data_1OP2 # _entry.id 1OP2 # _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 1OP2 RCSB RCSB018525 WWPDB D_1000018525 # _pdbx_database_related.db_name PDB _pdbx_database_related.db_id 1OP0 _pdbx_database_related.details 'The Crystal Structure of AaV-SP-I' _pdbx_database_related.content_type unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 1OP2 _pdbx_database_status.recvd_initial_deposition_date 2003-03-04 _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.pdb_format_compatible Y _pdbx_database_status.status_code_cs ? # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Zhu, Z.' 1 'Teng, M.' 2 'Niu, L.' 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 'Crystal Structures and Amidolytic Activities of Two Glycosylated Snake Venom Serine Proteinases' J.BIOL.CHEM. 280 10524 10529 2005 JBCHA3 US 0021-9258 0071 ? 15632114 10.1074/jbc.M412900200 1 ;Purification, N-terminal sequencing, partial characterization, crystallization and preliminary crystallographic analysis of two glycosylated serine proteinases from Agkistrodon acutus venom ; 'Acta Crystallogr.,Sect.D' 59 547 550 2003 ABCRE6 DK 0907-4449 0766 ? 12595722 10.1107/S0907444902023375 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Zhu, Z.' 1 primary 'Liang, Z.' 2 primary 'Zhang, T.' 3 primary 'Zhu, Z.' 4 primary 'Xu, W.' 5 primary 'Teng, M.' 6 primary 'Niu, L.' 7 1 'Zhu, Z.' 8 1 'Gong, P.' 9 1 'Teng, M.' 10 1 'Niu, L.' 11 # _cell.entry_id 1OP2 _cell.length_a 119.430 _cell.length_b 42.830 _cell.length_c 44.940 _cell.angle_alpha 90.00 _cell.angle_beta 99.61 _cell.angle_gamma 90.00 _cell.Z_PDB 4 _cell.pdbx_unique_axis ? # _symmetry.entry_id 1OP2 _symmetry.space_group_name_H-M 'C 1 2 1' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 5 _symmetry.space_group_name_Hall ? # loop_ _entity.id _entity.type _entity.src_method _entity.pdbx_description _entity.formula_weight _entity.pdbx_number_of_molecules _entity.pdbx_ec _entity.pdbx_mutation _entity.pdbx_fragment _entity.details 1 polymer nat 'Venom serine proteinase' 25356.693 1 3.4.21.- ? ? ? 2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 1 ? ? ? ? 3 non-polymer syn 'SULFATE ION' 96.063 1 ? ? ? ? 4 water nat water 18.015 143 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name 'snake venom serine proteinase, AaV-SP-I' # _entity_poly.entity_id 1 _entity_poly.type 'polypeptide(L)' _entity_poly.nstd_linkage no _entity_poly.nstd_monomer no _entity_poly.pdbx_seq_one_letter_code ;VIGGNECDINEHRFLVAFFNTTGFFCGGTLINPEWVVTAAHCDSTNFQMQLGVHSKKVLNEDEQTRNPKEKFICPNKNNN EVLDKDIMLIKLDKPISNSKHIAPLSLPSSPPSVGSVCRIMGWGSITPVKETFPDVPYCANINLLDHAVCQAGYPELLAE YRTLCAGIVQGGKDTCGGDSGGPLICNGQFQGIVSYGAHPCGQGPKPGIYTNVFDYTDWIQRNIAGNTDATCPP ; _entity_poly.pdbx_seq_one_letter_code_can ;VIGGNECDINEHRFLVAFFNTTGFFCGGTLINPEWVVTAAHCDSTNFQMQLGVHSKKVLNEDEQTRNPKEKFICPNKNNN EVLDKDIMLIKLDKPISNSKHIAPLSLPSSPPSVGSVCRIMGWGSITPVKETFPDVPYCANINLLDHAVCQAGYPELLAE YRTLCAGIVQGGKDTCGGDSGGPLICNGQFQGIVSYGAHPCGQGPKPGIYTNVFDYTDWIQRNIAGNTDATCPP ; _entity_poly.pdbx_strand_id A _entity_poly.pdbx_target_identifier ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 VAL n 1 2 ILE n 1 3 GLY n 1 4 GLY n 1 5 ASN n 1 6 GLU n 1 7 CYS n 1 8 ASP n 1 9 ILE n 1 10 ASN n 1 11 GLU n 1 12 HIS n 1 13 ARG n 1 14 PHE n 1 15 LEU n 1 16 VAL n 1 17 ALA n 1 18 PHE n 1 19 PHE n 1 20 ASN n 1 21 THR n 1 22 THR n 1 23 GLY n 1 24 PHE n 1 25 PHE n 1 26 CYS n 1 27 GLY n 1 28 GLY n 1 29 THR n 1 30 LEU n 1 31 ILE n 1 32 ASN n 1 33 PRO n 1 34 GLU n 1 35 TRP n 1 36 VAL n 1 37 VAL n 1 38 THR n 1 39 ALA n 1 40 ALA n 1 41 HIS n 1 42 CYS n 1 43 ASP n 1 44 SER n 1 45 THR n 1 46 ASN n 1 47 PHE n 1 48 GLN n 1 49 MET n 1 50 GLN n 1 51 LEU n 1 52 GLY n 1 53 VAL n 1 54 HIS n 1 55 SER n 1 56 LYS n 1 57 LYS n 1 58 VAL n 1 59 LEU n 1 60 ASN n 1 61 GLU n 1 62 ASP n 1 63 GLU n 1 64 GLN n 1 65 THR n 1 66 ARG n 1 67 ASN n 1 68 PRO n 1 69 LYS n 1 70 GLU n 1 71 LYS n 1 72 PHE n 1 73 ILE n 1 74 CYS n 1 75 PRO n 1 76 ASN n 1 77 LYS n 1 78 ASN n 1 79 ASN n 1 80 ASN n 1 81 GLU n 1 82 VAL n 1 83 LEU n 1 84 ASP n 1 85 LYS n 1 86 ASP n 1 87 ILE n 1 88 MET n 1 89 LEU n 1 90 ILE n 1 91 LYS n 1 92 LEU n 1 93 ASP n 1 94 LYS n 1 95 PRO n 1 96 ILE n 1 97 SER n 1 98 ASN n 1 99 SER n 1 100 LYS n 1 101 HIS n 1 102 ILE n 1 103 ALA n 1 104 PRO n 1 105 LEU n 1 106 SER n 1 107 LEU n 1 108 PRO n 1 109 SER n 1 110 SER n 1 111 PRO n 1 112 PRO n 1 113 SER n 1 114 VAL n 1 115 GLY n 1 116 SER n 1 117 VAL n 1 118 CYS n 1 119 ARG n 1 120 ILE n 1 121 MET n 1 122 GLY n 1 123 TRP n 1 124 GLY n 1 125 SER n 1 126 ILE n 1 127 THR n 1 128 PRO n 1 129 VAL n 1 130 LYS n 1 131 GLU n 1 132 THR n 1 133 PHE n 1 134 PRO n 1 135 ASP n 1 136 VAL n 1 137 PRO n 1 138 TYR n 1 139 CYS n 1 140 ALA n 1 141 ASN n 1 142 ILE n 1 143 ASN n 1 144 LEU n 1 145 LEU n 1 146 ASP n 1 147 HIS n 1 148 ALA n 1 149 VAL n 1 150 CYS n 1 151 GLN n 1 152 ALA n 1 153 GLY n 1 154 TYR n 1 155 PRO n 1 156 GLU n 1 157 LEU n 1 158 LEU n 1 159 ALA n 1 160 GLU n 1 161 TYR 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 VAL n 1 170 GLN n 1 171 GLY n 1 172 GLY n 1 173 LYS n 1 174 ASP n 1 175 THR n 1 176 CYS n 1 177 GLY 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 GLN n 1 190 PHE n 1 191 GLN n 1 192 GLY n 1 193 ILE n 1 194 VAL n 1 195 SER n 1 196 TYR n 1 197 GLY n 1 198 ALA n 1 199 HIS n 1 200 PRO n 1 201 CYS n 1 202 GLY n 1 203 GLN n 1 204 GLY n 1 205 PRO n 1 206 LYS n 1 207 PRO n 1 208 GLY n 1 209 ILE n 1 210 TYR n 1 211 THR n 1 212 ASN n 1 213 VAL n 1 214 PHE n 1 215 ASP n 1 216 TYR n 1 217 THR n 1 218 ASP n 1 219 TRP n 1 220 ILE n 1 221 GLN n 1 222 ARG n 1 223 ASN n 1 224 ILE n 1 225 ALA n 1 226 GLY n 1 227 ASN n 1 228 THR n 1 229 ASP n 1 230 ALA n 1 231 THR n 1 232 CYS n 1 233 PRO n 1 234 PRO n # _entity_src_nat.entity_id 1 _entity_src_nat.pdbx_src_id 1 _entity_src_nat.pdbx_alt_source_flag sample _entity_src_nat.pdbx_beg_seq_num ? _entity_src_nat.pdbx_end_seq_num ? _entity_src_nat.common_name 'Chinese moccasin' _entity_src_nat.pdbx_organism_scientific 'Deinagkistrodon acutus' _entity_src_nat.pdbx_ncbi_taxonomy_id 36307 _entity_src_nat.genus Deinagkistrodon _entity_src_nat.species ? _entity_src_nat.strain ? _entity_src_nat.tissue ? _entity_src_nat.tissue_fraction ? _entity_src_nat.pdbx_secretion 'venom gland' _entity_src_nat.pdbx_fragment ? _entity_src_nat.pdbx_variant ? _entity_src_nat.pdbx_cell_line ? _entity_src_nat.pdbx_atcc ? _entity_src_nat.pdbx_cellular_location ? _entity_src_nat.pdbx_organ ? _entity_src_nat.pdbx_organelle ? _entity_src_nat.pdbx_cell ? _entity_src_nat.pdbx_plasmid_name ? _entity_src_nat.pdbx_plasmid_details ? _entity_src_nat.details ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code VSP2_AGKAC _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ;VIGGNECDINEHRFLVAFFNTTGFFCGGTLINPEWVVTAAHCDSTNFQMQLGVHSKKVLNEDEQTRNPKEKFICPNKNNN EVLDKDIMLIKLDKPISNSKHIAPLSLPSSPPSVGSVCRIMGWGSITPVKETFPDVPYCANINLLDHAVCQAGYPELLAE YRTLCAGIVQGGKDTCGGDSGGPLICNGQFQGIVSYGAHPCGQGPKPGIYTNVFDYTDWIQRNIAGNTDATCPP ; _struct_ref.pdbx_align_begin 25 _struct_ref.pdbx_db_accession Q9I8X1 _struct_ref.pdbx_db_isoform ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 1OP2 _struct_ref_seq.pdbx_strand_id A _struct_ref_seq.seq_align_beg 1 _struct_ref_seq.pdbx_seq_align_beg_ins_code ? _struct_ref_seq.seq_align_end 234 _struct_ref_seq.pdbx_seq_align_end_ins_code G _struct_ref_seq.pdbx_db_accession Q9I8X1 _struct_ref_seq.db_align_beg 25 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 258 _struct_ref_seq.pdbx_db_align_end_ins_code ? _struct_ref_seq.pdbx_auth_seq_align_beg 16 _struct_ref_seq.pdbx_auth_seq_align_end 245 # loop_ _chem_comp.id _chem_comp.type _chem_comp.mon_nstd_flag _chem_comp.name _chem_comp.pdbx_synonyms _chem_comp.formula _chem_comp.formula_weight ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 SO4 non-polymer . 'SULFATE ION' ? 'O4 S -2' 96.063 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 # _exptl.entry_id 1OP2 _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.09 _exptl_crystal.density_percent_sol 40.64 _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.preparation ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method 'VAPOR DIFFUSION, HANGING DROP' _exptl_crystal_grow.temp 298 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH ? _exptl_crystal_grow.pdbx_details 'ammonium sulfate, PEG 4000, VAPOR DIFFUSION, HANGING DROP, temperature 298K' _exptl_crystal_grow.pdbx_pH_range . # _diffrn.id 1 _diffrn.ambient_temp 298 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector 'IMAGE PLATE' _diffrn_detector.type MARRESEARCH _diffrn_detector.pdbx_collection_date ? _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator GRAPHITE _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 1.5418 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source 'SEALED TUBE' _diffrn_source.type ? _diffrn_source.pdbx_synchrotron_site ? _diffrn_source.pdbx_synchrotron_beamline ? _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_wavelength_list 1.5418 # _reflns.entry_id 1OP2 _reflns.observed_criterion_sigma_I 0.00 _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 20.00 _reflns.d_resolution_high 2.10 _reflns.number_obs 12259 _reflns.number_all 12259 _reflns.percent_possible_obs 92.3 _reflns.pdbx_Rmerge_I_obs ? _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI ? _reflns.B_iso_Wilson_estimate 8.3 _reflns.pdbx_redundancy ? _reflns.R_free_details ? _reflns.limit_h_max ? _reflns.limit_h_min ? _reflns.limit_k_max ? _reflns.limit_k_min ? _reflns.limit_l_max ? _reflns.limit_l_min ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? _reflns.pdbx_ordinal 1 _reflns.pdbx_diffrn_id 1 # _reflns_shell.d_res_high 2.10 _reflns_shell.d_res_low 2.15 _reflns_shell.percent_possible_all 79.1 _reflns_shell.Rmerge_I_obs ? _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs ? _reflns_shell.pdbx_redundancy ? _reflns_shell.percent_possible_obs ? _reflns_shell.number_unique_all ? _reflns_shell.number_measured_all ? _reflns_shell.number_measured_obs ? _reflns_shell.number_unique_obs ? _reflns_shell.pdbx_chi_squared ? _reflns_shell.pdbx_ordinal 1 _reflns_shell.pdbx_diffrn_id 1 # _refine.entry_id 1OP2 _refine.ls_number_reflns_obs 11866 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F 0.0 _refine.pdbx_data_cutoff_high_absF 3881980.15 _refine.pdbx_data_cutoff_low_absF 0.000000 _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 19.90 _refine.ls_d_res_high 2.10 _refine.ls_percent_reflns_obs 89.3 _refine.ls_R_factor_obs 0.165 _refine.ls_R_factor_all 0.169 _refine.ls_R_factor_R_work 0.165 _refine.ls_R_factor_R_free 0.211 _refine.ls_R_factor_R_free_error 0.006 _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 10.3 _refine.ls_number_reflns_R_free 1222 _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 20.3 _refine.aniso_B[1][1] -2.15 _refine.aniso_B[2][2] 6.62 _refine.aniso_B[3][3] -4.47 _refine.aniso_B[1][2] 0.00 _refine.aniso_B[1][3] -0.88 _refine.aniso_B[2][3] 0.00 _refine.solvent_model_details 'FLAT MODEL' _refine.solvent_model_param_ksol 0.325442 _refine.solvent_model_param_bsol 45.9892 _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 ? _refine.pdbx_starting_model ? _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 ? _refine.pdbx_overall_ESU_R_Free ? _refine.overall_SU_ML ? _refine.overall_SU_B ? _refine.ls_redundancy_reflns_obs ? _refine.B_iso_min ? _refine.B_iso_max ? _refine.overall_SU_R_Cruickshank_DPI ? _refine.overall_SU_R_free ? _refine.ls_wR_factor_R_free ? _refine.ls_wR_factor_R_work ? _refine.overall_FOM_free_R_set ? _refine.overall_FOM_work_R_set ? _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.pdbx_overall_phase_error ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_analyze.entry_id 1OP2 _refine_analyze.Luzzati_coordinate_error_obs 0.20 _refine_analyze.Luzzati_sigma_a_obs 0.17 _refine_analyze.Luzzati_d_res_low_obs 5.00 _refine_analyze.Luzzati_coordinate_error_free 0.26 _refine_analyze.Luzzati_sigma_a_free 0.25 _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 1776 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 19 _refine_hist.number_atoms_solvent 143 _refine_hist.number_atoms_total 1938 _refine_hist.d_res_high 2.10 _refine_hist.d_res_low 19.90 # loop_ _refine_ls_restr.type _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.number _refine_ls_restr.pdbx_refine_id _refine_ls_restr.pdbx_restraint_function c_bond_d 0.005 ? ? ? 'X-RAY DIFFRACTION' ? c_angle_deg 1.3 ? ? ? 'X-RAY DIFFRACTION' ? c_dihedral_angle_d 25.2 ? ? ? 'X-RAY DIFFRACTION' ? c_improper_angle_d 0.79 ? ? ? 'X-RAY DIFFRACTION' ? c_mcbond_it 1.33 1.50 ? ? 'X-RAY DIFFRACTION' ? c_mcangle_it 2.07 2.00 ? ? 'X-RAY DIFFRACTION' ? c_scbond_it 2.05 2.00 ? ? 'X-RAY DIFFRACTION' ? c_scangle_it 3.03 2.50 ? ? 'X-RAY DIFFRACTION' ? # _refine_ls_shell.pdbx_total_number_of_bins_used 6 _refine_ls_shell.d_res_high 2.10 _refine_ls_shell.d_res_low 2.23 _refine_ls_shell.number_reflns_R_work 1578 _refine_ls_shell.R_factor_R_work 0.205 _refine_ls_shell.percent_reflns_obs 79.6 _refine_ls_shell.R_factor_R_free 0.254 _refine_ls_shell.R_factor_R_free_error 0.019 _refine_ls_shell.percent_reflns_R_free 10.2 _refine_ls_shell.number_reflns_R_free 179 _refine_ls_shell.number_reflns_obs ? _refine_ls_shell.redundancy_reflns_obs ? _refine_ls_shell.number_reflns_all ? _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_ls_shell.R_factor_all ? # loop_ _pdbx_xplor_file.serial_no _pdbx_xplor_file.param_file _pdbx_xplor_file.topol_file _pdbx_xplor_file.pdbx_refine_id 1 PROTEIN_REP.PARAM PROTEIN.TOP 'X-RAY DIFFRACTION' 2 WATER_REP.PARAM WATER.TOP 'X-RAY DIFFRACTION' 3 CARBOHYDRATE.PARAM CARBOHYDRATE.TOP 'X-RAY DIFFRACTION' 4 ION.PARAM ION.TOP 'X-RAY DIFFRACTION' # _struct.entry_id 1OP2 _struct.title 'Crystal Structure of AaV-SP-II, a Glycosylated Snake Venom Serine Proteinase from Agkistrodon acutus' _struct.pdbx_descriptor 'Venom serine proteinase(E.C.3.4.21.-)' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 1OP2 _struct_keywords.pdbx_keywords HYDROLASE _struct_keywords.text 'snake venom, serine proteinase, glycoprotein, Agkistrodon acutus, hydrolase' # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 3 ? D N N 4 ? # _struct_biol.id 1 _struct_biol.pdbx_parent_biol_id ? _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 39 ? ASP A 43 ? ALA A 55 ASP A 59 5 ? 5 HELX_P HELX_P2 2 ASP A 146 ? TYR A 154 ? ASP A 164 TYR A 172 1 ? 9 HELX_P HELX_P3 3 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 ? ? ? ? ? ? ? 2.028 ? disulf2 disulf ? ? A CYS 26 SG ? ? ? 1_555 A CYS 42 SG ? ? A CYS 42 A CYS 58 1_555 ? ? ? ? ? ? ? 2.029 ? disulf3 disulf ? ? A CYS 74 SG ? ? ? 1_555 A CYS 232 SG ? E A CYS 91 A CYS 245 1_555 ? ? ? ? ? ? ? 2.025 ? disulf4 disulf ? ? A CYS 118 SG ? ? ? 1_555 A CYS 186 SG ? ? A CYS 136 A CYS 201 1_555 ? ? ? ? ? ? ? 2.029 ? 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 ? ? ? ? ? ? ? 2.033 ? covale1 covale ? ? A ASN 20 ND2 ? ? ? 1_555 B NAG . C1 ? ? A ASN 35 A NAG 301 1_555 ? ? ? ? ? ? ? 1.451 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? # _struct_mon_prot_cis.pdbx_id 1 _struct_mon_prot_cis.label_comp_id HIS _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 HIS _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 -0.14 # 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 ASN A 5 ? GLU A 6 ? ASN A 20 GLU A 21 A 2 TYR A 138 ? LEU A 145 ? TYR A 156 LEU A 163 A 3 VAL A 117 ? GLY A 122 ? VAL A 135 GLY A 140 A 4 PRO A 183 ? CYS A 186 ? PRO A 198 CYS A 201 A 5 GLN A 189 ? TYR A 196 ? GLN A 208 TYR A 215 A 6 GLY A 208 ? ASN A 212 ? GLY A 226 ASN A 230 A 7 THR A 163 ? GLY A 167 ? THR A 180 GLY A 184 A 8 TYR A 138 ? LEU A 145 ? TYR A 156 LEU A 163 B 1 GLN A 64 ? ARG A 66 ? GLN A 81 ARG A 83 B 2 GLN A 48 ? LEU A 51 ? GLN A 65 LEU A 68 B 3 LEU A 15 ? ASN A 20 ? LEU A 30 ASN A 35 B 4 GLY A 23 ? ASN A 32 ? GLY A 39 ASN A 48 B 5 TRP A 35 ? THR A 38 ? TRP A 51 THR A 54 B 6 MET A 88 ? LEU A 92 ? MET A 104 LEU A 108 B 7 PRO A 68 ? ILE A 73 ? PRO A 85 ILE A 90 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id A 1 2 O ASN A 5 ? O ASN A 20 N CYS A 139 ? N CYS A 157 A 2 3 O ILE A 142 ? O ILE A 160 N CYS A 118 ? N CYS A 136 A 3 4 N MET A 121 ? N MET A 139 O PRO A 183 ? O PRO A 198 A 4 5 O CYS A 186 ? O CYS A 201 N GLN A 189 ? N GLN A 208 A 5 6 O TYR A 196 ? O TYR A 215 N ILE A 209 ? N ILE A 227 A 6 7 O TYR A 210 ? O TYR A 228 N LEU A 164 ? N LEU A 181 A 7 8 N GLY A 167 ? N GLY A 184 O ASN A 143 ? O ASN A 161 B 1 2 N ARG A 66 ? N ARG A 83 O MET A 49 ? O MET A 66 B 2 3 N GLN A 50 ? N GLN A 67 O ALA A 17 ? O ALA A 32 B 3 4 O ASN A 20 ? O ASN A 35 N GLY A 23 ? N GLY A 39 B 4 5 N ILE A 31 ? N ILE A 47 O TRP A 35 ? O TRP A 51 B 5 6 O THR A 38 ? O THR A 54 N MET A 88 ? N MET A 104 B 6 7 O LYS A 91 ? O LYS A 107 N LYS A 69 ? N LYS A 86 # loop_ _struct_site.id _struct_site.pdbx_evidence_code _struct_site.pdbx_auth_asym_id _struct_site.pdbx_auth_comp_id _struct_site.pdbx_auth_seq_id _struct_site.pdbx_auth_ins_code _struct_site.pdbx_num_residues _struct_site.details AC1 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE NAG A 301' AC2 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE SO4 A 401' # loop_ _struct_site_gen.id _struct_site_gen.site_id _struct_site_gen.pdbx_num_res _struct_site_gen.label_comp_id _struct_site_gen.label_asym_id _struct_site_gen.label_seq_id _struct_site_gen.pdbx_auth_ins_code _struct_site_gen.auth_comp_id _struct_site_gen.auth_asym_id _struct_site_gen.auth_seq_id _struct_site_gen.label_atom_id _struct_site_gen.label_alt_id _struct_site_gen.symmetry _struct_site_gen.details 1 AC1 6 ASN A 20 ? ASN A 35 . ? 1_555 ? 2 AC1 6 THR A 21 ? THR A 36 . ? 1_555 ? 3 AC1 6 THR A 22 ? THR A 38 . ? 1_555 ? 4 AC1 6 PHE A 25 ? PHE A 41 . ? 1_555 ? 5 AC1 6 HOH D . ? HOH A 693 . ? 1_555 ? 6 AC1 6 HOH D . ? HOH A 706 . ? 1_555 ? 7 AC2 4 ARG A 13 ? ARG A 28 . ? 1_555 ? 8 AC2 4 ASN A 98 ? ASN A 114 . ? 1_555 ? 9 AC2 4 LYS A 130 ? LYS A 148 . ? 1_565 ? 10 AC2 4 HOH D . ? HOH A 712 . ? 1_555 ? # _database_PDB_matrix.entry_id 1OP2 _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 1OP2 _atom_sites.fract_transf_matrix[1][1] 0.008373 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.001418 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.023348 _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] 0.022569 _atom_sites.fract_transf_vector[1] 0.00000 _atom_sites.fract_transf_vector[2] 0.00000 _atom_sites.fract_transf_vector[3] 0.00000 # loop_ _atom_type.symbol C N O S # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 N N . VAL A 1 1 ? 40.958 -9.117 2.289 1.00 11.11 ? 16 VAL A N 1 ATOM 2 C CA . VAL A 1 1 ? 39.545 -8.939 1.863 1.00 11.59 ? 16 VAL A CA 1 ATOM 3 C C . VAL A 1 1 ? 39.125 -10.040 0.899 1.00 14.64 ? 16 VAL A C 1 ATOM 4 O O . VAL A 1 1 ? 39.833 -10.343 -0.063 1.00 15.76 ? 16 VAL A O 1 ATOM 5 C CB . VAL A 1 1 ? 39.341 -7.574 1.191 1.00 11.49 ? 16 VAL A CB 1 ATOM 6 C CG1 . VAL A 1 1 ? 37.928 -7.467 0.655 1.00 10.05 ? 16 VAL A CG1 1 ATOM 7 C CG2 . VAL A 1 1 ? 39.598 -6.463 2.203 1.00 10.33 ? 16 VAL A CG2 1 ATOM 8 N N . ILE A 1 2 ? 37.965 -10.632 1.176 1.00 14.97 ? 17 ILE A N 1 ATOM 9 C CA . ILE A 1 2 ? 37.404 -11.719 0.375 1.00 15.72 ? 17 ILE A CA 1 ATOM 10 C C . ILE A 1 2 ? 36.262 -11.220 -0.510 1.00 15.54 ? 17 ILE A C 1 ATOM 11 O O . ILE A 1 2 ? 35.527 -10.308 -0.131 1.00 15.05 ? 17 ILE A O 1 ATOM 12 C CB . ILE A 1 2 ? 36.852 -12.838 1.297 1.00 17.30 ? 17 ILE A CB 1 ATOM 13 C CG1 . ILE A 1 2 ? 37.971 -13.383 2.182 1.00 19.17 ? 17 ILE A CG1 1 ATOM 14 C CG2 . ILE A 1 2 ? 36.241 -13.950 0.475 1.00 21.50 ? 17 ILE A CG2 1 ATOM 15 C CD1 . ILE A 1 2 ? 39.095 -14.022 1.412 1.00 19.63 ? 17 ILE A CD1 1 ATOM 16 N N . GLY A 1 3 ? 36.118 -11.815 -1.689 1.00 14.64 ? 18 GLY A N 1 ATOM 17 C CA . GLY A 1 3 ? 35.043 -11.425 -2.587 1.00 15.77 ? 18 GLY A CA 1 ATOM 18 C C . GLY A 1 3 ? 35.090 -10.010 -3.144 1.00 16.93 ? 18 GLY A C 1 ATOM 19 O O . GLY A 1 3 ? 34.054 -9.440 -3.499 1.00 17.81 ? 18 GLY A O 1 ATOM 20 N N . GLY A 1 4 ? 36.281 -9.432 -3.227 1.00 14.56 ? 19 GLY A N 1 ATOM 21 C CA . GLY A 1 4 ? 36.390 -8.089 -3.757 1.00 14.68 ? 19 GLY A CA 1 ATOM 22 C C . GLY A 1 4 ? 37.217 -8.041 -5.026 1.00 15.37 ? 19 GLY A C 1 ATOM 23 O O . GLY A 1 4 ? 37.473 -9.062 -5.661 1.00 13.47 ? 19 GLY A O 1 ATOM 24 N N . ASN A 1 5 ? 37.626 -6.840 -5.401 1.00 16.45 ? 20 ASN A N 1 ATOM 25 C CA . ASN A 1 5 ? 38.443 -6.628 -6.583 1.00 17.86 ? 20 ASN A CA 1 ATOM 26 C C . ASN A 1 5 ? 39.511 -5.633 -6.169 1.00 17.38 ? 20 ASN A C 1 ATOM 27 O O . ASN A 1 5 ? 39.394 -4.993 -5.129 1.00 17.47 ? 20 ASN A O 1 ATOM 28 C CB . ASN A 1 5 ? 37.615 -6.020 -7.724 1.00 23.58 ? 20 ASN A CB 1 ATOM 29 C CG . ASN A 1 5 ? 36.603 -6.992 -8.314 1.00 29.11 ? 20 ASN A CG 1 ATOM 30 O OD1 . ASN A 1 5 ? 36.967 -8.047 -8.841 1.00 31.91 ? 20 ASN A OD1 1 ATOM 31 N ND2 . ASN A 1 5 ? 35.322 -6.636 -8.232 1.00 32.20 ? 20 ASN A ND2 1 ATOM 32 N N . GLU A 1 6 ? 40.545 -5.494 -6.985 1.00 16.00 ? 21 GLU A N 1 ATOM 33 C CA . GLU A 1 6 ? 41.611 -4.557 -6.685 1.00 15.99 ? 21 GLU A CA 1 ATOM 34 C C . GLU A 1 6 ? 41.001 -3.167 -6.536 1.00 14.79 ? 21 GLU A C 1 ATOM 35 O O . GLU A 1 6 ? 40.197 -2.752 -7.365 1.00 14.76 ? 21 GLU A O 1 ATOM 36 C CB . GLU A 1 6 ? 42.630 -4.542 -7.824 1.00 16.81 ? 21 GLU A CB 1 ATOM 37 C CG . GLU A 1 6 ? 43.845 -3.681 -7.544 1.00 19.66 ? 21 GLU A CG 1 ATOM 38 C CD . GLU A 1 6 ? 44.747 -3.511 -8.754 1.00 20.38 ? 21 GLU A CD 1 ATOM 39 O OE1 . GLU A 1 6 ? 44.772 -4.411 -9.619 1.00 17.16 ? 21 GLU A OE1 1 ATOM 40 O OE2 . GLU A 1 6 ? 45.441 -2.476 -8.819 1.00 22.37 ? 21 GLU A OE2 1 ATOM 41 N N . CYS A 1 7 ? 41.369 -2.451 -5.481 1.00 13.52 ? 22 CYS A N 1 ATOM 42 C CA . CYS A 1 7 ? 40.844 -1.105 -5.277 1.00 12.59 ? 22 CYS A CA 1 ATOM 43 C C . CYS A 1 7 ? 41.380 -0.181 -6.355 1.00 13.67 ? 22 CYS A C 1 ATOM 44 O O . CYS A 1 7 ? 42.423 -0.448 -6.955 1.00 14.40 ? 22 CYS A O 1 ATOM 45 C CB . CYS A 1 7 ? 41.305 -0.521 -3.948 1.00 10.64 ? 22 CYS A CB 1 ATOM 46 S SG . CYS A 1 7 ? 40.905 -1.424 -2.427 1.00 12.35 ? 22 CYS A SG 1 ATOM 47 N N . ASP A 1 8 ? 40.688 0.930 -6.569 1.00 14.48 ? 23 ASP A N 1 ATOM 48 C CA . ASP A 1 8 ? 41.136 1.906 -7.553 1.00 16.62 ? 23 ASP A CA 1 ATOM 49 C C . ASP A 1 8 ? 42.389 2.580 -7.002 1.00 16.70 ? 23 ASP A C 1 ATOM 50 O O . ASP A 1 8 ? 42.512 2.777 -5.796 1.00 16.99 ? 23 ASP A O 1 ATOM 51 C CB . ASP A 1 8 ? 40.066 2.966 -7.789 1.00 18.63 ? 23 ASP A CB 1 ATOM 52 C CG . ASP A 1 8 ? 40.484 3.984 -8.829 1.00 23.20 ? 23 ASP A CG 1 ATOM 53 O OD1 . ASP A 1 8 ? 40.522 3.626 -10.022 1.00 26.48 ? 23 ASP A OD1 1 ATOM 54 O OD2 . ASP A 1 8 ? 40.790 5.127 -8.444 1.00 24.42 ? 23 ASP A OD2 1 ATOM 55 N N . ILE A 1 9 ? 43.302 2.949 -7.895 1.00 16.26 ? 24 ILE A N 1 ATOM 56 C CA . ILE A 1 9 ? 44.554 3.582 -7.510 1.00 15.79 ? 24 ILE A CA 1 ATOM 57 C C . ILE A 1 9 ? 44.368 4.875 -6.716 1.00 15.51 ? 24 ILE A C 1 ATOM 58 O O . ILE A 1 9 ? 45.201 5.205 -5.872 1.00 13.79 ? 24 ILE A O 1 ATOM 59 C CB . ILE A 1 9 ? 45.427 3.868 -8.768 1.00 18.81 ? 24 ILE A CB 1 ATOM 60 C CG1 . ILE A 1 9 ? 46.812 4.364 -8.358 1.00 21.25 ? 24 ILE A CG1 1 ATOM 61 C CG2 . ILE A 1 9 ? 