 28.27 ? 116 THR A C 1 ATOM 813 O O . THR A 1 102 ? 23.088 30.464 -10.866 1.00 28.78 ? 116 THR A O 1 ATOM 814 C CB . THR A 1 102 ? 24.310 29.325 -13.716 1.00 30.82 ? 116 THR A CB 1 ATOM 815 O OG1 . THR A 1 102 ? 25.340 28.479 -14.254 1.00 32.99 ? 116 THR A OG1 1 ATOM 816 C CG2 . THR A 1 102 ? 24.862 30.747 -13.556 1.00 31.81 ? 116 THR A CG2 1 ATOM 817 N N . HIS A 1 103 ? 21.606 29.601 -12.334 1.00 25.93 ? 117 HIS A N 1 ATOM 818 C CA . HIS A 1 103 ? 20.512 30.467 -11.897 1.00 27.37 ? 117 HIS A CA 1 ATOM 819 C C . HIS A 1 103 ? 19.470 29.774 -11.017 1.00 25.44 ? 117 HIS A C 1 ATOM 820 O O . HIS A 1 103 ? 18.421 30.354 -10.706 1.00 25.11 ? 117 HIS A O 1 ATOM 821 C CB . HIS A 1 103 ? 19.840 31.093 -13.121 1.00 27.68 ? 117 HIS A CB 1 ATOM 822 C CG . HIS A 1 103 ? 20.801 31.798 -14.033 1.00 31.66 ? 117 HIS A CG 1 ATOM 823 N ND1 . HIS A 1 103 ? 21.101 31.337 -15.299 1.00 33.56 ? 117 HIS A ND1 1 ATOM 824 C CD2 . HIS A 1 103 ? 21.542 32.920 -13.856 1.00 33.32 ? 117 HIS A CD2 1 ATOM 825 C CE1 . HIS A 1 103 ? 21.981 32.146 -15.864 1.00 33.66 ? 117 HIS A CE1 1 ATOM 826 N NE2 . HIS A 1 103 ? 22.266 33.113 -15.010 1.00 34.59 ? 117 HIS A NE2 1 ATOM 827 N N . ILE A 1 104 ? 19.745 28.538 -10.621 1.00 25.19 ? 118 ILE A N 1 ATOM 828 C CA . ILE A 1 104 ? 18.824 27.810 -9.752 1.00 24.74 ? 118 ILE A CA 1 ATOM 829 C C . ILE A 1 104 ? 19.604 27.206 -8.578 1.00 27.20 ? 118 ILE A C 1 ATOM 830 O O . ILE A 1 104 ? 20.452 26.320 -8.764 1.00 27.50 ? 118 ILE A O 1 ATOM 831 C CB . ILE A 1 104 ? 18.092 26.665 -10.501 1.00 25.47 ? 118 ILE A CB 1 ATOM 832 C CG1 . ILE A 1 104 ? 17.245 27.231 -11.645 1.00 23.27 ? 118 ILE A CG1 1 ATOM 833 C CG2 . ILE A 1 104 ? 17.224 25.868 -9.501 1.00 25.18 ? 118 ILE A CG2 1 ATOM 834 C CD1 . ILE A 1 104 ? 16.504 26.196 -12.458 1.00 23.62 ? 118 ILE A CD1 1 ATOM 835 N N . ALA A 1 105 ? 19.319 27.681 -7.372 1.00 25.84 ? 119 ALA A N 1 ATOM 836 C CA . ALA A 1 105 ? 19.988 27.189 -6.166 1.00 26.05 ? 119 ALA A CA 1 ATOM 837 C C . ALA A 1 105 ? 19.076 27.457 -4.976 1.00 26.05 ? 119 ALA A C 1 ATOM 838 O O . ALA A 1 105 ? 18.333 28.436 -4.971 1.00 25.37 ? 119 ALA A O 1 ATOM 839 C CB . ALA A 1 105 ? 21.325 27.911 -5.955 1.00 27.47 ? 119 ALA A CB 1 ATOM 840 N N . PRO A 1 106 ? 19.139 26.607 -3.948 1.00 25.73 ? 120 PRO A N 1 ATOM 841 C CA . PRO A 1 106 ? 18.295 26.789 -2.763 1.00 26.31 ? 120 PRO A CA 1 ATOM 842 C C . PRO A 1 106 ? 18.777 27.887 -1.837 1.00 25.94 ? 120 PRO A C 1 ATOM 843 O O . PRO A 1 106 ? 19.955 28.246 -1.842 1.00 25.21 ? 120 PRO A O 1 ATOM 844 C CB . PRO A 1 106 ? 18.372 25.426 -2.079 1.00 25.31 ? 120 PRO A CB 1 ATOM 845 C CG . PRO A 1 106 ? 19.816 25.000 -2.378 1.00 27.48 ? 120 PRO A CG 1 ATOM 846 C CD . PRO A 1 106 ? 20.042 25.445 -3.800 1.00 26.34 ? 120 PRO A CD 1 ATOM 847 N N . VAL A 1 107 ? 17.861 28.433 -1.042 1.00 26.02 ? 121 VAL A N 1 ATOM 848 C CA . VAL A 1 107 ? 18.254 29.426 -0.050 1.00 26.07 ? 121 VAL A CA 1 ATOM 849 C C . VAL A 1 107 ? 18.082 28.742 1.302 1.00 26.83 ? 121 VAL A C 1 ATOM 850 O O . VAL A 1 107 ? 17.190 27.906 1.471 1.00 27.84 ? 121 VAL A O 1 ATOM 851 C CB . VAL A 1 107 ? 17.381 30.721 -0.112 1.00 25.33 ? 121 VAL A CB 1 ATOM 852 C CG1 . VAL A 1 107 ? 15.913 30.389 0.112 1.00 23.94 ? 121 VAL A CG1 1 ATOM 853 C CG2 . VAL A 1 107 ? 17.873 31.733 0.935 1.00 25.63 ? 121 VAL A CG2 1 ATOM 854 N N . SER A 1 108 ? 18.930 29.104 2.254 1.00 27.61 ? 122 SER A N 1 ATOM 855 C CA . SER A 1 108 ? 18.880 28.534 3.585 1.00 30.26 ? 122 SER A CA 1 ATOM 856 C C . SER A 1 108 ? 17.767 29.112 4.448 1.00 31.11 ? 122 SER A C 1 ATOM 857 O O . SER A 1 108 ? 17.407 30.293 4.316 1.00 29.76 ? 122 SER A O 1 ATOM 858 C CB . SER A 1 108 ? 20.222 28.772 4.294 1.00 34.97 ? 122 SER A CB 1 ATOM 859 O OG . SER A 1 108 ? 20.097 28.532 5.687 1.00 38.02 ? 122 SER A OG 1 ATOM 860 N N . LEU A 1 109 ? 17.207 28.277 5.314 1.00 31.79 ? 123 LEU A N 1 ATOM 861 C CA . LEU A 1 109 ? 16.194 28.733 6.259 1.00 31.93 ? 123 LEU A CA 1 ATOM 862 C C . LEU A 1 109 ? 17.026 29.470 7.327 1.00 33.19 ? 123 LEU A C 1 ATOM 863 O O . LEU A 1 109 ? 18.260 29.383 7.330 1.00 32.93 ? 123 LEU A O 1 ATOM 864 C CB . LEU A 1 109 ? 15.458 27.541 6.875 1.00 33.53 ? 123 LEU A CB 1 ATOM 865 C CG . LEU A 1 109 ? 14.553 26.711 5.958 1.00 34.43 ? 123 LEU A CG 1 ATOM 866 C CD1 . LEU A 1 109 ? 13.946 25.564 6.753 1.00 35.28 ? 123 LEU A CD1 1 ATOM 867 C CD2 . LEU A 1 109 ? 13.441 27.594 5.366 1.00 32.99 ? 123 LEU A CD2 1 ATOM 868 N N . PRO A 1 110 ? 16.374 30.212 8.238 1.00 34.41 ? 124 PRO A N 1 ATOM 869 C CA . PRO A 1 110 ? 17.125 30.938 9.272 1.00 35.47 ? 124 PRO A CA 1 ATOM 870 C C . PRO A 1 110 ? 17.917 30.021 10.216 1.00 37.83 ? 124 PRO A C 1 ATOM 871 O O . PRO A 1 110 ? 17.389 29.027 10.711 1.00 37.13 ? 124 PRO A O 1 ATOM 872 C CB . PRO A 1 110 ? 16.035 31.710 10.032 1.00 35.84 ? 124 PRO A CB 1 ATOM 873 C CG . PRO A 1 110 ? 14.899 31.784 9.076 1.00 35.81 ? 124 PRO A CG 1 ATOM 874 C CD . PRO A 1 110 ? 14.927 30.453 8.368 1.00 33.82 ? 124 PRO A CD 1 ATOM 875 N N . SER A 1 111 ? 19.175 30.370 10.464 1.00 40.53 ? 125 SER A N 1 ATOM 876 C CA . SER A 1 111 ? 20.016 29.588 11.365 1.00 43.47 ? 125 SER A CA 1 ATOM 877 C C . SER A 1 111 ? 19.786 30.050 12.796 1.00 45.06 ? 125 SER A C 1 ATOM 878 O O . SER A 1 111 ? 20.033 29.307 13.742 1.00 47.77 ? 125 SER A O 1 ATOM 879 C CB . SER A 1 111 ? 21.494 29.751 11.004 1.00 42.97 ? 125 SER A CB 1 ATOM 880 O OG . SER A 1 111 ? 21.916 31.095 11.162 1.00 44.77 ? 125 SER A OG 1 ATOM 881 N N . ARG A 1 112 ? 19.311 31.281 12.944 1.00 45.97 ? 127 ARG A N 1 ATOM 882 C CA . ARG A 1 112 ? 19.024 31.880 14.251 1.00 46.57 ? 127 ARG A CA 1 ATOM 883 C C . ARG A 1 112 ? 18.033 33.002 14.006 1.00 46.27 ? 127 ARG A C 1 ATOM 884 O O . ARG A 1 112 ? 17.895 33.475 12.881 1.00 45.63 ? 127 ARG A O 1 ATOM 885 C CB . ARG A 1 112 ? 20.294 32.477 14.884 1.00 47.79 ? 127 ARG A CB 1 ATOM 886 C CG . ARG A 1 112 ? 21.136 33.321 13.915 1.00 51.75 ? 127 ARG A CG 1 ATOM 887 C CD . ARG A 1 112 ? 22.065 34.315 14.611 1.00 53.96 ? 127 ARG A CD 1 ATOM 888 N NE . ARG A 1 112 ? 21.320 35.443 15.165 1.00 57.47 ? 127 ARG A NE 1 ATOM 889 C CZ . ARG A 1 112 ? 21.876 36.525 15.701 1.00 58.02 ? 127 ARG A CZ 1 ATOM 890 N NH1 . ARG A 1 112 ? 23.197 36.634 15.763 1.00 58.31 ? 127 ARG A NH1 1 ATOM 891 N NH2 . ARG A 1 112 ? 21.105 37.504 16.168 1.00 58.19 ? 127 ARG A NH2 1 ATOM 892 N N . SER A 1 113 ? 17.345 33.433 15.053 1.00 44.70 ? 128 SER A N 1 ATOM 893 C CA . SER A 1 113 ? 16.396 34.520 14.904 1.00 43.61 ? 128 SER A CA 1 ATOM 894 C C . SER A 1 113 ? 17.115 35.855 14.733 1.00 42.96 ? 128 SER A C 1 ATOM 895 O O . SER A 1 113 ? 18.157 36.098 15.343 1.00 41.72 ? 128 SER A O 1 ATOM 896 C CB . SER A 1 113 ? 15.481 34.590 16.122 1.00 44.36 ? 128 SER A CB 1 ATOM 897 O OG . SER A 1 113 ? 14.609 35.694 16.022 1.00 45.95 ? 128 SER A OG 1 ATOM 898 N N . ARG A 1 114 ? 16.565 36.710 13.880 1.00 40.59 ? 129 ARG A N 1 ATOM 899 C CA . ARG A 1 114 ? 17.123 38.039 13.657 1.00 40.34 ? 129 ARG A CA 1 ATOM 900 C C . ARG A 1 114 ? 15.995 39.014 13.970 1.00 39.84 ? 129 ARG A C 1 ATOM 901 O O . ARG A 1 114 ? 14.829 38.751 13.652 1.00 38.14 ? 129 ARG A O 1 ATOM 902 C CB . ARG A 1 114 ? 17.572 38.202 12.215 1.00 41.70 ? 129 ARG A CB 1 ATOM 903 C CG . ARG A 1 114 ? 18.748 37.345 11.835 1.00 44.04 ? 129 ARG A CG 1 ATOM 904 C CD . ARG A 1 114 ? 20.039 38.100 11.984 1.00 47.98 ? 129 ARG A CD 1 ATOM 905 N NE . ARG A 1 114 ? 21.168 37.261 11.601 1.00 49.89 ? 129 ARG A NE 1 ATOM 906 C CZ . ARG A 1 114 ? 22.439 37.597 11.786 1.00 50.97 ? 129 ARG A CZ 1 ATOM 907 N NH1 . ARG A 1 114 ? 22.744 38.761 12.346 1.00 50.90 ? 129 ARG A NH1 1 ATOM 908 N NH2 . ARG A 1 114 ? 23.402 36.758 11.428 1.00 52.30 ? 129 ARG A NH2 1 ATOM 909 N N . GLY A 1 115 ? 16.336 40.129 14.605 1.00 38.68 ? 131 GLY A N 1 ATOM 910 C CA . GLY A 1 115 ? 15.314 41.084 14.969 1.00 39.09 ? 131 GLY A CA 1 ATOM 911 C C . GLY A 1 115 ? 15.617 42.520 14.627 1.00 38.88 ? 131 GLY A C 1 ATOM 912 O O . GLY A 1 115 ? 16.373 42.809 13.693 1.00 38.48 ? 131 GLY A O 1 ATOM 913 N N . VAL A 1 116 ? 15.022 43.415 15.411 1.00 38.42 ? 132 VAL A N 1 ATOM 914 C CA . VAL A 1 116 ? 15.147 44.851 15.217 1.00 37.99 ? 132 VAL A CA 1 ATOM 915 C C . VAL A 1 116 ? 16.550 45.321 14.890 1.00 38.48 ? 132 VAL A C 1 ATOM 916 O O . VAL A 1 116 ? 17.494 45.013 15.617 1.00 38.64 ? 132 VAL A O 1 ATOM 917 C CB . VAL A 1 116 ? 14.649 45.604 16.458 1.00 38.56 ? 132 VAL A CB 1 ATOM 918 C CG1 . VAL A 1 116 ? 14.766 47.109 16.231 1.00 38.03 ? 132 VAL A CG1 1 ATOM 919 C CG2 . VAL A 1 116 ? 13.210 45.206 16.752 1.00 37.12 ? 132 VAL A CG2 1 ATOM 920 N N . GLY A 1 117 ? 16.685 46.065 13.796 1.00 35.93 ? 133 GLY A N 1 ATOM 921 C CA . GLY A 1 117 ? 17.990 46.565 13.398 1.00 36.36 ? 133 GLY A CA 1 ATOM 922 C C . GLY A 1 117 ? 18.671 45.789 12.284 1.00 35.78 ? 133 GLY A C 1 ATOM 923 O O . GLY A 1 117 ? 19.525 46.339 11.594 1.00 38.18 ? 133 GLY A O 1 ATOM 924 N N . SER A 1 118 ? 18.313 44.521 12.102 1.00 34.75 ? 134 SER A N 1 ATOM 925 C CA . SER A 1 118 ? 18.913 43.697 11.044 1.00 33.84 ? 134 SER A CA 1 ATOM 926 C C . SER A 1 118 ? 18.590 44.278 9.677 1.00 31.97 ? 134 SER A C 1 ATOM 927 O O . SER A 1 118 ? 17.441 44.652 9.442 1.00 32.16 ? 134 SER A O 1 ATOM 928 C CB . SER A 1 118 ? 18.356 42.274 11.069 1.00 34.96 ? 134 SER A CB 1 ATOM 929 O OG . SER A 1 118 ? 18.385 41.696 12.358 1.00 37.85 ? 134 SER A OG 1 ATOM 930 N N . ARG A 1 119 ? 19.586 44.367 8.790 1.00 31.41 ? 135 ARG A N 1 ATOM 931 C CA . ARG A 1 119 ? 19.336 44.861 7.435 1.00 30.00 ? 135 ARG A CA 1 ATOM 932 C C . ARG A 1 119 ? 19.055 43.626 6.594 1.00 29.43 ? 135 ARG A C 1 ATOM 933 O O . ARG A 1 119 ? 19.740 42.600 6.721 1.00 28.27 ? 135 ARG A O 1 ATOM 934 C CB . ARG A 1 119 ? 20.532 45.635 6.849 1.00 31.68 ? 135 ARG A CB 1 ATOM 935 C CG . ARG A 1 119 ? 20.143 46.470 5.605 1.00 37.05 ? 135 ARG A CG 1 ATOM 936 C CD . ARG A 1 119 ? 21.283 47.300 4.999 1.00 37.86 ? 135 ARG A CD 1 ATOM 937 N NE . ARG A 1 119 ? 22.181 46.480 4.203 1.00 40.50 ? 135 ARG A NE 1 ATOM 938 C CZ . ARG A 1 119 ? 23.105 46.947 3.363 1.00 41.62 ? 135 ARG A CZ 1 ATOM 939 N NH1 . ARG A 1 119 ? 23.277 48.257 3.187 1.00 40.24 ? 135 ARG A NH1 1 ATOM 940 N NH2 . ARG A 1 119 ? 23.859 46.092 2.688 1.00 40.95 ? 135 ARG A NH2 1 ATOM 941 N N . CYS A 1 120 ? 18.044 43.725 5.738 1.00 27.13 ? 136 CYS A N 1 ATOM 942 C CA . CYS A 1 120 ? 17.642 42.604 4.898 1.00 25.77 ? 136 CYS A CA 1 ATOM 943 C C . CYS A 1 120 ? 17.393 43.084 3.490 1.00 24.90 ? 136 CYS A C 1 ATOM 944 O O . CYS A 1 120 ? 17.376 44.275 3.225 1.00 25.02 ? 136 CYS A O 1 ATOM 945 C CB . CYS A 1 120 ? 16.366 41.972 5.447 1.00 26.42 ? 136 CYS A CB 1 ATOM 946 S SG . CYS A 1 120 ? 16.460 41.523 7.212 1.00 29.65 ? 136 CYS A SG 1 ATOM 947 N N . ARG A 1 121 ? 17.188 42.145 2.583 1.00 24.86 ? 137 ARG A N 1 ATOM 948 C CA . ARG A 1 121 ? 16.943 42.498 1.192 1.00 23.60 ? 137 ARG A CA 1 ATOM 949 C C . ARG A 1 121 ? 15.588 41.946 0.781 1.00 23.04 ? 137 ARG A C 1 ATOM 950 O O . ARG A 1 121 ? 15.220 40.834 1.183 1.00 21.90 ? 137 ARG A O 1 ATOM 951 C CB . ARG A 1 121 ? 18.015 41.872 0.308 1.00 23.85 ? 137 ARG A CB 1 ATOM 952 C CG . ARG A 1 121 ? 18.091 42.383 -1.122 1.00 27.08 ? 137 ARG A CG 1 ATOM 953 C CD . ARG A 1 121 ? 19.544 42.275 -1.599 1.00 29.84 ? 137 ARG A CD 1 ATOM 954 N NE . ARG A 1 121 ? 19.772 42.744 -2.967 1.00 31.68 ? 137 ARG A NE 1 ATOM 955 C CZ . ARG A 1 121 ? 19.965 44.010 -3.330 1.00 31.87 ? 137 ARG A CZ 1 ATOM 956 N NH1 . ARG A 1 121 ? 19.951 44.985 -2.432 1.00 31.57 ? 137 ARG A NH1 1 ATOM 957 N NH2 . ARG A 1 121 ? 20.214 44.291 -4.600 1.00 32.20 ? 137 ARG A NH2 1 ATOM 958 N N . ILE A 1 122 ? 14.857 42.722 -0.013 1.00 21.07 ? 138 ILE A N 1 ATOM 959 C CA . ILE A 1 122 ? 13.570 42.268 -0.534 1.00 19.41 ? 138 ILE A CA 1 ATOM 960 C C . ILE A 1 122 ? 13.755 42.261 -2.051 1.00 20.38 ? 138 ILE A C 1 ATOM 961 O O . ILE A 1 122 ? 14.612 42.984 -2.578 1.00 21.42 ? 138 ILE A O 1 ATOM 962 C CB . ILE A 1 122 ? 12.381 43.201 -0.124 1.00 17.50 ? 138 ILE A CB 1 ATOM 963 C CG1 . ILE A 1 122 ? 12.776 44.676 -0.252 1.00 16.48 ? 138 ILE A CG1 1 ATOM 964 C CG2 . ILE A 1 122 ? 11.935 42.905 1.305 1.00 19.24 ? 138 ILE A CG2 1 ATOM 965 C CD1 . ILE A 1 122 ? 11.532 45.582 -0.159 1.00 16.86 ? 138 ILE A CD1 1 ATOM 966 N N . MET A 1 123 ? 12.965 41.440 -2.743 1.00 19.64 ? 139 MET A N 1 ATOM 967 C CA . MET A 1 123 ? 13.090 41.279 -4.187 1.00 18.70 ? 139 MET A CA 1 ATOM 968 C C . MET A 1 123 ? 11.816 40.641 -4.736 1.00 19.71 ? 139 MET A C 1 ATOM 969 O O . MET A 1 123 ? 11.194 39.806 -4.080 1.00 19.51 ? 139 MET A O 1 ATOM 970 C CB . MET A 1 123 ? 14.265 40.338 -4.483 1.00 19.41 ? 139 MET A CB 1 ATOM 971 C CG . MET A 1 123 ? 14.121 39.003 -3.769 1.00 22.19 ? 139 MET A CG 1 ATOM 972 S SD . MET A 1 123 ? 15.592 37.960 -3.807 1.00 26.23 ? 139 MET A SD 1 ATOM 973 C CE . MET A 1 123 ? 16.791 38.972 -2.973 1.00 27.74 ? 139 MET A CE 1 ATOM 974 N N . GLY A 1 124 ? 11.446 41.014 -5.958 1.00 17.54 ? 140 GLY A N 1 ATOM 975 C CA . GLY A 1 124 ? 10.261 40.436 -6.550 1.00 16.71 ? 140 GLY A CA 1 ATOM 976 C C . GLY A 1 124 ? 9.956 41.069 -7.883 1.00 19.23 ? 140 GLY A C 1 ATOM 977 O O . GLY A 1 124 ? 10.691 41.951 -8.344 1.00 20.62 ? 140 GLY A O 1 ATOM 978 N N . TRP A 1 125 ? 8.898 40.586 -8.517 1.00 20.90 ? 141 TRP A N 1 ATOM 979 C CA . TRP A 1 125 ? 8.454 41.128 -9.802 1.00 22.38 ? 141 TRP A CA 1 ATOM 980 C C . TRP A 1 125 ? 7.217 41.987 -9.576 1.00 23.29 ? 141 TRP A C 1 ATOM 981 O O . TRP A 1 125 ? 6.443 42.266 -10.523 1.00 22.79 ? 141 TRP A O 1 ATOM 982 C CB . TRP A 1 125 ? 8.113 39.982 -10.774 1.00 20.55 ? 141 TRP A CB 1 ATOM 983 C CG . TRP A 1 125 ? 9.306 39.251 -11.321 1.00 22.61 ? 141 TRP A CG 1 ATOM 984 C CD1 . TRP A 1 125 ? 9.992 39.524 -12.487 1.00 24.77 ? 141 TRP A CD1 1 ATOM 985 C CD2 . TRP A 1 125 ? 9.915 38.080 -10.764 1.00 21.13 ? 141 TRP A CD2 1 ATOM 986 N NE1 . TRP A 1 125 ? 10.985 38.582 -12.687 1.00 24.45 ? 141 TRP A NE1 1 ATOM 987 C CE2 . TRP A 1 125 ? 10.957 37.681 -11.649 1.00 23.04 ? 141 TRP A CE2 1 ATOM 988 C CE3 . TRP A 1 125 ? 9.680 37.322 -9.607 1.00 21.11 ? 141 TRP A CE3 1 ATOM 989 C CZ2 . TRP A 1 125 ? 11.753 36.560 -11.409 1.00 22.32 ? 141 TRP A CZ2 1 ATOM 990 C CZ3 . TRP A 1 125 ? 10.481 36.201 -9.367 1.00 21.47 ? 141 TRP A CZ3 1 ATOM 991 C CH2 . TRP A 1 125 ? 11.505 35.830 -10.268 1.00 24.06 ? 141 TRP A CH2 1 ATOM 992 N N . GLY A 1 126 ? 7.012 42.388 -8.319 1.00 21.52 ? 142 GLY A N 1 ATOM 993 C CA . GLY A 1 126 ? 5.866 43.214 -7.974 1.00 22.13 ? 142 GLY A CA 1 ATOM 994 C C . GLY A 1 126 ? 5.985 44.649 -8.474 1.00 21.84 ? 142 GLY A C 1 ATOM 995 O O . GLY A 1 126 ? 7.003 45.028 -9.028 1.00 21.86 ? 142 GLY A O 1 ATOM 996 N N . LYS A 1 127 ? 4.936 45.443 -8.288 1.00 22.75 ? 143 LYS A N 1 ATOM 997 C CA . LYS A 1 127 ? 4.942 46.835 -8.725 1.00 23.77 ? 143 LYS A CA 1 ATOM 998 C C . LYS A 1 127 ? 6.168 47.623 -8.298 1.00 25.48 ? 143 LYS A C 1 ATOM 999 O O . LYS A 1 127 ? 6.633 47.497 -7.165 1.00 23.74 ? 143 LYS A O 1 ATOM 1000 C CB . LYS A 1 127 ? 3.710 47.568 -8.203 1.00 26.11 ? 143 LYS A CB 1 ATOM 1001 C CG . LYS A 1 127 ? 2.569 47.616 -9.165 1.00 32.52 ? 