44.767 4.926 -9.646 1.00 19.57 ? 24 ILE A CG2 1 ATOM 62 C CD1 . ILE A 1 9 ? 47.654 3.328 -7.682 1.00 22.34 ? 24 ILE A CD1 1 ATOM 63 N N . ASN A 1 10 ? 43.271 5.591 -6.959 1.00 14.92 ? 25 ASN A N 1 ATOM 64 C CA . ASN A 1 10 ? 43.025 6.864 -6.274 1.00 16.21 ? 25 ASN A CA 1 ATOM 65 C C . ASN A 1 10 ? 41.920 6.907 -5.217 1.00 15.83 ? 25 ASN A C 1 ATOM 66 O O . ASN A 1 10 ? 41.574 7.988 -4.747 1.00 15.25 ? 25 ASN A O 1 ATOM 67 C CB . ASN A 1 10 ? 42.737 7.962 -7.304 1.00 19.79 ? 25 ASN A CB 1 ATOM 68 C CG . ASN A 1 10 ? 43.897 8.195 -8.253 1.00 22.19 ? 25 ASN A CG 1 ATOM 69 O OD1 . ASN A 1 10 ? 44.968 8.644 -7.848 1.00 25.25 ? 25 ASN A OD1 1 ATOM 70 N ND2 . ASN A 1 10 ? 43.689 7.883 -9.526 1.00 26.14 ? 25 ASN A ND2 1 ATOM 71 N N . GLU A 1 11 ? 41.372 5.763 -4.821 1.00 14.03 ? 26 GLU A N 1 ATOM 72 C CA . GLU A 1 11 ? 40.295 5.783 -3.828 1.00 14.80 ? 26 GLU A CA 1 ATOM 73 C C . GLU A 1 11 ? 40.700 5.499 -2.374 1.00 14.91 ? 26 GLU A C 1 ATOM 74 O O . GLU A 1 11 ? 39.829 5.410 -1.505 1.00 17.57 ? 26 GLU A O 1 ATOM 75 C CB . GLU A 1 11 ? 39.197 4.790 -4.222 1.00 14.72 ? 26 GLU A CB 1 ATOM 76 C CG . GLU A 1 11 ? 39.582 3.329 -3.995 1.00 13.65 ? 26 GLU A CG 1 ATOM 77 C CD . GLU A 1 11 ? 38.423 2.380 -4.239 1.00 13.88 ? 26 GLU A CD 1 ATOM 78 O OE1 . GLU A 1 11 ? 37.391 2.505 -3.545 1.00 13.21 ? 26 GLU A OE1 1 ATOM 79 O OE2 . GLU A 1 11 ? 38.543 1.507 -5.124 1.00 14.60 ? 26 GLU A OE2 1 ATOM 80 N N . HIS A 1 12 ? 41.996 5.352 -2.099 1.00 11.20 ? 27 HIS A N 1 ATOM 81 C CA . HIS A 1 12 ? 42.428 5.056 -0.732 1.00 9.87 ? 27 HIS A CA 1 ATOM 82 C C . HIS A 1 12 ? 43.643 5.859 -0.289 1.00 9.76 ? 27 HIS A C 1 ATOM 83 O O . HIS A 1 12 ? 44.580 5.312 0.279 1.00 8.69 ? 27 HIS A O 1 ATOM 84 C CB . HIS A 1 12 ? 42.708 3.554 -0.590 1.00 8.59 ? 27 HIS A CB 1 ATOM 85 C CG . HIS A 1 12 ? 43.791 3.045 -1.493 1.00 8.68 ? 27 HIS A CG 1 ATOM 86 N ND1 . HIS A 1 12 ? 45.130 3.141 -1.181 1.00 9.93 ? 27 HIS A ND1 1 ATOM 87 C CD2 . HIS A 1 12 ? 43.731 2.439 -2.703 1.00 7.96 ? 27 HIS A CD2 1 ATOM 88 C CE1 . HIS A 1 12 ? 45.849 2.614 -2.158 1.00 8.59 ? 27 HIS A CE1 1 ATOM 89 N NE2 . HIS A 1 12 ? 45.025 2.180 -3.093 1.00 6.53 ? 27 HIS A NE2 1 ATOM 90 N N . ARG A 1 13 ? 43.606 7.166 -0.539 1.00 9.78 ? 28 ARG A N 1 ATOM 91 C CA . ARG A 1 13 ? 44.708 8.065 -0.194 1.00 11.60 ? 28 ARG A CA 1 ATOM 92 C C . ARG A 1 13 ? 44.966 8.160 1.314 1.00 11.80 ? 28 ARG A C 1 ATOM 93 O O . ARG A 1 13 ? 46.040 8.582 1.746 1.00 11.51 ? 28 ARG A O 1 ATOM 94 C CB . ARG A 1 13 ? 44.414 9.460 -0.753 1.00 10.78 ? 28 ARG A CB 1 ATOM 95 C CG . ARG A 1 13 ? 44.106 9.466 -2.253 1.00 13.34 ? 28 ARG A CG 1 ATOM 96 C CD . ARG A 1 13 ? 43.567 10.823 -2.710 1.00 15.75 ? 28 ARG A CD 1 ATOM 97 N NE . ARG A 1 13 ? 44.583 11.869 -2.649 1.00 17.59 ? 28 ARG A NE 1 ATOM 98 C CZ . ARG A 1 13 ? 44.317 13.166 -2.531 1.00 20.31 ? 28 ARG A CZ 1 ATOM 99 N NH1 . ARG A 1 13 ? 43.062 13.586 -2.458 1.00 19.58 ? 28 ARG A NH1 1 ATOM 100 N NH2 . ARG A 1 13 ? 45.309 14.045 -2.481 1.00 19.67 ? 28 ARG A NH2 1 ATOM 101 N N . PHE A 1 14 ? 43.970 7.764 2.101 1.00 11.30 ? 29 PHE A N 1 ATOM 102 C CA . PHE A 1 14 ? 44.027 7.800 3.565 1.00 10.73 ? 29 PHE A CA 1 ATOM 103 C C . PHE A 1 14 ? 44.433 6.463 4.209 1.00 9.66 ? 29 PHE A C 1 ATOM 104 O O . PHE A 1 14 ? 44.644 6.396 5.419 1.00 12.47 ? 29 PHE A O 1 ATOM 105 C CB . PHE A 1 14 ? 42.649 8.195 4.082 1.00 11.62 ? 29 PHE A CB 1 ATOM 106 C CG . PHE A 1 14 ? 41.545 7.372 3.487 1.00 13.48 ? 29 PHE A CG 1 ATOM 107 C CD1 . PHE A 1 14 ? 41.384 6.036 3.851 1.00 15.22 ? 29 PHE A CD1 1 ATOM 108 C CD2 . PHE A 1 14 ? 40.725 7.900 2.494 1.00 15.19 ? 29 PHE A CD2 1 ATOM 109 C CE1 . PHE A 1 14 ? 40.423 5.236 3.227 1.00 14.87 ? 29 PHE A CE1 1 ATOM 110 C CE2 . PHE A 1 14 ? 39.761 7.109 1.865 1.00 12.81 ? 29 PHE A CE2 1 ATOM 111 C CZ . PHE A 1 14 ? 39.613 5.779 2.232 1.00 15.78 ? 29 PHE A CZ 1 ATOM 112 N N . LEU A 1 15 ? 44.522 5.404 3.408 1.00 10.34 ? 30 LEU A N 1 ATOM 113 C CA . LEU A 1 15 ? 44.876 4.071 3.908 1.00 9.41 ? 30 LEU A CA 1 ATOM 114 C C . LEU A 1 15 ? 46.368 3.925 4.221 1.00 11.15 ? 30 LEU A C 1 ATOM 115 O O . LEU A 1 15 ? 47.222 4.141 3.361 1.00 12.48 ? 30 LEU A O 1 ATOM 116 C CB . LEU A 1 15 ? 44.451 3.005 2.893 1.00 7.90 ? 30 LEU A CB 1 ATOM 117 C CG . LEU A 1 15 ? 44.687 1.530 3.257 1.00 7.09 ? 30 LEU A CG 1 ATOM 118 C CD1 . LEU A 1 15 ? 43.840 1.158 4.460 1.00 5.37 ? 30 LEU A CD1 1 ATOM 119 C CD2 . LEU A 1 15 ? 44.343 0.636 2.062 1.00 4.82 ? 30 LEU A CD2 1 ATOM 120 N N . VAL A 1 16 ? 46.665 3.542 5.461 1.00 11.21 ? 31 VAL A N 1 ATOM 121 C CA . VAL A 1 16 ? 48.038 3.374 5.930 1.00 10.79 ? 31 VAL A CA 1 ATOM 122 C C . VAL A 1 16 ? 48.383 1.902 6.136 1.00 10.29 ? 31 VAL A C 1 ATOM 123 O O . VAL A 1 16 ? 47.560 1.135 6.630 1.00 10.04 ? 31 VAL A O 1 ATOM 124 C CB . VAL A 1 16 ? 48.247 4.095 7.288 1.00 10.37 ? 31 VAL A CB 1 ATOM 125 C CG1 . VAL A 1 16 ? 49.695 3.970 7.731 1.00 9.08 ? 31 VAL A CG1 1 ATOM 126 C CG2 . VAL A 1 16 ? 47.839 5.563 7.172 1.00 11.78 ? 31 VAL A CG2 1 ATOM 127 N N . ALA A 1 17 ? 49.600 1.513 5.769 1.00 9.57 ? 32 ALA A N 1 ATOM 128 C CA . ALA A 1 17 ? 50.040 0.130 5.955 1.00 12.48 ? 32 ALA A CA 1 ATOM 129 C C . ALA A 1 17 ? 51.018 0.048 7.127 1.00 12.84 ? 32 ALA A C 1 ATOM 130 O O . ALA A 1 17 ? 51.981 0.808 7.183 1.00 14.44 ? 32 ALA A O 1 ATOM 131 C CB . ALA A 1 17 ? 50.711 -0.387 4.688 1.00 12.02 ? 32 ALA A CB 1 ATOM 132 N N . PHE A 1 18 ? 50.762 -0.856 8.070 1.00 13.41 ? 33 PHE A N 1 ATOM 133 C CA . PHE A 1 18 ? 51.652 -1.037 9.218 1.00 13.36 ? 33 PHE A CA 1 ATOM 134 C C . PHE A 1 18 ? 52.528 -2.239 8.931 1.00 14.74 ? 33 PHE A C 1 ATOM 135 O O . PHE A 1 18 ? 52.026 -3.290 8.525 1.00 13.49 ? 33 PHE A O 1 ATOM 136 C CB . PHE A 1 18 ? 50.859 -1.297 10.503 1.00 11.37 ? 33 PHE A CB 1 ATOM 137 C CG . PHE A 1 18 ? 50.243 -0.066 11.099 1.00 14.29 ? 33 PHE A CG 1 ATOM 138 C CD1 . PHE A 1 18 ? 49.344 0.708 10.367 1.00 13.37 ? 33 PHE A CD1 1 ATOM 139 C CD2 . PHE A 1 18 ? 50.565 0.326 12.394 1.00 13.88 ? 33 PHE A CD2 1 ATOM 140 C CE1 . PHE A 1 18 ? 48.777 1.853 10.917 1.00 12.14 ? 33 PHE A CE1 1 ATOM 141 C CE2 . PHE A 1 18 ? 50.003 1.472 12.954 1.00 15.27 ? 33 PHE A CE2 1 ATOM 142 C CZ . PHE A 1 18 ? 49.106 2.236 12.213 1.00 13.73 ? 33 PHE A CZ 1 ATOM 143 N N . PHE A 1 19 ? 53.832 -2.097 9.152 1.00 14.85 ? 34 PHE A N 1 ATOM 144 C CA . PHE A 1 19 ? 54.746 -3.199 8.887 1.00 14.82 ? 34 PHE A CA 1 ATOM 145 C C . PHE A 1 19 ? 55.978 -3.198 9.773 1.00 15.79 ? 34 PHE A C 1 ATOM 146 O O . PHE A 1 19 ? 56.326 -2.189 10.388 1.00 15.58 ? 34 PHE A O 1 ATOM 147 C CB . PHE A 1 19 ? 55.217 -3.158 7.428 1.00 14.68 ? 34 PHE A CB 1 ATOM 148 C CG . PHE A 1 19 ? 56.096 -1.976 7.107 1.00 13.11 ? 34 PHE A CG 1 ATOM 149 C CD1 . PHE A 1 19 ? 55.549 -0.711 6.923 1.00 13.25 ? 34 PHE A CD1 1 ATOM 150 C CD2 . PHE A 1 19 ? 57.481 -2.122 7.022 1.00 14.89 ? 34 PHE A CD2 1 ATOM 151 C CE1 . PHE A 1 19 ? 56.367 0.396 6.657 1.00 11.70 ? 34 PHE A CE1 1 ATOM 152 C CE2 . PHE A 1 19 ? 58.309 -1.021 6.756 1.00 11.79 ? 34 PHE A CE2 1 ATOM 153 C CZ . PHE A 1 19 ? 57.750 0.237 6.574 1.00 12.43 ? 34 PHE A CZ 1 ATOM 154 N N . ASN A 1 20 ? 56.630 -4.352 9.834 1.00 16.61 ? 35 ASN A N 1 ATOM 155 C CA . ASN A 1 20 ? 57.870 -4.495 10.578 1.00 18.63 ? 35 ASN A CA 1 ATOM 156 C C . ASN A 1 20 ? 58.737 -5.425 9.741 1.00 18.89 ? 35 ASN A C 1 ATOM 157 O O . ASN A 1 20 ? 58.386 -5.717 8.601 1.00 16.74 ? 35 ASN A O 1 ATOM 158 C CB . ASN A 1 20 ? 57.640 -5.035 12.001 1.00 20.73 ? 35 ASN A CB 1 ATOM 159 C CG . ASN A 1 20 ? 56.911 -6.365 12.038 1.00 25.90 ? 35 ASN A CG 1 ATOM 160 O OD1 . ASN A 1 20 ? 56.759 -7.051 11.025 1.00 23.53 ? 35 ASN A OD1 1 ATOM 161 N ND2 . ASN A 1 20 ? 56.478 -6.730 13.244 1.00 31.98 ? 35 ASN A ND2 1 ATOM 162 N N . THR A 1 21 ? 59.856 -5.891 10.280 1.00 19.06 ? 36 THR A N 1 ATOM 163 C CA . THR A 1 21 ? 60.745 -6.756 9.508 1.00 21.12 ? 36 THR A CA 1 ATOM 164 C C . THR A 1 21 ? 60.079 -7.969 8.850 1.00 21.12 ? 36 THR A C 1 ATOM 165 O O . THR A 1 21 ? 60.644 -8.554 7.929 1.00 20.71 ? 36 THR A O 1 ATOM 166 C CB . THR A 1 21 ? 61.936 -7.237 10.362 1.00 21.35 ? 36 THR A CB 1 ATOM 167 O OG1 . THR A 1 21 ? 61.458 -7.981 11.489 1.00 22.96 ? 36 THR A OG1 1 ATOM 168 C CG2 . THR A 1 21 ? 62.737 -6.044 10.855 1.00 21.10 ? 36 THR A CG2 1 ATOM 169 N N . THR A 1 22 ? 58.883 -8.341 9.296 1.00 20.98 ? 38 THR A N 1 ATOM 170 C CA . THR A 1 22 ? 58.202 -9.485 8.698 1.00 23.50 ? 38 THR A CA 1 ATOM 171 C C . THR A 1 22 ? 57.203 -9.076 7.616 1.00 22.29 ? 38 THR A C 1 ATOM 172 O O . THR A 1 22 ? 56.583 -9.933 6.989 1.00 24.32 ? 38 THR A O 1 ATOM 173 C CB . THR A 1 22 ? 57.446 -10.322 9.755 1.00 25.83 ? 38 THR A CB 1 ATOM 174 O OG1 . THR A 1 22 ? 56.376 -9.545 10.313 1.00 31.69 ? 38 THR A OG1 1 ATOM 175 C CG2 . THR A 1 22 ? 58.382 -10.744 10.862 1.00 27.91 ? 38 THR A CG2 1 ATOM 176 N N . GLY A 1 23 ? 57.040 -7.775 7.395 1.00 20.17 ? 39 GLY A N 1 ATOM 177 C CA . GLY A 1 23 ? 56.110 -7.325 6.371 1.00 16.58 ? 39 GLY A CA 1 ATOM 178 C C . GLY A 1 23 ? 54.863 -6.634 6.892 1.00 15.12 ? 39 GLY A C 1 ATOM 179 O O . GLY A 1 23 ? 54.815 -6.212 8.045 1.00 15.23 ? 39 GLY A O 1 ATOM 180 N N . PHE A 1 24 ? 53.858 -6.502 6.029 1.00 14.44 ? 40 PHE A N 1 ATOM 181 C CA . PHE A 1 24 ? 52.596 -5.860 6.388 1.00 15.66 ? 40 PHE A CA 1 ATOM 182 C C . PHE A 1 24 ? 51.836 -6.731 7.383 1.00 16.05 ? 40 PHE A C 1 ATOM 183 O O . PHE A 1 24 ? 51.818 -7.955 7.250 1.00 16.12 ? 40 PHE A O 1 ATOM 184 C CB . PHE A 1 24 ? 51.733 -5.660 5.135 1.00 16.94 ? 40 PHE A CB 1 ATOM 185 C CG . PHE A 1 24 ? 52.180 -4.522 4.243 1.00 18.68 ? 40 PHE A CG 1 ATOM 186 C CD1 . PHE A 1 24 ? 53.497 -4.069 4.255 1.00 18.67 ? 40 PHE A CD1 1 ATOM 187 C CD2 . PHE A 1 24 ? 51.280 -3.933 3.356 1.00 17.52 ? 40 PHE A CD2 1 ATOM 188 C CE1 . PHE A 1 24 ? 53.911 -3.047 3.395 1.00 20.09 ? 40 PHE A CE1 1 ATOM 189 C CE2 . PHE A 1 24 ? 51.682 -2.914 2.493 1.00 18.09 ? 40 PHE A CE2 1 ATOM 190 C CZ . PHE A 1 24 ? 52.999 -2.469 2.511 1.00 19.29 ? 40 PHE A CZ 1 ATOM 191 N N . PHE A 1 25 ? 51.207 -6.115 8.379 1.00 14.49 ? 41 PHE A N 1 ATOM 192 C CA . PHE A 1 25 ? 50.449 -6.895 9.354 1.00 14.26 ? 41 PHE A CA 1 ATOM 193 C C . PHE A 1 25 ? 49.135 -6.229 9.756 1.00 14.26 ? 41 PHE A C 1 ATOM 194 O O . PHE A 1 25 ? 48.271 -6.863 10.360 1.00 12.99 ? 41 PHE A O 1 ATOM 195 C CB . PHE A 1 25 ? 51.316 -7.209 10.594 1.00 13.98 ? 41 PHE A CB 1 ATOM 196 C CG . PHE A 1 25 ? 51.768 -5.993 11.372 1.00 12.64 ? 41 PHE A CG 1 ATOM 197 C CD1 . PHE A 1 25 ? 50.919 -5.374 12.282 1.00 13.04 ? 41 PHE A CD1 1 ATOM 198 C CD2 . PHE A 1 25 ? 53.052 -5.482 11.206 1.00 12.64 ? 41 PHE A CD2 1 ATOM 199 C CE1 . PHE A 1 25 ? 51.339 -4.263 13.016 1.00 13.42 ? 41 PHE A CE1 1 ATOM 200 C CE2 . PHE A 1 25 ? 53.484 -4.370 11.932 1.00 12.88 ? 41 PHE A CE2 1 ATOM 201 C CZ . PHE A 1 25 ? 52.624 -3.760 12.840 1.00 13.55 ? 41 PHE A CZ 1 ATOM 202 N N . CYS A 1 26 ? 48.979 -4.957 9.393 1.00 13.24 ? 42 CYS A N 1 ATOM 203 C CA . CYS A 1 26 ? 47.770 -4.203 9.713 1.00 12.79 ? 42 CYS A CA 1 ATOM 204 C C . CYS A 1 26 ? 47.612 -2.993 8.813 1.00 11.32 ? 42 CYS A C 1 ATOM 205 O O . CYS A 1 26 ? 48.547 -2.583 8.130 1.00 11.38 ? 42 CYS A O 1 ATOM 206 C CB . CYS A 1 26 ? 47.805 -3.703 11.160 1.00 12.00 ? 42 CYS A CB 1 ATOM 207 S SG . CYS A 1 26 ? 47.280 -4.888 12.433 1.00 13.47 ? 42 CYS A SG 1 ATOM 208 N N . GLY A 1 27 ? 46.415 -2.424 8.830 1.00 9.85 ? 43 GLY A N 1 ATOM 209 C CA . GLY A 1 27 ? 46.155 -1.230 8.056 1.00 8.73 ? 43 GLY A CA 1 ATOM 210 C C . GLY A 1 27 ? 45.880 -0.122 9.052 1.00 9.37 ? 43 GLY A C 1 ATOM 211 O O . GLY A 1 27 ? 45.883 -0.365 10.259 1.00 8.31 ? 43 GLY A O 1 ATOM 212 N N . GLY A 1 28 ? 45.640 1.088 8.560 1.00 8.30 ? 44 GLY A N 1 ATOM 213 C CA . GLY A 1 28 ? 45.354 2.207 9.440 1.00 9.37 ? 44 GLY A CA 1 ATOM 214 C C . GLY A 1 28 ? 44.717 3.335 8.645 1.00 10.58 ? 44 GLY A C 1 ATOM 215 O O . GLY A 1 28 ? 44.659 3.267 7.420 1.00 9.88 ? 44 GLY A O 1 ATOM 216 N N . THR A 1 29 ? 44.244 4.373 9.328 1.00 9.99 ? 45 THR A N 1 ATOM 217 C CA . THR A 1 29 ? 43.609 5.492 8.644 1.00 10.41 ? 45 THR A CA 1 ATOM 218 C C . THR A 1 29 ? 44.175 6.853 9.051 1.00 9.80 ? 45 THR A C 1 ATOM 219 O O . THR A 1 29 ? 44.149 7.225 10.223 1.00 10.57 ? 45 THR A O 1 ATOM 220 C CB . THR A 1 29 ? 42.084 5.502 8.907 1.00 10.99 ? 45 THR A CB 1 ATOM 221 O OG1 . THR A 1 29 ? 41.526 4.251 8.498 1.00 11.22 ? 45 THR A OG1 1 ATOM 222 C CG2 . THR A 1 29 ? 41.402 6.622 8.121 1.00 8.69 ? 45 THR A CG2 1 ATOM 223 N N . LEU A 1 30 ? 44.686 7.594 8.077 1.00 10.83 ? 46 LEU A N 1 ATOM 224 C CA . LEU A 1 30 ? 45.223 8.927 8.337 1.00 11.35 ? 46 LEU A CA 1 ATOM 225 C C . LEU A 1 30 ? 44.018 9.855 8.520 1.00 12.80 ? 46 LEU A C 1 ATOM 226 O O . LEU A 1 30 ? 43.209 9.990 7.603 1.00 12.13 ? 46 LEU A O 1 ATOM 227 C CB . LEU A 1 30 ? 46.057 9.396 7.142 1.00 11.46 ? 46 LEU A CB 1 ATOM 228 C CG . LEU A 1 30 ? 46.731 10.771 7.253 1.00 10.64 ? 46 LEU A CG 1 ATOM 229 C CD1 . LEU A 1 30 ? 47.829 10.720 8.319 1.00 9.91 ? 46 LEU A CD1 1 ATOM 230 C CD2 . LEU A 1 30 ? 47.317 11.160 5.907 1.00 9.92 ? 46 LEU A CD2 1 ATOM 231 N N . ILE A 1 31 ? 43.890 10.484 9.690 1.00 12.68 ? 47 ILE A N 1 ATOM 232 C CA . ILE A 1 31 ? 42.750 11.378 9.946 1.00 13.30 ? 47 ILE A CA 1 ATOM 233 C C . ILE A 1 31 ? 43.105 12.866 9.869 1.00 14.33 ? 47 ILE A C 1 ATOM 234 O O . ILE A 1 31 ? 42.225 13.727 9.825 1.00 11.79 ? 47 ILE A O 1 ATOM 235 C CB . ILE A 1 31 ? 42.099 11.092 11.317 1.00 13.92 ? 47 ILE A CB 1 ATOM 236 C CG1 . ILE A 1 31 ? 43.063 11.457 12.447 1.00 10.23 ? 47 ILE A CG1 1 ATOM 237 C CG2 . ILE A 1 31 ? 41.704 9.622 11.401 1.00 14.46 ? 47 ILE A CG2 1 ATOM 238 C CD1 . ILE A 1 31 ? 42.431 11.394 13.827 1.00 12.57 ? 47 ILE A CD1 1 ATOM 239 N N . ASN A 1 32 ? 44.399 13.157 9.884 1.00 14.81 ? 48 ASN A N 1 ATOM 240 C CA . ASN A 1 32 ? 44.898 14.519 9.740 1.00 16.53 ? 48 ASN A CA 1 ATOM 241 C C . ASN A 1 32 ? 46.405 14.403 9.515 1.00 16.89 ? 48 ASN A C 1 ATOM 242 O O . ASN A 1 32 ? 46.966 13.316 9.643 1.00 15.36 ? 48 ASN A O 1 ATOM 243 C CB . ASN A 1 32 ? 44.545 15.398 10.958 1.00 19.43 ? 48 ASN A CB 1 ATOM 244 C CG . ASN A 1 32 ? 45.417 15.132 12.162 1.00 20.01 ? 48 ASN A CG 1 ATOM 245 O OD1 . ASN A 1 32 ? 46.641 15.106 12.066 1.00 22.63 ? 48 ASN A OD1 1 ATOM 246 N ND2 . ASN A 1 32 ? 44.786 14.962 13.318 1.00 23.07 ? 48 ASN A ND2 1 ATOM 247 N N . PRO A 1 33 ? 47.080 15.513 9.175 1.00 16.41 ? 49 PRO A N 1 ATOM 248 C CA . PRO A 1 33 ? 48.525 15.520 8.919 1.00 17.72 ? 49 PRO A CA 1 ATOM 249 C C . PRO A 1 33 ? 49.456 14.757 9.866 1.00 18.81 ? 49 PRO A C 1 ATOM 250 O O . PRO A 1 33 ? 50.476 14.218 9.424 1.00 20.57 ? 49 PRO A O 1 ATOM 251 C CB . PRO A 1 33 ? 48.857 17.008 8.876 1.00 17.71 ? 49 PRO A CB 1 ATOM 252 C CG . PRO A 1 33 ? 47.617 17.601 8.318 1.00 19.10 ? 49 PRO A CG 1 ATOM 253 C CD . PRO A 1 33 ? 46.533 16.877 9.085 1.00 16.13 ? 49 PRO A CD 1 ATOM 254 N N . GLU A 1 34 ? 49.117 14.696 11.151 1.00 17.87 ? 50 GLU A N 1 ATOM 255 C CA . GLU A 1 34 ? 49.980 14.029 12.129 1.00 18.07 ? 50 GLU A CA 1 ATOM 256 C C . GLU A 1 34 ? 49.405 12.833 12.871 1.00 16.41 ? 50 GLU A C 1 ATOM 257 O O . GLU A 1 34 ? 50.107 12.230 13.681 1.00 17.84 ? 50 GLU A O 1 ATOM 258 C CB . GLU A 1 34 ? 50.427 15.020 13.201 1.00 19.25 ? 50 GLU A CB 1 ATOM 259 C CG . GLU A 1 34 ? 51.279 16.157 12.739 1.00 23.01 ? 50 GLU A CG 1 ATOM 260 C CD . GLU A 1 34 ? 51.609 17.089 13.886 1.00 26.98 ? 50 GLU A CD 1 ATOM 261 O OE1 . GLU A 1 34 ? 50.688 17.782 14.377 1.00 26.82 ? 50 GLU A OE1 1 ATOM 262 O OE2 . GLU A 1 34 ? 52.784 17.114 14.308 1.00 29.44 ? 50 GLU A OE2 1 ATOM 263 N N . TRP A 1 35 ? 48.145 12.492 12.627 1.00 16.17 ? 51 TRP A N 1 ATOM 264 C CA . TRP A 1 35 ? 47.539 11.387 13.361 1.00 13.84 ? 51 TRP A CA 1 ATOM 265 C C . TRP A 1 35 ? 46.968 10.250 12.544 1.00 12.80 ? 51 TRP A C 1 ATOM 266 O O . TRP A 1 35 ? 46.357 10.462 11.498 1.00 12.38 ? 51 TRP A O 1 ATOM 267 C CB . TRP A 1 35 ? 46.447 11.927 14.279 1.00 13.74 ? 51 TRP A CB 1 ATOM 268 C CG . TRP A 1 35 ? 46.962 12.893 15.284 1.00 14.51 ? 51 TRP A CG 1 ATOM 269 C CD1 . TRP A 1 35 ? 47.216 14.219 15.094 1.00 15.79 ? 51 TRP A CD1 1 ATOM 270 C CD2 . TRP A 1 35 ? 47.298 12.609 16.646 1.00 16.01 ? 51 TRP A CD2 1 ATOM 271 N NE1 . TRP A 1 35 ? 47.686 14.783 16.257 1.00 15.35 ? 51 TRP A NE1 1 ATOM 272 C CE2 . TRP A 1 35 ? 47.742 13.817 17.227 1.00 16.01 ? 51 TRP A CE2 1 ATOM 273 C CE3 . TRP A 1 35 ? 47.259 11.450 17.437 1.00 16.69 ? 51 TRP A CE3 1 ATOM 274 C CZ2 . TRP A 1 35 ? 48.152 13.900 18.560 1.00 15.51 ? 51 TRP A CZ2 1 ATOM 275 C CZ3 . TRP A 1 35 ? 47.667 11.532 18.764 1.00 16.53 ? 51 TRP A CZ3 1 ATOM 276 C CH2 . TRP A 1 35 ? 48.104 12.751 19.312 1.00 17.86 ? 51 TRP A CH2 1 ATOM 277 N N . VAL A 1 36 ? 47.165 9.041 13.056 1.00 10.58 ? 52 VAL A N 1 ATOM 278 C CA . VAL A 1 36 ? 46.677 7.827 12.423 1.00 11.44 ? 52 VAL A CA 1 ATOM 279 C C . VAL A 1 36 ? 45.868 7.018 13.431 1.00 12.45 ? 52 VAL A C 1 ATOM 280 O O . VAL A 1 36 ? 46.227 6.939 14.608 1.00 12.72 ? 52 VAL A O 1 ATOM 281 C CB . VAL A 1 36 ? 47.852 6.963 11.926 1.00 11.76 ? 52 VAL A CB 1 ATOM 282 C CG1 . VAL A 1 36 ? 47.350 5.627 11.430 1.00 11.77 ? 52 VAL A CG1 1 ATOM 283 C CG2 . VAL A 1 36 ? 48.591 7.685 10.825 1.00 11.78 ? 52 VAL A CG2 1 ATOM 284 N N . VAL A 1 37 ? 44.772 6.424 12.969 1.00 11.31 ? 53 VAL A N 1 ATOM 285 C CA . VAL A 1 37 ? 43.932 5.607 13.834 1.00 12.69 ? 53 VAL A CA 1 ATOM 286 C C . VAL A 1 37 ? 43.952 4.150 13.329 1.00 13.86 ? 53 VAL A C 1 ATOM 287 O O . VAL A 1 37 ? 43.851 3.895 12.122 1.00 11.97 ? 53 VAL A O 1 ATOM 288 C CB . VAL A 1 37 ? 42.475 6.145 13.855 1.00 12.41 ? 53 VAL A CB 1 ATOM 289 C CG1 . VAL A 1 37 ? 41.600 5.276 14.737 1.00 11.56 ? 53 VAL A CG1 1 ATOM 290 C CG2 . VAL A 1 37 ? 42.463 7.571 14.373 1.00 13.11 ? 53 VAL A CG2 1 ATOM 291 N N . THR A 1 38 ? 44.100 3.205 14.256 1.00 12.31 ? 54 THR A N 1 ATOM 292 C CA . THR A 1 38 ? 44.142 1.791 13.905 1.00 11.60 ? 54 THR A CA 1 ATOM 293 C C . THR A 1 38 ? 43.575 0.989 15.072 1.00 10.89 ? 54 THR A C 1 ATOM 294 O O . THR A 1 38 ? 43.019 1.571 16.004 1.00 10.91 ? 54 THR A O 1 ATOM 295 C CB . THR A 1 38 ? 45.594 1.342 13.598 1.00 10.44 ? 54 THR A CB 1 ATOM 296 O OG1 . THR A 1 38 ? 45.589 -0.014 13.133 1.00 12.40 ? 54 THR A OG1 1 ATOM 297 C CG2 . THR A 1 38 ? 46.477 1.454 14.846 1.00 10.60 ? 54 THR A CG2 1 ATOM 298 N N . ALA A 1 39 ? 43.685 -0.336 15.014 1.00 10.28 ? 55 ALA A N 1 ATOM 299 C CA . ALA A 1 39 ? 43.179 -1.179 16.094 1.00 10.54 ? 55 ALA A CA 1 ATOM 300 C C . ALA A 1 39 ? 44.255 -1.329 17.170 1.00 11.55 ? 55 ALA A C 1 ATOM 301 O O . ALA A 1 39 ? 45.451 -1.349 16.872 1.00 11.94 ? 55 ALA A O 1 ATOM 302 C CB . ALA A 1 39 ? 42.781 -2.555 15.551 1.00 10.79 ? 55 ALA A CB 1 ATOM 303 N N . ALA A 1 40 ? 43.827 -1.430 18.423 1.00 11.58 ? 56 ALA A N 1 ATOM 304 C CA . ALA A 1 40 ? 44.761 -1.585 19.527 1.00 10.53 ? 56 ALA A CA 1 ATOM 305 C C . ALA A 1 40 ? 45.539 -2.894 19.425 1.00 11.23 ? 56 ALA A C 1 ATOM 306 O O . ALA A 1 40 ? 46.719 -2.939 19.772 1.00 10.81 ? 56 ALA A O 1 ATOM 307 C CB . ALA A 1 40 ? 44.014 -1.531 20.850 1.00 9.12 ? 56 ALA A CB 1 ATOM 308 N N . HIS A 1 41 ? 44.899 -3.956 18.940 1.00 10.21 ? 57 HIS A N 1 ATOM 309 C CA . HIS A 1 41 ? 45.609 -5.228 18.845 1.00 12.92 ? 57 HIS A CA 1 ATOM 310 C C . HIS A 1 41 ? 46.660 -5.284 17.744 1.00 12.86 ? 57 HIS A C 1 ATOM 311 O O . HIS A 1 41 ? 47.267 -6.330 17.517 1.00 14.85 ? 57 HIS A O 1 ATOM 312 C CB . HIS A 1 41 ? 44.639 -6.420 18.713 1.00 13.08 ? 57 HIS A CB 1 ATOM 313 C CG . HIS A 1 41 ? 44.074 -6.617 17.339 1.00 14.76 ? 57 HIS A CG 1 ATOM 314 N ND1 . HIS A 1 41 ? 42.947 -5.959 16.893 1.00 14.09 ? 57 HIS A ND1 1 ATOM 315 C CD2 . HIS A 1 41 ? 44.453 -7.440 16.329 1.00 13.74 ? 57 HIS A CD2 1 ATOM 316 C CE1 . HIS A 1 41 ? 42.654 -6.369 15.671 1.00 15.22 ? 57 HIS A CE1 1 ATOM 317 N NE2 . HIS A 1 41 ? 43.552 -7.268 15.306 1.00 14.16 ? 57 HIS A NE2 1 ATOM 318 N N . CYS A 1 42 ? 46.877 -4.160 17.066 1.00 12.18 ? 58 CYS A N 1 ATOM 319 C CA . CYS A 1 42 ? 47.888 -4.080 16.018 1.00 13.19 ? 58 CYS A CA 1 ATOM 320 C C . CYS A 1 42 ? 49.194 -3.541 16.611 1.00 15.35 ? 58 CYS A C 1 ATOM 321 O O . CYS A 1 42 ? 50.230 -3.520 15.948 1.00 17.90 ? 58 CYS A O 1 ATOM 322 C CB . CYS A 1 42 ? 47.446 -3.136 14.901 1.00 13.22 ? 58 CYS A CB 1 ATOM 323 S SG . CYS A 1 42 ? 46.197 -3.764 13.730 1.00 12.36 ? 58 CYS A SG 1 ATOM 324 N N . ASP A 1 43 ? 49.138 -3.103 17.862 1.00 15.89 ? 59 ASP A N 1 ATOM 325 C CA . ASP A 1 43 ? 50.311 -2.538 18.520 1.00 17.71 ? 59 ASP A CA 1 ATOM 326 C C . ASP A 1 43 ? 51.454 -3.534 18.635 1.00 18.52 ? 59 ASP A C 1 ATOM 327 O O . ASP A 1 43 ? 51.241 -4.719 18.881 1.00 18.46 ? 59 ASP A O 1 ATOM 328 C CB . ASP A 1 43 ? 49.927 -2.003 19.902 1.00 16.88 ? 59 ASP A CB 1 ATOM 329 C CG . ASP A 1 43 ? 51.059 -1.257 20.574 1.00 17.87 ? 59 ASP A CG 1 ATOM 330 O OD1 . ASP A 1 43 ? 51.891 -0.652 19.861 1.00 17.03 ? 59 ASP A OD1 1 ATOM 331 O OD2 . ASP A 1 43 ? 51.106 -1.263 21.819 1.00 18.68 ? 59 ASP A OD2 1 ATOM 332 N N . SER A 1 44 ? 52.670 -3.038 18.433 1.00 21.68 ? 60 SER A N 1 ATOM 333 C CA . SER A 1 44 ? 53.879 -3.854 18.502 1.00 23.89 ? 60 SER A CA 1 ATOM 334 C C . SER A 1 44 ? 55.004 -2.981 19.048 1.00 24.02 ? 60 SER A C 1 ATOM 335 O O . SER A 1 44 ? 54.870 -1.755 19.098 1.00 22.64 ? 60 SER A O 1 ATOM 336 C CB . SER A 1 44 ? 54.244 -4.371 17.109 1.00 25.27 ? 60 SER A CB 1 ATOM 337 O OG . SER A 1 44 ? 55.453 -5.108 17.149 1.00 31.43 ? 60 SER A OG 1 ATOM 338 N N . THR A 1 45 ? 56.110 -3.602 19.451 1.00 24.48 ? 62 THR A N 1 ATOM 339 C CA . THR A 1 45 ? 57.225 -2.842 20.008 1.00 25.08 ? 62 THR A CA 1 ATOM 340 C C . THR A 1 45 ? 58.015 -2.099 18.930 1.00 26.27 ? 62 THR A C 1 ATOM 341 O O . THR A 1 45 ? 58.505 -0.995 19.173 1.00 26.48 ? 62 THR A O 1 ATOM 342 C CB . THR A 1 45 ? 58.188 -3.751 20.807 1.00 27.28 ? 62 THR A CB 1 ATOM 343 O OG1 . THR A 1 45 ? 59.153 -4.329 19.922 1.00 29.33 ? 62 THR A OG1 1 ATOM 344 C CG2 . THR A 1 45 ? 57.414 -4.874 21.482 1.00 28.59 ? 62 THR A CG2 1 ATOM 345 N N . ASN A 1 46 ? 58.132 -2.700 17.744 1.00 24.83 ? 63 ASN A N 1 ATOM 346 C CA . ASN A 1 46 ? 58.852 -2.079 16.637 1.00 25.08 ? 63 ASN A CA 1 ATOM 347 C C . ASN A 1 46 ? 58.125 -2.230 15.303 1.00 23.82 ? 63 ASN A C 1 ATOM 348 O O . ASN A 1 46 ? 58.040 -3.326 14.745 1.00 26.19 ? 63 ASN A O 1 ATOM 349 C CB . ASN A 1 46 ? 60.260 -2.672 16.491 1.00 27.73 ? 63 ASN A CB 1 ATOM 350 C CG . ASN A 1 46 ? 61.138 -2.409 17.700 1.00 31.03 ? 63 ASN A CG 1 ATOM 351 O OD1 . ASN A 1 46 ? 61.345 -1.257 18.100 1.00 32.65 ? 63 ASN A OD1 1 ATOM 352 N ND2 . ASN A 1 46 ? 61.660 -3.479 18.291 1.00 30.06 ? 63 ASN A ND2 1 ATOM 353 N N . PHE A 1 47 ? 57.602 -1.121 14.796 1.00 19.23 ? 64 PHE A N 1 ATOM 354 C CA . PHE A 1 47 ? 56.910 -1.121 13.517 1.00 16.58 ? 64 PHE A CA 1 ATOM 355 C C . PHE A 1 47 ? 56.998 0.261 12.901 1.00 13.84 ? 64 PHE A C 1 ATOM 356 O O . PHE A 1 47 ? 57.335 1.238 13.575 1.00 13.73 ? 64 PHE A O 1 ATOM 357 C CB . PHE A 1 47 ? 55.438 -1.535 13.685 1.00 15.32 ? 64 PHE A CB 1 ATOM 358 C CG . PHE A 1 47 ? 54.608 -0.558 14.473 1.00 15.32 ? 64 PHE A CG 1 ATOM 359 C CD1 . PHE A 1 47 ? 54.141 0.615 13.887 1.00 15.06 ? 64 PHE A CD1 1 ATOM 360 C CD2 . PHE A 1 47 ? 54.297 -0.809 15.805 1.00 16.13 ? 64 PHE A CD2 1 ATOM 361 C CE1 . PHE A 1 47 ? 53.380 1.520 14.614 1.00 15.99 ? 64 PHE A CE1 1 ATOM 362 C CE2 . PHE A 1 47 ? 53.535 0.092 16.543 1.00 13.91 ? 64 PHE A CE2 1 ATOM 363 C CZ . PHE A 1 47 ? 53.076 1.256 15.950 1.00 16.25 ? 64 PHE A CZ 1 ATOM 364 N N . GLN A 1 48 ? 56.713 0.331 11.608 1.00 13.00 ? 65 GLN A N 1 ATOM 365 C CA . GLN A 1 48 ? 56.739 1.589 10.878 1.00 11.66 ? 65 GLN A CA 1 ATOM 366 C C . GLN A 1 48 ? 55.444 1.675 10.094 1.00 11.41 ? 65 GLN A C 1 ATOM 367 O O . GLN A 1 48 ? 54.683 0.705 10.025 1.00 8.21 ? 65 GLN A O 1 ATOM 368 C CB . GLN A 1 48 ? 57.938 1.632 9.919 1.00 11.75 ? 65 GLN A CB 1 ATOM 369 C CG . GLN A 1 48 ? 59.289 1.717 10.613 1.00 11.36 ? 65 GLN A CG 1 ATOM 370 C CD . GLN A 1 48 ? 60.450 1.744 9.634 1.00 12.71 ? 65 GLN A CD 1 ATOM 371 O OE1 . GLN A 1 48 ? 60.715 0.763 8.941 1.00 10.14 ? 65 GLN A OE1 1 ATOM 372 N NE2 . GLN A 1 48 ? 61.147 2.874 9.572 1.00 12.53 ? 65 GLN A NE2 1 ATOM 373 N N . MET A 1 49 ? 55.196 2.836 9.508 1.00 10.31 ? 66 MET A N 1 ATOM 374 C CA . MET A 1 49 ? 53.988 3.046 8.727 1.00 11.41 ? 66 MET A CA 1 ATOM 375 C C . MET A 1 49 ? 54.338 3.567 7.343 1.00 12.97 ? 66 MET A C 1 ATOM 376 O O . MET A 1 49 ? 55.179 4.454 7.197 1.00 11.09 ? 66 MET A O 1 ATOM 377 C CB . MET A 1 49 ? 53.075 4.045 9.444 1.00 9.80 ? 66 MET A CB 1 ATOM 378 C CG . MET A 1 49 ? 52.548 3.524 10.774 1.00 9.79 ? 66 MET A CG 1 ATOM 379 S SD . MET A 1 49 ? 51.914 4.822 11.847 1.00 14.72 ? 66 MET A SD 1 ATOM 380 C CE . MET A 1 49 ? 53.472 5.467 12.540 1.00 9.67 ? 66 MET A CE 1 ATOM 381 N N . GLN A 1 50 ? 53.688 3.005 6.330 1.00 13.59 ? 67 GLN A N 1 ATOM 382 C CA . GLN A 1 50 ? 53.919 3.418 4.956 1.00 15.27 ? 67 GLN A CA 1 ATOM 383 C C . GLN A 1 50 ? 52.641 4.072 4.424 1.00 14.74 ? 67 GLN A C 1 ATOM 384 O O . GLN A 1 50 ? 51.569 3.474 4.471 1.00 14.74 ? 67 GLN A O 1 ATOM 385 C CB . GLN A 1 50 ? 54.285 2.199 4.109 1.00 14.64 ? 67 GLN A CB 1 ATOM 386 C CG . GLN A 1 50 ? 55.027 2.518 2.832 1.00 16.80 ? 67 GLN A CG 1 ATOM 387 C CD . GLN A 1 50 ? 56.408 3.090 3.076 1.00 19.60 ? 67 GLN A CD 1 ATOM 388 O OE1 . GLN A 1 50 ? 56.865 3.185 4.216 1.00 20.02 ? 67 GLN A OE1 1 ATOM 389 N NE2 . GLN A 1 50 ? 57.084 3.473 2.000 1.00 19.05 ? 67 GLN A NE2 1 ATOM 390 N N . LEU A 1 51 ? 52.754 5.306 3.940 1.00 13.66 ? 68 LEU A N 1 ATOM 391 C CA . LEU A 1 51 ? 51.602 6.017 3.397 1.00 13.10 ? 68 LEU A CA 1 ATOM 392 C C . LEU A 1 51 ? 51.775 6.249 1.896 1.00 12.05 ? 68 LEU A C 1 ATOM 393 O O . LEU A 1 51 ? 52.898 6.388 1.413 1.00 10.74 ? 68 LEU A O 1 ATOM 394 C CB . LEU A 1 51 ? 51.418 7.363 4.110 1.00 12.31 ? 68 LEU A CB 1 ATOM 395 C CG . LEU A 1 51 ? 51.238 7.288 5.631 1.00 12.55 ? 68 LEU A CG 1 ATOM 396 C CD1 . LEU A 1 51 ? 52.607 7.255 6.300 1.00 11.94 ? 68 LEU A CD1 1 ATOM 397 C CD2 . LEU A 1 51 ? 50.448 8.480 6.119 1.00 9.94 ? 68 LEU A CD2 1 ATOM 398 N N . GLY A 1 52 ? 50.658 6.280 1.168 1.00 10.78 ? 69 GLY A N 1 ATOM 399 C CA . GLY A 1 52 ? 50.696 6.493 -0.271 1.00 13.13 ? 69 GLY A CA 1 ATOM 400 C C . GLY A 1 52 ? 50.987 5.233 -1.066 1.00 14.01 ? 69 GLY A C 1 ATOM 401 O O . GLY A 1 52 ? 51.364 5.305 -2.233 1.00 14.47 ? 69 GLY A O 1 ATOM 402 N N . VAL A 1 53 ? 50.796 4.078 -0.432 1.00 14.18 ? 70 VAL A N 1 ATOM 403 C CA . VAL A 1 53 ? 51.051 2.781 -1.055 1.00 13.79 ? 70 VAL A CA 1 ATOM 404 C C . VAL A 1 53 ? 49.863 2.153 -1.782 1.00 13.86 ? 70 VAL A C 1 ATOM 405 O O . VAL A 1 53 ? 48.733 2.194 -1.296 1.00 14.85 ? 70 VAL A O 1 ATOM 406 C CB . VAL A 1 53 ? 51.494 1.732 0.002 1.00 15.27 ? 70 VAL A CB 1 ATOM 407 C CG1 . VAL A 1 53 ? 51.724 0.379 -0.657 1.00 14.44 ? 70 VAL A CG1 1 ATOM 408 C CG2 . VAL A 1 53 ? 52.746 2.181 0.705 1.00 14.15 ? 70 VAL A CG2 1 ATOM 409 N N . HIS A 1 54 ? 50.128 1.584 -2.956 1.00 12.38 ? 71 HIS A N 1 ATOM 410 C CA . HIS A 1 54 ? 49.104 0.851 -3.693 1.00 12.33 ? 71 HIS A CA 1 ATOM 411 C C . HIS A 1 54 ? 49.735 -0.508 -3.932 1.00 11.77 ? 71 HIS A C 1 ATOM 412 O O . HIS A 1 54 ? 49.448 -1.459 -3.224 1.00 12.33 ? 71 HIS A O 1 ATOM 413 C CB . HIS A 1 54 ? 48.742 1.482 -5.035 1.00 11.46 ? 71 HIS A CB 1 ATOM 414 C CG . HIS A 1 54 ? 47.611 0.782 -5.732 1.00 13.74 ? 71 HIS A CG 1 ATOM 415 N ND1 . HIS A 1 54 ? 46.304 0.835 -5.279 1.00 12.73 ? 71 HIS A ND1 1 ATOM 416 C CD2 . HIS A 1 54 ? 47.590 -0.016 -6.827 1.00 13.23 ? 71 HIS A CD2 1 ATOM 417 C CE1 . HIS A 1 54 ? 45.538 0.105 -6.065 1.00 13.49 ? 71 HIS A CE1 1 ATOM 418 N NE2 . HIS A 1 54 ? 46.293 -0.424 -7.014 1.00 13.72 ? 71 HIS A NE2 1 ATOM 419 N N . SER A 1 55 ? 50.617 -0.597 -4.919 1.00 13.09 ? 72 SER A N 1 ATOM 420 C CA . SER A 1 55 ? 51.296 -1.860 -5.192 1.00 14.38 ? 72 SER A CA 1 ATOM 421 C C . SER A 1 55 ? 52.539 -1.975 -4.310 1.00 17.08 ? 72 SER A C 1 ATOM 422 O O . SER A 1 55 ? 53.236 -0.983 -4.074 1.00 15.80 ? 72 SER A O 1 ATOM 423 C CB . SER A 1 55 ? 51.710 -1.939 -6.663 1.00 17.05 ? 72 SER A CB 1 ATOM 424 O OG . SER A 1 55 ? 52.545 -3.063 -6.893 1.00 16.53 ? 72 SER A OG 1 ATOM 425 N N . LYS A 1 56 ? 52.813 -3.183 -3.826 1.00 17.34 ? 73 LYS A N 1 ATOM 426 C CA . LYS A 1 56 ? 53.978 -3.428 -2.982 1.00 19.51 ? 73 LYS A CA 1 ATOM 427 C C . LYS A 1 56 ? 55.209 -3.735 -3.836 1.00 19.77 ? 73 LYS A C 1 ATOM 428 O O . LYS A 1 56 ? 56.323 -3.776 -3.326 1.00 20.60 ? 73 LYS A O 1 ATOM 429 C CB . LYS A 1 56 ? 53.688 -4.593 -2.024 1.00 22.19 ? 73 LYS A CB 1 ATOM 430 C CG . LYS A 1 56 ? 52.506 -4.319 -1.092 1.00 23.11 ? 73 LYS A CG 1 ATOM 431 C CD . LYS A 1 56 ? 51.894 -5.586 -0.503 1.00 24.61 ? 73 LYS A CD 1 ATOM 432 C CE . LYS A 1 56 ? 52.801 -6.258 0.516 1.00 24.63 ? 73 LYS A CE 1 ATOM 433 N NZ . LYS A 1 56 ? 52.095 -7.394 1.188 1.00 24.36 ? 73 LYS A NZ 1 ATOM 434 N N . LYS A 1 57 ? 55.002 -3.933 -5.137 1.00 20.64 ? 74 LYS A N 1 ATOM 435 C CA . LYS A 1 57 ? 56.089 -4.244 -6.070 1.00 22.06 ? 74 LYS A CA 1 ATOM 436 C C . LYS A 1 57 ? 56.446 -3.078 -6.995 1.00 21.29 ? 74 LYS A C 1 ATOM 437 O O . LYS A 1 57 ? 57.616 -2.858 -7.295 1.00 22.50 ? 74 LYS A O 1 ATOM 438 C CB . LYS A 1 57 ? 55.721 -5.466 -6.917 1.00 24.90 ? 74 LYS A CB 1 ATOM 439 C CG . LYS A 1 57 ? 55.375 -6.708 -6.107 1.00 27.88 ? 74 LYS A CG 1 ATOM 440 C CD . LYS A 1 57 ? 56.481 -7.069 -5.131 1.00 30.40 ? 74 LYS A CD 1 ATOM 441 C CE . LYS A 1 57 ? 56.153 -8.361 -4.391 1.00 34.05 ? 74 LYS A CE 1 ATOM 442 N NZ . LYS A 1 57 ? 57.170 -8.684 -3.351 1.00 37.26 ? 74 LYS A NZ 1 ATOM 443 N N . VAL A 1 58 ? 55.435 -2.362 -7.475 1.00 20.28 ? 75 VAL A N 1 ATOM 444 C CA . VAL A 1 58 ? 55.652 -1.196 -8.331 1.00 19.05 ? 75 VAL A CA 1 ATOM 445 C C . VAL A 1 58 ? 55.307 -0.038 -7.409 1.00 18.55 ? 75 VAL A C 1 ATOM 446 O O . VAL A 1 58 ? 54.141 0.191 -7.100 1.00 19.11 ? 75 VAL A O 1 ATOM 447 C CB . VAL A 1 58 ? 54.703 -1.189 -9.544 1.00 19.61 ? 75 VAL A CB 1 ATOM 448 C CG1 . VAL A 1 58 ? 55.039 -0.023 -10.466 1.00 17.12 ? 75 VAL A CG1 1 ATOM 449 C CG2 . VAL A 1 58 ? 54.811 -2.512 -10.291 1.00 18.65 ? 75 VAL A CG2 1 ATOM 450 N N . LEU A 1 59 ? 56.327 0.680 -6.957 1.00 17.74 ? 76 LEU A N 1 ATOM 451 C CA . LEU A 1 59 ? 56.122 1.766 -6.016 1.00 17.93 ? 76 LEU A CA 1 ATOM 452 C C . LEU A 1 59 ? 55.639 3.088 -6.580 1.00 17.50 ? 76 LEU A C 1 ATOM 453 O O . LEU A 1 59 ? 56.082 3.521 -7.643 1.00 15.82 ? 76 LEU A O 1 ATOM 454 C CB . LEU A 1 59 ? 57.412 2.016 -5.232 1.00 19.25 ? 76 LEU A CB 1 ATOM 455 C CG . LEU A 1 59 ? 58.135 0.798 -4.653 1.00 21.33 ? 76 LEU A CG 1 ATOM 456 C CD1 . LEU A 1 59 ? 59.236 1.281 -3.717 1.00 19.76 ? 76 LEU A CD1 1 ATOM 457 C CD2 . LEU A 1 59 ? 57.161 -0.092 -3.909 1.00 20.06 ? 76 LEU A CD2 1 ATOM 458 N N . ASN A 1 60 ? 54.714 3.721 -5.862 1.00 18.18 ? 77 ASN A N 1 ATOM 459 C CA . ASN A 1 60 ? 54.233 5.033 -6.259 1.00 18.64 ? 77 ASN A CA 1 ATOM 460 C C . ASN A 1 60 ? 55.437 5.893 -5.920 1.00 18.72 ? 77 ASN A C 1 ATOM 461 O O . ASN A 1 60 ? 56.170 5.587 -4.979 1.00 18.59 ? 77 ASN A O 1 ATOM 462 C CB . ASN A 1 60 ? 53.029 5.477 -5.424 1.00 19.29 ? 77 ASN A CB 1 ATOM 463 C CG . ASN A 1 60 ? 51.760 4.724 -5.774 1.00 20.72 ? 77 ASN A CG 1 ATOM 464 O OD1 . ASN A 1 60 ? 51.546 4.351 -6.925 1.00 21.88 ? 77 ASN A OD1 1 ATOM 465 N ND2 . ASN A 1 60 ? 50.903 4.516 -4.785 1.00 19.95 ? 77 ASN A ND2 1 ATOM 466 N N . GLU A 1 61 ? 55.650 6.960 -6.673 1.00 17.93 ? 78 GLU A N 1 ATOM 467 C CA . GLU A 1 61 ? 56.802 7.809 -6.438 1.00 19.39 ? 78 GLU A CA 1 ATOM 468 C C . GLU A 1 61 ? 56.647 8.726 -5.231 1.00 18.70 ? 78 GLU A C 1 ATOM 469 O O . GLU A 1 61 ? 57.633 9.260 -4.732 1.00 17.89 ? 78 GLU A O 1 ATOM 470 C CB . GLU A 1 61 ? 57.100 8.628 -7.699 1.00 21.29 ? 78 GLU A CB 1 ATOM 471 C CG . GLU A 1 61 ? 58.437 9.351 -7.676 1.00 26.72 ? 78 GLU A CG 1 ATOM 472 C CD . GLU A 1 61 ? 58.878 9.803 -9.060 1.00 29.08 ? 78 GLU A CD 1 ATOM 473 O OE1 . GLU A 1 61 ? 59.048 8.931 -9.938 1.00 28.87 ? 78 GLU A OE1 1 ATOM 474 O OE2 . GLU A 1 61 ? 59.055 11.025 -9.267 1.00 30.97 ? 78 GLU A OE2 1 ATOM 475 N N . ASP A 1 62 ? 55.418 8.891 -4.748 1.00 18.47 ? 79 ASP A N 1 ATOM 476 C CA . ASP A 1 62 ? 55.178 9.762 -3.603 1.00 19.06 ? 79 ASP A CA 1 ATOM 477 C C . ASP A 1 62 ? 54.937 9.023 -2.286 1.00 18.54 ? 79 ASP A C 1 ATOM 478 O O . ASP A 1 62 ? 54.333 9.572 -1.368 1.00 16.52 ? 79 ASP A O 1 ATOM 479 C CB . ASP A 1 62 ? 54.009 10.714 -3.900 1.00 19.35 ? 79 ASP A CB 1 ATOM 480 C CG . ASP A 1 62 ? 52.701 9.982 -4.115 1.00 20.49 ? 79 ASP A CG 1 ATOM 481 O OD1 . ASP A 1 62 ? 52.722 8.912 -4.764 1.00 20.46 ? 79 ASP A OD1 1 ATOM 482 O OD2 . ASP A 1 62 ? 51.654 10.481 -3.648 1.00 18.96 ? 79 ASP A OD2 1 ATOM 483 N N . GLU A 1 63 ? 55.409 7.781 -2.197 1.00 19.38 ? 80 GLU A N 1 ATOM 484 C CA . GLU A 1 63 ? 55.271 6.992 -0.969 1.00 20.28 ? 80 GLU A CA 1 ATOM 485 C C . GLU A 1 63 ? 56.047 7.664 0.169 1.00 20.79 ? 80 GLU A C 1 ATOM 486 O O . GLU A 1 63 ? 57.075 8.300 -0.070 1.00 21.40 ? 80 GLU A O 1 ATOM 487 C CB . GLU A 1 63 ? 55.811 5.569 -1.174 1.00 18.02 ? 80 GLU A CB 1 ATOM 488 C CG . GLU A 1 63 ? 54.765 4.562 -1.627 1.00 21.00 ? 80 GLU A CG 1 ATOM 489 C CD . GLU A 1 63 ? 55.282 3.131 -1.659 1.00 21.75 ? 80 GLU A CD 1 ATOM 490 O OE1 . GLU A 1 63 ? 56.109 2.770 -0.800 1.00 23.04 ? 80 GLU A OE1 1 ATOM 491 O OE2 . GLU A 1 63 ? 54.846 2.354 -2.532 1.00 22.50 ? 80 GLU A OE2 1 ATOM 492 N N . GLN A 1 64 ? 55.552 7.528 1.399 1.00 20.48 ? 81 GLN A N 1 ATOM 493 C CA . GLN A 1 64 ? 56.212 8.117 2.566 1.00 19.53 ? 81 GLN A CA 1 ATOM 494 C C . GLN A 1 64 ? 56.289 7.113 3.713 1.00 19.26 ? 81 GLN A C 1 ATOM 495 O O . GLN A 1 64 ? 55.371 6.308 3.909 1.00 18.09 ? 81 GLN A O 1 ATOM 496 C CB . GLN A 1 64 ? 55.444 9.346 3.065 1.00 20.85 ? 81 GLN A CB 1 ATOM 497 C CG . GLN A 1 64 ? 55.398 10.543 2.129 1.00 22.85 ? 81 GLN A CG 1 ATOM 498 C CD . GLN A 1 64 ? 56.732 11.241 2.001 1.00 24.73 ? 81 GLN A CD 1 ATOM 499 O OE1 . GLN A 1 64 ? 57.418 11.480 2.992 1.00 26.39 ? 81 GLN A OE1 1 ATOM 500 N NE2 . GLN A 1 64 ? 57.102 11.586 0.774 1.00 28.12 ? 81 GLN A NE2 1 ATOM 501 N N . THR A 1 65 ? 57.379 7.168 4.474 1.00 18.04 ? 82 THR A N 1 ATOM 502 C CA . THR A 1 65 ? 57.554 6.288 5.627 1.00 16.29 ? 82 THR A CA 1 ATOM 503 C C . THR A 1 65 ? 57.555 7.130 6.907 1.00 17.27 ? 82 THR A C 1 ATOM 504 O O . THR A 1 65 ? 58.194 8.183 6.964 1.00 15.88 ? 82 THR A O 1 ATOM 505 C CB . THR A 1 65 ? 58.882 5.504 5.555 1.00 17.34 ? 82 THR A CB 1 ATOM 506 O OG1 . THR A 1 65 ? 58.890 4.673 4.387 1.00 14.90 ? 82 THR A OG1 1 ATOM 507 C CG2 . THR A 1 65 ? 59.039 4.622 6.783 1.00 13.41 ? 82 THR A CG2 1 ATOM 508 N N . ARG A 1 66 ? 56.828 6.676 7.924 1.00 15.38 ? 83 ARG A N 1 ATOM 509 C CA . ARG A 1 66 ? 56.769 7.396 9.193 1.00 15.83 ? 83 ARG A CA 1 ATOM 510 C C . ARG A 1 66 ? 56.896 6.449 10.379 1.00 15.85 ? 83 ARG A C 1 ATOM 511 O O . ARG A 1 66 ? 56.570 5.269 10.282 1.00 15.82 ? 83 ARG A O 1 ATOM 512 C CB . ARG A 1 66 ? 55.461 8.185 9.306 1.00 16.53 ? 83 ARG A CB 1 ATOM 513 C CG . ARG A 1 66 ? 55.369 9.392 8.381 1.00 16.19 ? 83 ARG A CG 1 ATOM 514 C CD . ARG A 1 66 ? 56.351 10.480 8.786 1.00 16.74 ? 83 ARG A CD 1 ATOM 515 N NE . ARG A 1 66 ? 56.184 11.690 7.987 1.00 15.28 ? 83 ARG A NE 1 ATOM 516 C CZ . ARG A 1 66 ? 56.659 11.853 6.758 1.00 16.02 ? 83 ARG A CZ 1 ATOM 517 N NH1 . ARG A 1 66 ? 57.344 10.882 6.174 1.00 14.01 ? 83 ARG A NH1 1 ATOM 518 N NH2 . ARG A 1 66 ? 56.441 12.988 6.108 1.00 16.20 ? 83 ARG A NH2 1 ATOM 519 N N . ASN A 1 67 ? 57.386 6.975 11.497 1.00 15.55 ? 84 ASN A N 1 ATOM 520 C CA . ASN A 1 67 ? 57.555 6.180 12.704 1.00 15.61 ? 84 ASN A CA 1 ATOM 521 C C . ASN A 1 67 ? 56.595 6.677 13.781 1.00 15.37 ? 84 ASN A C 1 ATOM 522 O O . ASN A 1 67 ? 56.203 7.845 13.786 1.00 15.07 ? 84 ASN A O 1 ATOM 523 C CB . ASN A 1 67 ? 58.999 6.283 13.199 1.00 17.33 ? 84 ASN A CB 1 ATOM 524 C CG . ASN A 1 67 ? 60.001 5.803 12.167 1.00 20.48 ? 84 ASN A CG 1 ATOM 525 O OD1 . ASN A 1 67 ? 60.053 4.618 11.835 1.00 22.26 ? 84 ASN A OD1 1 ATOM 526 N ND2 . ASN A 1 67 ? 60.798 6.723 11.645 1.00 20.87 ? 84 ASN A ND2 1 ATOM 527 N N . PRO A 1 68 ? 56.185 5.787 14.695 1.00 15.14 ? 85 PRO A N 1 ATOM 528 C CA . PRO A 1 68 ? 55.267 6.176 15.767 1.00 16.44 ? 85 PRO A CA 1 ATOM 529 C C . PRO A 1 68 ? 55.978 7.016 16.831 1.00 17.93 ? 85 PRO A C 1 ATOM 530 O O . PRO A 1 68 ? 56.904 6.544 17.491 1.00 21.38 ? 85 PRO A O 1 ATOM 531 C CB . PRO A 1 68 ? 54.785 4.833 16.301 1.00 16.67 ? 85 PRO A CB 1 ATOM 532 C CG . PRO A 1 68 ? 55.993 3.957 16.121 1.00 15.69 ? 85 PRO A CG 1 ATOM 533 C CD . PRO A 1 68 ? 56.462 4.339 14.736 1.00 15.56 ? 85 PRO A CD 1 ATOM 534 N N . LYS A 1 69 ? 55.557 8.266 16.989 1.00 16.48 ? 86 LYS A N 1 ATOM 535 C CA . LYS A 1 69 ? 56.174 9.141 17.978 1.00 15.62 ? 86 LYS A CA 1 ATOM 536 C C . LYS A 1 69 ? 55.516 8.832 19.318 1.00 14.94 ? 86 LYS A C 1 ATOM 537 O O . LYS A 1 69 ? 56.196 8.552 20.305 1.00 15.10 ? 86 LYS A O 1 ATOM 538 C CB . LYS A 1 69 ? 55.962 10.612 17.585 1.00 15.57 ? 86 LYS A CB 1 ATOM 539 C CG . LYS A 1 69 ? 56.813 11.635 18.349 1.00 17.79 ? 86 LYS A CG 1 ATOM 540 C CD . LYS A 1 69 ? 56.714 13.005 17.670 1.00 20.44 ? 86 LYS A CD 1 ATOM 541 C CE . LYS A 1 69 ? 57.677 14.042 18.243 1.00 24.57 ? 86 LYS A CE 1 ATOM 542 N NZ . LYS A 1 69 ? 57.320 14.492 19.613 1.00 26.98 ? 86 LYS A NZ 1 ATOM 543 N N . GLU A 1 70 ? 54.187 8.863 19.337 1.00 14.61 ? 87 GLU A N 1 ATOM 544 C CA . GLU A 1 70 ? 53.418 8.580 20.547 1.00 16.55 ? 87 GLU A CA 1 ATOM 545 C C . GLU A 1 70 ? 52.237 7.655 20.247 1.00 16.84 ? 87 GLU A C 1 ATOM 546 O O . GLU A 1 70 ? 51.618 7.750 19.183 1.00 16.34 ? 87 GLU A O 1 ATOM 547 C CB . GLU A 1 70 ? 52.902 9.882 21.169 1.00 15.78 ? 87 GLU A CB 1 ATOM 548 C CG . GLU A 1 70 ? 53.984 10.763 21.746 1.00 20.13 ? 87 GLU A CG 1 ATOM 549 C CD . GLU A 1 70 ? 53.458 12.102 22.228 1.00 23.52 ? 87 GLU A CD 1 ATOM 550 O OE1 . GLU A 1 70 ? 52.485 12.116 23.013 1.00 24.73 ? 87 GLU A OE1 1 ATOM 551 O OE2 . GLU A 1 70 ? 54.024 13.142 21.828 1.00 25.91 ? 87 GLU A OE2 1 ATOM 552 N N . LYS A 1 71 ? 51.943 6.762 21.190 1.00 16.63 ? 88 LYS A N 1 ATOM 553 C CA . LYS A 1 71 ? 50.837 5.815 21.063 1.00 17.45 ? 88 LYS A CA 1 ATOM 554 C C . LYS A 1 71 ? 49.821 6.079 22.175 1.00 17.45 ? 88 LYS A C 1 ATOM 555 O O . LYS A 1 71 ? 50.200 6.305 23.327 1.00 16.06 ? 88 LYS A O 1 ATOM 556 C CB . LYS A 1 71 ? 51.327 4.378 21.221 1.00 19.49 ? 88 LYS A CB 1 ATOM 557 C CG . LYS A 1 71 ? 52.451 3.946 20.310 1.00 25.56 ? 88 LYS A CG 1 ATOM 558 C CD . LYS A 1 71 ? 52.812 2.503 20.640 1.00 28.27 ? 88 LYS A CD 1 ATOM 559 C CE . LYS A 1 71 ? 54.041 2.034 19.895 1.00 30.97 ? 88 LYS A CE 1 ATOM 560 N NZ . LYS A 1 71 ? 54.379 0.633 20.281 1.00 32.05 ? 88 LYS A NZ 1 ATOM 561 N N . PHE A 1 72 ? 48.536 6.031 21.836 1.00 15.28 ? 89 PHE A N 1 ATOM 562 C CA . PHE A 1 72 ? 47.490 6.253 22.824 1.00 16.29 ? 89 PHE A CA 1 ATOM 563 C C . PHE A 1 72 ? 46.484 5.119 22.830 1.00 16.19 ? 89 PHE A C 1 ATOM 564 O O . PHE A 1 72 ? 45.839 4.846 21.821 1.00 15.58 ? 89 PHE A O 1 ATOM 565 C CB . PHE A 1 72 ? 46.752 7.567 22.557 1.00 15.72 ? 89 PHE A CB 1 ATOM 566 C CG . PHE A 1 72 ? 47.621 8.781 22.638 1.00 18.12 ? 89 PHE A CG 1 ATOM 567 C CD1 . PHE A 1 72 ? 48.473 9.115 21.594 1.00 18.25 ? 89 PHE A CD1 1 ATOM 568 C CD2 . PHE A 1 72 ? 47.583 9.603 23.758 1.00 19.51 ? 89 PHE A CD2 1 ATOM 569 C CE1 . PHE A 1 72 ? 49.273 10.256 21.664 1.00 19.41 ? 89 PHE A CE1 1 ATOM 570 C CE2 . PHE A 1 72 ? 48.380 10.742 23.834 1.00 20.56 ? 89 PHE A CE2 1 ATOM 571 C CZ . PHE A 1 72 ? 49.225 11.068 22.786 1.00 18.31 ? 89 PHE A CZ 1 ATOM 572 N N . ILE A 1 73 ? 46.360 4.462 23.977 1.00 17.31 ? 90 ILE A N 1 ATOM 573 C CA . ILE A 1 73 ? 45.422 3.362 24.162 1.00 17.61 ? 90 ILE A CA 1 ATOM 574 C C . ILE A 1 73 ? 44.450 3.822 25.255 1.00 18.16 ? 90 ILE A C 1 ATOM 575 O O . ILE A 1 73 ? 44.792 4.682 26.065 1.00 16.94 ? 90 ILE A O 1 ATOM 576 C CB . ILE A 1 73 ? 46.160 2.085 24.637 1.00 19.98 ? 90 ILE A CB 1 ATOM 577 C CG1 . ILE A 1 73 ? 47.210 1.668 23.604 1.00 21.53 ? 90 ILE A CG1 1 ATOM 578 C CG2 . ILE A 1 73 ? 45.179 0.959 24.859 1.00 19.88 ? 90 ILE A CG2 1 ATOM 579 C CD1 . ILE A 1 73 ? 46.637 1.122 22.316 1.00 21.88 ? 90 ILE A CD1 1 ATOM 580 N N . CYS A 1 74 ? 43.237 3.280 25.273 1.00 17.62 ? 91 CYS A N 1 ATOM 581 C CA . CYS A 1 74 ? 42.283 3.666 26.307 1.00 17.83 ? 91 CYS A CA 1 ATOM 582 C C . CYS A 1 74 ? 42.875 3.351 27.671 1.00 19.64 ? 91 CYS A C 1 ATOM 583 O O . CYS A 1 74 ? 43.364 2.249 27.901 1.00 17.38 ? 91 CYS A O 1 ATOM 584 C CB . CYS A 1 74 ? 40.969 2.906 26.153 1.00 17.44 ? 91 CYS A CB 1 ATOM 585 S SG . CYS A 1 74 ? 39.954 3.508 24.777 1.00 17.74 ? 91 CYS A SG 1 ATOM 586 N N . PRO A 1 75 ? 42.858 4.326 28.588 1.00 21.41 ? 92 PRO A N 1 ATOM 587 C CA . PRO A 1 75 ? 43.413 4.064 29.915 1.00 24.55 ? 92 PRO A CA 1 ATOM 588 C C . PRO A 1 75 ? 42.615 2.988 30.649 1.00 26.69 ? 92 PRO A C 1 ATOM 589 O O . PRO A 1 75 ? 43.169 2.197 31.410 1.00 26.95 ? 92 PRO A O 1 ATOM 590 C CB . PRO A 1 75 ? 43.340 5.431 30.594 1.00 25.10 ? 92 PRO A CB 1 ATOM 591 C CG . PRO A 1 75 ? 42.197 6.110 29.884 1.00 25.19 ? 92 PRO A CG 1 ATOM 592 C CD . PRO A 1 75 ? 42.437 5.730 28.458 1.00 21.73 ? 92 PRO A CD 1 ATOM 593 N N . ASN A 1 76 ? 41.314 2.946 30.393 1.00 28.88 ? 93 ASN A N 1 ATOM 594 C CA . ASN A 1 76 ? 40.445 1.975 31.042 1.00 32.05 ? 93 ASN A CA 1 ATOM 595 C C . ASN A 1 76 ? 40.198 0.727 30.200 1.00 33.65 ? 93 ASN A C 1 ATOM 596 O O . ASN A 1 76 ? 39.063 0.270 30.068 1.00 33.74 ? 93 ASN A O 1 ATOM 597 C CB . ASN A 1 76 ? 39.115 2.649 31.420 1.00 32.59 ? 93 ASN A CB 1 ATOM 598 C CG . ASN A 1 76 ? 38.523 3.478 30.282 1.00 32.38 ? 93 ASN A CG 1 ATOM 599 O OD1 . ASN A 1 76 ? 39.237 4.205 29.585 1.00 32.13 ? 93 ASN A OD1 1 ATOM 600 N ND2 . ASN A 1 76 ? 37.208 3.384 30.106 1.00 30.62 ? 93 ASN A ND2 1 ATOM 601 N N . LYS A 1 77 ? 41.269 0.169 29.644 1.00 35.33 ? 94 LYS A N 1 ATOM 602 C CA . LYS A 1 77 ? 41.161 -1.023 28.810 1.00 36.28 ? 94 LYS A CA 1 ATOM 603 C C . LYS A 1 77 ? 41.743 -2.273 29.447 1.00 38.54 ? 94 LYS A C 1 ATOM 604 O O . LYS A 1 77 ? 42.796 -2.227 30.082 1.00 38.92 ? 94 LYS A O 1 ATOM 605 C CB . LYS A 1 77 ? 41.853 -0.796 27.459 1.00 34.48 ? 94 LYS A CB 1 ATOM 606 C CG . LYS A 1 77 ? 42.129 -2.084 26.685 1.00 32.79 ? 94 LYS A CG 1 ATOM 607 C CD . LYS A 1 77 ? 42.699 -1.815 25.303 1.00 32.87 ? 94 LYS A CD 1 ATOM 608 C CE . LYS A 1 77 ? 43.249 -3.087 24.661 1.00 31.29 ? 94 LYS A CE 1 ATOM 609 N NZ . LYS A 1 77 ? 42.243 -4.186 24.571 1.00 32.06 ? 94 LYS A NZ 1 ATOM 610 N N . ASN A 1 78 ? 41.041 -3.389 29.272 1.00 40.46 ? 95 ASN A N 1 ATOM 611 C CA . ASN A 1 78 ? 41.505 -4.674 29.778 1.00 42.71 ? 95 ASN A CA 1 ATOM 612 C C . ASN A 1 78 ? 42.419 -5.196 28.673 1.00 43.24 ? 95 ASN A C 1 ATOM 613 O O . ASN A 1 78 ? 41.944 -5.597 27.613 1.00 43.88 ? 95 ASN A O 1 ATOM 614 C CB . ASN A 1 78 ? 40.332 -5.641 29.967 1.00 44.51 ? 95 ASN A CB 1 ATOM 615 C CG . ASN A 1 78 ? 40.780 -7.017 30.438 1.00 46.19 ? 95 ASN A CG 1 ATOM 616 O OD1 . ASN A 1 78 ? 41.960 -7.366 30.341 1.00 46.58 ? 95 ASN A OD1 1 ATOM 617 N ND2 . ASN A 1 78 ? 39.835 -7.811 30.939 1.00 46.73 ? 95 ASN A ND2 1 ATOM 618 N N . ASN A 1 79 A 43.723 -5.202 28.918 1.00 44.71 ? 95 ASN A N 1 ATOM 619 C CA . ASN A 1 79 A 44.675 -5.644 27.907 1.00 46.64 ? 95 ASN A CA 1 ATOM 620 C C . ASN A 1 79 A 44.643 -7.135 27.597 1.00 46.77 ? 95 ASN A C 1 ATOM 621 O O . ASN A 1 79 A 45.482 -7.635 26.843 1.00 45.94 ? 95 ASN A O 1 ATOM 622 C CB . ASN A 1 79 A 46.087 -5.223 28.310 1.00 48.39 ? 95 ASN A CB 1 ATOM 623 C CG . ASN A 1 79 A 46.225 -3.721 28.431 1.00 51.13 ? 95 ASN A CG 1 ATOM 624 O OD1 . ASN A 1 79 A 46.077 -2.991 27.448 1.00 52.94 ? 95 ASN A OD1 1 ATOM 625 N ND2 . ASN A 1 79 A 46.492 -3.247 29.644 1.00 51.61 ? 95 ASN A ND2 1 ATOM 626 N N . ASN A 1 80 ? 43.677 -7.844 28.172 1.00 47.29 ? 96 ASN A N 1 ATOM 627 C CA . ASN A 1 80 ? 43.540 -9.275 27.919 1.00 48.20 ? 96 ASN A CA 1 ATOM 628 C C . ASN A 1 80 ? 42.399 -9.558 26.943 1.00 47.28 ? 96 ASN A C 1 ATOM 629 O O . ASN A 1 80 ? 42.447 -10.537 26.197 1.00 48.00 ? 96 ASN A O 1 ATOM 630 C CB . ASN A 1 80 ? 43.302 -10.035 29.225 1.00 49.38 ? 96 ASN A CB 1 ATOM 631 C CG . ASN A 1 80 ? 44.577 -10.247 30.012 1.00 51.36 ? 96 ASN A CG 1 ATOM 632 O OD1 . ASN A 1 80 ? 45.568 -10.755 29.482 1.00 52.09 ? 96 ASN A OD1 1 ATOM 633 N ND2 . ASN A 1 80 ? 44.563 -9.861 31.285 1.00 51.84 ? 96 ASN A ND2 1 ATOM 634 N N . GLU A 1 81 ? 41.383 -8.696 26.957 1.00 44.96 ? 97 GLU A N 1 ATOM 635 C CA . GLU A 1 81 ? 40.232 -8.828 26.069 1.00 42.24 ? 97 GLU A CA 1 ATOM 636 C C . GLU A 1 81 ? 40.419 -8.004 24.798 1.00 39.01 ? 97 GLU A C 1 ATOM 637 O O . GLU A 1 81 ? 40.334 -6.775 24.815 1.00 37.36 ? 97 GLU A O 1 ATOM 638 C CB . GLU A 1 81 ? 38.956 -8.387 26.785 1.00 44.62 ? 97 GLU A CB 1 ATOM 639 C CG . GLU A 1 81 ? 38.542 -9.316 27.909 1.00 49.55 ? 97 GLU A CG 1 ATOM 640 C CD . GLU A 1 81 ? 38.471 -10.769 27.455 1.00 52.34 ? 97 GLU A CD 1 ATOM 641 O OE1 . GLU A 1 81 ? 37.759 -11.050 26.466 1.00 53.70 ? 97 GLU A OE1 1 ATOM 642 O OE2 . GLU A 1 81 ? 39.127 -11.619 28.089 1.00 55.11 ? 97 GLU A OE2 1 ATOM 643 N N . VAL A 1 82 ? 40.666 -8.700 23.693 1.00 35.47 ? 98 VAL A N 1 ATOM 644 C CA . VAL A 1 82 ? 40.883 -8.056 22.405 1.00 32.64 ? 98 VAL A CA 1 ATOM 645 C C . VAL A 1 82 ? 39.693 -7.219 21.950 1.00 29.47 ? 98 VAL A C 1 ATOM 646 O O . VAL A 1 82 ? 39.864 -6.173 21.325 1.00 27.96 ? 98 VAL A O 1 ATOM 647 C CB . VAL A 1 82 ? 41.185 -9.100 21.314 1.00 33.85 ? 98 VAL A CB 1 ATOM 648 C CG1 . VAL A 1 82 ? 41.566 -8.399 20.015 1.00 35.00 ? 98 VAL A CG1 1 ATOM 649 C CG2 . VAL A 1 82 ? 42.304 -10.017 21.774 1.00 35.13 ? 98 VAL A CG2 1 ATOM 650 N N . LEU A 1 83 ? 38.488 -7.676 22.266 1.00 25.08 ? 99 LEU A N 1 ATOM 651 C CA . LEU A 1 83 ? 37.292 -6.957 21.866 1.00 22.85 ? 99 LEU A CA 1 ATOM 652 C C . LEU A 1 83 ? 37.009 -5.726 22.717 1.00 20.76 ? 99 LEU A C 1 ATOM 653 O O . LEU A 1 83 ? 36.134 -4.927 22.386 1.00 22.26 ? 99 LEU A O 1 ATOM 654 C CB . LEU A 1 83 ? 36.088 -7.899 21.892 1.00 22.55 ? 99 LEU A CB 1 ATOM 655 C CG . LEU A 1 83 ? 35.973 -8.847 20.698 1.00 23.11 ? 99 LEU A CG 1 ATOM 656 C CD1 . LEU A 1 83 ? 34.829 -9.826 20.913 1.00 23.29 ? 99 LEU A CD1 1 ATOM 657 C CD2 . LEU A 1 83 ? 35.747 -8.029 19.433 1.00 22.34 ? 99 LEU A CD2 1 ATOM 658 N N . ASP A 1 84 ? 37.752 -5.568 23.806 1.00 18.17 ? 100 ASP A N 1 ATOM 659 C CA . ASP A 1 84 ? 37.553 -4.423 24.681 1.00 16.55 ? 100 ASP A CA 1 ATOM 660 C C . ASP A 1 84 ? 38.290 -3.179 24.196 1.00 14.75 ? 100 ASP A C 1 ATOM 661 O O . ASP A 1 84 ? 39.517 -3.137 24.194 1.00 14.29 ? 100 ASP A O 1 ATOM 662 C CB . ASP A 1 84 ? 38.004 -4.762 26.097 1.00 17.84 ? 100 ASP A CB 1 ATOM 663 C CG . ASP A 1 84 ? 37.768 -3.619 27.071 1.00 19.98 ? 100 ASP A CG 1 ATOM 664 O OD1 . ASP A 1 84 ? 