143 LYS A CG 1 ATOM 1002 C CD . LYS A 1 127 ? 1.723 48.800 -8.793 1.00 33.01 ? 143 LYS A CD 1 ATOM 1003 C CE . LYS A 1 127 ? 0.494 48.920 -9.621 1.00 35.90 ? 143 LYS A CE 1 ATOM 1004 N NZ . LYS A 1 127 ? -0.362 49.935 -8.950 1.00 35.16 ? 143 LYS A NZ 1 ATOM 1005 N N . ILE A 1 128 ? 6.688 48.438 -9.215 1.00 23.85 ? 144 ILE A N 1 ATOM 1006 C CA . ILE A 1 128 ? 7.839 49.255 -8.899 1.00 25.05 ? 144 ILE A CA 1 ATOM 1007 C C . ILE A 1 128 ? 7.459 50.738 -8.775 1.00 25.77 ? 144 ILE A C 1 ATOM 1008 O O . ILE A 1 128 ? 8.310 51.566 -8.451 1.00 28.16 ? 144 ILE A O 1 ATOM 1009 C CB . ILE A 1 128 ? 8.988 49.105 -9.926 1.00 27.18 ? 144 ILE A CB 1 ATOM 1010 C CG1 . ILE A 1 128 ? 8.511 49.524 -11.324 1.00 28.75 ? 144 ILE A CG1 1 ATOM 1011 C CG2 . ILE A 1 128 ? 9.507 47.653 -9.948 1.00 26.00 ? 144 ILE A CG2 1 ATOM 1012 C CD1 . ILE A 1 128 ? 9.637 49.580 -12.335 1.00 32.25 ? 144 ILE A CD1 1 ATOM 1013 N N . SER A 1 129 ? 6.188 51.055 -9.008 1.00 27.68 ? 145 SER A N 1 ATOM 1014 C CA . SER A 1 129 ? 5.667 52.421 -8.914 1.00 31.25 ? 145 SER A CA 1 ATOM 1015 C C . SER A 1 129 ? 4.138 52.291 -8.943 1.00 34.08 ? 145 SER A C 1 ATOM 1016 O O . SER A 1 129 ? 3.625 51.210 -9.246 1.00 34.94 ? 145 SER A O 1 ATOM 1017 C CB . SER A 1 129 ? 6.144 53.253 -10.109 1.00 32.20 ? 145 SER A CB 1 ATOM 1018 O OG . SER A 1 129 ? 5.463 52.852 -11.293 1.00 33.57 ? 145 SER A OG 1 ATOM 1019 N N . THR A 1 130 ? 3.392 53.361 -8.654 1.00 35.72 ? 146 THR A N 1 ATOM 1020 C CA . THR A 1 130 ? 1.927 53.232 -8.660 1.00 38.00 ? 146 THR A CA 1 ATOM 1021 C C . THR A 1 130 ? 1.366 52.821 -10.019 1.00 38.90 ? 146 THR A C 1 ATOM 1022 O O . THR A 1 130 ? 0.199 52.446 -10.121 1.00 39.73 ? 146 THR A O 1 ATOM 1023 C CB . THR A 1 130 ? 1.194 54.552 -8.257 1.00 40.42 ? 146 THR A CB 1 ATOM 1024 O OG1 . THR A 1 130 ? 1.591 55.609 -9.139 1.00 40.80 ? 146 THR A OG1 1 ATOM 1025 C CG2 . THR A 1 130 ? 1.505 54.945 -6.810 1.00 40.76 ? 146 THR A CG2 1 ATOM 1026 N N . THR A 1 131 ? 2.197 52.858 -11.055 1.00 39.35 ? 147 THR A N 1 ATOM 1027 C CA . THR A 1 131 ? 1.718 52.558 -12.400 1.00 41.25 ? 147 THR A CA 1 ATOM 1028 C C . THR A 1 131 ? 2.429 51.462 -13.174 1.00 41.01 ? 147 THR A C 1 ATOM 1029 O O . THR A 1 131 ? 2.019 51.130 -14.291 1.00 41.67 ? 147 THR A O 1 ATOM 1030 C CB . THR A 1 131 ? 1.832 53.817 -13.281 1.00 43.95 ? 147 THR A CB 1 ATOM 1031 O OG1 . THR A 1 131 ? 1.528 53.486 -14.645 1.00 46.82 ? 147 THR A OG1 1 ATOM 1032 C CG2 . THR A 1 131 ? 3.263 54.351 -13.228 1.00 43.24 ? 147 THR A CG2 1 ATOM 1033 N N . THR A 1 132 ? 3.475 50.882 -12.605 1.00 39.19 ? 148 THR A N 1 ATOM 1034 C CA . THR A 1 132 ? 4.240 49.935 -13.382 1.00 37.45 ? 148 THR A CA 1 ATOM 1035 C C . THR A 1 132 ? 4.686 48.638 -12.737 1.00 35.45 ? 148 THR A C 1 ATOM 1036 O O . THR A 1 132 ? 5.167 48.636 -11.607 1.00 34.99 ? 148 THR A O 1 ATOM 1037 C CB . THR A 1 132 ? 5.504 50.646 -13.906 1.00 38.78 ? 148 THR A CB 1 ATOM 1038 O OG1 . THR A 1 132 ? 5.116 51.817 -14.636 1.00 40.36 ? 148 THR A OG1 1 ATOM 1039 C CG2 . THR A 1 132 ? 6.330 49.727 -14.802 1.00 38.65 ? 148 THR A CG2 1 ATOM 1040 N N . TYR A 1 133 ? 4.513 47.550 -13.483 1.00 32.63 ? 149 TYR A N 1 ATOM 1041 C CA . TYR A 1 133 ? 4.966 46.225 -13.080 1.00 31.15 ? 149 TYR A CA 1 ATOM 1042 C C . TYR A 1 133 ? 6.212 46.002 -13.938 1.00 32.04 ? 149 TYR A C 1 ATOM 1043 O O . TYR A 1 133 ? 6.200 46.280 -15.139 1.00 35.29 ? 149 TYR A O 1 ATOM 1044 C CB . TYR A 1 133 ? 3.926 45.159 -13.404 1.00 30.31 ? 149 TYR A CB 1 ATOM 1045 C CG . TYR A 1 133 ? 2.827 45.056 -12.380 1.00 30.25 ? 149 TYR A CG 1 ATOM 1046 C CD1 . TYR A 1 133 ? 1.613 45.713 -12.558 1.00 30.33 ? 149 TYR A CD1 1 ATOM 1047 C CD2 . TYR A 1 133 ? 3.015 44.325 -11.201 1.00 30.17 ? 149 TYR A CD2 1 ATOM 1048 C CE1 . TYR A 1 133 ? 0.607 45.647 -11.583 1.00 30.24 ? 149 TYR A CE1 1 ATOM 1049 C CE2 . TYR A 1 133 ? 2.025 44.251 -10.231 1.00 28.27 ? 149 TYR A CE2 1 ATOM 1050 C CZ . TYR A 1 133 ? 0.827 44.915 -10.422 1.00 30.33 ? 149 TYR A CZ 1 ATOM 1051 O OH . TYR A 1 133 ? -0.138 44.877 -9.444 1.00 32.04 ? 149 TYR A OH 1 ATOM 1052 N N . PRO A 1 134 ? 7.302 45.498 -13.348 1.00 31.13 ? 152 PRO A N 1 ATOM 1053 C CA . PRO A 1 134 ? 8.521 45.280 -14.132 1.00 30.71 ? 152 PRO A CA 1 ATOM 1054 C C . PRO A 1 134 ? 8.592 43.944 -14.849 1.00 32.47 ? 152 PRO A C 1 ATOM 1055 O O . PRO A 1 134 ? 7.780 43.044 -14.607 1.00 31.18 ? 152 PRO A O 1 ATOM 1056 C CB . PRO A 1 134 ? 9.616 45.409 -13.085 1.00 29.92 ? 152 PRO A CB 1 ATOM 1057 C CG . PRO A 1 134 ? 8.979 44.718 -11.871 1.00 26.54 ? 152 PRO A CG 1 ATOM 1058 C CD . PRO A 1 134 ? 7.518 45.194 -11.913 1.00 29.95 ? 152 PRO A CD 1 ATOM 1059 N N . ASP A 1 135 ? 9.566 43.825 -15.748 1.00 33.34 ? 153 ASP A N 1 ATOM 1060 C CA . ASP A 1 135 ? 9.774 42.568 -16.448 1.00 34.11 ? 153 ASP A CA 1 ATOM 1061 C C . ASP A 1 135 ? 10.919 41.808 -15.796 1.00 32.50 ? 153 ASP A C 1 ATOM 1062 O O . ASP A 1 135 ? 11.018 40.585 -15.936 1.00 35.07 ? 153 ASP A O 1 ATOM 1063 C CB . ASP A 1 135 ? 10.057 42.805 -17.927 1.00 39.47 ? 153 ASP A CB 1 ATOM 1064 C CG . ASP A 1 135 ? 8.836 43.307 -18.656 1.00 42.66 ? 153 ASP A CG 1 ATOM 1065 O OD1 . ASP A 1 135 ? 7.756 42.692 -18.480 1.00 43.75 ? 153 ASP A OD1 1 ATOM 1066 O OD2 . ASP A 1 135 ? 8.958 44.310 -19.388 1.00 45.89 ? 153 ASP A OD2 1 ATOM 1067 N N . VAL A 1 136 ? 11.773 42.536 -15.078 1.00 30.33 ? 154 VAL A N 1 ATOM 1068 C CA . VAL A 1 136 ? 12.904 41.945 -14.361 1.00 28.96 ? 154 VAL A CA 1 ATOM 1069 C C . VAL A 1 136 ? 12.675 42.201 -12.864 1.00 27.60 ? 154 VAL A C 1 ATOM 1070 O O . VAL A 1 136 ? 12.112 43.225 -12.484 1.00 27.99 ? 154 VAL A O 1 ATOM 1071 C CB . VAL A 1 136 ? 14.250 42.586 -14.789 1.00 30.49 ? 154 VAL A CB 1 ATOM 1072 C CG1 . VAL A 1 136 ? 14.525 42.287 -16.267 1.00 30.48 ? 154 VAL A CG1 1 ATOM 1073 C CG2 . VAL A 1 136 ? 14.200 44.089 -14.589 1.00 31.33 ? 154 VAL A CG2 1 ATOM 1074 N N . PRO A 1 137 ? 13.108 41.282 -12.000 1.00 26.22 ? 155 PRO A N 1 ATOM 1075 C CA . PRO A 1 137 ? 12.890 41.519 -10.565 1.00 26.09 ? 155 PRO A CA 1 ATOM 1076 C C . PRO A 1 137 ? 13.674 42.724 -10.027 1.00 26.02 ? 155 PRO A C 1 ATOM 1077 O O . PRO A 1 137 ? 14.795 43.001 -10.483 1.00 24.83 ? 155 PRO A O 1 ATOM 1078 C CB . PRO A 1 137 ? 13.345 40.212 -9.936 1.00 26.02 ? 155 PRO A CB 1 ATOM 1079 C CG . PRO A 1 137 ? 14.503 39.810 -10.841 1.00 26.47 ? 155 PRO A CG 1 ATOM 1080 C CD . PRO A 1 137 ? 13.924 40.078 -12.225 1.00 25.69 ? 155 PRO A CD 1 ATOM 1081 N N . HIS A 1 138 ? 13.080 43.435 -9.072 1.00 23.11 ? 156 HIS A N 1 ATOM 1082 C CA . HIS A 1 138 ? 13.737 44.587 -8.458 1.00 23.62 ? 156 HIS A CA 1 ATOM 1083 C C . HIS A 1 138 ? 14.033 44.257 -7.000 1.00 24.09 ? 156 HIS A C 1 ATOM 1084 O O . HIS A 1 138 ? 13.299 43.495 -6.353 1.00 22.54 ? 156 HIS A O 1 ATOM 1085 C CB . HIS A 1 138 ? 12.875 45.848 -8.576 1.00 22.75 ? 156 HIS A CB 1 ATOM 1086 C CG . HIS A 1 138 ? 12.864 46.428 -9.952 1.00 27.26 ? 156 HIS A CG 1 ATOM 1087 N ND1 . HIS A 1 138 ? 12.504 45.686 -11.060 1.00 26.32 ? 156 HIS A ND1 1 ATOM 1088 C CD2 . HIS A 1 138 ? 13.204 47.660 -10.414 1.00 27.35 ? 156 HIS A CD2 1 ATOM 1089 C CE1 . HIS A 1 138 ? 12.626 46.438 -12.143 1.00 29.60 ? 156 HIS A CE1 1 ATOM 1090 N NE2 . HIS A 1 138 ? 13.047 47.635 -11.777 1.00 29.53 ? 156 HIS A NE2 1 ATOM 1091 N N . CYS A 1 139 ? 15.106 44.854 -6.502 1.00 23.87 ? 157 CYS A N 1 ATOM 1092 C CA . CYS A 1 139 ? 15.628 44.606 -5.162 1.00 23.82 ? 157 CYS A CA 1 ATOM 1093 C C . CYS A 1 139 ? 15.934 45.900 -4.423 1.00 25.48 ? 157 CYS A C 1 ATOM 1094 O O . CYS A 1 139 ? 16.192 46.927 -5.045 1.00 25.29 ? 157 CYS A O 1 ATOM 1095 C CB . CYS A 1 139 ? 16.978 43.858 -5.288 1.00 25.18 ? 157 CYS A CB 1 ATOM 1096 S SG . CYS A 1 139 ? 16.930 42.096 -5.720 1.00 31.08 ? 157 CYS A SG 1 ATOM 1097 N N . THR A 1 140 ? 15.961 45.820 -3.096 1.00 23.94 ? 158 THR A N 1 ATOM 1098 C CA . THR A 1 140 ? 16.359 46.939 -2.258 1.00 24.84 ? 158 THR A CA 1 ATOM 1099 C C . THR A 1 140 ? 16.562 46.412 -0.831 1.00 24.08 ? 158 THR A C 1 ATOM 1100 O O . THR A 1 140 ? 16.176 45.292 -0.510 1.00 23.78 ? 158 THR A O 1 ATOM 1101 C CB . THR A 1 140 ? 15.339 48.118 -2.258 1.00 25.75 ? 158 THR A CB 1 ATOM 1102 O OG1 . THR A 1 140 ? 15.980 49.280 -1.687 1.00 26.35 ? 158 THR A OG1 1 ATOM 1103 C CG2 . THR A 1 140 ? 14.093 47.787 -1.412 1.00 24.42 ? 158 THR A CG2 1 ATOM 1104 N N . ASN A 1 141 ? 17.157 47.231 0.023 1.00 24.28 ? 159 ASN A N 1 ATOM 1105 C CA . ASN A 1 141 ? 17.396 46.827 1.397 1.00 26.53 ? 159 ASN A CA 1 ATOM 1106 C C . ASN A 1 141 ? 16.459 47.538 2.339 1.00 24.84 ? 159 ASN A C 1 ATOM 1107 O O . ASN A 1 141 ? 16.145 48.718 2.140 1.00 27.23 ? 159 ASN A O 1 ATOM 1108 C CB . ASN A 1 141 ? 18.844 47.150 1.782 1.00 28.71 ? 159 ASN A CB 1 ATOM 1109 C CG . ASN A 1 141 ? 19.837 46.382 0.943 1.00 31.01 ? 159 ASN A CG 1 ATOM 1110 O OD1 . ASN A 1 141 ? 19.598 45.221 0.600 1.00 30.06 ? 159 ASN A OD1 1 ATOM 1111 N ND2 . ASN A 1 141 ? 20.960 47.016 0.610 1.00 33.89 ? 159 ASN A ND2 1 ATOM 1112 N N . ILE A 1 142 ? 16.019 46.815 3.363 1.00 24.16 ? 160 ILE A N 1 ATOM 1113 C CA . ILE A 1 142 ? 15.158 47.383 4.370 1.00 24.38 ? 160 ILE A CA 1 ATOM 1114 C C . ILE A 1 142 ? 15.632 46.852 5.718 1.00 25.14 ? 160 ILE A C 1 ATOM 1115 O O . ILE A 1 142 ? 16.538 46.028 5.786 1.00 26.53 ? 160 ILE A O 1 ATOM 1116 C CB . ILE A 1 142 ? 13.682 47.009 4.132 1.00 22.92 ? 160 ILE A CB 1 ATOM 1117 C CG1 . ILE A 1 142 ? 13.484 45.492 4.217 1.00 21.41 ? 160 ILE A CG1 1 ATOM 1118 C CG2 . ILE A 1 142 ? 13.243 47.529 2.765 1.00 23.51 ? 160 ILE A CG2 1 ATOM 1119 C CD1 . ILE A 1 142 ? 11.990 45.101 4.167 1.00 23.10 ? 160 ILE A CD1 1 ATOM 1120 N N . PHE A 1 143 ? 15.017 47.326 6.789 1.00 26.09 ? 161 PHE A N 1 ATOM 1121 C CA . PHE A 1 143 ? 15.403 46.893 8.116 1.00 26.14 ? 161 PHE A CA 1 ATOM 1122 C C . PHE A 1 143 ? 14.235 46.290 8.836 1.00 27.01 ? 161 PHE A C 1 ATOM 1123 O O . PHE A 1 143 ? 13.081 46.649 8.574 1.00 24.88 ? 161 PHE A O 1 ATOM 1124 C CB . PHE A 1 143 ? 15.880 48.100 8.931 1.00 28.14 ? 161 PHE A CB 1 ATOM 1125 C CG . PHE A 1 143 ? 17.169 48.668 8.457 1.00 30.64 ? 161 PHE A CG 1 ATOM 1126 C CD1 . PHE A 1 143 ? 18.378 48.140 8.907 1.00 32.81 ? 161 PHE A CD1 1 ATOM 1127 C CD2 . PHE A 1 143 ? 17.186 49.696 7.534 1.00 32.35 ? 161 PHE A CD2 1 ATOM 1128 C CE1 . PHE A 1 143 ? 19.587 48.632 8.435 1.00 34.03 ? 161 PHE A CE1 1 ATOM 1129 C CE2 . PHE A 1 143 ? 18.403 50.200 7.052 1.00 35.22 ? 161 PHE A CE2 1 ATOM 1130 C CZ . PHE A 1 143 ? 19.595 49.668 7.500 1.00 33.94 ? 161 PHE A CZ 1 ATOM 1131 N N . ILE A 1 144 ? 14.528 45.362 9.743 1.00 26.08 ? 162 ILE A N 1 ATOM 1132 C CA . ILE A 1 144 ? 13.481 44.821 10.563 1.00 27.73 ? 162 ILE A CA 1 ATOM 1133 C C . ILE A 1 144 ? 13.348 45.933 11.596 1.00 27.57 ? 162 ILE A C 1 ATOM 1134 O O . ILE A 1 144 ? 14.355 46.447 12.085 1.00 28.59 ? 162 ILE A O 1 ATOM 1135 C CB . ILE A 1 144 ? 13.899 43.531 11.273 1.00 28.07 ? 162 ILE A CB 1 ATOM 1136 C CG1 . ILE A 1 144 ? 14.042 42.395 10.251 1.00 30.00 ? 162 ILE A CG1 1 ATOM 1137 C CG2 . ILE A 1 144 ? 12.852 43.191 12.339 1.00 25.94 ? 162 ILE A CG2 1 ATOM 1138 C CD1 . ILE A 1 144 ? 14.573 41.092 10.845 1.00 31.34 ? 162 ILE A CD1 1 ATOM 1139 N N . VAL A 1 145 ? 12.122 46.332 11.897 1.00 28.65 ? 163 VAL A N 1 ATOM 1140 C CA . VAL A 1 145 ? 11.893 47.397 12.863 1.00 30.01 ? 163 VAL A CA 1 ATOM 1141 C C . VAL A 1 145 ? 10.998 46.890 13.970 1.00 30.81 ? 163 VAL A C 1 ATOM 1142 O O . VAL A 1 145 ? 10.467 45.793 13.882 1.00 30.82 ? 163 VAL A O 1 ATOM 1143 C CB . VAL A 1 145 ? 11.218 48.616 12.214 1.00 28.48 ? 163 VAL A CB 1 ATOM 1144 C CG1 . VAL A 1 145 ? 12.094 49.150 11.118 1.00 29.44 ? 163 VAL A CG1 1 ATOM 1145 C CG2 . VAL A 1 145 ? 9.840 48.239 11.697 1.00 28.54 ? 163 VAL A CG2 1 ATOM 1146 N N . LYS A 1 146 ? 10.822 47.698 15.009 1.00 33.41 ? 164 LYS A N 1 ATOM 1147 C CA . LYS A 1 146 ? 9.976 47.297 16.123 1.00 36.09 ? 164 LYS A CA 1 ATOM 1148 C C . LYS A 1 146 ? 8.585 46.970 15.624 1.00 37.17 ? 164 LYS A C 1 ATOM 1149 O O . LYS A 1 146 ? 8.024 47.686 14.792 1.00 35.97 ? 164 LYS A O 1 ATOM 1150 C CB . LYS A 1 146 ? 9.893 48.406 17.173 1.00 37.88 ? 164 LYS A CB 1 ATOM 1151 C CG . LYS A 1 146 ? 11.164 48.586 17.982 1.00 43.21 ? 164 LYS A CG 1 ATOM 1152 C CD . LYS A 1 146 ? 11.033 49.764 18.947 1.00 46.33 ? 164 LYS A CD 1 ATOM 1153 C CE . LYS A 1 146 ? 12.388 50.140 19.529 1.00 49.85 ? 164 LYS A CE 1 ATOM 1154 N NZ . LYS A 1 146 ? 12.354 51.477 20.209 1.00 53.10 ? 164 LYS A NZ 1 ATOM 1155 N N . HIS A 1 147 ? 8.038 45.881 16.147 1.00 37.57 ? 165 HIS A N 1 ATOM 1156 C CA . HIS A 1 147 ? 6.712 45.428 15.768 1.00 39.39 ? 165 HIS A CA 1 ATOM 1157 C C . HIS A 1 147 ? 5.641 46.485 16.036 1.00 40.69 ? 165 HIS A C 1 ATOM 1158 O O . HIS A 1 147 ? 4.600 46.507 15.374 1.00 40.91 ? 165 HIS A O 1 ATOM 1159 C CB . HIS A 1 147 ? 6.397 44.136 16.521 1.00 40.41 ? 165 HIS A CB 1 ATOM 1160 C CG . HIS A 1 147 ? 5.805 43.067 15.661 1.00 41.24 ? 165 HIS A CG 1 ATOM 1161 N ND1 . HIS A 1 147 ? 4.444 42.878 15.538 1.00 42.58 ? 165 HIS A ND1 1 ATOM 1162 C CD2 . HIS A 1 147 ? 6.387 42.147 14.857 1.00 42.85 ? 165 HIS A CD2 1 ATOM 1163 C CE1 . HIS A 1 147 ? 4.215 41.886 14.695 1.00 43.97 ? 165 HIS A CE1 1 ATOM 1164 N NE2 . HIS A 1 147 ? 5.377 41.426 14.267 1.00 43.74 ? 165 HIS A NE2 1 ATOM 1165 N N . LYS A 1 148 ? 5.899 47.368 16.998 1.00 40.02 ? 166 LYS A N 1 ATOM 1166 C CA . LYS A 1 148 ? 4.945 48.417 17.331 1.00 40.91 ? 166 LYS A CA 1 ATOM 1167 C C . LYS A 1 148 ? 4.571 49.273 16.119 1.00 39.14 ? 166 LYS A C 1 ATOM 1168 O O . LYS A 1 148 ? 3.450 49.762 16.027 1.00 40.10 ? 166 LYS A O 1 ATOM 1169 C CB . LYS A 1 148 ? 5.501 49.339 18.420 1.00 43.64 ? 166 LYS A CB 1 ATOM 1170 C CG . LYS A 1 148 ? 6.662 50.200 17.946 1.00 47.46 ? 166 LYS A CG 1 ATOM 1171 C CD . LYS A 1 148 ? 6.860 51.427 18.819 1.00 51.00 ? 166 LYS A CD 1 ATOM 1172 C CE . LYS A 1 148 ? 8.008 52.286 18.295 1.00 52.17 ? 166 LYS A CE 1 ATOM 1173 N NZ . LYS A 1 148 ? 8.224 53.525 19.110 1.00 54.14 ? 166 LYS A NZ 1 ATOM 1174 N N . TRP A 1 149 ? 5.507 49.482 15.198 1.00 36.23 ? 167 TRP A N 1 ATOM 1175 C CA . TRP A 1 149 ? 5.188 50.293 14.029 1.00 35.00 ? 167 TRP A CA 1 ATOM 1176 C C . TRP A 1 149 ? 4.076 49.650 13.194 1.00 34.21 ? 167 TRP A C 1 ATOM 1177 O O . TRP A 1 149 ? 3.276 50.357 12.592 1.00 33.70 ? 167 TRP A O 1 ATOM 1178 C CB . TRP A 1 149 ? 6.429 50.499 13.156 1.00 33.03 ? 167 TRP A CB 1 ATOM 1179 C CG . TRP A 1 149 ? 7.439 51.413 13.757 1.00 34.02 ? 167 TRP A CG 1 ATOM 1180 C CD1 . TRP A 1 149 ? 8.688 51.087 14.195 1.00 36.69 ? 167 TRP A CD1 1 ATOM 1181 C CD2 . TRP A 1 149 ? 7.276 52.811 13.999 1.00 35.30 ? 167 TRP A CD2 1 ATOM 1182 N NE1 . TRP A 1 149 ? 9.317 52.203 14.697 1.00 37.29 ? 167 TRP A NE1 1 ATOM 1183 C CE2 . TRP A 1 149 ? 8.469 53.275 14.588 1.00 35.85 ? 167 TRP A CE2 1 ATOM 1184 C CE3 . TRP A 1 149 ? 6.230 53.721 13.770 1.00 35.50 ? 167 TRP A CE3 1 ATOM 1185 C CZ2 . TRP A 1 149 ? 8.652 54.612 14.959 1.00 37.52 ? 167 TRP A CZ2 1 ATOM 1186 C CZ3 . TRP A 1 149 ? 6.410 55.052 14.138 1.00 37.44 ? 167 TRP A CZ3 1 ATOM 1187 C CH2 . TRP A 1 149 ? 7.617 55.484 14.728 1.00 37.34 ? 167 TRP A CH2 1 ATOM 1188 N N . CYS A 1 150 ? 