36.669 -3.018 27.043 1.00 20.65 ? 100 ASP A OD1 1 ATOM 665 O OD2 . ASP A 1 84 ? 38.681 -3.328 27.869 1.00 21.75 ? 100 ASP A OD2 1 ATOM 666 N N . LYS A 1 85 ? 37.529 -2.174 23.775 1.00 12.92 ? 101 LYS A N 1 ATOM 667 C CA . LYS A 1 85 ? 38.094 -0.910 23.308 1.00 13.13 ? 101 LYS A CA 1 ATOM 668 C C . LYS A 1 85 ? 39.274 -1.142 22.364 1.00 13.63 ? 101 LYS A C 1 ATOM 669 O O . LYS A 1 85 ? 40.397 -0.713 22.639 1.00 13.49 ? 101 LYS A O 1 ATOM 670 C CB . LYS A 1 85 ? 38.551 -0.084 24.512 1.00 11.63 ? 101 LYS A CB 1 ATOM 671 C CG . LYS A 1 85 ? 37.486 0.088 25.594 1.00 13.85 ? 101 LYS A CG 1 ATOM 672 C CD . LYS A 1 85 ? 38.059 0.789 26.822 1.00 15.46 ? 101 LYS A CD 1 ATOM 673 C CE . LYS A 1 85 ? 37.036 0.905 27.942 1.00 16.61 ? 101 LYS A CE 1 ATOM 674 N NZ . LYS A 1 85 ? 36.636 -0.420 28.492 1.00 17.95 ? 101 LYS A NZ 1 ATOM 675 N N . ASP A 1 86 ? 39.013 -1.819 21.251 1.00 12.38 ? 102 ASP A N 1 ATOM 676 C CA . ASP A 1 86 ? 40.058 -2.119 20.282 1.00 11.85 ? 102 ASP A CA 1 ATOM 677 C C . ASP A 1 86 ? 40.321 -0.932 19.366 1.00 10.80 ? 102 ASP A C 1 ATOM 678 O O . ASP A 1 86 ? 39.925 -0.927 18.203 1.00 11.12 ? 102 ASP A O 1 ATOM 679 C CB . ASP A 1 86 ? 39.665 -3.346 19.459 1.00 11.47 ? 102 ASP A CB 1 ATOM 680 C CG . ASP A 1 86 ? 40.811 -3.877 18.620 1.00 14.33 ? 102 ASP A CG 1 ATOM 681 O OD1 . ASP A 1 86 ? 41.975 -3.489 18.875 1.00 11.89 ? 102 ASP A OD1 1 ATOM 682 O OD2 . ASP A 1 86 ? 40.548 -4.698 17.713 1.00 11.72 ? 102 ASP A OD2 1 ATOM 683 N N . ILE A 1 87 ? 40.987 0.079 19.909 1.00 11.15 ? 103 ILE A N 1 ATOM 684 C CA . ILE A 1 87 ? 41.318 1.280 19.154 1.00 11.75 ? 103 ILE A CA 1 ATOM 685 C C . ILE A 1 87 ? 42.621 1.872 19.680 1.00 12.47 ? 103 ILE A C 1 ATOM 686 O O . ILE A 1 87 ? 42.867 1.863 20.889 1.00 16.09 ? 103 ILE A O 1 ATOM 687 C CB . ILE A 1 87 ? 40.200 2.346 19.267 1.00 12.47 ? 103 ILE A CB 1 ATOM 688 C CG1 . ILE A 1 87 ? 40.583 3.586 18.447 1.00 13.50 ? 103 ILE A CG1 1 ATOM 689 C CG2 . ILE A 1 87 ? 39.974 2.725 20.730 1.00 11.14 ? 103 ILE A CG2 1 ATOM 690 C CD1 . ILE A 1 87 ? 39.504 4.649 18.386 1.00 15.19 ? 103 ILE A CD1 1 ATOM 691 N N . MET A 1 88 ? 43.464 2.356 18.772 1.00 11.11 ? 104 MET A N 1 ATOM 692 C CA . MET A 1 88 ? 44.730 2.975 19.151 1.00 12.69 ? 104 MET A CA 1 ATOM 693 C C . MET A 1 88 ? 45.004 4.205 18.285 1.00 13.04 ? 104 MET A C 1 ATOM 694 O O . MET A 1 88 ? 44.780 4.192 17.083 1.00 11.62 ? 104 MET A O 1 ATOM 695 C CB . MET A 1 88 ? 45.885 1.973 19.032 1.00 14.26 ? 104 MET A CB 1 ATOM 696 C CG . MET A 1 88 ? 47.262 2.586 19.282 1.00 15.32 ? 104 MET A CG 1 ATOM 697 S SD . MET A 1 88 ? 48.577 1.366 19.499 1.00 14.78 ? 104 MET A SD 1 ATOM 698 C CE . MET A 1 88 ? 48.768 0.761 17.830 1.00 15.33 ? 104 MET A CE 1 ATOM 699 N N . LEU A 1 89 ? 45.485 5.269 18.917 1.00 13.30 ? 105 LEU A N 1 ATOM 700 C CA . LEU A 1 89 ? 45.783 6.523 18.237 1.00 14.05 ? 105 LEU A CA 1 ATOM 701 C C . LEU A 1 89 ? 47.304 6.695 18.154 1.00 14.59 ? 105 LEU A C 1 ATOM 702 O O . LEU A 1 89 ? 48.009 6.515 19.146 1.00 14.73 ? 105 LEU A O 1 ATOM 703 C CB . LEU A 1 89 ? 45.144 7.668 19.028 1.00 16.45 ? 105 LEU A CB 1 ATOM 704 C CG . LEU A 1 89 ? 45.248 9.112 18.550 1.00 21.37 ? 105 LEU A CG 1 ATOM 705 C CD1 . LEU A 1 89 ? 44.553 9.286 17.208 1.00 22.96 ? 105 LEU A CD1 1 ATOM 706 C CD2 . LEU A 1 89 ? 44.606 10.021 19.601 1.00 21.87 ? 105 LEU A CD2 1 ATOM 707 N N . ILE A 1 90 ? 47.811 7.038 16.973 1.00 13.07 ? 106 ILE A N 1 ATOM 708 C CA . ILE A 1 90 ? 49.250 7.195 16.790 1.00 11.93 ? 106 ILE A CA 1 ATOM 709 C C . ILE A 1 90 ? 49.637 8.572 16.267 1.00 12.89 ? 106 ILE A C 1 ATOM 710 O O . ILE A 1 90 ? 49.108 9.023 15.250 1.00 12.54 ? 106 ILE A O 1 ATOM 711 C CB . ILE A 1 90 ? 49.813 6.172 15.768 1.00 12.01 ? 106 ILE A CB 1 ATOM 712 C CG1 . ILE A 1 90 ? 49.446 4.741 16.166 1.00 12.77 ? 106 ILE A CG1 1 ATOM 713 C CG2 . ILE A 1 90 ? 51.323 6.335 15.665 1.00 10.01 ? 106 ILE A CG2 1 ATOM 714 C CD1 . ILE A 1 90 ? 50.114 4.256 17.444 1.00 16.65 ? 106 ILE A CD1 1 ATOM 715 N N . LYS A 1 91 ? 50.558 9.239 16.956 1.00 11.96 ? 107 LYS A N 1 ATOM 716 C CA . LYS A 1 91 ? 51.024 10.538 16.491 1.00 13.73 ? 107 LYS A CA 1 ATOM 717 C C . LYS A 1 91 ? 52.304 10.276 15.692 1.00 13.28 ? 107 LYS A C 1 ATOM 718 O O . LYS A 1 91 ? 53.241 9.655 16.195 1.00 12.50 ? 107 LYS A O 1 ATOM 719 C CB . LYS A 1 91 ? 51.322 11.473 17.660 1.00 13.77 ? 107 LYS A CB 1 ATOM 720 C CG . LYS A 1 91 ? 51.809 12.843 17.203 1.00 15.48 ? 107 LYS A CG 1 ATOM 721 C CD . LYS A 1 91 ? 52.065 13.788 18.367 1.00 16.53 ? 107 LYS A CD 1 ATOM 722 C CE . LYS A 1 91 ? 52.304 15.197 17.847 1.00 19.30 ? 107 LYS A CE 1 ATOM 723 N NZ . LYS A 1 91 ? 52.466 16.191 18.936 1.00 21.32 ? 107 LYS A NZ 1 ATOM 724 N N . LEU A 1 92 ? 52.337 10.739 14.446 1.00 12.89 ? 108 LEU A N 1 ATOM 725 C CA . LEU A 1 92 ? 53.493 10.524 13.577 1.00 14.65 ? 108 LEU A CA 1 ATOM 726 C C . LEU A 1 92 ? 54.723 11.316 14.013 1.00 16.39 ? 108 LEU A C 1 ATOM 727 O O . LEU A 1 92 ? 54.600 12.387 14.608 1.00 17.06 ? 108 LEU A O 1 ATOM 728 C CB . LEU A 1 92 ? 53.129 10.891 12.136 1.00 14.77 ? 108 LEU A CB 1 ATOM 729 C CG . LEU A 1 92 ? 51.941 10.134 11.525 1.00 14.22 ? 108 LEU A CG 1 ATOM 730 C CD1 . LEU A 1 92 ? 51.750 10.592 10.093 1.00 15.37 ? 108 LEU A CD1 1 ATOM 731 C CD2 . LEU A 1 92 ? 52.181 8.624 11.572 1.00 14.66 ? 108 LEU A CD2 1 ATOM 732 N N . ASP A 1 93 ? 55.909 10.790 13.716 1.00 15.45 ? 109 ASP A N 1 ATOM 733 C CA . ASP A 1 93 ? 57.146 11.472 14.087 1.00 16.53 ? 109 ASP A CA 1 ATOM 734 C C . ASP A 1 93 ? 57.305 12.778 13.314 1.00 17.69 ? 109 ASP A C 1 ATOM 735 O O . ASP A 1 93 ? 57.934 13.714 13.801 1.00 16.91 ? 109 ASP A O 1 ATOM 736 C CB . ASP A 1 93 ? 58.348 10.558 13.856 1.00 17.25 ? 109 ASP A CB 1 ATOM 737 C CG . ASP A 1 93 ? 58.504 10.150 12.407 1.00 18.90 ? 109 ASP A CG 1 ATOM 738 O OD1 . ASP A 1 93 ? 57.498 9.784 11.765 1.00 17.96 ? 109 ASP A OD1 1 ATOM 739 O OD2 . ASP A 1 93 ? 59.643 10.185 11.914 1.00 22.09 ? 109 ASP A OD2 1 ATOM 740 N N . LYS A 1 94 ? 56.731 12.831 12.113 1.00 17.52 ? 110 LYS A N 1 ATOM 741 C CA . LYS A 1 94 ? 56.756 14.029 11.272 1.00 20.09 ? 110 LYS A CA 1 ATOM 742 C C . LYS A 1 94 ? 55.441 14.137 10.505 1.00 20.26 ? 110 LYS A C 1 ATOM 743 O O . LYS A 1 94 ? 54.858 13.125 10.110 1.00 19.48 ? 110 LYS A O 1 ATOM 744 C CB . LYS A 1 94 ? 57.892 13.991 10.248 1.00 22.83 ? 110 LYS A CB 1 ATOM 745 C CG . LYS A 1 94 ? 59.285 13.902 10.821 1.00 29.87 ? 110 LYS A CG 1 ATOM 746 C CD . LYS A 1 94 ? 60.295 14.484 9.843 1.00 34.97 ? 110 LYS A CD 1 ATOM 747 C CE . LYS A 1 94 ? 60.103 13.938 8.437 1.00 36.16 ? 110 LYS A CE 1 ATOM 748 N NZ . LYS A 1 94 ? 61.060 14.564 7.484 1.00 40.32 ? 110 LYS A NZ 1 ATOM 749 N N . PRO A 1 95 ? 54.965 15.371 10.276 1.00 20.16 ? 111 PRO A N 1 ATOM 750 C CA . PRO A 1 95 ? 53.716 15.615 9.553 1.00 20.03 ? 111 PRO A CA 1 ATOM 751 C C . PRO A 1 95 ? 53.784 15.144 8.109 1.00 20.85 ? 111 PRO A C 1 ATOM 752 O O . PRO A 1 95 ? 54.866 14.987 7.537 1.00 20.21 ? 111 PRO A O 1 ATOM 753 C CB . PRO A 1 95 ? 53.552 17.128 9.644 1.00 19.80 ? 111 PRO A CB 1 ATOM 754 C CG . PRO A 1 95 ? 54.261 17.469 10.912 1.00 21.43 ? 111 PRO A CG 1 ATOM 755 C CD . PRO A 1 95 ? 55.500 16.630 10.816 1.00 20.38 ? 111 PRO A CD 1 ATOM 756 N N . ILE A 1 96 ? 52.609 14.932 7.530 1.00 22.42 ? 112 ILE A N 1 ATOM 757 C CA . ILE A 1 96 ? 52.474 14.487 6.152 1.00 23.18 ? 112 ILE A CA 1 ATOM 758 C C . ILE A 1 96 ? 51.815 15.591 5.322 1.00 24.72 ? 112 ILE A C 1 ATOM 759 O O . ILE A 1 96 ? 50.929 16.293 5.808 1.00 25.64 ? 112 ILE A O 1 ATOM 760 C CB . ILE A 1 96 ? 51.613 13.191 6.098 1.00 24.63 ? 112 ILE A CB 1 ATOM 761 C CG1 . ILE A 1 96 ? 52.510 11.966 6.269 1.00 25.39 ? 112 ILE A CG1 1 ATOM 762 C CG2 . ILE A 1 96 ? 50.825 13.119 4.810 1.00 25.41 ? 112 ILE A CG2 1 ATOM 763 C CD1 . ILE A 1 96 ? 53.527 11.786 5.147 1.00 27.66 ? 112 ILE A CD1 1 ATOM 764 N N . SER A 1 97 ? 52.262 15.752 4.080 1.00 25.22 ? 113 SER A N 1 ATOM 765 C CA . SER A 1 97 ? 51.696 16.751 3.175 1.00 24.71 ? 113 SER A CA 1 ATOM 766 C C . SER A 1 97 ? 50.888 16.041 2.099 1.00 24.05 ? 113 SER A C 1 ATOM 767 O O . SER A 1 97 ? 51.259 14.955 1.654 1.00 23.87 ? 113 SER A O 1 ATOM 768 C CB . SER A 1 97 ? 52.801 17.567 2.498 1.00 25.12 ? 113 SER A CB 1 ATOM 769 O OG . SER A 1 97 ? 53.400 18.474 3.402 1.00 31.54 ? 113 SER A OG 1 ATOM 770 N N . ASN A 1 98 ? 49.789 16.657 1.678 1.00 22.01 ? 114 ASN A N 1 ATOM 771 C CA . ASN A 1 98 ? 48.946 16.071 0.647 1.00 20.36 ? 114 ASN A CA 1 ATOM 772 C C . ASN A 1 98 ? 49.710 15.883 -0.659 1.00 19.38 ? 114 ASN A C 1 ATOM 773 O O . ASN A 1 98 ? 50.490 16.743 -1.065 1.00 17.70 ? 114 ASN A O 1 ATOM 774 C CB . ASN A 1 98 ? 47.720 16.954 0.397 1.00 19.86 ? 114 ASN A CB 1 ATOM 775 C CG . ASN A 1 98 ? 46.641 16.760 1.440 1.00 19.44 ? 114 ASN A CG 1 ATOM 776 O OD1 . ASN A 1 98 ? 46.929 16.450 2.592 1.00 20.28 ? 114 ASN A OD1 1 ATOM 777 N ND2 . ASN A 1 98 ? 45.389 16.956 1.043 1.00 19.39 ? 114 ASN A ND2 1 ATOM 778 N N . SER A 1 99 ? 49.486 14.739 -1.298 1.00 18.68 ? 115 SER A N 1 ATOM 779 C CA . SER A 1 99 ? 50.109 14.412 -2.574 1.00 17.58 ? 115 SER A CA 1 ATOM 780 C C . SER A 1 99 ? 49.113 13.586 -3.374 1.00 17.45 ? 115 SER A C 1 ATOM 781 O O . SER A 1 99 ? 47.998 13.337 -2.919 1.00 17.76 ? 115 SER A O 1 ATOM 782 C CB . SER A 1 99 ? 51.402 13.617 -2.372 1.00 17.81 ? 115 SER A CB 1 ATOM 783 O OG . SER A 1 99 ? 51.153 12.353 -1.786 1.00 16.27 ? 115 SER A OG 1 ATOM 784 N N . LYS A 1 100 ? 49.519 13.166 -4.565 1.00 18.89 ? 116 LYS A N 1 ATOM 785 C CA . LYS A 1 100 ? 48.668 12.368 -5.441 1.00 19.28 ? 116 LYS A CA 1 ATOM 786 C C . LYS A 1 100 ? 47.982 11.219 -4.700 1.00 18.81 ? 116 LYS A C 1 ATOM 787 O O . LYS A 1 100 ? 46.762 11.066 -4.759 1.00 16.17 ? 116 LYS A O 1 ATOM 788 C CB . LYS A 1 100 ? 49.508 11.786 -6.582 1.00 22.50 ? 116 LYS A CB 1 ATOM 789 C CG . LYS A 1 100 ? 48.708 11.164 -7.724 1.00 25.34 ? 116 LYS A CG 1 ATOM 790 C CD . LYS A 1 100 ? 48.202 12.225 -8.680 1.00 30.21 ? 116 LYS A CD 1 ATOM 791 C CE . LYS A 1 100 ? 47.627 11.609 -9.951 1.00 34.18 ? 116 LYS A CE 1 ATOM 792 N NZ . LYS A 1 100 ? 46.432 10.765 -9.682 1.00 34.01 ? 116 LYS A NZ 1 ATOM 793 N N . HIS A 1 101 ? 48.770 10.423 -3.986 1.00 16.68 ? 117 HIS A N 1 ATOM 794 C CA . HIS A 1 101 ? 48.222 9.270 -3.288 1.00 16.85 ? 117 HIS A CA 1 ATOM 795 C C . HIS A 1 101 ? 48.158 9.373 -1.771 1.00 15.67 ? 117 HIS A C 1 ATOM 796 O O . HIS A 1 101 ? 48.042 8.354 -1.094 1.00 13.17 ? 117 HIS A O 1 ATOM 797 C CB . HIS A 1 101 ? 49.014 8.019 -3.688 1.00 16.55 ? 117 HIS A CB 1 ATOM 798 C CG . HIS A 1 101 ? 49.209 7.885 -5.166 1.00 17.06 ? 117 HIS A CG 1 ATOM 799 N ND1 . HIS A 1 101 ? 50.353 8.311 -5.808 1.00 15.44 ? 117 HIS A ND1 1 ATOM 800 C CD2 . HIS A 1 101 ? 48.379 7.435 -6.137 1.00 16.18 ? 117 HIS A CD2 1 ATOM 801 C CE1 . HIS A 1 101 ? 50.217 8.131 -7.109 1.00 15.87 ? 117 HIS A CE1 1 ATOM 802 N NE2 . HIS A 1 101 ? 49.028 7.602 -7.336 1.00 17.00 ? 117 HIS A NE2 1 ATOM 803 N N . ILE A 1 102 ? 48.219 10.593 -1.243 1.00 13.93 ? 118 ILE A N 1 ATOM 804 C CA . ILE A 1 102 ? 48.162 10.796 0.200 1.00 14.37 ? 118 ILE A CA 1 ATOM 805 C C . ILE A 1 102 ? 47.252 11.951 0.604 1.00 14.55 ? 118 ILE A C 1 ATOM 806 O O . ILE A 1 102 ? 47.405 13.077 0.131 1.00 13.92 ? 118 ILE A O 1 ATOM 807 C CB . ILE A 1 102 ? 49.560 11.063 0.784 1.00 12.46 ? 118 ILE A CB 1 ATOM 808 C CG1 . ILE A 1 102 ? 50.491 9.888 0.467 1.00 12.79 ? 118 ILE A CG1 1 ATOM 809 C CG2 . ILE A 1 102 ? 49.453 11.271 2.283 1.00 12.64 ? 118 ILE A CG2 1 ATOM 810 C CD1 . ILE A 1 102 ? 51.901 10.028 1.029 1.00 10.13 ? 118 ILE A CD1 1 ATOM 811 N N . ALA A 1 103 ? 46.305 11.658 1.488 1.00 15.14 ? 119 ALA A N 1 ATOM 812 C CA . ALA A 1 103 ? 45.364 12.656 1.980 1.00 16.15 ? 119 ALA A CA 1 ATOM 813 C C . ALA A 1 103 ? 44.575 12.057 3.135 1.00 15.91 ? 119 ALA A C 1 ATOM 814 O O . ALA A 1 103 ? 44.169 10.899 3.081 1.00 17.60 ? 119 ALA A O 1 ATOM 815 C CB . ALA A 1 103 ? 44.421 13.091 0.864 1.00 15.36 ? 119 ALA A CB 1 ATOM 816 N N . PRO A 1 104 ? 44.349 12.841 4.199 1.00 15.01 ? 120 PRO A N 1 ATOM 817 C CA . PRO A 1 104 ? 43.602 12.354 5.365 1.00 15.13 ? 120 PRO A CA 1 ATOM 818 C C . PRO A 1 104 ? 42.095 12.218 5.152 1.00 15.87 ? 120 PRO A C 1 ATOM 819 O O . PRO A 1 104 ? 41.539 12.762 4.201 1.00 15.93 ? 120 PRO A O 1 ATOM 820 C CB . PRO A 1 104 ? 43.950 13.375 6.445 1.00 15.34 ? 120 PRO A CB 1 ATOM 821 C CG . PRO A 1 104 ? 44.129 14.646 5.655 1.00 18.38 ? 120 PRO A CG 1 ATOM 822 C CD . PRO A 1 104 ? 44.905 14.185 4.443 1.00 14.51 ? 120 PRO A CD 1 ATOM 823 N N . LEU A 1 105 ? 41.449 11.470 6.037 1.00 14.64 ? 121 LEU A N 1 ATOM 824 C CA . LEU A 1 105 ? 40.005 11.261 5.980 1.00 17.92 ? 121 LEU A CA 1 ATOM 825 C C . LEU A 1 105 ? 39.517 11.687 7.362 1.00 17.58 ? 121 LEU A C 1 ATOM 826 O O . LEU A 1 105 ? 39.938 11.117 8.364 1.00 17.37 ? 121 LEU A O 1 ATOM 827 C CB . LEU A 1 105 ? 39.685 9.776 5.760 1.00 17.59 ? 121 LEU A CB 1 ATOM 828 C CG . LEU A 1 105 ? 38.426 9.373 4.988 1.00 21.70 ? 121 LEU A CG 1 ATOM 829 C CD1 . LEU A 1 105 ? 38.029 7.957 5.393 1.00 19.25 ? 121 LEU A CD1 1 ATOM 830 C CD2 . LEU A 1 105 ? 37.289 10.333 5.265 1.00 22.65 ? 121 LEU A CD2 1 ATOM 831 N N . SER A 1 106 ? 38.635 12.676 7.422 1.00 18.33 ? 122 SER A N 1 ATOM 832 C CA . SER A 1 106 ? 38.151 13.165 8.711 1.00 20.15 ? 122 SER A CA 1 ATOM 833 C C . SER A 1 106 ? 37.338 12.157 9.521 1.00 19.02 ? 122 SER A C 1 ATOM 834 O O . SER A 1 106 ? 36.844 11.156 8.996 1.00 17.88 ? 122 SER A O 1 ATOM 835 C CB . SER A 1 106 ? 37.320 14.440 8.515 1.00 22.02 ? 122 SER A CB 1 ATOM 836 O OG . SER A 1 106 ? 36.074 14.147 7.915 1.00 25.89 ? 122 SER A OG 1 ATOM 837 N N . LEU A 1 107 ? 37.220 12.440 10.815 1.00 17.61 ? 123 LEU A N 1 ATOM 838 C CA . LEU A 1 107 ? 36.462 11.611 11.739 1.00 16.45 ? 123 LEU A CA 1 ATOM 839 C C . LEU A 1 107 ? 34.984 11.725 11.368 1.00 16.40 ? 123 LEU A C 1 ATOM 840 O O . LEU A 1 107 ? 34.568 12.716 10.769 1.00 14.20 ? 123 LEU A O 1 ATOM 841 C CB . LEU A 1 107 ? 36.700 12.097 13.173 1.00 15.92 ? 123 LEU A CB 1 ATOM 842 C CG . LEU A 1 107 ? 38.142 11.934 13.675 1.00 16.55 ? 123 LEU A CG 1 ATOM 843 C CD1 . LEU A 1 107 ? 38.345 12.733 14.956 1.00 17.08 ? 123 LEU A CD1 1 ATOM 844 C CD2 . LEU A 1 107 ? 38.442 10.453 13.903 1.00 14.97 ? 123 LEU A CD2 1 ATOM 845 N N . PRO A 1 108 ? 34.168 10.713 11.714 1.00 15.87 ? 124 PRO A N 1 ATOM 846 C CA . PRO A 1 108 ? 32.744 10.781 11.372 1.00 18.12 ? 124 PRO A CA 1 ATOM 847 C C . PRO A 1 108 ? 32.014 11.906 12.093 1.00 21.34 ? 124 PRO A C 1 ATOM 848 O O . PRO A 1 108 ? 32.315 12.214 13.246 1.00 22.60 ? 124 PRO A O 1 ATOM 849 C CB . PRO A 1 108 ? 32.229 9.402 11.766 1.00 15.96 ? 124 PRO A CB 1 ATOM 850 C CG . PRO A 1 108 ? 33.089 9.049 12.928 1.00 15.22 ? 124 PRO A CG 1 ATOM 851 C CD . PRO A 1 108 ? 34.466 9.478 12.458 1.00 15.61 ? 124 PRO A CD 1 ATOM 852 N N . SER A 1 109 ? 31.057 12.517 11.404 1.00 24.38 ? 125 SER A N 1 ATOM 853 C CA . SER A 1 109 ? 30.284 13.611 11.975 1.00 27.99 ? 125 SER A CA 1 ATOM 854 C C . SER A 1 109 ? 28.899 13.148 12.411 1.00 29.46 ? 125 SER A C 1 ATOM 855 O O . SER A 1 109 ? 28.169 13.879 13.079 1.00 30.04 ? 125 SER A O 1 ATOM 856 C CB . SER A 1 109 ? 30.163 14.744 10.958 1.00 28.25 ? 125 SER A CB 1 ATOM 857 O OG . SER A 1 109 ? 29.732 14.244 9.708 1.00 31.14 ? 125 SER A OG 1 ATOM 858 N N . SER A 1 110 ? 28.543 11.926 12.032 1.00 30.17 ? 127 SER A N 1 ATOM 859 C CA . SER A 1 110 ? 27.250 11.363 12.399 1.00 30.75 ? 127 SER A CA 1 ATOM 860 C C . SER A 1 110 ? 27.372 9.855 12.612 1.00 30.90 ? 127 SER A C 1 ATOM 861 O O . SER A 1 110 ? 28.241 9.204 12.032 1.00 29.67 ? 127 SER A O 1 ATOM 862 C CB . SER A 1 110 ? 26.222 11.661 11.309 1.00 31.22 ? 127 SER A CB 1 ATOM 863 O OG . SER A 1 110 ? 26.687 11.213 10.050 1.00 33.94 ? 127 SER A OG 1 ATOM 864 N N . PRO A 1 111 ? 26.495 9.281 13.448 1.00 31.01 ? 128 PRO A N 1 ATOM 865 C CA . PRO A 1 111 ? 26.512 7.846 13.738 1.00 31.24 ? 128 PRO A CA 1 ATOM 866 C C . PRO A 1 111 ? 26.091 7.013 12.531 1.00 30.70 ? 128 PRO A C 1 ATOM 867 O O . PRO A 1 111 ? 25.319 7.469 11.691 1.00 30.79 ? 128 PRO A O 1 ATOM 868 C CB . PRO A 1 111 ? 25.523 7.728 14.889 1.00 31.27 ? 128 PRO A CB 1 ATOM 869 C CG . PRO A 1 111 ? 24.488 8.737 14.503 1.00 31.53 ? 128 PRO A CG 1 ATOM 870 C CD . PRO A 1 111 ? 25.332 9.926 14.086 1.00 31.56 ? 128 PRO A CD 1 ATOM 871 N N . PRO A 1 112 ? 26.594 5.777 12.434 1.00 30.12 ? 129 PRO A N 1 ATOM 872 C CA . PRO A 1 112 ? 26.241 4.910 11.307 1.00 29.61 ? 129 PRO A CA 1 ATOM 873 C C . PRO A 1 112 ? 24.762 4.531 11.315 1.00 28.58 ? 129 PRO A C 1 ATOM 874 O O . PRO A 1 112 ? 24.101 4.593 12.350 1.00 28.95 ? 129 PRO A O 1 ATOM 875 C CB . PRO A 1 112 ? 27.160 3.705 11.502 1.00 29.33 ? 129 PRO A CB 1 ATOM 876 C CG . PRO A 1 112 ? 27.294 3.629 12.987 1.00 29.65 ? 129 PRO A CG 1 ATOM 877 C CD . PRO A 1 112 ? 27.490 5.081 13.375 1.00 31.00 ? 129 PRO A CD 1 ATOM 878 N N . SER A 1 113 ? 24.248 4.148 10.153 1.00 27.05 ? 131 SER A N 1 ATOM 879 C CA . SER A 1 113 ? 22.851 3.755 10.020 1.00 25.96 ? 131 SER A CA 1 ATOM 880 C C . SER A 1 113 ? 22.754 2.332 9.469 1.00 24.59 ? 131 SER A C 1 ATOM 881 O O . SER A 1 113 ? 23.286 2.035 8.396 1.00 22.20 ? 131 SER A O 1 ATOM 882 C CB . SER A 1 113 ? 22.124 4.720 9.084 1.00 26.89 ? 131 SER A CB 1 ATOM 883 O OG . SER A 1 113 ? 20.810 4.264 8.814 1.00 32.76 ? 131 SER A OG 1 ATOM 884 N N . VAL A 1 114 ? 22.076 1.456 10.205 1.00 22.74 ? 132 VAL A N 1 ATOM 885 C CA . VAL A 1 114 ? 21.922 0.066 9.787 1.00 22.14 ? 132 VAL A CA 1 ATOM 886 C C . VAL A 1 114 ? 21.296 -0.014 8.399 1.00 21.22 ? 132 VAL A C 1 ATOM 887 O O . VAL A 1 114 ? 20.336 0.695 8.100 1.00 20.52 ? 132 VAL A O 1 ATOM 888 C CB . VAL A 1 114 ? 21.050 -0.730 10.796 1.00 22.69 ? 132 VAL A CB 1 ATOM 889 C CG1 . VAL A 1 114 ? 20.777 -2.134 10.266 1.00 23.92 ? 132 VAL A CG1 1 ATOM 890 C CG2 . VAL A 1 114 ? 21.766 -0.811 12.140 1.00 23.01 ? 132 VAL A CG2 1 ATOM 891 N N . GLY A 1 115 ? 21.859 -0.876 7.556 1.00 18.92 ? 133 GLY A N 1 ATOM 892 C CA . GLY A 1 115 ? 21.361 -1.037 6.203 1.00 17.58 ? 133 GLY A CA 1 ATOM 893 C C . GLY A 1 115 ? 22.209 -0.238 5.234 1.00 18.19 ? 133 GLY A C 1 ATOM 894 O O . GLY A 1 115 ? 22.145 -0.419 4.022 1.00 17.48 ? 133 GLY A O 1 ATOM 895 N N . SER A 1 116 ? 23.019 0.657 5.781 1.00 18.16 ? 134 SER A N 1 ATOM 896 C CA . SER A 1 116 ? 23.878 1.492 4.966 1.00 17.74 ? 134 SER A CA 1 ATOM 897 C C . SER A 1 116 ? 24.904 0.636 4.224 1.00 17.51 ? 134 SER A C 1 ATOM 898 O O . SER A 1 116 ? 25.297 -0.431 4.704 1.00 17.79 ? 134 SER A O 1 ATOM 899 C CB . SER A 1 116 ? 24.588 2.507 5.858 1.00 17.94 ? 134 SER A CB 1 ATOM 900 O OG . SER A 1 116 ? 25.319 3.428 5.079 1.00 28.85 ? 134 SER A OG 1 ATOM 901 N N . VAL A 1 117 ? 25.319 1.090 3.043 1.00 15.74 ? 135 VAL A N 1 ATOM 902 C CA . VAL A 1 117 ? 26.323 0.371 2.263 1.00 15.33 ? 135 VAL A CA 1 ATOM 903 C C . VAL A 1 117 ? 27.700 0.857 2.715 1.00 14.62 ? 135 VAL A C 1 ATOM 904 O O . VAL A 1 117 ? 27.935 2.058 2.797 1.00 13.99 ? 135 VAL A O 1 ATOM 905 C CB . VAL A 1 117 ? 26.166 0.634 0.750 1.00 14.99 ? 135 VAL A CB 1 ATOM 906 C CG1 . VAL A 1 117 ? 27.359 0.077 -0.007 1.00 16.18 ? 135 VAL A CG1 1 ATOM 907 C CG2 . VAL A 1 117 ? 24.901 -0.032 0.239 1.00 18.18 ? 135 VAL A CG2 1 ATOM 908 N N . CYS A 1 118 ? 28.600 -0.073 3.020 1.00 14.31 ? 136 CYS A N 1 ATOM 909 C CA . CYS A 1 118 ? 29.945 0.291 3.466 1.00 13.88 ? 136 CYS A CA 1 ATOM 910 C C . CYS A 1 118 ? 30.996 -0.367 2.587 1.00 13.60 ? 136 CYS A C 1 ATOM 911 O O . CYS A 1 118 ? 30.717 -1.355 1.913 1.00 14.67 ? 136 CYS A O 1 ATOM 912 C CB . CYS A 1 118 ? 30.166 -0.140 4.914 1.00 13.03 ? 136 CYS A CB 1 ATOM 913 S SG . CYS A 1 118 ? 28.884 0.375 6.104 1.00 13.24 ? 136 CYS A SG 1 ATOM 914 N N . ARG A 1 119 ? 32.206 0.178 2.601 1.00 12.30 ? 137 ARG A N 1 ATOM 915 C CA . ARG A 1 119 ? 33.283 -0.359 1.786 1.00 12.34 ? 137 ARG A CA 1 ATOM 916 C C . ARG A 1 119 ? 34.462 -0.757 2.670 1.00 13.16 ? 137 ARG A C 1 ATOM 917 O O . ARG A 1 119 ? 34.817 -0.036 3.608 1.00 14.13 ? 137 ARG A O 1 ATOM 918 C CB . ARG A 1 119 ? 33.713 0.698 0.761 1.00 14.05 ? 137 ARG A CB 1 ATOM 919 C CG . ARG A 1 119 ? 34.579 0.197 -0.402 1.00 16.01 ? 137 ARG A CG 1 ATOM 920 C CD . ARG A 1 119 ? 34.685 1.279 -1.479 1.00 13.80 ? 137 ARG A CD 1 ATOM 921 N NE . ARG A 1 119 ? 35.479 0.903 -2.650 1.00 13.66 ? 137 ARG A NE 1 ATOM 922 C CZ . ARG A 1 119 ? 35.206 -0.113 -3.470 1.00 14.55 ? 137 ARG A CZ 1 ATOM 923 N NH1 . ARG A 1 119 ? 34.152 -0.891 -3.258 1.00 14.79 ? 137 ARG A NH1 1 ATOM 924 N NH2 . ARG A 1 119 ? 35.974 -0.331 -4.529 1.00 12.51 ? 137 ARG A NH2 1 ATOM 925 N N . ILE A 1 120 ? 35.044 -1.921 2.392 1.00 10.57 ? 138 ILE A N 1 ATOM 926 C CA . ILE A 1 120 ? 36.197 -2.391 3.149 1.00 11.15 ? 138 ILE A CA 1 ATOM 927 C C . ILE A 1 120 ? 37.398 -2.466 2.212 1.00 10.52 ? 138 ILE A C 1 ATOM 928 O O . ILE A 1 120 ? 37.238 -2.603 1.000 1.00 9.92 ? 138 ILE A O 1 ATOM 929 C CB . ILE A 1 120 ? 35.948 -3.787 3.802 1.00 11.58 ? 138 ILE A CB 1 ATOM 930 C CG1 . ILE A 1 120 ? 35.437 -4.794 2.761 1.00 12.36 ? 138 ILE A CG1 1 ATOM 931 C CG2 . ILE A 1 120 ? 34.965 -3.644 4.955 1.00 10.11 ? 138 ILE A CG2 1 ATOM 932 C CD1 . ILE A 1 120 ? 35.209 -6.193 3.331 1.00 9.04 ? 138 ILE A CD1 1 ATOM 933 N N . MET A 1 121 ? 38.597 -2.376 2.777 1.00 10.87 ? 139 MET A N 1 ATOM 934 C CA . MET A 1 121 ? 39.821 -2.402 1.983 1.00 10.07 ? 139 MET A CA 1 ATOM 935 C C . MET A 1 121 ? 41.025 -2.836 2.809 1.00 11.14 ? 139 MET A C 1 ATOM 936 O O . MET A 1 121 ? 41.069 -2.621 4.023 1.00 10.05 ? 139 MET A O 1 ATOM 937 C CB . MET A 1 121 ? 40.087 -1.007 1.418 1.00 10.52 ? 139 MET A CB 1 ATOM 938 C CG . MET A 1 121 ? 40.286 0.051 2.496 1.00 10.55 ? 139 MET A CG 1 ATOM 939 S SD . MET A 1 121 ? 40.268 1.726 1.832 1.00 15.29 ? 139 MET A SD 1 ATOM 940 C CE . MET A 1 121 ? 38.555 1.891 1.377 1.00 13.14 ? 139 MET A CE 1 ATOM 941 N N . GLY A 1 122 ? 42.010 -3.428 2.141 1.00 10.44 ? 140 GLY A N 1 ATOM 942 C CA . GLY A 1 122 ? 43.203 -3.865 2.839 1.00 10.50 ? 140 GLY A CA 1 ATOM 943 C C . GLY A 1 122 ? 44.076 -4.796 2.022 1.00 12.14 ? 140 GLY A C 1 ATOM 944 O O . GLY A 1 122 ? 43.696 -5.229 0.927 1.00 9.99 ? 140 GLY A O 1 ATOM 945 N N . TRP A 1 123 ? 45.254 -5.097 2.562 1.00 10.94 ? 141 TRP A N 1 ATOM 946 C CA . TRP A 1 123 ? 46.199 -5.993 1.912 1.00 11.83 ? 141 TRP A CA 1 ATOM 947 C C . TRP A 1 123 ? 46.096 -7.366 2.581 1.00 12.59 ? 141 TRP A C 1 ATOM 948 O O . TRP A 1 123 ? 47.020 -8.175 2.507 1.00 10.74 ? 141 TRP A O 1 ATOM 949 C CB . TRP A 1 123 ? 47.629 -5.449 2.049 1.00 11.43 ? 141 TRP A CB 1 ATOM 950 C CG . TRP A 1 123 ? 47.914 -4.224 1.223 1.00 10.24 ? 141 TRP A CG 1 ATOM 951 C CD1 . TRP A 1 123 ? 48.342 -4.186 -0.074 1.00 11.99 ? 141 TRP A CD1 1 ATOM 952 C CD2 . TRP A 1 123 ? 47.811 -2.858 1.651 1.00 9.92 ? 141 TRP A CD2 1 ATOM 953 N NE1 . TRP A 1 123 ? 48.522 -2.877 -0.480 1.00 10.04 ? 141 TRP A NE1 1 ATOM 954 C CE2 . TRP A 1 123 ? 48.206 -2.045 0.563 1.00 10.80 ? 141 TRP A CE2 1 ATOM 955 C CE3 . TRP A 1 123 ? 47.432 -2.244 2.851 1.00 8.63 ? 141 TRP A CE3 1 ATOM 956 C CZ2 . TRP A 1 123 ? 48.225 -0.647 0.639 1.00 10.67 ? 141 TRP A CZ2 1 ATOM 957 C CZ3 . TRP A 1 123 ? 47.450 -0.856 2.927 1.00 12.31 ? 141 TRP A CZ3 1 ATOM 958 C CH2 . TRP A 1 123 ? 47.849 -0.073 1.827 1.00 11.39 ? 141 TRP A CH2 1 ATOM 959 N N . GLY A 1 124 ? 44.966 -7.618 3.238 1.00 12.95 ? 142 GLY A N 1 ATOM 960 C CA . GLY A 1 124 ? 44.764 -8.895 3.901 1.00 13.11 ? 142 GLY A CA 1 ATOM 961 C C . GLY A 1 124 ? 44.494 -10.026 2.916 1.00 14.18 ? 142 GLY A C 1 ATOM 962 O O . GLY A 1 124 ? 44.306 -9.794 1.720 1.00 12.71 ? 142 GLY A O 1 ATOM 963 N N . SER A 1 125 ? 44.457 -11.254 3.424 1.00 13.12 ? 143 SER A N 1 ATOM 964 C CA . SER A 1 125 ? 44.234 -12.431 2.591 1.00 13.64 ? 143 SER A CA 1 ATOM 965 C C . SER A 1 125 ? 42.999 -12.339 1.700 1.00 14.01 ? 143 SER A C 1 ATOM 966 O O . SER A 1 125 ? 41.927 -11.907 2.139 1.00 11.57 ? 143 SER A O 1 ATOM 967 C CB . SER A 1 125 ? 44.131 -13.680 3.476 1.00 14.57 ? 143 SER A CB 1 ATOM 968 O OG . SER A 1 125 ? 43.938 -14.850 2.699 1.00 14.72 ? 143 SER A OG 1 ATOM 969 N N . ILE A 1 126 ? 43.158 -12.751 0.444 1.00 13.35 ? 144 ILE A N 1 ATOM 970 C CA . ILE A 1 126 ? 42.053 -12.736 -0.502 1.00 13.74 ? 144 ILE A CA 1 ATOM 971 C C . ILE A 1 126 ? 41.419 -14.127 -0.642 1.00 15.65 ? 144 ILE A C 1 ATOM 972 O O . ILE A 1 126 ? 40.551 -14.331 -1.485 1.00 15.53 ? 144 ILE A O 1 ATOM 973 C CB . ILE A 1 126 ? 42.501 -12.226 -1.888 1.00 12.90 ? 144 ILE A CB 1 ATOM 974 C CG1 . ILE A 1 126 ? 43.589 -13.138 -2.461 1.00 13.77 ? 144 ILE A CG1 1 ATOM 975 C CG2 . ILE A 1 126 ? 43.017 -10.792 -1.765 1.00 11.82 ? 144 ILE A CG2 1 ATOM 976 C CD1 . ILE A 1 126 ? 43.956 -12.834 -3.905 1.00 13.53 ? 144 ILE A CD1 1 ATOM 977 N N . THR A 1 127 ? 41.860 -15.077 0.184 1.00 15.81 ? 145 THR A N 1 ATOM 978 C CA . THR A 1 127 ? 41.291 -16.431 0.186 1.00 19.07 ? 145 THR A CA 1 ATOM 979 C C . THR A 1 127 ? 40.791 -16.703 1.610 1.00 19.71 ? 145 THR A C 1 ATOM 980 O O . THR A 1 127 ? 41.496 -16.429 2.582 1.00 20.97 ? 145 THR A O 1 ATOM 981 C CB . THR A 1 127 ? 42.325 -17.505 -0.233 1.00 18.19 ? 145 THR A CB 1 ATOM 982 O OG1 . THR A 1 127 ? 43.555 -17.293 0.469 1.00 20.99 ? 145 THR A OG1 1 ATOM 983 C CG2 . THR A 1 127 ? 42.576 -17.441 -1.733 1.00 17.57 ? 145 THR A CG2 1 ATOM 984 N N . PRO A 1 128 ? 39.569 -17.250 1.745 1.00 20.94 ? 146 PRO A N 1 ATOM 985 C CA . PRO A 1 128 ? 38.906 -17.566 3.019 1.00 22.15 ? 146 PRO A CA 1 ATOM 986 C C . PRO A 1 128 ? 39.545 -18.545 4.006 1.00 23.14 ? 146 PRO A C 1 ATOM 987 O O . PRO A 1 128 ? 39.475 -18.331 5.218 1.00 22.46 ? 146 PRO A O 1 ATOM 988 C CB . PRO A 1 128 ? 37.517 -18.019 2.572 1.00 21.50 ? 146 PRO A CB 1 ATOM 989 C CG . PRO A 1 128 ? 37.801 -18.710 1.293 1.00 21.03 ? 146 PRO A CG 1 ATOM 990 C CD . PRO A 1 128 ? 38.773 -17.763 0.614 1.00 21.46 ? 146 PRO A CD 1 ATOM 991 N N . VAL A 1 129 ? 40.154 -19.612 3.504 1.00 23.75 ? 147 VAL A N 1 ATOM 992 C CA . VAL A 1 129 ? 40.774 -20.599 4.381 1.00 24.50 ? 147 VAL A CA 1 ATOM 993 C C . VAL A 1 129 ? 42.286 -20.415 4.369 1.00 25.72 ? 147 VAL A C 1 ATOM 994 O O . VAL A 1 129 ? 42.877 -19.953 5.351 1.00 23.34 ? 147 VAL A O 1 ATOM 995 C CB . VAL A 1 129 ? 40.439 -22.032 3.922 1.00 25.17 ? 147 VAL A CB 1 ATOM 996 C CG1 . VAL A 1 129 ? 40.861 -23.031 4.988 1.00 25.47 ? 147 VAL A CG1 1 ATOM 997 C CG2 . VAL A 1 129 ? 38.956 -22.146 3.630 1.00 26.03 ? 147 VAL A CG2 1 ATOM 998 N N . LYS A 1 130 ? 42.904 -20.795 3.254 1.00 25.00 ? 148 LYS A N 1 ATOM 999 C CA . LYS A 1 130 ? 44.339 -20.644 3.080 1.00 26.72 ? 148 LYS A CA 1 ATOM 1000 C C . LYS A 1 130 ? 44.627 -19.143 3.024 1.00 27.19 ? 148 LYS A C 1 ATOM 1001 O O . LYS A 1 130 ? 43.756 -18.357 2.657 1.00 26.31 ? 148 LYS A O 1 ATOM 1002 C CB . LYS A 1 130 ? 44.770 -21.310 1.770 1.00 29.13 ? 148 LYS A CB 1 ATOM 1003 C CG . LYS A 1 130 ? 46.191 -20.995 1.341 1.00 33.66 ? 148 LYS A CG 1 ATOM 1004 C CD . LYS A 1 130 ? 46.596 -21.811 0.123 1.00 36.08 ? 148 LYS A CD 1 ATOM 1005 C CE . LYS A 1 130 ? 45.675 -21.554 -1.059 1.00 37.87 ? 148 LYS A CE 1 ATOM 1006 N NZ . LYS A 1 130 ? 46.039 -22.413 -2.221 1.00 39.90 ? 148 LYS A NZ 1 ATOM 1007 N N . GLU A 1 131 ? 45.836 -18.738 3.394 1.00 26.26 ? 149 GLU A N 1 ATOM 1008 C CA . GLU A 1 131 ? 46.178 -17.324 3.358 1.00 26.82 ? 149 GLU A CA 1 ATOM 1009 C C . GLU A 1 131 ? 46.895 -16.949 2.073 1.00 26.67 ? 149 GLU A C 1 ATOM 1010 O O . GLU A 1 131 ? 47.932 -17.521 1.733 1.00 27.93 ? 149 GLU A O 1 ATOM 1011 C CB . GLU A 1 131 ? 47.042 -16.944 4.561 1.00 28.46 ? 149 GLU A CB 1 ATOM 1012 C CG . GLU A 1 131 ? 46.299 -17.016 5.880 1.00 32.37 ? 149 GLU A CG 1 ATOM 1013 C CD . GLU A 1 131 ? 47.105 -16.467 7.033 1.00 35.43 ? 149 GLU A CD 1 ATOM 1014 O OE1 . GLU A 1 131 ? 48.253 -16.923 7.223 1.00 37.14 ? 149 GLU A OE1 1 ATOM 1015 O OE2 . GLU A 1 131 ? 46.586 -15.583 7.750 1.00 37.44 ? 149 GLU A OE2 1 ATOM 1016 N N . THR A 1 132 ? 46.325 -15.981 1.365 1.00 24.46 ? 150 THR A N 1 ATOM 1017 C CA . THR A 1 132 ? 46.878 -15.495 0.111 1.00 23.48 ? 150 THR A CA 1 ATOM 1018 C C . THR A 1 132 ? 46.901 -13.972 0.170 1.00 22.73 ? 150 THR A C 1 ATOM 1019 O O . THR A 1 132 ? 45.863 -13.321 0.053 1.00 20.52 ? 150 THR A O 1 ATOM 1020 C CB . THR A 1 132 ? 46.014 -15.942 -1.078 1.00 24.07 ? 150 THR A CB 1 ATOM 1021 O OG1 . THR A 1 132 ? 45.990 -17.375 -1.130 1.00 25.54 ? 150 THR A OG1 1 ATOM 1022 C CG2 . THR A 1 132 ? 46.568 -15.389 -2.382 1.00 23.31 ? 150 THR A CG2 1 ATOM 1023 N N . PHE A 1 133 ? 48.088 -13.407 0.354 1.00 21.81 ? 151 PHE A N 1 ATOM 1024 C CA . PHE A 1 133 ? 48.239 -11.961 0.452 1.00 22.27 ? 151 PHE A CA 1 ATOM 1025 C C . PHE A 1 133 ? 48.572 -11.321 -0.890 1.00 21.29 ? 151 PHE A C 1 ATOM 1026 O O . PHE A 1 133 ? 49.527 -11.708 -1.558 1.00 23.03 ? 151 PHE A O 1 ATOM 1027 C CB . PHE A 1 133 ? 49.318 -11.642 1.488 1.00 22.90 ? 151 PHE A CB 1 ATOM 1028 C CG . PHE A 1 133 ? 49.016 -12.200 2.852 1.00 22.90 ? 151 PHE A CG 1 ATOM 1029 C CD1 . PHE A 1 133 ? 47.950 -11.702 3.598 1.00 21.35 ? 151 PHE A CD1 1 ATOM 1030 C CD2 . PHE A 1 133 ? 49.768 -13.251 3.375 1.00 23.87 ? 151 PHE A CD2 1 ATOM 1031 C CE1 . PHE A 1 133 ? 47.635 -12.240 4.840 1.00 20.58 ? 151 PHE A CE1 1 ATOM 1032 C CE2 . PHE A 1 133 ? 49.457 -13.801 4.625 1.00 23.83 ? 151 PHE A CE2 1 ATOM 1033 C CZ . PHE A 1 133 ? 48.385 -13.290 5.357 1.00 22.05 ? 151 PHE A CZ 1 ATOM 1034 N N . PRO A 1 134 ? 47.777 -10.327 -1.302 1.00 20.54 ? 152 PRO A N 1 ATOM 1035 C CA . PRO A 1 134 ? 47.968 -9.619 -2.568 1.00 19.19 ? 152 PRO A CA 1 ATOM 1036 C C . PRO A 1 134 ? 49.045 -8.540 -2.533 1.00 19.43 ? 152 PRO A C 1 ATOM 1037 O O . PRO A 1 134 ? 49.456 -8.090 -1.464 1.00 19.53 ? 152 PRO A O 1 ATOM 1038 C CB . PRO A 1 134 ? 46.586 -9.036 -2.835 1.00 18.93 ? 152 PRO A CB 1 ATOM 1039 C CG . PRO A 1 134 ? 46.129 -8.665 -1.462 1.00 19.05 ? 152 PRO A CG 1 ATOM 1040 C CD . PRO A 1 134 ? 46.549 -9.870 -0.626 1.00 19.98 ? 152 PRO A CD 1 ATOM 1041 N N . ASP A 1 135 ? 49.499 -8.134 -3.715 1.00 19.88 ? 153 ASP A N 1 ATOM 1042 C CA . ASP A 1 135 ? 50.503 -7.088 -3.819 1.00 21.04 ? 153 ASP A CA 1 ATOM 1043 C C . ASP A 1 135 ? 49.812 -5.734 -3.901 1.00 18.77 ? 153 ASP A C 1 ATOM 1044 O O . ASP A 1 135 ? 50.443 -4.688 -3.776 1.00 18.89 ? 153 ASP A O 1 ATOM 1045 C CB . ASP A 1 135 ? 51.377 -7.300 -5.052 1.00 22.93 ? 153 ASP A CB 1 ATOM 1046 C CG . ASP A 1 135 ? 52.256 -8.518 -4.929 1.00 26.62 ? 153 ASP A CG 1 ATOM 1047 O OD1 . ASP A 1 135 ? 52.881 -8.678 -3.857 1.00 28.34 ? 153 ASP A OD1 1 ATOM 1048 O OD2 . ASP A 1 135 ? 52.327 -9.308 -5.896 1.00 27.80 ? 153 ASP A OD2 1 ATOM 1049 N N . VAL A 1 136 ? 48.504 -5.772 -4.121 1.00 17.98 ? 154 VAL A N 1 ATOM 1050 C CA . VAL A 1 136 ? 47.691 -4.568 -4.213 1.00 15.85 ? 154 VAL A CA 1 ATOM 1051 C C . VAL A 1 136 ? 46.529 -4.714 -3.237 1.00 15.15 ? 154 VAL A C 1 ATOM 1052 O O . VAL A 1 136 ? 46.105 -5.825 -2.930 1.00 14.66 ? 154 VAL A O 1 ATOM 1053 C CB . VAL A 1 136 ? 47.133 -4.375 -5.642 1.00 18.63 ? 154 VAL A CB 1 ATOM 1054 C CG1 . VAL A 1 136 ? 48.267 -4.041 -6.607 1.00 17.51 ? 154 VAL A CG1 1 ATOM 1055 C CG2 . VAL A 1 136 ? 46.412 -5.643 -6.092 1.00 17.72 ? 154 VAL A CG2 1 ATOM 1056 N N . PRO A 1 137 ? 46.008 -3.594 -2.719 1.00 13.46 ? 155 PRO A N 1 ATOM 1057 C CA . PRO A 1 137 ? 44.888 -3.698 -1.778 1.00 13.96 ? 155 PRO A CA 1 ATOM 1058 C C . PRO A 1 137 ? 43.583 -4.059 -2.493 1.00 13.79 ? 155 PRO A C 1 ATOM 1059 O O . PRO A 1 137 ? 43.330 -3.594 -3.599 1.00 15.47 ? 155 PRO A O 1 ATOM 1060 C CB . PRO A 1 137 ? 44.839 -2.307 -1.155 1.00 12.52 ? 155 PRO A CB 1 ATOM 1061 C CG . PRO A 1 137 ? 45.249 -1.426 -2.311 1.00 11.92 ? 155 PRO A CG 1 ATOM 1062 C CD . PRO A 1 137 ? 46.415 -2.190 -2.911 1.00 10.96 ? 155 PRO A CD 1 ATOM 1063 N N . TYR A 1 138 ? 42.768 -4.904 -1.871 1.00 13.67 ? 156 TYR A N 1 ATOM 1064 C CA . TYR A 1 138 ? 41.488 -5.279 -2.452 1.00 13.28 ? 156 TYR A CA 1 ATOM 1065 C C . TYR A 1 138 ? 40.366 -4.530 -1.737 1.00 13.36 ? 156 TYR A C 1 ATOM 1066 O O . TYR A 1 138 ? 40.496 -4.188 -0.565 1.00 13.63 ? 156 TYR A O 1 ATOM 1067 C CB . TYR A 1 138 ? 41.268 -6.793 -2.359 1.00 12.31 ? 156 TYR A CB 1 ATOM 1068 C CG . TYR A 1 138 ? 41.850 -7.537 -3.538 1.00 14.00 ? 156 TYR A CG 1 ATOM 1069 C CD1 . TYR A 1 138 ? 43.214 -7.464 -3.827 1.00 14.22 ? 156 TYR A CD1 1 ATOM 1070 C CD2 . TYR A 1 138 ? 41.032 -8.283 -4.388 1.00 13.68 ? 156 TYR A CD2 1 ATOM 1071 C CE1 . TYR A 1 138 ? 43.751 -8.111 -4.937 1.00 15.45 ? 156 TYR A CE1 1 ATOM 1072 C CE2 . TYR A 1 138 ? 41.557 -8.937 -5.498 1.00 17.00 ? 156 TYR A CE2 1 ATOM 1073 C CZ . TYR A 1 138 ? 42.918 -8.844 -5.768 1.00 17.12 ? 156 TYR A CZ 1 ATOM 1074 O OH . TYR A 1 138 ? 43.441 -9.476 -6.871 1.00 19.90 ? 156 TYR A OH 1 ATOM 1075 N N . CYS A 1 139 ? 39.280 -4.277 -2.467 1.00 13.17 ? 157 CYS A N 1 ATOM 1076 C CA . CYS A 1 139 ? 38.108 -3.558 -1.975 1.00 11.86 ? 157 CYS A CA 1 ATOM 1077 C C . CYS A 1 139 ? 36.828 -4.347 -2.222 1.00 12.21 ? 157 CYS A C 1 ATOM 1078 O O . CYS A 1 139 ? 36.731 -5.108 -3.187 1.00 10.60 ? 157 CYS A O 1 ATOM 1079 C CB . CYS A 1 139 ? 37.982 -2.206 -2.687 1.00 12.61 ? 157 CYS A CB 1 ATOM 1080 S SG . CYS A 1 139 ? 39.003 -0.883 -1.976 1.00 11.48 ? 157 CYS A SG 1 ATOM 1081 N N . ALA A 1 140 ? 35.843 -4.135 -1.353 1.00 11.98 ? 158 ALA A N 1 ATOM 1082 C CA . ALA A 1 140 ? 34.552 -4.801 -1.455 1.00 12.71 ? 158 ALA A CA 1 ATOM 1083 C C . ALA A 1 140 ? 33.475 -3.974 -0.752 1.00 12.53 ? 158 ALA A C 1 ATOM 1084 O O . ALA A 1 140 ? 33.753 -3.263 0.216 1.00 14.63 ? 158 ALA A O 1 ATOM 1085 C CB . ALA A 1 140 ? 34.630 -6.202 -0.829 1.00 8.85 ? 158 ALA A CB 1 ATOM 1086 N N . ASN A 1 141 ? 32.247 -4.072 -1.249 1.00 13.13 ? 159 ASN A N 1 ATOM 1087 C CA . ASN A 1 141 ? 31.111 -3.364 -0.672 1.00 12.51 ? 159 ASN A CA 1 ATOM 1088 C C . ASN A 1 141 ? 30.291 -4.344 0.162 1.00 12.43 ? 159 ASN A C 1 ATOM 1089 O O . ASN A 1 141 ? 30.019 -5.464 -0.282 1.00 9.88 ? 159 ASN A O 1 ATOM 1090 C CB . ASN A 1 141 ? 30.215 -2.805 -1.778 1.00 13.99 ? 159 ASN A CB 1 ATOM 1091 C CG . ASN A 1 141 ? 30.867 -1.686 -2.558 1.00 15.67 ? 159 ASN A CG 1 ATOM 1092 O OD1 . ASN A 1 141 ? 30.655 -1.555 -3.765 1.00 18.74 ? 159 ASN A OD1 1 ATOM 1093 N ND2 . ASN A 1 141 ? 31.646 -0.861 -1.876 1.00 12.61 ? 159 ASN A ND2 1 ATOM 1094 N N . ILE A 1 142 ? 29.911 -3.931 1.367 1.00 10.28 ? 160 ILE A N 1 ATOM 1095 C CA . ILE A 1 142 ? 29.086 -4.764 2.236 1.00 11.73 ? 160 ILE A CA 1 ATOM 1096 C C . ILE A 1 142 ? 28.047 -3.866 2.896 1.00 11.72 ? 160 ILE A C 1 ATOM 1097 O O . ILE A 1 142 ? 27.984 -2.673 2.596 1.00 12.42 ? 160 ILE A O 1 ATOM 1098 C CB . ILE A 1 142 ? 29.926 -5.484 3.328 1.00 12.67 ? 160 ILE A CB 1 ATOM 1099 C CG1 . ILE A 1 142 ? 30.681 -4.461 4.180 1.00 12.28 ? 160 ILE A CG1 1 ATOM 1100 C CG2 . ILE A 1 142 ? 30.899 -6.469 2.671 1.00 11.83 ? 160 ILE A CG2 1 ATOM 1101 C CD1 . ILE A 1 142 ? 31.489 -5.088 5.315 1.00 12.34 ? 160 ILE A CD1 1 ATOM 1102 N N . ASN A 1 143 ? 27.240 -4.430 3.789 1.00 11.41 ? 161 ASN A N 1 ATOM 1103 C CA . ASN A 1 143 ? 26.200 -3.663 4.471 1.00 13.08 ? 161 ASN A CA 1 ATOM 1104 C C . ASN A 1 143 ? 26.371 -3.619 5.978 1.00 14.68 ? 161 ASN A C 1 ATOM 1105 O O . ASN A 1 143 ? 26.923 -4.543 6.583 1.00 15.49 ? 161 ASN A O 1 ATOM 1106 C CB . ASN A 1 143 ? 24.821 -4.254 4.188 1.00 14.73 ? 161 ASN A CB 1 ATOM 1107 C CG . ASN A 1 143 ? 24.508 -4.316 2.724 1.00 17.78 ? 161 ASN A CG 1 ATOM 1108 O OD1 . ASN A 1 143 ? 24.577 -3.312 2.027 1.00 20.39 ? 161 ASN A OD1 1 ATOM 1109 N ND2 . ASN A 1 143 ? 24.153 -5.500 2.244 1.00 18.63 ? 161 ASN A ND2 1 ATOM 1110 N N . LEU A 1 144 ? 25.884 -2.541 6.583 1.00 14.60 ? 162 LEU A N 1 ATOM 1111 C CA . LEU A 1 144 ? 25.936 -2.404 8.028 1.00 15.52 ? 162 LEU A CA 1 ATOM 1112 C C . LEU A 1 144 ? 24.736 -3.208 8.507 1.00 16.02 ? 162 LEU A C 1 ATOM 1113 O O . LEU A 1 144 ? 23.600 -2.910 8.138 1.00 15.80 ? 162 LEU A O 1 ATOM 1114 C CB . LEU A 1 144 ? 25.779 -0.944 8.440 1.00 16.23 ? 162 LEU A CB 1 ATOM 1115 C CG . LEU A 1 144 ? 26.098 -0.652 9.904 1.00 18.46 ? 162 LEU A CG 1 ATOM 1116 C CD1 . LEU A 1 144 ? 27.582 -0.868 10.156 1.00 17.19 ? 162 LEU A CD1 1 ATOM 1117 C CD2 . LEU A 1 144 ? 25.717 0.777 10.231 1.00 22.08 ? 162 LEU A CD2 1 ATOM 1118 N N . LEU A 1 145 ? 24.991 -4.227 9.320 1.00 14.01 ? 163 LEU A N 1 ATOM 1119 C CA . LEU A 1 145 ? 23.940 -5.102 9.826 1.00 15.31 ? 163 LEU A CA 1 ATOM 1120 C C . LEU A 1 145 ? 23.470 -4.772 11.232 1.00 15.03 ? 163 LEU A C 1 ATOM 1121 O O . LEU A 1 145 ? 24.130 -4.045 11.973 1.00 16.21 ? 163 LEU A O 1 ATOM 1122 C CB . LEU A 1 145 ? 24.430 -6.552 9.808 1.00 13.55 ? 163 LEU A CB 1 ATOM 1123 C CG . LEU A 1 145 ? 24.886 -7.121 8.462 1.00 17.14 ? 163 LEU A CG 1 ATOM 1124 C CD1 . LEU A 1 145 ? 25.533 -8.487 8.684 1.00 16.05 ? 163 LEU A CD1 1 ATOM 1125 C CD2 . LEU A 1 145 ? 23.694 -7.233 7.513 1.00 17.40 ? 163 LEU A CD2 1 ATOM 1126 N N . ASP A 1 146 ? 22.319 -5.323 11.598 1.00 17.64 ? 164 ASP A N 1 ATOM 1127 C CA . ASP A 1 146 ? 21.779 -5.120 12.935 1.00 19.24 ? 164 ASP A CA 1 ATOM 1128 C C . ASP A 1 146 ? 22.746 -5.787 13.910 1.00 18.85 ? 164 ASP A C 1 ATOM 1129 O O . ASP A 1 146 ? 23.195 -6.913 13.678 1.00 18.91 ? 164 ASP A O 1 ATOM 1130 C CB . ASP A 1 146 ? 20.400 -5.766 13.060 1.00 23.14 ? 164 ASP A CB 1 ATOM 1131 C CG . ASP A 1 146 ? 19.678 -5.346 14.323 1.00 27.58 ? 164 ASP A CG 1 ATOM 1132 O OD1 . ASP A 1 146 ? 20.248 -5.515 15.422 1.00 29.27 ? 164 ASP A OD1 1 ATOM 1133 O OD2 . ASP A 1 146 ? 18.539 -4.842 14.216 1.00 31.36 ? 164 ASP A OD2 1 ATOM 1134 N N . HIS A 1 147 ? 23.068 -5.092 14.995 1.00 19.37 ? 165 HIS A N 1 ATOM 1135 C CA . HIS A 1 147 ? 23.999 -5.609 15.995 1.00 20.24 ? 165 HIS A CA 1 ATOM 1136 C C . HIS A 1 147 ? 23.629 -6.999 16.516 1.00 19.56 ? 165 HIS A C 1 ATOM 1137 O O . HIS A 1 147 ? 24.503 -7.785 16.873 1.00 17.38 ? 165 HIS A O 1 ATOM 1138 C CB . HIS A 1 147 ? 24.086 -4.647 17.174 1.00 23.26 ? 165 HIS A CB 1 ATOM 1139 C CG . HIS A 1 147 ? 25.088 -5.058 18.208 1.00 28.64 ? 165 HIS A CG 1 ATOM 1140 N ND1 . HIS A 1 147 ? 26.448 -4.956 18.006 1.00 30.50 ? 165 HIS A ND1 1 ATOM 1141 C CD2 . HIS A 1 147 ? 24.928 -5.597 19.439 1.00 29.53 ? 165 HIS A CD2 1 ATOM 1142 C CE1 . HIS A 1 147 ? 27.083 -5.415 19.070 1.00 29.93 ? 165 HIS A CE1 1 ATOM 1143 N NE2 . HIS A 1 147 ? 26.185 -5.811 19.953 1.00 32.03 ? 165 HIS A NE2 1 ATOM 1144 N N . ALA A 1 148 ? 22.333 -7.291 16.561 1.00 20.03 ? 166 ALA A N 1 ATOM 1145 C CA . ALA A 1 148 ? 21.854 -8.585 17.041 1.00 20.44 ? 166 ALA A CA 1 ATOM 1146 C C . ALA A 1 148 ? 22.433 -9.741 16.231 1.00 19.51 ? 166 ALA A C 1 ATOM 1147 O O . ALA A 1 148 ? 22.601 -10.845 16.749 1.00 19.26 ? 166 ALA A O 1 ATOM 1148 C CB . ALA A 1 148 ? 20.331 -8.632 16.989 1.00 20.66 ? 166 ALA A CB 1 ATOM 1149 N N . VAL A 1 149 ? 22.736 -9.486 14.961 1.00 17.97 ? 167 VAL A N 1 ATOM 1150 C CA . VAL A 1 149 ? 23.286 -10.523 14.101 1.00 17.52 ? 167 VAL A CA 1 ATOM 1151 C C . VAL A 1 149 ? 24.643 -10.993 14.609 1.00 16.91 ? 167 VAL A C 1 ATOM 1152 O O . VAL A 1 149 ? 24.874 -12.197 14.744 1.00 16.28 ? 167 VAL A O 1 ATOM 1153 C CB . VAL A 1 149 ? 23.446 -10.037 12.643 1.00 18.89 ? 167 VAL A CB 1 ATOM 1154 C CG1 . VAL A 1 149 ? 23.937 -11.190 11.771 1.00 17.67 ? 167 VAL A CG1 1 ATOM 1155 C CG2 . VAL A 1 149 ? 22.117 -9.497 12.118 1.00 17.27 ? 167 VAL A CG2 1 ATOM 1156 N N . CYS A 1 150 ? 25.539 -10.050 14.888 1.00 14.38 ? 168 CYS A N 1 ATOM 1157 C CA . CYS A 1 150 ? 26.859 -10.407 15.385 1.00 13.53 ? 168 CYS A CA 1 ATOM 1158 C C . CYS A 1 150 ? 26.757 -11.007 16.782 1.00 14.67 ? 168 CYS A C 1 ATOM 1159 O O . CYS A 1 150 ? 27.484 -11.945 17.114 1.00 12.02 ? 168 CYS A O 1 ATOM 1160 C CB . CYS A 1 150 ? 27.775 -9.185 15.395 1.00 12.90 ? 168 CYS A CB 1 ATOM 1161 S SG . CYS A 1 150 ? 28.498 -8.779 13.771 1.00 13.13 ? 168 CYS A SG 1 ATOM 1162 N N . GLN A 1 151 ? 25.849 -10.470 17.593 1.00 14.78 ? 169 GLN A N 1 ATOM 1163 C CA . GLN A 1 151 ? 25.643 -10.971 18.950 1.00 18.75 ? 169 GLN A CA 1 ATOM 1164 C C . GLN A 1 151 ? 25.275 -12.454 18.933 1.00 18.07 ? 169 GLN A C 1 ATOM 1165 O O . GLN A 1 151 ? 25.769 -13.235 19.747 1.00 16.65 ? 169 GLN A O 1 ATOM 1166 C CB . GLN A 1 151 ? 24.536 -10.182 19.649 1.00 21.74 ? 169 GLN A CB 1 ATOM 1167 C CG . GLN A 1 151 ? 24.976 -8.847 20.215 1.00 31.08 ? 169 GLN A CG 1 ATOM 1168 C CD . GLN A 1 151 ? 25.766 -8.996 21.505 1.00 36.85 ? 169 GLN A CD 1 ATOM 1169 O OE1 . GLN A 1 151 ? 25.270 -9.547 22.491 1.00 39.48 ? 169 GLN A OE1 1 ATOM 1170 N NE2 . GLN A 1 151 ? 27.000 -8.506 21.504 1.00 38.97 ? 169 GLN A NE2 1 ATOM 1171 N N . ALA A 1 152 ? 24.409 -12.841 18.003 1.00 17.94 ? 170 ALA A N 1 ATOM 1172 C CA . ALA A 1 152 ? 23.997 -14.236 17.909 1.00 18.47 ? 170 ALA A CA 1 ATOM 1173 C C . ALA A 1 152 ? 25.119 -15.117 17.363 1.00 17.82 ? 170 ALA A C 1 ATOM 1174 O O . ALA A 1 152 ? 25.174 -16.313 17.648 1.00 18.02 ? 170 ALA A O 1 ATOM 1175 C CB . ALA A 1 152 ? 22.762 -14.360 17.027 1.00 16.98 ? 170 ALA A CB 1 ATOM 1176 N N . GLY A 1 153 ? 26.019 -14.520 16.588 1.00 17.34 ? 171 GLY A N 1 ATOM 1177 C CA . GLY A 1 153 ? 27.099 -15.291 16.004 1.00 15.92 ? 171 GLY A CA 1 ATOM 1178 C C . GLY A 1 153 ? 28.357 -15.431 16.840 1.00 16.05 ? 171 GLY A C 1 ATOM 1179 O O . GLY A 1 153 ? 29.149 -16.341 16.605 1.00 14.59 ? 171 GLY A O 1 ATOM 1180 N N . TYR A 1 154 ? 28.550 -14.542 17.809 1.00 14.92 ? 172 TYR A N 1 ATOM 1181 C CA . TYR A 1 154 ? 29.743 -14.586 18.653 1.00 15.67 ? 172 TYR A CA 1 ATOM 1182 C C . TYR A 1 154 ? 29.405 -14.548 20.140 1.00 16.61 ? 172 TYR A C 1 ATOM 1183 O O . TYR A 1 154 ? 28.967 -13.520 20.660 1.00 15.78 ? 172 TYR A O 1 ATOM 1184 C CB . TYR A 1 154 ? 30.653 -13.403 18.335 1.00 15.00 ? 172 TYR A CB 1 ATOM 1185 C CG . TYR A 1 154 ? 31.155 -13.353 16.908 1.00 17.83 ? 172 TYR A CG 1 ATOM 1186 C CD1 . TYR A 1 154 ? 32.350 -13.976 16.539 1.00 17.84 ? 172 TYR A CD1 1 ATOM 1187 C CD2 . TYR A 1 154 ? 30.454 -12.648 15.932 1.00 15.22 ? 172 TYR A CD2 1 ATOM 1188 C CE1 . TYR A 1 154 ? 32.833 -13.885 15.237 1.00 18.22 ? 172 TYR A CE1 1 ATOM 1189 C CE2 . TYR A 1 154 ? 30.928 -12.555 14.636 1.00 15.57 ? 172 TYR A CE2 1 ATOM 1190 C CZ . TYR A 1 154 ? 32.113 -13.168 14.293 1.00 15.34 ? 172 TYR A CZ 1 ATOM 1191 O OH . TYR A 1 154 ? 32.582 -13.042 13.011 1.00 16.71 ? 172 TYR A OH 1 ATOM 1192 N N . PRO A 1 155 A 29.609 -15.670 20.844 1.00 17.77 ? 172 PRO A N 1 ATOM 1193 C CA . PRO A 1 155 A 29.319 -15.734 22.279 1.00 19.65 ? 172 PRO A CA 1 ATOM 1194 C C . PRO A 1 155 A 30.232 -14.796 23.063 1.00 21.07 ? 172 PRO A C 1 ATOM 1195 O O . PRO A 1 155 A 29.848 -14.273 24.108 1.00 21.79 ? 172 PRO A O 1 ATOM 1196 C CB . PRO A 1 155 A 29.583 -17.201 22.621 1.00 20.21 ? 172 PRO A CB 1 ATOM 1197 C CG . PRO A 1 155 A 29.289 -17.913 21.325 1.00 21.18 ? 172 PRO A CG 1 ATOM 1198 C CD . PRO A 1 155 A 29.951 -17.005 20.320 1.00 19.19 ? 172 PRO A CD 1 ATOM 1199 N N . GLU A 1 156 ? 31.443 -14.587 22.550 1.00 21.31 ? 173 GLU A N 1 ATOM 1200 C CA . GLU A 1 156 ? 32.409 -13.724 23.214 1.00 22.70 ? 173 GLU A CA 1 ATOM 1201 C C . GLU A 1 156 ? 32.061 -12.246 23.108 1.00 23.44 ? 173 GLU A C 1 ATOM 1202 O O . GLU A 1 156 ? 32.577 -11.429 23.866 1.00 24.71 ? 173 GLU A O 1 ATOM 1203 C CB . GLU A 1 156 ? 33.815 -13.951 22.645 1.00 23.14 ? 173 GLU A CB 1 ATOM 1204 C CG . GLU A 1 156 ? 33.967 -13.677 21.147 1.00 22.91 ? 173 GLU A CG 1 ATOM 1205 C CD . GLU A 1 156 ? 33.789 -14.924 20.292 1.00 23.24 ? 173 GLU A CD 1 ATOM 1206 O OE1 . GLU A 1 156 ? 32.711 -15.552 20.363 1.00 24.56 ? 173 GLU A OE1 1 ATOM 1207 O OE2 . GLU A 1 156 ? 34.728 -15.275 19.544 1.00 17.99 ? 173 GLU A OE2 1 ATOM 1208 N N . LEU A 1 157 ? 31.182 -11.900 22.174 1.00 24.19 ? 174 LEU A N 1 ATOM 1209 C CA . LEU A 1 157 ? 30.809 -10.505 21.982 1.00 24.23 ? 174 LEU A CA 1 ATOM 1210 C C . LEU A 1 157 ? 29.889 -9.963 23.070 1.00 24.25 ? 174 LEU A C 1 ATOM 1211 O O . LEU A 1 157 ? 28.689 -10.215 23.071 1.00 24.94 ? 174 LEU A O 1 ATOM 1212 C CB . LEU A 1 157 ? 30.159 -10.315 20.607 1.00 24.05 ? 174 LEU A CB 1 ATOM 1213 C CG . LEU A 1 157 ? 29.805 -8.869 20.236 1.00 24.88 ? 174 LEU A CG 1 ATOM 1214 C CD1 . LEU A 1 157 ? 31.038 -7.982 20.339 1.00 24.02 ? 174 LEU A CD1 1 ATOM 1215 C CD2 . LEU A 1 157 ? 29.241 -8.829 18.831 1.00 24.63 ? 174 LEU A CD2 1 ATOM 1216 N N . LEU A 1 158 ? 30.463 -9.210 23.999 1.00 25.65 ? 175 LEU A N 1 ATOM 1217 C CA . LEU A 1 158 ? 29.686 -8.624 25.081 1.00 26.83 ? 175 LEU A CA 1 ATOM 1218 C C . LEU A 1 158 ? 28.999 -7.358 24.585 1.00 28.00 ? 175 LEU A C 1 ATOM 1219 O O . LEU A 1 158 ? 29.559 -6.602 23.784 1.00 26.77 ? 175 LEU A O 1 ATOM 1220 C CB . LEU A 1 158 ? 30.600 -8.296 26.257 1.00 27.83 ? 175 LEU A CB 1 ATOM 1221 C CG . LEU A 1 158 ? 31.372 -9.501 26.799 1.00 29.74 ? 175 LEU A CG 1 ATOM 1222 C CD1 . LEU A 1 158 ? 32.413 -9.037 27.800 1.00 31.32 ? 175 LEU A CD1 1 ATOM 1223 C CD2 . LEU A 1 158 ? 30.402 -10.484 27.437 1.00 31.06 ? 175 LEU A CD2 1 ATOM 1224 N N . ALA A 1 159 ? 27.784 -7.130 25.070 1.00 28.98 ? 176 ALA A N 1 ATOM 1225 C CA . ALA A 1 159 ? 27.009 -5.963 24.670 1.00 29.80 ? 176 ALA A CA 1 ATOM 1226 C C . ALA A 1 159 ? 27.675 -4.643 25.046 1.00 29.72 ? 176 ALA A C 1 ATOM 1227 O O . ALA A 1 159 ? 27.375 -3.606 24.455 1.00 31.23 ? 176 ALA A O 1 ATOM 1228 C CB . ALA A 1 159 ? 25.610 -6.037 25.279 1.00 30.98 ? 176 ALA A CB 1 ATOM 1229 N N . GLU A 1 160 ? 28.577 -4.675 26.021 1.00 29.75 ? 177 GLU A N 1 ATOM 1230 C CA . GLU A 1 160 ? 29.259 -3.456 26.450 1.00 30.55 ? 177 GLU A CA 1 ATOM 1231 C C . GLU A 1 160 ? 30.322 -2.967 25.475 1.00 29.14 ? 177 GLU A C 1 ATOM 1232 O O . GLU A 1 160 ? 30.689 -1.789 25.497 1.00 29.75 ? 177 GLU A O 1 ATOM 1233 C CB . GLU A 1 160 ? 29.897 -3.637 27.832 1.00 33.44 ? 177 GLU A CB 1 ATOM 1234 C CG . GLU A 1 160 ? 30.104 -5.077 28.260 1.00 40.18 ? 177 GLU A CG 1 ATOM 1235 C CD . GLU A 1 160 ? 28.793 -5.767 28.574 1.00 42.82 ? 177 GLU A CD 1 ATOM 1236 O OE1 . GLU A 1 160 ? 28.038 -5.246 29.425 1.00 46.11 ? 177 GLU A OE1 1 ATOM 1237 O OE2 . GLU A 1 160 ? 28.515 -6.825 27.972 1.00 46.96 ? 177 GLU A OE2 1 ATOM 1238 N N . TYR A 1 161 ? 30.833 -3.857 24.630 1.00 25.10 ? 178 TYR A N 1 ATOM 1239 C CA . TYR A 1 161 ? 31.843 -3.436 23.670 1.00 22.27 ? 178 TYR A CA 1 ATOM 1240 C C . TYR A 1 161 ? 31.147 -2.539 22.654 1.00 20.94 ? 178 TYR A C 1 ATOM 1241 O O . TYR A 1 161 ? 30.050 -2.849 22.190 1.00 21.83 ? 178 TYR A O 1 ATOM 1242 C CB . TYR A 1 161 ? 32.469 -4.642 22.967 1.00 20.85 ? 178 TYR A CB 1 ATOM 1243 C CG . TYR A 1 161 ? 33.142 -5.625 23.900 1.00 20.98 ? 178 TYR A CG 1 ATOM 1244 C CD1 . TYR A 1 161 ? 33.827 -5.188 25.035 1.00 19.82 ? 178 TYR A CD1 1 ATOM 1245 C CD2 . TYR A 1 161 ? 33.121 -6.994 23.632 1.00 20.57 ? 178 TYR A CD2 1 ATOM 1246 C CE1 . TYR A 1 161 ? 34.472 -6.087 25.882 1.00 19.47 ? 