4.037 48.314 13.159 1.00 33.90 ? 168 CYS A N 1 ATOM 1189 C CA . CYS A 1 150 ? 3.037 47.574 12.375 1.00 33.72 ? 168 CYS A CA 1 ATOM 1190 C C . CYS A 1 150 ? 1.689 47.346 13.057 1.00 36.19 ? 168 CYS A C 1 ATOM 1191 O O . CYS A 1 150 ? 0.646 47.390 12.404 1.00 35.05 ? 168 CYS A O 1 ATOM 1192 C CB . CYS A 1 150 ? 3.585 46.198 11.957 1.00 32.01 ? 168 CYS A CB 1 ATOM 1193 S SG . CYS A 1 150 ? 4.805 46.173 10.585 1.00 27.67 ? 168 CYS A SG 1 ATOM 1194 N N . GLU A 1 151 ? 1.712 47.090 14.362 1.00 37.14 ? 169 GLU A N 1 ATOM 1195 C CA . GLU A 1 151 ? 0.487 46.791 15.103 1.00 39.94 ? 169 GLU A CA 1 ATOM 1196 C C . GLU A 1 151 ? -0.713 47.707 14.869 1.00 39.11 ? 169 GLU A C 1 ATOM 1197 O O . GLU A 1 151 ? -1.819 47.222 14.645 1.00 40.75 ? 169 GLU A O 1 ATOM 1198 C CB . GLU A 1 151 ? 0.820 46.644 16.593 1.00 42.08 ? 169 GLU A CB 1 ATOM 1199 C CG . GLU A 1 151 ? 1.326 45.227 16.915 1.00 45.29 ? 169 GLU A CG 1 ATOM 1200 C CD . GLU A 1 151 ? 2.252 45.163 18.117 1.00 48.88 ? 169 GLU A CD 1 ATOM 1201 O OE1 . GLU A 1 151 ? 1.946 45.825 19.135 1.00 49.34 ? 169 GLU A OE1 1 ATOM 1202 O OE2 . GLU A 1 151 ? 3.282 44.439 18.044 1.00 47.96 ? 169 GLU A OE2 1 ATOM 1203 N N . PRO A 1 152 ? -0.518 49.034 14.901 1.00 38.70 ? 170 PRO A N 1 ATOM 1204 C CA . PRO A 1 152 ? -1.642 49.951 14.673 1.00 38.83 ? 170 PRO A CA 1 ATOM 1205 C C . PRO A 1 152 ? -2.099 50.003 13.213 1.00 37.76 ? 170 PRO A C 1 ATOM 1206 O O . PRO A 1 152 ? -3.253 50.329 12.918 1.00 39.40 ? 170 PRO A O 1 ATOM 1207 C CB . PRO A 1 152 ? -1.095 51.298 15.152 1.00 39.73 ? 170 PRO A CB 1 ATOM 1208 C CG . PRO A 1 152 ? 0.384 51.170 14.883 1.00 40.37 ? 170 PRO A CG 1 ATOM 1209 C CD . PRO A 1 152 ? 0.676 49.767 15.357 1.00 38.62 ? 170 PRO A CD 1 ATOM 1210 N N . LEU A 1 153 ? -1.194 49.674 12.298 1.00 33.88 ? 171 LEU A N 1 ATOM 1211 C CA . LEU A 1 153 ? -1.517 49.704 10.878 1.00 32.45 ? 171 LEU A CA 1 ATOM 1212 C C . LEU A 1 153 ? -2.309 48.482 10.451 1.00 29.86 ? 171 LEU A C 1 ATOM 1213 O O . LEU A 1 153 ? -3.186 48.564 9.594 1.00 29.22 ? 171 LEU A O 1 ATOM 1214 C CB . LEU A 1 153 ? -0.228 49.747 10.047 1.00 32.73 ? 171 LEU A CB 1 ATOM 1215 C CG . LEU A 1 153 ? 0.759 50.869 10.353 1.00 33.28 ? 171 LEU A CG 1 ATOM 1216 C CD1 . LEU A 1 153 ? 1.969 50.736 9.445 1.00 31.06 ? 171 LEU A CD1 1 ATOM 1217 C CD2 . LEU A 1 153 ? 0.064 52.207 10.161 1.00 33.02 ? 171 LEU A CD2 1 ATOM 1218 N N . TYR A 1 154 ? -1.993 47.347 11.058 1.00 28.89 ? 172 TYR A N 1 ATOM 1219 C CA . TYR A 1 154 ? -2.635 46.100 10.686 1.00 30.97 ? 172 TYR A CA 1 ATOM 1220 C C . TYR A 1 154 ? -3.230 45.414 11.915 1.00 33.17 ? 172 TYR A C 1 ATOM 1221 O O . TYR A 1 154 ? -2.600 44.547 12.512 1.00 33.58 ? 172 TYR A O 1 ATOM 1222 C CB . TYR A 1 154 ? -1.591 45.191 10.006 1.00 28.23 ? 172 TYR A CB 1 ATOM 1223 C CG . TYR A 1 154 ? -0.673 45.958 9.061 1.00 27.38 ? 172 TYR A CG 1 ATOM 1224 C CD1 . TYR A 1 154 ? 0.702 46.038 9.299 1.00 26.09 ? 172 TYR A CD1 1 ATOM 1225 C CD2 . TYR A 1 154 ? -1.189 46.628 7.948 1.00 27.13 ? 172 TYR A CD2 1 ATOM 1226 C CE1 . TYR A 1 154 ? 1.549 46.775 8.444 1.00 26.65 ? 172 TYR A CE1 1 ATOM 1227 C CE2 . TYR A 1 154 ? -0.356 47.367 7.091 1.00 27.80 ? 172 TYR A CE2 1 ATOM 1228 C CZ . TYR A 1 154 ? 1.006 47.441 7.347 1.00 26.32 ? 172 TYR A CZ 1 ATOM 1229 O OH . TYR A 1 154 ? 1.806 48.222 6.528 1.00 25.06 ? 172 TYR A OH 1 ATOM 1230 N N . PRO A 1 155 A -4.456 45.809 12.304 1.00 35.67 ? 172 PRO A N 1 ATOM 1231 C CA . PRO A 1 155 A -5.173 45.263 13.458 1.00 38.95 ? 172 PRO A CA 1 ATOM 1232 C C . PRO A 1 155 A -5.204 43.744 13.500 1.00 40.83 ? 172 PRO A C 1 ATOM 1233 O O . PRO A 1 155 A -5.196 43.151 14.580 1.00 42.79 ? 172 PRO A O 1 ATOM 1234 C CB . PRO A 1 155 A -6.569 45.857 13.303 1.00 39.92 ? 172 PRO A CB 1 ATOM 1235 C CG . PRO A 1 155 A -6.289 47.189 12.708 1.00 38.59 ? 172 PRO A CG 1 ATOM 1236 C CD . PRO A 1 155 A -5.258 46.862 11.651 1.00 37.36 ? 172 PRO A CD 1 ATOM 1237 N N . TRP A 1 156 ? -5.237 43.120 12.323 1.00 41.41 ? 173 TRP A N 1 ATOM 1238 C CA . TRP A 1 156 ? -5.275 41.668 12.204 1.00 41.59 ? 173 TRP A CA 1 ATOM 1239 C C . TRP A 1 156 ? -3.919 40.997 12.483 1.00 42.04 ? 173 TRP A C 1 ATOM 1240 O O . TRP A 1 156 ? -3.809 39.773 12.503 1.00 43.60 ? 173 TRP A O 1 ATOM 1241 C CB . TRP A 1 156 ? -5.809 41.288 10.811 1.00 41.67 ? 173 TRP A CB 1 ATOM 1242 C CG . TRP A 1 156 ? -5.134 42.011 9.669 1.00 41.93 ? 173 TRP A CG 1 ATOM 1243 C CD1 . TRP A 1 156 ? -4.061 41.575 8.941 1.00 41.86 ? 173 TRP A CD1 1 ATOM 1244 C CD2 . TRP A 1 156 ? -5.439 43.325 9.185 1.00 42.10 ? 173 TRP A CD2 1 ATOM 1245 N NE1 . TRP A 1 156 ? -3.673 42.543 8.035 1.00 42.24 ? 173 TRP A NE1 1 ATOM 1246 C CE2 . TRP A 1 156 ? -4.500 43.626 8.166 1.00 42.09 ? 173 TRP A CE2 1 ATOM 1247 C CE3 . TRP A 1 156 ? -6.408 44.281 9.514 1.00 42.50 ? 173 TRP A CE3 1 ATOM 1248 C CZ2 . TRP A 1 156 ? -4.504 44.844 7.477 1.00 41.66 ? 173 TRP A CZ2 1 ATOM 1249 C CZ3 . TRP A 1 156 ? -6.410 45.501 8.823 1.00 43.34 ? 173 TRP A CZ3 1 ATOM 1250 C CH2 . TRP A 1 156 ? -5.462 45.767 7.819 1.00 42.02 ? 173 TRP A CH2 1 ATOM 1251 N N . VAL A 1 157 ? -2.890 41.797 12.723 1.00 41.84 ? 174 VAL A N 1 ATOM 1252 C CA . VAL A 1 157 ? -1.564 41.262 13.017 1.00 43.01 ? 174 VAL A CA 1 ATOM 1253 C C . VAL A 1 157 ? -1.157 41.647 14.448 1.00 44.61 ? 174 VAL A C 1 ATOM 1254 O O . VAL A 1 157 ? -0.532 42.695 14.668 1.00 45.40 ? 174 VAL A O 1 ATOM 1255 C CB . VAL A 1 157 ? -0.515 41.819 12.031 1.00 41.95 ? 174 VAL A CB 1 ATOM 1256 C CG1 . VAL A 1 157 ? 0.875 41.296 12.387 1.00 41.19 ? 174 VAL A CG1 1 ATOM 1257 C CG2 . VAL A 1 157 ? -0.895 41.444 10.614 1.00 39.83 ? 174 VAL A CG2 1 ATOM 1258 N N . PRO A 1 158 ? -1.496 40.798 15.435 1.00 45.79 ? 175 PRO A N 1 ATOM 1259 C CA . PRO A 1 158 ? -1.184 41.033 16.851 1.00 46.83 ? 175 PRO A CA 1 ATOM 1260 C C . PRO A 1 158 ? 0.299 41.069 17.235 1.00 47.76 ? 175 PRO A C 1 ATOM 1261 O O . PRO A 1 158 ? 1.175 40.666 16.467 1.00 47.13 ? 175 PRO A O 1 ATOM 1262 C CB . PRO A 1 158 ? -1.934 39.901 17.554 1.00 46.89 ? 175 PRO A CB 1 ATOM 1263 C CG . PRO A 1 158 ? -1.867 38.800 16.564 1.00 46.40 ? 175 PRO A CG 1 ATOM 1264 C CD . PRO A 1 158 ? -2.209 39.520 15.274 1.00 46.00 ? 175 PRO A CD 1 ATOM 1265 N N . ALA A 1 159 ? 0.569 41.565 18.438 1.00 47.86 ? 176 ALA A N 1 ATOM 1266 C CA . ALA A 1 159 ? 1.931 41.649 18.933 1.00 48.62 ? 176 ALA A CA 1 ATOM 1267 C C . ALA A 1 159 ? 2.485 40.235 19.109 1.00 49.09 ? 176 ALA A C 1 ATOM 1268 O O . ALA A 1 159 ? 3.695 40.030 19.170 1.00 49.41 ? 176 ALA A O 1 ATOM 1269 C CB . ALA A 1 159 ? 1.952 42.398 20.261 1.00 49.22 ? 176 ALA A CB 1 ATOM 1270 N N . ASP A 1 160 ? 1.584 39.262 19.181 1.00 49.92 ? 177 ASP A N 1 ATOM 1271 C CA . ASP A 1 160 ? 1.965 37.864 19.353 1.00 50.39 ? 177 ASP A CA 1 ATOM 1272 C C . ASP A 1 160 ? 2.061 37.145 18.017 1.00 48.86 ? 177 ASP A C 1 ATOM 1273 O O . ASP A 1 160 ? 2.256 35.933 17.962 1.00 49.45 ? 177 ASP A O 1 ATOM 1274 C CB . ASP A 1 160 ? 0.935 37.152 20.230 1.00 52.67 ? 177 ASP A CB 1 ATOM 1275 C CG . ASP A 1 160 ? 1.412 36.970 21.649 1.00 55.35 ? 177 ASP A CG 1 ATOM 1276 O OD1 . ASP A 1 160 ? 2.269 37.776 22.090 1.00 55.37 ? 177 ASP A OD1 1 ATOM 1277 O OD2 . ASP A 1 160 ? 0.921 36.029 22.322 1.00 56.39 ? 177 ASP A OD2 1 ATOM 1278 N N . SER A 1 161 ? 1.898 37.898 16.942 1.00 46.20 ? 178 SER A N 1 ATOM 1279 C CA . SER A 1 161 ? 1.959 37.334 15.601 1.00 43.31 ? 178 SER A CA 1 ATOM 1280 C C . SER A 1 161 ? 3.373 36.852 15.284 1.00 40.23 ? 178 SER A C 1 ATOM 1281 O O . SER A 1 161 ? 4.356 37.497 15.655 1.00 40.48 ? 178 SER A O 1 ATOM 1282 C CB . SER A 1 161 ? 1.520 38.402 14.592 1.00 43.20 ? 178 SER A CB 1 ATOM 1283 O OG . SER A 1 161 ? 1.663 37.958 13.257 1.00 45.12 ? 178 SER A OG 1 ATOM 1284 N N . ARG A 1 162 ? 3.475 35.702 14.627 1.00 38.01 ? 179 ARG A N 1 ATOM 1285 C CA . ARG A 1 162 ? 4.777 35.169 14.238 1.00 36.38 ? 179 ARG A CA 1 ATOM 1286 C C . ARG A 1 162 ? 5.150 35.859 12.915 1.00 34.16 ? 179 ARG A C 1 ATOM 1287 O O . ARG A 1 162 ? 5.218 35.243 11.849 1.00 30.58 ? 179 ARG A O 1 ATOM 1288 C CB . ARG A 1 162 ? 4.691 33.654 14.065 1.00 39.74 ? 179 ARG A CB 1 ATOM 1289 C CG . ARG A 1 162 ? 4.249 32.940 15.354 1.00 44.27 ? 179 ARG A CG 1 ATOM 1290 C CD . ARG A 1 162 ? 4.254 31.432 15.206 1.00 47.48 ? 179 ARG A CD 1 ATOM 1291 N NE . ARG A 1 162 ? 3.703 30.739 16.377 1.00 50.77 ? 179 ARG A NE 1 ATOM 1292 C CZ . ARG A 1 162 ? 4.241 30.766 17.594 1.00 52.55 ? 179 ARG A CZ 1 ATOM 1293 N NH1 . ARG A 1 162 ? 5.355 31.454 17.820 1.00 52.84 ? 179 ARG A NH1 1 ATOM 1294 N NH2 . ARG A 1 162 ? 3.667 30.098 18.589 1.00 52.94 ? 179 ARG A NH2 1 ATOM 1295 N N . THR A 1 163 ? 5.384 37.160 13.015 1.00 32.03 ? 180 THR A N 1 ATOM 1296 C CA . THR A 1 163 ? 5.714 37.968 11.864 1.00 30.53 ? 180 THR A CA 1 ATOM 1297 C C . THR A 1 163 ? 6.822 38.946 12.174 1.00 31.34 ? 180 THR A C 1 ATOM 1298 O O . THR A 1 163 ? 7.136 39.225 13.336 1.00 31.91 ? 180 THR A O 1 ATOM 1299 C CB . THR A 1 163 ? 4.487 38.779 11.399 1.00 31.57 ? 180 THR A CB 1 ATOM 1300 O OG1 . THR A 1 163 ? 3.933 39.492 12.510 1.00 33.38 ? 180 THR A OG1 1 ATOM 1301 C CG2 . THR A 1 163 ? 3.428 37.878 10.846 1.00 28.90 ? 180 THR A CG2 1 ATOM 1302 N N . LEU A 1 164 ? 7.443 39.446 11.120 1.00 26.42 ? 181 LEU A N 1 ATOM 1303 C CA . LEU A 1 164 ? 8.478 40.436 11.257 1.00 26.39 ? 181 LEU A CA 1 ATOM 1304 C C . LEU A 1 164 ? 7.910 41.685 10.612 1.00 27.05 ? 181 LEU A C 1 ATOM 1305 O O . LEU A 1 164 ? 7.267 41.596 9.556 1.00 26.14 ? 181 LEU A O 1 ATOM 1306 C CB . LEU A 1 164 ? 9.732 40.023 10.503 1.00 27.09 ? 181 LEU A CB 1 ATOM 1307 C CG . LEU A 1 164 ? 10.485 38.792 11.002 1.00 28.48 ? 181 LEU A CG 1 ATOM 1308 C CD1 . LEU A 1 164 ? 11.634 38.475 10.052 1.00 26.14 ? 181 LEU A CD1 1 ATOM 1309 C CD2 . LEU A 1 164 ? 11.034 39.077 12.387 1.00 28.18 ? 181 LEU A CD2 1 ATOM 1310 N N . CYS A 1 165 ? 8.141 42.827 11.256 1.00 26.00 ? 182 CYS A N 1 ATOM 1311 C CA . CYS A 1 165 ? 7.702 44.132 10.765 1.00 26.75 ? 182 CYS A CA 1 ATOM 1312 C C . CYS A 1 165 ? 8.960 44.697 10.117 1.00 27.32 ? 182 CYS A C 1 ATOM 1313 O O . CYS A 1 165 ? 10.023 44.760 10.756 1.00 28.42 ? 182 CYS A O 1 ATOM 1314 C CB . CYS A 1 165 ? 7.255 45.013 11.937 1.00 28.62 ? 182 CYS A CB 1 ATOM 1315 S SG . CYS A 1 165 ? 6.584 46.644 11.444 1.00 29.11 ? 182 CYS A SG 1 ATOM 1316 N N . ALA A 1 166 ? 8.871 45.114 8.859 1.00 25.38 ? 183 ALA A N 1 ATOM 1317 C CA . ALA A 1 166 ? 10.080 45.580 8.211 1.00 23.56 ? 183 ALA A CA 1 ATOM 1318 C C . ALA A 1 166 ? 9.881 46.575 7.077 1.00 23.30 ? 183 ALA A C 1 ATOM 1319 O O . ALA A 1 166 ? 8.866 46.547 6.381 1.00 20.75 ? 183 ALA A O 1 ATOM 1320 C CB . ALA A 1 166 ? 10.873 44.357 7.700 1.00 22.11 ? 183 ALA A CB 1 ATOM 1321 N N . GLY A 1 167 ? 10.886 47.430 6.897 1.00 22.31 ? 184 GLY A N 1 ATOM 1322 C CA . GLY A 1 167 ? 10.866 48.424 5.849 1.00 22.86 ? 184 GLY A CA 1 ATOM 1323 C C . GLY A 1 167 ? 11.842 49.541 6.154 1.00 24.36 ? 184 GLY A C 1 ATOM 1324 O O . GLY A 1 167 ? 12.868 49.325 6.819 1.00 22.17 ? 184 GLY A O 1 ATOM 1325 N N . ILE A 1 168 ? 11.528 50.731 5.649 1.00 24.68 ? 185 ILE A N 1 ATOM 1326 C CA . ILE A 1 168 ? 12.355 51.923 5.835 1.00 25.84 ? 185 ILE A CA 1 ATOM 1327 C C . ILE A 1 168 ? 11.373 52.957 6.397 1.00 26.78 ? 185 ILE A C 1 ATOM 1328 O O . ILE A 1 168 ? 10.445 53.391 5.706 1.00 25.36 ? 185 ILE A O 1 ATOM 1329 C CB . ILE A 1 168 ? 12.957 52.386 4.464 1.00 28.06 ? 185 ILE A CB 1 ATOM 1330 C CG1 . ILE A 1 168 ? 13.965 51.340 3.969 1.00 26.58 ? 185 ILE A CG1 1 ATOM 1331 C CG2 . ILE A 1 168 ? 13.674 53.754 4.603 1.00 30.47 ? 185 ILE A CG2 1 ATOM 1332 C CD1 . ILE A 1 168 ? 15.213 51.252 4.838 1.00 29.00 ? 185 ILE A CD1 1 ATOM 1333 N N . LEU A 1 169 ? 11.569 53.335 7.654 1.00 26.00 ? 186 LEU A N 1 ATOM 1334 C CA . LEU A 1 169 ? 10.665 54.272 8.325 1.00 27.35 ? 186 LEU A CA 1 ATOM 1335 C C . LEU A 1 169 ? 10.540 55.607 7.623 1.00 27.22 ? 186 LEU A C 1 ATOM 1336 O O . LEU A 1 169 ? 9.480 56.249 7.671 1.00 27.72 ? 186 LEU A O 1 ATOM 1337 C CB . LEU A 1 169 ? 11.101 54.494 9.781 1.00 28.16 ? 186 LEU A CB 1 ATOM 1338 C CG . LEU A 1 169 ? 10.998 53.254 10.669 1.00 28.36 ? 186 LEU A CG 1 ATOM 1339 C CD1 . LEU A 1 169 ? 11.512 53.586 12.061 1.00 31.65 ? 186 LEU A CD1 1 ATOM 1340 C CD2 . LEU A 1 169 ? 9.567 52.763 10.726 1.00 27.96 ? 186 LEU A CD2 1 ATOM 1341 N N . LYS A 1 170 A 11.622 56.019 6.975 1.00 28.10 ? 186 LYS A N 1 ATOM 1342 C CA . LYS A 1 170 A 11.646 57.273 6.233 1.00 29.63 ? 186 LYS A CA 1 ATOM 1343 C C . LYS A 1 170 A 10.633 57.238 5.081 1.00 29.65 ? 186 LYS A C 1 ATOM 1344 O O . LYS A 1 170 A 10.078 58.283 4.707 1.00 29.40 ? 186 LYS A O 1 ATOM 1345 C CB . LYS A 1 170 A 13.047 57.502 5.661 1.00 32.35 ? 186 LYS A CB 1 ATOM 1346 C CG . LYS A 1 170 A 13.202 58.776 4.843 1.00 37.64 ? 186 LYS A CG 1 ATOM 1347 C CD . LYS A 1 170 A 14.590 58.834 4.190 1.00 41.30 ? 186 LYS A CD 1 ATOM 1348 C CE . LYS A 1 170 A 14.780 57.688 3.177 1.00 44.23 ? 186 LYS A CE 1 ATOM 1349 N NZ . LYS A 1 170 A 15.995 56.837 3.437 1.00 46.23 ? 186 LYS A NZ 1 ATOM 1350 N N . GLY A 1 171 B 10.391 56.037 4.544 1.00 27.62 ? 186 GLY A N 1 ATOM 1351 C CA . GLY A 1 171 B 9.476 55.863 3.421 1.00 25.87 ? 186 GLY A CA 1 ATOM 1352 C C . GLY A 1 171 B 10.281 55.702 2.131 1.00 26.99 ? 186 GLY A C 1 ATOM 1353 O O . GLY A 1 171 B 11.485 55.968 2.126 1.00 26.98 ? 186 GLY A O 1 ATOM 1354 N N . GLY A 1 172 ? 9.645 55.242 1.054 1.00 24.09 ? 187 GLY A N 1 ATOM 1355 C CA . GLY A 1 172 ? 10.345 55.121 -0.215 1.00 25.82 ? 187 GLY A CA 1 ATOM 1356 C C . GLY A 1 172 ? 10.736 53.731 -0.691 1.00 26.68 ? 187 GLY A C 1 ATOM 1357 O O . GLY A 1 172 ? 10.776 53.475 -1.891 1.00 27.91 ? 187 GLY A O 1 ATOM 1358 N N . ARG A 1 173 ? 10.999 52.825 0.240 1.00 24.98 ? 188 ARG A N 1 ATOM 1359 C CA . ARG A 1 173 ? 11.415 51.468 -0.118 1.00 25.02 ? 188 ARG A CA 1 ATOM 1360 C C . ARG A 1 173 ? 10.468 50.491 0.571 1.00 22.93 ? 188 ARG A C 1 ATOM 1361 O O . ARG A 1 173 ? 10.218 50.582 1.774 1.00 24.01 ? 188 ARG A O 1 ATOM 1362 C CB . ARG A 1 173 ? 12.873 51.249 0.308 1.00 26.15 ? 188 ARG A CB 1 ATOM 1363 C CG . ARG A 1 173 ? 13.905 52.097 -0.494 1.00 30.70 ? 188 ARG A CG 1 ATOM 1364 C CD . ARG A 1 173 ? 15.357 51.751 -0.098 1.00 36.31 ? 188 ARG A CD 1 ATOM 1365 N NE . ARG A 1 173 ? 15.851 52.639 0.953 1.00 43.48 ? 188 ARG A NE 1 ATOM 1366 C CZ . ARG A 1 173 ? 16.813 52.348 1.829 1.00 45.40 ? 188 ARG A CZ 1 ATOM 1367 N NH1 . ARG A 1 173 ? 17.422 51.166 1.811 1.00 44.38 ? 188 ARG A NH1 1 ATOM 1368 N NH2 . ARG A 1 173 ? 17.163 53.258 2.743 1.00 48.22 ? 188 ARG A NH2 1 ATOM 1369 N N . ASP A 1 174 ? 9.957 49.525 -0.177 1.00 22.84 ? 189 ASP A N 1 ATOM 1370 C CA . ASP A 1 174 ? 8.971 48.618 0.424 1.00 20.32 ? 189 ASP A CA 1 ATOM 1371 C C . ASP A 1 174 ? 8.656 47.553 -0.619 1.00 18.40 ? 189 ASP A C 1 ATOM 1372 O O . ASP A 1 174 ? 9.005 47.716 -1.792 1.00 18.74 ? 189 ASP A O 1 ATOM 1373 C CB . ASP A 1 174 ? 7.704 49.461 0.704 1.00 19.22 ? 189 ASP A CB 1 ATOM 1374 C CG . ASP A 1 174 ? 6.598 48.701 1.468 1.00 21.81 ? 189 ASP A CG 1 ATOM 1375 O OD1 . ASP A 1 174 ? 5.472 49.259 1.529 1.00 22.60 ? 189 ASP A OD1 1 ATOM 1376 O OD2 . ASP A 1 174 ? 6.850 47.591 2.014 1.00 20.49 ? 