178 TYR A CE1 1 ATOM 1247 C CE2 . TYR A 1 161 ? 33.767 -7.906 24.472 1.00 20.65 ? 178 TYR A CE2 1 ATOM 1248 C CZ . TYR A 1 161 ? 34.441 -7.446 25.593 1.00 20.81 ? 178 TYR A CZ 1 ATOM 1249 O OH . TYR A 1 161 ? 35.094 -8.343 26.414 1.00 20.50 ? 178 TYR A OH 1 ATOM 1250 N N . ARG A 1 162 ? 31.770 -1.416 22.324 1.00 17.25 ? 179 ARG A N 1 ATOM 1251 C CA . ARG A 1 162 ? 31.175 -0.495 21.369 1.00 16.70 ? 179 ARG A CA 1 ATOM 1252 C C . ARG A 1 162 ? 31.632 -0.895 19.976 1.00 15.55 ? 179 ARG A C 1 ATOM 1253 O O . ARG A 1 162 ? 32.657 -0.437 19.481 1.00 14.48 ? 179 ARG A O 1 ATOM 1254 C CB . ARG A 1 162 ? 31.582 0.938 21.725 1.00 16.65 ? 179 ARG A CB 1 ATOM 1255 C CG . ARG A 1 162 ? 31.014 1.369 23.073 1.00 16.63 ? 179 ARG A CG 1 ATOM 1256 C CD . ARG A 1 162 ? 31.634 2.652 23.599 1.00 18.84 ? 179 ARG A CD 1 ATOM 1257 N NE . ARG A 1 162 ? 31.101 2.984 24.917 1.00 17.56 ? 179 ARG A NE 1 ATOM 1258 C CZ . ARG A 1 162 ? 29.874 3.446 25.128 1.00 18.95 ? 179 ARG A CZ 1 ATOM 1259 N NH1 . ARG A 1 162 ? 29.055 3.638 24.106 1.00 17.71 ? 179 ARG A NH1 1 ATOM 1260 N NH2 . ARG A 1 162 ? 29.458 3.699 26.361 1.00 16.77 ? 179 ARG A NH2 1 ATOM 1261 N N . THR A 1 163 ? 30.846 -1.757 19.344 1.00 14.88 ? 180 THR A N 1 ATOM 1262 C CA . THR A 1 163 ? 31.193 -2.274 18.030 1.00 14.37 ? 180 THR A CA 1 ATOM 1263 C C . THR A 1 163 ? 30.086 -2.168 16.983 1.00 14.22 ? 180 THR A C 1 ATOM 1264 O O . THR A 1 163 ? 28.925 -1.876 17.296 1.00 11.49 ? 180 THR A O 1 ATOM 1265 C CB . THR A 1 163 ? 31.588 -3.752 18.150 1.00 15.23 ? 180 THR A CB 1 ATOM 1266 O OG1 . THR A 1 163 ? 30.463 -4.503 18.628 1.00 15.67 ? 180 THR A OG1 1 ATOM 1267 C CG2 . THR A 1 163 ? 32.732 -3.920 19.137 1.00 12.70 ? 180 THR A CG2 1 ATOM 1268 N N . LEU A 1 164 ? 30.468 -2.415 15.733 1.00 13.52 ? 181 LEU A N 1 ATOM 1269 C CA . LEU A 1 164 ? 29.537 -2.394 14.611 1.00 12.39 ? 181 LEU A CA 1 ATOM 1270 C C . LEU A 1 164 ? 29.580 -3.775 13.966 1.00 12.41 ? 181 LEU A C 1 ATOM 1271 O O . LEU A 1 164 ? 30.583 -4.485 14.062 1.00 9.53 ? 181 LEU A O 1 ATOM 1272 C CB . LEU A 1 164 ? 29.931 -1.321 13.593 1.00 12.20 ? 181 LEU A CB 1 ATOM 1273 C CG . LEU A 1 164 ? 29.889 0.132 14.090 1.00 12.95 ? 181 LEU A CG 1 ATOM 1274 C CD1 . LEU A 1 164 ? 30.306 1.062 12.963 1.00 15.55 ? 181 LEU A CD1 1 ATOM 1275 C CD2 . LEU A 1 164 ? 28.490 0.480 14.581 1.00 13.35 ? 181 LEU A CD2 1 ATOM 1276 N N . CYS A 1 165 ? 28.484 -4.147 13.314 1.00 11.34 ? 182 CYS A N 1 ATOM 1277 C CA . CYS A 1 165 ? 28.364 -5.447 12.669 1.00 12.39 ? 182 CYS A CA 1 ATOM 1278 C C . CYS A 1 165 ? 28.186 -5.211 11.173 1.00 12.75 ? 182 CYS A C 1 ATOM 1279 O O . CYS A 1 165 ? 27.223 -4.564 10.764 1.00 12.18 ? 182 CYS A O 1 ATOM 1280 C CB . CYS A 1 165 ? 27.143 -6.165 13.240 1.00 11.44 ? 182 CYS A CB 1 ATOM 1281 S SG . CYS A 1 165 ? 26.966 -7.907 12.763 1.00 14.52 ? 182 CYS A SG 1 ATOM 1282 N N . ALA A 1 166 ? 29.109 -5.729 10.363 1.00 11.82 ? 183 ALA A N 1 ATOM 1283 C CA . ALA A 1 166 ? 29.030 -5.534 8.920 1.00 10.93 ? 183 ALA A CA 1 ATOM 1284 C C . ALA A 1 166 ? 29.397 -6.756 8.076 1.00 11.11 ? 183 ALA A C 1 ATOM 1285 O O . ALA A 1 166 ? 30.350 -7.479 8.373 1.00 9.79 ? 183 ALA A O 1 ATOM 1286 C CB . ALA A 1 166 ? 29.892 -4.346 8.516 1.00 7.83 ? 183 ALA A CB 1 ATOM 1287 N N . GLY A 1 167 ? 28.616 -6.958 7.016 1.00 12.42 ? 184 GLY A N 1 ATOM 1288 C CA . GLY A 1 167 ? 28.813 -8.060 6.083 1.00 13.38 ? 184 GLY A CA 1 ATOM 1289 C C . GLY A 1 167 ? 27.592 -8.164 5.177 1.00 14.01 ? 184 GLY A C 1 ATOM 1290 O O . GLY A 1 167 ? 26.887 -7.171 4.972 1.00 13.36 ? 184 GLY A O 1 ATOM 1291 N N . ILE A 1 168 ? 27.351 -9.351 4.621 1.00 15.35 ? 185 ILE A N 1 ATOM 1292 C CA . ILE A 1 168 ? 26.183 -9.599 3.769 1.00 16.90 ? 185 ILE A CA 1 ATOM 1293 C C . ILE A 1 168 ? 25.585 -10.948 4.173 1.00 16.18 ? 185 ILE A C 1 ATOM 1294 O O . ILE A 1 168 ? 26.314 -11.916 4.382 1.00 15.67 ? 185 ILE A O 1 ATOM 1295 C CB . ILE A 1 168 ? 26.539 -9.618 2.256 1.00 17.29 ? 185 ILE A CB 1 ATOM 1296 C CG1 . ILE A 1 168 ? 27.754 -10.505 2.005 1.00 18.50 ? 185 ILE A CG1 1 ATOM 1297 C CG2 . ILE A 1 168 ? 26.780 -8.198 1.757 1.00 17.29 ? 185 ILE A CG2 1 ATOM 1298 C CD1 . ILE A 1 168 ? 28.116 -10.614 0.537 1.00 18.67 ? 185 ILE A CD1 1 ATOM 1299 N N . VAL A 1 169 ? 24.260 -11.008 4.279 1.00 15.87 ? 186 VAL A N 1 ATOM 1300 C CA . VAL A 1 169 ? 23.582 -12.231 4.709 1.00 16.72 ? 186 VAL A CA 1 ATOM 1301 C C . VAL A 1 169 ? 23.896 -13.513 3.944 1.00 16.26 ? 186 VAL A C 1 ATOM 1302 O O . VAL A 1 169 ? 23.937 -14.589 4.538 1.00 16.95 ? 186 VAL A O 1 ATOM 1303 C CB . VAL A 1 169 ? 22.042 -12.038 4.744 1.00 16.26 ? 186 VAL A CB 1 ATOM 1304 C CG1 . VAL A 1 169 ? 21.675 -11.083 5.854 1.00 17.60 ? 186 VAL A CG1 1 ATOM 1305 C CG2 . VAL A 1 169 ? 21.539 -11.501 3.415 1.00 15.21 ? 186 VAL A CG2 1 ATOM 1306 N N . GLN A 1 170 A 24.114 -13.420 2.638 1.00 16.41 ? 186 GLN A N 1 ATOM 1307 C CA . GLN A 1 170 A 24.413 -14.621 1.866 1.00 16.58 ? 186 GLN A CA 1 ATOM 1308 C C . GLN A 1 170 A 25.885 -15.007 1.995 1.00 17.12 ? 186 GLN A C 1 ATOM 1309 O O . GLN A 1 170 A 26.282 -16.083 1.564 1.00 17.95 ? 186 GLN A O 1 ATOM 1310 C CB . GLN A 1 170 A 24.065 -14.423 0.386 1.00 16.42 ? 186 GLN A CB 1 ATOM 1311 C CG . GLN A 1 170 A 24.917 -13.390 -0.331 1.00 16.97 ? 186 GLN A CG 1 ATOM 1312 C CD . GLN A 1 170 A 24.291 -12.009 -0.332 1.00 15.64 ? 186 GLN A CD 1 ATOM 1313 O OE1 . GLN A 1 170 A 23.626 -11.616 0.621 1.00 17.96 ? 186 GLN A OE1 1 ATOM 1314 N NE2 . GLN A 1 170 A 24.512 -11.263 -1.403 1.00 15.71 ? 186 GLN A NE2 1 ATOM 1315 N N . GLY A 1 171 B 26.686 -14.125 2.592 1.00 16.83 ? 186 GLY A N 1 ATOM 1316 C CA . GLY A 1 171 B 28.107 -14.393 2.764 1.00 15.66 ? 186 GLY A CA 1 ATOM 1317 C C . GLY A 1 171 B 28.926 -14.128 1.509 1.00 14.68 ? 186 GLY A C 1 ATOM 1318 O O . GLY A 1 171 B 28.394 -13.643 0.513 1.00 15.20 ? 186 GLY A O 1 ATOM 1319 N N . GLY A 1 172 ? 30.224 -14.417 1.555 1.00 13.14 ? 187 GLY A N 1 ATOM 1320 C CA . GLY A 1 172 ? 31.053 -14.220 0.377 1.00 13.75 ? 187 GLY A CA 1 ATOM 1321 C C . GLY A 1 172 ? 31.951 -12.998 0.304 1.00 12.62 ? 187 GLY A C 1 ATOM 1322 O O . GLY A 1 172 ? 32.892 -12.987 -0.486 1.00 12.29 ? 187 GLY A O 1 ATOM 1323 N N . LYS A 1 173 ? 31.660 -11.970 1.097 1.00 12.60 ? 188 LYS A N 1 ATOM 1324 C CA . LYS A 1 173 ? 32.472 -10.750 1.129 1.00 13.25 ? 188 LYS A CA 1 ATOM 1325 C C . LYS A 1 173 ? 32.750 -10.449 2.593 1.00 13.47 ? 188 LYS A C 1 ATOM 1326 O O . LYS A 1 173 ? 31.820 -10.370 3.396 1.00 16.05 ? 188 LYS A O 1 ATOM 1327 C CB . LYS A 1 173 ? 31.725 -9.576 0.503 1.00 13.20 ? 188 LYS A CB 1 ATOM 1328 C CG . LYS A 1 173 ? 31.372 -9.758 -0.955 1.00 16.37 ? 188 LYS A CG 1 ATOM 1329 C CD . LYS A 1 173 ? 30.582 -8.559 -1.433 1.00 20.75 ? 188 LYS A CD 1 ATOM 1330 C CE . LYS A 1 173 ? 30.144 -8.704 -2.869 1.00 23.52 ? 188 LYS A CE 1 ATOM 1331 N NZ . LYS A 1 173 ? 29.428 -7.470 -3.295 1.00 28.98 ? 188 LYS A NZ 1 ATOM 1332 N N . ASP A 1 174 ? 34.018 -10.261 2.945 1.00 13.28 ? 189 ASP A N 1 ATOM 1333 C CA . ASP A 1 174 ? 34.370 -10.032 4.345 1.00 12.80 ? 189 ASP A CA 1 ATOM 1334 C C . ASP A 1 174 ? 35.843 -9.638 4.427 1.00 13.81 ? 189 ASP A C 1 ATOM 1335 O O . ASP A 1 174 ? 36.571 -9.733 3.434 1.00 13.06 ? 189 ASP A O 1 ATOM 1336 C CB . ASP A 1 174 ? 34.108 -11.349 5.100 1.00 11.42 ? 189 ASP A CB 1 ATOM 1337 C CG . ASP A 1 174 ? 34.332 -11.256 6.605 1.00 12.51 ? 189 ASP A CG 1 ATOM 1338 O OD1 . ASP A 1 174 ? 34.298 -10.150 7.178 1.00 10.75 ? 189 ASP A OD1 1 ATOM 1339 O OD2 . ASP A 1 174 ? 34.517 -12.327 7.227 1.00 13.82 ? 189 ASP A OD2 1 ATOM 1340 N N . THR A 1 175 ? 36.271 -9.158 5.589 1.00 11.74 ? 190 THR A N 1 ATOM 1341 C CA . THR A 1 175 ? 37.674 -8.822 5.774 1.00 12.51 ? 190 THR A CA 1 ATOM 1342 C C . THR A 1 175 ? 38.281 -10.137 6.218 1.00 12.89 ? 190 THR A C 1 ATOM 1343 O O . THR A 1 175 ? 37.558 -11.042 6.634 1.00 12.32 ? 190 THR A O 1 ATOM 1344 C CB . THR A 1 175 ? 37.893 -7.770 6.875 1.00 12.26 ? 190 THR A CB 1 ATOM 1345 O OG1 . THR A 1 175 ? 37.095 -8.099 8.018 1.00 11.45 ? 190 THR A OG1 1 ATOM 1346 C CG2 . THR A 1 175 ? 37.528 -6.377 6.366 1.00 13.37 ? 190 THR A CG2 1 ATOM 1347 N N . CYS A 1 176 ? 39.596 -10.260 6.131 1.00 11.44 ? 191 CYS A N 1 ATOM 1348 C CA . CYS A 1 176 ? 40.229 -11.509 6.515 1.00 13.36 ? 191 CYS A CA 1 ATOM 1349 C C . CYS A 1 176 ? 41.586 -11.214 7.154 1.00 14.74 ? 191 CYS A C 1 ATOM 1350 O O . CYS A 1 176 ? 41.917 -10.051 7.426 1.00 12.54 ? 191 CYS A O 1 ATOM 1351 C CB . CYS A 1 176 ? 40.366 -12.394 5.265 1.00 13.05 ? 191 CYS A CB 1 ATOM 1352 S SG . CYS A 1 176 ? 40.401 -14.208 5.507 1.00 17.21 ? 191 CYS A SG 1 ATOM 1353 N N . GLY A 1 177 ? 42.364 -12.263 7.396 1.00 15.35 ? 192 GLY A N 1 ATOM 1354 C CA . GLY A 1 177 ? 43.667 -12.098 8.019 1.00 13.28 ? 192 GLY A CA 1 ATOM 1355 C C . GLY A 1 177 ? 44.519 -11.008 7.400 1.00 13.99 ? 192 GLY A C 1 ATOM 1356 O O . GLY A 1 177 ? 44.802 -11.031 6.206 1.00 14.03 ? 192 GLY A O 1 ATOM 1357 N N . GLY A 1 178 ? 44.935 -10.043 8.214 1.00 14.17 ? 193 GLY A N 1 ATOM 1358 C CA . GLY A 1 178 ? 45.765 -8.965 7.706 1.00 14.60 ? 193 GLY A CA 1 ATOM 1359 C C . GLY A 1 178 ? 45.056 -7.651 7.416 1.00 14.17 ? 193 GLY A C 1 ATOM 1360 O O . GLY A 1 178 ? 45.711 -6.661 7.111 1.00 15.78 ? 193 GLY A O 1 ATOM 1361 N N . ASP A 1 179 ? 43.731 -7.623 7.501 1.00 13.67 ? 194 ASP A N 1 ATOM 1362 C CA . ASP A 1 179 ? 42.996 -6.387 7.238 1.00 12.96 ? 194 ASP A CA 1 ATOM 1363 C C . ASP A 1 179 ? 42.765 -5.572 8.509 1.00 12.76 ? 194 ASP A C 1 ATOM 1364 O O . ASP A 1 179 ? 42.337 -4.420 8.446 1.00 12.72 ? 194 ASP A O 1 ATOM 1365 C CB . ASP A 1 179 ? 41.637 -6.680 6.589 1.00 12.28 ? 194 ASP A CB 1 ATOM 1366 C CG . ASP A 1 179 ? 41.758 -7.256 5.189 1.00 12.56 ? 194 ASP A CG 1 ATOM 1367 O OD1 . ASP A 1 179 ? 42.555 -6.725 4.385 1.00 13.35 ? 194 ASP A OD1 1 ATOM 1368 O OD2 . ASP A 1 179 ? 41.041 -8.232 4.888 1.00 12.00 ? 194 ASP A OD2 1 ATOM 1369 N N . SER A 1 180 ? 43.051 -6.170 9.660 1.00 13.18 ? 195 SER A N 1 ATOM 1370 C CA . SER A 1 180 ? 42.856 -5.505 10.943 1.00 13.62 ? 195 SER A CA 1 ATOM 1371 C C . SER A 1 180 ? 43.431 -4.096 10.977 1.00 12.49 ? 195 SER A C 1 ATOM 1372 O O . SER A 1 180 ? 44.486 -3.831 10.405 1.00 13.97 ? 195 SER A O 1 ATOM 1373 C CB . SER A 1 180 ? 43.475 -6.341 12.068 1.00 16.94 ? 195 SER A CB 1 ATOM 1374 O OG . SER A 1 180 ? 42.806 -7.588 12.203 1.00 18.06 ? 195 SER A OG 1 ATOM 1375 N N . GLY A 1 181 ? 42.723 -3.194 11.648 1.00 10.33 ? 196 GLY A N 1 ATOM 1376 C CA . GLY A 1 181 ? 43.184 -1.822 11.763 1.00 9.47 ? 196 GLY A CA 1 ATOM 1377 C C . GLY A 1 181 ? 42.705 -0.910 10.647 1.00 9.82 ? 196 GLY A C 1 ATOM 1378 O O . GLY A 1 181 ? 42.710 0.309 10.798 1.00 11.27 ? 196 GLY A O 1 ATOM 1379 N N . GLY A 1 182 ? 42.290 -1.502 9.531 1.00 8.85 ? 197 GLY A N 1 ATOM 1380 C CA . GLY A 1 182 ? 41.824 -0.731 8.391 1.00 9.25 ? 197 GLY A CA 1 ATOM 1381 C C . GLY A 1 182 ? 40.468 -0.080 8.591 1.00 9.80 ? 197 GLY A C 1 ATOM 1382 O O . GLY A 1 182 ? 39.756 -0.410 9.531 1.00 9.03 ? 197 GLY A O 1 ATOM 1383 N N . PRO A 1 183 ? 40.076 0.852 7.709 1.00 9.07 ? 198 PRO A N 1 ATOM 1384 C CA . PRO A 1 183 ? 38.786 1.528 7.839 1.00 9.12 ? 198 PRO A CA 1 ATOM 1385 C C . PRO A 1 183 ? 37.573 0.846 7.240 1.00 10.47 ? 198 PRO A C 1 ATOM 1386 O O . PRO A 1 183 ? 37.672 0.046 6.310 1.00 7.42 ? 198 PRO A O 1 ATOM 1387 C CB . PRO A 1 183 ? 39.035 2.865 7.159 1.00 7.83 ? 198 PRO A CB 1 ATOM 1388 C CG . PRO A 1 183 ? 39.918 2.481 6.026 1.00 8.65 ? 198 PRO A CG 1 ATOM 1389 C CD . PRO A 1 183 ? 40.901 1.511 6.679 1.00 9.46 ? 198 PRO A CD 1 ATOM 1390 N N . LEU A 1 184 ? 36.428 1.187 7.817 1.00 10.74 ? 199 LEU A N 1 ATOM 1391 C CA . LEU A 1 184 ? 35.129 0.740 7.366 1.00 10.20 ? 199 LEU A CA 1 ATOM 1392 C C . LEU A 1 184 ? 34.505 2.073 6.963 1.00 11.74 ? 199 LEU A C 1 ATOM 1393 O O . LEU A 1 184 ? 34.288 2.949 7.808 1.00 13.84 ? 199 LEU A O 1 ATOM 1394 C CB . LEU A 1 184 ? 34.322 0.110 8.505 1.00 8.89 ? 199 LEU A CB 1 ATOM 1395 C CG . LEU A 1 184 ? 32.830 -0.070 8.185 1.00 10.94 ? 199 LEU A CG 1 ATOM 1396 C CD1 . LEU A 1 184 ? 32.674 -0.922 6.940 1.00 14.15 ? 199 LEU A CD1 1 ATOM 1397 C CD2 . LEU A 1 184 ? 32.116 -0.720 9.354 1.00 10.53 ? 199 LEU A CD2 1 ATOM 1398 N N . ILE A 1 185 ? 34.222 2.233 5.678 1.00 11.86 ? 200 ILE A N 1 ATOM 1399 C CA . ILE A 1 185 ? 33.657 3.483 5.194 1.00 10.97 ? 200 ILE A CA 1 ATOM 1400 C C . ILE A 1 185 ? 32.197 3.314 4.779 1.00 10.20 ? 200 ILE A C 1 ATOM 1401 O O . ILE A 1 185 ? 31.888 2.575 3.849 1.00 8.61 ? 200 ILE A O 1 ATOM 1402 C CB . ILE A 1 185 ? 34.479 4.007 4.005 1.00 12.04 ? 200 ILE A CB 1 ATOM 1403 C CG1 . ILE A 1 185 ? 35.931 4.176 4.436 1.00 14.10 ? 200 ILE A CG1 1 ATOM 1404 C CG2 . ILE A 1 185 ? 33.913 5.338 3.513 1.00 15.34 ? 200 ILE A CG2 1 ATOM 1405 C CD1 . ILE A 1 185 ? 36.853 4.524 3.308 1.00 20.61 ? 200 ILE A CD1 1 ATOM 1406 N N . CYS A 1 186 ? 31.303 3.999 5.486 1.00 9.06 ? 201 CYS A N 1 ATOM 1407 C CA . CYS A 1 186 ? 29.877 3.926 5.194 1.00 11.64 ? 201 CYS A CA 1 ATOM 1408 C C . CYS A 1 186 ? 29.388 5.326 4.859 1.00 12.95 ? 201 CYS A C 1 ATOM 1409 O O . CYS A 1 186 ? 29.738 6.288 5.538 1.00 13.21 ? 201 CYS A O 1 ATOM 1410 C CB . CYS A 1 186 ? 29.107 3.406 6.405 1.00 10.43 ? 201 CYS A CB 1 ATOM 1411 S SG . CYS A 1 186 ? 29.726 1.873 7.183 1.00 12.25 ? 201 CYS A SG 1 ATOM 1412 N N . ASN A 1 187 ? 28.568 5.436 3.821 1.00 15.65 ? 202 ASN A N 1 ATOM 1413 C CA . ASN A 1 187 ? 28.061 6.734 3.392 1.00 18.66 ? 202 ASN A CA 1 ATOM 1414 C C . ASN A 1 187 ? 29.219 7.723 3.244 1.00 17.54 ? 202 ASN A C 1 ATOM 1415 O O . ASN A 1 187 ? 29.088 8.904 3.544 1.00 17.44 ? 202 ASN A O 1 ATOM 1416 C CB . ASN A 1 187 ? 27.029 7.273 4.391 1.00 22.07 ? 202 ASN A CB 1 ATOM 1417 C CG . ASN A 1 187 ? 25.826 6.353 4.546 1.00 27.14 ? 202 ASN A CG 1 ATOM 1418 O OD1 . ASN A 1 187 ? 25.239 5.896 3.559 1.00 29.61 ? 202 ASN A OD1 1 ATOM 1419 N ND2 . ASN A 1 187 ? 25.451 6.080 5.789 1.00 30.40 ? 202 ASN A ND2 1 ATOM 1420 N N . GLY A 1 188 ? 30.363 7.221 2.792 1.00 18.38 ? 207 GLY A N 1 ATOM 1421 C CA . GLY A 1 188 ? 31.524 8.074 2.593 1.00 17.14 ? 207 GLY A CA 1 ATOM 1422 C C . GLY A 1 188 ? 32.236 8.514 3.859 1.00 17.20 ? 207 GLY A C 1 ATOM 1423 O O . GLY A 1 188 ? 33.174 9.310 3.796 1.00 16.50 ? 207 GLY A O 1 ATOM 1424 N N . GLN A 1 189 ? 31.806 7.996 5.007 1.00 16.55 ? 208 GLN A N 1 ATOM 1425 C CA . GLN A 1 189 ? 32.419 8.362 6.282 1.00 17.81 ? 208 GLN A CA 1 ATOM 1426 C C . GLN A 1 189 ? 33.204 7.241 6.942 1.00 17.03 ? 208 GLN A C 1 ATOM 1427 O O . GLN A 1 189 ? 32.858 6.064 6.816 1.00 15.09 ? 208 GLN A O 1 ATOM 1428 C CB . GLN A 1 189 ? 31.360 8.819 7.283 1.00 21.05 ? 208 GLN A CB 1 ATOM 1429 C CG . GLN A 1 189 ? 30.637 10.090 6.934 1.00 27.49 ? 208 GLN A CG 1 ATOM 1430 C CD . GLN A 1 189 ? 29.903 10.638 8.132 1.00 31.36 ? 208 GLN A CD 1 ATOM 1431 O OE1 . GLN A 1 189 ? 29.096 9.944 8.747 1.00 35.38 ? 208 GLN A OE1 1 ATOM 1432 N NE2 . GLN A 1 189 ? 30.188 11.884 8.480 1.00 34.82 ? 208 GLN A NE2 1 ATOM 1433 N N . PHE A 1 190 ? 34.245 7.633 7.671 1.00 15.71 ? 209 PHE A N 1 ATOM 1434 C CA . PHE A 1 190 ? 35.099 6.704 8.416 1.00 15.65 ? 209 PHE A CA 1 ATOM 1435 C C . PHE A 1 190 ? 34.290 6.300 9.654 1.00 15.46 ? 209 PHE A C 1 ATOM 1436 O O . PHE A 1 190 ? 34.324 6.988 10.673 1.00 16.64 ? 209 PHE A O 1 ATOM 1437 C CB . PHE A 1 190 ? 36.395 7.442 8.796 1.00 13.79 ? 209 PHE A CB 1 ATOM 1438 C CG . PHE A 1 190 ? 37.295 6.695 9.744 1.00 12.75 ? 209 PHE A CG 1 ATOM 1439 C CD1 . PHE A 1 190 ? 37.428 5.308 9.678 1.00 9.46 ? 209 PHE A CD1 1 ATOM 1440 C CD2 . PHE A 1 190 ? 38.065 7.398 10.670 1.00 11.40 ? 209 PHE A CD2 1 ATOM 1441 C CE1 . PHE A 1 190 ? 38.319 4.636 10.520 1.00 9.03 ? 209 PHE A CE1 1 ATOM 1442 C CE2 . PHE A 1 190 ? 38.955 6.739 11.510 1.00 9.24 ? 209 PHE A CE2 1 ATOM 1443 C CZ . PHE A 1 190 ? 39.084 5.353 11.436 1.00 9.42 ? 209 PHE A CZ 1 ATOM 1444 N N . GLN A 1 191 ? 33.558 5.191 9.556 1.00 15.12 ? 210 GLN A N 1 ATOM 1445 C CA . GLN A 1 191 ? 32.702 4.730 10.655 1.00 14.72 ? 210 GLN A CA 1 ATOM 1446 C C . GLN A 1 191 ? 33.250 3.600 11.532 1.00 13.74 ? 210 GLN A C 1 ATOM 1447 O O . GLN A 1 191 ? 32.797 3.431 12.663 1.00 12.86 ? 210 GLN A O 1 ATOM 1448 C CB . GLN A 1 191 ? 31.329 4.274 10.119 1.00 16.46 ? 210 GLN A CB 1 ATOM 1449 C CG . GLN A 1 191 ? 30.496 5.324 9.399 1.00 21.56 ? 210 GLN A CG 1 ATOM 1450 C CD . GLN A 1 191 ? 29.889 6.362 10.325 1.00 25.70 ? 210 GLN A CD 1 ATOM 1451 O OE1 . GLN A 1 191 ? 29.204 7.284 9.875 1.00 29.66 ? 210 GLN A OE1 1 ATOM 1452 N NE2 . GLN A 1 191 ? 30.134 6.221 11.621 1.00 25.27 ? 210 GLN A NE2 1 ATOM 1453 N N . GLY A 1 192 ? 34.200 2.821 11.026 1.00 13.42 ? 211 GLY A N 1 ATOM 1454 C CA . GLY A 1 192 ? 34.718 1.722 11.825 1.00 10.89 ? 211 GLY A CA 1 ATOM 1455 C C . GLY A 1 192 ? 36.158 1.304 11.602 1.00 11.74 ? 211 GLY A C 1 ATOM 1456 O O . GLY A 1 192 ? 36.819 1.737 10.656 1.00 11.46 ? 211 GLY A O 1 ATOM 1457 N N . ILE A 1 193 ? 36.639 0.441 12.492 1.00 11.66 ? 212 ILE A N 1 ATOM 1458 C CA . ILE A 1 193 ? 38.000 -0.074 12.434 1.00 11.11 ? 212 ILE A CA 1 ATOM 1459 C C . ILE A 1 193 ? 37.931 -1.603 12.400 1.00 10.21 ? 212 ILE A C 1 ATOM 1460 O O . ILE A 1 193 ? 37.287 -2.206 13.252 1.00 9.65 ? 212 ILE A O 1 ATOM 1461 C CB . ILE A 1 193 ? 38.795 0.355 13.689 1.00 11.03 ? 212 ILE A CB 1 ATOM 1462 C CG1 . ILE A 1 193 ? 38.780 1.882 13.817 1.00 11.25 ? 212 ILE A CG1 1 ATOM 1463 C CG2 . ILE A 1 193 ? 40.209 -0.193 13.620 1.00 11.59 ? 212 ILE A CG2 1 ATOM 1464 C CD1 . ILE A 1 193 ? 39.545 2.408 15.019 1.00 13.48 ? 212 ILE A CD1 1 ATOM 1465 N N . VAL A 1 194 ? 38.585 -2.227 11.423 1.00 9.31 ? 213 VAL A N 1 ATOM 1466 C CA . VAL A 1 194 ? 38.562 -3.688 11.328 1.00 10.39 ? 213 VAL A CA 1 ATOM 1467 C C . VAL A 1 194 ? 39.110 -4.240 12.634 1.00 11.65 ? 213 VAL A C 1 ATOM 1468 O O . VAL A 1 194 ? 40.269 -4.011 12.981 1.00 12.58 ? 213 VAL A O 1 ATOM 1469 C CB . VAL A 1 194 ? 39.425 -4.191 10.157 1.00 8.70 ? 213 VAL A CB 1 ATOM 1470 C CG1 . VAL A 1 194 ? 39.260 -5.698 9.998 1.00 7.13 ? 213 VAL A CG1 1 ATOM 1471 C CG2 . VAL A 1 194 ? 39.025 -3.463 8.879 1.00 9.53 ? 213 VAL A CG2 1 ATOM 1472 N N . SER A 1 195 ? 38.280 -4.974 13.360 1.00 12.09 ? 214 SER A N 1 ATOM 1473 C CA . SER A 1 195 ? 38.705 -5.491 14.646 1.00 12.53 ? 214 SER A CA 1 ATOM 1474 C C . SER A 1 195 ? 38.678 -6.993 14.856 1.00 13.75 ? 214 SER A C 1 ATOM 1475 O O . SER A 1 195 ? 39.648 -7.571 15.347 1.00 12.89 ? 214 SER A O 1 ATOM 1476 C CB . SER A 1 195 ? 37.865 -4.847 15.752 1.00 11.48 ? 214 SER A CB 1 ATOM 1477 O OG . SER A 1 195 ? 38.093 -5.480 17.004 1.00 12.62 ? 214 SER A OG 1 ATOM 1478 N N . TYR A 1 196 ? 37.574 -7.627 14.485 1.00 14.13 ? 215 TYR A N 1 ATOM 1479 C CA . TYR A 1 196 ? 37.421 -9.051 14.748 1.00 15.85 ? 215 TYR A CA 1 ATOM 1480 C C . TYR A 1 196 ? 36.539 -9.756 13.715 1.00 16.11 ? 215 TYR A C 1 ATOM 1481 O O . TYR A 1 196 ? 35.678 -9.142 13.083 1.00 14.38 ? 215 TYR A O 1 ATOM 1482 C CB . TYR A 1 196 ? 36.799 -9.190 16.143 1.00 17.19 ? 215 TYR A CB 1 ATOM 1483 C CG . TYR A 1 196 ? 36.910 -10.534 16.820 1.00 21.30 ? 215 TYR A CG 1 ATOM 1484 C CD1 . TYR A 1 196 ? 38.116 -10.963 17.375 1.00 22.40 ? 215 TYR A CD1 1 ATOM 1485 C CD2 . TYR A 1 196 ? 35.782 -11.334 16.998 1.00 22.96 ? 215 TYR A CD2 1 ATOM 1486 C CE1 . TYR A 1 196 ? 38.190 -12.148 18.104 1.00 23.85 ? 215 TYR A CE1 1 ATOM 1487 C CE2 . TYR A 1 196 ? 35.846 -12.522 17.723 1.00 22.53 ? 215 TYR A CE2 1 ATOM 1488 C CZ . TYR A 1 196 ? 37.050 -12.919 18.276 1.00 24.43 ? 215 TYR A CZ 1 ATOM 1489 O OH . TYR A 1 196 ? 37.098 -14.069 19.035 1.00 26.59 ? 215 TYR A OH 1 ATOM 1490 N N . GLY A 1 197 ? 36.759 -11.058 13.569 1.00 15.67 ? 216 GLY A N 1 ATOM 1491 C CA . GLY A 1 197 ? 35.995 -11.853 12.631 1.00 16.71 ? 216 GLY A CA 1 ATOM 1492 C C . GLY A 1 197 ? 36.289 -13.317 12.886 1.00 18.10 ? 216 GLY A C 1 ATOM 1493 O O . GLY A 1 197 ? 37.003 -13.644 13.835 1.00 18.12 ? 216 GLY A O 1 ATOM 1494 N N . ALA A 1 198 ? 35.753 -14.198 12.047 1.00 17.32 ? 217 ALA A N 1 ATOM 1495 C CA . ALA A 1 198 ? 35.974 -15.630 12.209 1.00 18.35 ? 217 ALA A CA 1 ATOM 1496 C C . ALA A 1 198 ? 36.730 -16.244 11.032 1.00 19.16 ? 217 ALA A C 1 ATOM 1497 O O . ALA A 1 198 ? 36.954 -15.591 10.014 1.00 19.51 ? 217 ALA A O 1 ATOM 1498 C CB . ALA A 1 198 ? 34.631 -16.343 12.395 1.00 18.26 ? 217 ALA A CB 1 ATOM 1499 N N . HIS A 1 199 ? 37.120 -17.506 11.192 1.00 21.43 ? 218 HIS A N 1 ATOM 1500 C CA . HIS A 1 199 ? 37.833 -18.259 10.161 1.00 22.93 ? 218 HIS A CA 1 ATOM 1501 C C . HIS A 1 199 ? 37.195 -19.632 9.988 1.00 21.66 ? 218 HIS A C 1 ATOM 1502 O O . HIS A 1 199 ? 36.916 -20.321 10.964 1.00 23.35 ? 218 HIS A O 1 ATOM 1503 C CB . HIS A 1 199 ? 39.301 -18.434 10.544 1.00 26.69 ? 218 HIS A CB 1 ATOM 1504 C CG . HIS A 1 199 ? 40.167 -17.285 10.143 1.00 32.30 ? 218 HIS A CG 1 ATOM 1505 N ND1 . HIS A 1 199 ? 40.581 -17.086 8.843 1.00 34.63 ? 218 HIS A ND1 1 ATOM 1506 C CD2 . HIS A 1 199 ? 40.681 -16.259 10.863 1.00 34.68 ? 218 HIS A CD2 1 ATOM 1507 C CE1 . HIS A 1 199 ? 41.313 -15.988 8.780 1.00 35.57 ? 218 HIS A CE1 1 ATOM 1508 N NE2 . HIS A 1 199 ? 41.389 -15.467 9.992 1.00 35.80 ? 218 HIS A NE2 1 ATOM 1509 N N . PRO A 1 200 ? 36.943 -20.042 8.738 1.00 20.65 ? 219 PRO A N 1 ATOM 1510 C CA . PRO A 1 200 ? 37.235 -19.263 7.535 1.00 19.64 ? 219 PRO A CA 1 ATOM 1511 C C . PRO A 1 200 ? 36.448 -17.957 7.445 1.00 18.76 ? 219 PRO A C 1 ATOM 1512 O O . PRO A 1 200 ? 35.423 -17.773 8.115 1.00 16.67 ? 219 PRO A O 1 ATOM 1513 C CB . PRO A 1 200 ? 36.902 -20.235 6.406 1.00 20.56 ? 219 PRO A CB 1 ATOM 1514 C CG . PRO A 1 200 ? 35.840 -21.090 6.999 1.00 21.09 ? 219 PRO A CG 1 ATOM 1515 C CD . PRO A 1 200 ? 36.383 -21.354 8.381 1.00 21.67 ? 219 PRO A CD 1 ATOM 1516 N N . CYS A 1 201 ? 36.958 -17.055 6.613 1.00 15.82 ? 220 CYS A N 1 ATOM 1517 C CA . CYS A 1 201 ? 36.362 -15.746 6.398 1.00 15.33 ? 220 CYS A CA 1 ATOM 1518 C C . CYS A 1 201 ? 35.155 -15.825 5.463 1.00 15.24 ? 220 CYS A C 1 ATOM 1519 O O . CYS A 1 201 ? 35.048 -16.748 4.662 1.00 14.61 ? 220 CYS A O 1 ATOM 1520 C CB . CYS A 1 201 ? 37.420 -14.808 5.802 1.00 15.32 ? 220 CYS A CB 1 ATOM 1521 S SG . CYS A 1 201 ? 38.911 -14.597 6.834 1.00 16.35 ? 220 CYS A SG 1 ATOM 1522 N N . GLY A 1 202 ? 34.234 -14.873 5.585 1.00 15.75 ? 221 GLY A N 1 ATOM 1523 C CA . GLY A 1 202 ? 33.080 -14.842 4.699 1.00 17.01 ? 221 GLY A CA 1 ATOM 1524 C C . GLY A 1 202 ? 31.835 -15.653 5.016 1.00 16.99 ? 221 GLY A C 1 ATOM 1525 O O . GLY A 1 202 ? 30.952 -15.778 4.168 1.00 17.74 ? 221 GLY A O 1 ATOM 1526 N N . GLN A 1 203 A 31.746 -16.208 6.218 1.00 17.52 ? 221 GLN A N 1 ATOM 1527 C CA . GLN A 1 203 A 30.567 -16.981 6.593 1.00 16.28 ? 221 GLN A CA 1 ATOM 1528 C C . GLN A 1 203 A 29.384 -16.049 6.829 1.00 16.70 ? 221 GLN A C 1 ATOM 1529 O O . GLN A 1 203 A 29.505 -15.043 7.527 1.00 15.53 ? 221 GLN A O 1 ATOM 1530 C CB . GLN A 1 203 A 30.838 -17.782 7.864 1.00 18.37 ? 221 GLN A CB 1 ATOM 1531 C CG . GLN A 1 203 A 31.771 -18.960 7.678 1.00 18.35 ? 221 GLN A CG 1 ATOM 1532 C CD . GLN A 1 203 A 32.172 -19.575 9.002 1.00 20.99 ? 221 GLN A CD 1 ATOM 1533 O OE1 . GLN A 1 203 A 33.216 -19.238 9.569 1.00 23.45 ? 221 GLN A OE1 1 ATOM 1534 N NE2 . GLN A 1 203 A 31.335 -20.466 9.515 1.00 19.26 ? 221 GLN A NE2 1 ATOM 1535 N N . GLY A 1 204 ? 28.240 -16.385 6.244 1.00 16.07 ? 222 GLY A N 1 ATOM 1536 C CA . GLY A 1 204 ? 27.058 -15.560 6.418 1.00 15.77 ? 222 GLY A CA 1 ATOM 1537 C C . GLY A 1 204 ? 26.663 -15.300 7.865 1.00 15.28 ? 222 GLY A C 1 ATOM 1538 O O . GLY A 1 204 ? 26.382 -14.159 8.231 1.00 16.06 ? 222 GLY A O 1 ATOM 1539 N N . PRO A 1 205 ? 26.626 -16.336 8.718 1.00 15.14 ? 223 PRO A N 1 ATOM 1540 C CA . PRO A 1 205 ? 26.249 -16.152 10.124 1.00 14.88 ? 223 PRO A CA 1 ATOM 1541 C C . PRO A 1 205 ? 27.296 -15.506 11.037 1.00 14.83 ? 223 PRO A C 1 ATOM 1542 O O . PRO A 1 205 ? 27.020 -15.225 12.204 1.00 13.20 ? 223 PRO A O 1 ATOM 1543 C CB . PRO A 1 205 ? 25.876 -17.568 10.564 1.00 16.05 ? 223 PRO A CB 1 ATOM 1544 C CG . PRO A 1 205 ? 26.761 -18.418 9.733 1.00 16.76 ? 223 PRO A CG 1 ATOM 1545 C CD . PRO A 1 205 ? 26.687 -17.767 8.377 1.00 14.56 ? 223 PRO A CD 1 ATOM 1546 N N . LYS A 1 206 ? 28.491 -15.264 10.513 1.00 14.02 ? 224 LYS A N 1 ATOM 1547 C CA . LYS A 1 206 ? 29.539 -14.647 11.312 1.00 14.52 ? 224 LYS A CA 1 ATOM 1548 C C . LYS A 1 206 ? 30.134 -13.445 10.595 1.00 14.24 ? 224 LYS A C 1 ATOM 1549 O O . LYS A 1 206 ? 31.242 -13.507 10.070 1.00 13.98 ? 224 LYS A O 1 ATOM 1550 C CB . LYS A 1 206 ? 30.631 -15.666 11.629 1.00 15.46 ? 224 LYS A CB 1 ATOM 1551 C CG . LYS A 1 206 ? 30.125 -16.839 12.450 1.00 19.03 ? 224 LYS A CG 1 ATOM 1552 C CD . LYS A 1 206 ? 31.262 -17.654 13.041 1.00 21.97 ? 224 LYS A CD 1 ATOM 1553 C CE . LYS A 1 206 ? 30.730 -18.915 13.702 1.00 24.82 ? 224 LYS A CE 1 ATOM 1554 N NZ . LYS A 1 206 ? 29.647 -18.603 14.677 1.00 25.60 ? 224 LYS A NZ 1 ATOM 1555 N N . PRO A 1 207 ? 29.392 -12.330 10.557 1.00 13.13 ? 225 PRO A N 1 ATOM 1556 C CA . PRO A 1 207 ? 29.890 -11.126 9.889 1.00 12.30 ? 225 PRO A CA 1 ATOM 1557 C C . PRO A 1 207 ? 31.081 -10.519 10.626 1.00 11.62 ? 225 PRO A C 1 ATOM 1558 O O . PRO A 1 207 ? 31.490 -11.004 11.683 1.00 11.80 ? 225 PRO A O 1 ATOM 1559 C CB . PRO A 1 207 ? 28.667 -10.212 9.866 1.00 12.96 ? 225 PRO A CB 1 ATOM 1560 C CG . PRO A 1 207 ? 27.909 -10.625 11.093 1.00 13.65 ? 225 PRO A CG 1 ATOM 1561 C CD . PRO A 1 207 ? 28.037 -12.125 11.097 1.00 12.53 ? 225 PRO A CD 1 ATOM 1562 N N . GLY A 1 208 ? 31.647 -9.465 10.055 1.00 12.05 ? 226 GLY A N 1 ATOM 1563 C CA . GLY A 1 208 ? 32.786 -8.825 10.678 1.00 9.00 ? 226 GLY A CA 1 ATOM 1564 C C . GLY A 1 208 ? 32.372 -7.908 11.809 1.00 10.76 ? 226 GLY A C 1 ATOM 1565 O O . GLY A 1 208 ? 31.263 -7.377 11.814 1.00 8.44 ? 226 GLY A O 1 ATOM 1566 N N . ILE A 1 209 ? 33.269 -7.742 12.774 1.00 9.54 ? 227 ILE A N 1 ATOM 1567 C CA . ILE A 1 209 ? 33.039 -6.878 13.924 1.00 11.02 ? 227 ILE A CA 1 ATOM 1568 C C . ILE A 1 209 ? 34.017 -5.717 13.781 1.00 11.06 ? 227 ILE A C 1 ATOM 1569 O O . ILE A 1 209 ? 35.214 -5.926 13.572 1.00 12.68 ? 227 ILE A O 1 ATOM 1570 C CB . ILE A 1 209 ? 33.315 -7.623 15.255 1.00 10.36 ? 227 ILE A CB 1 ATOM 1571 C CG1 . ILE A 1 209 ? 32.319 -8.770 15.421 1.00 11.61 ? 227 ILE A CG1 1 ATOM 1572 C CG2 . ILE A 1 209 ? 33.207 -6.669 16.424 1.00 10.17 ? 227 ILE A CG2 1 ATOM 1573 C CD1 . ILE A 1 209 ? 32.581 -9.656 16.613 1.00 12.03 ? 227 ILE A CD1 1 ATOM 1574 N N . TYR A 1 210 ? 33.498 -4.500 13.885 1.00 10.15 ? 228 TYR A N 1 ATOM 1575 C CA . TYR A 1 210 ? 34.313 -3.307 13.748 1.00 11.14 ? 228 TYR A CA 1 ATOM 1576 C C . TYR A 1 210 ? 34.139 -2.388 14.946 1.00 11.22 ? 228 TYR A C 1 ATOM 1577 O O . TYR A 1 210 ? 33.066 -2.312 15.534 1.00 12.46 ? 228 TYR A O 1 ATOM 1578 C CB . TYR A 1 210 ? 33.926 -2.559 12.469 1.00 11.35 ? 228 TYR A CB 1 ATOM 1579 C CG . TYR A 1 210 ? 34.027 -3.411 11.217 1.00 13.48 ? 228 TYR A CG 1 ATOM 1580 C CD1 . TYR A 1 210 ? 33.089 -4.415 10.949 1.00 11.81 ? 228 TYR A CD1 1 ATOM 1581 C CD2 . TYR A 1 210 ? 35.086 -3.244 10.323 1.00 10.60 ? 228 TYR A CD2 1 ATOM 1582 C CE1 . TYR A 1 210 ? 33.210 -5.228 9.829 1.00 9.64 ? 228 TYR A CE1 1 ATOM 1583 C CE2 . TYR A 1 210 ? 35.212 -4.052 9.201 1.00 12.10 ? 228 TYR A CE2 1 ATOM 1584 C CZ . TYR A 1 210 ? 34.274 -5.040 8.959 1.00 11.38 ? 228 TYR A CZ 1 ATOM 1585 O OH . TYR A 1 210 ? 34.399 -5.835 7.843 1.00 13.71 ? 228 TYR A OH 1 ATOM 1586 N N . THR A 1 211 ? 35.204 -1.689 15.308 1.00 11.92 ? 229 THR A N 1 ATOM 1587 C CA . THR A 1 211 ? 35.151 -0.759 16.426 1.00 12.08 ? 229 THR A CA 1 ATOM 1588 C C . THR A 1 211 ? 34.321 0.453 16.011 1.00 11.83 ? 229 THR A C 1 ATOM 1589 O O . THR A 1 211 ? 34.528 1.009 14.933 1.00 12.54 ? 229 THR A O 1 ATOM 1590 C CB . THR A 1 211 ? 36.565 -0.298 16.806 1.00 11.79 ? 229 THR A CB 1 ATOM 1591 O OG1 . THR A 1 211 ? 37.353 -1.444 17.140 1.00 10.80 ? 229 THR A OG1 1 ATOM 1592 C CG2 . THR A 1 211 ? 36.525 0.657 17.995 1.00 11.99 ? 229 THR A CG2 1 ATOM 1593 N N . ASN A 1 212 ? 33.379 0.854 16.858 1.00 11.17 ? 230 ASN A N 1 ATOM 1594 C CA . ASN A 1 212 ? 32.531 2.005 16.558 1.00 12.91 ? 230 ASN A CA 1 ATOM 1595 C C . ASN A 1 212 ? 33.342 3.285 16.759 1.00 13.54 ? 230 ASN A C 1 ATOM 1596 O O . ASN A 1 212 ? 33.487 3.765 17.884 1.00 13.93 ? 230 ASN A O 1 ATOM 1597 C CB . ASN A 1 212 ? 31.314 2.017 17.487 1.00 13.60 ? 230 ASN A CB 1 ATOM 1598 C CG . ASN A 1 212 ? 30.288 3.065 17.097 1.00 17.53 ? 230 ASN A CG 1 ATOM 1599 O OD1 . ASN A 1 212 ? 30.609 4.063 16.446 1.00 20.80 ? 230 ASN A OD1 1 ATOM 1600 N ND2 . ASN A 1 212 ? 29.047 2.850 17.506 1.00 17.96 ? 230 ASN A ND2 1 ATOM 1601 N N . VAL A 1 213 ? 33.855 3.847 15.669 1.00 12.74 ? 231 VAL A N 1 ATOM 1602 C CA . VAL A 1 213 ? 34.668 5.059 15.752 1.00 14.37 ? 231 VAL A CA 1 ATOM 1603 C C . VAL A 1 213 ? 33.947 6.288 16.310 1.00 13.69 ? 231 VAL A C 1 ATOM 1604 O O . VAL A 1 213 ? 34.521 7.033 17.098 1.00 12.72 ? 231 VAL A O 1 ATOM 1605 C CB . VAL A 1 213 ? 35.272 5.430 14.370 1.00 13.05 ? 231 VAL A CB 1 ATOM 1606 C CG1 . VAL A 1 213 ? 36.129 6.685 14.498 1.00 15.02 ? 231 VAL A CG1 1 ATOM 1607 C CG2 . VAL A 1 213 ? 36.108 4.271 13.838 1.00 13.87 ? 231 VAL A CG2 1 ATOM 1608 N N . PHE A 1 214 ? 32.697 6.498 15.908 1.00 15.75 ? 232 PHE A N 1 ATOM 1609 C CA . PHE A 1 214 ? 31.934 7.655 16.374 1.00 16.90 ? 232 PHE A CA 1 ATOM 1610 C C . PHE A 1 214 ? 31.913 7.816 17.891 1.00 16.24 ? 232 PHE A C 1 ATOM 1611 O O . PHE A 1 214 ? 32.001 8.933 18.405 1.00 15.15 ? 232 PHE A O 1 ATOM 1612 C CB . PHE A 1 214 ? 30.490 7.587 15.880 1.00 20.46 ? 232 PHE A CB 1 ATOM 1613 C CG . PHE A 1 214 ? 29.701 8.840 16.164 1.00 24.88 ? 232 PHE A CG 1 ATOM 1614 C CD1 . PHE A 1 214 ? 29.919 9.997 15.418 1.00 25.45 ? 232 PHE A CD1 1 ATOM 1615 C CD2 . PHE A 1 214 ? 28.763 8.872 17.193 1.00 24.85 ? 232 PHE A CD2 1 ATOM 1616 C CE1 . PHE A 1 214 ? 29.213 11.167 15.691 1.00 27.87 ? 232 PHE A CE1 1 ATOM 1617 C CE2 . PHE A 1 214 ? 28.051 10.038 17.475 1.00 26.37 ? 232 PHE A CE2 1 ATOM 1618 C CZ . PHE A 1 214 ? 28.278 11.187 16.723 1.00 26.32 ? 232 PHE A CZ 1 ATOM 1619 N N . ASP A 1 215 ? 31.779 6.701 18.602 1.00 16.16 ? 233 ASP A N 1 ATOM 1620 C CA . ASP A 1 215 ? 31.741 6.723 20.059 1.00 16.49 ? 233 ASP A CA 1 ATOM 1621 C C . ASP A 1 215 ? 33.038 7.193 20.714 1.00 15.66 ? 233 ASP A C 1 ATOM 1622 O O . ASP A 1 215 ? 33.038 7.557 21.886 1.00 14.44 ? 233 ASP A O 1 ATOM 1623 C CB . ASP A 1 215 ? 31.387 5.334 20.598 1.00 18.03 ? 233 ASP A CB 1 ATOM 1624 C CG . ASP A 1 215 ? 29.893 5.063 20.576 1.00 20.48 ? 233 ASP A CG 1 ATOM 1625 O OD1 . ASP A 1 215 ? 29.136 5.929 20.096 1.00 20.44 ? 233 ASP A OD1 1 ATOM 1626 O OD2 . ASP A 1 215 ? 29.477 3.981 21.043 1.00 22.09 ? 233 ASP A OD2 1 ATOM 1627 N N . TYR A 1 216 ? 34.138 7.188 19.967 1.00 15.41 ? 234 TYR A N 1 ATOM 1628 C CA . TYR A 1 216 ? 35.426 7.601 20.525 1.00 15.15 ? 234 TYR A CA 1 ATOM 1629 C C . TYR A 1 216 ? 35.933 8.941 20.017 1.00 16.09 ? 234 TYR A C 1 ATOM 1630 O O . TYR A 1 216 ? 37.023 9.359 20.394 1.00 14.22 ? 234 TYR A O 1 ATOM 1631 C CB . TYR A 1 216 ? 36.507 6.557 20.228 1.00 12.47 ? 234 TYR A CB 1 ATOM 1632 C CG . TYR A 1 216 ? 36.297 5.209 20.883 1.00 15.07 ? 234 TYR A CG 1 ATOM 1633 C CD1 . TYR A 1 216 ? 35.444 4.261 20.320 1.00 14.31 ? 234 TYR A CD1 1 ATOM 1634 C CD2 . TYR A 1 216 ? 36.944 4.885 22.076 1.00 13.85 ? 234 TYR A CD2 1 ATOM 1635 C CE1 . TYR A 1 216 ? 35.239 3.022 20.930 1.00 12.17 ? 234 TYR A CE1 1 ATOM 1636 C CE2 . TYR A 1 216 ? 36.745 3.650 22.696 1.00 12.74 ? 234 TYR A CE2 1 ATOM 1637 C CZ . TYR A 1 216 ? 35.891 2.729 22.117 1.00 11.31 ? 234 TYR A CZ 1 ATOM 1638 O OH . TYR A 1 216 ? 35.677 1.521 22.734 1.00 12.70 ? 234 TYR A OH 1 ATOM 1639 N N . THR A 1 217 ? 35.163 9.612 19.165 1.00 17.49 ? 235 THR A N 1 ATOM 1640 C CA . THR A 1 217 ? 35.614 10.890 18.613 1.00 20.53 ? 235 THR A CA 1 ATOM 1641 C C . THR A 1 217 ? 35.981 11.920 19.681 1.00 21.03 ? 235 THR A C 1 ATOM 1642 O O . THR A 1 217 ? 36.926 12.687 19.510 1.00 21.39 ? 235 THR A O 1 ATOM 1643 C CB . THR A 1 217 ? 34.566 11.491 17.637 1.00 22.71 ? 235 THR A CB 1 ATOM 1644 O OG1 . THR A 1 217 ? 33.292 11.595 18.287 1.00 24.30 ? 235 THR A OG1 1 ATOM 1645 C CG2 . THR A 1 217 ? 34.432 10.604 16.397 1.00 23.73 ? 235 THR A CG2 1 ATOM 1646 N N . ASP A 1 218 ? 35.249 11.930 20.787 1.00 19.87 ? 236 ASP A N 1 ATOM 1647 C CA . ASP A 1 218 ? 35.538 12.862 21.866 1.00 21.62 ? 236 ASP A CA 1 ATOM 1648 C C . ASP A 1 218 ? 36.926 12.569 22.446 1.00 20.97 ? 236 ASP A C 1 ATOM 1649 O O . ASP A 1 218 ? 37.779 13.455 22.529 1.00 20.83 ? 236 ASP A O 1 ATOM 1650 C CB . ASP A 1 218 ? 34.476 12.741 22.961 1.00 24.95 ? 236 ASP A CB 1 ATOM 1651 C CG . ASP A 1 218 ? 34.704 13.712 24.103 1.00 27.83 ? 236 ASP A CG 1 ATOM 1652 O OD1 . ASP A 1 218 ? 34.693 14.936 23.850 1.00 29.99 ? 236 ASP A OD1 1 ATOM 1653 O OD2 . ASP A 1 218 ? 34.897 13.250 25.249 1.00 30.40 ? 236 ASP A OD2 1 ATOM 1654 N N . TRP A 1 219 ? 37.145 11.319 22.844 1.00 18.67 ? 237 TRP A N 1 ATOM 1655 C CA . TRP A 1 219 ? 38.427 10.901 23.404 1.00 18.17 ? 237 TRP A CA 1 ATOM 1656 C C . TRP A 1 219 ? 39.583 11.208 22.442 1.00 18.89 ? 237 TRP A C 1 ATOM 1657 O O . TRP A 1 219 ? 40.653 11.646 22.863 1.00 17.83 ? 237 TRP A O 1 ATOM 1658 C CB . TRP A 1 219 ? 38.393 9.399 23.717 1.00 18.35 ? 237 TRP A CB 1 ATOM 1659 C CG . TRP A 1 219 ? 39.715 8.819 24.151 1.00 19.58 ? 237 TRP A CG 1 ATOM 1660 C CD1 . TRP A 1 219 ? 40.356 9.022 25.343 1.00 20.92 ? 237 TRP A CD1 1 ATOM 1661 C CD2 . TRP A 1 219 ? 40.562 7.947 23.386 1.00 20.46 ? 237 TRP A CD2 1 ATOM 1662 N NE1 . TRP A 1 219 ? 41.550 8.330 25.366 1.00 21.29 ? 237 TRP A NE1 1 ATOM 1663 C CE2 . TRP A 1 219 ? 41.699 7.664 24.178 1.00 20.64 ? 237 TRP A CE2 1 ATOM 1664 C CE3 . TRP A 1 219 ? 40.469 7.377 22.108 1.00 20.87 ? 237 TRP A CE3 1 ATOM 1665 C CZ2 . TRP A 1 219 ? 42.735 6.836 23.732 1.00 19.31 ? 237 TRP A CZ2 1 ATOM 1666 C CZ3 . TRP A 1 219 ? 41.504 6.551 21.665 1.00 19.16 ? 237 TRP A CZ3 1 ATOM 1667 C CH2 . TRP A 1 219 ? 42.620 6.291 22.477 1.00 18.69 ? 237 TRP A CH2 1 ATOM 1668 N N . ILE A 1 220 ? 39.366 10.973 21.151 1.00 18.51 ? 238 ILE A N 1 ATOM 1669 C CA . ILE A 1 220 ? 40.398 11.235 20.155 1.00 19.70 ? 238 ILE A CA 1 ATOM 1670 C C . ILE A 1 220 ? 40.726 12.726 20.102 1.00 21.20 ? 238 ILE A C 1 ATOM 1671 O O . ILE A 1 220 ? 41.882 13.122 20.233 1.00 21.88 ? 238 ILE A O 1 ATOM 1672 C CB . ILE A 1 220 ? 39.956 10.763 18.743 1.00 19.80 ? 238 ILE A CB 1 ATOM 1673 C CG1 . ILE A 1 220 ? 39.738 9.246 18.740 1.00 18.51 ? 238 ILE A CG1 1 ATOM 1674 C CG2 . ILE A 1 220 ? 41.005 11.138 17.720 1.00 17.35 ? 238 ILE A CG2 1 ATOM 1675 C CD1 . ILE A 1 220 ? 39.283 8.684 17.409 1.00 18.72 ? 238 ILE A CD1 1 ATOM 1676 N N . GLN A 1 221 ? 39.704 13.552 19.918 1.00 21.54 ? 239 GLN A N 1 ATOM 1677 C CA . GLN A 1 221 ? 39.906 14.994 19.845 1.00 24.82 ? 239 GLN A CA 1 ATOM 1678 C C . GLN A 1 221 ? 40.563 15.566 21.099 1.00 24.12 ? 239 GLN A C 1 ATOM 1679 O O . GLN A 1 221 ? 41.345 16.507 21.012 1.00 24.78 ? 239 GLN A O 1 ATOM 1680 C CB . GLN A 1 221 ? 38.575 15.691 19.568 1.00 27.88 ? 239 GLN A CB 1 ATOM 1681 C CG . GLN A 1 221 ? 37.978 15.295 18.226 1.00 32.51 ? 239 GLN A CG 1 ATOM 1682 C CD . GLN A 1 221 ? 36.656 15.971 17.943 1.00 36.47 ? 239 GLN A CD 1 ATOM 1683 O OE1 . GLN A 1 221 ? 35.693 15.826 18.700 1.00 38.25 ? 239 GLN A OE1 1 ATOM 1684 N NE2 . GLN A 1 221 ? 36.600 16.717 16.844 1.00 38.32 ? 239 GLN A NE2 1 ATOM 1685 N N . ARG A 1 222 ? 40.255 14.997 22.259 1.00 25.34 ? 240 ARG A N 1 ATOM 1686 C CA . ARG A 1 222 ? 40.858 15.461 23.507 1.00 26.78 ? 240 ARG A CA 1 ATOM 1687 C C . ARG A 1 222 ? 42.345 15.108 23.567 1.00 27.14 ? 240 ARG A C 1 ATOM 1688 O O . ARG A 1 222 ? 43.147 15.875 24.098 1.00 26.16 ? 240 ARG A O 1 ATOM 1689 C CB . ARG A 1 222 ? 40.124 14.866 24.713 1.00 29.58 ? 240 ARG A CB 1 ATOM 1690 C CG . ARG A 1 222 ? 38.762 15.499 24.962 1.00 32.57 ? 240 ARG A CG 1 ATOM 1691 C CD . ARG A 1 222 ? 38.046 14.890 26.157 1.00 36.31 ? 240 ARG A CD 1 ATOM 1692 N NE . ARG A 1 222 ? 36.773 15.564 26.405 1.00 41.62 ? 240 ARG A NE 1 ATOM 1693 C CZ . ARG A 1 222 ? 35.889 15.197 27.329 1.00 45.21 ? 240 ARG A CZ 1 ATOM 1694 N NH1 . ARG A 1 222 ? 36.127 14.149 28.109 1.00 47.62 ? 240 ARG A NH1 1 ATOM 1695 N NH2 . ARG A 1 222 ? 34.762 15.879 27.477 1.00 45.89 ? 240 ARG A NH2 1 ATOM 1696 N N . ASN A 1 223 ? 42.712 13.948 23.026 1.00 26.36 ? 241 ASN A N 1 ATOM 1697 C CA . ASN A 1 223 ? 44.111 13.531 23.009 1.00 26.55 ? 241 ASN A CA 1 ATOM 1698 C C . ASN A 1 223 ? 44.885 14.396 22.024 1.00 26.13 ? 241 ASN A C 1 ATOM 1699 O O . ASN A 1 223 ? 46.025 14.767 22.274 1.00 25.92 ? 241 ASN A O 1 ATOM 1700 C CB . ASN A 1 223 ? 44.237 12.056 22.607 1.00 26.55 ? 241 ASN A CB 1 ATOM 1701 C CG . ASN A 1 223 ? 44.007 11.111 23.776 1.00 27.95 ? 241 ASN A CG 1 ATOM 1702 O OD1 . ASN A 1 223 ? 44.776 11.097 24.736 1.00 28.90 ? 241 ASN A OD1 1 ATOM 1703 N ND2 . ASN A 1 223 ? 42.945 10.323 23.701 1.00 29.14 ? 241 ASN A ND2 1 ATOM 1704 N N . ILE A 1 224 ? 44.255 14.711 20.900 1.00 26.35 ? 242 ILE A N 1 ATOM 1705 C CA . ILE A 1 224 ? 44.882 15.539 19.883 1.00 26.94 ? 242 ILE A CA 1 ATOM 1706 C C . ILE A 1 224 ? 45.056 16.958 20.411 1.00 29.02 ? 242 ILE A C 1 ATOM 1707 O O . ILE A 1 224 ? 46.055 17.616 20.125 1.00 28.11 ? 242 ILE A O 1 ATOM 1708 C CB . ILE A 1 224 ? 44.028 15.573 18.600 1.00 27.04 ? 242 ILE A CB 1 ATOM 1709 C CG1 . ILE A 1 224 ? 44.043 14.194 17.934 1.00 25.04 ? 242 ILE A CG1 1 ATOM 1710 C CG2 . ILE A 1 224 ? 44.543 16.650 17.658 1.00 27.49 ? 242 ILE A CG2 1 ATOM 1711 C CD1 . ILE A 1 224 ? 43.185 14.099 16.693 1.00 25.19 ? 242 ILE A CD1 1 ATOM 1712 N N . ALA A 1 225 ? 44.081 17.419 21.190 1.00 30.69 ? 243 ALA A N 1 ATOM 1713 C CA . ALA A 1 225 ? 44.120 18.760 21.766 1.00 33.66 ? 243 ALA A CA 1 ATOM 1714 C C . ALA A 1 225 ? 45.209 18.894 22.832 1.00 35.42 ? 243 ALA A C 1 ATOM 1715 O O . ALA A 1 225 ? 45.637 20.000 23.148 1.00 36.78 ? 243 ALA A O 1 ATOM 1716 C CB . ALA A 1 225 ? 42.757 19.121 22.354 1.00 32.27 ? 243 ALA A CB 1 ATOM 1717 N N . GLY A 1 226 ? 45.651 17.774 23.393 1.00 37.62 ? 244 GLY A N 1 ATOM 1718 C CA . GLY A 1 226 ? 46.700 17.836 24.393 1.00 41.18 ? 244 GLY A CA 1 ATOM 1719 C C . GLY A 1 226 ? 46.374 17.331 25.786 1.00 44.34 ? 244 GLY A C 1 ATOM 1720 O O . GLY A 1 226 ? 47.203 17.446 26.686 1.00 45.45 ? 244 GLY A O 1 ATOM 1721 N N . ASN A 1 227 ? 45.182 16.781 25.987 1.00 47.07 ? 245 ASN A N 1 ATOM 1722 C CA . ASN A 1 227 ? 44.821 16.265 27.304 1.00 50.25 ? 245 ASN A CA 1 ATOM 1723 C C . ASN A 1 227 ? 45.607 14.999 27.605 1.00 52.12 ? 245 ASN A C 1 ATOM 1724 O O . ASN A 1 227 ? 46.201 14.866 28.676 1.00 53.25 ? 245 ASN A O 1 ATOM 1725 C CB . ASN A 1 227 ? 43.324 15.964 27.378 1.00 50.84 ? 245 ASN A CB 1 ATOM 1726 C CG . ASN A 1 227 ? 42.494 17.208 27.597 1.00 51.00 ? 245 ASN A CG 1 ATOM 1727 O OD1 . ASN A 1 227 ? 42.623 18.188 26.864 1.00 51.56 ? 245 ASN A OD1 1 ATOM 1728 N ND2 . ASN A 1 227 ? 41.634 17.176 28.609 1.00 50.29 ? 245 ASN A ND2 1 ATOM 1729 N N . THR A 1 228 A 45.601 14.072 26.651 1.00 54.07 ? 245 THR A N 1 ATOM 1730 C CA . THR A 1 228 A 46.314 12.805 26.786 1.00 55.56 ? 245 THR A CA 1 ATOM 1731 C C . THR A 1 228 A 46.059 12.152 28.145 1.00 55.75 ? 245 THR A C 1 ATOM 1732 O O . THR A 1 228 A 46.784 11.245 28.557 1.00 56.75 ? 245 THR A O 1 ATOM 1733 C CB . THR A 1 228 A 47.833 13.009 26.606 1.00 56.64 ? 245 THR A CB 1 ATOM 1734 O OG1 . THR A 1 228 A 48.353 13.759 27.713 1.00 57.68 ? 245 THR A OG1 1 ATOM 1735 C CG2 . THR A 1 228 A 48.114 13.769 25.309 1.00 56.96 ? 245 THR A CG2 1 ATOM 1736 N N . ASP A 1 229 B 45.019 12.619 28.828 1.00 55.42 ? 245 ASP A N 1 ATOM 1737 C CA . ASP A 1 229 B 44.647 12.111 30.144 1.00 54.19 ? 245 ASP A CA 1 ATOM 1738 C C . ASP A 1 229 B 43.223 11.569 30.094 1.00 51.96 ? 245 ASP A C 1 ATOM 1739 O O . ASP A 1 229 B 42.866 10.651 30.833 1.00 52.60 ? 245 ASP A O 1 ATOM 1740 C CB . ASP A 1 229 B 44.716 13.242 31.173 1.00 56.21 ? 245 ASP A CB 1 ATOM 1741 C CG . ASP A 1 229 B 43.655 14.310 30.936 1.00 58.07 ? 245 ASP A CG 1 ATOM 1742 O OD1 . ASP A 1 229 B 42.457 14.017 31.135 1.00 59.32 ? 245 ASP A OD1 1 ATOM 1743 O OD2 . ASP A 1 229 B 44.015 15.441 30.544 1.00 59.31 ? 245 ASP A OD2 1 ATOM 1744 N N . ALA A 1 230 C 42.417 12.158 29.216 1.00 48.35 ? 245 ALA A N 1 ATOM 1745 C CA . ALA A 1 230 C 41.023 11.773 29.046 1.00 44.37 ? 245 ALA A CA 1 ATOM 1746 C C . ALA A 1 230 C 40.820 10.263 29.004 1.00 41.13 ? 245 ALA A C 1 ATOM 1747 O O . ALA A 1 230 C 41.702 9.509 28.586 1.00 40.19 ? 245 ALA A O 1 ATOM 1748 C CB . ALA A 1 230 C 40.467 12.405 27.779 1.00 44.70 ? 245 ALA A CB 1 ATOM 1749 N N . THR A 1 231 D 39.648 9.829 29.449 1.00 37.31 ? 245 THR A N 1 ATOM 1750 C CA . THR A 1 231 D 39.307 8.415 29.457 1.00 34.34 ? 245 THR A CA 1 ATOM 1751 C C . THR A 1 231 D 38.345 8.118 28.316 1.00 31.09 ? 245 THR A C 1 ATOM 1752 O O . THR A 1 231 D 37.693 9.017 27.781 1.00 30.01 ? 245 THR A O 1 ATOM 1753 C CB . THR A 1 231 D 38.627 8.006 30.775 1.00 34.78 ? 245 THR A CB 1 ATOM 1754 O OG1 . THR A 1 231 D 37.480 8.837 30.992 1.00 35.25 ? 245 THR A OG1 1 ATOM 1755 C CG2 . THR A 1 231 D 39.588 8.147 31.944 1.00 36.02 ? 245 THR A CG2 1 ATOM 1756 N N . CYS A 1 232 E 38.257 6.848 27.949 1.00 27.33 ? 245 CYS A N 1 ATOM 1757 C CA . CYS A 1 232 E 37.371 6.428 26.878 1.00 24.34 ? 245 CYS A CA 1 ATOM 1758 C C . CYS A 1 232 E 35.986 6.132 27.416 1.00 23.53 ? 245 CYS A C 1 ATOM 1759 O O . CYS A 1 232 E 35.813 5.908 28.612 1.00 23.51 ? 245 CYS A O 1 ATOM 1760 C CB . CYS A 1 232 E 37.904 5.163 26.224 1.00 21.87 ? 245 CYS A CB 1 ATOM 1761 S SG . CYS A 1 232 E 39.465 5.390 25.342 1.00 18.07 ? 245 CYS A SG 1 ATOM 1762 N N . PRO A 1 233 F 34.974 6.135 26.538 1.00 23.06 ? 245 PRO A N 1 ATOM 1763 C CA . PRO A 1 233 F 33.630 5.835 27.034 1.00 22.23 ? 245 PRO A CA 1 ATOM 1764 C C . PRO A 1 233 F 33.698 4.424 27.618 1.00 22.26 ? 245 PRO A C 1 ATOM 1765 O O . PRO A 1 233 F 34.392 3.563 27.079 1.00 20.42 ? 245 PRO A O 1 ATOM 1766 C CB . PRO A 1 233 F 32.770 5.916 25.774 1.00 22.16 ? 245 PRO A CB 1 ATOM 1767 C CG . PRO A 1 233 F 33.734 5.550 24.674 1.00 23.80 ? 245 PRO A CG 1 ATOM 1768 C CD . PRO A 1 233 F 34.977 6.305 25.076 1.00 22.78 ? 245 PRO A CD 1 ATOM 1769 N N . PRO A 1 234 G 32.994 4.174 28.734 1.00 22.50 ? 245 PRO A N 1 ATOM 1770 C CA . PRO A 1 234 G 33.011 2.852 29.363 1.00 23.40 ? 245 PRO A CA 1 ATOM 1771 C C . PRO A 1 234 G 32.341 1.760 28.538 1.00 23.79 ? 245 PRO A C 1 ATOM 1772 O O . PRO A 1 234 G 31.685 2.090 27.530 1.00 24.67 ? 245 PRO A O 1 ATOM 1773 C CB . PRO A 1 234 G 32.294 3.099 30.682 1.00 22.40 ? 245 PRO A CB 1 ATOM 1774 C CG . PRO A 1 234 G 31.288 4.133 30.308 1.00 22.62 ? 245 PRO A CG 1 ATOM 1775 C CD . PRO A 1 234 G 32.100 5.088 29.469 1.00 23.56 ? 245 PRO A CD 1 ATOM 1776 O OXT . PRO A 1 234 G 32.478 0.585 28.927 1.00 24.75 ? 245 PRO A OXT 1 HETATM 1777 C C1 . NAG B 2 . ? 55.376 -7.663 13.392 1.00 38.58 ? 301 NAG A C1 1 HETATM 1778 C C2 . NAG B 2 . ? 55.821 -8.866 14.215 1.00 41.92 ? 301 NAG A C2 1 HETATM 1779 C C3 . NAG B 2 . ? 54.673 -9.878 14.224 1.00 44.09 ? 301 NAG A C3 1 HETATM 1780 C C4 . NAG B 2 . ? 53.451 -9.215 14.872 1.00 44.28 ? 301 NAG A C4 1 HETATM 1781 C C5 . NAG B 2 . ? 53.098 -7.903 14.149 1.00 43.11 ? 301 NAG A C5 1 HETATM 1782 C C6 . NAG B 2 . ? 52.025 -7.119 14.888 1.00 43.95 ? 301 NAG A C6 1 HETATM 1783 C C7 . NAG B 2 . ? 58.205 -9.180 14.288 1.00 43.70 ? 301 NAG A C7 1 HETATM 1784 C C8 . NAG B 2 . ? 59.480 -9.544 13.546 1.00 43.50 ? 301 NAG A C8 1 HETATM 1785 N N2 . NAG B 2 . ? 57.045 -9.442 13.688 1.00 43.28 ? 301 NAG A N2 1 HETATM 1786 O O3 . NAG B 2 . ? 55.044 -11.041 14.953 1.00 44.71 ? 301 NAG A O3 1 HETATM 1787 O O4 . NAG B 2 . ? 52.338 -10.095 14.824 1.00 45.27 ? 301 NAG A O4 1 HETATM 1788 O O5 . NAG B 2 . ? 54.259 -7.036 14.047 1.00 41.92 ? 301 NAG A O5 1 HETATM 1789 O O6 . NAG B 2 . ? 51.968 -7.475 16.263 1.00 44.58 ? 301 NAG A O6 1 HETATM 1790 O O7 . NAG B 2 . ? 58.277 -8.654 15.402 1.00 45.29 ? 301 NAG A O7 1 HETATM 1791 S S . SO4 C 3 . ? 43.748 17.457 -2.179 1.00 62.64 ? 401 SO4 A S 1 HETATM 1792 O O1 . SO4 C 3 . ? 43.245 16.331 -1.367 1.00 63.54 ? 401 SO4 A O1 1 HETATM 1793 O O2 . SO4 C 3 . ? 43.352 18.732 -1.552 1.00 63.00 ? 401 SO4 A O2 1 HETATM 1794 O O3 . SO4 C 3 . ? 43.167 17.376 -3.531 1.00 63.14 ? 401 SO4 A O3 1 HETATM 1795 O O4 . SO4 C 3 . ? 45.219 17.386 -2.267 1.00 62.28 ? 401 SO4 A O4 1 HETATM 1796 O O . HOH D 4 . ? 48.049 6.604 2.325 1.00 13.60 ? 601 HOH A O 1 HETATM 1797 O O . HOH D 4 . ? 52.957 1.823 -3.984 1.00 10.14 ? 602 HOH A O 1 HETATM 1798 O O . HOH D 4 . ? 42.161 1.280 23.590 1.00 13.36 ? 603 HOH A O 1 HETATM 1799 O O . HOH D 4 . ? 36.319 -2.843 20.810 1.00 11.68 ? 604 HOH A O 1 HETATM 1800 O O . HOH D 4 . ? 41.339 2.801 10.840 1.00 8.06 ? 605 HOH A O 1 HETATM 1801 O O . HOH D 4 . ? 47.171 3.817 0.329 1.00 9.33 ? 606 HOH A O 1 HETATM 1802 O O . HOH D 4 . ? 32.730 -7.854 7.154 1.00 11.19 ? 607 HOH A O 1 HETATM 1803 O O . HOH D 4 . ? 45.504 -4.202 5.320 1.00 13.29 ? 608 HOH A O 1 HETATM 1804 O O . HOH D 4 . ? 43.000 -7.865 0.614 1.00 10.58 ? 609 HOH A O 1 HETATM 1805 O O . HOH D 4 . ? 34.587 10.556 7.688 1.00 18.61 ? 610 HOH A O 1 HETATM 1806 O O . HOH D 4 . ? 31.249 -13.070 6.771 1.00 12.54 ? 611 HOH A O 1 HETATM 1807 O O . HOH D 4 . ? 49.821 3.451 2.386 1.00 15.41 ? 612 HOH A O 1 HETATM 1808 O O . HOH D 4 . ? 38.845 -10.318 -2.611 1.00 18.17 ? 613 HOH A O 1 HETATM 1809 O O . HOH D 4 . ? 47.218 5.938 -1.639 1.00 15.08 ? 614 HOH A O 1 HETATM 1810 O O . HOH D 4 . ? 24.576 -14.878 13.463 1.00 19.06 ? 615 HOH A O 1 HETATM 1811 O O . HOH D 4 . ? 34.893 3.898 -4.266 1.00 13.38 ? 616 HOH A O 1 HETATM 1812 O O . HOH D 4 . ? 36.064 -3.741 18.134 1.00 20.25 ? 617 HOH A O 1 HETATM 1813 O O . HOH D 4 . ? 29.481 -11.188 5.069 1.00 20.95 ? 618 HOH A O 1 HETATM 1814 O O . HOH D 4 . ? 30.619 4.763 1.687 1.00 15.86 ? 619 HOH A O 1 HETATM 1815 O O . HOH D 4 . ? 60.448 -2.046 9.482 1.00 17.25 ? 620 HOH A O 1 HETATM 1816 O O . HOH D 4 . ? 51.651 1.490 -6.918 1.00 18.03 ? 621 HOH A O 1 HETATM 1817 O O . HOH D 4 . ? 34.350 1.475 25.325 1.00 32.36 ? 622 HOH A O 1 HETATM 1818 O O . HOH D 4 . ? 26.064 -2.625 13.333 1.00 18.85 ? 623 HOH A O 1 HETATM 1819 O O . HOH D 4 . ? 28.574 -4.695 -5.152 1.00 30.44 ? 624 HOH A O 1 HETATM 1820 O O . HOH D 4 . ? 33.932 -12.925 9.860 1.00 16.93 ? 625 HOH A O 1 HETATM 1821 O O . HOH D 4 . ? 47.752 4.780 -4.379 1.00 18.57 ? 626 HOH A O 1 HETATM 1822 O O . HOH D 4 . ? 41.116 8.644 -1.696 1.00 17.17 ? 627 HOH A O 1 HETATM 1823 O O . HOH D 4 . ? 26.209 -18.487 19.045 1.00 32.44 ? 628 HOH A O 1 HETATM 1824 O O . HOH D 4 . ? 31.036 5.181 13.823 1.00 21.46 ? 