189 ASP A OD2 1 ATOM 1377 N N . THR A 1 175 ? 8.043 46.447 -0.212 1.00 17.82 ? 190 THR A N 1 ATOM 1378 C CA . THR A 1 175 ? 7.599 45.487 -1.217 1.00 15.67 ? 190 THR A CA 1 ATOM 1379 C C . THR A 1 175 ? 6.281 46.093 -1.716 1.00 16.94 ? 190 THR A C 1 ATOM 1380 O O . THR A 1 175 ? 5.821 47.136 -1.206 1.00 17.45 ? 190 THR A O 1 ATOM 1381 C CB . THR A 1 175 ? 7.295 44.105 -0.605 1.00 17.47 ? 190 THR A CB 1 ATOM 1382 O OG1 . THR A 1 175 ? 6.677 44.285 0.672 1.00 18.91 ? 190 THR A OG1 1 ATOM 1383 C CG2 . THR A 1 175 ? 8.586 43.281 -0.474 1.00 15.88 ? 190 THR A CG2 1 ATOM 1384 N N . CYS A 1 176 ? 5.652 45.458 -2.700 1.00 17.37 ? 191 CYS A N 1 ATOM 1385 C CA . CYS A 1 176 ? 4.398 46.008 -3.211 1.00 17.96 ? 191 CYS A CA 1 ATOM 1386 C C . CYS A 1 176 ? 3.563 44.921 -3.867 1.00 19.58 ? 191 CYS A C 1 ATOM 1387 O O . CYS A 1 176 ? 3.896 43.735 -3.761 1.00 18.77 ? 191 CYS A O 1 ATOM 1388 C CB . CYS A 1 176 ? 4.701 47.155 -4.190 1.00 20.03 ? 191 CYS A CB 1 ATOM 1389 S SG . CYS A 1 176 ? 3.400 48.436 -4.351 1.00 22.65 ? 191 CYS A SG 1 ATOM 1390 N N . HIS A 1 177 ? 2.479 45.312 -4.536 1.00 19.29 ? 192 HIS A N 1 ATOM 1391 C CA . HIS A 1 177 ? 1.581 44.351 -5.173 1.00 20.05 ? 192 HIS A CA 1 ATOM 1392 C C . HIS A 1 177 ? 2.314 43.375 -6.057 1.00 20.34 ? 192 HIS A C 1 ATOM 1393 O O . HIS A 1 177 ? 3.061 43.782 -6.959 1.00 19.49 ? 192 HIS A O 1 ATOM 1394 C CB . HIS A 1 177 ? 0.519 45.097 -6.009 1.00 21.05 ? 192 HIS A CB 1 ATOM 1395 C CG . HIS A 1 177 ? -0.096 46.240 -5.266 1.00 23.00 ? 192 HIS A CG 1 ATOM 1396 N ND1 . HIS A 1 177 ? -0.836 46.062 -4.115 1.00 22.94 ? 192 HIS A ND1 1 ATOM 1397 C CD2 . HIS A 1 177 ? -0.014 47.579 -5.462 1.00 20.51 ? 192 HIS A CD2 1 ATOM 1398 C CE1 . HIS A 1 177 ? -1.185 47.244 -3.633 1.00 20.43 ? 192 HIS A CE1 1 ATOM 1399 N NE2 . HIS A 1 177 ? -0.694 48.179 -4.433 1.00 20.16 ? 192 HIS A NE2 1 ATOM 1400 N N . GLY A 1 178 ? 2.071 42.087 -5.807 1.00 18.70 ? 193 GLY A N 1 ATOM 1401 C CA . GLY A 1 178 ? 2.699 41.031 -6.580 1.00 19.03 ? 193 GLY A CA 1 ATOM 1402 C C . GLY A 1 178 ? 3.993 40.498 -5.957 1.00 19.92 ? 193 GLY A C 1 ATOM 1403 O O . GLY A 1 178 ? 4.576 39.553 -6.471 1.00 19.50 ? 193 GLY A O 1 ATOM 1404 N N . ASP A 1 179 ? 4.466 41.124 -4.877 1.00 17.57 ? 194 ASP A N 1 ATOM 1405 C CA . ASP A 1 179 ? 5.692 40.657 -4.223 1.00 18.12 ? 194 ASP A CA 1 ATOM 1406 C C . ASP A 1 179 ? 5.433 39.589 -3.144 1.00 18.61 ? 194 ASP A C 1 ATOM 1407 O O . ASP A 1 179 ? 6.378 38.978 -2.625 1.00 17.38 ? 194 ASP A O 1 ATOM 1408 C CB . ASP A 1 179 ? 6.431 41.830 -3.568 1.00 18.07 ? 194 ASP A CB 1 ATOM 1409 C CG . ASP A 1 179 ? 7.205 42.686 -4.575 1.00 19.52 ? 194 ASP A CG 1 ATOM 1410 O OD1 . ASP A 1 179 ? 7.712 42.137 -5.582 1.00 19.46 ? 194 ASP A OD1 1 ATOM 1411 O OD2 . ASP A 1 179 ? 7.329 43.899 -4.323 1.00 18.86 ? 194 ASP A OD2 1 ATOM 1412 N N . SER A 1 180 ? 4.171 39.348 -2.803 1.00 18.61 ? 195 SER A N 1 ATOM 1413 C CA . SER A 1 180 ? 3.898 38.359 -1.743 1.00 18.12 ? 195 SER A CA 1 ATOM 1414 C C . SER A 1 180 ? 4.492 37.017 -2.067 1.00 17.04 ? 195 SER A C 1 ATOM 1415 O O . SER A 1 180 ? 4.612 36.646 -3.234 1.00 16.47 ? 195 SER A O 1 ATOM 1416 C CB . SER A 1 180 ? 2.390 38.192 -1.494 1.00 19.20 ? 195 SER A CB 1 ATOM 1417 O OG . SER A 1 180 ? 1.916 39.294 -0.744 1.00 19.22 ? 195 SER A OG 1 ATOM 1418 N N . GLY A 1 181 ? 4.867 36.293 -1.017 1.00 17.35 ? 196 GLY A N 1 ATOM 1419 C CA . GLY A 1 181 ? 5.430 34.974 -1.198 1.00 16.84 ? 196 GLY A CA 1 ATOM 1420 C C . GLY A 1 181 ? 6.928 34.983 -1.343 1.00 17.20 ? 196 GLY A C 1 ATOM 1421 O O . GLY A 1 181 ? 7.570 33.981 -1.061 1.00 17.79 ? 196 GLY A O 1 ATOM 1422 N N . GLY A 1 182 ? 7.485 36.114 -1.780 1.00 18.81 ? 197 GLY A N 1 ATOM 1423 C CA . GLY A 1 182 ? 8.929 36.203 -1.965 1.00 19.61 ? 197 GLY A CA 1 ATOM 1424 C C . GLY A 1 182 ? 9.689 36.208 -0.651 1.00 19.06 ? 197 GLY A C 1 ATOM 1425 O O . GLY A 1 182 ? 9.097 36.386 0.420 1.00 17.53 ? 197 GLY A O 1 ATOM 1426 N N . PRO A 1 183 ? 11.011 36.041 -0.707 1.00 19.44 ? 198 PRO A N 1 ATOM 1427 C CA . PRO A 1 183 ? 11.810 36.021 0.520 1.00 19.92 ? 198 PRO A CA 1 ATOM 1428 C C . PRO A 1 183 ? 12.359 37.340 1.005 1.00 18.39 ? 198 PRO A C 1 ATOM 1429 O O . PRO A 1 183 ? 12.721 38.221 0.212 1.00 21.52 ? 198 PRO A O 1 ATOM 1430 C CB . PRO A 1 183 ? 12.952 35.050 0.167 1.00 19.40 ? 198 PRO A CB 1 ATOM 1431 C CG . PRO A 1 183 ? 13.209 35.392 -1.312 1.00 19.77 ? 198 PRO A CG 1 ATOM 1432 C CD . PRO A 1 183 ? 11.779 35.526 -1.863 1.00 19.12 ? 198 PRO A CD 1 ATOM 1433 N N . LEU A 1 184 ? 12.401 37.471 2.329 1.00 21.44 ? 199 LEU A N 1 ATOM 1434 C CA . LEU A 1 184 ? 13.023 38.611 2.998 1.00 19.68 ? 199 LEU A CA 1 ATOM 1435 C C . LEU A 1 184 ? 14.356 37.945 3.369 1.00 20.68 ? 199 LEU A C 1 ATOM 1436 O O . LEU A 1 184 ? 14.378 37.055 4.224 1.00 21.37 ? 199 LEU A O 1 ATOM 1437 C CB . LEU A 1 184 ? 12.276 38.983 4.283 1.00 19.62 ? 199 LEU A CB 1 ATOM 1438 C CG . LEU A 1 184 ? 13.009 40.003 5.156 1.00 20.10 ? 199 LEU A CG 1 ATOM 1439 C CD1 . LEU A 1 184 ? 13.048 41.376 4.465 1.00 19.37 ? 199 LEU A CD1 1 ATOM 1440 C CD2 . LEU A 1 184 ? 12.276 40.089 6.528 1.00 22.32 ? 199 LEU A CD2 1 ATOM 1441 N N . ILE A 1 185 ? 15.443 38.356 2.721 1.00 22.17 ? 200 ILE A N 1 ATOM 1442 C CA . ILE A 1 185 ? 16.772 37.759 2.947 1.00 24.11 ? 200 ILE A CA 1 ATOM 1443 C C . ILE A 1 185 ? 17.597 38.581 3.936 1.00 26.33 ? 200 ILE A C 1 ATOM 1444 O O . ILE A 1 185 ? 17.844 39.764 3.705 1.00 27.14 ? 200 ILE A O 1 ATOM 1445 C CB . ILE A 1 185 ? 17.574 37.663 1.607 1.00 25.85 ? 200 ILE A CB 1 ATOM 1446 C CG1 . ILE A 1 185 ? 16.788 36.841 0.581 1.00 23.14 ? 200 ILE A CG1 1 ATOM 1447 C CG2 . ILE A 1 185 ? 18.966 37.011 1.840 1.00 23.28 ? 200 ILE A CG2 1 ATOM 1448 C CD1 . ILE A 1 185 ? 16.640 35.370 0.953 1.00 24.66 ? 200 ILE A CD1 1 ATOM 1449 N N . CYS A 1 186 ? 18.019 37.966 5.040 1.00 26.77 ? 201 CYS A N 1 ATOM 1450 C CA . CYS A 1 186 ? 18.843 38.688 6.020 1.00 27.73 ? 201 CYS A CA 1 ATOM 1451 C C . CYS A 1 186 ? 20.050 37.792 6.288 1.00 29.43 ? 201 CYS A C 1 ATOM 1452 O O . CYS A 1 186 ? 19.897 36.647 6.698 1.00 28.00 ? 201 CYS A O 1 ATOM 1453 C CB . CYS A 1 186 ? 18.094 38.918 7.344 1.00 28.34 ? 201 CYS A CB 1 ATOM 1454 S SG . CYS A 1 186 ? 16.359 39.482 7.235 1.00 29.02 ? 201 CYS A SG 1 ATOM 1455 N N . ASN A 1 187 ? 21.237 38.317 6.021 1.00 32.86 ? 202 ASN A N 1 ATOM 1456 C CA . ASN A 1 187 ? 22.466 37.556 6.215 1.00 35.97 ? 202 ASN A CA 1 ATOM 1457 C C . ASN A 1 187 ? 22.455 36.251 5.426 1.00 35.38 ? 202 ASN A C 1 ATOM 1458 O O . ASN A 1 187 ? 22.760 35.178 5.951 1.00 36.04 ? 202 ASN A O 1 ATOM 1459 C CB . ASN A 1 187 ? 22.665 37.300 7.704 1.00 39.48 ? 202 ASN A CB 1 ATOM 1460 C CG . ASN A 1 187 ? 22.730 38.596 8.493 1.00 45.86 ? 202 ASN A CG 1 ATOM 1461 O OD1 . ASN A 1 187 ? 21.748 39.006 9.125 1.00 48.63 ? 202 ASN A OD1 1 ATOM 1462 N ND2 . ASN A 1 187 ? 23.884 39.272 8.434 1.00 48.28 ? 202 ASN A ND2 1 ATOM 1463 N N . GLY A 1 188 ? 22.093 36.354 4.152 1.00 33.92 ? 207 GLY A N 1 ATOM 1464 C CA . GLY A 1 188 ? 22.059 35.181 3.300 1.00 32.92 ? 207 GLY A CA 1 ATOM 1465 C C . GLY A 1 188 ? 20.999 34.139 3.621 1.00 32.02 ? 207 GLY A C 1 ATOM 1466 O O . GLY A 1 188 ? 20.972 33.103 2.970 1.00 35.75 ? 207 GLY A O 1 ATOM 1467 N N . GLU A 1 189 ? 20.115 34.398 4.586 1.00 30.32 ? 208 GLU A N 1 ATOM 1468 C CA . GLU A 1 189 ? 19.076 33.428 4.943 1.00 29.71 ? 208 GLU A CA 1 ATOM 1469 C C . GLU A 1 189 ? 17.661 34.002 4.742 1.00 27.77 ? 208 GLU A C 1 ATOM 1470 O O . GLU A 1 189 ? 17.469 35.212 4.763 1.00 27.98 ? 208 GLU A O 1 ATOM 1471 C CB . GLU A 1 189 ? 19.238 32.997 6.394 1.00 31.63 ? 208 GLU A CB 1 ATOM 1472 C CG . GLU A 1 189 ? 20.602 32.377 6.726 1.00 35.58 ? 208 GLU A CG 1 ATOM 1473 C CD . GLU A 1 189 ? 20.801 32.181 8.234 1.00 38.64 ? 208 GLU A CD 1 ATOM 1474 O OE1 . GLU A 1 189 ? 21.789 31.525 8.623 1.00 39.93 ? 208 GLU A OE1 1 ATOM 1475 O OE2 . GLU A 1 189 ? 19.977 32.683 9.030 1.00 40.39 ? 208 GLU A OE2 1 ATOM 1476 N N . MET A 1 190 ? 16.684 33.126 4.558 1.00 26.15 ? 209 MET A N 1 ATOM 1477 C CA . MET A 1 190 ? 15.313 33.561 4.328 1.00 25.39 ? 209 MET A CA 1 ATOM 1478 C C . MET A 1 190 ? 14.593 33.672 5.660 1.00 25.45 ? 209 MET A C 1 ATOM 1479 O O . MET A 1 190 ? 14.075 32.694 6.185 1.00 27.53 ? 209 MET A O 1 ATOM 1480 C CB . MET A 1 190 ? 14.603 32.565 3.397 1.00 24.57 ? 209 MET A CB 1 ATOM 1481 C CG . MET A 1 190 ? 13.145 32.882 3.110 1.00 22.36 ? 209 MET A CG 1 ATOM 1482 S SD . MET A 1 190 ? 12.430 31.755 1.862 1.00 22.62 ? 209 MET A SD 1 ATOM 1483 C CE . MET A 1 190 ? 10.722 32.323 1.926 1.00 25.97 ? 209 MET A CE 1 ATOM 1484 N N . HIS A 1 191 ? 14.559 34.882 6.193 1.00 23.89 ? 210 HIS A N 1 ATOM 1485 C CA . HIS A 1 191 ? 13.912 35.135 7.465 1.00 25.00 ? 210 HIS A CA 1 ATOM 1486 C C . HIS A 1 191 ? 12.446 35.484 7.344 1.00 25.23 ? 210 HIS A C 1 ATOM 1487 O O . HIS A 1 191 ? 11.703 35.394 8.318 1.00 23.89 ? 210 HIS A O 1 ATOM 1488 C CB . HIS A 1 191 ? 14.649 36.261 8.189 1.00 25.99 ? 210 HIS A CB 1 ATOM 1489 C CG . HIS A 1 191 ? 15.930 35.813 8.810 1.00 28.22 ? 210 HIS A CG 1 ATOM 1490 N ND1 . HIS A 1 191 ? 16.022 35.465 10.142 1.00 29.69 ? 210 HIS A ND1 1 ATOM 1491 C CD2 . HIS A 1 191 ? 17.136 35.533 8.261 1.00 31.10 ? 210 HIS A CD2 1 ATOM 1492 C CE1 . HIS A 1 191 ? 17.229 34.983 10.383 1.00 31.76 ? 210 HIS A CE1 1 ATOM 1493 N NE2 . HIS A 1 191 ? 17.924 35.013 9.259 1.00 30.18 ? 210 HIS A NE2 1 ATOM 1494 N N . GLY A 1 192 ? 12.022 35.897 6.151 1.00 24.43 ? 211 GLY A N 1 ATOM 1495 C CA . GLY A 1 192 ? 10.628 36.257 6.006 1.00 22.45 ? 211 GLY A CA 1 ATOM 1496 C C . GLY A 1 192 ? 9.995 35.886 4.680 1.00 21.59 ? 211 GLY A C 1 ATOM 1497 O O . GLY A 1 192 ? 10.685 35.606 3.693 1.00 20.96 ? 211 GLY A O 1 ATOM 1498 N N . ILE A 1 193 ? 8.667 35.856 4.688 1.00 21.15 ? 212 ILE A N 1 ATOM 1499 C CA . ILE A 1 193 ? 7.874 35.609 3.488 1.00 19.49 ? 212 ILE A CA 1 ATOM 1500 C C . ILE A 1 193 ? 7.004 36.857 3.362 1.00 20.50 ? 212 ILE A C 1 ATOM 1501 O O . ILE A 1 193 ? 6.256 37.200 4.294 1.00 21.00 ? 212 ILE A O 1 ATOM 1502 C CB . ILE A 1 193 ? 6.964 34.364 3.639 1.00 20.59 ? 212 ILE A CB 1 ATOM 1503 C CG1 . ILE A 1 193 ? 7.820 33.108 3.818 1.00 20.40 ? 212 ILE A CG1 1 ATOM 1504 C CG2 . ILE A 1 193 ? 6.066 34.212 2.399 1.00 19.17 ? 212 ILE A CG2 1 ATOM 1505 C CD1 . ILE A 1 193 ? 6.965 31.858 4.237 1.00 21.30 ? 212 ILE A CD1 1 ATOM 1506 N N . VAL A 1 194 ? 7.091 37.555 2.234 1.00 18.25 ? 213 VAL A N 1 ATOM 1507 C CA . VAL A 1 194 ? 6.282 38.766 2.063 1.00 18.08 ? 213 VAL A CA 1 ATOM 1508 C C . VAL A 1 194 ? 4.792 38.472 2.221 1.00 18.67 ? 213 VAL A C 1 ATOM 1509 O O . VAL A 1 194 ? 4.242 37.659 1.486 1.00 17.08 ? 213 VAL A O 1 ATOM 1510 C CB . VAL A 1 194 ? 6.489 39.399 0.640 1.00 19.81 ? 213 VAL A CB 1 ATOM 1511 C CG1 . VAL A 1 194 ? 5.705 40.691 0.549 1.00 16.83 ? 213 VAL A CG1 1 ATOM 1512 C CG2 . VAL A 1 194 ? 7.977 39.663 0.373 1.00 16.96 ? 213 VAL A CG2 1 ATOM 1513 N N . ALA A 1 195 ? 4.132 39.164 3.150 1.00 18.05 ? 214 ALA A N 1 ATOM 1514 C CA . ALA A 1 195 ? 2.713 38.928 3.384 1.00 19.61 ? 214 ALA A CA 1 ATOM 1515 C C . ALA A 1 195 ? 1.882 40.100 2.862 1.00 19.50 ? 214 ALA A C 1 ATOM 1516 O O . ALA A 1 195 ? 1.148 39.968 1.885 1.00 21.30 ? 214 ALA A O 1 ATOM 1517 C CB . ALA A 1 195 ? 2.448 38.721 4.891 1.00 19.83 ? 214 ALA A CB 1 ATOM 1518 N N . GLY A 1 196 ? 1.999 41.254 3.511 1.00 19.17 ? 215 GLY A N 1 ATOM 1519 C CA . GLY A 1 196 ? 1.230 42.395 3.069 1.00 18.64 ? 215 GLY A CA 1 ATOM 1520 C C . GLY A 1 196 ? 1.741 43.697 3.654 1.00 19.20 ? 215 GLY A C 1 ATOM 1521 O O . GLY A 1 196 ? 2.692 43.714 4.468 1.00 19.48 ? 215 GLY A O 1 ATOM 1522 N N . GLY A 1 197 ? 1.099 44.786 3.251 1.00 21.02 ? 216 GLY A N 1 ATOM 1523 C CA . GLY A 1 197 ? 1.504 46.084 3.753 1.00 21.83 ? 216 GLY A CA 1 ATOM 1524 C C . GLY A 1 197 ? 0.478 47.164 3.493 1.00 21.70 ? 216 GLY A C 1 ATOM 1525 O O . GLY A 1 197 ? -0.688 46.887 3.189 1.00 20.86 ? 216 GLY A O 1 ATOM 1526 N N . SER A 1 198 ? 0.921 48.411 3.595 1.00 21.57 ? 217 SER A N 1 ATOM 1527 C CA . SER A 1 198 ? 0.015 49.521 3.416 1.00 21.88 ? 217 SER A CA 1 ATOM 1528 C C . SER A 1 198 ? -0.166 49.929 1.944 1.00 21.83 ? 217 SER A C 1 ATOM 1529 O O . SER A 1 198 ? 0.591 49.520 1.059 1.00 21.86 ? 217 SER A O 1 ATOM 1530 C CB . SER A 1 198 ? 0.476 50.692 4.289 1.00 22.05 ? 217 SER A CB 1 ATOM 1531 O OG . SER A 1 198 ? 0.374 50.338 5.677 1.00 24.95 ? 217 SER A OG 1 ATOM 1532 N N . GLU A 1 199 ? -1.158 50.783 1.719 1.00 21.82 ? 218 GLU A N 1 ATOM 1533 C CA . GLU A 1 199 ? -1.559 51.195 0.381 1.00 22.62 ? 218 GLU A CA 1 ATOM 1534 C C . GLU A 1 199 ? -1.699 52.716 0.383 1.00 23.91 ? 218 GLU A C 1 ATOM 1535 O O . GLU A 1 199 ? -2.559 53.255 1.085 1.00 25.34 ? 218 GLU A O 1 ATOM 1536 C CB . GLU A 1 199 ? -2.914 50.513 0.091 1.00 23.12 ? 218 GLU A CB 1 ATOM 1537 C CG . GLU A 1 199 ? -3.566 50.834 -1.233 1.00 23.58 ? 218 GLU A CG 1 ATOM 1538 C CD . GLU A 1 199 ? -2.878 50.178 -2.408 1.00 22.60 ? 218 GLU A CD 1 ATOM 1539 O OE1 . GLU A 1 199 ? -3.516 49.305 -3.062 1.00 22.01 ? 218 GLU A OE1 1 ATOM 1540 O OE2 . GLU A 1 199 ? -1.706 50.534 -2.680 1.00 23.38 ? 218 GLU A OE2 1 ATOM 1541 N N . PRO A 1 200 ? -0.896 53.420 -0.431 1.00 23.47 ? 219 PRO A N 1 ATOM 1542 C CA . PRO A 1 200 ? 0.121 52.892 -1.353 1.00 21.48 ? 219 PRO A CA 1 ATOM 1543 C C . PRO A 1 200 ? 1.347 52.333 -0.649 1.00 22.67 ? 219 PRO A C 1 ATOM 1544 O O . PRO A 1 200 ? 1.549 52.577 0.528 1.00 21.30 ? 219 PRO A O 1 ATOM 1545 C CB . PRO A 1 200 ? 0.466 54.106 -2.218 1.00 21.98 ? 219 PRO A CB 1 ATOM 1546 C CG . PRO A 1 200 ? 0.294 55.237 -1.295 1.00 22.26 ? 219 PRO A CG 1 ATOM 1547 C CD . PRO A 1 200 ? -0.991 54.888 -0.550 1.00 23.56 ? 219 PRO A CD 1 ATOM 1548 N N . CYS A 1 201 ? 2.161 51.583 -1.383 1.00 21.75 ? 220 CYS A N 1 ATOM 1549 C CA . CYS A 1 201 ? 3.359 51.009 -0.817 1.00 20.44 ? 220 CYS A CA 1 ATOM 1550 C C . CYS A 1 201 ? 4.381 52.112 -0.592 1.00 20.60 ? 220 CYS A C 1 ATOM 1551 O O . CYS A 1 201 ? 4.297 53.175 -1.212 1.00 21.83 ? 220 CYS A O 1 ATOM 1552 C CB . CYS A 1 201 ? 3.949 50.006 -1.800 1.00 20.62 ? 220 CYS A CB 1 ATOM 1553 S SG . CYS A 1 201 ? 2.727 48.806 -2.456 1.00 22.73 ? 220 CYS A SG 1 ATOM 1554 N N . GLY A 1 202 ? 5.346 51.854 0.286 1.00 20.27 ? 221 GLY A N 1 ATOM 1555 C CA . GLY A 1 202 ? 6.420 52.810 0.515 1.00 21.44 ? 221 GLY A CA 1 ATOM 1556 C C . GLY A 1 202 ? 6.163 54.097 1.295 1.00 22.80 ? 221 GLY A C 1 ATOM 1557 O O . GLY A 1 202 ? 6.994 55.019 1.235 1.00 24.21 ? 221 GLY A O 1 ATOM 1558 N N . GLN A 1 203 A 5.046 54.188 2.004 1.00 22.66 ? 221 GLN A N 1 ATOM 1559 C CA . GLN A 1 203 A 4.764 55.387 2.811 1.00 23.42 ? 221 GLN A CA 1 ATOM 1560 C C . GLN A 1 203 A 5.638 55.532 4.056 1.00 24.72 ? 221 GLN A C 1 ATOM 1561 O O . GLN A 1 203 A 6.139 54.557 4.624 1.00 22.79 ? 221 GLN A O 1 ATOM 1562 C CB . GLN A 1 203 A 3.313 55.391 3.290 1.00 24.43 ? 221 GLN A CB 1 ATOM 1563 C CG . GLN A 1 203 A 2.269 55.402 2.202 1.00 26.22 ? 221 GLN A CG 1 ATOM 1564 C CD . GLN A 1 203 A 0.878 55.243 2.790 1.00 29.18 ? 221 GLN A CD 1 ATOM 1565 O OE1 . GLN A 1 203 A 0.384 56.136 3.483 1.00 29.87 ? 221 GLN A OE1 1 ATOM 1566 N NE2 . GLN A 1 203 A 0.252 54.093 2.548 1.00 26.18 ? 221 GLN A NE2 1 ATOM 1567 N N . HIS A 1 204 ? 5.813 56.782 4.473 1.00 24.00 ? 222 HIS A N 1 ATOM 1568 C CA . HIS A 1 204 ? 6.567 57.102 5.682 1.00 23.87 ? 222 HIS A CA 1 ATOM 1569 C C . HIS A 1 204 ? 5.889 56.416 6.884 1.00 22.23 ? 222 HIS A C 1 ATOM 1570 O O . HIS A 1 204 ? 4.657 56.426 7.007 1.00 23.28 ? 222 HIS A O 1 ATOM 1571 C CB . HIS A 1 204 ? 6.565 58.631 5.845 1.00 22.64 ? 222 HIS A CB 1 ATOM 1572 C CG . HIS A 1 204 ? 7.188 59.116 7.122 1.00 23.67 ? 222 HIS A CG 1 ATOM 1573 N ND1 . HIS A 1 204 ? 8.399 58.647 7.586 1.00 22.04 ? 222 HIS A ND1 1 ATOM 1574 C CD2 . HIS A 1 204 ? 6.797 60.084 7.994 1.00 22.81 ? 222 HIS A CD2 1 ATOM 1575 C CE1 . HIS A 1 204 ? 8.729 59.299 8.689 1.00 23.03 ? 222 HIS A CE1 1 ATOM 1576 N NE2 . HIS A 1 204 ? 7.775 60.176 8.956 1.00 22.34 ? 222 HIS A NE2 1 ATOM 1577 N N . LEU A 1 205 ? 6.689 55.791 7.744 1.00 22.72 ? 223 LEU A N 1 ATOM 1578 C CA . LEU A 1 205 ? 6.202 55.101 8.943 1.00 23.46 ? 223 LEU A CA 1 ATOM 1579 C C . LEU A 1 205 ? 5.256 53.947 8.673 1.00 23.80 ? 223 LEU A C 1 ATOM 1580 O O . LEU A 1 205 ? 4.447 53.601 9.538 1.00 23.34 ? 223 LEU A O 1 ATOM 1581 C CB . LEU A 1 205 ? 5.483 56.075 9.905 1.00 25.27 ? 223 LEU A CB 1 ATOM 1582 C CG . LEU A 1 205 ? 6.310 57.289 10.336 1.00 25.41 ? 223 LEU A CG 1 ATOM 1583 C CD1 . LEU A 1 205 ? 5.491 58.099 11.384 1.00 26.93 ? 223 LEU A CD1 1 ATOM 1584 C CD2 . LEU A 1 205 ? 7.660 56.828 10.908 1.00 23.24 ? 223 LEU A CD2 1 ATOM 1585 N N . LYS A 1 206 ? 5.323 53.345 7.491 1.00 22.44 ? 224 LYS A N 1 ATOM 1586 C CA . LYS A 1 206 ? 4.424 52.226 7.259 1.00 22.96 ? 224 LYS A CA 1 ATOM 1587 C C . LYS A 1 206 ? 5.186 51.000 6.765 1.00 23.22 ? 224 LYS A C 1 ATOM 1588 O O . LYS A 1 206 ? 5.147 50.657 5.580 1.00 24.76 ? 224 LYS A O 1 ATOM 1589 C CB . LYS A 1 206 ? 3.287 52.628 6.296 1.00 25.12 ? 224 LYS A CB 1 ATOM 1590 C CG . LYS A 1 206 ? 2.355 53.676 6.927 1.00 27.16 ? 224 LYS A CG 1 ATOM 1591 C CD . LYS A 1 206 ? 1.048 53.919 6.187 1.00 31.21 ? 224 LYS A CD 1 ATOM 1592 C CE . LYS A 1 206 ? 0.244 55.008 6.916 1.00 33.34 ? 224 LYS A CE 1 ATOM 1593 N NZ . LYS A 1 206 ? -1.125 55.093 6.366 1.00 36.93 ? 224 LYS A NZ 1 ATOM 1594 N N . PRO A 1 207 ? 5.935 50.362 7.673 1.00 23.47 ? 225 PRO A N 1 ATOM 1595 C CA . PRO A 1 207 ? 6.694 49.163 7.318 1.00 23.36 ? 225 PRO A CA 1 ATOM 1596 C C . PRO A 1 207 ? 5.650 48.089 6.971 1.00 22.37 ? 225 PRO A C 1 ATOM 1597 O O . PRO A 1 207 ? 4.453 48.270 7.224 1.00 22.12 ? 225 PRO A O 1 ATOM 1598 C CB . PRO A 1 207 ? 7.489 48.859 8.598 1.00 23.54 ? 225 PRO A CB 1 ATOM 1599 C CG . PRO A 1 207 ? 6.576 49.394 9.694 1.00 23.80 ? 225 PRO A CG 1 ATOM 1600 C CD . PRO A 1 207 ? 6.161 50.724 9.088 1.00 24.28 ? 225 PRO A CD 1 ATOM 1601 N N . ALA A 1 208 ? 6.113 46.981 6.405 1.00 22.81 ? 226 ALA A N 1 ATOM 1602 C CA . ALA A 1 208 ? 5.230 45.905 5.965 1.00 21.37 ? 226 ALA A CA 1 ATOM 1603 C C . ALA A 1 208 ? 5.416 44.662 6.825 1.00 21.33 ? 226 ALA A C 1 ATOM 1604 O O . ALA A 1 208 ? 6.331 44.595 7.651 1.00 21.22 ? 226 ALA A O 1 ATOM 1605 C CB . ALA A 1 208 ? 5.523 45.580 4.484 1.00 21.57 ? 226 ALA A CB 1 ATOM 1606 N N . VAL A 1 209 ? 4.549 43.682 6.595 1.00 20.05 ? 227 VAL A N 1 ATOM 1607 C CA . VAL A 1 209 ? 4.541 42.435 7.338 1.00 20.20 ? 227 VAL A CA 1 ATOM 1608 C C . VAL A 1 209 ? 5.096 41.245 6.539 1.00 19.77 ? 227 VAL A C 1 ATOM 1609 O O . VAL A 1 209 ? 4.687 40.993 5.390 1.00 20.31 ? 227 VAL A O 1 ATOM 1610 C CB . VAL A 1 209 ? 3.111 42.109 7.767 1.00 20.04 ? 227 VAL A CB 1 ATOM 1611 C CG1 . VAL A 1 209 ? 3.082 40.834 8.594 1.00 21.41 ? 227 VAL A CG1 1 ATOM 1612 C CG2 . VAL A 1 209 ? 2.554 43.280 8.593 1.00 24.43 ? 227 VAL A CG2 1 ATOM 1613 N N . TYR A 1 210 ? 6.005 40.518 7.171 1.00 19.71 ? 228 TYR A N 1 ATOM 1614 C CA . TYR A 1 210 ? 6.649 39.346 6.580 1.00 20.45 ? 228 TYR A CA 1 ATOM 1615 C C . TYR A 1 210 ? 6.479 38.179 7.542 1.00 23.48 ? 228 TYR A C 1 ATOM 1616 O O . TYR A 1 210 ? 6.750 38.322 8.728 1.00 23.94 ? 228 TYR A O 1 ATOM 1617 C CB . TYR A 1 210 ? 8.128 39.608 6.374 1.00 19.97 ? 228 TYR A CB 1 ATOM 1618 C CG . TYR A 1 210 ? 8.398 40.820 5.504 1.00 21.27 ? 228 TYR A CG 1 ATOM 1619 C CD1 . TYR A 1 210 ? 8.242 42.117 6.003 1.00 19.48 ? 228 TYR A CD1 1 ATOM 1620 C CD2 . TYR A 1 210 ? 8.721 40.656 4.157 1.00 20.80 ? 228 TYR A CD2 1 ATOM 1621 C CE1 . TYR A 1 210 ? 8.390 43.242 5.166 1.00 19.81 ? 228 TYR A CE1 1 ATOM 1622 C CE2 . TYR A 1 210 ? 8.871 41.742 3.320 1.00 20.30 ? 228 TYR A CE2 1 ATOM 1623 C CZ . TYR A 1 210 ? 8.700 43.028 3.815 1.00 18.78 ? 228 TYR A CZ 1 ATOM 1624 O OH . TYR A 1 210 ? 8.784 44.077 2.939 1.00 17.42 ? 228 TYR A OH 1 ATOM 1625 N N . THR A 1 211 ? 6.012 37.041 7.042 1.00 22.73 ? 229 THR A N 1 ATOM 1626 C CA . THR A 1 211 ? 5.839 35.868 7.924 1.00 24.72 ? 229 THR A CA 1 ATOM 1627 C C . THR A 1 211 ? 7.232 35.512 8.468 1.00 26.62 ? 229 THR A C 1 ATOM 1628 O O . THR A 1 211 ? 8.206 35.465 7.722 1.00 25.07 ? 229 THR A O 1 ATOM 1629 C CB . THR A 1 211 ? 5.206 34.720 7.133 1.00 24.10 ? 229 THR A CB 1 ATOM 1630 O OG1 . THR A 1 211 ? 3.939 35.161 6.622 1.00 24.35 ? 229 THR A OG1 1 ATOM 1631 C CG2 . THR A 1 211 ? 4.982 33.485 8.030 1.00 25.78 ? 229 THR A CG2 1 ATOM 1632 N N . LYS A 1 212 ? 7.341 35.304 9.780 1.00 27.26 ? 230 LYS A N 1 ATOM 1633 C CA . LYS A 1 212 ? 8.643 35.023 10.381 1.00 28.18 ? 230 LYS A CA 1 ATOM 1634 C C . LYS A 1 212 ? 9.007 33.559 10.204 1.00 27.85 ? 230 LYS A C 1 ATOM 1635 O O . LYS A 1 212 ? 8.565 32.704 10.960 1.00 31.10 ? 230 LYS A O 1 ATOM 1636 C CB . LYS A 1 212 ? 8.627 35.401 11.863 1.00 28.37 ? 230 LYS A CB 1 ATOM 1637 C CG . LYS A 1 212 ? 9.998 35.274 12.504 1.00 32.29 ? 230 LYS A CG 1 ATOM 1638 C CD . LYS A 1 212 ? 10.017 35.758 13.932 1.00 37.05 ? 230 LYS A CD 1 ATOM 1639 C CE . LYS A 1 212 ? 11.440 35.659 14.493 1.00 40.55 ? 230 LYS A CE 1 ATOM 1640 N NZ . LYS A 1 212 ? 11.503 36.181 15.891 1.00 40.30 ? 230 LYS A NZ 1 ATOM 1641 N N . VAL A 1 213 ? 9.829 33.280 9.206 1.00 26.16 ? 231 VAL A N 1 ATOM 1642 C CA . VAL A 1 213 ? 10.197 31.919 8.874 1.00 25.48 ? 231 VAL A CA 1 ATOM 1643 C C . VAL A 1 213 ? 10.812 31.053 9.986 1.00 29.46 ? 231 VAL A C 1 ATOM 1644 O O . VAL A 1 213 ? 10.440 29.885 10.123 1.00 30.14 ? 231 VAL A O 1 ATOM 1645 C CB . VAL A 1 213 ? 11.125 31.905 7.641 1.00 26.20 ? 231 VAL A CB 1 ATOM 1646 C CG1 . VAL A 1 213 ? 11.533 30.458 7.289 1.00 22.88 ? 231 VAL A CG1 1 ATOM 1647 C CG2 . VAL A 1 213 ? 10.387 32.569 6.452 1.00 22.28 ? 231 VAL A CG2 1 ATOM 1648 N N . PHE A 1 214 ? 11.724 31.623 10.764 1.00 31.22 ? 232 PHE A N 1 ATOM 1649 C CA . PHE A 1 214 ? 12.402 30.885 11.835 1.00 34.58 ? 232 PHE A CA 1 ATOM 1650 C C . PHE A 1 214 ? 11.452 30.062 12.702 1.00 34.94 ? 232 PHE A C 1 ATOM 1651 O O . PHE A 1 214 ? 11.758 28.924 13.062 1.00 36.42 ? 232 PHE A O 1 ATOM 1652 C CB . PHE A 1 214 ? 13.192 31.848 12.720 1.00 35.97 ? 232 PHE A CB 1 ATOM 1653 C CG . PHE A 1 214 ? 13.952 31.161 13.833 1.00 38.81 ? 232 PHE A CG 1 ATOM 1654 C CD1 . PHE A 1 214 ? 15.109 30.434 13.560 1.00 39.25 ? 232 PHE A CD1 1 ATOM 1655 C CD2 . PHE A 1 214 ? 13.508 31.249 15.143 1.00 39.31 ? 232 PHE A CD2 1 ATOM 1656 C CE1 . PHE A 1 214 ? 15.817 29.805 14.582 1.00 40.43 ? 232 PHE A CE1 1 ATOM 1657 C CE2 . PHE A 1 214 ? 14.207 30.624 16.174 1.00 39.74 ? 232 PHE A CE2 1 ATOM 1658 C CZ . PHE A 1 214 ? 15.364 29.902 15.892 1.00 39.98 ? 232 PHE A CZ 1 ATOM 1659 N N . ASP A 1 215 ? 10.304 30.637 13.027 1.00 36.07 ? 233 ASP A N 1 ATOM 1660 C CA . ASP A 1 215 ? 9.316 29.958 13.851 1.00 37.52 ? 233 ASP A CA 1 ATOM 1661 C C . ASP A 1 215 ? 8.770 28.692 13.214 1.00 36.96 ? 233 ASP A C 1 ATOM 1662 O O . ASP A 1 215 ? 8.370 27.756 13.917 1.00 36.50 ? 233 ASP A O 1 ATOM 1663 C CB . ASP A 1 215 ? 8.131 30.881 14.137 1.00 40.48 ? 233 ASP A CB 1 ATOM 1664 C CG . ASP A 1 215 ? 8.467 31.995 15.101 1.00 43.01 ? 233 ASP A CG 1 ATOM 1665 O OD1 . ASP A 1 215 ? 9.653 32.179 15.458 1.00 45.22 ? 233 ASP A OD1 1 ATOM 1666 O OD2 . ASP A 1 215 ? 7.518 32.706 15.495 1.00 47.20 ? 233 ASP A OD2 1 ATOM 1667 N N . TYR A 1 216 ? 8.729 28.669 11.885 1.00 33.28 ? 234 TYR A N 1 ATOM 1668 C CA . TYR A 1 216 ? 8.178 27.526 11.174 1.00 33.26 ? 234 TYR A CA 1 ATOM 1669 C C . TYR A 1 216 ? 9.246 26.526 10.725 1.00 32.53 ? 234 TYR A C 1 ATOM 1670 O O . TYR A 1 216 ? 8.943 25.565 10.025 1.00 33.32 ? 234 TYR A O 1 ATOM 1671 C CB . TYR A 1 216 ? 7.366 27.995 9.950 1.00 30.97 ? 234 TYR A CB 1 ATOM 1672 C CG . TYR A 1 216 ? 6.168 28.880 10.262 1.00 30.39 ? 234 TYR A CG 1 ATOM 1673 C CD1 . TYR A 1 216 ? 6.332 30.230 10.580 1.00 27.40 ? 234 TYR A CD1 1 ATOM 1674 C CD2 . TYR A 1 216 ? 4.867 28.360 10.228 1.00 29.55 ? 234 TYR A CD2 1 ATOM 1675 C CE1 . TYR A 1 216 ? 5.221 31.042 10.855 1.00 27.94 ? 234 TYR A CE1 1 ATOM 1676 C CE2 . TYR A 1 216 ? 3.756 29.155 10.506 1.00 29.45 ? 234 TYR A CE2 1 ATOM 1677 C CZ . TYR A 1 216 ? 3.939 30.495 10.823 1.00 27.28 ? 234 TYR A CZ 1 ATOM 1678 O OH . TYR A 1 216 ? 2.843 31.252 11.177 1.00 27.30 ? 234 TYR A OH 1 ATOM 1679 N N . ASN A 1 217 ? 10.494 26.760 11.116 1.00 33.15 ? 235 ASN A N 1 ATOM 1680 C CA . ASN A 1 217 ? 11.582 25.856 10.734 1.00 33.79 ? 235 ASN A CA 1 ATOM 1681 C C . ASN A 1 217 ? 11.281 24.367 10.964 1.00 35.11 ? 235 ASN A C 1 ATOM 1682 O O . ASN A 1 217 ? 11.497 23.549 10.073 1.00 34.54 ? 235 ASN A O 1 ATOM 1683 C CB . ASN A 1 217 ? 12.878 26.262 11.457 1.00 33.47 ? 235 ASN A CB 1 ATOM 1684 C CG . ASN A 1 217 ? 13.696 27.264 10.659 1.00 36.21 ? 235 ASN A CG 1 ATOM 1685 O OD1 . ASN A 1 217 ? 13.225 27.794 9.649 1.00 34.61 ? 235 ASN A OD1 1 ATOM 1686 N ND2 . ASN A 1 217 ? 14.924 27.531 11.105 1.00 37.93 ? 235 ASN A ND2 1 ATOM 1687 N N . ASN A 1 218 ? 10.766 24.004 12.136 1.00 37.02 ? 236 ASN A N 1 ATOM 1688 C CA . ASN A 1 218 ? 10.477 22.585 12.387 1.00 38.41 ? 236 ASN A CA 1 ATOM 1689 C C . ASN A 1 218 ? 9.341 22.068 11.522 1.00 37.46 ? 236 ASN A C 1 ATOM 1690 O O . ASN A 1 218 ? 9.416 20.965 10.972 1.00 37.27 ? 236 ASN A O 1 ATOM 1691 C CB . ASN A 1 218 ? 10.174 22.350 13.869 1.00 41.18 ? 236 ASN A CB 1 ATOM 1692 C CG . ASN A 1 218 ? 11.347 22.731 14.758 1.00 44.69 ? 236 ASN A CG 1 ATOM 1693 O OD1 . ASN A 1 218 ? 12.498 22.731 14.315 1.00 45.15 ? 236 ASN A OD1 1 ATOM 1694 N ND2 . ASN A 1 218 ? 11.064 23.055 16.021 1.00 47.44 ? 236 ASN A ND2 1 ATOM 1695 N N . TRP A 1 219 ? 8.288 22.868 11.388 1.00 36.68 ? 237 TRP A N 1 ATOM 1696 C CA . TRP A 1 219 ? 7.150 22.472 10.566 1.00 35.89 ? 237 TRP A CA 1 ATOM 1697 C C . TRP A 1 219 ? 7.641 22.233 9.137 1.00 35.06 ? 237 TRP A C 1 ATOM 1698 O O . TRP A 1 219 ? 7.347 21.206 8.521 1.00 34.74 ? 237 TRP A O 1 ATOM 1699 C CB . TRP A 1 219 ? 6.080 23.578 10.556 1.00 35.09 ? 237 TRP A CB 1 ATOM 1700 C CG . TRP A 1 219 ? 4.908 23.281 9.659 1.00 32.77 ? 237 TRP A CG 1 ATOM 1701 C CD1 . TRP A 1 219 ? 3.911 22.376 9.884 1.00 33.84 ? 237 TRP A CD1 1 ATOM 1702 C CD2 . TRP A 1 219 ? 4.639 23.859 8.368 1.00 33.17 ? 237 TRP A CD2 1 ATOM 1703 N NE1 . TRP A 1 219 ? 3.040 22.350 8.815 1.00 34.92 ? 237 TRP A NE1 1 ATOM 1704 C CE2 . TRP A 1 219 ? 3.464 23.249 7.872 1.00 32.34 ? 237 TRP A CE2 1 ATOM 1705 C CE3 . TRP A 1 219 ? 5.280 24.833 7.583 1.00 32.78 ? 237 TRP A CE3 1 ATOM 1706 C CZ2 . TRP A 1 219 ? 2.913 23.577 6.622 1.00 33.21 ? 237 TRP A CZ2 1 ATOM 1707 C CZ3 . TRP A 1 219 ? 4.728 25.159 6.337 1.00 31.99 ? 237 TRP A CZ3 1 ATOM 1708 C CH2 . TRP A 1 219 ? 3.558 24.531 5.873 1.00 31.87 ? 237 TRP A CH2 1 ATOM 1709 N N . ILE A 1 220 ? 8.392 23.196 8.615 1.00 34.30 ? 238 ILE A N 1 ATOM 1710 C CA . ILE A 1 220 ? 8.889 23.088 7.253 1.00 32.99 ? 238 ILE A CA 1 ATOM 1711 C C . ILE A 1 220 ? 9.711 21.818 7.064 1.00 33.36 ? 238 ILE A C 1 ATOM 1712 O O . ILE A 1 220 ? 9.467 21.050 6.145 1.00 31.38 ? 238 ILE A O 1 ATOM 1713 C CB . ILE A 1 220 ? 9.760 24.305 6.874 1.00 33.14 ? 238 ILE A CB 1 ATOM 1714 C CG1 . ILE A 1 220 ? 8.909 25.589 6.901 1.00 30.74 ? 238 ILE A CG1 1 ATOM 1715 C CG2 . ILE A 1 220 ? 10.377 24.090 5.496 1.00 31.76 ? 238 ILE A CG2 1 ATOM 1716 C CD1 . ILE A 1 220 ? 9.717 26.854 6.762 1.00 27.43 ? 238 ILE A CD1 1 ATOM 1717 N N . GLN A 1 221 ? 10.681 21.599 7.943 1.00 35.69 ? 239 GLN A N 1 ATOM 1718 C CA . GLN A 1 221 ? 11.530 20.428 7.810 1.00 38.57 ? 239 GLN A CA 1 ATOM 1719 C C . GLN A 1 221 ? 10.770 19.117 7.975 1.00 38.26 ? 239 GLN A C 1 ATOM 1720 O O . GLN A 1 221 ? 11.092 18.133 7.312 1.00 39.21 ? 239 GLN A O 1 ATOM 1721 C CB . GLN A 1 221 ? 12.704 20.539 8.787 1.00 41.80 ? 239 GLN A CB 1 ATOM 1722 C CG . GLN A 1 221 ? 13.595 21.741 8.445 1.00 44.07 ? 239 GLN A CG 1 ATOM 1723 C CD . GLN A 1 221 ? 14.597 22.091 9.527 1.00 46.52 ? 239 GLN A CD 1 ATOM 1724 O OE1 . GLN A 1 221 ? 14.243 22.203 10.700 1.00 49.76 ? 239 GLN A OE1 1 ATOM 1725 N NE2 . GLN A 1 221 ? 15.857 22.289 9.135 1.00 47.54 ? 239 GLN A NE2 1 ATOM 1726 N N . SER A 1 222 ? 9.737 19.102 8.810 1.00 39.06 ? 240 SER A N 1 ATOM 1727 C CA . SER A 1 222 ? 8.969 17.866 8.998 1.00 39.92 ? 240 SER A CA 1 ATOM 1728 C C . SER A 1 222 ? 8.124 17.549 7.766 1.00 39.52 ? 240 SER A C 1 ATOM 1729 O O . SER A 1 222 ? 7.989 16.389 7.384 1.00 39.41 ? 240 SER A O 1 ATOM 1730 C CB . SER A 1 222 ? 8.061 17.965 10.227 1.00 41.64 ? 240 SER A CB 1 ATOM 1731 O OG . SER A 1 222 ? 6.965 18.833 9.973 1.00 47.94 ? 240 SER A OG 1 ATOM 1732 N N . ILE A 1 223 ? 7.542 18.573 7.141 1.00 37.58 ? 241 ILE A N 1 ATOM 1733 C CA . ILE A 1 223 ? 6.739 18.346 5.939 1.00 35.64 ? 241 ILE A CA 1 ATOM 1734 C C . ILE A 1 223 ? 7.640 17.788 4.850 1.00 35.01 ? 241 ILE A C 1 ATOM 1735 O O . ILE A 1 223 ? 7.300 16.825 4.161 1.00 35.14 ? 241 ILE A O 1 ATOM 1736 C CB . ILE A 1 223 ? 6.115 19.659 5.401 1.00 34.53 ? 241 ILE A CB 1 ATOM 1737 C CG1 . ILE A 1 223 ? 5.049 20.163 6.372 1.00 33.79 ? 241 ILE A CG1 1 ATOM 1738 C CG2 . ILE A 1 223 ? 5.519 19.423 4.020 1.00 33.26 ? 241 ILE A CG2 1 ATOM 1739 C CD1 . ILE A 1 223 ? 3.774 19.359 6.350 1.00 33.45 ? 241 ILE A CD1 1 ATOM 1740 N N . ILE A 1 224 ? 8.795 18.417 4.688 1.00 35.16 ? 242 ILE A N 1 ATOM 1741 C CA . ILE A 1 224 ? 9.732 17.964 3.686 1.00 35.98 ? 242 ILE A CA 1 ATOM 1742 C C . ILE A 1 224 ? 10.126 16.513 3.979 1.00 38.90 ? 242 ILE A C 1 ATOM 1743 O O . ILE A 1 224 ? 10.203 15.691 3.062 1.00 38.73 ? 242 ILE A O 1 ATOM 1744 C CB . ILE A 1 224 ? 10.979 18.828 3.677 1.00 34.85 ? 242 ILE A CB 1 ATOM 1745 C CG1 . ILE A 1 224 ? 10.593 20.252 3.261 1.00 33.87 ? 242 ILE A CG1 1 ATOM 1746 C CG2 . ILE A 1 224 ? 12.034 18.201 2.743 1.00 33.25 ? 242 ILE A CG2 1 ATOM 1747 C CD1 . ILE A 1 224 ? 11.746 21.204 3.165 1.00 32.86 ? 242 ILE A CD1 1 ATOM 1748 N N . ALA A 1 225 ? 10.362 16.219 5.257 1.00 40.80 ? 243 ALA A N 1 ATOM 1749 C CA . ALA A 1 225 ? 10.742 14.881 5.696 1.00 43.66 ? 243 ALA A CA 1 ATOM 1750 C C . ALA A 1 225 ? 9.677 13.854 5.315 1.00 45.51 ? 243 ALA A C 1 ATOM 1751 O O . ALA A 1 225 ? 9.980 12.679 5.147 1.00 47.34 ? 243 ALA A O 1 ATOM 1752 C CB . ALA A 1 225 ? 10.963 14.866 7.199 1.00 43.11 ? 243 ALA A CB 1 ATOM 1753 N N . GLY A 1 226 ? 8.432 14.296 5.184 1.00 45.71 ? 244 GLY A N 1 ATOM 1754 C CA . GLY A 1 226 ? 7.374 13.379 4.819 1.00 46.95 ? 244 GLY A CA 1 ATOM 1755 C C . GLY A 1 226 ? 