629 HOH A O 1 HETATM 1825 O O . HOH D 4 . ? 44.725 5.959 -3.096 1.00 17.74 ? 630 HOH A O 1 HETATM 1826 O O . HOH D 4 . ? 33.288 -15.778 8.563 1.00 19.65 ? 631 HOH A O 1 HETATM 1827 O O . HOH D 4 . ? 42.347 -17.016 5.258 1.00 20.98 ? 632 HOH A O 1 HETATM 1828 O O . HOH D 4 . ? 40.831 -7.154 -9.249 1.00 23.68 ? 633 HOH A O 1 HETATM 1829 O O . HOH D 4 . ? 41.082 18.120 18.873 1.00 26.28 ? 634 HOH A O 1 HETATM 1830 O O . HOH D 4 . ? 22.275 -2.533 15.607 1.00 23.24 ? 635 HOH A O 1 HETATM 1831 O O . HOH D 4 . ? 37.913 -13.658 -2.971 1.00 24.16 ? 636 HOH A O 1 HETATM 1832 O O . HOH D 4 . ? 42.375 -4.998 21.561 1.00 16.68 ? 637 HOH A O 1 HETATM 1833 O O . HOH D 4 . ? 42.843 -2.740 6.215 1.00 14.04 ? 638 HOH A O 1 HETATM 1834 O O . HOH D 4 . ? 40.423 19.502 -2.537 1.00 36.58 ? 639 HOH A O 1 HETATM 1835 O O . HOH D 4 . ? 37.198 -12.821 9.287 1.00 27.00 ? 640 HOH A O 1 HETATM 1836 O O . HOH D 4 . ? 37.562 4.123 -1.180 1.00 24.17 ? 641 HOH A O 1 HETATM 1837 O O . HOH D 4 . ? 34.962 -0.498 21.425 1.00 26.04 ? 642 HOH A O 1 HETATM 1838 O O . HOH D 4 . ? 50.558 -15.095 0.003 1.00 27.81 ? 643 HOH A O 1 HETATM 1839 O O . HOH D 4 . ? 54.880 -0.342 -1.343 1.00 28.97 ? 644 HOH A O 1 HETATM 1840 O O . HOH D 4 . ? 25.796 -15.941 20.494 1.00 22.98 ? 645 HOH A O 1 HETATM 1841 O O . HOH D 4 . ? 29.843 0.350 26.749 1.00 31.93 ? 646 HOH A O 1 HETATM 1842 O O . HOH D 4 . ? 56.395 5.219 -9.881 1.00 34.21 ? 647 HOH A O 1 HETATM 1843 O O . HOH D 4 . ? 60.107 9.056 -3.686 1.00 24.95 ? 648 HOH A O 1 HETATM 1844 O O . HOH D 4 . ? 42.245 -11.739 -7.450 1.00 38.03 ? 649 HOH A O 1 HETATM 1845 O O . HOH D 4 . ? 58.503 10.476 -1.418 1.00 29.94 ? 650 HOH A O 1 HETATM 1846 O O . HOH D 4 . ? 41.084 -21.062 0.632 1.00 27.02 ? 651 HOH A O 1 HETATM 1847 O O . HOH D 4 . ? 31.079 1.786 -2.330 1.00 22.68 ? 652 HOH A O 1 HETATM 1848 O O . HOH D 4 . ? 27.527 4.193 1.335 1.00 31.18 ? 653 HOH A O 1 HETATM 1849 O O . HOH D 4 . ? 23.223 -15.747 6.905 1.00 27.47 ? 654 HOH A O 1 HETATM 1850 O O . HOH D 4 . ? 58.302 1.253 16.789 1.00 32.01 ? 655 HOH A O 1 HETATM 1851 O O . HOH D 4 . ? 27.317 -18.235 4.250 1.00 21.56 ? 656 HOH A O 1 HETATM 1852 O O . HOH D 4 . ? 34.242 -18.785 2.924 1.00 23.92 ? 657 HOH A O 1 HETATM 1853 O O . HOH D 4 . ? 38.724 -2.225 5.823 1.00 16.98 ? 658 HOH A O 1 HETATM 1854 O O . HOH D 4 . ? 56.257 0.956 18.315 1.00 37.01 ? 659 HOH A O 1 HETATM 1855 O O . HOH D 4 . ? 23.024 -8.161 3.415 1.00 28.82 ? 660 HOH A O 1 HETATM 1856 O O . HOH D 4 . ? 29.362 -5.258 21.148 1.00 21.50 ? 661 HOH A O 1 HETATM 1857 O O . HOH D 4 . ? 21.337 -4.012 6.910 1.00 29.48 ? 662 HOH A O 1 HETATM 1858 O O . HOH D 4 . ? 37.612 3.690 -10.739 1.00 40.40 ? 663 HOH A O 1 HETATM 1859 O O . HOH D 4 . ? 37.758 -10.267 23.604 1.00 29.53 ? 665 HOH A O 1 HETATM 1860 O O . HOH D 4 . ? 53.798 7.557 -8.644 1.00 34.28 ? 666 HOH A O 1 HETATM 1861 O O . HOH D 4 . ? 51.704 -4.708 -8.684 1.00 28.71 ? 667 HOH A O 1 HETATM 1862 O O . HOH D 4 . ? 53.574 13.366 1.079 1.00 37.28 ? 668 HOH A O 1 HETATM 1863 O O . HOH D 4 . ? 32.752 12.790 8.169 1.00 35.93 ? 670 HOH A O 1 HETATM 1864 O O . HOH D 4 . ? 48.057 -9.512 10.871 1.00 34.51 ? 671 HOH A O 1 HETATM 1865 O O . HOH D 4 . ? 36.114 -7.539 10.913 1.00 24.46 ? 672 HOH A O 1 HETATM 1866 O O . HOH D 4 . ? 53.587 17.219 -1.062 1.00 50.15 ? 673 HOH A O 1 HETATM 1867 O O . HOH D 4 . ? 48.395 17.592 16.896 1.00 39.03 ? 674 HOH A O 1 HETATM 1868 O O . HOH D 4 . ? 28.266 8.187 21.685 1.00 31.93 ? 675 HOH A O 1 HETATM 1869 O O . HOH D 4 . ? 28.327 0.815 19.211 1.00 36.49 ? 676 HOH A O 1 HETATM 1870 O O . HOH D 4 . ? 41.416 15.706 8.302 1.00 35.28 ? 677 HOH A O 1 HETATM 1871 O O . HOH D 4 . ? 27.076 -12.814 22.561 1.00 29.95 ? 678 HOH A O 1 HETATM 1872 O O . HOH D 4 . ? 34.541 -1.733 23.728 1.00 41.07 ? 679 HOH A O 1 HETATM 1873 O O . HOH D 4 . ? 34.768 9.469 23.211 1.00 25.05 ? 680 HOH A O 1 HETATM 1874 O O . HOH D 4 . ? 30.504 7.914 23.495 1.00 28.06 ? 681 HOH A O 1 HETATM 1875 O O . HOH D 4 . ? 36.144 2.150 32.725 1.00 40.70 ? 682 HOH A O 1 HETATM 1876 O O . HOH D 4 . ? 48.035 -20.509 4.249 1.00 57.85 ? 683 HOH A O 1 HETATM 1877 O O . HOH D 4 . ? 27.722 10.923 4.643 1.00 36.85 ? 684 HOH A O 1 HETATM 1878 O O . HOH D 4 . ? 41.265 -19.752 8.510 1.00 38.40 ? 685 HOH A O 1 HETATM 1879 O O . HOH D 4 . ? 20.482 2.427 12.589 1.00 31.74 ? 686 HOH A O 1 HETATM 1880 O O . HOH D 4 . ? 21.097 -11.657 19.232 1.00 41.56 ? 687 HOH A O 1 HETATM 1881 O O . HOH D 4 . ? 54.605 14.705 3.097 1.00 32.88 ? 689 HOH A O 1 HETATM 1882 O O . HOH D 4 . ? 51.849 5.260 -9.503 1.00 33.10 ? 690 HOH A O 1 HETATM 1883 O O . HOH D 4 . ? 49.225 -1.878 23.356 1.00 34.53 ? 691 HOH A O 1 HETATM 1884 O O . HOH D 4 . ? 40.792 11.926 -2.797 1.00 42.06 ? 692 HOH A O 1 HETATM 1885 O O . HOH D 4 . ? 58.955 -6.034 16.807 1.00 32.59 ? 693 HOH A O 1 HETATM 1886 O O . HOH D 4 . ? 49.574 6.563 -10.099 1.00 27.27 ? 694 HOH A O 1 HETATM 1887 O O . HOH D 4 . ? 31.115 -18.340 2.964 1.00 42.65 ? 695 HOH A O 1 HETATM 1888 O O . HOH D 4 . ? 28.960 -7.996 -6.149 1.00 48.07 ? 696 HOH A O 1 HETATM 1889 O O . HOH D 4 . ? 48.771 19.224 2.660 1.00 27.84 ? 697 HOH A O 1 HETATM 1890 O O . HOH D 4 . ? 43.598 0.349 -9.407 1.00 43.35 ? 700 HOH A O 1 HETATM 1891 O O . HOH D 4 . ? 36.069 -16.072 16.036 1.00 38.70 ? 701 HOH A O 1 HETATM 1892 O O . HOH D 4 . ? 33.224 -1.134 26.285 1.00 47.78 ? 703 HOH A O 1 HETATM 1893 O O . HOH D 4 . ? 27.660 -11.955 7.174 1.00 42.72 ? 704 HOH A O 1 HETATM 1894 O O . HOH D 4 . ? 32.153 10.937 20.973 1.00 38.99 ? 705 HOH A O 1 HETATM 1895 O O . HOH D 4 . ? 52.775 -12.165 16.404 1.00 39.14 ? 706 HOH A O 1 HETATM 1896 O O . HOH D 4 . ? 35.822 -10.437 9.488 1.00 26.37 ? 707 HOH A O 1 HETATM 1897 O O . HOH D 4 . ? 28.196 -12.209 26.016 1.00 51.50 ? 709 HOH A O 1 HETATM 1898 O O . HOH D 4 . ? 27.369 -6.133 -1.785 1.00 44.10 ? 710 HOH A O 1 HETATM 1899 O O . HOH D 4 . ? 51.653 14.325 -6.035 1.00 37.99 ? 711 HOH A O 1 HETATM 1900 O O . HOH D 4 . ? 41.720 19.123 0.914 1.00 33.90 ? 712 HOH A O 1 HETATM 1901 O O . HOH D 4 . ? 22.188 -5.701 -0.031 1.00 35.47 ? 713 HOH A O 1 HETATM 1902 O O . HOH D 4 . ? 23.247 -13.757 8.666 1.00 34.97 ? 715 HOH A O 1 HETATM 1903 O O . HOH D 4 . ? 50.793 8.416 -11.311 1.00 27.52 ? 716 HOH A O 1 HETATM 1904 O O . HOH D 4 . ? 39.164 6.869 -7.798 1.00 28.72 ? 717 HOH A O 1 HETATM 1905 O O . HOH D 4 . ? 43.242 17.734 3.249 1.00 41.73 ? 718 HOH A O 1 HETATM 1906 O O . HOH D 4 . ? 50.763 0.481 -9.549 1.00 34.08 ? 720 HOH A O 1 HETATM 1907 O O . HOH D 4 . ? 51.217 19.003 6.446 1.00 43.12 ? 721 HOH A O 1 HETATM 1908 O O . HOH D 4 . ? 22.813 -14.814 11.229 1.00 33.21 ? 722 HOH A O 1 HETATM 1909 O O . HOH D 4 . ? 20.874 -6.660 9.696 1.00 32.80 ? 723 HOH A O 1 HETATM 1910 O O . HOH D 4 . ? 58.436 7.082 20.648 1.00 32.72 ? 724 HOH A O 1 HETATM 1911 O O . HOH D 4 . ? 20.832 -9.244 20.683 1.00 45.02 ? 725 HOH A O 1 HETATM 1912 O O . HOH D 4 . ? 44.181 -10.542 12.446 1.00 39.23 ? 726 HOH A O 1 HETATM 1913 O O . HOH D 4 . ? 39.998 11.045 -0.331 1.00 34.51 ? 727 HOH A O 1 HETATM 1914 O O . HOH D 4 . ? 34.117 -20.259 12.287 1.00 41.16 ? 728 HOH A O 1 HETATM 1915 O O . HOH D 4 . ? 34.552 0.024 30.244 1.00 31.00 ? 730 HOH A O 1 HETATM 1916 O O . HOH D 4 . ? 48.308 -9.220 -5.927 1.00 32.70 ? 731 HOH A O 1 HETATM 1917 O O . HOH D 4 . ? 34.756 -11.707 25.869 1.00 45.86 ? 732 HOH A O 1 HETATM 1918 O O . HOH D 4 . ? 28.470 -20.359 5.746 1.00 35.92 ? 733 HOH A O 1 HETATM 1919 O O . HOH D 4 . ? 61.865 9.159 12.547 1.00 56.18 ? 734 HOH A O 1 HETATM 1920 O O . HOH D 4 . ? 37.385 13.782 4.643 1.00 40.58 ? 735 HOH A O 1 HETATM 1921 O O . HOH D 4 . ? 34.418 -21.280 3.756 1.00 35.50 ? 737 HOH A O 1 HETATM 1922 O O . HOH D 4 . ? 45.250 17.819 4.995 1.00 39.99 ? 740 HOH A O 1 HETATM 1923 O O . HOH D 4 . ? 37.144 -2.282 -6.487 1.00 39.32 ? 742 HOH A O 1 HETATM 1924 O O . HOH D 4 . ? 22.615 -8.896 0.787 1.00 55.56 ? 743 HOH A O 1 HETATM 1925 O O . HOH D 4 . ? 41.520 10.817 -5.531 1.00 41.32 ? 744 HOH A O 1 HETATM 1926 O O . HOH D 4 . ? 33.775 -17.079 17.683 1.00 33.97 ? 745 HOH A O 1 HETATM 1927 O O . HOH D 4 . ? 38.968 14.883 11.319 1.00 44.05 ? 749 HOH A O 1 HETATM 1928 O O . HOH D 4 . ? 33.978 -2.768 -5.928 1.00 39.05 ? 750 HOH A O 1 HETATM 1929 O O . HOH D 4 . ? 39.165 9.119 -9.263 1.00 27.05 ? 751 HOH A O 1 HETATM 1930 O O . HOH D 4 . ? 24.739 -0.807 15.106 1.00 37.14 ? 752 HOH A O 1 HETATM 1931 O O . HOH D 4 . ? 48.412 5.033 26.054 1.00 34.67 ? 753 HOH A O 1 HETATM 1932 O O . HOH D 4 . ? 17.625 -1.831 12.972 1.00 42.17 ? 754 HOH A O 1 HETATM 1933 O O . HOH D 4 . ? 41.224 6.107 -11.324 1.00 38.03 ? 757 HOH A O 1 HETATM 1934 O O . HOH D 4 . ? 31.759 -5.665 -3.745 1.00 26.86 ? 758 HOH A O 1 HETATM 1935 O O . HOH D 4 . ? 39.486 7.846 -11.833 1.00 33.84 ? 759 HOH A O 1 HETATM 1936 O O . HOH D 4 . ? 43.401 -15.289 7.062 1.00 23.52 ? 762 HOH A O 1 HETATM 1937 O O . HOH D 4 . ? 47.001 15.980 30.985 1.00 40.61 ? 763 HOH A O 1 HETATM 1938 O O . HOH D 4 . ? 31.563 -17.446 16.161 1.00 40.06 ? 765 HOH A O 1 # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 VAL 1 16 16 VAL VAL A . n A 1 2 ILE 2 17 17 ILE ILE A . n A 1 3 GLY 3 18 18 GLY GLY A . n A 1 4 GLY 4 19 19 GLY GLY A . n A 1 5 ASN 5 20 20 ASN ASN 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 ASP 8 23 23 ASP ASP A . n A 1 9 ILE 9 24 24 ILE ILE A . n A 1 10 ASN 10 25 25 ASN ASN A . n A 1 11 GLU 11 26 26 GLU GLU A . n A 1 12 HIS 12 27 27 HIS HIS A . n A 1 13 ARG 13 28 28 ARG ARG A . n A 1 14 PHE 14 29 29 PHE PHE A . n A 1 15 LEU 15 30 30 LEU LEU A . n A 1 16 VAL 16 31 31 VAL VAL A . n A 1 17 ALA 17 32 32 ALA ALA A . n A 1 18 PHE 18 33 33 PHE PHE A . n A 1 19 PHE 19 34 34 PHE PHE A . n A 1 20 ASN 20 35 35 ASN ASN A . n A 1 21 THR 21 36 36 THR THR A . n A 1 22 THR 22 38 38 THR THR A . n A 1 23 GLY 23 39 39 GLY GLY A . n A 1 24 PHE 24 40 40 PHE PHE A . n A 1 25 PHE 25 41 41 PHE PHE A . n A 1 26 CYS 26 42 42 CYS CYS A . n A 1 27 GLY 27 43 43 GLY GLY A . n A 1 28 GLY 28 44 44 GLY GLY A . n A 1 29 THR 29 45 45 THR THR A . n A 1 30 LEU 30 46 46 LEU LEU A . n A 1 31 ILE 31 47 47 ILE ILE A . n A 1 32 ASN 32 48 48 ASN ASN A . n A 1 33 PRO 33 49 49 PRO PRO A . n A 1 34 GLU 34 50 50 GLU GLU A . n A 1 35 TRP 35 51 51 TRP TRP A . n A 1 36 VAL 36 52 52 VAL VAL A . n A 1 37 VAL 37 53 53 VAL VAL A . n A 1 38 THR 38 54 54 THR THR A . n A 1 39 ALA 39 55 55 ALA ALA A . n A 1 40 ALA 40 56 56 ALA ALA A . n A 1 41 HIS 41 57 57 HIS HIS A . n A 1 42 CYS 42 58 58 CYS CYS A . n A 1 43 ASP 43 59 59 ASP ASP A . n A 1 44 SER 44 60 60 SER SER A . n A 1 45 THR 45 62 62 THR THR A . n A 1 46 ASN 46 63 63 ASN ASN A . n A 1 47 PHE 47 64 64 PHE PHE A . n A 1 48 GLN 48 65 65 GLN GLN A . n A 1 49 MET 49 66 66 MET MET A . n A 1 50 GLN 50 67 67 GLN GLN A . n A 1 51 LEU 51 68 68 LEU LEU A . n A 1 52 GLY 52 69 69 GLY GLY A . n A 1 53 VAL 53 70 70 VAL VAL A . n A 1 54 HIS 54 71 71 HIS HIS A . n A 1 55 SER 55 72 72 SER SER A . n A 1 56 LYS 56 73 73 LYS LYS A . n A 1 57 LYS 57 74 74 LYS LYS A . n A 1 58 VAL 58 75 75 VAL VAL A . n A 1 59 LEU 59 76 76 LEU LEU A . n A 1 60 ASN 60 77 77 ASN ASN A . n A 1 61 GLU 61 78 78 GLU GLU A . n A 1 62 ASP 62 79 79 ASP ASP A . n A 1 63 GLU 63 80 80 GLU GLU A . n A 1 64 GLN 64 81 81 GLN GLN A . n A 1 65 THR 65 82 82 THR THR A . n A 1 66 ARG 66 83 83 ARG ARG A . n A 1 67 ASN 67 84 84 ASN ASN A . n A 1 68 PRO 68 85 85 PRO PRO A . n A 1 69 LYS 69 86 86 LYS LYS A . n A 1 70 GLU 70 87 87 GLU GLU A . n A 1 71 LYS 71 88 88 LYS LYS A . n A 1 72 PHE 72 89 89 PHE PHE A . n A 1 73 ILE 73 90 90 ILE ILE A . n A 1 74 CYS 74 91 91 CYS CYS A . n A 1 75 PRO 75 92 92 PRO PRO A . n A 1 76 ASN 76 93 93 ASN ASN A . n A 1 77 LYS 77 94 94 LYS LYS A . n A 1 78 ASN 78 95 95 ASN ASN A . n A 1 79 ASN 79 95 95 ASN ASN A A n A 1 80 ASN 80 96 96 ASN ASN A . n A 1 81 GLU 81 97 97 GLU GLU A . n A 1 82 VAL 82 98 98 VAL VAL A . n A 1 83 LEU 83 99 99 LEU LEU A . n A 1 84 ASP 84 100 100 ASP ASP A . n A 1 85 LYS 85 101 101 LYS LYS A . n A 1 86 ASP 86 102 102 ASP ASP A . n A 1 87 ILE 87 103 103 ILE ILE A . n A 1 88 MET 88 104 104 MET MET A . n A 1 89 LEU 89 105 105 LEU LEU A . n A 1 90 ILE 90 106 106 ILE ILE A . n A 1 91 LYS 91 107 107 LYS LYS A . n A 1 92 LEU 92 108 108 LEU LEU A . n A 1 93 ASP 93 109 109 ASP ASP A . n A 1 94 LYS 94 110 110 LYS LYS A . n A 1 95 PRO 95 111 111 PRO PRO A . n A 1 96 ILE 96 112 112 ILE ILE A . n A 1 97 SER 97 113 113 SER SER A . n A 1 98 ASN 98 114 114 ASN ASN A . n A 1 99 SER 99 115 115 SER SER A . n A 1 100 LYS 100 116 116 LYS LYS A . n A 1 101 HIS 101 117 117 HIS HIS A . n A 1 102 ILE 102 118 118 ILE ILE A . n A 1 103 ALA 103 119 119 ALA ALA A . n A 1 104 PRO 104 120 120 PRO PRO A . n A 1 105 LEU 105 121 121 LEU LEU A . n A 1 106 SER 106 122 122 SER SER A . n A 1 107 LEU 107 123 123 LEU LEU A . n A 1 108 PRO 108 124 124 PRO PRO A . n A 1 109 SER 109 125 125 SER SER A . n A 1 110 SER 110 127 127 SER SER A . n A 1 111 PRO 111 128 128 PRO PRO A . n A 1 112 PRO 112 129 129 PRO PRO A . n A 1 113 SER 113 131 131 SER SER A . n A 1 114 VAL 114 132 132 VAL VAL A . n A 1 115 GLY 115 133 133 GLY GLY A . n A 1 116 SER 116 134 134 SER SER A . n A 1 117 VAL 117 135 135 VAL VAL A . n A 1 118 CYS 118 136 136 CYS CYS A . n A 1 119 ARG 119 137 137 ARG ARG A . n A 1 120 ILE 120 138 138 ILE ILE A . n A 1 121 MET 121 139 139 MET MET A . n A 1 122 GLY 122 140 140 GLY GLY A . n A 1 123 TRP 123 141 141 TRP TRP A . n A 1 124 GLY 124 142 142 GLY GLY A . n A 1 125 SER 125 143 143 SER SER A . n A 1 126 ILE 126 144 144 ILE ILE A . n A 1 127 THR 127 145 145 THR THR A . n A 1 128 PRO 128 146 146 PRO PRO A . n A 1 129 VAL 129 147 147 VAL VAL A . n A 1 130 LYS 130 148 148 LYS LYS A . n A 1 131 GLU 131 149 149 GLU GLU A . n A 1 132 THR 132 150 150 THR THR A . n A 1 133 PHE 133 151 151 PHE PHE 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 TYR 138 156 156 TYR TYR A . n A 1 139 CYS 139 157 157 CYS CYS A . n A 1 140 ALA 140 158 158 ALA ALA 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 ASN 143 161 161 ASN ASN A . n A 1 144 LEU 144 162 162 LEU LEU A . n A 1 145 LEU 145 163 163 LEU LEU A . n A 1 146 ASP 146 164 164 ASP ASP A . n A 1 147 HIS 147 165 165 HIS HIS A . n A 1 148 ALA 148 166 166 ALA ALA A . n A 1 149 VAL 149 167 167 VAL VAL A . n A 1 150 CYS 150 168 168 CYS CYS A . n A 1 151 GLN 151 169 169 GLN GLN A . n A 1 152 ALA 152 170 170 ALA ALA A . n A 1 153 GLY 153 171 171 GLY GLY 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 GLU 156 173 173 GLU GLU A . n A 1 157 LEU 157 174 174 LEU LEU A . n A 1 158 LEU 158 175 175 LEU LEU A . n A 1 159 ALA 159 176 176 ALA ALA A . n A 1 160 GLU 160 177 177 GLU GLU A . n A 1 161 TYR 161 178 178 TYR TYR 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 VAL 169 186 186 VAL VAL A . n A 1 170 GLN 170 186 186 GLN GLN 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 LYS 173 188 188 LYS LYS 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 GLY 177 192 192 GLY GLY 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 GLN 189 208 208 GLN GLN A . n A 1 190 PHE 190 209 209 PHE PHE A . n A 1 191 GLN 191 210 210 GLN GLN 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 SER 195 214 214 SER SER A . n A 1 196 TYR 196 215 215 TYR TYR A . n A 1 197 GLY 197 216 216 GLY GLY A . n A 1 198 ALA 198 217 217 ALA ALA A . n A 1 199 HIS 199 218 218 HIS HIS 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 GLY 204 222 222 GLY GLY A . n A 1 205 PRO 205 223 223 PRO PRO 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 GLY 208 226 226 GLY GLY A . n A 1 209 ILE 209 227 227 ILE ILE 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 ASN 212 230 230 ASN ASN 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 THR 217 235 235 THR THR A . n A 1 218 ASP 218 236 236 ASP ASP 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 ARG 222 240 240 ARG ARG A . n A 1 223 ASN 223 241 241 ASN ASN 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 THR 228 245 245 THR THR A A n A 1 229 ASP 229 245 245 ASP ASP A B n A 1 230 ALA 230 245 245 ALA ALA A C n A 1 231 THR 231 245 245 THR THR A D n A 1 232 CYS 232 245 245 CYS CYS A E n A 1 233 PRO 233 245 245 PRO PRO A F n A 1 234 PRO 234 245 245 PRO PRO A G n # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code B 2 NAG 1 301 301 NAG NAG A . C 3 SO4 1 401 401 SO4 SO4 A . D 4 HOH 1 601 601 HOH HOH A . D 4 HOH 2 602 602 HOH HOH A . D 4 HOH 3 603 603 HOH HOH A . D 4 HOH 4 604 604 HOH HOH A . D 4 HOH 5 605 605 HOH HOH A . D 4 HOH 6 606 606 HOH HOH A . D 4 HOH 7 607 607 HOH HOH A . D 4 HOH 8 608 608 HOH HOH A . D 4 HOH 9 609 609 HOH HOH A . D 4 HOH 10 610 610 HOH HOH A . D 4 HOH 11 611 611 HOH HOH A . D 4 HOH 12 612 612 HOH HOH A . D 4 HOH 13 613 613 HOH HOH A . D 4 HOH 14 614 614 HOH HOH A . D 4 HOH 15 615 615 HOH HOH A . D 4 HOH 16 616 616 HOH HOH A . D 4 HOH 17 617 617 HOH HOH A . D 4 HOH 18 618 618 HOH HOH A . D 4 HOH 19 619 619 HOH HOH A . D 4 HOH 20 620 620 HOH HOH A . D 4 HOH 21 621 621 HOH HOH A . D 4 HOH 22 622 622 HOH HOH A . D 4 HOH 23 623 623 HOH HOH A . D 4 HOH 24 624 624 HOH HOH A . D 4 HOH 25 625 625 HOH HOH A . D 4 HOH 26 626 626 HOH HOH A . D 4 HOH 27 627 627 HOH HOH A . D 4 HOH 28 628 628 HOH HOH A . D 4 HOH 29 629 629 HOH HOH A . D 4 HOH 30 630 630 HOH HOH A . D 4 HOH 31 631 631 HOH HOH A . D 4 HOH 32 632 632 HOH HOH A . D 4 HOH 33 633 633 HOH HOH A . D 4 HOH 34 634 634 HOH HOH A . D 4 HOH 35 635 635 HOH HOH A . D 4 HOH 36 636 636 HOH HOH A . D 4 HOH 37 637 637 HOH HOH A . D 4 HOH 38 638 638 HOH HOH A . D 4 HOH 39 639 639 HOH HOH A . D 4 HOH 40 640 640 HOH HOH A . D 4 HOH 41 641 641 HOH HOH A . D 4 HOH 42 642 642 HOH HOH A . D 4 HOH 43 643 643 HOH HOH A . D 4 HOH 44 644 644 HOH HOH A . D 4 HOH 45 645 645 HOH HOH A . D 4 HOH 46 646 646 HOH HOH A . D 4 HOH 47 647 647 HOH HOH A . D 4 HOH 48 648 648 HOH HOH A . D 4 HOH 49 649 649 HOH HOH A . D 4 HOH 50 650 650 HOH HOH A . D 4 HOH 51 651 651 HOH HOH A . D 4 HOH 52 652 652 HOH HOH A . D 4 HOH 53 653 653 HOH HOH A . D 4 HOH 54 654 654 HOH HOH A . D 4 HOH 55 655 655 HOH HOH A . D 4 HOH 56 656 656 HOH HOH A . D 4 HOH 57 657 657 HOH HOH A . D 4 HOH 58 658 658 HOH HOH A . D 4 HOH 59 659 659 HOH HOH A . D 4 HOH 60 660 660 HOH HOH A . D 4 HOH 61 661 661 HOH HOH A . D 4 HOH 62 662 662 HOH HOH A . D 4 HOH 63 663 663 HOH HOH A . D 4 HOH 64 665 665 HOH HOH A . D 4 HOH 65 666 666 HOH HOH A . D 4 HOH 66 667 667 HOH HOH A . D 4 HOH 67 668 668 HOH HOH A . D 4 HOH 68 670 670 HOH HOH A . D 4 HOH 69 671 671 HOH HOH A . D 4 HOH 70 672 672 HOH HOH A . D 4 HOH 71 673 673 HOH HOH A . D 4 HOH 72 674 674 HOH HOH A . D 4 HOH 73 675 675 HOH HOH A . D 4 HOH 74 676 676 HOH HOH A . D 4 HOH 75 677 677 HOH HOH A . D 4 HOH 76 678 678 HOH HOH A . D 4 HOH 77 679 679 HOH HOH A . D 4 HOH 78 680 680 HOH HOH A . D 4 HOH 79 681 681 HOH HOH A . D 4 HOH 80 682 682 HOH HOH A . D 4 HOH 81 683 683 HOH HOH A . D 4 HOH 82 684 684 HOH HOH A . D 4 HOH 83 685 685 HOH HOH A . D 4 HOH 84 686 686 HOH HOH A . D 4 HOH 85 687 687 HOH HOH A . D 4 HOH 86 689 689 HOH HOH A . D 4 HOH 87 690 690 HOH HOH A . D 4 HOH 88 691 691 HOH HOH A . D 4 HOH 89 692 692 HOH HOH A . D 4 HOH 90 693 693 HOH HOH A . D 4 HOH 91 694 694 HOH HOH A . D 4 HOH 92 695 695 HOH HOH A . D 4 HOH 93 696 696 HOH HOH A . D 4 HOH 94 697 697 HOH HOH A . D 4 HOH 95 700 700 HOH HOH A . D 4 HOH 96 701 701 HOH HOH A . D 4 HOH 97 703 703 HOH HOH A . D 4 HOH 98 704 704 HOH HOH A . D 4 HOH 99 705 705 HOH HOH A . D 4 HOH 100 706 706 HOH HOH A . D 4 HOH 101 707 707 HOH HOH A . D 4 HOH 102 709 709 HOH HOH A . D 4 HOH 103 710 710 HOH HOH A . D 4 HOH 104 711 711 HOH HOH A . D 4 HOH 105 712 712 HOH HOH A . D 4 HOH 106 713 713 HOH HOH A . D 4 HOH 107 715 715 HOH HOH A . D 4 HOH 108 716 716 HOH HOH A . D 4 HOH 109 717 717 HOH HOH A . D 4 HOH 110 718 718 HOH HOH A . D 4 HOH 111 720 720 HOH HOH A . D 4 HOH 112 721 721 HOH HOH A . D 4 HOH 113 722 722 HOH HOH A . D 4 HOH 114 723 723 HOH HOH A . D 4 HOH 115 724 724 HOH HOH A . D 4 HOH 116 725 725 HOH HOH A . D 4 HOH 117 726 726 HOH HOH A . D 4 HOH 118 727 727 HOH HOH A . D 4 HOH 119 728 728 HOH HOH A . D 4 HOH 120 730 730 HOH HOH A . D 4 HOH 121 731 731 HOH HOH A . D 4 HOH 122 732 732 HOH HOH A . D 4 HOH 123 733 733 HOH HOH A . D 4 HOH 124 734 734 HOH HOH A . D 4 HOH 125 735 735 HOH HOH A . D 4 HOH 126 737 737 HOH HOH A . D 4 HOH 127 740 740 HOH HOH A . D 4 HOH 128 742 742 HOH HOH A . D 4 HOH 129 743 743 HOH HOH A . D 4 HOH 130 744 744 HOH HOH A . D 4 HOH 131 745 745 HOH HOH A . D 4 HOH 132 749 749 HOH HOH A . D 4 HOH 133 750 750 HOH HOH A . D 4 HOH 134 751 751 HOH HOH A . D 4 HOH 135 752 752 HOH HOH A . D 4 HOH 136 753 753 HOH HOH A . D 4 HOH 137 754 754 HOH HOH A . D 4 HOH 138 757 757 HOH HOH A . D 4 HOH 139 758 758 HOH HOH A . D 4 HOH 140 759 759 HOH HOH A . D 4 HOH 141 762 762 HOH HOH A . D 4 HOH 142 763 763 HOH HOH A . D 4 HOH 143 765 765 HOH HOH A . # _pdbx_struct_mod_residue.id 1 _pdbx_struct_mod_residue.label_asym_id A _pdbx_struct_mod_residue.label_comp_id ASN _pdbx_struct_mod_residue.label_seq_id 20 _pdbx_struct_mod_residue.auth_asym_id A _pdbx_struct_mod_residue.auth_comp_id ASN _pdbx_struct_mod_residue.auth_seq_id 35 _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_defined_assembly _pdbx_struct_assembly.method_details ? _pdbx_struct_assembly.oligomeric_details monomeric _pdbx_struct_assembly.oligomeric_count 1 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D # _pdbx_struct_oper_list.id 1 _pdbx_struct_oper_list.type 'identity operation' _pdbx_struct_oper_list.name 1_555 _pdbx_struct_oper_list.symmetry_operation x,y,z _pdbx_struct_oper_list.matrix[1][1] 1.0000000000 _pdbx_struct_oper_list.matrix[1][2] 0.0000000000 _pdbx_struct_oper_list.matrix[1][3] 0.0000000000 _pdbx_struct_oper_list.vector[1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][2] 1.0000000000 _pdbx_struct_oper_list.matrix[2][3] 0.0000000000 _pdbx_struct_oper_list.vector[2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][1] 0.0000000000 _pdbx_struct_oper_list.matrix[3][2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][3] 1.0000000000 _pdbx_struct_oper_list.vector[3] 0.0000000000 # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 2004-05-25 2 'Structure model' 1 1 2008-04-29 3 'Structure model' 1 2 2011-07-13 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # loop_ _pdbx_audit_revision_group.ordinal _pdbx_audit_revision_group.revision_ordinal _pdbx_audit_revision_group.data_content_type _pdbx_audit_revision_group.group 1 2 'Structure model' 'Version format compliance' 2 3 'Structure model' 'Non-polymer description' 3 3 'Structure model' 'Version format compliance' # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal CNS refinement 1.0 ? 1 DENZO 'data reduction' . ? 2 SCALEPACK 'data scaling' . ? 3 AMoRE phasing . ? 4 # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 PHE A 41 ? ? -140.08 -12.65 2 1 HIS A 71 ? ? -125.43 -79.02 3 1 ASN A 93 ? ? -96.22 46.81 4 1 ASN A 95 A ? -69.45 6.43 5 1 ALA A 119 ? ? -170.70 138.46 6 1 VAL A 147 ? ? -103.56 -72.27 7 1 THR A 245 A ? 46.64 16.21 8 1 ALA A 245 C ? -44.48 150.72 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 N-ACETYL-D-GLUCOSAMINE NAG 3 'SULFATE ION' SO4 4 water HOH #