6.275 13.306 5.855 1.00 47.88 ? 244 GLY A C 1 ATOM 1756 O O . GLY A 1 226 ? 5.262 12.645 5.650 1.00 49.45 ? 244 GLY A O 1 ATOM 1757 N N . ASN A 1 227 ? 6.471 13.975 6.980 1.00 48.97 ? 245 ASN A N 1 ATOM 1758 C CA . ASN A 1 227 ? 5.472 13.975 8.036 1.00 49.82 ? 245 ASN A CA 1 ATOM 1759 C C . ASN A 1 227 ? 4.229 14.705 7.533 1.00 50.30 ? 245 ASN A C 1 ATOM 1760 O O . ASN A 1 227 ? 4.338 15.724 6.843 1.00 50.23 ? 245 ASN A O 1 ATOM 1761 C CB . ASN A 1 227 ? 6.016 14.694 9.258 1.00 51.93 ? 245 ASN A CB 1 ATOM 1762 C CG . ASN A 1 227 ? 5.206 14.420 10.497 1.00 56.23 ? 245 ASN A CG 1 ATOM 1763 O OD1 . ASN A 1 227 ? 3.973 14.478 10.472 1.00 55.08 ? 245 ASN A OD1 1 ATOM 1764 N ND2 . ASN A 1 227 ? 5.902 14.127 11.590 1.00 59.17 ? 245 ASN A ND2 1 ATOM 1765 N N . ARG A 1 228 A 3.051 14.192 7.873 1.00 49.09 ? 245 ARG A N 1 ATOM 1766 C CA . ARG A 1 228 A 1.815 14.828 7.444 1.00 49.54 ? 245 ARG A CA 1 ATOM 1767 C C . ARG A 1 228 A 0.839 15.094 8.573 1.00 50.76 ? 245 ARG A C 1 ATOM 1768 O O . ARG A 1 228 A -0.342 15.326 8.322 1.00 52.25 ? 245 ARG A O 1 ATOM 1769 C CB . ARG A 1 228 A 1.119 13.990 6.370 1.00 47.37 ? 245 ARG A CB 1 ATOM 1770 C CG . ARG A 1 228 A 1.898 13.880 5.076 1.00 46.82 ? 245 ARG A CG 1 ATOM 1771 C CD . ARG A 1 228 A 2.116 15.249 4.437 1.00 44.39 ? 245 ARG A CD 1 ATOM 1772 N NE . ARG A 1 228 A 2.940 15.140 3.238 1.00 44.92 ? 245 ARG A NE 1 ATOM 1773 C CZ . ARG A 1 228 A 4.260 15.284 3.215 1.00 44.16 ? 245 ARG A CZ 1 ATOM 1774 N NH1 . ARG A 1 228 A 4.919 15.553 4.333 1.00 45.33 ? 245 ARG A NH1 1 ATOM 1775 N NH2 . ARG A 1 228 A 4.923 15.143 2.074 1.00 43.93 ? 245 ARG A NH2 1 ATOM 1776 N N . THR A 1 229 B 1.313 15.054 9.814 1.00 50.96 ? 245 THR A N 1 ATOM 1777 C CA . THR A 1 229 B 0.431 15.324 10.945 1.00 51.32 ? 245 THR A CA 1 ATOM 1778 C C . THR A 1 229 B 1.005 16.445 11.787 1.00 50.69 ? 245 THR A C 1 ATOM 1779 O O . THR A 1 229 B 0.319 17.018 12.629 1.00 50.70 ? 245 THR A O 1 ATOM 1780 C CB . THR A 1 229 B 0.211 14.065 11.833 1.00 51.01 ? 245 THR A CB 1 ATOM 1781 O OG1 . THR A 1 229 B 1.444 13.673 12.449 1.00 51.31 ? 245 THR A OG1 1 ATOM 1782 C CG2 . THR A 1 229 B -0.323 12.919 10.993 1.00 51.90 ? 245 THR A CG2 1 ATOM 1783 N N . VAL A 1 230 C 2.272 16.769 11.542 1.00 51.63 ? 245 VAL A N 1 ATOM 1784 C CA . VAL A 1 230 C 2.940 17.843 12.265 1.00 50.35 ? 245 VAL A CA 1 ATOM 1785 C C . VAL A 1 230 C 2.118 19.141 12.177 1.00 51.41 ? 245 VAL A C 1 ATOM 1786 O O . VAL A 1 230 C 1.370 19.342 11.220 1.00 51.65 ? 245 VAL A O 1 ATOM 1787 C CB . VAL A 1 230 C 4.346 18.068 11.692 1.00 50.10 ? 245 VAL A CB 1 ATOM 1788 C CG1 . VAL A 1 230 C 4.266 18.265 10.167 1.00 49.59 ? 245 VAL A CG1 1 ATOM 1789 C CG2 . VAL A 1 230 C 4.996 19.245 12.380 1.00 49.77 ? 245 VAL A CG2 1 ATOM 1790 N N . THR A 1 231 D 2.241 20.006 13.179 1.00 51.37 ? 245 THR A N 1 ATOM 1791 C CA . THR A 1 231 D 1.493 21.261 13.202 1.00 52.31 ? 245 THR A CA 1 ATOM 1792 C C . THR A 1 231 D 2.399 22.495 13.282 1.00 52.52 ? 245 THR A C 1 ATOM 1793 O O . THR A 1 231 D 3.530 22.427 13.769 1.00 52.73 ? 245 THR A O 1 ATOM 1794 C CB . THR A 1 231 D 0.514 21.316 14.404 1.00 52.72 ? 245 THR A CB 1 ATOM 1795 O OG1 . THR A 1 231 D 1.258 21.263 15.630 1.00 53.38 ? 245 THR A OG1 1 ATOM 1796 C CG2 . THR A 1 231 D -0.471 20.156 14.353 1.00 52.59 ? 245 THR A CG2 1 ATOM 1797 N N . CYS A 1 232 E 1.891 23.627 12.805 1.00 52.21 ? 245 CYS A N 1 ATOM 1798 C CA . CYS A 1 232 E 2.653 24.868 12.836 1.00 50.89 ? 245 CYS A CA 1 ATOM 1799 C C . CYS A 1 232 E 2.712 25.418 14.239 1.00 52.17 ? 245 CYS A C 1 ATOM 1800 O O . CYS A 1 232 E 1.908 25.050 15.093 1.00 52.91 ? 245 CYS A O 1 ATOM 1801 C CB . CYS A 1 232 E 2.009 25.914 11.931 1.00 47.35 ? 245 CYS A CB 1 ATOM 1802 S SG . CYS A 1 232 E 2.142 25.525 10.167 1.00 44.35 ? 245 CYS A SG 1 ATOM 1803 N N . PRO A 1 233 F 3.674 26.305 14.506 1.00 52.96 ? 245 PRO A N 1 ATOM 1804 C CA . PRO A 1 233 F 3.725 26.844 15.861 1.00 53.72 ? 245 PRO A CA 1 ATOM 1805 C C . PRO A 1 233 F 2.355 27.429 16.186 1.00 55.00 ? 245 PRO A C 1 ATOM 1806 O O . PRO A 1 233 F 1.688 27.985 15.310 1.00 54.70 ? 245 PRO A O 1 ATOM 1807 C CB . PRO A 1 233 F 4.818 27.904 15.769 1.00 53.82 ? 245 PRO A CB 1 ATOM 1808 C CG . PRO A 1 233 F 4.758 28.332 14.320 1.00 54.54 ? 245 PRO A CG 1 ATOM 1809 C CD . PRO A 1 233 F 4.602 27.017 13.612 1.00 53.76 ? 245 PRO A CD 1 ATOM 1810 N N . PRO A 1 234 G 1.905 27.289 17.443 1.00 55.58 ? 245 PRO A N 1 ATOM 1811 C CA . PRO A 1 234 G 0.602 27.808 17.874 1.00 55.20 ? 245 PRO A CA 1 ATOM 1812 C C . PRO A 1 234 G 0.420 29.303 17.613 1.00 55.68 ? 245 PRO A C 1 ATOM 1813 O O . PRO A 1 234 G -0.647 29.683 17.073 1.00 55.51 ? 245 PRO A O 1 ATOM 1814 C CB . PRO A 1 234 G 0.568 27.461 19.362 1.00 54.92 ? 245 PRO A CB 1 ATOM 1815 C CG . PRO A 1 234 G 2.031 27.466 19.743 1.00 55.55 ? 245 PRO A CG 1 ATOM 1816 C CD . PRO A 1 234 G 2.649 26.732 18.586 1.00 55.45 ? 245 PRO A CD 1 ATOM 1817 O OXT . PRO A 1 234 G 1.343 30.077 17.957 1.00 54.44 ? 245 PRO A OXT 1 ATOM 1818 N N . ILE B 2 7 ? -9.138 41.186 7.662 1.00 42.50 ? 1539 ILE B N 1 ATOM 1819 C CA . ILE B 2 7 ? -8.015 41.646 6.782 1.00 40.24 ? 1539 ILE B CA 1 ATOM 1820 C C . ILE B 2 7 ? -8.491 42.625 5.707 1.00 39.48 ? 1539 ILE B C 1 ATOM 1821 O O . ILE B 2 7 ? -9.299 42.279 4.856 1.00 40.50 ? 1539 ILE B O 1 ATOM 1822 C CB . ILE B 2 7 ? -7.322 40.453 6.059 1.00 40.48 ? 1539 ILE B CB 1 ATOM 1823 C CG1 . ILE B 2 7 ? -6.780 39.444 7.078 1.00 39.99 ? 1539 ILE B CG1 1 ATOM 1824 C CG2 . ILE B 2 7 ? -6.185 40.969 5.179 1.00 38.85 ? 1539 ILE B CG2 1 ATOM 1825 C CD1 . ILE B 2 7 ? -5.981 38.301 6.438 1.00 39.67 ? 1539 ILE B CD1 1 ATOM 1826 N N . ALA B 2 8 ? -7.962 43.840 5.741 1.00 38.31 ? 1540 ALA B N 1 ATOM 1827 C CA . ALA B 2 8 ? -8.310 44.875 4.769 1.00 37.40 ? 1540 ALA B CA 1 ATOM 1828 C C . ALA B 2 8 ? -8.007 44.443 3.329 1.00 36.41 ? 1540 ALA B C 1 ATOM 1829 O O . ALA B 2 8 ? -7.012 43.762 3.061 1.00 35.55 ? 1540 ALA B O 1 ATOM 1830 C CB . ALA B 2 8 ? -7.556 46.171 5.106 1.00 38.11 ? 1540 ALA B CB 1 ATOM 1831 N N . ALA B 2 9 ? -8.857 44.871 2.400 1.00 36.68 ? 1541 ALA B N 1 ATOM 1832 C CA . ALA B 2 9 ? -8.711 44.514 0.982 1.00 35.59 ? 1541 ALA B CA 1 ATOM 1833 C C . ALA B 2 9 ? -7.438 45.027 0.293 1.00 34.20 ? 1541 ALA B C 1 ATOM 1834 O O . ALA B 2 9 ? -7.032 44.513 -0.747 1.00 33.88 ? 1541 ALA B O 1 ATOM 1835 C CB . ALA B 2 9 ? -9.959 44.993 0.204 1.00 37.24 ? 1541 ALA B CB 1 ATOM 1836 N N . TRP B 2 10 ? -6.804 46.031 0.876 1.00 31.24 ? 1542 TRP B N 1 ATOM 1837 C CA . TRP B 2 10 ? -5.604 46.605 0.270 1.00 29.62 ? 1542 TRP B CA 1 ATOM 1838 C C . TRP B 2 10 ? -4.314 46.036 0.849 1.00 26.55 ? 1542 TRP B C 1 ATOM 1839 O O . TRP B 2 10 ? -3.230 46.381 0.400 1.00 27.86 ? 1542 TRP B O 1 ATOM 1840 C CB . TRP B 2 10 ? -5.605 48.125 0.485 1.00 29.93 ? 1542 TRP B CB 1 ATOM 1841 C CG . TRP B 2 10 ? -5.962 48.543 1.913 1.00 31.09 ? 1542 TRP B CG 1 ATOM 1842 C CD1 . TRP B 2 10 ? -7.155 49.074 2.336 1.00 35.00 ? 1542 TRP B CD1 1 ATOM 1843 C CD2 . TRP B 2 10 ? -5.137 48.433 3.091 1.00 31.85 ? 1542 TRP B CD2 1 ATOM 1844 N NE1 . TRP B 2 10 ? -7.125 49.296 3.700 1.00 35.42 ? 1542 TRP B NE1 1 ATOM 1845 C CE2 . TRP B 2 10 ? -5.901 48.911 4.187 1.00 34.23 ? 1542 TRP B CE2 1 ATOM 1846 C CE3 . TRP B 2 10 ? -3.832 47.977 3.327 1.00 30.05 ? 1542 TRP B CE3 1 ATOM 1847 C CZ2 . TRP B 2 10 ? -5.401 48.941 5.499 1.00 32.49 ? 1542 TRP B CZ2 1 ATOM 1848 C CZ3 . TRP B 2 10 ? -3.333 48.006 4.633 1.00 29.28 ? 1542 TRP B CZ3 1 ATOM 1849 C CH2 . TRP B 2 10 ? -4.124 48.487 5.704 1.00 32.34 ? 1542 TRP B CH2 1 ATOM 1850 N N . TYR B 2 11 ? -4.432 45.144 1.825 1.00 24.62 ? 1543 TYR B N 1 ATOM 1851 C CA . TYR B 2 11 ? -3.263 44.622 2.509 1.00 22.31 ? 1543 TYR B CA 1 ATOM 1852 C C . TYR B 2 11 ? -2.434 43.534 1.845 1.00 22.90 ? 1543 TYR B C 1 ATOM 1853 O O . TYR B 2 11 ? -1.220 43.660 1.734 1.00 21.43 ? 1543 TYR B O 1 ATOM 1854 C CB . TYR B 2 11 ? -3.679 44.160 3.908 1.00 23.67 ? 1543 TYR B CB 1 ATOM 1855 C CG . TYR B 2 11 ? -2.618 43.412 4.691 1.00 24.58 ? 1543 TYR B CG 1 ATOM 1856 C CD1 . TYR B 2 11 ? -2.648 42.021 4.783 1.00 24.59 ? 1543 TYR B CD1 1 ATOM 1857 C CD2 . TYR B 2 11 ? -1.631 44.098 5.389 1.00 22.62 ? 1543 TYR B CD2 1 ATOM 1858 C CE1 . TYR B 2 11 ? -1.725 41.334 5.557 1.00 26.50 ? 1543 TYR B CE1 1 ATOM 1859 C CE2 . TYR B 2 11 ? -0.717 43.436 6.163 1.00 24.06 ? 1543 TYR B CE2 1 ATOM 1860 C CZ . TYR B 2 11 ? -0.766 42.047 6.250 1.00 24.60 ? 1543 TYR B CZ 1 ATOM 1861 O OH . TYR B 2 11 ? 0.116 41.383 7.053 1.00 26.51 ? 1543 TYR B OH 1 ATOM 1862 N N . LEU B 2 12 ? -3.083 42.461 1.415 1.00 22.60 ? 1544 LEU B N 1 ATOM 1863 C CA . LEU B 2 12 ? -2.352 41.353 0.821 1.00 22.81 ? 1544 LEU B CA 1 ATOM 1864 C C . LEU B 2 12 ? -1.653 41.758 -0.473 1.00 21.53 ? 1544 LEU B C 1 ATOM 1865 O O . LEU B 2 12 ? -2.258 42.369 -1.361 1.00 22.00 ? 1544 LEU B O 1 ATOM 1866 C CB . LEU B 2 12 ? -3.307 40.178 0.575 1.00 22.71 ? 1544 LEU B CB 1 ATOM 1867 C CG . LEU B 2 12 ? -3.970 39.613 1.841 1.00 23.46 ? 1544 LEU B CG 1 ATOM 1868 C CD1 . LEU B 2 12 ? -4.964 38.524 1.426 1.00 24.99 ? 1544 LEU B CD1 1 ATOM 1869 C CD2 . LEU B 2 12 ? -2.932 39.049 2.803 1.00 22.67 ? 1544 LEU B CD2 1 ATOM 1870 N N . ARG B 2 13 ? -0.374 41.414 -0.582 1.00 20.14 ? 1545 ARG B N 1 ATOM 1871 C CA . ARG B 2 13 ? 0.363 41.763 -1.785 1.00 18.95 ? 1545 ARG B CA 1 ATOM 1872 C C . ARG B 2 13 ? 0.546 40.576 -2.722 1.00 20.11 ? 1545 ARG B C 1 ATOM 1873 O O . ARG B 2 13 ? -0.329 39.679 -2.675 1.00 20.61 ? 1545 ARG B O 1 ATOM 1874 C CB . ARG B 2 13 ? 1.704 42.410 -1.413 1.00 20.51 ? 1545 ARG B CB 1 ATOM 1875 C CG . ARG B 2 13 ? 1.480 43.840 -0.920 1.00 20.78 ? 1545 ARG B CG 1 ATOM 1876 C CD . ARG B 2 13 ? 2.680 44.414 -0.172 1.00 21.13 ? 1545 ARG B CD 1 ATOM 1877 N NE . ARG B 2 13 ? 2.458 45.826 0.156 1.00 20.56 ? 1545 ARG B NE 1 ATOM 1878 C CZ . ARG B 2 13 ? 3.330 46.577 0.820 1.00 23.27 ? 1545 ARG B CZ 1 ATOM 1879 N NH1 . ARG B 2 13 ? 4.474 46.042 1.227 1.00 20.25 ? 1545 ARG B NH1 1 ATOM 1880 N NH2 . ARG B 2 13 ? 3.068 47.870 1.055 1.00 19.37 ? 1545 ARG B NH2 1 HETATM 1881 C C1 . NAG C 3 . ? 5.217 13.917 12.847 1.00 64.33 ? 801 NAG A C1 1 HETATM 1882 C C2 . NAG C 3 . ? 5.528 12.514 13.374 1.00 66.39 ? 801 NAG A C2 1 HETATM 1883 C C3 . NAG C 3 . ? 4.828 12.298 14.717 1.00 67.98 ? 801 NAG A C3 1 HETATM 1884 C C4 . NAG C 3 . ? 5.176 13.426 15.694 1.00 68.66 ? 801 NAG A C4 1 HETATM 1885 C C5 . NAG C 3 . ? 4.879 14.786 15.047 1.00 67.28 ? 801 NAG A C5 1 HETATM 1886 C C6 . NAG C 3 . ? 5.287 15.961 15.917 1.00 66.33 ? 801 NAG A C6 1 HETATM 1887 C C7 . NAG C 3 . ? 5.889 10.551 12.017 1.00 68.23 ? 801 NAG A C7 1 HETATM 1888 C C8 . NAG C 3 . ? 7.079 10.917 11.144 1.00 68.08 ? 801 NAG A C8 1 HETATM 1889 N N2 . NAG C 3 . ? 5.078 11.530 12.407 1.00 67.43 ? 801 NAG A N2 1 HETATM 1890 O O3 . NAG C 3 . ? 5.223 11.051 15.270 1.00 68.48 ? 801 NAG A O3 1 HETATM 1891 O O4 . NAG C 3 . ? 4.393 13.277 16.894 1.00 71.69 ? 801 NAG A O4 1 HETATM 1892 O O5 . NAG C 3 . ? 5.602 14.909 13.805 1.00 65.45 ? 801 NAG A O5 1 HETATM 1893 O O6 . NAG C 3 . ? 6.697 16.019 16.070 1.00 66.41 ? 801 NAG A O6 1 HETATM 1894 O O7 . NAG C 3 . ? 5.700 9.377 12.323 1.00 69.07 ? 801 NAG A O7 1 HETATM 1895 C C1 . NAG D 3 . ? 5.037 13.535 18.092 1.00 74.20 ? 802 NAG A C1 1 HETATM 1896 C C2 . NAG D 3 . ? 3.992 13.749 19.191 1.00 75.71 ? 802 NAG A C2 1 HETATM 1897 C C3 . NAG D 3 . ? 4.686 13.925 20.547 1.00 76.72 ? 802 NAG A C3 1 HETATM 1898 C C4 . NAG D 3 . ? 5.581 12.717 20.807 1.00 77.12 ? 802 NAG A C4 1 HETATM 1899 C C5 . NAG D 3 . ? 6.574 12.550 19.648 1.00 76.35 ? 802 NAG A C5 1 HETATM 1900 C C6 . NAG D 3 . ? 7.450 11.322 19.801 1.00 76.03 ? 802 NAG A C6 1 HETATM 1901 C C7 . NAG D 3 . ? 1.886 14.752 18.608 1.00 76.12 ? 802 NAG A C7 1 HETATM 1902 C C8 . NAG D 3 . ? 0.915 15.728 19.254 1.00 76.09 ? 802 NAG A C8 1 HETATM 1903 N N2 . NAG D 3 . ? 3.179 14.909 18.878 1.00 75.83 ? 802 NAG A N2 1 HETATM 1904 O O3 . NAG D 3 . ? 3.714 14.034 21.579 1.00 77.67 ? 802 NAG A O3 1 HETATM 1905 O O4 . NAG D 3 . ? 6.291 12.881 22.051 1.00 78.56 ? 802 NAG A O4 1 HETATM 1906 O O5 . NAG D 3 . ? 5.859 12.402 18.401 1.00 75.37 ? 802 NAG A O5 1 HETATM 1907 O O6 . NAG D 3 . ? 6.743 10.138 19.465 1.00 74.82 ? 802 NAG A O6 1 HETATM 1908 O O7 . NAG D 3 . ? 1.459 13.853 17.879 1.00 75.73 ? 802 NAG A O7 1 HETATM 1909 C C1 . BMA E 4 . ? 6.358 11.748 22.848 1.00 79.76 ? 803 BMA A C1 1 HETATM 1910 C C2 . BMA E 4 . ? 7.724 11.675 23.548 1.00 79.96 ? 803 BMA A C2 1 HETATM 1911 C C3 . BMA E 4 . ? 7.761 10.473 24.494 1.00 80.34 ? 803 BMA A C3 1 HETATM 1912 C C4 . BMA E 4 . ? 6.572 10.530 25.460 1.00 80.75 ? 803 BMA A C4 1 HETATM 1913 C C5 . BMA E 4 . ? 5.257 10.655 24.674 1.00 80.54 ? 803 BMA A C5 1 HETATM 1914 C C6 . BMA E 4 . ? 4.052 10.813 25.582 1.00 80.66 ? 803 BMA A C6 1 HETATM 1915 O O2 . BMA E 4 . ? 7.951 12.866 24.284 1.00 80.01 ? 803 BMA A O2 1 HETATM 1916 O O3 . BMA E 4 . ? 8.978 10.476 25.228 1.00 79.87 ? 803 BMA A O3 1 HETATM 1917 O O4 . BMA E 4 . ? 6.545 9.354 26.259 1.00 81.51 ? 803 BMA A O4 1 HETATM 1918 O O5 . BMA E 4 . ? 5.298 11.817 23.815 1.00 80.10 ? 803 BMA A O5 1 HETATM 1919 O O6 . BMA E 4 . ? 2.846 10.875 24.835 1.00 80.59 ? 803 BMA A O6 1 HETATM 1920 C C2 . BGC F 5 . ? 4.969 33.120 -20.297 1.00 49.44 ? 701 BGC A C2 1 HETATM 1921 C C3 . BGC F 5 . ? 6.448 33.047 -19.918 1.00 49.07 ? 701 BGC A C3 1 HETATM 1922 C C4 . BGC F 5 . ? 6.727 33.880 -18.660 1.00 48.06 ? 701 BGC A C4 1 HETATM 1923 C C5 . BGC F 5 . ? 5.773 33.449 -17.525 1.00 47.48 ? 701 BGC A C5 1 HETATM 1924 C C6 . BGC F 5 . ? 5.897 34.316 -16.277 1.00 46.08 ? 701 BGC A C6 1 HETATM 1925 C C1 . BGC F 5 . ? 4.115 32.689 -19.094 1.00 48.82 ? 701 BGC A C1 1 HETATM 1926 O O1 . BGC F 5 . ? 2.767 32.811 -19.398 1.00 49.00 ? 701 BGC A O1 1 HETATM 1927 O O2 . BGC F 5 . ? 4.718 32.263 -21.402 1.00 49.71 ? 701 BGC A O2 1 HETATM 1928 O O3 . BGC F 5 . ? 7.245 33.518 -20.991 1.00 49.40 ? 701 BGC A O3 1 HETATM 1929 O O4 . BGC F 5 . ? 8.080 33.690 -18.262 1.00 45.66 ? 701 BGC A O4 1 HETATM 1930 O O5 . BGC F 5 . ? 4.393 33.533 -17.966 1.00 48.15 ? 701 BGC A O5 1 HETATM 1931 O O6 . BGC F 5 . ? 5.533 35.670 -16.536 1.00 43.84 ? 701 BGC A O6 1 HETATM 1932 C C1 . GLC G 6 . ? 21.932 42.947 1.883 1.00 46.67 ? 702 GLC A C1 1 HETATM 1933 C C2 . GLC G 6 . ? 21.352 42.644 3.274 1.00 46.36 ? 702 GLC A C2 1 HETATM 1934 C C3 . GLC G 6 . ? 21.871 41.281 3.749 1.00 45.34 ? 702 GLC A C3 1 HETATM 1935 C C4 . GLC G 6 . ? 21.474 40.209 2.717 1.00 45.04 ? 702 GLC A C4 1 HETATM 1936 C C5 . GLC G 6 . ? 22.029 40.603 1.342 1.00 46.57 ? 702 GLC A C5 1 HETATM 1937 C C6 . GLC G 6 . ? 21.606 39.644 0.244 1.00 47.37 ? 702 GLC A C6 1 HETATM 1938 O O1 . GLC G 6 . ? 23.315 42.967 1.946 1.00 46.99 ? 702 GLC A O1 1 HETATM 1939 O O2 . GLC G 6 . ? 21.730 43.664 4.193 1.00 47.96 ? 702 GLC A O2 1 HETATM 1940 O O3 . GLC G 6 . ? 21.322 40.972 5.025 1.00 41.92 ? 702 GLC A O3 1 HETATM 1941 O O4 . GLC G 6 . ? 21.992 38.938 3.096 1.00 41.40 ? 702 GLC A O4 1 HETATM 1942 O O5 . GLC G 6 . ? 21.554 41.917 0.960 1.00 47.11 ? 702 GLC A O5 1 HETATM 1943 O O6 . GLC G 6 . ? 22.166 40.025 -1.006 1.00 48.85 ? 702 GLC A O6 1 HETATM 1944 C C . ACT H 7 . ? 1.405 51.196 -5.267 1.00 23.61 ? 901 ACT A C 1 HETATM 1945 O O . ACT H 7 . ? 0.942 50.638 -6.241 1.00 23.42 ? 901 ACT A O 1 HETATM 1946 O OXT . ACT H 7 . ? 0.787 51.185 -4.203 1.00 22.70 ? 901 ACT A OXT 1 HETATM 1947 C CH3 . ACT H 7 . ? 2.736 51.905 -5.372 1.00 24.01 ? 901 ACT A CH3 1 HETATM 1948 C C . ACT I 7 . ? 11.980 48.855 -14.857 1.00 48.29 ? 902 ACT A C 1 HETATM 1949 O O . ACT I 7 . ? 12.575 47.785 -14.897 1.00 47.43 ? 902 ACT A O 1 HETATM 1950 O OXT . ACT I 7 . ? 12.370 49.750 -14.105 1.00 46.03 ? 902 ACT A OXT 1 HETATM 1951 C CH3 . ACT I 7 . ? 10.771 49.076 -15.732 1.00 47.53 ? 902 ACT A CH3 1 HETATM 1952 C C . ACT J 7 . ? 26.104 33.162 -15.885 1.00 36.22 ? 903 ACT A C 1 HETATM 1953 O O . ACT J 7 . ? 25.284 33.253 -16.793 1.00 35.58 ? 903 ACT A O 1 HETATM 1954 O OXT . ACT J 7 . ? 25.934 33.773 -14.837 1.00 37.10 ? 903 ACT A OXT 1 HETATM 1955 C CH3 . ACT J 7 . ? 27.330 32.288 -16.049 1.00 38.64 ? 903 ACT A CH3 1 HETATM 1956 C C . ACT K 7 . ? 24.352 36.527 -16.699 1.00 39.52 ? 904 ACT A C 1 HETATM 1957 O O . ACT K 7 . ? 23.415 35.769 -16.406 1.00 39.56 ? 904 ACT A O 1 HETATM 1958 O OXT . ACT K 7 . ? 25.314 36.636 -15.943 1.00 38.74 ? 904 ACT A OXT 1 HETATM 1959 C CH3 . ACT K 7 . ? 24.310 37.317 -17.981 1.00 40.07 ? 904 ACT A CH3 1 HETATM 1960 ZN ZN . ZN L 8 . ? -0.920 50.180 -4.353 1.00 22.40 ? 501 ZN A ZN 1 HETATM 1961 ZN ZN . ZN M 8 . ? 13.750 49.311 -12.916 1.00 38.15 ? 502 ZN A ZN 1 HETATM 1962 ZN ZN . ZN N 8 . ? 23.922 34.447 -14.991 1.00 39.87 ? 503 ZN A ZN 1 HETATM 1963 O O . HOH O 9 . ? 8.839 46.608 3.715 1.00 17.84 ? 1 HOH A O 1 HETATM 1964 O O . HOH O 9 . ? 3.208 52.031 2.628 1.00 22.44 ? 2 HOH A O 1 HETATM 1965 O O . HOH O 9 . ? 11.110 40.097 -1.058 1.00 18.90 ? 3 HOH A O 1 HETATM 1966 O O . HOH O 9 . ? 15.285 33.717 -10.155 1.00 21.21 ? 4 HOH A O 1 HETATM 1967 O O . HOH O 9 . ? 24.240 20.746 -10.184 1.00 27.33 ? 5 HOH A O 1 HETATM 1968 O O . HOH O 9 . ? 12.214 49.338 -7.290 1.00 27.52 ? 6 HOH A O 1 HETATM 1969 O O . HOH O 9 . ? 12.665 32.227 -11.235 1.00 22.68 ? 7 HOH A O 1 HETATM 1970 O O . HOH O 9 . ? 7.127 38.728 -7.395 1.00 23.02 ? 8 HOH A O 1 HETATM 1971 O O . HOH O 9 . ? 8.671 38.873 -4.041 1.00 33.03 ? 9 HOH A O 1 HETATM 1972 O O . HOH O 9 . ? 12.696 34.336 10.611 1.00 29.85 ? 10 HOH A O 1 HETATM 1973 O O . HOH O 9 . ? 23.686 22.296 -13.505 1.00 26.19 ? 11 HOH A O 1 HETATM 1974 O O . HOH O 9 . ? 6.702 51.932 3.676 1.00 23.28 ? 12 HOH A O 1 HETATM 1975 O O . HOH O 9 . ? 20.038 34.809 -9.758 1.00 27.08 ? 13 HOH A O 1 HETATM 1976 O O . HOH O 9 . ? 21.298 19.210 -8.589 1.00 27.29 ? 14 HOH A O 1 HETATM 1977 O O . HOH O 9 . ? 9.013 50.384 4.309 1.00 23.64 ? 15 HOH A O 1 HETATM 1978 O O . HOH O 9 . ? -3.013 28.604 16.179 1.00 49.62 ? 61 HOH A O 1 HETATM 1979 O O . HOH O 9 . ? 2.466 13.865 -4.037 1.00 54.38 ? 126 HOH A O 1 HETATM 1980 O O . HOH O 9 . ? 8.783 13.657 -8.447 1.00 56.43 ? 130 HOH A O 1 HETATM 1981 O O . HOH O 9 . ? 15.988 49.582 -12.235 1.00 51.37 ? 150 HOH A O 1 HETATM 1982 O O . HOH O 9 . ? -6.636 31.068 -10.539 1.00 43.05 ? 151 HOH A O 1 HETATM 1983 O O . HOH O 9 . ? -4.748 30.198 0.137 1.00 34.05 ? 246 HOH A O 1 HETATM 1984 O O . HOH O 9 . ? 1.866 35.016 8.706 1.00 25.37 ? 247 HOH A O 1 HETATM 1985 O O . HOH O 9 . ? 12.450 50.195 15.011 1.00 33.71 ? 248 HOH A O 1 HETATM 1986 O O . HOH O 9 . ? -10.604 34.009 7.544 1.00 35.24 ? 249 HOH A O 1 HETATM 1987 O O . HOH O 9 . ? 21.246 30.825 1.804 1.00 30.93 ? 250 HOH A O 1 HETATM 1988 O O . HOH O 9 . ? 0.626 31.225 -18.491 1.00 35.62 ? 251 HOH A O 1 HETATM 1989 O O . HOH O 9 . ? 11.661 34.322 -19.183 1.00 36.38 ? 252 HOH A O 1 HETATM 1990 O O . HOH O 9 . ? 5.780 41.746 -13.054 1.00 32.12 ? 253 HOH A O 1 HETATM 1991 O O . HOH O 9 . ? 9.638 43.162 13.737 1.00 27.68 ? 254 HOH A O 1 HETATM 1992 O O . HOH O 9 . ? 20.070 45.565 -7.464 1.00 37.10 ? 255 HOH A O 1 HETATM 1993 O O . HOH O 9 . ? 17.820 33.084 -11.030 1.00 23.44 ? 256 HOH A O 1 HETATM 1994 O O . HOH O 9 . ? -7.343 30.023 -8.159 1.00 36.19 ? 257 HOH A O 1 HETATM 1995 O O . HOH O 9 . ? 2.830 33.871 11.050 1.00 28.71 ? 258 HOH A O 1 HETATM 1996 O O . HOH O 9 . ? 6.190 54.303 -13.332 1.00 46.64 ? 259 HOH A O 1 HETATM 1997 O O . HOH O 9 . ? 23.521 18.841 -3.467 1.00 36.07 ? 260 HOH A O 1 HETATM 1998 O O . HOH O 9 . ? 3.757 49.310 3.697 1.00 25.06 ? 261 HOH A O 1 HETATM 1999 O O . HOH O 9 . ? -2.392 57.263 7.650 1.00 47.32 ? 262 HOH A O 1 HETATM 2000 O O . HOH O 9 . ? 9.602 44.618 -8.226 1.00 21.68 ? 263 HOH A O 1 HETATM 2001 O O . HOH O 9 . ? -2.638 37.031 -4.220 1.00 33.44 ? 264 HOH A O 1 HETATM 2002 O O . HOH O 9 . ? -1.866 51.516 6.646 1.00 34.07 ? 265 HOH A O 1 HETATM 2003 O O . HOH O 9 . ? 14.388 36.500 12.123 1.00 31.74 ? 266 HOH A O 1 HETATM 2004 O O . HOH O 9 . ? -1.569 37.395 5.574 1.00 24.24 ? 267 HOH A O 1 HETATM 2005 O O . HOH O 9 . ? 3.462 40.348 -14.021 1.00 32.19 ? 268 HOH A O 1 HETATM 2006 O O . HOH O 9 . ? 18.679 23.963 -14.014 1.00 36.38 ? 269 HOH A O 1 HETATM 2007 O O . HOH O 9 . ? -2.123 24.026 -8.497 1.00 43.97 ? 270 HOH A O 1 HETATM 2008 O O . HOH O 9 . ? 14.993 34.909 -17.375 1.00 29.34 ? 271 HOH A O 1 HETATM 2009 O O . HOH O 9 . ? 15.044 30.177 -9.189 1.00 26.44 ? 272 HOH A O 1 HETATM 2010 O O . HOH O 9 . ? 14.376 55.279 7.781 1.00 37.37 ? 273 HOH A O 1 HETATM 2011 O O . HOH O 9 . ? -2.739 29.278 5.923 1.00 36.46 ? 274 HOH A O 1 HETATM 2012 O O . HOH O 9 . ? 2.731 58.287 6.865 1.00 42.10 ? 275 HOH A O 1 HETATM 2013 O O . HOH O 9 . ? -3.217 23.302 -13.855 1.00 53.42 ? 276 HOH A O 1 HETATM 2014 O O . HOH O 9 . ? 18.365 35.018 -13.102 1.00 25.35 ? 277 HOH A O 1 HETATM 2015 O O . HOH O 9 . ? 17.112 25.328 2.568 1.00 35.71 ? 278 HOH A O 1 HETATM 2016 O O . HOH O 9 . ? -1.874 21.172 4.448 1.00 38.47 ? 279 HOH A O 1 HETATM 2017 O O . HOH O 9 . ? -2.777 51.454 3.857 1.00 31.86 ? 280 HOH A O 1 HETATM 2018 O O . HOH O 9 . ? 3.244 53.666 11.719 1.00 41.82 ? 281 HOH A O 1 HETATM 2019 O O . HOH O 9 . ? 7.875 24.991 13.174 1.00 34.16 ? 282 HOH A O 1 HETATM 2020 O O . HOH O 9 . ? 21.671 34.740 -18.043 1.00 44.90 ? 283 HOH A O 1 HETATM 2021 O O . HOH O 9 . ? 20.061 20.479 -1.338 1.00 33.65 ? 284 HOH A O 1 HETATM 2022 O O . HOH O 9 . ? 16.948 38.295 -17.813 1.00 32.44 ? 285 HOH A O 1 HETATM 2023 O O . HOH O 9 . ? 12.487 12.450 -2.330 1.00 55.61 ? 286 HOH A O 1 HETATM 2024 O O . HOH O 9 . ? -2.307 54.125 4.241 1.00 39.02 ? 287 HOH A O 1 HETATM 2025 O O . HOH O 9 . ? 6.288 20.153 -13.403 1.00 32.45 ? 288 HOH A O 1 HETATM 2026 O O . HOH O 9 . ? 13.501 17.817 6.127 1.00 47.32 ? 289 HOH A O 1 HETATM 2027 O O . HOH O 9 . ? 16.423 21.751 -13.448 1.00 47.23 ? 290 HOH A O 1 HETATM 2028 O O . HOH O 9 . ? 25.237 24.994 -9.710 1.00 39.72 ? 291 HOH A O 1 HETATM 2029 O O . HOH O 9 . ? -1.332 41.436 -6.074 1.00 35.92 ? 292 HOH A O 1 HETATM 2030 O O . HOH O 9 . ? 20.901 48.258 12.602 1.00 49.72 ? 293 HOH A O 1 HETATM 2031 O O . HOH O 9 . ? -1.048 35.060 -11.984 1.00 27.75 ? 294 HOH A O 1 HETATM 2032 O O . HOH O 9 . ? 9.883 52.980 3.157 1.00 35.77 ? 295 HOH A O 1 HETATM 2033 O O . HOH O 9 . ? 7.779 43.785 -21.606 1.00 62.68 ? 296 HOH A O 1 HETATM 2034 O O . HOH O 9 . ? -0.011 36.932 9.092 1.00 35.69 ? 297 HOH A O 1 HETATM 2035 O O . HOH O 9 . ? 18.058 22.249 0.874 1.00 41.72 ? 298 HOH A O 1 HETATM 2036 O O . HOH O 9 . ? 20.564 41.092 8.851 1.00 43.32 ? 299 HOH A O 1 HETATM 2037 O O . HOH O 9 . ? 21.333 30.458 -2.971 1.00 44.88 ? 300 HOH A O 1 HETATM 2038 O O . HOH O 9 . ? 11.205 26.053 14.675 1.00 41.79 ? 301 HOH A O 1 HETATM 2039 O O . HOH O 9 . ? 1.249 34.070 13.492 1.00 39.27 ? 302 HOH A O 1 HETATM 2040 O O . HOH O 9 . ? 17.419 35.932 -19.314 1.00 51.01 ? 303 HOH A O 1 HETATM 2041 O O . HOH O 9 . ? 23.176 41.711 -4.415 1.00 61.49 ? 304 HOH A O 1 HETATM 2042 O O . HOH O 9 . ? 24.375 25.698 -15.098 1.00 42.65 ? 305 HOH A O 1 HETATM 2043 O O . HOH O 9 . ? -5.212 52.832 2.929 1.00 66.14 ? 306 HOH A O 1 HETATM 2044 O O . HOH O 9 . ? 10.138 60.901 6.022 1.00 44.43 ? 307 HOH A O 1 HETATM 2045 O O . HOH O 9 . ? 13.555 53.558 -7.291 1.00 50.32 ? 308 HOH A O 1 HETATM 2046 O O . HOH O 9 . ? -2.479 45.850 -9.712 1.00 52.31 ? 309 HOH A O 1 HETATM 2047 O O . HOH O 9 . ? -0.265 36.942 11.768 1.00 38.33 ? 310 HOH A O 1 HETATM 2048 O O . HOH O 9 . ? 10.983 53.980 19.186 1.00 65.74 ? 311 HOH A O 1 HETATM 2049 O O . HOH O 9 . ? 21.612 32.106 -19.393 1.00 48.71 ? 312 HOH A O 1 HETATM 2050 O O . HOH O 9 . ? 13.612 16.593 -13.217 1.00 49.37 ? 313 HOH A O 1 HETATM 2051 O O . HOH O 9 . ? 7.561 15.057 2.099 1.00 46.71 ? 314 HOH A O 1 HETATM 2052 O O . HOH O 9 . ? 18.757 16.833 -11.353 1.00 42.06 ? 315 HOH A O 1 HETATM 2053 O O . HOH O 9 . ? -6.983 25.578 12.314 1.00 54.44 ? 316 HOH A O 1 HETATM 2054 O O . HOH O 9 . ? 21.357 17.553 -0.915 1.00 31.85 ? 317 HOH A O 1 HETATM 2055 O O . HOH O 9 . ? -2.148 21.105 -8.025 1.00 54.94 ? 318 HOH A O 1 HETATM 2056 O O . HOH O 9 . ? 12.476 51.182 -9.329 1.00 44.74 ? 319 HOH A O 1 HETATM 2057 O O . HOH O 9 . ? 15.330 48.909 12.799 1.00 41.28 ? 320 HOH A O 1 HETATM 2058 O O . HOH O 9 . ? -1.335 18.333 -1.366 1.00 44.74 ? 321 HOH A O 1 HETATM 2059 O O . HOH O 9 . ? -1.128 23.890 -11.074 1.00 52.57 ? 322 HOH A O 1 HETATM 2060 O O . HOH O 9 . ? -5.926 48.077 -2.915 1.00 38.43 ? 323 HOH A O 1 HETATM 2061 O O . HOH O 9 . ? 0.338 40.824 -10.439 1.00 38.14 ? 324 HOH A O 1 HETATM 2062 O O . HOH O 9 . ? 14.786 23.456 12.735 1.00 57.20 ? 325 HOH A O 1 HETATM 2063 O O . HOH O 9 . ? 11.378 45.815 -16.195 1.00 41.45 ? 326 HOH A O 1 HETATM 2064 O O . HOH O 9 . ? 19.914 38.770 -3.441 1.00 44.42 ? 327 HOH A O 1 HETATM 2065 O O . HOH O 9 . ? 8.698 39.592 15.728 1.00 53.14 ? 328 HOH A O 1 HETATM 2066 O O . HOH O 9 . ? 10.875 23.232 -17.733 1.00 43.48 ? 329 HOH A O 1 HETATM 2067 O O . HOH O 9 . ? 4.602 58.951 3.017 1.00 35.08 ? 330 HOH A O 1 HETATM 2068 O O . HOH O 9 . ? 13.396 42.300 -20.219 1.00 54.65 ? 331 HOH A O 1 HETATM 2069 O O . HOH O 9 . ? -9.903 29.317 -8.591 1.00 43.15 ? 332 HOH A O 1 HETATM 2070 O O . HOH O 9 . ? -3.648 55.918 1.436 1.00 43.86 ? 333 HOH A O 1 HETATM 2071 O O . HOH O 9 . ? 4.085 28.233 -18.478 1.00 44.87 ? 334 HOH A O 1 HETATM 2072 O O . HOH O 9 . ? 13.338 27.561 14.850 1.00 49.20 ? 335 HOH A O 1 HETATM 2073 O O . HOH O 9 . ? 22.346 43.961 9.490 1.00 47.11 ? 336 HOH A O 1 HETATM 2074 O O . HOH O 9 . ? 14.979 54.795 -3.045 1.00 43.79 ? 337 HOH A O 1 HETATM 2075 O O . HOH O 9 . ? 22.644 27.443 -2.055 1.00 33.87 ? 338 HOH A O 1 HETATM 2076 O O . HOH O 9 . ? -7.383 31.200 -13.543 1.00 52.71 ? 339 HOH A O 1 HETATM 2077 O O . HOH O 9 . ? -11.225 34.537 3.247 1.00 43.87 ? 340 HOH A O 1 HETATM 2078 O O . HOH O 9 . ? 3.062 11.591 8.952 1.00 50.56 ? 341 HOH A O 1 HETATM 2079 O O . HOH O 9 . ? 10.087 33.610 -21.265 1.00 50.76 ? 342 HOH A O 1 HETATM 2080 O O . HOH O 9 . ? -1.314 19.940 -5.912 1.00 51.11 ? 343 HOH A O 1 HETATM 2081 O O . HOH O 9 . ? 11.144 15.606 -0.694 1.00 47.70 ? 344 HOH A O 1 HETATM 2082 O O . HOH O 9 . ? 8.795 54.819 -3.654 1.00 46.95 ? 345 HOH A O 1 HETATM 2083 O O . HOH O 9 . ? 4.954 55.454 -7.364 1.00 44.96 ? 346 HOH A O 1 HETATM 2084 O O . HOH O 9 . ? 8.987 15.623 -6.599 1.00 44.69 ? 347 HOH A O 1 HETATM 2085 O O . HOH O 9 . ? 5.176 54.124 -3.806 1.00 53.58 ? 348 HOH A O 1 HETATM 2086 O O . HOH O 9 . ? 18.048 25.525 5.515 1.00 47.42 ? 349 HOH A O 1 HETATM 2087 O O . HOH O 9 . ? 10.611 52.534 -7.591 1.00 51.33 ? 350 HOH A O 1 HETATM 2088 O O . HOH O 9 . ? 22.206 42.249 -13.765 1.00 44.78 ? 351 HOH A O 1 HETATM 2089 O O . HOH O 9 . ? 16.228 38.015 17.396 1.00 59.21 ? 352 HOH A O 1 HETATM 2090 O O . HOH O 9 . ? -3.449 53.538 9.553 1.00 56.64 ? 353 HOH A O 1 HETATM 2091 O O . HOH O 9 . ? 22.933 44.837 -0.798 1.00 57.34 ? 354 HOH A O 1 HETATM 2092 O O . HOH O 9 . ? 15.770 25.938 13.242 1.00 52.83 ? 355 HOH A O 1 HETATM 2093 O O . HOH O 9 . ? 10.898 28.488 -20.034 1.00 64.37 ? 356 HOH A O 1 HETATM 2094 O O . HOH O 9 . ? -0.849 16.117 -2.522 1.00 48.70 ? 357 HOH A O 1 HETATM 2095 O O . HOH O 9 . ? 21.036 49.990 1.256 1.00 52.92 ? 358 HOH A O 1 HETATM 2096 O O . HOH O 9 . ? -4.532 36.294 -9.680 1.00 43.12 ? 359 HOH A O 1 HETATM 2097 O O . HOH O 9 . ? -2.590 37.535 12.437 1.00 51.59 ? 360 HOH A O 1 HETATM 2098 O O . HOH O 9 . ? 23.604 43.499 -6.045 1.00 51.63 ? 361 HOH A O 1 HETATM 2099 O O . HOH O 9 . ? 3.810 15.139 -1.657 1.00 51.05 ? 362 HOH A O 1 HETATM 2100 O O . HOH O 9 . ? -0.263 28.138 6.388 1.00 33.58 ? 363 HOH A O 1 HETATM 2101 O O . HOH O 9 . ? 4.256 55.927 -1.387 1.00 40.54 ? 364 HOH A O 1 HETATM 2102 O O . HOH O 9 . ? -1.723 32.865 14.491 1.00 46.64 ? 365 HOH A O 1 HETATM 2103 O O . HOH O 9 . ? 23.512 26.339 -8.158 1.00 38.32 ? 366 HOH A O 1 HETATM 2104 O O . HOH O 9 . ? 15.109 48.505 -14.181 1.00 40.02 ? 367 HOH A O 1 HETATM 2105 O O . HOH O 9 . ? 14.070 50.966 -11.534 1.00 46.02 ? 368 HOH A O 1 HETATM 2106 O O . HOH O 9 . ? 10.815 41.444 15.518 1.00 48.54 ? 369 HOH A O 1 HETATM 2107 O O . HOH O 9 . ? 14.246 52.759 8.680 1.00 48.45 ? 370 HOH A O 1 HETATM 2108 O O . HOH O 9 . ? 11.907 60.849 8.177 1.00 48.88 ? 371 HOH A O 1 HETATM 2109 O O . HOH O 9 . ? -9.210 26.526 10.511 1.00 44.27 ? 372 HOH A O 1 HETATM 2110 O O . HOH O 9 . ? -5.516 35.550 -2.897 1.00 50.76 ? 373 HOH A O 1 HETATM 2111 O O . HOH O 9 . ? -2.819 19.916 -2.890 1.00 57.52 ? 374 HOH A O 1 HETATM 2112 O O . HOH O 9 . ? 19.925 42.649 -16.731 1.00 56.37 ? 375 HOH A O 1 HETATM 2113 O O . HOH O 9 . ? -0.677 20.606 -14.685 1.00 54.94 ? 376 HOH A O 1 HETATM 2114 O O . HOH O 9 . ? 22.702 24.940 -16.870 1.00 48.65 ? 377 HOH A O 1 HETATM 2115 O O . HOH O 9 . ? 11.926 58.583 9.419 1.00 40.19 ? 378 HOH A O 1 HETATM 2116 O O . HOH O 9 . ? 15.088 51.364 10.802 1.00 40.28 ? 379 HOH A O 1 HETATM 2117 O O . HOH O 9 . ? 5.224 44.037 -17.565 1.00 58.82 ? 380 HOH A O 1 HETATM 2118 O O . HOH O 9 . ? 7.362 46.251 19.318 1.00 53.90 ? 381 HOH A O 1 HETATM 2119 O O . HOH O 9 . ? 1.436 28.251 -18.619 1.00 58.41 ? 382 HOH A O 1 HETATM 2120 O O . HOH O 9 . ? 8.804 27.262 16.706 1.00 52.55 ? 383 HOH A O 1 HETATM 2121 O O . HOH O 9 . ? 0.163 15.000 0.847 1.00 50.92 ? 384 HOH A O 1 HETATM 2122 O O . HOH O 9 . ? 14.066 55.431 1.370 1.00 38.66 ? 385 HOH A O 1 HETATM 2123 O O . HOH O 9 . ? -4.109 37.260 -14.193 1.00 56.88 ? 386 HOH A O 1 HETATM 2124 O O . HOH O 9 . ? 21.026 44.283 -18.840 1.00 61.69 ? 387 HOH A O 1 HETATM 2125 O O . HOH O 9 . ? 27.654 33.426 -13.048 1.00 55.95 ? 388 HOH A O 1 HETATM 2126 O O . HOH O 9 . ? 16.402 45.496 -17.920 1.00 58.79 ? 389 HOH A O 1 HETATM 2127 O O . HOH O 9 . ? -10.151 37.799 5.351 1.00 61.66 ? 390 HOH A O 1 HETATM 2128 O O . HOH O 9 . ? 9.432 44.125 18.091 1.00 51.96 ? 391 HOH A O 1 HETATM 2129 O O . HOH O 9 . ? 14.384 42.427 18.117 1.00 47.02 ? 392 HOH A O 1 HETATM 2130 O O . HOH O 9 . ? -9.333 36.258 7.259 1.00 57.44 ? 393 HOH A O 1 HETATM 2131 O O . HOH O 9 . ? 17.965 50.233 -3.459 1.00 45.74 ? 394 HOH A O 1 HETATM 2132 O O . HOH O 9 . ? 5.395 53.657 17.341 1.00 61.37 ? 395 HOH A O 1 HETATM 2133 O O . HOH O 9 . ? -7.194 25.394 15.336 1.00 57.00 ? 396 HOH A O 1 HETATM 2134 O O . HOH O 9 . ? 13.908 38.630 18.130 1.00 66.33 ? 397 HOH A O 1 HETATM 2135 O O . HOH O 9 . ? 18.164 26.383 9.735 1.00 55.56 ? 398 HOH A O 1 HETATM 2136 O O . HOH O 9 . ? -7.630 33.622 1.181 1.00 37.62 ? 399 HOH A O 1 HETATM 2137 O O . HOH O 9 . ? 2.555 44.840 -16.967 1.00 55.97 ? 400 HOH A O 1 HETATM 2138 O O . HOH O 9 . ? -6.018 37.936 -4.950 1.00 53.06 ? 401 HOH A O 1 HETATM 2139 O O . HOH O 9 . ? -7.924 36.448 1.309 1.00 47.62 ? 402 HOH A O 1 HETATM 2140 O O . HOH O 9 . ? 3.427 58.282 -0.006 1.00 55.43 ? 403 HOH A O 1 HETATM 2141 O O . HOH O 9 . ? -3.481 44.464 -6.947 1.00 55.25 ? 404 HOH A O 1 HETATM 2142 O O . HOH O 9 . ? 10.816 9.815 26.829 1.00 63.68 ? 405 HOH A O 1 HETATM 2143 O O . HOH O 9 . ? 19.000 53.134 4.782 1.00 65.27 ? 406 HOH A O 1 HETATM 2144 O O . HOH O 9 . ? 11.838 52.832 16.728 1.00 63.44 ? 407 HOH A O 1 HETATM 2145 O O . HOH O 9 . ? 5.258 44.877 20.035 1.00 58.35 ? 408 HOH A O 1 HETATM 2146 O O . HOH O 9 . ? -0.377 42.250 -8.212 1.00 41.20 ? 409 HOH A O 1 HETATM 2147 O O . HOH O 9 . ? -12.616 38.593 5.565 1.00 65.30 ? 410 HOH A O 1 HETATM 2148 O O . HOH O 9 . ? 5.110 9.118 28.400 1.00 64.85 ? 411 HOH A O 1 HETATM 2149 O O . HOH P 9 . ? -0.026 47.010 -0.346 1.00 25.69 ? 16 HOH B O 1 HETATM 2150 O O . HOH P 9 . ? -0.700 38.625 -5.066 1.00 23.62 ? 22 HOH B O 1 HETATM 2151 O O . HOH P 9 . ? -1.592 43.281 -4.011 1.00 25.58 ? 23 HOH B O 1 HETATM 2152 O O . HOH P 9 . ? -5.929 42.025 1.288 1.00 30.27 ? 27 HOH B O 1 HETATM 2153 O O . HOH P 9 . ? -0.310 38.991 7.444 1.00 26.69 ? 29 HOH B O 1 HETATM 2154 O O . HOH P 9 . ? -2.098 45.195 -1.592 1.00 37.23 ? 74 HOH B O 1 HETATM 2155 O O . HOH P 9 . ? -4.825 43.448 -1.579 1.00 37.80 ? 76 HOH B O 1 HETATM 2156 O O . HOH P 9 . ? -3.209 39.744 -3.289 1.00 42.20 ? 78 HOH B O 1 HETATM 2157 O O . HOH P 9 . ? -11.046 46.739 2.800 1.00 49.47 ? 154 HOH B O 1 HETATM 2158 O O . HOH P 9 . ? -10.128 48.994 0.413 1.00 45.33 ? 164 HOH B O 1 # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 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 B 2 1 SER 1 1533 ? ? ? B . n B 2 2 ARG 2 1534 ? ? ? B . n B 2 3 ASP 3 1535 ? ? ? B . n B 2 4 PRO 4 1536 ? ? ? B . n B 2 5 ASP 5 1537 ? ? ? B . n B 2 6 ASN 6 1538 ? ? ? B . n B 2 7 ILE 7 1539 1539 ILE ILE B . n B 2 8 ALA 8 1540 1540 ALA ALA B . n B 2 9 ALA 9 1541 1541 ALA ALA B . n B 2 10 TRP 10 1542 1542 TRP TRP B . n B 2 11 TYR 11 1543 1543 TYR TYR B . n B 2 12 LEU 12 1544 1544 LEU LEU B . n B 2 13 ARG 13 1545 1545 ARG ARG B . n B 2 14 SER 14 1546 ? ? ? B . n # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code C 3 NAG 1 801 801 NAG NAG A . D 3 NAG 2 802 802 NAG NAG A . E 4 BMA 3 803 803 BMA BMA A . F 5 BGC 1 701 701 BGC BGC A . G 6 GLC 1 702 702 GLC GLC A . H 7 ACT 1 901 901 ACT ACT A . I 7 ACT 1 902 902 ACT ACT A . J 7 ACT 1 903 903 ACT ACT A . K 7 ACT 1 904 904 ACT ACT A . L 8 ZN 1 501 501 ZN ZN2 A . M 8 ZN 1 502 502 ZN ZN2 A . N 8 ZN 1 503 503 ZN ZN2 A . O 9 HOH 1 1 1 HOH TIP A . O 9 HOH 2 2 2 HOH TIP A . O 9 HOH 3 3 3 HOH TIP A . O 9 HOH 4 4 4 HOH TIP A . O 9 HOH 5 5 5 HOH TIP A . O 9 HOH 6 6 6 HOH TIP A . O 9 HOH 7 7 7 HOH TIP A . O 9 HOH 8 8 8 HOH TIP A . O 9 HOH 9 9 9 HOH TIP A . O 9 HOH 10 10 10 HOH TIP A . O 9 HOH 11 11 11 HOH TIP A . O 9 HOH 12 12 12 HOH TIP A . O 9 HOH 13 13 13 HOH TIP A . O 9 HOH 14 14 14 HOH TIP A . O 9 HOH 15 15 15 HOH TIP A . O 9 HOH 16 61 61 HOH TIP A . O 9 HOH 17 126 126 HOH TIP A . O 9 HOH 18 130 130 HOH TIP A . O 9 HOH 19 150 150 HOH TIP A . O 9 HOH 20 151 151 HOH TIP A . O 9 HOH 21 246 17 HOH TIP A . O 9 HOH 22 247 18 HOH TIP A . O 9 HOH 23 248 19 HOH TIP A . O 9 HOH 24 249 20 HOH TIP A . O 9 HOH 25 250 21 HOH TIP A . O 9 HOH 26 251 24 HOH TIP A . O 9 HOH 27 252 25 HOH TIP A . O 9 HOH 28 253 26 HOH TIP A . O 9 HOH 29 254 28 HOH TIP A . O 9 HOH 30 255 30 HOH TIP A . O 9 HOH 31 256 31 HOH TIP A . O 9 HOH 32 257 32 HOH TIP A . O 9 HOH 33 258 33 HOH TIP A . O 9 HOH 34 259 34 HOH TIP A . O 9 HOH 35 260 35 HOH TIP A . O 9 HOH 36 261 36 HOH TIP A . O 9 HOH 37 262 37 HOH TIP A . O 9 HOH 38 263 38 HOH TIP A . O 9 HOH 39 264 39 HOH TIP A . O 9 HOH 40 265 40 HOH TIP A . O 9 HOH 41 266 41 HOH TIP A . O 9 HOH 42 267 42 HOH TIP A . O 9 HOH 43 268 43 HOH TIP A . O 9 HOH 44 269 44 HOH TIP A . O 9 HOH 45 270 45 HOH TIP A . O 9 HOH 46 271 46 HOH TIP A . O 9 HOH 47 272 47 HOH TIP A . O 9 HOH 48 273 48 HOH TIP A . O 9 HOH 49 274 49 HOH TIP A . O 9 HOH 50 275 50 HOH TIP A . O 9 HOH 51 276 51 HOH TIP A . O 9 HOH 52 277 52 HOH TIP A . O 9 HOH 53 278 53 HOH TIP A . O 9 HOH 54 279 54 HOH TIP A . O 9 HOH 55 280 55 HOH TIP A . O 9 HOH 56 281 56 HOH TIP A . O 9 HOH 57 282 57 HOH TIP A . O 9 HOH 58 283 58 HOH TIP A . O 9 HOH 59 284 59 HOH TIP A . O 9 HOH 60 285 60 HOH TIP A . O 9 HOH 61 286 62 HOH TIP A . O 9 HOH 62 287 63 HOH TIP A . O 9 HOH 63 288 64 HOH TIP A . O 9 HOH 64 289 65 HOH TIP A . O 9 HOH 65 290 66 HOH TIP A . O 9 HOH 66 291 67 HOH TIP A . O 9 HOH 67 292 68 HOH TIP A . O 9 HOH 68 293 69 HOH TIP A . O 9 HOH 69 294 70 HOH TIP A . O 9 HOH 70 295 71 HOH TIP A . O 9 HOH 71 296 72 HOH TIP A . O 9 HOH 72 297 73 HOH TIP A . O 9 HOH 73 298 75 HOH TIP A . O 9 HOH 74 299 77 HOH TIP A . O 9 HOH 75 300 79 HOH TIP A . O 9 HOH 76 301 80 HOH TIP A . O 9 HOH 77 302 81 HOH TIP A . O 9 HOH 78 303 82 HOH TIP A . O 9 HOH 79 304 83 HOH TIP A . O 9 HOH 80 305 84 HOH TIP A . O 9 HOH 81 306 85 HOH TIP A . O 9 HOH 82 307 86 HOH TIP A . O 9 HOH 83 308 87 HOH TIP A . O 9 HOH 84 309 88 HOH TIP A . O 9 HOH 85 310 89 HOH TIP A . O 9 HOH 86 311 90 HOH TIP A . O 9 HOH 87 312 91 HOH TIP A . O 9 HOH 88 313 92 HOH TIP A . O 9 HOH 89 314 93 HOH TIP A . O 9 HOH 90 315 94 HOH TIP A . O 9 HOH 91 316 95 HOH TIP A . O 9 HOH 92 317 96 HOH TIP A . O 9 HOH 93 318 97 HOH TIP A . O 9 HOH 94 319 98 HOH TIP A . O 9 HOH 95 320 99 HOH TIP A . O 9 HOH 96 321 100 HOH TIP A . O 9 HOH 97 322 101 HOH TIP A . O 9 HOH 98 323 102 HOH TIP A . O 9 HOH 99 324 103 HOH TIP A . O 9 HOH 100 325 104 HOH TIP A . O 9 HOH 101 326 105 HOH TIP A . O 9 HOH 102 327 106 HOH TIP A . O 9 HOH 103 328 107 HOH TIP A . O 9 HOH 104 329 108 HOH TIP A . O 9 HOH 105 330 109 HOH TIP A . O 9 HOH 106 331 110 HOH TIP A . O 9 HOH 107 332 111 HOH TIP A . O 9 HOH 108 333 112 HOH TIP A . O 9 HOH 109 334 113 HOH TIP A . O 9 HOH 110 335 114 HOH TIP A . O 9 HOH 111 336 115 HOH TIP A . O 9 HOH 112 337 116 HOH TIP A . O 9 HOH 113 338 117 HOH TIP A . O 9 HOH 114 339 118 HOH TIP A . O 9 HOH 115 340 119 HOH TIP A . O 9 HOH 116 341 120 HOH TIP A . O 9 HOH 117 342 121 HOH TIP A . O 9 HOH 118 343 122 HOH TIP A . O 9 HOH 119 344 123 HOH TIP A . O 9 HOH 120 345 124 HOH TIP A . O 9 HOH 121 346 125 HOH TIP A . O 9 HOH 122 347 127 HOH TIP A . O 9 HOH 123 348 128 HOH TIP A . O 9 HOH 124 349 129 HOH TIP A . O 9 HOH 125 350 131 HOH TIP A . O 9 HOH 126 351 132 HOH TIP A . O 9 HOH 127 352 133 HOH TIP A . O 9 HOH 128 353 134 HOH TIP A . O 9 HOH 129 354 135 HOH TIP A . O 9 HOH 130 355 136 HOH TIP A . O 9 HOH 131 356 137 HOH TIP A . O 9 HOH 132 357 138 HOH TIP A . O 9 HOH 133 358 139 HOH TIP A . O 9 HOH 134 359 140 HOH TIP A . O 9 HOH 135 360 141 HOH TIP A . O 9 HOH 136 361 142 HOH TIP A . O 9 HOH 137 362 143 HOH TIP A . O 9 HOH 138 363 144 HOH TIP A . O 9 HOH 139 364 145 HOH TIP A . O 9 HOH 140 365 146 HOH TIP A . O 9 HOH 141 366 147 HOH TIP A . O 9 HOH 142 367 148 HOH TIP A . O 9 HOH 143 368 149 HOH TIP A . O 9 HOH 144 369 152 HOH TIP A . O 9 HOH 145 370 153 HOH TIP A . O 9 HOH 146 371 155 HOH TIP A . O 9 HOH 147 372 156 HOH TIP A . O 9 HOH 148 373 157 HOH TIP A . O 9 HOH 149 374 158 HOH TIP A . O 9 HOH 150 375 159 HOH TIP A . O 9 HOH 151 376 160 HOH TIP A . O 9 HOH 152 377 161 HOH TIP A . O 9 HOH 153 378 162 HOH TIP A . O 9 HOH 154 379 163 HOH TIP A . O 9 HOH 155 380 165 HOH TIP A . O 9 HOH 156 381 166 HOH TIP A . O 9 HOH 157 382 167 HOH TIP A . O 9 HOH 158 383 168 HOH TIP A . O 9 HOH 159 384 169 HOH TIP A . O 9 HOH 160 385 170 HOH TIP A . O 9 HOH 161 386 171 HOH TIP A . O 9 HOH 162 387 172 HOH TIP A . O 9 HOH 163 388 173 HOH TIP A . O 9 HOH 164 389 174 HOH TIP A . O 9 HOH 165 390 175 HOH TIP A . O 9 HOH 166 391 176 HOH TIP A . O 9 HOH 167 392 177 HOH TIP A . O 9 HOH 168 393 178 HOH TIP A . O 9 HOH 169 394 179 HOH TIP A . O 9 HOH 170 395 180 HOH TIP A . O 9 HOH 171 396 181 HOH TIP A . O 9 HOH 172 397 182 HOH TIP A . O 9 HOH 173 398 183 HOH TIP A . O 9 HOH 174 399 184 HOH TIP A . O 9 HOH 175 400 185 HOH TIP A . O 9 HOH 176 401 186 HOH TIP A . O 9 HOH 177 402 187 HOH TIP A . O 9 HOH 178 403 188 HOH TIP A . O 9 HOH 179 404 189 HOH TIP A . O 9 HOH 180 405 190 HOH TIP A . O 9 HOH 181 406 191 HOH TIP A . O 9 HOH 182 407 192 HOH TIP A . O 9 HOH 183 408 193 HOH TIP A . O 9 HOH 184 409 194 HOH TIP A . O 9 HOH 185 410 195 HOH TIP A . O 9 HOH 186 411 196 HOH TIP A . P 9 HOH 1 16 16 HOH TIP B . P 9 HOH 2 22 22 HOH TIP B . P 9 HOH 3 23 23 HOH TIP B . P 9 HOH 4 27 27 HOH TIP B . P 9 HOH 5 29 29 HOH TIP B . P 9 HOH 6 74 74 HOH TIP B . P 9 HOH 7 76 76 HOH TIP B . P 9 HOH 8 78 78 HOH TIP B . P 9 HOH 9 154 154 HOH TIP B . P 9 HOH 10 164 164 HOH TIP B . # _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 dimeric _pdbx_struct_assembly.oligomeric_count 2 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P # loop_ _pdbx_struct_assembly_prop.biol_id _pdbx_struct_assembly_prop.type _pdbx_struct_assembly_prop.value _pdbx_struct_assembly_prop.details 1 'ABSA (A^2)' 3080 ? 1 MORE -106 ? 1 'SSA (A^2)' 10940 ? # _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_struct_conn_angle.id _pdbx_struct_conn_angle.ptnr1_label_atom_id _pdbx_struct_conn_angle.ptnr1_label_alt_id _pdbx_struct_conn_angle.ptnr1_label_asym_id _pdbx_struct_conn_angle.ptnr1_label_comp_id _pdbx_struct_conn_angle.ptnr1_label_seq_id _pdbx_struct_conn_angle.ptnr1_auth_atom_id _pdbx_struct_conn_angle.ptnr1_auth_asym_id _pdbx_struct_conn_angle.ptnr1_auth_comp_id _pdbx_struct_conn_angle.ptnr1_auth_seq_id _pdbx_struct_conn_angle.ptnr1_PDB_ins_code _pdbx_struct_conn_angle.ptnr1_symmetry _pdbx_struct_conn_angle.ptnr2_label_atom_id _pdbx_struct_conn_angle.ptnr2_label_alt_id _pdbx_struct_conn_angle.ptnr2_label_asym_id _pdbx_struct_conn_angle.ptnr2_label_comp_id _pdbx_struct_conn_angle.ptnr2_label_seq_id _pdbx_struct_conn_angle.ptnr2_auth_atom_id _pdbx_struct_conn_angle.ptnr2_auth_asym_id _pdbx_struct_conn_angle.ptnr2_auth_comp_id _pdbx_struct_conn_angle.ptnr2_auth_seq_id _pdbx_struct_conn_angle.ptnr2_PDB_ins_code _pdbx_struct_conn_angle.ptnr2_symmetry _pdbx_struct_conn_angle.ptnr3_label_atom_id _pdbx_struct_conn_angle.ptnr3_label_alt_id _pdbx_struct_conn_angle.ptnr3_label_asym_id _pdbx_struct_conn_angle.ptnr3_label_comp_id _pdbx_struct_conn_angle.ptnr3_label_seq_id _pdbx_struct_conn_angle.ptnr3_auth_atom_id _pdbx_struct_conn_angle.ptnr3_auth_asym_id _pdbx_struct_conn_angle.ptnr3_auth_comp_id _pdbx_struct_conn_angle.ptnr3_auth_seq_id _pdbx_struct_conn_angle.ptnr3_PDB_ins_code _pdbx_struct_conn_angle.ptnr3_symmetry _pdbx_struct_conn_angle.value _pdbx_struct_conn_angle.value_esd 1 OXT ? I ACT . ? A ACT 902 ? 1_555 ZN ? M ZN . ? A ZN 502 ? 1_555 NE2 ? A HIS 138 ? A HIS 156 ? 1_555 106.2 ? 2 OXT ? I ACT . ? A ACT 902 ? 1_555 ZN ? M ZN . ? A ZN 502 ? 1_555 O ? O HOH . ? A HOH 367 ? 1_555 101.0 ? 3 NE2 ? A HIS 138 ? A HIS 156 ? 1_555 ZN ? M ZN . ? A ZN 502 ? 1_555 O ? O HOH . ? A HOH 367 ? 1_555 103.9 ? 4 OXT ? I ACT . ? A ACT 902 ? 1_555 ZN ? M ZN . ? A ZN 502 ? 1_555 O ? O HOH . ? A HOH 368 ? 1_555 109.4 ? 5 NE2 ? A HIS 138 ? A HIS 156 ? 1_555 ZN ? M ZN . ? A ZN 502 ? 1_555 O ? O HOH . ? A HOH 368 ? 1_555 107.7 ? 6 O ? O HOH . ? A HOH 367 ? 1_555 ZN ? M ZN . ? A ZN 502 ? 1_555 O ? O HOH . ? A HOH 368 ? 1_555 126.9 ? 7 OXT ? I ACT . ? A ACT 902 ? 1_555 ZN ? M ZN . ? A ZN 502 ? 1_555 O ? O HOH . ? A HOH 150 ? 1_555 148.9 ? 8 NE2 ? A HIS 138 ? A HIS 156 ? 1_555 ZN ? M ZN . ? A ZN 502 ? 1_555 O ? O HOH . ? A HOH 150 ? 1_555 104.3 ? 9 O ? O HOH . ? A HOH 367 ? 1_555 ZN ? M ZN . ? A ZN 502 ? 1_555 O ? O HOH . ? A HOH 150 ? 1_555 65.7 ? 10 O ? O HOH . ? A HOH 368 ? 1_555 ZN ? M ZN . ? A ZN 502 ? 1_555 O ? O HOH . ? A HOH 150 ? 1_555 65.8 ? 11 OE2 ? A GLU 199 ? A GLU 218 ? 1_555 ZN ? L ZN . ? A ZN 501 ? 1_555 OXT ? H ACT . ? A ACT 901 ? 1_555 101.3 ? 12 OE2 ? A GLU 199 ? A GLU 218 ? 1_555 ZN ? L ZN . ? A ZN 501 ? 1_555 NE2 ? A HIS 177 ? A HIS 192 ? 1_555 105.6 ? 13 OXT ? H ACT . ? A ACT 901 ? 1_555 ZN ? L ZN . ? A ZN 501 ? 1_555 NE2 ? A HIS 177 ? A HIS 192 ? 1_555 114.1 ? 14 OE2 ? A GLU 199 ? A GLU 218 ? 1_555 ZN ? L ZN . ? A ZN 501 ? 1_555 O ? H ACT . ? A ACT 901 ? 1_555 151.7 ? 15 OXT ? H ACT . ? A ACT 901 ? 1_555 ZN ? L ZN . ? A ZN 501 ? 1_555 O ? H ACT . ? A ACT 901 ? 1_555 51.1 ? 16 NE2 ? A HIS 177 ? A HIS 192 ? 1_555 ZN ? L ZN . ? A ZN 501 ? 1_555 O ? H ACT . ? A ACT 901 ? 1_555 93.6 ? 17 O ? K ACT . ? A ACT 904 ? 1_555 ZN ? N ZN . ? A ZN 503 ? 1_555 OD1 ? A ASN 10 ? A ASN 25 ? 1_555 118.0 ? 18 O ? K ACT . ? A ACT 904 ? 1_555 ZN ? N ZN . ? A ZN 503 ? 1_555 NE2 ? A HIS 103 ? A HIS 117 ? 1_555 102.2 ? 19 OD1 ? A ASN 10 ? A ASN 25 ? 1_555 ZN ? N ZN . ? A ZN 503 ? 1_555 NE2 ? A HIS 103 ? A HIS 117 ? 1_555 103.8 ? 20 O ? K ACT . ? A ACT 904 ? 1_555 ZN ? N ZN . ? A ZN 503 ? 1_555 OXT ? J ACT . ? A ACT 903 ? 1_555 120.0 ? 21 OD1 ? A ASN 10 ? A ASN 25 ? 1_555 ZN ? N ZN . ? A ZN 503 ? 1_555 OXT ? J ACT . ? A ACT 903 ? 1_555 89.7 ? 22 NE2 ? A HIS 103 ? A HIS 117 ? 1_555 ZN ? N ZN . ? A ZN 503 ? 1_555 OXT ? J ACT . ? A ACT 903 ? 1_555 122.6 ? 23 O ? K ACT . ? A ACT 904 ? 1_555 ZN ? N ZN . ? A ZN 503 ? 1_555 O ? J ACT . ? A ACT 903 ? 1_555 86.9 ? 24 OD1 ? A ASN 10 ? A ASN 25 ? 1_555 ZN ? N ZN . ? A ZN 503 ? 1_555 O ? J ACT . ? A ACT 903 ? 1_555 142.7 ? 25 NE2 ? A HIS 103 ? A HIS 117 ? 1_555 ZN ? N ZN . ? A ZN 503 ? 1_555 O ? J ACT . ? A ACT 903 ? 1_555 96.6 ? 26 OXT ? J ACT . ? A ACT 903 ? 1_555 ZN ? N ZN . ? A ZN 503 ? 1_555 O ? J ACT . ? A ACT 903 ? 1_555 53.0 ? # 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 3S9C _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 ? # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 ASN A 48 ? ? -171.73 -179.24 2 1 HIS A 71 ? ? -122.52 -89.80 3 1 ALA A 214 ? ? -108.11 -68.53 # loop_ _pdbx_unobs_or_zero_occ_residues.id _pdbx_unobs_or_zero_occ_residues.PDB_model_num _pdbx_unobs_or_zero_occ_residues.polymer_flag _pdbx_unobs_or_zero_occ_residues.occupancy_flag _pdbx_unobs_or_zero_occ_residues.auth_asym_id _pdbx_unobs_or_zero_occ_residues.auth_comp_id _pdbx_unobs_or_zero_occ_residues.auth_seq_id _pdbx_unobs_or_zero_occ_residues.PDB_ins_code _pdbx_unobs_or_zero_occ_residues.label_asym_id _pdbx_unobs_or_zero_occ_residues.label_comp_id _pdbx_unobs_or_zero_occ_residues.label_seq_id 1 1 Y 1 B SER 1533 ? B SER 1 2 1 Y 1 B ARG 1534 ? B ARG 2 3 1 Y 1 B ASP 1535 ? B ASP 3 4 1 Y 1 B PRO 1536 ? B PRO 4 5 1 Y 1 B ASP 1537 ? B ASP 5 6 1 Y 1 B ASN 1538 ? B ASN 6 7 1 Y 1 B SER 1546 ? B SER 14 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 3 N-ACETYL-D-GLUCOSAMINE NAG 4 BETA-D-MANNOSE BMA 5 BETA-D-GLUCOSE BGC 6 ALPHA-D-GLUCOSE GLC 7 'ACETATE ION' ACT 8 'ZINC ION' ZN 9 water HOH #